data_1DR9 # _entry.id 1DR9 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.289 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1DR9 RCSB RCSB010314 WWPDB D_1000010314 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1DR9 _pdbx_database_status.recvd_initial_deposition_date 2000-01-06 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Ikemizu, S.' 1 'Jones, E.Y.' 2 'Stuart, D.I.' 3 'Davis, S.J.' 4 # _citation.id primary _citation.title 'Structure and dimerization of a soluble form of B7-1.' _citation.journal_abbrev Immunity _citation.journal_volume 12 _citation.page_first 51 _citation.page_last 60 _citation.year 2000 _citation.journal_id_ASTM IUNIEH _citation.country US _citation.journal_id_ISSN 1074-7613 _citation.journal_id_CSD 2048 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 10661405 _citation.pdbx_database_id_DOI '10.1016/S1074-7613(00)80158-2' # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Ikemizu, S.' 1 primary 'Gilbert, R.J.' 2 primary 'Fennelly, J.A.' 3 primary 'Collins, A.V.' 4 primary 'Harlos, K.' 5 primary 'Jones, E.Y.' 6 primary 'Stuart, D.I.' 7 primary 'Davis, S.J.' 8 # _cell.entry_id 1DR9 _cell.length_a 57.280 _cell.length_b 57.280 _cell.length_c 298.930 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1DR9 _symmetry.space_group_name_H-M 'I 41 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 98 # 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 'T LYMPHOCYTE ACTIVATION ANTIGEN' 22993.123 1 ? ? 'EXTRACELLULAR REGION' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'B7-1 (CD80)' # _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 ;VIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTY ECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPE TELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTAK ; _entity_poly.pdbx_seq_one_letter_code_can ;VIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTY ECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPE TELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTAK ; _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 VAL n 1 2 ILE n 1 3 HIS n 1 4 VAL n 1 5 THR n 1 6 LYS n 1 7 GLU n 1 8 VAL n 1 9 LYS n 1 10 GLU n 1 11 VAL n 1 12 ALA n 1 13 THR n 1 14 LEU n 1 15 SER n 1 16 CYS n 1 17 GLY n 1 18 HIS n 1 19 ASN n 1 20 VAL n 1 21 SER n 1 22 VAL n 1 23 GLU n 1 24 GLU n 1 25 LEU n 1 26 ALA n 1 27 GLN n 1 28 THR n 1 29 ARG n 1 30 ILE n 1 31 TYR n 1 32 TRP n 1 33 GLN n 1 34 LYS n 1 35 GLU n 1 36 LYS n 1 37 LYS n 1 38 MET n 1 39 VAL n 1 40 LEU n 1 41 THR n 1 42 MET n 1 43 MET n 1 44 SER n 1 45 GLY n 1 46 ASP n 1 47 MET n 1 48 ASN n 1 49 ILE n 1 50 TRP n 1 51 PRO n 1 52 GLU n 1 53 TYR n 1 54 LYS n 1 55 ASN n 1 56 ARG n 1 57 THR n 1 58 ILE n 1 59 PHE n 1 60 ASP n 1 61 ILE n 1 62 THR n 1 63 ASN n 1 64 ASN n 1 65 LEU n 1 66 SER n 1 67 ILE n 1 68 VAL n 1 69 ILE n 1 70 LEU n 1 71 ALA n 1 72 LEU n 1 73 ARG n 1 74 PRO n 1 75 SER n 1 76 ASP n 1 77 GLU n 1 78 GLY n 1 79 THR n 1 80 TYR n 1 81 GLU n 1 82 CYS n 1 83 VAL n 1 84 VAL n 1 85 LEU n 1 86 LYS n 1 87 TYR n 1 88 GLU n 1 89 LYS n 1 90 ASP n 1 91 ALA n 1 92 PHE n 1 93 LYS n 1 94 ARG n 1 95 GLU n 1 96 HIS n 1 97 LEU n 1 98 ALA n 1 99 GLU n 1 100 VAL n 1 101 THR n 1 102 LEU n 1 103 SER n 1 104 VAL n 1 105 LYS n 1 106 ALA n 1 107 ASP n 1 108 PHE n 1 109 PRO n 1 110 THR n 1 111 PRO n 1 112 SER n 1 113 ILE n 1 114 SER n 1 115 ASP n 1 116 PHE n 1 117 GLU n 1 118 ILE n 1 119 PRO n 1 120 THR n 1 121 SER n 1 122 ASN n 1 123 ILE n 1 124 ARG n 1 125 ARG n 1 126 ILE n 1 127 ILE n 1 128 CYS n 1 129 SER n 1 130 THR n 1 131 SER n 1 132 GLY n 1 133 GLY n 1 134 PHE n 1 135 PRO n 1 136 GLU n 1 137 PRO n 1 138 HIS n 1 139 LEU n 1 140 SER n 1 141 TRP n 1 142 LEU n 1 143 GLU n 1 144 ASN n 1 145 GLY n 1 146 GLU n 1 147 GLU n 1 148 LEU n 1 149 ASN n 1 150 ALA n 1 151 ILE n 1 152 ASN n 1 153 THR n 1 154 THR n 1 155 VAL n 1 156 SER n 1 157 GLN n 1 158 ASP n 1 159 PRO n 1 160 GLU n 1 161 THR n 1 162 GLU n 1 163 LEU n 1 164 TYR n 1 165 ALA n 1 166 VAL n 1 167 SER n 1 168 SER n 1 169 LYS n 1 170 LEU n 1 171 ASP n 1 172 PHE n 1 173 ASN n 1 174 MET n 1 175 THR n 1 176 THR n 1 177 ASN n 1 178 HIS n 1 179 SER n 1 180 PHE n 1 181 MET n 1 182 CYS n 1 183 LEU n 1 184 ILE n 1 185 LYS n 1 186 TYR n 1 187 GLY n 1 188 HIS n 1 189 LEU n 1 190 ARG n 1 191 VAL n 1 192 ASN n 1 193 GLN n 1 194 THR n 1 195 PHE n 1 196 ASN n 1 197 TRP n 1 198 ASN n 1 199 THR n 1 200 ALA n 1 201 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus Homo _entity_src_gen.pdbx_gene_src_gene CHO _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 _entity_src_gen.host_org_genus Escherichia _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code CD80_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P33681 _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1DR9 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 201 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P33681 _struct_ref_seq.db_align_beg 35 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 234 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 201 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 1DR9 _struct_ref_seq_dif.mon_id ALA _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 200 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P33681 _struct_ref_seq_dif.db_mon_id THR _struct_ref_seq_dif.pdbx_seq_db_seq_num 234 _struct_ref_seq_dif.details ENGINEERED _struct_ref_seq_dif.pdbx_auth_seq_num 200 _struct_ref_seq_dif.pdbx_ordinal 1 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1DR9 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_percent_sol 53.85 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293.0 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_details 'PEG400, Na Hepes, CaCl2, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 20K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1998-11-24 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength . _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE BM14' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline BM14 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1DR9 _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 20 _reflns.d_resolution_high 3.0 _reflns.number_obs 5204 _reflns.number_all 105456 _reflns.percent_possible_obs 96.5 _reflns.pdbx_Rmerge_I_obs 0.114 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 24 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy .195 _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_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 3.0 _reflns_shell.d_res_low 3.1 _reflns_shell.percent_possible_all 88.9 _reflns_shell.Rmerge_I_obs 0.48 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 283 _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1DR9 _refine.ls_number_reflns_obs 5204 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 253290.04 _refine.pdbx_data_cutoff_low_absF 0.00 _refine.ls_d_res_low 19.55 _refine.ls_d_res_high 3.00 _refine.ls_percent_reflns_obs 96.5 _refine.ls_R_factor_obs 0.238 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.238 _refine.ls_R_factor_R_free 0.28 _refine.ls_R_factor_R_free_error 0.016 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.6 _refine.ls_number_reflns_R_free 289 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean 41.1 _refine.aniso_B[1][1] 11.91 _refine.aniso_B[2][2] 11.91 _refine.aniso_B[3][3] -23.83 _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 'FLAT MODEL' _refine.solvent_model_param_ksol 0.289 _refine.solvent_model_param_bsol 10 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1DR9 _refine_analyze.Luzzati_coordinate_error_obs 0.34 _refine_analyze.Luzzati_sigma_a_obs 0.36 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.42 _refine_analyze.Luzzati_sigma_a_free 0.45 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1603 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 42 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 1645 _refine_hist.d_res_high 3.00 _refine_hist.d_res_low 19.55 # 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 c_bond_d 0.008 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.4 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 26.7 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.73 ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.64 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 2.76 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.27 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.48 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 3.00 _refine_ls_shell.d_res_low 3.19 _refine_ls_shell.number_reflns_R_work 745 _refine_ls_shell.R_factor_R_work 0.291 _refine_ls_shell.percent_reflns_obs 92.1 _refine_ls_shell.R_factor_R_free 0.365 _refine_ls_shell.R_factor_R_free_error 0.049 _refine_ls_shell.percent_reflns_R_free 7.0 _refine_ls_shell.number_reflns_R_free 56 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PAR PROTEIN.TOP 'X-RAY DIFFRACTION' 2 CARBOHYDRATE.PAR CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1DR9 _struct.title 'CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)' _struct.pdbx_descriptor 'B7-1 (CD80), EXTRACELLULAR REGION' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1DR9 _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'IG SUPERFAMILY, IMMUNE SYSTEM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLU A 23 ? THR A 28 ? GLU A 23 THR A 28 1 ? 6 HELX_P HELX_P2 2 TRP A 50 ? ASN A 55 ? TRP A 50 ASN A 55 1 ? 6 HELX_P HELX_P3 3 ARG A 73 ? GLU A 77 ? ARG A 73 GLU A 77 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 16 SG ? ? ? 1_555 A CYS 82 SG ? ? A CYS 16 A CYS 82 1_555 ? ? ? ? ? ? ? 2.029 ? disulf2 disulf ? ? A CYS 128 SG ? ? ? 1_555 A CYS 182 SG ? ? A CYS 128 A CYS 182 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale ? ? A ASN 152 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 152 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.454 ? covale2 covale ? ? A ASN 192 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 192 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.445 ? covale3 covale ? ? A ASN 173 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 173 A NAG 1003 1_555 ? ? ? ? ? ? ? 1.457 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id PHE _struct_mon_prot_cis.label_seq_id 134 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id PHE _struct_mon_prot_cis.auth_seq_id 134 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 135 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 135 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 0.34 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 3 ? C ? 4 ? D ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 HIS A 3 ? GLU A 7 ? HIS A 3 GLU A 7 A 2 LYS A 93 ? LYS A 105 ? LYS A 93 LYS A 105 A 3 GLY A 78 ? LYS A 86 ? GLY A 78 LYS A 86 A 4 ARG A 29 ? LYS A 34 ? ARG A 29 LYS A 34 A 5 LYS A 37 ? MET A 43 ? LYS A 37 MET A 43 A 6 ASP A 46 ? ILE A 49 ? ASP A 46 ILE A 49 B 1 ALA A 12 ? LEU A 14 ? ALA A 12 LEU A 14 B 2 SER A 66 ? ILE A 69 ? SER A 66 ILE A 69 B 3 THR A 57 ? ASP A 60 ? THR A 57 ASP A 60 C 1 SER A 112 ? GLU A 117 ? SER A 112 GLU A 117 C 2 ILE A 123 ? GLY A 133 ? ILE A 123 GLY A 133 C 3 TYR A 164 ? ASN A 173 ? TYR A 164 ASN A 173 C 4 ASN A 152 ? GLN A 157 ? ASN A 152 GLN A 157 D 1 GLU A 147 ? LEU A 148 ? GLU A 147 LEU A 148 D 2 PRO A 137 ? GLU A 143 ? PRO A 137 GLU A 143 D 3 HIS A 178 ? TYR A 186 ? HIS A 178 TYR A 186 D 4 VAL A 191 ? TRP A 197 ? VAL A 191 TRP A 197 # 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 VAL A 4 ? N VAL A 4 O THR A 101 ? O THR A 101 A 2 3 N LEU A 102 ? N LEU A 102 O GLY A 78 ? O GLY A 78 A 3 4 N LEU A 85 ? N LEU A 85 O ARG A 29 ? O ARG A 29 A 4 5 N LYS A 34 ? N LYS A 34 O LYS A 37 ? O LYS A 37 A 5 6 O MET A 43 ? O MET A 43 N ASP A 46 ? N ASP A 46 B 1 2 N LEU A 14 ? N LEU A 14 O ILE A 67 ? O ILE A 67 B 2 3 N VAL A 68 ? N VAL A 68 O ILE A 58 ? O ILE A 58 C 1 2 O PHE A 116 ? O PHE A 116 N ARG A 125 ? N ARG A 125 C 2 3 N GLY A 132 ? N GLY A 132 O TYR A 164 ? O TYR A 164 C 3 4 N LYS A 169 ? N LYS A 169 O ASN A 152 ? O ASN A 152 D 1 2 N LEU A 148 ? N LEU A 148 O TRP A 141 ? O TRP A 141 D 2 3 N LEU A 142 ? N LEU A 142 O MET A 181 ? O MET A 181 D 3 4 N ILE A 184 ? N ILE A 184 O VAL A 191 ? O VAL A 191 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1001' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1002' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1003' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 3 ASN A 152 ? ASN A 152 . ? 1_555 ? 2 AC1 3 SER A 156 ? SER A 156 . ? 7_455 ? 3 AC1 3 LYS A 169 ? LYS A 169 . ? 1_555 ? 4 AC2 4 HIS A 188 ? HIS A 188 . ? 16_555 ? 5 AC2 4 LEU A 189 ? LEU A 189 . ? 16_555 ? 6 AC2 4 ARG A 190 ? ARG A 190 . ? 1_555 ? 7 AC2 4 ASN A 192 ? ASN A 192 . ? 1_555 ? 8 AC3 2 ASN A 173 ? ASN A 173 . ? 1_555 ? 9 AC3 2 THR A 175 ? THR A 175 . ? 1_555 ? # _database_PDB_matrix.entry_id 1DR9 _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 1DR9 _atom_sites.fract_transf_matrix[1][1] 0.017458 _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] 0.017458 _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] 0.003345 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . VAL A 1 1 ? 16.678 14.306 43.344 1.00 51.46 ? 1 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 16.137 14.225 44.731 1.00 53.23 ? 1 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 14.799 14.952 44.834 1.00 52.85 ? 1 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 14.530 15.880 44.074 1.00 54.71 ? 1 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 17.107 14.865 45.752 1.00 53.76 ? 1 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 16.678 14.514 47.166 1.00 56.32 ? 1 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 18.519 14.388 45.502 1.00 56.49 ? 1 VAL A CG2 1 ATOM 8 N N . ILE A 1 2 ? 13.963 14.520 45.771 1.00 52.09 ? 2 ILE A N 1 ATOM 9 C CA . ILE A 1 2 ? 12.668 15.152 45.989 1.00 52.92 ? 2 ILE A CA 1 ATOM 10 C C . ILE A 1 2 ? 12.854 16.184 47.097 1.00 53.60 ? 2 ILE A C 1 ATOM 11 O O . ILE A 1 2 ? 12.548 17.369 46.934 1.00 53.26 ? 2 ILE A O 1 ATOM 12 C CB . ILE A 1 2 ? 11.599 14.132 46.469 1.00 53.40 ? 2 ILE A CB 1 ATOM 13 C CG1 . ILE A 1 2 ? 11.395 13.032 45.418 1.00 53.55 ? 2 ILE A CG1 1 ATOM 14 C CG2 . ILE A 1 2 ? 10.292 14.854 46.764 1.00 51.78 ? 2 ILE A CG2 1 ATOM 15 C CD1 . ILE A 1 2 ? 10.597 11.825 45.918 1.00 49.65 ? 2 ILE A CD1 1 ATOM 16 N N . HIS A 1 3 ? 13.387 15.712 48.220 1.00 54.67 ? 3 HIS A N 1 ATOM 17 C CA . HIS A 1 3 ? 13.611 16.543 49.397 1.00 54.16 ? 3 HIS A CA 1 ATOM 18 C C . HIS A 1 3 ? 15.085 16.831 49.716 1.00 52.86 ? 3 HIS A C 1 ATOM 19 O O . HIS A 1 3 ? 15.973 16.018 49.455 1.00 52.46 ? 3 HIS A O 1 ATOM 20 C CB . HIS A 1 3 ? 12.949 15.863 50.596 1.00 55.62 ? 3 HIS A CB 1 ATOM 21 C CG . HIS A 1 3 ? 13.055 16.635 51.871 1.00 60.61 ? 3 HIS A CG 1 ATOM 22 N ND1 . HIS A 1 3 ? 12.624 17.939 51.988 1.00 63.51 ? 3 HIS A ND1 1 ATOM 23 C CD2 . HIS A 1 3 ? 13.511 16.276 53.093 1.00 63.14 ? 3 HIS A CD2 1 ATOM 24 C CE1 . HIS A 1 3 ? 12.809 18.350 53.230 1.00 63.88 ? 3 HIS A CE1 1 ATOM 25 N NE2 . HIS A 1 3 ? 13.346 17.360 53.920 1.00 64.67 ? 3 HIS A NE2 1 ATOM 26 N N . VAL A 1 4 ? 15.332 18.011 50.272 1.00 52.07 ? 4 VAL A N 1 ATOM 27 C CA . VAL A 1 4 ? 16.674 18.410 50.688 1.00 49.61 ? 4 VAL A CA 1 ATOM 28 C C . VAL A 1 4 ? 16.563 19.168 52.009 1.00 48.60 ? 4 VAL A C 1 ATOM 29 O O . VAL A 1 4 ? 15.637 19.965 52.207 1.00 48.45 ? 4 VAL A O 1 ATOM 30 C CB . VAL A 1 4 ? 17.370 19.325 49.665 1.00 49.12 ? 4 VAL A CB 1 ATOM 31 C CG1 . VAL A 1 4 ? 18.716 19.780 50.216 1.00 44.31 ? 4 VAL A CG1 1 ATOM 32 C CG2 . VAL A 1 4 ? 17.560 18.587 48.353 1.00 48.91 ? 4 VAL A CG2 1 ATOM 33 N N . THR A 1 5 ? 17.509 18.912 52.906 1.00 45.92 ? 5 THR A N 1 ATOM 34 C CA . THR A 1 5 ? 17.523 19.553 54.212 1.00 41.71 ? 5 THR A CA 1 ATOM 35 C C . THR A 1 5 ? 18.933 19.982 54.563 1.00 38.40 ? 5 THR A C 1 ATOM 36 O O . THR A 1 5 ? 19.828 19.157 54.652 1.00 38.09 ? 5 THR A O 1 ATOM 37 C CB . THR A 1 5 ? 17.039 18.591 55.312 1.00 42.29 ? 5 THR A CB 1 ATOM 38 O OG1 . THR A 1 5 ? 15.797 17.993 54.921 1.00 42.26 ? 5 THR A OG1 1 ATOM 39 C CG2 . THR A 1 5 ? 16.850 19.338 56.616 1.00 42.09 ? 5 THR A CG2 1 ATOM 40 N N . LYS A 1 6 ? 19.128 21.274 54.765 1.00 37.59 ? 6 LYS A N 1 ATOM 41 C CA . LYS A 1 6 ? 20.438 21.788 55.131 1.00 38.27 ? 6 LYS A CA 1 ATOM 42 C C . LYS A 1 6 ? 20.318 22.647 56.387 1.00 36.90 ? 6 LYS A C 1 ATOM 43 O O . LYS A 1 6 ? 19.213 22.964 56.822 1.00 36.69 ? 6 LYS A O 1 ATOM 44 C CB . LYS A 1 6 ? 21.015 22.612 53.976 1.00 40.15 ? 6 LYS A CB 1 ATOM 45 C CG . LYS A 1 6 ? 22.222 21.971 53.293 1.00 42.52 ? 6 LYS A CG 1 ATOM 46 C CD . LYS A 1 6 ? 21.899 20.589 52.760 1.00 42.27 ? 6 LYS A CD 1 ATOM 47 C CE . LYS A 1 6 ? 23.133 19.915 52.189 1.00 44.44 ? 6 LYS A CE 1 ATOM 48 N NZ . LYS A 1 6 ? 22.874 18.490 51.785 1.00 45.04 ? 6 LYS A NZ 1 ATOM 49 N N . GLU A 1 7 ? 21.450 23.008 56.981 1.00 35.97 ? 7 GLU A N 1 ATOM 50 C CA . GLU A 1 7 ? 21.436 23.855 58.172 1.00 35.50 ? 7 GLU A CA 1 ATOM 51 C C . GLU A 1 7 ? 21.512 25.313 57.715 1.00 35.40 ? 7 GLU A C 1 ATOM 52 O O . GLU A 1 7 ? 21.798 25.597 56.553 1.00 35.25 ? 7 GLU A O 1 ATOM 53 C CB . GLU A 1 7 ? 22.643 23.572 59.071 1.00 35.25 ? 7 GLU A CB 1 ATOM 54 C CG . GLU A 1 7 ? 22.770 22.165 59.626 1.00 38.75 ? 7 GLU A CG 1 ATOM 55 C CD . GLU A 1 7 ? 21.808 21.878 60.757 1.00 43.29 ? 7 GLU A CD 1 ATOM 56 O OE1 . GLU A 1 7 ? 22.102 20.972 61.570 1.00 45.61 ? 7 GLU A OE1 1 ATOM 57 O OE2 . GLU A 1 7 ? 20.756 22.546 60.833 1.00 46.05 ? 7 GLU A OE2 1 ATOM 58 N N . VAL A 1 8 ? 21.253 26.234 58.634 1.00 35.67 ? 8 VAL A N 1 ATOM 59 C CA . VAL A 1 8 ? 21.323 27.663 58.339 1.00 33.97 ? 8 VAL A CA 1 ATOM 60 C C . VAL A 1 8 ? 22.807 28.040 58.208 1.00 32.32 ? 8 VAL A C 1 ATOM 61 O O . VAL A 1 8 ? 23.663 27.459 58.872 1.00 32.57 ? 8 VAL A O 1 ATOM 62 C CB . VAL A 1 8 ? 20.693 28.492 59.494 1.00 34.10 ? 8 VAL A CB 1 ATOM 63 C CG1 . VAL A 1 8 ? 20.573 29.957 59.100 1.00 35.20 ? 8 VAL A CG1 1 ATOM 64 C CG2 . VAL A 1 8 ? 19.349 27.926 59.849 1.00 33.68 ? 8 VAL A CG2 1 ATOM 65 N N . LYS A 1 9 ? 23.106 29.013 57.359 1.00 30.35 ? 9 LYS A N 1 ATOM 66 C CA . LYS A 1 9 ? 24.479 29.457 57.148 1.00 29.42 ? 9 LYS A CA 1 ATOM 67 C C . LYS A 1 9 ? 25.234 28.503 56.215 1.00 29.25 ? 9 LYS A C 1 ATOM 68 O O . LYS A 1 9 ? 26.310 28.821 55.711 1.00 29.83 ? 9 LYS A O 1 ATOM 69 C CB . LYS A 1 9 ? 25.215 29.568 58.491 1.00 30.48 ? 9 LYS A CB 1 ATOM 70 C CG . LYS A 1 9 ? 24.561 30.493 59.524 1.00 30.49 ? 9 LYS A CG 1 ATOM 71 C CD . LYS A 1 9 ? 25.435 30.640 60.769 1.00 32.72 ? 9 LYS A CD 1 ATOM 72 C CE . LYS A 1 9 ? 24.731 31.444 61.865 1.00 40.24 ? 9 LYS A CE 1 ATOM 73 N NZ . LYS A 1 9 ? 25.391 31.354 63.222 1.00 41.67 ? 9 LYS A NZ 1 ATOM 74 N N . GLU A 1 10 ? 24.655 27.332 55.984 1.00 29.60 ? 10 GLU A N 1 ATOM 75 C CA . GLU A 1 10 ? 25.250 26.333 55.114 1.00 27.37 ? 10 GLU A CA 1 ATOM 76 C C . GLU A 1 10 ? 24.783 26.505 53.684 1.00 27.25 ? 