data_2E47 # _entry.id 2E47 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 2E47 RCSB RCSB026203 WWPDB D_1000026203 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 2E47 _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2E47 _pdbx_database_status.recvd_initial_deposition_date 2006-12-05 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Park, S.-Y.' 1 'Hiraki, T.' 2 # _citation.id primary _citation.title 'the clock protein EA4 ticks away with movement of a mobile copper ion' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Hiraki, T.' 1 primary 'Shibayama, N.' 2 primary 'Tame, J.R.M.' 3 primary 'Akashi, S.' 4 primary 'Park, S.-Y.' 5 # _cell.entry_id 2E47 _cell.length_a 47.098 _cell.length_b 73.894 _cell.length_c 47.446 _cell.angle_alpha 90.00 _cell.angle_beta 104.07 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2E47 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Time interval measuring enzyme TIME' 16635.301 2 ? ? 'residues 1-156' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn 'COPPER (II) ION' 63.546 2 ? ? ? ? 5 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 6 water nat water 18.015 200 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name EA4 # _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 ;HHGFTTPSRAIAVLSTETIRGNITFTQVQDGKVHVQGGITGLPPGEYGFHVHEKGDLSGGCLSTGSHFNPEHKDHGHPND VNRHVGDLGNVVFDENHYSRIDLVDDQISLSGPHGIIGRAVVLHEKADDYGKSDHPDSRKTGNAGGRVACGVIGIL ; _entity_poly.pdbx_seq_one_letter_code_can ;HHGFTTPSRAIAVLSTETIRGNITFTQVQDGKVHVQGGITGLPPGEYGFHVHEKGDLSGGCLSTGSHFNPEHKDHGHPND VNRHVGDLGNVVFDENHYSRIDLVDDQISLSGPHGIIGRAVVLHEKADDYGKSDHPDSRKTGNAGGRVACGVIGIL ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 HIS n 1 2 HIS n 1 3 GLY n 1 4 PHE n 1 5 THR n 1 6 THR n 1 7 PRO n 1 8 SER n 1 9 ARG n 1 10 ALA n 1 11 ILE n 1 12 ALA n 1 13 VAL n 1 14 LEU n 1 15 SER n 1 16 THR n 1 17 GLU n 1 18 THR n 1 19 ILE n 1 20 ARG n 1 21 GLY n 1 22 ASN n 1 23 ILE n 1 24 THR n 1 25 PHE n 1 26 THR n 1 27 GLN n 1 28 VAL n 1 29 GLN n 1 30 ASP n 1 31 GLY n 1 32 LYS n 1 33 VAL n 1 34 HIS n 1 35 VAL n 1 36 GLN n 1 37 GLY n 1 38 GLY n 1 39 ILE n 1 40 THR n 1 41 GLY n 1 42 LEU n 1 43 PRO n 1 44 PRO n 1 45 GLY n 1 46 GLU n 1 47 TYR n 1 48 GLY n 1 49 PHE n 1 50 HIS n 1 51 VAL n 1 52 HIS n 1 53 GLU n 1 54 LYS n 1 55 GLY n 1 56 ASP n 1 57 LEU n 1 58 SER n 1 59 GLY n 1 60 GLY n 1 61 CYS n 1 62 LEU n 1 63 SER n 1 64 THR n 1 65 GLY n 1 66 SER n 1 67 HIS n 1 68 PHE n 1 69 ASN n 1 70 PRO n 1 71 GLU n 1 72 HIS n 1 73 LYS n 1 74 ASP n 1 75 HIS n 1 76 GLY n 1 77 HIS n 1 78 PRO n 1 79 ASN n 1 80 ASP n 1 81 VAL n 1 82 ASN n 1 83 ARG n 1 84 HIS n 1 85 VAL n 1 86 GLY n 1 87 ASP n 1 88 LEU n 1 89 GLY n 1 90 ASN n 1 91 VAL n 1 92 VAL n 1 93 PHE n 1 94 ASP n 1 95 GLU n 1 96 ASN n 1 97 HIS n 1 98 TYR n 1 99 SER n 1 100 ARG n 1 101 ILE n 1 102 ASP n 1 103 LEU n 1 104 VAL n 1 105 ASP n 1 106 ASP n 1 107 GLN n 1 108 ILE n 1 109 SER n 1 110 LEU n 1 111 SER n 1 112 GLY n 1 113 PRO n 1 114 HIS n 1 115 GLY n 1 116 ILE n 1 117 ILE n 1 118 GLY n 1 119 ARG n 1 120 ALA n 1 121 VAL n 1 122 VAL n 1 123 LEU n 1 124 HIS n 1 125 GLU n 1 126 LYS n 1 127 ALA n 1 128 ASP n 1 129 ASP n 1 130 TYR n 1 131 GLY n 1 132 LYS n 1 133 SER n 1 134 ASP n 1 135 HIS n 1 136 PRO n 1 137 ASP n 1 138 SER n 1 139 ARG n 1 140 LYS n 1 141 THR n 1 142 GLY n 1 143 ASN n 1 144 ALA n 1 145 GLY n 1 146 GLY n 1 147 ARG n 1 148 VAL n 1 149 ALA n 1 150 CYS n 1 151 GLY n 1 152 VAL n 1 153 ILE n 1 154 GLY n 1 155 ILE n 1 156 LEU 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 'domestic silkworm' _entity_src_gen.gene_src_genus Bombyx _entity_src_gen.pdbx_gene_src_gene ? _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 'Bombyx mori' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 7091 _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 'domestic silkworm' _entity_src_gen.pdbx_host_org_scientific_name 'Bombyx mori' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7091 _entity_src_gen.host_org_genus Bombyx _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 BmN4 _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type BACULOVIRUS _entity_src_gen.pdbx_host_org_vector BmNPV _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 Q08J22_BOMMO _struct_ref.pdbx_db_accession Q08J22 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;HHGFTTPSRAIAVLSTETIRGNITFTQVQDGKVHVQGGITGLPPGEYGFHVHEKGDLSGGCLSTGSHFNPEHKDHGHPND VNRHVGDLGNVVFDENHYSRIDLVDDQISLSGPHGIIGRAVVLHEKADDYGKSDHPDSRKTGNAGGRVACGVIGIL ; _struct_ref.pdbx_align_begin 17 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 2E47 A 1 ? 156 ? Q08J22 17 ? 172 ? 1 156 2 1 2E47 B 1 ? 156 ? Q08J22 17 ? 172 ? 1 156 # 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 CU non-polymer . 'COPPER (II) ION' ? 'Cu 2' 63.546 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 2E47 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.41 _exptl_crystal.density_percent_sol 48.88 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_details '27% PEG 3350, 500mM magnesium chloride, 20mM sodium fluoride, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector ? _diffrn_detector.type ? _diffrn_detector.pdbx_collection_date 2005-02-02 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'PHOTON FACTORY BEAMLINE AR-NW12A' _diffrn_source.pdbx_synchrotron_site 'Photon Factory' _diffrn_source.pdbx_synchrotron_beamline AR-NW12A _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1 # _reflns.entry_id 2E47 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.d_resolution_high 2.1 _reflns.d_resolution_low 20.0 _reflns.number_all ? _reflns.number_obs 17500 _reflns.percent_possible_obs 95.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.1 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.1 _reflns_shell.d_res_low 2.18 _reflns_shell.percent_possible_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy 4.1 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 17500 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2E47 _refine.ls_number_reflns_obs 16602 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.00 _refine.ls_d_res_high 2.11 _refine.ls_percent_reflns_obs 95.29 _refine.ls_R_factor_obs 0.17425 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17019 _refine.ls_R_factor_R_free 0.2511 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 878 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.958 _refine.correlation_coeff_Fo_to_Fc_free 0.904 _refine.B_iso_mean 32.620 _refine.aniso_B[1][1] -1.58 _refine.aniso_B[2][2] -1.45 _refine.aniso_B[3][3] 1.42 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] -3.30 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 1E9P _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.237 _refine.pdbx_overall_ESU_R_Free 0.215 _refine.overall_SU_ML 0.135 _refine.overall_SU_B 4.980 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2299 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 71 _refine_hist.number_atoms_solvent 200 _refine_hist.number_atoms_total 2570 _refine_hist.d_res_high 2.11 _refine_hist.d_res_low 20.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.023 0.021 ? 2441 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.066 1.961 ? 3294 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.773 5.000 ? 305 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 40.756 24.035 ? 114 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 18.015 15.000 ? 356 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 18.570 15.000 ? 14 'X-RAY DIFFRACTION' ? r_chiral_restr 0.159 0.200 ? 367 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.008 0.020 ? 1863 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.227 0.200 ? 1060 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.322 0.200 ? 1583 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.195 0.200 ? 191 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.292 0.200 ? 50 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.186 0.200 ? 12 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.468 1.500 ? 1534 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 2.388 2.000 ? 2405 'X-RAY DIFFRACTION' ? r_scbond_it 4.443 3.000 ? 974 'X-RAY DIFFRACTION' ? r_scangle_it 5.813 4.500 ? 889 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.105 _refine_ls_shell.d_res_low 2.159 _refine_ls_shell.number_reflns_R_work 1035 _refine_ls_shell.R_factor_R_work 0.174 _refine_ls_shell.percent_reflns_obs 79.72 _refine_ls_shell.R_factor_R_free 0.244 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 42 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 2E47 _struct.title 'Crystal Structure Analysis of the clock protein EA4 (glycosylation form)' _struct.pdbx_descriptor 'Time interval measuring enzyme TIME' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag N _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2E47 _struct_keywords.pdbx_keywords 'METAL BINDING PROTEIN' _struct_keywords.text 'motalloprotein, glycoprotein, METAL BINDING PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 4 ? G N N 5 ? H N N 2 ? I N N 2 ? J N N 4 ? K N N 5 ? L N N 6 ? M N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLN A 29 ? GLY A 31 ? GLN A 29 GLY A 31 5 ? 3 HELX_P HELX_P2 2 GLY A 59 ? GLY A 65 ? GLY A 59 GLY A 65 5 ? 7 HELX_P HELX_P3 3 ASP A 137 ? GLY A 142 ? ASP A 137 GLY A 142 1 ? 6 HELX_P HELX_P4 4 GLY B 59 ? GLY B 65 ? GLY B 59 GLY B 65 5 ? 7 HELX_P HELX_P5 5 SER B 111 ? GLY B 115 ? SER B 111 GLY B 115 5 ? 5 HELX_P HELX_P6 6 ASP B 137 ? GLY B 142 ? ASP B 137 GLY B 142 1 ? 6 # _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 61 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 61 A CYS 150 1_555 ? ? ? ? ? ? ? 2.179 ? disulf2 disulf ? ? B CYS 61 SG ? ? ? 1_555 B CYS 150 SG ? ? B CYS 61 B CYS 150 1_555 ? ? ? ? ? ? ? 2.200 ? covale1 covale ? ? A ASN 22 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 22 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.461 ? metalc1 metalc ? ? F CU . CU ? ? ? 1_555 A HIS 50 ND1 ? ? A CU 171 A HIS 50 1_555 ? ? ? ? ? ? ? 2.038 ? metalc2 metalc ? ? F CU . CU ? ? ? 1_555 A HIS 52 NE2 ? ? A CU 171 A HIS 52 1_555 ? ? ? ? ? ? ? 2.058 ? metalc3 metalc ? ? F CU . CU ? ? ? 1_555 A HIS 67 NE2 ? ? A CU 171 A HIS 67 1_555 ? ? ? ? ? ? ? 2.040 ? metalc4 metalc ? ? F CU . CU ? ? ? 1_555 A HIS 124 NE2 ? ? A CU 171 A HIS 124 1_555 ? ? ? ? ? ? ? 2.079 ? metalc5 metalc ? ? G ZN . ZN ? ? ? 1_555 A HIS 67 ND1 ? ? A ZN 172 A HIS 67 1_555 ? ? ? ? ? ? ? 2.048 ? metalc6 metalc ? ? G ZN . ZN ? ? ? 1_555 A HIS 75 ND1 ? ? A ZN 172 A HIS 75 1_555 ? ? ? ? ? ? ? 2.066 ? metalc7 metalc ? ? G ZN . ZN ? ? ? 1_555 A HIS 84 ND1 ? ? A ZN 172 A HIS 84 1_555 ? ? ? ? ? ? ? 2.087 ? metalc8 metalc ? ? G ZN . ZN ? ? ? 1_555 A ASP 87 OD1 ? ? A ZN 172 A ASP 87 1_555 ? ? ? ? ? ? ? 2.081 ? covale2 covale ? ? B ASN 22 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 22 B NAG 2001 1_555 ? ? ? ? ? ? ? 1.439 ? metalc9 metalc ? ? J CU . CU ? ? ? 1_555 B HIS 50 ND1 ? ? B CU 171 B HIS 50 1_555 ? ? ? ? ? ? ? 2.051 ? metalc10 metalc ? ? J CU . CU ? ? ? 1_555 B HIS 52 NE2 ? ? B CU 171 B HIS 52 1_555 ? ? ? ? ? ? ? 2.084 ? metalc11 metalc ? ? J CU . CU ? ? ? 1_555 B HIS 67 NE2 ? ? B CU 171 B HIS 67 1_555 ? ? ? ? ? ? ? 2.080 ? metalc12 metalc ? ? J CU . CU ? ? ? 1_555 B HIS 124 NE2 ? ? B CU 171 B HIS 124 1_555 ? ? ? ? ? ? ? 2.058 ? metalc13 metalc ? ? K ZN . ZN ? ? ? 1_555 B HIS 67 ND1 ? ? B ZN 172 B HIS 67 1_555 ? ? ? ? ? ? ? 2.077 ? metalc14 metalc ? ? K ZN . ZN ? ? ? 1_555 B HIS 75 ND1 ? ? B ZN 172 B HIS 75 1_555 ? ? ? ? ? ? ? 2.075 ? metalc15 metalc ? ? K ZN . ZN ? ? ? 1_555 B HIS 84 ND1 ? ? B ZN 172 B HIS 84 1_555 ? ? ? ? ? ? ? 2.070 ? metalc16 metalc ? ? K ZN . ZN ? ? ? 1_555 B ASP 87 OD1 ? ? B ZN 172 B ASP 87 1_555 ? ? ? ? ? ? ? 2.066 ? covale3 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1001 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.466 ? covale4 covale ? ? D NAG . O4 ? ? ? 1_555 E MAN . C1 ? ? A NAG 1002 A MAN 1003 1_555 ? ? ? ? ? ? ? 1.461 ? covale5 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? B NAG 2001 B NAG 2002 1_555 ? ? ? ? ? ? ? 1.460 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 4 ? C ? 5 ? 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 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? 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 TYR A 98 ? ASP A 105 ? TYR A 98 ASP A 105 A 2 VAL A 33 ? THR A 40 ? VAL A 33 THR A 40 A 3 ARG A 20 ? GLN A 27 ? ARG A 20 GLN A 27 A 4 ARG A 9 ? SER A 15 ? ARG A 9 SER A 15 A 5 GLY A 154 ? ILE A 155 ? GLY A 154 ILE A 155 B 1 ASP A 87 ? PHE A 93 ? ASP A 87 PHE A 93 B 2 GLY A 45 ? HIS A 52 ? GLY A 45 HIS A 52 B 3 ALA A 120 ? HIS A 124 ? ALA A 120 HIS A 124 B 4 ARG A 147 ? VAL A 152 ? ARG A 147 VAL A 152 C 1 TYR B 98 ? ASP B 105 ? TYR B 98 ASP B 105 C 2 VAL B 33 ? THR B 40 ? VAL B 33 THR B 40 C 3 ARG B 20 ? GLN B 27 ? ARG B 20 GLN B 27 C 4 ARG B 9 ? SER B 15 ? ARG B 9 SER B 15 C 5 GLY B 154 ? ILE B 155 ? GLY B 154 ILE B 155 D 1 ASP B 87 ? PHE B 93 ? ASP B 87 PHE B 93 D 2 GLY B 45 ? HIS B 52 ? GLY B 45 HIS B 52 D 3 ALA B 120 ? HIS B 124 ? ALA B 120 HIS B 124 D 4 ARG B 147 ? VAL B 152 ? ARG B 147 VAL B 152 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ILE A 101 ? O ILE A 101 N GLY A 37 ? N GLY A 37 A 2 3 O HIS A 34 ? O HIS A 34 N THR A 26 ? N THR A 26 A 3 4 O PHE A 25 ? O PHE A 25 N ALA A 10 ? N ALA A 10 A 4 5 N ILE A 11 ? N ILE A 11 O GLY A 154 ? O GLY A 154 B 1 2 O VAL A 91 ? O VAL A 91 N TYR A 47 ? N TYR A 47 B 2 3 N GLY A 48 ? N GLY A 48 O HIS A 124 ? O HIS A 124 B 3 4 N LEU A 123 ? N LEU A 123 O ALA A 149 ? O ALA A 149 C 1 2 O SER B 99 ? O SER B 99 N ILE B 39 ? N ILE B 39 C 2 3 O GLN B 36 ? O GLN B 36 N THR B 24 ? N THR B 24 C 3 4 O PHE B 25 ? O PHE B 25 N ALA B 10 ? N ALA B 10 C 4 5 N ILE B 11 ? N ILE B 11 O GLY B 154 ? O GLY B 154 D 1 2 O PHE B 93 ? O PHE B 93 N GLY B 45 ? N GLY B 45 D 2 3 N HIS B 52 ? N HIS B 52 O ALA B 120 ? O ALA B 120 D 3 4 N LEU B 123 ? N LEU B 123 O ALA B 149 ? O ALA B 149 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1001' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1002' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 1003' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 2001' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 2002' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 171' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 172' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU B 171' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 172' # 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 4 ILE A 11 ? ILE A 11 . ? 1_555 ? 2 AC1 4 ASN A 22 ? ASN A 22 . ? 1_555 ? 3 AC1 4 NAG D . ? NAG A 1002 . ? 1_555 ? 4 AC1 4 SER B 58 ? SER B 58 . ? 1_555 ? 5 AC2 3 ASP A 134 ? ASP A 134 . ? 1_554 ? 6 AC2 3 NAG C . ? NAG A 1001 . ? 1_555 ? 7 AC2 3 MAN E . ? MAN A 1003 . ? 1_555 ? 8 AC3 2 ASP A 134 ? ASP A 134 . ? 1_554 ? 9 AC3 2 NAG D . ? NAG A 1002 . ? 1_555 ? 10 AC4 7 SER A 58 ? SER A 58 . ? 1_555 ? 11 AC4 7 ASN B 22 ? ASN B 22 . ? 1_555 ? 12 AC4 7 GLY B 38 ? GLY B 38 . ? 1_555 ? 13 AC4 7 NAG I . ? NAG B 2002 . ? 1_555 ? 14 AC4 7 HOH M . ? HOH B 2041 . ? 1_555 ? 15 AC4 7 HOH M . ? HOH B 2055 . ? 1_555 ? 16 AC4 7 HOH M . ? HOH B 2088 . ? 1_555 ? 17 AC5 1 NAG H . ? NAG B 2001 . ? 1_555 ? 18 AC6 4 HIS A 50 ? HIS A 50 . ? 1_555 ? 19 AC6 4 HIS A 52 ? HIS A 52 . ? 1_555 ? 20 AC6 4 HIS A 67 ? HIS A 67 . ? 1_555 ? 21 AC6 4 HIS A 124 ? HIS A 124 . ? 1_555 ? 22 AC7 4 HIS A 67 ? HIS A 67 . ? 1_555 ? 23 AC7 4 HIS A 75 ? HIS A 75 . ? 1_555 ? 24 AC7 4 HIS A 84 ? HIS A 84 . ? 1_555 ? 25 AC7 4 ASP A 87 ? ASP A 87 . ? 1_555 ? 26 AC8 5 HIS B 50 ? HIS B 50 . ? 1_555 ? 27 AC8 5 HIS B 52 ? HIS B 52 . ? 1_555 ? 28 AC8 5 HIS B 67 ? HIS B 67 . ? 1_555 ? 29 AC8 5 HIS B 124 ? HIS B 124 . ? 1_555 ? 30 AC8 5 HOH M . ? HOH B 2019 . ? 1_555 ? 31 AC9 4 HIS B 67 ? HIS B 67 . ? 1_555 ? 32 AC9 4 HIS B 75 ? HIS B 75 . ? 1_555 ? 33 AC9 4 HIS B 84 ? HIS B 84 . ? 1_555 ? 34 AC9 4 ASP B 87 ? ASP B 87 . ? 1_555 ? # _database_PDB_matrix.entry_id 2E47 _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 2E47 _atom_sites.fract_transf_matrix[1][1] 0.021232 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.005321 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013533 _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] 0.021728 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CU N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . HIS A 1 2 ? 5.404 -13.896 -7.972 1.00 50.65 ? 2 HIS A N 1 ATOM 2 C CA . HIS A 1 2 ? 4.694 -15.065 -7.312 1.00 49.39 ? 2 HIS A CA 1 ATOM 3 C C . HIS A 1 2 ? 5.596 -16.264 -7.121 1.00 48.11 ? 2 HIS A C 1 ATOM 4 O O . HIS A 1 2 ? 5.917 -16.977 -8.064 1.00 50.07 ? 2 HIS A O 1 ATOM 5 C CB . HIS A 1 2 ? 3.447 -15.507 -8.116 1.00 49.41 ? 2 HIS A CB 1 ATOM 6 C CG . HIS A 1 2 ? 2.241 -14.662 -7.859 1.00 52.00 ? 2 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 2 ? 1.855 -14.282 -6.584 1.00 54.03 ? 2 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 2 ? 1.329 -14.127 -8.706 1.00 53.22 ? 2 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 2 ? 0.766 -13.539 -6.659 1.00 55.73 ? 2 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 2 ? 0.428 -13.427 -7.935 1.00 58.24 ? 2 HIS A NE2 1 ATOM 11 N N . GLY A 1 3 ? 6.042 -16.531 -5.932 1.00 46.29 ? 3 GLY A N 1 ATOM 12 C CA . GLY A 1 3 ? 6.601 -17.871 -5.745 1.00 44.14 ? 3 GLY A CA 1 ATOM 13 C C . GLY A 1 3 ? 5.609 -18.548 -4.852 1.00 42.16 ? 3 GLY A C 1 ATOM 14 O O . GLY A 1 3 ? 4.412 -18.423 -5.054 1.00 43.05 ? 3 GLY A O 1 ATOM 15 N N . PHE A 1 4 ? 6.076 -19.244 -3.824 1.00 40.96 ? 4 PHE A N 1 ATOM 16 C CA . PHE A 1 4 ? 5.128 -19.662 -2.773 1.00 38.79 ? 4 PHE A CA 1 ATOM 17 C C . PHE A 1 4 ? 4.533 -18.423 -2.073 1.00 37.83 ? 4 PHE A C 1 ATOM 18 O O . PHE A 1 4 ? 5.122 -17.366 -2.063 1.00 36.01 ? 4 PHE A O 1 ATOM 19 C CB . PHE A 1 4 ? 5.800 -20.611 -1.779 1.00 38.10 ? 4 PHE A CB 1 ATOM 20 C CG . PHE A 1 4 ? 6.199 -21.907 -2.404 1.00 37.64 ? 4 PHE A CG 1 ATOM 21 C CD1 . PHE A 1 4 ? 7.520 -22.330 -2.373 1.00 37.67 ? 4 PHE A CD1 1 ATOM 22 C CD2 . PHE A 1 4 ? 5.249 -22.680 -3.097 1.00 36.27 ? 4 PHE A CD2 1 ATOM 23 C CE1 . PHE A 1 4 ? 7.882 -23.519 -2.986 1.00 36.75 ? 4 PHE A CE1 1 ATOM 24 C CE2 . PHE A 1 4 ? 5.598 -23.849 -3.690 1.00 35.02 ? 4 PHE A CE2 1 ATOM 25 C CZ . PHE A 1 4 ? 6.927 -24.264 -3.650 1.00 35.91 ? 4 PHE A CZ 1 ATOM 26 N N . THR A 1 5 ? 3.347 -18.561 -1.515 1.00 36.73 ? 5 THR A N 1 ATOM 27 C CA . THR A 1 5 ? 2.856 -17.513 -0.651 1.00 36.92 ? 5 THR A CA 1 ATOM 28 C C . THR A 1 5 ? 3.590 -17.747 0.674 1.00 38.46 ? 5 THR A C 1 ATOM 29 O O . THR A 1 5 ? 4.098 -18.858 0.914 1.00 37.51 ? 5 THR A O 1 ATOM 30 C CB . THR A 1 5 ? 1.389 -17.670 -0.379 1.00 35.92 ? 5 THR A CB 1 ATOM 31 O OG1 . THR A 1 5 ? 1.169 -19.053 -0.080 1.00 35.40 ? 5 THR A OG1 1 ATOM 32 C CG2 . THR A 1 5 ? 0.576 -17.227 -1.592 1.00 31.97 ? 5 THR A CG2 1 ATOM 33 N N . THR A 1 6 ? 3.597 -16.710 1.520 1.00 38.84 ? 6 THR A N 1 ATOM 34 C CA . THR A 1 6 ? 4.510 -16.617 2.656 1.00 40.51 ? 6 THR A CA 1 ATOM 35 C C . THR A 1 6 ? 3.681 -16.097 3.839 1.00 39.72 ? 6 THR A C 1 ATOM 36 O O . THR A 1 6 ? 2.960 -15.106 3.705 1.00 39.43 ? 6 THR A O 1 ATOM 37 C CB . THR A 1 6 ? 5.710 -15.615 2.378 1.00 40.63 ? 6 THR A CB 1 ATOM 38 O OG1 . THR A 1 6 ? 5.305 -14.304 2.746 1.00 43.49 ? 6 THR A OG1 1 ATOM 39 C CG2 . THR A 1 6 ? 6.105 -15.540 0.874 1.00 42.03 ? 6 THR A CG2 1 ATOM 40 N N . PRO A 1 7 ? 3.807 -16.753 5.004 1.00 39.84 ? 7 PRO A N 1 ATOM 41 C CA . PRO A 1 7 ? 2.957 -16.368 6.124 1.00 40.40 ? 7 PRO A CA 1 ATOM 42 C C . PRO A 1 7 ? 3.511 -15.095 6.790 1.00 40.56 ? 7 PRO A C 1 ATOM 43 O O . PRO A 1 7 ? 4.620 -14.627 6.448 1.00 39.35 ? 7 PRO A O 1 ATOM 44 C CB . PRO A 1 7 ? 3.023 -17.578 7.059 1.00 40.94 ? 7 PRO A CB 1 ATOM 45 C CG . PRO A 1 7 ? 4.361 -18.308 6.688 1.00 39.48 ? 7 PRO A CG 1 ATOM 46 C CD . PRO A 1 7 ? 4.786 -17.817 5.339 1.00 40.10 ? 7 PRO A CD 1 ATOM 47 N N . SER A 1 8 ? 2.709 -14.549 7.702 1.00 40.61 ? 8 SER A N 1 ATOM 48 C CA . SER A 1 8 ? 3.030 -13.345 8.480 1.00 39.14 ? 8 SER A CA 1 ATOM 49 C C . SER A 1 8 ? 4.248 -13.519 9.355 1.00 36.66 ? 8 SER A C 1 ATOM 50 O O . SER A 1 8 ? 4.353 -14.511 10.089 1.00 36.41 ? 8 SER A O 1 ATOM 51 C CB . SER A 1 8 ? 1.856 -12.973 9.381 1.00 40.59 ? 8 SER A CB 1 ATOM 52 O OG . SER A 1 8 ? 1.302 -11.745 8.919 1.00 45.11 ? 8 SER A OG 1 ATOM 53 N N . ARG A 1 9 ? 5.171 -12.562 9.229 1.00 32.81 ? 9 ARG A N 1 ATOM 54 C CA . ARG A 1 9 ? 6.294 -12.408 10.154 1.00 31.20 ? 9 ARG A CA 1 ATOM 55 C C . ARG A 1 9 ? 6.313 -10.962 10.700 1.00 28.55 ? 9 ARG A C 1 ATOM 56 O O . ARG A 1 9 ? 5.596 -10.083 10.212 1.00 27.00 ? 9 ARG A O 1 ATOM 57 C CB . ARG A 1 9 ? 7.614 -12.734 9.449 1.00 31.44 ? 9 ARG A CB 1 ATOM 58 C CG . ARG A 1 9 ? 7.595 -14.107 8.762 1.00 35.90 ? 9 ARG A CG 1 ATOM 59 C CD . ARG A 1 9 ? 8.970 -14.533 8.273 1.00 41.82 ? 9 ARG A CD 1 ATOM 60 N NE . ARG A 1 9 ? 9.527 -13.628 7.246 1.00 47.31 ? 9 ARG A NE 1 ATOM 61 C CZ . ARG A 1 9 ? 10.840 -13.441 7.020 1.00 47.55 ? 9 ARG A CZ 1 ATOM 62 N NH1 . ARG A 1 9 ? 11.767 -14.098 7.736 1.00 43.87 ? 9 ARG A NH1 1 ATOM 63 N NH2 . ARG A 1 9 ? 11.227 -12.570 6.085 1.00 48.42 ? 9 ARG A NH2 1 ATOM 64 N N . ALA A 1 10 ? 7.146 -10.719 11.697 1.00 25.73 ? 10 ALA A N 1 ATOM 65 C CA . ALA A 1 10 ? 7.283 -9.384 12.259 1.00 23.94 ? 10 ALA A CA 1 ATOM 66 C C . ALA A 1 10 ? 8.719 -9.213 12.661 1.00 22.72 ? 10 ALA A C 1 ATOM 67 O O . ALA A 1 10 ? 9.466 -10.175 12.748 1.00 22.22 ? 10 ALA A O 1 ATOM 68 C CB . ALA A 1 10 ? 6.380 -9.237 13.433 1.00 22.28 ? 10 ALA A CB 1 ATOM 69 N N . ILE A 1 11 ? 9.132 -7.991 12.894 1.00 21.34 ? 11 ILE A N 1 ATOM 70 C CA . ILE A 1 11 ? 10.539 -7.746 13.133 1.00 21.35 ? 11 ILE A CA 1 ATOM 71 C C . ILE A 1 11 ? 10.588 -6.468 13.966 1.00 20.17 ? 11 ILE A C 1 ATOM 72 O O . ILE A 1 11 ? 9.680 -5.608 13.838 1.00 20.44 ? 11 ILE A O 1 ATOM 73 C CB . ILE A 1 11 ? 11.279 -7.478 11.826 1.00 21.89 ? 11 ILE A CB 1 ATOM 74 C CG1 . ILE A 1 11 ? 12.776 -7.257 12.116 1.00 22.16 ? 11 ILE A CG1 1 ATOM 75 C CG2 . ILE A 1 11 ? 10.708 -6.211 11.108 1.00 22.70 ? 11 ILE A CG2 1 ATOM 76 C CD1 . ILE A 1 11 ? 13.705 -7.485 10.847 1.00 24.22 ? 11 ILE A CD1 1 ATOM 77 N N . ALA A 1 12 ? 11.569 -6.381 14.860 1.00 19.38 ? 12 ALA A N 1 ATOM 78 C CA . ALA A 1 12 ? 11.829 -5.157 15.682 1.00 19.96 ? 12 ALA A CA 1 ATOM 79 C C . ALA A 1 12 ? 13.288 -4.893 15.503 1.00 19.98 ? 12 ALA A C 1 ATOM 80 O O . ALA A 1 12 ? 14.090 -5.851 15.479 1.00 21.31 ? 12 ALA A O 1 ATOM 81 C CB . ALA A 1 12 ? 11.589 -5.431 17.189 1.00 16.07 ? 12 ALA A CB 1 ATOM 82 N N . VAL A 1 13 ? 13.665 -3.637 15.433 1.00 19.40 ? 13 VAL A N 1 ATOM 83 C CA . VAL A 1 13 ? 15.062 -3.296 15.275 1.00 19.26 ? 13 VAL A CA 1 ATOM 84 C C . VAL A 1 13 ? 15.465 -2.496 16.474 1.00 18.99 ? 13 VAL A C 1 ATOM 85 O O . VAL A 1 13 ? 14.792 -1.572 16.830 1.00 18.73 ? 13 VAL A O 1 ATOM 86 C CB . VAL A 1 13 ? 15.293 -2.497 13.920 1.00 19.78 ? 13 VAL A CB 1 ATOM 87 C CG1 . VAL A 1 13 ? 16.650 -1.986 13.829 1.00 21.11 ? 13 VAL A CG1 1 ATOM 88 C CG2 . VAL A 1 13 ? 14.990 -3.418 12.679 1.00 19.98 ? 13 VAL A CG2 1 ATOM 89 N N . LEU A 1 14 ? 16.558 -2.853 17.112 1.00 20.25 ? 14 LEU A N 1 ATOM 90 C CA . LEU A 1 14 ? 17.168 -2.045 18.187 1.00 22.37 ? 14 LEU A CA 1 ATOM 91 C C . LEU A 1 14 ? 18.330 -1.212 17.583 1.00 26.19 ? 14 LEU A C 1 ATOM 92 O O . LEU A 1 14 ? 19.136 -1.774 16.841 1.00 24.24 ? 14 LEU A O 1 ATOM 93 C CB . LEU A 1 14 ? 17.797 -3.044 19.131 1.00 22.92 ? 14 LEU A CB 1 ATOM 94 C CG . LEU A 1 14 ? 16.956 -3.575 20.307 1.00 25.36 ? 14 LEU A CG 1 ATOM 95 C CD1 . LEU A 1 14 ? 15.489 -3.273 20.201 1.00 21.04 ? 14 LEU A CD1 1 ATOM 96 C CD2 . LEU A 1 14 ? 17.279 -4.966 20.819 1.00 22.21 ? 14 LEU A CD2 1 ATOM 97 N N . SER A 1 15 ? 18.425 0.084 17.887 1.00 27.95 ? 15 SER A N 1 ATOM 98 C CA . SER A 1 15 ? 19.432 0.900 17.288 1.00 31.79 ? 15 SER A CA 1 ATOM 99 C C . SER A 1 15 ? 19.703 2.118 18.213 1.00 31.83 ? 15 SER A C 1 ATOM 100 O O . SER A 1 15 ? 18.866 3.035 18.308 1.00 31.78 ? 15 SER A O 1 ATOM 101 C CB . SER A 1 15 ? 19.002 1.357 15.867 1.00 31.02 ? 15 SER A CB 1 ATOM 102 O OG . SER A 1 15 ? 20.171 1.757 15.132 1.00 39.49 ? 15 SER A OG 1 ATOM 103 N N . THR A 1 16 ? 20.875 2.076 18.857 1.00 31.30 ? 16 THR A N 1 ATOM 104 C CA . THR A 1 16 ? 21.347 2.983 19.882 1.00 31.83 ? 16 THR A CA 1 ATOM 105 C C . THR A 1 16 ? 22.818 3.315 19.443 1.00 32.59 ? 16 THR A C 1 ATOM 106 O O . THR A 1 16 ? 23.319 2.696 18.481 1.00 30.40 ? 16 THR A O 1 ATOM 107 C CB . THR A 1 16 ? 21.205 2.187 21.208 1.00 32.26 ? 16 THR A CB 1 ATOM 108 O OG1 . THR A 1 16 ? 19.944 2.510 21.847 1.00 38.35 ? 16 THR A OG1 1 ATOM 109 C CG2 . THR A 1 16 ? 22.310 2.257 22.163 1.00 31.17 ? 16 THR A CG2 1 ATOM 110 N N . GLU A 1 17 ? 23.470 4.286 20.104 1.00 32.44 ? 17 GLU A N 1 ATOM 111 C CA . GLU A 1 17 ? 24.888 4.527 19.901 1.00 35.09 ? 17 GLU A CA 1 ATOM 112 C C . GLU A 1 17 ? 25.680 3.238 20.160 1.00 34.96 ? 17 GLU A C 1 ATOM 113 O O . GLU A 1 17 ? 26.655 2.947 19.434 1.00 34.21 ? 17 GLU A O 1 ATOM 114 C CB . GLU A 1 17 ? 25.424 5.614 20.853 1.00 36.21 ? 17 GLU A CB 1 ATOM 115 C CG . GLU A 1 17 ? 25.079 7.081 20.482 1.00 43.28 ? 17 GLU A CG 1 ATOM 116 C CD . GLU A 1 17 ? 25.144 7.359 18.970 1.00 51.28 ? 17 GLU A CD 1 ATOM 117 O OE1 . GLU A 1 17 ? 26.267 7.400 18.388 1.00 55.16 ? 17 GLU A OE1 1 ATOM 118 O OE2 . GLU A 1 17 ? 24.064 7.546 18.365 1.00 53.82 ? 17 GLU A OE2 1 ATOM 119 N N . THR A 1 18 ? 25.276 2.478 21.195 1.00 32.70 ? 18 THR A N 1 ATOM 120 C CA . THR A 1 18 ? 26.018 1.261 21.570 1.00 32.26 ? 18 THR A CA 1 ATOM 121 C C . THR A 1 18 ? 25.405 -0.100 21.176 1.00 30.93 ? 18 THR A C 1 ATOM 122 O O . THR A 1 18 ? 26.130 -1.080 21.048 1.00 30.52 ? 18 THR A O 1 ATOM 123 C CB . THR A 1 18 ? 26.378 1.262 23.098 1.00 33.10 ? 18 THR A CB 1 ATOM 124 O OG1 . THR A 1 18 ? 25.183 1.438 23.869 1.00 36.58 ? 18 THR A OG1 1 ATOM 125 C CG2 . THR A 1 18 ? 27.355 2.440 23.458 1.00 35.31 ? 18 THR A CG2 1 ATOM 126 N N . ILE A 1 19 ? 24.093 -0.159 20.975 1.00 28.88 ? 19 ILE A N 1 ATOM 127 C CA . ILE A 1 19 ? 23.402 -1.426 20.821 1.00 27.83 ? 19 ILE A CA 1 ATOM 128 C C . ILE A 1 19 ? 22.737 -1.540 19.477 1.00 27.88 ? 19 ILE A C 1 ATOM 129 O O . ILE A 1 19 ? 22.095 -0.579 19.034 1.00 28.00 ? 19 ILE A O 1 ATOM 130 C CB . ILE A 1 19 ? 22.358 -1.615 21.978 1.00 28.74 ? 19 ILE A CB 1 ATOM 131 C CG1 . ILE A 1 19 ? 23.085 -2.026 23.275 1.00 26.26 ? 19 ILE A CG1 1 ATOM 132 C CG2 . ILE A 1 19 ? 21.282 -2.659 21.557 1.00 26.69 ? 19 ILE A CG2 1 ATOM 133 C CD1 . ILE A 1 19 ? 22.336 -1.805 24.449 1.00 28.03 ? 19 ILE A CD1 1 ATOM 134 N N . ARG A 1 20 ? 22.919 -2.685 18.809 1.00 27.73 ? 20 ARG A N 1 ATOM 135 C CA . ARG A 1 20 ? 22.281 -2.926 17.524 1.00 28.21 ? 20 ARG A CA 1 ATOM 136 C C . ARG A 1 20 ? 21.770 -4.328 17.433 1.00 26.90 ? 20 ARG A C 1 ATOM 137 O O . ARG A 1 20 ? 22.486 -5.284 17.768 1.00 26.04 ? 20 ARG A O 1 ATOM 138 C CB . ARG A 1 20 ? 23.253 -2.722 16.315 1.00 30.00 ? 20 ARG A CB 1 ATOM 139 C CG . ARG A 1 20 ? 24.123 -1.477 16.390 1.00 34.61 ? 20 ARG A CG 1 ATOM 140 C CD . ARG A 1 20 ? 23.542 -0.345 15.595 1.00 45.09 ? 20 ARG A CD 1 ATOM 141 N NE . ARG A 1 20 ? 24.636 0.329 14.872 1.00 56.17 ? 20 ARG A NE 1 ATOM 142 C CZ . ARG A 1 20 ? 25.228 1.460 15.275 1.00 57.81 ? 20 ARG A CZ 1 ATOM 143 N NH1 . ARG A 1 20 ? 26.219 1.983 14.549 1.00 58.11 ? 20 ARG A NH1 1 ATOM 144 N NH2 . ARG A 1 20 ? 24.817 2.075 16.392 1.00 56.63 ? 20 ARG A NH2 1 ATOM 145 N N . GLY A 1 21 ? 20.564 -4.460 16.892 1.00 24.84 ? 21 GLY A N 1 ATOM 146 C CA . GLY A 1 21 ? 20.052 -5.780 16.622 1.00 24.44 ? 21 GLY A CA 1 ATOM 147 C C . GLY A 1 21 ? 18.808 -5.813 15.798 1.00 24.54 ? 21 GLY A C 1 ATOM 148 O O . GLY A 1 21 ? 18.162 -4.787 15.590 1.00 25.02 ? 21 GLY A O 1 ATOM 149 N N . ASN A 1 22 ? 18.508 -7.007 15.296 1.00 25.42 ? 22 ASN A N 1 ATOM 150 C CA . ASN A 1 22 ? 17.257 -7.334 14.609 1.00 26.08 ? 22 ASN A CA 1 ATOM 151 C C . ASN A 1 22 ? 16.687 -8.513 15.348 1.00 25.00 ? 22 ASN A C 1 ATOM 152 O O . ASN A 1 22 ? 17.423 -9.474 15.641 1.00 24.28 ? 22 ASN A O 1 ATOM 153 C CB . ASN A 1 22 ? 17.525 -7.822 13.169 1.00 28.80 ? 22 ASN A CB 1 ATOM 154 C CG . ASN A 1 22 ? 18.287 -6.771 12.331 1.00 35.55 ? 22 ASN A CG 1 ATOM 155 O OD1 . ASN A 1 22 ? 17.794 -5.633 12.189 1.00 35.05 ? 22 ASN A OD1 1 ATOM 156 N ND2 . ASN A 1 22 ? 19.514 -7.123 11.859 1.00 43.65 ? 22 ASN A ND2 1 ATOM 157 N N . ILE A 1 23 ? 15.393 -8.446 15.613 1.00 23.25 ? 23 ILE A N 1 ATOM 158 C CA . ILE A 1 23 ? 14.622 -9.572 16.184 1.00 23.61 ? 23 ILE A CA 1 ATOM 159 C C . ILE A 1 23 ? 13.417 -9.839 15.328 1.00 23.24 ? 23 ILE A C 1 ATOM 160 O O . ILE A 1 23 ? 12.626 -8.934 15.110 1.00 20.91 ? 23 ILE A O 1 ATOM 161 C CB . ILE A 1 23 ? 14.224 -9.296 17.666 1.00 25.08 ? 23 ILE A CB 1 ATOM 162 C CG1 . ILE A 1 23 ? 15.495 -9.019 18.483 1.00 25.29 ? 23 ILE A CG1 1 ATOM 163 C CG2 . ILE A 1 23 ? 13.440 -10.540 18.321 1.00 24.25 ? 23 ILE A CG2 1 ATOM 164 C CD1 . ILE A 1 23 ? 15.739 -7.585 18.562 1.00 32.84 ? 23 ILE A CD1 1 ATOM 165 N N . THR A 1 24 ? 13.297 -11.094 14.870 1.00 21.24 ? 24 THR A N 1 ATOM 166 C CA . THR A 1 24 ? 12.339 -11.536 13.914 1.00 21.31 ? 24 THR A CA 1 ATOM 167 C C . THR A 1 24 ? 11.337 -12.497 14.632 1.00 20.88 ? 24 THR A C 1 ATOM 168 O O . THR A 1 24 ? 11.761 -13.250 15.480 1.00 18.73 ? 24 THR A O 1 ATOM 169 C CB . THR A 1 24 ? 13.181 -12.250 12.803 1.00 23.66 ? 24 THR A CB 1 ATOM 170 O OG1 . THR A 1 24 ? 13.475 -11.332 11.701 1.00 30.33 ? 24 THR A OG1 1 ATOM 171 C CG2 . THR A 1 24 ? 12.646 -13.482 12.374 1.00 24.29 ? 24 THR A CG2 1 ATOM 172 N N . PHE A 1 25 ? 10.061 -12.492 14.254 1.00 18.90 ? 25 PHE A N 1 ATOM 173 C CA . PHE A 1 25 ? 9.056 -13.352 14.914 1.00 20.61 ? 25 PHE A CA 1 ATOM 174 C C . PHE A 1 25 ? 8.367 -14.109 13.820 1.00 21.79 ? 25 PHE A C 1 ATOM 175 O O . PHE A 1 25 ? 7.827 -13.485 12.939 1.00 21.95 ? 25 PHE A O 1 ATOM 176 C CB . PHE A 1 25 ? 8.014 -12.469 15.593 1.00 19.85 ? 25 PHE A CB 1 ATOM 177 C CG . PHE A 1 25 ? 8.587 -11.554 16.655 1.00 20.25 ? 25 PHE A CG 1 ATOM 178 C CD1 . PHE A 1 25 ? 