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*** 1T3R ***elNémo ID: 2602061630303072027Job options:ID = 2602061630303072027 JOBID = 1T3R USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 1T3R data_1T3R # _entry.id 1T3R # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.376 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code _database_2.pdbx_database_accession _database_2.pdbx_DOI PDB 1T3R pdb_00001t3r 10.2210/pdb1t3r/pdb RCSB RCSB022274 ? ? WWPDB D_1000022274 ? ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1F7A 'USED AS STARTING MODEL FOR MOLECULAR REPLACEMENT' unspecified PDB 1T7I . unspecified PDB 1T7J . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1T3R _pdbx_database_status.recvd_initial_deposition_date 2004-04-27 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry N _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.status_code_nmr_data ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'King, N.M.' 1 'Prabu-Jeyabalan, M.' 2 'Nalivaika, E.A.' 3 'Wigernick, P.B.' 4 'de Bethune, M.P.' 5 'Schiffer, C.A.' 6 # _citation.id primary _citation.title 'Discovery and selection of TMC114, a next generation HIV-1 protease inhibitor' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 48 _citation.page_first 1813 _citation.page_last 1822 _citation.year 2005 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 15771427 _citation.pdbx_database_id_DOI 10.1021/jm049560p # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Surleraux, D.L.' 1 ? primary 'Tahri, A.' 2 ? primary 'Verschueren, W.G.' 3 ? primary 'Pille, G.M.' 4 ? primary 'de Kock, H.A.' 5 ? primary 'Jonckers, T.H.' 6 ? primary 'Peeters, A.' 7 ? primary 'De Meyer, S.' 8 ? primary 'Azijn, H.' 9 ? primary 'Pauwels, R.' 10 ? primary 'de Bethune, M.P.' 11 ? primary 'King, N.M.' 12 ? primary 'Prabu-Jeyabalan, M.' 13 ? primary 'Schiffer, C.A.' 14 ? primary 'Wigerinck, P.B.' 15 ? # _cell.entry_id 1T3R _cell.length_a 50.746 _cell.length_b 57.807 _cell.length_c 62.006 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1T3R _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'protease RETROPEPSIN' 10801.763 2 3.4.23.16 Q7K,L63P ? 'complexed with TMC114' 2 non-polymer syn 'PHOSPHATE ION' 94.971 5 ? ? ? ? 3 non-polymer syn '(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE' 547.664 1 ? ? ? ? 4 water nat water 18.015 259 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'HIV-1 PROTEASE' # _entity_name_sys.entity_id 1 _entity_name_sys.name E.C.3.4.23.16 # _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 ;PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF ; _entity_poly.pdbx_seq_one_letter_code_can ;PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF ; _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 PRO n 1 2 GLN n 1 3 ILE n 1 4 THR n 1 5 LEU n 1 6 TRP n 1 7 LYS n 1 8 ARG n 1 9 PRO n 1 10 LEU n 1 11 VAL n 1 12 THR n 1 13 ILE n 1 14 ARG n 1 15 ILE n 1 16 GLY n 1 17 GLY n 1 18 GLN n 1 19 LEU n 1 20 LYS n 1 21 GLU n 1 22 ALA n 1 23 LEU n 1 24 LEU n 1 25 ASP n 1 26 THR n 1 27 GLY n 1 28 ALA n 1 29 ASP n 1 30 ASP n 1 31 THR n 1 32 VAL n 1 33 LEU n 1 34 GLU n 1 35 GLU n 1 36 MET n 1 37 ASN n 1 38 LEU n 1 39 PRO n 1 40 GLY n 1 41 LYS n 1 42 TRP n 1 43 LYS n 1 44 PRO n 1 45 LYS n 1 46 MET n 1 47 ILE n 1 48 GLY n 1 49 GLY n 1 50 ILE n 1 51 GLY n 1 52 GLY n 1 53 PHE n 1 54 ILE n 1 55 LYS n 1 56 VAL n 1 57 ARG n 1 58 GLN n 1 59 TYR n 1 60 ASP n 1 61 GLN n 1 62 ILE n 1 63 PRO n 1 64 VAL n 1 65 GLU n 1 66 ILE n 1 67 CYS n 1 68 GLY n 1 69 HIS n 1 70 LYS n 1 71 ALA n 1 72 ILE n 1 73 GLY n 1 74 THR n 1 75 VAL n 1 76 LEU n 1 77 VAL n 1 78 GLY n 1 79 PRO n 1 80 THR n 1 81 PRO n 1 82 VAL n 1 83 ASN n 1 84 ILE n 1 85 ILE n 1 86 GLY n 1 87 ARG n 1 88 ASN n 1 89 LEU n 1 90 LEU n 1 91 THR n 1 92 GLN n 1 93 ILE n 1 94 GLY n 1 95 CYS n 1 96 THR n 1 97 LEU n 1 98 ASN n 1 99 PHE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus Lentivirus _entity_src_gen.pdbx_gene_src_gene gag-pol _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 'Human immunodeficiency virus 1' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11676 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 _entity_src_gen.host_org_genus Escherichia _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name p566 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.entity_id 1 _struct_ref.db_name UNP _struct_ref.db_code POL_HV1A2 _struct_ref.pdbx_db_accession P03369 _struct_ref.pdbx_align_begin 57 _struct_ref.pdbx_seq_one_letter_code ;PQITLWQRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF ; _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 1T3R A 1 ? 99 ? P03369 57 ? 155 ? 1 99 2 1 1T3R B 1 ? 99 ? P03369 57 ? 155 ? 1 99 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 1T3R LYS A 7 ? UNP P03369 GLN 63 'engineered mutation' 7 1 2 1T3R LYS B 7 ? UNP P03369 GLN 63 'engineered mutation' 7 2 # 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 017 non-polymer . '(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE' 'Darunavir; TMC114; UIC-94017' 'C27 H37 N3 O7 S' 547.664 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1T3R _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 41.56 _exptl_crystal.density_Matthews 2.10 _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 300 _exptl_crystal_grow.pH 6.2 _exptl_crystal_grow.pdbx_details ;1 MG/ML PROTEIN; 5:1 LIGAND:PROTEIN; 30% AMSOR; SODIUM CITRATE AND SODIUM PHOSPHATE, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 300K ; _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 190 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type ? _diffrn_detector.pdbx_collection_date ? _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 0.900 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 5.0.1' _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 5.0.1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.900 # _reflns.entry_id 1T3R _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.20 _reflns.d_resolution_low 50. _reflns.number_all 55056 _reflns.number_obs 55056 _reflns.percent_possible_obs 95.5 _reflns.pdbx_Rmerge_I_obs 0.038 _reflns.pdbx_Rsym_value 0.038 _reflns.pdbx_netI_over_sigmaI 25 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.5 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.20 _reflns_shell.d_res_low 1.24 _reflns_shell.percent_possible_all 76.2 _reflns_shell.Rmerge_I_obs 0.317 _reflns_shell.pdbx_Rsym_value 0.317 _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 4320 _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 1T3R _refine.ls_number_reflns_obs 52226 _refine.ls_number_reflns_all 55001 _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 42.26 _refine.ls_d_res_high 1.20 _refine.ls_percent_reflns_obs 95.52 _refine.ls_R_factor_obs 0.14 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1397 _refine.ls_R_factor_R_free 0.179 _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 2775 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.976 _refine.correlation_coeff_Fo_to_Fc_free 0.965 _refine.B_iso_mean 15.422 _refine.aniso_B[1][1] -0.39 _refine.aniso_B[2][2] -0.06 _refine.aniso_B[3][3] 0.45 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 1F7A _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 0.040 _refine.pdbx_overall_ESU_R_Free 0.042 _refine.overall_SU_ML 0.028 _refine.overall_SU_B 0.622 _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 1496 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 63 _refine_hist.number_atoms_solvent 259 _refine_hist.number_atoms_total 1818 _refine_hist.d_res_high 1.20 _refine_hist.d_res_low 42.26 # 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 0.039 0.022 ? 1664 'X-RAY DIFFRACTION' ? r_bond_other_d 0.007 0.020 ? 1591 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.593 2.018 ? 2284 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.722 3.000 ? 3708 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.960 5.000 ? 215 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_chiral_restr 0.149 0.200 ? 270 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.021 0.020 ? 1822 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.028 0.020 ? 301 'X-RAY DIFFRACTION' ? r_nbd_refined 0.244 0.200 ? 285 'X-RAY DIFFRACTION' ? r_nbd_other 0.274 0.200 ? 1925 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.095 0.200 ? 1088 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.254 0.200 ? 172 '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 0.310 0.200 ? 18 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.312 0.200 ? 101 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.338 0.200 ? 49 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 3.219 1.500 ? 1033 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 4.242 2.000 ? 1690 'X-RAY DIFFRACTION' ? r_scbond_it 5.811 3.000 ? 631 'X-RAY DIFFRACTION' ? r_scangle_it 8.132 4.500 ? 593 'X-RAY DIFFRACTION' ? r_rigid_bond_restr 2.590 1.000 ? 1664 'X-RAY DIFFRACTION' ? r_sphericity_free 16.645 3.000 ? 267 'X-RAY DIFFRACTION' ? r_sphericity_bonded 9.511 3.000 ? 1628 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.200 _refine_ls_shell.d_res_low 1.232 _refine_ls_shell.number_reflns_R_work 2913 _refine_ls_shell.R_factor_R_work 0.204 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.264 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 146 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # _struct.entry_id 1T3R _struct.title 'HIV protease wild-type in complex with TMC114 inhibitor' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1T3R _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HIV-1 PROTEASE; DRUG RESISTANCE; THERMODYNAMICS; SUBSTRATE ENVELOPE, HYDROLASE' # 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 2 ? F N N 3 ? G N N 2 ? H N N 2 ? I N N 4 ? J N N 4 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLY A 86 ? THR A 91 ? GLY A 86 THR A 91 1 ? 6 HELX_P HELX_P2 2 GLY B 86 ? THR B 91 ? GLY B 86 THR B 91 1 ? 6 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 8 ? C ? 8 ? # 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 B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? parallel B 4 5 ? anti-parallel B 5 6 ? parallel B 6 7 ? anti-parallel B 7 8 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? parallel C 4 5 ? anti-parallel C 5 6 ? parallel C 6 7 ? anti-parallel C 7 8 ? 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 GLN A 2 ? ILE A 3 ? GLN A 2 ILE A 3 A 2 THR B 96 ? ASN B 98 ? THR B 96 ASN B 98 A 3 THR A 96 ? ASN A 98 ? THR A 96 ASN A 98 A 4 GLN B 2 ? THR B 4 ? GLN B 2 THR B 4 B 1 LYS A 43 ? GLY A 49 ? LYS A 43 GLY A 49 B 2 GLY A 52 ? ILE A 66 ? GLY A 52 ILE A 66 B 3 HIS A 69 ? VAL A 77 ? HIS A 69 VAL A 77 B 4 VAL A 32 ? LEU A 33 ? VAL A 32 LEU A 33 B 5 ILE A 84 ? ILE A 85 ? ILE A 84 ILE A 85 B 6 GLN A 18 ? LEU A 24 ? GLN A 18 LEU A 24 B 7 LEU A 10 ? ILE A 15 ? LEU A 10 ILE A 15 B 8 GLY A 52 ? ILE A 66 ? GLY A 52 ILE A 66 C 1 LYS B 43 ? GLY B 49 ? LYS B 43 GLY B 49 C 2 GLY B 52 ? ILE B 66 ? GLY B 52 ILE B 66 C 3 HIS B 69 ? VAL B 77 ? HIS B 69 VAL B 77 C 4 VAL B 32 ? LEU B 33 ? VAL B 32 LEU B 33 C 5 ILE B 84 ? ILE B 85 ? ILE B 84 ILE B 85 C 6 GLN B 18 ? LEU B 24 ? GLN B 18 LEU B 24 C 7 LEU B 10 ? ILE B 15 ? LEU B 10 ILE B 15 C 8 GLY B 52 ? ILE B 66 ? GLY B 52 ILE B 66 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N ILE A 3 ? N ILE A 3 O LEU B 97 ? O LEU B 97 A 2 3 O THR B 96 ? O THR B 96 N ASN A 98 ? N ASN A 98 A 3 4 N LEU A 97 ? N LEU A 97 O ILE B 3 ? O ILE B 3 B 1 2 N LYS A 43 ? N LYS A 43 O GLN A 58 ? O GLN A 58 B 2 3 N ILE A 66 ? N ILE A 66 O HIS A 69 ? O HIS A 69 B 3 4 O LEU A 76 ? O LEU A 76 N LEU A 33 ? N LEU A 33 B 4 5 N VAL A 32 ? N VAL A 32 O ILE A 84 ? O ILE A 84 B 5 6 O ILE A 85 ? O ILE A 85 N LEU A 23 ? N LEU A 23 B 6 7 O GLN A 18 ? O GLN A 18 N ILE A 15 ? N ILE A 15 B 7 8 N ARG A 14 ? N ARG A 14 O GLU A 65 ? O GLU A 65 C 1 2 N LYS B 43 ? N LYS B 43 O GLN B 58 ? O GLN B 58 C 2 3 N TYR B 59 ? N TYR B 59 O VAL B 75 ? O VAL B 75 C 3 4 O LEU B 76 ? O LEU B 76 N LEU B 33 ? N LEU B 33 C 4 5 N VAL B 32 ? N VAL B 32 O ILE B 84 ? O ILE B 84 C 5 6 O ILE B 85 ? O ILE B 85 N LEU B 23 ? N LEU B 23 C 6 7 O LYS B 20 ? O LYS B 20 N ILE B 13 ? N ILE B 13 C 7 8 N ARG B 14 ? N ARG B 14 O GLU B 65 ? O GLU B 65 # 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 B PO4 501 ? 10 'BINDING SITE FOR RESIDUE PO4 B 501' AC2 Software A PO4 502 ? 3 'BINDING SITE FOR RESIDUE PO4 A 502' AC3 Software B PO4 503 ? 7 'BINDING SITE FOR RESIDUE PO4 B 503' AC4 Software A PO4 504 ? 5 'BINDING SITE FOR RESIDUE PO4 A 504' AC5 Software A PO4 505 ? 6 'BINDING SITE FOR RESIDUE PO4 A 505' AC6 Software A 017 1200 ? 19 'BINDING SITE FOR RESIDUE 017 A 1200' # 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 10 ARG A 14 ? ARG A 14 . ? 1_455 ? 2 AC1 10 GLY A 16 ? GLY A 16 . ? 1_455 ? 3 AC1 10 GLY A 17 ? GLY A 17 . ? 1_455 ? 4 AC1 10 HOH I . ? HOH A 1242 . ? 1_455 ? 5 AC1 10 ARG B 14 ? ARG B 14 . ? 1_555 ? 6 AC1 10 GLY B 16 ? GLY B 16 . ? 1_555 ? 7 AC1 10 GLY B 17 ? GLY B 17 . ? 1_555 ? 8 AC1 10 HOH J . ? HOH B 515 . ? 1_555 ? 9 AC1 10 HOH J . ? HOH B 525 . ? 1_555 ? 10 AC1 10 HOH J . ? HOH B 617 . ? 1_555 ? 11 AC2 3 LYS A 7 ? LYS A 7 . ? 1_555 ? 12 AC2 3 ARG A 8 ? ARG A 8 . ? 1_555 ? 13 AC2 3 HOH I . ? HOH A 1225 . ? 1_555 ? 14 AC3 7 GLY A 68 ? GLY A 68 . ? 4_456 ? 15 AC3 7 HIS A 69 ? HIS A 69 . ? 4_456 ? 16 AC3 7 LYS A 70 ? LYS A 70 . ? 4_456 ? 17 AC3 7 HOH I . ? HOH A 1210 . ? 4_456 ? 18 AC3 7 HOH I . ? HOH A 1249 . ? 4_456 ? 19 AC3 7 PRO B 1 ? PRO B 1 . ? 1_555 ? 20 AC3 7 LYS B 55 ? LYS B 55 . ? 2_565 ? 21 AC4 5 MET A 36 ? MET A 36 . ? 1_555 ? 22 AC4 5 ASN A 37 ? ASN A 37 . ? 1_555 ? 23 AC4 5 PRO B 39 ? PRO B 39 . ? 1_655 ? 24 AC4 5 GLY B 40 ? GLY B 40 . ? 1_655 ? 25 AC4 5 HOH J . ? HOH B 621 . ? 1_655 ? 26 AC5 6 LYS A 20 ? LYS A 20 . ? 1_555 ? 27 AC5 6 GLU A 21 ? GLU A 21 . ? 1_555 ? 28 AC5 6 ASN A 83 ? ASN A 83 . ? 1_555 ? 29 AC5 6 HOH I . ? HOH A 1219 . ? 1_555 ? 30 AC5 6 HOH I . ? HOH A 1226 . ? 1_555 ? 31 AC5 6 HOH J . ? HOH B 616 . ? 3_655 ? 32 AC6 19 ASP A 25 ? ASP A 25 . ? 1_555 ? 33 AC6 19 GLY A 27 ? GLY A 27 . ? 1_555 ? 34 AC6 19 ALA A 28 ? ALA A 28 . ? 1_555 ? 35 AC6 19 ASP A 29 ? ASP A 29 . ? 1_555 ? 36 AC6 19 ASP A 30 ? ASP A 30 . ? 1_555 ? 37 AC6 19 GLY A 48 ? GLY A 48 . ? 1_555 ? 38 AC6 19 GLY A 49 ? GLY A 49 . ? 1_555 ? 39 AC6 19 ILE A 50 ? ILE A 50 . ? 1_555 ? 40 AC6 19 HOH I . ? HOH A 1203 . ? 1_555 ? 41 AC6 19 HOH I . ? HOH A 1311 . ? 1_555 ? 42 AC6 19 ASP B 25 ? ASP B 25 . ? 1_555 ? 43 AC6 19 GLY B 27 ? GLY B 27 . ? 1_555 ? 44 AC6 19 ALA B 28 ? ALA B 28 . ? 1_555 ? 45 AC6 19 ASP B 30 ? ASP B 30 . ? 1_555 ? 46 AC6 19 VAL B 32 ? VAL B 32 . ? 1_555 ? 47 AC6 19 GLY B 48 ? GLY B 48 . ? 1_555 ? 48 AC6 19 GLY B 49 ? GLY B 49 . ? 1_555 ? 49 AC6 19 VAL B 82 ? VAL B 82 . ? 1_555 ? 50 AC6 19 ILE B 84 ? ILE B 84 . ? 1_555 ? # _atom_sites.entry_id 1T3R _atom_sites.fract_transf_matrix[1][1] 0.019706 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.017299 _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] 0.016127 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O P S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 1 ? 28.699 21.454 33.798 1.00 26.41 ? 1 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? 27.719 22.265 34.525 1.00 24.79 ? 1 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? 26.240 22.015 34.064 1.00 21.25 ? 1 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? 26.033 21.403 33.071 1.00 22.75 ? 1 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? 28.122 23.699 34.165 1.00 29.49 ? 1 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? 28.733 23.595 32.866 1.00 29.10 ? 1 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? 29.425 22.266 32.812 1.00 28.00 ? 1 PRO A CD 1 ATOM 8 N N . GLN A 1 2 ? 25.279 22.419 34.914 1.00 21.01 ? 2 GLN A N 1 ATOM 9 C CA . GLN A 1 2 ? 23.872 22.620 34.516 1.00 17.82 ? 2 GLN A CA 1 ATOM 10 C C . GLN A 1 2 ? 23.654 24.078 34.247 1.00 18.11 ? 2 GLN A C 1 ATOM 11 O O . GLN A 1 2 ? 23.996 24.956 35.114 1.00 20.40 ? 2 GLN A O 1 ATOM 12 C CB . GLN A 1 2 ? 22.926 22.138 35.611 1.00 19.10 ? 2 GLN A CB 1 ATOM 13 C CG . GLN A 1 2 ? 21.447 22.401 35.328 1.00 18.52 ? 2 GLN A CG 1 ATOM 14 C CD . GLN A 1 2 ? 20.558 21.549 36.121 1.00 21.32 ? 2 GLN A CD 1 ATOM 15 O OE1 . GLN A 1 2 ? 20.145 20.502 35.662 1.00 22.49 ? 2 GLN A OE1 1 ATOM 16 N NE2 . GLN A 1 2 ? 20.336 21.926 37.380 1.00 21.05 ? 2 GLN A NE2 1 ATOM 17 N N . ILE A 1 3 ? 23.132 24.397 33.044 1.00 16.55 ? 3 ILE A N 1 ATOM 18 C CA . ILE A 1 3 ? 22.953 25.808 32.633 1.00 16.67 ? 3 ILE A CA 1 ATOM 19 C C . ILE A 1 3 ? 21.482 26.059 32.330 1.00 15.72 ? 3 ILE A C 1 ATOM 20 O O . ILE A 1 3 ? 20.868 25.364 31.520 1.00 15.91 ? 3 ILE A O 1 ATOM 21 C CB . ILE A 1 3 ? 23.812 26.118 31.387 1.00 18.38 ? 3 ILE A CB 1 ATOM 22 C CG1 . ILE A 1 3 ? 25.342 25.949 31.689 1.00 18.48 ? 3 ILE A CG1 1 ATOM 23 C CG2 . ILE A 1 3 ? 23.547 27.527 30.875 1.00 19.52 ? 3 ILE A CG2 1 ATOM 24 C CD1 . ILE A 1 3 ? 26.162 26.103 30.549 1.00 21.55 ? 3 ILE A CD1 1 ATOM 25 N N . THR A 1 4 ? 20.887 26.933 33.128 1.00 15.87 ? 4 THR A N 1 ATOM 26 C CA . THR A 1 4 ? 19.503 27.351 32.833 1.00 15.75 ? 4 THR A CA 1 ATOM 27 C C . THR A 1 4 ? 19.446 28.398 31.741 1.00 15.51 ? 4 THR A C 1 ATOM 28 O O . THR A 1 4 ? 20.430 28.870 31.310 1.00 16.38 ? 4 THR A O 1 ATOM 29 C CB . THR A 1 4 ? 18.816 27.912 34.134 1.00 16.86 ? 4 THR A CB 1 ATOM 30 O OG1 . THR A 1 4 ? 19.563 29.057 34.578 1.00 19.32 ? 4 THR A OG1 1 ATOM 31 C CG2 . THR A 1 4 ? 18.833 26.841 35.249 1.00 18.60 ? 4 THR A CG2 1 ATOM 32 N N . LEU A 1 5 ? 18.246 28.766 31.361 1.00 15.45 ? 5 LEU A N 1 ATOM 33 C CA . LEU A 1 5 ? 18.036 29.497 30.073 1.00 13.94 ? 5 LEU A CA 1 ATOM 34 C C . LEU A 1 5 ? 17.299 30.803 30.212 1.00 16.04 ? 5 LEU A C 1 ATOM 35 O O . LEU A 1 5 ? 16.815 31.385 29.209 1.00 15.73 ? 5 LEU A O 1 ATOM 36 C CB . LEU A 1 5 ? 17.384 28.590 29.088 1.00 13.41 ? 5 LEU A CB 1 ATOM 37 C CG . LEU A 1 5 ? 18.226 27.325 28.692 1.00 13.46 ? 5 LEU A CG 1 ATOM 38 C CD1 . LEU A 1 5 ? 