10 GLU A C 1 ATOM 77 O O . GLU A 1 10 ? 23.878 27.284 53.401 1.00 29.85 ? 10 GLU A O 1 ATOM 78 C CB . GLU A 1 10 ? 24.900 24.941 55.618 1.00 29.71 ? 10 GLU A CB 1 ATOM 79 C CG . GLU A 1 10 ? 25.469 24.667 56.993 1.00 34.95 ? 10 GLU A CG 1 ATOM 80 C CD . GLU A 1 10 ? 25.490 23.196 57.344 1.00 39.33 ? 10 GLU A CD 1 ATOM 81 O OE1 . GLU A 1 10 ? 26.172 22.844 58.330 1.00 42.31 ? 10 GLU A OE1 1 ATOM 82 O OE2 . GLU A 1 10 ? 24.824 22.394 56.644 1.00 40.56 ? 10 GLU A OE2 1 ATOM 83 N N . VAL A 1 11 ? 25.405 25.759 52.784 1.00 27.79 ? 11 VAL A N 1 ATOM 84 C CA . VAL A 1 11 ? 25.106 25.817 51.359 1.00 27.38 ? 11 VAL A CA 1 ATOM 85 C C . VAL A 1 11 ? 24.106 24.764 50.909 1.00 28.68 ? 11 VAL A C 1 ATOM 86 O O . VAL A 1 11 ? 24.108 23.635 51.390 1.00 30.10 ? 11 VAL A O 1 ATOM 87 C CB . VAL A 1 11 ? 26.399 25.622 50.537 1.00 28.88 ? 11 VAL A CB 1 ATOM 88 C CG1 . VAL A 1 11 ? 26.072 25.359 49.094 1.00 29.95 ? 11 VAL A CG1 1 ATOM 89 C CG2 . VAL A 1 11 ? 27.289 26.837 50.664 1.00 30.84 ? 11 VAL A CG2 1 ATOM 90 N N . ALA A 1 12 ? 23.254 25.143 49.969 1.00 31.85 ? 12 ALA A N 1 ATOM 91 C CA . ALA A 1 12 ? 22.267 24.230 49.416 1.00 33.00 ? 12 ALA A CA 1 ATOM 92 C C . ALA A 1 12 ? 22.491 24.175 47.920 1.00 33.73 ? 12 ALA A C 1 ATOM 93 O O . ALA A 1 12 ? 22.455 25.201 47.244 1.00 34.23 ? 12 ALA A O 1 ATOM 94 C CB . ALA A 1 12 ? 20.864 24.710 49.712 1.00 31.13 ? 12 ALA A CB 1 ATOM 95 N N . THR A 1 13 ? 22.765 22.975 47.417 1.00 36.05 ? 13 THR A N 1 ATOM 96 C CA . THR A 1 13 ? 22.978 22.766 45.990 1.00 35.52 ? 13 THR A CA 1 ATOM 97 C C . THR A 1 13 ? 21.769 22.040 45.436 1.00 36.75 ? 13 THR A C 1 ATOM 98 O O . THR A 1 13 ? 21.554 20.864 45.737 1.00 37.66 ? 13 THR A O 1 ATOM 99 C CB . THR A 1 13 ? 24.208 21.901 45.704 1.00 32.83 ? 13 THR A CB 1 ATOM 100 O OG1 . THR A 1 13 ? 25.395 22.629 46.031 1.00 32.76 ? 13 THR A OG1 1 ATOM 101 C CG2 . THR A 1 13 ? 24.243 21.510 44.235 1.00 31.22 ? 13 THR A CG2 1 ATOM 102 N N . LEU A 1 14 ? 20.978 22.752 44.642 1.00 36.63 ? 14 LEU A N 1 ATOM 103 C CA . LEU A 1 14 ? 19.791 22.182 44.023 1.00 36.93 ? 14 LEU A CA 1 ATOM 104 C C . LEU A 1 14 ? 20.144 21.906 42.566 1.00 37.62 ? 14 LEU A C 1 ATOM 105 O O . LEU A 1 14 ? 20.338 22.833 41.768 1.00 36.21 ? 14 LEU A O 1 ATOM 106 C CB . LEU A 1 14 ? 18.632 23.173 44.115 1.00 38.19 ? 14 LEU A CB 1 ATOM 107 C CG . LEU A 1 14 ? 18.397 23.762 45.514 1.00 39.64 ? 14 LEU A CG 1 ATOM 108 C CD1 . LEU A 1 14 ? 17.469 24.980 45.412 1.00 38.81 ? 14 LEU A CD1 1 ATOM 109 C CD2 . LEU A 1 14 ? 17.824 22.695 46.444 1.00 35.69 ? 14 LEU A CD2 1 ATOM 110 N N . SER A 1 15 ? 20.249 20.623 42.233 1.00 37.15 ? 15 SER A N 1 ATOM 111 C CA . SER A 1 15 ? 20.595 20.206 40.880 1.00 37.42 ? 15 SER A CA 1 ATOM 112 C C . SER A 1 15 ? 19.382 20.210 39.964 1.00 37.26 ? 15 SER A C 1 ATOM 113 O O . SER A 1 15 ? 18.270 19.926 40.402 1.00 37.84 ? 15 SER A O 1 ATOM 114 C CB . SER A 1 15 ? 21.208 18.800 40.911 1.00 38.39 ? 15 SER A CB 1 ATOM 115 O OG . SER A 1 15 ? 21.541 18.334 39.613 1.00 39.21 ? 15 SER A OG 1 ATOM 116 N N . CYS A 1 16 ? 19.596 20.548 38.698 1.00 37.94 ? 16 CYS A N 1 ATOM 117 C CA . CYS A 1 16 ? 18.512 20.553 37.724 1.00 39.69 ? 16 CYS A CA 1 ATOM 118 C C . CYS A 1 16 ? 18.415 19.146 37.138 1.00 38.84 ? 16 CYS A C 1 ATOM 119 O O . CYS A 1 16 ? 17.585 18.883 36.275 1.00 38.89 ? 16 CYS A O 1 ATOM 120 C CB . CYS A 1 16 ? 18.791 21.556 36.600 1.00 42.93 ? 16 CYS A CB 1 ATOM 121 S SG . CYS A 1 16 ? 17.373 21.834 35.487 1.00 49.45 ? 16 CYS A SG 1 ATOM 122 N N . GLY A 1 17 ? 19.276 18.251 37.617 1.00 38.98 ? 17 GLY A N 1 ATOM 123 C CA . GLY A 1 17 ? 19.289 16.881 37.137 1.00 40.06 ? 17 GLY A CA 1 ATOM 124 C C . GLY A 1 17 ? 19.465 16.790 35.635 1.00 42.86 ? 17 GLY A C 1 ATOM 125 O O . GLY A 1 17 ? 19.014 15.829 35.014 1.00 42.94 ? 17 GLY A O 1 ATOM 126 N N . HIS A 1 18 ? 20.143 17.785 35.062 1.00 45.39 ? 18 HIS A N 1 ATOM 127 C CA . HIS A 1 18 ? 20.371 17.869 33.618 1.00 46.84 ? 18 HIS A CA 1 ATOM 128 C C . HIS A 1 18 ? 21.607 18.720 33.297 1.00 46.79 ? 18 HIS A C 1 ATOM 129 O O . HIS A 1 18 ? 21.880 19.707 33.978 1.00 48.23 ? 18 HIS A O 1 ATOM 130 C CB . HIS A 1 18 ? 19.138 18.497 32.966 1.00 48.43 ? 18 HIS A CB 1 ATOM 131 C CG . HIS A 1 18 ? 19.147 18.465 31.471 1.00 51.28 ? 18 HIS A CG 1 ATOM 132 N ND1 . HIS A 1 18 ? 19.113 17.289 30.750 1.00 53.84 ? 18 HIS A ND1 1 ATOM 133 C CD2 . HIS A 1 18 ? 19.134 19.465 30.560 1.00 51.98 ? 18 HIS A CD2 1 ATOM 134 C CE1 . HIS A 1 18 ? 19.076 17.568 29.460 1.00 54.59 ? 18 HIS A CE1 1 ATOM 135 N NE2 . HIS A 1 18 ? 19.088 18.881 29.318 1.00 54.87 ? 18 HIS A NE2 1 ATOM 136 N N . ASN A 1 19 ? 22.347 18.353 32.255 1.00 46.43 ? 19 ASN A N 1 ATOM 137 C CA . ASN A 1 19 ? 23.539 19.110 31.874 1.00 45.85 ? 19 ASN A CA 1 ATOM 138 C C . ASN A 1 19 ? 23.448 19.590 30.413 1.00 45.57 ? 19 ASN A C 1 ATOM 139 O O . ASN A 1 19 ? 22.772 18.967 29.588 1.00 45.04 ? 19 ASN A O 1 ATOM 140 C CB . ASN A 1 19 ? 24.791 18.243 32.078 1.00 45.77 ? 19 ASN A CB 1 ATOM 141 C CG . ASN A 1 19 ? 26.039 19.072 32.319 1.00 47.05 ? 19 ASN A CG 1 ATOM 142 O OD1 . ASN A 1 19 ? 26.117 19.814 33.294 1.00 48.94 ? 19 ASN A OD1 1 ATOM 143 N ND2 . ASN A 1 19 ? 27.021 18.952 31.431 1.00 48.65 ? 19 ASN A ND2 1 ATOM 144 N N . VAL A 1 20 ? 24.123 20.696 30.097 1.00 43.90 ? 20 VAL A N 1 ATOM 145 C CA . VAL A 1 20 ? 24.104 21.252 28.745 1.00 44.56 ? 20 VAL A CA 1 ATOM 146 C C . VAL A 1 20 ? 25.452 21.874 28.372 1.00 47.69 ? 20 VAL A C 1 ATOM 147 O O . VAL A 1 20 ? 25.945 22.755 29.084 1.00 49.95 ? 20 VAL A O 1 ATOM 148 C CB . VAL A 1 20 ? 23.014 22.355 28.610 1.00 43.73 ? 20 VAL A CB 1 ATOM 149 C CG1 . VAL A 1 20 ? 23.085 23.007 27.239 1.00 43.48 ? 20 VAL A CG1 1 ATOM 150 C CG2 . VAL A 1 20 ? 21.634 21.765 28.831 1.00 41.79 ? 20 VAL A CG2 1 ATOM 151 N N . SER A 1 21 ? 26.032 21.429 27.253 1.00 47.97 ? 21 SER A N 1 ATOM 152 C CA . SER A 1 21 ? 27.322 21.942 26.759 1.00 47.45 ? 21 SER A CA 1 ATOM 153 C C . SER A 1 21 ? 27.255 23.452 26.456 1.00 47.45 ? 21 SER A C 1 ATOM 154 O O . SER A 1 21 ? 26.163 23.997 26.297 1.00 47.74 ? 21 SER A O 1 ATOM 155 C CB . SER A 1 21 ? 27.729 21.190 25.488 1.00 46.86 ? 21 SER A CB 1 ATOM 156 O OG . SER A 1 21 ? 26.888 21.536 24.404 1.00 46.80 ? 21 SER A OG 1 ATOM 157 N N . VAL A 1 22 ? 28.410 24.119 26.361 1.00 46.44 ? 22 VAL A N 1 ATOM 158 C CA . VAL A 1 22 ? 28.440 25.562 26.097 1.00 47.88 ? 22 VAL A CA 1 ATOM 159 C C . VAL A 1 22 ? 27.942 25.968 24.705 1.00 49.21 ? 22 VAL A C 1 ATOM 160 O O . VAL A 1 22 ? 27.479 27.097 24.505 1.00 46.28 ? 22 VAL A O 1 ATOM 161 C CB . VAL A 1 22 ? 29.855 26.164 26.306 1.00 47.24 ? 22 VAL A CB 1 ATOM 162 C CG1 . VAL A 1 22 ? 30.372 25.825 27.683 1.00 47.49 ? 22 VAL A CG1 1 ATOM 163 C CG2 . VAL A 1 22 ? 30.798 25.664 25.252 1.00 50.26 ? 22 VAL A CG2 1 ATOM 164 N N . GLU A 1 23 ? 28.034 25.051 23.748 1.00 52.33 ? 23 GLU A N 1 ATOM 165 C CA . GLU A 1 23 ? 27.576 25.321 22.389 1.00 55.68 ? 23 GLU A CA 1 ATOM 166 C C . GLU A 1 23 ? 26.054 25.394 22.389 1.00 56.40 ? 23 GLU A C 1 ATOM 167 O O . GLU A 1 23 ? 25.454 26.254 21.733 1.00 56.56 ? 23 GLU A O 1 ATOM 168 C CB . GLU A 1 23 ? 28.027 24.206 21.450 1.00 57.42 ? 23 GLU A CB 1 ATOM 169 C CG . GLU A 1 23 ? 29.524 24.026 21.393 1.00 62.88 ? 23 GLU A CG 1 ATOM 170 C CD . GLU A 1 23 ? 29.915 22.567 21.450 1.00 67.12 ? 23 GLU A CD 1 ATOM 171 O OE1 . GLU A 1 23 ? 29.574 21.902 22.455 1.00 68.73 ? 23 GLU A OE1 1 ATOM 172 O OE2 . GLU A 1 23 ? 30.558 22.081 20.492 1.00 69.65 ? 23 GLU A OE2 1 ATOM 173 N N . GLU A 1 24 ? 25.439 24.482 23.136 1.00 55.83 ? 24 GLU A N 1 ATOM 174 C CA . GLU A 1 24 ? 23.990 24.420 23.241 1.00 54.01 ? 24 GLU A CA 1 ATOM 175 C C . GLU A 1 24 ? 23.441 25.517 24.139 1.00 52.57 ? 24 GLU A C 1 ATOM 176 O O . GLU A 1 24 ? 22.276 25.887 24.019 1.00 51.36 ? 24 GLU A O 1 ATOM 177 C CB . GLU A 1 24 ? 23.568 23.057 23.777 1.00 54.24 ? 24 GLU A CB 1 ATOM 178 C CG . GLU A 1 24 ? 23.914 21.914 22.859 1.00 55.60 ? 24 GLU A CG 1 ATOM 179 C CD . GLU A 1 24 ? 23.436 20.587 23.395 1.00 58.65 ? 24 GLU A CD 1 ATOM 180 O OE1 . GLU A 1 24 ? 22.221 20.453 23.658 1.00 60.28 ? 24 GLU A OE1 1 ATOM 181 O OE2 . GLU A 1 24 ? 24.273 19.674 23.554 1.00 61.26 ? 24 GLU A OE2 1 ATOM 182 N N . LEU A 1 25 ? 24.278 26.029 25.039 1.00 51.89 ? 25 LEU A N 1 ATOM 183 C CA . LEU A 1 25 ? 23.868 27.094 25.950 1.00 52.44 ? 25 LEU A CA 1 ATOM 184 C C . LEU A 1 25 ? 23.272 28.245 25.172 1.00 53.40 ? 25 LEU A C 1 ATOM 185 O O . LEU A 1 25 ? 22.428 28.981 25.681 1.00 54.71 ? 25 LEU A O 1 ATOM 186 C CB . LEU A 1 25 ? 25.052 27.616 26.754 1.00 51.54 ? 25 LEU A CB 1 ATOM 187 C CG . LEU A 1 25 ? 25.465 26.840 27.997 1.00 50.23 ? 25 LEU A CG 1 ATOM 188 C CD1 . LEU A 1 25 ? 26.592 27.598 28.683 1.00 48.10 ? 25 LEU A CD1 1 ATOM 189 C CD2 . LEU A 1 25 ? 24.273 26.671 28.926 1.00 48.32 ? 25 LEU A CD2 1 ATOM 190 N N . ALA A 1 26 ? 23.738 28.409 23.941 1.00 53.54 ? 26 ALA A N 1 ATOM 191 C CA . ALA A 1 26 ? 23.234 29.456 23.077 1.00 54.14 ? 26 ALA A CA 1 ATOM 192 C C . ALA A 1 26 ? 21.745 29.193 22.831 1.00 54.93 ? 26 ALA A C 1 ATOM 193 O O . ALA A 1 26 ? 20.898 29.982 23.231 1.00 55.05 ? 26 ALA A O 1 ATOM 194 C CB . ALA A 1 26 ? 23.999 29.451 21.767 1.00 54.84 ? 26 ALA A CB 1 ATOM 195 N N . GLN A 1 27 ? 21.434 28.062 22.203 1.00 55.46 ? 27 GLN A N 1 ATOM 196 C CA . GLN A 1 27 ? 20.054 27.696 21.892 1.00 56.70 ? 27 GLN A CA 1 ATOM 197 C C . GLN A 1 27 ? 19.179 27.239 23.048 1.00 55.84 ? 27 GLN A C 1 ATOM 198 O O . GLN A 1 27 ? 17.994 26.973 22.843 1.00 57.71 ? 27 GLN A O 1 ATOM 199 C CB . GLN A 1 27 ? 20.012 26.583 20.841 1.00 60.76 ? 27 GLN A CB 1 ATOM 200 C CG . GLN A 1 27 ? 20.114 27.030 19.391 1.00 65.85 ? 27 GLN A CG 1 ATOM 201 C CD . GLN A 1 27 ? 19.329 26.116 18.465 1.00 66.63 ? 27 GLN A CD 1 ATOM 202 O OE1 . GLN A 1 27 ? 18.100 26.171 18.418 1.00 66.42 ? 27 GLN A OE1 1 ATOM 203 N NE2 . GLN A 1 27 ? 20.036 25.256 17.741 1.00 68.01 ? 27 GLN A NE2 1 ATOM 204 N N . THR A 1 28 ? 19.732 27.127 24.250 1.00 53.45 ? 28 THR A N 1 ATOM 205 C CA . THR A 1 28 ? 18.927 26.647 25.372 1.00 50.86 ? 28 THR A CA 1 ATOM 206 C C . THR A 1 28 ? 18.399 27.736 26.289 1.00 49.63 ? 28 THR A C 1 ATOM 207 O O . THR A 1 28 ? 19.031 28.776 26.470 1.00 49.27 ? 28 THR A O 1 ATOM 208 C CB . THR A 1 28 ? 19.714 25.611 26.240 1.00 49.01 ? 28 THR A CB 1 ATOM 209 O OG1 . THR A 1 28 ? 20.103 24.499 25.430 1.00 51.62 ? 28 THR A OG1 1 ATOM 210 C CG2 . THR A 1 28 ? 18.853 25.079 27.363 1.00 46.74 ? 28 THR A CG2 1 ATOM 211 N N . ARG A 1 29 ? 17.220 27.482 26.850 1.00 48.16 ? 29 ARG A N 1 ATOM 212 C CA . ARG A 1 29 ? 16.590 28.390 27.795 1.00 47.95 ? 29 ARG A CA 1 ATOM 213 C C . ARG A 1 29 ? 16.438 27.637 29.112 1.00 47.06 ? 29 ARG A C 1 ATOM 214 O O . ARG A 1 29 ? 16.010 26.479 29.113 1.00 45.28 ? 29 ARG A O 1 ATOM 215 C CB . ARG A 1 29 ? 15.220 28.854 27.285 1.00 49.21 ? 29 ARG A CB 1 ATOM 216 C CG . ARG A 1 29 ? 15.323 29.978 26.284 1.00 52.10 ? 29 ARG A CG 1 ATOM 217 C CD . ARG A 1 29 ? 13.976 30.537 25.871 1.00 55.28 ? 29 ARG A CD 1 ATOM 218 N NE . ARG A 1 29 ? 14.161 31.707 25.014 1.00 58.46 ? 29 ARG A NE 1 ATOM 219 C CZ . ARG A 1 29 ? 13.175 32.414 24.474 1.00 59.09 ? 29 ARG A CZ 1 ATOM 220 N NH1 . ARG A 1 29 ? 11.912 32.073 24.693 1.00 60.04 ? 29 ARG A NH1 1 ATOM 221 N NH2 . ARG A 1 29 ? 13.459 33.474 23.726 1.00 59.54 ? 29 ARG A NH2 1 ATOM 222 N N . ILE A 1 30 ? 16.793 28.294 30.222 1.00 46.56 ? 30 ILE A N 1 ATOM 223 C CA . ILE A 1 30 ? 16.719 27.694 31.559 1.00 44.60 ? 30 ILE A CA 1 ATOM 224 C C . ILE A 1 30 ? 15.919 28.530 32.556 1.00 45.35 ? 30 ILE A C 1 ATOM 225 O O . ILE A 1 30 ? 16.268 29.665 32.855 1.00 46.50 ? 30 ILE A O 1 ATOM 226 C CB . ILE A 1 30 ? 18.120 27.488 32.133 1.00 41.27 ? 30 ILE A CB 1 ATOM 227 C CG1 . ILE A 1 30 ? 19.022 26.874 31.061 1.00 41.54 ? 30 ILE A CG1 1 ATOM 228 C CG2 . ILE A 1 30 ? 18.047 26.585 33.341 1.00 38.74 ? 30 ILE A CG2 1 ATOM 229 C CD1 . ILE A 1 30 ? 20.464 26.785 31.440 1.00 41.44 ? 30 ILE A CD1 1 ATOM 230 N N . TYR A 1 31 ? 14.850 27.953 33.084 1.00 46.62 ? 31 TYR A N 1 ATOM 231 C CA . TYR A 1 31 ? 14.005 28.654 34.039 1.00 47.90 ? 31 TYR A CA 1 ATOM 232 C C . TYR A 1 31 ? 14.049 28.088 35.448 1.00 49.10 ? 31 TYR A C 1 ATOM 233 O O . TYR A 1 31 ? 13.415 27.062 35.733 1.00 50.27 ? 31 TYR A O 1 ATOM 234 C CB . TYR A 1 31 ? 12.543 28.625 33.591 1.00 48.63 ? 31 TYR A CB 1 ATOM 235 C CG . TYR A 1 31 ? 12.183 29.578 32.488 1.00 51.41 ? 31 TYR A CG 1 ATOM 236 C CD1 . TYR A 1 31 ? 11.173 29.262 31.578 1.00 53.10 ? 31 TYR A CD1 1 ATOM 237 C CD2 . TYR A 1 31 ? 12.827 30.807 32.360 1.00 51.81 ? 31 TYR A CD2 1 ATOM 238 C CE1 . TYR A 1 31 ? 10.814 30.146 30.561 1.00 52.31 ? 31 TYR A CE1 1 ATOM 239 C CE2 . TYR A 1 31 ? 12.473 31.703 31.346 1.00 51.75 ? 31 TYR A CE2 1 ATOM 240 C CZ . TYR A 1 31 ? 11.468 31.362 30.451 1.00 52.26 ? 31 TYR A CZ 1 ATOM 241 O OH . TYR A 1 31 ? 11.121 32.230 29.443 1.00 53.29 ? 31 TYR A OH 1 ATOM 242 N N . TRP A 1 32 ? 14.789 28.750 36.331 1.00 47.31 ? 32 TRP A N 1 ATOM 243 C CA . TRP A 1 32 ? 14.820 28.330 37.727 1.00 43.37 ? 32 TRP A CA 1 ATOM 244 C C . TRP A 1 32 ? 13.852 29.259 38.442 1.00 41.49 ? 32 TRP A C 1 ATOM 245 O O . TRP A 1 32 ? 13.893 30.477 38.273 1.00 40.01 ? 32 TRP A O 1 ATOM 246 C CB . TRP A 1 32 ? 16.210 28.489 38.347 1.00 40.65 ? 32 TRP A CB 1 ATOM 247 C CG . TRP A 1 32 ? 17.031 27.227 38.393 1.00 35.85 ? 32 TRP A CG 1 ATOM 248 C CD1 . TRP A 1 32 ? 18.192 26.979 37.715 1.00 32.20 ? 32 TRP A CD1 1 ATOM 249 C CD2 . TRP A 1 32 ? 16.786 26.072 39.197 1.00 32.17 ? 32 TRP A CD2 1 ATOM 250 N NE1 . TRP A 1 32 ? 18.685 25.749 38.056 1.00 30.02 ? 32 TRP A NE1 1 ATOM 251 C CE2 . TRP A 1 32 ? 17.843 25.167 38.964 1.00 30.48 ? 32 TRP A CE2 1 ATOM 252 C CE3 . TRP A 1 32 ? 15.775 25.714 40.097 1.00 31.08 ? 32 TRP A CE3 1 ATOM 253 C CZ2 . TRP A 1 32 ? 17.921 23.921 39.595 1.00 32.38 ? 32 TRP A CZ2 1 ATOM 254 C CZ3 . TRP A 1 32 ? 15.850 24.466 40.732 1.00 32.41 ? 32 TRP A CZ3 1 ATOM 255 C CH2 . TRP A 1 32 ? 16.918 23.588 40.476 1.00 33.05 ? 32 TRP A CH2 1 ATOM 256 N N . GLN A 1 33 ? 12.947 28.683 39.207 1.00 40.30 ? 33 GLN A N 1 ATOM 257 C CA . GLN A 1 33 ? 12.024 29.498 39.946 1.00 40.65 ? 33 GLN A CA 1 ATOM 258 C C . GLN A 1 33 ? 11.655 28.802 41.231 1.00 41.56 ? 33 GLN A C 1 ATOM 259 O O . GLN A 1 33 ? 11.731 27.570 41.347 1.00 38.65 ? 33 GLN A O 1 ATOM 260 C CB . GLN A 1 33 ? 10.774 29.810 39.125 1.00 42.37 ? 33 GLN A CB 1 ATOM 261 C CG . GLN A 1 33 ? 9.980 28.606 38.656 1.00 46.59 ? 33 GLN A CG 1 ATOM 262 C CD . GLN A 1 33 ? 8.690 29.014 37.969 1.00 48.21 ? 33 GLN A CD 1 ATOM 263 O OE1 . GLN A 1 33 ? 8.699 29.755 36.977 1.00 46.30 ? 33 GLN A OE1 1 ATOM 264 N NE2 . GLN A 1 33 ? 7.567 28.542 38.500 1.00 49.23 ? 33 GLN A NE2 1 ATOM 265 N N . LYS A 1 34 ? 11.290 29.623 42.205 1.00 42.13 ? 34 LYS A N 1 ATOM 266 C CA . LYS A 1 34 ? 10.895 29.151 43.508 1.00 42.53 ? 34 LYS A CA 1 ATOM 267 C C . LYS A 1 34 ? 9.413 29.415 43.596 1.00 43.80 ? 34 LYS A C 1 ATOM 268 O O . LYS A 1 34 ? 8.986 30.564 43.588 1.00 45.41 ? 34 LYS A O 1 ATOM 269 C CB . LYS A 1 34 ? 11.634 29.927 44.599 1.00 41.00 ? 34 LYS A CB 1 ATOM 270 C CG . LYS A 1 34 ? 11.314 29.479 46.017 1.00 40.31 ? 34 LYS A CG 1 ATOM 271 C CD . LYS A 1 34 ? 12.031 30.367 47.006 1.00 40.24 ? 34 LYS A CD 1 ATOM 272 C CE . LYS A 1 34 ? 11.505 30.233 48.422 1.00 39.46 ? 34 LYS A CE 1 ATOM 273 N NZ . LYS A 1 34 ? 12.297 31.137 49.310 1.00 38.51 ? 34 LYS A NZ 1 ATOM 274 N N . GLU A 1 35 ? 8.639 28.337 43.644 1.00 45.29 ? 35 GLU A N 1 ATOM 275 C CA . GLU A 1 35 ? 7.189 28.402 43.755 1.00 45.66 ? 35 GLU A CA 1 ATOM 276 C C . GLU A 1 35 ? 6.538 29.490 42.903 1.00 46.98 ? 35 GLU A C 1 ATOM 277 O O . GLU A 1 35 ? 5.995 30.477 43.411 1.00 44.47 ? 35 GLU A O 1 ATOM 278 C CB . GLU A 1 35 ? 6.836 28.530 45.235 1.00 44.76 ? 35 GLU A CB 1 ATOM 279 C CG . GLU A 1 35 ? 7.575 27.461 46.040 1.00 49.16 ? 35 GLU A CG 1 ATOM 280 C CD . GLU A 1 35 ? 7.218 27.416 47.508 1.00 50.57 ? 35 GLU A CD 1 ATOM 281 O OE1 . GLU A 1 35 ? 7.420 28.436 48.200 1.00 52.96 ? 35 GLU A OE1 1 ATOM 282 O OE2 . GLU A 1 35 ? 6.747 26.350 47.970 1.00 50.98 ? 35 GLU A OE2 1 ATOM 283 N N . LYS A 1 36 ? 6.614 29.283 41.589 1.00 49.97 ? 36 LYS A N 1 ATOM 284 C CA . LYS A 1 36 ? 6.046 30.189 40.594 1.00 53.24 ? 36 LYS A CA 1 ATOM 285 C C . LYS A 1 36 ? 6.790 31.528 40.490 1.00 54.27 ? 36 LYS A C 1 ATOM 286 O O . LYS A 1 36 ? 6.799 32.148 39.424 1.00 55.64 ? 36 LYS A O 1 ATOM 287 C CB . LYS A 1 36 ? 4.555 30.441 40.886 1.00 56.38 ? 36 LYS A CB 1 ATOM 288 C CG . LYS A 1 36 ? 3.687 29.187 41.126 1.00 55.67 ? 36 LYS A CG 1 ATOM 289 C CD . LYS A 1 36 ? 3.538 28.291 39.890 1.00 55.37 ? 36 LYS A CD 1 ATOM 290 C CE . LYS A 1 36 ? 4.708 27.326 39.727 1.00 54.04 ? 36 LYS A CE 1 ATOM 291 N NZ . LYS A 1 36 ? 4.626 26.534 38.465 1.00 51.91 ? 36 LYS A NZ 1 ATOM 292 N N . LYS A 1 37 ? 7.400 31.976 41.587 1.00 54.57 ? 37 LYS A N 1 ATOM 293 C CA . LYS A 1 37 ? 8.163 33.232 41.600 1.00 54.29 ? 37 LYS A CA 1 ATOM 294 C C . LYS A 1 37 ? 9.592 33.005 41.061 1.00 53.46 ? 37 LYS A C 1 ATOM 295 O O . LYS A 1 37 ? 10.386 32.303 41.681 1.00 53.30 ? 37 LYS A O 1 ATOM 296 C CB . LYS A 1 37 ? 8.227 33.779 43.027 1.00 55.18 ? 37 LYS A CB 1 ATOM 297 C CG . LYS A 1 37 ? 9.092 35.019 43.189 1.00 59.28 ? 37 LYS A CG 1 ATOM 298 C CD . LYS A 1 37 ? 9.017 35.580 44.616 1.00 60.66 ? 37 LYS A CD 1 ATOM 299 C CE . LYS A 1 37 ? 9.672 34.662 45.649 1.00 62.16 ? 37 LYS A CE 1 ATOM 300 N NZ . LYS A 1 37 ? 11.160 34.650 45.574 1.00 61.10 ? 37 LYS A NZ 1 ATOM 301 N N . MET A 1 38 ? 9.907 33.600 39.909 1.00 51.60 ? 38 MET A N 1 ATOM 302 C CA . MET A 1 38 ? 11.218 33.446 39.272 1.00 49.62 ? 38 MET A CA 1 ATOM 303 C C . MET A 1 38 ? 12.422 33.706 40.176 1.00 48.08 ? 38 MET A C 1 ATOM 304 O O . MET A 1 38 ? 12.329 34.437 41.162 1.00 48.46 ? 38 MET A O 1 ATOM 305 C CB . MET A 1 38 ? 11.325 34.359 38.044 1.00 51.13 ? 38 MET A CB 1 ATOM 306 C CG . MET A 1 38 ? 10.379 34.016 36.896 1.00 51.54 ? 38 MET A CG 1 ATOM 307 S SD . MET A 1 38 ? 10.705 32.422 36.134 1.00 50.61 ? 38 MET A SD 1 ATOM 308 C CE . MET A 1 38 ? 12.354 32.707 35.536 1.00 47.10 ? 38 MET A CE 1 ATOM 309 N N . VAL A 1 39 ? 13.550 33.095 39.810 1.00 45.01 ? 39 VAL A N 1 ATOM 310 C CA . VAL A 1 39 ? 14.812 33.221 40.533 1.00 40.74 ? 39 VAL A CA 1 ATOM 311 C C . VAL A 1 39 ? 15.877 33.723 39.558 1.00 41.68 ? 39 VAL A C 1 ATOM 312 O O . VAL A 1 39 ? 16.417 34.821 39.712 1.00 42.62 ? 39 VAL A O 1 ATOM 313 C CB . VAL A 1 39 ? 15.268 31.860 41.107 1.00 38.40 ? 39 VAL A CB 1 ATOM 314 C CG1 . VAL A 1 39 ? 16.682 31.957 41.617 1.00 37.22 ? 39 VAL A CG1 1 ATOM 315 C CG2 . VAL A 1 39 ? 14.349 31.432 42.236 1.00 36.78 ? 39 VAL A CG2 1 ATOM 316 N N . LEU A 1 40 ? 16.170 32.915 38.548 1.00 42.30 ? 40 LEU A N 1 ATOM 317 C CA . LEU A 1 40 ? 17.161 33.280 37.545 1.00 41.00 ? 40 LEU A CA 1 ATOM 318 C C . LEU A 1 40 ? 16.708 32.828 36.160 1.00 40.65 ? 40 LEU A C 1 ATOM 319 O O . LEU A 1 40 ? 15.860 31.952 36.019 1.00 41.14 ? 40 LEU A O 1 ATOM 320 C CB . LEU A 1 40 ? 18.522 32.667 37.904 1.00 40.33 ? 40 LEU A CB 1 ATOM 321 C CG . LEU A 1 40 ? 19.217 31.641 37.000 1.00 39.44 ? 40 LEU A CG 1 ATOM 322 C CD1 . LEU A 1 40 ? 20.513 31.264 37.670 1.00 40.86 ? 