data_3QQI # _entry.id 3QQI # _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 3QQI RCSB RCSB063975 WWPDB D_1000063975 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3QQB . unspecified PDB 3QQE . unspecified PDB 3QQO . unspecified # _pdbx_database_status.entry_id 3QQI _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2011-02-15 _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 _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xu, R.' 1 'Wilson, I.A.' 2 # _citation.id primary _citation.title 'Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin.' _citation.journal_abbrev J.Virol. _citation.journal_volume 85 _citation.page_first 5172 _citation.page_last 5182 _citation.year 2011 _citation.journal_id_ASTM JOVIAM _citation.country US _citation.journal_id_ISSN 0022-538X _citation.journal_id_CSD 0825 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21367895 _citation.pdbx_database_id_DOI 10.1128/JVI.02430-10 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xu, R.' 1 primary 'Wilson, I.A.' 2 # _cell.length_a 38.629 _cell.length_b 62.318 _cell.length_c 66.034 _cell.angle_alpha 64.250 _cell.angle_beta 80.040 _cell.angle_gamma 72.120 _cell.entry_id 3QQI _cell.pdbx_unique_axis ? _cell.Z_PDB 2 _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.space_group_name_H-M 'P 1' _symmetry.entry_id 3QQI _symmetry.Int_Tables_number 1 _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _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 Hemagglutinin 24569.625 2 ? ? 'HA1 receptor binding domain' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 2 ? ? ? ? 4 water nat water 18.015 616 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;GIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYIMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQH TTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVAKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLN KRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTINFESTGNLIAPEYGFKISKRGSSGIM ; _entity_poly.pdbx_seq_one_letter_code_can ;GIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYIMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQH TTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVAKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLN KRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTINFESTGNLIAPEYGFKISKRGSSGIM ; _entity_poly.pdbx_strand_id A,B _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 GLY n 1 2 ILE n 1 3 PRO n 1 4 PRO n 1 5 LEU n 1 6 GLU n 1 7 LEU n 1 8 GLY n 1 9 ASP n 1 10 CYS n 1 11 SER n 1 12 ILE n 1 13 ALA n 1 14 GLY n 1 15 TRP n 1 16 LEU n 1 17 LEU n 1 18 GLY n 1 19 ASN n 1 20 PRO n 1 21 GLU n 1 22 CYS n 1 23 ASP n 1 24 ARG n 1 25 LEU n 1 26 LEU n 1 27 SER n 1 28 VAL n 1 29 PRO n 1 30 GLU n 1 31 TRP n 1 32 SER n 1 33 TYR n 1 34 ILE n 1 35 MET n 1 36 GLU n 1 37 LYS n 1 38 GLU n 1 39 ASN n 1 40 PRO n 1 41 ARG n 1 42 ASP n 1 43 GLY n 1 44 LEU n 1 45 CYS n 1 46 TYR n 1 47 PRO n 1 48 GLY n 1 49 SER n 1 50 PHE n 1 51 ASN n 1 52 ASP n 1 53 TYR n 1 54 GLU n 1 55 GLU n 1 56 LEU n 1 57 LYS n 1 58 HIS n 1 59 LEU n 1 60 LEU n 1 61 SER n 1 62 SER n 1 63 VAL n 1 64 LYS n 1 65 HIS n 1 66 PHE n 1 67 GLU n 1 68 LYS n 1 69 VAL n 1 70 LYS n 1 71 ILE n 1 72 LEU n 1 73 PRO n 1 74 LYS n 1 75 ASP n 1 76 ARG n 1 77 TRP n 1 78 THR n 1 79 GLN n 1 80 HIS n 1 81 THR n 1 82 THR n 1 83 THR n 1 84 GLY n 1 85 GLY n 1 86 SER n 1 87 ARG n 1 88 ALA n 1 89 CYS n 1 90 ALA n 1 91 VAL n 1 92 SER n 1 93 GLY n 1 94 ASN n 1 95 PRO n 1 96 SER n 1 97 PHE n 1 98 PHE n 1 99 ARG n 1 100 ASN n 1 101 MET n 1 102 VAL n 1 103 TRP n 1 104 LEU n 1 105 THR n 1 106 GLU n 1 107 LYS n 1 108 GLY n 1 109 SER n 1 110 ASN n 1 111 TYR n 1 112 PRO n 1 113 VAL n 1 114 ALA n 1 115 LYS n 1 116 GLY n 1 117 SER n 1 118 TYR n 1 119 ASN n 1 120 ASN n 1 121 THR n 1 122 SER n 1 123 GLY n 1 124 GLU n 1 125 GLN n 1 126 MET n 1 127 LEU n 1 128 ILE n 1 129 ILE n 1 130 TRP n 1 131 GLY n 1 132 VAL n 1 133 HIS n 1 134 HIS n 1 135 PRO n 1 136 ASN n 1 137 ASP n 1 138 GLU n 1 139 THR n 1 140 GLU n 1 141 GLN n 1 142 ARG n 1 143 THR n 1 144 LEU n 1 145 TYR n 1 146 GLN n 1 147 ASN n 1 148 VAL n 1 149 GLY n 1 150 THR n 1 151 TYR n 1 152 VAL n 1 153 SER n 1 154 VAL n 1 155 GLY n 1 156 THR n 1 157 SER n 1 158 THR n 1 159 LEU n 1 160 ASN n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 THR n 1 165 PRO n 1 166 GLU n 1 167 ILE n 1 168 ALA n 1 169 THR n 1 170 ARG n 1 171 PRO n 1 172 LYS n 1 173 VAL n 1 174 ASN n 1 175 GLY n 1 176 GLN n 1 177 GLY n 1 178 GLY n 1 179 ARG n 1 180 MET n 1 181 GLU n 1 182 PHE n 1 183 SER n 1 184 TRP n 1 185 THR n 1 186 LEU n 1 187 LEU n 1 188 ASP n 1 189 MET n 1 190 TRP n 1 191 ASP n 1 192 THR n 1 193 ILE n 1 194 ASN n 1 195 PHE n 1 196 GLU n 1 197 SER n 1 198 THR n 1 199 GLY n 1 200 ASN n 1 201 LEU n 1 202 ILE n 1 203 ALA n 1 204 PRO n 1 205 GLU n 1 206 TYR n 1 207 GLY n 1 208 PHE n 1 209 LYS n 1 210 ILE n 1 211 SER n 1 212 LYS n 1 213 ARG n 1 214 GLY n 1 215 SER n 1 216 SER n 1 217 GLY n 1 218 ILE n 1 219 MET 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 ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'HA, hemagglutinin' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'A/Japan/305/1957 H2N2' _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 'Influenza A virus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 387161 _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 'Trichoplusia ni' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7111 _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 Hi5 _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 Baculovirus _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pFASTbac-HT _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code C7S226_I57A0 _struct_ref.pdbx_db_accession C7S226 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;GIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYIMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQH TTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVAKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLN KRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTINFESTGNLIAPEYGFKISKRGSSGIM ; _struct_ref.pdbx_align_begin 61 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3QQI A 1 ? 219 ? C7S226 61 ? 279 ? 55 268 2 1 3QQI B 1 ? 219 ? C7S226 61 ? 279 ? 55 268 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.crystals_number 1 _exptl.entry_id 3QQI _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.77 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 55.60 _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.pH 8.1 _exptl_crystal_grow.temp 295.5 _exptl_crystal_grow.pdbx_details '1.25 Sodium Citrate, 0.1M HEPES, pH 8.1, vapor diffusion, sitting drop, temperature 295.5K' _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 300 mm CCD' _diffrn_detector.pdbx_collection_date 2009-06-05 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator 'Si(111) monochromator' _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97958 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 23-ID-B' _diffrn_source.pdbx_wavelength_list 0.97958 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 23-ID-B # _reflns.entry_id 3QQI _reflns.d_resolution_high 1.650 _reflns.d_resolution_low 50.000 _reflns.number_obs 60290 _reflns.pdbx_Rmerge_I_obs 0.053 _reflns.pdbx_netI_over_sigmaI 12.000 _reflns.pdbx_chi_squared 1.046 _reflns.pdbx_redundancy 1.900 _reflns.percent_possible_obs 94.800 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.number_all ? _reflns.pdbx_Rsym_value ? _reflns.B_iso_Wilson_estimate 22.6 _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_scaling_rejects ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.number_measured_obs _reflns_shell.number_measured_all _reflns_shell.number_unique_obs _reflns_shell.Rmerge_I_obs _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.percent_possible_all _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal 1.650 1.710 ? ? ? 0.244 ? ? 1.092 1.600 ? 5312 83.800 ? 1 1.710 1.780 ? ? ? 0.207 ? ? 1.086 1.800 ? 5858 91.500 ? 2 1.780 1.860 ? ? ? 0.157 ? ? 1.071 1.800 ? 5999 94.700 ? 3 1.860 1.960 ? ? ? 0.123 ? ? 1.051 1.900 ? 6148 96.200 ? 4 1.960 2.080 ? ? ? 0.092 ? ? 1.095 1.900 ? 6127 96.600 ? 5 2.080 2.240 ? ? ? 0.083 ? ? 1.036 1.900 ? 6125 96.500 ? 6 2.240 2.460 ? ? ? 0.069 ? ? 0.976 1.900 ? 6150 96.900 ? 7 2.460 2.820 ? ? ? 0.059 ? ? 1.038 1.900 ? 6199 97.300 ? 8 2.820 3.550 ? ? ? 0.050 ? ? 1.006 1.900 ? 6214 97.700 ? 9 3.550 50.000 ? ? ? 0.037 ? ? 1.041 1.900 ? 6158 96.900 ? 10 # _refine.entry_id 3QQI _refine.ls_d_res_high 1.6500 _refine.ls_d_res_low 36.7200 _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs ? _refine.ls_number_reflns_obs 60214 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_R_Free_selection_details RANDOM _refine.details ? _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.2010 _refine.ls_R_factor_R_work 0.1993 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.2335 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.0800 _refine.ls_number_reflns_R_free 3056 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 26.9027 _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] 1.2510 _refine.aniso_B[2][2] 0.3335 _refine.aniso_B[3][3] -1.5845 _refine.aniso_B[1][2] 1.1955 _refine.aniso_B[1][3] 0.0121 _refine.aniso_B[2][3] 1.9371 _refine.correlation_coeff_Fo_to_Fc 0.9439 _refine.correlation_coeff_Fo_to_Fc_free 0.9261 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.solvent_model_details ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set ? _refine.B_iso_max 110.610 _refine.B_iso_min 10.250 _refine.occupancy_max 1.000 _refine.occupancy_min 0.500 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _refine.pdbx_diffrn_id 1 _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_analyze.entry_id 3QQI _refine_analyze.Luzzati_coordinate_error_obs 0.204 _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3452 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 58 _refine_hist.number_atoms_solvent 616 _refine_hist.number_atoms_total 4126 _refine_hist.d_res_high 1.6500 _refine_hist.d_res_low 36.7200 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function t_dihedral_angle_d 1261 ? ? 2.000 'X-RAY DIFFRACTION' ? t_trig_c_planes 88 ? ? 2.000 'X-RAY DIFFRACTION' ? t_gen_planes 528 ? ? 5.000 'X-RAY DIFFRACTION' ? t_it 3634 ? ? 20.000 'X-RAY DIFFRACTION' ? t_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? t_improper_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_pseud_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_chiral_improper_torsion 463 ? ? 5.000 'X-RAY DIFFRACTION' ? t_sum_occupancies ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_distance ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_ideal_dist_contact 4557 ? ? 4.000 'X-RAY DIFFRACTION' ? t_bond_d 3634 0.011 ? 2.000 'X-RAY DIFFRACTION' ? t_angle_deg 4943 1.120 ? 2.000 'X-RAY DIFFRACTION' ? t_omega_torsion ? 3.960 ? ? 'X-RAY DIFFRACTION' ? t_other_torsion ? 16.960 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.d_res_high 1.6500 _refine_ls_shell.d_res_low 1.6900 _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.number_reflns_R_work 3713 _refine_ls_shell.R_factor_all 0.2313 _refine_ls_shell.R_factor_R_work 0.2303 _refine_ls_shell.R_factor_R_free 0.2504 _refine_ls_shell.percent_reflns_R_free 4.9400 _refine_ls_shell.number_reflns_R_free 193 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.number_reflns_all 3906 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3QQI _struct.title 'Crystal structure of the HA1 receptor binding domain of H2 hemagglutinin' _struct.pdbx_descriptor Hemagglutinin _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3QQI _struct_keywords.text 'viral envelope protein, hemagglutinin, viral fusion protein, viral protein' _struct_keywords.pdbx_keywords 'VIRAL 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 1 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 3 ? G N N 4 ? H N N 4 ? # _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 11 ? GLY A 18 ? SER A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASN A 19 ? LEU A 26 ? ASN A 73 LEU A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 52 ? SER A 61 ? ASP A 104 SER A 113 1 ? 10 HELX_P HELX_P4 4 PRO A 73 ? TRP A 77 ? PRO A 122 TRP A 127 5 ? 5 HELX_P HELX_P5 5 ASP A 137 ? GLN A 146 ? ASP A 187 GLN A 196 1 ? 10 HELX_P HELX_P6 6 SER B 11 ? GLY B 18 ? SER B 65 GLY B 72 1 ? 8 HELX_P HELX_P7 7 ASN B 19 ? LEU B 26 ? ASN B 73 LEU B 80 5 ? 8 HELX_P HELX_P8 8 ASP B 52 ? SER B 61 ? ASP B 104 SER B 113 1 ? 10 HELX_P HELX_P9 9 PRO B 73 ? TRP B 77 ? PRO B 122 TRP B 127 5 ? 5 HELX_P HELX_P10 10 ASP B 137 ? GLN B 146 ? ASP B 187 GLN B 196 1 ? 10 # _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 10 SG ? ? ? 1_555 A CYS 22 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.076 ? disulf2 disulf ? ? A CYS 45 SG ? ? ? 1_555 A CYS 89 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.102 ? disulf3 disulf ? ? B CYS 10 SG ? ? ? 1_555 B CYS 22 SG ? ? B CYS 64 B CYS 76 1_555 ? ? ? ? ? ? ? 2.067 ? disulf4 disulf ? ? B CYS 45 SG ? ? ? 1_555 B CYS 89 SG ? ? B CYS 97 B CYS 139 1_555 ? ? ? ? ? ? ? 2.099 ? covale1 covale ? ? B ASN 119 ND2 ? ? ? 1_555 E NAG . C1 ? ? B ASN 169 B NAG 5467 1_555 ? ? ? ? ? ? ? 1.425 ? covale2 covale ? ? A ASN 119 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 169 A NAG 5467 1_555 ? ? ? ? ? ? ? 1.433 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id GLY _struct_mon_prot_cis.label_seq_id 1 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id GLY _struct_mon_prot_cis.auth_seq_id 55 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 ILE _struct_mon_prot_cis.pdbx_label_seq_id_2 2 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 ILE _struct_mon_prot_cis.pdbx_auth_seq_id_2 56 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -3.83 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 3 ? B ? 5 ? C ? 5 ? D ? 2 ? E ? 4 ? F ? 2 ? G ? 5 ? H ? 5 ? I ? 2 ? J ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel B 1 2 ? parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel D 1 2 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? parallel G 1 2 ? parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel G 4 5 ? anti-parallel H 1 2 ? parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel H 4 5 ? anti-parallel I 1 2 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? 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 LEU A 5 ? GLU A 6 ? LEU A 59 GLU A 60 A 2 TYR A 33 ? MET A 35 ? TYR A 86 MET A 88 A 3 GLY A 217 ? MET A 219 ? GLY A 266 MET A 268 B 1 GLY A 48 ? PHE A 50 ? GLY A 100 PHE A 102 B 2 ARG A 179 ? LEU A 187 ? ARG A 229 LEU A 237 B 3 MET A 126 ? HIS A 134 ? MET A 176 HIS A 184 B 4 GLY A 207 ? ARG A 213 ? GLY A 257 ARG A 263 B 5 VAL A 63 ? VAL A 69 ? VAL A 115 VAL A 118 C 1 GLY A 48 ? PHE A 50 ? GLY A 100 PHE A 102 C 2 ARG A 179 ? LEU A 187 ? ARG A 229 LEU A 237 C 3 MET A 126 ? HIS A 134 ? MET A 176 HIS A 184 C 4 LEU A 201 ? PRO A 204 ? LEU A 251 PRO A 254 C 5 MET A 101 ? TRP A 103 ? MET A 151 TRP A 153 D 1 SER A 86 ? VAL A 91 ? SER A 136 VAL A 141 D 2 ASN A 94 ? SER A 96 ? ASN A 144 SER A 146 E 1 ALA A 114 ? ASN A 119 ? ALA A 164 ASN A 169 E 2 THR A 192 ? SER A 197 ? THR A 242 SER A 247 E 3 VAL A 152 ? GLY A 155 ? VAL A 202 GLY A 205 E 4 ASN A 160 ? SER A 163 ? ASN A 210 SER A 213 F 1 LEU B 5 ? GLU B 6 ? LEU B 59 GLU B 60 F 2 ILE B 34 ? MET B 35 ? ILE B 87 MET B 88 G 1 GLY B 48 ? PHE B 50 ? GLY B 100 PHE B 102 G 2 ARG B 179 ? LEU B 187 ? ARG B 229 LEU B 237 G 3 MET B 126 ? HIS B 134 ? MET B 176 HIS B 184 G 4 TYR B 206 ? ARG B 213 ? TYR B 256 ARG B 263 G 5 VAL B 63 ? LYS B 70 ? VAL B 115 LYS B 119 H 1 GLY B 48 ? PHE B 50 ? GLY B 100 PHE B 102 H 2 ARG B 179 ? LEU B 187 ? ARG B 229 LEU B 237 H 3 MET B 126 ? HIS B 134 ? MET B 176 HIS B 184 H 4 LEU B 201 ? PRO B 204 ? LEU B 251 PRO B 254 H 5 MET B 101 ? TRP B 103 ? MET B 151 TRP B 153 I 1 SER B 86 ? VAL B 91 ? SER B 136 VAL B 141 I 2 ASN B 94 ? SER B 96 ? ASN B 144 SER B 146 J 1 ALA B 114 ? ASN B 119 ? ALA B 164 ASN B 169 J 2 THR B 192 ? SER B 197 ? THR B 242 SER B 247 J 3 VAL B 152 ? GLY B 155 ? VAL B 202 GLY B 205 J 4 ASN B 160 ? SER B 163 ? ASN B 210 SER B 213 # 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 LEU A 5 ? N LEU A 59 O MET A 35 ? O MET A 88 A 2 3 N ILE A 34 ? N ILE A 87 O MET A 219 ? O MET A 268 B 1 2 N SER A 49 ? N SER A 101 O PHE A 182 ? O PHE A 232 B 2 3 O ARG A 179 ? O ARG A 229 N HIS A 134 ? N HIS A 184 B 3 4 N LEU A 127 ? N LEU A 177 O PHE A 208 ? O PHE A 258 B 4 5 O GLY A 207 ? O GLY A 257 N VAL A 69 ? N VAL A 118 C 1 2 N SER A 49 ? N SER A 101 O PHE A 182 ? O PHE A 232 C 2 3 O ARG A 179 ? O ARG A 229 N HIS A 134 ? N HIS A 184 C 3 4 N GLY A 131 ? N GLY A 181 O ILE A 202 ? O ILE A 252 C 4 5 O ALA A 203 ? O ALA A 253 N VAL A 102 ? N VAL A 152 D 1 2 N SER A 86 ? N SER A 136 O SER A 96 ? O SER A 146 E 1 2 N GLY A 116 ? N GLY A 166 O PHE A 195 ? O PHE A 245 E 2 3 O GLU A 196 ? O GLU A 246 N SER A 153 ? N SER A 203 E 3 4 N VAL A 154 ? N VAL A 204 O LYS A 161 ? O LYS A 211 F 1 2 N LEU B 5 ? N LEU B 59 O MET B 35 ? O MET B 88 G 1 2 N SER B 49 ? N SER B 101 O PHE B 182 ? O PHE B 232 G 2 3 O ARG B 179 ? O ARG B 229 N HIS B 134 ? N HIS B 184 G 3 4 N LEU B 127 ? N LEU B 177 O PHE B 208 ? O PHE B 258 G 4 5 O GLY B 207 ? O GLY B 257 N VAL B 69 ? N VAL B 118 H 1 2 N SER B 49 ? N SER B 101 O PHE B 182 ? O PHE B 232 H 2 3 O ARG B 179 ? O ARG B 229 N HIS B 134 ? N HIS B 184 H 3 4 N GLY B 131 ? N GLY B 181 O ILE B 202 ? O ILE B 252 H 4 5 O ALA B 203 ? O ALA B 253 N VAL B 102 ? N VAL B 152 I 1 2 N SER B 86 ? N SER B 136 O SER B 96 ? O SER B 146 J 1 2 N GLY B 116 ? N GLY B 166 O PHE B 195 ? O PHE B 245 J 2 3 O GLU B 196 ? O GLU B 246 N SER B 153 ? N SER B 203 J 3 4 N VAL B 154 ? N VAL B 204 O LYS B 161 ? O LYS B 211 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG B 5467' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 5467' AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE EPE A 3380' AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE EPE B 3380' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 8 HOH G . ? HOH A 410 . ? 1_546 ? 2 AC1 8 ASN B 119 ? ASN B 169 . ? 1_555 ? 3 AC1 8 TRP B 190 ? TRP B 240 . ? 1_555 ? 4 AC1 8 HOH H . ? HOH B 287 . ? 1_555 ? 5 AC1 8 HOH H . ? HOH B 322 . ? 1_555 ? 6 AC1 8 HOH H . ? HOH B 353 . ? 1_555 ? 7 AC1 8 HOH H . ? HOH B 436 . ? 1_555 ? 8 AC1 8 HOH H . ? HOH B 730 . ? 1_555 ? 9 AC2 5 HOH G . ? HOH A 21 . ? 1_555 ? 10 AC2 5 ASN A 119 ? ASN A 169 . ? 1_555 ? 11 AC2 5 THR A 121 ? THR A 171 . ? 1_555 ? 12 AC2 5 TRP A 190 ? TRP A 240 . ? 1_555 ? 13 AC2 5 HOH H . ? HOH B 504 . ? 1_564 ? 14 AC3 10 THR A 83 ? THR A 133 . ? 1_555 ? 15 AC3 10 GLY A 84 ? GLY A 134 . ? 1_555 ? 16 AC3 10 GLY A 85 ? GLY A 135 . ? 1_555 ? 17 AC3 10 SER A 86 ? SER A 136 . ? 1_555 ? 18 AC3 10 LEU A 144 ? LEU A 194 . ? 1_555 ? 19 AC3 10 GLN A 176 ? GLN A 226 . ? 1_555 ? 20 AC3 10 HOH G . ? HOH A 330 . ? 1_555 ? 21 AC3 10 HOH G . ? HOH A 376 . ? 1_555 ? 22 AC3 10 HOH G . ? HOH A 400 . ? 1_555 ? 23 AC3 10 HOH G . ? HOH A 738 . ? 1_555 ? 24 AC4 10 THR B 83 ? THR B 133 . ? 1_555 ? 25 AC4 10 GLY B 84 ? GLY B 134 . ? 1_555 ? 26 AC4 10 GLY B 85 ? GLY B 135 . ? 1_555 ? 27 AC4 10 SER B 86 ? SER B 136 . ? 1_555 ? 28 AC4 10 LEU B 144 ? LEU B 194 . ? 1_555 ? 29 AC4 10 GLN B 176 ? GLN B 226 . ? 1_555 ? 30 AC4 10 HOH H . ? HOH B 331 . ? 1_555 ? 31 AC4 10 HOH H . ? HOH B 342 . ? 1_555 ? 32 AC4 10 HOH H . ? HOH B 370 . ? 1_555 ? 33 AC4 10 HOH H . ? HOH B 417 . ? 1_555 ? # _atom_sites.entry_id 3QQI _atom_sites.fract_transf_matrix[1][1] 0.025887 _atom_sites.fract_transf_matrix[1][2] -0.008351 _atom_sites.fract_transf_matrix[1][3] -0.001257 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016861 _atom_sites.fract_transf_matrix[2][3] -0.007509 _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] 0.016831 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLY A 1 1 ? 40.618 -41.526 -3.570 1.00 33.52 ? 55 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 40.261 -42.247 -4.798 1.00 30.76 ? 55 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 39.504 -43.558 -4.677 1.00 31.78 ? 55 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 40.121 -44.595 -4.392 1.00 36.80 ? 55 GLY A O 1 ATOM 5 N N . ILE A 1 2 ? 38.179 -43.572 -4.970 1.00 23.59 ? 56 ILE A N 1 ATOM 6 C CA . ILE A 1 2 ? 37.341 -42.387 -5.335 1.00 20.44 ? 56 ILE A CA 1 ATOM 7 C C . ILE A 1 2 ? 37.309 -41.425 -4.168 1.00 22.97 ? 56 ILE A C 1 ATOM 8 O O . ILE A 1 2 ? 37.049 -41.861 -3.052 1.00 21.90 ? 56 ILE A O 1 ATOM 9 C CB . ILE A 1 2 ? 35.916 -42.794 -5.806 1.00 22.78 ? 56 ILE A CB 1 ATOM 10 C CG1 . ILE A 1 2 ? 35.982 -43.520 -7.158 1.00 25.24 ? 56 ILE A CG1 1 ATOM 11 C CG2 . ILE A 1 2 ? 34.937 -41.584 -5.875 1.00 20.70 ? 56 ILE A CG2 1 ATOM 12 C CD1 . ILE A 1 2 ? 34.840 -44.445 -7.414 1.00 39.35 ? 56 ILE A CD1 1 ATOM 13 N N . PRO A 1 3 ? 37.578 -40.115 -4.393 1.00 20.47 ? 57 PRO A N 1 ATOM 14 C CA . PRO A 1 3 ? 37.610 -39.186 -3.261 1.00 21.52 ? 57 PRO A CA 1 ATOM 15 C C . PRO A 1 3 ? 36.244 -38.772 -2.735 1.00 23.24 ? 57 PRO A C 1 ATOM 16 O O . PRO A 1 3 ? 35.258 -38.809 -3.459 1.00 22.17 ? 57 PRO A O 1 ATOM 17 C CB . PRO A 1 3 ? 38.332 -37.958 -3.852 1.00 23.18 ? 57 PRO A CB 1 ATOM 18 C CG . PRO A 1 3 ? 37.970 -37.986 -5.286 1.00 26.32 ? 57 PRO A CG 1 ATOM 19 C CD . PRO A 1 3 ? 37.943 -39.438 -5.655 1.00 21.67 ? 57 PRO A CD 1 ATOM 20 N N . PRO A 1 4 ? 36.184 -38.266 -1.489 1.00 23.69 ? 58 PRO A N 1 ATOM 21 C CA . PRO A 1 4 ? 34.907 -37.719 -0.989 1.00 22.77 ? 58 PRO A CA 1 ATOM 22 C C . PRO A 1 4 ? 34.578 -36.393 -1.666 1.00 25.56 ? 58 PRO A C 1 ATOM 23 O O . PRO A 1 4 ? 35.470 -35.724 -2.224 1.00 26.80 ? 58 PRO A O 1 ATOM 24 C CB . PRO A 1 4 ? 35.191 -37.431 0.495 1.00 25.60 ? 58 PRO A CB 1 ATOM 25 C CG . PRO A 1 4 ? 36.484 -38.190 0.804 1.00 29.87 ? 58 PRO A CG 1 ATOM 26 C CD . PRO A 1 4 ? 37.255 -38.153 -0.477 1.00 24.92 ? 58 PRO A CD 1 ATOM 27 N N . LEU A 1 5 ? 33.307 -35.995 -1.567 1.00 18.19 ? 59 LEU A N 1 ATOM 28 C CA . LEU A 1 5 ? 32.852 -34.686 -1.986 1.00 16.66 ? 59 LEU A CA 1 ATOM 29 C C . LEU A 1 5 ? 32.901 -33.831 -0.695 1.00 19.50 ? 59 LEU A C 1 ATOM 30 O O . LEU A 1 5 ? 32.145 -34.082 0.225 1.00 19.11 ? 59 LEU A O 1 ATOM 31 C CB . LEU A 1 5 ? 31.416 -34.734 -2.547 1.00 17.04 ? 59 LEU A CB 1 ATOM 32 C CG . LEU A 1 5 ? 30.784 -33.386 -2.930 1.00 21.23 ? 59 LEU A CG 1 ATOM 33 C CD1 . LEU A 1 5 ? 31.681 -32.585 -3.905 1.00 21.86 ? 59 LEU A CD1 1 ATOM 34 C CD2 . LEU A 1 5 ? 29.378 -33.589 -3.499 1.00 22.92 ? 59 LEU A CD2 1 ATOM 35 N N . GLU A 1 6 ? 33.812 -32.853 -0.627 1.00 17.90 ? 60 GLU A N 1 ATOM 36 C CA . GLU A 1 6 ? 33.913 -31.998 0.549 1.00 18.75 ? 60 GLU A CA 1 ATOM 37 C C . GLU A 1 6 ? 33.176 -30.735 0.193 1.00 22.37 ? 60 GLU A C 1 ATOM 38 O O . GLU A 1 6 ? 33.572 -30.014 -0.749 1.00 24.03 ? 60 GLU A O 1 ATOM 39 C CB . GLU A 1 6 ? 35.384 -31.727 0.946 1.00 22.07 ? 60 GLU A CB 1 ATOM 40 C CG . GLU A 1 6 ? 35.541 -30.687 2.044 1.00 35.34 ? 60 GLU A CG 1 ATOM 41 C CD . GLU A 1 6 ? 34.860 -30.964 3.372 1.00 57.74 ? 60 GLU A CD 1 ATOM 42 O OE1 . GLU A 1 6 ? 35.339 -31.865 4.100 1.00 65.37 ? 60 GLU A OE1 1 ATOM 43 O OE2 . GLU A 1 6 ? 33.881 -30.253 3.705 1.00 40.61 ? 60 GLU A OE2 1 ATOM 44 N N . LEU A 1 7 ? 32.102 -30.457 0.935 1.00 18.50 ? 61 LEU A N 1 ATOM 45 C CA . LEU A 1 7 ? 31.298 -29.280 0.632 1.00 17.53 ? 61 LEU A CA 1 ATOM 46 C C . LEU A 1 7 ? 31.904 -27.991 1.161 1.00 21.81 ? 61 LEU A C 1 ATOM 47 O O . LEU A 1 7 ? 31.507 -26.927 0.704 1.00 21.22 ? 61 LEU A O 1 ATOM 48 C CB . LEU A 1 7 ? 29.839 -29.418 1.092 1.00 17.34 ? 61 LEU A CB 1 ATOM 49 C CG . LEU A 1 7 ? 29.034 -30.578 0.552 1.00 21.97 ? 61 LEU A CG 1 ATOM 50 C CD1 . LEU A 1 7 ? 27.783 -30.766 1.398 1.00 22.19 ? 61 LEU A CD1 1 ATOM 51 C CD2 . LEU A 1 7 ? 28.705 -30.384 -0.926 1.00 23.81 ? 61 LEU A CD2 1 ATOM 52 N N . GLY A 1 8 ? 32.897 -28.085 2.042 1.00 22.47 ? 62 GLY A N 1 ATOM 53 C CA . GLY A 1 8 ? 33.508 -26.895 2.634 1.00 22.13 ? 62 GLY A CA 1 ATOM 54 C C . GLY A 1 8 ? 32.452 -26.094 3.375 1.00 25.43 ? 62 GLY A C 1 ATOM 55 O O . GLY A 1 8 ? 31.700 -26.650 4.168 1.00 25.69 ? 62 GLY A O 1 ATOM 56 N N . ASP A 1 9 ? 32.291 -24.819 3.020 1.00 22.97 ? 63 ASP A N 1 ATOM 57 C CA . ASP A 1 9 ? 31.318 -23.890 3.623 1.00 23.79 ? 63 ASP A CA 1 ATOM 58 C C . ASP A 1 9 ? 29.878 -24.058 3.114 1.00 26.14 ? 63 ASP A C 1 ATOM 59 O O . ASP A 1 9 ? 28.975 -23.401 3.613 1.00 25.60 ? 63 ASP A O 1 ATOM 60 C CB . ASP A 1 9 ? 31.786 -22.459 3.290 1.00 26.80 ? 63 ASP A CB 1 ATOM 61 C CG . ASP A 1 9 ? 32.241 -22.316 1.837 1.00 47.10 ? 63 ASP A CG 1 ATOM 62 O OD1 . ASP A 1 9 ? 33.485 -22.354 1.587 1.00 47.54 ? 63 ASP A OD1 1 ATOM 63 O OD2 . ASP A 1 9 ? 31.362 -22.267 0.939 1.00 56.77 ? 63 ASP A OD2 1 ATOM 64 N N . CYS A 1 10 ? 29.683 -24.893 2.105 1.00 23.37 ? 64 CYS A N 1 ATOM 65 C CA . CYS A 1 10 ? 28.394 -25.064 1.463 1.00 24.07 ? 64 CYS A CA 1 ATOM 66 C C . CYS A 1 10 ? 27.544 -26.141 2.115 1.00 24.68 ? 64 CYS A C 1 ATOM 67 O O . CYS A 1 10 ? 28.063 -27.128 2.644 1.00 24.09 ? 64 CYS A O 1 ATOM 68 C CB . CYS A 1 10 ? 28.576 -25.294 -0.034 1.00 26.93 ? 64 CYS A CB 1 ATOM 69 S SG . CYS A 1 10 ? 29.073 -23.794 -0.942 1.00 32.82 ? 64 CYS A SG 1 ATOM 70 N N . SER A 1 11 ? 26.237 -25.877 2.186 1.00 21.14 ? 65 SER A N 1 ATOM 71 C CA . SER A 1 11 ? 25.279 -26.847 2.710 1.00 19.87 ? 65 SER A CA 1 ATOM 72 C C . SER A 1 11 ? 24.740 -27.640 1.500 1.00 21.34 ? 65 SER A C 1 ATOM 73 O O . SER A 1 11 ? 24.905 -27.216 0.362 1.00 19.66 ? 65 SER A O 1 ATOM 74 C CB . SER A 1 11 ? 24.133 -26.111 3.406 1.00 21.93 ? 65 SER A CB 1 ATOM 75 O OG . SER A 1 11 ? 23.293 -25.486 2.439 1.00 20.33 ? 65 SER A OG 1 ATOM 76 N N . ILE A 1 12 ? 24.056 -28.755 1.740 1.00 19.95 ? 66 ILE A N 1 ATOM 77 C CA . ILE A 1 12 ? 23.466 -29.543 0.662 1.00 18.77 ? 66 ILE A CA 1 ATOM 78 C C . ILE A 1 12 ? 22.475 -28.656 -0.132 1.00 19.32 ? 66 ILE A C 1 ATOM 79 O O . ILE A 1 12 ? 22.484 -28.678 -1.355 1.00 17.37 ? 66 ILE A O 1 ATOM 80 C CB . ILE A 1 12 ? 22.797 -30.822 1.266 1.00 22.89 ? 66 ILE A CB 1 ATOM 81 C CG1 . ILE A 1 12 ? 23.870 -31.833 1.771 1.00 25.27 ? 66 ILE A CG1 1 ATOM 82 C CG2 . ILE A 1 12 ? 21.794 -31.439 0.302 1.00 21.46 ? 66 ILE A CG2 1 ATOM 83 C CD1 . ILE A 1 12 ? 24.697 -32.601 0.717 1.00 35.60 ? 66 ILE A CD1 1 ATOM 84 N N . ALA A 1 13 ? 21.689 -27.839 0.575 1.00 17.79 ? 67 ALA A N 1 ATOM 85 C CA . ALA A 1 13 ? 20.760 -26.871 -0.023 1.00 17.94 ? 67 ALA A CA 1 ATOM 86 C C . ALA A 1 13 ? 21.495 -25.898 -0.926 1.00 18.16 ? 67 ALA A C 1 ATOM 87 O O . ALA A 1 13 ? 21.106 -25.738 -2.081 1.00 20.05 ? 67 ALA A O 1 ATOM 88 C CB . ALA A 1 13 ? 20.025 -26.110 1.070 1.00 19.49 ? 67 ALA A CB 1 ATOM 89 N N . GLY A 1 14 ? 22.613 -25.348 -0.454 1.00 16.38 ? 68 GLY A N 1 ATOM 90 C CA . GLY A 1 14 ? 23.387 -24.402 -1.259 1.00 15.45 ? 68 GLY A CA 1 ATOM 91 C C . GLY A 1 14 ? 23.895 -25.039 -2.532 1.00 16.65 ? 68 GLY A C 1 ATOM 92 O O . GLY A 1 14 ? 23.894 -24.421 -3.600 1.00 18.10 ? 68 GLY A O 1 ATOM 93 N N . TRP A 1 15 ? 24.409 -26.266 -2.412 1.00 14.38 ? 69 TRP A N 1 ATOM 94 C CA . TRP A 1 15 ? 24.918 -27.011 -3.566 1.00 14.26 ? 69 TRP A CA 1 ATOM 95 C C . TRP A 1 15 ? 23.825 -27.271 -4.617 1.00 17.40 ? 69 TRP A C 1 ATOM 96 O O . TRP A 1 15 ? 23.958 -26.861 -5.790 1.00 16.34 ? 69 TRP A O 1 ATOM 97 C CB . TRP A 1 15 ? 25.553 -28.305 -3.051 1.00 14.51 ? 69 TRP A CB 1 ATOM 98 C CG . TRP A 1 15 ? 25.841 -29.336 -4.078 1.00 15.73 ? 69 TRP A CG 1 ATOM 99 C CD1 . TRP A 1 15 ? 26.292 -29.145 -5.355 1.00 18.68 ? 69 TRP A CD1 1 ATOM 100 C CD2 . TRP A 1 15 ? 25.812 -30.755 -3.865 1.00 15.90 ? 69 TRP A CD2 1 ATOM 101 N NE1 . TRP A 1 15 ? 26.458 -30.362 -5.975 1.00 19.51 ? 69 TRP A NE1 1 ATOM 102 C CE2 . TRP A 1 15 ? 26.220 -31.365 -5.068 1.00 19.80 ? 69 TRP A CE2 1 ATOM 103 C CE3 . TRP A 1 15 ? 25.428 -31.565 -2.786 1.00 17.98 ? 69 TRP A CE3 1 ATOM 104 C CZ2 . TRP A 1 15 ? 26.290 -32.764 -5.216 1.00 20.25 ? 69 TRP A CZ2 1 ATOM 105 C CZ3 . TRP A 1 15 ? 25.535 -32.959 -2.918 1.00 19.75 ? 69 TRP A CZ3 1 ATOM 106 C CH2 . TRP A 1 15 ? 25.949 -33.533 -4.119 1.00 20.69 ? 69 TRP A CH2 1 ATOM 107 N N . LEU A 1 16 ? 22.746 -27.944 -4.193 1.00 13.91 ? 70 LEU A N 1 ATOM 108 C CA . LEU A 1 16 ? 21.636 -28.294 -5.089 1.00 16.19 ? 70 LEU A CA 1 ATOM 109 C C . LEU A 1 16 ? 20.879 -27.125 -5.679 1.00 17.09 ? 70 LEU A C 1 ATOM 110 O O . LEU A 1 16 ? 20.554 -27.152 -6.861 1.00 18.27 ? 70 LEU A O 1 ATOM 111 C CB . LEU A 1 16 ? 20.703 -29.286 -4.391 1.00 16.51 ? 70 LEU A CB 1 ATOM 112 C CG . LEU A 1 16 ? 21.424 -30.584 -3.910 1.00 22.01 ? 70 LEU A CG 1 ATOM 113 C CD1 . LEU A 1 16 ? 20.435 -31.570 -3.205 1.00 22.61 ? 70 LEU A CD1 1 ATOM 114 C CD2 . LEU A 1 16 ? 22.242 -31.248 -5.043 1.00 24.33 ? 70 LEU A CD2 1 ATOM 115 N N . LEU A 1 17 ? 20.639 -26.080 -4.900 1.00 13.27 ? 71 LEU A N 1 ATOM 116 C CA . LEU A 1 17 ? 19.980 -24.897 -5.435 1.00 13.25 ? 71 LEU A CA 1 ATOM 117 C C . LEU A 1 17 ? 20.916 -24.082 -6.328 1.00 16.10 ? 71 LEU A C 1 ATOM 118 O O . LEU A 1 17 ? 20.434 -23.369 -7.199 1.00 14.03 ? 71 LEU A O 1 ATOM 119 C CB . LEU A 1 17 ? 19.516 -24.004 -4.266 1.00 13.17 ? 71 LEU A CB 1 ATOM 120 C CG . LEU A 1 17 ? 18.381 -24.595 -3.450 1.00 16.08 ? 71 LEU A CG 1 ATOM 121 C CD1 . LEU A 1 17 ? 18.096 -23.794 -2.239 1.00 15.50 ? 71 LEU A CD1 1 ATOM 122 C CD2 . LEU A 1 17 ? 17.116 -24.733 -4.300 1.00 20.11 ? 71 LEU A CD2 1 ATOM 123 N N . GLY A 1 18 ? 22.220 -24.122 -6.043 1.00 12.64 ? 72 GLY A N 1 ATOM 124 C CA . GLY A 1 18 ? 23.185 -23.342 -6.811 1.00 14.26 ? 72 GLY A CA 1 ATOM 125 C C . GLY A 1 18 ? 23.433 -21.986 -6.202 1.00 14.43 ? 72 GLY A C 1 ATOM 126 O O . GLY A 1 18 ? 23.446 -20.975 -6.920 1.00 14.75 ? 72 GLY A O 1 ATOM 127 N N . ASN A 1 19 ? 23.592 -21.936 -4.866 1.00 14.18 ? 73 ASN A N 1 ATOM 128 C CA . ASN A 1 19 ? 23.929 -20.661 -4.231 1.00 15.20 ? 73 ASN A CA 1 ATOM 129 C C . ASN A 1 19 ? 25.227 -20.190 -4.942 1.00 16.75 ? 73 ASN A C 1 ATOM 130 O O . ASN A 1 19 ? 26.165 -20.960 -5.087 1.00 16.64 ? 73 ASN A O 1 ATOM 131 C CB . ASN A 1 19 ? 24.217 -20.897 -2.760 1.00 17.35 ? 73 ASN A CB 1 ATOM 132 C CG . ASN A 1 19 ? 24.662 -19.691 -1.972 1.00 24.90 ? 73 ASN A CG 1 ATOM 133 O OD1 . ASN A 1 19 ? 25.469 -18.834 -2.399 1.00 19.26 ? 73 ASN A OD1 1 ATOM 134 N ND2 . ASN A 1 19 ? 24.202 -19.626 -0.774 1.00 15.53 ? 73 ASN A ND2 1 ATOM 135 N N . PRO A 1 20 ? 25.300 -18.948 -5.431 1.00 18.14 ? 74 PRO A N 1 ATOM 136 C CA . PRO A 1 20 ? 26.508 -18.524 -6.186 1.00 18.73 ? 74 PRO A CA 1 ATOM 137 C C . PRO A 1 20 ? 27.838 -18.649 -5.422 1.00 23.35 ? 74 PRO A C 1 ATOM 138 O O . PRO A 1 20 ? 28.926 -18.895 -6.004 1.00 23.91 ? 74 PRO A O 1 ATOM 139 C CB . PRO A 1 20 ? 26.176 -17.091 -6.558 1.00 21.93 ? 74 PRO A CB 1 ATOM 140 C CG . PRO A 1 20 ? 24.647 -17.054 -6.629 1.00 24.35 ? 74 PRO A CG 1 ATOM 141 C CD . PRO A 1 20 ? 24.253 -17.891 -5.437 1.00 18.85 ? 74 PRO A CD 1 ATOM 142 N N . GLU A 1 21 ? 27.761 -18.581 -4.097 1.00 18.74 ? 75 GLU A N 1 ATOM 143 C CA . GLU A 1 21 ? 28.984 -18.791 -3.303 1.00 20.92 ? 75 GLU A CA 1 ATOM 144 C C . GLU A 1 21 ? 29.508 -20.265 -3.412 1.00 25.85 ? 75 GLU A C 1 ATOM 145 O O . GLU A 1 21 ? 30.636 -20.578 -2.995 1.00 25.03 ? 75 GLU A O 1 ATOM 146 C CB . GLU A 1 21 ? 28.703 -18.439 -1.835 1.00 22.76 ? 75 GLU A CB 1 ATOM 147 C CG . GLU A 1 21 ? 28.579 -16.938 -1.643 1.00 29.68 ? 75 GLU A CG 1 ATOM 148 C CD . GLU A 1 21 ? 29.832 -16.124 -1.364 1.00 65.72 ? 75 GLU A CD 1 ATOM 149 O OE1 . GLU A 1 21 ? 30.950 -16.584 -1.698 1.00 72.61 ? 75 GLU A OE1 1 ATOM 150 O OE2 . GLU A 1 21 ? 29.685 -14.998 -0.834 1.00 65.48 ? 75 GLU A OE2 1 ATOM 151 N N . CYS A 1 22 ? 28.674 -21.155 -3.952 1.00 22.32 ? 76 CYS A N 1 ATOM 152 C CA . CYS A 1 22 ? 28.940 -22.583 -4.106 1.00 23.49 ? 76 CYS A CA 1 ATOM 153 C C . CYS A 1 22 ? 29.274 -22.922 -5.563 1.00 22.06 ? 76 CYS A C 1 ATOM 154 O O . CYS A 1 22 ? 29.298 -24.101 -5.917 1.00 20.81 ? 76 CYS A O 1 ATOM 155 C CB . CYS A 1 22 ? 27.739 -23.386 -3.603 1.00 25.60 ? 76 CYS A CB 1 ATOM 156 S SG . CYS A 1 22 ? 27.350 -23.083 -1.855 1.00 30.68 ? 76 CYS A SG 1 ATOM 157 N N . ASP A 1 23 ? 29.576 -21.912 -6.397 1.00 20.57 ? 77 ASP A N 1 ATOM 158 C CA . ASP A 1 23 ? 29.914 -22.149 -7.818 1.00 19.77 ? 77 ASP A CA 1 ATOM 159 C C . ASP A 1 23 ? 30.971 -23.219 -8.072 1.00 21.86 ? 77 ASP A C 1 ATOM 160 O O . ASP A 1 23 ? 30.952 -23.890 -9.110 1.00 21.06 ? 77 ASP A O 1 ATOM 161 C CB . ASP A 1 23 ? 30.294 -20.845 -8.526 1.00 21.33 ? 77 ASP A CB 1 ATOM 162 C CG . ASP A 1 23 ? 29.137 -19.946 -8.870 1.00 27.44 ? 77 ASP A CG 1 ATOM 163 O OD1 . ASP A 1 23 ? 27.982 -20.404 -8.788 1.00 23.35 ? 77 ASP A OD1 1 ATOM 164 O OD2 . ASP A 1 23 ? 29.388 -18.793 -9.268 1.00 34.74 ? 77 ASP A OD2 1 ATOM 165 N N . ARG A 1 24 ? 31.906 -23.390 -7.128 1.00 17.48 ? 78 ARG A N 1 ATOM 166 C CA . ARG A 1 24 ? 32.901 -24.455 -7.256 1.00 18.07 ? 78 ARG A CA 1 ATOM 167 C C . ARG A 1 24 ? 32.305 -25.855 -7.372 1.00 21.05 ? 78 ARG A C 1 ATOM 168 O O . ARG A 1 24 ? 32.979 -26.758 -7.857 1.00 20.57 ? 78 ARG A O 1 ATOM 169 C CB . ARG A 1 24 ? 33.901 -24.377 -6.108 1.00 17.31 ? 78 ARG A CB 1 ATOM 170 C CG . ARG A 1 24 ? 33.402 -24.931 -4.802 1.00 18.42 ? 78 ARG A CG 1 ATOM 171 C CD . ARG A 1 24 ? 34.303 -24.460 -3.681 1.00 18.81 ? 78 ARG A CD 1 ATOM 172 N NE . ARG A 1 24 ? 33.736 -24.818 -2.391 1.00 21.97 ? 78 ARG A NE 1 ATOM 173 C CZ . ARG A 1 24 ? 32.836 -24.088 -1.743 1.00 17.76 ? 78 ARG A CZ 1 ATOM 174 N NH1 . ARG A 1 24 ? 32.428 -22.923 -2.243 1.00 21.82 ? 78 ARG A NH1 1 ATOM 175 N NH2 . ARG A 1 24 ? 32.364 -24.494 -0.576 1.00 26.58 ? 78 ARG A NH2 1 ATOM 176 N N . LEU A 1 25 ? 31.041 -26.026 -6.910 1.00 19.77 ? 79 LEU A N 1 ATOM 177 C CA . LEU A 1 25 ? 30.337 -27.299 -6.907 1.00 18.60 ? 79 LEU A CA 1 ATOM 178 C C . LEU A 1 25 ? 29.293 -27.417 -8.029 1.00 22.08 ? 79 LEU A C 1 ATOM 179 O O . LEU A 1 25 ? 28.470 -28.323 -7.974 1.00 20.29 ? 79 LEU A O 1 ATOM 180 C CB . LEU A 1 25 ? 29.644 -27.487 -5.529 1.00 18.47 ? 79 LEU A CB 1 ATOM 181 C CG . LEU A 1 25 ? 30.477 -27.327 -4.272 1.00 19.65 ? 79 LEU A CG 1 ATOM 182 C CD1 . LEU A 1 25 ? 29.537 -27.279 -3.021 1.00 19.56 ? 79 LEU A CD1 1 ATOM 183 C CD2 . LEU A 1 25 ? 31.496 -28.441 -4.130 1.00 25.37 ? 79 LEU A CD2 1 ATOM 184 N N . LEU A 1 26 ? 29.341 -26.540 -9.057 1.00 19.62 ? 80 LEU A N 1 ATOM 185 C CA . LEU A 1 26 ? 28.384 -26.594 -10.170 1.00 19.29 ? 80 LEU A CA 1 ATOM 186 C C . LEU A 1 26 ? 28.426 -27.867 -10.975 1.00 26.88 ? 80 LEU A C 1 ATOM 187 O O . LEU A 1 26 ? 27.402 -28.270 -11.508 1.00 28.08 ? 80 LEU A O 1 ATOM 188 C CB . LEU A 1 26 ? 28.496 -25.341 -11.085 1.00 20.05 ? 80 LEU A CB 1 ATOM 189 C CG . LEU A 1 26 ? 27.876 -24.091 -10.554 1.00 22.91 ? 80 LEU A CG 1 ATOM 190 C CD1 . LEU A 1 26 ? 28.491 -22.866 -11.213 1.00 23.38 ? 80 LEU A CD1 1 ATOM 191 C CD2 . LEU A 1 26 ? 26.345 -24.103 -10.722 1.00 26.73 ? 80 LEU A CD2 1 ATOM 192 N N . SER A 1 27 ? 29.587 -28.523 -11.015 1.00 23.68 ? 81 SER A N 1 ATOM 193 C CA . SER A 1 27 ? 29.767 -29.797 -11.704 1.00 25.03 ? 81 SER A CA 1 ATOM 194 C C . SER A 1 27 ? 30.730 -30.622 -10.888 1.00 27.69 ? 81 SER A C 1 ATOM 195 O O . SER A 1 27 ? 31.885 -30.221 -10.695 1.00 28.08 ? 81 SER A O 1 ATOM 196 C CB . SER A 1 27 ? 30.292 -29.569 -13.121 1.00 30.07 ? 81 SER A CB 1 ATOM 197 O OG . SER A 1 27 ? 29.968 -30.693 -13.923 1.00 42.25 ? 81 SER A OG 1 ATOM 198 N N . VAL A 1 28 A 30.251 -31.740 -10.342 1.00 22.26 ? 81 VAL A N 1 ATOM 199 C CA . VAL A 1 28 A 31.102 -32.563 -9.484 1.00 21.94 ? 81 VAL A CA 1 ATOM 200 C C . VAL A 1 28 A 31.171 -33.975 -9.983 1.00 24.74 ? 81 VAL A C 1 ATOM 201 O O . VAL A 1 28 A 30.158 -34.497 -10.484 1.00 24.88 ? 81 VAL A O 1 ATOM 202 C CB . VAL A 1 28 A 30.721 -32.494 -7.976 1.00 26.90 ? 81 VAL A CB 1 ATOM 203 C CG1 . VAL A 1 28 A 30.841 -31.069 -7.415 1.00 26.66 ? 81 VAL A CG1 1 ATOM 204 C CG2 . VAL A 1 28 A 29.349 -33.106 -7.704 1.00 26.59 ? 81 VAL A CG2 1 ATOM 205 N N . PRO A 1 29 ? 32.338 -34.638 -9.838 1.00 19.51 ? 82 PRO A N 1 ATOM 206 C CA . PRO A 1 29 ? 32.454 -36.030 -10.296 1.00 17.46 ? 82 PRO A CA 1 ATOM 207 C C . PRO A 1 29 ? 31.916 -36.959 -9.236 1.00 19.82 ? 82 PRO A C 1 ATOM 208 O O . PRO A 1 29 ? 31.459 -36.500 -8.179 1.00 21.39 ? 82 PRO A O 1 ATOM 209 C CB . PRO A 1 29 ? 33.974 -36.201 -10.490 1.00 19.58 ? 82 PRO A CB 1 ATOM 210 C CG . PRO A 1 29 ? 34.551 -35.353 -9.489 1.00 23.81 ? 82 PRO A CG 1 ATOM 211 C CD . PRO A 1 29 ? 33.625 -34.166 -9.278 1.00 20.92 ? 82 PRO A CD 1 ATOM 212 N N . GLU A 1 30 ? 31.974 -38.277 -9.511 1.00 18.78 ? 83 GLU A N 1 ATOM 213 C CA . GLU A 1 30 ? 31.525 -39.299 -8.554 1.00 17.90 ? 83 GLU A CA 1 ATOM 214 C C . GLU A 1 30 ? 32.313 -39.143 -7.266 1.00 18.07 ? 83 GLU A C 1 ATOM 215 O O . GLU A 1 30 ? 33.494 -38.779 -7.309 1.00 18.85 ? 83 GLU A O 1 ATOM 216 C CB . GLU A 1 30 ? 31.801 -40.671 -9.162 1.00 20.25 ? 83 GLU A CB 1 ATOM 217 C CG . GLU A 1 30 ? 31.293 -41.858 -8.368 1.00 29.84 ? 83 GLU A CG 1 ATOM 218 C CD . GLU A 1 30 ? 31.769 -43.194 -8.910 1.00 56.82 ? 83 GLU A CD 1 ATOM 219 O OE1 . GLU A 1 30 ? 32.150 -43.248 -10.104 1.00 39.51 ? 83 GLU A OE1 1 ATOM 220 O OE2 . GLU A 1 30 ? 31.720 -44.194 -8.155 1.00 42.67 ? 83 GLU A OE2 1 ATOM 221 N N . TRP A 1 31 ? 31.661 -39.402 -6.127 1.00 17.24 ? 84 TRP A N 1 ATOM 222 C CA . TRP A 1 31 ? 32.276 -39.302 -4.805 1.00 16.56 ? 84 TRP A CA 1 ATOM 223 C C . TRP A 1 31 ? 32.133 -40.607 -4.019 1.00 19.95 ? 84 TRP A C 1 ATOM 224 O O . TRP A 1 31 ? 31.281 -41.442 -4.341 1.00 18.73 ? 84 TRP A O 1 ATOM 225 C CB . TRP A 1 31 ? 31.666 -38.128 -4.020 1.00 14.94 ? 84 TRP A CB 1 ATOM 226 C CG . TRP A 1 31 ? 30.186 -38.281 -3.798 1.00 14.36 ? 84 TRP A CG 1 ATOM 227 C CD1 . TRP A 1 31 ? 29.573 -39.005 -2.816 1.00 17.31 ? 84 TRP A CD1 1 ATOM 228 C CD2 . TRP A 1 31 ? 29.143 -37.665 -4.555 1.00 14.34 ? 84 TRP A CD2 1 ATOM 229 N NE1 . TRP A 1 31 ? 28.210 -38.889 -2.925 1.00 15.64 ? 84 TRP A NE1 1 ATOM 230 C CE2 . TRP A 1 31 ? 27.916 -38.102 -4.008 1.00 16.69 ? 84 TRP A CE2 1 ATOM 231 C CE3 . TRP A 1 31 ? 29.125 -36.831 -5.685 1.00 15.50 ? 84 TRP A CE3 1 ATOM 232 C CZ2 . TRP A 1 31 ? 26.669 -37.698 -4.533 1.00 17.56 ? 84 TRP A CZ2 1 ATOM 233 C CZ3 . TRP A 1 31 ? 27.888 -36.376 -6.167 1.00 16.32 ? 84 TRP A CZ3 1 ATOM 234 C CH2 . TRP A 1 31 ? 26.688 -36.888 -5.661 1.00 15.57 ? 84 TRP A CH2 1 ATOM 235 N N . SER A 1 32 ? 32.971 -40.766 -2.982 1.00 17.36 ? 85 SER A N 1 ATOM 236 C CA . SER A 1 32 ? 32.934 -41.936 -2.072 1.00 18.03 ? 85 SER A CA 1 ATOM 237 C C . SER A 1 32 ? 31.916 -41.697 -0.933 1.00 21.86 ? 85 SER A C 1 ATOM 238 O O . SER A 1 32 ? 31.244 -42.638 -0.483 1.00 20.24 ? 85 SER A O 1 ATOM 239 C CB . SER A 1 32 ? 34.325 -42.207 -1.504 1.00 21.24 ? 85 SER A CB 1 ATOM 240 O OG . SER A 1 32 ? 34.858 -41.052 -0.879 1.00 23.78 ? 85 SER A OG 1 ATOM 241 N N . TYR A 1 33 ? 31.812 -40.441 -0.477 1.00 18.16 ? 86 TYR A N 1 ATOM 242 C CA . TYR A 1 33 ? 30.842 -39.959 0.508 1.00 18.34 ? 86 TYR A CA 1 ATOM 243 C C . TYR A 1 33 ? 30.878 -38.432 0.484 1.00 19.82 ? 86 TYR A C 1 ATOM 244 O O . TYR A 1 33 ? 31.773 -37.850 -0.142 1.00 20.13 ? 86 TYR A O 1 ATOM 245 C CB . TYR A 1 33 ? 31.092 -40.505 1.926 1.00 21.39 ? 86 TYR A CB 1 ATOM 246 C CG . TYR A 1 33 ? 32.499 -40.324 2.460 1.00 26.18 ? 86 TYR A CG 1 ATOM 247 C CD1 . TYR A 1 33 ? 32.846 -39.196 3.200 1.00 29.04 ? 86 TYR A CD1 1 ATOM 248 C CD2 . TYR A 1 33 ? 33.440 -41.346 2.356 1.00 28.31 ? 86 TYR A CD2 1 ATOM 249 C CE1 . TYR A 1 33 ? 34.124 -39.054 3.750 1.00 31.51 ? 86 TYR A CE1 1 ATOM 250 C CE2 . TYR A 1 33 ? 34.723 -41.206 2.880 1.00 30.43 ? 86 TYR A CE2 1 ATOM 251 C CZ . TYR A 1 33 ? 35.056 -40.063 3.587 1.00 41.28 ? 86 TYR A CZ 1 ATOM 252 O OH . TYR A 1 33 ? 36.313 -39.936 4.124 1.00 49.67 ? 86 TYR A OH 1 ATOM 253 N N . ILE A 1 34 ? 29.894 -37.805 1.121 1.00 19.34 ? 87 ILE A N 1 ATOM 254 C CA . ILE A 1 34 ? 29.776 -36.346 1.158 1.00 17.89 ? 87 ILE A CA 1 ATOM 255 C C . ILE A 1 34 ? 30.155 -35.851 2.537 1.00 23.49 ? 87 ILE A C 1 ATOM 256 O O . ILE A 1 34 ? 29.679 -36.405 3.527 1.00 22.37 ? 87 ILE A O 1 ATOM 257 C CB . ILE A 1 34 ? 28.344 -35.895 0.781 1.00 20.27 ? 87 ILE A CB 1 ATOM 258 C CG1 . ILE A 1 34 ? 27.944 -36.377 -0.628 1.00 20.20 ? 87 ILE A CG1 1 ATOM 259 C CG2 . ILE A 1 34 ? 28.186 -34.343 0.874 1.00 21.02 ? 87 ILE A CG2 1 ATOM 260 C CD1 . ILE A 1 34 ? 26.433 -36.410 -0.882 1.00 21.93 ? 87 ILE A CD1 1 ATOM 261 N N . MET A 1 35 ? 31.037 -34.822 2.604 1.00 21.82 ? 88 MET A N 1 ATOM 262 C CA . MET A 1 35 ? 31.456 -34.207 3.865 1.00 23.27 ? 88 MET A CA 1 ATOM 263 C C . MET A 1 35 ? 30.838 -32.811 4.006 1.00 26.53 ? 88 MET A C 1 ATOM 264 O O . MET A 1 35 ? 31.077 -31.937 3.168 1.00 23.39 ? 88 MET A O 1 ATOM 265 C CB . MET A 1 35 ? 32.985 -34.143 3.980 1.00 26.58 ? 88 MET A CB 1 ATOM 266 C CG . MET A 1 35 ? 33.653 -35.499 3.858 1.00 34.42 ? 88 MET A CG 1 ATOM 267 S SD . MET A 1 35 ? 35.474 -35.460 3.765 1.00 43.38 ? 88 MET A SD 1 ATOM 268 C CE . MET A 1 35 ? 35.892 -35.092 5.478 1.00 41.48 ? 88 MET A CE 1 ATOM 269 N N . GLU A 1 36 ? 29.997 -32.624 5.047 1.00 24.42 ? 89 GLU A N 1 ATOM 270 C CA . GLU A 1 36 ? 29.325 -31.369 5.325 1.00 25.03 ? 89 GLU A CA 1 ATOM 271 C C . GLU A 1 36 ? 29.684 -30.920 6.733 1.00 29.23 ? 89 GLU A C 1 ATOM 272 O O . GLU A 1 36 ? 29.754 -31.754 7.647 1.00 28.68 ? 89 GLU A O 1 ATOM 273 C CB . GLU A 1 36 ? 27.800 -31.549 5.204 1.00 27.02 ? 89 GLU A CB 1 ATOM 274 C CG . GLU A 1 36 ? 27.007 -30.252 5.116 1.00 35.87 ? 89 GLU A CG 1 ATOM 275 C CD . GLU A 1 36 ? 25.502 -30.410 5.210 1.00 52.88 ? 89 GLU A CD 1 ATOM 276 O OE1 . GLU A 1 36 ? 25.035 -31.253 6.009 1.00 41.83 ? 89 GLU A OE1 1 ATOM 277 O OE2 . GLU A 1 36 ? 24.783 -29.649 4.524 1.00 41.47 ? 89 GLU A OE2 1 ATOM 278 N N . LYS A 1 37 ? 29.894 -29.600 6.916 1.00 26.14 ? 90 LYS A N 1 ATOM 279 C CA . LYS A 1 37 ? 30.210 -29.027 8.231 1.00 26.44 ? 90 LYS A CA 1 ATOM 280 C C . LYS A 1 37 ? 28.965 -29.031 9.088 1.00 31.35 ? 90 LYS A C 1 ATOM 281 O O . LYS A 1 37 ? 27.869 -29.134 8.553 1.00 29.56 ? 90 LYS A O 1 ATOM 282 C CB . LYS A 1 37 ? 30.786 -27.606 8.110 1.00 28.59 ? 90 LYS A CB 1 ATOM 283 C CG . LYS A 1 37 ? 32.180 -27.553 7.493 1.00 42.60 ? 90 LYS A CG 1 ATOM 284 C CD . LYS A 1 37 ? 32.738 -26.137 7.487 1.00 50.22 ? 90 LYS A CD 1 ATOM 285 C CE . LYS A 1 37 ? 34.067 -26.067 6.783 1.00 53.26 ? 90 LYS A CE 1 ATOM 286 N NZ . LYS A 1 37 ? 34.602 -24.684 6.758 1.00 56.78 ? 90 LYS A NZ 1 ATOM 287 N N . GLU A 1 38 ? 29.127 -28.961 10.428 1.00 33.35 ? 91 GLU A N 1 ATOM 288 C CA . GLU A 1 38 ? 27.992 -28.972 11.359 1.00 35.15 ? 91 GLU A CA 1 ATOM 289 C C . GLU A 1 38 ? 27.023 -27.815 11.099 1.00 39.25 ? 91 GLU A C 1 ATOM 290 O O . GLU A 1 38 ? 25.814 -28.033 11.104 1.00 40.45 ? 91 GLU A O 1 ATOM 291 C CB . GLU A 1 38 ? 28.468 -29.011 12.825 1.00 38.02 ? 91 GLU A CB 1 ATOM 292 C CG . GLU A 1 38 ? 27.490 -29.700 13.766 1.00 49.79 ? 91 GLU A CG 1 ATOM 293 C CD . GLU A 1 38 ? 28.079 -30.732 14.715 1.00 72.39 ? 91 GLU A CD 1 ATOM 294 O OE1 . GLU A 1 38 ? 29.325 -30.801 14.836 1.00 59.02 ? 91 GLU A OE1 1 ATOM 295 O OE2 . GLU A 1 38 ? 27.287 -31.471 15.347 1.00 67.33 ? 91 GLU A OE2 1 ATOM 296 N N . ASN A 1 39 ? 27.546 -26.605 10.829 1.00 35.99 ? 92 ASN A N 1 ATOM 297 C CA . ASN A 1 39 ? 26.730 -25.421 10.497 1.00 34.33 ? 92 ASN A CA 1 ATOM 298 C C . ASN A 1 39 ? 27.343 -24.697 9.269 1.00 34.22 ? 92 ASN A C 1 ATOM 299 O O . ASN A 1 39 ? 28.136 -23.763 9.424 1.00 33.22 ? 92 ASN A O 1 ATOM 300 C CB . ASN A 1 39 ? 26.600 -24.469 11.692 1.00 38.03 ? 92 ASN A CB 1 ATOM 301 C CG . ASN A 1 39 ? 25.837 -25.041 12.854 1.00 57.23 ? 92 ASN A CG 1 ATOM 302 O OD1 . ASN A 1 39 ? 26.414 -25.396 13.881 1.00 50.15 ? 92 ASN A OD1 1 ATOM 303 N ND2 . ASN A 1 39 ? 24.521 -25.123 12.726 1.00 47.06 ? 92 ASN A ND2 1 ATOM 304 N N . PRO A 1 40 ? 27.019 -25.163 8.040 1.00 28.44 ? 93 PRO A N 1 ATOM 305 C CA . PRO A 1 40 ? 27.584 -24.517 6.833 1.00 26.46 ? 93 PRO A CA 1 ATOM 306 C C . PRO A 1 40 ? 27.082 -23.082 6.673 1.00 27.91 ? 93 PRO A C 1 ATOM 307 O O . PRO A 1 40 ? 25.937 -22.806 7.000 1.00 27.01 ? 93 PRO A O 1 ATOM 308 C CB . PRO A 1 40 ? 27.092 -25.405 5.687 1.00 27.41 ? 93 PRO A CB 1 ATOM 309 C CG . PRO A 1 40 ? 26.534 -26.658 6.342 1.00 32.80 ? 93 PRO A CG 1 ATOM 310 C CD . PRO A 1 40 ? 26.082 -26.252 7.689 1.00 29.46 ? 93 PRO A CD 1 ATOM 311 N N . ARG A 1 41 ? 27.916 -22.166 6.173 1.00 24.23 ? 94 ARG A N 1 ATOM 312 C CA . ARG A 1 41 ? 27.476 -20.764 6.052 1.00 23.59 ? 94 ARG A CA 1 ATOM 313 C C . ARG A 1 41 ? 26.671 -20.502 4.809 1.00 24.27 ? 94 ARG A C 1 ATOM 314 O O . ARG A 1 41 ? 25.843 -19.587 4.806 1.00 23.90 ? 94 ARG A O 1 ATOM 315 C CB . ARG A 1 41 ? 28.678 -19.800 5.963 1.00 26.42 ? 94 ARG A CB 1 ATOM 316 C CG . ARG A 1 41 ? 29.757 -19.937 6.990 1.00 36.69 ? 94 ARG A CG 1 ATOM 317 C CD . ARG A 1 41 ? 30.885 -19.035 6.524 1.00 30.21 ? 94 ARG A CD 1 ATOM 318 N NE . ARG A 1 41 ? 30.562 -17.666 6.904 1.00 36.38 ? 94 ARG A NE 1 ATOM 319 C CZ . ARG A 1 41 ? 30.408 -16.651 6.069 1.00 37.35 ? 94 ARG A CZ 1 ATOM 320 N NH1 . ARG A 1 41 ? 30.622 -16.809 4.771 1.00 29.15 ? 94 ARG A NH1 1 ATOM 321 N NH2 . ARG A 1 41 ? 30.113 -15.452 6.532 1.00 24.27 ? 94 ARG A NH2 1 ATOM 322 N N . ASP A 1 42 ? 26.998 -21.212 3.718 1.00 19.66 ? 95 ASP A N 1 ATOM 323 C CA . ASP A 1 42 ? 26.445 -20.971 2.388 1.00 19.77 ? 95 ASP A CA 1 ATOM 324 C C . ASP A 1 42 ? 25.334 -21.941 2.016 1.00 21.41 ? 95 ASP A C 1 ATOM 325 O O . ASP A 1 42 ? 25.585 -23.002 1.464 1.00 18.54 ? 95 ASP A O 1 ATOM 326 C CB . ASP A 1 42 ? 27.581 -20.899 1.366 1.00 20.32 ? 95 ASP A CB 1 ATOM 327 C CG . ASP A 1 42 ? 28.527 -19.726 1.605 1.00 28.92 ? 95 ASP A CG 1 ATOM 328 O OD1 . ASP A 1 42 ? 28.029 -18.593 1.886 1.00 26.53 ? 95 ASP A OD1 1 ATOM 329 O OD2 . ASP A 1 42 ? 29.770 -19.940 1.577 1.00 29.62 ? 95 ASP A OD2 1 ATOM 330 N N . GLY A 1 43 A 24.115 -21.536 2.343 1.00 19.78 ? 95 GLY A N 1 ATOM 331 C CA . GLY A 1 43 A 22.911 -22.325 2.116 1.00 19.30 ? 95 GLY A CA 1 ATOM 332 C C . GLY A 1 43 A 21.896 -21.566 1.313 1.00 22.68 ? 95 GLY A C 1 ATOM 333 O O . GLY A 1 43 A 22.081 -21.338 0.120 1.00 21.04 ? 95 GLY A O 1 ATOM 334 N N . LEU A 1 44 ? 20.833 -21.123 1.974 1.00 22.57 ? 96 LEU A N 1 ATOM 335 C CA . LEU A 1 44 ? 19.807 -20.346 1.312 1.00 21.72 ? 96 LEU A CA 1 ATOM 336 C C . LEU A 1 44 ? 20.229 -18.874 1.343 1.00 25.90 ? 96 LEU A C 1 ATOM 337 O O . LEU A 1 44 ? 20.025 -18.244 2.378 1.00 27.14 ? 96 LEU A O 1 ATOM 338 C CB . LEU A 1 44 ? 18.447 -20.554 2.044 1.00 21.82 ? 96 LEU A CB 1 ATOM 339 C CG . LEU A 1 44 ? 17.552 -21.773 1.628 1.00 26.78 ? 96 LEU A CG 1 ATOM 340 C CD1 . LEU A 1 44 ? 18.299 -22.971 1.360 1.00 25.98 ? 96 LEU A CD1 1 ATOM 341 C CD2 . LEU A 1 44 ? 16.510 -22.082 2.682 1.00 26.97 ? 96 LEU A CD2 1 ATOM 342 N N . CYS A 1 45 ? 20.810 -18.326 0.222 1.00 23.88 ? 97 CYS A N 1 ATOM 343 C CA . CYS A 1 45 ? 21.201 -16.898 0.087 1.00 25.42 ? 97 CYS A CA 1 ATOM 344 C C . CYS A 1 45 ? 19.977 -16.003 0.218 1.00 23.00 ? 97 CYS A C 1 ATOM 345 O O . CYS A 1 45 ? 19.955 -15.072 1.039 1.00 21.12 ? 97 CYS A O 1 ATOM 346 C CB . CYS A 1 45 ? 22.020 -16.593 -1.173 1.00 28.43 ? 97 CYS A CB 1 ATOM 347 S SG . CYS A 1 45 ? 21.267 -17.087 -2.753 1.00 33.96 ? 97 CYS A SG 1 ATOM 348 N N . TYR A 1 46 ? 18.913 -16.351 -0.513 1.00 17.17 ? 98 TYR A N 1 ATOM 349 C CA . TYR A 1 46 ? 17.633 -15.688 -0.298 1.00 15.91 ? 98 TYR A CA 1 ATOM 350 C C . TYR A 1 46 ? 17.072 -16.542 0.849 1.00 15.96 ? 98 TYR A C 1 ATOM 351 O O . TYR A 1 46 ? 17.035 -17.746 0.726 1.00 15.37 ? 98 TYR A O 1 ATOM 352 C CB . TYR A 1 46 ? 16.747 -15.746 -1.544 1.00 16.55 ? 98 TYR A CB 1 ATOM 353 C CG . TYR A 1 46 ? 15.546 -14.834 -1.346 1.00 16.70 ? 98 TYR A CG 1 ATOM 354 C CD1 . TYR A 1 46 ? 15.530 -13.544 -1.872 1.00 18.73 ? 98 TYR A CD1 1 ATOM 355 C CD2 . TYR A 1 46 ? 14.440 -15.256 -0.616 1.00 16.11 ? 98 TYR A CD2 1 ATOM 356 C CE1 . TYR A 1 46 ? 14.414 -12.725 -1.746 1.00 15.53 ? 98 TYR A CE1 1 ATOM 357 C CE2 . TYR A 1 46 ? 13.345 -14.416 -0.412 1.00 17.70 ? 98 TYR A CE2 1 ATOM 358 C CZ . TYR A 1 46 ? 13.340 -13.146 -0.974 1.00 19.63 ? 98 TYR A CZ 1 ATOM 359 O OH . TYR A 1 46 ? 12.235 -12.353 -0.816 1.00 19.69 ? 98 TYR A OH 1 ATOM 360 N N . PRO A 1 47 ? 16.663 -15.942 1.989 1.00 14.59 ? 99 PRO A N 1 ATOM 361 C CA . PRO A 1 47 ? 16.330 -16.770 3.178 1.00 13.41 ? 99 PRO A CA 1 ATOM 362 C C . PRO A 1 47 ? 15.085 -17.608 3.001 1.00 17.45 ? 99 PRO A C 1 ATOM 363 O O . PRO A 1 47 ? 14.232 -17.295 2.167 1.00 13.99 ? 99 PRO A O 1 ATOM 364 C CB . PRO A 1 47 ? 16.164 -15.732 4.295 1.00 17.10 ? 99 PRO A CB 1 ATOM 365 C CG . PRO A 1 47 ? 15.769 -14.478 3.571 1.00 20.42 ? 99 PRO A CG 1 ATOM 366 C CD . PRO A 1 47 ? 16.619 -14.501 2.318 1.00 17.69 ? 99 PRO A CD 1 ATOM 367 N N . GLY A 1 48 ? 14.997 -18.678 3.784 1.00 14.72 ? 100 GLY A N 1 ATOM 368 C CA . GLY A 1 48 ? 13.809 -19.507 3.710 1.00 16.08 ? 100 GLY A CA 1 ATOM 369 C C . GLY A 1 48 ? 13.961 -20.821 4.430 1.00 21.92 ? 100 GLY A C 1 ATOM 370 O O . GLY A 1 48 ? 14.644 -20.920 5.449 1.00 21.62 ? 100 GLY A O 1 ATOM 371 N N . SER A 1 49 ? 13.324 -21.837 3.877 1.00 17.64 ? 101 SER A N 1 ATOM 372 C CA . SER A 1 49 ? 13.333 -23.159 4.492 1.00 16.66 ? 101 SER A CA 1 ATOM 373 C C . SER A 1 49 ? 13.414 -24.212 3.449 1.00 18.28 ? 101 SER A C 1 ATOM 374 O O . SER A 1 49 ? 13.249 -23.940 2.272 1.00 16.61 ? 101 SER A O 1 ATOM 375 C CB . SER A 1 49 ? 12.100 -23.332 5.374 1.00 20.64 ? 101 SER A CB 1 ATOM 376 O OG . SER A 1 49 ? 10.915 -23.274 4.604 1.00 25.69 ? 101 SER A OG 1 ATOM 377 N N . PHE A 1 50 ? 13.669 -25.438 3.869 1.00 17.16 ? 102 PHE A N 1 ATOM 378 C CA . PHE A 1 50 ? 13.800 -26.556 2.939 1.00 16.56 ? 102 PHE A CA 1 ATOM 379 C C . PHE A 1 50 ? 13.066 -27.732 3.549 1.00 18.47 ? 102 PHE A C 1 ATOM 380 O O . PHE A 1 50 ? 13.478 -28.213 4.605 1.00 20.42 ? 102 PHE A O 1 ATOM 381 C CB . PHE A 1 50 ? 15.295 -26.870 2.751 1.00 17.92 ? 102 PHE A CB 1 ATOM 382 C CG . PHE A 1 50 ? 15.594 -27.581 1.451 1.00 19.42 ? 102 PHE A CG 1 ATOM 383 C CD1 . PHE A 1 50 ? 16.276 -26.934 0.435 1.00 21.16 ? 102 PHE A CD1 1 ATOM 384 C CD2 . PHE A 1 50 ? 15.107 -28.871 1.210 1.00 24.47 ? 102 PHE A CD2 1 ATOM 385 C CE1 . PHE A 1 50 ? 16.487 -27.561 -0.803 1.00 23.91 ? 102 PHE A CE1 1 ATOM 386 C CE2 . PHE A 1 50 ? 15.347 -29.507 -0.011 1.00 26.22 ? 102 PHE A CE2 1 ATOM 387 C CZ . PHE A 1 50 ? 16.014 -28.834 -1.019 1.00 23.73 ? 102 PHE A CZ 1 ATOM 388 N N . ASN A 1 51 ? 11.919 -28.115 2.969 1.00 15.39 ? 103 ASN A N 1 ATOM 389 C CA . ASN A 1 51 ? 11.048 -29.184 3.483 1.00 15.19 ? 103 ASN A CA 1 ATOM 390 C C . ASN A 1 51 ? 11.665 -30.543 3.383 1.00 18.95 ? 103 ASN A C 1 ATOM 391 O O . ASN A 1 51 ? 12.263 -30.876 2.362 1.00 17.60 ? 103 ASN A O 1 ATOM 392 C CB . ASN A 1 51 ? 9.693 -29.184 2.795 1.00 17.79 ? 103 ASN A CB 1 ATOM 393 C CG . ASN A 1 51 ? 8.878 -27.946 3.043 1.00 28.61 ? 103 ASN A CG 1 ATOM 394 O OD1 . ASN A 1 51 ? 8.748 -27.484 4.177 1.00 29.02 ? 103 ASN A OD1 1 ATOM 395 N ND2 . ASN A 1 51 ? 8.236 -27.449 1.990 1.00 21.45 ? 103 ASN A ND2 1 ATOM 396 N N . ASP A 1 52 ? 11.498 -31.346 4.455 1.00 17.22 ? 104 ASP A N 1 ATOM 397 C CA . ASP A 1 52 ? 12.009 -32.712 4.509 1.00 17.65 ? 104 ASP A CA 1 ATOM 398 C C . ASP A 1 52 ? 13.499 -32.755 4.208 1.00 18.96 ? 104 ASP A C 1 ATOM 399 O O . ASP A 1 52 ? 13.951 -33.578 3.429 1.00 18.92 ? 104 ASP A O 1 ATOM 400 C CB . ASP A 1 52 ? 11.173 -33.636 3.597 1.00 21.43 ? 104 ASP A CB 1 ATOM 401 C CG . ASP A 1 52 ? 9.749 -33.863 4.097 1.00 31.45 ? 104 ASP A CG 1 ATOM 402 O OD1 . ASP A 1 52 ? 9.493 -33.631 5.294 1.00 36.76 ? 104 ASP A OD1 1 ATOM 403 O OD2 . ASP A 1 52 ? 8.901 -34.271 3.292 1.00 43.93 ? 104 ASP A OD2 1 ATOM 404 N N . TYR A 1 53 ? 14.240 -31.823 4.802 1.00 17.72 ? 105 TYR A N 1 ATOM 405 C CA . TYR A 1 53 ? 15.673 -31.687 4.566 1.00 18.63 ? 105 TYR A CA 1 ATOM 406 C C . TYR A 1 53 ? 16.483 -32.882 5.056 1.00 21.45 ? 105 TYR A C 1 ATOM 407 O O . TYR A 1 53 ? 17.381 -33.338 4.339 1.00 20.20 ? 105 TYR A O 1 ATOM 408 C CB . TYR A 1 53 ? 16.157 -30.363 5.157 1.00 20.06 ? 105 TYR A CB 1 ATOM 409 C CG . TYR A 1 53 ? 17.536 -29.920 4.720 1.00 21.41 ? 105 TYR A CG 1 ATOM 410 C CD1 . TYR A 1 53 ? 17.887 -29.896 3.373 1.00 23.10 ? 105 TYR A CD1 1 ATOM 411 C CD2 . TYR A 1 53 ? 18.414 -29.343 5.625 1.00 23.79 ? 105 TYR A CD2 1 ATOM 412 C CE1 . TYR A 1 53 ? 19.134 -29.426 2.959 1.00 23.63 ? 105 TYR A CE1 1 ATOM 413 C CE2 . TYR A 1 53 ? 19.647 -28.840 5.221 1.00 25.92 ? 105 TYR A CE2 1 ATOM 414 C CZ . TYR A 1 53 ? 20.001 -28.884 3.883 1.00 29.44 ? 105 TYR A CZ 1 ATOM 415 O OH . TYR A 1 53 ? 21.191 -28.361 3.473 1.00 30.19 ? 105 TYR A OH 1 ATOM 416 N N . GLU A 1 54 ? 16.148 -33.421 6.247 1.00 20.59 ? 106 GLU A N 1 ATOM 417 C CA . GLU A 1 54 ? 16.849 -34.585 6.797 1.00 22.05 ? 106 GLU A CA 1 ATOM 418 C C . GLU A 1 54 ? 16.649 -35.786 5.906 1.00 24.06 ? 106 GLU A C 1 ATOM 419 O O . GLU A 1 54 ? 17.580 -36.550 5.685 1.00 23.74 ? 106 GLU A O 1 ATOM 420 C CB . GLU A 1 54 ? 16.368 -34.930 8.210 1.00 25.27 ? 106 GLU A CB 1 ATOM 421 C CG . GLU A 1 54 ? 16.847 -34.005 9.315 1.00 42.25 ? 106 GLU A CG 1 ATOM 422 C CD . GLU A 1 54 ? 16.747 -34.599 10.714 1.00 78.57 ? 106 GLU A CD 1 ATOM 423 O OE1 . GLU A 1 54 ? 15.910 -35.508 10.932 1.00 73.22 ? 106 GLU A OE1 1 ATOM 424 O OE2 . GLU A 1 54 ? 17.509 -34.147 11.599 1.00 81.67 ? 106 GLU A OE2 1 ATOM 425 N N . GLU A 1 55 ? 15.422 -35.958 5.389 1.00 20.59 ? 107 GLU A N 1 ATOM 426 C CA . GLU A 1 55 ? 15.084 -37.068 4.497 1.00 20.33 ? 107 GLU A CA 1 ATOM 427 C C . GLU A 1 55 ? 15.864 -36.972 3.190 1.00 22.34 ? 107 GLU A C 1 ATOM 428 O O . GLU A 1 55 ? 16.334 -37.998 2.685 1.00 21.82 ? 107 GLU A O 1 ATOM 429 C CB . GLU A 1 55 ? 13.571 -37.140 4.285 1.00 22.68 ? 107 GLU A CB 1 ATOM 430 C CG . GLU A 1 55 ? 12.807 -37.204 5.609 1.00 35.26 ? 107 GLU A CG 1 ATOM 431 C CD . GLU A 1 55 ? 12.290 -35.905 6.216 1.00 62.13 ? 107 GLU A CD 1 ATOM 432 O OE1 . GLU A 1 55 ? 13.106 -35.083 6.703 1.00 28.29 ? 107 GLU A OE1 1 ATOM 433 O OE2 . GLU A 1 55 ? 11.047 -35.760 6.292 1.00 63.77 ? 107 GLU A OE2 1 ATOM 434 N N . LEU A 1 56 ? 16.107 -35.728 2.693 1.00 19.06 ? 108 LEU A N 1 ATOM 435 C CA . LEU A 1 56 ? 16.935 -35.565 1.502 1.00 18.78 ? 108 LEU A CA 1 ATOM 436 C C . LEU A 1 56 ? 18.407 -35.962 1.811 1.00 20.06 ? 108 LEU A C 1 ATOM 437 O O . LEU A 1 56 ? 19.049 -36.654 1.008 1.00 20.20 ? 108 LEU A O 1 ATOM 438 C CB . LEU A 1 56 ? 16.821 -34.151 0.913 1.00 18.72 ? 108 LEU A CB 1 ATOM 439 C CG . LEU A 1 56 ? 17.744 -33.841 -0.280 1.00 21.71 ? 108 LEU A CG 1 ATOM 440 C CD1 . LEU A 1 56 ? 17.443 -34.758 -1.524 1.00 22.65 ? 108 LEU A CD1 1 ATOM 441 C CD2 . LEU A 1 56 ? 17.709 -32.380 -0.599 1.00 23.38 ? 108 LEU A CD2 1 ATOM 442 N N . LYS A 1 57 ? 18.925 -35.553 2.982 1.00 17.12 ? 109 LYS A N 1 ATOM 443 C CA . LYS A 1 57 ? 20.287 -35.917 3.395 1.00 16.64 ? 109 LYS A CA 1 ATOM 444 C C . LYS A 1 57 ? 20.434 -37.444 3.500 1.00 22.30 ? 109 LYS A C 1 ATOM 445 O O . LYS A 1 57 ? 21.451 -37.989 3.101 1.00 23.41 ? 109 LYS A O 1 ATOM 446 C CB . LYS A 1 57 ? 20.648 -35.235 4.712 1.00 19.94 ? 109 LYS A CB 1 ATOM 447 C CG . LYS A 1 57 ? 20.924 -33.753 4.565 1.00 29.48 ? 109 LYS A CG 1 ATOM 448 C CD . LYS A 1 57 ? 21.500 -33.228 5.862 1.00 29.89 ? 109 LYS A CD 1 ATOM 449 C CE . LYS A 1 57 ? 21.482 -31.732 5.911 1.00 44.06 ? 109 LYS A CE 1 ATOM 450 N NZ . LYS A 1 57 ? 22.254 -31.222 7.074 1.00 49.37 ? 109 LYS A NZ 1 ATOM 451 N N . HIS A 1 58 ? 19.389 -38.136 3.965 1.00 20.16 ? 110 HIS A N 1 ATOM 452 C CA . HIS A 1 58 ? 19.374 -39.589 4.054 1.00 23.13 ? 110 HIS A CA 1 ATOM 453 C C . HIS A 1 58 ? 19.387 -40.233 2.668 1.00 25.61 ? 110 HIS A C 1 ATOM 454 O O . HIS A 1 58 ? 20.074 -41.218 2.491 1.00 25.25 ? 110 HIS A O 1 ATOM 455 C CB . HIS A 1 58 ? 18.174 -40.076 4.880 1.00 25.80 ? 110 HIS A CB 1 ATOM 456 C CG . HIS A 1 58 ? 18.182 -41.558 5.143 1.00 31.40 ? 110 HIS A CG 1 ATOM 457 N ND1 . HIS A 1 58 ? 19.291 -42.192 5.687 1.00 34.49 ? 110 HIS A ND1 1 ATOM 458 C CD2 . HIS A 1 58 ? 17.199 -42.473 4.974 1.00 34.76 ? 110 HIS A CD2 1 ATOM 459 C CE1 . HIS A 1 58 ? 18.962 -43.469 5.792 1.00 34.29 ? 110 HIS A CE1 1 ATOM 460 N NE2 . HIS A 1 58 ? 17.709 -43.685 5.390 1.00 34.93 ? 110 HIS A NE2 1 ATOM 461 N N . LEU A 1 59 ? 18.647 -39.680 1.692 1.00 23.23 ? 111 LEU A N 1 ATOM 462 C CA . LEU A 1 59 ? 18.642 -40.187 0.313 1.00 24.25 ? 111 LEU A CA 1 ATOM 463 C C . LEU A 1 59 ? 20.040 -40.017 -0.284 1.00 25.94 ? 111 LEU A C 1 ATOM 464 O O . LEU A 1 59 ? 20.578 -40.980 -0.846 1.00 24.98 ? 111 LEU A O 1 ATOM 465 C CB . LEU A 1 59 ? 17.556 -39.484 -0.530 1.00 25.47 ? 111 LEU A CB 1 ATOM 466 C CG . LEU A 1 59 ? 17.714 -39.440 -2.080 1.00 31.70 ? 111 LEU A CG 1 ATOM 467 C CD1 . LEU A 1 59 ? 17.519 -40.839 -2.756 1.00 33.55 ? 111 LEU A CD1 1 ATOM 468 C CD2 . LEU A 1 59 ? 16.755 -38.441 -2.679 1.00 35.73 ? 111 LEU A CD2 1 ATOM 469 N N . LEU A 1 60 ? 20.681 -38.836 -0.049 1.00 22.76 ? 112 LEU A N 1 ATOM 470 C CA . LEU A 1 60 ? 22.032 -38.567 -0.576 1.00 22.46 ? 112 LEU A CA 1 ATOM 471 C C . LEU A 1 60 ? 23.100 -39.555 -0.064 1.00 24.89 ? 112 LEU A C 1 ATOM 472 O O . LEU A 1 60 ? 24.098 -39.803 -0.759 1.00 24.75 ? 112 LEU A O 1 ATOM 473 C CB . LEU A 1 60 ? 22.467 -37.136 -0.348 1.00 23.51 ? 112 LEU A CB 1 ATOM 474 C CG . LEU A 1 60 ? 21.724 -36.094 -1.141 1.00 30.06 ? 112 LEU A CG 1 ATOM 475 C CD1 . LEU A 1 60 ? 21.683 -34.811 -0.385 1.00 31.50 ? 112 LEU A CD1 1 ATOM 476 C CD2 . LEU A 1 60 ? 22.414 -35.832 -2.426 1.00 33.95 ? 112 LEU A CD2 1 ATOM 477 N N A SER A 1 61 ? 22.868 -40.154 1.116 0.50 22.77 ? 113 SER A N 1 ATOM 478 N N B SER A 1 61 ? 22.869 -40.151 1.120 0.50 21.24 ? 113 SER A N 1 ATOM 479 C CA A SER A 1 61 ? 23.760 -41.158 1.684 0.50 23.95 ? 113 SER A CA 1 ATOM 480 C CA B SER A 1 61 ? 23.777 -41.143 1.679 0.50 21.67 ? 113 SER A CA 1 ATOM 481 C C A SER A 1 61 ? 23.878 -42.400 0.789 0.50 27.52 ? 113 SER A C 1 ATOM 482 C C B SER A 1 61 ? 23.875 -42.407 0.801 0.50 26.55 ? 113 SER A C 1 ATOM 483 O O A SER A 1 61 ? 24.871 -43.120 0.873 0.50 28.47 ? 113 SER A O 1 ATOM 484 O O B SER A 1 61 ? 24.856 -43.140 0.898 0.50 27.62 ? 113 SER A O 1 ATOM 485 C CB A SER A 1 61 ? 23.310 -41.552 3.090 0.50 30.12 ? 113 SER A CB 1 ATOM 486 C CB B SER A 1 61 ? 23.416 -41.475 3.129 0.50 24.80 ? 113 SER A CB 1 ATOM 487 O OG A SER A 1 61 ? 23.553 -40.504 4.013 0.50 43.84 ? 113 SER A OG 1 ATOM 488 O OG B SER A 1 61 ? 22.307 -42.349 3.244 0.50 26.10 ? 113 SER A OG 1 ATOM 489 N N . SER A 1 62 ? 22.891 -42.613 -0.104 1.00 22.23 ? 114 SER A N 1 ATOM 490 C CA . SER A 1 62 ? 22.813 -43.761 -1.004 1.00 22.41 ? 114 SER A CA 1 ATOM 491 C C . SER A 1 62 ? 23.108 -43.380 -2.476 1.00 24.36 ? 114 SER A C 1 ATOM 492 O O . SER A 1 62 ? 23.040 -44.243 -3.353 1.00 26.40 ? 114 SER A O 1 ATOM 493 C CB . SER A 1 62 ? 21.435 -44.419 -0.885 1.00 28.94 ? 114 SER A CB 1 ATOM 494 O OG . SER A 1 62 ? 20.398 -43.588 -1.389 1.00 35.56 ? 114 SER A OG 1 ATOM 495 N N . VAL A 1 63 ? 23.412 -42.100 -2.728 1.00 18.37 ? 115 VAL A N 1 ATOM 496 C CA . VAL A 1 63 ? 23.747 -41.570 -4.056 1.00 15.62 ? 115 VAL A CA 1 ATOM 497 C C . VAL A 1 63 ? 25.253 -41.323 -4.094 1.00 20.01 ? 115 VAL A C 1 ATOM 498 O O . VAL A 1 63 ? 25.794 -40.781 -3.131 1.00 19.96 ? 115 VAL A O 1 ATOM 499 C CB . VAL A 1 63 ? 22.994 -40.254 -4.399 1.00 19.65 ? 115 VAL A CB 1 ATOM 500 C CG1 . VAL A 1 63 ? 23.377 -39.731 -5.781 1.00 19.45 ? 115 VAL A CG1 1 ATOM 501 C CG2 . VAL A 1 63 ? 21.480 -40.428 -4.288 1.00 19.89 ? 115 VAL A CG2 1 ATOM 502 N N . LYS A 1 64 ? 25.907 -41.674 -5.225 1.00 15.79 ? 116 LYS A N 1 ATOM 503 C CA . LYS A 1 64 ? 27.350 -41.469 -5.350 1.00 16.23 ? 116 LYS A CA 1 ATOM 504 C C . LYS A 1 64 ? 27.693 -40.599 -6.546 1.00 18.87 ? 116 LYS A C 1 ATOM 505 O O . LYS A 1 64 ? 28.864 -40.271 -6.748 1.00 18.71 ? 116 LYS A O 1 ATOM 506 C CB . LYS A 1 64 ? 28.096 -42.808 -5.371 1.00 17.32 ? 116 LYS A CB 1 ATOM 507 C CG . LYS A 1 64 ? 28.020 -43.584 -4.060 1.00 18.65 ? 116 LYS A CG 1 ATOM 508 C CD . LYS A 1 64 ? 28.616 -42.808 -2.888 1.00 19.41 ? 116 LYS A CD 1 ATOM 509 C CE . LYS A 1 64 ? 28.241 -43.455 -1.590 1.00 22.77 ? 116 LYS A CE 1 ATOM 510 N NZ . LYS A 1 64 ? 26.948 -42.962 -1.028 1.00 25.27 ? 116 LYS A NZ 1 ATOM 511 N N . HIS A 1 65 A 26.673 -40.212 -7.341 1.00 16.81 ? 116 HIS A N 1 ATOM 512 C CA . HIS A 1 65 A 26.879 -39.321 -8.464 1.00 16.87 ? 116 HIS A CA 1 ATOM 513 C C . HIS A 1 65 A 25.556 -38.854 -9.033 1.00 22.71 ? 116 HIS A C 1 ATOM 514 O O . HIS A 1 65 A 24.577 -39.607 -9.047 1.00 20.31 ? 116 HIS A O 1 ATOM 515 C CB . HIS A 1 65 A 27.771 -39.957 -9.539 1.00 19.47 ? 116 HIS A CB 1 ATOM 516 C CG . HIS A 1 65 A 28.290 -38.988 -10.549 1.00 22.66 ? 116 HIS A CG 1 ATOM 517 N ND1 . HIS A 1 65 A 28.219 -39.266 -11.893 1.00 25.35 ? 116 HIS A ND1 1 ATOM 518 C CD2 . HIS A 1 65 A 28.829 -37.756 -10.380 1.00 24.70 ? 116 HIS A CD2 1 ATOM 519 C CE1 . HIS A 1 65 A 28.752 -38.217 -12.507 1.00 25.12 ? 116 HIS A CE1 1 ATOM 520 N NE2 . HIS A 1 65 A 29.144 -37.286 -11.642 1.00 25.03 ? 116 HIS A NE2 1 ATOM 521 N N . PHE A 1 66 B 25.548 -37.594 -9.487 1.00 18.34 ? 116 PHE A N 1 ATOM 522 C CA . PHE A 1 66 B 24.436 -36.942 -10.133 1.00 17.48 ? 116 PHE A CA 1 ATOM 523 C C . PHE A 1 66 B 24.895 -36.472 -11.502 1.00 25.45 ? 116 PHE A C 1 ATOM 524 O O . PHE A 1 66 B 26.083 -36.142 -11.689 1.00 24.80 ? 116 PHE A O 1 ATOM 525 C CB . PHE A 1 66 B 23.987 -35.670 -9.365 1.00 19.08 ? 116 PHE A CB 1 ATOM 526 C CG . PHE A 1 66 B 23.201 -35.865 -8.097 1.00 20.31 ? 116 PHE A CG 1 ATOM 527 C CD1 . PHE A 1 66 B 22.052 -36.650 -8.085 1.00 21.84 ? 116 PHE A CD1 1 ATOM 528 C CD2 . PHE A 1 66 B 23.554 -35.196 -6.939 1.00 23.84 ? 116 PHE A CD2 1 ATOM 529 C CE1 . PHE A 1 66 B 21.282 -36.779 -6.926 1.00 24.33 ? 116 PHE A CE1 1 ATOM 530 C CE2 . PHE A 1 66 B 22.780 -35.320 -5.777 1.00 26.07 ? 116 PHE A CE2 1 ATOM 531 C CZ . PHE A 1 66 B 21.649 -36.108 -5.780 1.00 24.35 ? 116 PHE A CZ 1 ATOM 532 N N . GLU A 1 67 C 23.963 -36.443 -12.461 1.00 21.31 ? 116 GLU A N 1 ATOM 533 C CA . GLU A 1 67 C 24.170 -35.801 -13.764 1.00 21.34 ? 116 GLU A CA 1 ATOM 534 C C . GLU A 1 67 C 23.086 -34.705 -13.836 1.00 21.57 ? 116 GLU A C 1 ATOM 535 O O . GLU A 1 67 C 21.924 -35.030 -13.692 1.00 19.18 ? 116 GLU A O 1 ATOM 536 C CB . GLU A 1 67 C 24.001 -36.778 -14.939 1.00 23.73 ? 116 GLU A CB 1 ATOM 537 C CG . GLU A 1 67 C 25.179 -37.731 -15.101 1.00 40.90 ? 116 GLU A CG 1 ATOM 538 C CD . GLU A 1 67 C 24.989 -38.887 -16.069 1.00 68.92 ? 116 GLU A CD 1 ATOM 539 O OE1 . GLU A 1 67 C 24.126 -38.786 -16.973 1.00 55.51 ? 116 GLU A OE1 1 ATOM 540 O OE2 . GLU A 1 67 C 25.729 -39.889 -15.938 1.00 71.68 ? 116 GLU A OE2 1 ATOM 541 N N . LYS A 1 68 ? 23.458 -33.409 -13.922 1.00 21.20 ? 117 LYS A N 1 ATOM 542 C CA . LYS A 1 68 ? 22.442 -32.339 -14.017 1.00 20.53 ? 117 LYS A CA 1 ATOM 543 C C . LYS A 1 68 ? 21.778 -32.371 -15.402 1.00 23.97 ? 117 LYS A C 1 ATOM 544 O O . LYS A 1 68 ? 22.473 -32.358 -16.428 1.00 26.87 ? 117 LYS A O 1 ATOM 545 C CB . LYS A 1 68 ? 23.074 -30.956 -13.777 1.00 24.06 ? 117 LYS A CB 1 ATOM 546 C CG . LYS A 1 68 ? 23.476 -30.714 -12.347 1.00 32.26 ? 117 LYS A CG 1 ATOM 547 C CD . LYS A 1 68 ? 24.273 -29.439 -12.209 1.00 38.27 ? 117 LYS A CD 1 ATOM 548 C CE . LYS A 1 68 ? 23.500 -28.189 -12.502 1.00 33.18 ? 117 LYS A CE 1 ATOM 549 N NZ . LYS A 1 68 ? 24.296 -27.008 -12.088 1.00 44.36 ? 117 LYS A NZ 1 ATOM 550 N N . VAL A 1 69 ? 20.460 -32.448 -15.435 1.00 19.93 ? 118 VAL A N 1 ATOM 551 C CA . VAL A 1 69 ? 19.678 -32.543 -16.677 1.00 19.49 ? 118 VAL A CA 1 ATOM 552 C C . VAL A 1 69 ? 18.882 -31.239 -16.762 1.00 23.48 ? 118 VAL A C 1 ATOM 553 O O . VAL A 1 69 ? 18.243 -30.883 -15.777 1.00 22.13 ? 118 VAL A O 1 ATOM 554 C CB . VAL A 1 69 ? 18.731 -33.781 -16.663 1.00 22.81 ? 118 VAL A CB 1 ATOM 555 C CG1 . VAL A 1 69 ? 17.734 -33.761 -17.829 1.00 22.95 ? 118 VAL A CG1 1 ATOM 556 C CG2 . VAL A 1 69 ? 19.512 -35.095 -16.626 1.00 22.80 ? 118 VAL A CG2 1 ATOM 557 N N . LYS A 1 70 ? 18.928 -30.535 -17.920 1.00 20.32 ? 119 LYS A N 1 ATOM 558 C CA . LYS A 1 70 ? 18.179 -29.281 -18.120 1.00 18.70 ? 119 LYS A CA 1 ATOM 559 C C . LYS A 1 70 ? 16.696 -29.587 -18.383 1.00 22.24 ? 119 LYS A C 1 ATOM 560 O O . LYS A 1 70 ? 16.225 -29.568 -19.519 1.00 23.39 ? 119 LYS A O 1 ATOM 561 C CB . LYS A 1 70 ? 18.793 -28.440 -19.267 1.00 18.39 ? 119 LYS A CB 1 ATOM 562 C CG . LYS A 1 70 ? 18.297 -26.988 -19.284 1.00 29.28 ? 119 LYS A CG 1 ATOM 563 C CD . LYS A 1 70 ? 18.995 -26.188 -20.397 1.00 31.60 ? 119 LYS A CD 1 ATOM 564 C CE . LYS A 1 70 ? 20.335 -25.643 -19.946 1.00 44.37 ? 119 LYS A CE 1 ATOM 565 N NZ . LYS A 1 70 ? 21.125 -25.078 -21.076 1.00 52.79 ? 119 LYS A NZ 1 ATOM 566 N N . ILE A 1 71 ? 15.955 -29.825 -17.318 1.00 17.28 ? 120 ILE A N 1 ATOM 567 C CA . ILE A 1 71 ? 14.548 -30.218 -17.436 1.00 16.06 ? 120 ILE A CA 1 ATOM 568 C C . ILE A 1 71 ? 13.574 -29.143 -17.942 1.00 21.07 ? 120 ILE A C 1 ATOM 569 O O . ILE A 1 71 ? 12.551 -29.476 -18.539 1.00 21.34 ? 120 ILE A O 1 ATOM 570 C CB . ILE A 1 71 ? 14.072 -30.901 -16.132 1.00 17.42 ? 120 ILE A CB 1 ATOM 571 C CG1 . ILE A 1 71 ? 13.981 -29.910 -14.967 1.00 17.54 ? 120 ILE A CG1 1 ATOM 572 C CG2 . ILE A 1 71 ? 14.921 -32.144 -15.806 1.00 18.89 ? 120 ILE A CG2 1 ATOM 573 C CD1 . ILE A 1 71 ? 13.393 -30.507 -13.694 1.00 20.68 ? 120 ILE A CD1 1 ATOM 574 N N . LEU A 1 72 ? 13.848 -27.862 -17.632 1.00 18.29 ? 121 LEU A N 1 ATOM 575 C CA . LEU A 1 72 ? 12.974 -26.738 -17.947 1.00 18.11 ? 121 LEU A CA 1 ATOM 576 C C . LEU A 1 72 ? 13.854 -25.557 -18.347 1.00 20.55 ? 121 LEU A C 1 ATOM 577 O O . LEU A 1 72 ? 14.149 -24.716 -17.508 1.00 19.20 ? 121 LEU A O 1 ATOM 578 C CB . LEU A 1 72 ? 12.070 -26.380 -16.747 1.00 17.79 ? 121 LEU A CB 1 ATOM 579 C CG . LEU A 1 72 ? 11.039 -27.419 -16.268 1.00 21.67 ? 121 LEU A CG 1 ATOM 580 C CD1 . LEU A 1 72 ? 10.441 -26.990 -14.903 1.00 20.36 ? 121 LEU A CD1 1 ATOM 581 C CD2 . LEU A 1 72 ? 9.929 -27.597 -17.308 1.00 22.45 ? 121 LEU A CD2 1 ATOM 582 N N . PRO A 1 73 ? 14.346 -25.552 -19.605 1.00 18.91 ? 122 PRO A N 1 ATOM 583 C CA . PRO A 1 73 ? 15.187 -24.426 -20.084 1.00 19.56 ? 122 PRO A CA 1 ATOM 584 C C . PRO A 1 73 ? 14.497 -23.081 -19.826 1.00 23.88 ? 122 PRO A C 1 ATOM 585 O O . PRO A 1 73 ? 13.313 -22.941 -20.098 1.00 23.00 ? 122 PRO A O 1 ATOM 586 C CB . PRO A 1 73 ? 15.278 -24.685 -21.593 1.00 22.22 ? 122 PRO A CB 1 ATOM 587 C CG . PRO A 1 73 ? 15.042 -26.160 -21.756 1.00 26.88 ? 122 PRO A CG 1 ATOM 588 C CD . PRO A 1 73 ? 14.030 -26.494 -20.701 1.00 22.63 ? 122 PRO A CD 1 ATOM 589 N N . LYS A 1 74 ? 15.227 -22.114 -19.267 1.00 22.21 ? 123 LYS A N 1 ATOM 590 C CA . LYS A 1 74 ? 14.729 -20.786 -18.881 1.00 23.64 ? 123 LYS A CA 1 ATOM 591 C C . LYS A 1 74 ? 13.947 -20.066 -20.002 1.00 26.32 ? 123 LYS A C 1 ATOM 592 O O . LYS A 1 74 ? 12.914 -19.434 -19.742 1.00 26.30 ? 123 LYS A O 1 ATOM 593 C CB . LYS A 1 74 ? 15.929 -19.942 -18.413 1.00 29.12 ? 123 LYS A CB 1 ATOM 594 C CG . LYS A 1 74 ? 15.657 -18.936 -17.330 1.00 43.91 ? 123 LYS A CG 1 ATOM 595 C CD . LYS A 1 74 ? 16.878 -18.076 -17.085 1.00 48.82 ? 123 LYS A CD 1 ATOM 596 C CE . LYS A 1 74 ? 17.596 -18.440 -15.806 1.00 65.46 ? 123 LYS A CE 1 ATOM 597 N NZ . LYS A 1 74 ? 18.589 -17.398 -15.418 1.00 73.79 ? 123 LYS A NZ 1 ATOM 598 N N . ASP A 1 75 ? 14.391 -20.233 -21.256 1.00 23.20 ? 125 ASP A N 1 ATOM 599 C CA . ASP A 1 75 ? 13.771 -19.612 -22.426 1.00 23.48 ? 125 ASP A CA 1 ATOM 600 C C . ASP A 1 75 ? 12.331 -20.050 -22.678 1.00 27.53 ? 125 ASP A C 1 ATOM 601 O O . ASP A 1 75 ? 11.581 -19.348 -23.377 1.00 27.53 ? 125 ASP A O 1 ATOM 602 C CB . ASP A 1 75 ? 14.628 -19.866 -23.669 1.00 25.10 ? 125 ASP A CB 1 ATOM 603 C CG . ASP A 1 75 ? 14.597 -21.320 -24.139 1.00 35.69 ? 125 ASP A CG 1 ATOM 604 O OD1 . ASP A 1 75 ? 15.356 -22.134 -23.586 1.00 36.38 ? 125 ASP A OD1 1 ATOM 605 O OD2 . ASP A 1 75 ? 13.810 -21.633 -25.068 1.00 36.06 ? 125 ASP A OD2 1 ATOM 606 N N . ARG A 1 76 ? 11.927 -21.206 -22.094 1.00 23.53 ? 126 ARG A N 1 ATOM 607 C CA . ARG A 1 76 ? 10.585 -21.740 -22.305 1.00 24.42 ? 126 ARG A CA 1 ATOM 608 C C . ARG A 1 76 ? 9.522 -20.846 -21.697 1.00 26.33 ? 126 ARG A C 1 ATOM 609 O O . ARG A 1 76 ? 8.383 -20.864 -22.147 1.00 24.19 ? 126 ARG A O 1 ATOM 610 C CB . ARG A 1 76 ? 10.458 -23.173 -21.765 1.00 27.18 ? 126 ARG A CB 1 ATOM 611 C CG . ARG A 1 76 ? 11.097 -24.209 -22.684 1.00 47.07 ? 126 ARG A CG 1 ATOM 612 C CD . ARG A 1 76 ? 10.708 -25.638 -22.338 1.00 68.33 ? 126 ARG A CD 1 ATOM 613 N NE . ARG A 1 76 ? 11.000 -26.558 -23.441 1.00 78.85 ? 126 ARG A NE 1 ATOM 614 C CZ . ARG A 1 76 ? 10.105 -26.978 -24.333 1.00 94.58 ? 126 ARG A CZ 1 ATOM 615 N NH1 . ARG A 1 76 ? 8.843 -26.572 -24.260 1.00 79.16 ? 126 ARG A NH1 1 ATOM 616 N NH2 . ARG A 1 76 ? 10.465 -27.810 -25.301 1.00 85.92 ? 126 ARG A NH2 1 ATOM 617 N N . TRP A 1 77 ? 9.895 -20.047 -20.676 1.00 23.81 ? 127 TRP A N 1 ATOM 618 C CA . TRP A 1 77 ? 8.940 -19.184 -19.978 1.00 23.73 ? 127 TRP A CA 1 ATOM 619 C C . TRP A 1 77 ? 8.762 -17.872 -20.766 1.00 28.59 ? 127 TRP A C 1 ATOM 620 O O . TRP A 1 77 ? 9.124 -16.787 -20.307 1.00 27.44 ? 127 TRP A O 1 ATOM 621 C CB . TRP A 1 77 ? 9.407 -18.936 -18.530 1.00 20.34 ? 127 TRP A CB 1 ATOM 622 C CG . TRP A 1 77 ? 9.696 -20.177 -17.734 1.00 20.15 ? 127 TRP A CG 1 ATOM 623 C CD1 . TRP A 1 77 ? 10.912 -20.586 -17.276 1.00 21.96 ? 127 TRP A CD1 1 ATOM 624 C CD2 . TRP A 1 77 ? 8.747 -21.123 -17.251 1.00 20.20 ? 127 TRP A CD2 1 ATOM 625 N NE1 . TRP A 1 77 ? 10.775 -21.726 -16.523 1.00 21.41 ? 127 TRP A NE1 1 ATOM 626 C CE2 . TRP A 1 77 ? 9.456 -22.085 -16.498 1.00 23.04 ? 127 TRP A CE2 1 ATOM 627 C CE3 . TRP A 1 77 ? 7.351 -21.243 -17.356 1.00 22.67 ? 127 TRP A CE3 1 ATOM 628 C CZ2 . TRP A 1 77 ? 8.826 -23.168 -15.873 1.00 23.52 ? 127 TRP A CZ2 1 ATOM 629 C CZ3 . TRP A 1 77 ? 6.723 -22.309 -16.728 1.00 24.29 ? 127 TRP A CZ3 1 ATOM 630 C CH2 . TRP A 1 77 ? 7.452 -23.253 -15.994 1.00 24.86 ? 127 TRP A CH2 1 ATOM 631 N N . THR A 1 78 ? 8.174 -17.981 -21.964 1.00 27.09 ? 128 THR A N 1 ATOM 632 C CA . THR A 1 78 ? 8.046 -16.826 -22.863 1.00 26.86 ? 128 THR A CA 1 ATOM 633 C C . THR A 1 78 ? 7.094 -15.722 -22.415 1.00 30.39 ? 128 THR A C 1 ATOM 634 O O . THR A 1 78 ? 7.227 -14.590 -22.888 1.00 30.82 ? 128 THR A O 1 ATOM 635 C CB . THR A 1 78 ? 7.716 -17.278 -24.299 1.00 33.22 ? 128 THR A CB 1 ATOM 636 O OG1 . THR A 1 78 ? 6.405 -17.829 -24.307 1.00 33.28 ? 128 THR A OG1 1 ATOM 637 C CG2 . THR A 1 78 ? 8.718 -18.275 -24.844 1.00 34.21 ? 128 THR A CG2 1 ATOM 638 N N . GLN A 1 79 ? 6.141 -16.030 -21.527 1.00 25.23 ? 129 GLN A N 1 ATOM 639 C CA . GLN A 1 79 ? 5.177 -15.024 -21.075 1.00 25.86 ? 129 GLN A CA 1 ATOM 640 C C . GLN A 1 79 ? 5.565 -14.420 -19.710 1.00 26.73 ? 129 GLN A C 1 ATOM 641 O O . GLN A 1 79 ? 4.844 -13.581 -19.200 1.00 25.45 ? 129 GLN A O 1 ATOM 642 C CB . GLN A 1 79 ? 3.775 -15.631 -20.984 1.00 27.84 ? 129 GLN A CB 1 ATOM 643 C CG . GLN A 1 79 ? 3.136 -16.038 -22.309 1.00 41.72 ? 129 GLN A CG 1 ATOM 644 C CD . GLN A 1 79 ? 1.781 -16.654 -22.053 1.00 62.45 ? 129 GLN A CD 1 ATOM 645 O OE1 . GLN A 1 79 ? 1.671 -17.823 -21.662 1.00 55.82 ? 129 GLN A OE1 1 ATOM 646 N NE2 . GLN A 1 79 ? 0.721 -15.862 -22.218 1.00 56.69 ? 129 GLN A NE2 1 ATOM 647 N N . HIS A 1 80 ? 6.699 -14.836 -19.135 1.00 20.49 ? 130 HIS A N 1 ATOM 648 C CA . HIS A 1 80 ? 7.141 -14.369 -17.821 1.00 18.30 ? 130 HIS A CA 1 ATOM 649 C C . HIS A 1 80 ? 8.569 -13.811 -17.885 1.00 22.55 ? 130 HIS A C 1 ATOM 650 O O . HIS A 1 80 ? 9.333 -14.147 -18.781 1.00 22.36 ? 130 HIS A O 1 ATOM 651 C CB . HIS A 1 80 ? 7.122 -15.559 -16.836 1.00 17.55 ? 130 HIS A CB 1 ATOM 652 C CG . HIS A 1 80 ? 5.741 -16.074 -16.608 1.00 21.37 ? 130 HIS A CG 1 ATOM 653 N ND1 . HIS A 1 80 ? 5.141 -16.941 -17.504 1.00 22.88 ? 130 HIS A ND1 1 ATOM 654 C CD2 . HIS A 1 80 ? 4.843 -15.741 -15.649 1.00 22.66 ? 130 HIS A CD2 1 ATOM 655 C CE1 . HIS A 1 80 ? 3.911 -17.143 -17.049 1.00 22.47 ? 130 HIS A CE1 1 ATOM 656 N NE2 . HIS A 1 80 ? 3.683 -16.441 -15.934 1.00 22.10 ? 130 HIS A NE2 1 ATOM 657 N N . THR A 1 81 ? 8.916 -12.975 -16.908 1.00 17.76 ? 131 THR A N 1 ATOM 658 C CA . THR A 1 81 ? 10.263 -12.467 -16.725 1.00 17.57 ? 131 THR A CA 1 ATOM 659 C C . THR A 1 81 ? 11.016 -13.539 -15.945 1.00 19.45 ? 131 THR A C 1 ATOM 660 O O . THR A 1 81 ? 10.476 -14.133 -15.021 1.00 18.79 ? 131 THR A O 1 ATOM 661 C CB . THR A 1 81 ? 10.239 -11.105 -16.026 1.00 18.88 ? 131 THR A CB 1 ATOM 662 O OG1 . THR A 1 81 ? 9.503 -10.190 -16.838 1.00 22.27 ? 131 THR A OG1 1 ATOM 663 C CG2 . THR A 1 81 ? 11.645 -10.536 -15.776 1.00 18.77 ? 131 THR A CG2 1 ATOM 664 N N . THR A 1 82 ? 12.239 -13.838 -16.344 1.00 17.46 ? 132 THR A N 1 ATOM 665 C CA . THR A 1 82 ? 13.027 -14.884 -15.712 1.00 16.62 ? 132 THR A CA 1 ATOM 666 C C . THR A 1 82 ? 14.383 -14.365 -15.201 1.00 21.49 ? 132 THR A C 1 ATOM 667 O O . THR A 1 82 ? 15.164 -15.156 -14.711 1.00 21.89 ? 132 THR A O 1 ATOM 668 C CB . THR A 1 82 ? 13.320 -15.993 -16.742 1.00 24.71 ? 132 THR A CB 1 ATOM 669 O OG1 . THR A 1 82 ? 14.067 -15.426 -17.825 1.00 26.45 ? 132 THR A OG1 1 ATOM 670 C CG2 . THR A 1 82 ? 12.066 -16.676 -17.261 1.00 24.41 ? 132 THR A CG2 1 ATOM 671 N N . THR A 1 83 ? 14.658 -13.073 -15.366 1.00 22.04 ? 133 THR A N 1 ATOM 672 C CA . THR A 1 83 ? 15.936 -12.432 -15.003 1.00 22.16 ? 133 THR A CA 1 ATOM 673 C C . THR A 1 83 ? 16.044 -12.061 -13.519 1.00 27.58 ? 133 THR A C 1 ATOM 674 O O . THR A 1 83 ? 17.114 -11.622 -13.080 1.00 27.89 ? 133 THR A O 1 ATOM 675 C CB . THR A 1 83 ? 16.105 -11.158 -15.832 1.00 26.91 ? 133 THR A CB 1 ATOM 676 O OG1 . THR A 1 83 ? 14.972 -10.303 -15.593 1.00 28.56 ? 133 THR A OG1 1 ATOM 677 C CG2 . THR A 1 83 ? 16.257 -11.441 -17.310 1.00 31.86 ? 133 THR A CG2 1 ATOM 678 N N . GLY A 1 84 ? 14.949 -12.252 -12.775 1.00 22.42 ? 134 GLY A N 1 ATOM 679 C CA . GLY A 1 84 ? 14.829 -11.907 -11.359 1.00 21.34 ? 134 GLY A CA 1 ATOM 680 C C . GLY A 1 84 ? 16.002 -12.339 -10.511 1.00 23.65 ? 134 GLY A C 1 ATOM 681 O O . GLY A 1 84 ? 16.401 -13.502 -10.540 1.00 20.14 ? 134 GLY A O 1 ATOM 682 N N . GLY A 1 85 ? 16.555 -11.376 -9.787 1.00 20.50 ? 135 GLY A N 1 ATOM 683 C CA . GLY A 1 85 ? 17.680 -11.598 -8.898 1.00 22.05 ? 135 GLY A CA 1 ATOM 684 C C . GLY A 1 85 ? 17.561 -10.744 -7.654 1.00 26.19 ? 135 GLY A C 1 ATOM 685 O O . GLY A 1 85 ? 16.787 -9.780 -7.611 1.00 26.96 ? 135 GLY A O 1 ATOM 686 N N . SER A 1 86 ? 18.345 -11.067 -6.639 1.00 21.32 ? 136 SER A N 1 ATOM 687 C CA . SER A 1 86 ? 18.279 -10.282 -5.419 1.00 21.12 ? 136 SER A CA 1 ATOM 688 C C . SER A 1 86 ? 19.670 -9.942 -4.955 1.00 22.45 ? 136 SER A C 1 ATOM 689 O O . SER A 1 86 ? 20.637 -10.647 -5.308 1.00 19.84 ? 136 SER A O 1 ATOM 690 C CB . SER A 1 86 ? 17.512 -11.067 -4.342 1.00 23.17 ? 136 SER A CB 1 ATOM 691 O OG . SER A 1 86 ? 17.544 -10.449 -3.063 1.00 23.90 ? 136 SER A OG 1 ATOM 692 N N . ARG A 1 87 ? 19.787 -8.879 -4.129 1.00 21.42 ? 137 ARG A N 1 ATOM 693 C CA . ARG A 1 87 ? 21.088 -8.518 -3.562 1.00 20.81 ? 137 ARG A CA 1 ATOM 694 C C . ARG A 1 87 ? 21.488 -9.613 -2.530 1.00 25.75 ? 137 ARG A C 1 ATOM 695 O O . ARG A 1 87 ? 22.677 -9.757 -2.228 1.00 28.44 ? 137 ARG A O 1 ATOM 696 C CB . ARG A 1 87 ? 21.064 -7.124 -2.908 1.00 24.29 ? 137 ARG A CB 1 ATOM 697 C CG . ARG A 1 87 ? 20.699 -6.001 -3.865 1.00 46.85 ? 137 ARG A CG 1 ATOM 698 C CD . ARG A 1 87 ? 21.479 -4.735 -3.584 1.00 65.04 ? 137 ARG A CD 1 ATOM 699 N NE . ARG A 1 87 ? 22.776 -4.739 -4.261 1.00 79.98 ? 137 ARG A NE 1 ATOM 700 C CZ . ARG A 1 87 ? 22.987 -4.272 -5.488 1.00 95.93 ? 137 ARG A CZ 1 ATOM 701 N NH1 . ARG A 1 87 ? 21.986 -3.755 -6.193 1.00 82.54 ? 137 ARG A NH1 1 ATOM 702 N NH2 . ARG A 1 87 ? 24.199 -4.319 -6.021 1.00 83.47 ? 137 ARG A NH2 1 ATOM 703 N N . ALA A 1 88 ? 20.498 -10.427 -2.042 1.00 22.01 ? 138 ALA A N 1 ATOM 704 C CA . ALA A 1 88 ? 20.726 -11.546 -1.120 1.00 21.22 ? 138 ALA A CA 1 ATOM 705 C C . ALA A 1 88 ? 21.615 -12.616 -1.791 1.00 28.74 ? 138 ALA A C 1 ATOM 706 O O . ALA A 1 88 ? 22.290 -13.368 -1.096 1.00 30.87 ? 138 ALA A O 1 ATOM 707 C CB . ALA A 1 88 ? 19.402 -12.175 -0.737 1.00 20.72 ? 138 ALA A CB 1 ATOM 708 N N . CYS A 1 89 ? 21.574 -12.710 -3.132 1.00 27.51 ? 139 CYS A N 1 ATOM 709 C CA . CYS A 1 89 ? 22.347 -13.697 -3.893 1.00 27.42 ? 139 CYS A CA 1 ATOM 710 C C . CYS A 1 89 ? 23.311 -12.951 -4.849 1.00 29.35 ? 139 CYS A C 1 ATOM 711 O O . CYS A 1 89 ? 23.542 -13.446 -5.947 1.00 26.64 ? 139 CYS A O 1 ATOM 712 C CB . CYS A 1 89 ? 21.426 -14.642 -4.668 1.00 29.06 ? 139 CYS A CB 1 ATOM 713 S SG . CYS A 1 89 ? 20.196 -15.519 -3.654 1.00 33.76 ? 139 CYS A SG 1 ATOM 714 N N . ALA A 1 90 ? 23.836 -11.763 -4.437 1.00 28.38 ? 140 ALA A N 1 ATOM 715 C CA . ALA A 1 90 ? 24.682 -10.911 -5.271 1.00 29.04 ? 140 ALA A CA 1 ATOM 716 C C . ALA A 1 90 ? 26.013 -11.530 -5.688 1.00 32.09 ? 140 ALA A C 1 ATOM 717 O O . ALA A 1 90 ? 26.653 -12.225 -4.899 1.00 32.22 ? 140 ALA A O 1 ATOM 718 C CB . ALA A 1 90 ? 24.920 -9.548 -4.617 1.00 31.23 ? 140 ALA A CB 1 ATOM 719 N N . VAL A 1 91 ? 26.411 -11.282 -6.952 1.00 28.18 ? 141 VAL A N 1 ATOM 720 C CA . VAL A 1 91 ? 27.678 -11.755 -7.523 1.00 27.48 ? 141 VAL A CA 1 ATOM 721 C C . VAL A 1 91 ? 28.364 -10.524 -8.128 1.00 33.65 ? 141 VAL A C 1 ATOM 722 O O . VAL A 1 91 ? 27.754 -9.852 -8.959 1.00 31.26 ? 141 VAL A O 1 ATOM 723 C CB . VAL A 1 91 ? 27.498 -12.866 -8.599 1.00 30.67 ? 141 VAL A CB 1 ATOM 724 C CG1 . VAL A 1 91 ? 28.855 -13.287 -9.178 1.00 30.53 ? 141 VAL A CG1 1 ATOM 725 C CG2 . VAL A 1 91 ? 26.743 -14.088 -8.057 1.00 30.18 ? 141 VAL A CG2 1 ATOM 726 N N . SER A 1 92 ? 29.629 -10.241 -7.721 1.00 32.66 ? 142 SER A N 1 ATOM 727 C CA . SER A 1 92 ? 30.402 -9.099 -8.221 1.00 33.54 ? 142 SER A CA 1 ATOM 728 C C . SER A 1 92 ? 29.613 -7.777 -8.134 1.00 38.91 ? 142 SER A C 1 ATOM 729 O O . SER A 1 92 ? 29.584 -7.004 -9.094 1.00 38.06 ? 142 SER A O 1 ATOM 730 C CB . SER A 1 92 ? 30.911 -9.372 -9.637 1.00 39.40 ? 142 SER A CB 1 ATOM 731 O OG . SER A 1 92 ? 31.749 -10.518 -9.699 1.00 53.10 ? 142 SER A OG 1 ATOM 732 N N . GLY A 1 93 ? 28.932 -7.578 -6.995 1.00 35.47 ? 143 GLY A N 1 ATOM 733 C CA . GLY A 1 93 ? 28.144 -6.381 -6.701 1.00 35.97 ? 143 GLY A CA 1 ATOM 734 C C . GLY A 1 93 ? 26.848 -6.224 -7.471 1.00 38.26 ? 143 GLY A C 1 ATOM 735 O O . GLY A 1 93 ? 26.272 -5.139 -7.488 1.00 41.17 ? 143 GLY A O 1 ATOM 736 N N . ASN A 1 94 ? 26.376 -7.292 -8.106 1.00 31.15 ? 144 ASN A N 1 ATOM 737 C CA . ASN A 1 94 ? 25.183 -7.271 -8.931 1.00 29.04 ? 144 ASN A CA 1 ATOM 738 C C . ASN A 1 94 ? 24.170 -8.279 -8.388 1.00 28.30 ? 144 ASN A C 1 ATOM 739 O O . ASN A 1 94 ? 24.579 -9.338 -7.902 1.00 25.08 ? 144 ASN A O 1 ATOM 740 C CB . ASN A 1 94 ? 25.540 -7.617 -10.375 1.00 32.54 ? 144 ASN A CB 1 ATOM 741 C CG . ASN A 1 94 ? 26.457 -6.616 -11.045 1.00 56.26 ? 144 ASN A CG 1 ATOM 742 O OD1 . ASN A 1 94 ? 26.168 -5.414 -11.114 1.00 47.10 ? 144 ASN A OD1 1 ATOM 743 N ND2 . ASN A 1 94 ? 27.581 -7.096 -11.569 1.00 51.72 ? 144 ASN A ND2 1 ATOM 744 N N . PRO A 1 95 ? 22.855 -8.001 -8.489 1.00 24.67 ? 145 PRO A N 1 ATOM 745 C CA . PRO A 1 95 ? 21.878 -8.959 -7.964 1.00 21.00 ? 145 PRO A CA 1 ATOM 746 C C . PRO A 1 95 ? 21.874 -10.209 -8.806 1.00 24.38 ? 145 PRO A C 1 ATOM 747 O O . PRO A 1 95 ? 21.966 -10.143 -10.016 1.00 25.80 ? 145 PRO A O 1 ATOM 748 C CB . PRO A 1 95 ? 20.554 -8.210 -8.097 1.00 23.09 ? 145 PRO A CB 1 ATOM 749 C CG . PRO A 1 95 ? 20.961 -6.743 -8.187 1.00 29.22 ? 145 PRO A CG 1 ATOM 750 C CD . PRO A 1 95 ? 22.163 -6.823 -9.039 1.00 25.18 ? 145 PRO A CD 1 ATOM 751 N N . SER A 1 96 ? 21.784 -11.361 -8.165 1.00 21.00 ? 146 SER A N 1 ATOM 752 C CA . SER A 1 96 ? 21.787 -12.605 -8.919 1.00 18.74 ? 146 SER A CA 1 ATOM 753 C C . SER A 1 96 ? 20.829 -13.546 -8.220 1.00 18.38 ? 146 SER A C 1 ATOM 754 O O . SER A 1 96 ? 19.999 -13.122 -7.405 1.00 16.97 ? 146 SER A O 1 ATOM 755 C CB . SER A 1 96 ? 23.202 -13.187 -9.000 1.00 22.39 ? 146 SER A CB 1 ATOM 756 O OG . SER A 1 96 ? 23.352 -14.187 -9.999 1.00 28.47 ? 146 SER A OG 1 ATOM 757 N N . PHE A 1 97 ? 20.914 -14.828 -8.548 1.00 16.23 ? 147 PHE A N 1 ATOM 758 C CA . PHE A 1 97 ? 20.007 -15.811 -8.013 1.00 15.09 ? 147 PHE A CA 1 ATOM 759 C C . PHE A 1 97 ? 20.647 -17.158 -8.004 1.00 17.49 ? 147 PHE A C 1 ATOM 760 O O . PHE A 1 97 ? 21.691 -17.367 -8.638 1.00 17.92 ? 147 PHE A O 1 ATOM 761 C CB . PHE A 1 97 ? 18.708 -15.820 -8.869 1.00 17.13 ? 147 PHE A CB 1 ATOM 762 C CG . PHE A 1 97 ? 17.525 -16.406 -8.165 1.00 16.78 ? 147 PHE A CG 1 ATOM 763 C CD1 . PHE A 1 97 ? 17.055 -15.852 -6.972 1.00 17.50 ? 147 PHE A CD1 1 ATOM 764 C CD2 . PHE A 1 97 ? 16.844 -17.494 -8.705 1.00 16.49 ? 147 PHE A CD2 1 ATOM 765 C CE1 . PHE A 1 97 ? 15.978 -16.438 -6.282 1.00 16.73 ? 147 PHE A CE1 1 ATOM 766 C CE2 . PHE A 1 97 ? 15.760 -18.063 -8.028 1.00 18.18 ? 147 PHE A CE2 1 ATOM 767 C CZ . PHE A 1 97 ? 15.325 -17.517 -6.845 1.00 16.20 ? 147 PHE A CZ 1 ATOM 768 N N . PHE A 1 98 ? 19.976 -18.114 -7.363 1.00 16.05 ? 148 PHE A N 1 ATOM 769 C CA . PHE A 1 98 ? 20.418 -19.506 -7.334 1.00 16.47 ? 148 PHE A CA 1 ATOM 770 C C . PHE A 1 98 ? 20.662 -19.984 -8.760 1.00 17.54 ? 148 PHE A C 1 ATOM 771 O O . PHE A 1 98 ? 19.822 -19.745 -9.635 1.00 19.92 ? 148 PHE A O 1 ATOM 772 C CB . PHE A 1 98 ? 19.310 -20.363 -6.704 1.00 16.12 ? 148 PHE A CB 1 ATOM 773 C CG . PHE A 1 98 ? 19.017 -20.046 -5.255 1.00 16.50 ? 148 PHE A CG 1 ATOM 774 C CD1 . PHE A 1 98 ? 19.889 -20.441 -4.249 1.00 19.00 ? 148 PHE A CD1 1 ATOM 775 C CD2 . PHE A 1 98 ? 17.858 -19.378 -4.898 1.00 16.31 ? 148 PHE A CD2 1 ATOM 776 C CE1 . PHE A 1 98 ? 19.594 -20.180 -2.897 1.00 18.79 ? 148 PHE A CE1 1 ATOM 777 C CE2 . PHE A 1 98 ? 17.579 -19.091 -3.547 1.00 20.53 ? 148 PHE A CE2 1 ATOM 778 C CZ . PHE A 1 98 ? 18.427 -19.533 -2.558 1.00 18.95 ? 148 PHE A CZ 1 ATOM 779 N N . ARG A 1 99 ? 21.828 -20.590 -9.022 1.00 13.34 ? 149 ARG A N 1 ATOM 780 C CA . ARG A 1 99 ? 22.212 -20.969 -10.383 1.00 13.85 ? 149 ARG A CA 1 ATOM 781 C C . ARG A 1 99 ? 21.306 -21.975 -11.056 1.00 16.68 ? 149 ARG A C 1 ATOM 782 O O . ARG A 1 99 ? 21.210 -21.949 -12.273 1.00 19.26 ? 149 ARG A O 1 ATOM 783 C CB . ARG A 1 99 ? 23.656 -21.516 -10.459 1.00 15.31 ? 149 ARG A CB 1 ATOM 784 C CG . ARG A 1 99 ? 24.775 -20.653 -9.920 1.00 26.94 ? 149 ARG A CG 1 ATOM 785 C CD . ARG A 1 99 ? 24.802 -19.268 -10.472 1.00 34.48 ? 149 ARG A CD 1 ATOM 786 N NE . ARG A 1 99 ? 26.070 -18.607 -10.157 1.00 30.86 ? 149 ARG A NE 1 ATOM 787 C CZ . ARG A 1 99 ? 26.420 -17.416 -10.624 1.00 44.29 ? 149 ARG A CZ 1 ATOM 788 N NH1 . ARG A 1 99 ? 25.615 -16.757 -11.448 1.00 29.10 ? 149 ARG A NH1 1 ATOM 789 N NH2 . ARG A 1 99 ? 27.588 -16.882 -10.289 1.00 26.44 ? 149 ARG A NH2 1 ATOM 790 N N . ASN A 1 100 ? 20.704 -22.877 -10.291 1.00 15.27 ? 150 ASN A N 1 ATOM 791 C CA . ASN A 1 100 ? 19.900 -23.950 -10.864 1.00 14.26 ? 150 ASN A CA 1 ATOM 792 C C . ASN A 1 100 ? 18.427 -23.627 -10.879 1.00 16.55 ? 150 ASN A C 1 ATOM 793 O O . ASN A 1 100 ? 17.633 -24.469 -11.318 1.00 17.78 ? 150 ASN A O 1 ATOM 794 C CB . ASN A 1 100 ? 20.147 -25.255 -10.092 1.00 15.34 ? 150 ASN A CB 1 ATOM 795 C CG . ASN A 1 100 ? 21.615 -25.647 -10.120 1.00 19.76 ? 150 ASN A CG 1 ATOM 796 O OD1 . ASN A 1 100 ? 22.333 -25.344 -11.069 1.00 20.53 ? 150 ASN A OD1 1 ATOM 797 N ND2 . ASN A 1 100 ? 22.097 -26.282 -9.077 1.00 13.87 ? 150 ASN A ND2 1 ATOM 798 N N . MET A 1 101 ? 18.051 -22.434 -10.391 1.00 14.59 ? 151 MET A N 1 ATOM 799 C CA . MET A 1 101 ? 16.637 -22.042 -10.253 1.00 13.16 ? 151 MET A CA 1 ATOM 800 C C . MET A 1 101 ? 16.248 -20.831 -11.089 1.00 17.43 ? 151 MET A C 1 ATOM 801 O O . MET A 1 101 ? 17.093 -20.074 -11.568 1.00 17.26 ? 151 MET A O 1 ATOM 802 C CB . MET A 1 101 ? 16.281 -21.823 -8.760 1.00 13.92 ? 151 MET A CB 1 ATOM 803 C CG . MET A 1 101 ? 16.772 -22.946 -7.784 1.00 16.27 ? 151 MET A CG 1 ATOM 804 S SD . MET A 1 101 ? 16.117 -24.599 -8.204 1.00 19.56 ? 151 MET A SD 1 ATOM 805 C CE . MET A 1 101 ? 14.446 -24.444 -7.550 1.00 15.87 ? 151 MET A CE 1 ATOM 806 N N . VAL A 1 102 ? 14.924 -20.638 -11.274 1.00 15.77 ? 152 VAL A N 1 ATOM 807 C CA . VAL A 1 102 ? 14.398 -19.499 -12.059 1.00 14.54 ? 152 VAL A CA 1 ATOM 808 C C . VAL A 1 102 ? 13.325 -18.781 -11.257 1.00 15.08 ? 152 VAL A C 1 ATOM 809 O O . VAL A 1 102 ? 12.344 -19.388 -10.867 1.00 15.11 ? 152 VAL A O 1 ATOM 810 C CB . VAL A 1 102 ? 13.779 -19.974 -13.402 1.00 18.59 ? 