8.506 -11.923 18.002 1.00 25.21 ? 25 PHE A CD1 1 ATOM 179 C CD2 . PHE A 1 25 ? 9.212 -10.367 16.313 1.00 21.23 ? 25 PHE A CD2 1 ATOM 180 C CE1 . PHE A 1 25 ? 9.032 -11.110 18.984 1.00 25.89 ? 25 PHE A CE1 1 ATOM 181 C CE2 . PHE A 1 25 ? 9.763 -9.511 17.286 1.00 23.53 ? 25 PHE A CE2 1 ATOM 182 C CZ . PHE A 1 25 ? 9.657 -9.870 18.633 1.00 21.03 ? 25 PHE A CZ 1 ATOM 183 N N . THR A 1 26 ? 8.305 -15.427 13.883 1.00 22.93 ? 26 THR A N 1 ATOM 184 C CA . THR A 1 26 ? 7.723 -16.193 12.804 1.00 25.56 ? 26 THR A CA 1 ATOM 185 C C . THR A 1 26 ? 6.861 -17.251 13.429 1.00 26.94 ? 26 THR A C 1 ATOM 186 O O . THR A 1 26 ? 7.263 -17.897 14.400 1.00 28.19 ? 26 THR A O 1 ATOM 187 C CB . THR A 1 26 ? 8.847 -16.825 11.916 1.00 26.76 ? 26 THR A CB 1 ATOM 188 O OG1 . THR A 1 26 ? 9.598 -17.714 12.718 1.00 33.93 ? 26 THR A OG1 1 ATOM 189 C CG2 . THR A 1 26 ? 9.871 -15.810 11.587 1.00 24.64 ? 26 THR A CG2 1 ATOM 190 N N . GLN A 1 27 ? 5.648 -17.386 12.922 1.00 27.70 ? 27 GLN A N 1 ATOM 191 C CA . GLN A 1 27 ? 4.689 -18.269 13.495 1.00 31.16 ? 27 GLN A CA 1 ATOM 192 C C . GLN A 1 27 ? 5.110 -19.670 13.051 1.00 32.23 ? 27 GLN A C 1 ATOM 193 O O . GLN A 1 27 ? 5.571 -19.839 11.938 1.00 32.23 ? 27 GLN A O 1 ATOM 194 C CB . GLN A 1 27 ? 3.268 -17.912 12.994 1.00 31.02 ? 27 GLN A CB 1 ATOM 195 C CG . GLN A 1 27 ? 2.152 -18.684 13.752 1.00 35.61 ? 27 GLN A CG 1 ATOM 196 C CD . GLN A 1 27 ? 0.900 -17.839 14.082 1.00 39.47 ? 27 GLN A CD 1 ATOM 197 O OE1 . GLN A 1 27 ? 0.953 -16.608 14.239 1.00 42.41 ? 27 GLN A OE1 1 ATOM 198 N NE2 . GLN A 1 27 ? -0.229 -18.528 14.250 1.00 43.47 ? 27 GLN A NE2 1 ATOM 199 N N . VAL A 1 28 ? 5.049 -20.631 13.960 1.00 33.36 ? 28 VAL A N 1 ATOM 200 C CA . VAL A 1 28 ? 5.428 -21.998 13.651 1.00 34.31 ? 28 VAL A CA 1 ATOM 201 C C . VAL A 1 28 ? 4.257 -22.921 14.051 1.00 36.22 ? 28 VAL A C 1 ATOM 202 O O . VAL A 1 28 ? 3.176 -22.451 14.433 1.00 34.45 ? 28 VAL A O 1 ATOM 203 C CB . VAL A 1 28 ? 6.831 -22.425 14.284 1.00 34.55 ? 28 VAL A CB 1 ATOM 204 C CG1 . VAL A 1 28 ? 7.984 -21.661 13.694 1.00 33.08 ? 28 VAL A CG1 1 ATOM 205 C CG2 . VAL A 1 28 ? 6.883 -22.266 15.771 1.00 33.77 ? 28 VAL A CG2 1 ATOM 206 N N . GLN A 1 29 ? 4.504 -24.228 14.015 1.00 39.28 ? 29 GLN A N 1 ATOM 207 C CA . GLN A 1 29 ? 3.512 -25.248 14.367 1.00 41.06 ? 29 GLN A CA 1 ATOM 208 C C . GLN A 1 29 ? 2.728 -24.998 15.667 1.00 42.71 ? 29 GLN A C 1 ATOM 209 O O . GLN A 1 29 ? 3.276 -24.607 16.717 1.00 42.63 ? 29 GLN A O 1 ATOM 210 C CB . GLN A 1 29 ? 4.153 -26.650 14.346 1.00 41.97 ? 29 GLN A CB 1 ATOM 211 C CG . GLN A 1 29 ? 5.151 -26.892 13.142 1.00 43.57 ? 29 GLN A CG 1 ATOM 212 C CD . GLN A 1 29 ? 6.451 -25.995 13.203 1.00 47.62 ? 29 GLN A CD 1 ATOM 213 O OE1 . GLN A 1 29 ? 6.917 -25.441 12.173 1.00 42.75 ? 29 GLN A OE1 1 ATOM 214 N NE2 . GLN A 1 29 ? 7.038 -25.879 14.415 1.00 49.24 ? 29 GLN A NE2 1 ATOM 215 N N . ASP A 1 30 ? 1.415 -25.178 15.539 1.00 43.39 ? 30 ASP A N 1 ATOM 216 C CA . ASP A 1 30 ? 0.453 -25.050 16.624 1.00 44.51 ? 30 ASP A CA 1 ATOM 217 C C . ASP A 1 30 ? 0.342 -23.648 17.212 1.00 42.74 ? 30 ASP A C 1 ATOM 218 O O . ASP A 1 30 ? -0.048 -23.462 18.358 1.00 42.24 ? 30 ASP A O 1 ATOM 219 C CB . ASP A 1 30 ? 0.670 -26.174 17.653 1.00 46.10 ? 30 ASP A CB 1 ATOM 220 C CG . ASP A 1 30 ? 0.661 -27.608 16.976 1.00 50.85 ? 30 ASP A CG 1 ATOM 221 O OD1 . ASP A 1 30 ? -0.366 -27.991 16.334 1.00 53.35 ? 30 ASP A OD1 1 ATOM 222 O OD2 . ASP A 1 30 ? 1.684 -28.349 17.068 1.00 56.27 ? 30 ASP A OD2 1 ATOM 223 N N . GLY A 1 31 ? 0.661 -22.649 16.388 1.00 41.47 ? 31 GLY A N 1 ATOM 224 C CA . GLY A 1 31 ? 0.434 -21.240 16.769 1.00 38.28 ? 31 GLY A CA 1 ATOM 225 C C . GLY A 1 31 ? 1.510 -20.625 17.671 1.00 36.52 ? 31 GLY A C 1 ATOM 226 O O . GLY A 1 31 ? 1.349 -19.518 18.164 1.00 37.14 ? 31 GLY A O 1 ATOM 227 N N . LYS A 1 32 ? 2.609 -21.310 17.887 1.00 33.98 ? 32 LYS A N 1 ATOM 228 C CA . LYS A 1 32 ? 3.708 -20.695 18.675 1.00 33.60 ? 32 LYS A CA 1 ATOM 229 C C . LYS A 1 32 ? 4.561 -19.759 17.814 1.00 31.68 ? 32 LYS A C 1 ATOM 230 O O . LYS A 1 32 ? 4.464 -19.796 16.590 1.00 32.22 ? 32 LYS A O 1 ATOM 231 C CB . LYS A 1 32 ? 4.588 -21.779 19.306 1.00 33.88 ? 32 LYS A CB 1 ATOM 232 C CG . LYS A 1 32 ? 3.835 -22.667 20.329 1.00 38.21 ? 32 LYS A CG 1 ATOM 233 C CD . LYS A 1 32 ? 4.501 -24.024 20.362 1.00 46.58 ? 32 LYS A CD 1 ATOM 234 C CE . LYS A 1 32 ? 4.762 -24.501 21.785 1.00 51.91 ? 32 LYS A CE 1 ATOM 235 N NZ . LYS A 1 32 ? 3.508 -24.686 22.588 1.00 55.58 ? 32 LYS A NZ 1 ATOM 236 N N . VAL A 1 33 ? 5.447 -18.996 18.446 1.00 28.91 ? 33 VAL A N 1 ATOM 237 C CA . VAL A 1 33 ? 6.224 -18.022 17.682 1.00 26.23 ? 33 VAL A CA 1 ATOM 238 C C . VAL A 1 33 ? 7.706 -18.289 17.848 1.00 24.93 ? 33 VAL A C 1 ATOM 239 O O . VAL A 1 33 ? 8.191 -18.409 18.968 1.00 23.20 ? 33 VAL A O 1 ATOM 240 C CB . VAL A 1 33 ? 5.769 -16.558 18.005 1.00 26.58 ? 33 VAL A CB 1 ATOM 241 C CG1 . VAL A 1 33 ? 6.710 -15.447 17.377 1.00 24.09 ? 33 VAL A CG1 1 ATOM 242 C CG2 . VAL A 1 33 ? 4.286 -16.361 17.518 1.00 23.58 ? 33 VAL A CG2 1 ATOM 243 N N . HIS A 1 34 ? 8.423 -18.435 16.724 1.00 24.43 ? 34 HIS A N 1 ATOM 244 C CA . HIS A 1 34 ? 9.860 -18.578 16.787 1.00 23.82 ? 34 HIS A CA 1 ATOM 245 C C . HIS A 1 34 ? 10.416 -17.167 16.743 1.00 24.58 ? 34 HIS A C 1 ATOM 246 O O . HIS A 1 34 ? 10.219 -16.415 15.753 1.00 25.35 ? 34 HIS A O 1 ATOM 247 C CB . HIS A 1 34 ? 10.343 -19.406 15.591 1.00 24.81 ? 34 HIS A CB 1 ATOM 248 C CG . HIS A 1 34 ? 11.759 -19.843 15.694 1.00 27.16 ? 34 HIS A CG 1 ATOM 249 N ND1 . HIS A 1 34 ? 12.450 -20.377 14.622 1.00 35.90 ? 34 HIS A ND1 1 ATOM 250 C CD2 . HIS A 1 34 ? 12.615 -19.867 16.741 1.00 29.38 ? 34 HIS A CD2 1 ATOM 251 C CE1 . HIS A 1 34 ? 13.679 -20.689 15.005 1.00 35.23 ? 34 HIS A CE1 1 ATOM 252 N NE2 . HIS A 1 34 ? 13.802 -20.396 16.290 1.00 34.25 ? 34 HIS A NE2 1 ATOM 253 N N . VAL A 1 35 ? 11.135 -16.803 17.797 1.00 23.58 ? 35 VAL A N 1 ATOM 254 C CA . VAL A 1 35 ? 11.855 -15.517 17.925 1.00 21.83 ? 35 VAL A CA 1 ATOM 255 C C . VAL A 1 35 ? 13.338 -15.712 17.672 1.00 22.61 ? 35 VAL A C 1 ATOM 256 O O . VAL A 1 35 ? 13.973 -16.521 18.316 1.00 22.49 ? 35 VAL A O 1 ATOM 257 C CB . VAL A 1 35 ? 11.645 -14.981 19.381 1.00 20.68 ? 35 VAL A CB 1 ATOM 258 C CG1 . VAL A 1 35 ? 12.248 -13.571 19.615 1.00 20.09 ? 35 VAL A CG1 1 ATOM 259 C CG2 . VAL A 1 35 ? 10.130 -14.990 19.747 1.00 16.43 ? 35 VAL A CG2 1 ATOM 260 N N . GLN A 1 36 ? 13.935 -15.019 16.725 1.00 23.27 ? 36 GLN A N 1 ATOM 261 C CA . GLN A 1 36 ? 15.364 -15.189 16.524 1.00 25.34 ? 36 GLN A CA 1 ATOM 262 C C . GLN A 1 36 ? 16.086 -13.894 16.138 1.00 25.34 ? 36 GLN A C 1 ATOM 263 O O . GLN A 1 36 ? 15.489 -12.963 15.632 1.00 24.99 ? 36 GLN A O 1 ATOM 264 C CB . GLN A 1 36 ? 15.659 -16.323 15.510 1.00 27.43 ? 36 GLN A CB 1 ATOM 265 C CG . GLN A 1 36 ? 14.604 -16.564 14.462 1.00 28.76 ? 36 GLN A CG 1 ATOM 266 C CD . GLN A 1 36 ? 14.931 -17.652 13.421 1.00 33.22 ? 36 GLN A CD 1 ATOM 267 O OE1 . GLN A 1 36 ? 15.983 -18.389 13.454 1.00 35.81 ? 36 GLN A OE1 1 ATOM 268 N NE2 . GLN A 1 36 ? 13.998 -17.788 12.497 1.00 37.96 ? 36 GLN A NE2 1 ATOM 269 N N . GLY A 1 37 ? 17.387 -13.836 16.334 1.00 23.95 ? 37 GLY A N 1 ATOM 270 C CA . GLY A 1 37 ? 18.125 -12.697 15.836 1.00 22.21 ? 37 GLY A CA 1 ATOM 271 C C . GLY A 1 37 ? 19.371 -12.576 16.645 1.00 22.10 ? 37 GLY A C 1 ATOM 272 O O . GLY A 1 37 ? 19.804 -13.553 17.299 1.00 20.82 ? 37 GLY A O 1 ATOM 273 N N . GLY A 1 38 ? 19.929 -11.369 16.645 1.00 23.22 ? 38 GLY A N 1 ATOM 274 C CA . GLY A 1 38 ? 21.263 -11.163 17.180 1.00 22.79 ? 38 GLY A CA 1 ATOM 275 C C . GLY A 1 38 ? 21.246 -9.755 17.647 1.00 23.79 ? 38 GLY A C 1 ATOM 276 O O . GLY A 1 38 ? 20.603 -8.932 17.014 1.00 25.03 ? 38 GLY A O 1 ATOM 277 N N . ILE A 1 39 ? 21.925 -9.469 18.759 1.00 22.88 ? 39 ILE A N 1 ATOM 278 C CA . ILE A 1 39 ? 22.054 -8.094 19.269 1.00 22.34 ? 39 ILE A CA 1 ATOM 279 C C . ILE A 1 39 ? 23.514 -7.993 19.627 1.00 22.68 ? 39 ILE A C 1 ATOM 280 O O . ILE A 1 39 ? 24.073 -8.964 20.082 1.00 23.62 ? 39 ILE A O 1 ATOM 281 C CB . ILE A 1 39 ? 21.182 -7.862 20.508 1.00 21.67 ? 39 ILE A CB 1 ATOM 282 C CG1 . ILE A 1 39 ? 19.701 -8.153 20.197 1.00 21.79 ? 39 ILE A CG1 1 ATOM 283 C CG2 . ILE A 1 39 ? 21.305 -6.431 21.061 1.00 20.20 ? 39 ILE A CG2 1 ATOM 284 C CD1 . ILE A 1 39 ? 18.933 -8.184 21.536 1.00 25.98 ? 39 ILE A CD1 1 ATOM 285 N N . THR A 1 40 ? 24.147 -6.864 19.358 1.00 23.07 ? 40 THR A N 1 ATOM 286 C CA . THR A 1 40 ? 25.476 -6.599 19.890 1.00 25.59 ? 40 THR A CA 1 ATOM 287 C C . THR A 1 40 ? 25.483 -5.326 20.736 1.00 23.55 ? 40 THR A C 1 ATOM 288 O O . THR A 1 40 ? 24.675 -4.408 20.552 1.00 23.40 ? 40 THR A O 1 ATOM 289 C CB . THR A 1 40 ? 26.512 -6.438 18.743 1.00 27.88 ? 40 THR A CB 1 ATOM 290 O OG1 . THR A 1 40 ? 26.083 -5.337 17.926 1.00 33.48 ? 40 THR A OG1 1 ATOM 291 C CG2 . THR A 1 40 ? 26.482 -7.667 17.900 1.00 29.85 ? 40 THR A CG2 1 ATOM 292 N N . GLY A 1 41 ? 26.383 -5.276 21.695 1.00 23.27 ? 41 GLY A N 1 ATOM 293 C CA . GLY A 1 41 ? 26.584 -4.050 22.443 1.00 22.27 ? 41 GLY A CA 1 ATOM 294 C C . GLY A 1 41 ? 26.557 -4.162 23.948 1.00 22.38 ? 41 GLY A C 1 ATOM 295 O O . GLY A 1 41 ? 26.720 -3.160 24.610 1.00 22.56 ? 41 GLY A O 1 ATOM 296 N N . LEU A 1 42 ? 26.317 -5.345 24.521 1.00 21.16 ? 42 LEU A N 1 ATOM 297 C CA . LEU A 1 42 ? 26.420 -5.438 25.974 1.00 22.44 ? 42 LEU A CA 1 ATOM 298 C C . LEU A 1 42 ? 27.427 -6.480 26.389 1.00 22.18 ? 42 LEU A C 1 ATOM 299 O O . LEU A 1 42 ? 27.642 -7.449 25.683 1.00 23.92 ? 42 LEU A O 1 ATOM 300 C CB . LEU A 1 42 ? 25.103 -5.781 26.630 1.00 22.00 ? 42 LEU A CB 1 ATOM 301 C CG . LEU A 1 42 ? 24.005 -4.750 26.498 1.00 22.79 ? 42 LEU A CG 1 ATOM 302 C CD1 . LEU A 1 42 ? 22.679 -5.491 26.792 1.00 17.83 ? 42 LEU A CD1 1 ATOM 303 C CD2 . LEU A 1 42 ? 24.272 -3.574 27.348 1.00 19.63 ? 42 LEU A CD2 1 ATOM 304 N N . PRO A 1 43 ? 28.028 -6.288 27.551 1.00 22.89 ? 43 PRO A N 1 ATOM 305 C CA . PRO A 1 43 ? 29.033 -7.248 28.055 1.00 23.23 ? 43 PRO A CA 1 ATOM 306 C C . PRO A 1 43 ? 28.441 -8.643 28.343 1.00 23.16 ? 43 PRO A C 1 ATOM 307 O O . PRO A 1 43 ? 27.237 -8.741 28.507 1.00 24.62 ? 43 PRO A O 1 ATOM 308 C CB . PRO A 1 43 ? 29.521 -6.594 29.373 1.00 22.88 ? 43 PRO A CB 1 ATOM 309 C CG . PRO A 1 43 ? 28.643 -5.499 29.698 1.00 23.76 ? 43 PRO A CG 1 ATOM 310 C CD . PRO A 1 43 ? 27.835 -5.115 28.437 1.00 22.32 ? 43 PRO A CD 1 ATOM 311 N N . PRO A 1 44 ? 29.275 -9.687 28.489 1.00 23.33 ? 44 PRO A N 1 ATOM 312 C CA . PRO A 1 44 ? 28.736 -11.048 28.639 1.00 23.16 ? 44 PRO A CA 1 ATOM 313 C C . PRO A 1 44 ? 27.859 -11.060 29.929 1.00 22.05 ? 44 PRO A C 1 ATOM 314 O O . PRO A 1 44 ? 28.201 -10.428 30.917 1.00 21.92 ? 44 PRO A O 1 ATOM 315 C CB . PRO A 1 44 ? 29.996 -11.909 28.847 1.00 22.33 ? 44 PRO A CB 1 ATOM 316 C CG . PRO A 1 44 ? 31.068 -10.861 29.400 1.00 23.43 ? 44 PRO A CG 1 ATOM 317 C CD . PRO A 1 44 ? 30.753 -9.642 28.586 1.00 24.19 ? 44 PRO A CD 1 ATOM 318 N N . GLY A 1 45 ? 26.719 -11.715 29.884 1.00 22.92 ? 45 GLY A N 1 ATOM 319 C CA . GLY A 1 45 ? 25.757 -11.671 30.982 1.00 19.91 ? 45 GLY A CA 1 ATOM 320 C C . GLY A 1 45 ? 24.357 -11.933 30.471 1.00 21.54 ? 45 GLY A C 1 ATOM 321 O O . GLY A 1 45 ? 24.195 -12.408 29.377 1.00 21.02 ? 45 GLY A O 1 ATOM 322 N N . GLU A 1 46 ? 23.341 -11.682 31.293 1.00 22.73 ? 46 GLU A N 1 ATOM 323 C CA . GLU A 1 46 ? 21.936 -11.900 30.909 1.00 24.83 ? 46 GLU A CA 1 ATOM 324 C C . GLU A 1 46 ? 21.130 -10.662 31.202 1.00 22.59 ? 46 GLU A C 1 ATOM 325 O O . GLU A 1 46 ? 21.408 -9.945 32.180 1.00 22.01 ? 46 GLU A O 1 ATOM 326 C CB . GLU A 1 46 ? 21.315 -13.129 31.618 1.00 24.76 ? 46 GLU A CB 1 ATOM 327 C CG . GLU A 1 46 ? 21.183 -13.098 33.092 1.00 30.66 ? 46 GLU A CG 1 ATOM 328 C CD . GLU A 1 46 ? 20.520 -14.404 33.705 1.00 31.73 ? 46 GLU A CD 1 ATOM 329 O OE1 . GLU A 1 46 ? 20.275 -14.428 34.959 1.00 41.24 ? 46 GLU A OE1 1 ATOM 330 O OE2 . GLU A 1 46 ? 20.219 -15.353 32.939 1.00 35.56 ? 46 GLU A OE2 1 ATOM 331 N N . TYR A 1 47 ? 20.123 -10.400 30.364 1.00 21.49 ? 47 TYR A N 1 ATOM 332 C CA . TYR A 1 47 ? 19.443 -9.099 30.406 1.00 20.04 ? 47 TYR A CA 1 ATOM 333 C C . TYR A 1 47 ? 17.989 -9.324 30.065 1.00 19.73 ? 47 TYR A C 1 ATOM 334 O O . TYR A 1 47 ? 17.693 -10.048 29.087 1.00 20.74 ? 47 TYR A O 1 ATOM 335 C CB . TYR A 1 47 ? 20.068 -8.170 29.363 1.00 20.68 ? 47 TYR A CB 1 ATOM 336 C CG . TYR A 1 47 ? 21.592 -7.951 29.591 1.00 20.16 ? 47 TYR A CG 1 ATOM 337 C CD1 . TYR A 1 47 ? 22.534 -8.813 29.012 1.00 21.28 ? 47 TYR A CD1 1 ATOM 338 C CD2 . TYR A 1 47 ? 22.047 -6.921 30.347 1.00 18.36 ? 47 TYR A CD2 1 ATOM 339 C CE1 . TYR A 1 47 ? 23.911 -8.675 29.190 1.00 17.41 ? 47 TYR A CE1 1 ATOM 340 C CE2 . TYR A 1 47 ? 23.453 -6.753 30.524 1.00 22.24 ? 47 TYR A CE2 1 ATOM 341 C CZ . TYR A 1 47 ? 24.353 -7.645 29.946 1.00 21.88 ? 47 TYR A CZ 1 ATOM 342 O OH . TYR A 1 47 ? 25.721 -7.482 30.116 1.00 25.13 ? 47 TYR A OH 1 ATOM 343 N N . GLY A 1 48 ? 17.102 -8.685 30.832 1.00 17.77 ? 48 GLY A N 1 ATOM 344 C CA . GLY A 1 48 ? 15.665 -8.769 30.604 1.00 17.85 ? 48 GLY A CA 1 ATOM 345 C C . GLY A 1 48 ? 15.291 -8.380 29.215 1.00 18.08 ? 48 GLY A C 1 ATOM 346 O O . GLY A 1 48 ? 15.813 -7.403 28.670 1.00 19.03 ? 48 GLY A O 1 ATOM 347 N N . PHE A 1 49 ? 14.409 -9.158 28.600 1.00 19.82 ? 49 PHE A N 1 ATOM 348 C CA . PHE A 1 49 ? 13.968 -8.830 27.266 1.00 20.11 ? 49 PHE A CA 1 ATOM 349 C C . PHE A 1 49 ? 12.471 -9.103 27.212 1.00 19.30 ? 49 PHE A C 1 ATOM 350 O O . PHE A 1 49 ? 12.056 -10.217 27.423 1.00 19.24 ? 49 PHE A O 1 ATOM 351 C CB . PHE A 1 49 ? 14.684 -9.766 26.343 1.00 22.53 ? 49 PHE A CB 1 ATOM 352 C CG . PHE A 1 49 ? 14.488 -9.457 24.902 1.00 26.01 ? 49 PHE A CG 1 ATOM 353 C CD1 . PHE A 1 49 ? 13.906 -10.388 24.066 1.00 31.23 ? 49 PHE A CD1 1 ATOM 354 C CD2 . PHE A 1 49 ? 14.953 -8.294 24.387 1.00 28.43 ? 49 PHE A CD2 1 ATOM 355 C CE1 . PHE A 1 49 ? 13.747 -10.108 22.736 1.00 34.00 ? 49 PHE A CE1 1 ATOM 356 C CE2 . PHE A 1 49 ? 14.809 -7.999 23.081 1.00 32.98 ? 49 PHE A CE2 1 ATOM 357 C CZ . PHE A 1 49 ? 14.183 -8.908 22.247 1.00 32.62 ? 49 PHE A CZ 1 ATOM 358 N N . HIS A 1 50 ? 11.642 -8.082 26.986 1.00 18.43 ? 50 HIS A N 1 ATOM 359 C CA . HIS A 1 50 ? 10.184 -8.270 27.092 1.00 18.65 ? 50 HIS A CA 1 ATOM 360 C C . HIS A 1 50 ? 9.430 -7.555 25.983 1.00 18.90 ? 50 HIS A C 1 ATOM 361 O O . HIS A 1 50 ? 9.956 -6.600 25.463 1.00 19.38 ? 50 HIS A O 1 ATOM 362 C CB . HIS A 1 50 ? 9.668 -7.691 28.396 1.00 18.19 ? 50 HIS A CB 1 ATOM 363 C CG . HIS A 1 50 ? 10.565 -7.937 29.570 1.00 20.25 ? 50 HIS A CG 1 ATOM 364 N ND1 . HIS A 1 50 ? 11.016 -6.911 30.378 1.00 22.26 ? 50 HIS A ND1 1 ATOM 365 C CD2 . HIS A 1 50 ? 11.084 -9.095 30.076 1.00 20.30 ? 50 HIS A CD2 1 ATOM 366 C CE1 . HIS A 1 50 ? 11.779 -7.430 31.328 1.00 24.07 ? 50 HIS A CE1 1 ATOM 367 N NE2 . HIS A 1 50 ? 11.830 -8.752 31.179 1.00 19.08 ? 50 HIS A NE2 1 ATOM 368 N N . VAL A 1 51 ? 8.180 -7.951 25.709 1.00 18.02 ? 51 VAL A N 1 ATOM 369 C CA . VAL A 1 51 ? 7.271 -7.176 24.869 1.00 16.77 ? 51 VAL A CA 1 ATOM 370 C C . VAL A 1 51 ? 6.501 -6.271 25.808 1.00 19.88 ? 51 VAL A C 1 ATOM 371 O O . VAL A 1 51 ? 5.782 -6.761 26.769 1.00 19.70 ? 51 VAL A O 1 ATOM 372 C CB . VAL A 1 51 ? 6.312 -8.090 24.108 1.00 17.05 ? 51 VAL A CB 1 ATOM 373 C CG1 . VAL A 1 51 ? 5.303 -7.277 23.279 1.00 15.05 ? 51 VAL A CG1 1 ATOM 374 C CG2 . VAL A 1 51 ? 7.131 -9.086 23.175 1.00 13.32 ? 51 VAL A CG2 1 ATOM 375 N N . HIS A 1 52 ? 6.630 -4.970 25.591 1.00 18.84 ? 52 HIS A N 1 ATOM 376 C CA . HIS A 1 52 ? 5.920 -4.028 26.427 1.00 20.16 ? 52 HIS A CA 1 ATOM 377 C C . HIS A 1 52 ? 4.608 -3.643 25.689 1.00 21.22 ? 52 HIS A C 1 ATOM 378 O O . HIS A 1 52 ? 4.423 -3.899 24.493 1.00 19.70 ? 52 HIS A O 1 ATOM 379 C CB . HIS A 1 52 ? 6.831 -2.835 26.785 1.00 18.45 ? 52 HIS A CB 1 ATOM 380 C CG . HIS A 1 52 ? 7.865 -3.136 27.841 1.00 18.03 ? 52 HIS A CG 1 ATOM 381 N ND1 . HIS A 1 52 ? 8.156 -2.262 28.859 1.00 22.44 ? 52 HIS A ND1 1 ATOM 382 C CD2 . HIS A 1 52 ? 8.694 -4.186 28.022 1.00 18.24 ? 52 HIS A CD2 1 ATOM 383 C CE1 . HIS A 1 52 ? 9.123 -2.753 29.608 1.00 21.29 ? 52 HIS A CE1 1 ATOM 384 N NE2 . HIS A 1 52 ? 9.458 -3.938 29.134 1.00 26.89 ? 52 HIS A NE2 1 ATOM 385 N N . GLU A 1 53 ? 3.655 -3.095 26.423 1.00 22.96 ? 53 GLU A N 1 ATOM 386 C CA . GLU A 1 53 ? 2.311 -2.986 25.927 1.00 23.37 ? 53 GLU A CA 1 ATOM 387 C C . GLU A 1 53 ? 2.172 -1.992 24.747 1.00 23.52 ? 53 GLU A C 1 ATOM 388 O O . GLU A 1 53 ? 1.437 -2.250 23.813 1.00 23.47 ? 53 GLU A O 1 ATOM 389 C CB . GLU A 1 53 ? 1.389 -2.569 27.085 1.00 24.96 ? 53 GLU A CB 1 ATOM 390 C CG . GLU A 1 53 ? -0.014 -2.379 26.604 1.00 30.01 ? 53 GLU A CG 1 ATOM 391 C CD . GLU A 1 53 ? -0.955 -1.781 27.659 1.00 37.34 ? 53 GLU A CD 1 ATOM 392 O OE1 . GLU A 1 53 ? -2.198 -1.889 27.454 1.00 39.15 ? 53 GLU A OE1 1 ATOM 393 O OE2 . GLU A 1 53 ? -0.459 -1.214 28.659 1.00 36.83 ? 53 GLU A OE2 1 ATOM 394 N N . LYS A 1 54 ? 2.840 -0.848 24.800 1.00 23.74 ? 54 LYS A N 1 ATOM 395 C CA . LYS A 1 54 ? 2.586 0.162 23.791 1.00 24.56 ? 54 LYS A CA 1 ATOM 396 C C . LYS A 1 54 ? 3.805 0.268 22.841 1.00 24.79 ? 54 LYS A C 1 ATOM 397 O O . LYS A 1 54 ? 4.973 0.146 23.279 1.00 24.55 ? 54 LYS A O 1 ATOM 398 C CB . LYS A 1 54 ? 2.442 1.498 24.487 1.00 24.13 ? 54 LYS A CB 1 ATOM 399 C CG . LYS A 1 54 ? 1.207 1.670 25.426 1.00 26.86 ? 54 LYS A CG 1 ATOM 400 C CD . LYS A 1 54 ? 0.040 0.983 24.841 1.00 29.96 ? 54 LYS A CD 1 ATOM 401 C CE . LYS A 1 54 ? -1.248 1.243 25.659 1.00 39.79 ? 54 LYS A CE 1 ATOM 402 N NZ . LYS A 1 54 ? -2.480 0.842 24.865 1.00 40.06 ? 54 LYS A NZ 1 ATOM 403 N N . GLY A 1 55 ? 3.556 0.563 21.581 1.00 25.67 ? 55 GLY A N 1 ATOM 404 C CA . GLY A 1 55 ? 4.650 0.740 20.574 1.00 25.76 ? 55 GLY A CA 1 ATOM 405 C C . GLY A 1 55 ? 4.856 2.215 20.358 1.00 27.07 ? 55 GLY A C 1 ATOM 406 O O . GLY A 1 55 ? 4.972 2.703 19.238 1.00 26.10 ? 55 GLY A O 1 ATOM 407 N N . ASP A 1 56 ? 4.911 2.912 21.483 1.00 27.81 ? 56 ASP A N 1 ATOM 408 C CA . ASP A 1 56 ? 4.940 4.373 21.553 1.00 28.04 ? 56 ASP A CA 1 ATOM 409 C C . ASP A 1 56 ? 6.331 4.803 22.049 1.00 27.74 ? 56 ASP A C 1 ATOM 410 O O . ASP A 1 56 ? 6.677 4.651 23.238 1.00 27.21 ? 56 ASP A O 1 ATOM 411 C CB . ASP A 1 56 ? 3.888 4.851 22.538 1.00 26.99 ? 56 ASP A CB 1 ATOM 412 C CG . ASP A 1 56 ? 3.929 6.357 22.733 1.00 32.16 ? 56 ASP A CG 1 ATOM 413 O OD1 . ASP A 1 56 ? 4.740 7.062 22.069 1.00 36.50 ? 56 ASP A OD1 1 ATOM 414 O OD2 . ASP A 1 56 ? 3.172 6.862 23.559 1.00 37.36 ? 56 ASP A OD2 1 ATOM 415 N N . LEU A 1 57 ? 7.104 5.338 21.119 1.00 26.76 ? 57 LEU A N 1 ATOM 416 C CA . LEU A 1 57 ? 8.483 5.710 21.349 1.00 28.71 ? 57 LEU A CA 1 ATOM 417 C C . LEU A 1 57 ? 8.655 7.236 21.500 1.00 28.89 ? 57 LEU A C 1 ATOM 418 O O . LEU A 1 57 ? 9.780 7.732 21.445 1.00 29.29 ? 57 LEU A O 1 ATOM 419 C CB . LEU A 1 57 ? 9.357 5.169 20.179 1.00 28.32 ? 57 LEU A CB 1 ATOM 420 C CG . LEU A 1 57 ? 10.036 3.779 20.217 1.00 28.79 ? 57 LEU A CG 1 ATOM 421 C CD1 . LEU A 1 57 ? 9.319 2.704 21.005 1.00 25.07 ? 57 LEU A CD1 1 ATOM 422 C CD2 . LEU A 1 57 ? 10.390 3.311 18.808 1.00 29.22 ? 57 LEU A CD2 1 ATOM 423 N N . SER A 1 58 ? 7.542 7.962 21.667 1.00 29.16 ? 58 SER A N 1 ATOM 424 C CA . SER A 1 58 ? 7.546 9.409 21.772 1.00 29.74 ? 58 SER A CA 1 ATOM 425 C C . SER A 1 58 ? 8.244 9.909 23.016 1.00 29.80 ? 58 SER A C 1 ATOM 426 O O . SER A 1 58 ? 8.822 10.950 23.000 1.00 30.33 ? 58 SER A O 1 ATOM 427 C CB . SER A 1 58 ? 6.136 9.984 21.663 1.00 29.66 ? 58 SER A CB 1 ATOM 428 O OG . SER A 1 58 ? 5.324 9.631 22.773 1.00 31.53 ? 58 SER A OG 1 ATOM 429 N N . GLY A 1 59 ? 8.244 9.141 24.097 1.00 31.15 ? 59 GLY A N 1 ATOM 430 C CA . GLY A 1 59 ? 9.078 9.523 25.242 1.00 30.57 ? 59 GLY A CA 1 ATOM 431 C C . GLY A 1 59 ? 10.217 8.544 25.474 1.00 32.17 ? 59 GLY A C 1 ATOM 432 O O . GLY A 1 59 ? 10.557 8.232 26.639 1.00 32.90 ? 59 GLY A O 1 ATOM 433 N N . GLY A 1 60 ? 10.816 8.057 24.371 1.00 31.51 ? 60 GLY A N 1 ATOM 434 C CA . GLY A 1 60 ? 11.897 7.087 24.423 1.00 30.67 ? 60 GLY A CA 1 ATOM 435 C C . GLY A 1 60 ? 11.331 5.767 24.910 1.00 29.79 ? 60 GLY A C 1 ATOM 436 O O . GLY A 1 60 ? 10.158 5.526 24.724 1.00 29.51 ? 60 GLY A O 1 ATOM 437 N N . CYS A 1 61 ? 12.162 4.925 25.525 1.00 28.67 ? 61 CYS A N 1 ATOM 438 C CA . CYS A 1 61 ? 11.720 3.609 26.065 1.00 30.10 ? 61 CYS A CA 1 ATOM 439 C C . CYS A 1 61 ? 10.639 3.586 27.197 1.00 28.50 ? 61 CYS A C 1 ATOM 440 O O . CYS A 1 61 ? 9.850 2.634 27.269 1.00 28.40 ? 61 CYS A O 1 ATOM 441 C CB . CYS A 1 61 ? 12.908 2.691 26.388 1.00 30.55 ? 61 CYS A CB 1 ATOM 442 S SG . CYS A 1 61 ? 13.914 2.207 24.885 1.00 37.48 ? 61 CYS A SG 1 ATOM 443 N N . LEU A 1 62 ? 10.528 4.642 27.987 1.00 27.51 ? 62 LEU A N 1 ATOM 444 C CA . LEU A 1 62 ? 9.476 4.702 29.024 1.00 29.48 ? 62 LEU A CA 1 ATOM 445 C C . LEU A 1 62 ? 8.034 4.636 28.496 1.00 28.21 ? 62 LEU A C 1 ATOM 446 O O . LEU A 1 62 ? 7.167 4.014 29.120 1.00 29.02 ? 62 LEU A O 1 ATOM 447 C CB . LEU A 1 62 ? 9.642 5.980 29.859 1.00 30.29 ? 62 LEU A CB 1 ATOM 448 C CG . LEU A 1 62 ? 9.499 5.858 31.390 1.00 35.71 ? 62 LEU A CG 1 ATOM 449 C CD1 . LEU A 1 62 ? 8.023 5.720 31.828 1.00 39.96 ? 62 LEU A CD1 1 ATOM 450 C CD2 . LEU A 1 62 ? 10.340 4.676 31.986 1.00 37.79 ? 62 LEU A CD2 1 ATOM 451 N N . SER A 1 63 ? 7.770 5.293 27.368 1.00 26.18 ? 63 SER A N 1 ATOM 452 C CA . SER A 1 63 ? 6.411 5.449 26.850 1.00 26.03 ? 63 SER A CA 1 ATOM 453 C C . SER A 1 63 ? 5.921 4.143 26.239 1.00 26.21 ? 63 SER A C 1 ATOM 454 O O . SER A 1 63 ? 4.729 3.993 25.951 1.00 25.18 ? 63 SER A O 1 ATOM 455 C CB . SER A 1 63 ? 6.335 6.660 25.870 1.00 26.54 ? 63 SER A CB 1 ATOM 456 O OG . SER A 1 63 ? 7.299 6.497 24.794 1.00 30.07 ? 63 SER A OG 1 ATOM 457 N N . THR A 1 64 ? 6.802 3.132 26.145 1.00 24.45 ? 64 THR A N 1 ATOM 458 C CA . THR A 1 64 ? 6.303 1.827 25.775 1.00 25.36 ? 64 THR A CA 1 ATOM 459 C C . THR A 1 64 ? 5.415 1.149 26.820 1.00 26.08 ? 64 THR A C 1 ATOM 460 O O . THR A 1 64 ? 4.751 0.152 26.500 1.00 25.01 ? 64 THR A O 1 ATOM 461 C CB . THR A 1 64 ? 7.428 0.856 25.318 1.00 25.77 ? 64 THR A CB 1 ATOM 462 O OG1 . THR A 1 64 ? 8.168 0.441 26.453 1.00 26.24 ? 64 THR A OG1 1 ATOM 463 C CG2 . THR A 1 64 ? 8.330 1.543 24.279 1.00 24.15 ? 64 THR A CG2 1 ATOM 464 N N . GLY A 1 65 ? 5.385 1.695 28.050 1.00 26.45 ? 65 GLY A N 1 ATOM 465 C CA . GLY A 1 65 ? 4.487 1.210 29.085 1.00 26.13 ? 65 GLY A CA 1 ATOM 466 C C . GLY A 1 65 ? 5.092 0.011 29.825 1.00 26.31 ? 65 GLY A C 1 ATOM 467 O O . GLY A 1 65 ? 6.330 -0.142 29.889 1.00 24.30 ? 65 GLY A O 1 ATOM 468 N N . SER A 1 66 ? 4.226 -0.840 30.378 1.00 24.44 ? 66 SER A N 1 ATOM 469 C CA . SER A 1 66 ? 4.691 -1.981 31.158 1.00 26.35 ? 66 SER A CA 1 ATOM 470 C C . SER A 1 66 ? 4.597 -3.256 30.328 1.00 24.93 ? 66 SER A C 1 ATOM 471 O O . SER A 1 66 ? 4.322 -3.226 29.125 1.00 25.49 ? 66 SER A O 1 ATOM 472 C CB . SER A 1 66 ? 3.894 -2.094 32.480 1.00 27.77 ? 66 SER A CB 1 ATOM 473 O OG . SER A 1 66 ? 2.497 -2.119 32.265 1.00 31.78 ? 66 SER A OG 1 ATOM 474 N N . HIS A 1 67 ? 4.827 -4.395 30.945 1.00 23.76 ? 67 HIS A N 1 ATOM 475 C CA . HIS A 1 67 ? 4.906 -5.614 30.193 1.00 22.98 ? 67 HIS A CA 1 ATOM 476 C C . HIS A 1 67 ? 3.536 -5.882 29.583 1.00 24.16 ? 67 HIS A C 1 ATOM 477 O O . HIS A 1 67 ? 2.506 -5.702 30.260 1.00 24.56 ? 67 HIS A O 1 ATOM 478 C CB . HIS A 1 67 ? 5.432 -6.781 31.075 1.00 23.20 ? 67 HIS A CB 1 ATOM 479 C CG . HIS A 1 67 ? 6.867 -6.627 31.506 1.00 22.62 ? 67 HIS A CG 1 ATOM 480 N ND1 . HIS A 1 67 ? 7.467 -7.480 32.404 1.00 16.77 ? 67 HIS A ND1 1 ATOM 481 C CD2 . HIS A 1 67 ? 7.807 -5.696 31.143 1.00 20.87 ? 67 HIS A CD2 1 ATOM 482 C CE1 . HIS A 1 67 ? 8.737 -7.065 32.556 1.00 24.64 ? 67 HIS A CE1 1 ATOM 483 N NE2 . HIS A 1 67 ? 8.992 -6.022 31.748 1.00 25.56 ? 67 HIS A NE2 1 ATOM 484 N N . PHE A 1 68 ? 3.489 -6.349 28.339 1.00 23.36 ? 68 PHE A N 1 ATOM 485 C CA . PHE A 1 68 ? 2.230 -6.694 27.714 1.00 24.75 ? 68 PHE A CA 1 ATOM 486 C C . PHE A 1 68 ? 1.530 -7.812 28.529 1.00 26.00 ? 68 PHE A C 1 ATOM 487 O O . PHE A 1 68 ? 2.071 -8.902 28.676 1.00 27.63 ? 68 PHE A O 1 ATOM 488 C CB . PHE A 1 68 ? 2.468 -7.112 26.282 1.00 24.33 ? 68 PHE A CB 1 ATOM 489 C CG . PHE A 1 68 ? 1.217 -7.476 25.512 1.00 24.67 ? 68 PHE A CG 1 ATOM 490 C CD1 . PHE A 1 68 ? 0.047 -6.721 25.622 1.00 24.40 ? 68 PHE A CD1 1 ATOM 491 C CD2 . PHE A 1 68 ? 1.220 -8.582 24.671 1.00 23.37 ? 68 PHE A CD2 1 ATOM 492 C CE1 . PHE A 1 68 ? -1.074 -7.056 24.899 1.00 23.99 ? 68 PHE A CE1 1 ATOM 493 C CE2 . PHE A 1 68 ? 0.119 -8.934 23.917 1.00 22.47 ? 68 PHE A CE2 1 ATOM 494 C CZ . PHE A 1 68 ? -1.045 -8.165 24.034 1.00 24.56 ? 68 PHE A CZ 1 ATOM 495 N N . ASN A 1 69 ? 0.319 -7.549 29.032 1.00 26.81 ? 69 ASN A N 1 ATOM 496 C CA . ASN A 1 69 ? -0.319 -8.424 30.042 1.00 28.26 ? 69 ASN A CA 1 ATOM 497 C C . ASN A 1 69 ? -1.876 -8.457 29.869 1.00 29.96 ? 69 ASN A C 1 ATOM 498 O O . ASN A 1 69 ? -2.597 -8.007 30.760 1.00 30.76 ? 69 ASN A O 1 ATOM 499 C CB . ASN A 1 69 ? 0.088 -7.932 31.450 1.00 27.04 ? 69 ASN A CB 1 ATOM 500 C CG . ASN A 1 69 ? -0.414 -8.831 32.643 1.00 26.72 ? 69 ASN A CG 1 ATOM 501 O OD1 . ASN A 1 69 ? -0.510 -8.324 33.747 1.00 26.17 ? 69 ASN A OD1 1 ATOM 502 N ND2 . ASN A 1 69 ? -0.573 -10.119 32.455 1.00 16.78 ? 69 ASN A ND2 1 ATOM 503 N N . PRO A 1 70 ? -2.383 -8.978 28.710 1.00 30.37 ? 70 PRO A N 1 ATOM 504 C CA . PRO A 1 70 ? -3.809 -8.997 28.450 1.00 31.40 ? 70 PRO A CA 1 ATOM 505 C C . PRO A 1 70 ? -4.535 -9.969 29.382 1.00 33.90 ? 70 PRO A C 1 ATOM 506 O O . PRO A 1 70 ? -5.745 -9.846 29.584 1.00 33.42 ? 70 PRO A O 1 ATOM 507 C CB . PRO A 1 70 ? -3.885 -9.531 27.031 1.00 31.92 ? 70 PRO A CB 1 ATOM 508 C CG . PRO A 1 70 ? -2.693 -10.407 26.894 1.00 29.02 ? 70 PRO A CG 1 ATOM 509 C CD . PRO A 1 70 ? -1.628 -9.629 27.615 1.00 30.12 ? 70 PRO A CD 1 ATOM 510 N N . GLU A 1 71 ? -3.820 -10.935 29.959 1.00 34.65 ? 71 GLU A N 1 ATOM 511 C CA . GLU A 1 71 ? -4.514 -11.846 30.861 1.00 35.92 ? 71 GLU A CA 1 ATOM 512 C C . GLU A 1 71 ? -4.453 -11.422 32.337 1.00 36.39 ? 71 GLU A C 1 ATOM 513 O O . GLU A 1 71 ? -5.001 -12.114 33.197 1.00 37.32 ? 71 GLU A O 1 ATOM 514 C CB . GLU A 1 71 ? -4.050 -13.285 30.687 1.00 35.89 ? 71 GLU A CB 1 ATOM 515 C CG . GLU A 1 71 ? -3.946 -13.837 29.233 1.00 39.85 ? 71 GLU A CG 1 ATOM 516 C CD . GLU A 1 71 ? -5.287 -14.113 28.550 1.00 47.15 ? 71 GLU A CD 1 ATOM 517 O OE1 . GLU A 1 71 ? -5.272 -14.293 27.309 1.00 47.09 ? 71 GLU A OE1 1 ATOM 518 O OE2 . GLU A 1 71 ? -6.358 -14.128 29.226 1.00 51.02 ? 71 GLU A OE2 1 ATOM 519 N N . HIS A 1 72 ? -3.799 -10.290 32.626 1.00 35.60 ? 72 HIS A N 1 ATOM 520 C CA . HIS A 1 72 ? -3.652 -9.781 34.011 1.00 35.42 ? 72 HIS A CA 1 ATOM 521 C C . HIS A 1 72 ? -3.022 -10.770 34.944 1.00 34.13 ? 72 HIS A C 1 ATOM 522 O O . HIS A 1 72 ? -3.553 -10.979 36.032 1.00 34.90 ? 72 HIS A O 1 ATOM 523 C CB . HIS A 1 72 ? -5.009 -9.331 34.618 1.00 35.66 ? 72 HIS A CB 1 ATOM 524 C CG . HIS A 1 72 ? -5.835 -8.543 33.661 1.00 37.27 ? 72 HIS A CG 1 ATOM 525 N ND1 . HIS A 1 72 ? -5.759 -7.173 33.573 1.00 37.22 ? 72 HIS A ND1 1 ATOM 526 C CD2 . HIS A 1 72 ? -6.701 -8.939 32.700 1.00 37.05 ? 72 HIS A CD2 1 ATOM 527 C CE1 . HIS A 1 72 ? -6.556 -6.755 32.610 1.00 39.15 ? 72 HIS A CE1 1 ATOM 528 N NE2 . HIS A 1 72 ? -7.134 -7.806 32.060 1.00 39.82 ? 72 HIS A NE2 1 ATOM 529 N N . LYS A 1 73 ? -1.905 -11.370 34.547 1.00 30.57 ? 73 LYS A N 1 ATOM 530 C CA . LYS A 1 73 ? -1.190 -12.239 35.426 1.00 29.82 ? 73 LYS A CA 1 ATOM 531 C C . LYS A 1 73 ? -0.067 -11.459 36.094 1.00 27.62 ? 73 LYS A C 1 ATOM 532 O O . LYS A 1 73 ? 0.015 -10.205 35.960 1.00 26.77 ? 73 LYS A O 1 ATOM 533 C CB . LYS A 1 73 ? -0.678 -13.474 34.699 1.00 30.32 ? 73 LYS A CB 1 ATOM 534 C CG . LYS A 1 73 ? -1.797 -14.308 33.954 1.00 34.21 ? 73 LYS A CG 1 ATOM 535 C CD . LYS A 1 73 ? -1.322 -15.755 33.654 1.00 35.07 ? 73 LYS A CD 1 ATOM 536 C CE . LYS A 1 73 ? -2.385 -16.599 32.931 1.00 41.54 ? 73 LYS A CE 1 ATOM 537 N NZ . LYS A 1 73 ? -3.750 -16.112 33.331 1.00 47.80 ? 73 LYS A NZ 1 ATOM 538 N N . ASP A 1 74 ? 0.754 -12.174 36.862 1.00 26.13 ? 74 ASP A N 1 ATOM 539 C CA . ASP A 1 74 ? 1.923 -11.613 37.476 1.00 27.60 ? 74 ASP A CA 1 ATOM 540 C C . ASP A 1 74 ? 3.118 -11.871 36.535 1.00 26.39 ? 74 ASP A C 1 ATOM 541 O O . ASP A 1 74 ? 3.029 -12.701 35.587 1.00 24.56 ? 74 ASP A O 1 ATOM 542 C CB . ASP A 1 74 ? 2.197 -12.271 38.825 1.00 28.99 ? 74 ASP A CB 1 ATOM 543 C CG . ASP A 1 74 ? 1.042 -12.051 39.861 1.00 31.40 ? 74 ASP A CG 1 ATOM 544 O OD1 . ASP A 1 74 ? 0.633 -10.916 40.128 1.00 32.09 ? 74 ASP A OD1 1 ATOM 545 O OD2 . ASP A 1 74 ? 0.609 -13.032 40.452 1.00 35.90 ? 74 ASP A OD2 1 ATOM 546 N N . HIS A 1 75 ? 4.218 -11.211 36.842 1.00 25.59 ? 75 HIS A N 1 ATOM 547 C CA . HIS A 1 75 ? 5.429 -11.399 36.087 1.00 25.62 ? 75 HIS A CA 1 ATOM 548 C C . HIS A 1 75 ? 5.945 -12.759 36.390 1.00 25.70 ? 75 HIS A C 1 ATOM 549 O O . HIS A 1 75 ? 5.997 -13.141 37.531 1.00 27.56 ? 75 HIS A O 1 ATOM 550 C CB . HIS A 1 75 ? 6.499 -10.335 36.471 1.00 24.43 ? 75 HIS A CB 1 ATOM 551 C CG . HIS A 1 75 ? 7.754 -10.475 35.690 1.00 21.69 ? 75 HIS A CG 1 ATOM 552 N ND1 . HIS A 1 75 ? 7.843 -10.086 34.363 1.00 22.66 ? 75 HIS A ND1 1 ATOM 553 C CD2 . HIS A 1 75 ? 8.969 -10.971 36.030 1.00 21.95 ? 75 HIS A CD2 1 ATOM 554 C CE1 . HIS A 1 75 ? 9.059 -10.371 33.913 1.00 23.57 ? 75 HIS A CE1 1 ATOM 555 N NE2 . HIS A 1 75 ? 9.759 -10.907 34.897 1.00 24.55 ? 75 HIS A NE2 1 ATOM 556 N N . GLY A 1 76 ? 6.412 -13.487 35.387 1.00 25.47 ? 76 GLY A N 1 ATOM 557 C CA . GLY A 1 76 ? 6.987 -14.778 35.672 1.00 24.29 ? 76 GLY A CA 1 ATOM 558 C C . GLY A 1 76 ? 8.104 -15.166 34.728 1.00 23.92 ? 76 GLY A C 1 ATOM 559 O O . GLY A 1 76 ? 8.570 -14.366 33.929 1.00 23.59 ? 76 GLY A O 1 ATOM 560 N N . HIS A 1 77 ? 8.493 -16.420 34.836 1.00 24.14 ? 77 HIS A N 1 ATOM 561 C CA . HIS A 1 77 ? 9.367 -17.101 33.894 1.00 23.90 ? 77 HIS A CA 1 ATOM 562 C C . HIS A 1 77 ? 8.584 -17.486 32.625 1.00 22.90 ? 77 HIS A C 1 ATOM 563 O O . HIS A 1 77 ? 7.405 -17.905 32.710 1.00 21.99 ? 77 HIS A O 1 ATOM 564 C CB . HIS A 1 77 ? 9.996 -18.333 34.552 1.00 22.86 ? 77 HIS A CB 1 ATOM 565 C CG . HIS A 1 77 ? 11.029 -19.039 33.681 1.00 23.88 ? 77 HIS A CG 1 ATOM 566 N ND1 . HIS A 1 77 ? 12.394 -18.966 33.914 1.00 28.36 ? 