40 LEU A CD1 1 ATOM 323 C CD2 . LEU A 1 40 ? 18.367 30.399 36.778 1.00 37.63 ? 40 LEU A CD2 1 ATOM 324 N N . THR A 1 41 ? 17.301 33.426 35.139 1.00 40.41 ? 41 THR A N 1 ATOM 325 C CA . THR A 1 41 ? 16.961 33.132 33.764 1.00 38.62 ? 41 THR A CA 1 ATOM 326 C C . THR A 1 41 ? 18.223 33.127 32.914 1.00 39.94 ? 41 THR A C 1 ATOM 327 O O . THR A 1 41 ? 18.951 34.119 32.880 1.00 40.85 ? 41 THR A O 1 ATOM 328 C CB . THR A 1 41 ? 15.999 34.210 33.246 1.00 39.89 ? 41 THR A CB 1 ATOM 329 O OG1 . THR A 1 41 ? 14.657 33.841 33.574 1.00 37.21 ? 41 THR A OG1 1 ATOM 330 C CG2 . THR A 1 41 ? 16.154 34.423 31.745 1.00 42.27 ? 41 THR A CG2 1 ATOM 331 N N . MET A 1 42 ? 18.480 32.011 32.235 1.00 40.24 ? 42 MET A N 1 ATOM 332 C CA . MET A 1 42 ? 19.649 31.879 31.362 1.00 40.85 ? 42 MET A CA 1 ATOM 333 C C . MET A 1 42 ? 19.121 31.846 29.933 1.00 43.38 ? 42 MET A C 1 ATOM 334 O O . MET A 1 42 ? 19.376 30.917 29.172 1.00 45.67 ? 42 MET A O 1 ATOM 335 C CB . MET A 1 42 ? 20.413 30.586 31.689 1.00 39.76 ? 42 MET A CB 1 ATOM 336 C CG . MET A 1 42 ? 21.668 30.312 30.850 1.00 37.48 ? 42 MET A CG 1 ATOM 337 S SD . MET A 1 42 ? 22.983 31.531 31.007 1.00 35.03 ? 42 MET A SD 1 ATOM 338 C CE . MET A 1 42 ? 22.848 32.334 29.521 1.00 35.77 ? 42 MET A CE 1 ATOM 339 N N . MET A 1 43 ? 18.372 32.882 29.585 1.00 46.29 ? 43 MET A N 1 ATOM 340 C CA . MET A 1 43 ? 17.763 33.012 28.270 1.00 47.41 ? 43 MET A CA 1 ATOM 341 C C . MET A 1 43 ? 18.754 32.977 27.116 1.00 49.77 ? 43 MET A C 1 ATOM 342 O O . MET A 1 43 ? 19.379 33.987 26.788 1.00 49.94 ? 43 MET A O 1 ATOM 343 C CB . MET A 1 43 ? 16.975 34.323 28.189 1.00 46.66 ? 43 MET A CB 1 ATOM 344 C CG . MET A 1 43 ? 15.549 34.182 27.710 1.00 41.32 ? 43 MET A CG 1 ATOM 345 S SD . MET A 1 43 ? 14.491 33.634 29.025 1.00 39.13 ? 43 MET A SD 1 ATOM 346 C CE . MET A 1 43 ? 14.730 31.853 28.910 1.00 39.93 ? 43 MET A CE 1 ATOM 347 N N . SER A 1 44 ? 18.892 31.813 26.500 1.00 52.82 ? 44 SER A N 1 ATOM 348 C CA . SER A 1 44 ? 19.765 31.658 25.344 1.00 55.39 ? 44 SER A CA 1 ATOM 349 C C . SER A 1 44 ? 21.039 32.502 25.329 1.00 56.19 ? 44 SER A C 1 ATOM 350 O O . SER A 1 44 ? 21.139 33.457 24.563 1.00 57.29 ? 44 SER A O 1 ATOM 351 C CB . SER A 1 44 ? 18.956 31.951 24.081 1.00 56.25 ? 44 SER A CB 1 ATOM 352 O OG . SER A 1 44 ? 19.796 32.095 22.956 1.00 59.93 ? 44 SER A OG 1 ATOM 353 N N . GLY A 1 45 ? 22.008 32.149 26.170 1.00 57.62 ? 45 GLY A N 1 ATOM 354 C CA . GLY A 1 45 ? 23.274 32.871 26.201 1.00 56.23 ? 45 GLY A CA 1 ATOM 355 C C . GLY A 1 45 ? 23.382 33.996 27.212 1.00 55.24 ? 45 GLY A C 1 ATOM 356 O O . GLY A 1 45 ? 24.446 34.227 27.793 1.00 54.72 ? 45 GLY A O 1 ATOM 357 N N . ASP A 1 46 ? 22.266 34.676 27.443 1.00 55.04 ? 46 ASP A N 1 ATOM 358 C CA . ASP A 1 46 ? 22.206 35.806 28.365 1.00 55.07 ? 46 ASP A CA 1 ATOM 359 C C . ASP A 1 46 ? 21.517 35.442 29.674 1.00 53.18 ? 46 ASP A C 1 ATOM 360 O O . ASP A 1 46 ? 20.358 35.030 29.687 1.00 53.57 ? 46 ASP A O 1 ATOM 361 C CB . ASP A 1 46 ? 21.462 36.947 27.680 1.00 56.95 ? 46 ASP A CB 1 ATOM 362 C CG . ASP A 1 46 ? 21.555 36.854 26.166 1.00 60.66 ? 46 ASP A CG 1 ATOM 363 O OD1 . ASP A 1 46 ? 22.694 36.827 25.639 1.00 59.66 ? 46 ASP A OD1 1 ATOM 364 O OD2 . ASP A 1 46 ? 20.494 36.788 25.500 1.00 62.77 ? 46 ASP A OD2 1 ATOM 365 N N . MET A 1 47 ? 22.230 35.593 30.779 1.00 51.00 ? 47 MET A N 1 ATOM 366 C CA . MET A 1 47 ? 21.650 35.268 32.069 1.00 49.61 ? 47 MET A CA 1 ATOM 367 C C . MET A 1 47 ? 21.168 36.509 32.800 1.00 50.15 ? 47 MET A C 1 ATOM 368 O O . MET A 1 47 ? 21.657 37.615 32.564 1.00 49.55 ? 47 MET A O 1 ATOM 369 C CB . MET A 1 47 ? 22.661 34.530 32.937 1.00 47.31 ? 47 MET A CB 1 ATOM 370 C CG . MET A 1 47 ? 22.799 35.103 34.319 1.00 44.13 ? 47 MET A CG 1 ATOM 371 S SD . MET A 1 47 ? 22.889 33.814 35.507 1.00 43.22 ? 47 MET A SD 1 ATOM 372 C CE . MET A 1 47 ? 21.482 34.172 36.463 1.00 44.46 ? 47 MET A CE 1 ATOM 373 N N . ASN A 1 48 ? 20.203 36.314 33.691 1.00 50.20 ? 48 ASN A N 1 ATOM 374 C CA . ASN A 1 48 ? 19.666 37.414 34.466 1.00 49.35 ? 48 ASN A CA 1 ATOM 375 C C . ASN A 1 48 ? 18.921 36.884 35.690 1.00 48.17 ? 48 ASN A C 1 ATOM 376 O O . ASN A 1 48 ? 17.821 36.346 35.584 1.00 48.69 ? 48 ASN A O 1 ATOM 377 C CB . ASN A 1 48 ? 18.752 38.269 33.586 1.00 49.83 ? 48 ASN A CB 1 ATOM 378 C CG . ASN A 1 48 ? 18.856 39.750 33.905 1.00 52.08 ? 48 ASN A CG 1 ATOM 379 O OD1 . ASN A 1 48 ? 18.425 40.599 33.121 1.00 51.95 ? 48 ASN A OD1 1 ATOM 380 N ND2 . ASN A 1 48 ? 19.427 40.069 35.066 1.00 52.15 ? 48 ASN A ND2 1 ATOM 381 N N . ILE A 1 49 ? 19.557 37.032 36.848 1.00 46.39 ? 49 ILE A N 1 ATOM 382 C CA . ILE A 1 49 ? 19.011 36.595 38.125 1.00 45.22 ? 49 ILE A CA 1 ATOM 383 C C . ILE A 1 49 ? 18.247 37.770 38.729 1.00 46.46 ? 49 ILE A C 1 ATOM 384 O O . ILE A 1 49 ? 18.706 38.915 38.675 1.00 44.77 ? 49 ILE A O 1 ATOM 385 C CB . ILE A 1 49 ? 20.160 36.153 39.073 1.00 44.67 ? 49 ILE A CB 1 ATOM 386 C CG1 . ILE A 1 49 ? 19.616 35.744 40.439 1.00 42.86 ? 49 ILE A CG1 1 ATOM 387 C CG2 . ILE A 1 49 ? 21.171 37.268 39.217 1.00 42.71 ? 49 ILE A CG2 1 ATOM 388 C CD1 . ILE A 1 49 ? 20.704 35.263 41.380 1.00 39.85 ? 49 ILE A CD1 1 ATOM 389 N N . TRP A 1 50 ? 17.070 37.494 39.284 1.00 47.78 ? 50 TRP A N 1 ATOM 390 C CA . TRP A 1 50 ? 16.259 38.555 39.876 1.00 49.45 ? 50 TRP A CA 1 ATOM 391 C C . TRP A 1 50 ? 16.936 39.173 41.096 1.00 49.46 ? 50 TRP A C 1 ATOM 392 O O . TRP A 1 50 ? 17.693 38.502 41.803 1.00 49.35 ? 50 TRP A O 1 ATOM 393 C CB . TRP A 1 50 ? 14.867 38.035 40.263 1.00 48.67 ? 50 TRP A CB 1 ATOM 394 C CG . TRP A 1 50 ? 13.850 38.098 39.145 1.00 48.06 ? 50 TRP A CG 1 ATOM 395 C CD1 . TRP A 1 50 ? 12.602 38.641 39.211 1.00 47.19 ? 50 TRP A CD1 1 ATOM 396 C CD2 . TRP A 1 50 ? 13.975 37.551 37.823 1.00 46.92 ? 50 TRP A CD2 1 ATOM 397 N NE1 . TRP A 1 50 ? 11.939 38.465 38.022 1.00 44.49 ? 50 TRP A NE1 1 ATOM 398 C CE2 . TRP A 1 50 ? 12.758 37.795 37.152 1.00 43.75 ? 50 TRP A CE2 1 ATOM 399 C CE3 . TRP A 1 50 ? 14.999 36.873 37.144 1.00 45.13 ? 50 TRP A CE3 1 ATOM 400 C CZ2 . TRP A 1 50 ? 12.530 37.388 35.838 1.00 41.07 ? 50 TRP A CZ2 1 ATOM 401 C CZ3 . TRP A 1 50 ? 14.773 36.469 35.833 1.00 43.91 ? 50 TRP A CZ3 1 ATOM 402 C CH2 . TRP A 1 50 ? 13.545 36.727 35.196 1.00 42.27 ? 50 TRP A CH2 1 ATOM 403 N N . PRO A 1 51 ? 16.657 40.462 41.361 1.00 48.68 ? 51 PRO A N 1 ATOM 404 C CA . PRO A 1 51 ? 17.229 41.199 42.491 1.00 47.94 ? 51 PRO A CA 1 ATOM 405 C C . PRO A 1 51 ? 17.076 40.453 43.813 1.00 47.75 ? 51 PRO A C 1 ATOM 406 O O . PRO A 1 51 ? 18.013 40.379 44.611 1.00 47.79 ? 51 PRO A O 1 ATOM 407 C CB . PRO A 1 51 ? 16.444 42.510 42.478 1.00 48.24 ? 51 PRO A CB 1 ATOM 408 C CG . PRO A 1 51 ? 16.100 42.685 41.022 1.00 47.37 ? 51 PRO A CG 1 ATOM 409 C CD . PRO A 1 51 ? 15.680 41.296 40.635 1.00 46.82 ? 51 PRO A CD 1 ATOM 410 N N . GLU A 1 52 ? 15.886 39.903 44.037 1.00 46.58 ? 52 GLU A N 1 ATOM 411 C CA . GLU A 1 52 ? 15.597 39.172 45.263 1.00 44.89 ? 52 GLU A CA 1 ATOM 412 C C . GLU A 1 52 ? 16.712 38.156 45.519 1.00 43.02 ? 52 GLU A C 1 ATOM 413 O O . GLU A 1 52 ? 17.091 37.920 46.668 1.00 39.41 ? 52 GLU A O 1 ATOM 414 C CB . GLU A 1 52 ? 14.235 38.463 45.132 1.00 46.57 ? 52 GLU A CB 1 ATOM 415 C CG . GLU A 1 52 ? 13.388 38.399 46.409 1.00 48.54 ? 52 GLU A CG 1 ATOM 416 C CD . GLU A 1 52 ? 13.837 37.317 47.396 1.00 53.13 ? 52 GLU A CD 1 ATOM 417 O OE1 . GLU A 1 52 ? 15.043 37.271 47.741 1.00 53.16 ? 52 GLU A OE1 1 ATOM 418 O OE2 . GLU A 1 52 ? 12.977 36.516 47.839 1.00 52.00 ? 52 GLU A OE2 1 ATOM 419 N N . TYR A 1 53 ? 17.252 37.594 44.433 1.00 41.92 ? 53 TYR A N 1 ATOM 420 C CA . TYR A 1 53 ? 18.298 36.572 44.507 1.00 40.87 ? 53 TYR A CA 1 ATOM 421 C C . TYR A 1 53 ? 19.730 36.937 44.118 1.00 41.09 ? 53 TYR A C 1 ATOM 422 O O . TYR A 1 53 ? 20.665 36.210 44.452 1.00 40.22 ? 53 TYR A O 1 ATOM 423 C CB . TYR A 1 53 ? 17.880 35.368 43.676 1.00 38.44 ? 53 TYR A CB 1 ATOM 424 C CG . TYR A 1 53 ? 16.725 34.619 44.264 1.00 38.55 ? 53 TYR A CG 1 ATOM 425 C CD1 . TYR A 1 53 ? 15.412 35.019 44.027 1.00 37.07 ? 53 TYR A CD1 1 ATOM 426 C CD2 . TYR A 1 53 ? 16.944 33.524 45.096 1.00 40.66 ? 53 TYR A CD2 1 ATOM 427 C CE1 . TYR A 1 53 ? 14.349 34.348 44.609 1.00 39.15 ? 53 TYR A CE1 1 ATOM 428 C CE2 . TYR A 1 53 ? 15.890 32.847 45.686 1.00 40.25 ? 53 TYR A CE2 1 ATOM 429 C CZ . TYR A 1 53 ? 14.599 33.264 45.441 1.00 40.46 ? 53 TYR A CZ 1 ATOM 430 O OH . TYR A 1 53 ? 13.567 32.603 46.056 1.00 46.18 ? 53 TYR A OH 1 ATOM 431 N N . LYS A 1 54 ? 19.901 38.045 43.411 1.00 41.93 ? 54 LYS A N 1 ATOM 432 C CA . LYS A 1 54 ? 21.218 38.473 42.959 1.00 43.01 ? 54 LYS A CA 1 ATOM 433 C C . LYS A 1 54 ? 22.346 38.205 43.953 1.00 45.21 ? 54 LYS A C 1 ATOM 434 O O . LYS A 1 54 ? 23.396 37.669 43.589 1.00 45.95 ? 54 LYS A O 1 ATOM 435 C CB . LYS A 1 54 ? 21.195 39.968 42.618 1.00 42.12 ? 54 LYS A CB 1 ATOM 436 C CG . LYS A 1 54 ? 20.803 40.849 43.792 1.00 44.19 ? 54 LYS A CG 1 ATOM 437 C CD . LYS A 1 54 ? 20.940 42.335 43.476 1.00 48.02 ? 54 LYS A CD 1 ATOM 438 C CE . LYS A 1 54 ? 20.627 43.196 44.710 1.00 48.35 ? 54 LYS A CE 1 ATOM 439 N NZ . LYS A 1 54 ? 20.905 44.654 44.512 1.00 47.83 ? 54 LYS A NZ 1 ATOM 440 N N . ASN A 1 55 ? 22.117 38.556 45.214 1.00 45.83 ? 55 ASN A N 1 ATOM 441 C CA . ASN A 1 55 ? 23.141 38.413 46.242 1.00 43.99 ? 55 ASN A CA 1 ATOM 442 C C . ASN A 1 55 ? 23.615 37.032 46.707 1.00 41.89 ? 55 ASN A C 1 ATOM 443 O O . ASN A 1 55 ? 24.784 36.714 46.548 1.00 44.50 ? 55 ASN A O 1 ATOM 444 C CB . ASN A 1 55 ? 22.740 39.256 47.456 1.00 46.51 ? 55 ASN A CB 1 ATOM 445 C CG . ASN A 1 55 ? 22.865 40.758 47.195 1.00 50.15 ? 55 ASN A CG 1 ATOM 446 O OD1 . ASN A 1 55 ? 22.485 41.585 48.037 1.00 50.88 ? 55 ASN A OD1 1 ATOM 447 N ND2 . ASN A 1 55 ? 23.408 41.116 46.031 1.00 48.50 ? 55 ASN A ND2 1 ATOM 448 N N . ARG A 1 56 ? 22.735 36.204 47.261 1.00 39.11 ? 56 ARG A N 1 ATOM 449 C CA . ARG A 1 56 ? 23.163 34.906 47.777 1.00 36.73 ? 56 ARG A CA 1 ATOM 450 C C . ARG A 1 56 ? 23.081 33.677 46.877 1.00 38.95 ? 56 ARG A C 1 ATOM 451 O O . ARG A 1 56 ? 23.345 32.564 47.347 1.00 40.12 ? 56 ARG A O 1 ATOM 452 C CB . ARG A 1 56 ? 22.412 34.602 49.074 1.00 33.54 ? 56 ARG A CB 1 ATOM 453 C CG . ARG A 1 56 ? 22.689 35.585 50.214 1.00 35.99 ? 56 ARG A CG 1 ATOM 454 C CD . ARG A 1 56 ? 21.914 35.242 51.493 1.00 36.41 ? 56 ARG A CD 1 ATOM 455 N NE . ARG A 1 56 ? 20.499 35.009 51.215 1.00 41.01 ? 56 ARG A NE 1 ATOM 456 C CZ . ARG A 1 56 ? 19.939 33.807 51.080 1.00 41.21 ? 56 ARG A CZ 1 ATOM 457 N NH1 . ARG A 1 56 ? 20.672 32.709 51.214 1.00 38.88 ? 56 ARG A NH1 1 ATOM 458 N NH2 . ARG A 1 56 ? 18.649 33.703 50.771 1.00 41.17 ? 56 ARG A NH2 1 ATOM 459 N N . THR A 1 57 ? 22.745 33.847 45.596 1.00 38.60 ? 57 THR A N 1 ATOM 460 C CA . THR A 1 57 ? 22.613 32.688 44.695 1.00 36.35 ? 57 THR A CA 1 ATOM 461 C C . THR A 1 57 ? 23.609 32.572 43.539 1.00 36.39 ? 57 THR A C 1 ATOM 462 O O . THR A 1 57 ? 23.852 33.531 42.806 1.00 35.81 ? 57 THR A O 1 ATOM 463 C CB . THR A 1 57 ? 21.192 32.618 44.103 1.00 35.05 ? 57 THR A CB 1 ATOM 464 O OG1 . THR A 1 57 ? 20.231 32.612 45.166 1.00 32.54 ? 57 THR A OG1 1 ATOM 465 C CG2 . THR A 1 57 ? 21.023 31.355 43.270 1.00 33.79 ? 57 THR A CG2 1 ATOM 466 N N . ILE A 1 58 ? 24.168 31.375 43.381 1.00 36.36 ? 58 ILE A N 1 ATOM 467 C CA . ILE A 1 58 ? 25.145 31.093 42.329 1.00 37.11 ? 58 ILE A CA 1 ATOM 468 C C . ILE A 1 58 ? 24.568 30.130 41.298 1.00 38.27 ? 58 ILE A C 1 ATOM 469 O O . ILE A 1 58 ? 23.897 29.162 41.653 1.00 39.29 ? 58 ILE A O 1 ATOM 470 C CB . ILE A 1 58 ? 26.427 30.435 42.902 1.00 35.86 ? 58 ILE A CB 1 ATOM 471 C CG1 . ILE A 1 58 ? 27.111 31.374 43.900 1.00 36.86 ? 58 ILE A CG1 1 ATOM 472 C CG2 . ILE A 1 58 ? 27.363 30.046 41.774 1.00 32.97 ? 58 ILE A CG2 1 ATOM 473 C CD1 . ILE A 1 58 ? 27.582 32.689 43.323 1.00 35.85 ? 58 ILE A CD1 1 ATOM 474 N N . PHE A 1 59 ? 24.835 30.387 40.023 1.00 38.55 ? 59 PHE A N 1 ATOM 475 C CA . PHE A 1 59 ? 24.349 29.499 38.974 1.00 38.63 ? 59 PHE A CA 1 ATOM 476 C C . PHE A 1 59 ? 25.512 28.660 38.457 1.00 38.97 ? 59 PHE A C 1 ATOM 477 O O . PHE A 1 59 ? 26.348 29.128 37.674 1.00 36.52 ? 59 PHE A O 1 ATOM 478 C CB . PHE A 1 59 ? 23.709 30.291 37.831 1.00 36.72 ? 59 PHE A CB 1 ATOM 479 C CG . PHE A 1 59 ? 23.033 29.432 36.799 1.00 32.71 ? 59 PHE A CG 1 ATOM 480 C CD1 . PHE A 1 59 ? 22.441 28.223 37.160 1.00 32.01 ? 59 PHE A CD1 1 ATOM 481 C CD2 . PHE A 1 59 ? 22.955 29.847 35.476 1.00 33.21 ? 59 PHE A CD2 1 ATOM 482 C CE1 . PHE A 1 59 ? 21.775 27.436 36.221 1.00 31.70 ? 59 PHE A CE1 1 ATOM 483 C CE2 . PHE A 1 59 ? 22.289 29.067 34.523 1.00 34.49 ? 59 PHE A CE2 1 ATOM 484 C CZ . PHE A 1 59 ? 21.698 27.856 34.898 1.00 32.24 ? 59 PHE A CZ 1 ATOM 485 N N . ASP A 1 60 ? 25.549 27.419 38.930 1.00 38.64 ? 60 ASP A N 1 ATOM 486 C CA . ASP A 1 60 ? 26.580 26.463 38.577 1.00 38.91 ? 60 ASP A CA 1 ATOM 487 C C . ASP A 1 60 ? 26.209 25.750 37.280 1.00 39.77 ? 60 ASP A C 1 ATOM 488 O O . ASP A 1 60 ? 25.638 24.651 37.297 1.00 38.88 ? 60 ASP A O 1 ATOM 489 C CB . ASP A 1 60 ? 26.736 25.446 39.707 1.00 38.81 ? 60 ASP A CB 1 ATOM 490 C CG . ASP A 1 60 ? 28.008 24.641 39.595 1.00 39.18 ? 60 ASP A CG 1 ATOM 491 O OD1 . ASP A 1 60 ? 28.298 24.151 38.487 1.00 43.83 ? 60 ASP A OD1 1 ATOM 492 O OD2 . ASP A 1 60 ? 28.714 24.491 40.609 1.00 35.97 ? 60 ASP A OD2 1 ATOM 493 N N . ILE A 1 61 ? 26.533 26.389 36.160 1.00 38.61 ? 61 ILE A N 1 ATOM 494 C CA . ILE A 1 61 ? 26.258 25.836 34.838 1.00 37.68 ? 61 ILE A CA 1 ATOM 495 C C . ILE A 1 61 ? 26.944 24.483 34.662 1.00 37.04 ? 61 ILE A C 1 ATOM 496 O O . ILE A 1 61 ? 26.309 23.499 34.316 1.00 36.80 ? 61 ILE A O 1 ATOM 497 C CB . ILE A 1 61 ? 26.750 26.794 33.727 1.00 36.58 ? 61 ILE A CB 1 ATOM 498 C CG1 . ILE A 1 61 ? 25.934 28.094 33.764 1.00 35.28 ? 61 ILE A CG1 1 ATOM 499 C CG2 . ILE A 1 61 ? 26.648 26.111 32.372 1.00 34.57 ? 61 ILE A CG2 1 ATOM 500 C CD1 . ILE A 1 61 ? 26.437 29.180 32.829 1.00 32.79 ? 61 ILE A CD1 1 ATOM 501 N N . THR A 1 62 ? 28.244 24.449 34.918 1.00 38.00 ? 62 THR A N 1 ATOM 502 C CA . THR A 1 62 ? 29.045 23.235 34.793 1.00 39.44 ? 62 THR A CA 1 ATOM 503 C C . THR A 1 62 ? 28.473 22.015 35.524 1.00 41.23 ? 62 THR A C 1 ATOM 504 O O . THR A 1 62 ? 28.636 20.884 35.076 1.00 40.47 ? 62 THR A O 1 ATOM 505 C CB . THR A 1 62 ? 30.466 23.462 35.342 1.00 38.28 ? 62 THR A CB 1 ATOM 506 O OG1 . THR A 1 62 ? 30.990 24.688 34.831 1.00 38.81 ? 62 THR A OG1 1 ATOM 507 C CG2 . THR A 1 62 ? 31.374 22.323 34.939 1.00 36.27 ? 62 THR A CG2 1 ATOM 508 N N . ASN A 1 63 ? 27.816 22.252 36.653 1.00 43.07 ? 63 ASN A N 1 ATOM 509 C CA . ASN A 1 63 ? 27.252 21.180 37.463 1.00 45.13 ? 63 ASN A CA 1 ATOM 510 C C . ASN A 1 63 ? 25.753 20.951 37.293 1.00 45.99 ? 63 ASN A C 1 ATOM 511 O O . ASN A 1 63 ? 24.976 21.202 38.221 1.00 47.56 ? 63 ASN A O 1 ATOM 512 C CB . ASN A 1 63 ? 27.548 21.449 38.939 1.00 48.51 ? 63 ASN A CB 1 ATOM 513 C CG . ASN A 1 63 ? 28.883 20.893 39.376 1.00 50.94 ? 63 ASN A CG 1 ATOM 514 O OD1 . ASN A 1 63 ? 29.061 19.675 39.434 1.00 53.51 ? 63 ASN A OD1 1 ATOM 515 N ND2 . ASN A 1 63 ? 29.833 21.776 39.685 1.00 50.51 ? 63 ASN A ND2 1 ATOM 516 N N . ASN A 1 64 ? 25.345 20.469 36.125 1.00 43.99 ? 64 ASN A N 1 ATOM 517 C CA . ASN A 1 64 ? 23.933 20.200 35.877 1.00 43.51 ? 64 ASN A CA 1 ATOM 518 C C . ASN A 1 64 ? 23.044 21.420 36.026 1.00 43.08 ? 64 ASN A C 1 ATOM 519 O O . ASN A 1 64 ? 21.898 21.296 36.454 1.00 44.27 ? 64 ASN A O 1 ATOM 520 C CB . ASN A 1 64 ? 23.417 19.118 36.831 1.00 44.19 ? 64 ASN A CB 1 ATOM 521 C CG . ASN A 1 64 ? 23.791 17.720 36.393 1.00 45.66 ? 64 ASN A CG 1 ATOM 522 O OD1 . ASN A 1 64 ? 23.735 16.782 37.181 1.00 47.64 ? 64 ASN A OD1 1 ATOM 523 N ND2 . ASN A 1 64 ? 24.162 17.569 35.127 1.00 48.28 ? 64 ASN A ND2 1 ATOM 524 N N . LEU A 1 65 ? 23.564 22.598 35.698 1.00 40.78 ? 65 LEU A N 1 ATOM 525 C CA . LEU A 1 65 ? 22.763 23.816 35.793 1.00 37.79 ? 65 LEU A CA 1 ATOM 526 C C . LEU A 1 65 ? 22.157 24.061 37.179 1.00 35.26 ? 65 LEU A C 1 ATOM 527 O O . LEU A 1 65 ? 21.093 24.655 37.288 1.00 34.33 ? 65 LEU A O 1 ATOM 528 C CB . LEU A 1 65 ? 21.638 23.753 34.752 1.00 35.67 ? 65 LEU A CB 1 ATOM 529 C CG . LEU A 1 65 ? 22.151 23.519 33.328 1.00 32.85 ? 65 LEU A CG 1 ATOM 530 C CD1 . LEU A 1 65 ? 21.016 23.076 32.426 1.00 31.49 ? 65 LEU A CD1 1 ATOM 531 C CD2 . LEU A 1 65 ? 22.807 24.792 32.807 1.00 28.25 ? 65 LEU A CD2 1 ATOM 532 N N . SER A 1 66 ? 22.837 23.617 38.231 1.00 34.56 ? 66 SER A N 1 ATOM 533 C CA . SER A 1 66 ? 22.330 23.785 39.590 1.00 34.66 ? 66 SER A CA 1 ATOM 534 C C . SER A 1 66 ? 22.393 25.228 40.067 1.00 35.83 ? 66 SER A C 1 ATOM 535 O O . SER A 1 66 ? 23.096 26.060 39.490 1.00 37.54 ? 66 SER A O 1 ATOM 536 C CB . SER A 1 66 ? 23.136 22.933 40.571 1.00 31.92 ? 66 SER A CB 1 ATOM 537 O OG . SER A 1 66 ? 23.145 21.574 40.200 1.00 34.94 ? 66 SER A OG 1 ATOM 538 N N . ILE A 1 67 ? 21.634 25.517 41.121 1.00 33.18 ? 67 ILE A N 1 ATOM 539 C CA . ILE A 1 67 ? 21.648 26.826 41.740 1.00 30.35 ? 67 ILE A CA 1 ATOM 540 C C . ILE A 1 67 ? 22.083 26.541 43.172 1.00 33.20 ? 67 ILE A C 1 ATOM 541 O O . ILE A 1 67 ? 21.493 25.705 43.862 1.00 33.90 ? 67 ILE A O 1 ATOM 542 C CB . ILE A 1 67 ? 20.272 27.482 41.749 1.00 30.07 ? 67 ILE A CB 1 ATOM 543 C CG1 . ILE A 1 67 ? 19.246 26.565 42.407 1.00 32.30 ? 67 ILE A CG1 1 ATOM 544 C CG2 . ILE A 1 67 ? 19.855 27.797 40.350 1.00 31.75 ? 67 ILE A CG2 1 ATOM 545 C CD1 . ILE A 1 67 ? 17.944 27.278 42.769 1.00 31.30 ? 67 ILE A CD1 1 ATOM 546 N N . VAL A 1 68 ? 23.140 27.213 43.606 1.00 33.37 ? 68 VAL A N 1 ATOM 547 C CA . VAL A 1 68 ? 23.680 27.026 44.941 1.00 31.66 ? 68 VAL A CA 1 ATOM 548 C C . VAL A 1 68 ? 23.295 28.207 45.808 1.00 32.68 ? 68 VAL A C 1 ATOM 549 O O . VAL A 1 68 ? 23.642 29.346 45.494 1.00 35.71 ? 68 VAL A O 1 ATOM 550 C CB . VAL A 1 68 ? 25.212 26.943 44.888 1.00 31.34 ? 68 VAL A CB 1 ATOM 551 C CG1 . VAL A 1 68 ? 25.783 26.903 46.284 1.00 31.30 ? 68 VAL A CG1 1 ATOM 552 C CG2 . VAL A 1 68 ? 25.631 25.728 44.103 1.00 30.90 ? 68 VAL A CG2 1 ATOM 553 N N . ILE A 1 69 ? 22.577 27.947 46.894 1.00 30.54 ? 69 ILE A N 1 ATOM 554 C CA . ILE A 1 69 ? 22.187 29.025 47.786 1.00 29.45 ? 69 ILE A CA 1 ATOM 555 C C . ILE A 1 69 ? 23.221 29.065 48.891 1.00 29.99 ? 69 ILE A C 1 ATOM 556 O O . ILE A 1 69 ? 23.343 28.124 49.666 1.00 30.07 ? 69 ILE A O 1 ATOM 557 C CB . ILE A 1 69 ? 20.795 28.785 48.381 1.00 29.79 ? 69 ILE A CB 1 ATOM 558 C CG1 . ILE A 1 69 ? 19.801 28.498 47.249 1.00 28.27 ? 69 ILE A CG1 1 ATOM 559 C CG2 . ILE A 1 69 ? 20.354 30.014 49.179 1.00 26.73 ? 69 ILE A CG2 1 ATOM 560 C CD1 . ILE A 1 69 ? 18.398 28.189 47.722 1.00 24.20 ? 69 ILE A CD1 1 ATOM 561 N N . LEU A 1 70 ? 23.979 30.155 48.945 1.00 29.70 ? 70 LEU A N 1 ATOM 562 C CA . LEU A 1 70 ? 25.033 30.313 49.943 1.00 27.97 ? 70 LEU A CA 1 ATOM 563 C C . LEU A 1 70 ? 24.491 30.971 51.187 1.00 27.19 ? 70 LEU A C 1 ATOM 564 O O . LEU A 1 70 ? 23.662 31.861 51.097 1.00 30.58 ? 70 LEU A O 1 ATOM 565 C CB . LEU A 1 70 ? 26.156 31.205 49.405 1.00 27.68 ? 70 LEU A CB 1 ATOM 566 C CG . LEU A 1 70 ? 26.732 31.031 48.003 1.00 28.72 ? 70 LEU A CG 1 ATOM 567 C CD1 . LEU A 1 70 ? 27.772 32.113 47.755 1.00 23.31 ? 70 LEU A CD1 1 ATOM 568 C CD2 . LEU A 1 70 ? 