152 VAL A CB 1 ATOM 811 C CG1 . VAL A 1 102 ? 13.365 -18.787 -14.229 1.00 18.65 ? 152 VAL A CG1 1 ATOM 812 C CG2 . VAL A 1 102 ? 14.757 -20.867 -14.186 1.00 19.12 ? 152 VAL A CG2 1 ATOM 813 N N . TRP A 1 103 ? 13.497 -17.482 -11.040 1.00 13.65 ? 153 TRP A N 1 ATOM 814 C CA . TRP A 1 103 ? 12.486 -16.712 -10.336 1.00 13.31 ? 153 TRP A CA 1 ATOM 815 C C . TRP A 1 103 ? 11.558 -16.183 -11.430 1.00 16.07 ? 153 TRP A C 1 ATOM 816 O O . TRP A 1 103 ? 11.904 -15.244 -12.154 1.00 15.74 ? 153 TRP A O 1 ATOM 817 C CB . TRP A 1 103 ? 13.195 -15.574 -9.628 1.00 14.95 ? 153 TRP A CB 1 ATOM 818 C CG . TRP A 1 103 ? 12.329 -14.834 -8.654 1.00 16.29 ? 153 TRP A CG 1 ATOM 819 C CD1 . TRP A 1 103 ? 10.972 -14.954 -8.472 1.00 18.09 ? 153 TRP A CD1 1 ATOM 820 C CD2 . TRP A 1 103 ? 12.801 -13.997 -7.607 1.00 16.48 ? 153 TRP A CD2 1 ATOM 821 N NE1 . TRP A 1 103 ? 10.574 -14.156 -7.431 1.00 17.14 ? 153 TRP A NE1 1 ATOM 822 C CE2 . TRP A 1 103 ? 11.682 -13.611 -6.840 1.00 19.35 ? 153 TRP A CE2 1 ATOM 823 C CE3 . TRP A 1 103 ? 14.080 -13.558 -7.216 1.00 19.33 ? 153 TRP A CE3 1 ATOM 824 C CZ2 . TRP A 1 103 ? 11.791 -12.703 -5.764 1.00 20.60 ? 153 TRP A CZ2 1 ATOM 825 C CZ3 . TRP A 1 103 ? 14.180 -12.629 -6.184 1.00 21.09 ? 153 TRP A CZ3 1 ATOM 826 C CH2 . TRP A 1 103 ? 13.053 -12.257 -5.439 1.00 21.12 ? 153 TRP A CH2 1 ATOM 827 N N . LEU A 1 104 ? 10.341 -16.753 -11.521 1.00 13.45 ? 154 LEU A N 1 ATOM 828 C CA . LEU A 1 104 ? 9.417 -16.232 -12.526 1.00 14.30 ? 154 LEU A CA 1 ATOM 829 C C . LEU A 1 104 ? 8.680 -15.010 -11.971 1.00 15.73 ? 154 LEU A C 1 ATOM 830 O O . LEU A 1 104 ? 8.099 -15.077 -10.896 1.00 15.33 ? 154 LEU A O 1 ATOM 831 C CB . LEU A 1 104 ? 8.349 -17.278 -12.949 1.00 14.14 ? 154 LEU A CB 1 ATOM 832 C CG . LEU A 1 104 ? 8.897 -18.575 -13.550 1.00 20.04 ? 154 LEU A CG 1 ATOM 833 C CD1 . LEU A 1 104 ? 7.773 -19.588 -13.755 1.00 22.46 ? 154 LEU A CD1 1 ATOM 834 C CD2 . LEU A 1 104 ? 9.609 -18.274 -14.836 1.00 24.79 ? 154 LEU A CD2 1 ATOM 835 N N . THR A 1 105 ? 8.702 -13.908 -12.722 1.00 14.83 ? 155 THR A N 1 ATOM 836 C CA . THR A 1 105 ? 7.950 -12.703 -12.366 1.00 14.48 ? 155 THR A CA 1 ATOM 837 C C . THR A 1 105 ? 7.112 -12.171 -13.516 1.00 19.02 ? 155 THR A C 1 ATOM 838 O O . THR A 1 105 ? 7.208 -12.645 -14.659 1.00 17.93 ? 155 THR A O 1 ATOM 839 C CB . THR A 1 105 ? 8.865 -11.623 -11.742 1.00 20.85 ? 155 THR A CB 1 ATOM 840 O OG1 . THR A 1 105 ? 9.869 -11.235 -12.702 1.00 17.80 ? 155 THR A OG1 1 ATOM 841 C CG2 . THR A 1 105 ? 9.478 -12.072 -10.387 1.00 16.57 ? 155 THR A CG2 1 ATOM 842 N N . GLU A 1 106 ? 6.316 -11.139 -13.222 1.00 17.99 ? 156 GLU A N 1 ATOM 843 C CA . GLU A 1 106 ? 5.429 -10.479 -14.188 1.00 20.00 ? 156 GLU A CA 1 ATOM 844 C C . GLU A 1 106 ? 6.204 -9.967 -15.400 1.00 22.95 ? 156 GLU A C 1 ATOM 845 O O . GLU A 1 106 ? 7.350 -9.537 -15.272 1.00 22.68 ? 156 GLU A O 1 ATOM 846 C CB . GLU A 1 106 ? 4.679 -9.318 -13.490 1.00 21.78 ? 156 GLU A CB 1 ATOM 847 C CG . GLU A 1 106 ? 4.261 -8.109 -14.321 1.00 41.62 ? 156 GLU A CG 1 ATOM 848 C CD . GLU A 1 106 ? 5.310 -7.060 -14.650 1.00 55.74 ? 156 GLU A CD 1 ATOM 849 O OE1 . GLU A 1 106 ? 5.836 -6.417 -13.714 1.00 48.45 ? 156 GLU A OE1 1 ATOM 850 O OE2 . GLU A 1 106 ? 5.554 -6.829 -15.855 1.00 59.70 ? 156 GLU A OE2 1 ATOM 851 N N . LYS A 1 107 ? 5.555 -9.992 -16.551 1.00 19.74 ? 157 LYS A N 1 ATOM 852 C CA . LYS A 1 107 ? 6.107 -9.445 -17.799 1.00 20.75 ? 157 LYS A CA 1 ATOM 853 C C . LYS A 1 107 ? 5.002 -8.610 -18.435 1.00 25.99 ? 157 LYS A C 1 ATOM 854 O O . LYS A 1 107 ? 3.858 -9.073 -18.574 1.00 25.07 ? 157 LYS A O 1 ATOM 855 C CB . LYS A 1 107 ? 6.556 -10.567 -18.746 1.00 24.19 ? 157 LYS A CB 1 ATOM 856 C CG . LYS A 1 107 ? 7.139 -10.071 -20.073 1.00 37.62 ? 157 LYS A CG 1 ATOM 857 C CD . LYS A 1 107 ? 6.983 -11.137 -21.137 1.00 55.18 ? 157 LYS A CD 1 ATOM 858 C CE . LYS A 1 107 ? 7.261 -10.644 -22.536 1.00 71.31 ? 157 LYS A CE 1 ATOM 859 N NZ . LYS A 1 107 ? 6.847 -11.645 -23.558 1.00 78.40 ? 157 LYS A NZ 1 ATOM 860 N N . GLY A 1 108 ? 5.345 -7.368 -18.774 1.00 26.03 ? 158 GLY A N 1 ATOM 861 C CA . GLY A 1 108 ? 4.405 -6.440 -19.398 1.00 27.14 ? 158 GLY A CA 1 ATOM 862 C C . GLY A 1 108 ? 3.145 -6.230 -18.581 1.00 31.22 ? 158 GLY A C 1 ATOM 863 O O . GLY A 1 108 ? 2.044 -6.197 -19.136 1.00 30.77 ? 158 GLY A O 1 ATOM 864 N N . SER A 1 109 ? 3.309 -6.131 -17.243 1.00 27.79 ? 159 SER A N 1 ATOM 865 C CA . SER A 1 109 ? 2.238 -5.898 -16.266 1.00 28.11 ? 159 SER A CA 1 ATOM 866 C C . SER A 1 109 ? 1.208 -7.052 -16.171 1.00 32.49 ? 159 SER A C 1 ATOM 867 O O . SER A 1 109 ? 0.059 -6.839 -15.782 1.00 32.98 ? 159 SER A O 1 ATOM 868 C CB . SER A 1 109 ? 1.594 -4.526 -16.463 1.00 33.04 ? 159 SER A CB 1 ATOM 869 O OG . SER A 1 109 ? 1.031 -4.065 -15.248 1.00 48.19 ? 159 SER A OG 1 ATOM 870 N N . ASN A 1 110 ? 1.642 -8.285 -16.510 1.00 28.06 ? 160 ASN A N 1 ATOM 871 C CA . ASN A 1 110 ? 0.787 -9.470 -16.444 1.00 26.91 ? 160 ASN A CA 1 ATOM 872 C C . ASN A 1 110 ? 1.547 -10.667 -15.963 1.00 25.51 ? 160 ASN A C 1 ATOM 873 O O . ASN A 1 110 ? 2.711 -10.831 -16.317 1.00 23.22 ? 160 ASN A O 1 ATOM 874 C CB . ASN A 1 110 ? 0.216 -9.810 -17.831 1.00 29.85 ? 160 ASN A CB 1 ATOM 875 C CG . ASN A 1 110 ? -0.832 -8.835 -18.319 1.00 61.75 ? 160 ASN A CG 1 ATOM 876 O OD1 . ASN A 1 110 ? -0.671 -8.185 -19.356 1.00 59.90 ? 160 ASN A OD1 1 ATOM 877 N ND2 . ASN A 1 110 ? -1.918 -8.687 -17.570 1.00 55.57 ? 160 ASN A ND2 1 ATOM 878 N N . TYR A 1 111 ? 0.884 -11.546 -15.185 1.00 21.23 ? 161 TYR A N 1 ATOM 879 C CA . TYR A 1 111 ? 1.518 -12.819 -14.805 1.00 19.70 ? 161 TYR A CA 1 ATOM 880 C C . TYR A 1 111 ? 0.501 -13.871 -15.260 1.00 23.60 ? 161 TYR A C 1 ATOM 881 O O . TYR A 1 111 ? -0.412 -14.197 -14.504 1.00 23.23 ? 161 TYR A O 1 ATOM 882 C CB . TYR A 1 111 ? 1.875 -12.966 -13.295 1.00 18.04 ? 161 TYR A CB 1 ATOM 883 C CG . TYR A 1 111 ? 2.670 -14.224 -12.930 1.00 16.70 ? 161 TYR A CG 1 ATOM 884 C CD1 . TYR A 1 111 ? 3.975 -14.135 -12.434 1.00 15.00 ? 161 TYR A CD1 1 ATOM 885 C CD2 . TYR A 1 111 ? 2.081 -15.490 -12.974 1.00 16.66 ? 161 TYR A CD2 1 ATOM 886 C CE1 . TYR A 1 111 ? 4.677 -15.269 -12.033 1.00 10.25 ? 161 TYR A CE1 1 ATOM 887 C CE2 . TYR A 1 111 ? 2.788 -16.639 -12.597 1.00 17.40 ? 161 TYR A CE2 1 ATOM 888 C CZ . TYR A 1 111 ? 4.089 -16.524 -12.134 1.00 19.59 ? 161 TYR A CZ 1 ATOM 889 O OH . TYR A 1 111 ? 4.761 -17.674 -11.756 1.00 19.39 ? 161 TYR A OH 1 ATOM 890 N N . PRO A 1 112 ? 0.572 -14.355 -16.521 1.00 21.31 ? 162 PRO A N 1 ATOM 891 C CA . PRO A 1 112 ? -0.403 -15.367 -16.946 1.00 21.68 ? 162 PRO A CA 1 ATOM 892 C C . PRO A 1 112 ? -0.047 -16.692 -16.276 1.00 24.84 ? 162 PRO A C 1 ATOM 893 O O . PRO A 1 112 ? 0.989 -16.796 -15.590 1.00 22.82 ? 162 PRO A O 1 ATOM 894 C CB . PRO A 1 112 ? -0.264 -15.401 -18.470 1.00 25.50 ? 162 PRO A CB 1 ATOM 895 C CG . PRO A 1 112 ? 1.106 -14.881 -18.746 1.00 29.55 ? 162 PRO A CG 1 ATOM 896 C CD . PRO A 1 112 ? 1.533 -14.020 -17.596 1.00 24.62 ? 162 PRO A CD 1 ATOM 897 N N . VAL A 1 113 ? -0.931 -17.661 -16.391 1.00 21.99 ? 163 VAL A N 1 ATOM 898 C CA . VAL A 1 113 ? -0.662 -18.953 -15.793 1.00 21.79 ? 163 VAL A CA 1 ATOM 899 C C . VAL A 1 113 ? 0.643 -19.521 -16.364 1.00 24.18 ? 163 VAL A C 1 ATOM 900 O O . VAL A 1 113 ? 0.837 -19.568 -17.587 1.00 24.92 ? 163 VAL A O 1 ATOM 901 C CB . VAL A 1 113 ? -1.843 -19.955 -15.924 1.00 25.85 ? 163 VAL A CB 1 ATOM 902 C CG1 . VAL A 1 113 ? -1.543 -21.224 -15.130 1.00 24.93 ? 163 VAL A CG1 1 ATOM 903 C CG2 . VAL A 1 113 ? -3.157 -19.330 -15.452 1.00 26.75 ? 163 VAL A CG2 1 ATOM 904 N N . ALA A 1 114 ? 1.553 -19.903 -15.463 1.00 18.68 ? 164 ALA A N 1 ATOM 905 C CA . ALA A 1 114 ? 2.831 -20.513 -15.834 1.00 18.39 ? 164 ALA A CA 1 ATOM 906 C C . ALA A 1 114 ? 2.653 -22.033 -15.783 1.00 20.58 ? 164 ALA A C 1 ATOM 907 O O . ALA A 1 114 ? 2.237 -22.565 -14.755 1.00 22.05 ? 164 ALA A O 1 ATOM 908 C CB . ALA A 1 114 ? 3.908 -20.091 -14.871 1.00 18.83 ? 164 ALA A CB 1 ATOM 909 N N . LYS A 1 115 ? 2.907 -22.712 -16.877 1.00 18.94 ? 165 LYS A N 1 ATOM 910 C CA . LYS A 1 115 ? 2.787 -24.170 -16.976 1.00 19.48 ? 165 LYS A CA 1 ATOM 911 C C . LYS A 1 115 ? 4.036 -24.748 -17.621 1.00 21.35 ? 165 LYS A C 1 ATOM 912 O O . LYS A 1 115 ? 4.552 -24.202 -18.596 1.00 22.19 ? 165 LYS A O 1 ATOM 913 C CB . LYS A 1 115 ? 1.567 -24.575 -17.828 1.00 24.12 ? 165 LYS A CB 1 ATOM 914 C CG . LYS A 1 115 ? 0.235 -24.145 -17.240 1.00 31.15 ? 165 LYS A CG 1 ATOM 915 C CD . LYS A 1 115 ? -0.960 -24.845 -17.911 1.00 35.00 ? 165 LYS A CD 1 ATOM 916 C CE . LYS A 1 115 ? -2.245 -24.352 -17.303 1.00 43.36 ? 165 LYS A CE 1 ATOM 917 N NZ . LYS A 1 115 ? -3.426 -25.117 -17.778 1.00 52.06 ? 165 LYS A NZ 1 ATOM 918 N N . GLY A 1 116 ? 4.519 -25.834 -17.044 1.00 16.61 ? 166 GLY A N 1 ATOM 919 C CA . GLY A 1 116 ? 5.699 -26.514 -17.540 1.00 17.57 ? 166 GLY A CA 1 ATOM 920 C C . GLY A 1 116 ? 5.677 -27.957 -17.150 1.00 21.13 ? 166 GLY A C 1 ATOM 921 O O . GLY A 1 116 ? 5.171 -28.309 -16.082 1.00 21.09 ? 166 GLY A O 1 ATOM 922 N N . SER A 1 117 ? 6.208 -28.802 -18.013 1.00 17.64 ? 167 SER A N 1 ATOM 923 C CA . SER A 1 117 ? 6.242 -30.207 -17.670 1.00 17.96 ? 167 SER A CA 1 ATOM 924 C C . SER A 1 117 ? 7.521 -30.844 -18.173 1.00 20.45 ? 167 SER A C 1 ATOM 925 O O . SER A 1 117 ? 8.129 -30.342 -19.127 1.00 17.53 ? 167 SER A O 1 ATOM 926 C CB . SER A 1 117 ? 5.011 -30.926 -18.237 1.00 25.29 ? 167 SER A CB 1 ATOM 927 O OG . SER A 1 117 ? 5.052 -31.009 -19.651 1.00 34.83 ? 167 SER A OG 1 ATOM 928 N N . TYR A 1 118 ? 7.905 -31.962 -17.542 1.00 15.29 ? 168 TYR A N 1 ATOM 929 C CA . TYR A 1 118 ? 9.080 -32.710 -17.926 1.00 15.20 ? 168 TYR A CA 1 ATOM 930 C C . TYR A 1 118 ? 8.817 -34.203 -17.740 1.00 17.64 ? 168 TYR A C 1 ATOM 931 O O . TYR A 1 118 ? 8.455 -34.629 -16.647 1.00 16.24 ? 168 TYR A O 1 ATOM 932 C CB . TYR A 1 118 ? 10.355 -32.252 -17.136 1.00 14.12 ? 168 TYR A CB 1 ATOM 933 C CG . TYR A 1 118 ? 11.524 -33.191 -17.317 1.00 15.82 ? 168 TYR A CG 1 ATOM 934 C CD1 . TYR A 1 118 ? 12.267 -33.194 -18.496 1.00 18.87 ? 168 TYR A CD1 1 ATOM 935 C CD2 . TYR A 1 118 ? 11.815 -34.162 -16.368 1.00 16.52 ? 168 TYR A CD2 1 ATOM 936 C CE1 . TYR A 1 118 ? 13.321 -34.088 -18.684 1.00 16.21 ? 168 TYR A CE1 1 ATOM 937 C CE2 . TYR A 1 118 ? 12.816 -35.111 -16.581 1.00 17.55 ? 168 TYR A CE2 1 ATOM 938 C CZ . TYR A 1 118 ? 13.554 -35.086 -17.752 1.00 18.57 ? 168 TYR A CZ 1 ATOM 939 O OH . TYR A 1 118 ? 14.542 -36.030 -17.983 1.00 19.27 ? 168 TYR A OH 1 ATOM 940 N N . ASN A 1 119 ? 9.047 -34.976 -18.800 1.00 17.77 ? 169 ASN A N 1 ATOM 941 C CA . ASN A 1 119 ? 8.919 -36.442 -18.796 1.00 18.30 ? 169 ASN A CA 1 ATOM 942 C C . ASN A 1 119 ? 10.299 -37.046 -18.540 1.00 21.39 ? 169 ASN A C 1 ATOM 943 O O . ASN A 1 119 ? 11.236 -36.761 -19.278 1.00 21.93 ? 169 ASN A O 1 ATOM 944 C CB . ASN A 1 119 ? 8.341 -36.962 -20.122 1.00 20.85 ? 169 ASN A CB 1 ATOM 945 C CG . ASN A 1 119 ? 7.971 -38.429 -20.058 1.00 35.21 ? 169 ASN A CG 1 ATOM 946 O OD1 . ASN A 1 119 ? 8.258 -39.131 -19.084 1.00 26.29 ? 169 ASN A OD1 1 ATOM 947 N ND2 . ASN A 1 119 ? 7.337 -38.935 -21.102 1.00 36.92 ? 169 ASN A ND2 1 ATOM 948 N N . ASN A 1 120 ? 10.440 -37.813 -17.463 1.00 17.00 ? 170 ASN A N 1 ATOM 949 C CA . ASN A 1 120 ? 11.731 -38.384 -17.103 1.00 16.70 ? 170 ASN A CA 1 ATOM 950 C C . ASN A 1 120 ? 12.176 -39.515 -18.033 1.00 19.06 ? 170 ASN A C 1 ATOM 951 O O . ASN A 1 120 ? 12.027 -40.701 -17.736 1.00 17.91 ? 170 ASN A O 1 ATOM 952 C CB . ASN A 1 120 ? 11.792 -38.800 -15.626 1.00 16.33 ? 170 ASN A CB 1 ATOM 953 C CG . ASN A 1 120 ? 13.179 -39.236 -15.199 1.00 21.17 ? 170 ASN A CG 1 ATOM 954 O OD1 . ASN A 1 120 ? 14.157 -39.147 -15.942 1.00 21.80 ? 170 ASN A OD1 1 ATOM 955 N ND2 . ASN A 1 120 ? 13.298 -39.734 -13.996 1.00 17.60 ? 170 ASN A ND2 1 ATOM 956 N N . THR A 1 121 ? 12.779 -39.103 -19.143 1.00 17.03 ? 171 THR A N 1 ATOM 957 C CA . THR A 1 121 ? 13.325 -40.010 -20.164 1.00 18.51 ? 171 THR A CA 1 ATOM 958 C C . THR A 1 121 ? 14.858 -40.018 -20.036 1.00 23.31 ? 171 THR A C 1 ATOM 959 O O . THR A 1 121 ? 15.552 -40.433 -20.969 1.00 23.53 ? 171 THR A O 1 ATOM 960 C CB . THR A 1 121 ? 12.839 -39.573 -21.546 1.00 21.83 ? 171 THR A CB 1 ATOM 961 O OG1 . THR A 1 121 ? 13.281 -38.247 -21.787 1.00 27.29 ? 171 THR A OG1 1 ATOM 962 C CG2 . THR A 1 121 ? 11.332 -39.642 -21.701 1.00 23.37 ? 171 THR A CG2 1 ATOM 963 N N . SER A 1 122 ? 15.381 -39.619 -18.847 1.00 19.06 ? 172 SER A N 1 ATOM 964 C CA . SER A 1 122 ? 16.835 -39.533 -18.577 1.00 20.64 ? 172 SER A CA 1 ATOM 965 C C . SER A 1 122 ? 17.572 -40.876 -18.390 1.00 26.45 ? 172 SER A C 1 ATOM 966 O O . SER A 1 122 ? 18.804 -40.905 -18.510 1.00 26.58 ? 172 SER A O 1 ATOM 967 C CB . SER A 1 122 ? 17.105 -38.628 -17.373 1.00 21.67 ? 172 SER A CB 1 ATOM 968 O OG . SER A 1 122 ? 16.868 -39.330 -16.158 1.00 23.09 ? 172 SER A OG 1 ATOM 969 N N . GLY A 1 123 ? 16.839 -41.943 -18.040 1.00 24.01 ? 173 GLY A N 1 ATOM 970 C CA . GLY A 1 123 ? 17.425 -43.256 -17.801 1.00 24.12 ? 173 GLY A CA 1 ATOM 971 C C . GLY A 1 123 ? 17.571 -43.630 -16.334 1.00 26.88 ? 173 GLY A C 1 ATOM 972 O O . GLY A 1 123 ? 17.932 -44.766 -16.022 1.00 27.96 ? 173 GLY A O 1 ATOM 973 N N . GLU A 1 124 ? 17.297 -42.690 -15.417 1.00 20.18 ? 174 GLU A N 1 ATOM 974 C CA . GLU A 1 124 ? 17.327 -42.954 -13.972 1.00 20.37 ? 174 GLU A CA 1 ATOM 975 C C . GLU A 1 124 ? 16.369 -42.077 -13.203 1.00 22.63 ? 174 GLU A C 1 ATOM 976 O O . GLU A 1 124 ? 15.815 -41.122 -13.758 1.00 22.29 ? 174 GLU A O 1 ATOM 977 C CB . GLU A 1 124 ? 18.749 -42.879 -13.370 1.00 22.19 ? 174 GLU A CB 1 ATOM 978 C CG . GLU A 1 124 ? 19.195 -44.248 -12.853 1.00 39.74 ? 174 GLU A CG 1 ATOM 979 C CD . GLU A 1 124 ? 18.808 -44.582 -11.416 1.00 65.20 ? 174 GLU A CD 1 ATOM 980 O OE1 . GLU A 1 124 ? 17.593 -44.695 -11.118 1.00 39.45 ? 174 GLU A OE1 1 ATOM 981 O OE2 . GLU A 1 124 ? 19.734 -44.763 -10.589 1.00 62.71 ? 174 GLU A OE2 1 ATOM 982 N N . GLN A 1 125 ? 16.169 -42.407 -11.913 1.00 19.35 ? 175 GLN A N 1 ATOM 983 C CA . GLN A 1 125 ? 15.337 -41.585 -11.033 1.00 18.58 ? 175 GLN A CA 1 ATOM 984 C C . GLN A 1 125 ? 15.987 -40.199 -10.954 1.00 19.49 ? 175 GLN A C 1 ATOM 985 O O . GLN A 1 125 ? 17.216 -40.086 -11.010 1.00 19.85 ? 175 GLN A O 1 ATOM 986 C CB . GLN A 1 125 ? 15.342 -42.211 -9.650 1.00 21.63 ? 175 GLN A CB 1 ATOM 987 C CG . GLN A 1 125 ? 14.176 -41.810 -8.766 1.00 35.50 ? 175 GLN A CG 1 ATOM 988 C CD . GLN A 1 125 ? 14.047 -42.795 -7.627 1.00 45.38 ? 175 GLN A CD 1 ATOM 989 O OE1 . GLN A 1 125 ? 15.025 -43.431 -7.202 1.00 37.71 ? 175 GLN A OE1 1 ATOM 990 N NE2 . GLN A 1 125 ? 12.831 -42.973 -7.140 1.00 30.87 ? 175 GLN A NE2 1 ATOM 991 N N . MET A 1 126 ? 15.161 -39.158 -10.829 1.00 16.15 ? 176 MET A N 1 ATOM 992 C CA . MET A 1 126 ? 15.685 -37.796 -10.809 1.00 15.23 ? 176 MET A CA 1 ATOM 993 C C . MET A 1 126 ? 15.202 -37.018 -9.605 1.00 19.02 ? 176 MET A C 1 ATOM 994 O O . MET A 1 126 ? 14.014 -37.028 -9.294 1.00 19.30 ? 176 MET A O 1 ATOM 995 C CB . MET A 1 126 ? 15.241 -37.090 -12.078 1.00 17.08 ? 176 MET A CB 1 ATOM 996 C CG . MET A 1 126 ? 15.847 -35.736 -12.281 1.00 20.67 ? 176 MET A CG 1 ATOM 997 S SD . MET A 1 126 ? 15.144 -34.990 -13.773 1.00 23.21 ? 176 MET A SD 1 ATOM 998 C CE . MET A 1 126 ? 15.999 -36.014 -15.034 1.00 19.63 ? 176 MET A CE 1 ATOM 999 N N . LEU A 1 127 ? 16.130 -36.332 -8.943 1.00 14.63 ? 177 LEU A N 1 ATOM 1000 C CA . LEU A 1 127 ? 15.794 -35.453 -7.847 1.00 13.78 ? 177 LEU A CA 1 ATOM 1001 C C . LEU A 1 127 ? 15.427 -34.058 -8.464 1.00 17.15 ? 177 LEU A C 1 ATOM 1002 O O . LEU A 1 127 ? 16.170 -33.501 -9.285 1.00 15.33 ? 177 LEU A O 1 ATOM 1003 C CB . LEU A 1 127 ? 17.045 -35.321 -6.938 1.00 12.19 ? 177 LEU A CB 1 ATOM 1004 C CG . LEU A 1 127 ? 17.008 -34.264 -5.862 1.00 17.63 ? 177 LEU A CG 1 ATOM 1005 C CD1 . LEU A 1 127 ? 15.876 -34.517 -4.866 1.00 18.80 ? 177 LEU A CD1 1 ATOM 1006 C CD2 . LEU A 1 127 ? 18.378 -34.166 -5.120 1.00 17.88 ? 177 LEU A CD2 1 ATOM 1007 N N . ILE A 1 128 ? 14.275 -33.518 -8.060 1.00 13.73 ? 178 ILE A N 1 ATOM 1008 C CA . ILE A 1 128 ? 13.850 -32.215 -8.536 1.00 13.42 ? 178 ILE A CA 1 ATOM 1009 C C . ILE A 1 128 ? 13.437 -31.420 -7.305 1.00 15.91 ? 178 ILE A C 1 ATOM 1010 O O . ILE A 1 128 ? 12.779 -31.958 -6.419 1.00 15.62 ? 178 ILE A O 1 ATOM 1011 C CB . ILE A 1 128 ? 12.690 -32.308 -9.575 1.00 16.17 ? 178 ILE A CB 1 ATOM 1012 C CG1 . ILE A 1 128 ? 13.069 -33.185 -10.787 1.00 17.65 ? 178 ILE A CG1 1 ATOM 1013 C CG2 . ILE A 1 128 ? 12.147 -30.927 -9.978 1.00 17.46 ? 178 ILE A CG2 1 ATOM 1014 C CD1 . ILE A 1 128 ? 11.978 -33.440 -11.746 1.00 21.56 ? 178 ILE A CD1 1 ATOM 1015 N N . ILE A 1 129 ? 13.807 -30.149 -7.292 1.00 13.85 ? 179 ILE A N 1 ATOM 1016 C CA . ILE A 1 129 ? 13.523 -29.173 -6.217 1.00 11.29 ? 179 ILE A CA 1 ATOM 1017 C C . ILE A 1 129 ? 12.773 -28.003 -6.823 1.00 15.11 ? 179 ILE A C 1 ATOM 1018 O O . ILE A 1 129 ? 13.066 -27.602 -7.951 1.00 14.46 ? 179 ILE A O 1 ATOM 1019 C CB . ILE A 1 129 ? 14.889 -28.677 -5.599 1.00 14.82 ? 179 ILE A CB 1 ATOM 1020 C CG1 . ILE A 1 129 ? 15.636 -29.853 -4.933 1.00 16.44 ? 179 ILE A CG1 1 ATOM 1021 C CG2 . ILE A 1 129 ? 14.698 -27.502 -4.581 1.00 15.39 ? 179 ILE A CG2 1 ATOM 1022 C CD1 . ILE A 1 129 ? 17.127 -29.503 -4.642 1.00 21.15 ? 179 ILE A CD1 1 ATOM 1023 N N . TRP A 1 130 ? 11.824 -27.444 -6.086 1.00 12.20 ? 180 TRP A N 1 ATOM 1024 C CA . TRP A 1 130 ? 11.146 -26.219 -6.528 1.00 13.34 ? 180 TRP A CA 1 ATOM 1025 C C . TRP A 1 130 ? 10.869 -25.389 -5.305 1.00 14.80 ? 180 TRP A C 1 ATOM 1026 O O . TRP A 1 130 ? 10.948 -25.873 -4.177 1.00 14.28 ? 180 TRP A O 1 ATOM 1027 C CB . TRP A 1 130 ? 9.814 -26.534 -7.264 1.00 11.97 ? 180 TRP A CB 1 ATOM 1028 C CG . TRP A 1 130 ? 8.746 -27.037 -6.332 1.00 13.60 ? 180 TRP A CG 1 ATOM 1029 C CD1 . TRP A 1 130 ? 7.760 -26.315 -5.757 1.00 16.83 ? 180 TRP A CD1 1 ATOM 1030 C CD2 . TRP A 1 130 ? 8.543 -28.398 -5.925 1.00 14.77 ? 180 TRP A CD2 1 ATOM 1031 N NE1 . TRP A 1 130 ? 6.970 -27.136 -4.958 1.00 18.65 ? 180 TRP A NE1 1 ATOM 1032 C CE2 . TRP A 1 130 ? 7.457 -28.410 -5.019 1.00 20.27 ? 180 TRP A CE2 1 ATOM 1033 C CE3 . TRP A 1 130 ? 9.201 -29.605 -6.209 1.00 18.21 ? 180 TRP A CE3 1 ATOM 1034 C CZ2 . TRP A 1 130 ? 6.948 -29.604 -4.477 1.00 21.06 ? 180 TRP A CZ2 1 ATOM 1035 C CZ3 . TRP A 1 130 ? 8.754 -30.772 -5.575 1.00 20.03 ? 180 TRP A CZ3 1 ATOM 1036 C CH2 . TRP A 1 130 ? 7.654 -30.748 -4.711 1.00 20.57 ? 180 TRP A CH2 1 ATOM 1037 N N . GLY A 1 131 ? 10.603 -24.128 -5.531 1.00 10.99 ? 181 GLY A N 1 ATOM 1038 C CA . GLY A 1 131 ? 10.308 -23.272 -4.387 1.00 11.57 ? 181 GLY A CA 1 ATOM 1039 C C . GLY A 1 131 ? 9.030 -22.475 -4.475 1.00 15.64 ? 181 GLY A C 1 ATOM 1040 O O . GLY A 1 131 ? 8.438 -22.340 -5.556 1.00 15.00 ? 181 GLY A O 1 ATOM 1041 N N . VAL A 1 132 ? 8.572 -21.990 -3.301 1.00 12.47 ? 182 VAL A N 1 ATOM 1042 C CA . VAL A 1 132 ? 7.422 -21.095 -3.162 1.00 12.98 ? 182 VAL A CA 1 ATOM 1043 C C . VAL A 1 132 ? 7.921 -19.834 -2.482 1.00 15.40 ? 182 VAL A C 1 ATOM 1044 O O . VAL A 1 132 ? 8.518 -19.893 -1.382 1.00 14.30 ? 182 VAL A O 1 ATOM 1045 C CB . VAL A 1 132 ? 6.238 -21.736 -2.374 1.00 17.23 ? 182 VAL A CB 1 ATOM 1046 C CG1 . VAL A 1 132 ? 5.090 -20.731 -2.188 1.00 17.47 ? 182 VAL A CG1 1 ATOM 1047 C CG2 . VAL A 1 132 ? 5.762 -23.005 -3.099 1.00 17.87 ? 182 VAL A CG2 1 ATOM 1048 N N . HIS A 1 133 ? 7.681 -18.666 -3.127 1.00 12.05 ? 183 HIS A N 1 ATOM 1049 C CA . HIS A 1 133 ? 8.066 -17.399 -2.546 1.00 11.35 ? 183 HIS A CA 1 ATOM 1050 C C . HIS A 1 133 ? 6.947 -16.818 -1.693 1.00 15.99 ? 183 HIS A C 1 ATOM 1051 O O . HIS A 1 133 ? 5.783 -16.735 -2.136 1.00 13.60 ? 183 HIS A O 1 ATOM 1052 C CB . HIS A 1 133 ? 8.437 -16.410 -3.637 1.00 13.28 ? 183 HIS A CB 1 ATOM 1053 C CG . HIS A 1 133 ? 8.949 -15.122 -3.098 1.00 16.32 ? 183 HIS A CG 1 ATOM 1054 N ND1 . HIS A 1 133 ? 8.652 -13.936 -3.707 1.00 18.93 ? 183 HIS A ND1 1 ATOM 1055 C CD2 . HIS A 1 133 ? 9.759 -14.882 -2.031 1.00 17.47 ? 183 HIS A CD2 1 ATOM 1056 C CE1 . HIS A 1 133 ? 9.285 -12.998 -3.007 1.00 18.75 ? 183 HIS A CE1 1 ATOM 1057 N NE2 . HIS A 1 133 ? 9.943 -13.517 -1.973 1.00 18.12 ? 183 HIS A NE2 1 ATOM 1058 N N . HIS A 1 134 ? 7.289 -16.576 -0.431 1.00 14.14 ? 184 HIS A N 1 ATOM 1059 C CA . HIS A 1 134 ? 6.366 -16.052 0.576 1.00 13.14 ? 184 HIS A CA 1 ATOM 1060 C C . HIS A 1 134 ? 6.761 -14.590 0.798 1.00 14.83 ? 184 HIS A C 1 ATOM 1061 O O . HIS A 1 134 ? 7.695 -14.289 1.561 1.00 15.53 ? 184 HIS A O 1 ATOM 1062 C CB . HIS A 1 134 ? 6.495 -16.842 1.904 1.00 13.33 ? 184 HIS A CB 1 ATOM 1063 C CG . HIS A 1 134 ? 6.134 -18.282 1.775 1.00 16.59 ? 184 HIS A CG 1 ATOM 1064 N ND1 . HIS A 1 134 ? 4.825 -18.665 1.592 1.00 17.90 ? 184 HIS A ND1 1 ATOM 1065 C CD2 . HIS A 1 134 ? 6.920 -19.391 1.754 1.00 18.94 ? 184 HIS A CD2 1 ATOM 1066 C CE1 . HIS A 1 134 ? 4.836 -19.992 1.488 1.00 18.32 ? 184 HIS A CE1 1 ATOM 1067 N NE2 . HIS A 1 134 ? 6.075 -20.473 1.595 1.00 19.40 ? 184 HIS A NE2 1 ATOM 1068 N N . PRO A 1 135 ? 6.133 -13.636 0.120 1.00 13.24 ? 185 PRO A N 1 ATOM 1069 C CA . PRO A 1 135 ? 6.574 -12.242 0.255 1.00 14.00 ? 185 PRO A CA 1 ATOM 1070 C C . PRO A 1 135 ? 6.408 -11.636 1.640 1.00 16.98 ? 185 PRO A C 1 ATOM 1071 O O . PRO A 1 135 ? 5.667 -12.152 2.486 1.00 15.70 ? 185 PRO A O 1 ATOM 1072 C CB . PRO A 1 135 ? 5.747 -11.516 -0.804 1.00 15.99 ? 185 PRO A CB 1 ATOM 1073 C CG . PRO A 1 135 ? 5.416 -12.553 -1.778 1.00 21.65 ? 185 PRO A CG 1 ATOM 1074 C CD . PRO A 1 135 ? 5.085 -13.735 -0.906 1.00 17.77 ? 185 PRO A CD 1 ATOM 1075 N N . ASN A 1 136 ? 7.068 -10.505 1.827 1.00 14.89 ? 186 ASN A N 1 ATOM 1076 C CA . ASN A 1 136 ? 7.006 -9.766 3.081 1.00 14.40 ? 186 ASN A CA 1 ATOM 1077 C C . ASN A 1 136 ? 5.683 -9.020 3.236 1.00 20.06 ? 186 ASN A C 1 ATOM 1078 O O . ASN A 1 136 ? 5.199 -8.830 4.362 1.00 20.34 ? 186 ASN A O 1 ATOM 1079 C CB . ASN A 1 136 ? 8.188 -8.815 3.136 1.00 16.88 ? 186 ASN A CB 1 ATOM 1080 C CG . ASN A 1 136 ? 8.294 -8.076 4.435 1.00 22.08 ? 186 ASN A CG 1 ATOM 1081 O OD1 . ASN A 1 136 ? 8.729 -8.631 5.449 1.00 20.20 ? 186 ASN A OD1 1 ATOM 1082 N ND2 . ASN A 1 136 ? 7.809 -6.833 4.447 1.00 24.06 ? 186 ASN A ND2 1 ATOM 1083 N N . ASP A 1 137 ? 5.100 -8.569 2.108 1.00 16.95 ? 187 ASP A N 1 ATOM 1084 C CA . ASP A 1 137 ? 3.881 -7.734 2.131 1.00 16.45 ? 187 ASP A CA 1 ATOM 1085 C C . ASP A 1 137 ? 3.140 -7.791 0.801 1.00 17.80 ? 187 ASP A C 1 ATOM 1086 O O . ASP A 1 137 ? 3.661 -8.349 -0.171 1.00 17.24 ? 187 ASP A O 1 ATOM 1087 C CB . ASP A 1 137 ? 4.236 -6.282 2.479 1.00 19.45 ? 187 ASP A CB 1 ATOM 1088 C CG . ASP A 1 137 ? 5.347 -5.710 1.620 1.00 33.70 ? 187 ASP A CG 1 ATOM 1089 O OD1 . ASP A 1 137 ? 5.099 -5.452 0.425 1.00 34.35 ? 187 ASP A OD1 1 ATOM 1090 O OD2 . ASP A 1 137 ? 6.487 -5.602 2.121 1.00 35.58 ? 187 ASP A OD2 1 ATOM 1091 N N . GLU A 1 138 ? 1.887 -7.273 0.786 1.00 17.40 ? 188 GLU A N 1 ATOM 1092 C CA . GLU A 1 138 ? 1.048 -7.304 -0.408 1.00 17.78 ? 188 GLU A CA 1 ATOM 1093 C C . GLU A 1 138 ? 1.619 -6.423 -1.501 1.00 18.19 ? 188 GLU A C 1 ATOM 1094 O O . GLU A 1 138 ? 1.455 -6.767 -2.668 1.00 18.08 ? 188 GLU A O 1 ATOM 1095 C CB . GLU A 1 138 ? -0.418 -6.980 -0.084 1.00 20.44 ? 188 GLU A CB 1 ATOM 1096 C CG . GLU A 1 138 ? -1.098 -8.060 0.753 1.00 26.79 ? 188 GLU A CG 1 ATOM 1097 C CD . GLU A 1 138 ? -2.583 -7.871 1.051 1.00 50.71 ? 188 GLU A CD 1 ATOM 1098 O OE1 . GLU A 1 138 ? -2.961 -6.777 1.535 1.00 48.98 ? 188 GLU A OE1 1 ATOM 1099 O OE2 . GLU A 1 138 ? -3.363 -8.833 0.844 1.00 36.57 ? 188 GLU A OE2 1 ATOM 1100 N N . THR A 1 139 ? 2.315 -5.322 -1.143 1.00 17.38 ? 189 THR A N 1 ATOM 1101 C CA . THR A 1 139 ? 2.960 -4.480 -2.161 1.00 18.67 ? 189 THR A CA 1 ATOM 1102 C C . THR A 1 139 ? 4.000 -5.286 -2.966 1.00 21.19 ? 189 THR A C 1 ATOM 1103 O O . THR A 1 139 ? 3.961 -5.234 -4.180 1.00 19.61 ? 189 THR A O 1 ATOM 1104 C CB . THR A 1 139 ? 3.470 -3.153 -1.570 1.00 27.43 ? 189 THR A CB 1 ATOM 1105 O OG1 . THR A 1 139 ? 2.359 -2.475 -0.972 1.00 32.82 ? 189 THR A OG1 1 ATOM 1106 C CG2 . THR A 1 139 ? 4.118 -2.249 -2.639 1.00 28.85 ? 189 THR A CG2 1 ATOM 1107 N N . GLU A 1 140 ? 4.874 -6.056 -2.294 1.00 19.85 ? 190 GLU A N 1 ATOM 1108 C CA . GLU A 1 140 ? 5.883 -6.942 -2.891 1.00 19.78 ? 190 GLU A CA 1 ATOM 1109 C C . GLU A 1 140 ? 5.195 -8.010 -3.759 1.00 19.50 ? 190 GLU A C 1 ATOM 1110 O O . GLU A 1 140 ? 5.608 -8.258 -4.891 1.00 18.03 ? 190 GLU A O 1 ATOM 1111 C CB . GLU A 1 140 ? 6.668 -7.637 -1.758 1.00 21.73 ? 190 GLU A CB 1 ATOM 1112 C CG . GLU A 1 140 ? 8.143 -7.846 -2.025 1.00 39.25 ? 190 GLU A CG 1 ATOM 1113 C CD . GLU A 1 140 ? 8.712 -9.129 -1.442 1.00 62.75 ? 190 GLU A CD 1 ATOM 1114 O OE1 . GLU A 1 140 ? 8.752 -9.274 -0.198 1.00 36.42 ? 190 GLU A OE1 1 ATOM 1115 O OE2 . GLU A 1 140 ? 9.120 -9.997 -2.245 1.00 61.72 ? 190 GLU A OE2 1 ATOM 1116 N N . GLN A 1 141 ? 4.101 -8.605 -3.243 1.00 15.79 ? 191 GLN A N 1 ATOM 1117 C CA . GLN A 1 141 ? 3.355 -9.613 -3.979 1.00 13.83 ? 191 GLN A CA 1 ATOM 1118 C C . GLN A 1 141 ? 2.877 -9.061 -5.311 1.00 18.04 ? 191 GLN A C 1 ATOM 1119 O O . GLN A 1 141 ? 3.039 -9.736 -6.332 1.00 19.66 ? 191 GLN A O 1 ATOM 1120 C CB . GLN A 1 141 ? 2.147 -10.147 -3.156 1.00 14.04 ? 191 GLN A CB 1 ATOM 1121 C CG . GLN A 1 141 ? 1.178 -11.022 -3.983 1.00 13.87 ? 191 GLN A CG 1 ATOM 1122 C CD . GLN A 1 141 ? 1.750 -12.392 -4.234 1.00 17.11 ? 191 GLN A CD 1 ATOM 1123 O OE1 . GLN A 1 141 ? 2.625 -12.857 -3.481 1.00 17.53 ? 191 GLN A OE1 1 ATOM 1124 N NE2 . GLN A 1 141 ? 1.303 -13.029 -5.299 1.00 13.37 ? 191 GLN A NE2 1 ATOM 1125 N N . ARG A 1 142 ? 2.235 -7.870 -5.291 1.00 17.70 ? 192 ARG A N 1 ATOM 1126 C CA . ARG A 1 142 ? 1.731 -7.238 -6.516 1.00 15.97 ? 192 ARG A CA 1 ATOM 1127 C C . ARG A 1 142 ? 2.864 -6.825 -7.453 1.00 18.31 ? 192 ARG A C 1 ATOM 1128 O O . ARG A 1 142 ? 2.710 -6.942 -8.670 1.00 20.33 ? 192 ARG A O 1 ATOM 1129 C CB . ARG A 1 142 ? 0.788 -6.072 -6.168 1.00 17.77 ? 192 ARG A CB 1 ATOM 1130 C CG . ARG A 1 142 ? -0.468 -6.562 -5.444 1.00 24.92 ? 192 ARG A CG 1 ATOM 1131 C CD . ARG A 1 142 ? -1.515 -5.471 -5.256 1.00 33.80 ? 192 ARG A CD 1 ATOM 1132 N NE . ARG A 1 142 ? -2.713 -6.052 -4.655 1.00 43.91 ? 192 ARG A NE 1 ATOM 1133 C CZ . ARG A 1 142 ? -3.253 -5.667 -3.506 1.00 60.39 ? 192 ARG A CZ 1 ATOM 1134 N NH1 . ARG A 1 142 ? -2.749 -4.636 -2.839 1.00 57.73 ? 192 ARG A NH1 1 ATOM 1135 N NH2 . ARG A 1 142 ? -4.329 -6.283 -3.035 1.00 43.63 ? 192 ARG A NH2 1 ATOM 1136 N N . THR A 1 143 ? 3.995 -6.325 -6.922 1.00 16.36 ? 193 THR A N 1 ATOM 1137 C CA . THR A 1 143 ? 5.114 -5.900 -7.784 1.00 17.43 ? 193 THR A CA 1 ATOM 1138 C C . THR A 1 143 ? 5.728 -7.074 -8.553 1.00 21.18 ? 193 THR A C 1 ATOM 1139 O O . THR A 1 143 ? 6.064 -6.927 -9.720 1.00 21.14 ? 193 THR A O 1 ATOM 1140 C CB . THR A 1 143 ? 6.180 -5.163 -6.985 1.00 23.70 ? 193 THR A CB 1 ATOM 1141 O OG1 . THR A 1 143 ? 6.566 -5.968 -5.885 1.00 45.18 ? 193 THR A OG1 1 ATOM 1142 C CG2 . THR A 1 143 ? 5.684 -3.864 -6.467 1.00 23.02 ? 193 THR A CG2 1 ATOM 1143 N N . LEU A 1 144 ? 5.847 -8.230 -7.902 1.00 16.82 ? 194 LEU A N 1 ATOM 1144 C CA . LEU A 1 144 ? 6.457 -9.405 -8.539 1.00 16.29 ? 194 LEU A CA 1 ATOM 1145 C C . LEU A 1 144 ? 5.458 -10.205 -9.350 1.00 18.58 ? 194 LEU A C 1 ATOM 1146 O O . LEU A 1 144 ? 5.799 -10.702 -10.430 1.00 18.00 ? 194 LEU A O 1 ATOM 1147 C CB . LEU A 1 144 ? 7.032 -10.321 -7.463 1.00 16.29 ? 194 LEU A CB 1 ATOM 1148 C CG . LEU A 1 144 ? 8.201 -9.756 -6.629 1.00 20.79 ? 194 LEU A CG 1 ATOM 1149 C CD1 . LEU A 1 144 ? 8.463 -10.622 -5.426 1.00 20.55 ? 194 LEU A CD1 1 ATOM 1150 C CD2 . LEU A 1 144 ? 9.467 -9.617 -7.448 1.00 23.65 ? 194 LEU A CD2 1 ATOM 1151 N N . TYR A 1 145 ? 4.221 -10.353 -8.830 1.00 16.21 ? 195 TYR A N 1 ATOM 1152 C CA . TYR A 1 145 ? 3.260 -11.299 -9.418 1.00 15.80 ? 195 TYR A CA 1 ATOM 1153 C C . TYR A 1 145 ? 1.912 -10.707 -9.854 1.00 20.58 ? 195 TYR A C 1 ATOM 1154 O O . TYR A 1 145 ? 0.965 -11.465 -10.099 1.00 21.16 ? 195 TYR A O 1 ATOM 1155 C CB . TYR A 1 145 ? 3.058 -12.497 -8.457 1.00 16.32 ? 195 TYR A CB 1 ATOM 1156 C CG . TYR A 1 145 ? 4.363 -13.013 -7.864 1.00 15.92 ? 195 TYR A CG 1 ATOM 1157 C CD1 . TYR A 1 145 ? 5.347 -13.591 -8.672 1.00 18.01 ? 195 TYR A CD1 1 ATOM 1158 C CD2 . TYR A 1 145 ? 4.628 -12.890 -6.509 1.00 15.09 ? 195 TYR A CD2 1 ATOM 1159 C CE1 . TYR A 1 145 ? 6.553 -14.048 -8.131 1.00 17.92 ? 195 TYR A CE1 1 ATOM 1160 C CE2 . TYR A 1 145 ? 5.860 -13.277 -5.972 1.00 15.59 ? 195 TYR A CE2 1 ATOM 1161 C CZ . TYR A 1 145 ? 6.807 -13.884 -6.780 1.00 16.50 ? 195 TYR A CZ 1 ATOM 1162 O OH . TYR A 1 145 ? 8.005 -14.288 -6.241 1.00 15.75 ? 195 TYR A OH 1 ATOM 1163 N N . GLN A 1 146 ? 1.820 -9.367 -9.922 1.00 20.15 ? 196 GLN A N 1 ATOM 1164 C CA . GLN A 1 146 ? 0.619 -8.623 -10.298 1.00 20.18 ? 196 GLN A CA 1 ATOM 1165 C C . GLN A 1 146 ? -0.514 -8.594 -9.282 1.00 26.12 ? 196 GLN A C 1 ATOM 1166 O O . GLN A 1 146 ? -1.054 -7.511 -9.011 1.00 25.88 ? 196 GLN A O 1 ATOM 1167 C CB . GLN A 1 146 ? 0.111 -8.987 -11.703 1.00 23.64 ? 196 GLN A CB 1 ATOM 1168 C CG . GLN A 1 146 ? 0.879 -8.264 -12.799 1.00 45.78 ? 196 GLN A CG 1 ATOM 1169 C CD . GLN A 1 146 ? 0.632 -6.773 -12.779 1.00 62.81 ? 196 GLN A CD 1 ATOM 1170 O OE1 . GLN A 1 146 ? -0.503 -6.290 -12.883 1.00 56.20 ? 196 GLN A OE1 1 ATOM 1171 N NE2 . GLN A 1 146 ? 1.699 -6.015 -12.688 1.00 58.28 ? 196 GLN A NE2 1 ATOM 1172 N N . ASN A 1 147 ? -0.925 -9.771 -8.781 1.00 21.37 ? 197 ASN A N 1 ATOM 1173 C CA . ASN A 1 147 ? -2.044 -9.820 -7.849 1.00 23.24 ? 197 ASN A CA 1 ATOM 1174 C C . ASN A 1 147 ? -1.814 -10.712 -6.647 1.00 24.39 ? 197 ASN A C 1 ATOM 1175 O O . ASN A 1 147 ? -0.966 -11.595 -6.655 1.00 20.94 ? 197 ASN A O 1 ATOM 1176 C CB . ASN A 1 147 ? -3.283 -10.347 -8.557 1.00 25.09 ? 197 ASN A CB 1 ATOM 1177 C CG . ASN A 1 147 ? -3.908 -9.369 -9.508 1.00 37.12 ? 197 ASN A CG 1 ATOM 1178 O OD1 . ASN A 1 147 ? -4.546 -8.392 -9.102 1.00 36.67 ? 197 ASN A OD1 1 ATOM 1179 N ND2 . ASN A 1 147 ? -3.779 -9.645 -10.787 1.00 29.68 ? 197 ASN A ND2 1 ATOM 1180 N N . VAL A 1 148 ? -2.589 -10.435 -5.604 1.00 20.86 ? 198 VAL A N 1 ATOM 1181 C CA . VAL A 1 148 ? -2.671 -11.239 -4.390 1.00 21.48 ? 198 VAL A CA 1 ATOM 1182 C C . VAL A 1 148 ? -3.763 -12.285 -4.742 1.00 25.33 ? 198 VAL A C 1 ATOM 1183 O O . VAL A 1 148 ? -4.793 -11.913 -5.302 1.00 27.22 ? 198 VAL A O 1 ATOM 1184 C CB . VAL A 1 148 ? -3.078 -10.312 -3.206 1.00 26.41 ? 198 VAL A CB 1 ATOM 1185 C CG1 . VAL A 1 148 ? -3.579 -11.101 -1.994 1.00 27.46 ? 198 VAL A CG1 1 ATOM 1186 C CG2 . VAL A 1 148 ? -1.913 -9.402 -2.805 1.00 25.58 ? 198 VAL A CG2 1 ATOM 1187 N N . GLY A 1 149 ? -3.512 -13.550 -4.426 1.00 21.62 ? 199 GLY A N 1 ATOM 1188 C CA . GLY A 1 149 ? -4.436 -14.648 -4.676 1.00 22.17 ? 199 GLY A CA 1 ATOM 1189 C C . GLY A 1 149 ? -3.809 -15.585 -5.681 1.00 23.38 ? 199 GLY A C 1 ATOM 1190 O O . GLY A 1 149 ? -4.182 -15.570 -6.858 1.00 26.41 ? 199 GLY A O 1 ATOM 1191 N N . THR A 1 150 ? -2.730 -16.276 -5.256 1.00 15.70 ? 200 THR A N 1 ATOM 1192 C CA . THR A 1 150 ? -1.981 -17.147 -6.156 1.00 12.91 ? 200 THR A CA 1 ATOM 1193 C C . THR A 1 150 ? -1.766 -18.565 -5.601 1.00 15.39 ? 200 THR A C 1 ATOM 1194 O O . THR A 1 150 ? -1.967 -18.826 -4.420 1.00 17.13 ? 200 THR A O 1 ATOM 1195 C CB . THR A 1 150 ? -0.625 -16.508 -6.552 1.00 15.39 ? 200 THR A CB 1 ATOM 1196 O OG1 . THR A 1 150 ? 0.151 -16.387 -5.374 1.00 16.45 ? 200 THR A OG1 1 ATOM 1197 C CG2 . THR A 1 150 ? -0.772 -15.102 -7.201 1.00 12.93 ? 200 THR A CG2 1 ATOM 1198 N N . TYR A 1 151 ? -1.335 -19.446 -6.461 1.00 15.46 ? 201 TYR A N 1 ATOM 1199 C CA . TYR A 1 151 ? -0.990 -20.795 -6.046 1.00 14.64 ? 201 TYR A CA 1 ATOM 1200 C C . TYR A 1 151 ? 0.228 -21.297 -6.805 1.00 13.68 ? 201 TYR A C 1 ATOM 1201 O O . TYR A 1 151 ? 0.490 -20.842 -7.928 1.00 12.74 ? 201 TYR A O 1 ATOM 1202 C CB . TYR A 1 151 ? -2.162 -21.769 -6.134 1.00 14.51 ? 201 TYR A CB 1 ATOM 1203 C CG . TYR A 1 151 ? -2.665 -21.994 -7.544 1.00 16.89 ? 201 TYR A CG 1 ATOM 1204 C CD1 . TYR A 1 151 ? -2.073 -22.941 -8.376 1.00 17.49 ? 201 TYR A CD1 1 ATOM 1205 C CD2 . TYR A 1 151 ? -3.760 -21.290 -8.033 1.00 20.45 ? 201 TYR A CD2 1 ATOM 1206 C CE1 . TYR A 1 151 ? -2.519 -23.133 -9.685 1.00 19.56 ? 201 TYR A CE1 1 ATOM 1207 C CE2 . TYR A 1 151 ? -4.280 -21.555 -9.301 1.00 21.74 ? 201 TYR A CE2 1 ATOM 1208 C CZ . TYR A 1 151 ? -3.626 -22.438 -10.139 1.00 29.75 ? 201 TYR A CZ 1 ATOM 1209 O OH . TYR A 1 151 ? -4.105 -22.670 -11.396 1.00 31.50 ? 201 TYR A OH 1 ATOM 1210 N N . VAL A 1 152 ? 0.821 -22.380 -6.284 1.00 12.63 ? 202 VAL A N 1 ATOM 1211 C CA . VAL A 1 152 ? 1.921 -23.117 -6.953 1.00 13.31 ? 202 VAL A CA 1 ATOM 1212 C C . VAL A 1 152 ? 1.553 -24.587 -6.822 1.00 16.83 ? 202 VAL A C 1 ATOM 1213 O O . VAL A 1 152 ? 1.513 -25.100 -5.683 1.00 19.17 ? 202 VAL A O 1 ATOM 1214 C CB . VAL A 1 152 ? 3.332 -22.845 -6.338 1.00 15.60 ? 202 VAL A CB 1 ATOM 1215 C CG1 . VAL A 1 152 ? 4.418 -23.667 -7.050 1.00 15.17 ? 202 VAL A CG1 1 ATOM 1216 C CG2 . VAL A 1 152 ? 3.672 -21.352 -6.406 1.00 16.31 ? 202 VAL A CG2 1 ATOM 1217 N N . SER A 1 153 ? 1.296 -25.243 -7.954 1.00 13.72 ? 203 SER A N 1 ATOM 1218 C CA . SER A 1 153 ? 0.947 -26.668 -7.987 1.00 13.92 ? 203 SER A CA 1 ATOM 1219 C C . SER A 1 153 ? 2.030 -27.477 -8.647 1.00 16.47 ? 203 SER A C 1 ATOM 1220 O O . SER A 1 153 ? 2.469 -27.144 -9.761 1.00 17.35 ? 203 SER A O 1 ATOM 1221 C CB . SER A 1 153 ? -0.367 -26.878 -8.738 1.00 19.08 ? 203 SER A CB 1 ATOM 1222 O OG . SER A 1 153 ? -1.394 -26.109 -8.151 1.00 32.96 ? 203 SER A OG 1 ATOM 1223 N N . VAL A 1 154 ? 2.463 -28.556 -7.990 1.00 13.27 ? 204 VAL A N 1 ATOM 1224 C CA . VAL A 1 154 ? 3.442 -29.489 -8.593 1.00 11.41 ? 204 VAL A CA 1 ATOM 1225 C C . VAL A 1 154 ? 2.883 -30.883 -8.457 1.00 17.22 ? 204 VAL A C 1 ATOM 1226 O O . VAL A 1 154 ? 2.399 -31.261 -7.395 1.00 17.47 ? 204 VAL A O 1 ATOM 1227 C CB . VAL A 1 154 ? 4.810 -29.394 -7.860 1.00 14.76 ? 204 VAL A CB 1 ATOM 1228 C CG1 . VAL A 1 154 ? 5.851 -30.311 -8.534 1.00 14.35 ? 204 VAL A CG1 1 ATOM 1229 C CG2 . VAL A 1 154 ? 5.333 -27.957 -7.840 1.00 14.97 ? 204 VAL A CG2 1 ATOM 1230 N N . GLY A 1 155 ? 2.925 -31.640 -9.528 1.00 14.28 ? 205 GLY A N 1 ATOM 1231 C CA . GLY A 1 155 ? 2.366 -32.973 -9.472 1.00 13.68 ? 205 GLY A CA 1 ATOM 1232 C C . GLY A 1 155 ? 3.134 -33.979 -10.281 1.00 18.85 ? 205 GLY A C 1 ATOM 1233 O O . GLY A 1 155 ? 3.721 -33.655 -11.310 1.00 18.54 ? 205 GLY A O 1 ATOM 1234 N N . THR A 1 156 ? 3.152 -35.214 -9.789 1.00 15.59 ? 206 THR A N 1 ATOM 1235 C CA . THR A 1 156 ? 3.736 -36.353 -10.478 1.00 14.57 ? 206 THR A CA 1 ATOM 1236 C C . THR A 1 156 ? 2.749 -37.490 -10.150 1.00 19.45 ? 206 THR A C 1 ATOM 1237 O O . THR A 1 156 ? 1.676 -37.253 -9.560 1.00 20.09 ? 206 THR A O 1 ATOM 1238 C CB . THR A 1 156 ? 5.169 -36.735 -9.926 1.00 22.24 ? 206 THR A CB 1 ATOM 1239 O OG1 . THR A 1 156 ? 5.052 -37.337 -8.629 1.00 20.33 ? 206 THR A OG1 1 ATOM 1240 C CG2 . THR A 1 156 ? 6.165 -35.544 -9.860 1.00 19.49 ? 206 THR A CG2 1 ATOM 1241 N N . SER A 1 157 ? 3.117 -38.721 -10.491 1.00 17.56 ? 207 SER A N 1 ATOM 1242 C CA A SER A 1 157 ? 2.246 -39.856 -10.213 0.50 18.19 ? 207 SER A CA 1 ATOM 1243 C CA B SER A 1 157 ? 2.256 -39.870 -10.216 0.50 17.83 ? 207 SER A CA 1 ATOM 1244 C C . SER A 1 157 ? 2.271 -40.187 -8.721 1.00 23.03 ? 207 SER A C 1 ATOM 1245 O O . SER A 1 157 ? 1.401 -40.910 -8.245 1.00 24.47 ? 207 SER A O 1 ATOM 1246 C CB A SER A 1 157 ? 2.649 -41.058 -11.057 0.50 22.38 ? 207 SER A CB 1 ATOM 1247 C CB B SER A 1 157 ? 2.704 -41.084 -11.021 0.50 20.80 ? 207 SER A CB 1 ATOM 1248 O OG A SER A 1 157 ? 2.447 -40.777 -12.433 0.50 27.91 ? 207 SER A OG 1 ATOM 1249 O OG B SER A 1 157 ? 3.897 -41.643 -10.497 0.50 20.94 ? 207 SER A OG 1 ATOM 1250 N N . THR A 1 158 ? 3.285 -39.676 -7.994 1.00 19.26 ? 208 THR A N 1 ATOM 1251 C CA . THR A 1 158 ? 3.406 -39.920 -6.546 1.00 21.05 ? 208 THR A CA 1 ATOM 1252 C C . THR A 1 158 ? 3.329 -38.635 -5.667 1.00 24.40 ? 208 THR A C 1 ATOM 1253 O O . THR A 1 158 ? 3.358 -38.728 -4.444 1.00 25.38 ? 208 THR A O 1 ATOM 1254 C CB . THR A 1 158 ? 4.714 -40.679 -6.259 1.00 26.42 ? 208 THR A CB 1 ATOM 1255 O OG1 . THR A 1 158 ? 5.777 -39.950 -6.857 1.00 29.68 ? 208 THR A OG1 1 ATOM 1256 C CG2 . THR A 1 158 ? 4.695 -42.115 -6.801 1.00 30.61 ? 208 THR A CG2 1 ATOM 1257 N N . LEU A 1 159 ? 3.175 -37.465 -6.286 1.00 18.66 ? 209 LEU A N 1 ATOM 1258 C CA . LEU A 1 159 ? 3.144 -36.189 -5.602 1.00 17.27 ? 209 LEU A CA 1 ATOM 1259 C C . LEU A 1 159 ? 1.971 -35.311 -6.092 1.00 20.16 ? 209 LEU A C 1 ATOM 1260 O O . LEU A 1 159 ? 1.676 -35.293 -7.273 1.00 16.79 ? 209 LEU A O 1 ATOM 1261 C CB . LEU A 1 159 ? 4.453 -35.464 -5.924 1.00 17.16 ? 209 LEU A CB 1 ATOM 1262 C CG . LEU A 1 159 ? 4.606 -34.056 -5.334 1.00 21.33 ? 209 LEU A CG 1 ATOM 1263 C CD1 . LEU A 1 159 ? 5.102 -34.132 -3.922 1.00 24.15 ? 209 LEU A CD1 1 ATOM 1264 C CD2 . LEU A 1 159 ? 5.520 -33.210 -6.194 1.00 22.08 ? 209 LEU A CD2 1 ATOM 1265 N N . ASN A 1 160 ? 1.333 -34.575 -5.179 1.00 18.84 ? 210 ASN A N 1 ATOM 1266 C CA . ASN A 1 160 ? 0.301 -33.615 -5.503 1.00 19.53 ? 210 ASN A CA 1 ATOM 1267 C C . ASN A 1 160 ? 0.405 -32.511 -4.453 1.00 21.39 ? 210 ASN A C 1 ATOM 1268 O O . ASN A 1 160 ? -0.238 -32.611 -3.418 1.00 22.52 ? 210 ASN A O 1 ATOM 1269 C CB . ASN A 1 160 ? -1.079 -34.267 -5.498 1.00 23.26 ? 210 ASN A CB 1 ATOM 1270 C CG . ASN A 1 160 ? -2.220 -33.328 -5.861 1.00 39.31 ? 210 ASN A CG 1 ATOM 1271 O OD1 . ASN A 1 160 ? -2.023 -32.213 -6.358 1.00 29.65 ? 210 ASN A OD1 1 ATOM 1272 N ND2 . ASN A 1 160 ? -3.448 -33.775 -5.647 1.00 35.85 ? 210 ASN A ND2 1 ATOM 1273 N N . LYS A 1 161 ? 1.253 -31.498 -4.694 1.00 17.49 ? 211 LYS A N 1 ATOM 1274 C CA . LYS A 1 161 ? 1.429 -30.436 -3.722 1.00 16.13 ? 211 LYS A CA 1 ATOM 1275 C C . LYS A 1 161 ? 0.927 -29.152 -4.347 1.00 21.11 ? 211 LYS A C 1 ATOM 1276 O O . LYS A 1 161 ? 1.376 -28.778 -5.428 1.00 22.43 ? 211 LYS A O 1 ATOM 1277 C CB . LYS A 1 161 ? 2.902 -30.317 -3.316 1.00 18.47 ? 211 LYS A CB 1 ATOM 1278 C CG . LYS A 1 161 ? 3.102 -29.450 -2.064 1.00 33.48 ? 211 LYS A CG 1 ATOM 1279 C CD . LYS A 1 161 ? 4.486 -29.673 -1.485 1.00 51.52 ? 211 LYS A CD 1 ATOM 1280 C CE . LYS A 1 161 ? 4.738 -28.873 -0.233 1.00 58.05 ? 211 LYS A CE 1 ATOM 1281 N NZ . LYS A 1 161 ? 6.078 -29.182 0.330 1.00 64.33 ? 211 LYS A NZ 1 ATOM 1282 N N . ARG A 1 162 ? -0.031 -28.486 -3.689 1.00 17.07 ? 212 ARG A N 1 ATOM 1283 C CA . ARG A 1 162 ? -0.620 -27.271 -4.223 1.00 16.67 ? 212 ARG A CA 1 ATOM 1284 C C . ARG A 1 162 ? -0.607 -26.241 -3.085 1.00 21.86 ? 212 ARG A C 1 ATOM 1285 O O . ARG A 1 162 ? -1.500 -26.242 -2.220 1.00 25.44 ? 212 ARG A O 1 ATOM 1286 C CB . ARG A 1 162 ? -2.038 -27.556 -4.742 1.00 20.21 ? 212 ARG A CB 1 ATOM 1287 C CG . ARG A 1 162 ? -2.064 -28.659 -5.806 1.00 20.62 ? 212 ARG A CG 1 ATOM 1288 C CD . ARG A 1 162 ? -3.438 -29.004 -6.366 1.00 33.34 ? 212 ARG A CD 1 ATOM 1289 N NE . ARG A 1 162 ? -3.278 -30.036 -7.400 1.00 33.43 ? 212 ARG A NE 1 ATOM 1290 C CZ . ARG A 1 162 ? -3.965 -30.086 -8.534 1.00 40.47 ? 212 ARG A CZ 1 ATOM 1291 N NH1 . ARG A 1 162 ? -4.905 -29.186 -8.789 1.00 35.39 ? 212 ARG A NH1 1 ATOM 1292 N NH2 . ARG A 1 162 ? -3.734 -31.049 -9.414 1.00 26.04 ? 212 ARG A NH2 1 ATOM 1293 N N . SER A 1 163 ? 0.425 -25.373 -3.093 1.00 18.13 ? 213 SER A N 1 ATOM 1294 C CA . SER A 1 163 ? 0.758 -24.388 -2.095 1.00 17.32 ? 213 SER A CA 1 ATOM 1295 C C . SER A 1 163 ? 0.177 -22.994 -2.383 1.00 21.58 ? 213 SER A C 1 ATOM 1296 O O . SER A 1 163 ? -0.090 -22.618 -3.523 1.00 18.72 ? 213 SER A O 1 ATOM 1297 C CB . SER A 1 163 ? 2.278 -24.263 -1.999 1.00 19.19 ? 213 SER A CB 1 ATOM 1298 O OG . SER A 1 163 ? 2.903 -25.530 -1.880 1.00 27.73 ? 213 SER A OG 1 ATOM 1299 N N . THR A 1 164 ? -0.057 -22.279 -1.313 1.00 19.07 ? 214 THR A N 1 ATOM 1300 C CA . THR A 1 164 ? -0.545 -20.917 -1.321 1.00 19.64 ? 214 THR A CA 1 ATOM 1301 C C . THR A 1 164 ? 0.569 -20.102 -0.623 1.00 19.69 ? 214 THR A C 1 ATOM 1302 O O . THR A 1 164 ? 0.983 -20.456 0.475 1.00 20.45 ? 214 THR A O 1 ATOM 1303 C CB . THR A 1 164 ? -1.843 -20.818 -0.492 1.00 30.40 ? 214 THR A CB 1 ATOM 1304 O OG1 . THR A 1 164 ? -1.577 -21.378 0.789 1.00 37.68 ? 214 THR A OG1 1 ATOM 1305 C CG2 . THR A 1 164 ? -3.008 -21.564 -1.139 1.00 34.53 ? 214 THR A CG2 1 ATOM 1306 N N . PRO A 1 165 ? 0.999 -18.988 -1.188 1.00 16.80 ? 215 PRO A N 1 ATOM 1307 C CA . PRO A 1 165 ? 1.995 -18.154 -0.516 1.00 17.39 ? 215 PRO A CA 1 ATOM 1308 C C . PRO A 1 165 ? 1.469 -17.501 0.743 1.00 17.72 ? 215 PRO A C 1 ATOM 1309 O O . PRO A 1 165 ? 0.283 -17.157 0.839 1.00 18.98 ? 215 PRO A O 1 ATOM 1310 C CB . PRO A 1 165 ? 2.305 -17.061 -1.554 1.00 20.17 ? 215 PRO A CB 1 ATOM 1311 C CG . PRO A 1 165 ? 1.803 -17.626 -2.843 1.00 24.61 ? 215 PRO A CG 1 ATOM 1312 C CD . PRO A 1 165 ? 0.569 -18.377 -2.464 1.00 18.44 ? 215 PRO A CD 1 ATOM 1313 N N . GLU A 1 166 ? 2.344 -17.333 1.688 1.00 16.67 ? 216 GLU A N 1 ATOM 1314 C CA . GLU A 1 166 ? 2.021 -16.674 2.971 1.00 16.52 ? 216 GLU A CA 1 ATOM 1315 C C . GLU A 1 166 ? 2.652 -15.280 2.910 1.00 17.38 ? 216 GLU A C 1 ATOM 1316 O O . GLU A 1 166 ? 3.877 -15.144 2.803 1.00 20.12 ? 216 GLU A O 1 ATOM 1317 C CB . GLU A 1 166 ? 2.639 -17.422 4.173 1.00 18.13 ? 216 GLU A CB 1 ATOM 1318 C CG . GLU A 1 166 ? 1.985 -18.750 4.508 1.00 28.67 ? 216 GLU A CG 1 ATOM 1319 C CD . GLU A 1 166 ? 2.916 -19.815 5.051 1.00 51.74 ? 216 GLU A CD 1 ATOM 1320 O OE1 . GLU A 1 166 ? 3.882 -19.479 5.776 1.00 58.41 ? 216 GLU A OE1 1 ATOM 1321 O OE2 . GLU A 1 166 ? 2.678 -21.000 4.735 1.00 48.56 ? 216 GLU A OE2 1 ATOM 1322 N N . ILE A 1 167 ? 1.821 -14.244 2.969 1.00 16.19 ? 217 ILE A N 1 ATOM 1323 C CA . ILE A 1 167 ? 2.350 -12.876 2.923 1.00 15.06 ? 217 ILE A CA 1 ATOM 1324 C C . ILE A 1 167 ? 2.489 -12.395 4.370 1.00 14.83 ? 217 ILE A C 1 ATOM 1325 O O . ILE A 1 167 ? 1.490 -12.296 5.052 1.00 15.29 ? 217 ILE A O 1 ATOM 1326 C CB . ILE A 1 167 ? 1.400 -11.971 2.099 1.00 18.85 ? 217 ILE A CB 1 ATOM 1327 C CG1 . ILE A 1 167 ? 1.331 -12.451 0.618 1.00 19.86 ? 217 ILE A CG1 1 ATOM 1328 C CG2 . ILE A 1 167 ? 1.832 -10.504 2.203 1.00 21.01 ? 217 ILE A CG2 1 ATOM 1329 C CD1 . ILE A 1 167 ? 0.257 -11.803 -0.252 1.00 26.39 ? 217 ILE A CD1 1 ATOM 1330 N N . ALA A 1 168 ? 3.703 -12.095 4.842 1.00 17.35 ? 218 ALA A N 1 ATOM 1331 C CA . ALA A 1 168 ? 3.816 -11.708 6.231 1.00 15.74 ? 218 ALA A CA 1 ATOM 1332 C C . ALA A 1 168 ? 5.064 -10.911 6.459 1.00 17.46 ? 218 ALA A C 1 ATOM 1333 O O . ALA A 1 168 ? 6.101 -11.325 5.969 1.00 15.72 ? 218 ALA A O 1 ATOM 1334 C CB . ALA A 1 168 ? 3.867 -12.952 7.115 1.00 16.82 ? 218 ALA A CB 1 ATOM 1335 N N . THR A 1 169 ? 4.996 -9.880 7.330 1.00 16.81 ? 219 THR A N 1 ATOM 1336 C CA . THR A 1 169 ? 6.192 -9.106 7.668 1.00 19.02 ? 219 THR A CA 1 ATOM 1337 C C . THR A 1 169 ? 7.066 -10.000 8.515 1.00 23.54 ? 219 THR A C 1 ATOM 1338 O O . THR A 1 169 ? 6.577 -10.644 9.447 1.00 24.09 ? 219 THR A O 1 ATOM 1339 C CB . THR A 1 169 ? 5.874 -7.801 8.422 1.00 23.42 ? 219 THR A CB 1 ATOM 1340 O OG1 . THR A 1 169 ? 5.020 -6.989 7.615 1.00 24.71 ? 219 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 169 ? 7.143 -7.009 8.748 1.00 21.37 ? 219 THR A CG2 1 ATOM 1342 N N . ARG A 1 170 ? 8.370 -10.032 8.212 1.00 19.16 ? 220 ARG A N 1 ATOM 1343 C CA . ARG A 1 170 ? 9.276 -10.848 8.995 1.00 18.37 ? 220 ARG A CA 1 ATOM 1344 C C . ARG A 1 170 ? 10.518 -10.036 9.236 1.00 20.47 ? 220 ARG A C 1 ATOM 1345 O O . ARG A 1 170 ? 10.830 -9.164 8.427 1.00 19.55 ? 220 ARG A O 1 ATOM 1346 C CB . ARG A 1 170 ? 9.671 -12.131 8.220 1.00 17.53 ? 220 ARG A CB 1 ATOM 1347 C CG . ARG A 1 170 ? 8.438 -13.013 7.917 1.00 21.90 ? 220 ARG A CG 1 ATOM 1348 C CD . ARG A 1 170 ? 8.769 -14.220 7.064 1.00 25.44 ? 220 ARG A CD 1 ATOM 1349 N NE . ARG A 1 170 ? 7.546 -14.833 6.515 1.00 17.93 ? 220 ARG A NE 1 ATOM 1350 C CZ . ARG A 1 170 ? 6.992 -14.500 5.356 1.00 20.96 ? 220 ARG A CZ 1 ATOM 1351 N NH1 . ARG A 1 170 ? 7.580 -13.612 4.560 1.00 16.52 ? 220 ARG A NH1 1 ATOM 1352 N NH2 . ARG A 1 170 ? 5.878 -15.092 4.956 1.00 19.66 ? 220 ARG A NH2 1 ATOM 1353 N N . PRO A 1 171 ? 11.277 -10.355 10.291 1.00 21.22 ? 221 PRO A N 1 ATOM 1354 C CA . PRO A 1 171 ? 12.586 -9.687 10.459 1.00 21.53 ? 221 PRO A CA 1 ATOM 1355 C C . PRO A 1 171 ? 13.493 -9.927 9.236 1.00 22.70 ? 221 PRO A C 1 ATOM 1356 O O . PRO A 1 171 ? 13.434 -10.990 8.602 1.00 16.74 ? 221 PRO A O 1 ATOM 1357 C CB . PRO A 1 171 ? 13.166 -10.348 11.724 1.00 25.11 ? 221 PRO A CB 1 ATOM 1358 C CG . PRO A 1 171 ? 11.983 -10.961 12.444 1.00 29.79 ? 221 PRO A CG 1 ATOM 1359 C CD . PRO A 1 171 ? 11.074 -11.417 11.306 1.00 23.79 ? 221 PRO A CD 1 ATOM 1360 N N . LYS A 1 172 ? 14.250 -8.898 8.845 1.00 18.69 ? 222 LYS A N 1 ATOM 1361 C CA . LYS A 1 172 ? 15.110 -9.062 7.682 1.00 17.09 ? 222 LYS A CA 1 ATOM 1362 C C . LYS A 1 172 ? 16.192 -10.085 7.947 1.00 19.64 ? 222 LYS A C 1 ATOM 1363 O O . LYS A 1 172 ? 16.797 -10.094 9.016 1.00 20.34 ? 222 LYS A O 1 ATOM 1364 C CB . LYS A 1 172 ? 15.748 -7.741 7.229 1.00 20.77 ? 222 LYS A CB 1 ATOM 1365 C CG . LYS A 1 172 ? 14.750 -6.809 6.529 1.00 30.93 ? 222 LYS A CG 1 ATOM 1366 C CD . LYS A 1 172 ? 15.458 -5.526 6.089 1.00 42.42 ? 222 LYS A CD 1 ATOM 1367 C CE . LYS A 1 172 ? 14.663 -4.688 5.116 1.00 61.25 ? 222 LYS A CE 1 ATOM 1368 N NZ . LYS A 1 172 ? 14.580 -5.302 3.762 1.00 74.09 ? 222 LYS A NZ 1 ATOM 1369 N N . VAL A 1 173 ? 16.382 -10.983 7.004 1.00 15.96 ? 223 VAL A N 1 ATOM 1370 C CA . VAL A 1 173 ? 17.537 -11.909 7.041 1.00 16.15 ? 223 VAL A CA 1 ATOM 1371 C C . VAL A 1 173 ? 18.152 -11.785 5.654 1.00 19.09 ? 223 VAL A C 1 ATOM 1372 O O . VAL A 1 173 ? 17.439 -11.955 4.676 1.00 12.77 ? 223 VAL A O 1 ATOM 1373 C CB . VAL A 1 173 ? 17.156 -13.360 7.360 1.00 20.28 ? 223 VAL A CB 1 ATOM 1374 C CG1 . VAL A 1 173 ? 18.322 -14.334 7.108 1.00 20.28 ? 223 VAL A CG1 1 ATOM 1375 C CG2 . VAL A 1 173 ? 16.663 -13.456 8.784 1.00 19.05 ? 223 VAL A CG2 1 ATOM 1376 N N . ASN A 1 174 ? 19.470 -11.524 5.569 1.00 15.30 ? 224 ASN A N 1 ATOM 1377 C CA . ASN A 1 174 ? 20.120 -11.330 4.252 1.00 16.95 ? 224 ASN A CA 1 ATOM 1378 C C . ASN A 1 174 ? 19.427 -10.215 3.466 1.00 19.38 ? 224 ASN A C 1 ATOM 1379 O O . ASN A 1 174 ? 19.311 -10.291 2.245 1.00 20.04 ? 224 ASN A O 1 ATOM 1380 C CB . ASN A 1 174 ? 20.242 -12.637 3.442 1.00 19.00 ? 224 ASN A CB 1 ATOM 1381 C CG . ASN A 1 174 ? 20.918 -13.752 4.175 1.00 30.86 ? 224 ASN A CG 1 ATOM 1382 O OD1 . ASN A 1 174 ? 21.546 -13.546 5.197 1.00 21.19 ? 224 ASN A OD1 1 ATOM 1383 N ND2 . ASN A 1 174 ? 20.772 -14.976 3.689 1.00 24.36 ? 224 ASN A ND2 1 ATOM 1384 N N . GLY A 1 175 ? 18.960 -9.199 4.195 1.00 17.90 ? 225 GLY A N 1 ATOM 1385 C CA . GLY A 1 175 ? 18.300 -8.022 3.651 1.00 18.88 ? 225 GLY A CA 1 ATOM 1386 C C . GLY A 1 175 ? 16.848 -8.184 3.226 1.00 21.34 ? 225 GLY A C 1 ATOM 1387 O O . GLY A 1 175 ? 16.262 -7.201 2.781 1.00 21.52 ? 225 GLY A O 1 ATOM 1388 N N . GLN A 1 176 ? 16.228 -9.377 3.455 1.00 15.91 ? 226 GLN A N 1 ATOM 1389 C CA . GLN A 1 176 ? 14.867 -9.712 3.022 1.00 13.93 ? 226 GLN A CA 1 ATOM 1390 C C . GLN A 1 176 ? 13.897 -10.170 4.114 1.00 17.88 ? 226 GLN A C 1 ATOM 1391 O O . GLN A 1 176 ? 14.259 -10.961 4.974 1.00 17.05 ? 226 GLN A O 1 ATOM 1392 C CB . GLN A 1 176 ? 14.930 -10.887 2.016 1.00 14.85 ? 226 GLN A CB 1 ATOM 1393 C CG . GLN A 1 176 ? 15.919 -10.722 0.854 1.00 20.61 ? 226 GLN A CG 1 ATOM 1394 C CD . GLN A 1 176 ? 15.625 -9.497 0.001 1.00 29.29 ? 226 GLN A CD 1 ATOM 1395 O OE1 . GLN A 1 176 ? 14.470 -9.110 -0.232 1.00 31.45 ? 226 GLN A OE1 1 ATOM 1396 N NE2 . GLN A 1 176 ? 16.676 -8.841 -0.468 1.00 35.74 ? 226 GLN A NE2 1 ATOM 1397 N N . GLY A 1 177 ? 12.664 -9.664 4.047 1.00 14.49 ? 227 GLY A N 1 ATOM 1398 C CA . GLY A 1 177 ? 11.553 -10.106 4.881 1.00 15.23 ? 227 GLY A CA 1 ATOM 1399 C C . GLY A 1 177 ? 10.783 -11.244 4.191 1.00 16.67 ? 227 GLY A C 1 ATOM 1400 O O . GLY A 1 177 ? 10.065 -12.007 4.827 1.00 15.87 ? 227 GLY A O 1 ATOM 1401 N N . GLY A 1 178 ? 10.922 -11.362 2.875 1.00 16.59 ? 228 GLY A N 1 ATOM 1402 C CA . GLY A 1 178 ? 10.357 -12.494 2.154 1.00 15.99 ? 228 GLY A CA 1 ATOM 1403 C C . GLY A 1 178 ? 11.112 -13.784 2.459 1.00 15.31 ? 228 GLY A C 1 ATOM 1404 O O . GLY A 1 178 ? 12.227 -13.764 2.982 1.00 14.54 ? 228 GLY A O 1 ATOM 1405 N N . ARG A 1 179 ? 10.513 -14.914 2.149 1.00 12.97 ? 229 ARG A N 1 ATOM 1406 C CA . ARG A 1 179 ? 11.199 -16.190 2.358 1.00 10.87 ? 229 ARG A CA 1 ATOM 1407 C C . ARG A 1 179 ? 10.861 -17.109 1.197 1.00 14.59 ? 229 ARG A C 1 ATOM 1408 O O . ARG A 1 179 ? 9.745 -17.052 0.687 1.00 13.30 ? 229 ARG A O 1 ATOM 1409 C CB . ARG A 1 179 ? 10.649 -16.872 3.609 1.00 10.70 ? 229 ARG A CB 1 ATOM 1410 C CG . ARG A 1 179 ? 10.869 -16.146 4.926 1.00 11.26 ? 229 ARG A CG 1 ATOM 1411 C CD . ARG A 1 179 ? 12.329 -16.138 5.326 1.00 14.97 ? 229 ARG A CD 1 ATOM 1412 N NE . ARG A 1 179 ? 12.482 -15.485 6.619 1.00 20.24 ? 229 ARG A NE 1 ATOM 1413 C CZ . ARG A 1 179 ? 12.839 -14.218 6.768 1.00 20.05 ? 229 ARG A CZ 1 ATOM 1414 N NH1 . ARG A 1 179 ? 13.053 -13.448 5.703 1.00 18.67 ? 229 ARG A NH1 1 ATOM 1415 N NH2 . ARG A 1 179 ? 13.020 -13.718 7.976 1.00 18.71 ? 229 ARG A NH2 1 ATOM 1416 N N . MET A 1 180 ? 11.771 -18.023 0.863 1.00 13.68 ? 230 MET A N 1 ATOM 1417 C CA . MET A 1 180 ? 11.495 -19.003 -0.197 1.00 12.95 ? 230 MET A CA 1 ATOM 1418 C C . MET A 1 180 ? 11.482 -20.371 0.468 1.00 18.16 ? 230 MET A C 1 ATOM 1419 O O . MET A 1 180 ? 12.432 -20.706 1.197 1.00 19.24 ? 230 MET A O 1 ATOM 1420 C CB . MET A 1 180 ? 12.549 -18.907 -1.311 1.00 15.19 ? 230 MET A CB 1 ATOM 1421 C CG . MET A 1 180 ? 12.329 -17.669 -2.148 1.00 17.55 ? 230 MET A CG 1 ATOM 1422 S SD . MET A 1 180 ? 13.525 -17.500 -3.456 1.00 20.75 ? 230 MET A SD 1 ATOM 1423 C CE . MET A 1 180 ? 12.915 -15.937 -4.203 1.00 18.34 ? 230 MET A CE 1 ATOM 1424 N N . GLU A 1 181 ? 10.392 -21.123 0.293 1.00 12.79 ? 231 GLU A N 1 ATOM 1425 C CA . GLU A 1 181 ? 10.258 -22.440 0.926 1.00 12.53 ? 231 GLU A CA 1 ATOM 1426 C C . GLU A 1 181 ? 10.474 -23.468 -0.187 1.00 16.56 ? 231 GLU A C 1 ATOM 1427 O O . GLU A 1 181 ? 9.697 -23.541 -1.171 1.00 14.27 ? 231 GLU A O 1 ATOM 1428 C CB . GLU A 1 181 ? 8.863 -22.606 1.484 1.00 14.83 ? 231 GLU A CB 1 ATOM 1429 C CG . GLU A 1 181 ? 8.527 -24.005 1.949 1.00 21.59 ? 231 GLU A CG 1 ATOM 1430 C CD . GLU A 1 181 ? 7.097 -24.172 2.435 1.00 39.60 ? 231 GLU A CD 1 ATOM 1431 O OE1 . GLU A 1 181 ? 6.349 -23.172 2.526 1.00 35.12 ? 231 GLU A OE1 1 ATOM 1432 O OE2 . GLU A 1 181 ? 6.721 -25.326 2.715 1.00 31.03 ? 231 GLU A OE2 1 ATOM 1433 N N . PHE A 1 182 ? 11.514 -24.264 -0.032 1.00 13.26 ? 232 PHE A N 1 ATOM 1434 C CA . PHE A 1 182 ? 11.827 -25.253 -1.069 1.00 11.73 ? 232 PHE A CA 1 ATOM 1435 C C . PHE A 1 182 ? 11.344 -26.629 -0.685 1.00 14.19 ? 232 PHE A C 1 ATOM 1436 O O . PHE A 1 182 ? 11.288 -26.972 0.498 1.00 14.94 ? 232 PHE A O 1 ATOM 1437 C CB . PHE A 1 182 ? 13.363 -25.303 -1.327 1.00 12.85 ? 232 PHE A CB 1 ATOM 1438 C CG . PHE A 1 182 ? 13.863 -24.021 -1.946 1.00 12.39 ? 232 PHE A CG 1 ATOM 1439 C CD1 . PHE A 1 182 ? 13.701 -23.781 -3.304 1.00 12.75 ? 232 PHE A CD1 1 ATOM 1440 C CD2 . PHE A 1 182 ? 14.395 -23.019 -1.153 1.00 14.63 ? 232 PHE A CD2 1 ATOM 1441 C CE1 . PHE A 1 182 ? 14.141 -22.570 -3.881 1.00 15.84 ? 232 PHE A CE1 1 ATOM 1442 C CE2 . PHE A 1 182 ? 14.823 -21.793 -1.715 1.00 17.02 ? 232 PHE A CE2 1 ATOM 1443 C CZ . PHE A 1 182 ? 14.691 -21.581 -3.079 1.00 15.76 ? 232 PHE A CZ 1 ATOM 1444 N N . SER A 1 183 ? 10.978 -27.415 -1.681 1.00 11.45 ? 233 SER A N 1 ATOM 1445 C CA . SER A 1 183 ? 10.531 -28.810 -1.493 1.00 13.75 ? 233 SER A CA 1 ATOM 1446 C C . SER A 1 183 ? 11.224 -29.644 -2.572 1.00 16.38 ? 233 SER A C 1 ATOM 1447 O O . SER A 1 183 ? 11.751 -29.116 -3.558 1.00 14.93 ? 233 SER A O 1 ATOM 1448 C CB . SER A 1 183 ? 9.021 -28.926 -1.651 1.00 17.98 ? 233 SER A CB 1 ATOM 1449 O OG . SER A 1 183 ? 8.345 -28.117 -0.702 1.00 19.83 ? 233 SER A OG 1 ATOM 1450 N N . TRP A 1 184 ? 11.202 -30.952 -2.386 1.00 15.45 ? 234 TRP A N 1 ATOM 1451 C CA . TRP A 1 184 ? 11.869 -31.851 -3.319 1.00 14.97 ? 234 TRP A CA 1 ATOM 1452 C C . TRP A 1 184 ? 11.050 -33.083 -3.545 1.00 16.32 ? 234 TRP A C 1 ATOM 1453 O O . TRP A 1 184 ? 10.179 -33.432 -2.735 1.00 15.19 ? 234 TRP A O 1 ATOM 1454 C CB . TRP A 1 184 ? 13.271 -32.242 -2.817 1.00 14.06 ? 234 TRP A CB 1 ATOM 1455 C CG . TRP A 1 184 ? 13.287 -33.037 -1.546 1.00 15.52 ? 234 TRP A CG 1 ATOM 1456 C CD1 . TRP A 1 184 ? 13.279 -32.547 -0.269 1.00 19.06 ? 234 TRP A CD1 1 ATOM 1457 C CD2 . TRP A 1 184 ? 13.458 -34.453 -1.431 1.00 17.14 ? 234 TRP A CD2 1 ATOM 1458 N NE1 . TRP A 1 184 ? 13.305 -33.582 0.632 1.00 19.95 ? 234 TRP A NE1 1 ATOM 1459 C CE2 . TRP A 1 184 ? 13.454 -34.765 -0.051 1.00 21.87 ? 234 TRP A CE2 1 ATOM 1460 C CE3 . TRP A 1 184 ? 13.531 -35.501 -2.366 1.00 19.15 ? 234 TRP A CE3 1 ATOM 1461 C CZ2 . TRP A 1 184 ? 13.486 -36.077 0.413 1.00 22.70 ? 234 TRP A CZ2 1 ATOM 1462 C CZ3 . TRP A 1 184 ? 13.592 -36.802 -1.903 1.00 21.72 ? 234 TRP A CZ3 1 ATOM 1463 C CH2 . TRP A 1 184 ? 13.618 -37.077 -0.526 1.00 23.19 ? 234 TRP A CH2 1 ATOM 1464 N N . THR A 1 185 ? 11.307 -33.738 -4.681 1.00 13.88 ? 235 THR A N 1 ATOM 1465 C CA . THR A 1 185 ? 10.665 -35.006 -4.985 1.00 14.54 ? 235 THR A CA 1 ATOM 1466 C C . THR A 1 185 ? 11.635 -35.815 -5.816 1.00 15.98 ? 235 THR A C 1 ATOM 1467 O O . THR A 1 185 ? 12.571 -35.294 -6.435 1.00 16.80 ? 235 THR A O 1 ATOM 1468 C CB . THR A 1 185 ? 9.305 -34.778 -5.751 1.00 18.38 ? 235 THR A CB 1 ATOM 1469 O OG1 . THR A 1 185 ? 8.480 -35.947 -5.658 1.00 26.76 ? 235 THR A OG1 1 ATOM 1470 C CG2 . THR A 1 185 ? 9.498 -34.412 -7.219 1.00 17.67 ? 235 THR A CG2 1 ATOM 1471 N N . LEU A 1 186 ? 11.365 -37.075 -5.854 1.00 15.28 ? 236 LEU A N 1 ATOM 1472 C CA . LEU A 1 186 ? 12.073 -38.011 -6.689 1.00 18.92 ? 236 LEU A CA 1 ATOM 1473 C C . LEU A 1 186 ? 11.101 -38.399 -7.802 1.00 22.81 ? 236 LEU A C 1 ATOM 1474 O O . LEU A 1 186 ? 9.992 -38.895 -7.531 1.00 22.06 ? 236 LEU A O 1 ATOM 1475 C CB . LEU A 1 186 ? 12.486 -39.239 -5.863 1.00 21.49 ? 236 LEU A CB 1 ATOM 1476 C CG . LEU A 1 186 ? 13.779 -39.138 -5.062 1.00 28.04 ? 236 LEU A CG 1 ATOM 1477 C CD1 . LEU A 1 186 ? 14.042 -40.456 -4.342 1.00 29.69 ? 236 LEU A CD1 1 ATOM 1478 C CD2 . LEU A 1 186 ? 14.998 -38.828 -5.964 1.00 28.83 ? 236 LEU A CD2 1 ATOM 1479 N N . LEU A 1 187 ? 11.480 -38.068 -9.043 1.00 17.40 ? 237 LEU A N 1 ATOM 1480 C CA . LEU A 1 187 ? 10.660 -38.349 -10.219 1.00 16.30 ? 237 LEU A CA 1 ATOM 1481 C C . LEU A 1 187 ? 11.093 -39.670 -10.819 1.00 19.27 ? 237 LEU A C 1 ATOM 1482 O O . LEU A 1 187 ? 12.237 -39.819 -11.241 1.00 16.48 ? 237 LEU A O 1 ATOM 1483 C CB . LEU A 1 187 ? 10.772 -37.185 -11.259 1.00 16.32 ? 237 LEU A CB 1 ATOM 1484 C CG . LEU A 1 187 ? 9.927 -37.359 -12.540 1.00 18.79 ? 237 LEU A CG 1 ATOM 1485 C CD1 . LEU A 1 187 ? 8.424 -37.266 -12.244 1.00 20.48 ? 237 LEU A CD1 1 ATOM 1486 C CD2 . LEU A 1 187 ? 10.265 -36.298 -13.551 1.00 15.39 ? 237 LEU A CD2 1 ATOM 1487 N N . ASP A 1 188 ? 10.216 -40.668 -10.778 1.00 19.09 ? 238 ASP A N 1 ATOM 1488 C CA . ASP A 1 188 ? 10.573 -41.993 -11.276 1.00 19.58 ? 238 ASP A CA 1 ATOM 1489 C C . ASP A 1 188 ? 10.858 -41.965 -12.778 1.00 20.98 ? 238 ASP A C 1 ATOM 1490 O O . ASP A 1 188 ? 10.391 -41.063 -13.469 1.00 18.44 ? 238 ASP A O 1 ATOM 1491 C CB . ASP A 1 188 ? 9.426 -42.984 -10.981 1.00 22.16 ? 238 ASP A CB 1 ATOM 1492 C CG . ASP A 1 188 ? 9.218 -43.277 -9.510 1.00 45.18 ? 238 ASP A CG 1 ATOM 1493 O OD1 . ASP A 1 188 ? 10.203 -43.206 -8.745 1.00 47.33 ? 238 ASP A OD1 1 ATOM 1494 O OD2 . ASP A 1 188 ? 8.076 -43.627 -9.130 1.00 56.29 ? 238 ASP A OD2 1 ATOM 1495 N N . MET A 1 189 ? 11.558 -42.994 -13.288 1.00 18.71 ? 239 MET A N 1 ATOM 1496 C CA . MET A 1 189 ? 11.792 -43.104 -14.720 1.00 19.27 ? 239 MET A CA 1 ATOM 1497 C C . MET A 1 189 ? 10.432 -43.191 -15.420 1.00 22.65 ? 239 MET A C 1 ATOM 1498 O O . MET A 1 189 ? 9.527 -43.888 -14.933 1.00 23.43 ? 239 MET A O 1 ATOM 1499 C CB . MET A 1 189 ? 12.600 -44.372 -15.031 1.00 22.65 ? 239 MET A CB 1 ATOM 1500 C CG . MET A 1 189 ? 14.045 -44.243 -14.690 1.00 26.83 ? 239 MET A CG 1 ATOM 1501 S SD . MET A 1 189 ? 14.843 -45.852 -14.733 1.00 34.45 ? 239 MET A SD 1 ATOM 1502 C CE . MET A 1 189 ? 14.898 -46.214 -13.022 1.00 32.85 ? 239 MET A CE 1 ATOM 1503 N N . TRP A 1 190 ? 10.282 -42.486 -16.562 1.00 19.09 ? 240 TRP A N 1 ATOM 1504 C CA . TRP A 1 190 ? 9.083 -42.467 -17.416 1.00 20.68 ? 240 TRP A CA 1 ATOM 1505 C C . TRP A 1 190 ? 7.887 -41.715 -16.819 1.00 24.24 ? 240 TRP A C 1 ATOM 1506 O O . TRP A 1 190 ? 6.815 -41.636 -17.463 1.00 25.34 ? 240 TRP A O 1 ATOM 1507 C CB . TRP A 1 190 ? 8.699 -43.890 -17.926 1.00 22.24 ? 240 TRP A CB 1 ATOM 1508 C CG . TRP A 1 190 ? 9.881 -44.758 -18.243 1.00 24.69 ? 240 TRP A CG 1 ATOM 1509 C CD1 . TRP A 1 190 ? 10.251 -45.901 -17.593 1.00 28.15 ? 240 TRP A CD1 1 ATOM 1510 C CD2 . TRP A 1 190 ? 10.946 -44.449 -19.148 1.00 25.20 ? 240 TRP A CD2 1 ATOM 1511 N NE1 . TRP A 1 190 ? 11.440 -46.368 -18.098 1.00 29.03 ? 240 TRP A NE1 1 ATOM 1512 C CE2 . TRP A 1 190 ? 11.886 -45.501 -19.062 1.00 30.77 ? 240 TRP A CE2 1 ATOM 1513 C CE3 . TRP A 1 190 ? 11.154 -43.428 -20.102 1.00 26.98 ? 240 TRP A CE3 1 ATOM 1514 C CZ2 . TRP A 1 190 ? 13.038 -45.546 -19.859 1.00 30.95 ? 240 TRP A CZ2 1 ATOM 1515 C CZ3 . TRP A 1 190 ? 12.298 -43.473 -20.889 1.00 29.61 ? 240 TRP A CZ3 1 ATOM 1516 C CH2 . TRP A 1 190 ? 13.217 -44.528 -20.773 1.00 30.81 ? 240 TRP A CH2 1 ATOM 1517 N N . ASP A 1 191 ? 8.061 -41.150 -15.603 1.00 19.97 ? 241 ASP A N 1 ATOM 1518 C CA . ASP A 1 191 ? 6.997 -40.352 -15.022 1.00 18.91 ? 241 ASP A CA 1 ATOM 1519 C C . ASP A 1 191 ? 7.172 -38.890 -15.443 1.00 22.03 ? 241 ASP A C 1 ATOM 1520 O O . ASP A 1 191 ? 8.282 -38.475 -15.798 1.00 22.06 ? 241 ASP A O 1 ATOM 1521 C CB . ASP A 1 191 ? 6.954 -40.478 -13.490 1.00 20.34 ? 241 ASP A CB 1 ATOM 1522 C CG . ASP A 1 191 ? 5.627 -40.006 -12.898 1.00 26.96 ? 241 ASP A CG 1 ATOM 1523 O OD1 . ASP A 1 191 ? 4.603 -40.012 -13.637 1.00 28.35 ? 241 ASP A OD1 1 ATOM 1524 O OD2 . ASP A 1 191 ? 5.599 -39.666 -11.697 1.00 27.03 ? 241 ASP A OD2 1 ATOM 1525 N N . THR A 1 192 ? 6.089 -38.101 -15.362 1.00 17.35 ? 242 THR A N 1 ATOM 1526 C CA . THR A 1 192 ? 6.097 -36.687 -15.703 1.00 17.05 ? 242 THR A CA 1 ATOM 1527 C C . THR A 1 192 ? 5.820 -35.804 -14.468 1.00 18.82 ? 242 THR A C 1 ATOM 1528 O O . THR A 1 192 ? 4.906 -36.081 -13.677 1.00 19.65 ? 242 THR A O 1 ATOM 1529 C CB . THR A 1 192 ? 5.041 -36.437 -16.835 1.00 26.70 ? 242 THR A CB 1 ATOM 1530 O OG1 . THR A 1 192 ? 5.414 -37.157 -18.011 1.00 26.65 ? 242 THR A OG1 1 ATOM 1531 C CG2 . THR A 1 192 ? 4.848 -34.972 -17.176 1.00 24.02 ? 242 THR A CG2 1 ATOM 1532 N N . ILE A 1 193 ? 6.621 -34.748 -14.300 1.00 14.43 ? 243 ILE A N 1 ATOM 1533 C CA . ILE A 1 193 ? 6.368 -33.735 -13.322 1.00 14.78 ? 243 ILE A CA 1 ATOM 1534 C C . ILE A 1 193 ? 5.647 -32.588 -14.049 1.00 18.45 ? 243 ILE A C 1 ATOM 1535 O O . ILE A 1 193 ? 6.065 -32.213 -15.160 1.00 18.87 ? 243 ILE A O 1 ATOM 1536 C CB . ILE A 1 193 ? 7.658 -33.273 -12.616 1.00 16.95 ? 243 ILE A CB 1 ATOM 1537 C CG1 . ILE A 1 193 ? 7.322 -32.347 -11.409 1.00 18.53 ? 243 ILE A CG1 1 ATOM 1538 C CG2 . ILE A 1 193 ? 8.706 -32.679 -13.587 1.00 16.07 ? 243 ILE A CG2 1 ATOM 1539 C CD1 . ILE A 1 193 ? 8.376 -32.347 -10.356 1.00 19.53 ? 243 ILE A CD1 1 ATOM 1540 N N . ASN A 1 194 ? 4.563 -32.034 -13.440 1.00 16.50 ? 244 ASN A N 1 ATOM 1541 C CA . ASN A 1 194 ? 3.849 -30.908 -14.033 1.00 15.86 ? 244 ASN A CA 1 ATOM 1542 C C . ASN A 1 194 ? 3.839 -29.777 -13.051 1.00 17.82 ? 244 ASN A C 1 ATOM 1543 O O . ASN A 1 194 ? 3.607 -30.005 -11.859 1.00 18.73 ? 244 ASN A O 1 ATOM 1544 C CB . ASN A 1 194 ? 2.387 -31.263 -14.361 1.00 18.11 ? 244 ASN A CB 1 ATOM 1545 C CG . ASN A 1 194 ? 2.269 -32.212 -15.500 1.00 32.08 ? 244 ASN A CG 1 ATOM 1546 O OD1 . ASN A 1 194 ? 2.331 -31.831 -16.666 1.00 36.45 ? 244 ASN A OD1 1 ATOM 1547 N ND2 . ASN A 1 194 ? 2.113 -33.465 -15.179 1.00 27.78 ? 244 ASN A ND2 1 ATOM 1548 N N . PHE A 1 195 ? 4.122 -28.570 -13.540 1.00 13.44 ? 245 PHE A N 1 ATOM 1549 C CA . PHE A 1 195 ? 4.131 -27.350 -12.730 1.00 13.91 ? 245 PHE A CA 1 ATOM 1550 C C . PHE A 1 195 ? 3.080 -26.410 -13.259 1.00 16.34 ? 245 PHE A C 1 ATOM 1551 O O . PHE A 1 195 ? 2.931 -26.288 -14.477 1.00 16.19 ? 245 PHE A O 1 ATOM 1552 C CB . PHE A 1 195 ? 5.474 -26.598 -12.877 1.00 15.69 ? 245 PHE A CB 1 ATOM 1553 C CG . PHE A 1 195 ? 6.640 -27.263 -12.205 1.00 16.85 ? 245 PHE A CG 1 ATOM 1554 C CD1 . PHE A 1 195 ? 6.975 -26.946 -10.901 1.00 20.18 ? 245 PHE A CD1 1 ATOM 1555 C CD2 . PHE A 1 195 ? 7.374 -28.241 -12.864 1.00 17.71 ? 245 PHE A CD2 1 ATOM 1556 C CE1 . PHE A 1 195 ? 8.051 -27.577 -10.272 1.00 22.12 ? 245 PHE A CE1 1 ATOM 1557 C CE2 . PHE A 1 195 ? 8.457 -28.862 -12.239 1.00 20.90 ? 245 PHE A CE2 1 ATOM 1558 C CZ . PHE A 1 195 ? 8.787 -28.522 -10.949 1.00 19.52 ? 245 PHE A CZ 1 ATOM 1559 N N . GLU A 1 196 ? 2.306 -25.794 -12.352 1.00 15.36 ? 246 GLU A N 1 ATOM 1560 C CA . GLU A 1 196 ? 1.307 -24.800 -12.723 1.00 15.35 ? 246 GLU A CA 1 ATOM 1561 C C . GLU A 1 196 ? 1.322 -23.778 -11.637 1.00 18.49 ? 246 GLU A C 1 ATOM 1562 O O . GLU A 1 196 ? 1.205 -24.138 -10.468 1.00 20.60 ? 246 GLU A O 1 ATOM 1563 C CB . GLU A 1 196 ? -0.091 -25.407 -12.812 1.00 16.97 ? 246 GLU A CB 1 ATOM 1564 C CG . GLU A 1 196 ? -1.182 -24.453 -13.280 1.00 24.02 ? 246 GLU A CG 1 ATOM 1565 C CD . GLU A 1 196 ? -2.542 -25.113 -13.433 1.00 45.17 ? 246 GLU A CD 1 ATOM 1566 O OE1 . GLU A 1 196 ? -2.662 -26.050 -14.251 1.00 40.22 ? 246 GLU A OE1 1 ATOM 1567 O OE2 . GLU A 1 196 ? -3.487 -24.701 -12.725 1.00 49.98 ? 246 GLU A OE2 1 ATOM 1568 N N . SER A 1 197 ? 1.358 -22.508 -12.009 1.00 14.42 ? 247 SER A N 1 ATOM 1569 C CA . SER A 1 197 ? 1.348 -21.493 -10.961 1.00 12.83 ? 247 SER A CA 1 ATOM 1570 C C . SER A 1 197 ? 0.803 -20.215 -11.515 1.00 16.29 ? 247 SER A C 1 ATOM 1571 O O . SER A 1 197 ? 1.004 -19.903 -12.685 1.00 18.58 ? 247 SER A O 1 ATOM 1572 C CB . SER A 1 197 ? 2.759 -21.290 -10.410 1.00 16.81 ? 247 SER A CB 1 ATOM 1573 O OG . SER A 1 197 ? 2.835 -20.132 -9.589 1.00 17.46 ? 247 SER A OG 1 ATOM 1574 N N . THR A 1 198 ? 0.073 -19.490 -10.675 1.00 15.23 ? 248 THR A N 1 ATOM 1575 C CA . THR A 1 198 ? -0.450 -18.165 -10.984 1.00 15.62 ? 248 THR A CA 1 ATOM 1576 C C . THR A 1 198 ? 0.399 -17.093 -10.312 1.00 16.61 ? 248 THR A C 1 ATOM 1577 O O . THR A 1 198 ? 0.089 -15.914 -10.404 1.00 16.77 ? 248 THR A O 1 ATOM 1578 C CB . THR A 1 198 ? -1.913 -18.055 -10.597 1.00 17.35 ? 248 THR A CB 1 ATOM 1579 O OG1 . THR A 1 198 ? -2.025 -18.388 -9.211 1.00 18.48 ? 248 THR A OG1 1 ATOM 1580 C CG2 . THR A 1 198 ? -2.814 -18.953 -11.435 1.00 18.46 ? 248 THR A CG2 1 ATOM 1581 N N . GLY A 1 199 ? 1.501 -17.508 -9.694 1.00 14.01 ? 249 GLY A N 1 ATOM 1582 C CA . GLY A 1 199 ? 2.458 -16.613 -9.048 1.00 15.25 ? 249 GLY A CA 1 ATOM 1583 C C . GLY A 1 199 ? 3.199 -17.332 -7.961 1.00 17.74 ? 249 GLY A C 1 ATOM 1584 O O . GLY A 1 199 ? 2.705 -18.337 -7.439 1.00 18.04 ? 249 GLY A O 1 ATOM 1585 N N . ASN A 1 200 ? 4.410 -16.829 -7.638 1.00 13.23 ? 250 ASN A N 1 ATOM 1586 C CA . ASN A 1 200 ? 5.214 -17.260 -6.502 1.00 12.83 ? 250 ASN A CA 1 ATOM 1587 C C . ASN A 1 200 ? 6.029 -18.521 -6.691 1.00 15.17 ? 250 ASN A C 1 ATOM 1588 O O . ASN A 1 200 ? 6.559 -19.023 -5.731 1.00 13.46 ? 250 ASN A O 1 ATOM 1589 C CB . ASN A 1 200 ? 4.393 -17.286 -5.195 1.00 13.68 ? 250 ASN A CB 1 ATOM 1590 C CG . ASN A 1 200 ? 3.677 -15.978 -4.935 1.00 16.11 ? 250 ASN A CG 1 ATOM 1591 O OD1 . ASN A 1 200 ? 2.693 -15.657 -5.613 1.00 15.40 ? 250 ASN A OD1 1 ATOM 1592 N ND2 . ASN A 1 200 ? 4.108 -15.243 -3.898 1.00 12.64 ? 250 ASN A ND2 1 ATOM 1593 N N . LEU A 1 201 ? 6.109 -19.032 -7.925 1.00 15.11 ? 251 LEU A N 1 ATOM 1594 C CA . LEU A 1 201 ? 6.854 -20.246 -8.211 1.00 13.16 ? 251 LEU A CA 1 ATOM 1595 C C . LEU A 1 201 ? 8.312 -19.874 -8.465 1.00 13.96 ? 251 LEU A C 1 ATOM 1596 O O . LEU A 1 201 ? 8.616 -19.019 -9.315 1.00 13.82 ? 251 LEU A O 1 ATOM 1597 C CB . LEU A 1 201 ? 6.293 -20.878 -9.479 1.00 12.62 ? 251 LEU A CB 1 ATOM 1598 C CG . LEU A 1 201 ? 7.133 -21.987 -10.128 1.00 16.19 ? 251 LEU A CG 1 ATOM 1599 C CD1 . LEU A 1 201 ? 7.354 -23.171 -9.136 1.00 14.21 ? 251 LEU A CD1 1 ATOM 1600 C CD2 . LEU A 1 201 ? 6.463 -22.478 -11.367 1.00 18.98 ? 251 LEU A CD2 1 ATOM 1601 N N . ILE A 1 202 ? 9.197 -20.617 -7.788 1.00 11.51 ? 252 ILE A N 1 ATOM 1602 C CA . ILE A 1 202 ? 10.648 -20.620 -8.024 1.00 12.44 ? 252 ILE A CA 1 ATOM 1603 C C . ILE A 1 202 ? 10.884 -21.964 -8.712 1.00 15.67 ? 252 ILE A C 1 ATOM 1604 O O . ILE A 1 202 ? 10.830 -22.996 -8.067 1.00 15.54 ? 252 ILE A O 1 ATOM 1605 C CB . ILE A 1 202 ? 11.472 -20.488 -6.739 1.00 14.15 ? 252 ILE A CB 1 ATOM 1606 C CG1 . ILE A 1 202 ? 11.052 -19.209 -5.909 1.00 14.10 ? 252 ILE A CG1 1 ATOM 1607 C CG2 . ILE A 1 202 ? 12.975 -20.484 -7.122 1.00 15.96 ? 252 ILE A CG2 1 ATOM 1608 C CD1 . ILE A 1 202 ? 10.984 -17.890 -6.698 1.00 15.19 ? 252 ILE A CD1 1 ATOM 1609 N N . ALA A 1 203 ? 10.951 -21.950 -10.018 1.00 13.20 ? 253 ALA A N 1 ATOM 1610 C CA . ALA A 1 203 ? 11.055 -23.166 -10.804 1.00 13.27 ? 253 ALA A CA 1 ATOM 1611 C C . ALA A 1 203 ? 12.472 -23.692 -10.873 1.00 16.10 ? 253 ALA A C 1 ATOM 1612 O O . ALA A 1 203 ? 13.400 -22.892 -11.033 1.00 15.39 ? 253 ALA A O 1 ATOM 1613 C CB . ALA A 1 203 ? 10.546 -22.905 -12.235 1.00 16.03 ? 253 ALA A CB 1 ATOM 1614 N N . PRO A 1 204 ? 12.668 -25.021 -10.951 1.00 13.63 ? 254 PRO A N 1 ATOM 1615 C CA . PRO A 1 204 ? 14.020 -25.517 -11.207 1.00 14.05 ? 254 PRO A CA 1 ATOM 1616 C C . PRO A 1 204 ? 14.275 -25.339 -12.704 1.00 18.12 ? 254 PRO A C 1 ATOM 1617 O O . PRO A 1 204 ? 13.329 -25.436 -13.514 1.00 16.58 ? 254 PRO A O 1 ATOM 1618 C CB . PRO A 1 204 ? 13.914 -27.036 -10.905 1.00 15.52 ? 254 PRO A CB 1 ATOM 1619 C CG . PRO A 1 204 ? 12.479 -27.395 -11.181 1.00 19.01 ? 254 PRO A CG 1 ATOM 1620 C CD . PRO A 1 204 ? 11.689 -26.134 -10.794 1.00 15.69 ? 254 PRO A CD 1 ATOM 1621 N N . GLU A 1 205 ? 15.540 -25.125 -13.080 1.00 15.55 ? 255 GLU A N 1 ATOM 1622 C CA . GLU A 1 205 ? 15.879 -25.226 -14.507 1.00 15.54 ? 255 GLU A CA 1 ATOM 1623 C C . GLU A 1 205 ? 16.490 -26.652 -14.737 1.00 17.52 ? 255 GLU A C 1 ATOM 1624 O O . GLU A 1 205 ? 16.455 -27.187 -15.833 1.00 16.87 ? 255 GLU A O 1 ATOM 1625 C CB . GLU A 1 205 ? 16.882 -24.147 -14.915 1.00 18.00 ? 255 GLU A CB 1 ATOM 1626 C CG . GLU A 1 205 ? 17.128 -24.173 -16.417 1.00 28.53 ? 255 GLU A CG 1 ATOM 1627 C CD . GLU A 1 205 ? 17.955 -23.059 -17.008 1.00 43.15 ? 255 GLU A CD 1 ATOM 1628 O OE1 . GLU A 1 205 ? 18.585 -22.309 -16.228 1.00 30.13 ? 255 GLU A OE1 1 ATOM 1629 O OE2 . GLU A 1 205 ? 17.930 -22.907 -18.252 1.00 37.37 ? 255 GLU A OE2 1 ATOM 1630 N N . TYR A 1 206 ? 17.037 -27.248 -13.688 1.00 15.50 ? 256 TYR A N 1 ATOM 1631 C CA . TYR A 1 206 ? 17.686 -28.544 -13.774 1.00 14.75 ? 256 TYR A CA 1 ATOM 1632 C C . TYR A 1 206 ? 17.101 -29.503 -12.792 1.00 17.84 ? 256 TYR A C 1 ATOM 1633 O O . TYR A 1 206 ? 16.570 -29.103 -11.738 1.00 17.50 ? 256 TYR A O 1 ATOM 1634 C CB . TYR A 1 206 ? 19.224 -28.406 -13.452 1.00 14.68 ? 256 TYR A CB 1 ATOM 1635 C CG . TYR A 1 206 ? 19.989 -27.532 -14.410 1.00 19.60 ? 256 TYR A CG 1 ATOM 1636 C CD1 . TYR A 1 206 ? 20.577 -28.069 -15.555 1.00 22.16 ? 256 TYR A CD1 1 ATOM 1637 C CD2 . TYR A 1 206 ? 20.170 -26.175 -14.151 1.00 22.69 ? 256 TYR A CD2 1 ATOM 1638 C CE1 . TYR A 1 206 ? 21.296 -27.270 -16.439 1.00 27.02 ? 256 TYR A CE1 1 ATOM 1639 C CE2 . TYR A 1 206 ? 20.877 -25.358 -15.039 1.00 24.69 ? 256 TYR A CE2 1 ATOM 1640 C CZ . TYR A 1 206 ? 21.453 -25.917 -16.169 1.00 35.04 ? 256 TYR A CZ 1 ATOM 1641 O OH . TYR A 1 206 ? 22.163 -25.132 -17.043 1.00 38.91 ? 256 TYR A OH 1 ATOM 1642 N N . GLY A 1 207 ? 17.281 -30.775 -13.120 1.00 16.72 ? 257 GLY A N 1 ATOM 1643 C CA . GLY A 1 207 ? 17.011 -31.909 -12.241 1.00 17.63 ? 257 GLY A CA 1 ATOM 1644 C C . GLY A 1 207 ? 18.313 -32.670 -12.086 1.00 19.25 ? 257 GLY A C 1 ATOM 1645 O O . GLY A 1 207 ? 19.217 -32.528 -12.900 1.00 18.12 ? 257 GLY A O 1 ATOM 1646 N N . PHE A 1 208 ? 18.418 -33.482 -11.051 1.00 14.97 ? 258 PHE A N 1 ATOM 1647 C CA . PHE A 1 208 ? 19.648 -34.203 -10.783 1.00 14.21 ? 258 PHE A CA 1 ATOM 1648 C C . PHE A 1 208 ? 19.338 -35.689 -10.964 1.00 16.50 ? 258 PHE A C 1 ATOM 1649 O O . PHE A 1 208 ? 18.745 -36.315 -10.089 1.00 16.00 ? 258 PHE A O 1 ATOM 1650 C CB . PHE A 1 208 ? 20.108 -33.919 -9.342 1.00 14.12 ? 258 PHE A CB 1 ATOM 1651 C CG . PHE A 1 208 ? 20.558 -32.503 -9.111 1.00 16.05 ? 258 PHE A CG 1 ATOM 1652 C CD1 . PHE A 1 208 ? 21.910 -32.181 -9.109 1.00 19.50 ? 258 PHE A CD1 1 ATOM 1653 C CD2 . PHE A 1 208 ? 19.628 -31.470 -8.961 1.00 18.65 ? 258 PHE A CD2 1 ATOM 1654 C CE1 . PHE A 1 208 ? 22.333 -30.860 -8.918 1.00 21.18 ? 258 PHE A CE1 1 ATOM 1655 C CE2 . PHE A 1 208 ? 20.057 -30.149 -8.764 1.00 21.56 ? 258 PHE A CE2 1 ATOM 1656 C CZ . PHE A 1 208 ? 21.402 -29.865 -8.734 1.00 20.40 ? 258 PHE A CZ 1 ATOM 1657 N N . LYS A 1 209 ? 19.765 -36.233 -12.093 1.00 14.11 ? 259 LYS A N 1 ATOM 1658 C CA . LYS A 1 209 ? 19.621 -37.664 -12.382 1.00 14.62 ? 259 LYS A CA 1 ATOM 1659 C C . LYS A 1 209 ? 20.584 -38.439 -11.477 1.00 18.47 ? 259 LYS A C 1 ATOM 1660 O O . LYS A 1 209 ? 21.753 -38.092 -11.350 1.00 21.36 ? 259 LYS A O 1 ATOM 1661 C CB . LYS A 1 209 ? 19.901 -37.930 -13.885 1.00 18.65 ? 259 LYS A CB 1 ATOM 1662 C CG . LYS A 1 209 ? 20.011 -39.406 -14.231 1.00 27.11 ? 259 LYS A CG 1 ATOM 1663 C CD . LYS A 1 209 ? 20.555 -39.602 -15.627 1.00 29.28 ? 259 LYS A CD 1 ATOM 1664 C CE . LYS A 1 209 ? 21.413 -40.839 -15.713 1.00 39.31 ? 259 LYS A CE 1 ATOM 1665 N NZ . LYS A 1 209 ? 21.764 -41.166 -17.131 1.00 46.75 ? 259 LYS A NZ 1 ATOM 1666 N N . ILE A 1 210 ? 20.082 -39.425 -10.778 1.00 17.67 ? 260 ILE A N 1 ATOM 1667 C CA . ILE A 1 210 ? 20.914 -40.250 -9.902 1.00 17.61 ? 260 ILE A CA 1 ATOM 1668 C C . ILE A 1 210 ? 21.706 -41.208 -10.820 1.00 23.62 ? 260 ILE A C 1 ATOM 1669 O O . ILE A 1 210 ? 21.145 -42.180 -11.328 1.00 23.54 ? 260 ILE A O 1 ATOM 1670 C CB . ILE A 1 210 ? 20.042 -40.971 -8.853 1.00 20.33 ? 260 ILE A CB 1 ATOM 1671 C CG1 . ILE A 1 210 ? 19.283 -39.951 -7.984 1.00 20.77 ? 260 ILE A CG1 1 ATOM 1672 C CG2 . ILE A 1 210 ? 20.866 -41.982 -8.025 1.00 22.22 ? 260 ILE A CG2 1 ATOM 1673 C CD1 . ILE A 1 210 ? 18.180 -40.609 -7.034 1.00 29.41 ? 260 ILE A CD1 1 ATOM 1674 N N . SER A 1 211 ? 22.977 -40.880 -11.092 1.00 20.71 ? 261 SER A N 1 ATOM 1675 C CA . SER A 1 211 ? 23.775 -41.673 -12.035 1.00 22.02 ? 261 SER A CA 1 ATOM 1676 C C . SER A 1 211 ? 24.554 -42.803 -11.386 1.00 24.80 ? 261 SER A C 1 ATOM 1677 O O . SER A 1 211 ? 24.938 -43.748 -12.068 1.00 28.12 ? 261 SER A O 1 ATOM 1678 C CB . SER A 1 211 ? 24.693 -40.773 -12.855 1.00 27.31 ? 261 SER A CB 1 ATOM 1679 O OG . SER A 1 211 ? 25.513 -40.004 -11.992 1.00 41.21 ? 261 SER A OG 1 ATOM 1680 N N . LYS A 1 212 ? 24.821 -42.706 -10.078 1.00 20.11 ? 262 LYS A N 1 ATOM 1681 C CA . LYS A 1 212 ? 25.509 -43.769 -9.382 1.00 20.00 ? 262 LYS A CA 1 ATOM 1682 C C . LYS A 1 212 ? 24.920 -43.907 -8.018 1.00 21.00 ? 262 LYS A C 1 ATOM 1683 O O . LYS A 1 212 ? 24.585 -42.901 -7.378 1.00 19.99 ? 262 LYS A O 1 ATOM 1684 C CB . LYS A 1 212 ? 27.036 -43.573 -9.371 1.00 22.43 ? 262 LYS A CB 1 ATOM 1685 C CG . LYS A 1 212 ? 27.809 -44.838 -8.974 1.00 40.80 ? 262 LYS A CG 1 ATOM 1686 C CD . LYS A 1 212 ? 28.978 -45.092 -9.918 1.00 54.91 ? 262 LYS A CD 1 ATOM 1687 C CE . LYS A 1 212 ? 29.633 -46.440 -9.713 1.00 69.40 ? 262 LYS A CE 1 ATOM 1688 N NZ . LYS A 1 212 ? 29.310 -47.393 -10.813 1.00 74.08 ? 262 LYS A NZ 1 ATOM 1689 N N . ARG A 1 213 ? 24.665 -45.160 -7.630 1.00 21.49 ? 263 ARG A N 1 ATOM 1690 C CA . ARG A 1 213 ? 24.109 -45.489 -6.318 1.00 23.19 ? 263 ARG A CA 1 ATOM 1691 C C . ARG A 1 213 ? 25.134 -46.302 -5.567 1.00 28.75 ? 263 ARG A C 1 ATOM 1692 O O . ARG A 1 213 ? 25.876 -47.061 -6.185 1.00 29.71 ? 263 ARG A O 1 ATOM 1693 C CB . ARG A 1 213 ? 22.805 -46.290 -6.440 1.00 25.08 ? 263 ARG A CB 1 ATOM 1694 C CG . ARG A 1 213 ? 21.609 -45.473 -6.896 1.00 31.65 ? 263 ARG A CG 1 ATOM 1695 C CD . ARG A 1 213 ? 20.374 -46.342 -7.022 1.00 39.66 ? 263 ARG A CD 1 ATOM 1696 N NE . ARG A 1 213 ? 19.320 -45.690 -7.807 1.00 39.89 ? 263 ARG A NE 1 ATOM 1697 C CZ . ARG A 1 213 ? 18.383 -44.897 -7.302 1.00 45.98 ? 263 ARG A CZ 1 ATOM 1698 N NH1 . ARG A 1 213 ? 18.357 -44.633 -5.998 1.00 33.38 ? 263 ARG A NH1 1 ATOM 1699 N NH2 . ARG A 1 213 ? 17.462 -44.361 -8.094 1.00 28.79 ? 263 ARG A NH2 1 ATOM 1700 N N . GLY A 1 214 A 25.142 -46.183 -4.247 1.00 25.82 ? 263 GLY A N 1 ATOM 1701 C CA . GLY A 1 214 A 26.071 -46.952 -3.426 1.00 27.66 ? 263 GLY A CA 1 ATOM 1702 C C . GLY A 1 214 A 26.057 -46.554 -1.971 1.00 34.53 ? 263 GLY A C 1 ATOM 1703 O O . GLY A 1 214 A 25.554 -45.487 -1.613 1.00 33.54 ? 263 GLY A O 1 ATOM 1704 N N . SER A 1 215 ? 26.634 -47.397 -1.124 1.00 35.12 ? 264 SER A N 1 ATOM 1705 C CA . SER A 1 215 ? 26.679 -47.098 0.295 1.00 35.61 ? 264 SER A CA 1 ATOM 1706 C C . SER A 1 215 ? 28.001 -46.466 0.706 1.00 38.65 ? 264 SER A C 1 ATOM 1707 O O . SER A 1 215 ? 29.042 -46.757 0.127 1.00 38.96 ? 264 SER A O 1 ATOM 1708 C CB . SER A 1 215 ? 26.378 -48.344 1.132 1.00 41.17 ? 264 SER A CB 1 ATOM 1709 O OG . SER A 1 215 ? 27.445 -49.276 1.096 1.00 54.57 ? 264 SER A OG 1 ATOM 1710 N N . SER A 1 216 ? 27.897 -45.553 1.682 1.00 36.91 ? 265 SER A N 1 ATOM 1711 C CA . SER A 1 216 ? 28.841 -44.784 2.507 1.00 38.94 ? 265 SER A CA 1 ATOM 1712 C C . SER A 1 216 ? 28.145 -43.557 3.059 1.00 45.41 ? 265 SER A C 1 ATOM 1713 O O . SER A 1 216 ? 27.707 -43.631 4.205 1.00 47.73 ? 265 SER A O 1 ATOM 1714 C CB . SER A 1 216 ? 30.212 -44.551 1.893 1.00 44.24 ? 265 SER A CB 1 ATOM 1715 O OG . SER A 1 216 ? 31.185 -45.145 2.744 1.00 53.81 ? 265 SER A OG 1 ATOM 1716 N N . GLY A 1 217 ? 27.882 -42.521 2.254 1.00 40.84 ? 266 GLY A N 1 ATOM 1717 C CA . GLY A 1 217 ? 27.039 -41.445 2.778 1.00 39.53 ? 266 GLY A CA 1 ATOM 1718 C C . GLY A 1 217 ? 27.411 -39.991 2.902 1.00 43.94 ? 266 GLY A C 1 ATOM 1719 O O . GLY A 1 217 ? 27.803 -39.346 1.932 1.00 37.68 ? 266 GLY A O 1 ATOM 1720 N N . ILE A 1 218 ? 27.053 -39.430 4.068 1.00 46.50 ? 267 ILE A N 1 ATOM 1721 C CA . ILE A 1 218 ? 27.305 -38.040 4.447 1.00 47.29 ? 267 ILE A CA 1 ATOM 1722 C C . ILE A 1 218 ? 27.905 -38.010 5.846 1.00 53.26 ? 267 ILE A C 1 ATOM 1723 O O . ILE A 1 218 ? 27.276 -38.479 6.797 1.00 53.44 ? 267 ILE A O 1 ATOM 1724 C CB . ILE A 1 218 ? 26.076 -37.076 4.346 1.00 51.10 ? 267 ILE A CB 1 ATOM 1725 C CG1 . ILE A 1 218 ? 25.263 -37.243 3.036 1.00 51.28 ? 267 ILE A CG1 1 ATOM 1726 C CG2 . ILE A 1 218 ? 26.528 -35.606 4.547 1.00 53.07 ? 267 ILE A CG2 1 ATOM 1727 C CD1 . ILE A 1 218 ? 24.139 -36.145 2.820 1.00 59.43 ? 267 ILE A CD1 1 ATOM 1728 N N . MET A 1 219 ? 29.122 -37.473 5.961 1.00 50.79 ? 268 MET A N 1 ATOM 1729 C CA . MET A 1 219 ? 29.821 -37.268 7.225 1.00 76.90 ? 268 MET A CA 1 ATOM 1730 C C . MET A 1 219 ? 29.397 -35.883 7.718 1.00 89.05 ? 268 MET A C 1 ATOM 1731 O O . MET A 1 219 ? 29.236 -34.962 6.912 1.00 44.04 ? 268 MET A O 1 ATOM 1732 C CB . MET A 1 219 ? 31.345 -37.292 7.023 1.00 79.67 ? 268 MET A CB 1 ATOM 1733 C CG . MET A 1 219 ? 31.922 -38.667 6.852 1.00 83.93 ? 268 MET A CG 1 ATOM 1734 S SD . MET A 1 219 ? 33.164 -39.121 8.096 1.00 89.49 ? 268 MET A SD 1 ATOM 1735 C CE . MET A 1 219 ? 34.575 -38.152 7.529 1.00 86.09 ? 268 MET A CE 1 ATOM 1736 N N . GLY B 1 1 ? 41.410 -37.682 17.596 1.00 32.78 ? 55 GLY B N 1 ATOM 1737 C CA . GLY B 1 1 ? 40.217 -37.526 18.421 1.00 31.22 ? 55 GLY B CA 1 ATOM 1738 C C . GLY B 1 1 ? 39.521 -38.846 18.701 1.00 31.20 ? 55 GLY B C 1 ATOM 1739 O O . GLY B 1 1 ? 40.146 -39.919 18.645 1.00 30.36 ? 55 GLY B O 1 ATOM 1740 N N . ILE B 1 2 ? 38.215 -38.767 19.003 1.00 25.90 ? 56 ILE B N 1 ATOM 1741 C CA . ILE B 1 2 ? 37.374 -39.939 19.280 1.00 23.48 ? 56 ILE B CA 1 ATOM 1742 C C . ILE B 1 2 ? 37.386 -40.867 18.066 1.00 25.87 ? 56 ILE B C 1 ATOM 1743 O O . ILE B 1 2 ? 37.142 -40.414 16.946 1.00 25.61 ? 56 ILE B O 1 ATOM 1744 C CB . ILE B 1 2 ? 35.940 -39.538 19.713 1.00 26.28 ? 56 ILE B CB 1 ATOM 1745 C CG1 . ILE B 1 2 ? 35.964 -38.837 21.095 1.00 27.62 ? 56 ILE B CG1 1 ATOM 1746 C CG2 . ILE B 1 2 ? 34.980 -40.759 19.739 1.00 26.31 ? 56 ILE B CG2 1 ATOM 1747 C CD1 . ILE B 1 2 ? 34.920 -37.728 21.215 1.00 41.23 ? 56 ILE B CD1 1 ATOM 1748 N N . PRO B 1 3 ? 37.674 -42.162 18.265 1.00 22.16 ? 57 PRO B N 1 ATOM 1749 C CA . PRO B 1 3 ? 37.712 -43.076 17.120 1.00 21.83 ? 57 PRO B CA 1 ATOM 1750 C C . PRO B 1 3 ? 36.328 -43.514 16.595 1.00 22.90 ? 57 PRO B C 1 ATOM 1751 O O . PRO B 1 3 ? 35.337 -43.529 17.338 1.00 21.45 ? 57 PRO B O 1 ATOM 1752 C CB . PRO B 1 3 ? 38.482 -44.282 17.678 1.00 23.92 ? 57 PRO B CB 1 ATOM 1753 C CG . PRO B 1 3 ? 38.157 -44.294 19.116 1.00 28.10 ? 57 PRO B CG 1 ATOM 1754 C CD . PRO B 1 3 ? 38.013 -42.860 19.529 1.00 24.39 ? 57 PRO B CD 1 ATOM 1755 N N . PRO B 1 4 ? 36.275 -43.993 15.334 1.00 21.95 ? 58 PRO B N 1 ATOM 1756 C CA . PRO B 1 4 ? 35.005 -44.520 14.809 1.00 22.87 ? 58 PRO B CA 1 ATOM 1757 C C . PRO B 1 4 ? 34.671 -45.859 15.456 1.00 26.38 ? 58 PRO B C 1 ATOM 1758 O O . PRO B 1 4 ? 35.545 -46.479 16.095 1.00 26.60 ? 58 PRO B O 1 ATOM 1759 C CB . PRO B 1 4 ? 35.301 -44.764 13.319 1.00 25.57 ? 58 PRO B CB 1 ATOM 1760 C CG . PRO B 1 4 ? 36.606 -44.000 13.036 1.00 29.72 ? 58 PRO B CG 1 ATOM 1761 C CD . PRO B 1 4 ? 37.354 -44.063 14.318 1.00 24.60 ? 58 PRO B CD 1 ATOM 1762 N N . LEU B 1 5 ? 33.400 -46.286 15.303 1.00 20.51 ? 59 LEU B N 1 ATOM 1763 C CA . LEU B 1 5 ? 32.945 -47.597 15.732 1.00 19.11 ? 59 LEU B CA 1 ATOM 1764 C C . LEU B 1 5 ? 32.977 -48.439 14.451 1.00 23.09 ? 59 LEU B C 1 ATOM 1765 O O . LEU B 1 5 ? 32.209 -48.164 13.530 1.00 23.02 ? 59 LEU B O 1 ATOM 1766 C CB . LEU B 1 5 ? 31.507 -47.561 16.315 1.00 19.83 ? 59 LEU B CB 1 ATOM 1767 C CG . LEU B 1 5 ? 30.867 -48.925 16.614 1.00 24.47 ? 59 LEU B CG 1 ATOM 1768 C CD1 . LEU B 1 5 ? 31.678 -49.700 17.658 1.00 25.61 ? 59 LEU B CD1 1 ATOM 1769 C CD2 . LEU B 1 5 ? 29.410 -48.779 17.079 1.00 25.04 ? 59 LEU B CD2 1 ATOM 1770 N N . GLU B 1 6 ? 33.916 -49.391 14.353 1.00 18.75 ? 60 GLU B N 1 ATOM 1771 C CA . GLU B 1 6 ? 34.048 -50.218 13.149 1.00 17.77 ? 60 GLU B CA 1 ATOM 1772 C C . GLU B 1 6 ? 33.286 -51.499 13.442 1.00 21.51 ? 60 GLU B C 1 ATOM 1773 O O . GLU B 1 6 ? 33.624 -52.220 14.384 1.00 21.80 ? 60 GLU B O 1 ATOM 1774 C CB . GLU B 1 6 ? 35.542 -50.473 12.861 1.00 20.23 ? 60 GLU B CB 1 ATOM 1775 C CG . GLU B 1 6 ? 35.845 -51.592 11.872 1.00 31.93 ? 60 GLU B CG 1 ATOM 1776 C CD . GLU B 1 6 ? 35.405 -51.357 10.444 1.00 53.08 ? 60 GLU B CD 1 ATOM 1777 O OE1 . GLU B 1 6 ? 36.052 -50.545 9.744 1.00 60.39 ? 60 GLU B OE1 1 ATOM 1778 O OE2 . GLU B 1 6 ? 34.423 -52.009 10.019 1.00 44.49 ? 60 GLU B OE2 1 ATOM 1779 N N . LEU B 1 7 ? 32.225 -51.767 12.678 1.00 19.89 ? 61 LEU B N 1 ATOM 1780 C CA . LEU B 1 7 ? 31.413 -52.947 12.931 1.00 19.12 ? 61 LEU B CA 1 ATOM 1781 C C . LEU B 1 7 ? 31.996 -54.233 12.374 1.00 23.83 ? 61 LEU B C 1 ATOM 1782 O O . LEU B 1 7 ? 31.492 -55.300 12.705 1.00 21.80 ? 61 LEU B O 1 ATOM 1783 C CB . LEU B 1 7 ? 29.979 -52.796 12.441 1.00 19.21 ? 61 LEU B CB 1 ATOM 1784 C CG . LEU B 1 7 ? 29.166 -51.633 12.986 1.00 23.95 ? 61 LEU B CG 1 ATOM 1785 C CD1 . LEU B 1 7 ? 27.881 -51.543 12.224 1.00 24.69 ? 61 LEU B CD1 1 ATOM 1786 C CD2 . LEU B 1 7 ? 28.924 -51.748 14.512 1.00 23.36 ? 61 LEU B CD2 1 ATOM 1787 N N . GLY B 1 8 ? 33.050 -54.153 11.572 1.00 22.81 ? 62 GLY B N 1 ATOM 1788 C CA . GLY B 1 8 ? 33.620 -55.374 11.010 1.00 22.44 ? 62 GLY B CA 1 ATOM 1789 C C . GLY B 1 8 ? 32.598 -56.062 10.134 1.00 27.24 ? 62 GLY B C 1 ATOM 1790 O O . GLY B 1 8 ? 31.961 -55.419 9.300 1.00 27.36 ? 62 GLY B O 1 ATOM 1791 N N . ASP B 1 9 ? 32.379 -57.340 10.387 1.00 23.89 ? 63 ASP B N 1 ATOM 1792 C CA . ASP B 1 9 ? 31.439 -58.181 9.646 1.00 23.53 ? 63 ASP B CA 1 ATOM 1793 C C . ASP B 1 9 ? 30.021 -58.096 10.229 1.00 25.10 ? 63 ASP B C 1 ATOM 1794 O O . ASP B 1 9 ? 29.114 -58.759 9.726 1.00 23.80 ? 63 ASP B O 1 ATOM 1795 C CB . ASP B 1 9 ? 31.936 -59.647 9.712 1.00 26.22 ? 63 ASP B CB 1 ATOM 1796 C CG . ASP B 1 9 ? 33.031 -59.997 8.705 1.00 46.38 ? 63 ASP B CG 1 ATOM 1797 O OD1 . ASP B 1 9 ? 33.039 -59.406 7.603 1.00 44.73 ? 63 ASP B OD1 1 ATOM 1798 O OD2 . ASP B 1 9 ? 33.816 -60.939 8.983 1.00 59.49 ? 63 ASP B OD2 1 ATOM 1799 N N . CYS B 1 10 ? 29.842 -57.261 11.265 1.00 21.12 ? 64 CYS B N 1 ATOM 1800 C CA . CYS B 1 10 ? 28.581 -57.136 11.980 1.00 22.86 ? 64 CYS B CA 1 ATOM 1801 C C . CYS B 1 10 ? 27.645 -56.049 11.393 1.00 23.27 ? 64 CYS B C 1 ATOM 1802 O O . CYS B 1 10 ? 28.117 -55.016 10.897 1.00 22.29 ? 64 CYS B O 1 ATOM 1803 C CB . CYS B 1 10 ? 28.850 -56.935 13.473 1.00 26.90 ? 64 CYS B CB 1 ATOM 1804 S SG . CYS B 1 10 ? 29.220 -58.471 14.393 1.00 33.93 ? 64 CYS B SG 1 ATOM 1805 N N . SER B 1 11 ? 26.329 -56.330 11.340 1.00 18.71 ? 65 SER B N 1 ATOM 1806 C CA . SER B 1 11 ? 25.382 -55.320 10.844 1.00 17.54 ? 65 SER B CA 1 ATOM 1807 C C . SER B 1 11 ? 24.844 -54.489 12.009 1.00 19.69 ? 65 SER B C 1 ATOM 1808 O O . SER B 1 11 ? 24.982 -54.879 13.178 1.00 17.53 ? 65 SER B O 1 ATOM 1809 C CB . SER B 1 11 ? 24.237 -55.990 10.087 1.00 20.49 ? 65 SER B CB 1 ATOM 1810 O OG . SER B 1 11 ? 23.351 -56.643 10.988 1.00 22.03 ? 65 SER B OG 1 ATOM 1811 N N . ILE B 1 12 ? 24.196 -53.364 11.724 1.00 18.66 ? 66 ILE B N 1 ATOM 1812 C CA . ILE B 1 12 ? 23.560 -52.588 12.796 1.00 18.66 ? 66 ILE B CA 1 ATOM 1813 C C . ILE B 1 12 ? 22.585 -53.508 13.575 1.00 20.00 ? 66 ILE B C 1 ATOM 1814 O O . ILE B 1 12 ? 22.590 -53.502 14.797 1.00 18.21 ? 66 ILE B O 1 ATOM 1815 C CB . ILE B 1 12 ? 22.833 -51.343 12.215 1.00 23.35 ? 66 ILE B CB 1 ATOM 1816 C CG1 . ILE B 1 12 ? 23.860 -50.277 11.734 1.00 25.12 ? 66 ILE B CG1 1 ATOM 1817 C CG2 . ILE B 1 12 ? 21.822 -50.782 13.216 1.00 24.64 ? 66 ILE B CG2 1 ATOM 1818 C CD1 . ILE B 1 12 ? 24.831 -49.743 12.795 1.00 35.42 ? 66 ILE B CD1 1 ATOM 1819 N N . ALA B 1 13 ? 21.760 -54.303 12.856 1.00 17.24 ? 67 ALA B N 1 ATOM 1820 C CA . ALA B 1 13 ? 20.845 -55.244 13.518 1.00 16.75 ? 67 ALA B CA 1 ATOM 1821 C C . ALA B 1 13 ? 21.577 -56.265 14.420 1.00 20.40 ? 67 ALA B C 1 ATOM 1822 O O . ALA B 1 13 ? 21.202 -56.457 15.580 1.00 19.40 ? 67 ALA B O 1 ATOM 1823 C CB . ALA B 1 13 ? 19.967 -55.943 12.479 1.00 19.14 ? 67 ALA B CB 1 ATOM 1824 N N . GLY B 1 14 ? 22.664 -56.833 13.916 1.00 17.23 ? 68 GLY B N 1 ATOM 1825 C CA . GLY B 1 14 ? 23.474 -57.811 14.642 1.00 16.43 ? 68 GLY B CA 1 ATOM 1826 C C . GLY B 1 14 ? 23.992 -57.224 15.941 1.00 17.53 ? 68 GLY B C 1 ATOM 1827 O O . GLY B 1 14 ? 23.992 -57.882 16.979 1.00 18.50 ? 68 GLY B O 1 ATOM 1828 N N . TRP B 1 15 ? 24.504 -55.994 15.873 1.00 14.48 ? 69 TRP B N 1 ATOM 1829 C CA . TRP B 1 15 ? 25.028 -55.287 17.030 1.00 15.53 ? 69 TRP B CA 1 ATOM 1830 C C . TRP B 1 15 ? 23.926 -55.020 18.101 1.00 18.59 ? 69 TRP B C 1 ATOM 1831 O O . TRP B 1 15 ? 24.073 -55.397 19.277 1.00 18.26 ? 69 TRP B O 1 ATOM 1832 C CB . TRP B 1 15 ? 25.722 -53.997 16.545 1.00 15.89 ? 69 TRP B CB 1 ATOM 1833 C CG . TRP B 1 15 ? 26.000 -52.946 17.590 1.00 17.15 ? 69 TRP B CG 1 ATOM 1834 C CD1 . TRP B 1 15 ? 26.404 -53.134 18.883 1.00 19.79 ? 69 TRP B CD1 1 ATOM 1835 C CD2 . TRP B 1 15 ? 25.886 -51.527 17.406 1.00 17.65 ? 69 TRP B CD2 1 ATOM 1836 N NE1 . TRP B 1 15 ? 26.592 -51.915 19.500 1.00 20.50 ? 69 TRP B NE1 1 ATOM 1837 C CE2 . TRP B 1 15 ? 26.262 -50.914 18.624 1.00 21.68 ? 69 TRP B CE2 1 ATOM 1838 C CE3 . TRP B 1 15 ? 25.488 -50.715 16.333 1.00 19.92 ? 69 TRP B CE3 1 ATOM 1839 C CZ2 . TRP B 1 15 ? 26.266 -49.516 18.797 1.00 21.44 ? 69 TRP B CZ2 1 ATOM 1840 C CZ3 . TRP B 1 15 ? 25.549 -49.324 16.490 1.00 22.08 ? 69 TRP B CZ3 1 ATOM 1841 C CH2 . TRP B 1 15 ? 25.920 -48.749 17.713 1.00 23.15 ? 69 TRP B CH2 1 ATOM 1842 N N . LEU B 1 16 ? 22.825 -54.390 17.695 1.00 13.97 ? 70 LEU B N 1 ATOM 1843 C CA . LEU B 1 16 ? 21.774 -54.009 18.648 1.00 14.69 ? 70 LEU B CA 1 ATOM 1844 C C . LEU B 1 16 ? 20.989 -55.178 19.224 1.00 17.34 ? 70 LEU B C 1 ATOM 1845 O O . LEU B 1 16 ? 20.637 -55.149 20.412 1.00 17.04 ? 70 LEU B O 1 ATOM 1846 C CB . LEU B 1 16 ? 20.863 -52.977 18.000 1.00 15.36 ? 70 LEU B CB 1 ATOM 1847 C CG . LEU B 1 16 ? 21.573 -51.674 17.590 1.00 21.90 ? 70 LEU B CG 1 ATOM 1848 C CD1 . LEU B 1 16 ? 20.632 -50.752 16.832 1.00 23.46 ? 70 LEU B CD1 1 ATOM 1849 C CD2 . LEU B 1 16 ? 