77 HIS A ND1 1 ATOM 567 C CD2 . HIS A 1 77 ? 10.888 -19.862 32.612 1.00 23.75 ? 77 HIS A CD2 1 ATOM 568 C CE1 . HIS A 1 77 ? 13.044 -19.676 32.999 1.00 22.65 ? 77 HIS A CE1 1 ATOM 569 N NE2 . HIS A 1 77 ? 12.147 -20.221 32.186 1.00 24.80 ? 77 HIS A NE2 1 ATOM 570 N N . PRO A 1 78 ? 9.221 -17.359 31.430 1.00 22.29 ? 78 PRO A N 1 ATOM 571 C CA . PRO A 1 78 ? 8.506 -17.735 30.204 1.00 22.35 ? 78 PRO A CA 1 ATOM 572 C C . PRO A 1 78 ? 7.993 -19.189 30.247 1.00 23.49 ? 78 PRO A C 1 ATOM 573 O O . PRO A 1 78 ? 7.066 -19.514 29.533 1.00 23.53 ? 78 PRO A O 1 ATOM 574 C CB . PRO A 1 78 ? 9.552 -17.610 29.086 1.00 22.46 ? 78 PRO A CB 1 ATOM 575 C CG . PRO A 1 78 ? 10.764 -16.959 29.735 1.00 23.32 ? 78 PRO A CG 1 ATOM 576 C CD . PRO A 1 78 ? 10.566 -16.795 31.179 1.00 23.06 ? 78 PRO A CD 1 ATOM 577 N N . ASN A 1 79 ? 8.605 -20.066 31.025 1.00 24.24 ? 79 ASN A N 1 ATOM 578 C CA . ASN A 1 79 ? 8.041 -21.432 31.181 1.00 27.80 ? 79 ASN A CA 1 ATOM 579 C C . ASN A 1 79 ? 6.867 -21.530 32.175 1.00 27.61 ? 79 ASN A C 1 ATOM 580 O O . ASN A 1 79 ? 6.217 -22.538 32.233 1.00 28.87 ? 79 ASN A O 1 ATOM 581 C CB . ASN A 1 79 ? 9.111 -22.447 31.578 1.00 26.65 ? 79 ASN A CB 1 ATOM 582 C CG . ASN A 1 79 ? 10.092 -22.712 30.481 1.00 32.72 ? 79 ASN A CG 1 ATOM 583 O OD1 . ASN A 1 79 ? 9.768 -22.619 29.298 1.00 41.06 ? 79 ASN A OD1 1 ATOM 584 N ND2 . ASN A 1 79 ? 11.295 -23.097 30.857 1.00 31.89 ? 79 ASN A ND2 1 ATOM 585 N N . ASP A 1 80 ? 6.625 -20.506 32.983 1.00 29.32 ? 80 ASP A N 1 ATOM 586 C CA . ASP A 1 80 ? 5.431 -20.464 33.860 1.00 28.79 ? 80 ASP A CA 1 ATOM 587 C C . ASP A 1 80 ? 4.093 -20.160 33.161 1.00 30.45 ? 80 ASP A C 1 ATOM 588 O O . ASP A 1 80 ? 4.021 -19.348 32.241 1.00 29.98 ? 80 ASP A O 1 ATOM 589 C CB . ASP A 1 80 ? 5.582 -19.363 34.900 1.00 28.64 ? 80 ASP A CB 1 ATOM 590 C CG . ASP A 1 80 ? 6.803 -19.528 35.766 1.00 31.84 ? 80 ASP A CG 1 ATOM 591 O OD1 . ASP A 1 80 ? 7.123 -18.542 36.475 1.00 31.27 ? 80 ASP A OD1 1 ATOM 592 O OD2 . ASP A 1 80 ? 7.427 -20.634 35.741 1.00 34.77 ? 80 ASP A OD2 1 ATOM 593 N N . VAL A 1 81 ? 3.001 -20.687 33.723 1.00 30.29 ? 81 VAL A N 1 ATOM 594 C CA . VAL A 1 81 ? 1.656 -20.246 33.377 1.00 30.08 ? 81 VAL A CA 1 ATOM 595 C C . VAL A 1 81 ? 1.351 -18.871 33.919 1.00 30.10 ? 81 VAL A C 1 ATOM 596 O O . VAL A 1 81 ? 0.715 -18.083 33.212 1.00 31.13 ? 81 VAL A O 1 ATOM 597 C CB . VAL A 1 81 ? 0.580 -21.226 33.963 1.00 32.14 ? 81 VAL A CB 1 ATOM 598 C CG1 . VAL A 1 81 ? -0.827 -20.586 33.907 1.00 30.63 ? 81 VAL A CG1 1 ATOM 599 C CG2 . VAL A 1 81 ? 0.667 -22.593 33.217 1.00 30.51 ? 81 VAL A CG2 1 ATOM 600 N N . ASN A 1 82 ? 1.781 -18.567 35.151 1.00 28.71 ? 82 ASN A N 1 ATOM 601 C CA . ASN A 1 82 ? 1.538 -17.247 35.723 1.00 27.54 ? 82 ASN A CA 1 ATOM 602 C C . ASN A 1 82 ? 2.710 -16.356 35.281 1.00 26.26 ? 82 ASN A C 1 ATOM 603 O O . ASN A 1 82 ? 3.704 -16.215 35.992 1.00 26.45 ? 82 ASN A O 1 ATOM 604 C CB . ASN A 1 82 ? 1.400 -17.293 37.273 1.00 27.62 ? 82 ASN A CB 1 ATOM 605 C CG . ASN A 1 82 ? 1.055 -15.888 37.922 1.00 30.74 ? 82 ASN A CG 1 ATOM 606 O OD1 . ASN A 1 82 ? 1.205 -15.649 39.177 1.00 32.76 ? 82 ASN A OD1 1 ATOM 607 N ND2 . ASN A 1 82 ? 0.583 -14.987 37.100 1.00 27.94 ? 82 ASN A ND2 1 ATOM 608 N N . ARG A 1 83 ? 2.560 -15.721 34.130 1.00 25.01 ? 83 ARG A N 1 ATOM 609 C CA . ARG A 1 83 ? 3.583 -14.869 33.508 1.00 23.78 ? 83 ARG A CA 1 ATOM 610 C C . ARG A 1 83 ? 2.744 -13.897 32.717 1.00 23.76 ? 83 ARG A C 1 ATOM 611 O O . ARG A 1 83 ? 1.556 -14.161 32.383 1.00 24.78 ? 83 ARG A O 1 ATOM 612 C CB . ARG A 1 83 ? 4.498 -15.674 32.520 1.00 24.26 ? 83 ARG A CB 1 ATOM 613 C CG . ARG A 1 83 ? 3.758 -16.514 31.421 1.00 23.04 ? 83 ARG A CG 1 ATOM 614 C CD . ARG A 1 83 ? 4.661 -17.049 30.241 1.00 23.13 ? 83 ARG A CD 1 ATOM 615 N NE . ARG A 1 83 ? 4.941 -15.992 29.260 1.00 23.23 ? 83 ARG A NE 1 ATOM 616 C CZ . ARG A 1 83 ? 5.589 -16.184 28.086 1.00 25.74 ? 83 ARG A CZ 1 ATOM 617 N NH1 . ARG A 1 83 ? 5.733 -15.190 27.219 1.00 23.34 ? 83 ARG A NH1 1 ATOM 618 N NH2 . ARG A 1 83 ? 6.068 -17.366 27.761 1.00 22.64 ? 83 ARG A NH2 1 ATOM 619 N N . HIS A 1 84 ? 3.340 -12.774 32.383 1.00 22.72 ? 84 HIS A N 1 ATOM 620 C CA . HIS A 1 84 ? 2.773 -11.866 31.355 1.00 22.61 ? 84 HIS A CA 1 ATOM 621 C C . HIS A 1 84 ? 2.973 -12.485 29.979 1.00 22.16 ? 84 HIS A C 1 ATOM 622 O O . HIS A 1 84 ? 3.891 -13.209 29.812 1.00 23.20 ? 84 HIS A O 1 ATOM 623 C CB . HIS A 1 84 ? 3.487 -10.524 31.421 1.00 22.38 ? 84 HIS A CB 1 ATOM 624 C CG . HIS A 1 84 ? 3.408 -9.859 32.768 1.00 26.50 ? 84 HIS A CG 1 ATOM 625 N ND1 . HIS A 1 84 ? 4.474 -9.178 33.338 1.00 23.84 ? 84 HIS A ND1 1 ATOM 626 C CD2 . HIS A 1 84 ? 2.371 -9.748 33.647 1.00 25.96 ? 84 HIS A CD2 1 ATOM 627 C CE1 . HIS A 1 84 ? 4.089 -8.657 34.491 1.00 25.54 ? 84 HIS A CE1 1 ATOM 628 N NE2 . HIS A 1 84 ? 2.828 -9.010 34.715 1.00 28.02 ? 84 HIS A NE2 1 ATOM 629 N N . VAL A 1 85 ? 2.145 -12.160 28.976 1.00 22.39 ? 85 VAL A N 1 ATOM 630 C CA . VAL A 1 85 ? 2.363 -12.647 27.619 1.00 21.74 ? 85 VAL A CA 1 ATOM 631 C C . VAL A 1 85 ? 3.738 -12.127 27.117 1.00 21.83 ? 85 VAL A C 1 ATOM 632 O O . VAL A 1 85 ? 4.448 -12.835 26.395 1.00 22.86 ? 85 VAL A O 1 ATOM 633 C CB . VAL A 1 85 ? 1.174 -12.226 26.695 1.00 22.59 ? 85 VAL A CB 1 ATOM 634 C CG1 . VAL A 1 85 ? 1.501 -12.390 25.144 1.00 22.20 ? 85 VAL A CG1 1 ATOM 635 C CG2 . VAL A 1 85 ? -0.039 -13.089 27.041 1.00 19.36 ? 85 VAL A CG2 1 ATOM 636 N N . GLY A 1 86 ? 4.123 -10.920 27.549 1.00 20.99 ? 86 GLY A N 1 ATOM 637 C CA . GLY A 1 86 ? 5.370 -10.323 27.125 1.00 22.34 ? 86 GLY A CA 1 ATOM 638 C C . GLY A 1 86 ? 6.666 -10.769 27.792 1.00 21.40 ? 86 GLY A C 1 ATOM 639 O O . GLY A 1 86 ? 7.717 -10.215 27.491 1.00 19.91 ? 86 GLY A O 1 ATOM 640 N N . ASP A 1 87 ? 6.606 -11.722 28.720 1.00 21.40 ? 87 ASP A N 1 ATOM 641 C CA . ASP A 1 87 ? 7.769 -12.132 29.490 1.00 21.91 ? 87 ASP A CA 1 ATOM 642 C C . ASP A 1 87 ? 8.533 -13.105 28.632 1.00 22.92 ? 87 ASP A C 1 ATOM 643 O O . ASP A 1 87 ? 8.279 -14.297 28.726 1.00 24.56 ? 87 ASP A O 1 ATOM 644 C CB . ASP A 1 87 ? 7.313 -12.867 30.765 1.00 20.28 ? 87 ASP A CB 1 ATOM 645 C CG . ASP A 1 87 ? 6.701 -11.910 31.813 1.00 23.58 ? 87 ASP A CG 1 ATOM 646 O OD1 . ASP A 1 87 ? 6.797 -10.707 31.627 1.00 20.11 ? 87 ASP A OD1 1 ATOM 647 O OD2 . ASP A 1 87 ? 6.137 -12.357 32.816 1.00 22.48 ? 87 ASP A OD2 1 ATOM 648 N N . LEU A 1 88 ? 9.441 -12.650 27.792 1.00 23.25 ? 88 LEU A N 1 ATOM 649 C CA . LEU A 1 88 ? 10.224 -13.594 26.953 1.00 24.07 ? 88 LEU A CA 1 ATOM 650 C C . LEU A 1 88 ? 11.421 -14.068 27.710 1.00 25.09 ? 88 LEU A C 1 ATOM 651 O O . LEU A 1 88 ? 12.107 -14.952 27.225 1.00 28.70 ? 88 LEU A O 1 ATOM 652 C CB . LEU A 1 88 ? 10.696 -12.985 25.618 1.00 22.64 ? 88 LEU A CB 1 ATOM 653 C CG . LEU A 1 88 ? 9.563 -12.482 24.704 1.00 26.35 ? 88 LEU A CG 1 ATOM 654 C CD1 . LEU A 1 88 ? 10.076 -11.484 23.641 1.00 28.77 ? 88 LEU A CD1 1 ATOM 655 C CD2 . LEU A 1 88 ? 8.798 -13.637 24.045 1.00 29.72 ? 88 LEU A CD2 1 ATOM 656 N N . GLY A 1 89 ? 11.730 -13.490 28.866 1.00 23.41 ? 89 GLY A N 1 ATOM 657 C CA . GLY A 1 89 ? 12.876 -13.981 29.613 1.00 22.06 ? 89 GLY A CA 1 ATOM 658 C C . GLY A 1 89 ? 14.103 -13.057 29.551 1.00 22.00 ? 89 GLY A C 1 ATOM 659 O O . GLY A 1 89 ? 13.933 -11.844 29.589 1.00 22.42 ? 89 GLY A O 1 ATOM 660 N N . ASN A 1 90 ? 15.296 -13.635 29.541 1.00 19.19 ? 90 ASN A N 1 ATOM 661 C CA . ASN A 1 90 ? 16.560 -12.894 29.466 1.00 21.05 ? 90 ASN A CA 1 ATOM 662 C C . ASN A 1 90 ? 17.227 -13.310 28.204 1.00 22.06 ? 90 ASN A C 1 ATOM 663 O O . ASN A 1 90 ? 17.053 -14.477 27.795 1.00 23.61 ? 90 ASN A O 1 ATOM 664 C CB . ASN A 1 90 ? 17.502 -13.326 30.620 1.00 18.84 ? 90 ASN A CB 1 ATOM 665 C CG . ASN A 1 90 ? 17.055 -12.784 31.986 1.00 18.66 ? 90 ASN A CG 1 ATOM 666 O OD1 . ASN A 1 90 ? 16.829 -13.540 32.940 1.00 22.11 ? 90 ASN A OD1 1 ATOM 667 N ND2 . ASN A 1 90 ? 16.976 -11.497 32.092 1.00 10.15 ? 90 ASN A ND2 1 ATOM 668 N N . VAL A 1 91 ? 18.017 -12.418 27.601 1.00 22.34 ? 91 VAL A N 1 ATOM 669 C CA . VAL A 1 91 ? 18.888 -12.801 26.491 1.00 22.46 ? 91 VAL A CA 1 ATOM 670 C C . VAL A 1 91 ? 20.322 -12.822 26.989 1.00 21.89 ? 91 VAL A C 1 ATOM 671 O O . VAL A 1 91 ? 20.684 -12.025 27.826 1.00 21.02 ? 91 VAL A O 1 ATOM 672 C CB . VAL A 1 91 ? 18.774 -11.862 25.230 1.00 21.98 ? 91 VAL A CB 1 ATOM 673 C CG1 . VAL A 1 91 ? 17.384 -11.927 24.686 1.00 26.61 ? 91 VAL A CG1 1 ATOM 674 C CG2 . VAL A 1 91 ? 19.062 -10.450 25.545 1.00 21.85 ? 91 VAL A CG2 1 ATOM 675 N N . VAL A 1 92 ? 21.133 -13.731 26.451 1.00 21.67 ? 92 VAL A N 1 ATOM 676 C CA . VAL A 1 92 ? 22.496 -13.888 26.914 1.00 21.36 ? 92 VAL A CA 1 ATOM 677 C C . VAL A 1 92 ? 23.523 -13.335 25.948 1.00 22.72 ? 92 VAL A C 1 ATOM 678 O O . VAL A 1 92 ? 23.457 -13.654 24.765 1.00 24.23 ? 92 VAL A O 1 ATOM 679 C CB . VAL A 1 92 ? 22.786 -15.366 27.099 1.00 22.66 ? 92 VAL A CB 1 ATOM 680 C CG1 . VAL A 1 92 ? 24.271 -15.539 27.490 1.00 21.91 ? 92 VAL A CG1 1 ATOM 681 C CG2 . VAL A 1 92 ? 21.742 -15.994 28.153 1.00 20.48 ? 92 VAL A CG2 1 ATOM 682 N N . PHE A 1 93 ? 24.442 -12.502 26.443 1.00 21.83 ? 93 PHE A N 1 ATOM 683 C CA . PHE A 1 93 ? 25.549 -11.973 25.642 1.00 22.48 ? 93 PHE A CA 1 ATOM 684 C C . PHE A 1 93 ? 26.821 -12.777 25.877 1.00 24.55 ? 93 PHE A C 1 ATOM 685 O O . PHE A 1 93 ? 27.052 -13.245 26.988 1.00 23.72 ? 93 PHE A O 1 ATOM 686 C CB . PHE A 1 93 ? 25.794 -10.488 25.959 1.00 20.66 ? 93 PHE A CB 1 ATOM 687 C CG . PHE A 1 93 ? 24.777 -9.607 25.344 1.00 21.46 ? 93 PHE A CG 1 ATOM 688 C CD1 . PHE A 1 93 ? 25.067 -8.903 24.189 1.00 21.16 ? 93 PHE A CD1 1 ATOM 689 C CD2 . PHE A 1 93 ? 23.470 -9.541 25.889 1.00 19.24 ? 93 PHE A CD2 1 ATOM 690 C CE1 . PHE A 1 93 ? 24.117 -8.142 23.587 1.00 20.19 ? 93 PHE A CE1 1 ATOM 691 C CE2 . PHE A 1 93 ? 22.513 -8.725 25.321 1.00 20.90 ? 93 PHE A CE2 1 ATOM 692 C CZ . PHE A 1 93 ? 22.841 -8.016 24.161 1.00 20.49 ? 93 PHE A CZ 1 ATOM 693 N N . ASP A 1 94 ? 27.631 -12.949 24.812 1.00 27.58 ? 94 ASP A N 1 ATOM 694 C CA . ASP A 1 94 ? 28.876 -13.699 24.946 1.00 28.88 ? 94 ASP A CA 1 ATOM 695 C C . ASP A 1 94 ? 29.999 -12.741 25.222 1.00 30.38 ? 94 ASP A C 1 ATOM 696 O O . ASP A 1 94 ? 29.793 -11.526 25.283 1.00 29.25 ? 94 ASP A O 1 ATOM 697 C CB . ASP A 1 94 ? 29.180 -14.601 23.720 1.00 28.68 ? 94 ASP A CB 1 ATOM 698 C CG . ASP A 1 94 ? 29.424 -13.813 22.447 1.00 29.33 ? 94 ASP A CG 1 ATOM 699 O OD1 . ASP A 1 94 ? 29.192 -14.353 21.366 1.00 28.04 ? 94 ASP A OD1 1 ATOM 700 O OD2 . ASP A 1 94 ? 29.766 -12.618 22.523 1.00 31.76 ? 94 ASP A OD2 1 ATOM 701 N N . GLU A 1 95 ? 31.207 -13.294 25.371 1.00 33.47 ? 95 GLU A N 1 ATOM 702 C CA . GLU A 1 95 ? 32.422 -12.519 25.656 1.00 35.36 ? 95 GLU A CA 1 ATOM 703 C C . GLU A 1 95 ? 32.696 -11.482 24.583 1.00 35.03 ? 95 GLU A C 1 ATOM 704 O O . GLU A 1 95 ? 33.318 -10.459 24.850 1.00 36.74 ? 95 GLU A O 1 ATOM 705 C CB . GLU A 1 95 ? 33.598 -13.487 25.781 1.00 36.93 ? 95 GLU A CB 1 ATOM 706 C CG . GLU A 1 95 ? 33.498 -14.355 27.021 1.00 43.33 ? 95 GLU A CG 1 ATOM 707 C CD . GLU A 1 95 ? 34.558 -14.016 28.068 1.00 54.23 ? 95 GLU A CD 1 ATOM 708 O OE1 . GLU A 1 95 ? 34.465 -12.932 28.714 1.00 57.65 ? 95 GLU A OE1 1 ATOM 709 O OE2 . GLU A 1 95 ? 35.494 -14.851 28.241 1.00 57.59 ? 95 GLU A OE2 1 ATOM 710 N N . ASN A 1 96 ? 32.185 -11.735 23.380 1.00 34.92 ? 96 ASN A N 1 ATOM 711 C CA . ASN A 1 96 ? 32.270 -10.791 22.255 1.00 34.59 ? 96 ASN A CA 1 ATOM 712 C C . ASN A 1 96 ? 31.156 -9.749 22.230 1.00 33.14 ? 96 ASN A C 1 ATOM 713 O O . ASN A 1 96 ? 30.963 -9.111 21.192 1.00 32.20 ? 96 ASN A O 1 ATOM 714 C CB . ASN A 1 96 ? 32.237 -11.545 20.909 1.00 35.21 ? 96 ASN A CB 1 ATOM 715 C CG . ASN A 1 96 ? 33.346 -12.604 20.787 1.00 42.09 ? 96 ASN A CG 1 ATOM 716 O OD1 . ASN A 1 96 ? 33.259 -13.708 21.357 1.00 48.06 ? 96 ASN A OD1 1 ATOM 717 N ND2 . ASN A 1 96 ? 34.376 -12.279 20.021 1.00 44.16 ? 96 ASN A ND2 1 ATOM 718 N N . HIS A 1 97 ? 30.411 -9.572 23.336 1.00 30.82 ? 97 HIS A N 1 ATOM 719 C CA . HIS A 1 97 ? 29.304 -8.597 23.360 1.00 29.66 ? 97 HIS A CA 1 ATOM 720 C C . HIS A 1 97 ? 28.245 -8.839 22.281 1.00 28.49 ? 97 HIS A C 1 ATOM 721 O O . HIS A 1 97 ? 27.628 -7.905 21.764 1.00 28.37 ? 97 HIS A O 1 ATOM 722 C CB . HIS A 1 97 ? 29.844 -7.180 23.264 1.00 30.49 ? 97 HIS A CB 1 ATOM 723 C CG . HIS A 1 97 ? 30.711 -6.793 24.421 1.00 31.83 ? 97 HIS A CG 1 ATOM 724 N ND1 . HIS A 1 97 ? 31.698 -7.617 24.914 1.00 34.70 ? 97 HIS A ND1 1 ATOM 725 C CD2 . HIS A 1 97 ? 30.734 -5.683 25.191 1.00 33.36 ? 97 HIS A CD2 1 ATOM 726 C CE1 . HIS A 1 97 ? 32.290 -7.034 25.943 1.00 31.47 ? 97 HIS A CE1 1 ATOM 727 N NE2 . HIS A 1 97 ? 31.717 -5.866 26.141 1.00 32.03 ? 97 HIS A NE2 1 ATOM 728 N N . TYR A 1 98 ? 28.044 -10.103 21.955 1.00 27.24 ? 98 TYR A N 1 ATOM 729 C CA . TYR A 1 98 ? 27.067 -10.524 20.995 1.00 27.62 ? 98 TYR A CA 1 ATOM 730 C C . TYR A 1 98 ? 26.041 -11.509 21.623 1.00 27.65 ? 98 TYR A C 1 ATOM 731 O O . TYR A 1 98 ? 26.428 -12.415 22.354 1.00 28.04 ? 98 TYR A O 1 ATOM 732 C CB . TYR A 1 98 ? 27.758 -11.188 19.819 1.00 29.32 ? 98 TYR A CB 1 ATOM 733 C CG . TYR A 1 98 ? 26.820 -11.938 18.935 1.00 31.16 ? 98 TYR A CG 1 ATOM 734 C CD1 . TYR A 1 98 ? 26.037 -11.277 18.001 1.00 32.35 ? 98 TYR A CD1 1 ATOM 735 C CD2 . TYR A 1 98 ? 26.705 -13.330 19.036 1.00 34.54 ? 98 TYR A CD2 1 ATOM 736 C CE1 . TYR A 1 98 ? 25.146 -12.015 17.173 1.00 37.61 ? 98 TYR A CE1 1 ATOM 737 C CE2 . TYR A 1 98 ? 25.821 -14.054 18.220 1.00 34.68 ? 98 TYR A CE2 1 ATOM 738 C CZ . TYR A 1 98 ? 25.060 -13.383 17.295 1.00 33.88 ? 98 TYR A CZ 1 ATOM 739 O OH . TYR A 1 98 ? 24.192 -14.102 16.491 1.00 37.50 ? 98 TYR A OH 1 ATOM 740 N N . SER A 1 99 ? 24.752 -11.333 21.313 1.00 25.77 ? 99 SER A N 1 ATOM 741 C CA . SER A 1 99 ? 23.717 -12.189 21.829 1.00 25.85 ? 99 SER A CA 1 ATOM 742 C C . SER A 1 99 ? 22.987 -12.795 20.631 1.00 26.97 ? 99 SER A C 1 ATOM 743 O O . SER A 1 99 ? 22.449 -12.060 19.797 1.00 26.32 ? 99 SER A O 1 ATOM 744 C CB . SER A 1 99 ? 22.686 -11.417 22.602 1.00 24.21 ? 99 SER A CB 1 ATOM 745 O OG . SER A 1 99 ? 21.641 -12.330 22.940 1.00 23.24 ? 99 SER A OG 1 ATOM 746 N N . ARG A 1 100 ? 22.936 -14.119 20.614 1.00 27.74 ? 100 ARG A N 1 ATOM 747 C CA . ARG A 1 100 ? 22.191 -14.915 19.675 1.00 30.86 ? 100 ARG A CA 1 ATOM 748 C C . ARG A 1 100 ? 20.862 -15.209 20.350 1.00 30.15 ? 100 ARG A C 1 ATOM 749 O O . ARG A 1 100 ? 20.836 -15.821 21.396 1.00 31.43 ? 100 ARG A O 1 ATOM 750 C CB . ARG A 1 100 ? 22.944 -16.256 19.446 1.00 32.61 ? 100 ARG A CB 1 ATOM 751 C CG . ARG A 1 100 ? 22.777 -16.887 18.051 1.00 35.84 ? 100 ARG A CG 1 ATOM 752 C CD . ARG A 1 100 ? 21.387 -17.338 17.683 1.00 43.28 ? 100 ARG A CD 1 ATOM 753 N NE . ARG A 1 100 ? 20.934 -16.635 16.465 1.00 48.37 ? 100 ARG A NE 1 ATOM 754 C CZ . ARG A 1 100 ? 19.876 -16.941 15.694 1.00 49.86 ? 100 ARG A CZ 1 ATOM 755 N NH1 . ARG A 1 100 ? 19.589 -16.163 14.656 1.00 49.34 ? 100 ARG A NH1 1 ATOM 756 N NH2 . ARG A 1 100 ? 19.099 -17.982 15.941 1.00 49.87 ? 100 ARG A NH2 1 ATOM 757 N N . ILE A 1 101 ? 19.766 -14.717 19.795 1.00 29.88 ? 101 ILE A N 1 ATOM 758 C CA . ILE A 1 101 ? 18.449 -15.079 20.286 1.00 30.55 ? 101 ILE A CA 1 ATOM 759 C C . ILE A 1 101 ? 17.817 -16.219 19.453 1.00 30.22 ? 101 ILE A C 1 ATOM 760 O O . ILE A 1 101 ? 17.762 -16.163 18.213 1.00 28.90 ? 101 ILE A O 1 ATOM 761 C CB . ILE A 1 101 ? 17.521 -13.846 20.257 1.00 31.56 ? 101 ILE A CB 1 ATOM 762 C CG1 . ILE A 1 101 ? 18.110 -12.712 21.106 1.00 31.59 ? 101 ILE A CG1 1 ATOM 763 C CG2 . ILE A 1 101 ? 16.093 -14.209 20.717 1.00 29.14 ? 101 ILE A CG2 1 ATOM 764 C CD1 . ILE A 1 101 ? 17.442 -11.383 20.726 1.00 36.73 ? 101 ILE A CD1 1 ATOM 765 N N . ASP A 1 102 ? 17.332 -17.254 20.119 1.00 30.28 ? 102 ASP A N 1 ATOM 766 C CA . ASP A 1 102 ? 16.718 -18.343 19.407 1.00 31.01 ? 102 ASP A CA 1 ATOM 767 C C . ASP A 1 102 ? 15.806 -19.114 20.321 1.00 31.17 ? 102 ASP A C 1 ATOM 768 O O . ASP A 1 102 ? 16.228 -20.006 21.077 1.00 30.58 ? 102 ASP A O 1 ATOM 769 C CB . ASP A 1 102 ? 17.783 -19.251 18.816 1.00 33.03 ? 102 ASP A CB 1 ATOM 770 C CG . ASP A 1 102 ? 17.187 -20.360 17.924 1.00 37.96 ? 102 ASP A CG 1 ATOM 771 O OD1 . ASP A 1 102 ? 17.963 -21.172 17.334 1.00 43.19 ? 102 ASP A OD1 1 ATOM 772 O OD2 . ASP A 1 102 ? 15.941 -20.424 17.805 1.00 41.92 ? 102 ASP A OD2 1 ATOM 773 N N . LEU A 1 103 ? 14.524 -18.798 20.252 1.00 29.96 ? 103 LEU A N 1 ATOM 774 C CA . LEU A 1 103 ? 13.603 -19.400 21.196 1.00 28.87 ? 103 LEU A CA 1 ATOM 775 C C . LEU A 1 103 ? 12.241 -19.496 20.592 1.00 28.17 ? 103 LEU A C 1 ATOM 776 O O . LEU A 1 103 ? 11.908 -18.790 19.623 1.00 26.01 ? 103 LEU A O 1 ATOM 777 C CB . LEU A 1 103 ? 13.542 -18.623 22.500 1.00 27.52 ? 103 LEU A CB 1 ATOM 778 C CG . LEU A 1 103 ? 12.965 -17.200 22.390 1.00 31.00 ? 103 LEU A CG 1 ATOM 779 C CD1 . LEU A 1 103 ? 11.425 -17.039 22.420 1.00 27.12 ? 103 LEU A CD1 1 ATOM 780 C CD2 . LEU A 1 103 ? 13.549 -16.325 23.490 1.00 34.17 ? 103 LEU A CD2 1 ATOM 781 N N . VAL A 1 104 ? 11.470 -20.409 21.147 1.00 26.12 ? 104 VAL A N 1 ATOM 782 C CA . VAL A 1 104 ? 10.113 -20.571 20.738 1.00 28.81 ? 104 VAL A CA 1 ATOM 783 C C . VAL A 1 104 ? 9.264 -20.166 21.938 1.00 28.95 ? 104 VAL A C 1 ATOM 784 O O . VAL A 1 104 ? 9.557 -20.592 23.037 1.00 28.28 ? 104 VAL A O 1 ATOM 785 C CB . VAL A 1 104 ? 9.856 -22.011 20.337 1.00 28.07 ? 104 VAL A CB 1 ATOM 786 C CG1 . VAL A 1 104 ? 8.385 -22.237 20.089 1.00 29.30 ? 104 VAL A CG1 1 ATOM 787 C CG2 . VAL A 1 104 ? 10.713 -22.330 19.054 1.00 33.14 ? 104 VAL A CG2 1 ATOM 788 N N . ASP A 1 105 ? 8.240 -19.338 21.727 1.00 30.02 ? 105 ASP A N 1 ATOM 789 C CA . ASP A 1 105 ? 7.381 -18.886 22.810 1.00 31.70 ? 105 ASP A CA 1 ATOM 790 C C . ASP A 1 105 ? 5.922 -19.293 22.535 1.00 32.09 ? 105 ASP A C 1 ATOM 791 O O . ASP A 1 105 ? 5.410 -19.131 21.438 1.00 31.52 ? 105 ASP A O 1 ATOM 792 C CB . ASP A 1 105 ? 7.470 -17.378 22.983 1.00 31.34 ? 105 ASP A CB 1 ATOM 793 C CG . ASP A 1 105 ? 6.833 -16.892 24.311 1.00 36.13 ? 105 ASP A CG 1 ATOM 794 O OD1 . ASP A 1 105 ? 5.642 -16.498 24.304 1.00 37.86 ? 105 ASP A OD1 1 ATOM 795 O OD2 . ASP A 1 105 ? 7.515 -16.915 25.386 1.00 39.00 ? 105 ASP A OD2 1 ATOM 796 N N . ASP A 1 106 ? 5.237 -19.810 23.545 1.00 34.56 ? 106 ASP A N 1 ATOM 797 C CA . ASP A 1 106 ? 3.832 -20.251 23.345 1.00 36.19 ? 106 ASP A CA 1 ATOM 798 C C . ASP A 1 106 ? 2.792 -19.284 23.901 1.00 35.09 ? 106 ASP A C 1 ATOM 799 O O . ASP A 1 106 ? 1.625 -19.638 23.928 1.00 36.82 ? 106 ASP A O 1 ATOM 800 C CB . ASP A 1 106 ? 3.595 -21.650 23.949 1.00 38.40 ? 106 ASP A CB 1 ATOM 801 C CG . ASP A 1 106 ? 4.045 -21.739 25.418 1.00 42.92 ? 106 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 106 ? 4.592 -20.725 25.933 1.00 47.08 ? 106 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 106 ? 3.841 -22.806 26.061 1.00 51.85 ? 106 ASP A OD2 1 ATOM 804 N N . GLN A 1 107 ? 3.171 -18.076 24.319 1.00 33.25 ? 107 GLN A N 1 ATOM 805 C CA . GLN A 1 107 ? 2.160 -17.098 24.745 1.00 31.44 ? 107 GLN A CA 1 ATOM 806 C C . GLN A 1 107 ? 1.902 -15.972 23.706 1.00 29.51 ? 107 GLN A C 1 ATOM 807 O O . GLN A 1 107 ? 0.751 -15.611 23.443 1.00 28.81 ? 107 GLN A O 1 ATOM 808 C CB . GLN A 1 107 ? 2.597 -16.475 26.088 1.00 32.75 ? 107 GLN A CB 1 ATOM 809 C CG . GLN A 1 107 ? 1.631 -16.585 27.225 1.00 40.01 ? 107 GLN A CG 1 ATOM 810 C CD . GLN A 1 107 ? 1.271 -18.006 27.421 1.00 48.58 ? 107 GLN A CD 1 ATOM 811 O OE1 . GLN A 1 107 ? 2.142 -18.839 27.621 1.00 53.50 ? 107 GLN A OE1 1 ATOM 812 N NE2 . GLN A 1 107 ? -0.002 -18.322 27.271 1.00 51.76 ? 107 GLN A NE2 1 ATOM 813 N N . ILE A 1 108 ? 2.969 -15.393 23.150 1.00 25.60 ? 108 ILE A N 1 ATOM 814 C CA . ILE A 1 108 ? 2.832 -14.365 22.146 1.00 23.33 ? 108 ILE A CA 1 ATOM 815 C C . ILE A 1 108 ? 2.225 -14.919 20.835 1.00 24.19 ? 108 ILE A C 1 ATOM 816 O O . ILE A 1 108 ? 2.388 -16.091 20.506 1.00 24.62 ? 108 ILE A O 1 ATOM 817 C CB . ILE A 1 108 ? 4.200 -13.659 21.843 1.00 22.62 ? 108 ILE A CB 1 ATOM 818 C CG1 . ILE A 1 108 ? 5.266 -14.651 21.362 1.00 21.18 ? 108 ILE A CG1 1 ATOM 819 C CG2 . ILE A 1 108 ? 4.738 -12.872 23.111 1.00 20.91 ? 108 ILE A CG2 1 ATOM 820 C CD1 . ILE A 1 108 ? 6.629 -13.983 20.850 1.00 20.99 ? 108 ILE A CD1 1 ATOM 821 N N . SER A 1 109 ? 1.623 -14.042 20.068 1.00 24.09 ? 109 SER A N 1 ATOM 822 C CA . SER A 1 109 ? 1.092 -14.388 18.788 1.00 26.65 ? 109 SER A CA 1 ATOM 823 C C . SER A 1 109 ? 1.270 -13.146 17.870 1.00 27.75 ? 109 SER A C 1 ATOM 824 O O . SER A 1 109 ? 1.520 -12.004 18.321 1.00 25.61 ? 109 SER A O 1 ATOM 825 C CB . SER A 1 109 ? -0.404 -14.703 18.919 1.00 27.83 ? 109 SER A CB 1 ATOM 826 O OG . SER A 1 109 ? -0.946 -15.207 17.699 1.00 32.19 ? 109 SER A OG 1 ATOM 827 N N . LEU A 1 110 ? 1.108 -13.393 16.584 1.00 29.10 ? 110 LEU A N 1 ATOM 828 C CA . LEU A 1 110 ? 1.186 -12.373 15.567 1.00 31.32 ? 110 LEU A CA 1 ATOM 829 C C . LEU A 1 110 ? -0.176 -11.721 15.317 1.00 33.57 ? 110 LEU A C 1 ATOM 830 O O . LEU A 1 110 ? -0.250 -10.645 14.736 1.00 34.31 ? 110 LEU A O 1 ATOM 831 C CB . LEU A 1 110 ? 1.782 -12.971 14.304 1.00 30.48 ? 110 LEU A CB 1 ATOM 832 C CG . LEU A 1 110 ? 3.284 -13.325 14.435 1.00 29.44 ? 110 LEU A CG 1 ATOM 833 C CD1 . LEU A 1 110 ? 3.805 -13.371 13.036 1.00 29.11 ? 110 LEU A CD1 1 ATOM 834 C CD2 . LEU A 1 110 ? 4.119 -12.386 15.273 1.00 27.79 ? 110 LEU A CD2 1 ATOM 835 N N . SER A 1 111 ? -1.243 -12.337 15.829 1.00 34.26 ? 111 SER A N 1 ATOM 836 C CA . SER A 1 111 ? -2.594 -11.750 15.774 1.00 35.02 ? 111 SER A CA 1 ATOM 837 C C . SER A 1 111 ? -3.435 -12.196 16.985 1.00 35.10 ? 111 SER A C 1 ATOM 838 O O . SER A 1 111 ? -2.960 -12.934 17.843 1.00 34.72 ? 111 SER A O 1 ATOM 839 C CB . SER A 1 111 ? -3.305 -12.109 14.451 1.00 35.09 ? 111 SER A CB 1 ATOM 840 O OG . SER A 1 111 ? -3.498 -13.508 14.340 1.00 36.17 ? 111 SER A OG 1 ATOM 841 N N . GLY A 1 112 ? -4.661 -11.707 17.079 1.00 35.53 ? 112 GLY A N 1 ATOM 842 C CA . GLY A 1 112 ? -5.542 -12.091 18.191 1.00 35.63 ? 112 GLY A CA 1 ATOM 843 C C . GLY A 1 112 ? -5.265 -11.244 19.407 1.00 35.63 ? 112 GLY A C 1 ATOM 844 O O . GLY A 1 112 ? -4.530 -10.245 19.334 1.00 36.80 ? 112 GLY A O 1 ATOM 845 N N . PRO A 1 113 ? -5.846 -11.619 20.547 1.00 35.40 ? 113 PRO A N 1 ATOM 846 C CA . PRO A 1 113 ? -5.593 -10.756 21.689 1.00 34.28 ? 113 PRO A CA 1 ATOM 847 C C . PRO A 1 113 ? -4.178 -10.916 22.307 1.00 32.04 ? 113 PRO A C 1 ATOM 848 O O . PRO A 1 113 ? -3.814 -10.069 23.076 1.00 33.09 ? 113 PRO A O 1 ATOM 849 C CB . PRO A 1 113 ? -6.688 -11.158 22.698 1.00 35.50 ? 113 PRO A CB 1 ATOM 850 C CG . PRO A 1 113 ? -6.981 -12.590 22.366 1.00 35.88 ? 113 PRO A CG 1 ATOM 851 C CD . PRO A 1 113 ? -6.752 -12.740 20.863 1.00 35.96 ? 113 PRO A CD 1 ATOM 852 N N . HIS A 1 114 ? -3.396 -11.941 21.972 1.00 29.38 ? 114 HIS A N 1 ATOM 853 C CA . HIS A 1 114 ? -1.988 -11.974 22.379 1.00 27.05 ? 114 HIS A CA 1 ATOM 854 C C . HIS A 1 114 ? -1.068 -11.417 21.293 1.00 26.84 ? 114 HIS A C 1 ATOM 855 O O . HIS A 1 114 ? 0.161 -11.665 21.300 1.00 26.91 ? 114 HIS A O 1 ATOM 856 C CB . HIS A 1 114 ? -1.576 -13.391 22.666 1.00 27.53 ? 114 HIS A CB 1 ATOM 857 C CG . HIS A 1 114 ? -2.181 -13.964 23.898 1.00 29.99 ? 114 HIS A CG 1 ATOM 858 N ND1 . HIS A 1 114 ? -1.732 -15.144 24.459 1.00 34.40 ? 114 HIS A ND1 1 ATOM 859 C CD2 . HIS A 1 114 ? -3.195 -13.523 24.691 1.00 31.75 ? 114 HIS A CD2 1 ATOM 860 C CE1 . HIS A 1 114 ? -2.444 -15.406 25.548 1.00 35.89 ? 114 HIS A CE1 1 ATOM 861 N NE2 . HIS A 1 114 ? -3.336 -14.437 25.709 1.00 34.36 ? 114 HIS A NE2 1 ATOM 862 N N . GLY A 1 115 ? -1.669 -10.760 20.297 1.00 25.33 ? 115 GLY A N 1 ATOM 863 C CA . GLY A 1 115 ? -0.950 -10.301 19.118 1.00 22.34 ? 115 GLY A CA 1 ATOM 864 C C . GLY A 1 115 ? 0.014 -9.220 19.575 1.00 21.91 ? 115 GLY A C 1 ATOM 865 O O . GLY A 1 115 ? -0.377 -8.326 20.311 1.00 21.50 ? 115 GLY A O 1 ATOM 866 N N . ILE A 1 116 ? 1.281 -9.320 19.175 1.00 20.03 ? 116 ILE A N 1 ATOM 867 C CA . ILE A 1 116 ? 2.326 -8.301 19.547 1.00 19.71 ? 116 ILE A CA 1 ATOM 868 C C . ILE A 1 116 ? 2.677 -7.308 18.436 1.00 20.43 ? 116 ILE A C 1 ATOM 869 O O . ILE A 1 116 ? 3.507 -6.436 18.638 1.00 20.23 ? 116 ILE A O 1 ATOM 870 C CB . ILE A 1 116 ? 3.610 -8.953 20.031 1.00 18.15 ? 116 ILE A CB 1 ATOM 871 C CG1 . ILE A 1 116 ? 4.229 -9.802 18.906 1.00 20.24 ? 116 ILE A CG1 1 ATOM 872 C CG2 . ILE A 1 116 ? 3.289 -9.954 21.142 1.00 18.89 ? 116 ILE A CG2 1 ATOM 873 C CD1 . ILE A 1 116 ? 5.301 -10.756 19.440 1.00 22.20 ? 116 ILE A CD1 1 ATOM 874 N N . ILE A 1 117 ? 2.033 -7.394 17.281 1.00 21.22 ? 117 ILE A N 1 ATOM 875 C CA . ILE A 1 117 ? 2.377 -6.423 16.243 1.00 23.25 ? 117 ILE A CA 1 ATOM 876 C C . ILE A 1 117 ? 1.932 -5.026 16.649 1.00 23.63 ? 117 ILE A C 1 ATOM 877 O O . ILE A 1 117 ? 0.793 -4.825 17.116 1.00 24.74 ? 117 ILE A O 1 ATOM 878 C CB . ILE A 1 117 ? 1.868 -6.821 14.808 1.00 24.22 ? 117 ILE A CB 1 ATOM 879 C CG1 . ILE A 1 117 ? 2.689 -7.995 14.297 1.00 23.69 ? 117 ILE A CG1 1 ATOM 880 C CG2 . ILE A 1 117 ? 1.945 -5.617 13.839 1.00 22.42 ? 117 ILE A CG2 1 ATOM 881 C CD1 . ILE A 1 117 ? 1.993 -8.737 13.209 1.00 30.13 ? 117 ILE A CD1 1 ATOM 882 N N . GLY A 1 118 ? 2.855 -4.058 16.504 1.00 23.26 ? 118 GLY A N 1 ATOM 883 C CA . GLY A 1 118 ? 2.600 -2.693 16.953 1.00 20.89 ? 118 GLY A CA 1 ATOM 884 C C . GLY A 1 118 ? 2.970 -2.498 18.398 1.00 20.97 ? 118 GLY A C 1 ATOM 885 O O . GLY A 1 118 ? 2.837 -1.379 18.908 1.00 20.56 ? 118 GLY A O 1 ATOM 886 N N . ARG A 1 119 ? 3.387 -3.577 19.088 1.00 20.26 ? 119 ARG A N 1 ATOM 887 C CA . ARG A 1 119 ? 3.860 -3.448 20.467 1.00 22.12 ? 119 ARG A CA 1 ATOM 888 C C . ARG A 1 119 ? 5.381 -3.219 20.438 1.00 22.10 ? 119 ARG A C 1 ATOM 889 O O . ARG A 1 119 ? 5.918 -2.980 19.385 1.00 22.84 ? 119 ARG A O 1 ATOM 890 C CB . ARG A 1 119 ? 3.369 -4.637 21.353 1.00 22.85 ? 119 ARG A CB 1 ATOM 891 C CG . ARG A 1 119 ? 1.829 -4.667 21.282 1.00 21.90 ? 119 ARG A CG 1 ATOM 892 C CD . ARG A 1 119 ? 1.176 -5.618 22.190 1.00 26.98 ? 119 ARG A CD 1 ATOM 893 N NE . ARG A 1 119 ? -0.289 -5.700 21.948 1.00 29.69 ? 119 ARG A NE 1 ATOM 894 C CZ . ARG A 1 119 ? -1.208 -4.834 22.414 1.00 27.61 ? 119 ARG A CZ 1 ATOM 895 N NH1 . ARG A 1 119 ? -2.484 -5.038 22.138 1.00 27.83 ? 119 ARG A NH1 1 ATOM 896 N NH2 . ARG A 1 119 ? -0.885 -3.793 23.160 1.00 22.19 ? 119 ARG A NH2 1 ATOM 897 N N . ALA A 1 120 ? 6.071 -3.226 21.566 1.00 21.83 ? 120 ALA A N 1 ATOM 898 C CA . ALA A 1 120 ? 7.524 -2.886 21.538 1.00 20.76 ? 120 ALA A CA 1 ATOM 899 C C . ALA A 1 120 ? 8.307 -4.005 22.207 1.00 21.56 ? 120 ALA A C 1 ATOM 900 O O . ALA A 1 120 ? 7.811 -4.649 23.143 1.00 19.37 ? 120 ALA A O 1 ATOM 901 C CB . ALA A 1 120 ? 7.778 -1.612 22.280 1.00 20.01 ? 120 ALA A CB 1 ATOM 902 N N . VAL A 1 121 ? 9.511 -4.278 21.698 1.00 21.37 ? 121 VAL A N 1 ATOM 903 C CA . VAL A 1 121 ? 10.421 -5.142 22.424 1.00 21.87 ? 121 VAL A CA 1 ATOM 904 C C . VAL A 1 121 ? 11.307 -4.178 23.210 1.00 21.76 ? 121 VAL A C 1 ATOM 905 O O . VAL A 1 121 ? 11.679 -3.096 22.680 1.00 22.52 ? 121 VAL A O 1 ATOM 906 C CB . VAL A 1 121 ? 11.257 -5.939 21.426 1.00 22.67 ? 121 VAL A CB 1 ATOM 907 C CG1 . VAL A 1 121 ? 12.408 -6.502 22.164 1.00 29.44 ? 121 VAL A CG1 1 ATOM 908 C CG2 . VAL A 1 121 ? 10.448 -7.068 20.956 1.00 24.86 ? 121 VAL A CG2 1 ATOM 909 N N . VAL A 1 122 ? 11.659 -4.538 24.434 1.00 17.70 ? 122 VAL A N 1 ATOM 910 C CA . VAL A 1 122 ? 12.498 -3.694 25.277 1.00 16.87 ? 122 VAL A CA 1 ATOM 911 C C . VAL A 1 122 ? 13.599 -4.543 25.900 1.00 17.99 ? 122 VAL A C 1 ATOM 912 O O . VAL A 1 122 ? 13.314 -5.603 26.509 1.00 17.44 ? 122 VAL A O 1 ATOM 913 C CB . VAL A 1 122 ? 11.776 -3.020 26.428 1.00 16.41 ? 122 VAL A CB 1 ATOM 914 C CG1 . VAL A 1 122 ? 12.792 -2.156 27.249 1.00 14.54 ? 122 VAL A CG1 1 ATOM 915 C CG2 . VAL A 1 122 ? 10.650 -2.142 25.880 1.00 16.39 ? 122 VAL A CG2 1 ATOM 916 N N . LEU A 1 123 ? 14.840 -4.089 25.720 1.00 16.76 ? 123 LEU A N 1 ATOM 917 C CA . LEU A 1 123 ? 16.004 -4.748 26.336 1.00 17.76 ? 123 LEU A CA 1 ATOM 918 C C . LEU A 1 123 ? 16.367 -3.946 27.539 1.00 18.11 ? 123 LEU A C 1 ATOM 919 O O . LEU A 1 123 ? 16.561 -2.709 27.426 1.00 19.17 ? 123 LEU A O 1 ATOM 920 C CB . LEU A 1 123 ? 17.195 -4.677 25.386 1.00 17.41 ? 123 LEU A CB 1 ATOM 921 C CG . LEU A 1 123 ? 18.554 -5.246 25.780 1.00 20.65 ? 123 LEU A CG 1 ATOM 922 C CD1 . LEU A 1 123 ? 18.492 -6.728 26.006 1.00 21.19 ? 123 LEU A CD1 1 ATOM 923 C CD2 . LEU A 1 123 ? 19.513 -4.958 24.623 1.00 20.53 ? 123 LEU A CD2 1 ATOM 924 N N . HIS A 1 124 ? 16.629 -4.644 28.638 1.00 17.89 ? 124 HIS A N 1 ATOM 925 C CA . HIS A 1 124 ? 16.829 -3.992 29.912 1.00 18.39 ? 124 HIS A CA 1 ATOM 926 C C . HIS A 1 124 ? 18.250 -4.041 30.363 1.00 19.00 ? 124 HIS A C 1 ATOM 927 O O . HIS A 1 124 ? 19.056 -4.850 29.848 1.00 16.91 ? 124 HIS A O 1 ATOM 928 C CB . HIS A 1 124 ? 15.945 -4.733 30.950 1.00 18.55 ? 124 HIS A CB 1 ATOM 929 C CG . HIS A 1 124 ? 14.499 -4.511 30.731 1.00 19.24 ? 124 HIS A CG 1 ATOM 930 N ND1 . HIS A 1 124 ? 13.856 -3.384 31.186 1.00 20.39 ? 124 HIS A ND1 1 ATOM 931 C CD2 . HIS A 1 124 ? 13.569 -5.257 30.099 1.00 19.71 ? 124 HIS A CD2 1 ATOM 932 C CE1 . HIS A 1 124 ? 12.578 -3.464 30.860 1.00 22.58 ? 124 HIS A CE1 1 ATOM 933 N NE2 . HIS A 1 124 ? 12.366 -4.602 30.221 1.00 27.72 ? 124 HIS A NE2 1 ATOM 934 N N . GLU A 1 125 ? 18.560 -3.208 31.355 1.00 19.71 ? 125 GLU A N 1 ATOM 935 C CA . GLU A 1 125 ? 19.908 -3.048 31.825 1.00 22.90 ? 125 GLU A CA 1 ATOM 936 C C . GLU A 1 125 ? 20.399 -4.200 32.703 1.00 20.87 ? 125 GLU A C 1 ATOM 937 O O . GLU A 1 125 ? 21.590 -4.410 32.838 1.00 20.76 ? 125 GLU A O 1 ATOM 938 C CB . GLU A 1 125 ? 20.064 -1.678 32.539 1.00 24.17 ? 125 GLU A CB 1 ATOM 939 C CG . GLU A 1 125 ? 19.970 -1.671 34.060 1.00 31.97 ? 125 GLU A CG 1 ATOM 940 C CD . GLU A 1 125 ? 19.568 -0.248 34.632 1.00 33.45 ? 125 GLU A CD 1 ATOM 941 O OE1 . GLU A 1 125 ? 19.912 0.783 33.968 1.00 45.83 ? 125 GLU A OE1 1 ATOM 942 O OE2 . GLU A 1 125 ? 18.930 -0.168 35.722 1.00 38.37 ? 125 GLU A OE2 1 ATOM 943 N N . LYS A 1 126 ? 19.480 -4.961 33.290 1.00 19.98 ? 126 LYS A N 1 ATOM 944 C CA . LYS A 1 126 ? 19.870 -6.174 34.039 1.00 20.60 ? 126 LYS A CA 1 ATOM 945 C C . LYS A 1 126 ? 18.971 -7.333 33.848 1.00 18.88 ? 126 LYS A C 1 ATOM 946 O O . LYS A 1 126 ? 17.927 -7.234 33.175 1.00 16.35 ? 