27.330 29.641 47.862 1.00 29.36 ? 70 LEU A CD2 1 ATOM 569 N N . ALA A 1 71 ? 24.964 30.555 52.352 1.00 26.35 ? 71 ALA A N 1 ATOM 570 C CA . ALA A 1 71 ? 24.513 31.186 53.586 1.00 24.87 ? 71 ALA A CA 1 ATOM 571 C C . ALA A 1 71 ? 23.003 31.063 53.710 1.00 25.42 ? 71 ALA A C 1 ATOM 572 O O . ALA A 1 71 ? 22.291 32.066 53.720 1.00 25.84 ? 71 ALA A O 1 ATOM 573 C CB . ALA A 1 71 ? 24.923 32.665 53.582 1.00 19.08 ? 71 ALA A CB 1 ATOM 574 N N . LEU A 1 72 ? 22.518 29.831 53.800 1.00 26.97 ? 72 LEU A N 1 ATOM 575 C CA . LEU A 1 72 ? 21.083 29.575 53.907 1.00 28.17 ? 72 LEU A CA 1 ATOM 576 C C . LEU A 1 72 ? 20.334 30.385 54.972 1.00 28.83 ? 72 LEU A C 1 ATOM 577 O O . LEU A 1 72 ? 20.851 30.684 56.044 1.00 32.07 ? 72 LEU A O 1 ATOM 578 C CB . LEU A 1 72 ? 20.840 28.084 54.150 1.00 27.39 ? 72 LEU A CB 1 ATOM 579 C CG . LEU A 1 72 ? 20.277 27.289 52.971 1.00 29.14 ? 72 LEU A CG 1 ATOM 580 C CD1 . LEU A 1 72 ? 21.143 27.523 51.767 1.00 29.71 ? 72 LEU A CD1 1 ATOM 581 C CD2 . LEU A 1 72 ? 20.228 25.799 53.305 1.00 32.86 ? 72 LEU A CD2 1 ATOM 582 N N . ARG A 1 73 ? 19.110 30.759 54.657 1.00 28.38 ? 73 ARG A N 1 ATOM 583 C CA . ARG A 1 73 ? 18.290 31.482 55.607 1.00 29.16 ? 73 ARG A CA 1 ATOM 584 C C . ARG A 1 73 ? 17.012 30.680 55.760 1.00 32.23 ? 73 ARG A C 1 ATOM 585 O O . ARG A 1 73 ? 16.559 30.012 54.825 1.00 33.70 ? 73 ARG A O 1 ATOM 586 C CB . ARG A 1 73 ? 17.971 32.867 55.093 1.00 26.82 ? 73 ARG A CB 1 ATOM 587 C CG . ARG A 1 73 ? 19.069 33.835 55.307 1.00 30.41 ? 73 ARG A CG 1 ATOM 588 C CD . ARG A 1 73 ? 18.824 35.062 54.476 1.00 36.47 ? 73 ARG A CD 1 ATOM 589 N NE . ARG A 1 73 ? 19.792 36.117 54.742 1.00 40.64 ? 73 ARG A NE 1 ATOM 590 C CZ . ARG A 1 73 ? 19.781 37.289 54.127 1.00 42.30 ? 73 ARG A CZ 1 ATOM 591 N NH1 . ARG A 1 73 ? 18.847 37.532 53.219 1.00 46.20 ? 73 ARG A NH1 1 ATOM 592 N NH2 . ARG A 1 73 ? 20.694 38.210 54.415 1.00 45.63 ? 73 ARG A NH2 1 ATOM 593 N N . PRO A 1 74 ? 16.405 30.729 56.942 1.00 32.96 ? 74 PRO A N 1 ATOM 594 C CA . PRO A 1 74 ? 15.174 29.959 57.101 1.00 35.01 ? 74 PRO A CA 1 ATOM 595 C C . PRO A 1 74 ? 14.103 30.179 56.030 1.00 34.75 ? 74 PRO A C 1 ATOM 596 O O . PRO A 1 74 ? 13.250 29.319 55.836 1.00 37.30 ? 74 PRO A O 1 ATOM 597 C CB . PRO A 1 74 ? 14.706 30.346 58.504 1.00 33.73 ? 74 PRO A CB 1 ATOM 598 C CG . PRO A 1 74 ? 15.317 31.680 58.731 1.00 34.56 ? 74 PRO A CG 1 ATOM 599 C CD . PRO A 1 74 ? 16.684 31.541 58.134 1.00 32.92 ? 74 PRO A CD 1 ATOM 600 N N . SER A 1 75 ? 14.161 31.300 55.319 1.00 34.03 ? 75 SER A N 1 ATOM 601 C CA . SER A 1 75 ? 13.152 31.595 54.305 1.00 35.36 ? 75 SER A CA 1 ATOM 602 C C . SER A 1 75 ? 13.424 30.959 52.949 1.00 36.32 ? 75 SER A C 1 ATOM 603 O O . SER A 1 75 ? 12.551 30.930 52.083 1.00 37.30 ? 75 SER A O 1 ATOM 604 C CB . SER A 1 75 ? 12.986 33.111 54.141 1.00 34.21 ? 75 SER A CB 1 ATOM 605 O OG . SER A 1 75 ? 14.200 33.728 53.750 1.00 33.21 ? 75 SER A OG 1 ATOM 606 N N . ASP A 1 76 ? 14.632 30.447 52.758 1.00 37.29 ? 76 ASP A N 1 ATOM 607 C CA . ASP A 1 76 ? 14.975 29.816 51.489 1.00 36.94 ? 76 ASP A CA 1 ATOM 608 C C . ASP A 1 76 ? 14.151 28.545 51.323 1.00 37.52 ? 76 ASP A C 1 ATOM 609 O O . ASP A 1 76 ? 14.172 27.910 50.276 1.00 37.19 ? 76 ASP A O 1 ATOM 610 C CB . ASP A 1 76 ? 16.467 29.511 51.460 1.00 36.07 ? 76 ASP A CB 1 ATOM 611 C CG . ASP A 1 76 ? 17.307 30.764 51.400 1.00 33.57 ? 76 ASP A CG 1 ATOM 612 O OD1 . ASP A 1 76 ? 18.460 30.731 51.869 1.00 35.79 ? 76 ASP A OD1 1 ATOM 613 O OD2 . ASP A 1 76 ? 16.817 31.779 50.871 1.00 33.07 ? 76 ASP A OD2 1 ATOM 614 N N . GLU A 1 77 ? 13.431 28.183 52.380 1.00 37.99 ? 77 GLU A N 1 ATOM 615 C CA . GLU A 1 77 ? 12.563 27.023 52.374 1.00 38.41 ? 77 GLU A CA 1 ATOM 616 C C . GLU A 1 77 ? 11.634 27.168 51.192 1.00 39.51 ? 77 GLU A C 1 ATOM 617 O O . GLU A 1 77 ? 11.230 28.282 50.846 1.00 39.65 ? 77 GLU A O 1 ATOM 618 C CB . GLU A 1 77 ? 11.754 26.987 53.673 1.00 42.18 ? 77 GLU A CB 1 ATOM 619 C CG . GLU A 1 77 ? 10.350 26.366 53.590 1.00 46.56 ? 77 GLU A CG 1 ATOM 620 C CD . GLU A 1 77 ? 9.258 27.400 53.340 1.00 50.04 ? 77 GLU A CD 1 ATOM 621 O OE1 . GLU A 1 77 ? 9.380 28.523 53.878 1.00 49.38 ? 77 GLU A OE1 1 ATOM 622 O OE2 . GLU A 1 77 ? 8.273 27.092 52.621 1.00 52.51 ? 77 GLU A OE2 1 ATOM 623 N N . GLY A 1 78 ? 11.301 26.050 50.560 1.00 40.49 ? 78 GLY A N 1 ATOM 624 C CA . GLY A 1 78 ? 10.403 26.102 49.422 1.00 42.58 ? 78 GLY A CA 1 ATOM 625 C C . GLY A 1 78 ? 10.664 25.044 48.375 1.00 43.08 ? 78 GLY A C 1 ATOM 626 O O . GLY A 1 78 ? 11.610 24.264 48.480 1.00 42.91 ? 78 GLY A O 1 ATOM 627 N N . THR A 1 79 ? 9.812 25.011 47.360 1.00 44.08 ? 79 THR A N 1 ATOM 628 C CA . THR A 1 79 ? 9.973 24.046 46.289 1.00 45.88 ? 79 THR A CA 1 ATOM 629 C C . THR A 1 79 ? 10.505 24.729 45.043 1.00 45.50 ? 79 THR A C 1 ATOM 630 O O . THR A 1 79 ? 9.880 25.640 44.492 1.00 42.01 ? 79 THR A O 1 ATOM 631 C CB . THR A 1 79 ? 8.645 23.342 45.937 1.00 47.34 ? 79 THR A CB 1 ATOM 632 O OG1 . THR A 1 79 ? 8.155 22.652 47.091 1.00 47.29 ? 79 THR A OG1 1 ATOM 633 C CG2 . THR A 1 79 ? 8.858 22.326 44.801 1.00 46.65 ? 79 THR A CG2 1 ATOM 634 N N . TYR A 1 80 ? 11.675 24.278 44.614 1.00 46.82 ? 80 TYR A N 1 ATOM 635 C CA . TYR A 1 80 ? 12.311 24.817 43.427 1.00 49.50 ? 80 TYR A CA 1 ATOM 636 C C . TYR A 1 80 ? 12.054 23.870 42.271 1.00 51.33 ? 80 TYR A C 1 ATOM 637 O O . TYR A 1 80 ? 11.997 22.651 42.466 1.00 52.83 ? 80 TYR A O 1 ATOM 638 C CB . TYR A 1 80 ? 13.821 24.970 43.652 1.00 47.62 ? 80 TYR A CB 1 ATOM 639 C CG . TYR A 1 80 ? 14.133 25.968 44.735 1.00 46.89 ? 80 TYR A CG 1 ATOM 640 C CD1 . TYR A 1 80 ? 14.033 25.622 46.084 1.00 46.57 ? 80 TYR A CD1 1 ATOM 641 C CD2 . TYR A 1 80 ? 14.415 27.290 44.416 1.00 45.72 ? 80 TYR A CD2 1 ATOM 642 C CE1 . TYR A 1 80 ? 14.196 26.575 47.084 1.00 45.03 ? 80 TYR A CE1 1 ATOM 643 C CE2 . TYR A 1 80 ? 14.577 28.244 45.405 1.00 45.16 ? 80 TYR A CE2 1 ATOM 644 C CZ . TYR A 1 80 ? 14.464 27.884 46.730 1.00 44.86 ? 80 TYR A CZ 1 ATOM 645 O OH . TYR A 1 80 ? 14.599 28.850 47.690 1.00 48.21 ? 80 TYR A OH 1 ATOM 646 N N . GLU A 1 81 ? 11.868 24.434 41.078 1.00 50.88 ? 81 GLU A N 1 ATOM 647 C CA . GLU A 1 81 ? 11.648 23.634 39.878 1.00 49.58 ? 81 GLU A CA 1 ATOM 648 C C . GLU A 1 81 ? 12.502 24.216 38.771 1.00 47.37 ? 81 GLU A C 1 ATOM 649 O O . GLU A 1 81 ? 12.537 25.427 38.582 1.00 47.75 ? 81 GLU A O 1 ATOM 650 C CB . GLU A 1 81 ? 10.173 23.630 39.476 1.00 52.84 ? 81 GLU A CB 1 ATOM 651 C CG . GLU A 1 81 ? 9.501 24.989 39.447 1.00 56.35 ? 81 GLU A CG 1 ATOM 652 C CD . GLU A 1 81 ? 8.116 24.914 38.839 1.00 58.43 ? 81 GLU A CD 1 ATOM 653 O OE1 . GLU A 1 81 ? 7.359 23.986 39.203 1.00 58.80 ? 81 GLU A OE1 1 ATOM 654 O OE2 . GLU A 1 81 ? 7.781 25.779 38.001 1.00 59.01 ? 81 GLU A OE2 1 ATOM 655 N N . CYS A 1 82 ? 13.199 23.351 38.047 1.00 46.08 ? 82 CYS A N 1 ATOM 656 C CA . CYS A 1 82 ? 14.086 23.792 36.976 1.00 46.00 ? 82 CYS A CA 1 ATOM 657 C C . CYS A 1 82 ? 13.707 23.248 35.604 1.00 46.23 ? 82 CYS A C 1 ATOM 658 O O . CYS A 1 82 ? 13.868 22.055 35.335 1.00 48.39 ? 82 CYS A O 1 ATOM 659 C CB . CYS A 1 82 ? 15.522 23.385 37.310 1.00 44.57 ? 82 CYS A CB 1 ATOM 660 S SG . CYS A 1 82 ? 16.734 23.692 35.992 1.00 45.91 ? 82 CYS A SG 1 ATOM 661 N N . VAL A 1 83 ? 13.215 24.126 34.734 1.00 43.27 ? 83 VAL A N 1 ATOM 662 C CA . VAL A 1 83 ? 12.826 23.714 33.393 1.00 42.34 ? 83 VAL A CA 1 ATOM 663 C C . VAL A 1 83 ? 13.795 24.230 32.340 1.00 41.72 ? 83 VAL A C 1 ATOM 664 O O . VAL A 1 83 ? 14.133 25.408 32.323 1.00 42.64 ? 83 VAL A O 1 ATOM 665 C CB . VAL A 1 83 ? 11.403 24.202 33.051 1.00 42.31 ? 83 VAL A CB 1 ATOM 666 C CG1 . VAL A 1 83 ? 11.212 25.636 33.526 1.00 40.50 ? 83 VAL A CG1 1 ATOM 667 C CG2 . VAL A 1 83 ? 11.167 24.099 31.543 1.00 40.06 ? 83 VAL A CG2 1 ATOM 668 N N . VAL A 1 84 ? 14.246 23.336 31.468 1.00 40.47 ? 84 VAL A N 1 ATOM 669 C CA . VAL A 1 84 ? 15.175 23.700 30.405 1.00 40.27 ? 84 VAL A CA 1 ATOM 670 C C . VAL A 1 84 ? 14.501 23.403 29.069 1.00 40.07 ? 84 VAL A C 1 ATOM 671 O O . VAL A 1 84 ? 13.878 22.354 28.921 1.00 38.66 ? 84 VAL A O 1 ATOM 672 C CB . VAL A 1 84 ? 16.511 22.918 30.553 1.00 38.12 ? 84 VAL A CB 1 ATOM 673 C CG1 . VAL A 1 84 ? 16.252 21.570 31.154 1.00 39.55 ? 84 VAL A CG1 1 ATOM 674 C CG2 . VAL A 1 84 ? 17.186 22.756 29.209 1.00 39.62 ? 84 VAL A CG2 1 ATOM 675 N N . LEU A 1 85 ? 14.607 24.331 28.115 1.00 40.33 ? 85 LEU A N 1 ATOM 676 C CA . LEU A 1 85 ? 13.972 24.170 26.805 1.00 43.74 ? 85 LEU A CA 1 ATOM 677 C C . LEU A 1 85 ? 14.944 24.209 25.627 1.00 48.73 ? 85 LEU A C 1 ATOM 678 O O . LEU A 1 85 ? 15.808 25.092 25.541 1.00 51.86 ? 85 LEU A O 1 ATOM 679 C CB . LEU A 1 85 ? 12.908 25.254 26.591 1.00 40.48 ? 85 LEU A CB 1 ATOM 680 C CG . LEU A 1 85 ? 11.821 25.458 27.646 1.00 38.28 ? 85 LEU A CG 1 ATOM 681 C CD1 . LEU A 1 85 ? 12.423 26.068 28.888 1.00 42.07 ? 85 LEU A CD1 1 ATOM 682 C CD2 . LEU A 1 85 ? 10.766 26.380 27.114 1.00 37.01 ? 85 LEU A CD2 1 ATOM 683 N N . LYS A 1 86 ? 14.792 23.251 24.715 1.00 51.92 ? 86 LYS A N 1 ATOM 684 C CA . LYS A 1 86 ? 15.638 23.169 23.526 1.00 54.27 ? 86 LYS A CA 1 ATOM 685 C C . LYS A 1 86 ? 14.861 23.775 22.366 1.00 54.35 ? 86 LYS A C 1 ATOM 686 O O . LYS A 1 86 ? 13.643 23.645 22.299 1.00 52.25 ? 86 LYS A O 1 ATOM 687 C CB . LYS A 1 86 ? 15.971 21.706 23.209 1.00 56.57 ? 86 LYS A CB 1 ATOM 688 C CG . LYS A 1 86 ? 16.985 21.518 22.083 1.00 60.36 ? 86 LYS A CG 1 ATOM 689 C CD . LYS A 1 86 ? 18.342 22.110 22.461 1.00 62.68 ? 86 LYS A CD 1 ATOM 690 C CE . LYS A 1 86 ? 19.453 21.570 21.582 1.00 61.44 ? 86 LYS A CE 1 ATOM 691 N NZ . LYS A 1 86 ? 20.781 21.978 22.106 1.00 61.52 ? 86 LYS A NZ 1 ATOM 692 N N . TYR A 1 87 ? 15.554 24.441 21.451 1.00 57.25 ? 87 TYR A N 1 ATOM 693 C CA . TYR A 1 87 ? 14.847 25.038 20.327 1.00 60.77 ? 87 TYR A CA 1 ATOM 694 C C . TYR A 1 87 ? 14.583 24.036 19.206 1.00 64.71 ? 87 TYR A C 1 ATOM 695 O O . TYR A 1 87 ? 15.389 23.890 18.275 1.00 65.17 ? 87 TYR A O 1 ATOM 696 C CB . TYR A 1 87 ? 15.598 26.248 19.760 1.00 57.27 ? 87 TYR A CB 1 ATOM 697 C CG . TYR A 1 87 ? 14.743 27.093 18.828 1.00 55.72 ? 87 TYR A CG 1 ATOM 698 C CD1 . TYR A 1 87 ? 14.407 26.647 17.549 1.00 55.27 ? 87 TYR A CD1 1 ATOM 699 C CD2 . TYR A 1 87 ? 14.232 28.322 19.246 1.00 56.46 ? 87 TYR A CD2 1 ATOM 700 C CE1 . TYR A 1 87 ? 13.575 27.401 16.710 1.00 57.16 ? 87 TYR A CE1 1 ATOM 701 C CE2 . TYR A 1 87 ? 13.401 29.083 18.421 1.00 57.67 ? 87 TYR A CE2 1 ATOM 702 C CZ . TYR A 1 87 ? 13.072 28.620 17.155 1.00 58.81 ? 87 TYR A CZ 1 ATOM 703 O OH . TYR A 1 87 ? 12.224 29.362 16.357 1.00 56.99 ? 87 TYR A OH 1 ATOM 704 N N . GLU A 1 88 ? 13.454 23.335 19.316 1.00 67.21 ? 88 GLU A N 1 ATOM 705 C CA . GLU A 1 88 ? 13.041 22.389 18.293 1.00 68.07 ? 88 GLU A CA 1 ATOM 706 C C . GLU A 1 88 ? 12.646 23.301 17.143 1.00 69.66 ? 88 GLU A C 1 ATOM 707 O O . GLU A 1 88 ? 11.636 24.015 17.223 1.00 69.15 ? 88 GLU A O 1 ATOM 708 C CB . GLU A 1 88 ? 11.829 21.586 18.750 1.00 68.43 ? 88 GLU A CB 1 ATOM 709 C CG . GLU A 1 88 ? 11.134 20.849 17.628 1.00 70.35 ? 88 GLU A CG 1 ATOM 710 C CD . GLU A 1 88 ? 9.647 20.772 17.849 1.00 73.58 ? 88 GLU A CD 1 ATOM 711 O OE1 . GLU A 1 88 ? 9.014 21.842 18.001 1.00 75.74 ? 88 GLU A OE1 1 ATOM 712 O OE2 . GLU A 1 88 ? 9.102 19.647 17.878 1.00 75.46 ? 88 GLU A OE2 1 ATOM 713 N N . LYS A 1 89 ? 13.453 23.285 16.087 1.00 71.34 ? 89 LYS A N 1 ATOM 714 C CA . LYS A 1 89 ? 13.233 24.134 14.921 1.00 71.60 ? 89 LYS A CA 1 ATOM 715 C C . LYS A 1 89 ? 11.801 24.629 14.772 1.00 70.26 ? 89 LYS A C 1 ATOM 716 O O . LYS A 1 89 ? 10.876 23.842 14.540 1.00 69.15 ? 89 LYS A O 1 ATOM 717 C CB . LYS A 1 89 ? 13.712 23.401 13.673 1.00 72.85 ? 89 LYS A CB 1 ATOM 718 C CG . LYS A 1 89 ? 15.173 23.011 13.816 1.00 76.53 ? 89 LYS A CG 1 ATOM 719 C CD . LYS A 1 89 ? 15.845 22.708 12.486 1.00 80.14 ? 89 LYS A CD 1 ATOM 720 C CE . LYS A 1 89 ? 17.343 22.533 12.688 1.00 80.83 ? 89 LYS A CE 1 ATOM 721 N NZ . LYS A 1 89 ? 18.065 22.355 11.406 1.00 81.98 ? 89 LYS A NZ 1 ATOM 722 N N . ASP A 1 90 ? 11.663 25.946 14.936 1.00 68.04 ? 90 ASP A N 1 ATOM 723 C CA . ASP A 1 90 ? 10.407 26.690 14.868 1.00 66.06 ? 90 ASP A CA 1 ATOM 724 C C . ASP A 1 90 ? 9.983 27.166 16.237 1.00 63.79 ? 90 ASP A C 1 ATOM 725 O O . ASP A 1 90 ? 9.237 28.134 16.354 1.00 61.58 ? 90 ASP A O 1 ATOM 726 C CB . ASP A 1 90 ? 9.263 25.852 14.305 1.00 68.38 ? 90 ASP A CB 1 ATOM 727 C CG . ASP A 1 90 ? 7.903 26.344 14.779 1.00 70.22 ? 90 ASP A CG 1 ATOM 728 O OD1 . ASP A 1 90 ? 7.430 27.383 14.273 1.00 71.19 ? 90 ASP A OD1 1 ATOM 729 O OD2 . ASP A 1 90 ? 7.309 25.701 15.677 1.00 70.29 ? 90 ASP A OD2 1 ATOM 730 N N . ALA A 1 91 ? 10.438 26.479 17.277 1.00 62.99 ? 91 ALA A N 1 ATOM 731 C CA . ALA A 1 91 ? 10.043 26.871 18.617 1.00 62.27 ? 91 ALA A CA 1 ATOM 732 C C . ALA A 1 91 ? 10.944 26.342 19.713 1.00 60.82 ? 91 ALA A C 1 ATOM 733 O O . ALA A 1 91 ? 11.998 25.752 19.456 1.00 62.60 ? 91 ALA A O 1 ATOM 734 C CB . ALA A 1 91 ? 8.614 26.415 18.866 1.00 62.68 ? 91 ALA A CB 1 ATOM 735 N N . PHE A 1 92 ? 10.516 26.583 20.945 1.00 58.58 ? 92 PHE A N 1 ATOM 736 C CA . PHE A 1 92 ? 11.240 26.116 22.112 1.00 56.64 ? 92 PHE A CA 1 ATOM 737 C C . PHE A 1 92 ? 10.476 24.981 22.796 1.00 56.53 ? 92 PHE A C 1 ATOM 738 O O . PHE A 1 92 ? 9.526 25.221 23.545 1.00 56.40 ? 92 PHE A O 1 ATOM 739 C CB . PHE A 1 92 ? 11.452 27.251 23.123 1.00 54.12 ? 92 PHE A CB 1 ATOM 740 C CG . PHE A 1 92 ? 12.566 28.196 22.766 1.00 50.31 ? 92 PHE A CG 1 ATOM 741 C CD1 . PHE A 1 92 ? 12.285 29.455 22.259 1.00 48.74 ? 92 PHE A CD1 1 ATOM 742 C CD2 . PHE A 1 92 ? 13.893 27.828 22.955 1.00 47.95 ? 92 PHE A CD2 1 ATOM 743 C CE1 . PHE A 1 92 ? 13.309 30.335 21.948 1.00 49.16 ? 92 PHE A CE1 1 ATOM 744 C CE2 . PHE A 1 92 ? 14.923 28.702 22.645 1.00 46.81 ? 92 PHE A CE2 1 ATOM 745 C CZ . PHE A 1 92 ? 14.631 29.959 22.142 1.00 47.23 ? 92 PHE A CZ 1 ATOM 746 N N . LYS A 1 93 ? 10.890 23.746 22.530 1.00 57.68 ? 93 LYS A N 1 ATOM 747 C CA . LYS A 1 93 ? 10.278 22.564 23.145 1.00 58.19 ? 93 LYS A CA 1 ATOM 748 C C . LYS A 1 93 ? 11.139 22.222 24.371 1.00 59.22 ? 93 LYS A C 1 ATOM 749 O O . LYS A 1 93 ? 12.350 22.018 24.246 1.00 58.23 ? 93 LYS A O 1 ATOM 750 C CB . LYS A 1 93 ? 10.275 21.391 22.149 1.00 57.30 ? 93 LYS A CB 1 ATOM 751 C CG . LYS A 1 93 ? 9.456 20.171 22.579 1.00 57.67 ? 93 LYS A CG 1 ATOM 752 C CD . LYS A 1 93 ? 9.138 19.252 21.394 1.00 55.56 ? 93 LYS A CD 1 ATOM 753 C CE . LYS A 1 93 ? 10.322 18.408 20.955 1.00 56.37 ? 93 LYS A CE 1 ATOM 754 N NZ . LYS A 1 93 ? 10.626 17.289 21.894 1.00 55.65 ? 93 LYS A NZ 1 ATOM 755 N N . ARG A 1 94 ? 10.533 22.178 25.554 1.00 59.95 ? 94 ARG A N 1 ATOM 756 C CA . ARG A 1 94 ? 11.306 21.875 26.750 1.00 60.25 ? 94 ARG A CA 1 ATOM 757 C C . ARG A 1 94 ? 11.697 20.398 26.799 1.00 59.60 ? 94 ARG A C 1 ATOM 758 O O . ARG A 1 94 ? 10.857 19.505 26.648 1.00 59.72 ? 94 ARG A O 1 ATOM 759 C CB . ARG A 1 94 ? 10.536 22.280 28.010 1.00 60.53 ? 94 ARG A CB 1 ATOM 760 C CG . ARG A 1 94 ? 9.375 21.392 28.377 1.00 62.24 ? 94 ARG A CG 1 ATOM 761 C CD . ARG A 1 94 ? 8.682 21.943 29.599 1.00 63.08 ? 94 ARG A CD 1 ATOM 762 N NE . ARG A 1 94 ? 7.723 20.997 30.151 1.00 66.91 ? 94 ARG A NE 1 ATOM 763 C CZ . ARG A 1 94 ? 6.905 21.267 31.163 1.00 70.28 ? 94 ARG A CZ 1 ATOM 764 N NH1 . ARG A 1 94 ? 6.930 22.466 31.737 1.00 70.87 ? 94 ARG A NH1 1 ATOM 765 N NH2 . ARG A 1 94 ? 6.063 20.337 31.605 1.00 70.89 ? 94 ARG A NH2 1 ATOM 766 N N . GLU A 1 95 ? 12.988 20.159 27.008 1.00 57.18 ? 95 GLU A N 1 ATOM 767 C CA . GLU A 1 95 ? 13.521 18.818 27.037 1.00 55.91 ? 95 GLU A CA 1 ATOM 768 C C . GLU A 1 95 ? 13.825 18.322 28.440 1.00 55.93 ? 95 GLU A C 1 ATOM 769 O O . GLU A 1 95 ? 14.485 17.295 28.584 1.00 57.81 ? 95 GLU A O 1 ATOM 770 C CB . GLU A 1 95 ? 14.792 18.753 26.188 1.00 56.45 ? 95 GLU A CB 1 ATOM 771 C CG . GLU A 1 95 ? 16.057 19.124 26.941 1.00 59.52 ? 95 GLU A CG 1 ATOM 772 C CD . GLU A 1 95 ? 17.264 19.322 26.036 1.00 60.61 ? 95 GLU A CD 1 ATOM 773 O OE1 . GLU A 1 95 ? 17.383 18.598 25.024 1.00 59.71 ? 95 GLU A OE1 1 ATOM 774 O OE2 . GLU A 1 95 ? 18.104 20.196 26.349 1.00 60.39 ? 95 GLU A OE2 1 ATOM 775 N N . HIS A 1 96 ? 13.366 19.037 29.470 1.00 54.62 ? 96 HIS A N 1 ATOM 776 C CA . HIS A 1 96 ? 13.614 18.604 30.851 1.00 51.77 ? 96 HIS A CA 1 ATOM 777 C C . HIS A 1 96 ? 12.990 19.421 31.978 1.00 49.95 ? 96 HIS A C 1 ATOM 778 O O . HIS A 1 96 ? 12.782 20.629 31.868 1.00 49.69 ? 96 HIS A O 1 ATOM 779 C CB . HIS A 1 96 ? 15.111 18.503 31.128 1.00 51.42 ? 96 HIS A CB 1 ATOM 780 C CG . HIS A 1 96 ? 15.431 17.926 32.473 1.00 54.76 ? 96 HIS A CG 1 ATOM 781 N ND1 . HIS A 1 96 ? 15.089 16.638 32.831 1.00 55.83 ? 96 HIS A ND1 1 ATOM 782 C CD2 . HIS A 1 96 ? 16.044 18.464 33.552 1.00 54.64 ? 96 HIS A CD2 1 ATOM 783 C CE1 . HIS A 1 96 ? 15.479 16.410 34.072 1.00 56.37 ? 96 HIS A CE1 1 ATOM 784 N NE2 . HIS A 1 96 ? 16.060 17.502 34.533 1.00 54.22 ? 96 HIS A NE2 1 ATOM 785 N N . LEU A 1 97 ? 12.712 18.735 33.079 1.00 48.08 ? 97 LEU A N 1 ATOM 786 C CA . LEU A 1 97 ? 12.125 19.366 34.248 1.00 46.55 ? 97 LEU A CA 1 ATOM 787 C C . LEU A 1 97 ? 12.472 18.608 35.533 1.00 45.82 ? 97 LEU A C 1 ATOM 788 O O . LEU A 1 97 ? 12.168 17.419 35.678 1.00 44.93 ? 97 LEU A O 1 ATOM 789 C CB . LEU A 1 97 ? 10.604 19.449 34.103 1.00 44.09 ? 97 LEU A CB 1 ATOM 790 C CG . LEU A 1 97 ? 9.895 20.223 35.213 1.00 40.54 ? 97 LEU A CG 1 ATOM 791 C CD1 . LEU A 1 97 ? 10.246 21.694 35.067 1.00 41.53 ? 97 LEU A CD1 1 ATOM 792 C CD2 . LEU A 1 97 ? 8.393 20.020 35.132 1.00 37.69 ? 97 LEU A CD2 1 ATOM 793 N N . ALA A 1 98 ? 13.127 19.308 36.456 1.00 44.38 ? 98 ALA A N 1 ATOM 794 C CA . ALA A 1 98 ? 13.502 18.734 37.740 1.00 41.93 ? 98 ALA A CA 1 ATOM 795 C C . ALA A 1 98 ? 12.757 19.563 38.752 1.00 41.28 ? 98 ALA A C 1 ATOM 796 O O . ALA A 1 98 ? 12.391 20.708 38.478 1.00 39.51 ? 98 ALA A O 1 ATOM 797 C CB . ALA A 1 98 ? 15.002 18.841 37.975 1.00 37.99 ? 98 ALA A CB 1 ATOM 798 N N . GLU A 1 99 ? 12.513 18.979 39.914 1.00 42.86 ? 99 GLU A N 1 ATOM 799 C CA . GLU A 1 99 ? 11.794 19.668 40.970 1.00 44.12 ? 99 GLU A CA 1 ATOM 800 C C . GLU A 1 99 ? 12.309 19.149 42.295 1.00 45.38 ? 99 GLU A C 1 ATOM 801 O O . GLU A 1 99 ? 12.433 17.937 42.496 1.00 46.92 ? 99 GLU A O 1 ATOM 802 C CB . GLU A 1 99 ? 10.301 19.388 40.866 1.00 42.97 ? 99 GLU A CB 1 ATOM 803 C CG . GLU A 1 99 ? 9.445 20.306 41.692 1.00 47.56 ? 99 GLU A CG 1 ATOM 804 C CD . GLU A 1 99 ? 7.997 19.849 41.719 1.00 52.20 ? 99 GLU A CD 1 ATOM 805 O OE1 . GLU A 1 99 ? 7.729 18.805 42.359 1.00 52.68 ? 99 GLU A OE1 1 ATOM 806 O OE2 . GLU A 1 99 ? 7.136 20.519 41.097 1.00 50.09 ? 99 GLU A OE2 1 ATOM 807 N N . VAL A 1 100 ? 12.631 20.073 43.192 1.00 44.51 ? 100 VAL A N 1 ATOM 808 C CA . VAL A 1 100 ? 13.116 19.704 44.507 1.00 41.58 ? 100 VAL A CA 1 ATOM 809 C C . VAL A 1 100 ? 12.583 20.712 45.510 1.00 41.66 ? 100 VAL A C 1 ATOM 810 O O . VAL A 1 100 ? 12.405 21.892 45.189 1.00 41.13 ? 100 VAL A O 1 ATOM 811 C CB . VAL A 1 100 ? 14.667 19.676 44.557 1.00 39.66 ? 100 VAL A CB 1 ATOM 812 C CG1 . VAL A 1 100 ? 15.236 21.052 44.278 1.00 39.85 ? 100 VAL A CG1 1 ATOM 813 C CG2 . VAL A 1 100 ? 15.128 19.169 45.904 1.00 37.25 ? 