22.180 -50.948 18.805 1.00 21.62 ? 70 LEU B CD2 1 ATOM 1850 N N . LEU B 1 17 ? 20.766 -56.217 18.417 1.00 14.46 ? 71 LEU B N 1 ATOM 1851 C CA . LEU B 1 17 ? 20.111 -57.428 18.942 1.00 14.48 ? 71 LEU B CA 1 ATOM 1852 C C . LEU B 1 17 ? 21.074 -58.266 19.777 1.00 16.67 ? 71 LEU B C 1 ATOM 1853 O O . LEU B 1 17 ? 20.628 -58.966 20.672 1.00 16.29 ? 71 LEU B O 1 ATOM 1854 C CB . LEU B 1 17 ? 19.545 -58.296 17.795 1.00 14.83 ? 71 LEU B CB 1 ATOM 1855 C CG . LEU B 1 17 ? 18.445 -57.639 16.975 1.00 18.07 ? 71 LEU B CG 1 ATOM 1856 C CD1 . LEU B 1 17 ? 18.143 -58.414 15.683 1.00 17.51 ? 71 LEU B CD1 1 ATOM 1857 C CD2 . LEU B 1 17 ? 17.199 -57.489 17.804 1.00 20.70 ? 71 LEU B CD2 1 ATOM 1858 N N . GLY B 1 18 ? 22.385 -58.194 19.484 1.00 13.64 ? 72 GLY B N 1 ATOM 1859 C CA . GLY B 1 18 ? 23.392 -58.991 20.178 1.00 15.15 ? 72 GLY B CA 1 ATOM 1860 C C . GLY B 1 18 ? 23.609 -60.341 19.532 1.00 16.53 ? 72 GLY B C 1 ATOM 1861 O O . GLY B 1 18 ? 23.576 -61.375 20.217 1.00 15.38 ? 72 GLY B O 1 ATOM 1862 N N . ASN B 1 19 ? 23.767 -60.360 18.208 1.00 15.28 ? 73 ASN B N 1 ATOM 1863 C CA . ASN B 1 19 ? 24.057 -61.630 17.538 1.00 15.03 ? 73 ASN B CA 1 ATOM 1864 C C . ASN B 1 19 ? 25.349 -62.142 18.248 1.00 16.91 ? 73 ASN B C 1 ATOM 1865 O O . ASN B 1 19 ? 26.276 -61.368 18.410 1.00 17.57 ? 73 ASN B O 1 ATOM 1866 C CB . ASN B 1 19 ? 24.305 -61.385 16.052 1.00 18.20 ? 73 ASN B CB 1 ATOM 1867 C CG . ASN B 1 19 ? 24.762 -62.584 15.241 1.00 21.94 ? 73 ASN B CG 1 ATOM 1868 O OD1 . ASN B 1 19 ? 25.508 -63.442 15.710 1.00 20.88 ? 73 ASN B OD1 1 ATOM 1869 N ND2 . ASN B 1 19 ? 24.479 -62.573 13.967 1.00 17.14 ? 73 ASN B ND2 1 ATOM 1870 N N . PRO B 1 20 ? 25.440 -63.392 18.717 1.00 16.49 ? 74 PRO B N 1 ATOM 1871 C CA . PRO B 1 20 ? 26.674 -63.823 19.417 1.00 17.71 ? 74 PRO B CA 1 ATOM 1872 C C . PRO B 1 20 ? 27.988 -63.654 18.651 1.00 23.04 ? 74 PRO B C 1 ATOM 1873 O O . PRO B 1 20 ? 29.088 -63.455 19.238 1.00 23.30 ? 74 PRO B O 1 ATOM 1874 C CB . PRO B 1 20 ? 26.395 -65.281 19.735 1.00 20.70 ? 74 PRO B CB 1 ATOM 1875 C CG . PRO B 1 20 ? 24.880 -65.367 19.839 1.00 23.66 ? 74 PRO B CG 1 ATOM 1876 C CD . PRO B 1 20 ? 24.416 -64.468 18.719 1.00 19.01 ? 74 PRO B CD 1 ATOM 1877 N N . GLU B 1 21 ? 27.886 -63.674 17.325 1.00 20.08 ? 75 GLU B N 1 ATOM 1878 C CA . GLU B 1 21 ? 29.102 -63.440 16.523 1.00 20.86 ? 75 GLU B CA 1 ATOM 1879 C C . GLU B 1 21 ? 29.582 -61.981 16.679 1.00 26.24 ? 75 GLU B C 1 ATOM 1880 O O . GLU B 1 21 ? 30.706 -61.630 16.293 1.00 25.73 ? 75 GLU B O 1 ATOM 1881 C CB . GLU B 1 21 ? 28.844 -63.777 15.037 1.00 21.88 ? 75 GLU B CB 1 ATOM 1882 C CG . GLU B 1 21 ? 28.763 -65.278 14.810 1.00 28.92 ? 75 GLU B CG 1 ATOM 1883 C CD . GLU B 1 21 ? 30.094 -65.996 14.690 1.00 57.52 ? 75 GLU B CD 1 ATOM 1884 O OE1 . GLU B 1 21 ? 30.722 -65.898 13.612 1.00 44.13 ? 75 GLU B OE1 1 ATOM 1885 O OE2 . GLU B 1 21 ? 30.497 -66.680 15.658 1.00 59.78 ? 75 GLU B OE2 1 ATOM 1886 N N . CYS B 1 22 ? 28.761 -61.162 17.305 1.00 22.38 ? 76 CYS B N 1 ATOM 1887 C CA . CYS B 1 22 ? 29.037 -59.727 17.498 1.00 22.60 ? 76 CYS B CA 1 ATOM 1888 C C . CYS B 1 22 ? 29.351 -59.420 18.950 1.00 21.22 ? 76 CYS B C 1 ATOM 1889 O O . CYS B 1 22 ? 29.335 -58.249 19.339 1.00 20.56 ? 76 CYS B O 1 ATOM 1890 C CB . CYS B 1 22 ? 27.841 -58.920 16.994 1.00 25.22 ? 76 CYS B CB 1 ATOM 1891 S SG . CYS B 1 22 ? 27.479 -59.202 15.234 1.00 31.91 ? 76 CYS B SG 1 ATOM 1892 N N . ASP B 1 23 ? 29.740 -60.448 19.739 1.00 19.10 ? 77 ASP B N 1 ATOM 1893 C CA . ASP B 1 23 ? 30.069 -60.258 21.167 1.00 18.34 ? 77 ASP B CA 1 ATOM 1894 C C . ASP B 1 23 ? 31.135 -59.215 21.475 1.00 21.10 ? 77 ASP B C 1 ATOM 1895 O O . ASP B 1 23 ? 31.077 -58.569 22.520 1.00 19.82 ? 77 ASP B O 1 ATOM 1896 C CB . ASP B 1 23 ? 30.424 -61.581 21.841 1.00 19.91 ? 77 ASP B CB 1 ATOM 1897 C CG . ASP B 1 23 ? 29.275 -62.501 22.151 1.00 25.40 ? 77 ASP B CG 1 ATOM 1898 O OD1 . ASP B 1 23 ? 28.115 -62.037 22.122 1.00 26.95 ? 77 ASP B OD1 1 ATOM 1899 O OD2 . ASP B 1 23 ? 29.539 -63.663 22.528 1.00 29.03 ? 77 ASP B OD2 1 ATOM 1900 N N . ARG B 1 24 ? 32.055 -58.971 20.535 1.00 17.40 ? 78 ARG B N 1 ATOM 1901 C CA . ARG B 1 24 ? 33.080 -57.940 20.760 1.00 19.12 ? 78 ARG B CA 1 ATOM 1902 C C . ARG B 1 24 ? 32.447 -56.536 20.906 1.00 22.53 ? 78 ARG B C 1 ATOM 1903 O O . ARG B 1 24 ? 33.113 -55.603 21.369 1.00 22.95 ? 78 ARG B O 1 ATOM 1904 C CB . ARG B 1 24 ? 34.079 -57.937 19.596 1.00 20.06 ? 78 ARG B CB 1 ATOM 1905 C CG . ARG B 1 24 ? 33.567 -57.379 18.278 1.00 22.22 ? 78 ARG B CG 1 ATOM 1906 C CD . ARG B 1 24 ? 34.452 -57.801 17.128 1.00 17.85 ? 78 ARG B CD 1 ATOM 1907 N NE . ARG B 1 24 ? 33.836 -57.494 15.835 1.00 20.49 ? 78 ARG B NE 1 ATOM 1908 C CZ . ARG B 1 24 ? 32.948 -58.259 15.204 1.00 24.65 ? 78 ARG B CZ 1 ATOM 1909 N NH1 . ARG B 1 24 ? 32.614 -59.445 15.693 1.00 27.11 ? 78 ARG B NH1 1 ATOM 1910 N NH2 . ARG B 1 24 ? 32.412 -57.857 14.064 1.00 27.14 ? 78 ARG B NH2 1 ATOM 1911 N N . LEU B 1 25 ? 31.186 -56.393 20.434 1.00 19.18 ? 79 LEU B N 1 ATOM 1912 C CA . LEU B 1 25 ? 30.442 -55.134 20.428 1.00 18.03 ? 79 LEU B CA 1 ATOM 1913 C C . LEU B 1 25 ? 29.441 -55.014 21.572 1.00 21.43 ? 79 LEU B C 1 ATOM 1914 O O . LEU B 1 25 ? 28.604 -54.121 21.529 1.00 19.97 ? 79 LEU B O 1 ATOM 1915 C CB . LEU B 1 25 ? 29.687 -54.982 19.067 1.00 17.51 ? 79 LEU B CB 1 ATOM 1916 C CG . LEU B 1 25 ? 30.521 -54.944 17.795 1.00 19.51 ? 79 LEU B CG 1 ATOM 1917 C CD1 . LEU B 1 25 ? 29.606 -54.889 16.570 1.00 21.71 ? 79 LEU B CD1 1 ATOM 1918 C CD2 . LEU B 1 25 ? 31.508 -53.779 17.809 1.00 24.91 ? 79 LEU B CD2 1 ATOM 1919 N N . LEU B 1 26 ? 29.500 -55.895 22.588 1.00 20.07 ? 80 LEU B N 1 ATOM 1920 C CA . LEU B 1 26 ? 28.498 -55.826 23.672 1.00 20.95 ? 80 LEU B CA 1 ATOM 1921 C C . LEU B 1 26 ? 28.539 -54.551 24.500 1.00 27.18 ? 80 LEU B C 1 ATOM 1922 O O . LEU B 1 26 ? 27.511 -54.150 25.030 1.00 26.01 ? 80 LEU B O 1 ATOM 1923 C CB . LEU B 1 26 ? 28.552 -57.073 24.559 1.00 20.79 ? 80 LEU B CB 1 ATOM 1924 C CG . LEU B 1 26 ? 27.970 -58.327 23.954 1.00 24.47 ? 80 LEU B CG 1 ATOM 1925 C CD1 . LEU B 1 26 ? 28.545 -59.557 24.634 1.00 24.17 ? 80 LEU B CD1 1 ATOM 1926 C CD2 . LEU B 1 26 ? 26.451 -58.337 24.068 1.00 27.66 ? 80 LEU B CD2 1 ATOM 1927 N N . SER B 1 27 ? 29.702 -53.893 24.569 1.00 24.99 ? 81 SER B N 1 ATOM 1928 C CA . SER B 1 27 ? 29.841 -52.622 25.287 1.00 24.78 ? 81 SER B CA 1 ATOM 1929 C C . SER B 1 27 ? 30.809 -51.791 24.486 1.00 26.34 ? 81 SER B C 1 ATOM 1930 O O . SER B 1 27 ? 31.951 -52.221 24.283 1.00 26.04 ? 81 SER B O 1 ATOM 1931 C CB . SER B 1 27 ? 30.384 -52.860 26.697 1.00 30.32 ? 81 SER B CB 1 ATOM 1932 O OG . SER B 1 27 ? 30.458 -51.657 27.451 1.00 36.60 ? 81 SER B OG 1 ATOM 1933 N N . VAL B 1 28 A 30.357 -50.634 23.970 1.00 22.07 ? 81 VAL B N 1 ATOM 1934 C CA . VAL B 1 28 A 31.242 -49.818 23.150 1.00 20.38 ? 81 VAL B CA 1 ATOM 1935 C C . VAL B 1 28 A 31.287 -48.384 23.665 1.00 22.74 ? 81 VAL B C 1 ATOM 1936 O O . VAL B 1 28 A 30.252 -47.847 24.120 1.00 22.76 ? 81 VAL B O 1 ATOM 1937 C CB . VAL B 1 28 A 30.870 -49.865 21.631 1.00 24.61 ? 81 VAL B CB 1 ATOM 1938 C CG1 . VAL B 1 28 A 30.977 -51.285 21.057 1.00 24.37 ? 81 VAL B CG1 1 ATOM 1939 C CG2 . VAL B 1 28 A 29.495 -49.255 21.371 1.00 22.94 ? 81 VAL B CG2 1 ATOM 1940 N N . PRO B 1 29 ? 32.456 -47.739 23.579 1.00 18.86 ? 82 PRO B N 1 ATOM 1941 C CA . PRO B 1 29 ? 32.560 -46.351 24.056 1.00 18.66 ? 82 PRO B CA 1 ATOM 1942 C C . PRO B 1 29 ? 32.006 -45.388 23.001 1.00 19.52 ? 82 PRO B C 1 ATOM 1943 O O . PRO B 1 29 ? 31.543 -45.804 21.931 1.00 20.63 ? 82 PRO B O 1 ATOM 1944 C CB . PRO B 1 29 ? 34.077 -46.147 24.225 1.00 21.04 ? 82 PRO B CB 1 ATOM 1945 C CG . PRO B 1 29 ? 34.679 -47.058 23.257 1.00 25.97 ? 82 PRO B CG 1 ATOM 1946 C CD . PRO B 1 29 ? 33.764 -48.254 23.122 1.00 20.71 ? 82 PRO B CD 1 ATOM 1947 N N . GLU B 1 30 ? 32.076 -44.083 23.299 1.00 18.54 ? 83 GLU B N 1 ATOM 1948 C CA . GLU B 1 30 ? 31.613 -43.050 22.377 1.00 17.70 ? 83 GLU B CA 1 ATOM 1949 C C . GLU B 1 30 ? 32.385 -43.153 21.062 1.00 20.83 ? 83 GLU B C 1 ATOM 1950 O O . GLU B 1 30 ? 33.582 -43.483 21.067 1.00 20.12 ? 83 GLU B O 1 ATOM 1951 C CB . GLU B 1 30 ? 31.748 -41.657 23.042 1.00 20.36 ? 83 GLU B CB 1 ATOM 1952 C CG . GLU B 1 30 ? 31.400 -40.438 22.196 1.00 27.70 ? 83 GLU B CG 1 ATOM 1953 C CD . GLU B 1 30 ? 31.799 -39.124 22.851 1.00 52.59 ? 83 GLU B CD 1 ATOM 1954 O OE1 . GLU B 1 30 ? 32.150 -39.134 24.056 1.00 41.61 ? 83 GLU B OE1 1 ATOM 1955 O OE2 . GLU B 1 30 ? 31.752 -38.081 22.157 1.00 43.39 ? 83 GLU B OE2 1 ATOM 1956 N N . TRP B 1 31 ? 31.689 -42.920 19.948 1.00 17.18 ? 84 TRP B N 1 ATOM 1957 C CA . TRP B 1 31 ? 32.308 -43.010 18.609 1.00 17.17 ? 84 TRP B CA 1 ATOM 1958 C C . TRP B 1 31 ? 32.201 -41.708 17.838 1.00 20.65 ? 84 TRP B C 1 ATOM 1959 O O . TRP B 1 31 ? 31.361 -40.887 18.190 1.00 20.55 ? 84 TRP B O 1 ATOM 1960 C CB . TRP B 1 31 ? 31.694 -44.142 17.800 1.00 14.80 ? 84 TRP B CB 1 ATOM 1961 C CG . TRP B 1 31 ? 30.207 -44.011 17.591 1.00 15.32 ? 84 TRP B CG 1 ATOM 1962 C CD1 . TRP B 1 31 ? 29.583 -43.298 16.605 1.00 17.83 ? 84 TRP B CD1 1 ATOM 1963 C CD2 . TRP B 1 31 ? 29.173 -44.675 18.324 1.00 14.93 ? 84 TRP B CD2 1 ATOM 1964 N NE1 . TRP B 1 31 ? 28.224 -43.399 16.734 1.00 16.28 ? 84 TRP B NE1 1 ATOM 1965 C CE2 . TRP B 1 31 ? 27.938 -44.242 17.786 1.00 18.54 ? 84 TRP B CE2 1 ATOM 1966 C CE3 . TRP B 1 31 ? 29.159 -45.508 19.460 1.00 16.24 ? 84 TRP B CE3 1 ATOM 1967 C CZ2 . TRP B 1 31 ? 26.706 -44.652 18.316 1.00 18.14 ? 84 TRP B CZ2 1 ATOM 1968 C CZ3 . TRP B 1 31 ? 27.935 -45.986 19.930 1.00 16.91 ? 84 TRP B CZ3 1 ATOM 1969 C CH2 . TRP B 1 31 ? 26.728 -45.499 19.415 1.00 15.98 ? 84 TRP B CH2 1 ATOM 1970 N N . SER B 1 32 ? 33.032 -41.537 16.775 1.00 16.68 ? 85 SER B N 1 ATOM 1971 C CA . SER B 1 32 ? 32.985 -40.334 15.921 1.00 18.27 ? 85 SER B CA 1 ATOM 1972 C C . SER B 1 32 ? 31.971 -40.560 14.777 1.00 23.27 ? 85 SER B C 1 ATOM 1973 O O . SER B 1 32 ? 31.264 -39.629 14.369 1.00 23.81 ? 85 SER B O 1 ATOM 1974 C CB . SER B 1 32 ? 34.368 -40.001 15.375 1.00 22.71 ? 85 SER B CB 1 ATOM 1975 O OG . SER B 1 32 ? 34.930 -41.149 14.760 1.00 25.19 ? 85 SER B OG 1 ATOM 1976 N N . TYR B 1 33 ? 31.889 -41.809 14.301 1.00 18.80 ? 86 TYR B N 1 ATOM 1977 C CA . TYR B 1 33 ? 30.936 -42.303 13.286 1.00 18.95 ? 86 TYR B CA 1 ATOM 1978 C C . TYR B 1 33 ? 30.947 -43.813 13.295 1.00 20.82 ? 86 TYR B C 1 ATOM 1979 O O . TYR B 1 33 ? 31.845 -44.410 13.878 1.00 19.84 ? 86 TYR B O 1 ATOM 1980 C CB . TYR B 1 33 ? 31.225 -41.769 11.880 1.00 21.64 ? 86 TYR B CB 1 ATOM 1981 C CG . TYR B 1 33 ? 32.654 -41.900 11.415 1.00 26.56 ? 86 TYR B CG 1 ATOM 1982 C CD1 . TYR B 1 33 ? 33.080 -43.030 10.723 1.00 29.27 ? 86 TYR B CD1 1 ATOM 1983 C CD2 . TYR B 1 33 ? 33.550 -40.844 11.553 1.00 28.51 ? 86 TYR B CD2 1 ATOM 1984 C CE1 . TYR B 1 33 ? 34.381 -43.129 10.228 1.00 32.50 ? 86 TYR B CE1 1 ATOM 1985 C CE2 . TYR B 1 33 ? 34.860 -40.939 11.081 1.00 31.03 ? 86 TYR B CE2 1 ATOM 1986 C CZ . TYR B 1 33 ? 35.264 -42.077 10.403 1.00 40.24 ? 86 TYR B CZ 1 ATOM 1987 O OH . TYR B 1 33 ? 36.541 -42.169 9.909 1.00 46.81 ? 86 TYR B OH 1 ATOM 1988 N N . ILE B 1 34 ? 29.956 -44.421 12.665 1.00 19.80 ? 87 ILE B N 1 ATOM 1989 C CA . ILE B 1 34 ? 29.832 -45.880 12.586 1.00 18.47 ? 87 ILE B CA 1 ATOM 1990 C C . ILE B 1 34 ? 30.244 -46.319 11.182 1.00 23.68 ? 87 ILE B C 1 ATOM 1991 O O . ILE B 1 34 ? 29.751 -45.759 10.201 1.00 22.82 ? 87 ILE B O 1 ATOM 1992 C CB . ILE B 1 34 ? 28.417 -46.352 12.943 1.00 20.91 ? 87 ILE B CB 1 ATOM 1993 C CG1 . ILE B 1 34 ? 27.968 -45.826 14.336 1.00 20.86 ? 87 ILE B CG1 1 ATOM 1994 C CG2 . ILE B 1 34 ? 28.341 -47.895 12.872 1.00 20.40 ? 87 ILE B CG2 1 ATOM 1995 C CD1 . ILE B 1 34 ? 26.457 -45.882 14.597 1.00 18.90 ? 87 ILE B CD1 1 ATOM 1996 N N . MET B 1 35 ? 31.164 -47.320 11.088 1.00 21.63 ? 88 MET B N 1 ATOM 1997 C CA . MET B 1 35 ? 31.619 -47.877 9.810 1.00 24.00 ? 88 MET B CA 1 ATOM 1998 C C . MET B 1 35 ? 30.965 -49.240 9.631 1.00 27.56 ? 88 MET B C 1 ATOM 1999 O O . MET B 1 35 ? 31.187 -50.130 10.468 1.00 26.21 ? 88 MET B O 1 ATOM 2000 C CB . MET B 1 35 ? 33.153 -47.998 9.771 1.00 28.38 ? 88 MET B CB 1 ATOM 2001 C CG . MET B 1 35 ? 33.843 -46.692 10.171 1.00 35.58 ? 88 MET B CG 1 ATOM 2002 S SD . MET B 1 35 ? 35.646 -46.709 10.198 1.00 43.87 ? 88 MET B SD 1 ATOM 2003 C CE . MET B 1 35 ? 35.995 -46.421 8.467 1.00 41.68 ? 88 MET B CE 1 ATOM 2004 N N . GLU B 1 36 ? 30.109 -49.382 8.582 1.00 23.51 ? 89 GLU B N 1 ATOM 2005 C CA . GLU B 1 36 ? 29.421 -50.633 8.290 1.00 23.44 ? 89 GLU B CA 1 ATOM 2006 C C . GLU B 1 36 ? 29.737 -51.100 6.856 1.00 30.06 ? 89 GLU B C 1 ATOM 2007 O O . GLU B 1 36 ? 29.811 -50.273 5.932 1.00 31.83 ? 89 GLU B O 1 ATOM 2008 C CB . GLU B 1 36 ? 27.895 -50.486 8.535 1.00 25.26 ? 89 GLU B CB 1 ATOM 2009 C CG . GLU B 1 36 ? 27.117 -51.799 8.518 1.00 29.92 ? 89 GLU B CG 1 ATOM 2010 C CD . GLU B 1 36 ? 25.612 -51.669 8.365 1.00 51.34 ? 89 GLU B CD 1 ATOM 2011 O OE1 . GLU B 1 36 ? 25.163 -50.802 7.577 1.00 46.14 ? 89 GLU B OE1 1 ATOM 2012 O OE2 . GLU B 1 36 ? 24.880 -52.470 8.996 1.00 33.14 ? 89 GLU B OE2 1 ATOM 2013 N N . LYS B 1 37 ? 29.934 -52.419 6.662 1.00 25.97 ? 90 LYS B N 1 ATOM 2014 C CA . LYS B 1 37 ? 30.194 -52.968 5.313 1.00 26.14 ? 90 LYS B CA 1 ATOM 2015 C C . LYS B 1 37 ? 28.902 -52.897 4.468 1.00 32.94 ? 90 LYS B C 1 ATOM 2016 O O . LYS B 1 37 ? 27.813 -52.791 5.031 1.00 34.14 ? 90 LYS B O 1 ATOM 2017 C CB . LYS B 1 37 ? 30.727 -54.416 5.403 1.00 28.27 ? 90 LYS B CB 1 ATOM 2018 C CG . LYS B 1 37 ? 32.176 -54.515 5.840 1.00 40.10 ? 90 LYS B CG 1 ATOM 2019 C CD . LYS B 1 37 ? 32.641 -55.964 5.936 1.00 48.24 ? 90 LYS B CD 1 ATOM 2020 C CE . LYS B 1 37 ? 34.077 -56.049 6.394 1.00 53.22 ? 90 LYS B CE 1 ATOM 2021 N NZ . LYS B 1 37 ? 34.570 -57.447 6.378 1.00 60.86 ? 90 LYS B NZ 1 ATOM 2022 N N . GLU B 1 38 ? 29.019 -52.930 3.120 1.00 33.56 ? 91 GLU B N 1 ATOM 2023 C CA . GLU B 1 38 ? 27.868 -52.877 2.210 1.00 35.40 ? 91 GLU B CA 1 ATOM 2024 C C . GLU B 1 38 ? 26.944 -54.081 2.451 1.00 37.76 ? 91 GLU B C 1 ATOM 2025 O O . GLU B 1 38 ? 25.726 -53.908 2.521 1.00 36.93 ? 91 GLU B O 1 ATOM 2026 C CB . GLU B 1 38 ? 28.340 -52.830 0.736 1.00 38.37 ? 91 GLU B CB 1 ATOM 2027 C CG . GLU B 1 38 ? 27.226 -52.580 -0.277 1.00 53.77 ? 91 GLU B CG 1 ATOM 2028 C CD . GLU B 1 38 ? 27.403 -51.396 -1.216 1.00 82.80 ? 91 GLU B CD 1 ATOM 2029 O OE1 . GLU B 1 38 ? 28.562 -50.995 -1.475 1.00 84.69 ? 91 GLU B OE1 1 ATOM 2030 O OE2 . GLU B 1 38 ? 26.373 -50.870 -1.698 1.00 76.64 ? 91 GLU B OE2 1 ATOM 2031 N N . ASN B 1 39 ? 27.530 -55.290 2.597 1.00 33.29 ? 92 ASN B N 1 ATOM 2032 C CA . ASN B 1 39 ? 26.761 -56.504 2.855 1.00 32.39 ? 92 ASN B CA 1 ATOM 2033 C C . ASN B 1 39 ? 27.361 -57.239 4.066 1.00 33.73 ? 92 ASN B C 1 ATOM 2034 O O . ASN B 1 39 ? 28.167 -58.153 3.886 1.00 34.13 ? 92 ASN B O 1 ATOM 2035 C CB . ASN B 1 39 ? 26.706 -57.385 1.600 1.00 36.83 ? 92 ASN B CB 1 ATOM 2036 C CG . ASN B 1 39 ? 25.946 -56.759 0.452 1.00 57.78 ? 92 ASN B CG 1 ATOM 2037 O OD1 . ASN B 1 39 ? 26.522 -56.410 -0.577 1.00 57.09 ? 92 ASN B OD1 1 ATOM 2038 N ND2 . ASN B 1 39 ? 24.638 -56.591 0.608 1.00 47.83 ? 92 ASN B ND2 1 ATOM 2039 N N . PRO B 1 40 ? 27.054 -56.786 5.315 1.00 27.85 ? 93 PRO B N 1 ATOM 2040 C CA . PRO B 1 40 ? 27.628 -57.460 6.496 1.00 26.47 ? 93 PRO B CA 1 ATOM 2041 C C . PRO B 1 40 ? 27.141 -58.899 6.634 1.00 28.31 ? 93 PRO B C 1 ATOM 2042 O O . PRO B 1 40 ? 25.972 -59.178 6.390 1.00 28.30 ? 93 PRO B O 1 ATOM 2043 C CB . PRO B 1 40 ? 27.173 -56.582 7.682 1.00 27.41 ? 93 PRO B CB 1 ATOM 2044 C CG . PRO B 1 40 ? 26.534 -55.361 7.084 1.00 30.84 ? 93 PRO B CG 1 ATOM 2045 C CD . PRO B 1 40 ? 26.100 -55.725 5.705 1.00 28.00 ? 93 PRO B CD 1 ATOM 2046 N N . ARG B 1 41 ? 28.017 -59.808 7.037 1.00 23.75 ? 94 ARG B N 1 ATOM 2047 C CA . ARG B 1 41 ? 27.590 -61.202 7.138 1.00 22.82 ? 94 ARG B CA 1 ATOM 2048 C C . ARG B 1 41 ? 26.902 -61.574 8.430 1.00 23.82 ? 94 ARG B C 1 ATOM 2049 O O . ARG B 1 41 ? 26.094 -62.499 8.413 1.00 25.63 ? 94 ARG B O 1 ATOM 2050 C CB . ARG B 1 41 ? 28.683 -62.214 6.746 1.00 25.13 ? 94 ARG B CB 1 ATOM 2051 C CG . ARG B 1 41 ? 30.095 -61.864 7.145 1.00 35.67 ? 94 ARG B CG 1 ATOM 2052 C CD . ARG B 1 41 ? 31.035 -62.962 6.704 1.00 37.40 ? 94 ARG B CD 1 ATOM 2053 N NE . ARG B 1 41 ? 31.061 -63.968 7.749 1.00 42.08 ? 94 ARG B NE 1 ATOM 2054 C CZ . ARG B 1 41 ? 30.651 -65.222 7.626 1.00 35.53 ? 94 ARG B CZ 1 ATOM 2055 N NH1 . ARG B 1 41 ? 30.314 -65.707 6.434 1.00 27.90 ? 94 ARG B NH1 1 ATOM 2056 N NH2 . ARG B 1 41 ? 30.669 -66.029 8.667 1.00 36.45 ? 94 ARG B NH2 1 ATOM 2057 N N . ASP B 1 42 ? 27.225 -60.899 9.537 1.00 19.18 ? 95 ASP B N 1 ATOM 2058 C CA . ASP B 1 42 ? 26.641 -61.237 10.836 1.00 19.07 ? 95 ASP B CA 1 ATOM 2059 C C . ASP B 1 42 ? 25.521 -60.281 11.220 1.00 21.94 ? 95 ASP B C 1 ATOM 2060 O O . ASP B 1 42 ? 25.755 -59.207 11.785 1.00 22.33 ? 95 ASP B O 1 ATOM 2061 C CB . ASP B 1 42 ? 27.719 -61.363 11.928 1.00 19.37 ? 95 ASP B CB 1 ATOM 2062 C CG . ASP B 1 42 ? 28.685 -62.474 11.649 1.00 23.35 ? 95 ASP B CG 1 ATOM 2063 O OD1 . ASP B 1 42 ? 28.216 -63.632 11.377 1.00 22.95 ? 95 ASP B OD1 1 ATOM 2064 O OD2 . ASP B 1 42 ? 29.900 -62.217 11.711 1.00 25.78 ? 95 ASP B OD2 1 ATOM 2065 N N . GLY B 1 43 A 24.306 -60.716 10.925 1.00 21.47 ? 95 GLY B N 1 ATOM 2066 C CA . GLY B 1 43 A 23.101 -59.949 11.201 1.00 21.78 ? 95 GLY B CA 1 ATOM 2067 C C . GLY B 1 43 A 22.102 -60.716 12.030 1.00 23.81 ? 95 GLY B C 1 ATOM 2068 O O . GLY B 1 43 A 22.269 -60.922 13.236 1.00 22.38 ? 95 GLY B O 1 ATOM 2069 N N . LEU B 1 44 ? 21.027 -61.062 11.392 1.00 20.72 ? 96 LEU B N 1 ATOM 2070 C CA . LEU B 1 44 ? 19.984 -61.832 12.019 1.00 19.40 ? 96 LEU B CA 1 ATOM 2071 C C . LEU B 1 44 ? 20.383 -63.299 11.921 1.00 24.51 ? 96 LEU B C 1 ATOM 2072 O O . LEU B 1 44 ? 20.080 -63.922 10.912 1.00 26.86 ? 96 LEU B O 1 ATOM 2073 C CB . LEU B 1 44 ? 18.648 -61.573 11.260 1.00 20.86 ? 96 LEU B CB 1 ATOM 2074 C CG . LEU B 1 44 ? 17.763 -60.421 11.792 1.00 26.58 ? 96 LEU B CG 1 ATOM 2075 C CD1 . LEU B 1 44 ? 18.524 -59.160 12.013 1.00 26.28 ? 96 LEU B CD1 1 ATOM 2076 C CD2 . LEU B 1 44 ? 16.637 -60.150 10.842 1.00 29.20 ? 96 LEU B CD2 1 ATOM 2077 N N . CYS B 1 45 ? 21.067 -63.843 12.954 1.00 23.64 ? 97 CYS B N 1 ATOM 2078 C CA . CYS B 1 45 ? 21.442 -65.270 13.050 1.00 26.20 ? 97 CYS B CA 1 ATOM 2079 C C . CYS B 1 45 ? 20.183 -66.146 12.943 1.00 22.28 ? 97 CYS B C 1 ATOM 2080 O O . CYS B 1 45 ? 20.159 -67.063 12.143 1.00 18.95 ? 97 CYS B O 1 ATOM 2081 C CB . CYS B 1 45 ? 22.282 -65.597 14.290 1.00 30.23 ? 97 CYS B CB 1 ATOM 2082 S SG . CYS B 1 45 ? 21.565 -65.075 15.878 1.00 36.24 ? 97 CYS B SG 1 ATOM 2083 N N . TYR B 1 46 ? 19.116 -65.811 13.682 1.00 17.50 ? 98 TYR B N 1 ATOM 2084 C CA . TYR B 1 46 ? 17.822 -66.461 13.462 1.00 14.67 ? 98 TYR B CA 1 ATOM 2085 C C . TYR B 1 46 ? 17.217 -65.599 12.360 1.00 16.48 ? 98 TYR B C 1 ATOM 2086 O O . TYR B 1 46 ? 17.150 -64.387 12.522 1.00 15.59 ? 98 TYR B O 1 ATOM 2087 C CB . TYR B 1 46 ? 16.959 -66.441 14.733 1.00 15.27 ? 98 TYR B CB 1 ATOM 2088 C CG . TYR B 1 46 ? 15.746 -67.345 14.586 1.00 16.74 ? 98 TYR B CG 1 ATOM 2089 C CD1 . TYR B 1 46 ? 15.714 -68.600 15.179 1.00 18.07 ? 98 TYR B CD1 1 ATOM 2090 C CD2 . TYR B 1 46 ? 14.672 -66.974 13.787 1.00 16.99 ? 98 TYR B CD2 1 ATOM 2091 C CE1 . TYR B 1 46 ? 14.609 -69.441 15.040 1.00 14.61 ? 98 TYR B CE1 1 ATOM 2092 C CE2 . TYR B 1 46 ? 13.602 -67.844 13.565 1.00 17.12 ? 98 TYR B CE2 1 ATOM 2093 C CZ . TYR B 1 46 ? 13.562 -69.065 14.220 1.00 18.19 ? 98 TYR B CZ 1 ATOM 2094 O OH . TYR B 1 46 ? 12.486 -69.893 14.049 1.00 19.78 ? 98 TYR B OH 1 ATOM 2095 N N . PRO B 1 47 ? 16.837 -66.179 11.189 1.00 15.16 ? 99 PRO B N 1 ATOM 2096 C CA . PRO B 1 47 ? 16.473 -65.338 10.048 1.00 14.32 ? 99 PRO B CA 1 ATOM 2097 C C . PRO B 1 47 ? 15.212 -64.515 10.245 1.00 15.88 ? 99 PRO B C 1 ATOM 2098 O O . PRO B 1 47 ? 14.361 -64.877 11.044 1.00 14.50 ? 99 PRO B O 1 ATOM 2099 C CB . PRO B 1 47 ? 16.351 -66.347 8.891 1.00 17.06 ? 99 PRO B CB 1 ATOM 2100 C CG . PRO B 1 47 ? 15.931 -67.603 9.573 1.00 19.87 ? 99 PRO B CG 1 ATOM 2101 C CD . PRO B 1 47 ? 16.847 -67.605 10.794 1.00 18.00 ? 99 PRO B CD 1 ATOM 2102 N N . GLY B 1 48 ? 15.111 -63.421 9.518 1.00 15.31 ? 100 GLY B N 1 ATOM 2103 C CA . GLY B 1 48 ? 13.912 -62.597 9.585 1.00 14.94 ? 100 GLY B CA 1 ATOM 2104 C C . GLY B 1 48 ? 14.080 -61.258 8.928 1.00 21.77 ? 100 GLY B C 1 ATOM 2105 O O . GLY B 1 48 ? 14.732 -61.146 7.877 1.00 23.00 ? 100 GLY B O 1 ATOM 2106 N N . SER B 1 49 ? 13.496 -60.233 9.566 1.00 17.16 ? 101 SER B N 1 ATOM 2107 C CA . SER B 1 49 ? 13.506 -58.906 9.004 1.00 16.13 ? 101 SER B CA 1 ATOM 2108 C C . SER B 1 49 ? 13.546 -57.878 10.077 1.00 18.62 ? 101 SER B C 1 ATOM 2109 O O . SER B 1 49 ? 13.363 -58.179 11.245 1.00 17.96 ? 101 SER B O 1 ATOM 2110 C CB . SER B 1 49 ? 12.277 -58.708 8.126 1.00 21.44 ? 101 SER B CB 1 ATOM 2111 O OG . SER B 1 49 ? 11.074 -58.799 8.864 1.00 30.18 ? 101 SER B OG 1 ATOM 2112 N N . PHE B 1 50 ? 13.803 -56.629 9.675 1.00 17.77 ? 102 PHE B N 1 ATOM 2113 C CA . PHE B 1 50 ? 13.869 -55.539 10.610 1.00 17.94 ? 102 PHE B CA 1 ATOM 2114 C C . PHE B 1 50 ? 13.085 -54.390 9.998 1.00 19.09 ? 102 PHE B C 1 ATOM 2115 O O . PHE B 1 50 ? 13.438 -53.906 8.910 1.00 18.63 ? 102 PHE B O 1 ATOM 2116 C CB . PHE B 1 50 ? 15.353 -55.191 10.838 1.00 19.40 ? 102 PHE B CB 1 ATOM 2117 C CG . PHE B 1 50 ? 15.635 -54.550 12.169 1.00 20.49 ? 102 PHE B CG 1 ATOM 2118 C CD1 . PHE B 1 50 ? 16.383 -55.209 13.128 1.00 21.38 ? 102 PHE B CD1 1 ATOM 2119 C CD2 . PHE B 1 50 ? 15.079 -53.315 12.497 1.00 24.57 ? 102 PHE B CD2 1 ATOM 2120 C CE1 . PHE B 1 50 ? 16.659 -54.605 14.355 1.00 23.28 ? 102 PHE B CE1 1 ATOM 2121 C CE2 . PHE B 1 50 ? 15.327 -52.730 13.739 1.00 27.73 ? 102 PHE B CE2 1 ATOM 2122 C CZ . PHE B 1 50 ? 16.102 -53.391 14.667 1.00 24.60 ? 102 PHE B CZ 1 ATOM 2123 N N . ASN B 1 51 ? 11.971 -53.997 10.643 1.00 16.61 ? 103 ASN B N 1 ATOM 2124 C CA . ASN B 1 51 ? 11.085 -52.943 10.133 1.00 16.15 ? 103 ASN B CA 1 ATOM 2125 C C . ASN B 1 51 ? 11.731 -51.596 10.255 1.00 18.38 ? 103 ASN B C 1 ATOM 2126 O O . ASN B 1 51 ? 12.401 -51.341 11.247 1.00 16.78 ? 103 ASN B O 1 ATOM 2127 C CB . ASN B 1 51 ? 9.755 -52.940 10.823 1.00 18.77 ? 103 ASN B CB 1 ATOM 2128 C CG . ASN B 1 51 ? 8.947 -54.163 10.516 1.00 30.50 ? 103 ASN B CG 1 ATOM 2129 O OD1 . ASN B 1 51 ? 8.837 -54.618 9.356 1.00 26.13 ? 103 ASN B OD1 1 ATOM 2130 N ND2 . ASN B 1 51 ? 8.423 -54.747 11.551 1.00 21.88 ? 103 ASN B ND2 1 ATOM 2131 N N . ASP B 1 52 ? 11.540 -50.734 9.220 1.00 18.40 ? 104 ASP B N 1 ATOM 2132 C CA . ASP B 1 52 ? 12.064 -49.362 9.193 1.00 18.12 ? 104 ASP B CA 1 ATOM 2133 C C . ASP B 1 52 ? 13.557 -49.320 9.506 1.00 20.93 ? 104 ASP B C 1 ATOM 2134 O O . ASP B 1 52 ? 14.021 -48.500 10.305 1.00 19.65 ? 104 ASP B O 1 ATOM 2135 C CB . ASP B 1 52 ? 11.246 -48.473 10.137 1.00 21.06 ? 104 ASP B CB 1 ATOM 2136 C CG . ASP B 1 52 ? 9.780 -48.445 9.771 1.00 35.82 ? 104 ASP B CG 1 ATOM 2137 O OD1 . ASP B 1 52 ? 9.473 -48.383 8.563 1.00 37.48 ? 104 ASP B OD1 1 ATOM 2138 O OD2 . ASP B 1 52 ? 8.938 -48.505 10.693 1.00 51.94 ? 104 ASP B OD2 1 ATOM 2139 N N . TYR B 1 53 ? 14.292 -50.253 8.897 1.00 19.06 ? 105 TYR B N 1 ATOM 2140 C CA . TYR B 1 53 ? 15.723 -50.450 9.170 1.00 18.85 ? 105 TYR B CA 1 ATOM 2141 C C . TYR B 1 53 ? 16.561 -49.276 8.684 1.00 22.88 ? 105 TYR B C 1 ATOM 2142 O O . TYR B 1 53 ? 17.415 -48.779 9.424 1.00 20.44 ? 105 TYR B O 1 ATOM 2143 C CB . TYR B 1 53 ? 16.172 -51.799 8.563 1.00 19.62 ? 105 TYR B CB 1 ATOM 2144 C CG . TYR B 1 53 ? 17.570 -52.246 8.936 1.00 21.20 ? 105 TYR B CG 1 ATOM 2145 C CD1 . TYR B 1 53 ? 18.023 -52.162 10.250 1.00 23.37 ? 105 TYR B CD1 1 ATOM 2146 C CD2 . TYR B 1 53 ? 18.373 -52.909 8.016 1.00 25.15 ? 105 TYR B CD2 1 ATOM 2147 C CE1 . TYR B 1 53 ? 19.278 -52.651 10.615 1.00 24.25 ? 105 TYR B CE1 1 ATOM 2148 C CE2 . TYR B 1 53 ? 19.634 -53.387 8.365 1.00 26.51 ? 105 TYR B CE2 1 ATOM 2149 C CZ . TYR B 1 53 ? 20.074 -53.276 9.671 1.00 29.58 ? 105 TYR B CZ 1 ATOM 2150 O OH . TYR B 1 53 ? 21.322 -53.751 10.003 1.00 30.26 ? 105 TYR B OH 1 ATOM 2151 N N . GLU B 1 54 ? 16.239 -48.767 7.485 1.00 20.97 ? 106 GLU B N 1 ATOM 2152 C CA . GLU B 1 54 ? 16.929 -47.589 6.940 1.00 21.49 ? 106 GLU B CA 1 ATOM 2153 C C . GLU B 1 54 ? 16.724 -46.377 7.823 1.00 23.96 ? 106 GLU B C 1 ATOM 2154 O O . GLU B 1 54 ? 17.667 -45.623 8.063 1.00 24.27 ? 106 GLU B O 1 ATOM 2155 C CB . GLU B 1 54 ? 16.518 -47.323 5.484 1.00 24.11 ? 106 GLU B CB 1 ATOM 2156 C CG . GLU B 1 54 ? 16.916 -48.437 4.525 1.00 36.95 ? 106 GLU B CG 1 ATOM 2157 C CD . GLU B 1 54 ? 18.404 -48.740 4.473 1.00 66.70 ? 106 GLU B CD 1 ATOM 2158 O OE1 . GLU B 1 54 ? 19.212 -47.785 4.381 1.00 61.47 ? 106 GLU B OE1 1 ATOM 2159 O OE2 . GLU B 1 54 ? 18.760 -49.940 4.540 1.00 64.82 ? 106 GLU B OE2 1 ATOM 2160 N N . GLU B 1 55 ? 15.506 -46.225 8.356 1.00 20.71 ? 107 GLU B N 1 ATOM 2161 C CA . GLU B 1 55 ? 15.141 -45.148 9.273 1.00 20.13 ? 107 GLU B CA 1 ATOM 2162 C C . GLU B 1 55 ? 15.958 -45.219 10.581 1.00 20.16 ? 107 GLU B C 1 ATOM 2163 O O . GLU B 1 55 ? 16.408 -44.185 11.075 1.00 19.84 ? 107 GLU B O 1 ATOM 2164 C CB . GLU B 1 55 ? 13.637 -45.199 9.552 1.00 22.30 ? 107 GLU B CB 1 ATOM 2165 C CG . GLU B 1 55 ? 12.766 -44.919 8.322 1.00 37.00 ? 107 GLU B CG 1 ATOM 2166 C CD . GLU B 1 55 ? 12.916 -45.746 7.048 1.00 61.37 ? 107 GLU B CD 1 ATOM 2167 O OE1 . GLU B 1 55 ? 13.135 -46.981 7.126 1.00 33.35 ? 107 GLU B OE1 1 ATOM 2168 O OE2 . GLU B 1 55 ? 12.808 -45.139 5.956 1.00 64.31 ? 107 GLU B OE2 1 ATOM 2169 N N . LEU B 1 56 ? 16.215 -46.452 11.088 1.00 17.31 ? 108 LEU B N 1 ATOM 2170 C CA . LEU B 1 56 ? 17.032 -46.630 12.286 1.00 17.85 ? 108 LEU B CA 1 ATOM 2171 C C . LEU B 1 56 ? 18.473 -46.203 11.977 1.00 20.52 ? 108 LEU B C 1 ATOM 2172 O O . LEU B 1 56 ? 19.104 -45.490 12.763 1.00 19.27 ? 108 LEU B O 1 ATOM 2173 C CB . LEU B 1 56 ? 16.968 -48.085 12.809 1.00 17.04 ? 108 LEU B CB 1 ATOM 2174 C CG . LEU B 1 56 ? 17.831 -48.359 14.034 1.00 20.44 ? 108 LEU B CG 1 ATOM 2175 C CD1 . LEU B 1 56 ? 17.441 -47.463 15.225 1.00 20.88 ? 108 LEU B CD1 1 ATOM 2176 C CD2 . LEU B 1 56 ? 17.848 -49.808 14.354 1.00 23.28 ? 108 LEU B CD2 1 ATOM 2177 N N . LYS B 1 57 ? 18.976 -46.606 10.812 1.00 19.13 ? 109 LYS B N 1 ATOM 2178 C CA . LYS B 1 57 ? 20.320 -46.223 10.392 1.00 19.07 ? 109 LYS B CA 1 ATOM 2179 C C . LYS B 1 57 ? 20.421 -44.698 10.289 1.00 24.57 ? 109 LYS B C 1 ATOM 2180 O O . LYS B 1 57 ? 21.422 -44.119 10.730 1.00 26.18 ? 109 LYS B O 1 ATOM 2181 C CB . LYS B 1 57 ? 20.677 -46.894 9.072 1.00 20.71 ? 109 LYS B CB 1 ATOM 2182 C CG . LYS B 1 57 ? 20.892 -48.386 9.255 1.00 27.26 ? 109 LYS B CG 1 ATOM 2183 C CD . LYS B 1 57 ? 21.004 -49.079 7.924 1.00 32.49 ? 109 LYS B CD 1 ATOM 2184 C CE . LYS B 1 57 ? 21.895 -50.265 8.035 1.00 32.29 ? 109 LYS B CE 1 ATOM 2185 N NZ . LYS B 1 57 ? 22.160 -50.881 6.704 1.00 46.05 ? 109 LYS B NZ 1 ATOM 2186 N N . HIS B 1 58 ? 19.344 -44.036 9.836 1.00 21.62 ? 110 HIS B N 1 ATOM 2187 C CA . HIS B 1 58 ? 19.335 -42.574 9.800 1.00 23.06 ? 110 HIS B CA 1 ATOM 2188 C C . HIS B 1 58 ? 19.385 -41.965 11.204 1.00 25.48 ? 110 HIS B C 1 ATOM 2189 O O . HIS B 1 58 ? 20.054 -40.962 11.402 1.00 24.23 ? 110 HIS B O 1 ATOM 2190 C CB . HIS B 1 58 ? 18.104 -42.054 9.040 1.00 25.68 ? 110 HIS B CB 1 ATOM 2191 C CG . HIS B 1 58 ? 18.120 -40.574 8.819 1.00 31.51 ? 110 HIS B CG 1 ATOM 2192 N ND1 . HIS B 1 58 ? 19.276 -39.910 8.444 1.00 35.04 ? 110 HIS B ND1 1 ATOM 2193 C CD2 . HIS B 1 58 ? 17.106 -39.682 8.878 1.00 34.93 ? 110 HIS B CD2 1 ATOM 2194 C CE1 . HIS B 1 58 ? 18.934 -38.640 8.313 1.00 35.15 ? 110 HIS B CE1 1 ATOM 2195 N NE2 . HIS B 1 58 ? 17.642 -38.453 8.550 1.00 35.38 ? 110 HIS B NE2 1 ATOM 2196 N N . LEU B 1 59 ? 18.679 -42.551 12.178 1.00 21.62 ? 111 LEU B N 1 ATOM 2197 C CA . LEU B 1 59 ? 18.723 -42.046 13.558 1.00 22.25 ? 111 LEU B CA 1 ATOM 2198 C C . LEU B 1 59 ? 20.125 -42.221 14.112 1.00 24.98 ? 111 LEU B C 1 ATOM 2199 O O . LEU B 1 59 ? 20.651 -41.297 14.730 1.00 25.87 ? 111 LEU B O 1 ATOM 2200 C CB . LEU B 1 59 ? 17.678 -42.762 14.438 1.00 22.14 ? 111 LEU B CB 1 ATOM 2201 C CG . LEU B 1 59 ? 17.925 -42.772 15.965 1.00 28.50 ? 111 LEU B CG 1 ATOM 2202 C CD1 . LEU B 1 59 ? 17.546 -41.485 16.601 1.00 29.66 ? 111 LEU B CD1 1 ATOM 2203 C CD2 . LEU B 1 59 ? 17.174 -43.915 16.633 1.00 30.79 ? 111 LEU B CD2 1 ATOM 2204 N N . LEU B 1 60 ? 20.769 -43.370 13.821 1.00 21.88 ? 112 LEU B N 1 ATOM 2205 C CA . LEU B 1 60 ? 22.133 -43.635 14.284 1.00 23.24 ? 112 LEU B CA 1 ATOM 2206 C C . LEU B 1 60 ? 23.173 -42.625 13.793 1.00 26.06 ? 112 LEU B C 1 ATOM 2207 O O . LEU B 1 60 ? 24.197 -42.423 14.464 1.00 25.68 ? 112 LEU B O 1 ATOM 2208 C CB . LEU B 1 60 ? 22.568 -45.067 14.029 1.00 23.48 ? 112 LEU B CB 1 ATOM 2209 C CG . LEU B 1 60 ? 21.677 -46.121 14.679 1.00 28.48 ? 112 LEU B CG 1 ATOM 2210 C CD1 . LEU B 1 60 ? 22.029 -47.478 14.199 1.00 29.35 ? 112 LEU B CD1 1 ATOM 2211 C CD2 . LEU B 1 60 ? 21.796 -46.095 16.161 1.00 32.55 ? 112 LEU B CD2 1 ATOM 2212 N N A SER B 1 61 ? 22.894 -41.957 12.657 0.50 23.47 ? 113 SER B N 1 ATOM 2213 N N B SER B 1 61 ? 22.898 -41.960 12.650 0.50 21.89 ? 113 SER B N 1 ATOM 2214 C CA A SER B 1 61 ? 23.753 -40.916 12.110 0.50 24.13 ? 113 SER B CA 1 ATOM 2215 C CA B SER B 1 61 ? 23.770 -40.924 12.115 0.50 21.76 ? 113 SER B CA 1 ATOM 2216 C C A SER B 1 61 ? 23.882 -39.708 13.055 0.50 28.52 ? 113 SER B C 1 ATOM 2217 C C B SER B 1 61 ? 23.891 -39.712 13.062 0.50 27.40 ? 113 SER B C 1 ATOM 2218 O O A SER B 1 61 ? 24.864 -38.973 12.958 0.50 29.01 ? 113 SER B O 1 ATOM 2219 O O B SER B 1 61 ? 24.878 -38.982 12.977 0.50 27.83 ? 113 SER B O 1 ATOM 2220 C CB A SER B 1 61 ? 23.249 -40.459 10.743 0.50 29.83 ? 113 SER B CB 1 ATOM 2221 C CB B SER B 1 61 ? 23.323 -40.486 10.720 0.50 24.69 ? 113 SER B CB 1 ATOM 2222 O OG A SER B 1 61 ? 23.143 -41.552 9.847 0.50 39.92 ? 113 SER B OG 1 ATOM 2223 O OG B SER B 1 61 ? 22.227 -39.586 10.748 0.50 23.01 ? 113 SER B OG 1 ATOM 2224 N N . SER B 1 62 ? 22.907 -39.526 13.980 1.00 24.06 ? 114 SER B N 1 ATOM 2225 C CA . SER B 1 62 ? 22.893 -38.405 14.940 1.00 22.98 ? 114 SER B CA 1 ATOM 2226 C C . SER B 1 62 ? 23.197 -38.861 16.378 1.00 25.83 ? 114 SER B C 1 ATOM 2227 O O . SER B 1 62 ? 23.092 -38.067 17.319 1.00 27.64 ? 114 SER B O 1 ATOM 2228 C CB . SER B 1 62 ? 21.538 -37.704 14.901 1.00 28.30 ? 114 SER B CB 1 ATOM 2229 O OG . SER B 1 62 ? 20.529 -38.613 15.317 1.00 36.16 ? 114 SER B OG 1 ATOM 2230 N N . VAL B 1 63 ? 23.474 -40.152 16.561 1.00 19.36 ? 115 VAL B N 1 ATOM 2231 C CA . VAL B 1 63 ? 23.797 -40.726 17.872 1.00 17.82 ? 115 VAL B CA 1 ATOM 2232 C C . VAL B 1 63 ? 25.280 -40.989 17.878 1.00 21.60 ? 115 VAL B C 1 ATOM 2233 O O . VAL B 1 63 ? 25.789 -41.511 16.888 1.00 19.45 ? 115 VAL B O 1 ATOM 2234 C CB . VAL B 1 63 ? 23.005 -42.043 18.135 1.00 20.49 ? 115 VAL B CB 1 ATOM 2235 C CG1 . VAL B 1 63 ? 23.437 -42.720 19.422 1.00 19.62 ? 115 VAL B CG1 1 ATOM 2236 C CG2 . VAL B 1 63 ? 21.514 -41.776 18.163 1.00 21.16 ? 115 VAL B CG2 1 ATOM 2237 N N . LYS B 1 64 ? 25.961 -40.649 18.994 1.00 16.76 ? 116 LYS B N 1 ATOM 2238 C CA . LYS B 1 64 ? 27.408 -40.887 19.169 1.00 17.05 ? 116 LYS B CA 1 ATOM 2239 C C . LYS B 1 64 ? 27.755 -41.803 20.342 1.00 20.95 ? 116 LYS B C 1 ATOM 2240 O O . LYS B 1 64 ? 28.936 -42.150 20.524 1.00 19.99 ? 116 LYS B O 1 ATOM 2241 C CB . LYS B 1 64 ? 28.165 -39.558 19.233 1.00 17.76 ? 116 LYS B CB 1 ATOM 2242 C CG . LYS B 1 64 ? 28.031 -38.767 17.952 1.00 21.73 ? 116 LYS B CG 1 ATOM 2243 C CD . LYS B 1 64 ? 28.596 -39.528 16.750 1.00 22.77 ? 116 LYS B CD 1 ATOM 2244 C CE . LYS B 1 64 ? 28.335 -38.852 15.449 1.00 19.94 ? 116 LYS B CE 1 ATOM 2245 N NZ . LYS B 1 64 ? 27.116 -39.343 14.777 1.00 22.80 ? 116 LYS B NZ 1 ATOM 2246 N N . HIS B 1 65 A 26.737 -42.209 21.146 1.00 16.55 ? 116 HIS B N 1 ATOM 2247 C CA . HIS B 1 65 A 26.976 -43.119 22.244 1.00 16.75 ? 116 HIS B CA 1 ATOM 2248 C C . HIS B 1 65 A 25.672 -43.598 22.788 1.00 22.15 ? 116 HIS B C 1 ATOM 2249 O O . HIS B 1 65 A 24.732 -42.818 22.909 1.00 20.55 ? 116 HIS B O 1 ATOM 2250 C CB . HIS B 1 65 A 27.782 -42.466 23.406 1.00 18.45 ? 116 HIS B CB 1 ATOM 2251 C CG . HIS B 1 65 A 28.349 -43.475 24.343 1.00 22.21 ? 116 HIS B CG 1 ATOM 2252 N ND1 . HIS B 1 65 A 28.388 -43.248 25.693 1.00 25.20 ? 116 HIS B ND1 1 ATOM 2253 C CD2 . HIS B 1 65 A 28.850 -44.713 24.083 1.00 23.68 ? 116 HIS B CD2 1 ATOM 2254 C CE1 . HIS B 1 65 A 28.899 -44.356 26.224 1.00 24.89 ? 116 HIS B CE1 1 ATOM 2255 N NE2 . HIS B 1 65 A 29.216 -45.251 25.290 1.00 24.56 ? 116 HIS B NE2 1 ATOM 2256 N N . PHE B 1 66 B 25.645 -44.870 23.186 1.00 18.93 ? 116 PHE B N 1 ATOM 2257 C CA . PHE B 1 66 B 24.520 -45.490 23.835 1.00 18.85 ? 116 PHE B CA 1 ATOM 2258 C C . PHE B 1 66 B 24.985 -45.998 25.192 1.00 26.93 ? 116 PHE B C 1 ATOM 2259 O O . PHE B 1 66 B 26.138 -46.422 25.343 1.00 27.28 ? 116 PHE B O 1 ATOM 2260 C CB . PHE B 1 66 B 24.083 -46.751 23.062 1.00 20.02 ? 116 PHE B CB 1 ATOM 2261 C CG . PHE B 1 66 B 23.232 -46.524 21.847 1.00 20.93 ? 116 PHE B CG 1 ATOM 2262 C CD1 . PHE B 1 66 B 22.059 -45.777 21.929 1.00 25.41 ? 116 PHE B CD1 1 ATOM 2263 C CD2 . PHE B 1 66 B 23.553 -47.115 20.642 1.00 23.19 ? 116 PHE B CD2 1 ATOM 2264 C CE1 . PHE B 1 66 B 21.244 -45.598 20.805 1.00 25.51 ? 116 PHE B CE1 1 ATOM 2265 C CE2 . PHE B 1 66 B 22.719 -46.967 19.529 1.00 26.26 ? 116 PHE B CE2 1 ATOM 2266 C CZ . PHE B 1 66 B 21.573 -46.204 19.623 1.00 25.49 ? 116 PHE B CZ 1 ATOM 2267 N N . GLU B 1 67 C 24.080 -46.011 26.162 1.00 21.62 ? 116 GLU B N 1 ATOM 2268 C CA . GLU B 1 67 C 24.332 -46.696 27.430 1.00 22.54 ? 116 GLU B CA 1 ATOM 2269 C C . GLU B 1 67 C 23.270 -47.786 27.469 1.00 21.51 ? 116 GLU B C 1 ATOM 2270 O O . GLU B 1 67 C 22.108 -47.469 27.342 1.00 19.62 ? 116 GLU B O 1 ATOM 2271 C CB . GLU B 1 67 C 24.181 -45.755 28.630 1.00 25.53 ? 116 GLU B CB 1 ATOM 2272 C CG . GLU B 1 67 C 25.385 -44.831 28.754 1.00 39.06 ? 116 GLU B CG 1 ATOM 2273 C CD . GLU B 1 67 C 25.251 -43.618 29.655 1.00 63.25 ? 116 GLU B CD 1 ATOM 2274 O OE1 . GLU B 1 67 C 24.115 -43.286 30.064 1.00 55.93 ? 116 GLU B OE1 1 ATOM 2275 O OE2 . GLU B 1 67 C 26.285 -42.955 29.896 1.00 63.27 ? 116 GLU B OE2 1 ATOM 2276 N N . LYS B 1 68 ? 23.665 -49.062 27.540 1.00 21.15 ? 117 LYS B N 1 ATOM 2277 C CA . LYS B 1 68 ? 22.685 -50.174 27.646 1.00 21.30 ? 117 LYS B CA 1 ATOM 2278 C C . LYS B 1 68 ? 22.074 -50.149 29.048 1.00 25.65 ? 117 LYS B C 1 ATOM 2279 O O . LYS B 1 68 ? 22.805 -50.056 30.051 1.00 28.95 ? 117 LYS B O 1 ATOM 2280 C CB . LYS B 1 68 ? 23.362 -51.537 27.394 1.00 25.72 ? 117 LYS B CB 1 ATOM 2281 C CG . LYS B 1 68 ? 22.906 -52.229 26.118 1.00 37.97 ? 117 LYS B CG 1 ATOM 2282 C CD . LYS B 1 68 ? 23.880 -53.309 25.615 1.00 31.95 ? 117 LYS B CD 1 ATOM 2283 C CE . LYS B 1 68 ? 23.773 -54.590 26.382 1.00 33.26 ? 117 LYS B CE 1 ATOM 2284 N NZ . LYS B 1 68 ? 24.626 -55.641 25.757 1.00 33.70 ? 117 LYS B NZ 1 ATOM 2285 N N . VAL B 1 69 ? 20.746 -50.183 29.124 1.00 19.84 ? 118 VAL B N 1 ATOM 2286 C CA . VAL B 1 69 ? 19.953 -50.123 30.370 1.00 21.44 ? 118 VAL B CA 1 ATOM 2287 C C . VAL B 1 69 ? 19.086 -51.389 30.487 1.00 22.39 ? 118 VAL B C 1 ATOM 2288 O O . VAL B 1 69 ? 18.364 -51.725 29.540 1.00 20.94 ? 118 VAL B O 1 ATOM 2289 C CB . VAL B 1 69 ? 19.093 -48.817 30.370 1.00 24.89 ? 118 VAL B CB 1 ATOM 2290 C CG1 . VAL B 1 69 ? 18.004 -48.818 31.454 1.00 26.17 ? 118 VAL B CG1 1 ATOM 2291 C CG2 . VAL B 1 69 ? 19.976 -47.575 30.478 1.00 24.92 ? 118 VAL B CG2 1 ATOM 2292 N N . LYS B 1 70 ? 19.134 -52.107 31.643 1.00 22.11 ? 119 LYS B N 1 ATOM 2293 C CA . LYS B 1 70 ? 18.282 -53.303 31.769 1.00 22.53 ? 119 LYS B CA 1 ATOM 2294 C C . LYS B 1 70 ? 16.850 -52.856 32.079 1.00 28.96 ? 119 LYS B C 1 ATOM 2295 O O . LYS B 1 70 ? 16.568 -52.415 33.191 1.00 34.67 ? 119 LYS B O 1 ATOM 2296 C CB . LYS B 1 70 ? 18.802 -54.279 32.828 1.00 25.74 ? 119 LYS B CB 1 ATOM 2297 C CG . LYS B 1 70 ? 18.217 -55.692 32.701 1.00 31.97 ? 119 LYS B CG 1 ATOM 2298 C CD . LYS B 1 70 ? 18.893 -56.696 33.634 1.00 36.97 ? 119 LYS B CD 1 ATOM 2299 C CE . LYS B 1 70 ? 20.040 -57.405 32.952 1.00 50.71 ? 119 LYS B CE 1 ATOM 2300 N NZ . LYS B 1 70 ? 20.838 -58.207 33.911 1.00 61.02 ? 119 LYS B NZ 1 ATOM 2301 N N . ILE B 1 71 ? 15.977 -52.899 31.076 1.00 20.62 ? 120 ILE B N 1 ATOM 2302 C CA . ILE B 1 71 ? 14.572 -52.447 31.171 1.00 20.52 ? 120 ILE B CA 1 ATOM 2303 C C . ILE B 1 71 ? 13.607 -53.561 31.555 1.00 25.00 ? 120 ILE B C 1 ATOM 2304 O O . ILE B 1 71 ? 12.550 -53.305 32.148 1.00 25.62 ? 120 ILE B O 1 ATOM 2305 C CB . ILE B 1 71 ? 14.124 -51.736 29.864 1.00 22.47 ? 120 ILE B CB 1 ATOM 2306 C CG1 . ILE B 1 71 ? 14.176 -52.659 28.614 1.00 22.44 ? 120 ILE B CG1 1 ATOM 2307 C CG2 . ILE B 1 71 ? 14.957 -50.473 29.641 1.00 24.74 ? 120 ILE B CG2 1 ATOM 2308 C CD1 . ILE B 1 71 ? 13.563 -52.033 27.316 1.00 24.47 ? 120 ILE B CD1 1 ATOM 2309 N N . LEU B 1 72 ? 13.905 -54.783 31.124 1.00 21.32 ? 121 LEU B N 1 ATOM 2310 C CA . LEU B 1 72 ? 13.032 -55.922 31.405 1.00 21.22 ? 121 LEU B CA 1 ATOM 2311 C C . LEU B 1 72 ? 13.908 -57.120 31.821 1.00 23.33 ? 121 LEU B C 1 ATOM 2312 O O . LEU B 1 72 ? 14.157 -58.022 31.010 1.00 21.03 ? 121 LEU B O 1 ATOM 2313 C CB . LEU B 1 72 ? 12.167 -56.256 30.179 1.00 21.41 ? 121 LEU B CB 1 ATOM 2314 C CG . LEU B 1 72 ? 11.005 -55.289 29.826 1.00 27.32 ? 121 LEU B CG 1 ATOM 2315 C CD1 . LEU B 1 72 ? 10.433 -55.611 28.447 1.00 26.67 ? 121 LEU B CD1 1 ATOM 2316 C CD2 . LEU B 1 72 ? 9.858 -55.394 30.821 1.00 28.16 ? 121 LEU B CD2 1 ATOM 2317 N N . PRO B 1 73 ? 14.410 -57.140 33.076 1.00 23.35 ? 122 PRO B N 1 ATOM 2318 C CA . PRO B 1 73 ? 15.257 -58.269 33.506 1.00 23.74 ? 122 PRO B CA 1 ATOM 2319 C C . PRO B 1 73 ? 14.585 -59.616 33.247 1.00 27.21 ? 122 PRO B C 1 ATOM 2320 O O . PRO B 1 73 ? 13.403 -59.755 33.560 1.00 26.82 ? 122 PRO B O 1 ATOM 2321 C CB . PRO B 1 73 ? 15.429 -58.033 35.022 1.00 27.03 ? 122 PRO B CB 1 ATOM 2322 C CG . PRO B 1 73 ? 15.172 -56.567 35.217 1.00 31.28 ? 122 PRO B CG 1 ATOM 2323 C CD . PRO B 1 73 ? 14.198 -56.156 34.158 1.00 25.44 ? 122 PRO B CD 1 ATOM 2324 N N . LYS B 1 74 ? 15.315 -60.585 32.649 1.00 22.73 ? 123 LYS B N 1 ATOM 2325 C CA . LYS B 1 74 ? 14.843 -61.958 32.338 1.00 23.55 ? 123 LYS B CA 1 ATOM 2326 C C . LYS B 1 74 ? 14.160 -62.626 33.536 1.00 25.95 ? 123 LYS B C 1 ATOM 2327 O O . LYS B 1 74 ? 13.217 -63.417 33.347 1.00 23.98 ? 123 LYS B O 1 ATOM 2328 C CB . LYS B 1 74 ? 16.020 -62.865 31.913 1.00 28.21 ? 123 LYS B CB 1 ATOM 2329 C CG . LYS B 1 74 ? 16.409 -62.799 30.457 1.00 50.03 ? 123 LYS B CG 1 ATOM 2330 C CD . LYS B 1 74 ? 16.976 -64.131 29.954 1.00 63.54 ? 123 LYS B CD 1 ATOM 2331 C CE . LYS B 1 74 ? 18.480 -64.227 30.058 1.00 79.52 ? 123 LYS B CE 1 ATOM 2332 N NZ . LYS B 1 74 ? 18.996 -65.468 29.422 1.00 89.94 ? 123 LYS B NZ 1 ATOM 2333 N N . ASP B 1 75 ? 14.639 -62.309 34.776 1.00 22.58 ? 125 ASP B N 1 ATOM 2334 C CA . ASP B 1 75 ? 14.091 -62.881 36.009 1.00 23.56 ? 125 ASP B CA 1 ATOM 2335 C C . ASP B 1 75 ? 12.611 -62.557 36.266 1.00 25.39 ? 125 ASP B C 1 ATOM 2336 O O . ASP B 1 75 ? 11.956 -63.240 37.055 1.00 24.95 ? 125 ASP B O 1 ATOM 2337 C CB . ASP B 1 75 ? 14.975 -62.548 37.222 1.00 27.61 ? 125 ASP B CB 1 ATOM 2338 C CG . ASP B 1 75 ? 14.963 -61.112 37.730 1.00 42.37 ? 125 ASP B CG 1 ATOM 2339 O OD1 . ASP B 1 75 ? 14.284 -60.265 37.112 1.00 40.18 ? 125 ASP B OD1 1 ATOM 2340 O OD2 . ASP B 1 75 ? 15.615 -60.843 38.769 1.00 53.21 ? 125 ASP B OD2 1 ATOM 2341 N N . ARG B 1 76 ? 12.083 -61.523 35.614 1.00 22.13 ? 126 ARG B N 1 ATOM 2342 C CA . ARG B 1 76 ? 10.677 -61.147 35.806 1.00 21.93 ? 126 ARG B CA 1 ATOM 2343 C C . ARG B 1 76 ? 9.686 -62.167 35.212 1.00 24.01 ? 126 ARG B C 1 ATOM 2344 O O . ARG B 1 76 ? 8.520 -62.181 35.596 1.00 24.57 ? 126 ARG B O 1 ATOM 2345 C CB . ARG B 1 76 ? 10.409 -59.747 35.220 1.00 21.06 ? 126 ARG B CB 1 ATOM 2346 C CG . ARG B 1 76 ? 10.350 -59.708 33.689 1.00 22.70 ? 126 ARG B CG 1 ATOM 2347 C CD . ARG B 1 76 ? 10.164 -58.287 33.143 1.00 24.64 ? 126 ARG B CD 1 ATOM 2348 N NE . ARG B 1 76 ? 9.042 -57.593 33.791 1.00 26.61 ? 126 ARG B NE 1 ATOM 2349 C CZ . ARG B 1 76 ? 7.762 -57.862 33.551 1.00 31.47 ? 126 ARG B CZ 1 ATOM 2350 N NH1 . ARG B 1 76 ? 7.430 -58.823 32.711 1.00 29.51 ? 126 ARG B NH1 1 ATOM 2351 N NH2 . ARG B 1 76 ? 6.807 -57.213 34.201 1.00 32.90 ? 126 ARG B NH2 1 ATOM 2352 N N . TRP B 1 77 ? 10.141 -63.006 34.268 1.00 18.54 ? 127 TRP B N 1 ATOM 2353 C CA . TRP B 1 77 ? 9.281 -63.938 33.557 1.00 18.68 ? 127 TRP B CA 1 ATOM 2354 C C . TRP B 1 77 ? 9.175 -65.275 34.252 1.00 23.33 ? 127 TRP B C 1 ATOM 2355 O O . TRP B 1 77 ? 9.670 -66.286 33.760 1.00 24.87 ? 127 TRP B O 1 ATOM 2356 C CB . TRP B 1 77 ? 9.790 -64.097 32.114 1.00 17.24 ? 127 TRP B CB 1 ATOM 2357 C CG . TRP B 1 77 ? 9.980 -62.808 31.358 1.00 16.81 ? 127 TRP B CG 1 ATOM 2358 C CD1 . TRP B 1 77 ? 11.161 -62.310 30.885 1.00 19.14 ? 127 TRP B CD1 1 ATOM 2359 C CD2 . TRP B 1 77 ? 8.960 -61.930 30.887 1.00 16.51 ? 127 TRP B CD2 1 ATOM 2360 N NE1 . TRP B 1 77 ? 10.939 -61.145 30.188 1.00 19.23 ? 127 TRP B NE1 1 ATOM 2361 C CE2 . TRP B 1 77 ? 9.596 -60.904 30.144 1.00 20.47 ? 127 TRP B CE2 1 ATOM 2362 C CE3 . TRP B 1 77 ? 7.553 -61.932 30.968 1.00 18.46 ? 127 TRP B CE3 1 ATOM 2363 C CZ2 . TRP B 1 77 ? 8.889 -59.837 29.566 1.00 19.47 ? 127 TRP B CZ2 1 ATOM 2364 C CZ3 . TRP B 1 77 ? 6.850 -60.887 30.365 1.00 19.31 ? 127 TRP B CZ3 1 ATOM 2365 C CH2 . TRP B 1 77 ? 7.518 -59.874 29.646 1.00 19.86 ? 127 TRP B CH2 1 ATOM 2366 N N . THR B 1 78 ? 8.505 -65.290 35.402 1.00 21.41 ? 128 THR B N 1 ATOM 2367 C CA . THR B 1 78 ? 8.377 -66.503 36.220 1.00 21.20 ? 128 THR B CA 1 ATOM 2368 C C . THR B 1 78 ? 7.406 -67.535 35.691 1.00 25.39 ? 128 THR B C 1 ATOM 2369 O O . THR B 1 78 ? 7.386 -68.656 36.210 1.00 26.89 ? 128 THR B O 1 ATOM 2370 C CB . THR B 1 78 ? 7.975 -66.116 37.643 1.00 29.29 ? 128 THR B CB 1 ATOM 2371 O OG1 . THR B 1 78 ? 6.686 -65.486 37.609 1.00 26.64 ? 128 THR B OG1 1 ATOM 2372 C CG2 . THR B 1 78 ? 9.005 -65.227 38.303 1.00 25.11 ? 128 THR B CG2 1 ATOM 2373 N N . GLN B 1 79 ? 6.543 -67.170 34.726 1.00 21.21 ? 129 GLN B N 1 ATOM 2374 C CA . GLN B 1 79 ? 5.555 -68.141 34.223 1.00 20.60 ? 129 GLN B CA 1 ATOM 2375 C C . GLN B 1 79 ? 5.831 -68.546 32.798 1.00 21.11 ? 129 GLN B C 1 ATOM 2376 O O . GLN B 1 79 ? 5.040 -69.256 32.207 1.00 20.04 ? 129 GLN B O 1 ATOM 2377 C CB . GLN B 1 79 ? 4.122 -67.613 34.358 1.00 22.36 ? 129 GLN B CB 1 ATOM 2378 C CG . GLN B 1 79 ? 3.798 -67.147 35.763 1.00 20.15 ? 129 GLN B CG 1 ATOM 2379 C CD . GLN B 1 79 ? 3.868 -68.240 36.810 1.00 26.61 ? 129 GLN B CD 1 ATOM 2380 O OE1 . GLN B 1 79 ? 3.544 -69.405 36.575 1.00 24.88 ? 129 GLN B OE1 1 ATOM 2381 N NE2 . GLN B 1 79 ? 4.244 -67.863 38.008 1.00 24.31 ? 129 GLN B NE2 1 ATOM 2382 N N . HIS B 1 80 ? 6.985 -68.130 32.265 1.00 17.54 ? 130 HIS B N 1 ATOM 2383 C CA . HIS B 1 80 ? 7.363 -68.504 30.912 1.00 16.73 ? 130 HIS B CA 1 ATOM 2384 C C . HIS B 1 80 ? 8.778 -69.068 30.959 1.00 21.11 ? 130 HIS B C 1 ATOM 2385 O O . HIS B 1 80 ? 9.559 -68.717 31.845 1.00 21.31 ? 130 HIS B O 1 ATOM 2386 C CB . HIS B 1 80 ? 7.366 -67.237 30.009 1.00 15.51 ? 130 HIS B CB 1 ATOM 2387 C CG . HIS B 1 80 ? 6.004 -66.646 29.834 1.00 18.58 ? 130 HIS B CG 1 ATOM 2388 N ND1 . HIS B 1 80 ? 5.479 -65.765 30.760 1.00 20.24 ? 130 HIS B ND1 1 ATOM 2389 C CD2 . HIS B 1 80 ? 5.059 -66.917 28.901 1.00 20.29 ? 130 HIS B CD2 1 ATOM 2390 C CE1 . HIS B 1 80 ? 4.252 -65.485 30.341 1.00 20.42 ? 130 HIS B CE1 1 ATOM 2391 N NE2 . HIS B 1 80 ? 3.959 -66.149 29.218 1.00 20.45 ? 130 HIS B NE2 1 ATOM 2392 N N . THR B 1 81 ? 9.131 -69.871 29.959 1.00 17.42 ? 131 THR B N 1 ATOM 2393 C CA . THR B 1 81 ? 10.505 -70.330 29.789 1.00 17.73 ? 131 THR B CA 1 ATOM 2394 C C . THR B 1 81 ? 11.252 -69.176 29.074 1.00 20.01 ? 131 THR B C 1 ATOM 2395 O O . THR B 1 81 ? 10.703 -68.566 28.162 1.00 16.93 ? 131 THR B O 1 ATOM 2396 C CB . THR B 1 81 ? 10.532 -71.648 29.010 1.00 18.88 ? 131 THR B CB 1 ATOM 2397 O OG1 . THR B 1 81 ? 9.827 -72.670 29.742 1.00 21.96 ? 131 THR B OG1 1 ATOM 2398 C CG2 . THR B 1 81 ? 11.931 -72.147 28.744 1.00 21.66 ? 131 THR B CG2 1 ATOM 2399 N N . THR B 1 82 ? 12.497 -68.865 29.516 1.00 16.91 ? 132 THR B N 1 ATOM 2400 C CA . THR B 1 82 ? 13.292 -67.805 28.911 1.00 16.64 ? 132 THR B CA 1 ATOM 2401 C C . THR B 1 82 ? 14.658 -68.284 28.359 1.00 19.48 ? 132 THR B C 1 ATOM 2402 O O . THR B 1 82 ? 15.403 -67.466 27.845 1.00 19.37 ? 132 THR B O 1 ATOM 2403 C CB . THR B 1 82 ? 13.560 -66.690 29.940 1.00 22.47 ? 132 THR B CB 1 ATOM 2404 O OG1 . THR B 1 82 ? 14.298 -67.242 31.044 1.00 25.18 ? 132 THR B OG1 1 ATOM 2405 C CG2 . THR B 1 82 ? 12.284 -66.024 30.441 1.00 22.24 ? 132 THR B CG2 1 ATOM 2406 N N . THR B 1 83 ? 14.942 -69.566 28.430 1.00 20.75 ? 133 THR B N 1 ATOM 2407 C CA . THR B 1 83 ? 16.233 -70.178 28.024 1.00 21.17 ? 133 THR B CA 1 ATOM 2408 C C . THR B 1 83 ? 16.298 -70.510 26.518 1.00 25.42 ? 133 THR B C 1 ATOM 2409 O O . THR B 1 83 ? 17.324 -71.014 26.042 1.00 25.65 ? 133 THR B O 1 ATOM 2410 C CB . THR B 1 83 ? 16.429 -71.491 28.819 1.00 27.41 ? 133 THR B CB 1 ATOM 2411 O OG1 . THR B 1 83 ? 15.311 -72.363 28.565 1.00 27.47 ? 133 THR B OG1 1 ATOM 2412 C CG2 . THR B 1 83 ? 16.597 -71.258 30.321 1.00 29.45 ? 133 THR B CG2 1 ATOM 2413 N N . GLY B 1 84 ? 15.215 -70.248 25.809 1.00 21.09 ? 134 GLY B N 1 ATOM 2414 C CA . GLY B 1 84 ? 15.062 -70.590 24.397 1.00 21.80 ? 134 GLY B CA 1 ATOM 2415 C C . GLY B 1 84 ? 16.238 -70.131 23.565 1.00 24.36 ? 134 GLY B C 1 ATOM 2416 O O . GLY B 1 84 ? 16.605 -68.961 23.604 1.00 21.38 ? 134 GLY B O 1 ATOM 2417 N N . GLY B 1 85 ? 16.825 -71.082 22.861 1.00 22.95 ? 135 GLY B N 1 ATOM 2418 C CA . GLY B 1 85 ? 17.948 -70.856 21.964 1.00 22.49 ? 135 GLY B CA 1 ATOM 2419 C C . GLY B 1 85 ? 17.791 -71.657 20.686 1.00 24.73 ? 135 GLY B C 1 ATOM 2420 O O . GLY B 1 85 ? 16.997 -72.611 20.629 1.00 26.37 ? 135 GLY B O 1 ATOM 2421 N N . SER B 1 86 ? 18.547 -71.292 19.657 1.00 20.52 ? 136 SER B N 1 ATOM 2422 C CA . SER B 1 86 ? 18.466 -71.997 18.370 1.00 20.25 ? 136 SER B CA 1 ATOM 2423 C C . SER B 1 86 ? 19.858 -72.332 17.862 1.00 23.22 ? 136 SER B C 1 ATOM 2424 O O . SER B 1 86 ? 20.828 -71.608 18.194 1.00 20.58 ? 136 SER B O 1 ATOM 2425 C CB . SER B 1 86 ? 17.757 -71.108 17.345 1.00 22.17 ? 136 SER B CB 1 ATOM 2426 O OG . SER B 1 86 ? 17.734 -71.734 16.070 1.00 27.00 ? 136 SER B OG 1 ATOM 2427 N N . ARG B 1 87 ? 19.963 -73.403 17.012 1.00 21.39 ? 137 ARG B N 1 ATOM 2428 C CA . ARG B 1 87 ? 21.264 -73.735 16.414 1.00 23.37 ? 137 ARG B CA 1 ATOM 2429 C C . ARG B 1 87 ? 21.613 -72.593 15.413 1.00 27.10 ? 137 ARG B C 1 ATOM 2430 O O . ARG B 1 87 ? 22.770 -72.449 14.993 1.00 29.29 ? 137 ARG B O 1 ATOM 2431 C CB . ARG B 1 87 ? 21.242 -75.108 15.710 1.00 23.28 ? 137 ARG B CB 1 ATOM 2432 C CG . ARG B 1 87 ? 20.774 -76.255 16.602 1.00 44.99 ? 137 ARG B CG 1 ATOM 2433 C CD . ARG B 1 87 ? 21.573 -77.523 16.386 1.00 57.30 ? 137 ARG B CD 1 ATOM 2434 N NE . ARG B 1 87 ? 22.745 -77.582 17.262 1.00 65.86 ? 137 ARG B NE 1 ATOM 2435 C CZ . ARG B 1 87 ? 22.739 -78.076 18.498 1.00 80.11 ? 137 ARG B CZ 1 ATOM 2436 N NH1 . ARG B 1 87 ? 21.617 -78.553 19.025 1.00 64.37 ? 137 ARG B NH1 1 ATOM 2437 N NH2 . ARG B 1 87 ? 23.852 -78.090 19.218 1.00 69.01 ? 137 ARG B NH2 1 ATOM 2438 N N . ALA B 1 88 ? 20.618 -71.772 15.052 1.00 23.52 ? 138 ALA B N 1 ATOM 2439 C CA . ALA B 1 88 ? 20.864 -70.623 14.175 1.00 22.68 ? 138 ALA B CA 1 ATOM 2440 C C . ALA B 1 88 ? 21.730 -69.563 14.863 1.00 29.66 ? 138 ALA B C 1 ATOM 2441 O O . ALA B 1 88 ? 22.400 -68.809 14.165 1.00 32.67 ? 138 ALA B O 1 ATOM 2442 C CB . ALA B 1 88 ? 19.550 -70.008 13.739 1.00 22.69 ? 138 ALA B CB 1 ATOM 2443 N N . CYS B 1 89 ? 21.743 -69.513 16.206 1.00 27.90 ? 139 CYS B N 1 ATOM 2444 C CA . CYS B 1 89 ? 22.552 -68.543 16.981 1.00 29.33 ? 139 CYS B CA 1 ATOM 2445 C C . CYS B 1 89 ? 23.540 -69.305 17.882 1.00 30.94 ? 139 CYS B C 1 ATOM 2446 O O . CYS B 1 89 ? 23.775 -68.910 19.028 1.00 28.18 ? 139 CYS B O 1 ATOM 2447 C CB . CYS B 1 89 ? 21.664 -67.601 17.796 1.00 32.04 ? 139 CYS B CB 1 ATOM 2448 S SG . CYS B 1 89 ? 20.488 -66.613 16.816 1.00 37.16 ? 139 CYS B SG 1 ATOM 2449 N N . ALA B 1 90 ? 24.109 -70.408 17.358 1.00 30.07 ? 140 ALA B N 1 ATOM 2450 C CA . ALA B 1 90 ? 24.974 -71.314 18.104 1.00 30.64 ? 140 ALA B CA 1 ATOM 2451 C C . ALA B 1 90 ? 26.256 -70.698 18.653 1.00 34.12 ? 140 ALA B C 1 ATOM 2452 O O . ALA B 1 90 ? 26.924 -69.946 17.950 1.00 35.46 ? 140 ALA B O 1 ATOM 2453 C CB . ALA B 1 90 ? 25.289 -72.549 17.280 1.00 32.01 ? 140 ALA B CB 1 ATOM 2454 N N . VAL B 1 91 ? 26.605 -71.042 19.906 1.00 28.81 ? 141 VAL B N 1 ATOM 2455 C CA . VAL B 1 91 ? 27.829 -70.576 20.593 1.00 28.45 ? 141 VAL B CA 1 ATOM 2456 C C . VAL B 1 91 ? 28.530 -71.788 21.247 1.00 33.74 ? 141 VAL B C 1 ATOM 2457 O O . VAL B 1 91 ? 27.921 -72.464 22.085 1.00 30.95 ? 141 VAL B O 1 ATOM 2458 C CB . VAL B 1 91 ? 27.531 -69.462 21.629 1.00 31.81 ? 141 VAL B CB 1 ATOM 2459 C CG1 . VAL B 1 91 ? 28.791 -69.058 22.399 1.00 32.20 ? 141 VAL B CG1 1 ATOM 2460 C CG2 . VAL B 1 91 ? 26.902 -68.242 20.967 1.00 30.83 ? 141 VAL B CG2 1 ATOM 2461 N N . SER B 1 92 ? 29.816 -72.030 20.878 1.00 33.20 ? 142 SER B N 1 ATOM 2462 C CA . SER B 1 92 ? 30.624 -73.159 21.354 1.00 34.81 ? 142 SER B CA 1 ATOM 2463 C C . SER B 1 92 ? 29.870 -74.502 21.205 1.00 38.01 ? 142 SER B C 1 ATOM 2464 O O . SER B 1 92 ? 29.825 -75.304 22.142 1.00 36.95 ? 142 SER B O 1 ATOM 2465 C CB . SER B 1 92 ? 31.110 -72.923 22.786 1.00 40.92 ? 142 SER B CB 1 ATOM 2466 O OG . SER B 1 92 ? 31.931 -71.768 22.881 1.00 51.67 ? 142 SER B OG 1 ATOM 2467 N N . GLY B 1 93 ? 29.242 -74.682 20.038 1.00 35.11 ? 143 GLY B N 1 ATOM 2468 C CA . GLY B 1 93 ? 28.486 -75.878 19.659 1.00 35.54 ? 143 GLY B CA 1 ATOM 2469 C C . GLY B 1 93 ? 27.141 -76.092 20.323 1.00 36.19 ? 143 GLY B C 1 ATOM 2470 O O . GLY B 1 93 ? 26.586 -77.190 20.252 1.00 37.72 ? 143 GLY B O 1 ATOM 2471 N N . ASN B 1 94 ? 26.613 -75.071 20.996 1.00 30.31 ? 144 ASN B N 1 ATOM 2472 C CA . ASN B 1 94 ? 25.337 -75.189 21.686 1.00 28.11 ? 144 ASN B CA 1 ATOM 2473 C C . ASN B 1 94 ? 24.357 -74.118 21.206 1.00 29.54 ? 144 ASN B C 1 ATOM 2474 O O . ASN B 1 94 ? 24.803 -73.002 20.859 1.00 28.61 ? 144 ASN B O 1 ATOM 2475 C CB . ASN B 1 94 ? 25.545 -75.080 23.188 1.00 28.64 ? 144 ASN B CB 1 ATOM 2476 C CG . ASN B 1 94 ? 26.432 -76.164 23.734 1.00 52.31 ? 144 ASN B CG 1 ATOM 2477 O OD1 . ASN B 1 94 ? 26.125 -77.352 23.628 1.00 40.16 ? 144 ASN B OD1 1 ATOM 2478 N ND2 . ASN B 1 94 ? 27.563 -75.774 24.305 1.00 46.52 ? 144 ASN B ND2 1 ATOM 2479 N N . PRO B 1 95 ? 23.028 -74.433 21.230 1.00 25.25 ? 145 PRO B N 1 ATOM 2480 C CA . PRO B 1 95 ? 22.030 -73.449 20.815 1.00 24.43 ? 145 PRO B CA 1 ATOM 2481 C C . PRO B 1 95 ? 22.086 -72.248 21.719 1.00 24.86 ? 145 PRO B C 1 ATOM 2482 O O . PRO B 1 95 ? 22.196 -72.392 22.941 1.00 26.67 ? 145 PRO B O 1 ATOM 2483 C CB . PRO B 1 95 ? 20.704 -74.194 20.993 1.00 27.00 ? 145 PRO B CB 1 ATOM 2484 C CG . PRO B 1 95 ? 21.064 -75.632 20.970 1.00 32.77 ? 145 PRO B CG 1 ATOM 2485 C CD . PRO B 1 95 ? 22.369 -75.677 21.683 1.00 28.57 ? 145 PRO B CD 1 ATOM 2486 N N . SER B 1 96 ? 21.989 -71.059 21.139 1.00 21.73 ? 146 SER B N 1 ATOM 2487 C CA . SER B 1 96 ? 22.013 -69.838 21.941 1.00 19.91 ? 146 SER B CA 1 ATOM 2488 C C . SER B 1 96 ? 21.034 -68.821 21.347 1.00 19.91 ? 146 SER B C 1 ATOM 2489 O O . SER B 1 96 ? 20.169 -69.196 20.555 1.00 16.75 ? 146 SER B O 1 ATOM 2490 C CB . SER B 1 96 ? 23.436 -69.297 22.055 1.00 24.21 ? 146 SER B CB 1 ATOM 2491 O OG . SER B 1 96 ? 23.559 -68.398 23.146 1.00 34.08 ? 146 SER B OG 1 ATOM 2492 N N . PHE B 1 97 ? 21.119 -67.570 21.752 1.00 18.55 ? 147 PHE B N 1 ATOM 2493 C CA . PHE B 1 97 ? 20.212 -66.558 21.241 1.00 16.34 ? 147 PHE B CA 1 ATOM 2494 C C . PHE B 1 97 ? 20.840 -65.211 21.304 1.00 17.33 ? 147 PHE B C 1 ATOM 2495 O O . PHE B 1 97 ? 21.879 -65.012 21.969 1.00 17.31 ? 147 PHE B O 1 ATOM 2496 C CB . PHE B 1 97 ? 18.874 -66.590 22.031 1.00 17.13 ? 147 PHE B CB 1 ATOM 2497 C CG . PHE B 1 97 ? 17.675 -65.990 21.335 1.00 17.22 ? 147 PHE B CG 1 ATOM 2498 C CD1 . PHE B 1 97 ? 17.256 -66.467 20.093 1.00 18.41 ? 147 PHE B CD1 1 ATOM 2499 C CD2 . PHE B 1 97 ? 16.962 -64.944 21.920 1.00 17.96 ? 147 PHE B CD2 1 ATOM 2500 C CE1 . PHE B 1 97 ? 16.124 -65.922 19.454 1.00 16.92 ? 147 PHE B CE1 1 ATOM 2501 C CE2 . PHE B 1 97 ? 15.800 -64.446 21.314 1.00 17.96 ? 147 PHE B CE2 1 ATOM 2502 C CZ . PHE B 1 97 ? 15.404 -64.916 20.076 1.00 15.07 ? 147 PHE B CZ 1 ATOM 2503 N N . PHE B 1 98 ? 20.206 -64.258 20.638 1.00 16.14 ? 148 PHE B N 1 ATOM 2504 C CA . PHE B 1 98 ? 20.580 -62.826 20.639 1.00 13.13 ? 148 PHE B CA 1 ATOM 2505 C C . PHE B 1 98 ? 20.808 -62.391 22.083 1.00 17.65 ? 148 PHE B C 1 ATOM 2506 O O . PHE B 1 98 ? 19.950 -62.654 22.929 1.00 19.54 ? 148 PHE B O 1 ATOM 2507 C CB . PHE B 1 98 ? 19.421 -62.021 20.037 1.00 14.20 ? 148 PHE B CB 1 ATOM 2508 C CG . PHE B 1 98 ? 19.145 -62.278 18.575 1.00 15.86 ? 148 PHE B CG 1 ATOM 2509 C CD1 . PHE B 1 98 ? 20.007 -61.794 17.588 1.00 17.32 ? 148 PHE B CD1 1 ATOM 2510 C CD2 . PHE B 1 98 ? 17.987 -62.935 18.178 1.00 17.09 ? 148 PHE B CD2 1 ATOM 2511 C CE1 . PHE B 1 98 ? 19.725 -61.986 16.224 1.00 16.97 ? 148 PHE B CE1 1 ATOM 2512 C CE2 . PHE B 1 98 ? 17.708 -63.133 16.811 1.00 19.92 ? 148 PHE B CE2 1 ATOM 2513 C CZ . PHE B 1 98 ? 18.578 -62.647 15.848 1.00 16.67 ? 148 PHE B CZ 1 ATOM 2514 N N . ARG B 1 99 ? 21.952 -61.766 22.387 1.00 14.33 ? 149 ARG B N 1 ATOM 2515 C CA . ARG B 1 99 ? 22.325 -61.433 23.771 1.00 15.27 ? 149 ARG B CA 1 ATOM 2516 C C . ARG B 1 99 ? 21.429 -60.436 24.441 1.00 19.13 ? 149 ARG B C 1 ATOM 2517 O O . ARG B 1 99 ? 21.341 -60.438 25.660 1.00 19.86 ? 149 ARG B O 1 ATOM 2518 C CB . ARG B 1 99 ? 23.769 -60.885 23.864 1.00 13.73 ? 149 ARG B CB 1 ATOM 2519 C CG . ARG B 1 99 ? 24.859 -61.751 23.254 1.00 30.88 ? 149 ARG B CG 1 ATOM 2520 C CD . ARG B 1 99 ? 24.829 -63.189 23.683 1.00 30.85 ? 149 ARG B CD 1 ATOM 2521 N NE . ARG B 1 99 ? 26.128 -63.815 23.423 1.00 24.90 ? 149 ARG B NE 1 ATOM 2522 C CZ . ARG B 1 99 ? 26.557 -64.916 24.028 1.00 41.04 ? 149 ARG B CZ 1 ATOM 2523 N NH1 . ARG B 1 99 ? 25.803 -65.517 24.940 1.00 26.18 ? 149 ARG B NH1 1 ATOM 2524 N NH2 . ARG B 1 99 ? 27.761 -65.404 23.753 1.00 26.55 ? 149 ARG B NH2 1 ATOM 2525 N N . ASN B 1 100 ? 20.798 -59.583 23.671 1.00 14.53 ? 150 ASN B N 1 ATOM 2526 C CA . ASN B 1 100 ? 20.018 -58.515 24.264 1.00 14.88 ? 150 ASN B CA 1 ATOM 2527 C C . ASN B 1 100 ? 18.532 -58.828 24.327 1.00 19.35 ? 150 ASN B C 1 ATOM 2528 O O . ASN B 1 100 ? 17.776 -58.006 24.874 1.00 16.70 ? 150 ASN B O 1 ATOM 2529 C CB . ASN B 1 100 ? 20.288 -57.243 23.514 1.00 13.38 ? 150 ASN B CB 1 ATOM 2530 C CG . ASN B 1 100 ? 21.742 -56.804 23.618 1.00 18.41 ? 150 ASN B CG 1 ATOM 2531 O OD1 . ASN B 1 100 ? 22.422 -57.149 24.572 1.00 19.08 ? 150 ASN B OD1 1 ATOM 2532 N ND2 . ASN B 1 100 ? 22.260 -56.130 22.594 1.00 16.70 ? 150 ASN B ND2 1 ATOM 2533 N N . MET B 1 101 ? 18.119 -60.011 23.780 1.00 15.71 ? 151 MET B N 1 ATOM 2534 C CA . MET B 1 101 ? 16.708 -60.384 23.601 1.00 13.77 ? 151 MET B CA 1 ATOM 2535 C C . MET B 1 101 ? 16.361 -61.603 24.432 1.00 16.78 ? 151 MET B C 1 ATOM 2536 O O . MET B 1 101 ? 17.253 -62.333 24.823 1.00 15.59 ? 151 MET B O 1 ATOM 2537 C CB . MET B 1 101 ? 16.412 -60.633 22.084 1.00 15.41 ? 151 MET B CB 1 ATOM 2538 C CG . MET B 1 101 ? 16.805 -59.434 21.121 1.00 17.39 ? 151 MET B CG 1 ATOM 2539 S SD . MET B 1 101 ? 16.228 -57.806 21.724 1.00 21.40 ? 151 MET B SD 1 ATOM 2540 C CE . MET B 1 101 ? 14.529 -57.914 21.091 1.00 17.59 ? 151 MET B CE 1 ATOM 2541 N N . VAL B 1 102 ? 15.058 -61.849 24.671 1.00 14.46 ? 152 VAL B N 1 ATOM 2542 C CA . VAL B 1 102 ? 14.570 -62.982 25.468 1.00 13.56 ? 152 VAL B CA 1 ATOM 2543 C C . VAL B 1 102 ? 13.510 -63.673 24.649 1.00 16.19 ? 152 VAL B C 1 ATOM 2544 O O . VAL B 1 102 ? 12.544 -63.038 24.262 1.00 15.45 ? 152 VAL B O 1 ATOM 2545 C CB . VAL B 1 102 ? 13.951 -62.518 26.825 1.00 17.71 ? 152 VAL B CB 1 ATOM 2546 C CG1 . VAL B 1 102 ? 13.494 -63.721 27.651 1.00 19.55 ? 152 VAL B CG1 1 ATOM 2547 C CG2 . VAL B 1 102 ? 14.929 -61.647 27.631 1.00 17.67 ? 152 VAL B CG2 1 ATOM 2548 N N . TRP B 1 103 ? 13.679 -64.959 24.423 1.00 13.30 ? 153 TRP B N 1 ATOM 2549 C CA . TRP B 1 103 ? 12.693 -65.712 23.666 1.00 14.85 ? 153 TRP B CA 1 ATOM 2550 C C . TRP B 1 103 ? 11.744 -66.327 24.709 1.00 17.21 ? 153 TRP B C 1 ATOM 2551 O O . TRP B 1 103 ? 12.125 -67.279 25.396 1.00 17.82 ? 153 TRP B O 1 ATOM 2552 C CB . TRP B 1 103 ? 13.435 -66.830 22.921 1.00 15.69 ? 153 TRP B CB 1 ATOM 2553 C CG . TRP B 1 103 ? 12.587 -67.546 21.920 1.00 16.65 ? 153 TRP B CG 1 ATOM 2554 C CD1 . TRP B 1 103 ? 11.231 -67.436 21.740 1.00 18.78 ? 153 TRP B CD1 1 ATOM 2555 C CD2 . TRP B 1 103 ? 13.060 -68.411 20.899 1.00 17.13 ? 153 TRP B CD2 1 ATOM 2556 N NE1 . TRP B 1 103 ? 10.833 -68.188 20.659 1.00 17.19 ? 153 TRP B NE1 1 ATOM 2557 C CE2 . TRP B 1 103 ? 11.935 -68.818 20.136 1.00 21.15 ? 153 TRP B CE2 1 ATOM 2558 C CE3 . TRP B 1 103 ? 14.341 -68.817 20.491 1.00 19.96 ? 153 TRP B CE3 1 ATOM 2559 C CZ2 . TRP B 1 103 ? 12.055 -69.648 19.009 1.00 22.27 ? 153 TRP B CZ2 1 ATOM 2560 C CZ3 . TRP B 1 103 ? 14.456 -69.667 19.396 1.00 22.52 ? 153 TRP B CZ3 1 ATOM 2561 C CH2 . TRP B 1 103 ? 13.321 -70.090 18.683 1.00 23.24 ? 153 TRP B CH2 1 ATOM 2562 N N . LEU B 1 104 ? 10.516 -65.768 24.839 1.00 14.60 ? 154 LEU B N 1 ATOM 2563 C CA . LEU B 1 104 ? 9.575 -66.317 25.808 1.00 14.36 ? 154 LEU B CA 1 ATOM 2564 C C . LEU B 1 104 ? 8.852 -67.510 25.179 1.00 16.67 ? 154 LEU B C 1 ATOM 2565 O O . LEU B 1 104 ? 8.284 -67.390 24.080 1.00 14.66 ? 154 LEU B O 1 ATOM 2566 C CB . LEU B 1 104 ? 8.508 -65.278 26.208 1.00 15.82 ? 154 LEU B CB 1 ATOM 2567 C CG . LEU B 1 104 ? 8.967 -64.056 27.047 1.00 23.91 ? 154 LEU B CG 1 ATOM 2568 C CD1 . LEU B 1 104 ? 9.739 -63.085 26.222 1.00 27.83 ? 154 LEU B CD1 1 ATOM 2569 C CD2 . LEU B 1 104 ? 7.760 -63.290 27.539 1.00 29.17 ? 154 LEU B CD2 1 ATOM 2570 N N . THR B 1 105 ? 8.873 -68.649 25.868 1.00 14.68 ? 155 THR B N 1 ATOM 2571 C CA . THR B 1 105 ? 8.174 -69.816 25.385 1.00 15.34 ? 155 THR B CA 1 ATOM 2572 C C . THR B 1 105 ? 7.365 -70.417 26.511 1.00 18.41 ? 155 THR B C 1 ATOM 2573 O O . THR B 1 105 ? 7.455 -69.986 27.661 1.00 17.13 ? 155 THR B O 1 ATOM 2574 C CB . THR B 1 105 ? 9.131 -70.868 24.741 1.00 17.88 ? 155 THR B CB 1 ATOM 2575 O OG1 . THR B 1 105 ? 10.085 -71.356 25.693 1.00 19.30 ? 155 THR B OG1 1 ATOM 2576 C CG2 . THR B 1 105 ? 9.841 -70.333 23.474 1.00 17.68 ? 155 THR B CG2 1 ATOM 2577 N N . GLU B 1 106 ? 6.570 -71.414 26.169 1.00 15.62 ? 156 GLU B N 1 ATOM 2578 C CA . GLU B 1 106 ? 5.724 -72.059 27.162 1.00 15.80 ? 156 GLU B CA 1 ATOM 2579 C C . GLU B 1 106 ? 6.482 -72.676 28.321 1.00 21.08 ? 156 GLU B C 1 ATOM 2580 O O . GLU B 1 106 ? 7.639 -73.070 28.186 1.00 20.75 ? 156 GLU B O 1 ATOM 2581 C CB . GLU B 1 106 ? 4.781 -73.094 26.512 1.00 17.65 ? 156 GLU B CB 1 ATOM 2582 C CG . GLU B 1 106 ? 5.518 -74.253 25.844 1.00 21.82 ? 156 GLU B CG 1 ATOM 2583 C CD . GLU B 1 106 ? 5.909 -75.442 26.718 1.00 51.96 ? 156 GLU B CD 1 ATOM 2584 O OE1 . GLU B 1 106 ? 6.695 -76.296 26.247 1.00 55.96 ? 156 GLU B OE1 1 ATOM 2585 O OE2 . GLU B 1 106 ? 5.465 -75.502 27.886 1.00 44.49 ? 156 GLU B OE2 1 ATOM 2586 N N . LYS B 1 107 ? 5.813 -72.766 29.459 1.00 19.93 ? 157 LYS B N 1 ATOM 2587 C CA . LYS B 1 107 ? 6.363 -73.367 30.660 1.00 21.20 ? 157 LYS B CA 1 ATOM 2588 C C . LYS B 1 107 ? 5.263 -74.307 31.175 1.00 27.64 ? 157 LYS B C 1 ATOM 2589 O O . LYS B 1 107 ? 4.109 -73.890 31.303 1.00 25.53 ? 157 LYS B O 1 ATOM 2590 C CB . LYS B 1 107 ? 6.709 -72.289 31.695 1.00 23.60 ? 157 LYS B CB 1 ATOM 2591 C CG . LYS B 1 107 ? 7.374 -72.846 32.951 1.00 26.65 ? 157 LYS B CG 1 ATOM 2592 C CD . LYS B 1 107 ? 7.677 -71.728 33.938 1.00 25.75 ? 157 LYS B CD 1 ATOM 2593 C CE . LYS B 1 107 ? 8.187 -72.315 35.222 1.00 34.72 ? 157 LYS B CE 1 ATOM 2594 N NZ . LYS B 1 107 ? 8.269 -71.300 36.290 1.00 33.75 ? 157 LYS B NZ 1 ATOM 2595 N N . GLY B 1 108 ? 5.620 -75.565 31.382 1.00 29.23 ? 158 GLY B N 1 ATOM 2596 C CA . GLY B 1 108 ? 4.702 -76.591 31.869 1.00 30.86 ? 158 GLY B CA 1 ATOM 2597 C C . GLY B 1 108 ? 3.440 -76.718 31.043 1.00 36.36 ? 158 GLY B C 1 ATOM 2598 O O . GLY B 1 108 ? 2.342 -76.840 31.598 1.00 36.97 ? 158 GLY B O 1 ATOM 2599 N N . SER B 1 109 ? 3.596 -76.660 29.704 1.00 32.80 ? 159 SER B N 1 ATOM 2600 C CA . SER B 1 109 ? 2.524 -76.761 28.707 1.00 32.65 ? 159 SER B CA 1 ATOM 2601 C C . SER B 1 109 ? 1.514 -75.607 28.813 1.00 34.76 ? 159 SER B C 1 ATOM 2602 O O . SER B 1 109 ? 0.323 -75.797 28.581 1.00 36.91 ? 159 SER B O 1 ATOM 2603 C CB . SER B 1 109 ? 1.865 -78.145 28.750 1.00 39.36 ? 159 SER B CB 1 ATOM 2604 O OG . SER B 1 109 ? 0.896 -78.293 27.724 1.00 57.26 ? 159 SER B OG 1 ATOM 2605 N N . ASN B 1 110 ? 1.990 -74.401 29.186 1.00 27.01 ? 160 ASN B N 1 ATOM 2606 C CA . ASN B 1 110 ? 1.128 -73.231 29.275 1.00 25.04 ? 160 ASN B CA 1 ATOM 2607 C C . ASN B 1 110 ? 1.889 -71.999 28.869 1.00 24.13 ? 160 ASN B C 1 ATOM 2608 O O . ASN B 1 110 ? 3.080 -71.899 29.149 1.00 23.03 ? 160 ASN B O 1 ATOM 2609 C CB . ASN B 1 110 ? 0.577 -73.047 30.693 1.00 29.24 ? 160 ASN B CB 1 ATOM 2610 C CG . ASN B 1 110 ? -0.532 -74.018 31.031 1.00 62.66 ? 160 ASN B CG 1 ATOM 2611 O OD1 . ASN B 1 110 ? -0.324 -75.013 31.732 1.00 67.19 ? 160 ASN B OD1 1 ATOM 2612 N ND2 . ASN B 1 110 ? -1.724 -73.783 30.502 1.00 53.13 ? 160 ASN B ND2 1 ATOM 2613 N N . TYR B 1 111 ? 1.203 -71.061 28.236 1.00 20.81 ? 161 TYR B N 1 ATOM 2614 C CA . TYR B 1 111 ? 1.770 -69.756 27.900 1.00 18.06 ? 161 TYR B CA 1 ATOM 2615 C C . TYR B 1 111 ? 0.746 -68.734 28.416 1.00 22.13 ? 161 TYR B C 1 ATOM 2616 O O . TYR B 1 111 ? -0.202 -68.415 27.695 1.00 21.67 ? 161 TYR B O 1 ATOM 2617 C CB . TYR B 1 111 ? 2.038 -69.556 26.392 1.00 17.42 ? 161 TYR B CB 1 ATOM 2618 C CG . TYR B 1 111 ? 2.838 -68.299 26.065 1.00 16.24 ? 161 TYR B CG 1 ATOM 2619 C CD1 . TYR B 1 111 ? 4.154 -68.379 25.618 1.00 15.00 ? 161 TYR B CD1 1 ATOM 2620 C CD2 . TYR B 1 111 ? 2.272 -67.028 26.188 1.00 16.57 ? 161 TYR B CD2 1 ATOM 2621 C CE1 . TYR B 1 111 ? 4.884 -67.230 25.305 1.00 14.67 ? 161 TYR B CE1 1 ATOM 2622 C CE2 . TYR B 1 111 ? 2.997 -65.870 25.881 1.00 17.01 ? 161 TYR B CE2 1 ATOM 2623 C CZ . TYR B 1 111 ? 4.307 -65.975 25.455 1.00 18.55 ? 161 TYR B CZ 1 ATOM 2624 O OH . TYR B 1 111 ? 4.966 -64.816 25.099 1.00 20.16 ? 161 TYR B OH 1 ATOM 2625 N N . PRO B 1 112 ? 0.836 -68.250 29.678 1.00 20.14 ? 162 PRO B N 1 ATOM 2626 C CA . PRO B 1 112 ? -0.153 -67.258 30.120 1.00 20.13 ? 162 PRO B CA 1 ATOM 2627 C C . PRO B 1 112 ? 0.174 -65.907 29.487 1.00 21.29 ? 162 PRO B C 1 ATOM 2628 O O . PRO B 1 112 ? 1.231 -65.760 28.858 1.00 19.32 ? 162 PRO B O 1 ATOM 2629 C CB . PRO B 1 112 ? -0.018 -67.237 31.653 1.00 23.28 ? 162 PRO B CB 1 ATOM 2630 C CG . PRO B 1 112 ? 1.251 -67.885 31.956 1.00 26.52 ? 162 PRO B CG 1 ATOM 2631 C CD . PRO B 1 112 ? 1.831 -68.537 30.728 1.00 23.72 ? 162 PRO B CD 1 ATOM 2632 N N . VAL B 1 113 ? -0.738 -64.934 29.605 1.00 21.96 ? 163 VAL B N 1 ATOM 2633 C CA . VAL B 1 113 ? -0.452 -63.630 29.016 1.00 21.65 ? 163 VAL B CA 1 ATOM 2634 C C . VAL B 1 113 ? 0.825 -63.082 29.643 1.00 23.02 ? 163 VAL B C 1 ATOM 2635 O O . VAL B 1 113 ? 0.996 -63.115 30.875 1.00 25.71 ? 163 VAL B O 1 ATOM 2636 C CB . VAL B 1 113 ? -1.635 -62.630 29.161 1.00 27.13 ? 163 VAL B CB 1 ATOM 2637 C CG1 . VAL B 1 113 ? -1.353 -61.355 28.368 1.00 26.68 ? 163 VAL B CG1 1 ATOM 2638 C CG2 . VAL B 1 113 ? -2.952 -63.264 28.714 1.00 28.24 ? 163 VAL B CG2 1 ATOM 2639 N N . ALA B 1 114 ? 1.723 -62.624 28.793 1.00 18.52 ? 164 ALA B N 1 ATOM 2640 C CA . ALA B 1 114 ? 3.011 -62.019 29.173 1.00 17.39 ? 164 ALA B CA 1 ATOM 2641 C C . ALA B 1 114 ? 2.806 -60.519 29.149 1.00 21.53 ? 164 ALA B C 1 ATOM 2642 O O . ALA B 1 114 ? 2.405 -59.977 28.121 1.00 21.23 ? 164 ALA B O 1 ATOM 2643 C CB . ALA B 1 114 ? 4.088 -62.403 28.160 1.00 18.89 ? 164 ALA B CB 1 ATOM 2644 N N . LYS B 1 115 ? 3.056 -59.861 30.275 1.00 17.21 ? 165 LYS B N 1 ATOM 2645 C CA . LYS B 1 115 ? 2.924 -58.415 30.409 1.00 16.93 ? 165 LYS B CA 1 ATOM 2646 C C . LYS B 1 115 ? 4.162 -57.833 31.050 1.00 20.43 ? 165 LYS B C 1 ATOM 2647 O O . LYS B 1 115 ? 4.703 -58.387 31.991 1.00 21.17 ? 165 LYS B O 1 ATOM 2648 C CB . LYS B 1 115 ? 1.677 -58.051 31.227 1.00 20.59 ? 165 LYS B CB 1 ATOM 2649 C CG . LYS B 1 115 ? 0.378 -58.202 30.436 1.00 29.25 ? 165 LYS B CG 1 ATOM 2650 C CD . LYS B 1 115 ? -0.843 -57.935 31.307 1.00 42.06 ? 165 LYS B CD 1 ATOM 2651 C CE . LYS B 1 115 ? -2.121 -58.338 30.619 1.00 56.95 ? 165 LYS B CE 1 ATOM 2652 N NZ . LYS B 1 115 ? -3.302 -58.218 31.518 1.00 68.09 ? 165 LYS B NZ 1 ATOM 2653 N N . GLY B 1 116 ? 4.601 -56.706 30.536 1.00 16.96 ? 166 GLY B N 1 ATOM 2654 C CA . GLY B 1 116 ? 5.761 -56.023 31.085 1.00 17.72 ? 166 GLY B CA 1 ATOM 2655 C C . GLY B 1 116 ? 5.708 -54.580 30.686 1.00 20.91 ? 166 GLY B C 1 ATOM 2656 O O . GLY B 1 116 ? 5.237 -54.259 29.599 1.00 19.82 ? 166 GLY B O 1 ATOM 2657 N N . SER B 1 117 ? 6.183 -53.723 31.540 1.00 17.85 ? 167 SER B N 1 ATOM 2658 C CA . SER B 1 117 ? 6.210 -52.307 31.226 1.00 17.90 ? 167 SER B CA 1 ATOM 2659 C C . SER B 1 117 ? 7.468 -51.656 31.774 1.00 20.12 ? 167 SER B C 1 ATOM 2660 O O . SER B 1 117 ? 8.072 -52.165 32.709 1.00 18.64 ? 167 SER B O 1 ATOM 2661 C CB . SER B 1 117 ? 4.938 -51.613 31.714 1.00 24.08 ? 167 SER B CB 1 ATOM 2662 O OG . SER B 1 117 ? 4.983 -51.170 33.059 1.00 31.71 ? 167 SER B OG 1 ATOM 2663 N N . TYR B 1 118 ? 7.877 -50.550 31.172 1.00 17.46 ? 168 TYR B N 1 ATOM 2664 C CA . TYR B 1 118 ? 9.073 -49.823 31.626 1.00 17.39 ? 168 TYR B CA 1 ATOM 2665 C C . TYR B 1 118 ? 8.843 -48.319 31.456 1.00 18.55 ? 168 TYR B C 1 ATOM 2666 O O . TYR B 1 118 ? 8.518 -47.876 30.357 1.00 16.20 ? 168 TYR B O 1 ATOM 2667 C CB . TYR B 1 118 ? 10.341 -50.266 30.842 1.00 17.16 ? 168 TYR B CB 1 ATOM 2668 C CG . TYR B 1 118 ? 11.532 -49.373 31.125 1.00 18.10 ? 168 TYR B CG 1 ATOM 2669 C CD1 . TYR B 1 118 ? 12.193 -49.426 32.348 1.00 19.96 ? 168 TYR B CD1 1 ATOM 2670 C CD2 . TYR B 1 118 ? 11.910 -48.380 30.227 1.00 17.71 ? 168 TYR B CD2 1 ATOM 2671 C CE1 . TYR B 1 118 ? 13.239 -48.547 32.647 1.00 20.63 ? 168 TYR B CE1 1 ATOM 2672 C CE2 . TYR B 1 118 ? 12.972 -47.522 30.499 1.00 18.18 ? 168 TYR B CE2 1 ATOM 2673 C CZ . TYR B 1 118 ? 13.645 -47.618 31.701 1.00 21.34 ? 168 TYR B CZ 1 ATOM 2674 O OH . TYR B 1 118 ? 14.642 -46.704 31.953 1.00 22.48 ? 168 TYR B OH 1 ATOM 2675 N N . ASN B 1 119 ? 9.000 -47.555 32.543 1.00 16.53 ? 169 ASN B N 1 ATOM 2676 C CA . ASN B 1 119 ? 8.866 -46.094 32.496 1.00 16.84 ? 169 ASN B CA 1 ATOM 2677 C C . ASN B 1 119 ? 10.284 -45.562 32.280 1.00 20.72 ? 169 ASN B C 1 ATOM 2678 O O . ASN B 1 119 ? 11.190 -45.900 33.050 1.00 20.48 ? 169 ASN B O 1 ATOM 2679 C CB . ASN B 1 119 ? 8.306 -45.580 33.822 1.00 17.41 ? 169 ASN B CB 1 ATOM 2680 C CG . ASN B 1 119 ? 8.057 -44.092 33.842 1.00 34.12 ? 169 ASN B CG 1 ATOM 2681 O OD1 . ASN B 1 119 ? 8.510 -43.346 32.959 1.00 25.06 ? 169 ASN B OD1 1 ATOM 2682 N ND2 . ASN B 1 119 ? 7.338 -43.626 34.875 1.00 30.30 ? 169 ASN B ND2 1 ATOM 2683 N N . ASN B 1 120 ? 10.488 -44.744 31.225 1.00 16.47 ? 170 ASN B N 1 ATOM 2684 C CA . ASN B 1 120 ? 11.807 -44.241 30.932 1.00 17.62 ? 170 ASN B CA 1 ATOM 2685 C C . ASN B 1 120 ? 12.258 -43.148 31.896 1.00 22.67 ? 170 ASN B C 1 ATOM 2686 O O . ASN B 1 120 ? 12.136 -41.953 31.604 1.00 21.95 ? 170 ASN B O 1 ATOM 2687 C CB . ASN B 1 120 ? 11.880 -43.761 29.497 1.00 16.72 ? 170 ASN B CB 1 ATOM 2688 C CG . ASN B 1 120 ? 13.266 -43.331 29.088 1.00 22.72 ? 170 ASN B CG 1 ATOM 2689 O OD1 . ASN B 1 120 ? 14.234 -43.468 29.847 1.00 20.07 ? 170 ASN B OD1 1 ATOM 2690 N ND2 . ASN B 1 120 ? 13.371 -42.719 27.905 1.00 18.54 ? 170 ASN B ND2 1 ATOM 2691 N N . THR B 1 121 ? 12.860 -43.573 33.018 1.00 19.96 ? 171 THR B N 1 ATOM 2692 C CA . THR B 1 121 ? 13.423 -42.636 33.996 1.00 21.15 ? 171 THR B CA 1 ATOM 2693 C C . THR B 1 121 ? 14.968 -42.540 33.821 1.00 26.59 ? 171 THR B C 1 ATOM 2694 O O . THR B 1 121 ? 15.625 -41.983 34.703 1.00 27.57 ? 171 THR B O 1 ATOM 2695 C CB . THR B 1 121 ? 13.066 -43.101 35.413 1.00 25.83 ? 171 THR B CB 1 ATOM 2696 O OG1 . THR B 1 121 ? 13.545 -44.443 35.575 1.00 27.73 ? 171 THR B OG1 1 ATOM 2697 C CG2 . THR B 1 121 ? 11.575 -43.018 35.693 1.00 23.95 ? 171 THR B CG2 1 ATOM 2698 N N . SER B 1 122 ? 15.529 -43.069 32.694 1.00 22.78 ? 172 SER B N 1 ATOM 2699 C CA . SER B 1 122 ? 16.979 -43.095 32.403 1.00 23.14 ? 172 SER B CA 1 ATOM 2700 C C . SER B 1 122 ? 17.647 -41.721 32.272 1.00 29.42 ? 172 SER B C 1 ATOM 2701 O O . SER B 1 122 ? 18.863 -41.635 32.446 1.00 32.26 ? 172 SER B O 1 ATOM 2702 C CB . SER B 1 122 ? 17.288 -43.956 31.168 1.00 25.09 ? 172 SER B CB 1 ATOM 2703 O OG . SER B 1 122 ? 16.999 -43.243 29.971 1.00 23.12 ? 172 SER B OG 1 ATOM 2704 N N . GLY B 1 123 ? 16.880 -40.671 31.965 1.00 23.85 ? 173 GLY B N 1 ATOM 2705 C CA . GLY B 1 123 ? 17.444 -39.335 31.781 1.00 24.19 ? 173 GLY B CA 1 ATOM 2706 C C . GLY B 1 123 ? 17.586 -38.922 30.321 1.00 27.41 ? 173 GLY B C 1 ATOM 2707 O O . GLY B 1 123 ? 17.946 -37.785 30.037 1.00 29.34 ? 173 GLY B O 1 ATOM 2708 N N . GLU B 1 124 ? 17.320 -39.833 29.383 1.00 22.28 ? 174 GLU B N 1 ATOM 2709 C CA . GLU B 1 124 ? 17.335 -39.518 27.945 1.00 22.23 ? 174 GLU B CA 1 ATOM 2710 C C . GLU B 1 124 ? 16.386 -40.428 27.166 1.00 22.36 ? 174 GLU B C 1 ATOM 2711 O O . GLU B 1 124 ? 15.892 -41.407 27.714 1.00 21.02 ? 174 GLU B O 1 ATOM 2712 C CB . GLU B 1 124 ? 18.745 -39.583 27.337 1.00 24.48 ? 174 GLU B CB 1 ATOM 2713 C CG . GLU B 1 124 ? 19.283 -38.204 26.955 1.00 38.89 ? 174 GLU B CG 1 ATOM 2714 C CD . GLU B 1 124 ? 18.918 -37.701 25.567 1.00 59.82 ? 174 GLU B CD 1 ATOM 2715 O OE1 . GLU B 1 124 ? 17.730 -37.790 25.170 1.00 36.25 ? 174 GLU B OE1 1 ATOM 2716 O OE2 . GLU B 1 124 ? 19.833 -37.195 24.877 1.00 54.96 ? 174 GLU B OE2 1 ATOM 2717 N N . GLN B 1 125 ? 16.132 -40.084 25.892 1.00 19.47 ? 175 GLN B N 1 ATOM 2718 C CA . GLN B 1 125 ? 15.339 -40.916 24.992 1.00 19.83 ? 175 GLN B CA 1 ATOM 2719 C C . GLN B 1 125 ? 16.042 -42.279 24.892 1.00 19.67 ? 175 GLN B C 1 ATOM 2720 O O . GLN B 1 125 ? 17.273 -42.367 24.973 1.00 18.93 ? 175 GLN B O 1 ATOM 2721 C CB . GLN B 1 125 ? 15.317 -40.286 23.599 1.00 22.66 ? 175 GLN B CB 1 ATOM 2722 C CG . GLN B 1 125 ? 14.190 -39.317 23.337 1.00 42.17 ? 175 GLN B CG 1 ATOM 2723 C CD . GLN B 1 125 ? 14.118 -39.081 21.851 1.00 54.24 ? 175 GLN B CD 1 ATOM 2724 O OE1 . GLN B 1 125 ? 15.119 -38.745 21.205 1.00 47.23 ? 175 GLN B OE1 1 ATOM 2725 N NE2 . GLN B 1 125 ? 12.970 -39.370 21.257 1.00 36.34 ? 175 GLN B NE2 1 ATOM 2726 N N . MET B 1 126 ? 15.251 -43.350 24.731 1.00 15.64 ? 176 MET B N 1 ATOM 2727 C CA . MET B 1 126 ? 15.810 -44.671 24.672 1.00 15.01 ? 176 MET B CA 1 ATOM 2728 C C . MET B 1 126 ? 15.319 -45.418 23.452 1.00 17.76 ? 176 MET B C 1 ATOM 2729 O O . MET B 1 126 ? 14.116 -45.437 23.196 1.00 18.54 ? 176 MET B O 1 ATOM 2730 C CB . MET B 1 126 ? 15.402 -45.411 25.950 1.00 16.50 ? 176 MET B CB 1 ATOM 2731 C CG . MET B 1 126 ? 15.932 -46.796 26.061 1.00 19.32 ? 176 MET B CG 1 ATOM 2732 S SD . MET B 1 126 ? 15.259 -47.561 27.531 1.00 22.64 ? 176 MET B SD 1 ATOM 2733 C CE . MET B 1 126 ? 16.142 -46.621 28.820 1.00 19.91 ? 176 MET B CE 1 ATOM 2734 N N . LEU B 1 127 ? 16.237 -46.056 22.742 1.00 15.45 ? 177 LEU B N 1 ATOM 2735 C CA . LEU B 1 127 ? 15.910 -46.944 21.619 1.00 14.92 ? 177 LEU B CA 1 ATOM 2736 C C . LEU B 1 127 ? 15.553 -48.348 22.204 1.00 17.71 ? 177 LEU B C 1 ATOM 2737 O O . LEU B 1 127 ? 16.319 -48.907 23.020 1.00 16.70 ? 177 LEU B O 1 ATOM 2738 C CB . LEU B 1 127 ? 17.121 -47.035 20.663 1.00 14.16 ? 177 LEU B CB 1 ATOM 2739 C CG . LEU B 1 127 ? 17.107 -48.158 19.611 1.00 17.83 ? 177 LEU B CG 1 ATOM 2740 C CD1 . LEU B 1 127 ? 15.960 -47.984 18.654 1.00 19.56 ? 177 LEU B CD1 1 ATOM 2741 C CD2 . LEU B 1 127 ? 18.454 -48.222 18.870 1.00 22.44 ? 177 LEU B CD2 1 ATOM 2742 N N . ILE B 1 128 ? 14.391 -48.916 21.772 1.00 12.94 ? 178 ILE B N 1 ATOM 2743 C CA . ILE B 1 128 ? 13.943 -50.226 22.231 1.00 12.76 ? 178 ILE B CA 1 ATOM 2744 C C . ILE B 1 128 ? 13.516 -51.035 21.020 1.00 14.64 ? 178 ILE B C 1 ATOM 2745 O O . ILE B 1 128 ? 12.769 -50.547 20.174 1.00 15.16 ? 178 ILE B O 1 ATOM 2746 C CB . ILE B 1 128 ? 12.795 -50.155 23.270 1.00 15.68 ? 178 ILE B CB 1 ATOM 2747 C CG1 . ILE B 1 128 ? 13.218 -49.345 24.540 1.00 15.76 ? 178 ILE B CG1 1 ATOM 2748 C CG2 . ILE B 1 128 ? 12.365 -51.557 23.715 1.00 17.93 ? 178 ILE B CG2 1 ATOM 2749 C CD1 . ILE B 1 128 ? 12.039 -48.980 25.423 1.00 20.11 ? 178 ILE B CD1 1 ATOM 2750 N N . ILE B 1 129 ? 13.977 -52.270 20.969 1.00 13.70 ? 179 ILE B N 1 ATOM 2751 C CA . ILE B 1 129 ? 13.689 -53.186 19.868 1.00 14.00 ? 179 ILE B CA 1 ATOM 2752 C C . ILE B 1 129 ? 12.915 -54.401 20.414 1.00 15.64 ? 179 ILE B C 1 ATOM 2753 O O . ILE B 1 129 ? 13.189 -54.854 21.502 1.00 15.00 ? 179 ILE B O 1 ATOM 2754 C CB . ILE B 1 129 ? 15.029 -53.617 19.191 1.00 17.26 ? 179 ILE B CB 1 ATOM 2755 C CG1 . ILE B 1 129 ? 15.747 -52.383 18.578 1.00 17.78 ? 179 ILE B CG1 1 ATOM 2756 C CG2 . ILE B 1 129 ? 14.788 -54.708 18.099 1.00 16.73 ? 179 ILE B CG2 1 ATOM 2757 C CD1 . ILE B 1 129 ? 17.268 -52.600 18.330 1.00 24.00 ? 179 ILE B CD1 1 ATOM 2758 N N . TRP B 1 130 ? 11.945 -54.938 19.660 1.00 13.38 ? 180 TRP B N 1 ATOM 2759 C CA . TRP B 1 130 ? 11.251 -56.180 20.058 1.00 14.49 ? 180 TRP B CA 1 ATOM 2760 C C . TRP B 1 130 ? 11.008 -56.970 18.795 1.00 16.44 ? 180 TRP B C 1 ATOM 2761 O O . TRP B 1 130 ? 11.087 -56.420 17.693 1.00 14.22 ? 180 TRP B O 1 ATOM 2762 C CB . TRP B 1 130 ? 9.903 -55.919 20.764 1.00 14.17 ? 180 TRP B CB 1 ATOM 2763 C CG . TRP B 1 130 ? 8.865 -55.306 19.857 1.00 16.09 ? 180 TRP B CG 1 ATOM 2764 C CD1 . TRP B 1 130 ? 7.865 -55.945 19.195 1.00 19.48 ? 180 TRP B CD1 1 ATOM 2765 C CD2 . TRP B 1 130 ? 8.752 -53.920 19.515 1.00 17.13 ? 180 TRP B CD2 1 ATOM 2766 N NE1 . TRP B 1 130 ? 7.135 -55.041 18.447 1.00 20.05 ? 180 TRP B NE1 1 ATOM 2767 C CE2 . TRP B 1 130 ? 7.640 -53.788 18.653 1.00 22.92 ? 180 TRP B CE2 1 ATOM 2768 C CE3 . TRP B 1 130 ? 9.476 -52.773 19.864 1.00 20.26 ? 180 TRP B CE3 1 ATOM 2769 C CZ2 . TRP B 1 130 ? 7.225 -52.550 18.155 1.00 23.35 ? 180 TRP B CZ2 1 ATOM 2770 C CZ3 . TRP B 1 130 ? 9.074 -51.551 19.343 1.00 23.32 ? 180 TRP B CZ3 1 ATOM 2771 C CH2 . TRP B 1 130 ? 7.966 -51.453 18.502 1.00 24.02 ? 180 TRP B CH2 1 ATOM 2772 N N . GLY B 1 131 ? 10.757 -58.256 18.954 1.00 14.00 ? 181 GLY B N 1 ATOM 2773 C CA . GLY B 1 131 ? 10.435 -59.051 17.788 1.00 13.01 ? 181 GLY B CA 1 ATOM 2774 C C . GLY B 1 131 ? 9.142 -59.834 17.905 1.00 15.17 ? 181 GLY B C 1 ATOM 2775 O O . GLY B 1 131 ? 8.582 -59.998 18.982 1.00 12.07 ? 181 GLY B O 1 ATOM 2776 N N . VAL B 1 132 ? 8.672 -60.300 16.751 1.00 12.72 ? 182 VAL B N 1 ATOM 2777 C CA . VAL B 1 132 ? 7.533 -61.202 16.608 1.00 11.66 ? 182 VAL B CA 1 ATOM 2778 C C . VAL B 1 132 ? 8.099 -62.418 15.850 1.00 14.89 ? 182 VAL B C 1 ATOM 2779 O O . VAL B 1 132 ? 8.683 -62.297 14.752 1.00 16.05 ? 182 VAL B O 1 ATOM 2780 C CB . VAL B 1 132 ? 6.343 -60.541 15.862 1.00 15.68 ? 182 VAL B CB 1 ATOM 2781 C CG1 . VAL B 1 132 ? 5.215 -61.561 15.625 1.00 17.54 ? 182 VAL B CG1 1 ATOM 2782 C CG2 . VAL B 1 132 ? 5.798 -59.331 16.679 1.00 16.12 ? 182 VAL B CG2 1 ATOM 2783 N N . HIS B 1 133 ? 7.876 -63.622 16.428 1.00 10.51 ? 183 HIS B N 1 ATOM 2784 C CA . HIS B 1 133 ? 8.287 -64.844 15.762 1.00 11.09 ? 183 HIS B CA 1 ATOM 2785 C C . HIS B 1 133 ? 7.142 -65.359 14.878 1.00 14.80 ? 183 HIS B C 1 ATOM 2786 O O . HIS B 1 133 ? 5.980 -65.491 15.334 1.00 13.15 ? 183 HIS B O 1 ATOM 2787 C CB . HIS B 1 133 ? 8.596 -65.908 16.803 1.00 12.28 ? 183 HIS B CB 1 ATOM 2788 C CG . HIS B 1 133 ? 9.157 -67.159 16.222 1.00 15.62 ? 183 HIS B CG 1 ATOM 2789 N ND1 . HIS B 1 133 ? 8.870 -68.369 16.768 1.00 18.00 ? 183 HIS B ND1 1 ATOM 2790 C CD2 . HIS B 1 133 ? 9.984 -67.338 15.161 1.00 17.57 ? 183 HIS B CD2 1 ATOM 2791 C CE1 . HIS B 1 133 ? 9.541 -69.260 16.053 1.00 18.90 ? 183 HIS B CE1 1 ATOM 2792 N NE2 . HIS B 1 133 ? 10.225 -68.673 15.072 1.00 19.22 ? 183 HIS B NE2 1 ATOM 2793 N N . HIS B 1 134 ? 7.487 -65.606 13.601 1.00 11.98 ? 184 HIS B N 1 ATOM 2794 C CA . HIS B 1 134 ? 6.540 -66.106 12.590 1.00 11.70 ? 184 HIS B CA 1 ATOM 2795 C C . HIS B 1 134 ? 6.904 -67.569 12.331 1.00 14.63 ? 184 HIS B C 1 ATOM 2796 O O . HIS B 1 134 ? 7.825 -67.855 11.561 1.00 14.09 ? 184 HIS B O 1 ATOM 2797 C CB . HIS B 1 134 ? 6.639 -65.259 11.308 1.00 12.29 ? 184 HIS B CB 1 ATOM 2798 C CG . HIS B 1 134 ? 6.244 -63.824 11.516 1.00 15.98 ? 184 HIS B CG 1 ATOM 2799 N ND1 . HIS B 1 134 ? 4.943 -63.474 11.711 1.00 16.46 ? 184 HIS B ND1 1 ATOM 2800 C CD2 . HIS B 1 134 ? 7.010 -62.706 11.585 1.00 17.81 ? 184 HIS B CD2 1 ATOM 2801 C CE1 . HIS B 1 134 ? 4.923 -62.145 11.879 1.00 16.47 ? 184 HIS B CE1 1 ATOM 2802 N NE2 . HIS B 1 134 ? 6.146 -61.639 11.780 1.00 17.23 ? 184 HIS B NE2 1 ATOM 2803 N N . PRO B 1 135 ? 6.299 -68.548 13.019 1.00 13.33 ? 185 PRO B N 1 ATOM 2804 C CA . PRO B 1 135 ? 6.741 -69.935 12.841 1.00 13.59 ? 185 PRO B CA 1 ATOM 2805 C C . PRO B 1 135 ? 6.553 -70.522 11.456 1.00 16.63 ? 185 PRO B C 1 ATOM 2806 O O . PRO B 1 135 ? 5.817 -69.993 10.594 1.00 16.26 ? 185 PRO B O 1 ATOM 2807 C CB . PRO B 1 135 ? 5.937 -70.689 13.913 1.00 16.51 ? 185 PRO B CB 1 ATOM 2808 C CG . PRO B 1 135 ? 5.686 -69.609 14.975 1.00 19.77 ? 185 PRO B CG 1 ATOM 2809 C CD . PRO B 1 135 ? 5.265 -68.471 14.060 1.00 16.98 ? 185 PRO B CD 1 ATOM 2810 N N . ASN B 1 136 ? 7.255 -71.634 11.246 1.00 14.68 ? 186 ASN B N 1 ATOM 2811 C CA . ASN B 1 136 ? 7.210 -72.402 9.996 1.00 15.22 ? 186 ASN B CA 1 ATOM 2812 C C . ASN B 1 136 ? 5.854 -73.161 9.808 1.00 18.66 ? 186 ASN B C 1 ATOM 2813 O O . ASN B 1 136 ? 5.383 -73.360 8.675 1.00 17.55 ? 186 ASN B O 1 ATOM 2814 C CB . ASN B 1 136 ? 8.358 -73.446 9.995 1.00 16.92 ? 186 ASN B CB 1 ATOM 2815 C CG . ASN B 1 136 ? 8.473 -74.148 8.660 1.00 22.48 ? 186 ASN B CG 1 ATOM 2816 O OD1 . ASN B 1 136 ? 8.901 -73.531 7.654 1.00 21.78 ? 186 ASN B OD1 1 ATOM 2817 N ND2 . ASN B 1 136 ? 7.994 -75.407 8.580 1.00 24.53 ? 186 ASN B ND2 1 ATOM 2818 N N . ASP B 1 137 ? 5.264 -73.637 10.914 1.00 15.87 ? 187 ASP B N 1 ATOM 2819 C CA . ASP B 1 137 ? 4.070 -74.496 10.855 1.00 15.63 ? 187 ASP B CA 1 ATOM 2820 C C . ASP B 1 137 ? 3.291 -74.456 12.151 1.00 17.29 ? 187 ASP B C 1 ATOM 2821 O O . ASP B 1 137 ? 3.812 -73.963 13.144 1.00 17.17 ? 187 ASP B O 1 ATOM 2822 C CB . ASP B 1 137 ? 4.469 -75.947 10.515 1.00 19.31 ? 187 ASP B CB 1 ATOM 2823 C CG . ASP B 1 137 ? 5.587 -76.486 11.384 1.00 31.84 ? 187 ASP B CG 1 ATOM 2824 O OD1 . ASP B 1 137 ? 5.341 -76.716 12.578 1.00 30.97 ? 187 ASP B OD1 1 ATOM 2825 O OD2 . ASP B 1 137 ? 6.736 -76.579 10.890 1.00 36.34 ? 187 ASP B OD2 1 ATOM 2826 N N . GLU B 1 138 ? 2.033 -74.938 12.152 1.00 17.05 ? 188 GLU B N 1 ATOM 2827 C CA . GLU B 1 138 ? 1.206 -74.888 13.351 1.00 18.42 ? 188 GLU B CA 1 ATOM 2828 C C . GLU B 1 138 ? 1.745 -75.774 14.481 1.00 21.52 ? 188 GLU B C 1 ATOM 2829 O O . GLU B 1 138 ? 1.552 -75.453 15.659 1.00 20.02 ? 188 GLU B O 1 ATOM 2830 C CB . GLU B 1 138 ? -0.272 -75.181 13.032 1.00 19.87 ? 188 GLU B CB 1 ATOM 2831 C CG . GLU B 1 138 ? -0.929 -74.120 12.158 1.00 25.97 ? 188 GLU B CG 1 ATOM 2832 C CD . GLU B 1 138 ? -2.437 -74.273 12.000 1.00 43.58 ? 188 GLU B CD 1 ATOM 2833 O OE1 . GLU B 1 138 ? -2.884 -75.377 11.609 1.00 39.07 ? 188 GLU B OE1 1 ATOM 2834 O OE2 . GLU B 1 138 ? -3.172 -73.284 12.237 1.00 35.11 ? 188 GLU B OE2 1 ATOM 2835 N N . THR B 1 139 ? 2.454 -76.856 14.116 1.00 21.01 ? 189 THR B N 1 ATOM 2836 C CA . THR B 1 139 ? 3.099 -77.738 15.090 1.00 21.65 ? 189 THR B CA 1 ATOM 2837 C C . THR B 1 139 ? 4.149 -76.946 15.876 1.00 22.91 ? 189 THR B C 1 ATOM 2838 O O . THR B 1 139 ? 4.161 -77.036 17.101 1.00 21.78 ? 189 THR B O 1 ATOM 2839 C CB . THR B 1 139 ? 3.644 -79.001 14.405 1.00 27.49 ? 189 THR B CB 1 ATOM 2840 O OG1 . THR B 1 139 ? 2.552 -79.711 13.813 1.00 29.51 ? 189 THR B OG1 1 ATOM 2841 C CG2 . THR B 1 139 ? 4.395 -79.923 15.369 1.00 27.63 ? 189 THR B CG2 1 ATOM 2842 N N . GLU B 1 140 ? 4.991 -76.136 15.180 1.00 19.94 ? 190 GLU B N 1 ATOM 2843 C CA . GLU B 1 140 ? 6.006 -75.302 15.817 1.00 18.64 ? 190 GLU B CA 1 ATOM 2844 C C . GLU B 1 140 ? 5.352 -74.269 16.726 1.00 18.83 ? 190 GLU B C 1 ATOM 2845 O O . GLU B 1 140 ? 5.804 -74.057 17.844 1.00 19.64 ? 190 GLU B O 1 ATOM 2846 C CB . GLU B 1 140 ? 6.897 -74.614 14.758 1.00 20.17 ? 190 GLU B CB 1 ATOM 2847 C CG . GLU B 1 140 ? 8.127 -73.963 15.378 1.00 30.21 ? 190 GLU B CG 1 ATOM 2848 C CD . GLU B 1 140 ? 9.029 -73.045 14.564 1.00 53.51 ? 190 GLU B CD 1 ATOM 2849 O OE1 . GLU B 1 140 ? 8.868 -72.935 13.329 1.00 33.77 ? 190 GLU B OE1 1 ATOM 2850 O OE2 . GLU B 1 140 ? 9.907 -72.413 15.190 1.00 50.75 ? 190 GLU B OE2 1 ATOM 2851 N N . GLN B 1 141 ? 4.259 -73.657 16.263 1.00 15.72 ? 191 GLN B N 1 ATOM 2852 C CA . GLN B 1 141 ? 3.524 -72.674 17.044 1.00 14.21 ? 191 GLN B CA 1 ATOM 2853 C C . GLN B 1 141 ? 3.062 -73.291 18.371 1.00 17.95 ? 191 GLN B C 1 ATOM 2854 O O . GLN B 1 141 ? 3.210 -72.674 19.420 1.00 20.03 ? 191 GLN B O 1 ATOM 2855 C CB . GLN B 1 141 ? 2.304 -72.182 16.249 1.00 15.82 ? 191 GLN B CB 1 ATOM 2856 C CG . GLN B 1 141 ? 1.388 -71.232 17.014 1.00 14.99 ? 191 GLN B CG 1 ATOM 2857 C CD . GLN B 1 141 ? 2.007 -69.930 17.364 1.00 17.55 ? 191 GLN B CD 1 ATOM 2858 O OE1 . GLN B 1 141 ? 2.853 -69.401 16.608 1.00 17.46 ? 191 GLN B OE1 1 ATOM 2859 N NE2 . GLN B 1 141 ? 1.493 -69.311 18.431 1.00 14.26 ? 191 GLN B NE2 1 ATOM 2860 N N . ARG B 1 142 ? 2.488 -74.504 18.316 1.00 18.00 ? 192 ARG B N 1 ATOM 2861 C CA . ARG B 1 142 ? 1.999 -75.172 19.520 1.00 19.03 ? 192 ARG B CA 1 ATOM 2862 C C . ARG B 1 142 ? 3.115 -75.590 20.445 1.00 22.08 ? 192 ARG B C 1 ATOM 2863 O O . ARG B 1 142 ? 2.972 -75.457 21.661 1.00 21.03 ? 192 ARG B O 1 ATOM 2864 C CB . ARG B 1 142 ? 1.072 -76.340 19.166 1.00 18.39 ? 192 ARG B CB 1 ATOM 2865 C CG . ARG B 1 142 ? -0.275 -75.833 18.652 1.00 27.42 ? 192 ARG B CG 1 ATOM 2866 C CD . ARG B 1 142 ? -1.268 -76.959 18.395 1.00 29.90 ? 192 ARG B CD 1 ATOM 2867 N NE . ARG B 1 142 ? -2.541 -76.427 17.910 1.00 37.92 ? 192 ARG B NE 1 ATOM 2868 C CZ . ARG B 1 142 ? -2.934 -76.448 16.641 1.00 51.88 ? 192 ARG B CZ 1 ATOM 2869 N NH1 . ARG B 1 142 ? -2.177 -77.024 15.712 1.00 38.82 ? 192 ARG B NH1 1 ATOM 2870 N NH2 . ARG B 1 142 ? -4.103 -75.924 16.294 1.00 39.61 ? 192 ARG B NH2 1 ATOM 2871 N N . THR B 1 143 ? 4.226 -76.054 19.889 1.00 19.32 ? 193 THR B N 1 ATOM 2872 C CA . THR B 1 143 ? 5.369 -76.476 20.697 1.00 19.33 ? 193 THR B CA 1 ATOM 2873 C C . THR B 1 143 ? 5.940 -75.322 21.491 1.00 22.52 ? 193 THR B C 1 ATOM 2874 O O . THR B 1 143 ? 6.264 -75.481 22.667 1.00 22.65 ? 193 THR B O 1 ATOM 2875 C CB . THR B 1 143 ? 6.457 -77.153 19.847 1.00 25.98 ? 193 THR B CB 1 ATOM 2876 O OG1 . THR B 1 143 ? 6.949 -76.229 18.893 1.00 40.69 ? 193 THR B OG1 1 ATOM 2877 C CG2 . THR B 1 143 ? 5.960 -78.376 19.135 1.00 19.59 ? 193 THR B CG2 1 ATOM 2878 N N . LEU B 1 144 ? 6.066 -74.165 20.847 1.00 17.11 ? 194 LEU B N 1 ATOM 2879 C CA . LEU B 1 144 ? 6.683 -73.021 21.500 1.00 16.32 ? 194 LEU B CA 1 ATOM 2880 C C . LEU B 1 144 ? 5.722 -72.250 22.361 1.00 19.61 ? 194 LEU B C 1 ATOM 2881 O O . LEU B 1 144 ? 6.103 -71.836 23.447 1.00 20.12 ? 194 LEU B O 1 ATOM 2882 C CB . LEU B 1 144 ? 7.257 -72.079 20.454 1.00 16.19 ? 194 LEU B CB 1 ATOM 2883 C CG . LEU B 1 144 ? 8.406 -72.625 19.575 1.00 20.29 ? 194 LEU B CG 1 ATOM 2884 C CD1 . LEU B 1 144 ? 8.625 -71.728 18.365 1.00 21.86 ? 194 LEU B CD1 1 ATOM 2885 C CD2 . LEU B 1 144 ? 9.711 -72.752 20.374 1.00 22.65 ? 194 LEU B CD2 1 ATOM 2886 N N . TYR B 1 145 ? 4.473 -72.052 21.889 1.00 16.19 ? 195 TYR B N 1 ATOM 2887 C CA . TYR B 1 145 ? 3.502 -71.141 22.508 1.00 16.84 ? 195 TYR B CA 1 ATOM 2888 C C . TYR B 1 145 ? 2.147 -71.730 22.880 1.00 19.84 ? 195 TYR B C 1 ATOM 2889 O O . TYR B 1 145 ? 1.196 -70.976 23.114 1.00 19.32 ? 195 TYR B O 1 ATOM 2890 C CB . TYR B 1 145 ? 3.303 -69.880 21.618 1.00 17.15 ? 195 TYR B CB 1 ATOM 2891 C CG . TYR B 1 145 ? 4.594 -69.364 21.020 1.00 13.75 ? 195 TYR B CG 1 ATOM 2892 C CD1 . TYR B 1 145 ? 5.551 -68.746 21.812 1.00 15.20 ? 195 TYR B CD1 1 ATOM 2893 C CD2 . TYR B 1 145 ? 