126 LYS A O 1 ATOM 947 C CB . LYS A 1 126 ? 20.053 -5.917 35.521 1.00 22.60 ? 126 LYS A CB 1 ATOM 948 C CG . LYS A 1 126 ? 18.938 -5.236 36.252 1.00 25.65 ? 126 LYS A CG 1 ATOM 949 C CD . LYS A 1 126 ? 19.595 -4.509 37.407 1.00 34.03 ? 126 LYS A CD 1 ATOM 950 C CE . LYS A 1 126 ? 18.591 -4.246 38.573 1.00 39.80 ? 126 LYS A CE 1 ATOM 951 N NZ . LYS A 1 126 ? 19.222 -4.446 39.936 1.00 40.32 ? 126 LYS A NZ 1 ATOM 952 N N . ALA A 1 127 ? 19.366 -8.416 34.484 1.00 19.66 ? 127 ALA A N 1 ATOM 953 C CA . ALA A 1 127 ? 18.672 -9.686 34.346 1.00 21.08 ? 127 ALA A CA 1 ATOM 954 C C . ALA A 1 127 ? 17.249 -9.635 34.901 1.00 21.77 ? 127 ALA A C 1 ATOM 955 O O . ALA A 1 127 ? 16.966 -8.952 35.867 1.00 23.20 ? 127 ALA A O 1 ATOM 956 C CB . ALA A 1 127 ? 19.462 -10.803 35.040 1.00 21.35 ? 127 ALA A CB 1 ATOM 957 N N . ASP A 1 128 ? 16.358 -10.356 34.263 1.00 22.32 ? 128 ASP A N 1 ATOM 958 C CA . ASP A 1 128 ? 15.004 -10.577 34.782 1.00 24.16 ? 128 ASP A CA 1 ATOM 959 C C . ASP A 1 128 ? 15.111 -11.668 35.874 1.00 23.22 ? 128 ASP A C 1 ATOM 960 O O . ASP A 1 128 ? 15.648 -12.734 35.593 1.00 22.24 ? 128 ASP A O 1 ATOM 961 C CB . ASP A 1 128 ? 14.194 -11.122 33.605 1.00 24.15 ? 128 ASP A CB 1 ATOM 962 C CG . ASP A 1 128 ? 12.686 -11.248 33.886 1.00 27.20 ? 128 ASP A CG 1 ATOM 963 O OD1 . ASP A 1 128 ? 11.940 -11.200 32.873 1.00 22.73 ? 128 ASP A OD1 1 ATOM 964 O OD2 . ASP A 1 128 ? 12.251 -11.419 35.062 1.00 25.73 ? 128 ASP A OD2 1 ATOM 965 N N . ASP A 1 129 ? 14.561 -11.429 37.077 1.00 24.38 ? 129 ASP A N 1 ATOM 966 C CA . ASP A 1 129 ? 14.656 -12.416 38.185 1.00 24.35 ? 129 ASP A CA 1 ATOM 967 C C . ASP A 1 129 ? 13.399 -13.325 38.245 1.00 24.84 ? 129 ASP A C 1 ATOM 968 O O . ASP A 1 129 ? 13.197 -14.127 39.179 1.00 25.39 ? 129 ASP A O 1 ATOM 969 C CB . ASP A 1 129 ? 14.886 -11.667 39.506 1.00 24.14 ? 129 ASP A CB 1 ATOM 970 C CG . ASP A 1 129 ? 13.630 -10.897 39.986 1.00 27.83 ? 129 ASP A CG 1 ATOM 971 O OD1 . ASP A 1 129 ? 13.790 -10.044 40.896 1.00 28.31 ? 129 ASP A OD1 1 ATOM 972 O OD2 . ASP A 1 129 ? 12.488 -11.112 39.459 1.00 23.83 ? 129 ASP A OD2 1 ATOM 973 N N . TYR A 1 130 ? 12.562 -13.175 37.226 1.00 23.28 ? 130 TYR A N 1 ATOM 974 C CA . TYR A 1 130 ? 11.434 -14.044 36.897 1.00 22.99 ? 130 TYR A CA 1 ATOM 975 C C . TYR A 1 130 ? 10.344 -13.988 37.954 1.00 25.88 ? 130 TYR A C 1 ATOM 976 O O . TYR A 1 130 ? 9.520 -14.905 38.033 1.00 25.40 ? 130 TYR A O 1 ATOM 977 C CB . TYR A 1 130 ? 11.844 -15.475 36.626 1.00 21.92 ? 130 TYR A CB 1 ATOM 978 C CG . TYR A 1 130 ? 12.953 -15.700 35.646 1.00 22.55 ? 130 TYR A CG 1 ATOM 979 C CD1 . TYR A 1 130 ? 12.858 -15.250 34.306 1.00 20.99 ? 130 TYR A CD1 1 ATOM 980 C CD2 . TYR A 1 130 ? 14.115 -16.403 36.041 1.00 21.99 ? 130 TYR A CD2 1 ATOM 981 C CE1 . TYR A 1 130 ? 13.901 -15.495 33.376 1.00 21.82 ? 130 TYR A CE1 1 ATOM 982 C CE2 . TYR A 1 130 ? 15.160 -16.594 35.159 1.00 24.50 ? 130 TYR A CE2 1 ATOM 983 C CZ . TYR A 1 130 ? 15.043 -16.162 33.819 1.00 25.64 ? 130 TYR A CZ 1 ATOM 984 O OH . TYR A 1 130 ? 16.084 -16.418 32.948 1.00 27.77 ? 130 TYR A OH 1 ATOM 985 N N . GLY A 1 131 ? 10.310 -12.901 38.728 1.00 27.75 ? 131 GLY A N 1 ATOM 986 C CA . GLY A 1 131 ? 9.303 -12.717 39.788 1.00 30.71 ? 131 GLY A CA 1 ATOM 987 C C . GLY A 1 131 ? 9.554 -13.585 41.036 1.00 33.07 ? 131 GLY A C 1 ATOM 988 O O . GLY A 1 131 ? 8.677 -13.762 41.843 1.00 32.92 ? 131 GLY A O 1 ATOM 989 N N . LYS A 1 132 ? 10.763 -14.108 41.191 1.00 35.22 ? 132 LYS A N 1 ATOM 990 C CA . LYS A 1 132 ? 11.066 -15.118 42.210 1.00 37.74 ? 132 LYS A CA 1 ATOM 991 C C . LYS A 1 132 ? 11.846 -14.547 43.400 1.00 40.05 ? 132 LYS A C 1 ATOM 992 O O . LYS A 1 132 ? 12.098 -15.252 44.419 1.00 41.33 ? 132 LYS A O 1 ATOM 993 C CB . LYS A 1 132 ? 11.855 -16.261 41.595 1.00 36.90 ? 132 LYS A CB 1 ATOM 994 C CG . LYS A 1 132 ? 11.120 -16.936 40.496 1.00 37.76 ? 132 LYS A CG 1 ATOM 995 C CD . LYS A 1 132 ? 11.997 -17.958 39.808 1.00 43.83 ? 132 LYS A CD 1 ATOM 996 C CE . LYS A 1 132 ? 11.139 -18.749 38.780 1.00 46.36 ? 132 LYS A CE 1 ATOM 997 N NZ . LYS A 1 132 ? 11.951 -18.983 37.571 1.00 40.62 ? 132 LYS A NZ 1 ATOM 998 N N . SER A 1 133 ? 12.218 -13.274 43.294 1.00 40.71 ? 133 SER A N 1 ATOM 999 C CA . SER A 1 133 ? 12.916 -12.647 44.389 1.00 41.62 ? 133 SER A CA 1 ATOM 1000 C C . SER A 1 133 ? 11.975 -11.848 45.310 1.00 42.98 ? 133 SER A C 1 ATOM 1001 O O . SER A 1 133 ? 10.763 -11.765 45.115 1.00 41.15 ? 133 SER A O 1 ATOM 1002 C CB . SER A 1 133 ? 14.022 -11.733 43.858 1.00 41.32 ? 133 SER A CB 1 ATOM 1003 O OG . SER A 1 133 ? 13.471 -10.443 43.714 1.00 38.63 ? 133 SER A OG 1 ATOM 1004 N N . ASP A 1 134 ? 12.634 -11.188 46.247 1.00 45.07 ? 134 ASP A N 1 ATOM 1005 C CA . ASP A 1 134 ? 12.092 -10.475 47.363 1.00 48.27 ? 134 ASP A CA 1 ATOM 1006 C C . ASP A 1 134 ? 12.069 -8.937 47.133 1.00 48.65 ? 134 ASP A C 1 ATOM 1007 O O . ASP A 1 134 ? 11.491 -8.185 47.946 1.00 49.13 ? 134 ASP A O 1 ATOM 1008 C CB . ASP A 1 134 ? 13.060 -10.813 48.510 1.00 49.84 ? 134 ASP A CB 1 ATOM 1009 C CG . ASP A 1 134 ? 14.483 -11.182 47.978 1.00 53.39 ? 134 ASP A CG 1 ATOM 1010 O OD1 . ASP A 1 134 ? 15.464 -10.417 48.232 1.00 57.33 ? 134 ASP A OD1 1 ATOM 1011 O OD2 . ASP A 1 134 ? 14.607 -12.237 47.280 1.00 55.58 ? 134 ASP A OD2 1 ATOM 1012 N N . HIS A 1 135 ? 12.736 -8.481 46.062 1.00 48.54 ? 135 HIS A N 1 ATOM 1013 C CA . HIS A 1 135 ? 12.793 -7.058 45.653 1.00 48.24 ? 135 HIS A CA 1 ATOM 1014 C C . HIS A 1 135 ? 11.352 -6.557 45.346 1.00 48.25 ? 135 HIS A C 1 ATOM 1015 O O . HIS A 1 135 ? 10.544 -7.326 44.853 1.00 48.75 ? 135 HIS A O 1 ATOM 1016 C CB . HIS A 1 135 ? 13.739 -6.942 44.441 1.00 48.52 ? 135 HIS A CB 1 ATOM 1017 C CG . HIS A 1 135 ? 13.855 -5.557 43.886 1.00 49.51 ? 135 HIS A CG 1 ATOM 1018 N ND1 . HIS A 1 135 ? 12.849 -4.960 43.155 1.00 50.63 ? 135 HIS A ND1 1 ATOM 1019 C CD2 . HIS A 1 135 ? 14.849 -4.635 43.984 1.00 51.89 ? 135 HIS A CD2 1 ATOM 1020 C CE1 . HIS A 1 135 ? 13.210 -3.730 42.830 1.00 50.94 ? 135 HIS A CE1 1 ATOM 1021 N NE2 . HIS A 1 135 ? 14.417 -3.503 43.328 1.00 53.13 ? 135 HIS A NE2 1 ATOM 1022 N N . PRO A 1 136 ? 10.984 -5.301 45.711 1.00 48.16 ? 136 PRO A N 1 ATOM 1023 C CA . PRO A 1 136 ? 9.566 -4.866 45.521 1.00 47.86 ? 136 PRO A CA 1 ATOM 1024 C C . PRO A 1 136 ? 8.958 -4.921 44.091 1.00 47.93 ? 136 PRO A C 1 ATOM 1025 O O . PRO A 1 136 ? 7.730 -5.105 43.948 1.00 47.73 ? 136 PRO A O 1 ATOM 1026 C CB . PRO A 1 136 ? 9.559 -3.415 46.023 1.00 47.89 ? 136 PRO A CB 1 ATOM 1027 C CG . PRO A 1 136 ? 10.782 -3.270 46.841 1.00 48.75 ? 136 PRO A CG 1 ATOM 1028 C CD . PRO A 1 136 ? 11.796 -4.264 46.375 1.00 48.20 ? 136 PRO A CD 1 ATOM 1029 N N . ASP A 1 137 ? 9.796 -4.747 43.054 1.00 46.82 ? 137 ASP A N 1 ATOM 1030 C CA . ASP A 1 137 ? 9.356 -4.806 41.632 1.00 45.99 ? 137 ASP A CA 1 ATOM 1031 C C . ASP A 1 137 ? 9.249 -6.260 41.055 1.00 43.44 ? 137 ASP A C 1 ATOM 1032 O O . ASP A 1 137 ? 8.832 -6.437 39.912 1.00 43.35 ? 137 ASP A O 1 ATOM 1033 C CB . ASP A 1 137 ? 10.334 -4.008 40.715 1.00 46.58 ? 137 ASP A CB 1 ATOM 1034 C CG . ASP A 1 137 ? 10.517 -2.517 41.136 1.00 49.77 ? 137 ASP A CG 1 ATOM 1035 O OD1 . ASP A 1 137 ? 11.683 -2.077 41.308 1.00 51.07 ? 137 ASP A OD1 1 ATOM 1036 O OD2 . ASP A 1 137 ? 9.514 -1.778 41.277 1.00 52.92 ? 137 ASP A OD2 1 ATOM 1037 N N . SER A 1 138 ? 9.641 -7.277 41.813 1.00 40.06 ? 138 SER A N 1 ATOM 1038 C CA . SER A 1 138 ? 9.864 -8.598 41.212 1.00 37.87 ? 138 SER A CA 1 ATOM 1039 C C . SER A 1 138 ? 8.642 -9.175 40.458 1.00 37.19 ? 138 SER A C 1 ATOM 1040 O O . SER A 1 138 ? 8.779 -9.610 39.297 1.00 35.78 ? 138 SER A O 1 ATOM 1041 C CB . SER A 1 138 ? 10.492 -9.585 42.200 1.00 37.92 ? 138 SER A CB 1 ATOM 1042 O OG . SER A 1 138 ? 10.880 -10.817 41.543 1.00 37.08 ? 138 SER A OG 1 ATOM 1043 N N . ARG A 1 139 ? 7.454 -9.139 41.081 1.00 36.00 ? 139 ARG A N 1 ATOM 1044 C CA . ARG A 1 139 ? 6.271 -9.754 40.502 1.00 36.23 ? 139 ARG A CA 1 ATOM 1045 C C . ARG A 1 139 ? 5.596 -8.885 39.469 1.00 34.91 ? 139 ARG A C 1 ATOM 1046 O O . ARG A 1 139 ? 4.587 -9.311 38.914 1.00 33.41 ? 139 ARG A O 1 ATOM 1047 C CB . ARG A 1 139 ? 5.221 -10.111 41.574 1.00 38.57 ? 139 ARG A CB 1 ATOM 1048 C CG . ARG A 1 139 ? 5.613 -11.319 42.469 1.00 44.29 ? 139 ARG A CG 1 ATOM 1049 C CD . ARG A 1 139 ? 5.384 -12.706 41.764 1.00 53.72 ? 139 ARG A CD 1 ATOM 1050 N NE . ARG A 1 139 ? 4.164 -13.479 42.131 1.00 58.72 ? 139 ARG A NE 1 ATOM 1051 C CZ . ARG A 1 139 ? 3.115 -13.074 42.872 1.00 61.91 ? 139 ARG A CZ 1 ATOM 1052 N NH1 . ARG A 1 139 ? 2.114 -13.925 43.084 1.00 62.46 ? 139 ARG A NH1 1 ATOM 1053 N NH2 . ARG A 1 139 ? 3.031 -11.849 43.406 1.00 62.37 ? 139 ARG A NH2 1 ATOM 1054 N N . LYS A 1 140 ? 6.154 -7.689 39.215 1.00 33.14 ? 140 LYS A N 1 ATOM 1055 C CA . LYS A 1 140 ? 5.714 -6.807 38.158 1.00 33.07 ? 140 LYS A CA 1 ATOM 1056 C C . LYS A 1 140 ? 6.684 -6.699 36.956 1.00 32.01 ? 140 LYS A C 1 ATOM 1057 O O . LYS A 1 140 ? 6.254 -6.648 35.797 1.00 31.02 ? 140 LYS A O 1 ATOM 1058 C CB . LYS A 1 140 ? 5.507 -5.390 38.694 1.00 35.09 ? 140 LYS A CB 1 ATOM 1059 C CG . LYS A 1 140 ? 4.787 -5.289 40.012 1.00 40.03 ? 140 LYS A CG 1 ATOM 1060 C CD . LYS A 1 140 ? 3.969 -3.978 40.059 1.00 49.25 ? 140 LYS A CD 1 ATOM 1061 C CE . LYS A 1 140 ? 2.635 -4.063 39.254 1.00 52.09 ? 140 LYS A CE 1 ATOM 1062 N NZ . LYS A 1 140 ? 1.513 -4.716 40.031 1.00 50.32 ? 140 LYS A NZ 1 ATOM 1063 N N . THR A 1 141 ? 7.975 -6.541 37.246 1.00 29.87 ? 141 THR A N 1 ATOM 1064 C CA . THR A 1 141 ? 8.929 -6.247 36.225 1.00 29.53 ? 141 THR A CA 1 ATOM 1065 C C . THR A 1 141 ? 10.067 -7.234 36.222 1.00 28.06 ? 141 THR A C 1 ATOM 1066 O O . THR A 1 141 ? 10.927 -7.169 35.372 1.00 27.44 ? 141 THR A O 1 ATOM 1067 C CB . THR A 1 141 ? 9.547 -4.831 36.414 1.00 30.63 ? 141 THR A CB 1 ATOM 1068 O OG1 . THR A 1 141 ? 10.263 -4.806 37.649 1.00 29.74 ? 141 THR A OG1 1 ATOM 1069 C CG2 . THR A 1 141 ? 8.468 -3.698 36.420 1.00 29.66 ? 141 THR A CG2 1 ATOM 1070 N N . GLY A 1 142 ? 10.155 -8.095 37.225 1.00 27.42 ? 142 GLY A N 1 ATOM 1071 C CA . GLY A 1 142 ? 11.354 -8.945 37.278 1.00 25.14 ? 142 GLY A CA 1 ATOM 1072 C C . GLY A 1 142 ? 12.623 -8.250 37.783 1.00 24.40 ? 142 GLY A C 1 ATOM 1073 O O . GLY A 1 142 ? 13.683 -8.893 37.808 1.00 23.35 ? 142 GLY A O 1 ATOM 1074 N N . ASN A 1 143 ? 12.482 -6.993 38.263 1.00 23.60 ? 143 ASN A N 1 ATOM 1075 C CA . ASN A 1 143 ? 13.593 -6.169 38.736 1.00 24.32 ? 143 ASN A CA 1 ATOM 1076 C C . ASN A 1 143 ? 14.681 -6.075 37.631 1.00 24.69 ? 143 ASN A C 1 ATOM 1077 O O . ASN A 1 143 ? 15.892 -6.291 37.916 1.00 23.43 ? 143 ASN A O 1 ATOM 1078 C CB . ASN A 1 143 ? 14.164 -6.802 40.031 1.00 24.86 ? 143 ASN A CB 1 ATOM 1079 C CG . ASN A 1 143 ? 15.205 -5.933 40.743 1.00 28.31 ? 143 ASN A CG 1 ATOM 1080 O OD1 . ASN A 1 143 ? 16.099 -6.464 41.430 1.00 34.00 ? 143 ASN A OD1 1 ATOM 1081 N ND2 . ASN A 1 143 ? 15.106 -4.640 40.592 1.00 28.28 ? 143 ASN A ND2 1 ATOM 1082 N N . ALA A 1 144 ? 14.263 -5.846 36.375 1.00 23.62 ? 144 ALA A N 1 ATOM 1083 C CA . ALA A 1 144 ? 15.270 -5.868 35.277 1.00 24.83 ? 144 ALA A CA 1 ATOM 1084 C C . ALA A 1 144 ? 15.876 -4.500 35.036 1.00 24.46 ? 144 ALA A C 1 ATOM 1085 O O . ALA A 1 144 ? 16.840 -4.324 34.253 1.00 24.31 ? 144 ALA A O 1 ATOM 1086 C CB . ALA A 1 144 ? 14.705 -6.549 33.951 1.00 24.41 ? 144 ALA A CB 1 ATOM 1087 N N . GLY A 1 145 ? 15.331 -3.516 35.743 1.00 24.59 ? 145 GLY A N 1 ATOM 1088 C CA . GLY A 1 145 ? 15.955 -2.198 35.799 1.00 25.07 ? 145 GLY A CA 1 ATOM 1089 C C . GLY A 1 145 ? 15.560 -1.336 34.615 1.00 25.03 ? 145 GLY A C 1 ATOM 1090 O O . GLY A 1 145 ? 14.531 -1.568 34.016 1.00 25.01 ? 145 GLY A O 1 ATOM 1091 N N . GLY A 1 146 ? 16.410 -0.357 34.283 1.00 24.28 ? 146 GLY A N 1 ATOM 1092 C CA . GLY A 1 146 ? 16.158 0.614 33.231 1.00 23.02 ? 146 GLY A CA 1 ATOM 1093 C C . GLY A 1 146 ? 16.211 -0.050 31.860 1.00 23.95 ? 146 GLY A C 1 ATOM 1094 O O . GLY A 1 146 ? 16.552 -1.239 31.718 1.00 23.21 ? 146 GLY A O 1 ATOM 1095 N N . ARG A 1 147 ? 15.863 0.746 30.849 1.00 24.00 ? 147 ARG A N 1 ATOM 1096 C CA . ARG A 1 147 ? 15.555 0.247 29.532 1.00 23.59 ? 147 ARG A CA 1 ATOM 1097 C C . ARG A 1 147 ? 16.675 0.684 28.626 1.00 24.27 ? 147 ARG A C 1 ATOM 1098 O O . ARG A 1 147 ? 16.866 1.852 28.449 1.00 23.71 ? 147 ARG A O 1 ATOM 1099 C CB . ARG A 1 147 ? 14.228 0.862 29.095 1.00 23.00 ? 147 ARG A CB 1 ATOM 1100 C CG . ARG A 1 147 ? 13.082 0.438 30.052 1.00 21.73 ? 147 ARG A CG 1 ATOM 1101 C CD . ARG A 1 147 ? 11.725 0.823 29.554 1.00 22.34 ? 147 ARG A CD 1 ATOM 1102 N NE . ARG A 1 147 ? 10.768 0.455 30.580 1.00 23.98 ? 147 ARG A NE 1 ATOM 1103 C CZ . ARG A 1 147 ? 9.444 0.574 30.513 1.00 25.48 ? 147 ARG A CZ 1 ATOM 1104 N NH1 . ARG A 1 147 ? 8.721 0.192 31.557 1.00 25.64 ? 147 ARG A NH1 1 ATOM 1105 N NH2 . ARG A 1 147 ? 8.838 1.067 29.436 1.00 24.49 ? 147 ARG A NH2 1 ATOM 1106 N N . VAL A 1 148 ? 17.445 -0.248 28.086 1.00 24.74 ? 148 VAL A N 1 ATOM 1107 C CA . VAL A 1 148 ? 18.648 0.208 27.344 1.00 24.47 ? 148 VAL A CA 1 ATOM 1108 C C . VAL A 1 148 ? 18.365 0.414 25.847 1.00 23.58 ? 148 VAL A C 1 ATOM 1109 O O . VAL A 1 148 ? 19.062 1.171 25.188 1.00 22.82 ? 148 VAL A O 1 ATOM 1110 C CB . VAL A 1 148 ? 19.907 -0.663 27.585 1.00 24.85 ? 148 VAL A CB 1 ATOM 1111 C CG1 . VAL A 1 148 ? 20.245 -0.734 29.087 1.00 27.17 ? 148 VAL A CG1 1 ATOM 1112 C CG2 . VAL A 1 148 ? 19.725 -2.017 27.080 1.00 23.96 ? 148 VAL A CG2 1 ATOM 1113 N N . ALA A 1 149 ? 17.359 -0.295 25.305 1.00 22.43 ? 149 ALA A N 1 ATOM 1114 C CA . ALA A 1 149 ? 16.959 -0.101 23.919 1.00 20.66 ? 149 ALA A CA 1 ATOM 1115 C C . ALA A 1 149 ? 15.582 -0.668 23.720 1.00 20.17 ? 149 ALA A C 1 ATOM 1116 O O . ALA A 1 149 ? 15.183 -1.572 24.447 1.00 18.53 ? 149 ALA A O 1 ATOM 1117 C CB . ALA A 1 149 ? 18.019 -0.828 22.986 1.00 18.72 ? 149 ALA A CB 1 ATOM 1118 N N . CYS A 1 150 ? 14.874 -0.152 22.706 1.00 20.94 ? 150 CYS A N 1 ATOM 1119 C CA . CYS A 1 150 ? 13.556 -0.640 22.345 1.00 23.59 ? 150 CYS A CA 1 ATOM 1120 C C . CYS A 1 150 ? 13.294 -0.505 20.868 1.00 22.94 ? 150 CYS A C 1 ATOM 1121 O O . CYS A 1 150 ? 13.935 0.326 20.193 1.00 23.04 ? 150 CYS A O 1 ATOM 1122 C CB . CYS A 1 150 ? 12.429 0.119 23.116 1.00 23.98 ? 150 CYS A CB 1 ATOM 1123 S SG . CYS A 1 150 ? 12.575 1.842 23.205 1.00 35.56 ? 150 CYS A SG 1 ATOM 1124 N N . GLY A 1 151 ? 12.352 -1.288 20.355 1.00 21.32 ? 151 GLY A N 1 ATOM 1125 C CA . GLY A 1 151 ? 11.940 -1.113 18.974 1.00 19.62 ? 151 GLY A CA 1 ATOM 1126 C C . GLY A 1 151 ? 10.490 -1.491 18.844 1.00 19.60 ? 151 GLY A C 1 ATOM 1127 O O . GLY A 1 151 ? 10.045 -2.416 19.500 1.00 19.45 ? 151 GLY A O 1 ATOM 1128 N N . VAL A 1 152 ? 9.764 -0.798 17.991 1.00 17.73 ? 152 VAL A N 1 ATOM 1129 C CA . VAL A 1 152 ? 8.409 -1.224 17.645 1.00 18.69 ? 152 VAL A CA 1 ATOM 1130 C C . VAL A 1 152 ? 8.422 -2.507 16.793 1.00 18.48 ? 152 VAL A C 1 ATOM 1131 O O . VAL A 1 152 ? 9.242 -2.681 15.879 1.00 16.18 ? 152 VAL A O 1 ATOM 1132 C CB . VAL A 1 152 ? 7.619 -0.126 16.876 1.00 18.27 ? 152 VAL A CB 1 ATOM 1133 C CG1 . VAL A 1 152 ? 6.187 -0.568 16.733 1.00 18.69 ? 152 VAL A CG1 1 ATOM 1134 C CG2 . VAL A 1 152 ? 7.663 1.193 17.612 1.00 17.86 ? 152 VAL A CG2 1 ATOM 1135 N N . ILE A 1 153 ? 7.535 -3.428 17.098 1.00 17.25 ? 153 ILE A N 1 ATOM 1136 C CA . ILE A 1 153 ? 7.422 -4.658 16.283 1.00 17.81 ? 153 ILE A CA 1 ATOM 1137 C C . ILE A 1 153 ? 6.596 -4.400 15.026 1.00 19.38 ? 153 ILE A C 1 ATOM 1138 O O . ILE A 1 153 ? 5.387 -4.157 15.140 1.00 19.98 ? 153 ILE A O 1 ATOM 1139 C CB . ILE A 1 153 ? 6.761 -5.751 17.098 1.00 18.58 ? 153 ILE A CB 1 ATOM 1140 C CG1 . ILE A 1 153 ? 7.567 -5.981 18.373 1.00 16.81 ? 153 ILE A CG1 1 ATOM 1141 C CG2 . ILE A 1 153 ? 6.622 -7.054 16.285 1.00 21.09 ? 153 ILE A CG2 1 ATOM 1142 C CD1 . ILE A 1 153 ? 6.874 -6.880 19.493 1.00 16.30 ? 153 ILE A CD1 1 ATOM 1143 N N . GLY A 1 154 ? 7.259 -4.412 13.845 1.00 20.13 ? 154 GLY A N 1 ATOM 1144 C CA . GLY A 1 154 ? 6.619 -4.064 12.596 1.00 20.90 ? 154 GLY A CA 1 ATOM 1145 C C . GLY A 1 154 ? 6.345 -5.292 11.746 1.00 21.28 ? 154 GLY A C 1 ATOM 1146 O O . GLY A 1 154 ? 6.932 -6.329 11.978 1.00 21.20 ? 154 GLY A O 1 ATOM 1147 N N . ILE A 1 155 ? 5.462 -5.149 10.766 1.00 21.56 ? 155 ILE A N 1 ATOM 1148 C CA . ILE A 1 155 ? 5.125 -6.190 9.828 1.00 23.69 ? 155 ILE A CA 1 ATOM 1149 C C . ILE A 1 155 ? 6.338 -6.333 8.914 1.00 25.92 ? 155 ILE A C 1 ATOM 1150 O O . ILE A 1 155 ? 6.845 -5.390 8.325 1.00 25.03 ? 155 ILE A O 1 ATOM 1151 C CB . ILE A 1 155 ? 3.799 -5.873 9.002 1.00 23.23 ? 155 ILE A CB 1 ATOM 1152 C CG1 . ILE A 1 155 ? 2.601 -5.973 9.931 1.00 25.10 ? 155 ILE A CG1 1 ATOM 1153 C CG2 . ILE A 1 155 ? 3.605 -6.917 7.882 1.00 22.29 ? 155 ILE A CG2 1 ATOM 1154 C CD1 . ILE A 1 155 ? 1.273 -5.341 9.428 1.00 23.62 ? 155 ILE A CD1 1 ATOM 1155 N N . LEU A 1 156 ? 6.858 -7.539 8.892 1.00 28.87 ? 156 LEU A N 1 ATOM 1156 C CA . LEU A 1 156 ? 7.893 -7.922 7.990 1.00 30.68 ? 156 LEU A CA 1 ATOM 1157 C C . LEU A 1 156 ? 7.094 -8.642 6.916 1.00 33.87 ? 156 LEU A C 1 ATOM 1158 O O . LEU A 1 156 ? 7.654 -8.960 5.858 1.00 38.53 ? 156 LEU A O 1 ATOM 1159 C CB . LEU A 1 156 ? 8.864 -8.893 8.714 1.00 31.56 ? 156 LEU A CB 1 ATOM 1160 C CG . LEU A 1 156 ? 10.105 -9.488 8.035 1.00 30.06 ? 156 LEU A CG 1 ATOM 1161 C CD1 . LEU A 1 156 ? 11.128 -8.435 7.854 1.00 28.53 ? 156 LEU A CD1 1 ATOM 1162 C CD2 . LEU A 1 156 ? 10.634 -10.564 8.920 1.00 29.89 ? 156 LEU A CD2 1 ATOM 1163 N N . THR B 1 5 ? -10.250 -6.271 22.183 1.00 62.35 ? 5 THR B N 1 ATOM 1164 C CA . THR B 1 5 ? -10.164 -4.778 22.005 1.00 62.43 ? 5 THR B CA 1 ATOM 1165 C C . THR B 1 5 ? -9.151 -4.315 20.935 1.00 61.92 ? 5 THR B C 1 ATOM 1166 O O . THR B 1 5 ? -7.989 -4.039 21.263 1.00 62.34 ? 5 THR B O 1 ATOM 1167 C CB . THR B 1 5 ? -9.840 -4.051 23.353 1.00 62.46 ? 5 THR B CB 1 ATOM 1168 O OG1 . THR B 1 5 ? -9.020 -4.892 24.175 1.00 61.45 ? 5 THR B OG1 1 ATOM 1169 C CG2 . THR B 1 5 ? -11.125 -3.712 24.109 1.00 63.68 ? 5 THR B CG2 1 ATOM 1170 N N . THR B 1 6 ? -9.574 -4.210 19.668 1.00 61.03 ? 6 THR B N 1 ATOM 1171 C CA . THR B 1 6 ? -8.703 -3.549 18.668 1.00 60.37 ? 6 THR B CA 1 ATOM 1172 C C . THR B 1 6 ? -8.325 -2.117 19.159 1.00 59.06 ? 6 THR B C 1 ATOM 1173 O O . THR B 1 6 ? -9.079 -1.504 19.949 1.00 59.95 ? 6 THR B O 1 ATOM 1174 C CB . THR B 1 6 ? -9.304 -3.535 17.228 1.00 60.45 ? 6 THR B CB 1 ATOM 1175 O OG1 . THR B 1 6 ? -10.580 -2.884 17.215 1.00 60.65 ? 6 THR B OG1 1 ATOM 1176 C CG2 . THR B 1 6 ? -9.445 -4.967 16.687 1.00 61.98 ? 6 THR B CG2 1 ATOM 1177 N N . PRO B 1 7 ? -7.161 -1.579 18.723 1.00 56.94 ? 7 PRO B N 1 ATOM 1178 C CA . PRO B 1 7 ? -6.803 -0.285 19.313 1.00 54.59 ? 7 PRO B CA 1 ATOM 1179 C C . PRO B 1 7 ? -7.719 0.841 18.830 1.00 51.69 ? 7 PRO B C 1 ATOM 1180 O O . PRO B 1 7 ? -8.311 0.745 17.751 1.00 51.75 ? 7 PRO B O 1 ATOM 1181 C CB . PRO B 1 7 ? -5.339 -0.067 18.836 1.00 54.45 ? 7 PRO B CB 1 ATOM 1182 C CG . PRO B 1 7 ? -4.889 -1.418 18.356 1.00 55.80 ? 7 PRO B CG 1 ATOM 1183 C CD . PRO B 1 7 ? -6.129 -2.028 17.769 1.00 57.02 ? 7 PRO B CD 1 ATOM 1184 N N . SER B 1 8 ? -7.846 1.888 19.641 1.00 48.15 ? 8 SER B N 1 ATOM 1185 C CA . SER B 1 8 ? -8.487 3.104 19.186 1.00 44.64 ? 8 SER B CA 1 ATOM 1186 C C . SER B 1 8 ? -7.412 4.109 18.727 1.00 41.43 ? 8 SER B C 1 ATOM 1187 O O . SER B 1 8 ? -7.710 5.001 17.941 1.00 40.06 ? 8 SER B O 1 ATOM 1188 C CB . SER B 1 8 ? -9.382 3.714 20.280 1.00 45.06 ? 8 SER B CB 1 ATOM 1189 O OG . SER B 1 8 ? -8.650 3.961 21.488 1.00 47.17 ? 8 SER B OG 1 ATOM 1190 N N . ARG B 1 9 ? -6.167 3.939 19.179 1.00 37.25 ? 9 ARG B N 1 ATOM 1191 C CA . ARG B 1 9 ? -5.117 4.934 18.891 1.00 35.02 ? 9 ARG B CA 1 ATOM 1192 C C . ARG B 1 9 ? -3.751 4.359 18.504 1.00 33.18 ? 9 ARG B C 1 ATOM 1193 O O . ARG B 1 9 ? -3.294 3.359 19.089 1.00 31.44 ? 9 ARG B O 1 ATOM 1194 C CB . ARG B 1 9 ? -4.940 5.900 20.075 1.00 35.24 ? 9 ARG B CB 1 ATOM 1195 C CG . ARG B 1 9 ? -6.226 6.655 20.443 1.00 36.48 ? 9 ARG B CG 1 ATOM 1196 C CD . ARG B 1 9 ? -6.058 8.022 21.077 1.00 40.01 ? 9 ARG B CD 1 ATOM 1197 N NE . ARG B 1 9 ? -5.024 8.217 22.098 1.00 45.66 ? 9 ARG B NE 1 ATOM 1198 C CZ . ARG B 1 9 ? -4.884 7.504 23.216 1.00 47.44 ? 9 ARG B CZ 1 ATOM 1199 N NH1 . ARG B 1 9 ? -5.687 6.466 23.457 1.00 48.70 ? 9 ARG B NH1 1 ATOM 1200 N NH2 . ARG B 1 9 ? -3.899 7.804 24.074 1.00 44.82 ? 9 ARG B NH2 1 ATOM 1201 N N . ALA B 1 10 ? -3.077 5.012 17.557 1.00 30.06 ? 10 ALA B N 1 ATOM 1202 C CA . ALA B 1 10 ? -1.726 4.590 17.171 1.00 28.08 ? 10 ALA B CA 1 ATOM 1203 C C . ALA B 1 10 ? -0.797 5.773 17.061 1.00 27.48 ? 10 ALA B C 1 ATOM 1204 O O . ALA B 1 10 ? -1.251 6.946 16.988 1.00 25.93 ? 10 ALA B O 1 ATOM 1205 C CB . ALA B 1 10 ? -1.763 3.850 15.911 1.00 27.42 ? 10 ALA B CB 1 ATOM 1206 N N . ILE B 1 11 ? 0.508 5.495 17.070 1.00 25.02 ? 11 ILE B N 1 ATOM 1207 C CA . ILE B 1 11 ? 1.487 6.534 16.926 1.00 25.27 ? 11 ILE B CA 1 ATOM 1208 C C . ILE B 1 11 ? 2.719 6.056 16.094 1.00 24.30 ? 11 ILE B C 1 ATOM 1209 O O . ILE B 1 11 ? 3.092 4.910 16.188 1.00 24.01 ? 11 ILE B O 1 ATOM 1210 C CB . ILE B 1 11 ? 1.941 7.058 18.333 1.00 24.49 ? 11 ILE B CB 1 ATOM 1211 C CG1 . ILE B 1 11 ? 2.878 8.237 18.193 1.00 23.33 ? 11 ILE B CG1 1 ATOM 1212 C CG2 . ILE B 1 11 ? 2.581 5.929 19.135 1.00 25.39 ? 11 ILE B CG2 1 ATOM 1213 C CD1 . ILE B 1 11 ? 2.997 9.153 19.490 1.00 26.36 ? 11 ILE B CD1 1 ATOM 1214 N N . ALA B 1 12 ? 3.300 6.957 15.291 1.00 23.69 ? 12 ALA B N 1 ATOM 1215 C CA . ALA B 1 12 ? 4.616 6.766 14.657 1.00 23.69 ? 12 ALA B CA 1 ATOM 1216 C C . ALA B 1 12 ? 5.512 7.898 15.045 1.00 22.90 ? 12 ALA B C 1 ATOM 1217 O O . ALA B 1 12 ? 5.090 9.031 15.069 1.00 23.23 ? 12 ALA B O 1 ATOM 1218 C CB . ALA B 1 12 ? 4.494 6.676 13.148 1.00 22.67 ? 12 ALA B CB 1 ATOM 1219 N N . VAL B 1 13 ? 6.743 7.580 15.439 1.00 23.39 ? 13 VAL B N 1 ATOM 1220 C CA . VAL B 1 13 ? 7.742 8.571 15.830 1.00 21.77 ? 13 VAL B CA 1 ATOM 1221 C C . VAL B 1 13 ? 8.857 8.695 14.787 1.00 22.35 ? 13 VAL B C 1 ATOM 1222 O O . VAL B 1 13 ? 9.418 7.691 14.325 1.00 22.33 ? 13 VAL B O 1 ATOM 1223 C CB . VAL B 1 13 ? 8.350 8.213 17.233 1.00 23.13 ? 13 VAL B CB 1 ATOM 1224 C CG1 . VAL B 1 13 ? 9.544 9.102 17.588 1.00 21.26 ? 13 VAL B CG1 1 ATOM 1225 C CG2 . VAL B 1 13 ? 7.289 8.413 18.313 1.00 20.39 ? 13 VAL B CG2 1 ATOM 1226 N N . LEU B 1 14 ? 9.157 9.909 14.364 1.00 22.42 ? 14 LEU B N 1 ATOM 1227 C CA . LEU B 1 14 ? 10.253 10.094 13.415 1.00 24.01 ? 14 LEU B CA 1 ATOM 1228 C C . LEU B 1 14 ? 11.388 10.619 14.217 1.00 25.21 ? 14 LEU B C 1 ATOM 1229 O O . LEU B 1 14 ? 11.194 11.531 15.062 1.00 23.82 ? 14 LEU B O 1 ATOM 1230 C CB . LEU B 1 14 ? 9.883 11.141 12.389 1.00 24.03 ? 14 LEU B CB 1 ATOM 1231 C CG . LEU B 1 14 ? 9.046 10.797 11.138 1.00 24.74 ? 14 LEU B CG 1 ATOM 1232 C CD1 . LEU B 1 14 ? 8.441 9.443 10.930 1.00 22.21 ? 14 LEU B CD1 1 ATOM 1233 C CD2 . LEU B 1 14 ? 8.140 11.922 10.767 1.00 24.21 ? 14 LEU B CD2 1 ATOM 1234 N N . SER B 1 15 ? 12.588 10.093 13.972 1.00 26.39 ? 15 SER B N 1 ATOM 1235 C CA . SER B 1 15 ? 13.725 10.497 14.809 1.00 26.99 ? 15 SER B CA 1 ATOM 1236 C C . SER B 1 15 ? 15.004 10.337 14.059 1.00 27.26 ? 15 SER B C 1 ATOM 1237 O O . SER B 1 15 ? 15.527 9.238 13.881 1.00 26.98 ? 15 SER B O 1 ATOM 1238 C CB . SER B 1 15 ? 13.821 9.645 16.061 1.00 28.09 ? 15 SER B CB 1 ATOM 1239 O OG . SER B 1 15 ? 14.873 10.122 16.873 1.00 33.60 ? 15 SER B OG 1 ATOM 1240 N N . THR B 1 16 ? 15.546 11.441 13.634 1.00 26.42 ? 16 THR B N 1 ATOM 1241 C CA . THR B 1 16 ? 16.751 11.394 12.863 1.00 27.43 ? 16 THR B CA 1 ATOM 1242 C C . THR B 1 16 ? 17.705 12.481 13.434 1.00 27.54 ? 16 THR B C 1 ATOM 1243 O O . THR B 1 16 ? 17.328 13.232 14.322 1.00 25.42 ? 16 THR B O 1 ATOM 1244 C CB . THR B 1 16 ? 16.231 11.703 11.473 1.00 29.90 ? 16 THR B CB 1 ATOM 1245 O OG1 . THR B 1 16 ? 15.989 10.469 10.714 1.00 31.63 ? 16 THR B OG1 1 ATOM 1246 C CG2 . THR B 1 16 ? 16.964 12.753 10.823 1.00 22.95 ? 16 THR B CG2 1 ATOM 1247 N N . GLU B 1 17 ? 18.917 12.589 12.902 1.00 27.33 ? 17 GLU B N 1 ATOM 1248 C CA . GLU B 1 17 ? 19.821 13.652 13.292 1.00 28.10 ? 17 GLU B CA 1 ATOM 1249 C C . GLU B 1 17 ? 19.242 14.989 12.961 1.00 26.53 ? 17 GLU B C 1 ATOM 1250 O O . GLU B 1 17 ? 19.698 15.986 13.483 1.00 25.56 ? 17 GLU B O 1 ATOM 1251 C CB . GLU B 1 17 ? 21.186 13.509 12.534 1.00 29.38 ? 17 GLU B CB 1 ATOM 1252 C CG . GLU B 1 17 ? 22.318 12.821 13.355 1.00 38.04 ? 17 GLU B CG 1 ATOM 1253 C CD . GLU B 1 17 ? 22.216 11.253 13.519 1.00 51.26 ? 17 GLU B CD 1 ATOM 1254 O OE1 . GLU B 1 17 ? 23.155 10.535 13.025 1.00 55.16 ? 17 GLU B OE1 1 ATOM 1255 O OE2 . GLU B 1 17 ? 21.238 10.730 14.160 1.00 54.35 ? 17 GLU B OE2 1 ATOM 1256 N N . THR B 1 18 ? 18.342 15.064 11.984 1.00 26.40 ? 18 THR B N 1 ATOM 1257 C CA . THR B 1 18 ? 17.790 16.365 11.615 1.00 26.62 ? 18 THR B CA 1 ATOM 1258 C C . THR B 1 18 ? 16.271 16.526 11.805 1.00 26.27 ? 18 THR B C 1 ATOM 1259 O O . THR B 1 18 ? 15.781 17.660 11.903 1.00 27.12 ? 18 THR B O 1 ATOM 1260 C CB . THR B 1 18 ? 18.251 16.831 10.193 1.00 28.27 ? 18 THR B CB 1 ATOM 1261 O OG1 . THR B 1 18 ? 17.703 15.964 9.196 1.00 30.95 ? 18 THR B OG1 1 ATOM 1262 C CG2 . THR B 1 18 ? 19.806 16.771 10.094 1.00 25.78 ? 18 THR B CG2 1 ATOM 1263 N N . ILE B 1 19 ? 15.560 15.413 11.885 1.00 23.87 ? 19 ILE B N 1 ATOM 1264 C CA . ILE B 1 19 ? 14.081 15.362 11.880 1.00 24.31 ? 19 ILE B CA 1 ATOM 1265 C C . ILE B 1 19 ? 13.561 14.697 13.174 1.00 25.21 ? 19 ILE B C 1 ATOM 1266 O O . ILE B 1 19 ? 14.082 13.655 13.521 1.00 23.65 ? 19 ILE B O 1 ATOM 1267 C CB . ILE B 1 19 ? 13.556 14.559 10.646 1.00 23.08 ? 19 ILE B CB 1 ATOM 1268 C CG1 . ILE B 1 19 ? 14.151 15.200 9.385 1.00 25.68 ? 19 ILE B CG1 1 ATOM 1269 C CG2 . ILE B 1 19 ? 12.036 14.512 10.624 1.00 22.59 ? 19 ILE B CG2 1 ATOM 1270 C CD1 . ILE B 1 19 ? 13.336 15.265 8.248 1.00 25.63 ? 19 ILE B CD1 1 ATOM 1271 N N . ARG B 1 20 ? 12.594 15.327 13.879 1.00 24.29 ? 20 ARG B N 1 ATOM 1272 C CA . ARG B 1 20 ? 11.939 14.756 15.055 1.00 26.55 ? 20 ARG B CA 1 ATOM 1273 C C . ARG B 1 20 ? 10.444 15.082 14.947 1.00 24.33 ? 20 ARG B C 1 ATOM 1274 O O . ARG B 1 20 ? 10.053 16.229 14.647 1.00 22.23 ? 20 ARG B O 1 ATOM 1275 C CB . ARG B 1 20 ? 12.477 15.356 16.361 1.00 28.66 ? 20 ARG B CB 1 ATOM 1276 C CG . ARG B 1 20 ? 13.666 16.368 16.195 1.00 35.63 ? 20 ARG B CG 1 ATOM 1277 C CD . ARG B 1 20 ? 14.131 17.095 17.530 1.00 36.00 ? 20 ARG B CD 1 ATOM 1278 N NE . ARG B 1 20 ? 13.071 17.299 18.545 1.00 47.97 ? 20 ARG B NE 1 ATOM 1279 C CZ . ARG B 1 20 ? 13.279 17.832 19.758 1.00 53.66 ? 20 ARG B CZ 1 ATOM 1280 N NH1 . ARG B 1 20 ? 14.507 18.250 20.128 1.00 56.08 ? 20 ARG B NH1 1 ATOM 1281 N NH2 . ARG B 1 20 ? 12.261 17.967 20.604 1.00 56.32 ? 20 ARG B NH2 1 ATOM 1282 N N . GLY B 1 21 ? 9.591 14.102 15.179 1.00 23.45 ? 21 GLY B N 1 ATOM 1283 C CA . GLY B 1 21 ? 8.158 14.315 15.051 1.00 24.12 ? 21 GLY B CA 1 ATOM 1284 C C . GLY B 1 21 ? 7.379 13.160 15.631 1.00 24.68 ? 21 GLY B C 1 ATOM 1285 O O . GLY B 1 21 ? 7.928 12.100 15.798 1.00 21.77 ? 21 GLY B O 1 ATOM 1286 N N . ASN B 1 22 ? 6.114 13.389 15.997 1.00 25.42 ? 22 ASN B N 1 ATOM 1287 C CA . ASN B 1 22 ? 5.201 12.301 16.399 1.00 25.95 ? 22 ASN B CA 1 ATOM 1288 C C . ASN B 1 22 ? 3.964 12.432 15.540 1.00 25.44 ? 22 ASN B C 1 ATOM 1289 O O . ASN B 1 22 ? 3.469 13.540 15.380 1.00 24.92 ? 22 ASN B O 1 ATOM 1290 C CB . ASN B 1 22 ? 4.703 12.449 17.814 1.00 27.34 ? 22 ASN B CB 1 ATOM 1291 C CG . ASN B 1 22 ? 5.774 12.733 18.775 1.00 30.97 ? 22 ASN B CG 1 ATOM 1292 O OD1 . ASN B 1 22 ? 6.812 12.049 18.827 1.00 28.77 ? 22 ASN B OD1 1 ATOM 1293 N ND2 . ASN B 1 22 ? 5.501 13.721 19.614 1.00 35.05 ? 22 ASN B ND2 1 ATOM 1294 N N . ILE B 1 23 ? 3.460 11.326 15.021 1.00 24.03 ? 23 ILE B N 1 ATOM 1295 C CA . ILE B 1 23 ? 2.240 11.340 14.195 1.00 25.78 ? 23 ILE B CA 1 ATOM 1296 C C . ILE B 1 23 ? 1.306 10.358 14.850 1.00 26.32 ? 23 ILE B C 1 ATOM 1297 O O . ILE B 1 23 ? 1.686 9.175 15.001 1.00 26.38 ? 23 ILE B O 1 ATOM 1298 C CB . ILE B 1 23 ? 2.537 10.915 12.741 1.00 25.66 ? 23 ILE B CB 1 ATOM 1299 C CG1 . ILE B 1 23 ? 3.388 11.996 12.026 1.00 26.58 ? 23 ILE B CG1 1 ATOM 1300 C CG2 . ILE B 1 23 ? 1.248 10.707 11.947 1.00 26.19 ? 23 ILE B CG2 1 ATOM 1301 C CD1 . ILE B 1 23 ? 4.807 11.601 11.940 1.00 33.10 ? 23 ILE B CD1 1 ATOM 1302 N N . THR B 1 24 ? 0.127 10.824 15.297 1.00 26.72 ? 24 THR B N 1 ATOM 1303 C CA . THR B 1 24 ? -0.833 9.941 15.985 1.00 27.21 ? 24 THR B CA 1 ATOM 1304 C C . THR B 1 24 ? -2.025 9.711 15.093 1.00 26.92 ? 24 THR B C 1 ATOM 1305 O O . THR B 1 24 ? -2.338 10.540 14.239 1.00 26.87 ? 24 THR B O 1 ATOM 1306 C CB . THR B 1 24 ? -1.294 10.499 17.331 1.00 27.91 ? 24 THR B CB 1 ATOM 1307 O OG1 . THR B 1 24 ? -2.117 11.670 17.091 1.00 33.44 ? 24 THR B OG1 1 ATOM 1308 C CG2 . THR B 1 24 ? -0.071 10.939 18.166 1.00 29.78 ? 24 THR B CG2 1 ATOM 1309 N N . PHE B 1 25 ? -2.657 8.558 15.252 1.00 27.55 ? 25 PHE B N 1 ATOM 1310 C CA . PHE B 1 25 ? -3.760 8.146 14.416 1.00 28.56 ? 25 PHE B CA 1 ATOM 1311 C C . PHE B 1 25 ? -4.868 7.711 15.409 1.00 32.33 ? 25 PHE B C 1 ATOM 1312 O O . PHE B 1 25 ? -4.640 6.870 16.271 1.00 32.67 ? 25 PHE B O 1 ATOM 1313 C CB . PHE B 1 25 ? -3.376 6.959 13.582 1.00 27.81 ? 25 PHE B CB 1 ATOM 1314 C CG . PHE B 1 25 ? -2.231 7.193 12.612 1.00 24.40 ? 25 PHE B CG 1 ATOM 1315 C CD1 . PHE B 1 25 ? -2.505 7.404 11.277 1.00 23.99 ? 25 PHE B CD1 1 ATOM 1316 C CD2 . PHE B 1 25 ? -0.905 7.087 13.023 1.00 28.38 ? 25 PHE B CD2 1 ATOM 1317 C CE1 . PHE B 1 25 ? -1.492 7.586 10.355 1.00 23.13 ? 25 PHE B CE1 1 ATOM 1318 C CE2 . PHE B 1 25 ? 0.186 7.275 12.087 1.00 23.48 ? 25 PHE B CE2 1 ATOM 1319 C CZ . PHE B 1 25 ? -0.130 7.524 10.767 1.00 21.54 ? 25 PHE B CZ 1 ATOM 1320 N N . THR B 1 26 ? -6.047 8.302 15.315 1.00 33.84 ? 26 THR B N 1 ATOM 1321 C CA . THR B 1 26 ? -7.133 7.973 16.245 1.00 36.75 ? 26 THR B CA 1 ATOM 1322 C C . THR B 1 26 ? -8.388 7.595 15.449 1.00 38.47 ? 26 THR B C 1 ATOM 1323 O O . THR B 1 26 ? -8.803 8.291 14.517 1.00 38.07 ? 26 THR B O 1 ATOM 1324 C CB . THR B 1 26 ? -7.344 9.107 17.296 1.00 36.47 ? 26 THR B CB 1 ATOM 1325 O OG1 . THR B 1 26 ? -8.614 8.948 17.979 1.00 40.84 ? 26 THR B OG1 1 ATOM 1326 C CG2 . THR B 1 26 ? -7.380 10.402 16.641 1.00 39.77 ? 26 THR B CG2 1 ATOM 1327 N N . GLN B 1 27 ? -8.957 6.446 15.759 1.00 41.70 ? 