100 VAL A CG2 1 ATOM 814 N N . THR A 1 101 ? 12.295 20.234 46.715 1.00 41.11 ? 101 THR A N 1 ATOM 815 C CA . THR A 1 101 ? 11.796 21.100 47.777 1.00 39.48 ? 101 THR A CA 1 ATOM 816 C C . THR A 1 101 ? 12.901 21.192 48.835 1.00 38.76 ? 101 THR A C 1 ATOM 817 O O . THR A 1 101 ? 13.501 20.177 49.201 1.00 37.66 ? 101 THR A O 1 ATOM 818 C CB . THR A 1 101 ? 10.550 20.517 48.420 1.00 37.84 ? 101 THR A CB 1 ATOM 819 O OG1 . THR A 1 101 ? 10.946 19.721 49.538 1.00 40.99 ? 101 THR A OG1 1 ATOM 820 C CG2 . THR A 1 101 ? 9.789 19.644 47.425 1.00 34.17 ? 101 THR A CG2 1 ATOM 821 N N . LEU A 1 102 ? 13.158 22.404 49.328 1.00 36.98 ? 102 LEU A N 1 ATOM 822 C CA . LEU A 1 102 ? 14.218 22.627 50.312 1.00 34.14 ? 102 LEU A CA 1 ATOM 823 C C . LEU A 1 102 ? 13.769 22.927 51.734 1.00 31.20 ? 102 LEU A C 1 ATOM 824 O O . LEU A 1 102 ? 12.975 23.830 51.962 1.00 31.55 ? 102 LEU A O 1 ATOM 825 C CB . LEU A 1 102 ? 15.123 23.769 49.846 1.00 33.50 ? 102 LEU A CB 1 ATOM 826 C CG . LEU A 1 102 ? 16.317 24.083 50.746 1.00 31.56 ? 102 LEU A CG 1 ATOM 827 C CD1 . LEU A 1 102 ? 17.254 22.892 50.761 1.00 30.54 ? 102 LEU A CD1 1 ATOM 828 C CD2 . LEU A 1 102 ? 17.022 25.335 50.248 1.00 28.40 ? 102 LEU A CD2 1 ATOM 829 N N . SER A 1 103 ? 14.293 22.167 52.688 1.00 29.66 ? 103 SER A N 1 ATOM 830 C CA . SER A 1 103 ? 13.979 22.375 54.098 1.00 29.92 ? 103 SER A CA 1 ATOM 831 C C . SER A 1 103 ? 15.198 23.021 54.720 1.00 30.10 ? 103 SER A C 1 ATOM 832 O O . SER A 1 103 ? 16.323 22.707 54.349 1.00 33.03 ? 103 SER A O 1 ATOM 833 C CB . SER A 1 103 ? 13.707 21.048 54.825 1.00 29.70 ? 103 SER A CB 1 ATOM 834 O OG . SER A 1 103 ? 12.336 20.685 54.777 1.00 32.53 ? 103 SER A OG 1 ATOM 835 N N . VAL A 1 104 ? 14.978 23.922 55.664 1.00 28.84 ? 104 VAL A N 1 ATOM 836 C CA . VAL A 1 104 ? 16.078 24.601 56.333 1.00 27.13 ? 104 VAL A CA 1 ATOM 837 C C . VAL A 1 104 ? 15.962 24.441 57.853 1.00 26.40 ? 104 VAL A C 1 ATOM 838 O O . VAL A 1 104 ? 15.091 25.039 58.479 1.00 26.76 ? 104 VAL A O 1 ATOM 839 C CB . VAL A 1 104 ? 16.077 26.110 55.961 1.00 26.51 ? 104 VAL A CB 1 ATOM 840 C CG1 . VAL A 1 104 ? 17.051 26.873 56.829 1.00 29.47 ? 104 VAL A CG1 1 ATOM 841 C CG2 . VAL A 1 104 ? 16.422 26.283 54.501 1.00 25.51 ? 104 VAL A CG2 1 ATOM 842 N N . LYS A 1 105 ? 16.832 23.633 58.448 1.00 26.93 ? 105 LYS A N 1 ATOM 843 C CA . LYS A 1 105 ? 16.816 23.432 59.907 1.00 28.17 ? 105 LYS A CA 1 ATOM 844 C C . LYS A 1 105 ? 17.473 24.625 60.635 1.00 26.34 ? 105 LYS A C 1 ATOM 845 O O . LYS A 1 105 ? 18.526 25.120 60.217 1.00 26.19 ? 105 LYS A O 1 ATOM 846 C CB . LYS A 1 105 ? 17.548 22.130 60.273 1.00 29.69 ? 105 LYS A CB 1 ATOM 847 C CG . LYS A 1 105 ? 16.957 20.880 59.626 1.00 34.55 ? 105 LYS A CG 1 ATOM 848 C CD . LYS A 1 105 ? 15.760 20.359 60.400 1.00 39.90 ? 105 LYS A CD 1 ATOM 849 C CE . LYS A 1 105 ? 16.204 19.773 61.748 1.00 45.68 ? 105 LYS A CE 1 ATOM 850 N NZ . LYS A 1 105 ? 15.067 19.425 62.661 1.00 48.35 ? 105 LYS A NZ 1 ATOM 851 N N . ALA A 1 106 ? 16.842 25.086 61.712 1.00 22.40 ? 106 ALA A N 1 ATOM 852 C CA . ALA A 1 106 ? 17.355 26.216 62.480 1.00 21.32 ? 106 ALA A CA 1 ATOM 853 C C . ALA A 1 106 ? 17.171 26.008 63.969 1.00 22.80 ? 106 ALA A C 1 ATOM 854 O O . ALA A 1 106 ? 16.612 26.869 64.642 1.00 23.46 ? 106 ALA A O 1 ATOM 855 C CB . ALA A 1 106 ? 16.653 27.499 62.062 1.00 18.35 ? 106 ALA A CB 1 ATOM 856 N N . ASP A 1 107 ? 17.645 24.879 64.487 1.00 22.82 ? 107 ASP A N 1 ATOM 857 C CA . ASP A 1 107 ? 17.498 24.594 65.902 1.00 24.88 ? 107 ASP A CA 1 ATOM 858 C C . ASP A 1 107 ? 18.230 25.600 66.757 1.00 27.46 ? 107 ASP A C 1 ATOM 859 O O . ASP A 1 107 ? 19.157 26.268 66.293 1.00 28.40 ? 107 ASP A O 1 ATOM 860 C CB . ASP A 1 107 ? 18.001 23.192 66.234 1.00 26.51 ? 107 ASP A CB 1 ATOM 861 C CG . ASP A 1 107 ? 17.043 22.117 65.791 1.00 29.29 ? 107 ASP A CG 1 ATOM 862 O OD1 . ASP A 1 107 ? 15.903 22.474 65.445 1.00 33.87 ? 107 ASP A OD1 1 ATOM 863 O OD2 . ASP A 1 107 ? 17.415 20.923 65.798 1.00 31.35 ? 107 ASP A OD2 1 ATOM 864 N N . PHE A 1 108 ? 17.783 25.707 68.008 1.00 28.52 ? 108 PHE A N 1 ATOM 865 C CA . PHE A 1 108 ? 18.366 26.607 68.994 1.00 27.27 ? 108 PHE A CA 1 ATOM 866 C C . PHE A 1 108 ? 19.340 25.805 69.826 1.00 25.40 ? 108 PHE A C 1 ATOM 867 O O . PHE A 1 108 ? 18.986 24.776 70.372 1.00 26.90 ? 108 PHE A O 1 ATOM 868 C CB . PHE A 1 108 ? 17.271 27.199 69.900 1.00 27.42 ? 108 PHE A CB 1 ATOM 869 C CG . PHE A 1 108 ? 16.727 28.516 69.410 1.00 31.08 ? 108 PHE A CG 1 ATOM 870 C CD1 . PHE A 1 108 ? 15.523 28.577 68.723 1.00 29.04 ? 108 PHE A CD1 1 ATOM 871 C CD2 . PHE A 1 108 ? 17.470 29.689 69.565 1.00 30.33 ? 108 PHE A CD2 1 ATOM 872 C CE1 . PHE A 1 108 ? 15.070 29.778 68.195 1.00 29.56 ? 108 PHE A CE1 1 ATOM 873 C CE2 . PHE A 1 108 ? 17.027 30.893 69.036 1.00 28.47 ? 108 PHE A CE2 1 ATOM 874 C CZ . PHE A 1 108 ? 15.827 30.940 68.350 1.00 28.32 ? 108 PHE A CZ 1 ATOM 875 N N . PRO A 1 109 ? 20.593 26.241 69.914 1.00 26.31 ? 109 PRO A N 1 ATOM 876 C CA . PRO A 1 109 ? 21.492 25.425 70.739 1.00 26.61 ? 109 PRO A CA 1 ATOM 877 C C . PRO A 1 109 ? 20.993 25.442 72.181 1.00 28.03 ? 109 PRO A C 1 ATOM 878 O O . PRO A 1 109 ? 20.307 26.369 72.591 1.00 29.76 ? 109 PRO A O 1 ATOM 879 C CB . PRO A 1 109 ? 22.842 26.117 70.569 1.00 25.72 ? 109 PRO A CB 1 ATOM 880 C CG . PRO A 1 109 ? 22.458 27.566 70.358 1.00 30.15 ? 109 PRO A CG 1 ATOM 881 C CD . PRO A 1 109 ? 21.255 27.461 69.421 1.00 26.87 ? 109 PRO A CD 1 ATOM 882 N N . THR A 1 110 ? 21.312 24.414 72.950 1.00 31.00 ? 110 THR A N 1 ATOM 883 C CA . THR A 1 110 ? 20.879 24.363 74.335 1.00 33.22 ? 110 THR A CA 1 ATOM 884 C C . THR A 1 110 ? 21.359 25.648 75.017 1.00 35.68 ? 110 THR A C 1 ATOM 885 O O . THR A 1 110 ? 22.552 25.968 74.983 1.00 37.23 ? 110 THR A O 1 ATOM 886 C CB . THR A 1 110 ? 21.456 23.125 75.033 1.00 33.18 ? 110 THR A CB 1 ATOM 887 O OG1 . THR A 1 110 ? 21.247 23.241 76.439 1.00 38.97 ? 110 THR A OG1 1 ATOM 888 C CG2 . THR A 1 110 ? 22.941 22.991 74.763 1.00 38.45 ? 110 THR A CG2 1 ATOM 889 N N . PRO A 1 111 ? 20.432 26.408 75.642 1.00 36.91 ? 111 PRO A N 1 ATOM 890 C CA . PRO A 1 111 ? 20.778 27.665 76.317 1.00 35.49 ? 111 PRO A CA 1 ATOM 891 C C . PRO A 1 111 ? 21.779 27.499 77.441 1.00 35.79 ? 111 PRO A C 1 ATOM 892 O O . PRO A 1 111 ? 21.810 26.461 78.103 1.00 35.88 ? 111 PRO A O 1 ATOM 893 C CB . PRO A 1 111 ? 19.431 28.160 76.824 1.00 35.69 ? 111 PRO A CB 1 ATOM 894 C CG . PRO A 1 111 ? 18.726 26.878 77.162 1.00 34.48 ? 111 PRO A CG 1 ATOM 895 C CD . PRO A 1 111 ? 19.038 26.027 75.949 1.00 35.68 ? 111 PRO A CD 1 ATOM 896 N N . SER A 1 112 ? 22.595 28.526 77.649 1.00 35.71 ? 112 SER A N 1 ATOM 897 C CA . SER A 1 112 ? 23.588 28.512 78.719 1.00 37.03 ? 112 SER A CA 1 ATOM 898 C C . SER A 1 112 ? 23.171 29.542 79.765 1.00 38.05 ? 112 SER A C 1 ATOM 899 O O . SER A 1 112 ? 22.753 30.646 79.409 1.00 39.48 ? 112 SER A O 1 ATOM 900 C CB . SER A 1 112 ? 24.966 28.872 78.179 1.00 35.73 ? 112 SER A CB 1 ATOM 901 O OG . SER A 1 112 ? 24.960 30.181 77.651 1.00 36.93 ? 112 SER A OG 1 ATOM 902 N N . ILE A 1 113 ? 23.302 29.176 81.042 1.00 38.29 ? 113 ILE A N 1 ATOM 903 C CA . ILE A 1 113 ? 22.933 30.032 82.179 1.00 36.83 ? 113 ILE A CA 1 ATOM 904 C C . ILE A 1 113 ? 24.096 30.610 83.029 1.00 36.49 ? 113 ILE A C 1 ATOM 905 O O . ILE A 1 113 ? 25.043 29.911 83.373 1.00 36.10 ? 113 ILE A O 1 ATOM 906 C CB . ILE A 1 113 ? 21.993 29.262 83.120 1.00 34.62 ? 113 ILE A CB 1 ATOM 907 C CG1 . ILE A 1 113 ? 20.715 28.880 82.376 1.00 37.24 ? 113 ILE A CG1 1 ATOM 908 C CG2 . ILE A 1 113 ? 21.669 30.096 84.325 1.00 37.52 ? 113 ILE A CG2 1 ATOM 909 C CD1 . ILE A 1 113 ? 19.673 28.165 83.243 1.00 35.52 ? 113 ILE A CD1 1 ATOM 910 N N . SER A 1 114 ? 24.011 31.894 83.362 1.00 37.00 ? 114 SER A N 1 ATOM 911 C CA . SER A 1 114 ? 25.023 32.548 84.190 1.00 38.00 ? 114 SER A CA 1 ATOM 912 C C . SER A 1 114 ? 24.392 32.932 85.523 1.00 41.33 ? 114 SER A C 1 ATOM 913 O O . SER A 1 114 ? 23.213 33.289 85.572 1.00 43.52 ? 114 SER A O 1 ATOM 914 C CB . SER A 1 114 ? 25.545 33.806 83.512 1.00 33.84 ? 114 SER A CB 1 ATOM 915 O OG . SER A 1 114 ? 26.145 33.474 82.289 1.00 34.56 ? 114 SER A OG 1 ATOM 916 N N . ASP A 1 115 ? 25.167 32.855 86.601 1.00 42.28 ? 115 ASP A N 1 ATOM 917 C CA . ASP A 1 115 ? 24.652 33.209 87.912 1.00 43.95 ? 115 ASP A CA 1 ATOM 918 C C . ASP A 1 115 ? 25.608 34.115 88.659 1.00 44.22 ? 115 ASP A C 1 ATOM 919 O O . ASP A 1 115 ? 26.817 33.892 88.653 1.00 45.83 ? 115 ASP A O 1 ATOM 920 C CB . ASP A 1 115 ? 24.365 31.956 88.746 1.00 44.70 ? 115 ASP A CB 1 ATOM 921 C CG . ASP A 1 115 ? 25.589 31.102 88.968 1.00 48.13 ? 115 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 115 ? 25.523 30.197 89.828 1.00 52.47 ? 115 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 115 ? 26.615 31.317 88.287 1.00 52.62 ? 115 ASP A OD2 1 ATOM 924 N N . PHE A 1 116 ? 25.064 35.144 89.299 1.00 44.11 ? 116 PHE A N 1 ATOM 925 C CA . PHE A 1 116 ? 25.890 36.074 90.048 1.00 43.45 ? 116 PHE A CA 1 ATOM 926 C C . PHE A 1 116 ? 25.081 36.995 90.945 1.00 43.80 ? 116 PHE A C 1 ATOM 927 O O . PHE A 1 116 ? 23.932 37.318 90.644 1.00 45.42 ? 116 PHE A O 1 ATOM 928 C CB . PHE A 1 116 ? 26.744 36.883 89.078 1.00 42.74 ? 116 PHE A CB 1 ATOM 929 C CG . PHE A 1 116 ? 25.960 37.578 88.010 1.00 42.61 ? 116 PHE A CG 1 ATOM 930 C CD1 . PHE A 1 116 ? 25.374 38.814 88.256 1.00 43.96 ? 116 PHE A CD1 1 ATOM 931 C CD2 . PHE A 1 116 ? 25.840 37.019 86.742 1.00 42.02 ? 116 PHE A CD2 1 ATOM 932 C CE1 . PHE A 1 116 ? 24.681 39.495 87.246 1.00 43.38 ? 116 PHE A CE1 1 ATOM 933 C CE2 . PHE A 1 116 ? 25.152 37.688 85.728 1.00 42.23 ? 116 PHE A CE2 1 ATOM 934 C CZ . PHE A 1 116 ? 24.575 38.927 85.981 1.00 43.62 ? 116 PHE A CZ 1 ATOM 935 N N . GLU A 1 117 ? 25.691 37.412 92.051 1.00 43.55 ? 117 GLU A N 1 ATOM 936 C CA . GLU A 1 117 ? 25.042 38.294 93.013 1.00 42.09 ? 117 GLU A CA 1 ATOM 937 C C . GLU A 1 117 ? 24.914 39.732 92.538 1.00 41.97 ? 117 GLU A C 1 ATOM 938 O O . GLU A 1 117 ? 25.766 40.243 91.810 1.00 39.55 ? 117 GLU A O 1 ATOM 939 C CB . GLU A 1 117 ? 25.814 38.302 94.319 1.00 40.46 ? 117 GLU A CB 1 ATOM 940 C CG . GLU A 1 117 ? 25.860 36.982 95.035 1.00 43.63 ? 117 GLU A CG 1 ATOM 941 C CD . GLU A 1 117 ? 26.769 37.045 96.244 1.00 47.06 ? 117 GLU A CD 1 ATOM 942 O OE1 . GLU A 1 117 ? 28.003 37.174 96.056 1.00 45.56 ? 117 GLU A OE1 1 ATOM 943 O OE2 . GLU A 1 117 ? 26.245 36.984 97.379 1.00 48.30 ? 117 GLU A OE2 1 ATOM 944 N N . ILE A 1 118 ? 23.837 40.375 92.971 1.00 42.33 ? 118 ILE A N 1 ATOM 945 C CA . ILE A 1 118 ? 23.574 41.768 92.646 1.00 44.62 ? 118 ILE A CA 1 ATOM 946 C C . ILE A 1 118 ? 23.655 42.495 93.985 1.00 47.86 ? 118 ILE A C 1 ATOM 947 O O . ILE A 1 118 ? 23.781 41.849 95.028 1.00 47.91 ? 118 ILE A O 1 ATOM 948 C CB . ILE A 1 118 ? 22.166 41.950 92.062 1.00 44.99 ? 118 ILE A CB 1 ATOM 949 C CG1 . ILE A 1 118 ? 21.138 41.255 92.967 1.00 45.75 ? 118 ILE A CG1 1 ATOM 950 C CG2 . ILE A 1 118 ? 22.117 41.411 90.641 1.00 45.05 ? 118 ILE A CG2 1 ATOM 951 C CD1 . ILE A 1 118 ? 19.714 41.367 92.481 1.00 43.41 ? 118 ILE A CD1 1 ATOM 952 N N . PRO A 1 119 ? 23.590 43.841 93.980 1.00 49.93 ? 119 PRO A N 1 ATOM 953 C CA . PRO A 1 119 ? 23.662 44.580 95.243 1.00 51.18 ? 119 PRO A CA 1 ATOM 954 C C . PRO A 1 119 ? 22.301 44.574 95.938 1.00 52.42 ? 119 PRO A C 1 ATOM 955 O O . PRO A 1 119 ? 21.572 45.561 95.912 1.00 55.40 ? 119 PRO A O 1 ATOM 956 C CB . PRO A 1 119 ? 24.077 45.977 94.793 1.00 51.40 ? 119 PRO A CB 1 ATOM 957 C CG . PRO A 1 119 ? 23.303 46.131 93.518 1.00 49.47 ? 119 PRO A CG 1 ATOM 958 C CD . PRO A 1 119 ? 23.505 44.772 92.837 1.00 50.92 ? 119 PRO A CD 1 ATOM 959 N N . THR A 1 120 ? 21.957 43.447 96.541 1.00 52.17 ? 120 THR A N 1 ATOM 960 C CA . THR A 1 120 ? 20.692 43.295 97.241 1.00 52.14 ? 120 THR A CA 1 ATOM 961 C C . THR A 1 120 ? 20.843 42.036 98.064 1.00 52.61 ? 120 THR A C 1 ATOM 962 O O . THR A 1 120 ? 21.034 40.948 97.528 1.00 52.92 ? 120 THR A O 1 ATOM 963 C CB . THR A 1 120 ? 19.498 43.117 96.267 1.00 52.27 ? 120 THR A CB 1 ATOM 964 O OG1 . THR A 1 120 ? 19.308 44.309 95.491 1.00 50.88 ? 120 THR A OG1 1 ATOM 965 C CG2 . THR A 1 120 ? 18.224 42.823 97.043 1.00 50.26 ? 120 THR A CG2 1 ATOM 966 N N . SER A 1 121 ? 20.767 42.194 99.375 1.00 53.25 ? 121 SER A N 1 ATOM 967 C CA . SER A 1 121 ? 20.918 41.078 100.290 1.00 54.17 ? 121 SER A CA 1 ATOM 968 C C . SER A 1 121 ? 20.139 39.829 99.898 1.00 53.65 ? 121 SER A C 1 ATOM 969 O O . SER A 1 121 ? 18.921 39.871 99.741 1.00 54.95 ? 121 SER A O 1 ATOM 970 C CB . SER A 1 121 ? 20.510 41.513 101.698 1.00 54.35 ? 121 SER A CB 1 ATOM 971 O OG . SER A 1 121 ? 19.264 42.186 101.669 1.00 57.56 ? 121 SER A OG 1 ATOM 972 N N . ASN A 1 122 ? 20.858 38.723 99.732 1.00 53.43 ? 122 ASN A N 1 ATOM 973 C CA . ASN A 1 122 ? 20.256 37.432 99.404 1.00 52.92 ? 122 ASN A CA 1 ATOM 974 C C . ASN A 1 122 ? 19.885 37.153 97.951 1.00 50.68 ? 122 ASN A C 1 ATOM 975 O O . ASN A 1 122 ? 19.762 35.992 97.559 1.00 47.83 ? 122 ASN A O 1 ATOM 976 C CB . ASN A 1 122 ? 19.019 37.208 100.279 1.00 55.96 ? 122 ASN A CB 1 ATOM 977 C CG . ASN A 1 122 ? 19.372 36.801 101.696 1.00 58.77 ? 122 ASN A CG 1 ATOM 978 O OD1 . ASN A 1 122 ? 18.533 36.853 102.596 1.00 61.84 ? 122 ASN A OD1 1 ATOM 979 N ND2 . ASN A 1 122 ? 20.616 36.379 101.898 1.00 57.12 ? 122 ASN A ND2 1 ATOM 980 N N . ILE A 1 123 ? 19.731 38.205 97.153 1.00 48.81 ? 123 ILE A N 1 ATOM 981 C CA . ILE A 1 123 ? 19.332 38.047 95.756 1.00 44.44 ? 123 ILE A CA 1 ATOM 982 C C . ILE A 1 123 ? 20.430 37.714 94.759 1.00 43.78 ? 123 ILE A C 1 ATOM 983 O O . ILE A 1 123 ? 21.408 38.450 94.615 1.00 43.88 ? 123 ILE A O 1 ATOM 984 C CB . ILE A 1 123 ? 18.601 39.303 95.240 1.00 40.71 ? 123 ILE A CB 1 ATOM 985 C CG1 . ILE A 1 123 ? 17.461 39.690 96.190 1.00 37.47 ? 123 ILE A CG1 1 ATOM 986 C CG2 . ILE A 1 123 ? 18.066 39.045 93.849 1.00 39.33 ? 123 ILE A CG2 1 ATOM 987 C CD1 . ILE A 1 123 ? 16.505 38.555 96.516 1.00 36.60 ? 123 ILE A CD1 1 ATOM 988 N N . ARG A 1 124 ? 20.236 36.595 94.063 1.00 42.10 ? 124 ARG A N 1 ATOM 989 C CA . ARG A 1 124 ? 21.157 36.129 93.033 1.00 39.71 ? 124 ARG A CA 1 ATOM 990 C C . ARG A 1 124 ? 20.449 36.224 91.677 1.00 39.82 ? 124 ARG A C 1 ATOM 991 O O . ARG A 1 124 ? 19.246 35.985 91.575 1.00 41.25 ? 124 ARG A O 1 ATOM 992 C CB . ARG A 1 124 ? 21.572 34.686 93.304 1.00 36.46 ? 124 ARG A CB 1 ATOM 993 C CG . ARG A 1 124 ? 22.564 34.139 92.298 1.00 36.94 ? 124 ARG A CG 1 ATOM 994 C CD . ARG A 1 124 ? 23.255 32.902 92.839 1.00 37.45 ? 124 ARG A CD 1 ATOM 995 N NE . ARG A 1 124 ? 24.209 33.255 93.890 1.00 36.68 ? 124 ARG A NE 1 ATOM 996 C CZ . ARG A 1 124 ? 25.526 33.303 93.719 1.00 35.53 ? 124 ARG A CZ 1 ATOM 997 N NH1 . ARG A 1 124 ? 26.050 33.009 92.542 1.00 32.95 ? 124 ARG A NH1 1 ATOM 998 N NH2 . ARG A 1 124 ? 26.319 33.672 94.717 1.00 36.45 ? 124 ARG A NH2 1 ATOM 999 N N . ARG A 1 125 ? 21.192 36.578 90.638 1.00 38.15 ? 125 ARG A N 1 ATOM 1000 C CA . ARG A 1 125 ? 20.609 36.724 89.310 1.00 35.40 ? 125 ARG A CA 1 ATOM 1001 C C . ARG A 1 125 ? 21.112 35.697 88.297 1.00 33.85 ? 125 ARG A C 1 ATOM 1002 O O . ARG A 1 125 ? 22.294 35.374 88.274 1.00 33.72 ? 125 ARG A O 1 ATOM 1003 C CB . ARG A 1 125 ? 20.900 38.131 88.786 1.00 34.16 ? 125 ARG A CB 1 ATOM 1004 C CG . ARG A 1 125 ? 20.482 38.344 87.357 1.00 33.61 ? 125 ARG A CG 1 ATOM 1005 C CD . ARG A 1 125 ? 20.373 39.814 87.052 1.00 37.85 ? 125 ARG A CD 1 ATOM 1006 N NE . ARG A 1 125 ? 19.611 40.525 88.078 1.00 39.86 ? 125 ARG A NE 1 ATOM 1007 C CZ . ARG A 1 125 ? 19.103 41.745 87.922 1.00 40.66 ? 125 ARG A CZ 1 ATOM 1008 N NH1 . ARG A 1 125 ? 19.271 42.394 86.782 1.00 40.00 ? 125 ARG A NH1 1 ATOM 1009 N NH2 . ARG A 1 125 ? 18.414 42.320 88.897 1.00 42.70 ? 125 ARG A NH2 1 ATOM 1010 N N . ILE A 1 126 ? 20.214 35.177 87.467 1.00 30.92 ? 126 ILE A N 1 ATOM 1011 C CA . ILE A 1 126 ? 20.619 34.223 86.449 1.00 30.90 ? 126 ILE A CA 1 ATOM 1012 C C . ILE A 1 126 ? 20.187 34.683 85.076 1.00 31.12 ? 126 ILE A C 1 ATOM 1013 O O . ILE A 1 126 ? 19.099 35.220 84.900 1.00 29.55 ? 126 ILE A O 1 ATOM 1014 C CB . ILE A 1 126 ? 20.042 32.808 86.682 1.00 32.02 ? 126 ILE A CB 1 ATOM 1015 C CG1 . ILE A 1 126 ? 18.562 32.895 87.038 1.00 29.14 ? 126 ILE A CG1 1 ATOM 1016 C CG2 . ILE A 1 126 ? 20.843 32.082 87.749 1.00 33.29 ? 126 ILE A CG2 1 ATOM 1017 C CD1 . ILE A 1 126 ? 17.961 31.557 87.359 1.00 27.34 ? 126 ILE A CD1 1 ATOM 1018 N N . ILE A 1 127 ? 21.057 34.475 84.098 1.00 31.40 ? 127 ILE A N 1 ATOM 1019 C CA . ILE A 1 127 ? 20.747 34.855 82.739 1.00 31.21 ? 127 ILE A CA 1 ATOM 1020 C C . ILE A 1 127 ? 20.838 33.650 81.807 1.00 33.19 ? 127 ILE A C 1 ATOM 1021 O O . ILE A 1 127 ? 21.861 32.987 81.721 1.00 36.27 ? 127 ILE A O 1 ATOM 1022 C CB . ILE A 1 127 ? 21.680 35.962 82.252 1.00 28.46 ? 127 ILE A CB 1 ATOM 1023 C CG1 . ILE A 1 127 ? 21.363 37.250 83.003 1.00 26.30 ? 127 ILE A CG1 1 ATOM 1024 C CG2 . ILE A 1 127 ? 21.520 36.162 80.755 1.00 26.10 ? 127 ILE A CG2 1 ATOM 1025 C CD1 . ILE A 1 127 ? 22.323 38.364 82.691 1.00 28.24 ? 127 ILE A CD1 1 ATOM 1026 N N . CYS A 1 128 ? 19.731 33.376 81.130 1.00 32.67 ? 128 CYS A N 1 ATOM 1027 C CA . CYS A 1 128 ? 19.616 32.283 80.192 1.00 29.12 ? 128 CYS A CA 1 ATOM 1028 C C . CYS A 1 128 ? 19.589 32.894 78.804 1.00 26.65 ? 128 CYS A C 1 ATOM 1029 O O . CYS A 1 128 ? 18.741 33.715 78.506 1.00 27.91 ? 128 CYS A O 1 ATOM 1030 C CB . CYS A 1 128 ? 18.311 31.526 80.462 1.00 29.25 ? 128 CYS A CB 1 ATOM 1031 S SG . CYS A 1 128 ? 17.790 30.316 79.206 1.00 29.65 ? 128 CYS A SG 1 ATOM 1032 N N . SER A 1 129 ? 20.530 32.517 77.960 1.00 24.68 ? 129 SER A N 1 ATOM 1033 C CA . SER A 1 129 ? 20.543 33.037 76.609 1.00 25.71 ? 129 SER A CA 1 ATOM 1034 C C . SER A 1 129 ? 20.935 31.930 75.634 1.00 27.03 ? 129 SER A C 1 ATOM 1035 O O . SER A 1 129 ? 21.585 30.953 76.008 1.00 28.55 ? 129 SER A O 1 ATOM 1036 C CB . SER A 1 129 ? 21.518 34.218 76.502 1.00 26.80 ? 129 SER A CB 1 ATOM 1037 O OG . SER A 1 129 ? 22.805 33.869 76.974 1.00 29.21 ? 129 SER A OG 1 ATOM 1038 N N . THR A 1 130 ? 20.492 32.074 74.392 1.00 25.15 ? 130 THR A N 1 ATOM 1039 C CA . THR A 1 130 ? 20.801 31.127 73.333 1.00 24.61 ? 130 THR A CA 1 ATOM 1040 C C . THR A 1 130 ? 20.546 31.859 72.021 1.00 24.40 ? 130 THR A C 1 ATOM 1041 O O . THR A 1 130 ? 19.886 32.900 72.019 1.00 25.22 ? 130 THR A O 1 ATOM 1042 C CB . THR A 1 130 ? 19.912 29.897 73.400 1.00 26.08 ? 130 THR A CB 1 ATOM 1043 O OG1 . THR A 1 130 ? 20.128 29.105 72.222 1.00 27.60 ? 130 THR A OG1 1 ATOM 1044 C CG2 . THR A 1 130 ? 18.447 30.311 73.489 1.00 28.11 ? 130 THR A CG2 1 ATOM 1045 N N . SER A 1 131 ? 21.054 31.338 70.909 1.00 21.59 ? 131 SER A N 1 ATOM 1046 C CA . SER A 1 131 ? 20.858 32.033 69.643 1.00 23.31 ? 131 SER A CA 1 ATOM 1047 C C . SER A 1 131 ? 21.267 31.251 68.404 1.00 25.45 ? 131 SER A C 1 ATOM 1048 O O . SER A 1 131 ? 21.918 30.212 68.493 1.00 27.96 ? 131 SER A O 1 ATOM 1049 C CB . SER A 1 131 ? 21.613 33.365 69.657 1.00 23.49 ? 131 SER A CB 1 ATOM 1050 O OG . SER A 1 131 ? 23.007 33.171 69.800 1.00 16.90 ? 131 SER A OG 1 ATOM 1051 N N . GLY A 1 132 ? 20.887 31.777 67.246 1.00 25.10 ? 