4.877 -69.538 19.670 1.00 14.12 ? 195 TYR B CD2 1 ATOM 2894 C CE1 . TYR B 1 145 ? 6.757 -68.299 21.274 1.00 16.72 ? 195 TYR B CE1 1 ATOM 2895 C CE2 . TYR B 1 145 ? 6.057 -69.057 19.108 1.00 14.46 ? 195 TYR B CE2 1 ATOM 2896 C CZ . TYR B 1 145 ? 7.018 -68.475 19.922 1.00 15.83 ? 195 TYR B CZ 1 ATOM 2897 O OH . TYR B 1 145 ? 8.205 -68.065 19.397 1.00 15.18 ? 195 TYR B OH 1 ATOM 2898 N N . GLN B 1 146 ? 2.037 -73.081 22.877 1.00 18.28 ? 196 GLN B N 1 ATOM 2899 C CA . GLN B 1 146 ? 0.838 -73.828 23.254 1.00 19.21 ? 196 GLN B CA 1 ATOM 2900 C C . GLN B 1 146 ? -0.348 -73.819 22.277 1.00 23.79 ? 196 GLN B C 1 ATOM 2901 O O . GLN B 1 146 ? -0.920 -74.878 22.004 1.00 24.90 ? 196 GLN B O 1 ATOM 2902 C CB . GLN B 1 146 ? 0.443 -73.577 24.718 1.00 21.69 ? 196 GLN B CB 1 ATOM 2903 C CG . GLN B 1 146 ? -0.523 -74.610 25.297 1.00 41.91 ? 196 GLN B CG 1 ATOM 2904 C CD . GLN B 1 146 ? 0.005 -76.035 25.411 1.00 69.32 ? 196 GLN B CD 1 ATOM 2905 O OE1 . GLN B 1 146 ? 1.214 -76.295 25.533 1.00 64.39 ? 196 GLN B OE1 1 ATOM 2906 N NE2 . GLN B 1 146 ? -0.914 -76.988 25.450 1.00 64.48 ? 196 GLN B NE2 1 ATOM 2907 N N . ASN B 1 147 ? -0.722 -72.637 21.767 1.00 21.01 ? 197 ASN B N 1 ATOM 2908 C CA . ASN B 1 147 ? -1.882 -72.551 20.883 1.00 22.54 ? 197 ASN B CA 1 ATOM 2909 C C . ASN B 1 147 ? -1.655 -71.642 19.703 1.00 26.55 ? 197 ASN B C 1 ATOM 2910 O O . ASN B 1 147 ? -0.793 -70.753 19.743 1.00 23.28 ? 197 ASN B O 1 ATOM 2911 C CB . ASN B 1 147 ? -3.082 -72.001 21.658 1.00 25.58 ? 197 ASN B CB 1 ATOM 2912 C CG . ASN B 1 147 ? -3.708 -72.975 22.617 1.00 38.76 ? 197 ASN B CG 1 ATOM 2913 O OD1 . ASN B 1 147 ? -4.309 -73.981 22.221 1.00 37.69 ? 197 ASN B OD1 1 ATOM 2914 N ND2 . ASN B 1 147 ? -3.651 -72.650 23.893 1.00 28.61 ? 197 ASN B ND2 1 ATOM 2915 N N . VAL B 1 148 ? -2.464 -71.873 18.654 1.00 23.06 ? 198 VAL B N 1 ATOM 2916 C CA . VAL B 1 148 ? -2.524 -71.015 17.485 1.00 22.97 ? 198 VAL B CA 1 ATOM 2917 C C . VAL B 1 148 ? -3.551 -69.947 17.879 1.00 28.00 ? 198 VAL B C 1 ATOM 2918 O O . VAL B 1 148 ? -4.591 -70.269 18.483 1.00 30.36 ? 198 VAL B O 1 ATOM 2919 C CB . VAL B 1 148 ? -2.943 -71.811 16.216 1.00 27.03 ? 198 VAL B CB 1 ATOM 2920 C CG1 . VAL B 1 148 ? -3.299 -70.880 15.040 1.00 27.76 ? 198 VAL B CG1 1 ATOM 2921 C CG2 . VAL B 1 148 ? -1.840 -72.798 15.809 1.00 26.84 ? 198 VAL B CG2 1 ATOM 2922 N N . GLY B 1 149 ? -3.269 -68.702 17.527 1.00 22.07 ? 199 GLY B N 1 ATOM 2923 C CA . GLY B 1 149 ? -4.178 -67.601 17.788 1.00 21.82 ? 199 GLY B CA 1 ATOM 2924 C C . GLY B 1 149 ? -3.612 -66.750 18.901 1.00 25.43 ? 199 GLY B C 1 ATOM 2925 O O . GLY B 1 149 ? -4.017 -66.881 20.053 1.00 26.96 ? 199 GLY B O 1 ATOM 2926 N N . THR B 1 150 ? -2.567 -66.006 18.576 1.00 18.06 ? 200 THR B N 1 ATOM 2927 C CA . THR B 1 150 ? -1.831 -65.166 19.551 1.00 13.54 ? 200 THR B CA 1 ATOM 2928 C C . THR B 1 150 ? -1.646 -63.753 18.979 1.00 15.32 ? 200 THR B C 1 ATOM 2929 O O . THR B 1 150 ? -1.883 -63.515 17.804 1.00 16.09 ? 200 THR B O 1 ATOM 2930 C CB . THR B 1 150 ? -0.437 -65.824 19.858 1.00 16.57 ? 200 THR B CB 1 ATOM 2931 O OG1 . THR B 1 150 ? 0.288 -65.954 18.644 1.00 17.25 ? 200 THR B OG1 1 ATOM 2932 C CG2 . THR B 1 150 ? -0.557 -67.284 20.451 1.00 16.37 ? 200 THR B CG2 1 ATOM 2933 N N . TYR B 1 151 ? -1.199 -62.846 19.821 1.00 14.92 ? 201 TYR B N 1 ATOM 2934 C CA . TYR B 1 151 ? -0.862 -61.481 19.419 1.00 13.95 ? 201 TYR B CA 1 ATOM 2935 C C . TYR B 1 151 ? 0.355 -60.985 20.174 1.00 15.89 ? 201 TYR B C 1 ATOM 2936 O O . TYR B 1 151 ? 0.666 -61.473 21.256 1.00 13.70 ? 201 TYR B O 1 ATOM 2937 C CB . TYR B 1 151 ? -2.020 -60.528 19.639 1.00 14.40 ? 201 TYR B CB 1 ATOM 2938 C CG . TYR B 1 151 ? -2.514 -60.413 21.068 1.00 15.92 ? 201 TYR B CG 1 ATOM 2939 C CD1 . TYR B 1 151 ? -1.916 -59.532 21.968 1.00 17.76 ? 201 TYR B CD1 1 ATOM 2940 C CD2 . TYR B 1 151 ? -3.688 -61.061 21.474 1.00 18.53 ? 201 TYR B CD2 1 ATOM 2941 C CE1 . TYR B 1 151 ? -2.410 -59.384 23.273 1.00 18.41 ? 201 TYR B CE1 1 ATOM 2942 C CE2 . TYR B 1 151 ? -4.216 -60.876 22.740 1.00 19.75 ? 201 TYR B CE2 1 ATOM 2943 C CZ . TYR B 1 151 ? -3.566 -60.057 23.644 1.00 28.73 ? 201 TYR B CZ 1 ATOM 2944 O OH . TYR B 1 151 ? -4.091 -59.931 24.895 1.00 32.83 ? 201 TYR B OH 1 ATOM 2945 N N . VAL B 1 152 ? 1.001 -59.939 19.623 1.00 13.58 ? 202 VAL B N 1 ATOM 2946 C CA . VAL B 1 152 ? 2.103 -59.243 20.297 1.00 13.15 ? 202 VAL B CA 1 ATOM 2947 C C . VAL B 1 152 ? 1.693 -57.785 20.217 1.00 17.35 ? 202 VAL B C 1 ATOM 2948 O O . VAL B 1 152 ? 1.612 -57.249 19.097 1.00 19.27 ? 202 VAL B O 1 ATOM 2949 C CB . VAL B 1 152 ? 3.508 -59.467 19.646 1.00 15.07 ? 202 VAL B CB 1 ATOM 2950 C CG1 . VAL B 1 152 ? 4.634 -58.664 20.373 1.00 15.01 ? 202 VAL B CG1 1 ATOM 2951 C CG2 . VAL B 1 152 ? 3.866 -60.950 19.603 1.00 15.66 ? 202 VAL B CG2 1 ATOM 2952 N N . SER B 1 153 ? 1.438 -57.156 21.376 1.00 12.79 ? 203 SER B N 1 ATOM 2953 C CA A SER B 1 153 ? 1.062 -55.739 21.429 0.50 12.55 ? 203 SER B CA 1 ATOM 2954 C CA B SER B 1 153 ? 1.061 -55.740 21.419 0.50 13.34 ? 203 SER B CA 1 ATOM 2955 C C . SER B 1 153 ? 2.096 -54.889 22.163 1.00 14.77 ? 203 SER B C 1 ATOM 2956 O O . SER B 1 153 ? 2.525 -55.244 23.260 1.00 16.49 ? 203 SER B O 1 ATOM 2957 C CB A SER B 1 153 ? -0.311 -55.582 22.072 0.50 14.79 ? 203 SER B CB 1 ATOM 2958 C CB B SER B 1 153 ? -0.339 -55.568 22.009 0.50 18.32 ? 203 SER B CB 1 ATOM 2959 O OG A SER B 1 153 ? -1.272 -56.320 21.342 0.50 19.45 ? 203 SER B OG 1 ATOM 2960 O OG B SER B 1 153 ? -0.351 -55.611 23.427 0.50 33.54 ? 203 SER B OG 1 ATOM 2961 N N . VAL B 1 154 ? 2.527 -53.790 21.551 1.00 13.80 ? 204 VAL B N 1 ATOM 2962 C CA . VAL B 1 154 ? 3.525 -52.878 22.138 1.00 13.37 ? 204 VAL B CA 1 ATOM 2963 C C . VAL B 1 154 ? 2.978 -51.472 22.037 1.00 18.06 ? 204 VAL B C 1 ATOM 2964 O O . VAL B 1 154 ? 2.539 -51.082 20.955 1.00 18.86 ? 204 VAL B O 1 ATOM 2965 C CB . VAL B 1 154 ? 4.907 -53.002 21.418 1.00 16.73 ? 204 VAL B CB 1 ATOM 2966 C CG1 . VAL B 1 154 ? 5.962 -52.149 22.119 1.00 17.03 ? 204 VAL B CG1 1 ATOM 2967 C CG2 . VAL B 1 154 ? 5.367 -54.463 21.354 1.00 17.31 ? 204 VAL B CG2 1 ATOM 2968 N N . GLY B 1 155 ? 2.994 -50.728 23.132 1.00 13.89 ? 205 GLY B N 1 ATOM 2969 C CA . GLY B 1 155 ? 2.457 -49.384 23.083 1.00 15.09 ? 205 GLY B CA 1 ATOM 2970 C C . GLY B 1 155 ? 3.207 -48.389 23.923 1.00 19.19 ? 205 GLY B C 1 ATOM 2971 O O . GLY B 1 155 ? 3.757 -48.739 24.960 1.00 20.34 ? 205 GLY B O 1 ATOM 2972 N N . THR B 1 156 ? 3.230 -47.119 23.457 1.00 16.76 ? 206 THR B N 1 ATOM 2973 C CA . THR B 1 156 ? 3.781 -46.030 24.219 1.00 17.52 ? 206 THR B CA 1 ATOM 2974 C C . THR B 1 156 ? 2.807 -44.880 23.924 1.00 20.08 ? 206 THR B C 1 ATOM 2975 O O . THR B 1 156 ? 1.798 -45.077 23.243 1.00 18.92 ? 206 THR B O 1 ATOM 2976 C CB . THR B 1 156 ? 5.220 -45.646 23.696 1.00 20.01 ? 206 THR B CB 1 ATOM 2977 O OG1 . THR B 1 156 ? 5.091 -45.036 22.402 1.00 19.00 ? 206 THR B OG1 1 ATOM 2978 C CG2 . THR B 1 156 ? 6.203 -46.863 23.605 1.00 18.97 ? 206 THR B CG2 1 ATOM 2979 N N . SER B 1 157 ? 3.136 -43.668 24.364 1.00 19.78 ? 207 SER B N 1 ATOM 2980 C CA A SER B 1 157 ? 2.259 -42.534 24.067 0.50 20.09 ? 207 SER B CA 1 ATOM 2981 C CA B SER B 1 157 ? 2.271 -42.520 24.075 0.50 20.04 ? 207 SER B CA 1 ATOM 2982 C C . SER B 1 157 ? 2.253 -42.236 22.557 1.00 22.94 ? 207 SER B C 1 ATOM 2983 O O . SER B 1 157 ? 1.322 -41.574 22.082 1.00 23.86 ? 207 SER B O 1 ATOM 2984 C CB A SER B 1 157 ? 2.696 -41.306 24.861 0.50 24.33 ? 207 SER B CB 1 ATOM 2985 C CB B SER B 1 157 ? 2.760 -41.287 24.835 0.50 24.00 ? 207 SER B CB 1 ATOM 2986 O OG A SER B 1 157 ? 2.489 -41.534 26.244 0.50 30.97 ? 207 SER B OG 1 ATOM 2987 O OG B SER B 1 157 ? 3.985 -40.812 24.303 0.50 30.15 ? 207 SER B OG 1 ATOM 2988 N N . THR B 1 158 ? 3.292 -42.707 21.791 1.00 17.93 ? 208 THR B N 1 ATOM 2989 C CA . THR B 1 158 ? 3.388 -42.428 20.345 1.00 18.19 ? 208 THR B CA 1 ATOM 2990 C C . THR B 1 158 ? 3.353 -43.671 19.433 1.00 22.89 ? 208 THR B C 1 ATOM 2991 O O . THR B 1 158 ? 3.457 -43.540 18.214 1.00 23.98 ? 208 THR B O 1 ATOM 2992 C CB . THR B 1 158 ? 4.669 -41.592 20.034 1.00 28.29 ? 208 THR B CB 1 ATOM 2993 O OG1 . THR B 1 158 ? 5.806 -42.366 20.403 1.00 24.08 ? 208 THR B OG1 1 ATOM 2994 C CG2 . THR B 1 158 ? 4.707 -40.254 20.770 1.00 31.05 ? 208 THR B CG2 1 ATOM 2995 N N . LEU B 1 159 ? 3.170 -44.867 20.023 1.00 18.89 ? 209 LEU B N 1 ATOM 2996 C CA . LEU B 1 159 ? 3.206 -46.127 19.322 1.00 17.52 ? 209 LEU B CA 1 ATOM 2997 C C . LEU B 1 159 ? 2.029 -47.013 19.777 1.00 19.32 ? 209 LEU B C 1 ATOM 2998 O O . LEU B 1 159 ? 1.689 -47.034 20.940 1.00 18.67 ? 209 LEU B O 1 ATOM 2999 C CB . LEU B 1 159 ? 4.522 -46.821 19.655 1.00 17.22 ? 209 LEU B CB 1 ATOM 3000 C CG . LEU B 1 159 ? 4.678 -48.258 19.110 1.00 22.46 ? 209 LEU B CG 1 ATOM 3001 C CD1 . LEU B 1 159 ? 4.932 -48.261 17.607 1.00 23.21 ? 209 LEU B CD1 1 ATOM 3002 C CD2 . LEU B 1 159 ? 5.736 -49.021 19.880 1.00 23.05 ? 209 LEU B CD2 1 ATOM 3003 N N . ASN B 1 160 ? 1.416 -47.725 18.850 1.00 17.43 ? 210 ASN B N 1 ATOM 3004 C CA . ASN B 1 160 ? 0.354 -48.689 19.138 1.00 17.21 ? 210 ASN B CA 1 ATOM 3005 C C . ASN B 1 160 ? 0.457 -49.772 18.076 1.00 20.88 ? 210 ASN B C 1 ATOM 3006 O O . ASN B 1 160 ? -0.141 -49.636 17.009 1.00 22.42 ? 210 ASN B O 1 ATOM 3007 C CB . ASN B 1 160 ? -1.015 -48.019 19.190 1.00 20.68 ? 210 ASN B CB 1 ATOM 3008 C CG . ASN B 1 160 ? -2.141 -48.925 19.632 1.00 42.65 ? 210 ASN B CG 1 ATOM 3009 O OD1 . ASN B 1 160 ? -1.954 -50.093 20.030 1.00 40.14 ? 210 ASN B OD1 1 ATOM 3010 N ND2 . ASN B 1 160 ? -3.356 -48.421 19.510 1.00 42.17 ? 210 ASN B ND2 1 ATOM 3011 N N . LYS B 1 161 ? 1.316 -50.802 18.318 1.00 15.42 ? 211 LYS B N 1 ATOM 3012 C CA . LYS B 1 161 ? 1.522 -51.844 17.312 1.00 16.31 ? 211 LYS B CA 1 ATOM 3013 C C . LYS B 1 161 ? 1.026 -53.141 17.875 1.00 22.10 ? 211 LYS B C 1 ATOM 3014 O O . LYS B 1 161 ? 1.505 -53.561 18.919 1.00 23.79 ? 211 LYS B O 1 ATOM 3015 C CB . LYS B 1 161 ? 3.012 -51.929 16.920 1.00 20.23 ? 211 LYS B CB 1 ATOM 3016 C CG . LYS B 1 161 ? 3.291 -52.825 15.710 1.00 38.21 ? 211 LYS B CG 1 ATOM 3017 C CD . LYS B 1 161 ? 4.667 -52.523 15.144 1.00 48.02 ? 211 LYS B CD 1 ATOM 3018 C CE . LYS B 1 161 ? 5.014 -53.355 13.932 1.00 58.23 ? 211 LYS B CE 1 ATOM 3019 N NZ . LYS B 1 161 ? 6.292 -52.892 13.318 1.00 60.98 ? 211 LYS B NZ 1 ATOM 3020 N N . ARG B 1 162 ? 0.042 -53.770 17.209 1.00 15.57 ? 212 ARG B N 1 ATOM 3021 C CA . ARG B 1 162 ? -0.538 -55.018 17.715 1.00 15.24 ? 212 ARG B CA 1 ATOM 3022 C C . ARG B 1 162 ? -0.525 -56.045 16.550 1.00 23.56 ? 212 ARG B C 1 ATOM 3023 O O . ARG B 1 162 ? -1.422 -56.053 15.693 1.00 25.83 ? 212 ARG B O 1 ATOM 3024 C CB . ARG B 1 162 ? -1.950 -54.757 18.230 1.00 19.47 ? 212 ARG B CB 1 ATOM 3025 C CG . ARG B 1 162 ? -2.021 -53.578 19.190 1.00 19.63 ? 212 ARG B CG 1 ATOM 3026 C CD . ARG B 1 162 ? -3.345 -53.418 19.945 1.00 29.10 ? 212 ARG B CD 1 ATOM 3027 N NE . ARG B 1 162 ? -3.191 -52.380 20.975 1.00 32.44 ? 212 ARG B NE 1 ATOM 3028 C CZ . ARG B 1 162 ? -3.941 -52.245 22.062 1.00 40.34 ? 212 ARG B CZ 1 ATOM 3029 N NH1 . ARG B 1 162 ? -4.936 -53.094 22.306 1.00 27.00 ? 212 ARG B NH1 1 ATOM 3030 N NH2 . ARG B 1 162 ? -3.698 -51.262 22.922 1.00 29.22 ? 212 ARG B NH2 1 ATOM 3031 N N . SER B 1 163 ? 0.515 -56.914 16.548 1.00 20.41 ? 213 SER B N 1 ATOM 3032 C CA . SER B 1 163 ? 0.833 -57.866 15.514 1.00 20.53 ? 213 SER B CA 1 ATOM 3033 C C . SER B 1 163 ? 0.264 -59.222 15.757 1.00 23.46 ? 213 SER B C 1 ATOM 3034 O O . SER B 1 163 ? 0.047 -59.642 16.898 1.00 20.64 ? 213 SER B O 1 ATOM 3035 C CB . SER B 1 163 ? 2.353 -58.033 15.404 1.00 20.60 ? 213 SER B CB 1 ATOM 3036 O OG . SER B 1 163 ? 3.029 -56.781 15.442 1.00 28.89 ? 213 SER B OG 1 ATOM 3037 N N . THR B 1 164 ? 0.065 -59.926 14.651 1.00 20.38 ? 214 THR B N 1 ATOM 3038 C CA . THR B 1 164 ? -0.371 -61.293 14.669 1.00 20.56 ? 214 THR B CA 1 ATOM 3039 C C . THR B 1 164 ? 0.726 -62.091 13.927 1.00 20.93 ? 214 THR B C 1 ATOM 3040 O O . THR B 1 164 ? 1.141 -61.684 12.841 1.00 21.68 ? 214 THR B O 1 ATOM 3041 C CB . THR B 1 164 ? -1.759 -61.430 14.015 1.00 32.71 ? 214 THR B CB 1 ATOM 3042 O OG1 . THR B 1 164 ? -1.671 -61.092 12.634 1.00 42.96 ? 214 THR B OG1 1 ATOM 3043 C CG2 . THR B 1 164 ? -2.820 -60.569 14.710 1.00 31.17 ? 214 THR B CG2 1 ATOM 3044 N N . PRO B 1 165 ? 1.194 -63.211 14.488 1.00 15.77 ? 215 PRO B N 1 ATOM 3045 C CA . PRO B 1 165 ? 2.209 -64.029 13.782 1.00 16.76 ? 215 PRO B CA 1 ATOM 3046 C C . PRO B 1 165 ? 1.703 -64.656 12.503 1.00 15.87 ? 215 PRO B C 1 ATOM 3047 O O . PRO B 1 165 ? 0.513 -64.956 12.386 1.00 19.12 ? 215 PRO B O 1 ATOM 3048 C CB . PRO B 1 165 ? 2.562 -65.144 14.775 1.00 20.02 ? 215 PRO B CB 1 ATOM 3049 C CG . PRO B 1 165 ? 1.985 -64.710 16.070 1.00 25.65 ? 215 PRO B CG 1 ATOM 3050 C CD . PRO B 1 165 ? 0.800 -63.827 15.769 1.00 20.27 ? 215 PRO B CD 1 ATOM 3051 N N . GLU B 1 166 ? 2.604 -64.830 11.542 1.00 14.42 ? 216 GLU B N 1 ATOM 3052 C CA . GLU B 1 166 ? 2.267 -65.446 10.244 1.00 14.95 ? 216 GLU B CA 1 ATOM 3053 C C . GLU B 1 166 ? 2.862 -66.857 10.184 1.00 17.75 ? 216 GLU B C 1 ATOM 3054 O O . GLU B 1 166 ? 4.077 -67.008 10.182 1.00 20.87 ? 216 GLU B O 1 ATOM 3055 C CB . GLU B 1 166 ? 2.821 -64.582 9.120 1.00 18.24 ? 216 GLU B CB 1 ATOM 3056 C CG . GLU B 1 166 ? 2.047 -63.298 8.871 1.00 31.58 ? 216 GLU B CG 1 ATOM 3057 C CD . GLU B 1 166 ? 2.793 -62.350 7.951 1.00 57.71 ? 216 GLU B CD 1 ATOM 3058 O OE1 . GLU B 1 166 ? 2.981 -62.696 6.762 1.00 55.52 ? 216 GLU B OE1 1 ATOM 3059 O OE2 . GLU B 1 166 ? 3.226 -61.278 8.431 1.00 51.58 ? 216 GLU B OE2 1 ATOM 3060 N N . ILE B 1 167 ? 2.017 -67.903 10.167 1.00 14.40 ? 217 ILE B N 1 ATOM 3061 C CA . ILE B 1 167 ? 2.516 -69.282 10.139 1.00 14.35 ? 217 ILE B CA 1 ATOM 3062 C C . ILE B 1 167 ? 2.588 -69.730 8.699 1.00 15.31 ? 217 ILE B C 1 ATOM 3063 O O . ILE B 1 167 ? 1.561 -69.837 8.048 1.00 14.43 ? 217 ILE B O 1 ATOM 3064 C CB . ILE B 1 167 ? 1.616 -70.207 11.005 1.00 17.61 ? 217 ILE B CB 1 ATOM 3065 C CG1 . ILE B 1 167 ? 1.701 -69.803 12.507 1.00 18.56 ? 217 ILE B CG1 1 ATOM 3066 C CG2 . ILE B 1 167 ? 1.988 -71.684 10.765 1.00 21.57 ? 217 ILE B CG2 1 ATOM 3067 C CD1 . ILE B 1 167 ? 0.523 -70.191 13.347 1.00 23.86 ? 217 ILE B CD1 1 ATOM 3068 N N . ALA B 1 168 ? 3.806 -70.007 8.202 1.00 15.22 ? 218 ALA B N 1 ATOM 3069 C CA . ALA B 1 168 ? 3.964 -70.367 6.815 1.00 15.45 ? 218 ALA B CA 1 ATOM 3070 C C . ALA B 1 168 ? 5.232 -71.127 6.605 1.00 18.44 ? 218 ALA B C 1 ATOM 3071 O O . ALA B 1 168 ? 6.276 -70.747 7.162 1.00 17.09 ? 218 ALA B O 1 ATOM 3072 C CB . ALA B 1 168 ? 3.975 -69.098 5.960 1.00 16.67 ? 218 ALA B CB 1 ATOM 3073 N N . THR B 1 169 ? 5.178 -72.177 5.732 1.00 16.15 ? 219 THR B N 1 ATOM 3074 C CA . THR B 1 169 ? 6.368 -72.932 5.403 1.00 17.43 ? 219 THR B CA 1 ATOM 3075 C C . THR B 1 169 ? 7.251 -72.011 4.598 1.00 20.97 ? 219 THR B C 1 ATOM 3076 O O . THR B 1 169 ? 6.770 -71.289 3.747 1.00 22.41 ? 219 THR B O 1 ATOM 3077 C CB . THR B 1 169 ? 6.033 -74.240 4.683 1.00 22.96 ? 219 THR B CB 1 ATOM 3078 O OG1 . THR B 1 169 ? 5.213 -75.019 5.543 1.00 27.66 ? 219 THR B OG1 1 ATOM 3079 C CG2 . THR B 1 169 ? 7.286 -75.053 4.321 1.00 22.94 ? 219 THR B CG2 1 ATOM 3080 N N . ARG B 1 170 ? 8.545 -71.997 4.880 1.00 16.33 ? 220 ARG B N 1 ATOM 3081 C CA . ARG B 1 170 ? 9.461 -71.156 4.108 1.00 16.82 ? 220 ARG B CA 1 ATOM 3082 C C . ARG B 1 170 ? 10.718 -71.939 3.870 1.00 21.95 ? 220 ARG B C 1 ATOM 3083 O O . ARG B 1 170 ? 11.024 -72.854 4.645 1.00 20.04 ? 220 ARG B O 1 ATOM 3084 C CB . ARG B 1 170 ? 9.846 -69.864 4.857 1.00 16.88 ? 220 ARG B CB 1 ATOM 3085 C CG . ARG B 1 170 ? 8.659 -68.949 5.086 1.00 16.65 ? 220 ARG B CG 1 ATOM 3086 C CD . ARG B 1 170 ? 8.972 -67.858 6.079 1.00 21.29 ? 220 ARG B CD 1 ATOM 3087 N NE . ARG B 1 170 ? 7.747 -67.267 6.623 1.00 20.12 ? 220 ARG B NE 1 ATOM 3088 C CZ . ARG B 1 170 ? 7.219 -67.576 7.801 1.00 22.01 ? 220 ARG B CZ 1 ATOM 3089 N NH1 . ARG B 1 170 ? 7.804 -68.466 8.585 1.00 18.51 ? 220 ARG B NH1 1 ATOM 3090 N NH2 . ARG B 1 170 ? 6.112 -66.982 8.212 1.00 22.70 ? 220 ARG B NH2 1 ATOM 3091 N N . PRO B 1 171 ? 11.485 -71.574 2.822 1.00 22.23 ? 221 PRO B N 1 ATOM 3092 C CA . PRO B 1 171 ? 12.791 -72.246 2.619 1.00 23.05 ? 221 PRO B CA 1 ATOM 3093 C C . PRO B 1 171 ? 13.687 -72.090 3.861 1.00 23.05 ? 221 PRO B C 1 ATOM 3094 O O . PRO B 1 171 ? 13.645 -71.063 4.549 1.00 18.36 ? 221 PRO B O 1 ATOM 3095 C CB . PRO B 1 171 ? 13.385 -71.537 1.392 1.00 26.12 ? 221 PRO B CB 1 ATOM 3096 C CG . PRO B 1 171 ? 12.265 -70.777 0.768 1.00 30.01 ? 221 PRO B CG 1 ATOM 3097 C CD . PRO B 1 171 ? 11.282 -70.467 1.858 1.00 24.64 ? 221 PRO B CD 1 ATOM 3098 N N . LYS B 1 172 ? 14.451 -73.137 4.202 1.00 17.63 ? 222 LYS B N 1 ATOM 3099 C CA . LYS B 1 172 ? 15.261 -72.975 5.396 1.00 15.48 ? 222 LYS B CA 1 ATOM 3100 C C . LYS B 1 172 ? 16.352 -71.960 5.158 1.00 17.75 ? 222 LYS B C 1 ATOM 3101 O O . LYS B 1 172 ? 16.963 -71.951 4.091 1.00 16.71 ? 222 LYS B O 1 ATOM 3102 C CB . LYS B 1 172 ? 15.872 -74.296 5.876 1.00 21.50 ? 222 LYS B CB 1 ATOM 3103 C CG . LYS B 1 172 ? 14.899 -75.233 6.594 1.00 29.66 ? 222 LYS B CG 1 ATOM 3104 C CD . LYS B 1 172 ? 15.682 -76.468 7.055 1.00 43.41 ? 222 LYS B CD 1 ATOM 3105 C CE . LYS B 1 172 ? 14.850 -77.401 7.887 1.00 62.46 ? 222 LYS B CE 1 ATOM 3106 N NZ . LYS B 1 172 ? 15.648 -78.539 8.412 1.00 77.17 ? 222 LYS B NZ 1 ATOM 3107 N N . VAL B 1 173 ? 16.514 -71.047 6.113 1.00 13.67 ? 223 VAL B N 1 ATOM 3108 C CA . VAL B 1 173 ? 17.669 -70.132 6.094 1.00 14.40 ? 223 VAL B CA 1 ATOM 3109 C C . VAL B 1 173 ? 18.268 -70.270 7.451 1.00 18.32 ? 223 VAL B C 1 ATOM 3110 O O . VAL B 1 173 ? 17.537 -70.166 8.443 1.00 12.73 ? 223 VAL B O 1 ATOM 3111 C CB . VAL B 1 173 ? 17.294 -68.661 5.775 1.00 18.38 ? 223 VAL B CB 1 ATOM 3112 C CG1 . VAL B 1 173 ? 18.525 -67.751 5.880 1.00 18.87 ? 223 VAL B CG1 1 ATOM 3113 C CG2 . VAL B 1 173 ? 16.696 -68.577 4.387 1.00 18.73 ? 223 VAL B CG2 1 ATOM 3114 N N . ASN B 1 174 ? 19.607 -70.506 7.508 1.00 15.20 ? 224 ASN B N 1 ATOM 3115 C CA . ASN B 1 174 ? 20.269 -70.726 8.805 1.00 17.67 ? 224 ASN B CA 1 ATOM 3116 C C . ASN B 1 174 ? 19.573 -71.883 9.588 1.00 19.76 ? 224 ASN B C 1 ATOM 3117 O O . ASN B 1 174 ? 19.444 -71.830 10.809 1.00 20.32 ? 224 ASN B O 1 ATOM 3118 C CB . ASN B 1 174 ? 20.300 -69.424 9.617 1.00 16.69 ? 224 ASN B CB 1 ATOM 3119 C CG . ASN B 1 174 ? 21.074 -68.332 8.915 1.00 33.47 ? 224 ASN B CG 1 ATOM 3120 O OD1 . ASN B 1 174 ? 21.681 -68.544 7.871 1.00 21.99 ? 224 ASN B OD1 1 ATOM 3121 N ND2 . ASN B 1 174 ? 21.017 -67.134 9.431 1.00 23.22 ? 224 ASN B ND2 1 ATOM 3122 N N . GLY B 1 175 ? 19.139 -72.900 8.860 1.00 16.93 ? 225 GLY B N 1 ATOM 3123 C CA . GLY B 1 175 ? 18.454 -74.082 9.386 1.00 18.37 ? 225 GLY B CA 1 ATOM 3124 C C . GLY B 1 175 ? 17.014 -73.923 9.856 1.00 21.77 ? 225 GLY B C 1 ATOM 3125 O O . GLY B 1 175 ? 16.443 -74.878 10.390 1.00 23.09 ? 225 GLY B O 1 ATOM 3126 N N . GLN B 1 176 ? 16.410 -72.749 9.624 1.00 16.76 ? 226 GLN B N 1 ATOM 3127 C CA . GLN B 1 176 ? 15.041 -72.429 10.070 1.00 15.10 ? 226 GLN B CA 1 ATOM 3128 C C . GLN B 1 176 ? 14.052 -71.981 8.993 1.00 15.07 ? 226 GLN B C 1 ATOM 3129 O O . GLN B 1 176 ? 14.403 -71.189 8.138 1.00 16.57 ? 226 GLN B O 1 ATOM 3130 C CB . GLN B 1 176 ? 15.106 -71.297 11.125 1.00 14.46 ? 226 GLN B CB 1 ATOM 3131 C CG . GLN B 1 176 ? 16.105 -71.527 12.285 1.00 20.18 ? 226 GLN B CG 1 ATOM 3132 C CD . GLN B 1 176 ? 15.758 -72.737 13.114 1.00 32.99 ? 226 GLN B CD 1 ATOM 3133 O OE1 . GLN B 1 176 ? 14.601 -73.147 13.204 1.00 33.52 ? 226 GLN B OE1 1 ATOM 3134 N NE2 . GLN B 1 176 ? 16.753 -73.347 13.717 1.00 36.01 ? 226 GLN B NE2 1 ATOM 3135 N N . GLY B 1 177 ? 12.826 -72.476 9.076 1.00 14.98 ? 227 GLY B N 1 ATOM 3136 C CA . GLY B 1 177 ? 11.706 -72.014 8.243 1.00 15.11 ? 227 GLY B CA 1 ATOM 3137 C C . GLY B 1 177 ? 10.955 -70.864 8.886 1.00 18.22 ? 227 GLY B C 1 ATOM 3138 O O . GLY B 1 177 ? 10.314 -70.053 8.220 1.00 17.53 ? 227 GLY B O 1 ATOM 3139 N N . GLY B 1 178 ? 11.074 -70.759 10.199 1.00 15.57 ? 228 GLY B N 1 ATOM 3140 C CA . GLY B 1 178 ? 10.499 -69.639 10.922 1.00 15.83 ? 228 GLY B CA 1 ATOM 3141 C C . GLY B 1 178 ? 11.274 -68.353 10.685 1.00 17.27 ? 228 GLY B C 1 ATOM 3142 O O . GLY B 1 178 ? 12.430 -68.369 10.239 1.00 15.19 ? 228 GLY B O 1 ATOM 3143 N N . ARG B 1 179 ? 10.630 -67.225 10.998 1.00 15.62 ? 229 ARG B N 1 ATOM 3144 C CA . ARG B 1 179 ? 11.262 -65.916 10.821 1.00 13.99 ? 229 ARG B CA 1 ATOM 3145 C C . ARG B 1 179 ? 10.933 -65.018 11.972 1.00 14.61 ? 229 ARG B C 1 ATOM 3146 O O . ARG B 1 179 ? 9.823 -65.097 12.524 1.00 13.63 ? 229 ARG B O 1 ATOM 3147 C CB . ARG B 1 179 ? 10.767 -65.234 9.556 1.00 12.98 ? 229 ARG B CB 1 ATOM 3148 C CG . ARG B 1 179 ? 11.020 -66.010 8.282 1.00 13.00 ? 229 ARG B CG 1 ATOM 3149 C CD . ARG B 1 179 ? 12.460 -65.868 7.842 1.00 15.28 ? 229 ARG B CD 1 ATOM 3150 N NE . ARG B 1 179 ? 12.627 -66.534 6.552 1.00 17.84 ? 229 ARG B NE 1 ATOM 3151 C CZ . ARG B 1 179 ? 12.981 -67.809 6.407 1.00 20.77 ? 229 ARG B CZ 1 ATOM 3152 N NH1 . ARG B 1 179 ? 13.176 -68.573 7.469 1.00 17.30 ? 229 ARG B NH1 1 ATOM 3153 N NH2 . ARG B 1 179 ? 13.152 -68.321 5.199 1.00 19.25 ? 229 ARG B NH2 1 ATOM 3154 N N . MET B 1 180 ? 11.921 -64.181 12.363 1.00 12.17 ? 230 MET B N 1 ATOM 3155 C CA . MET B 1 180 ? 11.671 -63.210 13.443 1.00 10.98 ? 230 MET B CA 1 ATOM 3156 C C . MET B 1 180 ? 11.664 -61.827 12.822 1.00 16.82 ? 230 MET B C 1 ATOM 3157 O O . MET B 1 180 ? 12.594 -61.467 12.090 1.00 16.46 ? 230 MET B O 1 ATOM 3158 C CB . MET B 1 180 ? 12.739 -63.343 14.546 1.00 13.63 ? 230 MET B CB 1 ATOM 3159 C CG . MET B 1 180 ? 12.450 -64.565 15.437 1.00 16.58 ? 230 MET B CG 1 ATOM 3160 S SD . MET B 1 180 ? 13.680 -64.764 16.711 1.00 21.04 ? 230 MET B SD 1 ATOM 3161 C CE . MET B 1 180 ? 13.169 -66.331 17.354 1.00 17.40 ? 230 MET B CE 1 ATOM 3162 N N . GLU B 1 181 ? 10.591 -61.071 13.069 1.00 13.03 ? 231 GLU B N 1 ATOM 3163 C CA . GLU B 1 181 ? 10.398 -59.731 12.512 1.00 13.05 ? 231 GLU B CA 1 ATOM 3164 C C . GLU B 1 181 ? 10.610 -58.751 13.648 1.00 14.75 ? 231 GLU B C 1 ATOM 3165 O O . GLU B 1 181 ? 9.853 -58.726 14.636 1.00 13.15 ? 231 GLU B O 1 ATOM 3166 C CB . GLU B 1 181 ? 8.952 -59.598 12.034 1.00 14.37 ? 231 GLU B CB 1 ATOM 3167 C CG . GLU B 1 181 ? 8.635 -58.229 11.453 1.00 23.09 ? 231 GLU B CG 1 ATOM 3168 C CD . GLU B 1 181 ? 7.209 -58.062 10.959 1.00 35.90 ? 231 GLU B CD 1 ATOM 3169 O OE1 . GLU B 1 181 ? 6.561 -59.071 10.594 1.00 42.28 ? 231 GLU B OE1 1 ATOM 3170 O OE2 . GLU B 1 181 ? 6.737 -56.908 10.943 1.00 31.89 ? 231 GLU B OE2 1 ATOM 3171 N N . PHE B 1 182 ? 11.638 -57.930 13.515 1.00 11.56 ? 232 PHE B N 1 ATOM 3172 C CA . PHE B 1 182 ? 11.933 -56.956 14.552 1.00 10.51 ? 232 PHE B CA 1 ATOM 3173 C C . PHE B 1 182 ? 11.423 -55.584 14.208 1.00 13.58 ? 232 PHE B C 1 ATOM 3174 O O . PHE B 1 182 ? 11.425 -55.194 13.027 1.00 14.28 ? 232 PHE B O 1 ATOM 3175 C CB . PHE B 1 182 ? 13.469 -56.913 14.789 1.00 13.21 ? 232 PHE B CB 1 ATOM 3176 C CG . PHE B 1 182 ? 13.955 -58.199 15.382 1.00 13.35 ? 232 PHE B CG 1 ATOM 3177 C CD1 . PHE B 1 182 ? 13.791 -58.461 16.741 1.00 13.22 ? 232 PHE B CD1 1 ATOM 3178 C CD2 . PHE B 1 182 ? 14.481 -59.199 14.575 1.00 16.65 ? 232 PHE B CD2 1 ATOM 3179 C CE1 . PHE B 1 182 ? 14.171 -59.682 17.286 1.00 16.02 ? 232 PHE B CE1 1 ATOM 3180 C CE2 . PHE B 1 182 ? 14.912 -60.419 15.132 1.00 17.43 ? 232 PHE B CE2 1 ATOM 3181 C CZ . PHE B 1 182 ? 14.740 -60.655 16.475 1.00 16.39 ? 232 PHE B CZ 1 ATOM 3182 N N . SER B 1 183 ? 11.074 -54.833 15.237 1.00 11.40 ? 233 SER B N 1 ATOM 3183 C CA . SER B 1 183 ? 10.643 -53.434 15.123 1.00 13.08 ? 233 SER B CA 1 ATOM 3184 C C . SER B 1 183 ? 11.345 -52.636 16.199 1.00 16.18 ? 233 SER B C 1 ATOM 3185 O O . SER B 1 183 ? 11.865 -53.198 17.160 1.00 14.91 ? 233 SER B O 1 ATOM 3186 C CB . SER B 1 183 ? 9.126 -53.293 15.256 1.00 16.67 ? 233 SER B CB 1 ATOM 3187 O OG . SER B 1 183 ? 8.393 -54.173 14.425 1.00 19.13 ? 233 SER B OG 1 ATOM 3188 N N . TRP B 1 184 ? 11.289 -51.319 16.093 1.00 15.08 ? 234 TRP B N 1 ATOM 3189 C CA . TRP B 1 184 ? 11.968 -50.469 17.041 1.00 15.11 ? 234 TRP B CA 1 ATOM 3190 C C . TRP B 1 184 ? 11.150 -49.215 17.284 1.00 17.36 ? 234 TRP B C 1 ATOM 3191 O O . TRP B 1 184 ? 10.254 -48.865 16.506 1.00 16.67 ? 234 TRP B O 1 ATOM 3192 C CB . TRP B 1 184 ? 13.392 -50.110 16.548 1.00 14.24 ? 234 TRP B CB 1 ATOM 3193 C CG . TRP B 1 184 ? 13.423 -49.264 15.306 1.00 15.07 ? 234 TRP B CG 1 ATOM 3194 C CD1 . TRP B 1 184 ? 13.388 -49.695 14.012 1.00 18.17 ? 234 TRP B CD1 1 ATOM 3195 C CD2 . TRP B 1 184 ? 13.516 -47.833 15.251 1.00 16.55 ? 234 TRP B CD2 1 ATOM 3196 N NE1 . TRP B 1 184 ? 13.430 -48.615 13.150 1.00 19.39 ? 234 TRP B NE1 1 ATOM 3197 C CE2 . TRP B 1 184 ? 13.539 -47.463 13.885 1.00 21.27 ? 234 TRP B CE2 1 ATOM 3198 C CE3 . TRP B 1 184 ? 13.599 -46.825 16.228 1.00 18.80 ? 234 TRP B CE3 1 ATOM 3199 C CZ2 . TRP B 1 184 ? 13.609 -46.123 13.473 1.00 22.31 ? 234 TRP B CZ2 1 ATOM 3200 C CZ3 . TRP B 1 184 ? 13.691 -45.507 15.817 1.00 22.04 ? 234 TRP B CZ3 1 ATOM 3201 C CH2 . TRP B 1 184 ? 13.707 -45.165 14.456 1.00 23.45 ? 234 TRP B CH2 1 ATOM 3202 N N . THR B 1 185 ? 11.427 -48.592 18.404 1.00 13.70 ? 235 THR B N 1 ATOM 3203 C CA . THR B 1 185 ? 10.790 -47.333 18.759 1.00 14.05 ? 235 THR B CA 1 ATOM 3204 C C . THR B 1 185 ? 11.771 -46.509 19.567 1.00 15.41 ? 235 THR B C 1 ATOM 3205 O O . THR B 1 185 ? 12.718 -47.058 20.137 1.00 17.63 ? 235 THR B O 1 ATOM 3206 C CB . THR B 1 185 ? 9.474 -47.585 19.516 1.00 17.90 ? 235 THR B CB 1 ATOM 3207 O OG1 . THR B 1 185 ? 8.717 -46.366 19.544 1.00 24.11 ? 235 THR B OG1 1 ATOM 3208 C CG2 . THR B 1 185 ? 9.690 -48.040 20.950 1.00 19.85 ? 235 THR B CG2 1 ATOM 3209 N N . LEU B 1 186 ? 11.499 -45.236 19.675 1.00 14.33 ? 236 LEU B N 1 ATOM 3210 C CA . LEU B 1 186 ? 12.281 -44.345 20.512 1.00 16.34 ? 236 LEU B CA 1 ATOM 3211 C C . LEU B 1 186 ? 11.339 -43.930 21.648 1.00 22.73 ? 236 LEU B C 1 ATOM 3212 O O . LEU B 1 186 ? 10.273 -43.358 21.388 1.00 23.61 ? 236 LEU B O 1 ATOM 3213 C CB . LEU B 1 186 ? 12.742 -43.134 19.645 1.00 18.42 ? 236 LEU B CB 1 ATOM 3214 C CG . LEU B 1 186 ? 14.078 -42.504 19.909 1.00 26.93 ? 236 LEU B CG 1 ATOM 3215 C CD1 . LEU B 1 186 ? 15.221 -43.547 19.860 1.00 27.83 ? 236 LEU B CD1 1 ATOM 3216 C CD2 . LEU B 1 186 ? 14.367 -41.448 18.815 1.00 30.61 ? 236 LEU B CD2 1 ATOM 3217 N N . LEU B 1 187 ? 11.637 -44.380 22.877 1.00 18.57 ? 237 LEU B N 1 ATOM 3218 C CA . LEU B 1 187 ? 10.786 -44.106 24.050 1.00 17.46 ? 237 LEU B CA 1 ATOM 3219 C C . LEU B 1 187 ? 11.231 -42.806 24.696 1.00 19.51 ? 237 LEU B C 1 ATOM 3220 O O . LEU B 1 187 ? 12.373 -42.712 25.130 1.00 17.81 ? 237 LEU B O 1 ATOM 3221 C CB . LEU B 1 187 ? 10.828 -45.309 25.031 1.00 17.72 ? 237 LEU B CB 1 ATOM 3222 C CG . LEU B 1 187 ? 10.015 -45.172 26.312 1.00 19.14 ? 237 LEU B CG 1 ATOM 3223 C CD1 . LEU B 1 187 ? 8.511 -45.196 26.001 1.00 18.82 ? 237 LEU B CD1 1 ATOM 3224 C CD2 . LEU B 1 187 ? 10.357 -46.295 27.284 1.00 17.76 ? 237 LEU B CD2 1 ATOM 3225 N N . ASP B 1 188 ? 10.331 -41.797 24.723 1.00 18.60 ? 238 ASP B N 1 ATOM 3226 C CA . ASP B 1 188 ? 10.631 -40.484 25.265 1.00 18.41 ? 238 ASP B CA 1 ATOM 3227 C C . ASP B 1 188 ? 10.904 -40.533 26.756 1.00 20.27 ? 238 ASP B C 1 ATOM 3228 O O . ASP B 1 188 ? 10.421 -41.434 27.462 1.00 18.78 ? 238 ASP B O 1 ATOM 3229 C CB . ASP B 1 188 ? 9.458 -39.484 24.981 1.00 21.25 ? 238 ASP B CB 1 ATOM 3230 C CG . ASP B 1 188 ? 9.392 -38.979 23.544 1.00 39.00 ? 238 ASP B CG 1 ATOM 3231 O OD1 . ASP B 1 188 ? 10.467 -38.822 22.916 1.00 40.91 ? 238 ASP B OD1 1 ATOM 3232 O OD2 . ASP B 1 188 ? 8.267 -38.685 23.066 1.00 46.02 ? 238 ASP B OD2 1 ATOM 3233 N N . MET B 1 189 ? 11.618 -39.507 27.258 1.00 20.51 ? 239 MET B N 1 ATOM 3234 C CA . MET B 1 189 ? 11.823 -39.420 28.700 1.00 20.75 ? 239 MET B CA 1 ATOM 3235 C C . MET B 1 189 ? 10.448 -39.336 29.394 1.00 23.46 ? 239 MET B C 1 ATOM 3236 O O . MET B 1 189 ? 9.555 -38.596 28.955 1.00 24.06 ? 239 MET B O 1 ATOM 3237 C CB . MET B 1 189 ? 12.666 -38.203 29.077 1.00 23.56 ? 239 MET B CB 1 ATOM 3238 C CG . MET B 1 189 ? 14.028 -38.219 28.440 1.00 27.63 ? 239 MET B CG 1 ATOM 3239 S SD . MET B 1 189 ? 14.937 -36.674 28.715 1.00 35.09 ? 239 MET B SD 1 ATOM 3240 C CE . MET B 1 189 ? 14.030 -35.553 27.714 1.00 33.72 ? 239 MET B CE 1 ATOM 3241 N N . TRP B 1 190 ? 10.289 -40.115 30.470 1.00 20.00 ? 240 TRP B N 1 ATOM 3242 C CA . TRP B 1 190 ? 9.122 -40.143 31.366 1.00 20.83 ? 240 TRP B CA 1 ATOM 3243 C C . TRP B 1 190 ? 7.908 -40.822 30.752 1.00 24.40 ? 240 TRP B C 1 ATOM 3244 O O . TRP B 1 190 ? 6.838 -40.852 31.373 1.00 26.41 ? 240 TRP B O 1 ATOM 3245 C CB . TRP B 1 190 ? 8.791 -38.739 31.918 1.00 22.39 ? 240 TRP B CB 1 ATOM 3246 C CG . TRP B 1 190 ? 9.998 -37.884 32.231 1.00 24.49 ? 240 TRP B CG 1 ATOM 3247 C CD1 . TRP B 1 190 ? 10.345 -36.713 31.626 1.00 27.94 ? 240 TRP B CD1 1 ATOM 3248 C CD2 . TRP B 1 190 ? 11.042 -38.172 33.177 1.00 25.09 ? 240 TRP B CD2 1 ATOM 3249 N NE1 . TRP B 1 190 ? 11.541 -36.247 32.138 1.00 28.09 ? 240 TRP B NE1 1 ATOM 3250 C CE2 . TRP B 1 190 ? 11.985 -37.119 33.096 1.00 29.41 ? 240 TRP B CE2 1 ATOM 3251 C CE3 . TRP B 1 190 ? 11.285 -39.235 34.075 1.00 26.56 ? 240 TRP B CE3 1 ATOM 3252 C CZ2 . TRP B 1 190 ? 13.137 -37.080 33.892 1.00 28.62 ? 240 TRP B CZ2 1 ATOM 3253 C CZ3 . TRP B 1 190 ? 12.425 -39.189 34.872 1.00 28.53 ? 240 TRP B CZ3 1 ATOM 3254 C CH2 . TRP B 1 190 ? 13.326 -38.117 34.787 1.00 29.25 ? 240 TRP B CH2 1 ATOM 3255 N N . ASP B 1 191 ? 8.086 -41.407 29.552 1.00 19.39 ? 241 ASP B N 1 ATOM 3256 C CA . ASP B 1 191 ? 7.011 -42.153 28.932 1.00 18.49 ? 241 ASP B CA 1 ATOM 3257 C C . ASP B 1 191 ? 7.211 -43.615 29.291 1.00 20.83 ? 241 ASP B C 1 ATOM 3258 O O . ASP B 1 191 ? 8.350 -44.041 29.543 1.00 19.53 ? 241 ASP B O 1 ATOM 3259 C CB . ASP B 1 191 ? 7.025 -41.983 27.403 1.00 19.97 ? 241 ASP B CB 1 ATOM 3260 C CG . ASP B 1 191 ? 5.721 -42.440 26.751 1.00 24.60 ? 241 ASP B CG 1 ATOM 3261 O OD1 . ASP B 1 191 ? 4.682 -42.531 27.471 1.00 26.10 ? 241 ASP B OD1 1 ATOM 3262 O OD2 . ASP B 1 191 ? 5.730 -42.709 25.531 1.00 25.16 ? 241 ASP B OD2 1 ATOM 3263 N N . THR B 1 192 ? 6.115 -44.396 29.240 1.00 17.11 ? 242 THR B N 1 ATOM 3264 C CA . THR B 1 192 ? 6.159 -45.825 29.518 1.00 15.75 ? 242 THR B CA 1 ATOM 3265 C C . THR B 1 192 ? 5.889 -46.657 28.254 1.00 19.07 ? 242 THR B C 1 ATOM 3266 O O . THR B 1 192 ? 4.982 -46.354 27.485 1.00 20.27 ? 242 THR B O 1 ATOM 3267 C CB . THR B 1 192 ? 5.116 -46.148 30.616 1.00 22.41 ? 242 THR B CB 1 ATOM 3268 O OG1 . THR B 1 192 ? 5.445 -45.403 31.802 1.00 24.98 ? 242 THR B OG1 1 ATOM 3269 C CG2 . THR B 1 192 ? 5.006 -47.666 30.933 1.00 20.88 ? 242 THR B CG2 1 ATOM 3270 N N . ILE B 1 193 ? 6.662 -47.736 28.068 1.00 15.69 ? 243 ILE B N 1 ATOM 3271 C CA . ILE B 1 193 ? 6.394 -48.723 27.043 1.00 15.32 ? 243 ILE B CA 1 ATOM 3272 C C . ILE B 1 193 ? 5.687 -49.903 27.717 1.00 18.96 ? 243 ILE B C 1 ATOM 3273 O O . ILE B 1 193 ? 6.081 -50.308 28.826 1.00 15.74 ? 243 ILE B O 1 ATOM 3274 C CB . ILE B 1 193 ? 7.681 -49.145 26.299 1.00 18.72 ? 243 ILE B CB 1 ATOM 3275 C CG1 . ILE B 1 193 ? 7.334 -50.117 25.156 1.00 17.52 ? 243 ILE B CG1 1 ATOM 3276 C CG2 . ILE B 1 193 ? 8.764 -49.694 27.266 1.00 17.78 ? 243 ILE B CG2 1 ATOM 3277 C CD1 . ILE B 1 193 ? 8.349 -50.076 24.050 1.00 16.71 ? 243 ILE B CD1 1 ATOM 3278 N N . ASN B 1 194 ? 4.599 -50.431 27.080 1.00 15.58 ? 244 ASN B N 1 ATOM 3279 C CA . ASN B 1 194 ? 3.871 -51.557 27.638 1.00 13.58 ? 244 ASN B CA 1 ATOM 3280 C C . ASN B 1 194 ? 3.911 -52.673 26.631 1.00 18.06 ? 244 ASN B C 1 ATOM 3281 O O . ASN B 1 194 ? 3.628 -52.419 25.460 1.00 17.67 ? 244 ASN B O 1 ATOM 3282 C CB . ASN B 1 194 ? 2.408 -51.148 27.864 1.00 16.33 ? 244 ASN B CB 1 ATOM 3283 C CG . ASN B 1 194 ? 2.280 -50.142 28.951 1.00 36.72 ? 244 ASN B CG 1 ATOM 3284 O OD1 . ASN B 1 194 ? 2.501 -50.451 30.117 1.00 33.85 ? 244 ASN B OD1 1 ATOM 3285 N ND2 . ASN B 1 194 ? 2.045 -48.899 28.577 1.00 32.93 ? 244 ASN B ND2 1 ATOM 3286 N N . PHE B 1 195 ? 4.208 -53.902 27.091 1.00 14.19 ? 245 PHE B N 1 ATOM 3287 C CA . PHE B 1 195 ? 4.237 -55.087 26.243 1.00 15.26 ? 245 PHE B CA 1 ATOM 3288 C C . PHE B 1 195 ? 3.145 -56.013 26.711 1.00 16.38 ? 245 PHE B C 1 ATOM 3289 O O . PHE B 1 195 ? 2.964 -56.185 27.920 1.00 15.07 ? 245 PHE B O 1 ATOM 3290 C CB . PHE B 1 195 ? 5.563 -55.863 26.386 1.00 16.38 ? 245 PHE B CB 1 ATOM 3291 C CG . PHE B 1 195 ? 6.735 -55.186 25.739 1.00 16.63 ? 245 PHE B CG 1 ATOM 3292 C CD1 . PHE B 1 195 ? 7.059 -55.446 24.407 1.00 17.93 ? 245 PHE B CD1 1 ATOM 3293 C CD2 . PHE B 1 195 ? 7.498 -54.268 26.442 1.00 16.36 ? 245 PHE B CD2 1 ATOM 3294 C CE1 . PHE B 1 195 ? 8.125 -54.774 23.791 1.00 19.41 ? 245 PHE B CE1 1 ATOM 3295 C CE2 . PHE B 1 195 ? 8.544 -53.584 25.813 1.00 16.97 ? 245 PHE B CE2 1 ATOM 3296 C CZ . PHE B 1 195 ? 8.877 -53.873 24.517 1.00 17.22 ? 245 PHE B CZ 1 ATOM 3297 N N . GLU B 1 196 ? 2.408 -56.585 25.763 1.00 14.53 ? 246 GLU B N 1 ATOM 3298 C CA . GLU B 1 196 ? 1.408 -57.598 26.124 1.00 13.96 ? 246 GLU B CA 1 ATOM 3299 C C . GLU B 1 196 ? 1.405 -58.651 25.048 1.00 18.63 ? 246 GLU B C 1 ATOM 3300 O O . GLU B 1 196 ? 1.334 -58.315 23.866 1.00 19.83 ? 246 GLU B O 1 ATOM 3301 C CB . GLU B 1 196 ? 0.025 -56.981 26.340 1.00 14.83 ? 246 GLU B CB 1 ATOM 3302 C CG . GLU B 1 196 ? -1.028 -57.987 26.732 1.00 26.78 ? 246 GLU B CG 1 ATOM 3303 C CD . GLU B 1 196 ? -2.423 -57.448 26.976 1.00 41.21 ? 246 GLU B CD 1 ATOM 3304 O OE1 . GLU B 1 196 ? -2.554 -56.430 27.688 1.00 31.41 ? 246 GLU B OE1 1 ATOM 3305 O OE2 . GLU B 1 196 ? -3.392 -58.100 26.528 1.00 36.32 ? 246 GLU B OE2 1 ATOM 3306 N N . SER B 1 197 ? 1.494 -59.935 25.427 1.00 15.03 ? 247 SER B N 1 ATOM 3307 C CA . SER B 1 197 ? 1.502 -60.958 24.374 1.00 14.18 ? 247 SER B CA 1 ATOM 3308 C C . SER B 1 197 ? 0.970 -62.281 24.908 1.00 14.74 ? 247 SER B C 1 ATOM 3309 O O . SER B 1 197 ? 1.178 -62.625 26.077 1.00 16.72 ? 247 SER B O 1 ATOM 3310 C CB . SER B 1 197 ? 2.938 -61.189 23.906 1.00 16.60 ? 247 SER B CB 1 ATOM 3311 O OG . SER B 1 197 ? 3.003 -62.287 23.008 1.00 20.54 ? 247 SER B OG 1 ATOM 3312 N N . THR B 1 198 ? 0.246 -63.018 24.049 1.00 14.26 ? 248 THR B N 1 ATOM 3313 C CA . THR B 1 198 ? -0.258 -64.358 24.336 1.00 14.48 ? 248 THR B CA 1 ATOM 3314 C C . THR B 1 198 ? 0.578 -65.397 23.598 1.00 16.53 ? 248 THR B C 1 ATOM 3315 O O . THR B 1 198 ? 0.270 -66.598 23.649 1.00 17.45 ? 248 THR B O 1 ATOM 3316 C CB . THR B 1 198 ? -1.739 -64.452 23.995 1.00 14.93 ? 248 THR B CB 1 ATOM 3317 O OG1 . THR B 1 198 ? -1.832 -64.066 22.603 1.00 15.85 ? 248 THR B OG1 1 ATOM 3318 C CG2 . THR B 1 198 ? -2.577 -63.517 24.846 1.00 16.15 ? 248 THR B CG2 1 ATOM 3319 N N . GLY B 1 199 ? 1.685 -64.948 23.010 1.00 14.78 ? 249 GLY B N 1 ATOM 3320 C CA . GLY B 1 199 ? 2.656 -65.825 22.370 1.00 14.10 ? 249 GLY B CA 1 ATOM 3321 C C . GLY B 1 199 ? 3.398 -65.057 21.318 1.00 17.67 ? 249 GLY B C 1 ATOM 3322 O O . GLY B 1 199 ? 2.896 -64.045 20.840 1.00 17.32 ? 249 GLY B O 1 ATOM 3323 N N . ASN B 1 200 ? 4.585 -65.550 20.962 1.00 12.79 ? 250 ASN B N 1 ATOM 3324 C CA . ASN B 1 200 ? 5.365 -65.064 19.819 1.00 11.50 ? 250 ASN B CA 1 ATOM 3325 C C . ASN B 1 200 ? 6.154 -63.803 20.010 1.00 14.13 ? 250 ASN B C 1 ATOM 3326 O O . ASN B 1 200 ? 6.695 -63.329 19.050 1.00 13.44 ? 250 ASN B O 1 ATOM 3327 C CB . ASN B 1 200 ? 4.531 -65.028 18.547 1.00 12.44 ? 250 ASN B CB 1 ATOM 3328 C CG . ASN B 1 200 ? 3.845 -66.337 18.234 1.00 19.24 ? 250 ASN B CG 1 ATOM 3329 O OD1 . ASN B 1 200 ? 2.848 -66.697 18.882 1.00 15.68 ? 250 ASN B OD1 1 ATOM 3330 N ND2 . ASN B 1 200 ? 4.311 -67.049 17.195 1.00 12.41 ? 250 ASN B ND2 1 ATOM 3331 N N . LEU B 1 201 ? 6.242 -63.282 21.236 1.00 13.27 ? 251 LEU B N 1 ATOM 3332 C CA . LEU B 1 201 ? 7.027 -62.081 21.533 1.00 11.28 ? 251 LEU B CA 1 ATOM 3333 C C . LEU B 1 201 ? 8.481 -62.472 21.783 1.00 15.40 ? 251 LEU B C 1 ATOM 3334 O O . LEU B 1 201 ? 8.778 -63.418 22.534 1.00 14.58 ? 251 LEU B O 1 ATOM 3335 C CB . LEU B 1 201 ? 6.464 -61.459 22.786 1.00 11.40 ? 251 LEU B CB 1 ATOM 3336 C CG . LEU B 1 201 ? 7.313 -60.350 23.476 1.00 16.16 ? 251 LEU B CG 1 ATOM 3337 C CD1 . LEU B 1 201 ? 7.526 -59.121 22.540 1.00 15.47 ? 251 LEU B CD1 1 ATOM 3338 C CD2 . LEU B 1 201 ? 6.615 -59.914 24.813 1.00 20.03 ? 251 LEU B CD2 1 ATOM 3339 N N . ILE B 1 202 ? 9.372 -61.707 21.149 1.00 11.51 ? 252 ILE B N 1 ATOM 3340 C CA . ILE B 1 202 ? 10.821 -61.800 21.378 1.00 12.32 ? 252 ILE B CA 1 ATOM 3341 C C . ILE B 1 202 ? 11.057 -60.496 22.107 1.00 14.53 ? 252 ILE B C 1 ATOM 3342 O O . ILE B 1 202 ? 11.023 -59.439 21.504 1.00 13.44 ? 252 ILE B O 1 ATOM 3343 C CB . ILE B 1 202 ? 11.641 -61.937 20.066 1.00 15.17 ? 252 ILE B CB 1 ATOM 3344 C CG1 . ILE B 1 202 ? 11.169 -63.198 19.224 1.00 16.09 ? 252 ILE B CG1 1 ATOM 3345 C CG2 . ILE B 1 202 ? 13.139 -62.015 20.429 1.00 16.98 ? 252 ILE B CG2 1 ATOM 3346 C CD1 . ILE B 1 202 ? 11.048 -64.505 19.959 1.00 16.84 ? 252 ILE B CD1 1 ATOM 3347 N N . ALA B 1 203 ? 11.134 -60.569 23.421 1.00 13.33 ? 253 ALA B N 1 ATOM 3348 C CA . ALA B 1 203 ? 11.192 -59.354 24.230 1.00 13.57 ? 253 ALA B CA 1 ATOM 3349 C C . ALA B 1 203 ? 12.602 -58.786 24.348 1.00 17.45 ? 253 ALA B C 1 ATOM 3350 O O . ALA B 1 203 ? 13.560 -59.561 24.482 1.00 16.57 ? 253 ALA B O 1 ATOM 3351 C CB . ALA B 1 203 ? 10.657 -59.659 25.634 1.00 15.96 ? 253 ALA B CB 1 ATOM 3352 N N . PRO B 1 204 ? 12.763 -57.449 24.474 1.00 14.35 ? 254 PRO B N 1 ATOM 3353 C CA . PRO B 1 204 ? 14.104 -56.955 24.802 1.00 13.77 ? 254 PRO B CA 1 ATOM 3354 C C . PRO B 1 204 ? 14.353 -57.159 26.303 1.00 18.05 ? 254 PRO B C 1 ATOM 3355 O O . PRO B 1 204 ? 13.427 -57.108 27.123 1.00 19.09 ? 254 PRO B O 1 ATOM 3356 C CB . PRO B 1 204 ? 14.021 -55.441 24.535 1.00 14.96 ? 254 PRO B CB 1 ATOM 3357 C CG . PRO B 1 204 ? 12.549 -55.090 24.759 1.00 19.01 ? 254 PRO B CG 1 ATOM 3358 C CD . PRO B 1 204 ? 11.759 -56.348 24.387 1.00 16.44 ? 254 PRO B CD 1 ATOM 3359 N N . GLU B 1 205 ? 15.620 -57.293 26.670 1.00 16.51 ? 255 GLU B N 1 ATOM 3360 C CA . GLU B 1 205 ? 16.003 -57.279 28.075 1.00 18.35 ? 255 GLU B CA 1 ATOM 3361 C C . GLU B 1 205 ? 16.585 -55.878 28.342 1.00 20.91 ? 255 GLU B C 1 ATOM 3362 O O . GLU B 1 205 ? 16.528 -55.361 29.460 1.00 20.17 ? 255 GLU B O 1 ATOM 3363 C CB . GLU B 1 205 ? 17.051 -58.354 28.381 1.00 21.08 ? 255 GLU B CB 1 ATOM 3364 C CG . GLU B 1 205 ? 17.436 -58.377 29.850 1.00 29.64 ? 255 GLU B CG 1 ATOM 3365 C CD . GLU B 1 205 ? 18.037 -59.654 30.398 1.00 49.50 ? 255 GLU B CD 1 ATOM 3366 O OE1 . GLU B 1 205 ? 18.618 -60.440 29.614 1.00 35.46 ? 255 GLU B OE1 1 ATOM 3367 O OE2 . GLU B 1 205 ? 17.918 -59.867 31.627 1.00 35.98 ? 255 GLU B OE2 1 ATOM 3368 N N . TYR B 1 206 ? 17.157 -55.280 27.292 1.00 16.36 ? 256 TYR B N 1 ATOM 3369 C CA . TYR B 1 206 ? 17.809 -53.981 27.381 1.00 17.09 ? 256 TYR B CA 1 ATOM 3370 C C . TYR B 1 206 ? 17.195 -52.972 26.452 1.00 20.50 ? 256 TYR B C 1 ATOM 3371 O O . TYR B 1 206 ? 16.544 -53.321 25.448 1.00 20.87 ? 256 TYR B O 1 ATOM 3372 C CB . TYR B 1 206 ? 19.320 -54.095 27.047 1.00 18.38 ? 256 TYR B CB 1 ATOM 3373 C CG . TYR B 1 206 ? 20.091 -55.044 27.943 1.00 23.38 ? 256 TYR B CG 1 ATOM 3374 C CD1 . TYR B 1 206 ? 20.684 -54.595 29.125 1.00 26.54 ? 256 TYR B CD1 1 ATOM 3375 C CD2 . TYR B 1 206 ? 20.270 -56.377 27.587 1.00 25.03 ? 256 TYR B CD2 1 ATOM 3376 C CE1 . TYR B 1 206 ? 21.403 -55.459 29.946 1.00 29.73 ? 256 TYR B CE1 1 ATOM 3377 C CE2 . TYR B 1 206 ? 20.947 -57.263 28.425 1.00 28.37 ? 256 TYR B CE2 1 ATOM 3378 C CZ . TYR B 1 206 ? 21.538 -56.791 29.590 1.00 39.72 ? 256 TYR B CZ 1 ATOM 3379 O OH . TYR B 1 206 ? 22.248 -57.651 30.400 1.00 46.65 ? 256 TYR B OH 1 ATOM 3380 N N . GLY B 1 207 ? 17.407 -51.736 26.821 1.00 18.88 ? 257 GLY B N 1 ATOM 3381 C CA . GLY B 1 207 ? 17.102 -50.546 26.043 1.00 17.65 ? 257 GLY B CA 1 ATOM 3382 C C . GLY B 1 207 ? 18.410 -49.796 25.863 1.00 19.67 ? 257 GLY B C 1 ATOM 3383 O O . GLY B 1 207 ? 19.347 -49.958 26.649 1.00 18.47 ? 257 GLY B O 1 ATOM 3384 N N . PHE B 1 208 ? 18.480 -48.973 24.838 1.00 14.93 ? 258 PHE B N 1 ATOM 3385 C CA . PHE B 1 208 ? 19.701 -48.257 24.554 1.00 13.66 ? 258 PHE B CA 1 ATOM 3386 C C . PHE B 1 208 ? 19.430 -46.791 24.792 1.00 17.65 ? 258 PHE B C 1 ATOM 3387 O O . PHE B 1 208 ? 18.788 -46.154 23.965 1.00 15.50 ? 258 PHE B O 1 ATOM 3388 C CB . PHE B 1 208 ? 20.126 -48.508 23.095 1.00 16.04 ? 258 PHE B CB 1 ATOM 3389 C CG . PHE B 1 208 ? 20.585 -49.921 22.819 1.00 17.63 ? 258 PHE B CG 1 ATOM 3390 C CD1 . PHE B 1 208 ? 21.931 -50.256 22.894 1.00 22.43 ? 258 PHE B CD1 1 ATOM 3391 C CD2 . PHE B 1 208 ? 19.670 -50.916 22.483 1.00 21.76 ? 258 PHE B CD2 1 ATOM 3392 C CE1 . PHE B 1 208 ? 22.360 -51.563 22.622 1.00 24.01 ? 258 PHE B CE1 1 ATOM 3393 C CE2 . PHE B 1 208 ? 20.100 -52.232 22.238 1.00 25.69 ? 258 PHE B CE2 1 ATOM 3394 C CZ . PHE B 1 208 ? 21.440 -52.542 22.334 1.00 23.43 ? 258 PHE B CZ 1 ATOM 3395 N N . LYS B 1 209 ? 19.949 -46.252 25.915 1.00 15.96 ? 259 LYS B N 1 ATOM 3396 C CA . LYS B 1 209 ? 19.762 -44.836 26.211 1.00 16.25 ? 259 LYS B CA 1 ATOM 3397 C C . LYS B 1 209 ? 20.671 -44.047 25.295 1.00 19.40 ? 259 LYS B C 1 ATOM 3398 O O . LYS B 1 209 ? 21.851 -44.386 25.179 1.00 19.48 ? 259 LYS B O 1 ATOM 3399 C CB . LYS B 1 209 ? 20.062 -44.547 27.685 1.00 19.50 ? 259 LYS B CB 1 ATOM 3400 C CG . LYS B 1 209 ? 20.137 -43.059 28.021 1.00 23.58 ? 259 LYS B CG 1 ATOM 3401 C CD . LYS B 1 209 ? 20.559 -42.887 29.483 1.00 31.33 ? 259 LYS B CD 1 ATOM 3402 C CE . LYS B 1 209 ? 21.203 -41.548 29.721 1.00 52.84 ? 259 LYS B CE 1 ATOM 3403 N NZ . LYS B 1 209 ? 21.560 -41.353 31.155 1.00 65.74 ? 259 LYS B NZ 1 ATOM 3404 N N . ILE B 1 210 ? 20.130 -43.035 24.622 1.00 16.85 ? 260 ILE B N 1 ATOM 3405 C CA . ILE B 1 210 ? 20.937 -42.155 23.763 1.00 18.10 ? 260 ILE B CA 1 ATOM 3406 C C . ILE B 1 210 ? 21.754 -41.223 24.694 1.00 23.81 ? 260 ILE B C 1 ATOM 3407 O O . ILE B 1 210 ? 21.215 -40.281 25.268 1.00 24.34 ? 260 ILE B O 1 ATOM 3408 C CB . ILE B 1 210 ? 20.059 -41.452 22.685 1.00 21.34 ? 260 ILE B CB 1 ATOM 3409 C CG1 . ILE B 1 210 ? 19.419 -42.536 21.782 1.00 21.65 ? 260 ILE B CG1 1 ATOM 3410 C CG2 . ILE B 1 210 ? 20.900 -40.436 21.860 1.00 23.62 ? 260 ILE B CG2 1 ATOM 3411 C CD1 . ILE B 1 210 ? 18.314 -42.095 20.910 1.00 29.18 ? 260 ILE B CD1 1 ATOM 3412 N N . SER B 1 211 ? 23.024 -41.540 24.902 1.00 21.10 ? 261 SER B N 1 ATOM 3413 C CA . SER B 1 211 ? 23.866 -40.803 25.870 1.00 22.21 ? 261 SER B CA 1 ATOM 3414 C C . SER B 1 211 ? 24.631 -39.628 25.314 1.00 25.22 ? 261 SER B C 1 ATOM 3415 O O . SER B 1 211 ? 25.016 -38.728 26.056 1.00 28.20 ? 261 SER B O 1 ATOM 3416 C CB . SER B 1 211 ? 24.811 -41.759 26.595 1.00 27.71 ? 261 SER B CB 1 ATOM 3417 O OG . SER B 1 211 ? 25.312 -42.758 25.722 1.00 35.42 ? 261 SER B OG 1 ATOM 3418 N N . LYS B 1 212 ? 24.888 -39.637 24.023 1.00 18.95 ? 262 LYS B N 1 ATOM 3419 C CA . LYS B 1 212 ? 25.577 -38.560 23.351 1.00 19.11 ? 262 LYS B CA 1 ATOM 3420 C C . LYS B 1 212 ? 24.975 -38.440 21.981 1.00 22.54 ? 262 LYS B C 1 ATOM 3421 O O . LYS B 1 212 ? 24.730 -39.448 21.316 1.00 21.17 ? 262 LYS B O 1 ATOM 3422 C CB . LYS B 1 212 ? 27.092 -38.828 23.286 1.00 22.31 ? 262 LYS B CB 1 ATOM 3423 C CG . LYS B 1 212 ? 27.949 -37.608 22.902 1.00 43.74 ? 262 LYS B CG 1 ATOM 3424 C CD . LYS B 1 212 ? 28.483 -36.888 24.142 1.00 61.09 ? 262 LYS B CD 1 ATOM 3425 C CE . LYS B 1 212 ? 29.434 -35.766 23.797 1.00 79.20 ? 262 LYS B CE 1 ATOM 3426 N NZ . LYS B 1 212 ? 29.841 -34.999 25.006 1.00 89.36 ? 262 LYS B NZ 1 ATOM 3427 N N . ARG B 1 213 ? 24.744 -37.193 21.561 1.00 23.22 ? 263 ARG B N 1 ATOM 3428 C CA . ARG B 1 213 ? 24.179 -36.847 20.261 1.00 22.89 ? 263 ARG B CA 1 ATOM 3429 C C . ARG B 1 213 ? 25.214 -36.026 19.503 1.00 28.71 ? 263 ARG B C 1 ATOM 3430 O O . ARG B 1 213 ? 26.028 -35.335 20.124 1.00 28.02 ? 263 ARG B O 1 ATOM 3431 C CB . ARG B 1 213 ? 22.897 -36.036 20.446 1.00 22.57 ? 263 ARG B CB 1 ATOM 3432 C CG . ARG B 1 213 ? 21.759 -36.826 21.080 1.00 25.18 ? 263 ARG B CG 1 ATOM 3433 C CD . ARG B 1 213 ? 20.539 -35.939 21.278 1.00 34.72 ? 263 ARG B CD 1 ATOM 3434 N NE . ARG B 1 213 ? 19.483 -36.631 22.019 1.00 36.17 ? 263 ARG B NE 1 ATOM 3435 C CZ . ARG B 1 213 ? 18.515 -37.350 21.462 1.00 44.76 ? 263 ARG B CZ 1 ATOM 3436 N NH1 . ARG B 1 213 ? 18.454 -37.487 20.143 1.00 30.63 ? 263 ARG B NH1 1 ATOM 3437 N NH2 . ARG B 1 213 ? 17.603 -37.948 22.221 1.00 25.51 ? 263 ARG B NH2 1 ATOM 3438 N N . GLY B 1 214 A 25.169 -36.091 18.178 1.00 27.37 ? 263 GLY B N 1 ATOM 3439 C CA . GLY B 1 214 A 26.080 -35.326 17.339 1.00 29.49 ? 263 GLY B CA 1 ATOM 3440 C C . GLY B 1 214 A 26.027 -35.748 15.892 1.00 37.56 ? 263 GLY B C 1 ATOM 3441 O O . GLY B 1 214 A 25.603 -36.864 15.582 1.00 35.81 ? 263 GLY B O 1 ATOM 3442 N N . SER B 1 215 ? 26.512 -34.881 15.012 1.00 39.27 ? 264 SER B N 1 ATOM 3443 C CA . SER B 1 215 ? 26.529 -35.125 13.569 1.00 41.11 ? 264 SER B CA 1 ATOM 3444 C C . SER B 1 215 ? 27.784 -35.860 13.090 1.00 45.64 ? 264 SER B C 1 ATOM 3445 O O . SER B 1 215 ? 28.867 -35.647 13.633 1.00 44.01 ? 264 SER B O 1 ATOM 3446 C CB . SER B 1 215 ? 26.356 -33.814 12.806 1.00 47.11 ? 264 SER B CB 1 ATOM 3447 O OG . SER B 1 215 ? 26.022 -34.077 11.453 1.00 59.85 ? 264 SER B OG 1 ATOM 3448 N N . SER B 1 216 ? 27.600 -36.695 12.035 1.00 44.85 ? 265 SER B N 1 ATOM 3449 C CA . SER B 1 216 ? 28.500 -37.584 11.268 1.00 46.76 ? 265 SER B CA 1 ATOM 3450 C C . SER B 1 216 ? 28.303 -39.061 11.664 1.00 55.35 ? 265 SER B C 1 ATOM 3451 O O . SER B 1 216 ? 28.874 -39.517 12.648 1.00 56.19 ? 265 SER B O 1 ATOM 3452 C CB . SER B 1 216 ? 29.962 -37.138 11.312 1.00 49.30 ? 265 SER B CB 1 ATOM 3453 O OG . SER B 1 216 ? 30.129 -35.878 10.681 1.00 52.34 ? 265 SER B OG 1 ATOM 3454 N N . GLY B 1 217 ? 27.479 -39.784 10.908 1.00 53.95 ? 266 GLY B N 1 ATOM 3455 C CA . GLY B 1 217 ? 27.154 -41.173 11.218 1.00 53.88 ? 266 GLY B CA 1 ATOM 3456 C C . GLY B 1 217 ? 27.632 -42.263 10.296 1.00 59.75 ? 266 GLY B C 1 ATOM 3457 O O . GLY B 1 217 ? 28.756 -42.205 9.802 1.00 61.73 ? 266 GLY B O 1 ATOM 3458 N N . ILE B 1 218 ? 26.763 -43.271 10.074 1.00 56.39 ? 267 ILE B N 1 ATOM 3459 C CA . ILE B 1 218 ? 26.998 -44.498 9.295 1.00 56.21 ? 267 ILE B CA 1 ATOM 3460 C C . ILE B 1 218 ? 27.707 -44.345 7.937 1.00 60.54 ? 267 ILE B C 1 ATOM 3461 O O . ILE B 1 218 ? 27.161 -43.751 7.012 1.00 60.04 ? 267 ILE B O 1 ATOM 3462 C CB . ILE B 1 218 ? 25.769 -45.468 9.277 1.00 59.26 ? 267 ILE B CB 1 ATOM 3463 C CG1 . ILE B 1 218 ? 25.291 -45.775 10.721 1.00 59.04 ? 267 ILE B CG1 1 ATOM 3464 C CG2 . ILE B 1 218 ? 26.076 -46.782 8.505 1.00 60.30 ? 267 ILE B CG2 1 ATOM 3465 C CD1 . ILE B 1 218 ? 24.007 -46.540 10.843 1.00 60.23 ? 267 ILE B CD1 1 ATOM 3466 N N . MET B 1 219 ? 28.910 -44.933 7.829 1.00 57.42 ? 268 MET B N 1 ATOM 3467 C CA . MET B 1 219 ? 29.743 -44.949 6.626 1.00 85.23 ? 268 MET B CA 1 ATOM 3468 C C . MET B 1 219 ? 29.735 -46.322 5.962 1.00 110.61 ? 268 MET B C 1 ATOM 3469 O O . MET B 1 219 ? 30.013 -47.325 6.615 1.00 71.91 ? 268 MET B O 1 ATOM 3470 C CB . MET B 1 219 ? 31.185 -44.515 6.944 1.00 87.97 ? 268 MET B CB 1 ATOM 3471 C CG . MET B 1 219 ? 31.293 -43.146 7.598 1.00 92.03 ? 268 MET B CG 1 ATOM 3472 S SD . MET B 1 219 ? 30.250 -41.858 6.870 1.00 97.04 ? 268 MET B SD 1 ATOM 3473 C CE . MET B 1 219 ? 30.939 -41.763 5.245 1.00 94.64 ? 268 MET B CE 1 HETATM 3474 C C1 . NAG C 2 . ? 6.977 -40.321 -21.046 1.00 32.99 ? 5467 NAG A C1 1 HETATM 3475 C C2 . NAG C 2 . ? 5.515 -40.582 -21.570 1.00 34.89 ? 5467 NAG A C2 1 HETATM 3476 C C3 . NAG C 2 . ? 5.241 -42.091 -21.758 1.00 36.46 ? 5467 NAG A C3 1 HETATM 3477 C C4 . NAG C 2 . ? 6.400 -42.785 -22.519 1.00 37.21 ? 5467 NAG A C4 1 HETATM 3478 C C5 . NAG C 2 . ? 7.825 -42.400 -22.022 1.00 36.48 ? 5467 NAG A C5 1 HETATM 3479 C C6 . NAG C 2 . ? 8.845 -42.697 -23.160 1.00 38.02 ? 5467 NAG A C6 1 HETATM 3480 C C7 . NAG C 2 . ? 3.501 -39.149 -21.407 1.00 37.22 ? 5467 NAG A C7 1 HETATM 3481 C C8 . NAG C 2 . ? 2.571 -38.453 -20.425 1.00 37.98 ? 5467 NAG A C8 1 HETATM 3482 N N2 . NAG C 2 . ? 4.509 -39.867 -20.795 1.00 35.75 ? 5467 NAG A N2 1 HETATM 3483 O O3 . NAG C 2 . ? 4.034 -42.093 -22.561 1.00 38.74 ? 5467 NAG A O3 1 HETATM 3484 O O4 . NAG C 2 . ? 6.258 -44.215 -22.398 1.00 39.99 ? 5467 NAG A O4 1 HETATM 3485 O O5 . NAG C 2 . ? 7.934 -40.925 -21.881 1.00 34.59 ? 5467 NAG A O5 1 HETATM 3486 O O6 . NAG C 2 . ? 9.184 -44.084 -23.098 1.00 41.83 ? 5467 NAG A O6 1 HETATM 3487 O O7 . NAG C 2 . ? 3.391 -39.089 -22.634 1.00 39.22 ? 5467 NAG A O7 1 HETATM 3488 N N1 . EPE D 3 . ? 13.104 -8.345 -7.976 1.00 33.89 ? 3380 EPE A N1 1 HETATM 3489 C C2 . EPE D 3 . ? 12.858 -9.670 -8.618 1.00 33.69 ? 3380 EPE A C2 1 HETATM 3490 C C3 . EPE D 3 . ? 12.392 -9.454 -10.078 1.00 33.53 ? 3380 EPE A C3 1 HETATM 3491 N N4 . EPE D 3 . ? 13.323 -8.557 -10.843 1.00 33.57 ? 3380 EPE A N4 1 HETATM 3492 C C5 . EPE D 3 . ? 13.391 -7.230 -10.181 1.00 34.51 ? 3380 EPE A C5 1 HETATM 3493 C C6 . EPE D 3 . ? 14.027 -7.471 -8.785 1.00 34.52 ? 3380 EPE A C6 1 HETATM 3494 C C7 . EPE D 3 . ? 12.819 -8.461 -12.210 1.00 34.77 ? 3380 EPE A C7 1 HETATM 3495 C C8 . EPE D 3 . ? 13.955 -8.024 -13.102 1.00 35.64 ? 3380 EPE A C8 1 HETATM 3496 O O8 . EPE D 3 . ? 14.744 -9.149 -13.357 1.00 38.29 ? 3380 EPE A O8 1 HETATM 3497 C C9 . EPE D 3 . ? 13.788 -8.667 -6.723 1.00 34.69 ? 3380 EPE A C9 1 HETATM 3498 C C10 . EPE D 3 . ? 13.776 -7.461 -5.822 1.00 34.21 ? 3380 EPE A C10 1 HETATM 3499 S S . EPE D 3 . ? 14.287 -8.077 -4.192 1.00 38.32 ? 3380 EPE A S 1 HETATM 3500 O O1S . EPE D 3 . ? 13.162 -8.652 -3.527 1.00 39.92 ? 3380 EPE A O1S 1 HETATM 3501 O O2S . EPE D 3 . ? 15.585 -8.600 -4.161 1.00 41.59 ? 3380 EPE A O2S 1 HETATM 3502 O O3S . EPE D 3 . ? 14.513 -6.732 -3.479 1.00 41.23 ? 3380 EPE A O3S 1 HETATM 3503 C C1 . NAG E 2 . ? 7.020 -42.244 35.014 1.00 26.57 ? 5467 NAG B C1 1 HETATM 3504 C C2 . NAG E 2 . ? 5.543 -41.975 35.439 1.00 28.61 ? 5467 NAG B C2 1 HETATM 3505 C C3 . NAG E 2 . ? 5.280 -40.449 35.493 1.00 30.21 ? 5467 NAG B C3 1 HETATM 3506 C C4 . NAG E 2 . ? 6.361 -39.696 36.298 1.00 30.82 ? 5467 NAG B C4 1 HETATM 3507 C C5 . NAG E 2 . ? 7.789 -40.133 35.753 1.00 29.95 ? 5467 NAG B C5 1 HETATM 3508 C C6 . NAG E 2 . ? 8.953 -39.495 36.515 1.00 31.34 ? 5467 NAG B C6 1 HETATM 3509 C C7 . NAG E 2 . ? 3.524 -43.361 35.051 1.00 31.58 ? 5467 NAG B C7 1 HETATM 3510 C C8 . NAG E 2 . ? 2.658 -43.953 33.988 1.00 32.41 ? 5467 NAG B C8 1 HETATM 3511 N N2 . NAG E 2 . ? 4.585 -42.611 34.564 1.00 29.81 ? 5467 NAG B N2 1 HETATM 3512 O O3 . NAG E 2 . ? 4.007 -40.298 36.141 1.00 32.33 ? 5467 NAG B O3 1 HETATM 3513 O O4 . NAG E 2 . ? 6.043 -38.321 35.985 1.00 33.62 ? 5467 NAG B O4 1 HETATM 3514 O O5 . NAG E 2 . ? 7.964 -41.593 35.856 1.00 28.06 ? 5467 NAG B O5 1 HETATM 3515 O O6 . NAG E 2 . ? 8.833 -39.910 37.864 1.00 34.79 ? 5467 NAG B O6 1 HETATM 3516 O O7 . NAG E 2 . ? 3.362 -43.528 36.274 1.00 33.80 ? 5467 NAG B O7 1 HETATM 3517 N N1 . EPE F 3 . ? 13.358 -74.157 20.980 1.00 30.67 ? 3380 EPE B N1 1 HETATM 3518 C C2 . EPE F 3 . ? 13.094 -72.828 21.616 1.00 30.54 ? 3380 EPE B C2 1 HETATM 3519 C C3 . EPE F 3 . ? 12.603 -73.017 23.050 1.00 30.10 ? 3380 EPE B C3 1 HETATM 3520 N N4 . EPE F 3 . ? 13.631 -73.759 23.826 1.00 30.32 ? 3380 EPE B N4 1 HETATM 3521 C C5 . EPE F 3 . ? 13.911 -75.110 23.212 1.00 31.28 ? 3380 EPE B C5 1 HETATM 3522 C C6 . EPE F 3 . ? 14.423 -74.882 21.764 1.00 31.30 ? 3380 EPE B C6 1 HETATM 3523 C C7 . EPE F 3 . ? 13.085 -73.897 25.219 1.00 31.19 ? 3380 EPE B C7 1 HETATM 3524 C C8 . EPE F 3 . ? 14.114 -74.436 26.217 1.00 31.96 ? 3380 EPE B C8 1 HETATM 3525 O O8 . EPE F 3 . ? 15.390 -73.823 26.217 1.00 34.26 ? 3380 EPE B O8 1 HETATM 3526 C C9 . EPE F 3 . ? 13.913 -73.697 19.703 1.00 31.43 ? 3380 EPE B C9 1 HETATM 3527 C C10 . EPE F 3 . ? 14.231 -74.843 18.773 1.00 31.14 ? 3380 EPE B C10 1 HETATM 3528 S S . EPE F 3 . ? 14.425 -74.058 17.140 1.00 35.46 ? 3380 EPE B S 1 HETATM 3529 O O1S . EPE F 3 . ? 13.153 -73.670 16.653 1.00 37.00 ? 3380 EPE B O1S 1 HETATM 3530 O O2S . EPE F 3 . ? 15.512 -73.154 17.065 1.00 39.66 ? 3380 EPE B O2S 1 HETATM 3531 O O3S . EPE F 3 . ? 14.727 -75.293 16.310 1.00 38.52 ? 3380 EPE B O3S 1 HETATM 3532 O O . HOH G 4 . ? 26.492 -22.470 -7.578 1.00 22.99 ? 1 HOH A O 1 HETATM 3533 O O . HOH G 4 . ? 25.416 -17.544 1.152 1.00 21.84 ? 6 HOH A O 1 HETATM 3534 O O . HOH G 4 . ? 34.550 -36.814 -5.634 1.00 20.70 ? 8 HOH A O 1 HETATM 3535 O O . HOH G 4 . ? 29.618 -27.990 4.651 1.00 25.28 ? 9 HOH A O 1 HETATM 3536 O O . HOH G 4 . ? 17.755 -27.459 -7.834 1.00 19.66 ? 10 HOH A O 1 HETATM 3537 O O . HOH G 4 . ? 26.582 -30.042 -8.851 1.00 22.99 ? 11 HOH A O 1 HETATM 3538 O O . HOH G 4 . ? 3.957 -11.004 10.319 1.00 20.37 ? 14 HOH A O 1 HETATM 3539 O O . HOH G 4 . ? -1.339 -15.583 -0.808 1.00 22.55 ? 15 HOH A O 1 HETATM 3540 O O . HOH G 4 . ? 16.113 -29.304 -9.106 1.00 18.43 ? 16 HOH A O 1 HETATM 3541 O O . HOH G 4 . ? 10.244 -20.461 4.555 1.00 28.48 ? 18 HOH A O 1 HETATM 3542 O O . HOH G 4 . ? 22.977 -13.996 1.332 1.00 27.20 ? 19 HOH A O 1 HETATM 3543 O O . HOH G 4 . ? 32.604 -34.950 -6.191 1.00 25.45 ? 20 HOH A O 1 HETATM 3544 O O . HOH G 4 . ? 4.900 -39.813 -18.063 1.00 24.12 ? 21 HOH A O 1 HETATM 3545 O O . HOH G 4 . ? 15.842 -15.862 -11.998 1.00 17.64 ? 23 HOH A O 1 HETATM 3546 O O . HOH G 4 . ? 12.209 -12.673 -12.940 1.00 20.05 ? 25 HOH A O 1 HETATM 3547 O O . HOH G 4 . ? 24.864 -27.332 -8.597 1.00 29.65 ? 28 HOH A O 1 HETATM 3548 O O . HOH G 4 . ? 29.689 -16.640 2.023 1.00 29.80 ? 29 HOH A O 1 HETATM 3549 O O . HOH G 4 . ? 10.142 -31.618 0.270 1.00 22.21 ? 30 HOH A O 1 HETATM 3550 O O . HOH G 4 . ? -0.936 -14.481 -3.383 1.00 21.77 ? 31 HOH A O 1 HETATM 3551 O O . HOH G 4 . ? 6.770 -17.091 -9.936 1.00 18.60 ? 32 HOH A O 1 HETATM 3552 O O . HOH G 4 . ? 14.016 -42.684 -17.800 1.00 29.94 ? 34 HOH A O 1 HETATM 3553 O O . HOH G 4 . ? 31.626 -44.039 -5.163 1.00 25.48 ? 36 HOH A O 1 HETATM 3554 O O . HOH G 4 . ? 21.021 -25.145 4.190 1.00 35.89 ? 44 HOH A O 1 HETATM 3555 O O . HOH G 4 . ? 21.951 -14.827 7.559 1.00 24.96 ? 45 HOH A O 1 HETATM 3556 O O . HOH G 4 . ? 32.014 -18.430 -10.295 1.00 27.99 ? 47 HOH A O 1 HETATM 3557 O O . HOH G 4 . ? 27.017 -40.164 -0.570 1.00 19.59 ? 48 HOH A O 1 HETATM 3558 O O . HOH G 4 . ? 17.211 -19.025 5.585 1.00 24.85 ? 49 HOH A O 1 HETATM 3559 O O . HOH G 4 . ? 30.745 -23.053 6.782 1.00 33.89 ? 50 HOH A O 1 HETATM 3560 O O . HOH G 4 . ? 20.261 -18.216 -11.612 1.00 31.13 ? 53 HOH A O 1 HETATM 3561 O O . HOH G 4 . ? 25.072 -15.901 -2.306 1.00 26.81 ? 54 HOH A O 1 HETATM 3562 O O . HOH G 4 . ? 18.836 -21.059 -13.786 1.00 30.84 ? 124 HOH A O 1 HETATM 3563 O O . HOH G 4 . ? 27.913 -14.215 1.016 1.00 26.82 ? 269 HOH A O 1 HETATM 3564 O O . HOH G 4 . ? 32.460 -17.087 0.779 1.00 26.03 ? 270 HOH A O 1 HETATM 3565 O O . HOH G 4 . ? 32.566 -21.542 -4.851 1.00 26.04 ? 271 HOH A O 1 HETATM 3566 O O . HOH G 4 . ? -0.934 -36.668 -8.737 1.00 46.26 ? 272 HOH A O 1 HETATM 3567 O O . HOH G 4 . ? 0.918 -6.650 3.387 1.00 23.72 ? 273 HOH A O 1 HETATM 3568 O O . HOH G 4 . ? 32.626 -19.400 -1.676 1.00 37.60 ? 274 HOH A O 1 HETATM 3569 O O . HOH G 4 . ? -4.543 -32.538 -12.264 1.00 41.56 ? 275 HOH A O 1 HETATM 3570 O O . HOH G 4 . ? 33.551 -20.190 4.580 1.00 52.62 ? 276 HOH A O 1 HETATM 3571 O O . HOH G 4 . ? 5.704 -25.604 -0.640 1.00 46.52 ? 277 HOH A O 1 HETATM 3572 O O . HOH G 4 . ? 22.445 -17.080 -11.191 1.00 39.96 ? 278 HOH A O 1 HETATM 3573 O O . HOH G 4 . ? 21.066 -19.658 -13.627 1.00 48.21 ? 279 HOH A O 1 HETATM 3574 O O . HOH G 4 . ? 32.038 -34.076 7.276 1.00 59.68 ? 280 HOH A O 1 HETATM 3575 O O . HOH G 4 . ? 1.860 -35.220 -2.226 1.00 23.39 ? 281 HOH A O 1 HETATM 3576 O O . HOH G 4 . ? 2.967 -37.481 -1.315 1.00 42.68 ? 282 HOH A O 1 HETATM 3577 O O . HOH G 4 . ? 12.949 -12.955 -19.120 1.00 30.94 ? 283 HOH A O 1 HETATM 3578 O O . HOH G 4 . ? 29.337 -15.076 -5.056 1.00 45.17 ? 284 HOH A O 1 HETATM 3579 O O . HOH G 4 . ? 4.005 -26.504 -4.278 1.00 26.66 ? 285 HOH A O 1 HETATM 3580 O O . HOH G 4 . ? 12.366 -44.972 -11.306 1.00 36.78 ? 286 HOH A O 1 HETATM 3581 O O . HOH G 4 . ? 9.386 -25.267 5.563 1.00 39.05 ? 287 HOH A O 1 HETATM 3582 O O . HOH G 4 . ? -3.317 -16.777 -17.598 1.00 35.25 ? 288 HOH A O 1 HETATM 3583 O O . HOH G 4 . ? 6.725 -44.158 -14.438 1.00 33.09 ? 289 HOH A O 1 HETATM 3584 O O . HOH G 4 . ? 9.161 -8.668 -13.450 1.00 21.98 ? 290 HOH A O 1 HETATM 3585 O O . HOH G 4 . ? 27.031 -14.813 -3.814 1.00 27.68 ? 291 HOH A O 1 HETATM 3586 O O . HOH G 4 . ? -2.296 -24.724 -0.205 1.00 57.18 ? 292 HOH A O 1 HETATM 3587 O O . HOH G 4 . ? -0.827 -29.642 -1.164 1.00 31.11 ? 293 HOH A O 1 HETATM 3588 O O . HOH G 4 . ? -2.824 -11.450 1.513 1.00 24.40 ? 294 HOH A O 1 HETATM 3589 O O . HOH G 4 . ? 23.713 -18.627 3.016 1.00 26.93 ? 295 HOH A O 1 HETATM 3590 O O . HOH G 4 . ? 6.127 -33.195 -20.935 1.00 39.81 ? 296 HOH A O 1 HETATM 3591 O O . HOH G 4 . ? 18.055 -17.147 -12.366 1.00 31.16 ? 297 HOH A O 1 HETATM 3592 O O . HOH G 4 . ? 27.291 -32.139 -10.590 1.00 38.78 ? 298 HOH A O 1 HETATM 3593 O O . HOH G 4 . ? 37.796 -34.700 -1.388 1.00 29.48 ? 299 HOH A O 1 HETATM 3594 O O . HOH G 4 . ? 36.919 -41.755 0.641 1.00 45.91 ? 300 HOH A O 1 HETATM 3595 O O . HOH G 4 . ? 25.717 -17.841 6.800 1.00 29.77 ? 301 HOH A O 1 HETATM 3596 O O . HOH G 4 . ? 13.908 -32.363 7.990 1.00 27.51 ? 302 HOH A O 1 HETATM 3597 O O . HOH G 4 . ? 30.181 -25.927 11.270 1.00 37.75 ? 303 HOH A O 1 HETATM 3598 O O . HOH G 4 . ? 14.214 -8.272 -17.097 1.00 36.81 ? 304 HOH A O 1 HETATM 3599 O O . HOH G 4 . ? 12.847 -23.352 -15.562 1.00 20.59 ? 305 HOH A O 1 HETATM 3600 O O . HOH G 4 . ? 8.475 -8.493 12.222 1.00 30.83 ? 306 HOH A O 1 HETATM 3601 O O . HOH G 4 . ? 13.558 -46.648 -10.025 1.00 62.91 ? 307 HOH A O 1 HETATM 3602 O O . HOH G 4 . ? -4.715 -18.023 -8.409 1.00 25.91 ? 308 HOH A O 1 HETATM 3603 O O . HOH G 4 . ? 25.799 -39.717 8.639 1.00 41.32 ? 309 HOH A O 1 HETATM 3604 O O . HOH G 4 . ? 5.749 -18.360 -19.862 1.00 29.23 ? 310 HOH A O 1 HETATM 3605 O O . HOH G 4 . ? 19.502 -23.206 -22.181 1.00 39.77 ? 311 HOH A O 1 HETATM 3606 O O . HOH G 4 . ? 15.583 -36.610 -20.350 1.00 27.87 ? 312 HOH A O 1 HETATM 3607 O O . HOH G 4 . ? 27.336 -34.949 -9.788 1.00 26.88 ? 313 HOH A O 1 HETATM 3608 O O . HOH G 4 . ? 16.518 -11.221 11.602 1.00 23.42 ? 314 HOH A O 1 HETATM 3609 O O . HOH G 4 . ? 26.493 -25.416 -7.055 1.00 32.11 ? 315 HOH A O 1 HETATM 3610 O O . HOH G 4 . ? 23.091 -30.190 -18.671 1.00 38.16 ? 316 HOH A O 1 HETATM 3611 O O . HOH G 4 . ? 0.196 -23.820 1.303 1.00 34.13 ? 317 HOH A O 1 HETATM 3612 O O . HOH G 4 . ? 0.565 -29.466 -11.320 1.00 32.71 ? 318 HOH A O 1 HETATM 3613 O O . HOH G 4 . ? 18.324 -8.043 9.874 1.00 25.24 ? 319 HOH A O 1 HETATM 3614 O O . HOH G 4 . ? -0.549 -30.838 -8.358 1.00 37.03 ? 320 HOH A O 1 HETATM 3615 O O . HOH G 4 . ? 10.202 -14.963 -25.155 1.00 39.21 ? 321 HOH A O 1 HETATM 3616 O O . HOH G 4 . ? -1.744 -10.769 -14.123 1.00 29.89 ? 322 HOH A O 1 HETATM 3617 O O . HOH G 4 . ? 23.625 -24.102 -13.203 1.00 31.92 ? 323 HOH A O 1 HETATM 3618 O O . HOH G 4 . ? 8.718 -33.801 -21.262 1.00 30.68 ? 324 HOH A O 1 HETATM 3619 O O . HOH G 4 . ? -0.962 -34.095 -8.651 1.00 36.86 ? 325 HOH A O 1 HETATM 3620 O O . HOH G 4 . ? 32.537 -36.808 -13.737 1.00 44.97 ? 326 HOH A O 1 HETATM 3621 O O . HOH G 4 . ? -2.897 -28.087 -11.394 1.00 36.41 ? 327 HOH A O 1 HETATM 3622 O O . HOH G 4 . ? 19.558 -18.018 5.273 1.00 35.33 ? 328 HOH A O 1 HETATM 3623 O O . HOH G 4 . ? 10.468 -29.712 -20.218 1.00 26.02 ? 329 HOH A O 1 HETATM 3624 O O . HOH G 4 . ? 17.694 -7.131 -4.191 1.00 34.25 ? 330 HOH A O 1 HETATM 3625 O O . HOH G 4 . ? 2.098 -5.328 5.751 1.00 45.31 ? 331 HOH A O 1 HETATM 3626 O O . HOH G 4 . ? 11.673 -23.231 -25.640 1.00 65.58 ? 332 HOH A O 1 HETATM 3627 O O . HOH G 4 . ? -1.776 -17.318 2.641 1.00 25.40 ? 333 HOH A O 1 HETATM 3628 O O . HOH G 4 . ? 27.549 -15.009 -12.209 1.00 30.05 ? 334 HOH A O 1 HETATM 3629 O O . HOH G 4 . ? 9.561 -38.355 -3.907 1.00 36.29 ? 335 HOH A O 1 HETATM 3630 O O . HOH G 4 . ? 24.957 -33.837 6.843 1.00 64.13 ? 336 HOH A O 1 HETATM 3631 O O . HOH G 4 . ? 27.464 -20.684 10.083 1.00 46.90 ? 337 HOH A O 1 HETATM 3632 O O . HOH G 4 . ? 19.261 -13.261 -11.467 1.00 29.80 ? 338 HOH A O 1 HETATM 3633 O O . HOH G 4 . ? 3.049 -11.699 -19.782 1.00 30.85 ? 339 HOH A O 1 HETATM 3634 O O . HOH G 4 . ? 19.212 -8.397 0.177 1.00 30.19 ? 340 HOH A O 1 HETATM 3635 O O . HOH G 4 . ? 10.587 -6.568 -14.495 1.00 32.66 ? 341 HOH A O 1 HETATM 3636 O O . HOH G 4 . ? 14.540 -6.542 10.373 1.00 29.63 ? 342 HOH A O 1 HETATM 3637 O O . HOH G 4 . ? 25.420 -15.205 0.254 1.00 25.98 ? 343 HOH A O 1 HETATM 3638 O O . HOH G 4 . ? 11.530 -4.743 -12.430 1.00 38.09 ? 344 HOH A O 1 HETATM 3639 O O . HOH G 4 . ? 11.841 -7.315 2.518 1.00 31.28 ? 345 HOH A O 1 HETATM 3640 O O . HOH G 4 . ? 30.468 -34.846 -13.672 1.00 30.51 ? 346 HOH A O 1 HETATM 3641 O O . HOH G 4 . ? -2.268 -12.036 -11.862 1.00 31.26 ? 347 HOH A O 1 HETATM 3642 O O . HOH G 4 . ? -1.686 -15.745 -12.979 1.00 45.00 ? 348 HOH A O 1 HETATM 3643 O O . HOH G 4 . ? 28.651 -8.304 -4.046 1.00 43.13 ? 349 HOH A O 1 HETATM 3644 O O . HOH G 4 . ? 10.446 -8.254 -18.487 1.00 35.62 ? 350 HOH A O 1 HETATM 3645 O O . HOH G 4 . ? 32.121 -26.814 -10.788 1.00 40.07 ? 351 HOH A O 1 HETATM 3646 O O . HOH G 4 . ? 7.518 -37.656 -7.578 1.00 27.24 ? 352 HOH A O 1 HETATM 3647 O O . HOH G 4 . ? 18.423 -36.496 -20.283 1.00 32.64 ? 353 HOH A O 1 HETATM 3648 O O . HOH G 4 . ? 11.955 -30.307 -25.196 1.00 37.63 ? 354 HOH A O 1 HETATM 3649 O O . HOH G 4 . ? 7.548 -40.219 -9.796 1.00 27.67 ? 355 HOH A O 1 HETATM 3650 O O . HOH G 4 . ? 36.714 -27.944 3.845 1.00 40.55 ? 356 HOH A O 1 HETATM 3651 O O . HOH G 4 . ? 7.781 -24.465 -19.426 1.00 37.28 ? 357 HOH A O 1 HETATM 3652 O O . HOH G 4 . ? 5.099 -22.727 5.170 1.00 47.91 ? 358 HOH A O 1 HETATM 3653 O O . HOH G 4 . ? 8.459 -7.294 -10.945 1.00 29.46 ? 359 HOH A O 1 HETATM 3654 O O . HOH G 4 . ? 7.213 -3.965 -0.674 1.00 39.85 ? 360 HOH A O 1 HETATM 3655 O O . HOH G 4 . ? 11.866 -9.781 0.773 1.00 37.60 ? 361 HOH A O 1 HETATM 3656 O O . HOH G 4 . ? 31.830 -18.898 3.017 1.00 29.74 ? 362 HOH A O 1 HETATM 3657 O O . HOH G 4 . ? 31.543 -13.423 -2.468 1.00 42.98 ? 363 HOH A O 1 HETATM 3658 O O . HOH G 4 . ? 1.540 -3.483 1.436 1.00 43.54 ? 364 HOH A O 1 HETATM 3659 O O . HOH G 4 . ? 1.565 -43.714 -8.245 1.00 33.44 ? 365 HOH A O 1 HETATM 3660 O O . HOH G 4 . ? 4.833 -35.715 -20.500 1.00 36.95 ? 366 HOH A O 1 HETATM 3661 O O . HOH G 4 . ? 31.581 -32.236 10.198 1.00 50.90 ? 367 HOH A O 1 HETATM 3662 O O . HOH G 4 . ? 10.907 -14.887 -20.749 1.00 32.41 ? 368 HOH A O 1 HETATM 3663 O O . HOH G 4 . ? 18.606 -5.943 7.731 1.00 47.70 ? 369 HOH A O 1 HETATM 3664 O O . HOH G 4 . ? 35.391 -39.368 -9.047 1.00 33.74 ? 370 HOH A O 1 HETATM 3665 O O . HOH G 4 . ? 25.064 -47.394 -9.681 1.00 42.09 ? 371 HOH A O 1 HETATM 3666 O O . HOH G 4 . ? 11.148 -17.176 8.694 1.00 37.30 ? 372 HOH A O 1 HETATM 3667 O O . HOH G 4 . ? 20.449 -29.333 8.734 1.00 41.10 ? 373 HOH A O 1 HETATM 3668 O O . HOH G 4 . ? 20.693 -22.173 4.800 1.00 33.15 ? 374 HOH A O 1 HETATM 3669 O O . HOH G 4 . ? 27.929 -35.411 -13.796 1.00 43.02 ? 375 HOH A O 1 HETATM 3670 O O . HOH G 4 . ? 16.348 -8.731 -10.667 1.00 40.37 ? 376 HOH A O 1 HETATM 3671 O O . HOH G 4 . ? 5.570 -4.981 -11.523 1.00 36.65 ? 377 HOH A O 1 HETATM 3672 O O . HOH G 4 . ? -2.944 -32.331 -2.799 1.00 38.82 ? 378 HOH A O 1 HETATM 3673 O O . HOH G 4 . ? 14.812 -25.627 6.697 1.00 30.80 ? 379 HOH A O 1 HETATM 3674 O O . HOH G 4 . ? 16.593 -14.650 -18.361 1.00 52.92 ? 380 HOH A O 1 HETATM 3675 O O . HOH G 4 . ? -6.295 -20.358 -11.927 1.00 34.35 ? 381 HOH A O 1 HETATM 3676 O O . HOH G 4 . ? 12.229 -6.755 -16.593 1.00 33.66 ? 382 HOH A O 1 HETATM 3677 O O . HOH G 4 . ? 10.300 -36.377 -1.273 1.00 33.84 ? 383 HOH A O 1 HETATM 3678 O O . HOH G 4 . ? 7.637 -36.531 -3.252 1.00 30.09 ? 384 HOH A O 1 HETATM 3679 O O . HOH G 4 . ? 13.259 -30.070 6.912 1.00 30.59 ? 385 HOH A O 1 HETATM 3680 O O . HOH G 4 . ? 27.211 -32.039 -13.269 1.00 47.99 ? 386 HOH A O 1 HETATM 3681 O O . HOH G 4 . ? 15.834 -44.095 -4.778 1.00 41.56 ? 387 HOH A O 1 HETATM 3682 O O . HOH G 4 . ? 10.410 -30.282 6.988 1.00 37.19 ? 388 HOH A O 1 HETATM 3683 O O . HOH G 4 . ? -3.544 -26.196 -9.644 1.00 31.36 ? 389 HOH A O 1 HETATM 3684 O O . HOH G 4 . ? 0.640 -11.878 -20.856 1.00 43.02 ? 390 HOH A O 1 HETATM 3685 O O . HOH G 4 . ? 14.461 -30.036 -21.460 1.00 31.25 ? 391 HOH A O 1 HETATM 3686 O O . HOH G 4 . ? 8.234 -25.697 -2.258 1.00 25.76 ? 392 HOH A O 1 HETATM 3687 O O . HOH G 4 . ? 0.674 -2.468 -4.672 1.00 49.03 ? 393 HOH A O 1 HETATM 3688 O O . HOH G 4 . ? 37.092 -44.654 -2.597 1.00 47.62 ? 394 HOH A O 1 HETATM 3689 O O . HOH G 4 . ? 32.026 -45.221 -0.923 1.00 43.96 ? 395 HOH A O 1 HETATM 3690 O O . HOH G 4 . ? 28.451 -12.280 -1.193 1.00 60.49 ? 396 HOH A O 1 HETATM 3691 O O . HOH G 4 . ? 5.729 -3.345 4.200 1.00 40.33 ? 397 HOH A O 1 HETATM 3692 O O . HOH G 4 . ? 1.360 -27.915 -16.012 1.00 30.05 ? 398 HOH A O 1 HETATM 3693 O O . HOH G 4 . ? 2.908 -2.917 -5.963 1.00 34.38 ? 399 HOH A O 1 HETATM 3694 O O . HOH G 4 . ? 11.113 -6.505 -7.673 1.00 33.36 ? 400 HOH A O 1 HETATM 3695 O O . HOH G 4 . ? 7.589 -27.186 -20.103 1.00 40.39 ? 401 HOH A O 1 HETATM 3696 O O . HOH G 4 . ? -3.918 -15.205 -11.937 1.00 33.73 ? 402 HOH A O 1 HETATM 3697 O O . HOH G 4 . ? 17.526 -6.432 -10.145 1.00 37.88 ? 403 HOH A O 1 HETATM 3698 O O . HOH G 4 . ? 1.478 -26.540 0.525 1.00 36.76 ? 404 HOH A O 1 HETATM 3699 O O . HOH G 4 . ? 6.989 -20.859 5.298 1.00 46.52 ? 405 HOH A O 1 HETATM 3700 O O . HOH G 4 . ? -0.840 -13.462 -10.285 1.00 33.38 ? 406 HOH A O 1 HETATM 3701 O O . HOH G 4 . ? -3.068 -17.170 -2.413 1.00 33.53 ? 407 HOH A O 1 HETATM 3702 O O . HOH G 4 . ? 34.161 -27.342 -1.328 1.00 23.94 ? 408 HOH A O 1 HETATM 3703 O O . HOH G 4 . ? -4.433 -7.869 -5.807 1.00 37.35 ? 409 HOH A O 1 HETATM 3704 O O . HOH G 4 . ? 9.618 -12.802 -21.681 1.00 47.53 ? 410 HOH A O 1 HETATM 3705 O O . HOH G 4 . ? 30.609 -12.138 -12.059 1.00 47.77 ? 411 HOH A O 1 HETATM 3706 O O . HOH G 4 . ? 40.108 -40.180 -0.505 1.00 37.24 ? 412 HOH A O 1 HETATM 3707 O O . HOH G 4 . ? 25.842 -26.242 -14.491 1.00 32.60 ? 413 HOH A O 1 HETATM 3708 O O . HOH G 4 . ? 17.644 -7.000 -7.260 1.00 31.84 ? 414 HOH A O 1 HETATM 3709 O O . HOH G 4 . ? 22.744 -28.621 5.578 1.00 48.21 ? 415 HOH A O 1 HETATM 3710 O O . HOH G 4 . ? 2.867 -33.118 -0.598 1.00 38.73 ? 416 HOH A O 1 HETATM 3711 O O . HOH G 4 . ? 7.690 -33.347 -1.984 1.00 36.74 ? 417 HOH A O 1 HETATM 3712 O O . HOH G 4 . ? 2.356 -34.769 -20.046 1.00 46.63 ? 418 HOH A O 1 HETATM 3713 O O . HOH G 4 . ? 7.348 -3.570 -3.799 1.00 57.60 ? 419 HOH A O 1 HETATM 3714 O O . HOH G 4 . ? 17.940 -22.603 -24.188 1.00 35.80 ? 420 HOH A O 1 HETATM 3715 O O . HOH G 4 . ? 2.842 -37.915 -13.814 1.00 41.92 ? 421 HOH A O 1 HETATM 3716 O O . HOH G 4 . ? 5.892 -36.966 -22.671 1.00 32.34 ? 422 HOH A O 1 HETATM 3717 O O . HOH G 4 . ? 7.981 -6.307 -18.142 1.00 38.20 ? 423 HOH A O 1 HETATM 3718 O O . HOH G 4 . ? 2.714 -22.858 1.347 1.00 35.08 ? 424 HOH A O 1 HETATM 3719 O O . HOH G 4 . ? -1.487 -5.498 3.250 1.00 39.52 ? 425 HOH A O 1 HETATM 3720 O O . HOH G 4 . ? 30.836 -13.022 -5.905 1.00 62.31 ? 426 HOH A O 1 HETATM 3721 O O . HOH G 4 . ? 22.438 -45.755 -10.809 1.00 55.51 ? 427 HOH A O 1 HETATM 3722 O O . HOH G 4 . ? 30.032 -16.769 -7.683 1.00 47.58 ? 428 HOH A O 1 HETATM 3723 O O . HOH G 4 . ? 9.553 -46.196 -13.587 1.00 35.60 ? 429 HOH A O 1 HETATM 3724 O O . HOH G 4 . ? 25.380 -45.123 2.635 1.00 36.69 ? 430 HOH A O 1 HETATM 3725 O O . HOH G 4 . ? 12.374 -42.480 -24.173 1.00 46.05 ? 431 HOH A O 1 HETATM 3726 O O . HOH G 4 . ? 4.409 -16.894 7.006 1.00 30.24 ? 432 HOH A O 1 HETATM 3727 O O . HOH G 4 . ? 33.470 -45.442 -3.728 1.00 37.10 ? 434 HOH A O 1 HETATM 3728 O O . HOH G 4 . ? -1.995 -23.981 3.383 1.00 60.52 ? 435 HOH A O 1 HETATM 3729 O O . HOH G 4 . ? 3.264 -4.224 -12.106 1.00 43.21 ? 437 HOH A O 1 HETATM 3730 O O . HOH G 4 . ? 1.015 -21.789 2.805 1.00 44.16 ? 440 HOH A O 1 HETATM 3731 O O . HOH G 4 . ? 24.447 -34.294 -18.007 1.00 50.51 ? 446 HOH A O 1 HETATM 3732 O O . HOH G 4 . ? 10.915 -19.267 6.981 1.00 45.66 ? 448 HOH A O 1 HETATM 3733 O O . HOH G 4 . ? 31.641 -28.638 11.738 1.00 46.89 ? 449 HOH A O 1 HETATM 3734 O O . HOH G 4 . ? 19.074 -9.583 -11.940 1.00 53.07 ? 453 HOH A O 1 HETATM 3735 O O . HOH G 4 . ? -0.787 -19.140 -19.884 1.00 45.70 ? 457 HOH A O 1 HETATM 3736 O O . HOH G 4 . ? -2.703 -8.285 -14.328 1.00 36.91 ? 458 HOH A O 1 HETATM 3737 O O . HOH G 4 . ? 15.282 -27.975 8.039 1.00 46.07 ? 459 HOH A O 1 HETATM 3738 O O . HOH G 4 . ? 7.151 -31.992 4.517 1.00 52.81 ? 464 HOH A O 1 HETATM 3739 O O . HOH G 4 . ? 30.807 -23.103 9.517 1.00 54.25 ? 465 HOH A O 1 HETATM 3740 O O . HOH G 4 . ? -3.443 -13.695 -8.623 1.00 55.20 ? 473 HOH A O 1 HETATM 3741 O O . HOH G 4 . ? 11.070 -26.546 7.210 1.00 55.00 ? 474 HOH A O 1 HETATM 3742 O O . HOH G 4 . ? 3.783 -44.028 -9.525 1.00 43.79 ? 475 HOH A O 1 HETATM 3743 O O . HOH G 4 . ? 8.927 -5.903 1.141 1.00 53.28 ? 477 HOH A O 1 HETATM 3744 O O . HOH G 4 . ? 26.855 -47.075 4.755 1.00 74.58 ? 481 HOH A O 1 HETATM 3745 O O . HOH G 4 . ? 5.045 -43.535 -18.153 1.00 39.02 ? 487 HOH A O 1 HETATM 3746 O O . HOH G 4 . ? 18.994 -3.587 -6.386 1.00 53.95 ? 496 HOH A O 1 HETATM 3747 O O . HOH G 4 . ? 2.141 -35.701 -13.782 1.00 34.27 ? 498 HOH A O 1 HETATM 3748 O O . HOH G 4 . ? 20.117 -5.653 1.241 1.00 45.23 ? 502 HOH A O 1 HETATM 3749 O O . HOH G 4 . ? 27.074 -28.985 -14.055 1.00 42.34 ? 503 HOH A O 1 HETATM 3750 O O . HOH G 4 . ? 23.441 -18.480 -13.626 1.00 67.27 ? 505 HOH A O 1 HETATM 3751 O O . HOH G 4 . ? 25.476 -42.707 -16.549 1.00 48.70 ? 509 HOH A O 1 HETATM 3752 O O . HOH G 4 . ? 13.103 -13.781 14.446 1.00 56.21 ? 513 HOH A O 1 HETATM 3753 O O . HOH G 4 . ? -1.128 -40.976 -9.255 1.00 37.82 ? 519 HOH A O 1 HETATM 3754 O O . HOH G 4 . ? 7.222 -46.257 -11.228 1.00 50.47 ? 524 HOH A O 1 HETATM 3755 O O . HOH G 4 . ? 12.820 -14.797 10.485 1.00 40.73 ? 525 HOH A O 1 HETATM 3756 O O . HOH G 4 . ? 17.520 -25.888 6.727 1.00 103.10 ? 527 HOH A O 1 HETATM 3757 O O . HOH G 4 . ? -1.594 -28.111 -15.607 1.00 47.16 ? 531 HOH A O 1 HETATM 3758 O O . HOH G 4 . ? 8.304 -5.322 -15.566 1.00 48.20 ? 538 HOH A O 1 HETATM 3759 O O . HOH G 4 . ? 13.291 -10.214 -19.862 1.00 57.47 ? 540 HOH A O 1 HETATM 3760 O O . HOH G 4 . ? 17.428 -4.940 1.954 1.00 42.11 ? 541 HOH A O 1 HETATM 3761 O O . HOH G 4 . ? 10.356 -4.759 -1.151 1.00 67.99 ? 542 HOH A O 1 HETATM 3762 O O . HOH G 4 . ? 6.055 -38.668 -3.273 1.00 43.99 ? 543 HOH A O 1 HETATM 3763 O O . HOH G 4 . ? 2.215 -3.537 -9.153 1.00 54.91 ? 544 HOH A O 1 HETATM 3764 O O . HOH G 4 . ? 25.732 -21.373 12.468 1.00 58.07 ? 548 HOH A O 1 HETATM 3765 O O . HOH G 4 . ? 24.943 -29.992 8.371 1.00 46.66 ? 549 HOH A O 1 HETATM 3766 O O . HOH G 4 . ? 23.177 -21.272 5.731 1.00 53.96 ? 551 HOH A O 1 HETATM 3767 O O . HOH G 4 . ? 23.881 -24.385 -21.015 1.00 67.25 ? 554 HOH A O 1 HETATM 3768 O O . HOH G 4 . ? 3.538 -13.312 -24.354 1.00 49.37 ? 555 HOH A O 1 HETATM 3769 O O . HOH G 4 . ? 36.616 -27.645 0.554 1.00 37.83 ? 556 HOH A O 1 HETATM 3770 O O . HOH G 4 . ? -0.868 -34.900 -13.955 1.00 33.95 ? 558 HOH A O 1 HETATM 3771 O O . HOH G 4 . ? 15.266 -40.526 2.327 1.00 45.26 ? 559 HOH A O 1 HETATM 3772 O O . HOH G 4 . ? 10.201 -40.881 -3.093 1.00 37.31 ? 560 HOH A O 1 HETATM 3773 O O . HOH G 4 . ? 31.297 -24.925 -13.108 1.00 44.21 ? 561 HOH A O 1 HETATM 3774 O O . HOH G 4 . ? 7.503 -2.692 -11.802 1.00 59.11 ? 562 HOH A O 1 HETATM 3775 O O . HOH G 4 . ? 4.135 -42.937 -13.822 1.00 47.81 ? 566 HOH A O 1 HETATM 3776 O O . HOH G 4 . ? 30.263 -46.378 -4.499 1.00 39.73 ? 568 HOH A O 1 HETATM 3777 O O . HOH G 4 . ? 8.192 -29.616 -23.693 1.00 44.14 ? 575 HOH A O 1 HETATM 3778 O O . HOH G 4 . ? -0.408 -4.960 -9.785 1.00 43.32 ? 578 HOH A O 1 HETATM 3779 O O . HOH G 4 . ? 11.707 -40.656 -0.874 1.00 42.43 ? 579 HOH A O 1 HETATM 3780 O O . HOH G 4 . ? 2.792 -28.412 -19.028 1.00 44.68 ? 580 HOH A O 1 HETATM 3781 O O . HOH G 4 . ? 9.486 -34.294 0.162 1.00 33.74 ? 581 HOH A O 1 HETATM 3782 O O . HOH G 4 . ? 7.032 -31.595 1.106 1.00 65.55 ? 583 HOH A O 1 HETATM 3783 O O . HOH G 4 . ? 3.705 -21.210 -19.123 1.00 34.86 ? 585 HOH A O 1 HETATM 3784 O O . HOH G 4 . ? -2.616 -11.655 -16.435 1.00 54.65 ? 589 HOH A O 1 HETATM 3785 O O . HOH G 4 . ? 13.175 -16.471 -20.561 1.00 48.42 ? 595 HOH A O 1 HETATM 3786 O O . HOH G 4 . ? 19.396 -21.118 -19.380 1.00 44.40 ? 599 HOH A O 1 HETATM 3787 O O . HOH G 4 . ? 18.283 -4.807 -1.619 1.00 46.73 ? 601 HOH A O 1 HETATM 3788 O O . HOH G 4 . ? 22.605 -26.322 6.762 1.00 43.17 ? 602 HOH A O 1 HETATM 3789 O O . HOH G 4 . ? 22.425 -8.325 -12.115 1.00 48.92 ? 603 HOH A O 1 HETATM 3790 O O . HOH G 4 . ? -0.447 -33.611 -11.718 1.00 54.88 ? 609 HOH A O 1 HETATM 3791 O O . HOH G 4 . ? 31.308 -15.258 -11.182 1.00 42.43 ? 610 HOH A O 1 HETATM 3792 O O . HOH G 4 . ? 17.138 -21.098 -21.788 1.00 43.72 ? 614 HOH A O 1 HETATM 3793 O O . HOH G 4 . ? 8.861 -40.269 -0.306 1.00 42.09 ? 619 HOH A O 1 HETATM 3794 O O . HOH G 4 . ? 29.045 -19.608 -13.137 1.00 49.96 ? 625 HOH A O 1 HETATM 3795 O O . HOH G 4 . ? 38.800 -42.807 -0.679 1.00 39.57 ? 628 HOH A O 1 HETATM 3796 O O . HOH G 4 . ? -5.234 -23.320 -15.749 1.00 57.10 ? 629 HOH A O 1 HETATM 3797 O O . HOH G 4 . ? 12.444 -45.220 -24.129 1.00 55.58 ? 638 HOH A O 1 HETATM 3798 O O . HOH G 4 . ? 46.137 -42.858 -0.359 1.00 36.22 ? 639 HOH A O 1 HETATM 3799 O O . HOH G 4 . ? 29.336 -32.516 11.762 1.00 60.01 ? 640 HOH A O 1 HETATM 3800 O O . HOH G 4 . ? 17.703 -18.188 -21.111 1.00 40.69 ? 641 HOH A O 1 HETATM 3801 O O . HOH G 4 . ? -2.611 -3.948 0.209 1.00 57.73 ? 642 HOH A O 1 HETATM 3802 O O . HOH G 4 . ? 22.889 -46.979 1.898 1.00 61.62 ? 643 HOH A O 1 HETATM 3803 O O . HOH G 4 . ? 19.631 -11.859 -19.595 1.00 52.88 ? 645 HOH A O 1 HETATM 3804 O O . HOH G 4 . ? 11.492 -16.774 -23.459 1.00 47.42 ? 648 HOH A O 1 HETATM 3805 O O . HOH G 4 . ? 20.409 -15.246 -12.106 1.00 33.08 ? 649 HOH A O 1 HETATM 3806 O O . HOH G 4 . ? 30.863 -40.840 -13.650 1.00 49.01 ? 653 HOH A O 1 HETATM 3807 O O . HOH G 4 . ? 22.678 -44.182 -14.682 1.00 54.51 ? 661 HOH A O 1 HETATM 3808 O O . HOH G 4 . ? 33.318 -22.188 6.552 1.00 61.80 ? 662 HOH A O 1 HETATM 3809 O O . HOH G 4 . ? 9.690 -41.602 -6.809 1.00 43.77 ? 666 HOH A O 1 HETATM 3810 O O . HOH G 4 . ? 22.772 -9.435 1.872 1.00 44.40 ? 668 HOH A O 1 HETATM 3811 O O . HOH G 4 . ? 20.507 -34.662 -20.955 1.00 42.44 ? 669 HOH A O 1 HETATM 3812 O O . HOH G 4 . ? 18.636 -8.871 -18.512 1.00 45.86 ? 680 HOH A O 1 HETATM 3813 O O . HOH G 4 . ? 20.699 -20.334 -16.251 1.00 62.01 ? 681 HOH A O 1 HETATM 3814 O O . HOH G 4 . ? 17.638 -21.716 6.365 1.00 46.75 ? 686 HOH A O 1 HETATM 3815 O O . HOH G 4 . ? 24.019 -48.014 5.178 1.00 55.36 ? 687 HOH A O 1 HETATM 3816 O O . HOH G 4 . ? 31.547 -16.510 -5.594 1.00 46.29 ? 689 HOH A O 1 HETATM 3817 O O . HOH G 4 . ? -2.256 -12.536 -19.399 1.00 46.26 ? 690 HOH A O 1 HETATM 3818 O O . HOH G 4 . ? 25.893 -10.911 -12.996 1.00 50.87 ? 692 HOH A O 1 HETATM 3819 O O . HOH G 4 . ? 7.985 -41.598 -4.067 1.00 42.29 ? 693 HOH A O 1 HETATM 3820 O O . HOH G 4 . ? 39.050 -37.298 3.286 1.00 55.22 ? 694 HOH A O 1 HETATM 3821 O O . HOH G 4 . ? 4.680 -29.133 3.242 1.00 44.13 ? 695 HOH A O 1 HETATM 3822 O O . HOH G 4 . ? 19.825 -13.348 -15.943 1.00 56.02 ? 699 HOH A O 1 HETATM 3823 O O . HOH G 4 . ? -5.670 -16.913 -12.244 1.00 53.98 ? 700 HOH A O 1 HETATM 3824 O O . HOH G 4 . ? 27.336 -43.124 -13.960 1.00 41.01 ? 705 HOH A O 1 HETATM 3825 O O . HOH G 4 . ? 34.476 -44.587 2.262 1.00 67.25 ? 706 HOH A O 1 HETATM 3826 O O . HOH G 4 . ? 34.110 -43.022 5.847 1.00 59.32 ? 714 HOH A O 1 HETATM 3827 O O . HOH G 4 . ? 40.424 -33.627 4.013 1.00 44.84 ? 715 HOH A O 1 HETATM 3828 O O . HOH G 4 . ? 12.049 -6.940 -1.182 1.00 42.25 ? 718 HOH A O 1 HETATM 3829 O O . HOH G 4 . ? 22.045 -11.780 -12.567 1.00 50.22 ? 723 HOH A O 1 HETATM 3830 O O . HOH G 4 . ? 25.843 -45.971 -13.648 1.00 57.32 ? 725 HOH A O 1 HETATM 3831 O O . HOH G 4 . ? 43.605 -45.605 -6.140 1.00 38.40 ? 728 HOH A O 1 HETATM 3832 O O . HOH G 4 . ? -0.477 -3.662 -2.266 1.00 57.33 ? 729 HOH A O 1 HETATM 3833 O O . HOH G 4 . ? 37.254 -28.192 8.074 1.00 47.77 ? 736 HOH A O 1 HETATM 3834 O O . HOH G 4 . ? 11.534 -10.375 -2.507 1.00 42.48 ? 738 HOH A O 1 HETATM 3835 O O . HOH G 4 . ? 34.926 -40.448 -18.261 1.00 43.16 ? 743 HOH A O 1 HETATM 3836 O O . HOH G 4 . ? 0.084 -29.934 -18.927 1.00 44.72 ? 744 HOH A O 1 HETATM 3837 O O . HOH H 4 . ? 34.641 -45.486 19.304 1.00 20.41 ? 2 HOH B O 1 HETATM 3838 O O . HOH H 4 . ? 16.013 -66.674 25.216 1.00 18.46 ? 3 HOH B O 1 HETATM 3839 O O . HOH H 4 . ? 26.622 -59.864 21.070 1.00 24.16 ? 4 HOH B O 1 HETATM 3840 O O . HOH H 4 . ? 12.446 -69.845 25.895 1.00 19.19 ? 5 HOH B O 1 HETATM 3841 O O . HOH H 4 . ? 32.730 -47.410 19.944 1.00 25.42 ? 7 HOH B O 1 HETATM 3842 O O . HOH H 4 . ? 17.914 -55.013 21.456 1.00 23.47 ? 12 HOH B O 1 HETATM 3843 O O . HOH H 4 . ? 25.330 -66.271 15.581 1.00 33.81 ? 13 HOH B O 1 HETATM 3844 O O . HOH H 4 . ? 26.628 -52.402 22.317 1.00 22.09 ? 17 HOH B O 1 HETATM 3845 O O . HOH H 4 . ? 29.752 -65.666 11.188 1.00 23.41 ? 22 HOH B O 1 HETATM 3846 O O . HOH H 4 . ? 32.843 -60.864 18.279 1.00 23.29 ? 24 HOH B O 1 HETATM 3847 O O . HOH H 4 . ? 10.235 -50.619 13.422 1.00 23.79 ? 26 HOH B O 1 HETATM 3848 O O . HOH H 4 . ? 25.624 -64.587 12.024 1.00 22.91 ? 27 HOH B O 1 HETATM 3849 O O . HOH H 4 . ? 12.860 -59.391 29.022 1.00 21.64 ? 33 HOH B O 1 HETATM 3850 O O . HOH H 4 . ? 27.011 -42.151 14.262 1.00 21.30 ? 35 HOH B O 1 HETATM 3851 O O . HOH H 4 . ? 25.004 -54.919 22.187 1.00 27.59 ? 37 HOH B O 1 HETATM 3852 O O . HOH H 4 . ? 29.643 -54.126 8.961 1.00 23.29 ? 38 HOH B O 1 HETATM 3853 O O . HOH H 4 . ? 14.087 -40.071 31.637 1.00 28.85 ? 39 HOH B O 1 HETATM 3854 O O . HOH H 4 . ? 6.887 -65.381 23.135 1.00 17.45 ? 40 HOH B O 1 HETATM 3855 O O . HOH H 4 . ? 9.368 -73.907 26.163 1.00 23.36 ? 41 HOH B O 1 HETATM 3856 O O . HOH H 4 . ? 16.209 -53.091 22.754 1.00 20.42 ? 42 HOH B O 1 HETATM 3857 O O . HOH H 4 . ? 12.424 -37.346 25.402 1.00 38.97 ? 43 HOH B O 1 HETATM 3858 O O . HOH H 4 . ? 31.608 -38.206 19.053 1.00 26.36 ? 46 HOH B O 1 HETATM 3859 O O . HOH H 4 . ? 19.529 -73.771 6.229 1.00 20.87 ? 51 HOH B O 1 HETATM 3860 O O . HOH H 4 . ? 23.235 -68.110 11.767 1.00 24.96 ? 52 HOH B O 1 HETATM 3861 O O . HOH H 4 . ? 30.817 -59.006 6.275 1.00 31.92 ? 269 HOH B O 1 HETATM 3862 O O . HOH H 4 . ? 7.306 -78.596 13.842 1.00 37.37 ? 270 HOH B O 1 HETATM 3863 O O . HOH H 4 . ? 16.850 -67.733 31.636 1.00 46.54 ? 271 HOH B O 1 HETATM 3864 O O . HOH H 4 . ? 30.482 -47.519 27.147 1.00 30.09 ? 272 HOH B O 1 HETATM 3865 O O . HOH H 4 . ? 32.336 -55.600 24.267 1.00 42.30 ? 273 HOH B O 1 HETATM 3866 O O . HOH H 4 . ? 7.586 -44.739 21.372 1.00 24.81 ? 274 HOH B O 1 HETATM 3867 O O . HOH H 4 . ? 32.142 -63.950 23.597 1.00 27.92 ? 275 HOH B O 1 HETATM 3868 O O . HOH H 4 . ? 10.774 -74.042 31.888 1.00 34.82 ? 276 HOH B O 1 HETATM 3869 O O . HOH H 4 . ? -1.107 -66.673 13.991 1.00 22.26 ? 277 HOH B O 1 HETATM 3870 O O . HOH H 4 . ? 8.291 -56.674 15.594 1.00 25.44 ? 278 HOH B O 1 HETATM 3871 O O . HOH H 4 . ? 10.387 -61.599 8.771 1.00 32.68 ? 279 HOH B O 1 HETATM 3872 O O . HOH H 4 . ? 27.389 -47.786 23.574 1.00 28.30 ? 280 HOH B O 1 HETATM 3873 O O . HOH H 4 . ? 21.381 -75.449 7.757 1.00 36.21 ? 281 HOH B O 1 HETATM 3874 O O . HOH H 4 . ? 27.261 -50.379 24.306 1.00 33.05 ? 282 HOH B O 1 HETATM 3875 O O . HOH H 4 . ? -4.510 -64.636 21.837 1.00 23.97 ? 283 HOH B O 1 HETATM 3876 O O . HOH H 4 . ? 22.168 -67.276 5.446 1.00 22.45 ? 284 HOH B O 1 HETATM 3877 O O . HOH H 4 . ? 4.014 -71.070 2.833 1.00 21.65 ? 285 HOH B O 1 HETATM 3878 O O . HOH H 4 . ? 25.452 -66.988 12.817 1.00 26.67 ? 286 HOH B O 1 HETATM 3879 O O . HOH H 4 . ? 4.947 -42.656 31.776 1.00 24.20 ? 287 HOH B O 1 HETATM 3880 O O . HOH H 4 . ? 14.018 -49.782 5.531 1.00 30.35 ? 288 HOH B O 1 HETATM 3881 O O . HOH H 4 . ? 32.686 -65.036 12.503 1.00 27.56 ? 289 HOH B O 1 HETATM 3882 O O . HOH H 4 . ? 10.307 -76.909 22.929 1.00 29.47 ? 290 HOH B O 1 HETATM 3883 O O . HOH H 4 . ? 18.064 -65.174 25.693 1.00 30.11 ? 291 HOH B O 1 HETATM 3884 O O . HOH H 4 . ? 0.132 -67.685 6.904 1.00 20.60 ? 292 HOH B O 1 HETATM 3885 O O . HOH H 4 . ? 9.497 -56.716 7.886 1.00 42.20 ? 293 HOH B O 1 HETATM 3886 O O . HOH H 4 . ? -1.582 -65.028 10.700 1.00 30.43 ? 294 HOH B O 1 HETATM 3887 O O . HOH H 4 . ? 28.819 -69.328 14.790 1.00 35.71 ? 295 HOH B O 1 HETATM 3888 O O . HOH H 4 . ? 1.812 -47.114 15.982 1.00 24.42 ? 296 HOH B O 1 HETATM 3889 O O . HOH H 4 . ? 27.398 -67.466 17.124 1.00 28.20 ? 297 HOH B O 1 HETATM 3890 O O . HOH H 4 . ? 6.221 -49.312 34.249 1.00 33.19 ? 298 HOH B O 1 HETATM 3891 O O . HOH H 4 . ? -1.969 -66.072 34.277 1.00 46.46 ? 299 HOH B O 1 HETATM 3892 O O . HOH H 4 . ? 4.592 -65.236 6.191 1.00 35.74 ? 300 HOH B O 1 HETATM 3893 O O . HOH H 4 . ? 32.509 -63.346 19.278 1.00 36.21 ? 301 HOH B O 1 HETATM 3894 O O . HOH H 4 . ? -0.496 -63.872 33.111 1.00 39.17 ? 302 HOH B O 1 HETATM 3895 O O . HOH H 4 . ? -2.309 -70.571 25.078 1.00 29.73 ? 303 HOH B O 1 HETATM 3896 O O . HOH H 4 . ? 13.327 -70.162 32.061 1.00 28.33 ? 304 HOH B O 1 HETATM 3897 O O . HOH H 4 . ? 17.668 -75.441 20.320 1.00 45.44 ? 305 HOH B O 1 HETATM 3898 O O . HOH H 4 . ? -2.551 -54.145 24.687 1.00 38.79 ? 306 HOH B O 1 HETATM 3899 O O . HOH H 4 . ? 32.611 -43.471 25.974 1.00 29.20 ? 307 HOH B O 1 HETATM 3900 O O . HOH H 4 . ? -0.591 -69.035 23.744 1.00 34.57 ? 308 HOH B O 1 HETATM 3901 O O . HOH H 4 . ? 12.240 -74.639 10.849 1.00 38.93 ? 309 HOH B O 1 HETATM 3902 O O . HOH H 4 . ? 25.863 -64.163 6.378 1.00 27.76 ? 310 HOH B O 1 HETATM 3903 O O . HOH H 4 . ? -3.850 -67.340 25.393 1.00 34.42 ? 311 HOH B O 1 HETATM 3904 O O . HOH H 4 . ? 2.254 -66.014 5.180 1.00 34.22 ? 312 HOH B O 1 HETATM 3905 O O . HOH H 4 . ? 35.764 -43.677 22.531 1.00 40.50 ? 313 HOH B O 1 HETATM 3906 O O . HOH H 4 . ? -4.396 -74.207 18.934 1.00 33.31 ? 314 HOH B O 1 HETATM 3907 O O . HOH H 4 . ? 6.092 -64.770 33.256 1.00 22.61 ? 315 HOH B O 1 HETATM 3908 O O . HOH H 4 . ? 34.291 -54.919 14.830 1.00 21.72 ? 316 HOH B O 1 HETATM 3909 O O . HOH H 4 . ? 33.170 -67.685 14.737 1.00 34.68 ? 317 HOH B O 1 HETATM 3910 O O . HOH H 4 . ? 17.319 -63.114 7.534 1.00 28.39 ? 318 HOH B O 1 HETATM 3911 O O . HOH H 4 . ? 2.921 -59.389 12.136 1.00 42.08 ? 319 HOH B O 1 HETATM 3912 O O . HOH H 4 . ? 11.317 -62.419 6.527 1.00 44.46 ? 320 HOH B O 1 HETATM 3913 O O . HOH H 4 . ? -2.896 -68.031 12.653 1.00 28.43 ? 321 HOH B O 1 HETATM 3914 O O . HOH H 4 . ? 8.346 -43.424 38.268 1.00 44.96 ? 322 HOH B O 1 HETATM 3915 O O . HOH H 4 . ? 26.435 -57.059 20.558 1.00 31.07 ? 323 HOH B O 1 HETATM 3916 O O . HOH H 4 . ? 18.457 -74.168 3.156 1.00 20.87 ? 324 HOH B O 1 HETATM 3917 O O . HOH H 4 . ? -0.770 -67.803 16.584 1.00 23.95 ? 325 HOH B O 1 HETATM 3918 O O . HOH H 4 . ? 22.736 -53.467 7.692 1.00 49.12 ? 326 HOH B O 1 HETATM 3919 O O . HOH H 4 . ? 15.045 -75.208 2.410 1.00 34.84 ? 327 HOH B O 1 HETATM 3920 O O . HOH H 4 . ? 29.491 -66.740 18.113 1.00 38.23 ? 328 HOH B O 1 HETATM 3921 O O . HOH H 4 . ? 4.198 -55.912 17.824 1.00 25.56 ? 329 HOH B O 1 HETATM 3922 O O . HOH H 4 . ? 26.987 -53.081 27.429 1.00 50.30 ? 330 HOH B O 1 HETATM 3923 O O . HOH H 4 . ? 12.004 -71.679 15.602 1.00 31.87 ? 331 HOH B O 1 HETATM 3924 O O . HOH H 4 . ? 10.458 -52.957 33.781 1.00 25.98 ? 332 HOH B O 1 HETATM 3925 O O . HOH H 4 . ? 0.204 -58.379 12.169 1.00 27.63 ? 333 HOH B O 1 HETATM 3926 O O . HOH H 4 . ? 12.834 -64.227 39.473 1.00 29.98 ? 334 HOH B O 1 HETATM 3927 O O . HOH H 4 . ? 19.831 -63.850 8.143 1.00 43.20 ? 335 HOH B O 1 HETATM 3928 O O . HOH H 4 . ? 1.256 -54.709 29.400 1.00 27.62 ? 336 HOH B O 1 HETATM 3929 O O . HOH H 4 . ? -3.379 -56.065 23.350 1.00 31.93 ? 337 HOH B O 1 HETATM 3930 O O . HOH H 4 . ? 34.463 -58.660 11.972 1.00 35.25 ? 338 HOH B O 1 HETATM 3931 O O . HOH H 4 . ? 9.916 -47.586 13.672 1.00 45.41 ? 339 HOH B O 1 HETATM 3932 O O . HOH H 4 . ? 19.575 -38.363 12.347 1.00 41.87 ? 340 HOH B O 1 HETATM 3933 O O . HOH H 4 . ? 3.208 -71.069 32.871 1.00 26.81 ? 341 HOH B O 1 HETATM 3934 O O . HOH H 4 . ? 11.341 -76.003 20.336 1.00 31.91 ? 342 HOH B O 1 HETATM 3935 O O . HOH H 4 . ? 