27 GLN B N 1 ATOM 1328 C CA . GLN B 1 27 ? -10.048 5.956 14.956 1.00 45.36 ? 27 GLN B CA 1 ATOM 1329 C C . GLN B 1 27 ? -11.314 6.725 15.358 1.00 47.64 ? 27 GLN B C 1 ATOM 1330 O O . GLN B 1 27 ? -11.736 6.671 16.506 1.00 47.53 ? 27 GLN B O 1 ATOM 1331 C CB . GLN B 1 27 ? -10.192 4.450 15.121 1.00 45.47 ? 27 GLN B CB 1 ATOM 1332 C CG . GLN B 1 27 ? -11.187 3.823 14.183 1.00 47.56 ? 27 GLN B CG 1 ATOM 1333 C CD . GLN B 1 27 ? -10.580 3.079 13.022 1.00 46.61 ? 27 GLN B CD 1 ATOM 1334 O OE1 . GLN B 1 27 ? -10.986 3.269 11.898 1.00 49.72 ? 27 GLN B OE1 1 ATOM 1335 N NE2 . GLN B 1 27 ? -9.670 2.168 13.299 1.00 48.43 ? 27 GLN B NE2 1 ATOM 1336 N N . VAL B 1 28 ? -11.871 7.489 14.412 1.00 50.41 ? 28 VAL B N 1 ATOM 1337 C CA . VAL B 1 28 ? -13.048 8.346 14.693 1.00 53.59 ? 28 VAL B CA 1 ATOM 1338 C C . VAL B 1 28 ? -14.357 7.848 14.026 1.00 55.65 ? 28 VAL B C 1 ATOM 1339 O O . VAL B 1 28 ? -14.632 6.640 13.998 1.00 56.19 ? 28 VAL B O 1 ATOM 1340 C CB . VAL B 1 28 ? -12.775 9.901 14.414 1.00 52.93 ? 28 VAL B CB 1 ATOM 1341 C CG1 . VAL B 1 28 ? -11.661 10.452 15.305 1.00 52.23 ? 28 VAL B CG1 1 ATOM 1342 C CG2 . VAL B 1 28 ? -12.443 10.172 12.959 1.00 53.69 ? 28 VAL B CG2 1 ATOM 1343 N N . GLN B 1 29 ? -15.153 8.829 13.575 1.00 58.16 ? 29 GLN B N 1 ATOM 1344 C CA . GLN B 1 29 ? -16.343 8.775 12.658 1.00 60.01 ? 29 GLN B CA 1 ATOM 1345 C C . GLN B 1 29 ? -16.965 7.495 12.055 1.00 60.31 ? 29 GLN B C 1 ATOM 1346 O O . GLN B 1 29 ? -17.056 6.416 12.690 1.00 60.52 ? 29 GLN B O 1 ATOM 1347 C CB . GLN B 1 29 ? -16.139 9.791 11.504 1.00 60.10 ? 29 GLN B CB 1 ATOM 1348 C CG . GLN B 1 29 ? -16.208 11.282 11.947 1.00 62.80 ? 29 GLN B CG 1 ATOM 1349 C CD . GLN B 1 29 ? -17.640 11.850 11.975 1.00 64.08 ? 29 GLN B CD 1 ATOM 1350 O OE1 . GLN B 1 29 ? -17.917 12.894 11.375 1.00 65.28 ? 29 GLN B OE1 1 ATOM 1351 N NE2 . GLN B 1 29 ? -18.544 11.170 12.681 1.00 64.77 ? 29 GLN B NE2 1 ATOM 1352 N N . ASP B 1 30 ? -17.451 7.703 10.825 1.00 60.34 ? 30 ASP B N 1 ATOM 1353 C CA . ASP B 1 30 ? -17.933 6.655 9.929 1.00 59.80 ? 30 ASP B CA 1 ATOM 1354 C C . ASP B 1 30 ? -16.740 5.945 9.286 1.00 58.43 ? 30 ASP B C 1 ATOM 1355 O O . ASP B 1 30 ? -16.428 6.177 8.093 1.00 58.98 ? 30 ASP B O 1 ATOM 1356 C CB . ASP B 1 30 ? -18.823 7.277 8.842 1.00 60.36 ? 30 ASP B CB 1 ATOM 1357 C CG . ASP B 1 30 ? -19.516 6.221 7.957 1.00 62.76 ? 30 ASP B CG 1 ATOM 1358 O OD1 . ASP B 1 30 ? -20.265 6.623 7.013 1.00 60.79 ? 30 ASP B OD1 1 ATOM 1359 O OD2 . ASP B 1 30 ? -19.303 4.993 8.206 1.00 65.09 ? 30 ASP B OD2 1 ATOM 1360 N N . GLY B 1 31 ? -16.079 5.089 10.078 1.00 56.26 ? 31 GLY B N 1 ATOM 1361 C CA . GLY B 1 31 ? -14.825 4.406 9.675 1.00 53.26 ? 31 GLY B CA 1 ATOM 1362 C C . GLY B 1 31 ? -13.703 5.335 9.210 1.00 50.86 ? 31 GLY B C 1 ATOM 1363 O O . GLY B 1 31 ? -13.115 5.108 8.135 1.00 51.18 ? 31 GLY B O 1 ATOM 1364 N N . LYS B 1 32 ? -13.417 6.378 10.001 1.00 47.40 ? 32 LYS B N 1 ATOM 1365 C CA . LYS B 1 32 ? -12.419 7.392 9.623 1.00 45.38 ? 32 LYS B CA 1 ATOM 1366 C C . LYS B 1 32 ? -11.298 7.528 10.648 1.00 41.10 ? 32 LYS B C 1 ATOM 1367 O O . LYS B 1 32 ? -11.530 7.344 11.815 1.00 42.04 ? 32 LYS B O 1 ATOM 1368 C CB . LYS B 1 32 ? -13.064 8.761 9.290 1.00 45.43 ? 32 LYS B CB 1 ATOM 1369 C CG . LYS B 1 32 ? -13.756 8.770 7.844 1.00 48.00 ? 32 LYS B CG 1 ATOM 1370 C CD . LYS B 1 32 ? -14.100 10.182 7.312 1.00 48.31 ? 32 LYS B CD 1 ATOM 1371 C CE . LYS B 1 32 ? -15.602 10.431 7.150 1.00 51.78 ? 32 LYS B CE 1 ATOM 1372 N NZ . LYS B 1 32 ? -16.302 10.527 8.468 1.00 58.11 ? 32 LYS B NZ 1 ATOM 1373 N N . VAL B 1 33 ? -10.085 7.830 10.190 1.00 37.02 ? 33 VAL B N 1 ATOM 1374 C CA . VAL B 1 33 ? -8.935 8.031 11.095 1.00 31.81 ? 33 VAL B CA 1 ATOM 1375 C C . VAL B 1 33 ? -8.486 9.482 11.093 1.00 28.86 ? 33 VAL B C 1 ATOM 1376 O O . VAL B 1 33 ? -8.245 10.085 10.070 1.00 26.69 ? 33 VAL B O 1 ATOM 1377 C CB . VAL B 1 33 ? -7.751 7.062 10.761 1.00 31.64 ? 33 VAL B CB 1 ATOM 1378 C CG1 . VAL B 1 33 ? -6.559 7.205 11.757 1.00 29.79 ? 33 VAL B CG1 1 ATOM 1379 C CG2 . VAL B 1 33 ? -8.216 5.670 10.769 1.00 27.79 ? 33 VAL B CG2 1 ATOM 1380 N N . HIS B 1 34 ? -8.353 10.019 12.286 1.00 27.45 ? 34 HIS B N 1 ATOM 1381 C CA . HIS B 1 34 ? -7.857 11.369 12.470 1.00 26.04 ? 34 HIS B CA 1 ATOM 1382 C C . HIS B 1 34 ? -6.330 11.352 12.745 1.00 25.76 ? 34 HIS B C 1 ATOM 1383 O O . HIS B 1 34 ? -5.860 10.786 13.778 1.00 24.06 ? 34 HIS B O 1 ATOM 1384 C CB . HIS B 1 34 ? -8.620 11.997 13.609 1.00 25.27 ? 34 HIS B CB 1 ATOM 1385 C CG . HIS B 1 34 ? -8.293 13.437 13.838 1.00 26.68 ? 34 HIS B CG 1 ATOM 1386 N ND1 . HIS B 1 34 ? -7.774 14.255 12.846 1.00 27.58 ? 34 HIS B ND1 1 ATOM 1387 C CD2 . HIS B 1 34 ? -8.444 14.213 14.931 1.00 24.92 ? 34 HIS B CD2 1 ATOM 1388 C CE1 . HIS B 1 34 ? -7.576 15.462 13.344 1.00 26.59 ? 34 HIS B CE1 1 ATOM 1389 N NE2 . HIS B 1 34 ? -7.990 15.465 14.600 1.00 30.31 ? 34 HIS B NE2 1 ATOM 1390 N N . VAL B 1 35 ? -5.572 11.946 11.801 1.00 26.36 ? 35 VAL B N 1 ATOM 1391 C CA . VAL B 1 35 ? -4.097 11.920 11.817 1.00 24.83 ? 35 VAL B CA 1 ATOM 1392 C C . VAL B 1 35 ? -3.673 13.265 12.307 1.00 25.75 ? 35 VAL B C 1 ATOM 1393 O O . VAL B 1 35 ? -4.034 14.238 11.692 1.00 27.55 ? 35 VAL B O 1 ATOM 1394 C CB . VAL B 1 35 ? -3.495 11.691 10.422 1.00 25.25 ? 35 VAL B CB 1 ATOM 1395 C CG1 . VAL B 1 35 ? -1.910 11.663 10.508 1.00 22.94 ? 35 VAL B CG1 1 ATOM 1396 C CG2 . VAL B 1 35 ? -4.039 10.366 9.749 1.00 23.72 ? 35 VAL B CG2 1 ATOM 1397 N N . GLN B 1 36 ? -2.932 13.339 13.398 1.00 25.15 ? 36 GLN B N 1 ATOM 1398 C CA . GLN B 1 36 ? -2.488 14.591 13.971 1.00 26.53 ? 36 GLN B CA 1 ATOM 1399 C C . GLN B 1 36 ? -1.006 14.478 14.236 1.00 27.77 ? 36 GLN B C 1 ATOM 1400 O O . GLN B 1 36 ? -0.462 13.388 14.400 1.00 29.03 ? 36 GLN B O 1 ATOM 1401 C CB . GLN B 1 36 ? -3.195 14.866 15.334 1.00 27.14 ? 36 GLN B CB 1 ATOM 1402 C CG . GLN B 1 36 ? -4.662 15.094 15.146 1.00 27.79 ? 36 GLN B CG 1 ATOM 1403 C CD . GLN B 1 36 ? -5.390 15.320 16.463 1.00 34.94 ? 36 GLN B CD 1 ATOM 1404 O OE1 . GLN B 1 36 ? -5.622 16.464 16.876 1.00 34.90 ? 36 GLN B OE1 1 ATOM 1405 N NE2 . GLN B 1 36 ? -5.780 14.243 17.098 1.00 34.50 ? 36 GLN B NE2 1 ATOM 1406 N N . GLY B 1 37 ? -0.309 15.580 14.284 1.00 28.22 ? 37 GLY B N 1 ATOM 1407 C CA . GLY B 1 37 ? 1.105 15.415 14.575 1.00 26.63 ? 37 GLY B CA 1 ATOM 1408 C C . GLY B 1 37 ? 1.813 16.710 14.394 1.00 25.66 ? 37 GLY B C 1 ATOM 1409 O O . GLY B 1 37 ? 1.217 17.686 13.936 1.00 22.48 ? 37 GLY B O 1 ATOM 1410 N N . GLY B 1 38 ? 3.081 16.694 14.765 1.00 23.73 ? 38 GLY B N 1 ATOM 1411 C CA . GLY B 1 38 ? 3.936 17.808 14.494 1.00 25.08 ? 38 GLY B CA 1 ATOM 1412 C C . GLY B 1 38 ? 5.304 17.247 14.216 1.00 24.14 ? 38 GLY B C 1 ATOM 1413 O O . GLY B 1 38 ? 5.698 16.252 14.861 1.00 25.97 ? 38 GLY B O 1 ATOM 1414 N N . ILE B 1 39 ? 5.997 17.855 13.270 1.00 21.38 ? 39 ILE B N 1 ATOM 1415 C CA . ILE B 1 39 ? 7.385 17.511 12.912 1.00 20.45 ? 39 ILE B CA 1 ATOM 1416 C C . ILE B 1 39 ? 8.167 18.774 12.792 1.00 20.42 ? 39 ILE B C 1 ATOM 1417 O O . ILE B 1 39 ? 7.626 19.792 12.294 1.00 19.63 ? 39 ILE B O 1 ATOM 1418 C CB . ILE B 1 39 ? 7.420 16.754 11.501 1.00 19.73 ? 39 ILE B CB 1 ATOM 1419 C CG1 . ILE B 1 39 ? 6.297 15.693 11.436 1.00 23.04 ? 39 ILE B CG1 1 ATOM 1420 C CG2 . ILE B 1 39 ? 8.742 16.002 11.265 1.00 16.68 ? 39 ILE B CG2 1 ATOM 1421 C CD1 . ILE B 1 39 ? 5.993 15.077 9.936 1.00 19.71 ? 39 ILE B CD1 1 ATOM 1422 N N . THR B 1 40 ? 9.439 18.736 13.198 1.00 19.71 ? 40 THR B N 1 ATOM 1423 C CA . THR B 1 40 ? 10.395 19.752 12.812 1.00 21.36 ? 40 THR B CA 1 ATOM 1424 C C . THR B 1 40 ? 11.536 19.184 11.918 1.00 20.52 ? 40 THR B C 1 ATOM 1425 O O . THR B 1 40 ? 11.883 17.987 12.013 1.00 21.00 ? 40 THR B O 1 ATOM 1426 C CB . THR B 1 40 ? 11.037 20.464 14.071 1.00 21.44 ? 40 THR B CB 1 ATOM 1427 O OG1 . THR B 1 40 ? 11.588 19.474 14.945 1.00 23.07 ? 40 THR B OG1 1 ATOM 1428 C CG2 . THR B 1 40 ? 9.982 21.181 14.848 1.00 23.64 ? 40 THR B CG2 1 ATOM 1429 N N . GLY B 1 41 ? 12.121 20.031 11.102 1.00 18.02 ? 41 GLY B N 1 ATOM 1430 C CA . GLY B 1 41 ? 13.440 19.758 10.603 1.00 20.58 ? 41 GLY B CA 1 ATOM 1431 C C . GLY B 1 41 ? 13.607 19.938 9.101 1.00 21.96 ? 41 GLY B C 1 ATOM 1432 O O . GLY B 1 41 ? 14.673 19.674 8.557 1.00 22.45 ? 41 GLY B O 1 ATOM 1433 N N . LEU B 1 42 ? 12.542 20.326 8.405 1.00 21.90 ? 42 LEU B N 1 ATOM 1434 C CA . LEU B 1 42 ? 12.655 20.583 7.002 1.00 22.78 ? 42 LEU B CA 1 ATOM 1435 C C . LEU B 1 42 ? 12.301 22.033 6.684 1.00 23.16 ? 42 LEU B C 1 ATOM 1436 O O . LEU B 1 42 ? 11.385 22.609 7.314 1.00 24.61 ? 42 LEU B O 1 ATOM 1437 C CB . LEU B 1 42 ? 11.789 19.571 6.173 1.00 21.94 ? 42 LEU B CB 1 ATOM 1438 C CG . LEU B 1 42 ? 12.323 18.135 5.965 1.00 24.61 ? 42 LEU B CG 1 ATOM 1439 C CD1 . LEU B 1 42 ? 11.175 17.250 5.426 1.00 26.98 ? 42 LEU B CD1 1 ATOM 1440 C CD2 . LEU B 1 42 ? 13.571 17.910 5.044 1.00 22.64 ? 42 LEU B CD2 1 ATOM 1441 N N . PRO B 1 43 ? 12.963 22.606 5.687 1.00 22.87 ? 43 PRO B N 1 ATOM 1442 C CA . PRO B 1 43 ? 12.684 23.970 5.187 1.00 24.28 ? 43 PRO B CA 1 ATOM 1443 C C . PRO B 1 43 ? 11.194 24.118 4.741 1.00 24.03 ? 43 PRO B C 1 ATOM 1444 O O . PRO B 1 43 ? 10.517 23.075 4.532 1.00 25.12 ? 43 PRO B O 1 ATOM 1445 C CB . PRO B 1 43 ? 13.633 24.120 3.932 1.00 23.83 ? 43 PRO B CB 1 ATOM 1446 C CG . PRO B 1 43 ? 14.337 22.889 3.732 1.00 23.69 ? 43 PRO B CG 1 ATOM 1447 C CD . PRO B 1 43 ? 14.017 21.908 4.902 1.00 24.22 ? 43 PRO B CD 1 ATOM 1448 N N . PRO B 1 44 ? 10.660 25.364 4.651 1.00 24.67 ? 44 PRO B N 1 ATOM 1449 C CA . PRO B 1 44 ? 9.231 25.547 4.227 1.00 24.57 ? 44 PRO B CA 1 ATOM 1450 C C . PRO B 1 44 ? 8.938 24.869 2.907 1.00 25.19 ? 44 PRO B C 1 ATOM 1451 O O . PRO B 1 44 ? 9.776 24.872 1.998 1.00 25.91 ? 44 PRO B O 1 ATOM 1452 C CB . PRO B 1 44 ? 9.043 27.061 4.087 1.00 23.95 ? 44 PRO B CB 1 ATOM 1453 C CG . PRO B 1 44 ? 10.251 27.670 4.672 1.00 24.16 ? 44 PRO B CG 1 ATOM 1454 C CD . PRO B 1 44 ? 11.307 26.630 4.984 1.00 24.89 ? 44 PRO B CD 1 ATOM 1455 N N . GLY B 1 45 ? 7.780 24.227 2.808 1.00 26.30 ? 45 GLY B N 1 ATOM 1456 C CA . GLY B 1 45 ? 7.412 23.546 1.544 1.00 26.30 ? 45 GLY B CA 1 ATOM 1457 C C . GLY B 1 45 ? 6.604 22.302 1.795 1.00 25.26 ? 45 GLY B C 1 ATOM 1458 O O . GLY B 1 45 ? 6.245 22.054 2.937 1.00 24.61 ? 45 GLY B O 1 ATOM 1459 N N . GLU B 1 46 ? 6.342 21.520 0.737 1.00 25.89 ? 46 GLU B N 1 ATOM 1460 C CA . GLU B 1 46 ? 5.489 20.322 0.805 1.00 26.86 ? 46 GLU B CA 1 ATOM 1461 C C . GLU B 1 46 ? 6.306 19.044 0.575 1.00 25.40 ? 46 GLU B C 1 ATOM 1462 O O . GLU B 1 46 ? 7.262 19.013 -0.265 1.00 23.10 ? 46 GLU B O 1 ATOM 1463 C CB . GLU B 1 46 ? 4.328 20.395 -0.188 1.00 27.68 ? 46 GLU B CB 1 ATOM 1464 C CG . GLU B 1 46 ? 3.228 21.429 0.255 1.00 32.80 ? 46 GLU B CG 1 ATOM 1465 C CD . GLU B 1 46 ? 1.991 21.467 -0.668 1.00 33.75 ? 46 GLU B CD 1 ATOM 1466 O OE1 . GLU B 1 46 ? 1.800 20.507 -1.477 1.00 36.08 ? 46 GLU B OE1 1 ATOM 1467 O OE2 . GLU B 1 46 ? 1.225 22.493 -0.599 1.00 40.86 ? 46 GLU B OE2 1 ATOM 1468 N N . TYR B 1 47 ? 5.959 18.006 1.336 1.00 21.65 ? 47 TYR B N 1 ATOM 1469 C CA . TYR B 1 47 ? 6.821 16.795 1.360 1.00 22.82 ? 47 TYR B CA 1 ATOM 1470 C C . TYR B 1 47 ? 5.915 15.623 1.379 1.00 21.12 ? 47 TYR B C 1 ATOM 1471 O O . TYR B 1 47 ? 4.928 15.627 2.132 1.00 20.29 ? 47 TYR B O 1 ATOM 1472 C CB . TYR B 1 47 ? 7.772 16.767 2.572 1.00 23.38 ? 47 TYR B CB 1 ATOM 1473 C CG . TYR B 1 47 ? 8.728 17.951 2.606 1.00 24.61 ? 47 TYR B CG 1 ATOM 1474 C CD1 . TYR B 1 47 ? 8.332 19.162 3.187 1.00 27.86 ? 47 TYR B CD1 1 ATOM 1475 C CD2 . TYR B 1 47 ? 10.000 17.885 2.010 1.00 23.94 ? 47 TYR B CD2 1 ATOM 1476 C CE1 . TYR B 1 47 ? 9.172 20.268 3.216 1.00 26.24 ? 47 TYR B CE1 1 ATOM 1477 C CE2 . TYR B 1 47 ? 10.861 18.983 2.045 1.00 27.11 ? 47 TYR B CE2 1 ATOM 1478 C CZ . TYR B 1 47 ? 10.407 20.185 2.623 1.00 25.82 ? 47 TYR B CZ 1 ATOM 1479 O OH . TYR B 1 47 ? 11.211 21.276 2.694 1.00 30.26 ? 47 TYR B OH 1 ATOM 1480 N N . GLY B 1 48 ? 6.204 14.650 0.515 1.00 20.15 ? 48 GLY B N 1 ATOM 1481 C CA . GLY B 1 48 ? 5.400 13.436 0.431 1.00 21.01 ? 48 GLY B CA 1 ATOM 1482 C C . GLY B 1 48 ? 5.300 12.698 1.764 1.00 22.57 ? 48 GLY B C 1 ATOM 1483 O O . GLY B 1 48 ? 6.298 12.537 2.467 1.00 23.72 ? 48 GLY B O 1 ATOM 1484 N N . PHE B 1 49 ? 4.106 12.270 2.131 1.00 23.58 ? 49 PHE B N 1 ATOM 1485 C CA . PHE B 1 49 ? 3.921 11.605 3.424 1.00 25.66 ? 49 PHE B CA 1 ATOM 1486 C C . PHE B 1 49 ? 3.036 10.374 3.199 1.00 25.45 ? 49 PHE B C 1 ATOM 1487 O O . PHE B 1 49 ? 1.893 10.523 2.761 1.00 25.79 ? 49 PHE B O 1 ATOM 1488 C CB . PHE B 1 49 ? 3.258 12.574 4.360 1.00 28.73 ? 49 PHE B CB 1 ATOM 1489 C CG . PHE B 1 49 ? 3.139 12.075 5.769 1.00 33.37 ? 49 PHE B CG 1 ATOM 1490 C CD1 . PHE B 1 49 ? 1.892 12.086 6.410 1.00 37.20 ? 49 PHE B CD1 1 ATOM 1491 C CD2 . PHE B 1 49 ? 4.262 11.634 6.457 1.00 37.09 ? 49 PHE B CD2 1 ATOM 1492 C CE1 . PHE B 1 49 ? 1.761 11.631 7.720 1.00 38.00 ? 49 PHE B CE1 1 ATOM 1493 C CE2 . PHE B 1 49 ? 4.146 11.186 7.770 1.00 42.24 ? 49 PHE B CE2 1 ATOM 1494 C CZ . PHE B 1 49 ? 2.885 11.174 8.400 1.00 38.42 ? 49 PHE B CZ 1 ATOM 1495 N N . HIS B 1 50 ? 3.569 9.160 3.399 1.00 22.98 ? 50 HIS B N 1 ATOM 1496 C CA . HIS B 1 50 ? 2.791 7.942 3.071 1.00 22.96 ? 50 HIS B CA 1 ATOM 1497 C C . HIS B 1 50 ? 2.913 6.856 4.108 1.00 22.51 ? 50 HIS B C 1 ATOM 1498 O O . HIS B 1 50 ? 3.901 6.795 4.794 1.00 19.11 ? 50 HIS B O 1 ATOM 1499 C CB . HIS B 1 50 ? 3.250 7.301 1.740 1.00 23.71 ? 50 HIS B CB 1 ATOM 1500 C CG . HIS B 1 50 ? 3.632 8.296 0.693 1.00 24.45 ? 50 HIS B CG 1 ATOM 1501 N ND1 . HIS B 1 50 ? 4.821 8.205 0.000 1.00 28.96 ? 50 HIS B ND1 1 ATOM 1502 C CD2 . HIS B 1 50 ? 3.017 9.422 0.263 1.00 24.80 ? 50 HIS B CD2 1 ATOM 1503 C CE1 . HIS B 1 50 ? 4.889 9.205 -0.857 1.00 27.18 ? 50 HIS B CE1 1 ATOM 1504 N NE2 . HIS B 1 50 ? 3.821 9.976 -0.703 1.00 28.33 ? 50 HIS B NE2 1 ATOM 1505 N N . VAL B 1 51 ? 1.927 5.959 4.150 1.00 22.93 ? 51 VAL B N 1 ATOM 1506 C CA . VAL B 1 51 ? 2.067 4.718 4.941 1.00 23.27 ? 51 VAL B CA 1 ATOM 1507 C C . VAL B 1 51 ? 2.612 3.684 3.939 1.00 23.53 ? 51 VAL B C 1 ATOM 1508 O O . VAL B 1 51 ? 1.970 3.418 2.881 1.00 22.47 ? 51 VAL B O 1 ATOM 1509 C CB . VAL B 1 51 ? 0.714 4.224 5.514 1.00 22.71 ? 51 VAL B CB 1 ATOM 1510 C CG1 . VAL B 1 51 ? 0.892 2.891 6.256 1.00 23.04 ? 51 VAL B CG1 1 ATOM 1511 C CG2 . VAL B 1 51 ? 0.109 5.321 6.403 1.00 23.18 ? 51 VAL B CG2 1 ATOM 1512 N N . HIS B 1 52 ? 3.797 3.147 4.246 1.00 22.24 ? 52 HIS B N 1 ATOM 1513 C CA . HIS B 1 52 ? 4.422 2.175 3.357 1.00 23.47 ? 52 HIS B CA 1 ATOM 1514 C C . HIS B 1 52 ? 4.054 0.824 3.948 1.00 25.07 ? 52 HIS B C 1 ATOM 1515 O O . HIS B 1 52 ? 3.583 0.762 5.084 1.00 25.46 ? 52 HIS B O 1 ATOM 1516 C CB . HIS B 1 52 ? 5.916 2.399 3.287 1.00 21.31 ? 52 HIS B CB 1 ATOM 1517 C CG . HIS B 1 52 ? 6.321 3.497 2.361 1.00 23.08 ? 52 HIS B CG 1 ATOM 1518 N ND1 . HIS B 1 52 ? 7.302 3.334 1.394 1.00 24.97 ? 52 HIS B ND1 1 ATOM 1519 C CD2 . HIS B 1 52 ? 5.925 4.788 2.268 1.00 21.24 ? 52 HIS B CD2 1 ATOM 1520 C CE1 . HIS B 1 52 ? 7.440 4.458 0.713 1.00 20.64 ? 52 HIS B CE1 1 ATOM 1521 N NE2 . HIS B 1 52 ? 6.639 5.364 1.242 1.00 29.52 ? 52 HIS B NE2 1 ATOM 1522 N N . GLU B 1 53 ? 4.212 -0.242 3.161 1.00 25.52 ? 53 GLU B N 1 ATOM 1523 C CA . GLU B 1 53 ? 3.646 -1.567 3.452 1.00 26.65 ? 53 GLU B CA 1 ATOM 1524 C C . GLU B 1 53 ? 4.233 -2.326 4.644 1.00 24.48 ? 53 GLU B C 1 ATOM 1525 O O . GLU B 1 53 ? 3.507 -3.005 5.335 1.00 22.84 ? 53 GLU B O 1 ATOM 1526 C CB . GLU B 1 53 ? 3.790 -2.458 2.203 1.00 25.86 ? 53 GLU B CB 1 ATOM 1527 C CG . GLU B 1 53 ? 3.147 -3.813 2.396 1.00 32.40 ? 53 GLU B CG 1 ATOM 1528 C CD . GLU B 1 53 ? 3.622 -4.838 1.338 1.00 34.23 ? 53 GLU B CD 1 ATOM 1529 O OE1 . GLU B 1 53 ? 2.947 -5.896 1.225 1.00 41.69 ? 53 GLU B OE1 1 ATOM 1530 O OE2 . GLU B 1 53 ? 4.640 -4.573 0.625 1.00 39.84 ? 53 GLU B OE2 1 ATOM 1531 N N . LYS B 1 54 ? 5.539 -2.190 4.875 1.00 24.48 ? 54 LYS B N 1 ATOM 1532 C CA . LYS B 1 54 ? 6.289 -3.008 5.837 1.00 25.73 ? 54 LYS B CA 1 ATOM 1533 C C . LYS B 1 54 ? 6.767 -2.094 6.988 1.00 25.78 ? 54 LYS B C 1 ATOM 1534 O O . LYS B 1 54 ? 7.167 -0.941 6.719 1.00 24.58 ? 54 LYS B O 1 ATOM 1535 C CB . LYS B 1 54 ? 7.561 -3.579 5.169 1.00 26.74 ? 54 LYS B CB 1 ATOM 1536 C CG . LYS B 1 54 ? 7.345 -4.629 4.006 1.00 29.94 ? 54 LYS B CG 1 ATOM 1537 C CD . LYS B 1 54 ? 6.415 -5.751 4.544 1.00 34.52 ? 54 LYS B CD 1 ATOM 1538 C CE . LYS B 1 54 ? 6.090 -6.877 3.512 1.00 37.03 ? 54 LYS B CE 1 ATOM 1539 N NZ . LYS B 1 54 ? 4.997 -7.821 4.070 1.00 38.66 ? 54 LYS B NZ 1 ATOM 1540 N N . GLY B 1 55 ? 6.742 -2.591 8.242 1.00 25.44 ? 55 GLY B N 1 ATOM 1541 C CA . GLY B 1 55 ? 7.351 -1.872 9.383 1.00 25.50 ? 55 GLY B CA 1 ATOM 1542 C C . GLY B 1 55 ? 8.668 -2.515 9.728 1.00 26.95 ? 55 GLY B C 1 ATOM 1543 O O . GLY B 1 55 ? 8.892 -2.905 10.871 1.00 28.32 ? 55 GLY B O 1 ATOM 1544 N N . ASP B 1 56 ? 9.496 -2.698 8.698 1.00 27.22 ? 56 ASP B N 1 ATOM 1545 C CA . ASP B 1 56 ? 10.819 -3.295 8.759 1.00 27.04 ? 56 ASP B CA 1 ATOM 1546 C C . ASP B 1 56 ? 11.850 -2.211 8.529 1.00 27.58 ? 56 ASP B C 1 ATOM 1547 O O . ASP B 1 56 ? 12.037 -1.693 7.383 1.00 28.95 ? 56 ASP B O 1 ATOM 1548 C CB . ASP B 1 56 ? 10.929 -4.326 7.646 1.00 26.98 ? 56 ASP B CB 1 ATOM 1549 C CG . ASP B 1 56 ? 12.337 -4.955 7.522 1.00 29.40 ? 56 ASP B CG 1 ATOM 1550 O OD1 . ASP B 1 56 ? 13.289 -4.609 8.233 1.00 35.34 ? 56 ASP B OD1 1 ATOM 1551 O OD2 . ASP B 1 56 ? 12.475 -5.866 6.702 1.00 32.72 ? 56 ASP B OD2 1 ATOM 1552 N N . LEU B 1 57 ? 12.523 -1.856 9.617 1.00 27.10 ? 57 LEU B N 1 ATOM 1553 C CA . LEU B 1 57 ? 13.526 -0.818 9.621 1.00 27.17 ? 57 LEU B CA 1 ATOM 1554 C C . LEU B 1 57 ? 14.924 -1.391 9.581 1.00 26.47 ? 57 LEU B C 1 ATOM 1555 O O . LEU B 1 57 ? 15.842 -0.657 9.705 1.00 26.60 ? 57 LEU B O 1 ATOM 1556 C CB . LEU B 1 57 ? 13.359 0.068 10.872 1.00 26.33 ? 57 LEU B CB 1 ATOM 1557 C CG . LEU B 1 57 ? 12.554 1.387 10.774 1.00 31.83 ? 57 LEU B CG 1 ATOM 1558 C CD1 . LEU B 1 57 ? 11.375 1.288 9.831 1.00 29.88 ? 57 LEU B CD1 1 ATOM 1559 C CD2 . LEU B 1 57 ? 12.118 1.954 12.161 1.00 30.19 ? 57 LEU B CD2 1 ATOM 1560 N N . SER B 1 58 ? 15.086 -2.689 9.350 1.00 27.58 ? 58 SER B N 1 ATOM 1561 C CA . SER B 1 58 ? 16.424 -3.312 9.377 1.00 29.42 ? 58 SER B CA 1 ATOM 1562 C C . SER B 1 58 ? 17.336 -2.814 8.221 1.00 29.72 ? 58 SER B C 1 ATOM 1563 O O . SER B 1 58 ? 18.539 -2.721 8.365 1.00 28.86 ? 58 SER B O 1 ATOM 1564 C CB . SER B 1 58 ? 16.309 -4.817 9.309 1.00 28.21 ? 58 SER B CB 1 ATOM 1565 O OG . SER B 1 58 ? 15.832 -5.162 8.029 1.00 31.75 ? 58 SER B OG 1 ATOM 1566 N N . GLY B 1 59 ? 16.744 -2.436 7.098 1.00 31.11 ? 59 GLY B N 1 ATOM 1567 C CA . GLY B 1 59 ? 17.530 -1.754 6.071 1.00 32.11 ? 59 GLY B CA 1 ATOM 1568 C C . GLY B 1 59 ? 17.264 -0.268 6.036 1.00 32.20 ? 59 GLY B C 1 ATOM 1569 O O . GLY B 1 59 ? 17.382 0.358 4.963 1.00 32.87 ? 59 GLY B O 1 ATOM 1570 N N . GLY B 1 60 ? 16.882 0.309 7.178 1.00 31.92 ? 60 GLY B N 1 ATOM 1571 C CA . GLY B 1 60 ? 16.520 1.766 7.229 1.00 29.92 ? 60 GLY B CA 1 ATOM 1572 C C . GLY B 1 60 ? 15.199 2.017 6.534 1.00 29.33 ? 60 GLY B C 1 ATOM 1573 O O . GLY B 1 60 ? 14.383 1.118 6.464 1.00 27.93 ? 60 GLY B O 1 ATOM 1574 N N . CYS B 1 61 ? 14.957 3.232 6.017 1.00 29.52 ? 61 CYS B N 1 ATOM 1575 C CA . CYS B 1 61 ? 13.661 3.529 5.405 1.00 29.92 ? 61 CYS B CA 1 ATOM 1576 C C . CYS B 1 61 ? 13.304 2.728 4.149 1.00 29.19 ? 61 CYS B C 1 ATOM 1577 O O . CYS B 1 61 ? 12.120 2.578 3.806 1.00 25.92 ? 61 CYS B O 1 ATOM 1578 C CB . CYS B 1 61 ? 13.550 5.019 5.113 1.00 31.53 ? 61 CYS B CB 1 ATOM 1579 S SG . CYS B 1 61 ? 13.521 5.978 6.671 1.00 36.55 ? 61 CYS B SG 1 ATOM 1580 N N . LEU B 1 62 ? 14.341 2.274 3.437 1.00 29.57 ? 62 LEU B N 1 ATOM 1581 C CA . LEU B 1 62 ? 14.187 1.478 2.215 1.00 30.39 ? 62 LEU B CA 1 ATOM 1582 C C . LEU B 1 62 ? 13.455 0.108 2.397 1.00 29.06 ? 62 LEU B C 1 ATOM 1583 O O . LEU B 1 62 ? 12.658 -0.285 1.526 1.00 28.14 ? 62 LEU B O 1 ATOM 1584 C CB . LEU B 1 62 ? 15.560 1.242 1.616 1.00 32.07 ? 62 LEU B CB 1 ATOM 1585 C CG . LEU B 1 62 ? 15.757 1.450 0.091 1.00 40.45 ? 62 LEU B CG 1 ATOM 1586 C CD1 . LEU B 1 62 ? 15.211 0.276 -0.787 1.00 43.63 ? 62 LEU B CD1 1 ATOM 1587 C CD2 . LEU B 1 62 ? 15.263 2.828 -0.446 1.00 43.21 ? 62 LEU B CD2 1 ATOM 1588 N N . SER B 1 63 ? 13.716 -0.606 3.505 1.00 26.91 ? 63 SER B N 1 ATOM 1589 C CA . SER B 1 63 ? 13.002 -1.889 3.775 1.00 25.83 ? 63 SER B CA 1 ATOM 1590 C C . SER B 1 63 ? 11.514 -1.754 4.169 1.00 26.56 ? 63 SER B C 1 ATOM 1591 O O . SER B 1 63 ? 10.839 -2.773 4.402 1.00 27.80 ? 63 SER B O 1 ATOM 1592 C CB . SER B 1 63 ? 13.747 -2.695 4.861 1.00 26.02 ? 63 SER B CB 1 ATOM 1593 O OG . SER B 1 63 ? 14.154 -1.859 5.934 1.00 25.86 ? 63 SER B OG 1 ATOM 1594 N N . THR B 1 64 ? 10.999 -0.525 4.288 1.00 24.15 ? 64 THR B N 1 ATOM 1595 C CA . THR B 1 64 ? 9.577 -0.347 4.493 1.00 24.69 ? 64 THR B CA 1 ATOM 1596 C C . THR B 1 64 ? 8.704 -0.660 3.228 1.00 24.85 ? 64 THR B C 1 ATOM 1597 O O . THR B 1 64 ? 7.440 -0.760 3.313 1.00 24.24 ? 64 THR B O 1 ATOM 1598 C CB . THR B 1 64 ? 9.268 1.048 5.070 1.00 25.92 ? 64 THR B CB 1 ATOM 1599 O OG1 . THR B 1 64 ? 9.580 2.028 4.087 1.00 25.06 ? 64 THR B OG1 1 ATOM 1600 C CG2 . THR B 1 64 ? 10.109 1.335 6.309 1.00 20.69 ? 64 THR B CG2 1 ATOM 1601 N N . GLY B 1 65 ? 9.363 -0.929 2.098 1.00 22.79 ? 65 GLY B N 1 ATOM 1602 C CA . GLY B 1 65 ? 8.621 -1.390 0.924 1.00 21.38 ? 65 GLY B CA 1 ATOM 1603 C C . GLY B 1 65 ? 8.043 -0.184 0.209 1.00 21.75 ? 65 GLY B C 1 ATOM 1604 O O . GLY B 1 65 ? 8.601 0.939 0.278 1.00 21.98 ? 65 GLY B O 1 ATOM 1605 N N . SER B 1 66 ? 6.955 -0.388 -0.509 1.00 21.80 ? 66 SER B N 1 ATOM 1606 C CA . SER B 1 66 ? 6.353 0.678 -1.285 1.00 24.52 ? 66 SER B CA 1 ATOM 1607 C C . SER B 1 66 ? 5.088 1.144 -0.583 1.00 23.55 ? 66 SER B C 1 ATOM 1608 O O . SER B 1 66 ? 4.795 0.704 0.542 1.00 23.33 ? 66 SER B O 1 ATOM 1609 C CB . SER B 1 66 ? 6.036 0.144 -2.677 1.00 26.08 ? 66 SER B CB 1 ATOM 1610 O OG . SER B 1 66 ? 5.283 -1.060 -2.522 1.00 30.63 ? 66 SER B OG 1 ATOM 1611 N N . HIS B 1 67 ? 4.334 2.039 -1.212 1.00 23.31 ? 67 HIS B N 1 ATOM 1612 C CA . HIS B 1 67 ? 3.130 2.571 -0.588 1.00 24.22 ? 67 HIS B CA 1 ATOM 1613 C C . HIS B 1 67 ? 2.175 1.419 -0.202 1.00 24.47 ? 67 HIS B C 1 ATOM 1614 O O . HIS B 1 67 ? 1.995 0.525 -0.989 1.00 25.33 ? 67 HIS B O 1 ATOM 1615 C CB . HIS B 1 67 ? 2.458 3.636 -1.504 1.00 22.85 ? 67 HIS B CB 1 ATOM 1616 C CG . HIS B 1 67 ? 3.321 4.825 -1.732 1.00 25.59 ? 67 HIS B CG 1 ATOM 1617 N ND1 . HIS B 1 67 ? 3.024 5.856 -2.634 1.00 26.48 ? 67 HIS B ND1 1 ATOM 1618 C CD2 . HIS B 1 67 ? 4.513 5.126 -1.151 1.00 25.93 ? 67 HIS B CD2 1 ATOM 1619 C CE1 . HIS B 1 67 ? 4.053 6.714 -2.567 1.00 25.54 ? 67 HIS B CE1 1 ATOM 1620 N NE2 . HIS B 1 67 ? 4.918 6.348 -1.611 1.00 30.40 ? 67 HIS B NE2 1 ATOM 1621 N N . PHE B 1 68 ? 1.487 1.490 0.954 1.00 25.86 ? 68 PHE B N 1 ATOM 1622 C CA . PHE B 1 68 ? 0.601 0.427 1.344 1.00 25.40 ? 68 PHE B CA 1 ATOM 1623 C C . PHE B 1 68 ? -0.606 0.440 0.377 1.00 27.58 ? 68 PHE B C 1 ATOM 1624 O O . PHE B 1 68 ? -1.271 1.489 0.161 1.00 26.81 ? 68 PHE B O 1 ATOM 1625 C CB . PHE B 1 68 ? 0.183 0.605 2.769 1.00 24.70 ? 68 PHE B CB 1 ATOM 1626 C CG . PHE B 1 68 ? -0.804 -0.396 3.246 1.00 22.53 ? 68 PHE B CG 1 ATOM 1627 C CD1 . PHE B 1 68 ? -0.587 -1.729 3.060 1.00 23.60 ? 68 PHE B CD1 1 ATOM 1628 C CD2 . PHE B 1 68 ? -1.924 0.008 3.959 1.00 24.79 ? 68 PHE B CD2 1 ATOM 1629 C CE1 . PHE B 1 68 ? -1.528 -2.673 3.505 1.00 25.92 ? 68 PHE B CE1 1 ATOM 1630 C CE2 . PHE B 1 68 ? -2.866 -0.909 4.438 1.00 25.97 ? 68 PHE B CE2 1 ATOM 1631 C CZ . PHE B 1 68 ? -2.666 -2.265 4.217 1.00 26.32 ? 68 PHE B CZ 1 ATOM 1632 N N . ASN B 1 69 ? -0.874 -0.733 -0.215 1.00 27.96 ? 69 ASN B N 1 ATOM 1633 C CA . ASN B 1 69 ? -1.716 -0.798 -1.420 1.00 29.09 ? 69 ASN B CA 1 ATOM 1634 C C . ASN B 1 69 ? -2.486 -2.113 -1.537 1.00 29.14 ? 69 ASN B C 1 ATOM 1635 O O . ASN B 1 69 ? -2.318 -2.822 -2.527 1.00 29.59 ? 69 ASN B O 1 ATOM 1636 C CB . ASN B 1 69 ? -0.831 -0.600 -2.662 1.00 28.56 ? 69 ASN B CB 1 ATOM 1637 C CG . ASN B 1 69 ? -1.656 -0.466 -4.008 1.00 29.28 ? 69 ASN B CG 1 ATOM 1638 O OD1 . ASN B 1 69 ? -1.092 -0.607 -5.114 1.00 30.36 ? 69 ASN B OD1 1 ATOM 1639 N ND2 . ASN B 1 69 ? -2.947 -0.213 -3.902 1.00 24.40 ? 69 ASN B ND2 1 ATOM 1640 N N . PRO B 1 70 ? -3.320 -2.431 -0.542 1.00 29.60 ? 70 PRO B N 1 ATOM 1641 C CA . PRO B 1 70 ? -3.991 -3.707 -0.548 1.00 30.34 ? 70 PRO B CA 1 ATOM 1642 C C . PRO B 1 70 ? -5.041 -3.865 -1.649 1.00 33.58 ? 70 PRO B C 1 ATOM 1643 O O . PRO B 1 70 ? -5.408 -5.031 -1.994 1.00 31.96 ? 70 PRO B O 1 ATOM 1644 C CB . PRO B 1 70 ? -4.710 -3.761 0.809 1.00 30.24 ? 70 PRO B CB 1 ATOM 1645 C CG . PRO B 1 70 ? -4.920 -2.355 1.231 1.00 28.57 ? 70 PRO B CG 1 ATOM 1646 C CD . PRO B 1 70 ? -3.690 -1.617 0.648 1.00 28.18 ? 70 PRO B CD 1 ATOM 1647 N N . GLU B 1 71 ? -5.551 -2.726 -2.145 1.00 34.69 ? 71 GLU B N 1 ATOM 1648 C CA . GLU B 1 71 ? -6.579 -2.728 -3.160 1.00 37.74 ? 71 GLU B CA 1 ATOM 1649 C C . GLU B 1 71 ? -6.025 -2.782 -4.524 1.00 38.56 ? 71 GLU B C 1 ATOM 1650 O O . GLU B 1 71 ? -6.790 -2.813 -5.456 1.00 39.92 ? 71 GLU B O 1 ATOM 1651 C CB . GLU B 1 71 ? -7.457 -1.501 -3.073 1.00 38.56 ? 71 GLU B CB 1 ATOM 1652 C CG . GLU B 1 71 ? -8.782 -1.709 -2.334 1.00 45.15 ? 71 GLU B CG 1 ATOM 1653 C CD . GLU B 1 71 ? -8.614 -2.286 -0.955 1.00 54.07 ? 71 GLU B CD 1 ATOM 1654 O OE1 . GLU B 1 71 ? -7.830 -1.682 -0.160 1.00 60.89 ? 71 GLU B OE1 1 ATOM 1655 O OE2 . GLU B 1 71 ? -9.261 -3.322 -0.659 1.00 54.36 ? 71 GLU B OE2 1 ATOM 1656 N N . HIS B 1 72 ? -4.701 -2.798 -4.649 1.00 39.99 ? 72 HIS B N 1 ATOM 1657 C CA . HIS B 1 72 ? -3.986 -2.789 -5.956 1.00 41.12 ? 72 HIS B CA 1 ATOM 1658 C C . HIS B 1 72 ? -4.447 -1.687 -6.945 1.00 40.94 ? 72 HIS B C 1 ATOM 1659 O O . HIS B 1 72 ? -4.752 -1.958 -8.115 1.00 40.34 ? 72 HIS B O 1 ATOM 1660 C CB . HIS B 1 72 ? -3.937 -4.206 -6.591 1.00 42.59 ? 72 HIS B CB 1 ATOM 1661 C CG . HIS B 1 72 ? -3.610 -5.290 -5.598 1.00 44.74 ? 72 HIS B CG 1 ATOM 1662 N ND1 . HIS B 1 72 ? -2.360 -5.866 -5.502 1.00 49.00 ? 72 HIS B ND1 1 ATOM 1663 C CD2 . HIS B 1 72 ? -4.365 -5.863 -4.631 1.00 48.41 ? 72 HIS B CD2 1 ATOM 1664 C CE1 . HIS B 1 72 ? -2.369 -6.763 -4.530 1.00 49.25 ? 72 HIS B CE1 1 ATOM 1665 N NE2 . HIS B 1 72 ? -3.573 -6.772 -3.979 1.00 48.53 ? 72 HIS B NE2 1 ATOM 1666 N N . LYS B 1 73 ? -4.445 -0.438 -6.454 1.00 39.13 ? 73 LYS B N 1 ATOM 1667 C CA . LYS B 1 73 ? -4.843 0.712 -7.240 1.00 37.25 ? 73 LYS B CA 1 ATOM 1668 C C . LYS B 1 73 ? -3.566 1.408 -7.642 1.00 36.47 ? 73 LYS B C 1 ATOM 1669 O O . LYS B 1 73 ? -2.492 0.933 -7.300 1.00 36.48 ? 73 LYS B O 1 ATOM 1670 C CB . LYS B 1 73 ? -5.792 1.577 -6.422 1.00 36.33 ? 73 LYS B CB 1 ATOM 1671 C CG . LYS B 1 73 ? -7.131 0.881 -6.284 1.00 40.38 ? 73 LYS B CG 1 ATOM 1672 C CD . LYS B 1 73 ? -8.272 1.732 -5.698 1.00 43.78 ? 73 LYS B CD 1 ATOM 1673 C CE . LYS B 1 73 ? -9.652 1.152 -6.063 1.00 45.09 ? 73 LYS B CE 1 ATOM 1674 N NZ . LYS B 1 73 ? -9.831 1.086 -7.566 1.00 49.32 ? 73 LYS B NZ 1 ATOM 1675 N N . ASP B 1 74 ? -3.680 2.503 -8.389 1.00 34.87 ? 74 ASP B N 1 ATOM 1676 C CA . ASP B 1 74 ? -2.542 3.360 -8.732 1.00 34.50 ? 74 ASP B CA 1 ATOM 1677 C C . ASP B 1 74 ? -2.325 4.508 -7.729 1.00 30.90 ? 74 ASP B C 1 ATOM 1678 O O . ASP B 1 74 ? -3.174 4.837 -6.968 1.00 30.34 ? 74 ASP B O 1 ATOM 1679 C CB . ASP B 1 74 ? -2.730 3.931 -10.148 1.00 35.93 ? 74 ASP B CB 1 ATOM 1680 C CG . ASP B 1 74 ? -2.615 2.854 -11.221 1.00 40.79 ? 74 ASP B CG 1 ATOM 1681 O OD1 . ASP B 1 74 ? -1.451 2.481 -11.587 1.00 48.68 ? 74 ASP B OD1 1 ATOM 1682 O OD2 . ASP B 1 74 ? -3.677 2.387 -11.694 1.00 45.91 ? 74 ASP B OD2 1 ATOM 1683 N N . HIS B 1 75 ? -1.187 5.136 -7.798 1.00 30.88 ? 75 HIS B N 1 ATOM 1684 C CA . HIS B 1 75 ? -0.913 6.289 -6.945 1.00 31.20 ? 75 HIS B CA 1 ATOM 1685 C C . HIS B 1 75 ? -1.811 7.483 -7.218 1.00 30.87 ? 75 HIS B C 1 ATOM 1686 O O . HIS B 1 75 ? -1.947 7.900 -8.372 1.00 31.64 ? 75 HIS B O 1 ATOM 1687 C CB . HIS B 1 75 ? 0.553 6.716 -7.038 1.00 30.02 ? 75 HIS B CB 1 ATOM 1688 C CG . HIS B 1 75 ? 0.915 7.769 -6.039 1.00 29.24 ? 75 HIS B CG 1 ATOM 1689 N ND1 . HIS B 1 75 ? 1.066 7.485 -4.702 1.00 20.76 ? 75 HIS B ND1 1 ATOM 1690 C CD2 . HIS B 1 75 ? 1.119 9.106 -6.176 1.00 27.05 ? 75 HIS B CD2 1 ATOM 1691 C CE1 . HIS B 1 75 ? 1.399 8.598 -4.060 1.00 24.31 ? 75 HIS B CE1 1 ATOM 1692 N NE2 . HIS B 1 75 ? 1.432 9.595 -4.928 1.00 25.47 ? 75 HIS B NE2 1 ATOM 1693 N N . GLY B 1 76 ? -2.428 8.040 -6.180 1.00 29.72 ? 76 GLY B N 1 ATOM 1694 C CA . GLY B 1 76 ? -3.187 9.270 -6.400 1.00 29.42 ? 76 GLY B CA 1 ATOM 1695 C C . GLY B 1 76 ? -3.234 10.212 -5.209 1.00 29.30 ? 76 GLY B C 1 ATOM 1696 O O . GLY B 1 76 ? -2.407 10.104 -4.311 1.00 28.99 ? 76 GLY B O 1 ATOM 1697 N N . HIS B 1 77 ? -4.223 11.114 -5.213 1.00 26.94 ? 77 HIS B N 1 ATOM 1698 C CA . HIS B 1 77 ? -4.386 12.115 -4.198 1.00 26.48 ? 77 HIS B CA 1 ATOM 1699 C C . HIS B 1 77 ? -5.336 11.542 -3.117 1.00 26.27 ? 77 HIS B C 1 ATOM 1700 O O . HIS B 1 77 ? -6.263 10.818 -3.451 1.00 24.61 ? 77 HIS B O 1 ATOM 1701 C CB . HIS B 1 77 ? -4.955 13.426 -4.842 1.00 27.32 ? 77 HIS B CB 1 ATOM 1702 C CG . HIS B 1 77 ? -5.125 14.547 -3.859 1.00 25.33 ? 77 HIS B CG 1 ATOM 1703 N ND1 . HIS B 1 77 ? -6.197 14.612 -2.986 1.00 24.77 ? 77 HIS B ND1 1 ATOM 1704 C CD2 . HIS B 1 77 ? -4.339 15.603 -3.567 1.00 24.52 ? 77 HIS B CD2 1 ATOM 1705 C CE1 . HIS B 1 77 ? -6.071 15.681 -2.216 1.00 25.79 ? 77 HIS B CE1 1 ATOM 1706 N NE2 . HIS B 1 77 ? -4.942 16.285 -2.538 1.00 27.82 ? 77 HIS B NE2 1 ATOM 1707 N N . PRO B 1 78 ? -5.123 11.869 -1.827 1.00 26.19 ? 78 PRO B N 1 ATOM 1708 C CA . PRO B 1 78 ? -6.077 11.193 -0.913 1.00 27.96 ? 78 PRO B CA 1 ATOM 1709 C C . PRO B 1 78 ? -7.588 11.369 -1.231 1.00 29.89 ? 78 PRO B C 1 ATOM 1710 O O . PRO B 1 78 ? -8.385 10.537 -0.778 1.00 30.18 ? 78 PRO B O 1 ATOM 1711 C CB . PRO B 1 78 ? -5.701 11.724 0.477 1.00 27.03 ? 78 PRO B CB 1 ATOM 1712 C CG . PRO B 1 78 ? -4.791 12.888 0.199 1.00 27.77 ? 78 PRO B CG 1 ATOM 1713 C CD . PRO B 1 78 ? -4.143 12.691 -1.101 1.00 25.36 ? 78 PRO B CD 1 ATOM 1714 N N . ASN B 1 79 ? -7.989 12.416 -1.980 1.00 30.99 ? 79 ASN B N 1 ATOM 1715 C CA . ASN B 1 79 ? -9.397 12.599 -2.315 1.00 32.63 ? 