132 GLY A N 1 ATOM 1052 C CA . GLY A 1 132 ? 21.190 31.115 65.997 1.00 24.44 ? 132 GLY A CA 1 ATOM 1053 C C . GLY A 1 132 ? 20.024 30.227 65.639 1.00 26.75 ? 132 GLY A C 1 ATOM 1054 O O . GLY A 1 132 ? 20.157 29.315 64.825 1.00 27.63 ? 132 GLY A O 1 ATOM 1055 N N . GLY A 1 133 ? 18.873 30.494 66.257 1.00 29.16 ? 133 GLY A N 1 ATOM 1056 C CA . GLY A 1 133 ? 17.684 29.705 65.982 1.00 31.67 ? 133 GLY A CA 1 ATOM 1057 C C . GLY A 1 133 ? 16.574 30.383 65.187 1.00 31.35 ? 133 GLY A C 1 ATOM 1058 O O . GLY A 1 133 ? 16.642 31.573 64.898 1.00 31.58 ? 133 GLY A O 1 ATOM 1059 N N . PHE A 1 134 ? 15.552 29.604 64.833 1.00 30.98 ? 134 PHE A N 1 ATOM 1060 C CA . PHE A 1 134 ? 14.384 30.089 64.088 1.00 28.38 ? 134 PHE A CA 1 ATOM 1061 C C . PHE A 1 134 ? 13.240 29.060 64.197 1.00 28.64 ? 134 PHE A C 1 ATOM 1062 O O . PHE A 1 134 ? 13.478 27.839 64.176 1.00 27.11 ? 134 PHE A O 1 ATOM 1063 C CB . PHE A 1 134 ? 14.753 30.303 62.621 1.00 27.86 ? 134 PHE A CB 1 ATOM 1064 C CG . PHE A 1 134 ? 13.686 30.986 61.823 1.00 26.71 ? 134 PHE A CG 1 ATOM 1065 C CD1 . PHE A 1 134 ? 13.490 32.358 61.929 1.00 27.43 ? 134 PHE A CD1 1 ATOM 1066 C CD2 . PHE A 1 134 ? 12.870 30.258 60.967 1.00 26.05 ? 134 PHE A CD2 1 ATOM 1067 C CE1 . PHE A 1 134 ? 12.495 32.992 61.188 1.00 26.40 ? 134 PHE A CE1 1 ATOM 1068 C CE2 . PHE A 1 134 ? 11.873 30.879 60.222 1.00 22.63 ? 134 PHE A CE2 1 ATOM 1069 C CZ . PHE A 1 134 ? 11.685 32.242 60.330 1.00 24.66 ? 134 PHE A CZ 1 ATOM 1070 N N . PRO A 1 135 ? 11.981 29.531 64.285 1.00 28.20 ? 135 PRO A N 1 ATOM 1071 C CA . PRO A 1 135 ? 11.486 30.913 64.289 1.00 28.06 ? 135 PRO A CA 1 ATOM 1072 C C . PRO A 1 135 ? 11.728 31.680 65.585 1.00 29.75 ? 135 PRO A C 1 ATOM 1073 O O . PRO A 1 135 ? 12.528 31.270 66.429 1.00 29.54 ? 135 PRO A O 1 ATOM 1074 C CB . PRO A 1 135 ? 10.004 30.738 64.013 1.00 24.84 ? 135 PRO A CB 1 ATOM 1075 C CG . PRO A 1 135 ? 9.708 29.490 64.789 1.00 25.64 ? 135 PRO A CG 1 ATOM 1076 C CD . PRO A 1 135 ? 10.852 28.588 64.401 1.00 27.73 ? 135 PRO A CD 1 ATOM 1077 N N . GLU A 1 136 ? 11.014 32.794 65.735 1.00 28.42 ? 136 GLU A N 1 ATOM 1078 C CA . GLU A 1 136 ? 11.152 33.624 66.918 1.00 27.19 ? 136 GLU A CA 1 ATOM 1079 C C . GLU A 1 136 ? 10.906 32.781 68.163 1.00 27.59 ? 136 GLU A C 1 ATOM 1080 O O . GLU A 1 136 ? 9.896 32.086 68.269 1.00 28.30 ? 136 GLU A O 1 ATOM 1081 C CB . GLU A 1 136 ? 10.164 34.790 66.867 1.00 27.22 ? 136 GLU A CB 1 ATOM 1082 C CG . GLU A 1 136 ? 10.374 35.834 67.952 1.00 28.42 ? 136 GLU A CG 1 ATOM 1083 C CD . GLU A 1 136 ? 9.082 36.465 68.429 1.00 31.18 ? 136 GLU A CD 1 ATOM 1084 O OE1 . GLU A 1 136 ? 8.278 36.924 67.589 1.00 33.11 ? 136 GLU A OE1 1 ATOM 1085 O OE2 . GLU A 1 136 ? 8.879 36.508 69.657 1.00 32.50 ? 136 GLU A OE2 1 ATOM 1086 N N . PRO A 1 137 ? 11.840 32.836 69.120 1.00 28.95 ? 137 PRO A N 1 ATOM 1087 C CA . PRO A 1 137 ? 11.851 32.126 70.406 1.00 30.27 ? 137 PRO A CA 1 ATOM 1088 C C . PRO A 1 137 ? 11.000 32.724 71.525 1.00 31.40 ? 137 PRO A C 1 ATOM 1089 O O . PRO A 1 137 ? 10.769 33.929 71.573 1.00 34.35 ? 137 PRO A O 1 ATOM 1090 C CB . PRO A 1 137 ? 13.325 32.130 70.770 1.00 27.91 ? 137 PRO A CB 1 ATOM 1091 C CG . PRO A 1 137 ? 13.749 33.470 70.261 1.00 29.97 ? 137 PRO A CG 1 ATOM 1092 C CD . PRO A 1 137 ? 13.122 33.530 68.903 1.00 30.90 ? 137 PRO A CD 1 ATOM 1093 N N . HIS A 1 138 ? 10.536 31.865 72.423 1.00 30.22 ? 138 HIS A N 1 ATOM 1094 C CA . HIS A 1 138 ? 9.742 32.306 73.555 1.00 31.99 ? 138 HIS A CA 1 ATOM 1095 C C . HIS A 1 138 ? 10.317 31.694 74.817 1.00 32.17 ? 138 HIS A C 1 ATOM 1096 O O . HIS A 1 138 ? 10.266 30.485 75.027 1.00 31.26 ? 138 HIS A O 1 ATOM 1097 C CB . HIS A 1 138 ? 8.275 31.937 73.362 1.00 34.29 ? 138 HIS A CB 1 ATOM 1098 C CG . HIS A 1 138 ? 7.601 32.745 72.299 1.00 37.19 ? 138 HIS A CG 1 ATOM 1099 N ND1 . HIS A 1 138 ? 7.742 32.474 70.954 1.00 37.98 ? 138 HIS A ND1 1 ATOM 1100 C CD2 . HIS A 1 138 ? 6.830 33.856 72.379 1.00 39.42 ? 138 HIS A CD2 1 ATOM 1101 C CE1 . HIS A 1 138 ? 7.086 33.383 70.253 1.00 41.33 ? 138 HIS A CE1 1 ATOM 1102 N NE2 . HIS A 1 138 ? 6.523 34.233 71.094 1.00 40.98 ? 138 HIS A NE2 1 ATOM 1103 N N . LEU A 1 139 ? 10.877 32.558 75.652 1.00 31.81 ? 139 LEU A N 1 ATOM 1104 C CA . LEU A 1 139 ? 11.526 32.129 76.871 1.00 32.83 ? 139 LEU A CA 1 ATOM 1105 C C . LEU A 1 139 ? 10.635 32.251 78.101 1.00 34.03 ? 139 LEU A C 1 ATOM 1106 O O . LEU A 1 139 ? 9.890 33.217 78.259 1.00 34.16 ? 139 LEU A O 1 ATOM 1107 C CB . LEU A 1 139 ? 12.828 32.921 77.025 1.00 30.12 ? 139 LEU A CB 1 ATOM 1108 C CG . LEU A 1 139 ? 13.838 32.542 78.094 1.00 28.80 ? 139 LEU A CG 1 ATOM 1109 C CD1 . LEU A 1 139 ? 15.172 33.087 77.678 1.00 28.23 ? 139 LEU A CD1 1 ATOM 1110 C CD2 . LEU A 1 139 ? 13.424 33.095 79.455 1.00 29.96 ? 139 LEU A CD2 1 ATOM 1111 N N . SER A 1 140 ? 10.711 31.244 78.963 1.00 34.34 ? 140 SER A N 1 ATOM 1112 C CA . SER A 1 140 ? 9.912 31.203 80.176 1.00 34.44 ? 140 SER A CA 1 ATOM 1113 C C . SER A 1 140 ? 10.687 30.504 81.280 1.00 32.66 ? 140 SER A C 1 ATOM 1114 O O . SER A 1 140 ? 11.374 29.519 81.033 1.00 31.84 ? 140 SER A O 1 ATOM 1115 C CB . SER A 1 140 ? 8.594 30.458 79.916 1.00 37.62 ? 140 SER A CB 1 ATOM 1116 O OG . SER A 1 140 ? 8.818 29.132 79.445 1.00 38.74 ? 140 SER A OG 1 ATOM 1117 N N . TRP A 1 141 ? 10.578 31.029 82.495 1.00 31.44 ? 141 TRP A N 1 ATOM 1118 C CA . TRP A 1 141 ? 11.254 30.457 83.644 1.00 29.60 ? 141 TRP A CA 1 ATOM 1119 C C . TRP A 1 141 ? 10.290 29.568 84.411 1.00 30.99 ? 141 TRP A C 1 ATOM 1120 O O . TRP A 1 141 ? 9.133 29.915 84.612 1.00 29.32 ? 141 TRP A O 1 ATOM 1121 C CB . TRP A 1 141 ? 11.774 31.560 84.553 1.00 28.01 ? 141 TRP A CB 1 ATOM 1122 C CG . TRP A 1 141 ? 12.819 32.379 83.906 1.00 32.84 ? 141 TRP A CG 1 ATOM 1123 C CD1 . TRP A 1 141 ? 12.647 33.525 83.181 1.00 34.62 ? 141 TRP A CD1 1 ATOM 1124 C CD2 . TRP A 1 141 ? 14.228 32.123 83.932 1.00 34.53 ? 141 TRP A CD2 1 ATOM 1125 N NE1 . TRP A 1 141 ? 13.868 34.006 82.759 1.00 35.47 ? 141 TRP A NE1 1 ATOM 1126 C CE2 . TRP A 1 141 ? 14.854 33.170 83.208 1.00 35.54 ? 141 TRP A CE2 1 ATOM 1127 C CE3 . TRP A 1 141 ? 15.023 31.118 84.500 1.00 32.41 ? 141 TRP A CE3 1 ATOM 1128 C CZ2 . TRP A 1 141 ? 16.237 33.233 83.044 1.00 35.92 ? 141 TRP A CZ2 1 ATOM 1129 C CZ3 . TRP A 1 141 ? 16.398 31.185 84.335 1.00 33.38 ? 141 TRP A CZ3 1 ATOM 1130 C CH2 . TRP A 1 141 ? 16.991 32.237 83.615 1.00 36.01 ? 141 TRP A CH2 1 ATOM 1131 N N . LEU A 1 142 ? 10.777 28.412 84.836 1.00 32.51 ? 142 LEU A N 1 ATOM 1132 C CA . LEU A 1 142 ? 9.954 27.476 85.565 1.00 33.53 ? 142 LEU A CA 1 ATOM 1133 C C . LEU A 1 142 ? 10.483 27.176 86.963 1.00 37.31 ? 142 LEU A C 1 ATOM 1134 O O . LEU A 1 142 ? 11.697 27.086 87.192 1.00 38.60 ? 142 LEU A O 1 ATOM 1135 C CB . LEU A 1 142 ? 9.850 26.176 84.774 1.00 31.55 ? 142 LEU A CB 1 ATOM 1136 C CG . LEU A 1 142 ? 9.132 26.253 83.431 1.00 31.21 ? 142 LEU A CG 1 ATOM 1137 C CD1 . LEU A 1 142 ? 9.222 24.925 82.714 1.00 31.87 ? 142 LEU A CD1 1 ATOM 1138 C CD2 . LEU A 1 142 ? 7.680 26.604 83.654 1.00 32.46 ? 142 LEU A CD2 1 ATOM 1139 N N . GLU A 1 143 ? 9.552 27.033 87.897 1.00 39.39 ? 143 GLU A N 1 ATOM 1140 C CA . GLU A 1 143 ? 9.871 26.679 89.273 1.00 41.30 ? 143 GLU A CA 1 ATOM 1141 C C . GLU A 1 143 ? 8.717 25.845 89.799 1.00 42.84 ? 143 GLU A C 1 ATOM 1142 O O . GLU A 1 143 ? 7.629 26.366 90.070 1.00 43.00 ? 143 GLU A O 1 ATOM 1143 C CB . GLU A 1 143 ? 10.050 27.912 90.155 1.00 40.78 ? 143 GLU A CB 1 ATOM 1144 C CG . GLU A 1 143 ? 10.113 27.573 91.635 1.00 39.56 ? 143 GLU A CG 1 ATOM 1145 C CD . GLU A 1 143 ? 11.188 28.343 92.362 1.00 41.95 ? 143 GLU A CD 1 ATOM 1146 O OE1 . GLU A 1 143 ? 11.167 29.594 92.301 1.00 42.94 ? 143 GLU A OE1 1 ATOM 1147 O OE2 . GLU A 1 143 ? 12.059 27.700 92.994 1.00 42.46 ? 143 GLU A OE2 1 ATOM 1148 N N . ASN A 1 144 ? 8.960 24.547 89.927 1.00 43.96 ? 144 ASN A N 1 ATOM 1149 C CA . ASN A 1 144 ? 7.937 23.638 90.409 1.00 46.35 ? 144 ASN A CA 1 ATOM 1150 C C . ASN A 1 144 ? 6.774 23.640 89.437 1.00 45.10 ? 144 ASN A C 1 ATOM 1151 O O . ASN A 1 144 ? 5.632 23.829 89.851 1.00 44.90 ? 144 ASN A O 1 ATOM 1152 C CB . ASN A 1 144 ? 7.430 24.080 91.784 1.00 50.85 ? 144 ASN A CB 1 ATOM 1153 C CG . ASN A 1 144 ? 6.371 23.140 92.337 1.00 55.78 ? 144 ASN A CG 1 ATOM 1154 O OD1 . ASN A 1 144 ? 6.682 22.012 92.729 1.00 57.51 ? 144 ASN A OD1 1 ATOM 1155 N ND2 . ASN A 1 144 ? 5.108 23.591 92.358 1.00 55.48 ? 144 ASN A ND2 1 ATOM 1156 N N . GLY A 1 145 ? 7.064 23.434 88.156 1.00 45.05 ? 145 GLY A N 1 ATOM 1157 C CA . GLY A 1 145 ? 6.015 23.427 87.147 1.00 47.39 ? 145 GLY A CA 1 ATOM 1158 C C . GLY A 1 145 ? 5.150 24.676 87.213 1.00 49.37 ? 145 GLY A C 1 ATOM 1159 O O . GLY A 1 145 ? 3.940 24.625 86.958 1.00 49.14 ? 145 GLY A O 1 ATOM 1160 N N . GLU A 1 146 ? 5.785 25.797 87.562 1.00 50.08 ? 146 GLU A N 1 ATOM 1161 C CA . GLU A 1 146 ? 5.121 27.089 87.679 1.00 49.66 ? 146 GLU A CA 1 ATOM 1162 C C . GLU A 1 146 ? 5.934 28.104 86.886 1.00 47.98 ? 146 GLU A C 1 ATOM 1163 O O . GLU A 1 146 ? 7.164 28.094 86.958 1.00 47.96 ? 146 GLU A O 1 ATOM 1164 C CB . GLU A 1 146 ? 5.062 27.504 89.150 1.00 52.79 ? 146 GLU A CB 1 ATOM 1165 C CG . GLU A 1 146 ? 3.676 27.929 89.620 1.00 59.92 ? 146 GLU A CG 1 ATOM 1166 C CD . GLU A 1 146 ? 2.670 26.783 89.607 1.00 62.70 ? 146 GLU A CD 1 ATOM 1167 O OE1 . GLU A 1 146 ? 2.631 26.001 90.586 1.00 63.85 ? 146 GLU A OE1 1 ATOM 1168 O OE2 . GLU A 1 146 ? 1.924 26.659 88.609 1.00 65.07 ? 146 GLU A OE2 1 ATOM 1169 N N . GLU A 1 147 ? 5.250 28.969 86.134 1.00 45.58 ? 147 GLU A N 1 ATOM 1170 C CA . GLU A 1 147 ? 5.923 29.982 85.317 1.00 44.40 ? 147 GLU A CA 1 ATOM 1171 C C . GLU A 1 147 ? 6.182 31.290 86.036 1.00 41.82 ? 147 GLU A C 1 ATOM 1172 O O . GLU A 1 147 ? 5.270 32.086 86.233 1.00 42.98 ? 147 GLU A O 1 ATOM 1173 C CB . GLU A 1 147 ? 5.114 30.307 84.072 1.00 46.86 ? 147 GLU A CB 1 ATOM 1174 C CG . GLU A 1 147 ? 4.864 29.141 83.169 1.00 53.33 ? 147 GLU A CG 1 ATOM 1175 C CD . GLU A 1 147 ? 4.127 29.555 81.915 1.00 58.46 ? 147 GLU A CD 1 ATOM 1176 O OE1 . GLU A 1 147 ? 4.732 30.258 81.067 1.00 61.27 ? 147 GLU A OE1 1 ATOM 1177 O OE2 . GLU A 1 147 ? 2.935 29.191 81.784 1.00 60.10 ? 147 GLU A OE2 1 ATOM 1178 N N . LEU A 1 148 ? 7.437 31.525 86.391 1.00 38.33 ? 148 LEU A N 1 ATOM 1179 C CA . LEU A 1 148 ? 7.822 32.744 87.077 1.00 34.93 ? 148 LEU A CA 1 ATOM 1180 C C . LEU A 1 148 ? 7.873 33.905 86.091 1.00 31.83 ? 148 LEU A C 1 ATOM 1181 O O . LEU A 1 148 ? 7.950 33.697 84.887 1.00 30.43 ? 148 LEU A O 1 ATOM 1182 C CB . LEU A 1 148 ? 9.196 32.555 87.720 1.00 36.13 ? 148 LEU A CB 1 ATOM 1183 C CG . LEU A 1 148 ? 9.322 31.231 88.468 1.00 35.35 ? 148 LEU A CG 1 ATOM 1184 C CD1 . LEU A 1 148 ? 10.739 31.047 88.987 1.00 35.08 ? 148 LEU A CD1 1 ATOM 1185 C CD2 . LEU A 1 148 ? 8.298 31.207 89.585 1.00 35.17 ? 148 LEU A CD2 1 ATOM 1186 N N . ASN A 1 149 ? 7.827 35.125 86.615 1.00 31.33 ? 149 ASN A N 1 ATOM 1187 C CA . ASN A 1 149 ? 7.888 36.324 85.787 1.00 29.28 ? 149 ASN A CA 1 ATOM 1188 C C . ASN A 1 149 ? 9.334 36.670 85.557 1.00 27.26 ? 149 ASN A C 1 ATOM 1189 O O . ASN A 1 149 ? 10.137 36.588 86.477 1.00 26.39 ? 149 ASN A O 1 ATOM 1190 C CB . ASN A 1 149 ? 7.229 37.516 86.480 1.00 29.68 ? 149 ASN A CB 1 ATOM 1191 C CG . ASN A 1 149 ? 5.734 37.384 86.580 1.00 28.58 ? 149 ASN A CG 1 ATOM 1192 O OD1 . ASN A 1 149 ? 5.022 37.280 85.572 1.00 28.05 ? 149 ASN A OD1 1 ATOM 1193 N ND2 . ASN A 1 149 ? 5.241 37.395 87.806 1.00 29.10 ? 149 ASN A ND2 1 ATOM 1194 N N . ALA A 1 150 ? 9.649 37.080 84.331 1.00 27.09 ? 150 ALA A N 1 ATOM 1195 C CA . ALA A 1 150 ? 11.008 37.451 83.952 1.00 27.32 ? 150 ALA A CA 1 ATOM 1196 C C . ALA A 1 150 ? 11.329 38.914 84.246 1.00 27.84 ? 150 ALA A C 1 ATOM 1197 O O . ALA A 1 150 ? 10.513 39.804 84.007 1.00 26.03 ? 150 ALA A O 1 ATOM 1198 C CB . ALA A 1 150 ? 11.223 37.167 82.477 1.00 24.08 ? 150 ALA A CB 1 ATOM 1199 N N . ILE A 1 151 ? 12.532 39.145 84.760 1.00 30.13 ? 151 ILE A N 1 ATOM 1200 C CA . ILE A 1 151 ? 13.012 40.488 85.077 1.00 32.58 ? 151 ILE A CA 1 ATOM 1201 C C . ILE A 1 151 ? 13.252 41.305 83.799 1.00 35.57 ? 151 ILE A C 1 ATOM 1202 O O . ILE A 1 151 ? 12.804 42.447 83.692 1.00 38.03 ? 151 ILE A O 1 ATOM 1203 C CB . ILE A 1 151 ? 14.338 40.415 85.854 1.00 31.70 ? 151 ILE A CB 1 ATOM 1204 C CG1 . ILE A 1 151 ? 14.156 39.542 87.091 1.00 34.06 ? 151 ILE A CG1 1 ATOM 1205 C CG2 . ILE A 1 151 ? 14.813 41.795 86.226 1.00 30.43 ? 151 ILE A CG2 1 ATOM 1206 C CD1 . ILE A 1 151 ? 12.969 39.927 87.941 1.00 38.24 ? 151 ILE A CD1 1 ATOM 1207 N N . ASN A 1 152 ? 13.950 40.705 82.833 1.00 34.70 ? 152 ASN A N 1 ATOM 1208 C CA . ASN A 1 152 ? 14.287 41.356 81.564 1.00 33.11 ? 152 ASN A CA 1 ATOM 1209 C C . ASN A 1 152 ? 14.369 40.276 80.464 1.00 32.78 ? 152 ASN A C 1 ATOM 1210 O O . ASN A 1 152 ? 14.900 39.195 80.701 1.00 35.13 ? 152 ASN A O 1 ATOM 1211 C CB . ASN A 1 152 ? 15.651 42.048 81.730 1.00 33.10 ? 152 ASN A CB 1 ATOM 1212 C CG . ASN A 1 152 ? 16.080 42.848 80.512 1.00 35.03 ? 152 ASN A CG 1 ATOM 1213 O OD1 . ASN A 1 152 ? 15.817 42.468 79.377 1.00 39.73 ? 152 ASN A OD1 1 ATOM 1214 N ND2 . ASN A 1 152 ? 16.778 43.954 80.755 1.00 36.59 ? 152 ASN A ND2 1 ATOM 1215 N N . THR A 1 153 ? 13.829 40.542 79.276 1.00 27.45 ? 153 THR A N 1 ATOM 1216 C CA . THR A 1 153 ? 13.928 39.571 78.200 1.00 26.94 ? 153 THR A CA 1 ATOM 1217 C C . THR A 1 153 ? 13.985 40.230 76.844 1.00 29.01 ? 153 THR A C 1 ATOM 1218 O O . THR A 1 153 ? 12.983 40.716 76.331 1.00 31.85 ? 153 THR A O 1 ATOM 1219 C CB . THR A 1 153 ? 12.769 38.578 78.185 1.00 26.05 ? 153 THR A CB 1 ATOM 1220 O OG1 . THR A 1 153 ? 12.648 37.987 79.473 1.00 32.91 ? 153 THR A OG1 1 ATOM 1221 C CG2 . THR A 1 153 ? 13.037 37.456 77.183 1.00 20.95 ? 153 THR A CG2 1 ATOM 1222 N N . THR A 1 154 ? 15.172 40.220 76.254 1.00 29.10 ? 154 THR A N 1 ATOM 1223 C CA . THR A 1 154 ? 15.383 40.811 74.947 1.00 27.95 ? 154 THR A CA 1 ATOM 1224 C C . THR A 1 154 ? 15.314 39.716 73.900 1.00 27.84 ? 154 THR A C 1 ATOM 1225 O O . THR A 1 154 ? 15.683 38.581 74.169 1.00 30.27 ? 154 THR A O 1 ATOM 1226 C CB . THR A 1 154 ? 16.752 41.488 74.889 1.00 27.48 ? 154 THR A CB 1 ATOM 1227 O OG1 . THR A 1 154 ? 17.424 41.294 76.138 1.00 31.75 ? 154 THR A OG1 1 ATOM 1228 C CG2 . THR A 1 154 ? 16.604 42.962 74.635 1.00 23.55 ? 154 THR A CG2 1 ATOM 1229 N N . VAL A 1 155 ? 14.834 40.066 72.711 1.00 26.90 ? 155 VAL A N 1 ATOM 1230 C CA . VAL A 1 155 ? 14.712 39.131 71.595 1.00 25.99 ? 155 VAL A CA 1 ATOM 1231 C C . VAL A 1 155 ? 14.876 39.902 70.289 1.00 28.03 ? 155 VAL A C 1 ATOM 1232 O O . VAL A 1 155 ? 14.088 40.795 69.988 1.00 31.50 ? 155 VAL A O 1 ATOM 1233 C CB . VAL A 1 155 ? 13.333 38.425 71.620 1.00 24.22 ? 155 VAL A CB 1 ATOM 1234 C CG1 . VAL A 1 155 ? 12.897 38.034 70.220 1.00 24.54 ? 155 VAL A CG1 1 ATOM 1235 C CG2 . VAL A 1 155 ? 13.424 37.189 72.482 1.00 25.07 ? 155 VAL A CG2 1 ATOM 1236 N N . SER A 1 156 ? 15.901 39.580 69.509 1.00 28.52 ? 156 SER A N 1 ATOM 1237 C CA . SER A 1 156 ? 16.095 40.307 68.254 1.00 30.14 ? 156 SER A CA 1 ATOM 1238 C C . SER A 1 156 ? 16.445 39.380 67.122 1.00 29.83 ? 156 SER A C 1 ATOM 1239 O O . SER A 1 156 ? 16.860 38.245 67.347 1.00 31.76 ? 156 SER A O 1 ATOM 1240 C CB . SER A 1 156 ? 17.191 41.371 68.393 1.00 29.09 ? 156 SER A CB 1 ATOM 1241 O OG . SER A 1 156 ? 18.457 40.796 68.662 1.00 24.14 ? 156 SER A OG 1 ATOM 1242 N N . GLN A 1 157 ? 16.270 39.870 65.902 1.00 27.99 ? 157 GLN A N 1 ATOM 1243 C CA . GLN A 1 157 ? 16.561 39.072 64.730 1.00 28.59 ? 157 GLN A CA 1 ATOM 1244 C C . GLN A 1 157 ? 17.604 39.715 63.834 1.00 29.90 ? 157 GLN A C 1 ATOM 1245 O O . GLN A 1 157 ? 17.527 40.896 63.484 1.00 28.56 ? 157 GLN A O 1 ATOM 1246 C CB . GLN A 1 157 ? 15.284 38.807 63.935 1.00 27.13 ? 157 GLN A CB 1 ATOM 1247 C CG . GLN A 1 157 ? 15.500 37.924 62.734 1.00 26.16 ? 157 GLN A CG 1 ATOM 1248 C CD . GLN A 1 157 ? 14.257 37.770 61.917 1.00 27.61 ? 157 GLN A CD 1 ATOM 1249 O OE1 . GLN A 1 157 ? 13.559 38.750 61.656 1.00 31.07 ? 157 GLN A OE1 1 ATOM 1250 N NE2 . GLN A 1 157 ? 13.973 36.546 61.482 1.00 27.17 ? 157 GLN A NE2 1 ATOM 1251 N N . ASP A 1 158 ? 18.591 38.913 63.467 1.00 32.63 ? 158 ASP A N 1 ATOM 1252 C CA . ASP A 1 158 ? 19.658 39.391 62.620 1.00 33.97 ? 158 ASP A CA 1 ATOM 1253 C C . ASP A 1 158 ? 19.130 39.601 61.215 1.00 35.58 ? 158 ASP A C 1 ATOM 1254 O O . ASP A 1 158 ? 18.582 38.683 60.599 1.00 32.95 ? 158 ASP A O 1 ATOM 1255 C CB . ASP A 1 158 ? 20.796 38.387 62.590 1.00 34.97 ? 158 ASP A CB 1 ATOM 1256 C CG . ASP A 1 158 ? 22.104 39.027 62.250 1.00 34.77 ? 158 ASP A CG 1 ATOM 1257 O OD1 . ASP A 1 158 ? 22.120 39.823 61.283 1.00 33.97 ? 158 ASP A OD1 1 ATOM 1258 O OD2 . ASP A 1 158 ? 23.101 38.730 62.951 1.00 32.11 ? 158 ASP A OD2 1 ATOM 1259 N N . PRO A 1 159 ? 19.287 40.828 60.691 1.00 37.29 ? 159 PRO A N 1 ATOM 1260 C CA . PRO A 1 159 ? 18.835 41.204 59.347 1.00 37.26 ? 159 PRO A CA 1 ATOM 1261 C C . PRO A 1 159 ? 19.572 40.361 58.309 1.00 37.64 ? 159 PRO A C 1 ATOM 1262 O O . PRO A 1 159 ? 19.035 40.011 57.265 1.00 37.05 ? 159 PRO A O 1 ATOM 1263 C CB . PRO A 1 159 ? 19.224 42.677 59.256 1.00 36.12 ? 159 PRO A CB 1 ATOM 1264 C CG . PRO A 1 159 ? 19.336 43.117 60.677 1.00 33.94 ? 159 PRO A CG 1 ATOM 1265 C CD . PRO A 1 159 ? 19.968 41.958 61.346 1.00 34.80 ? 159 PRO A CD 1 ATOM 1266 N N . GLU A 1 160 ? 20.820 40.052 58.634 1.00 39.23 ? 160 GLU A N 1 ATOM 1267 C CA . GLU A 1 160 ? 21.697 39.267 57.786 1.00 41.74 ? 160 GLU A CA 1 ATOM 1268 C C . GLU A 1 160 ? 21.347 37.779 57.803 1.00 40.21 ? 160 GLU A C 1 ATOM 1269 O O . GLU A 1 160 ? 20.771 37.256 56.855 1.00 40.46 ? 160 GLU A O 1 ATOM 1270 C CB . GLU A 1 160 ? 23.142 39.484 58.246 1.00 45.63 ? 160 GLU A CB 1 ATOM 1271 C CG . GLU A 1 160 ? 23.875 40.571 57.490 1.00 51.21 ? 160 GLU A CG 1 ATOM 1272 C CD . GLU A 1 160 ? 24.609 40.015 56.283 1.00 56.12 ? 160 GLU A CD 1 ATOM 1273 O OE1 . GLU A 1 160 ? 25.662 39.364 56.482 1.00 58.10 ? 160 GLU A OE1 1 ATOM 1274 O OE2 . GLU A 1 160 ? 24.132 40.211 55.141 1.00 57.15 ? 160 GLU A OE2 1 ATOM 1275 N N . THR A 1 161 ? 21.697 37.110 58.893 1.00 38.30 ? 161 THR A N 1 ATOM 1276 C CA . THR A 1 161 ? 21.438 35.693 59.052 1.00 35.28 ? 161 THR A CA 1 ATOM 1277 C C . THR A 1 161 ? 19.952 35.366 59.126 1.00 34.98 ? 161 THR A C 1 ATOM 1278 O O . THR A 1 161 ? 19.555 34.233 58.867 1.00 35.74 ? 161 THR A O 1 ATOM 1279 C CB . THR A 1 161 ? 22.103 35.166 60.323 1.00 36.97 ? 161 THR A CB 1 ATOM 1280 O OG1 . THR A 1 161 ? 21.506 35.778 61.473 1.00 34.27 ? 161 THR A OG1 1 ATOM 1281 C CG2 . THR A 1 161 ? 23.578 35.486 60.308 1.00 40.22 ? 161 THR A CG2 1 ATOM 1282 N N . GLU A 1 162 ? 19.135 36.351 59.492 1.00 34.58 ? 162 GLU A N 1 ATOM 1283 C CA . GLU A 1 162 ? 17.688 36.151 59.609 1.00 31.56 ? 162 GLU A CA 1 ATOM 1284 C C . GLU A 1 162 ? 17.374 35.299 60.845 1.00 31.53 ? 162 GLU A C 1 ATOM 1285 O O . GLU A 1 162 ? 16.257 34.807 61.008 1.00 30.63 ? 162 GLU A O 1 ATOM 1286 C CB . GLU A 1 162 ? 17.171 35.475 58.336 1.00 26.31 ? 162 GLU A CB 1 ATOM 1287 C CG . GLU A 1 162 ? 15.696 35.188 58.285 1.00 20.26 ? 162 GLU A CG 1 ATOM 1288 C CD . GLU A 1 162 ? 15.229 34.913 56.862 1.00 24.24 ? 