17.455 26.412 27.870 1.00 14.28 ? 5 LEU A CD1 1 ATOM 39 C CD2 . LEU A 1 5 ? 19.482 27.737 27.925 1.00 14.09 ? 5 LEU A CD2 1 ATOM 40 N N . TRP A 1 6 ? 17.284 31.375 31.434 1.00 16.86 ? 6 TRP A N 1 ATOM 41 C CA . TRP A 1 6 ? 16.707 32.666 31.611 1.00 17.05 ? 6 TRP A CA 1 ATOM 42 C C . TRP A 1 6 ? 17.659 33.763 31.019 1.00 18.33 ? 6 TRP A C 1 ATOM 43 O O . TRP A 1 6 ? 17.204 34.845 30.676 1.00 20.73 ? 6 TRP A O 1 ATOM 44 C CB . TRP A 1 6 ? 16.356 32.919 33.157 1.00 20.30 ? 6 TRP A CB 1 ATOM 45 C CG . TRP A 1 6 ? 15.026 32.189 33.646 1.00 18.85 ? 6 TRP A CG 1 ATOM 46 C CD1 . TRP A 1 6 ? 13.705 32.558 33.336 1.00 19.94 ? 6 TRP A CD1 1 ATOM 47 C CD2 . TRP A 1 6 ? 14.941 30.990 34.423 1.00 20.40 ? 6 TRP A CD2 1 ATOM 48 N NE1 . TRP A 1 6 ? 12.820 31.577 33.761 1.00 21.82 ? 6 TRP A NE1 1 ATOM 49 C CE2 . TRP A 1 6 ? 13.542 30.616 34.493 1.00 20.77 ? 6 TRP A CE2 1 ATOM 50 C CE3 . TRP A 1 6 ? 15.875 30.123 34.920 1.00 20.29 ? 6 TRP A CE3 1 ATOM 51 C CZ2 . TRP A 1 6 ? 13.127 29.428 35.041 1.00 21.27 ? 6 TRP A CZ2 1 ATOM 52 C CZ3 . TRP A 1 6 ? 15.452 28.956 35.526 1.00 23.27 ? 6 TRP A CZ3 1 ATOM 53 C CH2 . TRP A 1 6 ? 14.085 28.634 35.609 1.00 21.71 ? 6 TRP A CH2 1 ATOM 54 N N . LYS A 1 7 ? 18.943 33.460 30.863 1.00 18.01 ? 7 LYS A N 1 ATOM 55 C CA . LYS A 1 7 ? 19.868 34.291 30.152 1.00 18.47 ? 7 LYS A CA 1 ATOM 56 C C . LYS A 1 7 ? 20.407 33.514 28.970 1.00 16.89 ? 7 LYS A C 1 ATOM 57 O O . LYS A 1 7 ? 20.390 32.305 28.964 1.00 16.24 ? 7 LYS A O 1 ATOM 58 C CB . LYS A 1 7 ? 21.039 34.694 31.043 1.00 22.07 ? 7 LYS A CB 1 ATOM 59 N N . ARG A 1 8 ? 21.063 34.206 28.059 1.00 15.16 ? 8 ARG A N 1 ATOM 60 C CA . ARG A 1 8 ? 21.751 33.512 26.958 1.00 14.08 ? 8 ARG A CA 1 ATOM 61 C C . ARG A 1 8 ? 22.831 32.627 27.523 1.00 14.01 ? 8 ARG A C 1 ATOM 62 O O . ARG A 1 8 ? 23.644 33.098 28.358 1.00 15.33 ? 8 ARG A O 1 ATOM 63 C CB . ARG A 1 8 ? 22.393 34.533 25.995 1.00 15.05 ? 8 ARG A CB 1 ATOM 64 C CG . ARG A 1 8 ? 21.388 35.299 25.145 1.00 16.10 ? 8 ARG A CG 1 ATOM 65 C CD . ARG A 1 8 ? 21.981 36.283 24.289 1.00 18.66 ? 8 ARG A CD 1 ATOM 66 N NE . ARG A 1 8 ? 20.974 36.967 23.478 1.00 26.58 ? 8 ARG A NE 1 ATOM 67 C CZ . ARG A 1 8 ? 21.155 38.127 22.865 1.00 28.39 ? 8 ARG A CZ 1 ATOM 68 N NH1 . ARG A 1 8 ? 22.298 38.861 23.072 1.00 32.61 ? 8 ARG A NH1 1 ATOM 69 N NH2 . ARG A 1 8 ? 20.234 38.582 22.075 1.00 27.89 ? 8 ARG A NH2 1 ATOM 70 N N . PRO A 1 9 ? 22.993 31.412 26.985 1.00 13.20 ? 9 PRO A N 1 ATOM 71 C CA . PRO A 1 9 ? 24.058 30.507 27.473 1.00 12.81 ? 9 PRO A CA 1 ATOM 72 C C . PRO A 1 9 ? 25.393 30.784 26.831 1.00 13.39 ? 9 PRO A C 1 ATOM 73 O O . PRO A 1 9 ? 25.886 30.054 25.979 1.00 13.14 ? 9 PRO A O 1 ATOM 74 C CB . PRO A 1 9 ? 23.517 29.138 27.156 1.00 12.80 ? 9 PRO A CB 1 ATOM 75 C CG . PRO A 1 9 ? 22.661 29.333 25.968 1.00 11.86 ? 9 PRO A CG 1 ATOM 76 C CD . PRO A 1 9 ? 21.995 30.679 26.191 1.00 12.06 ? 9 PRO A CD 1 ATOM 77 N N . LEU A 1 10 ? 25.975 31.915 27.261 1.00 15.80 ? 10 LEU A N 1 ATOM 78 C CA . LEU A 1 10 ? 27.264 32.344 26.801 1.00 14.99 ? 10 LEU A CA 1 ATOM 79 C C . LEU A 1 10 ? 28.381 31.764 27.624 1.00 17.09 ? 10 LEU A C 1 ATOM 80 O O . LEU A 1 10 ? 28.286 31.737 28.859 1.00 22.73 ? 10 LEU A O 1 ATOM 81 C CB . LEU A 1 10 ? 27.364 33.892 26.837 1.00 18.92 ? 10 LEU A CB 1 ATOM 82 C CG . LEU A 1 10 ? 26.444 34.574 25.905 1.00 20.44 ? 10 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 10 ? 26.254 36.027 26.276 1.00 23.88 ? 10 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 10 ? 26.983 34.490 24.453 1.00 21.23 ? 10 LEU A CD2 1 ATOM 85 N N . VAL A 1 11 ? 29.375 31.255 27.011 1.00 14.84 ? 11 VAL A N 1 ATOM 86 C CA . VAL A 1 11 ? 30.473 30.664 27.715 1.00 16.59 ? 11 VAL A CA 1 ATOM 87 C C . VAL A 1 11 ? 31.810 31.113 27.103 1.00 14.71 ? 11 VAL A C 1 ATOM 88 O O . VAL A 1 11 ? 31.877 31.590 25.971 1.00 15.58 ? 11 VAL A O 1 ATOM 89 C CB . VAL A 1 11 ? 30.397 29.207 27.749 1.00 19.02 ? 11 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 11 ? 29.094 28.704 28.409 1.00 23.88 ? 11 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 11 ? 30.583 28.631 26.486 1.00 19.95 ? 11 VAL A CG2 1 ATOM 92 N N . THR A 1 12 ? 32.875 30.963 27.866 1.00 16.70 ? 12 THR A N 1 ATOM 93 C CA . THR A 1 12 ? 34.172 31.223 27.350 1.00 16.58 ? 12 THR A CA 1 ATOM 94 C C . THR A 1 12 ? 34.751 30.001 26.690 1.00 16.89 ? 12 THR A C 1 ATOM 95 O O . THR A 1 12 ? 34.684 28.888 27.273 1.00 17.57 ? 12 THR A O 1 ATOM 96 C CB . THR A 1 12 ? 35.130 31.713 28.518 1.00 19.89 ? 12 THR A CB 1 ATOM 97 O OG1 . THR A 1 12 ? 34.586 32.859 29.079 1.00 20.17 ? 12 THR A OG1 1 ATOM 98 C CG2 . THR A 1 12 ? 36.444 32.085 28.007 1.00 20.97 ? 12 THR A CG2 1 ATOM 99 N N . ILE A 1 13 ? 35.321 30.172 25.494 1.00 15.74 ? 13 ILE A N 1 ATOM 100 C CA . ILE A 1 13 ? 36.036 29.162 24.798 1.00 16.14 ? 13 ILE A CA 1 ATOM 101 C C . ILE A 1 13 ? 37.486 29.576 24.558 1.00 18.01 ? 13 ILE A C 1 ATOM 102 O O . ILE A 1 13 ? 37.809 30.785 24.600 1.00 18.55 ? 13 ILE A O 1 ATOM 103 C CB . ILE A 1 13 ? 35.326 28.822 23.452 1.00 15.76 ? 13 ILE A CB 1 ATOM 104 C CG1 . ILE A 1 13 ? 35.489 29.988 22.407 1.00 16.94 ? 13 ILE A CG1 1 ATOM 105 C CG2 . ILE A 1 13 ? 33.854 28.522 23.730 1.00 15.87 ? 13 ILE A CG2 1 ATOM 106 C CD1 . ILE A 1 13 ? 35.054 29.629 20.995 1.00 15.73 ? 13 ILE A CD1 1 ATOM 107 N N . ARG A 1 14 ? 38.351 28.546 24.283 1.00 19.24 ? 14 ARG A N 1 ATOM 108 C CA . ARG A 1 14 ? 39.740 28.714 23.796 1.00 19.48 ? 14 ARG A CA 1 ATOM 109 C C . ARG A 1 14 ? 39.918 28.028 22.436 1.00 20.28 ? 14 ARG A C 1 ATOM 110 O O . ARG A 1 14 ? 39.637 26.872 22.330 1.00 21.28 ? 14 ARG A O 1 ATOM 111 C CB . ARG A 1 14 ? 40.748 27.997 24.860 1.00 25.11 ? 14 ARG A CB 1 ATOM 112 C CG . ARG A 1 14 ? 41.974 28.524 25.047 1.00 26.05 ? 14 ARG A CG 1 ATOM 113 C CD . ARG A 1 14 ? 42.876 27.685 26.109 1.00 28.26 ? 14 ARG A CD 1 ATOM 114 N NE . ARG A 1 14 ? 44.159 27.228 25.525 1.00 28.29 ? 14 ARG A NE 1 ATOM 115 C CZ . ARG A 1 14 ? 45.195 26.746 26.259 1.00 25.16 ? 14 ARG A CZ 1 ATOM 116 N NH1 . ARG A 1 14 ? 45.134 26.730 27.627 1.00 31.96 ? 14 ARG A NH1 1 ATOM 117 N NH2 . ARG A 1 14 ? 46.281 26.301 25.639 1.00 25.69 ? 14 ARG A NH2 1 ATOM 118 N N . ILE A 1 15 ? 40.496 28.785 21.374 1.00 17.55 ? 15 ILE A N 1 ATOM 119 C CA . ILE A 1 15 ? 40.664 28.280 20.005 1.00 18.93 ? 15 ILE A CA 1 ATOM 120 C C . ILE A 1 15 ? 41.849 29.017 19.370 1.00 22.09 ? 15 ILE A C 1 ATOM 121 O O . ILE A 1 15 ? 41.974 30.256 19.540 1.00 22.91 ? 15 ILE A O 1 ATOM 122 C CB . ILE A 1 15 ? 39.370 28.512 19.202 1.00 18.63 ? 15 ILE A CB 1 ATOM 123 C CG1 . ILE A 1 15 ? 39.539 27.963 17.824 1.00 20.53 ? 15 ILE A CG1 1 ATOM 124 C CG2 . ILE A 1 15 ? 38.906 30.049 19.262 1.00 22.07 ? 15 ILE A CG2 1 ATOM 125 C CD1 . ILE A 1 15 ? 38.335 28.008 16.992 1.00 21.04 ? 15 ILE A CD1 1 ATOM 126 N N . GLY A 1 16 ? 42.710 28.265 18.585 1.00 20.04 ? 16 GLY A N 1 ATOM 127 C CA . GLY A 1 16 ? 43.870 28.844 17.943 1.00 21.12 ? 16 GLY A CA 1 ATOM 128 C C . GLY A 1 16 ? 44.732 29.561 18.902 1.00 22.23 ? 16 GLY A C 1 ATOM 129 O O . GLY A 1 16 ? 45.498 30.522 18.511 1.00 23.46 ? 16 GLY A O 1 ATOM 130 N N . GLY A 1 17 ? 44.609 29.232 20.109 1.00 20.72 ? 17 GLY A N 1 ATOM 131 C CA . GLY A 1 17 ? 45.383 29.828 21.189 1.00 25.17 ? 17 GLY A CA 1 ATOM 132 C C . GLY A 1 17 ? 44.727 30.930 21.930 1.00 23.89 ? 17 GLY A C 1 ATOM 133 O O . GLY A 1 17 ? 45.299 31.459 22.831 1.00 26.29 ? 17 GLY A O 1 ATOM 134 N N . GLN A 1 18 ? 43.639 31.479 21.343 1.00 21.91 ? 18 GLN A N 1 ATOM 135 C CA . GLN A 1 18 ? 42.946 32.713 21.880 1.00 22.92 ? 18 GLN A CA 1 ATOM 136 C C . GLN A 1 18 ? 41.507 32.418 22.671 1.00 23.47 ? 18 GLN A C 1 ATOM 137 O O . GLN A 1 18 ? 40.861 31.451 22.428 1.00 26.51 ? 18 GLN A O 1 ATOM 138 C CB . GLN A 1 18 ? 42.656 33.686 20.670 1.00 23.78 ? 18 GLN A CB 1 ATOM 139 C CG . GLN A 1 18 ? 43.872 34.050 19.911 1.00 31.20 ? 18 GLN A CG 1 ATOM 140 C CD . GLN A 1 18 ? 44.718 34.960 20.660 1.00 30.20 ? 18 GLN A CD 1 ATOM 141 O OE1 . GLN A 1 18 ? 44.237 36.091 21.096 1.00 27.16 ? 18 GLN A OE1 1 ATOM 142 N NE2 . GLN A 1 18 ? 45.999 34.565 20.884 1.00 29.54 ? 18 GLN A NE2 1 ATOM 143 N N A LEU A 1 19 ? 41.185 33.264 23.682 0.50 21.32 ? 19 LEU A N 1 ATOM 144 N N B LEU A 1 19 ? 41.153 33.288 23.569 0.50 19.10 ? 19 LEU A N 1 ATOM 145 C CA A LEU A 1 19 ? 39.800 33.235 24.388 0.50 24.41 ? 19 LEU A CA 1 ATOM 146 C CA B LEU A 1 19 ? 39.837 33.221 24.286 0.50 21.98 ? 19 LEU A CA 1 ATOM 147 C C A LEU A 1 19 ? 38.770 34.025 23.636 0.50 21.26 ? 19 LEU A C 1 ATOM 148 C C B LEU A 1 19 ? 38.774 34.075 23.682 0.50 18.95 ? 19 LEU A C 1 ATOM 149 O O A LEU A 1 19 ? 39.058 35.123 23.132 0.50 26.30 ? 19 LEU A O 1 ATOM 150 O O B LEU A 1 19 ? 38.981 35.286 23.492 0.50 23.09 ? 19 LEU A O 1 ATOM 151 C CB A LEU A 1 19 ? 39.862 33.793 25.850 0.50 23.07 ? 19 LEU A CB 1 ATOM 152 C CB B LEU A 1 19 ? 39.984 33.634 25.654 0.50 20.78 ? 19 LEU A CB 1 ATOM 153 C CG A LEU A 1 19 ? 40.627 32.946 26.937 0.50 25.76 ? 19 LEU A CG 1 ATOM 154 C CG B LEU A 1 19 ? 41.050 32.880 26.462 0.50 18.52 ? 19 LEU A CG 1 ATOM 155 C CD1 A LEU A 1 19 ? 42.060 32.745 26.506 0.50 26.02 ? 19 LEU A CD1 1 ATOM 156 C CD1 B LEU A 1 19 ? 41.201 33.481 27.694 0.50 18.51 ? 19 LEU A CD1 1 ATOM 157 C CD2 A LEU A 1 19 ? 40.547 33.647 28.307 0.50 24.53 ? 19 LEU A CD2 1 ATOM 158 C CD2 B LEU A 1 19 ? 40.668 31.509 26.641 0.50 15.71 ? 19 LEU A CD2 1 ATOM 159 N N . LYS A 1 20 ? 37.513 33.520 23.671 1.00 20.23 ? 20 LYS A N 1 ATOM 160 C CA . LYS A 1 20 ? 36.328 34.205 23.109 1.00 17.88 ? 20 LYS A CA 1 ATOM 161 C C . LYS A 1 20 ? 35.070 33.857 23.886 1.00 17.07 ? 20 LYS A C 1 ATOM 162 O O . LYS A 1 20 ? 35.007 32.812 24.512 1.00 19.34 ? 20 LYS A O 1 ATOM 163 C CB . LYS A 1 20 ? 36.137 33.795 21.686 1.00 20.70 ? 20 LYS A CB 1 ATOM 164 C CG . LYS A 1 20 ? 37.224 34.141 20.858 1.00 22.91 ? 20 LYS A CG 1 ATOM 165 C CD . LYS A 1 20 ? 37.058 33.621 19.526 1.00 20.63 ? 20 LYS A CD 1 ATOM 166 C CE . LYS A 1 20 ? 38.024 34.263 18.584 1.00 27.61 ? 20 LYS A CE 1 ATOM 167 N NZ . LYS A 1 20 ? 37.605 35.541 18.134 1.00 25.91 ? 20 LYS A NZ 1 ATOM 168 N N A GLU A 1 21 ? 34.054 34.645 23.757 0.50 16.90 ? 21 GLU A N 1 ATOM 169 N N B GLU A 1 21 ? 34.002 34.643 23.669 0.50 17.10 ? 21 GLU A N 1 ATOM 170 C CA A GLU A 1 21 ? 32.820 34.252 24.177 0.50 15.90 ? 21 GLU A CA 1 ATOM 171 C CA B GLU A 1 21 ? 32.684 34.357 24.231 0.50 16.10 ? 21 GLU A CA 1 ATOM 172 C C A GLU A 1 21 ? 32.056 33.618 23.043 0.50 13.94 ? 21 GLU A C 1 ATOM 173 C C B GLU A 1 21 ? 31.778 33.810 23.163 0.50 12.52 ? 21 GLU A C 1 ATOM 174 O O A GLU A 1 21 ? 32.174 34.070 21.815 0.50 11.55 ? 21 GLU A O 1 ATOM 175 O O B GLU A 1 21 ? 31.626 34.403 22.168 0.50 10.50 ? 21 GLU A O 1 ATOM 176 C CB A GLU A 1 21 ? 32.025 35.452 24.767 0.50 17.73 ? 21 GLU A CB 1 ATOM 177 C CB B GLU A 1 21 ? 32.057 35.626 24.776 0.50 18.52 ? 21 GLU A CB 1 ATOM 178 C CG A GLU A 1 21 ? 32.740 36.131 26.034 0.50 19.06 ? 21 GLU A CG 1 ATOM 179 C CG B GLU A 1 21 ? 30.733 35.411 25.410 0.50 19.19 ? 21 GLU A CG 1 ATOM 180 C CD A GLU A 1 21 ? 32.849 35.201 27.181 0.50 19.91 ? 21 GLU A CD 1 ATOM 181 C CD B GLU A 1 21 ? 30.248 36.632 26.247 0.50 24.59 ? 21 GLU A CD 1 ATOM 182 O OE1 A GLU A 1 21 ? 33.949 34.909 27.552 0.50 18.25 ? 21 GLU A OE1 1 ATOM 183 O OE1 B GLU A 1 21 ? 29.889 37.722 25.612 0.50 31.64 ? 21 GLU A OE1 1 ATOM 184 O OE2 A GLU A 1 21 ? 31.773 34.835 27.782 0.50 22.31 ? 21 GLU A OE2 1 ATOM 185 O OE2 B GLU A 1 21 ? 30.107 36.482 27.566 0.50 27.19 ? 21 GLU A OE2 1 ATOM 186 N N . ALA A 1 22 ? 31.225 32.651 23.384 1.00 12.59 ? 22 ALA A N 1 ATOM 187 C CA . ALA A 1 22 ? 30.334 31.986 22.363 1.00 11.08 ? 22 ALA A CA 1 ATOM 188 C C . ALA A 1 22 ? 29.057 31.509 22.993 1.00 11.70 ? 22 ALA A C 1 ATOM 189 O O . ALA A 1 22 ? 29.012 31.196 24.174 1.00 13.28 ? 22 ALA A O 1 ATOM 190 C CB . ALA A 1 22 ? 31.084 30.851 21.700 1.00 11.90 ? 22 ALA A CB 1 ATOM 191 N N . LEU A 1 23 ? 28.027 31.359 22.169 1.00 10.64 ? 23 LEU A N 1 ATOM 192 C CA . LEU A 1 23 ? 26.747 30.934 22.555 1.00 10.58 ? 23 LEU A CA 1 ATOM 193 C C . LEU A 1 23 ? 26.536 29.464 22.322 1.00 9.27 ? 23 LEU A C 1 ATOM 194 O O . LEU A 1 23 ? 26.706 28.956 21.217 1.00 10.54 ? 23 LEU A O 1 ATOM 195 C CB . LEU A 1 23 ? 25.728 31.732 21.731 1.00 11.16 ? 23 LEU A CB 1 ATOM 196 C CG . LEU A 1 23 ? 24.261 31.532 21.950 1.00 11.73 ? 23 LEU A CG 1 ATOM 197 C CD1 . LEU A 1 23 ? 23.847 32.113 23.292 1.00 14.01 ? 23 LEU A CD1 1 ATOM 198 C CD2 . LEU A 1 23 ? 23.448 32.173 20.820 1.00 12.25 ? 23 LEU A CD2 1 ATOM 199 N N . LEU A 1 24 ? 26.167 28.747 23.370 1.00 9.83 ? 24 LEU A N 1 ATOM 200 C CA . LEU A 1 24 ? 25.804 27.311 23.210 1.00 9.65 ? 24 LEU A CA 1 ATOM 201 C C . LEU A 1 24 ? 24.456 27.233 22.520 1.00 9.90 ? 24 LEU A C 1 ATOM 202 O O . LEU A 1 24 ? 23.464 27.683 23.030 1.00 10.55 ? 24 LEU A O 1 ATOM 203 C CB . LEU A 1 24 ? 25.761 26.606 24.556 1.00 10.38 ? 24 LEU A CB 1 ATOM 204 C CG . LEU A 1 24 ? 27.005 26.692 25.428 1.00 11.77 ? 24 LEU A CG 1 ATOM 205 C CD1 . LEU A 1 24 ? 26.786 25.947 26.736 1.00 15.11 ? 24 LEU A CD1 1 ATOM 206 C CD2 . LEU A 1 24 ? 28.214 26.124 24.701 1.00 14.24 ? 24 LEU A CD2 1 ATOM 207 N N . ASP A 1 25 ? 24.465 26.647 21.304 1.00 9.16 ? 25 ASP A N 1 ATOM 208 C CA . ASP A 1 25 ? 23.340 26.812 20.393 1.00 8.39 ? 25 ASP A CA 1 ATOM 209 C C . ASP A 1 25 ? 22.846 25.472 19.860 1.00 8.33 ? 25 ASP A C 1 ATOM 210 O O . ASP A 1 25 ? 23.339 24.932 18.863 1.00 8.65 ? 25 ASP A O 1 ATOM 211 C CB . ASP A 1 25 ? 23.793 27.733 19.249 1.00 9.39 ? 25 ASP A CB 1 ATOM 212 C CG . ASP A 1 25 ? 22.718 28.138 18.307 1.00 10.38 ? 25 ASP A CG 1 ATOM 213 O OD1 . ASP A 1 25 ? 21.606 27.554 18.423 1.00 10.49 ? 25 ASP A OD1 1 ATOM 214 O OD2 . ASP A 1 25 ? 22.950 28.989 17.433 1.00 11.81 ? 25 ASP A OD2 1 ATOM 215 N N . THR A 1 26 ? 21.859 24.905 20.562 1.00 8.41 ? 26 THR A N 1 ATOM 216 C CA . THR A 1 26 ? 21.386 23.566 20.190 1.00 8.04 ? 26 THR A CA 1 ATOM 217 C C . THR A 1 26 ? 20.648 23.556 18.880 1.00 8.17 ? 26 THR A C 1 ATOM 218 O O . THR A 1 26 ? 20.489 22.492 18.288 1.00 8.68 ? 26 THR A O 1 ATOM 219 C CB . THR A 1 26 ? 20.495 22.967 21.267 1.00 8.00 ? 26 THR A CB 1 ATOM 220 O OG1 . THR A 1 26 ? 19.409 23.844 21.563 1.00 8.69 ? 26 THR A OG1 1 ATOM 221 C CG2 . THR A 1 26 ? 21.295 22.709 22.560 1.00 9.09 ? 26 THR A CG2 1 ATOM 222 N N . GLY A 1 27 ? 20.199 24.723 18.372 1.00 7.84 ? 27 GLY A N 1 ATOM 223 C CA . GLY A 1 27 ? 19.612 24.838 17.068 1.00 8.65 ? 27 GLY A CA 1 ATOM 224 C C . GLY A 1 27 ? 20.580 24.986 15.932 1.00 8.31 ? 27 GLY A C 1 ATOM 225 O O . GLY A 1 27 ? 20.132 25.123 14.773 1.00 9.35 ? 27 GLY A O 1 ATOM 226 N N . ALA A 1 28 ? 21.856 24.973 16.210 1.00 8.21 ? 28 ALA A N 1 ATOM 227 C CA . ALA A 1 28 ? 22.892 25.033 15.169 1.00 8.59 ? 28 ALA A CA 1 ATOM 228 C C . ALA A 1 28 ? 23.503 23.665 14.958 1.00 7.71 ? 28 ALA A C 1 ATOM 229 O O . ALA A 1 28 ? 23.988 23.034 15.918 1.00 8.48 ? 28 ALA A O 1 ATOM 230 C CB . ALA A 1 28 ? 23.972 25.991 15.571 1.00 8.31 ? 28 ALA A CB 1 ATOM 231 N N . ASP A 1 29 ? 23.492 23.160 13.718 1.00 8.50 ? 29 ASP A N 1 ATOM 232 C CA . ASP A 1 29 ? 24.191 21.928 13.416 1.00 9.24 ? 29 ASP A CA 1 ATOM 233 C C . ASP A 1 29 ? 25.682 22.139 13.572 1.00 9.82 ? 29 ASP A C 1 ATOM 234 O O . ASP A 1 29 ? 26.423 21.208 13.962 1.00 10.77 ? 29 ASP A O 1 ATOM 235 C CB . ASP A 1 29 ? 23.934 21.480 11.973 1.00 10.16 ? 29 ASP A CB 1 ATOM 236 C CG . ASP A 1 29 ? 22.488 21.270 11.630 1.00 11.43 ? 29 ASP A CG 1 ATOM 237 O OD1 . ASP A 1 29 ? 21.602 21.095 12.505 1.00 11.34 ? 29 ASP A OD1 1 ATOM 238 O OD2 . ASP A 1 29 ? 22.200 21.166 10.403 1.00 13.84 ? 29 ASP A OD2 1 ATOM 239 N N . ASP A 1 30 ? 26.121 23.313 13.168 1.00 9.92 ? 30 ASP A N 1 ATOM 240 C CA . ASP A 1 30 ? 27.545 23.670 12.985 1.00 10.48 ? 30 ASP A CA 1 ATOM 241 C C . ASP A 1 30 ? 27.963 24.783 13.918 1.00 10.14 ? 30 ASP A C 1 ATOM 242 O O . ASP A 1 30 ? 27.174 25.630 14.287 1.00 11.06 ? 30 ASP A O 1 ATOM 243 C CB . ASP A 1 30 ? 27.790 24.095 11.544 1.00 12.80 ? 30 ASP A CB 1 ATOM 244 C CG . ASP A 1 30 ? 27.304 23.090 10.567 1.00 16.56 ? 30 ASP A CG 1 ATOM 245 O OD1 . ASP A 1 30 ? 27.611 21.936 10.719 1.00 20.66 ? 30 ASP A OD1 1 ATOM 246 O OD2 . ASP A 1 30 ? 26.521 23.392 9.651 1.00 29.18 ? 30 ASP A OD2 1 ATOM 247 N N . THR A 1 31 ? 29.260 24.806 14.222 1.00 10.81 ? 31 THR A N 1 ATOM 248 C CA . THR A 1 31 ? 29.929 25.874 14.976 1.00 9.68 ? 31 THR A CA 1 ATOM 249 C C . THR A 1 31 ? 30.409 26.961 14.006 1.00 10.39 ? 31 THR A C 1 ATOM 250 O O . THR A 1 31 ? 31.077 26.652 13.017 1.00 11.54 ? 31 THR A O 1 ATOM 251 C CB . THR A 1 31 ? 31.070 25.255 15.742 1.00 9.79 ? 31 THR A CB 1 ATOM 252 O OG1 . THR A 1 31 ? 30.521 24.363 16.716 1.00 10.39 ? 31 THR A OG1 1 ATOM 253 C CG2 . THR A 1 31 ? 31.896 26.279 16.453 1.00 11.59 ? 31 THR A CG2 1 ATOM 254 N N . VAL A 1 32 ? 29.989 28.192 14.273 1.00 10.02 ? 32 VAL A N 1 ATOM 255 C CA . VAL A 1 32 ? 30.273 29.340 13.384 1.00 9.86 ? 32 VAL A CA 1 ATOM 256 C C . VAL A 1 32 ? 30.794 30.447 14.228 1.00 10.43 ? 32 VAL A C 1 ATOM 257 O O . VAL A 1 32 ? 30.123 30.918 15.153 1.00 10.70 ? 32 VAL A O 1 ATOM 258 C CB . VAL A 1 32 ? 29.035 29.788 12.591 1.00 9.96 ? 32 VAL A CB 1 ATOM 259 C CG1 . VAL A 1 32 ? 29.472 30.685 11.457 1.00 11.45 ? 32 VAL A CG1 1 ATOM 260 C CG2 . VAL A 1 32 ? 28.280 28.616 12.052 1.00 11.48 ? 32 VAL A CG2 1 ATOM 261 N N . LEU A 1 33 ? 32.020 30.890 13.917 1.00 10.63 ? 33 LEU A N 1 ATOM 262 C CA . LEU A 1 33 ? 32.664 31.982 14.629 1.00 10.43 ? 33 LEU A CA 1 ATOM 263 C C . LEU A 1 33 ? 32.821 33.187 13.708 1.00 10.99 ? 33 LEU A C 1 ATOM 264 O O . LEU A 1 33 ? 32.975 33.045 12.513 1.00 11.39 ? 33 LEU A O 1 ATOM 265 C CB . LEU A 1 33 ? 34.034 31.555 15.158 1.00 11.75 ? 33 LEU A CB 1 ATOM 266 C CG . LEU A 1 33 ? 34.038 30.342 16.075 1.00 13.47 ? 33 LEU A CG 1 ATOM 267 C CD1 . LEU A 1 33 ? 35.442 30.092 16.586 1.00 15.13 ? 33 LEU A CD1 1 ATOM 268 C CD2 . LEU A 1 33 ? 33.078 30.477 17.215 1.00 14.00 ? 33 LEU A CD2 1 ATOM 269 N N . GLU A 1 34 ? 32.767 34.347 14.319 1.00 11.96 ? 34 GLU A N 1 ATOM 270 C CA . GLU A 1 34 ? 33.059 35.623 13.638 1.00 13.57 ? 34 GLU A CA 1 ATOM 271 C C . GLU A 1 34 ? 34.468 35.634 13.124 1.00 14.26 ? 34 GLU A C 1 ATOM 272 O O . GLU A 1 34 ? 35.351 34.823 13.564 1.00 15.97 ? 34 GLU A O 1 ATOM 273 C CB . GLU A 1 34 ? 