7.874 -78.219 16.415 1.00 54.01 ? 343 HOH B O 1 HETATM 3936 O O . HOH H 4 . ? 21.123 -62.604 27.068 1.00 30.67 ? 344 HOH B O 1 HETATM 3937 O O . HOH H 4 . ? 7.728 -35.678 34.567 1.00 35.84 ? 345 HOH B O 1 HETATM 3938 O O . HOH H 4 . ? -6.039 -62.069 25.468 1.00 37.16 ? 346 HOH B O 1 HETATM 3939 O O . HOH H 4 . ? 31.554 -37.134 15.024 1.00 37.20 ? 347 HOH B O 1 HETATM 3940 O O . HOH H 4 . ? 30.801 -65.547 20.152 1.00 38.04 ? 348 HOH B O 1 HETATM 3941 O O . HOH H 4 . ? 19.286 -73.746 12.865 1.00 33.21 ? 349 HOH B O 1 HETATM 3942 O O . HOH H 4 . ? 1.714 -54.936 13.262 1.00 37.71 ? 350 HOH B O 1 HETATM 3943 O O . HOH H 4 . ? 14.494 -74.244 30.433 1.00 39.19 ? 351 HOH B O 1 HETATM 3944 O O . HOH H 4 . ? 17.414 -61.249 35.439 1.00 36.15 ? 352 HOH B O 1 HETATM 3945 O O . HOH H 4 . ? 11.400 -40.312 38.680 1.00 46.46 ? 353 HOH B O 1 HETATM 3946 O O . HOH H 4 . ? 13.245 -66.093 33.943 1.00 30.93 ? 354 HOH B O 1 HETATM 3947 O O . HOH H 4 . ? 20.670 -51.149 33.795 1.00 39.63 ? 355 HOH B O 1 HETATM 3948 O O . HOH H 4 . ? 31.893 -63.315 10.341 1.00 27.44 ? 356 HOH B O 1 HETATM 3949 O O . HOH H 4 . ? 24.149 -40.994 7.027 1.00 44.14 ? 357 HOH B O 1 HETATM 3950 O O . HOH H 4 . ? -3.123 -65.004 15.584 1.00 28.25 ? 358 HOH B O 1 HETATM 3951 O O . HOH H 4 . ? -1.905 -54.674 13.055 1.00 34.97 ? 359 HOH B O 1 HETATM 3952 O O . HOH H 4 . ? 16.354 -73.378 0.501 1.00 29.71 ? 360 HOH B O 1 HETATM 3953 O O . HOH H 4 . ? 25.939 -42.114 5.565 1.00 37.18 ? 361 HOH B O 1 HETATM 3954 O O . HOH H 4 . ? -1.564 -66.621 26.317 1.00 29.51 ? 362 HOH B O 1 HETATM 3955 O O . HOH H 4 . ? 13.451 -53.922 36.892 1.00 51.21 ? 363 HOH B O 1 HETATM 3956 O O . HOH H 4 . ? 37.956 -47.497 15.113 1.00 39.11 ? 364 HOH B O 1 HETATM 3957 O O . HOH H 4 . ? 11.601 -46.740 35.498 1.00 39.67 ? 365 HOH B O 1 HETATM 3958 O O . HOH H 4 . ? 16.262 -64.752 5.460 1.00 41.39 ? 366 HOH B O 1 HETATM 3959 O O . HOH H 4 . ? 20.797 -60.195 8.453 1.00 42.76 ? 367 HOH B O 1 HETATM 3960 O O . HOH H 4 . ? 2.814 -77.250 23.545 1.00 42.79 ? 368 HOH B O 1 HETATM 3961 O O . HOH H 4 . ? 1.052 -60.452 10.555 1.00 47.27 ? 369 HOH B O 1 HETATM 3962 O O . HOH H 4 . ? 17.743 -75.160 16.641 1.00 30.36 ? 370 HOH B O 1 HETATM 3963 O O . HOH H 4 . ? 10.763 -75.992 27.540 1.00 34.57 ? 371 HOH B O 1 HETATM 3964 O O . HOH H 4 . ? 4.878 -46.606 34.258 1.00 28.88 ? 372 HOH B O 1 HETATM 3965 O O . HOH H 4 . ? 22.013 -56.047 6.935 1.00 44.95 ? 373 HOH B O 1 HETATM 3966 O O . HOH H 4 . ? 3.511 -73.607 33.759 1.00 40.57 ? 374 HOH B O 1 HETATM 3967 O O . HOH H 4 . ? 23.813 -63.488 10.201 1.00 27.91 ? 375 HOH B O 1 HETATM 3968 O O . HOH H 4 . ? -2.350 -57.426 13.525 1.00 49.94 ? 376 HOH B O 1 HETATM 3969 O O . HOH H 4 . ? 2.618 -54.085 32.889 1.00 28.66 ? 377 HOH B O 1 HETATM 3970 O O . HOH H 4 . ? 21.127 -56.664 9.358 1.00 40.17 ? 378 HOH B O 1 HETATM 3971 O O . HOH H 4 . ? 19.667 -35.705 8.351 1.00 57.82 ? 379 HOH B O 1 HETATM 3972 O O . HOH H 4 . ? 8.944 -48.912 35.018 1.00 27.80 ? 380 HOH B O 1 HETATM 3973 O O . HOH H 4 . ? 22.928 -72.618 11.432 1.00 36.44 ? 381 HOH B O 1 HETATM 3974 O O . HOH H 4 . ? -3.736 -51.149 16.921 1.00 44.57 ? 382 HOH B O 1 HETATM 3975 O O . HOH H 4 . ? 1.630 -38.414 22.489 1.00 38.35 ? 383 HOH B O 1 HETATM 3976 O O . HOH H 4 . ? 7.662 -42.082 23.784 1.00 24.23 ? 384 HOH B O 1 HETATM 3977 O O . HOH H 4 . ? 30.371 -56.049 2.493 1.00 47.90 ? 385 HOH B O 1 HETATM 3978 O O . HOH H 4 . ? -1.389 -72.034 27.227 1.00 28.94 ? 386 HOH B O 1 HETATM 3979 O O . HOH H 4 . ? 20.354 -63.929 25.158 1.00 30.64 ? 387 HOH B O 1 HETATM 3980 O O . HOH H 4 . ? -3.142 -65.949 30.945 1.00 35.76 ? 388 HOH B O 1 HETATM 3981 O O . HOH H 4 . ? 9.403 -36.320 27.467 1.00 37.86 ? 389 HOH B O 1 HETATM 3982 O O . HOH H 4 . ? 13.304 -51.802 6.708 1.00 34.26 ? 390 HOH B O 1 HETATM 3983 O O . HOH H 4 . ? 9.606 -43.877 17.657 1.00 33.29 ? 391 HOH B O 1 HETATM 3984 O O . HOH H 4 . ? 30.115 -64.648 3.584 1.00 40.60 ? 392 HOH B O 1 HETATM 3985 O O . HOH H 4 . ? 16.140 -38.325 18.597 1.00 34.29 ? 393 HOH B O 1 HETATM 3986 O O . HOH H 4 . ? 7.793 -46.044 16.793 1.00 33.32 ? 394 HOH B O 1 HETATM 3987 O O . HOH H 4 . ? 1.484 -48.732 31.682 1.00 39.78 ? 395 HOH B O 1 HETATM 3988 O O . HOH H 4 . ? -0.511 -53.009 14.577 1.00 35.91 ? 396 HOH B O 1 HETATM 3989 O O . HOH H 4 . ? 1.942 -78.416 11.539 1.00 28.74 ? 397 HOH B O 1 HETATM 3990 O O . HOH H 4 . ? 31.088 -57.184 26.899 1.00 43.25 ? 398 HOH B O 1 HETATM 3991 O O . HOH H 4 . ? 0.107 -68.053 35.618 1.00 36.09 ? 399 HOH B O 1 HETATM 3992 O O . HOH H 4 . ? 8.642 -75.200 23.947 1.00 29.34 ? 400 HOH B O 1 HETATM 3993 O O . HOH H 4 . ? 10.331 -41.648 16.622 1.00 32.83 ? 401 HOH B O 1 HETATM 3994 O O . HOH H 4 . ? 15.340 -41.797 11.942 1.00 38.71 ? 402 HOH B O 1 HETATM 3995 O O . HOH H 4 . ? 0.832 -53.203 25.026 1.00 27.80 ? 403 HOH B O 1 HETATM 3996 O O . HOH H 4 . ? 31.768 -69.484 15.989 1.00 36.22 ? 404 HOH B O 1 HETATM 3997 O O . HOH H 4 . ? 22.291 -65.091 24.648 1.00 30.63 ? 405 HOH B O 1 HETATM 3998 O O . HOH H 4 . ? 17.888 -76.313 23.007 1.00 39.82 ? 406 HOH B O 1 HETATM 3999 O O . HOH H 4 . ? 27.375 -67.669 25.618 1.00 42.56 ? 407 HOH B O 1 HETATM 4000 O O . HOH H 4 . ? -2.435 -74.427 27.680 1.00 49.05 ? 408 HOH B O 1 HETATM 4001 O O . HOH H 4 . ? -5.842 -65.688 25.637 1.00 37.96 ? 409 HOH B O 1 HETATM 4002 O O . HOH H 4 . ? 16.322 -49.778 34.650 1.00 40.93 ? 410 HOH B O 1 HETATM 4003 O O . HOH H 4 . ? 14.682 -56.326 6.941 1.00 32.57 ? 411 HOH B O 1 HETATM 4004 O O . HOH H 4 . ? 6.004 -45.676 36.427 1.00 28.80 ? 412 HOH B O 1 HETATM 4005 O O . HOH H 4 . ? -1.493 -76.681 9.927 1.00 31.76 ? 413 HOH B O 1 HETATM 4006 O O . HOH H 4 . ? 5.437 -66.172 3.329 1.00 46.31 ? 414 HOH B O 1 HETATM 4007 O O . HOH H 4 . ? 33.117 -53.684 2.529 1.00 55.68 ? 415 HOH B O 1 HETATM 4008 O O . HOH H 4 . ? -7.370 -69.582 18.721 1.00 45.89 ? 416 HOH B O 1 HETATM 4009 O O . HOH H 4 . ? 16.757 -73.746 23.917 1.00 38.25 ? 417 HOH B O 1 HETATM 4010 O O . HOH H 4 . ? 19.059 -61.315 27.271 1.00 34.15 ? 418 HOH B O 1 HETATM 4011 O O . HOH H 4 . ? 40.234 -42.300 14.388 1.00 40.52 ? 419 HOH B O 1 HETATM 4012 O O . HOH H 4 . ? 19.662 -67.218 25.664 1.00 50.70 ? 420 HOH B O 1 HETATM 4013 O O . HOH H 4 . ? 12.045 -72.447 12.406 1.00 31.48 ? 421 HOH B O 1 HETATM 4014 O O . HOH H 4 . ? 19.495 -69.341 24.563 1.00 33.80 ? 422 HOH B O 1 HETATM 4015 O O . HOH H 4 . ? 12.659 -69.394 -2.360 1.00 40.29 ? 423 HOH B O 1 HETATM 4016 O O . HOH H 4 . ? 29.106 -73.708 17.283 1.00 50.79 ? 424 HOH B O 1 HETATM 4017 O O . HOH H 4 . ? 2.535 -41.420 16.714 1.00 27.26 ? 425 HOH B O 1 HETATM 4018 O O . HOH H 4 . ? -1.531 -55.089 29.796 1.00 55.40 ? 426 HOH B O 1 HETATM 4019 O O . HOH H 4 . ? 10.751 -50.920 35.691 1.00 32.07 ? 427 HOH B O 1 HETATM 4020 O O . HOH H 4 . ? 6.646 -38.431 28.441 1.00 33.98 ? 428 HOH B O 1 HETATM 4021 O O . HOH H 4 . ? 32.681 -58.036 24.983 1.00 40.17 ? 429 HOH B O 1 HETATM 4022 O O . HOH H 4 . ? 8.245 -76.454 31.205 1.00 38.32 ? 430 HOH B O 1 HETATM 4023 O O . HOH H 4 . ? 32.356 -62.818 14.670 1.00 33.85 ? 431 HOH B O 1 HETATM 4024 O O . HOH H 4 . ? 27.730 -60.978 2.729 1.00 47.66 ? 432 HOH B O 1 HETATM 4025 O O . HOH H 4 . ? 14.243 -76.545 11.018 1.00 34.17 ? 433 HOH B O 1 HETATM 4026 O O . HOH H 4 . ? -0.236 -51.443 21.701 1.00 35.93 ? 434 HOH B O 1 HETATM 4027 O O . HOH H 4 . ? 26.462 -49.970 26.864 1.00 44.14 ? 435 HOH B O 1 HETATM 4028 O O . HOH H 4 . ? 5.347 -36.929 33.798 1.00 40.15 ? 436 HOH B O 1 HETATM 4029 O O . HOH H 4 . ? 5.649 -57.208 14.100 1.00 36.18 ? 437 HOH B O 1 HETATM 4030 O O . HOH H 4 . ? 24.382 -40.576 30.132 1.00 62.36 ? 438 HOH B O 1 HETATM 4031 O O . HOH H 4 . ? 14.905 -36.009 24.618 1.00 50.93 ? 439 HOH B O 1 HETATM 4032 O O . HOH H 4 . ? 1.046 -75.775 9.580 1.00 27.71 ? 440 HOH B O 1 HETATM 4033 O O . HOH H 4 . ? 26.165 -56.252 27.873 1.00 39.71 ? 441 HOH B O 1 HETATM 4034 O O . HOH H 4 . ? 12.474 -75.779 29.616 1.00 46.58 ? 442 HOH B O 1 HETATM 4035 O O . HOH H 4 . ? 3.023 -79.358 18.724 1.00 35.48 ? 443 HOH B O 1 HETATM 4036 O O . HOH H 4 . ? 14.171 -63.243 5.754 1.00 37.50 ? 444 HOH B O 1 HETATM 4037 O O . HOH H 4 . ? 26.381 -60.809 0.268 1.00 49.32 ? 445 HOH B O 1 HETATM 4038 O O . HOH H 4 . ? 2.533 -76.847 6.977 1.00 51.90 ? 450 HOH B O 1 HETATM 4039 O O . HOH H 4 . ? 11.020 -72.038 37.129 1.00 47.55 ? 451 HOH B O 1 HETATM 4040 O O . HOH H 4 . ? 18.087 -56.655 9.451 1.00 46.90 ? 452 HOH B O 1 HETATM 4041 O O . HOH H 4 . ? 22.558 -43.317 7.814 1.00 49.64 ? 454 HOH B O 1 HETATM 4042 O O . HOH H 4 . ? 37.320 -37.980 15.705 1.00 49.21 ? 455 HOH B O 1 HETATM 4043 O O . HOH H 4 . ? 6.009 -78.696 8.909 1.00 50.28 ? 456 HOH B O 1 HETATM 4044 O O . HOH H 4 . ? 11.940 -77.628 25.211 1.00 39.99 ? 461 HOH B O 1 HETATM 4045 O O . HOH H 4 . ? 23.540 -58.780 26.963 1.00 37.79 ? 462 HOH B O 1 HETATM 4046 O O . HOH H 4 . ? 19.468 -60.970 33.329 1.00 48.23 ? 463 HOH B O 1 HETATM 4047 O O . HOH H 4 . ? 0.653 -79.641 17.632 1.00 45.99 ? 468 HOH B O 1 HETATM 4048 O O . HOH H 4 . ? -2.107 -53.212 31.606 1.00 47.13 ? 471 HOH B O 1 HETATM 4049 O O . HOH H 4 . ? 1.706 -43.340 29.897 1.00 40.75 ? 472 HOH B O 1 HETATM 4050 O O . HOH H 4 . ? 3.036 -49.095 14.463 1.00 38.87 ? 478 HOH B O 1 HETATM 4051 O O . HOH H 4 . ? 11.267 -64.437 4.691 1.00 48.12 ? 479 HOH B O 1 HETATM 4052 O O . HOH H 4 . ? 19.338 -72.636 24.496 1.00 49.13 ? 482 HOH B O 1 HETATM 4053 O O . HOH H 4 . ? 10.616 -51.987 6.462 1.00 43.59 ? 483 HOH B O 1 HETATM 4054 O O . HOH H 4 . ? 11.015 -69.257 36.508 1.00 41.30 ? 484 HOH B O 1 HETATM 4055 O O . HOH H 4 . ? 6.836 -50.163 8.304 1.00 47.86 ? 486 HOH B O 1 HETATM 4056 O O . HOH H 4 . ? -0.983 -45.587 22.980 1.00 35.47 ? 489 HOH B O 1 HETATM 4057 O O . HOH H 4 . ? 4.906 -38.987 31.889 1.00 39.37 ? 491 HOH B O 1 HETATM 4058 O O . HOH H 4 . ? 22.763 -35.815 7.871 1.00 58.77 ? 494 HOH B O 1 HETATM 4059 O O . HOH H 4 . ? -5.184 -60.210 29.387 1.00 51.83 ? 495 HOH B O 1 HETATM 4060 O O . HOH H 4 . ? 15.775 -46.317 34.137 1.00 46.79 ? 497 HOH B O 1 HETATM 4061 O O . HOH H 4 . ? 23.416 -57.483 33.197 1.00 54.56 ? 500 HOH B O 1 HETATM 4062 O O . HOH H 4 . ? 8.767 -76.907 28.809 1.00 44.39 ? 501 HOH B O 1 HETATM 4063 O O . HOH H 4 . ? -3.608 -73.554 34.133 1.00 52.37 ? 504 HOH B O 1 HETATM 4064 O O . HOH H 4 . ? 2.001 -64.615 33.416 1.00 58.40 ? 507 HOH B O 1 HETATM 4065 O O . HOH H 4 . ? 36.611 -57.141 8.983 1.00 49.90 ? 508 HOH B O 1 HETATM 4066 O O . HOH H 4 . ? 11.181 -55.386 6.213 1.00 54.23 ? 510 HOH B O 1 HETATM 4067 O O . HOH H 4 . ? 14.615 -52.483 35.089 1.00 43.08 ? 511 HOH B O 1 HETATM 4068 O O . HOH H 4 . ? 18.563 -46.042 34.409 1.00 39.77 ? 517 HOH B O 1 HETATM 4069 O O . HOH H 4 . ? 23.170 -52.034 32.235 1.00 43.41 ? 520 HOH B O 1 HETATM 4070 O O . HOH H 4 . ? 2.688 -44.767 27.788 1.00 38.87 ? 522 HOH B O 1 HETATM 4071 O O . HOH H 4 . ? -2.967 -77.550 13.123 1.00 40.56 ? 526 HOH B O 1 HETATM 4072 O O . HOH H 4 . ? 24.019 -68.949 25.749 1.00 47.60 ? 528 HOH B O 1 HETATM 4073 O O . HOH H 4 . ? -3.235 -68.885 28.798 1.00 46.63 ? 530 HOH B O 1 HETATM 4074 O O . HOH H 4 . ? 7.243 -61.376 7.885 1.00 56.28 ? 532 HOH B O 1 HETATM 4075 O O . HOH H 4 . ? 5.636 -43.889 16.696 1.00 48.64 ? 533 HOH B O 1 HETATM 4076 O O . HOH H 4 . ? -5.726 -62.321 31.120 1.00 41.55 ? 534 HOH B O 1 HETATM 4077 O O . HOH H 4 . ? 7.455 -65.122 4.757 1.00 46.32 ? 535 HOH B O 1 HETATM 4078 O O . HOH H 4 . ? 7.798 -48.446 15.781 1.00 33.94 ? 536 HOH B O 1 HETATM 4079 O O . HOH H 4 . ? 11.392 -68.273 33.787 1.00 45.31 ? 539 HOH B O 1 HETATM 4080 O O . HOH H 4 . ? -6.295 -72.321 18.165 1.00 54.87 ? 545 HOH B O 1 HETATM 4081 O O . HOH H 4 . ? 8.258 -42.343 19.236 1.00 52.77 ? 546 HOH B O 1 HETATM 4082 O O . HOH H 4 . ? 24.777 -34.854 23.121 1.00 52.12 ? 547 HOH B O 1 HETATM 4083 O O . HOH H 4 . ? 37.277 -44.516 25.401 1.00 58.97 ? 552 HOH B O 1 HETATM 4084 O O . HOH H 4 . ? 8.886 -42.292 14.242 1.00 51.91 ? 557 HOH B O 1 HETATM 4085 O O . HOH H 4 . ? 18.158 -64.020 35.922 1.00 49.11 ? 565 HOH B O 1 HETATM 4086 O O . HOH H 4 . ? 31.346 -40.599 26.643 1.00 44.66 ? 567 HOH B O 1 HETATM 4087 O O . HOH H 4 . ? 22.353 -37.401 25.100 1.00 43.98 ? 569 HOH B O 1 HETATM 4088 O O . HOH H 4 . ? 4.027 -81.504 12.226 1.00 49.82 ? 570 HOH B O 1 HETATM 4089 O O . HOH H 4 . ? 10.341 -45.337 14.949 1.00 48.60 ? 573 HOH B O 1 HETATM 4090 O O . HOH H 4 . ? 1.553 -70.312 35.109 1.00 42.08 ? 574 HOH B O 1 HETATM 4091 O O . HOH H 4 . ? -4.719 -54.327 27.124 1.00 45.64 ? 576 HOH B O 1 HETATM 4092 O O . HOH H 4 . ? 0.742 -52.507 31.054 1.00 54.12 ? 577 HOH B O 1 HETATM 4093 O O . HOH H 4 . ? 20.404 -36.902 17.938 1.00 44.37 ? 582 HOH B O 1 HETATM 4094 O O . HOH H 4 . ? 37.337 -40.260 13.723 1.00 46.83 ? 584 HOH B O 1 HETATM 4095 O O . HOH H 4 . ? -3.914 -76.270 20.451 1.00 48.05 ? 588 HOH B O 1 HETATM 4096 O O . HOH H 4 . ? 20.143 -76.326 12.618 1.00 45.29 ? 590 HOH B O 1 HETATM 4097 O O . HOH H 4 . ? 21.632 -74.526 10.305 1.00 48.22 ? 592 HOH B O 1 HETATM 4098 O O . HOH H 4 . ? 24.833 -70.315 14.006 1.00 41.75 ? 593 HOH B O 1 HETATM 4099 O O . HOH H 4 . ? 16.708 -39.108 12.064 1.00 57.12 ? 597 HOH B O 1 HETATM 4100 O O . HOH H 4 . ? 22.409 -34.619 16.102 1.00 65.70 ? 598 HOH B O 1 HETATM 4101 O O . HOH H 4 . ? 15.507 -58.786 5.651 1.00 45.85 ? 604 HOH B O 1 HETATM 4102 O O . HOH H 4 . ? 9.949 -45.844 37.773 1.00 39.32 ? 605 HOH B O 1 HETATM 4103 O O . HOH H 4 . ? -0.334 -47.375 27.214 1.00 35.03 ? 606 HOH B O 1 HETATM 4104 O O . HOH H 4 . ? -4.876 -69.674 26.443 1.00 60.76 ? 607 HOH B O 1 HETATM 4105 O O . HOH H 4 . ? 15.432 -54.168 5.418 1.00 52.93 ? 611 HOH B O 1 HETATM 4106 O O . HOH H 4 . ? 33.521 -37.045 17.509 1.00 38.34 ? 612 HOH B O 1 HETATM 4107 O O . HOH H 4 . ? 36.673 -54.221 8.853 1.00 38.57 ? 613 HOH B O 1 HETATM 4108 O O . HOH H 4 . ? 20.382 -41.539 35.418 1.00 56.73 ? 618 HOH B O 1 HETATM 4109 O O . HOH H 4 . ? 37.960 -56.019 11.011 1.00 54.89 ? 621 HOH B O 1 HETATM 4110 O O . HOH H 4 . ? 33.522 -37.276 11.135 1.00 60.28 ? 626 HOH B O 1 HETATM 4111 O O . HOH H 4 . ? 32.552 -52.222 8.840 1.00 37.53 ? 627 HOH B O 1 HETATM 4112 O O . HOH H 4 . ? 31.088 -69.717 25.964 1.00 46.98 ? 632 HOH B O 1 HETATM 4113 O O . HOH H 4 . ? 35.354 -42.747 24.920 1.00 37.81 ? 633 HOH B O 1 HETATM 4114 O O . HOH H 4 . ? 4.364 -81.652 18.723 1.00 47.50 ? 634 HOH B O 1 HETATM 4115 O O . HOH H 4 . ? 2.973 -79.036 21.525 1.00 46.85 ? 635 HOH B O 1 HETATM 4116 O O . HOH H 4 . ? 11.283 -75.972 14.191 1.00 50.86 ? 637 HOH B O 1 HETATM 4117 O O . HOH H 4 . ? -5.276 -76.387 23.003 1.00 47.11 ? 644 HOH B O 1 HETATM 4118 O O . HOH H 4 . ? 20.258 -62.480 35.731 1.00 60.76 ? 646 HOH B O 1 HETATM 4119 O O . HOH H 4 . ? 24.696 -55.129 29.874 1.00 44.50 ? 650 HOH B O 1 HETATM 4120 O O . HOH H 4 . ? 10.136 -39.952 18.681 1.00 62.60 ? 651 HOH B O 1 HETATM 4121 O O . HOH H 4 . ? 36.910 -62.506 9.338 1.00 42.27 ? 652 HOH B O 1 HETATM 4122 O O . HOH H 4 . ? 4.731 -53.149 10.544 1.00 61.15 ? 656 HOH B O 1 HETATM 4123 O O . HOH H 4 . ? 23.975 -61.086 7.091 1.00 40.83 ? 658 HOH B O 1 HETATM 4124 O O . HOH H 4 . ? 18.580 -56.158 5.923 1.00 51.12 ? 659 HOH B O 1 HETATM 4125 O O . HOH H 4 . ? 33.014 -39.168 28.920 1.00 56.28 ? 660 HOH B O 1 HETATM 4126 O O . HOH H 4 . ? 39.350 -44.840 10.870 1.00 47.63 ? 664 HOH B O 1 HETATM 4127 O O . HOH H 4 . ? 24.984 -38.489 28.811 1.00 53.54 ? 665 HOH B O 1 HETATM 4128 O O . HOH H 4 . ? 2.278 -52.464 10.145 1.00 57.52 ? 672 HOH B O 1 HETATM 4129 O O . HOH H 4 . ? 29.847 -35.602 16.358 1.00 54.88 ? 685 HOH B O 1 HETATM 4130 O O . HOH H 4 . ? 25.138 -52.351 5.094 1.00 43.63 ? 691 HOH B O 1 HETATM 4131 O O . HOH H 4 . ? 11.529 -42.879 10.793 1.00 46.66 ? 696 HOH B O 1 HETATM 4132 O O . HOH H 4 . ? 3.189 -44.954 14.981 1.00 48.96 ? 698 HOH B O 1 HETATM 4133 O O . HOH H 4 . ? 0.176 -40.806 27.183 1.00 44.64 ? 701 HOH B O 1 HETATM 4134 O O . HOH H 4 . ? 36.639 -59.868 9.231 1.00 50.69 ? 702 HOH B O 1 HETATM 4135 O O . HOH H 4 . ? 22.714 -48.324 32.252 1.00 54.77 ? 707 HOH B O 1 HETATM 4136 O O . HOH H 4 . ? 22.300 -38.110 28.882 1.00 75.60 ? 709 HOH B O 1 HETATM 4137 O O . HOH H 4 . ? 5.673 -45.991 14.303 1.00 55.12 ? 719 HOH B O 1 HETATM 4138 O O . HOH H 4 . ? 27.112 -56.579 14.751 1.00 25.56 ? 726 HOH B O 1 HETATM 4139 O O . HOH H 4 . ? 7.105 -36.106 36.985 1.00 45.10 ? 730 HOH B O 1 HETATM 4140 O O . HOH H 4 . ? 17.655 -60.538 7.032 1.00 43.80 ? 739 HOH B O 1 HETATM 4141 O O . HOH H 4 . ? 18.162 -77.143 14.699 1.00 55.90 ? 740 HOH B O 1 HETATM 4142 O O . HOH H 4 . ? 3.990 -38.193 23.961 1.00 45.88 ? 741 HOH B O 1 HETATM 4143 O O . HOH H 4 . ? -2.419 -69.598 32.204 1.00 47.46 ? 742 HOH B O 1 HETATM 4144 O O . HOH H 4 . ? 23.562 -35.532 10.734 1.00 59.22 ? 745 HOH B O 1 HETATM 4145 O O . HOH H 4 . ? 28.835 -56.469 28.277 1.00 48.75 ? 746 HOH B O 1 HETATM 4146 O O . HOH H 4 . ? 39.045 -41.955 11.866 1.00 64.64 ? 747 HOH B O 1 HETATM 4147 O O . HOH H 4 . ? 6.723 -67.558 1.077 1.00 57.73 ? 748 HOH B 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 . GLY A 1 ? 0.3731 0.4212 0.4794 0.0688 -0.0068 -0.0079 55 GLY A N 2 C CA . GLY A 1 ? 0.3410 0.3818 0.4458 0.0675 -0.0013 -0.0080 55 GLY A CA 3 C C . GLY A 1 ? 0.3610 0.3886 0.4580 0.0704 -0.0016 -0.0041 55 GLY A C 4 O O . GLY A 1 ? 0.4241 0.4497 0.5245 0.0767 -0.0041 -0.0037 55 GLY A O 5 N N . ILE A 2 ? 0.2634 0.2816 0.3513 0.0659 0.0013 -0.0016 56 ILE A N 6 C CA . ILE A 2 ? 0.2246 0.2443 0.3079 0.0588 0.0043 -0.0018 56 ILE A CA 7 C C . ILE A 2 ? 0.2558 0.2803 0.3367 0.0577 0.0006 0.0000 56 ILE A C 8 O O . ILE A 2 ? 0.2456 0.2658 0.3207 0.0607 -0.0032 0.0039 56 ILE A O 9 C CB . ILE A 2 ? 0.2607 0.2693 0.3354 0.0553 0.0072 0.0002 56 ILE A CB 10 C CG1 . ILE A 2 ? 0.2919 0.2977 0.3696 0.0560 0.0109 -0.0036 56 ILE A CG1 11 C CG2 . ILE A 2 ? 0.2362 0.2455 0.3049 0.0488 0.0090 0.0010 56 ILE A CG2 12 C CD1 . ILE A 2 ? 0.4762 0.4702 0.5487 0.0553 0.0119 -0.0024 56 ILE A CD1 13 N N . PRO A 3 ? 0.2197 0.2530 0.3051 0.0536 0.0018 -0.0028 57 PRO A N 14 C CA . PRO A 3 ? 0.2313 0.2702 0.3160 0.0528 -0.0022 -0.0025 57 PRO A CA 15 C C . PRO A 3 ? 0.2591 0.2914 0.3326 0.0491 -0.0022 0.0011 57 PRO A C 16 O O . PRO A 3 ? 0.2496 0.2751 0.3177 0.0452 0.0018 0.0025 57 PRO A O 17 C CB . PRO A 3 ? 0.2451 0.2947 0.3408 0.0492 0.0002 -0.0071 57 PRO A CB 18 C CG . PRO A 3 ? 0.2863 0.3324 0.3813 0.0458 0.0067 -0.0073 57 PRO A CG 19 C CD . PRO A 3 ? 0.2307 0.2698 0.3228 0.0501 0.0070 -0.0064 57 PRO A CD 20 N N . PRO A 4 ? 0.2647 0.3003 0.3350 0.0501 -0.0066 0.0020 58 PRO A N 21 C CA . PRO A 4 ? 0.2579 0.2888 0.3184 0.0463 -0.0061 0.0047 58 PRO A CA 22 C C . PRO A 4 ? 0.2908 0.3254 0.3550 0.0398 -0.0028 0.0019 58 PRO A C 23 O O . PRO A 4 ? 0.3003 0.3428 0.3752 0.0385 -0.0017 -0.0021 58 PRO A O 24 C CB . PRO A 4 ? 0.2929 0.3292 0.3506 0.0501 -0.0121 0.0048 58 PRO A CB 25 C CG . PRO A 4 ? 0.3434 0.3844 0.4071 0.0571 -0.0161 0.0037 58 PRO A CG 26 C CD . PRO A 4 ? 0.2757 0.3202 0.3510 0.0554 -0.0126 -0.0002 58 PRO A CD 27 N N . LEU A 5 ? 0.2020 0.2310 0.2580 0.0359 -0.0012 0.0042 59 LEU A N 28 C CA . LEU A 5 ? 0.1811 0.2128 0.2391 0.0303 0.0012 0.0023 59 LEU A CA 29 C C . LEU A 5 ? 0.2153 0.2528 0.2730 0.0307 -0.0033 0.0007 59 LEU A C 30 O O . LEU A 5 ? 0.2146 0.2484 0.2630 0.0319 -0.0053 0.0035 59 LEU A O 31 C CB . LEU A 5 ? 0.1916 0.2147 0.2412 0.0264 0.0048 0.0050 59 LEU A CB 32 C CG . LEU A 5 ? 0.2438 0.2686 0.2942 0.0212 0.0071 0.0038 59 LEU A CG 33 C CD1 . LEU A 5 ? 0.2463 0.2773 0.3068 0.0195 0.0101 0.0009 59 LEU A CD1 34 C CD2 . LEU A 5 ? 0.2706 0.2873 0.3129 0.0183 0.0100 0.0061 59 LEU A CD2 35 N N . GLU A 6 ? 0.1882 0.2352 0.2568 0.0298 -0.0046 -0.0040 60 GLU A N 36 C CA . GLU A 6 ? 0.1964 0.2498 0.2661 0.0303 -0.0094 -0.0070 60 GLU A CA 37 C C . GLU A 6 ? 0.2419 0.2948 0.3133 0.0243 -0.0064 -0.0082 60 GLU A C 38 O O . GLU A 6 ? 0.2587 0.3141 0.3401 0.0207 -0.0026 -0.0101 60 GLU A O 39 C CB . GLU A 6 ? 0.2304 0.2952 0.3131 0.0334 -0.0136 -0.0126 60 GLU A CB 40 C CG . GLU A 6 ? 0.3945 0.4673 0.4809 0.0335 -0.0186 -0.0177 60 GLU A CG 41 C CD . GLU A 6 ? 0.6832 0.7547 0.7560 0.0374 -0.0234 -0.0160 60 GLU A CD 42 O OE1 . GLU A 6 ? 0.7809 0.8541 0.8488 0.0441 -0.0278 -0.0148 60 GLU A OE1 43 O OE2 . GLU A 6 ? 0.4689 0.5381 0.5361 0.0342 -0.0226 -0.0159 60 GLU A OE2 44 N N . LEU A 7 ? 0.1972 0.2467 0.2591 0.0234 -0.0076 -0.0068 61 LEU A N 45 C CA . LEU A 7 ? 0.1849 0.2332 0.2480 0.0180 -0.0049 -0.0077 61 LEU A CA 46 C C . LEU A 7 ? 0.2324 0.2895 0.3066 0.0167 -0.0077 -0.0138 61 LEU A C 47 O O . LEU A 7 ? 0.2236 0.2801 0.3027 0.0121 -0.0048 -0.0150 61 LEU A O 48 C CB . LEU A 7 ? 0.1890 0.2304 0.2392 0.0170 -0.0044 -0.0043 61 LEU A CB 49 C CG . LEU A 7 ? 0.2539 0.2861 0.2948 0.0173 -0.0013 0.0011 61 LEU A CG 50 C CD1 . LEU A 7 ? 0.2618 0.2894 0.2917 0.0173 -0.0017 0.0039 61 LEU A CD1 51 C CD2 . LEU A 7 ? 0.2775 0.3058 0.3213 0.0135 0.0038 0.0019 61 LEU A CD2 52 N N . GLY A 8 ? 0.2364 0.3017 0.3158 0.0208 -0.0131 -0.0180 62 GLY A N 53 C CA . GLY A 8 ? 0.2248 0.2995 0.3164 0.0198 -0.0165 -0.0253 62 GLY A CA 54 C C . GLY A 8 ? 0.2692 0.3426 0.3543 0.0181 -0.0179 -0.0266 62 GLY A C 55 O O . GLY A 8 ? 0.2783 0.3487 0.3492 0.0211 -0.0200 -0.0238 62 GLY A O 56 N N . ASP A 9 ? 0.2345 0.3088 0.3294 0.0131 -0.0156 -0.0298 63 ASP A N 57 C CA . ASP A 9 ? 0.2463 0.3197 0.3377 0.0110 -0.0165 -0.0320 63 ASP A CA 58 C C . ASP A 9 ? 0.2837 0.3468 0.3626 0.0084 -0.0118 -0.0256 63 ASP A C 59 O O . ASP A 9 ? 0.2785 0.3405 0.3536 0.0070 -0.0123 -0.0269 63 ASP A O 60 C CB . ASP A 9 ? 0.2770 0.3546 0.3866 0.0065 -0.0152 -0.0378 63 ASP A CB 61 C CG . ASP A 9 ? 0.5320 0.6063 0.6513 0.0027 -0.0085 -0.0343 63 ASP A CG 62 O OD1 . ASP A 9 ? 0.5313 0.6118 0.6632 0.0035 -0.0088 -0.0371 63 ASP A OD1 63 O OD2 . ASP A 9 ? 0.6593 0.7252 0.7726 -0.0002 -0.0030 -0.0286 63 ASP A OD2 64 N N . CYS A 10 ? 0.2525 0.3090 0.3265 0.0078 -0.0075 -0.0195 64 CYS A N 65 C CA . CYS A 10 ? 0.2675 0.3151 0.3321 0.0053 -0.0032 -0.0143 64 CYS A CA 66 C C . CYS A 10 ? 0.2817 0.3248 0.3312 0.0082 -0.0044 -0.0104 64 CYS A C 67 O O . CYS A 10 ? 0.2752 0.3196 0.3205 0.0124 -0.0069 -0.0092 64 CYS A O 68 C CB . CYS A 10 ? 0.3040 0.3473 0.3718 0.0032 0.0022 -0.0107 64 CYS A CB 69 S SG . CYS A 10 ? 0.3727 0.4182 0.4560 -0.0013 0.0062 -0.0129 64 CYS A SG 70 N N . SER A 11 ? 0.2408 0.2792 0.2832 0.0061 -0.0026 -0.0086 65 SER A N 71 C CA . SER A 11 ? 0.2306 0.2641 0.2602 0.0079 -0.0023 -0.0044 65 SER A CA 72 C C . SER A 11 ? 0.2528 0.2785 0.2796 0.0061 0.0021 0.0002 65 SER A C 73 O O . SER A 11 ? 0.2299 0.2545 0.2627 0.0036 0.0047 -0.0001 65 SER A O 74 C CB . SER A 11 ? 0.2584 0.2917 0.2833 0.0064 -0.0024 -0.0056 65 SER A CB 75 O OG . SER A 11 ? 0.2387 0.2677 0.2661 0.0021 0.0012 -0.0050 65 SER A OG 76 N N . ILE A 12 ? 0.2398 0.2602 0.2579 0.0075 0.0031 0.0043 66 ILE A N 77 C CA . ILE A 12 ? 0.2279 0.2413 0.2442 0.0060 0.0067 0.0074 66 ILE A CA 78 C C . ILE A 12 ? 0.2349 0.2465 0.2526 0.0019 0.0091 0.0064 66 ILE A C 79 O O . ILE A 12 ? 0.2101 0.2194 0.2304 0.0005 0.0113 0.0067 66 ILE A O 80 C CB . ILE A 12 ? 0.2846 0.2925 0.2928 0.0079 0.0075 0.0116 66 ILE A CB 81 C CG1 . ILE A 12 ? 0.3149 0.3233 0.3220 0.0127 0.0054 0.0135 66 ILE A CG1 82 C CG2 . ILE A 12 ? 0.2691 0.2701 0.2764 0.0054 0.0110 0.0134 66 ILE A CG2 83 C CD1 . ILE A 12 ? 0.4447 0.4513 0.4568 0.0136 0.0062 0.0136 66 ILE A CD1 84 N N . ALA A 13 ? 0.2156 0.2286 0.2315 0.0005 0.0085 0.0051 67 ALA A N 85 C CA . ALA A 13 ? 0.2174 0.2292 0.2351 -0.0028 0.0102 0.0039 67 ALA A CA 86 C C . ALA A 13 ? 0.2168 0.2307 0.2424 -0.0041 0.0109 0.0021 67 ALA A C 87 O O . ALA A 13 ? 0.2415 0.2525 0.2678 -0.0055 0.0133 0.0033 67 ALA A O 88 C CB . ALA A 13 ? 0.2368 0.2512 0.2524 -0.0033 0.0090 0.0020 67 ALA A CB 89 N N . GLY A 14 ? 0.1903 0.2096 0.2224 -0.0033 0.0089 -0.0005 68 GLY A N 90 C CA . GLY A 14 ? 0.1747 0.1961 0.2163 -0.0049 0.0104 -0.0019 68 GLY A CA 91 C C . GLY A 14 ? 0.1905 0.2096 0.2327 -0.0044 0.0133 0.0008 68 GLY A C 92 O O . GLY A 14 ? 0.2081 0.2258 0.2537 -0.0059 0.0165 0.0019 68 GLY A O 93 N N . TRP A 15 ? 0.1628 0.1817 0.2020 -0.0019 0.0124 0.0019 69 TRP A N 94 C CA . TRP A 15 ? 0.1617 0.1789 0.2013 -0.0009 0.0150 0.0037 69 TRP A CA 95 C C . TRP A 15 ? 0.2053 0.2169 0.2387 -0.0018 0.0176 0.0057 69 TRP A C 96 O O . TRP A 15 ? 0.1915 0.2028 0.2266 -0.0022 0.0206 0.0066 69 TRP A O 97 C CB . TRP A 15 ? 0.1654 0.1829 0.2029 0.0023 0.0129 0.0041 69 TRP A CB 98 C CG . TRP A 15 ? 0.1823 0.1969 0.2185 0.0039 0.0151 0.0055 69 TRP A CG 99 C CD1 . TRP A 15 ? 0.2183 0.2335 0.2578 0.0036 0.0184 0.0056 69 TRP A CD1 100 C CD2 . TRP A 15 ? 0.1871 0.1982 0.2189 0.0065 0.0141 0.0069 69 TRP A CD2 101 N NE1 . TRP A 15 ? 0.2307 0.2433 0.2675 0.0059 0.0192 0.0061 69 TRP A NE1 102 C CE2 . TRP A 15 ? 0.2365 0.2463 0.2696 0.0076 0.0165 0.0068 69 TRP A CE2 103 C CE3 . TRP A 15 ? 0.2161 0.2244 0.2427 0.0082 0.0118 0.0085 69 TRP A CE3 104 C CZ2 . TRP A 15 ? 0.2444 0.2502 0.2751 0.0102 0.0163 0.0075 69 TRP A CZ2 105 C CZ3 . TRP A 15 ? 0.2407 0.2446 0.2651 0.0108 0.0120 0.0102 69 TRP A CZ3 106 C CH2 . TRP A 15 ? 0.2522 0.2548 0.2792 0.0116 0.0140 0.0093 69 TRP A CH2 107 N N . LEU A 16 ? 0.1647 0.1725 0.1913 -0.0018 0.0165 0.0065 70 LEU A N 108 C CA . LEU A 16 ? 0.1967 0.2001 0.2185 -0.0024 0.0181 0.0072 70 LEU A CA 109 C C . LEU A 16 ? 0.2080 0.2112 0.2300 -0.0042 0.0194 0.0071 70 LEU A C 110 O O . LEU A 16 ? 0.2242 0.2259 0.2442 -0.0037 0.0211 0.0076 70 LEU A O 111 C CB . LEU A 16 ? 0.2035 0.2032 0.2205 -0.0024 0.0171 0.0078 70 LEU A CB 112 C CG . LEU A 16 ? 0.2738 0.2722 0.2902 0.0001 0.0163 0.0089 70 LEU A CG 113 C CD1 . LEU A 16 ? 0.2844 0.2781 0.2967 -0.0001 0.0163 0.0105 70 LEU A CD1 114 C CD2 . LEU A 16 ? 0.3027 0.3006 0.3211 0.0019 0.0175 0.0084 70 LEU A CD2 115 N N . LEU A 17 ? 0.1582 0.1632 0.1826 -0.0058 0.0184 0.0063 71 LEU A N 116 C CA . LEU A 17 ? 0.1578 0.1623 0.1834 -0.0071 0.0196 0.0064 71 LEU A CA 117 C C . LEU A 17 ? 0.1916 0.1975 0.2225 -0.0070 0.0222 0.0076 71 LEU A C 118 O O . LEU A 17 ? 0.1663 0.1704 0.1965 -0.0070 0.0242 0.0091 71 LEU A O 119 C CB . LEU A 17 ? 0.1555 0.1617 0.1833 -0.0087 0.0177 0.0045 71 LEU A CB 120 C CG . LEU A 17 ? 0.1946 0.1994 0.2170 -0.0090 0.0163 0.0039 71 LEU A CG 121 C CD1 . LEU A 17 ? 0.1859 0.1934 0.2099 -0.0099 0.0147 0.0017 71 LEU A CD1 122 C CD2 . LEU A 17 ? 0.2479 0.2495 0.2668 -0.0094 0.0173 0.0044 71 LEU A CD2 123 N N . GLY A 18 ? 0.1447 0.1539 0.1816 -0.0067 0.0224 0.0070 72 GLY A N 124 C CA . GLY A 18 ? 0.1623 0.1732 0.2064 -0.0070 0.0258 0.0083 72 GLY A CA 125 C C . GLY A 18 ? 0.1606 0.1735 0.2140 -0.0092 0.0257 0.0067 72 GLY A C 126 O O . GLY A 18 ? 0.1638 0.1753 0.2214 -0.0101 0.0291 0.0088 72 GLY A O 127 N N . ASN A 19 ? 0.1555 0.1715 0.2118 -0.0098 0.0219 0.0031 73 ASN A N 128 C CA . ASN A 19 ? 0.1640 0.1827 0.2308 -0.0117 0.0212 0.0001 73 ASN A CA 129 C C . ASN A 19 ? 0.1791 0.2001 0.2572 -0.0124 0.0250 0.0009 73 ASN A C 130 O O . ASN A 19 ? 0.1762 0.2001 0.2559 -0.0111 0.0252 0.0008 73 ASN A O 131 C CB . ASN A 19 ? 0.1892 0.2127 0.2572 -0.0110 0.0163 -0.0046 73 ASN A CB 132 C CG . ASN A 19 ? 0.2795 0.3072 0.3592 -0.0126 0.0145 -0.0096 73 ASN A CG 133 O OD1 . ASN A 19 ? 0.2035 0.2327 0.2958 -0.0143 0.0169 -0.0105 73 ASN A OD1 134 N ND2 . ASN A 19 ? 0.1612 0.1913 0.2377 -0.0118 0.0103 -0.0133 73 ASN A ND2 135 N N . PRO A 20 ? 0.1943 0.2138 0.2810 -0.0144 0.0284 0.0020 74 PRO A N 136 C CA . PRO A 20 ? 0.1974 0.2187 0.2955 -0.0153 0.0334 0.0037 74 PRO A CA 137 C C . PRO A 20 ? 0.2494 0.2780 0.3597 -0.0158 0.0312 -0.0014 74 PRO A C 138 O O . PRO A 20 ? 0.2532 0.2848 0.3706 -0.0156 0.0346 -0.0004 74 PRO A O 139 C CB . PRO A 20 ? 0.2367 0.2542 0.3423 -0.0174 0.0370 0.0056 74 PRO A CB 140 C CG . PRO A 20 ? 0.2733 0.2856 0.3662 -0.0164 0.0353 0.0074 74 PRO A CG 141 C CD . PRO A 20 ? 0.2047 0.2201 0.2913 -0.0157 0.0289 0.0026 74 PRO A CD 142 N N . GLU A 21 ? 0.1892 0.2215 0.3015 -0.0158 0.0253 -0.0072 75 GLU A N 143 C CA . GLU A 21 ? 0.2106 0.2509 0.3334 -0.0153 0.0220 -0.0127 75 GLU A CA 144 C C . GLU A 21 ? 0.2749 0.3173 0.3899 -0.0120 0.0207 -0.0113 75 GLU A C 145 O O . GLU A 21 ? 0.2595 0.3086 0.3830 -0.0109 0.0185 -0.0150 75 GLU A O 146 C CB . GLU A 21 ? 0.2322 0.2765 0.3560 -0.0149 0.0153 -0.0194 75 GLU A CB 147 C CG . GLU A 21 ? 0.3157 0.3597 0.4524 -0.0180 0.0161 -0.0229 75 GLU A CG 148 C CD . GLU A 21 ? 0.7631 0.8126 0.9214 -0.0204 0.0172 -0.0278 75 GLU A CD 149 O OE1 . GLU A 21 ? 0.8462 0.9014 1.0112 -0.0194 0.0170 -0.0293 75 GLU A OE1 150 O OE2 . GLU A 21 ? 0.7566 0.8048 0.9265 -0.0231 0.0184 -0.0305 75 GLU A OE2 151 N N . CYS A 22 ? 0.2371 0.2740 0.3371 -0.0104 0.0216 -0.0066 76 CYS A N 152 C CA . CYS A 22 ? 0.2546 0.2916 0.3463 -0.0073 0.0206 -0.0051 76 CYS A CA 153 C C . CYS A 22 ? 0.2375 0.2722 0.3284 -0.0069 0.0265 -0.0008 76 CYS A C 154 O O . CYS A 22 ? 0.2247 0.2582 0.3079 -0.0044 0.0263 0.0008 76 CYS A O 155 C CB . CYS A 22 ? 0.2877 0.3203 0.3645 -0.0058 0.0174 -0.0038 76 CYS A CB 156 S SG . CYS A 22 ? 0.3514 0.3875 0.4269 -0.0052 0.0111 -0.0085 76 CYS A SG 157 N N . ASP A 23 ? 0.2160 0.2504 0.3153 -0.0091 0.0319 0.0012 77 ASP A N 158 C CA . ASP A 23 ? 0.2069 0.2397 0.3045 -0.0081 0.0383 0.0057 77 ASP A CA 159 C C . ASP A 23 ? 0.2313 0.2685 0.3310 -0.0057 0.0387 0.0047 77 ASP A C 160 O O . ASP A 23 ? 0.2240 0.2594 0.3166 -0.0035 0.0422 0.0077 77 ASP A O 161 C CB . ASP A 23 ? 0.2232 0.2557 0.3317 -0.0107 0.0447 0.0082 77 ASP A CB 162 C CG . ASP A 23 ? 0.3044 0.3306 0.4076 -0.0119 0.0464 0.0116 77 ASP A CG 163 O OD1 . ASP A 23 ? 0.2584 0.2807 0.3483 -0.0106 0.0432 0.0122 77 ASP A OD1 164 O OD2 . ASP A 23 ? 0.3939 0.4191 0.5070 -0.0140 0.0512 0.0138 77 ASP A OD2 165 N N . ARG A 24 ? 0.1704 0.2139 0.2799 -0.0054 0.0349 0.0000 78 ARG A N 166 C CA . ARG A 24 ? 0.1757 0.2236 0.2875 -0.0025 0.0345 -0.0013 78 ARG A CA 167 C C . ARG A 24 ? 0.2198 0.2634 0.3168 0.0009 0.0321 0.0002 78 ARG A C 168 O O . ARG A 24 ? 0.2131 0.2584 0.3102 0.0035 0.0334 0.0002 78 ARG A O 169 C CB . ARG A 24 ? 0.1593 0.2150 0.2835 -0.0021 0.0295 -0.0070 78 ARG A CB 170 C CG . ARG A 24 ? 0.1760 0.2315 0.2922 0.0000 0.0217 -0.0096 78 ARG A CG 171 C CD . ARG A 24 ? 0.1737 0.2378 0.3030 0.0003 0.0168 -0.0159 78 ARG A CD 172 N NE . ARG A 24 ? 0.2169 0.2809 0.3371 0.0026 0.0096 -0.0179 78 ARG A NE 173 C CZ . ARG A 24 ? 0.1655 0.2274 0.2817 0.0009 0.0076 -0.0189 78 ARG A CZ 174 N NH1 . ARG A 24 ? 0.2159 0.2754 0.3378 -0.0033 0.0116 -0.0185 78 ARG A NH1 175 N NH2 . ARG A 24 ? 0.2803 0.3426 0.3872 0.0036 0.0018 -0.0204 78 ARG A NH2 176 N N . LEU A 25 ? 0.2092 0.2472 0.2946 0.0007 0.0288 0.0012 79 LEU A N 177 C CA . LEU A 25 ? 0.2003 0.2334 0.2731 0.0032 0.0266 0.0024 79 LEU A CA 178 C C . LEU A 25 ? 0.2497 0.2768 0.3125 0.0030 0.0299 0.0055 79 LEU A C 179 O O . LEU A 25 ? 0.2316 0.2543 0.2852 0.0043 0.0279 0.0059 79 LEU A O 180 C CB . LEU A 25 ? 0.2008 0.2325 0.2685 0.0034 0.0208 0.0011 79 LEU A CB 181 C CG . LEU A 25 ? 0.2111 0.2491 0.2862 0.0045 0.0162 -0.0025 79 LEU A CG 182 C CD1 . LEU A 25 ? 0.2133 0.2494 0.2807 0.0045 0.0116 -0.0030 79 LEU A CD1 183 C CD2 . LEU A 25 ? 0.2820 0.3229 0.3591 0.0084 0.0143 -0.0033 79 LEU A CD2 184 N N . LEU A 26 ? 0.2177 0.2449 0.2827 0.0018 0.0352 0.0076 80 LEU A N 185 C CA . LEU A 26 ? 0.2184 0.2410 0.2733 0.0026 0.0379 0.0103 80 LEU A CA 186 C C . LEU A 26 ? 0.3173 0.3387 0.3654 0.0059 0.0386 0.0099 80 LEU A C 187 O O . LEU A 26 ? 0.3370 0.3544 0.3756 0.0069 0.0380 0.0103 80 LEU A O 188 C CB . LEU A 26 ? 0.2269 0.2497 0.2850 0.0014 0.0437 0.0136 80 LEU A CB 189 C CG . LEU A 26 ? 0.2628 0.2838 0.3240 -0.0017 0.0430 0.0144 80 LEU A CG 190 C CD1 . LEU A 26 ? 0.2654 0.2876 0.3354 -0.0031 0.0492 0.0175 80 LEU A CD1 191 C CD2 . LEU A 26 ? 0.3169 0.3325 0.3664 -0.0013 0.0409 0.0154 80 LEU A CD2 192 N N . SER A 27 ? 0.2735 0.2988 0.3273 0.0077 0.0392 0.0084 81 SER A N 193 C CA . SER A 27 ? 0.2925 0.3171 0.3415 0.0112 0.0397 0.0071 81 SER A CA 194 C C . SER A 27 ? 0.3230 0.3505 0.3787 0.0127 0.0367 0.0047 81 SER A C 195 O O . SER A 27 ? 0.3226 0.3558 0.3886 0.0126 0.0382 0.0041 81 SER A O 196 C CB . SER A 27 ? 0.3556 0.3829 0.4041 0.0131 0.0460 0.0085 81 SER A CB 197 O OG . SER A 27 ? 0.5132 0.5385 0.5536 0.0166 0.0458 0.0067 81 SER A OG 198 N N . VAL A 28 A 0.2572 0.2806 0.3080 0.0143 0.0326 0.0035 81 VAL A N 199 C CA . VAL A 28 A 0.2508 0.2760 0.3068 0.0165 0.0293 0.0020 81 VAL A CA 200 C C . VAL A 28 A 0.2883 0.3104 0.3412 0.0200 0.0291 0.0006 81 VAL A C 201 O O . VAL A 28 A 0.2945 0.3111 0.3397 0.0201 0.0291 0.0005 81 VAL A O 202 C CB . VAL A 28 A 0.3143 0.3381 0.3696 0.0155 0.0241 0.0024 81 VAL A CB 203 C CG1 . VAL A 28 A 0.3082 0.3362 0.3688 0.0123 0.0240 0.0024 81 VAL A CG1 204 C CG2 . VAL A 28 A 0.3161 0.3323 0.3618 0.0150 0.0222 0.0037 81 VAL A CG2 205 N N . PRO A 29 ? 0.2186 0.2444 0.2783 0.0231 0.0285 -0.0010 82 PRO A N 206 C CA . PRO A 29 ? 0.1943 0.2168 0.2522 0.0268 0.0282 -0.0027 82 PRO A CA 207 C C . PRO A 29 ? 0.2275 0.2435 0.2822 0.0279 0.0236 -0.0017 82 PRO A C 208 O O . PRO A 29 ? 0.2484 0.2633 0.3012 0.0260 0.0208 0.0004 82 PRO A O 209 C CB . PRO A 29 ? 0.2154 0.2452 0.2832 0.0297 0.0296 -0.0046 82 PRO A CB 210 C CG . PRO A 29 ? 0.2650 0.3000 0.3397 0.0281 0.0275 -0.0040 82 PRO A CG 211 C CD . PRO A 29 ? 0.2303 0.2638 0.3008 0.0236 0.0279 -0.0019 82 PRO A CD 212 N N . GLU A 30 ? 0.2158 0.2274 0.2702 0.0312 0.0230 -0.0031 83 GLU A N 213 C CA . GLU A 30 ? 0.2079 0.2122 0.2601 0.0327 0.0195 -0.0013 83 GLU A CA 214 C C . GLU A 30 ? 0.2076 0.2154 0.2634 0.0345 0.0161 0.0007 83 GLU A C 215 O O . GLU A 30 ? 0.2126 0.2282 0.2755 0.0361 0.0161 -0.0009 83 GLU A O 216 C CB . GLU A 30 ? 0.2382 0.2386 0.2927 0.0365 0.0200 -0.0038 83 GLU A CB 217 C CG . GLU A 30 ? 0.3631 0.3542 0.4164 0.0382 0.0176 -0.0017 83 GLU A CG 218 C CD . GLU A 30 ? 0.7044 0.6919 0.7624 0.0425 0.0179 -0.0045 83 GLU A CD 219 O OE1 . GLU A 30 ? 0.4833 0.4745 0.5433 0.0435 0.0203 -0.0091 83 GLU A OE1 220 O OE2 . GLU A 30 ? 0.5271 0.5077 0.5864 0.0451 0.0160 -0.0020 83 GLU A OE2 221 N N . TRP A 31 ? 0.2004 0.2032 0.2515 0.0344 0.0133 0.0041 84 TRP A N 222 C CA . TRP A 31 ? 0.1904 0.1963 0.2425 0.0370 0.0093 0.0062 84 TRP A CA 223 C C . TRP A 31 ? 0.2369 0.2351 0.2860 0.0412 0.0072 0.0097 84 TRP A C 224 O O . TRP A 31 ? 0.2254 0.2147 0.2715 0.0405 0.0091 0.0109 84 TRP A O 225 C CB . TRP A 31 ? 0.1704 0.1789 0.2185 0.0335 0.0081 0.0075 84 TRP A CB 226 C CG . TRP A 31 ? 0.1684 0.1688 0.2083 0.0307 0.0092 0.0103 84 TRP A CG 227 C CD1 . TRP A 31 ? 0.2098 0.2038 0.2441 0.0322 0.0078 0.0144 84 TRP A CD1 228 C CD2 . TRP A 31 ? 0.1697 0.1682 0.2068 0.0259 0.0120 0.0093 84 TRP A CD2 229 N NE1 . TRP A 31 ? 0.1921 0.1806 0.2215 0.0283 0.0100 0.0156 84 TRP A NE1 230 C CE2 . TRP A 31 ? 0.2040 0.1951 0.2350 0.0246 0.0122 0.0122 84 TRP A CE2 231 C CE3 . TRP A 31 ? 0.1826 0.1848 0.2217 0.0231 0.0147 0.0066 84 TRP A CE3 232 C CZ2 . TRP A 31 ? 0.2170 0.2052 0.2449 0.0204 0.0143 0.0116 84 TRP A CZ2 233 C CZ3 . TRP A 31 ? 0.1955 0.1946 0.2300 0.0194 0.0165 0.0066 84 TRP A CZ3 234 C CH2 . TRP A 31 ? 0.1900 0.1822 0.2195 0.0182 0.0161 0.0085 84 TRP A CH2 235 N N . SER A 32 ? 0.2025 0.2042 0.2529 0.0457 0.0033 0.0112 85 SER A N 236 C CA . SER A 32 ? 0.2146 0.2092 0.2613 0.0507 0.0012 0.0159 85 SER A CA 237 C C . SER A 32 ? 0.2676 0.2583 0.3048 0.0495 0.0004 0.0208 85 SER A C 238 O O . SER A 32 ? 0.2518 0.2329 0.2842 0.0510 0.0015 0.0258 85 SER A O 239 C CB . SER A 32 ? 0.2513 0.2524 0.3031 0.0572 -0.0030 0.0152 85 SER A CB 240 O OG . SER A 32 ? 0.2795 0.2913 0.3328 0.0568 -0.0062 0.0130 85 SER A OG 241 N N . TYR A 33 ? 0.2188 0.2169 0.2541 0.0469 -0.0011 0.0194 86 TYR A N 242 C CA . TYR A 33 ? 0.2247 0.2210 0.2513 0.0452 -0.0015 0.0227 86 TYR A CA 243 C C . TYR A 33 ? 0.2397 0.2450 0.2683 0.0412 -0.0024 0.0184 86 TYR A C 244 O O . TYR A 33 ? 0.2383 0.2511 0.2753 0.0405 -0.0028 0.0137 86 TYR A O 245 C CB . TYR A 33 ? 0.2657 0.2612 0.2856 0.0516 -0.0049 0.0276 86 TYR A CB 246 C CG . TYR A 33 ? 0.3219 0.3270 0.3459 0.0573 -0.0104 0.0250 86 TYR A CG 247 C CD1 . TYR A 33 ? 0.3548 0.3703 0.3785 0.0577 -0.0143 0.0217 86 TYR A CD1 248 C CD2 . TYR A 33 ? 0.3478 0.3517 0.3761 0.0631 -0.0120 0.0258 86 TYR A CD2 249 C CE1 . TYR A 33 ? 0.3812 0.4065 0.4097 0.0633 -0.0200 0.0185 86 TYR A CE1 250 C CE2 . TYR A 33 ? 0.3698 0.3834 0.4028 0.0688 -0.0174 0.0230 86 TYR A CE2 251 C CZ . TYR A 33 ? 0.5036 0.5281 0.5367 0.0689 -0.0216 0.0192 86 TYR A CZ 252 O OH . TYR A 33 ? 0.6045 0.6394 0.6433 0.0748 -0.0275 0.0156 86 TYR A OH 253 N N . ILE A 34 ? 0.2362 0.2407 0.2581 0.0385 -0.0020 0.0199 87 ILE A N 254 C CA . ILE A 34 ? 0.2147 0.2264 0.2386 0.0346 -0.0027 0.0160 87 ILE A CA 255 C C . ILE A 34 ? 0.2845 0.3030 0.3050 0.0382 -0.0075 0.0155 87 ILE A C 256 O O . ILE A 34 ? 0.2746 0.2894 0.2859 0.0414 -0.0083 0.0200 87 ILE A O 257 C CB . ILE A 34 ? 0.2480 0.2546 0.2676 0.0289 0.0010 0.0169 87 ILE A CB 258 C CG1 . ILE A 34 ? 0.2480 0.2489 0.2706 0.0260 0.0051 0.0164 87 ILE A CG1 259 C CG2 . ILE A 34 ? 0.2543 0.2679 0.2764 0.0252 0.0003 0.0130 87 ILE A CG2 260 C CD1 . ILE A 34 ? 0.2737 0.2679 0.2915 0.0219 0.0082 0.0180 87 ILE A CD1 261 N N . MET A 35 ? 0.2573 0.2860 0.2858 0.0379 -0.0105 0.0099 88 MET A N 262 C CA . MET A 35 ? 0.2734 0.3104 0.3003 0.0414 -0.0159 0.0073 88 MET A CA 263 C C . MET A 35 ? 0.3130 0.3538 0.3411 0.0364 -0.0155 0.0036 88 MET A C 264 O O . MET A 35 ? 0.2689 0.3128 0.3069 0.0318 -0.0137 -0.0004 88 MET A O 265 C CB . MET A 35 ? 0.3087 0.3554 0.3457 0.0455 -0.0205 0.0026 88 MET A CB 266 C CG . MET A 35 ? 0.4095 0.4529 0.4454 0.0514 -0.0215 0.0061 88 MET A CG 267 S SD . MET A 35 ? 0.5141 0.5690 0.5651 0.0555 -0.0258 -0.0001 88 MET A SD 268 C CE . MET A 35 ? 0.4872 0.5532 0.5355 0.0616 -0.0344 -0.0040 88 MET A CE 269 N N . GLU A 36 ? 0.2901 0.3300 0.3080 0.0374 -0.0166 0.0053 89 GLU A N 270 C CA . GLU A 36 ? 0.2966 0.3397 0.3148 0.0335 -0.0165 0.0017 89 GLU A CA 271 C C . GLU A 36 ? 0.3482 0.3999 0.3626 0.0384 -0.0225 -0.0018 89 GLU A C 272 O O . GLU A 36 ? 0.3447 0.3960 0.3491 0.0446 -0.0248 0.0019 89 GLU A O 273 C CB . GLU A 36 ? 0.3277 0.3620 0.3368 0.0300 -0.0118 0.0065 89 GLU A CB 274 C CG . GLU A 36 ? 0.4385 0.4745 0.4499 0.0249 -0.0105 0.0029 89 GLU A CG 275 C CD . GLU A 36 ? 0.6593 0.6883 0.6617 0.0224 -0.0066 0.0069 89 GLU A CD 276 O OE1 . GLU A 36 ? 0.5237 0.5495 0.5162 0.0258 -0.0062 0.0117 89 GLU A OE1 277 O OE2 . GLU A 36 ? 0.5141 0.5415 0.5200 0.0173 -0.0040 0.0053 89 GLU A OE2 278 N N . LYS A 37 ? 0.3037 0.3633 0.3262 0.0360 -0.0249 -0.0091 90 LYS A N 279 C CA . LYS A 37 ? 0.3051 0.3743 0.3253 0.0406 -0.0312 -0.0145 90 LYS A CA 280 C C . LYS A 37 ? 0.3732 0.4391 0.3788 0.0416 -0.0300 -0.0112 90 LYS A C 281 O O . LYS A 37 ? 0.3548 0.4122 0.3562 0.0371 -0.0243 -0.0066 90 LYS A O 282 C CB . LYS A 37 ? 0.3243 0.4024 0.3597 0.0372 -0.0338 -0.0240 90 LYS A CB 283 C CG . LYS A 37 ? 0.4944 0.5784 0.5458 0.0371 -0.0356 -0.0283 90 LYS A CG 284 C CD . LYS A 37 ? 0.5825 0.6750 0.6508 0.0334 -0.0375 -0.0377 90 LYS A CD 285 C CE . LYS A 37 ? 0.6132 0.7117 0.6988 0.0328 -0.0382 -0.0417 90 LYS A CE 286 N NZ . LYS A 37 ? 0.6489 0.7555 0.7529 0.0291 -0.0398 -0.0510 90 LYS A NZ 287 N N . GLU A 38 ? 0.3988 0.4721 0.3963 0.0480 -0.0353 -0.0137 91 GLU A N 288 C CA . GLU A 38 ? 0.4271 0.4986 0.4098 0.0499 -0.0339 -0.0107 91 GLU A CA 289 C C . GLU A 38 ? 0.4781 0.5485 0.4646 0.0431 -0.0308 -0.0142 91 GLU A C 290 O O . GLU A 38 ? 0.4985 0.5617 0.4765 0.0409 -0.0256 -0.0088 91 GLU A O 291 C CB . GLU A 38 ? 0.4632 0.5447 0.4369 0.0587 -0.0408 -0.0141 91 GLU A CB 292 C CG . GLU A 38 ? 0.6198 0.6978 0.5741 0.0632 -0.0383 -0.0071 91 GLU A CG 293 C CD . GLU A 38 ? 0.9105 0.9882 0.8518 0.0726 -0.0404 -0.0003 91 GLU A CD 294 O OE1 . GLU A 38 ? 0.7373 0.8222 0.6831 0.0779 -0.0469 -0.0041 91 GLU A OE1 295 O OE2 . GLU A 38 ? 0.8536 0.9240 0.7804 0.0749 -0.0355 0.0089 91 GLU A OE2 296 N N . ASN A 39 ? 0.4300 0.5071 0.4304 0.0398 -0.0336 -0.0232 92 ASN A N 297 C CA . ASN A 39 ? 0.4075 0.4833 0.4136 0.0336 -0.0308 -0.0269 92 ASN A CA 298 C C . ASN A 39 ? 0.4001 0.4756 0.4244 0.0276 -0.0295 -0.0306 92 ASN A C 299 O O . ASN A 39 ? 0.3805 0.4640 0.4175 0.0271 -0.0335 -0.0389 92 ASN A O 300 C CB . ASN A 39 ? 0.4520 0.5369 0.4560 0.0364 -0.0355 -0.0348 92 ASN A CB 301 C CG . ASN A 39 ? 0.7013 0.7867 0.6865 0.0424 -0.0357 -0.0309 92 ASN A CG 302 O OD1 . ASN A 39 ? 0.6116 0.7044 0.5895 0.0499 -0.0410 -0.0328 92 ASN A OD1 303 N ND2 . ASN A 39 ? 0.5776 0.6558 0.5548 0.0394 -0.0298 -0.0255 92 ASN A ND2 304 N N . PRO A 40 ? 0.3294 0.3959 0.3554 0.0233 -0.0239 -0.0244 93 PRO A N 305 C CA . PRO A 40 ? 0.2992 0.3652 0.3408 0.0181 -0.0216 -0.0266 93 PRO A CA 306 C C . PRO A 40 ? 0.3146 0.3814 0.3646 0.0134 -0.0206 -0.0316 93 PRO A C 307 O O . PRO A 40 ? 0.3067 0.3704 0.3491 0.0124 -0.0190 -0.0305 93 PRO A O 308 C CB . PRO A 40 ? 0.3160 0.3721 0.3533 0.0156 -0.0159 -0.0187 93 PRO A CB 309 C CG . PRO A 40 ? 0.3908 0.4427 0.4128 0.0198 -0.0158 -0.0127 93 PRO A CG 310 C CD . PRO A 40 ? 0.3494 0.4062 0.3637 0.0229 -0.0190 -0.0154 93 PRO A CD 311 N N . ARG A 41 ? 0.2612 0.3319 0.3276 0.0106 -0.0209 -0.0368 94 ARG A N 312 C CA . ARG A 41 ? 0.2499 0.3207 0.3255 0.0063 -0.0199 -0.0415 94 ARG A CA 313 C C . ARG A 41 ? 0.2614 0.3230 0.3378 0.0013 -0.0133 -0.0359 94 ARG A C 314 O O . ARG A 41 ? 0.2569 0.3163 0.3350 -0.0013 -0.0120 -0.0375 94 ARG A O 315 C CB . ARG A 41 ? 0.2767 0.3549 0.3723 0.0048 -0.0221 -0.0494 94 ARG A CB 316 C CG . ARG A 41 ? 0.4018 0.4910 0.5012 0.0096 -0.0294 -0.0569 94 ARG A CG 317 C CD . ARG A 41 ? 0.3104 0.4049 0.4326 0.0065 -0.0295 -0.0632 94 ARG A CD 318 N NE . ARG A 41 ? 0.3842 0.4808 0.5174 0.0035 -0.0305 -0.0706 94 ARG A NE 319 C CZ . ARG A 41 ? 0.3936 0.4854 0.5401 -0.0023 -0.0253 -0.0703 94 ARG A CZ 320 N NH1 . ARG A 41 ? 0.2904 0.3759 0.4412 -0.0057 -0.0187 -0.0632 94 ARG A NH1 321 N NH2 . ARG A 41 ? 0.2240 0.3176 0.3805 -0.0043 -0.0268 -0.0775 94 ARG A NH2 322 N N . ASP A 42 ? 0.2045 0.2616 0.2809 0.0003 -0.0095 -0.0301 95 ASP A N 323 C CA . ASP A 42 ? 0.2080 0.2575 0.2858 -0.0036 -0.0035 -0.0251 95 ASP A CA 324 C C . ASP A 42 ? 0.2361 0.2783 0.2991 -0.0031 -0.0010 -0.0185 95 ASP A C 325 O O . ASP A 42 ? 0.2021 0.2416 0.2606 -0.0019 0.0005 -0.0144 95 ASP A O 326 C CB . ASP A 42 ? 0.2107 0.2611 0.3003 -0.0051 -0.0006 -0.0243 95 ASP A CB 327 C CG . ASP A 42 ? 0.3114 0.3683 0.4190 -0.0069 -0.0018 -0.0310 95 ASP A CG 328 O OD1 . ASP A 42 ? 0.2794 0.3359 0.3926 -0.0092 -0.0020 -0.0344 95 ASP A OD1 329 O OD2 . ASP A 42 ? 0.3151 0.3777 0.4325 -0.0059 -0.0029 -0.0335 95 ASP A OD2 330 N N . GLY A 43 A 0.2184 0.2578 0.2755 -0.0042 -0.0006 -0.0184 95 GLY A N 331 C CA . GLY A 43 A 0.2184 0.2517 0.2633 -0.0041 0.0016 -0.0134 95 GLY A CA 332 C C . GLY A 43 A 0.2625 0.2909 0.3085 -0.0073 0.0048 -0.0120 95 GLY A C 333 O O . GLY A 43 A 0.2413 0.2666 0.2917 -0.0089 0.0079 -0.0097 95 GLY A O 334 N N . LEU A 44 ? 0.2625 0.2907 0.3046 -0.0077 0.0042 -0.0136 96 LEU A N 335 C CA . LEU A 44 ? 0.2526 0.2767 0.2961 -0.0101 0.0067 -0.0128 96 LEU A CA 336 C C . LEU A 44 ? 0.3008 0.3272 0.3562 -0.0117 0.0061 -0.0172 96 LEU A C 337 O O . LEU A 44 ? 0.3146 0.3448 0.3718 -0.0112 0.0035 -0.0222 96 LEU A O 338 C CB . LEU A 44 ? 0.2569 0.2803 0.2920 -0.0097 0.0065 -0.0129 96 LEU A CB 339 C CG . LEU A 44 ? 0.3243 0.3432 0.3502 -0.0095 0.0087 -0.0081 96 LEU A CG 340 C CD1 . LEU A 44 ? 0.3155 0.3331 0.3385 -0.0081 0.0089 -0.0050 96 LEU A CD1 341 C CD2 . LEU A 44 ? 0.3287 0.3486 0.3476 -0.0087 0.0087 -0.0085 96 LEU A CD2 342 N N . CYS A 45 ? 0.2731 0.2971 0.3371 -0.0134 0.0089 -0.0154 97 CYS A N 343 C CA . CYS A 45 ? 0.2880 0.3125 0.3653 -0.0154 0.0096 -0.0184 97 CYS A CA 344 C C . CYS A 45 ? 0.2584 0.2801 0.3354 -0.0162 0.0098 -0.0196 97 CYS A C 345 O O . CYS A 45 ? 0.2312 0.2558 0.3154 -0.0166 0.0076 -0.0254 97 CYS A O 346 C CB . CYS A 45 ? 0.3244 0.3462 0.4098 -0.0167 0.0138 -0.0147 97 CYS A CB 347 S SG . CYS A 45 ? 0.3999 0.4146 0.4758 -0.0163 0.0184 -0.0066 97 CYS A SG 348 N N . TYR A 46 ? 0.1891 0.2058 0.2576 -0.0160 0.0119 -0.0149 98 TYR A N 349 C CA . TYR A 46 ? 0.1742 0.1891 0.2413 -0.0162 0.0117 -0.0162 98 TYR A CA 350 C C . TYR A 46 ? 0.1768 0.1953 0.2344 -0.0148 0.0091 -0.0185 98 TYR A C 351 O O . TYR A 46 ? 0.1722 0.1902 0.2215 -0.0139 0.0095 -0.0153 98 TYR A O 352 C CB . TYR A 46 ? 0.1859 0.1950 0.2481 -0.0160 0.0145 -0.0108 98 TYR A CB 353 C CG . TYR A 46 ? 0.1877 0.1953 0.2514 -0.0160 0.0140 -0.0128 98 TYR A CG 354 C CD1 . TYR A 46 ? 0.2117 0.2158 0.2843 -0.0165 0.0156 -0.0123 98 TYR A CD1 355 C CD2 . TYR A 46 ? 0.1819 0.1914 0.2388 -0.0154 0.0124 -0.0149 98 TYR A CD2 356 C CE1 . TYR A 46 ? 0.1711 0.1735 0.2453 -0.0160 0.0151 -0.0139 98 TYR A CE1 357 C CE2 . TYR A 46 ? 0.2016 0.2104 0.2606 -0.0152 0.0120 -0.0172 98 TYR A CE2 358 C CZ . TYR A 46 ? 0.2243 0.2296 0.2921 -0.0154 0.0130 -0.0169 98 TYR A CZ 359 O OH . TYR A 46 ? 0.2246 0.2289 0.2945 -0.0148 0.0125 -0.0191 98 TYR A OH 360 N N . PRO A 47 ? 0.1578 0.1800 0.2167 -0.0144 0.0068 -0.0240 99 PRO A N 361 C CA . PRO A 47 ? 0.1445 0.1710 0.1940 -0.0125 0.0049 -0.0257 99 PRO A CA 362 C C . PRO A 47 ? 0.1998 0.2235 0.2396 -0.0123 0.0069 -0.0217 99 PRO A C 363 O O . PRO A 47 ? 0.1570 0.1768 0.1979 -0.0135 0.0087 -0.0198 99 PRO A O 364 C CB . PRO A 47 ? 0.1881 0.2195 0.2423 -0.0118 0.0023 -0.0330 99 PRO A CB 365 C CG . PRO A 47 ? 0.2282 0.2556 0.2922 -0.0138 0.0037 -0.0339 99 PRO A CG 366 C CD . PRO A 47 ? 0.1932 0.2163 0.2628 -0.0152 0.0058 -0.0292 99 PRO A CD 367 N N . GLY A 48 ? 0.1675 0.1934 0.1984 -0.0107 0.0066 -0.0206 100 GLY A N 368 C CA . GLY A 48 ? 0.1880 0.2114 0.2116 -0.0110 0.0091 -0.0172 100 GLY A CA 369 C C . GLY A 48 ? 0.2646 0.2889 0.2794 -0.0092 0.0096 -0.0143 100 GLY A C 370 O O . GLY A 48 ? 0.2604 0.2890 0.2721 -0.0068 0.0076 -0.0160 100 GLY A O 371 N N . SER A 49 ? 0.2130 0.2331 0.2241 -0.0101 0.0122 -0.0099 101 SER A N 372 C CA . SER A 49 ? 0.2034 0.2228 0.2069 -0.0086 0.0137 -0.0062 101 SER A CA 373 C C . SER A 49 ? 0.2256 0.2397 0.2292 -0.0095 0.0152 -0.0021 101 SER A C 374 O O . SER A 49 ? 0.2039 0.2154 0.2119 -0.0112 0.0154 -0.0023 101 SER A O 375 C CB . SER A 49 ? 0.2548 0.2756 0.2538 -0.0085 0.0163 -0.0060 101 SER A CB 376 O OG . SER A 49 ? 0.3184 0.3365 0.3211 -0.0111 0.0184 -0.0059 101 SER A OG 377 N N . PHE A 50 ? 0.2138 0.2261 0.2121 -0.0080 0.0164 0.0017 102 PHE A N 378 C CA . PHE A 50 ? 0.2078 0.2148 0.2067 -0.0087 0.0178 0.0050 102 PHE A CA 379 C C . PHE A 50 ? 0.2344 0.2384 0.2291 -0.0085 0.0211 0.0088 102 PHE A C 380 O O . PHE A 50 ? 0.2607 0.2657 0.2496 -0.0058 0.0214 0.0113 102 PHE A O 381 C CB . PHE A 50 ? 0.2247 0.2321 0.2240 -0.0066 0.0155 0.0058 102 PHE A CB 382 C CG . PHE A 50 ? 0.2442 0.2472 0.2464 -0.0074 0.0162 0.0073 102 PHE A CG 383 C CD1 . PHE A 50 ? 0.2645 0.2682 0.2713 -0.0079 0.0150 0.0055 102 PHE A CD1 384 C CD2 . PHE A 50 ? 0.3104 0.3084 0.3110 -0.0077 0.0185 0.0101 102 PHE A CD2 385 C CE1 . PHE A 50 ? 0.2999 0.3003 0.3084 -0.0081 0.0159 0.0065 102 PHE A CE1 386 C CE2 . PHE A 50 ? 0.3327 0.3273 0.3361 -0.0080 0.0189 0.0103 102 PHE A CE2 387 C CZ . PHE A 50 ? 0.2996 0.2958 0.3062 -0.0080 0.0175 0.0083 102 PHE A CZ 388 N N . ASN A 51 ? 0.1952 0.1963 0.1931 -0.0111 0.0237 0.0090 103 ASN A N 389 C CA . ASN A 51 ? 0.1943 0.1922 0.1908 -0.0118 0.0279 0.0124 103 ASN A CA 390 C C . ASN A 51 ? 0.2440 0.2367 0.2393 -0.0105 0.0291 0.0166 103 ASN A C 391 O O . ASN A 51 ? 0.2266 0.2169 0.2250 -0.0106 0.0274 0.0158 103 ASN A O 392 C CB . ASN A 51 ? 0.2254 0.2222 0.2282 -0.0150 0.0299 0.0102 103 ASN A CB 393 C CG . ASN A 51 ? 0.3604 0.3621 0.3647 -0.0160 0.0294 0.0065 103 ASN A CG 394 O OD1 . ASN A 51 ? 0.3658 0.3710 0.3659 -0.0148 0.0305 0.0067 103 ASN A OD1 395 N ND2 . ASN A 51 ? 0.2676 0.2696 0.2777 -0.0177 0.0281 0.0030 103 ASN A ND2 396 N N . ASP A 52 ? 0.2242 0.2151 0.2148 -0.0090 0.0325 0.0214 104 ASP A N 397 C CA . ASP A 52 ? 0.2321 0.2169 0.2217 -0.0074 0.0343 0.0263 104 ASP A CA 398 C C . ASP A 52 ? 0.2491 0.2344 0.2368 -0.0044 0.0300 0.0261 104 ASP A C 399 O O . ASP A 52 ? 0.2490 0.2298 0.2401 -0.0043 0.0297 0.0268 104 ASP A O 400 C CB . ASP A 52 ? 0.2790 0.2581 0.2771 -0.0109 0.0371 0.0260 104 ASP A CB 401 C CG . ASP A 52 ? 0.4052 0.3833 0.4064 -0.0136 0.0424 0.0273 104 ASP A CG 402 O OD1 . ASP A 52 ? 0.4737 0.4542 0.4687 -0.0121 0.0451 0.0305 104 ASP A OD1 403 O OD2 . ASP A 52 ? 0.5612 0.5367 0.5712 -0.0169 0.0440 0.0249 104 ASP A OD2 404 N N . TYR A 53 ? 0.2329 0.2242 0.2161 -0.0020 0.0266 0.0243 105 TYR A N 405 C CA . TYR A 53 ? 0.2437 0.2372 0.2269 0.0007 0.0223 0.0232 105 TYR A CA 406 C C . TYR A 53 ? 0.2820 0.2720 0.2611 0.0048 0.0225 0.0282 105 TYR A C 407 O O . TYR A 53 ? 0.2656 0.2539 0.2481 0.0057 0.0207 0.0279 105 TYR A O 408 C CB . TYR A 53 ? 0.2598 0.2610 0.2413 0.0020 0.0187 0.0191 105 TYR A CB 409 C CG . TYR A 53 ? 0.2745 0.2793 0.2597 0.0035 0.0144 0.0161 105 TYR A CG 410 C CD1 . TYR A 53 ? 0.2944 0.2971 0.2863 0.0014 0.0141 0.0145 105 TYR A CD1 411 C CD2 . TYR A 53 ? 0.3033 0.3145 0.2860 0.0069 0.0107 0.0139 105 TYR A CD2 412 C CE1 . TYR A 53 ? 0.2983 0.3047 0.2947 0.0024 0.0111 0.0119 105 TYR A CE1 413 C CE2 . TYR A 53 ? 0.3270 0.3423 0.3156 0.0077 0.0070 0.0103 105 TYR A CE2 414 C CZ . TYR A 53 ? 0.3701 0.3827 0.3658 0.0052 0.0077 0.0097 105 TYR A CZ 415 O OH . TYR A 53 ? 0.3760 0.3928 0.3784 0.0057 0.0050 0.0065 105 TYR A OH 416 N N . GLU A 54 ? 0.2740 0.2628 0.2457 0.0075 0.0251 0.0333 106 GLU A N 417 C CA . GLU A 54 ? 0.2953 0.2801 0.2623 0.0121 0.0256 0.0392 106 GLU A CA 418 C C . GLU A 54 ? 0.3216 0.2976 0.2950 0.0101 0.0286 0.0418 106 GLU A C 419 O O . GLU A 54 ? 0.3183 0.2913 0.2925 0.0130 0.0271 0.0436 106 GLU A O 420 C CB . GLU A 54 ? 0.3395 0.3240 0.2966 0.0156 0.0289 0.0451 106 GLU A CB 421 C CG . GLU A 54 ? 0.5543 0.5479 0.5029 0.0198 0.0253 0.0429 106 GLU A CG 422 C CD . GLU A 54 ? 1.0186 1.0118 0.9549 0.0256 0.0279 0.0501 106 GLU A CD 423 O OE1 . GLU A 54 ? 0.9538 0.9397 0.8886 0.0248 0.0345 0.0569 106 GLU A OE1 424 O OE2 . GLU A 54 ? 1.0581 1.0584 0.9865 0.0314 0.0234 0.0487 106 GLU A OE2 425 N N . GLU A 55 ? 0.2771 0.2494 0.2560 0.0053 0.0326 0.0411 107 GLU A N 426 C CA . GLU A 55 ? 0.2738 0.2381 0.2605 0.0029 0.0353 0.0420 107 GLU A CA 427 C C . GLU A 55 ? 0.2970 0.2621 0.2896 0.0023 0.0314 0.0368 107 GLU A C 428 O O . GLU A 55 ? 0.2911 0.2507 0.2874 0.0035 0.0317 0.0380 107 GLU A O 429 C CB . GLU A 55 ? 0.3025 0.2645 0.2947 -0.0019 0.0399 0.0413 107 GLU A CB 430 C CG . GLU A 55 ? 0.4640 0.4254 0.4503 -0.0010 0.0449 0.0472 107 GLU A CG 431 C CD . GLU A 55 ? 0.8038 0.7729 0.7839 -0.0010 0.0448 0.0455 107 GLU A CD 432 O OE1 . GLU A 55 ? 0.3747 0.3506 0.3497 0.0013 0.0398 0.0423 107 GLU A OE1 433 O OE2 . GLU A 55 ? 0.8245 0.7930 0.8054 -0.0030 0.0501 0.0478 107 GLU A OE2 434 N N . LEU A 56 ? 0.2531 0.2251 0.2461 0.0011 0.0278 0.0314 108 LEU A N 435 C CA . LEU A 56 ? 0.2476 0.2209 0.2450 0.0011 0.0247 0.0273 108 LEU A CA 436 C C . LEU A 56 ? 0.2643 0.2384 0.2595 0.0058 0.0221 0.0292 108 LEU A C 437 O O . LEU A 56 ? 0.2657 0.2371 0.2649 0.0068 0.0216 0.0284 108 LEU A O 438 C CB . LEU A 56 ? 0.2442 0.2238 0.2431 -0.0011 0.0225 0.0222 108 LEU A CB 439 C CG . LEU A 56 ? 0.2802 0.2618 0.2829 -0.0008 0.0202 0.0188 108 LEU A CG 440 C CD1 . LEU A 56 ? 0.2922 0.2688 0.2995 -0.0018 0.0214 0.0172 108 LEU A CD1 441 C CD2 . LEU A 56 ? 0.2992 0.2865 0.3027 -0.0023 0.0186 0.0154 108 LEU A CD2 442 N N . LYS A 57 ? 0.2277 0.2061 0.2167 0.0090 0.0203 0.0312 109 LYS A N 443 C CA . LYS A 57 ? 0.2216 0.2019 0.2088 0.0141 0.0173 0.0327 109 LYS A CA 444 C C . LYS A 57 ? 0.2960 0.2682 0.2830 0.0168 0.0195 0.0380 109 LYS A C 445 O O . LYS A 57 ? 0.3094 0.2809 0.2992 0.0196 0.0175 0.0377 109 LYS A O 446 C CB . LYS A 57 ? 0.2634 0.2504 0.2436 0.0175 0.0146 0.0332 109 LYS A CB 447 C CG . LYS A 57 ? 0.3806 0.3759 0.3636 0.0156 0.0114 0.0270 109 LYS A CG 448 C CD . LYS A 57 ? 0.3854 0.3878 0.3626 0.0200 0.0078 0.0264 109 LYS A CD 449 C CE . LYS A 57 ? 0.5612 0.5710 0.5418 0.0177 0.0054 0.0201 109 LYS A CE 450 N NZ . LYS A 57 ? 0.6271 0.6451 0.6038 0.0223 0.0008 0.0175 109 LYS A NZ 451 N N . HIS A 58 ? 0.2718 0.2374 0.2568 0.0157 0.0239 0.0426 110 HIS A N 452 C CA . HIS A 58 ? 0.3120 0.2684 0.2984 0.0177 0.0270 0.0481 110 HIS A CA 453 C C . HIS A 58 ? 0.3418 0.2935 0.3379 0.0151 0.0275 0.0443 110 HIS A C 454 O O . HIS A 58 ? 0.3380 0.2849 0.3366 0.0182 0.0273 0.0462 110 HIS A O 455 C CB . HIS A 58 ? 0.3486 0.2994 0.3322 0.0164 0.0327 0.0538 110 HIS A CB 456 C CG . HIS A 58 ? 0.4224 0.3628 0.4077 0.0187 0.0366 0.0607 110 HIS A CG 457 N ND1 . HIS A 58 ? 0.4637 0.4022 0.4446 0.0252 0.0347 0.0654 110 HIS A ND1 458 C CD2 . HIS A 58 ? 0.4658 0.3975 0.4574 0.0155 0.0425 0.0637 110 HIS A CD2 459 C CE1 . HIS A 58 ? 0.4635 0.3914 0.4478 0.0258 0.0395 0.0714 110 HIS A CE1 460 N NE2 . HIS A 58 ? 0.4709 0.3943 0.4621 0.0199 0.0446 0.0706 110 HIS A NE2 461 N N . LEU A 59 ? 0.3094 0.2628 0.3107 0.0101 0.0279 0.0387 111 LEU A N 462 C CA . LEU A 59 ? 0.3205 0.2710 0.3299 0.0082 0.0278 0.0340 111 LEU A CA 463 C C . LEU A 59 ? 0.3403 0.2951 0.3504 0.0113 0.0240 0.0311 111 LEU A C 464 O O . LEU A 59 ? 0.3280 0.2785 0.3425 0.0133 0.0240 0.0306 111 LEU A O 465 C CB . LEU A 59 ? 0.3339 0.2868 0.3470 0.0032 0.0283 0.0286 111 LEU A CB 466 C CG . LEU A 59 ? 0.4106 0.3649 0.4291 0.0021 0.0265 0.0219 111 LEU A CG 467 C CD1 . LEU A 59 ? 0.4340 0.3808 0.4600 0.0022 0.0281 0.0204 111 LEU A CD1 468 C CD2 . LEU A 59 ? 0.4599 0.4184 0.4791 -0.0016 0.0262 0.0176 111 LEU A CD2 469 N N . LEU A 60 ? 0.2985 0.2616 0.3047 0.0121 0.0210 0.0295 112 LEU A N 470 C CA . LEU A 60 ? 0.2922 0.2604 0.3006 0.0147 0.0179 0.0267 112 LEU A CA 471 C C . LEU A 60 ? 0.3239 0.2897 0.3322 0.0201 0.0166 0.0301 112 LEU A C 472 O O . LEU A 60 ? 0.3201 0.2877 0.3327 0.0222 0.0152 0.0275 112 LEU A O 473 C CB . LEU A 60 ? 0.3031 0.2803 0.3099 0.0141 0.0154 0.0242 112 LEU A CB 474 C CG . LEU A 60 ? 0.3847 0.3645 0.3927 0.0097 0.0162 0.0205 112 LEU A CG 475 C CD1 . LEU A 60 ? 0.4016 0.3880 0.4073 0.0090 0.0144 0.0197 112 LEU A CD1 476 C CD2 . LEU A 60 ? 0.4318 0.4138 0.4444 0.0092 0.0161 0.0167 112 LEU A CD2 477 N N A SER A 61 ? 0.3000 0.2616 0.3033 0.0227 0.0176 0.0360 113 SER A N 478 N N B SER A 61 ? 0.2807 0.2424 0.2839 0.0227 0.0175 0.0360 113 SER A N 479 C CA A SER A 61 ? 0.3165 0.2748 0.3188 0.0285 0.0165 0.0403 113 SER A CA 480 C CA B SER A 61 ? 0.2875 0.2461 0.2899 0.0285 0.0164 0.0401 113 SER A CA 481 C C A SER A 61 ? 0.3618 0.3123 0.3714 0.0289 0.0183 0.0397 113 SER A C 482 C C B SER A 61 ? 0.3497 0.3001 0.3591 0.0290 0.0183 0.0398 113 SER A C 483 O O A SER A 61 ? 0.3738 0.3230 0.3850 0.0338 0.0166 0.0410 113 SER A O 484 O O B SER A 61 ? 0.3632 0.3121 0.3743 0.0339 0.0167 0.0413 113 SER A O 485 C CB A SER A 61 ? 0.3986 0.3528 0.3930 0.0313 0.0182 0.0478 113 SER A CB 486 C CB B SER A 61 ? 0.3308 0.2867 0.3248 0.0318 0.0173 0.0474 113 SER A CB 487 O OG A SER A 61 ? 0.5719 0.5345 0.5591 0.0333 0.0153 0.0479 113 SER A OG 488 O OG B SER A 61 ? 0.3504 0.2966 0.3447 0.0298 0.0225 0.0520 113 SER A OG 489 N N . SER A 62 ? 0.2947 0.2408 0.3091 0.0241 0.0212 0.0367 114 SER A N 490 C CA . SER A 62 ? 0.2968 0.2356 0.3190 0.0240 0.0229 0.0347 114 SER A CA 491 C C . SER A 62 ? 0.3183 0.2619 0.3454 0.0222 0.0215 0.0267 114 SER A C 492 O O . SER A 62 ? 0.3436 0.2824 0.3772 0.0222 0.0225 0.0233 114 SER A O 493 C CB . SER A 62 ? 0.3813 0.3115 0.4066 0.0204 0.0272 0.0369 114 SER A CB 494 O OG . SER A 62 ? 0.4638 0.3977 0.4898 0.0151 0.0279 0.0325 114 SER A OG 495 N N . VAL A 63 ? 0.2403 0.1931 0.2645 0.0209 0.0196 0.0238 115 VAL A N 496 C CA . VAL A 63 ? 0.2027 0.1609 0.2298 0.0198 0.0189 0.0174 115 VAL A CA 497 C C . VAL A 63 ? 0.2559 0.2203 0.2840 0.0236 0.0167 0.0167 115 VAL A C 498 O O . VAL A 63 ? 0.2548 0.2235 0.2799 0.0252 0.0148 0.0195 115 VAL A O 499 C CB . VAL A 63 ? 0.2529 0.2165 0.2770 0.0156 0.0190 0.0151 115 VAL A CB 500 C CG1 . VAL A 63 ? 0.2481 0.2169 0.2740 0.0153 0.0189 0.0097 115 VAL A CG1 501 C CG2 . VAL A 63 ? 0.2577 0.2163 0.2817 0.0118 0.0209 0.0153 115 VAL A CG2 502 N N . LYS A 64 ? 0.2004 0.1664 0.2330 0.0251 0.0169 0.0123 116 LYS A N 503 C CA . LYS A 64 ? 0.2029 0.1755 0.2382 0.0286 0.0154 0.0112 116 LYS A CA 504 C C . LYS A 64 ? 0.2335 0.2132 0.2703 0.0271 0.0166 0.0066 116 LYS A C 505 O O . LYS A 64 ? 0.2281 0.2143 0.2684 0.0293 0.0162 0.0053 116 LYS A O 506 C CB . LYS A 64 ? 0.2168 0.1848 0.2566 0.0334 0.0149 0.0115 116 LYS A CB 507 C CG . LYS A 64 ? 0.2364 0.1980 0.2743 0.0361 0.0139 0.0176 116 LYS A CG 508 C CD . LYS A 64 ? 0.2453 0.2132 0.2791 0.0380 0.0110 0.0209 116 LYS A CD 509 C CE . LYS A 64 ? 0.2917 0.2530 0.3206 0.0406 0.0107 0.0276 116 LYS A CE 510 N NZ . LYS A 64 ? 0.3261 0.2849 0.3490 0.0364 0.0124 0.0305 116 LYS A NZ 511 N N . HIS A 65 A 0.2085 0.1873 0.2429 0.0237 0.0182 0.0043 116 HIS A N 512 C CA . HIS A 65 A 0.2074 0.1924 0.2413 0.0227 0.0198 0.0011 116 HIS A CA 513 C C . HIS A 65 A 0.2832 0.2667 0.3131 0.0194 0.0206 -0.0003 116 HIS A C 514 O O . HIS A 65 A 0.2549 0.2323 0.2846 0.0184 0.0204 -0.0013 116 HIS A O 515 C CB . HIS A 65 A 0.2384 0.2255 0.2760 0.0261 0.0211 -0.0026 116 HIS A CB 516 C CG . HIS A 65 A 0.2764 0.2710 0.3137 0.0260 0.0235 -0.0045 116 HIS A CG 517 N ND1 . HIS A 65 A 0.3106 0.3063 0.3464 0.0276 0.0256 -0.0085 116 HIS A ND1 518 C CD2 . HIS A 65 A 0.2998 0.3007 0.3380 0.0245 0.0244 -0.0026 116 HIS A CD2 519 C CE1 . HIS A 65 A 0.3056 0.3080 0.3407 0.0273 0.0283 -0.0080 116 HIS A CE1 520 N NE2 . HIS A 65 A 0.3027 0.3082 0.3403 0.0252 0.0278 -0.0046 116 HIS A NE2 521 N N . PHE A 66 B 0.2268 0.2157 0.2544 0.0177 0.0217 -0.0004 116 PHE A N 522 C CA . PHE A 66 B 0.2172 0.2061 0.2407 0.0153 0.0224 -0.0017 116 PHE A CA 523 C C . PHE A 66 B 0.3171 0.3109 0.3390 0.0171 0.0246 -0.0040 116 PHE A C 524 O O . PHE A 66 B 0.3063 0.3049 0.3310 0.0186 0.0263 -0.0032 116 PHE A O 525 C CB . PHE A 66 B 0.2375 0.2284 0.2590 0.0121 0.0219 0.0013 116 PHE A CB 526 C CG . PHE A 66 B 0.2546 0.2416 0.2754 0.0101 0.0203 0.0036 116 PHE A CG 527 C CD1 . PHE A 66 B 0.2761 0.2575 0.2962 0.0090 0.0200 0.0026 116 PHE A CD1 528 C CD2 . PHE A 66 B 0.2984 0.2878 0.3195 0.0094 0.0192 0.0064 116 PHE A CD2 529 C CE1 . PHE A 66 B 0.3090 0.2870 0.3284 0.0071 0.0196 0.0054 116 PHE A CE1 530 C CE2 . PHE A 66 B 0.3284 0.3147 0.3473 0.0080 0.0182 0.0087 116 PHE A CE2 531 C CZ . PHE A 66 B 0.3090 0.2895 0.3268 0.0068 0.0188 0.0086 116 PHE A CZ 532 N N . GLU A 67 C 0.2663 0.2594 0.2840 0.0172 0.0248 -0.0068 116 GLU A N 533 C CA . GLU A 67 C 0.2664 0.2644 0.2800 0.0192 0.0272 -0.0080 116 GLU A CA 534 C C . GLU A 67 C 0.2708 0.2691 0.2798 0.0169 0.0269 -0.0065 116 GLU A C 535 O O . GLU A 67 C 0.2419 0.2370 0.2499 0.0156 0.0245 -0.0085 116 GLU A O 536 C CB . GLU A 67 C 0.2975 0.2954 0.3089 0.0228 0.0272 -0.0135 116 GLU A CB 537 C CG . GLU A 67 C 0.5131 0.5118 0.5291 0.0258 0.0283 -0.0152 116 GLU A CG 538 C CD . GLU A 67 C 0.8684 0.8661 0.8841 0.0294 0.0276 -0.0217 116 GLU A CD 539 O OE1 . GLU A 67 C 0.7001 0.6982 0.7110 0.0303 0.0266 -0.0257 116 GLU A OE1 540 O OE2 . GLU A 67 C 0.9020 0.8989 0.9228 0.0316 0.0279 -0.0234 116 GLU A OE2 541 N N . LYS A 68 ? 0.2652 0.2670 0.2732 0.0161 0.0291 -0.0028 117 LYS A N 542 C CA . LYS A 68 ? 0.2582 0.2598 0.2622 0.0144 0.0288 -0.0012 117 LYS A CA 543 C C . LYS A 68 ? 0.3036 0.3066 0.3005 0.0177 0.0290 -0.0038 117 LYS A C 544 O O . LYS A 68 ? 0.3404 0.3466 0.3340 0.0212 0.0319 -0.0039 117 LYS A O 545 C CB . LYS A 68 ? 0.3012 0.3055 0.3075 0.0128 0.0315 0.0033 117 LYS A CB 546 C CG . LYS A 68 ? 0.4030 0.4070 0.4159 0.0098 0.0301 0.0049 117 LYS A CG 547 C CD . LYS A 68 ? 0.4765 0.4838 0.4940 0.0084 0.0329 0.0080 117 LYS A CD 548 C CE . LYS A 68 ? 0.4130 0.4196 0.4280 0.0072 0.0338 0.0102 117 LYS A CE 549 N NZ . LYS A 68 ? 0.5514 0.5604 0.5738 0.0052 0.0362 0.0127 117 LYS A NZ 550 N N . VAL A 69 ? 0.2540 0.2550 0.2483 0.0170 0.0260 -0.0063 118 VAL A N 551 C CA . VAL A 69 ? 0.2500 0.2529 0.2377 0.0206 0.0248 -0.0100 118 VAL A CA 552 C C . VAL A 69 ? 0.3015 0.3052 0.2853 0.0200 0.0247 -0.0069 118 VAL A C 553 O O . VAL A 69 ? 0.2840 0.2853 0.2715 0.0162 0.0230 -0.0057 118 VAL A O 554 C CB . VAL A 69 ? 0.2920 0.2926 0.2822 0.0204 0.0209 -0.0167 118 VAL A CB 555 C CG1 . VAL A 69 ? 0.2948 0.2983 0.2789 0.0241 0.0184 -0.0216 118 VAL A CG1 556 C CG2 . VAL A 69 ? 0.2910 0.2900 0.2855 0.0215 0.0211 -0.0198 118 VAL A CG2 557 N N . LYS A 70 ? 0.2630 0.2698 0.2391 0.0242 0.0266 -0.0053 119 LYS A N 558 C CA . LYS A 70 ? 0.2439 0.2509 0.2158 0.0246 0.0265 -0.0018 119 LYS A CA 559 C C . LYS A 70 ? 0.2894 0.2968 0.2589 0.0257 0.0214 -0.0071 119 LYS A C 560 O O . LYS A 70 ? 0.3055 0.3159 0.2672 0.0309 0.0201 -0.0095 119 LYS A O 561 C CB . LYS A 70 ? 0.2416 0.2514 0.2058 0.0293 0.0310 0.0028 119 LYS A CB 562 C CG . LYS A 70 ? 0.3806 0.3892 0.3427 0.0292 0.0323 0.0085 119 LYS A CG 563 C CD . LYS A 70 ? 0.4117 0.4222 0.3666 0.0338 0.0381 0.0146 119 LYS A CD 564 C CE . LYS A 70 ? 0.5711 0.5808 0.5338 0.0306 0.0440 0.0200 119 LYS A CE 565 N NZ . LYS A 70 ? 0.6790 0.6908 0.6360 0.0350 0.0508 0.0257 119 LYS A NZ 566 N N . ILE A 71 ? 0.2252 0.2299 0.2015 0.0212 0.0187 -0.0090 120 ILE A N 567 C CA . ILE A 71 ? 0.2093 0.2147 0.1863 0.0215 0.0140 -0.0148 120 ILE A CA 568 C C . ILE A 71 ? 0.2737 0.2813 0.2457 0.0240 0.0122 -0.0138 120 ILE A C 569 O O . ILE A 71 ? 0.2768 0.2869 0.2472 0.0266 0.0082 -0.0196 120 ILE A O 570 C CB . ILE A 71 ? 0.2245 0.2265 0.2109 0.0159 0.0126 -0.0168 120 ILE A CB 571 C CG1 . ILE A 71 ? 0.2256 0.2256 0.2152 0.0119 0.0139 -0.0116 120 ILE A CG1 572 C CG2 . ILE A 71 ? 0.2424 0.2420 0.2332 0.0149 0.0137 -0.0183 120 ILE A CG2 573 C CD1 . ILE A 71 ? 0.2638 0.2610 0.2611 0.0071 0.0130 -0.0130 120 ILE A CD1 574 N N . LEU A 72 ? 0.2392 0.2456 0.2101 0.0231 0.0150 -0.0071 121 LEU A N 575 C CA . LEU A 72 ? 0.2379 0.2450 0.2052 0.0251 0.0136 -0.0051 121 LEU A CA 576 C C . LEU A 72 ? 0.2705 0.2767 0.2334 0.0271 0.0185 0.0029 121 LEU A C 577 O O . LEU A 72 ? 0.2526 0.2561 0.2207 0.0234 0.0207 0.0073 121 LEU A O 578 C CB . LEU A 72 ? 0.2318 0.2371 0.2069 0.0202 0.0117 -0.0058 121 LEU A CB 579 C CG . LEU A 72 ? 0.2786 0.2847 0.2600 0.0177 0.0077 -0.0129 121 LEU A CG 580 C CD1 . LEU A 72 ? 0.2602 0.2643 0.2489 0.0125 0.0077 -0.0119 121 LEU A CD1 581 C CD2 . LEU A 72 ? 0.2884 0.2986 0.2661 0.0224 0.0032 -0.0187 121 LEU A CD2 582 N N . PRO A 73 ? 0.2521 0.2607 0.2058 0.0329 0.0205 0.0045 122 PRO A N 583 C CA . PRO A 73 ? 0.2621 0.2695 0.2118 0.0351 0.0263 0.0129 122 PRO A CA 584 C C . PRO A 73 ? 0.3173 0.3222 0.2680 0.0349 0.0261 0.0174 122 PRO A C 585 O O . PRO A 73 ? 0.3068 0.3130 0.2541 0.0376 0.0217 0.0147 122 PRO A O 586 C CB . PRO A 73 ? 0.2986 0.3098 0.2357 0.0431 0.0269 0.0126 122 PRO A CB 587 C CG . PRO A 73 ? 0.3566 0.3709 0.2939 0.0436 0.0226 0.0035 122 PRO A CG 588 C CD . PRO A 73 ? 0.3002 0.3129 0.2466 0.0384 0.0175 -0.0015 122 PRO A CD 589 N N . LYS A 74 ? 0.2953 0.2968 0.2519 0.0316 0.0308 0.0237 123 LYS A N 590 C CA . LYS A 74 ? 0.3133 0.3114 0.2734 0.0306 0.0312 0.0279 123 LYS A CA 591 C C . LYS A 74 ? 0.3506 0.3488 0.3006 0.0377 0.0307 0.0314 123 LYS A C 592 O O . LYS A 74 ? 0.3503 0.3474 0.3016 0.0381 0.0274 0.0309 123 LYS A O 593 C CB . LYS A 74 ? 0.3809 0.3759 0.3495 0.0267 0.0373 0.0337 123 LYS A CB 594 C CG . LYS A 74 ? 0.5663 0.5578 0.5441 0.0227 0.0372 0.0354 123 LYS A CG 595 C CD . LYS A 74 ? 0.6263 0.6154 0.6131 0.0196 0.0434 0.0405 123 LYS A CD 596 C CE . LYS A 74 ? 0.8331 0.8236 0.8303 0.0135 0.0424 0.0362 123 LYS A CE 597 N NZ . LYS A 74 ? 0.9355 0.9243 0.9437 0.0103 0.0476 0.0398 123 LYS A NZ 598 N N . ASP A 75 ? 0.3140 0.3143 0.2532 0.0439 0.0335 0.0343 125 ASP A N 599 C CA . ASP A 75 ? 0.3213 0.3223 0.2485 0.0520 0.0333 0.0384 125 ASP A CA 600 C C . ASP A 75 ? 0.3730 0.3778 0.2953 0.0558 0.0250 0.0312 125 ASP A C 601 O O . ASP A 75 ? 0.3755 0.3805 0.2900 0.0621 0.0232 0.0340 125 ASP A O 602 C CB . ASP A 75 ? 0.3448 0.3482 0.2606 0.0582 0.0383 0.0424 125 ASP A CB 603 C CG . ASP A 75 ? 0.4788 0.4882 0.3889 0.0605 0.0343 0.0338 125 ASP A CG 604 O OD1 . ASP A 75 ? 0.4850 0.4949 0.4022 0.0555 0.0354 0.0303 125 ASP A OD1 605 O OD2 . ASP A 75 ? 0.4859 0.4997 0.3846 0.0678 0.0299 0.0303 125 ASP A OD2 606 N N . ARG A 76 ? 0.3194 0.3272 0.2473 0.0519 0.0199 0.0218 126 ARG A N 607 C CA . ARG A 76 ? 0.3299 0.3420 0.2559 0.0546 0.0122 0.0137 126 ARG A CA 608 C C . ARG A 76 ? 0.3528 0.3632 0.2845 0.0533 0.0092 0.0141 126 ARG A C 609 O O . ARG A 76 ? 0.3256 0.3397 0.2540 0.0577 0.0034 0.0097 126 ARG A O 610 C CB . ARG A 76 ? 0.3617 0.3764 0.2947 0.0501 0.0086 0.0042 126 ARG A CB 611 C CG . ARG A 76 ? 0.6148 0.6331 0.5406 0.0539 0.0091 0.0009 126 ARG A CG 612 C CD . ARG A 76 ? 0.8809 0.9017 0.8136 0.0508 0.0045 -0.0095 126 ARG A CD 613 N NE . ARG A 76 ? 1.0152 1.0406 0.9401 0.0565 0.0032 -0.0147 126 ARG A NE 614 C CZ . ARG A 76 ? 1.2145 1.2458 1.1333 0.0628 -0.0026 -0.0219 126 ARG A CZ 615 N NH1 . ARG A 76 ? 1.0181 1.0514 0.9382 0.0644 -0.0078 -0.0245 126 ARG A NH1 616 N NH2 . ARG A 76 ? 1.1056 1.1414 1.0174 0.0681 -0.0036 -0.0272 126 ARG A NH2 617 N N . TRP A 77 ? 0.3197 0.3248 0.2604 0.0473 0.0128 0.0189 127 TRP A N 618 C CA . TRP A 77 ? 0.3169 0.3203 0.2643 0.0456 0.0103 0.0188 127 TRP A CA 619 C C . TRP A 77 ? 0.3818 0.3825 0.3222 0.0521 0.0120 0.0266 127 TRP A C 620 O O . TRP A 77 ? 0.3672 0.3625 0.3129 0.0499 0.0161 0.0330 127 TRP A O 621 C CB . TRP A 77 ? 0.2711 0.2706 0.2310 0.0370 0.0130 0.0193 127 TRP A CB 622 C CG . TRP A 77 ? 0.2662 0.2674 0.2318 0.0313 0.0120 0.0133 127 TRP A CG 623 C CD1 . TRP A 77 ? 0.2886 0.2882 0.2574 0.0272 0.0160 0.0149 127 TRP A CD1 624 C CD2 . TRP A 77 ? 0.2644 0.2689 0.2344 0.0290 0.0072 0.0053 127 TRP A CD2 625 N NE1 . TRP A 77 ? 0.2795 0.2807 0.2533 0.0230 0.0137 0.0089 127 TRP A NE1 626 C CE2 . TRP A 77 ? 0.2989 0.3028 0.2737 0.0237 0.0088 0.0031 127 TRP A CE2 627 C CE3 . TRP A 77 ? 0.2940 0.3020 0.2652 0.0308 0.0019 -0.0004 127 TRP A CE3 628 C CZ2 . TRP A 77 ? 0.3025 0.3082 0.2830 0.0203 0.0058 -0.0036 127 TRP A CZ2 629 C CZ3 . TRP A 77 ? 0.3114 0.3219 0.2896 0.0269 -0.0010 -0.0077 127 TRP A CZ3 630 C CH2 . TRP A 77 ? 0.3177 0.3266 0.3002 0.0217 0.0013 -0.0089 127 TRP A CH2 631 N N . THR A 78 ? 0.3653 0.3700 0.2940 0.0606 0.0086 0.0258 128 THR A N 632 C CA . THR A 78 ? 0.3662 0.3684 0.2859 0.0683 0.0106 0.0343 128 THR A CA 633 C C . THR A 78 ? 0.4101 0.4093 0.3354 0.0689 0.0083 0.0361 128 THR A C 634 O O . THR A 78 ? 0.4185 0.4129 0.3395 0.0735 0.0118 0.0452 128 THR A O 635 C CB . THR A 78 ? 0.4501 0.4582 0.3539 0.0785 0.0073 0.0330 128 THR A CB 636 O OG1 . THR A 78 ? 0.4483 0.4627 0.3535 0.0805 -0.0016 0.0230 128 THR A OG1 637 C CG2 . THR A 78 ? 0.4638 0.4747 0.3613 0.0789 0.0102 0.0316 128 THR A CG2 638 N N . GLN A 79 ? 0.3405 0.3424 0.2758 0.0644 0.0029 0.0280 129 GLN A N 639 C CA . GLN A 79 ? 0.3471 0.3470 0.2884 0.0652 0.0004 0.0287 129 GLN A CA 640 C C . GLN A 79 ? 0.3554 0.3497 0.3106 0.0565 0.0042 0.0301 129 GLN A C 641 O O . GLN A 79 ? 0.3376 0.3301 0.2994 0.0562 0.0026 0.0299 129 GLN A O 642 C CB . GLN A 79 ? 0.3689 0.3760 0.3129 0.0666 -0.0079 0.0185 129 GLN A CB 643 C CG . GLN A 79 ? 0.5465 0.5604 0.4783 0.0761 -0.0134 0.0153 129 GLN A CG 644 C CD . GLN A 79 ? 0.8041 0.8256 0.7430 0.0758 -0.0214 0.0039 129 GLN A CD 645 O OE1 . GLN A 79 ? 0.7167 0.7423 0.6618 0.0706 -0.0233 -0.0044 129 GLN A OE1 646 N NE2 . GLN A 79 ? 0.7303 0.7536 0.6700 0.0811 -0.0258 0.0035 129 GLN A NE2 647 N N . HIS A 80 ? 0.2756 0.2678 0.2350 0.0500 0.0089 0.0310 130 HIS A N 648 C CA . HIS A 80 ? 0.2450 0.2333 0.2171 0.0421 0.0119 0.0310 130 HIS A CA 649 C C . HIS A 80 ? 0.3002 0.2829 0.2737 0.0402 0.0193 0.0389 130 HIS A C 650 O O . HIS A 80 ? 0.3005 0.2833 0.2657 0.0433 0.0225 0.0429 130 HIS A O 651 C CB . HIS A 80 ? 0.2321 0.2244 0.2102 0.0354 0.0098 0.0229 130 HIS A CB 652 C CG . HIS A 80 ? 0.2781 0.2755 0.2582 0.0358 0.0035 0.0151 130 HIS A CG 653 N ND1 . HIS A 80 ? 0.2978 0.3006 0.2709 0.0404 -0.0008 0.0107 130 HIS A ND1 654 C CD2 . HIS A 80 ? 0.2911 0.2895 0.2801 0.0328 0.0012 0.0109 130 HIS A CD2 655 C CE1 . HIS A 80 ? 0.2892 0.2961 0.2683 0.0396 -0.0056 0.0038 130 HIS A CE1 656 N NE2 . HIS A 80 ? 0.2823 0.2867 0.2707 0.0351 -0.0043 0.0040 130 HIS A NE2 657 N N . THR A 81 ? 0.2372 0.2155 0.2221 0.0352 0.0220 0.0403 131 THR A N 658 C CA . THR A 81 ? 0.2344 0.2082 0.2250 0.0318 0.0287 0.0457 131 THR A CA 659 C C . THR A 81 ? 0.2557 0.2330 0.2502 0.0257 0.0287 0.0405 131 THR A C 660 O O . THR A 81 ? 0.2450 0.2256 0.2433 0.0220 0.0246 0.0334 131 THR A O 661 C CB . THR A 81 ? 0.2490 0.2171 0.2513 0.0294 0.0307 0.0481 131 THR A CB 662 O OG1 . THR A 81 ? 0.2946 0.2591 0.2924 0.0360 0.0306 0.0535 131 THR A OG1 663 C CG2 . THR A 81 ? 0.2459 0.2098 0.2574 0.0253 0.0376 0.0526 131 THR A CG2 664 N N . THR A 82 ? 0.2312 0.2081 0.2243 0.0250 0.0335 0.0441 132 THR A N 665 C CA . THR A 82 ? 0.2184 0.1986 0.2146 0.0201 0.0335 0.0396 132 THR A CA 666 C C . THR A 82 ? 0.2774 0.2552 0.2839 0.0157 0.0389 0.0425 132 THR A C 667 O O . THR A 82 ? 0.2806 0.2612 0.2899 0.0123 0.0391 0.0395 132 THR A O 668 C CB . THR A 82 ? 0.3234 0.3071 0.3085 0.0239 0.0336 0.0397 132 THR A CB 669 O OG1 . THR A 82 ? 0.3478 0.3291 0.3281 0.0279 0.0397 0.0477 132 THR A OG1 670 C CG2 . THR A 82 ? 0.3214 0.3087 0.2974 0.0282 0.0278 0.0352 132 THR A CG2 671 N N . THR A 83 ? 0.2840 0.2569 0.2966 0.0161 0.0431 0.0483 133 THR A N 672 C CA . THR A 83 ? 0.2822 0.2527 0.3069 0.0121 0.0488 0.0510 133 THR A CA 673 C C . THR A 83 ? 0.3461 0.3171 0.3846 0.0061 0.0463 0.0449 133 THR A C 674 O O . THR A 83 ? 0.3464 0.3168 0.3966 0.0024 0.0499 0.0452 133 THR A O 675 C CB . THR A 83 ? 0.3439 0.3081 0.3706 0.0152 0.0548 0.0600 133 THR A CB 676 O OG1 . THR A 83 ? 0.3654 0.3261 0.3936 0.0168 0.0517 0.0597 133 THR A OG1 677 C CG2 . THR A 83 ? 0.4112 0.3753 0.4240 0.0217 0.0586 0.0671 133 THR A CG2 678 N N . GLY A 84 ? 0.2807 0.2534 0.3178 0.0055 0.0404 0.0391 134 GLY A N 679 C CA . GLY A 84 ? 0.2631 0.2369 0.3108 0.0009 0.0375 0.0328 134 GLY A CA 680 C C . GLY A 84 ? 0.2887 0.2659 0.3441 -0.0036 0.0381 0.0291 134 GLY A C 681 O O . GLY A 84 ? 0.2449 0.2259 0.2945 -0.0038 0.0371 0.0276 134 GLY A O 682 N N . GLY A 85 ? 0.2447 0.2207 0.3137 -0.0067 0.0394 0.0274 135 GLY A N 683 C CA . GLY A 85 ? 0.2599 0.2398 0.3381 -0.0106 0.0393 0.0230 135 GLY A CA 684 C C . GLY A 85 ? 0.3082 0.2887 0.3983 -0.0135 0.0367 0.0167 135 GLY A C 685 O O . GLY A 85 ? 0.3180 0.2947 0.4117 -0.0128 0.0364 0.0168 135 GLY A O 686 N N . SER A 86 ? 0.2426 0.2283 0.3391 -0.0163 0.0345 0.0108 136 SER A N 687 C CA . SER A 86 ? 0.2359 0.2233 0.3433 -0.0185 0.0316 0.0037 136 SER A CA 688 C C . SER A 86 ? 0.2468 0.2373 0.3688 -0.0214 0.0327 0.0003 136 SER A C 689 O O . SER A 86 ? 0.2130 0.2061 0.3346 -0.0217 0.0345 0.0022 136 SER A O 690 C CB . SER A 86 ? 0.2630 0.2554 0.3618 -0.0182 0.0259 -0.0022 136 SER A CB 691 O OG . SER A 86 ? 0.2682 0.2641 0.3758 -0.0197 0.0227 -0.0100 136 SER A OG 692 N N . ARG A 87 ? 0.2289 0.2198 0.3650 -0.0233 0.0313 -0.0057 137 ARG A N 693 C CA . ARG A 87 ? 0.2144 0.2095 0.3667 -0.0261 0.0313 -0.0110 137 ARG A CA 694 C C . ARG A 87 ? 0.2761 0.2801 0.4221 -0.0257 0.0258 -0.0173 137 ARG A C 695 O O . ARG A 87 ? 0.3055 0.3144 0.4608 -0.0271 0.0254 -0.0207 137 ARG A O 696 C CB . ARG A 87 ? 0.2532 0.2470 0.4228 -0.0281 0.0306 -0.0173 137 ARG A CB 697 C CG . ARG A 87 ? 0.5398 0.5240 0.7163 -0.0281 0.0360 -0.0108 137 ARG A CG 698 C CD . ARG A 87 ? 0.7629 0.7453 0.9632 -0.0312 0.0383 -0.0151 137 ARG A CD 699 N NE . ARG A 87 ? 0.9483 0.9309 1.1597 -0.0335 0.0438 -0.0114 137 ARG A NE 700 C CZ . ARG A 87 ? 1.1516 1.1266 1.3666 -0.0335 0.0518 -0.0013 137 ARG A CZ 701 N NH1 . ARG A 87 ? 0.9872 0.9537 1.1951 -0.0310 0.0546 0.0062 137 ARG A NH1 702 N NH2 . ARG A 87 ? 0.9898 0.9661 1.2154 -0.0357 0.0571 0.0015 137 ARG A NH2 703 N N . ALA A 88 ? 0.2335 0.2392 0.3638 -0.0236 0.0219 -0.0183 138 ALA A N 704 C CA . ALA A 88 ? 0.2239 0.2367 0.3459 -0.0225 0.0173 -0.0224 138 ALA A CA 705 C C . ALA A 88 ? 0.3202 0.3341 0.4378 -0.0221 0.0193 -0.0178 138 ALA A C 706 O O . ALA A 88 ? 0.3456 0.3655 0.4619 -0.0214 0.0162 -0.0212 138 ALA A O 707 C CB . ALA A 88 ? 0.2227 0.2353 0.3293 -0.0206 0.0149 -0.0220 138 ALA A CB 708 N N . CYS A 89 ? 0.3075 0.3160 0.4219 -0.0218 0.0243 -0.0100 139 CYS A N 709 C CA . CYS A 89 ? 0.3076 0.3170 0.4174 -0.0210 0.0267 -0.0056 139 CYS A CA 710 C C . CYS A 89 ? 0.3285 0.3356 0.4509 -0.0225 0.0328 -0.0018 139 CYS A C 711 O O . CYS A 89 ? 0.2968 0.3017 0.4135 -0.0213 0.0369 0.0045 139 CYS A O 712 C CB . CYS A 89 ? 0.3349 0.3409 0.4282 -0.0187 0.0274 -0.0002 139 CYS A CB 713 S SG . CYS A 89 ? 0.3983 0.4061 0.4783 -0.0174 0.0220 -0.0036 139 CYS A SG 714 N N . ALA A 90 ? 0.3103 0.3179 0.4501 -0.0251 0.0336 -0.0056 140 ALA A N 715 C CA . ALA A 90 ? 0.3149 0.3195 0.4691 -0.0270 0.0402 -0.0018 140 ALA A CA 716 C C . ALA A 90 ? 0.3503 0.3593 0.5097 -0.0275 0.0432 -0.0005 140 ALA A C 717 O O . ALA A 90 ? 0.3491 0.3653 0.5099 -0.0274 0.0387 -0.0063 140 ALA A O 718 C CB . ALA A 90 ? 0.3361 0.3405 0.5100 -0.0299 0.0400 -0.0075 140 ALA A CB 719 N N . VAL A 91 ? 0.3014 0.3063 0.4631 -0.0275 0.0510 0.0075 141 VAL A N 720 C CA . VAL A 91 ? 0.2893 0.2980 0.4570 -0.0279 0.0554 0.0095 141 VAL A CA 721 C C . VAL A 91 ? 0.3623 0.3675 0.5488 -0.0307 0.0634 0.0131 141 VAL A C 722 O O . VAL A 91 ? 0.3357 0.3332 0.5189 -0.0298 0.0686 0.0205 141 VAL A O 723 C CB . VAL A 91 ? 0.3361 0.3435 0.4856 -0.0243 0.0581 0.0165 141 VAL A CB 724 C CG1 . VAL A 91 ? 0.3302 0.3420 0.4876 -0.0247 0.0633 0.0183 141 VAL A CG1 725 C CG2 . VAL A 91 ? 0.3350 0.3445 0.4672 -0.0218 0.0508 0.0134 141 VAL A CG2 726 N N . SER A 92 ? 0.3409 0.3521 0.5477 -0.0338 0.0646 0.0080 142 SER A N 727 C CA . SER A 92 ? 0.3459 0.3544 0.5741 -0.0372 0.0729 0.0109 142 SER A CA 728 C C . SER A 92 ? 0.4144 0.4146 0.6494 -0.0386 0.0743 0.0121 142 SER A C 729 O O . SER A 92 ? 0.4047 0.3973 0.6441 -0.0389 0.0829 0.0209 142 SER A O 730 C CB . SER A 92 ? 0.4224 0.4284 0.6464 -0.0358 0.0827 0.0213 142 SER A CB 731 O OG . SER A 92 ? 0.5943 0.6081 0.8151 -0.0346 0.0819 0.0194 142 SER A OG 732 N N . GLY A 93 ? 0.3705 0.3722 0.6048 -0.0388 0.0659 0.0038 143 GLY A N 733 C CA . GLY A 93 ? 0.3768 0.3718 0.6183 -0.0399 0.0656 0.0027 143 GLY A CA 734 C C . GLY A 93 ? 0.4147 0.4006 0.6385 -0.0366 0.0675 0.0115 143 GLY A C 735 O O . GLY A 93 ? 0.4515 0.4305 0.6823 -0.0372 0.0689 0.0124 143 GLY A O 736 N N . ASN A 94 ? 0.3320 0.3178 0.5337 -0.0329 0.0673 0.0174 144 ASN A N 737 C CA . ASN A 94 ? 0.3135 0.2920 0.4977 -0.0290 0.0688 0.0254 144 ASN A CA 738 C C . ASN A 94 ? 0.3095 0.2914 0.4744 -0.0264 0.0605 0.0213 144 ASN A C 739 O O . ASN A 94 ? 0.2681 0.2571 0.4280 -0.0265 0.0564 0.0167 144 ASN A O 740 C CB . ASN A 94 ? 0.3618 0.3373 0.5373 -0.0264 0.0768 0.0363 144 ASN A CB 741 C CG . ASN A 94 ? 0.6578 0.6289 0.8511 -0.0286 0.0868 0.0425 144 ASN A CG 742 O OD1 . ASN A 94 ? 0.5408 0.5044 0.7445 -0.0295 0.0901 0.0453 144 ASN A OD1 743 N ND2 . ASN A 94 ? 0.5975 0.5726 0.7951 -0.0294 0.0922 0.0450 144 ASN A ND2 744 N N . PRO A 95 ? 0.2687 0.2457 0.4230 -0.0239 0.0583 0.0233 145 PRO A N 745 C CA . PRO A 95 ? 0.2266 0.2070 0.3644 -0.0219 0.0512 0.0194 145 PRO A CA 746 C C . PRO A 95 ? 0.2743 0.2563 0.3956 -0.0190 0.0520 0.0241 145 PRO A C 747 O O . PRO A 95 ? 0.2952 0.2735 0.4116 -0.0167 0.0576 0.0321 145 PRO A O 748 C CB . PRO A 95 ? 0.2566 0.2309 0.3900 -0.0198 0.0502 0.0213 145 PRO A CB 749 C CG . PRO A 95 ? 0.3299 0.2986 0.4820 -0.0219 0.0550 0.0228 145 PRO A CG 750 C CD . PRO A 95 ? 0.2771 0.2454 0.4343 -0.0227 0.0620 0.0290 145 PRO A CD 751 N N . SER A 96 ? 0.2325 0.2202 0.3452 -0.0187 0.0467 0.0192 146 SER A N 752 C CA . SER A 96 ? 0.2082 0.1974 0.3065 -0.0161 0.0471 0.0227 146 SER A CA 753 C C . SER A 96 ? 0.2067 0.1985 0.2933 -0.0151 0.0406 0.0182 146 SER A C 754 O O . SER A 96 ? 0.1885 0.1801 0.2760 -0.0158 0.0369 0.0142 146 SER A O 755 C CB . SER A 96 ? 0.2508 0.2447 0.3551 -0.0173 0.0495 0.0221 146 SER A CB 756 O OG . SER A 96 ? 0.3316 0.3260 0.4242 -0.0144 0.0518 0.0266 146 SER A OG 757 N N . PHE A 97 ? 0.1822 0.1764 0.2582 -0.0134 0.0397 0.0188 147 PHE A N 758 C CA . PHE A 97 ? 0.1707 0.1665 0.2361 -0.0125 0.0346 0.0156 147 PHE A CA 759 C C . PHE A 97 ? 0.2016 0.2009 0.2621 -0.0119 0.0337 0.0147 147 PHE A C 760 O O . PHE A 97 ? 0.2057 0.2061 0.2690 -0.0115 0.0371 0.0171 147 PHE A O 761 C CB . PHE A 97 ? 0.2014 0.1935 0.2560 -0.0096 0.0345 0.0188 147 PHE A CB 762 C CG . PHE A 97 ? 0.1988 0.1921 0.2468 -0.0095 0.0296 0.0149 147 PHE A CG 763 C CD1 . PHE A 97 ? 0.2058 0.2001 0.2590 -0.0115 0.0268 0.0104 147 PHE A CD1 764 C CD2 . PHE A 97 ? 0.1986 0.1921 0.2358 -0.0074 0.0282 0.0152 147 PHE A CD2 765 C CE1 . PHE A 97 ? 0.1976 0.1934 0.2448 -0.0115 0.0232 0.0070 147 PHE A CE1 766 C CE2 . PHE A 97 ? 0.2211 0.2157 0.2540 -0.0078 0.0244 0.0116 147 PHE A CE2 767 C CZ . PHE A 97 ? 0.1940 0.1897 0.2317 -0.0098 0.0224 0.0081 147 PHE A CZ 768 N N . PHE A 98 ? 0.1854 0.1861 0.2383 -0.0115 0.0295 0.0117 148 PHE A N 769 C CA . PHE A 98 ? 0.1918 0.1947 0.2393 -0.0105 0.0284 0.0110 148 PHE A CA 770 C C . PHE A 98 ? 0.2077 0.2092 0.2497 -0.0081 0.0318 0.0151 148 PHE A C 771 O O . PHE A 98 ? 0.2408 0.2395 0.2766 -0.0063 0.0328 0.0175 148 PHE A O 772 C CB . PHE A 98 ? 0.1902 0.1928 0.2295 -0.0101 0.0246 0.0088 148 PHE A CB 773 C CG . PHE A 98 ? 0.1933 0.1981 0.2357 -0.0117 0.0215 0.0049 148 PHE A CG 774 C CD1 . PHE A 98 ? 0.2226 0.2311 0.2681 -0.0120 0.0195 0.0022 148 PHE A CD1 775 C CD2 . PHE A 98 ? 0.1916 0.1951 0.2331 -0.0123 0.0203 0.0035 148 PHE A CD2 776 C CE1 . PHE A 98 ? 0.2188 0.2300 0.2653 -0.0126 0.0164 -0.0016 148 PHE A CE1 777 C CE2 . PHE A 98 ? 0.2435 0.2496 0.2870 -0.0133 0.0176 -0.0004 148 PHE A CE2 778 C CZ . PHE A 98 ? 0.2216 0.2316 0.2667 -0.0133 0.0157 -0.0029 148 PHE A CZ 779 N N . ARG A 99 ? 0.1529 0.1568 0.1972 -0.0075 0.0336 0.0155 149 ARG A N 780 C CA . ARG A 99 ? 0.1611 0.1645 0.2008 -0.0049 0.0375 0.0190 149 ARG A CA 781 C C . ARG A 99 ? 0.2014 0.2032 0.2292 -0.0022 0.0358 0.0188 149 ARG A C 782 O O . ARG A 99 ? 0.2362 0.2372 0.2583 0.0006 0.0386 0.0216 149 ARG A O 783 C CB . ARG A 99 ? 0.1765 0.1835 0.2217 -0.0048 0.0396 0.0187 149 ARG A CB 784 C CG . ARG A 99 ? 0.3182 0.3281 0.3774 -0.0073 0.0415 0.0181 149 ARG A CG 785 C CD . ARG A 99 ? 0.4123 0.4199 0.4778 -0.0084 0.0460 0.0216 149 ARG A CD 786 N NE . ARG A 99 ? 0.3602 0.3711 0.4412 -0.0108 0.0489 0.0207 149 ARG A NE 787 C CZ . ARG A 99 ? 0.5278 0.5369 0.6181 -0.0122 0.0544 0.0242 149 ARG A CZ 788 N NH1 . ARG A 99 ? 0.3393 0.3430 0.4234 -0.0108 0.0576 0.0295 149 ARG A NH1 789 N NH2 . ARG A 99 ? 0.2951 0.3078 0.4017 -0.0148 0.0569 0.0225 149 ARG A NH2 790 N N . ASN A 100 ? 0.1846 0.1864 0.2092 -0.0028 0.0316 0.0154 150 ASN A N 791 C CA . ASN A 100 ? 0.1751 0.1757 0.1911 -0.0006 0.0299 0.0141 150 ASN A CA 792 C C . ASN A 100 ? 0.2060 0.2047 0.2179 -0.0006 0.0276 0.0132 150 ASN A C 793 O O . ASN A 100 ? 0.2237 0.2218 0.2300 0.0009 0.0257 0.0112 150 ASN A O 794 C CB . ASN A 100 ? 0.1885 0.1896 0.2046 -0.0012 0.0274 0.0113 150 ASN A CB 795 C CG . ASN A 100 ? 0.2422 0.2458 0.2628 -0.0006 0.0292 0.0117 150 ASN A CG 796 O OD1 . ASN A 100 ? 0.2512 0.2562 0.2726 0.0009 0.0328 0.0137 150 ASN A OD1 797 N ND2 . ASN A 100 ? 0.1663 0.1709 0.1900 -0.0014 0.0271 0.0101 150 ASN A ND2 798 N N . MET A 101 ? 0.1803 0.1782 0.1959 -0.0022 0.0275 0.0141 151 MET A N 799 C CA . MET A 101 ? 0.1634 0.1601 0.1766 -0.0023 0.0252 0.0128 151 MET A CA 800 C C . MET A 101 ? 0.2182 0.2133 0.2306 -0.0004 0.0269 0.0160 151 MET A C 801 O O . MET A 101 ? 0.2154 0.2097 0.2306 0.0001 0.0305 0.0197 151 MET A O 802 C CB . MET A 101 ? 0.1712 0.1685 0.1891 -0.0055 0.0229 0.0102 151 MET A CB 803 C CG . MET A 101 ? 0.2004 0.1990 0.2188 -0.0068 0.0215 0.0082 151 MET A CG 804 S SD . MET A 101 ? 0.2444 0.2419 0.2568 -0.0056 0.0202 0.0065 151 MET A SD 805 C CE . MET A 101 ? 0.1980 0.1951 0.2100 -0.0071 0.0182 0.0042 151 MET A CE 806 N N . VAL A 102 ? 0.1987 0.1931 0.2075 0.0008 0.0244 0.0147 152 VAL A N 807 C CA . VAL A 102 ? 0.1843 0.1768 0.1915 0.0035 0.0255 0.0179 152 VAL A CA 808 C C . VAL A 102 ? 0.1899 0.1819 0.2010 0.0020 0.0229 0.0157 152 VAL A C 809 O O . VAL A 102 ? 0.1903 0.1839 0.1999 0.0015 0.0197 0.0117 152 VAL A O 810 C CB . VAL A 102 ? 0.2384 0.2317 0.2361 0.0084 0.0245 0.0183 152 VAL A CB 811 C CG1 . VAL A 102 ? 0.2408 0.2320 0.2357 0.0121 0.0258 0.0228 152 VAL A CG1 812 C CG2 . VAL A 102 ? 0.2463 0.2409 0.2393 0.0103 0.0266 0.0192 152 VAL A CG2 813 N N . TRP A 103 ? 0.1707 0.1604 0.1874 0.0014 0.0247 0.0181 153 TRP A N 814 C CA . TRP A 103 ? 0.1652 0.1545 0.1860 0.0005 0.0224 0.0157 153 TRP A CA 815 C C . TRP A 103 ? 0.2024 0.1901 0.2180 0.0051 0.0218 0.0183 153 TRP A C 816 O O . TRP A 103 ? 0.1993 0.1836 0.2152 0.0075 0.0247 0.0235 153 TRP A O 817 C CB . TRP A 103 ? 0.1833 0.1707 0.2138 -0.0020 0.0245 0.0166 153 TRP A CB 818 C CG . TRP A 103 ? 0.1984 0.1860 0.2344 -0.0034 0.0222 0.0129 153 TRP A CG 819 C CD1 . TRP A 103 ? 0.2217 0.2107 0.2550 -0.0025 0.0191 0.0099 153 TRP A CD1 820 C CD2 . TRP A 103 ? 0.1976 0.1851 0.2434 -0.0063 0.0226 0.0104 153 TRP A CD2 821 N NE1 . TRP A 103 ? 0.2072 0.1965 0.2476 -0.0043 0.0181 0.0065 153 TRP A NE1 822 C CE2 . TRP A 103 ? 0.2330 0.2216 0.2807 -0.0067 0.0198 0.0062 153 TRP A CE2 823 C CE3 . TRP A 103 ? 0.2310 0.2183 0.2851 -0.0087 0.0248 0.0106 153 TRP A CE3 824 C CZ2 . TRP A 103 ? 0.2456 0.2347 0.3025 -0.0088 0.0193 0.0024 153 TRP A CZ2 825 C CZ3 . TRP A 103 ? 0.2498 0.2375 0.3139 -0.0108 0.0239 0.0065 153 TRP A CZ3 826 C CH2 . TRP A 103 ? 0.2496 0.2384 0.3144 -0.0108 0.0211 0.0022 153 TRP A CH2 827 N N . LEU A 104 ? 0.1698 0.1599 0.1814 0.0066 0.0179 0.0146 154 LEU A N 828 C CA . LEU A 104 ? 0.1823 0.1718 0.1892 0.0117 0.0164 0.0163 154 LEU A CA 829 C C . LEU A 104 ? 0.1989 0.1866 0.2122 0.0115 0.0155 0.0160 154 LEU A C 830 O O . LEU A 104 ? 0.1913 0.1811 0.2100 0.0083 0.0136 0.0111 154 LEU A O 831 C CB . LEU A 104 ? 0.1805 0.1743 0.1822 0.0138 0.0121 0.0115 154 LEU A CB 832 C CG . LEU A 104 ? 0.2567 0.2524 0.2525 0.0144 0.0122 0.0104 154 LEU A CG 833 C CD1 . LEU A 104 ? 0.2863 0.2863 0.2806 0.0155 0.0078 0.0041 154 LEU A CD1 834 C CD2 . LEU A 104 ? 0.3198 0.3140 0.3080 0.0192 0.0148 0.0159 154 LEU A CD2 835 N N . THR A 105 ? 0.1890 0.1728 0.2016 0.0153 0.0173 0.0214 155 THR A N 836 C CA . THR A 105 ? 0.1833 0.1648 0.2019 0.0162 0.0164 0.0214 155 THR A CA 837 C C . THR A 105 ? 0.2433 0.2235 0.2557 0.0232 0.0148 0.0249 155 THR A C 838 O O . THR A 105 ? 0.2325 0.2136 0.2350 0.0278 0.0147 0.0279 155 THR A O 839 C CB . THR A 105 ? 0.2624 0.2391 0.2909 0.0131 0.0203 0.0240 155 THR A CB 840 O OG1 . THR A 105 ? 0.2259 0.1984 0.2520 0.0152 0.0251 0.0316 155 THR A OG1 841 C CG2 . THR A 105 ? 0.2049 0.1844 0.2402 0.0068 0.0203 0.0187 155 THR A CG2 842 N N . GLU A 106 ? 0.2291 0.2073 0.2471 0.0246 0.0134 0.0245 156 GLU A N 843 C CA . GLU A 106 ? 0.2566 0.2335 0.2697 0.0318 0.0113 0.0278 156 GLU A CA 844 C C . GLU A 106 ? 0.2982 0.2698 0.3041 0.0368 0.0156 0.0374 156 GLU A C 845 O O . GLU A 106 ? 0.2949 0.2618 0.3050 0.0340 0.0211 0.0421 156 GLU A O 846 C CB . GLU A 106 ? 0.2767 0.2511 0.2997 0.0318 0.0101 0.0262 156 GLU A CB 847 C CG . GLU A 106 ? 0.5303 0.4990 0.5521 0.0386 0.0107 0.0328 156 GLU A CG 848 C CD . GLU A 106 ? 0.7109 0.6707 0.7361 0.0389 0.0170 0.0416 156 GLU A CD 849 O OE1 . GLU A 106 ? 0.6157 0.5721 0.6532 0.0337 0.0196 0.0402 156 GLU A OE1 850 O OE2 . GLU A 106 ? 0.7653 0.7216 0.7816 0.0448 0.0194 0.0499 156 GLU A OE2 851 N N . LYS A 107 ? 0.2605 0.2334 0.2560 0.0445 0.0131 0.0401 157 LYS A N 852 C CA . LYS A 107 ? 0.2779 0.2460 0.2645 0.0509 0.0173 0.0501 157 LYS A CA 853 C C . LYS A 107 ? 0.3461 0.3127 0.3288 0.0589 0.0140 0.0529 157 LYS A C 854 O O . LYS A 107 ? 0.3334 0.3064 0.3127 0.0623 0.0072 0.0467 157 LYS A O 855 C CB . LYS A 107 ? 0.3243 0.2969 0.2978 0.0539 0.0173 0.0505 157 LYS A CB 856 C CG . LYS A 107 ? 0.4995 0.4682 0.4617 0.0613 0.0221 0.0611 157 LYS A CG 857 C CD . LYS A 107 ? 0.7246 0.7001 0.6719 0.0669 0.0191 0.0589 157 LYS A CD 858 C CE . LYS A 107 ? 0.9344 0.9078 0.8672 0.0768 0.0221 0.0685 157 LYS A CE 859 N NZ . LYS A 107 ? 1.0263 1.0079 0.9445 0.0836 0.0171 0.0641 157 LYS A NZ 860 N N . GLY A 108 ? 