162 GLU A CD 1 ATOM 1289 O OE1 . GLU A 1 162 ? 14.625 33.851 56.625 1.00 22.41 ? 162 GLU A OE1 1 ATOM 1290 O OE2 . GLU A 1 162 ? 15.460 35.767 55.972 1.00 24.70 ? 162 GLU A OE2 1 ATOM 1291 N N . LEU A 1 163 ? 18.369 35.161 61.722 1.00 29.53 ? 163 LEU A N 1 ATOM 1292 C CA . LEU A 1 163 ? 18.239 34.355 62.923 1.00 26.61 ? 163 LEU A CA 1 ATOM 1293 C C . LEU A 1 163 ? 18.014 35.156 64.196 1.00 25.76 ? 163 LEU A C 1 ATOM 1294 O O . LEU A 1 163 ? 18.355 36.341 64.274 1.00 23.39 ? 163 LEU A O 1 ATOM 1295 C CB . LEU A 1 163 ? 19.476 33.471 63.062 1.00 26.58 ? 163 LEU A CB 1 ATOM 1296 C CG . LEU A 1 163 ? 19.729 32.631 61.805 1.00 29.35 ? 163 LEU A CG 1 ATOM 1297 C CD1 . LEU A 1 163 ? 21.098 31.971 61.870 1.00 28.37 ? 163 LEU A CD1 1 ATOM 1298 C CD2 . LEU A 1 163 ? 18.622 31.591 61.662 1.00 29.68 ? 163 LEU A CD2 1 ATOM 1299 N N . TYR A 1 164 ? 17.460 34.473 65.199 1.00 24.21 ? 164 TYR A N 1 ATOM 1300 C CA . TYR A 1 164 ? 17.122 35.063 66.493 1.00 23.57 ? 164 TYR A CA 1 ATOM 1301 C C . TYR A 1 164 ? 18.098 34.813 67.626 1.00 24.55 ? 164 TYR A C 1 ATOM 1302 O O . TYR A 1 164 ? 18.904 33.891 67.576 1.00 26.78 ? 164 TYR A O 1 ATOM 1303 C CB . TYR A 1 164 ? 15.744 34.572 66.949 1.00 24.30 ? 164 TYR A CB 1 ATOM 1304 C CG . TYR A 1 164 ? 14.588 35.187 66.210 1.00 22.42 ? 164 TYR A CG 1 ATOM 1305 C CD1 . TYR A 1 164 ? 14.073 34.593 65.058 1.00 21.68 ? 164 TYR A CD1 1 ATOM 1306 C CD2 . TYR A 1 164 ? 14.026 36.386 66.653 1.00 21.61 ? 164 TYR A CD2 1 ATOM 1307 C CE1 . TYR A 1 164 ? 13.027 35.178 64.368 1.00 23.99 ? 164 TYR A CE1 1 ATOM 1308 C CE2 . TYR A 1 164 ? 12.988 36.981 65.977 1.00 22.79 ? 164 TYR A CE2 1 ATOM 1309 C CZ . TYR A 1 164 ? 12.487 36.375 64.838 1.00 24.73 ? 164 TYR A CZ 1 ATOM 1310 O OH . TYR A 1 164 ? 11.424 36.953 64.193 1.00 25.59 ? 164 TYR A OH 1 ATOM 1311 N N . ALA A 1 165 ? 17.989 35.643 68.661 1.00 23.77 ? 165 ALA A N 1 ATOM 1312 C CA . ALA A 1 165 ? 18.832 35.563 69.856 1.00 25.18 ? 165 ALA A CA 1 ATOM 1313 C C . ALA A 1 165 ? 18.012 36.011 71.070 1.00 26.39 ? 165 ALA A C 1 ATOM 1314 O O . ALA A 1 165 ? 17.523 37.138 71.109 1.00 30.41 ? 165 ALA A O 1 ATOM 1315 C CB . ALA A 1 165 ? 20.076 36.461 69.697 1.00 21.19 ? 165 ALA A CB 1 ATOM 1316 N N . VAL A 1 166 ? 17.861 35.132 72.055 1.00 24.92 ? 166 VAL A N 1 ATOM 1317 C CA . VAL A 1 166 ? 17.099 35.453 73.258 1.00 23.43 ? 166 VAL A CA 1 ATOM 1318 C C . VAL A 1 166 ? 17.997 35.546 74.465 1.00 24.35 ? 166 VAL A C 1 ATOM 1319 O O . VAL A 1 166 ? 18.988 34.829 74.573 1.00 28.12 ? 166 VAL A O 1 ATOM 1320 C CB . VAL A 1 166 ? 16.123 34.365 73.633 1.00 23.55 ? 166 VAL A CB 1 ATOM 1321 C CG1 . VAL A 1 166 ? 15.038 34.929 74.500 1.00 24.03 ? 166 VAL A CG1 1 ATOM 1322 C CG2 . VAL A 1 166 ? 15.606 33.708 72.426 1.00 27.29 ? 166 VAL A CG2 1 ATOM 1323 N N . SER A 1 167 ? 17.618 36.402 75.396 1.00 22.30 ? 167 SER A N 1 ATOM 1324 C CA . SER A 1 167 ? 18.368 36.553 76.620 1.00 20.21 ? 167 SER A CA 1 ATOM 1325 C C . SER A 1 167 ? 17.436 37.109 77.693 1.00 22.26 ? 167 SER A C 1 ATOM 1326 O O . SER A 1 167 ? 16.842 38.176 77.522 1.00 23.19 ? 167 SER A O 1 ATOM 1327 C CB . SER A 1 167 ? 19.555 37.473 76.398 1.00 15.91 ? 167 SER A CB 1 ATOM 1328 O OG . SER A 1 167 ? 20.434 37.403 77.502 1.00 13.48 ? 167 SER A OG 1 ATOM 1329 N N . SER A 1 168 ? 17.298 36.379 78.793 1.00 20.04 ? 168 SER A N 1 ATOM 1330 C CA . SER A 1 168 ? 16.429 36.820 79.866 1.00 21.43 ? 168 SER A CA 1 ATOM 1331 C C . SER A 1 168 ? 17.098 36.678 81.226 1.00 22.84 ? 168 SER A C 1 ATOM 1332 O O . SER A 1 168 ? 17.869 35.753 81.454 1.00 22.70 ? 168 SER A O 1 ATOM 1333 C CB . SER A 1 168 ? 15.116 36.033 79.828 1.00 21.88 ? 168 SER A CB 1 ATOM 1334 O OG . SER A 1 168 ? 14.345 36.276 80.988 1.00 20.30 ? 168 SER A OG 1 ATOM 1335 N N . LYS A 1 169 ? 16.792 37.619 82.115 1.00 23.00 ? 169 LYS A N 1 ATOM 1336 C CA . LYS A 1 169 ? 17.339 37.666 83.470 1.00 21.95 ? 169 LYS A CA 1 ATOM 1337 C C . LYS A 1 169 ? 16.259 37.336 84.489 1.00 21.92 ? 169 LYS A C 1 ATOM 1338 O O . LYS A 1 169 ? 15.093 37.652 84.290 1.00 22.68 ? 169 LYS A O 1 ATOM 1339 C CB . LYS A 1 169 ? 17.857 39.066 83.775 1.00 20.44 ? 169 LYS A CB 1 ATOM 1340 C CG . LYS A 1 169 ? 18.604 39.705 82.647 1.00 16.21 ? 169 LYS A CG 1 ATOM 1341 C CD . LYS A 1 169 ? 18.774 41.182 82.901 1.00 20.36 ? 169 LYS A CD 1 ATOM 1342 C CE . LYS A 1 169 ? 20.143 41.669 82.452 1.00 22.40 ? 169 LYS A CE 1 ATOM 1343 N NZ . LYS A 1 169 ? 20.125 43.089 82.006 1.00 20.89 ? 169 LYS A NZ 1 ATOM 1344 N N . LEU A 1 170 ? 16.665 36.720 85.588 1.00 22.98 ? 170 LEU A N 1 ATOM 1345 C CA . LEU A 1 170 ? 15.744 36.348 86.651 1.00 26.01 ? 170 LEU A CA 1 ATOM 1346 C C . LEU A 1 170 ? 16.434 36.407 88.003 1.00 27.50 ? 170 LEU A C 1 ATOM 1347 O O . LEU A 1 170 ? 17.579 35.994 88.139 1.00 30.33 ? 170 LEU A O 1 ATOM 1348 C CB . LEU A 1 170 ? 15.210 34.932 86.448 1.00 24.90 ? 170 LEU A CB 1 ATOM 1349 C CG . LEU A 1 170 ? 14.325 34.554 87.638 1.00 26.20 ? 170 LEU A CG 1 ATOM 1350 C CD1 . LEU A 1 170 ? 12.946 35.163 87.420 1.00 26.64 ? 170 LEU A CD1 1 ATOM 1351 C CD2 . LEU A 1 170 ? 14.219 33.050 87.808 1.00 25.31 ? 170 LEU A CD2 1 ATOM 1352 N N . ASP A 1 171 ? 15.730 36.910 89.005 1.00 28.72 ? 171 ASP A N 1 ATOM 1353 C CA . ASP A 1 171 ? 16.289 37.006 90.338 1.00 30.12 ? 171 ASP A CA 1 ATOM 1354 C C . ASP A 1 171 ? 15.583 36.046 91.273 1.00 32.06 ? 171 ASP A C 1 ATOM 1355 O O . ASP A 1 171 ? 14.444 35.664 91.030 1.00 32.23 ? 171 ASP A O 1 ATOM 1356 C CB . ASP A 1 171 ? 16.142 38.428 90.869 1.00 31.33 ? 171 ASP A CB 1 ATOM 1357 C CG . ASP A 1 171 ? 17.039 39.406 90.157 1.00 32.17 ? 171 ASP A CG 1 ATOM 1358 O OD1 . ASP A 1 171 ? 17.728 38.977 89.208 1.00 31.63 ? 171 ASP A OD1 1 ATOM 1359 O OD2 . ASP A 1 171 ? 17.054 40.593 90.548 1.00 30.68 ? 171 ASP A OD2 1 ATOM 1360 N N . PHE A 1 172 ? 16.282 35.644 92.331 1.00 34.90 ? 172 PHE A N 1 ATOM 1361 C CA . PHE A 1 172 ? 15.726 34.746 93.343 1.00 38.91 ? 172 PHE A CA 1 ATOM 1362 C C . PHE A 1 172 ? 16.438 34.966 94.669 1.00 41.30 ? 172 PHE A C 1 ATOM 1363 O O . PHE A 1 172 ? 17.558 35.464 94.697 1.00 40.75 ? 172 PHE A O 1 ATOM 1364 C CB . PHE A 1 172 ? 15.826 33.266 92.921 1.00 35.68 ? 172 PHE A CB 1 ATOM 1365 C CG . PHE A 1 172 ? 17.225 32.776 92.726 1.00 34.71 ? 172 PHE A CG 1 ATOM 1366 C CD1 . PHE A 1 172 ? 17.987 33.218 91.655 1.00 32.24 ? 172 PHE A CD1 1 ATOM 1367 C CD2 . PHE A 1 172 ? 17.791 31.875 93.621 1.00 35.97 ? 172 PHE A CD2 1 ATOM 1368 C CE1 . PHE A 1 172 ? 19.291 32.775 91.476 1.00 33.44 ? 172 PHE A CE1 1 ATOM 1369 C CE2 . PHE A 1 172 ? 19.102 31.425 93.451 1.00 34.91 ? 172 PHE A CE2 1 ATOM 1370 C CZ . PHE A 1 172 ? 19.851 31.878 92.375 1.00 33.61 ? 172 PHE A CZ 1 ATOM 1371 N N . ASN A 1 173 ? 15.769 34.612 95.762 1.00 46.19 ? 173 ASN A N 1 ATOM 1372 C CA . ASN A 1 173 ? 16.331 34.775 97.095 1.00 49.81 ? 173 ASN A CA 1 ATOM 1373 C C . ASN A 1 173 ? 17.199 33.564 97.407 1.00 50.12 ? 173 ASN A C 1 ATOM 1374 O O . ASN A 1 173 ? 16.728 32.422 97.339 1.00 52.08 ? 173 ASN A O 1 ATOM 1375 C CB . ASN A 1 173 ? 15.202 34.907 98.121 1.00 53.59 ? 173 ASN A CB 1 ATOM 1376 C CG . ASN A 1 173 ? 15.700 35.359 99.472 1.00 58.29 ? 173 ASN A CG 1 ATOM 1377 O OD1 . ASN A 1 173 ? 16.413 34.622 100.145 1.00 58.57 ? 173 ASN A OD1 1 ATOM 1378 N ND2 . ASN A 1 173 ? 15.343 36.584 99.855 1.00 63.81 ? 173 ASN A ND2 1 ATOM 1379 N N . MET A 1 174 ? 18.465 33.813 97.739 1.00 49.33 ? 174 MET A N 1 ATOM 1380 C CA . MET A 1 174 ? 19.418 32.742 98.034 1.00 48.05 ? 174 MET A CA 1 ATOM 1381 C C . MET A 1 174 ? 19.152 31.966 99.317 1.00 48.84 ? 174 MET A C 1 ATOM 1382 O O . MET A 1 174 ? 19.733 30.899 99.523 1.00 49.56 ? 174 MET A O 1 ATOM 1383 C CB . MET A 1 174 ? 20.837 33.301 98.106 1.00 45.38 ? 174 MET A CB 1 ATOM 1384 C CG . MET A 1 174 ? 21.379 33.835 96.811 1.00 43.17 ? 174 MET A CG 1 ATOM 1385 S SD . MET A 1 174 ? 23.015 34.538 97.028 1.00 38.27 ? 174 MET A SD 1 ATOM 1386 C CE . MET A 1 174 ? 22.646 36.261 97.100 1.00 40.51 ? 174 MET A CE 1 ATOM 1387 N N . THR A 1 175 ? 18.287 32.492 100.181 1.00 49.47 ? 175 THR A N 1 ATOM 1388 C CA . THR A 1 175 ? 17.998 31.830 101.451 1.00 48.69 ? 175 THR A CA 1 ATOM 1389 C C . THR A 1 175 ? 17.440 30.427 101.305 1.00 49.37 ? 175 THR A C 1 ATOM 1390 O O . THR A 1 175 ? 17.762 29.556 102.111 1.00 50.85 ? 175 THR A O 1 ATOM 1391 C CB . THR A 1 175 ? 17.014 32.632 102.316 1.00 47.20 ? 175 THR A CB 1 ATOM 1392 O OG1 . THR A 1 175 ? 15.752 32.718 101.643 1.00 48.44 ? 175 THR A OG1 1 ATOM 1393 C CG2 . THR A 1 175 ? 17.565 34.021 102.602 1.00 41.96 ? 175 THR A CG2 1 ATOM 1394 N N . THR A 1 176 ? 16.608 30.196 100.295 1.00 50.28 ? 176 THR A N 1 ATOM 1395 C CA . THR A 1 176 ? 16.040 28.859 100.103 1.00 53.55 ? 176 THR A CA 1 ATOM 1396 C C . THR A 1 176 ? 16.700 28.073 98.967 1.00 53.69 ? 176 THR A C 1 ATOM 1397 O O . THR A 1 176 ? 17.473 28.625 98.176 1.00 54.23 ? 176 THR A O 1 ATOM 1398 C CB . THR A 1 176 ? 14.531 28.924 99.810 1.00 53.47 ? 176 THR A CB 1 ATOM 1399 O OG1 . THR A 1 176 ? 14.323 29.615 98.575 1.00 57.29 ? 176 THR A OG1 1 ATOM 1400 C CG2 . THR A 1 176 ? 13.799 29.657 100.923 1.00 53.85 ? 176 THR A CG2 1 ATOM 1401 N N . ASN A 1 177 ? 16.401 26.776 98.909 1.00 53.23 ? 177 ASN A N 1 ATOM 1402 C CA . ASN A 1 177 ? 16.924 25.907 97.854 1.00 52.81 ? 177 ASN A CA 1 ATOM 1403 C C . ASN A 1 177 ? 16.088 26.193 96.602 1.00 50.70 ? 177 ASN A C 1 ATOM 1404 O O . ASN A 1 177 ? 14.893 26.479 96.707 1.00 50.90 ? 177 ASN A O 1 ATOM 1405 C CB . ASN A 1 177 ? 16.771 24.427 98.244 1.00 54.01 ? 177 ASN A CB 1 ATOM 1406 C CG . ASN A 1 177 ? 17.842 23.950 99.218 1.00 54.51 ? 177 ASN A CG 1 ATOM 1407 O OD1 . ASN A 1 177 ? 19.033 23.941 98.900 1.00 55.38 ? 177 ASN A OD1 1 ATOM 1408 N ND2 . ASN A 1 177 ? 17.417 23.537 100.406 1.00 55.62 ? 177 ASN A ND2 1 ATOM 1409 N N . HIS A 1 178 ? 16.703 26.130 95.424 1.00 47.47 ? 178 HIS A N 1 ATOM 1410 C CA . HIS A 1 178 ? 15.967 26.388 94.192 1.00 44.63 ? 178 HIS A CA 1 ATOM 1411 C C . HIS A 1 178 ? 16.390 25.471 93.058 1.00 43.53 ? 178 HIS A C 1 ATOM 1412 O O . HIS A 1 178 ? 17.511 24.971 93.032 1.00 42.88 ? 178 HIS A O 1 ATOM 1413 C CB . HIS A 1 178 ? 16.155 27.837 93.739 1.00 44.22 ? 178 HIS A CB 1 ATOM 1414 C CG . HIS A 1 178 ? 15.476 28.844 94.613 1.00 45.29 ? 178 HIS A CG 1 ATOM 1415 N ND1 . HIS A 1 178 ? 14.108 28.900 94.762 1.00 44.23 ? 178 HIS A ND1 1 ATOM 1416 C CD2 . HIS A 1 178 ? 15.980 29.838 95.385 1.00 46.36 ? 178 HIS A CD2 1 ATOM 1417 C CE1 . HIS A 1 178 ? 13.798 29.885 95.588 1.00 45.56 ? 178 HIS A CE1 1 ATOM 1418 N NE2 . HIS A 1 178 ? 14.917 30.469 95.981 1.00 44.70 ? 178 HIS A NE2 1 ATOM 1419 N N . SER A 1 179 ? 15.477 25.274 92.114 1.00 44.26 ? 179 SER A N 1 ATOM 1420 C CA . SER A 1 179 ? 15.718 24.444 90.940 1.00 43.60 ? 179 SER A CA 1 ATOM 1421 C C . SER A 1 179 ? 14.903 24.968 89.736 1.00 43.71 ? 179 SER A C 1 ATOM 1422 O O . SER A 1 179 ? 13.778 24.512 89.491 1.00 45.05 ? 179 SER A O 1 ATOM 1423 C CB . SER A 1 179 ? 15.328 23.000 91.248 1.00 42.29 ? 179 SER A CB 1 ATOM 1424 O OG . SER A 1 179 ? 15.683 22.154 90.174 1.00 43.38 ? 179 SER A OG 1 ATOM 1425 N N . PHE A 1 180 ? 15.465 25.924 88.990 1.00 40.73 ? 180 PHE A N 1 ATOM 1426 C CA . PHE A 1 180 ? 14.765 26.492 87.834 1.00 37.70 ? 180 PHE A CA 1 ATOM 1427 C C . PHE A 1 180 ? 15.124 25.877 86.494 1.00 36.57 ? 180 PHE A C 1 ATOM 1428 O O . PHE A 1 180 ? 16.237 25.405 86.278 1.00 34.50 ? 180 PHE A O 1 ATOM 1429 C CB . PHE A 1 180 ? 15.035 27.991 87.675 1.00 37.27 ? 180 PHE A CB 1 ATOM 1430 C CG . PHE A 1 180 ? 15.071 28.747 88.950 1.00 37.16 ? 180 PHE A CG 1 ATOM 1431 C CD1 . PHE A 1 180 ? 16.248 28.856 89.665 1.00 36.99 ? 180 PHE A CD1 1 ATOM 1432 C CD2 . PHE A 1 180 ? 13.926 29.364 89.435 1.00 37.51 ? 180 PHE A CD2 1 ATOM 1433 C CE1 . PHE A 1 180 ? 16.288 29.565 90.847 1.00 37.35 ? 180 PHE A CE1 1 ATOM 1434 C CE2 . PHE A 1 180 ? 13.952 30.073 90.613 1.00 35.48 ? 180 PHE A CE2 1 ATOM 1435 C CZ . PHE A 1 180 ? 15.138 30.176 91.323 1.00 37.14 ? 180 PHE A CZ 1 ATOM 1436 N N . MET A 1 181 ? 14.163 25.928 85.580 1.00 36.82 ? 181 MET A N 1 ATOM 1437 C CA . MET A 1 181 ? 14.369 25.454 84.220 1.00 36.85 ? 181 MET A CA 1 ATOM 1438 C C . MET A 1 181 ? 14.101 26.638 83.289 1.00 36.09 ? 181 MET A C 1 ATOM 1439 O O . MET A 1 181 ? 13.135 27.387 83.481 1.00 35.21 ? 181 MET A O 1 ATOM 1440 C CB . MET A 1 181 ? 13.404 24.314 83.856 1.00 36.78 ? 181 MET A CB 1 ATOM 1441 C CG . MET A 1 181 ? 13.590 23.845 82.408 1.00 35.38 ? 181 MET A CG 1 ATOM 1442 S SD . MET A 1 181 ? 12.450 22.606 81.824 1.00 32.49 ? 181 MET A SD 1 ATOM 1443 C CE . MET A 1 181 ? 12.843 21.207 82.910 1.00 27.11 ? 181 MET A CE 1 ATOM 1444 N N . CYS A 1 182 ? 14.967 26.827 82.304 1.00 33.13 ? 182 CYS A N 1 ATOM 1445 C CA . CYS A 1 182 ? 14.754 27.896 81.350 1.00 30.76 ? 182 CYS A CA 1 ATOM 1446 C C . CYS A 1 182 ? 14.226 27.164 80.151 1.00 30.41 ? 182 CYS A C 1 ATOM 1447 O O . CYS A 1 182 ? 14.944 26.381 79.544 1.00 32.38 ? 182 CYS A O 1 ATOM 1448 C CB . CYS A 1 182 ? 16.057 28.588 80.985 1.00 29.59 ? 182 CYS A CB 1 ATOM 1449 S SG . CYS A 1 182 ? 15.869 29.901 79.737 1.00 30.19 ? 182 CYS A SG 1 ATOM 1450 N N . LEU A 1 183 ? 12.963 27.386 79.826 1.00 28.08 ? 183 LEU A N 1 ATOM 1451 C CA . LEU A 1 183 ? 12.378 26.711 78.688 1.00 26.62 ? 183 LEU A CA 1 ATOM 1452 C C . LEU A 1 183 ? 12.298 27.710 77.570 1.00 26.48 ? 183 LEU A C 1 ATOM 1453 O O . LEU A 1 183 ? 11.911 28.849 77.793 1.00 28.70 ? 183 LEU A O 1 ATOM 1454 C CB . LEU A 1 183 ? 10.982 26.198 79.041 1.00 27.14 ? 183 LEU A CB 1 ATOM 1455 C CG . LEU A 1 183 ? 10.298 25.258 78.046 1.00 25.94 ? 183 LEU A CG 1 ATOM 1456 C CD1 . LEU A 1 183 ? 11.248 24.127 77.648 1.00 25.19 ? 183 LEU A CD1 1 ATOM 1457 C CD2 . LEU A 1 183 ? 9.028 24.711 78.686 1.00 24.60 ? 183 LEU A CD2 1 ATOM 1458 N N . ILE A 1 184 ? 12.683 27.294 76.369 1.00 27.06 ? 184 ILE A N 1 ATOM 1459 C CA . ILE A 1 184 ? 12.640 28.174 75.201 1.00 25.79 ? 184 ILE A CA 1 ATOM 1460 C C . ILE A 1 184 ? 11.882 27.509 74.054 1.00 24.82 ? 184 ILE A C 1 ATOM 1461 O O . ILE A 1 184 ? 12.359 26.561 73.436 1.00 26.15 ? 184 ILE A O 1 ATOM 1462 C CB . ILE A 1 184 ? 14.072 28.556 74.728 1.00 24.19 ? 184 ILE A CB 1 ATOM 1463 C CG1 . ILE A 1 184 ? 14.888 29.062 75.916 1.00 26.79 ? 184 ILE A CG1 1 ATOM 1464 C CG2 . ILE A 1 184 ? 14.000 29.660 73.704 1.00 18.05 ? 184 ILE A CG2 1 ATOM 1465 C CD1 . ILE A 1 184 ? 16.314 29.404 75.605 1.00 29.51 ? 184 ILE A CD1 1 ATOM 1466 N N . LYS A 1 185 ? 10.684 28.010 73.791 1.00 23.83 ? 185 LYS A N 1 ATOM 1467 C CA . LYS A 1 185 ? 9.842 27.487 72.730 1.00 24.01 ? 185 LYS A CA 1 ATOM 1468 C C . LYS A 1 185 ? 10.007 28.326 71.479 1.00 26.08 ? 185 LYS A C 1 ATOM 1469 O O . LYS A 1 185 ? 10.011 29.550 71.531 1.00 27.14 ? 185 LYS A O 1 ATOM 1470 C CB . LYS A 1 185 ? 8.374 27.530 73.143 1.00 22.89 ? 185 LYS A CB 1 ATOM 1471 C CG . LYS A 1 185 ? 7.983 26.542 74.208 1.00 26.44 ? 185 LYS A CG 1 ATOM 1472 C CD . LYS A 1 185 ? 6.655 26.929 74.842 1.00 30.97 ? 185 LYS A CD 1 ATOM 1473 C CE . LYS A 1 185 ? 6.310 26.028 76.034 1.00 33.76 ? 185 LYS A CE 1 ATOM 1474 N NZ . LYS A 1 185 ? 5.210 26.585 76.872 1.00 35.68 ? 185 LYS A NZ 1 ATOM 1475 N N . TYR A 1 186 ? 10.155 27.655 70.351 1.00 27.00 ? 186 TYR A N 1 ATOM 1476 C CA . TYR A 1 186 ? 10.274 28.328 69.072 1.00 27.35 ? 186 TYR A CA 1 ATOM 1477 C C . TYR A 1 186 ? 9.570 27.352 68.138 1.00 29.30 ? 186 TYR A C 1 ATOM 1478 O O . TYR A 1 186 ? 10.012 26.216 67.953 1.00 28.42 ? 186 TYR A O 1 ATOM 1479 C CB . TYR A 1 186 ? 11.747 28.561 68.706 1.00 24.55 ? 186 TYR A CB 1 ATOM 1480 C CG . TYR A 1 186 ? 12.578 27.319 68.536 1.00 21.61 ? 186 TYR A CG 1 ATOM 1481 C CD1 . TYR A 1 186 ? 12.742 26.748 67.285 1.00 19.82 ? 186 TYR A CD1 1 ATOM 1482 C CD2 . TYR A 1 186 ? 13.212 26.722 69.621 1.00 18.53 ? 186 TYR A CD2 1 ATOM 1483 C CE1 . TYR A 1 186 ? 13.518 25.614 67.110 1.00 20.89 ? 186 TYR A CE1 1 ATOM 1484 C CE2 . TYR A 1 186 ? 13.996 25.587 69.454 1.00 18.00 ? 186 TYR A CE2 1 ATOM 1485 C CZ . TYR A 1 186 ? 14.145 25.037 68.192 1.00 17.32 ? 186 TYR A CZ 1 ATOM 1486 O OH . TYR A 1 186 ? 14.919 23.920 67.979 1.00 13.18 ? 186 TYR A OH 1 ATOM 1487 N N . GLY A 1 187 ? 8.448 27.798 67.585 1.00 31.21 ? 187 GLY A N 1 ATOM 1488 C CA . GLY A 1 187 ? 7.659 26.934 66.733 1.00 33.09 ? 187 GLY A CA 1 ATOM 1489 C C . GLY A 1 187 ? 7.074 25.880 67.664 1.00 35.15 ? 187 GLY A C 1 ATOM 1490 O O . GLY A 1 187 ? 6.725 26.183 68.815 1.00 33.46 ? 187 GLY A O 1 ATOM 1491 N N . HIS A 1 188 ? 6.993 24.638 67.195 1.00 35.04 ? 188 HIS A N 1 ATOM 1492 C CA . HIS A 1 188 ? 6.463 23.571 68.017 1.00 35.31 ? 188 HIS A CA 1 ATOM 1493 C C . HIS A 1 188 ? 7.548 22.736 68.672 1.00 34.59 ? 188 HIS A C 1 ATOM 1494 O O . HIS A 1 188 ? 7.300 21.643 69.160 1.00 36.84 ? 188 HIS A O 1 ATOM 1495 C CB . HIS A 1 188 ? 5.516 22.716 67.185 1.00 40.23 ? 188 HIS A CB 1 ATOM 1496 C CG . HIS A 1 188 ? 4.325 23.478 66.686 1.00 46.22 ? 188 HIS A CG 1 ATOM 1497 N ND1 . HIS A 1 188 ? 3.415 24.069 67.539 1.00 46.38 ? 188 HIS A ND1 1 ATOM 1498 C CD2 . HIS A 1 188 ? 3.938 23.813 65.432 1.00 46.38 ? 188 HIS A CD2 1 ATOM 1499 C CE1 . HIS A 1 188 ? 2.524 24.739 66.830 1.00 48.56 ? 188 HIS A CE1 1 ATOM 1500 N NE2 . HIS A 1 188 ? 2.818 24.601 65.550 1.00 48.20 ? 188 HIS A NE2 1 ATOM 1501 N N . LEU A 1 189 ? 8.762 23.268 68.691 1.00 35.34 ? 189 LEU A N 1 ATOM 1502 C CA . LEU A 1 189 ? 9.893 22.594 69.326 1.00 33.98 ? 189 LEU A CA 1 ATOM 1503 C C . LEU A 1 189 ? 10.144 23.240 70.694 1.00 35.21 ? 189 LEU A C 1 ATOM 1504 O O . LEU A 1 189 ? 9.310 24.003 71.201 1.00 39.01 ? 189 LEU A O 1 ATOM 1505 C CB . LEU A 1 189 ? 11.140 22.730 68.449 1.00 30.14 ? 189 LEU A CB 1 ATOM 1506 C CG . LEU A 1 189 ? 11.094 22.086 67.057 1.00 26.53 ? 189 LEU A CG 1 ATOM 1507 C CD1 . LEU A 1 189 ? 12.422 22.279 66.367 1.00 23.16 ? 189 LEU A CD1 1 ATOM 1508 C CD2 . LEU A 1 189 ? 10.776 20.593 67.169 1.00 23.87 ? 189 LEU A CD2 1 ATOM 1509 N N . ARG A 1 190 ? 11.277 22.930 71.306 1.00 32.34 ? 190 ARG A N 1 ATOM 1510 C CA . ARG A 1 190 ? 11.602 23.528 72.594 1.00 32.37 ? 190 ARG A CA 1 ATOM 1511 C C . ARG A 1 190 ? 12.937 23.022 73.105 1.00 31.15 ? 190 ARG A C 1 ATOM 1512 O O . ARG A 1 190 ? 13.244 21.836 72.997 1.00 28.80 ? 190 ARG A O 1 ATOM 1513 C CB . ARG A 1 190 ? 10.497 23.263 73.631 1.00 34.02 ? 190 ARG A CB 1 ATOM 1514 C CG . ARG A 1 190 ? 10.051 21.812 73.740 1.00 36.86 ? 190 ARG A CG 1 ATOM 1515 C CD . ARG A 1 190 ? 9.612 21.457 75.157 1.00 37.78 ? 190 ARG A CD 1 ATOM 1516 N NE . ARG A 1 190 ? 8.473 22.251 75.618 1.00 37.98 ? 190 ARG A NE 1 ATOM 1517 C CZ . ARG A 1 190 ? 7.880 22.087 76.798 1.00 37.40 ? 190 ARG A CZ 1 ATOM 1518 N NH1 . ARG A 1 190 ? 8.320 21.160 77.643 1.00 34.36 ? 190 ARG A NH1 1 ATOM 1519 N NH2 . ARG A 1 190 ? 6.838 22.838 77.127 1.00 38.18 ? 190 ARG A NH2 1 ATOM 1520 N N . VAL A 1 191 ? 13.735 23.946 73.636 1.00 31.21 ? 191 VAL A N 1 ATOM 1521 C CA . VAL A 1 191 ? 15.051 23.620 74.175 1.00 32.49 ? 191 VAL A CA 1 ATOM 1522 C C . VAL A 1 191 ? 15.123 24.190 75.592 1.00 33.50 ? 191 VAL A C 1 ATOM 1523 O O . VAL A 1 191 ? 14.363 25.100 75.934 1.00 35.29 ? 191 VAL A O 1 ATOM 1524 C CB . VAL A 1 191 ? 16.192 24.220 73.298 1.00 29.62 ? 191 VAL A CB 1 ATOM 1525 C CG1 . VAL A 1 191 ? 