79 ASN B CA 1 ATOM 1716 C C . ASN B 1 79 ? -9.847 11.752 -3.512 1.00 34.94 ? 79 ASN B C 1 ATOM 1717 O O . ASN B 1 79 ? -11.049 11.681 -3.807 1.00 36.76 ? 79 ASN B O 1 ATOM 1718 C CB . ASN B 1 79 ? -9.737 14.083 -2.558 1.00 33.35 ? 79 ASN B CB 1 ATOM 1719 C CG . ASN B 1 79 ? -9.808 14.875 -1.267 1.00 33.28 ? 79 ASN B CG 1 ATOM 1720 O OD1 . ASN B 1 79 ? -10.112 14.312 -0.224 1.00 31.62 ? 79 ASN B OD1 1 ATOM 1721 N ND2 . ASN B 1 79 ? -9.504 16.173 -1.326 1.00 29.56 ? 79 ASN B ND2 1 ATOM 1722 N N . ASP B 1 80 ? -8.904 11.112 -4.209 1.00 35.03 ? 80 ASP B N 1 ATOM 1723 C CA . ASP B 1 80 ? -9.248 10.259 -5.337 1.00 34.40 ? 80 ASP B CA 1 ATOM 1724 C C . ASP B 1 80 ? -9.801 8.878 -4.964 1.00 35.01 ? 80 ASP B C 1 ATOM 1725 O O . ASP B 1 80 ? -9.415 8.254 -3.953 1.00 34.42 ? 80 ASP B O 1 ATOM 1726 C CB . ASP B 1 80 ? -8.038 10.027 -6.214 1.00 33.41 ? 80 ASP B CB 1 ATOM 1727 C CG . ASP B 1 80 ? -7.481 11.300 -6.816 1.00 35.42 ? 80 ASP B CG 1 ATOM 1728 O OD1 . ASP B 1 80 ? -6.302 11.239 -7.286 1.00 34.89 ? 80 ASP B OD1 1 ATOM 1729 O OD2 . ASP B 1 80 ? -8.185 12.367 -6.840 1.00 35.20 ? 80 ASP B OD2 1 ATOM 1730 N N . VAL B 1 81 ? -10.675 8.363 -5.823 1.00 33.94 ? 81 VAL B N 1 ATOM 1731 C CA . VAL B 1 81 ? -11.072 6.960 -5.720 1.00 34.25 ? 81 VAL B CA 1 ATOM 1732 C C . VAL B 1 81 ? -9.869 6.045 -6.124 1.00 33.75 ? 81 VAL B C 1 ATOM 1733 O O . VAL B 1 81 ? -9.567 5.028 -5.476 1.00 33.46 ? 81 VAL B O 1 ATOM 1734 C CB . VAL B 1 81 ? -12.326 6.670 -6.612 1.00 35.53 ? 81 VAL B CB 1 ATOM 1735 C CG1 . VAL B 1 81 ? -12.580 5.139 -6.721 1.00 35.51 ? 81 VAL B CG1 1 ATOM 1736 C CG2 . VAL B 1 81 ? -13.576 7.437 -6.074 1.00 33.38 ? 81 VAL B CG2 1 ATOM 1737 N N . ASN B 1 82 ? -9.170 6.408 -7.185 1.00 31.59 ? 82 ASN B N 1 ATOM 1738 C CA . ASN B 1 82 ? -8.033 5.588 -7.585 1.00 31.88 ? 82 ASN B CA 1 ATOM 1739 C C . ASN B 1 82 ? -6.722 6.024 -6.866 1.00 31.47 ? 82 ASN B C 1 ATOM 1740 O O . ASN B 1 82 ? -5.999 6.858 -7.388 1.00 31.13 ? 82 ASN B O 1 ATOM 1741 C CB . ASN B 1 82 ? -7.902 5.653 -9.122 1.00 32.12 ? 82 ASN B CB 1 ATOM 1742 C CG . ASN B 1 82 ? -6.800 4.702 -9.712 1.00 34.66 ? 82 ASN B CG 1 ATOM 1743 O OD1 . ASN B 1 82 ? -6.243 4.995 -10.797 1.00 35.85 ? 82 ASN B OD1 1 ATOM 1744 N ND2 . ASN B 1 82 ? -6.541 3.557 -9.055 1.00 31.38 ? 82 ASN B ND2 1 ATOM 1745 N N . ARG B 1 83 ? -6.442 5.475 -5.679 1.00 30.29 ? 83 ARG B N 1 ATOM 1746 C CA . ARG B 1 83 ? -5.218 5.819 -4.868 1.00 29.13 ? 83 ARG B CA 1 ATOM 1747 C C . ARG B 1 83 ? -4.783 4.572 -4.053 1.00 26.25 ? 83 ARG B C 1 ATOM 1748 O O . ARG B 1 83 ? -5.568 3.662 -3.885 1.00 25.57 ? 83 ARG B O 1 ATOM 1749 C CB . ARG B 1 83 ? -5.526 6.955 -3.858 1.00 27.99 ? 83 ARG B CB 1 ATOM 1750 C CG . ARG B 1 83 ? -6.784 6.672 -2.973 1.00 29.67 ? 83 ARG B CG 1 ATOM 1751 C CD . ARG B 1 83 ? -6.905 7.578 -1.731 1.00 30.17 ? 83 ARG B CD 1 ATOM 1752 N NE . ARG B 1 83 ? -6.156 7.131 -0.540 1.00 28.55 ? 83 ARG B NE 1 ATOM 1753 C CZ . ARG B 1 83 ? -6.390 7.626 0.677 1.00 33.34 ? 83 ARG B CZ 1 ATOM 1754 N NH1 . ARG B 1 83 ? -5.731 7.174 1.749 1.00 36.46 ? 83 ARG B NH1 1 ATOM 1755 N NH2 . ARG B 1 83 ? -7.288 8.601 0.833 1.00 29.45 ? 83 ARG B NH2 1 ATOM 1756 N N . HIS B 1 84 ? -3.554 4.566 -3.532 1.00 24.64 ? 84 HIS B N 1 ATOM 1757 C CA . HIS B 1 84 ? -3.126 3.573 -2.550 1.00 23.26 ? 84 HIS B CA 1 ATOM 1758 C C . HIS B 1 84 ? -3.776 3.885 -1.192 1.00 25.36 ? 84 HIS B C 1 ATOM 1759 O O . HIS B 1 84 ? -3.980 5.072 -0.806 1.00 25.89 ? 84 HIS B O 1 ATOM 1760 C CB . HIS B 1 84 ? -1.655 3.678 -2.408 1.00 23.19 ? 84 HIS B CB 1 ATOM 1761 C CG . HIS B 1 84 ? -0.923 3.438 -3.687 1.00 21.90 ? 84 HIS B CG 1 ATOM 1762 N ND1 . HIS B 1 84 ? 0.240 4.091 -4.011 1.00 21.17 ? 84 HIS B ND1 1 ATOM 1763 C CD2 . HIS B 1 84 ? -1.216 2.634 -4.742 1.00 19.33 ? 84 HIS B CD2 1 ATOM 1764 C CE1 . HIS B 1 84 ? 0.698 3.628 -5.162 1.00 17.97 ? 84 HIS B CE1 1 ATOM 1765 N NE2 . HIS B 1 84 ? -0.190 2.751 -5.632 1.00 21.37 ? 84 HIS B NE2 1 ATOM 1766 N N . VAL B 1 85 ? -4.093 2.857 -0.428 1.00 25.05 ? 85 VAL B N 1 ATOM 1767 C CA . VAL B 1 85 ? -4.518 3.130 0.933 1.00 25.27 ? 85 VAL B CA 1 ATOM 1768 C C . VAL B 1 85 ? -3.519 4.052 1.680 1.00 25.73 ? 85 VAL B C 1 ATOM 1769 O O . VAL B 1 85 ? -3.908 4.936 2.473 1.00 25.89 ? 85 VAL B O 1 ATOM 1770 C CB . VAL B 1 85 ? -4.785 1.848 1.720 1.00 25.12 ? 85 VAL B CB 1 ATOM 1771 C CG1 . VAL B 1 85 ? -5.042 2.185 3.139 1.00 24.50 ? 85 VAL B CG1 1 ATOM 1772 C CG2 . VAL B 1 85 ? -6.040 1.138 1.131 1.00 27.99 ? 85 VAL B CG2 1 ATOM 1773 N N . GLY B 1 86 ? -2.245 3.901 1.435 1.00 24.41 ? 86 GLY B N 1 ATOM 1774 C CA . GLY B 1 86 ? -1.339 4.724 2.249 1.00 26.48 ? 86 GLY B CA 1 ATOM 1775 C C . GLY B 1 86 ? -1.020 6.108 1.684 1.00 26.27 ? 86 GLY B C 1 ATOM 1776 O O . GLY B 1 86 ? -0.088 6.745 2.118 1.00 25.18 ? 86 GLY B O 1 ATOM 1777 N N . ASP B 1 87 ? -1.762 6.574 0.670 1.00 27.24 ? 87 ASP B N 1 ATOM 1778 C CA . ASP B 1 87 ? -1.490 7.912 0.110 1.00 26.12 ? 87 ASP B CA 1 ATOM 1779 C C . ASP B 1 87 ? -2.156 8.939 0.980 1.00 26.20 ? 87 ASP B C 1 ATOM 1780 O O . ASP B 1 87 ? -3.372 9.063 0.919 1.00 28.12 ? 87 ASP B O 1 ATOM 1781 C CB . ASP B 1 87 ? -2.125 8.029 -1.234 1.00 25.27 ? 87 ASP B CB 1 ATOM 1782 C CG . ASP B 1 87 ? -1.404 7.214 -2.281 1.00 27.92 ? 87 ASP B CG 1 ATOM 1783 O OD1 . ASP B 1 87 ? -0.224 6.770 -2.077 1.00 23.22 ? 87 ASP B OD1 1 ATOM 1784 O OD2 . ASP B 1 87 ? -2.087 6.972 -3.291 1.00 27.99 ? 87 ASP B OD2 1 ATOM 1785 N N . LEU B 1 88 ? -1.390 9.657 1.789 1.00 25.58 ? 88 LEU B N 1 ATOM 1786 C CA . LEU B 1 88 ? -1.957 10.722 2.655 1.00 26.01 ? 88 LEU B CA 1 ATOM 1787 C C . LEU B 1 88 ? -1.573 12.116 2.124 1.00 25.73 ? 88 LEU B C 1 ATOM 1788 O O . LEU B 1 88 ? -1.769 13.131 2.805 1.00 26.13 ? 88 LEU B O 1 ATOM 1789 C CB . LEU B 1 88 ? -1.468 10.552 4.093 1.00 25.34 ? 88 LEU B CB 1 ATOM 1790 C CG . LEU B 1 88 ? -1.783 9.214 4.772 1.00 26.92 ? 88 LEU B CG 1 ATOM 1791 C CD1 . LEU B 1 88 ? -1.188 9.164 6.124 1.00 31.37 ? 88 LEU B CD1 1 ATOM 1792 C CD2 . LEU B 1 88 ? -3.259 9.068 4.820 1.00 32.10 ? 88 LEU B CD2 1 ATOM 1793 N N . GLY B 1 89 ? -0.916 12.154 0.956 1.00 25.82 ? 89 GLY B N 1 ATOM 1794 C CA . GLY B 1 89 ? -0.681 13.433 0.285 1.00 24.08 ? 89 GLY B CA 1 ATOM 1795 C C . GLY B 1 89 ? 0.632 13.979 0.788 1.00 25.60 ? 89 GLY B C 1 ATOM 1796 O O . GLY B 1 89 ? 1.597 13.204 0.933 1.00 25.11 ? 89 GLY B O 1 ATOM 1797 N N . ASN B 1 90 ? 0.670 15.295 1.024 1.00 24.01 ? 90 ASN B N 1 ATOM 1798 C CA . ASN B 1 90 ? 1.884 15.987 1.413 1.00 23.15 ? 90 ASN B CA 1 ATOM 1799 C C . ASN B 1 90 ? 1.649 16.551 2.779 1.00 22.70 ? 90 ASN B C 1 ATOM 1800 O O . ASN B 1 90 ? 0.532 16.929 3.078 1.00 22.80 ? 90 ASN B O 1 ATOM 1801 C CB . ASN B 1 90 ? 2.156 17.174 0.523 1.00 21.71 ? 90 ASN B CB 1 ATOM 1802 C CG . ASN B 1 90 ? 2.665 16.785 -0.871 1.00 22.75 ? 90 ASN B CG 1 ATOM 1803 O OD1 . ASN B 1 90 ? 2.054 17.117 -1.893 1.00 27.95 ? 90 ASN B OD1 1 ATOM 1804 N ND2 . ASN B 1 90 ? 3.787 16.108 -0.912 1.00 15.13 ? 90 ASN B ND2 1 ATOM 1805 N N . VAL B 1 91 ? 2.724 16.697 3.559 1.00 21.91 ? 91 VAL B N 1 ATOM 1806 C CA . VAL B 1 91 ? 2.699 17.600 4.693 1.00 21.59 ? 91 VAL B CA 1 ATOM 1807 C C . VAL B 1 91 ? 3.430 18.922 4.354 1.00 22.92 ? 91 VAL B C 1 ATOM 1808 O O . VAL B 1 91 ? 4.238 18.962 3.438 1.00 23.13 ? 91 VAL B O 1 ATOM 1809 C CB . VAL B 1 91 ? 3.310 16.922 5.972 1.00 19.77 ? 91 VAL B CB 1 ATOM 1810 C CG1 . VAL B 1 91 ? 2.434 15.729 6.377 1.00 19.55 ? 91 VAL B CG1 1 ATOM 1811 C CG2 . VAL B 1 91 ? 4.715 16.442 5.688 1.00 20.67 ? 91 VAL B CG2 1 ATOM 1812 N N . VAL B 1 92 ? 3.118 19.975 5.108 1.00 21.99 ? 92 VAL B N 1 ATOM 1813 C CA . VAL B 1 92 ? 3.573 21.329 4.846 1.00 23.42 ? 92 VAL B CA 1 ATOM 1814 C C . VAL B 1 92 ? 4.445 21.798 6.000 1.00 22.18 ? 92 VAL B C 1 ATOM 1815 O O . VAL B 1 92 ? 4.037 21.698 7.168 1.00 23.14 ? 92 VAL B O 1 ATOM 1816 C CB . VAL B 1 92 ? 2.322 22.312 4.727 1.00 23.52 ? 92 VAL B CB 1 ATOM 1817 C CG1 . VAL B 1 92 ? 2.747 23.765 4.629 1.00 24.00 ? 92 VAL B CG1 1 ATOM 1818 C CG2 . VAL B 1 92 ? 1.471 21.956 3.495 1.00 25.76 ? 92 VAL B CG2 1 ATOM 1819 N N . PHE B 1 93 ? 5.654 22.237 5.699 1.00 22.14 ? 93 PHE B N 1 ATOM 1820 C CA . PHE B 1 93 ? 6.500 22.844 6.732 1.00 22.53 ? 93 PHE B CA 1 ATOM 1821 C C . PHE B 1 93 ? 6.450 24.352 6.569 1.00 23.91 ? 93 PHE B C 1 ATOM 1822 O O . PHE B 1 93 ? 6.651 24.857 5.497 1.00 24.67 ? 93 PHE B O 1 ATOM 1823 C CB . PHE B 1 93 ? 7.941 22.379 6.680 1.00 19.68 ? 93 PHE B CB 1 ATOM 1824 C CG . PHE B 1 93 ? 8.159 21.005 7.238 1.00 21.31 ? 93 PHE B CG 1 ATOM 1825 C CD1 . PHE B 1 93 ? 8.800 20.830 8.415 1.00 20.37 ? 93 PHE B CD1 1 ATOM 1826 C CD2 . PHE B 1 93 ? 7.682 19.866 6.553 1.00 21.81 ? 93 PHE B CD2 1 ATOM 1827 C CE1 . PHE B 1 93 ? 8.978 19.547 8.914 1.00 19.52 ? 93 PHE B CE1 1 ATOM 1828 C CE2 . PHE B 1 93 ? 7.841 18.601 7.057 1.00 21.88 ? 93 PHE B CE2 1 ATOM 1829 C CZ . PHE B 1 93 ? 8.467 18.441 8.231 1.00 17.32 ? 93 PHE B CZ 1 ATOM 1830 N N . ASP B 1 94 ? 6.199 25.036 7.665 1.00 26.64 ? 94 ASP B N 1 ATOM 1831 C CA . ASP B 1 94 ? 6.058 26.487 7.675 1.00 28.03 ? 94 ASP B CA 1 ATOM 1832 C C . ASP B 1 94 ? 7.439 27.106 7.798 1.00 27.61 ? 94 ASP B C 1 ATOM 1833 O O . ASP B 1 94 ? 8.473 26.390 7.789 1.00 25.27 ? 94 ASP B O 1 ATOM 1834 C CB . ASP B 1 94 ? 5.133 26.901 8.806 1.00 28.56 ? 94 ASP B CB 1 ATOM 1835 C CG . ASP B 1 94 ? 5.785 26.820 10.188 1.00 31.96 ? 94 ASP B CG 1 ATOM 1836 O OD1 . ASP B 1 94 ? 5.036 26.945 11.193 1.00 32.86 ? 94 ASP B OD1 1 ATOM 1837 O OD2 . ASP B 1 94 ? 7.025 26.640 10.309 1.00 32.06 ? 94 ASP B OD2 1 ATOM 1838 N N . GLU B 1 95 ? 7.482 28.425 7.965 1.00 27.63 ? 95 GLU B N 1 ATOM 1839 C CA . GLU B 1 95 ? 8.739 29.135 7.821 1.00 27.35 ? 95 GLU B CA 1 ATOM 1840 C C . GLU B 1 95 ? 9.699 28.914 8.994 1.00 26.48 ? 95 GLU B C 1 ATOM 1841 O O . GLU B 1 95 ? 10.889 29.235 8.881 1.00 26.39 ? 95 GLU B O 1 ATOM 1842 C CB . GLU B 1 95 ? 8.496 30.623 7.595 1.00 30.29 ? 95 GLU B CB 1 ATOM 1843 C CG . GLU B 1 95 ? 7.613 31.340 8.623 1.00 34.55 ? 95 GLU B CG 1 ATOM 1844 C CD . GLU B 1 95 ? 6.144 30.838 8.721 1.00 42.45 ? 95 GLU B CD 1 ATOM 1845 O OE1 . GLU B 1 95 ? 5.539 31.062 9.812 1.00 42.40 ? 95 GLU B OE1 1 ATOM 1846 O OE2 . GLU B 1 95 ? 5.605 30.256 7.719 1.00 42.06 ? 95 GLU B OE2 1 ATOM 1847 N N . ASN B 1 96 ? 9.187 28.390 10.099 1.00 23.59 ? 96 ASN B N 1 ATOM 1848 C CA . ASN B 1 96 ? 9.996 28.038 11.258 1.00 23.94 ? 96 ASN B CA 1 ATOM 1849 C C . ASN B 1 96 ? 10.379 26.529 11.226 1.00 23.71 ? 96 ASN B C 1 ATOM 1850 O O . ASN B 1 96 ? 10.729 25.979 12.275 1.00 23.39 ? 96 ASN B O 1 ATOM 1851 C CB . ASN B 1 96 ? 9.234 28.403 12.551 1.00 23.12 ? 96 ASN B CB 1 ATOM 1852 C CG . ASN B 1 96 ? 8.822 29.875 12.576 1.00 25.32 ? 96 ASN B CG 1 ATOM 1853 O OD1 . ASN B 1 96 ? 9.618 30.733 12.206 1.00 27.71 ? 96 ASN B OD1 1 ATOM 1854 N ND2 . ASN B 1 96 ? 7.551 30.161 12.918 1.00 21.71 ? 96 ASN B ND2 1 ATOM 1855 N N . HIS B 1 97 ? 10.308 25.919 10.015 1.00 24.22 ? 97 HIS B N 1 ATOM 1856 C CA . HIS B 1 97 ? 10.620 24.502 9.729 1.00 23.20 ? 97 HIS B CA 1 ATOM 1857 C C . HIS B 1 97 ? 9.834 23.548 10.633 1.00 22.36 ? 97 HIS B C 1 ATOM 1858 O O . HIS B 1 97 ? 10.367 22.588 11.196 1.00 20.73 ? 97 HIS B O 1 ATOM 1859 C CB . HIS B 1 97 ? 12.137 24.235 9.904 1.00 24.39 ? 97 HIS B CB 1 ATOM 1860 C CG . HIS B 1 97 ? 13.019 24.987 8.953 1.00 23.93 ? 97 HIS B CG 1 ATOM 1861 N ND1 . HIS B 1 97 ? 14.196 24.462 8.464 1.00 25.01 ? 97 HIS B ND1 1 ATOM 1862 C CD2 . HIS B 1 97 ? 12.951 26.249 8.471 1.00 26.38 ? 97 HIS B CD2 1 ATOM 1863 C CE1 . HIS B 1 97 ? 14.809 25.356 7.713 1.00 22.74 ? 97 HIS B CE1 1 ATOM 1864 N NE2 . HIS B 1 97 ? 14.051 26.434 7.660 1.00 22.45 ? 97 HIS B NE2 1 ATOM 1865 N N . TYR B 1 98 ? 8.571 23.869 10.828 1.00 21.73 ? 98 TYR B N 1 ATOM 1866 C CA . TYR B 1 98 ? 7.693 23.113 11.644 1.00 21.90 ? 98 TYR B CA 1 ATOM 1867 C C . TYR B 1 98 ? 6.505 22.705 10.767 1.00 22.34 ? 98 TYR B C 1 ATOM 1868 O O . TYR B 1 98 ? 6.029 23.512 9.928 1.00 21.32 ? 98 TYR B O 1 ATOM 1869 C CB . TYR B 1 98 ? 7.189 23.955 12.819 1.00 22.19 ? 98 TYR B CB 1 ATOM 1870 C CG . TYR B 1 98 ? 6.071 23.312 13.641 1.00 23.35 ? 98 TYR B CG 1 ATOM 1871 C CD1 . TYR B 1 98 ? 6.340 22.229 14.510 1.00 22.56 ? 98 TYR B CD1 1 ATOM 1872 C CD2 . TYR B 1 98 ? 4.763 23.813 13.600 1.00 21.93 ? 98 TYR B CD2 1 ATOM 1873 C CE1 . TYR B 1 98 ? 5.309 21.623 15.223 1.00 22.03 ? 98 TYR B CE1 1 ATOM 1874 C CE2 . TYR B 1 98 ? 3.724 23.233 14.336 1.00 23.79 ? 98 TYR B CE2 1 ATOM 1875 C CZ . TYR B 1 98 ? 4.004 22.130 15.144 1.00 27.26 ? 98 TYR B CZ 1 ATOM 1876 O OH . TYR B 1 98 ? 2.973 21.515 15.927 1.00 31.27 ? 98 TYR B OH 1 ATOM 1877 N N . SER B 1 99 ? 6.033 21.474 10.953 1.00 21.17 ? 99 SER B N 1 ATOM 1878 C CA . SER B 1 99 ? 4.835 20.994 10.240 1.00 22.06 ? 99 SER B CA 1 ATOM 1879 C C . SER B 1 99 ? 3.796 20.542 11.272 1.00 23.08 ? 99 SER B C 1 ATOM 1880 O O . SER B 1 99 ? 4.074 19.653 12.084 1.00 21.13 ? 99 SER B O 1 ATOM 1881 C CB . SER B 1 99 ? 5.178 19.794 9.342 1.00 22.17 ? 99 SER B CB 1 ATOM 1882 O OG . SER B 1 99 ? 4.045 19.383 8.578 1.00 24.40 ? 99 SER B OG 1 ATOM 1883 N N . ARG B 1 100 ? 2.587 21.107 11.201 1.00 23.29 ? 100 ARG B N 1 ATOM 1884 C CA . ARG B 1 100 ? 1.472 20.531 11.927 1.00 24.60 ? 100 ARG B CA 1 ATOM 1885 C C . ARG B 1 100 ? 0.680 19.661 10.997 1.00 25.05 ? 100 ARG B C 1 ATOM 1886 O O . ARG B 1 100 ? 0.342 20.055 9.875 1.00 23.78 ? 100 ARG B O 1 ATOM 1887 C CB . ARG B 1 100 ? 0.549 21.631 12.448 1.00 26.56 ? 100 ARG B CB 1 ATOM 1888 C CG . ARG B 1 100 ? -0.532 21.123 13.420 1.00 32.07 ? 100 ARG B CG 1 ATOM 1889 C CD . ARG B 1 100 ? -1.280 22.349 13.925 1.00 46.01 ? 100 ARG B CD 1 ATOM 1890 N NE . ARG B 1 100 ? -2.570 22.036 14.562 1.00 53.47 ? 100 ARG B NE 1 ATOM 1891 C CZ . ARG B 1 100 ? -3.705 21.736 13.915 1.00 55.89 ? 100 ARG B CZ 1 ATOM 1892 N NH1 . ARG B 1 100 ? -3.730 21.656 12.582 1.00 55.63 ? 100 ARG B NH1 1 ATOM 1893 N NH2 . ARG B 1 100 ? -4.821 21.484 14.615 1.00 55.89 ? 100 ARG B NH2 1 ATOM 1894 N N . ILE B 1 101 ? 0.323 18.475 11.455 1.00 25.62 ? 101 ILE B N 1 ATOM 1895 C CA . ILE B 1 101 ? -0.546 17.623 10.648 1.00 25.10 ? 101 ILE B CA 1 ATOM 1896 C C . ILE B 1 101 ? -1.876 17.574 11.344 1.00 26.00 ? 101 ILE B C 1 ATOM 1897 O O . ILE B 1 101 ? -1.953 17.392 12.569 1.00 24.69 ? 101 ILE B O 1 ATOM 1898 C CB . ILE B 1 101 ? 0.100 16.233 10.475 1.00 26.04 ? 101 ILE B CB 1 ATOM 1899 C CG1 . ILE B 1 101 ? 1.449 16.409 9.737 1.00 26.34 ? 101 ILE B CG1 1 ATOM 1900 C CG2 . ILE B 1 101 ? -0.804 15.258 9.711 1.00 25.44 ? 101 ILE B CG2 1 ATOM 1901 C CD1 . ILE B 1 101 ? 2.458 15.442 10.156 1.00 24.63 ? 101 ILE B CD1 1 ATOM 1902 N N . ASP B 1 102 ? -2.956 17.737 10.592 1.00 29.05 ? 102 ASP B N 1 ATOM 1903 C CA . ASP B 1 102 ? -4.268 17.530 11.190 1.00 31.83 ? 102 ASP B CA 1 ATOM 1904 C C . ASP B 1 102 ? -5.159 17.163 10.050 1.00 33.00 ? 102 ASP B C 1 ATOM 1905 O O . ASP B 1 102 ? -5.695 18.033 9.384 1.00 34.51 ? 102 ASP B O 1 ATOM 1906 C CB . ASP B 1 102 ? -4.787 18.802 11.894 1.00 31.87 ? 102 ASP B CB 1 ATOM 1907 C CG . ASP B 1 102 ? -5.926 18.500 12.993 1.00 38.01 ? 102 ASP B CG 1 ATOM 1908 O OD1 . ASP B 1 102 ? -5.958 19.137 14.113 1.00 38.95 ? 102 ASP B OD1 1 ATOM 1909 O OD2 . ASP B 1 102 ? -6.783 17.626 12.765 1.00 42.78 ? 102 ASP B OD2 1 ATOM 1910 N N . LEU B 1 103 ? -5.331 15.878 9.785 1.00 33.69 ? 103 LEU B N 1 ATOM 1911 C CA . LEU B 1 103 ? -6.184 15.513 8.652 1.00 33.75 ? 103 LEU B CA 1 ATOM 1912 C C . LEU B 1 103 ? -7.066 14.364 8.979 1.00 33.77 ? 103 LEU B C 1 ATOM 1913 O O . LEU B 1 103 ? -6.851 13.684 9.980 1.00 34.70 ? 103 LEU B O 1 ATOM 1914 C CB . LEU B 1 103 ? -5.367 15.280 7.390 1.00 33.58 ? 103 LEU B CB 1 ATOM 1915 C CG . LEU B 1 103 ? -4.316 14.213 7.513 1.00 32.29 ? 103 LEU B CG 1 ATOM 1916 C CD1 . LEU B 1 103 ? -5.048 12.942 7.210 1.00 35.19 ? 103 LEU B CD1 1 ATOM 1917 C CD2 . LEU B 1 103 ? -3.151 14.415 6.544 1.00 34.92 ? 103 LEU B CD2 1 ATOM 1918 N N . VAL B 1 104 ? -8.081 14.153 8.156 1.00 34.38 ? 104 VAL B N 1 ATOM 1919 C CA . VAL B 1 104 ? -8.969 13.021 8.333 1.00 34.90 ? 104 VAL B CA 1 ATOM 1920 C C . VAL B 1 104 ? -8.999 12.117 7.111 1.00 35.48 ? 104 VAL B C 1 ATOM 1921 O O . VAL B 1 104 ? -9.191 12.566 5.981 1.00 34.01 ? 104 VAL B O 1 ATOM 1922 C CB . VAL B 1 104 ? -10.383 13.514 8.697 1.00 35.86 ? 104 VAL B CB 1 ATOM 1923 C CG1 . VAL B 1 104 ? -11.311 12.332 9.053 1.00 32.77 ? 104 VAL B CG1 1 ATOM 1924 C CG2 . VAL B 1 104 ? -10.245 14.428 9.864 1.00 37.23 ? 104 VAL B CG2 1 ATOM 1925 N N . ASP B 1 105 ? -8.779 10.830 7.337 1.00 37.27 ? 105 ASP B N 1 ATOM 1926 C CA . ASP B 1 105 ? -8.750 9.886 6.209 1.00 39.37 ? 105 ASP B CA 1 ATOM 1927 C C . ASP B 1 105 ? -9.729 8.714 6.326 1.00 39.19 ? 105 ASP B C 1 ATOM 1928 O O . ASP B 1 105 ? -10.012 8.217 7.411 1.00 40.20 ? 105 ASP B O 1 ATOM 1929 C CB . ASP B 1 105 ? -7.327 9.397 5.938 1.00 39.87 ? 105 ASP B CB 1 ATOM 1930 C CG . ASP B 1 105 ? -7.222 8.646 4.631 1.00 41.94 ? 105 ASP B CG 1 ATOM 1931 O OD1 . ASP B 1 105 ? -7.125 7.414 4.656 1.00 44.51 ? 105 ASP B OD1 1 ATOM 1932 O OD2 . ASP B 1 105 ? -7.265 9.284 3.556 1.00 48.51 ? 105 ASP B OD2 1 ATOM 1933 N N . ASP B 1 106 ? -10.248 8.257 5.202 1.00 39.74 ? 106 ASP B N 1 ATOM 1934 C CA . ASP B 1 106 ? -11.305 7.230 5.255 1.00 40.04 ? 106 ASP B CA 1 ATOM 1935 C C . ASP B 1 106 ? -10.888 5.966 4.540 1.00 38.39 ? 106 ASP B C 1 ATOM 1936 O O . ASP B 1 106 ? -11.692 5.062 4.416 1.00 36.92 ? 106 ASP B O 1 ATOM 1937 C CB . ASP B 1 106 ? -12.606 7.736 4.636 1.00 41.53 ? 106 ASP B CB 1 ATOM 1938 C CG . ASP B 1 106 ? -12.417 8.208 3.181 1.00 46.39 ? 106 ASP B CG 1 ATOM 1939 O OD1 . ASP B 1 106 ? -11.386 8.849 2.875 1.00 49.12 ? 106 ASP B OD1 1 ATOM 1940 O OD2 . ASP B 1 106 ? -13.309 7.955 2.336 1.00 54.88 ? 106 ASP B OD2 1 ATOM 1941 N N . GLN B 1 107 ? -9.643 5.909 4.054 1.00 36.89 ? 107 GLN B N 1 ATOM 1942 C CA . GLN B 1 107 ? -9.090 4.650 3.508 1.00 35.57 ? 107 GLN B CA 1 ATOM 1943 C C . GLN B 1 107 ? -8.266 3.876 4.579 1.00 34.14 ? 107 GLN B C 1 ATOM 1944 O O . GLN B 1 107 ? -8.368 2.664 4.678 1.00 33.99 ? 107 GLN B O 1 ATOM 1945 C CB . GLN B 1 107 ? -8.241 4.920 2.252 1.00 35.86 ? 107 GLN B CB 1 ATOM 1946 C CG . GLN B 1 107 ? -8.931 4.703 0.863 1.00 41.01 ? 107 GLN B CG 1 ATOM 1947 C CD . GLN B 1 107 ? -10.444 4.455 0.966 1.00 48.92 ? 107 GLN B CD 1 ATOM 1948 O OE1 . GLN B 1 107 ? -10.915 3.299 0.957 1.00 50.06 ? 107 GLN B OE1 1 ATOM 1949 N NE2 . GLN B 1 107 ? -11.211 5.538 1.077 1.00 51.99 ? 107 GLN B NE2 1 ATOM 1950 N N . ILE B 1 108 ? -7.399 4.562 5.318 1.00 31.44 ? 108 ILE B N 1 ATOM 1951 C CA . ILE B 1 108 ? -6.583 3.881 6.286 1.00 30.12 ? 108 ILE B CA 1 ATOM 1952 C C . ILE B 1 108 ? -7.467 3.471 7.505 1.00 30.91 ? 108 ILE B C 1 ATOM 1953 O O . ILE B 1 108 ? -8.456 4.140 7.864 1.00 28.75 ? 108 ILE B O 1 ATOM 1954 C CB . ILE B 1 108 ? -5.319 4.720 6.738 1.00 29.81 ? 108 ILE B CB 1 ATOM 1955 C CG1 . ILE B 1 108 ? -5.689 6.093 7.258 1.00 27.79 ? 108 ILE B CG1 1 ATOM 1956 C CG2 . ILE B 1 108 ? -4.291 4.860 5.660 1.00 25.82 ? 108 ILE B CG2 1 ATOM 1957 C CD1 . ILE B 1 108 ? -4.527 6.721 7.960 1.00 25.89 ? 108 ILE B CD1 1 ATOM 1958 N N . SER B 1 109 ? -7.118 2.360 8.145 1.00 31.28 ? 109 SER B N 1 ATOM 1959 C CA . SER B 1 109 ? -7.850 1.961 9.360 1.00 30.92 ? 109 SER B CA 1 ATOM 1960 C C . SER B 1 109 ? -6.829 1.528 10.388 1.00 31.51 ? 109 SER B C 1 ATOM 1961 O O . SER B 1 109 ? -5.649 1.376 10.043 1.00 32.09 ? 109 SER B O 1 ATOM 1962 C CB . SER B 1 109 ? -8.816 0.812 9.053 1.00 31.47 ? 109 SER B CB 1 ATOM 1963 O OG . SER B 1 109 ? -9.581 0.433 10.207 1.00 30.48 ? 109 SER B OG 1 ATOM 1964 N N . LEU B 1 110 ? -7.265 1.382 11.639 1.00 32.14 ? 110 LEU B N 1 ATOM 1965 C CA . LEU B 1 110 ? -6.446 0.840 12.689 1.00 33.50 ? 110 LEU B CA 1 ATOM 1966 C C . LEU B 1 110 ? -6.604 -0.689 12.864 1.00 35.77 ? 110 LEU B C 1 ATOM 1967 O O . LEU B 1 110 ? -5.884 -1.309 13.692 1.00 36.62 ? 110 LEU B O 1 ATOM 1968 C CB . LEU B 1 110 ? -6.657 1.616 13.969 1.00 32.87 ? 110 LEU B CB 1 ATOM 1969 C CG . LEU B 1 110 ? -6.174 3.067 13.897 1.00 33.85 ? 110 LEU B CG 1 ATOM 1970 C CD1 . LEU B 1 110 ? -6.065 3.643 15.278 1.00 34.94 ? 110 LEU B CD1 1 ATOM 1971 C CD2 . LEU B 1 110 ? -4.792 3.147 13.241 1.00 34.53 ? 110 LEU B CD2 1 ATOM 1972 N N . SER B 1 111 ? -7.498 -1.288 12.061 1.00 36.47 ? 111 SER B N 1 ATOM 1973 C CA . SER B 1 111 ? -7.715 -2.742 12.044 1.00 38.64 ? 111 SER B CA 1 ATOM 1974 C C . SER B 1 111 ? -8.278 -3.187 10.702 1.00 38.54 ? 111 SER B C 1 ATOM 1975 O O . SER B 1 111 ? -8.621 -2.362 9.866 1.00 38.53 ? 111 SER B O 1 ATOM 1976 C CB . SER B 1 111 ? -8.636 -3.197 13.200 1.00 39.01 ? 111 SER B CB 1 ATOM 1977 O OG . SER B 1 111 ? -9.902 -2.537 13.162 1.00 42.20 ? 111 SER B OG 1 ATOM 1978 N N . GLY B 1 112 ? -8.348 -4.499 10.493 1.00 39.80 ? 112 GLY B N 1 ATOM 1979 C CA . GLY B 1 112 ? -8.849 -5.084 9.246 1.00 38.72 ? 112 GLY B CA 1 ATOM 1980 C C . GLY B 1 112 ? -7.876 -4.994 8.085 1.00 38.87 ? 112 GLY B C 1 ATOM 1981 O O . GLY B 1 112 ? -6.674 -4.771 8.273 1.00 39.44 ? 112 GLY B O 1 ATOM 1982 N N . PRO B 1 113 ? -8.389 -5.162 6.856 1.00 37.82 ? 113 PRO B N 1 ATOM 1983 C CA . PRO B 1 113 ? -7.524 -5.218 5.688 1.00 36.54 ? 113 PRO B CA 1 ATOM 1984 C C . PRO B 1 113 ? -6.823 -3.876 5.384 1.00 34.91 ? 113 PRO B C 1 ATOM 1985 O O . PRO B 1 113 ? -5.790 -3.851 4.690 1.00 35.15 ? 113 PRO B O 1 ATOM 1986 C CB . PRO B 1 113 ? -8.493 -5.590 4.541 1.00 36.42 ? 113 PRO B CB 1 ATOM 1987 C CG . PRO B 1 113 ? -9.768 -6.033 5.236 1.00 38.29 ? 113 PRO B CG 1 ATOM 1988 C CD . PRO B 1 113 ? -9.816 -5.271 6.499 1.00 37.81 ? 113 PRO B CD 1 ATOM 1989 N N . HIS B 1 114 ? -7.374 -2.788 5.904 1.00 32.93 ? 114 HIS B N 1 ATOM 1990 C CA . HIS B 1 114 ? -6.812 -1.468 5.660 1.00 30.73 ? 114 HIS B CA 1 ATOM 1991 C C . HIS B 1 114 ? -6.048 -1.016 6.889 1.00 28.89 ? 114 HIS B C 1 ATOM 1992 O O . HIS B 1 114 ? -5.760 0.165 7.045 1.00 27.56 ? 114 HIS B O 1 ATOM 1993 C CB . HIS B 1 114 ? -7.946 -0.486 5.352 1.00 30.21 ? 114 HIS B CB 1 ATOM 1994 C CG . HIS B 1 114 ? -8.437 -0.539 3.934 1.00 31.49 ? 114 HIS B CG 1 ATOM 1995 N ND1 . HIS B 1 114 ? -9.204 0.465 3.371 1.00 32.31 ? 114 HIS B ND1 1 ATOM 1996 C CD2 . HIS B 1 114 ? -8.273 -1.477 2.962 1.00 31.12 ? 114 HIS B CD2 1 ATOM 1997 C CE1 . HIS B 1 114 ? -9.519 0.127 2.126 1.00 33.55 ? 114 HIS B CE1 1 ATOM 1998 N NE2 . HIS B 1 114 ? -8.966 -1.047 1.855 1.00 31.09 ? 114 HIS B NE2 1 ATOM 1999 N N . GLY B 1 115 ? -5.775 -1.970 7.787 1.00 27.31 ? 115 GLY B N 1 ATOM 2000 C CA . GLY B 1 115 ? -5.066 -1.678 9.007 1.00 25.40 ? 115 GLY B CA 1 ATOM 2001 C C . GLY B 1 115 ? -3.620 -1.260 8.769 1.00 25.23 ? 115 GLY B C 1 ATOM 2002 O O . GLY B 1 115 ? -2.909 -1.835 7.915 1.00 24.44 ? 115 GLY B O 1 ATOM 2003 N N . ILE B 1 116 ? -3.172 -0.272 9.533 1.00 24.82 ? 116 ILE B N 1 ATOM 2004 C CA . ILE B 1 116 ? -1.840 0.273 9.342 1.00 26.58 ? 116 ILE B CA 1 ATOM 2005 C C . ILE B 1 116 ? -0.884 0.004 10.517 1.00 26.34 ? 116 ILE B C 1 ATOM 2006 O O . ILE B 1 116 ? 0.285 0.407 10.483 1.00 24.27 ? 116 ILE B O 1 ATOM 2007 C CB . ILE B 1 116 ? -1.898 1.759 8.989 1.00 26.87 ? 116 ILE B CB 1 ATOM 2008 C CG1 . ILE B 1 116 ? -2.616 2.551 10.080 1.00 28.93 ? 116 ILE B CG1 1 ATOM 2009 C CG2 . ILE B 1 116 ? -2.673 1.968 7.641 1.00 26.84 ? 116 ILE B CG2 1 ATOM 2010 C CD1 . ILE B 1 116 ? -2.583 4.057 9.800 1.00 29.85 ? 116 ILE B CD1 1 ATOM 2011 N N . ILE B 1 117 ? -1.394 -0.654 11.555 1.00 24.90 ? 117 ILE B N 1 ATOM 2012 C CA . ILE B 1 117 ? -0.584 -0.910 12.710 1.00 25.20 ? 117 ILE B CA 1 ATOM 2013 C C . ILE B 1 117 ? 0.532 -1.871 12.299 1.00 23.52 ? 117 ILE B C 1 ATOM 2014 O O . ILE B 1 117 ? 0.276 -2.840 11.639 1.00 22.79 ? 117 ILE B O 1 ATOM 2015 C CB . ILE B 1 117 ? -1.466 -1.377 13.920 1.00 26.68 ? 117 ILE B CB 1 ATOM 2016 C CG1 . ILE B 1 117 ? -2.213 -0.148 14.503 1.00 26.87 ? 117 ILE B CG1 1 ATOM 2017 C CG2 . ILE B 1 117 ? -0.578 -1.933 15.080 1.00 26.70 ? 117 ILE B CG2 1 ATOM 2018 C CD1 . ILE B 1 117 ? -3.469 -0.465 15.227 1.00 33.75 ? 117 ILE B CD1 1 ATOM 2019 N N . GLY B 1 118 ? 1.778 -1.578 12.639 1.00 21.77 ? 118 GLY B N 1 ATOM 2020 C CA . GLY B 1 118 ? 2.818 -2.483 12.189 1.00 22.09 ? 118 GLY B CA 1 ATOM 2021 C C . GLY B 1 118 ? 3.467 -2.069 10.922 1.00 21.38 ? 118 GLY B C 1 ATOM 2022 O O . GLY B 1 118 ? 4.506 -2.610 10.545 1.00 23.58 ? 118 GLY B O 1 ATOM 2023 N N . ARG B 1 119 ? 2.908 -1.050 10.293 1.00 22.00 ? 119 ARG B N 1 ATOM 2024 C CA . ARG B 1 119 ? 3.398 -0.553 9.055 1.00 22.61 ? 119 ARG B CA 1 ATOM 2025 C C . ARG B 1 119 ? 4.253 0.706 9.301 1.00 23.82 ? 119 ARG B C 1 ATOM 2026 O O . ARG B 1 119 ? 4.453 1.119 10.437 1.00 26.30 ? 119 ARG B O 1 ATOM 2027 C CB . ARG B 1 119 ? 2.203 -0.358 8.104 1.00 22.51 ? 119 ARG B CB 1 ATOM 2028 C CG . ARG B 1 119 ? 1.449 -1.710 7.923 1.00 23.98 ? 119 ARG B CG 1 ATOM 2029 C CD . ARG B 1 119 ? 0.575 -1.740 6.707 1.00 25.67 ? 119 ARG B CD 1 ATOM 2030 N NE . ARG B 1 119 ? -0.398 -2.835 6.714 1.00 24.58 ? 119 ARG B NE 1 ATOM 2031 C CZ . ARG B 1 119 ? -0.168 -4.024 6.169 1.00 27.22 ? 119 ARG B CZ 1 ATOM 2032 N NH1 . ARG B 1 119 ? -1.095 -4.967 6.251 1.00 25.11 ? 119 ARG B NH1 1 ATOM 2033 N NH2 . ARG B 1 119 ? 1.001 -4.290 5.591 1.00 18.24 ? 119 ARG B NH2 1 ATOM 2034 N N . ALA B 1 120 ? 4.780 1.320 8.264 1.00 23.82 ? 120 ALA B N 1 ATOM 2035 C CA . ALA B 1 120 ? 5.647 2.463 8.462 1.00 22.79 ? 120 ALA B CA 1 ATOM 2036 C C . ALA B 1 120 ? 5.030 3.734 7.870 1.00 22.71 ? 120 ALA B C 1 ATOM 2037 O O . ALA B 1 120 ? 4.337 3.683 6.859 1.00 24.15 ? 120 ALA B O 1 ATOM 2038 C CB . ALA B 1 120 ? 6.963 2.162 7.851 1.00 22.40 ? 120 ALA B CB 1 ATOM 2039 N N . VAL B 1 121 ? 5.242 4.859 8.536 1.00 21.39 ? 121 VAL B N 1 ATOM 2040 C CA . VAL B 1 121 ? 5.007 6.172 7.976 1.00 23.21 ? 121 VAL B CA 1 ATOM 2041 C C . VAL B 1 121 ? 6.389 6.593 7.389 1.00 22.83 ? 121 VAL B C 1 ATOM 2042 O O . VAL B 1 121 ? 7.403 6.373 8.062 1.00 22.56 ? 121 VAL B O 1 ATOM 2043 C CB . VAL B 1 121 ? 4.593 7.076 9.143 1.00 24.39 ? 121 VAL B CB 1 ATOM 2044 C CG1 . VAL B 1 121 ? 5.042 8.439 8.958 1.00 27.43 ? 121 VAL B CG1 1 ATOM 2045 C CG2 . VAL B 1 121 ? 3.086 6.962 9.391 1.00 26.68 ? 121 VAL B CG2 1 ATOM 2046 N N . VAL B 1 122 ? 6.433 7.153 6.169 1.00 21.45 ? 122 VAL B N 1 ATOM 2047 C CA . VAL B 1 122 ? 7.695 7.631 5.559 1.00 19.27 ? 122 VAL B CA 1 ATOM 2048 C C . VAL B 1 122 ? 7.474 9.023 5.090 1.00 18.50 ? 122 VAL B C 1 ATOM 2049 O O . VAL B 1 122 ? 6.474 9.336 4.446 1.00 17.83 ? 122 VAL B O 1 ATOM 2050 C CB . VAL B 1 122 ? 8.161 6.764 4.325 1.00 20.95 ? 122 VAL B CB 1 ATOM 2051 C CG1 . VAL B 1 122 ? 9.520 7.283 3.683 1.00 21.37 ? 122 VAL B CG1 1 ATOM 2052 C CG2 . VAL B 1 122 ? 8.333 5.263 4.720 1.00 17.69 ? 122 VAL B CG2 1 ATOM 2053 N N . LEU B 1 123 ? 8.375 9.895 5.497 1.00 19.47 ? 123 LEU B N 1 ATOM 2054 C CA . LEU B 1 123 ? 8.407 11.293 5.099 1.00 20.48 ? 123 LEU B CA 1 ATOM 2055 C C . LEU B 1 123 ? 9.449 11.404 3.966 1.00 21.13 ? 123 LEU B C 1 ATOM 2056 O O . LEU B 1 123 ? 10.578 10.866 4.076 1.00 18.20 ? 123 LEU B O 1 ATOM 2057 C CB . LEU B 1 123 ? 8.861 12.145 6.309 1.00 20.50 ? 123 LEU B CB 1 ATOM 2058 C CG . LEU B 1 123 ? 9.110 13.631 6.011 1.00 21.47 ? 123 LEU B CG 1 ATOM 2059 C CD1 . LEU B 1 123 ? 7.820 14.255 5.433 1.00 22.29 ? 123 LEU B CD1 1 ATOM 2060 C CD2 . LEU B 1 123 ? 9.614 14.395 7.246 1.00 20.66 ? 123 LEU B CD2 1 ATOM 2061 N N . HIS B 1 124 ? 9.062 12.083 2.885 1.00 22.38 ? 124 HIS B N 1 ATOM 2062 C CA . HIS B 1 124 ? 9.859 12.048 1.643 1.00 23.14 ? 124 HIS B CA 1 ATOM 2063 C C . HIS B 1 124 ? 10.620 13.339 1.399 1.00 24.19 ? 124 HIS B C 1 ATOM 2064 O O . HIS B 1 124 ? 10.354 14.357 2.033 1.00 25.00 ? 124 HIS B O 1 ATOM 2065 C CB . HIS B 1 124 ? 8.955 11.703 0.463 1.00 22.60 ? 124 HIS B CB 1 ATOM 2066 C CG . HIS B 1 124 ? 8.439 10.289 0.483 1.00 24.84 ? 124 HIS B CG 1 ATOM 2067 N ND1 . HIS B 1 124 ? 9.168 9.241 -0.018 1.00 23.50 ? 124 HIS B ND1 1 ATOM 2068 C CD2 . HIS B 1 124 ? 7.286 9.750 0.972 1.00 22.86 ? 124 HIS B CD2 1 ATOM 2069 C CE1 . HIS B 1 124 ? 8.492 8.111 0.152 1.00 28.44 ? 124 HIS B CE1 1 ATOM 2070 N NE2 . HIS B 1 124 ? 7.345 8.386 0.754 1.00 32.71 ? 124 HIS B NE2 1 ATOM 2071 N N . GLU B 1 125 ? 11.585 13.319 0.494 1.00 26.03 ? 125 GLU B N 1 ATOM 2072 C CA . GLU B 1 125 ? 12.469 14.474 0.309 1.00 28.71 ? 125 GLU B CA 1 ATOM 2073 C C . GLU B 1 125 ? 11.782 15.639 -0.418 1.00 27.91 ? 125 GLU B C 1 ATOM 2074 O O . GLU B 1 125 ? 12.154 16.793 -0.243 1.00 27.61 ? 125 GLU B O 1 ATOM 2075 C CB . GLU B 1 125 ? 13.836 14.054 -0.316 1.00 28.88 ? 125 GLU B CB 1 ATOM 2076 C CG . GLU B 1 125 ? 14.154 14.488 -1.734 1.00 34.74 ? 125 GLU B CG 1 ATOM 2077 C CD . GLU B 1 125 ? 15.175 13.497 -2.436 1.00 36.60 ? 125 GLU B CD 1 ATOM 2078 O OE1 . GLU B 1 125 ? 14.801 12.798 -3.428 1.00 41.37 ? 125 GLU B OE1 1 ATOM 2079 O OE2 . GLU B 1 125 ? 16.339 13.377 -1.946 1.00 47.08 ? 125 GLU B OE2 1 ATOM 2080 N N . LYS B 1 126 ? 10.772 15.330 -1.221 1.00 27.98 ? 126 LYS B N 1 ATOM 2081 C CA . LYS B 1 126 ? 10.060 16.385 -1.938 1.00 29.49 ? 126 LYS B CA 1 ATOM 2082 C C . LYS B 1 126 ? 8.577 16.075 -2.088 1.00 28.60 ? 126 LYS B C 1 ATOM 2083 O O . LYS B 1 126 ? 8.029 15.096 -1.479 1.00 27.12 ? 126 LYS B O 1 ATOM 2084 C CB . LYS B 1 126 ? 10.752 16.755 -3.291 1.00 29.44 ? 126 LYS B CB 1 ATOM 2085 C CG . LYS B 1 126 ? 11.025 15.571 -4.219 1.00 29.17 ? 126 LYS B CG 1 ATOM 2086 C CD . LYS B 1 126 ? 11.948 16.031 -5.378 1.00 34.23 ? 126 LYS B CD 1 ATOM 2087 C CE . LYS B 1 126 ? 12.227 14.915 -6.429 1.00 37.41 ? 126 LYS B CE 1 ATOM 2088 N NZ . LYS B 1 126 ? 13.614 15.074 -7.047 1.00 43.21 ? 126 LYS B NZ 1 ATOM 2089 N N . ALA B 1 127 ? 7.910 16.974 -2.814 1.00 27.64 ? 127 ALA B N 1 ATOM 2090 C CA . ALA B 1 127 ? 6.467 16.978 -2.829 1.00 27.60 ? 127 ALA B CA 1 ATOM 2091 C C . ALA B 1 127 ? 5.971 15.825 -3.669 1.00 27.41 ? 127 ALA B C 1 ATOM 2092 O O . ALA B 1 127 ? 6.564 15.468 -4.693 1.00 27.40 ? 127 ALA B O 1 ATOM 2093 C CB . ALA B 1 127 ? 5.932 18.313 -3.350 1.00 28.22 ? 127 ALA B CB 1 ATOM 2094 N N . ASP B 1 128 ? 4.878 15.233 -3.217 1.00 26.59 ? 128 ASP B N 1 ATOM 2095 C CA . ASP B 1 128 ? 4.128 14.214 -3.973 1.00 26.05 ? 128 ASP B CA 1 ATOM 2096 C C . ASP B 1 128 ? 3.275 14.957 -5.023 1.00 26.13 ? 128 ASP B C 1 ATOM 2097 O O . ASP B 1 128 ? 2.586 15.943 -4.687 1.00 26.13 ? 128 ASP B O 1 ATOM 2098 C CB . ASP B 1 128 ? 3.224 13.501 -2.918 1.00 25.88 ? 128 ASP B CB 1 ATOM 2099 C CG . ASP B 1 128 ? 2.352 12.386 -3.488 1.00 27.61 ? 128 ASP B CG 1 ATOM 2100 O OD1 . ASP B 1 128 ? 1.826 11.615 -2.679 1.00 30.74 ? 128 ASP B OD1 1 ATOM 2101 O OD2 . ASP B 1 128 ? 2.146 12.257 -4.717 1.00 31.26 ? 128 ASP B OD2 1 ATOM 2102 N N . ASP B 1 129 ? 3.270 14.463 -6.257 1.00 27.24 ? 129 ASP B N 1 ATOM 2103 C CA . ASP B 1 129 ? 2.514 15.069 -7.395 1.00 28.37 ? 129 ASP B CA 1 ATOM 2104 C C . ASP B 1 129 ? 1.218 14.337 -7.665 1.00 28.12 ? 129 ASP B C 1 ATOM 2105 O O . ASP B 1 129 ? 0.518 14.652 -8.614 1.00 26.88 ? 129 ASP B O 1 ATOM 2106 C CB . ASP B 1 129 ? 3.362 15.159 -8.683 1.00 28.88 ? 129 ASP B CB 1 ATOM 2107 C CG . ASP B 1 129 ? 3.652 13.800 -9.317 1.00 29.84 ? 129 ASP B CG 1 ATOM 2108 O OD1 . ASP B 1 129 ? 4.666 13.692 -10.064 1.00 32.77 ? 129 ASP B OD1 1 ATOM 2109 O OD2 . ASP B 1 129 ? 2.880 12.840 -9.102 1.00 32.05 ? 129 ASP B OD2 1 ATOM 2110 N N . TYR B 1 130 ? 0.899 13.378 -6.799 1.00 27.35 ? 130 TYR B N 1 ATOM 2111 C CA . TYR B 1 130 ? -0.462 12.860 -6.661 1.00 28.22 ? 130 TYR B CA 1 ATOM 2112 C C . TYR B 1 130 ? -0.812 11.993 -7.883 1.00 28.12 ? 130 TYR B C 1 ATOM 2113 O O . TYR B 1 130 ? -1.982 11.729 -8.177 1.00 27.36 ? 130 TYR B O 1 ATOM 2114 C CB . TYR B 1 130 ? -1.568 13.949 -6.438 1.00 28.01 ? 130 TYR B CB 1 ATOM 2115 C CG . TYR B 1 130 ? -1.343 14.986 -5.361 1.00 28.45 ? 130 TYR B CG 1 ATOM 2116 C CD1 . TYR B 1 130 ? -1.210 14.635 -3.978 1.00 27.83 ? 130 TYR B CD1 1 ATOM 2117 C CD2 . TYR B 1 130 ? -1.285 16.322 -5.705 1.00 30.61 ? 130 TYR B CD2 1 ATOM 2118 C CE1 . TYR B 1 130 ? -0.972 15.609 -3.005 1.00 25.30 ? 130 TYR B CE1 1 ATOM 2119 C CE2 . TYR B 1 130 ? -1.057 17.293 -4.758 1.00 28.58 ? 130 TYR B CE2 1 ATOM 2120 C CZ . TYR B 1 130 ? -0.924 16.930 -3.398 1.00 29.07 ? 130 TYR B CZ 1 ATOM 2121 O OH . TYR B 1 130 ? -0.698 17.947 -2.510 1.00 32.14 ? 130 TYR B OH 1 ATOM 2122 N N . GLY B 1 131 ? 0.198 11.560 -8.609 1.00 29.59 ? 131 GLY B N 1 ATOM 2123 C CA . GLY B 1 131 ? -0.101 10.686 -9.719 1.00 31.89 ? 131 GLY B CA 1 ATOM 2124 C C . GLY B 1 131 ? -0.523 11.476 -10.946 1.00 33.19 ? 131 GLY B C 1 ATOM 2125 O O . GLY B 1 131 ? -1.000 10.867 -11.924 1.00 33.88 ? 131 GLY B O 1 ATOM 2126 N N . LYS B 1 132 ? -0.263 12.787 -10.933 1.00 34.29 ? 132 LYS B N 1 ATOM 2127 C CA . LYS B 1 132 ? -0.755 13.729 -11.966 1.00 36.90 ? 132 LYS B CA 1 ATOM 2128 C C . LYS B 1 132 ? 0.302 14.462 -12.747 1.00 38.30 ? 132 LYS B C 1 ATOM 2129 O O . LYS B 1 132 ? 0.036 15.537 -13.228 1.00 41.01 ? 132 LYS B O 1 ATOM 2130 C CB . LYS B 1 132 ? -1.713 14.772 -11.344 1.00 35.96 ? 132 LYS B CB 1 ATOM 2131 C CG . LYS B 1 132 ? -2.873 14.147 -10.645 1.00 37.98 ? 132 LYS B CG 1 ATOM 2132 C CD . LYS B 1 132 ? -3.670 15.211 -9.862 1.00 46.75 ? 132 LYS B CD 1 ATOM 2133 C CE . LYS B 1 132 ? -4.565 14.593 -8.785 1.00 49.60 ? 132 LYS B CE 1 ATOM 2134 N NZ . LYS B 1 132 ? -5.297 13.402 -9.335 1.00 48.46 ? 132 LYS B NZ 1 ATOM 2135 N N . SER B 1 133 ? 1.511 13.948 -12.893 1.00 40.14 ? 133 SER B N 1 ATOM 2136 C CA . SER B 1 133 ? 2.413 14.588 -13.836 1.00 41.81 ? 133 SER B CA 1 ATOM 2137 C C . SER B 1 133 ? 2.735 13.636 -14.972 1.00 44.14 ? 133 SER B C 1 ATOM 2138 O O . SER B 1 133 ? 2.367 12.451 -14.896 1.00 44.50 ? 133 SER B O 1 ATOM 2139 C CB . SER B 1 133 ? 3.710 15.020 -13.160 1.00 40.77 ? 133 SER B CB 1 ATOM 2140 O OG . SER B 1 133 ? 4.412 13.870 -12.748 1.00 42.26 ? 133 SER B OG 1 ATOM 2141 N N . ASP B 1 134 ? 3.426 14.157 -16.006 1.00 46.34 ? 134 ASP B N 1 ATOM 2142 C CA . ASP B 1 134 ? 4.074 13.326 -17.047 1.00 48.70 ? 134 ASP B CA 1 ATOM 2143 C C . ASP B 1 134 ? 5.311 12.564 -16.528 1.00 49.03 ? 134 ASP B C 1 ATOM 2144 O O . ASP B 1 134 ? 5.744 11.585 -17.143 1.00 49.97 ? 134 ASP B O 1 ATOM 2145 C CB . ASP B 1 134 ? 4.458 14.170 -18.281 1.00 49.66 ? 134 ASP B CB 1 ATOM 2146 C CG . ASP B 1 134 ? 5.815 14.861 -18.121 1.00 55.18 ? 134 ASP B CG 1 ATOM 2147 O OD1 . ASP B 1 134 ? 5.946 15.722 -17.218 1.00 60.03 ? 134 ASP B OD1 1 ATOM 2148 O OD2 . ASP B 1 134 ? 6.772 14.542 -18.890 1.00 62.28 ? 134 ASP B OD2 1 ATOM 2149 N N . HIS B 1 135 ? 5.868 12.983 -15.395 1.00 49.15 ? 135 HIS B N 1 ATOM 2150 C CA . HIS B 1 135 ? 7.076 12.345 -14.843 1.00 49.03 ? 135 HIS B CA 1 ATOM 2151 C C . HIS B 1 135 ? 6.919 10.836 -14.714 1.00 49.02 ? 135 HIS B C 1 ATOM 2152 O O . HIS B 1 135 ? 5.881 10.378 -14.256 1.00 49.08 ? 135 HIS B O 1 ATOM 2153 C CB . HIS B 1 135 ? 7.431 12.945 -13.487 1.00 48.99 ? 135 HIS B CB 1 ATOM 2154 C CG . HIS B 1 135 ? 8.714 12.425 -12.912 1.00 49.34 ? 135 HIS B CG 1 ATOM 2155 N ND1 . HIS B 1 135 ? 9.889 13.146 -12.950 1.00 49.88 ? 135 HIS B ND1 1 ATOM 2156 C CD2 . HIS B 1 135 ? 9.009 11.251 -12.294 1.00 48.26 ? 135 HIS B CD2 1 ATOM 2157 C CE1 . HIS B 1 135 ? 10.852 12.443 -12.373 1.00 50.87 ? 135 HIS B CE1 1 ATOM 2158 N NE2 . HIS B 1 135 ? 10.344 11.287 -11.973 1.00 50.41 ? 135 HIS B NE2 1 ATOM 2159 N N . PRO B 1 136 ? 7.949 10.060 -15.130 1.00 48.97 ? 136 PRO B N 1 ATOM 2160 C CA . PRO B 1 136 ? 7.935 8.582 -15.177 1.00 49.19 ? 136 PRO B CA 1 ATOM 2161 C C . PRO B 1 136 ? 7.420 7.889 -13.905 1.00 49.36 ? 136 PRO B C 1 ATOM 2162 O O . PRO B 1 136 ? 6.615 6.948 -13.993 1.00 49.91 ? 136 PRO B O 1 ATOM 2163 C CB . PRO B 1 136 ? 9.407 8.219 -15.401 1.00 49.42 ? 136 PRO B CB 1 ATOM 2164 C CG . PRO B 1 136 ? 9.979 9.404 -16.146 1.00 49.83 ? 136 PRO B CG 1 ATOM 2165 C CD . PRO B 1 136 ? 9.227 10.617 -15.623 1.00 49.02 ? 136 PRO B CD 1 ATOM 2166 N N . ASP B 1 137 ? 7.860 8.371 -12.742 1.00 48.91 ? 137 ASP B N 1 ATOM 2167 C CA . ASP B 1 137 ? 7.440 7.813 -11.453 1.00 48.23 ? 137 ASP B CA 1 ATOM 2168 C C . ASP B 1 137 ? 6.049 8.221 -10.951 1.00 46.28 ? 137 ASP B C 1 ATOM 2169 O O . ASP B 1 137 ? 5.467 7.533 -10.096 1.00 46.78 ? 137 ASP B O 1 ATOM 2170 C CB . ASP B 1 137 ? 8.497 8.121 -10.420 1.00 48.65 ? 137 ASP B CB 1 ATOM 2171 C CG . ASP B 1 137 ? 9.667 7.203 -10.555 1.00 53.38 ? 137 ASP B CG 1 ATOM 2172 O OD1 . ASP B 1 137 ? 10.837 7.696 -10.587 1.00 56.76 ? 137 ASP B OD1 1 ATOM 2173 O OD2 . ASP B 1 137 ? 9.391 5.974 -10.683 1.00 55.96 ? 137 ASP B OD2 1 ATOM 2174 N N . SER B 1 138 ? 5.495 9.298 -11.513 1.00 44.12 ? 138 SER B N 1 ATOM 2175 C CA . SER B 1 138 ? 4.239 9.842 -11.026 1.00 41.12 ? 138 SER B CA 1 ATOM 2176 C C . SER B 1 138 ? 3.232 8.818 -10.561 1.00 40.38 ? 138 SER B C 1 ATOM 2177 O O . SER B 1 138 ? 2.738 8.935 -9.461 1.00 39.07 ? 138 SER B O 1 ATOM 2178 C CB . SER B 1 138 ? 3.634 10.844 -12.001 1.00 41.25 ? 138 SER B CB 1 ATOM 2179 O OG . SER B 1 138 ? 2.507 11.493 -11.412 1.00 40.45 ? 138 SER B OG 1 ATOM 2180 N N . ARG B 1 139 ? 2.947 7.791 -11.361 1.00 41.29 ? 139 ARG B N 1 ATOM 2181 C CA . ARG B 1 139 ? 1.831 6.846 -11.079 1.00 42.32 ? 139 ARG B CA 1 ATOM 2182 C C . ARG B 1 139 ? 2.046 5.770 -10.020 1.00 41.55 ? 139 ARG B C 1 ATOM 2183 O O . ARG B 1 139 ? 1.088 5.132 -9.557 1.00 39.62 ? 139 ARG B O 1 ATOM 2184 C CB . ARG B 1 139 ? 1.291 6.200 -12.372 1.00 43.93 ? 139 ARG B CB 1 ATOM 2185 C CG . ARG B 1 139 ? 0.083 6.959 -12.977 1.00 49.91 ? 139 ARG B CG 1 ATOM 2186 C CD . ARG B 1 139 ? -0.901 5.989 -13.596 1.00 58.83 ? 139 ARG B CD 1 ATOM 2187 N NE . ARG B 1 139 ? -0.290 5.111 -14.602 1.00 64.99 ? 139 ARG B NE 1 ATOM 2188 C CZ . ARG B 1 139 ? -0.670 5.046 -15.882 1.00 69.18 ? 139 ARG B CZ 1 ATOM 2189 N NH1 . ARG B 1 139 ? -0.065 4.200 -16.718 1.00 70.03 ? 139 ARG B NH1 1 ATOM 2190 N NH2 . ARG B 1 139 ? -1.656 5.823 -16.330 1.00 70.78 ? 139 ARG B NH2 1 ATOM 2191 N N . LYS B 1 140 ? 3.307 5.585 -9.625 1.00 41.87 ? 140 LYS B N 1 ATOM 2192 C CA . LYS B 1 140 ? 3.634 4.672 -8.543 1.00 41.07 ? 140 LYS B CA 1 ATOM 2193 C C . LYS B 1 140 ? 3.941 5.365 -7.179 1.00 39.62 ? 140 LYS B C 1 ATOM 2194 O O . LYS B 1 140 ? 3.442 4.951 -6.126 1.00 39.03 ? 140 LYS B O 1 ATOM 2195 C CB . LYS B 1 140 ? 4.798 3.794 -8.992 1.00 42.36 ? 140 LYS B CB 1 ATOM 2196 C CG . LYS B 1 140 ? 4.394 2.813 -10.081 1.00 44.58 ? 140 LYS B CG 1 ATOM 2197 C CD . LYS B 1 140 ? 5.600 2.026 -10.621 1.00 47.55 ? 140 LYS B CD 1 ATOM 2198 C CE . LYS B 1 140 ? 5.238 1.242 -11.940 1.00 48.43 ? 140 LYS B CE 1 ATOM 2199 N NZ . LYS B 1 140 ? 4.063 0.258 -11.806 1.00 49.07 ? 140 LYS B NZ 1 ATOM 2200 N N . THR B 1 141 ? 4.743 6.429 -7.224 1.00 38.32 ? 141 THR B N 1 ATOM 2201 C CA . THR B 1 141 ? 5.279 7.068 -6.021 1.00 36.45 ? 141 THR B CA 1 ATOM 2202 C C . THR B 1 141 ? 4.929 8.556 -5.909 1.00 36.13 ? 141 THR B C 1 ATOM 2203 O O . THR B 1 141 ? 5.213 9.221 -4.859 1.00 35.24 ? 141 THR B O 1 ATOM 2204 C CB . THR B 1 141 ? 6.829 6.974 -6.032 1.00 36.92 ? 141 THR B CB 1 ATOM 2205 O OG1 . THR B 1 141 ? 7.319 7.909 -6.980 1.00 38.29 ? 141 THR B OG1 1 ATOM 2206 C CG2 . THR B 1 141 ? 7.323 5.548 -6.432 1.00 35.46 ? 141 THR B CG2 1 ATOM 2207 N N . GLY B 1 142 ? 4.386 9.118 -6.996 1.00 34.45 ? 142 GLY B N 1 ATOM 2208 C CA . GLY B 1 142 ? 4.161 10.558 -7.052 1.00 31.80 ? 142 GLY B CA 1 ATOM 2209 C C . GLY B 1 142 ? 5.433 11.356 -7.176 1.00 31.46 ? 142 GLY B C 1 ATOM 2210 O O . GLY B 1 142 ? 5.455 12.546 -6.914 1.00 29.72 ? 142 GLY B O 1 ATOM 2211 N N . ASN B 1 143 ? 6.503 10.703 -7.579 1.00 31.08 ? 143 ASN B N 1 ATOM 2212 C CA . ASN B 1 143 ? 7.764 11.352 -7.741 1.00 31.61 ? 143 ASN B CA 1 ATOM 2213 C C . ASN B 1 143 ? 8.066 12.217 -6.496 1.00 31.80 ? 143 ASN B C 1 ATOM 2214 O O . ASN B 1 143 ? 8.492 13.384 -6.607 1.00 30.72 ? 143 ASN B O 1 ATOM 2215 C CB . ASN B 1 143 ? 7.773 12.153 -9.061 1.00 32.33 ? 143 ASN B CB 1 ATOM 2216 C CG . ASN B 1 143 ? 9.107 12.865 -9.331 1.00 34.67 ? 143 ASN B CG 1 ATOM 2217 O OD1 . ASN B 1 143 ? 9.119 14.012 -9.800 1.00 39.84 ? 143 ASN B OD1 1 ATOM 2218 N ND2 . ASN B 1 143 ? 10.210 12.232 -8.990 1.00 36.00 ? 143 ASN B ND2 1 ATOM 2219 N N . ALA B 1 144 ? 7.840 11.648 -5.311 1.00 31.74 ? 144 ALA B N 1 ATOM 2220 C CA . ALA B 1 144 ? 8.208 12.363 -4.065 1.00 32.36 ? 144 ALA B CA 1 ATOM 2221 C C . ALA B 1 144 ? 9.675 12.182 -3.641 1.00 32.91 ? 144 ALA B C 1 ATOM 2222 O O . ALA B 1 144 ? 10.121 12.766 -2.629 1.00 32.91 ? 144 ALA B O 1 ATOM 2223 C CB . ALA B 1 144 ? 7.242 12.028 -2.915 1.00 33.02 ? 144 ALA B CB 1 ATOM 2224 N N . GLY B 1 145 ? 10.437 11.386 -4.404 1.00 31.53 ? 145 GLY B N 1 ATOM 2225 C CA . GLY B 1 145 ? 11.885 11.336 -4.189 1.00 30.19 ? 145 GLY B CA 1 ATOM 2226 C C . GLY B 1 145 ? 12.216 10.392 -3.023 1.00 29.48 ? 145 GLY B C 1 ATOM 2227 O O . GLY B 1 145 ? 11.372 9.590 -2.609 1.00 29.40 ? 145 GLY B O 1 ATOM 2228 N N . GLY B 1 146 ? 13.425 10.550 -2.480 1.00 27.92 ? 146 GLY B N 1 ATOM 2229 C CA . GLY B 1 146 ? 13.975 9.678 -1.438 1.00 28.73 ? 146 GLY B CA 1 ATOM 2230 C C . GLY B 1 146 ? 13.267 9.789 -0.083 1.00 28.03 ? 146 GLY B C 1 ATOM 2231 O O . GLY B 1 146 ? 12.456 10.694 0.151 1.00 27.58 ? 146 GLY B O 1 ATOM 2232 N N . ARG B 1 147 ? 13.639 8.895 0.807 1.00 26.67 ? 147 ARG B N 1 ATOM 2233 C CA . ARG B 1 147 ? 13.015 8.769 2.106 1.00 27.68 ? 147 ARG B CA 1 ATOM 2234 C C . ARG B 1 147 ? 13.885 9.472 3.128 1.00 27.80 ? 147 ARG B C 1 ATOM 2235 O O . ARG B 1 147 ? 15.039 9.025 3.343 1.00 28.51 ? 147 ARG B O 1 ATOM 2236 C CB . ARG B 1 147 ? 12.914 7.278 2.415 1.00 27.63 ? 147 ARG B CB 1 ATOM 2237 C CG . ARG B 1 147 ? 11.959 6.587 1.470 1.00 24.79 ? 147 ARG B CG 1 ATOM 2238 C CD . ARG B 1 147 ? 12.031 5.091 1.550 1.00 23.29 ? 147 ARG B CD 1 ATOM 2239 N NE . ARG B 1 147 ? 11.371 4.605 0.351 1.00 23.84 ? 147 ARG B NE 1 ATOM 2240 C CZ . ARG B 1 147 ? 10.705 3.467 0.227 1.00 29.48 ? 147 ARG B CZ 1 ATOM 2241 N NH1 . ARG B 1 147 ? 10.114 3.204 -0.944 1.00 28.42 ? 147 ARG B NH1 1 ATOM 2242 N NH2 . ARG B 1 147 ? 10.597 2.594 1.245 1.00 24.15 ? 147 ARG B NH2 1 ATOM 2243 N N . VAL B 1 148 ? 13.376 10.546 3.761 1.00 26.72 ? 148 VAL B N 1 ATOM 2244 C CA . VAL B 1 148 ? 14.172 11.228 4.779 1.00 26.32 ? 148 VAL B CA 1 ATOM 2245 C C . VAL B 1 148 ? 13.996 10.756 6.263 1.00 26.14 ? 148 VAL B C 1 ATOM 2246 O O . VAL B 1 148 ? 14.869 11.003 7.085 1.00 25.31 ? 148 VAL B O 1 ATOM 2247 C CB . VAL B 1 148 ? 14.000 12.771 4.762 1.00 25.98 ? 148 VAL B CB 1 ATOM 2248 C CG1 . VAL B 1 148 ? 14.479 13.340 3.423 1.00 29.65 ? 148 VAL B CG1 1 ATOM 2249 C CG2 . VAL B 1 148 ? 12.592 13.171 5.119 1.00 26.44 ? 148 VAL B CG2 1 ATOM 2250 N N . ALA B 1 149 ? 12.850 10.161 6.588 1.00 23.81 ? 149 ALA B N 1 ATOM 2251 C CA . ALA B 1 149 ? 12.596 9.620 7.937 1.00 22.98 ? 149 ALA B CA 1 ATOM 2252 C C . ALA B 1 149 ? 11.393 8.702 7.839 1.00 22.75 ? 149 ALA B C 1 ATOM 2253 O O . ALA B 1 149 ? 10.500 8.896 6.958 1.00 20.65 ? 149 ALA B O 1 ATOM 2254 C CB . ALA B 1 149 ? 12.312 10.747 8.964 1.00 23.13 ? 149 ALA B CB 1 ATOM 2255 N N . CYS B 1 150 ? 11.385 7.678 8.695 1.00 21.98 ? 150 CYS B N 1 ATOM 2256 C CA . CYS B 1 150 ? 10.277 6.770 8.774 1.00 23.28 ? 150 CYS B CA 1 ATOM 2257 C C . CYS B 1 150 ? 10.145 6.259 10.243 1.00 22.12 ? 150 CYS B C 1 ATOM 2258 O O . CYS B 1 150 ? 11.089 6.355 11.048 1.00 21.17 ? 150 CYS B O 1 ATOM 2259 C CB . CYS B 1 150 ? 10.567 5.635 7.794 1.00 24.15 ? 150 CYS B CB 1 ATOM 2260 S SG . CYS B 1 150 ? 12.191 4.888 8.043 1.00 35.35 ? 150 CYS B SG 1 ATOM 2261 N N . GLY B 1 151 ? 8.974 5.774 10.595 1.00 19.71 ? 151 GLY B N 1 ATOM 2262 C CA . GLY B 1 151 ? 8.789 5.202 11.891 1.00 18.95 ? 151 GLY B CA 1 ATOM 2263 C C . GLY B 1 151 ? 7.676 4.216 11.768 1.00 20.15 ? 151 GLY B C 1 ATOM 2264 O O . GLY B 1 151 ? 6.743 4.405 10.964 1.00 18.25 ? 151 GLY B O 1 ATOM 2265 N N . VAL B 1 152 ? 7.795 3.130 12.535 1.00 19.11 ? 152 VAL B N 1 ATOM 2266 C CA . VAL B 1 152 ? 6.829 2.020 12.509 1.00 18.96 ? 152 VAL B CA 1 ATOM 2267 C C . VAL B 1 152 ? 5.578 2.556 13.242 1.00 19.09 ? 152 VAL B C 1 ATOM 2268 O O . VAL B 1 152 ? 5.688 3.346 14.181 1.00 17.66 ? 152 VAL B O 1 ATOM 2269 C CB . VAL B 1 152 ? 7.418 0.786 13.265 1.00 18.98 ? 152 VAL B CB 1 ATOM 2270 C CG1 . VAL B 1 152 ? 6.500 -0.438 13.146 1.00 18.85 ? 152 VAL B CG1 1 ATOM 2271 C CG2 . VAL B 1 152 ? 8.765 0.371 12.631 1.00 21.25 ? 152 VAL B CG2 1 ATOM 2272 N N . ILE B 1 153 ? 4.417 2.156 12.781 1.00 19.10 ? 153 ILE B N 1 ATOM 2273 C CA . ILE B 1 153 ? 3.186 2.622 13.392 1.00 21.27 ? 153 ILE B CA 1 ATOM 2274 C C . ILE B 1 153 ? 2.858 1.662 14.531 1.00 22.33 ? 153 ILE B C 1 ATOM 2275 O O . ILE B 1 153 ? 2.630 0.470 14.301 1.00 21.19 ? 153 ILE B O 1 ATOM 2276 C CB . ILE B 1 153 ? 2.064 2.720 12.408 1.00 20.60 ? 153 ILE B CB 1 ATOM 2277 C CG1 . ILE B 1 153 ? 2.363 3.828 11.410 1.00 21.23 ? 153 ILE B CG1 1 ATOM 2278 C CG2 . ILE B 1 153 ? 0.736 3.064 13.138 1.00 22.52 ? 153 ILE B CG2 1 ATOM 2279 C CD1 . ILE B 1 153 ? 1.493 3.689 10.196 1.00 25.29 ? 153 ILE B CD1 1 ATOM 2280 N N . GLY B 1 154 ? 2.954 2.178 15.758 1.00 23.71 ? 154 GLY B N 1 ATOM 2281 C CA . GLY B 1 154 ? 2.753 1.324 16.929 1.00 25.34 ? 154 GLY B CA 1 ATOM 2282 C C . GLY B 1 154 ? 1.497 1.697 17.717 1.00 25.86 ? 154 GLY B C 1 ATOM 2283 O O . GLY B 1 154 ? 1.021 2.823 17.674 1.00 23.91 ? 154 GLY B O 1 ATOM 2284 N N . ILE B 1 155 ? 1.024 0.753 18.490 1.00 26.70 ? 155 ILE B N 1 ATOM 2285 C CA . ILE B 1 155 ? -0.135 0.936 19.322 1.00 29.60 ? 155 ILE B CA 1 ATOM 2286 C C . ILE B 1 155 ? 0.097 1.997 20.402 1.00 31.19 ? 155 ILE B C 1 ATOM 2287 O O . ILE B 1 155 ? 1.142 2.038 21.076 1.00 32.22 ? 155 ILE B O 1 ATOM 2288 C CB . ILE B 1 155 ? -0.515 -0.395 19.965 1.00 30.99 ? 155 ILE B CB 1 ATOM 2289 C CG1 . ILE B 1 155 ? -0.956 -1.353 18.878 1.00 27.41 ? 155 ILE B CG1 1 ATOM 2290 C CG2 . ILE B 1 155 ? -1.550 -0.179 21.095 1.00 33.59 ? 155 ILE B CG2 1 ATOM 2291 C CD1 . ILE B 1 155 ? -1.312 -2.728 19.369 1.00 29.99 ? 155 ILE B CD1 1 ATOM 2292 N N . LEU B 1 156 ? -0.871 2.885 20.538 1.00 32.90 ? 156 LEU B N 1 ATOM 2293 C CA . LEU B 1 156 ? -0.759 3.999 21.461 1.00 35.66 ? 156 LEU B CA 1 ATOM 2294 C C . LEU B 1 156 ? -1.565 3.797 22.721 1.00 37.31 ? 156 LEU B C 1 ATOM 2295 O O . LEU B 1 156 ? -1.199 4.404 23.754 1.00 40.63 ? 156 LEU B O 1 ATOM 2296 C CB . LEU B 1 156 ? -1.161 5.327 20.803 1.00 35.10 ? 156 LEU B CB 1 ATOM 2297 C CG . LEU B 1 156 ? -1.016 6.556 21.668 1.00 37.42 ? 156 LEU B CG 1 ATOM 2298 C CD1 . LEU B 1 156 ? 0.426 6.691 21.982 1.00 41.65 ? 156 LEU B CD1 1 ATOM 2299 C CD2 . LEU B 1 156 ? -1.519 7.809 20.936 1.00 36.97 ? 156 LEU B CD2 1 HETATM 2300 C C1 . NAG C 2 . ? 19.727 -6.960 10.423 1.00 59.31 ? 1001 NAG A C1 1 HETATM 2301 C C2 . NAG C 2 . ? 19.197 -7.356 9.029 1.00 67.55 ? 1001 NAG A C2 1 HETATM 2302 C C3 . NAG C 2 . ? 20.204 -7.110 7.886 1.00 70.91 ? 1001 NAG A C3 1 HETATM 2303 C C4 . NAG C 2 . ? 21.279 -6.034 8.076 1.00 74.69 ? 1001 NAG A C4 1 HETATM 2304 C C5 . NAG C 2 . ? 21.417 -5.518 9.511 1.00 72.96 ? 1001 NAG A C5 1 HETATM 2305 C C6 . NAG C 2 . ? 21.804 -4.034 9.532 1.00 74.31 ? 1001 NAG A C6 1 HETATM 2306 C C7 . NAG C 2 . ? 17.417 -9.150 8.836 1.00 69.84 ? 1001 NAG A C7 1 HETATM 2307 C C8 . NAG C 2 . ? 16.395 -8.392 9.603 1.00 69.46 ? 1001 NAG A C8 1 HETATM 2308 N N2 . NAG C 2 . ? 18.709 -8.756 8.946 1.00 69.26 ? 1001 NAG A N2 1 HETATM 2309 O O3 . NAG C 2 . ? 19.514 -6.877 6.674 1.00 69.01 ? 1001 NAG A O3 1 HETATM 2310 O O4 . NAG C 2 . ? 22.484 -6.721 7.820 1.00 84.03 ? 1001 NAG A O4 1 HETATM 2311 O O5 . NAG C 2 . ? 20.219 -5.661 10.262 1.00 66.64 ? 1001 NAG A O5 1 HETATM 2312 O O6 . NAG C 2 . ? 23.002 -3.759 8.830 1.00 75.88 ? 1001 NAG A O6 1 HETATM 2313 O O7 . NAG C 2 . ? 17.005 -10.091 8.156 1.00 70.39 ? 1001 NAG A O7 1 HETATM 2314 C C1 . NAG D 2 . ? 23.488 -6.262 6.856 1.00 89.00 ? 1002 NAG A C1 1 HETATM 2315 C C2 . NAG D 2 . ? 23.139 -5.272 5.726 1.00 92.00 ? 1002 NAG A C2 1 HETATM 2316 C C3 . NAG D 2 . ? 24.349 -4.432 5.261 1.00 93.91 ? 1002 NAG A C3 1 HETATM 2317 C C4 . NAG D 2 . ? 25.739 -5.100 5.450 1.00 93.94 ? 1002 NAG A C4 1 HETATM 2318 C C5 . NAG D 2 . ? 25.742 -6.138 6.606 1.00 93.07 ? 1002 NAG A C5 1 HETATM 2319 C C6 . NAG D 2 . ? 27.047 -6.306 7.403 1.00 92.67 ? 1002 NAG A C6 1 HETATM 2320 C C7 . NAG D 2 . ? 21.483 -6.151 4.076 1.00 93.56 ? 1002 NAG A C7 1 HETATM 2321 C C8 . NAG D 2 . ? 20.613 -4.903 3.994 1.00 92.21 ? 1002 NAG A C8 1 HETATM 2322 N N2 . NAG D 2 . ? 22.737 -6.000 4.535 1.00 93.13 ? 1002 NAG A N2 1 HETATM 2323 O O3 . NAG D 2 . ? 24.305 -3.137 5.842 1.00 95.34 ? 1002 NAG A O3 1 HETATM 2324 O O4 . NAG D 2 . ? 26.173 -5.674 4.211 1.00 94.65 ? 1002 NAG A O4 1 HETATM 2325 O O5 . NAG D 2 . ? 24.680 -5.861 7.495 1.00 90.57 ? 1002 NAG A O5 1 HETATM 2326 O O6 . NAG D 2 . ? 27.866 -5.158 7.306 1.00 92.53 ? 1002 NAG A O6 1 HETATM 2327 O O7 . NAG D 2 . ? 21.067 -7.276 3.713 1.00 94.49 ? 1002 NAG A O7 1 HETATM 2328 C C1 . MAN E 3 . ? 27.611 -5.514 4.005 1.00 96.14 ? 1003 MAN A C1 1 HETATM 2329 C C2 . MAN E 3 . ? 28.406 -6.792 4.390 1.00 96.75 ? 1003 MAN A C2 1 HETATM 2330 C C3 . MAN E 3 . ? 29.913 -6.586 4.212 1.00 96.93 ? 1003 MAN A C3 1 HETATM 2331 C C4 . MAN E 3 . ? 30.204 -6.101 2.789 1.00 96.98 ? 1003 MAN A C4 1 HETATM 2332 C C5 . MAN E 3 . ? 29.370 -4.843 2.459 1.00 96.91 ? 1003 MAN A C5 1 HETATM 2333 C C6 . MAN E 3 . ? 29.562 -4.416 1.003 1.00 96.30 ? 1003 MAN A C6 1 HETATM 2334 O O2 . MAN E 3 . ? 27.982 -7.947 3.677 1.00 97.62 ? 1003 MAN A O2 1 HETATM 2335 O O3 . MAN E 3 . ? 30.610 -7.783 4.483 1.00 95.90 ? 1003 MAN A O3 1 HETATM 2336 O O4 . MAN E 3 . ? 31.589 -5.873 2.655 1.00 96.46 ? 1003 MAN A O4 1 HETATM 2337 O O5 . MAN E 3 . ? 27.969 -5.029 2.708 1.00 96.63 ? 1003 MAN A O5 1 HETATM 2338 O O6 . MAN E 3 . ? 29.159 -3.073 0.879 1.00 95.16 ? 1003 MAN A O6 1 HETATM 2339 CU CU . CU F 4 . ? 10.369 -4.997 30.645 1.00 52.69 ? 171 CU A CU 1 HETATM 2340 ZN ZN . ZN G 5 . ? 6.538 -9.194 33.032 1.00 24.30 ? 172 ZN A ZN 1 HETATM 2341 C C1 . NAG H 2 . ? 6.475 14.109 20.599 1.00 38.91 ? 2001 NAG B C1 1 HETATM 2342 C C2 . NAG H 2 . ? 6.534 15.639 20.628 1.00 41.82 ? 2001 NAG B C2 1 HETATM 2343 C C3 . NAG H 2 . ? 7.408 16.128 21.786 1.00 48.69 ? 2001 NAG B C3 1 HETATM 2344 C C4 . NAG H 2 . ? 7.060 15.352 23.073 1.00 51.57 ? 2001 NAG B C4 1 HETATM 2345 C C5 . NAG H 2 . ? 6.954 13.834 22.858 1.00 47.13 ? 2001 NAG B C5 1 HETATM 2346 C C6 . NAG H 2 . ? 6.515 13.046 24.104 1.00 46.14 ? 2001 NAG B C6 1 HETATM 2347 C C7 . NAG H 2 . ? 6.299 16.855 18.500 1.00 41.29 ? 2001 NAG B C7 1 HETATM 2348 C C8 . NAG H 2 . ? 7.035 17.780 17.561 1.00 42.03 ? 2001 NAG B C8 1 HETATM 2349 N N2 . NAG H 2 . ? 7.030 16.163 19.377 1.00 38.69 ? 2001 NAG B N2 1 HETATM 2350 O O3 . NAG H 2 . ? 7.229 17.539 21.956 1.00 48.80 ? 2001 NAG B O3 1 HETATM 2351 O O4 . NAG H 2 . ? 7.808 15.724 24.225 1.00 63.77 ? 2001 NAG B O4 1 HETATM 2352 O O5 . NAG H 2 . ? 5.982 13.680 21.850 1.00 39.81 ? 2001 NAG B O5 1 HETATM 2353 O O6 . NAG H 2 . ? 5.268 13.551 24.548 1.00 46.91 ? 2001 NAG B O6 1 HETATM 2354 O O7 . NAG H 2 . ? 5.068 16.799 18.400 1.00 45.59 ? 2001 NAG B O7 1 HETATM 2355 C C1 . NAG I 2 . ? 6.719 16.149 25.099 1.00 75.28 ? 2002 NAG B C1 1 HETATM 2356 C C2 . NAG I 2 . ? 7.152 16.506 26.525 1.00 80.16 ? 2002 NAG B C2 1 HETATM 2357 C C3 . NAG I 2 . ? 6.534 17.807 27.074 1.00 81.46 ? 2002 NAG B C3 1 HETATM 2358 C C4 . NAG I 2 . ? 5.335 18.443 26.340 1.00 82.15 ? 2002 NAG B C4 1 HETATM 2359 C C5 . NAG I 2 . ? 4.822 17.679 25.130 1.00 82.66 ? 2002 NAG B C5 1 HETATM 2360 C C6 . NAG I 2 . ? 4.034 18.641 24.216 1.00 84.99 ? 2002 NAG B C6 1 HETATM 2361 C C7 . NAG I 2 . ? 6.812 15.443 28.769 1.00 86.04 ? 2002 NAG B C7 1 HETATM 2362 C C8 . NAG I 2 . ? 6.590 14.114 29.463 1.00 86.60 ? 2002 NAG B C8 1 HETATM 2363 N N2 . NAG I 2 . ? 6.901 15.375 27.425 1.00 84.04 ? 2002 NAG B N2 1 HETATM 2364 O O3 . NAG I 2 . ? 7.603 18.730 27.132 1.00 83.51 ? 2002 NAG B O3 1 HETATM 2365 O O4 . NAG I 2 . ? 4.228 18.590 27.200 1.00 82.90 ? 2002 NAG B O4 1 HETATM 2366 O O5 . NAG I 2 . ? 5.928 17.138 24.448 1.00 79.85 ? 2002 NAG B O5 1 HETATM 2367 O O6 . NAG I 2 . ? 4.737 19.011 23.029 1.00 85.91 ? 2002 NAG B O6 1 HETATM 2368 O O7 . NAG I 2 . ? 6.909 16.498 29.429 1.00 85.21 ? 2002 NAG B O7 1 HETATM 2369 CU CU . CU J 4 . ? 6.350 6.851 -0.189 1.00 56.73 ? 171 CU B CU 1 HETATM 2370 ZN ZN . ZN K 5 . ? 1.091 5.874 -3.394 1.00 25.79 ? 172 ZN B ZN 1 HETATM 2371 O O . HOH L 6 . ? 11.376 1.001 16.135 1.00 15.70 ? 1004 HOH A O 1 HETATM 2372 O O . HOH L 6 . ? 11.424 -1.712 14.888 1.00 17.67 ? 1005 HOH A O 1 HETATM 2373 O O . HOH L 6 . ? 6.184 4.895 18.269 1.00 19.32 ? 1006 HOH A O 1 HETATM 2374 O O . HOH L 6 . ? 3.504 -22.940 36.033 1.00 19.72 ? 1007 HOH A O 1 HETATM 2375 O O . HOH L 6 . ? 30.022 -9.235 32.299 1.00 22.11 ? 1008 HOH A O 1 HETATM 2376 O O . HOH L 6 . ? 18.461 -17.096 34.196 1.00 22.27 ? 1009 HOH A O 1 HETATM 2377 O O . HOH L 6 . ? 16.136 2.853 21.941 1.00 23.05 ? 1010 HOH A O 1 HETATM 2378 O O . HOH L 6 . ? 22.289 -8.559 34.459 1.00 23.70 ? 1011 HOH A O 1 HETATM 2379 O O . HOH L 6 . ? 10.492 -13.250 31.989 1.00 26.05 ? 1012 HOH A O 1 HETATM 2380 O O . HOH L 6 . ? 23.463 -6.252 34.225 1.00 26.10 ? 1013 HOH A O 1 HETATM 2381 O O . HOH L 6 . ? 5.175 -4.984 34.090 1.00 26.36 ? 1014 HOH A O 1 HETATM 2382 O O . HOH L 6 . ? 21.260 -18.281 31.709 1.00 27.39 ? 1015 HOH A O 1 HETATM 2383 O O . HOH L 6 . ? -0.416 -8.793 16.368 1.00 27.85 ? 1016 HOH A O 1 HETATM 2384 O O . HOH L 6 . ? -1.092 -5.003 28.826 1.00 28.14 ? 1017 HOH A O 1 HETATM 2385 O O . HOH L 6 . ? -0.816 -11.700 30.188 1.00 28.22 ? 1018 HOH A O 1 HETATM 2386 O O . HOH L 6 . ? 7.119 -2.873 33.362 1.00 28.78 ? 1019 HOH A O 1 HETATM 2387 O O . HOH L 6 . ? 5.348 -17.279 37.711 1.00 29.38 ? 1020 HOH A O 1 HETATM 2388 O O . HOH L 6 . ? 23.850 -2.991 31.907 1.00 29.39 ? 1021 HOH A O 1 HETATM 2389 O O . HOH L 6 . ? 17.576 -16.904 23.137 1.00 29.92 ? 1022 HOH A O 1 HETATM 2390 O O . HOH L 6 . ? 9.748 -2.985 33.077 1.00 30.61 ? 1023 HOH A O 1 HETATM 2391 O O . HOH L 6 . ? 16.072 -9.368 41.719 1.00 30.78 ? 1024 HOH A O 1 HETATM 2392 O O . HOH L 6 . ? 14.024 3.387 20.472 1.00 31.35 ? 1025 HOH A O 1 HETATM 2393 O O . HOH L 6 . ? 12.777 -22.396 22.879 1.00 31.74 ? 1026 HOH A O 1 HETATM 2394 O O . HOH L 6 . ? 16.497 1.100 19.662 1.00 31.89 ? 1027 HOH A O 1 HETATM 2395 O O . HOH L 6 . ? 0.213 -16.675 3.292 1.00 32.11 ? 1028 HOH A O 1 HETATM 2396 O O . HOH L 6 . ? 14.054 0.863 16.357 1.00 32.23 ? 1029 HOH A O 1 HETATM 2397 O O . HOH L 6 . ? 6.114 1.393 33.222 1.00 32.54 ? 1030 HOH A O 1 HETATM 2398 O O . HOH L 6 . ? 19.999 -15.352 24.480 1.00 32.95 ? 1031 HOH A O 1 HETATM 2399 O O . HOH L 6 . ? 17.901 -14.191 37.073 1.00 33.16 ? 1032 HOH A O 1 HETATM 2400 O O . HOH L 6 . ? -3.773 -14.101 20.254 1.00 33.24 ? 1033 HOH A O 1 HETATM 2401 O O . HOH L 6 . ? -2.899 -7.668 20.814 1.00 33.58 ? 1034 HOH A O 1 HETATM 2402 O O . HOH L 6 . ? 3.017 -20.699 37.123 1.00 34.22 ? 1035 HOH A O 1 HETATM 2403 O O . HOH L 6 . ? -0.402 -14.370 30.659 1.00 34.46 ? 1036 HOH A O 1 HETATM 2404 O O . HOH L 6 . ? 11.870 -15.733 13.609 1.00 34.54 ? 1037 HOH A O 1 HETATM 2405 O O . HOH L 6 . ? 9.181 -14.047 -7.440 1.00 34.93 ? 1038 HOH A O 1 HETATM 2406 O O . HOH L 6 . ? 17.597 -8.284 38.285 1.00 35.01 ? 1039 HOH A O 1 HETATM 2407 O O . HOH L 6 . ? 29.457 -4.245 20.700 1.00 35.37 ? 1040 HOH A O 1 HETATM 2408 O O . HOH L 6 . ? 2.085 -20.965 -2.623 1.00 35.37 ? 1041 HOH A O 1 HETATM 2409 O O . HOH L 6 . ? -4.663 -3.170 22.706 1.00 35.75 ? 1042 HOH A O 1 HETATM 2410 O O . HOH L 6 . ? 15.353 -15.432 40.123 1.00 36.09 ? 1043 HOH A O 1 HETATM 2411 O O . HOH L 6 . ? 1.986 -7.617 36.819 1.00 36.43 ? 1044 HOH A O 1 HETATM 2412 O O . HOH L 6 . ? 15.005 3.526 31.905 1.00 36.69 ? 1045 HOH A O 1 HETATM 2413 O O . HOH L 6 . ? 9.997 -17.324 25.599 1.00 37.01 ? 1046 HOH A O 1 HETATM 2414 O O . HOH L 6 . ? 1.180 -0.225 30.026 1.00 37.05 ? 1047 HOH A O 1 HETATM 2415 O O . HOH L 6 . ? 11.789 -2.546 37.566 1.00 37.36 ? 1048 HOH A O 1 HETATM 2416 O O . HOH L 6 . ? 11.557 -5.139 33.549 1.00 38.41 ? 1049 HOH A O 1 HETATM 2417 O O . HOH L 6 . ? 9.118 -17.410 -5.165 1.00 38.44 ? 1050 HOH A O 1 HETATM 2418 O O . HOH L 6 . ? 17.649 4.046 23.630 1.00 38.77 ? 1051 HOH A O 1 HETATM 2419 O O . HOH L 6 . ? 15.127 -16.800 30.411 1.00 38.81 ? 1052 HOH A O 1 HETATM 2420 O O . HOH L 6 . ? 2.048 -12.709 -10.531 1.00 40.45 ? 1053 HOH A O 1 HETATM 2421 O O . HOH L 6 . ? 3.572 -3.864 35.779 1.00 40.91 ? 1054 HOH A O 1 HETATM 2422 O O . HOH L 6 . ? 33.833 -7.714 28.665 1.00 41.47 ? 1055 HOH A O 1 HETATM 2423 O O . HOH L 6 . ? 21.850 6.151 22.205 1.00 41.92 ? 1056 HOH A O 1 HETATM 2424 O O . HOH L 6 . ? -4.525 -5.382 25.223 1.00 42.00 ? 1057 HOH A O 1 HETATM 2425 O O . HOH L 6 . ? 6.798 -0.583 34.303 1.00 42.06 ? 1058 HOH A O 1 HETATM 2426 O O . HOH L 6 . ? 32.543 -8.357 30.870 1.00 42.69 ? 1059 HOH A O 1 HETATM 2427 O O . HOH L 6 . ? 20.968 -20.289 17.504 1.00 42.94 ? 1060 HOH A O 1 HETATM 2428 O O . HOH L 6 . ? -2.963 -1.834 24.339 1.00 43.60 ? 1061 HOH A O 1 HETATM 2429 O O . HOH L 6 . ? 6.993 -15.126 -9.319 1.00 44.27 ? 1062 HOH A O 1 HETATM 2430 O O . HOH L 6 . ? 12.146 -2.878 34.520 1.00 44.56 ? 1063 HOH A O 1 HETATM 2431 O O . HOH L 6 . ? 12.382 7.737 19.897 1.00 44.70 ? 1064 HOH A O 1 HETATM 2432 O O . HOH L 6 . ? -1.557 -5.480 16.028 1.00 44.86 ? 1065 HOH A O 1 HETATM 2433 O O . HOH L 6 . ? 7.137 -20.122 26.239 1.00 45.06 ? 1066 HOH A O 1 HETATM 2434 O O . HOH L 6 . ? 22.181 -6.933 12.847 1.00 45.25 ? 1067 HOH A O 1 HETATM 2435 O O . HOH L 6 . ? 11.796 -0.133 33.486 1.00 45.89 ? 1068 HOH A O 1 HETATM 2436 O O . HOH L 6 . ? 7.358 -27.710 10.989 1.00 46.39 ? 1069 HOH A O 1 HETATM 2437 O O . HOH L 6 . ? -5.012 -0.850 22.684 1.00 46.47 ? 1070 HOH A O 1 HETATM 2438 O O . HOH L 6 . ? 9.441 -9.887 3.953 1.00 46.53 ? 1071 HOH A O 1 HETATM 2439 O O . HOH L 6 . ? -1.611 -12.907 42.289 1.00 46.98 ? 1072 HOH A O 1 HETATM 2440 O O . HOH L 6 . ? 36.451 -14.364 20.470 1.00 47.73 ? 1073 HOH A O 1 HETATM 2441 O O . HOH L 6 . ? -1.153 -8.027 37.573 1.00 48.13 ? 1074 HOH A O 1 HETATM 2442 O O . HOH L 6 . ? -8.927 -11.097 30.189 1.00 48.93 ? 1075 HOH A O 1 HETATM 2443 O O . HOH L 6 . ? -0.705 -11.694 10.951 1.00 49.19 ? 1076 HOH A O 1 HETATM 2444 O O . HOH L 6 . ? -1.266 -8.604 41.932 1.00 49.52 ? 1077 HOH A O 1 HETATM 2445 O O . HOH L 6 . ? 26.609 -17.062 20.189 1.00 49.58 ? 1078 HOH A O 1 HETATM 2446 O O . HOH L 6 . ? 18.890 2.995 34.608 1.00 49.76 ? 1079 HOH A O 1 HETATM 2447 O O . HOH L 6 . ? 22.751 -16.536 23.421 1.00 49.92 ? 1080 HOH A O 1 HETATM 2448 O O . HOH L 6 . ? 2.982 -14.194 -3.969 1.00 50.28 ? 1081 HOH A O 1 HETATM 2449 O O . HOH L 6 . ? 26.051 -5.122 14.907 1.00 50.96 ? 1082 HOH A O 1 HETATM 2450 O O . HOH L 6 . ? -1.945 -5.238 13.327 1.00 52.05 ? 1083 HOH A O 1 HETATM 2451 O O . HOH L 6 . ? 34.849 -11.633 31.520 1.00 52.12 ? 1084 HOH A O 1 HETATM 2452 O O . HOH L 6 . ? -5.381 -7.734 24.155 1.00 52.19 ? 1085 HOH A O 1 HETATM 2453 O O . HOH L 6 . ? 38.163 -15.462 27.524 1.00 52.92 ? 1086 HOH A O 1 HETATM 2454 O O . HOH L 6 . ? 18.497 -0.488 38.430 1.00 53.49 ? 1087 HOH A O 1 HETATM 2455 O O . HOH L 6 . ? 12.379 7.222 28.422 1.00 55.97 ? 1088 HOH A O 1 HETATM 2456 O O . HOH L 6 . ? 25.591 -14.997 22.122 1.00 56.01 ? 1089 HOH A O 1 HETATM 2457 O O . HOH L 6 . ? 13.322 10.070 24.881 1.00 57.97 ? 1090 HOH A O 1 HETATM 2458 O O . HOH L 6 . ? 35.580 -16.084 25.528 1.00 62.42 ? 1091 HOH A O 1 HETATM 2459 O O . HOH L 6 . ? 10.719 -25.419 29.152 1.00 68.42 ? 1092 HOH A O 1 HETATM 2460 O O . HOH L 6 . ? -3.072 -5.410 27.032 1.00 70.89 ? 1093 HOH A O 1 HETATM 2461 O O . HOH M 6 . ? 10.081 3.429 14.715 1.00 13.59 ? 2003 HOH B O 1 HETATM 2462 O O . HOH M 6 . ? 7.475 4.772 15.839 1.00 15.65 ? 2004 HOH B O 1 HETATM 2463 O O . HOH M 6 . ? 11.335 -2.710 12.278 1.00 22.67 ? 2005 HOH B O 1 HETATM 2464 O O . HOH M 6 . ? 1.037 19.647 6.939 1.00 25.32 ? 2006 HOH B O 1 HETATM 2465 O O . HOH M 6 . ? 14.316 7.397 10.040 1.00 26.90 ? 2007 HOH B O 1 HETATM 2466 O O . HOH M 6 . ? 2.286 23.318 8.867 1.00 27.04 ? 2008 HOH B O 1 HETATM 2467 O O . HOH M 6 . ? -6.769 1.803 -2.550 1.00 28.14 ? 2009 HOH B O 1 HETATM 2468 O O . HOH M 6 . ? -4.784 11.206 15.988 1.00 28.87 ? 2010 HOH B O 1 HETATM 2469 O O . HOH M 6 . ? -1.083 11.042 -2.214 1.00 30.09 ? 2011 HOH B O 1 HETATM 2470 O O . HOH M 6 . ? -4.031 -2.212 11.974 1.00 30.31 ? 2012 HOH B O 1 HETATM 2471 O O . HOH M 6 . ? 15.852 7.040 0.024 1.00 30.38 ? 2013 HOH B O 1 HETATM 2472 O O . HOH M 6 . ? 14.431 17.774 1.055 1.00 30.90 ? 2014 HOH B O 1 HETATM 2473 O O . HOH M 6 . ? 3.338 20.370 -4.017 1.00 30.92 ? 