0.3486 0.3069 0.3333 0.0620 0.0188 0.0621 158 GLY A N 861 C CA . GLY A 108 ? 0.3650 0.3203 0.3461 0.0704 0.0164 0.0665 158 GLY A CA 862 C C . GLY A 108 ? 0.4124 0.3712 0.4024 0.0694 0.0099 0.0580 158 GLY A C 863 O O . GLY A 108 ? 0.4075 0.3701 0.3917 0.0766 0.0041 0.0564 158 GLY A O 864 N N . SER A 109 ? 0.3644 0.3228 0.3685 0.0607 0.0107 0.0520 159 SER A N 865 C CA . SER A 109 ? 0.3641 0.3257 0.3785 0.0585 0.0058 0.0436 159 SER A CA 866 C C . SER A 109 ? 0.4172 0.3895 0.4280 0.0588 -0.0011 0.0340 159 SER A C 867 O O . SER A 109 ? 0.4202 0.3963 0.4368 0.0601 -0.0057 0.0282 159 SER A O 868 C CB . SER A 109 ? 0.4270 0.3823 0.4460 0.0643 0.0055 0.0482 159 SER A CB 869 O OG . SER A 109 ? 0.6140 0.5706 0.6464 0.0603 0.0032 0.0406 159 SER A OG 870 N N . ASN A 110 ? 0.3620 0.3393 0.3648 0.0572 -0.0014 0.0320 160 ASN A N 871 C CA . ASN A 110 ? 0.3449 0.3318 0.3459 0.0567 -0.0072 0.0228 160 ASN A CA 872 C C . ASN A 110 ? 0.3262 0.3159 0.3271 0.0497 -0.0053 0.0192 160 ASN A C 873 O O . ASN A 110 ? 0.3001 0.2862 0.2959 0.0487 -0.0008 0.0246 160 ASN A O 874 C CB . ASN A 110 ? 0.3849 0.3761 0.3734 0.0659 -0.0117 0.0238 160 ASN A CB 875 C CG . ASN A 110 ? 0.7889 0.7800 0.7773 0.0740 -0.0159 0.0252 160 ASN A CG 876 O OD1 . ASN A 110 ? 0.7700 0.7576 0.7483 0.0825 -0.0155 0.0330 160 ASN A OD1 877 N ND2 . ASN A 110 ? 0.7058 0.7004 0.7052 0.0720 -0.0195 0.0181 160 ASN A ND2 878 N N . TYR A 111 ? 0.2678 0.2642 0.2745 0.0451 -0.0084 0.0101 161 TYR A N 879 C CA . TYR A 111 ? 0.2478 0.2469 0.2538 0.0392 -0.0070 0.0068 161 TYR A CA 880 C C . TYR A 111 ? 0.2952 0.3024 0.2991 0.0416 -0.0126 -0.0005 161 TYR A C 881 O O . TYR A 111 ? 0.2862 0.2980 0.2984 0.0385 -0.0150 -0.0075 161 TYR A O 882 C CB . TYR A 111 ? 0.2237 0.2222 0.2394 0.0307 -0.0042 0.0035 161 TYR A CB 883 C CG . TYR A 111 ? 0.2069 0.2069 0.2209 0.0255 -0.0023 0.0016 161 TYR A CG 884 C CD1 . TYR A 111 ? 0.1864 0.1821 0.2014 0.0213 0.0023 0.0053 161 TYR A CD1 885 C CD2 . TYR A 111 ? 0.2046 0.2104 0.2181 0.0244 -0.0051 -0.0045 161 TYR A CD2 886 C CE1 . TYR A 111 ? 0.1261 0.1233 0.1401 0.0170 0.0038 0.0036 161 TYR A CE1 887 C CE2 . TYR A 111 ? 0.2140 0.2204 0.2268 0.0198 -0.0032 -0.0059 161 TYR A CE2 888 C CZ . TYR A 111 ? 0.2433 0.2454 0.2557 0.0164 0.0011 -0.0016 161 TYR A CZ 889 O OH . TYR A 111 ? 0.2408 0.2436 0.2525 0.0125 0.0026 -0.0031 161 TYR A OH 890 N N . PRO A 112 ? 0.2690 0.2784 0.2624 0.0475 -0.0148 0.0005 162 PRO A N 891 C CA . PRO A 112 ? 0.2709 0.2886 0.2643 0.0496 -0.0206 -0.0079 162 PRO A CA 892 C C . PRO A 112 ? 0.3087 0.3285 0.3066 0.0422 -0.0191 -0.0131 162 PRO A C 893 O O . PRO A 112 ? 0.2844 0.2994 0.2834 0.0366 -0.0140 -0.0096 162 PRO A O 894 C CB . PRO A 112 ? 0.3234 0.3424 0.3032 0.0587 -0.0230 -0.0049 162 PRO A CB 895 C CG . PRO A 112 ? 0.3796 0.3910 0.3521 0.0587 -0.0166 0.0051 162 PRO A CG 896 C CD . PRO A 112 ? 0.3163 0.3212 0.2981 0.0527 -0.0119 0.0090 162 PRO A CD 897 N N . VAL A 113 ? 0.2689 0.2956 0.2710 0.0421 -0.0235 -0.0216 163 VAL A N 898 C CA . VAL A 113 ? 0.2642 0.2923 0.2714 0.0354 -0.0219 -0.0262 163 VAL A CA 899 C C . VAL A 113 ? 0.2988 0.3234 0.2966 0.0358 -0.0191 -0.0221 163 VAL A C 900 O O . VAL A 113 ? 0.3109 0.3371 0.2989 0.0424 -0.0213 -0.0212 163 VAL A O 901 C CB . VAL A 113 ? 0.3104 0.3464 0.3253 0.0352 -0.0269 -0.0364 163 VAL A CB 902 C CG1 . VAL A 113 ? 0.2966 0.3322 0.3183 0.0276 -0.0239 -0.0398 163 VAL A CG1 903 C CG2 . VAL A 113 ? 0.3171 0.3574 0.3419 0.0355 -0.0296 -0.0407 163 VAL A CG2 904 N N . ALA A 114 ? 0.2295 0.2500 0.2301 0.0292 -0.0142 -0.0198 164 ALA A N 905 C CA . ALA A 114 ? 0.2290 0.2467 0.2229 0.0287 -0.0111 -0.0165 164 ALA A CA 906 C C . ALA A 114 ? 0.2545 0.2754 0.2522 0.0258 -0.0126 -0.0235 164 ALA A C 907 O O . ALA A 114 ? 0.2697 0.2911 0.2768 0.0201 -0.0119 -0.0270 164 ALA A O 908 C CB . ALA A 114 ? 0.2359 0.2479 0.2317 0.0236 -0.0056 -0.0107 164 ALA A CB 909 N N . LYS A 115 ? 0.2351 0.2583 0.2261 0.0301 -0.0146 -0.0257 165 LYS A N 910 C CA . LYS A 115 ? 0.2398 0.2656 0.2349 0.0280 -0.0162 -0.0328 165 LYS A CA 911 C C . LYS A 115 ? 0.2669 0.2906 0.2538 0.0298 -0.0139 -0.0304 165 LYS A C 912 O O . LYS A 115 ? 0.2811 0.3050 0.2571 0.0357 -0.0137 -0.0263 165 LYS A O 913 C CB . LYS A 115 ? 0.2954 0.3285 0.2926 0.0327 -0.0228 -0.0417 165 LYS A CB 914 C CG . LYS A 115 ? 0.3799 0.4164 0.3871 0.0312 -0.0255 -0.0456 165 LYS A CG 915 C CD . LYS A 115 ? 0.4239 0.4686 0.4375 0.0341 -0.0321 -0.0565 165 LYS A CD 916 C CE . LYS A 115 ? 0.5250 0.5737 0.5489 0.0331 -0.0344 -0.0600 165 LYS A CE 917 N NZ . LYS A 115 ? 0.6291 0.6863 0.6625 0.0349 -0.0406 -0.0715 165 LYS A NZ 918 N N . GLY A 116 ? 0.2057 0.2275 0.1980 0.0248 -0.0119 -0.0325 166 GLY A N 919 C CA . GLY A 116 ? 0.2204 0.2405 0.2067 0.0259 -0.0097 -0.0311 166 GLY A CA 920 C C . GLY A 116 ? 0.2630 0.2827 0.2574 0.0219 -0.0099 -0.0370 166 GLY A C 921 O O . GLY A 116 ? 0.2595 0.2777 0.2640 0.0162 -0.0090 -0.0385 166 GLY A O 922 N N . SER A 117 ? 0.2197 0.2406 0.2100 0.0250 -0.0107 -0.0404 167 SER A N 923 C CA . SER A 117 ? 0.2213 0.2409 0.2203 0.0213 -0.0107 -0.0459 167 SER A CA 924 C C . SER A 117 ? 0.2553 0.2731 0.2486 0.0232 -0.0084 -0.0447 167 SER A C 925 O O . SER A 117 ? 0.2213 0.2410 0.2035 0.0287 -0.0081 -0.0421 167 SER A O 926 C CB . SER A 117 ? 0.3100 0.3350 0.3161 0.0229 -0.0163 -0.0566 167 SER A CB 927 O OG . SER A 117 ? 0.4320 0.4621 0.4294 0.0304 -0.0202 -0.0613 167 SER A OG 928 N N . TYR A 118 ? 0.1885 0.2026 0.1896 0.0189 -0.0066 -0.0465 168 TYR A N 929 C CA . TYR A 118 ? 0.1891 0.2014 0.1869 0.0204 -0.0046 -0.0462 168 TYR A CA 930 C C . TYR A 118 ? 0.2171 0.2275 0.2256 0.0179 -0.0057 -0.0535 168 TYR A C 931 O O . TYR A 118 ? 0.1974 0.2038 0.2157 0.0123 -0.0041 -0.0526 168 TYR A O 932 C CB . TYR A 118 ? 0.1780 0.1857 0.1730 0.0178 0.0007 -0.0368 168 TYR A CB 933 C CG . TYR A 118 ? 0.2003 0.2059 0.1949 0.0185 0.0029 -0.0371 168 TYR A CG 934 C CD1 . TYR A 118 ? 0.2407 0.2494 0.2267 0.0242 0.0032 -0.0379 168 TYR A CD1 935 C CD2 . TYR A 118 ? 0.2079 0.2087 0.2111 0.0142 0.0045 -0.0371 168 TYR A CD2 936 C CE1 . TYR A 118 ? 0.2074 0.2147 0.1938 0.0251 0.0051 -0.0388 168 TYR A CE1 937 C CE2 . TYR A 118 ? 0.2214 0.2203 0.2252 0.0154 0.0059 -0.0382 168 TYR A CE2 938 C CZ . TYR A 118 ? 0.2357 0.2381 0.2316 0.0208 0.0060 -0.0396 168 TYR A CZ 939 O OH . TYR A 118 ? 0.2447 0.2457 0.2419 0.0222 0.0075 -0.0413 168 TYR A OH 940 N N . ASN A 119 ? 0.2185 0.2317 0.2250 0.0223 -0.0080 -0.0602 169 ASN A N 941 C CA . ASN A 119 ? 0.2223 0.2334 0.2395 0.0206 -0.0091 -0.0680 169 ASN A CA 942 C C . ASN A 119 ? 0.2635 0.2697 0.2794 0.0201 -0.0051 -0.0639 169 ASN A C 943 O O . ASN A 119 ? 0.2731 0.2815 0.2788 0.0246 -0.0041 -0.0619 169 ASN A O 944 C CB . ASN A 119 ? 0.2525 0.2702 0.2693 0.0262 -0.0147 -0.0794 169 ASN A CB 945 C CG . ASN A 119 ? 0.4303 0.4457 0.4618 0.0237 -0.0162 -0.0887 169 ASN A CG 946 O OD1 . ASN A 119 ? 0.3166 0.3248 0.3574 0.0183 -0.0126 -0.0857 169 ASN A OD1 947 N ND2 . ASN A 119 ? 0.4491 0.4706 0.4832 0.0279 -0.0218 -0.1004 169 ASN A ND2 948 N N . ASN A 120 ? 0.2068 0.2064 0.2326 0.0148 -0.0024 -0.0618 170 ASN A N 949 C CA . ASN A 120 ? 0.2048 0.1997 0.2301 0.0145 0.0011 -0.0575 170 ASN A CA 950 C C . ASN A 120 ? 0.2338 0.2292 0.2612 0.0183 -0.0005 -0.0654 170 ASN A C 951 O O . ASN A 120 ? 0.2170 0.2078 0.2556 0.0161 -0.0004 -0.0697 170 ASN A O 952 C CB . ASN A 120 ? 0.1997 0.1874 0.2332 0.0088 0.0044 -0.0518 170 ASN A CB 953 C CG . ASN A 120 ? 0.2630 0.2465 0.2950 0.0092 0.0076 -0.0466 170 ASN A CG 954 O OD1 . ASN A 120 ? 0.2723 0.2583 0.2977 0.0132 0.0079 -0.0468 170 ASN A OD1 955 N ND2 . ASN A 120 ? 0.2177 0.1950 0.2559 0.0054 0.0102 -0.0420 170 ASN A ND2 956 N N . THR A 121 ? 0.2099 0.2108 0.2264 0.0241 -0.0012 -0.0667 171 THR A N 957 C CA . THR A 121 ? 0.2282 0.2312 0.2438 0.0290 -0.0025 -0.0742 171 THR A CA 958 C C . THR A 121 ? 0.2913 0.2924 0.3019 0.0303 0.0019 -0.0678 171 THR A C 959 O O . THR A 121 ? 0.2946 0.2988 0.3008 0.0353 0.0019 -0.0720 171 THR A O 960 C CB . THR A 121 ? 0.2706 0.2821 0.2768 0.0354 -0.0065 -0.0809 171 THR A CB 961 O OG1 . THR A 121 ? 0.3431 0.3580 0.3359 0.0380 -0.0042 -0.0726 171 THR A OG1 962 C CG2 . THR A 121 ? 0.2869 0.3014 0.2997 0.0346 -0.0116 -0.0886 171 THR A CG2 963 N N . SER A 122 ? 0.2385 0.2348 0.2508 0.0259 0.0055 -0.0583 172 SER A N 964 C CA . SER A 122 ? 0.2600 0.2551 0.2692 0.0267 0.0094 -0.0519 172 SER A CA 965 C C . SER A 122 ? 0.3325 0.3230 0.3494 0.0271 0.0102 -0.0549 172 SER A C 966 O O . SER A 122 ? 0.3347 0.3262 0.3488 0.0295 0.0128 -0.0520 172 SER A O 967 C CB . SER A 122 ? 0.2740 0.2665 0.2828 0.0224 0.0120 -0.0421 172 SER A CB 968 O OG . SER A 122 ? 0.2911 0.2770 0.3092 0.0180 0.0123 -0.0404 172 SER A OG 969 N N . GLY A 123 ? 0.2996 0.2851 0.3274 0.0247 0.0084 -0.0600 173 GLY A N 970 C CA . GLY A 123 ? 0.3001 0.2798 0.3367 0.0250 0.0091 -0.0625 173 GLY A CA 971 C C . GLY A 123 ? 0.3353 0.3069 0.3792 0.0204 0.0115 -0.0552 173 GLY A C 972 O O . GLY A 123 ? 0.3482 0.3137 0.4004 0.0206 0.0122 -0.0564 173 GLY A O 973 N N . GLU A 124 ? 0.2516 0.2229 0.2922 0.0169 0.0127 -0.0474 174 GLU A N 974 C CA . GLU A 124 ? 0.2546 0.2190 0.3003 0.0131 0.0148 -0.0402 174 GLU A CA 975 C C . GLU A 124 ? 0.2836 0.2485 0.3278 0.0090 0.0151 -0.0359 174 GLU A C 976 O O . GLU A 124 ? 0.2792 0.2499 0.3178 0.0092 0.0136 -0.0376 174 GLU A O 977 C CB . GLU A 124 ? 0.2790 0.2425 0.3216 0.0148 0.0169 -0.0333 174 GLU A CB 978 C CG . GLU A 124 ? 0.5011 0.4567 0.5523 0.0154 0.0178 -0.0330 174 GLU A CG 979 C CD . GLU A 124 ? 0.8245 0.7726 0.8801 0.0121 0.0196 -0.0262 174 GLU A CD 980 O OE1 . GLU A 124 ? 0.4977 0.4432 0.5579 0.0085 0.0200 -0.0271 174 GLU A OE1 981 O OE2 . GLU A 124 ? 0.7941 0.7395 0.8489 0.0135 0.0208 -0.0200 174 GLU A OE2 982 N N . GLN A 125 ? 0.2426 0.2014 0.2913 0.0058 0.0172 -0.0302 175 GLN A N 983 C CA . GLN A 125 ? 0.2332 0.1926 0.2802 0.0021 0.0180 -0.0256 175 GLN A CA 984 C C . GLN A 125 ? 0.2461 0.2114 0.2829 0.0032 0.0178 -0.0211 175 GLN A C 985 O O . GLN A 125 ? 0.2516 0.2182 0.2846 0.0058 0.0183 -0.0186 175 GLN A O 986 C CB . GLN A 125 ? 0.2728 0.2250 0.3240 -0.0001 0.0209 -0.0190 175 GLN A CB 987 C CG . GLN A 125 ? 0.4482 0.3996 0.5008 -0.0042 0.0226 -0.0158 175 GLN A CG 988 C CD . GLN A 125 ? 0.5741 0.5171 0.6330 -0.0058 0.0261 -0.0107 175 GLN A CD 989 O OE1 . GLN A 125 ? 0.4785 0.4170 0.5371 -0.0034 0.0271 -0.0069 175 GLN A OE1 990 N NE2 . GLN A 125 ? 0.3889 0.3296 0.4544 -0.0096 0.0283 -0.0107 175 GLN A NE2 991 N N . MET A 126 ? 0.2036 0.1725 0.2374 0.0011 0.0173 -0.0204 176 MET A N 992 C CA . MET A 126 ? 0.1930 0.1670 0.2187 0.0019 0.0172 -0.0166 176 MET A CA 993 C C . MET A 126 ? 0.2413 0.2151 0.2661 -0.0012 0.0182 -0.0116 176 MET A C 994 O O . MET A 126 ? 0.2441 0.2171 0.2723 -0.0039 0.0182 -0.0129 176 MET A O 995 C CB . MET A 126 ? 0.2160 0.1954 0.2376 0.0038 0.0153 -0.0211 176 MET A CB 996 C CG . MET A 126 ? 0.2623 0.2463 0.2766 0.0051 0.0159 -0.0173 176 MET A CG 997 S SD . MET A 126 ? 0.2945 0.2841 0.3031 0.0081 0.0138 -0.0217 176 MET A SD 998 C CE . MET A 126 ? 0.2494 0.2401 0.2565 0.0130 0.0136 -0.0269 176 MET A CE 999 N N . LEU A 127 ? 0.1866 0.1620 0.2074 -0.0008 0.0190 -0.0066 177 LEU A N 1000 C CA . LEU A 127 ? 0.1761 0.1525 0.1950 -0.0031 0.0195 -0.0027 177 LEU A CA 1001 C C . LEU A 127 ? 0.2183 0.1997 0.2337 -0.0032 0.0185 -0.0039 177 LEU A C 1002 O O . LEU A 127 ? 0.1952 0.1797 0.2077 -0.0011 0.0183 -0.0041 177 LEU A O 1003 C CB . LEU A 127 ? 0.1565 0.1332 0.1735 -0.0019 0.0200 0.0019 177 LEU A CB 1004 C CG . LEU A 127 ? 0.2254 0.2048 0.2398 -0.0032 0.0200 0.0051 177 LEU A CG 1005 C CD1 . LEU A 127 ? 0.2408 0.2175 0.2559 -0.0056 0.0211 0.0065 177 LEU A CD1 1006 C CD2 . LEU A 127 ? 0.2284 0.2093 0.2415 -0.0012 0.0195 0.0081 177 LEU A CD2 1007 N N . ILE A 128 ? 0.1745 0.1566 0.1906 -0.0055 0.0183 -0.0043 178 ILE A N 1008 C CA . ILE A 128 ? 0.1701 0.1563 0.1835 -0.0054 0.0173 -0.0049 178 ILE A CA 1009 C C . ILE A 128 ? 0.2014 0.1882 0.2150 -0.0078 0.0179 -0.0023 178 ILE A C 1010 O O . ILE A 128 ? 0.1975 0.1823 0.2136 -0.0098 0.0189 -0.0018 178 ILE A O 1011 C CB . ILE A 128 ? 0.2041 0.1916 0.2186 -0.0048 0.0155 -0.0099 178 ILE A CB 1012 C CG1 . ILE A 128 ? 0.2230 0.2103 0.2372 -0.0019 0.0146 -0.0138 178 ILE A CG1 1013 C CG2 . ILE A 128 ? 0.2203 0.2114 0.2318 -0.0042 0.0144 -0.0099 178 ILE A CG2 1014 C CD1 . ILE A 128 ? 0.2713 0.2607 0.2871 -0.0007 0.0121 -0.0199 178 ILE A CD1 1015 N N . ILE A 129 ? 0.1751 0.1648 0.1864 -0.0074 0.0176 -0.0007 179 ILE A N 1016 C CA . ILE A 129 ? 0.1421 0.1333 0.1535 -0.0092 0.0178 0.0008 179 ILE A CA 1017 C C . ILE A 129 ? 0.1898 0.1833 0.2011 -0.0090 0.0169 -0.0005 179 ILE A C 1018 O O . ILE A 129 ? 0.1819 0.1761 0.1913 -0.0070 0.0165 -0.0007 179 ILE A O 1019 C CB . ILE A 129 ? 0.1865 0.1792 0.1973 -0.0085 0.0181 0.0034 179 ILE A CB 1020 C CG1 . ILE A 129 ? 0.2078 0.1985 0.2184 -0.0078 0.0185 0.0051 179 ILE A CG1 1021 C CG2 . ILE A 129 ? 0.1927 0.1879 0.2042 -0.0098 0.0177 0.0038 179 ILE A CG2 1022 C CD1 . ILE A 129 ? 0.2665 0.2596 0.2775 -0.0064 0.0181 0.0065 179 ILE A CD1 1023 N N . TRP A 130 ? 0.1521 0.1466 0.1649 -0.0107 0.0168 -0.0012 180 TRP A N 1024 C CA . TRP A 130 ? 0.1657 0.1622 0.1788 -0.0102 0.0158 -0.0022 180 TRP A CA 1025 C C . TRP A 130 ? 0.1832 0.1811 0.1980 -0.0119 0.0161 -0.0019 180 TRP A C 1026 O O . TRP A 130 ? 0.1767 0.1745 0.1915 -0.0133 0.0171 -0.0013 180 TRP A O 1027 C CB . TRP A 130 ? 0.1477 0.1448 0.1622 -0.0098 0.0144 -0.0057 180 TRP A CB 1028 C CG . TRP A 130 ? 0.1669 0.1643 0.1854 -0.0124 0.0151 -0.0074 180 TRP A CG 1029 C CD1 . TRP A 130 ? 0.2062 0.2059 0.2274 -0.0136 0.0151 -0.0087 180 TRP A CD1 1030 C CD2 . TRP A 130 ? 0.1815 0.1769 0.2027 -0.0141 0.0166 -0.0079 180 TRP A CD2 1031 N NE1 . TRP A 130 ? 0.2280 0.2275 0.2531 -0.0160 0.0169 -0.0098 180 TRP A NE1 1032 C CE2 . TRP A 130 ? 0.2495 0.2459 0.2746 -0.0165 0.0181 -0.0088 180 TRP A CE2 1033 C CE3 . TRP A 130 ? 0.2261 0.2185 0.2472 -0.0137 0.0172 -0.0075 180 TRP A CE3 1034 C CZ2 . TRP A 130 ? 0.2587 0.2531 0.2882 -0.0186 0.0205 -0.0090 180 TRP A CZ2 1035 C CZ3 . TRP A 130 ? 0.2487 0.2385 0.2741 -0.0158 0.0193 -0.0075 180 TRP A CZ3 1036 C CH2 . TRP A 130 ? 0.2538 0.2444 0.2832 -0.0183 0.0212 -0.0079 180 TRP A CH2 1037 N N . GLY A 131 ? 0.1343 0.1334 0.1500 -0.0114 0.0155 -0.0022 181 GLY A N 1038 C CA . GLY A 131 ? 0.1403 0.1411 0.1582 -0.0127 0.0156 -0.0029 181 GLY A CA 1039 C C . GLY A 131 ? 0.1906 0.1928 0.2109 -0.0127 0.0148 -0.0052 181 GLY A C 1040 O O . GLY A 131 ? 0.1826 0.1846 0.2029 -0.0111 0.0136 -0.0058 181 GLY A O 1041 N N . VAL A 132 ? 0.1491 0.1533 0.1714 -0.0140 0.0152 -0.0067 182 VAL A N 1042 C CA . VAL A 132 ? 0.1538 0.1599 0.1795 -0.0139 0.0145 -0.0093 182 VAL A CA 1043 C C . VAL A 132 ? 0.1834 0.1903 0.2113 -0.0138 0.0143 -0.0099 182 VAL A C 1044 O O . VAL A 132 ? 0.1693 0.1778 0.1964 -0.0146 0.0148 -0.0103 182 VAL A O 1045 C CB . VAL A 132 ? 0.2062 0.2148 0.2335 -0.0155 0.0158 -0.0115 182 VAL A CB 1046 C CG1 . VAL A 132 ? 0.2069 0.2182 0.2386 -0.0151 0.0152 -0.0146 182 VAL A CG1 1047 C CG2 . VAL A 132 ? 0.2147 0.2222 0.2422 -0.0159 0.0160 -0.0116 182 VAL A CG2 1048 N N . HIS A 133 ? 0.1402 0.1462 0.1713 -0.0124 0.0133 -0.0101 183 HIS A N 1049 C CA . HIS A 133 ? 0.1299 0.1361 0.1652 -0.0124 0.0130 -0.0114 183 HIS A CA 1050 C C . HIS A 133 ? 0.1866 0.1958 0.2252 -0.0126 0.0127 -0.0154 183 HIS A C 1051 O O . HIS A 133 ? 0.1557 0.1656 0.1955 -0.0118 0.0121 -0.0165 183 HIS A O 1052 C CB . HIS A 133 ? 0.1547 0.1574 0.1926 -0.0107 0.0129 -0.0089 183 HIS A CB 1053 C CG . HIS A 133 ? 0.1911 0.1932 0.2357 -0.0111 0.0130 -0.0103 183 HIS A CG 1054 N ND1 . HIS A 133 ? 0.2236 0.2227 0.2728 -0.0095 0.0130 -0.0094 183 HIS A ND1 1055 C CD2 . HIS A 133 ? 0.2040 0.2081 0.2517 -0.0126 0.0129 -0.0129 183 HIS A CD2 1056 C CE1 . HIS A 133 ? 0.2191 0.2180 0.2754 -0.0105 0.0132 -0.0115 183 HIS A CE1 1057 N NE2 . HIS A 133 ? 0.2101 0.2125 0.2658 -0.0124 0.0128 -0.0143 183 HIS A NE2 1058 N N . HIS A 134 ? 0.1620 0.1739 0.2014 -0.0135 0.0130 -0.0180 184 HIS A N 1059 C CA . HIS A 134 ? 0.1472 0.1629 0.1890 -0.0135 0.0131 -0.0224 184 HIS A CA 1060 C C . HIS A 134 ? 0.1667 0.1819 0.2151 -0.0128 0.0118 -0.0251 184 HIS A C 1061 O O . HIS A 134 ? 0.1747 0.1913 0.2242 -0.0132 0.0112 -0.0271 184 HIS A O 1062 C CB . HIS A 134 ? 0.1499 0.1696 0.1869 -0.0143 0.0144 -0.0235 184 HIS A CB 1063 C CG . HIS A 134 ? 0.1931 0.2123 0.2251 -0.0152 0.0163 -0.0205 184 HIS A CG 1064 N ND1 . HIS A 134 ? 0.2087 0.2292 0.2424 -0.0158 0.0177 -0.0212 184 HIS A ND1 1065 C CD2 . HIS A 134 ? 0.2249 0.2426 0.2522 -0.0156 0.0170 -0.0171 184 HIS A CD2 1066 C CE1 . HIS A 134 ? 0.2155 0.2347 0.2459 -0.0168 0.0194 -0.0184 184 HIS A CE1 1067 N NE2 . HIS A 134 ? 0.2313 0.2486 0.2573 -0.0166 0.0191 -0.0156 184 HIS A NE2 1068 N N . PRO A 135 ? 0.1455 0.1584 0.1991 -0.0116 0.0111 -0.0255 185 PRO A N 1069 C CA . PRO A 135 ? 0.1532 0.1642 0.2145 -0.0111 0.0103 -0.0278 185 PRO A CA 1070 C C . PRO A 135 ? 0.1882 0.2038 0.2531 -0.0112 0.0097 -0.0343 185 PRO A C 1071 O O . PRO A 135 ? 0.1717 0.1921 0.2326 -0.0112 0.0102 -0.0370 185 PRO A O 1072 C CB . PRO A 135 ? 0.1785 0.1858 0.2433 -0.0090 0.0099 -0.0259 185 PRO A CB 1073 C CG . PRO A 135 ? 0.2526 0.2591 0.3108 -0.0085 0.0101 -0.0217 185 PRO A CG 1074 C CD . PRO A 135 ? 0.2034 0.2149 0.2568 -0.0103 0.0108 -0.0238 185 PRO A CD 1075 N N . ASN A 136 ? 0.1596 0.1736 0.2326 -0.0111 0.0088 -0.0370 186 ASN A N 1076 C CA . ASN A 136 ? 0.1503 0.1687 0.2280 -0.0108 0.0076 -0.0445 186 ASN A CA 1077 C C . ASN A 136 ? 0.2203 0.2396 0.3022 -0.0092 0.0075 -0.0481 186 ASN A C 1078 O O . ASN A 136 ? 0.2221 0.2470 0.3040 -0.0085 0.0071 -0.0543 186 ASN A O 1079 C CB . ASN A 136 ? 0.1794 0.1955 0.2666 -0.0114 0.0065 -0.0469 186 ASN A CB 1080 C CG . ASN A 136 ? 0.2416 0.2630 0.3344 -0.0108 0.0046 -0.0559 186 ASN A CG 1081 O OD1 . ASN A 136 ? 0.2176 0.2451 0.3048 -0.0106 0.0035 -0.0594 186 ASN A OD1 1082 N ND2 . ASN A 136 ? 0.2640 0.2832 0.3669 -0.0100 0.0041 -0.0600 186 ASN A ND2 1083 N N . ASP A 137 ? 0.1816 0.1957 0.2668 -0.0082 0.0077 -0.0444 187 ASP A N 1084 C CA . ASP A 137 ? 0.1732 0.1876 0.2641 -0.0062 0.0072 -0.0477 187 ASP A CA 1085 C C . ASP A 137 ? 0.1921 0.2023 0.2821 -0.0044 0.0071 -0.0422 187 ASP A C 1086 O O . ASP A 137 ? 0.1877 0.1943 0.2730 -0.0046 0.0076 -0.0359 187 ASP A O 1087 C CB . ASP A 137 ? 0.2083 0.2201 0.3108 -0.0055 0.0062 -0.0525 187 ASP A CB 1088 C CG . ASP A 137 ? 0.3892 0.3935 0.4977 -0.0061 0.0067 -0.0479 187 ASP A CG 1089 O OD1 . ASP A 137 ? 0.3994 0.3976 0.5083 -0.0047 0.0074 -0.0416 187 ASP A OD1 1090 O OD2 . ASP A 137 ? 0.4117 0.4167 0.5236 -0.0080 0.0064 -0.0503 187 ASP A OD2 1091 N N . GLU A 138 ? 0.1852 0.1968 0.2791 -0.0021 0.0064 -0.0450 188 GLU A N 1092 C CA . GLU A 138 ? 0.1912 0.2003 0.2842 0.0005 0.0055 -0.0409 188 GLU A CA 1093 C C . GLU A 138 ? 0.1979 0.1986 0.2945 0.0026 0.0052 -0.0353 188 GLU A C 1094 O O . GLU A 138 ? 0.1990 0.1970 0.2907 0.0046 0.0048 -0.0297 188 GLU A O 1095 C CB . GLU A 138 ? 0.2218 0.2355 0.3192 0.0026 0.0045 -0.0458 188 GLU A CB 1096 C CG . GLU A 138 ? 0.3009 0.3230 0.3941 0.0006 0.0059 -0.0495 188 GLU A CG 1097 C CD . GLU A 138 ? 0.6001 0.6280 0.6984 0.0023 0.0056 -0.0544 188 GLU A CD 1098 O OE1 . GLU A 138 ? 0.5757 0.6040 0.6815 0.0042 0.0050 -0.0592 188 GLU A OE1 1099 O OE2 . GLU A 138 ? 0.4204 0.4527 0.5163 0.0017 0.0062 -0.0541 188 GLU A OE2 1100 N N . THR A 139 ? 0.1862 0.1828 0.2913 0.0022 0.0057 -0.0370 189 THR A N 1101 C CA . THR A 139 ? 0.2041 0.1918 0.3135 0.0039 0.0067 -0.0307 189 THR A CA 1102 C C . THR A 139 ? 0.2393 0.2245 0.3411 0.0025 0.0084 -0.0237 189 THR A C 1103 O O . THR A 139 ? 0.2222 0.2027 0.3204 0.0053 0.0090 -0.0168 189 THR A O 1104 C CB . THR A 139 ? 0.3120 0.2956 0.4345 0.0033 0.0073 -0.0345 189 THR A CB 1105 O OG1 . THR A 139 ? 0.3773 0.3635 0.5060 0.0054 0.0056 -0.0408 189 THR A OG1 1106 C CG2 . THR A 139 ? 0.3314 0.3048 0.4598 0.0049 0.0095 -0.0270 189 THR A CG2 1107 N N . GLU A 140 ? 0.2223 0.2111 0.3210 -0.0011 0.0091 -0.0256 190 GLU A N 1108 C CA . GLU A 140 ? 0.2240 0.2118 0.3158 -0.0026 0.0106 -0.0202 190 GLU A CA 1109 C C . GLU A 140 ? 0.2234 0.2129 0.3044 -0.0008 0.0099 -0.0164 190 GLU A C 1110 O O . GLU A 140 ? 0.2077 0.1936 0.2839 0.0008 0.0110 -0.0100 190 GLU A O 1111 C CB . GLU A 140 ? 0.2474 0.2404 0.3379 -0.0062 0.0106 -0.0245 190 GLU A CB 1112 C CG . GLU A 140 ? 0.4706 0.4617 0.5589 -0.0079 0.0123 -0.0200 190 GLU A CG 1113 C CD . GLU A 140 ? 0.7682 0.7648 0.8511 -0.0103 0.0118 -0.0224 190 GLU A CD 1114 O OE1 . GLU A 140 ? 0.4325 0.4341 0.5170 -0.0113 0.0103 -0.0288 190 GLU A OE1 1115 O OE2 . GLU A 140 ? 0.7575 0.7533 0.8343 -0.0107 0.0129 -0.0178 190 GLU A OE2 1116 N N . GLN A 141 ? 0.1755 0.1709 0.2536 -0.0007 0.0082 -0.0208 191 GLN A N 1117 C CA . GLN A 141 ? 0.1525 0.1502 0.2229 0.0007 0.0071 -0.0188 191 GLN A CA 1118 C C . GLN A 141 ? 0.2075 0.2011 0.2770 0.0054 0.0061 -0.0142 191 GLN A C 1119 O O . GLN A 141 ? 0.2308 0.2235 0.2929 0.0070 0.0059 -0.0099 191 GLN A O 1120 C CB . GLN A 141 ? 0.1527 0.1573 0.2233 -0.0001 0.0060 -0.0247 191 GLN A CB 1121 C CG . GLN A 141 ? 0.1512 0.1586 0.2174 0.0017 0.0045 -0.0240 191 GLN A CG 1122 C CD . GLN A 141 ? 0.1943 0.2026 0.2533 -0.0004 0.0053 -0.0218 191 GLN A CD 1123 O OE1 . GLN A 141 ? 0.2001 0.2087 0.2573 -0.0035 0.0072 -0.0218 191 GLN A OE1 1124 N NE2 . GLN A 141 ? 0.1481 0.1569 0.2031 0.0018 0.0037 -0.0202 191 GLN A NE2 1125 N N . ARG A 142 ? 0.2016 0.1930 0.2780 0.0080 0.0052 -0.0154 192 ARG A N 1126 C CA . ARG A 142 ? 0.1814 0.1686 0.2568 0.0135 0.0040 -0.0106 192 ARG A CA 1127 C C . ARG A 142 ? 0.2143 0.1940 0.2873 0.0149 0.0067 -0.0025 192 ARG A C 1128 O O . ARG A 142 ? 0.2429 0.2205 0.3089 0.0193 0.0062 0.0031 192 ARG A O 1129 C CB . ARG A 142 ? 0.2016 0.1880 0.2858 0.0162 0.0025 -0.0139 192 ARG A CB 1130 C CG . ARG A 142 ? 0.2888 0.2836 0.3745 0.0157 0.0001 -0.0213 192 ARG A CG 1131 C CD . ARG A 142 ? 0.3983 0.3934 0.4926 0.0190 -0.0017 -0.0251 192 ARG A CD 1132 N NE . ARG A 142 ? 0.5227 0.5269 0.6188 0.0176 -0.0029 -0.0323 192 ARG A NE 1133 C CZ . ARG A 142 ? 0.7275 0.7351 0.8318 0.0179 -0.0033 -0.0386 192 ARG A CZ 1134 N NH1 . ARG A 142 ? 0.6929 0.6955 0.8052 0.0198 -0.0033 -0.0392 192 ARG A NH1 1135 N NH2 . ARG A 142 ? 0.5119 0.5282 0.6175 0.0164 -0.0035 -0.0444 192 ARG A NH2 1136 N N . THR A 143 ? 0.1888 0.1648 0.2679 0.0114 0.0097 -0.0019 193 THR A N 1137 C CA . THR A 143 ? 0.2048 0.1738 0.2837 0.0122 0.0133 0.0060 193 THR A CA 1138 C C . THR A 143 ? 0.2554 0.2261 0.3231 0.0121 0.0143 0.0101 193 THR A C 1139 O O . THR A 143 ? 0.2581 0.2246 0.3206 0.0157 0.0163 0.0174 193 THR A O 1140 C CB . THR A 143 ? 0.2815 0.2474 0.3717 0.0081 0.0161 0.0042 193 THR A CB 1141 O OG1 . THR A 143 ? 0.5514 0.5238 0.6412 0.0035 0.0150 -0.0022 193 THR A OG1 1142 C CG2 . THR A 143 ? 0.2700 0.2327 0.3719 0.0089 0.0155 0.0007 193 THR A CG2 1143 N N . LEU A 144 ? 0.1994 0.1762 0.2634 0.0085 0.0131 0.0055 194 LEU A N 1144 C CA . LEU A 144 ? 0.1952 0.1738 0.2499 0.0082 0.0139 0.0084 194 LEU A CA 1145 C C . LEU A 144 ? 0.2262 0.2082 0.2718 0.0119 0.0109 0.0083 194 LEU A C 1146 O O . LEU A 144 ? 0.2217 0.2029 0.2592 0.0146 0.0116 0.0128 194 LEU A O 1147 C CB . LEU A 144 ? 0.1935 0.1767 0.2488 0.0031 0.0139 0.0036 194 LEU A CB 1148 C CG . LEU A 144 ? 0.2481 0.2297 0.3120 -0.0006 0.0162 0.0025 194 LEU A CG 1149 C CD1 . LEU A 144 ? 0.2433 0.2305 0.3068 -0.0044 0.0150 -0.0032 194 LEU A CD1 1150 C CD2 . LEU A 144 ? 0.2857 0.2631 0.3498 -0.0005 0.0199 0.0087 194 LEU A CD2 1151 N N . TYR A 145 ? 0.1940 0.1804 0.2415 0.0121 0.0076 0.0026 195 TYR A N 1152 C CA . TYR A 145 ? 0.1892 0.1806 0.2304 0.0146 0.0044 0.0004 195 TYR A CA 1153 C C . TYR A 145 ? 0.2488 0.2417 0.2915 0.0195 0.0009 -0.0012 195 TYR A C 1154 O O . TYR A 145 ? 0.2550 0.2535 0.2956 0.0208 -0.0024 -0.0052 195 TYR A O 1155 C CB . TYR A 145 ? 0.1937 0.1908 0.2356 0.0098 0.0039 -0.0054 195 TYR A CB 1156 C CG . TYR A 145 ? 0.1894 0.1853 0.2304 0.0054 0.0068 -0.0043 195 TYR A CG 1157 C CD1 . TYR A 145 ? 0.2186 0.2125 0.2533 0.0059 0.0083 0.0001 195 TYR A CD1 1158 C CD2 . TYR A 145 ? 0.1766 0.1739 0.2229 0.0013 0.0079 -0.0077 195 TYR A CD2 1159 C CE1 . TYR A 145 ? 0.2176 0.2109 0.2525 0.0023 0.0107 0.0008 195 TYR A CE1 1160 C CE2 . TYR A 145 ? 0.1833 0.1799 0.2291 -0.0019 0.0100 -0.0068 195 TYR A CE2 1161 C CZ . TYR A 145 ? 0.1973 0.1920 0.2378 -0.0015 0.0113 -0.0026 195 TYR A CZ 1162 O OH . TYR A 145 ? 0.1876 0.1823 0.2285 -0.0044 0.0130 -0.0021 195 TYR A OH 1163 N N . GLN A 146 ? 0.2433 0.2314 0.2909 0.0221 0.0015 0.0015 196 GLN A N 1164 C CA . GLN A 146 ? 0.2427 0.2314 0.2928 0.0274 -0.0018 0.0006 196 GLN A CA 1165 C C . GLN A 146 ? 0.3133 0.3077 0.3715 0.0256 -0.0041 -0.0075 196 GLN A C 1166 O O . GLN A 146 ? 0.3085 0.3010 0.3737 0.0278 -0.0048 -0.0084 196 GLN A O 1167 C CB . GLN A 146 ? 0.2891 0.2794 0.3298 0.0341 -0.0049 0.0034 196 GLN A CB 1168 C CG . GLN A 146 ? 0.5742 0.5570 0.6084 0.0389 -0.0023 0.0130 196 GLN A CG 1169 C CD . GLN A 146 ? 0.7898 0.7660 0.8307 0.0421 -0.0012 0.0169 196 GLN A CD 1170 O OE1 . GLN A 146 ? 0.7046 0.6824 0.7483 0.0466 -0.0049 0.0147 196 GLN A OE1 1171 N NE2 . GLN A 146 ? 0.7339 0.7024 0.7781 0.0402 0.0039 0.0227 196 GLN A NE2 1172 N N . ASN A 147 ? 0.2510 0.2524 0.3086 0.0221 -0.0051 -0.0130 197 ASN A N 1173 C CA . ASN A 147 ? 0.2701 0.2776 0.3354 0.0204 -0.0064 -0.0203 197 ASN A CA 1174 C C . ASN A 147 ? 0.2828 0.2944 0.3497 0.0139 -0.0039 -0.0245 197 ASN A C 1175 O O . ASN A 147 ? 0.2412 0.2519 0.3026 0.0110 -0.0022 -0.0225 197 ASN A O 1176 C CB . ASN A 147 ? 0.2915 0.3053 0.3565 0.0241 -0.0106 -0.0238 197 ASN A CB 1177 C CG . ASN A 147 ? 0.4444 0.4564 0.5095 0.0316 -0.0141 -0.0215 197 ASN A CG 1178 O OD1 . ASN A 147 ? 0.4363 0.4481 0.5088 0.0334 -0.0149 -0.0236 197 ASN A OD1 1179 N ND2 . ASN A 147 ? 0.3535 0.3645 0.4099 0.0365 -0.0163 -0.0175 197 ASN A ND2 1180 N N . VAL A 148 ? 0.2341 0.2500 0.3084 0.0123 -0.0036 -0.0301 198 VAL A N 1181 C CA . VAL A 148 ? 0.2399 0.2606 0.3156 0.0071 -0.0010 -0.0343 198 VAL A CA 1182 C C . VAL A 148 ? 0.2862 0.3134 0.3630 0.0072 -0.0025 -0.0377 198 VAL A C 1183 O O . VAL A 148 ? 0.3077 0.3378 0.3889 0.0110 -0.0056 -0.0401 198 VAL A O 1184 C CB . VAL A 148 ? 0.2992 0.3219 0.3824 0.0065 0.0002 -0.0390 198 VAL A CB 1185 C CG1 . VAL A 148 ? 0.3096 0.3392 0.3946 0.0026 0.0029 -0.0438 198 VAL A CG1 1186 C CG2 . VAL A 148 ? 0.2906 0.3073 0.3741 0.0057 0.0016 -0.0368 198 VAL A CG2 1187 N N . GLY A 149 ? 0.2395 0.2687 0.3134 0.0033 -0.0005 -0.0379 199 GLY A N 1188 C CA . GLY A 149 ? 0.2435 0.2785 0.3204 0.0024 -0.0012 -0.0415 199 GLY A CA 1189 C C . GLY A 149 ? 0.2619 0.2944 0.3321 0.0028 -0.0025 -0.0384 199 GLY A C 1190 O O . GLY A 149 ? 0.3005 0.3336 0.3694 0.0069 -0.0064 -0.0387 199 GLY A O 1191 N N . THR A 150 ? 0.1674 0.1967 0.2323 -0.0008 0.0006 -0.0353 200 THR A N 1192 C CA . THR A 150 ? 0.1353 0.1618 0.1936 -0.0004 -0.0002 -0.0324 200 THR A CA 1193 C C . THR A 150 ? 0.1664 0.1937 0.2246 -0.0050 0.0027 -0.0330 200 THR A C 1194 O O . THR A 150 ? 0.1868 0.2159 0.2482 -0.0084 0.0061 -0.0342 200 THR A O 1195 C CB . THR A 150 ? 0.1712 0.1912 0.2223 0.0011 0.0003 -0.0265 200 THR A CB 1196 O OG1 . THR A 150 ? 0.1853 0.2036 0.2363 -0.0025 0.0036 -0.0253 200 THR A OG1 1197 C CG2 . THR A 150 ? 0.1408 0.1584 0.1920 0.0059 -0.0019 -0.0245 200 THR A CG2 1198 N N . TYR A 151 ? 0.1690 0.1949 0.2234 -0.0044 0.0016 -0.0321 201 TYR A N 1199 C CA . TYR A 151 ? 0.1589 0.1842 0.2133 -0.0082 0.0043 -0.0319 201 TYR A CA 1200 C C . TYR A 151 ? 0.1508 0.1717 0.1974 -0.0072 0.0039 -0.0282 201 TYR A C 1201 O O . TYR A 151 ? 0.1407 0.1605 0.1827 -0.0031 0.0009 -0.0271 201 TYR A O 1202 C CB . TYR A 151 ? 0.1529 0.1828 0.2157 -0.0099 0.0041 -0.0373 201 TYR A CB 1203 C CG . TYR A 151 ? 0.1818 0.2143 0.2456 -0.0061 -0.0010 -0.0410 201 TYR A CG 1204 C CD1 . TYR A 151 ? 0.1913 0.2219 0.2512 -0.0054 -0.0023 -0.0409 201 TYR A CD1 1205 C CD2 . TYR A 151 ? 0.2236 0.2611 0.2924 -0.0027 -0.0048 -0.0451 201 TYR A CD2 1206 C CE1 . TYR A 151 ? 0.2165 0.2503 0.2763 -0.0011 -0.0074 -0.0450 201 TYR A CE1 1207 C CE2 . TYR A 151 ? 0.2384 0.2795 0.3080 0.0015 -0.0101 -0.0493 201 TYR A CE2 1208 C CZ . TYR A 151 ? 0.3422 0.3815 0.4066 0.0025 -0.0115 -0.0492 201 TYR A CZ 1209 O OH . TYR A 151 ? 0.3631 0.4065 0.4271 0.0073 -0.0171 -0.0539 201 TYR A OH 1210 N N . VAL A 152 ? 0.1385 0.1574 0.1841 -0.0104 0.0067 -0.0269 202 VAL A N 1211 C CA . VAL A 152 ? 0.1503 0.1656 0.1899 -0.0097 0.0066 -0.0243 202 VAL A CA 1212 C C . VAL A 152 ? 0.1932 0.2089 0.2375 -0.0125 0.0079 -0.0270 202 VAL A C 1213 O O . VAL A 152 ? 0.2221 0.2372 0.2691 -0.0160 0.0116 -0.0258 202 VAL A O 1214 C CB . VAL A 152 ? 0.1825 0.1939 0.2164 -0.0107 0.0090 -0.0192 202 VAL A CB 1215 C CG1 . VAL A 152 ? 0.1798 0.1881 0.2087 -0.0099 0.0090 -0.0170 202 VAL A CG1 1216 C CG2 . VAL A 152 ? 0.1925 0.2030 0.2244 -0.0086 0.0083 -0.0170 202 VAL A CG2 1217 N N . SER A 153 ? 0.1530 0.1699 0.1983 -0.0105 0.0050 -0.0303 203 SER A N 1218 C CA . SER A 153 ? 0.1535 0.1704 0.2051 -0.0130 0.0059 -0.0337 203 SER A CA 1219 C C . SER A 153 ? 0.1887 0.2020 0.2350 -0.0118 0.0055 -0.0323 203 SER A C 1220 O O . SER A 153 ? 0.2018 0.2156 0.2419 -0.0077 0.0024 -0.0325 203 SER A O 1221 C CB . SER A 153 ? 0.2143 0.2366 0.2742 -0.0118 0.0023 -0.0410 203 SER A CB 1222 O OG . SER A 153 ? 0.3869 0.4131 0.4525 -0.0126 0.0026 -0.0426 203 SER A OG 1223 N N . VAL A 154 ? 0.1487 0.1583 0.1972 -0.0150 0.0090 -0.0307 204 VAL A N 1224 C CA . VAL A 154 ? 0.1273 0.1335 0.1725 -0.0139 0.0087 -0.0302 204 VAL A CA 1225 C C . VAL A 154 ? 0.1981 0.2031 0.2531 -0.0168 0.0101 -0.0339 204 VAL A C 1226 O O . VAL A 154 ? 0.1996 0.2033 0.2607 -0.0206 0.0140 -0.0325 204 VAL A O 1227 C CB . VAL A 154 ? 0.1736 0.1754 0.2117 -0.0145 0.0117 -0.0234 204 VAL A CB 1228 C CG1 . VAL A 154 ? 0.1706 0.1693 0.2056 -0.0130 0.0114 -0.0230 204 VAL A CG1 1229 C CG2 . VAL A 154 ? 0.1782 0.1811 0.2094 -0.0125 0.0109 -0.0199 204 VAL A CG2 1230 N N . GLY A 155 ? 0.1601 0.1655 0.2170 -0.0149 0.0073 -0.0388 205 GLY A N 1231 C CA . GLY A 155 ? 0.1492 0.1531 0.2176 -0.0178 0.0085 -0.0433 205 GLY A CA 1232 C C . GLY A 155 ? 0.2159 0.2170 0.2835 -0.0160 0.0072 -0.0457 205 GLY A C 1233 O O . GLY A 155 ? 0.2141 0.2170 0.2733 -0.0115 0.0037 -0.0470 205 GLY A O 1234 N N . THR A 156 ? 0.1734 0.1696 0.2495 -0.0192 0.0105 -0.0459 206 THR A N 1235 C CA . THR A 156 ? 0.1606 0.1537 0.2392 -0.0180 0.0095 -0.0494 206 THR A CA 1236 C C . THR A 156 ? 0.2174 0.2086 0.3131 -0.0223 0.0118 -0.0541 206 THR A C 1237 O O . THR A 156 ? 0.2220 0.2155 0.3259 -0.0255 0.0136 -0.0549 206 THR A O 1238 C CB . THR A 156 ? 0.2625 0.2489 0.3337 -0.0177 0.0128 -0.0417 206 THR A CB 1239 O OG1 . THR A 156 ? 0.2382 0.2190 0.3152 -0.0218 0.0183 -0.0364 206 THR A OG1 1240 C CG2 . THR A 156 ? 0.2320 0.2197 0.2887 -0.0149 0.0124 -0.0354 206 THR A CG2 1241 N N . SER A 157 ? 0.1928 0.1794 0.2949 -0.0225 0.0121 -0.0573 207 SER A N 1242 C CA A SER A 157 ? 0.1956 0.1795 0.3159 -0.0268 0.0148 -0.0618 207 SER A CA 1243 C CA B SER A 157 ? 0.1911 0.1749 0.3114 -0.0268 0.0148 -0.0618 207 SER A CA 1244 C C . SER A 157 ? 0.2583 0.2353 0.3815 -0.0312 0.0225 -0.0524 207 SER A C 1245 O O . SER A 157 ? 0.2723 0.2469 0.4106 -0.0355 0.0264 -0.0540 207 SER A O 1246 C CB A SER A 157 ? 0.2475 0.2283 0.3745 -0.0254 0.0127 -0.0686 207 SER A CB 1247 C CB B SER A 157 ? 0.2278 0.2081 0.3545 -0.0254 0.0130 -0.0680 207 SER A CB 1248 O OG A SER A 157 ? 0.3158 0.3043 0.4404 -0.0209 0.0055 -0.0782 207 SER A OG 1249 O OG B SER A 157 ? 0.2341 0.2062 0.3553 -0.0252 0.0168 -0.0603 207 SER A OG 1250 N N . THR A 158 ? 0.2163 0.1901 0.3253 -0.0298 0.0248 -0.0427 208 THR A N 1251 C CA . THR A 158 ? 0.2411 0.2090 0.3499 -0.0327 0.0317 -0.0332 208 THR A CA 1252 C C . THR A 158 ? 0.2856 0.2575 0.3840 -0.0326 0.0330 -0.0271 208 THR A C 1253 O O . THR A 158 ? 0.2997 0.2681 0.3965 -0.0343 0.0385 -0.0197 208 THR A O 1254 C CB . THR A 158 ? 0.3135 0.2737 0.4166 -0.0308 0.0336 -0.0272 208 THR A CB 1255 O OG1 . THR A 158 ? 0.3583 0.3215 0.4479 -0.0265 0.0291 -0.0268 208 THR A OG1 1256 C CG2 . THR A 158 ? 0.3641 0.3185 0.4803 -0.0317 0.0342 -0.0320 208 THR A CG2 1257 N N . LEU A 159 ? 0.2127 0.1917 0.3046 -0.0304 0.0282 -0.0305 209 LEU A N 1258 C CA . LEU A 159 ? 0.1968 0.1795 0.2797 -0.0299 0.0286 -0.0261 209 LEU A CA 1259 C C . LEU A 159 ? 0.2294 0.2198 0.3168 -0.0301 0.0255 -0.0324 209 LEU A C 1260 O O . LEU A 159 ? 0.1846 0.1786 0.2748 -0.0281 0.0205 -0.0395 209 LEU A O 1261 C CB . LEU A 159 ? 0.2002 0.1831 0.2688 -0.0260 0.0255 -0.0229 209 LEU A CB 1262 C CG . LEU A 159 ? 0.2548 0.2415 0.3144 -0.0250 0.0251 -0.0192 209 LEU A CG 1263 C CD1 . LEU A 159 ? 0.2930 0.2765 0.3482 -0.0261 0.0297 -0.0118 209 LEU A CD1 1264 C CD2 . LEU A 159 ? 0.2667 0.2555 0.3167 -0.0213 0.0209 -0.0193 209 LEU A CD2 1265 N N . ASN A 160 ? 0.2118 0.2049 0.2991 -0.0318 0.0282 -0.0298 210 ASN A N 1266 C CA . ASN A 160 ? 0.2170 0.2175 0.3076 -0.0314 0.0253 -0.0348 210 ASN A CA 1267 C C . ASN A 160 ? 0.2428 0.2447 0.3252 -0.0313 0.0276 -0.0292 210 ASN A C 1268 O O . ASN A 160 ? 0.2553 0.2577 0.3426 -0.0341 0.0326 -0.0271 210 ASN A O 1269 C CB . ASN A 160 ? 0.2577 0.2609 0.3652 -0.0348 0.0270 -0.0408 210 ASN A CB 1270 C CG . ASN A 160 ? 0.4565 0.4680 0.5691 -0.0341 0.0237 -0.0467 210 ASN A CG 1271 O OD1 . ASN A 160 ? 0.3360 0.3510 0.4395 -0.0304 0.0191 -0.0472 210 ASN A OD1 1272 N ND2 . ASN A 160 ? 0.4064 0.4211 0.5347 -0.0376 0.0261 -0.0515 210 ASN A ND2 1273 N N . LYS A 161 ? 0.1971 0.1998 0.2678 -0.0280 0.0243 -0.0269 211 LYS A N 1274 C CA . LYS A 161 ? 0.1816 0.1857 0.2455 -0.0277 0.0260 -0.0226 211 LYS A CA 1275 C C . LYS A 161 ? 0.2432 0.2526 0.3061 -0.0254 0.0217 -0.0263 211 LYS A C 1276 O O . LYS A 161 ? 0.2613 0.2710 0.3198 -0.0223 0.0172 -0.0278 211 LYS A O 1277 C CB . LYS A 161 ? 0.2162 0.2164 0.2690 -0.0260 0.0264 -0.0167 211 LYS A CB 1278 C CG . LYS A 161 ? 0.4078 0.4094 0.4547 -0.0260 0.0287 -0.0128 211 LYS A CG 1279 C CD . LYS A 161 ? 0.6404 0.6383 0.6788 -0.0247 0.0296 -0.0074 211 LYS A CD 1280 C CE . LYS A 161 ? 0.7244 0.7246 0.7567 -0.0240 0.0309 -0.0047 211 LYS A CE 1281 N NZ . LYS A 161 ? 0.8074 0.8047 0.8322 -0.0223 0.0312 -0.0001 211 LYS A NZ 1282 N N . ARG A 162 ? 0.1893 0.2028 0.2564 -0.0265 0.0232 -0.0276 212 ARG A N 1283 C CA . ARG A 162 ? 0.1826 0.2009 0.2500 -0.0241 0.0191 -0.0311 212 ARG A CA 1284 C C . ARG A 162 ? 0.2490 0.2687 0.3127 -0.0243 0.0215 -0.0283 212 ARG A C 1285 O O . ARG A 162 ? 0.2914 0.3142 0.3611 -0.0265 0.0250 -0.0294 212 ARG A O 1286 C CB . ARG A 162 ? 0.2216 0.2450 0.3012 -0.0249 0.0177 -0.0379 212 ARG A CB 1287 C CG . ARG A 162 ? 0.2255 0.2480 0.3101 -0.0247 0.0152 -0.0420 212 ARG A CG 1288 C CD . ARG A 162 ? 0.3800 0.4084 0.4783 -0.0253 0.0130 -0.0502 212 ARG A CD 1289 N NE . ARG A 162 ? 0.3804 0.4078 0.4821 -0.0245 0.0100 -0.0546 212 ARG A NE 1290 C CZ . ARG A 162 ? 0.4659 0.4988 0.5730 -0.0217 0.0041 -0.0624 212 ARG A CZ 1291 N NH1 . ARG A 162 ? 0.3982 0.4377 0.5087 -0.0195 0.0007 -0.0664 212 ARG A NH1 1292 N NH2 . ARG A 162 ? 0.2826 0.3147 0.3923 -0.0207 0.0013 -0.0669 212 ARG A NH2 1293 N N . SER A 163 ? 0.2054 0.2232 0.2601 -0.0220 0.0197 -0.0251 213 SER A N 1294 C CA . SER A 163 ? 0.1964 0.2150 0.2469 -0.0217 0.0211 -0.0230 213 SER A CA 1295 C C . SER A 163 ? 0.2486 0.2704 0.3010 -0.0195 0.0182 -0.0259 213 SER A C 1296 O O . SER A 163 ? 0.2118 0.2342 0.2654 -0.0171 0.0143 -0.0279 213 SER A O 1297 C CB . SER A 163 ? 0.2242 0.2388 0.2660 -0.0206 0.0206 -0.0187 213 SER A CB 1298 O OG . SER A 163 ? 0.3343 0.3453 0.3741 -0.0218 0.0226 -0.0159 213 SER A OG 1299 N N . THR A 164 ? 0.2159 0.2401 0.2685 -0.0199 0.0202 -0.0261 214 THR A N 1300 C CA . THR A 164 ? 0.2215 0.2483 0.2764 -0.0179 0.0181 -0.0287 214 THR A CA 1301 C C . THR A 164 ? 0.2249 0.2496 0.2737 -0.0172 0.0183 -0.0263 214 THR A C 1302 O O . THR A 164 ? 0.2355 0.2606 0.2810 -0.0185 0.0213 -0.0248 214 THR A O 1303 C CB . THR A 164 ? 0.3537 0.3860 0.4156 -0.0193 0.0208 -0.0323 214 THR A CB 1304 O OG1 . THR A 164 ? 0.4468 0.4793 0.5054 -0.0214 0.0257 -0.0300 214 THR A OG1 1305 C CG2 . THR A 164 ? 0.4019 0.4373 0.4726 -0.0203 0.0207 -0.0357 214 THR A CG2 1306 N N . PRO A 165 ? 0.1891 0.2120 0.2373 -0.0149 0.0153 -0.0261 215 PRO A N 1307 C CA . PRO A 165 ? 0.1979 0.2195 0.2433 -0.0145 0.0153 -0.0252 215 PRO A CA 1308 C C . PRO A 165 ? 0.1999 0.2257 0.2477 -0.0147 0.0169 -0.0286 215 PRO A C 1309 O O . PRO A 165 ? 0.2129 0.2421 0.2660 -0.0143 0.0171 -0.0319 215 PRO A O 1310 C CB . PRO A 165 ? 0.2336 0.2522 0.2805 -0.0119 0.0123 -0.0244 215 PRO A CB 1311 C CG . PRO A 165 ? 0.2902 0.3080 0.3369 -0.0106 0.0106 -0.0236 215 PRO A CG 1312 C CD . PRO A 165 ? 0.2092 0.2315 0.2599 -0.0121 0.0117 -0.0270 215 PRO A CD 1313 N N . GLU A 166 ? 0.1878 0.2138 0.2320 -0.0150 0.0177 -0.0283 216 GLU A N 1314 C CA . GLU A 166 ? 0.1840 0.2145 0.2291 -0.0145 0.0190 -0.0321 216 GLU A CA 1315 C C . GLU A 166 ? 0.1943 0.2233 0.2427 -0.0130 0.0162 -0.0344 216 GLU A C 1316 O O . GLU A 166 ? 0.2306 0.2568 0.2771 -0.0130 0.0149 -0.0327 216 GLU A O 1317 C CB . GLU A 166 ? 0.2062 0.2387 0.2441 -0.0150 0.0214 -0.0308 216 GLU A CB 1318 C CG . GLU A 166 ? 0.3400 0.3739 0.3753 -0.0165 0.0255 -0.0283 216 GLU A CG 1319 C CD . GLU A 166 ? 0.6353 0.6677 0.6628 -0.0167 0.0272 -0.0240 216 GLU A CD 1320 O OE1 . GLU A 166 ? 0.7210 0.7549 0.7433 -0.0150 0.0263 -0.0246 216 GLU A OE1 1321 O OE2 . GLU A 166 ? 0.5962 0.6259 0.6231 -0.0182 0.0293 -0.0204 216 GLU A OE2 1322 N N . ILE A 167 ? 0.1766 0.2073 0.2312 -0.0118 0.0154 -0.0384 217 ILE A N 1323 C CA . ILE A 167 ? 0.1613 0.1899 0.2211 -0.0104 0.0130 -0.0408 217 ILE A CA 1324 C C . ILE A 167 ? 0.1567 0.1902 0.2164 -0.0099 0.0136 -0.0462 217 ILE A C 1325 O O . ILE A 167 ? 0.1606 0.1989 0.2215 -0.0094 0.0151 -0.0499 217 ILE A O 1326 C CB . ILE A 167 ? 0.2074 0.2344 0.2743 -0.0086 0.0115 -0.0420 217 ILE A CB 1327 C CG1 . ILE A 167 ? 0.2222 0.2449 0.2875 -0.0080 0.0104 -0.0369 217 ILE A CG1 1328 C CG2 . ILE A 167 ? 0.2334 0.2577 0.3073 -0.0071 0.0098 -0.0448 217 ILE A CG2 1329 C CD1 . ILE A 167 ? 0.3033 0.3254 0.3739 -0.0054 0.0086 -0.0376 217 ILE A CD1 1330 N N . ALA A 168 ? 0.1890 0.2221 0.2480 -0.0099 0.0123 -0.0473 218 ALA A N 1331 C CA . ALA A 168 ? 0.1671 0.2059 0.2251 -0.0088 0.0122 -0.0532 218 ALA A CA 1332 C C . ALA A 168 ? 0.1877 0.2255 0.2500 -0.0084 0.0094 -0.0563 218 ALA A C 1333 O O . ALA A 168 ? 0.1674 0.2020 0.2280 -0.0095 0.0087 -0.0523 218 ALA A O 1334 C CB . ALA A 168 ? 0.1827 0.2260 0.2302 -0.0089 0.0147 -0.0513 218 ALA A CB 1335 N N . THR A 169 ? 0.1765 0.2181 0.2440 -0.0069 0.0080 -0.0639 219 THR A N 1336 C CA . THR A 169 ? 0.2025 0.2441 0.2761 -0.0067 0.0050 -0.0685 219 THR A CA 1337 C C . THR A 169 ? 0.2612 0.3077 0.3255 -0.0060 0.0044 -0.0684 219 THR A C 1338 O O . THR A 169 ? 0.2694 0.3217 0.3243 -0.0044 0.0059 -0.0694 219 THR A O 1339 C CB . THR A 169 ? 0.2542 0.2990 0.3366 -0.0049 0.0033 -0.0779 219 THR A CB 1340 O OG1 . THR A 169 ? 0.2694 0.3091 0.3605 -0.0050 0.0038 -0.0773 219 THR A OG1 1341 C CG2 . THR A 169 ? 0.2253 0.2704 0.3163 -0.0050 0.0000 -0.0837 219 THR A CG2 1342 N N . ARG A 170 ? 0.2055 0.2499 0.2726 -0.0069 0.0024 -0.0674 220 ARG A N 1343 C CA . ARG A 170 ? 0.1967 0.2460 0.2555 -0.0057 0.0011 -0.0677 220 ARG A CA 1344 C C . ARG A 170 ? 0.2194 0.2703 0.2879 -0.0055 -0.0027 -0.0737 220 ARG A C 1345 O O . ARG A 170 ? 0.2054 0.2509 0.2863 -0.0075 -0.0030 -0.0740 220 ARG A O 1346 C CB . ARG A 170 ? 0.1897 0.2350 0.2413 -0.0071 0.0029 -0.0585 220 ARG A CB 1347 C CG . ARG A 170 ? 0.2482 0.2917 0.2923 -0.0077 0.0067 -0.0528 220 ARG A CG 1348 C CD . ARG A 170 ? 0.2962 0.3353 0.3349 -0.0091 0.0083 -0.0446 220 ARG A CD 1349 N NE . ARG A 170 ? 0.2029 0.2396 0.2388 -0.0102 0.0115 -0.0405 220 ARG A NE 1350 C CZ . ARG A 170 ? 0.2410 0.2730 0.2825 -0.0115 0.0118 -0.0385 220 ARG A CZ 1351 N NH1 . ARG A 170 ? 0.1836 0.2117 0.2326 -0.0119 0.0101 -0.0387 220 ARG A NH1 1352 N NH2 . ARG A 170 ? 0.2254 0.2567 0.2651 -0.0122 0.0141 -0.0360 220 ARG A NH2 1353 N N . PRO A 171 ? 0.2283 0.2863 0.2917 -0.0031 -0.0055 -0.0781 221 PRO A N 1354 C CA . PRO A 171 ? 0.2279 0.2881 0.3020 -0.0031 -0.0095 -0.0843 221 PRO A CA 1355 C C . PRO A 171 ? 0.2429 0.2964 0.3233 -0.0063 -0.0085 -0.0776 221 PRO A C 1356 O O . PRO A 171 ? 0.1714 0.2213 0.2433 -0.0071 -0.0060 -0.0689 221 PRO A O 1357 C CB . PRO A 171 ? 0.2737 0.3432 0.3372 0.0009 -0.0126 -0.0882 221 PRO A CB 1358 C CG . PRO A 171 ? 0.3367 0.4095 0.3855 0.0035 -0.0099 -0.0862 221 PRO A CG 1359 C CD . PRO A 171 ? 0.2641 0.3283 0.3117 0.0001 -0.0049 -0.0768 221 PRO A CD 1360 N N . LYS A 172 ? 0.1874 0.2389 0.2840 -0.0082 -0.0099 -0.0817 222 LYS A N 1361 C CA . LYS A 172 ? 0.1670 0.2125 0.2700 -0.0110 -0.0081 -0.0753 222 LYS A CA 1362 C C . LYS A 172 ? 0.1998 0.2497 0.2968 -0.0100 -0.0099 -0.0738 222 LYS A C 1363 O O . LYS A 172 ? 0.2060 0.2640 0.3028 -0.0075 -0.0141 -0.0811 222 LYS A O 1364 C CB . LYS A 172 ? 0.2080 0.2501 0.3310 -0.0134 -0.0083 -0.0795 222 LYS A CB 1365 C CG . LYS A 172 ? 0.3371 0.3716 0.4664 -0.0146 -0.0054 -0.0775 222 LYS A CG 1366 C CD . LYS A 172 ? 0.4771 0.5074 0.6272 -0.0170 -0.0049 -0.0809 222 LYS A CD 1367 C CE . LYS A 172 ? 0.7168 0.7373 0.8732 -0.0180 -0.0011 -0.0757 222 LYS A CE 1368 N NZ . LYS A 172 ? 0.8842 0.8978 1.0332 -0.0188 0.0031 -0.0635 222 LYS A NZ 1369 N N . VAL A 173 ? 0.1567 0.2017 0.2480 -0.0112 -0.0070 -0.0647 223 VAL A N 1370 C CA . VAL A 173 ? 0.1590 0.2071 0.2474 -0.0105 -0.0084 -0.0627 223 VAL A CA 1371 C C . VAL A 173 ? 0.1955 0.2370 0.2928 -0.0136 -0.0052 -0.0568 223 VAL A C 1372 O O . VAL A 173 ? 0.1191 0.1537 0.2123 -0.0149 -0.0014 -0.0497 223 VAL A O 1373 C CB . VAL A 173 ? 0.2168 0.2661 0.2875 -0.0081 -0.0078 -0.0571 223 VAL A CB 1374 C CG1 . VAL A 173 ? 0.2173 0.2676 0.2859 -0.0075 -0.0085 -0.0534 223 VAL A CG1 1375 C CG2 . VAL A 173 ? 0.2019 0.2584 0.2637 -0.0045 -0.0105 -0.0625 223 VAL A CG2 1376 N N . ASN A 174 ? 0.1428 0.1868 0.2516 -0.0145 -0.0065 -0.0597 224 ASN A N 1377 C CA . ASN A 174 ? 0.1625 0.2006 0.2807 -0.0174 -0.0024 -0.0539 224 ASN A CA 1378 C C . ASN A 174 ? 0.1931 0.2237 0.3194 -0.0196 0.0012 -0.0518 224 ASN A C 1379 O O . ASN A 174 ? 0.2040 0.2278 0.3295 -0.0208 0.0056 -0.0438 224 ASN A O 1380 C CB . ASN A 174 ? 0.1933 0.2285 0.2999 -0.0170 0.0002 -0.0450 224 ASN A CB 1381 C CG . ASN A 174 ? 0.3441 0.3856 0.4428 -0.0144 -0.0031 -0.0462 224 ASN A CG 1382 O OD1 . ASN A 174 ? 0.2178 0.2667 0.3208 -0.0128 -0.0075 -0.0536 224 ASN A OD1 1383 N ND2 . ASN A 174 ? 0.2667 0.3056 0.3534 -0.0135 -0.0014 -0.0392 224 ASN A ND2 1384 N N . GLY A 175 ? 0.1715 0.2036 0.3050 -0.0195 -0.0009 -0.0591 225 GLY A N 1385 C CA . GLY A 175 ? 0.1831 0.2084 0.3258 -0.0210 0.0018 -0.0584 225 GLY A CA 1386 C C . GLY A 175 ? 0.2199 0.2402 0.3509 -0.0198 0.0037 -0.0531 225 GLY A C 1387 O O . GLY A 175 ? 0.2216 0.2363 0.3600 -0.0204 0.0055 -0.0525 225 GLY A O 1388 N N . GLN A 176 ? 0.1560 0.1787 0.2700 -0.0180 0.0029 -0.0501 226 GLN A N 1389 C CA . GLN A 176 ? 0.1356 0.1546 0.2390 -0.0171 0.0047 -0.0452 226 GLN A CA 1390 C C . GLN A 176 ? 0.1873 0.2117 0.2804 -0.0151 0.0026 -0.0491 226 GLN A C 1391 O O . GLN A 176 ? 0.1772 0.2075 0.2631 -0.0139 0.0006 -0.0513 226 GLN A O 1392 C CB . GLN A 176 ? 0.1517 0.1677 0.2448 -0.0171 0.0071 -0.0364 226 GLN A CB 1393 C CG . GLN A 176 ? 0.2240 0.2355 0.3238 -0.0185 0.0100 -0.0311 226 GLN A CG 1394 C CD . GLN A 176 ? 0.3328 0.3377 0.4426 -0.0192 0.0128 -0.0288 226 GLN A CD 1395 O OE1 . GLN A 176 ? 0.3621 0.3637 0.4693 -0.0180 0.0132 -0.0276 226 GLN A OE1 1396 N NE2 . GLN A 176 ? 0.4109 0.4137 0.5334 -0.0208 0.0149 -0.0282 226 GLN A NE2 1397 N N . GLY A 177 ? 0.1451 0.1675 0.2378 -0.0146 0.0034 -0.0496 227 GLY A N 1398 C CA . GLY A 177 ? 0.1563 0.1830 0.2394 -0.0129 0.0028 -0.0520 227 GLY A CA 1399 C C . GLY A 177 ? 0.1791 0.2033 0.2512 -0.0130 0.0052 -0.0445 227 GLY A C 1400 O O . GLY A 177 ? 0.1707 0.1985 0.2338 -0.0120 0.0057 -0.0447 227 GLY A O 1401 N N . GLY A 178 ? 0.1797 0.1978 0.2529 -0.0139 0.0070 -0.0381 228 GLY A N 1402 C CA . GLY A 178 ? 0.1759 0.1921 0.2397 -0.0138 0.0087 -0.0321 228 GLY A CA 1403 C C . GLY A 178 ? 0.1691 0.1877 0.2251 -0.0140 0.0086 -0.0298 228 GLY A C 1404 O O . GLY A 178 ? 0.1577 0.1788 0.2159 -0.0140 0.0073 -0.0319 228 GLY A O 1405 N N . ARG A 179 ? 0.1424 0.1602 0.1902 -0.0139 0.0100 -0.0259 229 ARG A N 1406 C CA . ARG A 179 ? 0.1177 0.1366 0.1586 -0.0139 0.0102 -0.0232 229 ARG A CA 1407 C C . ARG A 179 ? 0.1675 0.1823 0.2044 -0.0143 0.0119 -0.0179 229 ARG A C 1408 O O . ARG A 179 ? 0.1517 0.1651 0.1884 -0.0143 0.0126 -0.0174 229 ARG A O 1409 C CB . ARG A 179 ? 0.1165 0.1398 0.1503 -0.0130 0.0105 -0.0248 229 ARG A CB 1410 C CG . ARG A 179 ? 0.1213 0.1502 0.1563 -0.0116 0.0087 -0.0309 229 ARG A CG 1411 C CD . ARG A 179 ? 0.1670 0.1983 0.2035 -0.0108 0.0062 -0.0325 229 ARG A CD 1412 N NE . ARG A 179 ? 0.2313 0.2691 0.2686 -0.0088 0.0038 -0.0393 229 ARG A NE 1413 C CZ . ARG A 179 ? 0.2250 0.2643 0.2724 -0.0091 0.0016 -0.0454 229 ARG A CZ 1414 N NH1 . ARG A 179 ? 0.2059 0.2401 0.2634 -0.0112 0.0022 -0.0444 229 ARG A NH1 1415 N NH2 . ARG A 179 ? 0.2057 0.2516 0.2534 -0.0069 -0.0011 -0.0526 229 ARG A NH2 1416 N N . MET A 180 ? 0.1575 0.1712 0.1911 -0.0142 0.0122 -0.0147 230 MET A N 1417 C CA . MET A 180 ? 0.1506 0.1609 0.1804 -0.0143 0.0134 -0.0106 230 MET A CA 1418 C C . MET A 180 ? 0.2184 0.2298 0.2419 -0.0142 0.0141 -0.0093 230 MET A C 1419 O O . MET A 180 ? 0.2320 0.2452 0.2537 -0.0135 0.0134 -0.0093 230 MET A O 1420 C CB . MET A 180 ? 0.1792 0.1868 0.2111 -0.0140 0.0138 -0.0078 230 MET A CB 1421 C CG . MET A 180 ? 0.2081 0.2133 0.2453 -0.0138 0.0142 -0.0075 230 MET A CG 1422 S SD . MET A 180 ? 0.2490 0.2511 0.2884 -0.0132 0.0159 -0.0033 230 MET A SD 1423 C CE . MET A 180 ? 0.2177 0.2164 0.2627 -0.0123 0.0168 -0.0022 230 MET A CE 1424 N N . GLU A 181 ? 0.1516 0.1619 0.1725 -0.0148 0.0155 -0.0084 231 GLU A N 1425 C CA . GLU A 181 ? 0.1499 0.1601 0.1660 -0.0149 0.0171 -0.0065 231 GLU A CA 1426 C C . GLU A 181 ? 0.2025 0.2089 0.2179 -0.0150 0.0176 -0.0039 231 GLU A C 1427 O O . GLU A 181 ? 0.1732 0.1782 0.1906 -0.0155 0.0176 -0.0044 231 GLU A O 1428 C CB . GLU A 181 ? 0.1786 0.1902 0.1946 -0.0158 0.0190 -0.0077 231 GLU A CB 1429 C CG . GLU A 181 ? 0.2657 0.2761 0.2783 -0.0163 0.0218 -0.0049 231 GLU A CG 1430 C CD . GLU A 181 ? 0.4928 0.5048 0.5071 -0.0176 0.0247 -0.0059 231 GLU A CD 1431 O OE1 . GLU A 181 ? 0.4339 0.4489 0.4514 -0.0178 0.0242 -0.0093 231 GLU A OE1 1432 O OE2 . GLU A 181 ? 0.3851 0.3953 0.3987 -0.0184 0.0277 -0.0033 231 GLU A OE2 1433 N N . PHE A 182 ? 0.1619 0.1672 0.1746 -0.0142 0.0176 -0.0016 232 PHE A N 1434 C CA . PHE A 182 ? 0.1439 0.1457 0.1562 -0.0140 0.0179 0.0002 232 PHE A CA 1435 C C . PHE A 182 ? 0.1764 0.1759 0.1870 -0.0144 0.0199 0.0020 232 PHE A C 1436 O O . PHE A 182 ? 0.1866 0.1869 0.1944 -0.0142 0.0212 0.0034 232 PHE A O 1437 C CB . PHE A 182 ? 0.1582 0.1600 0.1703 -0.0126 0.0169 0.0016 232 PHE A CB 1438 C CG . PHE A 182 ? 0.1507 0.1538 0.1664 -0.0125 0.0159 0.0004 232 PHE A CG 1439 C CD1 . PHE A 182 ? 0.1554 0.1567 0.1722 -0.0122 0.0163 0.0009 232 PHE A CD1 1440 C CD2 . PHE A 182 ? 0.1771 0.1833 0.1956 -0.0124 0.0148 -0.0013 232 PHE A CD2 1441 C CE1 . PHE A 182 ? 0.1934 0.1950 0.2136 -0.0119 0.0163 0.0010 232 PHE A CE1 1442 C CE2 . PHE A 182 ? 0.2055 0.2120 0.2293 -0.0127 0.0146 -0.0021 232 PHE A CE2 1443 C CZ . PHE A 182 ? 0.1902 0.1940 0.2147 -0.0125 0.0158 -0.0003 232 PHE A CZ 1444 N N . SER A 183 ? 0.1420 0.1387 0.1543 -0.0149 0.0203 0.0018 233 SER A N 1445 C CA . SER A 183 ? 0.1720 0.1655 0.1850 -0.0157 0.0225 0.0031 233 SER A CA 1446 C C . SER A 183 ? 0.2060 0.1965 0.2197 -0.0146 0.0216 0.0032 233 SER A C 1447 O O . SER A 183 ? 0.1875 0.1790 0.2009 -0.0134 0.0198 0.0019 233 SER A O 1448 C CB . SER A 183 ? 0.2239 0.2177 0.2414 -0.0177 0.0238 0.0007 233 SER A CB 1449 O OG . SER A 183 ? 0.2463 0.2435 0.2636 -0.0185 0.0248 0.0002 233 SER A OG 1450 N N . TRP A 184 ? 0.1952 0.1819 0.2100 -0.0148 0.0234 0.0047 234 TRP A N 1451 C CA . TRP A 184 ? 0.1897 0.1735 0.2057 -0.0135 0.0227 0.0042 234 TRP A CA 1452 C C . TRP A 184 ? 0.2063 0.1862 0.2275 -0.0150 0.0244 0.0030 234 TRP A C 1453 O O . TRP A 184 ? 0.1916 0.1702 0.2154 -0.0169 0.0271 0.0042 234 TRP A O 1454 C CB . TRP A 184 ? 0.1797 0.1623 0.1923 -0.0113 0.0226 0.0076 234 TRP A CB 1455 C CG . TRP A 184 ? 0.1996 0.1794 0.2106 -0.0111 0.0249 0.0117 234 TRP A CG 1456 C CD1 . TRP A 184 ? 0.2451 0.2271 0.2519 -0.0106 0.0255 0.0142 234 TRP A CD1 1457 C CD2 . TRP A 184 ? 0.2214 0.1955 0.2342 -0.0104 0.0267 0.0141 234 TRP A CD2 1458 N NE1 . TRP A 184 ? 0.2583 0.2364 0.2632 -0.0096 0.0281 0.0186 234 TRP A NE1 1459 C CE2 . TRP A 184 ? 0.2830 0.2558 0.2920 -0.0095 0.0290 0.0190 234 TRP A CE2 1460 C CE3 . TRP A 184 ? 0.2468 0.2167 0.2643 -0.0102 0.0269 0.0123 234 TRP A CE3 1461 C CZ2 . TRP A 184 ? 0.2953 0.2618 0.3053 -0.0086 0.0318 0.0232 234 TRP A CZ2 1462 C CZ3 . TRP A 184 ? 0.2806 0.2444 0.3004 -0.0097 0.0294 0.0156 234 TRP A CZ3 1463 C CH2 . TRP A 184 ? 0.3012 0.2630 0.3171 -0.0088 0.0319 0.0215 234 TRP A CH2 1464 N N . THR A 185 ? 0.1752 0.1535 0.1989 -0.0139 0.0232 0.0001 235 THR A N 1465 C CA . THR A 185 ? 0.1825 0.1567 0.2131 -0.0152 0.0245 -0.0021 235 THR A CA 1466 C C . THR A 185 ? 0.2015 0.1733 0.2322 -0.0128 0.0233 -0.0033 235 THR A C 1467 O O . THR A 185 ? 0.2127 0.1870 0.2386 -0.0103 0.0214 -0.0036 235 THR A O 1468 C CB . THR A 185 ? 0.2283 0.2054 0.2646 -0.0168 0.0232 -0.0080 235 THR A CB 1469 O OG1 . THR A 185 ? 0.3326 0.3061 0.3782 -0.0191 0.0253 -0.0101 235 THR A OG1 1470 C CG2 . THR A 185 ? 0.2189 0.1993 0.2533 -0.0142 0.0194 -0.0128 235 THR A CG2 1471 N N . LEU A 186 ? 0.1922 0.1591 0.2293 -0.0135 0.0248 -0.0044 236 LEU A N 1472 C CA . LEU A 186 ? 0.2384 0.2026 0.2778 -0.0114 0.0238 -0.0069 236 LEU A CA 1473 C C . LEU A 186 ? 0.2850 0.2503 0.3315 -0.0121 0.0220 -0.0148 236 LEU A C 1474 O O . LEU A 186 ? 0.2733 0.2367 0.3282 -0.0151 0.0235 -0.0168 236 LEU A O 1475 C CB . LEU A 186 ? 0.2722 0.2292 0.3150 -0.0114 0.0268 -0.0025 236 LEU A CB 1476 C CG . LEU A 186 ? 0.3578 0.3138 0.3937 -0.0087 0.0272 0.0038 236 LEU A CG 1477 C CD1 . LEU A 186 ? 0.3801 0.3281 0.4200 -0.0079 0.0300 0.0078 236 LEU A CD1 1478 C CD2 . LEU A 186 ? 0.3680 0.3275 0.3999 -0.0054 0.0243 0.0016 236 LEU A CD2 1479 N N . LEU A 187 ? 0.2163 0.1857 0.2592 -0.0092 0.0188 -0.0194 237 LEU A N 1480 C CA . LEU A 187 ? 0.1998 0.1719 0.2475 -0.0086 0.0160 -0.0277 237 LEU A CA 1481 C C . LEU A 187 ? 0.2369 0.2052 0.2902 -0.0070 0.0156 -0.0321 237 LEU A C 1482 O O . LEU A 187 ? 0.2032 0.1714 0.2515 -0.0038 0.0153 -0.0312 237 LEU A O 1483 C CB . LEU A 187 ? 0.2006 0.1797 0.2397 -0.0053 0.0128 -0.0299 237 LEU A CB 1484 C CG . LEU A 187 ? 0.2296 0.2129 0.2714 -0.0033 0.0090 -0.0389 237 LEU A CG 1485 C CD1 . LEU A 187 ? 0.2477 0.2328 0.2976 -0.0064 0.0082 -0.0424 237 LEU A CD1 1486 C CD2 . LEU A 187 ? 0.1881 0.1772 0.2194 0.0011 0.0067 -0.0393 237 LEU A CD2 1487 N N . ASP A 188 ? 0.2318 0.1968 0.2969 -0.0094 0.0162 -0.0366 238 ASP A N 1488 C CA . ASP A 188 ? 0.2369 0.1975 0.3095 -0.0082 0.0160 -0.0412 238 ASP A CA 1489 C C . ASP A 188 ? 0.2540 0.2201 0.3230 -0.0037 0.0117 -0.0494 238 ASP A C 1490 O O . ASP A 188 ? 0.2214 0.1944 0.2849 -0.0022 0.0087 -0.0527 238 ASP A O 1491 C CB . ASP A 188 ? 0.2659 0.2220 0.3542 -0.0122 0.0177 -0.0452 238 ASP A CB 1492 C CG . ASP A 188 ? 0.5584 0.5075 0.6507 -0.0159 0.0232 -0.0364 238 ASP A CG 1493 O OD1 . ASP A 188 ? 0.5894 0.5360 0.6728 -0.0147 0.0253 -0.0279 238 ASP A OD1 1494 O OD2 . ASP A 188 ? 0.6959 0.6423 0.8005 -0.0199 0.0257 -0.0383 238 ASP A OD2 1495 N N . MET A 189 ? 0.2251 0.1880 0.2976 -0.0013 0.0114 -0.0531 239 MET A N 1496 C CA . MET A 189 ? 0.2315 0.1999 0.3008 0.0034 0.0075 -0.0618 239 MET A CA 1497 C C . MET A 189 ? 0.2704 0.2433 0.3471 0.0028 0.0038 -0.0718 239 MET A C 1498 O O . MET A 189 ? 0.2769 0.2460 0.3675 -0.0014 0.0047 -0.0745 239 MET A O 1499 C CB . MET A 189 ? 0.2740 0.2375 0.3490 0.0056 0.0080 -0.0653 239 MET A CB 1500 C CG . MET A 189 ? 0.3303 0.2914 0.3977 0.0075 0.0106 -0.0572 239 MET A CG 1501 S SD . MET A 189 ? 0.4261 0.3802 0.5027 0.0098 0.0114 -0.0611 239 MET A SD 1502 C CE . MET A 189 ? 0.4064 0.3500 0.4919 0.0052 0.0157 -0.0524 239 MET A CE 1503 N N . TRP A 190 ? 0.2253 0.2068 0.2933 0.0072 -0.0003 -0.0771 240 TRP A N 1504 C CA . TRP A 190 ? 0.2417 0.2297 0.3145 0.0084 -0.0053 -0.0876 240 TRP A CA 1505 C C . TRP A 190 ? 0.2849 0.2750 0.3612 0.0046 -0.0055 -0.0857 240 TRP A C 1506 O O . TRP A 190 ? 0.2951 0.2913 0.3765 0.0056 -0.0099 -0.0946 240 TRP A O 1507 C CB . TRP A 190 ? 0.2571 0.2431 0.3450 0.0084 -0.0074 -0.0992 240 TRP A CB 1508 C CG . TRP A 190 ? 0.2896 0.2718 0.3767 0.0113 -0.0063 -0.1003 240 TRP A CG 1509 C CD1 . TRP A 190 ? 0.3327 0.3056 0.4313 0.0084 -0.0030 -0.0990 240 TRP A CD1 1510 C CD2 . TRP A 190 ? 0.2993 0.2861 0.3722 0.0176 -0.0073 -0.1006 240 TRP A CD2 1511 N NE1 . TRP A 190 ? 0.3459 0.3178 0.4393 0.0128 -0.0027 -0.0998 240 TRP A NE1 1512 C CE2 . TRP A 190 ? 0.3701 0.3508 0.4480 0.0184 -0.0052 -0.1011 240 TRP A CE2 1513 C CE3 . TRP A 190 ? 0.3242 0.3198 0.3813 0.0232 -0.0098 -0.1010 240 TRP A CE3 1514 C CZ2 . TRP A 190 ? 0.3747 0.3585 0.4427 0.0242 -0.0053 -0.1023 240 TRP A CZ2 1515 C CZ3 . TRP A 190 ? 0.3601 0.3583 0.4069 0.0289 -0.0092 -0.1014 240 TRP A CZ3 1516 C CH2 . TRP A 190 ? 0.3751 0.3680 0.4277 0.0293 -0.0071 -0.1025 240 TRP A CH2 1517 N N . ASP A 191 ? 0.2330 0.2188 0.3070 0.0006 -0.0010 -0.0750 241 ASP A N 1518 C CA . ASP A 191 ? 0.2179 0.2063 0.2942 -0.0025 -0.0009 -0.0730 241 ASP A CA 1519 C C . ASP A 191 ? 0.2604 0.2550 0.3217 0.0011 -0.0029 -0.0693 241 ASP A C 1520 O O . ASP A 191 ? 0.2646 0.2595 0.3141 0.0046 -0.0022 -0.0649 241 ASP A O 1521 C CB . ASP A 191 ? 0.2366 0.2181 0.3181 -0.0082 0.0047 -0.0642 241 ASP A CB 1522 C CG . ASP A 191 ? 0.3172 0.3012 0.4058 -0.0120 0.0053 -0.0647 241 ASP A CG 1523 O OD1 . ASP A 191 ? 0.3306 0.3204 0.4261 -0.0114 0.0012 -0.0739 241 ASP A OD1 1524 O OD2 . ASP A 191 ? 0.3195 0.3001 0.4076 -0.0155 0.0097 -0.0565 241 ASP A OD2 1525 N N . THR A 192 ? 0.1991 0.1983 0.2618 0.0002 -0.0047 -0.0705 242 THR A N 1526 C CA . THR A 192 ? 0.1978 0.2020 0.2481 0.0035 -0.0063 -0.0668 242 THR A CA 1527 C C . THR A 192 ? 0.2209 0.2232 0.2711 -0.0007 -0.0029 -0.0587 242 THR A C 1528 O O . THR A 192 ? 0.2281 0.2293 0.2892 -0.0052 -0.0015 -0.0598 242 THR A O 1529 C CB . THR A 192 ? 0.3170 0.3295 0.3680 0.0076 -0.0125 -0.0762 242 THR A CB 1530 O OG1 . THR A 192 ? 0.3162 0.3314 0.3650 0.0125 -0.0159 -0.0838 242 THR A OG1 1531 C CG2 . THR A 192 ? 0.2853 0.3026 0.3249 0.0113 -0.0143 -0.0723 242 THR A CG2 1532 N N . ILE A 193 ? 0.1692 0.1712 0.2079 0.0008 -0.0013 -0.0510 243 ILE A N 1533 C CA . ILE A 193 ? 0.1742 0.1758 0.2116 -0.0019 0.0008 -0.0448 243 ILE A CA 1534 C C . ILE A 193 ? 0.2203 0.2280 0.2528 0.0017 -0.0029 -0.0467 243 ILE A C 1535 O O . ILE A 193 ? 0.2277 0.2381 0.2511 0.0070 -0.0052 -0.0475 243 ILE A O 1536 C CB . ILE A 193 ? 0.2054 0.2031 0.2354 -0.0025 0.0045 -0.0360 243 ILE A CB 1537 C CG1 . ILE A 193 ? 0.2255 0.2227 0.2560 -0.0058 0.0068 -0.0307 243 ILE A CG1 1538 C CG2 . ILE A 193 ? 0.1974 0.1968 0.2164 0.0023 0.0038 -0.0338 243 ILE A CG2 1539 C CD1 . ILE A 193 ? 0.2403 0.2334 0.2681 -0.0077 0.0104 -0.0239 243 ILE A CD1 1540 N N . ASN A 194 ? 0.1931 0.2028 0.2312 -0.0007 -0.0032 -0.0472 244 ASN A N 1541 C CA . ASN A 194 ? 0.1845 0.1995 0.2186 0.0029 -0.0067 -0.0485 244 ASN A CA 1542 C C . ASN A 194 ? 0.2105 0.2240 0.2427 0.0006 -0.0040 -0.0419 244 ASN A C 1543 O O . ASN A 194 ? 0.2206 0.2317 0.2593 -0.0043 -0.0007 -0.0400 244 ASN A O 1544 C CB . ASN A 194 ? 0.2077 0.2281 0.2522 0.0029 -0.0107 -0.0575 244 ASN A CB 1545 C CG . ASN A 194 ? 0.3830 0.4064 0.4295 0.0062 -0.0147 -0.0660 244 ASN A CG 1546 O OD1 . ASN A 194 ? 0.4397 0.4674 0.4776 0.0125 -0.0189 -0.0686 244 ASN A OD1 1547 N ND2 . ASN A 194 ? 0.3255 0.3466 0.3835 0.0022 -0.0134 -0.0704 244 ASN A ND2 1548 N N . PHE A 195 ? 0.1576 0.1724 0.1809 0.0045 -0.0050 -0.0382 245 PHE A N 1549 C CA . PHE A 195 ? 0.1643 0.1779 0.1862 0.0030 -0.0029 -0.0326 245 PHE A CA 1550 C C . PHE A 195 ? 0.1937 0.2118 0.2155 0.0065 -0.0066 -0.0349 245 PHE A C 1551 O O . PHE A 195 ? 0.1925 0.2136 0.2089 0.0120 -0.0102 -0.0374 245 PHE A O 1552 C CB . PHE A 195 ? 0.1911 0.2015 0.2037 0.0048 -0.0006 -0.0254 245 PHE A CB 1553 C CG . PHE A 195 ? 0.2072 0.2134 0.2195 0.0018 0.0031 -0.0220 245 PHE A CG 1554 C CD1 . PHE A 195 ? 0.2494 0.2532 0.2642 -0.0022 0.0061 -0.0182 245 PHE A CD1 1555 C CD2 . PHE A 195 ? 0.2193 0.2246 0.2292 0.0032 0.0031 -0.0234 245 PHE A CD2 1556 C CE1 . PHE A 195 ? 0.2752 0.2758 0.2895 -0.0042 0.0088 -0.0152 245 PHE A CE1 1557 C CE2 . PHE A 195 ? 0.2607 0.2624 0.2709 0.0009 0.0062 -0.0203 245 PHE A CE2 1558 C CZ . PHE A 195 ? 0.2434 0.2428 0.2556 -0.0027 0.0088 -0.0161 245 PHE A CZ 1559 N N . GLU A 196 ? 0.1789 0.1979 0.2067 0.0038 -0.0058 -0.0348 246 GLU A N 1560 C CA . GLU A 196 ? 0.1772 0.2002 0.2057 0.0073 -0.0092 -0.0366 246 GLU A CA 1561 C C . GLU A 196 ? 0.2172 0.2381 0.2473 0.0047 -0.0063 -0.0322 246 GLU A C 1562 O O . GLU A 196 ? 0.2423 0.2623 0.2783 -0.0004 -0.0032 -0.0323 246 GLU A O 1563 C CB . GLU A 196 ? 0.1924 0.2212 0.2313 0.0067 -0.0125 -0.0450 246 GLU A CB 1564 C CG . GLU A 196 ? 0.2794 0.3134 0.3199 0.0110 -0.0168 -0.0479 246 GLU A CG 1565 C CD . GLU A 196 ? 0.5410 0.5818 0.5935 0.0105 -0.0204 -0.0572 246 GLU A CD 1566 O OE1 . GLU A 196 ? 0.4767 0.5203 0.5310 0.0121 -0.0235 -0.0632 246 GLU A OE1 1567 O OE2 . GLU A 196 ? 0.5980 0.6417 0.6593 0.0084 -0.0200 -0.0592 246 GLU A OE2 1568 N N . SER A 197 ? 0.1674 0.1879 0.1927 0.0084 -0.0074 -0.0289 247 SER A N 1569 C CA . SER A 197 ? 0.1469 0.1655 0.1750 0.0060 -0.0049 -0.0258 247 SER A CA 1570 C C . SER A 197 ? 0.1910 0.2106 0.2176 0.0108 -0.0075 -0.0248 247 SER A C 1571 O O . SER A 197 ? 0.2224 0.2418 0.2419 0.0163 -0.0097 -0.0229 247 SER A O 1572 C CB . SER A 197 ? 0.2005 0.2139 0.2243 0.0037 -0.0008 -0.0198 247 SER A CB 1573 O OG . SER A 197 ? 0.2085 0.2203 0.2345 0.0025 0.0008 -0.0173 247 SER A OG 1574 N N . THR A 198 ? 0.1748 0.1958 0.2080 0.0093 -0.0071 -0.0261 248 THR A N 1575 C CA . THR A 198 ? 0.1798 0.2008 0.2130 0.0136 -0.0091 -0.0248 248 THR A CA 1576 C C . THR A 198 ? 0.1943 0.2099 0.2268 0.0121 -0.0057 -0.0194 248 THR A C 1577 O O . THR A 198 ? 0.1963 0.2106 0.2302 0.0150 -0.0065 -0.0178 248 THR A O 1578 C CB . THR A 198 ? 0.1967 0.2235 0.2391 0.0135 -0.0116 -0.0310 248 THR A CB 1579 O OG1 . THR A 198 ? 0.2085 0.2359 0.2577 0.0073 -0.0079 -0.0327 248 THR A OG1 1580 C CG2 . THR A 198 ? 0.2079 0.2408 0.2528 0.0158 -0.0159 -0.0372 248 THR A CG2 1581 N N . GLY A 199 ? 0.1630 0.1755 0.1939 0.0080 -0.0021 -0.0168 249 GLY A N 1582 C CA . GLY A 199 ? 0.1801 0.1881 0.2113 0.0063 0.0010 -0.0127 249 GLY A CA 1583 C C . GLY A 199 ? 0.2113 0.2191 0.2435 0.0012 0.0039 -0.0130 249 GLY A C 1584 O O . GLY A 199 ? 0.2135 0.2243 0.2477 -0.0015 0.0040 -0.0164 249 GLY A O 1585 N N . ASN A 200 ? 0.1558 0.1598 0.1869 0.0000 0.0063 -0.0093 250 ASN A N 1586 C CA . ASN A 200 ? 0.1505 0.1545 0.1826 -0.0041 0.0085 -0.0096 250 ASN A CA 1587 C C . ASN A 200 ? 0.1817 0.1852 0.2093 -0.0054 0.0096 -0.0082 250 ASN A C 1588 O O . ASN A 200 ? 0.1598 0.1638 0.1878 -0.0082 0.0110 -0.0086 250 ASN A O 1589 C CB . ASN A 200 ? 0.1585 0.1661 0.1952 -0.0067 0.0089 -0.0139 250 ASN A CB 1590 C CG . ASN A 200 ? 0.1874 0.1955 0.2293 -0.0053 0.0079 -0.0157 250 ASN A CG 1591 O OD1 . ASN A 200 ? 0.1775 0.1866 0.2210 -0.0026 0.0059 -0.0169 250 ASN A OD1 1592 N ND2 . ASN A 200 ? 0.1423 0.1503 0.1876 -0.0068 0.0091 -0.0169 250 ASN A ND2 1593 N N . LEU A 201 ? 0.1827 0.1856 0.2059 -0.0028 0.0086 -0.0069 251 LEU A N 1594 C CA . LEU A 201 ? 0.1594 0.1618 0.1789 -0.0035 0.0094 -0.0061 251 LEU A CA 1595 C C . LEU A 201 ? 0.1712 0.1708 0.1885 -0.0032 0.0116 -0.0017 251 LEU A C 1596 O O . LEU A 201 ? 0.1706 0.1683 0.1862 -0.0003 0.0121 0.0014 251 LEU A O 1597 C CB . LEU A 201 ? 0.1533 0.1570 0.1693 -0.0003 0.0072 -0.0076 251 LEU A CB 1598 C CG . LEU A 201 ? 0.2003 0.2031 0.2119 0.0003 0.0078 -0.0069 251 LEU A CG 1599 C CD1 . LEU A 201 ? 0.1742 0.1769 0.1887 -0.0038 0.0091 -0.0085 251 LEU A CD1 1600 C CD2 . LEU A 201 ? 0.2359 0.2409 0.2444 0.0040 0.0049 -0.0098 251 LEU A CD2 1601 N N . ILE A 202 ? 0.1402 0.1395 0.1575 -0.0056 0.0130 -0.0014 252 ILE A N 1602 C CA . ILE A 202 ? 0.1529 0.1506 0.1691 -0.0055 0.0150 0.0018 252 ILE A CA 1603 C C . ILE A 202 ? 0.1953 0.1931 0.2071 -0.0045 0.0148 0.0015 252 ILE A C 1604 O O . ILE A 202 ? 0.1933 0.1915 0.2056 -0.0064 0.0146 -0.0003 252 ILE A O 1605 C CB . ILE A 202 ? 0.1732 0.1714 0.1931 -0.0083 0.0159 0.0016 252 ILE A CB 1606 C CG1 . ILE A 202 ? 0.1707 0.1695 0.1957 -0.0093 0.0155 0.0001 252 ILE A CG1 1607 C CG2 . ILE A 202 ? 0.1963 0.1937 0.2166 -0.0080 0.0178 0.0044 252 ILE A CG2 1608 C CD1 . ILE A 202 ? 0.1843 0.1809 0.2118 -0.0075 0.0161 0.0023 252 ILE A CD1 1609 N N . ALA A 203 ? 0.1655 0.1630 0.1731 -0.0012 0.0148 0.0028 253 ALA A N 1610 C CA . ALA A 203 ? 0.1675 0.1655 0.1711 0.0005 0.0141 0.0013 253 ALA A CA 1611 C C . ALA A 203 ? 0.2040 0.2012 0.2067 0.0002 0.0165 0.0034 253 ALA A C 1612 O O . ALA A 203 ? 0.1949 0.1915 0.1982 0.0006 0.0188 0.0070 253 ALA A O 1613 C CB . ALA A 203 ? 0.2041 0.2031 0.2021 0.0052 0.0128 0.0013 253 ALA A CB 1614 N N . PRO A 204 ? 0.1729 0.1702 0.1747 0.0001 0.0160 0.0012 254 PRO A N 1615 C CA . PRO A 204 ? 0.1787 0.1757 0.1796 0.0008 0.0181 0.0030 254 PRO A CA 1616 C C . PRO A 204 ? 0.2319 0.2298 0.2269 0.0051 0.0190 0.0041 254 PRO A C 1617 O O . PRO A 204 ? 0.2132 0.2122 0.2044 0.0078 0.0168 0.0018 254 PRO A O 1618 C CB . PRO A 204 ? 0.1973 0.1934 0.1991 -0.0002 0.0170 -0.0002 254 PRO A CB 1619 C CG . PRO A 204 ? 0.2412 0.2379 0.2433 0.0001 0.0144 -0.0042 254 PRO A CG 1620 C CD . PRO A 204 ? 0.1984 0.1960 0.2016 -0.0008 0.0139 -0.0032 254 PRO A CD 1621 N N . GLU A 205 ? 0.1995 0.1975 0.1939 0.0061 0.0222 0.0074 255 GLU A N 1622 C CA . GLU A 205 ? 0.2010 0.2004 0.1889 0.0107 0.0238 0.0084 255 GLU A CA 1623 C C . GLU A 205 ? 0.2261 0.2263 0.2133 0.0115 0.0236 0.0053 255 GLU A C 1624 O O . GLU A 205 ? 0.2192 0.2211 0.2008 0.0155 0.0234 0.0033 255 GLU A O 1625 C CB . GLU A 205 ? 0.2322 0.2314 0.2203 0.0117 0.0284 0.0142 255 GLU A CB 1626 C CG . GLU A 205 ? 0.3679 0.3687 0.3474 0.0173 0.0305 0.0160 255 GLU A CG 1627 C CD . GLU A 205 ? 0.5534 0.5536 0.5324 0.0188 0.0363 0.0227 255 GLU A CD 1628 O OE1 . GLU A 205 ? 0.3861 0.3849 0.3737 0.0150 0.0387 0.0254 255 GLU A OE1 1629 O OE2 . GLU A 205 ? 0.4827 0.4841 0.4530 0.0241 0.0384 0.0252 255 GLU A OE2 1630 N N . TYR A 206 ? 0.1990 0.1981 0.1919 0.0083 0.0235 0.0046 256 TYR A N 1631 C CA . TYR A 206 ? 0.1892 0.1883 0.1829 0.0090 0.0235 0.0022 256 TYR A CA 1632 C C . TYR A 206 ? 0.2278 0.2246 0.2255 0.0063 0.0209 -0.0008 256 TYR A C 1633 O O . TYR A 206 ? 0.2229 0.2186 0.2236 0.0032 0.0200 0.0002 256 TYR A O 1634 C CB . TYR A 206 ? 0.1866 0.1867 0.1843 0.0084 0.0267 0.0052 256 TYR A CB 1635 C CG . TYR A 206 ? 0.2490 0.2513 0.2445 0.0108 0.0307 0.0088 256 TYR A CG 1636 C CD1 . TYR A 206 ? 0.2822 0.2866 0.2733 0.0147 0.0329 0.0082 256 TYR A CD1 1637 C CD2 . TYR A 206 ? 0.2872 0.2894 0.2856 0.0092 0.0328 0.0129 256 TYR A CD2 1638 C CE1 . TYR A 206 ? 0.3437 0.3502 0.3327 0.0170 0.0377 0.0124 256 TYR A CE1 1639 C CE2 . TYR A 206 ? 0.3123 0.3158 0.3098 0.0112 0.0376 0.0171 256 TYR A CE2 1640 C CZ . TYR A 206 ? 0.4444 0.4501 0.4369 0.0151 0.0403 0.0172 256 TYR A CZ 1641 O OH . TYR A 206 ? 0.4934 0.5004 0.4847 0.0173 0.0460 0.0221 256 TYR A OH 1642 N N . GLY A 207 ? 0.2138 0.2098 0.2118 0.0076 0.0202 -0.0040 257 GLY A N 1643 C CA . GLY A 207 ? 0.2248 0.2176 0.2275 0.0054 0.0189 -0.0059 257 GLY A CA 1644 C C . GLY A 207 ? 0.2449 0.2370 0.2496 0.0065 0.0203 -0.0051 257 GLY A C 1645 O O . GLY A 207 ? 0.2303 0.2250 0.2330 0.0092 0.0220 -0.0047 257 GLY A O 1646 N N . PHE A 208 ? 0.1904 0.1793 0.1991 0.0049 0.0199 -0.0045 258 PHE A N 1647 C CA . PHE A 208 ? 0.1801 0.1684 0.1912 0.0063 0.0207 -0.0034 258 PHE A CA 1648 C C . PHE A 208 ? 0.2096 0.1936 0.2235 0.0072 0.0199 -0.0069 258 PHE A C 1649 O O . PHE A 208 ? 0.2037 0.1835 0.2206 0.0052 0.0194 -0.0062 258 PHE A O 1650 C CB . PHE A 208 ? 0.1785 0.1663 0.1917 0.0045 0.0206 0.0005 258 PHE A CB 1651 C CG . PHE A 208 ? 0.2017 0.1937 0.2145 0.0036 0.0212 0.0029 258 PHE A CG 1652 C CD1 . PHE A 208 ? 0.2435 0.2388 0.2588 0.0049 0.0223 0.0042 258 PHE A CD1 1653 C CD2 . PHE A 208 ? 0.2350 0.2276 0.2461 0.0015 0.0209 0.0033 258 PHE A CD2 1654 C CE1 . PHE A 208 ? 0.2628 0.2618 0.2800 0.0037 0.0231 0.0058 258 PHE A CE1 1655 C CE2 . PHE A 208 ? 0.2704 0.2662 0.2827 0.0006 0.0216 0.0052 258 PHE A CE2 1656 C CZ . PHE A 208 ? 0.2535 0.2523 0.2692 0.0016 0.0228 0.0064 258 PHE A CZ 1657 N N . LYS A 209 ? 0.1791 0.1644 0.1924 0.0103 0.0202 -0.0105 259 LYS A N 1658 C CA . LYS A 209 ? 0.1855 0.1669 0.2029 0.0116 0.0194 -0.0147 259 LYS A CA 1659 C C . LYS A 209 ? 0.2342 0.2121 0.2556 0.0120 0.0201 -0.0117 259 LYS A C 1660 O O . LYS A 209 ? 0.2699 0.2508 0.2908 0.0136 0.0210 -0.0091 259 LYS A O 1661 C CB . LYS A 209 ? 0.2363 0.2212 0.2510 0.0155 0.0194 -0.0200 259 LYS A CB 1662 C CG . LYS A 209 ? 0.3429 0.3242 0.3629 0.0174 0.0186 -0.0252 259 LYS A CG 1663 C CD . LYS A 209 ? 0.3701 0.3559 0.3865 0.0220 0.0188 -0.0304 259 LYS A CD 1664 C CE . LYS A 209 ? 0.4963 0.4800 0.5176 0.0246 0.0195 -0.0324 259 LYS A CE 1665 N NZ . LYS A 209 ? 0.5899 0.5778 0.6085 0.0294 0.0194 -0.0395 259 LYS A NZ 1666 N N . ILE A 210 ? 0.2245 0.1964 0.2506 0.0108 0.0197 -0.0116 260 ILE A N 1667 C CA . ILE A 210 ? 0.2240 0.1918 0.2535 0.0120 0.0202 -0.0082 260 ILE A CA 1668 C C . ILE A 210 ? 0.2991 0.2665 0.3318 0.0158 0.0203 -0.0125 260 ILE A C 1669 O O . ILE A 210 ? 0.2979 0.2613 0.3351 0.0161 0.0199 -0.0172 260 ILE A O 1670 C CB . ILE A 210 ? 0.2595 0.2202 0.2927 0.0096 0.0208 -0.0055 260 ILE A CB 1671 C CG1 . ILE A 210 ? 0.2658 0.2282 0.2953 0.0064 0.0210 -0.0018 260 ILE A CG1 1672 C CG2 . ILE A 210 ? 0.2842 0.2395 0.3205 0.0120 0.0214 -0.0017 260 ILE A CG2 1673 C CD1 . ILE A 210 ? 0.3761 0.3320 0.4093 0.0036 0.0226 0.0007 260 ILE A CD1 1674 N N . SER A 211 ? 0.2612 0.2332 0.2924 0.0185 0.0208 -0.0116 261 SER A N 1675 C CA . SER A 211 ? 0.2766 0.2495 0.3104 0.0224 0.0212 -0.0162 261 SER A CA 1676 C C . SER A 211 ? 0.3116 0.2796 0.3512 0.0248 0.0210 -0.0146 261 SER A C 1677 O O . SER A 211 ? 0.3528 0.3192 0.3964 0.0278 0.0210 -0.0192 261 SER A O 1678 C CB . SER A 211 ? 0.3422 0.3233 0.3722 0.0245 0.0226 -0.0168 261 SER A CB 1679 O OG . SER A 211 ? 0.5171 0.5013 0.5473 0.0239 0.0231 -0.0115 261 SER A OG 1680 N N . LYS A 212 ? 0.2528 0.2187 0.2926 0.0241 0.0206 -0.0084 262 LYS A N 1681 C CA . LYS A 212 ? 0.2516 0.2123 0.2960 0.0270 0.0201 -0.0060 262 LYS A CA 1682 C C . LYS A 212 ? 0.2666 0.2216 0.3100 0.0252 0.0199 0.0001 262 LYS A C 1683 O O . LYS A 212 ? 0.2542 0.2125 0.2928 0.0227 0.0197 0.0034 262 LYS A O 1684 C CB . LYS A 212 ? 0.2800 0.2467 0.3255 0.0307 0.0198 -0.0053 262 LYS A CB 1685 C CG . LYS A 212 ? 0.5124 0.4741 0.5637 0.0351 0.0191 -0.0045 262 LYS A CG 1686 C CD . LYS A 212 ? 0.6880 0.6553 0.7429 0.0390 0.0195 -0.0089 262 LYS A CD 1687 C CE . LYS A 212 ? 0.8712 0.8330 0.9328 0.0436 0.0188 -0.0095 262 LYS A CE 1688 N NZ . LYS A 212 ? 0.9306 0.8878 0.9962 0.0445 0.0197 -0.0161 262 LYS A NZ 1689 N N . ARG A 213 ? 0.2741 0.2201 0.3223 0.0263 0.0205 0.0014 263 ARG A N 1690 C CA . ARG A 213 ? 0.2982 0.2376 0.3454 0.0254 0.0214 0.0083 263 ARG A CA 1691 C C . ARG A 213 ? 0.3692 0.3049 0.4181 0.0304 0.0207 0.0129 263 ARG A C 1692 O O . ARG A 213 ? 0.3801 0.3146 0.4342 0.0337 0.0202 0.0096 263 ARG A O 1693 C CB . ARG A 213 ? 0.3232 0.2541 0.3757 0.0222 0.0235 0.0071 263 ARG A CB 1694 C CG . ARG A 213 ? 0.4057 0.3402 0.4566 0.0174 0.0238 0.0034 263 ARG A CG 1695 C CD . ARG A 213 ? 0.5071 0.4339 0.5658 0.0144 0.0257 0.0011 263 ARG A CD 1696 N NE . ARG A 213 ? 0.5085 0.4399 0.5673 0.0107 0.0251 -0.0048 263 ARG A NE 1697 C CZ . ARG A 213 ? 0.5860 0.5194 0.6417 0.0071 0.0258 -0.0025 263 ARG A CZ 1698 N NH1 . ARG A 213 ? 0.4284 0.3601 0.4798 0.0065 0.0275 0.0055 263 ARG A NH1 1699 N NH2 . ARG A 213 ? 0.3667 0.3043 0.4231 0.0045 0.0248 -0.0084 263 ARG A NH2 1700 N N . GLY A 214 A 0.3343 0.2681 0.3785 0.0313 0.0207 0.0203 263 GLY A N 1701 C CA . GLY A 214 A 0.3588 0.2889 0.4033 0.0370 0.0197 0.0255 263 GLY A CA 1702 C C . GLY A 214 A 0.4482 0.3791 0.4847 0.0384 0.0191 0.0332 263 GLY A C 1703 O O . GLY A 214 A 0.4356 0.3722 0.4665 0.0353 0.0188 0.0335 263 GLY A O 1704 N N . SER A 215 ? 0.4577 0.3834 0.4933 0.0438 0.0187 0.0393 264 SER A N 1705 C CA . SER A 215 ? 0.4665 0.3935 0.4930 0.0465 0.0178 0.0466 264 SER A CA 1706 C C . SER A 215 ? 0.5026 0.4397 0.5261 0.0516 0.0127 0.0458 264 SER A C 1707 O O . SER A 215 ? 0.5038 0.4434 0.5333 0.0549 0.0106 0.0422 264 SER A O 1708 C CB . SER A 215 ? 0.5412 0.4561 0.5668 0.0498 0.0208 0.0553 264 SER A CB 1709 O OG . SER A 215 ? 0.7110 0.6220 0.7405 0.0563 0.0191 0.0569 264 SER A OG 1710 N N . SER A 216 ? 0.4811 0.4249 0.4964 0.0520 0.0109 0.0480 265 SER A N 1711 C CA . SER A 216 ? 0.5050 0.4591 0.5157 0.0565 0.0058 0.0479 265 SER A CA 1712 C C . SER A 216 ? 0.5870 0.5474 0.5908 0.0529 0.0055 0.0474 265 SER A C 1713 O O . SER A 216 ? 0.6197 0.5790 0.6148 0.0558 0.0054 0.0531 265 SER A O 1714 C CB . SER A 216 ? 0.5668 0.5293 0.5850 0.0590 0.0021 0.0418 265 SER A CB 1715 O OG . SER A 216 ? 0.6880 0.6521 0.7045 0.0671 -0.0018 0.0451 265 SER A OG 1716 N N . GLY A 217 ? 0.5262 0.4919 0.5335 0.0467 0.0062 0.0413 266 GLY A N 1717 C CA . GLY A 217 ? 0.5103 0.4801 0.5115 0.0431 0.0065 0.0413 266 GLY A CA 1718 C C . GLY A 217 ? 0.5624 0.5436 0.5636 0.0414 0.0033 0.0361 266 GLY A C 1719 O O . GLY A 217 ? 0.4792 0.4653 0.4872 0.0383 0.0030 0.0304 266 GLY A O 1720 N N . ILE A 218 ? 0.5964 0.5809 0.5895 0.0427 0.0020 0.0383 267 ILE A N 1721 C CA . ILE A 218 ? 0.6030 0.5981 0.5958 0.0416 -0.0014 0.0334 267 ILE A CA 1722 C C . ILE A 218 ? 0.6792 0.6797 0.6646 0.0486 -0.0058 0.0354 267 ILE A C 1723 O O . ILE A 218 ? 0.6862 0.6824 0.6618 0.0513 -0.0043 0.0414 267 ILE A O 1724 C CB . ILE A 218 ? 0.6518 0.6472 0.6424 0.0355 0.0013 0.0318 267 ILE A CB 1725 C CG1 . ILE A 218 ? 0.6548 0.6436 0.6502 0.0295 0.0058 0.0310 267 ILE A CG1 1726 C CG2 . ILE A 218 ? 0.6722 0.6784 0.6659 0.0342 -0.0023 0.0255 267 ILE A CG2 1727 C CD1 . ILE A 218 ? 0.7574 0.7483 0.7523 0.0237 0.0076 0.0282 267 ILE A CD1 1728 N N . MET A 219 ? 0.6430 0.6533 0.6334 0.0516 -0.0112 0.0303 268 MET A N 1729 C CA . MET A 219 ? 0.9730 0.9913 0.9576 0.0585 -0.0168 0.0300 268 MET A CA 1730 C C . MET A 219 ? 1.1248 1.1507 1.1081 0.0553 -0.0183 0.0248 268 MET A C 1731 O O . MET A 219 ? 0.5510 0.5793 0.5428 0.0489 -0.0170 0.0196 268 MET A O 1732 C CB . MET A 219 ? 1.0024 1.0288 0.9959 0.0629 -0.0222 0.0252 268 MET A CB 1733 C CG . MET A 219 ? 1.0579 1.0783 1.0526 0.0678 -0.0219 0.0297 268 MET A CG 1734 S SD . MET A 219 ? 1.1263 1.1551 1.1189 0.0791 -0.0300 0.0295 268 MET A SD 1735 C CE . MET A 219 ? 1.0726 1.1160 1.0824 0.0767 -0.0346 0.0178 268 MET A CE 1736 N N . GLY B 1 ? 0.3545 0.3727 0.5183 -0.0783 0.0411 -0.0155 55 GLY B N 1737 C CA . GLY B 1 ? 0.3402 0.3522 0.4938 -0.0758 0.0366 -0.0160 55 GLY B CA 1738 C C . GLY B 1 ? 0.3421 0.3572 0.4863 -0.0705 0.0320 -0.0152 55 GLY B C 1739 O O . GLY B 1 ? 0.3273 0.3507 0.4756 -0.0690 0.0302 -0.0159 55 GLY B O 1740 N N . ILE B 2 ? 0.2811 0.2893 0.4138 -0.0678 0.0304 -0.0139 56 ILE B N 1741 C CA . ILE B 2 ? 0.2531 0.2628 0.3761 -0.0630 0.0264 -0.0128 56 ILE B CA 1742 C C . ILE B 2 ? 0.2833 0.2956 0.4039 -0.0603 0.0298 -0.0088 56 ILE B C 1743 O O . ILE B 2 ? 0.2825 0.2904 0.4003 -0.0608 0.0354 -0.0049 56 ILE B O 1744 C CB . ILE B 2 ? 0.2948 0.2964 0.4072 -0.0610 0.0253 -0.0122 56 ILE B CB 1745 C CG1 . ILE B 2 ? 0.3114 0.3122 0.4258 -0.0637 0.0215 -0.0179 56 ILE B CG1 1746 C CG2 . ILE B 2 ? 0.2984 0.3009 0.4004 -0.0561 0.0225 -0.0101 56 ILE B CG2 1747 C CD1 . ILE B 2 ? 0.4883 0.4794 0.5990 -0.0641 0.0239 -0.0181 56 ILE B CD1 1748 N N . PRO B 3 ? 0.2336 0.2530 0.3553 -0.0577 0.0265 -0.0096 57 PRO B N 1749 C CA . PRO B 3 ? 0.2290 0.2512 0.3494 -0.0554 0.0301 -0.0070 57 PRO B CA 1750 C C . PRO B 3 ? 0.2488 0.2656 0.3558 -0.0517 0.0308 -0.0035 57 PRO B C 1751 O O . PRO B 3 ? 0.2343 0.2470 0.3337 -0.0497 0.0270 -0.0034 57 PRO B O 1752 C CB . PRO B 3 ? 0.2497 0.2809 0.3781 -0.0538 0.0256 -0.0097 57 PRO B CB 1753 C CG . PRO B 3 ? 0.3037 0.3345 0.4294 -0.0534 0.0183 -0.0115 57 PRO B CG 1754 C CD . PRO B 3 ? 0.2589 0.2842 0.3837 -0.0570 0.0193 -0.0129 57 PRO B CD 1755 N N . PRO B 4 ? 0.2373 0.2552 0.3416 -0.0507 0.0355 -0.0010 58 PRO B N 1756 C CA . PRO B 4 ? 0.2541 0.2683 0.3464 -0.0472 0.0357 0.0019 58 PRO B CA 1757 C C . PRO B 4 ? 0.2978 0.3156 0.3889 -0.0435 0.0307 0.0001 58 PRO B C 1758 O O . PRO B 4 ? 0.2956 0.3195 0.3957 -0.0435 0.0278 -0.0027 58 PRO B O 1759 C CB . PRO B 4 ? 0.2880 0.3045 0.3790 -0.0481 0.0419 0.0038 58 PRO B CB 1760 C CG . PRO B 4 ? 0.3362 0.3555 0.4376 -0.0527 0.0462 0.0028 58 PRO B CG 1761 C CD . PRO B 4 ? 0.2666 0.2897 0.3785 -0.0532 0.0413 -0.0013 58 PRO B CD 1762 N N . LEU B 5 ? 0.2282 0.2422 0.3089 -0.0404 0.0296 0.0021 59 LEU B N 1763 C CA . LEU B 5 ? 0.2102 0.2268 0.2889 -0.0369 0.0259 0.0011 59 LEU B CA 1764 C C . LEU B 5 ? 0.2600 0.2796 0.3378 -0.0357 0.0300 0.0015 59 LEU B C 1765 O O . LEU B 5 ? 0.2631 0.2793 0.3324 -0.0355 0.0330 0.0040 59 LEU B O 1766 C CB . LEU B 5 ? 0.2246 0.2355 0.2932 -0.0346 0.0228 0.0024 59 LEU B CB 1767 C CG . LEU B 5 ? 0.2839 0.2965 0.3494 -0.0312 0.0197 0.0021 59 LEU B CG 1768 C CD1 . LEU B 5 ? 0.2940 0.3118 0.3671 -0.0311 0.0151 0.0002 59 LEU B CD1 1769 C CD2 . LEU B 5 ? 0.2961 0.3033 0.3520 -0.0295 0.0177 0.0033 59 LEU B CD2 1770 N N . GLU B 6 ? 0.1996 0.2260 0.2867 -0.0352 0.0302 -0.0011 60 GLU B N 1771 C CA . GLU B 6 ? 0.1860 0.2159 0.2734 -0.0346 0.0348 -0.0021 60 GLU B CA 1772 C C . GLU B 6 ? 0.2340 0.2642 0.3190 -0.0307 0.0314 -0.0028 60 GLU B C 1773 O O . GLU B 6 ? 0.2345 0.2671 0.3267 -0.0291 0.0267 -0.0040 60 GLU B O 1774 C CB . GLU B 6 ? 0.2101 0.2473 0.3114 -0.0365 0.0379 -0.0053 60 GLU B CB 1775 C CG . GLU B 6 ? 0.3551 0.3976 0.4604 -0.0354 0.0420 -0.0083 60 GLU B CG 1776 C CD . GLU B 6 ? 0.6266 0.6682 0.7220 -0.0371 0.0486 -0.0075 60 GLU B CD 1777 O OE1 . GLU B 6 ? 0.7185 0.7613 0.8147 -0.0409 0.0540 -0.0071 60 GLU B OE1 1778 O OE2 . GLU B 6 ? 0.5212 0.5611 0.6080 -0.0349 0.0483 -0.0072 60 GLU B OE2 1779 N N . LEU B 7 ? 0.2177 0.2452 0.2926 -0.0294 0.0332 -0.0016 61 LEU B N 1780 C CA . LEU B 7 ? 0.2090 0.2362 0.2815 -0.0261 0.0302 -0.0023 61 LEU B CA 1781 C C . LEU B 7 ? 0.2639 0.2967 0.3447 -0.0249 0.0324 -0.0059 61 LEU B C 1782 O O . LEU B 7 ? 0.2378 0.2706 0.3197 -0.0222 0.0296 -0.0068 61 LEU B O 1783 C CB . LEU B 7 ? 0.2159 0.2385 0.2756 -0.0250 0.0305 -0.0001 61 LEU B CB 1784 C CG . LEU B 7 ? 0.2804 0.2969 0.3325 -0.0254 0.0283 0.0032 61 LEU B CG 1785 C CD1 . LEU B 7 ? 0.2944 0.3077 0.3360 -0.0244 0.0292 0.0052 61 LEU B CD1 1786 C CD2 . LEU B 7 ? 0.2730 0.2876 0.3269 -0.0242 0.0228 0.0031 61 LEU B CD2 1787 N N . GLY B 8 ? 0.2471 0.2848 0.3348 -0.0270 0.0375 -0.0084 62 GLY B N 1788 C CA . GLY B 8 ? 0.2374 0.2807 0.3347 -0.0259 0.0402 -0.0129 62 GLY B CA 1789 C C . GLY B 8 ? 0.3014 0.3438 0.3897 -0.0248 0.0424 -0.0141 62 GLY B C 1790 O O . GLY B 8 ? 0.3077 0.3480 0.3838 -0.0265 0.0453 -0.0124 62 GLY B O 1791 N N . ASP B 9 ? 0.2567 0.3001 0.3508 -0.0219 0.0403 -0.0165 63 ASP B N 1792 C CA . ASP B 9 ? 0.2545 0.2974 0.3422 -0.0207 0.0419 -0.0187 63 ASP B CA 1793 C C . ASP B 9 ? 0.2801 0.3169 0.3567 -0.0189 0.0369 -0.0148 63 ASP B C 1794 O O . ASP B 9 ? 0.2657 0.3018 0.3369 -0.0178 0.0374 -0.0163 63 ASP B O 1795 C CB . ASP B 9 ? 0.2825 0.3291 0.3846 -0.0184 0.0422 -0.0236 63 ASP B CB 1796 C CG . ASP B 9 ? 0.5324 0.5858 0.6441 -0.0202 0.0493 -0.0296 63 ASP B CG 1797 O OD1 . ASP B 9 ? 0.5138 0.5691 0.6166 -0.0235 0.0550 -0.0307 63 ASP B OD1 1798 O OD2 . ASP B 9 ? 0.6917 0.7487 0.8199 -0.0184 0.0493 -0.0334 63 ASP B OD2 1799 N N . CYS B 10 ? 0.2320 0.2649 0.3057 -0.0188 0.0326 -0.0105 64 CYS B N 1800 C CA . CYS B 10 ? 0.2587 0.2863 0.3237 -0.0173 0.0281 -0.0072 64 CYS B CA 1801 C C . CYS B 10 ? 0.2695 0.2936 0.3211 -0.0185 0.0295 -0.0045 64 CYS B C 1802 O O . CYS B 10 ? 0.2578 0.2821 0.3071 -0.0209 0.0323 -0.0032 64 CYS B O 1803 C CB . CYS B 10 ? 0.3091 0.3348 0.3783 -0.0167 0.0228 -0.0048 64 CYS B CB 1804 S SG . CYS B 10 ? 0.3936 0.4210 0.4745 -0.0140 0.0184 -0.0057 64 CYS B SG 1805 N N . SER B 11 ? 0.2152 0.2365 0.2591 -0.0170 0.0277 -0.0036 65 SER B N 1806 C CA . SER B 11 ? 0.2051 0.2231 0.2381 -0.0177 0.0280 -0.0006 65 SER B CA 1807 C C . SER B 11 ? 0.2346 0.2478 0.2655 -0.0172 0.0243 0.0025 65 SER B C 1808 O O . SER B 11 ? 0.2061 0.2185 0.2415 -0.0162 0.0212 0.0022 65 SER B O 1809 C CB . SER B 11 ? 0.2444 0.2629 0.2711 -0.0166 0.0281 -0.0016 65 SER B CB 1810 O OG . SER B 11 ? 0.2645 0.2807 0.2919 -0.0143 0.0244 -0.0017 65 SER B OG 1811 N N . ILE B 12 ? 0.2250 0.2347 0.2491 -0.0178 0.0244 0.0056 66 ILE B N 1812 C CA . ILE B 12 ? 0.2271 0.2321 0.2497 -0.0172 0.0214 0.0075 66 ILE B CA 1813 C C . ILE B 12 ? 0.2445 0.2488 0.2665 -0.0150 0.0184 0.0063 66 ILE B C 1814 O O . ILE B 12 ? 0.2217 0.2245 0.2458 -0.0149 0.0161 0.0061 66 ILE B O 1815 C CB . ILE B 12 ? 0.2898 0.2911 0.3065 -0.0177 0.0220 0.0109 66 ILE B CB 1816 C CG1 . ILE B 12 ? 0.3119 0.3126 0.3300 -0.0204 0.0249 0.0128 66 ILE B CG1 1817 C CG2 . ILE B 12 ? 0.3079 0.3046 0.3235 -0.0164 0.0193 0.0117 66 ILE B CG2 1818 C CD1 . ILE B 12 ? 0.4403 0.4403 0.4652 -0.0218 0.0244 0.0116 66 ILE B CD1 1819 N N . ALA B 13 ? 0.2102 0.2158 0.2291 -0.0137 0.0187 0.0055 67 ALA B N 1820 C CA . ALA B 13 ? 0.2040 0.2091 0.2231 -0.0119 0.0163 0.0043 67 ALA B CA 1821 C C . ALA B 13 ? 0.2476 0.2541 0.2733 -0.0117 0.0150 0.0028 67 ALA B C 1822 O O . ALA B 13 ? 0.2355 0.2401 0.2615 -0.0113 0.0125 0.0034 67 ALA B O 1823 C CB . ALA B 13 ? 0.2349 0.2418 0.2506 -0.0110 0.0170 0.0030 67 ALA B CB 1824 N N . GLY B 14 ? 0.2044 0.2144 0.2358 -0.0121 0.0166 0.0011 68 GLY B N 1825 C CA . GLY B 14 ? 0.1910 0.2026 0.2307 -0.0116 0.0150 0.0001 68 GLY B CA 1826 C C . GLY B 14 ? 0.2050 0.2151 0.2461 -0.0125 0.0120 0.0021 68 GLY B C 1827 O O . GLY B 14 ? 0.2165 0.2261 0.2602 -0.0120 0.0089 0.0030 68 GLY B O 1828 N N . TRP B 15 ? 0.1669 0.1766 0.2067 -0.0141 0.0131 0.0028 69 TRP B N 1829 C CA . TRP B 15 ? 0.1801 0.1889 0.2211 -0.0156 0.0106 0.0039 69 TRP B CA 1830 C C . TRP B 15 ? 0.2223 0.2273 0.2566 -0.0155 0.0081 0.0049 69 TRP B C 1831 O O . TRP B 15 ? 0.2178 0.2230 0.2529 -0.0160 0.0048 0.0055 69 TRP B O 1832 C CB . TRP B 15 ? 0.1846 0.1933 0.2259 -0.0176 0.0130 0.0040 69 TRP B CB 1833 C CG . TRP B 15 ? 0.2013 0.2082 0.2422 -0.0195 0.0111 0.0044 69 TRP B CG 1834 C CD1 . TRP B 15 ? 0.2337 0.2415 0.2768 -0.0203 0.0072 0.0042 69 TRP B CD1 1835 C CD2 . TRP B 15 ? 0.2096 0.2133 0.2478 -0.0211 0.0130 0.0049 69 TRP B CD2 1836 N NE1 . TRP B 15 ? 0.2437 0.2497 0.2855 -0.0226 0.0068 0.0036 69 TRP B NE1 1837 C CE2 . TRP B 15 ? 0.2603 0.2634 0.2998 -0.0230 0.0105 0.0040 69 TRP B CE2 1838 C CE3 . TRP B 15 ? 0.2402 0.2415 0.2751 -0.0214 0.0163 0.0063 69 TRP B CE3 1839 C CZ2 . TRP B 15 ? 0.2587 0.2585 0.2975 -0.0250 0.0117 0.0036 69 TRP B CZ2 1840 C CZ3 . TRP B 15 ? 0.2689 0.2666 0.3036 -0.0232 0.0172 0.0070 69 TRP B CZ3 1841 C CH2 . TRP B 15 ? 0.2819 0.2787 0.3190 -0.0249 0.0152 0.0053 69 TRP B CH2 1842 N N . LEU B 16 ? 0.1668 0.1690 0.1951 -0.0151 0.0097 0.0052 70 LEU B N 1843 C CA . LEU B 16 ? 0.1786 0.1776 0.2018 -0.0153 0.0084 0.0054 70 LEU B CA 1844 C C . LEU B 16 ? 0.2127 0.2117 0.2345 -0.0143 0.0067 0.0055 70 LEU B C 1845 O O . LEU B 16 ? 0.2103 0.2081 0.2292 -0.0154 0.0050 0.0056 70 LEU B O 1846 C CB . LEU B 16 ? 0.1894 0.1855 0.2088 -0.0149 0.0104 0.0057 70 LEU B CB 1847 C CG . LEU B 16 ? 0.2721 0.2670 0.2929 -0.0164 0.0121 0.0063 70 LEU B CG 1848 C CD1 . LEU B 16 ? 0.2940 0.2856 0.3119 -0.0155 0.0136 0.0077 70 LEU B CD1 1849 C CD2 . LEU B 16 ? 0.2684 0.2623 0.2908 -0.0186 0.0108 0.0050 70 LEU B CD2 1850 N N . LEU B 17 ? 0.1751 0.1756 0.1988 -0.0126 0.0074 0.0053 71 LEU B N 1851 C CA . LEU B 17 ? 0.1754 0.1757 0.1992 -0.0118 0.0060 0.0055 71 LEU B CA 1852 C C . LEU B 17 ? 0.2010 0.2027 0.2297 -0.0123 0.0032 0.0068 71 LEU B C 1853 O O . LEU B 17 ? 0.1970 0.1976 0.2244 -0.0126 0.0012 0.0083 71 LEU B O 1854 C CB . LEU B 17 ? 0.1789 0.1804 0.2042 -0.0101 0.0077 0.0042 71 LEU B CB 1855 C CG . LEU B 17 ? 0.2218 0.2224 0.2423 -0.0095 0.0094 0.0035 71 LEU B CG 1856 C CD1 . LEU B 17 ? 0.2135 0.2165 0.2352 -0.0084 0.0108 0.0017 71 LEU B CD1 1857 C CD2 . LEU B 17 ? 0.2571 0.2554 0.2741 -0.0095 0.0087 0.0038 71 LEU B CD2 1858 N N . GLY B 18 ? 0.1597 0.1639 0.1944 -0.0125 0.0029 0.0067 72 GLY B N 1859 C CA . GLY B 18 ? 0.1761 0.1822 0.2176 -0.0126 -0.0004 0.0082 72 GLY B CA 1860 C C . GLY B 18 ? 0.1903 0.1979 0.2399 -0.0106 0.0001 0.0075 72 GLY B C 1861 O O . GLY B 18 ? 0.1748 0.1817 0.2278 -0.0101 -0.0027 0.0096 72 GLY B O 1862 N N . ASN B 19 ? 0.1731 0.1824 0.2253 -0.0097 0.0038 0.0046 73 ASN B N 1863 C CA . ASN B 19 ? 0.1663 0.1773 0.2274 -0.0081 0.0049 0.0027 73 ASN B CA 1864 C C . ASN B 19 ? 0.1859 0.1990 0.2578 -0.0078 0.0016 0.0043 73 ASN B C 1865 O O . ASN B 19 ? 0.1928 0.2082 0.2667 -0.0089 0.0010 0.0045 73 ASN B O 1866 C CB . ASN B 19 ? 0.2052 0.2190 0.2672 -0.0081 0.0097 -0.0012 73 ASN B CB 1867 C CG . ASN B 19 ? 0.2484 0.2648 0.3202 -0.0068 0.0118 -0.0048 73 ASN B CG 1868 O OD1 . ASN B 19 ? 0.2311 0.2485 0.3139 -0.0058 0.0099 -0.0045 73 ASN B OD1 1869 N ND2 . ASN B 19 ? 0.1879 0.2062 0.2571 -0.0072 0.0160 -0.0085 73 ASN B ND2 1870 N N . PRO B 20 ? 0.1782 0.1907 0.2578 -0.0064 -0.0010 0.0058 74 PRO B N 1871 C CA . PRO B 20 ? 0.1892 0.2039 0.2798 -0.0060 -0.0051 0.0081 74 PRO B CA 1872 C C . PRO B 20 ? 0.2513 0.2709 0.3531 -0.0056 -0.0030 0.0048 74 PRO B C 1873 O O . PRO B 20 ? 0.2512 0.2737 0.3603 -0.0059 -0.0063 0.0064 74 PRO B O 1874 C CB . PRO B 20 ? 0.2254 0.2379 0.3233 -0.0043 -0.0073 0.0101 74 PRO B CB 1875 C CG . PRO B 20 ? 0.2680 0.2764 0.3547 -0.0048 -0.0060 0.0106 74 PRO B CG 1876 C CD . PRO B 20 ? 0.2111 0.2207 0.2905 -0.0054 -0.0009 0.0061 74 PRO B CD 1877 N N . GLU B 21 ? 0.2131 0.2342 0.3156 -0.0052 0.0028 -0.0001 75 GLU B N 1878 C CA . GLU B 21 ? 0.2181 0.2442 0.3302 -0.0055 0.0061 -0.0039 75 GLU B CA 1879 C C . GLU B 21 ? 0.2879 0.3153 0.3940 -0.0078 0.0063 -0.0029 75 GLU B C 1880 O O . GLU B 21 ? 0.2772 0.3090 0.3915 -0.0086 0.0082 -0.0050 75 GLU B O 1881 C CB . GLU B 21 ? 0.2303 0.2582 0.3428 -0.0054 0.0127 -0.0096 75 GLU B CB 1882 C CG . GLU B 21 ? 0.3159 0.3435 0.4395 -0.0031 0.0131 -0.0121 75 GLU B CG 1883 C CD . GLU B 21 ? 0.6703 0.7020 0.8131 -0.0017 0.0134 -0.0147 75 GLU B CD 1884 O OE1 . GLU B 21 ? 0.4975 0.5338 0.6455 -0.0025 0.0191 -0.0203 75 GLU B OE1 1885 O OE2 . GLU B 21 ? 0.6959 0.7265 0.8490 0.0001 0.0082 -0.0111 75 GLU B OE2 1886 N N . CYS B 22 ? 0.2444 0.2683 0.3377 -0.0091 0.0044 0.0000 76 CYS B N 1887 C CA . CYS B 22 ? 0.2492 0.2732 0.3363 -0.0115 0.0047 0.0007 76 CYS B CA 1888 C C . CYS B 22 ? 0.2319 0.2555 0.3186 -0.0124 -0.0013 0.0041 76 CYS B C 1889 O O . CYS B 22 ? 0.2261 0.2487 0.3062 -0.0146 -0.0016 0.0046 76 CYS B O 1890 C CB . CYS B 22 ? 0.2882 0.3085 0.3617 -0.0123 0.0076 0.0006 76 CYS B CB 1891 S SG . CYS B 22 ? 0.3729 0.3947 0.4449 -0.0118 0.0140 -0.0031 76 CYS B SG 1892 N N . ASP B 23 ? 0.2021 0.2267 0.2967 -0.0111 -0.0061 0.0064 77 ASP B N 1893 C CA . ASP B 23 ? 0.1928 0.2177 0.2861 -0.0125 -0.0126 0.0101 77 ASP B CA 1894 C C . ASP B 23 ? 0.2255 0.2541 0.3221 -0.0147 -0.0139 0.0093 77 ASP B C 1895 O O . ASP B 23 ? 0.2117 0.2397 0.3016 -0.0170 -0.0177 0.0110 77 ASP B O 1896 C CB . ASP B 23 ? 0.2094 0.2351 0.3119 -0.0107 -0.0179 0.0135 77 ASP B CB 1897 C CG . ASP B 23 ? 0.2823 0.3035 0.3793 -0.0095 -0.0186 0.0161 77 ASP B CG 1898 O OD1 . ASP B 23 ? 0.3075 0.3250 0.3916 -0.0105 -0.0161 0.0156 77 ASP B OD1 1899 O OD2 . ASP B 23 ? 0.3253 0.3464 0.4312 -0.0079 -0.0223 0.0190 77 ASP B OD2 1900 N N . ARG B 24 ? 0.1742 0.2065 0.2804 -0.0146 -0.0101 0.0060 78 ARG B N 1901 C CA . ARG B 24 ? 0.1933 0.2293 0.3037 -0.0171 -0.0109 0.0049 78 ARG B CA 1902 C C . ARG B 24 ? 0.2422 0.2746 0.3392 -0.0199 -0.0089 0.0044 78 ARG B C 1903 O O . ARG B 24 ? 0.2465 0.2807 0.3449 -0.0225 -0.0103 0.0036 78 ARG B O 1904 C CB . ARG B 24 ? 0.1997 0.2401 0.3222 -0.0168 -0.0058 0.0012 78 ARG B CB 1905 C CG . ARG B 24 ? 0.2300 0.2685 0.3457 -0.0176 0.0020 -0.0015 78 ARG B CG 1906 C CD . ARG B 24 ? 0.1691 0.2124 0.2969 -0.0171 0.0073 -0.0053 78 ARG B CD 1907 N NE . ARG B 24 ? 0.2058 0.2473 0.3253 -0.0177 0.0144 -0.0073 78 ARG B NE 1908 C CZ . ARG B 24 ? 0.2609 0.3003 0.3753 -0.0160 0.0166 -0.0082 78 ARG B CZ 1909 N NH1 . ARG B 24 ? 0.2910 0.3296 0.4095 -0.0133 0.0130 -0.0074 78 ARG B NH1 1910 N NH2 . ARG B 24 ? 0.2958 0.3340 0.4014 -0.0171 0.0223 -0.0096 78 ARG B NH2 1911 N N . LEU B 25 ? 0.2051 0.2325 0.2909 -0.0193 -0.0054 0.0043 79 LEU B N 1912 C CA . LEU B 25 ? 0.1957 0.2189 0.2704 -0.0212 -0.0030 0.0038 79 LEU B CA 1913 C C . LEU B 25 ? 0.2434 0.2630 0.3077 -0.0219 -0.0064 0.0055 79 LEU B C 1914 O O . LEU B 25 ? 0.2291 0.2449 0.2849 -0.0228 -0.0040 0.0048 79 LEU B O 1915 C CB . LEU B 25 ? 0.1916 0.2123 0.2615 -0.0201 0.0031 0.0028 79 LEU B CB 1916 C CG . LEU B 25 ? 0.2135 0.2374 0.2906 -0.0203 0.0080 0.0008 79 LEU B CG 1917 C CD1 . LEU B 25 ? 0.2446 0.2661 0.3142 -0.0195 0.0128 0.0005 79 LEU B CD1 1918 C CD2 . LEU B 25 ? 0.2799 0.3056 0.3611 -0.0232 0.0091 0.0000 79 LEU B CD2 1919 N N . LEU B 26 ? 0.2256 0.2464 0.2906 -0.0215 -0.0117 0.0078 80 LEU B N 1920 C CA . LEU B 26 ? 0.2415 0.2591 0.2954 -0.0227 -0.0141 0.0092 80 LEU B CA 1921 C C . LEU B 26 ? 0.3226 0.3397 0.3705 -0.0261 -0.0151 0.0075 80 LEU B C 1922 O O . LEU B 26 ? 0.3122 0.3259 0.3503 -0.0272 -0.0143 0.0070 80 LEU B O 1923 C CB . LEU B 26 ? 0.2386 0.2574 0.2938 -0.0220 -0.0195 0.0129 80 LEU B CB 1924 C CG . LEU B 26 ? 0.2849 0.3020 0.3429 -0.0189 -0.0181 0.0143 80 LEU B CG 1925 C CD1 . LEU B 26 ? 0.2779 0.2971 0.3433 -0.0179 -0.0238 0.0183 80 LEU B CD1 1926 C CD2 . LEU B 26 ? 0.3305 0.3430 0.3773 -0.0189 -0.0158 0.0145 80 LEU B CD2 1927 N N . SER B 27 ? 0.2915 0.3120 0.3460 -0.0279 -0.0162 0.0060 81 SER B N 1928 C CA . SER B 27 ? 0.2904 0.3106 0.3407 -0.0316 -0.0168 0.0034 81 SER B CA 1929 C C . SER B 27 ? 0.3066 0.3285 0.3657 -0.0324 -0.0139 0.0012 81 SER B C 1930 O O . SER B 27 ? 0.2977 0.3245 0.3673 -0.0321 -0.0158 0.0016 81 SER B O 1931 C CB . SER B 27 ? 0.3596 0.3837 0.4087 -0.0341 -0.0237 0.0044 81 SER B CB 1932 O OG . SER B 27 ? 0.4409 0.4648 0.4850 -0.0381 -0.0241 0.0010 81 SER B OG 1933 N N . VAL B 28 A 0.2549 0.2728 0.3108 -0.0334 -0.0090 -0.0010 81 VAL B N 1934 C CA . VAL B 28 A 0.2305 0.2495 0.2944 -0.0346 -0.0057 -0.0024 81 VAL B CA 1935 C C . VAL B 28 A 0.2618 0.2783 0.3240 -0.0382 -0.0048 -0.0054 81 VAL B C 1936 O O . VAL B 28 A 0.2664 0.2783 0.3202 -0.0387 -0.0039 -0.0065 81 VAL B O 1937 C CB . VAL B 28 A 0.2848 0.3012 0.3491 -0.0323 0.0002 -0.0013 81 VAL B CB 1938 C CG1 . VAL B 28 A 0.2796 0.2990 0.3475 -0.0292 -0.0001 0.0004 81 VAL B CG1 1939 C CG2 . VAL B 28 A 0.2690 0.2789 0.3239 -0.0316 0.0033 -0.0009 81 VAL B CG2 1940 N N . PRO B 29 ? 0.2088 0.2283 0.2797 -0.0407 -0.0047 -0.0072 82 PRO B N 1941 C CA . PRO B 29 ? 0.2071 0.2242 0.2778 -0.0444 -0.0037 -0.0107 82 PRO B CA 1942 C C . PRO B 29 ? 0.2204 0.2311 0.2903 -0.0441 0.0027 -0.0102 82 PRO B C 1943 O O . PRO B 29 ? 0.2356 0.2444 0.3038 -0.0413 0.0060 -0.0072 82 PRO B O 1944 C CB . PRO B 29 ? 0.2312 0.2547 0.3135 -0.0472 -0.0059 -0.0124 82 PRO B CB 1945 C CG . PRO B 29 ? 0.2900 0.3172 0.3797 -0.0446 -0.0047 -0.0099 82 PRO B CG 1946 C CD . PRO B 29 ? 0.2261 0.2520 0.3089 -0.0406 -0.0055 -0.0068 82 PRO B CD 1947 N N . GLU B 30 ? 0.2085 0.2160 0.2801 -0.0473 0.0044 -0.0131 83 GLU B N 1948 C CA . GLU B 30 ? 0.1999 0.2006 0.2719 -0.0473 0.0099 -0.0120 83 GLU B CA 1949 C C . GLU B 30 ? 0.2370 0.2393 0.3152 -0.0469 0.0136 -0.0090 83 GLU B C 1950 O O . GLU B 30 ? 0.2233 0.2318 0.3094 -0.0484 0.0124 -0.0099 83 GLU B O 1951 C CB . GLU B 30 ? 0.2338 0.2310 0.3089 -0.0511 0.0107 -0.0163 83 GLU B CB 1952 C CG . GLU B 30 ? 0.3283 0.3180 0.4062 -0.0517 0.0161 -0.0149 83 GLU B CG 1953 C CD . GLU B 30 ? 0.6422 0.6293 0.7265 -0.0560 0.0168 -0.0198 83 GLU B CD 1954 O OE1 . GLU B 30 ? 0.5018 0.4929 0.5861 -0.0586 0.0130 -0.0249 83 GLU B OE1 1955 O OE2 . GLU B 30 ? 0.5261 0.5072 0.6153 -0.0571 0.0210 -0.0184 83 GLU B OE2 1956 N N . TRP B 31 ? 0.1935 0.1910 0.2682 -0.0451 0.0178 -0.0054 84 TRP B N 1957 C CA . TRP B 31 ? 0.1917 0.1907 0.2701 -0.0453 0.0220 -0.0023 84 TRP B CA 1958 C C . TRP B 31 ? 0.2374 0.2301 0.3171 -0.0473 0.0267 0.0000 84 TRP B C 1959 O O . TRP B 31 ? 0.2392 0.2255 0.3161 -0.0472 0.0266 -0.0001 84 TRP B O 1960 C CB . TRP B 31 ? 0.1632 0.1636 0.2356 -0.0416 0.0226 0.0005 84 TRP B CB 1961 C CG . TRP B 31 ? 0.1748 0.1692 0.2380 -0.0390 0.0229 0.0028 84 TRP B CG 1962 C CD1 . TRP B 31 ? 0.2095 0.1986 0.2693 -0.0387 0.0263 0.0065 84 TRP B CD1 1963 C CD2 . TRP B 31 ? 0.1722 0.1659 0.2291 -0.0363 0.0195 0.0019 84 TRP B CD2 1964 N NE1 . TRP B 31 ? 0.1934 0.1787 0.2464 -0.0359 0.0249 0.0075 84 TRP B NE1 1965 C CE2 . TRP B 31 ? 0.2218 0.2098 0.2729 -0.0345 0.0212 0.0045 84 TRP B CE2 1966 C CE3 . TRP B 31 ? 0.1881 0.1852 0.2439 -0.0357 0.0151 -0.0005 84 TRP B CE3 1967 C CZ2 . TRP B 31 ? 0.2194 0.2055 0.2645 -0.0320 0.0191 0.0039 84 TRP B CZ2 1968 C CZ3 . TRP B 31 ? 0.1997 0.1947 0.2482 -0.0334 0.0134 -0.0005 84 TRP B CZ3 1969 C CH2 . TRP B 31 ? 0.1913 0.1809 0.2350 -0.0317 0.0155 0.0012 84 TRP B CH2 1970 N N . SER B 32 ? 0.1851 0.1796 0.2692 -0.0491 0.0310 0.0022 85 SER B N 1971 C CA . SER B 32 ? 0.2069 0.1952 0.2919 -0.0514 0.0356 0.0058 85 SER B CA 1972 C C . SER B 32 ? 0.2746 0.2594 0.3501 -0.0487 0.0377 0.0113 85 SER B C 1973 O O . SER B 32 ? 0.2848 0.2623 0.3577 -0.0488 0.0392 0.0151 85 SER B O 1974 C CB . SER B 32 ? 0.2590 0.2510 0.3530 -0.0554 0.0395 0.0057 85 SER B CB 1975 O OG . SER B 32 ? 0.2878 0.2873 0.3821 -0.0544 0.0407 0.0056 85 SER B OG 1976 N N . TYR B 33 ? 0.2178 0.2079 0.2888 -0.0464 0.0374 0.0116 86 TYR B N 1977 C CA . TYR B 33 ? 0.2232 0.2121 0.2846 -0.0437 0.0384 0.0157 86 TYR B CA 1978 C C . TYR B 33 ? 0.2454 0.2408 0.3049 -0.0411 0.0367 0.0132 86 TYR B C 1979 O O . TYR B 33 ? 0.2287 0.2298 0.2952 -0.0416 0.0354 0.0094 86 TYR B O 1980 C CB . TYR B 33 ? 0.2585 0.2461 0.3175 -0.0462 0.0436 0.0206 86 TYR B CB 1981 C CG . TYR B 33 ? 0.3165 0.3101 0.3824 -0.0498 0.0478 0.0191 86 TYR B CG 1982 C CD1 . TYR B 33 ? 0.3490 0.3497 0.4137 -0.0493 0.0499 0.0175 86 TYR B CD1 1983 C CD2 . TYR B 33 ? 0.3392 0.3310 0.4132 -0.0539 0.0504 0.0192 86 TYR B CD2 1984 C CE1 . TYR B 33 ? 0.3854 0.3919 0.4574 -0.0527 0.0546 0.0158 86 TYR B CE1 1985 C CE2 . TYR B 33 ? 0.3666 0.3643 0.4479 -0.0574 0.0548 0.0177 86 TYR B CE2 1986 C CZ . TYR B 33 ? 0.4812 0.4864 0.5614 -0.0568 0.0571 0.0160 86 TYR B CZ 1987 O OH . TYR B 33 ? 0.5597 0.5711 0.6479 -0.0604 0.0621 0.0140 86 TYR B OH 1988 N N . ILE B 34 ? 0.2355 0.2303 0.2866 -0.0384 0.0364 0.0153 87 ILE B N 1989 C CA . ILE B 34 ? 0.2174 0.2177 0.2667 -0.0358 0.0350 0.0130 87 ILE B CA 1990 C C . ILE B 34 ? 0.2829 0.2872 0.3298 -0.0370 0.0397 0.0141 87 ILE B C 1991 O O . ILE B 34 ? 0.2753 0.2765 0.3151 -0.0379 0.0421 0.0183 87 ILE B O 1992 C CB . ILE B 34 ? 0.2516 0.2492 0.2939 -0.0322 0.0315 0.0135 87 ILE B CB 1993 C CG1 . ILE B 34 ? 0.2517 0.2454 0.2956 -0.0317 0.0277 0.0119 87 ILE B CG1 1994 C CG2 . ILE B 34 ? 0.2435 0.2463 0.2851 -0.0299 0.0303 0.0110 87 ILE B CG2 1995 C CD1 . ILE B 34 ? 0.2304 0.2200 0.2676 -0.0288 0.0254 0.0129 87 ILE B CD1 1996 N N . MET B 35 ? 0.2525 0.2637 0.3056 -0.0372 0.0411 0.0104 88 MET B N 1997 C CA . MET B 35 ? 0.2814 0.2975 0.3331 -0.0386 0.0462 0.0098 88 MET B CA 1998 C C . MET B 35 ? 0.3266 0.3456 0.3750 -0.0353 0.0446 0.0074 88 MET B C 1999 O O . MET B 35 ? 0.3063 0.3279 0.3617 -0.0331 0.0414 0.0040 88 MET B O 2000 C CB . MET B 35 ? 0.3309 0.3531 0.3943 -0.0412 0.0496 0.0064 88 MET B CB 2001 C CG . MET B 35 ? 0.4211 0.4406 0.4900 -0.0445 0.0505 0.0079 88 MET B CG 2002 S SD . MET B 35 ? 0.5184 0.5455 0.6031 -0.0480 0.0542 0.0038 88 MET B SD 2003 C CE . MET B 35 ? 0.4917 0.5209 0.5711 -0.0520 0.0631 0.0058 88 MET B CE 2004 N N . GLU B 36 ? 0.2791 0.2973 0.3170 -0.0351 0.0462 0.0094 89 GLU B N 2005 C CA . GLU B 36 ? 0.2785 0.2992 0.3129 -0.0324 0.0451 0.0068 89 GLU B CA 2006 C C . GLU B 36 ? 0.3619 0.3878 0.3922 -0.0347 0.0507 0.0051 89 GLU B C 2007 O O . GLU B 36 ? 0.3870 0.4122 0.4102 -0.0379 0.0542 0.0086 89 GLU B O 2008 C CB . GLU B 36 ? 0.3063 0.3218 0.3318 -0.0298 0.0407 0.0099 89 GLU B CB 2009 C CG . GLU B 36 ? 0.3652 0.3828 0.3888 -0.0269 0.0387 0.0069 89 GLU B CG 2010 C CD . GLU B 36 ? 0.6407 0.6547 0.6552 -0.0250 0.0356 0.0096 89 GLU B CD 2011 O OE1 . GLU B 36 ? 0.5782 0.5900 0.5849 -0.0264 0.0364 0.0138 89 GLU B OE1 2012 O OE2 . GLU B 36 ? 0.4101 0.4236 0.4255 -0.0222 0.0323 0.0078 89 GLU B OE2 2013 N N . LYS B 37 ? 0.3070 0.3381 0.3417 -0.0334 0.0519 -0.0003 90 LYS B N 2014 C CA . LYS B 37 ? 0.3086 0.3453 0.3394 -0.0358 0.0577 -0.0035 90 LYS B CA 2015 C C . LYS B 37 ? 0.4004 0.4352 0.4161 -0.0358 0.0566 -0.0006 90 LYS B C 2016 O O . LYS B 37 ? 0.4184 0.4485 0.4301 -0.0330 0.0512 0.0023 90 LYS B O 2017 C CB . LYS B 37 ? 0.3302 0.3725 0.3716 -0.0342 0.0591 -0.0107 90 LYS B CB 2018 C CG . LYS B 37 ? 0.4735 0.5199 0.5303 -0.0350 0.0615 -0.0141 90 LYS B CG 2019 C CD . LYS B 37 ? 0.5708 0.6221 0.6399 -0.0327 0.0621 -0.0208 90 LYS B CD 2020 C CE . LYS B 37 ? 0.6267 0.6825 0.7130 -0.0331 0.0638 -0.0238 90 LYS B CE 2021 N NZ . LYS B 37 ? 0.7172 0.7783 0.8169 -0.0312 0.0655 -0.0306 90 LYS B NZ 2022 N N . GLU B 38 ? 0.4096 0.4486 0.4170 -0.0393 0.0617 -0.0014 91 GLU B N 2023 C CA . GLU B 38 ? 0.4379 0.4764 0.4306 -0.0399 0.0605 0.0012 91 GLU B CA 2024 C C . GLU B 38 ? 0.4673 0.5068 0.4608 -0.0363 0.0569 -0.0031 91 GLU B C 2025 O O . GLU B 38 ? 0.4603 0.4964 0.4464 -0.0344 0.0521 0.0003 91 GLU B O 2026 C CB . GLU B 38 ? 0.4765 0.5208 0.4606 -0.0451 0.0673 -0.0002 91 GLU B CB 2027 C CG . GLU B 38 ? 0.6772 0.7216 0.6443 -0.0467 0.0658 0.0039 91 GLU B CG 2028 C CD . GLU B 38 ? 1.0494 1.0915 1.0053 -0.0508 0.0673 0.0123 91 GLU B CD 2029 O OE1 . GLU B 38 ? 1.0717 1.1142 1.0317 -0.0540 0.0723 0.0134 91 GLU B OE1 2030 O OE2 . GLU B 38 ? 0.9761 1.0161 0.9199 -0.0509 0.0634 0.0180 91 GLU B OE2 2031 N N . ASN B 39 ? 0.4058 0.4498 0.4094 -0.0354 0.0592 -0.0106 92 ASN B N 2032 C CA . ASN B 39 ? 0.3933 0.4379 0.3995 -0.0322 0.0563 -0.0150 92 ASN B CA 2033 C C . ASN B 39 ? 0.4052 0.4491 0.4273 -0.0290 0.0545 -0.0181 92 ASN B C 2034 O O . ASN B 39 ? 0.4054 0.4539 0.4375 -0.0292 0.0581 -0.0244 92 ASN B O 2035 C CB . ASN B 39 ? 0.4491 0.5001 0.4502 -0.0346 0.0608 -0.0213 92 ASN B CB 2036 C CG . ASN B 39 ? 0.7199 0.7718 0.7036 -0.0377 0.0610 -0.0175 92 ASN B CG 2037 O OD1 . ASN B 39 ? 0.7120 0.7681 0.6889 -0.0421 0.0663 -0.0179 92 ASN B OD1 2038 N ND2 . ASN B 39 ? 0.5975 0.6459 0.5739 -0.0356 0.0550 -0.0135 92 ASN B ND2 2039 N N . PRO B 40 ? 0.3315 0.3699 0.3567 -0.0264 0.0491 -0.0137 93 PRO B N 2040 C CA . PRO B 40 ? 0.3096 0.3475 0.3487 -0.0238 0.0466 -0.0157 93 PRO B CA 2041 C C . PRO B 40 ? 0.3308 0.3698 0.3750 -0.0212 0.0453 -0.0203 93 PRO B C 2042 O O . PRO B 40 ? 0.3339 0.3713 0.3702 -0.0204 0.0434 -0.0200 93 PRO B O 2043 C CB . PRO B 40 ? 0.3242 0.3560 0.3613 -0.0222 0.0412 -0.0099 93 PRO B CB 2044 C CG . PRO B 40 ? 0.3726 0.4016 0.3975 -0.0241 0.0416 -0.0051 93 PRO B CG 2045 C CD . PRO B 40 ? 0.3384 0.3709 0.3547 -0.0257 0.0448 -0.0070 93 PRO B CD 2046 N N . ARG B 41 ? 0.2676 0.3091 0.3259 -0.0200 0.0461 -0.0243 94 ARG B N 2047 C CA . ARG B 41 ? 0.2535 0.2955 0.3181 -0.0177 0.0451 -0.0285 94 ARG B CA 2048 C C . ARG B 41 ? 0.2670 0.3039 0.3340 -0.0146 0.0387 -0.0250 94 ARG B C 2049 O O . ARG B 41 ? 0.2902 0.3260 0.3576 -0.0132 0.0375 -0.0270 94 ARG B O 2050 C CB . ARG B 41 ? 0.2762 0.3234 0.3554 -0.0177 0.0495 -0.0354 94 ARG B CB 2051 C CG . ARG B 41 ? 0.4047 0.4547 0.4958 -0.0182 0.0510 -0.0355 94 ARG B CG 2052 C CD . ARG B 41 ? 0.4196 0.4749 0.5267 -0.0178 0.0553 -0.0430 94 ARG B CD 2053 N NE . ARG B 41 ? 0.4752 0.5280 0.5956 -0.0140 0.0502 -0.0424 94 ARG B NE 2054 C CZ . ARG B 41 ? 0.3900 0.4423 0.5175 -0.0120 0.0501 -0.0464 94 ARG B CZ 2055 N NH1 . ARG B 41 ? 0.2934 0.3489 0.4179 -0.0136 0.0557 -0.0533 94 ARG B NH1 2056 N NH2 . ARG B 41 ? 0.3990 0.4482 0.5378 -0.0087 0.0448 -0.0441 94 ARG B NH2 2057 N N . ASP B 42 ? 0.2086 0.2427 0.2775 -0.0140 0.0350 -0.0202 95 ASP B N 2058 C CA . ASP B 42 ? 0.2081 0.2378 0.2787 -0.0116 0.0292 -0.0168 95 ASP B CA 2059 C C . ASP B 42 ? 0.2502 0.2754 0.3080 -0.0119 0.0264 -0.0123 95 ASP B C 2060 O O . ASP B 42 ? 0.2567 0.2801 0.3115 -0.0127 0.0250 -0.0088 95 ASP B O 2061 C CB . ASP B 42 ? 0.2078 0.2379 0.2901 -0.0108 0.0262 -0.0152 95 ASP B CB 2062 C CG . ASP B 42 ? 0.2518 0.2860 0.3493 -0.0098 0.0281 -0.0196 95 ASP B CG 2063 O OD1 . ASP B 42 ? 0.2455 0.2794 0.3471 -0.0083 0.0286 -0.0226 95 ASP B OD1 2064 O OD2 . ASP B 42 ? 0.2784 0.3160 0.3850 -0.0104 0.0291 -0.0204 95 ASP B OD2 2065 N N . GLY B 43 A 0.2468 0.2705 0.2986 -0.0111 0.0258 -0.0129 95 GLY B N 2066 C CA . GLY B 43 A 0.2555 0.2754 0.2968 -0.0110 0.0235 -0.0094 95 GLY B CA 2067 C C . GLY B 43 A 0.2818 0.2989 0.3237 -0.0092 0.0202 -0.0087 95 GLY B C 2068 O O . GLY B 43 A 0.2633 0.2781 0.3091 -0.0085 0.0172 -0.0065 95 GLY B O 2069 N N . LEU B 44 ? 0.2444 0.2617 0.2813 -0.0090 0.0205 -0.0102 96 LEU B N 2070 C CA . LEU B 44 ? 0.2282 0.2431 0.2658 -0.0077 0.0182 -0.0101 96 LEU B CA 2071 C C . LEU B 44 ? 0.2892 0.3056 0.3366 -0.0070 0.0191 -0.0138 96 LEU B C 2072 O O . LEU B 44 ? 0.3180 0.3369 0.3657 -0.0073 0.0213 -0.0181 96 LEU B O 2073 C CB . LEU B 44 ? 0.2492 0.2646 0.2787 -0.0079 0.0182 -0.0107 96 LEU B CB 2074 C CG . LEU B 44 ? 0.3250 0.3374 0.3476 -0.0077 0.0160 -0.0067 96 LEU B CG 2075 C CD1 . LEU B 44 ? 0.3223 0.3335 0.3426 -0.0085 0.0163 -0.0037 96 LEU B CD1 2076 C CD2 . LEU B 44 ? 0.3598 0.3736 0.3762 -0.0077 0.0157 -0.0073 96 LEU B CD2 2077 N N . CYS B 45 ? 0.2758 0.2906 0.3317 -0.0062 0.0171 -0.0121 97 CYS B N 2078 C CA . CYS B 45 ? 0.3043 0.3193 0.3719 -0.0050 0.0173 -0.0146 97 CYS B CA 2079 C C . CYS B 45 ? 0.2554 0.2688 0.3223 -0.0047 0.0170 -0.0163 97 CYS B C 2080 O O . CYS B 45 ? 0.2108 0.2259 0.2832 -0.0046 0.0194 -0.0213 97 CYS B O 2081 C CB . CYS B 45 ? 0.3532 0.3664 0.4291 -0.0042 0.0139 -0.0108 97 CYS B CB 2082 S SG . CYS B 45 ? 0.4333 0.4420 0.5016 -0.0046 0.0092 -0.0042 97 CYS B SG 2083 N N . TYR B 46 ? 0.1982 0.2085 0.2582 -0.0048 0.0146 -0.0128 98 TYR B N 2084 C CA . TYR B 46 ? 0.1631 0.1725 0.2216 -0.0048 0.0148 -0.0147 98 TYR B CA 2085 C C . TYR B 46 ? 0.1882 0.2006 0.2375 -0.0056 0.0163 -0.0168 98 TYR B C 2086 O O . TYR B 46 ? 0.1795 0.1915 0.2213 -0.0059 0.0155 -0.0138 98 TYR B O 2087 C CB . TYR B 46 ? 0.1730 0.1784 0.2287 -0.0050 0.0121 -0.0102 98 TYR B CB 2088 C CG . TYR B 46 ? 0.1914 0.1959 0.2488 -0.0052 0.0125 -0.0124 98 TYR B CG 2089 C CD1 . TYR B 46 ? 0.2063 0.2080 0.2724 -0.0050 0.0119 -0.0117 98 TYR B CD1 2090 C CD2 . TYR B 46 ? 0.1957 0.2024 0.2473 -0.0056 0.0133 -0.0150 98 TYR B CD2 2091 C CE1 . TYR B 46 ? 0.1619 0.1627 0.2305 -0.0055 0.0125 -0.0139 98 TYR B CE1 2092 C CE2 . TYR B 46 ? 0.1964 0.2032 0.2509 -0.0059 0.0137 -0.0179 98 TYR B CE2 2093 C CZ . TYR B 46 ? 0.2082 0.2118 0.2712 -0.0060 0.0135 -0.0174 98 TYR B CZ 2094 O OH . TYR B 46 ? 0.2273 0.2306 0.2937 -0.0067 0.0141 -0.0201 98 TYR B OH 2095 N N . PRO B 47 ? 0.1702 0.1857 0.2199 -0.0061 0.0183 -0.0221 99 PRO B N 2096 C CA . PRO B 47 ? 0.1615 0.1806 0.2019 -0.0072 0.0193 -0.0236 99 PRO B CA 2097 C C . PRO B 47 ? 0.1844 0.2024 0.2168 -0.0070 0.0169 -0.0204 99 PRO B C 2098 O O . PRO B 47 ? 0.1670 0.1825 0.2014 -0.0064 0.0152 -0.0192 99 PRO B O 2099 C CB . PRO B 47 ? 0.1939 0.2169 0.2373 -0.0081 0.0218 -0.0305 99 PRO B CB 2100 C CG . PRO B 47 ? 0.2272 0.2475 0.2801 -0.0073 0.0210 -0.0320 99 PRO B CG 2101 C CD . PRO B 47 ? 0.2028 0.2192 0.2619 -0.0060 0.0199 -0.0273 99 PRO B CD 2102 N N . GLY B 48 ? 0.1792 0.1991 0.2033 -0.0076 0.0168 -0.0190 100 GLY B N 2103 C CA . GLY B 48 ? 0.1768 0.1961 0.1950 -0.0072 0.0143 -0.0161 100 GLY B CA 2104 C C . GLY B 48 ? 0.2655 0.2857 0.2759 -0.0077 0.0140 -0.0130 100 GLY B C 2105 O O . GLY B 48 ? 0.2813 0.3047 0.2881 -0.0091 0.0159 -0.0143 100 GLY B O 2106 N N . SER B 49 ? 0.2089 0.2261 0.2171 -0.0068 0.0120 -0.0087 101 SER B N 2107 C CA . SER B 49 ? 0.1979 0.2150 0.1999 -0.0070 0.0113 -0.0050 101 SER B CA 2108 C C . SER B 49 ? 0.2305 0.2431 0.2336 -0.0062 0.0105 -0.0012 101 SER B C 2109 O O . SER B 49 ? 0.2217 0.2318 0.2289 -0.0056 0.0103 -0.0016 101 SER B O 2110 C CB . SER B 49 ? 0.2656 0.2856 0.2634 -0.0068 0.0087 -0.0047 101 SER B CB 2111 O OG . SER B 49 ? 0.3755 0.3942 0.3771 -0.0053 0.0066 -0.0047 101 SER B OG 2112 N N . PHE B 50 ? 0.2215 0.2329 0.2206 -0.0065 0.0103 0.0025 102 PHE B N 2113 C CA . PHE B 50 ? 0.2247 0.2316 0.2254 -0.0060 0.0099 0.0055 102 PHE B CA 2114 C C . PHE B 50 ? 0.2406 0.2466 0.2384 -0.0053 0.0080 0.0093 102 PHE B C 2115 O O . PHE B 50 ? 0.2358 0.2431 0.2288 -0.0063 0.0081 0.0118 102 PHE B O 2116 C CB . PHE B 50 ? 0.2433 0.2491 0.2447 -0.0074 0.0122 0.0062 102 PHE B CB 2117 C CG . PHE B 50 ? 0.2575 0.2592 0.2620 -0.0074 0.0120 0.0072 102 PHE B CG 2118 C CD1 . PHE B 50 ? 0.2676 0.2691 0.2758 -0.0079 0.0125 0.0054 102 PHE B CD1 2119 C CD2 . PHE B 50 ? 0.3102 0.3085 0.3146 -0.0068 0.0111 0.0096 102 PHE B CD2 2120 C CE1 . PHE B 50 ? 0.2920 0.2905 0.3019 -0.0084 0.0121 0.0060 102 PHE B CE1 2121 C CE2 . PHE B 50 ? 0.3505 0.3455 0.3577 -0.0072 0.0113 0.0094 102 PHE B CE2 2122 C CZ . PHE B 50 ? 0.3101 0.3054 0.3191 -0.0082 0.0117 0.0075 102 PHE B CZ 2123 N N . ASN B 51 ? 0.2087 0.2128 0.2097 -0.0036 0.0061 0.0098 103 ASN B N 2124 C CA . ASN B 51 ? 0.2032 0.2064 0.2040 -0.0024 0.0037 0.0134 103 ASN B CA 2125 C C . ASN B 51 ? 0.2328 0.2316 0.2339 -0.0028 0.0044 0.0172 103 ASN B C 2126 O O . ASN B 51 ? 0.2127 0.2085 0.2163 -0.0034 0.0064 0.0161 103 ASN B O 2127 C CB . ASN B 51 ? 0.2347 0.2375 0.2410 -0.0005 0.0021 0.0120 103 ASN B CB 2128 C CG . ASN B 51 ? 0.3815 0.3889 0.3883 -0.0002 0.0009 0.0087 103 ASN B CG 2129 O OD1 . ASN B 51 ? 0.3262 0.3377 0.3289 -0.0007 -0.0006 0.0087 103 ASN B OD1 2130 N ND2 . ASN B 51 ? 0.2711 0.2779 0.2824 0.0001 0.0019 0.0055 103 ASN B ND2 2131 N N . ASP B 52 ? 0.2342 0.2327 0.2324 -0.0027 0.0025 0.0221 104 ASP B N 2132 C CA . ASP B 52 ? 0.2319 0.2256 0.2309 -0.0031 0.0031 0.0266 104 ASP B CA 2133 C C . ASP B 52 ? 0.2684 0.2607 0.2661 -0.0055 0.0067 0.0257 104 ASP B C 2134 O O . ASP B 52 ? 0.2522 0.2402 0.2541 -0.0059 0.0081 0.0260 104 ASP B O 2135 C CB . ASP B 52 ? 0.2679 0.2572 0.2750 -0.0010 0.0021 0.0268 104 ASP B CB 2136 C CG . ASP B 52 ? 0.4533 0.4443 0.4635 0.0015 -0.0017 0.0284 104 ASP B CG 2137 O OD1 . ASP B 52 ? 0.4749 0.4689 0.4801 0.0014 -0.0045 0.0320 104 ASP B OD1 2138 O OD2 . ASP B 52 ? 0.6554 0.6449 0.6731 0.0033 -0.0019 0.0260 104 ASP B OD2 2139 N N . TYR B 53 ? 0.2448 0.2414 0.2378 -0.0072 0.0083 0.0239 105 TYR B N 2140 C CA . TYR B 53 ? 0.2421 0.2388 0.2354 -0.0093 0.0117 0.0221 105 TYR B CA 2141 C C . TYR B 53 ? 0.2945 0.2884 0.2863 -0.0113 0.0133 0.0266 105 TYR B C 2142 O O . TYR B 53 ? 0.2632 0.2544 0.2592 -0.0123 0.0151 0.0260 105 TYR B O 2143 C CB . TYR B 53 ? 0.2510 0.2533 0.2413 -0.0104 0.0132 0.0184 105 TYR B CB 2144 C CG . TYR B 53 ? 0.2696 0.2729 0.2628 -0.0120 0.0163 0.0156 105 TYR B CG 2145 C CD1 . TYR B 53 ? 0.2961 0.2968 0.2951 -0.0117 0.0164 0.0142 105 TYR B CD1 2146 C CD2 . TYR B 53 ? 0.3190 0.3268 0.3097 -0.0139 0.0190 0.0136 105 TYR B CD2 2147 C CE1 . TYR B 53 ? 0.3053 0.3077 0.3082 -0.0129 0.0184 0.0117 105 TYR B CE1 2148 C CE2 . TYR B 53 ? 0.3341 0.3435 0.3296 -0.0150 0.0217 0.0107 105 TYR B CE2 2149 C CZ . TYR B 53 ? 0.3718 0.3784 0.3738 -0.0143 0.0210 0.0100 105 TYR B CZ 2150 O OH . TYR B 53 ? 0.3778 0.3865 0.3856 -0.0153 0.0230 0.0075 105 TYR B OH 2151 N N . GLU B 54 ? 0.2721 0.2665 0.2583 -0.0119 0.0122 0.0314 106 GLU B N 2152 C CA . GLU B 54 ? 0.2802 0.2715 0.2648 -0.0140 0.0137 0.0368 106 GLU B CA 2153 C C . GLU B 54 ? 0.3113 0.2958 0.3032 -0.0129 0.0129 0.0389 106 GLU B C 2154 O O . GLU B 54 ? 0.3155 0.2967 0.3100 -0.0148 0.0154 0.0401 106 GLU B O 2155 C CB . GLU B 54 ? 0.3157 0.3088 0.2918 -0.0151 0.0121 0.0424 106 GLU B CB 2156 C CG . GLU B 54 ? 0.4786 0.4788 0.4467 -0.0174 0.0141 0.0395 106 GLU B CG 2157 C CD . GLU B 54 ? 0.8545 0.8566 0.8230 -0.0203 0.0194 0.0363 106 GLU B CD 2158 O OE1 . GLU B 54 ? 0.7891 0.7880 0.7584 -0.0225 0.0218 0.0400 106 GLU B OE1 2159 O OE2 . GLU B 54 ? 0.8289 0.8358 0.7983 -0.0205 0.0212 0.0301 106 GLU B OE2 2160 N N . GLU B 55 ? 0.2695 0.2521 0.2655 -0.0099 0.0098 0.0386 107 GLU B N 2161 C CA . GLU B 55 ? 0.2613 0.2378 0.2656 -0.0085 0.0093 0.0391 107 GLU B CA 2162 C C . GLU B 55 ? 0.2607 0.2358 0.2696 -0.0096 0.0120 0.0337 107 GLU B C 2163 O O . GLU B 55 ? 0.2565 0.2268 0.2704 -0.0106 0.0134 0.0345 107 GLU B O 2164 C CB . GLU B 55 ? 0.2876 0.2640 0.2958 -0.0052 0.0060 0.0385 107 GLU B CB 2165 C CG . GLU B 55 ? 0.4744 0.4521 0.4794 -0.0039 0.0021 0.0445 107 GLU B CG 2166 C CD . GLU B 55 ? 0.7845 0.7681 0.7790 -0.0055 0.0012 0.0463 107 GLU B CD 2167 O OE1 . GLU B 55 ? 0.4292 0.4179 0.4202 -0.0062 0.0026 0.0410 107 GLU B OE1 2168 O OE2 . GLU B 55 ? 0.8233 0.8066 0.8133 -0.0062 -0.0009 0.0531 107 GLU B OE2 2169 N N . LEU B 56 ? 0.2237 0.2032 0.2310 -0.0098 0.0127 0.0286 108 LEU B N 2170 C CA . LEU B 56 ? 0.2295 0.2086 0.2402 -0.0111 0.0145 0.0242 108 LEU B CA 2171 C C . LEU B 56 ? 0.2634 0.2422 0.2741 -0.0140 0.0170 0.0255 108 LEU B C 2172 O O . LEU B 56 ? 0.2469 0.2229 0.2623 -0.0154 0.0181 0.0242 108 LEU B O 2173 C CB . LEU B 56 ? 0.2182 0.2019 0.2275 -0.0105 0.0141 0.0197 108 LEU B CB 2174 C CG . LEU B 56 ? 0.2602 0.2440 0.2723 -0.0119 0.0149 0.0160 108 LEU B CG 2175 C CD1 . LEU B 56 ? 0.2659 0.2456 0.2820 -0.0120 0.0148 0.0142 108 LEU B CD1 2176 C CD2 . LEU B 56 ? 0.2952 0.2831 0.3062 -0.0114 0.0143 0.0131 108 LEU B CD2 2177 N N . LYS B 57 ? 0.2462 0.2284 0.2521 -0.0152 0.0181 0.0277 109 LYS B N 2178 C CA . LYS B 57 ? 0.2452 0.2279 0.2514 -0.0182 0.0212 0.0289 109 LYS B CA 2179 C C . LYS B 57 ? 0.3160 0.2926 0.3250 -0.0194 0.0218 0.0333 109 LYS B C 2180 O O . LYS B 57 ? 0.3354 0.3102 0.3490 -0.0217 0.0239 0.0324 109 LYS B O 2181 C CB . LYS B 57 ? 0.2666 0.2542 0.2663 -0.0196 0.0229 0.0302 109 LYS B CB 2182 C CG . LYS B 57 ? 0.3476 0.3408 0.3472 -0.0189 0.0231 0.0248 109 LYS B CG 2183 C CD . LYS B 57 ? 0.4144 0.4126 0.4075 -0.0200 0.0247 0.0250 109 LYS B CD 2184 C CE . LYS B 57 ? 0.4090 0.4122 0.4055 -0.0208 0.0271 0.0197 109 LYS B CE 2185 N NZ . LYS B 57 ? 0.5834 0.5920 0.5742 -0.0226 0.0300 0.0187 109 LYS B NZ 2186 N N . HIS B 58 ? 0.2801 0.2531 0.2881 -0.0177 0.0197 0.0378 110 HIS B N 2187 C CA . HIS B 58 ? 0.2991 0.2654 0.3116 -0.0184 0.0200 0.0422 110 HIS B CA 2188 C C . HIS B 58 ? 0.3283 0.2904 0.3495 -0.0181 0.0202 0.0378 110 HIS B C 2189 O O . HIS B 58 ? 0.3122 0.2701 0.3385 -0.0202 0.0221 0.0388 110 HIS B O 2190 C CB . HIS B 58 ? 0.3337 0.2973 0.3446 -0.0162 0.0168 0.0482 110 HIS B CB 2191 C CG . HIS B 58 ? 0.4083 0.3645 0.4243 -0.0169 0.0170 0.0541 110 HIS B CG 2192 N ND1 . HIS B 58 ? 0.4538 0.4078 0.4699 -0.0206 0.0202 0.0571 110 HIS B ND1 2193 C CD2 . HIS B 58 ? 0.4515 0.4023 0.4735 -0.0144 0.0143 0.0577 110 HIS B CD2 2194 C CE1 . HIS B 58 ? 0.4556 0.4023 0.4775 -0.0203 0.0194 0.0625 110 HIS B CE1 2195 N NE2 . HIS B 58 ? 0.4580 0.4025 0.4839 -0.0165 0.0157 0.0632 110 HIS B NE2 2196 N N . LEU B 59 ? 0.2784 0.2419 0.3012 -0.0160 0.0187 0.0327 111 LEU B N 2197 C CA . LEU B 59 ? 0.2851 0.2457 0.3147 -0.0163 0.0192 0.0277 111 LEU B CA 2198 C C . LEU B 59 ? 0.3186 0.2814 0.3491 -0.0195 0.0211 0.0243 111 LEU B C 2199 O O . LEU B 59 ? 0.3292 0.2884 0.3655 -0.0214 0.0224 0.0227 111 LEU B O 2200 C CB . LEU B 59 ? 0.2830 0.2455 0.3126 -0.0139 0.0175 0.0231 111 LEU B CB 2201 C CG . LEU B 59 ? 0.3626 0.3250 0.3953 -0.0152 0.0183 0.0165 111 LEU B CG 2202 C CD1 . LEU B 59 ? 0.3768 0.3334 0.4169 -0.0154 0.0193 0.0148 111 LEU B CD1 2203 C CD2 . LEU B 59 ? 0.3913 0.3576 0.4208 -0.0137 0.0171 0.0128 111 LEU B CD2 2204 N N . LEU B 60 ? 0.2789 0.2476 0.3048 -0.0200 0.0213 0.0233 112 LEU B N 2205 C CA . LEU B 60 ? 0.2944 0.2662 0.3225 -0.0227 0.0226 0.0204 112 LEU B CA 2206 C C . LEU B 60 ? 0.3297 0.2991 0.3615 -0.0258 0.0253 0.0229 112 LEU B C 2207 O O . LEU B 60 ? 0.3229 0.2933 0.3594 -0.0283 0.0261 0.0199 112 LEU B O 2208 C CB . LEU B 60 ? 0.2965 0.2748 0.3211 -0.0223 0.0224 0.0189 112 LEU B CB 2209 C CG . LEU B 60 ? 0.3598 0.3402 0.3820 -0.0199 0.0199 0.0160 112 LEU B CG 2210 C CD1 . LEU B 60 ? 0.3700 0.3558 0.3895 -0.0192 0.0199 0.0153 112 LEU B CD1 2211 C CD2 . LEU B 60 ? 0.4104 0.3907 0.4357 -0.0208 0.0186 0.0118 112 LEU B CD2 2212 N N A SER B 61 ? 0.2985 0.2648 0.3283 -0.0260 0.0264 0.0288 113 SER B N 2213 N N B SER B 61 ? 0.2786 0.2449 0.3084 -0.0260 0.0264 0.0288 113 SER B N 2214 C CA A SER B 61 ? 0.3069 0.2700 0.3400 -0.0292 0.0292 0.0323 113 SER B CA 2215 C CA B SER B 61 ? 0.2769 0.2400 0.3100 -0.0292 0.0293 0.0322 113 SER B CA 2216 C C A SER B 61 ? 0.3617 0.3188 0.4033 -0.0304 0.0296 0.0303 113 SER B C 2217 C C B SER B 61 ? 0.3475 0.3046 0.3891 -0.0304 0.0296 0.0303 113 SER B C 2218 O O A SER B 61 ? 0.3668 0.3222 0.4131 -0.0337 0.0321 0.0310 113 SER B O 2219 O O B SER B 61 ? 0.3519 0.3073 0.3983 -0.0338 0.0321 0.0310 113 SER B O 2220 C CB A SER B 61 ? 0.3816 0.3421 0.4096 -0.0290 0.0297 0.0399 113 SER B CB 2221 C CB B SER B 61 ? 0.3164 0.2772 0.3444 -0.0292 0.0299 0.0399 113 SER B CB 2222 O OG A SER B 61 ? 0.5103 0.4767 0.5299 -0.0282 0.0295 0.0409 113 SER B OG 2223 O OG B SER B 61 ? 0.2965 0.2507 0.3269 -0.0271 0.0279 0.0434 113 SER B OG 2224 N N . SER B 62 ? 0.3052 0.2595 0.3493 -0.0281 0.0274 0.0271 114 SER B N 2225 C CA . SER B 62 ? 0.2907 0.2394 0.3431 -0.0293 0.0280 0.0239 114 SER B CA 2226 C C . SER B 62 ? 0.3251 0.2774 0.3789 -0.0302 0.0270 0.0158 114 SER B C 2227 O O . SER B 62 ? 0.3473 0.2960 0.4068 -0.0313 0.0273 0.0115 114 SER B O 2228 C CB . SER B 62 ? 0.3591 0.3018 0.4145 -0.0264 0.0268 0.0259 114 SER B CB 2229 O OG . SER B 62 ? 0.4589 0.4050 0.5100 -0.0232 0.0246 0.0232 114 SER B OG 2230 N N . VAL B 63 ? 0.2428 0.2019 0.2911 -0.0297 0.0256 0.0139 115 VAL B N 2231 C CA . VAL B 63 ? 0.2220 0.1851 0.2701 -0.0307 0.0239 0.0076 115 VAL B CA 2232 C C . VAL B 63 ? 0.2675 0.2352 0.3180 -0.0337 0.0243 0.0067 115 VAL B C 2233 O O . VAL B 63 ? 0.2398 0.2104 0.2886 -0.0335 0.0254 0.0101 115 VAL B O 2234 C CB . VAL B 63 ? 0.2566 0.2239 0.2981 -0.0279 0.0216 0.0067 115 VAL B CB 2235 C CG1 . VAL B 63 ? 0.2445 0.2161 0.2849 -0.0293 0.0196 0.0016 115 VAL B CG1 2236 C CG2 . VAL B 63 ? 0.2666 0.2300 0.3072 -0.0251 0.0214 0.0070 115 VAL B CG2 2237 N N . LYS B 64 ? 0.2044 0.1732 0.2591 -0.0365 0.0235 0.0016 116 LYS B N 2238 C CA . LYS B 64 ? 0.2050 0.1791 0.2637 -0.0394 0.0231 0.0000 116 LYS B CA 2239 C C . LYS B 64 ? 0.2529 0.2330 0.3099 -0.0399 0.0193 -0.0042 116 LYS B C 2240 O O . LYS B 64 ? 0.2376 0.2230 0.2987 -0.0418 0.0180 -0.0054 116 LYS B O 2241 C CB . LYS B 64 ? 0.2124 0.1830 0.2792 -0.0431 0.0253 -0.0013 116 LYS B CB 2242 C CG . LYS B 64 ? 0.2640 0.2292 0.3325 -0.0431 0.0290 0.0044 116 LYS B CG 2243 C CD . LYS B 64 ? 0.2766 0.2461 0.3424 -0.0426 0.0305 0.0090 116 LYS B CD 2244 C CE . LYS B 64 ? 0.2428 0.2074 0.3075 -0.0427 0.0338 0.0155 116 LYS B CE 2245 N NZ . LYS B 64 ? 0.2821 0.2455 0.3388 -0.0389 0.0328 0.0194 116 LYS B NZ 2246 N N . HIS B 65 A 0.1994 0.1789 0.2505 -0.0383 0.0173 -0.0062 116 HIS B N 2247 C CA . HIS B 65 A 0.2012 0.1861 0.2493 -0.0389 0.0134 -0.0090 116 HIS B CA 2248 C C . HIS B 65 A 0.2724 0.2559 0.3133 -0.0368 0.0125 -0.0097 116 HIS B C 2249 O O . HIS B 65 A 0.2540 0.2326 0.2944 -0.0365 0.0145 -0.0112 116 HIS B O 2250 C CB . HIS B 65 A 0.2210 0.2077 0.2725 -0.0431 0.0116 -0.0141 116 HIS B CB 2251 C CG . HIS B 65 A 0.2671 0.2605 0.3161 -0.0441 0.0068 -0.0153 116 HIS B CG 2252 N ND1 . HIS B 65 A 0.3054 0.3006 0.3516 -0.0472 0.0040 -0.0199 116 HIS B ND1 2253 C CD2 . HIS B 65 A 0.2840 0.2825 0.3333 -0.0423 0.0043 -0.0122 116 HIS B CD2 2254 C CE1 . HIS B 65 A 0.3002 0.3014 0.3441 -0.0472 -0.0006 -0.0186 116 HIS B CE1 2255 N NE2 . HIS B 65 A 0.2944 0.2977 0.3412 -0.0441 -0.0006 -0.0140 116 HIS B NE2 2256 N N . PHE B 66 B 0.2316 0.2196 0.2681 -0.0357 0.0096 -0.0089 116 PHE B N 2257 C CA . PHE B 66 B 0.2330 0.2206 0.2626 -0.0344 0.0086 -0.0097 116 PHE B CA 2258 C C . PHE B 66 B 0.3350 0.3270 0.3612 -0.0371 0.0047 -0.0121 116 PHE B C 2259 O O . PHE B 66 B 0.3369 0.3334 0.3663 -0.0383 0.0018 -0.0112 116 PHE B O 2260 C CB . PHE B 66 B 0.2481 0.2373 0.2752 -0.0309 0.0082 -0.0057 116 PHE B CB 2261 C CG . PHE B 66 B 0.2608 0.2465 0.2880 -0.0280 0.0112 -0.0031 116 PHE B CG 2262 C CD1 . PHE B 66 B 0.3194 0.3005 0.3455 -0.0272 0.0131 -0.0042 116 PHE B CD1 2263 C CD2 . PHE B 66 B 0.2885 0.2758 0.3170 -0.0262 0.0119 0.0003 116 PHE B CD2 2264 C CE1 . PHE B 66 B 0.3215 0.2998 0.3479 -0.0244 0.0148 -0.0012 116 PHE B CE1 2265 C CE2 . PHE B 66 B 0.3286 0.3134 0.3558 -0.0238 0.0139 0.0029 116 PHE B CE2 2266 C CZ . PHE B 66 B 0.3207 0.3010 0.3468 -0.0229 0.0150 0.0025 116 PHE B CZ 2267 N N . GLU B 67 C 0.2701 0.2613 0.2900 -0.0381 0.0046 -0.0148 116 GLU B N 2268 C CA . GLU B 67 C 0.2823 0.2779 0.2963 -0.0407 0.0006 -0.0158 116 GLU B CA 2269 C C . GLU B 67 C 0.2713 0.2666 0.2793 -0.0383 0.0006 -0.0131 116 GLU B C 2270 O O . GLU B 67 C 0.2492 0.2411 0.2552 -0.0371 0.0039 -0.0146 116 GLU B O 2271 C CB . GLU B 67 C 0.3215 0.3168 0.3319 -0.0450 0.0010 -0.0218 116 GLU B CB 2272 C CG . GLU B 67 C 0.4904 0.4869 0.5069 -0.0480 0.0000 -0.0247 116 GLU B CG 2273 C CD . GLU B 67 C 0.7975 0.7926 0.8131 -0.0523 0.0017 -0.0320 116 GLU B CD 2274 O OE1 . GLU B 67 C 0.7072 0.6996 0.7182 -0.0526 0.0047 -0.0353 116 GLU B OE1 2275 O OE2 . GLU B 67 C 0.7955 0.7923 0.8161 -0.0554 0.0004 -0.0348 116 GLU B OE2 2276 N N . LYS B 68 ? 0.2659 0.2647 0.2728 -0.0372 -0.0029 -0.0091 117 LYS B N 2277 C CA . LYS B 68 ? 0.2698 0.2682 0.2714 -0.0354 -0.0029 -0.0066 117 LYS B CA 2278 C C . LYS B 68 ? 0.3276 0.3267 0.3202 -0.0389 -0.0035 -0.0090 117 LYS B C 2279 O O . LYS B 68 ? 0.3694 0.3718 0.3588 -0.0425 -0.0071 -0.0100 117 LYS B O 2280 C CB . LYS B 68 ? 0.3238 0.3254 0.3281 -0.0336 -0.0067 -0.0017 117 LYS B CB 2281 C CG . LYS B 68 ? 0.4781 0.4781 0.4867 -0.0295 -0.0044 0.0007 117 LYS B CG 2282 C CD . LYS B 68 ? 0.3985 0.4018 0.4135 -0.0277 -0.0073 0.0041 117 LYS B CD 2283 C CE . LYS B 68 ? 0.4156 0.4201 0.4278 -0.0277 -0.0108 0.0073 117 LYS B CE 2284 N NZ . LYS B 68 ? 0.4176 0.4246 0.4384 -0.0254 -0.0130 0.0102 117 LYS B NZ 2285 N N . VAL B 69 ? 0.2563 0.2528 0.2449 -0.0382 -0.0001 -0.0104 118 VAL B N 2286 C CA . VAL B 69 ? 0.2792 0.2764 0.2590 -0.0417 0.0010 -0.0135 118 VAL B CA 2287 C C . VAL B 69 ? 0.2927 0.2900 0.2681 -0.0405 0.0010 -0.0098 118 VAL B C 2288 O O . VAL B 69 ? 0.2737 0.2688 0.2531 -0.0368 0.0033 -0.0083 118 VAL B O 2289 C CB . VAL B 69 ? 0.3235 0.3173 0.3050 -0.0422 0.0063 -0.0197 118 VAL B CB 2290 C CG1 . VAL B 69 ? 0.3421 0.3364 0.3157 -0.0452 0.0092 -0.0236 118 VAL B CG1 2291 C CG2 . VAL B 69 ? 0.3226 0.3159 0.3083 -0.0443 0.0063 -0.0236 118 VAL B CG2 2292 N N . LYS B 70 ? 0.2912 0.2911 0.2579 -0.0440 -0.0016 -0.0080 119 LYS B N 2293 C CA . LYS B 70 ? 0.2978 0.2973 0.2609 -0.0432 -0.0012 -0.0042 119 LYS B CA 2294 C C . LYS B 70 ? 0.3810 0.3788 0.3404 -0.0443 0.0046 -0.0088 119 LYS B C 2295 O O . LYS B 70 ? 0.4556 0.4549 0.4069 -0.0489 0.0060 -0.0123 119 LYS B O 2296 C CB . LYS B 70 ? 0.3400 0.3424 0.2956 -0.0464 -0.0062 0.0006 119 LYS B CB 2297 C CG . LYS B 70 ? 0.4193 0.4206 0.3747 -0.0447 -0.0068 0.0062 119 LYS B CG 2298 C CD . LYS B 70 ? 0.4839 0.4875 0.4332 -0.0476 -0.0125 0.0124 119 LYS B CD 2299 C CE . LYS B 70 ? 0.6547 0.6593 0.6129 -0.0446 -0.0181 0.0175 119 LYS B CE 2300 N NZ . LYS B 70 ? 0.7860 0.7931 0.7395 -0.0474 -0.0247 0.0238 119 LYS B NZ 2301 N N . ILE B 71 ? 0.2740 0.2694 0.2399 -0.0404 0.0080 -0.0093 120 ILE B N 2302 C CA . ILE B 71 ? 0.2733 0.2674 0.2391 -0.0405 0.0135 -0.0138 120 ILE B CA 2303 C C . ILE B 71 ? 0.3313 0.3259 0.2928 -0.0413 0.0149 -0.0115 120 ILE B C 2304 O O . ILE B 71 ? 0.3400 0.3349 0.2987 -0.0434 0.0194 -0.0155 120 ILE B O 2305 C CB . ILE B 71 ? 0.2955 0.2869 0.2714 -0.0358 0.0158 -0.0155 120 ILE B CB 2306 C CG1 . ILE B 71 ? 0.2936 0.2844 0.2748 -0.0314 0.0139 -0.0104 120 ILE B CG1 2307 C CG2 . ILE B 71 ? 0.3233 0.3134 0.3032 -0.0359 0.0154 -0.0181 120 ILE B CG2 2308 C CD1 . ILE B 71 ? 0.3172 0.3059 0.3067 -0.0272 0.0159 -0.0114 120 ILE B CD1 2309 N N . LEU B 72 ? 0.2842 0.2789 0.2470 -0.0394 0.0117 -0.0055 121 LEU B N 2310 C CA . LEU B 72 ? 0.2838 0.2785 0.2439 -0.0401 0.0129 -0.0028 121 LEU B CA 2311 C C . LEU B 72 ? 0.3115 0.3069 0.2680 -0.0413 0.0077 0.0041 121 LEU B C 2312 O O . LEU B 72 ? 0.2807 0.2751 0.2434 -0.0380 0.0056 0.0081 121 LEU B O 2313 C CB . LEU B 72 ? 0.2838 0.2770 0.2526 -0.0356 0.0150 -0.0028 121 LEU B CB 2314 C CG . LEU B 72 ? 0.3573 0.3500 0.3306 -0.0342 0.0199 -0.0086 121 LEU B CG 2315 C CD1 . LEU B 72 ? 0.3464 0.3384 0.3286 -0.0295 0.0201 -0.0077 121 LEU B CD1 2316 C CD2 . LEU B 72 ? 0.3691 0.3630 0.3378 -0.0378 0.0245 -0.0116 121 LEU B CD2 2317 N N . PRO B 73 ? 0.3143 0.3115 0.2612 -0.0461 0.0055 0.0055 122 PRO B N 2318 C CA . PRO B 73 ? 0.3199 0.3178 0.2643 -0.0471 -0.0003 0.0130 122 PRO B CA 2319 C C . PRO B 73 ? 0.3637 0.3595 0.3107 -0.0457 0.0003 0.0178 122 PRO B C 2320 O O . PRO B 73 ? 0.3601 0.3553 0.3035 -0.0476 0.0049 0.0161 122 PRO B O 2321 C CB . PRO B 73 ? 0.3652 0.3656 0.2963 -0.0535 -0.0016 0.0131 122 PRO B CB 2322 C CG . PRO B 73 ? 0.4193 0.4208 0.3483 -0.0552 0.0026 0.0046 122 PRO B CG 2323 C CD . PRO B 73 ? 0.3431 0.3422 0.2812 -0.0510 0.0080 0.0002 122 PRO B CD 2324 N N . LYS B 74 ? 0.3047 0.2996 0.2592 -0.0426 -0.0040 0.0231 123 LYS B N 2325 C CA . LYS B 74 ? 0.3145 0.3069 0.2735 -0.0412 -0.0041 0.0279 123 LYS B CA 2326 C C . LYS B 74 ? 0.3482 0.3402 0.2974 -0.0461 -0.0032 0.0318 123 LYS B C 2327 O O . LYS B 74 ? 0.3232 0.3131 0.2749 -0.0459 -0.0003 0.0330 123 LYS B O 2328 C CB . LYS B 74 ? 0.3709 0.3628 0.3383 -0.0383 -0.0099 0.0335 123 LYS B CB 2329 C CG . LYS B 74 ? 0.6433 0.6350 0.6228 -0.0331 -0.0094 0.0307 123 LYS B CG 2330 C CD . LYS B 74 ? 0.8115 0.8017 0.8010 -0.0304 -0.0129 0.0356 123 LYS B CD 2331 C CE . LYS B 74 ? 1.0119 1.0040 1.0053 -0.0299 -0.0190 0.0392 123 LYS B CE 2332 N NZ . LYS B 74 ? 1.1402 1.1309 1.1461 -0.0267 -0.0217 0.0430 123 LYS B NZ 2333 N N . ASP B 75 ? 0.3087 0.3028 0.2465 -0.0510 -0.0059 0.0337 125 ASP B N 2334 C CA . ASP B 75 ? 0.3250 0.3191 0.2512 -0.0566 -0.0052 0.0380 125 ASP B CA 2335 C C . ASP B 75 ? 0.3497 0.3439 0.2710 -0.0592 0.0028 0.0327 125 ASP B C 2336 O O . ASP B 75 ? 0.3468 0.3404 0.2607 -0.0635 0.0047 0.0363 125 ASP B O 2337 C CB . ASP B 75 ? 0.3792 0.3764 0.2934 -0.0615 -0.0101 0.0407 125 ASP B CB 2338 C CG . ASP B 75 ? 0.5676 0.5683 0.4741 -0.0645 -0.0074 0.0326 125 ASP B CG 2339 O OD1 . ASP B 75 ? 0.5385 0.5387 0.4494 -0.0625 -0.0015 0.0247 125 ASP B OD1 2340 O OD2 . ASP B 75 ? 0.7073 0.7111 0.6032 -0.0692 -0.0113 0.0341 125 ASP B OD2 2341 N N . ARG B 76 ? 0.3067 0.3016 0.2327 -0.0569 0.0075 0.0243 126 ARG B N 2342 C CA . ARG B 76 ? 0.3047 0.3001 0.2285 -0.0590 0.0151 0.0186 126 ARG B CA 2343 C C . ARG B 76 ? 0.3293 0.3224 0.2606 -0.0570 0.0180 0.0206 126 ARG B C 2344 O O . ARG B 76 ? 0.3368 0.3307 0.2660 -0.0597 0.0239 0.0176 126 ARG B O 2345 C CB . ARG B 76 ? 0.2915 0.2881 0.2206 -0.0564 0.0187 0.0096 126 ARG B CB 2346 C CG . ARG B 76 ? 0.3082 0.3030 0.2512 -0.0497 0.0182 0.0083 126 ARG B CG 2347 C CD . ARG B 76 ? 0.3310 0.3264 0.2789 -0.0473 0.0209 0.0009 126 ARG B CD 2348 N NE . ARG B 76 ? 0.3564 0.3533 0.3012 -0.0504 0.0273 -0.0055 126 ARG B NE 2349 C CZ . ARG B 76 ? 0.4164 0.4135 0.3660 -0.0498 0.0320 -0.0079 126 ARG B CZ 2350 N NH1 . ARG B 76 ? 0.3896 0.3854 0.3462 -0.0466 0.0309 -0.0043 126 ARG B NH1 2351 N NH2 . ARG B 76 ? 0.4345 0.4335 0.3822 -0.0528 0.0381 -0.0141 126 ARG B NH2 2352 N N . TRP B 77 ? 0.2575 0.2482 0.1986 -0.0525 0.0142 0.0248 127 TRP B N 2353 C CA . TRP B 77 ? 0.2571 0.2458 0.2070 -0.0503 0.0165 0.0256 127 TRP B CA 2354 C C . TRP B 77 ? 0.3178 0.3043 0.2644 -0.0536 0.0153 0.0334 127 TRP B C 2355 O O . TRP B 77 ? 0.3357 0.3194 0.2897 -0.0511 0.0115 0.0386 127 TRP B O 2356 C CB . TRP B 77 ? 0.2350 0.2227 0.1975 -0.0440 0.0137 0.0248 127 TRP B CB 2357 C CG . TRP B 77 ? 0.2278 0.2172 0.1936 -0.0408 0.0144 0.0185 127 TRP B CG 2358 C CD1 . TRP B 77 ? 0.2564 0.2461 0.2246 -0.0381 0.0104 0.0186 127 TRP B CD1 2359 C CD2 . TRP B 77 ? 0.2226 0.2133 0.1915 -0.0395 0.0192 0.0117 127 TRP B CD2 2360 N NE1 . TRP B 77 ? 0.2562 0.2470 0.2275 -0.0358 0.0126 0.0126 127 TRP B NE1 2361 C CE2 . TRP B 77 ? 0.2713 0.2626 0.2438 -0.0362 0.0176 0.0086 127 TRP B CE2 2362 C CE3 . TRP B 77 ? 0.2463 0.2380 0.2170 -0.0406 0.0245 0.0081 127 TRP B CE3 2363 C CZ2 . TRP B 77 ? 0.2570 0.2493 0.2336 -0.0342 0.0209 0.0026 127 TRP B CZ2 2364 C CZ3 . TRP B 77 ? 0.2549 0.2481 0.2308 -0.0383 0.0276 0.0017 127 TRP B CZ3 2365 C CH2 . TRP B 77 ? 0.2609 0.2541 0.2398 -0.0349 0.0255 -0.0006 127 TRP B CH2 2366 N N . THR B 78 ? 0.2967 0.2841 0.2325 -0.0595 0.0190 0.0341 128 THR B N 2367 C CA . THR B 78 ? 0.2966 0.2816 0.2272 -0.0637 0.0181 0.0426 128 THR B CA 2368 C C . THR B 78 ? 0.3474 0.3298 0.2874 -0.0629 0.0215 0.0436 128 THR B C 2369 O O . THR B 78 ? 0.3681 0.3475 0.3063 -0.0657 0.0202 0.0515 128 THR B O 2370 C CB . THR B 78 ? 0.4037 0.3912 0.3181 -0.0712 0.0214 0.0427 128 THR B CB 2371 O OG1 . THR B 78 ? 0.3691 0.3590 0.2842 -0.0726 0.0297 0.0343 128 THR B OG1 2372 C CG2 . THR B 78 ? 0.3532 0.3435 0.2573 -0.0731 0.0174 0.0421 128 THR B CG2 2373 N N . GLN B 79 ? 0.2909 0.2744 0.2405 -0.0595 0.0258 0.0361 129 GLN B N 2374 C CA . GLN B 79 ? 0.2807 0.2624 0.2398 -0.0590 0.0291 0.0364 129 GLN B CA 2375 C C . GLN B 79 ? 0.2828 0.2630 0.2562 -0.0527 0.0262 0.0348 129 GLN B C 2376 O O . GLN B 79 ? 0.2666 0.2458 0.2491 -0.0518 0.0287 0.0334 129 GLN B O 2377 C CB . GLN B 79 ? 0.3018 0.2867 0.2611 -0.0613 0.0368 0.0293 129 GLN B CB 2378 C CG . GLN B 79 ? 0.2780 0.2650 0.2228 -0.0680 0.0408 0.0293 129 GLN B CG 2379 C CD . GLN B 79 ? 0.3636 0.3479 0.2996 -0.0739 0.0404 0.0385 129 GLN B CD 2380 O OE1 . GLN B 79 ? 0.3405 0.3215 0.2832 -0.0741 0.0405 0.0432 129 GLN B OE1 2381 N NE2 . GLN B 79 ? 0.3391 0.3249 0.2597 -0.0793 0.0403 0.0410 129 GLN B NE2 2382 N N . HIS B 80 ? 0.2369 0.2172 0.2122 -0.0488 0.0211 0.0348 130 HIS B N 2383 C CA . HIS B 80 ? 0.2229 0.2022 0.2107 -0.0432 0.0186 0.0331 130 HIS B CA 2384 C C . HIS B 80 ? 0.2786 0.2555 0.2680 -0.0417 0.0123 0.0394 130 HIS B C 2385 O O . HIS B 80 ? 0.2840 0.2613 0.2645 -0.0439 0.0093 0.0433 130 HIS B O 2386 C CB . HIS B 80 ? 0.2055 0.1882 0.1957 -0.0394 0.0193 0.0256 130 HIS B CB 2387 C CG . HIS B 80 ? 0.2431 0.2285 0.2345 -0.0399 0.0248 0.0192 130 HIS B CG 2388 N ND1 . HIS B 80 ? 0.2662 0.2536 0.2492 -0.0434 0.0284 0.0167 130 HIS B ND1 2389 C CD2 . HIS B 80 ? 0.2613 0.2477 0.2620 -0.0378 0.0271 0.0151 130 HIS B CD2 2390 C CE1 . HIS B 80 ? 0.2658 0.2555 0.2545 -0.0428 0.0328 0.0112 130 HIS B CE1 2391 N NE2 . HIS B 80 ? 0.2628 0.2521 0.2620 -0.0395 0.0318 0.0102 130 HIS B NE2 2392 N N . THR B 81 ? 0.2285 0.2035 0.2298 -0.0379 0.0103 0.0396 131 THR B N 2393 C CA . THR B 81 ? 0.2313 0.2047 0.2375 -0.0355 0.0047 0.0440 131 THR B CA 2394 C C . THR B 81 ? 0.2591 0.2359 0.2654 -0.0321 0.0033 0.0389 131 THR B C 2395 O O . THR B 81 ? 0.2184 0.1974 0.2274 -0.0299 0.0063 0.0322 131 THR B O 2396 C CB . THR B 81 ? 0.2424 0.2125 0.2625 -0.0330 0.0040 0.0451 131 THR B CB 2397 O OG1 . THR B 81 ? 0.2827 0.2490 0.3027 -0.0366 0.0055 0.0503 131 THR B OG1 2398 C CG2 . THR B 81 ? 0.2754 0.2440 0.3034 -0.0300 -0.0013 0.0487 131 THR B CG2 2399 N N . THR B 82 ? 0.2206 0.1980 0.2240 -0.0319 -0.0013 0.0423 132 THR B N 2400 C CA . THR B 82 ? 0.2159 0.1964 0.2199 -0.0292 -0.0025 0.0380 132 THR B CA 2401 C C . THR B 82 ? 0.2487 0.2290 0.2625 -0.0259 -0.0071 0.0402 132 THR B C 2402 O O . THR B 82 ? 0.2461 0.2290 0.2610 -0.0240 -0.0080 0.0371 132 THR B O 2403 C CB . THR B 82 ? 0.2931 0.2758 0.2849 -0.0324 -0.0034 0.0383 132 THR B CB 2404 O OG1 . THR B 82 ? 0.3292 0.3110 0.3167 -0.0351 -0.0081 0.0458 132 THR B OG1 2405 C CG2 . THR B 82 ? 0.2927 0.2764 0.2758 -0.0355 0.0018 0.0346 132 THR B CG2 2406 N N . THR B 83 ? 0.2632 0.2405 0.2849 -0.0254 -0.0094 0.0451 133 THR B N 2407 C CA . THR B 83 ? 0.2646 0.2417 0.2979 -0.0223 -0.0138 0.0475 133 THR B CA 2408 C C . THR B 83 ? 0.3142 0.2918 0.3599 -0.0183 -0.0112 0.0413 133 THR B C 2409 O O . THR B 83 ? 0.3133 0.2911 0.3701 -0.0156 -0.0136 0.0417 133 THR B O 2410 C CB . THR B 83 ? 0.3436 0.3166 0.3814 -0.0236 -0.0174 0.0560 133 THR B CB 2411 O OG1 . THR B 83 ? 0.3442 0.3138 0.3857 -0.0242 -0.0136 0.0555 133 THR B OG1 2412 C CG2 . THR B 83 ? 0.3735 0.3466 0.3989 -0.0279 -0.0212 0.0633 133 THR B CG2 2413 N N . GLY B 84 ? 0.2598 0.2379 0.3036 -0.0181 -0.0064 0.0356 134 GLY B N 2414 C CA . GLY B 84 ? 0.2653 0.2443 0.3187 -0.0151 -0.0037 0.0294 134 GLY B CA 2415 C C . GLY B 84 ? 0.2951 0.2770 0.3536 -0.0123 -0.0047 0.0263 134 GLY B C 2416 O O . GLY B 84 ? 0.2587 0.2434 0.3103 -0.0125 -0.0050 0.0251 134 GLY B O 2417 N N . GLY B 85 ? 0.2731 0.2545 0.3444 -0.0101 -0.0050 0.0250 135 GLY B N 2418 C CA . GLY B 85 ? 0.2637 0.2483 0.3423 -0.0076 -0.0050 0.0213 135 GLY B CA 2419 C C . GLY B 85 ? 0.2885 0.2735 0.3776 -0.0057 -0.0018 0.0151 135 GLY B C 2420 O O . GLY B 85 ? 0.3088 0.2909 0.4023 -0.0062 -0.0005 0.0147 135 GLY B O 2421 N N . SER B 86 ? 0.2326 0.2213 0.3257 -0.0041 -0.0002 0.0100 136 SER B N 2422 C CA . SER B 86 ? 0.2257 0.2157 0.3278 -0.0028 0.0034 0.0030 136 SER B CA 2423 C C . SER B 86 ? 0.2585 0.2508 0.3730 -0.0009 0.0034 0.0007 136 SER B C 2424 O O . SER B 86 ? 0.2247 0.2192 0.3380 -0.0005 0.0015 0.0031 136 SER B O 2425 C CB . SER B 86 ? 0.2521 0.2458 0.3446 -0.0034 0.0068 -0.0027 136 SER B CB 2426 O OG . SER B 86 ? 0.3101 0.3061 0.4098 -0.0027 0.0101 -0.0099 136 SER B OG 2427 N N . ARG B 87 ? 0.2311 0.2234 0.3584 0.0003 0.0061 -0.0048 137 ARG B N 2428 C CA . ARG B 87 ? 0.2507 0.2458 0.3913 0.0021 0.0071 -0.0084 137 ARG B CA 2429 C C . ARG B 87 ? 0.2988 0.2997 0.4311 0.0015 0.0105 -0.0137 137 ARG B C 2430 O O . ARG B 87 ? 0.3229 0.3273 0.4625 0.0024 0.0117 -0.0162 137 ARG B O 2431 C CB . ARG B 87 ? 0.2448 0.2387 0.4012 0.0031 0.0100 -0.0143 137 ARG B CB 2432 C CG . ARG B 87 ? 0.5191 0.5066 0.6836 0.0033 0.0073 -0.0092 137 ARG B CG 2433 C CD . ARG B 87 ? 0.6683 0.6540 0.8546 0.0054 0.0080 -0.0121 137 ARG B CD 2434 N NE . ARG B 87 ? 0.7736 0.7588 0.9701 0.0074 0.0035 -0.0059 137 ARG B NE 2435 C CZ . ARG B 87 ? 0.9544 0.9345 1.1548 0.0078 -0.0020 0.0039 137 ARG B CZ 2436 N NH1 . ARG B 87 ? 0.7588 0.7335 0.9534 0.0061 -0.0031 0.0085 137 ARG B NH1 2437 N NH2 . ARG B 87 ? 0.8105 0.7911 1.0204 0.0096 -0.0066 0.0092 137 ARG B NH2 2438 N N . ALA B 88 ? 0.2581 0.2600 0.3756 -0.0001 0.0119 -0.0149 138 ALA B N 2439 C CA . ALA B 88 ? 0.2488 0.2555 0.3573 -0.0009 0.0145 -0.0183 138 ALA B CA 2440 C C . ALA B 88 ? 0.3383 0.3458 0.4428 -0.0010 0.0121 -0.0133 138 ALA B C 2441 O O . ALA B 88 ? 0.3759 0.3872 0.4781 -0.0014 0.0144 -0.0159 138 ALA B O 2442 C CB . ALA B 88 ? 0.2534 0.2605 0.3483 -0.0023 0.0156 -0.0195 138 ALA B CB 2443 N N . CYS B 89 ? 0.3175 0.3217 0.4209 -0.0009 0.0076 -0.0065 139 CYS B N 2444 C CA . CYS B 89 ? 0.3366 0.3417 0.4362 -0.0014 0.0047 -0.0020 139 CYS B CA 2445 C C . CYS B 89 ? 0.3531 0.3572 0.4651 -0.0002 0.0006 0.0021 139 CYS B C 2446 O O . CYS B 89 ? 0.3198 0.3228 0.4280 -0.0009 -0.0038 0.0080 139 CYS B O 2447 C CB . CYS B 89 ? 0.3764 0.3793 0.4616 -0.0030 0.0028 0.0021 139 CYS B CB 2448 S SG . CYS B 89 ? 0.4453 0.4493 0.5174 -0.0040 0.0066 -0.0017 139 CYS B SG 2449 N N . ALA B 90 ? 0.3368 0.3415 0.4642 0.0016 0.0018 -0.0010 140 ALA B N 2450 C CA . ALA B 90 ? 0.3396 0.3430 0.4817 0.0032 -0.0024 0.0031 140 ALA B CA 2451 C C . ALA B 90 ? 0.3813 0.3879 0.5273 0.0035 -0.0059 0.0063 140 ALA B C 2452 O O . ALA B 90 ? 0.3967 0.4078 0.5428 0.0032 -0.0030 0.0020 140 ALA B O 2453 C CB . ALA B 90 ? 0.3512 0.3546 0.5105 0.0052 0.0005 -0.0022 140 ALA B CB 2454 N N . VAL B 91 ? 0.3135 0.3180 0.4632 0.0038 -0.0123 0.0138 141 VAL B N 2455 C CA . VAL B 91 ? 0.3060 0.3140 0.4608 0.0039 -0.0172 0.0176 141 VAL B CA 2456 C C . VAL B 91 ? 0.3677 0.3742 0.5400 0.0062 -0.0227 0.0227 141 VAL B C 2457 O O . VAL B 91 ? 0.3348 0.3363 0.5048 0.0058 -0.0265 0.0290 141 VAL B O 2458 C CB . VAL B 91 ? 0.3545 0.3622 0.4920 0.0011 -0.0208 0.0225 141 VAL B CB 2459 C CG1 . VAL B 91 ? 0.3563 0.3678 0.4994 0.0010 -0.0266 0.0263 141 VAL B CG1 2460 C CG2 . VAL B 91 ? 0.3465 0.3553 0.4695 -0.0006 -0.0156 0.0177 141 VAL B CG2 2461 N N . SER B 92 ? 0.3535 0.3644 0.5437 0.0083 -0.0232 0.0203 142 SER B N 2462 C CA . SER B 92 ? 0.3673 0.3775 0.5779 0.0110 -0.0284 0.0245 142 SER B CA 2463 C C . SER B 92 ? 0.4072 0.4113 0.6257 0.0125 -0.0272 0.0250 142 SER B C 2464 O O . SER B 92 ? 0.3933 0.3931 0.6174 0.0133 -0.0333 0.0331 142 SER B O 2465 C CB . SER B 92 ? 0.4455 0.4561 0.6533 0.0102 -0.0377 0.0343 142 SER B CB 2466 O OG . SER B 92 ? 0.5807 0.5974 0.7849 0.0089 -0.0388 0.0329 142 SER B OG 2467 N N . GLY B 93 ? 0.3710 0.3746 0.5885 0.0125 -0.0195 0.0165 143 GLY B N 2468 C CA . GLY B 93 ? 0.3755 0.3740 0.6008 0.0135 -0.0167 0.0143 143 GLY B CA 2469 C C . GLY B 93 ? 0.3906 0.3829 0.6016 0.0115 -0.0181 0.0196 143 GLY B C 2470 O O . GLY B 93 ? 0.4088 0.3961 0.6281 0.0122 -0.0171 0.0196 143 GLY B O 2471 N N . ASN B 94 ? 0.3229 0.3152 0.5134 0.0088 -0.0201 0.0240 144 ASN B N 2472 C CA . ASN B 94 ? 0.3014 0.2886 0.4780 0.0065 -0.0210 0.0289 144 ASN B CA 2473 C C . ASN B 94 ? 0.3255 0.3143 0.4828 0.0042 -0.0162 0.0240 144 ASN B C 2474 O O . ASN B 94 ? 0.3143 0.3079 0.4649 0.0037 -0.0149 0.0209 144 ASN B O 2475 C CB . ASN B 94 ? 0.3108 0.2961 0.4813 0.0051 -0.0286 0.0398 144 ASN B CB 2476 C CG . ASN B 94 ? 0.6049 0.5883 0.7944 0.0075 -0.0345 0.0460 144 ASN B CG 2477 O OD1 . ASN B 94 ? 0.4485 0.4271 0.6505 0.0089 -0.0339 0.0469 144 ASN B OD1 2478 N ND2 . ASN B 94 ? 0.5291 0.5163 0.7223 0.0080 -0.0403 0.0504 144 ASN B ND2 2479 N N . PRO B 95 ? 0.2751 0.2600 0.4242 0.0026 -0.0140 0.0241 145 PRO B N 2480 C CA . PRO B 95 ? 0.2698 0.2563 0.4022 0.0006 -0.0101 0.0200 145 PRO B CA 2481 C C . PRO B 95 ? 0.2796 0.2675 0.3973 -0.0014 -0.0130 0.0246 145 PRO B C 2482 O O . PRO B 95 ? 0.3043 0.2900 0.4190 -0.0026 -0.0179 0.0322 145 PRO B O 2483 C CB . PRO B 95 ? 0.3048 0.2866 0.4345 -0.0007 -0.0086 0.0210 145 PRO B CB 2484 C CG . PRO B 95 ? 0.3732 0.3513 0.5207 0.0010 -0.0097 0.0223 145 PRO B CG 2485 C CD . PRO B 95 ? 0.3170 0.2959 0.4724 0.0024 -0.0152 0.0282 145 PRO B CD 2486 N N . SER B 96 ? 0.2421 0.2336 0.3501 -0.0020 -0.0101 0.0200 146 SER B N 2487 C CA . SER B 96 ? 0.2231 0.2159 0.3177 -0.0040 -0.0122 0.0231 146 SER B CA 2488 C C . SER B 96 ? 0.2269 0.2207 0.3089 -0.0052 -0.0079 0.0185 146 SER B C 2489 O O . SER B 96 ? 0.1871 0.1801 0.2693 -0.0048 -0.0044 0.0146 146 SER B O 2490 C CB . SER B 96 ? 0.2745 0.2711 0.3743 -0.0033 -0.0149 0.0237 146 SER B CB 2491 O OG . SER B 96 ? 0.4029 0.4001 0.4920 -0.0056 -0.0186 0.0281 146 SER B OG 2492 N N . PHE B 97 ? 0.2125 0.2079 0.2843 -0.0067 -0.0085 0.0192 147 PHE B N 2493 C CA . PHE B 97 ? 0.1878 0.1838 0.2492 -0.0075 -0.0050 0.0156 147 PHE B CA 2494 C C . PHE B 97 ? 0.2013 0.1998 0.2573 -0.0083 -0.0052 0.0149 147 PHE B C 2495 O O . PHE B 97 ? 0.1999 0.1996 0.2583 -0.0088 -0.0086 0.0176 147 PHE B O 2496 C CB . PHE B 97 ? 0.2019 0.1949 0.2542 -0.0094 -0.0047 0.0177 147 PHE B CB 2497 C CG . PHE B 97 ? 0.2050 0.1984 0.2509 -0.0095 -0.0009 0.0136 147 PHE B CG 2498 C CD1 . PHE B 97 ? 0.2182 0.2125 0.2687 -0.0080 0.0019 0.0091 147 PHE B CD1 2499 C CD2 . PHE B 97 ? 0.2179 0.2110 0.2535 -0.0112 -0.0003 0.0139 147 PHE B CD2 2500 C CE1 . PHE B 97 ? 0.2010 0.1961 0.2459 -0.0081 0.0045 0.0059 147 PHE B CE1 2501 C CE2 . PHE B 97 ? 0.2192 0.2126 0.2507 -0.0110 0.0027 0.0105 147 PHE B CE2 2502 C CZ . PHE B 97 ? 0.1807 0.1753 0.2167 -0.0094 0.0047 0.0069 147 PHE B CZ 2503 N N . PHE B 98 ? 0.1884 0.1875 0.2375 -0.0085 -0.0020 0.0116 148 PHE B N 2504 C CA . PHE B 98 ? 0.1517 0.1522 0.1950 -0.0095 -0.0016 0.0109 148 PHE B CA 2505 C C . PHE B 98 ? 0.2110 0.2106 0.2491 -0.0117 -0.0050 0.0144 148 PHE B C 2506 O O . PHE B 98 ? 0.2374 0.2349 0.2700 -0.0130 -0.0057 0.0164 148 PHE B O 2507 C CB . PHE B 98 ? 0.1680 0.1677 0.2037 -0.0096 0.0016 0.0084 148 PHE B CB 2508 C CG . PHE B 98 ? 0.1876 0.1888 0.2259 -0.0081 0.0046 0.0048 148 PHE B CG 2509 C CD1 . PHE B 98 ? 0.2045 0.2083 0.2452 -0.0078 0.0063 0.0028 148 PHE B CD1 2510 C CD2 . PHE B 98 ? 0.2037 0.2042 0.2413 -0.0076 0.0058 0.0033 148 PHE B CD2 2511 C CE1 . PHE B 98 ? 0.1993 0.2051 0.2404 -0.0070 0.0092 -0.0005 148 PHE B CE1 2512 C CE2 . PHE B 98 ? 0.2385 0.2410 0.2773 -0.0066 0.0083 -0.0003 148 PHE B CE2 2513 C CZ . PHE B 98 ? 0.1961 0.2013 0.2359 -0.0065 0.0099 -0.0021 148 PHE B CZ 2514 N N . ARG B 99 ? 0.1675 0.1693 0.2075 -0.0124 -0.0070 0.0150 149 ARG B N 2515 C CA . ARG B 99 ? 0.1809 0.1828 0.2164 -0.0148 -0.0110 0.0181 149 ARG B CA 2516 C C . ARG B 99 ? 0.2341 0.2345 0.2584 -0.0172 -0.0097 0.0172 149 ARG B C 2517 O O . ARG B 99 ? 0.2454 0.2454 0.2638 -0.0196 -0.0124 0.0195 149 ARG B O 2518 C CB . ARG B 99 ? 0.1585 0.1638 0.1993 -0.0153 -0.0134 0.0181 149 ARG B CB 2519 C CG . ARG B 99 ? 0.3704 0.3782 0.4246 -0.0131 -0.0146 0.0184 149 ARG B CG 2520 C CD . ARG B 99 ? 0.3685 0.3751 0.4286 -0.0119 -0.0177 0.0221 149 ARG B CD 2521 N NE . ARG B 99 ? 0.2873 0.2970 0.3618 -0.0101 -0.0200 0.0226 149 ARG B NE 2522 C CZ . ARG B 99 ? 0.4891 0.4986 0.5718 -0.0092 -0.0246 0.0270 149 ARG B CZ 2523 N NH1 . ARG B 99 ? 0.3040 0.3101 0.3805 -0.0103 -0.0273 0.0317 149 ARG B NH1 2524 N NH2 . ARG B 99 ? 0.2995 0.3123 0.3971 -0.0073 -0.0266 0.0270 149 ARG B NH2 2525 N N . ASN B 100 ? 0.1770 0.1765 0.1985 -0.0166 -0.0058 0.0137 150 ASN B N 2526 C CA . ASN B 100 ? 0.1847 0.1828 0.1978 -0.0186 -0.0043 0.0121 150 ASN B CA 2527 C C . ASN B 100 ? 0.2436 0.2395 0.2523 -0.0184 -0.0019 0.0115 150 ASN B C 2528 O O . ASN B 100 ? 0.2123 0.2072 0.2151 -0.0200 -0.0001 0.0097 150 ASN B O 2529 C CB . ASN B 100 ? 0.1655 0.1637 0.1793 -0.0182 -0.0020 0.0093 150 ASN B CB 2530 C CG . ASN B 100 ? 0.2269 0.2275 0.2450 -0.0192 -0.0041 0.0095 150 ASN B CG 2531 O OD1 . ASN B 100 ? 0.2348 0.2370 0.2530 -0.0207 -0.0078 0.0114 150 ASN B OD1 2532 N ND2 . ASN B 100 ? 0.2039 0.2050 0.2258 -0.0183 -0.0019 0.0080 150 ASN B ND2 2533 N N . MET B 101 ? 0.1962 0.1917 0.2090 -0.0166 -0.0015 0.0125 151 MET B N 2534 C CA . MET B 101 ? 0.1728 0.1669 0.1836 -0.0162 0.0011 0.0114 151 MET B CA 2535 C C . MET B 101 ? 0.2114 0.2043 0.2218 -0.0174 -0.0003 0.0145 151 MET B C 2536 O O . MET B 101 ? 0.1953 0.1884 0.2089 -0.0176 -0.0035 0.0178 151 MET B O 2537 C CB . MET B 101 ? 0.1916 0.1864 0.2076 -0.0134 0.0031 0.0091 151 MET B CB 2538 C CG . MET B 101 ? 0.2164 0.2121 0.2323 -0.0124 0.0045 0.0070 151 MET B CG 2539 S SD . MET B 101 ? 0.2697 0.2640 0.2796 -0.0138 0.0057 0.0056 151 MET B SD 2540 C CE . MET B 101 ? 0.2216 0.2155 0.2312 -0.0123 0.0080 0.0038 151 MET B CE 2541 N N . VAL B 102 ? 0.1835 0.1752 0.1909 -0.0182 0.0020 0.0138 152 VAL B N 2542 C CA . VAL B 102 ? 0.1728 0.1630 0.1793 -0.0199 0.0015 0.0170 152 VAL B CA 2543 C C . VAL B 102 ? 0.2048 0.1944 0.2159 -0.0184 0.0041 0.0150 152 VAL B C 2544 O O . VAL B 102 ? 0.1957 0.1861 0.2054 -0.0180 0.0068 0.0115 152 VAL B O 2545 C CB . VAL B 102 ? 0.2287 0.2186 0.2257 -0.0237 0.0024 0.0177 152 VAL B CB 2546 C CG1 . VAL B 102 ? 0.2531 0.2412 0.2485 -0.0261 0.0020 0.0220 152 VAL B CG1 2547 C CG2 . VAL B 102 ? 0.2297 0.2207 0.2211 -0.0258 0.0000 0.0185 152 VAL B CG2 2548 N N . TRP B 103 ? 0.1664 0.1549 0.1839 -0.0176 0.0030 0.0171 153 TRP B N 2549 C CA . TRP B 103 ? 0.1846 0.1727 0.2071 -0.0166 0.0053 0.0147 153 TRP B CA 2550 C C . TRP B 103 ? 0.2161 0.2023 0.2355 -0.0195 0.0065 0.0173 153 TRP B C 2551 O O . TRP B 103 ? 0.2242 0.2080 0.2450 -0.0209 0.0045 0.0221 153 TRP B O 2552 C CB . TRP B 103 ? 0.1921 0.1797 0.2244 -0.0145 0.0039 0.0151 153 TRP B CB 2553 C CG . TRP B 103 ? 0.2022 0.1900 0.2405 -0.0134 0.0061 0.0114 153 TRP B CG 2554 C CD1 . TRP B 103 ? 0.2295 0.2181 0.2660 -0.0141 0.0086 0.0086 153 TRP B CD1 2555 C CD2 . TRP B 103 ? 0.2050 0.1933 0.2526 -0.0114 0.0061 0.0089 153 TRP B CD2 2556 N NE1 . TRP B 103 ? 0.2067 0.1963 0.2503 -0.0128 0.0097 0.0048 153 TRP B NE1 2557 C CE2 . TRP B 103 ? 0.2547 0.2440 0.3049 -0.0113 0.0085 0.0047 153 TRP B CE2 2558 C CE3 . TRP B 103 ? 0.2384 0.2271 0.2929 -0.0098 0.0046 0.0090 153 TRP B CE3 2559 C CZ2 . TRP B 103 ? 0.2658 0.2562 0.3243 -0.0099 0.0093 0.0005 153 TRP B CZ2 2560 C CZ3 . TRP B 103 ? 0.2675 0.2570 0.3310 -0.0083 0.0060 0.0048 153 TRP B CZ3 2561 C CH2 . TRP B 103 ? 0.2760 0.2662 0.3410 -0.0085 0.0083 0.0005 153 TRP B CH2 2562 N N . LEU B 104 ? 0.1839 0.1710 0.1996 -0.0207 0.0097 0.0144 154 LEU B N 2563 C CA . LEU B 104 ? 0.1824 0.1681 0.1951 -0.0240 0.0117 0.0164 154 LEU B CA 2564 C C . LEU B 104 ? 0.2092 0.1939 0.2303 -0.0233 0.0130 0.0155 154 LEU B C 2565 O O . LEU B 104 ? 0.1814 0.1682 0.2075 -0.0211 0.0143 0.0107 154 LEU B O 2566 C CB . LEU B 104 ? 0.2020 0.1896 0.2093 -0.0255 0.0153 0.0127 154 LEU B CB 2567 C CG . LEU B 104 ? 0.3071 0.2955 0.3057 -0.0272 0.0151 0.0125 154 LEU B CG 2568 C CD1 . LEU B 104 ? 0.3559 0.3455 0.3561 -0.0242 0.0132 0.0104 154 LEU B CD1 2569 C CD2 . LEU B 104 ? 0.3742 0.3643 0.3697 -0.0290 0.0195 0.0084 154 LEU B CD2 2570 N N . THR B 105 ? 0.1845 0.1662 0.2071 -0.0255 0.0125 0.0203 155 THR B N 2571 C CA . THR B 105 ? 0.1905 0.1707 0.2217 -0.0254 0.0140 0.0194 155 THR B CA 2572 C C . THR B 105 ? 0.2311 0.2091 0.2592 -0.0297 0.0162 0.0232 155 THR B C 2573 O O . THR B 105 ? 0.2183 0.1959 0.2368 -0.0327 0.0163 0.0268 155 THR B O 2574 C CB . THR B 105 ? 0.2202 0.1982 0.2612 -0.0231 0.0112 0.0210 155 THR B CB 2575 O OG1 . THR B 105 ? 0.2397 0.2144 0.2793 -0.0243 0.0079 0.0281 155 THR B OG1 2576 C CG2 . THR B 105 ? 0.2154 0.1963 0.2599 -0.0193 0.0101 0.0161 155 THR B CG2 2577 N N . GLU B 106 ? 0.1937 0.1703 0.2296 -0.0303 0.0182 0.0222 156 GLU B N 2578 C CA . GLU B 106 ? 0.1974 0.1718 0.2312 -0.0347 0.0210 0.0259 156 GLU B CA 2579 C C . GLU B 106 ? 0.2673 0.2374 0.2963 -0.0375 0.0185 0.0349 156 GLU B C 2580 O O . GLU B 106 ? 0.2626 0.2306 0.2951 -0.0354 0.0142 0.0385 156 GLU B O 2581 C CB . GLU B 106 ? 0.2174 0.1909 0.2624 -0.0350 0.0236 0.0231 156 GLU B CB 2582 C CG . GLU B 106 ? 0.2677 0.2377 0.3238 -0.0327 0.0208 0.0244 156 GLU B CG 2583 C CD . GLU B 106 ? 0.6505 0.6144 0.7095 -0.0352 0.0195 0.0327 156 GLU B CD 2584 O OE1 . GLU B 106 ? 0.6989 0.6595 0.7679 -0.0330 0.0170 0.0340 156 GLU B OE1 2585 O OE2 . GLU B 106 ? 0.5591 0.5212 0.6102 -0.0395 0.0210 0.0382 156 GLU B OE2 2586 N N . LYS B 107 ? 0.2555 0.2248 0.2769 -0.0424 0.0213 0.0385 157 LYS B N 2587 C CA . LYS B 107 ? 0.2750 0.2404 0.2899 -0.0460 0.0189 0.0479 157 LYS B CA 2588 C C . LYS B 107 ? 0.3569 0.3196 0.3736 -0.0504 0.0232 0.0507 157 LYS B C 2589 O O . LYS B 107 ? 0.3300 0.2957 0.3442 -0.0528 0.0286 0.0459 157 LYS B O 2590 C CB . LYS B 107 ? 0.3097 0.2778 0.3093 -0.0487 0.0183 0.0494 157 LYS B CB 2591 C CG . LYS B 107 ? 0.3522 0.3171 0.3433 -0.0528 0.0149 0.0597 157 LYS B CG 2592 C CD . LYS B 107 ? 0.3448 0.3133 0.3201 -0.0559 0.0145 0.0599 157 LYS B CD 2593 C CE . LYS B 107 ? 0.4626 0.4287 0.4278 -0.0610 0.0114 0.0702 157 LYS B CE 2594 N NZ . LYS B 107 ? 0.4547 0.4246 0.4032 -0.0652 0.0115 0.0699 157 LYS B NZ 2595 N N . GLY B 108 ? 0.3769 0.3341 0.3998 -0.0513 0.0209 0.0579 158 GLY B N 2596 C CA . GLY B 108 ? 0.3978 0.3514 0.4235 -0.0558 0.0246 0.0618 158 GLY B CA 2597 C C . GLY B 108 ? 0.4635 0.4193 0.4988 -0.0553 0.0300 0.0534 158 GLY B C 2598 O O . GLY B 108 ? 0.4718 0.4283 0.5045 -0.0600 0.0354 0.0532 158 GLY B O 2599 N N . SER B 109 ? 0.4141 0.3718 0.4603 -0.0501 0.0287 0.0461 159 SER B N 2600 C CA . SER B 109 ? 0.4079 0.3685 0.4642 -0.0489 0.0323 0.0375 159 SER B CA 2601 C C . SER B 109 ? 0.4347 0.4017 0.4844 -0.0501 0.0366 0.0312 159 SER B C 2602 O O . SER B 109 ? 0.4592 0.4284 0.5148 -0.0519 0.0409 0.0266 159 SER B O 2603 C CB . SER B 109 ? 0.4909 0.4469 0.5579 -0.0518 0.0348 0.0399 159 SER B CB 2604 O OG . SER B 109 ? 0.7129 0.6722 0.7904 -0.0509 0.0379 0.0312 159 SER B OG 2605 N N . ASN B 110 ? 0.3393 0.3093 0.3777 -0.0493 0.0354 0.0308 160 ASN B N 2606 C CA . ASN B 110 ? 0.3140 0.2897 0.3476 -0.0500 0.0392 0.0245 160 ASN B CA 2607 C C . ASN B 110 ? 0.3032 0.2819 0.3318 -0.0460 0.0361 0.0214 160 ASN B C 2608 O O . ASN B 110 ? 0.2919 0.2683 0.3149 -0.0451 0.0320 0.0260 160 ASN B O 2609 C CB . ASN B 110 ? 0.3708 0.3467 0.3936 -0.0560 0.0437 0.0278 160 ASN B CB 2610 C CG . ASN B 110 ? 0.7925 0.7672 0.8210 -0.0605 0.0487 0.0288 160 ASN B CG 2611 O OD1 . ASN B 110 ? 0.8522 0.8219 0.8787 -0.0643 0.0488 0.0366 160 ASN B OD1 2612 N ND2 . ASN B 110 ? 0.6675 0.6467 0.7043 -0.0601 0.0528 0.0212 160 ASN B ND2 2613 N N . TYR B 111 ? 0.2587 0.2424 0.2896 -0.0439 0.0379 0.0141 161 TYR B N 2614 C CA . TYR B 111 ? 0.2245 0.2109 0.2507 -0.0406 0.0357 0.0110 161 TYR B CA 2615 C C . TYR B 111 ? 0.2758 0.2663 0.2986 -0.0425 0.0404 0.0064 161 TYR B C 2616 O O . TYR B 111 ? 0.2661 0.2604 0.2969 -0.0408 0.0422 0.0006 161 TYR B O 2617 C CB . TYR B 111 ? 0.2131 0.2014 0.2473 -0.0352 0.0325 0.0066 161 TYR B CB 2618 C CG . TYR B 111 ? 0.1994 0.1893 0.2284 -0.0321 0.0298 0.0051 161 TYR B CG 2619 C CD1 . TYR B 111 ? 0.1846 0.1726 0.2128 -0.0296 0.0256 0.0076 161 TYR B CD1 2620 C CD2 . TYR B 111 ? 0.2033 0.1966 0.2295 -0.0318 0.0319 0.0010 161 TYR B CD2 2621 C CE1 . TYR B 111 ? 0.1813 0.1707 0.2053 -0.0271 0.0235 0.0062 161 TYR B CE1 2622 C CE2 . TYR B 111 ? 0.2099 0.2041 0.2324 -0.0291 0.0297 -0.0002 161 TYR B CE2 2623 C CZ . TYR B 111 ? 0.2305 0.2228 0.2514 -0.0270 0.0255 0.0026 161 TYR B CZ 2624 O OH . TYR B 111 ? 0.2516 0.2449 0.2695 -0.0246 0.0237 0.0012 161 TYR B OH 2625 N N . PRO B 112 ? 0.2543 0.2446 0.2663 -0.0465 0.0428 0.0085 162 PRO B N 2626 C CA . PRO B 112 ? 0.2532 0.2478 0.2639 -0.0482 0.0480 0.0028 162 PRO B CA 2627 C C . PRO B 112 ? 0.2667 0.2638 0.2783 -0.0438 0.0460 -0.0019 162 PRO B C 2628 O O . PRO B 112 ? 0.2426 0.2380 0.2535 -0.0403 0.0409 -0.0001 162 PRO B O 2629 C CB . PRO B 112 ? 0.2977 0.2913 0.2955 -0.0543 0.0511 0.0064 162 PRO B CB 2630 C CG . PRO B 112 ? 0.3424 0.3316 0.3335 -0.0547 0.0459 0.0142 162 PRO B CG 2631 C CD . PRO B 112 ? 0.3044 0.2913 0.3054 -0.0497 0.0408 0.0156 162 PRO B CD 2632 N N . VAL B 113 ? 0.2731 0.2740 0.2873 -0.0440 0.0500 -0.0080 163 VAL B N 2633 C CA . VAL B 113 ? 0.2680 0.2706 0.2840 -0.0398 0.0480 -0.0119 163 VAL B CA 2634 C C . VAL B 113 ? 0.2900 0.2901 0.2946 -0.0407 0.0456 -0.0090 163 VAL B C 2635 O O . VAL B 113 ? 0.3276 0.3270 0.3223 -0.0455 0.0481 -0.0072 163 VAL B O 2636 C CB . VAL B 113 ? 0.3340 0.3408 0.3559 -0.0399 0.0529 -0.0189 163 VAL B CB 2637 C CG1 . VAL B 113 ? 0.3267 0.3344 0.3527 -0.0350 0.0501 -0.0220 163 VAL B CG1 2638 C CG2 . VAL B 113 ? 0.3432 0.3532 0.3766 -0.0399 0.0556 -0.0217 163 VAL B CG2 2639 N N . ALA B 114 ? 0.2330 0.2320 0.2387 -0.0365 0.0408 -0.0083 164 ALA B N 2640 C CA . ALA B 114 ? 0.2221 0.2192 0.2194 -0.0366 0.0378 -0.0061 164 ALA B CA 2641 C C . ALA B 114 ? 0.2736 0.2725 0.2720 -0.0353 0.0396 -0.0116 164 ALA B C 2642 O O . ALA B 114 ? 0.2666 0.2666 0.2736 -0.0312 0.0388 -0.0144 164 ALA B O 2643 C CB . ALA B 114 ? 0.2409 0.2361 0.2408 -0.0327 0.0321 -0.0027 164 ALA B CB 2644 N N . LYS B 115 ? 0.2216 0.2206 0.2117 -0.0389 0.0419 -0.0130 165 LYS B N 2645 C CA . LYS B 115 ? 0.2172 0.2173 0.2087 -0.0382 0.0440 -0.0187 165 LYS B CA 2646 C C . LYS B 115 ? 0.2652 0.2639 0.2473 -0.0401 0.0417 -0.0175 165 LYS B C 2647 O O . LYS B 115 ? 0.2780 0.2763 0.2500 -0.0442 0.0411 -0.0141 165 LYS B O 2648 C CB . LYS B 115 ? 0.2622 0.2651 0.2551 -0.0415 0.0510 -0.0244 165 LYS B CB 2649 C CG . LYS B 115 ? 0.3667 0.3720 0.3727 -0.0386 0.0531 -0.0274 165 LYS B CG 2650 C CD . LYS B 115 ? 0.5269 0.5355 0.5356 -0.0422 0.0605 -0.0335 165 LYS B CD 2651 C CE . LYS B 115 ? 0.7104 0.7219 0.7314 -0.0404 0.0623 -0.0353 165 LYS B CE 2652 N NZ . LYS B 115 ? 0.8489 0.8643 0.8740 -0.0440 0.0702 -0.0416 165 LYS B NZ 2653 N N . GLY B 116 ? 0.2203 0.2183 0.2060 -0.0372 0.0403 -0.0201 166 GLY B N 2654 C CA . GLY B 116 ? 0.2326 0.2297 0.2110 -0.0389 0.0383 -0.0200 166 GLY B CA 2655 C C . GLY B 116 ? 0.2711 0.2676 0.2559 -0.0365 0.0394 -0.0252 166 GLY B C 2656 O O . GLY B 116 ? 0.2540 0.2502 0.2488 -0.0320 0.0389 -0.0259 166 GLY B O 2657 N N . SER B 117 ? 0.2341 0.2307 0.2135 -0.0396 0.0408 -0.0286 167 SER B N 2658 C CA . SER B 117 ? 0.2329 0.2282 0.2191 -0.0376 0.0419 -0.0336 167 SER B CA 2659 C C . SER B 117 ? 0.2636 0.2580 0.2430 -0.0401 0.0398 -0.0342 167 SER B C 2660 O O . SER B 117 ? 0.2480 0.2438 0.2165 -0.0445 0.0386 -0.0325 167 SER B O 2661 C CB . SER B 117 ? 0.3087 0.3056 0.3007 -0.0387 0.0485 -0.0411 167 SER B CB 2662 O OG . SER B 117 ? 0.4075 0.4058 0.3915 -0.0444 0.0526 -0.0465 167 SER B OG 2663 N N . TYR B 118 ? 0.2282 0.2205 0.2146 -0.0374 0.0389 -0.0362 168 TYR B N 2664 C CA . TYR B 118 ? 0.2292 0.2206 0.2111 -0.0397 0.0370 -0.0374 168 TYR B CA 2665 C C . TYR B 118 ? 0.2415 0.2307 0.2326 -0.0385 0.0400 -0.0437 168 TYR B C 2666 O O . TYR B 118 ? 0.2090 0.1958 0.2105 -0.0337 0.0394 -0.0424 168 TYR B O 2667 C CB . TYR B 118 ? 0.2268 0.2172 0.2081 -0.0374 0.0308 -0.0306 168 TYR B CB 2668 C CG . TYR B 118 ? 0.2395 0.2291 0.2192 -0.0392 0.0289 -0.0323 168 TYR B CG 2669 C CD1 . TYR B 118 ? 0.2655 0.2574 0.2353 -0.0445 0.0280 -0.0339 168 TYR B CD1 2670 C CD2 . TYR B 118 ? 0.2326 0.2193 0.2211 -0.0362 0.0284 -0.0329 168 TYR B CD2 2671 C CE1 . TYR B 118 ? 0.2743 0.2660 0.2434 -0.0466 0.0263 -0.0364 168 TYR B CE1 2672 C CE2 . TYR B 118 ? 0.2389 0.2248 0.2271 -0.0382 0.0271 -0.0349 168 TYR B CE2 2673 C CZ . TYR B 118 ? 0.2811 0.2697 0.2600 -0.0434 0.0260 -0.0370 168 TYR B CZ 2674 O OH . TYR B 118 ? 0.2953 0.2835 0.2752 -0.0455 0.0248 -0.0398 168 TYR B OH 2675 N N . ASN B 119 ? 0.2170 0.2069 0.2042 -0.0431 0.0430 -0.0503 169 ASN B N 2676 C CA . ASN B 119 ? 0.2186 0.2059 0.2153 -0.0424 0.0461 -0.0570 169 ASN B CA 2677 C C . ASN B 119 ? 0.2688 0.2542 0.2644 -0.0428 0.0419 -0.0551 169 ASN B C 2678 O O . ASN B 119 ? 0.2685 0.2562 0.2535 -0.0470 0.0395 -0.0546 169 ASN B O 2679 C CB . ASN B 119 ? 0.2263 0.2158 0.2195 -0.0477 0.0522 -0.0663 169 ASN B CB 2680 C CG . ASN B 119 ? 0.4349 0.4216 0.4398 -0.0471 0.0561 -0.0743 169 ASN B CG 2681 O OD1 . ASN B 119 ? 0.3184 0.3010 0.3327 -0.0434 0.0537 -0.0723 169 ASN B OD1 2682 N ND2 . ASN B 119 ? 0.3859 0.3747 0.3905 -0.0512 0.0627 -0.0838 169 ASN B ND2 2683 N N . ASN B 120 ? 0.2126 0.1939 0.2191 -0.0386 0.0408 -0.0537 170 ASN B N 2684 C CA . ASN B 120 ? 0.2277 0.2073 0.2343 -0.0390 0.0373 -0.0516 170 ASN B CA 2685 C C . ASN B 120 ? 0.2920 0.2711 0.2984 -0.0436 0.0397 -0.0596 170 ASN B C 2686 O O . ASN B 120 ? 0.2806 0.2558 0.2978 -0.0423 0.0420 -0.0634 170 ASN B O 2687 C CB . ASN B 120 ? 0.2143 0.1898 0.2314 -0.0338 0.0355 -0.0469 170 ASN B CB 2688 C CG . ASN B 120 ? 0.2906 0.2645 0.3082 -0.0342 0.0323 -0.0441 170 ASN B CG 2689 O OD1 . ASN B 120 ? 0.2587 0.2348 0.2691 -0.0382 0.0305 -0.0455 170 ASN B OD1 2690 N ND2 . ASN B 120 ? 0.2361 0.2059 0.2626 -0.0305 0.0314 -0.0404 170 ASN B ND2 2691 N N . THR B 121 ? 0.2603 0.2434 0.2546 -0.0490 0.0387 -0.0617 171 THR B N 2692 C CA . THR B 121 ? 0.2758 0.2595 0.2682 -0.0541 0.0403 -0.0696 171 THR B CA 2693 C C . THR B 121 ? 0.3452 0.3293 0.3357 -0.0553 0.0347 -0.0661 171 THR B C 2694 O O . THR B 121 ? 0.3584 0.3443 0.3449 -0.0603 0.0346 -0.0718 171 THR B O 2695 C CB . THR B 121 ? 0.3377 0.3265 0.3172 -0.0601 0.0426 -0.0746 171 THR B CB 2696 O OG1 . THR B 121 ? 0.3644 0.3567 0.3324 -0.0610 0.0375 -0.0667 171 THR B OG1 2697 C CG2 . THR B 121 ? 0.3128 0.3017 0.2956 -0.0598 0.0492 -0.0798 171 THR B CG2 2698 N N . SER B 122 ? 0.2964 0.2792 0.2900 -0.0510 0.0304 -0.0573 172 SER B N 2699 C CA . SER B 122 ? 0.3008 0.2845 0.2941 -0.0516 0.0254 -0.0534 172 SER B CA 2700 C C . SER B 122 ? 0.3785 0.3590 0.3805 -0.0529 0.0265 -0.0580 172 SER B C 2701 O O . SER B 122 ? 0.4141 0.3967 0.4149 -0.0553 0.0230 -0.0574 172 SER B O 2702 C CB . SER B 122 ? 0.3248 0.3079 0.3206 -0.0467 0.0220 -0.0442 172 SER B CB 2703 O OG . SER B 122 ? 0.2978 0.2760 0.3045 -0.0425 0.0239 -0.0426 172 SER B OG 2704 N N . GLY B 123 ? 0.3062 0.2818 0.3182 -0.0512 0.0312 -0.0625 173 GLY B N 2705 C CA . GLY B 123 ? 0.3086 0.2801 0.3305 -0.0523 0.0326 -0.0665 173 GLY B CA 2706 C C . GLY B 123 ? 0.3476 0.3137 0.3802 -0.0473 0.0321 -0.0599 173 GLY B C 2707 O O . GLY B 123 ? 0.3702 0.3319 0.4126 -0.0477 0.0337 -0.0621 173 GLY B O 2708 N N . GLU B 124 ? 0.2830 0.2497 0.3139 -0.0430 0.0300 -0.0518 174 GLU B N 2709 C CA . GLU B 124 ? 0.2810 0.2432 0.3203 -0.0385 0.0296 -0.0451 174 GLU B CA 2710 C C . GLU B 124 ? 0.2831 0.2459 0.3206 -0.0338 0.0289 -0.0394 174 GLU B C 2711 O O . GLU B 124 ? 0.2673 0.2341 0.2971 -0.0342 0.0285 -0.0399 174 GLU B O 2712 C CB . GLU B 124 ? 0.3093 0.2721 0.3488 -0.0392 0.0265 -0.0403 174 GLU B CB 2713 C CG . GLU B 124 ? 0.4901 0.4475 0.5401 -0.0402 0.0283 -0.0419 174 GLU B CG 2714 C CD . GLU B 124 ? 0.7542 0.7057 0.8128 -0.0361 0.0293 -0.0358 174 GLU B CD 2715 O OE1 . GLU B 124 ? 0.4559 0.4060 0.5156 -0.0323 0.0300 -0.0334 174 GLU B OE1 2716 O OE2 . GLU B 124 ? 0.6919 0.6403 0.7562 -0.0370 0.0294 -0.0333 174 GLU B OE2 2717 N N . GLN B 125 ? 0.2455 0.2043 0.2900 -0.0299 0.0287 -0.0338 175 GLN B N 2718 C CA . GLN B 125 ? 0.2501 0.2100 0.2932 -0.0256 0.0274 -0.0281 175 GLN B CA 2719 C C . GLN B 125 ? 0.2497 0.2147 0.2831 -0.0261 0.0242 -0.0241 175 GLN B C 2720 O O . GLN B 125 ? 0.2405 0.2071 0.2716 -0.0284 0.0225 -0.0232 175 GLN B O 2721 C CB . GLN B 125 ? 0.2851 0.2405 0.3355 -0.0223 0.0268 -0.0220 175 GLN B CB 2722 C CG . GLN B 125 ? 0.5303 0.4806 0.5914 -0.0198 0.0289 -0.0231 175 GLN B CG 2723 C CD . GLN B 125 ? 0.6829 0.6305 0.7475 -0.0163 0.0268 -0.0147 175 GLN B CD 2724 O OE1 . GLN B 125 ? 0.5948 0.5408 0.6588 -0.0173 0.0259 -0.0103 175 GLN B OE1 2725 N NE2 . GLN B 125 ? 0.4553 0.4033 0.5221 -0.0126 0.0259 -0.0121 175 GLN B NE2 2726 N N . MET B 126 ? 0.1990 0.1669 0.2282 -0.0240 0.0235 -0.0221 176 MET B N 2727 C CA . MET B 126 ? 0.1920 0.1642 0.2139 -0.0243 0.0207 -0.0187 176 MET B CA 2728 C C . MET B 126 ? 0.2266 0.1994 0.2488 -0.0205 0.0195 -0.0133 176 MET B C 2729 O O . MET B 126 ? 0.2360 0.2080 0.2606 -0.0181 0.0205 -0.0135 176 MET B O 2730 C CB . MET B 126 ? 0.2122 0.1877 0.2271 -0.0268 0.0211 -0.0223 176 MET B CB 2731 C CG . MET B 126 ? 0.2488 0.2283 0.2569 -0.0272 0.0180 -0.0187 176 MET B CG 2732 S SD . MET B 126 ? 0.2926 0.2752 0.2925 -0.0304 0.0188 -0.0220 176 MET B SD 2733 C CE . MET B 126 ? 0.2589 0.2421 0.2557 -0.0358 0.0189 -0.0276 176 MET B CE 2734 N N . LEU B 127 ? 0.1975 0.1721 0.2175 -0.0200 0.0174 -0.0091 177 LEU B N 2735 C CA . LEU B 127 ? 0.1906 0.1669 0.2095 -0.0171 0.0161 -0.0048 177 LEU B CA 2736 C C . LEU B 127 ? 0.2264 0.2063 0.2402 -0.0173 0.0151 -0.0053 177 LEU B C 2737 O O . LEU B 127 ? 0.2140 0.1961 0.2243 -0.0196 0.0138 -0.0060 177 LEU B O 2738 C CB . LEU B 127 ? 0.1805 0.1577 0.1998 -0.0172 0.0151 -0.0011 177 LEU B CB 2739 C CG . LEU B 127 ? 0.2268 0.2069 0.2438 -0.0151 0.0140 0.0023 177 LEU B CG 2740 C CD1 . LEU B 127 ? 0.2487 0.2276 0.2667 -0.0124 0.0142 0.0042 177 LEU B CD1 2741 C CD2 . LEU B 127 ? 0.2845 0.2661 0.3022 -0.0160 0.0138 0.0045 177 LEU B CD2 2742 N N . ILE B 128 ? 0.1656 0.1463 0.1797 -0.0150 0.0154 -0.0046 178 ILE B N 2743 C CA . ILE B 128 ? 0.1637 0.1471 0.1740 -0.0152 0.0148 -0.0048 178 ILE B CA 2744 C C . ILE B 128 ? 0.1866 0.1716 0.1979 -0.0124 0.0138 -0.0020 178 ILE B C 2745 O O . ILE B 128 ? 0.1925 0.1766 0.2069 -0.0102 0.0140 -0.0012 178 ILE B O 2746 C CB . ILE B 128 ? 0.2008 0.1842 0.2106 -0.0162 0.0169 -0.0085 178 ILE B CB 2747 C CG1 . ILE B 128 ? 0.2029 0.1853 0.2106 -0.0197 0.0182 -0.0123 178 ILE B CG1 2748 C CG2 . ILE B 128 ? 0.2298 0.2158 0.2357 -0.0169 0.0164 -0.0078 178 ILE B CG2 2749 C CD1 . ILE B 128 ? 0.2579 0.2400 0.2662 -0.0209 0.0215 -0.0171 178 ILE B CD1 2750 N N . ILE B 129 ? 0.1747 0.1621 0.1837 -0.0126 0.0124 -0.0006 179 ILE B N 2751 C CA . ILE B 129 ? 0.1776 0.1669 0.1874 -0.0106 0.0117 0.0010 179 ILE B CA 2752 C C . ILE B 129 ? 0.1982 0.1889 0.2071 -0.0108 0.0117 0.0002 179 ILE B C 2753 O O . ILE B 129 ? 0.1909 0.1817 0.1975 -0.0128 0.0115 -0.0001 179 ILE B O 2754 C CB . ILE B 129 ? 0.2183 0.2091 0.2283 -0.0107 0.0106 0.0029 179 ILE B CB 2755 C CG1 . ILE B 129 ? 0.2251 0.2143 0.2361 -0.0109 0.0112 0.0039 179 ILE B CG1 2756 C CG2 . ILE B 129 ? 0.2105 0.2038 0.2213 -0.0091 0.0103 0.0034 179 ILE B CG2 2757 C CD1 . ILE B 129 ? 0.3031 0.2939 0.3151 -0.0120 0.0108 0.0049 179 ILE B CD1 2758 N N . TRP B 130 ? 0.1685 0.1606 0.1792 -0.0090 0.0117 0.0000 180 TRP B N 2759 C CA . TRP B 130 ? 0.1821 0.1755 0.1930 -0.0094 0.0119 -0.0006 180 TRP B CA 2760 C C . TRP B 130 ? 0.2053 0.2009 0.2184 -0.0076 0.0110 -0.0004 180 TRP B C 2761 O O . TRP B 130 ? 0.1769 0.1732 0.1904 -0.0062 0.0104 0.0001 180 TRP B O 2762 C CB . TRP B 130 ? 0.1778 0.1710 0.1897 -0.0099 0.0137 -0.0028 180 TRP B CB 2763 C CG . TRP B 130 ? 0.2004 0.1944 0.2165 -0.0075 0.0137 -0.0037 180 TRP B CG 2764 C CD1 . TRP B 130 ? 0.2415 0.2379 0.2607 -0.0062 0.0132 -0.0044 180 TRP B CD1 2765 C CD2 . TRP B 130 ? 0.2133 0.2059 0.2316 -0.0063 0.0137 -0.0037 180 TRP B CD2 2766 N NE1 . TRP B 130 ? 0.2472 0.2442 0.2702 -0.0040 0.0124 -0.0045 180 TRP B NE1 2767 C CE2 . TRP B 130 ? 0.2846 0.2789 0.3073 -0.0040 0.0128 -0.0038 180 TRP B CE2 2768 C CE3 . TRP B 130 ? 0.2541 0.2440 0.2717 -0.0070 0.0142 -0.0035 180 TRP B CE3 2769 C CZ2 . TRP B 130 ? 0.2891 0.2821 0.3159 -0.0021 0.0122 -0.0031 180 TRP B CZ2 2770 C CZ3 . TRP B 130 ? 0.2919 0.2802 0.3138 -0.0053 0.0141 -0.0031 180 TRP B CZ3 2771 C CH2 . TRP B 130 ? 0.2988 0.2885 0.3252 -0.0028 0.0130 -0.0026 180 TRP B CH2 2772 N N . GLY B 131 ? 0.1737 0.1703 0.1880 -0.0081 0.0109 -0.0008 181 GLY B N 2773 C CA . GLY B 131 ? 0.1596 0.1585 0.1763 -0.0067 0.0104 -0.0017 181 GLY B CA 2774 C C . GLY B 131 ? 0.1856 0.1857 0.2052 -0.0068 0.0109 -0.0035 181 GLY B C 2775 O O . GLY B 131 ? 0.1466 0.1456 0.1662 -0.0082 0.0121 -0.0036 181 GLY B O 2776 N N . VAL B 132 ? 0.1529 0.1557 0.1747 -0.0057 0.0102 -0.0050 182 VAL B N 2777 C CA . VAL B 132 ? 0.1375 0.1422 0.1632 -0.0059 0.0104 -0.0073 182 VAL B CA 2778 C C . VAL B 132 ? 0.1773 0.1833 0.2050 -0.0060 0.0101 -0.0087 182 VAL B C 2779 O O . VAL B 132 ? 0.1919 0.1998 0.2182 -0.0053 0.0093 -0.0094 182 VAL B O 2780 C CB . VAL B 132 ? 0.1869 0.1946 0.2143 -0.0045 0.0093 -0.0086 182 VAL B CB 2781 C CG1 . VAL B 132 ? 0.2077 0.2182 0.2403 -0.0049 0.0093 -0.0115 182 VAL B CG1 2782 C CG2 . VAL B 132 ? 0.1929 0.1991 0.2207 -0.0042 0.0101 -0.0079 182 VAL B CG2 2783 N N . HIS B 133 ? 0.1210 0.1258 0.1525 -0.0072 0.0110 -0.0093 183 HIS B N 2784 C CA . HIS B 133 ? 0.1267 0.1324 0.1623 -0.0073 0.0110 -0.0114 183 HIS B CA 2785 C C . HIS B 133 ? 0.1714 0.1806 0.2105 -0.0073 0.0108 -0.0153 183 HIS B C 2786 O O . HIS B 133 ? 0.1494 0.1591 0.1911 -0.0079 0.0112 -0.0160 183 HIS B O 2787 C CB . HIS B 133 ? 0.1417 0.1439 0.1810 -0.0086 0.0118 -0.0096 183 HIS B CB 2788 C CG . HIS B 133 ? 0.1820 0.1841 0.2275 -0.0085 0.0120 -0.0117 183 HIS B CG 2789 N ND1 . HIS B 133 ? 0.2109 0.2105 0.2624 -0.0097 0.0127 -0.0114 183 HIS B ND1 2790 C CD2 . HIS B 133 ? 0.2055 0.2096 0.2525 -0.0076 0.0120 -0.0143 183 HIS B CD2 2791 C CE1 . HIS B 133 ? 0.2202 0.2201 0.2778 -0.0091 0.0129 -0.0140 183 HIS B CE1 2792 N NE2 . HIS B 133 ? 0.2241 0.2270 0.2790 -0.0080 0.0127 -0.0161 183 HIS B NE2 2793 N N . HIS B 134 ? 0.1346 0.1470 0.1737 -0.0068 0.0101 -0.0183 184 HIS B N 2794 C CA . HIS B 134 ? 0.1288 0.1455 0.1704 -0.0071 0.0094 -0.0227 184 HIS B CA 2795 C C . HIS B 134 ? 0.1639 0.1803 0.2118 -0.0082 0.0108 -0.0264 184 HIS B C 2796 O O . HIS B 134 ? 0.1568 0.1743 0.2044 -0.0082 0.0114 -0.0285 184 HIS B O 2797 C CB . HIS B 134 ? 0.1368 0.1577 0.1724 -0.0065 0.0076 -0.0234 184 HIS B CB 2798 C CG . HIS B 134 ? 0.1850 0.2058 0.2163 -0.0052 0.0060 -0.0196 184 HIS B CG 2799 N ND1 . HIS B 134 ? 0.1897 0.2121 0.2237 -0.0048 0.0046 -0.0197 184 HIS B ND1 2800 C CD2 . HIS B 134 ? 0.2106 0.2295 0.2367 -0.0045 0.0058 -0.0159 184 HIS B CD2 2801 C CE1 . HIS B 134 ? 0.1913 0.2127 0.2220 -0.0035 0.0036 -0.0161 184 HIS B CE1 2802 N NE2 . HIS B 134 ? 0.2033 0.2225 0.2290 -0.0034 0.0042 -0.0137 184 HIS B NE2 2803 N N . PRO B 135 ? 0.1459 0.1601 0.2005 -0.0092 0.0118 -0.0271 185 PRO B N 2804 C CA . PRO B 135 ? 0.1471 0.1599 0.2093 -0.0101 0.0132 -0.0302 185 PRO B CA 2805 C C . PRO B 135 ? 0.1832 0.2007 0.2478 -0.0107 0.0133 -0.0370 185 PRO B C 2806 O O . PRO B 135 ? 0.1782 0.2009 0.2387 -0.0109 0.0116 -0.0395 185 PRO B O 2807 C CB . PRO B 135 ? 0.1833 0.1926 0.2514 -0.0114 0.0143 -0.0286 185 PRO B CB 2808 C CG . PRO B 135 ? 0.2272 0.2348 0.2891 -0.0112 0.0139 -0.0232 185 PRO B CG 2809 C CD . PRO B 135 ? 0.1921 0.2046 0.2484 -0.0100 0.0122 -0.0250 185 PRO B CD 2810 N N . ASN B 136 ? 0.1567 0.1726 0.2285 -0.0112 0.0150 -0.0402 186 ASN B N 2811 C CA . ASN B 136 ? 0.1609 0.1809 0.2364 -0.0123 0.0159 -0.0480 186 ASN B CA 2812 C C . ASN B 136 ? 0.2019 0.2239 0.2833 -0.0140 0.0156 -0.0525 186 ASN B C 2813 O O . ASN B 136 ? 0.1861 0.2138 0.2669 -0.0153 0.0150 -0.0589 186 ASN B O 2814 C CB . ASN B 136 ? 0.1805 0.1973 0.2650 -0.0122 0.0184 -0.0503 186 ASN B CB 2815 C CG . ASN B 136 ? 0.2483 0.2698 0.3361 -0.0136 0.0201 -0.0595 186 ASN B CG 2816 O OD1 . ASN B 136 ? 0.2403 0.2669 0.3203 -0.0138 0.0202 -0.0623 186 ASN B OD1 2817 N ND2 . ASN B 136 ? 0.2710 0.2913 0.3698 -0.0149 0.0214 -0.0647 186 ASN B ND2 2818 N N . ASP B 137 ? 0.1660 0.1835 0.2533 -0.0145 0.0161 -0.0492 187 ASP B N 2819 C CA . ASP B 137 ? 0.1600 0.1787 0.2553 -0.0165 0.0165 -0.0534 187 ASP B CA 2820 C C . ASP B 137 ? 0.1816 0.1965 0.2789 -0.0171 0.0170 -0.0479 187 ASP B C 2821 O O . ASP B 137 ? 0.1828 0.1934 0.2760 -0.0161 0.0172 -0.0413 187 ASP B O 2822 C CB . ASP B 137 ? 0.2035 0.2199 0.3102 -0.0177 0.0188 -0.0589 187 ASP B CB 2823 C CG . ASP B 137 ? 0.3629 0.3719 0.4750 -0.0167 0.0204 -0.0542 187 ASP B CG 2824 O OD1 . ASP B 137 ? 0.3527 0.3564 0.4677 -0.0171 0.0207 -0.0482 187 ASP B OD1 2825 O OD2 . ASP B 137 ? 0.4196 0.4287 0.5325 -0.0156 0.0212 -0.0560 187 ASP B OD2 2826 N N . GLU B 138 ? 0.1758 0.1927 0.2792 -0.0189 0.0173 -0.0510 188 GLU B N 2827 C CA . GLU B 138 ? 0.1935 0.2076 0.2987 -0.0201 0.0184 -0.0464 188 GLU B CA 2828 C C . GLU B 138 ? 0.2338 0.2398 0.3442 -0.0211 0.0208 -0.0415 188 GLU B C 2829 O O . GLU B 138 ? 0.2168 0.2195 0.3242 -0.0218 0.0218 -0.0354 188 GLU B O 2830 C CB . GLU B 138 ? 0.2081 0.2270 0.3197 -0.0220 0.0183 -0.0512 188 GLU B CB 2831 C CG . GLU B 138 ? 0.2846 0.3115 0.3907 -0.0208 0.0150 -0.0540 188 GLU B CG 2832 C CD . GLU B 138 ? 0.5034 0.5357 0.6167 -0.0225 0.0144 -0.0579 188 GLU B CD 2833 O OE1 . GLU B 138 ? 0.4429 0.4761 0.5654 -0.0248 0.0153 -0.0633 188 GLU B OE1 2834 O OE2 . GLU B 138 ? 0.3959 0.4315 0.5066 -0.0215 0.0131 -0.0558 188 GLU B OE2 2835 N N . THR B 139 ? 0.2258 0.2287 0.3440 -0.0213 0.0217 -0.0441 189 THR B N 2836 C CA . THR B 139 ? 0.2344 0.2294 0.3587 -0.0219 0.0231 -0.0388 189 THR B CA 2837 C C . THR B 139 ? 0.2543 0.2463 0.3698 -0.0201 0.0219 -0.0313 189 THR B C 2838 O O . THR B 139 ? 0.2421 0.2293 0.3563 -0.0212 0.0224 -0.0242 189 THR B O 2839 C CB . THR B 139 ? 0.3051 0.2979 0.4415 -0.0221 0.0242 -0.0441 189 THR B CB 2840 O OG1 . THR B 139 ? 0.3272 0.3227 0.4716 -0.0245 0.0254 -0.0510 189 THR B OG1 2841 C CG2 . THR B 139 ? 0.3071 0.2913 0.4513 -0.0223 0.0250 -0.0378 189 THR B CG2 2842 N N . GLU B 140 ? 0.2178 0.2131 0.3267 -0.0177 0.0204 -0.0327 190 GLU B N 2843 C CA . GLU B 140 ? 0.2046 0.1980 0.3056 -0.0161 0.0191 -0.0265 190 GLU B CA 2844 C C . GLU B 140 ? 0.2101 0.2039 0.3017 -0.0167 0.0188 -0.0218 190 GLU B C 2845 O O . GLU B 140 ? 0.2229 0.2128 0.3106 -0.0171 0.0184 -0.0152 190 GLU B O 2846 C CB . GLU B 140 ? 0.2242 0.2217 0.3206 -0.0139 0.0180 -0.0299 190 GLU B CB 2847 C CG . GLU B 140 ? 0.3538 0.3489 0.4451 -0.0124 0.0168 -0.0241 190 GLU B CG 2848 C CD . GLU B 140 ? 0.6497 0.6484 0.7349 -0.0106 0.0162 -0.0258 190 GLU B CD 2849 O OE1 . GLU B 140 ? 0.3984 0.4020 0.4825 -0.0105 0.0167 -0.0318 190 GLU B OE1 2850 O OE2 . GLU B 140 ? 0.6167 0.6137 0.6978 -0.0097 0.0151 -0.0208 190 GLU B OE2 2851 N N . GLN B 141 ? 0.1700 0.1688 0.2587 -0.0170 0.0188 -0.0253 191 GLN B N 2852 C CA . GLN B 141 ? 0.1527 0.1525 0.2347 -0.0176 0.0191 -0.0222 191 GLN B CA 2853 C C . GLN B 141 ? 0.2009 0.1961 0.2852 -0.0203 0.0212 -0.0177 191 GLN B C 2854 O O . GLN B 141 ? 0.2301 0.2234 0.3076 -0.0210 0.0217 -0.0127 191 GLN B O 2855 C CB . GLN B 141 ? 0.1707 0.1768 0.2534 -0.0175 0.0186 -0.0274 191 GLN B CB 2856 C CG . GLN B 141 ? 0.1611 0.1687 0.2399 -0.0180 0.0194 -0.0253 191 GLN B CG 2857 C CD . GLN B 141 ? 0.1967 0.2038 0.2663 -0.0163 0.0185 -0.0218 191 GLN B CD 2858 O OE1 . GLN B 141 ? 0.1965 0.2048 0.2620 -0.0142 0.0164 -0.0222 191 GLN B OE1 2859 N NE2 . GLN B 141 ? 0.1563 0.1627 0.2229 -0.0174 0.0202 -0.0192 191 GLN B NE2 2860 N N . ARG B 142 ? 0.1989 0.1925 0.2926 -0.0223 0.0228 -0.0197 192 ARG B N 2861 C CA . ARG B 142 ? 0.2126 0.2017 0.3087 -0.0255 0.0252 -0.0150 192 ARG B CA 2862 C C . ARG B 142 ? 0.2540 0.2368 0.3482 -0.0258 0.0244 -0.0076 192 ARG B C 2863 O O . ARG B 142 ? 0.2434 0.2234 0.3321 -0.0281 0.0255 -0.0017 192 ARG B O 2864 C CB . ARG B 142 ? 0.2006 0.1897 0.3083 -0.0277 0.0272 -0.0191 192 ARG B CB 2865 C CG . ARG B 142 ? 0.3123 0.3081 0.4213 -0.0283 0.0280 -0.0247 192 ARG B CG 2866 C CD . ARG B 142 ? 0.3395 0.3358 0.4606 -0.0310 0.0300 -0.0291 192 ARG B CD 2867 N NE . ARG B 142 ? 0.4379 0.4417 0.5612 -0.0313 0.0300 -0.0348 192 ARG B NE 2868 C CZ . ARG B 142 ? 0.6113 0.6210 0.7390 -0.0302 0.0277 -0.0420 192 ARG B CZ 2869 N NH1 . ARG B 142 ? 0.4453 0.4541 0.5757 -0.0291 0.0262 -0.0454 192 ARG B NH1 2870 N NH2 . ARG B 142 ? 0.4527 0.4694 0.5827 -0.0303 0.0270 -0.0462 192 ARG B NH2 2871 N N . THR B 143 ? 0.2182 0.1991 0.3166 -0.0236 0.0225 -0.0080 193 THR B N 2872 C CA . THR B 143 ? 0.2202 0.1954 0.3187 -0.0235 0.0209 -0.0009 193 THR B CA 2873 C C . THR B 143 ? 0.2646 0.2404 0.3507 -0.0231 0.0193 0.0041 193 THR B C 2874 O O . THR B 143 ? 0.2689 0.2407 0.3511 -0.0249 0.0186 0.0114 193 THR B O 2875 C CB . THR B 143 ? 0.3019 0.2757 0.4094 -0.0209 0.0194 -0.0035 193 THR B CB 2876 O OG1 . THR B 143 ? 0.4882 0.4672 0.5908 -0.0183 0.0183 -0.0081 193 THR B OG1 2877 C CG2 . THR B 143 ? 0.2169 0.1897 0.3376 -0.0216 0.0212 -0.0090 193 THR B CG2 2878 N N . LEU B 144 ? 0.1965 0.1772 0.2763 -0.0209 0.0186 0.0003 194 LEU B N 2879 C CA . LEU B 144 ? 0.1899 0.1711 0.2590 -0.0205 0.0171 0.0041 194 LEU B CA 2880 C C . LEU B 144 ? 0.2339 0.2164 0.2949 -0.0228 0.0191 0.0053 194 LEU B C 2881 O O . LEU B 144 ? 0.2435 0.2242 0.2969 -0.0244 0.0186 0.0104 194 LEU B O 2882 C CB . LEU B 144 ? 0.1877 0.1732 0.2541 -0.0175 0.0158 -0.0002 194 LEU B CB 2883 C CG . LEU B 144 ? 0.2376 0.2227 0.3107 -0.0151 0.0144 -0.0020 194 LEU B CG 2884 C CD1 . LEU B 144 ? 0.2568 0.2469 0.3268 -0.0130 0.0141 -0.0072 194 LEU B CD1 2885 C CD2 . LEU B 144 ? 0.2687 0.2504 0.3416 -0.0147 0.0120 0.0040 194 LEU B CD2 2886 N N . TYR B 145 ? 0.1886 0.1747 0.2518 -0.0233 0.0214 0.0003 195 TYR B N 2887 C CA . TYR B 145 ? 0.1980 0.1866 0.2552 -0.0249 0.0237 -0.0003 195 TYR B CA 2888 C C . TYR B 145 ? 0.2343 0.2234 0.2963 -0.0280 0.0272 -0.0016 195 TYR B C 2889 O O . TYR B 145 ? 0.2272 0.2197 0.2872 -0.0288 0.0294 -0.0041 195 TYR B O 2890 C CB . TYR B 145 ? 0.2011 0.1946 0.2559 -0.0221 0.0227 -0.0050 195 TYR B CB 2891 C CG . TYR B 145 ? 0.1591 0.1526 0.2107 -0.0192 0.0197 -0.0045 195 TYR B CG 2892 C CD1 . TYR B 145 ? 0.1807 0.1721 0.2250 -0.0194 0.0186 -0.0003 195 TYR B CD1 2893 C CD2 . TYR B 145 ? 0.1616 0.1574 0.2175 -0.0168 0.0181 -0.0084 195 TYR B CD2 2894 C CE1 . TYR B 145 ? 0.2004 0.1920 0.2428 -0.0170 0.0161 0.0001 195 TYR B CE1 2895 C CE2 . TYR B 145 ? 0.1667 0.1628 0.2198 -0.0146 0.0160 -0.0080 195 TYR B CE2 2896 C CZ . TYR B 145 ? 0.1868 0.1807 0.2339 -0.0147 0.0151 -0.0037 195 TYR B CZ 2897 O OH . TYR B 145 ? 0.1790 0.1733 0.2246 -0.0128 0.0134 -0.0035 195 TYR B OH 2898 N N . GLN B 146 ? 0.2130 0.1988 0.2827 -0.0296 0.0278 -0.0004 196 GLN B N 2899 C CA . GLN B 146 ? 0.2229 0.2084 0.2984 -0.0330 0.0314 -0.0011 196 GLN B CA 2900 C C . GLN B 146 ? 0.2764 0.2674 0.3602 -0.0324 0.0325 -0.0087 196 GLN B C 2901 O O . GLN B 146 ? 0.2875 0.2776 0.3808 -0.0341 0.0339 -0.0106 196 GLN B O 2902 C CB . GLN B 146 ? 0.2575 0.2414 0.3252 -0.0370 0.0346 0.0038 196 GLN B CB 2903 C CG . GLN B 146 ? 0.5123 0.4944 0.5857 -0.0415 0.0386 0.0050 196 GLN B CG 2904 C CD . GLN B 146 ? 0.8593 0.8350 0.9395 -0.0428 0.0377 0.0097 196 GLN B CD 2905 O OE1 . GLN B 146 ? 0.7988 0.7702 0.8773 -0.0413 0.0343 0.0146 196 GLN B OE1 2906 N NE2 . GLN B 146 ? 0.7953 0.7701 0.8846 -0.0458 0.0410 0.0085 196 GLN B NE2 2907 N N . ASN B 147 ? 0.2403 0.2369 0.3212 -0.0302 0.0317 -0.0128 197 ASN B N 2908 C CA . ASN B 147 ? 0.2550 0.2575 0.3438 -0.0296 0.0320 -0.0194 197 ASN B CA 2909 C C . ASN B 147 ? 0.3050 0.3121 0.3919 -0.0257 0.0282 -0.0231 197 ASN B C 2910 O O . ASN B 147 ? 0.2664 0.2727 0.3453 -0.0236 0.0265 -0.0207 197 ASN B O 2911 C CB . ASN B 147 ? 0.2924 0.2979 0.3816 -0.0319 0.0357 -0.0204 197 ASN B CB 2912 C CG . ASN B 147 ? 0.4590 0.4616 0.5521 -0.0366 0.0401 -0.0181 197 ASN B CG 2913 O OD1 . ASN B 147 ? 0.4420 0.4450 0.5450 -0.0382 0.0411 -0.0207 197 ASN B OD1 2914 N ND2 . ASN B 147 ? 0.3339 0.3340 0.4190 -0.0393 0.0432 -0.0136 197 ASN B ND2 2915 N N . VAL B 148 ? 0.2565 0.2688 0.3511 -0.0250 0.0270 -0.0289 198 VAL B N 2916 C CA . VAL B 148 ? 0.2539 0.2717 0.3472 -0.0219 0.0233 -0.0324 198 VAL B CA 2917 C C . VAL B 148 ? 0.3161 0.3379 0.4099 -0.0216 0.0242 -0.0330 198 VAL B C 2918 O O . VAL B 148 ? 0.3435 0.3666 0.4436 -0.0241 0.0274 -0.0343 198 VAL B O 2919 C CB . VAL B 148 ? 0.3014 0.3234 0.4023 -0.0219 0.0211 -0.0383 198 VAL B CB 2920 C CG1 . VAL B 148 ? 0.3087 0.3378 0.4081 -0.0193 0.0169 -0.0416 198 VAL B CG1 2921 C CG2 . VAL B 148 ? 0.3003 0.3182 0.4014 -0.0220 0.0207 -0.0384 198 VAL B CG2 2922 N N . GLY B 149 ? 0.2421 0.2660 0.3305 -0.0186 0.0217 -0.0323 199 GLY B N 2923 C CA . GLY B 149 ? 0.2370 0.2646 0.3276 -0.0177 0.0221 -0.0333 199 GLY B CA 2924 C C . GLY B 149 ? 0.2865 0.3101 0.3695 -0.0178 0.0246 -0.0295 199 GLY B C 2925 O O . GLY B 149 ? 0.3064 0.3283 0.3896 -0.0205 0.0289 -0.0287 199 GLY B O 2926 N N . THR B 150 ? 0.1964 0.2180 0.2718 -0.0154 0.0220 -0.0270 200 THR B N 2927 C CA . THR B 150 ? 0.1431 0.1607 0.2105 -0.0156 0.0237 -0.0237 200 THR B CA 2928 C C . THR B 150 ? 0.1658 0.1850 0.2312 -0.0123 0.0210 -0.0236 200 THR B C 2929 O O . THR B 150 ? 0.1735 0.1963 0.2417 -0.0099 0.0173 -0.0249 200 THR B O 2930 C CB . THR B 150 ? 0.1858 0.1980 0.2460 -0.0165 0.0234 -0.0198 200 THR B CB 2931 O OG1 . THR B 150 ? 0.1944 0.2074 0.2538 -0.0142 0.0197 -0.0202 200 THR B OG1 2932 C CG2 . THR B 150 ? 0.1832 0.1928 0.2462 -0.0198 0.0257 -0.0188 200 THR B CG2 2933 N N . TYR B 151 ? 0.1634 0.1799 0.2236 -0.0125 0.0227 -0.0218 201 TYR B N 2934 C CA . TYR B 151 ? 0.1517 0.1683 0.2099 -0.0096 0.0205 -0.0211 201 TYR B CA 2935 C C . TYR B 151 ? 0.1809 0.1927 0.2303 -0.0105 0.0215 -0.0183 201 TYR B C 2936 O O . TYR B 151 ? 0.1554 0.1646 0.2006 -0.0134 0.0243 -0.0172 201 TYR B O 2937 C CB . TYR B 151 ? 0.1540 0.1736 0.2197 -0.0086 0.0219 -0.0239 201 TYR B CB 2938 C CG . TYR B 151 ? 0.1733 0.1920 0.2395 -0.0116 0.0274 -0.0256 201 TYR B CG 2939 C CD1 . TYR B 151 ? 0.1996 0.2150 0.2600 -0.0124 0.0297 -0.0250 201 TYR B CD1 2940 C CD2 . TYR B 151 ? 0.2029 0.2248 0.2765 -0.0136 0.0307 -0.0287 201 TYR B CD2 2941 C CE1 . TYR B 151 ? 0.2080 0.2234 0.2682 -0.0156 0.0352 -0.0274 201 TYR B CE1 2942 C CE2 . TYR B 151 ? 0.2181 0.2399 0.2922 -0.0167 0.0364 -0.0308 201 TYR B CE2 2943 C CZ . TYR B 151 ? 0.3354 0.3540 0.4021 -0.0178 0.0387 -0.0303 201 TYR B CZ 2944 O OH . TYR B 151 ? 0.3874 0.4065 0.4536 -0.0214 0.0448 -0.0329 201 TYR B OH 2945 N N . VAL B 152 ? 0.1527 0.1637 0.1995 -0.0081 0.0191 -0.0169 202 VAL B N 2946 C CA . VAL B 152 ? 0.1510 0.1581 0.1907 -0.0088 0.0198 -0.0148 202 VAL B CA 2947 C C . VAL B 152 ? 0.2029 0.2104 0.2460 -0.0068 0.0198 -0.0160 202 VAL B C 2948 O O . VAL B 152 ? 0.2258 0.2346 0.2716 -0.0040 0.0165 -0.0151 202 VAL B O 2949 C CB . VAL B 152 ? 0.1778 0.1830 0.2119 -0.0080 0.0170 -0.0118 202 VAL B CB 2950 C CG1 . VAL B 152 ? 0.1802 0.1819 0.2082 -0.0088 0.0175 -0.0100 202 VAL B CG1 2951 C CG2 . VAL B 152 ? 0.1855 0.1904 0.2189 -0.0094 0.0168 -0.0110 202 VAL B CG2 2952 N N . SER B 153 ? 0.1455 0.1518 0.1886 -0.0085 0.0234 -0.0179 203 SER B N 2953 C CA A SER B 153 ? 0.1410 0.1468 0.1889 -0.0068 0.0241 -0.0197 203 SER B CA 2954 C CA B SER B 153 ? 0.1510 0.1569 0.1990 -0.0067 0.0240 -0.0197 203 SER B CA 2955 C C . SER B 153 ? 0.1725 0.1745 0.2143 -0.0081 0.0253 -0.0192 203 SER B C 2956 O O . SER B 153 ? 0.1968 0.1976 0.2322 -0.0114 0.0278 -0.0198 203 SER B O 2957 C CB A SER B 153 ? 0.1658 0.1744 0.2219 -0.0075 0.0278 -0.0241 203 SER B CB 2958 C CB B SER B 153 ? 0.2102 0.2190 0.2669 -0.0072 0.0276 -0.0241 203 SER B CB 2959 O OG A SER B 153 ? 0.2211 0.2338 0.2841 -0.0063 0.0263 -0.0247 203 SER B OG 2960 O OG B SER B 153 ? 0.4046 0.4125 0.4573 -0.0111 0.0327 -0.0266 203 SER B OG 2961 N N . VAL B 154 ? 0.1602 0.1604 0.2037 -0.0057 0.0232 -0.0180 204 VAL B N 2962 C CA . VAL B 154 ? 0.1575 0.1540 0.1965 -0.0069 0.0241 -0.0179 204 VAL B CA 2963 C C . VAL B 154 ? 0.2144 0.2098 0.2620 -0.0048 0.0249 -0.0200 204 VAL B C 2964 O O . VAL B 154 ? 0.2222 0.2183 0.2761 -0.0015 0.0219 -0.0180 204 VAL B O 2965 C CB . VAL B 154 ? 0.2028 0.1974 0.2355 -0.0064 0.0207 -0.0135 204 VAL B CB 2966 C CG1 . VAL B 154 ? 0.2090 0.2004 0.2377 -0.0081 0.0217 -0.0138 204 VAL B CG1 2967 C CG2 . VAL B 154 ? 0.2115 0.2076 0.2387 -0.0077 0.0196 -0.0116 204 VAL B CG2 2968 N N . GLY B 155 ? 0.1621 0.1558 0.2100 -0.0069 0.0287 -0.0240 205 GLY B N 2969 C CA . GLY B 155 ? 0.1744 0.1666 0.2324 -0.0049 0.0299 -0.0266 205 GLY B CA 2970 C C . GLY B 155 ? 0.2282 0.2168 0.2842 -0.0070 0.0324 -0.0294 205 GLY B C 2971 O O . GLY B 155 ? 0.2456 0.2343 0.2930 -0.0110 0.0348 -0.0315 205 GLY B O 2972 N N . THR B 156 ? 0.1957 0.1811 0.2600 -0.0045 0.0316 -0.0292 206 THR B N 2973 C CA . THR B 156 ? 0.2062 0.1881 0.2715 -0.0065 0.0344 -0.0331 206 THR B CA 2974 C C . THR B 156 ? 0.2339 0.2141 0.3149 -0.0031 0.0355 -0.0355 206 THR B C 2975 O O . THR B 156 ? 0.2157 0.1983 0.3049 0.0001 0.0338 -0.0340 206 THR B O 2976 C CB . THR B 156 ? 0.2410 0.2191 0.3004 -0.0067 0.0312 -0.0284 206 THR B CB 2977 O OG1 . THR B 156 ? 0.2265 0.2024 0.2932 -0.0026 0.0276 -0.0233 206 THR B OG1 2978 C CG2 . THR B 156 ? 0.2314 0.2115 0.2779 -0.0086 0.0288 -0.0244 206 THR B CG2 2979 N N . SER B 157 ? 0.2297 0.2059 0.3160 -0.0038 0.0378 -0.0390 207 SER B N 2980 C CA A SER B 157 ? 0.2287 0.2026 0.3320 -0.0003 0.0386 -0.0410 207 SER B CA 2981 C CA B SER B 157 ? 0.2281 0.2020 0.3314 -0.0004 0.0387 -0.0411 207 SER B CA 2982 C C . SER B 157 ? 0.2637 0.2356 0.3724 0.0043 0.0324 -0.0324 207 SER B C 2983 O O . SER B 157 ? 0.2707 0.2420 0.3940 0.0081 0.0314 -0.0321 207 SER B O 2984 C CB A SER B 157 ? 0.2822 0.2517 0.3906 -0.0023 0.0426 -0.0469 207 SER B CB 2985 C CB B SER B 157 ? 0.2782 0.2475 0.3863 -0.0023 0.0425 -0.0468 207 SER B CB 2986 O OG A SER B 157 ? 0.3668 0.3390 0.4708 -0.0068 0.0485 -0.0556 207 SER B OG 2987 O OG B SER B 157 ? 0.3590 0.3236 0.4628 -0.0024 0.0393 -0.0416 207 SER B OG 2988 N N . THR B 158 ? 0.2043 0.1754 0.3016 0.0040 0.0283 -0.0255 208 THR B N 2989 C CA . THR B 158 ? 0.2073 0.1767 0.3072 0.0075 0.0227 -0.0171 208 THR B CA 2990 C C . THR B 158 ? 0.2682 0.2422 0.3592 0.0083 0.0185 -0.0118 208 THR B C 2991 O O . THR B 158 ? 0.2823 0.2558 0.3730 0.0106 0.0139 -0.0050 208 THR B O 2992 C CB . THR B 158 ? 0.3382 0.3018 0.4349 0.0065 0.0218 -0.0133 208 THR B CB 2993 O OG1 . THR B 158 ? 0.2891 0.2541 0.3717 0.0029 0.0224 -0.0135 208 THR B OG1 2994 C CG2 . THR B 158 ? 0.3714 0.3298 0.4786 0.0059 0.0254 -0.0183 208 THR B CG2 2995 N N . LEU B 159 ? 0.2184 0.1970 0.3023 0.0062 0.0203 -0.0151 209 LEU B N 2996 C CA . LEU B 159 ? 0.2025 0.1852 0.2782 0.0063 0.0173 -0.0116 209 LEU B CA 2997 C C . LEU B 159 ? 0.2224 0.2101 0.3014 0.0062 0.0190 -0.0157 209 LEU B C 2998 O O . LEU B 159 ? 0.2135 0.2018 0.2942 0.0041 0.0236 -0.0215 209 LEU B O 2999 C CB . LEU B 159 ? 0.2032 0.1854 0.2658 0.0029 0.0180 -0.0109 209 LEU B CB 3000 C CG . LEU B 159 ? 0.2709 0.2571 0.3253 0.0025 0.0158 -0.0085 209 LEU B CG 3001 C CD1 . LEU B 159 ? 0.2808 0.2675 0.3336 0.0047 0.0113 -0.0026 209 LEU B CD1 3002 C CD2 . LEU B 159 ? 0.2818 0.2679 0.3262 -0.0009 0.0175 -0.0096 209 LEU B CD2 3003 N N . ASN B 160 ? 0.1969 0.1886 0.2769 0.0081 0.0154 -0.0129 210 ASN B N 3004 C CA . ASN B 160 ? 0.1913 0.1881 0.2744 0.0078 0.0166 -0.0163 210 ASN B CA 3005 C C . ASN B 160 ? 0.2387 0.2389 0.3156 0.0082 0.0123 -0.0124 210 ASN B C 3006 O O . ASN B 160 ? 0.2557 0.2584 0.3378 0.0110 0.0079 -0.0094 210 ASN B O 3007 C CB . ASN B 160 ? 0.2294 0.2282 0.3281 0.0105 0.0170 -0.0191 210 ASN B CB 3008 C CG . ASN B 160 ? 0.5043 0.5086 0.6078 0.0096 0.0194 -0.0237 210 ASN B CG 3009 O OD1 . ASN B 160 ? 0.4746 0.4808 0.5695 0.0066 0.0212 -0.0248 210 ASN B OD1 3010 N ND2 . ASN B 160 ? 0.4923 0.4994 0.6108 0.0123 0.0190 -0.0258 210 ASN B ND2 3011 N N . LYS B 161 ? 0.1732 0.1735 0.2389 0.0054 0.0133 -0.0121 211 LYS B N 3012 C CA . LYS B 161 ? 0.1855 0.1887 0.2456 0.0056 0.0098 -0.0093 211 LYS B CA 3013 C C . LYS B 161 ? 0.2580 0.2643 0.3173 0.0036 0.0120 -0.0125 211 LYS B C 3014 O O . LYS B 161 ? 0.2817 0.2863 0.3359 0.0008 0.0155 -0.0143 211 LYS B O 3015 C CB . LYS B 161 ? 0.2394 0.2398 0.2893 0.0045 0.0088 -0.0058 211 LYS B CB 3016 C CG . LYS B 161 ? 0.4679 0.4713 0.5126 0.0048 0.0054 -0.0032 211 LYS B CG 3017 C CD . LYS B 161 ? 0.5954 0.5962 0.6327 0.0042 0.0045 0.0004 211 LYS B CD 3018 C CE . LYS B 161 ? 0.7257 0.7296 0.7573 0.0040 0.0021 0.0021 211 LYS B CE 3019 N NZ . LYS B 161 ? 0.7633 0.7650 0.7888 0.0033 0.0017 0.0056 211 LYS B NZ 3020 N N . ARG B 162 ? 0.1720 0.1831 0.2365 0.0047 0.0098 -0.0132 212 ARG B N 3021 C CA . ARG B 162 ? 0.1666 0.1805 0.2318 0.0026 0.0121 -0.0164 212 ARG B CA 3022 C C . ARG B 162 ? 0.2717 0.2890 0.3344 0.0029 0.0083 -0.0151 212 ARG B C 3023 O O . ARG B 162 ? 0.2969 0.3186 0.3659 0.0047 0.0050 -0.0154 212 ARG B O 3024 C CB . ARG B 162 ? 0.2154 0.2323 0.2919 0.0031 0.0143 -0.0203 212 ARG B CB 3025 C CG . ARG B 162 ? 0.2170 0.2311 0.2976 0.0031 0.0180 -0.0224 212 ARG B CG 3026 C CD . ARG B 162 ? 0.3321 0.3493 0.4241 0.0028 0.0219 -0.0276 212 ARG B CD 3027 N NE . ARG B 162 ? 0.3750 0.3889 0.4685 0.0019 0.0264 -0.0306 212 ARG B NE 3028 C CZ . ARG B 162 ? 0.4727 0.4882 0.5719 -0.0001 0.0323 -0.0362 212 ARG B CZ 3029 N NH1 . ARG B 162 ? 0.3005 0.3206 0.4049 -0.0015 0.0346 -0.0391 212 ARG B NH1 3030 N NH2 . ARG B 162 ? 0.3326 0.3451 0.4326 -0.0011 0.0362 -0.0393 212 ARG B NH2 3031 N N . SER B 163 ? 0.2352 0.2507 0.2894 0.0010 0.0088 -0.0140 213 SER B N 3032 C CA . SER B 163 ? 0.2371 0.2550 0.2880 0.0009 0.0062 -0.0135 213 SER B CA 3033 C C . SER B 163 ? 0.2725 0.2926 0.3263 -0.0010 0.0077 -0.0165 213 SER B C 3034 O O . SER B 163 ? 0.2369 0.2554 0.2920 -0.0030 0.0114 -0.0179 213 SER B O 3035 C CB . SER B 163 ? 0.2420 0.2565 0.2841 -0.0001 0.0064 -0.0111 213 SER B CB 3036 O OG . SER B 163 ? 0.3491 0.3604 0.3883 0.0009 0.0061 -0.0084 213 SER B OG 3037 N N . THR B 164 ? 0.2320 0.2559 0.2864 -0.0007 0.0047 -0.0174 214 THR B N 3038 C CA . THR B 164 ? 0.2325 0.2585 0.2901 -0.0026 0.0057 -0.0205 214 THR B CA 3039 C C . THR B 164 ? 0.2395 0.2647 0.2910 -0.0033 0.0048 -0.0202 214 THR B C 3040 O O . THR B 164 ? 0.2498 0.2768 0.2972 -0.0022 0.0018 -0.0192 214 THR B O 3041 C CB . THR B 164 ? 0.3816 0.4137 0.4475 -0.0019 0.0032 -0.0233 214 THR B CB 3042 O OG1 . THR B 164 ? 0.5111 0.5468 0.5744 -0.0004 -0.0017 -0.0225 214 THR B OG1 3043 C CG2 . THR B 164 ? 0.3590 0.3923 0.4328 -0.0007 0.0042 -0.0239 214 THR B CG2 3044 N N . PRO B 165 ? 0.1750 0.1976 0.2264 -0.0053 0.0074 -0.0211 215 PRO B N 3045 C CA . PRO B 165 ? 0.1888 0.2109 0.2369 -0.0059 0.0069 -0.0217 215 PRO B CA 3046 C C . PRO B 165 ? 0.1750 0.2024 0.2255 -0.0060 0.0045 -0.0255 215 PRO B C 3047 O O . PRO B 165 ? 0.2130 0.2440 0.2696 -0.0064 0.0037 -0.0282 215 PRO B O 3048 C CB . PRO B 165 ? 0.2307 0.2489 0.2811 -0.0078 0.0099 -0.0217 215 PRO B CB 3049 C CG . PRO B 165 ? 0.3023 0.3184 0.3539 -0.0087 0.0122 -0.0201 215 PRO B CG 3050 C CD . PRO B 165 ? 0.2318 0.2519 0.2866 -0.0073 0.0110 -0.0214 215 PRO B CD 3051 N N . GLU B 166 ? 0.1580 0.1863 0.2037 -0.0060 0.0035 -0.0262 216 GLU B N 3052 C CA . GLU B 166 ? 0.1627 0.1966 0.2089 -0.0068 0.0014 -0.0306 216 GLU B CA 3053 C C . GLU B 166 ? 0.1975 0.2299 0.2470 -0.0085 0.0039 -0.0344 216 GLU B C 3054 O O . GLU B 166 ? 0.2388 0.2685 0.2854 -0.0085 0.0055 -0.0336 216 GLU B O 3055 C CB . GLU B 166 ? 0.2062 0.2427 0.2442 -0.0060 -0.0011 -0.0289 216 GLU B CB 3056 C CG . GLU B 166 ? 0.3750 0.4136 0.4113 -0.0043 -0.0046 -0.0254 216 GLU B CG 3057 C CD . GLU B 166 ? 0.7086 0.7480 0.7359 -0.0038 -0.0065 -0.0220 216 GLU B CD 3058 O OE1 . GLU B 166 ? 0.6812 0.7249 0.7035 -0.0052 -0.0078 -0.0243 216 GLU B OE1 3059 O OE2 . GLU B 166 ? 0.6330 0.6687 0.6580 -0.0024 -0.0062 -0.0172 216 GLU B OE2 3060 N N . ILE B 167 ? 0.1519 0.1862 0.2090 -0.0100 0.0043 -0.0387 217 ILE B N 3061 C CA . ILE B 167 ? 0.1502 0.1825 0.2125 -0.0116 0.0068 -0.0425 217 ILE B CA 3062 C C . ILE B 167 ? 0.1610 0.1988 0.2219 -0.0127 0.0055 -0.0484 217 ILE B C 3063 O O . ILE B 167 ? 0.1474 0.1907 0.2102 -0.0135 0.0031 -0.0520 217 ILE B O 3064 C CB . ILE B 167 ? 0.1890 0.2192 0.2609 -0.0131 0.0086 -0.0437 217 ILE B CB 3065 C CG1 . ILE B 167 ? 0.2030 0.2276 0.2744 -0.0127 0.0106 -0.0377 217 ILE B CG1 3066 C CG2 . ILE B 167 ? 0.2374 0.2658 0.3164 -0.0148 0.0108 -0.0483 217 ILE B CG2 3067 C CD1 . ILE B 167 ? 0.2681 0.2923 0.3462 -0.0142 0.0121 -0.0379 217 ILE B CD1 3068 N N . ALA B 168 ? 0.1611 0.1980 0.2192 -0.0129 0.0071 -0.0499 218 ALA B N 3069 C CA . ALA B 168 ? 0.1630 0.2056 0.2183 -0.0144 0.0065 -0.0561 218 ALA B CA 3070 C C . ALA B 168 ? 0.2009 0.2412 0.2585 -0.0150 0.0101 -0.0592 218 ALA B C 3071 O O . ALA B 168 ? 0.1858 0.2218 0.2416 -0.0136 0.0116 -0.0548 218 ALA B O 3072 C CB . ALA B 168 ? 0.1807 0.2280 0.2247 -0.0138 0.0034 -0.0535 218 ALA B CB 3073 N N . THR B 169 ? 0.1693 0.2131 0.2312 -0.0172 0.0113 -0.0675 219 THR B N 3074 C CA . THR B 169 ? 0.1848 0.2272 0.2505 -0.0178 0.0151 -0.0719 219 THR B CA 3075 C C . THR B 169 ? 0.2322 0.2779 0.2867 -0.0177 0.0152 -0.0708 219 THR B C 3076 O O . THR B 169 ? 0.2518 0.3032 0.2965 -0.0187 0.0126 -0.0709 219 THR B O 3077 C CB . THR B 169 ? 0.2510 0.2964 0.3249 -0.0203 0.0167 -0.0818 219 THR B CB 3078 O OG1 . THR B 169 ? 0.3083 0.3496 0.3929 -0.0204 0.0167 -0.0815 219 THR B OG1 3079 C CG2 . THR B 169 ? 0.2493 0.2931 0.3292 -0.0208 0.0212 -0.0872 219 THR B CG2 3080 N N . ARG B 170 ? 0.1740 0.2163 0.2300 -0.0168 0.0182 -0.0692 220 ARG B N 3081 C CA . ARG B 170 ? 0.1825 0.2281 0.2285 -0.0172 0.0191 -0.0685 220 ARG B CA 3082 C C . ARG B 170 ? 0.2454 0.2902 0.2984 -0.0177 0.0238 -0.0736 220 ARG B C 3083 O O . ARG B 170 ? 0.2187 0.2584 0.2843 -0.0166 0.0254 -0.0744 220 ARG B O 3084 C CB . ARG B 170 ? 0.1865 0.2285 0.2262 -0.0150 0.0176 -0.0590 220 ARG B CB 3085 C CG . ARG B 170 ? 0.1855 0.2283 0.2190 -0.0143 0.0132 -0.0539 220 ARG B CG 3086 C CD . ARG B 170 ? 0.2468 0.2847 0.2776 -0.0121 0.0122 -0.0454 220 ARG B CD 3087 N NE . ARG B 170 ? 0.2324 0.2697 0.2625 -0.0110 0.0088 -0.0415 220 ARG B NE 3088 C CZ . ARG B 170 ? 0.2555 0.2886 0.2923 -0.0101 0.0088 -0.0396 220 ARG B CZ 3089 N NH1 . ARG B 170 ? 0.2102 0.2388 0.2545 -0.0100 0.0112 -0.0401 220 ARG B NH1 3090 N NH2 . ARG B 170 ? 0.2642 0.2975 0.3006 -0.0093 0.0063 -0.0368 220 ARG B NH2 3091 N N . PRO B 171 ? 0.2498 0.2995 0.2953 -0.0194 0.0261 -0.0769 221 PRO B N 3092 C CA . PRO B 171 ? 0.2575 0.3070 0.3112 -0.0197 0.0313 -0.0820 221 PRO B CA 3093 C C . PRO B 171 ? 0.2572 0.2998 0.3187 -0.0167 0.0316 -0.0753 221 PRO B C 3094 O O . PRO B 171 ? 0.2007 0.2406 0.2561 -0.0151 0.0288 -0.0668 221 PRO B O 3095 C CB . PRO B 171 ? 0.2983 0.3544 0.3396 -0.0223 0.0335 -0.0846 221 PRO B CB 3096 C CG . PRO B 171 ? 0.3510 0.4112 0.3781 -0.0237 0.0291 -0.0817 221 PRO B CG 3097 C CD . PRO B 171 ? 0.2837 0.3391 0.3135 -0.0211 0.0243 -0.0749 221 PRO B CD 3098 N N . LYS B 172 ? 0.1847 0.2245 0.2607 -0.0158 0.0346 -0.0790 222 LYS B N 3099 C CA . LYS B 172 ? 0.1571 0.1911 0.2400 -0.0131 0.0338 -0.0719 222 LYS B CA 3100 C C . LYS B 172 ? 0.1872 0.2234 0.2637 -0.0131 0.0352 -0.0691 222 LYS B C 3101 O O . LYS B 172 ? 0.1732 0.2146 0.2474 -0.0150 0.0391 -0.0752 222 LYS B O 3102 C CB . LYS B 172 ? 0.2285 0.2585 0.3298 -0.0118 0.0358 -0.0752 222 LYS B CB 3103 C CG . LYS B 172 ? 0.3307 0.3559 0.4404 -0.0113 0.0338 -0.0746 222 LYS B CG 3104 C CD . LYS B 172 ? 0.5000 0.5207 0.6288 -0.0098 0.0357 -0.0765 222 LYS B CD 3105 C CE . LYS B 172 ? 0.7400 0.7550 0.8783 -0.0096 0.0340 -0.0750 222 LYS B CE 3106 N NZ . LYS B 172 ? 0.9220 0.9313 1.0789 -0.0077 0.0348 -0.0743 222 LYS B NZ 3107 N N . VAL B 173 ? 0.1381 0.1706 0.2106 -0.0113 0.0323 -0.0602 223 VAL B N 3108 C CA . VAL B 173 ? 0.1481 0.1817 0.2174 -0.0112 0.0336 -0.0571 223 VAL B CA 3109 C C . VAL B 173 ? 0.1964 0.2245 0.2750 -0.0087 0.0315 -0.0513 223 VAL B C 3110 O O . VAL B 173 ? 0.1276 0.1513 0.2047 -0.0076 0.0278 -0.0457 223 VAL B O 3111 C CB . VAL B 173 ? 0.2033 0.2385 0.2565 -0.0121 0.0318 -0.0520 223 VAL B CB 3112 C CG1 . VAL B 173 ? 0.2099 0.2455 0.2616 -0.0121 0.0332 -0.0484 223 VAL B CG1 3113 C CG2 . VAL B 173 ? 0.2090 0.2502 0.2525 -0.0148 0.0331 -0.0571 223 VAL B CG2 3114 N N . ASN B 174 ? 0.1535 0.1823 0.2418 -0.0080 0.0339 -0.0527 224 ASN B N 3115 C CA . ASN B 174 ? 0.1831 0.2071 0.2812 -0.0057 0.0312 -0.0470 224 ASN B CA 3116 C C . ASN B 174 ? 0.2081 0.2271 0.3154 -0.0045 0.0288 -0.0460 224 ASN B C 3117 O O . ASN B 174 ? 0.2164 0.2308 0.3249 -0.0033 0.0250 -0.0390 224 ASN B O 3118 C CB . ASN B 174 ? 0.1746 0.1968 0.2627 -0.0054 0.0278 -0.0388 224 ASN B CB 3119 C CG . ASN B 174 ? 0.3881 0.4144 0.4694 -0.0067 0.0302 -0.0392 224 ASN B CG 3120 O OD1 . ASN B 174 ? 0.2403 0.2711 0.3242 -0.0080 0.0346 -0.0452 224 ASN B OD1 3121 N ND2 . ASN B 174 ? 0.2618 0.2866 0.3340 -0.0069 0.0279 -0.0331 224 ASN B ND2 3122 N N . GLY B 175 ? 0.1698 0.1901 0.2833 -0.0052 0.0314 -0.0533 225 GLY B N 3123 C CA . GLY B 175 ? 0.1864 0.2020 0.3096 -0.0046 0.0301 -0.0536 225 GLY B CA 3124 C C . GLY B 175 ? 0.2332 0.2462 0.3477 -0.0053 0.0272 -0.0499 225 GLY B C 3125 O O . GLY B 175 ? 0.2486 0.2575 0.3712 -0.0051 0.0262 -0.0493 225 GLY B O 3126 N N . GLN B 176 ? 0.1740 0.1896 0.2732 -0.0062 0.0261 -0.0477 226 GLN B N 3127 C CA . GLN B 176 ? 0.1563 0.1702 0.2474 -0.0068 0.0234 -0.0442 226 GLN B CA 3128 C C . GLN B 176 ? 0.1575 0.1765 0.2386 -0.0085 0.0238 -0.0486 226 GLN B C 3129 O O . GLN B 176 ? 0.1778 0.2012 0.2507 -0.0092 0.0248 -0.0501 226 GLN B O 3130 C CB . GLN B 176 ? 0.1518 0.1632 0.2346 -0.0060 0.0205 -0.0356 226 GLN B CB 3131 C CG . GLN B 176 ? 0.2231 0.2304 0.3133 -0.0046 0.0189 -0.0301 226 GLN B CG 3132 C CD . GLN B 176 ? 0.3836 0.3859 0.4840 -0.0043 0.0178 -0.0282 226 GLN B CD 3133 O OE1 . GLN B 176 ? 0.3909 0.3919 0.4906 -0.0053 0.0177 -0.0289 226 GLN B OE1 3134 N NE2 . GLN B 176 ? 0.4192 0.4189 0.5303 -0.0031 0.0170 -0.0258 226 GLN B NE2 3135 N N . GLY B 177 ? 0.1562 0.1746 0.2382 -0.0092 0.0228 -0.0499 227 GLY B N 3136 C CA . GLY B 177 ? 0.1594 0.1825 0.2322 -0.0107 0.0217 -0.0527 227 GLY B CA 3137 C C . GLY B 177 ? 0.2021 0.2242 0.2658 -0.0100 0.0187 -0.0459 227 GLY B C 3138 O O . GLY B 177 ? 0.1951 0.2213 0.2498 -0.0105 0.0171 -0.0460 227 GLY B O 3139 N N . GLY B 178 ? 0.1695 0.1864 0.2357 -0.0089 0.0177 -0.0397 228 GLY B N 3140 C CA . GLY B 178 ? 0.1759 0.1916 0.2342 -0.0083 0.0155 -0.0338 228 GLY B CA 3141 C C . GLY B 178 ? 0.1965 0.2134 0.2465 -0.0077 0.0151 -0.0307 228 GLY B C 3142 O O . GLY B 178 ? 0.1695 0.1874 0.2204 -0.0076 0.0166 -0.0320 228 GLY B O 3143 N N . ARG B 179 ? 0.1780 0.1948 0.2209 -0.0073 0.0132 -0.0268 229 ARG B N 3144 C CA . ARG B 179 ? 0.1596 0.1769 0.1950 -0.0068 0.0128 -0.0235 229 ARG B CA 3145 C C . ARG B 179 ? 0.1694 0.1833 0.2022 -0.0061 0.0115 -0.0183 229 ARG B C 3146 O O . ARG B 179 ? 0.1569 0.1700 0.1909 -0.0061 0.0107 -0.0178 229 ARG B O 3147 C CB . ARG B 179 ? 0.1477 0.1697 0.1761 -0.0072 0.0119 -0.0250 229 ARG B CB 3148 C CG . ARG B 179 ? 0.1461 0.1727 0.1750 -0.0086 0.0134 -0.0310 229 ARG B CG 3149 C CD . ARG B 179 ? 0.1751 0.2024 0.2029 -0.0091 0.0160 -0.0316 229 ARG B CD 3150 N NE . ARG B 179 ? 0.2062 0.2386 0.2333 -0.0109 0.0180 -0.0382 229 ARG B NE 3151 C CZ . ARG B 179 ? 0.2402 0.2731 0.2760 -0.0114 0.0205 -0.0441 229 ARG B CZ 3152 N NH1 . ARG B 179 ? 0.1944 0.2226 0.2403 -0.0101 0.0207 -0.0432 229 ARG B NH1 3153 N NH2 . ARG B 179 ? 0.2197 0.2576 0.2543 -0.0134 0.0228 -0.0509 229 ARG B NH2 3154 N N . MET B 180 ? 0.1402 0.1522 0.1701 -0.0058 0.0116 -0.0149 230 MET B N 3155 C CA . MET B 180 ? 0.1271 0.1361 0.1541 -0.0055 0.0106 -0.0107 230 MET B CA 3156 C C . MET B 180 ? 0.2026 0.2129 0.2235 -0.0052 0.0100 -0.0091 230 MET B C 3157 O O . MET B 180 ? 0.1983 0.2099 0.2170 -0.0054 0.0108 -0.0090 230 MET B O 3158 C CB . MET B 180 ? 0.1609 0.1668 0.1901 -0.0058 0.0108 -0.0081 230 MET B CB 3159 C CG . MET B 180 ? 0.1972 0.2009 0.2318 -0.0063 0.0107 -0.0079 230 MET B CG 3160 S SD . MET B 180 ? 0.2541 0.2546 0.2908 -0.0068 0.0096 -0.0039 230 MET B SD 3161 C CE . MET B 180 ? 0.2066 0.2047 0.2500 -0.0074 0.0095 -0.0034 230 MET B CE 3162 N N . GLU B 181 ? 0.1553 0.1652 0.1745 -0.0046 0.0089 -0.0078 231 GLU B N 3163 C CA . GLU B 181 ? 0.1569 0.1672 0.1717 -0.0040 0.0078 -0.0056 231 GLU B CA 3164 C C . GLU B 181 ? 0.1798 0.1862 0.1943 -0.0039 0.0082 -0.0029 231 GLU B C 3165 O O . GLU B 181 ? 0.1595 0.1643 0.1760 -0.0039 0.0083 -0.0031 231 GLU B O 3166 C CB . GLU B 181 ? 0.1725 0.1853 0.1881 -0.0032 0.0060 -0.0064 231 GLU B CB 3167 C CG . GLU B 181 ? 0.2839 0.2968 0.2964 -0.0022 0.0042 -0.0033 231 GLU B CG 3168 C CD . GLU B 181 ? 0.4445 0.4604 0.4590 -0.0011 0.0015 -0.0037 231 GLU B CD 3169 O OE1 . GLU B 181 ? 0.5235 0.5430 0.5400 -0.0015 0.0008 -0.0070 231 GLU B OE1 3170 O OE2 . GLU B 181 ? 0.3939 0.4088 0.4090 0.0002 -0.0001 -0.0008 231 GLU B OE2 3171 N N . PHE B 182 ? 0.1407 0.1458 0.1527 -0.0042 0.0086 -0.0008 232 PHE B N 3172 C CA . PHE B 182 ? 0.1286 0.1302 0.1404 -0.0045 0.0090 0.0010 232 PHE B CA 3173 C C . PHE B 182 ? 0.1683 0.1687 0.1791 -0.0037 0.0083 0.0030 232 PHE B C 3174 O O . PHE B 182 ? 0.1774 0.1793 0.1860 -0.0032 0.0074 0.0045 232 PHE B O 3175 C CB . PHE B 182 ? 0.1632 0.1639 0.1747 -0.0056 0.0098 0.0018 232 PHE B CB 3176 C CG . PHE B 182 ? 0.1639 0.1651 0.1782 -0.0062 0.0100 0.0005 232 PHE B CG 3177 C CD1 . PHE B 182 ? 0.1627 0.1619 0.1778 -0.0069 0.0096 0.0009 232 PHE B CD1 3178 C CD2 . PHE B 182 ? 0.2041 0.2079 0.2205 -0.0061 0.0105 -0.0011 232 PHE B CD2 3179 C CE1 . PHE B 182 ? 0.1972 0.1964 0.2152 -0.0074 0.0092 0.0008 232 PHE B CE1 3180 C CE2 . PHE B 182 ? 0.2126 0.2162 0.2336 -0.0063 0.0105 -0.0020 232 PHE B CE2 3181 C CZ . PHE B 182 ? 0.1999 0.2011 0.2217 -0.0069 0.0095 -0.0005 232 PHE B CZ 3182 N N . SER B 183 ? 0.1410 0.1386 0.1535 -0.0037 0.0087 0.0031 233 SER B N 3183 C CA . SER B 183 ? 0.1627 0.1580 0.1764 -0.0028 0.0083 0.0048 233 SER B CA 3184 C C . SER B 183 ? 0.2029 0.1948 0.2170 -0.0041 0.0098 0.0045 233 SER B C 3185 O O . SER B 183 ? 0.1873 0.1790 0.2004 -0.0056 0.0106 0.0030 233 SER B O 3186 C CB . SER B 183 ? 0.2065 0.2026 0.2243 -0.0013 0.0076 0.0036 233 SER B CB 3187 O OG . SER B 183 ? 0.2363 0.2363 0.2543 -0.0004 0.0060 0.0030 233 SER B OG 3188 N N . TRP B 184 ? 0.1893 0.1783 0.2053 -0.0036 0.0099 0.0060 234 TRP B N 3189 C CA . TRP B 184 ? 0.1904 0.1762 0.2073 -0.0052 0.0113 0.0051 234 TRP B CA 3190 C C . TRP B 184 ? 0.2183 0.2010 0.2404 -0.0041 0.0118 0.0047 234 TRP B C 3191 O O . TRP B 184 ? 0.2084 0.1912 0.2336 -0.0019 0.0105 0.0065 234 TRP B O 3192 C CB . TRP B 184 ? 0.1803 0.1654 0.1952 -0.0065 0.0115 0.0073 234 TRP B CB 3193 C CG . TRP B 184 ? 0.1912 0.1750 0.2063 -0.0056 0.0109 0.0112 234 TRP B CG 3194 C CD1 . TRP B 184 ? 0.2306 0.2171 0.2426 -0.0049 0.0098 0.0138 234 TRP B CD1 3195 C CD2 . TRP B 184 ? 0.2102 0.1897 0.2287 -0.0056 0.0113 0.0131 234 TRP B CD2 3196 N NE1 . TRP B 184 ? 0.2467 0.2310 0.2589 -0.0046 0.0093 0.0179 234 TRP B NE1 3197 C CE2 . TRP B 184 ? 0.2706 0.2501 0.2873 -0.0050 0.0102 0.0179 234 TRP B CE2 3198 C CE3 . TRP B 184 ? 0.2386 0.2142 0.2615 -0.0065 0.0127 0.0112 234 TRP B CE3 3199 C CZ2 . TRP B 184 ? 0.2842 0.2595 0.3040 -0.0049 0.0101 0.0216 234 TRP B CZ2 3200 C CZ3 . TRP B 184 ? 0.2797 0.2510 0.3066 -0.0063 0.0129 0.0139 234 TRP B CZ3 3201 C CH2 . TRP B 184 ? 0.2982 0.2690 0.3237 -0.0054 0.0116 0.0196 234 TRP B CH2 3202 N N . THR B 185 ? 0.1723 0.1526 0.1958 -0.0058 0.0136 0.0019 235 THR B N 3203 C CA . THR B 185 ? 0.1757 0.1526 0.2055 -0.0051 0.0148 0.0005 235 THR B CA 3204 C C . THR B 185 ? 0.1938 0.1677 0.2238 -0.0076 0.0165 -0.0015 235 THR B C 3205 O O . THR B 185 ? 0.2231 0.1985 0.2482 -0.0100 0.0166 -0.0025 235 THR B O 3206 C CB . THR B 185 ? 0.2229 0.2011 0.2562 -0.0045 0.0162 -0.0035 235 THR B CB 3207 O OG1 . THR B 185 ? 0.2996 0.2748 0.3416 -0.0029 0.0171 -0.0046 235 THR B OG1 3208 C CG2 . THR B 185 ? 0.2486 0.2277 0.2781 -0.0075 0.0185 -0.0080 235 THR B CG2 3209 N N . LEU B 186 ? 0.1793 0.1492 0.2159 -0.0072 0.0176 -0.0024 236 LEU B N 3210 C CA . LEU B 186 ? 0.2052 0.1722 0.2434 -0.0099 0.0195 -0.0055 236 LEU B CA 3211 C C . LEU B 186 ? 0.2849 0.2512 0.3275 -0.0104 0.0223 -0.0118 236 LEU B C 3212 O O . LEU B 186 ? 0.2940 0.2587 0.3444 -0.0079 0.0229 -0.0123 236 LEU B O 3213 C CB . LEU B 186 ? 0.2313 0.1936 0.2749 -0.0091 0.0192 -0.0017 236 LEU B CB 3214 C CG . LEU B 186 ? 0.3399 0.2999 0.3833 -0.0121 0.0201 -0.0022 236 LEU B CG 3215 C CD1 . LEU B 186 ? 0.3525 0.3168 0.3880 -0.0140 0.0189 -0.0010 236 LEU B CD1 3216 C CD2 . LEU B 186 ? 0.3863 0.3417 0.4349 -0.0111 0.0197 0.0033 236 LEU B CD2 3217 N N . LEU B 187 ? 0.2333 0.2017 0.2704 -0.0137 0.0238 -0.0164 237 LEU B N 3218 C CA . LEU B 187 ? 0.2184 0.1872 0.2578 -0.0152 0.0271 -0.0231 237 LEU B CA 3219 C C . LEU B 187 ? 0.2439 0.2091 0.2881 -0.0175 0.0295 -0.0279 237 LEU B C 3220 O O . LEU B 187 ? 0.2240 0.1893 0.2635 -0.0205 0.0288 -0.0286 237 LEU B O 3221 C CB . LEU B 187 ? 0.2234 0.1967 0.2532 -0.0181 0.0274 -0.0251 237 LEU B CB 3222 C CG . LEU B 187 ? 0.2411 0.2156 0.2705 -0.0207 0.0314 -0.0321 237 LEU B CG 3223 C CD1 . LEU B 187 ? 0.2343 0.2094 0.2714 -0.0177 0.0333 -0.0333 237 LEU B CD1 3224 C CD2 . LEU B 187 ? 0.2261 0.2046 0.2441 -0.0243 0.0311 -0.0325 237 LEU B CD2 3225 N N . ASP B 188 ? 0.2299 0.1920 0.2847 -0.0158 0.0320 -0.0312 238 ASP B N 3226 C CA . ASP B 188 ? 0.2266 0.1845 0.2884 -0.0177 0.0347 -0.0363 238 ASP B CA 3227 C C . ASP B 188 ? 0.2514 0.2118 0.3070 -0.0227 0.0376 -0.0443 238 ASP B C 3228 O O . ASP B 188 ? 0.2335 0.1983 0.2818 -0.0243 0.0387 -0.0467 238 ASP B O 3229 C CB . ASP B 188 ? 0.2589 0.2130 0.3355 -0.0144 0.0368 -0.0384 238 ASP B CB 3230 C CG . ASP B 188 ? 0.4825 0.4326 0.5666 -0.0101 0.0336 -0.0303 238 ASP B CG 3231 O OD1 . ASP B 188 ? 0.5085 0.4567 0.5890 -0.0107 0.0312 -0.0250 238 ASP B OD1 3232 O OD2 . ASP B 188 ? 0.5684 0.5174 0.6627 -0.0063 0.0334 -0.0294 238 ASP B OD2 3233 N N . MET B 189 ? 0.2543 0.2117 0.3132 -0.0256 0.0392 -0.0488 239 MET B N 3234 C CA . MET B 189 ? 0.2584 0.2185 0.3115 -0.0309 0.0421 -0.0573 239 MET B CA 3235 C C . MET B 189 ? 0.2909 0.2524 0.3481 -0.0309 0.0469 -0.0643 239 MET B C 3236 O O . MET B 189 ? 0.2952 0.2532 0.3657 -0.0276 0.0491 -0.0658 239 MET B O 3237 C CB . MET B 189 ? 0.2935 0.2501 0.3517 -0.0339 0.0434 -0.0623 239 MET B CB 3238 C CG . MET B 189 ? 0.3463 0.3021 0.4016 -0.0344 0.0393 -0.0562 239 MET B CG 3239 S SD . MET B 189 ? 0.4393 0.3900 0.5041 -0.0376 0.0411 -0.0617 239 MET B SD 3240 C CE . MET B 189 ? 0.4190 0.3618 0.5006 -0.0324 0.0429 -0.0588 239 MET B CE 3241 N N . TRP B 190 ? 0.2491 0.2158 0.2951 -0.0349 0.0485 -0.0683 240 TRP B N 3242 C CA . TRP B 190 ? 0.2583 0.2276 0.3053 -0.0367 0.0539 -0.0760 240 TRP B CA 3243 C C . TRP B 190 ? 0.3017 0.2724 0.3531 -0.0324 0.0542 -0.0724 240 TRP B C 3244 O O . TRP B 190 ? 0.3254 0.2985 0.3798 -0.0333 0.0591 -0.0785 240 TRP B O 3245 C CB . TRP B 190 ? 0.2752 0.2414 0.3340 -0.0381 0.0593 -0.0860 240 TRP B CB 3246 C CG . TRP B 190 ? 0.3029 0.2665 0.3612 -0.0415 0.0585 -0.0891 240 TRP B CG 3247 C CD1 . TRP B 190 ? 0.3443 0.3017 0.4158 -0.0394 0.0584 -0.0893 240 TRP B CD1 3248 C CD2 . TRP B 190 ? 0.3139 0.2812 0.3581 -0.0476 0.0572 -0.0918 240 TRP B CD2 3249 N NE1 . TRP B 190 ? 0.3478 0.3048 0.4148 -0.0440 0.0575 -0.0925 240 TRP B NE1 3250 C CE2 . TRP B 190 ? 0.3679 0.3313 0.4182 -0.0490 0.0565 -0.0942 240 TRP B CE2 3251 C CE3 . TRP B 190 ? 0.3361 0.3098 0.3634 -0.0520 0.0560 -0.0917 240 TRP B CE3 3252 C CZ2 . TRP B 190 ? 0.3601 0.3264 0.4007 -0.0547 0.0547 -0.0974 240 TRP B CZ2 3253 C CZ3 . TRP B 190 ? 0.3635 0.3398 0.3805 -0.0576 0.0538 -0.0942 240 TRP B CZ3 3254 C CH2 . TRP B 190 ? 0.3715 0.3445 0.3953 -0.0589 0.0531 -0.0974 240 TRP B CH2 3255 N N . ASP B 191 ? 0.2383 0.2082 0.2901 -0.0280 0.0492 -0.0629 241 ASP B N 3256 C CA . ASP B 191 ? 0.2252 0.1971 0.2803 -0.0243 0.0487 -0.0593 241 ASP B CA 3257 C C . ASP B 191 ? 0.2581 0.2346 0.2989 -0.0266 0.0470 -0.0560 241 ASP B C 3258 O O . ASP B 191 ? 0.2449 0.2221 0.2751 -0.0292 0.0441 -0.0532 241 ASP B O 3259 C CB . ASP B 191 ? 0.2424 0.2111 0.3051 -0.0187 0.0442 -0.0512 241 ASP B CB 3260 C CG . ASP B 191 ? 0.2980 0.2687 0.3680 -0.0146 0.0439 -0.0491 241 ASP B CG 3261 O OD1 . ASP B 191 ? 0.3148 0.2882 0.3887 -0.0155 0.0483 -0.0553 241 ASP B OD1 3262 O OD2 . ASP B 191 ? 0.3047 0.2747 0.3765 -0.0108 0.0394 -0.0417 241 ASP B OD2 3263 N N . THR B 192 ? 0.2096 0.1892 0.2514 -0.0254 0.0484 -0.0556 242 THR B N 3264 C CA . THR B 192 ? 0.1950 0.1784 0.2252 -0.0273 0.0470 -0.0520 242 THR B CA 3265 C C . THR B 192 ? 0.2360 0.2198 0.2688 -0.0227 0.0428 -0.0446 242 THR B C 3266 O O . THR B 192 ? 0.2476 0.2310 0.2913 -0.0188 0.0430 -0.0443 242 THR B O 3267 C CB . THR B 192 ? 0.2787 0.2658 0.3071 -0.0308 0.0528 -0.0583 242 THR B CB 3268 O OG1 . THR B 192 ? 0.3127 0.2999 0.3367 -0.0357 0.0567 -0.0657 242 THR B OG1 3269 C CG2 . THR B 192 ? 0.2617 0.2523 0.2792 -0.0329 0.0518 -0.0541 242 THR B CG2 3270 N N . ILE B 193 ? 0.1960 0.1809 0.2192 -0.0234 0.0391 -0.0389 243 ILE B N 3271 C CA . ILE B 193 ? 0.1906 0.1768 0.2148 -0.0202 0.0359 -0.0331 243 ILE B CA 3272 C C . ILE B 193 ? 0.2372 0.2268 0.2563 -0.0226 0.0379 -0.0337 243 ILE B C 3273 O O . ILE B 193 ? 0.1992 0.1899 0.2088 -0.0271 0.0393 -0.0349 243 ILE B O 3274 C CB . ILE B 193 ? 0.2357 0.2208 0.2548 -0.0192 0.0310 -0.0269 243 ILE B CB 3275 C CG1 . ILE B 193 ? 0.2194 0.2060 0.2402 -0.0160 0.0281 -0.0221 243 ILE B CG1 3276 C CG2 . ILE B 193 ? 0.2271 0.2131 0.2353 -0.0235 0.0300 -0.0263 243 ILE B CG2 3277 C CD1 . ILE B 193 ? 0.2098 0.1950 0.2300 -0.0139 0.0242 -0.0172 243 ILE B CD1 3278 N N . ASN B 194 ? 0.1916 0.1831 0.2172 -0.0199 0.0381 -0.0329 244 ASN B N 3279 C CA . ASN B 194 ? 0.1665 0.1610 0.1887 -0.0223 0.0403 -0.0334 244 ASN B CA 3280 C C . ASN B 194 ? 0.2229 0.2181 0.2452 -0.0198 0.0364 -0.0279 244 ASN B C 3281 O O . ASN B 194 ? 0.2155 0.2107 0.2453 -0.0157 0.0339 -0.0263 244 ASN B O 3282 C CB . ASN B 194 ? 0.1972 0.1939 0.2293 -0.0218 0.0451 -0.0390 244 ASN B CB 3283 C CG . ASN B 194 ? 0.4555 0.4519 0.4876 -0.0249 0.0501 -0.0458 244 ASN B CG 3284 O OD1 . ASN B 194 ? 0.4221 0.4196 0.4443 -0.0300 0.0530 -0.0478 244 ASN B OD1 3285 N ND2 . ASN B 194 ? 0.4047 0.3993 0.4473 -0.0222 0.0509 -0.0491 244 ASN B ND2 3286 N N . PHE B 195 ? 0.1762 0.1723 0.1908 -0.0224 0.0359 -0.0250 245 PHE B N 3287 C CA . PHE B 195 ? 0.1893 0.1861 0.2046 -0.0206 0.0327 -0.0207 245 PHE B CA 3288 C C . PHE B 195 ? 0.2023 0.2014 0.2189 -0.0226 0.0358 -0.0219 245 PHE B C 3289 O O . PHE B 195 ? 0.1874 0.1870 0.1983 -0.0268 0.0394 -0.0235 245 PHE B O 3290 C CB . PHE B 195 ? 0.2068 0.2021 0.2137 -0.0220 0.0294 -0.0159 245 PHE B CB 3291 C CG . PHE B 195 ? 0.2106 0.2041 0.2170 -0.0200 0.0261 -0.0140 245 PHE B CG 3292 C CD1 . PHE B 195 ? 0.2260 0.2194 0.2360 -0.0165 0.0228 -0.0113 245 PHE B CD1 3293 C CD2 . PHE B 195 ? 0.2091 0.2012 0.2114 -0.0219 0.0264 -0.0155 245 PHE B CD2 3294 C CE1 . PHE B 195 ? 0.2453 0.2373 0.2550 -0.0150 0.0204 -0.0097 245 PHE B CE1 3295 C CE2 . PHE B 195 ? 0.2171 0.2075 0.2202 -0.0202 0.0238 -0.0139 245 PHE B CE2 3296 C CZ . PHE B 195 ? 0.2191 0.2095 0.2256 -0.0169 0.0209 -0.0108 245 PHE B CZ 3297 N N . GLU B 196 ? 0.1758 0.1767 0.1996 -0.0199 0.0346 -0.0214 246 GLU B N 3298 C CA . GLU B 196 ? 0.1671 0.1702 0.1931 -0.0220 0.0374 -0.0222 246 GLU B CA 3299 C C . GLU B 196 ? 0.2249 0.2286 0.2541 -0.0199 0.0338 -0.0193 246 GLU B C 3300 O O . GLU B 196 ? 0.2380 0.2427 0.2728 -0.0161 0.0307 -0.0192 246 GLU B O 3301 C CB . GLU B 196 ? 0.1742 0.1803 0.2091 -0.0219 0.0416 -0.0277 246 GLU B CB 3302 C CG . GLU B 196 ? 0.3236 0.3325 0.3616 -0.0244 0.0450 -0.0290 246 GLU B CG 3303 C CD . GLU B 196 ? 0.5015 0.5142 0.5501 -0.0245 0.0497 -0.0349 246 GLU B CD 3304 O OE1 . GLU B 196 ? 0.3772 0.3900 0.4262 -0.0255 0.0533 -0.0390 246 GLU B OE1 3305 O OE2 . GLU B 196 ? 0.4358 0.4516 0.4925 -0.0239 0.0501 -0.0358 246 GLU B OE2 3306 N N . SER B 197 ? 0.1807 0.1838 0.2066 -0.0225 0.0343 -0.0168 247 SER B N 3307 C CA . SER B 197 ? 0.1682 0.1719 0.1985 -0.0204 0.0312 -0.0150 247 SER B CA 3308 C C . SER B 197 ? 0.1752 0.1788 0.2061 -0.0236 0.0334 -0.0139 247 SER B C 3309 O O . SER B 197 ? 0.2031 0.2048 0.2274 -0.0275 0.0358 -0.0119 247 SER B O 3310 C CB . SER B 197 ? 0.2015 0.2024 0.2267 -0.0191 0.0271 -0.0111 247 SER B CB 3311 O OG . SER B 197 ? 0.2500 0.2513 0.2791 -0.0179 0.0249 -0.0100 247 SER B OG 3312 N N . THR B 198 ? 0.1657 0.1714 0.2046 -0.0224 0.0327 -0.0153 248 THR B N 3313 C CA . THR B 198 ? 0.1677 0.1731 0.2093 -0.0251 0.0345 -0.0143 248 THR B CA 3314 C C . THR B 198 ? 0.1943 0.1974 0.2365 -0.0239 0.0308 -0.0116 248 THR B C 3315 O O . THR B 198 ? 0.2050 0.2071 0.2509 -0.0257 0.0317 -0.0107 248 THR B O 3316 C CB . THR B 198 ? 0.1686 0.1784 0.2202 -0.0251 0.0368 -0.0188 248 THR B CB 3317 O OG1 . THR B 198 ? 0.1775 0.1901 0.2347 -0.0208 0.0326 -0.0209 248 THR B OG1 3318 C CG2 . THR B 198 ? 0.1830 0.1951 0.2356 -0.0266 0.0412 -0.0221 248 THR B CG2 3319 N N . GLY B 199 ? 0.1737 0.1756 0.2124 -0.0212 0.0272 -0.0102 249 GLY B N 3320 C CA . GLY B 199 ? 0.1655 0.1654 0.2047 -0.0201 0.0242 -0.0080 249 GLY B CA 3321 C C . GLY B 199 ? 0.2107 0.2117 0.2488 -0.0167 0.0211 -0.0088 249 GLY B C 3322 O O . GLY B 199 ? 0.2051 0.2088 0.2440 -0.0149 0.0208 -0.0111 249 GLY B O 3323 N N . ASN B 200 ? 0.1500 0.1490 0.1869 -0.0159 0.0189 -0.0066 250 ASN B N 3324 C CA . ASN B 200 ? 0.1335 0.1338 0.1698 -0.0131 0.0163 -0.0076 250 ASN B CA 3325 C C . ASN B 200 ? 0.1689 0.1685 0.1993 -0.0122 0.0155 -0.0060 250 ASN B C 3326 O O . ASN B 200 ? 0.1599 0.1608 0.1899 -0.0102 0.0138 -0.0066 250 ASN B O 3327 C CB . ASN B 200 ? 0.1424 0.1468 0.1833 -0.0114 0.0155 -0.0115 250 ASN B CB 3328 C CG . ASN B 200 ? 0.2259 0.2314 0.2736 -0.0125 0.0161 -0.0139 250 ASN B CG 3329 O OD1 . ASN B 200 ? 0.1797 0.1853 0.2306 -0.0143 0.0182 -0.0144 250 ASN B OD1 3330 N ND2 . ASN B 200 ? 0.1382 0.1446 0.1887 -0.0116 0.0148 -0.0159 250 ASN B ND2 3331 N N . LEU B 201 ? 0.1601 0.1579 0.1860 -0.0140 0.0168 -0.0042 251 LEU B N 3332 C CA . LEU B 201 ? 0.1370 0.1340 0.1578 -0.0136 0.0161 -0.0033 251 LEU B CA 3333 C C . LEU B 201 ? 0.1906 0.1856 0.2089 -0.0140 0.0141 -0.0001 251 LEU B C 3334 O O . LEU B 201 ? 0.1809 0.1741 0.1988 -0.0158 0.0139 0.0026 251 LEU B O 3335 C CB . LEU B 201 ? 0.1399 0.1362 0.1571 -0.0160 0.0186 -0.0037 251 LEU B CB 3336 C CG . LEU B 201 ? 0.2026 0.1976 0.2140 -0.0168 0.0183 -0.0030 251 LEU B CG 3337 C CD1 . LEU B 201 ? 0.1930 0.1886 0.2063 -0.0140 0.0173 -0.0044 251 LEU B CD1 3338 C CD2 . LEU B 201 ? 0.2529 0.2478 0.2605 -0.0200 0.0217 -0.0045 251 LEU B CD2 3339 N N . ILE B 202 ? 0.1415 0.1369 0.1588 -0.0124 0.0127 0.0000 252 ILE B N 3340 C CA . ILE B 202 ? 0.1527 0.1469 0.1685 -0.0126 0.0108 0.0025 252 ILE B CA 3341 C C . ILE B 202 ? 0.1826 0.1762 0.1934 -0.0137 0.0111 0.0026 252 ILE B C 3342 O O . ILE B 202 ? 0.1686 0.1627 0.1794 -0.0124 0.0115 0.0011 252 ILE B O 3343 C CB . ILE B 202 ? 0.1871 0.1827 0.2064 -0.0104 0.0097 0.0017 252 ILE B CB 3344 C CG1 . ILE B 202 ? 0.1965 0.1933 0.2214 -0.0096 0.0100 0.0000 252 ILE B CG1 3345 C CG2 . ILE B 202 ? 0.2102 0.2052 0.2297 -0.0108 0.0079 0.0041 252 ILE B CG2 3346 C CD1 . ILE B 202 ? 0.2056 0.2004 0.2337 -0.0109 0.0099 0.0016 252 ILE B CD1 3347 N N . ALA B 203 ? 0.1692 0.1616 0.1758 -0.0164 0.0112 0.0041 253 ALA B N 3348 C CA . ALA B 203 ? 0.1739 0.1660 0.1757 -0.0180 0.0122 0.0029 253 ALA B CA 3349 C C . ALA B 203 ? 0.2237 0.2156 0.2238 -0.0183 0.0098 0.0042 253 ALA B C 3350 O O . ALA B 203 ? 0.2122 0.2042 0.2131 -0.0185 0.0073 0.0071 253 ALA B O 3351 C CB . ALA B 203 ? 0.2061 0.1977 0.2025 -0.0216 0.0136 0.0035 253 ALA B CB 3352 N N . PRO B 204 ? 0.1851 0.1767 0.1835 -0.0187 0.0107 0.0020 254 PRO B N 3353 C CA . PRO B 204 ? 0.1781 0.1699 0.1750 -0.0197 0.0085 0.0031 254 PRO B CA 3354 C C . PRO B 204 ? 0.2344 0.2264 0.2249 -0.0235 0.0074 0.0041 254 PRO B C 3355 O O . PRO B 204 ? 0.2491 0.2410 0.2353 -0.0257 0.0096 0.0026 254 PRO B O 3356 C CB . PRO B 204 ? 0.1933 0.1842 0.1908 -0.0194 0.0102 0.0001 254 PRO B CB 3357 C CG . PRO B 204 ? 0.2449 0.2352 0.2423 -0.0194 0.0133 -0.0028 254 PRO B CG 3358 C CD . PRO B 204 ? 0.2115 0.2027 0.2105 -0.0182 0.0135 -0.0015 254 PRO B CD 3359 N N . GLU B 205 ? 0.2147 0.2077 0.2047 -0.0245 0.0040 0.0064 255 GLU B N 3360 C CA . GLU B 205 ? 0.2402 0.2340 0.2231 -0.0285 0.0021 0.0075 255 GLU B CA 3361 C C . GLU B 205 ? 0.2729 0.2672 0.2543 -0.0300 0.0024 0.0040 255 GLU B C 3362 O O . GLU B 205 ? 0.2655 0.2606 0.2403 -0.0337 0.0026 0.0021 255 GLU B O 3363 C CB . GLU B 205 ? 0.2740 0.2689 0.2582 -0.0288 -0.0027 0.0126 255 GLU B CB 3364 C CG . GLU B 205 ? 0.3847 0.3810 0.3605 -0.0332 -0.0055 0.0146 255 GLU B CG 3365 C CD . GLU B 205 ? 0.6360 0.6328 0.6119 -0.0340 -0.0103 0.0210 255 GLU B CD 3366 O OE1 . GLU B 205 ? 0.4553 0.4518 0.4402 -0.0307 -0.0123 0.0237 255 GLU B OE1 3367 O OE2 . GLU B 205 ? 0.4675 0.4651 0.4345 -0.0381 -0.0120 0.0234 255 GLU B OE2 3368 N N . TYR B 206 ? 0.2133 0.2073 0.2010 -0.0274 0.0025 0.0031 256 TYR B N 3369 C CA . TYR B 206 ? 0.2223 0.2163 0.2107 -0.0286 0.0027 0.0002 256 TYR B CA 3370 C C . TYR B 206 ? 0.2649 0.2566 0.2574 -0.0264 0.0062 -0.0026 256 TYR B C 3371 O O . TYR B 206 ? 0.2688 0.2596 0.2646 -0.0234 0.0076 -0.0017 256 TYR B O 3372 C CB . TYR B 206 ? 0.2364 0.2324 0.2294 -0.0282 -0.0009 0.0024 256 TYR B CB 3373 C CG . TYR B 206 ? 0.2996 0.2981 0.2905 -0.0301 -0.0056 0.0059 256 TYR B CG 3374 C CD1 . TYR B 206 ? 0.3407 0.3413 0.3264 -0.0340 -0.0083 0.0051 256 TYR B CD1 3375 C CD2 . TYR B 206 ? 0.3191 0.3182 0.3137 -0.0280 -0.0077 0.0100 256 TYR B CD2 3376 C CE1 . TYR B 206 ? 0.3809 0.3842 0.3646 -0.0358 -0.0135 0.0092 256 TYR B CE1 3377 C CE2 . TYR B 206 ? 0.3611 0.3621 0.3548 -0.0295 -0.0125 0.0142 256 TYR B CE2 3378 C CZ . TYR B 206 ? 0.5059 0.5091 0.4940 -0.0333 -0.0158 0.0141 256 TYR B CZ 3379 O OH . TYR B 206 ? 0.5932 0.5987 0.5805 -0.0348 -0.0214 0.0190 256 TYR B OH 3380 N N . GLY B 207 ? 0.2447 0.2355 0.2371 -0.0282 0.0074 -0.0060 257 GLY B N 3381 C CA . GLY B 207 ? 0.2284 0.2164 0.2258 -0.0266 0.0101 -0.0082 257 GLY B CA 3382 C C . GLY B 207 ? 0.2529 0.2411 0.2535 -0.0277 0.0088 -0.0084 257 GLY B C 3383 O O . GLY B 207 ? 0.2377 0.2282 0.2360 -0.0304 0.0061 -0.0085 257 GLY B O 3384 N N . PHE B 208 ? 0.1919 0.1777 0.1979 -0.0258 0.0104 -0.0081 258 PHE B N 3385 C CA . PHE B 208 ? 0.1745 0.1602 0.1843 -0.0270 0.0097 -0.0080 258 PHE B CA 3386 C C . PHE B 208 ? 0.2252 0.2073 0.2379 -0.0283 0.0123 -0.0118 258 PHE B C 3387 O O . PHE B 208 ? 0.1979 0.1766 0.2145 -0.0261 0.0144 -0.0110 258 PHE B O 3388 C CB . PHE B 208 ? 0.2033 0.1891 0.2172 -0.0243 0.0099 -0.0042 258 PHE B CB 3389 C CG . PHE B 208 ? 0.2225 0.2119 0.2356 -0.0231 0.0077 -0.0014 258 PHE B CG 3390 C CD1 . PHE B 208 ? 0.2812 0.2737 0.2973 -0.0243 0.0056 -0.0005 258 PHE B CD1 3391 C CD2 . PHE B 208 ? 0.2753 0.2651 0.2864 -0.0209 0.0078 0.0000 258 PHE B CD2 3392 C CE1 . PHE B 208 ? 0.2996 0.2953 0.3172 -0.0229 0.0037 0.0018 258 PHE B CE1 3393 C CE2 . PHE B 208 ? 0.3239 0.3165 0.3357 -0.0198 0.0060 0.0021 258 PHE B CE2 3394 C CZ . PHE B 208 ? 0.2932 0.2886 0.3085 -0.0208 0.0040 0.0030 258 PHE B CZ 3395 N N . LYS B 209 ? 0.2041 0.1871 0.2154 -0.0321 0.0117 -0.0158 259 LYS B N 3396 C CA . LYS B 209 ? 0.2076 0.1869 0.2228 -0.0337 0.0145 -0.0203 259 LYS B CA 3397 C C . LYS B 209 ? 0.2459 0.2231 0.2682 -0.0334 0.0148 -0.0184 259 LYS B C 3398 O O . LYS B 209 ? 0.2457 0.2259 0.2685 -0.0346 0.0125 -0.0167 259 LYS B O 3399 C CB . LYS B 209 ? 0.2495 0.2309 0.2604 -0.0384 0.0139 -0.0260 259 LYS B CB 3400 C CG . LYS B 209 ? 0.3005 0.2785 0.3169 -0.0407 0.0167 -0.0317 259 LYS B CG 3401 C CD . LYS B 209 ? 0.3994 0.3808 0.4101 -0.0460 0.0157 -0.0378 259 LYS B CD 3402 C CE . LYS B 209 ? 0.6704 0.6496 0.6876 -0.0490 0.0170 -0.0430 259 LYS B CE 3403 N NZ . LYS B 209 ? 0.8346 0.8177 0.8456 -0.0547 0.0160 -0.0497 259 LYS B NZ 3404 N N . ILE B 210 ? 0.2133 0.1855 0.2414 -0.0319 0.0176 -0.0184 260 ILE B N 3405 C CA . ILE B 210 ? 0.2280 0.1972 0.2627 -0.0321 0.0185 -0.0162 260 ILE B CA 3406 C C . ILE B 210 ? 0.2993 0.2682 0.3373 -0.0365 0.0188 -0.0216 260 ILE B C 3407 O O . ILE B 210 ? 0.3061 0.2715 0.3474 -0.0377 0.0211 -0.0265 260 ILE B O 3408 C CB . ILE B 210 ? 0.2691 0.2329 0.3088 -0.0289 0.0207 -0.0129 260 ILE B CB 3409 C CG1 . ILE B 210 ? 0.2738 0.2397 0.3091 -0.0253 0.0195 -0.0079 260 ILE B CG1 3410 C CG2 . ILE B 210 ? 0.2970 0.2571 0.3433 -0.0299 0.0219 -0.0101 260 ILE B CG2 3411 C CD1 . ILE B 210 ? 0.3694 0.3315 0.4079 -0.0220 0.0205 -0.0049 260 ILE B CD1 3412 N N . SER B 211 ? 0.2637 0.2367 0.3014 -0.0389 0.0165 -0.0214 261 SER B N 3413 C CA . SER B 211 ? 0.2766 0.2507 0.3167 -0.0435 0.0160 -0.0270 261 SER B CA 3414 C C . SER B 211 ? 0.3128 0.2832 0.3621 -0.0451 0.0179 -0.0271 261 SER B C 3415 O O . SER B 211 ? 0.3496 0.3191 0.4028 -0.0488 0.0186 -0.0328 261 SER B O 3416 C CB . SER B 211 ? 0.3453 0.3266 0.3808 -0.0457 0.0115 -0.0273 261 SER B CB 3417 O OG . SER B 211 ? 0.4420 0.4262 0.4777 -0.0431 0.0098 -0.0213 261 SER B OG 3418 N N . LYS B 212 ? 0.2328 0.2016 0.2856 -0.0429 0.0190 -0.0211 262 LYS B N 3419 C CA . LYS B 212 ? 0.2333 0.1982 0.2946 -0.0445 0.0214 -0.0200 262 LYS B CA 3420 C C . LYS B 212 ? 0.2780 0.2383 0.3401 -0.0409 0.0235 -0.0132 262 LYS B C 3421 O O . LYS B 212 ? 0.2615 0.2247 0.3183 -0.0381 0.0225 -0.0088 262 LYS B O 3422 C CB . LYS B 212 ? 0.2711 0.2413 0.3353 -0.0472 0.0198 -0.0196 262 LYS B CB 3423 C CG . LYS B 212 ? 0.5404 0.5071 0.6144 -0.0504 0.0224 -0.0201 262 LYS B CG 3424 C CD . LYS B 212 ? 0.7586 0.7259 0.8366 -0.0549 0.0216 -0.0280 262 LYS B CD 3425 C CE . LYS B 212 ? 0.9855 0.9496 1.0742 -0.0584 0.0242 -0.0288 262 LYS B CE 3426 N NZ . LYS B 212 ? 1.1126 1.0769 1.2058 -0.0630 0.0237 -0.0374 262 LYS B NZ 3427 N N . ARG B 213 ? 0.2866 0.2399 0.3558 -0.0413 0.0263 -0.0124 263 ARG B N 3428 C CA . ARG B 213 ? 0.2835 0.2318 0.3543 -0.0385 0.0279 -0.0053 263 ARG B CA 3429 C C . ARG B 213 ? 0.3560 0.3015 0.4332 -0.0412 0.0301 -0.0019 263 ARG B C 3430 O O . ARG B 213 ? 0.3454 0.2902 0.4289 -0.0449 0.0310 -0.0064 263 ARG B O 3431 C CB . ARG B 213 ? 0.2803 0.2220 0.3553 -0.0364 0.0291 -0.0065 263 ARG B CB 3432 C CG . ARG B 213 ? 0.3144 0.2587 0.3834 -0.0337 0.0276 -0.0093 263 ARG B CG 3433 C CD . ARG B 213 ? 0.4352 0.3733 0.5108 -0.0317 0.0292 -0.0112 263 ARG B CD 3434 N NE . ARG B 213 ? 0.4540 0.3951 0.5251 -0.0299 0.0286 -0.0154 263 ARG B NE 3435 C CZ . ARG B 213 ? 0.5636 0.5062 0.6308 -0.0261 0.0274 -0.0116 263 ARG B CZ 3436 N NH1 . ARG B 213 ? 0.3853 0.3269 0.4517 -0.0236 0.0263 -0.0036 263 ARG B NH1 3437 N NH2 . ARG B 213 ? 0.3201 0.2655 0.3839 -0.0251 0.0274 -0.0159 263 ARG B NH2 3438 N N . GLY B 214 A 0.3401 0.2842 0.4155 -0.0397 0.0311 0.0058 263 GLY B N 3439 C CA . GLY B 214 A 0.3663 0.3075 0.4468 -0.0425 0.0338 0.0100 263 GLY B CA 3440 C C . GLY B 214 A 0.4702 0.4121 0.5449 -0.0410 0.0345 0.0183 263 GLY B C 3441 O O . GLY B 214 A 0.4491 0.3958 0.5157 -0.0383 0.0328 0.0195 263 GLY B O 3442 N N . SER B 215 ? 0.4920 0.4296 0.5706 -0.0433 0.0373 0.0238 264 SER B N 3443 C CA . SER B 215 ? 0.5172 0.4555 0.5894 -0.0429 0.0385 0.0320 264 SER B CA 3444 C C . SER B 215 ? 0.5729 0.5184 0.6427 -0.0459 0.0408 0.0318 264 SER B C 3445 O O . SER B 215 ? 0.5494 0.4968 0.6261 -0.0493 0.0422 0.0277 264 SER B O 3446 C CB . SER B 215 ? 0.5947 0.5240 0.6713 -0.0439 0.0404 0.0394 264 SER B CB 3447 O OG . SER B 215 ? 0.7588 0.6887 0.8266 -0.0428 0.0403 0.0478 264 SER B OG 3448 N N . SER B 216 ? 0.5645 0.5143 0.6253 -0.0446 0.0410 0.0360 265 SER B N 3449 C CA . SER B 216 ? 0.5876 0.5450 0.6443 -0.0465 0.0435 0.0365 265 SER B CA 3450 C C . SER B 216 ? 0.6955 0.6604 0.7473 -0.0435 0.0409 0.0318 265 SER B C 3451 O O . SER B 216 ? 0.7032 0.6724 0.7595 -0.0438 0.0396 0.0257 265 SER B O 3452 C CB . SER B 216 ? 0.6164 0.5756 0.6811 -0.0513 0.0472 0.0347 265 SER B CB 3453 O OG . SER B 216 ? 0.6564 0.6088 0.7235 -0.0543 0.0504 0.0409 265 SER B OG 3454 N N . GLY B 217 ? 0.6803 0.6465 0.7232 -0.0407 0.0397 0.0348 266 GLY B N 3455 C CA . GLY B 217 ? 0.6789 0.6510 0.7174 -0.0377 0.0372 0.0309 266 GLY B CA 3456 C C . GLY B 217 ? 0.7525 0.7317 0.7860 -0.0381 0.0392 0.0309 266 GLY B C 3457 O O . GLY B 217 ? 0.7755 0.7581 0.8117 -0.0414 0.0430 0.0306 266 GLY B O 3458 N N . ILE B 218 ? 0.7114 0.6930 0.7381 -0.0350 0.0370 0.0305 267 ILE B N 3459 C CA . ILE B 218 ? 0.7085 0.6969 0.7303 -0.0347 0.0385 0.0291 267 ILE B CA 3460 C C . ILE B 218 ? 0.7636 0.7549 0.7816 -0.0383 0.0434 0.0320 267 ILE B C 3461 O O . ILE B 218 ? 0.7607 0.7492 0.7713 -0.0392 0.0441 0.0378 267 ILE B O 3462 C CB . ILE B 218 ? 0.7488 0.7382 0.7645 -0.0309 0.0350 0.0283 267 ILE B CB 3463 C CG1 . ILE B 218 ? 0.7446 0.7336 0.7649 -0.0283 0.0313 0.0238 267 ILE B CG1 3464 C CG2 . ILE B 218 ? 0.7613 0.7576 0.7721 -0.0310 0.0369 0.0264 267 ILE B CG2 3465 C CD1 . ILE B 218 ? 0.7611 0.7504 0.7770 -0.0249 0.0281 0.0231 267 ILE B CD1 3466 N N . MET B 219 ? 0.7204 0.7177 0.7434 -0.0403 0.0468 0.0280 268 MET B N 3467 C CA . MET B 219 ? 1.0721 1.0737 1.0926 -0.0442 0.0526 0.0290 268 MET B CA 3468 C C . MET B 219 ? 1.3927 1.4013 1.4088 -0.0433 0.0540 0.0252 268 MET B C 3469 O O . MET B 219 ? 0.8991 0.9117 0.9215 -0.0411 0.0526 0.0195 268 MET B O 3470 C CB . MET B 219 ? 1.1024 1.1064 1.1337 -0.0476 0.0562 0.0265 268 MET B CB 3471 C CG . MET B 219 ? 1.1542 1.1515 1.1910 -0.0490 0.0553 0.0293 268 MET B CG 3472 S SD . MET B 219 ? 1.2235 1.2116 1.2517 -0.0498 0.0549 0.0384 268 MET B SD 3473 C CE . MET B 219 ? 1.1944 1.1860 1.2153 -0.0548 0.0617 0.0427 268 MET B CE # 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 GLY 1 55 55 GLY GLY A . n A 1 2 ILE 2 56 56 ILE ILE A . n A 1 3 PRO 3 57 57 PRO PRO A . n A 1 4 PRO 4 58 58 PRO PRO A . n A 1 5 LEU 5 59 59 LEU LEU A . n A 1 6 GLU 6 60 60 GLU GLU A . n A 1 7 LEU 7 61 61 LEU LEU A . n A 1 8 GLY 8 62 62 GLY GLY A . n A 1 9 ASP 9 63 63 ASP ASP A . n A 1 10 CYS 10 64 64 CYS CYS A . n A 1 11 SER 11 65 65 SER SER A . n A 1 12 ILE 12 66 66 ILE ILE A . n A 1 13 ALA 13 67 67 ALA ALA A . n A 1 14 GLY 14 68 68 GLY GLY A . n A 1 15 TRP 15 69 69 TRP TRP A . n A 1 16 LEU 16 70 70 LEU LEU A . n A 1 17 LEU 17 71 71 LEU LEU A . n A 1 18 GLY 18 72 72 GLY GLY A . n A 1 19 ASN 19 73 73 ASN ASN A . n A 1 20 PRO 20 74 74 PRO PRO A . n A 1 21 GLU 21 75 75 GLU GLU A . n A 1 22 CYS 22 76 76 CYS CYS A . n A 1 23 ASP 23 77 77 ASP ASP A . n A 1 24 ARG 24 78 78 ARG ARG A . n A 1 25 LEU 25 79 79 LEU LEU A . n A 1 26 LEU 26 80 80 LEU LEU A . n A 1 27 SER 27 81 81 SER SER A . n A 1 28 VAL 28 81 81 VAL VAL A A n A 1 29 PRO 29 82 82 PRO PRO A . n A 1 30 GLU 30 83 83 GLU GLU A . n A 1 31 TRP 31 84 84 TRP TRP A . n A 1 32 SER 32 85 85 SER SER A . n A 1 33 TYR 33 86 86 TYR TYR A . n A 1 34 ILE 34 87 87 ILE ILE A . n A 1 35 MET 35 88 88 MET MET A . n A 1 36 GLU 36 89 89 GLU GLU A . n A 1 37 LYS 37 90 90 LYS LYS A . n A 1 38 GLU 38 91 91 GLU GLU A . n A 1 39 ASN 39 92 92 ASN ASN A . n A 1 40 PRO 40 93 93 PRO PRO A . n A 1 41 ARG 41 94 94 ARG ARG A . n A 1 42 ASP 42 95 95 ASP ASP A . n A 1 43 GLY 43 95 95 GLY GLY A A n A 1 44 LEU 44 96 96 LEU LEU A . n A 1 45 CYS 45 97 97 CYS CYS A . n A 1 46 TYR 46 98 98 TYR TYR A . n A 1 47 PRO 47 99 99 PRO PRO A . n A 1 48 GLY 48 100 100 GLY GLY A . n A 1 49 SER 49 101 101 SER SER A . n A 1 50 PHE 50 102 102 PHE PHE A . n A 1 51 ASN 51 103 103 ASN ASN A . n A 1 52 ASP 52 104 104 ASP ASP A . n A 1 53 TYR 53 105 105 TYR TYR A . n A 1 54 GLU 54 106 106 GLU GLU A . n A 1 55 GLU 55 107 107 GLU GLU A . n A 1 56 LEU 56 108 108 LEU LEU A . n A 1 57 LYS 57 109 109 LYS LYS A . n A 1 58 HIS 58 110 110 HIS HIS A . n A 1 59 LEU 59 111 111 LEU LEU A . n A 1 60 LEU 60 112 112 LEU LEU A . n A 1 61 SER 61 113 113 SER SER A . n A 1 62 SER 62 114 114 SER SER A . n A 1 63 VAL 63 115 115 VAL VAL A . n A 1 64 LYS 64 116 116 LYS LYS A . n A 1 65 HIS 65 116 116 HIS HIS A A n A 1 66 PHE 66 116 116 PHE PHE A B n A 1 67 GLU 67 116 116 GLU GLU A C n A 1 68 LYS 68 117 117 LYS LYS A . n A 1 69 VAL 69 118 118 VAL VAL A . n A 1 70 LYS 70 119 119 LYS LYS A . n A 1 71 ILE 71 120 120 ILE ILE A . n A 1 72 LEU 72 121 121 LEU LEU A . n A 1 73 PRO 73 122 122 PRO PRO A . n A 1 74 LYS 74 123 123 LYS LYS A . n A 1 75 ASP 75 125 125 ASP ASP A . n A 1 76 ARG 76 126 126 ARG ARG A . n A 1 77 TRP 77 127 127 TRP TRP A . n A 1 78 THR 78 128 128 THR THR A . n A 1 79 GLN 79 129 129 GLN GLN A . n A 1 80 HIS 80 130 130 HIS HIS A . n A 1 81 THR 81 131 131 THR THR A . n A 1 82 THR 82 132 132 THR THR A . n A 1 83 THR 83 133 133 THR THR A . n A 1 84 GLY 84 134 134 GLY GLY A . n A 1 85 GLY 85 135 135 GLY GLY A . n A 1 86 SER 86 136 136 SER SER A . n A 1 87 ARG 87 137 137 ARG ARG A . n A 1 88 ALA 88 138 138 ALA ALA A . n A 1 89 CYS 89 139 139 CYS CYS A . n A 1 90 ALA 90 140 140 ALA ALA A . n A 1 91 VAL 91 141 141 VAL VAL A . n A 1 92 SER 92 142 142 SER SER A . n A 1 93 GLY 93 143 143 GLY GLY A . n A 1 94 ASN 94 144 144 ASN ASN A . n A 1 95 PRO 95 145 145 PRO PRO A . n A 1 96 SER 96 146 146 SER SER A . n A 1 97 PHE 97 147 147 PHE PHE A . n A 1 98 PHE 98 148 148 PHE PHE A . n A 1 99 ARG 99 149 149 ARG ARG A . n A 1 100 ASN 100 150 150 ASN ASN A . n A 1 101 MET 101 151 151 MET MET A . n A 1 102 VAL 102 152 152 VAL VAL A . n A 1 103 TRP 103 153 153 TRP TRP A . n A 1 104 LEU 104 154 154 LEU LEU A . n A 1 105 THR 105 155 155 THR THR A . n A 1 106 GLU 106 156 156 GLU GLU A . n A 1 107 LYS 107 157 157 LYS LYS A . n A 1 108 GLY 108 158 158 GLY GLY A . n A 1 109 SER 109 159 159 SER SER A . n A 1 110 ASN 110 160 160 ASN ASN A . n A 1 111 TYR 111 161 161 TYR TYR A . n A 1 112 PRO 112 162 162 PRO PRO A . n A 1 113 VAL 113 163 163 VAL VAL A . n A 1 114 ALA 114 164 164 ALA ALA A . n A 1 115 LYS 115 165 165 LYS LYS A . n A 1 116 GLY 116 166 166 GLY GLY A . n A 1 117 SER 117 167 167 SER SER A . n A 1 118 TYR 118 168 168 TYR TYR A . n A 1 119 ASN 119 169 169 ASN ASN A . n A 1 120 ASN 120 170 170 ASN ASN A . n A 1 121 THR 121 171 171 THR THR A . n A 1 122 SER 122 172 172 SER SER A . n A 1 123 GLY 123 173 173 GLY GLY A . n A 1 124 GLU 124 174 174 GLU GLU A . n A 1 125 GLN 125 175 175 GLN GLN A . n A 1 126 MET 126 176 176 MET MET A . n A 1 127 LEU 127 177 177 LEU LEU A . n A 1 128 ILE 128 178 178 ILE ILE A . n A 1 129 ILE 129 179 179 ILE ILE A . n A 1 130 TRP 130 180 180 TRP TRP A . n A 1 131 GLY 131 181 181 GLY GLY A . n A 1 132 VAL 132 182 182 VAL VAL A . n A 1 133 HIS 133 183 183 HIS HIS A . n A 1 134 HIS 134 184 184 HIS HIS A . n A 1 135 PRO 135 185 185 PRO PRO A . n A 1 136 ASN 136 186 186 ASN ASN A . n A 1 137 ASP 137 187 187 ASP ASP A . n A 1 138 GLU 138 188 188 GLU GLU A . n A 1 139 THR 139 189 189 THR THR A . n A 1 140 GLU 140 190 190 GLU GLU A . n A 1 141 GLN 141 191 191 GLN GLN A . n A 1 142 ARG 142 192 192 ARG ARG A . n A 1 143 THR 143 193 193 THR THR A . n A 1 144 LEU 144 194 194 LEU LEU A . n A 1 145 TYR 145 195 195 TYR TYR A . n A 1 146 GLN 146 196 196 GLN GLN A . n A 1 147 ASN 147 197 197 ASN ASN A . n A 1 148 VAL 148 198 198 VAL VAL A . n A 1 149 GLY 149 199 199 GLY GLY A . n A 1 150 THR 150 200 200 THR THR A . n A 1 151 TYR 151 201 201 TYR TYR A . n A 1 152 VAL 152 202 202 VAL VAL A . n A 1 153 SER 153 203 203 SER SER A . n A 1 154 VAL 154 204 204 VAL VAL A . n A 1 155 GLY 155 205 205 GLY GLY A . n A 1 156 THR 156 206 206 THR THR A . n A 1 157 SER 157 207 207 SER SER A . n A 1 158 THR 158 208 208 THR THR A . n A 1 159 LEU 159 209 209 LEU LEU A . n A 1 160 ASN 160 210 210 ASN ASN A . n A 1 161 LYS 161 211 211 LYS LYS A . n A 1 162 ARG 162 212 212 ARG ARG A . n A 1 163 SER 163 213 213 SER SER A . n A 1 164 THR 164 214 214 THR THR A . n A 1 165 PRO 165 215 215 PRO PRO A . n A 1 166 GLU 166 216 216 GLU GLU A . n A 1 167 ILE 167 217 217 ILE ILE A . n A 1 168 ALA 168 218 218 ALA ALA A . n A 1 169 THR 169 219 219 THR THR A . n A 1 170 ARG 170 220 220 ARG ARG A . n A 1 171 PRO 171 221 221 PRO PRO A . n A 1 172 LYS 172 222 222 LYS LYS A . n A 1 173 VAL 173 223 223 VAL VAL A . n A 1 174 ASN 174 224 224 ASN ASN A . n A 1 175 GLY 175 225 225 GLY GLY A . n A 1 176 GLN 176 226 226 GLN GLN A . n A 1 177 GLY 177 227 227 GLY GLY A . n A 1 178 GLY 178 228 228 GLY GLY A . n A 1 179 ARG 179 229 229 ARG ARG A . n A 1 180 MET 180 230 230 MET MET A . n A 1 181 GLU 181 231 231 GLU GLU A . n A 1 182 PHE 182 232 232 PHE PHE A . n A 1 183 SER 183 233 233 SER SER A . n A 1 184 TRP 184 234 234 TRP TRP A . n A 1 185 THR 185 235 235 THR THR A . n A 1 186 LEU 186 236 236 LEU LEU A . n A 1 187 LEU 187 237 237 LEU LEU A . n A 1 188 ASP 188 238 238 ASP ASP A . n A 1 189 MET 189 239 239 MET MET A . n A 1 190 TRP 190 240 240 TRP TRP A . n A 1 191 ASP 191 241 241 ASP ASP A . n A 1 192 THR 192 242 242 THR THR A . n A 1 193 ILE 193 243 243 ILE ILE A . n A 1 194 ASN 194 244 244 ASN ASN A . n A 1 195 PHE 195 245 245 PHE PHE A . n A 1 196 GLU 196 246 246 GLU GLU A . n A 1 197 SER 197 247 247 SER SER A . n A 1 198 THR 198 248 248 THR THR A . n A 1 199 GLY 199 249 249 GLY GLY A . n A 1 200 ASN 200 250 250 ASN ASN A . n A 1 201 LEU 201 251 251 LEU LEU A . n A 1 202 ILE 202 252 252 ILE ILE A . n A 1 203 ALA 203 253 253 ALA ALA A . n A 1 204 PRO 204 254 254 PRO PRO A . n A 1 205 GLU 205 255 255 GLU GLU A . n A 1 206 TYR 206 256 256 TYR TYR A . n A 1 207 GLY 207 257 257 GLY GLY A . n A 1 208 PHE 208 258 258 PHE PHE A . n A 1 209 LYS 209 259 259 LYS LYS A . n A 1 210 ILE 210 260 260 ILE ILE A . n A 1 211 SER 211 261 261 SER SER A . n A 1 212 LYS 212 262 262 LYS LYS A . n A 1 213 ARG 213 263 263 ARG ARG A . n A 1 214 GLY 214 263 263 GLY GLY A A n A 1 215 SER 215 264 264 SER SER A . n A 1 216 SER 216 265 265 SER SER A . n A 1 217 GLY 217 266 266 GLY GLY A . n A 1 218 ILE 218 267 267 ILE ILE A . n A 1 219 MET 219 268 268 MET MET A . n B 1 1 GLY 1 55 55 GLY GLY B . n B 1 2 ILE 2 56 56 ILE ILE B . n B 1 3 PRO 3 57 57 PRO PRO B . n B 1 4 PRO 4 58 58 PRO PRO B . n B 1 5 LEU 5 59 59 LEU LEU B . n B 1 6 GLU 6 60 60 GLU GLU B . n B 1 7 LEU 7 61 61 LEU LEU B . n B 1 8 GLY 8 62 62 GLY GLY B . n B 1 9 ASP 9 63 63 ASP ASP B . n B 1 10 CYS 10 64 64 CYS CYS B . n B 1 11 SER 11 65 65 SER SER B . n B 1 12 ILE 12 66 66 ILE ILE B . n B 1 13 ALA 13 67 67 ALA ALA B . n B 1 14 GLY 14 68 68 GLY GLY B . n B 1 15 TRP 15 69 69 TRP TRP B . n B 1 16 LEU 16 70 70 LEU LEU B . n B 1 17 LEU 17 71 71 LEU LEU B . n B 1 18 GLY 18 72 72 GLY GLY B . n B 1 19 ASN 19 73 73 ASN ASN B . n B 1 20 PRO 20 74 74 PRO PRO B . n B 1 21 GLU 21 75 75 GLU GLU B . n B 1 22 CYS 22 76 76 CYS CYS B . n B 1 23 ASP 23 77 77 ASP ASP B . n B 1 24 ARG 24 78 78 ARG ARG B . n B 1 25 LEU 25 79 79 LEU LEU B . n B 1 26 LEU 26 80 80 LEU LEU B . n B 1 27 SER 27 81 81 SER SER B . n B 1 28 VAL 28 81 81 VAL VAL B A n B 1 29 PRO 29 82 82 PRO PRO B . n B 1 30 GLU 30 83 83 GLU GLU B . n B 1 31 TRP 31 84 84 TRP TRP B . n B 1 32 SER 32 85 85 SER SER B . n B 1 33 TYR 33 86 86 TYR TYR B . n B 1 34 ILE 34 87 87 ILE ILE B . n B 1 35 MET 35 88 88 MET MET B . n B 1 36 GLU 36 89 89 GLU GLU B . n B 1 37 LYS 37 90 90 LYS LYS B . n B 1 38 GLU 38 91 91 GLU GLU B . n B 1 39 ASN 39 92 92 ASN ASN B . n B 1 40 PRO 40 93 93 PRO PRO B . n B 1 41 ARG 41 94 94 ARG ARG B . n B 1 42 ASP 42 95 95 ASP ASP B . n B 1 43 GLY 43 95 95 GLY GLY B A n B 1 44 LEU 44 96 96 LEU LEU B . n B 1 45 CYS 45 97 97 CYS CYS B . n B 1 46 TYR 46 98 98 TYR TYR B . n B 1 47 PRO 47 99 99 PRO PRO B . n B 1 48 GLY 48 100 100 GLY GLY B . n B 1 49 SER 49 101 101 SER SER B . n B 1 50 PHE 50 102 102 PHE PHE B . n B 1 51 ASN 51 103 103 ASN ASN B . n B 1 52 ASP 52 104 104 ASP ASP B . n B 1 53 TYR 53 105 105 TYR TYR B . n B 1 54 GLU 54 106 106 GLU GLU B . n B 1 55 GLU 55 107 107 GLU GLU B . n B 1 56 LEU 56 108 108 LEU LEU B . n B 1 57 LYS 57 109 109 LYS LYS B . n B 1 58 HIS 58 110 110 HIS HIS B . n B 1 59 LEU 59 111 111 LEU LEU B . n B 1 60 LEU 60 112 112 LEU LEU B . n B 1 61 SER 61 113 113 SER SER B . n B 1 62 SER 62 114 114 SER SER B . n B 1 63 VAL 63 115 115 VAL VAL B . n B 1 64 LYS 64 116 116 LYS LYS B . n B 1 65 HIS 65 116 116 HIS HIS B A n B 1 66 PHE 66 116 116 PHE PHE B B n B 1 67 GLU 67 116 116 GLU GLU B C n B 1 68 LYS 68 117 117 LYS LYS B . n B 1 69 VAL 69 118 118 VAL VAL B . n B 1 70 LYS 70 119 119 LYS LYS B . n B 1 71 ILE 71 120 120 ILE ILE B . n B 1 72 LEU 72 121 121 LEU LEU B . n B 1 73 PRO 73 122 122 PRO PRO B . n B 1 74 LYS 74 123 123 LYS LYS B . n B 1 75 ASP 75 125 125 ASP ASP B . n B 1 76 ARG 76 126 126 ARG ARG B . n B 1 77 TRP 77 127 127 TRP TRP B . n B 1 78 THR 78 128 128 THR THR B . n B 1 79 GLN 79 129 129 GLN GLN B . n B 1 80 HIS 80 130 130 HIS HIS B . n B 1 81 THR 81 131 131 THR THR B . n B 1 82 THR 82 132 132 THR THR B . n B 1 83 THR 83 133 133 THR THR B . n B 1 84 GLY 84 134 134 GLY GLY B . n B 1 85 GLY 85 135 135 GLY GLY B . n B 1 86 SER 86 136 136 SER SER B . n B 1 87 ARG 87 137 137 ARG ARG B . n B 1 88 ALA 88 138 138 ALA ALA B . n B 1 89 CYS 89 139 139 CYS CYS B . n B 1 90 ALA 90 140 140 ALA ALA B . n B 1 91 VAL 91 141 141 VAL VAL B . n B 1 92 SER 92 142 142 SER SER B . n B 1 93 GLY 93 143 143 GLY GLY B . n B 1 94 ASN 94 144 144 ASN ASN B . n B 1 95 PRO 95 145 145 PRO PRO B . n B 1 96 SER 96 146 146 SER SER B . n B 1 97 PHE 97 147 147 PHE PHE B . n B 1 98 PHE 98 148 148 PHE PHE B . n B 1 99 ARG 99 149 149 ARG ARG B . n B 1 100 ASN 100 150 150 ASN ASN B . n B 1 101 MET 101 151 151 MET MET B . n B 1 102 VAL 102 152 152 VAL VAL B . n B 1 103 TRP 103 153 153 TRP TRP B . n B 1 104 LEU 104 154 154 LEU LEU B . n B 1 105 THR 105 155 155 THR THR B . n B 1 106 GLU 106 156 156 GLU GLU B . n B 1 107 LYS 107 157 157 LYS LYS B . n B 1 108 GLY 108 158 158 GLY GLY B . n B 1 109 SER 109 159 159 SER SER B . n B 1 110 ASN 110 160 160 ASN ASN B . n B 1 111 TYR 111 161 161 TYR TYR B . n B 1 112 PRO 112 162 162 PRO PRO B . n B 1 113 VAL 113 163 163 VAL VAL B . n B 1 114 ALA 114 164 164 ALA ALA B . n B 1 115 LYS 115 165 165 LYS LYS B . n B 1 116 GLY 116 166 166 GLY GLY B . n B 1 117 SER 117 167 167 SER SER B . n B 1 118 TYR 118 168 168 TYR TYR B . n B 1 119 ASN 119 169 169 ASN ASN B . n B 1 120 ASN 120 170 170 ASN ASN B . n B 1 121 THR 121 171 171 THR THR B . n B 1 122 SER 122 172 172 SER SER B . n B 1 123 GLY 123 173 173 GLY GLY B . n B 1 124 GLU 124 174 174 GLU GLU B . n B 1 125 GLN 125 175 175 GLN GLN B . n B 1 126 MET 126 176 176 MET MET B . n B 1 127 LEU 127 177 177 LEU LEU B . n B 1 128 ILE 128 178 178 ILE ILE B . n B 1 129 ILE 129 179 179 ILE ILE B . n B 1 130 TRP 130 180 180 TRP TRP B . n B 1 131 GLY 131 181 181 GLY GLY B . n B 1 132 VAL 132 182 182 VAL VAL B . n B 1 133 HIS 133 183 183 HIS HIS B . n B 1 134 HIS 134 184 184 HIS HIS B . n B 1 135 PRO 135 185 185 PRO PRO B . n B 1 136 ASN 136 186 186 ASN ASN B . n B 1 137 ASP 137 187 187 ASP ASP B . n B 1 138 GLU 138 188 188 GLU GLU B . n B 1 139 THR 139 189 189 THR THR B . n B 1 140 GLU 140 190 190 GLU GLU B . n B 1 141 GLN 141 191 191 GLN GLN B . n B 1 142 ARG 142 192 192 ARG ARG B . n B 1 143 THR 143 193 193 THR THR B . n B 1 144 LEU 144 194 194 LEU LEU B . n B 1 145 TYR 145 195 195 TYR TYR B . n B 1 146 GLN 146 196 196 GLN GLN B . n B 1 147 ASN 147 197 197 ASN ASN B . n B 1 148 VAL 148 198 198 VAL VAL B . n B 1 149 GLY 149 199 199 GLY GLY B . n B 1 150 THR 150 200 200 THR THR B . n B 1 151 TYR 151 201 201 TYR TYR B . n B 1 152 VAL 152 202 202 VAL VAL B . n B 1 153 SER 153 203 203 SER SER B . n B 1 154 VAL 154 204 204 VAL VAL B . n B 1 155 GLY 155 205 205 GLY GLY B . n B 1 156 THR 156 206 206 THR THR B . n B 1 157 SER 157 207 207 SER SER B . n B 1 158 THR 158 208 208 THR THR B . n B 1 159 LEU 159 209 209 LEU LEU B . n B 1 160 ASN 160 210 210 ASN ASN B . n B 1 161 LYS 161 211 211 LYS LYS B . n B 1 162 ARG 162 212 212 ARG ARG B . n B 1 163 SER 163 213 213 SER SER B . n B 1 164 THR 164 214 214 THR THR B . n B 1 165 PRO 165 215 215 PRO PRO B . n B 1 166 GLU 166 216 216 GLU GLU B . n B 1 167 ILE 167 217 217 ILE ILE B . n B 1 168 ALA 168 218 218 ALA ALA B . n B 1 169 THR 169 219 219 THR THR B . n B 1 170 ARG 170 220 220 ARG ARG B . n B 1 171 PRO 171 221 221 PRO PRO B . n B 1 172 LYS 172 222 222 LYS LYS B . n B 1 173 VAL 173 223 223 VAL VAL B . n B 1 174 ASN 174 224 224 ASN ASN B . n B 1 175 GLY 175 225 225 GLY GLY B . n B 1 176 GLN 176 226 226 GLN GLN B . n B 1 177 GLY 177 227 227 GLY GLY B . n B 1 178 GLY 178 228 228 GLY GLY B . n B 1 179 ARG 179 229 229 ARG ARG B . n B 1 180 MET 180 230 230 MET MET B . n B 1 181 GLU 181 231 231 GLU GLU B . n B 1 182 PHE 182 232 232 PHE PHE B . n B 1 183 SER 183 233 233 SER SER B . n B 1 184 TRP 184 234 234 TRP TRP B . n B 1 185 THR 185 235 235 THR THR B . n B 1 186 LEU 186 236 236 LEU LEU B . n B 1 187 LEU 187 237 237 LEU LEU B . n B 1 188 ASP 188 238 238 ASP ASP B . n B 1 189 MET 189 239 239 MET MET B . n B 1 190 TRP 190 240 240 TRP TRP B . n B 1 191 ASP 191 241 241 ASP ASP B . n B 1 192 THR 192 242 242 THR THR B . n B 1 193 ILE 193 243 243 ILE ILE B . n B 1 194 ASN 194 244 244 ASN ASN B . n B 1 195 PHE 195 245 245 PHE PHE B . n B 1 196 GLU 196 246 246 GLU GLU B . n B 1 197 SER 197 247 247 SER SER B . n B 1 198 THR 198 248 248 THR THR B . n B 1 199 GLY 199 249 249 GLY GLY B . n B 1 200 ASN 200 250 250 ASN ASN B . n B 1 201 LEU 201 251 251 LEU LEU B . n B 1 202 ILE 202 252 252 ILE ILE B . n B 1 203 ALA 203 253 253 ALA ALA B . n B 1 204 PRO 204 254 254 PRO PRO B . n B 1 205 GLU 205 255 255 GLU GLU B . n B 1 206 TYR 206 256 256 TYR TYR B . n B 1 207 GLY 207 257 257 GLY GLY B . n B 1 208 PHE 208 258 258 PHE PHE B . n B 1 209 LYS 209 259 259 LYS LYS B . n B 1 210 ILE 210 260 260 ILE ILE B . n B 1 211 SER 211 261 261 SER SER B . n B 1 212 LYS 212 262 262 LYS LYS B . n B 1 213 ARG 213 263 263 ARG ARG B . n B 1 214 GLY 214 263 263 GLY GLY B A n B 1 215 SER 215 264 264 SER SER B . n B 1 216 SER 216 265 265 SER SER B . n B 1 217 GLY 217 266 266 GLY GLY B . n B 1 218 ILE 218 267 267 ILE ILE B . n B 1 219 MET 219 268 268 MET MET B . 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 C 2 NAG 1 5467 5467 NAG NAG A . D 3 EPE 1 3380 3380 EPE EPE A . E 2 NAG 1 5467 5467 NAG NAG B . F 3 EPE 1 3380 3380 EPE EPE B . G 4 HOH 1 1 1 HOH HOH A . G 4 HOH 2 6 6 HOH HOH A . G 4 HOH 3 8 8 HOH HOH A . G 4 HOH 4 9 9 HOH HOH A . G 4 HOH 5 10 10 HOH HOH A . G 4 HOH 6 11 11 HOH HOH A . G 4 HOH 7 14 14 HOH HOH A . G 4 HOH 8 15 15 HOH HOH A . G 4 HOH 9 16 16 HOH HOH A . G 4 HOH 10 18 18 HOH HOH A . G 4 HOH 11 19 19 HOH HOH A . G 4 HOH 12 20 20 HOH HOH A . G 4 HOH 13 21 21 HOH HOH A . G 4 HOH 14 23 23 HOH HOH A . G 4 HOH 15 25 25 HOH HOH A . G 4 HOH 16 28 28 HOH HOH A . G 4 HOH 17 29 29 HOH HOH A . G 4 HOH 18 30 30 HOH HOH A . G 4 HOH 19 31 31 HOH HOH A . G 4 HOH 20 32 32 HOH HOH A . G 4 HOH 21 34 34 HOH HOH A . G 4 HOH 22 36 36 HOH HOH A . G 4 HOH 23 44 44 HOH HOH A . G 4 HOH 24 45 45 HOH HOH A . G 4 HOH 25 47 47 HOH HOH A . G 4 HOH 26 48 48 HOH HOH A . G 4 HOH 27 49 49 HOH HOH A . G 4 HOH 28 50 50 HOH HOH A . G 4 HOH 29 53 53 HOH HOH A . G 4 HOH 30 54 54 HOH HOH A . G 4 HOH 31 124 124 HOH HOH A . G 4 HOH 32 269 56 HOH HOH A . G 4 HOH 33 270 57 HOH HOH A . G 4 HOH 34 271 58 HOH HOH A . G 4 HOH 35 272 272 HOH HOH A . G 4 HOH 36 273 59 HOH HOH A . G 4 HOH 37 274 274 HOH HOH A . G 4 HOH 38 275 275 HOH HOH A . G 4 HOH 39 276 60 HOH HOH A . G 4 HOH 40 277 277 HOH HOH A . G 4 HOH 41 278 278 HOH HOH A . G 4 HOH 42 279 279 HOH HOH A . G 4 HOH 43 280 280 HOH HOH A . G 4 HOH 44 281 66 HOH HOH A . G 4 HOH 45 282 282 HOH HOH A . G 4 HOH 46 283 67 HOH HOH A . G 4 HOH 47 284 284 HOH HOH A . G 4 HOH 48 285 74 HOH HOH A . G 4 HOH 49 286 76 HOH HOH A . G 4 HOH 50 287 287 HOH HOH A . G 4 HOH 51 288 288 HOH HOH A . G 4 HOH 52 289 289 HOH HOH A . G 4 HOH 53 290 78 HOH HOH A . G 4 HOH 54 291 79 HOH HOH A . G 4 HOH 55 292 292 HOH HOH A . G 4 HOH 56 293 81 HOH HOH A . G 4 HOH 57 294 83 HOH HOH A . G 4 HOH 58 295 85 HOH HOH A . G 4 HOH 59 296 296 HOH HOH A . G 4 HOH 60 297 297 HOH HOH A . G 4 HOH 61 298 87 HOH HOH A . G 4 HOH 62 299 88 HOH HOH A . G 4 HOH 63 300 300 HOH HOH A . G 4 HOH 64 301 93 HOH HOH A . G 4 HOH 65 302 95 HOH HOH A . G 4 HOH 66 303 303 HOH HOH A . G 4 HOH 67 304 304 HOH HOH A . G 4 HOH 68 305 96 HOH HOH A . G 4 HOH 69 306 97 HOH HOH A . G 4 HOH 70 307 307 HOH HOH A . G 4 HOH 71 308 98 HOH HOH A . G 4 HOH 72 309 100 HOH HOH A . G 4 HOH 73 310 102 HOH HOH A . G 4 HOH 74 311 103 HOH HOH A . G 4 HOH 75 312 104 HOH HOH A . G 4 HOH 76 313 109 HOH HOH A . G 4 HOH 77 314 110 HOH HOH A . G 4 HOH 78 315 115 HOH HOH A . G 4 HOH 79 316 316 HOH HOH A . G 4 HOH 80 317 317 HOH HOH A . G 4 HOH 81 318 318 HOH HOH A . G 4 HOH 82 319 117 HOH HOH A . G 4 HOH 83 320 120 HOH HOH A . G 4 HOH 84 321 321 HOH HOH A . G 4 HOH 85 322 121 HOH HOH A . G 4 HOH 86 323 323 HOH HOH A . G 4 HOH 87 324 128 HOH HOH A . G 4 HOH 88 325 325 HOH HOH A . G 4 HOH 89 326 326 HOH HOH A . G 4 HOH 90 327 327 HOH HOH A . G 4 HOH 91 328 129 HOH HOH A . G 4 HOH 92 329 329 HOH HOH A . G 4 HOH 93 330 132 HOH HOH A . G 4 HOH 94 331 331 HOH HOH A . G 4 HOH 95 332 332 HOH HOH A . G 4 HOH 96 333 133 HOH HOH A . G 4 HOH 97 334 334 HOH HOH A . G 4 HOH 98 335 335 HOH HOH A . G 4 HOH 99 336 336 HOH HOH A . G 4 HOH 100 337 337 HOH HOH A . G 4 HOH 101 338 135 HOH HOH A . G 4 HOH 102 339 137 HOH HOH A . G 4 HOH 103 340 141 HOH HOH A . G 4 HOH 104 341 341 HOH HOH A . G 4 HOH 105 342 142 HOH HOH A . G 4 HOH 106 343 143 HOH HOH A . G 4 HOH 107 344 344 HOH HOH A . G 4 HOH 108 345 144 HOH HOH A . G 4 HOH 109 346 145 HOH HOH A . G 4 HOH 110 347 146 HOH HOH A . G 4 HOH 111 348 348 HOH HOH A . G 4 HOH 112 349 349 HOH HOH A . G 4 HOH 113 350 350 HOH HOH A . G 4 HOH 114 351 351 HOH HOH A . G 4 HOH 115 352 147 HOH HOH A . G 4 HOH 116 353 148 HOH HOH A . G 4 HOH 117 354 354 HOH HOH A . G 4 HOH 118 355 149 HOH HOH A . G 4 HOH 119 356 356 HOH HOH A . G 4 HOH 120 357 155 HOH HOH A . G 4 HOH 121 358 358 HOH HOH A . G 4 HOH 122 359 161 HOH HOH A . G 4 HOH 123 360 163 HOH HOH A . G 4 HOH 124 361 164 HOH HOH A . G 4 HOH 125 362 167 HOH HOH A . G 4 HOH 126 363 169 HOH HOH A . G 4 HOH 127 364 171 HOH HOH A . G 4 HOH 128 365 172 HOH HOH A . G 4 HOH 129 366 366 HOH HOH A . G 4 HOH 130 367 367 HOH HOH A . G 4 HOH 131 368 173 HOH HOH A . G 4 HOH 132 369 180 HOH HOH A . G 4 HOH 133 370 370 HOH HOH A . G 4 HOH 134 371 371 HOH HOH A . G 4 HOH 135 372 372 HOH HOH A . G 4 HOH 136 373 182 HOH HOH A . G 4 HOH 137 374 186 HOH HOH A . G 4 HOH 138 375 375 HOH HOH A . G 4 HOH 139 376 376 HOH HOH A . G 4 HOH 140 377 377 HOH HOH A . G 4 HOH 141 378 378 HOH HOH A . G 4 HOH 142 379 187 HOH HOH A . G 4 HOH 143 380 380 HOH HOH A . G 4 HOH 144 381 189 HOH HOH A . G 4 HOH 145 382 382 HOH HOH A . G 4 HOH 146 383 383 HOH HOH A . G 4 HOH 147 384 384 HOH HOH A . G 4 HOH 148 385 192 HOH HOH A . G 4 HOH 149 386 386 HOH HOH A . G 4 HOH 150 387 387 HOH HOH A . G 4 HOH 151 388 388 HOH HOH A . G 4 HOH 152 389 193 HOH HOH A . G 4 HOH 153 390 390 HOH HOH A . G 4 HOH 154 391 194 HOH HOH A . G 4 HOH 155 392 195 HOH HOH A . G 4 HOH 156 393 393 HOH HOH A . G 4 HOH 157 394 394 HOH HOH A . G 4 HOH 158 395 197 HOH HOH A . G 4 HOH 159 396 198 HOH HOH A . G 4 HOH 160 397 203 HOH HOH A . G 4 HOH 161 398 210 HOH HOH A . G 4 HOH 162 399 212 HOH HOH A . G 4 HOH 163 400 400 HOH HOH A . G 4 HOH 164 401 215 HOH HOH A . G 4 HOH 165 402 402 HOH HOH A . G 4 HOH 166 403 403 HOH HOH A . G 4 HOH 167 404 216 HOH HOH A . G 4 HOH 168 405 405 HOH HOH A . G 4 HOH 169 406 217 HOH HOH A . G 4 HOH 170 407 219 HOH HOH A . G 4 HOH 171 408 220 HOH HOH A . G 4 HOH 172 409 223 HOH HOH A . G 4 HOH 173 410 232 HOH HOH A . G 4 HOH 174 411 411 HOH HOH A . G 4 HOH 175 412 234 HOH HOH A . G 4 HOH 176 413 235 HOH HOH A . G 4 HOH 177 414 237 HOH HOH A . G 4 HOH 178 415 241 HOH HOH A . G 4 HOH 179 416 245 HOH HOH A . G 4 HOH 180 417 417 HOH HOH A . G 4 HOH 181 418 418 HOH HOH A . G 4 HOH 182 419 246 HOH HOH A . G 4 HOH 183 420 247 HOH HOH A . G 4 HOH 184 421 421 HOH HOH A . G 4 HOH 185 422 250 HOH HOH A . G 4 HOH 186 423 423 HOH HOH A . G 4 HOH 187 424 251 HOH HOH A . G 4 HOH 188 425 252 HOH HOH A . G 4 HOH 189 426 254 HOH HOH A . G 4 HOH 190 427 427 HOH HOH A . G 4 HOH 191 428 255 HOH HOH A . G 4 HOH 192 429 257 HOH HOH A . G 4 HOH 193 430 259 HOH HOH A . G 4 HOH 194 431 431 HOH HOH A . G 4 HOH 195 432 261 HOH HOH A . G 4 HOH 196 434 434 HOH HOH A . G 4 HOH 197 435 435 HOH HOH A . G 4 HOH 198 437 437 HOH HOH A . G 4 HOH 199 440 440 HOH HOH A . G 4 HOH 200 446 446 HOH HOH A . G 4 HOH 201 448 448 HOH HOH A . G 4 HOH 202 449 449 HOH HOH A . G 4 HOH 203 453 453 HOH HOH A . G 4 HOH 204 457 457 HOH HOH A . G 4 HOH 205 458 458 HOH HOH A . G 4 HOH 206 459 459 HOH HOH A . G 4 HOH 207 464 464 HOH HOH A . G 4 HOH 208 465 465 HOH HOH A . G 4 HOH 209 473 473 HOH HOH A . G 4 HOH 210 474 474 HOH HOH A . G 4 HOH 211 475 475 HOH HOH A . G 4 HOH 212 477 477 HOH HOH A . G 4 HOH 213 481 481 HOH HOH A . G 4 HOH 214 487 487 HOH HOH A . G 4 HOH 215 496 496 HOH HOH A . G 4 HOH 216 498 498 HOH HOH A . G 4 HOH 217 502 502 HOH HOH A . G 4 HOH 218 503 503 HOH HOH A . G 4 HOH 219 505 505 HOH HOH A . G 4 HOH 220 509 509 HOH HOH A . G 4 HOH 221 513 513 HOH HOH A . G 4 HOH 222 519 519 HOH HOH A . G 4 HOH 223 524 524 HOH HOH A . G 4 HOH 224 525 525 HOH HOH A . G 4 HOH 225 527 527 HOH HOH A . G 4 HOH 226 531 531 HOH HOH A . G 4 HOH 227 538 538 HOH HOH A . G 4 HOH 228 540 540 HOH HOH A . G 4 HOH 229 541 541 HOH HOH A . G 4 HOH 230 542 542 HOH HOH A . G 4 HOH 231 543 543 HOH HOH A . G 4 HOH 232 544 544 HOH HOH A . G 4 HOH 233 548 548 HOH HOH A . G 4 HOH 234 549 549 HOH HOH A . G 4 HOH 235 551 551 HOH HOH A . G 4 HOH 236 554 554 HOH HOH A . G 4 HOH 237 555 555 HOH HOH A . G 4 HOH 238 556 556 HOH HOH A . G 4 HOH 239 558 558 HOH HOH A . G 4 HOH 240 559 559 HOH HOH A . G 4 HOH 241 560 560 HOH HOH A . G 4 HOH 242 561 561 HOH HOH A . G 4 HOH 243 562 562 HOH HOH A . G 4 HOH 244 566 566 HOH HOH A . G 4 HOH 245 568 568 HOH HOH A . G 4 HOH 246 575 575 HOH HOH A . G 4 HOH 247 578 578 HOH HOH A . G 4 HOH 248 579 579 HOH HOH A . G 4 HOH 249 580 580 HOH HOH A . G 4 HOH 250 581 581 HOH HOH A . G 4 HOH 251 583 583 HOH HOH A . G 4 HOH 252 585 585 HOH HOH A . G 4 HOH 253 589 589 HOH HOH A . G 4 HOH 254 595 595 HOH HOH A . G 4 HOH 255 599 599 HOH HOH A . G 4 HOH 256 601 601 HOH HOH A . G 4 HOH 257 602 602 HOH HOH A . G 4 HOH 258 603 603 HOH HOH A . G 4 HOH 259 609 609 HOH HOH A . G 4 HOH 260 610 610 HOH HOH A . G 4 HOH 261 614 614 HOH HOH A . G 4 HOH 262 619 619 HOH HOH A . G 4 HOH 263 625 625 HOH HOH A . G 4 HOH 264 628 628 HOH HOH A . G 4 HOH 265 629 629 HOH HOH A . G 4 HOH 266 638 638 HOH HOH A . G 4 HOH 267 639 639 HOH HOH A . G 4 HOH 268 640 640 HOH HOH A . G 4 HOH 269 641 641 HOH HOH A . G 4 HOH 270 642 642 HOH HOH A . G 4 HOH 271 643 643 HOH HOH A . G 4 HOH 272 645 645 HOH HOH A . G 4 HOH 273 648 648 HOH HOH A . G 4 HOH 274 649 649 HOH HOH A . G 4 HOH 275 653 653 HOH HOH A . G 4 HOH 276 661 661 HOH HOH A . G 4 HOH 277 662 662 HOH HOH A . G 4 HOH 278 666 666 HOH HOH A . G 4 HOH 279 668 668 HOH HOH A . G 4 HOH 280 669 669 HOH HOH A . G 4 HOH 281 680 680 HOH HOH A . G 4 HOH 282 681 681 HOH HOH A . G 4 HOH 283 686 686 HOH HOH A . G 4 HOH 284 687 687 HOH HOH A . G 4 HOH 285 689 689 HOH HOH A . G 4 HOH 286 690 690 HOH HOH A . G 4 HOH 287 692 692 HOH HOH A . G 4 HOH 288 693 693 HOH HOH A . G 4 HOH 289 694 694 HOH HOH A . G 4 HOH 290 695 695 HOH HOH A . G 4 HOH 291 699 699 HOH HOH A . G 4 HOH 292 700 700 HOH HOH A . G 4 HOH 293 705 705 HOH HOH A . G 4 HOH 294 706 706 HOH HOH A . G 4 HOH 295 714 714 HOH HOH A . G 4 HOH 296 715 715 HOH HOH A . G 4 HOH 297 718 718 HOH HOH A . G 4 HOH 298 723 723 HOH HOH A . G 4 HOH 299 725 725 HOH HOH A . G 4 HOH 300 728 728 HOH HOH A . G 4 HOH 301 729 729 HOH HOH A . G 4 HOH 302 736 736 HOH HOH A . G 4 HOH 303 738 738 HOH HOH A . G 4 HOH 304 743 743 HOH HOH A . G 4 HOH 305 744 744 HOH HOH A . H 4 HOH 1 2 2 HOH HOH B . H 4 HOH 2 3 3 HOH HOH B . H 4 HOH 3 4 4 HOH HOH B . H 4 HOH 4 5 5 HOH HOH B . H 4 HOH 5 7 7 HOH HOH B . H 4 HOH 6 12 12 HOH HOH B . H 4 HOH 7 13 13 HOH HOH B . H 4 HOH 8 17 17 HOH HOH B . H 4 HOH 9 22 22 HOH HOH B . H 4 HOH 10 24 24 HOH HOH B . H 4 HOH 11 26 26 HOH HOH B . H 4 HOH 12 27 27 HOH HOH B . H 4 HOH 13 33 33 HOH HOH B . H 4 HOH 14 35 35 HOH HOH B . H 4 HOH 15 37 37 HOH HOH B . H 4 HOH 16 38 38 HOH HOH B . H 4 HOH 17 39 39 HOH HOH B . H 4 HOH 18 40 40 HOH HOH B . H 4 HOH 19 41 41 HOH HOH B . H 4 HOH 20 42 42 HOH HOH B . H 4 HOH 21 43 43 HOH HOH B . H 4 HOH 22 46 46 HOH HOH B . H 4 HOH 23 51 51 HOH HOH B . H 4 HOH 24 52 52 HOH HOH B . H 4 HOH 25 269 55 HOH HOH B . H 4 HOH 26 270 270 HOH HOH B . H 4 HOH 27 271 271 HOH HOH B . H 4 HOH 28 272 61 HOH HOH B . H 4 HOH 29 273 273 HOH HOH B . H 4 HOH 30 274 62 HOH HOH B . H 4 HOH 31 275 63 HOH HOH B . H 4 HOH 32 276 276 HOH HOH B . H 4 HOH 33 277 64 HOH HOH B . H 4 HOH 34 278 65 HOH HOH B . H 4 HOH 35 279 68 HOH HOH B . H 4 HOH 36 280 69 HOH HOH B . H 4 HOH 37 281 281 HOH HOH B . H 4 HOH 38 282 70 HOH HOH B . H 4 HOH 39 283 71 HOH HOH B . H 4 HOH 40 284 72 HOH HOH B . H 4 HOH 41 285 73 HOH HOH B . H 4 HOH 42 286 75 HOH HOH B . H 4 HOH 43 287 77 HOH HOH B . H 4 HOH 44 288 80 HOH HOH B . H 4 HOH 45 289 82 HOH HOH B . H 4 HOH 46 290 290 HOH HOH B . H 4 HOH 47 291 291 HOH HOH B . H 4 HOH 48 292 84 HOH HOH B . H 4 HOH 49 293 293 HOH HOH B . H 4 HOH 50 294 294 HOH HOH B . H 4 HOH 51 295 295 HOH HOH B . H 4 HOH 52 296 86 HOH HOH B . H 4 HOH 53 297 89 HOH HOH B . H 4 HOH 54 298 298 HOH HOH B . H 4 HOH 55 299 299 HOH HOH B . H 4 HOH 56 300 90 HOH HOH B . H 4 HOH 57 301 301 HOH HOH B . H 4 HOH 58 302 302 HOH HOH B . H 4 HOH 59 303 91 HOH HOH B . H 4 HOH 60 304 94 HOH HOH B . H 4 HOH 61 305 305 HOH HOH B . H 4 HOH 62 306 306 HOH HOH B . H 4 HOH 63 307 101 HOH HOH B . H 4 HOH 64 308 308 HOH HOH B . H 4 HOH 65 309 309 HOH HOH B . H 4 HOH 66 310 105 HOH HOH B . H 4 HOH 67 311 311 HOH HOH B . H 4 HOH 68 312 312 HOH HOH B . H 4 HOH 69 313 313 HOH HOH B . H 4 HOH 70 314 314 HOH HOH B . H 4 HOH 71 315 106 HOH HOH B . H 4 HOH 72 316 107 HOH HOH B . H 4 HOH 73 317 108 HOH HOH B . H 4 HOH 74 318 112 HOH HOH B . H 4 HOH 75 319 319 HOH HOH B . H 4 HOH 76 320 320 HOH HOH B . H 4 HOH 77 321 113 HOH HOH B . H 4 HOH 78 322 322 HOH HOH B . H 4 HOH 79 323 114 HOH HOH B . H 4 HOH 80 324 116 HOH HOH B . H 4 HOH 81 325 118 HOH HOH B . H 4 HOH 82 326 119 HOH HOH B . H 4 HOH 83 327 122 HOH HOH B . H 4 HOH 84 328 328 HOH HOH B . H 4 HOH 85 329 123 HOH HOH B . H 4 HOH 86 330 330 HOH HOH B . H 4 HOH 87 331 125 HOH HOH B . H 4 HOH 88 332 126 HOH HOH B . H 4 HOH 89 333 333 HOH HOH B . H 4 HOH 90 334 127 HOH HOH B . H 4 HOH 91 335 130 HOH HOH B . H 4 HOH 92 336 131 HOH HOH B . H 4 HOH 93 337 134 HOH HOH B . H 4 HOH 94 338 136 HOH HOH B . H 4 HOH 95 339 339 HOH HOH B . H 4 HOH 96 340 340 HOH HOH B . H 4 HOH 97 341 138 HOH HOH B . H 4 HOH 98 342 342 HOH HOH B . H 4 HOH 99 343 139 HOH HOH B . H 4 HOH 100 344 140 HOH HOH B . H 4 HOH 101 345 345 HOH HOH B . H 4 HOH 102 346 346 HOH HOH B . H 4 HOH 103 347 347 HOH HOH B . H 4 HOH 104 348 150 HOH HOH B . H 4 HOH 105 349 151 HOH HOH B . H 4 HOH 106 350 152 HOH HOH B . H 4 HOH 107 351 153 HOH HOH B . H 4 HOH 108 352 156 HOH HOH B . H 4 HOH 109 353 353 HOH HOH B . H 4 HOH 110 354 157 HOH HOH B . H 4 HOH 111 355 355 HOH HOH B . H 4 HOH 112 356 158 HOH HOH B . H 4 HOH 113 357 357 HOH HOH B . H 4 HOH 114 358 159 HOH HOH B . H 4 HOH 115 359 359 HOH HOH B . H 4 HOH 116 360 160 HOH HOH B . H 4 HOH 117 361 162 HOH HOH B . H 4 HOH 118 362 362 HOH HOH B . H 4 HOH 119 363 363 HOH HOH B . H 4 HOH 120 364 364 HOH HOH B . H 4 HOH 121 365 365 HOH HOH B . H 4 HOH 122 366 165 HOH HOH B . H 4 HOH 123 367 166 HOH HOH B . H 4 HOH 124 368 368 HOH HOH B . H 4 HOH 125 369 369 HOH HOH B . H 4 HOH 126 370 170 HOH HOH B . H 4 HOH 127 371 174 HOH HOH B . H 4 HOH 128 372 175 HOH HOH B . H 4 HOH 129 373 373 HOH HOH B . H 4 HOH 130 374 374 HOH HOH B . H 4 HOH 131 375 177 HOH HOH B . H 4 HOH 132 376 178 HOH HOH B . H 4 HOH 133 377 179 HOH HOH B . H 4 HOH 134 378 181 HOH HOH B . H 4 HOH 135 379 379 HOH HOH B . H 4 HOH 136 380 183 HOH HOH B . H 4 HOH 137 381 381 HOH HOH B . H 4 HOH 138 382 184 HOH HOH B . H 4 HOH 139 383 185 HOH HOH B . H 4 HOH 140 384 188 HOH HOH B . H 4 HOH 141 385 385 HOH HOH B . H 4 HOH 142 386 190 HOH HOH B . H 4 HOH 143 387 191 HOH HOH B . H 4 HOH 144 388 196 HOH HOH B . H 4 HOH 145 389 389 HOH HOH B . H 4 HOH 146 390 200 HOH HOH B . H 4 HOH 147 391 391 HOH HOH B . H 4 HOH 148 392 392 HOH HOH B . H 4 HOH 149 393 204 HOH HOH B . H 4 HOH 150 394 205 HOH HOH B . H 4 HOH 151 395 395 HOH HOH B . H 4 HOH 152 396 206 HOH HOH B . H 4 HOH 153 397 207 HOH HOH B . H 4 HOH 154 398 398 HOH HOH B . H 4 HOH 155 399 209 HOH HOH B . H 4 HOH 156 400 211 HOH HOH B . H 4 HOH 157 401 401 HOH HOH B . H 4 HOH 158 402 213 HOH HOH B . H 4 HOH 159 403 214 HOH HOH B . H 4 HOH 160 404 218 HOH HOH B . H 4 HOH 161 405 222 HOH HOH B . H 4 HOH 162 406 406 HOH HOH B . H 4 HOH 163 407 407 HOH HOH B . H 4 HOH 164 408 408 HOH HOH B . H 4 HOH 165 409 409 HOH HOH B . H 4 HOH 166 410 410 HOH HOH B . H 4 HOH 167 411 225 HOH HOH B . H 4 HOH 168 412 227 HOH HOH B . H 4 HOH 169 413 229 HOH HOH B . H 4 HOH 170 414 414 HOH HOH B . H 4 HOH 171 415 415 HOH HOH B . H 4 HOH 172 416 230 HOH HOH B . H 4 HOH 173 417 231 HOH HOH B . H 4 HOH 174 418 236 HOH HOH B . H 4 HOH 175 419 419 HOH HOH B . H 4 HOH 176 420 420 HOH HOH B . H 4 HOH 177 421 238 HOH HOH B . H 4 HOH 178 422 239 HOH HOH B . H 4 HOH 179 423 240 HOH HOH B . H 4 HOH 180 424 242 HOH HOH B . H 4 HOH 181 425 244 HOH HOH B . H 4 HOH 182 426 426 HOH HOH B . H 4 HOH 183 427 253 HOH HOH B . H 4 HOH 184 428 428 HOH HOH B . H 4 HOH 185 429 256 HOH HOH B . H 4 HOH 186 430 430 HOH HOH B . H 4 HOH 187 431 258 HOH HOH B . H 4 HOH 188 432 432 HOH HOH B . H 4 HOH 189 433 433 HOH HOH B . H 4 HOH 190 434 260 HOH HOH B . H 4 HOH 191 435 263 HOH HOH B . H 4 HOH 192 436 436 HOH HOH B . H 4 HOH 193 437 264 HOH HOH B . H 4 HOH 194 438 438 HOH HOH B . H 4 HOH 195 439 439 HOH HOH B . H 4 HOH 196 440 265 HOH HOH B . H 4 HOH 197 441 266 HOH HOH B . H 4 HOH 198 442 442 HOH HOH B . H 4 HOH 199 443 268 HOH HOH B . H 4 HOH 200 444 444 HOH HOH B . H 4 HOH 201 445 445 HOH HOH B . H 4 HOH 202 450 450 HOH HOH B . H 4 HOH 203 451 451 HOH HOH B . H 4 HOH 204 452 452 HOH HOH B . H 4 HOH 205 454 454 HOH HOH B . H 4 HOH 206 455 455 HOH HOH B . H 4 HOH 207 456 456 HOH HOH B . H 4 HOH 208 461 461 HOH HOH B . H 4 HOH 209 462 462 HOH HOH B . H 4 HOH 210 463 463 HOH HOH B . H 4 HOH 211 468 468 HOH HOH B . H 4 HOH 212 471 471 HOH HOH B . H 4 HOH 213 472 472 HOH HOH B . H 4 HOH 214 478 478 HOH HOH B . H 4 HOH 215 479 479 HOH HOH B . H 4 HOH 216 482 482 HOH HOH B . H 4 HOH 217 483 483 HOH HOH B . H 4 HOH 218 484 484 HOH HOH B . H 4 HOH 219 486 486 HOH HOH B . H 4 HOH 220 489 489 HOH HOH B . H 4 HOH 221 491 491 HOH HOH B . H 4 HOH 222 494 494 HOH HOH B . H 4 HOH 223 495 495 HOH HOH B . H 4 HOH 224 497 497 HOH HOH B . H 4 HOH 225 500 500 HOH HOH B . H 4 HOH 226 501 501 HOH HOH B . H 4 HOH 227 504 504 HOH HOH B . H 4 HOH 228 507 507 HOH HOH B . H 4 HOH 229 508 508 HOH HOH B . H 4 HOH 230 510 510 HOH HOH B . H 4 HOH 231 511 511 HOH HOH B . H 4 HOH 232 517 517 HOH HOH B . H 4 HOH 233 520 520 HOH HOH B . H 4 HOH 234 522 522 HOH HOH B . H 4 HOH 235 526 526 HOH HOH B . H 4 HOH 236 528 528 HOH HOH B . H 4 HOH 237 530 530 HOH HOH B . H 4 HOH 238 532 532 HOH HOH B . H 4 HOH 239 533 533 HOH HOH B . H 4 HOH 240 534 534 HOH HOH B . H 4 HOH 241 535 535 HOH HOH B . H 4 HOH 242 536 536 HOH HOH B . H 4 HOH 243 539 539 HOH HOH B . H 4 HOH 244 545 545 HOH HOH B . H 4 HOH 245 546 546 HOH HOH B . H 4 HOH 246 547 547 HOH HOH B . H 4 HOH 247 552 552 HOH HOH B . H 4 HOH 248 557 557 HOH HOH B . H 4 HOH 249 565 565 HOH HOH B . H 4 HOH 250 567 567 HOH HOH B . H 4 HOH 251 569 569 HOH HOH B . H 4 HOH 252 570 570 HOH HOH B . H 4 HOH 253 573 573 HOH HOH B . H 4 HOH 254 574 574 HOH HOH B . H 4 HOH 255 576 576 HOH HOH B . H 4 HOH 256 577 577 HOH HOH B . H 4 HOH 257 582 582 HOH HOH B . H 4 HOH 258 584 584 HOH HOH B . H 4 HOH 259 588 588 HOH HOH B . H 4 HOH 260 590 590 HOH HOH B . H 4 HOH 261 592 592 HOH HOH B . H 4 HOH 262 593 593 HOH HOH B . H 4 HOH 263 597 597 HOH HOH B . H 4 HOH 264 598 598 HOH HOH B . H 4 HOH 265 604 604 HOH HOH B . H 4 HOH 266 605 605 HOH HOH B . H 4 HOH 267 606 606 HOH HOH B . H 4 HOH 268 607 607 HOH HOH B . H 4 HOH 269 611 611 HOH HOH B . H 4 HOH 270 612 612 HOH HOH B . H 4 HOH 271 613 613 HOH HOH B . H 4 HOH 272 618 618 HOH HOH B . H 4 HOH 273 621 621 HOH HOH B . H 4 HOH 274 626 626 HOH HOH B . H 4 HOH 275 627 627 HOH HOH B . H 4 HOH 276 632 632 HOH HOH B . H 4 HOH 277 633 633 HOH HOH B . H 4 HOH 278 634 634 HOH HOH B . H 4 HOH 279 635 635 HOH HOH B . H 4 HOH 280 637 637 HOH HOH B . H 4 HOH 281 644 644 HOH HOH B . H 4 HOH 282 646 646 HOH HOH B . H 4 HOH 283 650 650 HOH HOH B . H 4 HOH 284 651 651 HOH HOH B . H 4 HOH 285 652 652 HOH HOH B . H 4 HOH 286 656 656 HOH HOH B . H 4 HOH 287 658 658 HOH HOH B . H 4 HOH 288 659 659 HOH HOH B . H 4 HOH 289 660 660 HOH HOH B . H 4 HOH 290 664 664 HOH HOH B . H 4 HOH 291 665 665 HOH HOH B . H 4 HOH 292 672 672 HOH HOH B . H 4 HOH 293 685 685 HOH HOH B . H 4 HOH 294 691 691 HOH HOH B . H 4 HOH 295 696 696 HOH HOH B . H 4 HOH 296 698 698 HOH HOH B . H 4 HOH 297 701 701 HOH HOH B . H 4 HOH 298 702 702 HOH HOH B . H 4 HOH 299 707 707 HOH HOH B . H 4 HOH 300 709 709 HOH HOH B . H 4 HOH 301 719 719 HOH HOH B . H 4 HOH 302 726 726 HOH HOH B . H 4 HOH 303 730 730 HOH HOH B . H 4 HOH 304 739 739 HOH HOH B . H 4 HOH 305 740 740 HOH HOH B . H 4 HOH 306 741 741 HOH HOH B . H 4 HOH 307 742 742 HOH HOH B . H 4 HOH 308 745 745 HOH HOH B . H 4 HOH 309 746 746 HOH HOH B . H 4 HOH 310 747 747 HOH HOH B . H 4 HOH 311 748 748 HOH HOH B . # 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 B ASN 119 B ASN 169 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 119 A ASN 169 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA monomeric 1 2 author_and_software_defined_assembly PISA monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,G 2 1 B,E,F,H # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2011-03-09 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-08 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _diffrn_reflns.diffrn_id 1 _diffrn_reflns.pdbx_d_res_high 1.650 _diffrn_reflns.pdbx_d_res_low 50.000 _diffrn_reflns.pdbx_number_obs 60290 _diffrn_reflns.pdbx_Rmerge_I_obs 0.053 _diffrn_reflns.pdbx_Rsym_value ? _diffrn_reflns.pdbx_chi_squared 1.05 _diffrn_reflns.av_sigmaI_over_netI 11.50 _diffrn_reflns.pdbx_redundancy 1.90 _diffrn_reflns.pdbx_percent_possible_obs 94.80 _diffrn_reflns.number 112600 _diffrn_reflns.pdbx_observed_criterion ? _diffrn_reflns.limit_h_max ? _diffrn_reflns.limit_h_min ? _diffrn_reflns.limit_k_max ? _diffrn_reflns.limit_k_min ? _diffrn_reflns.limit_l_max ? _diffrn_reflns.limit_l_min ? # loop_ _pdbx_diffrn_reflns_shell.diffrn_id _pdbx_diffrn_reflns_shell.d_res_high _pdbx_diffrn_reflns_shell.d_res_low _pdbx_diffrn_reflns_shell.number_obs _pdbx_diffrn_reflns_shell.rejects _pdbx_diffrn_reflns_shell.Rmerge_I_obs _pdbx_diffrn_reflns_shell.Rsym_value _pdbx_diffrn_reflns_shell.chi_squared _pdbx_diffrn_reflns_shell.redundancy _pdbx_diffrn_reflns_shell.percent_possible_obs 1 3.55 50.00 ? ? 0.037 ? 1.041 1.90 96.90 1 2.82 3.55 ? ? 0.050 ? 1.006 1.90 97.70 1 2.46 2.82 ? ? 0.059 ? 1.038 1.90 97.30 1 2.24 2.46 ? ? 0.069 ? 0.976 1.90 96.90 1 2.08 2.24 ? ? 0.083 ? 1.036 1.90 96.50 1 1.96 2.08 ? ? 0.092 ? 1.095 1.90 96.60 1 1.86 1.96 ? ? 0.123 ? 1.051 1.90 96.20 1 1.78 1.86 ? ? 0.157 ? 1.071 1.80 94.70 1 1.71 1.78 ? ? 0.207 ? 1.086 1.80 91.50 1 1.65 1.71 ? ? 0.244 ? 1.092 1.60 83.80 # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 15.3139 -25.3004 -6.0786 -0.0017 -0.0040 0.0120 -0.0086 0.0180 0.0042 1.1522 0.8120 0.4396 -0.4629 -0.1296 0.2848 0.0233 -0.0413 0.0179 0.0112 0.0191 -0.0286 -0.0303 0.0281 0.0170 'X-RAY DIFFRACTION' 2 ? refined 15.4329 -57.0581 19.5309 -0.0124 -0.0174 -0.0005 -0.0106 0.0084 0.0036 1.0982 0.8208 0.3387 0.3288 -0.0557 0.1564 0.0338 -0.0377 0.0039 -0.0127 -0.0156 -0.0293 0.0388 -0.0250 0.0138 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 48 A 266 '{ A|48 - A|266 }' ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 48 B 266 '{ B|48 - B|266 }' ? ? ? ? ? # _pdbx_phasing_MR.entry_id 3QQI _pdbx_phasing_MR.method_rotation ? _pdbx_phasing_MR.method_translation ? _pdbx_phasing_MR.model_details 'Phaser MODE: MR_FRF' _pdbx_phasing_MR.R_factor ? _pdbx_phasing_MR.R_rigid_body ? _pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ? _pdbx_phasing_MR.correlation_coeff_Io_to_Ic ? _pdbx_phasing_MR.d_res_high_rotation 2.500 _pdbx_phasing_MR.d_res_low_rotation 36.720 _pdbx_phasing_MR.d_res_high_translation ? _pdbx_phasing_MR.d_res_low_translation ? _pdbx_phasing_MR.packing ? _pdbx_phasing_MR.reflns_percent_rotation ? _pdbx_phasing_MR.reflns_percent_translation ? _pdbx_phasing_MR.sigma_F_rotation ? _pdbx_phasing_MR.sigma_F_translation ? _pdbx_phasing_MR.sigma_I_rotation ? _pdbx_phasing_MR.sigma_I_translation ? # _phasing.method mr # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 DENZO . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 2 SCALEPACK . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 3 PHASER 1.3.3 'Fri Oct 20 12:51:01 2006' program 'Randy J. Read' cimr-phaser@lists.cam.ac.uk phasing http://www-structmed.cimr.cam.ac.uk/phaser/ ? ? 4 BUSTER-TNT . ? program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement http://www.globalphasing.com/buster/ ? ? 5 PDB_EXTRACT 3.10 'June 10, 2010' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 6 HKL-2000 . ? ? ? ? 'data collection' ? ? ? 7 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 8 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? 9 BUSTER 2.8.0 ? ? ? ? refinement ? ? ? # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 CB _pdbx_validate_close_contact.auth_asym_id_1 B _pdbx_validate_close_contact.auth_comp_id_1 CYS _pdbx_validate_close_contact.auth_seq_id_1 64 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 B _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 726 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.19 # 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 GLN A 196 ? ? 72.22 -51.19 2 1 ASN A 250 ? ? 81.21 9.56 3 1 SER A 265 ? ? 158.75 -74.05 4 1 GLN B 196 ? ? 73.15 -46.98 5 1 SER B 265 ? ? 103.31 95.45 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 4 water HOH #