16.546 25.629 73.762 1.00 30.89 ? 191 VAL A CG1 1 ATOM 1526 C CG2 . VAL A 1 191 ? 17.401 23.333 73.362 1.00 28.17 ? 191 VAL A CG2 1 ATOM 1527 N N . ASN A 1 192 ? 16.008 23.656 76.426 1.00 32.73 ? 192 ASN A N 1 ATOM 1528 C CA . ASN A 1 192 ? 16.110 24.173 77.779 1.00 33.28 ? 192 ASN A CA 1 ATOM 1529 C C . ASN A 1 192 ? 17.381 23.814 78.525 1.00 32.47 ? 192 ASN A C 1 ATOM 1530 O O . ASN A 1 192 ? 18.238 23.092 78.045 1.00 30.79 ? 192 ASN A O 1 ATOM 1531 C CB . ASN A 1 192 ? 14.898 23.730 78.607 1.00 36.04 ? 192 ASN A CB 1 ATOM 1532 C CG . ASN A 1 192 ? 15.083 22.361 79.258 1.00 38.39 ? 192 ASN A CG 1 ATOM 1533 O OD1 . ASN A 1 192 ? 15.894 22.189 80.163 1.00 39.26 ? 192 ASN A OD1 1 ATOM 1534 N ND2 . ASN A 1 192 ? 14.308 21.390 78.799 1.00 38.82 ? 192 ASN A ND2 1 ATOM 1535 N N . GLN A 1 193 ? 17.489 24.356 79.721 1.00 34.23 ? 193 GLN A N 1 ATOM 1536 C CA . GLN A 1 193 ? 18.624 24.096 80.578 1.00 36.45 ? 193 GLN A CA 1 ATOM 1537 C C . GLN A 1 193 ? 18.086 24.348 81.969 1.00 36.62 ? 193 GLN A C 1 ATOM 1538 O O . GLN A 1 193 ? 17.027 24.965 82.124 1.00 36.82 ? 193 GLN A O 1 ATOM 1539 C CB . GLN A 1 193 ? 19.785 25.046 80.260 1.00 36.71 ? 193 GLN A CB 1 ATOM 1540 C CG . GLN A 1 193 ? 21.008 24.832 81.138 1.00 35.57 ? 193 GLN A CG 1 ATOM 1541 C CD . GLN A 1 193 ? 21.520 23.392 81.112 1.00 36.93 ? 193 GLN A CD 1 ATOM 1542 O OE1 . GLN A 1 193 ? 22.087 22.926 80.117 1.00 32.55 ? 193 GLN A OE1 1 ATOM 1543 N NE2 . GLN A 1 193 ? 21.315 22.679 82.215 1.00 38.03 ? 193 GLN A NE2 1 ATOM 1544 N N . THR A 1 194 ? 18.792 23.866 82.979 1.00 36.44 ? 194 THR A N 1 ATOM 1545 C CA . THR A 1 194 ? 18.325 24.062 84.336 1.00 38.60 ? 194 THR A CA 1 ATOM 1546 C C . THR A 1 194 ? 19.370 24.715 85.224 1.00 39.28 ? 194 THR A C 1 ATOM 1547 O O . THR A 1 194 ? 20.533 24.873 84.839 1.00 39.92 ? 194 THR A O 1 ATOM 1548 C CB . THR A 1 194 ? 17.888 22.726 84.970 1.00 37.60 ? 194 THR A CB 1 ATOM 1549 O OG1 . THR A 1 194 ? 18.967 21.789 84.896 1.00 38.37 ? 194 THR A OG1 1 ATOM 1550 C CG2 . THR A 1 194 ? 16.677 22.161 84.243 1.00 36.65 ? 194 THR A CG2 1 ATOM 1551 N N . PHE A 1 195 ? 18.932 25.113 86.413 1.00 38.91 ? 195 PHE A N 1 ATOM 1552 C CA . PHE A 1 195 ? 19.815 25.731 87.379 1.00 40.26 ? 195 PHE A CA 1 ATOM 1553 C C . PHE A 1 195 ? 19.437 25.271 88.772 1.00 42.03 ? 195 PHE A C 1 ATOM 1554 O O . PHE A 1 195 ? 18.302 25.457 89.210 1.00 44.24 ? 195 PHE A O 1 ATOM 1555 C CB . PHE A 1 195 ? 19.721 27.254 87.322 1.00 38.22 ? 195 PHE A CB 1 ATOM 1556 C CG . PHE A 1 195 ? 20.744 27.939 88.172 1.00 35.05 ? 195 PHE A CG 1 ATOM 1557 C CD1 . PHE A 1 195 ? 22.033 28.125 87.704 1.00 33.23 ? 195 PHE A CD1 1 ATOM 1558 C CD2 . PHE A 1 195 ? 20.442 28.332 89.467 1.00 34.27 ? 195 PHE A CD2 1 ATOM 1559 C CE1 . PHE A 1 195 ? 23.006 28.684 88.512 1.00 32.97 ? 195 PHE A CE1 1 ATOM 1560 C CE2 . PHE A 1 195 ? 21.408 28.889 90.279 1.00 33.67 ? 195 PHE A CE2 1 ATOM 1561 C CZ . PHE A 1 195 ? 22.692 29.065 89.799 1.00 34.67 ? 195 PHE A CZ 1 ATOM 1562 N N . ASN A 1 196 ? 20.391 24.675 89.471 1.00 43.59 ? 196 ASN A N 1 ATOM 1563 C CA . ASN A 1 196 ? 20.138 24.198 90.818 1.00 45.61 ? 196 ASN A CA 1 ATOM 1564 C C . ASN A 1 196 ? 20.778 25.104 91.836 1.00 45.22 ? 196 ASN A C 1 ATOM 1565 O O . ASN A 1 196 ? 21.962 25.421 91.734 1.00 45.55 ? 196 ASN A O 1 ATOM 1566 C CB . ASN A 1 196 ? 20.683 22.785 90.979 1.00 47.86 ? 196 ASN A CB 1 ATOM 1567 C CG . ASN A 1 196 ? 19.946 21.794 90.123 1.00 50.25 ? 196 ASN A CG 1 ATOM 1568 O OD1 . ASN A 1 196 ? 18.752 21.563 90.324 1.00 49.27 ? 196 ASN A OD1 1 ATOM 1569 N ND2 . ASN A 1 196 ? 20.642 21.209 89.150 1.00 50.29 ? 196 ASN A ND2 1 ATOM 1570 N N . TRP A 1 197 ? 19.989 25.544 92.807 1.00 44.83 ? 197 TRP A N 1 ATOM 1571 C CA . TRP A 1 197 ? 20.524 26.391 93.850 1.00 46.33 ? 197 TRP A CA 1 ATOM 1572 C C . TRP A 1 197 ? 20.364 25.705 95.189 1.00 49.64 ? 197 TRP A C 1 ATOM 1573 O O . TRP A 1 197 ? 19.248 25.483 95.662 1.00 49.09 ? 197 TRP A O 1 ATOM 1574 C CB . TRP A 1 197 ? 19.838 27.750 93.896 1.00 42.14 ? 197 TRP A CB 1 ATOM 1575 C CG . TRP A 1 197 ? 20.317 28.538 95.063 1.00 39.49 ? 197 TRP A CG 1 ATOM 1576 C CD1 . TRP A 1 197 ? 19.700 28.688 96.271 1.00 39.02 ? 197 TRP A CD1 1 ATOM 1577 C CD2 . TRP A 1 197 ? 21.564 29.241 95.159 1.00 37.78 ? 197 TRP A CD2 1 ATOM 1578 N NE1 . TRP A 1 197 ? 20.488 29.440 97.115 1.00 39.49 ? 197 TRP A NE1 1 ATOM 1579 C CE2 . TRP A 1 197 ? 21.637 29.791 96.455 1.00 38.01 ? 197 TRP A CE2 1 ATOM 1580 C CE3 . TRP A 1 197 ? 22.629 29.456 94.271 1.00 36.41 ? 197 TRP A CE3 1 ATOM 1581 C CZ2 . TRP A 1 197 ? 22.733 30.544 96.885 1.00 36.83 ? 197 TRP A CZ2 1 ATOM 1582 C CZ3 . TRP A 1 197 ? 23.726 30.209 94.706 1.00 33.06 ? 197 TRP A CZ3 1 ATOM 1583 C CH2 . TRP A 1 197 ? 23.766 30.739 95.998 1.00 32.54 ? 197 TRP A CH2 1 ATOM 1584 N N . ASN A 1 198 ? 21.499 25.360 95.784 1.00 53.80 ? 198 ASN A N 1 ATOM 1585 C CA . ASN A 1 198 ? 21.523 24.702 97.077 1.00 56.84 ? 198 ASN A CA 1 ATOM 1586 C C . ASN A 1 198 ? 21.963 25.715 98.114 1.00 59.56 ? 198 ASN A C 1 ATOM 1587 O O . ASN A 1 198 ? 23.056 26.280 98.040 1.00 60.88 ? 198 ASN A O 1 ATOM 1588 C CB . ASN A 1 198 ? 22.469 23.504 97.044 1.00 56.66 ? 198 ASN A CB 1 ATOM 1589 C CG . ASN A 1 198 ? 21.989 22.421 96.094 1.00 56.80 ? 198 ASN A CG 1 ATOM 1590 O OD1 . ASN A 1 198 ? 20.852 21.954 96.200 1.00 56.94 ? 198 ASN A OD1 1 ATOM 1591 N ND2 . ASN A 1 198 ? 22.849 22.012 95.162 1.00 55.70 ? 198 ASN A ND2 1 ATOM 1592 N N . THR A 1 199 ? 21.069 25.947 99.063 1.00 62.66 ? 199 THR A N 1 ATOM 1593 C CA . THR A 1 199 ? 21.278 26.899 100.134 1.00 65.68 ? 199 THR A CA 1 ATOM 1594 C C . THR A 1 199 ? 22.596 26.738 100.883 1.00 66.33 ? 199 THR A C 1 ATOM 1595 O O . THR A 1 199 ? 23.653 27.135 100.389 1.00 65.97 ? 199 THR A O 1 ATOM 1596 C CB . THR A 1 199 ? 20.104 26.824 101.128 1.00 66.17 ? 199 THR A CB 1 ATOM 1597 O OG1 . THR A 1 199 ? 20.358 27.688 102.234 1.00 68.15 ? 199 THR A OG1 1 ATOM 1598 C CG2 . THR A 1 199 ? 19.907 25.394 101.627 1.00 66.30 ? 199 THR A CG2 1 ATOM 1599 N N . ALA A 1 200 ? 22.525 26.166 102.080 1.00 68.41 ? 200 ALA A N 1 ATOM 1600 C CA . ALA A 1 200 ? 23.710 25.973 102.910 1.00 71.35 ? 200 ALA A CA 1 ATOM 1601 C C . ALA A 1 200 ? 24.074 24.495 103.025 1.00 71.83 ? 200 ALA A C 1 ATOM 1602 O O . ALA A 1 200 ? 25.198 24.139 102.618 1.00 71.31 ? 200 ALA A O 1 ATOM 1603 C CB . ALA A 1 200 ? 23.471 26.564 104.310 1.00 71.02 ? 200 ALA A CB 1 HETATM 1604 C C1 . NAG B 2 . ? 17.628 44.528 79.724 1.00 36.78 ? 1001 NAG A C1 1 HETATM 1605 C C2 . NAG B 2 . ? 17.840 46.033 79.976 1.00 37.49 ? 1001 NAG A C2 1 HETATM 1606 C C3 . NAG B 2 . ? 18.778 46.636 78.915 1.00 38.51 ? 1001 NAG A C3 1 HETATM 1607 C C4 . NAG B 2 . ? 20.046 45.809 78.725 1.00 37.18 ? 1001 NAG A C4 1 HETATM 1608 C C5 . NAG B 2 . ? 19.710 44.314 78.561 1.00 35.06 ? 1001 NAG A C5 1 HETATM 1609 C C6 . NAG B 2 . ? 20.950 43.438 78.511 1.00 34.75 ? 1001 NAG A C6 1 HETATM 1610 C C7 . NAG B 2 . ? 16.215 47.549 80.919 1.00 39.94 ? 1001 NAG A C7 1 HETATM 1611 C C8 . NAG B 2 . ? 14.884 48.273 80.781 1.00 38.44 ? 1001 NAG A C8 1 HETATM 1612 N N2 . NAG B 2 . ? 16.573 46.740 79.923 1.00 38.07 ? 1001 NAG A N2 1 HETATM 1613 O O3 . NAG B 2 . ? 19.146 47.956 79.290 1.00 41.83 ? 1001 NAG A O3 1 HETATM 1614 O O4 . NAG B 2 . ? 20.733 46.282 77.573 1.00 35.61 ? 1001 NAG A O4 1 HETATM 1615 O O5 . NAG B 2 . ? 18.894 43.854 79.665 1.00 33.85 ? 1001 NAG A O5 1 HETATM 1616 O O6 . NAG B 2 . ? 21.510 43.243 79.803 1.00 32.88 ? 1001 NAG A O6 1 HETATM 1617 O O7 . NAG B 2 . ? 16.901 47.714 81.932 1.00 41.12 ? 1001 NAG A O7 1 HETATM 1618 C C1 . NAG C 2 . ? 14.642 20.007 79.054 1.00 39.44 ? 1002 NAG A C1 1 HETATM 1619 C C2 . NAG C 2 . ? 13.426 19.123 78.682 1.00 40.70 ? 1002 NAG A C2 1 HETATM 1620 C C3 . NAG C 2 . ? 13.771 17.633 78.667 1.00 39.35 ? 1002 NAG A C3 1 HETATM 1621 C C4 . NAG C 2 . ? 15.046 17.362 77.887 1.00 38.74 ? 1002 NAG A C4 1 HETATM 1622 C C5 . NAG C 2 . ? 16.160 18.255 78.430 1.00 40.04 ? 1002 NAG A C5 1 HETATM 1623 C C6 . NAG C 2 . ? 17.494 18.051 77.737 1.00 39.55 ? 1002 NAG A C6 1 HETATM 1624 C C7 . NAG C 2 . ? 11.223 19.951 79.189 1.00 41.32 ? 1002 NAG A C7 1 HETATM 1625 C C8 . NAG C 2 . ? 10.083 20.112 80.186 1.00 41.63 ? 1002 NAG A C8 1 HETATM 1626 N N2 . NAG C 2 . ? 12.322 19.327 79.603 1.00 40.00 ? 1002 NAG A N2 1 HETATM 1627 O O3 . NAG C 2 . ? 12.706 16.920 78.071 1.00 42.16 ? 1002 NAG A O3 1 HETATM 1628 O O4 . NAG C 2 . ? 15.401 15.997 78.038 1.00 37.88 ? 1002 NAG A O4 1 HETATM 1629 O O5 . NAG C 2 . ? 15.792 19.647 78.272 1.00 38.80 ? 1002 NAG A O5 1 HETATM 1630 O O6 . NAG C 2 . ? 17.324 17.769 76.360 1.00 40.96 ? 1002 NAG A O6 1 HETATM 1631 O O7 . NAG C 2 . ? 11.109 20.412 78.055 1.00 40.92 ? 1002 NAG A O7 1 HETATM 1632 C C1 . NAG D 2 . ? 15.061 36.900 101.249 1.00 66.73 ? 1003 NAG A C1 1 HETATM 1633 C C2 . NAG D 2 . ? 13.795 37.762 101.346 1.00 67.72 ? 1003 NAG A C2 1 HETATM 1634 C C3 . NAG D 2 . ? 13.557 38.143 102.814 1.00 69.05 ? 1003 NAG A C3 1 HETATM 1635 C C4 . NAG D 2 . ? 13.455 36.868 103.656 1.00 70.00 ? 1003 NAG A C4 1 HETATM 1636 C C5 . NAG D 2 . ? 14.714 36.010 103.457 1.00 70.05 ? 1003 NAG A C5 1 HETATM 1637 C C6 . NAG D 2 . ? 14.662 34.681 104.195 1.00 69.37 ? 1003 NAG A C6 1 HETATM 1638 C C7 . NAG D 2 . ? 13.586 38.918 99.234 1.00 59.89 ? 1003 NAG A C7 1 HETATM 1639 C C8 . NAG D 2 . ? 13.765 40.206 98.454 1.00 58.69 ? 1003 NAG A C8 1 HETATM 1640 N N2 . NAG D 2 . ? 13.927 38.949 100.521 1.00 63.95 ? 1003 NAG A N2 1 HETATM 1641 O O3 . NAG D 2 . ? 12.356 38.892 102.931 1.00 70.93 ? 1003 NAG A O3 1 HETATM 1642 O O4 . NAG D 2 . ? 13.304 37.213 105.027 1.00 69.27 ? 1003 NAG A O4 1 HETATM 1643 O O5 . NAG D 2 . ? 14.903 35.715 102.049 1.00 69.94 ? 1003 NAG A O5 1 HETATM 1644 O O6 . NAG D 2 . ? 13.537 33.910 103.798 1.00 70.05 ? 1003 NAG A O6 1 HETATM 1645 O O7 . NAG D 2 . ? 13.145 37.914 98.671 1.00 55.83 ? 1003 NAG A O7 1 # 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 VAL 1 1 1 VAL VAL A . n A 1 2 ILE 2 2 2 ILE ILE A . n A 1 3 HIS 3 3 3 HIS HIS A . n A 1 4 VAL 4 4 4 VAL VAL A . n A 1 5 THR 5 5 5 THR THR A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 GLU 7 7 7 GLU GLU A . n A 1 8 VAL 8 8 8 VAL VAL A . n A 1 9 LYS 9 9 9 LYS LYS A . n A 1 10 GLU 10 10 10 GLU GLU A . n A 1 11 VAL 11 11 11 VAL VAL A . n A 1 12 ALA 12 12 12 ALA ALA A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 SER 15 15 15 SER SER A . n A 1 16 CYS 16 16 16 CYS CYS A . n A 1 17 GLY 17 17 17 GLY GLY A . n A 1 18 HIS 18 18 18 HIS HIS A . n A 1 19 ASN 19 19 19 ASN ASN A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 SER 21 21 21 SER SER A . n A 1 22 VAL 22 22 22 VAL VAL A . n A 1 23 GLU 23 23 23 GLU GLU A . n A 1 24 GLU 24 24 24 GLU GLU A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 ALA 26 26 26 ALA ALA A . n A 1 27 GLN 27 27 27 GLN GLN A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 ARG 29 29 29 ARG ARG A . n A 1 30 ILE 30 30 30 ILE ILE A . n A 1 31 TYR 31 31 31 TYR TYR A . n A 1 32 TRP 32 32 32 TRP TRP A . n A 1 33 GLN 33 33 33 GLN GLN A . n A 1 34 LYS 34 34 34 LYS LYS A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 LYS 36 36 36 LYS LYS A . n A 1 37 LYS 37 37 37 LYS LYS A . n A 1 38 MET 38 38 38 MET MET A . n A 1 39 VAL 39 39 39 VAL VAL A . n A 1 40 LEU 40 40 40 LEU LEU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 MET 42 42 42 MET MET A . n A 1 43 MET 43 43 43 MET MET A . n A 1 44 SER 44 44 44 SER SER A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 MET 47 47 47 MET MET A . n A 1 48 ASN 48 48 48 ASN ASN A . n A 1 49 ILE 49 49 49 ILE ILE A . n A 1 50 TRP 50 50 50 TRP TRP A . n A 1 51 PRO 51 51 51 PRO PRO A . n A 1 52 GLU 52 52 52 GLU GLU A . n A 1 53 TYR 53 53 53 TYR TYR A . n A 1 54 LYS 54 54 54 LYS LYS A . n A 1 55 ASN 55 55 55 ASN ASN A . n A 1 56 ARG 56 56 56 ARG ARG A . n A 1 57 THR 57 57 57 THR THR A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 PHE 59 59 59 PHE PHE A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 ILE 61 61 61 ILE ILE A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 LEU 65 65 65 LEU LEU A . n A 1 66 SER 66 66 66 SER SER A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 VAL 68 68 68 VAL VAL A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 ALA 71 71 71 ALA ALA A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 ARG 73 73 73 ARG ARG A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 SER 75 75 75 SER SER A . n A 1 76 ASP 76 76 76 ASP ASP A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 THR 79 79 79 THR THR A . n A 1 80 TYR 80 80 80 TYR TYR A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 CYS 82 82 82 CYS CYS A . n A 1 83 VAL 83 83 83 VAL VAL A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 LEU 85 85 85 LEU LEU A . n A 1 86 LYS 86 86 86 LYS LYS A . n A 1 87 TYR 87 87 87 TYR TYR A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 LYS 89 89 89 LYS LYS A . n A 1 90 ASP 90 90 90 ASP ASP A . n A 1 91 ALA 91 91 91 ALA ALA A . n A 1 92 PHE 92 92 92 PHE PHE A . n A 1 93 LYS 93 93 93 LYS LYS A . n A 1 94 ARG 94 94 94 ARG ARG A . n A 1 95 GLU 95 95 95 GLU GLU A . n A 1 96 HIS 96 96 96 HIS HIS A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 ALA 98 98 98 ALA ALA A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 VAL 100 100 100 VAL VAL A . n A 1 101 THR 101 101 101 THR THR A . n A 1 102 LEU 102 102 102 LEU LEU A . n A 1 103 SER 103 103 103 SER SER A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 LYS 105 105 105 LYS LYS A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 ASP 107 107 107 ASP ASP A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 PRO 109 109 109 PRO PRO A . n A 1 110 THR 110 110 110 THR THR A . n A 1 111 PRO 111 111 111 PRO PRO A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 ILE 113 113 113 ILE ILE A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 PHE 116 116 116 PHE PHE A . n A 1 117 GLU 117 117 117 GLU GLU A . n A 1 118 ILE 118 118 118 ILE ILE A . n A 1 119 PRO 119 119 119 PRO PRO A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 ASN 122 122 122 ASN ASN A . n A 1 123 ILE 123 123 123 ILE ILE A . n A 1 124 ARG 124 124 124 ARG ARG A . n A 1 125 ARG 125 125 125 ARG ARG A . n A 1 126 ILE 126 126 126 ILE ILE A . n A 1 127 ILE 127 127 127 ILE ILE A . n A 1 128 CYS 128 128 128 CYS CYS A . n A 1 129 SER 129 129 129 SER SER A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 SER 131 131 131 SER SER A . n A 1 132 GLY 132 132 132 GLY GLY A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 PHE 134 134 134 PHE PHE A . n A 1 135 PRO 135 135 135 PRO CPR A . n A 1 136 GLU 136 136 136 GLU GLU A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 HIS 138 138 138 HIS HIS A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 SER 140 140 140 SER SER A . n A 1 141 TRP 141 141 141 TRP TRP A . n A 1 142 LEU 142 142 142 LEU LEU A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 ASN 144 144 144 ASN ASN A . n A 1 145 GLY 145 145 145 GLY GLY A . n A 1 146 GLU 146 146 146 GLU GLU A . n A 1 147 GLU 147 147 147 GLU GLU A . n A 1 148 LEU 148 148 148 LEU LEU A . n A 1 149 ASN 149 149 149 ASN ASN A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 THR 154 154 154 THR THR A . n A 1 155 VAL 155 155 155 VAL VAL A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 GLN 157 157 157 GLN GLN A . n A 1 158 ASP 158 158 158 ASP ASP A . n A 1 159 PRO 159 159 159 PRO PRO A . n A 1 160 GLU 160 160 160 GLU GLU A . n A 1 161 THR 161 161 161 THR THR A . n A 1 162 GLU 162 162 162 GLU GLU A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ALA 165 165 165 ALA ALA A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 SER 167 167 167 SER SER A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 LYS 169 169 169 LYS LYS A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 PHE 172 172 172 PHE PHE A . n A 1 173 ASN 173 173 173 ASN ASN A . n A 1 174 MET 174 174 174 MET MET A . n A 1 175 THR 175 175 175 THR THR A . n A 1 176 THR 176 176 176 THR THR A . n A 1 177 ASN 177 177 177 ASN ASN A . n A 1 178 HIS 178 178 178 HIS HIS A . n A 1 179 SER 179 179 179 SER SER A . n A 1 180 PHE 180 180 180 PHE PHE A . n A 1 181 MET 181 181 181 MET MET A . n A 1 182 CYS 182 182 182 CYS CYS A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 ILE 184 184 184 ILE ILE A . n A 1 185 LYS 185 185 185 LYS LYS A . n A 1 186 TYR 186 186 186 TYR TYR A . n A 1 187 GLY 187 187 187 GLY GLY A . n A 1 188 HIS 188 188 188 HIS HIS A . n A 1 189 LEU 189 189 189 LEU LEU A . n A 1 190 ARG 190 190 190 ARG ARG A . n A 1 191 VAL 191 191 191 VAL VAL A . n A 1 192 ASN 192 192 192 ASN ASN A . n A 1 193 GLN 193 193 193 GLN GLN A . n A 1 194 THR 194 194 194 THR THR A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 ASN 196 196 196 ASN ASN A . n A 1 197 TRP 197 197 197 TRP TRP A . n A 1 198 ASN 198 198 198 ASN ASN A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 ALA 200 200 200 ALA ALA A . n A 1 201 LYS 201 201 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 1001 1 NAG NAG A . C 2 NAG 1 1002 2 NAG NAG A . D 2 NAG 1 1003 3 NAG NAG A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 152 A ASN 152 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 192 A ASN 192 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 173 A ASN 173 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2000-01-10 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2018-01-31 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' 4 4 'Structure model' 'Experimental preparation' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category exptl_crystal_grow # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 4 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_exptl_crystal_grow.temp' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 SOLVE phasing . ? 3 CNS refinement 0.9 ? 4 # 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 LYS A 9 ? ? 79.27 -13.44 2 1 LYS A 36 ? ? 69.97 -28.90 3 1 VAL A 39 ? ? -123.78 -63.75 4 1 MET A 42 ? ? -110.04 55.94 5 1 MET A 43 ? ? -57.56 98.23 6 1 SER A 44 ? ? 34.14 72.40 7 1 ASN A 48 ? ? -162.05 105.43 8 1 ASN A 63 ? ? -100.26 68.29 9 1 LYS A 89 ? ? -21.45 112.98 10 1 ASP A 90 ? ? 108.58 -24.64 11 1 ALA A 106 ? ? -140.72 53.23 12 1 THR A 120 ? ? -165.89 117.46 13 1 ASN A 122 ? ? 80.89 -20.65 14 1 PRO A 135 ? ? -74.17 -164.10 15 1 GLU A 160 ? ? -75.22 -74.93 16 1 LEU A 189 ? ? -101.65 -167.83 17 1 ARG A 190 ? ? 179.66 137.09 18 1 THR A 199 ? ? -50.88 -103.53 # _pdbx_unobs_or_zero_occ_residues.id 1 _pdbx_unobs_or_zero_occ_residues.PDB_model_num 1 _pdbx_unobs_or_zero_occ_residues.polymer_flag Y _pdbx_unobs_or_zero_occ_residues.occupancy_flag 1 _pdbx_unobs_or_zero_occ_residues.auth_asym_id A _pdbx_unobs_or_zero_occ_residues.auth_comp_id LYS _pdbx_unobs_or_zero_occ_residues.auth_seq_id 201 _pdbx_unobs_or_zero_occ_residues.PDB_ins_code ? _pdbx_unobs_or_zero_occ_residues.label_asym_id A _pdbx_unobs_or_zero_occ_residues.label_comp_id LYS _pdbx_unobs_or_zero_occ_residues.label_seq_id 201 # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG #