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*** ***elNémo ID: 2605271016541555293Job options:ID = 2605271016541555293 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:data_3CM3 # _entry.id 3CM3 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.377 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code _database_2.pdbx_database_accession _database_2.pdbx_DOI PDB 3CM3 pdb_00003cm3 10.2210/pdb3cm3/pdb RCSB RCSB046940 ? ? WWPDB D_1000046940 ? ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 2RF6 'Vaccinia Virus Dual-Specificity Phosphatase VH1' unspecified PDB 3CEO 'Vaccinia Virus Dual-Specificity Phosphatase VH1 Bound to Xenon Gas' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3CM3 _pdbx_database_status.recvd_initial_deposition_date 2008-03-20 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.status_code_nmr_data ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Koksal, A.C.' 1 'Cingolani, G.' 2 # _citation.id primary _citation.title 'Dimeric Quaternary Structure of the Prototypical Dual Specificity Phosphatase VH1.' _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 284 _citation.page_first 10129 _citation.page_last 10137 _citation.year 2009 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19211553 _citation.pdbx_database_id_DOI 10.1074/jbc.M808362200 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Koksal, A.C.' 1 ? primary 'Nardozzi, J.D.' 2 ? primary 'Cingolani, G.' 3 ? # _cell.entry_id 3CM3 _cell.length_a 63.816 _cell.length_b 38.690 _cell.length_c 134.987 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3CM3 _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 _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 'Dual specificity protein phosphatase' 20262.455 1 '3.1.3.48, 3.1.3.-' C110S ? ? 2 non-polymer syn 'PHOSPHATE ION' 94.971 1 ? ? ? ? 3 non-polymer syn BETA-MERCAPTOETHANOL 78.133 2 ? ? ? ? 4 water nat water 18.015 300 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Late protein H1' # _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 ;GPEIRMDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHI PLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHSAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVEN PSFKRQIIEKYVIDKN ; _entity_poly.pdbx_seq_one_letter_code_can ;GPEIRMDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHI PLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHSAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVEN PSFKRQIIEKYVIDKN ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 PRO n 1 3 GLU n 1 4 ILE n 1 5 ARG n 1 6 MET n 1 7 ASP n 1 8 LYS n 1 9 LYS n 1 10 SER n 1 11 LEU n 1 12 TYR n 1 13 LYS n 1 14 TYR n 1 15 LEU n 1 16 LEU n 1 17 LEU n 1 18 ARG n 1 19 SER n 1 20 THR n 1 21 GLY n 1 22 ASP n 1 23 MET n 1 24 HIS n 1 25 LYS n 1 26 ALA n 1 27 LYS n 1 28 SER n 1 29 PRO n 1 30 THR n 1 31 ILE n 1 32 MET n 1 33 THR n 1 34 ARG n 1 35 VAL n 1 36 THR n 1 37 ASN n 1 38 ASN n 1 39 VAL n 1 40 TYR n 1 41 LEU n 1 42 GLY n 1 43 ASN n 1 44 TYR n 1 45 LYS n 1 46 ASN n 1 47 ALA n 1 48 MET n 1 49 ASP n 1 50 ALA n 1 51 PRO n 1 52 SER n 1 53 SER n 1 54 GLU n 1 55 VAL n 1 56 LYS n 1 57 PHE n 1 58 LYS n 1 59 TYR n 1 60 VAL n 1 61 LEU n 1 62 ASN n 1 63 LEU n 1 64 THR n 1 65 MET n 1 66 ASP n 1 67 LYS n 1 68 TYR n 1 69 THR n 1 70 LEU n 1 71 PRO n 1 72 ASN n 1 73 SER n 1 74 ASN n 1 75 ILE n 1 76 ASN n 1 77 ILE n 1 78 ILE n 1 79 HIS n 1 80 ILE n 1 81 PRO n 1 82 LEU n 1 83 VAL n 1 84 ASP n 1 85 ASP n 1 86 THR n 1 87 THR n 1 88 THR n 1 89 ASP n 1 90 ILE n 1 91 SER n 1 92 LYS n 1 93 TYR n 1 94 PHE n 1 95 ASP n 1 96 ASP n 1 97 VAL n 1 98 THR n 1 99 ALA n 1 100 PHE n 1 101 LEU n 1 102 SER n 1 103 LYS n 1 104 CYS n 1 105 ASP n 1 106 GLN n 1 107 ARG n 1 108 ASN n 1 109 GLU n 1 110 PRO n 1 111 VAL n 1 112 LEU n 1 113 VAL n 1 114 HIS n 1 115 SER n 1 116 ALA n 1 117 ALA n 1 118 GLY n 1 119 VAL n 1 120 ASN n 1 121 ARG n 1 122 SER n 1 123 GLY n 1 124 ALA n 1 125 MET n 1 126 ILE n 1 127 LEU n 1 128 ALA n 1 129 TYR n 1 130 LEU n 1 131 MET n 1 132 SER n 1 133 LYS n 1 134 ASN n 1 135 LYS n 1 136 GLU n 1 137 SER n 1 138 LEU n 1 139 PRO n 1 140 MET n 1 141 LEU n 1 142 TYR n 1 143 PHE n 1 144 LEU n 1 145 TYR n 1 146 VAL n 1 147 TYR n 1 148 HIS n 1 149 SER n 1 150 MET n 1 151 ARG n 1 152 ASP n 1 153 LEU n 1 154 ARG n 1 155 GLY n 1 156 ALA n 1 157 PHE n 1 158 VAL n 1 159 GLU n 1 160 ASN n 1 161 PRO n 1 162 SER n 1 163 PHE n 1 164 LYS n 1 165 ARG n 1 166 GLN n 1 167 ILE n 1 168 ILE n 1 169 GLU n 1 170 LYS n 1 171 TYR n 1 172 VAL n 1 173 ILE n 1 174 ASP n 1 175 LYS n 1 176 ASN 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 'H1 ORF' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'Western Reserve / WR' _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 'Vaccinia virus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id ? _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 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ? _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 BL21 _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 Plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PET14B _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code DUSP_VACCV _struct_ref.pdbx_db_accession P07239 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;MDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHIPLVDD TTTDISKYFDDVTAFLSKCDQRNEPVLVHCAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVENPSFKR QIIEKYVIDKN ; _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3CM3 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 6 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 176 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P07239 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 171 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1003 _struct_ref_seq.pdbx_auth_seq_align_end 1173 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3CM3 GLY A 1 ? UNP P07239 ? ? 'expression tag' 998 1 1 3CM3 PRO A 2 ? UNP P07239 ? ? 'expression tag' 999 2 1 3CM3 GLU A 3 ? UNP P07239 ? ? 'expression tag' 1000 3 1 3CM3 ILE A 4 ? UNP P07239 ? ? 'expression tag' 1001 4 1 3CM3 ARG A 5 ? UNP P07239 ? ? 'expression tag' 1002 5 1 3CM3 SER A 115 ? UNP P07239 CYS 110 'engineered mutation' 1112 6 # 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 BME non-polymer . BETA-MERCAPTOETHANOL ? 'C2 H6 O S' 78.133 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 3CM3 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.06 _exptl_crystal.density_percent_sol 40.18 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method Batch _exptl_crystal_grow.temp 297 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8 _exptl_crystal_grow.pdbx_details '62% PEG 400, 0.1M Tris pH 8 , Batch, temperature 297K' _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 'ADSC Q-270' _diffrn_detector.pdbx_collection_date 2007-10-20 _diffrn_detector.details 'Horizontal bent Si(111), asymmetrically cut with water cooled Cu Block. Rh-coated Si mirror for vertical focusing.' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si 111' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.918 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'CHESS BEAMLINE F1' _diffrn_source.pdbx_synchrotron_site CHESS _diffrn_source.pdbx_synchrotron_beamline F1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.918 # _reflns.entry_id 3CM3 _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.32 _reflns.d_resolution_low 20 _reflns.number_all 39499 _reflns.number_obs 35905 _reflns.percent_possible_obs 90.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.057 _reflns.pdbx_netI_over_sigmaI 65.6 _reflns.B_iso_Wilson_estimate 19.326 _reflns.pdbx_redundancy 15.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 1.32 _reflns_shell.d_res_low 1.37 _reflns_shell.percent_possible_all 51.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.357 _reflns_shell.meanI_over_sigI_obs 2.5 _reflns_shell.pdbx_redundancy 4.4 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 3868 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 3CM3 _refine.ls_number_reflns_obs 33998 _refine.ls_number_reflns_all 37455 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 14.11 _refine.ls_d_res_high 1.32 _refine.ls_percent_reflns_obs 90.77 _refine.ls_R_factor_obs 0.1717 _refine.ls_R_factor_all 0.1717 _refine.ls_R_factor_R_work 0.17098 _refine.ls_R_factor_R_free 0.18458 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1800 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.971 _refine.correlation_coeff_Fo_to_Fc_free 0.963 _refine.B_iso_mean 26.352 _refine.aniso_B[1][1] 0.00 _refine.aniso_B[2][2] 0.00 _refine.aniso_B[3][3] 0.00 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB Entry 2RF6' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model Anisotropic _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.071 _refine.pdbx_overall_ESU_R_Free 0.057 _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1366 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 13 _refine_hist.number_atoms_solvent 300 _refine_hist.number_atoms_total 1679 _refine_hist.d_res_high 1.32 _refine_hist.d_res_low 14.11 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.008 0.022 ? 1411 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.186 1.976 ? 1916 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.494 5.000 ? 176 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.513 23.934 ? 61 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.109 15.000 ? 254 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.492 15.000 ? 7 'X-RAY DIFFRACTION' ? r_chiral_restr 0.076 0.200 ? 216 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 1049 'X-RAY DIFFRACTION' ? r_nbd_refined 0.257 0.200 ? 724 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.320 0.200 ? 978 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.242 0.200 ? 215 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.207 0.200 ? 62 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.229 0.200 ? 40 'X-RAY DIFFRACTION' ? r_mcbond_it 2.158 1.500 ? 853 'X-RAY DIFFRACTION' ? r_mcangle_it 3.819 2.000 ? 1398 'X-RAY DIFFRACTION' ? r_scbond_it 3.739 3.000 ? 558 'X-RAY DIFFRACTION' ? r_scangle_it 6.064 4.500 ? 515 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.32 _refine_ls_shell.d_res_low 1.357 _refine_ls_shell.number_reflns_R_work 1248 _refine_ls_shell.R_factor_R_work 0.362 _refine_ls_shell.percent_reflns_obs 46.10 _refine_ls_shell.R_factor_R_free 0.384 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 65 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs 1250 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3CM3 _struct.title 'High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3CM3 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Dual-specificity phosphatase, Vaccinia virus, VH1, Hydrolase, Late Protein, Protein phosphatase' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 4 ? # _struct_biol.id 1 _struct_biol.details 'One copy of the biologically relevant monomer is present in the asymmetric unit' # 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 10 ? THR A 20 ? SER A 1007 THR A 1017 1 ? 11 HELX_P HELX_P2 2 ASN A 43 ? ASP A 49 ? ASN A 1040 ASP A 1046 1 ? 7 HELX_P HELX_P3 3 ALA A 50 ? SER A 53 ? ALA A 1047 SER A 1050 5 ? 4 HELX_P HELX_P4 4 ILE A 90 ? LYS A 92 ? ILE A 1087 LYS A 1089 5 ? 3 HELX_P HELX_P5 5 TYR A 93 ? ASN A 108 ? TYR A 1090 ASN A 1105 1 ? 16 HELX_P HELX_P6 6 ASN A 120 ? ASN A 134 ? ASN A 1117 ASN A 1131 1 ? 15 HELX_P HELX_P7 7 LEU A 138 ? GLY A 155 ? LEU A 1135 GLY A 1152 1 ? 18 HELX_P HELX_P8 8 ASN A 160 ? VAL A 172 ? ASN A 1157 VAL A 1169 1 ? 13 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # _struct_sheet.id A _struct_sheet.type ? _struct_sheet.number_strands 5 _struct_sheet.details ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 THR A 33 ? ARG A 34 ? THR A 1030 ARG A 1031 A 2 VAL A 39 ? GLY A 42 ? VAL A 1036 GLY A 1039 A 3 VAL A 111 ? HIS A 114 ? VAL A 1108 HIS A 1111 A 4 TYR A 59 ? ASN A 62 ? TYR A 1056 ASN A 1059 A 5 ASN A 76 ? HIS A 79 ? ASN A 1073 HIS A 1076 # 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 THR A 33 ? N THR A 1030 O LEU A 41 ? O LEU A 1038 A 2 3 N TYR A 40 ? N TYR A 1037 O VAL A 113 ? O VAL A 1110 A 3 4 O LEU A 112 ? O LEU A 1109 N LEU A 61 ? N LEU A 1058 A 4 5 N VAL A 60 ? N VAL A 1057 O ILE A 78 ? O ILE A 1075 # 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 A PO4 1 ? 8 'BINDING SITE FOR RESIDUE PO4 A 1' AC2 Software A BME 1174 ? 5 'BINDING SITE FOR RESIDUE BME A 1174' AC3 Software A BME 2 ? 3 'BINDING SITE FOR RESIDUE BME A 2' # 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 ASP A 84 ? ASP A 1081 . ? 1_555 ? 2 AC1 8 SER A 115 ? SER A 1112 . ? 1_555 ? 3 AC1 8 ALA A 116 ? ALA A 1113 . ? 1_555 ? 4 AC1 8 ALA A 117 ? ALA A 1114 . ? 1_555 ? 5 AC1 8 GLY A 118 ? GLY A 1115 . ? 1_555 ? 6 AC1 8 ASN A 120 ? ASN A 1117 . ? 1_555 ? 7 AC1 8 ARG A 121 ? ARG A 1118 . ? 1_555 ? 8 AC1 8 HOH E . ? HOH A 1199 . ? 1_555 ? 9 AC2 5 ASN A 120 ? ASN A 1117 . ? 1_555 ? 10 AC2 5 GLU A 159 ? GLU A 1156 . ? 1_555 ? 11 AC2 5 ASN A 160 ? ASN A 1157 . ? 1_555 ? 12 AC2 5 HOH E . ? HOH A 1251 . ? 1_555 ? 13 AC2 5 HOH E . ? HOH A 1391 . ? 1_555 ? 14 AC3 3 ASN A 134 ? ASN A 1131 . ? 1_555 ? 15 AC3 3 LYS A 135 ? LYS A 1132 . ? 1_555 ? 16 AC3 3 SER A 137 ? SER A 1134 . ? 1_555 ? # _database_PDB_matrix.entry_id 3CM3 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3CM3 _atom_sites.fract_transf_matrix[1][1] 0.015670 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.025846 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.007408 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O P S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . SER A 1 10 ? 23.183 -12.243 7.340 1.00 44.49 ? 1007 SER A N 1 ATOM 2 C CA . SER A 1 10 ? 21.716 -12.220 7.558 1.00 43.59 ? 1007 SER A CA 1 ATOM 3 C C . SER A 1 10 ? 21.163 -10.798 7.556 1.00 42.26 ? 1007 SER A C 1 ATOM 4 O O . SER A 1 10 ? 20.211 -10.492 6.830 1.00 41.39 ? 1007 SER A O 1 ATOM 5 C CB . SER A 1 10 ? 21.378 -12.924 8.872 1.00 44.08 ? 1007 SER A CB 1 ATOM 6 O OG . SER A 1 10 ? 21.891 -14.249 8.855 1.00 44.41 ? 1007 SER A OG 1 ATOM 7 N N . LEU A 1 11 ? 21.763 -9.925 8.369 1.00 42.33 ? 1008 LEU A N 1 ATOM 8 C CA . LEU A 1 11 ? 21.334 -8.523 8.461 1.00 41.98 ? 1008 LEU A CA 1 ATOM 9 C C . LEU A 1 11 ? 21.441 -7.823 7.107 1.00 39.42 ? 1008 LEU A C 1 ATOM 10 O O . LEU A 1 11 ? 20.696 -6.897 6.781 1.00 38.54 ? 1008 LEU A O 1 ATOM 11 C CB . LEU A 1 11 ? 22.160 -7.770 9.514 1.00 44.48 ? 1008 LEU A CB 1 ATOM 12 C CG . LEU A 1 11 ? 21.858 -8.020 10.999 1.00 50.00 ? 1008 LEU A CG 1 ATOM 13 C CD1 . LEU A 1 11 ? 22.859 -7.267 11.891 1.00 54.59 ? 1008 LEU A CD1 1 ATOM 14 C CD2 . LEU A 1 11 ? 20.410 -7.636 11.363 1.00 53.72 ? 1008 LEU A CD2 1 ATOM 15 N N . TYR A 1 12 ? 22.388 -8.300 6.305 1.00 37.60 ? 1009 TYR A N 1 ATOM 16 C CA . TYR A 1 12 ? 22.604 -7.778 4.968 1.00 36.44 ? 1009 TYR A CA 1 ATOM 17 C C . TYR A 1 12 ? 21.475 -8.159 3.995 1.00 34.46 ? 1009 TYR A C 1 ATOM 18 O O . TYR A 1 12 ? 20.937 -7.287 3.301 1.00 34.03 ? 1009 TYR A O 1 ATOM 19 C CB . TYR A 1 12 ? 23.987 -8.247 4.515 1.00 37.35 ? 1009 TYR A CB 1 ATOM 20 C CG . TYR A 1 12 ? 24.576 -7.492 3.353 1.00 37.20 ? 1009 TYR A CG 1 ATOM 21 C CD1 . TYR A 1 12 ? 24.371 -6.124 3.190 1.00 37.62 ? 1009 TYR A CD1 1 ATOM 22 C CD2 . TYR A 1 12 ? 25.360 -8.165 2.425 1.00 36.76 ? 1009 TYR A CD2 1 ATOM 23 C CE1 . TYR A 1 12 ? 24.921 -5.445 2.108 1.00 37.68 ? 1009 TYR A CE1 1 ATOM 24 C CE2 . TYR A 1 12 ? 25.913 -7.500 1.347 1.00 37.22 ? 1009 TYR A CE2 1 ATOM 25 C CZ . TYR A 1 12 ? 25.691 -6.147 1.197 1.00 37.60 ? 1009 TYR A CZ 1 ATOM 26 O OH . TYR A 1 12 ? 26.249 -5.509 0.122 1.00 39.04 ? 1009 TYR A OH 1 ATOM 27 N N . LYS A 1 13 ? 21.090 -9.440 3.972 1.00 30.45 ? 1010 LYS A N 1 ATOM 28 C CA . LYS A 1 13 ? 19.977 -9.930 3.157 1.00 27.79 ? 1010 LYS A CA 1 ATOM 29 C C . LYS A 1 13 ? 18.679 -9.227 3.576 1.00 24.44 ? 1010 LYS A C 1 ATOM 30 O O . LYS A 1 13 ? 17.820 -8.854 2.764 1.00 24.09 ? 1010 LYS A O 1 ATOM 31 C CB . LYS A 1 13 ? 19.820 -11.439 3.344 1.00 28.79 ? 1010 LYS A CB 1 ATOM 32 C CG . LYS A 1 13 ? 19.274 -12.183 2.133 1.00 33.33 ? 1010 LYS A CG 1 ATOM 33 C CD . LYS A 1 13 ? 18.705 -13.550 2.516 1.00 38.32 ? 1010 LYS A CD 1 ATOM 34 C CE . LYS A 1 13 ? 19.780 -14.482 3.067 1.00 40.07 ? 1010 LYS A CE 1 ATOM 35 N NZ . LYS A 1 13 ? 19.278 -15.893 3.007 1.00 41.44 ? 1010 LYS A NZ 1 ATOM 36 N N . TYR A 1 14 ? 18.542 -9.040 4.879 1.00 22.01 ? 1011 TYR A N 1 ATOM 37 C CA . TYR A 1 14 ? 17.431 -8.298 5.473 1.00 20.62 ? 1011 TYR A CA 1 ATOM 38 C C . TYR A 1 14 ? 17.342 -6.888 4.890 1.00 20.56 ? 1011 TYR A C 1 ATOM 39 O O . TYR A 1 14 ? 16.295 -6.441 4.426 1.00 21.05 ? 1011 TYR A O 1 ATOM 40 C CB . TYR A 1 14 ? 17.612 -8.268 6.997 1.00 21.04 ? 1011 TYR A CB 1 ATOM 41 C CG . TYR A 1 14 ? 16.783 -7.222 7.718 1.00 21.17 ? 1011 TYR A CG 1 ATOM 42 C CD1 . TYR A 1 14 ? 15.425 -7.417 7.966 1.00 22.32 ? 1011 TYR A CD1 1 ATOM 43 C CD2 . TYR A 1 14 ? 17.361 -6.043 8.183 1.00 22.45 ? 1011 TYR A CD2 1 ATOM 44 C CE1 . TYR A 1 14 ? 14.674 -6.447 8.644 1.00 23.41 ? 1011 TYR A CE1 1 ATOM 45 C CE2 . TYR A 1 14 ? 16.626 -5.070 8.849 1.00 23.11 ? 1011 TYR A CE2 1 ATOM 46 C CZ . TYR A 1 14 ? 15.276 -5.275 9.082 1.00 23.60 ? 1011 TYR A CZ 1 ATOM 47 O OH . TYR A 1 14 ? 14.553 -4.304 9.753 1.00 25.16 ? 1011 TYR A OH 1 ATOM 48 N N . LEU A 1 15 ? 18.464 -6.178 4.897 1.00 20.33 ? 1012 LEU A N 1 ATOM 49 C CA . LEU A 1 15 ? 18.478 -4.801 4.399 1.00 21.01 ? 1012 LEU A CA 1 ATOM 50 C C . LEU A 1 15 ? 18.076 -4.684 2.934 1.00 20.09 ? 1012 LEU A C 1 ATOM 51 O O . LEU A 1 15 ? 17.345 -3.764 2.549 1.00 19.44 ? 1012 LEU A O 1 ATOM 52 C CB . LEU A 1 15 ? 19.873 -4.173 4.578 1.00 22.64 ? 1012 LEU A CB 1 ATOM 53 C CG . LEU A 1 15 ? 20.184 -3.318 5.801 1.00 27.44 ? 1012 LEU A CG 1 ATOM 54 C CD1 . LEU A 1 15 ? 19.322 -3.659 6.999 1.00 30.89 ? 1012 LEU A CD1 1 ATOM 55 C CD2 . LEU A 1 15 ? 21.682 -3.373 6.124 1.00 28.98 ? 1012 LEU A CD2 1 ATOM 56 N N . LEU A 1 16 ? 18.561 -5.620 2.120 1.00 20.25 ? 1013 LEU A N 1 ATOM 57 C CA . LEU A 1 16 ? 18.340 -5.547 0.673 1.00 19.43 ? 1013 LEU A CA 1 ATOM 58 C C . LEU A 1 16 ? 16.918 -5.903 0.275 1.00 18.78 ? 1013 LEU A C 1 ATOM 59 O O . LEU A 1 16 ? 16.395 -5.315 -0.681 1.00 18.98 ? 1013 LEU A O 1 ATOM 60 C CB . LEU A 1 16 ? 19.375 -6.396 -0.075 1.00 20.50 ? 1013 LEU A CB 1 ATOM 61 C CG . LEU A 1 16 ? 20.809 -5.863 0.013 1.00 22.36 ? 1013 LEU A CG 1 ATOM 62 C CD1 . LEU A 1 16 ? 21.757 -6.870 -0.607 1.00 25.73 ? 1013 LEU A CD1 1 ATOM 63 C CD2 . LEU A 1 16 ? 20.918 -4.517 -0.676 1.00 23.69 ? 1013 LEU A CD2 1 ATOM 64 N N . LEU A 1 17 ? 16.304 -6.830 1.022 1.00 18.27 ? 1014 LEU A N 1 ATOM 65 C CA . LEU A 1 17 ? 14.889 -7.151 0.792 1.00 18.82 ? 1014 LEU A CA 1 ATOM 66 C C . LEU A 1 17 ? 14.012 -5.994 1.233 1.00 18.60 ? 1014 LEU A C 1 ATOM 67 O O . LEU A 1 17 ? 13.097 -5.589 0.511 1.00 19.82 ? 1014 LEU A O 1 ATOM 68 C CB . LEU A 1 17 ? 14.473 -8.446 1.490 1.00 19.45 ? 1014 LEU A CB 1 ATOM 69 C CG . LEU A 1 17 ? 15.042 -9.718 0.855 1.00 20.59 ? 1014 LEU A CG 1 ATOM 70 C CD1 . LEU A 1 17 ? 14.845 -10.925 1.761 1.00 23.30 ? 1014 LEU A CD1 1 ATOM 71 C CD2 . LEU A 1 17 ? 14.391 -9.961 -0.499 1.00 21.37 ? 1014 LEU A CD2 1 ATOM 72 N N . ARG A 1 18 ? 14.295 -5.441 2.414 1.00 18.33 ? 1015 ARG A N 1 ATOM 73 C CA . ARG A 1 18 ? 13.552 -4.267 2.876 1.00 19.23 ? 1015 ARG A CA 1 ATOM 74 C C . ARG A 1 18 ? 13.692 -3.112 1.887 1.00 19.25 ? 1015 ARG A C 1 ATOM 75 O O . ARG A 1 18 ? 12.766 -2.317 1.713 1.00 20.80 ? 1015 ARG A O 1 ATOM 76 C CB . ARG A 1 18 ? 14.033 -3.804 4.254 1.00 19.86 ? 1015 ARG A CB 1 ATOM 77 C CG . ARG A 1 18 ? 13.618 -4.681 5.409 1.00 19.49 ? 1015 ARG A CG 1 ATOM 78 C CD . ARG A 1 18 ? 12.189 -4.338 5.822 1.00 21.63 ? 1015 ARG A CD 1 ATOM 79 N NE . ARG A 1 18 ? 11.763 -5.069 7.013 1.00 24.10 ? 1015 ARG A NE 1 ATOM 80 C CZ . ARG A 1 18 ? 11.262 -6.306 6.998 1.00 25.97 ? 1015 ARG A CZ 1 ATOM 81 N NH1 . ARG A 1 18 ? 11.123 -6.966 5.849 1.00 26.45 ? 1015 ARG A NH1 1 ATOM 82 N NH2 . ARG A 1 18 ? 10.915 -6.890 8.139 1.00 28.74 ? 1015 ARG A NH2 1 ATOM 83 N N . SER A 1 19 ? 14.861 -3.017 1.259 1.00 18.28 ? 1016 SER A N 1 ATOM 84 C CA . SER A 1 19 ? 15.174 -1.901 0.381 1.00 18.14 ? 1016 SER A CA 1 ATOM 85 C C . SER A 1 19 ? 14.520 -2.030 -0.993 1.00 18.62 ? 1016 SER A C 1 ATOM 86 O O . SER A 1 19 ? 14.470 -1.063 -1.759 1.00 20.16 ? 1016 SER A O 1 ATOM 87 C CB . SER A 1 19 ? 16.690 -1.765 0.229 1.00 18.16 ? 1016 SER A CB 1 ATOM 88 O OG . SER A 1 19 ? 17.258 -1.282 1.429 1.00 19.88 ? 1016 SER A OG 1 ATOM 89 N N . THR A 1 20 ? 14.017 -3.222 -1.304 1.00 18.90 ? 1017 THR A N 1 ATOM 90 C CA . THR A 1 20 ? 13.371 -3.432 -2.604 1.00 19.63 ? 1017 THR A CA 1 ATOM 91 C C . THR A 1 20 ? 11.878 -3.734 -2.488 1.00 22.21 ? 1017 THR A C 1 ATOM 92 O O . THR A 1 20 ? 11.291 -4.458 -3.310 1.00 22.54 ? 1017 THR A O 1 ATOM 93 C CB . THR A 1 20 ? 14.118 -4.494 -3.420 1.00 19.24 ? 1017 THR A CB 1 ATOM 94 O OG1 . THR A 1 20 ? 14.310 -5.664 -2.631 1.00 20.92 ? 1017 THR A OG1 1 ATOM 95 C CG2 . THR A 1 20 ? 15.484 -3.953 -3.845 1.00 19.98 ? 1017 THR A CG2 1 ATOM 96 N N . GLY A 1 21 ? 11.267 -3.160 -1.460 1.00 25.57 ? 1018 GLY A N 1 ATOM 97 C CA . GLY A 1 21 ? 9.812 -3.133 -1.365 1.00 29.05 ? 1018 GLY A CA 1 ATOM 98 C C . GLY A 1 21 ? 9.203 -4.108 -0.388 1.00 30.47 ? 1018 GLY A C 1 ATOM 99 O O . GLY A 1 21 ? 7.992 -4.157 -0.233 1.00 31.07 ? 1018 GLY A O 1 ATOM 100 N N . ASP A 1 22 ? 10.049 -4.871 0.291 1.00 30.58 ? 1019 ASP A N 1 ATOM 101 C CA . ASP A 1 22 ? 9.591 -5.824 1.293 1.00 31.86 ? 1019 ASP A CA 1 ATOM 102 C C . ASP A 1 22 ? 9.420 -5.129 2.645 1.00 32.65 ? 1019 ASP A C 1 ATOM 103 O O . ASP A 1 22 ? 10.106 -5.462 3.617 1.00 33.37 ? 1019 ASP A O 1 ATOM 104 C CB . ASP A 1 22 ? 10.589 -6.977 1.399 1.00 32.67 ? 1019 ASP A CB 1 ATOM 105 C CG . ASP A 1 22 ? 9.922 -8.315 1.620 1.00 35.72 ? 1019 ASP A CG 1 ATOM 106 O OD1 . ASP A 1 22 ? 8.675 -8.381 1.625 1.00 40.17 ? 1019 ASP A OD1 1 ATOM 107 O OD2 . ASP A 1 22 ? 10.655 -9.309 1.788 1.00 37.19 ? 1019 ASP A OD2 1 ATOM 108 N N . MET A 1 23 ? 8.515 -4.150 2.686 1.00 33.80 ? 1020 MET A N 1 ATOM 109 C CA . MET A 1 23 ? 8.201 -3.408 3.907 1.00 36.03 ? 1020 MET A CA 1 ATOM 110 C C . MET A 1 23 ? 6.725 -3.584 4.233 1.00 35.57 ? 1020 MET A C 1 ATOM 111 O O . MET A 1 23 ? 5.913 -3.787 3.331 1.00 36.84 ? 1020 MET A O 1 ATOM 112 C CB . MET A 1 23 ? 8.497 -1.915 3.724 1.00 36.98 ? 1020 MET A CB 1 ATOM 113 C CG . MET A 1 23 ? 9.956 -1.574 3.451 1.00 39.78 ? 1020 MET A CG 1 ATOM 114 S SD . MET A 1 23 ? 10.187 0.131 2.896 1.00 37.05 ? 1020 MET A SD 1 ATOM 115 C CE . MET A 1 23 ? 9.710 1.045 4.359 1.00 38.64 ? 1020 MET A CE 1 ATOM 116 N N . HIS A 1 24 ? 6.377 -3.495 5.514 1.00 34.13 ? 1021 HIS A N 1 ATOM 117 C CA . HIS A 1 24 ? 4.967 -3.519 5.914 1.00 33.82 ? 1021 HIS A CA 1 ATOM 118 C C . HIS A 1 24 ? 4.347 -2.137 5.753 1.00 33.67 ? 1021 HIS A C 1 ATOM 119 O O . HIS A 1 24 ? 5.060 -1.133 5.768 1.00 34.06 ? 1021 HIS A O 1 ATOM 120 C CB . HIS A 1 24 ? 4.812 -3.980 7.368 1.00 33.83 ? 1021 HIS A CB 1 ATOM 121 C CG . HIS A 1 24 ? 5.461 -3.073 8.371 1.00 35.75 ? 1021 HIS A CG 1 ATOM 122 N ND1 . HIS A 1 24 ? 4.796 -2.045 9.006 1.00 38.16 ? 1021 HIS A ND1 1 ATOM 123 C CD2 . HIS A 1 24 ? 6.728 -3.039 8.850 1.00 36.72 ? 1021 HIS A CD2 1 ATOM 124 C CE1 . HIS A 1 24 ? 5.617 -1.420 9.830 1.00 39.04 ? 1021 HIS A CE1 1 ATOM 125 N NE2 . HIS A 1 24 ? 6.802 -2.003 9.752 1.00 38.17 ? 1021 HIS A NE2 1 ATOM 126 N N . LYS A 1 25 ? 3.023 -2.075 5.607 1.00 34.26 ? 1022 LYS A N 1 ATOM 127 C CA . LYS A 1 25 ? 2.320 -0.795 5.610 1.00 35.95 ? 1022 LYS A CA 1 ATOM 128 C C . LYS A 1 25 ? 2.526 -0.107 6.958 1.00 33.73 ? 1022 LYS A C 1 ATOM 129 O O . LYS A 1 25 ? 2.576 -0.773 7.994 1.00 34.00 ? 1022 LYS A O 1 ATOM 130 C CB . LYS A 1 25 ? 0.820 -0.983 5.369 1.00 38.34 ? 1022 LYS A CB 1 ATOM 131 C CG . LYS A 1 25 ? 0.027 0.324 5.298 1.00 44.81 ? 1022 LYS A CG 1 ATOM 132 C CD . LYS A 1 25 ? -1.190 0.306 6.219 1.00 52.86 ? 1022 LYS A CD 1 ATOM 133 C CE . LYS A 1 25 ? -2.291 -0.594 5.668 1.00 54.96 ? 1022 LYS A CE 1 ATOM 134 N NZ . LYS A 1 25 ? -2.980 0.029 4.467 1.00 57.76 ? 1022 LYS A NZ 1 ATOM 135 N N . ALA A 1 26 ? 2.655 1.215 6.943 1.00 31.62 ? 1023 ALA A N 1 ATOM 136 C CA . ALA A 1 26 ? 2.866 1.979 8.169 1.00 29.59 ? 1023 ALA A CA 1 ATOM 137 C C . ALA A 1 26 ? 1.743 1.778 9.181 1.00 28.94 ? 1023 ALA A C 1 ATOM 138 O O . ALA A 1 26 ? 0.552 1.746 8.820 1.00 29.53 ? 1023 ALA A O 1 ATOM 139 C CB . ALA A 1 26 ? 3.046 3.459 7.856 1.00 29.89 ? 1023 ALA A CB 1 ATOM 140 N N . LYS A 1 27 ? 2.140 1.618 10.441 1.00 28.48 ? 1024 LYS A N 1 ATOM 141 C CA . LYS A 1 27 ? 1.193 1.603 11.551 1.00 29.17 ? 1024 LYS A CA 1 ATOM 142 C C . LYS A 1 27 ? 1.667 2.519 12.684 1.00 27.80 ? 1024 LYS A C 1 ATOM 143 O O . LYS A 1 27 ? 2.868 2.626 12.959 1.00 27.14 ? 1024 LYS A O 1 ATOM 144 C CB . LYS A 1 27 ? 0.877 0.178 12.026 1.00 30.86 ? 1024 LYS A CB 1 ATOM 145 C CG . LYS A 1 27 ? 1.951 -0.563 12.789 1.00 37.50 ? 1024 LYS A CG 1 ATOM 146 C CD . LYS A 1 27 ? 1.691 -0.548 14.304 1.00 44.81 ? 1024 LYS A CD 1 ATOM 147 C CE . LYS A 1 27 ? 2.874 -1.170 15.046 1.00 46.58 ? 1024 LYS A CE 1 ATOM 148 N NZ . LYS A 1 27 ? 3.055 -0.630 16.423 1.00 46.50 ? 1024 LYS A NZ 1 ATOM 149 N N . SER A 1 28 ? 0.722 3.211 13.310 1.00 27.12 ? 1025 SER A N 1 ATOM 150 C CA . SER A 1 28 ? 1.045 4.230 14.309 1.00 27.36 ? 1025 SER A CA 1 ATOM 151 C C . SER A 1 28 ? 1.682 3.638 15.557 1.00 25.25 ? 1025 SER A C 1 ATOM 152 O O . SER A 1 28 ? 1.158 2.679 16.134 1.00 27.10 ? 1025 SER A O 1 ATOM 153 C CB . SER A 1 28 ? -0.231 4.973 14.714 1.00 28.47 ? 1025 SER A CB 1 ATOM 154 O OG . SER A 1 28 ? -0.814 5.648 13.606 1.00 33.15 ? 1025 SER A OG 1 ATOM 155 N N . PRO A 1 29 ? 2.805 4.205 16.000 1.00 24.05 ? 1026 PRO A N 1 ATOM 156 C CA . PRO A 1 29 ? 3.391 3.754 17.253 1.00 24.50 ? 1026 PRO A CA 1 ATOM 157 C C . PRO A 1 29 ? 2.484 4.093 18.435 1.00 25.82 ? 1026 PRO A C 1 ATOM 158 O O . PRO A 1 29 ? 1.745 5.076 18.404 1.00 27.09 ? 1026 PRO A O 1 ATOM 159 C CB . PRO A 1 29 ? 4.703 4.546 17.342 1.00 23.89 ? 1026 PRO A CB 1 ATOM 160 C CG . PRO A 1 29 ? 4.945 5.078 15.983 1.00 23.76 ? 1026 PRO A CG 1 ATOM 161 C CD . PRO A 1 29 ? 3.614 5.245 15.344 1.00 22.80 ? 1026 PRO A CD 1 ATOM 162 N N . THR A 1 30 ? 2.570 3.296 19.486 1.00 28.48 ? 1027 THR A N 1 ATOM 163 C CA . THR A 1 30 ? 1.749 3.516 20.668 1.00 31.11 ? 1027 THR A CA 1 ATOM 164 C C . THR A 1 30 ? 2.619 3.709 21.898 1.00 30.14 ? 1027 THR A C 1 ATOM 165 O O . THR A 1 30 ? 2.490 4.698 22.630 1.00 31.69 ? 1027 THR A O 1 ATOM 166 C CB . THR A 1 30 ? 0.766 2.328 20.904 1.00 32.58 ? 1027 THR A CB 1 ATOM 167 O OG1 . THR A 1 30 ? 1.489 1.091 20.919 1.00 36.29 ? 1027 THR A OG1 1 ATOM 168 C CG2 . THR A 1 30 ? -0.269 2.256 19.794 1.00 34.64 ? 1027 THR A CG2 1 ATOM 169 N N . ILE A 1 31 ? 3.504 2.744 22.127 1.00 29.61 ? 1028 ILE A N 1 ATOM 170 C CA . ILE A 1 31 ? 4.366 2.773 23.294 1.00 29.34 ? 1028 ILE A CA 1 ATOM 171 C C . ILE A 1 31 ? 5.685 3.471 22.992 1.00 27.43 ? 1028 ILE A C 1 ATOM 172 O O . ILE A 1 31 ? 6.198 3.447 21.872 1.00 27.83 ? 1028 ILE A O 1 ATOM 173 C CB . ILE A 1 31 ? 4.623 1.359 23.883 1.00 30.74 ? 1028 ILE A CB 1 ATOM 174 C CG1 . ILE A 1 31 ? 5.357 0.456 22.886 1.00 33.34 ? 1028 ILE A CG1 1 ATOM 175 C CG2 . ILE A 1 31 ? 3.308 0.737 24.355 1.00 32.45 ? 1028 ILE A CG2 1 ATOM 176 C CD1 . ILE A 1 31 ? 5.969 -0.795 23.507 1.00 35.77 ? 1028 ILE A CD1 1 ATOM 177 N N . MET A 1 32 ? 6.197 4.136 24.020 1.00 25.83 ? 1029 MET A N 1 ATOM 178 C CA . MET A 1 32 ? 7.531 4.715 24.016 1.00 24.73 ? 1029 MET A CA 1 ATOM 179 C C . MET A 1 32 ? 8.556 3.657 23.634 1.00 23.67 ? 1029 MET A C 1 ATOM 180 O O . MET A 1 32 ? 8.382 2.480 23.942 1.00 24.72 ? 1029 MET A O 1 ATOM 181 C CB . MET A 1 32 ? 7.834 5.225 25.421 1.00 26.43 ? 1029 MET A CB 1 ATOM 182 C CG . MET A 1 32 ? 8.792 6.386 25.489 1.00 27.62 ? 1029 MET A CG 1 ATOM 183 S SD . MET A 1 32 ? 8.811 7.070 27.157 1.00 24.41 ? 1029 MET A SD 1 ATOM 184 C CE . MET A 1 32 ? 8.728 5.599 28.178 1.00 27.97 ? 1029 MET A CE 1 ATOM 185 N N . THR A 1 33 ? 9.627 4.077 22.969 1.00 22.04 ? 1030 THR A N 1 ATOM 186 C CA . THR A 1 33 ? 10.718 3.164 22.660 1.00 22.32 ? 1030 THR A CA 1 ATOM 187 C C . THR A 1 33 ? 12.021 3.691 23.253 1.00 21.34 ? 1030 THR A C 1 ATOM 188 O O . THR A 1 33 ? 12.376 4.852 23.035 1.00 21.73 ? 1030 THR A O 1 ATOM 189 C CB . THR A 1 33 ? 10.868 3.013 21.130 1.00 22.88 ? 1030 THR A CB 1 ATOM 190 O OG1 . THR A 1 33 ? 9.693 2.409 20.575 1.00 24.99 ? 1030 THR A OG1 1 ATOM 191 C CG2 . THR A 1 33 ? 12.076 2.156 20.777 1.00 24.61 ? 1030 THR A CG2 1 ATOM 192 N N . ARG A 1 34 ? 12.725 2.841 23.995 1.00 22.39 ? 1031 ARG A N 1 ATOM 193 C CA . ARG A 1 34 ? 14.070 3.151 24.456 1.00 23.26 ? 1031 ARG A CA 1 ATOM 194 C C . ARG A 1 34 ? 15.027 2.913 23.294 1.00 23.42 ? 1031 ARG A C 1 ATOM 195 O O . ARG A 1 34 ? 15.159 1.796 22.799 1.00 24.53 ? 1031 ARG A O 1 ATOM 196 C CB . ARG A 1 34 ? 14.467 2.278 25.643 1.00 23.78 ? 1031 ARG A CB 1 ATOM 197 C CG . ARG A 1 34 ? 15.796 2.664 26.277 1.00 25.82 ? 1031 ARG A CG 1 ATOM 198 C CD . ARG A 1 34 ? 16.122 1.771 27.464 1.00 28.55 ? 1031 ARG A CD 1 ATOM 199 N NE . ARG A 1 34 ? 17.212 2.303 28.276 1.00 30.12 ? 1031 ARG A NE 1 ATOM 200 C CZ . ARG A 1 34 ? 17.817 1.627 29.259 1.00 31.37 ? 1031 ARG A CZ 1 ATOM 201 N NH1 . ARG A 1 34 ? 17.452 0.383 29.555 1.00 33.10 ? 1031 ARG A NH1 1 ATOM 202 N NH2 . ARG A 1 34 ? 18.796 2.192 29.957 1.00 32.35 ? 1031 ARG A NH2 1 ATOM 203 N N . VAL A 1 35 ? 15.695 3.970 22.848 1.00 23.60 ? 1032 VAL A N 1 ATOM 204 C CA . VAL A 1 35 ? 16.581 3.864 21.695 1.00 25.03 ? 1032 VAL A CA 1 ATOM 205 C C . VAL A 1 35 ? 18.026 3.629 22.123 1.00 24.78 ? 1032 VAL A C 1 ATOM 206 O O . VAL A 1 35 ? 18.724 2.792 21.554 1.00 25.88 ? 1032 VAL A O 1 ATOM 207 C CB . VAL A 1 35 ? 16.502 5.112 20.797 1.00 25.43 ? 1032 VAL A CB 1 ATOM 208 C CG1 . VAL A 1 35 ? 15.056 5.414 20.435 1.00 25.75 ? 1032 VAL A CG1 1 ATOM 209 C CG2 . VAL A 1 35 ? 17.148 6.303 21.485 1.00 26.23 ? 1032 VAL A CG2 1 ATOM 210 N N . THR A 1 36 ? 18.463 4.373 23.132 1.00 24.78 ? 1033 THR A N 1 ATOM 211 C CA . THR A 1 36 ? 19.783 4.176 23.732 1.00 24.79 ? 1033 THR A CA 1 ATOM 212 C C . THR A 1 36 ? 19.611 4.058 25.247 1.00 24.89 ? 1033 THR A C 1 ATOM 213 O O . THR A 1 36 ? 18.477 3.965 25.743 1.00 25.48 ? 1033 THR A O 1 ATOM 214 C CB . THR A 1 36 ? 20.755 5.333 23.401 1.00 24.72 ? 1033 THR A CB 1 ATOM 215 O OG1 . THR A 1 36 ? 20.293 6.536 24.029 1.00 24.91 ? 1033 THR A OG1 1 ATOM 216 C CG2 . THR A 1 36 ? 20.879 5.541 21.883 1.00 25.07 ? 1033 THR A CG2 1 ATOM 217 N N . ASN A 1 37 ? 20.712 4.067 25.993 1.00 25.29 ? 1034 ASN A N 1 ATOM 218 C CA . ASN A 1 37 ? 20.618 3.994 27.448 1.00 25.21 ? 1034 ASN A CA 1 ATOM 219 C C . ASN A 1 37 ? 19.669 5.052 28.017 1.00 25.21 ? 1034 ASN A C 1 ATOM 220 O O . ASN A 1 37 ? 18.836 4.745 28.875 1.00 25.96 ? 1034 ASN A O 1 ATOM 221 C CB . ASN A 1 37 ? 21.984 4.106 28.120 1.00 25.64 ? 1034 ASN A CB 1 ATOM 222 C CG . ASN A 1 37 ? 22.691 2.771 28.236 1.00 27.43 ? 1034 ASN A CG 1 ATOM 223 O OD1 . ASN A 1 37 ? 22.328 1.788 27.591 1.00 28.98 ? 1034 ASN A OD1 1 ATOM 224 N ND2 . ASN A 1 37 ? 23.714 2.724 29.077 1.00 29.63 ? 1034 ASN A ND2 1 ATOM 225 N N . ASN A 1 38 ? 19.790 6.287 27.531 1.00 24.07 ? 1035 ASN A N 1 ATOM 226 C CA . ASN A 1 38 ? 19.006 7.393 28.098 1.00 23.48 ? 1035 ASN A CA 1 ATOM 227 C C . ASN A 1 38 ? 18.076 8.130 27.142 1.00 21.79 ? 1035 ASN A C 1 ATOM 228 O O . ASN A 1 38 ? 17.318 9.001 27.590 1.00 22.34 ? 1035 ASN A O 1 ATOM 229 C CB . ASN A 1 38 ? 19.922 8.419 28.761 1.00 24.36 ? 1035 ASN A CB 1 ATOM 230 C CG . ASN A 1 38 ? 20.632 7.841 29.956 1.00 26.85 ? 1035 ASN A CG 1 ATOM 231 O OD1 . ASN A 1 38 ? 20.079 7.797 31.046 1.00 29.45 ? 1035 ASN A OD1 1 ATOM 232 N ND2 . ASN A 1 38 ? 21.854 7.378 29.733 1.00 29.77 ? 1035 ASN A ND2 1 ATOM 233 N N . VAL A 1 39 ? 18.146 7.795 25.858 1.00 19.70 ? 1036 VAL A N 1 ATOM 234 C CA . VAL A 1 39 ? 17.313 8.479 24.867 1.00 17.87 ? 1036 VAL A CA 1 ATOM 235 C C . VAL A 1 39 ? 16.114 7.628 24.451 1.00 18.05 ? 1036 VAL A C 1 ATOM 236 O O . VAL A 1 39 ? 16.246 6.470 24.046 1.00 18.78 ? 1036 VAL A O 1 ATOM 237 C CB . VAL A 1 39 ? 18.128 8.923 23.629 1.00 17.75 ? 1036 VAL A CB 1 ATOM 238 C CG1 . VAL A 1 39 ? 17.259 9.671 22.633 1.00 17.13 ? 1036 VAL A CG1 1 ATOM 239 C CG2 . VAL A 1 39 ? 19.300 9.803 24.049 1.00 17.65 ? 1036 VAL A CG2 1 ATOM 240 N N . TYR A 1 40 ? 14.932 8.245 24.558 1.00 17.40 ? 1037 TYR A N 1 ATOM 241 C CA . TYR A 1 40 ? 13.660 7.583 24.264 1.00 17.61 ? 1037 TYR A CA 1 ATOM 242 C C . TYR A 1 40 ? 12.937 8.320 23.134 1.00 15.89 ? 1037 TYR A C 1 ATOM 243 O O . TYR A 1 40 ? 13.147 9.522 22.934 1.00 15.68 ? 1037 TYR A O 1 ATOM 244 C CB . TYR A 1 40 ? 12.766 7.535 25.518 1.00 18.45 ? 1037 TYR A CB 1 ATOM 245 C CG . TYR A 1 40 ? 13.310 6.665 26.635 1.00 20.62 ? 1037 TYR A CG 1 ATOM 246 C CD1 . TYR A 1 40 ? 12.720 5.447 26.961 1.00 22.65 ? 1037 TYR A CD1 1 ATOM 247 C CD2 . TYR A 1 40 ? 14.425 7.060 27.375 1.00 21.91 ? 1037 TYR A CD2 1 ATOM 248 C CE1 . TYR A 1 40 ? 13.225 4.643 27.987 1.00 24.00 ? 1037 TYR A CE1 1 ATOM 249 C CE2 . TYR A 1 40 ? 14.944 6.269 28.395 1.00 23.67 ? 1037 TYR A CE2 1 ATOM 250 C CZ . TYR A 1 40 ? 14.335 5.057 28.708 1.00 24.23 ? 1037 TYR A CZ 1 ATOM 251 O OH . TYR A 1 40 ? 14.843 4.257 29.721 1.00 26.78 ? 1037 TYR A OH 1 ATOM 252 N N . LEU A 1 41 ? 12.106 7.575 22.398 1.00 15.76 ? 1038 LEU A N 1 ATOM 253 C CA . LEU A 1 41 ? 11.323 8.114 21.275 1.00 15.83 ? 1038 LEU A CA 1 ATOM 254 C C . LEU A 1 41 ? 9.834 7.890 21.541 1.00 15.88 ? 1038 LEU A C 1 ATOM 255 O O . LEU A 1 41 ? 9.450 6.782 21.916 1.00 17.25 ? 1038 LEU A O 1 ATOM 256 C CB . LEU A 1 41 ? 11.727 7.420 19.966 1.00 15.99 ? 1038 LEU A CB 1 ATOM 257 C CG . LEU A 1 41 ? 10.886 7.673 18.702 1.00 14.71 ? 1038 LEU A CG 1 ATOM 258 C CD1 . LEU A 1 41 ? 10.781 9.143 18.343 1.00 15.69 ? 1038 LEU A CD1 1 ATOM 259 C CD2 . LEU A 1 41 ? 11.474 6.877 17.540 1.00 15.78 ? 1038 LEU A CD2 1 ATOM 260 N N . GLY A 1 42 ? 9.018 8.924 21.343 1.00 15.65 ? 1039 GLY A N 1 ATOM 261 C CA . GLY A 1 42 ? 7.616 8.850 21.725 1.00 16.64 ? 1039 GLY A CA 1 ATOM 262 C C . GLY A 1 42 ? 6.701 9.784 20.963 1.00 15.71 ? 1039 GLY A C 1 ATOM 263 O O . GLY A 1 42 ? 7.149 10.631 20.186 1.00 15.60 ? 1039 GLY A O 1 ATOM 264 N N . ASN A 1 43 ? 5.401 9.613 21.201 1.00 16.29 ? 1040 ASN A N 1 ATOM 265 C CA . ASN A 1 43 ? 4.389 10.498 20.658 1.00 16.59 ? 1040 ASN A CA 1 ATOM 266 C C . ASN A 1 43 ? 3.883 11.458 21.745 1.00 16.94 ? 1040 ASN A C 1 ATOM 267 O O . ASN A 1 43 ? 4.439 11.541 22.852 1.00 17.08 ? 1040 ASN A O 1 ATOM 268 C CB . ASN A 1 43 ? 3.257 9.672 20.040 1.00 17.02 ? 1040 ASN A CB 1 ATOM 269 C CG . ASN A 1 43 ? 2.533 8.825 21.069 1.00 18.37 ? 1040 ASN A CG 1 ATOM 270 O OD1 . ASN A 1 43 ? 2.685 9.005 22.284 1.00 20.29 ? 1040 ASN A OD1 1 ATOM 271 N ND2 . ASN A 1 43 ? 1.724 7.897 20.571 1.00 21.96 ? 1040 ASN A ND2 1 ATOM 272 N N . TYR A 1 44 ? 2.829 12.203 21.432 1.00 17.21 ? 1041 TYR A N 1 ATOM 273 C CA A TYR A 1 44 ? 2.318 13.197 22.369 0.50 18.26 ? 1041 TYR A CA 1 ATOM 274 C CA B TYR A 1 44 ? 2.309 13.199 22.361 0.50 18.24 ? 1041 TYR A CA 1 ATOM 275 C C . TYR A 1 44 ? 1.783 12.576 23.659 1.00 18.55 ? 1041 TYR A C 1 ATOM 276 O O . TYR A 1 44 ? 2.062 13.069 24.758 1.00 18.17 ? 1041 TYR A O 1 ATOM 277 C CB A TYR A 1 44 ? 1.249 14.085 21.720 0.50 19.19 ? 1041 TYR A CB 1 ATOM 278 C CB B TYR A 1 44 ? 1.225 14.032 21.676 0.50 19.14 ? 1041 TYR A CB 1 ATOM 279 C CG A TYR A 1 44 ? 1.065 15.382 22.469 0.50 20.88 ? 1041 TYR A CG 1 ATOM 280 C CG B TYR A 1 44 ? 0.408 14.879 22.612 0.50 20.72 ? 1041 TYR A CG 1 ATOM 281 C CD1 A TYR A 1 44 ? 2.043 16.372 22.427 0.50 24.43 ? 1041 TYR A CD1 1 ATOM 282 C CD1 B TYR A 1 44 ? 0.869 16.118 23.045 0.50 23.02 ? 1041 TYR A CD1 1 ATOM 283 C CD2 A TYR A 1 44 ? -0.070 15.613 23.237 0.50 23.74 ? 1041 TYR A CD2 1 ATOM 284 C CD2 B TYR A 1 44 ? -0.841 14.448 23.051 0.50 22.46 ? 1041 TYR A CD2 1 ATOM 285 C CE1 A TYR A 1 44 ? 1.887 17.558 23.122 0.50 26.41 ? 1041 TYR A CE1 1 ATOM 286 C CE1 B TYR A 1 44 ? 0.110 16.906 23.902 0.50 24.32 ? 1041 TYR A CE1 1 ATOM 287 C CE2 A TYR A 1 44 ? -0.234 16.800 23.934 0.50 25.83 ? 1041 TYR A CE2 1 ATOM 288 C CE2 B TYR A 1 44 ? -1.601 15.225 23.912 0.50 23.59 ? 1041 TYR A CE2 1 ATOM 289 C CZ A TYR A 1 44 ? 0.748 17.770 23.870 0.50 27.41 ? 1041 TYR A CZ 1 ATOM 290 C CZ B TYR A 1 44 ? -1.127 16.453 24.334 0.50 25.09 ? 1041 TYR A CZ 1 ATOM 291 O OH A TYR A 1 44 ? 0.591 18.944 24.564 0.50 29.19 ? 1041 TYR A OH 1 ATOM 292 O OH B TYR A 1 44 ? -1.887 17.223 25.190 0.50 25.88 ? 1041 TYR A OH 1 ATOM 293 N N . LYS A 1 45 ? 1.020 11.495 23.541 1.00 19.06 ? 1042 LYS A N 1 ATOM 294 C CA . LYS A 1 45 ? 0.528 10.800 24.734 1.00 20.22 ? 1042 LYS A CA 1 ATOM 295 C C . LYS A 1 45 ? 1.678 10.362 25.634 1.00 19.20 ? 1042 LYS A C 1 ATOM 296 O O . LYS A 1 45 ? 1.616 10.499 26.857 1.00 20.16 ? 1042 LYS A O 1 ATOM 297 C CB . LYS A 1 45 ? -0.330 9.591 24.334 1.00 21.89 ? 1042 LYS A CB 1 ATOM 298 C CG . LYS A 1 45 ? -0.797 8.743 25.523 1.00 26.76 ? 1042 LYS A CG 1 ATOM 299 C CD . LYS A 1 45 ? -2.112 8.040 25.246 1.00 34.34 ? 1042 LYS A CD 1 ATOM 300 C CE . LYS A 1 45 ? -2.525 7.166 26.421 1.00 36.89 ? 1042 LYS A CE 1 ATOM 301 N NZ . LYS A 1 45 ? -2.532 7.883 27.734 1.00 37.59 ? 1042 LYS A NZ 1 ATOM 302 N N . ASN A 1 46 ? 2.755 9.855 25.023 1.00 18.59 ? 1043 ASN A N 1 ATOM 303 C CA . ASN A 1 46 ? 3.910 9.452 25.807 1.00 18.14 ? 1043 ASN A CA 1 ATOM 304 C C . ASN A 1 46 ? 4.485 10.651 26.576 1.00 17.43 ? 1043 ASN A C 1 ATOM 305 O O . ASN A 1 46 ? 4.966 10.500 27.711 1.00 18.63 ? 1043 ASN A O 1 ATOM 306 C CB . ASN A 1 46 ? 5.006 8.845 24.918 1.00 18.46 ? 1043 ASN A CB 1 ATOM 307 C CG . ASN A 1 46 ? 4.577 7.588 24.166 1.00 19.82 ? 1043 ASN A CG 1 ATOM 308 O OD1 . ASN A 1 46 ? 3.698 6.814 24.590 1.00 23.49 ? 1043 ASN A OD1 1 ATOM 309 N ND2 . ASN A 1 46 ? 5.230 7.357 23.043 1.00 21.05 ? 1043 ASN A ND2 1 ATOM 310 N N . ALA A 1 47 ? 4.440 11.841 25.959 1.00 16.59 ? 1044 ALA A N 1 ATOM 311 C CA . ALA A 1 47 ? 4.961 13.040 26.648 1.00 16.89 ? 1044 ALA A CA 1 ATOM 312 C C . ALA A 1 47 ? 4.076 13.386 27.849 1.00 17.61 ? 1044 ALA A C 1 ATOM 313 O O . ALA A 1 47 ? 4.560 13.723 28.939 1.00 18.47 ? 1044 ALA A O 1 ATOM 314 C CB . ALA A 1 47 ? 5.056 14.211 25.693 1.00 16.99 ? 1044 ALA A CB 1 ATOM 315 N N . MET A 1 48 ? 2.765 13.301 27.647 1.00 18.92 ? 1045 MET A N 1 ATOM 316 C CA . MET A 1 48 ? 1.820 13.582 28.734 1.00 20.47 ? 1045 MET A CA 1 ATOM 317 C C . MET A 1 48 ? 1.975 12.598 29.893 1.00 21.18 ? 1045 MET A C 1 ATOM 318 O O . MET A 1 48 ? 1.778 12.966 31.048 1.00 22.17 ? 1045 MET A O 1 ATOM 319 C CB . MET A 1 48 ? 0.385 13.598 28.201 1.00 21.53 ? 1045 MET A CB 1 ATOM 320 C CG . MET A 1 48 ? 0.104 14.683 27.167 1.00 21.67 ? 1045 MET A CG 1 ATOM 321 S SD . MET A 1 48 ? 0.587 16.361 27.598 1.00 26.38 ? 1045 MET A SD 1 ATOM 322 C CE . MET A 1 48 ? 2.169 16.532 26.750 1.00 25.37 ? 1045 MET A CE 1 ATOM 323 N N . ASP A 1 49 ? 2.352 11.361 29.570 1.00 21.77 ? 1046 ASP A N 1 ATOM 324 C CA . ASP A 1 49 ? 2.556 10.312 30.567 1.00 22.83 ? 1046 ASP A CA 1 ATOM 325 C C . ASP A 1 49 ? 3.967 10.279 31.139 1.00 23.32 ? 1046 ASP A C 1 ATOM 326 O O . ASP A 1 49 ? 4.257 9.492 32.050 1.00 24.36 ? 1046 ASP A O 1 ATOM 327 C CB . ASP A 1 49 ? 2.222 8.940 29.969 1.00 23.87 ? 1046 ASP A CB 1 ATOM 328 C CG . ASP A 1 49 ? 0.752 8.796 29.631 1.00 25.17 ? 1046 ASP A CG 1 ATOM 329 O OD1 . ASP A 1 49 ? -0.068 9.513 30.247 1.00 29.86 ? 1046 ASP A OD1 1 ATOM 330 O OD2 . ASP A 1 49 ? 0.415 7.978 28.743 1.00 26.57 ? 1046 ASP A OD2 1 ATOM 331 N N . ALA A 1 50 ? 4.831 11.146 30.622 1.00 22.61 ? 1047 ALA A N 1 ATOM 332 C CA . ALA A 1 50 ? 6.226 11.200 31.042 1.00 22.15 ? 1047 ALA A CA 1 ATOM 333 C C . ALA A 1 50 ? 6.403 11.304 32.559 1.00 23.00 ? 1047 ALA A C 1 ATOM 334 O O . ALA A 1 50 ? 7.154 10.526 33.142 1.00 23.48 ? 1047 ALA A O 1 ATOM 335 C CB . ALA A 1 50 ? 6.971 12.326 30.330 1.00 22.10 ? 1047 ALA A CB 1 ATOM 336 N N . PRO A 1 51 ? 5.718 12.257 33.207 1.00 24.16 ? 1048 PRO A N 1 ATOM 337 C CA . PRO A 1 51 ? 5.928 12.421 34.655 1.00 25.88 ? 1048 PRO A CA 1 ATOM 338 C C . PRO A 1 51 ? 5.686 11.160 35.496 1.00 27.51 ? 1048 PRO A C 1 ATOM 339 O O . PRO A 1 51 ? 6.316 10.990 36.547 1.00 28.55 ? 1048 PRO A O 1 ATOM 340 C CB . PRO A 1 51 ? 4.924 13.524 35.024 1.00 25.82 ? 1048 PRO A CB 1 ATOM 341 C CG . PRO A 1 51 ? 4.807 14.326 33.746 1.00 25.01 ? 1048 PRO A CG 1 ATOM 342 C CD . PRO A 1 51 ? 4.773 13.264 32.685 1.00 24.06 ? 1048 PRO A CD 1 ATOM 343 N N . SER A 1 52 ? 4.813 10.266 35.034 1.00 27.83 ? 1049 SER A N 1 ATOM 344 C CA A SER A 1 52 ? 4.483 9.049 35.777 0.50 28.62 ? 1049 SER A CA 1 ATOM 345 C CA B SER A 1 52 ? 4.461 9.048 35.763 0.50 28.79 ? 1049 SER A CA 1 ATOM 346 C C . SER A 1 52 ? 5.167 7.794 35.242 1.00 28.90 ? 1049 SER A C 1 ATOM 347 O O . SER A 1 52 ? 4.951 6.686 35.759 1.00 28.92 ? 1049 SER A O 1 ATOM 348 C CB A SER A 1 52 ? 2.971 8.824 35.803 0.50 28.69 ? 1049 SER A CB 1 ATOM 349 C CB B SER A 1 52 ? 2.945 8.853 35.708 0.50 29.08 ? 1049 SER A CB 1 ATOM 350 O OG A SER A 1 52 ? 2.346 9.783 36.633 0.50 29.61 ? 1049 SER A OG 1 ATOM 351 O OG B SER A 1 52 ? 2.565 7.633 36.313 0.50 30.66 ? 1049 SER A OG 1 ATOM 352 N N . SER A 1 53 ? 5.994 7.983 34.215 1.00 29.64 ? 1050 SER A N 1 ATOM 353 C CA . SER A 1 53 ? 6.733 6.889 33.599 1.00 30.90 ? 1050 SER A CA 1 ATOM 354 C C . SER A 1 53 ? 7.679 6.160 34.547 1.00 32.23 ? 1050 SER A C 1 ATOM 355 O O . SER A 1 53 ? 8.201 6.747 35.494 1.00 32.55 ? 1050 SER A O 1 ATOM 356 C CB . SER A 1 53 ? 7.592 7.432 32.447 1.00 29.90 ? 1050 SER A CB 1 ATOM 357 O OG . SER A 1 53 ? 8.520 6.459 32.001 1.00 31.06 ? 1050 SER A OG 1 ATOM 358 N N . GLU A 1 54 ? 7.907 4.878 34.262 1.00 34.10 ? 1051 GLU A N 1 ATOM 359 C CA . GLU A 1 54 ? 8.893 4.072 34.983 1.00 35.15 ? 1051 GLU A CA 1 ATOM 360 C C . GLU A 1 54 ? 10.280 4.721 34.903 1.00 33.70 ? 1051 GLU A C 1 ATOM 361 O O . GLU A 1 54 ? 11.125 4.517 35.782 1.00 34.43 ? 1051 GLU A O 1 ATOM 362 C CB . GLU A 1 54 ? 8.938 2.649 34.423 1.00 36.14 ? 1051 GLU A CB 1 ATOM 363 C CG . GLU A 1 54 ? 7.623 1.888 34.559 1.00 39.64 ? 1051 GLU A CG 1 ATOM 364 C CD . GLU A 1 54 ? 7.346 1.498 35.995 1.00 43.57 ? 1051 GLU A CD 1 ATOM 365 O OE1 . GLU A 1 54 ? 6.515 2.162 36.653 1.00 45.67 ? 1051 GLU A OE1 1 ATOM 366 O OE2 . GLU A 1 54 ? 7.977 0.524 36.468 1.00 45.62 ? 1051 GLU A OE2 1 ATOM 367 N N . VAL A 1 55 ? 10.486 5.496 33.846 1.00 31.35 ? 1052 VAL A N 1 ATOM 368 C CA . VAL A 1 55 ? 11.722 6.227 33.593 1.00 30.26 ? 1052 VAL A CA 1 ATOM 369 C C . VAL A 1 55 ? 11.668 7.595 34.259 1.00 31.01 ? 1052 VAL A C 1 ATOM 370 O O . VAL A 1 55 ? 10.680 8.317 34.106 1.00 31.45 ? 1052 VAL A O 1 ATOM 371 C CB . VAL A 1 55 ? 11.942 6.416 32.071 1.00 29.32 ? 1052 VAL A CB 1 ATOM 372 C CG1 . VAL A 1 55 ? 13.241 7.160 31.777 1.00 28.96 ? 1052 VAL A CG1 1 ATOM 373 C CG2 . VAL A 1 55 ? 11.917 5.070 31.360 1.00 30.35 ? 1052 VAL A CG2 1 ATOM 374 N N . LYS A 1 56 ? 12.720 7.952 34.991 1.00 32.74 ? 1053 LYS A N 1 ATOM 375 C CA . LYS A 1 56 ? 12.800 9.283 35.610 1.00 33.63 ? 1053 LYS A CA 1 ATOM 376 C C . LYS A 1 56 ? 13.408 10.310 34.651 1.00 29.46 ? 1053 LYS A C 1 ATOM 377 O O . LYS A 1 56 ? 14.600 10.606 34.707 1.00 29.49 ? 1053 LYS A O 1 ATOM 378 C CB . LYS A 1 56 ? 13.576 9.244 36.940 1.00 36.36 ? 1053 LYS A CB 1 ATOM 379 C CG . LYS A 1 56 ? 14.676 8.177 37.070 1.00 42.95 ? 1053 LYS A CG 1 ATOM 380 C CD . LYS A 1 56 ? 15.928 8.465 36.240 1.00 49.58 ? 1053 LYS A CD 1 ATOM 381 C CE . LYS A 1 56 ? 17.036 7.462 36.528 1.00 51.67 ? 1053 LYS A CE 1 ATOM 382 N NZ . LYS A 1 56 ? 18.236 7.688 35.670 1.00 52.59 ? 1053 LYS A NZ 1 ATOM 383 N N . PHE A 1 57 ? 12.587 10.870 33.768 1.00 24.67 ? 1054 PHE A N 1 ATOM 384 C CA . PHE A 1 57 ? 13.109 11.819 32.777 1.00 21.19 ? 1054 PHE A CA 1 ATOM 385 C C . PHE A 1 57 ? 13.603 13.106 33.417 1.00 20.72 ? 1054 PHE A C 1 ATOM 386 O O . PHE A 1 57 ? 12.924 13.681 34.286 1.00 21.90 ? 1054 PHE A O 1 ATOM 387 C CB . PHE A 1 57 ? 12.036 12.167 31.737 1.00 19.93 ? 1054 PHE A CB 1 ATOM 388 C CG . PHE A 1 57 ? 11.725 11.013 30.836 1.00 19.62 ? 1054 PHE A CG 1 ATOM 389 C CD1 . PHE A 1 57 ? 12.622 10.648 29.841 1.00 19.09 ? 1054 PHE A CD1 1 ATOM 390 C CD2 . PHE A 1 57 ? 10.553 10.285 30.979 1.00 20.12 ? 1054 PHE A CD2 1 ATOM 391 C CE1 . PHE A 1 57 ? 12.347 9.570 29.006 1.00 20.27 ? 1054 PHE A CE1 1 ATOM 392 C CE2 . PHE A 1 57 ? 10.263 9.212 30.150 1.00 20.71 ? 1054 PHE A CE2 1 ATOM 393 C CZ . PHE A 1 57 ? 11.164 8.850 29.150 1.00 21.72 ? 1054 PHE A CZ 1 ATOM 394 N N . LYS A 1 58 ? 14.773 13.557 32.970 1.00 20.09 ? 1055 LYS A N 1 ATOM 395 C CA . LYS A 1 58 ? 15.242 14.898 33.297 1.00 19.99 ? 1055 LYS A CA 1 ATOM 396 C C . LYS A 1 58 ? 14.719 15.891 32.261 1.00 18.40 ? 1055 LYS A C 1 ATOM 397 O O . LYS A 1 58 ? 14.354 17.030 32.598 1.00 18.95 ? 1055 LYS A O 1 ATOM 398 C CB . LYS A 1 58 ? 16.772 14.965 33.378 1.00 20.97 ? 1055 LYS A CB 1 ATOM 399 C CG . LYS A 1 58 ? 17.284 16.355 33.729 1.00 23.84 ? 1055 LYS A CG 1 ATOM 400 C CD . LYS A 1 58 ? 18.752 16.374 34.121 1.00 27.22 ? 1055 LYS A CD 1 ATOM 401 C CE . LYS A 1 58 ? 19.153 17.785 34.533 1.00 29.92 ? 1055 LYS A CE 1 ATOM 402 N NZ . LYS A 1 58 ? 20.544 17.822 35.076 1.00 33.20 ? 1055 LYS A NZ 1 ATOM 403 N N . TYR A 1 59 ? 14.669 15.444 31.008 1.00 17.19 ? 1056 TYR A N 1 ATOM 404 C CA . TYR A 1 59 ? 14.303 16.300 29.890 1.00 16.24 ? 1056 TYR A CA 1 ATOM 405 C C . TYR A 1 59 ? 13.226 15.666 29.028 1.00 15.16 ? 1056 TYR A C 1 ATOM 406 O O . TYR A 1 59 ? 13.153 14.442 28.909 1.00 16.05 ? 1056 TYR A O 1 ATOM 407 C CB . TYR A 1 59 ? 15.520 16.540 28.995 1.00 16.38 ? 1056 TYR A CB 1 ATOM 408 C CG . TYR A 1 59 ? 16.623 17.357 29.625 1.00 17.51 ? 1056 TYR A CG 1 ATOM 409 C CD1 . TYR A 1 59 ? 16.473 18.727 29.822 1.00 18.87 ? 1056 TYR A CD1 1 ATOM 410 C CD2 . TYR A 1 59 ? 17.820 16.767 29.998 1.00 19.48 ? 1056 TYR A CD2 1 ATOM 411 C CE1 . TYR A 1 59 ? 17.471 19.485 30.395 1.00 20.50 ? 1056 TYR A CE1 1 ATOM 412 C CE2 . TYR A 1 59 ? 18.826 17.516 30.564 1.00 20.02 ? 1056 TYR A CE2 1 ATOM 413 C CZ . TYR A 1 59 ? 18.653 18.874 30.753 1.00 20.72 ? 1056 TYR A CZ 1 ATOM 414 O OH . TYR A 1 59 ? 19.667 19.617 31.315 1.00 23.83 ? 1056 TYR A OH 1 ATOM 415 N N . VAL A 1 60 ? 12.400 16.517 28.422 1.00 15.04 ? 1057 VAL A N 1 ATOM 416 C CA . VAL A 1 60 ? 11.561 16.144 27.281 1.00 14.89 ? 1057 VAL A CA 1 ATOM 417 C C . VAL A 1 60 ? 11.859 17.145 26.157 1.00 14.16 ? 1057 VAL A C 1 ATOM 418 O O . VAL A 1 60 ? 11.823 18.373 26.398 1.00 15.59 ? 1057 VAL A O 1 ATOM 419 C CB . VAL A 1 60 ? 10.062 16.165 27.662 1.00 15.50 ? 1057 VAL A CB 1 ATOM 420 C CG1 . VAL A 1 60 ? 9.175 16.008 26.421 1.00 16.66 ? 1057 VAL A CG1 1 ATOM 421 C CG2 . VAL A 1 60 ? 9.749 15.047 28.638 1.00 16.87 ? 1057 VAL A CG2 1 ATOM 422 N N . LEU A 1 61 ? 12.158 16.612 24.966 1.00 13.51 ? 1058 LEU A N 1 ATOM 423 C CA . LEU A 1 61 ? 12.355 17.447 23.801 1.00 13.34 ? 1058 LEU A CA 1 ATOM 424 C C . LEU A 1 61 ? 11.042 17.431 22.993 1.00 12.88 ? 1058 LEU A C 1 ATOM 425 O O . LEU A 1 61 ? 10.702 16.444 22.356 1.00 13.17 ? 1058 LEU A O 1 ATOM 426 C CB . LEU A 1 61 ? 13.550 16.932 22.981 1.00 14.47 ? 1058 LEU A CB 1 ATOM 427 C CG . LEU A 1 61 ? 13.865 17.721 21.731 1.00 16.30 ? 1058 LEU A CG 1 ATOM 428 C CD1 . LEU A 1 61 ? 14.176 19.165 22.074 1.00 20.08 ? 1058 LEU A CD1 1 ATOM 429 C CD2 . LEU A 1 61 ? 15.092 17.060 21.074 1.00 19.02 ? 1058 LEU A CD2 1 ATOM 430 N N . ASN A 1 62 ? 10.344 18.555 23.078 1.00 13.42 ? 1059 ASN A N 1 ATOM 431 C CA . ASN A 1 62 ? 9.053 18.750 22.429 1.00 13.06 ? 1059 ASN A CA 1 ATOM 432 C C . ASN A 1 62 ? 9.293 19.376 21.052 1.00 12.83 ? 1059 ASN A C 1 ATOM 433 O O . ASN A 1 62 ? 9.641 20.548 20.957 1.00 13.51 ? 1059 ASN A O 1 ATOM 434 C CB . ASN A 1 62 ? 8.207 19.687 23.289 1.00 13.61 ? 1059 ASN A CB 1 ATOM 435 C CG . ASN A 1 62 ? 6.924 20.139 22.593 1.00 13.59 ? 1059 ASN A CG 1 ATOM 436 O OD1 . ASN A 1 62 ? 6.456 19.491 21.650 1.00 14.91 ? 1059 ASN A OD1 1 ATOM 437 N ND2 . ASN A 1 62 ? 6.388 21.267 23.040 1.00 15.20 ? 1059 ASN A ND2 1 ATOM 438 N N . LEU A 1 63 ? 9.076 18.578 20.012 1.00 13.22 ? 1060 LEU A N 1 ATOM 439 C CA . LEU A 1 63 ? 9.279 19.005 18.636 1.00 14.22 ? 1060 LEU A CA 1 ATOM 440 C C . LEU A 1 63 ? 7.978 19.475 17.990 1.00 14.55 ? 1060 LEU A C 1 ATOM 441 O O . LEU A 1 63 ? 7.965 19.838 16.815 1.00 14.86 ? 1060 LEU A O 1 ATOM 442 C CB . LEU A 1 63 ? 9.864 17.858 17.807 1.00 14.16 ? 1060 LEU A CB 1 ATOM 443 C CG . LEU A 1 63 ? 11.384 17.697 17.741 1.00 20.88 ? 1060 LEU A CG 1 ATOM 444 C CD1 . LEU A 1 63 ? 12.085 18.546 18.787 1.00 19.64 ? 1060 LEU A CD1 1 ATOM 445 C CD2 . LEU A 1 63 ? 11.767 16.233 17.879 1.00 19.00 ? 1060 LEU A CD2 1 ATOM 446 N N . THR A 1 64 ? 6.882 19.463 18.745 1.00 15.20 ? 1061 THR A N 1 ATOM 447 C CA . THR A 1 64 ? 5.604 19.940 18.191 1.00 16.25 ? 1061 THR A CA 1 ATOM 448 C C . THR A 1 64 ? 5.564 21.461 18.216 1.00 16.50 ? 1061 THR A C 1 ATOM 449 O O . THR A 1 64 ? 6.392 22.110 18.869 1.00 17.13 ? 1061 THR A O 1 ATOM 450 C CB . THR A 1 64 ? 4.365 19.400 18.955 1.00 16.31 ? 1061 THR A CB 1 ATOM 451 O OG1 . THR A 1 64 ? 4.255 20.051 20.229 1.00 17.05 ? 1061 THR A OG1 1 ATOM 452 C CG2 . THR A 1 64 ? 4.439 17.899 19.121 1.00 16.82 ? 1061 THR A CG2 1 ATOM 453 N N . MET A 1 65 ? 4.550 22.048 17.572 1.00 17.17 ? 1062 MET A N 1 ATOM 454 C CA . MET A 1 65 ? 4.501 23.505 17.496 1.00 18.33 ? 1062 MET A CA 1 ATOM 455 C C . MET A 1 65 ? 4.006 24.157 18.790 1.00 19.51 ? 1062 MET A C 1 ATOM 456 O O . MET A 1 65 ? 4.286 25.331 19.035 1.00 21.58 ? 1062 MET A O 1 ATOM 457 C CB . MET A 1 65 ? 3.626 23.964 16.318 1.00 18.54 ? 1062 MET A CB 1 ATOM 458 C CG . MET A 1 65 ? 4.263 23.666 14.975 1.00 19.83 ? 1062 MET A CG 1 ATOM 459 S SD . MET A 1 65 ? 5.766 24.624 14.686 1.00 21.54 ? 1062 MET A SD 1 ATOM 460 C CE . MET A 1 65 ? 5.055 26.247 14.367 1.00 24.35 ? 1062 MET A CE 1 ATOM 461 N N A ASP A 1 66 ? 3.285 23.403 19.620 0.50 19.66 ? 1063 ASP A N 1 ATOM 462 N N B ASP A 1 66 ? 3.327 23.402 19.639 0.50 19.66 ? 1063 ASP A N 1 ATOM 463 C CA A ASP A 1 66 ? 2.675 23.958 20.839 0.50 20.18 ? 1063 ASP A CA 1 ATOM 464 C CA B ASP A 1 66 ? 2.711 24.021 20.802 0.50 20.17 ? 1063 ASP A CA 1 ATOM 465 C C A ASP A 1 66 ? 3.593 23.854 22.058 0.50 19.32 ? 1063 ASP A C 1 ATOM 466 C C B ASP A 1 66 ? 3.489 23.844 22.108 0.50 19.33 ? 1063 ASP A C 1 ATOM 467 O O A ASP A 1 66 ? 4.143 22.787 22.343 0.50 19.24 ? 1063 ASP A O 1 ATOM 468 O O B ASP A 1 66 ? 3.861 22.731 22.482 0.50 19.36 ? 1063 ASP A O 1 ATOM 469 C CB A ASP A 1 66 ? 1.322 23.286 21.135 0.50 20.71 ? 1063 ASP A CB 1 ATOM 470 C CB B ASP A 1 66 ? 1.241 23.622 20.908 0.50 20.69 ? 1063 ASP A CB 1 ATOM 471 C CG A ASP A 1 66 ? 0.621 23.877 22.360 0.50 20.44 ? 1063 ASP A CG 1 ATOM 472 C CG B ASP A 1 66 ? 0.425 24.144 19.737 0.50 20.97 ? 1063 ASP A CG 1 ATOM 473 O OD1 A ASP A 1 66 ? 0.327 25.092 22.362 0.50 21.35 ? 1063 ASP A OD1 1 ATOM 474 O OD1 B ASP A 1 66 ? -0.007 25.316 19.798 0.50 21.49 ? 1063 ASP A OD1 1 ATOM 475 O OD2 A ASP A 1 66 ? 0.346 23.121 23.319 0.50 22.12 ? 1063 ASP A OD2 1 ATOM 476 O OD2 B ASP A 1 66 ? 0.238 23.397 18.749 0.50 21.25 ? 1063 ASP A OD2 1 ATOM 477 N N . LYS A 1 67 ? 3.742 24.967 22.776 1.00 19.06 ? 1064 LYS A N 1 ATOM 478 C CA . LYS A 1 67 ? 4.563 25.007 23.985 1.00 20.33 ? 1064 LYS A CA 1 ATOM 479 C C . LYS A 1 67 ? 3.780 24.632 25.242 1.00 20.33 ? 1064 LYS A C 1 ATOM 480 O O . LYS A 1 67 ? 3.382 25.498 26.032 1.00 22.68 ? 1064 LYS A O 1 ATOM 481 C CB . LYS A 1 67 ? 5.193 26.403 24.141 1.00 21.33 ? 1064 LYS A CB 1 ATOM 482 C CG . LYS A 1 67 ? 6.323 26.480 25.168 1.00 24.80 ? 1064 LYS A CG 1 ATOM 483 C CD . LYS A 1 67 ? 6.808 27.906 25.352 1.00 28.42 ? 1064 LYS A CD 1 ATOM 484 C CE . LYS A 1 67 ? 7.377 28.511 24.061 1.00 31.73 ? 1064 LYS A CE 1 ATOM 485 N NZ . LYS A 1 67 ? 8.621 27.833 23.592 1.00 32.14 ? 1064 LYS A NZ 1 ATOM 486 N N . TYR A 1 68 ? 3.587 23.344 25.450 1.00 18.35 ? 1065 TYR A N 1 ATOM 487 C CA . TYR A 1 68 ? 2.849 22.870 26.617 1.00 17.78 ? 1065 TYR A CA 1 ATOM 488 C C . TYR A 1 68 ? 3.729 22.921 27.867 1.00 18.03 ? 1065 TYR A C 1 ATOM 489 O O . TYR A 1 68 ? 4.970 23.048 27.780 1.00 18.69 ? 1065 TYR A O 1 ATOM 490 C CB . TYR A 1 68 ? 2.283 21.452 26.367 1.00 17.17 ? 1065 TYR A CB 1 ATOM 491 C CG . TYR A 1 68 ? 3.354 20.395 26.276 1.00 16.69 ? 1065 TYR A CG 1 ATOM 492 C CD1 . TYR A 1 68 ? 3.901 19.788 27.413 1.00 16.44 ? 1065 TYR A CD1 1 ATOM 493 C CD2 . TYR A 1 68 ? 3.848 20.001 25.039 1.00 15.81 ? 1065 TYR A CD2 1 ATOM 494 C CE1 . TYR A 1 68 ? 4.900 18.831 27.323 1.00 16.82 ? 1065 TYR A CE1 1 ATOM 495 C CE2 . TYR A 1 68 ? 4.845 19.041 24.940 1.00 15.58 ? 1065 TYR A CE2 1 ATOM 496 C CZ . TYR A 1 68 ? 5.355 18.457 26.073 1.00 16.68 ? 1065 TYR A CZ 1 ATOM 497 O OH . TYR A 1 68 ? 6.364 17.524 25.985 1.00 15.76 ? 1065 TYR A OH 1 ATOM 498 N N . THR A 1 69 ? 3.095 22.781 29.025 1.00 18.93 ? 1066 THR A N 1 ATOM 499 C CA . THR A 1 69 ? 3.788 22.629 30.289 1.00 19.73 ? 1066 THR A CA 1 ATOM 500 C C . THR A 1 69 ? 3.369 21.325 30.965 1.00 18.67 ? 1066 THR A C 1 ATOM 501 O O . THR A 1 69 ? 2.313 20.746 30.639 1.00 19.44 ? 1066 THR A O 1 ATOM 502 C CB . THR A 1 69 ? 3.508 23.811 31.243 1.00 20.54 ? 1066 THR A CB 1 ATOM 503 O OG1 . THR A 1 69 ? 2.105 23.854 31.531 1.00 23.21 ? 1066 THR A OG1 1 ATOM 504 C CG2 . THR A 1 69 ? 3.923 25.135 30.622 1.00 22.66 ? 1066 THR A CG2 1 ATOM 505 N N . LEU A 1 70 ? 4.212 20.864 31.881 1.00 18.09 ? 1067 LEU A N 1 ATOM 506 C CA . LEU A 1 70 ? 3.894 19.777 32.794 1.00 17.24 ? 1067 LEU A CA 1 ATOM 507 C C . LEU A 1 70 ? 4.128 20.305 34.208 1.00 17.92 ? 1067 LEU A C 1 ATOM 508 O O . LEU A 1 70 ? 5.129 19.968 34.852 1.00 19.03 ? 1067 LEU A O 1 ATOM 509 C CB . LEU A 1 70 ? 4.787 18.558 32.509 1.00 17.21 ? 1067 LEU A CB 1 ATOM 510 C CG . LEU A 1 70 ? 4.658 17.945 31.111 1.00 17.52 ? 1067 LEU A CG 1 ATOM 511 C CD1 . LEU A 1 70 ? 5.829 17.004 30.836 1.00 19.69 ? 1067 LEU A CD1 1 ATOM 512 C CD2 . LEU A 1 70 ? 3.318 17.227 30.924 1.00 20.43 ? 1067 LEU A CD2 1 ATOM 513 N N . PRO A 1 71 ? 3.201 21.148 34.688 1.00 18.93 ? 1068 PRO A N 1 ATOM 514 C CA . PRO A 1 71 ? 3.458 21.994 35.860 1.00 19.50 ? 1068 PRO A CA 1 ATOM 515 C C . PRO A 1 71 ? 3.580 21.232 37.172 1.00 19.79 ? 1068 PRO A C 1 ATOM 516 O O . PRO A 1 71 ? 4.112 21.788 38.147 1.00 21.01 ? 1068 PRO A O 1 ATOM 517 C CB . PRO A 1 71 ? 2.237 22.924 35.907 1.00 20.58 ? 1068 PRO A CB 1 ATOM 518 C CG . PRO A 1 71 ? 1.151 22.127 35.259 1.00 20.13 ? 1068 PRO A CG 1 ATOM 519 C CD . PRO A 1 71 ? 1.834 21.345 34.167 1.00 19.31 ? 1068 PRO A CD 1 ATOM 520 N N . ASN A 1 72 ? 3.110 19.987 37.194 1.00 18.75 ? 1069 ASN A N 1 ATOM 521 C CA . ASN A 1 72 ? 3.225 19.168 38.403 1.00 19.53 ? 1069 ASN A CA 1 ATOM 522 C C . ASN A 1 72 ? 4.465 18.281 38.421 1.00 19.72 ? 1069 ASN A C 1 ATOM 523 O O . ASN A 1 72 ? 4.653 17.484 39.327 1.00 21.60 ? 1069 ASN A O 1 ATOM 524 C CB . ASN A 1 72 ? 1.940 18.360 38.556 1.00 19.24 ? 1069 ASN A CB 1 ATOM 525 C CG . ASN A 1 72 ? 0.724 19.271 38.472 1.00 19.35 ? 1069 ASN A CG 1 ATOM 526 O OD1 . ASN A 1 72 ? 0.606 20.199 39.262 1.00 20.67 ? 1069 ASN A OD1 1 ATOM 527 N ND2 . ASN A 1 72 ? -0.148 19.023 37.496 1.00 20.12 ? 1069 ASN A ND2 1 ATOM 528 N N . SER A 1 73 ? 5.340 18.456 37.431 1.00 19.56 ? 1070 SER A N 1 ATOM 529 C CA . SER A 1 73 ? 6.534 17.640 37.251 1.00 19.89 ? 1070 SER A CA 1 ATOM 530 C C . SER A 1 73 ? 7.772 18.520 37.305 1.00 20.04 ? 1070 SER A C 1 ATOM 531 O O . SER A 1 73 ? 7.683 19.712 37.021 1.00 21.05 ? 1070 SER A O 1 ATOM 532 C CB . SER A 1 73 ? 6.454 17.000 35.874 1.00 20.59 ? 1070 SER A CB 1 ATOM 533 O OG . SER A 1 73 ? 7.605 16.285 35.544 1.00 23.24 ? 1070 SER A OG 1 ATOM 534 N N . ASN A 1 74 ? 8.918 17.931 37.632 1.00 19.97 ? 1071 ASN A N 1 ATOM 535 C CA . ASN A 1 74 ? 10.172 18.683 37.614 1.00 20.71 ? 1071 ASN A CA 1 ATOM 536 C C . ASN A 1 74 ? 10.912 18.495 36.294 1.00 19.30 ? 1071 ASN A C 1 ATOM 537 O O . ASN A 1 74 ? 12.077 18.860 36.186 1.00 19.63 ? 1071 ASN A O 1 ATOM 538 C CB . ASN A 1 74 ? 11.065 18.313 38.808 1.00 23.16 ? 1071 ASN A CB 1 ATOM 539 C CG . ASN A 1 74 ? 11.522 16.853 38.787 1.00 28.00 ? 1071 ASN A CG 1 ATOM 540 O OD1 . ASN A 1 74 ? 11.282 16.106 37.835 1.00 31.09 ? 1071 ASN A OD1 1 ATOM 541 N ND2 . ASN A 1 74 ? 12.188 16.439 39.861 1.00 34.74 ? 1071 ASN A ND2 1 ATOM 542 N N . ILE A 1 75 ? 10.237 17.948 35.287 1.00 18.58 ? 1072 ILE A N 1 ATOM 543 C CA . ILE A 1 75 ? 10.858 17.738 33.971 1.00 18.45 ? 1072 ILE A CA 1 ATOM 544 C C . ILE A 1 75 ? 11.157 19.082 33.313 1.00 18.09 ? 1072 ILE A C 1 ATOM 545 O O . ILE A 1 75 ? 10.345 20.009 33.408 1.00 18.64 ? 1072 ILE A O 1 ATOM 546 C CB . ILE A 1 75 ? 9.946 16.887 33.045 1.00 18.39 ? 1072 ILE A CB 1 ATOM 547 C CG1 . ILE A 1 75 ? 9.886 15.440 33.545 1.00 19.83 ? 1072 ILE A CG1 1 ATOM 548 C CG2 . ILE A 1 75 ? 10.395 16.977 31.586 1.00 19.49 ? 1072 ILE A CG2 1 ATOM 549 C CD1 . ILE A 1 75 ? 8.786 14.599 32.902 1.00 20.79 ? 1072 ILE A CD1 1 ATOM 550 N N . ASN A 1 76 ? 12.334 19.197 32.684 1.00 18.03 ? 1073 ASN A N 1 ATOM 551 C CA . ASN A 1 76 ? 12.642 20.377 31.885 1.00 18.87 ? 1073 ASN A CA 1 ATOM 552 C C . ASN A 1 76 ? 12.234 20.088 30.456 1.00 17.25 ? 1073 ASN A C 1 ATOM 553 O O . ASN A 1 76 ? 12.747 19.141 29.855 1.00 16.70 ? 1073 ASN A O 1 ATOM 554 C CB . ASN A 1 76 ? 14.135 20.705 31.938 1.00 20.97 ? 1073 ASN A CB 1 ATOM 555 C CG . ASN A 1 76 ? 14.515 22.007 31.235 1.00 27.48 ? 1073 ASN A CG 1 ATOM 556 O OD1 . ASN A 1 76 ? 13.932 22.404 30.227 1.00 33.59 ? 1073 ASN A OD1 1 ATOM 557 N ND2 . ASN A 1 76 ? 15.531 22.680 31.771 1.00 34.28 ? 1073 ASN A ND2 1 ATOM 558 N N . ILE A 1 77 ? 11.289 20.891 29.946 1.00 16.39 ? 1074 ILE A N 1 ATOM 559 C CA . ILE A 1 77 ? 10.748 20.698 28.598 1.00 16.22 ? 1074 ILE A CA 1 ATOM 560 C C . ILE A 1 77 ? 11.443 21.684 27.647 1.00 15.84 ? 1074 ILE A C 1 ATOM 561 O O . ILE A 1 77 ? 11.278 22.905 27.773 1.00 17.92 ? 1074 ILE A O 1 ATOM 562 C CB . ILE A 1 77 ? 9.212 20.889 28.528 1.00 16.35 ? 1074 ILE A CB 1 ATOM 563 C CG1 . ILE A 1 77 ? 8.504 20.010 29.556 1.00 19.34 ? 1074 ILE A CG1 1 ATOM 564 C CG2 . ILE A 1 77 ? 8.705 20.596 27.116 1.00 17.44 ? 1074 ILE A CG2 1 ATOM 565 C CD1 . ILE A 1 77 ? 7.134 20.499 29.937 1.00 20.62 ? 1074 ILE A CD1 1 ATOM 566 N N . ILE A 1 78 ? 12.226 21.138 26.724 1.00 15.47 ? 1075 ILE A N 1 ATOM 567 C CA . ILE A 1 78 ? 12.890 21.944 25.714 1.00 16.32 ? 1075 ILE A CA 1 ATOM 568 C C . ILE A 1 78 ? 12.022 21.974 24.468 1.00 15.17 ? 1075 ILE A C 1 ATOM 569 O O . ILE A 1 78 ? 11.664 20.929 23.926 1.00 15.96 ? 1075 ILE A O 1 ATOM 570 C CB . ILE A 1 78 ? 14.263 21.359 25.362 1.00 17.27 ? 1075 ILE A CB 1 ATOM 571 C CG1 . ILE A 1 78 ? 15.135 21.280 26.617 1.00 21.44 ? 1075 ILE A CG1 1 ATOM 572 C CG2 . ILE A 1 78 ? 14.939 22.197 24.279 1.00 18.95 ? 1075 ILE A CG2 1 ATOM 573 C CD1 . ILE A 1 78 ? 16.016 20.067 26.649 1.00 28.66 ? 1075 ILE A CD1 1 ATOM 574 N N . HIS A 1 79 ? 11.676 23.178 24.029 1.00 15.63 ? 1076 HIS A N 1 ATOM 575 C CA . HIS A 1 79 ? 10.763 23.335 22.910 1.00 15.70 ? 1076 HIS A CA 1 ATOM 576 C C . HIS A 1 79 ? 11.518 23.741 21.653 1.00 15.26 ? 1076 HIS A C 1 ATOM 577 O O . HIS A 1 79 ? 12.110 24.825 21.595 1.00 16.59 ? 1076 HIS A O 1 ATOM 578 C CB . HIS A 1 79 ? 9.696 24.374 23.237 1.00 15.76 ? 1076 HIS A CB 1 ATOM 579 C CG . HIS A 1 79 ? 8.581 24.421 22.242 1.00 16.39 ? 1076 HIS A CG 1 ATOM 580 N ND1 . HIS A 1 79 ? 7.802 25.542 22.048 1.00 17.73 ? 1076 HIS A ND1 1 ATOM 581 C CD2 . HIS A 1 79 ? 8.119 23.487 21.377 1.00 16.39 ? 1076 HIS A CD2 1 ATOM 582 C CE1 . HIS A 1 79 ? 6.896 25.292 21.119 1.00 17.83 ? 1076 HIS A CE1 1 ATOM 583 N NE2 . HIS A 1 79 ? 7.059 24.049 20.703 1.00 17.25 ? 1076 HIS A NE2 1 ATOM 584 N N . ILE A 1 80 ? 11.493 22.863 20.655 1.00 14.82 ? 1077 ILE A N 1 ATOM 585 C CA . ILE A 1 80 ? 11.993 23.202 19.323 1.00 16.72 ? 1077 ILE A CA 1 ATOM 586 C C . ILE A 1 80 ? 10.830 23.020 18.348 1.00 15.59 ? 1077 ILE A C 1 ATOM 587 O O . ILE A 1 80 ? 10.599 21.919 17.855 1.00 15.56 ? 1077 ILE A O 1 ATOM 588 C CB . ILE A 1 80 ? 13.187 22.317 18.901 1.00 18.44 ? 1077 ILE A CB 1 ATOM 589 C CG1 . ILE A 1 80 ? 14.331 22.416 19.921 1.00 21.16 ? 1077 ILE A CG1 1 ATOM 590 C CG2 . ILE A 1 80 ? 13.669 22.724 17.520 1.00 20.81 ? 1077 ILE A CG2 1 ATOM 591 C CD1 . ILE A 1 80 ? 15.527 21.532 19.603 1.00 24.35 ? 1077 ILE A CD1 1 ATOM 592 N N . PRO A 1 81 ? 10.082 24.097 18.092 1.00 16.61 ? 1078 PRO A N 1 ATOM 593 C CA . PRO A 1 81 ? 8.858 23.954 17.294 1.00 17.29 ? 1078 PRO A CA 1 ATOM 594 C C . PRO A 1 81 ? 9.158 23.680 15.827 1.00 17.59 ? 1078 PRO A C 1 ATOM 595 O O . PRO A 1 81 ? 9.865 24.470 15.185 1.00 19.28 ? 1078 PRO A O 1 ATOM 596 C CB . PRO A 1 81 ? 8.152 25.297 17.468 1.00 17.97 ? 1078 PRO A CB 1 ATOM 597 C CG . PRO A 1 81 ? 9.180 26.247 17.960 1.00 17.19 ? 1078 PRO A CG 1 ATOM 598 C CD . PRO A 1 81 ? 10.226 25.437 18.670 1.00 17.06 ? 1078 PRO A CD 1 ATOM 599 N N . LEU A 1 82 ? 8.650 22.554 15.332 1.00 15.63 ? 1079 LEU A N 1 ATOM 600 C CA . LEU A 1 82 ? 8.786 22.173 13.933 1.00 16.17 ? 1079 LEU A CA 1 ATOM 601 C C . LEU A 1 82 ? 7.425 21.774 13.397 1.00 15.33 ? 1079 LEU A C 1 ATOM 602 O O . LEU A 1 82 ? 6.560 21.348 14.157 1.00 16.02 ? 1079 LEU A O 1 ATOM 603 C CB . LEU A 1 82 ? 9.734 20.984 13.794 1.00 16.49 ? 1079 LEU A CB 1 ATOM 604 C CG . LEU A 1 82 ? 11.161 21.187 14.290 1.00 18.33 ? 1079 LEU A CG 1 ATOM 605 C CD1 . LEU A 1 82 ? 11.847 19.837 14.402 1.00 19.45 ? 1079 LEU A CD1 1 ATOM 606 C CD2 . LEU A 1 82 ? 11.901 22.100 13.329 1.00 21.85 ? 1079 LEU A CD2 1 ATOM 607 N N . VAL A 1 83 ? 7.263 21.904 12.085 1.00 15.82 ? 1080 VAL A N 1 ATOM 608 C CA . VAL A 1 83 ? 6.085 21.383 11.388 1.00 16.27 ? 1080 VAL A CA 1 ATOM 609 C C . VAL A 1 83 ? 6.434 20.090 10.640 1.00 15.97 ? 1080 VAL A C 1 ATOM 610 O O . VAL A 1 83 ? 7.499 19.969 10.028 1.00 17.00 ? 1080 VAL A O 1 ATOM 611 C CB . VAL A 1 83 ? 5.481 22.418 10.409 1.00 17.46 ? 1080 VAL A CB 1 ATOM 612 C CG1 . VAL A 1 83 ? 4.240 21.846 9.737 1.00 19.03 ? 1080 VAL A CG1 1 ATOM 613 C CG2 . VAL A 1 83 ? 5.111 23.710 11.135 1.00 19.43 ? 1080 VAL A CG2 1 ATOM 614 N N . ASP A 1 84 ? 5.539 19.107 10.674 1.00 15.65 ? 1081 ASP A N 1 ATOM 615 C CA . ASP A 1 84 ? 5.693 17.888 9.883 1.00 15.85 ? 1081 ASP A CA 1 ATOM 616 C C . ASP A 1 84 ? 5.130 18.142 8.492 1.00 17.12 ? 1081 ASP A C 1 ATOM 617 O O . ASP A 1 84 ? 3.948 17.885 8.230 1.00 18.48 ? 1081 ASP A O 1 ATOM 618 C CB . ASP A 1 84 ? 5.002 16.702 10.554 1.00 15.96 ? 1081 ASP A CB 1 ATOM 619 C CG . ASP A 1 84 ? 5.144 15.409 9.770 1.00 15.78 ? 1081 ASP A CG 1 ATOM 620 O OD1 . ASP A 1 84 ? 6.001 15.325 8.835 1.00 17.87 ? 1081 ASP A OD1 1 ATOM 621 O OD2 . ASP A 1 84 ? 4.441 14.435 10.120 1.00 17.70 ? 1081 ASP A OD2 1 ATOM 622 N N . ASP A 1 85 ? 5.949 18.697 7.611 1.00 18.82 ? 1082 ASP A N 1 ATOM 623 C CA . ASP A 1 85 ? 5.527 18.915 6.236 1.00 22.20 ? 1082 ASP A CA 1 ATOM 624 C C . ASP A 1 85 ? 6.715 18.741 5.312 1.00 23.91 ? 1082 ASP A C 1 ATOM 625 O O . ASP A 1 85 ? 7.840 18.548 5.771 1.00 22.05 ? 1082 ASP A O 1 ATOM 626 C CB . ASP A 1 85 ? 4.906 20.304 6.064 1.00 24.70 ? 1082 ASP A CB 1 ATOM 627 C CG . ASP A 1 85 ? 5.907 21.423 6.272 1.00 28.61 ? 1082 ASP A CG 1 ATOM 628 O OD1 . ASP A 1 85 ? 7.116 21.187 6.077 1.00 32.19 ? 1082 ASP A OD1 1 ATOM 629 O OD2 . ASP A 1 85 ? 5.484 22.542 6.630 1.00 32.66 ? 1082 ASP A OD2 1 ATOM 630 N N . THR A 1 86 ? 6.470 18.787 4.010 1.00 28.33 ? 1083 THR A N 1 ATOM 631 C CA . THR A 1 86 ? 7.529 18.440 3.066 1.00 32.64 ? 1083 THR A CA 1 ATOM 632 C C . THR A 1 86 ? 8.364 19.672 2.674 1.00 33.91 ? 1083 THR A C 1 ATOM 633 O O . THR A 1 86 ? 9.265 19.568 1.836 1.00 34.76 ? 1083 THR A O 1 ATOM 634 C CB . THR A 1 86 ? 6.991 17.650 1.846 1.00 33.50 ? 1083 THR A CB 1 ATOM 635 O OG1 . THR A 1 86 ? 5.870 18.328 1.284 1.00 34.07 ? 1083 THR A OG1 1 ATOM 636 C CG2 . THR A 1 86 ? 6.532 16.253 2.278 1.00 35.03 ? 1083 THR A CG2 1 ATOM 637 N N . THR A 1 87 ? 8.108 20.804 3.339 1.00 36.15 ? 1084 THR A N 1 ATOM 638 C CA . THR A 1 87 ? 8.807 22.071 3.073 1.00 38.29 ? 1084 THR A CA 1 ATOM 639 C C . THR A 1 87 ? 9.799 22.536 4.169 1.00 36.95 ? 1084 THR A C 1 ATOM 640 O O . THR A 1 87 ? 10.773 23.229 3.871 1.00 38.69 ? 1084 THR A O 1 ATOM 641 C CB . THR A 1 87 ? 7.802 23.206 2.702 1.00 39.78 ? 1084 THR A CB 1 ATOM 642 O OG1 . THR A 1 87 ? 8.376 24.055 1.699 1.00 41.75 ? 1084 THR A OG1 1 ATOM 643 C CG2 . THR A 1 87 ? 7.408 24.039 3.927 1.00 39.99 ? 1084 THR A CG2 1 ATOM 644 N N . THR A 1 88 ? 9.582 22.110 5.411 1.00 33.95 ? 1085 THR A N 1 ATOM 645 C CA . THR A 1 88 ? 10.409 22.547 6.541 1.00 30.96 ? 1085 THR A CA 1 ATOM 646 C C . THR A 1 88 ? 11.836 21.992 6.512 1.00 27.45 ? 1085 THR A C 1 ATOM 647 O O . THR A 1 88 ? 12.042 20.815 6.228 1.00 26.52 ? 1085 THR A O 1 ATOM 648 C CB . THR A 1 88 ? 9.769 22.156 7.889 1.00 32.57 ? 1085 THR A CB 1 ATOM 649 O OG1 . THR A 1 88 ? 8.697 23.056 8.191 1.00 34.81 ? 1085 THR A OG1 1 ATOM 650 C CG2 . THR A 1 88 ? 10.799 22.206 9.009 1.00 33.37 ? 1085 THR A CG2 1 ATOM 651 N N A ASP A 1 89 ? 12.783 22.838 6.500 0.50 26.21 ? 1086 ASP A N 1 ATOM 652 N N B ASP A 1 89 ? 12.812 22.844 6.827 0.50 26.36 ? 1086 ASP A N 1 ATOM 653 C CA A ASP A 1 89 ? 14.099 22.434 6.969 0.50 24.01 ? 1086 ASP A CA 1 ATOM 654 C CA B ASP A 1 89 ? 14.211 22.424 6.927 0.50 24.42 ? 1086 ASP A CA 1 ATOM 655 C C A ASP A 1 89 ? 14.021 21.979 8.419 0.50 21.54 ? 1086 ASP A C 1 ATOM 656 C C B ASP A 1 89 ? 14.615 22.031 8.345 0.50 22.57 ? 1086 ASP A C 1 ATOM 657 O O A ASP A 1 89 ? 13.553 22.715 9.288 0.50 19.63 ? 1086 ASP A O 1 ATOM 658 O O B ASP A 1 89 ? 15.071 22.866 9.127 0.50 22.27 ? 1086 ASP A O 1 ATOM 659 C CB A ASP A 1 89 ? 15.106 23.575 6.822 0.50 25.56 ? 1086 ASP A CB 1 ATOM 660 C CB B ASP A 1 89 ? 15.152 23.521 6.427 0.50 25.52 ? 1086 ASP A CB 1 ATOM 661 C CG A ASP A 1 89 ? 16.498 23.182 7.267 0.50 27.04 ? 1086 ASP A CG 1 ATOM 662 C CG B ASP A 1 89 ? 16.612 23.218 6.730 0.50 25.97 ? 1086 ASP A CG 1 ATOM 663 O OD1 A ASP A 1 89 ? 17.026 23.821 8.198 0.50 29.52 ? 1086 ASP A OD1 1 ATOM 664 O OD1 B ASP A 1 89 ? 16.981 22.027 6.745 0.50 27.24 ? 1086 ASP A OD1 1 ATOM 665 O OD2 A ASP A 1 89 ? 17.061 22.229 6.691 0.50 29.27 ? 1086 ASP A OD2 1 ATOM 666 O OD2 B ASP A 1 89 ? 17.392 24.168 6.950 0.50 26.62 ? 1086 ASP A OD2 1 ATOM 667 N N . ILE A 1 90 ? 14.467 20.754 8.667 1.00 18.79 ? 1087 ILE A N 1 ATOM 668 C CA . ILE A 1 90 ? 14.739 20.281 10.026 1.00 17.74 ? 1087 ILE A CA 1 ATOM 669 C C . ILE A 1 90 ? 16.247 20.152 10.237 1.00 16.48 ? 1087 ILE A C 1 ATOM 670 O O . ILE A 1 90 ? 16.716 20.108 11.374 1.00 16.21 ? 1087 ILE A O 1 ATOM 671 C CB . ILE A 1 90 ? 14.003 18.962 10.338 1.00 18.11 ? 1087 ILE A CB 1 ATOM 672 C CG1 . ILE A 1 90 ? 14.447 17.827 9.405 1.00 18.88 ? 1087 ILE A CG1 1 ATOM 673 C CG2 . ILE A 1 90 ? 12.491 19.197 10.325 1.00 20.90 ? 1087 ILE A CG2 1 ATOM 674 C CD1 . ILE A 1 90 ? 14.136 16.452 9.960 1.00 22.96 ? 1087 ILE A CD1 1 ATOM 675 N N . SER A 1 91 ? 17.000 20.104 9.135 1.00 17.09 ? 1088 SER A N 1 ATOM 676 C CA . SER A 1 91 ? 18.441 19.878 9.226 1.00 18.12 ? 1088 SER A CA 1 ATOM 677 C C . SER A 1 91 ? 19.154 21.004 9.972 1.00 17.58 ? 1088 SER A C 1 ATOM 678 O O . SER A 1 91 ? 20.217 20.756 10.538 1.00 17.77 ? 1088 SER A O 1 ATOM 679 C CB . SER A 1 91 ? 19.043 19.685 7.830 1.00 18.83 ? 1088 SER A CB 1 ATOM 680 O OG . SER A 1 91 ? 19.201 20.918 7.159 1.00 23.03 ? 1088 SER A OG 1 ATOM 681 N N . LYS A 1 92 ? 18.577 22.211 10.002 1.00 17.93 ? 1089 LYS A N 1 ATOM 682 C CA . LYS A 1 92 ? 19.216 23.331 10.719 1.00 19.03 ? 1089 LYS A CA 1 ATOM 683 C C . LYS A 1 92 ? 19.460 23.020 12.200 1.00 17.34 ? 1089 LYS A C 1 ATOM 684 O O . LYS A 1 92 ? 20.329 23.640 12.827 1.00 18.54 ? 1089 LYS A O 1 ATOM 685 C CB . LYS A 1 92 ? 18.421 24.643 10.570 1.00 20.47 ? 1089 LYS A CB 1 ATOM 686 C CG . LYS A 1 92 ? 17.061 24.659 11.240 1.00 25.29 ? 1089 LYS A CG 1 ATOM 687 C CD . LYS A 1 92 ? 16.360 26.017 11.138 1.00 32.49 ? 1089 LYS A CD 1 ATOM 688 C CE . LYS A 1 92 ? 15.317 26.050 10.037 1.00 36.94 ? 1089 LYS A CE 1 ATOM 689 N NZ . LYS A 1 92 ? 15.813 26.660 8.765 1.00 38.74 ? 1089 LYS A NZ 1 ATOM 690 N N . TYR A 1 93 ? 18.706 22.074 12.759 1.00 16.07 ? 1090 TYR A N 1 ATOM 691 C CA . TYR A 1 93 ? 18.829 21.728 14.176 1.00 15.20 ? 1090 TYR A CA 1 ATOM 692 C C . TYR A 1 93 ? 19.570 20.429 14.448 1.00 14.36 ? 1090 TYR A C 1 ATOM 693 O O . TYR A 1 93 ? 19.777 20.088 15.608 1.00 15.13 ? 1090 TYR A O 1 ATOM 694 C CB . TYR A 1 93 ? 17.428 21.612 14.808 1.00 16.74 ? 1090 TYR A CB 1 ATOM 695 C CG . TYR A 1 93 ? 16.603 22.867 14.683 1.00 20.77 ? 1090 TYR A CG 1 ATOM 696 C CD1 . TYR A 1 93 ? 16.870 23.985 15.465 1.00 26.44 ? 1090 TYR A CD1 1 ATOM 697 C CD2 . TYR A 1 93 ? 15.531 22.934 13.783 1.00 24.91 ? 1090 TYR A CD2 1 ATOM 698 C CE1 . TYR A 1 93 ? 16.095 25.148 15.356 1.00 29.65 ? 1090 TYR A CE1 1 ATOM 699 C CE2 . TYR A 1 93 ? 14.758 24.087 13.666 1.00 27.88 ? 1090 TYR A CE2 1 ATOM 700 C CZ . TYR A 1 93 ? 15.038 25.184 14.458 1.00 29.45 ? 1090 TYR A CZ 1 ATOM 701 O OH . TYR A 1 93 ? 14.291 26.325 14.330 1.00 33.81 ? 1090 TYR A OH 1 ATOM 702 N N . PHE A 1 94 ? 19.977 19.687 13.409 1.00 14.51 ? 1091 PHE A N 1 ATOM 703 C CA . PHE A 1 94 ? 20.632 18.396 13.637 1.00 15.09 ? 1091 PHE A CA 1 ATOM 704 C C . PHE A 1 94 ? 21.870 18.495 14.548 1.00 16.11 ? 1091 PHE A C 1 ATOM 705 O O . PHE A 1 94 ? 22.010 17.716 15.488 1.00 16.38 ? 1091 PHE A O 1 ATOM 706 C CB . PHE A 1 94 ? 21.050 17.745 12.320 1.00 15.88 ? 1091 PHE A CB 1 ATOM 707 C CG . PHE A 1 94 ? 19.915 17.161 11.496 1.00 15.26 ? 1091 PHE A CG 1 ATOM 708 C CD1 . PHE A 1 94 ? 18.665 16.863 12.038 1.00 16.77 ? 1091 PHE A CD1 1 ATOM 709 C CD2 . PHE A 1 94 ? 20.139 16.892 10.139 1.00 18.25 ? 1091 PHE A CD2 1 ATOM 710 C CE1 . PHE A 1 94 ? 17.653 16.300 11.234 1.00 16.67 ? 1091 PHE A CE1 1 ATOM 711 C CE2 . PHE A 1 94 ? 19.148 16.342 9.331 1.00 19.29 ? 1091 PHE A CE2 1 ATOM 712 C CZ . PHE A 1 94 ? 17.894 16.049 9.883 1.00 19.54 ? 1091 PHE A CZ 1 ATOM 713 N N . ASP A 1 95 ? 22.770 19.437 14.269 1.00 17.24 ? 1092 ASP A N 1 ATOM 714 C CA . ASP A 1 95 ? 23.997 19.491 15.066 1.00 18.86 ? 1092 ASP A CA 1 ATOM 715 C C . ASP A 1 95 ? 23.732 19.721 16.553 1.00 18.20 ? 1092 ASP A C 1 ATOM 716 O O . ASP A 1 95 ? 24.244 18.996 17.418 1.00 18.52 ? 1092 ASP A O 1 ATOM 717 C CB . ASP A 1 95 ? 24.938 20.556 14.514 1.00 19.74 ? 1092 ASP A CB 1 ATOM 718 C CG . ASP A 1 95 ? 25.602 20.148 13.215 1.00 23.75 ? 1092 ASP A CG 1 ATOM 719 O OD1 . ASP A 1 95 ? 25.514 18.966 12.822 1.00 28.53 ? 1092 ASP A OD1 1 ATOM 720 O OD2 . ASP A 1 95 ? 26.223 21.021 12.571 1.00 29.05 ? 1092 ASP A OD2 1 ATOM 721 N N . ASP A 1 96 ? 22.912 20.717 16.879 1.00 17.96 ? 1093 ASP A N 1 ATOM 722 C CA . ASP A 1 96 ? 22.655 21.023 18.285 1.00 18.55 ? 1093 ASP A CA 1 ATOM 723 C C . ASP A 1 96 ? 21.803 19.958 18.970 1.00 16.11 ? 1093 ASP A C 1 ATOM 724 O O . ASP A 1 96 ? 21.999 19.655 20.143 1.00 16.72 ? 1093 ASP A O 1 ATOM 725 C CB . ASP A 1 96 ? 22.037 22.413 18.442 1.00 21.11 ? 1093 ASP A CB 1 ATOM 726 C CG . ASP A 1 96 ? 23.070 23.530 18.276 1.00 26.65 ? 1093 ASP A CG 1 ATOM 727 O OD1 . ASP A 1 96 ? 24.271 23.243 18.064 1.00 30.59 ? 1093 ASP A OD1 1 ATOM 728 O OD2 . ASP A 1 96 ? 22.672 24.707 18.364 1.00 32.41 ? 1093 ASP A OD2 1 ATOM 729 N N . VAL A 1 97 ? 20.841 19.377 18.252 1.00 15.26 ? 1094 VAL A N 1 ATOM 730 C CA . VAL A 1 97 ? 20.019 18.331 18.869 1.00 15.15 ? 1094 VAL A CA 1 ATOM 731 C C . VAL A 1 97 ? 20.870 17.093 19.164 1.00 14.88 ? 1094 VAL A C 1 ATOM 732 O O . VAL A 1 97 ? 20.816 16.544 20.260 1.00 15.72 ? 1094 VAL A O 1 ATOM 733 C CB . VAL A 1 97 ? 18.769 17.970 18.036 1.00 15.00 ? 1094 VAL A CB 1 ATOM 734 C CG1 . VAL A 1 97 ? 18.101 16.693 18.567 1.00 15.18 ? 1094 VAL A CG1 1 ATOM 735 C CG2 . VAL A 1 97 ? 17.785 19.140 18.053 1.00 15.64 ? 1094 VAL A CG2 1 ATOM 736 N N . THR A 1 98 ? 21.669 16.659 18.189 1.00 15.56 ? 1095 THR A N 1 ATOM 737 C CA . THR A 1 98 ? 22.445 15.446 18.403 1.00 16.87 ? 1095 THR A CA 1 ATOM 738 C C . THR A 1 98 ? 23.516 15.664 19.492 1.00 17.67 ? 1095 THR A C 1 ATOM 739 O O . THR A 1 98 ? 23.776 14.753 20.276 1.00 18.54 ? 1095 THR A O 1 ATOM 740 C CB . THR A 1 98 ? 23.109 14.920 17.100 1.00 16.88 ? 1095 THR A CB 1 ATOM 741 O OG1 . THR A 1 98 ? 24.003 15.902 16.564 1.00 18.21 ? 1095 THR A OG1 1 ATOM 742 C CG2 . THR A 1 98 ? 22.027 14.618 16.059 1.00 17.33 ? 1095 THR A CG2 1 ATOM 743 N N . ALA A 1 99 ? 24.074 16.866 19.593 1.00 18.34 ? 1096 ALA A N 1 ATOM 744 C CA . ALA A 1 99 ? 25.042 17.155 20.665 1.00 19.03 ? 1096 ALA A CA 1 ATOM 745 C C . ALA A 1 99 ? 24.346 17.106 22.029 1.00 19.09 ? 1096 ALA A C 1 ATOM 746 O O . ALA A 1 99 ? 24.883 16.601 23.013 1.00 20.48 ? 1096 ALA A O 1 ATOM 747 C CB . ALA A 1 99 ? 25.683 18.506 20.441 1.00 19.92 ? 1096 ALA A CB 1 ATOM 748 N N . PHE A 1 100 ? 23.109 17.603 22.086 1.00 18.08 ? 1097 PHE A N 1 ATOM 749 C CA . PHE A 1 100 ? 22.359 17.580 23.330 1.00 17.92 ? 1097 PHE A CA 1 ATOM 750 C C . PHE A 1 100 ? 21.999 16.149 23.740 1.00 17.23 ? 1097 PHE A C 1 ATOM 751 O O . PHE A 1 100 ? 22.147 15.763 24.910 1.00 17.79 ? 1097 PHE A O 1 ATOM 752 C CB . PHE A 1 100 ? 21.102 18.451 23.205 1.00 17.87 ? 1097 PHE A CB 1 ATOM 753 C CG . PHE A 1 100 ? 20.082 18.217 24.299 1.00 20.56 ? 1097 PHE A CG 1 ATOM 754 C CD1 . PHE A 1 100 ? 20.363 18.555 25.618 1.00 25.57 ? 1097 PHE A CD1 1 ATOM 755 C CD2 . PHE A 1 100 ? 18.835 17.662 23.984 1.00 22.53 ? 1097 PHE A CD2 1 ATOM 756 C CE1 . PHE A 1 100 ? 19.405 18.341 26.623 1.00 27.35 ? 1097 PHE A CE1 1 ATOM 757 C CE2 . PHE A 1 100 ? 17.888 17.435 24.986 1.00 26.57 ? 1097 PHE A CE2 1 ATOM 758 C CZ . PHE A 1 100 ? 18.181 17.768 26.304 1.00 27.36 ? 1097 PHE A CZ 1 ATOM 759 N N . LEU A 1 101 ? 21.533 15.359 22.776 1.00 16.50 ? 1098 LEU A N 1 ATOM 760 C CA . LEU A 1 101 ? 21.228 13.955 23.080 1.00 16.83 ? 1098 LEU A CA 1 ATOM 761 C C . LEU A 1 101 ? 22.488 13.177 23.527 1.00 18.22 ? 1098 LEU A C 1 ATOM 762 O O . LEU A 1 101 ? 22.408 12.380 24.456 1.00 19.00 ? 1098 LEU A O 1 ATOM 763 C CB . LEU A 1 101 ? 20.547 13.305 21.889 1.00 16.18 ? 1098 LEU A CB 1 ATOM 764 C CG . LEU A 1 101 ? 19.162 13.897 21.579 1.00 15.12 ? 1098 LEU A CG 1 ATOM 765 C CD1 . LEU A 1 101 ? 18.617 13.198 20.353 1.00 15.30 ? 1098 LEU A CD1 1 ATOM 766 C CD2 . LEU A 1 101 ? 18.193 13.795 22.779 1.00 15.28 ? 1098 LEU A CD2 1 ATOM 767 N N A SER A 1 102 ? 23.627 13.424 22.880 0.50 19.83 ? 1099 SER A N 1 ATOM 768 N N B SER A 1 102 ? 23.621 13.422 22.870 0.50 19.58 ? 1099 SER A N 1 ATOM 769 C CA A SER A 1 102 ? 24.885 12.804 23.277 0.50 21.42 ? 1099 SER A CA 1 ATOM 770 C CA B SER A 1 102 ? 24.877 12.809 23.267 0.50 20.62 ? 1099 SER A CA 1 ATOM 771 C C A SER A 1 102 ? 25.260 13.144 24.714 0.50 21.63 ? 1099 SER A C 1 ATOM 772 C C B SER A 1 102 ? 25.208 13.129 24.723 0.50 21.26 ? 1099 SER A C 1 ATOM 773 O O A SER A 1 102 ? 25.777 12.300 25.446 0.50 22.48 ? 1099 SER A O 1 ATOM 774 O O B SER A 1 102 ? 25.634 12.256 25.479 0.50 22.31 ? 1099 SER A O 1 ATOM 775 C CB A SER A 1 102 ? 25.970 13.256 22.315 0.50 21.97 ? 1099 SER A CB 1 ATOM 776 C CB B SER A 1 102 ? 25.975 13.310 22.341 0.50 20.68 ? 1099 SER A CB 1 ATOM 777 O OG A SER A 1 102 ? 25.861 12.537 21.101 0.50 24.89 ? 1099 SER A OG 1 ATOM 778 O OG B SER A 1 102 ? 27.217 12.741 22.718 0.50 20.67 ? 1099 SER A OG 1 ATOM 779 N N . LYS A 1 103 ? 24.994 14.382 25.117 1.00 21.75 ? 1100 LYS A N 1 ATOM 780 C CA . LYS A 1 103 ? 25.268 14.835 26.479 1.00 23.27 ? 1100 LYS A CA 1 ATOM 781 C C . LYS A 1 103 ? 24.335 14.143 27.474 1.00 22.89 ? 1100 LYS A C 1 ATOM 782 O O . LYS A 1 103 ? 24.761 13.751 28.564 1.00 24.04 ? 1100 LYS A O 1 ATOM 783 C CB . LYS A 1 103 ? 25.190 16.361 26.550 1.00 24.45 ? 1100 LYS A CB 1 ATOM 784 C CG . LYS A 1 103 ? 25.571 16.991 27.882 1.00 29.27 ? 1100 LYS A CG 1 ATOM 785 C CD . LYS A 1 103 ? 25.968 18.456 27.705 1.00 36.42 ? 1100 LYS A CD 1 ATOM 786 C CE . LYS A 1 103 ? 24.790 19.421 27.798 1.00 40.63 ? 1100 LYS A CE 1 ATOM 787 N NZ . LYS A 1 103 ? 23.813 19.245 26.686 1.00 44.34 ? 1100 LYS A NZ 1 ATOM 788 N N . CYS A 1 104 ? 23.062 13.965 27.101 1.00 22.32 ? 1101 CYS A N 1 ATOM 789 C CA . CYS A 1 104 ? 22.146 13.223 27.965 1.00 21.76 ? 1101 CYS A CA 1 ATOM 790 C C . CYS A 1 104 ? 22.649 11.795 28.202 1.00 23.32 ? 1101 CYS A C 1 ATOM 791 O O . CYS A 1 104 ? 22.616 11.296 29.331 1.00 24.32 ? 1101 CYS A O 1 ATOM 792 C CB . CYS A 1 104 ? 20.750 13.209 27.368 1.00 21.30 ? 1101 CYS A CB 1 ATOM 793 S SG . CYS A 1 104 ? 19.951 14.828 27.403 1.00 20.73 ? 1101 CYS A SG 1 ATOM 794 N N . ASP A 1 105 ? 23.143 11.152 27.146 1.00 25.12 ? 1102 ASP A N 1 ATOM 795 C CA . ASP A 1 105 ? 23.702 9.807 27.299 1.00 26.89 ? 1102 ASP A CA 1 ATOM 796 C C . ASP A 1 105 ? 24.986 9.774 28.138 1.00 28.63 ? 1102 ASP A C 1 ATOM 797 O O . ASP A 1 105 ? 25.195 8.847 28.919 1.00 29.89 ? 1102 ASP A O 1 ATOM 798 C CB . ASP A 1 105 ? 23.899 9.138 25.926 1.00 26.74 ? 1102 ASP A CB 1 ATOM 799 C CG . ASP A 1 105 ? 22.729 8.239 25.535 1.00 27.50 ? 1102 ASP A CG 1 ATOM 800 O OD1 . ASP A 1 105 ? 22.398 8.148 24.330 1.00 26.64 ? 1102 ASP A OD1 1 ATOM 801 O OD2 . ASP A 1 105 ? 22.150 7.594 26.442 1.00 28.08 ? 1102 ASP A OD2 1 ATOM 802 N N . GLN A 1 106 ? 25.827 10.795 27.992 1.00 29.62 ? 1103 GLN A N 1 ATOM 803 C CA . GLN A 1 106 ? 27.069 10.883 28.771 1.00 32.70 ? 1103 GLN A CA 1 ATOM 804 C C . GLN A 1 106 ? 26.765 11.063 30.259 1.00 32.82 ? 1103 GLN A C 1 ATOM 805 O O . GLN A 1 106 ? 27.431 10.483 31.115 1.00 33.98 ? 1103 GLN A O 1 ATOM 806 C CB . GLN A 1 106 ? 27.926 12.054 28.285 1.00 33.30 ? 1103 GLN A CB 1 ATOM 807 C CG . GLN A 1 106 ? 28.528 11.886 26.902 1.00 40.41 ? 1103 GLN A CG 1 ATOM 808 C CD . GLN A 1 106 ? 29.079 13.191 26.346 1.00 46.96 ? 1103 GLN A CD 1 ATOM 809 O OE1 . GLN A 1 106 ? 30.064 13.729 26.855 1.00 49.68 ? 1103 GLN A OE1 1 ATOM 810 N NE2 . GLN A 1 106 ? 28.442 13.705 25.297 1.00 49.86 ? 1103 GLN A NE2 1 ATOM 811 N N . ARG A 1 107 ? 25.754 11.877 30.547 1.00 33.01 ? 1104 ARG A N 1 ATOM 812 C CA . ARG A 1 107 ? 25.420 12.254 31.916 1.00 32.86 ? 1104 ARG A CA 1 ATOM 813 C C . ARG A 1 107 ? 24.373 11.354 32.577 1.00 32.77 ? 1104 ARG A C 1 ATOM 814 O O . ARG A 1 107 ? 24.023 11.562 33.745 1.00 33.11 ? 1104 ARG A O 1 ATOM 815 C CB . ARG A 1 107 ? 24.952 13.718 31.964 1.00 32.85 ? 1104 ARG A CB 1 ATOM 816 C CG . ARG A 1 107 ? 25.995 14.730 31.517 1.00 34.68 ? 1104 ARG A CG 1 ATOM 817 C CD . ARG A 1 107 ? 25.432 16.142 31.417 1.00 36.46 ? 1104 ARG A CD 1 ATOM 818 N NE . ARG A 1 107 ? 24.868 16.630 32.674 1.00 40.66 ? 1104 ARG A NE 1 ATOM 819 C CZ . ARG A 1 107 ? 25.492 17.416 33.547 1.00 43.53 ? 1104 ARG A CZ 1 ATOM 820 N NH1 . ARG A 1 107 ? 26.736 17.827 33.321 1.00 45.80 ? 1104 ARG A NH1 1 ATOM 821 N NH2 . ARG A 1 107 ? 24.880 17.802 34.664 1.00 45.42 ? 1104 ARG A NH2 1 ATOM 822 N N . ASN A 1 108 ? 23.879 10.349 31.851 1.00 32.21 ? 1105 ASN A N 1 ATOM 823 C CA . ASN A 1 108 ? 22.814 9.469 32.359 1.00 32.57 ? 1105 ASN A CA 1 ATOM 824 C C . ASN A 1 108 ? 21.582 10.270 32.782 1.00 30.66 ? 1105 ASN A C 1 ATOM 825 O O . ASN A 1 108 ? 21.035 10.076 33.876 1.00 31.30 ? 1105 ASN A O 1 ATOM 826 C CB . ASN A 1 108 ? 23.284 8.559 33.503 1.00 34.23 ? 1105 ASN A CB 1 ATOM 827 C CG . ASN A 1 108 ? 23.890 7.257 33.004 1.00 36.90 ? 1105 ASN A CG 1 ATOM 828 O OD1 . ASN A 1 108 ? 23.533 6.733 31.941 1.00 39.10 ? 1105 ASN A OD1 1 ATOM 829 N ND2 . ASN A 1 108 ? 24.821 6.720 33.784 1.00 40.39 ? 1105 ASN A ND2 1 ATOM 830 N N . GLU A 1 109 ? 21.161 11.166 31.893 1.00 27.37 ? 