2015 HOH B O 1 HETATM 2474 O O . HOH M 6 . ? -9.881 17.938 7.754 1.00 32.11 ? 2016 HOH B O 1 HETATM 2475 O O . HOH M 6 . ? 9.954 -0.108 -2.178 1.00 32.26 ? 2017 HOH B O 1 HETATM 2476 O O . HOH M 6 . ? 0.883 -3.032 -0.307 1.00 32.54 ? 2018 HOH B O 1 HETATM 2477 O O . HOH M 6 . ? 8.281 5.618 -2.210 1.00 32.56 ? 2019 HOH B O 1 HETATM 2478 O O . HOH M 6 . ? -4.570 0.120 -2.172 1.00 32.66 ? 2020 HOH B O 1 HETATM 2479 O O . HOH M 6 . ? 9.307 20.557 -1.416 1.00 34.19 ? 2021 HOH B O 1 HETATM 2480 O O . HOH M 6 . ? 6.159 -3.222 -0.482 1.00 34.49 ? 2022 HOH B O 1 HETATM 2481 O O . HOH M 6 . ? 7.019 22.918 -1.813 1.00 34.58 ? 2023 HOH B O 1 HETATM 2482 O O . HOH M 6 . ? 16.645 12.595 8.066 1.00 34.69 ? 2024 HOH B O 1 HETATM 2483 O O . HOH M 6 . ? 4.935 26.717 4.184 1.00 35.20 ? 2025 HOH B O 1 HETATM 2484 O O . HOH M 6 . ? 2.754 18.116 -10.416 1.00 35.45 ? 2026 HOH B O 1 HETATM 2485 O O . HOH M 6 . ? 1.936 -6.590 4.169 1.00 35.48 ? 2027 HOH B O 1 HETATM 2486 O O . HOH M 6 . ? 6.683 3.289 -3.303 1.00 35.70 ? 2028 HOH B O 1 HETATM 2487 O O . HOH M 6 . ? -1.048 18.192 5.748 1.00 35.81 ? 2029 HOH B O 1 HETATM 2488 O O . HOH M 6 . ? 12.761 7.938 12.333 1.00 35.86 ? 2030 HOH B O 1 HETATM 2489 O O . HOH M 6 . ? 19.934 10.102 11.579 1.00 36.08 ? 2031 HOH B O 1 HETATM 2490 O O . HOH M 6 . ? -3.603 -4.667 7.246 1.00 36.56 ? 2032 HOH B O 1 HETATM 2491 O O . HOH M 6 . ? -9.464 8.716 -9.108 1.00 36.92 ? 2033 HOH B O 1 HETATM 2492 O O . HOH M 6 . ? 5.313 21.749 -4.105 1.00 37.23 ? 2034 HOH B O 1 HETATM 2493 O O . HOH M 6 . ? 9.507 32.547 14.526 1.00 37.24 ? 2035 HOH B O 1 HETATM 2494 O O . HOH M 6 . ? 14.001 5.251 11.344 1.00 37.38 ? 2036 HOH B O 1 HETATM 2495 O O . HOH M 6 . ? 8.173 16.184 -6.362 1.00 37.55 ? 2037 HOH B O 1 HETATM 2496 O O . HOH M 6 . ? 11.621 12.296 17.616 1.00 37.88 ? 2038 HOH B O 1 HETATM 2497 O O . HOH M 6 . ? -8.375 16.469 6.369 1.00 38.05 ? 2039 HOH B O 1 HETATM 2498 O O . HOH M 6 . ? 0.687 1.664 -7.922 1.00 38.99 ? 2040 HOH B O 1 HETATM 2499 O O . HOH M 6 . ? 8.484 19.770 20.396 1.00 39.06 ? 2041 HOH B O 1 HETATM 2500 O O . HOH M 6 . ? 16.283 7.550 8.770 1.00 39.22 ? 2042 HOH B O 1 HETATM 2501 O O . HOH M 6 . ? 11.630 6.086 -2.158 1.00 39.34 ? 2043 HOH B O 1 HETATM 2502 O O . HOH M 6 . ? 6.298 15.455 -10.509 1.00 39.84 ? 2044 HOH B O 1 HETATM 2503 O O . HOH M 6 . ? -10.078 -2.822 -5.911 1.00 40.00 ? 2045 HOH B O 1 HETATM 2504 O O . HOH M 6 . ? 9.943 18.626 16.891 1.00 40.05 ? 2046 HOH B O 1 HETATM 2505 O O . HOH M 6 . ? 5.074 18.421 -7.267 1.00 40.17 ? 2047 HOH B O 1 HETATM 2506 O O . HOH M 6 . ? -2.485 18.437 7.714 1.00 40.73 ? 2048 HOH B O 1 HETATM 2507 O O . HOH M 6 . ? 16.979 1.463 11.970 1.00 40.77 ? 2049 HOH B O 1 HETATM 2508 O O . HOH M 6 . ? 0.741 17.286 -9.500 1.00 40.89 ? 2050 HOH B O 1 HETATM 2509 O O . HOH M 6 . ? 18.841 -0.621 2.756 1.00 40.93 ? 2051 HOH B O 1 HETATM 2510 O O . HOH M 6 . ? 5.872 32.601 12.876 1.00 41.04 ? 2052 HOH B O 1 HETATM 2511 O O . HOH M 6 . ? 3.009 18.547 -5.637 1.00 41.34 ? 2053 HOH B O 1 HETATM 2512 O O . HOH M 6 . ? 9.261 12.643 19.173 1.00 41.44 ? 2054 HOH B O 1 HETATM 2513 O O . HOH M 6 . ? 2.829 16.207 18.344 1.00 41.50 ? 2055 HOH B O 1 HETATM 2514 O O . HOH M 6 . ? 11.148 5.852 14.986 1.00 41.53 ? 2056 HOH B O 1 HETATM 2515 O O . HOH M 6 . ? -2.078 -6.221 2.803 1.00 41.62 ? 2057 HOH B O 1 HETATM 2516 O O . HOH M 6 . ? 9.069 -2.499 -2.892 1.00 41.65 ? 2058 HOH B O 1 HETATM 2517 O O . HOH M 6 . ? 13.616 11.708 -7.393 1.00 41.77 ? 2059 HOH B O 1 HETATM 2518 O O . HOH M 6 . ? 12.289 30.307 6.901 1.00 41.96 ? 2060 HOH B O 1 HETATM 2519 O O . HOH M 6 . ? -9.747 -2.318 7.136 1.00 42.33 ? 2061 HOH B O 1 HETATM 2520 O O . HOH M 6 . ? 16.957 15.200 16.117 1.00 42.47 ? 2062 HOH B O 1 HETATM 2521 O O . HOH M 6 . ? -0.460 -5.320 0.785 1.00 42.58 ? 2063 HOH B O 1 HETATM 2522 O O . HOH M 6 . ? 14.337 29.007 6.278 1.00 43.13 ? 2064 HOH B O 1 HETATM 2523 O O . HOH M 6 . ? -5.743 10.457 20.485 1.00 43.48 ? 2065 HOH B O 1 HETATM 2524 O O . HOH M 6 . ? 9.069 19.417 -3.865 1.00 43.53 ? 2066 HOH B O 1 HETATM 2525 O O . HOH M 6 . ? 10.074 8.987 -6.770 1.00 43.65 ? 2067 HOH B O 1 HETATM 2526 O O . HOH M 6 . ? -11.650 10.263 -8.168 1.00 43.76 ? 2068 HOH B O 1 HETATM 2527 O O . HOH M 6 . ? -1.066 17.218 17.336 1.00 44.05 ? 2069 HOH B O 1 HETATM 2528 O O . HOH M 6 . ? -4.399 -6.226 4.041 1.00 44.36 ? 2070 HOH B O 1 HETATM 2529 O O . HOH M 6 . ? 10.201 28.052 0.665 1.00 44.41 ? 2071 HOH B O 1 HETATM 2530 O O . HOH M 6 . ? 4.750 20.511 18.592 1.00 44.74 ? 2072 HOH B O 1 HETATM 2531 O O . HOH M 6 . ? 12.545 6.464 17.241 1.00 44.94 ? 2073 HOH B O 1 HETATM 2532 O O . HOH M 6 . ? 3.870 7.431 -13.926 1.00 45.52 ? 2074 HOH B O 1 HETATM 2533 O O . HOH M 6 . ? -13.285 11.613 -0.485 1.00 46.56 ? 2075 HOH B O 1 HETATM 2534 O O . HOH M 6 . ? 16.337 8.512 19.535 1.00 46.74 ? 2076 HOH B O 1 HETATM 2535 O O . HOH M 6 . ? 4.450 -7.101 -0.651 1.00 47.53 ? 2077 HOH B O 1 HETATM 2536 O O . HOH M 6 . ? -10.619 -7.017 9.990 1.00 47.58 ? 2078 HOH B O 1 HETATM 2537 O O . HOH M 6 . ? 2.215 25.919 10.819 1.00 47.80 ? 2079 HOH B O 1 HETATM 2538 O O . HOH M 6 . ? -13.342 10.236 -3.879 1.00 47.91 ? 2080 HOH B O 1 HETATM 2539 O O . HOH M 6 . ? 12.361 0.078 -1.142 1.00 48.13 ? 2081 HOH B O 1 HETATM 2540 O O . HOH M 6 . ? 19.024 10.755 16.084 1.00 48.32 ? 2082 HOH B O 1 HETATM 2541 O O . HOH M 6 . ? -8.536 17.289 -4.407 1.00 48.67 ? 2083 HOH B O 1 HETATM 2542 O O . HOH M 6 . ? 1.479 19.466 16.675 1.00 49.25 ? 2084 HOH B O 1 HETATM 2543 O O . HOH M 6 . ? 6.460 -1.818 -5.573 1.00 49.41 ? 2085 HOH B O 1 HETATM 2544 O O . HOH M 6 . ? 16.651 11.546 0.108 1.00 50.07 ? 2086 HOH B O 1 HETATM 2545 O O . HOH M 6 . ? 16.291 13.086 17.580 1.00 50.52 ? 2087 HOH B O 1 HETATM 2546 O O . HOH M 6 . ? 9.159 15.707 18.639 1.00 50.59 ? 2088 HOH B O 1 HETATM 2547 O O . HOH M 6 . ? 16.988 15.484 6.207 1.00 51.57 ? 2089 HOH B O 1 HETATM 2548 O O . HOH M 6 . ? -0.167 -7.558 5.209 1.00 52.11 ? 2090 HOH B O 1 HETATM 2549 O O . HOH M 6 . ? 17.708 6.589 20.937 1.00 52.82 ? 2091 HOH B O 1 HETATM 2550 O O . HOH M 6 . ? 17.109 17.552 15.076 1.00 52.95 ? 2092 HOH B O 1 HETATM 2551 O O . HOH M 6 . ? -5.034 22.925 11.248 1.00 53.06 ? 2093 HOH B O 1 HETATM 2552 O O . HOH M 6 . ? -11.479 -2.594 -3.073 1.00 53.69 ? 2094 HOH B O 1 HETATM 2553 O O . HOH M 6 . ? 17.814 10.758 2.014 1.00 54.58 ? 2095 HOH B O 1 HETATM 2554 O O . HOH M 6 . ? 1.845 24.696 0.282 1.00 55.44 ? 2096 HOH B O 1 HETATM 2555 O O . HOH M 6 . ? -13.230 14.289 -3.660 1.00 56.80 ? 2097 HOH B O 1 HETATM 2556 O O . HOH M 6 . ? 4.096 24.071 -6.357 1.00 57.82 ? 2098 HOH B O 1 HETATM 2557 O O . HOH M 6 . ? 2.391 -8.029 2.168 1.00 58.65 ? 2099 HOH B O 1 HETATM 2558 O O . HOH M 6 . ? -0.991 -0.485 -8.766 1.00 58.68 ? 2100 HOH B O 1 HETATM 2559 O O . HOH M 6 . ? -16.433 1.969 8.826 1.00 59.81 ? 2101 HOH B O 1 HETATM 2560 O O . HOH M 6 . ? 2.150 24.435 -3.906 1.00 59.84 ? 2102 HOH B O 1 HETATM 2561 O O . HOH M 6 . ? -22.528 5.760 6.897 1.00 60.71 ? 2103 HOH B O 1 HETATM 2562 O O . HOH M 6 . ? -5.500 14.600 20.482 1.00 62.51 ? 2104 HOH B O 1 HETATM 2563 O O . HOH M 6 . ? -12.969 8.437 -1.072 1.00 63.09 ? 2105 HOH B O 1 HETATM 2564 O O . HOH M 6 . ? -7.977 0.613 -9.516 1.00 63.15 ? 2106 HOH B O 1 HETATM 2565 O O . HOH M 6 . ? 6.471 33.702 10.188 1.00 64.05 ? 2107 HOH B O 1 HETATM 2566 O O . HOH M 6 . ? 7.085 16.504 -14.837 1.00 65.12 ? 2108 HOH B O 1 HETATM 2567 O O . HOH M 6 . ? -6.119 -4.391 15.087 1.00 66.79 ? 2109 HOH B O 1 HETATM 2568 O O . HOH M 6 . ? -1.690 18.721 15.301 1.00 67.07 ? 2110 HOH B O 1 HETATM 2569 O O . HOH M 6 . ? 19.326 14.049 8.813 1.00 68.24 ? 2111 HOH B O 1 HETATM 2570 O O . HOH M 6 . ? -20.828 3.397 7.811 1.00 74.62 ? 2112 HOH B O 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 HIS 1 1 ? ? ? A . n A 1 2 HIS 2 2 2 HIS HIS A . n A 1 3 GLY 3 3 3 GLY GLY A . n A 1 4 PHE 4 4 4 PHE PHE A . n A 1 5 THR 5 5 5 THR THR A . n A 1 6 THR 6 6 6 THR THR A . n A 1 7 PRO 7 7 7 PRO PRO A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 ARG 9 9 9 ARG ARG A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 ILE 11 11 11 ILE ILE A . n A 1 12 ALA 12 12 12 ALA ALA A . n A 1 13 VAL 13 13 13 VAL VAL 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 THR 16 16 16 THR THR A . n A 1 17 GLU 17 17 17 GLU GLU A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 ARG 20 20 20 ARG ARG A . n A 1 21 GLY 21 21 21 GLY GLY A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 ILE 23 23 23 ILE ILE A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 PHE 25 25 25 PHE PHE A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 GLN 27 27 27 GLN GLN A . n A 1 28 VAL 28 28 28 VAL VAL A . n A 1 29 GLN 29 29 29 GLN GLN A . n A 1 30 ASP 30 30 30 ASP ASP A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 LYS 32 32 32 LYS LYS A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 HIS 34 34 34 HIS HIS A . n A 1 35 VAL 35 35 35 VAL VAL A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 GLY 37 37 37 GLY GLY A . n A 1 38 GLY 38 38 38 GLY GLY A . n A 1 39 ILE 39 39 39 ILE ILE A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 GLY 41 41 41 GLY GLY A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 PRO 43 43 43 PRO PRO A . n A 1 44 PRO 44 44 44 PRO PRO A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 TYR 47 47 47 TYR TYR A . n A 1 48 GLY 48 48 48 GLY GLY A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 HIS 50 50 50 HIS HIS A . n A 1 51 VAL 51 51 51 VAL VAL A . n A 1 52 HIS 52 52 52 HIS HIS A . n A 1 53 GLU 53 53 53 GLU GLU A . n A 1 54 LYS 54 54 54 LYS LYS A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 ASP 56 56 56 ASP ASP A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 CYS 61 61 61 CYS CYS A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 SER 63 63 63 SER SER A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 SER 66 66 66 SER SER A . n A 1 67 HIS 67 67 67 HIS HIS A . n A 1 68 PHE 68 68 68 PHE PHE A . n A 1 69 ASN 69 69 69 ASN ASN A . n A 1 70 PRO 70 70 70 PRO PRO A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 HIS 72 72 72 HIS HIS A . n A 1 73 LYS 73 73 73 LYS LYS A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 HIS 75 75 75 HIS HIS A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 HIS 77 77 77 HIS HIS A . n A 1 78 PRO 78 78 78 PRO PRO A . n A 1 79 ASN 79 79 79 ASN ASN A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 VAL 81 81 81 VAL VAL A . n A 1 82 ASN 82 82 82 ASN ASN A . n A 1 83 ARG 83 83 83 ARG ARG A . n A 1 84 HIS 84 84 84 HIS HIS A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 GLY 86 86 86 GLY GLY A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 LEU 88 88 88 LEU LEU A . n A 1 89 GLY 89 89 89 GLY GLY A . n A 1 90 ASN 90 90 90 ASN ASN A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 VAL 92 92 92 VAL VAL A . n A 1 93 PHE 93 93 93 PHE PHE A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 GLU 95 95 95 GLU GLU A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 HIS 97 97 97 HIS HIS A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 SER 99 99 99 SER SER A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 ILE 101 101 101 ILE ILE A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 LEU 103 103 103 LEU LEU A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 ASP 105 105 105 ASP ASP A . n A 1 106 ASP 106 106 106 ASP ASP A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 SER 109 109 109 SER SER A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 SER 111 111 111 SER SER A . n A 1 112 GLY 112 112 112 GLY GLY A . n A 1 113 PRO 113 113 113 PRO PRO A . n A 1 114 HIS 114 114 114 HIS HIS A . n A 1 115 GLY 115 115 115 GLY GLY A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 ARG 119 119 119 ARG ARG A . n A 1 120 ALA 120 120 120 ALA ALA A . n A 1 121 VAL 121 121 121 VAL VAL A . n A 1 122 VAL 122 122 122 VAL VAL A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 HIS 124 124 124 HIS HIS A . n A 1 125 GLU 125 125 125 GLU GLU A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 ASP 128 128 128 ASP ASP A . n A 1 129 ASP 129 129 129 ASP ASP A . n A 1 130 TYR 130 130 130 TYR TYR A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 LYS 132 132 132 LYS LYS A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ASP 134 134 134 ASP ASP A . n A 1 135 HIS 135 135 135 HIS HIS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 SER 138 138 138 SER SER A . n A 1 139 ARG 139 139 139 ARG ARG A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 THR 141 141 141 THR THR A . n A 1 142 GLY 142 142 142 GLY GLY A . n A 1 143 ASN 143 143 143 ASN ASN A . n A 1 144 ALA 144 144 144 ALA ALA A . n A 1 145 GLY 145 145 145 GLY GLY A . n A 1 146 GLY 146 146 146 GLY GLY A . n A 1 147 ARG 147 147 147 ARG ARG A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 ALA 149 149 149 ALA ALA A . n A 1 150 CYS 150 150 150 CYS CYS A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 ILE 153 153 153 ILE ILE A . n A 1 154 GLY 154 154 154 GLY GLY A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 LEU 156 156 156 LEU LEU A . n B 1 1 HIS 1 1 ? ? ? B . n B 1 2 HIS 2 2 ? ? ? B . n B 1 3 GLY 3 3 ? ? ? B . n B 1 4 PHE 4 4 ? ? ? B . n B 1 5 THR 5 5 5 THR THR B . n B 1 6 THR 6 6 6 THR THR B . n B 1 7 PRO 7 7 7 PRO PRO B . n B 1 8 SER 8 8 8 SER SER B . n B 1 9 ARG 9 9 9 ARG ARG B . n B 1 10 ALA 10 10 10 ALA ALA B . n B 1 11 ILE 11 11 11 ILE ILE B . n B 1 12 ALA 12 12 12 ALA ALA B . n B 1 13 VAL 13 13 13 VAL VAL B . n B 1 14 LEU 14 14 14 LEU LEU B . n B 1 15 SER 15 15 15 SER SER B . n B 1 16 THR 16 16 16 THR THR B . n B 1 17 GLU 17 17 17 GLU GLU B . n B 1 18 THR 18 18 18 THR THR B . n B 1 19 ILE 19 19 19 ILE ILE B . n B 1 20 ARG 20 20 20 ARG ARG B . n B 1 21 GLY 21 21 21 GLY GLY B . n B 1 22 ASN 22 22 22 ASN ASN B . n B 1 23 ILE 23 23 23 ILE ILE B . n B 1 24 THR 24 24 24 THR THR B . n B 1 25 PHE 25 25 25 PHE PHE B . n B 1 26 THR 26 26 26 THR THR B . n B 1 27 GLN 27 27 27 GLN GLN B . n B 1 28 VAL 28 28 28 VAL VAL B . n B 1 29 GLN 29 29 29 GLN GLN B . n B 1 30 ASP 30 30 30 ASP ASP B . n B 1 31 GLY 31 31 31 GLY GLY B . n B 1 32 LYS 32 32 32 LYS LYS B . n B 1 33 VAL 33 33 33 VAL VAL B . n B 1 34 HIS 34 34 34 HIS HIS B . n B 1 35 VAL 35 35 35 VAL VAL B . n B 1 36 GLN 36 36 36 GLN GLN B . n B 1 37 GLY 37 37 37 GLY GLY B . n B 1 38 GLY 38 38 38 GLY GLY B . n B 1 39 ILE 39 39 39 ILE ILE B . n B 1 40 THR 40 40 40 THR THR B . n B 1 41 GLY 41 41 41 GLY GLY B . n B 1 42 LEU 42 42 42 LEU LEU B . n B 1 43 PRO 43 43 43 PRO PRO B . n B 1 44 PRO 44 44 44 PRO PRO B . n B 1 45 GLY 45 45 45 GLY GLY B . n B 1 46 GLU 46 46 46 GLU GLU B . n B 1 47 TYR 47 47 47 TYR TYR B . n B 1 48 GLY 48 48 48 GLY GLY B . n B 1 49 PHE 49 49 49 PHE PHE B . n B 1 50 HIS 50 50 50 HIS HIS B . n B 1 51 VAL 51 51 51 VAL VAL B . n B 1 52 HIS 52 52 52 HIS HIS B . n B 1 53 GLU 53 53 53 GLU GLU B . n B 1 54 LYS 54 54 54 LYS LYS B . n B 1 55 GLY 55 55 55 GLY GLY B . n B 1 56 ASP 56 56 56 ASP ASP B . n B 1 57 LEU 57 57 57 LEU LEU B . n B 1 58 SER 58 58 58 SER SER B . n B 1 59 GLY 59 59 59 GLY GLY B . n B 1 60 GLY 60 60 60 GLY GLY B . n B 1 61 CYS 61 61 61 CYS CYS B . n B 1 62 LEU 62 62 62 LEU LEU B . n B 1 63 SER 63 63 63 SER SER B . n B 1 64 THR 64 64 64 THR THR B . n B 1 65 GLY 65 65 65 GLY GLY B . n B 1 66 SER 66 66 66 SER SER B . n B 1 67 HIS 67 67 67 HIS HIS B . n B 1 68 PHE 68 68 68 PHE PHE B . n B 1 69 ASN 69 69 69 ASN ASN B . n B 1 70 PRO 70 70 70 PRO PRO B . n B 1 71 GLU 71 71 71 GLU GLU B . n B 1 72 HIS 72 72 72 HIS HIS B . n B 1 73 LYS 73 73 73 LYS LYS B . n B 1 74 ASP 74 74 74 ASP ASP B . n B 1 75 HIS 75 75 75 HIS HIS B . n B 1 76 GLY 76 76 76 GLY GLY B . n B 1 77 HIS 77 77 77 HIS HIS B . n B 1 78 PRO 78 78 78 PRO PRO B . n B 1 79 ASN 79 79 79 ASN ASN B . n B 1 80 ASP 80 80 80 ASP ASP B . n B 1 81 VAL 81 81 81 VAL VAL B . n B 1 82 ASN 82 82 82 ASN ASN B . n B 1 83 ARG 83 83 83 ARG ARG B . n B 1 84 HIS 84 84 84 HIS HIS B . n B 1 85 VAL 85 85 85 VAL VAL B . n B 1 86 GLY 86 86 86 GLY GLY B . n B 1 87 ASP 87 87 87 ASP ASP B . n B 1 88 LEU 88 88 88 LEU LEU B . n B 1 89 GLY 89 89 89 GLY GLY B . n B 1 90 ASN 90 90 90 ASN ASN B . n B 1 91 VAL 91 91 91 VAL VAL B . n B 1 92 VAL 92 92 92 VAL VAL B . n B 1 93 PHE 93 93 93 PHE PHE B . n B 1 94 ASP 94 94 94 ASP ASP B . n B 1 95 GLU 95 95 95 GLU GLU B . n B 1 96 ASN 96 96 96 ASN ASN B . n B 1 97 HIS 97 97 97 HIS HIS B . n B 1 98 TYR 98 98 98 TYR TYR B . n B 1 99 SER 99 99 99 SER SER B . n B 1 100 ARG 100 100 100 ARG ARG B . n B 1 101 ILE 101 101 101 ILE ILE B . n B 1 102 ASP 102 102 102 ASP ASP B . n B 1 103 LEU 103 103 103 LEU LEU B . n B 1 104 VAL 104 104 104 VAL VAL B . n B 1 105 ASP 105 105 105 ASP ASP B . n B 1 106 ASP 106 106 106 ASP ASP B . n B 1 107 GLN 107 107 107 GLN GLN B . n B 1 108 ILE 108 108 108 ILE ILE B . n B 1 109 SER 109 109 109 SER SER B . n B 1 110 LEU 110 110 110 LEU LEU B . n B 1 111 SER 111 111 111 SER SER B . n B 1 112 GLY 112 112 112 GLY GLY B . n B 1 113 PRO 113 113 113 PRO PRO B . n B 1 114 HIS 114 114 114 HIS HIS B . n B 1 115 GLY 115 115 115 GLY GLY B . n B 1 116 ILE 116 116 116 ILE ILE B . n B 1 117 ILE 117 117 117 ILE ILE B . n B 1 118 GLY 118 118 118 GLY GLY B . n B 1 119 ARG 119 119 119 ARG ARG B . n B 1 120 ALA 120 120 120 ALA ALA B . n B 1 121 VAL 121 121 121 VAL VAL B . n B 1 122 VAL 122 122 122 VAL VAL B . n B 1 123 LEU 123 123 123 LEU LEU B . n B 1 124 HIS 124 124 124 HIS HIS B . n B 1 125 GLU 125 125 125 GLU GLU B . n B 1 126 LYS 126 126 126 LYS LYS B . n B 1 127 ALA 127 127 127 ALA ALA B . n B 1 128 ASP 128 128 128 ASP ASP B . n B 1 129 ASP 129 129 129 ASP ASP B . n B 1 130 TYR 130 130 130 TYR TYR B . n B 1 131 GLY 131 131 131 GLY GLY B . n B 1 132 LYS 132 132 132 LYS LYS B . n B 1 133 SER 133 133 133 SER SER B . n B 1 134 ASP 134 134 134 ASP ASP B . n B 1 135 HIS 135 135 135 HIS HIS B . n B 1 136 PRO 136 136 136 PRO PRO B . n B 1 137 ASP 137 137 137 ASP ASP B . n B 1 138 SER 138 138 138 SER SER B . n B 1 139 ARG 139 139 139 ARG ARG B . n B 1 140 LYS 140 140 140 LYS LYS B . n B 1 141 THR 141 141 141 THR THR B . n B 1 142 GLY 142 142 142 GLY GLY B . n B 1 143 ASN 143 143 143 ASN ASN B . n B 1 144 ALA 144 144 144 ALA ALA B . n B 1 145 GLY 145 145 145 GLY GLY B . n B 1 146 GLY 146 146 146 GLY GLY B . n B 1 147 ARG 147 147 147 ARG ARG B . n B 1 148 VAL 148 148 148 VAL VAL B . n B 1 149 ALA 149 149 149 ALA ALA B . n B 1 150 CYS 150 150 150 CYS CYS B . n B 1 151 GLY 151 151 151 GLY GLY B . n B 1 152 VAL 152 152 152 VAL VAL B . n B 1 153 ILE 153 153 153 ILE ILE B . n B 1 154 GLY 154 154 154 GLY GLY B . n B 1 155 ILE 155 155 155 ILE ILE B . n B 1 156 LEU 156 156 156 LEU LEU B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 1001 1001 NAG NAG A . D 2 NAG 2 1002 1002 NAG NAG A . E 3 MAN 3 1003 1003 MAN MAN A . F 4 CU 1 171 171 CU CU A . G 5 ZN 1 172 172 ZN ZN A . H 2 NAG 1 2001 2001 NAG NAG B . I 2 NAG 2 2002 2002 NAG NAG B . J 4 CU 1 171 171 CU CU B . K 5 ZN 1 172 172 ZN ZN B . L 6 HOH 1 1004 3 HOH HOH A . L 6 HOH 2 1005 4 HOH HOH A . L 6 HOH 3 1006 5 HOH HOH A . L 6 HOH 4 1007 6 HOH HOH A . L 6 HOH 5 1008 7 HOH HOH A . L 6 HOH 6 1009 8 HOH HOH A . L 6 HOH 7 1010 10 HOH HOH A . L 6 HOH 8 1011 11 HOH HOH A . L 6 HOH 9 1012 13 HOH HOH A . L 6 HOH 10 1013 14 HOH HOH A . L 6 HOH 11 1014 15 HOH HOH A . L 6 HOH 12 1015 18 HOH HOH A . L 6 HOH 13 1016 19 HOH HOH A . L 6 HOH 14 1017 20 HOH HOH A . L 6 HOH 15 1018 22 HOH HOH A . L 6 HOH 16 1019 23 HOH HOH A . L 6 HOH 17 1020 25 HOH HOH A . L 6 HOH 18 1021 26 HOH HOH A . L 6 HOH 19 1022 27 HOH HOH A . L 6 HOH 20 1023 31 HOH HOH A . L 6 HOH 21 1024 32 HOH HOH A . L 6 HOH 22 1025 35 HOH HOH A . L 6 HOH 23 1026 36 HOH HOH A . L 6 HOH 24 1027 37 HOH HOH A . L 6 HOH 25 1028 39 HOH HOH A . L 6 HOH 26 1029 40 HOH HOH A . L 6 HOH 27 1030 42 HOH HOH A . L 6 HOH 28 1031 46 HOH HOH A . L 6 HOH 29 1032 47 HOH HOH A . L 6 HOH 30 1033 48 HOH HOH A . L 6 HOH 31 1034 49 HOH HOH A . L 6 HOH 32 1035 51 HOH HOH A . L 6 HOH 33 1036 52 HOH HOH A . L 6 HOH 34 1037 54 HOH HOH A . L 6 HOH 35 1038 57 HOH HOH A . L 6 HOH 36 1039 58 HOH HOH A . L 6 HOH 37 1040 60 HOH HOH A . L 6 HOH 38 1041 61 HOH HOH A . L 6 HOH 39 1042 65 HOH HOH A . L 6 HOH 40 1043 69 HOH HOH A . L 6 HOH 41 1044 70 HOH HOH A . L 6 HOH 42 1045 72 HOH HOH A . L 6 HOH 43 1046 74 HOH HOH A . L 6 HOH 44 1047 75 HOH HOH A . L 6 HOH 45 1048 78 HOH HOH A . L 6 HOH 46 1049 83 HOH HOH A . L 6 HOH 47 1050 84 HOH HOH A . L 6 HOH 48 1051 85 HOH HOH A . L 6 HOH 49 1052 86 HOH HOH A . L 6 HOH 50 1053 95 HOH HOH A . L 6 HOH 51 1054 99 HOH HOH A . L 6 HOH 52 1055 104 HOH HOH A . L 6 HOH 53 1056 110 HOH HOH A . L 6 HOH 54 1057 112 HOH HOH A . L 6 HOH 55 1058 113 HOH HOH A . L 6 HOH 56 1059 117 HOH HOH A . L 6 HOH 57 1060 118 HOH HOH A . L 6 HOH 58 1061 122 HOH HOH A . L 6 HOH 59 1062 126 HOH HOH A . L 6 HOH 60 1063 129 HOH HOH A . L 6 HOH 61 1064 130 HOH HOH A . L 6 HOH 62 1065 132 HOH HOH A . L 6 HOH 63 1066 134 HOH HOH A . L 6 HOH 64 1067 135 HOH HOH A . L 6 HOH 65 1068 137 HOH HOH A . L 6 HOH 66 1069 138 HOH HOH A . L 6 HOH 67 1070 139 HOH HOH A . L 6 HOH 68 1071 140 HOH HOH A . L 6 HOH 69 1072 143 HOH HOH A . L 6 HOH 70 1073 146 HOH HOH A . L 6 HOH 71 1074 149 HOH HOH A . L 6 HOH 72 1075 153 HOH HOH A . L 6 HOH 73 1076 154 HOH HOH A . L 6 HOH 74 1077 157 HOH HOH A . L 6 HOH 75 1078 158 HOH HOH A . L 6 HOH 76 1079 159 HOH HOH A . L 6 HOH 77 1080 160 HOH HOH A . L 6 HOH 78 1081 162 HOH HOH A . L 6 HOH 79 1082 165 HOH HOH A . L 6 HOH 80 1083 167 HOH HOH A . L 6 HOH 81 1084 169 HOH HOH A . L 6 HOH 82 1085 170 HOH HOH A . L 6 HOH 83 1086 172 HOH HOH A . L 6 HOH 84 1087 175 HOH HOH A . L 6 HOH 85 1088 179 HOH HOH A . L 6 HOH 86 1089 180 HOH HOH A . L 6 HOH 87 1090 183 HOH HOH A . L 6 HOH 88 1091 189 HOH HOH A . L 6 HOH 89 1092 198 HOH HOH A . L 6 HOH 90 1093 199 HOH HOH A . M 6 HOH 1 2003 1 HOH HOH B . M 6 HOH 2 2004 2 HOH HOH B . M 6 HOH 3 2005 9 HOH HOH B . M 6 HOH 4 2006 12 HOH HOH B . M 6 HOH 5 2007 16 HOH HOH B . M 6 HOH 6 2008 17 HOH HOH B . M 6 HOH 7 2009 21 HOH HOH B . M 6 HOH 8 2010 24 HOH HOH B . M 6 HOH 9 2011 28 HOH HOH B . M 6 HOH 10 2012 29 HOH HOH B . M 6 HOH 11 2013 30 HOH HOH B . M 6 HOH 12 2014 33 HOH HOH B . M 6 HOH 13 2015 34 HOH HOH B . M 6 HOH 14 2016 38 HOH HOH B . M 6 HOH 15 2017 41 HOH HOH B . M 6 HOH 16 2018 43 HOH HOH B . M 6 HOH 17 2019 44 HOH HOH B . M 6 HOH 18 2020 45 HOH HOH B . M 6 HOH 19 2021 50 HOH HOH B . M 6 HOH 20 2022 53 HOH HOH B . M 6 HOH 21 2023 55 HOH HOH B . M 6 HOH 22 2024 56 HOH HOH B . M 6 HOH 23 2025 59 HOH HOH B . M 6 HOH 24 2026 62 HOH HOH B . M 6 HOH 25 2027 63 HOH HOH B . M 6 HOH 26 2028 64 HOH HOH B . M 6 HOH 27 2029 66 HOH HOH B . M 6 HOH 28 2030 67 HOH HOH B . M 6 HOH 29 2031 68 HOH HOH B . M 6 HOH 30 2032 71 HOH HOH B . M 6 HOH 31 2033 73 HOH HOH B . M 6 HOH 32 2034 76 HOH HOH B . M 6 HOH 33 2035 77 HOH HOH B . M 6 HOH 34 2036 79 HOH HOH B . M 6 HOH 35 2037 80 HOH HOH B . M 6 HOH 36 2038 81 HOH HOH B . M 6 HOH 37 2039 82 HOH HOH B . M 6 HOH 38 2040 87 HOH HOH B . M 6 HOH 39 2041 88 HOH HOH B . M 6 HOH 40 2042 89 HOH HOH B . M 6 HOH 41 2043 90 HOH HOH B . M 6 HOH 42 2044 91 HOH HOH B . M 6 HOH 43 2045 92 HOH HOH B . M 6 HOH 44 2046 93 HOH HOH B . M 6 HOH 45 2047 94 HOH HOH B . M 6 HOH 46 2048 96 HOH HOH B . M 6 HOH 47 2049 97 HOH HOH B . M 6 HOH 48 2050 98 HOH HOH B . M 6 HOH 49 2051 100 HOH HOH B . M 6 HOH 50 2052 101 HOH HOH B . M 6 HOH 51 2053 102 HOH HOH B . M 6 HOH 52 2054 103 HOH HOH B . M 6 HOH 53 2055 105 HOH HOH B . M 6 HOH 54 2056 106 HOH HOH B . M 6 HOH 55 2057 107 HOH HOH B . M 6 HOH 56 2058 108 HOH HOH B . M 6 HOH 57 2059 109 HOH HOH B . M 6 HOH 58 2060 111 HOH HOH B . M 6 HOH 59 2061 114 HOH HOH B . M 6 HOH 60 2062 115 HOH HOH B . M 6 HOH 61 2063 116 HOH HOH B . M 6 HOH 62 2064 119 HOH HOH B . M 6 HOH 63 2065 120 HOH HOH B . M 6 HOH 64 2066 121 HOH HOH B . M 6 HOH 65 2067 123 HOH HOH B . M 6 HOH 66 2068 124 HOH HOH B . M 6 HOH 67 2069 125 HOH HOH B . M 6 HOH 68 2070 127 HOH HOH B . M 6 HOH 69 2071 128 HOH HOH B . M 6 HOH 70 2072 131 HOH HOH B . M 6 HOH 71 2073 133 HOH HOH B . M 6 HOH 72 2074 136 HOH HOH B . M 6 HOH 73 2075 141 HOH HOH B . M 6 HOH 74 2076 142 HOH HOH B . M 6 HOH 75 2077 144 HOH HOH B . M 6 HOH 76 2078 145 HOH HOH B . M 6 HOH 77 2079 147 HOH HOH B . M 6 HOH 78 2080 148 HOH HOH B . M 6 HOH 79 2081 150 HOH HOH B . M 6 HOH 80 2082 151 HOH HOH B . M 6 HOH 81 2083 152 HOH HOH B . M 6 HOH 82 2084 155 HOH HOH B . M 6 HOH 83 2085 156 HOH HOH B . M 6 HOH 84 2086 161 HOH HOH B . M 6 HOH 85 2087 163 HOH HOH B . M 6 HOH 86 2088 164 HOH HOH B . M 6 HOH 87 2089 166 HOH HOH B . M 6 HOH 88 2090 168 HOH HOH B . M 6 HOH 89 2091 171 HOH HOH B . M 6 HOH 90 2092 173 HOH HOH B . M 6 HOH 91 2093 174 HOH HOH B . M 6 HOH 92 2094 176 HOH HOH B . M 6 HOH 93 2095 177 HOH HOH B . M 6 HOH 94 2096 178 HOH HOH B . M 6 HOH 95 2097 181 HOH HOH B . M 6 HOH 96 2098 182 HOH HOH B . M 6 HOH 97 2099 184 HOH HOH B . M 6 HOH 98 2100 185 HOH HOH B . M 6 HOH 99 2101 186 HOH HOH B . M 6 HOH 100 2102 187 HOH HOH B . M 6 HOH 101 2103 188 HOH HOH B . M 6 HOH 102 2104 190 HOH HOH B . M 6 HOH 103 2105 191 HOH HOH B . M 6 HOH 104 2106 192 HOH HOH B . M 6 HOH 105 2107 193 HOH HOH B . M 6 HOH 106 2108 194 HOH HOH B . M 6 HOH 107 2109 195 HOH HOH B . M 6 HOH 108 2110 196 HOH HOH B . M 6 HOH 109 2111 197 HOH HOH B . M 6 HOH 110 2112 200 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 22 A ASN 22 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 22 B ASN 22 ? 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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 ND1 ? A HIS 50 ? A HIS 50 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 52 ? A HIS 52 ? 1_555 121.8 ? 2 ND1 ? A HIS 50 ? A HIS 50 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 67 ? A HIS 67 ? 1_555 79.2 ? 3 NE2 ? A HIS 52 ? A HIS 52 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 67 ? A HIS 67 ? 1_555 110.9 ? 4 ND1 ? A HIS 50 ? A HIS 50 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 124 ? A HIS 124 ? 1_555 81.2 ? 5 NE2 ? A HIS 52 ? A HIS 52 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 124 ? A HIS 124 ? 1_555 100.2 ? 6 NE2 ? A HIS 67 ? A HIS 67 ? 1_555 CU ? F CU . ? A CU 171 ? 1_555 NE2 ? A HIS 124 ? A HIS 124 ? 1_555 148.6 ? 7 ND1 ? A HIS 67 ? A HIS 67 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 ND1 ? A HIS 75 ? A HIS 75 ? 1_555 105.8 ? 8 ND1 ? A HIS 67 ? A HIS 67 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 ND1 ? A HIS 84 ? A HIS 84 ? 1_555 119.2 ? 9 ND1 ? A HIS 75 ? A HIS 75 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 ND1 ? A HIS 84 ? A HIS 84 ? 1_555 122.2 ? 10 ND1 ? A HIS 67 ? A HIS 67 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 OD1 ? A ASP 87 ? A ASP 87 ? 1_555 110.2 ? 11 ND1 ? A HIS 75 ? A HIS 75 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 OD1 ? A ASP 87 ? A ASP 87 ? 1_555 92.4 ? 12 ND1 ? A HIS 84 ? A HIS 84 ? 1_555 ZN ? G ZN . ? A ZN 172 ? 1_555 OD1 ? A ASP 87 ? A ASP 87 ? 1_555 103.2 ? 13 ND1 ? B HIS 50 ? B HIS 50 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 52 ? B HIS 52 ? 1_555 120.7 ? 14 ND1 ? B HIS 50 ? B HIS 50 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 67 ? B HIS 67 ? 1_555 73.1 ? 15 NE2 ? B HIS 52 ? B HIS 52 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 67 ? B HIS 67 ? 1_555 113.1 ? 16 ND1 ? B HIS 50 ? B HIS 50 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 124 ? B HIS 124 ? 1_555 80.0 ? 17 NE2 ? B HIS 52 ? B HIS 52 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 124 ? B HIS 124 ? 1_555 98.7 ? 18 NE2 ? B HIS 67 ? B HIS 67 ? 1_555 CU ? J CU . ? B CU 171 ? 1_555 NE2 ? B HIS 124 ? B HIS 124 ? 1_555 145.7 ? 19 ND1 ? B HIS 67 ? B HIS 67 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 ND1 ? B HIS 75 ? B HIS 75 ? 1_555 104.4 ? 20 ND1 ? B HIS 67 ? B HIS 67 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 ND1 ? B HIS 84 ? B HIS 84 ? 1_555 119.0 ? 21 ND1 ? B HIS 75 ? B HIS 75 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 ND1 ? B HIS 84 ? B HIS 84 ? 1_555 118.4 ? 22 ND1 ? B HIS 67 ? B HIS 67 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 OD1 ? B ASP 87 ? B ASP 87 ? 1_555 111.3 ? 23 ND1 ? B HIS 75 ? B HIS 75 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 OD1 ? B ASP 87 ? B ASP 87 ? 1_555 93.3 ? 24 ND1 ? B HIS 84 ? B HIS 84 ? 1_555 ZN ? K ZN . ? B ZN 172 ? 1_555 OD1 ? B ASP 87 ? B ASP 87 ? 1_555 107.6 ? # 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 2007-12-11 2 'Structure model' 1 1 2011-07-13 # _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' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0005 ? 1 HKL-2000 'data collection' . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 MOLREP phasing . ? 5 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 CB _pdbx_validate_rmsd_angle.auth_asym_id_1 B _pdbx_validate_rmsd_angle.auth_comp_id_1 LEU _pdbx_validate_rmsd_angle.auth_seq_id_1 14 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CG _pdbx_validate_rmsd_angle.auth_asym_id_2 B _pdbx_validate_rmsd_angle.auth_comp_id_2 LEU _pdbx_validate_rmsd_angle.auth_seq_id_2 14 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CD1 _pdbx_validate_rmsd_angle.auth_asym_id_3 B _pdbx_validate_rmsd_angle.auth_comp_id_3 LEU _pdbx_validate_rmsd_angle.auth_seq_id_3 14 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 122.21 _pdbx_validate_rmsd_angle.angle_target_value 111.00 _pdbx_validate_rmsd_angle.angle_deviation 11.21 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.70 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 VAL B 28 ? ? -109.52 -142.78 2 1 GLN B 29 ? ? 2.75 -145.93 3 1 ASN B 69 ? ? -150.42 58.92 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id MAN _pdbx_validate_chiral.auth_seq_id 1003 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A HIS 1 ? A HIS 1 2 1 Y 1 B HIS 1 ? B HIS 1 3 1 Y 1 B HIS 2 ? B HIS 2 4 1 Y 1 B GLY 3 ? B GLY 3 5 1 Y 1 B PHE 4 ? B PHE 4 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'COPPER (II) ION' CU 5 'ZINC ION' ZN 6 water HOH #