1106 GLU A N 1 ATOM 831 C CA . GLU A 1 109 ? 19.993 11.999 32.128 1.00 24.21 ? 1106 GLU A CA 1 ATOM 832 C C . GLU A 1 109 ? 18.941 11.619 31.100 1.00 22.55 ? 1106 GLU A C 1 ATOM 833 O O . GLU A 1 109 ? 19.070 11.999 29.942 1.00 22.81 ? 1106 GLU A O 1 ATOM 834 C CB . GLU A 1 109 ? 20.357 13.483 32.037 1.00 23.59 ? 1106 GLU A CB 1 ATOM 835 C CG . GLU A 1 109 ? 21.342 13.892 33.127 1.00 24.78 ? 1106 GLU A CG 1 ATOM 836 C CD . GLU A 1 109 ? 21.872 15.308 33.009 1.00 26.12 ? 1106 GLU A CD 1 ATOM 837 O OE1 . GLU A 1 109 ? 21.783 15.901 31.906 1.00 26.04 ? 1106 GLU A OE1 1 ATOM 838 O OE2 . GLU A 1 109 ? 22.401 15.807 34.035 1.00 27.49 ? 1106 GLU A OE2 1 ATOM 839 N N . PRO A 1 110 ? 17.948 10.816 31.508 1.00 22.19 ? 1107 PRO A N 1 ATOM 840 C CA . PRO A 1 110 ? 16.952 10.343 30.544 1.00 20.80 ? 1107 PRO A CA 1 ATOM 841 C C . PRO A 1 110 ? 16.202 11.481 29.858 1.00 18.92 ? 1107 PRO A C 1 ATOM 842 O O . PRO A 1 110 ? 15.828 12.472 30.500 1.00 18.98 ? 1107 PRO A O 1 ATOM 843 C CB . PRO A 1 110 ? 16.010 9.484 31.386 1.00 21.48 ? 1107 PRO A CB 1 ATOM 844 C CG . PRO A 1 110 ? 16.834 9.062 32.554 1.00 23.65 ? 1107 PRO A CG 1 ATOM 845 C CD . PRO A 1 110 ? 17.716 10.250 32.849 1.00 23.00 ? 1107 PRO A CD 1 ATOM 846 N N . VAL A 1 111 ? 16.008 11.330 28.552 1.00 17.43 ? 1108 VAL A N 1 ATOM 847 C CA . VAL A 1 111 ? 15.337 12.347 27.748 1.00 16.24 ? 1108 VAL A CA 1 ATOM 848 C C . VAL A 1 111 ? 14.373 11.663 26.789 1.00 15.32 ? 1108 VAL A C 1 ATOM 849 O O . VAL A 1 111 ? 14.706 10.665 26.149 1.00 16.43 ? 1108 VAL A O 1 ATOM 850 C CB . VAL A 1 111 ? 16.349 13.217 26.953 1.00 15.93 ? 1108 VAL A CB 1 ATOM 851 C CG1 . VAL A 1 111 ? 17.301 12.348 26.147 1.00 17.57 ? 1108 VAL A CG1 1 ATOM 852 C CG2 . VAL A 1 111 ? 15.656 14.220 26.015 1.00 16.51 ? 1108 VAL A CG2 1 ATOM 853 N N . LEU A 1 112 ? 13.157 12.205 26.729 1.00 15.12 ? 1109 LEU A N 1 ATOM 854 C CA . LEU A 1 112 ? 12.159 11.726 25.778 1.00 14.14 ? 1109 LEU A CA 1 ATOM 855 C C . LEU A 1 112 ? 12.076 12.694 24.598 1.00 13.40 ? 1109 LEU A C 1 ATOM 856 O O . LEU A 1 112 ? 11.778 13.877 24.815 1.00 14.04 ? 1109 LEU A O 1 ATOM 857 C CB . LEU A 1 112 ? 10.783 11.608 26.455 1.00 15.12 ? 1109 LEU A CB 1 ATOM 858 C CG . LEU A 1 112 ? 9.603 11.315 25.508 1.00 15.87 ? 1109 LEU A CG 1 ATOM 859 C CD1 . LEU A 1 112 ? 9.735 9.965 24.822 1.00 17.43 ? 1109 LEU A CD1 1 ATOM 860 C CD2 . LEU A 1 112 ? 8.278 11.381 26.259 1.00 16.99 ? 1109 LEU A CD2 1 ATOM 861 N N . VAL A 1 113 ? 12.361 12.194 23.388 1.00 12.93 ? 1110 VAL A N 1 ATOM 862 C CA . VAL A 1 113 ? 12.215 12.977 22.169 1.00 13.05 ? 1110 VAL A CA 1 ATOM 863 C C . VAL A 1 113 ? 10.844 12.649 21.576 1.00 12.29 ? 1110 VAL A C 1 ATOM 864 O O . VAL A 1 113 ? 10.566 11.487 21.287 1.00 13.30 ? 1110 VAL A O 1 ATOM 865 C CB . VAL A 1 113 ? 13.339 12.629 21.147 1.00 13.55 ? 1110 VAL A CB 1 ATOM 866 C CG1 . VAL A 1 113 ? 13.184 13.504 19.903 1.00 14.43 ? 1110 VAL A CG1 1 ATOM 867 C CG2 . VAL A 1 113 ? 14.718 12.835 21.794 1.00 15.29 ? 1110 VAL A CG2 1 ATOM 868 N N . HIS A 1 114 ? 9.994 13.654 21.409 1.00 12.41 ? 1111 HIS A N 1 ATOM 869 C CA . HIS A 1 114 ? 8.645 13.364 20.929 1.00 12.61 ? 1111 HIS A CA 1 ATOM 870 C C . HIS A 1 114 ? 8.125 14.365 19.923 1.00 11.93 ? 1111 HIS A C 1 ATOM 871 O O . HIS A 1 114 ? 8.560 15.512 19.864 1.00 12.80 ? 1111 HIS A O 1 ATOM 872 C CB . HIS A 1 114 ? 7.643 13.211 22.091 1.00 12.84 ? 1111 HIS A CB 1 ATOM 873 C CG . HIS A 1 114 ? 7.092 14.511 22.588 1.00 13.20 ? 1111 HIS A CG 1 ATOM 874 N ND1 . HIS A 1 114 ? 5.947 15.084 22.072 1.00 13.68 ? 1111 HIS A ND1 1 ATOM 875 C CD2 . HIS A 1 114 ? 7.543 15.360 23.540 1.00 13.83 ? 1111 HIS A CD2 1 ATOM 876 C CE1 . HIS A 1 114 ? 5.720 16.230 22.686 1.00 14.00 ? 1111 HIS A CE1 1 ATOM 877 N NE2 . HIS A 1 114 ? 6.665 16.417 23.590 1.00 13.86 ? 1111 HIS A NE2 1 ATOM 878 N N . SER A 1 115 ? 7.131 13.907 19.160 1.00 13.40 ? 1112 SER A N 1 ATOM 879 C CA . SER A 1 115 ? 6.340 14.779 18.306 1.00 14.44 ? 1112 SER A CA 1 ATOM 880 C C . SER A 1 115 ? 4.865 14.512 18.601 1.00 15.48 ? 1112 SER A C 1 ATOM 881 O O . SER A 1 115 ? 4.536 14.112 19.708 1.00 16.65 ? 1112 SER A O 1 ATOM 882 C CB . SER A 1 115 ? 6.687 14.525 16.838 1.00 14.65 ? 1112 SER A CB 1 ATOM 883 O OG . SER A 1 115 ? 6.707 13.134 16.576 1.00 15.24 ? 1112 SER A OG 1 ATOM 884 N N . ALA A 1 116 ? 4.004 14.721 17.617 1.00 16.37 ? 1113 ALA A N 1 ATOM 885 C CA . ALA A 1 116 ? 2.583 14.404 17.811 1.00 17.29 ? 1113 ALA A CA 1 ATOM 886 C C . ALA A 1 116 ? 2.363 12.903 17.637 1.00 17.43 ? 1113 ALA A C 1 ATOM 887 O O . ALA A 1 116 ? 1.832 12.227 18.530 1.00 17.63 ? 1113 ALA A O 1 ATOM 888 C CB . ALA A 1 116 ? 1.735 15.193 16.839 1.00 17.76 ? 1113 ALA A CB 1 ATOM 889 N N . ALA A 1 117 ? 2.778 12.383 16.484 1.00 16.78 ? 1114 ALA A N 1 ATOM 890 C CA . ALA A 1 117 ? 2.620 10.971 16.175 1.00 16.95 ? 1114 ALA A CA 1 ATOM 891 C C . ALA A 1 117 ? 3.785 10.090 16.616 1.00 16.02 ? 1114 ALA A C 1 ATOM 892 O O . ALA A 1 117 ? 3.663 8.862 16.613 1.00 16.87 ? 1114 ALA A O 1 ATOM 893 C CB . ALA A 1 117 ? 2.353 10.781 14.689 1.00 16.95 ? 1114 ALA A CB 1 ATOM 894 N N . GLY A 1 118 ? 4.918 10.695 16.971 1.00 15.16 ? 1115 GLY A N 1 ATOM 895 C CA . GLY A 1 118 ? 6.106 9.918 17.296 1.00 14.90 ? 1115 GLY A CA 1 ATOM 896 C C . GLY A 1 118 ? 6.717 9.197 16.100 1.00 13.89 ? 1115 GLY A C 1 ATOM 897 O O . GLY A 1 118 ? 7.319 8.128 16.245 1.00 14.66 ? 1115 GLY A O 1 ATOM 898 N N . VAL A 1 119 ? 6.560 9.793 14.919 1.00 14.05 ? 1116 VAL A N 1 ATOM 899 C CA . VAL A 1 119 ? 6.996 9.176 13.670 1.00 14.16 ? 1116 VAL A CA 1 ATOM 900 C C . VAL A 1 119 ? 8.018 10.032 12.913 1.00 13.47 ? 1116 VAL A C 1 ATOM 901 O O . VAL A 1 119 ? 9.107 9.550 12.555 1.00 13.92 ? 1116 VAL A O 1 ATOM 902 C CB . VAL A 1 119 ? 5.776 8.881 12.752 1.00 14.06 ? 1116 VAL A CB 1 ATOM 903 C CG1 . VAL A 1 119 ? 6.225 8.426 11.376 1.00 14.88 ? 1116 VAL A CG1 1 ATOM 904 C CG2 . VAL A 1 119 ? 4.884 7.828 13.383 1.00 16.56 ? 1116 VAL A CG2 1 ATOM 905 N N . ASN A 1 120 ? 7.660 11.289 12.656 1.00 13.24 ? 1117 ASN A N 1 ATOM 906 C CA . ASN A 1 120 ? 8.381 12.093 11.674 1.00 12.59 ? 1117 ASN A CA 1 ATOM 907 C C . ASN A 1 120 ? 9.349 13.081 12.278 1.00 12.84 ? 1117 ASN A C 1 ATOM 908 O O . ASN A 1 120 ? 10.562 12.911 12.112 1.00 13.12 ? 1117 ASN A O 1 ATOM 909 C CB . ASN A 1 120 ? 7.435 12.787 10.698 1.00 13.08 ? 1117 ASN A CB 1 ATOM 910 C CG . ASN A 1 120 ? 6.878 11.841 9.664 1.00 13.98 ? 1117 ASN A CG 1 ATOM 911 O OD1 . ASN A 1 120 ? 7.531 10.896 9.243 1.00 14.87 ? 1117 ASN A OD1 1 ATOM 912 N ND2 . ASN A 1 120 ? 5.628 12.089 9.253 1.00 16.78 ? 1117 ASN A ND2 1 ATOM 913 N N . ARG A 1 121 ? 8.889 14.107 12.980 1.00 12.34 ? 1118 ARG A N 1 ATOM 914 C CA . ARG A 1 121 ? 9.831 15.103 13.527 1.00 11.82 ? 1118 ARG A CA 1 ATOM 915 C C . ARG A 1 121 ? 10.729 14.424 14.542 1.00 11.50 ? 1118 ARG A C 1 ATOM 916 O O . ARG A 1 121 ? 11.985 14.620 14.525 1.00 12.70 ? 1118 ARG A O 1 ATOM 917 C CB . ARG A 1 121 ? 9.085 16.270 14.170 1.00 12.41 ? 1118 ARG A CB 1 ATOM 918 C CG . ARG A 1 121 ? 8.391 17.142 13.130 1.00 13.79 ? 1118 ARG A CG 1 ATOM 919 C CD . ARG A 1 121 ? 7.344 18.039 13.758 1.00 14.75 ? 1118 ARG A CD 1 ATOM 920 N NE . ARG A 1 121 ? 6.150 17.256 14.113 1.00 14.64 ? 1118 ARG A NE 1 ATOM 921 C CZ . ARG A 1 121 ? 5.031 17.806 14.599 1.00 15.22 ? 1118 ARG A CZ 1 ATOM 922 N NH1 . ARG A 1 121 ? 4.963 19.116 14.800 1.00 15.41 ? 1118 ARG A NH1 1 ATOM 923 N NH2 . ARG A 1 121 ? 4.005 17.005 14.898 1.00 15.72 ? 1118 ARG A NH2 1 ATOM 924 N N . SER A 1 122 ? 10.156 13.633 15.434 1.00 11.45 ? 1119 SER A N 1 ATOM 925 C CA . SER A 1 122 ? 10.934 12.938 16.469 1.00 11.91 ? 1119 SER A CA 1 ATOM 926 C C . SER A 1 122 ? 11.746 11.812 15.867 1.00 11.82 ? 1119 SER A C 1 ATOM 927 O O . SER A 1 122 ? 12.937 11.641 16.210 1.00 12.43 ? 1119 SER A O 1 ATOM 928 C CB . SER A 1 122 ? 9.971 12.429 17.552 1.00 12.27 ? 1119 SER A CB 1 ATOM 929 O OG . SER A 1 122 ? 8.938 11.641 16.963 1.00 13.78 ? 1119 SER A OG 1 ATOM 930 N N . GLY A 1 123 ? 11.152 11.004 14.989 1.00 11.82 ? 1120 GLY A N 1 ATOM 931 C CA . GLY A 1 123 ? 11.886 9.920 14.345 1.00 11.99 ? 1120 GLY A CA 1 ATOM 932 C C . GLY A 1 123 ? 13.092 10.479 13.621 1.00 11.38 ? 1120 GLY A C 1 ATOM 933 O O . GLY A 1 123 ? 14.188 9.884 13.680 1.00 12.31 ? 1120 GLY A O 1 ATOM 934 N N . ALA A 1 124 ? 12.954 11.606 12.950 1.00 11.12 ? 1121 ALA A N 1 ATOM 935 C CA . ALA A 1 124 ? 14.095 12.179 12.199 1.00 11.08 ? 1121 ALA A CA 1 ATOM 936 C C . ALA A 1 124 ? 15.212 12.605 13.140 1.00 11.54 ? 1121 ALA A C 1 ATOM 937 O O . ALA A 1 124 ? 16.399 12.400 12.813 1.00 12.42 ? 1121 ALA A O 1 ATOM 938 C CB . ALA A 1 124 ? 13.644 13.347 11.355 1.00 11.84 ? 1121 ALA A CB 1 ATOM 939 N N . MET A 1 125 ? 14.917 13.200 14.285 1.00 11.24 ? 1122 MET A N 1 ATOM 940 C CA . MET A 1 125 ? 15.965 13.604 15.234 1.00 11.44 ? 1122 MET A CA 1 ATOM 941 C C . MET A 1 125 ? 16.610 12.395 15.832 1.00 11.75 ? 1122 MET A C 1 ATOM 942 O O . MET A 1 125 ? 17.847 12.420 16.058 1.00 13.24 ? 1122 MET A O 1 ATOM 943 C CB . MET A 1 125 ? 15.404 14.526 16.324 1.00 12.27 ? 1122 MET A CB 1 ATOM 944 C CG . MET A 1 125 ? 14.919 15.862 15.774 1.00 13.75 ? 1122 MET A CG 1 ATOM 945 S SD . MET A 1 125 ? 16.263 16.729 14.907 1.00 15.59 ? 1122 MET A SD 1 ATOM 946 C CE . MET A 1 125 ? 15.391 18.232 14.405 1.00 20.03 ? 1122 MET A CE 1 ATOM 947 N N . ILE A 1 126 ? 15.878 11.314 16.068 1.00 11.60 ? 1123 ILE A N 1 ATOM 948 C CA . ILE A 1 126 ? 16.482 10.081 16.570 1.00 11.88 ? 1123 ILE A CA 1 ATOM 949 C C . ILE A 1 126 ? 17.366 9.450 15.505 1.00 11.83 ? 1123 ILE A C 1 ATOM 950 O O . ILE A 1 126 ? 18.488 8.978 15.797 1.00 12.75 ? 1123 ILE A O 1 ATOM 951 C CB . ILE A 1 126 ? 15.387 9.069 17.012 1.00 12.79 ? 1123 ILE A CB 1 ATOM 952 C CG1 . ILE A 1 126 ? 14.682 9.552 18.287 1.00 15.14 ? 1123 ILE A CG1 1 ATOM 953 C CG2 . ILE A 1 126 ? 15.937 7.664 17.147 1.00 14.38 ? 1123 ILE A CG2 1 ATOM 954 C CD1 . ILE A 1 126 ? 15.587 9.710 19.505 1.00 15.91 ? 1123 ILE A CD1 1 ATOM 955 N N . LEU A 1 127 ? 16.929 9.438 14.254 1.00 11.85 ? 1124 LEU A N 1 ATOM 956 C CA . LEU A 1 127 ? 17.764 8.899 13.172 1.00 12.19 ? 1124 LEU A CA 1 ATOM 957 C C . LEU A 1 127 ? 19.036 9.725 13.049 1.00 12.01 ? 1124 LEU A C 1 ATOM 958 O O . LEU A 1 127 ? 20.155 9.163 12.895 1.00 13.29 ? 1124 LEU A O 1 ATOM 959 C CB . LEU A 1 127 ? 16.971 8.891 11.865 1.00 11.72 ? 1124 LEU A CB 1 ATOM 960 C CG . LEU A 1 127 ? 17.572 8.208 10.652 1.00 15.17 ? 1124 LEU A CG 1 ATOM 961 C CD1 . LEU A 1 127 ? 18.275 6.891 10.947 1.00 18.57 ? 1124 LEU A CD1 1 ATOM 962 C CD2 . LEU A 1 127 ? 16.574 8.036 9.516 1.00 14.35 ? 1124 LEU A CD2 1 ATOM 963 N N . ALA A 1 128 ? 18.926 11.044 13.103 1.00 12.04 ? 1125 ALA A N 1 ATOM 964 C CA . ALA A 1 128 ? 20.114 11.918 13.069 1.00 12.17 ? 1125 ALA A CA 1 ATOM 965 C C . ALA A 1 128 ? 21.047 11.590 14.229 1.00 12.85 ? 1125 ALA A C 1 ATOM 966 O O . ALA A 1 128 ? 22.278 11.475 14.042 1.00 14.23 ? 1125 ALA A O 1 ATOM 967 C CB . ALA A 1 128 ? 19.714 13.372 13.172 1.00 12.67 ? 1125 ALA A CB 1 ATOM 968 N N . TYR A 1 129 ? 20.511 11.391 15.416 1.00 12.97 ? 1126 TYR A N 1 ATOM 969 C CA . TYR A 1 129 ? 21.338 11.075 16.584 1.00 13.85 ? 1126 TYR A CA 1 ATOM 970 C C . TYR A 1 129 ? 22.086 9.791 16.323 1.00 14.71 ? 1126 TYR A C 1 ATOM 971 O O . TYR A 1 129 ? 23.318 9.728 16.511 1.00 16.15 ? 1126 TYR A O 1 ATOM 972 C CB . TYR A 1 129 ? 20.478 10.957 17.838 1.00 14.61 ? 1126 TYR A CB 1 ATOM 973 C CG . TYR A 1 129 ? 21.262 10.603 19.091 1.00 14.93 ? 1126 TYR A CG 1 ATOM 974 C CD1 . TYR A 1 129 ? 22.457 11.257 19.403 1.00 17.35 ? 1126 TYR A CD1 1 ATOM 975 C CD2 . TYR A 1 129 ? 20.819 9.622 19.967 1.00 16.21 ? 1126 TYR A CD2 1 ATOM 976 C CE1 . TYR A 1 129 ? 23.173 10.933 20.555 1.00 18.35 ? 1126 TYR A CE1 1 ATOM 977 C CE2 . TYR A 1 129 ? 21.529 9.294 21.124 1.00 18.23 ? 1126 TYR A CE2 1 ATOM 978 C CZ . TYR A 1 129 ? 22.709 9.953 21.421 1.00 18.75 ? 1126 TYR A CZ 1 ATOM 979 O OH . TYR A 1 129 ? 23.425 9.622 22.559 1.00 22.28 ? 1126 TYR A OH 1 ATOM 980 N N . LEU A 1 130 ? 21.388 8.746 15.890 1.00 14.44 ? 1127 LEU A N 1 ATOM 981 C CA . LEU A 1 130 ? 22.063 7.468 15.662 1.00 15.89 ? 1127 LEU A CA 1 ATOM 982 C C . LEU A 1 130 ? 23.111 7.561 14.560 1.00 14.84 ? 1127 LEU A C 1 ATOM 983 O O . LEU A 1 130 ? 24.214 6.999 14.710 1.00 16.30 ? 1127 LEU A O 1 ATOM 984 C CB . LEU A 1 130 ? 21.048 6.365 15.381 1.00 16.30 ? 1127 LEU A CB 1 ATOM 985 C CG . LEU A 1 130 ? 20.119 6.037 16.561 1.00 19.19 ? 1127 LEU A CG 1 ATOM 986 C CD1 . LEU A 1 130 ? 19.009 5.105 16.128 1.00 22.03 ? 1127 LEU A CD1 1 ATOM 987 C CD2 . LEU A 1 130 ? 20.897 5.437 17.738 1.00 23.27 ? 1127 LEU A CD2 1 ATOM 988 N N . MET A 1 131 ? 22.831 8.288 13.484 1.00 14.87 ? 1128 MET A N 1 ATOM 989 C CA . MET A 1 131 ? 23.828 8.464 12.435 1.00 15.33 ? 1128 MET A CA 1 ATOM 990 C C . MET A 1 131 ? 25.027 9.207 13.017 1.00 15.53 ? 1128 MET A C 1 ATOM 991 O O . MET A 1 131 ? 26.198 8.886 12.671 1.00 17.14 ? 1128 MET A O 1 ATOM 992 C CB . MET A 1 131 ? 23.271 9.259 11.254 1.00 14.71 ? 1128 MET A CB 1 ATOM 993 C CG . MET A 1 131 ? 22.174 8.552 10.453 1.00 15.33 ? 1128 MET A CG 1 ATOM 994 S SD . MET A 1 131 ? 22.579 6.918 9.816 1.00 15.80 ? 1128 MET A SD 1 ATOM 995 C CE . MET A 1 131 ? 23.885 7.300 8.613 1.00 17.51 ? 1128 MET A CE 1 ATOM 996 N N . SER A 1 132 ? 24.796 10.180 13.884 1.00 16.25 ? 1129 SER A N 1 ATOM 997 C CA . SER A 1 132 ? 25.874 11.029 14.410 1.00 18.04 ? 1129 SER A CA 1 ATOM 998 C C . SER A 1 132 ? 26.783 10.204 15.299 1.00 19.20 ? 1129 SER A C 1 ATOM 999 O O . SER A 1 132 ? 27.987 10.494 15.396 1.00 21.59 ? 1129 SER A O 1 ATOM 1000 C CB . SER A 1 132 ? 25.347 12.239 15.192 1.00 17.67 ? 1129 SER A CB 1 ATOM 1001 O OG . SER A 1 132 ? 24.861 11.875 16.477 1.00 20.04 ? 1129 SER A OG 1 ATOM 1002 N N . LYS A 1 133 ? 26.229 9.181 15.942 1.00 20.20 ? 1130 LYS A N 1 ATOM 1003 C CA . LYS A 1 133 ? 26.978 8.364 16.895 1.00 22.76 ? 1130 LYS A CA 1 ATOM 1004 C C . LYS A 1 133 ? 27.735 7.264 16.173 1.00 22.13 ? 1130 LYS A C 1 ATOM 1005 O O . LYS A 1 133 ? 28.651 6.665 16.747 1.00 22.88 ? 1130 LYS A O 1 ATOM 1006 C CB . LYS A 1 133 ? 26.025 7.767 17.935 1.00 24.04 ? 1130 LYS A CB 1 ATOM 1007 C CG . LYS A 1 133 ? 25.729 8.687 19.102 1.00 29.75 ? 1130 LYS A CG 1 ATOM 1008 C CD . LYS A 1 133 ? 26.651 8.383 20.288 1.00 38.03 ? 1130 LYS A CD 1 ATOM 1009 C CE . LYS A 1 133 ? 26.523 9.404 21.408 1.00 41.31 ? 1130 LYS A CE 1 ATOM 1010 N NZ . LYS A 1 133 ? 27.609 10.435 21.343 1.00 44.20 ? 1130 LYS A NZ 1 ATOM 1011 N N . ASN A 1 134 ? 27.379 6.998 14.920 1.00 21.56 ? 1131 ASN A N 1 ATOM 1012 C CA . ASN A 1 134 ? 28.062 5.957 14.152 1.00 21.38 ? 1131 ASN A CA 1 ATOM 1013 C C . ASN A 1 134 ? 29.427 6.410 13.661 1.00 20.85 ? 1131 ASN A C 1 ATOM 1014 O O . ASN A 1 134 ? 29.512 7.325 12.842 1.00 21.40 ? 1131 ASN A O 1 ATOM 1015 C CB . ASN A 1 134 ? 27.216 5.516 12.954 1.00 20.91 ? 1131 ASN A CB 1 ATOM 1016 C CG . ASN A 1 134 ? 28.009 4.668 11.969 1.00 20.44 ? 1131 ASN A CG 1 ATOM 1017 O OD1 . ASN A 1 134 ? 28.637 3.679 12.354 1.00 22.84 ? 1131 ASN A OD1 1 ATOM 1018 N ND2 . ASN A 1 134 ? 27.997 5.062 10.700 1.00 20.89 ? 1131 ASN A ND2 1 ATOM 1019 N N . LYS A 1 135 ? 30.484 5.754 14.159 1.00 20.37 ? 1132 LYS A N 1 ATOM 1020 C CA . LYS A 1 135 ? 31.873 6.003 13.735 1.00 20.99 ? 1132 LYS A CA 1 ATOM 1021 C C . LYS A 1 135 ? 32.470 4.767 13.052 1.00 20.29 ? 1132 LYS A C 1 ATOM 1022 O O . LYS A 1 135 ? 33.600 4.807 12.531 1.00 22.30 ? 1132 LYS A O 1 ATOM 1023 C CB . LYS A 1 135 ? 32.731 6.401 14.940 1.00 22.10 ? 1132 LYS A CB 1 ATOM 1024 C CG . LYS A 1 135 ? 32.185 7.560 15.761 1.00 26.75 ? 1132 LYS A CG 1 ATOM 1025 C CD . LYS A 1 135 ? 33.124 7.939 16.890 1.00 34.43 ? 1132 LYS A CD 1 ATOM 1026 C CE . LYS A 1 135 ? 33.815 9.268 16.603 1.00 38.65 ? 1132 LYS A CE 1 ATOM 1027 N NZ . LYS A 1 135 ? 34.854 9.568 17.634 1.00 41.36 ? 1132 LYS A NZ 1 ATOM 1028 N N . GLU A 1 136 ? 31.713 3.670 13.068 1.00 21.01 ? 1133 GLU A N 1 ATOM 1029 C CA . GLU A 1 136 ? 32.227 2.344 12.714 1.00 21.55 ? 1133 GLU A CA 1 ATOM 1030 C C . GLU A 1 136 ? 31.814 1.881 11.319 1.00 21.18 ? 1133 GLU A C 1 ATOM 1031 O O . GLU A 1 136 ? 32.641 1.338 10.570 1.00 22.64 ? 1133 GLU A O 1 ATOM 1032 C CB . GLU A 1 136 ? 31.763 1.299 13.737 1.00 22.57 ? 1133 GLU A CB 1 ATOM 1033 C CG . GLU A 1 136 ? 32.320 1.477 15.141 1.00 23.21 ? 1133 GLU A CG 1 ATOM 1034 C CD . GLU A 1 136 ? 33.593 0.682 15.369 1.00 23.54 ? 1133 GLU A CD 1 ATOM 1035 O OE1 . GLU A 1 136 ? 33.731 -0.408 14.781 1.00 26.77 ? 1133 GLU A OE1 1 ATOM 1036 O OE2 . GLU A 1 136 ? 34.435 1.145 16.159 1.00 22.31 ? 1133 GLU A OE2 1 ATOM 1037 N N . SER A 1 137 ? 30.537 2.075 10.986 1.00 20.85 ? 1134 SER A N 1 ATOM 1038 C CA . SER A 1 137 ? 29.943 1.431 9.817 1.00 21.39 ? 1134 SER A CA 1 ATOM 1039 C C . SER A 1 137 ? 29.787 2.371 8.627 1.00 20.53 ? 1134 SER A C 1 ATOM 1040 O O . SER A 1 137 ? 29.643 3.576 8.810 1.00 20.50 ? 1134 SER A O 1 ATOM 1041 C CB . SER A 1 137 ? 28.569 0.864 10.215 1.00 21.71 ? 1134 SER A CB 1 ATOM 1042 O OG . SER A 1 137 ? 28.680 -0.130 11.229 1.00 26.07 ? 1134 SER A OG 1 ATOM 1043 N N . LEU A 1 138 ? 29.814 1.826 7.412 1.00 20.77 ? 1135 LEU A N 1 ATOM 1044 C CA . LEU A 1 138 ? 29.584 2.638 6.214 1.00 20.53 ? 1135 LEU A CA 1 ATOM 1045 C C . LEU A 1 138 ? 28.234 3.331 6.363 1.00 18.80 ? 1135 LEU A C 1 ATOM 1046 O O . LEU A 1 138 ? 27.245 2.658 6.610 1.00 18.79 ? 1135 LEU A O 1 ATOM 1047 C CB . LEU A 1 138 ? 29.598 1.776 4.943 1.00 22.63 ? 1135 LEU A CB 1 ATOM 1048 C CG . LEU A 1 138 ? 30.868 0.957 4.693 1.00 27.13 ? 1135 LEU A CG 1 ATOM 1049 C CD1 . LEU A 1 138 ? 30.627 -0.114 3.643 1.00 30.37 ? 1135 LEU A CD1 1 ATOM 1050 C CD2 . LEU A 1 138 ? 32.035 1.858 4.284 1.00 31.32 ? 1135 LEU A CD2 1 ATOM 1051 N N . PRO A 1 139 ? 28.205 4.660 6.233 1.00 17.99 ? 1136 PRO A N 1 ATOM 1052 C CA . PRO A 1 139 ? 26.963 5.409 6.468 1.00 17.65 ? 1136 PRO A CA 1 ATOM 1053 C C . PRO A 1 139 ? 25.777 4.871 5.677 1.00 17.43 ? 1136 PRO A C 1 ATOM 1054 O O . PRO A 1 139 ? 24.676 4.794 6.234 1.00 17.20 ? 1136 PRO A O 1 ATOM 1055 C CB . PRO A 1 139 ? 27.326 6.823 6.026 1.00 18.11 ? 1136 PRO A CB 1 ATOM 1056 C CG . PRO A 1 139 ? 28.777 6.924 6.339 1.00 18.68 ? 1136 PRO A CG 1 ATOM 1057 C CD . PRO A 1 139 ? 29.357 5.561 6.024 1.00 18.65 ? 1136 PRO A CD 1 ATOM 1058 N N . MET A 1 140 ? 25.964 4.503 4.413 1.00 17.90 ? 1137 MET A N 1 ATOM 1059 C CA . MET A 1 140 ? 24.809 4.032 3.613 1.00 19.83 ? 1137 MET A CA 1 ATOM 1060 C C . MET A 1 140 ? 24.192 2.783 4.245 1.00 18.70 ? 1137 MET A C 1 ATOM 1061 O O . MET A 1 140 ? 22.962 2.652 4.356 1.00 18.80 ? 1137 MET A O 1 ATOM 1062 C CB . MET A 1 140 ? 25.214 3.765 2.159 1.00 22.36 ? 1137 MET A CB 1 ATOM 1063 C CG . MET A 1 140 ? 24.155 2.988 1.399 1.00 27.32 ? 1137 MET A CG 1 ATOM 1064 S SD . MET A 1 140 ? 24.675 2.420 -0.217 0.50 31.00 ? 1137 MET A SD 1 ATOM 1065 C CE . MET A 1 140 ? 26.432 2.167 0.041 1.00 34.11 ? 1137 MET A CE 1 ATOM 1066 N N . LEU A 1 141 ? 25.037 1.857 4.686 1.00 19.23 ? 1138 LEU A N 1 ATOM 1067 C CA . LEU A 1 141 ? 24.575 0.610 5.278 1.00 19.86 ? 1138 LEU A CA 1 ATOM 1068 C C . LEU A 1 141 ? 23.963 0.875 6.640 1.00 18.00 ? 1138 LEU A C 1 ATOM 1069 O O . LEU A 1 141 ? 22.923 0.316 6.982 1.00 18.87 ? 1138 LEU A O 1 ATOM 1070 C CB . LEU A 1 141 ? 25.727 -0.387 5.430 1.00 22.00 ? 1138 LEU A CB 1 ATOM 1071 C CG . LEU A 1 141 ? 26.264 -1.026 4.151 1.00 27.00 ? 1138 LEU A CG 1 ATOM 1072 C CD1 . LEU A 1 141 ? 27.491 -1.871 4.474 1.00 31.02 ? 1138 LEU A CD1 1 ATOM 1073 C CD2 . LEU A 1 141 ? 25.191 -1.887 3.498 1.00 31.25 ? 1138 LEU A CD2 1 ATOM 1074 N N . TYR A 1 142 ? 24.602 1.735 7.432 1.00 17.45 ? 1139 TYR A N 1 ATOM 1075 C CA . TYR A 1 142 ? 24.096 2.031 8.770 1.00 17.16 ? 1139 TYR A CA 1 ATOM 1076 C C . TYR A 1 142 ? 22.729 2.725 8.683 1.00 16.16 ? 1139 TYR A C 1 ATOM 1077 O O . TYR A 1 142 ? 21.816 2.433 9.483 1.00 17.41 ? 1139 TYR A O 1 ATOM 1078 C CB . TYR A 1 142 ? 25.103 2.868 9.579 1.00 18.01 ? 1139 TYR A CB 1 ATOM 1079 C CG . TYR A 1 142 ? 24.776 2.836 11.054 1.00 18.44 ? 1139 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 142 ? 24.939 1.656 11.787 1.00 20.16 ? 1139 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 142 ? 24.296 3.959 11.716 1.00 18.37 ? 1139 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 142 ? 24.621 1.608 13.133 1.00 22.71 ? 1139 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 142 ? 23.987 3.925 13.078 1.00 20.44 ? 1139 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 142 ? 24.141 2.743 13.775 1.00 21.59 ? 1139 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 142 ? 23.835 2.684 15.109 1.00 24.93 ? 1139 TYR A OH 1 ATOM 1086 N N . PHE A 1 143 ? 22.583 3.646 7.737 1.00 15.12 ? 1140 PHE A N 1 ATOM 1087 C CA . PHE A 1 143 ? 21.316 4.355 7.511 1.00 13.71 ? 1140 PHE A CA 1 ATOM 1088 C C . PHE A 1 143 ? 20.213 3.358 7.200 1.00 13.51 ? 1140 PHE A C 1 ATOM 1089 O O . PHE A 1 143 ? 19.125 3.416 7.789 1.00 14.09 ? 1140 PHE A O 1 ATOM 1090 C CB . PHE A 1 143 ? 21.468 5.343 6.349 1.00 14.06 ? 1140 PHE A CB 1 ATOM 1091 C CG . PHE A 1 143 ? 20.162 5.931 5.859 1.00 13.37 ? 1140 PHE A CG 1 ATOM 1092 C CD1 . PHE A 1 143 ? 19.494 6.919 6.589 1.00 13.62 ? 1140 PHE A CD1 1 ATOM 1093 C CD2 . PHE A 1 143 ? 19.632 5.489 4.648 1.00 14.76 ? 1140 PHE A CD2 1 ATOM 1094 C CE1 . PHE A 1 143 ? 18.279 7.465 6.105 1.00 14.25 ? 1140 PHE A CE1 1 ATOM 1095 C CE2 . PHE A 1 143 ? 18.435 6.006 4.173 1.00 16.06 ? 1140 PHE A CE2 1 ATOM 1096 C CZ . PHE A 1 143 ? 17.766 6.991 4.909 1.00 15.32 ? 1140 PHE A CZ 1 ATOM 1097 N N . LEU A 1 144 ? 20.451 2.436 6.279 1.00 13.80 ? 1141 LEU A N 1 ATOM 1098 C CA . LEU A 1 144 ? 19.422 1.449 5.940 1.00 14.71 ? 1141 LEU A CA 1 ATOM 1099 C C . LEU A 1 144 ? 19.090 0.554 7.131 1.00 15.68 ? 1141 LEU A C 1 ATOM 1100 O O . LEU A 1 144 ? 17.926 0.233 7.387 1.00 16.70 ? 1141 LEU A O 1 ATOM 1101 C CB . LEU A 1 144 ? 19.823 0.601 4.731 1.00 15.68 ? 1141 LEU A CB 1 ATOM 1102 C CG . LEU A 1 144 ? 19.924 1.383 3.411 1.00 17.12 ? 1141 LEU A CG 1 ATOM 1103 C CD1 . LEU A 1 144 ? 20.446 0.468 2.325 1.00 19.02 ? 1141 LEU A CD1 1 ATOM 1104 C CD2 . LEU A 1 144 ? 18.568 1.985 3.011 1.00 19.10 ? 1141 LEU A CD2 1 ATOM 1105 N N . TYR A 1 145 ? 20.119 0.141 7.871 1.00 16.82 ? 1142 TYR A N 1 ATOM 1106 C CA . TYR A 1 145 ? 19.924 -0.708 9.033 1.00 18.61 ? 1142 TYR A CA 1 ATOM 1107 C C . TYR A 1 145 ? 19.088 -0.011 10.102 1.00 18.24 ? 1142 TYR A C 1 ATOM 1108 O O . TYR A 1 145 ? 18.099 -0.594 10.595 1.00 19.04 ? 1142 TYR A O 1 ATOM 1109 C CB . TYR A 1 145 ? 21.268 -1.174 9.631 1.00 20.94 ? 1142 TYR A CB 1 ATOM 1110 C CG . TYR A 1 145 ? 21.042 -1.905 10.940 1.00 25.78 ? 1142 TYR A CG 1 ATOM 1111 C CD1 . TYR A 1 145 ? 20.528 -3.201 10.929 1.00 31.30 ? 1142 TYR A CD1 1 ATOM 1112 C CD2 . TYR A 1 145 ? 21.289 -1.307 12.173 1.00 31.06 ? 1142 TYR A CD2 1 ATOM 1113 C CE1 . TYR A 1 145 ? 20.287 -3.890 12.110 1.00 35.87 ? 1142 TYR A CE1 1 ATOM 1114 C CE2 . TYR A 1 145 ? 21.049 -1.990 13.365 1.00 35.28 ? 1142 TYR A CE2 1 ATOM 1115 C CZ . TYR A 1 145 ? 20.550 -3.282 13.323 1.00 37.19 ? 1142 TYR A CZ 1 ATOM 1116 O OH . TYR A 1 145 ? 20.309 -3.976 14.488 1.00 40.20 ? 1142 TYR A OH 1 ATOM 1117 N N . VAL A 1 146 ? 19.474 1.204 10.472 1.00 17.65 ? 1143 VAL A N 1 ATOM 1118 C CA . VAL A 1 146 ? 18.756 1.932 11.523 1.00 17.14 ? 1143 VAL A CA 1 ATOM 1119 C C . VAL A 1 146 ? 17.327 2.216 11.051 1.00 15.15 ? 1143 VAL A C 1 ATOM 1120 O O . VAL A 1 146 ? 16.380 2.042 11.824 1.00 15.53 ? 1143 VAL A O 1 ATOM 1121 C CB . VAL A 1 146 ? 19.453 3.249 11.969 1.00 18.19 ? 1143 VAL A CB 1 ATOM 1122 C CG1 . VAL A 1 146 ? 18.501 4.073 12.869 1.00 19.56 ? 1143 VAL A CG1 1 ATOM 1123 C CG2 . VAL A 1 146 ? 20.772 2.943 12.678 1.00 21.82 ? 1143 VAL A CG2 1 ATOM 1124 N N . TYR A 1 147 ? 17.185 2.656 9.796 1.00 14.00 ? 1144 TYR A N 1 ATOM 1125 C CA . TYR A 1 147 ? 15.871 2.990 9.271 1.00 13.74 ? 1144 TYR A CA 1 ATOM 1126 C C . TYR A 1 147 ? 14.945 1.790 9.412 1.00 13.79 ? 1144 TYR A C 1 ATOM 1127 O O . TYR A 1 147 ? 13.857 1.878 10.008 1.00 14.34 ? 1144 TYR A O 1 ATOM 1128 C CB . TYR A 1 147 ? 15.936 3.480 7.800 1.00 13.42 ? 1144 TYR A CB 1 ATOM 1129 C CG . TYR A 1 147 ? 14.523 3.844 7.396 1.00 13.58 ? 1144 TYR A CG 1 ATOM 1130 C CD1 . TYR A 1 147 ? 14.017 5.083 7.783 1.00 13.87 ? 1144 TYR A CD1 1 ATOM 1131 C CD2 . TYR A 1 147 ? 13.695 2.960 6.714 1.00 15.46 ? 1144 TYR A CD2 1 ATOM 1132 C CE1 . TYR A 1 147 ? 12.713 5.435 7.488 1.00 15.53 ? 1144 TYR A CE1 1 ATOM 1133 C CE2 . TYR A 1 147 ? 12.370 3.310 6.411 1.00 16.21 ? 1144 TYR A CE2 1 ATOM 1134 C CZ . TYR A 1 147 ? 11.901 4.549 6.804 1.00 14.83 ? 1144 TYR A CZ 1 ATOM 1135 O OH . TYR A 1 147 ? 10.597 4.909 6.522 1.00 18.25 ? 1144 TYR A OH 1 ATOM 1136 N N . HIS A 1 148 ? 15.340 0.671 8.824 1.00 14.69 ? 1145 HIS A N 1 ATOM 1137 C CA . HIS A 1 148 ? 14.439 -0.485 8.772 1.00 16.21 ? 1145 HIS A CA 1 ATOM 1138 C C . HIS A 1 148 ? 14.230 -1.155 10.117 1.00 17.03 ? 1145 HIS A C 1 ATOM 1139 O O . HIS A 1 148 ? 13.114 -1.596 10.417 1.00 18.52 ? 1145 HIS A O 1 ATOM 1140 C CB . HIS A 1 148 ? 14.882 -1.466 7.688 1.00 16.78 ? 1145 HIS A CB 1 ATOM 1141 C CG . HIS A 1 148 ? 14.593 -0.951 6.318 1.00 18.16 ? 1145 HIS A CG 1 ATOM 1142 N ND1 . HIS A 1 148 ? 13.314 -0.734 5.858 1.00 19.58 ? 1145 HIS A ND1 1 ATOM 1143 C CD2 . HIS A 1 148 ? 15.420 -0.580 5.306 1.00 18.79 ? 1145 HIS A CD2 1 ATOM 1144 C CE1 . HIS A 1 148 ? 13.362 -0.258 4.621 1.00 20.03 ? 1145 HIS A CE1 1 ATOM 1145 N NE2 . HIS A 1 148 ? 14.632 -0.158 4.260 1.00 19.34 ? 1145 HIS A NE2 1 ATOM 1146 N N . SER A 1 149 ? 15.269 -1.220 10.941 1.00 17.75 ? 1146 SER A N 1 ATOM 1147 C CA . SER A 1 149 ? 15.132 -1.851 12.246 1.00 18.58 ? 1146 SER A CA 1 ATOM 1148 C C . SER A 1 149 ? 14.224 -1.016 13.157 1.00 17.62 ? 1146 SER A C 1 ATOM 1149 O O . SER A 1 149 ? 13.400 -1.583 13.884 1.00 18.70 ? 1146 SER A O 1 ATOM 1150 C CB . SER A 1 149 ? 16.487 -2.131 12.901 1.00 20.01 ? 1146 SER A CB 1 ATOM 1151 O OG . SER A 1 149 ? 17.208 -0.939 13.151 1.00 22.64 ? 1146 SER A OG 1 ATOM 1152 N N . MET A 1 150 ? 14.351 0.311 13.104 1.00 16.66 ? 1147 MET A N 1 ATOM 1153 C CA . MET A 1 150 ? 13.469 1.186 13.884 1.00 16.08 ? 1147 MET A CA 1 ATOM 1154 C C . MET A 1 150 ? 12.029 1.120 13.385 1.00 16.41 ? 1147 MET A C 1 ATOM 1155 O O . MET A 1 150 ? 11.078 1.118 14.172 1.00 17.64 ? 1147 MET A O 1 ATOM 1156 C CB . MET A 1 150 ? 13.964 2.638 13.845 1.00 16.00 ? 1147 MET A CB 1 ATOM 1157 C CG . MET A 1 150 ? 15.200 2.944 14.702 1.00 18.11 ? 1147 MET A CG 1 ATOM 1158 S SD . MET A 1 150 ? 14.935 2.658 16.481 1.00 24.07 ? 1147 MET A SD 1 ATOM 1159 C CE . MET A 1 150 ? 13.679 3.863 16.862 1.00 25.03 ? 1147 MET A CE 1 ATOM 1160 N N . ARG A 1 151 ? 11.863 1.082 12.074 1.00 16.68 ? 1148 ARG A N 1 ATOM 1161 C CA . ARG A 1 151 ? 10.523 1.031 11.499 1.00 17.53 ? 1148 ARG A CA 1 ATOM 1162 C C . ARG A 1 151 ? 9.817 -0.274 11.854 1.00 18.40 ? 1148 ARG A C 1 ATOM 1163 O O . ARG A 1 151 ? 8.603 -0.291 12.147 1.00 19.26 ? 1148 ARG A O 1 ATOM 1164 C CB . ARG A 1 151 ? 10.582 1.214 9.982 1.00 17.34 ? 1148 ARG A CB 1 ATOM 1165 C CG . ARG A 1 151 ? 9.200 1.483 9.396 1.00 19.17 ? 1148 ARG A CG 1 ATOM 1166 C CD . ARG A 1 151 ? 9.312 1.750 7.923 1.00 20.36 ? 1148 ARG A CD 1 ATOM 1167 N NE . ARG A 1 151 ? 8.051 2.218 7.363 1.00 21.34 ? 1148 ARG A NE 1 ATOM 1168 C CZ . ARG A 1 151 ? 7.118 1.429 6.852 1.00 23.26 ? 1148 ARG A CZ 1 ATOM 1169 N NH1 . ARG A 1 151 ? 7.275 0.112 6.809 1.00 25.20 ? 1148 ARG A NH1 1 ATOM 1170 N NH2 . ARG A 1 151 ? 6.018 1.971 6.366 1.00 23.35 ? 1148 ARG A NH2 1 ATOM 1171 N N . ASP A 1 152 ? 10.565 -1.377 11.829 1.00 20.64 ? 1149 ASP A N 1 ATOM 1172 C CA . ASP A 1 152 ? 10.003 -2.677 12.192 1.00 23.37 ? 1149 ASP A CA 1 ATOM 1173 C C . ASP A 1 152 ? 9.552 -2.697 13.654 1.00 24.16 ? 1149 ASP A C 1 ATOM 1174 O O . ASP A 1 152 ? 8.533 -3.300 14.000 1.00 24.97 ? 1149 ASP A O 1 ATOM 1175 C CB . ASP A 1 152 ? 11.026 -3.788 11.927 1.00 24.80 ? 1149 ASP A CB 1 ATOM 1176 C CG . ASP A 1 152 ? 11.193 -4.102 10.447 1.00 27.73 ? 1149 ASP A CG 1 ATOM 1177 O OD1 . ASP A 1 152 ? 10.468 -3.520 9.603 1.00 31.16 ? 1149 ASP A OD1 1 ATOM 1178 O OD2 . ASP A 1 152 ? 12.064 -4.932 10.111 1.00 31.22 ? 1149 ASP A OD2 1 ATOM 1179 N N . LEU A 1 153 ? 10.318 -2.014 14.500 1.00 23.53 ? 1150 LEU A N 1 ATOM 1180 C CA . LEU A 1 153 ? 10.049 -1.943 15.934 1.00 24.05 ? 1150 LEU A CA 1 ATOM 1181 C C . LEU A 1 153 ? 8.884 -1.018 16.269 1.00 23.69 ? 1150 LEU A C 1 ATOM 1182 O O . LEU A 1 153 ? 8.024 -1.367 17.097 1.00 24.94 ? 1150 LEU A O 1 ATOM 1183 C CB . LEU A 1 153 ? 11.308 -1.481 16.685 1.00 24.92 ? 1150 LEU A CB 1 ATOM 1184 C CG . LEU A 1 153 ? 11.201 -1.342 18.209 1.00 28.06 ? 1150 LEU A CG 1 ATOM 1185 C CD1 . LEU A 1 153 ? 10.763 -2.651 18.860 1.00 30.46 ? 1150 LEU A CD1 1 ATOM 1186 C CD2 . LEU A 1 153 ? 12.525 -0.851 18.774 1.00 30.45 ? 1150 LEU A CD2 1 ATOM 1187 N N . ARG A 1 154 ? 8.844 0.146 15.629 1.00 21.55 ? 1151 ARG A N 1 ATOM 1188 C CA . ARG A 1 154 ? 7.869 1.193 15.929 1.00 20.98 ? 1151 ARG A CA 1 ATOM 1189 C C . ARG A 1 154 ? 6.575 1.066 15.132 1.00 20.63 ? 1151 ARG A C 1 ATOM 1190 O O . ARG A 1 154 ? 5.533 1.491 15.625 1.00 22.41 ? 1151 ARG A O 1 ATOM 1191 C CB . ARG A 1 154 ? 8.468 2.577 15.647 1.00 20.95 ? 1151 ARG A CB 1 ATOM 1192 C CG . ARG A 1 154 ? 9.780 2.900 16.356 1.00 22.57 ? 1151 ARG A CG 1 ATOM 1193 C CD . ARG A 1 154 ? 9.551 3.568 17.691 1.00 21.03 ? 1151 ARG A CD 1 ATOM 1194 N NE . ARG A 1 154 ? 8.734 4.787 17.638 1.00 17.77 ? 1151 ARG A NE 1 ATOM 1195 C CZ . ARG A 1 154 ? 7.951 5.172 18.651 1.00 18.11 ? 1151 ARG A CZ 1 ATOM 1196 N NH1 . ARG A 1 154 ? 7.881 4.417 19.755 1.00 20.47 ? 1151 ARG A NH1 1 ATOM 1197 N NH2 . ARG A 1 154 ? 7.238 6.293 18.554 1.00 16.43 ? 1151 ARG A NH2 1 ATOM 1198 N N . GLY A 1 155 ? 6.648 0.516 13.924 1.00 19.38 ? 1152 GLY A N 1 ATOM 1199 C CA . GLY A 1 155 ? 5.479 0.429 13.031 1.00 19.57 ? 1152 GLY A CA 1 ATOM 1200 C C . GLY A 1 155 ? 5.498 1.486 11.935 1.00 18.31 ? 1152 GLY A C 1 ATOM 1201 O O . GLY A 1 155 ? 5.059 1.234 10.807 1.00 19.75 ? 1152 GLY A O 1 ATOM 1202 N N . ALA A 1 156 ? 6.002 2.667 12.280 1.00 18.39 ? 1153 ALA A N 1 ATOM 1203 C CA . ALA A 1 156 ? 6.195 3.756 11.334 1.00 17.22 ? 1153 ALA A CA 1 ATOM 1204 C C . ALA A 1 156 ? 7.353 4.613 11.840 1.00 16.22 ? 1153 ALA A C 1 ATOM 1205 O O . ALA A 1 156 ? 7.494 4.820 13.042 1.00 17.23 ? 1153 ALA A O 1 ATOM 1206 C CB . ALA A 1 156 ? 4.921 4.591 11.201 1.00 18.59 ? 1153 ALA A CB 1 ATOM 1207 N N . PHE A 1 157 ? 8.178 5.104 10.921 1.00 15.01 ? 1154 PHE A N 1 ATOM 1208 C CA . PHE A 1 157 ? 9.435 5.761 11.289 1.00 13.87 ? 1154 PHE A CA 1 ATOM 1209 C C . PHE A 1 157 ? 9.854 6.618 10.107 1.00 13.36 ? 1154 PHE A C 1 ATOM 1210 O O . PHE A 1 157 ? 10.002 6.113 8.997 1.00 14.14 ? 1154 PHE A O 1 ATOM 1211 C CB . PHE A 1 157 ? 10.494 4.718 11.675 1.00 14.09 ? 1154 PHE A CB 1 ATOM 1212 C CG . PHE A 1 157 ? 11.793 5.307 12.167 1.00 13.49 ? 1154 PHE A CG 1 ATOM 1213 C CD1 . PHE A 1 157 ? 11.868 5.965 13.390 1.00 12.71 ? 1154 PHE A CD1 1 ATOM 1214 C CD2 . PHE A 1 157 ? 12.943 5.184 11.408 1.00 13.30 ? 1154 PHE A CD2 1 ATOM 1215 C CE1 . PHE A 1 157 ? 13.064 6.499 13.844 1.00 13.66 ? 1154 PHE A CE1 1 ATOM 1216 C CE2 . PHE A 1 157 ? 14.143 5.715 11.859 1.00 13.17 ? 1154 PHE A CE2 1 ATOM 1217 C CZ . PHE A 1 157 ? 14.201 6.369 13.076 1.00 13.14 ? 1154 PHE A CZ 1 ATOM 1218 N N . VAL A 1 158 ? 10.039 7.909 10.358 1.00 13.22 ? 1155 VAL A N 1 ATOM 1219 C CA . VAL A 1 158 ? 10.333 8.875 9.307 1.00 13.67 ? 1155 VAL A CA 1 ATOM 1220 C C . VAL A 1 158 ? 9.734 8.571 7.940 1.00 14.04 ? 1155 VAL A C 1 ATOM 1221 O O . VAL A 1 158 ? 10.446 8.458 6.946 1.00 14.77 ? 1155 VAL A O 1 ATOM 1222 C CB . VAL A 1 158 ? 11.855 9.070 9.163 1.00 13.68 ? 1155 VAL A CB 1 ATOM 1223 C CG1 . VAL A 1 158 ? 12.149 10.387 8.469 1.00 15.32 ? 1155 VAL A CG1 1 ATOM 1224 C CG2 . VAL A 1 158 ? 12.524 9.024 10.530 1.00 14.09 ? 1155 VAL A CG2 1 ATOM 1225 N N . GLU A 1 159 ? 8.412 8.444 7.902 1.00 14.46 ? 1156 GLU A N 1 ATOM 1226 C CA . GLU A 1 159 ? 7.692 8.304 6.643 1.00 15.42 ? 1156 GLU A CA 1 ATOM 1227 C C . GLU A 1 159 ? 7.804 9.525 5.733 1.00 15.40 ? 1156 GLU A C 1 ATOM 1228 O O . GLU A 1 159 ? 7.679 9.413 4.516 1.00 17.35 ? 1156 GLU A O 1 ATOM 1229 C CB . GLU A 1 159 ? 6.222 7.961 6.906 1.00 16.18 ? 1156 GLU A CB 1 ATOM 1230 C CG . GLU A 1 159 ? 6.019 6.853 7.929 1.00 17.90 ? 1156 GLU A CG 1 ATOM 1231 C CD . GLU A 1 159 ? 6.546 5.512 7.455 1.00 20.00 ? 1156 GLU A CD 1 ATOM 1232 O OE1 . GLU A 1 159 ? 6.276 5.140 6.296 1.00 22.40 ? 1156 GLU A OE1 1 ATOM 1233 O OE2 . GLU A 1 159 ? 7.228 4.824 8.244 1.00 19.97 ? 1156 GLU A OE2 1 ATOM 1234 N N . ASN A 1 160 ? 8.046 10.686 6.332 1.00 15.50 ? 1157 ASN A N 1 ATOM 1235 C CA . ASN A 1 160 ? 8.144 11.946 5.589 1.00 15.38 ? 1157 ASN A CA 1 ATOM 1236 C C . ASN A 1 160 ? 9.379 11.894 4.674 1.00 15.20 ? 1157 ASN A C 1 ATOM 1237 O O . ASN A 1 160 ? 10.500 11.840 5.169 1.00 15.75 ? 1157 ASN A O 1 ATOM 1238 C CB . ASN A 1 160 ? 8.210 13.106 6.593 1.00 15.21 ? 1157 ASN A CB 1 ATOM 1239 C CG . ASN A 1 160 ? 8.334 14.472 5.937 1.00 15.78 ? 1157 ASN A CG 1 ATOM 1240 O OD1 . ASN A 1 160 ? 8.961 14.633 4.883 1.00 18.14 ? 1157 ASN A OD1 1 ATOM 1241 N ND2 . ASN A 1 160 ? 7.773 15.479 6.606 1.00 15.67 ? 1157 ASN A ND2 1 ATOM 1242 N N . PRO A 1 161 ? 9.185 11.852 3.349 1.00 16.48 ? 1158 PRO A N 1 ATOM 1243 C CA . PRO A 1 161 ? 10.350 11.688 2.468 1.00 17.26 ? 1158 PRO A CA 1 ATOM 1244 C C . PRO A 1 161 ? 11.292 12.887 2.459 1.00 16.34 ? 1158 PRO A C 1 ATOM 1245 O O . PRO A 1 161 ? 12.476 12.711 2.157 1.00 16.53 ? 1158 PRO A O 1 ATOM 1246 C CB . PRO A 1 161 ? 9.725 11.476 1.085 1.00 18.60 ? 1158 PRO A CB 1 ATOM 1247 C CG . PRO A 1 161 ? 8.367 12.086 1.179 1.00 19.58 ? 1158 PRO A CG 1 ATOM 1248 C CD . PRO A 1 161 ? 7.910 11.913 2.595 1.00 16.77 ? 1158 PRO A CD 1 ATOM 1249 N N . SER A 1 162 ? 10.799 14.088 2.764 1.00 15.77 ? 1159 SER A N 1 ATOM 1250 C CA A SER A 1 162 ? 11.662 15.274 2.850 0.50 15.49 ? 1159 SER A CA 1 ATOM 1251 C CA B SER A 1 162 ? 11.675 15.252 2.822 0.50 15.30 ? 1159 SER A CA 1 ATOM 1252 C C . SER A 1 162 ? 12.608 15.170 4.038 1.00 14.66 ? 1159 SER A C 1 ATOM 1253 O O . SER A 1 162 ? 13.788 15.554 3.963 1.00 14.86 ? 1159 SER A O 1 ATOM 1254 C CB A SER A 1 162 ? 10.868 16.576 2.968 0.50 16.22 ? 1159 SER A CB 1 ATOM 1255 C CB B SER A 1 162 ? 10.847 16.538 2.793 0.50 15.89 ? 1159 SER A CB 1 ATOM 1256 O OG A SER A 1 162 ? 11.745 17.666 3.258 0.50 17.47 ? 1159 SER A OG 1 ATOM 1257 O OG B SER A 1 162 ? 10.100 16.606 1.579 0.50 15.63 ? 1159 SER A OG 1 ATOM 1258 N N . PHE A 1 163 ? 12.117 14.651 5.150 1.00 14.35 ? 1160 PHE A N 1 ATOM 1259 C CA . PHE A 1 163 ? 12.967 14.476 6.326 1.00 13.11 ? 1160 PHE A CA 1 ATOM 1260 C C . PHE A 1 163 ? 14.016 13.402 6.032 1.00 12.99 ? 1160 PHE A C 1 ATOM 1261 O O . PHE A 1 163 ? 15.194 13.562 6.378 1.00 13.24 ? 1160 PHE A O 1 ATOM 1262 C CB . PHE A 1 163 ? 12.118 14.077 7.537 1.00 13.31 ? 1160 PHE A CB 1 ATOM 1263 C CG . PHE A 1 163 ? 11.265 15.195 8.104 1.00 13.56 ? 1160 PHE A CG 1 ATOM 1264 C CD1 . PHE A 1 163 ? 11.256 16.472 7.546 1.00 14.65 ? 1160 PHE A CD1 1 ATOM 1265 C CD2 . PHE A 1 163 ? 10.486 14.958 9.210 1.00 14.06 ? 1160 PHE A CD2 1 ATOM 1266 C CE1 . PHE A 1 163 ? 10.455 17.484 8.094 1.00 14.87 ? 1160 PHE A CE1 1 ATOM 1267 C CE2 . PHE A 1 163 ? 9.680 15.952 9.758 1.00 13.77 ? 1160 PHE A CE2 1 ATOM 1268 C CZ . PHE A 1 163 ? 9.680 17.211 9.215 1.00 14.71 ? 1160 PHE A CZ 1 ATOM 1269 N N . LYS A 1 164 ? 13.616 12.306 5.389 1.00 12.88 ? 1161 LYS A N 1 ATOM 1270 C CA . LYS A 1 164 ? 14.591 11.267 5.002 1.00 13.43 ? 1161 LYS A CA 1 ATOM 1271 C C . LYS A 1 164 ? 15.644 11.847 4.082 1.00 12.49 ? 1161 LYS A C 1 ATOM 1272 O O . LYS A 1 164 ? 16.840 11.547 4.243 1.00 12.93 ? 1161 LYS A O 1 ATOM 1273 C CB . LYS A 1 164 ? 13.931 10.072 4.319 1.00 14.32 ? 1161 LYS A CB 1 ATOM 1274 C CG . LYS A 1 164 ? 13.158 9.217 5.300 1.00 18.69 ? 1161 LYS A CG 1 ATOM 1275 C CD . LYS A 1 164 ? 12.722 7.915 4.699 1.00 21.76 ? 1161 LYS A CD 1 ATOM 1276 C CE . LYS A 1 164 ? 11.544 8.133 3.784 1.00 24.97 ? 1161 LYS A CE 1 ATOM 1277 N NZ . LYS A 1 164 ? 10.552 7.040 3.999 1.00 25.44 ? 1161 LYS A NZ 1 ATOM 1278 N N . ARG A 1 165 ? 15.228 12.667 3.131 1.00 12.06 ? 1162 ARG A N 1 ATOM 1279 C CA . ARG A 1 165 ? 16.176 13.289 2.188 1.00 12.25 ? 1162 ARG A CA 1 ATOM 1280 C C . ARG A 1 165 ? 17.216 14.101 2.959 1.00 11.93 ? 1162 ARG A C 1 ATOM 1281 O O . ARG A 1 165 ? 18.417 14.040 2.656 1.00 12.93 ? 1162 ARG A O 1 ATOM 1282 C CB . ARG A 1 165 ? 15.455 14.215 1.215 1.00 12.87 ? 1162 ARG A CB 1 ATOM 1283 C CG . ARG A 1 165 ? 16.381 14.864 0.168 1.00 14.02 ? 1162 ARG A CG 1 ATOM 1284 C CD . ARG A 1 165 ? 15.773 16.115 -0.432 1.00 16.03 ? 1162 ARG A CD 1 ATOM 1285 N NE . ARG A 1 165 ? 15.878 17.258 0.484 1.00 16.82 ? 1162 ARG A NE 1 ATOM 1286 C CZ . ARG A 1 165 ? 14.853 17.965 0.947 1.00 15.46 ? 1162 ARG A CZ 1 ATOM 1287 N NH1 . ARG A 1 165 ? 13.592 17.641 0.624 1.00 18.03 ? 1162 ARG A NH1 1 ATOM 1288 N NH2 . ARG A 1 165 ? 15.065 18.987 1.752 1.00 17.65 ? 1162 ARG A NH2 1 ATOM 1289 N N . GLN A 1 166 ? 16.770 14.861 3.951 1.00 12.32 ? 1163 GLN A N 1 ATOM 1290 C CA . GLN A 1 166 ? 17.668 15.710 4.753 1.00 12.31 ? 1163 GLN A CA 1 ATOM 1291 C C . GLN A 1 166 ? 18.657 14.885 5.565 1.00 12.52 ? 1163 GLN A C 1 ATOM 1292 O O . GLN A 1 166 ? 19.836 15.263 5.690 1.00 13.84 ? 1163 GLN A O 1 ATOM 1293 C CB . GLN A 1 166 ? 16.868 16.659 5.638 1.00 12.54 ? 1163 GLN A CB 1 ATOM 1294 C CG . GLN A 1 166 ? 16.171 17.712 4.786 1.00 13.50 ? 1163 GLN A CG 1 ATOM 1295 C CD . GLN A 1 166 ? 15.263 18.590 5.618 1.00 14.05 ? 1163 GLN A CD 1 ATOM 1296 O OE1 . GLN A 1 166 ? 15.714 19.227 6.580 1.00 16.73 ? 1163 GLN A OE1 1 ATOM 1297 N NE2 . GLN A 1 166 ? 13.970 18.657 5.244 1.00 15.99 ? 1163 GLN A NE2 1 ATOM 1298 N N . ILE A 1 167 ? 18.229 13.758 6.111 1.00 12.06 ? 1164 ILE A N 1 ATOM 1299 C CA . ILE A 1 167 ? 19.122 12.845 6.808 1.00 12.76 ? 1164 ILE A CA 1 ATOM 1300 C C . ILE A 1 167 ? 20.155 12.293 5.828 1.00 13.08 ? 1164 ILE A C 1 ATOM 1301 O O . ILE A 1 167 ? 21.360 12.235 6.152 1.00 13.75 ? 1164 ILE A O 1 ATOM 1302 C CB . ILE A 1 167 ? 18.360 11.675 7.463 1.00 13.19 ? 1164 ILE A CB 1 ATOM 1303 C CG1 . ILE A 1 167 ? 17.485 12.214 8.607 1.00 14.54 ? 1164 ILE A CG1 1 ATOM 1304 C CG2 . ILE A 1 167 ? 19.328 10.586 7.945 1.00 14.43 ? 1164 ILE A CG2 1 ATOM 1305 C CD1 . ILE A 1 167 ? 18.270 12.566 9.848 1.00 17.86 ? 1164 ILE A CD1 1 ATOM 1306 N N . ILE A 1 168 ? 19.716 11.869 4.651 1.00 12.68 ? 1165 ILE A N 1 ATOM 1307 C CA . ILE A 1 168 ? 20.642 11.315 3.662 1.00 13.20 ? 1165 ILE A CA 1 ATOM 1308 C C . ILE A 1 168 ? 21.676 12.353 3.253 1.00 13.49 ? 1165 ILE A C 1 ATOM 1309 O O . ILE A 1 168 ? 22.887 12.043 3.126 1.00 14.94 ? 1165 ILE A O 1 ATOM 1310 C CB . ILE A 1 168 ? 19.871 10.786 2.422 1.00 12.96 ? 1165 ILE A CB 1 ATOM 1311 C CG1 . ILE A 1 168 ? 19.092 9.519 2.808 1.00 13.98 ? 1165 ILE A CG1 1 ATOM 1312 C CG2 . ILE A 1 168 ? 20.813 10.508 1.251 1.00 15.49 ? 1165 ILE A CG2 1 ATOM 1313 C CD1 . ILE A 1 168 ? 17.922 9.222 1.872 1.00 15.36 ? 1165 ILE A CD1 1 ATOM 1314 N N . GLU A 1 169 ? 21.242 13.581 3.006 1.00 14.05 ? 1166 GLU A N 1 ATOM 1315 C CA . GLU A 1 169 ? 22.167 14.666 2.625 1.00 15.72 ? 1166 GLU A CA 1 ATOM 1316 C C . GLU A 1 169 ? 23.228 14.922 3.701 1.00 16.32 ? 1166 GLU A C 1 ATOM 1317 O O . GLU A 1 169 ? 24.429 15.048 3.403 1.00 18.77 ? 1166 GLU A O 1 ATOM 1318 C CB . GLU A 1 169 ? 21.384 15.947 2.337 1.00 16.51 ? 1166 GLU A CB 1 ATOM 1319 C CG . GLU A 1 169 ? 20.546 15.850 1.079 1.00 17.77 ? 1166 GLU A CG 1 ATOM 1320 C CD . GLU A 1 169 ? 19.459 16.915 0.990 1.00 21.46 ? 1166 GLU A CD 1 ATOM 1321 O OE1 . GLU A 1 169 ? 19.162 17.598 1.999 1.00 23.81 ? 1166 GLU A OE1 1 ATOM 1322 O OE2 . GLU A 1 169 ? 18.897 17.074 -0.113 1.00 23.76 ? 1166 GLU A OE2 1 ATOM 1323 N N . LYS A 1 170 ? 22.798 14.994 4.961 1.00 16.60 ? 1167 LYS A N 1 ATOM 1324 C CA . LYS A 1 170 ? 23.703 15.331 6.059 1.00 16.87 ? 1167 LYS A CA 1 ATOM 1325 C C . LYS A 1 170 ? 24.689 14.210 6.403 1.00 16.31 ? 1167 LYS A C 1 ATOM 1326 O O . LYS A 1 170 ? 25.896 14.451 6.572 1.00 17.98 ? 1167 LYS A O 1 ATOM 1327 C CB . LYS A 1 170 ? 22.878 15.682 7.305 1.00 17.64 ? 1167 LYS A CB 1 ATOM 1328 C CG . LYS A 1 170 ? 23.685 15.898 8.577 1.00 21.59 ? 1167 LYS A CG 1 ATOM 1329 C CD . LYS A 1 170 ? 24.322 17.271 8.631 1.00 26.41 ? 1167 LYS A CD 1 ATOM 1330 C CE . LYS A 1 170 ? 24.840 17.568 10.036 1.00 26.97 ? 1167 LYS A CE 1 ATOM 1331 N NZ . LYS A 1 170 ? 25.630 18.831 10.084 1.00 29.39 ? 1167 LYS A NZ 1 ATOM 1332 N N . TYR A 1 171 ? 24.192 12.983 6.495 1.00 15.80 ? 1168 TYR A N 1 ATOM 1333 C CA . TYR A 1 171 ? 24.966 11.898 7.090 1.00 16.26 ? 1168 TYR A CA 1 ATOM 1334 C C . TYR A 1 171 ? 25.478 10.857 6.103 1.00 16.33 ? 1168 TYR A C 1 ATOM 1335 O O . TYR A 1 171 ? 26.368 10.078 6.467 1.00 18.30 ? 1168 TYR A O 1 ATOM 1336 C CB . TYR A 1 171 ? 24.142 11.210 8.193 1.00 15.89 ? 1168 TYR A CB 1 ATOM 1337 C CG . TYR A 1 171 ? 23.803 12.153 9.321 1.00 15.31 ? 1168 TYR A CG 1 ATOM 1338 C CD1 . TYR A 1 171 ? 24.767 12.525 10.253 1.00 16.07 ? 1168 TYR A CD1 1 ATOM 1339 C CD2 . TYR A 1 171 ? 22.505 12.676 9.459 1.00 15.27 ? 1168 TYR A CD2 1 ATOM 1340 C CE1 . TYR A 1 171 ? 24.495 13.396 11.278 1.00 15.94 ? 1168 TYR A CE1 1 ATOM 1341 C CE2 . TYR A 1 171 ? 22.226 13.542 10.479 1.00 15.06 ? 1168 TYR A CE2 1 ATOM 1342 C CZ . TYR A 1 171 ? 23.200 13.902 11.400 1.00 15.10 ? 1168 TYR A CZ 1 ATOM 1343 O OH . TYR A 1 171 ? 22.901 14.782 12.419 1.00 16.98 ? 1168 TYR A OH 1 ATOM 1344 N N . VAL A 1 172 ? 24.945 10.833 4.884 1.00 16.94 ? 1169 VAL A N 1 ATOM 1345 C CA . VAL A 1 172 ? 25.348 9.824 3.904 1.00 19.42 ? 1169 VAL A CA 1 ATOM 1346 C C . VAL A 1 172 ? 26.101 10.414 2.709 1.00 22.34 ? 1169 VAL A C 1 ATOM 1347 O O . VAL A 1 172 ? 27.180 9.937 2.362 1.00 23.60 ? 1169 VAL A O 1 ATOM 1348 C CB . VAL A 1 172 ? 24.158 8.967 3.410 1.00 18.33 ? 1169 VAL A CB 1 ATOM 1349 C CG1 . VAL A 1 172 ? 24.650 7.899 2.431 1.00 20.33 ? 1169 VAL A CG1 1 ATOM 1350 C CG2 . VAL A 1 172 ? 23.450 8.323 4.584 1.00 19.34 ? 1169 VAL A CG2 1 ATOM 1351 N N A ILE A 1 173 ? 25.536 11.445 2.090 0.50 25.94 ? 1170 ILE A N 1 ATOM 1352 N N B ILE A 1 173 ? 25.537 11.439 2.079 0.50 25.94 ? 1170 ILE A N 1 ATOM 1353 C CA A ILE A 1 173 ? 26.162 12.092 0.940 0.50 32.66 ? 1170 ILE A CA 1 ATOM 1354 C CA B ILE A 1 173 ? 26.180 12.076 0.932 0.50 32.66 ? 1170 ILE A CA 1 ATOM 1355 C C A ILE A 1 173 ? 27.315 12.971 1.403 0.50 36.82 ? 1170 ILE A C 1 ATOM 1356 C C B ILE A 1 173 ? 27.270 13.027 1.419 0.50 36.81 ? 1170 ILE A C 1 ATOM 1357 O O A ILE A 1 173 ? 27.122 13.890 2.196 0.50 40.85 ? 1170 ILE A O 1 ATOM 1358 O O B ILE A 1 173 ? 27.016 13.900 2.250 0.50 40.85 ? 1170 ILE A O 1 ATOM 1359 C CB A ILE A 1 173 ? 25.158 12.967 0.147 0.50 32.66 ? 1170 ILE A CB 1 ATOM 1360 C CB B ILE A 1 173 ? 25.170 12.863 0.065 0.50 32.66 ? 1170 ILE A CB 1 ATOM 1361 C CG1 A ILE A 1 173 ? 23.922 12.148 -0.273 0.50 33.07 ? 1170 ILE A CG1 1 ATOM 1362 C CG1 B ILE A 1 173 ? 24.114 11.919 -0.515 0.50 33.06 ? 1170 ILE A CG1 1 ATOM 1363 C CG2 A ILE A 1 173 ? 25.846 13.613 -1.066 0.50 34.05 ? 1170 ILE A CG2 1 ATOM 1364 C CG2 B ILE A 1 173 ? 25.898 13.617 -1.052 0.50 34.05 ? 1170 ILE A CG2 1 ATOM 1365 C CD1 A ILE A 1 173 ? 24.248 10.789 -0.885 0.50 32.94 ? 1170 ILE A CD1 1 ATOM 1366 C CD1 B ILE A 1 173 ? 22.939 12.636 -1.178 0.50 33.14 ? 1170 ILE A CD1 1 HETATM 1367 P P . PO4 B 2 . ? 5.072 13.619 13.693 1.00 13.65 ? 1 PO4 A P 1 HETATM 1368 O O1 . PO4 B 2 . ? 6.106 14.649 13.264 1.00 13.51 ? 1 PO4 A O1 1 HETATM 1369 O O2 . PO4 B 2 . ? 4.360 13.130 12.425 1.00 14.95 ? 1 PO4 A O2 1 HETATM 1370 O O3 . PO4 B 2 . ? 5.643 12.397 14.359 1.00 13.69 ? 1 PO4 A O3 1 HETATM 1371 O O4 . PO4 B 2 . ? 4.038 14.233 14.641 1.00 14.45 ? 1 PO4 A O4 1 HETATM 1372 C C1 . BME C 3 . ? 4.781 11.652 4.964 0.50 27.69 ? 1174 BME A C1 1 HETATM 1373 C C2 . BME C 3 . ? 4.822 11.780 6.481 0.50 29.48 ? 1174 BME A C2 1 HETATM 1374 O O1 . BME C 3 . ? 4.809 12.940 4.394 0.50 30.81 ? 1174 BME A O1 1 HETATM 1375 S S2 . BME C 3 . ? 3.897 10.470 7.314 0.50 37.46 ? 1174 BME A S2 1 HETATM 1376 C C1 . BME D 3 . ? 31.941 5.668 9.642 1.00 45.25 ? 2 BME A C1 1 HETATM 1377 C C2 . BME D 3 . ? 32.113 7.084 9.118 1.00 46.23 ? 2 BME A C2 1 HETATM 1378 O O1 . BME D 3 . ? 32.848 4.826 8.968 1.00 44.94 ? 2 BME A O1 1 HETATM 1379 S S2 . BME D 3 . ? 30.905 8.216 9.837 1.00 49.10 ? 2 BME A S2 1 HETATM 1380 O O . HOH E 4 . ? 22.648 -5.597 8.297 1.00 36.79 ? 1175 HOH A O 1 HETATM 1381 O O . HOH E 4 . ? 25.181 8.246 23.385 1.00 38.19 ? 1176 HOH A O 1 HETATM 1382 O O . HOH E 4 . ? 10.298 -1.929 0.772 1.00 38.08 ? 1177 HOH A O 1 HETATM 1383 O O . HOH E 4 . ? 20.996 2.776 29.976 1.00 35.56 ? 1178 HOH A O 1 HETATM 1384 O O . HOH E 4 . ? 22.824 18.903 28.988 1.00 39.30 ? 1179 HOH A O 1 HETATM 1385 O O . HOH E 4 . ? 20.332 6.040 37.438 1.00 35.00 ? 1180 HOH A O 1 HETATM 1386 O O . HOH E 4 . ? 8.556 28.226 27.113 1.00 37.96 ? 1181 HOH A O 1 HETATM 1387 O O . HOH E 4 . ? 8.576 -4.758 7.515 1.00 37.60 ? 1182 HOH A O 1 HETATM 1388 O O . HOH E 4 . ? 16.328 -14.416 3.423 1.00 35.16 ? 1183 HOH A O 1 HETATM 1389 O O . HOH E 4 . ? 8.982 27.703 21.295 1.00 38.67 ? 1184 HOH A O 1 HETATM 1390 O O . HOH E 4 . ? 11.882 -7.740 3.809 1.00 40.22 ? 1185 HOH A O 1 HETATM 1391 O O . HOH E 4 . ? -2.145 14.681 26.957 1.00 38.54 ? 1186 HOH A O 1 HETATM 1392 O O . HOH E 4 . ? 14.138 22.403 34.616 1.00 38.20 ? 1187 HOH A O 1 HETATM 1393 O O . HOH E 4 . ? 10.296 13.719 35.223 1.00 40.24 ? 1188 HOH A O 1 HETATM 1394 O O . HOH E 4 . ? 7.939 25.195 6.494 1.00 39.60 ? 1189 HOH A O 1 HETATM 1395 O O . HOH E 4 . ? 1.749 26.482 28.080 1.00 38.98 ? 1190 HOH A O 1 HETATM 1396 O O . HOH E 4 . ? 35.341 9.788 14.757 1.00 39.69 ? 1191 HOH A O 1 HETATM 1397 O O . HOH E 4 . ? 14.746 25.685 20.914 1.00 36.41 ? 1192 HOH A O 1 HETATM 1398 O O . HOH E 4 . ? 24.346 -0.195 26.947 1.00 38.76 ? 1193 HOH A O 1 HETATM 1399 O O . HOH E 4 . ? 6.857 22.869 25.455 1.00 19.27 ? 1194 HOH A O 1 HETATM 1400 O O . HOH E 4 . ? 34.800 -0.048 11.826 1.00 21.38 ? 1195 HOH A O 1 HETATM 1401 O O . HOH E 4 . ? 2.358 17.922 35.117 1.00 20.63 ? 1196 HOH A O 1 HETATM 1402 O O . HOH E 4 . ? 8.782 6.113 15.071 1.00 16.02 ? 1197 HOH A O 1 HETATM 1403 O O . HOH E 4 . ? 9.555 10.684 34.609 1.00 28.19 ? 1198 HOH A O 1 HETATM 1404 O O . HOH E 4 . ? 1.497 14.484 13.350 1.00 24.30 ? 1199 HOH A O 1 HETATM 1405 O O . HOH E 4 . ? 5.114 6.284 20.544 1.00 22.44 ? 1200 HOH A O 1 HETATM 1406 O O . HOH E 4 . ? -0.069 22.867 38.698 1.00 26.53 ? 1201 HOH A O 1 HETATM 1407 O O . HOH E 4 . ? 26.906 7.774 10.147 1.00 20.77 ? 1202 HOH A O 1 HETATM 1408 O O . HOH E 4 . ? 27.027 18.131 17.125 1.00 38.65 ? 1203 HOH A O 1 HETATM 1409 O O . HOH E 4 . ? 2.148 6.730 27.079 1.00 27.33 ? 1204 HOH A O 1 HETATM 1410 O O . HOH E 4 . ? 30.244 3.700 16.184 1.00 32.35 ? 1205 HOH A O 1 HETATM 1411 O O . HOH E 4 . ? 1.443 7.514 17.555 1.00 23.79 ? 1206 HOH A O 1 HETATM 1412 O O . HOH E 4 . ? 14.512 18.116 35.198 1.00 32.56 ? 1207 HOH A O 1 HETATM 1413 O O . HOH E 4 . ? 28.049 9.883 8.557 1.00 25.71 ? 1208 HOH A O 1 HETATM 1414 O O . HOH E 4 . ? 6.163 8.225 28.772 1.00 26.66 ? 1209 HOH A O 1 HETATM 1415 O O . HOH E 4 . ? 22.177 22.776 14.910 1.00 22.04 ? 1210 HOH A O 1 HETATM 1416 O O . HOH E 4 . ? 24.973 15.618 13.983 1.00 25.12 ? 1211 HOH A O 1 HETATM 1417 O O . HOH E 4 . ? 22.576 21.214 11.953 1.00 26.39 ? 1212 HOH A O 1 HETATM 1418 O O . HOH E 4 . ? 8.922 24.252 26.825 1.00 22.01 ? 1213 HOH A O 1 HETATM 1419 O O . HOH E 4 . ? 17.814 18.868 -1.812 1.00 21.18 ? 1214 HOH A O 1 HETATM 1420 O O . HOH E 4 . ? 10.542 19.064 5.020 1.00 22.88 ? 1215 HOH A O 1 HETATM 1421 O O . HOH E 4 . ? 8.434 4.924 4.521 1.00 26.56 ? 1216 HOH A O 1 HETATM 1422 O O . HOH E 4 . ? -3.978 6.156 29.168 1.00 41.47 ? 1217 HOH A O 1 HETATM 1423 O O . HOH E 4 . ? 6.438 22.509 32.975 1.00 24.95 ? 1218 HOH A O 1 HETATM 1424 O O . HOH E 4 . ? 7.019 24.578 28.724 1.00 23.58 ? 1219 HOH A O 1 HETATM 1425 O O . HOH E 4 . ? 27.565 16.513 23.201 1.00 34.37 ? 1220 HOH A O 1 HETATM 1426 O O . HOH E 4 . ? 12.145 26.275 15.829 1.00 28.79 ? 1221 HOH A O 1 HETATM 1427 O O . HOH E 4 . ? 9.990 26.674 25.896 1.00 35.29 ? 1222 HOH A O 1 HETATM 1428 O O . HOH E 4 . ? 11.850 15.909 -0.678 1.00 26.07 ? 1223 HOH A O 1 HETATM 1429 O O . HOH E 4 . ? 10.458 23.169 31.568 1.00 27.76 ? 1224 HOH A O 1 HETATM 1430 O O . HOH E 4 . ? 0.363 6.372 22.695 1.00 44.54 ? 1225 HOH A O 1 HETATM 1431 O O . HOH E 4 . ? 24.505 4.799 16.401 1.00 30.77 ? 1226 HOH A O 1 HETATM 1432 O O . HOH E 4 . ? 28.395 5.334 2.735 1.00 28.21 ? 1227 HOH A O 1 HETATM 1433 O O . HOH E 4 . ? 12.709 25.472 8.831 1.00 38.00 ? 1228 HOH A O 1 HETATM 1434 O O . HOH E 4 . ? 9.396 -0.184 21.439 1.00 37.81 ? 1229 HOH A O 1 HETATM 1435 O O . HOH E 4 . ? 22.198 16.477 29.233 1.00 28.07 ? 1230 HOH A O 1 HETATM 1436 O O . HOH E 4 . ? 4.010 5.658 4.910 1.00 39.83 ? 1231 HOH A O 1 HETATM 1437 O O . HOH E 4 . ? 1.194 21.054 18.653 1.00 33.60 ? 1232 HOH A O 1 HETATM 1438 O O . HOH E 4 . ? 20.575 17.961 5.369 1.00 27.49 ? 1233 HOH A O 1 HETATM 1439 O O . HOH E 4 . ? 16.620 21.469 3.931 1.00 27.53 ? 1234 HOH A O 1 HETATM 1440 O O . HOH E 4 . ? 0.666 17.055 13.499 1.00 42.92 ? 1235 HOH A O 1 HETATM 1441 O O . HOH E 4 . ? 30.209 -1.177 7.429 1.00 38.12 ? 1236 HOH A O 1 HETATM 1442 O O . HOH E 4 . ? 12.617 25.592 25.336 1.00 31.05 ? 1237 HOH A O 1 HETATM 1443 O O . HOH E 4 . ? 23.527 24.076 11.173 1.00 45.30 ? 1238 HOH A O 1 HETATM 1444 O O . HOH E 4 . ? 28.738 15.951 20.790 1.00 36.39 ? 1239 HOH A O 1 HETATM 1445 O O . HOH E 4 . ? 23.383 3.412 24.991 1.00 33.76 ? 1240 HOH A O 1 HETATM 1446 O O . HOH E 4 . ? 13.943 -8.629 5.098 1.00 40.10 ? 1241 HOH A O 1 HETATM 1447 O O . HOH E 4 . ? 27.172 10.085 24.609 1.00 33.43 ? 1242 HOH A O 1 HETATM 1448 O O . HOH E 4 . ? 10.997 19.345 0.000 0.50 30.21 ? 1243 HOH A O 1 HETATM 1449 O O . HOH E 4 . ? 7.975 21.028 34.421 1.00 34.34 ? 1244 HOH A O 1 HETATM 1450 O O . HOH E 4 . ? 2.468 15.335 36.389 1.00 35.39 ? 1245 HOH A O 1 HETATM 1451 O O . HOH E 4 . ? 16.865 5.360 31.014 1.00 46.69 ? 1246 HOH A O 1 HETATM 1452 O O . HOH E 4 . ? 26.378 12.749 18.580 1.00 30.98 ? 1247 HOH A O 1 HETATM 1453 O O . HOH E 4 . ? -0.332 10.773 20.966 1.00 32.00 ? 1248 HOH A O 1 HETATM 1454 O O . HOH E 4 . ? 11.824 13.301 36.898 1.00 44.93 ? 1249 HOH A O 1 HETATM 1455 O O . HOH E 4 . ? 20.347 26.214 18.304 1.00 43.13 ? 1250 HOH A O 1 HETATM 1456 O O . HOH E 4 . ? 4.324 14.598 6.541 1.00 41.61 ? 1251 HOH A O 1 HETATM 1457 O O . HOH E 4 . ? 8.621 24.245 10.740 1.00 29.74 ? 1252 HOH A O 1 HETATM 1458 O O . HOH E 4 . ? 11.778 0.135 24.369 1.00 36.76 ? 1253 HOH A O 1 HETATM 1459 O O . HOH E 4 . ? 9.888 -0.758 35.513 1.00 31.51 ? 1254 HOH A O 1 HETATM 1460 O O . HOH E 4 . ? 4.780 3.763 26.575 1.00 35.74 ? 1255 HOH A O 1 HETATM 1461 O O . HOH E 4 . ? 23.282 21.301 22.028 1.00 32.04 ? 1256 HOH A O 1 HETATM 1462 O O . HOH E 4 . ? 7.941 14.365 37.260 1.00 40.08 ? 1257 HOH A O 1 HETATM 1463 O O . HOH E 4 . ? 1.722 14.849 10.450 1.00 31.15 ? 1258 HOH A O 1 HETATM 1464 O O . HOH E 4 . ? 1.723 19.389 21.108 1.00 31.25 ? 1259 HOH A O 1 HETATM 1465 O O . HOH E 4 . ? 13.879 -0.704 22.992 1.00 44.41 ? 1260 HOH A O 1 HETATM 1466 O O . HOH E 4 . ? 25.482 -11.939 5.879 1.00 50.43 ? 1261 HOH A O 1 HETATM 1467 O O . HOH E 4 . ? 18.477 26.238 19.621 1.00 43.72 ? 1262 HOH A O 1 HETATM 1468 O O . HOH E 4 . ? 5.501 1.916 19.505 1.00 42.46 ? 1263 HOH A O 1 HETATM 1469 O O . HOH E 4 . ? 19.222 6.496 33.257 1.00 47.53 ? 1264 HOH A O 1 HETATM 1470 O O . HOH E 4 . ? 2.919 27.620 21.884 1.00 35.66 ? 1265 HOH A O 1 HETATM 1471 O O . HOH E 4 . ? 17.790 26.660 6.901 1.00 37.21 ? 1266 HOH A O 1 HETATM 1472 O O . HOH E 4 . ? 29.388 10.115 12.889 1.00 32.49 ? 1267 HOH A O 1 HETATM 1473 O O . HOH E 4 . ? -0.461 13.107 14.399 1.00 42.40 ? 1268 HOH A O 1 HETATM 1474 O O . HOH E 4 . ? 5.386 24.449 34.654 1.00 34.98 ? 1269 HOH A O 1 HETATM 1475 O O . HOH E 4 . ? 34.451 7.195 11.435 1.00 37.54 ? 1270 HOH A O 1 HETATM 1476 O O . HOH E 4 . ? 29.092 18.998 20.837 1.00 49.68 ? 1271 HOH A O 1 HETATM 1477 O O . HOH E 4 . ? 20.373 20.791 35.414 1.00 37.23 ? 1272 HOH A O 1 HETATM 1478 O O . HOH E 4 . ? 3.450 6.899 32.517 1.00 34.85 ? 1273 HOH A O 1 HETATM 1479 O O . HOH E 4 . ? 26.656 21.693 18.206 1.00 48.01 ? 1274 HOH A O 1 HETATM 1480 O O . HOH E 4 . ? 18.687 23.923 20.216 1.00 45.95 ? 1275 HOH A O 1 HETATM 1481 O O . HOH E 4 . ? 10.114 25.187 12.410 1.00 40.92 ? 1276 HOH A O 1 HETATM 1482 O O . HOH E 4 . ? 12.289 13.441 -1.370 1.00 40.23 ? 1277 HOH A O 1 HETATM 1483 O O . HOH E 4 . ? 5.331 -2.750 14.826 1.00 47.31 ? 1278 HOH A O 1 HETATM 1484 O O . HOH E 4 . ? 6.985 3.981 31.046 1.00 41.57 ? 1279 HOH A O 1 HETATM 1485 O O . HOH E 4 . ? 25.298 8.891 36.418 1.00 41.35 ? 1280 HOH A O 1 HETATM 1486 O O . HOH E 4 . ? 29.884 7.424 19.008 1.00 38.76 ? 1281 HOH A O 1 HETATM 1487 O O . HOH E 4 . ? 0.820 17.106 19.696 1.00 35.34 ? 1282 HOH A O 1 HETATM 1488 O O . HOH E 4 . ? 12.189 25.757 4.768 1.00 50.06 ? 1283 HOH A O 1 HETATM 1489 O O . HOH E 4 . ? -1.312 19.848 25.688 1.00 27.43 ? 1284 HOH A O 1 HETATM 1490 O O . HOH E 4 . ? 24.215 20.345 24.312 1.00 39.40 ? 1285 HOH A O 1 HETATM 1491 O O . HOH E 4 . ? 11.109 -1.502 7.684 1.00 36.26 ? 1286 HOH A O 1 HETATM 1492 O O . HOH E 4 . ? 2.152 11.565 33.908 1.00 41.22 ? 1287 HOH A O 1 HETATM 1493 O O . HOH E 4 . ? 24.875 -5.025 7.853 1.00 49.77 ? 1288 HOH A O 1 HETATM 1494 O O . HOH E 4 . ? 23.178 21.842 37.325 1.00 45.43 ? 1289 HOH A O 1 HETATM 1495 O O . HOH E 4 . ? 7.881 24.098 31.215 1.00 26.99 ? 1290 HOH A O 1 HETATM 1496 O O . HOH E 4 . ? 12.594 26.235 12.075 1.00 42.32 ? 1291 HOH A O 1 HETATM 1497 O O . HOH E 4 . ? 24.740 5.496 24.008 1.00 60.68 ? 1292 HOH A O 1 HETATM 1498 O O . HOH E 4 . ? 20.676 25.244 16.245 1.00 43.67 ? 1293 HOH A O 1 HETATM 1499 O O . HOH E 4 . ? 7.950 11.326 -2.275 1.00 44.53 ? 1294 HOH A O 1 HETATM 1500 O O . HOH E 4 . ? 11.493 27.410 21.793 1.00 35.95 ? 1295 HOH A O 1 HETATM 1501 O O . HOH E 4 . ? 18.949 12.597 35.675 1.00 49.13 ? 1296 HOH A O 1 HETATM 1502 O O . HOH E 4 . ? 2.588 10.806 10.971 1.00 40.48 ? 1297 HOH A O 1 HETATM 1503 O O . HOH E 4 . ? 10.686 -11.520 2.279 1.00 42.88 ? 1298 HOH A O 1 HETATM 1504 O O . HOH E 4 . ? 16.993 25.440 32.647 1.00 42.06 ? 1299 HOH A O 1 HETATM 1505 O O . HOH E 4 . ? 19.906 4.074 33.666 1.00 44.02 ? 1300 HOH A O 1 HETATM 1506 O O . HOH E 4 . ? 13.956 14.116 -2.989 1.00 34.06 ? 1301 HOH A O 1 HETATM 1507 O O . HOH E 4 . ? 18.937 21.910 21.262 1.00 42.39 ? 1302 HOH A O 1 HETATM 1508 O O . HOH E 4 . ? 20.506 27.029 14.580 1.00 42.68 ? 1303 HOH A O 1 HETATM 1509 O O . HOH E 4 . ? 14.076 16.778 -3.541 1.00 37.69 ? 1304 HOH A O 1 HETATM 1510 O O . HOH E 4 . ? 26.922 15.574 18.190 1.00 37.07 ? 1305 HOH A O 1 HETATM 1511 O O . HOH E 4 . ? 5.204 27.585 18.095 1.00 32.06 ? 1306 HOH A O 1 HETATM 1512 O O . HOH E 4 . ? 16.233 20.552 34.976 1.00 56.40 ? 1307 HOH A O 1 HETATM 1513 O O . HOH E 4 . ? -1.256 1.524 15.930 1.00 47.26 ? 1308 HOH A O 1 HETATM 1514 O O . HOH E 4 . ? 30.833 10.461 16.911 1.00 51.40 ? 1309 HOH A O 1 HETATM 1515 O O . HOH E 4 . ? 7.309 28.654 16.191 1.00 47.33 ? 1310 HOH A O 1 HETATM 1516 O O . HOH E 4 . ? 24.732 24.691 15.253 1.00 50.64 ? 1311 HOH A O 1 HETATM 1517 O O . HOH E 4 . ? 13.571 -4.242 14.694 1.00 34.99 ? 1312 HOH A O 1 HETATM 1518 O O . HOH E 4 . ? 23.255 20.572 9.350 1.00 49.90 ? 1313 HOH A O 1 HETATM 1519 O O . HOH E 4 . ? 16.702 11.240 36.290 1.00 41.59 ? 1314 HOH A O 1 HETATM 1520 O O . HOH E 4 . ? 4.146 20.210 2.820 1.00 37.07 ? 1315 HOH A O 1 HETATM 1521 O O . HOH E 4 . ? 8.762 -2.118 7.196 1.00 42.09 ? 1316 HOH A O 1 HETATM 1522 O O . HOH E 4 . ? 27.849 1.903 14.334 1.00 50.40 ? 1317 HOH A O 1 HETATM 1523 O O . HOH E 4 . ? 2.151 25.966 33.710 1.00 44.33 ? 1318 HOH A O 1 HETATM 1524 O O . HOH E 4 . ? 8.702 -7.732 -2.519 1.00 43.32 ? 1319 HOH A O 1 HETATM 1525 O O . HOH E 4 . ? 0.420 20.851 23.294 1.00 36.95 ? 1320 HOH A O 1 HETATM 1526 O O . HOH E 4 . ? -1.924 3.087 12.267 1.00 47.14 ? 1321 HOH A O 1 HETATM 1527 O O . HOH E 4 . ? 3.570 27.731 27.443 1.00 42.16 ? 1322 HOH A O 1 HETATM 1528 O O . HOH E 4 . ? 3.142 3.040 4.431 1.00 37.95 ? 1323 HOH A O 1 HETATM 1529 O O . HOH E 4 . ? 28.059 -7.298 -1.215 1.00 41.97 ? 1324 HOH A O 1 HETATM 1530 O O . HOH E 4 . ? 12.312 0.000 0.000 0.50 45.50 ? 1325 HOH A O 1 HETATM 1531 O O . HOH E 4 . ? 1.818 -4.987 6.139 1.00 52.01 ? 1326 HOH A O 1 HETATM 1532 O O . HOH E 4 . ? -0.268 5.059 30.095 1.00 56.31 ? 1327 HOH A O 1 HETATM 1533 O O . HOH E 4 . ? 15.211 24.333 34.215 1.00 50.43 ? 1328 HOH A O 1 HETATM 1534 O O . HOH E 4 . ? 8.524 15.572 39.127 1.00 39.77 ? 1329 HOH A O 1 HETATM 1535 O O . HOH E 4 . ? 22.545 14.178 36.424 1.00 49.07 ? 1330 HOH A O 1 HETATM 1536 O O . HOH E 4 . ? 13.803 1.920 30.583 1.00 37.47 ? 1331 HOH A O 1 HETATM 1537 O O . HOH E 4 . ? 9.445 12.038 36.894 1.00 53.31 ? 1332 HOH A O 1 HETATM 1538 O O . HOH E 4 . ? 22.991 3.973 31.479 1.00 53.92 ? 1333 HOH A O 1 HETATM 1539 O O . HOH E 4 . ? -2.715 12.347 27.171 1.00 54.74 ? 1334 HOH A O 1 HETATM 1540 O O . HOH E 4 . ? 27.330 3.604 17.256 1.00 46.97 ? 1335 HOH A O 1 HETATM 1541 O O . HOH E 4 . ? 29.115 11.725 18.520 1.00 41.24 ? 1336 HOH A O 1 HETATM 1542 O O . HOH E 4 . ? -4.448 2.101 10.325 1.00 52.05 ? 1337 HOH A O 1 HETATM 1543 O O . HOH E 4 . ? 24.670 -14.104 8.565 1.00 44.47 ? 1338 HOH A O 1 HETATM 1544 O O . HOH E 4 . ? 15.738 -1.052 28.257 1.00 45.68 ? 1339 HOH A O 1 HETATM 1545 O O . HOH E 4 . ? 7.268 -0.429 19.725 1.00 42.19 ? 1340 HOH A O 1 HETATM 1546 O O . HOH E 4 . ? 20.690 2.549 32.149 1.00 51.62 ? 1341 HOH A O 1 HETATM 1547 O O . HOH E 4 . ? -0.899 4.961 19.122 1.00 40.43 ? 1342 HOH A O 1 HETATM 1548 O O . HOH E 4 . ? 14.382 -10.861 6.112 1.00 41.11 ? 1343 HOH A O 1 HETATM 1549 O O . HOH E 4 . ? -0.263 16.178 36.365 1.00 48.17 ? 1344 HOH A O 1 HETATM 1550 O O . HOH E 4 . ? 24.974 -10.257 9.088 1.00 48.08 ? 1345 HOH A O 1 HETATM 1551 O O . HOH E 4 . ? 22.924 27.781 14.020 1.00 45.94 ? 1346 HOH A O 1 HETATM 1552 O O . HOH E 4 . ? 19.389 0.843 16.656 1.00 48.43 ? 1347 HOH A O 1 HETATM 1553 O O . HOH E 4 . ? -4.033 -2.128 8.786 1.00 46.99 ? 1348 HOH A O 1 HETATM 1554 O O . HOH E 4 . ? 16.053 -11.883 4.833 1.00 48.50 ? 1349 HOH A O 1 HETATM 1555 O O . HOH E 4 . ? 24.711 -11.581 10.942 1.00 43.65 ? 1350 HOH A O 1 HETATM 1556 O O . HOH E 4 . ? -3.023 11.943 21.905 1.00 57.73 ? 1351 HOH A O 1 HETATM 1557 O O . HOH E 4 . ? 10.593 28.826 15.161 1.00 49.35 ? 1352 HOH A O 1 HETATM 1558 O O . HOH E 4 . ? 13.134 -9.857 7.748 1.00 45.32 ? 1353 HOH A O 1 HETATM 1559 O O . HOH E 4 . ? 20.159 16.424 37.318 1.00 45.28 ? 1354 HOH A O 1 HETATM 1560 O O . HOH E 4 . ? 23.024 -16.039 1.684 1.00 45.03 ? 1355 HOH A O 1 HETATM 1561 O O . HOH E 4 . ? 17.974 15.002 37.299 1.00 42.88 ? 1356 HOH A O 1 HETATM 1562 O O . HOH E 4 . ? 15.445 15.796 37.055 1.00 47.15 ? 1357 HOH A O 1 HETATM 1563 O O . HOH E 4 . ? 18.719 18.610 38.276 1.00 39.75 ? 1358 HOH A O 1 HETATM 1564 O O . HOH E 4 . ? 18.310 -9.835 10.927 1.00 41.73 ? 1359 HOH A O 1 HETATM 1565 O O . HOH E 4 . ? 3.309 14.282 38.426 1.00 44.85 ? 1360 HOH A O 1 HETATM 1566 O O . HOH E 4 . ? 2.816 12.059 37.932 1.00 55.50 ? 1361 HOH A O 1 HETATM 1567 O O . HOH E 4 . ? 0.514 10.380 34.980 1.00 49.52 ? 1362 HOH A O 1 HETATM 1568 O O . HOH E 4 . ? -4.409 3.437 13.568 1.00 54.60 ? 1363 HOH A O 1 HETATM 1569 O O . HOH E 4 . ? 1.365 3.487 29.707 1.00 49.89 ? 1364 HOH A O 1 HETATM 1570 O O . HOH E 4 . ? 0.483 24.964 30.077 1.00 40.90 ? 1365 HOH A O 1 HETATM 1571 O O . HOH E 4 . ? 5.789 28.689 21.165 1.00 58.42 ? 1366 HOH A O 1 HETATM 1572 O O . HOH E 4 . ? 8.802 26.698 14.172 1.00 44.58 ? 1367 HOH A O 1 HETATM 1573 O O . HOH E 4 . ? 28.724 -1.326 21.595 1.00 60.18 ? 1368 HOH A O 1 HETATM 1574 O O . HOH E 4 . ? 29.053 14.778 29.570 1.00 44.96 ? 1369 HOH A O 1 HETATM 1575 O O . HOH E 4 . ? 12.253 18.646 -2.519 1.00 34.27 ? 1370 HOH A O 1 HETATM 1576 O O . HOH E 4 . ? 33.371 1.678 7.700 1.00 41.49 ? 1371 HOH A O 1 HETATM 1577 O O . HOH E 4 . ? 4.293 5.884 28.378 1.00 40.53 ? 1372 HOH A O 1 HETATM 1578 O O . HOH E 4 . ? 0.000 17.424 33.744 0.50 51.54 ? 1373 HOH A O 1 HETATM 1579 O O . HOH E 4 . ? 24.197 6.168 28.863 1.00 46.74 ? 1374 HOH A O 1 HETATM 1580 O O . HOH E 4 . ? 26.821 19.490 24.439 1.00 49.12 ? 1375 HOH A O 1 HETATM 1581 O O . HOH E 4 . ? 13.433 26.643 17.921 1.00 48.43 ? 1376 HOH A O 1 HETATM 1582 O O . HOH E 4 . ? 16.532 -5.022 13.482 1.00 93.25 ? 1377 HOH A O 1 HETATM 1583 O O . HOH E 4 . ? 0.820 13.436 35.422 1.00 51.77 ? 1378 HOH A O 1 HETATM 1584 O O . HOH E 4 . ? 25.444 1.755 26.734 1.00 67.32 ? 1379 HOH A O 1 HETATM 1585 O O . HOH E 4 . ? 5.572 13.103 38.717 1.00 52.77 ? 1380 HOH A O 1 HETATM 1586 O O . HOH E 4 . ? 19.163 21.609 33.167 1.00 45.13 ? 1381 HOH A O 1 HETATM 1587 O O . HOH E 4 . ? -5.901 7.739 28.167 1.00 42.83 ? 1382 HOH A O 1 HETATM 1588 O O . HOH E 4 . ? 21.078 0.292 25.203 1.00 60.86 ? 1383 HOH A O 1 HETATM 1589 O O . HOH E 4 . ? 21.107 21.659 40.044 1.00 44.59 ? 1384 HOH A O 1 HETATM 1590 O O . HOH E 4 . ? 19.500 21.922 24.408 1.00 54.57 ? 1385 HOH A O 1 HETATM 1591 O O . HOH E 4 . ? 27.350 7.577 25.785 1.00 48.09 ? 1386 HOH A O 1 HETATM 1592 O O . HOH E 4 . ? 5.046 11.458 -0.271 1.00 66.43 ? 1387 HOH A O 1 HETATM 1593 O O . HOH E 4 . ? 34.658 9.818 11.645 1.00 67.16 ? 1388 HOH A O 1 HETATM 1594 O O . HOH E 4 . ? 9.583 29.754 17.605 1.00 42.38 ? 1389 HOH A O 1 HETATM 1595 O O . HOH E 4 . ? 7.343 -6.675 5.722 1.00 51.43 ? 1390 HOH A O 1 HETATM 1596 O O . HOH E 4 . ? 2.483 8.085 7.111 1.00 49.81 ? 1391 HOH A O 1 HETATM 1597 O O . HOH E 4 . ? 19.481 29.447 14.838 1.00 64.19 ? 1392 HOH A O 1 HETATM 1598 O O . HOH E 4 . ? 9.155 -0.112 24.281 1.00 44.53 ? 1393 HOH A O 1 HETATM 1599 O O . HOH E 4 . ? 29.397 -9.341 0.443 1.00 49.19 ? 1394 HOH A O 1 HETATM 1600 O O . HOH E 4 . ? 21.884 23.994 21.923 1.00 48.92 ? 1395 HOH A O 1 HETATM 1601 O O . HOH E 4 . ? 3.969 4.846 30.769 1.00 48.35 ? 1396 HOH A O 1 HETATM 1602 O O . HOH E 4 . ? -2.905 0.125 14.438 1.00 60.22 ? 1397 HOH A O 1 HETATM 1603 O O . HOH E 4 . ? -4.178 15.587 26.756 1.00 55.51 ? 1398 HOH A O 1 HETATM 1604 O O . HOH E 4 . ? 17.477 0.414 18.854 1.00 58.75 ? 1399 HOH A O 1 HETATM 1605 O O . HOH E 4 . ? 30.299 -3.079 19.372 1.00 75.94 ? 1400 HOH A O 1 HETATM 1606 O O . HOH E 4 . ? 29.615 17.800 27.302 1.00 61.79 ? 1401 HOH A O 1 HETATM 1607 O O . HOH E 4 . ? 4.009 3.647 35.152 1.00 62.65 ? 1402 HOH A O 1 HETATM 1608 O O . HOH E 4 . ? 20.883 -10.747 11.577 1.00 56.66 ? 1403 HOH A O 1 HETATM 1609 O O . HOH E 4 . ? 11.520 -3.581 22.417 1.00 61.18 ? 1404 HOH A O 1 HETATM 1610 O O . HOH E 4 . ? 1.083 6.125 10.115 1.00 51.70 ? 1405 HOH A O 1 HETATM 1611 O O . HOH E 4 . ? 17.353 -0.129 16.245 1.00 55.11 ? 1406 HOH A O 1 HETATM 1612 O O . HOH E 4 . ? 27.240 1.119 23.265 1.00 57.17 ? 1407 HOH A O 1 HETATM 1613 O O . HOH E 4 . ? -3.015 6.695 15.235 1.00 77.22 ? 1408 HOH A O 1 HETATM 1614 O O . HOH E 4 . ? 22.591 18.583 36.720 1.00 59.19 ? 1409 HOH A O 1 HETATM 1615 O O . HOH E 4 . ? 29.139 8.237 30.974 1.00 50.15 ? 1410 HOH A O 1 HETATM 1616 O O . HOH E 4 . ? 0.300 26.446 26.404 1.00 48.44 ? 1411 HOH A O 1 HETATM 1617 O O . HOH E 4 . ? 1.271 12.727 7.301 1.00 83.97 ? 1412 HOH A O 1 HETATM 1618 O O . HOH E 4 . ? 24.978 5.304 26.281 1.00 62.20 ? 1413 HOH A O 1 HETATM 1619 O O . HOH E 4 . ? 10.013 27.315 29.495 1.00 58.85 ? 1414 HOH A O 1 HETATM 1620 O O . HOH E 4 . ? 8.023 29.682 20.543 1.00 57.08 ? 1415 HOH A O 1 HETATM 1621 O O . HOH E 4 . ? 7.833 9.145 37.343 1.00 51.51 ? 1416 HOH A O 1 HETATM 1622 O O . HOH E 4 . ? -0.693 8.991 16.272 1.00 46.97 ? 1417 HOH A O 1 HETATM 1623 O O . HOH E 4 . ? 9.089 25.774 8.413 1.00 59.71 ? 1418 HOH A O 1 HETATM 1624 O O . HOH E 4 . ? 22.869 19.155 5.464 1.00 54.45 ? 1419 HOH A O 1 HETATM 1625 O O . HOH E 4 . ? 27.521 20.568 35.149 1.00 54.52 ? 1420 HOH A O 1 HETATM 1626 O O . HOH E 4 . ? 25.367 18.818 5.360 1.00 43.22 ? 1421 HOH A O 1 HETATM 1627 O O . HOH E 4 . ? -0.474 8.285 13.737 1.00 51.47 ? 1422 HOH A O 1 HETATM 1628 O O . HOH E 4 . ? 19.379 19.540 4.208 1.00 58.93 ? 1423 HOH A O 1 HETATM 1629 O O . HOH E 4 . ? 28.187 1.969 25.170 1.00 58.78 ? 1424 HOH A O 1 HETATM 1630 O O . HOH E 4 . ? 29.386 0.984 21.340 1.00 41.82 ? 1425 HOH A O 1 HETATM 1631 O O . HOH E 4 . ? 23.111 -11.283 5.112 1.00 41.20 ? 1426 HOH A O 1 HETATM 1632 O O . HOH E 4 . ? 6.305 27.206 28.748 1.00 35.14 ? 1427 HOH A O 1 HETATM 1633 O O . HOH E 4 . ? 6.094 20.598 1.444 1.00 37.16 ? 1428 HOH A O 1 HETATM 1634 O O . HOH E 4 . ? 22.529 26.042 12.583 1.00 43.14 ? 1429 HOH A O 1 HETATM 1635 O O . HOH E 4 . ? 28.387 15.083 3.856 1.00 63.38 ? 1430 HOH A O 1 HETATM 1636 O O . HOH E 4 . ? 25.004 -2.587 10.824 1.00 59.37 ? 1431 HOH A O 1 HETATM 1637 O O . HOH E 4 . ? 20.279 -15.183 6.686 1.00 55.02 ? 1432 HOH A O 1 HETATM 1638 O O . HOH E 4 . ? 3.040 18.056 3.525 1.00 61.03 ? 1433 HOH A O 1 HETATM 1639 O O . HOH E 4 . ? 26.244 22.146 20.833 1.00 48.08 ? 1434 HOH A O 1 HETATM 1640 O O . HOH E 4 . ? 30.296 -1.961 11.334 1.00 50.07 ? 1435 HOH A O 1 HETATM 1641 O O . HOH E 4 . ? 30.146 10.057 20.071 1.00 48.32 ? 1436 HOH A O 1 HETATM 1642 O O . HOH E 4 . ? 28.622 6.680 28.565 1.00 46.88 ? 1437 HOH A O 1 HETATM 1643 O O . HOH E 4 . ? 29.024 -8.145 -3.428 1.00 55.24 ? 1438 HOH A O 1 HETATM 1644 O O . HOH E 4 . ? 27.044 17.354 13.620 1.00 55.89 ? 1439 HOH A O 1 HETATM 1645 O O . HOH E 4 . ? 29.954 14.989 16.518 1.00 65.60 ? 1440 HOH A O 1 HETATM 1646 O O . HOH E 4 . ? 13.170 24.303 28.555 1.00 53.76 ? 1441 HOH A O 1 HETATM 1647 O O . HOH E 4 . ? 27.522 -5.222 11.198 1.00 50.44 ? 1442 HOH A O 1 HETATM 1648 O O . HOH E 4 . ? 33.875 -0.753 6.683 1.00 57.64 ? 1443 HOH A O 1 HETATM 1649 O O . HOH E 4 . ? 34.408 3.461 5.044 1.00 56.77 ? 1444 HOH A O 1 HETATM 1650 O O . HOH E 4 . ? 10.605 -9.827 8.295 1.00 61.96 ? 1445 HOH A O 1 HETATM 1651 O O . HOH E 4 . ? 11.514 1.481 29.781 1.00 51.35 ? 1446 HOH A O 1 HETATM 1652 O O . HOH E 4 . ? 0.348 10.853 11.465 1.00 51.72 ? 1447 HOH A O 1 HETATM 1653 O O . HOH E 4 . ? 7.912 26.254 11.908 1.00 65.30 ? 1448 HOH A O 1 HETATM 1654 O O . HOH E 4 . ? 6.819 -8.437 -0.041 1.00 67.67 ? 1449 HOH A O 1 HETATM 1655 O O . HOH E 4 . ? 20.777 1.770 21.409 1.00 79.31 ? 1450 HOH A O 1 HETATM 1656 O O . HOH E 4 . ? 11.330 28.637 19.244 1.00 85.97 ? 1451 HOH A O 1 HETATM 1657 O O . HOH E 4 . ? 27.756 9.476 34.726 1.00 51.33 ? 1452 HOH A O 1 HETATM 1658 O O . HOH E 4 . ? 21.109 10.749 36.202 1.00 55.76 ? 1453 HOH A O 1 HETATM 1659 O O . HOH E 4 . ? 26.863 5.178 29.906 1.00 56.54 ? 1454 HOH A O 1 HETATM 1660 O O . HOH E 4 . ? 4.983 -5.033 -1.210 1.00 71.08 ? 1455 HOH A O 1 HETATM 1661 O O . HOH E 4 . ? 30.748 -6.131 18.543 1.00 61.36 ? 1456 HOH A O 1 HETATM 1662 O O . HOH E 4 . ? 18.184 23.733 30.354 1.00 75.75 ? 1457 HOH A O 1 HETATM 1663 O O . HOH E 4 . ? 30.010 0.895 17.931 1.00 104.49 ? 1458 HOH A O 1 HETATM 1664 O O . HOH E 4 . ? 12.848 -6.855 11.943 1.00 60.32 ? 1459 HOH A O 1 HETATM 1665 O O . HOH E 4 . ? 24.290 14.730 38.259 1.00 60.39 ? 1460 HOH A O 1 HETATM 1666 O O . HOH E 4 . ? 28.694 -4.498 1.841 1.00 58.32 ? 1461 HOH A O 1 HETATM 1667 O O . HOH E 4 . ? 29.541 11.919 5.621 1.00 63.94 ? 1462 HOH A O 1 HETATM 1668 O O . HOH E 4 . ? 15.349 25.788 28.068 1.00 67.28 ? 1463 HOH A O 1 HETATM 1669 O O . HOH E 4 . ? 24.314 4.328 19.709 1.00 61.14 ? 1464 HOH A O 1 HETATM 1670 O O . HOH E 4 . ? 21.617 -2.312 17.294 1.00 83.94 ? 1465 HOH A O 1 HETATM 1671 O O . HOH E 4 . ? 28.393 11.545 10.867 1.00 45.78 ? 1466 HOH A O 1 HETATM 1672 O O . HOH E 4 . ? 16.185 -2.835 16.999 1.00 74.59 ? 1467 HOH A O 1 HETATM 1673 O O . HOH E 4 . ? -2.525 6.846 12.689 1.00 113.76 ? 1468 HOH A O 1 HETATM 1674 O O . HOH E 4 . ? 21.634 0.477 16.718 1.00 74.99 ? 1469 HOH A O 1 HETATM 1675 O O . HOH E 4 . ? 4.708 -4.528 12.545 1.00 62.15 ? 1470 HOH A O 1 HETATM 1676 O O . HOH E 4 . ? 20.745 24.458 24.672 1.00 63.73 ? 1471 HOH A O 1 HETATM 1677 O O . HOH E 4 . ? 4.844 -2.213 21.020 1.00 75.57 ? 1472 HOH A O 1 HETATM 1678 O O . HOH E 4 . ? -2.451 3.616 28.450 1.00 65.14 ? 1473 HOH A O 1 HETATM 1679 O O . HOH E 4 . ? 31.675 19.029 24.964 1.00 57.70 ? 1474 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . SER A 10 ? 0.8216 0.3592 0.5095 0.1023 0.1280 0.0164 1007 SER A N 2 C CA . SER A 10 ? 0.8036 0.3596 0.4931 0.0834 0.1225 0.0087 1007 SER A CA 3 C C . SER A 10 ? 0.7731 0.3589 0.4738 0.0820 0.0900 -0.0142 1007 SER A C 4 O O . SER A 10 ? 0.7764 0.3474 0.4487 0.0658 0.0806 -0.0126 1007 SER A O 5 C CB . SER A 10 ? 0.8223 0.3643 0.4881 0.0833 0.1322 0.0081 1007 SER A CB 6 O OG . SER A 10 ? 0.7896 0.3876 0.5102 0.0678 0.1747 0.0337 1007 SER A OG 7 N N . LEU A 11 ? 0.7350 0.3720 0.5012 0.0759 0.0406 -0.0263 1008 LEU A N 8 C CA . LEU A 11 ? 0.6830 0.3948 0.5173 0.0513 0.0240 -0.0274 1008 LEU A CA 9 C C . LEU A 11 ? 0.5795 0.3722 0.5461 0.0059 0.0181 -0.0005 1008 LEU A C 10 O O . LEU A 11 ? 0.5314 0.3657 0.5673 -0.0135 0.0164 0.0153 1008 LEU A O 11 C CB . LEU A 11 ? 0.7426 0.4363 0.5113 0.0635 0.0125 -0.0485 1008 LEU A CB 12 C CG . LEU A 11 ? 0.8524 0.5324 0.5149 0.0551 0.0006 -0.0427 1008 LEU A CG 13 C CD1 . LEU A 11 ? 0.9429 0.6126 0.5188 0.0560 -0.0313 -0.0527 1008 LEU A CD1 14 C CD2 . LEU A 11 ? 0.9136 0.5931 0.5345 0.0395 0.0093 -0.0153 1008 LEU A CD2 15 N N . TYR A 12 ? 0.4841 0.3722 0.5722 -0.0395 0.0273 0.0436 1009 TYR A N 16 C CA . TYR A 12 ? 0.4217 0.3923 0.5705 -0.0489 0.0399 0.0785 1009 TYR A CA 17 C C . TYR A 12 ? 0.3806 0.3657 0.5630 -0.0487 0.0679 0.0891 1009 TYR A C 18 O O . TYR A 12 ? 0.3440 0.3614 0.5874 -0.0467 0.0876 0.1000 1009 TYR A O 19 C CB . TYR A 12 ? 0.4318 0.4250 0.5625 -0.0478 0.0186 0.0957 1009 TYR A CB 20 C CG . TYR A 12 ? 0.4244 0.4611 0.5278 -0.0421 -0.0137 0.1150 1009 TYR A CG 21 C CD1 . TYR A 12 ? 0.4332 0.4863 0.5098 -0.0496 -0.0450 0.1194 1009 TYR A CD1 22 C CD2 . TYR A 12 ? 0.4153 0.4863 0.4949 -0.0467 -0.0390 0.1333 1009 TYR A CD2 23 C CE1 . TYR A 12 ? 0.4419 0.4971 0.4924 -0.0744 -0.0702 0.1314 1009 TYR A CE1 24 C CE2 . TYR A 12 ? 0.4499 0.5036 0.4607 -0.0658 -0.0661 0.1412 1009 TYR A CE2 25 C CZ . TYR A 12 ? 0.4544 0.5052 0.4690 -0.0912 -0.0772 0.1342 1009 TYR A CZ 26 O OH . TYR A 12 ? 0.4874 0.5281 0.4679 -0.1133 -0.0732 0.1421 1009 TYR A OH 27 N N . LYS A 13 ? 0.3280 0.3388 0.4902 -0.0186 0.1049 0.0601 1010 LYS A N 28 C CA . LYS A 13 ? 0.3384 0.3183 0.3991 0.0031 0.0991 0.0153 1010 LYS A CA 29 C C . LYS A 13 ? 0.2779 0.3140 0.3366 -0.0093 0.1054 -0.0027 1010 LYS A C 30 O O . LYS A 13 ? 0.2867 0.3145 0.3143 -0.0049 0.1093 -0.0173 1010 LYS A O 31 C CB . LYS A 13 ? 0.3743 0.3167 0.4029 0.0137 0.0829 0.0120 1010 LYS A CB 32 C CG . LYS A 13 ? 0.4706 0.3370 0.4589 0.0285 0.0074 -0.0104 1010 LYS A CG 33 C CD . LYS A 13 ? 0.5404 0.3574 0.5580 0.0357 -0.0723 -0.0285 1010 LYS A CD 34 C CE . LYS A 13 ? 0.5457 0.3634 0.6132 0.0395 -0.0873 -0.0208 1010 LYS A CE 35 N NZ . LYS A 13 ? 0.5435 0.3720 0.6589 0.0315 -0.1045 -0.0153 1010 LYS A NZ 36 N N . TYR A 14 ? 0.2266 0.3070 0.3027 -0.0346 0.0794 -0.0263 1011 TYR A N 37 C CA . TYR A 14 ? 0.1912 0.3201 0.2723 -0.0496 0.0496 -0.0339 1011 TYR A CA 38 C C . TYR A 14 ? 0.1852 0.3127 0.2831 -0.0461 0.0249 -0.0340 1011 TYR A C 39 O O . TYR A 14 ? 0.1817 0.3364 0.2815 -0.0432 0.0217 -0.0419 1011 TYR A O 40 C CB . TYR A 14 ? 0.1946 0.3316 0.2734 -0.0489 0.0342 -0.0445 1011 TYR A CB 41 C CG . TYR A 14 ? 0.2008 0.3431 0.2606 -0.0540 0.0417 -0.0522 1011 TYR A CG 42 C CD1 . TYR A 14 ? 0.2313 0.3424 0.2741 -0.0766 0.0684 -0.0718 1011 TYR A CD1 43 C CD2 . TYR A 14 ? 0.2213 0.3592 0.2725 -0.0529 0.0093 -0.0640 1011 TYR A CD2 44 C CE1 . TYR A 14 ? 0.2655 0.3289 0.2949 -0.0775 0.0891 -0.0785 1011 TYR A CE1 45 C CE2 . TYR A 14 ? 0.2426 0.3388 0.2967 -0.0715 0.0392 -0.0644 1011 TYR A CE2 46 C CZ . TYR A 14 ? 0.2572 0.3228 0.3167 -0.0744 0.0692 -0.0776 1011 TYR A CZ 47 O OH . TYR A 14 ? 0.3032 0.3334 0.3194 -0.0709 0.0869 -0.0662 1011 TYR A OH 48 N N . LEU A 15 ? 0.1800 0.3034 0.2890 -0.0599 0.0043 -0.0087 1012 LEU A N 49 C CA . LEU A 15 ? 0.1658 0.3136 0.3188 -0.0485 -0.0082 0.0107 1012 LEU A CA 50 C C . LEU A 15 ? 0.1641 0.2908 0.3084 -0.0438 0.0153 0.0017 1012 LEU A C 51 O O . LEU A 15 ? 0.1448 0.3059 0.2879 -0.0375 -0.0020 -0.0109 1012 LEU A O 52 C CB . LEU A 15 ? 0.1886 0.3160 0.3555 -0.0597 -0.0284 0.0274 1012 LEU A CB 53 C CG . LEU A 15 ? 0.2307 0.4129 0.3991 -0.0688 -0.0780 0.0368 1012 LEU A CG 54 C CD1 . LEU A 15 ? 0.3131 0.4598 0.4007 -0.0939 -0.1062 0.0485 1012 LEU A CD1 55 C CD2 . LEU A 15 ? 0.2318 0.4038 0.4654 -0.0662 -0.1368 0.0465 1012 LEU A CD2 56 N N . LEU A 16 ? 0.1430 0.2964 0.3300 -0.0434 0.0394 -0.0164 1013 LEU A N 57 C CA . LEU A 16 ? 0.1221 0.2836 0.3327 -0.0434 0.0631 -0.0296 1013 LEU A CA 58 C C . LEU A 16 ? 0.1269 0.2745 0.3120 -0.0412 0.0653 -0.0225 1013 LEU A C 59 O O . LEU A 16 ? 0.1171 0.2971 0.3070 -0.0344 0.0675 -0.0091 1013 LEU A O 60 C CB . LEU A 16 ? 0.1141 0.2933 0.3716 -0.0386 0.0666 -0.0388 1013 LEU A CB 61 C CG . LEU A 16 ? 0.1208 0.3314 0.3973 -0.0509 0.0710 -0.0573 1013 LEU A CG 62 C CD1 . LEU A 16 ? 0.1194 0.3819 0.4765 -0.0421 0.0754 -0.0952 1013 LEU A CD1 63 C CD2 . LEU A 16 ? 0.1316 0.3718 0.3968 -0.0675 0.0570 -0.0463 1013 LEU A CD2 64 N N . LEU A 17 ? 0.1307 0.2933 0.2702 -0.0630 0.0693 -0.0348 1014 LEU A N 65 C CA . LEU A 17 ? 0.1499 0.2975 0.2678 -0.0678 0.0631 -0.0505 1014 LEU A CA 66 C C . LEU A 17 ? 0.1488 0.3088 0.2493 -0.0631 0.0395 -0.0688 1014 LEU A C 67 O O . LEU A 17 ? 0.1445 0.3440 0.2644 -0.0537 0.0226 -0.0736 1014 LEU A O 68 C CB . LEU A 17 ? 0.1703 0.2973 0.2716 -0.0724 0.0728 -0.0524 1014 LEU A CB 69 C CG . LEU A 17 ? 0.1852 0.3086 0.2885 -0.0586 0.0715 -0.0496 1014 LEU A CG 70 C CD1 . LEU A 17 ? 0.2630 0.3127 0.3097 -0.0684 0.0702 -0.0450 1014 LEU A CD1 71 C CD2 . LEU A 17 ? 0.1562 0.3574 0.2985 -0.0741 0.0666 -0.0617 1014 LEU A CD2 72 N N . ARG A 18 ? 0.1439 0.3199 0.2328 -0.0595 0.0405 -0.0746 1015 ARG A N 73 C CA . ARG A 18 ? 0.1518 0.3366 0.2423 -0.0395 0.0364 -0.0851 1015 ARG A CA 74 C C . ARG A 18 ? 0.1509 0.3330 0.2477 -0.0208 0.0219 -0.0878 1015 ARG A C 75 O O . ARG A 18 ? 0.1365 0.3637 0.2901 -0.0093 0.0074 -0.0907 1015 ARG A O 76 C CB . ARG A 18 ? 0.1623 0.3546 0.2377 -0.0333 0.0483 -0.0829 1015 ARG A CB 77 C CG . ARG A 18 ? 0.1315 0.3382 0.2707 -0.0230 0.0496 -0.0586 1015 ARG A CG 78 C CD . ARG A 18 ? 0.1474 0.3531 0.3215 -0.0140 0.0746 -0.0293 1015 ARG A CD 79 N NE . ARG A 18 ? 0.1974 0.3650 0.3533 -0.0240 0.0590 -0.0175 1015 ARG A NE 80 C CZ . ARG A 18 ? 0.2433 0.3679 0.3756 -0.0163 0.0829 -0.0228 1015 ARG A CZ 81 N NH1 . ARG A 18 ? 0.2220 0.3882 0.3946 -0.0054 0.0560 -0.0491 1015 ARG A NH1 82 N NH2 . ARG A 18 ? 0.2836 0.3989 0.4095 -0.0333 0.0816 0.0005 1015 ARG A NH2 83 N N . SER A 19 ? 0.1412 0.3192 0.2338 -0.0208 0.0052 -0.0772 1016 SER A N 84 C CA . SER A 19 ? 0.1474 0.3041 0.2378 -0.0229 -0.0153 -0.0714 1016 SER A CA 85 C C . SER A 19 ? 0.1612 0.3129 0.2333 -0.0240 -0.0098 -0.0693 1016 SER A C 86 O O . SER A 19 ? 0.2044 0.3194 0.2421 -0.0219 -0.0229 -0.0627 1016 SER A O 87 C CB . SER A 19 ? 0.1474 0.3064 0.2363 -0.0259 -0.0073 -0.0649 1016 SER A CB 88 O OG . SER A 19 ? 0.1473 0.3255 0.2824 -0.0333 -0.0518 -0.0548 1016 SER A OG 89 N N . THR A 20 ? 0.1479 0.3294 0.2407 -0.0205 -0.0252 -0.0772 1017 THR A N 90 C CA . THR A 20 ? 0.1250 0.3639 0.2569 -0.0037 -0.0186 -0.0798 1017 THR A CA 91 C C . THR A 20 ? 0.1280 0.4275 0.2883 0.0126 -0.0034 -0.0886 1017 THR A C 92 O O . THR A 20 ? 0.1132 0.4429 0.3003 -0.0093 -0.0046 -0.0900 1017 THR A O 93 C CB . THR A 20 ? 0.1191 0.3569 0.2549 0.0027 -0.0230 -0.0697 1017 THR A CB 94 O OG1 . THR A 20 ? 0.1852 0.3447 0.2648 0.0057 -0.0318 -0.0627 1017 THR A OG1 95 C CG2 . THR A 20 ? 0.0982 0.3973 0.2637 -0.0054 -0.0194 -0.0614 1017 THR A CG2 96 N N . GLY A 21 ? 0.1349 0.4981 0.3384 0.0450 0.0109 -0.0895 1018 GLY A N 97 C CA . GLY A 21 ? 0.1509 0.5475 0.4052 0.0617 0.0186 -0.0749 1018 GLY A CA 98 C C . GLY A 21 ? 0.1703 0.5519 0.4356 0.0489 -0.0031 -0.0741 1018 GLY A C 99 O O . GLY A 21 ? 0.1683 0.5792 0.4329 0.0549 0.0035 -0.0627 1018 GLY A O 100 N N . ASP A 22 ? 0.1834 0.5177 0.4609 0.0366 -0.0302 -0.0891 1019 ASP A N 101 C CA . ASP A 22 ? 0.2125 0.5120 0.4859 0.0208 -0.0513 -0.0882 1019 ASP A CA 102 C C . ASP A 22 ? 0.2298 0.5309 0.4798 -0.0041 -0.0284 -0.0898 1019 ASP A C 103 O O . ASP A 22 ? 0.2475 0.5364 0.4838 -0.0081 -0.0403 -0.0776 1019 ASP A O 104 C CB . ASP A 22 ? 0.2266 0.5044 0.5102 0.0353 -0.0754 -0.0847 1019 ASP A CB 105 C CG . ASP A 22 ? 0.2606 0.5149 0.5817 0.0408 -0.0935 -0.0520 1019 ASP A CG 106 O OD1 . ASP A 22 ? 0.2883 0.5475 0.6904 0.0359 -0.0930 0.0052 1019 ASP A OD1 107 O OD2 . ASP A 22 ? 0.2639 0.5320 0.6172 0.0533 -0.0472 -0.0293 1019 ASP A OD2 108 N N . MET A 23 ? 0.2196 0.5766 0.4881 -0.0379 0.0324 -0.1062 1020 MET A N 109 C CA . MET A 23 ? 0.2398 0.6219 0.5073 -0.0662 0.0900 -0.1193 1020 MET A CA 110 C C . MET A 23 ? 0.2257 0.6348 0.4910 -0.0538 0.0842 -0.1436 1020 MET A C 111 O O . MET A 23 ? 0.2451 0.6736 0.4809 -0.0241 0.0828 -0.1500 1020 MET A O 112 C CB . MET A 23 ? 0.2511 0.6190 0.5349 -0.0807 0.0944 -0.1181 1020 MET A CB 113 C CG . MET A 23 ? 0.2730 0.6657 0.5727 -0.1058 0.1102 -0.0560 1020 MET A CG 114 S SD . MET A 23 ? 0.2205 0.6790 0.5083 -0.0966 0.0445 -0.0394 1020 MET A SD 115 C CE . MET A 23 ? 0.2572 0.7181 0.4928 -0.0581 0.0680 -0.0186 1020 MET A CE 116 N N . HIS A 24 ? 0.1897 0.6115 0.4956 -0.0767 0.0781 -0.1594 1021 HIS A N 117 C CA . HIS A 24 ? 0.1606 0.5917 0.5328 -0.0960 0.0579 -0.1536 1021 HIS A CA 118 C C . HIS A 24 ? 0.1473 0.5957 0.5363 -0.1036 0.0214 -0.1712 1021 HIS A C 119 O O . HIS A 24 ? 0.1474 0.5896 0.5572 -0.1141 0.0331 -0.1773 1021 HIS A O 120 C CB . HIS A 24 ? 0.1615 0.5806 0.5432 -0.1061 0.0649 -0.1500 1021 HIS A CB 121 C CG . HIS A 24 ? 0.1923 0.5565 0.6097 -0.0732 0.0397 -0.1674 1021 HIS A CG 122 N ND1 . HIS A 24 ? 0.2213 0.5400 0.6887 -0.0537 0.0219 -0.1852 1021 HIS A ND1 123 C CD2 . HIS A 24 ? 0.2071 0.5188 0.6692 -0.0636 0.0131 -0.1921 1021 HIS A CD2 124 C CE1 . HIS A 24 ? 0.2560 0.5070 0.7203 -0.0410 0.0104 -0.1993 1021 HIS A CE1 125 N NE2 . HIS A 24 ? 0.2383 0.5004 0.7116 -0.0463 0.0109 -0.2020 1021 HIS A NE2 126 N N . LYS A 25 ? 0.1483 0.6291 0.5245 -0.0864 -0.0270 -0.1817 1022 LYS A N 127 C CA . LYS A 25 ? 0.1867 0.6751 0.5040 -0.0485 -0.0732 -0.1791 1022 LYS A CA 128 C C . LYS A 25 ? 0.1903 0.6377 0.4535 -0.0562 -0.0560 -0.1665 1022 LYS A C 129 O O . LYS A 25 ? 0.2072 0.6352 0.4496 -0.0671 -0.0252 -0.1615 1022 LYS A O 130 C CB . LYS A 25 ? 0.1941 0.7225 0.5400 -0.0322 -0.1084 -0.1744 1022 LYS A CB 131 C CG . LYS A 25 ? 0.2319 0.8553 0.6154 0.0401 -0.1289 -0.1263 1022 LYS A CG 132 C CD . LYS A 25 ? 0.2624 1.0339 0.7120 0.1162 -0.1418 -0.0544 1022 LYS A CD 133 C CE . LYS A 25 ? 0.2361 1.1181 0.7342 0.1571 -0.1410 -0.0333 1022 LYS A CE 134 N NZ . LYS A 25 ? 0.2858 1.1706 0.7383 0.1764 -0.1289 -0.0259 1022 LYS A NZ 135 N N . ALA A 26 ? 0.1808 0.6129 0.4077 -0.0610 -0.0348 -0.1453 1023 ALA A N 136 C CA . ALA A 26 ? 0.1474 0.5921 0.3849 -0.0793 -0.0098 -0.1263 1023 ALA A CA 137 C C . ALA A 26 ? 0.1233 0.5787 0.3977 -0.0908 -0.0020 -0.1162 1023 ALA A C 138 O O . ALA A 26 ? 0.1146 0.5981 0.4092 -0.0913 -0.0148 -0.1079 1023 ALA A O 139 C CB . ALA A 26 ? 0.1747 0.5956 0.3652 -0.0856 0.0024 -0.1177 1023 ALA A CB 140 N N . LYS A 27 ? 0.1054 0.5655 0.4113 -0.0842 0.0175 -0.1307 1024 LYS A N 141 C CA . LYS A 27 ? 0.1189 0.5521 0.4372 -0.0763 0.0313 -0.1342 1024 LYS A CA 142 C C . LYS A 27 ? 0.0961 0.5350 0.4253 -0.0612 0.0394 -0.1421 1024 LYS A C 143 O O . LYS A 27 ? 0.0724 0.5170 0.4417 -0.0727 0.0498 -0.1483 1024 LYS A O 144 C CB . LYS A 27 ? 0.1527 0.5687 0.4510 -0.0790 0.0230 -0.1216 1024 LYS A CB 145 C CG . LYS A 27 ? 0.2867 0.6258 0.5123 -0.0772 -0.0379 -0.0815 1024 LYS A CG 146 C CD . LYS A 27 ? 0.4266 0.6941 0.5820 -0.0674 -0.0926 -0.0226 1024 LYS A CD 147 C CE . LYS A 27 ? 0.4541 0.7045 0.6111 -0.0573 -0.1155 -0.0031 1024 LYS A CE 148 N NZ . LYS A 27 ? 0.4343 0.7031 0.6294 -0.0434 -0.1137 -0.0062 1024 LYS A NZ 149 N N . SER A 28 ? 0.1017 0.4992 0.4293 -0.0474 0.0478 -0.1342 1025 SER A N 150 C CA . SER A 28 ? 0.1298 0.4809 0.4287 -0.0542 0.0571 -0.0988 1025 SER A CA 151 C C . SER A 28 ? 0.1263 0.4499 0.3831 -0.0766 0.0736 -0.0886 1025 SER A C 152 O O . SER A 28 ? 0.1559 0.4702 0.4034 -0.1027 0.0700 -0.0793 1025 SER A O 153 C CB . SER A 28 ? 0.1474 0.4798 0.4544 -0.0317 0.0619 -0.1022 1025 SER A CB 154 O OG . SER A 28 ? 0.2011 0.5174 0.5411 -0.0197 0.0507 -0.0493 1025 SER A OG 155 N N . PRO A 29 ? 0.1393 0.4379 0.3366 -0.0929 0.0785 -0.0640 1026 PRO A N 156 C CA . PRO A 29 ? 0.1728 0.4345 0.3235 -0.0948 0.0878 -0.0559 1026 PRO A CA 157 C C . PRO A 29 ? 0.2157 0.4347 0.3307 -0.1171 0.1032 -0.0553 1026 PRO A C 158 O O . PRO A 29 ? 0.2301 0.4616 0.3375 -0.1001 0.1096 -0.0553 1026 PRO A O 159 C CB . PRO A 29 ? 0.1492 0.4460 0.3127 -0.0930 0.0772 -0.0551 1026 PRO A CB 160 C CG . PRO A 29 ? 0.1315 0.4372 0.3339 -0.0798 0.0652 -0.0403 1026 PRO A CG 161 C CD . PRO A 29 ? 0.1132 0.4282 0.3249 -0.0833 0.0776 -0.0582 1026 PRO A CD 162 N N . THR A 30 ? 0.2856 0.4415 0.3551 -0.1456 0.1150 -0.0406 1027 THR A N 163 C CA . THR A 30 ? 0.3355 0.4541 0.3925 -0.1650 0.1132 -0.0307 1027 THR A CA 164 C C . THR A 30 ? 0.3436 0.4230 0.3785 -0.1404 0.1186 -0.0351 1027 THR A C 165 O O . THR A 30 ? 0.3740 0.4244 0.4056 -0.1229 0.0876 -0.0531 1027 THR A O 166 C CB . THR A 30 ? 0.3479 0.4731 0.4169 -0.1833 0.1096 -0.0197 1027 THR A CB 167 O OG1 . THR A 30 ? 0.4320 0.4763 0.4706 -0.1914 0.0820 -0.0087 1027 THR A OG1 168 C CG2 . THR A 30 ? 0.3528 0.5169 0.4465 -0.2010 0.1049 -0.0274 1027 THR A CG2 169 N N . ILE A 31 ? 0.3463 0.4086 0.3702 -0.1272 0.1333 -0.0260 1028 ILE A N 170 C CA . ILE A 31 ? 0.3497 0.3914 0.3736 -0.1172 0.1447 0.0059 1028 ILE A CA 171 C C . ILE A 31 ? 0.3384 0.3855 0.3185 -0.1075 0.1324 -0.0015 1028 ILE A C 172 O O . ILE A 31 ? 0.3422 0.4117 0.3034 -0.1127 0.1412 -0.0041 1028 ILE A O 173 C CB . ILE A 31 ? 0.3643 0.3932 0.4104 -0.1158 0.1465 0.0131 1028 ILE A CB 174 C CG1 . ILE A 31 ? 0.3867 0.4151 0.4650 -0.0842 0.1393 0.0326 1028 ILE A CG1 175 C CG2 . ILE A 31 ? 0.3772 0.3995 0.4564 -0.1163 0.1562 0.0472 1028 ILE A CG2 176 C CD1 . ILE A 31 ? 0.3946 0.4587 0.5059 -0.0383 0.1220 0.0553 1028 ILE A CD1 177 N N . MET A 32 ? 0.3185 0.3662 0.2969 -0.0636 0.0925 0.0046 1029 MET A N 178 C CA . MET A 32 ? 0.3120 0.3386 0.2890 -0.0292 0.0599 0.0076 1029 MET A CA 179 C C . MET A 32 ? 0.2921 0.3217 0.2856 -0.0093 0.0412 0.0193 1029 MET A C 180 O O . MET A 32 ? 0.2890 0.3208 0.3294 -0.0074 0.0496 0.0322 1029 MET A O 181 C CB . MET A 32 ? 0.3388 0.3610 0.3046 -0.0251 0.0412 -0.0126 1029 MET A CB 182 C CG . MET A 32 ? 0.3680 0.3819 0.2996 -0.0263 0.0472 -0.0151 1029 MET A CG 183 S SD . MET A 32 ? 0.2524 0.4205 0.2545 0.0051 0.0476 -0.0164 1029 MET A SD 184 C CE . MET A 32 ? 0.3824 0.3871 0.2933 -0.0082 0.0342 -0.0346 1029 MET A CE 185 N N . THR A 33 ? 0.2903 0.2962 0.2511 0.0087 0.0285 0.0098 1030 THR A N 186 C CA . THR A 33 ? 0.3181 0.2937 0.2362 0.0285 0.0172 -0.0020 1030 THR A CA 187 C C . THR A 33 ? 0.3057 0.2872 0.2178 0.0405 0.0208 0.0098 1030 THR A C 188 O O . THR A 33 ? 0.3097 0.2870 0.2289 0.0329 0.0186 0.0151 1030 THR A O 189 C CB . THR A 33 ? 0.3364 0.2955 0.2372 0.0285 0.0173 -0.0172 1030 THR A CB 190 O OG1 . THR A 33 ? 0.3808 0.3129 0.2558 0.0120 -0.0030 -0.0114 1030 THR A OG1 191 C CG2 . THR A 33 ? 0.3689 0.3170 0.2492 0.0476 0.0252 -0.0098 1030 THR A CG2 192 N N . ARG A 34 ? 0.3253 0.3086 0.2169 0.0601 0.0115 0.0173 1031 ARG A N 193 C CA . ARG A 34 ? 0.3425 0.3262 0.2149 0.0750 0.0097 0.0228 1031 ARG A CA 194 C C . ARG A 34 ? 0.3474 0.3176 0.2249 0.0696 0.0219 0.0148 1031 ARG A C 195 O O . ARG A 34 ? 0.3533 0.3224 0.2563 0.0693 0.0270 0.0087 1031 ARG A O 196 C CB . ARG A 34 ? 0.3560 0.3359 0.2117 0.0908 0.0041 0.0285 1031 ARG A CB 197 C CG . ARG A 34 ? 0.4065 0.3607 0.2140 0.1018 -0.0230 0.0357 1031 ARG A CG 198 C CD . ARG A 34 ? 0.4659 0.4029 0.2158 0.1544 -0.0263 0.0509 1031 ARG A CD 199 N NE . ARG A 34 ? 0.4778 0.4629 0.2037 0.1902 -0.0208 0.0518 1031 ARG A NE 200 C CZ . ARG A 34 ? 0.4938 0.4863 0.2117 0.2178 -0.0142 0.0639 1031 ARG A CZ 201 N NH1 . ARG A 34 ? 0.5260 0.4902 0.2416 0.2274 -0.0049 0.0640 1031 ARG A NH1 202 N NH2 . ARG A 34 ? 0.4946 0.5156 0.2187 0.2318 -0.0320 0.0595 1031 ARG A NH2 203 N N . VAL A 35 ? 0.3517 0.3237 0.2213 0.0732 0.0377 0.0230 1032 VAL A N 204 C CA . VAL A 35 ? 0.3722 0.3420 0.2368 0.0872 0.0533 0.0296 1032 VAL A CA 205 C C . VAL A 35 ? 0.3777 0.3407 0.2230 0.1115 0.0467 0.0228 1032 VAL A C 206 O O . VAL A 35 ? 0.3989 0.3537 0.2308 0.1238 0.0230 0.0092 1032 VAL A O 207 C CB . VAL A 35 ? 0.3655 0.3522 0.2486 0.0860 0.0640 0.0447 1032 VAL A CB 208 C CG1 . VAL A 35 ? 0.3666 0.3571 0.2545 0.0794 0.0584 0.0386 1032 VAL A CG1 209 C CG2 . VAL A 35 ? 0.3623 0.3736 0.2606 0.0776 0.0850 0.0485 1032 VAL A CG2 210 N N . THR A 36 ? 0.3675 0.3578 0.2161 0.1400 0.0406 0.0261 1033 THR A N 211 C CA . THR A 36 ? 0.3512 0.3799 0.2108 0.1544 0.0458 0.0373 1033 THR A CA 212 C C . THR A 36 ? 0.3264 0.4070 0.2124 0.1597 0.0443 0.0329 1033 THR A C 213 O O . THR A 36 ? 0.3194 0.4334 0.2152 0.1649 0.0491 0.0392 1033 THR A O 214 C CB . THR A 36 ? 0.3564 0.3747 0.2081 0.1532 0.0472 0.0331 1033 THR A CB 215 O OG1 . THR A 36 ? 0.3370 0.3901 0.2194 0.1562 0.0427 0.0170 1033 THR A OG1 216 C CG2 . THR A 36 ? 0.3542 0.3883 0.2099 0.1524 0.0643 0.0388 1033 THR A CG2 217 N N . ASN A 37 ? 0.3079 0.4284 0.2247 0.1699 0.0355 0.0215 1034 ASN A N 218 C CA . ASN A 37 ? 0.2951 0.4323 0.2304 0.1676 0.0161 0.0137 1034 ASN A CA 219 C C . ASN A 37 ? 0.3032 0.4440 0.2107 0.1817 0.0208 0.0164 1034 ASN A C 220 O O . ASN A 37 ? 0.3088 0.4571 0.2205 0.1875 0.0315 0.0219 1034 ASN A O 221 C CB . ASN A 37 ? 0.2854 0.4356 0.2531 0.1544 0.0073 0.0137 1034 ASN A CB 222 C CG . ASN A 37 ? 0.2996 0.4313 0.3113 0.1221 -0.0381 -0.0010 1034 ASN A CG 223 O OD1 . ASN A 37 ? 0.2736 0.4383 0.3892 0.0878 -0.0461 -0.0082 1034 ASN A OD1 224 N ND2 . ASN A 37 ? 0.2912 0.4584 0.3763 0.0939 -0.0670 0.0076 1034 ASN A ND2 225 N N . ASN A 38 ? 0.2840 0.4383 0.1923 0.1858 -0.0003 0.0062 1035 ASN A N 226 C CA . ASN A 38 ? 0.2705 0.4408 0.1808 0.1771 -0.0185 -0.0035 1035 ASN A CA 227 C C . ASN A 38 ? 0.2462 0.4086 0.1729 0.1518 -0.0203 -0.0062 1035 ASN A C 228 O O . ASN A 38 ? 0.2508 0.4189 0.1791 0.1562 -0.0153 -0.0076 1035 ASN A O 229 C CB . ASN A 38 ? 0.2752 0.4634 0.1869 0.1861 -0.0307 -0.0093 1035 ASN A CB 230 C CG . ASN A 38 ? 0.2924 0.5213 0.2064 0.1973 -0.0417 0.0109 1035 ASN A CG 231 O OD1 . ASN A 38 ? 0.3355 0.5658 0.2176 0.1976 -0.0333 0.0219 1035 ASN A OD1 232 N ND2 . ASN A 38 ? 0.3023 0.5651 0.2639 0.2073 -0.0443 0.0082 1035 ASN A ND2 233 N N . VAL A 39 ? 0.2060 0.3756 0.1668 0.1216 -0.0054 0.0087 1036 VAL A N 234 C CA . VAL A 39 ? 0.1693 0.3416 0.1682 0.0882 -0.0017 0.0159 1036 VAL A CA 235 C C . VAL A 39 ? 0.1764 0.3197 0.1897 0.0803 0.0136 0.0152 1036 VAL A C 236 O O . VAL A 39 ? 0.1932 0.3219 0.1985 0.0877 0.0137 0.0148 1036 VAL A O 237 C CB . VAL A 39 ? 0.1579 0.3461 0.1703 0.0772 -0.0020 0.0186 1036 VAL A CB 238 C CG1 . VAL A 39 ? 0.1588 0.3323 0.1597 0.0649 -0.0193 0.0197 1036 VAL A CG1 239 C CG2 . VAL A 39 ? 0.1172 0.3596 0.1939 0.0758 -0.0092 -0.0031 1036 VAL A CG2 240 N N . TYR A 40 ? 0.1588 0.3192 0.1832 0.0736 0.0120 0.0068 1037 TYR A N 241 C CA . TYR A 40 ? 0.1747 0.3125 0.1817 0.0522 0.0186 0.0006 1037 TYR A CA 242 C C . TYR A 40 ? 0.1488 0.2842 0.1708 0.0408 0.0175 -0.0137 1037 TYR A C 243 O O . TYR A 40 ? 0.1154 0.2854 0.1949 0.0252 0.0120 -0.0109 1037 TYR A O 244 C CB . TYR A 40 ? 0.1939 0.3321 0.1752 0.0524 0.0229 0.0076 1037 TYR A CB 245 C CG . TYR A 40 ? 0.2468 0.3517 0.1851 0.0680 0.0401 0.0197 1037 TYR A CG 246 C CD1 . TYR A 40 ? 0.2946 0.3684 0.1975 0.0706 0.0489 0.0337 1037 TYR A CD1 247 C CD2 . TYR A 40 ? 0.2655 0.3759 0.1912 0.0847 0.0344 0.0241 1037 TYR A CD2 248 C CE1 . TYR A 40 ? 0.3248 0.3939 0.1932 0.0847 0.0471 0.0417 1037 TYR A CE1 249 C CE2 . TYR A 40 ? 0.3129 0.3941 0.1923 0.0957 0.0535 0.0476 1037 TYR A CE2 250 C CZ . TYR A 40 ? 0.3336 0.3939 0.1932 0.0970 0.0482 0.0480 1037 TYR A CZ 251 O OH . TYR A 40 ? 0.3729 0.4147 0.2298 0.1018 0.0502 0.0644 1037 TYR A OH 252 N N . LEU A 41 ? 0.1464 0.2698 0.1826 0.0197 0.0164 -0.0098 1038 LEU A N 253 C CA . LEU A 41 ? 0.1333 0.2741 0.1941 0.0164 0.0172 -0.0082 1038 LEU A CA 254 C C . LEU A 41 ? 0.1386 0.2583 0.2064 0.0057 0.0241 -0.0108 1038 LEU A C 255 O O . LEU A 41 ? 0.1630 0.2669 0.2257 0.0098 0.0388 -0.0017 1038 LEU A O 256 C CB . LEU A 41 ? 0.1324 0.2777 0.1976 0.0295 0.0074 -0.0082 1038 LEU A CB 257 C CG . LEU A 41 ? 0.0891 0.2791 0.1905 0.0081 0.0175 -0.0071 1038 LEU A CG 258 C CD1 . LEU A 41 ? 0.1080 0.2851 0.2029 0.0195 0.0395 0.0049 1038 LEU A CD1 259 C CD2 . LEU A 41 ? 0.1221 0.2748 0.2027 0.0175 0.0436 -0.0131 1038 LEU A CD2 260 N N . GLY A 42 ? 0.1158 0.2671 0.2116 -0.0031 0.0331 -0.0073 1039 GLY A N 261 C CA . GLY A 42 ? 0.1208 0.2867 0.2247 -0.0115 0.0461 -0.0068 1039 GLY A CA 262 C C . GLY A 42 ? 0.1009 0.2842 0.2117 -0.0296 0.0505 -0.0175 1039 GLY A C 263 O O . GLY A 42 ? 0.0956 0.2973 0.2000 -0.0175 0.0529 -0.0162 1039 GLY A O 264 N N . ASN A 43 ? 0.0895 0.3111 0.2185 -0.0355 0.0612 -0.0388 1040 ASN A N 265 C CA . ASN A 43 ? 0.0781 0.3312 0.2212 -0.0472 0.0706 -0.0458 1040 ASN A CA 266 C C . ASN A 43 ? 0.0787 0.3429 0.2222 -0.0307 0.0723 -0.0408 1040 ASN A C 267 O O . ASN A 43 ? 0.0876 0.3470 0.2143 -0.0359 0.0710 -0.0458 1040 ASN A O 268 C CB . ASN A 43 ? 0.0856 0.3422 0.2187 -0.0599 0.0709 -0.0419 1040 ASN A CB 269 C CG . ASN A 43 ? 0.1061 0.3679 0.2240 -0.0788 0.0863 -0.0375 1040 ASN A CG 270 O OD1 . ASN A 43 ? 0.1365 0.4065 0.2280 -0.0710 0.0798 -0.0193 1040 ASN A OD1 271 N ND2 . ASN A 43 ? 0.1622 0.3964 0.2759 -0.1168 0.0710 -0.0203 1040 ASN A ND2 272 N N . TYR A 44 ? 0.0619 0.3558 0.2362 -0.0237 0.0842 -0.0274 1041 TYR A N 273 C CA A TYR A 44 ? 0.0867 0.3698 0.2372 -0.0060 0.0812 -0.0186 1041 TYR A CA 274 C CA B TYR A 44 ? 0.0900 0.3677 0.2354 -0.0062 0.0790 -0.0197 1041 TYR A CA 275 C C . TYR A 44 ? 0.0996 0.3698 0.2354 -0.0241 0.0834 -0.0208 1041 TYR A C 276 O O . TYR A 44 ? 0.0725 0.3799 0.2380 -0.0285 0.0834 -0.0258 1041 TYR A O 277 C CB A TYR A 44 ? 0.0970 0.3873 0.2449 0.0091 0.0768 -0.0174 1041 TYR A CB 278 C CB B TYR A 44 ? 0.1014 0.3817 0.2442 0.0097 0.0715 -0.0215 1041 TYR A CB 279 C CG A TYR A 44 ? 0.1217 0.4124 0.2594 0.0421 0.0516 -0.0241 1041 TYR A CG 280 C CG B TYR A 44 ? 0.1243 0.4174 0.2453 0.0460 0.0597 -0.0296 1041 TYR A CG 281 C CD1 A TYR A 44 ? 0.1956 0.4415 0.2910 0.0252 0.0524 -0.0381 1041 TYR A CD1 282 C CD1 B TYR A 44 ? 0.1588 0.4359 0.2799 0.0649 0.0644 -0.0428 1041 TYR A CD1 283 C CD2 A TYR A 44 ? 0.1720 0.4458 0.2842 0.0533 0.0544 -0.0421 1041 TYR A CD2 284 C CD2 B TYR A 44 ? 0.1377 0.4487 0.2671 0.0595 0.0737 -0.0386 1041 TYR A CD2 285 C CE1 A TYR A 44 ? 0.2152 0.4620 0.3264 0.0182 0.0671 -0.0597 1041 TYR A CE1 286 C CE1 B TYR A 44 ? 0.1641 0.4386 0.3212 0.0816 0.0929 -0.0467 1041 TYR A CE1 287 C CE2 A TYR A 44 ? 0.1941 0.4566 0.3307 0.0450 0.0608 -0.0601 1041 TYR A CE2 288 C CE2 B TYR A 44 ? 0.1492 0.4426 0.3046 0.0864 0.0983 -0.0403 1041 TYR A CE2 289 C CZ A TYR A 44 ? 0.2202 0.4706 0.3508 0.0280 0.0723 -0.0684 1041 TYR A CZ 290 C CZ B TYR A 44 ? 0.1791 0.4347 0.3395 0.0900 0.1093 -0.0381 1041 TYR A CZ 291 O OH A TYR A 44 ? 0.2313 0.4813 0.3962 0.0118 0.0728 -0.0829 1041 TYR A OH 292 O OH B TYR A 44 ? 0.1993 0.4142 0.3698 0.0988 0.1421 -0.0318 1041 TYR A OH 293 N N . LYS A 45 ? 0.1042 0.3758 0.2442 -0.0489 0.0806 -0.0247 1042 LYS A N 294 C CA . LYS A 45 ? 0.1386 0.3831 0.2467 -0.0790 0.0891 -0.0386 1042 LYS A CA 295 C C . LYS A 45 ? 0.1500 0.3607 0.2187 -0.0652 0.0926 -0.0364 1042 LYS A C 296 O O . LYS A 45 ? 0.1404 0.4027 0.2228 -0.0740 0.0961 -0.0392 1042 LYS A O 297 C CB . LYS A 45 ? 0.1571 0.3894 0.2854 -0.0929 0.0850 -0.0401 1042 LYS A CB 298 C CG . LYS A 45 ? 0.2311 0.4259 0.3596 -0.1500 0.1032 -0.0427 1042 LYS A CG 299 C CD . LYS A 45 ? 0.3316 0.5109 0.4623 -0.2166 0.1190 -0.0491 1042 LYS A CD 300 C CE . LYS A 45 ? 0.3702 0.5353 0.4960 -0.2483 0.1238 -0.0489 1042 LYS A CE 301 N NZ . LYS A 45 ? 0.3603 0.5648 0.5030 -0.2469 0.1360 -0.0511 1042 LYS A NZ 302 N N . ASN A 46 ? 0.1623 0.3425 0.2017 -0.0467 0.0930 -0.0230 1043 ASN A N 303 C CA . ASN A 46 ? 0.1788 0.3095 0.2010 -0.0348 0.0873 -0.0219 1043 ASN A CA 304 C C . ASN A 46 ? 0.1743 0.3000 0.1879 -0.0320 0.0860 -0.0164 1043 ASN A C 305 O O . ASN A 46 ? 0.1851 0.3233 0.1993 -0.0353 0.0715 -0.0063 1043 ASN A O 306 C CB . ASN A 46 ? 0.1949 0.3088 0.1976 -0.0320 0.0921 -0.0263 1043 ASN A CB 307 C CG . ASN A 46 ? 0.2132 0.3059 0.2338 -0.0471 0.1076 -0.0241 1043 ASN A CG 308 O OD1 . ASN A 46 ? 0.2721 0.3422 0.2782 -0.0834 0.1289 -0.0175 1043 ASN A OD1 309 N ND2 . ASN A 46 ? 0.2806 0.3032 0.2161 -0.0509 0.1216 -0.0317 1043 ASN A ND2 310 N N . ALA A 47 ? 0.1263 0.2978 0.2064 -0.0206 0.0854 -0.0203 1044 ALA A N 311 C CA . ALA A 47 ? 0.1262 0.2996 0.2161 -0.0161 0.0876 -0.0274 1044 ALA A CA 312 C C . ALA A 47 ? 0.1084 0.3368 0.2240 -0.0274 0.0886 -0.0467 1044 ALA A C 313 O O . ALA A 47 ? 0.1168 0.3576 0.2273 -0.0322 0.0820 -0.0469 1044 ALA A O 314 C CB . ALA A 47 ? 0.1206 0.2935 0.2316 -0.0035 0.0693 -0.0184 1044 ALA A CB 315 N N . MET A 48 ? 0.1124 0.3740 0.2325 -0.0372 0.1032 -0.0568 1045 MET A N 316 C CA . MET A 48 ? 0.1253 0.4149 0.2374 -0.0366 0.1039 -0.0610 1045 MET A CA 317 C C . MET A 48 ? 0.1553 0.4129 0.2365 -0.0493 0.1128 -0.0577 1045 MET A C 318 O O . MET A 48 ? 0.1712 0.4262 0.2450 -0.0564 0.1212 -0.0630 1045 MET A O 319 C CB . MET A 48 ? 0.1289 0.4415 0.2477 -0.0348 0.0951 -0.0666 1045 MET A CB 320 C CG . MET A 48 ? 0.0775 0.4620 0.2838 -0.0388 0.0693 -0.0612 1045 MET A CG 321 S SD . MET A 48 ? 0.1492 0.4747 0.3783 0.0282 0.0597 -0.0934 1045 MET A SD 322 C CE . MET A 48 ? 0.1133 0.4424 0.4083 -0.0140 0.0432 -0.0671 1045 MET A CE 323 N N . ASP A 49 ? 0.1897 0.3968 0.2406 -0.0749 0.1186 -0.0452 1046 ASP A N 324 C CA . ASP A 49 ? 0.2150 0.4054 0.2469 -0.0869 0.1199 -0.0274 1046 ASP A CA 325 C C . ASP A 49 ? 0.2293 0.3973 0.2592 -0.0842 0.1067 -0.0182 1046 ASP A C 326 O O . ASP A 49 ? 0.2329 0.4241 0.2685 -0.0903 0.1023 -0.0113 1046 ASP A O 327 C CB . ASP A 49 ? 0.2398 0.4072 0.2599 -0.0948 0.1186 -0.0197 1046 ASP A CB 328 C CG . ASP A 49 ? 0.2381 0.4645 0.2538 -0.1164 0.1412 -0.0342 1046 ASP A CG 329 O OD1 . ASP A 49 ? 0.2763 0.5508 0.3075 -0.1127 0.1576 -0.0505 1046 ASP A OD1 330 O OD2 . ASP A 49 ? 0.2529 0.4702 0.2865 -0.1286 0.1324 -0.0355 1046 ASP A OD2 331 N N . ALA A 50 ? 0.2221 0.3984 0.2386 -0.0781 0.0986 -0.0197 1047 ALA A N 332 C CA . ALA A 50 ? 0.2310 0.3885 0.2222 -0.0595 0.0913 -0.0109 1047 ALA A CA 333 C C . ALA A 50 ? 0.2698 0.3880 0.2161 -0.0502 0.0850 -0.0118 1047 ALA A C 334 O O . ALA A 50 ? 0.2718 0.4002 0.2203 -0.0392 0.0878 -0.0082 1047 ALA A O 335 C CB . ALA A 50 ? 0.2230 0.3901 0.2266 -0.0615 0.0776 0.0010 1047 ALA A CB 336 N N . PRO A 51 ? 0.2971 0.4065 0.2143 -0.0375 0.0860 -0.0227 1048 PRO A N 337 C CA . PRO A 51 ? 0.3431 0.4237 0.2167 -0.0163 0.0882 -0.0230 1048 PRO A CA 338 C C . PRO A 51 ? 0.3795 0.4402 0.2257 0.0120 0.0996 -0.0038 1048 PRO A C 339 O O . PRO A 51 ? 0.3943 0.4666 0.2240 0.0204 0.0974 -0.0035 1048 PRO A O 340 C CB . PRO A 51 ? 0.3433 0.4203 0.2175 -0.0197 0.0895 -0.0274 1048 PRO A CB 341 C CG . PRO A 51 ? 0.3249 0.4144 0.2108 -0.0351 0.0763 -0.0359 1048 PRO A CG 342 C CD . PRO A 51 ? 0.3009 0.3930 0.2201 -0.0436 0.0776 -0.0285 1048 PRO A CD 343 N N . SER A 52 ? 0.3759 0.4327 0.2489 0.0263 0.1190 0.0216 1049 SER A N 344 C CA A SER A 52 ? 0.3957 0.4347 0.2572 0.0285 0.1305 0.0320 1049 SER A CA 345 C CA B SER A 52 ? 0.3905 0.4347 0.2685 0.0305 0.1208 0.0438 1049 SER A CA 346 C C . SER A 52 ? 0.4117 0.4298 0.2567 0.0302 0.1342 0.0436 1049 SER A C 347 O O . SER A 52 ? 0.4052 0.4287 0.2651 0.0261 0.1404 0.0449 1049 SER A O 348 C CB A SER A 52 ? 0.3901 0.4314 0.2687 0.0263 0.1324 0.0361 1049 SER A CB 349 C CB B SER A 52 ? 0.3822 0.4379 0.2849 0.0274 0.1208 0.0511 1049 SER A CB 350 O OG A SER A 52 ? 0.3853 0.4623 0.2773 0.0219 0.1366 0.0205 1049 SER A OG 351 O OG B SER A 52 ? 0.3919 0.4474 0.3257 0.0247 0.0917 0.0700 1049 SER A OG 352 N N . SER A 53 ? 0.4462 0.4329 0.2469 0.0206 0.1491 0.0368 1050 SER A N 353 C CA . SER A 53 ? 0.4708 0.4462 0.2569 0.0208 0.1289 0.0386 1050 SER A CA 354 C C . SER A 53 ? 0.4942 0.4535 0.2768 0.0054 0.1171 0.0592 1050 SER A C 355 O O . SER A 53 ? 0.4787 0.4738 0.2842 0.0073 0.1168 0.0568 1050 SER A O 356 C CB . SER A 53 ? 0.4625 0.4417 0.2319 0.0296 0.1365 0.0313 1050 SER A CB 357 O OG . SER A 53 ? 0.4539 0.4674 0.2590 0.0434 0.1111 0.0370 1050 SER A OG 358 N N . GLU A 54 ? 0.5278 0.4375 0.3303 -0.0171 0.0744 0.0882 1051 GLU A N 359 C CA . GLU A 54 ? 0.5605 0.4329 0.3420 -0.0241 0.0548 0.1096 1051 GLU A CA 360 C C . GLU A 54 ? 0.5375 0.4401 0.3030 -0.0065 0.0509 0.1146 1051 GLU A C 361 O O . GLU A 54 ? 0.5493 0.4638 0.2949 -0.0093 0.0423 0.1199 1051 GLU A O 362 C CB . GLU A 54 ? 0.5849 0.4223 0.3659 -0.0353 0.0540 0.1168 1051 GLU A CB 363 C CG . GLU A 54 ? 0.6452 0.4426 0.4185 -0.0555 0.0623 0.1031 1051 GLU A CG 364 C CD . GLU A 54 ? 0.7099 0.4767 0.4690 -0.0754 0.1014 0.0979 1051 GLU A CD 365 O OE1 . GLU A 54 ? 0.7257 0.5077 0.5019 -0.0768 0.1074 0.0803 1051 GLU A OE1 366 O OE2 . GLU A 54 ? 0.7529 0.5041 0.4765 -0.0619 0.1092 0.1053 1051 GLU A OE2 367 N N . VAL A 55 ? 0.4924 0.4345 0.2642 0.0337 0.0653 0.0925 1052 VAL A N 368 C CA . VAL A 55 ? 0.4706 0.4305 0.2486 0.0529 0.0610 0.0767 1052 VAL A CA 369 C C . VAL A 55 ? 0.4881 0.4541 0.2361 0.0494 0.0384 0.0666 1052 VAL A C 370 O O . VAL A 55 ? 0.4913 0.4553 0.2484 0.0540 0.0399 0.0571 1052 VAL A O 371 C CB . VAL A 55 ? 0.4474 0.4277 0.2390 0.0606 0.0759 0.0662 1052 VAL A CB 372 C CG1 . VAL A 55 ? 0.4248 0.4239 0.2515 0.0644 0.0825 0.0696 1052 VAL A CG1 373 C CG2 . VAL A 55 ? 0.4596 0.4239 0.2696 0.0662 0.0623 0.0584 1052 VAL A CG2 374 N N . LYS A 56 ? 0.5141 0.4845 0.2453 0.0350 -0.0054 0.0772 1053 LYS A N 375 C CA . LYS A 56 ? 0.5138 0.5134 0.2504 0.0261 -0.0450 0.0758 1053 LYS A CA 376 C C . LYS A 56 ? 0.4250 0.4758 0.2187 0.0423 -0.0230 0.0505 1053 LYS A C 377 O O . LYS A 56 ? 0.4099 0.4917 0.2187 0.0573 -0.0274 0.0425 1053 LYS A O 378 C CB . LYS A 56 ? 0.5647 0.5483 0.2685 0.0186 -0.0658 0.0908 1053 LYS A CB 379 C CG . LYS A 56 ? 0.6121 0.6704 0.3495 0.0227 -0.1058 0.0895 1053 LYS A CG 380 C CD . LYS A 56 ? 0.6603 0.8191 0.4045 0.0428 -0.1154 0.0732 1053 LYS A CD 381 C CE . LYS A 56 ? 0.6664 0.8790 0.4178 0.0516 -0.1181 0.0544 1053 LYS A CE 382 N NZ . LYS A 56 ? 0.6751 0.9114 0.4117 0.0507 -0.1212 0.0509 1053 LYS A NZ 383 N N . PHE A 57 ? 0.3258 0.4237 0.1878 0.0379 -0.0010 0.0137 1054 PHE A N 384 C CA . PHE A 57 ? 0.2381 0.3941 0.1728 0.0328 0.0076 -0.0120 1054 PHE A CA 385 C C . PHE A 57 ? 0.2034 0.4041 0.1797 0.0340 0.0107 -0.0304 1054 PHE A C 386 O O . PHE A 57 ? 0.2117 0.4131 0.2073 0.0406 0.0153 -0.0410 1054 PHE A O 387 C CB . PHE A 57 ? 0.2148 0.3740 0.1684 0.0346 0.0153 -0.0141 1054 PHE A CB 388 C CG . PHE A 57 ? 0.2184 0.3537 0.1735 0.0285 0.0153 -0.0087 1054 PHE A CG 389 C CD1 . PHE A 57 ? 0.2336 0.3269 0.1648 0.0482 0.0305 0.0040 1054 PHE A CD1 390 C CD2 . PHE A 57 ? 0.2380 0.3404 0.1861 0.0207 0.0419 -0.0031 1054 PHE A CD2 391 C CE1 . PHE A 57 ? 0.2354 0.3400 0.1949 0.0399 0.0366 -0.0062 1054 PHE A CE1 392 C CE2 . PHE A 57 ? 0.2511 0.3366 0.1993 0.0063 0.0507 -0.0037 1054 PHE A CE2 393 C CZ . PHE A 57 ? 0.2842 0.3355 0.2055 0.0137 0.0562 0.0000 1054 PHE A CZ 394 N N . LYS A 58 ? 0.1738 0.4126 0.1770 0.0370 -0.0070 -0.0282 1055 LYS A N 395 C CA . LYS A 58 ? 0.1500 0.4235 0.1861 0.0272 -0.0252 -0.0296 1055 LYS A CA 396 C C . LYS A 58 ? 0.1189 0.4038 0.1764 0.0293 -0.0197 -0.0333 1055 LYS A C 397 O O . LYS A 58 ? 0.1164 0.4104 0.1932 0.0241 -0.0031 -0.0438 1055 LYS A O 398 C CB . LYS A 58 ? 0.1527 0.4336 0.2106 0.0315 -0.0326 -0.0285 1055 LYS A CB 399 C CG . LYS A 58 ? 0.1737 0.4717 0.2606 0.0109 -0.0582 -0.0417 1055 LYS A CG 400 C CD . LYS A 58 ? 0.1773 0.5044 0.3524 0.0031 -0.0678 -0.0662 1055 LYS A CD 401 C CE . LYS A 58 ? 0.1817 0.5292 0.4259 -0.0285 -0.0684 -0.0794 1055 LYS A CE 402 N NZ . LYS A 58 ? 0.2319 0.5572 0.4722 -0.0197 -0.0750 -0.0974 1055 LYS A NZ 403 N N . TYR A 59 ? 0.0981 0.3874 0.1676 0.0148 -0.0141 -0.0230 1056 TYR A N 404 C CA . TYR A 59 ? 0.0770 0.3664 0.1738 0.0131 -0.0071 -0.0262 1056 TYR A CA 405 C C . TYR A 59 ? 0.0664 0.3334 0.1761 0.0219 -0.0098 -0.0259 1056 TYR A C 406 O O . TYR A 59 ? 0.0847 0.3258 0.1993 0.0263 -0.0125 -0.0175 1056 TYR A O 407 C CB . TYR A 59 ? 0.0585 0.3869 0.1770 0.0092 0.0006 -0.0285 1056 TYR A CB 408 C CG . TYR A 59 ? 0.0675 0.4110 0.1867 0.0070 -0.0006 -0.0511 1056 TYR A CG 409 C CD1 . TYR A 59 ? 0.0833 0.4320 0.2017 0.0097 0.0057 -0.0820 1056 TYR A CD1 410 C CD2 . TYR A 59 ? 0.1084 0.4316 0.2002 0.0195 -0.0207 -0.0544 1056 TYR A CD2 411 C CE1 . TYR A 59 ? 0.1075 0.4435 0.2280 0.0109 -0.0065 -0.0750 1056 TYR A CE1 412 C CE2 . TYR A 59 ? 0.0971 0.4528 0.2108 -0.0035 -0.0131 -0.0820 1056 TYR A CE2 413 C CZ . TYR A 59 ? 0.0863 0.4623 0.2386 0.0107 -0.0141 -0.0825 1056 TYR A CZ 414 O OH . TYR A 59 ? 0.1324 0.4949 0.2779 -0.0252 -0.0307 -0.0746 1056 TYR A OH 415 N N . VAL A 60 ? 0.0604 0.3269 0.1843 0.0263 -0.0093 -0.0344 1057 VAL A N 416 C CA . VAL A 60 ? 0.0623 0.3264 0.1771 0.0109 -0.0005 -0.0302 1057 VAL A CA 417 C C . VAL A 60 ? 0.0482 0.3125 0.1773 -0.0023 0.0043 -0.0370 1057 VAL A C 418 O O . VAL A 60 ? 0.0759 0.3190 0.1976 -0.0087 0.0035 -0.0395 1057 VAL A O 419 C CB . VAL A 60 ? 0.0705 0.3336 0.1849 -0.0003 0.0031 -0.0274 1057 VAL A CB 420 C CG1 . VAL A 60 ? 0.0498 0.3804 0.2029 0.0313 0.0049 -0.0392 1057 VAL A CG1 421 C CG2 . VAL A 60 ? 0.1123 0.3289 0.1999 -0.0070 0.0219 -0.0205 1057 VAL A CG2 422 N N . LEU A 61 ? 0.0426 0.2969 0.1738 -0.0015 0.0006 -0.0280 1058 LEU A N 423 C CA . LEU A 61 ? 0.0260 0.2998 0.1808 0.0088 0.0065 -0.0230 1058 LEU A CA 424 C C . LEU A 61 ? 0.0263 0.2883 0.1747 0.0052 0.0112 -0.0210 1058 LEU A C 425 O O . LEU A 61 ? 0.0269 0.2880 0.1853 0.0000 0.0160 -0.0240 1058 LEU A O 426 C CB . LEU A 61 ? 0.0306 0.3172 0.2020 0.0113 0.0162 -0.0283 1058 LEU A CB 427 C CG . LEU A 61 ? 0.0307 0.3503 0.2381 0.0194 0.0295 -0.0060 1058 LEU A CG 428 C CD1 . LEU A 61 ? 0.1246 0.3709 0.2673 0.0252 0.0599 -0.0097 1058 LEU A CD1 429 C CD2 . LEU A 61 ? 0.0421 0.4025 0.2779 0.0296 0.0606 0.0038 1058 LEU A CD2 430 N N . ASN A 62 ? 0.0269 0.2935 0.1896 0.0074 0.0148 -0.0054 1059 ASN A N 431 C CA . ASN A 62 ? 0.0281 0.2944 0.1738 0.0092 0.0186 -0.0118 1059 ASN A CA 432 C C . ASN A 62 ? 0.0286 0.2754 0.1835 0.0105 0.0210 -0.0074 1059 ASN A C 433 O O . ASN A 62 ? 0.0306 0.2795 0.2034 0.0093 0.0294 -0.0043 1059 ASN A O 434 C CB . ASN A 62 ? 0.0281 0.3025 0.1863 0.0172 0.0148 -0.0215 1059 ASN A CB 435 C CG . ASN A 62 ? 0.0346 0.3124 0.1692 0.0252 0.0306 -0.0125 1059 ASN A CG 436 O OD1 . ASN A 62 ? 0.0377 0.3402 0.1888 0.0217 0.0401 -0.0249 1059 ASN A OD1 437 N ND2 . ASN A 62 ? 0.0410 0.3055 0.2310 0.0076 0.0555 -0.0204 1059 ASN A ND2 438 N N . LEU A 63 ? 0.0276 0.2991 0.1755 0.0057 0.0175 -0.0126 1060 LEU A N 439 C CA . LEU A 63 ? 0.0284 0.3124 0.1995 0.0283 0.0048 -0.0206 1060 LEU A CA 440 C C . LEU A 63 ? 0.0302 0.3269 0.1958 0.0353 0.0098 -0.0092 1060 LEU A C 441 O O . LEU A 63 ? 0.0289 0.3346 0.2011 0.0285 0.0109 -0.0118 1060 LEU A O 442 C CB . LEU A 63 ? 0.0298 0.3025 0.2055 0.0349 0.0026 -0.0170 1060 LEU A CB 443 C CG . LEU A 63 ? 0.0593 0.3483 0.3858 0.0417 -0.0031 -0.0715 1060 LEU A CG 444 C CD1 . LEU A 63 ? 0.0483 0.3379 0.3600 0.0571 -0.0206 -0.0586 1060 LEU A CD1 445 C CD2 . LEU A 63 ? 0.0408 0.3424 0.3388 0.0623 -0.0054 -0.0803 1060 LEU A CD2 446 N N . THR A 64 ? 0.0344 0.3194 0.2238 0.0423 0.0219 -0.0142 1061 THR A N 447 C CA . THR A 64 ? 0.0357 0.3416 0.2401 0.0502 0.0226 0.0000 1061 THR A CA 448 C C . THR A 64 ? 0.0386 0.3418 0.2465 0.0582 0.0238 0.0015 1061 THR A C 449 O O . THR A 64 ? 0.0337 0.3452 0.2720 0.0493 0.0148 0.0068 1061 THR A O 450 C CB . THR A 64 ? 0.0313 0.3459 0.2423 0.0393 0.0149 -0.0063 1061 THR A CB 451 O OG1 . THR A 64 ? 0.0296 0.3612 0.2569 0.0266 0.0216 -0.0119 1061 THR A OG1 452 C CG2 . THR A 64 ? 0.0315 0.3479 0.2596 0.0446 0.0023 -0.0011 1061 THR A CG2 453 N N . MET A 65 ? 0.0456 0.3503 0.2565 0.0762 0.0263 0.0109 1062 MET A N 454 C CA . MET A 65 ? 0.0611 0.3671 0.2682 0.0854 0.0284 0.0068 1062 MET A CA 455 C C . MET A 65 ? 0.0886 0.3731 0.2795 0.0917 0.0377 0.0031 1062 MET A C 456 O O . MET A 65 ? 0.1360 0.3770 0.3070 0.0816 0.0524 -0.0065 1062 MET A O 457 C CB . MET A 65 ? 0.0531 0.3797 0.2718 0.0974 0.0186 0.0126 1062 MET A CB 458 C CG . MET A 65 ? 0.0746 0.3955 0.2833 0.0833 0.0119 0.0037 1062 MET A CG 459 S SD . MET A 65 ? 0.0741 0.4246 0.3197 0.0680 0.0153 0.0260 1062 MET A SD 460 C CE . MET A 65 ? 0.0855 0.4336 0.4059 0.0675 0.0417 0.0163 1062 MET A CE 461 N N A ASP A 66 ? 0.0759 0.3975 0.2736 0.0834 0.0472 0.0038 1063 ASP A N 462 N N B ASP A 66 ? 0.0758 0.3975 0.2736 0.0834 0.0472 0.0038 1063 ASP A N 463 C CA A ASP A 66 ? 0.0921 0.3982 0.2763 0.0737 0.0586 0.0006 1063 ASP A CA 464 C CA B ASP A 66 ? 0.0919 0.3982 0.2763 0.0737 0.0586 0.0006 1063 ASP A CA 465 C C A ASP A 66 ? 0.0876 0.3743 0.2723 0.0706 0.0749 0.0006 1063 ASP A C 466 C C B ASP A 66 ? 0.0878 0.3745 0.2723 0.0706 0.0746 0.0006 1063 ASP A C 467 O O A ASP A 66 ? 0.0816 0.3720 0.2773 0.0706 0.0789 -0.0017 1063 ASP A O 468 O O B ASP A 66 ? 0.0847 0.3727 0.2781 0.0706 0.0771 -0.0019 1063 ASP A O 469 C CB A ASP A 66 ? 0.0974 0.4151 0.2745 0.0680 0.0579 0.0031 1063 ASP A CB 470 C CB B ASP A 66 ? 0.0962 0.4156 0.2743 0.0680 0.0575 0.0031 1063 ASP A CB 471 C CG A ASP A 66 ? 0.0988 0.4038 0.2739 0.0324 0.0502 0.0096 1063 ASP A CG 472 C CG B ASP A 66 ? 0.1067 0.4088 0.2811 0.0351 0.0496 0.0054 1063 ASP A CG 473 O OD1 A ASP A 66 ? 0.0991 0.4201 0.2921 0.0296 0.0423 0.0230 1063 ASP A OD1 474 O OD1 B ASP A 66 ? 0.1115 0.4111 0.2939 0.0513 0.0181 0.0228 1063 ASP A OD1 475 O OD2 A ASP A 66 ? 0.1333 0.4162 0.2908 0.0087 0.0425 0.0109 1063 ASP A OD2 476 O OD2 B ASP A 66 ? 0.0935 0.4158 0.2980 0.0205 0.0366 0.0065 1063 ASP A OD2 477 N N . LYS A 67 ? 0.0943 0.3521 0.2777 0.0449 0.0917 0.0071 1064 LYS A N 478 C CA . LYS A 67 ? 0.1429 0.3393 0.2903 0.0031 0.0987 0.0147 1064 LYS A CA 479 C C . LYS A 67 ? 0.1630 0.3192 0.2901 0.0020 0.1120 0.0175 1064 LYS A C 480 O O . LYS A 67 ? 0.2185 0.3298 0.3136 0.0052 0.1251 0.0124 1064 LYS A O 481 C CB . LYS A 67 ? 0.1479 0.3470 0.3156 -0.0126 0.0992 0.0087 1064 LYS A CB 482 C CG . LYS A 67 ? 0.1967 0.3826 0.3630 -0.0186 0.0803 -0.0186 1064 LYS A CG 483 C CD . LYS A 67 ? 0.2335 0.4097 0.4368 -0.0350 0.0736 -0.0307 1064 LYS A CD 484 C CE . LYS A 67 ? 0.2847 0.4338 0.4870 -0.0272 0.0798 -0.0284 1064 LYS A CE 485 N NZ . LYS A 67 ? 0.2784 0.4314 0.5113 -0.0339 0.0768 -0.0498 1064 LYS A NZ 486 N N . TYR A 68 ? 0.1061 0.3082 0.2829 -0.0015 0.1000 0.0247 1065 TYR A N 487 C CA . TYR A 68 ? 0.1034 0.3039 0.2682 0.0068 0.0939 0.0192 1065 TYR A CA 488 C C . TYR A 68 ? 0.1042 0.3115 0.2694 0.0012 0.0988 0.0137 1065 TYR A C 489 O O . TYR A 68 ? 0.0972 0.3282 0.2847 -0.0040 0.0872 0.0082 1065 TYR A O 490 C CB . TYR A 68 ? 0.0681 0.3027 0.2815 0.0087 0.0803 0.0228 1065 TYR A CB 491 C CG . TYR A 68 ? 0.0723 0.3104 0.2515 0.0181 0.0627 0.0175 1065 TYR A CG 492 C CD1 . TYR A 68 ? 0.0462 0.3395 0.2388 0.0317 0.0625 0.0131 1065 TYR A CD1 493 C CD2 . TYR A 68 ? 0.0377 0.3294 0.2337 0.0186 0.0493 0.0194 1065 TYR A CD2 494 C CE1 . TYR A 68 ? 0.0482 0.3583 0.2327 0.0296 0.0577 0.0063 1065 TYR A CE1 495 C CE2 . TYR A 68 ? 0.0308 0.3292 0.2318 0.0096 0.0333 0.0131 1065 TYR A CE2 496 C CZ . TYR A 68 ? 0.0620 0.3443 0.2275 0.0247 0.0599 0.0173 1065 TYR A CZ 497 O OH . TYR A 68 ? 0.0329 0.3420 0.2240 0.0229 0.0236 0.0017 1065 TYR A OH 498 N N . THR A 69 ? 0.1421 0.3167 0.2606 0.0068 0.1062 0.0118 1066 THR A N 499 C CA . THR A 69 ? 0.1527 0.3282 0.2687 0.0141 0.1180 0.0082 1066 THR A CA 500 C C . THR A 69 ? 0.1322 0.3303 0.2469 0.0005 0.1005 0.0103 1066 THR A C 501 O O . THR A 69 ? 0.1384 0.3434 0.2569 -0.0102 0.0952 0.0057 1066 THR A O 502 C CB . THR A 69 ? 0.1720 0.3346 0.2739 0.0109 0.1185 0.0037 1066 THR A CB 503 O OG1 . THR A 69 ? 0.2017 0.3585 0.3215 0.0377 0.1420 0.0031 1066 THR A OG1 504 C CG2 . THR A 69 ? 0.2099 0.3373 0.3138 0.0153 0.1456 0.0035 1066 THR A CG2 505 N N . LEU A 70 ? 0.1351 0.3240 0.2284 0.0081 0.0850 -0.0013 1067 LEU A N 506 C CA . LEU A 70 ? 0.1098 0.3188 0.2266 0.0065 0.0631 -0.0197 1067 LEU A CA 507 C C . LEU A 70 ? 0.1305 0.3237 0.2266 0.0063 0.0658 -0.0197 1067 LEU A C 508 O O . LEU A 70 ? 0.1263 0.3630 0.2336 -0.0043 0.0590 -0.0258 1067 LEU A O 509 C CB . LEU A 70 ? 0.1150 0.3203 0.2187 0.0120 0.0584 -0.0252 1067 LEU A CB 510 C CG . LEU A 70 ? 0.0935 0.3348 0.2374 0.0035 0.0438 -0.0294 1067 LEU A CG 511 C CD1 . LEU A 70 ? 0.1342 0.3463 0.2675 0.0357 0.0438 -0.0388 1067 LEU A CD1 512 C CD2 . LEU A 70 ? 0.1331 0.3495 0.2937 -0.0109 0.0186 -0.0318 1067 LEU A CD2 513 N N . PRO A 71 ? 0.1342 0.3357 0.2495 0.0049 0.0838 -0.0271 1068 PRO A N 514 C CA . PRO A 71 ? 0.1418 0.3294 0.2698 -0.0103 0.0934 -0.0296 1068 PRO A CA 515 C C . PRO A 71 ? 0.1392 0.3499 0.2628 -0.0230 0.0942 -0.0315 1068 PRO A C 516 O O . PRO A 71 ? 0.1428 0.3716 0.2840 -0.0342 0.0776 -0.0333 1068 PRO A O 517 C CB . PRO A 71 ? 0.1523 0.3388 0.2908 -0.0030 0.1018 -0.0401 1068 PRO A CB 518 C CG . PRO A 71 ? 0.1525 0.3495 0.2628 -0.0006 0.0926 -0.0313 1068 PRO A CG 519 C CD . PRO A 71 ? 0.1287 0.3474 0.2576 0.0070 0.0895 -0.0219 1068 PRO A CD 520 N N . ASN A 72 ? 0.1052 0.3481 0.2592 -0.0197 0.0876 -0.0063 1069 ASN A N 521 C CA . ASN A 72 ? 0.1186 0.3655 0.2581 -0.0183 0.0741 0.0076 1069 ASN A CA 522 C C . ASN A 72 ? 0.1272 0.3621 0.2599 -0.0185 0.0634 0.0104 1069 ASN A C 523 O O . ASN A 72 ? 0.1659 0.3865 0.2682 -0.0140 0.0619 0.0219 1069 ASN A O 524 C CB . ASN A 72 ? 0.1076 0.3562 0.2671 -0.0120 0.0842 0.0153 1069 ASN A CB 525 C CG . ASN A 72 ? 0.1115 0.3601 0.2635 -0.0062 0.0793 0.0068 1069 ASN A CG 526 O OD1 . ASN A 72 ? 0.1168 0.4077 0.2610 0.0035 0.0665 -0.0119 1069 ASN A OD1 527 N ND2 . ASN A 72 ? 0.0734 0.3711 0.3201 -0.0071 0.0652 -0.0218 1069 ASN A ND2 528 N N . SER A 73 ? 0.1106 0.3734 0.2592 -0.0230 0.0403 -0.0160 1070 SER A N 529 C CA . SER A 73 ? 0.1036 0.3840 0.2682 -0.0274 0.0237 -0.0410 1070 SER A CA 530 C C . SER A 73 ? 0.1036 0.3986 0.2594 -0.0263 0.0006 -0.0467 1070 SER A C 531 O O . SER A 73 ? 0.1069 0.3858 0.3070 -0.0386 0.0219 -0.0463 1070 SER A O 532 C CB . SER A 73 ? 0.1186 0.3810 0.2829 -0.0130 -0.0006 -0.0595 1070 SER A CB 533 O OG . SER A 73 ? 0.1421 0.4413 0.2996 -0.0252 0.0307 -0.0675 1070 SER A OG 534 N N . ASN A 74 ? 0.0921 0.4453 0.2213 -0.0170 -0.0051 -0.0560 1071 ASN A N 535 C CA . ASN A 74 ? 0.1054 0.4805 0.2011 -0.0003 -0.0120 -0.0579 1071 ASN A CA 536 C C . ASN A 74 ? 0.1097 0.4352 0.1884 -0.0038 0.0000 -0.0582 1071 ASN A C 537 O O . ASN A 74 ? 0.0945 0.4557 0.1958 -0.0057 -0.0020 -0.0634 1071 ASN A O 538 C CB . ASN A 74 ? 0.1368 0.5307 0.2124 -0.0010 -0.0170 -0.0386 1071 ASN A CB 539 C CG . ASN A 74 ? 0.2020 0.6211 0.2407 0.0658 -0.0392 -0.0185 1071 ASN A CG 540 O OD1 . ASN A 74 ? 0.2533 0.6521 0.2757 0.0903 -0.0581 -0.0026 1071 ASN A OD1 541 N ND2 . ASN A 74 ? 0.3160 0.7171 0.2870 0.1027 -0.0652 0.0080 1071 ASN A ND2 542 N N . ILE A 75 ? 0.1162 0.4117 0.1779 -0.0109 0.0208 -0.0631 1072 ILE A N 543 C CA . ILE A 75 ? 0.1186 0.3986 0.1840 -0.0208 0.0263 -0.0604 1072 ILE A CA 544 C C . ILE A 75 ? 0.1000 0.3984 0.1888 -0.0173 0.0370 -0.0640 1072 ILE A C 545 O O . ILE A 75 ? 0.0918 0.3925 0.2239 -0.0250 0.0412 -0.0627 1072 ILE A O 546 C CB . ILE A 75 ? 0.1221 0.3887 0.1878 -0.0153 0.0216 -0.0590 1072 ILE A CB 547 C CG1 . ILE A 75 ? 0.1474 0.3921 0.2140 -0.0252 0.0241 -0.0474 1072 ILE A CG1 548 C CG2 . ILE A 75 ? 0.1315 0.4266 0.1826 -0.0370 0.0250 -0.0553 1072 ILE A CG2 549 C CD1 . ILE A 75 ? 0.1588 0.3790 0.2520 -0.0229 0.0027 -0.0335 1072 ILE A CD1 550 N N . ASN A 76 ? 0.0798 0.4140 0.1914 -0.0184 0.0285 -0.0606 1073 ASN A N 551 C CA . ASN A 76 ? 0.0961 0.4047 0.2161 -0.0230 0.0250 -0.0595 1073 ASN A CA 552 C C . ASN A 76 ? 0.1080 0.3395 0.2081 -0.0093 0.0238 -0.0516 1073 ASN A C 553 O O . ASN A 76 ? 0.0890 0.3341 0.2116 -0.0038 0.0119 -0.0533 1073 ASN A O 554 C CB . ASN A 76 ? 0.1025 0.4481 0.2460 -0.0487 0.0241 -0.0648 1073 ASN A CB 555 C CG . ASN A 76 ? 0.1764 0.5284 0.3395 -0.0991 0.0000 -0.0362 1073 ASN A CG 556 O OD1 . ASN A 76 ? 0.2476 0.6118 0.4169 -0.1377 -0.0010 -0.0062 1073 ASN A OD1 557 N ND2 . ASN A 76 ? 0.2603 0.5866 0.4557 -0.1357 -0.0197 -0.0282 1073 ASN A ND2 558 N N . ILE A 77 ? 0.0986 0.3176 0.2064 0.0052 0.0381 -0.0390 1074 ILE A N 559 C CA . ILE A 77 ? 0.0830 0.3097 0.2237 0.0048 0.0460 -0.0359 1074 ILE A CA 560 C C . ILE A 77 ? 0.0938 0.2980 0.2099 -0.0005 0.0439 -0.0445 1074 ILE A C 561 O O . ILE A 77 ? 0.1288 0.3018 0.2504 -0.0024 0.0644 -0.0458 1074 ILE A O 562 C CB . ILE A 77 ? 0.0761 0.3106 0.2345 0.0103 0.0518 -0.0403 1074 ILE A CB 563 C CG1 . ILE A 77 ? 0.1102 0.3515 0.2732 0.0107 0.0520 -0.0252 1074 ILE A CG1 564 C CG2 . ILE A 77 ? 0.0786 0.3231 0.2608 -0.0041 0.0296 -0.0296 1074 ILE A CG2 565 C CD1 . ILE A 77 ? 0.0805 0.3980 0.3048 0.0065 0.0571 -0.0489 1074 ILE A CD1 566 N N . ILE A 78 ? 0.0761 0.3088 0.2029 -0.0120 0.0307 -0.0419 1075 ILE A N 567 C CA . ILE A 78 ? 0.0636 0.3404 0.2161 -0.0225 0.0208 -0.0284 1075 ILE A CA 568 C C . ILE A 78 ? 0.0474 0.3106 0.2184 -0.0195 0.0272 -0.0208 1075 ILE A C 569 O O . ILE A 78 ? 0.0505 0.3199 0.2361 -0.0147 0.0098 -0.0252 1075 ILE A O 570 C CB . ILE A 78 ? 0.0588 0.3688 0.2284 -0.0227 0.0217 -0.0216 1075 ILE A CB 571 C CG1 . ILE A 78 ? 0.1316 0.4140 0.2689 -0.0432 -0.0130 -0.0248 1075 ILE A CG1 572 C CG2 . ILE A 78 ? 0.0780 0.4023 0.2398 -0.0366 0.0326 -0.0164 1075 ILE A CG2 573 C CD1 . ILE A 78 ? 0.2682 0.4753 0.3454 -0.0719 -0.0307 -0.0230 1075 ILE A CD1 574 N N . HIS A 79 ? 0.0514 0.3106 0.2319 -0.0159 0.0318 -0.0120 1076 HIS A N 575 C CA . HIS A 79 ? 0.0549 0.3046 0.2370 0.0017 0.0474 -0.0068 1076 HIS A CA 576 C C . HIS A 79 ? 0.0443 0.2921 0.2435 0.0010 0.0474 -0.0098 1076 HIS A C 577 O O . HIS A 79 ? 0.0691 0.2926 0.2685 -0.0193 0.0500 -0.0046 1076 HIS A O 578 C CB . HIS A 79 ? 0.0357 0.3138 0.2492 0.0003 0.0480 -0.0173 1076 HIS A CB 579 C CG . HIS A 79 ? 0.0500 0.3222 0.2506 0.0074 0.0476 -0.0081 1076 HIS A CG 580 N ND1 . HIS A 79 ? 0.0741 0.3321 0.2675 0.0151 0.0588 -0.0003 1076 HIS A ND1 581 C CD2 . HIS A 79 ? 0.0406 0.3291 0.2529 0.0085 0.0397 -0.0013 1076 HIS A CD2 582 C CE1 . HIS A 79 ? 0.0744 0.3413 0.2617 0.0474 0.0408 0.0031 1076 HIS A CE1 583 N NE2 . HIS A 79 ? 0.0535 0.3312 0.2707 0.0346 0.0392 0.0082 1076 HIS A NE2 584 N N . ILE A 80 ? 0.0359 0.2980 0.2293 0.0049 0.0460 -0.0081 1077 ILE A N 585 C CA . ILE A 80 ? 0.0802 0.3091 0.2458 0.0183 0.0570 -0.0118 1077 ILE A CA 586 C C . ILE A 80 ? 0.0834 0.2754 0.2335 0.0152 0.0597 -0.0043 1077 ILE A C 587 O O . ILE A 80 ? 0.0697 0.2732 0.2484 0.0114 0.0603 0.0024 1077 ILE A O 588 C CB . ILE A 80 ? 0.1005 0.3370 0.2632 0.0239 0.0538 -0.0125 1077 ILE A CB 589 C CG1 . ILE A 80 ? 0.0878 0.4097 0.3064 0.0627 0.0546 -0.0324 1077 ILE A CG1 590 C CG2 . ILE A 80 ? 0.1226 0.3828 0.2851 0.0204 0.0776 -0.0263 1077 ILE A CG2 591 C CD1 . ILE A 80 ? 0.1103 0.4535 0.3614 0.0798 0.0630 -0.0317 1077 ILE A CD1 592 N N . PRO A 81 ? 0.0846 0.2809 0.2655 0.0197 0.0498 -0.0129 1078 PRO A N 593 C CA . PRO A 81 ? 0.0980 0.2969 0.2619 0.0241 0.0412 -0.0230 1078 PRO A CA 594 C C . PRO A 81 ? 0.1018 0.3068 0.2599 0.0252 0.0454 -0.0208 1078 PRO A C 595 O O . PRO A 81 ? 0.1412 0.3188 0.2725 0.0049 0.0494 -0.0076 1078 PRO A O 596 C CB . PRO A 81 ? 0.1084 0.2991 0.2754 0.0252 0.0392 -0.0247 1078 PRO A CB 597 C CG . PRO A 81 ? 0.0842 0.2860 0.2831 0.0270 0.0405 -0.0181 1078 PRO A CG 598 C CD . PRO A 81 ? 0.0922 0.2791 0.2768 0.0175 0.0458 -0.0093 1078 PRO A CD 599 N N . LEU A 82 ? 0.0368 0.3242 0.2328 0.0329 0.0348 -0.0205 1079 LEU A N 600 C CA . LEU A 82 ? 0.0359 0.3440 0.2345 0.0452 0.0208 -0.0152 1079 LEU A CA 601 C C . LEU A 82 ? 0.0370 0.3398 0.2056 0.0472 0.0266 -0.0114 1079 LEU A C 602 O O . LEU A 82 ? 0.0326 0.3720 0.2039 0.0432 0.0195 0.0097 1079 LEU A O 603 C CB . LEU A 82 ? 0.0355 0.3384 0.2527 0.0410 0.0131 -0.0160 1079 LEU A CB 604 C CG . LEU A 82 ? 0.0322 0.3797 0.2845 0.0419 0.0228 0.0057 1079 LEU A CG 605 C CD1 . LEU A 82 ? 0.0293 0.3851 0.3246 0.0320 0.0207 0.0296 1079 LEU A CD1 606 C CD2 . LEU A 82 ? 0.0893 0.3914 0.3495 0.0230 0.0348 0.0249 1079 LEU A CD2 607 N N . VAL A 83 ? 0.0395 0.3596 0.2018 0.0383 0.0219 -0.0063 1080 VAL A N 608 C CA . VAL A 83 ? 0.0518 0.3574 0.2090 0.0511 0.0109 -0.0038 1080 VAL A CA 609 C C . VAL A 83 ? 0.0392 0.3560 0.2116 0.0535 0.0074 -0.0012 1080 VAL A C 610 O O . VAL A 83 ? 0.0436 0.3759 0.2265 0.0573 0.0196 -0.0063 1080 VAL A O 611 C CB . VAL A 83 ? 0.0821 0.3564 0.2249 0.0524 0.0031 -0.0003 1080 VAL A CB 612 C CG1 . VAL A 83 ? 0.0766 0.3907 0.2558 0.0584 -0.0120 0.0005 1080 VAL A CG1 613 C CG2 . VAL A 83 ? 0.1280 0.3583 0.2520 0.0581 0.0186 0.0012 1080 VAL A CG2 614 N N . ASP A 84 ? 0.0331 0.3630 0.1985 0.0509 0.0031 -0.0005 1081 ASP A N 615 C CA . ASP A 84 ? 0.0443 0.3763 0.1817 0.0571 0.0054 0.0043 1081 ASP A CA 616 C C . ASP A 84 ? 0.0571 0.4142 0.1791 0.0798 0.0073 0.0065 1081 ASP A C 617 O O . ASP A 84 ? 0.0434 0.4481 0.2108 0.0863 -0.0068 0.0098 1081 ASP A O 618 C CB . ASP A 84 ? 0.0331 0.3689 0.2043 0.0516 0.0024 0.0041 1081 ASP A CB 619 C CG . ASP A 84 ? 0.0309 0.3765 0.1921 0.0443 -0.0024 0.0041 1081 ASP A CG 620 O OD1 . ASP A 84 ? 0.0557 0.4205 0.2027 0.0551 0.0274 -0.0031 1081 ASP A OD1 621 O OD2 . ASP A 84 ? 0.0308 0.3772 0.2646 0.0421 0.0105 0.0000 1081 ASP A OD2 622 N N . ASP A 85 ? 0.0930 0.4431 0.1788 0.1164 0.0129 0.0159 1082 ASP A N 623 C CA . ASP A 85 ? 0.1356 0.5156 0.1923 0.1824 0.0241 0.0373 1082 ASP A CA 624 C C . ASP A 85 ? 0.1570 0.5697 0.1817 0.2011 0.0252 0.0487 1082 ASP A C 625 O O . ASP A 85 ? 0.1212 0.5281 0.1885 0.1629 0.0091 0.0368 1082 ASP A O 626 C CB . ASP A 85 ? 0.1914 0.5144 0.2328 0.1905 0.0285 0.0469 1082 ASP A CB 627 C CG . ASP A 85 ? 0.2433 0.5120 0.3316 0.2046 0.0529 0.0612 1082 ASP A CG 628 O OD1 . ASP A 85 ? 0.2772 0.5008 0.4449 0.1985 0.0930 0.0815 1082 ASP A OD1 629 O OD2 . ASP A 85 ? 0.2813 0.5310 0.4286 0.2081 0.0842 0.0724 1082 ASP A OD2 630 N N . THR A 86 ? 0.1967 0.7041 0.1756 0.2388 0.0252 0.0540 1083 THR A N 631 C CA . THR A 86 ? 0.2610 0.7911 0.1879 0.2691 0.0417 0.0617 1083 THR A CA 632 C C . THR A 86 ? 0.2694 0.8093 0.2097 0.2930 0.0520 0.0908 1083 THR A C 633 O O . THR A 86 ? 0.2554 0.8403 0.2249 0.3064 0.0617 0.0986 1083 THR A O 634 C CB . THR A 86 ? 0.2775 0.8011 0.1941 0.2709 0.0296 0.0502 1083 THR A CB 635 O OG1 . THR A 86 ? 0.2894 0.7997 0.2055 0.2608 0.0285 0.0456 1083 THR A OG1 636 C CG2 . THR A 86 ? 0.3152 0.8008 0.2149 0.2748 0.0337 0.0386 1083 THR A CG2 637 N N . THR A 87 ? 0.3251 0.7713 0.2772 0.3237 0.0850 0.1280 1084 THR A N 638 C CA . THR A 87 ? 0.3943 0.7135 0.3472 0.3337 0.1168 0.1551 1084 THR A CA 639 C C . THR A 87 ? 0.3847 0.6420 0.3772 0.3000 0.1448 0.1578 1084 THR A C 640 O O . THR A 87 ? 0.4122 0.6402 0.4176 0.2937 0.1553 0.1805 1084 THR A O 641 C CB . THR A 87 ? 0.4194 0.7322 0.3598 0.3452 0.1133 0.1597 1084 THR A CB 642 O OG1 . THR A 87 ? 0.4629 0.7336 0.3898 0.3330 0.1023 0.1624 1084 THR A OG1 643 C CG2 . THR A 87 ? 0.4259 0.7206 0.3731 0.3646 0.0930 0.1518 1084 THR A CG2 644 N N . THR A 88 ? 0.3583 0.5618 0.3700 0.2583 0.1462 0.1230 1085 THR A N 645 C CA . THR A 88 ? 0.3253 0.4884 0.3625 0.1967 0.1456 0.0811 1085 THR A CA 646 C C . THR A 88 ? 0.3097 0.4004 0.3330 0.1553 0.1401 0.0570 1085 THR A C 647 O O . THR A 88 ? 0.2989 0.3819 0.3269 0.1473 0.1368 0.0586 1085 THR A O 648 C CB . THR A 88 ? 0.3337 0.5464 0.3576 0.2108 0.1490 0.0780 1085 THR A CB 649 O OG1 . THR A 88 ? 0.3576 0.5727 0.3925 0.2117 0.1395 0.0701 1085 THR A OG1 650 C CG2 . THR A 88 ? 0.3307 0.5539 0.3833 0.1958 0.1532 0.0789 1085 THR A CG2 651 N N A ASP A 89 ? 0.3125 0.3614 0.3219 0.1324 0.1230 0.0526 1086 ASP A N 652 N N B ASP A 89 ? 0.3140 0.3580 0.3294 0.1254 0.1411 0.0485 1086 ASP A N 653 C CA A ASP A 89 ? 0.2858 0.3264 0.3000 0.1026 0.1168 0.0474 1086 ASP A CA 654 C CA B ASP A 89 ? 0.3034 0.3143 0.3102 0.0864 0.1303 0.0460 1086 ASP A CA 655 C C A ASP A 89 ? 0.2405 0.3082 0.2696 0.0719 0.0838 0.0274 1086 ASP A C 656 C C B ASP A 89 ? 0.2694 0.3041 0.2842 0.0476 0.1026 0.0241 1086 ASP A C 657 O O A ASP A 89 ? 0.1693 0.3023 0.2743 0.0700 0.0785 0.0296 1086 ASP A O 658 O O B ASP A 89 ? 0.2560 0.2975 0.2926 0.0153 0.1062 0.0230 1086 ASP A O 659 C CB A ASP A 89 ? 0.3161 0.3366 0.3185 0.1076 0.1386 0.0489 1086 ASP A CB 660 C CB B ASP A 89 ? 0.3264 0.3143 0.3289 0.0952 0.1500 0.0540 1086 ASP A CB 661 C CG A ASP A 89 ? 0.3316 0.3528 0.3429 0.0939 0.1518 0.0597 1086 ASP A CG 662 C CG B ASP A 89 ? 0.3472 0.2842 0.3555 0.0847 0.1430 0.0768 1086 ASP A CG 663 O OD1 A ASP A 89 ? 0.3576 0.4056 0.3585 0.0829 0.1676 0.0579 1086 ASP A OD1 664 O OD1 B ASP A 89 ? 0.3576 0.2888 0.3885 0.0762 0.1656 0.0847 1086 ASP A OD1 665 O OD2 A ASP A 89 ? 0.3431 0.3984 0.3707 0.1098 0.1553 0.0533 1086 ASP A OD2 666 O OD2 B ASP A 89 ? 0.3562 0.2833 0.3720 0.0684 0.1518 0.0855 1086 ASP A OD2 667 N N . ILE A 90 ? 0.1720 0.3000 0.2421 0.0373 0.0533 0.0153 1087 ILE A N 668 C CA . ILE A 90 ? 0.1166 0.3228 0.2347 -0.0012 0.0131 0.0043 1087 ILE A CA 669 C C . ILE A 90 ? 0.0900 0.3176 0.2187 -0.0035 0.0192 -0.0147 1087 ILE A C 670 O O . ILE A 90 ? 0.0719 0.3226 0.2213 -0.0208 0.0080 -0.0184 1087 ILE A O 671 C CB . ILE A 90 ? 0.1150 0.3361 0.2370 -0.0135 -0.0142 0.0175 1087 ILE A CB 672 C CG1 . ILE A 90 ? 0.1230 0.3289 0.2655 -0.0269 -0.0522 0.0318 1087 ILE A CG1 673 C CG2 . ILE A 90 ? 0.1321 0.3786 0.2833 -0.0196 -0.0164 0.0148 1087 ILE A CG2 674 C CD1 . ILE A 90 ? 0.1967 0.3598 0.3160 -0.0482 -0.0785 0.0553 1087 ILE A CD1 675 N N . SER A 91 ? 0.0891 0.3251 0.2352 -0.0076 0.0318 -0.0294 1088 SER A N 676 C CA . SER A 91 ? 0.0973 0.3388 0.2524 -0.0102 0.0478 -0.0388 1088 SER A CA 677 C C . SER A 91 ? 0.0988 0.3192 0.2500 -0.0142 0.0414 -0.0252 1088 SER A C 678 O O . SER A 91 ? 0.0833 0.3409 0.2511 -0.0080 0.0441 -0.0270 1088 SER A O 679 C CB . SER A 91 ? 0.0986 0.3535 0.2633 -0.0020 0.0494 -0.0408 1088 SER A CB 680 O OG . SER A 91 ? 0.1824 0.3939 0.2987 0.0017 0.0899 -0.0329 1088 SER A OG 681 N N . LYS A 92 ? 0.1104 0.3055 0.2655 -0.0136 0.0357 -0.0147 1089 LYS A N 682 C CA . LYS A 92 ? 0.1518 0.2978 0.2736 -0.0164 0.0263 -0.0046 1089 LYS A CA 683 C C . LYS A 92 ? 0.1092 0.2867 0.2628 -0.0260 0.0344 -0.0087 1089 LYS A C 684 O O . LYS A 92 ? 0.1194 0.3097 0.2752 -0.0522 0.0417 -0.0097 1089 LYS A O 685 C CB . LYS A 92 ? 0.1850 0.3084 0.2845 0.0006 0.0124 -0.0074 1089 LYS A CB 686 C CG . LYS A 92 ? 0.2542 0.3919 0.3147 0.0447 -0.0013 -0.0285 1089 LYS A CG 687 C CD . LYS A 92 ? 0.3542 0.5194 0.3607 0.1357 -0.0152 -0.0241 1089 LYS A CD 688 C CE . LYS A 92 ? 0.4210 0.6003 0.3824 0.1720 -0.0125 -0.0326 1089 LYS A CE 689 N NZ . LYS A 92 ? 0.4350 0.6621 0.3747 0.1964 0.0076 -0.0285 1089 LYS A NZ 690 N N . TYR A 93 ? 0.0629 0.2949 0.2529 -0.0322 0.0324 -0.0104 1090 TYR A N 691 C CA . TYR A 93 ? 0.0346 0.2951 0.2477 -0.0328 0.0372 -0.0263 1090 TYR A CA 692 C C . TYR A 93 ? 0.0318 0.2928 0.2210 -0.0344 0.0239 -0.0329 1090 TYR A C 693 O O . TYR A 93 ? 0.0350 0.3203 0.2196 -0.0240 0.0206 -0.0271 1090 TYR A O 694 C CB . TYR A 93 ? 0.0410 0.3176 0.2773 -0.0342 0.0526 -0.0285 1090 TYR A CB 695 C CG . TYR A 93 ? 0.0858 0.3400 0.3634 -0.0142 0.0832 -0.0186 1090 TYR A CG 696 C CD1 . TYR A 93 ? 0.2117 0.3750 0.4178 0.0386 0.0930 -0.0361 1090 TYR A CD1 697 C CD2 . TYR A 93 ? 0.1149 0.3734 0.4582 0.0175 0.0922 0.0076 1090 TYR A CD2 698 C CE1 . TYR A 93 ? 0.2484 0.3966 0.4816 0.0612 0.1203 -0.0272 1090 TYR A CE1 699 C CE2 . TYR A 93 ? 0.1392 0.3905 0.5296 0.0185 0.1115 0.0282 1090 TYR A CE2 700 C CZ . TYR A 93 ? 0.1835 0.4029 0.5324 0.0560 0.1500 -0.0012 1090 TYR A CZ 701 O OH . TYR A 93 ? 0.2356 0.4329 0.6161 0.0588 0.1465 0.0038 1090 TYR A OH 702 N N . PHE A 94 ? 0.0306 0.2969 0.2238 -0.0186 0.0252 -0.0324 1091 PHE A N 703 C CA . PHE A 94 ? 0.0421 0.2994 0.2319 -0.0098 0.0142 -0.0397 1091 PHE A CA 704 C C . PHE A 94 ? 0.0509 0.3156 0.2457 -0.0114 0.0136 -0.0436 1091 PHE A C 705 O O . PHE A 94 ? 0.0375 0.3393 0.2457 -0.0146 0.0087 -0.0383 1091 PHE A O 706 C CB . PHE A 94 ? 0.0487 0.3088 0.2458 -0.0109 0.0120 -0.0460 1091 PHE A CB 707 C CG . PHE A 94 ? 0.0388 0.2910 0.2500 0.0120 -0.0164 -0.0456 1091 PHE A CG 708 C CD1 . PHE A 94 ? 0.0377 0.2896 0.3097 0.0098 -0.0307 -0.0269 1091 PHE A CD1 709 C CD2 . PHE A 94 ? 0.0649 0.3558 0.2727 0.0417 -0.0197 -0.0736 1091 PHE A CD2 710 C CE1 . PHE A 94 ? 0.0294 0.2966 0.3073 0.0131 -0.0324 -0.0366 1091 PHE A CE1 711 C CE2 . PHE A 94 ? 0.0995 0.3546 0.2788 0.0509 -0.0482 -0.0630 1091 PHE A CE2 712 C CZ . PHE A 94 ? 0.0865 0.3321 0.3237 0.0184 -0.0344 -0.0535 1091 PHE A CZ 713 N N . ASP A 95 ? 0.0491 0.3467 0.2594 -0.0152 0.0184 -0.0454 1092 ASP A N 714 C CA . ASP A 95 ? 0.0593 0.3903 0.2669 -0.0285 0.0197 -0.0518 1092 ASP A CA 715 C C . ASP A 95 ? 0.0571 0.3725 0.2619 -0.0293 0.0273 -0.0465 1092 ASP A C 716 O O . ASP A 95 ? 0.0412 0.3869 0.2754 -0.0293 0.0357 -0.0456 1092 ASP A O 717 C CB . ASP A 95 ? 0.0634 0.4120 0.2748 -0.0384 0.0197 -0.0494 1092 ASP A CB 718 C CG . ASP A 95 ? 0.0763 0.5188 0.3072 -0.0549 0.0381 -0.0670 1092 ASP A CG 719 O OD1 . ASP A 95 ? 0.1278 0.5924 0.3637 -0.0241 0.0520 -0.0996 1092 ASP A OD1 720 O OD2 . ASP A 95 ? 0.1148 0.6503 0.3388 -0.1133 0.0653 -0.0702 1092 ASP A OD2 721 N N . ASP A 96 ? 0.0480 0.3704 0.2639 -0.0307 0.0357 -0.0423 1093 ASP A N 722 C CA . ASP A 96 ? 0.0794 0.3495 0.2759 -0.0357 0.0241 -0.0447 1093 ASP A CA 723 C C . ASP A 96 ? 0.0295 0.3467 0.2360 -0.0219 0.0160 -0.0408 1093 ASP A C 724 O O . ASP A 96 ? 0.0350 0.3639 0.2362 -0.0346 0.0026 -0.0368 1093 ASP A O 725 C CB . ASP A 96 ? 0.1272 0.3501 0.3249 -0.0377 0.0410 -0.0527 1093 ASP A CB 726 C CG . ASP A 96 ? 0.2099 0.3564 0.4462 -0.0614 0.0428 -0.0571 1093 ASP A CG 727 O OD1 . ASP A 96 ? 0.2453 0.3878 0.5289 -0.0921 0.0388 -0.0768 1093 ASP A OD1 728 O OD2 . ASP A 96 ? 0.3075 0.3713 0.5526 -0.0706 0.0732 -0.0507 1093 ASP A OD2 729 N N . VAL A 97 ? 0.0276 0.3300 0.2221 -0.0140 0.0000 -0.0366 1094 VAL A N 730 C CA . VAL A 97 ? 0.0253 0.3368 0.2133 -0.0007 0.0000 -0.0274 1094 VAL A CA 731 C C . VAL A 97 ? 0.0253 0.3433 0.1967 -0.0031 0.0017 -0.0406 1094 VAL A C 732 O O . VAL A 97 ? 0.0265 0.3806 0.1903 0.0194 0.0028 -0.0287 1094 VAL A O 733 C CB . VAL A 97 ? 0.0258 0.3197 0.2243 0.0006 -0.0097 -0.0213 1094 VAL A CB 734 C CG1 . VAL A 97 ? 0.0263 0.3167 0.2338 0.0080 -0.0126 -0.0086 1094 VAL A CG1 735 C CG2 . VAL A 97 ? 0.0285 0.3181 0.2474 0.0295 0.0061 -0.0155 1094 VAL A CG2 736 N N . THR A 98 ? 0.0253 0.3638 0.2020 0.0026 0.0000 -0.0562 1095 THR A N 737 C CA . THR A 98 ? 0.0255 0.3817 0.2335 0.0077 -0.0019 -0.0644 1095 THR A CA 738 C C . THR A 98 ? 0.0258 0.3977 0.2477 0.0131 -0.0035 -0.0719 1095 THR A C 739 O O . THR A 98 ? 0.0271 0.4158 0.2617 0.0219 -0.0142 -0.0658 1095 THR A O 740 C CB . THR A 98 ? 0.0263 0.3822 0.2328 0.0103 0.0017 -0.0610 1095 THR A CB 741 O OG1 . THR A 98 ? 0.0263 0.4144 0.2511 0.0018 0.0146 -0.0615 1095 THR A OG1 742 C CG2 . THR A 98 ? 0.0258 0.3982 0.2345 0.0132 -0.0056 -0.0665 1095 THR A CG2 743 N N . ALA A 99 ? 0.0256 0.4235 0.2476 0.0027 -0.0082 -0.0697 1096 ALA A N 744 C CA . ALA A 99 ? 0.0291 0.4426 0.2515 -0.0109 -0.0172 -0.0640 1096 ALA A CA 745 C C . ALA A 99 ? 0.0282 0.4469 0.2502 0.0076 -0.0184 -0.0577 1096 ALA A C 746 O O . ALA A 99 ? 0.0527 0.4724 0.2529 0.0082 -0.0238 -0.0573 1096 ALA A O 747 C CB . ALA A 99 ? 0.0304 0.4575 0.2691 -0.0263 -0.0252 -0.0538 1096 ALA A CB 748 N N . PHE A 100 ? 0.0263 0.4198 0.2410 0.0102 -0.0136 -0.0635 1097 PHE A N 749 C CA . PHE A 100 ? 0.0373 0.4061 0.2372 0.0285 -0.0093 -0.0586 1097 PHE A CA 750 C C . PHE A 100 ? 0.0355 0.3977 0.2213 0.0425 -0.0159 -0.0538 1097 PHE A C 751 O O . PHE A 100 ? 0.0339 0.4226 0.2195 0.0489 -0.0285 -0.0555 1097 PHE A O 752 C CB . PHE A 100 ? 0.0282 0.4056 0.2450 0.0252 0.0125 -0.0496 1097 PHE A CB 753 C CG . PHE A 100 ? 0.0754 0.4399 0.2657 0.0353 0.0520 -0.0397 1097 PHE A CG 754 C CD1 . PHE A 100 ? 0.1729 0.5062 0.2924 0.0557 0.0819 -0.0269 1097 PHE A CD1 755 C CD2 . PHE A 100 ? 0.0749 0.4666 0.3147 0.0342 0.0988 -0.0120 1097 PHE A CD2 756 C CE1 . PHE A 100 ? 0.2063 0.5296 0.3034 0.0995 0.0948 0.0012 1097 PHE A CE1 757 C CE2 . PHE A 100 ? 0.1692 0.5012 0.3393 0.0763 0.1216 0.0060 1097 PHE A CE2 758 C CZ . PHE A 100 ? 0.2046 0.5249 0.3102 0.0868 0.1429 0.0120 1097 PHE A CZ 759 N N . LEU A 101 ? 0.0366 0.3777 0.2125 0.0610 -0.0186 -0.0461 1098 LEU A N 760 C CA . LEU A 101 ? 0.0388 0.3889 0.2117 0.0666 -0.0217 -0.0368 1098 LEU A CA 761 C C . LEU A 101 ? 0.0416 0.4250 0.2257 0.0768 -0.0241 -0.0388 1098 LEU A C 762 O O . LEU A 101 ? 0.0483 0.4420 0.2318 0.0872 -0.0361 -0.0241 1098 LEU A O 763 C CB . LEU A 101 ? 0.0386 0.3679 0.2081 0.0658 -0.0173 -0.0368 1098 LEU A CB 764 C CG . LEU A 101 ? 0.0307 0.3531 0.1906 0.0422 -0.0021 -0.0192 1098 LEU A CG 765 C CD1 . LEU A 101 ? 0.0340 0.3472 0.2000 0.0513 0.0047 -0.0260 1098 LEU A CD1 766 C CD2 . LEU A 101 ? 0.0280 0.3513 0.2011 0.0287 -0.0052 -0.0154 1098 LEU A CD2 767 N N A SER A 102 ? 0.0405 0.4708 0.2422 0.0741 -0.0313 -0.0425 1099 SER A N 768 N N B SER A 102 ? 0.0408 0.4668 0.2362 0.0754 -0.0305 -0.0447 1099 SER A N 769 C CA A SER A 102 ? 0.0406 0.5148 0.2585 0.0688 -0.0344 -0.0487 1099 SER A CA 770 C CA B SER A 102 ? 0.0405 0.4953 0.2477 0.0749 -0.0315 -0.0520 1099 SER A CA 771 C C A SER A 102 ? 0.0444 0.5152 0.2623 0.0674 -0.0430 -0.0507 1099 SER A C 772 C C B SER A 102 ? 0.0439 0.5119 0.2518 0.0687 -0.0390 -0.0502 1099 SER A C 773 O O A SER A 102 ? 0.0726 0.5141 0.2675 0.0649 -0.0505 -0.0522 1099 SER A O 774 O O B SER A 102 ? 0.0728 0.5145 0.2603 0.0675 -0.0467 -0.0496 1099 SER A O 775 C CB A SER A 102 ? 0.0372 0.5296 0.2680 0.0697 -0.0287 -0.0463 1099 SER A CB 776 C CB B SER A 102 ? 0.0388 0.4992 0.2476 0.0722 -0.0313 -0.0549 1099 SER A CB 777 O OG A SER A 102 ? 0.0592 0.6014 0.2851 0.0658 -0.0274 -0.0493 1099 SER A OG 778 O OG B SER A 102 ? 0.0421 0.4834 0.2599 0.0842 -0.0274 -0.0579 1099 SER A OG 779 N N . LYS A 103 ? 0.0531 0.5223 0.2509 0.0723 -0.0485 -0.0509 1100 LYS A N 780 C CA . LYS A 103 ? 0.0841 0.5457 0.2545 0.0807 -0.0498 -0.0568 1100 LYS A CA 781 C C . LYS A 103 ? 0.0802 0.5483 0.2413 0.0988 -0.0500 -0.0520 1100 LYS A C 782 O O . LYS A 103 ? 0.0986 0.5702 0.2444 0.0851 -0.0542 -0.0480 1100 LYS A O 783 C CB . LYS A 103 ? 0.1087 0.5522 0.2680 0.0781 -0.0546 -0.0693 1100 LYS A CB 784 C CG . LYS A 103 ? 0.1958 0.5946 0.3219 0.0487 -0.0515 -0.0878 1100 LYS A CG 785 C CD . LYS A 103 ? 0.3023 0.6560 0.4255 0.0142 -0.0562 -0.0763 1100 LYS A CD 786 C CE . LYS A 103 ? 0.3616 0.7031 0.4791 -0.0006 -0.0680 -0.0315 1100 LYS A CE 787 N NZ . LYS A 103 ? 0.3847 0.7562 0.5440 -0.0197 -0.0856 -0.0019 1100 LYS A NZ 788 N N . CYS A 104 ? 0.0886 0.5256 0.2337 0.1040 -0.0476 -0.0531 1101 CYS A N 789 C CA . CYS A 104 ? 0.1085 0.4924 0.2257 0.1186 -0.0522 -0.0612 1101 CYS A CA 790 C C . CYS A 104 ? 0.1562 0.5088 0.2211 0.1553 -0.0535 -0.0670 1101 CYS A C 791 O O . CYS A 104 ? 0.1736 0.5278 0.2228 0.1595 -0.0627 -0.0597 1101 CYS A O 792 C CB . CYS A 104 ? 0.0917 0.4841 0.2334 0.1023 -0.0527 -0.0529 1101 CYS A CB 793 S SG . CYS A 104 ? 0.0797 0.4596 0.2484 0.0688 -0.0296 -0.0463 1101 CYS A SG 794 N N . ASP A 105 ? 0.2026 0.5289 0.2231 0.1888 -0.0737 -0.0869 1102 ASP A N 795 C CA . ASP A 105 ? 0.2249 0.5594 0.2372 0.2152 -0.0973 -0.0986 1102 ASP A CA 796 C C . ASP A 105 ? 0.2345 0.5942 0.2590 0.2248 -0.1208 -0.1022 1102 ASP A C 797 O O . ASP A 105 ? 0.2368 0.6140 0.2847 0.2275 -0.1181 -0.0930 1102 ASP A O 798 C CB . ASP A 105 ? 0.2333 0.5493 0.2334 0.2150 -0.0961 -0.0996 1102 ASP A CB 799 C CG . ASP A 105 ? 0.2487 0.5615 0.2345 0.2073 -0.0767 -0.1049 1102 ASP A CG 800 O OD1 . ASP A 105 ? 0.2222 0.5442 0.2459 0.1985 -0.0979 -0.0913 1102 ASP A OD1 801 O OD2 . ASP A 105 ? 0.2347 0.5895 0.2426 0.1985 -0.0780 -0.0860 1102 ASP A OD2 802 N N . GLN A 106 ? 0.2203 0.6248 0.2802 0.2328 -0.1404 -0.1080 1103 GLN A N 803 C CA . GLN A 106 ? 0.2585 0.6657 0.3183 0.2213 -0.1597 -0.1089 1103 GLN A CA 804 C C . GLN A 106 ? 0.2542 0.6998 0.2930 0.2291 -0.1597 -0.1133 1103 GLN A C 805 O O . GLN A 106 ? 0.2711 0.7185 0.3016 0.2372 -0.1497 -0.1052 1103 GLN A O 806 C CB . GLN A 106 ? 0.2495 0.6664 0.3494 0.2099 -0.1718 -0.1080 1103 GLN A CB 807 C CG . GLN A 106 ? 0.3542 0.6674 0.5138 0.1779 -0.2055 -0.0964 1103 GLN A CG 808 C CD . GLN A 106 ? 0.4304 0.6765 0.6772 0.1492 -0.2414 -0.0790 1103 GLN A CD 809 O OE1 . GLN A 106 ? 0.4745 0.6966 0.7164 0.1445 -0.2186 -0.1075 1103 GLN A OE1 810 N NE2 . GLN A 106 ? 0.4343 0.7024 0.7577 0.1535 -0.2460 -0.0661 1103 GLN A NE2 811 N N . ARG A 107 ? 0.2707 0.7092 0.2745 0.2283 -0.1541 -0.0986 1104 ARG A N 812 C CA . ARG A 107 ? 0.2842 0.6987 0.2657 0.2117 -0.1497 -0.0913 1104 ARG A CA 813 C C . ARG A 107 ? 0.3230 0.6638 0.2585 0.2301 -0.1324 -0.0728 1104 ARG A C 814 O O . ARG A 107 ? 0.3296 0.6771 0.2515 0.2292 -0.1358 -0.0781 1104 ARG A O 815 C CB . ARG A 107 ? 0.2766 0.6998 0.2716 0.1923 -0.1483 -0.0935 1104 ARG A CB 816 C CG . ARG A 107 ? 0.2851 0.7415 0.2910 0.1348 -0.1368 -0.0895 1104 ARG A CG 817 C CD . ARG A 107 ? 0.3027 0.7710 0.3115 0.0571 -0.1014 -0.1014 1104 ARG A CD 818 N NE . ARG A 107 ? 0.3671 0.8177 0.3601 0.0175 -0.0719 -0.1289 1104 ARG A NE 819 C CZ . ARG A 107 ? 0.4282 0.8467 0.3790 0.0076 -0.0640 -0.1465 1104 ARG A CZ 820 N NH1 . ARG A 107 ? 0.4557 0.8827 0.4018 -0.0370 -0.0732 -0.1489 1104 ARG A NH1 821 N NH2 . ARG A 107 ? 0.4785 0.8564 0.3907 0.0421 -0.0555 -0.1500 1104 ARG A NH2 822 N N . ASN A 108 ? 0.3452 0.6291 0.2495 0.2431 -0.1145 -0.0430 1105 ASN A N 823 C CA . ASN A 108 ? 0.3761 0.6147 0.2467 0.2441 -0.0957 -0.0124 1105 ASN A CA 824 C C . ASN A 108 ? 0.3508 0.5867 0.2275 0.2090 -0.0850 -0.0216 1105 ASN A C 825 O O . ASN A 108 ? 0.3689 0.5964 0.2238 0.2061 -0.0877 -0.0185 1105 ASN A O 826 C CB . ASN A 108 ? 0.4065 0.6438 0.2502 0.2662 -0.0851 -0.0015 1105 ASN A CB 827 C CG . ASN A 108 ? 0.4526 0.6832 0.2662 0.3079 -0.0754 0.0262 1105 ASN A CG 828 O OD1 . ASN A 108 ? 0.4498 0.7368 0.2989 0.3497 -0.0727 0.0252 1105 ASN A OD1 829 N ND2 . ASN A 108 ? 0.4798 0.7368 0.3181 0.3402 -0.0727 0.0270 1105 ASN A ND2 830 N N . GLU A 109 ? 0.2818 0.5422 0.2159 0.1685 -0.0724 -0.0331 1106 GLU A N 831 C CA . GLU A 109 ? 0.2132 0.4949 0.2117 0.1119 -0.0584 -0.0405 1106 GLU A CA 832 C C . GLU A 109 ? 0.2098 0.4539 0.1932 0.0917 -0.0434 -0.0142 1106 GLU A C 833 O O . GLU A 109 ? 0.2035 0.4690 0.1941 0.0820 -0.0320 -0.0131 1106 GLU A O 834 C CB . GLU A 109 ? 0.1870 0.4978 0.2113 0.1014 -0.0592 -0.0480 1106 GLU A CB 835 C CG . GLU A 109 ? 0.1587 0.5440 0.2387 0.0671 -0.0626 -0.0631 1106 GLU A CG 836 C CD . GLU A 109 ? 0.1553 0.5655 0.2714 0.0529 -0.0604 -0.0697 1106 GLU A CD 837 O OE1 . GLU A 109 ? 0.1448 0.5619 0.2827 0.0590 -0.0627 -0.0737 1106 GLU A OE1 838 O OE2 . GLU A 109 ? 0.1605 0.5989 0.2851 0.0518 -0.0898 -0.0688 1106 GLU A OE2 839 N N . PRO A 110 ? 0.2125 0.4347 0.1958 0.0856 -0.0335 0.0135 1107 PRO A N 840 C CA . PRO A 110 ? 0.2046 0.4034 0.1823 0.0790 -0.0241 0.0164 1107 PRO A CA 841 C C . PRO A 110 ? 0.1676 0.3837 0.1676 0.0772 -0.0135 -0.0035 1107 PRO A C 842 O O . PRO A 110 ? 0.1711 0.3774 0.1726 0.0697 -0.0098 -0.0118 1107 PRO A O 843 C CB . PRO A 110 ? 0.1982 0.4169 0.2011 0.0825 -0.0164 0.0218 1107 PRO A CB 844 C CG . PRO A 110 ? 0.2441 0.4489 0.2055 0.0790 -0.0241 0.0421 1107 PRO A CG 845 C CD . PRO A 110 ? 0.2275 0.4462 0.2002 0.0850 -0.0388 0.0294 1107 PRO A CD 846 N N . VAL A 111 ? 0.1472 0.3555 0.1597 0.0631 -0.0131 -0.0054 1108 VAL A N 847 C CA . VAL A 111 ? 0.1118 0.3388 0.1664 0.0540 -0.0093 -0.0120 1108 VAL A CA 848 C C . VAL A 111 ? 0.1080 0.3197 0.1544 0.0469 0.0020 -0.0131 1108 VAL A C 849 O O . VAL A 111 ? 0.1286 0.3262 0.1693 0.0498 0.0019 -0.0137 1108 VAL A O 850 C CB . VAL A 111 ? 0.1023 0.3294 0.1737 0.0504 -0.0024 -0.0120 1108 VAL A CB 851 C CG1 . VAL A 111 ? 0.0885 0.3932 0.1860 0.0678 -0.0049 -0.0285 1108 VAL A CG1 852 C CG2 . VAL A 111 ? 0.0865 0.3488 0.1921 0.0386 -0.0215 -0.0054 1108 VAL A CG2 853 N N . LEU A 112 ? 0.0913 0.3068 0.1763 0.0329 0.0057 -0.0073 1109 LEU A N 854 C CA . LEU A 112 ? 0.0925 0.2912 0.1536 0.0164 0.0230 -0.0115 1109 LEU A CA 855 C C . LEU A 112 ? 0.0733 0.2822 0.1536 0.0146 0.0285 -0.0115 1109 LEU A C 856 O O . LEU A 112 ? 0.0753 0.2739 0.1841 0.0120 0.0307 -0.0137 1109 LEU A O 857 C CB . LEU A 112 ? 0.0979 0.2930 0.1835 0.0015 0.0274 -0.0087 1109 LEU A CB 858 C CG . LEU A 112 ? 0.0957 0.3169 0.1902 -0.0017 0.0383 -0.0283 1109 LEU A CG 859 C CD1 . LEU A 112 ? 0.1482 0.3235 0.1905 -0.0074 0.0331 -0.0203 1109 LEU A CD1 860 C CD2 . LEU A 112 ? 0.0913 0.3425 0.2117 -0.0006 0.0522 -0.0208 1109 LEU A CD2 861 N N . VAL A 113 ? 0.0509 0.2973 0.1430 0.0148 0.0252 -0.0059 1110 VAL A N 862 C CA . VAL A 113 ? 0.0287 0.3142 0.1528 0.0171 0.0172 -0.0028 1110 VAL A CA 863 C C . VAL A 113 ? 0.0299 0.2739 0.1632 0.0161 0.0217 -0.0083 1110 VAL A C 864 O O . VAL A 113 ? 0.0289 0.2759 0.2004 0.0153 0.0199 -0.0170 1110 VAL A O 865 C CB . VAL A 113 ? 0.0293 0.3415 0.1439 0.0225 0.0164 -0.0024 1110 VAL A CB 866 C CG1 . VAL A 113 ? 0.0282 0.3614 0.1585 0.0031 0.0195 0.0153 1110 VAL A CG1 867 C CG2 . VAL A 113 ? 0.0255 0.3621 0.1932 0.0089 0.0008 0.0059 1110 VAL A CG2 868 N N . HIS A 114 ? 0.0271 0.2716 0.1729 0.0085 0.0142 -0.0086 1111 HIS A N 869 C CA . HIS A 114 ? 0.0282 0.2806 0.1703 -0.0054 0.0200 -0.0015 1111 HIS A CA 870 C C . HIS A 114 ? 0.0299 0.2620 0.1614 0.0040 0.0244 -0.0118 1111 HIS A C 871 O O . HIS A 114 ? 0.0269 0.2635 0.1958 0.0115 0.0128 -0.0039 1111 HIS A O 872 C CB . HIS A 114 ? 0.0337 0.2840 0.1703 -0.0038 0.0346 -0.0074 1111 HIS A CB 873 C CG . HIS A 114 ? 0.0339 0.2903 0.1773 0.0027 0.0357 -0.0124 1111 HIS A CG 874 N ND1 . HIS A 114 ? 0.0390 0.3000 0.1808 -0.0049 0.0460 -0.0054 1111 HIS A ND1 875 C CD2 . HIS A 114 ? 0.0370 0.2930 0.1955 0.0000 0.0439 -0.0304 1111 HIS A CD2 876 C CE1 . HIS A 114 ? 0.0340 0.3199 0.1781 0.0010 0.0359 -0.0175 1111 HIS A CE1 877 N NE2 . HIS A 114 ? 0.0368 0.3055 0.1844 0.0000 0.0425 -0.0185 1111 HIS A NE2 878 N N . SER A 115 ? 0.0256 0.3109 0.1722 -0.0048 0.0065 -0.0130 1112 SER A N 879 C CA . SER A 115 ? 0.0280 0.3373 0.1835 -0.0043 0.0204 -0.0091 1112 SER A CA 880 C C . SER A 115 ? 0.0277 0.3635 0.1968 -0.0118 0.0187 -0.0059 1112 SER A C 881 O O . SER A 115 ? 0.0273 0.4032 0.2021 -0.0166 0.0151 -0.0013 1112 SER A O 882 C CB . SER A 115 ? 0.0255 0.3395 0.1915 -0.0026 0.0051 -0.0050 1112 SER A CB 883 O OG . SER A 115 ? 0.0289 0.3481 0.2020 0.0186 0.0197 -0.0183 1112 SER A OG 884 N N . ALA A 116 ? 0.0302 0.3907 0.2011 -0.0097 0.0286 -0.0238 1113 ALA A N 885 C CA . ALA A 116 ? 0.0294 0.3923 0.2352 -0.0074 0.0291 -0.0335 1113 ALA A CA 886 C C . ALA A 116 ? 0.0286 0.3998 0.2339 -0.0135 0.0252 -0.0368 1113 ALA A C 887 O O . ALA A 116 ? 0.0329 0.4007 0.2363 -0.0092 0.0399 -0.0373 1113 ALA A O 888 C CB . ALA A 116 ? 0.0285 0.4101 0.2363 -0.0108 0.0252 -0.0320 1113 ALA A CB 889 N N . ALA A 117 ? 0.0311 0.3819 0.2247 -0.0209 0.0320 -0.0394 1114 ALA A N 890 C CA . ALA A 117 ? 0.0329 0.3810 0.2300 -0.0305 0.0349 -0.0417 1114 ALA A CA 891 C C . ALA A 117 ? 0.0337 0.3564 0.2187 -0.0384 0.0322 -0.0450 1114 ALA A C 892 O O . ALA A 117 ? 0.0435 0.3540 0.2433 -0.0520 0.0531 -0.0467 1114 ALA A O 893 C CB . ALA A 117 ? 0.0340 0.3804 0.2297 -0.0406 0.0320 -0.0306 1114 ALA A CB 894 N N . GLY A 118 ? 0.0324 0.3355 0.2081 -0.0296 0.0310 -0.0379 1115 GLY A N 895 C CA . GLY A 118 ? 0.0306 0.3379 0.1976 -0.0086 0.0296 -0.0351 1115 GLY A CA 896 C C . GLY A 118 ? 0.0328 0.3025 0.1923 -0.0207 0.0329 -0.0225 1115 GLY A C 897 O O . GLY A 118 ? 0.0447 0.3052 0.2072 -0.0208 0.0348 -0.0160 1115 GLY A O 898 N N . VAL A 119 ? 0.0284 0.3253 0.1800 -0.0161 0.0195 -0.0216 1116 VAL A N 899 C CA . VAL A 119 ? 0.0428 0.3093 0.1861 -0.0250 0.0175 -0.0186 1116 VAL A CA 900 C C . VAL A 119 ? 0.0291 0.2967 0.1860 -0.0049 0.0225 -0.0120 1116 VAL A C 901 O O . VAL A 119 ? 0.0284 0.3055 0.1949 0.0087 0.0217 -0.0023 1116 VAL A O 902 C CB . VAL A 119 ? 0.0320 0.3100 0.1923 -0.0274 0.0175 -0.0270 1116 VAL A CB 903 C CG1 . VAL A 119 ? 0.0397 0.3264 0.1993 -0.0313 0.0285 -0.0307 1116 VAL A CG1 904 C CG2 . VAL A 119 ? 0.0577 0.3537 0.2178 -0.0460 0.0295 -0.0219 1116 VAL A CG2 905 N N . ASN A 120 ? 0.0364 0.2991 0.1676 0.0006 0.0076 0.0003 1117 ASN A N 906 C CA . ASN A 120 ? 0.0263 0.2882 0.1638 0.0162 -0.0006 -0.0106 1117 ASN A CA 907 C C . ASN A 120 ? 0.0259 0.2910 0.1709 0.0120 -0.0020 -0.0227 1117 ASN A C 908 O O . ASN A 120 ? 0.0281 0.2982 0.1721 0.0272 0.0010 -0.0120 1117 ASN A O 909 C CB . ASN A 120 ? 0.0262 0.3089 0.1615 0.0156 -0.0005 -0.0060 1117 ASN A CB 910 C CG . ASN A 120 ? 0.0315 0.3181 0.1817 0.0375 0.0070 -0.0342 1117 ASN A CG 911 O OD1 . ASN A 120 ? 0.0271 0.3364 0.2014 0.0227 0.0023 -0.0254 1117 ASN A OD1 912 N ND2 . ASN A 120 ? 0.0299 0.3840 0.2237 0.0305 -0.0225 -0.0276 1117 ASN A ND2 913 N N . ARG A 121 ? 0.0259 0.2799 0.1632 0.0107 0.0031 -0.0186 1118 ARG A N 914 C CA . ARG A 121 ? 0.0267 0.2594 0.1629 0.0103 0.0109 -0.0038 1118 ARG A CA 915 C C . ARG A 121 ? 0.0273 0.2554 0.1544 0.0098 0.0085 0.0019 1118 ARG A C 916 O O . ARG A 121 ? 0.0260 0.2824 0.1743 0.0056 0.0092 0.0061 1118 ARG A O 917 C CB . ARG A 121 ? 0.0291 0.2671 0.1755 0.0226 0.0152 -0.0049 1118 ARG A CB 918 C CG . ARG A 121 ? 0.0318 0.3057 0.1862 0.0408 0.0094 0.0037 1118 ARG A CG 919 C CD . ARG A 121 ? 0.0335 0.2939 0.2329 0.0230 0.0364 0.0071 1118 ARG A CD 920 N NE . ARG A 121 ? 0.0289 0.3224 0.2047 0.0309 0.0071 0.0010 1118 ARG A NE 921 C CZ . ARG A 121 ? 0.0322 0.3240 0.2222 0.0443 0.0074 0.0125 1118 ARG A CZ 922 N NH1 . ARG A 121 ? 0.0291 0.3323 0.2241 0.0328 -0.0077 0.0000 1118 ARG A NH1 923 N NH2 . ARG A 121 ? 0.0282 0.3528 0.2161 0.0231 0.0151 0.0020 1118 ARG A NH2 924 N N . SER A 122 ? 0.0265 0.2585 0.1499 0.0145 0.0071 0.0125 1119 SER A N 925 C CA . SER A 122 ? 0.0395 0.2560 0.1571 0.0085 0.0219 0.0087 1119 SER A CA 926 C C . SER A 122 ? 0.0267 0.2563 0.1660 0.0131 0.0093 -0.0006 1119 SER A C 927 O O . SER A 122 ? 0.0267 0.2777 0.1676 0.0164 0.0057 -0.0006 1119 SER A O 928 C CB . SER A 122 ? 0.0412 0.2590 0.1659 -0.0020 0.0260 0.0043 1119 SER A CB 929 O OG . SER A 122 ? 0.0342 0.2858 0.2037 -0.0193 0.0366 -0.0038 1119 SER A OG 930 N N . GLY A 123 ? 0.0260 0.2603 0.1626 0.0040 0.0092 -0.0039 1120 GLY A N 931 C CA . GLY A 123 ? 0.0465 0.2442 0.1648 -0.0113 0.0263 0.0052 1120 GLY A CA 932 C C . GLY A 123 ? 0.0276 0.2493 0.1553 -0.0074 0.0163 0.0081 1120 GLY A C 933 O O . GLY A 123 ? 0.0264 0.2655 0.1756 0.0108 0.0099 0.0044 1120 GLY A O 934 N N . ALA A 124 ? 0.0295 0.2474 0.1456 -0.0104 0.0197 0.0164 1121 ALA A N 935 C CA . ALA A 124 ? 0.0274 0.2477 0.1460 -0.0151 0.0103 0.0135 1121 ALA A CA 936 C C . ALA A 124 ? 0.0253 0.2526 0.1604 0.0015 0.0014 -0.0052 1121 ALA A C 937 O O . ALA A 124 ? 0.0287 0.2703 0.1729 0.0276 0.0064 -0.0020 1121 ALA A O 938 C CB . ALA A 124 ? 0.0289 0.2732 0.1476 -0.0008 0.0204 0.0311 1121 ALA A CB 939 N N . MET A 125 ? 0.0260 0.2472 0.1536 0.0121 -0.0040 -0.0153 1122 MET A N 940 C CA . MET A 125 ? 0.0256 0.2486 0.1605 -0.0050 0.0058 -0.0099 1122 MET A CA 941 C C . MET A 125 ? 0.0258 0.2538 0.1668 0.0030 0.0076 -0.0020 1122 MET A C 942 O O . MET A 125 ? 0.0260 0.2964 0.1807 0.0123 0.0041 -0.0117 1122 MET A O 943 C CB . MET A 125 ? 0.0263 0.2612 0.1787 -0.0040 0.0074 -0.0186 1122 MET A CB 944 C CG . MET A 125 ? 0.0273 0.2624 0.2329 -0.0100 0.0182 -0.0093 1122 MET A CG 945 S SD . MET A 125 ? 0.0255 0.3012 0.2654 0.0038 0.0065 0.0095 1122 MET A SD 946 C CE . MET A 125 ? 0.0522 0.3023 0.4065 0.0015 -0.0208 0.0463 1122 MET A CE 947 N N . ILE A 126 ? 0.0273 0.2476 0.1659 0.0164 0.0104 0.0108 1123 ILE A N 948 C CA . ILE A 126 ? 0.0430 0.2486 0.1597 0.0093 0.0142 -0.0013 1123 ILE A CA 949 C C . ILE A 126 ? 0.0265 0.2651 0.1580 0.0145 0.0059 -0.0079 1123 ILE A C 950 O O . ILE A 126 ? 0.0275 0.2794 0.1775 0.0235 0.0000 0.0000 1123 ILE A O 951 C CB . ILE A 126 ? 0.0544 0.2517 0.1800 0.0074 0.0263 0.0093 1123 ILE A CB 952 C CG1 . ILE A 126 ? 0.0934 0.3079 0.1738 0.0175 0.0240 -0.0034 1123 ILE A CG1 953 C CG2 . ILE A 126 ? 0.0780 0.2592 0.2090 0.0192 0.0263 0.0131 1123 ILE A CG2 954 C CD1 . ILE A 126 ? 0.1001 0.3212 0.1831 0.0372 0.0006 0.0172 1123 ILE A CD1 955 N N . LEU A 127 ? 0.0273 0.2707 0.1521 0.0201 0.0048 -0.0174 1124 LEU A N 956 C CA . LEU A 127 ? 0.0412 0.2666 0.1553 0.0130 0.0043 -0.0151 1124 LEU A CA 957 C C . LEU A 127 ? 0.0276 0.2547 0.1738 0.0227 0.0018 -0.0097 1124 LEU A C 958 O O . LEU A 127 ? 0.0348 0.2790 0.1911 0.0461 0.0115 -0.0087 1124 LEU A O 959 C CB . LEU A 127 ? 0.0260 0.2725 0.1468 0.0134 -0.0005 -0.0158 1124 LEU A CB 960 C CG . LEU A 127 ? 0.0579 0.3508 0.1676 0.0562 -0.0186 -0.0322 1124 LEU A CG 961 C CD1 . LEU A 127 ? 0.1288 0.3528 0.2240 0.0612 -0.0230 -0.0216 1124 LEU A CD1 962 C CD2 . LEU A 127 ? 0.0265 0.3607 0.1580 0.0196 -0.0057 -0.0434 1124 LEU A CD2 963 N N . ALA A 128 ? 0.0260 0.2514 0.1800 0.0123 0.0008 -0.0065 1125 ALA A N 964 C CA . ALA A 128 ? 0.0256 0.2657 0.1710 0.0093 0.0003 0.0020 1125 ALA A CA 965 C C . ALA A 128 ? 0.0276 0.2946 0.1659 0.0247 -0.0005 -0.0007 1125 ALA A C 966 O O . ALA A 128 ? 0.0311 0.3140 0.1957 0.0388 0.0091 -0.0027 1125 ALA A O 967 C CB . ALA A 128 ? 0.0254 0.2576 0.1982 0.0043 -0.0021 -0.0038 1125 ALA A CB 968 N N . TYR A 129 ? 0.0311 0.3084 0.1532 0.0401 -0.0006 0.0107 1126 TYR A N 969 C CA . TYR A 129 ? 0.0434 0.3215 0.1615 0.0553 -0.0005 0.0000 1126 TYR A CA 970 C C . TYR A 129 ? 0.0434 0.3305 0.1852 0.0636 -0.0031 -0.0137 1126 TYR A C 971 O O . TYR A 129 ? 0.0408 0.3718 0.2011 0.0727 -0.0119 -0.0304 1126 TYR A O 972 C CB . TYR A 129 ? 0.0663 0.3395 0.1492 0.0697 0.0006 0.0046 1126 TYR A CB 973 C CG . TYR A 129 ? 0.0692 0.3339 0.1640 0.0916 -0.0197 0.0019 1126 TYR A CG 974 C CD1 . TYR A 129 ? 0.0944 0.3734 0.1914 0.0856 -0.0362 -0.0186 1126 TYR A CD1 975 C CD2 . TYR A 129 ? 0.0974 0.3501 0.1685 0.1115 -0.0109 0.0120 1126 TYR A CD2 976 C CE1 . TYR A 129 ? 0.1316 0.4007 0.1650 0.1067 -0.0394 -0.0082 1126 TYR A CE1 977 C CE2 . TYR A 129 ? 0.1360 0.3783 0.1782 0.1120 -0.0115 0.0115 1126 TYR A CE2 978 C CZ . TYR A 129 ? 0.1421 0.4011 0.1692 0.1111 -0.0292 -0.0142 1126 TYR A CZ 979 O OH . TYR A 129 ? 0.1624 0.4874 0.1967 0.1216 -0.0337 0.0006 1126 TYR A OH 980 N N . LEU A 130 ? 0.0419 0.3224 0.1844 0.0701 -0.0041 -0.0129 1127 LEU A N 981 C CA . LEU A 130 ? 0.0832 0.3185 0.2020 0.0706 0.0031 -0.0093 1127 LEU A CA 982 C C . LEU A 130 ? 0.0518 0.3046 0.2073 0.0744 -0.0048 -0.0153 1127 LEU A C 983 O O . LEU A 130 ? 0.0553 0.3287 0.2354 0.0922 -0.0219 -0.0074 1127 LEU A O 984 C CB . LEU A 130 ? 0.0848 0.3192 0.2152 0.0700 0.0091 -0.0034 1127 LEU A CB 985 C CG . LEU A 130 ? 0.1324 0.3650 0.2317 0.0731 0.0348 0.0098 1127 LEU A CG 986 C CD1 . LEU A 130 ? 0.1659 0.3670 0.3041 0.0627 0.0553 0.0006 1127 LEU A CD1 987 C CD2 . LEU A 130 ? 0.1993 0.4192 0.2657 0.0832 0.0485 0.0390 1127 LEU A CD2 988 N N . MET A 131 ? 0.0394 0.3255 0.2000 0.0649 -0.0046 -0.0227 1128 MET A N 989 C CA . MET A 131 ? 0.0497 0.3300 0.2029 0.0465 -0.0049 -0.0373 1128 MET A CA 990 C C . MET A 131 ? 0.0342 0.3418 0.2140 0.0527 -0.0051 -0.0516 1128 MET A C 991 O O . MET A 131 ? 0.0390 0.3842 0.2280 0.0684 -0.0026 -0.0684 1128 MET A O 992 C CB . MET A 131 ? 0.0311 0.3258 0.2020 0.0417 -0.0035 -0.0285 1128 MET A CB 993 C CG . MET A 131 ? 0.0260 0.3425 0.2140 0.0116 -0.0077 -0.0254 1128 MET A CG 994 S SD . MET A 131 ? 0.0304 0.3413 0.2286 0.0263 0.0043 -0.0215 1128 MET A SD 995 C CE . MET A 131 ? 0.0399 0.3573 0.2682 0.0148 0.0274 -0.0162 1128 MET A CE 996 N N . SER A 132 ? 0.0348 0.3594 0.2231 0.0555 -0.0164 -0.0658 1129 SER A N 997 C CA . SER A 132 ? 0.0456 0.3968 0.2430 0.0604 -0.0285 -0.0797 1129 SER A CA 998 C C . SER A 132 ? 0.0427 0.4280 0.2587 0.0798 -0.0324 -0.0744 1129 SER A C 999 O O . SER A 132 ? 0.0375 0.4781 0.3048 0.0666 -0.0366 -0.0794 1129 SER A O 1000 C CB . SER A 132 ? 0.0359 0.3925 0.2428 0.0563 -0.0326 -0.0864 1129 SER A CB 1001 O OG . SER A 132 ? 0.0353 0.4695 0.2567 0.0656 -0.0195 -0.0807 1129 SER A OG 1002 N N . LYS A 133 ? 0.0568 0.4514 0.2592 0.1110 -0.0395 -0.0606 1130 LYS A N 1003 C CA . LYS A 133 ? 0.1168 0.4820 0.2657 0.1421 -0.0386 -0.0640 1130 LYS A CA 1004 C C . LYS A 133 ? 0.0864 0.4760 0.2786 0.1359 -0.0315 -0.0653 1130 LYS A C 1005 O O . LYS A 133 ? 0.0752 0.4935 0.3007 0.1492 -0.0414 -0.0557 1130 LYS A O 1006 C CB . LYS A 133 ? 0.1544 0.5095 0.2495 0.1544 -0.0361 -0.0568 1130 LYS A CB 1007 C CG . LYS A 133 ? 0.2416 0.6050 0.2836 0.2002 -0.0487 -0.0913 1130 LYS A CG 1008 C CD . LYS A 133 ? 0.3700 0.7458 0.3291 0.2257 -0.0631 -0.1482 1130 LYS A CD 1009 C CE . LYS A 133 ? 0.4099 0.7746 0.3851 0.2404 -0.0608 -0.1826 1130 LYS A CE 1010 N NZ . LYS A 133 ? 0.4663 0.7846 0.4284 0.2345 -0.0326 -0.2016 1130 LYS A NZ 1011 N N . ASN A 134 ? 0.0640 0.4726 0.2827 0.1315 -0.0229 -0.0750 1131 ASN A N 1012 C CA . ASN A 134 ? 0.0661 0.4650 0.2811 0.1132 -0.0153 -0.0719 1131 ASN A CA 1013 C C . ASN A 134 ? 0.0601 0.4508 0.2813 0.1115 -0.0274 -0.0590 1131 ASN A C 1014 O O . ASN A 134 ? 0.0562 0.4591 0.2976 0.1055 -0.0472 -0.0403 1131 ASN A O 1015 C CB . ASN A 134 ? 0.0544 0.4627 0.2775 0.1111 -0.0054 -0.0762 1131 ASN A CB 1016 C CG . ASN A 134 ? 0.0493 0.4318 0.2953 0.0955 0.0025 -0.0736 1131 ASN A CG 1017 O OD1 . ASN A 134 ? 0.1129 0.4140 0.3409 0.0715 0.0038 -0.0825 1131 ASN A OD1 1018 N ND2 . ASN A 134 ? 0.0368 0.4672 0.2899 0.0649 0.0120 -0.0671 1131 ASN A ND2 1019 N N . LYS A 135 ? 0.0500 0.4329 0.2910 0.0983 -0.0272 -0.0483 1132 LYS A N 1020 C CA . LYS A 135 ? 0.0527 0.4286 0.3163 0.0908 -0.0274 -0.0604 1132 LYS A CA 1021 C C . LYS A 135 ? 0.0518 0.4158 0.3034 0.1000 -0.0262 -0.0439 1132 LYS A C 1022 O O . LYS A 135 ? 0.0848 0.4350 0.3276 0.0974 -0.0019 -0.0377 1132 LYS A O 1023 C CB . LYS A 135 ? 0.0706 0.4370 0.3321 0.0832 -0.0322 -0.0662 1132 LYS A CB 1024 C CG . LYS A 135 ? 0.1412 0.4798 0.3953 0.0498 -0.0450 -0.1212 1132 LYS A CG 1025 C CD . LYS A 135 ? 0.2791 0.5482 0.4809 0.0153 -0.0441 -0.1534 1132 LYS A CD 1026 C CE . LYS A 135 ? 0.3495 0.5881 0.5310 0.0023 -0.0208 -0.1586 1132 LYS A CE 1027 N NZ . LYS A 135 ? 0.3948 0.6168 0.5598 0.0031 -0.0052 -0.1430 1132 LYS A NZ 1028 N N . GLU A 136 ? 0.0743 0.4214 0.3025 0.1067 -0.0337 -0.0571 1133 GLU A N 1029 C CA . GLU A 136 ? 0.0864 0.4280 0.3043 0.1180 -0.0505 -0.0627 1133 GLU A CA 1030 C C . GLU A 136 ? 0.0719 0.4311 0.3018 0.1312 -0.0456 -0.0675 1133 GLU A C 1031 O O . GLU A 136 ? 0.0898 0.4487 0.3219 0.1303 -0.0373 -0.0768 1133 GLU A O 1032 C CB . GLU A 136 ? 0.1112 0.4435 0.3030 0.1221 -0.0493 -0.0549 1133 GLU A CB 1033 C CG . GLU A 136 ? 0.0903 0.4758 0.3156 0.1348 -0.0603 -0.0640 1133 GLU A CG 1034 C CD . GLU A 136 ? 0.0798 0.5120 0.3027 0.1316 -0.0230 -0.0913 1133 GLU A CD 1035 O OE1 . GLU A 136 ? 0.1225 0.5303 0.3643 0.1588 -0.0542 -0.0970 1133 GLU A OE1 1036 O OE2 . GLU A 136 ? 0.0439 0.4586 0.3452 0.0831 -0.0393 -0.0568 1133 GLU A OE2 1037 N N . SER A 137 ? 0.0588 0.4257 0.3077 0.1054 -0.0390 -0.0688 1134 SER A N 1038 C CA . SER A 137 ? 0.0621 0.4508 0.3000 0.0864 -0.0164 -0.0630 1134 SER A CA 1039 C C . SER A 137 ? 0.0427 0.4494 0.2881 0.0841 -0.0010 -0.0709 1134 SER A C 1040 O O . SER A 137 ? 0.0428 0.4582 0.2779 0.0858 -0.0028 -0.0696 1134 SER A O 1041 C CB . SER A 137 ? 0.0688 0.4539 0.3021 0.0702 -0.0204 -0.0535 1134 SER A CB 1042 O OG . SER A 137 ? 0.1191 0.5216 0.3497 0.0640 -0.0087 -0.0197 1134 SER A OG 1043 N N . LEU A 138 ? 0.0456 0.4519 0.2915 0.0784 0.0049 -0.0749 1135 LEU A N 1044 C CA . LEU A 138 ? 0.0456 0.4503 0.2842 0.0680 0.0219 -0.0719 1135 LEU A CA 1045 C C . LEU A 138 ? 0.0306 0.4106 0.2730 0.0386 0.0135 -0.0487 1135 LEU A C 1046 O O . LEU A 138 ? 0.0480 0.3937 0.2721 0.0274 0.0108 -0.0361 1135 LEU A O 1047 C CB . LEU A 138 ? 0.0776 0.4798 0.3025 0.0658 0.0193 -0.0872 1135 LEU A CB 1048 C CG . LEU A 138 ? 0.1298 0.5403 0.3607 0.0702 0.0384 -0.1230 1135 LEU A CG 1049 C CD1 . LEU A 138 ? 0.1949 0.5752 0.3837 0.0803 0.0293 -0.1419 1135 LEU A CD1 1050 C CD2 . LEU A 138 ? 0.1527 0.6165 0.4208 0.0496 0.0397 -0.1474 1135 LEU A CD2 1051 N N . PRO A 139 ? 0.0285 0.3935 0.2614 0.0217 0.0189 -0.0310 1136 PRO A N 1052 C CA . PRO A 139 ? 0.0264 0.3844 0.2597 0.0180 0.0057 -0.0245 1136 PRO A CA 1053 C C . PRO A 139 ? 0.0284 0.3896 0.2441 0.0098 0.0000 -0.0164 1136 PRO A C 1054 O O . PRO A 139 ? 0.0264 0.3727 0.2545 0.0161 0.0080 -0.0208 1136 PRO A O 1055 C CB . PRO A 139 ? 0.0259 0.3856 0.2766 0.0136 -0.0041 -0.0186 1136 PRO A CB 1056 C CG . PRO A 139 ? 0.0260 0.3932 0.2906 0.0000 0.0138 -0.0170 1136 PRO A CG 1057 C CD . PRO A 139 ? 0.0276 0.4029 0.2781 0.0090 0.0220 -0.0331 1136 PRO A CD 1058 N N . MET A 140 ? 0.0331 0.4077 0.2395 -0.0015 -0.0043 -0.0170 1137 MET A N 1059 C CA . MET A 140 ? 0.0734 0.4419 0.2381 -0.0142 -0.0057 -0.0153 1137 MET A CA 1060 C C . MET A 140 ? 0.0579 0.4018 0.2509 0.0057 0.0148 -0.0296 1137 MET A C 1061 O O . MET A 140 ? 0.0460 0.3971 0.2712 0.0109 0.0208 -0.0384 1137 MET A O 1062 C CB . MET A 140 ? 0.1307 0.4888 0.2301 -0.0340 -0.0174 -0.0120 1137 MET A CB 1063 C CG . MET A 140 ? 0.2117 0.5799 0.2465 -0.0706 -0.0230 -0.0153 1137 MET A CG 1064 S SD . MET A 140 ? 0.3253 0.5971 0.2554 -0.0856 -0.0107 -0.0315 1137 MET A SD 1065 C CE . MET A 140 ? 0.3634 0.6610 0.2718 -0.0837 -0.0142 -0.0401 1137 MET A CE 1066 N N . LEU A 141 ? 0.0708 0.3822 0.2775 0.0195 0.0225 -0.0359 1138 LEU A N 1067 C CA . LEU A 141 ? 0.0939 0.3625 0.2982 0.0410 0.0357 -0.0467 1138 LEU A CA 1068 C C . LEU A 141 ? 0.0601 0.3395 0.2845 0.0410 0.0271 -0.0364 1138 LEU A C 1069 O O . LEU A 141 ? 0.0697 0.3476 0.2996 0.0263 0.0324 -0.0322 1138 LEU A O 1070 C CB . LEU A 141 ? 0.1254 0.3704 0.3400 0.0540 0.0518 -0.0627 1138 LEU A CB 1071 C CG . LEU A 141 ? 0.2184 0.4079 0.3995 0.0688 0.0925 -0.0860 1138 LEU A CG 1072 C CD1 . LEU A 141 ? 0.2657 0.4307 0.4823 0.0961 0.1347 -0.1080 1138 LEU A CD1 1073 C CD2 . LEU A 141 ? 0.2985 0.4438 0.4449 0.0649 0.0952 -0.1132 1138 LEU A CD2 1074 N N . TYR A 142 ? 0.0627 0.3343 0.2660 0.0471 0.0087 -0.0219 1139 TYR A N 1075 C CA . TYR A 142 ? 0.0557 0.3433 0.2529 0.0557 -0.0063 -0.0065 1139 TYR A CA 1076 C C . TYR A 142 ? 0.0460 0.3233 0.2448 0.0434 -0.0093 0.0000 1139 TYR A C 1077 O O . TYR A 142 ? 0.0571 0.3370 0.2675 0.0386 -0.0038 0.0098 1139 TYR A O 1078 C CB . TYR A 142 ? 0.0719 0.3713 0.2412 0.0584 -0.0152 0.0019 1139 TYR A CB 1079 C CG . TYR A 142 ? 0.0597 0.4065 0.2345 0.0610 -0.0175 0.0109 1139 TYR A CG 1080 C CD1 . TYR A 142 ? 0.0864 0.4352 0.2442 0.0538 -0.0174 0.0322 1139 TYR A CD1 1081 C CD2 . TYR A 142 ? 0.0329 0.4244 0.2406 0.0511 -0.0150 0.0000 1139 TYR A CD2 1082 C CE1 . TYR A 142 ? 0.1747 0.4415 0.2465 0.0531 -0.0219 0.0197 1139 TYR A CE1 1083 C CE2 . TYR A 142 ? 0.0900 0.4345 0.2522 0.0522 -0.0059 -0.0015 1139 TYR A CE2 1084 C CZ . TYR A 142 ? 0.1421 0.4377 0.2407 0.0384 -0.0241 0.0040 1139 TYR A CZ 1085 O OH . TYR A 142 ? 0.2108 0.4634 0.2730 0.0269 -0.0082 0.0043 1139 TYR A OH 1086 N N . PHE A 143 ? 0.0291 0.2996 0.2458 0.0252 -0.0126 0.0031 1140 PHE A N 1087 C CA . PHE A 143 ? 0.0285 0.2739 0.2187 0.0076 -0.0153 0.0010 1140 PHE A CA 1088 C C . PHE A 143 ? 0.0346 0.2750 0.2037 0.0000 -0.0076 -0.0026 1140 PHE A C 1089 O O . PHE A 143 ? 0.0262 0.2949 0.2142 0.0096 0.0098 0.0006 1140 PHE A O 1090 C CB . PHE A 143 ? 0.0269 0.2829 0.2242 0.0027 -0.0173 0.0099 1140 PHE A CB 1091 C CG . PHE A 143 ? 0.0256 0.2838 0.1987 0.0014 -0.0071 -0.0017 1140 PHE A CG 1092 C CD1 . PHE A 143 ? 0.0260 0.2842 0.2071 0.0014 -0.0110 -0.0089 1140 PHE A CD1 1093 C CD2 . PHE A 143 ? 0.0408 0.3165 0.2037 -0.0074 -0.0096 -0.0130 1140 PHE A CD2 1094 C CE1 . PHE A 143 ? 0.0322 0.3106 0.1985 0.0065 0.0082 0.0024 1140 PHE A CE1 1095 C CE2 . PHE A 143 ? 0.0900 0.3041 0.2161 0.0046 -0.0259 -0.0035 1140 PHE A CE2 1096 C CZ . PHE A 143 ? 0.0719 0.2985 0.2117 -0.0027 0.0065 0.0020 1140 PHE A CZ 1097 N N . LEU A 144 ? 0.0460 0.2621 0.2161 -0.0049 -0.0043 -0.0062 1141 LEU A N 1098 C CA . LEU A 144 ? 0.0597 0.2569 0.2425 -0.0060 0.0020 -0.0065 1141 LEU A CA 1099 C C . LEU A 144 ? 0.0577 0.2736 0.2644 0.0000 0.0086 0.0086 1141 LEU A C 1100 O O . LEU A 144 ? 0.0483 0.2858 0.3005 -0.0114 0.0219 0.0005 1141 LEU A O 1101 C CB . LEU A 144 ? 0.0776 0.2648 0.2533 -0.0137 0.0104 -0.0175 1141 LEU A CB 1102 C CG . LEU A 144 ? 0.0912 0.2912 0.2680 0.0109 0.0175 -0.0175 1141 LEU A CG 1103 C CD1 . LEU A 144 ? 0.0926 0.3370 0.2930 0.0035 0.0461 -0.0467 1141 LEU A CD1 1104 C CD2 . LEU A 144 ? 0.0802 0.3179 0.3276 -0.0038 0.0031 -0.0109 1141 LEU A CD2 1105 N N . TYR A 145 ? 0.0716 0.2890 0.2786 0.0225 0.0086 0.0284 1142 TYR A N 1106 C CA . TYR A 145 ? 0.1035 0.3115 0.2921 0.0410 0.0175 0.0397 1142 TYR A CA 1107 C C . TYR A 145 ? 0.1057 0.3037 0.2836 0.0313 0.0164 0.0320 1142 TYR A C 1108 O O . TYR A 145 ? 0.0986 0.3059 0.3188 0.0173 0.0322 0.0296 1142 TYR A O 1109 C CB . TYR A 145 ? 0.1366 0.3431 0.3158 0.0688 0.0186 0.0644 1142 TYR A CB 1110 C CG . TYR A 145 ? 0.2002 0.4178 0.3616 0.1194 0.0450 0.1118 1142 TYR A CG 1111 C CD1 . TYR A 145 ? 0.3003 0.4584 0.4307 0.1439 0.0847 0.1571 1142 TYR A CD1 1112 C CD2 . TYR A 145 ? 0.2973 0.4989 0.3840 0.1606 0.0595 0.1473 1142 TYR A CD2 1113 C CE1 . TYR A 145 ? 0.3901 0.5113 0.4616 0.1500 0.1124 0.1825 1142 TYR A CE1 1114 C CE2 . TYR A 145 ? 0.3828 0.5414 0.4162 0.1694 0.1000 0.1720 1142 TYR A CE2 1115 C CZ . TYR A 145 ? 0.4147 0.5478 0.4505 0.1648 0.1313 0.1869 1142 TYR A CZ 1116 O OH . TYR A 145 ? 0.4623 0.5849 0.4802 0.1756 0.1553 0.1897 1142 TYR A OH 1117 N N . VAL A 146 ? 0.0794 0.3113 0.2800 0.0270 0.0164 0.0120 1143 VAL A N 1118 C CA . VAL A 146 ? 0.0684 0.3359 0.2469 0.0153 0.0071 0.0043 1143 VAL A CA 1119 C C . VAL A 146 ? 0.0522 0.3021 0.2213 0.0006 0.0142 0.0074 1143 VAL A C 1120 O O . VAL A 146 ? 0.0666 0.3086 0.2150 0.0006 0.0185 0.0031 1143 VAL A O 1121 C CB . VAL A 146 ? 0.0689 0.3625 0.2596 0.0193 -0.0031 -0.0173 1143 VAL A CB 1122 C CG1 . VAL A 146 ? 0.0850 0.3935 0.2646 0.0196 0.0017 -0.0252 1143 VAL A CG1 1123 C CG2 . VAL A 146 ? 0.0948 0.4528 0.2813 0.0241 -0.0109 -0.0109 1143 VAL A CG2 1124 N N . TYR A 147 ? 0.0406 0.2845 0.2069 0.0059 0.0091 0.0049 1144 TYR A N 1125 C CA . TYR A 147 ? 0.0479 0.2651 0.2090 -0.0024 0.0148 -0.0074 1144 TYR A CA 1126 C C . TYR A 147 ? 0.0666 0.2624 0.1949 -0.0071 0.0340 -0.0164 1144 TYR A C 1127 O O . TYR A 147 ? 0.0392 0.2879 0.2178 -0.0071 0.0386 -0.0237 1144 TYR A O 1128 C CB . TYR A 147 ? 0.0269 0.2770 0.2060 -0.0001 0.0171 -0.0018 1144 TYR A CB 1129 C CG . TYR A 147 ? 0.0269 0.2969 0.1920 0.0045 0.0156 -0.0174 1144 TYR A CG 1130 C CD1 . TYR A 147 ? 0.0333 0.2944 0.1992 0.0250 0.0082 -0.0129 1144 TYR A CD1 1131 C CD2 . TYR A 147 ? 0.0300 0.3373 0.2201 0.0375 0.0000 -0.0496 1144 TYR A CD2 1132 C CE1 . TYR A 147 ? 0.0593 0.3359 0.1949 0.0450 -0.0068 -0.0241 1144 TYR A CE1 1133 C CE2 . TYR A 147 ? 0.0291 0.3607 0.2258 0.0355 -0.0063 -0.0688 1144 TYR A CE2 1134 C CZ . TYR A 147 ? 0.0405 0.3328 0.1903 0.0296 -0.0093 -0.0335 1144 TYR A CZ 1135 O OH . TYR A 147 ? 0.0304 0.4056 0.2574 0.0362 -0.0241 -0.0564 1144 TYR A OH 1136 N N . HIS A 148 ? 0.0917 0.2502 0.2161 -0.0175 0.0480 -0.0228 1145 HIS A N 1137 C CA . HIS A 148 ? 0.1254 0.2517 0.2389 -0.0184 0.0653 -0.0230 1145 HIS A CA 1138 C C . HIS A 148 ? 0.1316 0.2687 0.2469 -0.0184 0.0772 -0.0151 1145 HIS A C 1139 O O . HIS A 148 ? 0.1360 0.2908 0.2768 -0.0362 0.0913 -0.0219 1145 HIS A O 1140 C CB . HIS A 148 ? 0.1392 0.2560 0.2422 -0.0305 0.0631 -0.0335 1145 HIS A CB 1141 C CG . HIS A 148 ? 0.1509 0.2869 0.2522 -0.0318 0.0489 -0.0377 1145 HIS A CG 1142 N ND1 . HIS A 148 ? 0.1420 0.3217 0.2804 -0.0405 0.0386 -0.0549 1145 HIS A ND1 1143 C CD2 . HIS A 148 ? 0.1576 0.3088 0.2477 -0.0511 0.0355 -0.0296 1145 HIS A CD2 1144 C CE1 . HIS A 148 ? 0.1594 0.3298 0.2718 -0.0390 0.0294 -0.0548 1145 HIS A CE1 1145 N NE2 . HIS A 148 ? 0.1527 0.3402 0.2417 -0.0463 0.0229 -0.0465 1145 HIS A NE2 1146 N N . SER A 149 ? 0.1473 0.2768 0.2504 0.0073 0.0776 -0.0054 1146 SER A N 1147 C CA . SER A 149 ? 0.1615 0.2763 0.2680 0.0296 0.0829 0.0060 1146 SER A CA 1148 C C . SER A 149 ? 0.1532 0.2644 0.2520 0.0102 0.0939 0.0000 1146 SER A C 1149 O O . SER A 149 ? 0.1597 0.2815 0.2694 -0.0048 0.1089 0.0046 1146 SER A O 1150 C CB . SER A 149 ? 0.1835 0.2964 0.2802 0.0428 0.0715 0.0087 1146 SER A CB 1151 O OG . SER A 149 ? 0.1851 0.3357 0.3393 0.0511 0.0478 0.0098 1146 SER A OG 1152 N N . MET A 150 ? 0.1177 0.2612 0.2540 0.0074 0.0763 -0.0164 1147 MET A N 1153 C CA . MET A 150 ? 0.0873 0.2725 0.2513 -0.0026 0.0564 -0.0252 1147 MET A CA 1154 C C . MET A 150 ? 0.0840 0.2933 0.2460 -0.0153 0.0599 -0.0307 1147 MET A C 1155 O O . MET A 150 ? 0.0891 0.3271 0.2542 -0.0197 0.0619 -0.0357 1147 MET A O 1156 C CB . MET A 150 ? 0.0812 0.2716 0.2551 0.0000 0.0447 -0.0237 1147 MET A CB 1157 C CG . MET A 150 ? 0.0969 0.3260 0.2651 0.0104 0.0162 -0.0184 1147 MET A CG 1158 S SD . MET A 150 ? 0.2442 0.4047 0.2655 0.0031 0.0119 -0.0031 1147 MET A SD 1159 C CE . MET A 150 ? 0.1360 0.5788 0.2363 0.0781 0.0357 -0.0293 1147 MET A CE 1160 N N . ARG A 151 ? 0.0867 0.2975 0.2496 -0.0219 0.0568 -0.0390 1148 ARG A N 1161 C CA . ARG A 151 ? 0.1044 0.2978 0.2639 -0.0271 0.0560 -0.0320 1148 ARG A CA 1162 C C . ARG A 151 ? 0.1224 0.2933 0.2833 -0.0443 0.0846 -0.0480 1148 ARG A C 1163 O O . ARG A 151 ? 0.1025 0.3296 0.2998 -0.0489 0.0979 -0.0482 1148 ARG A O 1164 C CB . ARG A 151 ? 0.0943 0.3084 0.2560 -0.0109 0.0516 -0.0322 1148 ARG A CB 1165 C CG . ARG A 151 ? 0.1000 0.3391 0.2894 -0.0098 0.0130 -0.0241 1148 ARG A CG 1166 C CD . ARG A 151 ? 0.1071 0.3731 0.2935 0.0076 -0.0081 -0.0428 1148 ARG A CD 1167 N NE . ARG A 151 ? 0.0991 0.3973 0.3143 -0.0153 -0.0296 -0.0500 1148 ARG A NE 1168 C CZ . ARG A 151 ? 0.1604 0.4138 0.3095 -0.0606 -0.0063 -0.0416 1148 ARG A CZ 1169 N NH1 . ARG A 151 ? 0.1976 0.4135 0.3463 -0.0723 0.0241 -0.0340 1148 ARG A NH1 1170 N NH2 . ARG A 151 ? 0.1000 0.4888 0.2984 -0.0588 -0.0030 -0.0353 1148 ARG A NH2 1171 N N . ASP A 152 ? 0.1756 0.2851 0.3237 -0.0606 0.1049 -0.0568 1149 ASP A N 1172 C CA . ASP A 152 ? 0.2425 0.2930 0.3526 -0.0653 0.1092 -0.0540 1149 ASP A CA 1173 C C . ASP A 152 ? 0.2635 0.3109 0.3436 -0.0656 0.1067 -0.0294 1149 ASP A C 1174 O O . ASP A 152 ? 0.2536 0.3458 0.3494 -0.0696 0.1067 -0.0186 1149 ASP A O 1175 C CB . ASP A 152 ? 0.2660 0.2874 0.3887 -0.0706 0.1119 -0.0627 1149 ASP A CB 1176 C CG . ASP A 152 ? 0.2960 0.3143 0.4433 -0.0702 0.1251 -0.0900 1149 ASP A CG 1177 O OD1 . ASP A 152 ? 0.3576 0.3734 0.4528 -0.0741 0.1392 -0.0806 1149 ASP A OD1 1178 O OD2 . ASP A 152 ? 0.3100 0.3411 0.5353 -0.0675 0.1579 -0.1225 1149 ASP A OD2 1179 N N . LEU A 153 ? 0.2533 0.3172 0.3237 -0.0379 0.1000 -0.0108 1150 LEU A N 1180 C CA . LEU A 153 ? 0.2691 0.3249 0.3197 -0.0170 0.0904 0.0082 1150 LEU A CA 1181 C C . LEU A 153 ? 0.2508 0.3203 0.3289 -0.0142 0.1058 0.0024 1150 LEU A C 1182 O O . LEU A 153 ? 0.2606 0.3486 0.3384 -0.0114 0.1238 0.0208 1150 LEU A O 1183 C CB . LEU A 153 ? 0.2942 0.3321 0.3206 -0.0131 0.0776 0.0015 1150 LEU A CB 1184 C CG . LEU A 153 ? 0.3790 0.3659 0.3212 -0.0087 0.0467 0.0142 1150 LEU A CG 1185 C CD1 . LEU A 153 ? 0.4370 0.3937 0.3267 -0.0034 0.0280 0.0197 1150 LEU A CD1 1186 C CD2 . LEU A 153 ? 0.4359 0.3952 0.3257 -0.0031 -0.0010 0.0204 1150 LEU A CD2 1187 N N . ARG A 154 ? 0.1949 0.3122 0.3118 -0.0208 0.0820 -0.0259 1151 ARG A N 1188 C CA . ARG A 154 ? 0.1641 0.3312 0.3018 -0.0208 0.0684 -0.0571 1151 ARG A CA 1189 C C . ARG A 154 ? 0.1351 0.3504 0.2985 -0.0401 0.0798 -0.0688 1151 ARG A C 1190 O O . ARG A 154 ? 0.1339 0.3968 0.3206 -0.0230 0.0886 -0.0851 1151 ARG A O 1191 C CB . ARG A 154 ? 0.1483 0.3185 0.3291 -0.0195 0.0469 -0.0643 1151 ARG A CB 1192 C CG . ARG A 154 ? 0.1606 0.3576 0.3395 0.0051 0.0324 -0.0714 1151 ARG A CG 1193 C CD . ARG A 154 ? 0.1439 0.3677 0.2876 0.0388 0.0313 -0.0390 1151 ARG A CD 1194 N NE . ARG A 154 ? 0.1050 0.3355 0.2347 0.0208 0.0472 -0.0195 1151 ARG A NE 1195 C CZ . ARG A 154 ? 0.1430 0.2991 0.2460 -0.0208 0.0571 -0.0160 1151 ARG A CZ 1196 N NH1 . ARG A 154 ? 0.2178 0.3244 0.2356 -0.0109 0.0573 -0.0120 1151 ARG A NH1 1197 N NH2 . ARG A 154 ? 0.1008 0.2980 0.2255 -0.0175 0.0573 -0.0329 1151 ARG A NH2 1198 N N . GLY A 155 ? 0.0992 0.3553 0.2818 -0.0498 0.0828 -0.0635 1152 GLY A N 1199 C CA . GLY A 155 ? 0.0894 0.3698 0.2842 -0.0636 0.0675 -0.0568 1152 GLY A CA 1200 C C . GLY A 155 ? 0.0612 0.3625 0.2720 -0.0546 0.0557 -0.0621 1152 GLY A C 1201 O O . GLY A 155 ? 0.0663 0.3984 0.2858 -0.0679 0.0460 -0.0652 1152 GLY A O 1202 N N . ALA A 156 ? 0.0571 0.3684 0.2732 -0.0582 0.0377 -0.0498 1153 ALA A N 1203 C CA . ALA A 156 ? 0.0379 0.3562 0.2603 -0.0445 0.0208 -0.0460 1153 ALA A CA 1204 C C . ALA A 156 ? 0.0439 0.3357 0.2365 -0.0416 0.0164 -0.0430 1153 ALA A C 1205 O O . ALA A 156 ? 0.0693 0.3553 0.2299 -0.0505 0.0262 -0.0390 1153 ALA A O 1206 C CB . ALA A 156 ? 0.0421 0.3844 0.2797 -0.0359 0.0103 -0.0483 1153 ALA A CB 1207 N N . PHE A 157 ? 0.0289 0.3177 0.2236 -0.0315 0.0090 -0.0329 1154 PHE A N 1208 C CA . PHE A 157 ? 0.0267 0.2863 0.2140 -0.0186 0.0044 -0.0205 1154 PHE A CA 1209 C C . PHE A 157 ? 0.0262 0.2828 0.1985 -0.0150 0.0008 -0.0283 1154 PHE A C 1210 O O . PHE A 157 ? 0.0263 0.2974 0.2134 -0.0005 0.0137 -0.0345 1154 PHE A O 1211 C CB . PHE A 157 ? 0.0284 0.2949 0.2122 -0.0153 0.0096 -0.0120 1154 PHE A CB 1212 C CG . PHE A 157 ? 0.0465 0.2587 0.2073 -0.0140 0.0228 -0.0135 1154 PHE A CG 1213 C CD1 . PHE A 157 ? 0.0263 0.2453 0.2113 -0.0136 0.0055 -0.0115 1154 PHE A CD1 1214 C CD2 . PHE A 157 ? 0.0320 0.2714 0.2019 -0.0087 0.0296 -0.0071 1154 PHE A CD2 1215 C CE1 . PHE A 157 ? 0.0518 0.2565 0.2108 0.0019 0.0329 -0.0160 1154 PHE A CE1 1216 C CE2 . PHE A 157 ? 0.0306 0.2648 0.2048 -0.0065 0.0305 -0.0153 1154 PHE A CE2 1217 C CZ . PHE A 157 ? 0.0333 0.2498 0.2159 -0.0001 0.0390 -0.0057 1154 PHE A CZ 1218 N N . VAL A 158 ? 0.0262 0.2851 0.1908 -0.0146 0.0043 -0.0217 1155 VAL A N 1219 C CA . VAL A 158 ? 0.0264 0.3066 0.1862 -0.0170 0.0044 -0.0087 1155 VAL A CA 1220 C C . VAL A 158 ? 0.0359 0.3131 0.1844 -0.0181 0.0131 -0.0186 1155 VAL A C 1221 O O . VAL A 158 ? 0.0259 0.3310 0.2044 -0.0006 0.0103 -0.0190 1155 VAL A O 1222 C CB . VAL A 158 ? 0.0264 0.3177 0.1755 -0.0164 0.0059 0.0017 1155 VAL A CB 1223 C CG1 . VAL A 158 ? 0.0513 0.3300 0.2008 -0.0098 0.0142 0.0163 1155 VAL A CG1 1224 C CG2 . VAL A 158 ? 0.0335 0.3174 0.1844 -0.0131 0.0120 -0.0012 1155 VAL A CG2 1225 N N . GLU A 159 ? 0.0258 0.3321 0.1914 -0.0115 -0.0017 -0.0153 1156 GLU A N 1226 C CA . GLU A 159 ? 0.0265 0.3690 0.1903 -0.0202 0.0000 -0.0258 1156 GLU A CA 1227 C C . GLU A 159 ? 0.0254 0.3779 0.1819 -0.0057 -0.0008 -0.0201 1156 GLU A C 1228 O O . GLU A 159 ? 0.0754 0.3901 0.1938 -0.0093 -0.0074 -0.0195 1156 GLU A O 1229 C CB . GLU A 159 ? 0.0280 0.3822 0.2046 -0.0307 0.0035 -0.0297 1156 GLU A CB 1230 C CG . GLU A 159 ? 0.0472 0.3862 0.2467 -0.0353 0.0017 -0.0346 1156 GLU A CG 1231 C CD . GLU A 159 ? 0.0795 0.4032 0.2772 -0.0439 -0.0120 -0.0526 1156 GLU A CD 1232 O OE1 . GLU A 159 ? 0.0872 0.4598 0.3041 -0.0388 -0.0241 -0.0763 1156 GLU A OE1 1233 O OE2 . GLU A 159 ? 0.0752 0.4041 0.2793 -0.0494 0.0170 -0.0461 1156 GLU A OE2 1234 N N . ASN A 160 ? 0.0254 0.3781 0.1853 0.0045 0.0027 -0.0147 1157 ASN A N 1235 C CA . ASN A 160 ? 0.0263 0.3824 0.1758 0.0118 0.0088 -0.0126 1157 ASN A CA 1236 C C . ASN A 160 ? 0.0295 0.3785 0.1694 0.0175 0.0038 -0.0208 1157 ASN A C 1237 O O . ASN A 160 ? 0.0262 0.4005 0.1717 0.0182 -0.0006 -0.0131 1157 ASN A O 1238 C CB . ASN A 160 ? 0.0326 0.3761 0.1694 0.0297 0.0252 -0.0063 1157 ASN A CB 1239 C CG . ASN A 160 ? 0.0453 0.3785 0.1756 0.0544 0.0203 -0.0017 1157 ASN A CG 1240 O OD1 . ASN A 160 ? 0.1005 0.3878 0.2008 0.0535 0.0537 0.0103 1157 ASN A OD1 1241 N ND2 . ASN A 160 ? 0.0350 0.3813 0.1791 0.0575 0.0052 -0.0136 1157 ASN A ND2 1242 N N . PRO A 161 ? 0.0496 0.4142 0.1622 0.0131 0.0000 -0.0115 1158 PRO A N 1243 C CA . PRO A 161 ? 0.0819 0.4088 0.1650 0.0263 0.0126 -0.0076 1158 PRO A CA 1244 C C . PRO A 161 ? 0.0652 0.3855 0.1703 0.0487 0.0237 0.0115 1158 PRO A C 1245 O O . PRO A 161 ? 0.0427 0.3973 0.1879 0.0588 0.0151 0.0005 1158 PRO A O 1246 C CB . PRO A 161 ? 0.1007 0.4386 0.1676 0.0226 0.0087 -0.0098 1158 PRO A CB 1247 C CG . PRO A 161 ? 0.1106 0.4623 0.1712 0.0104 -0.0153 -0.0197 1158 PRO A CG 1248 C CD . PRO A 161 ? 0.0577 0.4117 0.1676 0.0115 -0.0120 -0.0020 1158 PRO A CD 1249 N N . SER A 162 ? 0.0597 0.3709 0.1684 0.0606 0.0152 0.0230 1159 SER A N 1250 C CA A SER A 162 ? 0.0636 0.3528 0.1720 0.0634 0.0216 0.0364 1159 SER A CA 1251 C CA B SER A 162 ? 0.0575 0.3560 0.1676 0.0593 0.0197 0.0364 1159 SER A CA 1252 C C . SER A 162 ? 0.0544 0.3413 0.1612 0.0621 0.0219 0.0218 1159 SER A C 1253 O O . SER A 162 ? 0.0553 0.3303 0.1790 0.0454 0.0261 0.0197 1159 SER A O 1254 C CB A SER A 162 ? 0.0708 0.3567 0.1886 0.0640 0.0219 0.0452 1159 SER A CB 1255 C CB B SER A 162 ? 0.0597 0.3625 0.1817 0.0586 0.0175 0.0414 1159 SER A CB 1256 O OG A SER A 162 ? 0.0750 0.3621 0.2266 0.0820 0.0342 0.0469 1159 SER A OG 1257 O OG B SER A 162 ? 0.0353 0.3655 0.1932 0.0535 0.0249 0.0593 1159 SER A OG 1258 N N . PHE A 163 ? 0.0500 0.3420 0.1534 0.0540 0.0205 0.0175 1160 PHE A N 1259 C CA . PHE A 163 ? 0.0388 0.3127 0.1465 0.0489 0.0252 0.0030 1160 PHE A CA 1260 C C . PHE A 163 ? 0.0318 0.2976 0.1641 0.0335 0.0171 -0.0060 1160 PHE A C 1261 O O . PHE A 163 ? 0.0287 0.3084 0.1659 0.0290 0.0079 0.0068 1160 PHE A O 1262 C CB . PHE A 163 ? 0.0379 0.3185 0.1492 0.0518 0.0209 0.0046 1160 PHE A CB 1263 C CG . PHE A 163 ? 0.0337 0.3179 0.1634 0.0469 0.0115 0.0080 1160 PHE A CG 1264 C CD1 . PHE A 163 ? 0.0434 0.3183 0.1948 0.0678 0.0226 0.0113 1160 PHE A CD1 1265 C CD2 . PHE A 163 ? 0.0366 0.3476 0.1500 0.0474 0.0006 -0.0052 1160 PHE A CD2 1266 C CE1 . PHE A 163 ? 0.0560 0.3210 0.1879 0.0634 0.0137 0.0196 1160 PHE A CE1 1267 C CE2 . PHE A 163 ? 0.0328 0.3416 0.1489 0.0461 0.0098 0.0034 1160 PHE A CE2 1268 C CZ . PHE A 163 ? 0.0372 0.3517 0.1699 0.0617 0.0092 0.0219 1160 PHE A CZ 1269 N N . LYS A 164 ? 0.0403 0.2752 0.1738 0.0291 0.0313 -0.0076 1161 LYS A N 1270 C CA . LYS A 164 ? 0.0693 0.2594 0.1815 0.0173 0.0403 0.0065 1161 LYS A CA 1271 C C . LYS A 164 ? 0.0579 0.2544 0.1624 0.0241 0.0285 0.0151 1161 LYS A C 1272 O O . LYS A 164 ? 0.0326 0.2689 0.1897 0.0366 0.0186 0.0115 1161 LYS A O 1273 C CB . LYS A 164 ? 0.0805 0.2680 0.1956 0.0024 0.0518 -0.0068 1161 LYS A CB 1274 C CG . LYS A 164 ? 0.1524 0.3095 0.2483 -0.0364 0.0656 -0.0068 1161 LYS A CG 1275 C CD . LYS A 164 ? 0.1753 0.3445 0.3070 -0.0653 0.0575 -0.0296 1161 LYS A CD 1276 C CE . LYS A 164 ? 0.1949 0.3822 0.3716 -0.0759 0.0259 -0.0445 1161 LYS A CE 1277 N NZ . LYS A 164 ? 0.1500 0.3921 0.4246 -0.0820 0.0303 -0.0666 1161 LYS A NZ 1278 N N . ARG A 165 ? 0.0438 0.2599 0.1544 0.0153 0.0226 0.0274 1162 ARG A N 1279 C CA . ARG A 165 ? 0.0710 0.2524 0.1421 0.0052 0.0207 0.0219 1162 ARG A CA 1280 C C . ARG A 165 ? 0.0540 0.2457 0.1536 0.0194 0.0263 0.0024 1162 ARG A C 1281 O O . ARG A 165 ? 0.0340 0.2829 0.1744 0.0252 0.0307 0.0035 1162 ARG A O 1282 C CB . ARG A 165 ? 0.0864 0.2599 0.1427 0.0086 0.0218 0.0320 1162 ARG A CB 1283 C CG . ARG A 165 ? 0.1086 0.2689 0.1553 0.0098 0.0263 0.0438 1162 ARG A CG 1284 C CD . ARG A 165 ? 0.1351 0.2621 0.2117 0.0115 0.0377 0.0480 1162 ARG A CD 1285 N NE . ARG A 165 ? 0.1404 0.2685 0.2301 0.0280 0.0205 0.0342 1162 ARG A NE 1286 C CZ . ARG A 165 ? 0.1023 0.2781 0.2071 0.0041 0.0013 0.0291 1162 ARG A CZ 1287 N NH1 . ARG A 165 ? 0.0864 0.3379 0.2608 -0.0065 -0.0147 0.0527 1162 ARG A NH1 1288 N NH2 . ARG A 165 ? 0.1676 0.3021 0.2008 0.0015 0.0017 0.0164 1162 ARG A NH2 1289 N N . GLN A 166 ? 0.0603 0.2417 0.1659 0.0241 0.0208 -0.0113 1163 GLN A N 1290 C CA . GLN A 166 ? 0.0675 0.2290 0.1712 0.0239 0.0164 -0.0038 1163 GLN A CA 1291 C C . GLN A 166 ? 0.0522 0.2356 0.1879 0.0219 0.0148 0.0046 1163 GLN A C 1292 O O . GLN A 166 ? 0.0439 0.2745 0.2073 -0.0074 0.0205 0.0043 1163 GLN A O 1293 C CB . GLN A 166 ? 0.0665 0.2442 0.1657 0.0284 0.0065 -0.0087 1163 GLN A CB 1294 C CG . GLN A 166 ? 0.0675 0.2596 0.1859 0.0438 0.0126 0.0000 1163 GLN A CG 1295 C CD . GLN A 166 ? 0.0849 0.2714 0.1773 0.0666 -0.0059 -0.0115 1163 GLN A CD 1296 O OE1 . GLN A 166 ? 0.1402 0.2989 0.1967 0.0522 -0.0109 -0.0296 1163 GLN A OE1 1297 N NE2 . GLN A 166 ? 0.0777 0.3260 0.2037 0.0715 0.0092 0.0093 1163 GLN A NE2 1298 N N . ILE A 167 ? 0.0410 0.2381 0.1791 0.0285 0.0173 0.0163 1164 ILE A N 1299 C CA . ILE A 167 ? 0.0439 0.2504 0.1905 0.0351 0.0159 0.0135 1164 ILE A CA 1300 C C . ILE A 167 ? 0.0392 0.2630 0.1946 0.0247 0.0186 -0.0003 1164 ILE A C 1301 O O . ILE A 167 ? 0.0285 0.2966 0.1972 0.0140 0.0211 0.0057 1164 ILE A O 1302 C CB . ILE A 167 ? 0.0497 0.2617 0.1897 0.0417 0.0153 0.0208 1164 ILE A CB 1303 C CG1 . ILE A 167 ? 0.0509 0.3145 0.1870 0.0388 0.0208 0.0087 1164 ILE A CG1 1304 C CG2 . ILE A 167 ? 0.0364 0.2861 0.2256 0.0500 0.0241 0.0397 1164 ILE A CG2 1305 C CD1 . ILE A 167 ? 0.1097 0.3643 0.2046 0.0423 0.0003 -0.0054 1164 ILE A CD1 1306 N N . ILE A 168 ? 0.0340 0.2671 0.1808 0.0093 0.0280 0.0026 1165 ILE A N 1307 C CA . ILE A 168 ? 0.0504 0.2642 0.1870 0.0124 0.0248 0.0057 1165 ILE A CA 1308 C C . ILE A 168 ? 0.0348 0.2669 0.2109 0.0142 0.0403 0.0096 1165 ILE A C 1309 O O . ILE A 168 ? 0.0372 0.3152 0.2152 0.0307 0.0414 0.0115 1165 ILE A O 1310 C CB . ILE A 168 ? 0.0285 0.2795 0.1842 0.0092 0.0212 -0.0008 1165 ILE A CB 1311 C CG1 . ILE A 168 ? 0.0447 0.2829 0.2037 0.0015 0.0087 -0.0104 1165 ILE A CG1 1312 C CG2 . ILE A 168 ? 0.0744 0.3125 0.2016 0.0208 0.0384 -0.0148 1165 ILE A CG2 1313 C CD1 . ILE A 168 ? 0.0362 0.2982 0.2492 0.0140 -0.0194 -0.0295 1165 ILE A CD1 1314 N N . GLU A 169 ? 0.0491 0.2655 0.2194 0.0010 0.0491 0.0230 1166 GLU A N 1315 C CA . GLU A 169 ? 0.0810 0.2894 0.2266 -0.0087 0.0500 0.0136 1166 GLU A CA 1316 C C . GLU A 169 ? 0.0662 0.3142 0.2395 -0.0137 0.0500 -0.0015 1166 GLU A C 1317 O O . GLU A 169 ? 0.0614 0.3833 0.2685 -0.0130 0.0621 -0.0142 1166 GLU A O 1318 C CB . GLU A 169 ? 0.1001 0.2799 0.2474 -0.0197 0.0520 0.0315 1166 GLU A CB 1319 C CG . GLU A 169 ? 0.0891 0.3282 0.2578 0.0093 0.0571 0.0537 1166 GLU A CG 1320 C CD . GLU A 169 ? 0.1676 0.3364 0.3115 0.0164 0.0368 0.0754 1166 GLU A CD 1321 O OE1 . GLU A 169 ? 0.1727 0.3797 0.3524 0.0617 0.0599 0.0653 1166 GLU A OE1 1322 O OE2 . GLU A 169 ? 0.1949 0.3546 0.3531 -0.0074 -0.0086 0.1013 1166 GLU A OE2 1323 N N . LYS A 170 ? 0.0814 0.3194 0.2301 -0.0041 0.0388 -0.0065 1167 LYS A N 1324 C CA . LYS A 170 ? 0.0867 0.3109 0.2433 -0.0102 0.0335 -0.0126 1167 LYS A CA 1325 C C . LYS A 170 ? 0.0541 0.3203 0.2451 -0.0035 0.0333 -0.0104 1167 LYS A C 1326 O O . LYS A 170 ? 0.0357 0.3619 0.2854 -0.0186 0.0322 -0.0104 1167 LYS A O 1327 C CB . LYS A 170 ? 0.1130 0.3212 0.2360 0.0057 0.0285 -0.0228 1167 LYS A CB 1328 C CG . LYS A 170 ? 0.1747 0.3781 0.2675 -0.0219 0.0049 -0.0454 1167 LYS A CG 1329 C CD . LYS A 170 ? 0.2492 0.4359 0.3183 -0.0496 0.0005 -0.0715 1167 LYS A CD 1330 C CE . LYS A 170 ? 0.2416 0.4514 0.3318 -0.0644 0.0000 -0.0886 1167 LYS A CE 1331 N NZ . LYS A 170 ? 0.2734 0.4877 0.3553 -0.0687 0.0241 -0.0841 1167 LYS A NZ 1332 N N . TYR A 171 ? 0.0410 0.3134 0.2460 0.0120 0.0368 -0.0063 1168 TYR A N 1333 C CA . TYR A 171 ? 0.0527 0.3298 0.2353 0.0261 0.0274 -0.0147 1168 TYR A CA 1334 C C . TYR A 171 ? 0.0395 0.3528 0.2283 0.0443 0.0285 -0.0185 1168 TYR A C 1335 O O . TYR A 171 ? 0.0562 0.3860 0.2531 0.0688 0.0065 -0.0307 1168 TYR A O 1336 C CB . TYR A 171 ? 0.0593 0.3296 0.2148 0.0274 0.0274 -0.0120 1168 TYR A CB 1337 C CG . TYR A 171 ? 0.0289 0.3228 0.2299 0.0197 0.0197 -0.0197 1168 TYR A CG 1338 C CD1 . TYR A 171 ? 0.0362 0.3384 0.2361 0.0197 0.0003 -0.0292 1168 TYR A CD1 1339 C CD2 . TYR A 171 ? 0.0311 0.3330 0.2161 0.0241 0.0262 -0.0093 1168 TYR A CD2 1340 C CE1 . TYR A 171 ? 0.0285 0.3362 0.2409 0.0083 0.0243 -0.0289 1168 TYR A CE1 1341 C CE2 . TYR A 171 ? 0.0478 0.3093 0.2152 -0.0102 0.0131 -0.0115 1168 TYR A CE2 1342 C CZ . TYR A 171 ? 0.0262 0.3111 0.2363 0.0087 0.0098 -0.0296 1168 TYR A CZ 1343 O OH . TYR A 171 ? 0.0256 0.3535 0.2659 -0.0052 0.0077 -0.0610 1168 TYR A OH 1344 N N . VAL A 172 ? 0.0342 0.3785 0.2308 0.0328 0.0324 -0.0214 1169 VAL A N 1345 C CA . VAL A 172 ? 0.0645 0.4219 0.2515 0.0537 0.0388 -0.0164 1169 VAL A CA 1346 C C . VAL A 172 ? 0.0804 0.4820 0.2863 0.0494 0.0894 0.0027 1169 VAL A C 1347 O O . VAL A 172 ? 0.0646 0.5317 0.3003 0.0798 0.0850 -0.0031 1169 VAL A O 1348 C CB . VAL A 172 ? 0.0638 0.3844 0.2480 0.0573 0.0194 -0.0263 1169 VAL A CB 1349 C CG1 . VAL A 172 ? 0.0895 0.4162 0.2666 0.0724 0.0031 -0.0410 1169 VAL A CG1 1350 C CG2 . VAL A 172 ? 0.1053 0.3671 0.2623 0.0507 0.0097 -0.0196 1169 VAL A CG2 1351 N N A ILE A 173 ? 0.1238 0.5400 0.3219 0.0381 0.1167 0.0408 1170 ILE A N 1352 N N B ILE A 173 ? 0.1237 0.5400 0.3219 0.0383 0.1167 0.0408 1170 ILE A N 1353 C CA A ILE A 173 ? 0.2319 0.6280 0.3810 -0.0057 0.1448 0.0728 1170 ILE A CA 1354 C CA B ILE A 173 ? 0.2319 0.6280 0.3810 -0.0057 0.1448 0.0728 1170 ILE A CA 1355 C C A ILE A 173 ? 0.2773 0.6977 0.4239 -0.0584 0.1456 0.0697 1170 ILE A C 1356 C C B ILE A 173 ? 0.2773 0.6977 0.4237 -0.0584 0.1456 0.0697 1170 ILE A C 1357 O O A ILE A 173 ? 0.3231 0.7713 0.4578 -0.1010 0.1526 0.0513 1170 ILE A O 1358 O O B ILE A 173 ? 0.3231 0.7713 0.4578 -0.1010 0.1526 0.0515 1170 ILE A O 1359 C CB A ILE A 173 ? 0.2469 0.6171 0.3768 -0.0017 0.1410 0.0929 1170 ILE A CB 1360 C CB B ILE A 173 ? 0.2469 0.6171 0.3767 -0.0017 0.1411 0.0929 1170 ILE A CB 1361 C CG1 A ILE A 173 ? 0.2574 0.6165 0.3826 0.0197 0.1360 0.0820 1170 ILE A CG1 1362 C CG1 B ILE A 173 ? 0.2569 0.6165 0.3826 0.0197 0.1360 0.0820 1170 ILE A CG1 1363 C CG2 A ILE A 173 ? 0.2576 0.6557 0.3806 0.0120 0.1571 0.1014 1170 ILE A CG2 1364 C CG2 B ILE A 173 ? 0.2574 0.6557 0.3806 0.0120 0.1571 0.1014 1170 ILE A CG2 1365 C CD1 A ILE A 173 ? 0.2585 0.6082 0.3849 0.0362 0.1149 0.0807 1170 ILE A CD1 1366 C CD1 B ILE A 173 ? 0.2594 0.6093 0.3903 0.0384 0.1106 0.0807 1170 ILE A CD1 1367 P P . PO4 B . ? 0.0320 0.3075 0.1791 -0.0046 0.0274 -0.0034 1 PO4 A P 1368 O O1 . PO4 B . ? 0.0291 0.2935 0.1905 0.0230 0.0175 0.0060 1 PO4 A O1 1369 O O2 . PO4 B . ? 0.0410 0.3366 0.1905 0.0082 0.0489 -0.0328 1 PO4 A O2 1370 O O3 . PO4 B . ? 0.0384 0.2831 0.1985 -0.0285 0.0412 0.0003 1 PO4 A O3 1371 O O4 . PO4 B . ? 0.0318 0.3348 0.1826 0.0164 0.0285 -0.0164 1 PO4 A O4 1372 C C1 . BME C . ? 0.3370 0.3418 0.3734 0.0013 0.0048 -0.0035 1174 BME A C1 1373 C C2 . BME C . ? 0.3522 0.3774 0.3905 -0.0003 -0.0040 0.0242 1174 BME A C2 1374 O O1 . BME C . ? 0.3704 0.4007 0.3995 -0.0087 -0.0109 -0.0142 1174 BME A O1 1375 S S2 . BME C . ? 0.4505 0.4910 0.4816 -0.0082 0.0000 -0.0065 1174 BME A S2 1376 C C1 . BME D . ? 0.5758 0.5799 0.5636 0.0126 -0.0161 -0.0081 2 BME A C1 1377 C C2 . BME D . ? 0.5881 0.5896 0.5787 0.0115 -0.0184 -0.0015 2 BME A C2 1378 O O1 . BME D . ? 0.5651 0.5741 0.5683 0.0153 -0.0160 -0.0051 2 BME A O1 1379 S S2 . BME D . ? 0.6111 0.6334 0.6211 0.0114 -0.0065 -0.0137 2 BME A S2 1380 O O . HOH E . ? 0.4517 0.4819 0.4643 -0.0043 -0.0119 0.0035 1175 HOH A O 1381 O O . HOH E . ? 0.4528 0.5008 0.4975 0.0006 -0.0131 -0.0013 1176 HOH A O 1382 O O . HOH E . ? 0.4611 0.5008 0.4848 0.0048 -0.0012 -0.0054 1177 HOH A O 1383 O O . HOH E . ? 0.4359 0.4657 0.4496 0.0087 -0.0108 -0.0071 1178 HOH A O 1384 O O . HOH E . ? 0.4884 0.5163 0.4884 -0.0057 0.0043 -0.0035 1179 HOH A O 1385 O O . HOH E . ? 0.4074 0.4754 0.4472 0.0093 -0.0076 -0.0052 1180 HOH A O 1386 O O . HOH E . ? 0.4616 0.4910 0.4896 0.0000 0.0097 0.0020 1181 HOH A O 1387 O O . HOH E . ? 0.4548 0.4898 0.4839 0.0065 -0.0063 -0.0038 1182 HOH A O 1388 O O . HOH E . ? 0.4189 0.4665 0.4507 -0.0085 -0.0043 -0.0010 1183 HOH A O 1389 O O . HOH E . ? 0.4702 0.4970 0.5019 -0.0049 0.0026 0.0049 1184 HOH A O 1390 O O . HOH E . ? 0.5138 0.5174 0.4970 -0.0038 0.0030 0.0054 1185 HOH A O 1391 O O . HOH E . ? 0.4747 0.5076 0.4819 0.0035 0.0013 0.0043 1186 HOH A O 1392 O O . HOH E . ? 0.4665 0.5102 0.4749 0.0000 0.0026 0.0049 1187 HOH A O 1393 O O . HOH E . ? 0.5044 0.5199 0.5044 -0.0063 0.0091 -0.0108 1188 HOH A O 1394 O O . HOH E . ? 0.4855 0.5212 0.4978 -0.0003 -0.0081 -0.0051 1189 HOH A O 1395 O O . HOH E . ? 0.4881 0.4995 0.4934 -0.0006 0.0035 0.0076 1190 HOH A O 1396 O O . HOH E . ? 0.4925 0.5041 0.5112 0.0043 -0.0006 0.0026 1191 HOH A O 1397 O O . HOH E . ? 0.4363 0.4708 0.4763 0.0062 0.0118 -0.0063 1192 HOH A O 1398 O O . HOH E . ? 0.4805 0.4988 0.4934 0.0000 0.0103 -0.0057 1193 HOH A O 1399 O O . HOH E . ? 0.0868 0.3639 0.2813 0.0240 0.0502 -0.0436 1194 HOH A O 1400 O O . HOH E . ? 0.0528 0.4429 0.3165 0.1001 0.0311 -0.0027 1195 HOH A O 1401 O O . HOH E . ? 0.1693 0.3804 0.2343 -0.0412 0.0724 0.0219 1196 HOH A O 1402 O O . HOH E . ? 0.0629 0.3382 0.2074 -0.0109 0.0452 -0.0270 1197 HOH A O 1403 O O . HOH E . ? 0.2754 0.4598 0.3359 0.0282 0.0513 -0.0582 1198 HOH A O 1404 O O . HOH E . ? 0.0518 0.5296 0.3418 0.0710 0.0199 -0.0649 1199 HOH A O 1405 O O . HOH E . ? 0.1924 0.3865 0.2736 -0.0625 0.1136 -0.0275 1200 HOH A O 1406 O O . HOH E . ? 0.1686 0.4356 0.4038 -0.0397 0.1577 0.0247 1201 HOH A O 1407 O O . HOH E . ? 0.0419 0.4641 0.2833 0.0401 0.0027 -0.0489 1202 HOH A O 1408 O O . HOH E . ? 0.2669 0.7250 0.4765 0.1234 0.1553 0.0186 1203 HOH A O 1409 O O . HOH E . ? 0.2881 0.4359 0.3145 -0.0575 0.1071 0.0500 1204 HOH A O 1410 O O . HOH E . ? 0.1492 0.6441 0.4356 0.1080 0.0027 0.1519 1205 HOH A O 1411 O O . HOH E . ? 0.1124 0.4539 0.3375 -0.0763 0.0643 -0.0252 1206 HOH A O 1412 O O . HOH E . ? 0.2477 0.6269 0.3625 0.0731 -0.0304 -0.1823 1207 HOH A O 1413 O O . HOH E . ? 0.1437 0.4928 0.3402 0.0714 -0.0592 -0.0193 1208 HOH A O 1414 O O . HOH E . ? 0.2842 0.4356 0.2933 0.0051 0.0864 0.0281 1209 HOH A O 1415 O O . HOH E . ? 0.0746 0.4198 0.3429 -0.0340 0.0260 0.0052 1210 HOH A O 1416 O O . HOH E . ? 0.0560 0.5223 0.3761 -0.0678 -0.0170 -0.0683 1211 HOH A O 1417 O O . HOH E . ? 0.1291 0.4905 0.3831 -0.0615 0.0165 0.0427 1212 HOH A O 1418 O O . HOH E . ? 0.1165 0.3914 0.3282 -0.0140 0.0696 -0.0505 1213 HOH A O 1419 O O . HOH E . ? 0.1238 0.3544 0.3264 -0.0219 -0.0020 0.0166 1214 HOH A O 1420 O O . HOH E . ? 0.1421 0.4605 0.2666 0.1133 0.0458 0.0559 1215 HOH A O 1421 O O . HOH E . ? 0.0935 0.5533 0.3625 -0.0040 0.0505 -0.0344 1216 HOH A O 1422 O O . HOH E . ? 0.5640 0.5978 0.4138 -0.2344 0.2222 -0.0577 1217 HOH A O 1423 O O . HOH E . ? 0.1351 0.4785 0.3343 -0.0636 0.0714 -0.0339 1218 HOH A O 1424 O O . HOH E . ? 0.1360 0.4176 0.3425 -0.0005 0.0876 -0.0307 1219 HOH A O 1425 O O . HOH E . ? 0.1509 0.7699 0.3849 0.0540 -0.0264 -0.0926 1220 HOH A O 1426 O O . HOH E . ? 0.1942 0.4805 0.4189 -0.0114 0.0868 -0.0416 1221 HOH A O 1427 O O . HOH E . ? 0.3533 0.4629 0.5248 -0.1142 0.1720 -0.0531 1222 HOH A O 1428 O O . HOH E . ? 0.2035 0.5005 0.2865 -0.0410 -0.0076 0.0511 1223 HOH A O 1429 O O . HOH E . ? 0.1967 0.4720 0.3862 -0.0024 0.0120 -0.1525 1224 HOH A O 1430 O O . HOH E . ? 0.5378 0.6923 0.4623 -0.2451 0.1606 0.0518 1225 HOH A O 1431 O O . HOH E . ? 0.3743 0.4695 0.3255 0.1720 -0.0731 0.0098 1226 HOH A O 1432 O O . HOH E . ? 0.1465 0.6190 0.3064 0.0031 0.0474 -0.0524 1227 HOH A O 1433 O O . HOH E . ? 0.3467 0.3964 0.7009 0.0394 0.1523 -0.0443 1228 HOH A O 1434 O O . HOH E . ? 0.5345 0.4232 0.4790 0.0175 0.0000 -0.0049 1229 HOH A O 1435 O O . HOH E . ? 0.1481 0.6054 0.3129 0.0649 -0.0186 -0.0241 1230 HOH A O 1436 O O . HOH E . ? 0.3364 0.6832 0.4935 -0.0564 -0.1598 0.0263 1231 HOH A O 1437 O O . HOH E . ? 0.3170 0.5486 0.4110 0.1524 0.0626 -0.0794 1232 HOH A O 1438 O O . HOH E . ? 0.3050 0.3583 0.3813 -0.0283 0.1280 -0.0351 1233 HOH A O 1439 O O . HOH E . ? 0.2790 0.3777 0.3892 -0.0118 0.1023 -0.0315 1234 HOH A O 1440 O O . HOH E . ? 0.3941 0.5518 0.6847 0.1518 -0.0546 -0.0207 1235 HOH A O 1441 O O . HOH E . ? 0.5166 0.4826 0.4490 0.1955 0.1106 0.0086 1236 HOH A O 1442 O O . HOH E . ? 0.3210 0.3993 0.4593 -0.0803 0.0254 -0.0820 1237 HOH A O 1443 O O . HOH E . ? 0.5938 0.5594 0.5680 0.1976 -0.0696 0.0489 1238 HOH A O 1444 O O . HOH E . ? 0.2754 0.5848 0.5224 -0.0148 0.0680 -0.0068 1239 HOH A O 1445 O O . HOH E . ? 0.2583 0.6649 0.3596 0.0750 0.0401 0.0575 1240 HOH A O 1446 O O . HOH E . ? 0.4447 0.5942 0.4848 -0.0260 0.2064 -0.0511 1241 HOH A O 1447 O O . HOH E . ? 0.2556 0.6337 0.3810 0.0741 -0.0759 -0.0297 1242 HOH A O 1448 O O . HOH E . ? 0.0964 0.7307 0.3206 0.0000 0.0000 -0.1018 1243 HOH A O 1449 O O . HOH E . ? 0.2578 0.5526 0.4942 0.0636 0.1377 0.1439 1244 HOH A O 1450 O O . HOH E . ? 0.2915 0.4713 0.5817 0.0794 0.1314 0.1089 1245 HOH A O 1451 O O . HOH E . ? 0.5708 0.5802 0.6230 0.0175 0.0031 -0.0454 1246 HOH A O 1452 O O . HOH E . ? 0.1676 0.6035 0.4059 0.0159 -0.0621 -0.1243 1247 HOH A O 1453 O O . HOH E . ? 0.2637 0.5684 0.3837 -0.0296 -0.0005 -0.0890 1248 HOH A O 1454 O O . HOH E . ? 0.5422 0.5586 0.6065 0.0353 0.2169 0.1076 1249 HOH A O 1455 O O . HOH E . ? 0.3765 0.6757 0.5866 0.1009 0.0187 -0.1992 1250 HOH A O 1456 O O . HOH E . ? 0.3589 0.6941 0.5281 -0.0850 -0.0294 -0.0076 1251 HOH A O 1457 O O . HOH E . ? 0.1949 0.4954 0.4393 -0.0043 0.0604 0.0992 1252 HOH A O 1458 O O . HOH E . ? 0.5389 0.3567 0.5011 -0.0060 0.0754 0.0996 1253 HOH A O 1459 O O . HOH E . ? 0.2374 0.5138 0.4458 0.0320 -0.0785 0.0537 1254 HOH A O 1460 O O . HOH E . ? 0.4313 0.5249 0.4018 -0.0243 0.1656 0.0438 1255 HOH A O 1461 O O . HOH E . ? 0.3463 0.4887 0.3822 -0.0608 -0.0631 -0.0597 1256 HOH A O 1462 O O . HOH E . ? 0.4440 0.6524 0.4266 0.0644 -0.0974 0.0135 1257 HOH A O 1463 O O . HOH E . ? 0.1482 0.6000 0.4352 0.0381 0.0054 -0.0573 1258 HOH A O 1464 O O . HOH E . ? 0.1203 0.5579 0.5091 -0.0531 0.1272 -0.1142 1259 HOH A O 1465 O O . HOH E . ? 0.6211 0.4956 0.5705 -0.0207 0.0533 0.0364 1260 HOH A O 1466 O O . HOH E . ? 0.5870 0.6710 0.6582 -0.0326 0.0511 0.2029 1261 HOH A O 1467 O O . HOH E . ? 0.6011 0.6503 0.4099 -0.1537 -0.0780 -0.1202 1262 HOH A O 1468 O O . HOH E . ? 0.4794 0.6147 0.5191 -0.2256 0.1379 0.0392 1263 HOH A O 1469 O O . HOH E . ? 0.5065 0.6294 0.6699 0.1596 0.0877 0.2458 1264 HOH A O 1470 O O . HOH E . ? 0.3609 0.5141 0.4801 0.2123 0.0027 0.0886 1265 HOH A O 1471 O O . HOH E . ? 0.5885 0.4978 0.3273 -0.1622 -0.0241 -0.0017 1266 HOH A O 1472 O O . HOH E . ? 0.2585 0.5198 0.4562 0.1193 0.0593 0.0175 1267 HOH A O 1473 O O . HOH E . ? 0.4370 0.6230 0.5511 -0.0719 0.0623 0.1084 1268 HOH A O 1474 O O . HOH E . ? 0.3864 0.4711 0.4715 -0.1391 0.1879 -0.0684 1269 HOH A O 1475 O O . HOH E . ? 0.3368 0.6226 0.4668 -0.0313 -0.0120 0.0860 1270 HOH A O 1476 O O . HOH E . ? 0.3580 0.7092 0.8205 -0.1164 -0.0820 -0.0076 1271 HOH A O 1477 O O . HOH E . ? 0.4827 0.5253 0.4065 -0.0060 -0.0428 -0.0825 1272 HOH A O 1478 O O . HOH E . ? 0.4663 0.4496 0.4083 -0.0737 -0.0630 0.0339 1273 HOH A O 1479 O O . HOH E . ? 0.5396 0.7203 0.5641 -0.0597 0.0988 0.0218 1274 HOH A O 1480 O O . HOH E . ? 0.5824 0.7257 0.4379 0.0882 0.0653 -0.0978 1275 HOH A O 1481 O O . HOH E . ? 0.5004 0.6298 0.4246 -0.1093 0.1569 0.0926 1276 HOH A O 1482 O O . HOH E . ? 0.1977 0.6140 0.7166 0.1225 0.0485 0.0109 1277 HOH A O 1483 O O . HOH E . ? 0.5396 0.5572 0.7008 -0.0549 -0.0851 0.0649 1278 HOH A O 1484 O O . HOH E . ? 0.5098 0.6043 0.4654 0.1254 -0.1243 0.0640 1279 HOH A O 1485 O O . HOH E . ? 0.4277 0.6682 0.4751 0.1127 -0.1203 -0.0035 1280 HOH A O 1486 O O . HOH E . ? 0.3497 0.6348 0.4881 0.2353 -0.1956 -0.1625 1281 HOH A O 1487 O O . HOH E . ? 0.2211 0.6219 0.4996 -0.0417 0.0644 -0.0057 1282 HOH A O 1488 O O . HOH E . ? 0.6593 0.6481 0.5946 -0.0197 0.0584 0.1516 1283 HOH A O 1489 O O . HOH E . ? 0.2099 0.5267 0.3055 0.0098 0.0476 -0.0104 1284 HOH A O 1490 O O . HOH E . ? 0.3655 0.6898 0.4417 -0.2081 -0.1622 -0.0197 1285 HOH A O 1491 O O . HOH E . ? 0.3495 0.5842 0.4442 -0.2064 0.1527 -0.1456 1286 HOH A O 1492 O O . HOH E . ? 0.5677 0.6534 0.3452 -0.1546 0.1659 -0.0115 1287 HOH A O 1493 O O . HOH E . ? 0.6017 0.7469 0.5425 0.0230 0.0208 -0.1032 1288 HOH A O 1494 O O . HOH E . ? 0.5137 0.6545 0.5580 0.1428 0.2861 0.1230 1289 HOH A O 1495 O O . HOH E . ? 0.2152 0.4711 0.3393 -0.0467 0.1105 -0.0416 1290 HOH A O 1496 O O . HOH E . ? 0.5102 0.5167 0.5812 -0.0230 -0.0706 0.1668 1291 HOH A O 1497 O O . HOH E . ? 0.7354 0.7455 0.8248 0.0570 0.0983 -0.1922 1292 HOH A O 1498 O O . HOH E . ? 0.5770 0.6423 0.4399 0.0357 -0.1243 -0.0929 1293 HOH A O 1499 O O . HOH E . ? 0.5508 0.6933 0.4480 0.0271 -0.1333 -0.0943 1294 HOH A O 1500 O O . HOH E . ? 0.3368 0.3943 0.6348 -0.0152 0.1269 -0.0544 1295 HOH A O 1501 O O . HOH E . ? 0.7734 0.8062 0.2870 0.1186 0.0375 -0.0864 1296 HOH A O 1502 O O . HOH E . ? 0.5184 0.6251 0.3944 0.0540 -0.0219 0.0834 1297 HOH A O 1503 O O . HOH E . ? 0.5271 0.5878 0.5144 0.0794 -0.0877 0.0529 1298 HOH A O 1504 O O . HOH E . ? 0.5554 0.5230 0.5195 -0.0405 0.0185 -0.1412 1299 HOH A O 1505 O O . HOH E . ? 0.4688 0.6262 0.5777 0.0891 -0.0516 0.2002 1300 HOH A O 1506 O O . HOH E . ? 0.6125 0.3752 0.3063 -0.0750 -0.0463 -0.0038 1301 HOH A O 1507 O O . HOH E . ? 0.4485 0.7171 0.4451 -0.0147 0.0544 -0.1286 1302 HOH A O 1508 O O . HOH E . ? 0.4582 0.4388 0.7246 -0.0126 -0.1729 0.0575 1303 HOH A O 1509 O O . HOH E . ? 0.3869 0.6359 0.4092 -0.1641 -0.2029 0.2144 1304 HOH A O 1510 O O . HOH E . ? 0.1544 0.5982 0.6557 -0.1035 0.0658 -0.1921 1305 HOH A O 1511 O O . HOH E . ? 0.3176 0.4431 0.4573 0.0175 -0.0560 -0.0485 1306 HOH A O 1512 O O . HOH E . ? 0.7009 0.7149 0.7271 -0.1541 -0.0326 -0.1133 1307 HOH A O 1513 O O . HOH E . ? 0.4559 0.6129 0.7268 -0.1674 0.1155 -0.0456 1308 HOH A O 1514 O O . HOH E . ? 0.5461 0.6496 0.7573 -0.1199 0.0230 -0.0302 1309 HOH A O 1515 O O . HOH E . ? 0.5921 0.5920 0.6144 0.1272 0.0566 0.2125 1310 HOH A O 1516 O O . HOH E . ? 0.6564 0.6593 0.6082 0.0164 -0.0674 0.1571 1311 HOH A O 1517 O O . HOH E . ? 0.3998 0.4007 0.5288 0.0438 0.1745 0.0218 1312 HOH A O 1518 O O . HOH E . ? 0.6575 0.6261 0.6122 0.0794 -0.0020 0.0942 1313 HOH A O 1519 O O . HOH E . ? 0.5059 0.7245 0.3499 0.0891 -0.0340 -0.0017 1314 HOH A O 1520 O O . HOH E . ? 0.2522 0.7950 0.3612 0.1303 -0.0593 0.0445 1315 HOH A O 1521 O O . HOH E . ? 0.3790 0.6065 0.6136 -0.1835 -0.0239 0.0807 1316 HOH A O 1522 O O . HOH E . ? 0.5741 0.7098 0.6312 -0.0575 0.0152 -0.0419 1317 HOH A O 1523 O O . HOH E . ? 0.6984 0.5084 0.4774 0.1164 0.3115 -0.0238 1318 HOH A O 1524 O O . HOH E . ? 0.5497 0.6309 0.4652 -0.0109 0.0271 -0.1684 1319 HOH A O 1525 O O . HOH E . ? 0.4259 0.5989 0.3792 0.0983 0.0553 -0.0626 1320 HOH A O 1526 O O . HOH E . ? 0.4081 0.7077 0.6754 -0.0031 0.0868 -0.2426 1321 HOH A O 1527 O O . HOH E . ? 0.5497 0.5155 0.5368 -0.0882 0.1562 -0.1252 1322 HOH A O 1528 O O . HOH E . ? 0.3222 0.6779 0.4420 -0.1727 -0.0452 0.0285 1323 HOH A O 1529 O O . HOH E . ? 0.3373 0.7026 0.5546 -0.1571 -0.0608 -0.0357 1324 HOH A O 1530 O O . HOH E . ? 0.5726 0.5501 0.6061 0.0000 0.0000 0.0109 1325 HOH A O 1531 O O . HOH E . ? 0.4386 0.7667 0.7710 -0.1391 0.1145 -0.1939 1326 HOH A O 1532 O O . HOH E . ? 0.6915 0.7393 0.7088 -0.0379 0.0762 -0.0259 1327 HOH A O 1533 O O . HOH E . ? 0.6273 0.6355 0.6535 0.1207 0.0854 -0.0328 1328 HOH A O 1534 O O . HOH E . ? 0.4345 0.5062 0.5702 0.0087 0.0785 0.0186 1329 HOH A O 1535 O O . HOH E . ? 0.8190 0.6194 0.4259 0.0882 -0.1544 -0.0518 1330 HOH A O 1536 O O . HOH E . ? 0.5503 0.4744 0.3991 0.0131 0.1473 0.0197 1331 HOH A O 1537 O O . HOH E . ? 0.7426 0.6955 0.5874 -0.1102 -0.0463 -0.2953 1332 HOH A O 1538 O O . HOH E . ? 0.6363 0.6830 0.7293 -0.1430 0.0476 0.1456 1333 HOH A O 1539 O O . HOH E . ? 0.7414 0.6710 0.6675 -0.0430 -0.1111 -0.0630 1334 HOH A O 1540 O O . HOH E . ? 0.3977 0.8475 0.5393 0.1361 0.0172 -0.0188 1335 HOH A O 1541 O O . HOH E . ? 0.2687 0.6219 0.6765 -0.0148 -0.1726 0.0395 1336 HOH A O 1542 O O . HOH E . ? 0.6226 0.7346 0.6205 -0.0421 0.1351 -0.0375 1337 HOH A O 1543 O O . HOH E . ? 0.5112 0.5299 0.6485 0.0263 -0.0339 -0.1480 1338 HOH A O 1544 O O . HOH E . ? 0.4834 0.6219 0.6301 0.0750 -0.1067 0.0943 1339 HOH A O 1545 O O . HOH E . ? 0.6190 0.6108 0.3734 -0.0746 0.1907 -0.0161 1340 HOH A O 1546 O O . HOH E . ? 0.7871 0.6345 0.5399 -0.0649 -0.1896 -0.0434 1341 HOH A O 1547 O O . HOH E . ? 0.3251 0.6438 0.5672 0.0192 0.1765 -0.0040 1342 HOH A O 1548 O O . HOH E . ? 0.5802 0.4713 0.5105 -0.1439 0.1339 -0.0608 1343 HOH A O 1549 O O . HOH E . ? 0.6183 0.5777 0.6344 0.0842 0.0573 0.1995 1344 HOH A O 1550 O O . HOH E . ? 0.3350 0.7210 0.7710 -0.1212 0.1905 -0.0908 1345 HOH A O 1551 O O . HOH E . ? 0.4838 0.5472 0.7145 0.0076 0.0502 0.0661 1346 HOH A O 1552 O O . HOH E . ? 0.6772 0.4679 0.6952 0.0535 0.1576 0.1492 1347 HOH A O 1553 O O . HOH E . ? 0.4120 0.6786 0.6948 0.0939 0.1852 -0.1404 1348 HOH A O 1554 O O . HOH E . ? 0.7684 0.4289 0.6456 -0.0436 0.0706 0.0697 1349 HOH A O 1555 O O . HOH E . ? 0.7591 0.4751 0.4244 -0.0491 0.0361 0.0834 1350 HOH A O 1556 O O . HOH E . ? 0.7020 0.8518 0.6398 -0.1168 -0.0370 0.0197 1351 HOH A O 1557 O O . HOH E . ? 0.7275 0.5296 0.6179 -0.0416 0.1879 -0.0126 1352 HOH A O 1558 O O . HOH E . ? 0.4715 0.5619 0.6887 0.0864 -0.0038 -0.1127 1353 HOH A O 1559 O O . HOH E . ? 0.4356 0.7825 0.5023 -0.0763 -0.1349 -0.0518 1354 HOH A O 1560 O O . HOH E . ? 0.4327 0.5734 0.7048 -0.0232 -0.1560 0.0137 1355 HOH A O 1561 O O . HOH E . ? 0.4930 0.6804 0.4560 0.1123 0.0595 0.0922 1356 HOH A O 1562 O O . HOH E . ? 0.5568 0.7199 0.5149 -0.0634 -0.1133 0.0649 1357 HOH A O 1563 O O . HOH E . ? 0.4945 0.5533 0.4627 -0.0966 -0.0184 -0.0388 1358 HOH A O 1564 O O . HOH E . ? 0.6758 0.4368 0.4729 -0.0272 -0.0516 0.1518 1359 HOH A O 1565 O O . HOH E . ? 0.5676 0.6241 0.5123 -0.0220 0.1023 0.1080 1360 HOH A O 1566 O O . HOH E . ? 0.7056 0.7940 0.6093 0.1162 0.1437 -0.1993 1361 HOH A O 1567 O O . HOH E . ? 0.6473 0.6567 0.5776 0.0741 0.0697 -0.0199 1362 HOH A O 1568 O O . HOH E . ? 0.5536 0.8177 0.7034 -0.3296 -0.0333 0.0939 1363 HOH A O 1569 O O . HOH E . ? 0.6603 0.6413 0.5939 -0.0027 0.0781 0.1263 1364 HOH A O 1570 O O . HOH E . ? 0.3276 0.6516 0.5748 -0.0071 0.0961 -0.0627 1365 HOH A O 1571 O O . HOH E . ? 0.8011 0.6434 0.7753 -0.0684 -0.0996 0.1106 1366 HOH A O 1572 O O . HOH E . ? 0.5249 0.6614 0.5077 0.0496 -0.0017 0.1577 1367 HOH A O 1573 O O . HOH E . ? 0.6796 0.8712 0.7358 0.0590 -0.1194 -0.0417 1368 HOH A O 1574 O O . HOH E . ? 0.3998 0.7680 0.5404 0.0577 0.0331 -0.0017 1369 HOH A O 1575 O O . HOH E . ? 0.3763 0.6294 0.2964 -0.2073 0.0575 0.0599 1370 HOH A O 1576 O O . HOH E . ? 0.1738 0.7616 0.6412 0.0114 -0.0856 -0.0754 1371 HOH A O 1577 O O . HOH E . ? 0.5349 0.5544 0.4505 -0.0636 0.1967 0.0013 1372 HOH A O 1578 O O . HOH E . ? 0.6837 0.5429 0.7318 0.0000 -0.0425 0.0000 1373 HOH A O 1579 O O . HOH E . ? 0.5472 0.6571 0.5716 -0.0644 -0.0204 0.1377 1374 HOH A O 1580 O O . HOH E . ? 0.6158 0.6958 0.5546 -0.1798 -0.1446 0.1541 1375 HOH A O 1581 O O . HOH E . ? 0.5892 0.6740 0.5770 -0.0736 0.0465 -0.0276 1376 HOH A O 1582 O O . HOH E . ? 1.1836 1.1352 1.2243 -0.0054 0.0265 0.0142 1377 HOH A O 1583 O O . HOH E . ? 0.6995 0.8654 0.4023 -0.0759 0.2301 -0.2325 1378 HOH A O 1584 O O . HOH E . ? 0.8676 0.8287 0.8614 -0.0939 0.0375 0.1049 1379 HOH A O 1585 O O . HOH E . ? 0.6394 0.7713 0.5945 0.0450 -0.0803 0.0043 1380 HOH A O 1586 O O . HOH E . ? 0.5281 0.5551 0.6315 0.0366 -0.0126 -0.1084 1381 HOH A O 1587 O O . HOH E . ? 0.4638 0.7372 0.4262 -0.0656 0.1412 -0.0608 1382 HOH A O 1588 O O . HOH E . ? 0.9820 0.8281 0.5023 -0.0220 0.1296 -0.2275 1383 HOH A O 1589 O O . HOH E . ? 0.4887 0.6244 0.5813 -0.1202 -0.1467 -0.0020 1384 HOH A O 1590 O O . HOH E . ? 0.6327 0.5899 0.8507 0.1323 -0.0302 -0.0493 1385 HOH A O 1591 O O . HOH E . ? 0.5655 0.6237 0.6380 0.1746 0.0287 0.0656 1386 HOH A O 1592 O O . HOH E . ? 0.7835 0.8766 0.8640 -0.0544 -0.0478 -0.0859 1387 HOH A O 1593 O O . HOH E . ? 0.9143 0.7710 0.8665 0.1168 0.1146 -0.0388 1388 HOH A O 1594 O O . HOH E . ? 0.4232 0.4778 0.7092 -0.0207 0.2092 -0.0649 1389 HOH A O 1595 O O . HOH E . ? 0.6223 0.6499 0.6819 -0.0375 0.0410 -0.0643 1390 HOH A O 1596 O O . HOH E . ? 0.5544 0.6460 0.6923 0.0684 0.0921 0.0408 1391 HOH A O 1597 O O . HOH E . ? 0.8798 0.7095 0.8496 0.0043 -0.0487 0.2265 1392 HOH A O 1598 O O . HOH E . ? 0.6057 0.5152 0.5712 0.0593 -0.0568 0.0992 1393 HOH A O 1599 O O . HOH E . ? 0.6189 0.7807 0.4693 -0.0052 -0.0772 0.0087 1394 HOH A O 1600 O O . HOH E . ? 0.6399 0.7335 0.4855 0.0627 -0.0151 0.0076 1395 HOH A O 1601 O O . HOH E . ? 0.6255 0.5263 0.6851 -0.1642 0.0104 0.0741 1396 HOH A O 1602 O O . HOH E . ? 0.7382 0.8367 0.7131 -0.0263 -0.0741 -0.0882 1397 HOH A O 1603 O O . HOH E . ? 0.6154 0.7882 0.7056 -0.0724 -0.0658 -0.0428 1398 HOH A O 1604 O O . HOH E . ? 0.6190 0.8651 0.7483 0.2152 -0.0891 0.0074 1399 HOH A O 1605 O O . HOH E . ? 0.9046 1.0204 0.9603 -0.0209 -0.0780 -0.0188 1400 HOH A O 1606 O O . HOH E . ? 0.7738 0.7418 0.8323 -0.0964 0.0034 -0.0333 1401 HOH A O 1607 O O . HOH E . ? 0.8155 0.7508 0.8140 0.0891 0.1211 0.0662 1402 HOH A O 1608 O O . HOH E . ? 0.6668 0.6485 0.8374 -0.0171 -0.0432 -0.0571 1403 HOH A O 1609 O O . HOH E . ? 0.7932 0.8245 0.7070 -0.0432 -0.1429 0.0304 1404 HOH A O 1610 O O . HOH E . ? 0.6341 0.6312 0.6990 0.1668 0.0736 -0.0076 1405 HOH A O 1611 O O . HOH E . ? 0.6894 0.6998 0.7049 0.0604 -0.0982 -0.0878 1406 HOH A O 1612 O O . HOH E . ? 0.7045 0.7103 0.7573 -0.0080 -0.0671 -0.1659 1407 HOH A O 1613 O O . HOH E . ? 0.9570 0.9480 1.0290 0.0671 -0.0662 -0.0003 1408 HOH A O 1614 O O . HOH E . ? 0.7253 0.7947 0.7289 0.1142 -0.0153 -0.0243 1409 HOH A O 1615 O O . HOH E . ? 0.6315 0.7505 0.5235 -0.0886 -0.0043 -0.0230 1410 HOH A O 1616 O O . HOH E . ? 0.6241 0.6215 0.5950 -0.0794 0.0864 -0.0458 1411 HOH A O 1617 O O . HOH E . ? 1.0635 0.9879 1.1390 0.0054 0.0104 -0.0252 1412 HOH A O 1618 O O . HOH E . ? 0.6937 0.8007 0.8689 0.0087 0.0043 0.0772 1413 HOH A O 1619 O O . HOH E . ? 0.7182 0.8019 0.7160 -0.1747 0.0093 -0.0555 1414 HOH A O 1620 O O . HOH E . ? 0.5715 0.7572 0.8399 -0.0017 -0.0218 -0.1421 1415 HOH A O 1621 O O . HOH E . ? 0.6420 0.8137 0.5016 -0.0706 -0.0038 0.0285 1416 HOH A O 1622 O O . HOH E . ? 0.3440 0.6948 0.7458 0.0252 0.0131 0.0137 1417 HOH A O 1623 O O . HOH E . ? 0.7910 0.7153 0.7623 -0.0136 -0.0447 0.0351 1418 HOH A O 1624 O O . HOH E . ? 0.6079 0.6779 0.7831 -0.2309 -0.0436 0.0917 1419 HOH A O 1625 O O . HOH E . ? 0.6237 0.6559 0.7918 0.1404 -0.1150 -0.0886 1420 HOH A O 1626 O O . HOH E . ? 0.4859 0.5497 0.6064 -0.0828 -0.0287 0.1324 1421 HOH A O 1627 O O . HOH E . ? 0.5920 0.6326 0.7311 -0.1861 -0.0793 0.0527 1422 HOH A O 1628 O O . HOH E . ? 0.7505 0.7828 0.7056 0.0775 0.1062 0.0705 1423 HOH A O 1629 O O . HOH E . ? 0.7433 0.7990 0.6909 0.0621 -0.0148 0.0494 1424 HOH A O 1630 O O . HOH E . ? 0.4158 0.6685 0.5048 0.1280 -0.1058 0.0337 1425 HOH A O 1631 O O . HOH E . ? 0.5788 0.4598 0.5270 0.0860 -0.0577 0.0974 1426 HOH A O 1632 O O . HOH E . ? 0.3661 0.4697 0.4995 -0.0649 0.0974 0.0454 1427 HOH A O 1633 O O . HOH E . ? 0.3817 0.6363 0.3941 0.0644 -0.0810 -0.0957 1428 HOH A O 1634 O O . HOH E . ? 0.6140 0.5360 0.4891 -0.0922 -0.1208 0.1023 1429 HOH A O 1635 O O . HOH E . ? 0.8039 0.8222 0.7820 0.0364 0.0109 -0.0604 1430 HOH A O 1636 O O . HOH E . ? 0.6111 0.7386 0.9060 0.0315 -0.0242 0.0198 1431 HOH A O 1637 O O . HOH E . ? 0.7810 0.6158 0.6937 -0.0794 0.0952 -0.0170 1432 HOH A O 1638 O O . HOH E . ? 0.7324 0.9042 0.6822 0.0465 -0.1518 0.0627 1433 HOH A O 1639 O O . HOH E . ? 0.6352 0.6693 0.5223 -0.1711 0.0507 -0.0020 1434 HOH A O 1640 O O . HOH E . ? 0.5766 0.6007 0.7250 0.1638 -0.1162 -0.1026 1435 HOH A O 1641 O O . HOH E . ? 0.5457 0.6424 0.6477 0.0526 -0.1172 -0.0054 1436 HOH A O 1642 O O . HOH E . ? 0.5580 0.7045 0.5188 -0.0697 0.0913 0.0237 1437 HOH A O 1643 O O . HOH E . ? 0.6538 0.6934 0.7516 -0.2205 -0.0710 0.0126 1438 HOH A O 1644 O O . HOH E . ? 0.6796 0.7856 0.6585 -0.0656 0.0000 0.0485 1439 HOH A O 1645 O O . HOH E . ? 0.8658 0.8539 0.7728 0.0207 -0.0065 0.0803 1440 HOH A O 1646 O O . HOH E . ? 0.7044 0.6625 0.6757 0.0296 0.0006 -0.1001 1441 HOH A O 1647 O O . HOH E . ? 0.5895 0.6233 0.7038 -0.1014 0.0882 -0.0368 1442 HOH A O 1648 O O . HOH E . ? 0.7289 0.7275 0.7336 0.0907 0.0346 -0.0194 1443 HOH A O 1649 O O . HOH E . ? 0.6369 0.7983 0.7218 0.1819 -0.0474 -0.0197 1444 HOH A O 1650 O O . HOH E . ? 0.7620 0.6994 0.8927 -0.0010 0.0812 -0.0601 1445 HOH A O 1651 O O . HOH E . ? 0.6011 0.6510 0.6991 -0.0584 -0.0575 0.0781 1446 HOH A O 1652 O O . HOH E . ? 0.5970 0.7713 0.5968 -0.1667 -0.0366 -0.0680 1447 HOH A O 1653 O O . HOH E . ? 0.8420 0.8011 0.8381 -0.0648 0.0408 -0.1136 1448 HOH A O 1654 O O . HOH E . ? 0.7609 0.9398 0.8705 -0.0658 -0.0590 0.0904 1449 HOH A O 1655 O O . HOH E . ? 1.0499 0.9940 0.9695 0.0445 0.0015 -0.0535 1450 HOH A O 1656 O O . HOH E . ? 1.0707 1.0381 1.1576 -0.0900 0.0120 -0.0151 1451 HOH A O 1657 O O . HOH E . ? 0.5795 0.6430 0.7279 -0.0640 -0.0043 0.0297 1452 HOH A O 1658 O O . HOH E . ? 0.7210 0.7900 0.6075 -0.0608 -0.0524 -0.0869 1453 HOH A O 1659 O O . HOH E . ? 0.7153 0.6075 0.8256 -0.0619 -0.0480 0.1360 1454 HOH A O 1660 O O . HOH E . ? 0.9404 0.9150 0.8452 -0.0221 -0.1193 0.0838 1455 HOH A O 1661 O O . HOH E . ? 0.8342 0.7329 0.7644 -0.0487 -0.0403 -0.0204 1456 HOH A O 1662 O O . HOH E . ? 0.9937 0.8751 1.0094 -0.0114 -0.0507 0.0513 1457 HOH A O 1663 O O . HOH E . ? 1.3538 1.2991 1.3171 0.0322 0.0006 0.0983 1458 HOH A O 1664 O O . HOH E . ? 0.7677 0.8284 0.6959 0.0165 0.1093 -0.1123 1459 HOH A O 1665 O O . HOH E . ? 0.7275 0.7249 0.8421 0.0652 -0.0610 0.0183 1460 HOH A O 1666 O O . HOH E . ? 0.6822 0.7846 0.7491 0.0263 -0.1212 -0.1613 1461 HOH A O 1667 O O . HOH E . ? 0.6757 0.9488 0.8051 -0.0070 0.0024 -0.0586 1462 HOH A O 1668 O O . HOH E . ? 0.8816 0.8234 0.8514 -0.0082 0.0414 0.0353 1463 HOH A O 1669 O O . HOH E . ? 0.7070 0.7792 0.8367 0.0412 0.0740 0.0489 1464 HOH A O 1670 O O . HOH E . ? 0.9860 1.1167 1.0865 -0.0329 -0.0217 0.0108 1465 HOH A O 1671 O O . HOH E . ? 0.3853 0.7055 0.6485 0.0109 0.0303 -0.0662 1466 HOH A O 1672 O O . HOH E . ? 0.9243 0.9567 0.9530 -0.0705 0.0715 -0.0671 1467 HOH A O 1673 O O . HOH E . ? 1.4328 1.4364 1.4529 -0.0006 -0.0048 0.1316 1468 HOH A O 1674 O O . HOH E . ? 0.9656 0.9509 0.9329 0.0076 0.0154 -0.0405 1469 HOH A O 1675 O O . HOH E . ? 0.7544 0.7950 0.8119 0.0269 0.0441 0.1207 1470 HOH A O 1676 O O . HOH E . ? 0.8633 0.6883 0.8697 0.0272 -0.0379 -0.0710 1471 HOH A O 1677 O O . HOH E . ? 0.9416 0.9437 0.9862 -0.1133 0.0445 0.0406 1472 HOH A O 1678 O O . HOH E . ? 0.8608 0.7659 0.8482 0.1237 -0.1142 0.0500 1473 HOH A O 1679 O O . HOH E . ? 0.6420 0.8216 0.7286 0.0340 0.0798 0.0856 1474 HOH A O # 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 1 998 ? ? ? A . n A 1 2 PRO 2 999 ? ? ? A . n A 1 3 GLU 3 1000 ? ? ? A . n A 1 4 ILE 4 1001 ? ? ? A . n A 1 5 ARG 5 1002 ? ? ? A . n A 1 6 MET 6 1003 ? ? ? A . n A 1 7 ASP 7 1004 ? ? ? A . n A 1 8 LYS 8 1005 ? ? ? A . n A 1 9 LYS 9 1006 ? ? ? A . n A 1 10 SER 10 1007 1007 SER SER A . n A 1 11 LEU 11 1008 1008 LEU LEU A . n A 1 12 TYR 12 1009 1009 TYR TYR A . n A 1 13 LYS 13 1010 1010 LYS LYS A . n A 1 14 TYR 14 1011 1011 TYR TYR A . n A 1 15 LEU 15 1012 1012 LEU LEU A . n A 1 16 LEU 16 1013 1013 LEU LEU A . n A 1 17 LEU 17 1014 1014 LEU LEU A . n A 1 18 ARG 18 1015 1015 ARG ARG A . n A 1 19 SER 19 1016 1016 SER SER A . n A 1 20 THR 20 1017 1017 THR THR A . n A 1 21 GLY 21 1018 1018 GLY GLY A . n A 1 22 ASP 22 1019 1019 ASP ASP A . n A 1 23 MET 23 1020 1020 MET MET A . n A 1 24 HIS 24 1021 1021 HIS HIS A . n A 1 25 LYS 25 1022 1022 LYS LYS A . n A 1 26 ALA 26 1023 1023 ALA ALA A . n A 1 27 LYS 27 1024 1024 LYS LYS A . n A 1 28 SER 28 1025 1025 SER SER A . n A 1 29 PRO 29 1026 1026 PRO PRO A . n A 1 30 THR 30 1027 1027 THR THR A . n A 1 31 ILE 31 1028 1028 ILE ILE A . n A 1 32 MET 32 1029 1029 MET MET A . n A 1 33 THR 33 1030 1030 THR THR A . n A 1 34 ARG 34 1031 1031 ARG ARG A . n A 1 35 VAL 35 1032 1032 VAL VAL A . n A 1 36 THR 36 1033 1033 THR THR A . n A 1 37 ASN 37 1034 1034 ASN ASN A . n A 1 38 ASN 38 1035 1035 ASN ASN A . n A 1 39 VAL 39 1036 1036 VAL VAL A . n A 1 40 TYR 40 1037 1037 TYR TYR A . n A 1 41 LEU 41 1038 1038 LEU LEU A . n A 1 42 GLY 42 1039 1039 GLY GLY A . n A 1 43 ASN 43 1040 1040 ASN ASN A . n A 1 44 TYR 44 1041 1041 TYR TYR A . n A 1 45 LYS 45 1042 1042 LYS LYS A . n A 1 46 ASN 46 1043 1043 ASN ASN A . n A 1 47 ALA 47 1044 1044 ALA ALA A . n A 1 48 MET 48 1045 1045 MET MET A . n A 1 49 ASP 49 1046 1046 ASP ASP A . n A 1 50 ALA 50 1047 1047 ALA ALA A . n A 1 51 PRO 51 1048 1048 PRO PRO A . n A 1 52 SER 52 1049 1049 SER SER A . n A 1 53 SER 53 1050 1050 SER SER A . n A 1 54 GLU 54 1051 1051 GLU GLU A . n A 1 55 VAL 55 1052 1052 VAL VAL A . n A 1 56 LYS 56 1053 1053 LYS LYS A . n A 1 57 PHE 57 1054 1054 PHE PHE A . n A 1 58 LYS 58 1055 1055 LYS LYS A . n A 1 59 TYR 59 1056 1056 TYR TYR A . n A 1 60 VAL 60 1057 1057 VAL VAL A . n A 1 61 LEU 61 1058 1058 LEU LEU A . n A 1 62 ASN 62 1059 1059 ASN ASN A . n A 1 63 LEU 63 1060 1060 LEU LEU A . n A 1 64 THR 64 1061 1061 THR THR A . n A 1 65 MET 65 1062 1062 MET MET A . n A 1 66 ASP 66 1063 1063 ASP ASP A . n A 1 67 LYS 67 1064 1064 LYS LYS A . n A 1 68 TYR 68 1065 1065 TYR TYR A . n A 1 69 THR 69 1066 1066 THR THR A . n A 1 70 LEU 70 1067 1067 LEU LEU A . n A 1 71 PRO 71 1068 1068 PRO PRO A . n A 1 72 ASN 72 1069 1069 ASN ASN A . n A 1 73 SER 73 1070 1070 SER SER A . n A 1 74 ASN 74 1071 1071 ASN ASN A . n A 1 75 ILE 75 1072 1072 ILE ILE A . n A 1 76 ASN 76 1073 1073 ASN ASN A . n A 1 77 ILE 77 1074 1074 ILE ILE A . n A 1 78 ILE 78 1075 1075 ILE ILE A . n A 1 79 HIS 79 1076 1076 HIS HIS A . n A 1 80 ILE 80 1077 1077 ILE ILE A . n A 1 81 PRO 81 1078 1078 PRO PRO A . n A 1 82 LEU 82 1079 1079 LEU LEU A . n A 1 83 VAL 83 1080 1080 VAL VAL A . n A 1 84 ASP 84 1081 1081 ASP ASP A . n A 1 85 ASP 85 1082 1082 ASP ASP A . n A 1 86 THR 86 1083 1083 THR THR A . n A 1 87 THR 87 1084 1084 THR THR A . n A 1 88 THR 88 1085 1085 THR THR A . n A 1 89 ASP 89 1086 1086 ASP ASP A . n A 1 90 ILE 90 1087 1087 ILE ILE A . n A 1 91 SER 91 1088 1088 SER SER A . n A 1 92 LYS 92 1089 1089 LYS LYS A . n A 1 93 TYR 93 1090 1090 TYR TYR A . n A 1 94 PHE 94 1091 1091 PHE PHE A . n A 1 95 ASP 95 1092 1092 ASP ASP A . n A 1 96 ASP 96 1093 1093 ASP ASP A . n A 1 97 VAL 97 1094 1094 VAL VAL A . n A 1 98 THR 98 1095 1095 THR THR A . n A 1 99 ALA 99 1096 1096 ALA ALA A . n A 1 100 PHE 100 1097 1097 PHE PHE A . n A 1 101 LEU 101 1098 1098 LEU LEU A . n A 1 102 SER 102 1099 1099 SER SER A . n A 1 103 LYS 103 1100 1100 LYS LYS A . n A 1 104 CYS 104 1101 1101 CYS CYS A . n A 1 105 ASP 105 1102 1102 ASP ASP A . n A 1 106 GLN 106 1103 1103 GLN GLN A . n A 1 107 ARG 107 1104 1104 ARG ARG A . n A 1 108 ASN 108 1105 1105 ASN ASN A . n A 1 109 GLU 109 1106 1106 GLU GLU A . n A 1 110 PRO 110 1107 1107 PRO PRO A . n A 1 111 VAL 111 1108 1108 VAL VAL A . n A 1 112 LEU 112 1109 1109 LEU LEU A . n A 1 113 VAL 113 1110 1110 VAL VAL A . n A 1 114 HIS 114 1111 1111 HIS HIS A . n A 1 115 SER 115 1112 1112 SER SER A . n A 1 116 ALA 116 1113 1113 ALA ALA A . n A 1 117 ALA 117 1114 1114 ALA ALA A . n A 1 118 GLY 118 1115 1115 GLY GLY A . n A 1 119 VAL 119 1116 1116 VAL VAL A . n A 1 120 ASN 120 1117 1117 ASN ASN A . n A 1 121 ARG 121 1118 1118 ARG ARG A . n A 1 122 SER 122 1119 1119 SER SER A . n A 1 123 GLY 123 1120 1120 GLY GLY A . n A 1 124 ALA 124 1121 1121 ALA ALA A . n A 1 125 MET 125 1122 1122 MET MET A . n A 1 126 ILE 126 1123 1123 ILE ILE A . n A 1 127 LEU 127 1124 1124 LEU LEU A . n A 1 128 ALA 128 1125 1125 ALA ALA A . n A 1 129 TYR 129 1126 1126 TYR TYR A . n A 1 130 LEU 130 1127 1127 LEU LEU A . n A 1 131 MET 131 1128 1128 MET MET A . n A 1 132 SER 132 1129 1129 SER SER A . n A 1 133 LYS 133 1130 1130 LYS LYS A . n A 1 134 ASN 134 1131 1131 ASN ASN A . n A 1 135 LYS 135 1132 1132 LYS LYS A . n A 1 136 GLU 136 1133 1133 GLU GLU A . n A 1 137 SER 137 1134 1134 SER SER A . n A 1 138 LEU 138 1135 1135 LEU LEU A . n A 1 139 PRO 139 1136 1136 PRO PRO A . n A 1 140 MET 140 1137 1137 MET MET A . n A 1 141 LEU 141 1138 1138 LEU LEU A . n A 1 142 TYR 142 1139 1139 TYR TYR A . n A 1 143 PHE 143 1140 1140 PHE PHE A . n A 1 144 LEU 144 1141 1141 LEU LEU A . n A 1 145 TYR 145 1142 1142 TYR TYR A . n A 1 146 VAL 146 1143 1143 VAL VAL A . n A 1 147 TYR 147 1144 1144 TYR TYR A . n A 1 148 HIS 148 1145 1145 HIS HIS A . n A 1 149 SER 149 1146 1146 SER SER A . n A 1 150 MET 150 1147 1147 MET MET A . n A 1 151 ARG 151 1148 1148 ARG ARG A . n A 1 152 ASP 152 1149 1149 ASP ASP A . n A 1 153 LEU 153 1150 1150 LEU LEU A . n A 1 154 ARG 154 1151 1151 ARG ARG A . n A 1 155 GLY 155 1152 1152 GLY GLY A . n A 1 156 ALA 156 1153 1153 ALA ALA A . n A 1 157 PHE 157 1154 1154 PHE PHE A . n A 1 158 VAL 158 1155 1155 VAL VAL A . n A 1 159 GLU 159 1156 1156 GLU GLU A . n A 1 160 ASN 160 1157 1157 ASN ASN A . n A 1 161 PRO 161 1158 1158 PRO PRO A . n A 1 162 SER 162 1159 1159 SER SER A . n A 1 163 PHE 163 1160 1160 PHE PHE A . n A 1 164 LYS 164 1161 1161 LYS LYS A . n A 1 165 ARG 165 1162 1162 ARG ARG A . n A 1 166 GLN 166 1163 1163 GLN GLN A . n A 1 167 ILE 167 1164 1164 ILE ILE A . n A 1 168 ILE 168 1165 1165 ILE ILE A . n A 1 169 GLU 169 1166 1166 GLU GLU A . n A 1 170 LYS 170 1167 1167 LYS LYS A . n A 1 171 TYR 171 1168 1168 TYR TYR A . n A 1 172 VAL 172 1169 1169 VAL VAL A . n A 1 173 ILE 173 1170 1170 ILE ILE A . n A 1 174 ASP 174 1171 ? ? ? A . n A 1 175 LYS 175 1172 ? ? ? A . n A 1 176 ASN 176 1173 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 PO4 1 1 1 PO4 PO4 A . C 3 BME 1 1174 1 BME BME A . D 3 BME 1 2 2 BME BME A . E 4 HOH 1 1175 2 HOH HOH A . E 4 HOH 2 1176 3 HOH HOH A . E 4 HOH 3 1177 4 HOH HOH A . E 4 HOH 4 1178 5 HOH HOH A . E 4 HOH 5 1179 6 HOH HOH A . E 4 HOH 6 1180 7 HOH HOH A . E 4 HOH 7 1181 8 HOH HOH A . E 4 HOH 8 1182 9 HOH HOH A . E 4 HOH 9 1183 10 HOH HOH A . E 4 HOH 10 1184 11 HOH HOH A . E 4 HOH 11 1185 12 HOH HOH A . E 4 HOH 12 1186 13 HOH HOH A . E 4 HOH 13 1187 14 HOH HOH A . E 4 HOH 14 1188 15 HOH HOH A . E 4 HOH 15 1189 16 HOH HOH A . E 4 HOH 16 1190 17 HOH HOH A . E 4 HOH 17 1191 18 HOH HOH A . E 4 HOH 18 1192 19 HOH HOH A . E 4 HOH 19 1193 20 HOH HOH A . E 4 HOH 20 1194 21 HOH HOH A . E 4 HOH 21 1195 22 HOH HOH A . E 4 HOH 22 1196 23 HOH HOH A . E 4 HOH 23 1197 24 HOH HOH A . E 4 HOH 24 1198 25 HOH HOH A . E 4 HOH 25 1199 26 HOH HOH A . E 4 HOH 26 1200 27 HOH HOH A . E 4 HOH 27 1201 28 HOH HOH A . E 4 HOH 28 1202 29 HOH HOH A . E 4 HOH 29 1203 30 HOH HOH A . E 4 HOH 30 1204 31 HOH HOH A . E 4 HOH 31 1205 32 HOH HOH A . E 4 HOH 32 1206 33 HOH HOH A . E 4 HOH 33 1207 34 HOH HOH A . E 4 HOH 34 1208 35 HOH HOH A . E 4 HOH 35 1209 36 HOH HOH A . E 4 HOH 36 1210 37 HOH HOH A . E 4 HOH 37 1211 38 HOH HOH A . E 4 HOH 38 1212 39 HOH HOH A . E 4 HOH 39 1213 40 HOH HOH A . E 4 HOH 40 1214 41 HOH HOH A . E 4 HOH 41 1215 42 HOH HOH A . E 4 HOH 42 1216 43 HOH HOH A . E 4 HOH 43 1217 44 HOH HOH A . E 4 HOH 44 1218 45 HOH HOH A . E 4 HOH 45 1219 46 HOH HOH A . E 4 HOH 46 1220 47 HOH HOH A . E 4 HOH 47 1221 48 HOH HOH A . E 4 HOH 48 1222 49 HOH HOH A . E 4 HOH 49 1223 50 HOH HOH A . E 4 HOH 50 1224 51 HOH HOH A . E 4 HOH 51 1225 52 HOH HOH A . E 4 HOH 52 1226 53 HOH HOH A . E 4 HOH 53 1227 54 HOH HOH A . E 4 HOH 54 1228 55 HOH HOH A . E 4 HOH 55 1229 56 HOH HOH A . E 4 HOH 56 1230 57 HOH HOH A . E 4 HOH 57 1231 58 HOH HOH A . E 4 HOH 58 1232 59 HOH HOH A . E 4 HOH 59 1233 60 HOH HOH A . E 4 HOH 60 1234 61 HOH HOH A . E 4 HOH 61 1235 62 HOH HOH A . E 4 HOH 62 1236 63 HOH HOH A . E 4 HOH 63 1237 64 HOH HOH A . E 4 HOH 64 1238 65 HOH HOH A . E 4 HOH 65 1239 66 HOH HOH A . E 4 HOH 66 1240 67 HOH HOH A . E 4 HOH 67 1241 68 HOH HOH A . E 4 HOH 68 1242 69 HOH HOH A . E 4 HOH 69 1243 70 HOH HOH A . E 4 HOH 70 1244 71 HOH HOH A . E 4 HOH 71 1245 72 HOH HOH A . E 4 HOH 72 1246 73 HOH HOH A . E 4 HOH 73 1247 74 HOH HOH A . E 4 HOH 74 1248 75 HOH HOH A . E 4 HOH 75 1249 76 HOH HOH A . E 4 HOH 76 1250 77 HOH HOH A . E 4 HOH 77 1251 78 HOH HOH A . E 4 HOH 78 1252 79 HOH HOH A . E 4 HOH 79 1253 80 HOH HOH A . E 4 HOH 80 1254 81 HOH HOH A . E 4 HOH 81 1255 82 HOH HOH A . E 4 HOH 82 1256 83 HOH HOH A . E 4 HOH 83 1257 84 HOH HOH A . E 4 HOH 84 1258 85 HOH HOH A . E 4 HOH 85 1259 86 HOH HOH A . E 4 HOH 86 1260 87 HOH HOH A . E 4 HOH 87 1261 88 HOH HOH A . E 4 HOH 88 1262 89 HOH HOH A . E 4 HOH 89 1263 90 HOH HOH A . E 4 HOH 90 1264 91 HOH HOH A . E 4 HOH 91 1265 92 HOH HOH A . E 4 HOH 92 1266 93 HOH HOH A . E 4 HOH 93 1267 94 HOH HOH A . E 4 HOH 94 1268 95 HOH HOH A . E 4 HOH 95 1269 96 HOH HOH A . E 4 HOH 96 1270 97 HOH HOH A . E 4 HOH 97 1271 98 HOH HOH A . E 4 HOH 98 1272 99 HOH HOH A . E 4 HOH 99 1273 100 HOH HOH A . E 4 HOH 100 1274 101 HOH HOH A . E 4 HOH 101 1275 102 HOH HOH A . E 4 HOH 102 1276 103 HOH HOH A . E 4 HOH 103 1277 104 HOH HOH A . E 4 HOH 104 1278 105 HOH HOH A . E 4 HOH 105 1279 106 HOH HOH A . E 4 HOH 106 1280 107 HOH HOH A . E 4 HOH 107 1281 108 HOH HOH A . E 4 HOH 108 1282 109 HOH HOH A . E 4 HOH 109 1283 110 HOH HOH A . E 4 HOH 110 1284 111 HOH HOH A . E 4 HOH 111 1285 112 HOH HOH A . E 4 HOH 112 1286 113 HOH HOH A . E 4 HOH 113 1287 114 HOH HOH A . E 4 HOH 114 1288 115 HOH HOH A . E 4 HOH 115 1289 116 HOH HOH A . E 4 HOH 116 1290 117 HOH HOH A . E 4 HOH 117 1291 118 HOH HOH A . E 4 HOH 118 1292 119 HOH HOH A . E 4 HOH 119 1293 120 HOH HOH A . E 4 HOH 120 1294 121 HOH HOH A . E 4 HOH 121 1295 122 HOH HOH A . E 4 HOH 122 1296 123 HOH HOH A . E 4 HOH 123 1297 124 HOH HOH A . E 4 HOH 124 1298 125 HOH HOH A . E 4 HOH 125 1299 126 HOH HOH A . E 4 HOH 126 1300 127 HOH HOH A . E 4 HOH 127 1301 128 HOH HOH A . E 4 HOH 128 1302 129 HOH HOH A . E 4 HOH 129 1303 130 HOH HOH A . E 4 HOH 130 1304 131 HOH HOH A . E 4 HOH 131 1305 132 HOH HOH A . E 4 HOH 132 1306 133 HOH HOH A . E 4 HOH 133 1307 134 HOH HOH A . E 4 HOH 134 1308 135 HOH HOH A . E 4 HOH 135 1309 136 HOH HOH A . E 4 HOH 136 1310 137 HOH HOH A . E 4 HOH 137 1311 138 HOH HOH A . E 4 HOH 138 1312 139 HOH HOH A . E 4 HOH 139 1313 140 HOH HOH A . E 4 HOH 140 1314 141 HOH HOH A . E 4 HOH 141 1315 142 HOH HOH A . E 4 HOH 142 1316 143 HOH HOH A . E 4 HOH 143 1317 144 HOH HOH A . E 4 HOH 144 1318 145 HOH HOH A . E 4 HOH 145 1319 146 HOH HOH A . E 4 HOH 146 1320 147 HOH HOH A . E 4 HOH 147 1321 148 HOH HOH A . E 4 HOH 148 1322 149 HOH HOH A . E 4 HOH 149 1323 150 HOH HOH A . E 4 HOH 150 1324 151 HOH HOH A . E 4 HOH 151 1325 152 HOH HOH A . E 4 HOH 152 1326 153 HOH HOH A . E 4 HOH 153 1327 154 HOH HOH A . E 4 HOH 154 1328 155 HOH HOH A . E 4 HOH 155 1329 156 HOH HOH A . E 4 HOH 156 1330 157 HOH HOH A . E 4 HOH 157 1331 158 HOH HOH A . E 4 HOH 158 1332 159 HOH HOH A . E 4 HOH 159 1333 160 HOH HOH A . E 4 HOH 160 1334 161 HOH HOH A . E 4 HOH 161 1335 162 HOH HOH A . E 4 HOH 162 1336 163 HOH HOH A . E 4 HOH 163 1337 164 HOH HOH A . E 4 HOH 164 1338 165 HOH HOH A . E 4 HOH 165 1339 166 HOH HOH A . E 4 HOH 166 1340 167 HOH HOH A . E 4 HOH 167 1341 168 HOH HOH A . E 4 HOH 168 1342 169 HOH HOH A . E 4 HOH 169 1343 170 HOH HOH A . E 4 HOH 170 1344 171 HOH HOH A . E 4 HOH 171 1345 172 HOH HOH A . E 4 HOH 172 1346 173 HOH HOH A . E 4 HOH 173 1347 174 HOH HOH A . E 4 HOH 174 1348 175 HOH HOH A . E 4 HOH 175 1349 176 HOH HOH A . E 4 HOH 176 1350 177 HOH HOH A . E 4 HOH 177 1351 178 HOH HOH A . E 4 HOH 178 1352 179 HOH HOH A . E 4 HOH 179 1353 180 HOH HOH A . E 4 HOH 180 1354 181 HOH HOH A . E 4 HOH 181 1355 182 HOH HOH A . E 4 HOH 182 1356 183 HOH HOH A . E 4 HOH 183 1357 184 HOH HOH A . E 4 HOH 184 1358 185 HOH HOH A . E 4 HOH 185 1359 186 HOH HOH A . E 4 HOH 186 1360 187 HOH HOH A . E 4 HOH 187 1361 188 HOH HOH A . E 4 HOH 188 1362 189 HOH HOH A . E 4 HOH 189 1363 190 HOH HOH A . E 4 HOH 190 1364 191 HOH HOH A . E 4 HOH 191 1365 192 HOH HOH A . E 4 HOH 192 1366 193 HOH HOH A . E 4 HOH 193 1367 194 HOH HOH A . E 4 HOH 194 1368 195 HOH HOH A . E 4 HOH 195 1369 196 HOH HOH A . E 4 HOH 196 1370 197 HOH HOH A . E 4 HOH 197 1371 198 HOH HOH A . E 4 HOH 198 1372 199 HOH HOH A . E 4 HOH 199 1373 200 HOH HOH A . E 4 HOH 200 1374 201 HOH HOH A . E 4 HOH 201 1375 202 HOH HOH A . E 4 HOH 202 1376 203 HOH HOH A . E 4 HOH 203 1377 204 HOH HOH A . E 4 HOH 204 1378 205 HOH HOH A . E 4 HOH 205 1379 206 HOH HOH A . E 4 HOH 206 1380 207 HOH HOH A . E 4 HOH 207 1381 208 HOH HOH A . E 4 HOH 208 1382 209 HOH HOH A . E 4 HOH 209 1383 210 HOH HOH A . E 4 HOH 210 1384 211 HOH HOH A . E 4 HOH 211 1385 212 HOH HOH A . E 4 HOH 212 1386 213 HOH HOH A . E 4 HOH 213 1387 214 HOH HOH A . E 4 HOH 214 1388 215 HOH HOH A . E 4 HOH 215 1389 216 HOH HOH A . E 4 HOH 216 1390 217 HOH HOH A . E 4 HOH 217 1391 218 HOH HOH A . E 4 HOH 218 1392 219 HOH HOH A . E 4 HOH 219 1393 220 HOH HOH A . E 4 HOH 220 1394 221 HOH HOH A . E 4 HOH 221 1395 222 HOH HOH A . E 4 HOH 222 1396 223 HOH HOH A . E 4 HOH 223 1397 224 HOH HOH A . E 4 HOH 224 1398 225 HOH HOH A . E 4 HOH 225 1399 226 HOH HOH A . E 4 HOH 226 1400 227 HOH HOH A . E 4 HOH 227 1401 228 HOH HOH A . E 4 HOH 228 1402 229 HOH HOH A . E 4 HOH 229 1403 230 HOH HOH A . E 4 HOH 230 1404 231 HOH HOH A . E 4 HOH 231 1405 232 HOH HOH A . E 4 HOH 232 1406 233 HOH HOH A . E 4 HOH 233 1407 234 HOH HOH A . E 4 HOH 234 1408 235 HOH HOH A . E 4 HOH 235 1409 236 HOH HOH A . E 4 HOH 236 1410 237 HOH HOH A . E 4 HOH 237 1411 238 HOH HOH A . E 4 HOH 238 1412 239 HOH HOH A . E 4 HOH 239 1413 240 HOH HOH A . E 4 HOH 240 1414 241 HOH HOH A . E 4 HOH 241 1415 242 HOH HOH A . E 4 HOH 242 1416 243 HOH HOH A . E 4 HOH 243 1417 244 HOH HOH A . E 4 HOH 244 1418 245 HOH HOH A . E 4 HOH 245 1419 246 HOH HOH A . E 4 HOH 246 1420 247 HOH HOH A . E 4 HOH 247 1421 248 HOH HOH A . E 4 HOH 248 1422 249 HOH HOH A . E 4 HOH 249 1423 250 HOH HOH A . E 4 HOH 250 1424 251 HOH HOH A . E 4 HOH 251 1425 252 HOH HOH A . E 4 HOH 252 1426 253 HOH HOH A . E 4 HOH 253 1427 254 HOH HOH A . E 4 HOH 254 1428 255 HOH HOH A . E 4 HOH 255 1429 256 HOH HOH A . E 4 HOH 256 1430 257 HOH HOH A . E 4 HOH 257 1431 258 HOH HOH A . E 4 HOH 258 1432 259 HOH HOH A . E 4 HOH 259 1433 260 HOH HOH A . E 4 HOH 260 1434 261 HOH HOH A . E 4 HOH 261 1435 262 HOH HOH A . E 4 HOH 262 1436 263 HOH HOH A . E 4 HOH 263 1437 264 HOH HOH A . E 4 HOH 264 1438 265 HOH HOH A . E 4 HOH 265 1439 266 HOH HOH A . E 4 HOH 266 1440 267 HOH HOH A . E 4 HOH 267 1441 268 HOH HOH A . E 4 HOH 268 1442 269 HOH HOH A . E 4 HOH 269 1443 270 HOH HOH A . E 4 HOH 270 1444 271 HOH HOH A . E 4 HOH 271 1445 272 HOH HOH A . E 4 HOH 272 1446 273 HOH HOH A . E 4 HOH 273 1447 274 HOH HOH A . E 4 HOH 274 1448 275 HOH HOH A . E 4 HOH 275 1449 276 HOH HOH A . E 4 HOH 276 1450 277 HOH HOH A . E 4 HOH 277 1451 278 HOH HOH A . E 4 HOH 278 1452 279 HOH HOH A . E 4 HOH 279 1453 280 HOH HOH A . E 4 HOH 280 1454 281 HOH HOH A . E 4 HOH 281 1455 282 HOH HOH A . E 4 HOH 282 1456 283 HOH HOH A . E 4 HOH 283 1457 284 HOH HOH A . E 4 HOH 284 1458 285 HOH HOH A . E 4 HOH 285 1459 286 HOH HOH A . E 4 HOH 286 1460 287 HOH HOH A . E 4 HOH 287 1461 288 HOH HOH A . E 4 HOH 288 1462 289 HOH HOH A . E 4 HOH 289 1463 290 HOH HOH A . E 4 HOH 290 1464 291 HOH HOH A . E 4 HOH 291 1465 292 HOH HOH A . E 4 HOH 292 1466 293 HOH HOH A . E 4 HOH 293 1467 294 HOH HOH A . E 4 HOH 294 1468 295 HOH HOH A . E 4 HOH 295 1469 296 HOH HOH A . E 4 HOH 296 1470 297 HOH HOH A . E 4 HOH 297 1471 298 HOH HOH A . E 4 HOH 298 1472 299 HOH HOH A . E 4 HOH 299 1473 300 HOH HOH A . E 4 HOH 300 1474 301 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 3230 ? 1 MORE -42.0 ? 1 'SSA (A^2)' 15430 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 4_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 1243 ? E HOH . 2 1 A HOH 1325 ? E HOH . 3 1 A HOH 1373 ? E HOH . # 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 2009-02-10 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2021-10-20 4 'Structure model' 1 3 2023-08-30 # _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 ? _pdbx_audit_revision_details.details ? # 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' 'Database references' 3 3 'Structure model' 'Derived calculations' 4 4 'Structure model' 'Data collection' 5 4 'Structure model' 'Refinement description' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 3 'Structure model' database_2 2 3 'Structure model' struct_ref_seq_dif 3 3 'Structure model' struct_site 4 4 'Structure model' chem_comp_atom 5 4 'Structure model' chem_comp_bond 6 4 'Structure model' pdbx_initial_refinement_model # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 3 'Structure model' '_database_2.pdbx_DOI' 2 3 'Structure model' '_database_2.pdbx_database_accession' 3 3 'Structure model' '_struct_ref_seq_dif.details' 4 3 'Structure model' '_struct_site.pdbx_auth_asym_id' 5 3 'Structure model' '_struct_site.pdbx_auth_comp_id' 6 3 'Structure model' '_struct_site.pdbx_auth_seq_id' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0019 ? 1 ADSC 'data collection' Quantum ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 MOLREP phasing . ? 5 # 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 THR A 1027 ? ? -121.78 -53.99 2 1 SER A 1112 ? ? -128.88 -151.55 3 1 VAL A 1116 ? ? -121.11 -54.11 4 1 ASN A 1117 ? ? -101.60 -67.46 5 1 VAL A 1155 ? ? 30.91 57.66 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLY 998 ? A GLY 1 2 1 Y 1 A PRO 999 ? A PRO 2 3 1 Y 1 A GLU 1000 ? A GLU 3 4 1 Y 1 A ILE 1001 ? A ILE 4 5 1 Y 1 A ARG 1002 ? A ARG 5 6 1 Y 1 A MET 1003 ? A MET 6 7 1 Y 1 A ASP 1004 ? A ASP 7 8 1 Y 1 A LYS 1005 ? A LYS 8 9 1 Y 1 A LYS 1006 ? A LYS 9 10 1 Y 1 A ASP 1171 ? A ASP 174 11 1 Y 1 A LYS 1172 ? A LYS 175 12 1 Y 1 A ASN 1173 ? A ASN 176 # loop_ _chem_comp_atom.comp_id _chem_comp_atom.atom_id _chem_comp_atom.type_symbol _chem_comp_atom.pdbx_aromatic_flag _chem_comp_atom.pdbx_stereo_config _chem_comp_atom.pdbx_ordinal ALA N N N N 1 ALA CA C N S 2 ALA C C N N 3 ALA O O N N 4 ALA CB C N N 5 ALA OXT O N N 6 ALA H H N N 7 ALA H2 H N N 8 ALA HA H N N 9 ALA HB1 H N N 10 ALA HB2 H N N 11 ALA HB3 H N N 12 ALA HXT H N N 13 ARG N N N N 14 ARG CA C N S 15 ARG C C N N 16 ARG O O N N 17 ARG CB C N N 18 ARG CG C N N 19 ARG CD C N N 20 ARG NE N N N 21 ARG CZ C N N 22 ARG NH1 N N N 23 ARG NH2 N N N 24 ARG OXT O N N 25 ARG H H N N 26 ARG H2 H N N 27 ARG HA H N N 28 ARG HB2 H N N 29 ARG HB3 H N N 30 ARG HG2 H N N 31 ARG HG3 H N N 32 ARG HD2 H N N 33 ARG HD3 H N N 34 ARG HE H N N 35 ARG HH11 H N N 36 ARG HH12 H N N 37 ARG HH21 H N N 38 ARG HH22 H N N 39 ARG HXT H N N 40 ASN N N N N 41 ASN CA C N S 42 ASN C C N N 43 ASN O O N N 44 ASN CB C N N 45 ASN CG C N N 46 ASN OD1 O N N 47 ASN ND2 N N N 48 ASN OXT O N N 49 ASN H H N N 50 ASN H2 H N N 51 ASN HA H N N 52 ASN HB2 H N N 53 ASN HB3 H N N 54 ASN HD21 H N N 55 ASN HD22 H N N 56 ASN HXT H N N 57 ASP N N N N 58 ASP CA C N S 59 ASP C C N N 60 ASP O O N N 61 ASP CB C N N 62 ASP CG C N N 63 ASP OD1 O N N 64 ASP OD2 O N N 65 ASP OXT O N N 66 ASP H H N N 67 ASP H2 H N N 68 ASP HA H N N 69 ASP HB2 H N N 70 ASP HB3 H N N 71 ASP HD2 H N N 72 ASP HXT H N N 73 BME C1 C N N 74 BME C2 C N N 75 BME O1 O N N 76 BME S2 S N N 77 BME H11 H N N 78 BME H12 H N N 79 BME H21 H N N 80 BME H22 H N N 81 BME HO1 H N N 82 BME HS2 H N N 83 CYS N N N N 84 CYS CA C N R 85 CYS C C N N 86 CYS O O N N 87 CYS CB C N N 88 CYS SG S N N 89 CYS OXT O N N 90 CYS H H N N 91 CYS H2 H N N 92 CYS HA H N N 93 CYS HB2 H N N 94 CYS HB3 H N N 95 CYS HG H N N 96 CYS HXT H N N 97 GLN N N N N 98 GLN CA C N S 99 GLN C C N N 100 GLN O O N N 101 GLN CB C N N 102 GLN CG C N N 103 GLN CD C N N 104 GLN OE1 O N N 105 GLN NE2 N N N 106 GLN OXT O N N 107 GLN H H N N 108 GLN H2 H N N 109 GLN HA H N N 110 GLN HB2 H N N 111 GLN HB3 H N N 112 GLN HG2 H N N 113 GLN HG3 H N N 114 GLN HE21 H N N 115 GLN HE22 H N N 116 GLN HXT H N N 117 GLU N N N N 118 GLU CA C N S 119 GLU C C N N 120 GLU O O N N 121 GLU CB C N N 122 GLU CG C N N 123 GLU CD C N N 124 GLU OE1 O N N 125 GLU OE2 O N N 126 GLU OXT O N N 127 GLU H H N N 128 GLU H2 H N N 129 GLU HA H N N 130 GLU HB2 H N N 131 GLU HB3 H N N 132 GLU HG2 H N N 133 GLU HG3 H N N 134 GLU HE2 H N N 135 GLU HXT H N N 136 GLY N N N N 137 GLY CA C N N 138 GLY C C N N 139 GLY O O N N 140 GLY OXT O N N 141 GLY H H N N 142 GLY H2 H N N 143 GLY HA2 H N N 144 GLY HA3 H N N 145 GLY HXT H N N 146 HIS N N N N 147 HIS CA C N S 148 HIS C C N N 149 HIS O O N N 150 HIS CB C N N 151 HIS CG C Y N 152 HIS ND1 N Y N 153 HIS CD2 C Y N 154 HIS CE1 C Y N 155 HIS NE2 N Y N 156 HIS OXT O N N 157 HIS H H N N 158 HIS H2 H N N 159 HIS HA H N N 160 HIS HB2 H N N 161 HIS HB3 H N N 162 HIS HD1 H N N 163 HIS HD2 H N N 164 HIS HE1 H N N 165 HIS HE2 H N N 166 HIS HXT H N N 167 HOH O O N N 168 HOH H1 H N N 169 HOH H2 H N N 170 ILE N N N N 171 ILE CA C N S 172 ILE C C N N 173 ILE O O N N 174 ILE CB C N S 175 ILE CG1 C N N 176 ILE CG2 C N N 177 ILE CD1 C N N 178 ILE OXT O N N 179 ILE H H N N 180 ILE H2 H N N 181 ILE HA H N N 182 ILE HB H N N 183 ILE HG12 H N N 184 ILE HG13 H N N 185 ILE HG21 H N N 186 ILE HG22 H N N 187 ILE HG23 H N N 188 ILE HD11 H N N 189 ILE HD12 H N N 190 ILE HD13 H N N 191 ILE HXT H N N 192 LEU N N N N 193 LEU CA C N S 194 LEU C C N N 195 LEU O O N N 196 LEU CB C N N 197 LEU CG C N N 198 LEU CD1 C N N 199 LEU CD2 C N N 200 LEU OXT O N N 201 LEU H H N N 202 LEU H2 H N N 203 LEU HA H N N 204 LEU HB2 H N N 205 LEU HB3 H N N 206 LEU HG H N N 207 LEU HD11 H N N 208 LEU HD12 H N N 209 LEU HD13 H N N 210 LEU HD21 H N N 211 LEU HD22 H N N 212 LEU HD23 H N N 213 LEU HXT H N N 214 LYS N N N N 215 LYS CA C N S 216 LYS C C N N 217 LYS O O N N 218 LYS CB C N N 219 LYS CG C N N 220 LYS CD C N N 221 LYS CE C N N 222 LYS NZ N N N 223 LYS OXT O N N 224 LYS H H N N 225 LYS H2 H N N 226 LYS HA H N N 227 LYS HB2 H N N 228 LYS HB3 H N N 229 LYS HG2 H N N 230 LYS HG3 H N N 231 LYS HD2 H N N 232 LYS HD3 H N N 233 LYS HE2 H N N 234 LYS HE3 H N N 235 LYS HZ1 H N N 236 LYS HZ2 H N N 237 LYS HZ3 H N N 238 LYS HXT H N N 239 MET N N N N 240 MET CA C N S 241 MET C C N N 242 MET O O N N 243 MET CB C N N 244 MET CG C N N 245 MET SD S N N 246 MET CE C N N 247 MET OXT O N N 248 MET H H N N 249 MET H2 H N N 250 MET HA H N N 251 MET HB2 H N N 252 MET HB3 H N N 253 MET HG2 H N N 254 MET HG3 H N N 255 MET HE1 H N N 256 MET HE2 H N N 257 MET HE3 H N N 258 MET HXT H N N 259 PHE N N N N 260 PHE CA C N S 261 PHE C C N N 262 PHE O O N N 263 PHE CB C N N 264 PHE CG C Y N 265 PHE CD1 C Y N 266 PHE CD2 C Y N 267 PHE CE1 C Y N 268 PHE CE2 C Y N 269 PHE CZ C Y N 270 PHE OXT O N N 271 PHE H H N N 272 PHE H2 H N N 273 PHE HA H N N 274 PHE HB2 H N N 275 PHE HB3 H N N 276 PHE HD1 H N N 277 PHE HD2 H N N 278 PHE HE1 H N N 279 PHE HE2 H N N 280 PHE HZ H N N 281 PHE HXT H N N 282 PO4 P P N N 283 PO4 O1 O N N 284 PO4 O2 O N N 285 PO4 O3 O N N 286 PO4 O4 O N N 287 PRO N N N N 288 PRO CA C N S 289 PRO C C N N 290 PRO O O N N 291 PRO CB C N N 292 PRO CG C N N 293 PRO CD C N N 294 PRO OXT O N N 295 PRO H H N N 296 PRO HA H N N 297 PRO HB2 H N N 298 PRO HB3 H N N 299 PRO HG2 H N N 300 PRO HG3 H N N 301 PRO HD2 H N N 302 PRO HD3 H N N 303 PRO HXT H N N 304 SER N N N N 305 SER CA C N S 306 SER C C N N 307 SER O O N N 308 SER CB C N N 309 SER OG O N N 310 SER OXT O N N 311 SER H H N N 312 SER H2 H N N 313 SER HA H N N 314 SER HB2 H N N 315 SER HB3 H N N 316 SER HG H N N 317 SER HXT H N N 318 THR N N N N 319 THR CA C N S 320 THR C C N N 321 THR O O N N 322 THR CB C N R 323 THR OG1 O N N 324 THR CG2 C N N 325 THR OXT O N N 326 THR H H N N 327 THR H2 H N N 328 THR HA H N N 329 THR HB H N N 330 THR HG1 H N N 331 THR HG21 H N N 332 THR HG22 H N N 333 THR HG23 H N N 334 THR HXT H N N 335 TYR N N N N 336 TYR CA C N S 337 TYR C C N N 338 TYR O O N N 339 TYR CB C N N 340 TYR CG C Y N 341 TYR CD1 C Y N 342 TYR CD2 C Y N 343 TYR CE1 C Y N 344 TYR CE2 C Y N 345 TYR CZ C Y N 346 TYR OH O N N 347 TYR OXT O N N 348 TYR H H N N 349 TYR H2 H N N 350 TYR HA H N N 351 TYR HB2 H N N 352 TYR HB3 H N N 353 TYR HD1 H N N 354 TYR HD2 H N N 355 TYR HE1 H N N 356 TYR HE2 H N N 357 TYR HH H N N 358 TYR HXT H N N 359 VAL N N N N 360 VAL CA C N S 361 VAL C C N N 362 VAL O O N N 363 VAL CB C N N 364 VAL CG1 C N N 365 VAL CG2 C N N 366 VAL OXT O N N 367 VAL H H N N 368 VAL H2 H N N 369 VAL HA H N N 370 VAL HB H N N 371 VAL HG11 H N N 372 VAL HG12 H N N 373 VAL HG13 H N N 374 VAL HG21 H N N 375 VAL HG22 H N N 376 VAL HG23 H N N 377 VAL HXT H N N 378 # loop_ _chem_comp_bond.comp_id _chem_comp_bond.atom_id_1 _chem_comp_bond.atom_id_2 _chem_comp_bond.value_order _chem_comp_bond.pdbx_aromatic_flag _chem_comp_bond.pdbx_stereo_config _chem_comp_bond.pdbx_ordinal ALA N CA sing N N 1 ALA N H sing N N 2 ALA N H2 sing N N 3 ALA CA C sing N N 4 ALA CA CB sing N N 5 ALA CA HA sing N N 6 ALA C O doub N N 7 ALA C OXT sing N N 8 ALA CB HB1 sing N N 9 ALA CB HB2 sing N N 10 ALA CB HB3 sing N N 11 ALA OXT HXT sing N N 12 ARG N CA sing N N 13 ARG N H sing N N 14 ARG N H2 sing N N 15 ARG CA C sing N N 16 ARG CA CB sing N N 17 ARG CA HA sing N N 18 ARG C O doub N N 19 ARG C OXT sing N N 20 ARG CB CG sing N N 21 ARG CB HB2 sing N N 22 ARG CB HB3 sing N N 23 ARG CG CD sing N N 24 ARG CG HG2 sing N N 25 ARG CG HG3 sing N N 26 ARG CD NE sing N N 27 ARG CD HD2 sing N N 28 ARG CD HD3 sing N N 29 ARG NE CZ sing N N 30 ARG NE HE sing N N 31 ARG CZ NH1 sing N N 32 ARG CZ NH2 doub N N 33 ARG NH1 HH11 sing N N 34 ARG NH1 HH12 sing N N 35 ARG NH2 HH21 sing N N 36 ARG NH2 HH22 sing N N 37 ARG OXT HXT sing N N 38 ASN N CA sing N N 39 ASN N H sing N N 40 ASN N H2 sing N N 41 ASN CA C sing N N 42 ASN CA CB sing N N 43 ASN CA HA sing N N 44 ASN C O doub N N 45 ASN C OXT sing N N 46 ASN CB CG sing N N 47 ASN CB HB2 sing N N 48 ASN CB HB3 sing N N 49 ASN CG OD1 doub N N 50 ASN CG ND2 sing N N 51 ASN ND2 HD21 sing N N 52 ASN ND2 HD22 sing N N 53 ASN OXT HXT sing N N 54 ASP N CA sing N N 55 ASP N H sing N N 56 ASP N H2 sing N N 57 ASP CA C sing N N 58 ASP CA CB sing N N 59 ASP CA HA sing N N 60 ASP C O doub N N 61 ASP C OXT sing N N 62 ASP CB CG sing N N 63 ASP CB HB2 sing N N 64 ASP CB HB3 sing N N 65 ASP CG OD1 doub N N 66 ASP CG OD2 sing N N 67 ASP OD2 HD2 sing N N 68 ASP OXT HXT sing N N 69 BME C1 C2 sing N N 70 BME C1 O1 sing N N 71 BME C1 H11 sing N N 72 BME C1 H12 sing N N 73 BME C2 S2 sing N N 74 BME C2 H21 sing N N 75 BME C2 H22 sing N N 76 BME O1 HO1 sing N N 77 BME S2 HS2 sing N N 78 CYS N CA sing N N 79 CYS N H sing N N 80 CYS N H2 sing N N 81 CYS CA C sing N N 82 CYS CA CB sing N N 83 CYS CA HA sing N N 84 CYS C O doub N N 85 CYS C OXT sing N N 86 CYS CB SG sing N N 87 CYS CB HB2 sing N N 88 CYS CB HB3 sing N N 89 CYS SG HG sing N N 90 CYS OXT HXT sing N N 91 GLN N CA sing N N 92 GLN N H sing N N 93 GLN N H2 sing N N 94 GLN CA C sing N N 95 GLN CA CB sing N N 96 GLN CA HA sing N N 97 GLN C O doub N N 98 GLN C OXT sing N N 99 GLN CB CG sing N N 100 GLN CB HB2 sing N N 101 GLN CB HB3 sing N N 102 GLN CG CD sing N N 103 GLN CG HG2 sing N N 104 GLN CG HG3 sing N N 105 GLN CD OE1 doub N N 106 GLN CD NE2 sing N N 107 GLN NE2 HE21 sing N N 108 GLN NE2 HE22 sing N N 109 GLN OXT HXT sing N N 110 GLU N CA sing N N 111 GLU N H sing N N 112 GLU N H2 sing N N 113 GLU CA C sing N N 114 GLU CA CB sing N N 115 GLU CA HA sing N N 116 GLU C O doub N N 117 GLU C OXT sing N N 118 GLU CB CG sing N N 119 GLU CB HB2 sing N N 120 GLU CB HB3 sing N N 121 GLU CG CD sing N N 122 GLU CG HG2 sing N N 123 GLU CG HG3 sing N N 124 GLU CD OE1 doub N N 125 GLU CD OE2 sing N N 126 GLU OE2 HE2 sing N N 127 GLU OXT HXT sing N N 128 GLY N CA sing N N 129 GLY N H sing N N 130 GLY N H2 sing N N 131 GLY CA C sing N N 132 GLY CA HA2 sing N N 133 GLY CA HA3 sing N N 134 GLY C O doub N N 135 GLY C OXT sing N N 136 GLY OXT HXT sing N N 137 HIS N CA sing N N 138 HIS N H sing N N 139 HIS N H2 sing N N 140 HIS CA C sing N N 141 HIS CA CB sing N N 142 HIS CA HA sing N N 143 HIS C O doub N N 144 HIS C OXT sing N N 145 HIS CB CG sing N N 146 HIS CB HB2 sing N N 147 HIS CB HB3 sing N N 148 HIS CG ND1 sing Y N 149 HIS CG CD2 doub Y N 150 HIS ND1 CE1 doub Y N 151 HIS ND1 HD1 sing N N 152 HIS CD2 NE2 sing Y N 153 HIS CD2 HD2 sing N N 154 HIS CE1 NE2 sing Y N 155 HIS CE1 HE1 sing N N 156 HIS NE2 HE2 sing N N 157 HIS OXT HXT sing N N 158 HOH O H1 sing N N 159 HOH O H2 sing N N 160 ILE N CA sing N N 161 ILE N H sing N N 162 ILE N H2 sing N N 163 ILE CA C sing N N 164 ILE CA CB sing N N 165 ILE CA HA sing N N 166 ILE C O doub N N 167 ILE C OXT sing N N 168 ILE CB CG1 sing N N 169 ILE CB CG2 sing N N 170 ILE CB HB sing N N 171 ILE CG1 CD1 sing N N 172 ILE CG1 HG12 sing N N 173 ILE CG1 HG13 sing N N 174 ILE CG2 HG21 sing N N 175 ILE CG2 HG22 sing N N 176 ILE CG2 HG23 sing N N 177 ILE CD1 HD11 sing N N 178 ILE CD1 HD12 sing N N 179 ILE CD1 HD13 sing N N 180 ILE OXT HXT sing N N 181 LEU N CA sing N N 182 LEU N H sing N N 183 LEU N H2 sing N N 184 LEU CA C sing N N 185 LEU CA CB sing N N 186 LEU CA HA sing N N 187 LEU C O doub N N 188 LEU C OXT sing N N 189 LEU CB CG sing N N 190 LEU CB HB2 sing N N 191 LEU CB HB3 sing N N 192 LEU CG CD1 sing N N 193 LEU CG CD2 sing N N 194 LEU CG HG sing N N 195 LEU CD1 HD11 sing N N 196 LEU CD1 HD12 sing N N 197 LEU CD1 HD13 sing N N 198 LEU CD2 HD21 sing N N 199 LEU CD2 HD22 sing N N 200 LEU CD2 HD23 sing N N 201 LEU OXT HXT sing N N 202 LYS N CA sing N N 203 LYS N H sing N N 204 LYS N H2 sing N N 205 LYS CA C sing N N 206 LYS CA CB sing N N 207 LYS CA HA sing N N 208 LYS C O doub N N 209 LYS C OXT sing N N 210 LYS CB CG sing N N 211 LYS CB HB2 sing N N 212 LYS CB HB3 sing N N 213 LYS CG CD sing N N 214 LYS CG HG2 sing N N 215 LYS CG HG3 sing N N 216 LYS CD CE sing N N 217 LYS CD HD2 sing N N 218 LYS CD HD3 sing N N 219 LYS CE NZ sing N N 220 LYS CE HE2 sing N N 221 LYS CE HE3 sing N N 222 LYS NZ HZ1 sing N N 223 LYS NZ HZ2 sing N N 224 LYS NZ HZ3 sing N N 225 LYS OXT HXT sing N N 226 MET N CA sing N N 227 MET N H sing N N 228 MET N H2 sing N N 229 MET CA C sing N N 230 MET CA CB sing N N 231 MET CA HA sing N N 232 MET C O doub N N 233 MET C OXT sing N N 234 MET CB CG sing N N 235 MET CB HB2 sing N N 236 MET CB HB3 sing N N 237 MET CG SD sing N N 238 MET CG HG2 sing N N 239 MET CG HG3 sing N N 240 MET SD CE sing N N 241 MET CE HE1 sing N N 242 MET CE HE2 sing N N 243 MET CE HE3 sing N N 244 MET OXT HXT sing N N 245 PHE N CA sing N N 246 PHE N H sing N N 247 PHE N H2 sing N N 248 PHE CA C sing N N 249 PHE CA CB sing N N 250 PHE CA HA sing N N 251 PHE C O doub N N 252 PHE C OXT sing N N 253 PHE CB CG sing N N 254 PHE CB HB2 sing N N 255 PHE CB HB3 sing N N 256 PHE CG CD1 doub Y N 257 PHE CG CD2 sing Y N 258 PHE CD1 CE1 sing Y N 259 PHE CD1 HD1 sing N N 260 PHE CD2 CE2 doub Y N 261 PHE CD2 HD2 sing N N 262 PHE CE1 CZ doub Y N 263 PHE CE1 HE1 sing N N 264 PHE CE2 CZ sing Y N 265 PHE CE2 HE2 sing N N 266 PHE CZ HZ sing N N 267 PHE OXT HXT sing N N 268 PO4 P O1 doub N N 269 PO4 P O2 sing N N 270 PO4 P O3 sing N N 271 PO4 P O4 sing N N 272 PRO N CA sing N N 273 PRO N CD sing N N 274 PRO N H sing N N 275 PRO CA C sing N N 276 PRO CA CB sing N N 277 PRO CA HA sing N N 278 PRO C O doub N N 279 PRO C OXT sing N N 280 PRO CB CG sing N N 281 PRO CB HB2 sing N N 282 PRO CB HB3 sing N N 283 PRO CG CD sing N N 284 PRO CG HG2 sing N N 285 PRO CG HG3 sing N N 286 PRO CD HD2 sing N N 287 PRO CD HD3 sing N N 288 PRO OXT HXT sing N N 289 SER N CA sing N N 290 SER N H sing N N 291 SER N H2 sing N N 292 SER CA C sing N N 293 SER CA CB sing N N 294 SER CA HA sing N N 295 SER C O doub N N 296 SER C OXT sing N N 297 SER CB OG sing N N 298 SER CB HB2 sing N N 299 SER CB HB3 sing N N 300 SER OG HG sing N N 301 SER OXT HXT sing N N 302 THR N CA sing N N 303 THR N H sing N N 304 THR N H2 sing N N 305 THR CA C sing N N 306 THR CA CB sing N N 307 THR CA HA sing N N 308 THR C O doub N N 309 THR C OXT sing N N 310 THR CB OG1 sing N N 311 THR CB CG2 sing N N 312 THR CB HB sing N N 313 THR OG1 HG1 sing N N 314 THR CG2 HG21 sing N N 315 THR CG2 HG22 sing N N 316 THR CG2 HG23 sing N N 317 THR OXT HXT sing N N 318 TYR N CA sing N N 319 TYR N H sing N N 320 TYR N H2 sing N N 321 TYR CA C sing N N 322 TYR CA CB sing N N 323 TYR CA HA sing N N 324 TYR C O doub N N 325 TYR C OXT sing N N 326 TYR CB CG sing N N 327 TYR CB HB2 sing N N 328 TYR CB HB3 sing N N 329 TYR CG CD1 doub Y N 330 TYR CG CD2 sing Y N 331 TYR CD1 CE1 sing Y N 332 TYR CD1 HD1 sing N N 333 TYR CD2 CE2 doub Y N 334 TYR CD2 HD2 sing N N 335 TYR CE1 CZ doub Y N 336 TYR CE1 HE1 sing N N 337 TYR CE2 CZ sing Y N 338 TYR CE2 HE2 sing N N 339 TYR CZ OH sing N N 340 TYR OH HH sing N N 341 TYR OXT HXT sing N N 342 VAL N CA sing N N 343 VAL N H sing N N 344 VAL N H2 sing N N 345 VAL CA C sing N N 346 VAL CA CB sing N N 347 VAL CA HA sing N N 348 VAL C O doub N N 349 VAL C OXT sing N N 350 VAL CB CG1 sing N N 351 VAL CB CG2 sing N N 352 VAL CB HB sing N N 353 VAL CG1 HG11 sing N N 354 VAL CG1 HG12 sing N N 355 VAL CG1 HG13 sing N N 356 VAL CG2 HG21 sing N N 357 VAL CG2 HG22 sing N N 358 VAL CG2 HG23 sing N N 359 VAL OXT HXT sing N N 360 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'PHOSPHATE ION' PO4 3 BETA-MERCAPTOETHANOL BME 4 water HOH # _pdbx_initial_refinement_model.id 1 _pdbx_initial_refinement_model.entity_id_list ? _pdbx_initial_refinement_model.type 'experimental model' _pdbx_initial_refinement_model.source_name PDB _pdbx_initial_refinement_model.accession_code 2RF6 _pdbx_initial_refinement_model.details 'PDB Entry 2RF6' # If you find results from this site helpful for your research, please cite one of our papers:
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