32.847 36.786 14.626 1.00 16.99 ? 34 GLU A CB 1 ATOM 274 C CG . GLU A 1 34 ? 31.411 36.889 15.194 1.00 19.71 ? 34 GLU A CG 1 ATOM 275 C CD . GLU A 1 34 ? 31.191 38.118 15.959 1.00 26.10 ? 34 GLU A CD 1 ATOM 276 O OE1 . GLU A 1 34 ? 30.475 39.176 15.395 1.00 26.28 ? 34 GLU A OE1 1 ATOM 277 O OE2 . GLU A 1 34 ? 31.700 38.176 17.047 1.00 29.34 ? 34 GLU A OE2 1 ATOM 278 N N . GLU A 1 35 ? 34.698 36.514 12.175 1.00 16.36 ? 35 GLU A N 1 ATOM 279 C CA . GLU A 1 35 ? 35.990 36.650 11.528 1.00 17.77 ? 35 GLU A CA 1 ATOM 280 C C . GLU A 1 35 ? 37.135 36.609 12.473 1.00 16.71 ? 35 GLU A C 1 ATOM 281 O O . GLU A 1 35 ? 37.159 37.301 13.446 1.00 19.45 ? 35 GLU A O 1 ATOM 282 C CB . GLU A 1 35 ? 36.047 37.946 10.703 1.00 19.52 ? 35 GLU A CB 1 ATOM 283 C CG . GLU A 1 35 ? 37.436 38.255 10.102 1.00 26.36 ? 35 GLU A CG 1 ATOM 284 C CD . GLU A 1 35 ? 37.994 37.106 9.206 1.00 34.20 ? 35 GLU A CD 1 ATOM 285 O OE1 . GLU A 1 35 ? 37.193 36.358 8.636 1.00 37.42 ? 35 GLU A OE1 1 ATOM 286 O OE2 . GLU A 1 35 ? 39.302 36.994 9.056 1.00 43.68 ? 35 GLU A OE2 1 ATOM 287 N N . MET A 1 36 ? 38.071 35.717 12.179 1.00 18.40 ? 36 MET A N 1 ATOM 288 C CA . MET A 1 36 ? 39.325 35.509 12.967 1.00 19.59 ? 36 MET A CA 1 ATOM 289 C C . MET A 1 36 ? 40.285 34.749 12.085 1.00 21.04 ? 36 MET A C 1 ATOM 290 O O . MET A 1 36 ? 39.923 34.228 11.096 1.00 20.86 ? 36 MET A O 1 ATOM 291 C CB . MET A 1 36 ? 39.040 34.723 14.206 1.00 18.89 ? 36 MET A CB 1 ATOM 292 C CG . MET A 1 36 ? 38.683 33.296 13.972 1.00 17.19 ? 36 MET A CG 1 ATOM 293 S SD . MET A 1 36 ? 38.555 32.305 15.425 1.00 20.88 ? 36 MET A SD 1 ATOM 294 C CE . MET A 1 36 ? 40.313 32.377 16.087 1.00 19.79 ? 36 MET A CE 1 ATOM 295 N N . ASN A 1 37 ? 41.582 34.807 12.419 1.00 21.74 ? 37 ASN A N 1 ATOM 296 C CA . ASN A 1 37 ? 42.570 33.987 11.732 1.00 21.71 ? 37 ASN A CA 1 ATOM 297 C C . ASN A 1 37 ? 42.726 32.644 12.445 1.00 20.22 ? 37 ASN A C 1 ATOM 298 O O . ASN A 1 37 ? 42.709 32.595 13.651 1.00 20.97 ? 37 ASN A O 1 ATOM 299 C CB . ASN A 1 37 ? 43.900 34.715 11.669 1.00 25.14 ? 37 ASN A CB 1 ATOM 300 C CG . ASN A 1 37 ? 43.805 36.057 10.895 1.00 27.66 ? 37 ASN A CG 1 ATOM 301 O OD1 . ASN A 1 37 ? 44.126 37.178 11.454 1.00 35.11 ? 37 ASN A OD1 1 ATOM 302 N ND2 . ASN A 1 37 ? 43.404 35.980 9.690 1.00 30.91 ? 37 ASN A ND2 1 ATOM 303 N N . LEU A 1 38 ? 42.770 31.587 11.682 1.00 19.08 ? 38 LEU A N 1 ATOM 304 C CA . LEU A 1 38 ? 43.145 30.242 12.191 1.00 20.76 ? 38 LEU A CA 1 ATOM 305 C C . LEU A 1 38 ? 44.216 29.639 11.276 1.00 20.91 ? 38 LEU A C 1 ATOM 306 O O . LEU A 1 38 ? 44.149 29.752 10.093 1.00 23.11 ? 38 LEU A O 1 ATOM 307 C CB . LEU A 1 38 ? 41.915 29.296 12.215 1.00 21.98 ? 38 LEU A CB 1 ATOM 308 C CG . LEU A 1 38 ? 40.893 29.505 13.284 1.00 21.42 ? 38 LEU A CG 1 ATOM 309 C CD1 . LEU A 1 38 ? 39.650 28.635 13.067 1.00 20.59 ? 38 LEU A CD1 1 ATOM 310 C CD2 . LEU A 1 38 ? 41.500 29.256 14.649 1.00 21.38 ? 38 LEU A CD2 1 ATOM 311 N N . PRO A 1 39 ? 45.081 28.825 11.834 1.00 25.42 ? 39 PRO A N 1 ATOM 312 C CA . PRO A 1 39 ? 46.090 28.159 11.052 1.00 26.48 ? 39 PRO A CA 1 ATOM 313 C C . PRO A 1 39 ? 45.562 27.031 10.171 1.00 25.01 ? 39 PRO A C 1 ATOM 314 O O . PRO A 1 39 ? 44.673 26.312 10.562 1.00 27.21 ? 39 PRO A O 1 ATOM 315 C CB . PRO A 1 39 ? 47.070 27.607 12.120 1.00 27.82 ? 39 PRO A CB 1 ATOM 316 C CG . PRO A 1 39 ? 46.598 28.174 13.455 1.00 29.92 ? 39 PRO A CG 1 ATOM 317 C CD . PRO A 1 39 ? 45.194 28.542 13.275 1.00 25.52 ? 39 PRO A CD 1 ATOM 318 N N . GLY A 1 40 ? 46.273 26.771 9.080 1.00 26.67 ? 40 GLY A N 1 ATOM 319 C CA . GLY A 1 40 ? 46.069 25.598 8.306 1.00 27.90 ? 40 GLY A CA 1 ATOM 320 C C . GLY A 1 40 ? 45.135 25.804 7.129 1.00 25.39 ? 40 GLY A C 1 ATOM 321 O O . GLY A 1 40 ? 44.690 26.967 6.791 1.00 26.01 ? 40 GLY A O 1 ATOM 322 N N . LYS A 1 41 ? 44.866 24.735 6.474 1.00 25.54 ? 41 LYS A N 1 ATOM 323 C CA . LYS A 1 41 ? 44.077 24.731 5.314 1.00 24.79 ? 41 LYS A CA 1 ATOM 324 C C . LYS A 1 41 ? 42.588 25.015 5.658 1.00 22.94 ? 41 LYS A C 1 ATOM 325 O O . LYS A 1 41 ? 42.093 24.657 6.796 1.00 24.65 ? 41 LYS A O 1 ATOM 326 C CB . LYS A 1 41 ? 44.194 23.364 4.616 1.00 27.25 ? 41 LYS A CB 1 ATOM 327 N N . TRP A 1 42 ? 41.906 25.708 4.761 1.00 20.48 ? 42 TRP A N 1 ATOM 328 C CA . TRP A 1 42 ? 40.471 25.831 4.864 1.00 17.40 ? 42 TRP A CA 1 ATOM 329 C C . TRP A 1 42 ? 39.828 25.668 3.497 1.00 18.14 ? 42 TRP A C 1 ATOM 330 O O . TRP A 1 42 ? 40.511 25.744 2.470 1.00 20.51 ? 42 TRP A O 1 ATOM 331 C CB . TRP A 1 42 ? 40.076 27.165 5.499 1.00 17.80 ? 42 TRP A CB 1 ATOM 332 C CG . TRP A 1 42 ? 40.619 28.413 4.760 1.00 18.54 ? 42 TRP A CG 1 ATOM 333 C CD1 . TRP A 1 42 ? 41.801 28.989 4.950 1.00 22.42 ? 42 TRP A CD1 1 ATOM 334 C CD2 . TRP A 1 42 ? 39.995 29.117 3.696 1.00 17.55 ? 42 TRP A CD2 1 ATOM 335 N NE1 . TRP A 1 42 ? 41.933 30.073 4.151 1.00 22.53 ? 42 TRP A NE1 1 ATOM 336 C CE2 . TRP A 1 42 ? 40.848 30.138 3.322 1.00 19.64 ? 42 TRP A CE2 1 ATOM 337 C CE3 . TRP A 1 42 ? 38.789 29.015 3.073 1.00 17.18 ? 42 TRP A CE3 1 ATOM 338 C CZ2 . TRP A 1 42 ? 40.491 31.095 2.357 1.00 22.13 ? 42 TRP A CZ2 1 ATOM 339 C CZ3 . TRP A 1 42 ? 38.447 29.930 2.088 1.00 20.03 ? 42 TRP A CZ3 1 ATOM 340 C CH2 . TRP A 1 42 ? 39.281 30.946 1.756 1.00 21.14 ? 42 TRP A CH2 1 ATOM 341 N N . LYS A 1 43 ? 38.530 25.368 3.481 1.00 16.57 ? 43 LYS A N 1 ATOM 342 C CA . LYS A 1 43 ? 37.784 25.272 2.263 1.00 18.91 ? 43 LYS A CA 1 ATOM 343 C C . LYS A 1 43 ? 36.677 26.281 2.281 1.00 16.98 ? 43 LYS A C 1 ATOM 344 O O . LYS A 1 43 ? 36.012 26.458 3.269 1.00 16.53 ? 43 LYS A O 1 ATOM 345 C CB . LYS A 1 43 ? 37.225 23.898 2.129 1.00 24.19 ? 43 LYS A CB 1 ATOM 346 N N . PRO A 1 44 ? 36.377 26.858 1.126 1.00 16.62 ? 44 PRO A N 1 ATOM 347 C CA . PRO A 1 44 ? 35.176 27.666 1.004 1.00 16.12 ? 44 PRO A CA 1 ATOM 348 C C . PRO A 1 44 ? 33.929 26.831 1.098 1.00 16.08 ? 44 PRO A C 1 ATOM 349 O O . PRO A 1 44 ? 33.823 25.799 0.471 1.00 18.72 ? 44 PRO A O 1 ATOM 350 C CB . PRO A 1 44 ? 35.302 28.262 -0.399 1.00 17.89 ? 44 PRO A CB 1 ATOM 351 C CG . PRO A 1 44 ? 36.699 28.037 -0.837 1.00 20.86 ? 44 PRO A CG 1 ATOM 352 C CD . PRO A 1 44 ? 37.216 26.876 -0.079 1.00 18.30 ? 44 PRO A CD 1 ATOM 353 N N . LYS A 1 45 ? 32.960 27.292 1.884 1.00 14.76 ? 45 LYS A N 1 ATOM 354 C CA . LYS A 1 45 ? 31.672 26.614 2.032 1.00 14.58 ? 45 LYS A CA 1 ATOM 355 C C . LYS A 1 45 ? 30.576 27.697 2.122 1.00 13.40 ? 45 LYS A C 1 ATOM 356 O O . LYS A 1 45 ? 30.877 28.890 2.350 1.00 14.14 ? 45 LYS A O 1 ATOM 357 C CB . LYS A 1 45 ? 31.665 25.726 3.266 1.00 18.03 ? 45 LYS A CB 1 ATOM 358 C CG . LYS A 1 45 ? 32.634 24.460 3.145 1.00 24.24 ? 45 LYS A CG 1 ATOM 359 C CD . LYS A 1 45 ? 32.063 23.377 2.296 1.00 27.54 ? 45 LYS A CD 1 ATOM 360 C CE . LYS A 1 45 ? 32.953 22.065 2.333 1.00 28.24 ? 45 LYS A CE 1 ATOM 361 N NZ . LYS A 1 45 ? 32.731 21.251 1.084 1.00 39.83 ? 45 LYS A NZ 1 ATOM 362 N N . MET A 1 46 ? 29.358 27.260 1.998 1.00 13.14 ? 46 MET A N 1 ATOM 363 C CA . MET A 1 46 ? 28.178 28.123 2.243 1.00 13.59 ? 46 MET A CA 1 ATOM 364 C C . MET A 1 46 ? 27.286 27.454 3.219 1.00 13.33 ? 46 MET A C 1 ATOM 365 O O . MET A 1 46 ? 27.165 26.243 3.223 1.00 15.98 ? 46 MET A O 1 ATOM 366 C CB . MET A 1 46 ? 27.428 28.373 0.937 1.00 13.92 ? 46 MET A CB 1 ATOM 367 C CG . MET A 1 46 ? 28.192 29.272 0.003 1.00 15.83 ? 46 MET A CG 1 ATOM 368 S SD . MET A 1 46 ? 27.339 29.508 -1.542 1.00 19.09 ? 46 MET A SD 1 ATOM 369 C CE . MET A 1 46 ? 25.876 30.430 -0.989 1.00 20.19 ? 46 MET A CE 1 ATOM 370 N N A ILE A 1 47 ? 26.614 28.259 4.045 0.50 11.47 ? 47 ILE A N 1 ATOM 371 N N B ILE A 1 47 ? 26.684 28.244 4.130 0.50 11.95 ? 47 ILE A N 1 ATOM 372 C CA A ILE A 1 47 ? 25.721 27.757 5.045 0.50 12.92 ? 47 ILE A CA 1 ATOM 373 C CA B ILE A 1 47 ? 25.632 27.730 5.008 0.50 12.13 ? 47 ILE A CA 1 ATOM 374 C C A ILE A 1 47 ? 24.520 28.717 5.159 0.50 12.79 ? 47 ILE A C 1 ATOM 375 C C B ILE A 1 47 ? 24.480 28.684 5.063 0.50 12.05 ? 47 ILE A C 1 ATOM 376 O O A ILE A 1 47 ? 24.661 29.907 4.948 0.50 12.70 ? 47 ILE A O 1 ATOM 377 O O B ILE A 1 47 ? 24.657 29.887 4.910 0.50 12.53 ? 47 ILE A O 1 ATOM 378 C CB A ILE A 1 47 ? 26.460 27.598 6.438 0.50 13.91 ? 47 ILE A CB 1 ATOM 379 C CB B ILE A 1 47 ? 26.165 27.442 6.474 0.50 11.48 ? 47 ILE A CB 1 ATOM 380 C CG1 A ILE A 1 47 ? 25.631 26.829 7.391 0.50 16.03 ? 47 ILE A CG1 1 ATOM 381 C CG1 B ILE A 1 47 ? 26.745 28.728 7.117 0.50 11.13 ? 47 ILE A CG1 1 ATOM 382 C CG2 A ILE A 1 47 ? 26.807 28.962 7.058 0.50 16.42 ? 47 ILE A CG2 1 ATOM 383 C CG2 B ILE A 1 47 ? 27.195 26.398 6.444 0.50 12.59 ? 47 ILE A CG2 1 ATOM 384 C CD1 A ILE A 1 47 ? 26.404 26.234 8.490 0.50 18.22 ? 47 ILE A CD1 1 ATOM 385 C CD1 B ILE A 1 47 ? 26.915 28.692 8.641 0.50 11.62 ? 47 ILE A CD1 1 ATOM 386 N N . GLY A 1 48 ? 23.357 28.156 5.461 1.00 12.00 ? 48 GLY A N 1 ATOM 387 C CA . GLY A 1 48 ? 22.140 28.930 5.627 1.00 12.49 ? 48 GLY A CA 1 ATOM 388 C C . GLY A 1 48 ? 21.682 28.998 7.054 1.00 10.90 ? 48 GLY A C 1 ATOM 389 O O . GLY A 1 48 ? 21.710 28.020 7.754 1.00 13.65 ? 48 GLY A O 1 ATOM 390 N N . GLY A 1 49 ? 21.127 30.125 7.401 1.00 12.17 ? 49 GLY A N 1 ATOM 391 C CA . GLY A 1 49 ? 20.531 30.386 8.694 1.00 11.10 ? 49 GLY A CA 1 ATOM 392 C C . GLY A 1 49 ? 19.125 30.987 8.484 1.00 11.19 ? 49 GLY A C 1 ATOM 393 O O . GLY A 1 49 ? 18.503 30.806 7.401 1.00 12.43 ? 49 GLY A O 1 ATOM 394 N N . ILE A 1 50 ? 18.607 31.602 9.501 1.00 10.19 ? 50 ILE A N 1 ATOM 395 C CA . ILE A 1 50 ? 17.245 32.068 9.435 1.00 10.92 ? 50 ILE A CA 1 ATOM 396 C C . ILE A 1 50 ? 17.054 33.106 8.329 1.00 11.50 ? 50 ILE A C 1 ATOM 397 O O . ILE A 1 50 ? 15.949 33.258 7.803 1.00 12.89 ? 50 ILE A O 1 ATOM 398 C CB . ILE A 1 50 ? 16.762 32.604 10.811 1.00 12.62 ? 50 ILE A CB 1 ATOM 399 C CG1 . ILE A 1 50 ? 15.244 32.402 10.939 1.00 13.79 ? 50 ILE A CG1 1 ATOM 400 C CG2 . ILE A 1 50 ? 17.244 34.025 11.037 1.00 14.24 ? 50 ILE A CG2 1 ATOM 401 C CD1 . ILE A 1 50 ? 14.670 32.795 12.264 1.00 16.34 ? 50 ILE A CD1 1 ATOM 402 N N . GLY A 1 51 ? 18.093 33.877 8.024 1.00 12.09 ? 51 GLY A N 1 ATOM 403 C CA . GLY A 1 51 ? 17.999 35.016 7.146 1.00 12.75 ? 51 GLY A CA 1 ATOM 404 C C . GLY A 1 51 ? 18.533 34.794 5.785 1.00 13.69 ? 51 GLY A C 1 ATOM 405 O O . GLY A 1 51 ? 18.530 35.731 4.983 1.00 16.49 ? 51 GLY A O 1 ATOM 406 N N . GLY A 1 52 ? 18.975 33.583 5.460 1.00 12.96 ? 52 GLY A N 1 ATOM 407 C CA . GLY A 1 52 ? 19.580 33.270 4.143 1.00 15.11 ? 52 GLY A CA 1 ATOM 408 C C . GLY A 1 52 ? 20.961 32.649 4.313 1.00 11.45 ? 52 GLY A C 1 ATOM 409 O O . GLY A 1 52 ? 21.323 32.162 5.367 1.00 13.35 ? 52 GLY A O 1 ATOM 410 N N . PHE A 1 53 ? 21.719 32.715 3.235 1.00 11.37 ? 53 PHE A N 1 ATOM 411 C CA . PHE A 1 53 ? 22.973 32.032 3.102 1.00 10.60 ? 53 PHE A CA 1 ATOM 412 C C . PHE A 1 53 ? 24.141 32.987 3.193 1.00 10.82 ? 53 PHE A C 1 ATOM 413 O O . PHE A 1 53 ? 24.081 34.093 2.717 1.00 12.42 ? 53 PHE A O 1 ATOM 414 C CB . PHE A 1 53 ? 23.017 31.226 1.805 1.00 13.29 ? 53 PHE A CB 1 ATOM 415 C CG . PHE A 1 53 ? 22.251 29.989 1.874 1.00 14.51 ? 53 PHE A CG 1 ATOM 416 C CD1 . PHE A 1 53 ? 20.855 29.994 1.857 1.00 15.65 ? 53 PHE A CD1 1 ATOM 417 C CD2 . PHE A 1 53 ? 22.898 28.798 2.053 1.00 15.67 ? 53 PHE A CD2 1 ATOM 418 C CE1 . PHE A 1 53 ? 20.145 28.860 2.083 1.00 18.18 ? 53 PHE A CE1 1 ATOM 419 C CE2 . PHE A 1 53 ? 22.157 27.587 2.147 1.00 18.77 ? 53 PHE A CE2 1 ATOM 420 C CZ . PHE A 1 53 ? 20.801 27.659 2.229 1.00 18.35 ? 53 PHE A CZ 1 ATOM 421 N N . ILE A 1 54 ? 25.249 32.475 3.756 1.00 10.69 ? 54 ILE A N 1 ATOM 422 C CA . ILE A 1 54 ? 26.504 33.162 3.817 1.00 10.77 ? 54 ILE A CA 1 ATOM 423 C C . ILE A 1 54 ? 27.643 32.272 3.359 1.00 10.93 ? 54 ILE A C 1 ATOM 424 O O . ILE A 1 54 ? 27.529 31.043 3.330 1.00 11.77 ? 54 ILE A O 1 ATOM 425 C CB . ILE A 1 54 ? 26.799 33.684 5.294 1.00 10.94 ? 54 ILE A CB 1 ATOM 426 C CG1 . ILE A 1 54 ? 26.981 32.499 6.274 1.00 10.79 ? 54 ILE A CG1 1 ATOM 427 C CG2 . ILE A 1 54 ? 25.727 34.626 5.767 1.00 12.19 ? 54 ILE A CG2 1 ATOM 428 C CD1 . ILE A 1 54 ? 27.571 32.927 7.581 1.00 11.45 ? 54 ILE A CD1 1 ATOM 429 N N . LYS A 1 55 ? 28.744 32.912 2.999 1.00 10.89 ? 55 LYS A N 1 ATOM 430 C CA . LYS A 1 55 ? 29.984 32.258 2.741 1.00 11.78 ? 55 LYS A CA 1 ATOM 431 C C . LYS A 1 55 ? 30.814 32.183 4.001 1.00 11.28 ? 55 LYS A C 1 ATOM 432 O O . LYS A 1 55 ? 30.868 33.115 4.762 1.00 13.06 ? 55 LYS A O 1 ATOM 433 C CB . LYS A 1 55 ? 30.781 32.994 1.660 1.00 12.60 ? 55 LYS A CB 1 ATOM 434 C CG . LYS A 1 55 ? 30.100 32.998 0.307 1.00 15.31 ? 55 LYS A CG 1 ATOM 435 C CD . LYS A 1 55 ? 30.691 34.017 -0.642 1.00 18.61 ? 55 LYS A CD 1 ATOM 436 C CE . LYS A 1 55 ? 32.068 33.732 -0.973 1.00 21.97 ? 55 LYS A CE 1 ATOM 437 N NZ . LYS A 1 55 ? 32.607 34.726 -1.947 1.00 28.59 ? 55 LYS A NZ 1 ATOM 438 N N . VAL A 1 56 ? 31.389 31.022 4.250 1.00 11.48 ? 56 VAL A N 1 ATOM 439 C CA . VAL A 1 56 ? 32.262 30.783 5.368 1.00 11.33 ? 56 VAL A CA 1 ATOM 440 C C . VAL A 1 56 ? 33.556 30.087 4.887 1.00 13.60 ? 56 VAL A C 1 ATOM 441 O O . VAL A 1 56 ? 33.617 29.495 3.807 1.00 14.57 ? 56 VAL A O 1 ATOM 442 C CB . VAL A 1 56 ? 31.565 29.890 6.474 1.00 12.18 ? 56 VAL A CB 1 ATOM 443 C CG1 . VAL A 1 56 ? 30.416 30.614 7.050 1.00 13.28 ? 56 VAL A CG1 1 ATOM 444 C CG2 . VAL A 1 56 ? 31.165 28.535 5.935 1.00 13.59 ? 56 VAL A CG2 1 ATOM 445 N N . ARG A 1 57 ? 34.535 30.131 5.768 1.00 12.36 ? 57 ARG A N 1 ATOM 446 C CA . ARG A 1 57 ? 35.747 29.317 5.648 1.00 12.54 ? 57 ARG A CA 1 ATOM 447 C C . ARG A 1 57 ? 35.633 28.150 6.602 1.00 13.16 ? 57 ARG A C 1 ATOM 448 O O . ARG A 1 57 ? 35.399 28.336 7.783 1.00 13.25 ? 57 ARG A O 1 ATOM 449 C CB . ARG A 1 57 ? 37.002 30.155 6.009 1.00 14.02 ? 57 ARG A CB 1 ATOM 450 C CG . ARG A 1 57 ? 37.164 31.460 5.161 1.00 16.21 ? 57 ARG A CG 1 ATOM 451 C CD . ARG A 1 57 ? 38.492 32.086 5.242 1.00 18.93 ? 57 ARG A CD 1 ATOM 452 N NE . ARG A 1 57 ? 38.955 32.250 6.528 1.00 21.79 ? 57 ARG A NE 1 ATOM 453 C CZ . ARG A 1 57 ? 38.786 33.339 7.295 1.00 23.99 ? 57 ARG A CZ 1 ATOM 454 N NH1 . ARG A 1 57 ? 37.908 34.290 6.961 1.00 30.84 ? 57 ARG A NH1 1 ATOM 455 N NH2 . ARG A 1 57 ? 39.412 33.414 8.455 1.00 25.76 ? 57 ARG A NH2 1 ATOM 456 N N . GLN A 1 58 ? 35.774 26.931 6.062 1.00 13.70 ? 58 GLN A N 1 ATOM 457 C CA . GLN A 1 58 ? 35.655 25.697 6.859 1.00 14.73 ? 58 GLN A CA 1 ATOM 458 C C . GLN A 1 58 ? 36.992 25.206 7.228 1.00 16.12 ? 58 GLN A C 1 ATOM 459 O O . GLN A 1 58 ? 37.813 24.852 6.333 1.00 16.24 ? 58 GLN A O 1 ATOM 460 C CB . GLN A 1 58 ? 34.907 24.608 6.116 1.00 15.98 ? 58 GLN A CB 1 ATOM 461 C CG . GLN A 1 58 ? 34.880 23.308 6.844 1.00 19.05 ? 58 GLN A CG 1 ATOM 462 C CD . GLN A 1 58 ? 34.080 22.227 6.132 1.00 22.51 ? 58 GLN A CD 1 ATOM 463 O OE1 . GLN A 1 58 ? 33.035 22.504 5.567 1.00 28.13 ? 58 GLN A OE1 1 ATOM 464 N NE2 . GLN A 1 58 ? 34.435 20.988 6.397 1.00 28.81 ? 58 GLN A NE2 1 ATOM 465 N N . TYR A 1 59 ? 37.280 25.189 8.537 1.00 14.95 ? 59 TYR A N 1 ATOM 466 C CA . TYR A 1 59 ? 38.467 24.614 9.068 1.00 15.20 ? 59 TYR A CA 1 ATOM 467 C C . TYR A 1 59 ? 38.098 23.298 9.756 1.00 16.18 ? 59 TYR A C 1 ATOM 468 O O . TYR A 1 59 ? 37.283 23.275 10.684 1.00 17.45 ? 59 TYR A O 1 ATOM 469 C CB . TYR A 1 59 ? 39.078 25.553 10.098 1.00 14.84 ? 59 TYR A CB 1 ATOM 470 C CG . TYR A 1 59 ? 39.570 26.927 9.538 1.00 15.73 ? 59 TYR A CG 1 ATOM 471 C CD1 . TYR A 1 59 ? 38.699 27.947 9.350 1.00 16.06 ? 59 TYR A CD1 1 ATOM 472 C CD2 . TYR A 1 59 ? 40.914 27.137 9.196 1.00 16.55 ? 59 TYR A CD2 1 ATOM 473 C CE1 . TYR A 1 59 ? 39.098 29.125 8.881 1.00 16.82 ? 59 TYR A CE1 1 ATOM 474 C CE2 . TYR A 1 59 ? 41.315 28.370 8.723 1.00 17.81 ? 59 TYR A CE2 1 ATOM 475 C CZ . TYR A 1 59 ? 40.414 29.343 8.573 1.00 18.86 ? 59 TYR A CZ 1 ATOM 476 O OH . TYR A 1 59 ? 40.808 30.628 8.062 1.00 23.73 ? 59 TYR A OH 1 ATOM 477 N N . ASP A 1 60 ? 38.837 22.240 9.444 1.00 19.24 ? 60 ASP A N 1 ATOM 478 C CA . ASP A 1 60 ? 38.545 20.953 9.994 1.00 19.11 ? 60 ASP A CA 1 ATOM 479 C C . ASP A 1 60 ? 39.469 20.595 11.129 1.00 18.20 ? 60 ASP A C 1 ATOM 480 O O . ASP A 1 60 ? 40.642 21.038 11.191 1.00 20.89 ? 60 ASP A O 1 ATOM 481 C CB . ASP A 1 60 ? 38.592 19.894 8.920 1.00 22.52 ? 60 ASP A CB 1 ATOM 482 C CG . ASP A 1 60 ? 37.455 20.030 7.920 1.00 27.11 ? 60 ASP A CG 1 ATOM 483 O OD1 . ASP A 1 60 ? 36.234 20.343 8.361 1.00 27.27 ? 60 ASP A OD1 1 ATOM 484 O OD2 . ASP A 1 60 ? 37.599 19.725 6.745 1.00 34.21 ? 60 ASP A OD2 1 ATOM 485 N N . GLN A 1 61 ? 38.999 19.716 12.002 1.00 18.26 ? 61 GLN A N 1 ATOM 486 C CA . GLN A 1 61 ? 39.825 19.080 12.997 1.00 20.18 ? 61 GLN A CA 1 ATOM 487 C C . GLN A 1 61 ? 40.547 20.079 13.806 1.00 15.81 ? 61 GLN A C 1 ATOM 488 O O . GLN A 1 61 ? 41.768 19.969 14.076 1.00 21.66 ? 61 GLN A O 1 ATOM 489 C CB . GLN A 1 61 ? 40.796 18.026 12.364 1.00 22.14 ? 61 GLN A CB 1 ATOM 490 C CG . GLN A 1 61 ? 41.002 16.904 13.144 1.00 22.33 ? 61 GLN A CG 1 ATOM 491 C CD . GLN A 1 61 ? 41.654 15.759 12.354 1.00 21.08 ? 61 GLN A CD 1 ATOM 492 O OE1 . GLN A 1 61 ? 41.188 15.416 11.287 1.00 28.33 ? 61 GLN A OE1 1 ATOM 493 N NE2 . GLN A 1 61 ? 42.691 15.140 12.937 1.00 21.08 ? 61 GLN A NE2 1 ATOM 494 N N . ILE A 1 62 ? 39.801 21.134 14.225 1.00 16.87 ? 62 ILE A N 1 ATOM 495 C CA . ILE A 1 62 ? 40.319 22.184 15.069 1.00 14.81 ? 62 ILE A CA 1 ATOM 496 C C . ILE A 1 62 ? 40.049 21.974 16.602 1.00 16.43 ? 62 ILE A C 1 ATOM 497 O O . ILE A 1 62 ? 38.912 21.892 17.018 1.00 15.43 ? 62 ILE A O 1 ATOM 498 C CB . ILE A 1 62 ? 39.673 23.609 14.660 1.00 17.42 ? 62 ILE A CB 1 ATOM 499 C CG1 . ILE A 1 62 ? 39.955 23.977 13.265 1.00 18.86 ? 62 ILE A CG1 1 ATOM 500 C CG2 . ILE A 1 62 ? 40.094 24.628 15.597 1.00 16.46 ? 62 ILE A CG2 1 ATOM 501 C CD1 . ILE A 1 62 ? 41.451 24.195 12.951 1.00 21.10 ? 62 ILE A CD1 1 ATOM 502 N N . PRO A 1 63 ? 41.062 22.062 17.427 1.00 16.92 ? 63 PRO A N 1 ATOM 503 C CA . PRO A 1 63 ? 40.838 21.982 18.915 1.00 17.34 ? 63 PRO A CA 1 ATOM 504 C C . PRO A 1 63 ? 40.127 23.214 19.487 1.00 17.13 ? 63 PRO A C 1 ATOM 505 O O . PRO A 1 63 ? 40.477 24.354 19.126 1.00 18.14 ? 63 PRO A O 1 ATOM 506 C CB . PRO A 1 63 ? 42.315 21.773 19.488 1.00 18.47 ? 63 PRO A CB 1 ATOM 507 C CG . PRO A 1 63 ? 43.092 21.194 18.214 1.00 18.76 ? 63 PRO A CG 1 ATOM 508 C CD . PRO A 1 63 ? 42.528 21.961 17.087 1.00 16.79 ? 63 PRO A CD 1 ATOM 509 N N . VAL A 1 64 ? 39.067 22.981 20.261 1.00 16.71 ? 64 VAL A N 1 ATOM 510 C CA . VAL A 1 64 ? 38.362 24.033 20.905 1.00 14.86 ? 64 VAL A CA 1 ATOM 511 C C . VAL A 1 64 ? 38.025 23.591 22.362 1.00 16.83 ? 64 VAL A C 1 ATOM 512 O O . VAL A 1 64 ? 37.442 22.544 22.557 1.00 17.41 ? 64 VAL A O 1 ATOM 513 C CB . VAL A 1 64 ? 36.982 24.368 20.192 1.00 15.91 ? 64 VAL A CB 1 ATOM 514 C CG1 . VAL A 1 64 ? 36.329 25.524 20.906 1.00 16.34 ? 64 VAL A CG1 1 ATOM 515 C CG2 . VAL A 1 64 ? 37.164 24.679 18.795 1.00 15.94 ? 64 VAL A CG2 1 ATOM 516 N N . GLU A 1 65 ? 38.393 24.417 23.365 1.00 17.11 ? 65 GLU A N 1 ATOM 517 C CA . GLU A 1 65 ? 38.066 24.113 24.779 1.00 17.76 ? 65 GLU A CA 1 ATOM 518 C C . GLU A 1 65 ? 36.845 24.978 25.247 1.00 17.35 ? 65 GLU A C 1 ATOM 519 O O . GLU A 1 65 ? 36.878 26.193 25.184 1.00 21.08 ? 65 GLU A O 1 ATOM 520 C CB . GLU A 1 65 ? 39.279 24.358 25.725 1.00 21.09 ? 65 GLU A CB 1 ATOM 521 C CG . GLU A 1 65 ? 39.048 23.764 27.105 1.00 22.67 ? 65 GLU A CG 1 ATOM 522 C CD . GLU A 1 65 ? 40.335 23.784 28.021 1.00 32.00 ? 65 GLU A CD 1 ATOM 523 O OE1 . GLU A 1 65 ? 40.209 23.524 29.224 1.00 40.34 ? 65 GLU A OE1 1 ATOM 524 O OE2 . GLU A 1 65 ? 41.337 23.892 27.528 1.00 32.44 ? 65 GLU A OE2 1 ATOM 525 N N . ILE A 1 66 ? 35.798 24.326 25.686 1.00 16.71 ? 66 ILE A N 1 ATOM 526 C CA . ILE A 1 66 ? 34.543 24.984 25.984 1.00 17.69 ? 66 ILE A CA 1 ATOM 527 C C . ILE A 1 66 ? 34.200 24.779 27.430 1.00 18.36 ? 66 ILE A C 1 ATOM 528 O O . ILE A 1 66 ? 33.973 23.670 27.865 1.00 18.90 ? 66 ILE A O 1 ATOM 529 C CB . ILE A 1 66 ? 33.379 24.364 25.098 1.00 16.46 ? 66 ILE A CB 1 ATOM 530 C CG1 . ILE A 1 66 ? 33.742 24.403 23.554 1.00 17.32 ? 66 ILE A CG1 1 ATOM 531 C CG2 . ILE A 1 66 ? 32.046 24.983 25.423 1.00 18.85 ? 66 ILE A CG2 1 ATOM 532 C CD1 . ILE A 1 66 ? 32.997 23.507 22.749 1.00 18.67 ? 66 ILE A CD1 1 ATOM 533 N N . CYS A 1 67 ? 34.258 25.849 28.232 1.00 21.23 ? 67 CYS A N 1 ATOM 534 C CA . CYS A 1 67 ? 34.069 25.709 29.704 1.00 24.95 ? 67 CYS A CA 1 ATOM 535 C C . CYS A 1 67 ? 34.967 24.641 30.264 1.00 25.34 ? 67 CYS A C 1 ATOM 536 O O . CYS A 1 67 ? 34.529 23.837 31.111 1.00 27.50 ? 67 CYS A O 1 ATOM 537 C CB . CYS A 1 67 ? 32.676 25.323 30.022 1.00 26.53 ? 67 CYS A CB 1 ATOM 538 S SG . CYS A 1 67 ? 31.562 26.480 29.783 1.00 34.91 ? 67 CYS A SG 1 ATOM 539 N N . GLY A 1 68 ? 36.157 24.533 29.747 1.00 21.55 ? 68 GLY A N 1 ATOM 540 C CA . GLY A 1 68 ? 37.120 23.554 30.275 1.00 22.70 ? 68 GLY A CA 1 ATOM 541 C C . GLY A 1 68 ? 37.041 22.134 29.657 1.00 22.05 ? 68 GLY A C 1 ATOM 542 O O . GLY A 1 68 ? 37.810 21.293 30.016 1.00 25.26 ? 68 GLY A O 1 ATOM 543 N N . HIS A 1 69 ? 36.077 21.905 28.796 1.00 18.23 ? 69 HIS A N 1 ATOM 544 C CA . HIS A 1 69 ? 35.898 20.596 28.135 1.00 16.56 ? 69 HIS A CA 1 ATOM 545 C C . HIS A 1 69 ? 36.478 20.658 26.770 1.00 15.74 ? 69 HIS A C 1 ATOM 546 O O . HIS A 1 69 ? 36.245 21.612 26.027 1.00 18.21 ? 69 HIS A O 1 ATOM 547 C CB . HIS A 1 69 ? 34.405 20.221 28.038 1.00 17.79 ? 69 HIS A CB 1 ATOM 548 C CG . HIS A 1 69 ? 33.700 20.067 29.363 1.00 22.72 ? 69 HIS A CG 1 ATOM 549 N ND1 . HIS A 1 69 ? 32.361 20.163 29.440 1.00 41.64 ? 69 HIS A ND1 1 ATOM 550 C CD2 . HIS A 1 69 ? 34.082 19.598 30.541 1.00 35.67 ? 69 HIS A CD2 1 ATOM 551 C CE1 . HIS A 1 69 ? 31.999 20.112 30.734 1.00 39.78 ? 69 HIS A CE1 1 ATOM 552 N NE2 . HIS A 1 69 ? 33.015 19.821 31.412 1.00 28.19 ? 69 HIS A NE2 1 ATOM 553 N N . LYS A 1 70 ? 37.190 19.605 26.373 1.00 16.80 ? 70 LYS A N 1 ATOM 554 C CA . LYS A 1 70 ? 37.874 19.557 25.090 1.00 18.05 ? 70 LYS A CA 1 ATOM 555 C C . LYS A 1 70 ? 37.013 19.024 23.913 1.00 16.03 ? 70 LYS A C 1 ATOM 556 O O . LYS A 1 70 ? 36.346 17.976 24.020 1.00 17.43 ? 70 LYS A O 1 ATOM 557 C CB . LYS A 1 70 ? 39.163 18.767 25.225 1.00 21.90 ? 70 LYS A CB 1 ATOM 558 C CG . LYS A 1 70 ? 40.224 19.486 26.169 1.00 27.91 ? 70 LYS A CG 1 ATOM 559 C CD . LYS A 1 70 ? 41.442 18.586 26.499 1.00 35.63 ? 70 LYS A CD 1 ATOM 560 C CE . LYS A 1 70 ? 42.224 19.177 27.626 1.00 41.28 ? 70 LYS A CE 1 ATOM 561 N NZ . LYS A 1 70 ? 43.671 19.204 27.341 1.00 47.17 ? 70 LYS A NZ 1 ATOM 562 N N . ALA A 1 71 ? 37.136 19.676 22.788 1.00 14.39 ? 71 ALA A N 1 ATOM 563 C CA . ALA A 1 71 ? 36.590 19.188 21.546 1.00 13.87 ? 71 ALA A CA 1 ATOM 564 C C . ALA A 1 71 ? 37.637 19.380 20.443 1.00 13.38 ? 71 ALA A C 1 ATOM 565 O O . ALA A 1 71 ? 38.532 20.244 20.579 1.00 16.36 ? 71 ALA A O 1 ATOM 566 C CB . ALA A 1 71 ? 35.306 19.952 21.209 1.00 13.51 ? 71 ALA A CB 1 ATOM 567 N N . ILE A 1 72 ? 37.537 18.618 19.419 1.00 14.18 ? 72 ILE A N 1 ATOM 568 C CA . ILE A 1 72 ? 38.308 18.847 18.169 1.00 14.64 ? 72 ILE A CA 1 ATOM 569 C C . ILE A 1 72 ? 37.449 18.558 16.991 1.00 14.94 ? 72 ILE A C 1 ATOM 570 O O . ILE A 1 72 ? 37.004 17.446 16.802 1.00 15.92 ? 72 ILE A O 1 ATOM 571 C CB . ILE A 1 72 ? 39.591 17.876 18.107 1.00 15.63 ? 72 ILE A CB 1 ATOM 572 C CG1 . ILE A 1 72 ? 40.406 17.934 19.373 1.00 14.90 ? 72 ILE A CG1 1 ATOM 573 C CG2 . ILE A 1 72 ? 40.386 18.197 16.872 1.00 16.56 ? 72 ILE A CG2 1 ATOM 574 C CD1 . ILE A 1 72 ? 41.605 16.965 19.408 1.00 17.18 ? 72 ILE A CD1 1 ATOM 575 N N . GLY A 1 73 ? 37.126 19.590 16.203 1.00 14.38 ? 73 GLY A N 1 ATOM 576 C CA . GLY A 1 73 ? 36.213 19.418 15.104 1.00 15.04 ? 73 GLY A CA 1 ATOM 577 C C . GLY A 1 73 ? 36.126 20.611 14.238 1.00 13.49 ? 73 GLY A C 1 ATOM 578 O O . GLY A 1 73 ? 37.028 21.462 14.250 1.00 15.26 ? 73 GLY A O 1 ATOM 579 N N . THR A 1 74 ? 35.109 20.634 13.415 1.00 14.48 ? 74 THR A N 1 ATOM 580 C CA . THR A 1 74 ? 34.984 21.623 12.362 1.00 13.41 ? 74 THR A CA 1 ATOM 581 C C . THR A 1 74 ? 34.521 22.943 12.904 1.00 13.32 ? 74 THR A C 1 ATOM 582 O O . THR A 1 74 ? 33.567 23.029 13.711 1.00 13.10 ? 74 THR A O 1 ATOM 583 C CB . THR A 1 74 ? 34.045 21.083 11.325 1.00 15.86 ? 74 THR A CB 1 ATOM 584 O OG1 . THR A 1 74 ? 34.596 19.868 10.758 1.00 20.19 ? 74 THR A OG1 1 ATOM 585 C CG2 . THR A 1 74 ? 33.856 22.000 10.238 1.00 16.58 ? 74 THR A CG2 1 ATOM 586 N N . VAL A 1 75 ? 35.204 24.013 12.511 1.00 12.43 ? 75 VAL A N 1 ATOM 587 C CA . VAL A 1 75 ? 34.819 25.377 12.818 1.00 12.87 ? 75 VAL A CA 1 ATOM 588 C C . VAL A 1 75 ? 34.663 26.137 11.521 1.00 11.91 ? 75 VAL A C 1 ATOM 589 O O . VAL A 1 75 ? 35.532 26.126 10.656 1.00 13.58 ? 75 VAL A O 1 ATOM 590 C CB . VAL A 1 75 ? 35.873 26.028 13.705 1.00 14.34 ? 75 VAL A CB 1 ATOM 591 C CG1 . VAL A 1 75 ? 35.643 27.460 13.925 1.00 13.91 ? 75 VAL A CG1 1 ATOM 592 C CG2 . VAL A 1 75 ? 36.030 25.271 15.027 1.00 15.38 ? 75 VAL A CG2 1 ATOM 593 N N . LEU A 1 76 ? 33.529 26.786 11.370 1.00 11.62 ? 76 LEU A N 1 ATOM 594 C CA . LEU A 1 76 ? 33.255 27.664 10.242 1.00 11.68 ? 76 LEU A CA 1 ATOM 595 C C . LEU A 1 76 ? 33.507 29.072 10.688 1.00 10.98 ? 76 LEU A C 1 ATOM 596 O O . LEU A 1 76 ? 33.077 29.460 11.764 1.00 13.71 ? 76 LEU A O 1 ATOM 597 C CB . LEU A 1 76 ? 31.775 27.470 9.774 1.00 11.74 ? 76 LEU A CB 1 ATOM 598 C CG . LEU A 1 76 ? 31.379 26.038 9.503 1.00 12.04 ? 76 LEU A CG 1 ATOM 599 C CD1 . LEU A 1 76 ? 29.930 25.962 9.028 1.00 13.14 ? 76 LEU A CD1 1 ATOM 600 C CD2 . LEU A 1 76 ? 32.302 25.353 8.471 1.00 13.45 ? 76 LEU A CD2 1 ATOM 601 N N . VAL A 1 77 ? 34.123 29.884 9.826 1.00 11.10 ? 77 VAL A N 1 ATOM 602 C CA . VAL A 1 77 ? 34.415 31.270 10.144 1.00 11.76 ? 77 VAL A CA 1 ATOM 603 C C . VAL A 1 77 ? 33.751 32.162 9.108 1.00 11.36 ? 77 VAL A C 1 ATOM 604 O O . VAL A 1 77 ? 33.965 31.989 7.912 1.00 12.22 ? 77 VAL A O 1 ATOM 605 C CB . VAL A 1 77 ? 35.952 31.530 10.155 1.00 13.68 ? 77 VAL A CB 1 ATOM 606 C CG1 . VAL A 1 77 ? 36.265 33.011 10.403 1.00 15.32 ? 77 VAL A CG1 1 ATOM 607 C CG2 . VAL A 1 77 ? 36.622 30.679 11.213 1.00 16.07 ? 77 VAL A CG2 1 ATOM 608 N N . GLY A 1 78 ? 32.960 33.109 9.559 1.00 11.45 ? 78 GLY A N 1 ATOM 609 C CA . GLY A 1 78 ? 32.274 34.021 8.626 1.00 13.32 ? 78 GLY A CA 1 ATOM 610 C C . GLY A 1 78 ? 31.315 34.913 9.371 1.00 12.43 ? 78 GLY A C 1 ATOM 611 O O . GLY A 1 78 ? 31.325 35.004 10.593 1.00 13.28 ? 78 GLY A O 1 ATOM 612 N N . PRO A 1 79 ? 30.449 35.606 8.611 1.00 13.00 ? 79 PRO A N 1 ATOM 613 C CA . PRO A 1 79 ? 29.646 36.704 9.175 1.00 13.49 ? 79 PRO A CA 1 ATOM 614 C C . PRO A 1 79 ? 28.442 36.186 9.885 1.00 13.71 ? 79 PRO A C 1 ATOM 615 O O . PRO A 1 79 ? 27.342 36.499 9.535 1.00 18.42 ? 79 PRO A O 1 ATOM 616 C CB . PRO A 1 79 ? 29.257 37.538 7.952 1.00 14.97 ? 79 PRO A CB 1 ATOM 617 C CG . PRO A 1 79 ? 29.242 36.562 6.826 1.00 14.79 ? 79 PRO A CG 1 ATOM 618 C CD . PRO A 1 79 ? 30.424 35.611 7.112 1.00 14.11 ? 79 PRO A CD 1 ATOM 619 N N . THR A 1 80 ? 28.648 35.451 10.892 1.00 17.95 ? 80 THR A N 1 ATOM 620 C CA . THR A 1 80 ? 27.599 35.138 11.841 1.00 16.10 ? 80 THR A CA 1 ATOM 621 C C . THR A 1 80 ? 27.349 36.321 12.780 1.00 15.16 ? 80 THR A C 1 ATOM 622 O O . THR A 1 80 ? 28.304 37.062 13.127 1.00 18.24 ? 80 THR A O 1 ATOM 623 C CB . THR A 1 80 ? 27.957 33.895 12.659 1.00 14.80 ? 80 THR A CB 1 ATOM 624 O OG1 . THR A 1 80 ? 26.930 33.665 13.645 1.00 15.00 ? 80 THR A OG1 1 ATOM 625 C CG2 . THR A 1 80 ? 29.318 34.039 13.414 1.00 13.19 ? 80 THR A CG2 1 ATOM 626 N N . PRO A 1 81 ? 26.105 36.536 13.276 1.00 16.32 ? 81 PRO A N 1 ATOM 627 C CA . PRO A 1 81 ? 25.849 37.615 14.204 1.00 15.89 ? 81 PRO A CA 1 ATOM 628 C C . PRO A 1 81 ? 26.561 37.488 15.582 1.00 14.60 ? 81 PRO A C 1 ATOM 629 O O . PRO A 1 81 ? 26.748 38.497 16.309 1.00 17.40 ? 81 PRO A O 1 ATOM 630 C CB . PRO A 1 81 ? 24.319 37.568 14.395 1.00 18.96 ? 81 PRO A CB 1 ATOM 631 C CG . PRO A 1 81 ? 23.956 36.212 14.000 1.00 21.16 ? 81 PRO A CG 1 ATOM 632 C CD . PRO A 1 81 ? 24.843 35.838 12.878 1.00 18.23 ? 81 PRO A CD 1 ATOM 633 N N A VAL A 1 82 ? 26.899 36.280 15.945 0.50 14.33 ? 82 VAL A N 1 ATOM 634 N N B VAL A 1 82 ? 26.749 36.295 16.038 0.50 13.89 ? 82 VAL A N 1 ATOM 635 C CA A VAL A 1 82 ? 27.455 35.976 17.262 0.50 15.62 ? 82 VAL A CA 1 ATOM 636 C CA B VAL A 1 82 ? 27.548 36.039 17.293 0.50 13.59 ? 82 VAL A CA 1 ATOM 637 C C A VAL A 1 82 ? 28.215 34.637 17.101 0.50 12.57 ? 82 VAL A C 1 ATOM 638 C C B VAL A 1 82 ? 28.200 34.677 17.118 0.50 11.42 ? 82 VAL A C 1 ATOM 639 O O A VAL A 1 82 ? 27.873 33.829 16.251 0.50 13.64 ? 82 VAL A O 1 ATOM 640 O O B VAL A 1 82 ? 27.713 33.831 16.341 0.50 11.84 ? 82 VAL A O 1 ATOM 641 C CB A VAL A 1 82 ? 26.289 35.865 18.366 0.50 18.94 ? 82 VAL A CB 1 ATOM 642 C CB B VAL A 1 82 ? 26.636 36.055 18.584 0.50 13.45 ? 82 VAL A CB 1 ATOM 643 C CG1 A VAL A 1 82 ? 26.777 35.361 19.587 0.50 20.58 ? 82 VAL A CG1 1 ATOM 644 C CG1 B VAL A 1 82 ? 25.606 34.866 18.524 0.50 13.39 ? 82 VAL A CG1 1 ATOM 645 C CG2 A VAL A 1 82 ? 25.646 37.225 18.579 0.50 21.35 ? 82 VAL A CG2 1 ATOM 646 C CG2 B VAL A 1 82 ? 27.500 36.040 19.918 0.50 17.64 ? 82 VAL A CG2 1 ATOM 647 N N . ASN A 1 83 ? 29.262 34.454 17.843 1.00 12.23 ? 83 ASN A N 1 ATOM 648 C CA . ASN A 1 83 ? 29.918 33.163 17.868 1.00 10.18 ? 83 ASN A CA 1 ATOM 649 C C . ASN A 1 83 ? 28.940 32.126 18.410 1.00 9.56 ? 83 ASN A C 1 ATOM 650 O O . ASN A 1 83 ? 28.401 32.316 19.499 1.00 10.88 ? 83 ASN A O 1 ATOM 651 C CB . ASN A 1 83 ? 31.117 33.193 18.780 1.00 11.76 ? 83 ASN A CB 1 ATOM 652 C CG . ASN A 1 83 ? 32.228 34.110 18.333 1.00 12.81 ? 83 ASN A CG 1 ATOM 653 O OD1 . ASN A 1 83 ? 32.509 34.281 17.161 1.00 14.86 ? 83 ASN A OD1 1 ATOM 654 N ND2 . ASN A 1 83 ? 32.948 34.643 19.332 1.00 14.53 ? 83 ASN A ND2 1 ATOM 655 N N . ILE A 1 84 ? 28.751 31.011 17.701 1.00 9.71 ? 84 ILE A N 1 ATOM 656 C CA . ILE A 1 84 ? 27.874 29.936 18.121 1.00 9.20 ? 84 ILE A CA 1 ATOM 657 C C . ILE A 1 84 ? 28.601 28.631 18.142 1.00 9.26 ? 84 ILE A C 1 ATOM 658 O O . ILE A 1 84 ? 29.316 28.267 17.216 1.00 10.16 ? 84 ILE A O 1 ATOM 659 C CB . ILE A 1 84 ? 26.576 29.869 17.267 1.00 9.70 ? 84 ILE A CB 1 ATOM 660 C CG1 . ILE A 1 84 ? 26.827 29.553 15.830 1.00 11.46 ? 84 ILE A CG1 1 ATOM 661 C CG2 . ILE A 1 84 ? 25.763 31.145 17.415 1.00 10.32 ? 84 ILE A CG2 1 ATOM 662 C CD1 . ILE A 1 84 ? 25.551 29.561 14.956 1.00 11.38 ? 84 ILE A CD1 1 ATOM 663 N N . ILE A 1 85 ? 28.365 27.876 19.221 1.00 9.14 ? 85 ILE A N 1 ATOM 664 C CA . ILE A 1 85 ? 28.828 26.486 19.351 1.00 9.36 ? 85 ILE A CA 1 ATOM 665 C C . ILE A 1 85 ? 27.675 25.579 19.001 1.00 8.57 ? 85 ILE A C 1 ATOM 666 O O . ILE A 1 85 ? 26.640 25.590 19.683 1.00 9.80 ? 85 ILE A O 1 ATOM 667 C CB . ILE A 1 85 ? 29.323 26.183 20.762 1.00 10.01 ? 85 ILE A CB 1 ATOM 668 C CG1 . ILE A 1 85 ? 30.370 27.194 21.246 1.00 11.67 ? 85 ILE A CG1 1 ATOM 669 C CG2 . ILE A 1 85 ? 29.861 24.734 20.790 1.00 11.12 ? 85 ILE A CG2 1 ATOM 670 C CD1 . ILE A 1 85 ? 31.564 27.345 20.370 1.00 13.23 ? 85 ILE A CD1 1 ATOM 671 N N . GLY A 1 86 ? 27.790 24.868 17.881 1.00 8.59 ? 86 GLY A N 1 ATOM 672 C CA . GLY A 1 86 ? 26.758 23.991 17.406 1.00 8.51 ? 86 GLY A CA 1 ATOM 673 C C . GLY A 1 86 ? 26.921 22.578 17.831 1.00 8.53 ? 86 GLY A C 1 ATOM 674 O O . GLY A 1 86 ? 27.866 22.214 18.537 1.00 8.90 ? 86 GLY A O 1 ATOM 675 N N . ARG A 1 87 ? 26.007 21.718 17.375 1.00 8.02 ? 87 ARG A N 1 ATOM 676 C CA . ARG A 1 87 ? 25.947 20.365 17.846 1.00 8.66 ? 87 ARG A CA 1 ATOM 677 C C . ARG A 1 87 ? 27.176 19.545 17.514 1.00 9.21 ? 87 ARG A C 1 ATOM 678 O O . ARG A 1 87 ? 27.501 18.630 18.264 1.00 9.73 ? 87 ARG A O 1 ATOM 679 C CB . ARG A 1 87 ? 24.700 19.647 17.320 1.00 8.89 ? 87 ARG A CB 1 ATOM 680 C CG . ARG A 1 87 ? 23.394 20.197 17.875 1.00 8.86 ? 87 ARG A CG 1 ATOM 681 C CD . ARG A 1 87 ? 22.170 19.403 17.430 1.00 9.28 ? 87 ARG A CD 1 ATOM 682 N NE . ARG A 1 87 ? 21.968 19.409 15.990 1.00 9.49 ? 87 ARG A NE 1 ATOM 683 C CZ . ARG A 1 87 ? 22.388 18.449 15.166 1.00 10.06 ? 87 ARG A CZ 1 ATOM 684 N NH1 . ARG A 1 87 ? 22.890 17.326 15.617 1.00 10.43 ? 87 ARG A NH1 1 ATOM 685 N NH2 . ARG A 1 87 ? 22.216 18.648 13.886 1.00 10.97 ? 87 ARG A NH2 1 ATOM 686 N N . ASN A 1 88 ? 27.887 19.896 16.470 1.00 9.32 ? 88 ASN A N 1 ATOM 687 C CA . ASN A 1 88 ? 29.106 19.153 16.155 1.00 10.08 ? 88 ASN A CA 1 ATOM 688 C C . ASN A 1 88 ? 30.087 19.154 17.303 1.00 9.96 ? 88 ASN A C 1 ATOM 689 O O . ASN A 1 88 ? 30.781 18.162 17.501 1.00 12.07 ? 88 ASN A O 1 ATOM 690 C CB . ASN A 1 88 ? 29.735 19.654 14.850 1.00 11.21 ? 88 ASN A CB 1 ATOM 691 C CG . ASN A 1 88 ? 30.436 20.961 15.006 1.00 11.05 ? 88 ASN A CG 1 ATOM 692 O OD1 . ASN A 1 88 ? 29.816 21.949 15.423 1.00 10.95 ? 88 ASN A OD1 1 ATOM 693 N ND2 . ASN A 1 88 ? 31.706 21.004 14.621 1.00 11.46 ? 88 ASN A ND2 1 ATOM 694 N N . LEU A 1 89 ? 30.193 20.262 18.060 1.00 9.73 ? 89 LEU A N 1 ATOM 695 C CA . LEU A 1 89 ? 31.034 20.331 19.239 1.00 10.55 ? 89 LEU A CA 1 ATOM 696 C C . LEU A 1 89 ? 30.293 20.075 20.534 1.00 9.81 ? 89 LEU A C 1 ATOM 697 O O . LEU A 1 89 ? 30.881 19.546 21.469 1.00 11.24 ? 89 LEU A O 1 ATOM 698 C CB . LEU A 1 89 ? 31.836 21.634 19.272 1.00 10.63 ? 89 LEU A CB 1 ATOM 699 C CG . LEU A 1 89 ? 32.687 21.958 18.057 1.00 11.41 ? 89 LEU A CG 1 ATOM 700 C CD1 . LEU A 1 89 ? 33.503 23.222 18.294 1.00 13.05 ? 89 LEU A CD1 1 ATOM 701 C CD2 . LEU A 1 89 ? 33.615 20.800 17.673 1.00 12.99 ? 89 LEU A CD2 1 ATOM 702 N N . LEU A 1 90 ? 29.012 20.439 20.626 1.00 9.75 ? 90 LEU A N 1 ATOM 703 C CA . LEU A 1 90 ? 28.258 20.161 21.849 1.00 9.36 ? 90 LEU A CA 1 ATOM 704 C C . LEU A 1 90 ? 28.221 18.668 22.129 1.00 9.28 ? 90 LEU A C 1 ATOM 705 O O . LEU A 1 90 ? 28.290 18.263 23.285 1.00 10.52 ? 90 LEU A O 1 ATOM 706 C CB . LEU A 1 90 ? 26.836 20.707 21.745 1.00 9.47 ? 90 LEU A CB 1 ATOM 707 C CG . LEU A 1 90 ? 26.686 22.226 21.620 1.00 10.22 ? 90 LEU A CG 1 ATOM 708 C CD1 . LEU A 1 90 ? 25.228 22.610 21.379 1.00 11.95 ? 90 LEU A CD1 1 ATOM 709 C CD2 . LEU A 1 90 ? 27.219 22.988 22.825 1.00 12.09 ? 90 LEU A CD2 1 ATOM 710 N N . THR A 1 91 ? 28.118 17.837 21.093 1.00 9.64 ? 91 THR A N 1 ATOM 711 C CA . THR A 1 91 ? 28.120 16.392 21.315 1.00 10.34 ? 91 THR A CA 1 ATOM 712 C C . THR A 1 91 ? 29.464 15.914 21.878 1.00 9.88 ? 91 THR A C 1 ATOM 713 O O . THR A 1 91 ? 29.499 15.047 22.733 1.00 12.32 ? 91 THR A O 1 ATOM 714 C CB . THR A 1 91 ? 27.808 15.643 20.040 1.00 10.84 ? 91 THR A CB 1 ATOM 715 O OG1 . THR A 1 91 ? 28.726 16.002 19.005 1.00 12.52 ? 91 THR A OG1 1 ATOM 716 C CG2 . THR A 1 91 ? 26.405 15.853 19.571 1.00 12.40 ? 91 THR A CG2 1 ATOM 717 N N . GLN A 1 92 ? 30.539 16.517 21.465 1.00 10.75 ? 92 GLN A N 1 ATOM 718 C CA . GLN A 1 92 ? 31.878 16.096 21.906 1.00 11.30 ? 92 GLN A CA 1 ATOM 719 C C . GLN A 1 92 ? 32.089 16.354 23.350 1.00 11.86 ? 92 GLN A C 1 ATOM 720 O O . GLN A 1 92 ? 32.775 15.580 24.018 1.00 14.53 ? 92 GLN A O 1 ATOM 721 C CB . GLN A 1 92 ? 32.983 16.797 21.104 1.00 12.37 ? 92 GLN A CB 1 ATOM 722 C CG . GLN A 1 92 ? 33.011 16.429 19.624 1.00 12.82 ? 92 GLN A CG 1 ATOM 723 C CD . GLN A 1 92 ? 34.300 16.739 18.977 1.00 13.14 ? 92 GLN A CD 1 ATOM 724 O OE1 . GLN A 1 92 ? 35.323 16.922 19.678 1.00 14.38 ? 92 GLN A OE1 1 ATOM 725 N NE2 . GLN A 1 92 ? 34.329 16.732 17.674 1.00 14.02 ? 92 GLN A NE2 1 ATOM 726 N N . ILE A 1 93 ? 31.497 17.425 23.911 1.00 11.35 ? 93 ILE A N 1 ATOM 727 C CA . ILE A 1 93 ? 31.625 17.763 25.302 1.00 12.60 ? 93 ILE A CA 1 ATOM 728 C C . ILE A 1 93 ? 30.558 17.128 26.177 1.00 13.73 ? 93 ILE A C 1 ATOM 729 O O . ILE A 1 93 ? 30.514 17.394 27.407 1.00 15.32 ? 93 ILE A O 1 ATOM 730 C CB . ILE A 1 93 ? 31.745 19.306 25.539 1.00 14.20 ? 93 ILE A CB 1 ATOM 731 C CG1 . ILE A 1 93 ? 30.416 20.029 25.238 1.00 12.80 ? 93 ILE A CG1 1 ATOM 732 C CG2 . ILE A 1 93 ? 32.910 19.873 24.748 1.00 14.93 ? 93 ILE A CG2 1 ATOM 733 C CD1 . ILE A 1 93 ? 30.451 21.460 25.580 1.00 14.98 ? 93 ILE A CD1 1 ATOM 734 N N . GLY A 1 94 ? 29.678 16.304 25.567 1.00 12.23 ? 94 GLY A N 1 ATOM 735 C CA . GLY A 1 94 ? 28.703 15.562 26.316 1.00 13.46 ? 94 GLY A CA 1 ATOM 736 C C . GLY A 1 94 ? 27.461 16.334 26.689 1.00 13.64 ? 94 GLY A C 1 ATOM 737 O O . GLY A 1 94 ? 26.793 15.972 27.620 1.00 15.30 ? 94 GLY A O 1 ATOM 738 N N A CYS A 1 95 ? 27.101 17.327 25.899 0.50 13.18 ? 95 CYS A N 1 ATOM 739 N N B CYS A 1 95 ? 27.155 17.364 25.954 0.50 12.75 ? 95 CYS A N 1 ATOM 740 C CA A CYS A 1 95 ? 25.865 18.124 26.160 0.50 13.40 ? 95 CYS A CA 1 ATOM 741 C CA B CYS A 1 95 ? 26.063 18.261 26.299 0.50 12.64 ? 95 CYS A CA 1 ATOM 742 C C A CYS A 1 95 ? 24.674 17.402 25.909 0.50 13.81 ? 95 CYS A C 1 ATOM 743 C C B CYS A 1 95 ? 24.701 17.680 25.814 0.50 13.90 ? 95 CYS A C 1 ATOM 744 O O A CYS A 1 95 ? 24.485 16.789 24.794 0.50 15.63 ? 95 CYS A O 1 ATOM 745 O O B CYS A 1 95 ? 24.589 17.165 24.708 0.50 15.65 ? 95 CYS A O 1 ATOM 746 C CB A CYS A 1 95 ? 25.836 19.309 25.300 0.50 13.29 ? 95 CYS A CB 1 ATOM 747 C CB B CYS A 1 95 ? 26.313 19.608 25.637 0.50 12.05 ? 95 CYS A CB 1 ATOM 748 S SG A CYS A 1 95 ? 26.822 20.561 25.810 0.50 19.46 ? 95 CYS A SG 1 ATOM 749 S SG B CYS A 1 95 ? 25.189 20.907 26.088 0.50 11.53 ? 95 CYS A SG 1 ATOM 750 N N . THR A 1 96 ? 23.713 17.650 26.759 1.00 13.94 ? 96 THR A N 1 ATOM 751 C CA . THR A 1 96 ? 22.378 17.248 26.480 1.00 13.59 ? 96 THR A CA 1 ATOM 752 C C . THR A 1 96 ? 21.397 18.301 26.950 1.00 12.68 ? 96 THR A C 1 ATOM 753 O O . THR A 1 96 ? 21.734 19.172 27.712 1.00 13.65 ? 96 THR A O 1 ATOM 754 C CB . THR A 1 96 ? 21.987 15.914 27.176 1.00 16.90 ? 96 THR A CB 1 ATOM 755 O OG1 . THR A 1 96 ? 22.143 16.053 28.602 1.00 17.81 ? 96 THR A OG1 1 ATOM 756 C CG2 . THR A 1 96 ? 22.879 14.735 26.688 1.00 18.35 ? 96 THR A CG2 1 ATOM 757 N N . LEU A 1 97 ? 20.177 18.221 26.421 1.00 12.57 ? 97 LEU A N 1 ATOM 758 C CA . LEU A 1 97 ? 19.041 19.029 26.932 1.00 12.96 ? 97 LEU A CA 1 ATOM 759 C C . LEU A 1 97 ? 18.255 18.178 27.906 1.00 13.77 ? 97 LEU A C 1 ATOM 760 O O . LEU A 1 97 ? 18.061 17.025 27.669 1.00 15.41 ? 97 LEU A O 1 ATOM 761 C CB . LEU A 1 97 ? 18.118 19.475 25.775 1.00 11.64 ? 97 LEU A CB 1 ATOM 762 C CG . LEU A 1 97 ? 18.726 20.533 24.914 1.00 10.77 ? 97 LEU A CG 1 ATOM 763 C CD1 . LEU A 1 97 ? 18.001 20.608 23.601 1.00 13.97 ? 97 LEU A CD1 1 ATOM 764 C CD2 . LEU A 1 97 ? 18.709 21.813 25.589 1.00 14.48 ? 97 LEU A CD2 1 ATOM 765 N N . ASN A 1 98 ? 17.753 18.812 28.977 1.00 14.50 ? 98 ASN A N 1 ATOM 766 C CA . ASN A 1 98 ? 17.076 18.128 30.058 1.00 15.60 ? 98 ASN A CA 1 ATOM 767 C C . ASN A 1 98 ? 15.911 18.958 30.534 1.00 15.56 ? 98 ASN A C 1 ATOM 768 O O . ASN A 1 98 ? 16.061 20.118 30.826 1.00 18.26 ? 98 ASN A O 1 ATOM 769 C CB . ASN A 1 98 ? 18.055 17.798 31.230 1.00 16.66 ? 98 ASN A CB 1 ATOM 770 C CG . ASN A 1 98 ? 19.140 16.852 30.800 1.00 19.48 ? 98 ASN A CG 1 ATOM 771 O OD1 . ASN A 1 98 ? 18.924 15.608 30.827 1.00 22.18 ? 98 ASN A OD1 1 ATOM 772 N ND2 . ASN A 1 98 ? 20.186 17.375 30.236 1.00 19.32 ? 98 ASN A ND2 1 ATOM 773 N N . PHE A 1 99 ? 14.824 18.328 30.719 1.00 18.27 ? 99 PHE A N 1 ATOM 774 C CA . PHE A 1 99 ? 13.679 18.998 31.345 1.00 18.40 ? 99 PHE A CA 1 ATOM 775 C C . PHE A 1 99 ? 12.735 17.947 32.006 1.00 22.44 ? 99 PHE A C 1 ATOM 776 O O . PHE A 1 99 ? 13.146 16.777 32.048 1.00 23.51 ? 99 PHE A O 1 ATOM 777 C CB . PHE A 1 99 ? 12.933 19.918 30.343 1.00 20.12 ? 99 PHE A CB 1 ATOM 778 C CG . PHE A 1 99 ? 12.351 19.205 29.167 1.00 20.26 ? 99 PHE A CG 1 ATOM 779 C CD1 . PHE A 1 99 ? 13.075 19.057 28.024 1.00 25.24 ? 99 PHE A CD1 1 ATOM 780 C CD2 . PHE A 1 99 ? 11.026 18.889 29.137 1.00 28.26 ? 99 PHE A CD2 1 ATOM 781 C CE1 . PHE A 1 99 ? 12.509 18.483 26.918 1.00 24.03 ? 99 PHE A CE1 1 ATOM 782 C CE2 . PHE A 1 99 ? 10.500 18.330 28.110 1.00 27.07 ? 99 PHE A CE2 1 ATOM 783 C CZ . PHE A 1 99 ? 11.259 18.123 26.946 1.00 29.77 ? 99 PHE A CZ 1 ATOM 784 O OXT . PHE A 1 99 ? 11.671 18.362 32.563 1.00 25.87 ? 99 PHE A OXT 1 ATOM 785 N N . PRO B 1 1 ? 12.872 14.625 30.481 1.00 26.37 ? 1 PRO B N 1 ATOM 786 C CA . PRO B 1 1 ? 13.702 13.683 29.741 1.00 27.13 ? 1 PRO B CA 1 ATOM 787 C C . PRO B 1 1 ? 14.927 14.281 29.298 1.00 23.81 ? 1 PRO B C 1 ATOM 788 O O . PRO B 1 1 ? 15.187 15.454 29.666 1.00 25.05 ? 1 PRO B O 1 ATOM 789 C CB . PRO B 1 1 ? 12.833 13.323 28.535 1.00 30.44 ? 1 PRO B CB 1 ATOM 790 C CG . PRO B 1 1 ? 11.907 14.442 28.388 1.00 32.22 ? 1 PRO B CG 1 ATOM 791 C CD . PRO B 1 1 ? 11.782 15.127 29.670 1.00 29.07 ? 1 PRO B CD 1 ATOM 792 N N . GLN B 1 2 ? 15.784 13.457 28.795 1.00 23.48 ? 2 GLN B N 1 ATOM 793 C CA . GLN B 1 2 ? 17.042 13.870 28.261 1.00 22.76 ? 2 GLN B CA 1 ATOM 794 C C . GLN B 1 2 ? 17.085 13.741 26.716 1.00 22.86 ? 2 GLN B C 1 ATOM 795 O O . GLN B 1 2 ? 16.745 12.674 26.125 1.00 22.96 ? 2 GLN B O 1 ATOM 796 C CB . GLN B 1 2 ? 18.163 13.040 28.867 1.00 24.33 ? 2 GLN B CB 1 ATOM 797 C CG . GLN B 1 2 ? 19.454 13.476 28.448 1.00 23.12 ? 2 GLN B CG 1 ATOM 798 C CD . GLN B 1 2 ? 20.528 12.781 29.156 1.00 26.04 ? 2 GLN B CD 1 ATOM 799 O OE1 . GLN B 1 2 ? 21.120 11.784 28.599 1.00 28.07 ? 2 GLN B OE1 1 ATOM 800 N NE2 . GLN B 1 2 ? 20.950 13.335 30.364 1.00 26.69 ? 2 GLN B NE2 1 ATOM 801 N N . ILE B 1 3 ? 17.463 14.836 26.069 1.00 20.40 ? 3 ILE B N 1 ATOM 802 C CA . ILE B 1 3 ? 17.585 14.885 24.634 1.00 20.06 ? 3 ILE B CA 1 ATOM 803 C C . ILE B 1 3 ? 19.008 15.052 24.193 1.00 18.06 ? 3 ILE B C 1 ATOM 804 O O . ILE B 1 3 ? 19.716 15.949 24.638 1.00 16.86 ? 3 ILE B O 1 ATOM 805 C CB . ILE B 1 3 ? 16.716 15.956 24.095 1.00 18.75 ? 3 ILE B CB 1 ATOM 806 C CG1 . ILE B 1 3 ? 15.336 15.680 24.509 1.00 24.56 ? 3 ILE B CG1 1 ATOM 807 C CG2 . ILE B 1 3 ? 16.817 16.033 22.581 1.00 21.61 ? 3 ILE B CG2 1 ATOM 808 C CD1 . ILE B 1 3 ? 14.593 16.522 24.230 1.00 22.20 ? 3 ILE B CD1 1 ATOM 809 N N . THR B 1 4 ? 19.478 13.985 23.540 1.00 20.89 ? 4 THR B N 1 ATOM 810 C CA . THR B 1 4 ? 20.674 13.936 22.871 1.00 19.54 ? 4 THR B CA 1 ATOM 811 C C . THR B 1 4 ? 20.847 14.999 21.796 1.00 14.64 ? 4 THR B C 1 ATOM 812 O O . THR B 1 4 ? 19.897 15.354 21.179 1.00 16.96 ? 4 THR B O 1 ATOM 813 C CB . THR B 1 4 ? 20.756 12.384 22.010 1.00 19.57 ? 4 THR B CB 1 ATOM 814 O OG1 . THR B 1 4 ? 21.890 12.259 21.599 1.00 22.11 ? 4 THR B OG1 1 ATOM 815 C CG2 . THR B 1 4 ? 19.934 12.449 20.615 1.00 25.26 ? 4 THR B CG2 1 ATOM 816 N N . LEU B 1 5 ? 22.106 15.314 21.454 1.00 11.97 ? 5 LEU B N 1 ATOM 817 C CA . LEU B 1 5 ? 22.356 16.291 20.383 1.00 9.93 ? 5 LEU B CA 1 ATOM 818 C C . LEU B 1 5 ? 23.064 15.662 19.173 1.00 10.10 ? 5 LEU B C 1 ATOM 819 O O . LEU B 1 5 ? 23.510 16.363 18.276 1.00 10.06 ? 5 LEU B O 1 ATOM 820 C CB . LEU B 1 5 ? 23.104 17.470 20.914 1.00 10.43 ? 5 LEU B CB 1 ATOM 821 C CG . LEU B 1 5 ? 22.317 18.306 21.955 1.00 10.63 ? 5 LEU B CG 1 ATOM 822 C CD1 . LEU B 1 5 ? 23.196 19.343 22.547 1.00 11.55 ? 5 LEU B CD1 1 ATOM 823 C CD2 . LEU B 1 5 ? 21.099 18.935 21.357 1.00 11.34 ? 5 LEU B CD2 1 ATOM 824 N N . TRP B 1 6 ? 23.052 14.325 19.078 1.00 10.96 ? 6 TRP B N 1 ATOM 825 C CA . TRP B 1 6 ? 23.524 13.655 17.876 1.00 11.27 ? 6 TRP B CA 1 ATOM 826 C C . TRP B 1 6 ? 22.725 14.056 16.667 1.00 11.44 ? 6 TRP B C 1 ATOM 827 O O . TRP B 1 6 ? 23.249 14.045 15.540 1.00 14.13 ? 6 TRP B O 1 ATOM 828 C CB . TRP B 1 6 ? 23.478 12.139 18.030 1.00 11.89 ? 6 TRP B CB 1 ATOM 829 C CG . TRP B 1 6 ? 24.383 11.562 19.008 1.00 11.74 ? 6 TRP B CG 1 ATOM 830 C CD1 . TRP B 1 6 ? 24.028 10.776 20.065 1.00 16.18 ? 6 TRP B CD1 1 ATOM 831 C CD2 . TRP B 1 6 ? 25.766 11.520 18.949 1.00 12.39 ? 6 TRP B CD2 1 ATOM 832 N NE1 . TRP B 1 6 ? 25.113 10.313 20.685 1.00 18.51 ? 6 TRP B NE1 1 ATOM 833 C CE2 . TRP B 1 6 ? 26.198 10.655 20.006 1.00 15.16 ? 6 TRP B CE2 1 ATOM 834 C CE3 . TRP B 1 6 ? 26.711 12.015 18.081 1.00 14.34 ? 6 TRP B CE3 1 ATOM 835 C CZ2 . TRP B 1 6 ? 27.520 10.356 20.222 1.00 17.51 ? 6 TRP B CZ2 1 ATOM 836 C CZ3 . TRP B 1 6 ? 28.083 11.737 18.360 1.00 17.74 ? 6 TRP B CZ3 1 ATOM 837 C CH2 . TRP B 1 6 ? 28.438 10.909 19.395 1.00 18.15 ? 6 TRP B CH2 1 ATOM 838 N N . LYS B 1 7 ? 21.454 14.304 16.845 1.00 11.00 ? 7 LYS B N 1 ATOM 839 C CA . LYS B 1 7 ? 20.574 14.755 15.767 1.00 10.96 ? 7 LYS B CA 1 ATOM 840 C C . LYS B 1 7 ? 19.888 16.049 16.244 1.00 9.99 ? 7 LYS B C 1 ATOM 841 O O . LYS B 1 7 ? 19.980 16.436 17.400 1.00 10.64 ? 7 LYS B O 1 ATOM 842 C CB . LYS B 1 7 ? 19.508 13.669 15.406 1.00 13.34 ? 7 LYS B CB 1 ATOM 843 C CG . LYS B 1 7 ? 18.559 13.314 16.346 1.00 18.18 ? 7 LYS B CG 1 ATOM 844 C CD . LYS B 1 7 ? 17.454 12.215 15.713 1.00 24.02 ? 7 LYS B CD 1 ATOM 845 C CE . LYS B 1 7 ? 16.544 11.634 16.772 1.00 26.45 ? 7 LYS B CE 1 ATOM 846 N NZ . LYS B 1 7 ? 15.347 10.832 16.155 1.00 36.56 ? 7 LYS B NZ 1 ATOM 847 N N . ARG B 1 8 ? 19.212 16.707 15.362 1.00 10.71 ? 8 ARG B N 1 ATOM 848 C CA . ARG B 1 8 ? 18.504 17.931 15.739 1.00 10.03 ? 8 ARG B CA 1 ATOM 849 C C . ARG B 1 8 ? 17.504 17.647 16.813 1.00 10.29 ? 8 ARG B C 1 ATOM 850 O O . ARG B 1 8 ? 16.778 16.643 16.718 1.00 11.64 ? 8 ARG B O 1 ATOM 851 C CB . ARG B 1 8 ? 17.799 18.508 14.549 1.00 11.87 ? 8 ARG B CB 1 ATOM 852 C CG . ARG B 1 8 ? 18.728 19.074 13.465 1.00 12.33 ? 8 ARG B CG 1 ATOM 853 C CD . ARG B 1 8 ? 17.984 19.805 12.366 1.00 16.65 ? 8 ARG B CD 1 ATOM 854 N NE . ARG B 1 8 ? 18.893 20.425 11.448 1.00 20.33 ? 8 ARG B NE 1 ATOM 855 C CZ . ARG B 1 8 ? 18.528 21.454 10.553 1.00 20.26 ? 8 ARG B CZ 1 ATOM 856 N NH1 . ARG B 1 8 ? 17.356 22.175 10.798 1.00 29.12 ? 8 ARG B NH1 1 ATOM 857 N NH2 . ARG B 1 8 ? 19.452 21.980 9.735 1.00 19.66 ? 8 ARG B NH2 1 ATOM 858 N N . PRO B 1 9 ? 17.392 18.489 17.828 1.00 9.33 ? 9 PRO B N 1 ATOM 859 C CA . PRO B 1 9 ? 16.482 18.214 18.959 1.00 10.43 ? 9 PRO B CA 1 ATOM 860 C C . PRO B 1 9 ? 15.065 18.681 18.623 1.00 9.79 ? 9 PRO B C 1 ATOM 861 O O . PRO B 1 9 ? 14.547 19.634 19.165 1.00 10.89 ? 9 PRO B O 1 ATOM 862 C CB . PRO B 1 9 ? 17.093 19.015 20.102 1.00 10.83 ? 9 PRO B CB 1 ATOM 863 C CG . PRO B 1 9 ? 17.775 20.173 19.393 1.00 10.48 ? 9 PRO B CG 1 ATOM 864 C CD . PRO B 1 9 ? 18.340 19.575 18.137 1.00 9.92 ? 9 PRO B CD 1 ATOM 865 N N . LEU B 1 10 ? 14.429 17.958 17.701 1.00 11.79 ? 10 LEU B N 1 ATOM 866 C CA . LEU B 1 10 ? 13.067 18.190 17.302 1.00 11.46 ? 10 LEU B CA 1 ATOM 867 C C . LEU B 1 10 ? 12.110 17.479 18.202 1.00 13.24 ? 10 LEU B C 1 ATOM 868 O O . LEU B 1 10 ? 12.273 16.330 18.487 1.00 15.54 ? 10 LEU B O 1 ATOM 869 C CB . LEU B 1 10 ? 12.893 17.698 15.904 1.00 15.18 ? 10 LEU B CB 1 ATOM 870 C CG . LEU B 1 10 ? 13.632 18.463 14.814 1.00 16.90 ? 10 LEU B CG 1 ATOM 871 C CD1 . LEU B 1 10 ? 13.660 17.698 13.525 1.00 23.06 ? 10 LEU B CD1 1 ATOM 872 C CD2 . LEU B 1 10 ? 12.973 19.930 14.586 1.00 18.90 ? 10 LEU B CD2 1 ATOM 873 N N . VAL B 1 11 ? 11.109 18.190 18.637 1.00 12.06 ? 11 VAL B N 1 ATOM 874 C CA . VAL B 1 11 ? 10.054 17.653 19.463 1.00 13.10 ? 11 VAL B CA 1 ATOM 875 C C . VAL B 1 11 ? 8.702 18.109 18.995 1.00 13.85 ? 11 VAL B C 1 ATOM 876 O O . VAL B 1 11 ? 8.596 19.022 18.162 1.00 14.46 ? 11 VAL B O 1 ATOM 877 C CB . VAL B 1 11 ? 10.228 18.057 20.944 1.00 16.23 ? 11 VAL B CB 1 ATOM 878 C CG1 . VAL B 1 11 ? 11.540 17.546 21.485 1.00 18.98 ? 11 VAL B CG1 1 ATOM 879 C CG2 . VAL B 1 11 ? 10.081 19.562 21.093 1.00 18.48 ? 11 VAL B CG2 1 ATOM 880 N N . THR B 1 12 ? 7.661 17.465 19.473 1.00 14.81 ? 12 THR B N 1 ATOM 881 C CA . THR B 1 12 ? 6.309 17.838 19.125 1.00 16.16 ? 12 THR B CA 1 ATOM 882 C C . THR B 1 12 ? 5.801 18.909 20.042 1.00 15.55 ? 12 THR B C 1 ATOM 883 O O . THR B 1 12 ? 5.855 18.794 21.227 1.00 18.18 ? 12 THR B O 1 ATOM 884 C CB . THR B 1 12 ? 5.378 16.583 19.163 1.00 17.76 ? 12 THR B CB 1 ATOM 885 O OG1 . THR B 1 12 ? 5.901 15.589 18.269 1.00 20.95 ? 12 THR B OG1 1 ATOM 886 C CG2 . THR B 1 12 ? 3.970 16.907 18.603 1.00 20.74 ? 12 THR B CG2 1 ATOM 887 N N . ILE B 1 13 ? 5.216 19.915 19.435 1.00 17.31 ? 13 ILE B N 1 ATOM 888 C CA . ILE B 1 13 ? 4.528 20.982 20.170 1.00 15.98 ? 13 ILE B CA 1 ATOM 889 C C . ILE B 1 13 ? 3.097 21.106 19.723 1.00 18.34 ? 13 ILE B C 1 ATOM 890 O O . ILE B 1 13 ? 2.746 20.644 18.660 1.00 20.02 ? 13 ILE B O 1 ATOM 891 C CB . ILE B 1 13 ? 5.271 22.334 19.947 1.00 16.98 ? 13 ILE B CB 1 ATOM 892 C CG1 . ILE B 1 13 ? 5.179 22.803 18.552 1.00 16.60 ? 13 ILE B CG1 1 ATOM 893 C CG2 . ILE B 1 13 ? 6.716 22.166 20.292 1.00 16.95 ? 13 ILE B CG2 1 ATOM 894 C CD1 . ILE B 1 13 ? 5.575 24.223 18.362 1.00 19.27 ? 13 ILE B CD1 1 ATOM 895 N N . ARG B 1 14 ? 2.282 21.748 20.562 1.00 18.55 ? 14 ARG B N 1 ATOM 896 C CA . ARG B 1 14 ? 0.890 22.087 20.207 1.00 20.16 ? 14 ARG B CA 1 ATOM 897 C C . ARG B 1 14 ? 0.696 23.558 20.381 1.00 14.32 ? 14 ARG B C 1 ATOM 898 O O . ARG B 1 14 ? 0.979 24.120 21.420 1.00 19.12 ? 14 ARG B O 1 ATOM 899 C CB . ARG B 1 14 ? -0.061 21.302 21.031 1.00 23.10 ? 14 ARG B CB 1 ATOM 900 C CG . ARG B 1 14 ? -1.536 21.491 20.625 1.00 27.46 ? 14 ARG B CG 1 ATOM 901 C CD . ARG B 1 14 ? -2.569 20.623 21.489 1.00 29.93 ? 14 ARG B CD 1 ATOM 902 N NE . ARG B 1 14 ? -3.724 21.417 21.858 1.00 33.37 ? 14 ARG B NE 1 ATOM 903 C CZ . ARG B 1 14 ? -4.769 21.431 21.213 1.00 41.32 ? 14 ARG B CZ 1 ATOM 904 N NH1 . ARG B 1 14 ? -4.834 20.749 20.077 1.00 50.56 ? 14 ARG B NH1 1 ATOM 905 N NH2 . ARG B 1 14 ? -5.891 22.096 21.696 1.00 40.22 ? 14 ARG B NH2 1 ATOM 906 N N . ILE B 1 15 ? 0.175 24.179 19.340 1.00 19.64 ? 15 ILE B N 1 ATOM 907 C CA . ILE B 1 15 ? -0.056 25.637 19.395 1.00 19.19 ? 15 ILE B CA 1 ATOM 908 C C . ILE B 1 15 ? -1.175 25.998 18.496 1.00 20.95 ? 15 ILE B C 1 ATOM 909 O O . ILE B 1 15 ? -1.312 25.453 17.417 1.00 27.04 ? 15 ILE B O 1 ATOM 910 C CB . ILE B 1 15 ? 1.307 26.420 19.037 1.00 19.96 ? 15 ILE B CB 1 ATOM 911 C CG1 . ILE B 1 15 ? 1.114 27.923 19.222 1.00 24.87 ? 15 ILE B CG1 1 ATOM 912 C CG2 . ILE B 1 15 ? 1.821 26.012 17.700 1.00 19.04 ? 15 ILE B CG2 1 ATOM 913 C CD1 . ILE B 1 15 ? 0.899 28.597 18.094 1.00 27.07 ? 15 ILE B CD1 1 ATOM 914 N N . GLY B 1 16 ? -2.090 26.882 18.988 1.00 20.74 ? 16 GLY B N 1 ATOM 915 C CA . GLY B 1 16 ? -3.192 27.291 18.219 1.00 22.97 ? 16 GLY B CA 1 ATOM 916 C C . GLY B 1 16 ? -4.059 26.119 17.739 1.00 23.82 ? 16 GLY B C 1 ATOM 917 O O . GLY B 1 16 ? -4.681 26.230 16.696 1.00 28.40 ? 16 GLY B O 1 ATOM 918 N N . GLY B 1 17 ? -4.102 24.987 18.551 1.00 21.83 ? 17 GLY B N 1 ATOM 919 C CA . GLY B 1 17 ? -4.576 23.593 18.116 1.00 22.44 ? 17 GLY B CA 1 ATOM 920 C C . GLY B 1 17 ? -4.111 23.010 16.867 1.00 25.99 ? 17 GLY B C 1 ATOM 921 O O . GLY B 1 17 ? -4.809 22.110 16.302 1.00 29.71 ? 17 GLY B O 1 ATOM 922 N N . GLN B 1 18 ? -2.832 23.264 16.528 1.00 24.80 ? 18 GLN B N 1 ATOM 923 C CA . GLN B 1 18 ? -2.092 22.379 15.603 1.00 24.41 ? 18 GLN B CA 1 ATOM 924 C C . GLN B 1 18 ? -0.876 21.733 16.334 1.00 23.94 ? 18 GLN B C 1 ATOM 925 O O . GLN B 1 18 ? -0.324 22.311 17.244 1.00 24.70 ? 18 GLN B O 1 ATOM 926 C CB . GLN B 1 18 ? -1.464 23.176 14.280 1.00 21.11 ? 18 GLN B CB 1 ATOM 927 C CG . GLN B 1 18 ? -2.397 23.903 13.487 1.00 25.47 ? 18 GLN B CG 1 ATOM 928 C CD . GLN B 1 18 ? -1.772 24.583 12.336 1.00 26.79 ? 18 GLN B CD 1 ATOM 929 O OE1 . GLN B 1 18 ? -1.997 24.157 11.119 1.00 34.37 ? 18 GLN B OE1 1 ATOM 930 N NE2 . GLN B 1 18 ? -0.862 25.547 12.618 1.00 30.78 ? 18 GLN B NE2 1 ATOM 931 N N . LEU B 1 19 ? -0.581 20.491 15.983 1.00 21.74 ? 19 LEU B N 1 ATOM 932 C CA . LEU B 1 19 ? 0.629 19.842 16.456 1.00 20.03 ? 19 LEU B CA 1 ATOM 933 C C . LEU B 1 19 ? 1.677 20.061 15.416 1.00 21.22 ? 19 LEU B C 1 ATOM 934 O O . LEU B 1 19 ? 1.401 20.021 14.256 1.00 25.14 ? 19 LEU B O 1 ATOM 935 C CB . LEU B 1 19 ? 0.407 18.324 16.705 1.00 20.87 ? 19 LEU B CB 1 ATOM 936 C CG . LEU B 1 19 ? -0.395 17.872 17.837 1.00 21.62 ? 19 LEU B CG 1 ATOM 937 C CD1 . LEU B 1 19 ? -0.235 16.385 17.951 1.00 27.22 ? 19 LEU B CD1 1 ATOM 938 C CD2 . LEU B 1 19 ? -0.051 18.486 19.085 1.00 25.61 ? 19 LEU B CD2 1 ATOM 939 N N . LYS B 1 20 ? 2.904 20.394 15.854 1.00 19.57 ? 20 LYS B N 1 ATOM 940 C CA . LYS B 1 20 ? 3.968 20.718 14.943 1.00 19.04 ? 20 LYS B CA 1 ATOM 941 C C . LYS B 1 20 ? 5.324 20.100 15.494 1.00 17.50 ? 20 LYS B C 1 ATOM 942 O O . LYS B 1 20 ? 5.444 19.898 16.614 1.00 19.01 ? 20 LYS B O 1 ATOM 943 C CB . LYS B 1 20 ? 4.194 22.291 14.853 1.00 19.49 ? 20 LYS B CB 1 ATOM 944 C CG . LYS B 1 20 ? 2.958 23.031 14.535 1.00 19.62 ? 20 LYS B CG 1 ATOM 945 C CD . LYS B 1 20 ? 3.129 24.473 14.653 1.00 21.62 ? 20 LYS B CD 1 ATOM 946 C CE . LYS B 1 20 ? 1.970 25.236 14.040 1.00 22.40 ? 20 LYS B CE 1 ATOM 947 N NZ . LYS B 1 20 ? 2.058 25.347 12.538 1.00 23.87 ? 20 LYS B NZ 1 ATOM 948 N N . GLU B 1 21 ? 6.300 19.977 14.626 1.00 17.84 ? 21 GLU B N 1 ATOM 949 C CA . GLU B 1 21 ? 7.724 19.613 15.052 1.00 16.17 ? 21 GLU B CA 1 ATOM 950 C C . GLU B 1 21 ? 8.539 20.875 15.132 1.00 15.54 ? 21 GLU B C 1 ATOM 951 O O . GLU B 1 21 ? 8.535 21.698 14.195 1.00 16.25 ? 21 GLU B O 1 ATOM 952 C CB . GLU B 1 21 ? 8.378 18.644 14.034 1.00 18.44 ? 21 GLU B CB 1 ATOM 953 C CG . GLU B 1 21 ? 7.723 17.274 13.927 1.00 24.39 ? 21 GLU B CG 1 ATOM 954 C CD . GLU B 1 21 ? 7.663 16.559 15.253 1.00 25.99 ? 21 GLU B CD 1 ATOM 955 O OE1 . GLU B 1 21 ? 6.500 16.318 15.777 1.00 28.19 ? 21 GLU B OE1 1 ATOM 956 O OE2 . GLU B 1 21 ? 8.754 16.121 15.764 1.00 30.07 ? 21 GLU B OE2 1 ATOM 957 N N . ALA B 1 22 ? 9.254 21.031 16.208 1.00 13.63 ? 22 ALA B N 1 ATOM 958 C CA . ALA B 1 22 ? 10.031 22.247 16.434 1.00 12.58 ? 22 ALA B CA 1 ATOM 959 C C . ALA B 1 22 ? 11.360 21.897 17.139 1.00 10.83 ? 22 ALA B C 1 ATOM 960 O O . ALA B 1 22 ? 11.439 20.958 17.920 1.00 12.18 ? 22 ALA B O 1 ATOM 961 C CB . ALA B 1 22 ? 9.247 23.191 17.292 1.00 12.98 ? 22 ALA B CB 1 ATOM 962 N N . LEU B 1 23 ? 12.332 22.751 16.910 1.00 11.09 ? 23 LEU B N 1 ATOM 963 C CA . LEU B 1 23 ? 13.662 22.627 17.505 1.00 9.96 ? 23 LEU B CA 1 ATOM 964 C C . LEU B 1 23 ? 13.684 23.189 18.884 1.00 9.75 ? 23 LEU B C 1 ATOM 965 O O . LEU B 1 23 ? 13.306 24.369 19.080 1.00 12.57 ? 23 LEU B O 1 ATOM 966 C CB . LEU B 1 23 ? 14.642 23.393 16.707 1.00 12.52 ? 23 LEU B CB 1 ATOM 967 C CG . LEU B 1 23 ? 15.292 22.940 15.519 1.00 16.52 ? 23 LEU B CG 1 ATOM 968 C CD1 . LEU B 1 23 ? 16.162 24.055 14.930 1.00 15.74 ? 23 LEU B CD1 1 ATOM 969 C CD2 . LEU B 1 23 ? 16.129 21.714 15.762 1.00 16.06 ? 23 LEU B CD2 1 ATOM 970 N N . LEU B 1 24 ? 14.219 22.458 19.838 1.00 9.78 ? 24 LEU B N 1 ATOM 971 C CA . LEU B 1 24 ? 14.536 23.029 21.136 1.00 10.42 ? 24 LEU B CA 1 ATOM 972 C C . LEU B 1 24 ? 15.858 23.780 21.008 1.00 9.89 ? 24 LEU B C 1 ATOM 973 O O . LEU B 1 24 ? 16.891 23.139 20.880 1.00 10.79 ? 24 LEU B O 1 ATOM 974 C CB . LEU B 1 24 ? 14.649 21.957 22.196 1.00 11.60 ? 24 LEU B CB 1 ATOM 975 C CG . LEU B 1 24 ? 13.425 21.106 22.422 1.00 12.65 ? 24 LEU B CG 1 ATOM 976 C CD1 . LEU B 1 24 ? 13.834 19.936 23.434 1.00 16.75 ? 24 LEU B CD1 1 ATOM 977 C CD2 . LEU B 1 24 ? 12.223 21.901 22.935 1.00 17.13 ? 24 LEU B CD2 1 ATOM 978 N N . ASP B 1 25 ? 15.794 25.119 20.987 1.00 9.19 ? 25 ASP B N 1 ATOM 979 C CA . ASP B 1 25 ? 16.906 25.958 20.533 1.00 9.04 ? 25 ASP B CA 1 ATOM 980 C C . ASP B 1 25 ? 17.392 26.917 21.582 1.00 9.18 ? 25 ASP B C 1 ATOM 981 O O . ASP B 1 25 ? 16.856 28.021 21.775 1.00 9.82 ? 25 ASP B O 1 ATOM 982 C CB . ASP B 1 25 ? 16.530 26.693 19.313 1.00 8.66 ? 25 ASP B CB 1 ATOM 983 C CG . ASP B 1 25 ? 17.674 27.300 18.619 1.00 9.06 ? 25 ASP B CG 1 ATOM 984 O OD1 . ASP B 1 25 ? 18.811 27.268 19.209 1.00 9.95 ? 25 ASP B OD1 1 ATOM 985 O OD2 . ASP B 1 25 ? 17.548 27.810 17.484 1.00 10.37 ? 25 ASP B OD2 1 ATOM 986 N N . THR B 1 26 ? 18.468 26.541 22.265 1.00 9.25 ? 26 THR B N 1 ATOM 987 C CA . THR B 1 26 ? 19.064 27.393 23.266 1.00 9.41 ? 26 THR B CA 1 ATOM 988 C C . THR B 1 26 ? 19.709 28.658 22.685 1.00 9.20 ? 26 THR B C 1 ATOM 989 O O . THR B 1 26 ? 19.994 29.582 23.434 1.00 10.59 ? 26 THR B O 1 ATOM 990 C CB . THR B 1 26 ? 20.092 26.630 24.058 1.00 9.31 ? 26 THR B CB 1 ATOM 991 O OG1 . THR B 1 26 ? 21.171 26.194 23.211 1.00 9.58 ? 26 THR B OG1 1 ATOM 992 C CG2 . THR B 1 26 ? 19.509 25.427 24.714 1.00 9.94 ? 26 THR B CG2 1 ATOM 993 N N . GLY B 1 27 ? 19.948 28.682 21.378 1.00 9.31 ? 27 GLY B N 1 ATOM 994 C CA . GLY B 1 27 ? 20.481 29.841 20.709 1.00 10.14 ? 27 GLY B CA 1 ATOM 995 C C . GLY B 1 27 ? 19.470 30.904 20.315 1.00 9.76 ? 27 GLY B C 1 ATOM 996 O O . GLY B 1 27 ? 19.845 31.926 19.780 1.00 11.36 ? 27 GLY B O 1 ATOM 997 N N . ALA B 1 28 ? 18.195 30.611 20.502 1.00 9.54 ? 28 ALA B N 1 ATOM 998 C CA . ALA B 1 28 ? 17.115 31.482 20.082 1.00 10.67 ? 28 ALA B CA 1 ATOM 999 C C . ALA B 1 28 ? 16.526 32.175 21.333 1.00 10.65 ? 28 ALA B C 1 ATOM 1000 O O . ALA B 1 28 ? 16.056 31.518 22.252 1.00 10.66 ? 28 ALA B O 1 ATOM 1001 C CB . ALA B 1 28 ? 16.023 30.684 19.434 1.00 10.57 ? 28 ALA B CB 1 ATOM 1002 N N . ASP B 1 29 ? 16.479 33.509 21.337 1.00 10.60 ? 29 ASP B N 1 ATOM 1003 C CA . ASP B 1 29 ? 15.920 34.212 22.459 1.00 11.21 ? 29 ASP B CA 1 ATOM 1004 C C . ASP B 1 29 ? 14.441 33.954 22.545 1.00 12.25 ? 29 ASP B C 1 ATOM 1005 O O . ASP B 1 29 ? 13.881 33.799 23.633 1.00 13.35 ? 29 ASP B O 1 ATOM 1006 C CB . ASP B 1 29 ? 16.151 35.731 22.292 1.00 13.12 ? 29 ASP B CB 1 ATOM 1007 C CG . ASP B 1 29 ? 17.541 36.137 22.317 1.00 14.78 ? 29 ASP B CG 1 ATOM 1008 O OD1 . ASP B 1 29 ? 18.433 35.462 22.913 1.00 14.23 ? 29 ASP B OD1 1 ATOM 1009 O OD2 . ASP B 1 29 ? 17.799 37.300 21.955 1.00 19.65 ? 29 ASP B OD2 1 ATOM 1010 N N . ASP B 1 30 ? 13.764 33.955 21.402 1.00 12.01 ? 30 ASP B N 1 ATOM 1011 C CA . ASP B 1 30 ? 12.337 33.876 21.321 1.00 12.45 ? 30 ASP B CA 1 ATOM 1012 C C . ASP B 1 30 ? 11.926 32.802 20.337 1.00 10.49 ? 30 ASP B C 1 ATOM 1013 O O . ASP B 1 30 ? 12.525 32.664 19.311 1.00 16.23 ? 30 ASP B O 1 ATOM 1014 C CB . ASP B 1 30 ? 11.662 35.225 20.959 1.00 15.93 ? 30 ASP B CB 1 ATOM 1015 C CG . ASP B 1 30 ? 11.675 36.200 22.098 1.00 20.71 ? 30 ASP B CG 1 ATOM 1016 O OD1 . ASP B 1 30 ? 11.163 35.857 23.248 1.00 23.88 ? 30 ASP B OD1 1 ATOM 1017 O OD2 . ASP B 1 30 ? 12.190 37.229 21.983 1.00 28.67 ? 30 ASP B OD2 1 ATOM 1018 N N . THR B 1 31 ? 10.812 32.211 20.597 1.00 11.55 ? 31 THR B N 1 ATOM 1019 C CA . THR B 1 31 ? 10.194 31.210 19.777 1.00 10.95 ? 31 THR B CA 1 ATOM 1020 C C . THR B 1 31 ? 9.725 31.796 18.437 1.00 10.47 ? 31 THR B C 1 ATOM 1021 O O . THR B 1 31 ? 9.052 32.857 18.417 1.00 11.63 ? 31 THR B O 1 ATOM 1022 C CB . THR B 1 31 ? 8.996 30.650 20.581 1.00 10.86 ? 31 THR B CB 1 ATOM 1023 O OG1 . THR B 1 31 ? 9.532 29.958 21.708 1.00 11.64 ? 31 THR B OG1 1 ATOM 1024 C CG2 . THR B 1 31 ? 8.152 29.702 19.791 1.00 11.82 ? 31 THR B CG2 1 ATOM 1025 N N A VAL B 1 32 ? 9.986 31.087 17.371 0.50 9.67 ? 32 VAL B N 1 ATOM 1026 N N B VAL B 1 32 ? 10.038 31.124 17.363 0.50 9.96 ? 32 VAL B N 1 ATOM 1027 C CA A VAL B 1 32 ? 9.677 31.536 15.998 0.50 10.27 ? 32 VAL B CA 1 ATOM 1028 C CA B VAL B 1 32 ? 9.595 31.576 16.039 0.50 10.37 ? 32 VAL B CA 1 ATOM 1029 C C A VAL B 1 32 ? 9.067 30.330 15.302 0.50 10.69 ? 32 VAL B C 1 ATOM 1030 C C B VAL B 1 32 ? 9.131 30.396 15.213 0.50 11.58 ? 32 VAL B C 1 ATOM 1031 O O A VAL B 1 32 ? 9.653 29.275 15.285 0.50 12.01 ? 32 VAL B O 1 ATOM 1032 O O B VAL B 1 32 ? 9.883 29.415 14.984 0.50 10.76 ? 32 VAL B O 1 ATOM 1033 C CB A VAL B 1 32 ? 10.951 32.007 15.202 0.50 12.58 ? 32 VAL B CB 1 ATOM 1034 C CB B VAL B 1 32 ? 10.613 32.441 15.331 0.50 10.87 ? 32 VAL B CB 1 ATOM 1035 C CG1 A VAL B 1 32 ? 10.531 32.779 13.929 0.50 14.76 ? 32 VAL B CG1 1 ATOM 1036 C CG1 B VAL B 1 32 ? 11.912 31.703 15.139 0.50 9.64 ? 32 VAL B CG1 1 ATOM 1037 C CG2 A VAL B 1 32 ? 11.851 32.854 16.060 0.50 12.18 ? 32 VAL B CG2 1 ATOM 1038 C CG2 B VAL B 1 32 ? 10.039 32.913 13.931 0.50 12.58 ? 32 VAL B CG2 1 ATOM 1039 N N . LEU B 1 33 ? 7.868 30.490 14.756 1.00 11.96 ? 33 LEU B N 1 ATOM 1040 C CA . LEU B 1 33 ? 7.216 29.418 14.074 1.00 11.24 ? 33 LEU B CA 1 ATOM 1041 C C . LEU B 1 33 ? 7.002 29.790 12.642 1.00 11.12 ? 33 LEU B C 1 ATOM 1042 O O . LEU B 1 33 ? 6.810 30.994 12.262 1.00 12.51 ? 33 LEU B O 1 ATOM 1043 C CB . LEU B 1 33 ? 5.857 29.088 14.678 1.00 13.77 ? 33 LEU B CB 1 ATOM 1044 C CG . LEU B 1 33 ? 5.931 28.738 16.215 1.00 16.72 ? 33 LEU B CG 1 ATOM 1045 C CD1 . LEU B 1 33 ? 4.606 28.398 16.743 1.00 18.93 ? 33 LEU B CD1 1 ATOM 1046 C CD2 . LEU B 1 33 ? 6.875 27.635 16.489 1.00 19.01 ? 33 LEU B CD2 1 ATOM 1047 N N . GLU B 1 34 ? 6.947 28.752 11.801 1.00 12.53 ? 34 GLU B N 1 ATOM 1048 C CA . GLU B 1 34 ? 6.660 28.878 10.440 1.00 13.58 ? 34 GLU B CA 1 ATOM 1049 C C . GLU B 1 34 ? 5.322 29.529 10.227 1.00 13.54 ? 34 GLU B C 1 ATOM 1050 O O . GLU B 1 34 ? 4.419 29.460 11.081 1.00 13.84 ? 34 GLU B O 1 ATOM 1051 C CB . GLU B 1 34 ? 6.665 27.499 9.785 1.00 14.53 ? 34 GLU B CB 1 ATOM 1052 C CG . GLU B 1 34 ? 8.080 26.765 9.833 1.00 18.78 ? 34 GLU B CG 1 ATOM 1053 C CD . GLU B 1 34 ? 7.993 25.322 9.455 1.00 20.50 ? 34 GLU B CD 1 ATOM 1054 O OE1 . GLU B 1 34 ? 6.962 24.904 8.970 1.00 28.89 ? 34 GLU B OE1 1 ATOM 1055 O OE2 . GLU B 1 34 ? 9.022 24.587 9.611 1.00 28.63 ? 34 GLU B OE2 1 ATOM 1056 N N . GLU B 1 35 ? 5.186 30.158 9.070 1.00 14.04 ? 35 GLU B N 1 ATOM 1057 C CA . GLU B 1 35 ? 4.008 30.894 8.764 1.00 14.57 ? 35 GLU B CA 1 ATOM 1058 C C . GLU B 1 35 ? 2.736 30.099 9.033 1.00 15.23 ? 35 GLU B C 1 ATOM 1059 O O . GLU B 1 35 ? 2.618 28.985 8.623 1.00 17.36 ? 35 GLU B O 1 ATOM 1060 C CB . GLU B 1 35 ? 4.068 31.332 7.305 1.00 17.17 ? 35 GLU B CB 1 ATOM 1061 C CG . GLU B 1 35 ? 2.870 32.108 6.843 1.00 20.98 ? 35 GLU B CG 1 ATOM 1062 C CD . GLU B 1 35 ? 2.585 33.345 7.670 1.00 22.72 ? 35 GLU B CD 1 ATOM 1063 O OE1 . GLU B 1 35 ? 1.408 33.515 8.064 1.00 28.18 ? 35 GLU B OE1 1 ATOM 1064 O OE2 . GLU B 1 35 ? 3.546 34.159 7.932 1.00 24.58 ? 35 GLU B OE2 1 ATOM 1065 N N . MET B 1 36 ? 1.805 30.723 9.840 1.00 14.73 ? 36 MET B N 1 ATOM 1066 C CA . MET B 1 36 ? 0.527 30.139 10.236 1.00 17.36 ? 36 MET B CA 1 ATOM 1067 C C . MET B 1 36 ? -0.407 31.321 10.552 1.00 19.25 ? 36 MET B C 1 ATOM 1068 O O . MET B 1 36 ? 0.023 32.360 11.007 1.00 18.96 ? 36 MET B O 1 ATOM 1069 C CB . MET B 1 36 ? 0.692 29.236 11.466 1.00 19.82 ? 36 MET B CB 1 ATOM 1070 C CG . MET B 1 36 ? 1.229 29.898 12.577 1.00 19.29 ? 36 MET B CG 1 ATOM 1071 S SD . MET B 1 36 ? 1.356 28.807 14.099 1.00 22.97 ? 36 MET B SD 1 ATOM 1072 C CE . MET B 1 36 ? -0.360 28.226 14.294 1.00 24.95 ? 36 MET B CE 1 ATOM 1073 N N . ASN B 1 37 ? -1.709 31.132 10.332 1.00 20.26 ? 37 ASN B N 1 ATOM 1074 C CA . ASN B 1 37 ? -2.638 32.231 10.517 1.00 21.01 ? 37 ASN B CA 1 ATOM 1075 C C . ASN B 1 37 ? -3.266 32.173 11.886 1.00 21.41 ? 37 ASN B C 1 ATOM 1076 O O . ASN B 1 37 ? -4.454 31.833 12.014 1.00 24.76 ? 37 ASN B O 1 ATOM 1077 C CB . ASN B 1 37 ? -3.729 32.237 9.417 1.00 25.16 ? 37 ASN B CB 1 ATOM 1078 C CG . ASN B 1 37 ? -4.495 33.615 9.318 1.00 28.86 ? 37 ASN B CG 1 ATOM 1079 O OD1 . ASN B 1 37 ? -5.650 33.678 8.768 1.00 41.63 ? 37 ASN B OD1 1 ATOM 1080 N ND2 . ASN B 1 37 ? -3.954 34.630 9.900 1.00 30.12 ? 37 ASN B ND2 1 ATOM 1081 N N . LEU B 1 38 ? -2.522 32.587 12.908 1.00 21.91 ? 38 LEU B N 1 ATOM 1082 C CA . LEU B 1 38 ? -3.034 32.656 14.287 1.00 19.95 ? 38 LEU B CA 1 ATOM 1083 C C . LEU B 1 38 ? -4.029 33.750 14.449 1.00 21.78 ? 38 LEU B C 1 ATOM 1084 O O . LEU B 1 38 ? -3.793 34.868 14.014 1.00 21.95 ? 38 LEU B O 1 ATOM 1085 C CB . LEU B 1 38 ? -1.936 32.923 15.259 1.00 22.74 ? 38 LEU B CB 1 ATOM 1086 C CG . LEU B 1 38 ? -1.069 31.902 15.648 1.00 25.13 ? 38 LEU B CG 1 ATOM 1087 C CD1 . LEU B 1 38 ? 0.047 32.416 16.502 1.00 21.59 ? 38 LEU B CD1 1 ATOM 1088 C CD2 . LEU B 1 38 ? -1.812 30.783 16.428 1.00 24.06 ? 38 LEU B CD2 1 ATOM 1089 N N . PRO B 1 39 ? -4.979 33.534 15.305 1.00 21.55 ? 39 PRO B N 1 ATOM 1090 C CA . PRO B 1 39 ? -5.876 34.619 15.681 1.00 22.44 ? 39 PRO B CA 1 ATOM 1091 C C . PRO B 1 39 ? -5.241 35.554 16.642 1.00 21.52 ? 39 PRO B C 1 ATOM 1092 O O . PRO B 1 39 ? -4.319 35.148 17.343 1.00 23.61 ? 39 PRO B O 1 ATOM 1093 C CB . PRO B 1 39 ? -7.020 33.916 16.322 1.00 25.66 ? 39 PRO B CB 1 ATOM 1094 C CG . PRO B 1 39 ? -6.481 32.552 16.730 1.00 24.43 ? 39 PRO B CG 1 ATOM 1095 C CD . PRO B 1 39 ? -5.407 32.216 15.866 1.00 24.15 ? 39 PRO B CD 1 ATOM 1096 N N . GLY B 1 40 ? -5.745 36.767 16.704 1.00 24.99 ? 40 GLY B N 1 ATOM 1097 C CA . GLY B 1 40 ? -5.375 37.721 17.748 1.00 25.65 ? 40 GLY B CA 1 ATOM 1098 C C . GLY B 1 40 ? -4.521 38.948 17.226 1.00 24.98 ? 40 GLY B C 1 ATOM 1099 O O . GLY B 1 40 ? -4.058 38.973 16.068 1.00 24.97 ? 40 GLY B O 1 ATOM 1100 N N . LYS B 1 41 ? -4.249 39.859 18.112 1.00 22.61 ? 41 LYS B N 1 ATOM 1101 C CA . LYS B 1 41 ? -3.396 41.006 17.797 1.00 22.18 ? 41 LYS B CA 1 ATOM 1102 C C . LYS B 1 41 ? -1.942 40.606 17.690 1.00 19.98 ? 41 LYS B C 1 ATOM 1103 O O . LYS B 1 41 ? -1.494 39.687 18.375 1.00 21.49 ? 41 LYS B O 1 ATOM 1104 C CB . LYS B 1 41 ? -3.527 42.037 18.815 1.00 24.29 ? 41 LYS B CB 1 ATOM 1105 N N . TRP B 1 42 ? -1.191 41.380 16.943 1.00 17.83 ? 42 TRP B N 1 ATOM 1106 C CA . TRP B 1 42 ? 0.227 41.166 16.820 1.00 16.77 ? 42 TRP B CA 1 ATOM 1107 C C . TRP B 1 42 ? 0.923 42.476 16.515 1.00 19.20 ? 42 TRP B C 1 ATOM 1108 O O . TRP B 1 42 ? 0.256 43.504 16.205 1.00 19.32 ? 42 TRP B O 1 ATOM 1109 C CB . TRP B 1 42 ? 0.489 40.155 15.762 1.00 17.79 ? 42 TRP B CB 1 ATOM 1110 C CG . TRP B 1 42 ? -0.066 40.502 14.375 1.00 20.38 ? 42 TRP B CG 1 ATOM 1111 C CD1 . TRP B 1 42 ? -1.329 40.198 13.883 1.00 25.45 ? 42 TRP B CD1 1 ATOM 1112 C CD2 . TRP B 1 42 ? 0.618 41.195 13.312 1.00 21.83 ? 42 TRP B CD2 1 ATOM 1113 N NE1 . TRP B 1 42 ? -1.460 40.670 12.600 1.00 27.98 ? 42 TRP B NE1 1 ATOM 1114 C CE2 . TRP B 1 42 ? -0.312 41.351 12.247 1.00 25.46 ? 42 TRP B CE2 1 ATOM 1115 C CE3 . TRP B 1 42 ? 1.862 41.799 13.189 1.00 20.31 ? 42 TRP B CE3 1 ATOM 1116 C CZ2 . TRP B 1 42 ? 0.025 41.973 11.050 1.00 29.34 ? 42 TRP B CZ2 1 ATOM 1117 C CZ3 . TRP B 1 42 ? 2.172 42.434 12.012 1.00 24.40 ? 42 TRP B CZ3 1 ATOM 1118 C CH2 . TRP B 1 42 ? 1.280 42.439 10.927 1.00 26.01 ? 42 TRP B CH2 1 ATOM 1119 N N . LYS B 1 43 ? 2.250 42.460 16.608 1.00 17.48 ? 43 LYS B N 1 ATOM 1120 C CA . LYS B 1 43 ? 3.093 43.659 16.384 1.00 17.00 ? 43 LYS B CA 1 ATOM 1121 C C . LYS B 1 43 ? 4.218 43.209 15.433 1.00 15.16 ? 43 LYS B C 1 ATOM 1122 O O . LYS B 1 43 ? 4.762 42.138 15.617 1.00 15.41 ? 43 LYS B O 1 ATOM 1123 C CB . LYS B 1 43 ? 3.747 44.098 17.746 1.00 21.14 ? 43 LYS B CB 1 ATOM 1124 N N . PRO B 1 44 ? 4.634 44.042 14.449 1.00 14.87 ? 44 PRO B N 1 ATOM 1125 C CA . PRO B 1 44 ? 5.751 43.669 13.585 1.00 16.08 ? 44 PRO B CA 1 ATOM 1126 C C . PRO B 1 44 ? 7.053 43.707 14.292 1.00 14.07 ? 44 PRO B C 1 ATOM 1127 O O . PRO B 1 44 ? 7.311 44.549 15.161 1.00 15.46 ? 44 PRO B O 1 ATOM 1128 C CB . PRO B 1 44 ? 5.668 44.716 12.424 1.00 18.36 ? 44 PRO B CB 1 ATOM 1129 C CG . PRO B 1 44 ? 4.908 45.753 12.928 1.00 20.62 ? 44 PRO B CG 1 ATOM 1130 C CD . PRO B 1 44 ? 4.013 45.294 14.021 1.00 16.20 ? 44 PRO B CD 1 ATOM 1131 N N . LYS B 1 45 ? 7.976 42.792 13.856 1.00 12.76 ? 45 LYS B N 1 ATOM 1132 C CA . LYS B 1 45 ? 9.294 42.745 14.409 1.00 13.22 ? 45 LYS B CA 1 ATOM 1133 C C . LYS B 1 45 ? 10.238 42.236 13.336 1.00 11.33 ? 45 LYS B C 1 ATOM 1134 O O . LYS B 1 45 ? 9.804 41.550 12.424 1.00 12.84 ? 45 LYS B O 1 ATOM 1135 C CB . LYS B 1 45 ? 9.262 41.746 15.645 1.00 14.85 ? 45 LYS B CB 1 ATOM 1136 C CG . LYS B 1 45 ? 10.453 41.652 16.442 1.00 16.26 ? 45 LYS B CG 1 ATOM 1137 C CD . LYS B 1 45 ? 10.251 40.656 17.625 1.00 18.57 ? 45 LYS B CD 1 ATOM 1138 C CE . LYS B 1 45 ? 11.388 40.350 18.247 1.00 24.01 ? 45 LYS B CE 1 ATOM 1139 N NZ . LYS B 1 45 ? 11.766 41.253 19.087 1.00 31.36 ? 45 LYS B NZ 1 ATOM 1140 N N A MET B 1 46 ? 11.526 42.568 13.486 0.50 10.65 ? 46 MET B N 1 ATOM 1141 N N B MET B 1 46 ? 11.506 42.525 13.476 0.50 10.79 ? 46 MET B N 1 ATOM 1142 C CA A MET B 1 46 ? 12.615 41.969 12.670 0.50 10.47 ? 46 MET B CA 1 ATOM 1143 C CA B MET B 1 46 ? 12.502 41.909 12.624 0.50 10.99 ? 46 MET B CA 1 ATOM 1144 C C A MET B 1 46 ? 13.445 41.164 13.610 0.50 11.30 ? 46 MET B C 1 ATOM 1145 C C B MET B 1 46 ? 13.537 41.236 13.513 0.50 11.55 ? 46 MET B C 1 ATOM 1146 O O A MET B 1 46 ? 13.809 41.643 14.668 0.50 14.12 ? 46 MET B O 1 ATOM 1147 O O B MET B 1 46 ? 13.898 41.764 14.567 0.50 14.14 ? 46 MET B O 1 ATOM 1148 C CB A MET B 1 46 ? 13.466 43.059 12.058 0.50 11.76 ? 46 MET B CB 1 ATOM 1149 C CB B MET B 1 46 ? 13.111 42.949 11.663 0.50 12.91 ? 46 MET B CB 1 ATOM 1150 C CG A MET B 1 46 ? 12.789 43.857 11.007 0.50 13.09 ? 46 MET B CG 1 ATOM 1151 C CG B MET B 1 46 ? 12.029 43.400 10.392 0.50 11.70 ? 46 MET B CG 1 ATOM 1152 S SD A MET B 1 46 ? 12.639 42.926 9.468 0.50 17.21 ? 46 MET B SD 1 ATOM 1153 S SD B MET B 1 46 ? 12.735 44.629 9.414 0.50 13.86 ? 46 MET B SD 1 ATOM 1154 C CE A MET B 1 46 ? 14.151 43.490 8.578 0.50 19.01 ? 46 MET B CE 1 ATOM 1155 C CE B MET B 1 46 ? 14.231 43.876 8.903 0.50 12.74 ? 46 MET B CE 1 ATOM 1156 N N . ILE B 1 47 ? 13.842 39.964 13.186 1.00 10.84 ? 47 ILE B N 1 ATOM 1157 C CA . ILE B 1 47 ? 14.813 39.177 13.940 1.00 11.08 ? 47 ILE B CA 1 ATOM 1158 C C . ILE B 1 47 ? 15.931 38.753 13.009 1.00 10.70 ? 47 ILE B C 1 ATOM 1159 O O . ILE B 1 47 ? 15.724 38.518 11.826 1.00 11.02 ? 47 ILE B O 1 ATOM 1160 C CB . ILE B 1 47 ? 14.181 37.966 14.625 1.00 11.77 ? 47 ILE B CB 1 ATOM 1161 C CG1 . ILE B 1 47 ? 13.549 37.010 13.637 1.00 11.90 ? 47 ILE B CG1 1 ATOM 1162 C CG2 . ILE B 1 47 ? 13.173 38.421 15.662 1.00 13.94 ? 47 ILE B CG2 1 ATOM 1163 C CD1 . ILE B 1 47 ? 13.022 35.724 14.291 1.00 13.69 ? 47 ILE B CD1 1 ATOM 1164 N N . GLY B 1 48 ? 17.120 38.669 13.564 1.00 11.46 ? 48 GLY B N 1 ATOM 1165 C CA . GLY B 1 48 ? 18.320 38.474 12.794 1.00 13.20 ? 48 GLY B CA 1 ATOM 1166 C C . GLY B 1 48 ? 19.102 37.292 13.169 1.00 10.80 ? 48 GLY B C 1 ATOM 1167 O O . GLY B 1 48 ? 19.208 36.916 14.325 1.00 12.91 ? 48 GLY B O 1 ATOM 1168 N N . GLY B 1 49 ? 19.683 36.657 12.171 1.00 10.19 ? 49 GLY B N 1 ATOM 1169 C CA . GLY B 1 49 ? 20.538 35.477 12.381 1.00 11.55 ? 49 GLY B CA 1 ATOM 1170 C C . GLY B 1 49 ? 21.561 35.370 11.272 1.00 10.81 ? 49 GLY B C 1 ATOM 1171 O O . GLY B 1 49 ? 21.815 36.339 10.553 1.00 10.84 ? 49 GLY B O 1 ATOM 1172 N N . ILE B 1 50 ? 22.071 34.177 11.061 1.00 11.10 ? 50 ILE B N 1 ATOM 1173 C CA . ILE B 1 50 ? 22.936 33.957 9.913 1.00 10.38 ? 50 ILE B CA 1 ATOM 1174 C C . ILE B 1 50 ? 22.138 34.215 8.636 1.00 10.65 ? 50 ILE B C 1 ATOM 1175 O O . ILE B 1 50 ? 21.036 33.724 8.470 1.00 11.98 ? 50 ILE B O 1 ATOM 1176 C CB . ILE B 1 50 ? 23.506 32.538 9.991 1.00 10.60 ? 50 ILE B CB 1 ATOM 1177 C CG1 . ILE B 1 50 ? 24.579 32.499 11.107 1.00 12.14 ? 50 ILE B CG1 1 ATOM 1178 C CG2 . ILE B 1 50 ? 24.076 32.097 8.657 1.00 11.67 ? 50 ILE B CG2 1 ATOM 1179 C CD1 . ILE B 1 50 ? 25.054 31.129 11.469 1.00 12.48 ? 50 ILE B CD1 1 ATOM 1180 N N . GLY B 1 51 ? 22.724 35.054 7.768 1.00 11.06 ? 51 GLY B N 1 ATOM 1181 C CA . GLY B 1 51 ? 22.117 35.473 6.544 1.00 11.38 ? 51 GLY B CA 1 ATOM 1182 C C . GLY B 1 51 ? 21.413 36.789 6.607 1.00 12.55 ? 51 GLY B C 1 ATOM 1183 O O . GLY B 1 51 ? 21.164 37.361 5.561 1.00 17.52 ? 51 GLY B O 1 ATOM 1184 N N . GLY B 1 52 ? 21.137 37.318 7.779 1.00 11.23 ? 52 GLY B N 1 ATOM 1185 C CA . GLY B 1 52 ? 20.416 38.577 7.923 1.00 11.90 ? 52 GLY B CA 1 ATOM 1186 C C . GLY B 1 52 ? 19.111 38.420 8.657 1.00 10.49 ? 52 GLY B C 1 ATOM 1187 O O . GLY B 1 52 ? 18.942 37.539 9.473 1.00 11.27 ? 52 GLY B O 1 ATOM 1188 N N . PHE B 1 53 ? 18.185 39.321 8.346 1.00 12.20 ? 53 PHE B N 1 ATOM 1189 C CA . PHE B 1 53 ? 16.957 39.462 9.112 1.00 11.56 ? 53 PHE B CA 1 ATOM 1190 C C . PHE B 1 53 ? 15.774 38.933 8.369 1.00 12.01 ? 53 PHE B C 1 ATOM 1191 O O . PHE B 1 53 ? 15.726 38.936 7.123 1.00 14.24 ? 53 PHE B O 1 ATOM 1192 C CB . PHE B 1 53 ? 16.725 40.951 9.501 1.00 12.89 ? 53 PHE B CB 1 ATOM 1193 C CG . PHE B 1 53 ? 17.579 41.421 10.634 1.00 12.18 ? 53 PHE B CG 1 ATOM 1194 C CD1 . PHE B 1 53 ? 18.942 41.726 10.437 1.00 14.55 ? 53 PHE B CD1 1 ATOM 1195 C CD2 . PHE B 1 53 ? 17.064 41.636 11.845 1.00 12.87 ? 53 PHE B CD2 1 ATOM 1196 C CE1 . PHE B 1 53 ? 19.705 42.160 11.508 1.00 14.95 ? 53 PHE B CE1 1 ATOM 1197 C CE2 . PHE B 1 53 ? 17.868 42.077 12.876 1.00 14.30 ? 53 PHE B CE2 1 ATOM 1198 C CZ . PHE B 1 53 ? 19.203 42.267 12.664 1.00 16.23 ? 53 PHE B CZ 1 ATOM 1199 N N . ILE B 1 54 ? 14.734 38.522 9.114 1.00 11.86 ? 54 ILE B N 1 ATOM 1200 C CA . ILE B 1 54 ? 13.400 38.256 8.561 1.00 12.23 ? 54 ILE B CA 1 ATOM 1201 C C . ILE B 1 54 ? 12.393 39.047 9.341 1.00 10.99 ? 54 ILE B C 1 ATOM 1202 O O . ILE B 1 54 ? 12.606 39.407 10.497 1.00 11.96 ? 54 ILE B O 1 ATOM 1203 C CB . ILE B 1 54 ? 13.024 36.761 8.529 1.00 13.71 ? 54 ILE B CB 1 ATOM 1204 C CG1 . ILE B 1 54 ? 12.995 36.149 9.924 1.00 14.03 ? 54 ILE B CG1 1 ATOM 1205 C CG2 . ILE B 1 54 ? 13.908 36.034 7.589 1.00 15.57 ? 54 ILE B CG2 1 ATOM 1206 C CD1 . ILE B 1 54 ? 12.236 34.848 10.004 1.00 15.87 ? 54 ILE B CD1 1 ATOM 1207 N N . LYS B 1 55 ? 11.280 39.342 8.666 1.00 11.17 ? 55 LYS B N 1 ATOM 1208 C CA . LYS B 1 55 ? 10.174 39.996 9.260 1.00 11.43 ? 55 LYS B CA 1 ATOM 1209 C C . LYS B 1 55 ? 9.198 38.981 9.859 1.00 10.36 ? 55 LYS B C 1 ATOM 1210 O O . LYS B 1 55 ? 8.862 38.018 9.201 1.00 12.33 ? 55 LYS B O 1 ATOM 1211 C CB . LYS B 1 55 ? 9.432 40.791 8.181 1.00 13.42 ? 55 LYS B CB 1 ATOM 1212 C CG . LYS B 1 55 ? 10.264 41.756 7.342 1.00 20.94 ? 55 LYS B CG 1 ATOM 1213 C CD . LYS B 1 55 ? 9.439 42.429 6.150 1.00 24.72 ? 55 LYS B CD 1 ATOM 1214 C CE . LYS B 1 55 ? 10.298 43.532 5.433 1.00 27.31 ? 55 LYS B CE 1 ATOM 1215 N NZ . LYS B 1 55 ? 11.712 43.053 5.257 1.00 36.64 ? 55 LYS B NZ 1 ATOM 1216 N N . VAL B 1 56 ? 8.757 39.233 11.072 1.00 11.07 ? 56 VAL B N 1 ATOM 1217 C CA . VAL B 1 56 ? 7.844 38.344 11.760 1.00 12.25 ? 56 VAL B CA 1 ATOM 1218 C C . VAL B 1 56 ? 6.728 39.131 12.437 1.00 13.12 ? 56 VAL B C 1 ATOM 1219 O O . VAL B 1 56 ? 6.803 40.363 12.608 1.00 13.57 ? 56 VAL B O 1 ATOM 1220 C CB . VAL B 1 56 ? 8.611 37.467 12.831 1.00 11.73 ? 56 VAL B CB 1 ATOM 1221 C CG1 . VAL B 1 56 ? 9.655 36.610 12.170 1.00 13.60 ? 56 VAL B CG1 1 ATOM 1222 C CG2 . VAL B 1 56 ? 9.237 38.330 13.896 1.00 13.51 ? 56 VAL B CG2 1 ATOM 1223 N N . ARG B 1 57 ? 5.696 38.403 12.787 1.00 12.50 ? 57 ARG B N 1 ATOM 1224 C CA . ARG B 1 57 ? 4.560 38.942 13.570 1.00 13.08 ? 57 ARG B CA 1 ATOM 1225 C C . ARG B 1 57 ? 4.664 38.433 14.984 1.00 12.16 ? 57 ARG B C 1 ATOM 1226 O O . ARG B 1 57 ? 4.804 37.195 15.199 1.00 13.63 ? 57 ARG B O 1 ATOM 1227 C CB . ARG B 1 57 ? 3.225 38.471 12.966 1.00 13.94 ? 57 ARG B CB 1 ATOM 1228 C CG . ARG B 1 57 ? 3.043 38.872 11.615 1.00 16.79 ? 57 ARG B CG 1 ATOM 1229 C CD . ARG B 1 57 ? 1.632 38.607 11.044 1.00 21.28 ? 57 ARG B CD 1 ATOM 1230 N NE . ARG B 1 57 ? 1.161 37.191 11.178 1.00 22.37 ? 57 ARG B NE 1 ATOM 1231 C CZ . ARG B 1 57 ? 1.465 36.189 10.335 1.00 21.77 ? 57 ARG B CZ 1 ATOM 1232 N NH1 . ARG B 1 57 ? 2.387 36.360 9.365 1.00 27.38 ? 57 ARG B NH1 1 ATOM 1233 N NH2 . ARG B 1 57 ? 0.865 35.026 10.476 1.00 26.50 ? 57 ARG B NH2 1 ATOM 1234 N N . GLN B 1 58 ? 4.697 39.355 15.955 1.00 13.39 ? 58 GLN B N 1 ATOM 1235 C CA . GLN B 1 58 ? 4.841 39.000 17.350 1.00 13.81 ? 58 GLN B CA 1 ATOM 1236 C C . GLN B 1 58 ? 3.486 38.871 18.028 1.00 13.68 ? 58 GLN B C 1 ATOM 1237 O O . GLN B 1 58 ? 2.746 39.890 18.138 1.00 15.93 ? 58 GLN B O 1 ATOM 1238 C CB . GLN B 1 58 ? 5.690 40.064 18.100 1.00 14.31 ? 58 GLN B CB 1 ATOM 1239 C CG . GLN B 1 58 ? 5.791 39.794 19.548 1.00 17.30 ? 58 GLN B CG 1 ATOM 1240 C CD . GLN B 1 58 ? 6.558 40.800 20.306 1.00 21.37 ? 58 GLN B CD 1 ATOM 1241 O OE1 . GLN B 1 58 ? 7.463 41.445 19.772 1.00 23.86 ? 58 GLN B OE1 1 ATOM 1242 N NE2 . GLN B 1 58 ? 6.225 40.944 21.634 1.00 29.58 ? 58 GLN B NE2 1 ATOM 1243 N N . TYR B 1 59 ? 3.128 37.677 18.463 1.00 14.84 ? 59 TYR B N 1 ATOM 1244 C CA . TYR B 1 59 ? 1.911 37.412 19.242 1.00 15.48 ? 59 TYR B CA 1 ATOM 1245 C C . TYR B 1 59 ? 2.275 37.193 20.712 1.00 18.41 ? 59 TYR B C 1 ATOM 1246 O O . TYR B 1 59 ? 3.236 36.515 21.014 1.00 22.25 ? 59 TYR B O 1 ATOM 1247 C CB . TYR B 1 59 ? 1.206 36.183 18.708 1.00 17.04 ? 59 TYR B CB 1 ATOM 1248 C CG . TYR B 1 59 ? 0.683 36.268 17.298 1.00 16.53 ? 59 TYR B CG 1 ATOM 1249 C CD1 . TYR B 1 59 ? 1.502 36.057 16.219 1.00 18.28 ? 59 TYR B CD1 1 ATOM 1250 C CD2 . TYR B 1 59 ? -0.659 36.587 17.040 1.00 19.02 ? 59 TYR B CD2 1 ATOM 1251 C CE1 . TYR B 1 59 ? 1.067 36.099 15.006 1.00 18.51 ? 59 TYR B CE1 1 ATOM 1252 C CE2 . TYR B 1 59 ? -1.119 36.650 15.765 1.00 22.07 ? 59 TYR B CE2 1 ATOM 1253 C CZ . TYR B 1 59 ? -0.258 36.397 14.736 1.00 24.91 ? 59 TYR B CZ 1 ATOM 1254 O OH . TYR B 1 59 ? -0.661 36.458 13.375 1.00 29.61 ? 59 TYR B OH 1 ATOM 1255 N N . ASP B 1 60 ? 1.455 37.666 21.594 1.00 17.87 ? 60 ASP B N 1 ATOM 1256 C CA . ASP B 1 60 ? 1.731 37.530 22.961 1.00 19.83 ? 60 ASP B CA 1 ATOM 1257 C C . ASP B 1 60 ? 0.758 36.627 23.689 1.00 17.14 ? 60 ASP B C 1 ATOM 1258 O O . ASP B 1 60 ? -0.392 36.374 23.190 1.00 18.65 ? 60 ASP B O 1 ATOM 1259 C CB . ASP B 1 60 ? 1.781 38.819 23.570 1.00 23.44 ? 60 ASP B CB 1 ATOM 1260 C CG . ASP B 1 60 ? 2.976 39.730 22.992 1.00 26.11 ? 60 ASP B CG 1 ATOM 1261 O OD1 . ASP B 1 60 ? 4.110 39.185 22.656 1.00 27.61 ? 60 ASP B OD1 1 ATOM 1262 O OD2 . ASP B 1 60 ? 2.854 40.919 22.869 1.00 31.72 ? 60 ASP B OD2 1 ATOM 1263 N N . GLN B 1 61 ? 1.269 35.955 24.712 1.00 17.98 ? 61 GLN B N 1 ATOM 1264 C CA . GLN B 1 61 ? 0.439 35.145 25.614 1.00 19.30 ? 61 GLN B CA 1 ATOM 1265 C C . GLN B 1 61 ? -0.295 34.047 24.808 1.00 18.65 ? 61 GLN B C 1 ATOM 1266 O O . GLN B 1 61 ? -1.468 33.750 25.031 1.00 20.35 ? 61 GLN B O 1 ATOM 1267 C CB . GLN B 1 61 ? -0.484 36.051 26.455 1.00 22.41 ? 61 GLN B CB 1 ATOM 1268 C CG . GLN B 1 61 ? 0.288 36.873 27.501 1.00 27.29 ? 61 GLN B CG 1 ATOM 1269 C CD . GLN B 1 61 ? 0.981 35.947 28.615 1.00 34.82 ? 61 GLN B CD 1 ATOM 1270 O OE1 . GLN B 1 61 ? 2.207 35.795 28.623 1.00 37.57 ? 61 GLN B OE1 1 ATOM 1271 N NE2 . GLN B 1 61 ? 0.125 35.273 29.500 1.00 33.81 ? 61 GLN B NE2 1 ATOM 1272 N N . ILE B 1 62 ? 0.471 33.333 23.970 1.00 15.71 ? 62 ILE B N 1 ATOM 1273 C CA . ILE B 1 62 ? -0.064 32.232 23.229 1.00 14.75 ? 62 ILE B CA 1 ATOM 1274 C C . ILE B 1 62 ? 0.257 30.949 23.995 1.00 15.32 ? 62 ILE B C 1 ATOM 1275 O O . ILE B 1 62 ? 1.419 30.668 24.255 1.00 14.88 ? 62 ILE B O 1 ATOM 1276 C CB . ILE B 1 62 ? 0.561 32.163 21.805 1.00 15.35 ? 62 ILE B CB 1 ATOM 1277 C CG1 . ILE B 1 62 ? 0.320 33.510 21.039 1.00 16.21 ? 62 ILE B CG1 1 ATOM 1278 C CG2 . ILE B 1 62 ? 0.053 30.959 21.050 1.00 17.95 ? 62 ILE B CG2 1 ATOM 1279 C CD1 . ILE B 1 62 ? -1.134 33.857 20.839 1.00 21.41 ? 62 ILE B CD1 1 ATOM 1280 N N . PRO B 1 63 ? -0.757 30.078 24.249 1.00 15.79 ? 63 PRO B N 1 ATOM 1281 C CA . PRO B 1 63 ? -0.478 28.785 24.834 1.00 15.81 ? 63 PRO B CA 1 ATOM 1282 C C . PRO B 1 63 ? 0.180 27.854 23.840 1.00 17.90 ? 63 PRO B C 1 ATOM 1283 O O . PRO B 1 63 ? -0.332 27.656 22.761 1.00 20.19 ? 63 PRO B O 1 ATOM 1284 C CB . PRO B 1 63 ? -1.858 28.294 25.296 1.00 16.62 ? 63 PRO B CB 1 ATOM 1285 C CG . PRO B 1 63 ? -2.847 29.158 24.687 1.00 21.46 ? 63 PRO B CG 1 ATOM 1286 C CD . PRO B 1 63 ? -2.213 30.354 24.122 1.00 16.28 ? 63 PRO B CD 1 ATOM 1287 N N . VAL B 1 64 ? 1.273 27.233 24.291 1.00 18.73 ? 64 VAL B N 1 ATOM 1288 C CA . VAL B 1 64 ? 2.082 26.260 23.472 1.00 20.00 ? 64 VAL B CA 1 ATOM 1289 C C . VAL B 1 64 ? 2.442 25.064 24.412 1.00 20.52 ? 64 VAL B C 1 ATOM 1290 O O . VAL B 1 64 ? 2.982 25.272 25.472 1.00 25.35 ? 64 VAL B O 1 ATOM 1291 C CB . VAL B 1 64 ? 3.390 26.862 22.972 1.00 21.59 ? 64 VAL B CB 1 ATOM 1292 C CG1 . VAL B 1 64 ? 4.155 25.811 22.022 1.00 21.11 ? 64 VAL B CG1 1 ATOM 1293 C CG2 . VAL B 1 64 ? 3.151 28.103 22.222 1.00 21.40 ? 64 VAL B CG2 1 ATOM 1294 N N A GLU B 1 65 ? 2.089 23.875 24.045 0.50 19.18 ? 65 GLU B N 1 ATOM 1295 N N B GLU B 1 65 ? 2.003 23.810 23.945 0.50 18.67 ? 65 GLU B N 1 ATOM 1296 C CA A GLU B 1 65 ? 2.536 22.729 24.809 0.50 19.38 ? 65 GLU B CA 1 ATOM 1297 C CA B GLU B 1 65 ? 2.279 22.520 24.628 0.50 18.85 ? 65 GLU B CA 1 ATOM 1298 C C A GLU B 1 65 ? 3.643 22.060 24.072 0.50 18.94 ? 65 GLU B C 1 ATOM 1299 C C B GLU B 1 65 ? 3.483 21.853 23.982 0.50 19.15 ? 65 GLU B C 1 ATOM 1300 O O A GLU B 1 65 ? 3.696 22.094 22.897 0.50 19.26 ? 65 GLU B O 1 ATOM 1301 O O B GLU B 1 65 ? 3.447 21.543 22.794 0.50 18.55 ? 65 GLU B O 1 ATOM 1302 C CB A GLU B 1 65 ? 1.381 21.757 25.077 0.50 19.40 ? 65 GLU B CB 1 ATOM 1303 C CB B GLU B 1 65 ? 1.002 21.559 24.537 0.50 19.51 ? 65 GLU B CB 1 ATOM 1304 C CG A GLU B 1 65 ? 1.582 20.823 26.243 0.50 20.44 ? 65 GLU B CG 1 ATOM 1305 C CG B GLU B 1 65 ? -0.283 22.188 25.096 0.50 18.26 ? 65 GLU B CG 1 ATOM 1306 C CD A GLU B 1 65 ? 0.334 19.866 26.468 0.50 25.76 ? 65 GLU B CD 1 ATOM 1307 C CD B GLU B 1 65 ? -0.863 23.316 24.172 0.50 16.66 ? 65 GLU B CD 1 ATOM 1308 O OE1 A GLU B 1 65 ? 0.139 18.890 25.646 0.50 32.72 ? 65 GLU B OE1 1 ATOM 1309 O OE1 B GLU B 1 65 ? -1.206 23.027 22.991 0.50 16.36 ? 65 GLU B OE1 1 ATOM 1310 O OE2 A GLU B 1 65 ? -0.479 20.165 27.338 0.50 30.56 ? 65 GLU B OE2 1 ATOM 1311 O OE2 B GLU B 1 65 ? -0.977 24.486 24.629 0.50 17.64 ? 65 GLU B OE2 1 ATOM 1312 N N . ILE B 1 66 ? 4.571 21.627 24.800 1.00 18.41 ? 66 ILE B N 1 ATOM 1313 C CA . ILE B 1 66 ? 5.835 21.110 24.258 1.00 18.93 ? 66 ILE B CA 1 ATOM 1314 C C . ILE B 1 66 ? 6.100 19.787 24.970 1.00 19.74 ? 66 ILE B C 1 ATOM 1315 O O . ILE B 1 66 ? 6.411 19.753 26.180 1.00 20.51 ? 66 ILE B O 1 ATOM 1316 C CB . ILE B 1 66 ? 6.950 22.062 24.510 1.00 17.44 ? 66 ILE B CB 1 ATOM 1317 C CG1 . ILE B 1 66 ? 6.659 23.423 23.842 1.00 19.85 ? 66 ILE B CG1 1 ATOM 1318 C CG2 . ILE B 1 66 ? 8.303 21.483 24.002 1.00 19.65 ? 66 ILE B CG2 1 ATOM 1319 C CD1 . ILE B 1 66 ? 7.307 24.492 24.460 1.00 23.26 ? 66 ILE B CD1 1 ATOM 1320 N N . CYS B 1 67 ? 6.008 18.742 24.250 1.00 21.88 ? 67 CYS B N 1 ATOM 1321 C CA . CYS B 1 67 ? 6.182 17.375 24.873 1.00 24.28 ? 67 CYS B CA 1 ATOM 1322 C C . CYS B 1 67 ? 5.366 17.172 26.108 1.00 25.79 ? 67 CYS B C 1 ATOM 1323 O O . CYS B 1 67 ? 5.855 16.673 27.101 1.00 27.22 ? 67 CYS B O 1 ATOM 1324 C CB . CYS B 1 67 ? 7.633 17.111 25.199 1.00 24.09 ? 67 CYS B CB 1 ATOM 1325 S SG . CYS B 1 67 ? 8.604 17.099 23.894 1.00 31.16 ? 67 CYS B SG 1 ATOM 1326 N N . GLY B 1 68 ? 4.180 17.713 26.107 1.00 25.90 ? 68 GLY B N 1 ATOM 1327 C CA . GLY B 1 68 ? 3.290 17.572 27.238 1.00 27.05 ? 68 GLY B CA 1 ATOM 1328 C C . GLY B 1 68 ? 3.498 18.534 28.363 1.00 26.45 ? 68 GLY B C 1 ATOM 1329 O O . GLY B 1 68 ? 2.704 18.531 29.315 1.00 33.24 ? 68 GLY B O 1 ATOM 1330 N N . HIS B 1 69 ? 4.375 19.493 28.190 1.00 21.02 ? 69 HIS B N 1 ATOM 1331 C CA . HIS B 1 69 ? 4.559 20.500 29.180 1.00 21.59 ? 69 HIS B CA 1 ATOM 1332 C C . HIS B 1 69 ? 3.892 21.775 28.685 1.00 19.88 ? 69 HIS B C 1 ATOM 1333 O O . HIS B 1 69 ? 4.115 22.197 27.529 1.00 22.83 ? 69 HIS B O 1 ATOM 1334 C CB . HIS B 1 69 ? 6.070 20.777 29.452 1.00 21.94 ? 69 HIS B CB 1 ATOM 1335 C CG . HIS B 1 69 ? 6.802 19.631 30.091 1.00 22.26 ? 69 HIS B CG 1 ATOM 1336 N ND1 . HIS B 1 69 ? 7.445 19.750 31.308 1.00 22.01 ? 69 HIS B ND1 1 ATOM 1337 C CD2 . HIS B 1 69 ? 7.171 18.455 29.592 1.00 23.64 ? 69 HIS B CD2 1 ATOM 1338 C CE1 . HIS B 1 69 ? 7.989 18.572 31.621 1.00 26.97 ? 69 HIS B CE1 1 ATOM 1339 N NE2 . HIS B 1 69 ? 7.787 17.756 30.613 1.00 22.01 ? 69 HIS B NE2 1 ATOM 1340 N N . LYS B 1 70 ? 3.107 22.421 29.529 1.00 17.34 ? 70 LYS B N 1 ATOM 1341 C CA . LYS B 1 70 ? 2.416 23.604 29.142 1.00 17.00 ? 70 LYS B CA 1 ATOM 1342 C C . LYS B 1 70 ? 3.288 24.807 29.246 1.00 17.01 ? 70 LYS B C 1 ATOM 1343 O O . LYS B 1 70 ? 4.014 24.943 30.108 1.00 17.75 ? 70 LYS B O 1 ATOM 1344 C CB . LYS B 1 70 ? 1.237 23.779 30.027 1.00 16.10 ? 70 LYS B CB 1 ATOM 1345 C CG . LYS B 1 70 ? 0.160 22.712 29.840 1.00 16.98 ? 70 LYS B CG 1 ATOM 1346 C CD . LYS B 1 70 ? -1.005 22.918 30.816 1.00 17.86 ? 70 LYS B CD 1 ATOM 1347 C CE . LYS B 1 70 ? -2.078 21.899 30.621 1.00 20.28 ? 70 LYS B CE 1 ATOM 1348 N NZ . LYS B 1 70 ? -1.640 20.530 30.988 1.00 26.13 ? 70 LYS B NZ 1 ATOM 1349 N N . ALA B 1 71 ? 3.130 25.731 28.289 1.00 18.17 ? 71 ALA B N 1 ATOM 1350 C CA . ALA B 1 71 ? 3.816 26.993 28.324 1.00 17.47 ? 71 ALA B CA 1 ATOM 1351 C C . ALA B 1 71 ? 2.837 28.074 27.783 1.00 14.22 ? 71 ALA B C 1 ATOM 1352 O O . ALA B 1 71 ? 1.858 27.725 27.133 1.00 16.13 ? 71 ALA B O 1 ATOM 1353 C CB . ALA B 1 71 ? 5.095 26.925 27.444 1.00 19.26 ? 71 ALA B CB 1 ATOM 1354 N N . ILE B 1 72 ? 3.179 29.298 27.996 1.00 15.20 ? 72 ILE B N 1 ATOM 1355 C CA . ILE B 1 72 ? 2.384 30.403 27.471 1.00 14.64 ? 72 ILE B CA 1 ATOM 1356 C C . ILE B 1 72 ? 3.219 31.617 27.364 1.00 13.60 ? 72 ILE B C 1 ATOM 1357 O O . ILE B 1 72 ? 3.908 32.002 28.282 1.00 15.90 ? 72 ILE B O 1 ATOM 1358 C CB . ILE B 1 72 ? 1.077 30.651 28.311 1.00 15.67 ? 72 ILE B CB 1 ATOM 1359 C CG1 . ILE B 1 72 ? 0.319 31.794 27.716 1.00 16.78 ? 72 ILE B CG1 1 ATOM 1360 C CG2 . ILE B 1 72 ? 1.381 30.863 29.746 1.00 18.77 ? 72 ILE B CG2 1 ATOM 1361 C CD1 . ILE B 1 72 ? -1.007 32.000 28.331 1.00 18.13 ? 72 ILE B CD1 1 ATOM 1362 N N . GLY B 1 73 ? 3.288 32.165 26.187 1.00 14.86 ? 73 GLY B N 1 ATOM 1363 C CA . GLY B 1 73 ? 4.132 33.324 25.987 1.00 15.71 ? 73 GLY B CA 1 ATOM 1364 C C . GLY B 1 73 ? 4.194 33.816 24.562 1.00 13.54 ? 73 GLY B C 1 ATOM 1365 O O . GLY B 1 73 ? 3.365 33.521 23.769 1.00 15.33 ? 73 GLY B O 1 ATOM 1366 N N . THR B 1 74 ? 5.247 34.518 24.277 1.00 15.55 ? 74 THR B N 1 ATOM 1367 C CA . THR B 1 74 ? 5.407 35.125 22.969 1.00 15.05 ? 74 THR B CA 1 ATOM 1368 C C . THR B 1 74 ? 5.758 34.136 21.922 1.00 13.14 ? 74 THR B C 1 ATOM 1369 O O . THR B 1 74 ? 6.640 33.290 22.110 1.00 14.41 ? 74 THR B O 1 ATOM 1370 C CB . THR B 1 74 ? 6.474 36.220 23.037 1.00 17.25 ? 74 THR B CB 1 ATOM 1371 O OG1 . THR B 1 74 ? 6.019 37.276 23.883 1.00 21.90 ? 74 THR B OG1 1 ATOM 1372 C CG2 . THR B 1 74 ? 6.756 36.909 21.628 1.00 20.88 ? 74 THR B CG2 1 ATOM 1373 N N . VAL B 1 75 ? 5.102 34.253 20.773 1.00 13.79 ? 75 VAL B N 1 ATOM 1374 C CA . VAL B 1 75 ? 5.382 33.457 19.636 1.00 13.36 ? 75 VAL B CA 1 ATOM 1375 C C . VAL B 1 75 ? 5.531 34.384 18.431 1.00 13.07 ? 75 VAL B C 1 ATOM 1376 O O . VAL B 1 75 ? 4.672 35.251 18.206 1.00 15.35 ? 75 VAL B O 1 ATOM 1377 C CB . VAL B 1 75 ? 4.250 32.408 19.366 1.00 17.14 ? 75 VAL B CB 1 ATOM 1378 C CG1 . VAL B 1 75 ? 4.410 31.732 18.096 1.00 19.65 ? 75 VAL B CG1 1 ATOM 1379 C CG2 . VAL B 1 75 ? 4.189 31.381 20.486 1.00 16.16 ? 75 VAL B CG2 1 ATOM 1380 N N . LEU B 1 76 ? 6.645 34.278 17.764 1.00 11.62 ? 76 LEU B N 1 ATOM 1381 C CA . LEU B 1 76 ? 6.872 35.022 16.525 1.00 11.76 ? 76 LEU B CA 1 ATOM 1382 C C . LEU B 1 76 ? 6.490 34.153 15.367 1.00 13.28 ? 76 LEU B C 1 ATOM 1383 O O . LEU B 1 76 ? 6.704 32.905 15.449 1.00 16.04 ? 76 LEU B O 1 ATOM 1384 C CB . LEU B 1 76 ? 8.343 35.439 16.439 1.00 11.19 ? 76 LEU B CB 1 ATOM 1385 C CG . LEU B 1 76 ? 8.894 36.181 17.689 1.00 11.60 ? 76 LEU B CG 1 ATOM 1386 C CD1 . LEU B 1 76 ? 10.385 36.463 17.491 1.00 11.91 ? 76 LEU B CD1 1 ATOM 1387 C CD2 . LEU B 1 76 ? 8.142 37.409 17.977 1.00 12.22 ? 76 LEU B CD2 1 ATOM 1388 N N . VAL B 1 77 ? 5.874 34.716 14.342 1.00 11.99 ? 77 VAL B N 1 ATOM 1389 C CA . VAL B 1 77 ? 5.465 33.952 13.192 1.00 11.32 ? 77 VAL B CA 1 ATOM 1390 C C . VAL B 1 77 ? 5.982 34.613 11.937 1.00 12.45 ? 77 VAL B C 1 ATOM 1391 O O . VAL B 1 77 ? 5.785 35.814 11.728 1.00 12.71 ? 77 VAL B O 1 ATOM 1392 C CB . VAL B 1 77 ? 3.874 33.835 13.112 1.00 13.96 ? 77 VAL B CB 1 ATOM 1393 C CG1 . VAL B 1 77 ? 3.486 33.081 11.873 1.00 14.29 ? 77 VAL B CG1 1 ATOM 1394 C CG2 . VAL B 1 77 ? 3.351 33.147 14.348 1.00 13.90 ? 77 VAL B CG2 1 ATOM 1395 N N . GLY B 1 78 ? 6.629 33.837 11.086 1.00 11.83 ? 78 GLY B N 1 ATOM 1396 C CA . GLY B 1 78 ? 7.126 34.368 9.834 1.00 12.40 ? 78 GLY B CA 1 ATOM 1397 C C . GLY B 1 78 ? 7.859 33.346 9.076 1.00 12.37 ? 78 GLY B C 1 ATOM 1398 O O . GLY B 1 78 ? 7.770 32.138 9.404 1.00 13.09 ? 78 GLY B O 1 ATOM 1399 N N . PRO B 1 79 ? 8.585 33.749 8.054 1.00 12.67 ? 79 PRO B N 1 ATOM 1400 C CA . PRO B 1 79 ? 9.089 32.809 7.052 1.00 12.58 ? 79 PRO B CA 1 ATOM 1401 C C . PRO B 1 79 ? 10.408 32.208 7.529 1.00 12.83 ? 79 PRO B C 1 ATOM 1402 O O . PRO B 1 79 ? 11.400 32.231 6.795 1.00 14.93 ? 79 PRO B O 1 ATOM 1403 C CB . PRO B 1 79 ? 9.232 33.690 5.770 1.00 14.43 ? 79 PRO B CB 1 ATOM 1404 C CG . PRO B 1 79 ? 9.540 35.090 6.346 1.00 13.68 ? 79 PRO B CG 1 ATOM 1405 C CD . PRO B 1 79 ? 8.711 35.187 7.588 1.00 14.05 ? 79 PRO B CD 1 ATOM 1406 N N . THR B 1 80 ? 10.398 31.573 8.699 1.00 13.07 ? 80 THR B N 1 ATOM 1407 C CA . THR B 1 80 ? 11.514 30.801 9.145 1.00 12.42 ? 80 THR B CA 1 ATOM 1408 C C . THR B 1 80 ? 11.468 29.475 8.428 1.00 13.63 ? 80 THR B C 1 ATOM 1409 O O . THR B 1 80 ? 10.434 28.892 8.229 1.00 15.02 ? 80 THR B O 1 ATOM 1410 C CB . THR B 1 80 ? 11.483 30.622 10.657 1.00 12.39 ? 80 THR B CB 1 ATOM 1411 O OG1 . THR B 1 80 ? 12.580 29.738 11.040 1.00 13.35 ? 80 THR B OG1 1 ATOM 1412 C CG2 . THR B 1 80 ? 10.198 30.032 11.164 1.00 12.94 ? 80 THR B CG2 1 ATOM 1413 N N . PRO B 1 81 ? 12.647 28.897 8.141 1.00 15.73 ? 81 PRO B N 1 ATOM 1414 C CA . PRO B 1 81 ? 12.663 27.593 7.545 1.00 16.83 ? 81 PRO B CA 1 ATOM 1415 C C . PRO B 1 81 ? 12.360 26.420 8.501 1.00 17.68 ? 81 PRO B C 1 ATOM 1416 O O . PRO B 1 81 ? 12.108 25.302 8.037 1.00 19.76 ? 81 PRO B O 1 ATOM 1417 C CB . PRO B 1 81 ? 14.067 27.457 7.000 1.00 17.95 ? 81 PRO B CB 1 ATOM 1418 C CG . PRO B 1 81 ? 14.882 28.338 7.692 1.00 20.48 ? 81 PRO B CG 1 ATOM 1419 C CD . PRO B 1 81 ? 13.949 29.488 8.173 1.00 16.07 ? 81 PRO B CD 1 ATOM 1420 N N A VAL B 1 82 ? 12.402 26.670 9.785 0.50 15.90 ? 82 VAL B N 1 ATOM 1421 N N B VAL B 1 82 ? 12.388 26.681 9.783 0.50 15.81 ? 82 VAL B N 1 ATOM 1422 C CA A VAL B 1 82 ? 12.115 25.636 10.800 0.50 15.75 ? 82 VAL B CA 1 ATOM 1423 C CA B VAL B 1 82 ? 12.203 25.650 10.810 0.50 15.48 ? 82 VAL B CA 1 ATOM 1424 C C A VAL B 1 82 ? 11.376 26.263 11.944 0.50 12.80 ? 82 VAL B C 1 ATOM 1425 C C B VAL B 1 82 ? 11.410 26.271 11.959 0.50 13.04 ? 82 VAL B C 1 ATOM 1426 O O A VAL B 1 82 ? 11.625 27.433 12.292 0.50 14.53 ? 82 VAL B O 1 ATOM 1427 O O B VAL B 1 82 ? 11.630 27.439 12.303 0.50 14.55 ? 82 VAL B O 1 ATOM 1428 C CB A VAL B 1 82 ? 13.410 24.982 11.312 0.50 15.71 ? 82 VAL B CB 1 ATOM 1429 C CB B VAL B 1 82 ? 13.597 25.119 11.328 0.50 15.79 ? 82 VAL B CB 1 ATOM 1430 C CG1 A VAL B 1 82 ? 14.046 24.150 10.247 0.50 19.47 ? 82 VAL B CG1 1 ATOM 1431 C CG1 B VAL B 1 82 ? 13.409 24.045 12.348 0.50 15.59 ? 82 VAL B CG1 1 ATOM 1432 C CG2 A VAL B 1 82 ? 14.360 26.018 11.802 0.50 15.45 ? 82 VAL B CG2 1 ATOM 1433 C CG2 B VAL B 1 82 ? 14.444 24.615 10.180 0.50 17.10 ? 82 VAL B CG2 1 ATOM 1434 N N . ASN B 1 83 ? 10.552 25.493 12.623 1.00 13.45 ? 83 ASN B N 1 ATOM 1435 C CA . ASN B 1 83 ? 9.913 25.948 13.859 1.00 13.03 ? 83 ASN B CA 1 ATOM 1436 C C . ASN B 1 83 ? 10.962 25.876 14.980 1.00 11.00 ? 83 ASN B C 1 ATOM 1437 O O . ASN B 1 83 ? 11.658 24.863 15.113 1.00 12.32 ? 83 ASN B O 1 ATOM 1438 C CB . ASN B 1 83 ? 8.729 25.043 14.268 1.00 14.23 ? 83 ASN B CB 1 ATOM 1439 C CG . ASN B 1 83 ? 7.555 25.068 13.300 1.00 14.00 ? 83 ASN B CG 1 ATOM 1440 O OD1 . ASN B 1 83 ? 7.032 26.125 12.951 1.00 15.78 ? 83 ASN B OD1 1 ATOM 1441 N ND2 . ASN B 1 83 ? 7.094 23.906 12.930 1.00 17.67 ? 83 ASN B ND2 1 ATOM 1442 N N . ILE B 1 84 ? 11.069 26.933 15.716 1.00 10.55 ? 84 ILE B N 1 ATOM 1443 C CA . ILE B 1 84 ? 12.066 27.097 16.740 1.00 10.30 ? 84 ILE B CA 1 ATOM 1444 C C . ILE B 1 84 ? 11.422 27.415 18.089 1.00 10.72 ? 84 ILE B C 1 ATOM 1445 O O . ILE B 1 84 ? 10.715 28.444 18.205 1.00 11.44 ? 84 ILE B O 1 ATOM 1446 C CB . ILE B 1 84 ? 13.018 28.257 16.333 1.00 10.72 ? 84 ILE B CB 1 ATOM 1447 C CG1 . ILE B 1 84 ? 13.836 27.841 15.107 1.00 12.61 ? 84 ILE B CG1 1 ATOM 1448 C CG2 . ILE B 1 84 ? 13.962 28.701 17.485 1.00 12.47 ? 84 ILE B CG2 1 ATOM 1449 C CD1 . ILE B 1 84 ? 14.544 28.997 14.424 1.00 13.63 ? 84 ILE B CD1 1 ATOM 1450 N N . ILE B 1 85 ? 11.675 26.581 19.108 1.00 10.21 ? 85 ILE B N 1 ATOM 1451 C CA . ILE B 1 85 ? 11.297 26.930 20.476 1.00 10.72 ? 85 ILE B CA 1 ATOM 1452 C C . ILE B 1 85 ? 12.493 27.592 21.121 1.00 9.85 ? 85 ILE B C 1 ATOM 1453 O O . ILE B 1 85 ? 13.560 26.972 21.266 1.00 10.94 ? 85 ILE B O 1 ATOM 1454 C CB . ILE B 1 85 ? 10.880 25.654 21.304 1.00 12.09 ? 85 ILE B CB 1 ATOM 1455 C CG1 . ILE B 1 85 ? 9.754 24.932 20.582 1.00 15.23 ? 85 ILE B CG1 1 ATOM 1456 C CG2 . ILE B 1 85 ? 10.524 26.063 22.665 1.00 12.69 ? 85 ILE B CG2 1 ATOM 1457 C CD1 . ILE B 1 85 ? 8.467 25.766 20.430 1.00 18.65 ? 85 ILE B CD1 1 ATOM 1458 N N . GLY B 1 86 ? 12.333 28.857 21.483 1.00 10.06 ? 86 GLY B N 1 ATOM 1459 C CA . GLY B 1 86 ? 13.383 29.610 22.055 1.00 9.99 ? 86 GLY B CA 1 ATOM 1460 C C . GLY B 1 86 ? 13.328 29.669 23.553 1.00 9.83 ? 86 GLY B C 1 ATOM 1461 O O . GLY B 1 86 ? 12.439 29.093 24.212 1.00 11.00 ? 86 GLY B O 1 ATOM 1462 N N . ARG B 1 87 ? 14.278 30.351 24.130 1.00 10.61 ? 87 ARG B N 1 ATOM 1463 C CA . ARG B 1 87 ? 14.458 30.370 25.564 1.00 10.61 ? 87 ARG B CA 1 ATOM 1464 C C . ARG B 1 87 ? 13.252 30.891 26.323 1.00 12.37 ? 87 ARG B C 1 ATOM 1465 O O . ARG B 1 87 ? 12.985 30.426 27.462 1.00 13.84 ? 87 ARG B O 1 ATOM 1466 C CB . ARG B 1 87 ? 15.676 31.153 25.942 1.00 10.62 ? 87 ARG B CB 1 ATOM 1467 C CG . ARG B 1 87 ? 16.983 30.575 25.492 1.00 11.63 ? 87 ARG B CG 1 ATOM 1468 C CD . ARG B 1 87 ? 18.210 31.314 26.036 1.00 12.31 ? 87 ARG B CD 1 ATOM 1469 N NE . ARG B 1 87 ? 18.308 32.667 25.573 1.00 12.98 ? 87 ARG B NE 1 ATOM 1470 C CZ . ARG B 1 87 ? 17.923 33.750 26.266 1.00 14.06 ? 87 ARG B CZ 1 ATOM 1471 N NH1 . ARG B 1 87 ? 17.482 33.674 27.521 1.00 14.54 ? 87 ARG B NH1 1 ATOM 1472 N NH2 . ARG B 1 87 ? 17.988 34.931 25.701 1.00 15.22 ? 87 ARG B NH2 1 ATOM 1473 N N . ASN B 1 88 ? 12.454 31.772 25.714 1.00 11.17 ? 88 ASN B N 1 ATOM 1474 C CA . ASN B 1 88 ? 11.272 32.266 26.405 1.00 12.83 ? 88 ASN B CA 1 ATOM 1475 C C . ASN B 1 88 ? 10.330 31.186 26.827 1.00 13.19 ? 88 ASN B C 1 ATOM 1476 O O . ASN B 1 88 ? 9.654 31.352 27.847 1.00 15.57 ? 88 ASN B O 1 ATOM 1477 C CB . ASN B 1 88 ? 10.568 33.349 25.527 1.00 12.79 ? 88 ASN B CB 1 ATOM 1478 C CG . ASN B 1 88 ? 9.803 32.782 24.387 1.00 13.49 ? 88 ASN B CG 1 ATOM 1479 O OD1 . ASN B 1 88 ? 10.351 32.034 23.533 1.00 12.59 ? 88 ASN B OD1 1 ATOM 1480 N ND2 . ASN B 1 88 ? 8.531 33.181 24.274 1.00 13.57 ? 88 ASN B ND2 1 ATOM 1481 N N . LEU B 1 89 ? 10.210 30.103 26.056 1.00 13.00 ? 89 LEU B N 1 ATOM 1482 C CA . LEU B 1 89 ? 9.413 28.958 26.411 1.00 13.92 ? 89 LEU B CA 1 ATOM 1483 C C . LEU B 1 89 ? 10.193 27.791 26.992 1.00 13.78 ? 89 LEU B C 1 ATOM 1484 O O . LEU B 1 89 ? 9.644 27.042 27.818 1.00 15.18 ? 89 LEU B O 1 ATOM 1485 C CB . LEU B 1 89 ? 8.590 28.506 25.270 1.00 13.59 ? 89 LEU B CB 1 ATOM 1486 C CG . LEU B 1 89 ? 7.658 29.568 24.600 1.00 13.46 ? 89 LEU B CG 1 ATOM 1487 C CD1 . LEU B 1 89 ? 6.853 28.923 23.541 1.00 15.36 ? 89 LEU B CD1 1 ATOM 1488 C CD2 . LEU B 1 89 ? 6.752 30.269 25.656 1.00 15.01 ? 89 LEU B CD2 1 ATOM 1489 N N . LEU B 1 90 ? 11.475 27.643 26.634 1.00 12.29 ? 90 LEU B N 1 ATOM 1490 C CA . LEU B 1 90 ? 12.274 26.603 27.228 1.00 12.48 ? 90 LEU B CA 1 ATOM 1491 C C . LEU B 1 90 ? 12.338 26.726 28.715 1.00 13.48 ? 90 LEU B C 1 ATOM 1492 O O . LEU B 1 90 ? 12.306 25.707 29.410 1.00 16.04 ? 90 LEU B O 1 ATOM 1493 C CB . LEU B 1 90 ? 13.692 26.573 26.629 1.00 11.51 ? 90 LEU B CB 1 ATOM 1494 C CG . LEU B 1 90 ? 13.788 26.238 25.125 1.00 11.34 ? 90 LEU B CG 1 ATOM 1495 C CD1 . LEU B 1 90 ? 15.226 26.468 24.633 1.00 11.34 ? 90 LEU B CD1 1 ATOM 1496 C CD2 . LEU B 1 90 ? 13.358 24.827 24.881 1.00 12.38 ? 90 LEU B CD2 1 ATOM 1497 N N . THR B 1 91 ? 12.497 27.923 29.225 1.00 14.65 ? 91 THR B N 1 ATOM 1498 C CA . THR B 1 91 ? 12.514 28.086 30.712 1.00 16.50 ? 91 THR B CA 1 ATOM 1499 C C . THR B 1 91 ? 11.186 27.602 31.324 1.00 17.17 ? 91 THR B C 1 ATOM 1500 O O . THR B 1 91 ? 11.203 27.023 32.450 1.00 18.29 ? 91 THR B O 1 ATOM 1501 C CB . THR B 1 91 ? 12.764 29.538 31.103 1.00 18.89 ? 91 THR B CB 1 ATOM 1502 O OG1 . THR B 1 91 ? 11.819 30.395 30.494 1.00 19.93 ? 91 THR B OG1 1 ATOM 1503 C CG2 . THR B 1 91 ? 14.145 30.047 30.670 1.00 18.42 ? 91 THR B CG2 1 ATOM 1504 N N . GLN B 1 92 ? 10.071 27.832 30.653 1.00 16.73 ? 92 GLN B N 1 ATOM 1505 C CA . GLN B 1 92 ? 8.791 27.545 31.232 1.00 18.14 ? 92 GLN B CA 1 ATOM 1506 C C . GLN B 1 92 ? 8.529 26.039 31.369 1.00 19.54 ? 92 GLN B C 1 ATOM 1507 O O . GLN B 1 92 ? 7.802 25.598 32.277 1.00 21.58 ? 92 GLN B O 1 ATOM 1508 C CB . GLN B 1 92 ? 7.732 28.144 30.405 1.00 17.22 ? 92 GLN B CB 1 ATOM 1509 C CG . GLN B 1 92 ? 7.712 29.654 30.394 1.00 17.95 ? 92 GLN B CG 1 ATOM 1510 C CD . GLN B 1 92 ? 6.454 30.223 29.783 1.00 17.33 ? 92 GLN B CD 1 ATOM 1511 O OE1 . GLN B 1 92 ? 5.679 29.511 29.362 1.00 23.32 ? 92 GLN B OE1 1 ATOM 1512 N NE2 . GLN B 1 92 ? 6.483 31.502 29.461 1.00 24.09 ? 92 GLN B NE2 1 ATOM 1513 N N . ILE B 1 93 ? 9.182 25.254 30.533 1.00 19.08 ? 93 ILE B N 1 ATOM 1514 C CA . ILE B 1 93 ? 9.050 23.771 30.601 1.00 20.74 ? 93 ILE B CA 1 ATOM 1515 C C . ILE B 1 93 ? 10.219 23.103 31.326 1.00 20.47 ? 93 ILE B C 1 ATOM 1516 O O . ILE B 1 93 ? 10.264 21.866 31.441 1.00 24.52 ? 93 ILE B O 1 ATOM 1517 C CB . ILE B 1 93 ? 8.900 23.129 29.231 1.00 19.73 ? 93 ILE B CB 1 ATOM 1518 C CG1 . ILE B 1 93 ? 10.196 23.290 28.417 1.00 19.59 ? 93 ILE B CG1 1 ATOM 1519 C CG2 . ILE B 1 93 ? 7.757 23.755 28.458 1.00 20.63 ? 93 ILE B CG2 1 ATOM 1520 C CD1 . ILE B 1 93 ? 10.176 22.541 27.111 1.00 21.14 ? 93 ILE B CD1 1 ATOM 1521 N N . GLY B 1 94 ? 11.050 23.876 31.922 1.00 19.19 ? 94 GLY B N 1 ATOM 1522 C CA . GLY B 1 94 ? 12.074 23.324 32.808 1.00 21.76 ? 94 GLY B CA 1 ATOM 1523 C C . GLY B 1 94 ? 13.375 22.893 32.148 1.00 19.87 ? 94 GLY B C 1 ATOM 1524 O O . GLY B 1 94 ? 14.147 22.175 32.749 1.00 21.90 ? 94 GLY B O 1 ATOM 1525 N N . CYS B 1 95 ? 13.631 23.370 30.943 1.00 18.57 ? 95 CYS B N 1 ATOM 1526 C CA . CYS B 1 95 ? 14.751 22.865 30.121 1.00 17.40 ? 95 CYS B CA 1 ATOM 1527 C C . CYS B 1 95 ? 16.098 23.520 30.542 1.00 16.89 ? 95 CYS B C 1 ATOM 1528 O O . CYS B 1 95 ? 16.240 24.742 30.594 1.00 20.06 ? 95 CYS B O 1 ATOM 1529 C CB . CYS B 1 95 ? 14.445 23.138 28.633 1.00 17.32 ? 95 CYS B CB 1 ATOM 1530 S SG . CYS B 1 95 ? 15.519 22.343 27.529 1.00 18.62 ? 95 CYS B SG 1 ATOM 1531 N N . THR B 1 96 ? 17.141 22.650 30.687 1.00 16.03 ? 96 THR B N 1 ATOM 1532 C CA . THR B 1 96 ? 18.489 23.082 30.938 1.00 16.44 ? 96 THR B CA 1 ATOM 1533 C C . THR B 1 96 ? 19.433 22.409 29.949 1.00 13.17 ? 96 THR B C 1 ATOM 1534 O O . THR B 1 96 ? 19.087 21.390 29.353 1.00 14.87 ? 96 THR B O 1 ATOM 1535 C CB . THR B 1 96 ? 18.970 22.705 32.364 1.00 18.50 ? 96 THR B CB 1 ATOM 1536 O OG1 . THR B 1 96 ? 18.750 21.317 32.595 1.00 18.58 ? 96 THR B OG1 1 ATOM 1537 C CG2 . THR B 1 96 ? 18.209 23.472 33.445 1.00 21.13 ? 96 THR B CG2 1 ATOM 1538 N N . LEU B 1 97 ? 20.609 22.972 29.837 1.00 14.65 ? 97 LEU B N 1 ATOM 1539 C CA . LEU B 1 97 ? 21.738 22.344 29.161 1.00 13.67 ? 97 LEU B CA 1 ATOM 1540 C C . LEU B 1 97 ? 22.591 21.705 30.215 1.00 14.83 ? 97 LEU B C 1 ATOM 1541 O O . LEU B 1 97 ? 22.842 22.322 31.254 1.00 17.70 ? 97 LEU B O 1 ATOM 1542 C CB . LEU B 1 97 ? 22.591 23.388 28.477 1.00 16.03 ? 97 LEU B CB 1 ATOM 1543 C CG . LEU B 1 97 ? 22.060 23.965 27.249 1.00 16.05 ? 97 LEU B CG 1 ATOM 1544 C CD1 . LEU B 1 97 ? 22.789 25.296 26.813 1.00 19.24 ? 97 LEU B CD1 1 ATOM 1545 C CD2 . LEU B 1 97 ? 22.135 22.934 26.122 1.00 17.64 ? 97 LEU B CD2 1 ATOM 1546 N N . ASN B 1 98 ? 23.163 20.574 29.936 1.00 15.03 ? 98 ASN B N 1 ATOM 1547 C CA . ASN B 1 98 ? 23.929 19.848 30.932 1.00 16.84 ? 98 ASN B CA 1 ATOM 1548 C C . ASN B 1 98 ? 25.108 19.170 30.258 1.00 16.26 ? 98 ASN B C 1 ATOM 1549 O O . ASN B 1 98 ? 24.949 18.437 29.320 1.00 17.04 ? 98 ASN B O 1 ATOM 1550 C CB . ASN B 1 98 ? 23.076 18.787 31.618 1.00 16.41 ? 98 ASN B CB 1 ATOM 1551 C CG . ASN B 1 98 ? 21.897 19.359 32.314 1.00 17.32 ? 98 ASN B CG 1 ATOM 1552 O OD1 . ASN B 1 98 ? 20.861 19.696 31.696 1.00 21.19 ? 98 ASN B OD1 1 ATOM 1553 N ND2 . ASN B 1 98 ? 21.968 19.398 33.597 1.00 21.01 ? 98 ASN B ND2 1 ATOM 1554 N N . PHE B 1 99 ? 26.308 19.340 30.868 1.00 19.05 ? 99 PHE B N 1 ATOM 1555 C CA . PHE B 1 99 ? 27.477 18.594 30.495 1.00 19.26 ? 99 PHE B CA 1 ATOM 1556 C C . PHE B 1 99 ? 28.480 18.540 31.605 1.00 23.60 ? 99 PHE B C 1 ATOM 1557 O O . PHE B 1 99 ? 29.553 17.923 31.408 1.00 26.36 ? 99 PHE B O 1 ATOM 1558 C CB . PHE B 1 99 ? 28.125 19.197 29.195 1.00 18.95 ? 99 PHE B CB 1 ATOM 1559 C CG . PHE B 1 99 ? 28.559 20.660 29.319 1.00 20.10 ? 99 PHE B CG 1 ATOM 1560 C CD1 . PHE B 1 99 ? 27.689 21.660 29.066 1.00 19.53 ? 99 PHE B CD1 1 ATOM 1561 C CD2 . PHE B 1 99 ? 29.904 20.980 29.389 1.00 22.05 ? 99 PHE B CD2 1 ATOM 1562 C CE1 . PHE B 1 99 ? 28.111 22.973 29.105 1.00 21.02 ? 99 PHE B CE1 1 ATOM 1563 C CE2 . PHE B 1 99 ? 30.313 22.255 29.420 1.00 22.95 ? 99 PHE B CE2 1 ATOM 1564 C CZ . PHE B 1 99 ? 29.422 23.262 29.175 1.00 23.61 ? 99 PHE B CZ 1 ATOM 1565 O OXT . PHE B 1 99 ? 28.224 19.068 32.704 1.00 24.03 ? 99 PHE B OXT 1 HETATM 1566 P P . PO4 C 2 . ? 21.885 38.055 28.472 1.00 48.18 ? 502 PO4 A P 1 HETATM 1567 O O1 . PO4 C 2 . ? 20.858 37.017 28.170 1.00 29.71 ? 502 PO4 A O1 1 HETATM 1568 O O2 . PO4 C 2 . ? 22.214 37.997 29.948 1.00 51.15 ? 502 PO4 A O2 1 HETATM 1569 O O3 . PO4 C 2 . ? 21.307 39.440 28.149 1.00 53.51 ? 502 PO4 A O3 1 HETATM 1570 O O4 . PO4 C 2 . ? 23.219 37.809 27.658 1.00 51.63 ? 502 PO4 A O4 1 HETATM 1571 P P . PO4 D 2 . ? 42.373 37.711 14.743 1.00 40.32 ? 504 PO4 A P 1 HETATM 1572 O O1 . PO4 D 2 . ? 41.820 36.448 15.184 1.00 27.77 ? 504 PO4 A O1 1 HETATM 1573 O O2 . PO4 D 2 . ? 43.098 38.349 15.925 1.00 48.29 ? 504 PO4 A O2 1 HETATM 1574 O O3 . PO4 D 2 . ? 41.277 38.652 14.226 1.00 44.12 ? 504 PO4 A O3 1 HETATM 1575 O O4 . PO4 D 2 . ? 43.377 37.445 13.606 1.00 50.93 ? 504 PO4 A O4 1 HETATM 1576 P P . PO4 E 2 . ? 34.643 38.029 22.219 1.00 49.35 ? 505 PO4 A P 1 HETATM 1577 O O1 . PO4 E 2 . ? 34.551 36.694 21.697 1.00 35.99 ? 505 PO4 A O1 1 HETATM 1578 O O2 . PO4 E 2 . ? 34.964 37.984 23.733 1.00 51.20 ? 505 PO4 A O2 1 HETATM 1579 O O3 . PO4 E 2 . ? 33.267 38.781 21.998 1.00 49.54 ? 505 PO4 A O3 1 HETATM 1580 O O4 . PO4 E 2 . ? 35.779 38.755 21.456 1.00 55.19 ? 505 PO4 A O4 1 HETATM 1581 N N1 . 017 F 3 . ? 14.279 34.925 18.220 1.00 14.67 ? 1200 017 A N1 1 HETATM 1582 C C2 . 017 F 3 . ? 15.195 34.330 17.380 1.00 12.94 ? 1200 017 A C2 1 HETATM 1583 C C3 . 017 F 3 . ? 16.193 35.169 16.760 1.00 12.63 ? 1200 017 A C3 1 HETATM 1584 C C4 . 017 F 3 . ? 17.180 34.513 15.867 1.00 11.85 ? 1200 017 A C4 1 HETATM 1585 C C5 . 017 F 3 . ? 17.012 33.220 15.616 1.00 10.81 ? 1200 017 A C5 1 HETATM 1586 C C6 . 017 F 3 . ? 15.919 32.472 16.187 1.00 13.71 ? 1200 017 A C6 1 HETATM 1587 C C7 . 017 F 3 . ? 14.979 33.107 17.003 1.00 14.04 ? 1200 017 A C7 1 HETATM 1588 S S8 . 017 F 3 . ? 18.136 32.331 14.660 1.00 10.16 ? 1200 017 A S8 1 HETATM 1589 O O9 . 017 F 3 . ? 18.756 33.247 13.785 1.00 11.32 ? 1200 017 A O9 1 HETATM 1590 O O10 . 017 F 3 . ? 17.453 31.221 14.098 1.00 11.42 ? 1200 017 A O10 1 HETATM 1591 N N11 . 017 F 3 . ? 19.316 31.708 15.598 1.00 10.03 ? 1200 017 A N11 1 HETATM 1592 C C12 . 017 F 3 . ? 20.128 32.699 16.353 1.00 11.72 ? 1200 017 A C12 1 HETATM 1593 C C13 . 017 F 3 . ? 21.628 32.355 16.432 1.00 11.02 ? 1200 017 A C13 1 HETATM 1594 C C14 . 017 F 3 . ? 22.279 32.317 15.034 1.00 12.13 ? 1200 017 A C14 1 HETATM 1595 C C15 . 017 F 3 . ? 22.282 33.401 17.329 1.00 12.08 ? 1200 017 A C15 1 HETATM 1596 C C16 . 017 F 3 . ? 19.063 30.433 16.294 1.00 9.17 ? 1200 017 A C16 1 HETATM 1597 C C17 . 017 F 3 . ? 19.962 29.337 15.738 1.00 8.55 ? 1200 017 A C17 1 HETATM 1598 O O18 . 017 F 3 . ? 19.895 28.206 16.604 1.00 9.54 ? 1200 017 A O18 1 HETATM 1599 C C19 . 017 F 3 . ? 19.599 28.895 14.297 1.00 8.43 ? 1200 017 A C19 1 HETATM 1600 N N20 . 017 F 3 . ? 20.709 28.031 13.805 1.00 8.78 ? 1200 017 A N20 1 HETATM 1601 C C21 . 017 F 3 . ? 21.566 28.405 12.887 1.00 9.33 ? 1200 017 A C21 1 HETATM 1602 O O22 . 017 F 3 . ? 21.634 29.442 12.299 1.00 9.69 ? 1200 017 A O22 1 HETATM 1603 O O23 . 017 F 3 . ? 22.469 27.402 12.655 1.00 9.66 ? 1200 017 A O23 1 HETATM 1604 C C24 . 017 F 3 . ? 23.321 27.511 11.496 1.00 10.12 ? 1200 017 A C24 1 HETATM 1605 C C25 . 017 F 3 . ? 24.640 26.896 11.912 1.00 10.46 ? 1200 017 A C25 1 HETATM 1606 O O26 . 017 F 3 . ? 24.413 25.475 11.833 1.00 10.09 ? 1200 017 A O26 1 HETATM 1607 C C27 . 017 F 3 . ? 23.493 25.227 10.779 1.00 10.21 ? 1200 017 A C27 1 HETATM 1608 O O28 . 017 F 3 . ? 22.483 24.363 11.236 1.00 10.86 ? 1200 017 A O28 1 HETATM 1609 C C29 . 017 F 3 . ? 21.193 25.063 11.296 1.00 10.64 ? 1200 017 A C29 1 HETATM 1610 C C30 . 017 F 3 . ? 21.363 26.256 10.383 1.00 10.81 ? 1200 017 A C30 1 HETATM 1611 C C31 . 017 F 3 . ? 22.839 26.537 10.396 1.00 10.71 ? 1200 017 A C31 1 HETATM 1612 C C32 . 017 F 3 . ? 18.307 28.149 14.166 1.00 9.08 ? 1200 017 A C32 1 HETATM 1613 C C33 . 017 F 3 . ? 18.054 26.400 12.363 1.00 10.63 ? 1200 017 A C33 1 HETATM 1614 C C34 . 017 F 3 . ? 17.831 26.025 11.051 1.00 11.17 ? 1200 017 A C34 1 HETATM 1615 C C35 . 017 F 3 . ? 17.597 26.981 10.098 1.00 11.51 ? 1200 017 A C35 1 HETATM 1616 C C36 . 017 F 3 . ? 17.550 28.293 10.460 1.00 11.00 ? 1200 017 A C36 1 HETATM 1617 C C37 . 017 F 3 . ? 17.765 28.674 11.767 1.00 10.26 ? 1200 017 A C37 1 HETATM 1618 C C38 . 017 F 3 . ? 18.024 27.733 12.757 1.00 9.32 ? 1200 017 A C38 1 HETATM 1619 P P . PO4 G 2 . ? -5.626 26.300 22.085 1.00 23.36 ? 501 PO4 B P 1 HETATM 1620 O O1 . PO4 G 2 . ? -4.465 25.632 22.864 1.00 24.90 ? 501 PO4 B O1 1 HETATM 1621 O O2 . PO4 G 2 . ? -4.920 27.015 21.053 1.00 26.37 ? 501 PO4 B O2 1 HETATM 1622 O O3 . PO4 G 2 . ? -6.680 25.278 21.514 1.00 31.16 ? 501 PO4 B O3 1 HETATM 1623 O O4 . PO4 G 2 . ? -6.552 27.339 22.925 1.00 28.48 ? 501 PO4 B O4 1 HETATM 1624 P P . PO4 H 2 . ? 12.482 12.194 33.278 1.00 38.88 ? 503 PO4 B P 1 HETATM 1625 O O1 . PO4 H 2 . ? 12.623 10.721 33.366 1.00 39.20 ? 503 PO4 B O1 1 HETATM 1626 O O2 . PO4 H 2 . ? 13.862 12.883 33.347 1.00 49.22 ? 503 PO4 B O2 1 HETATM 1627 O O3 . PO4 H 2 . ? 11.756 12.585 32.008 1.00 43.18 ? 503 PO4 B O3 1 HETATM 1628 O O4 . PO4 H 2 . ? 11.649 12.645 34.454 1.00 51.01 ? 503 PO4 B O4 1 HETATM 1629 O O . HOH I 4 . ? 20.056 21.395 15.795 1.00 9.72 ? 1201 HOH A O 1 HETATM 1630 O O . HOH I 4 . ? 19.502 22.761 13.407 1.00 11.00 ? 1202 HOH A O 1 HETATM 1631 O O . HOH I 4 . ? 20.376 31.870 11.841 1.00 11.01 ? 1203 HOH A O 1 HETATM 1632 O O . HOH I 4 . ? 24.470 14.948 23.041 1.00 18.99 ? 1204 HOH A O 1 HETATM 1633 O O . HOH I 4 . ? 32.126 16.598 15.801 1.00 20.67 ? 1205 HOH A O 1 HETATM 1634 O O . HOH I 4 . ? 31.152 23.564 12.349 1.00 14.98 ? 1206 HOH A O 1 HETATM 1635 O O . HOH I 4 . ? 19.773 31.510 33.212 1.00 23.07 ? 1207 HOH A O 1 HETATM 1636 O O . HOH I 4 . ? 38.527 15.568 15.489 1.00 16.16 ? 1208 HOH A O 1 HETATM 1637 O O . HOH I 4 . ? 30.242 38.855 12.622 1.00 19.27 ? 1209 HOH A O 1 HETATM 1638 O O . HOH I 4 . ? 37.509 18.927 30.928 1.00 66.30 ? 1210 HOH A O 1 HETATM 1639 O O . HOH I 4 . ? 22.554 36.018 1.390 1.00 22.79 ? 1211 HOH A O 1 HETATM 1640 O O . HOH I 4 . ? 15.214 33.413 5.158 1.00 23.27 ? 1212 HOH A O 1 HETATM 1641 O O . HOH I 4 . ? 32.655 38.325 11.281 1.00 18.19 ? 1213 HOH A O 1 HETATM 1642 O O . HOH I 4 . ? 36.725 18.360 11.936 1.00 23.65 ? 1214 HOH A O 1 HETATM 1643 O O . HOH I 4 . ? 30.244 36.892 19.101 1.00 19.55 ? 1215 HOH A O 1 HETATM 1644 O O . HOH I 4 . ? 22.211 30.573 30.150 1.00 20.39 ? 1216 HOH A O 1 HETATM 1645 O O . HOH I 4 . ? 26.106 18.484 13.537 1.00 24.44 ? 1217 HOH A O 1 HETATM 1646 O O . HOH I 4 . ? 40.990 22.357 7.513 1.00 26.41 ? 1218 HOH A O 1 HETATM 1647 O O . HOH I 4 . ? 35.011 36.725 19.441 1.00 27.60 ? 1219 HOH A O 1 HETATM 1648 O O . HOH I 4 . ? 28.937 24.711 0.721 1.00 26.97 ? 1220 HOH A O 1 HETATM 1649 O O . HOH I 4 . ? 32.743 37.872 8.649 1.00 27.12 ? 1221 HOH A O 1 HETATM 1650 O O . HOH I 4 . ? 30.254 21.326 11.163 1.00 27.66 ? 1222 HOH A O 1 HETATM 1651 O O . HOH I 4 . ? 24.667 15.436 29.507 1.00 21.39 ? 1223 HOH A O 1 HETATM 1652 O O . HOH I 4 . ? 35.448 34.771 16.380 1.00 21.81 ? 1224 HOH A O 1 HETATM 1653 O O . HOH I 4 . ? 24.419 35.603 29.375 1.00 26.71 ? 1225 HOH A O 1 HETATM 1654 O O . HOH I 4 . ? 31.153 37.034 21.547 1.00 24.76 ? 1226 HOH A O 1 HETATM 1655 O O . HOH I 4 . ? 23.183 25.239 5.038 1.00 25.08 ? 1227 HOH A O 1 HETATM 1656 O O . HOH I 4 . ? 40.557 20.352 22.611 1.00 25.67 ? 1228 HOH A O 1 HETATM 1657 O O . HOH I 4 . ? 34.909 34.098 6.281 1.00 27.77 ? 1229 HOH A O 1 HETATM 1658 O O . HOH I 4 . ? 26.947 37.818 4.115 1.00 34.01 ? 1230 HOH A O 1 HETATM 1659 O O . HOH I 4 . ? 19.571 33.367 35.118 1.00 30.22 ? 1231 HOH A O 1 HETATM 1660 O O . HOH I 4 . ? 14.317 35.443 30.347 1.00 41.94 ? 1232 HOH A O 1 HETATM 1661 O O . HOH I 4 . ? 24.076 21.260 8.457 1.00 32.39 ? 1233 HOH A O 1 HETATM 1662 O O . HOH I 4 . ? 32.796 30.455 0.789 1.00 28.13 ? 1234 HOH A O 1 HETATM 1663 O O . HOH I 4 . ? 16.879 37.933 4.787 1.00 28.00 ? 1235 HOH A O 1 HETATM 1664 O O . HOH I 4 . ? 24.953 40.472 16.765 1.00 34.00 ? 1236 HOH A O 1 HETATM 1665 O O . HOH I 4 . ? 34.545 31.412 1.720 1.00 30.01 ? 1237 HOH A O 1 HETATM 1666 O O . HOH I 4 . ? 35.938 33.777 31.163 1.00 29.47 ? 1238 HOH A O 1 HETATM 1667 O O . HOH I 4 . ? 14.337 33.445 28.692 1.00 30.90 ? 1239 HOH A O 1 HETATM 1668 O O . HOH I 4 . ? 22.650 28.564 34.792 1.00 26.66 ? 1240 HOH A O 1 HETATM 1669 O O . HOH I 4 . ? 25.499 12.874 24.637 1.00 29.83 ? 1241 HOH A O 1 HETATM 1670 O O . HOH I 4 . ? 41.746 25.134 22.803 1.00 24.60 ? 1242 HOH A O 1 HETATM 1671 O O . HOH I 4 . ? 42.773 18.912 22.293 1.00 35.51 ? 1243 HOH A O 1 HETATM 1672 O O . HOH I 4 . ? 28.371 14.951 16.383 1.00 27.22 ? 1244 HOH A O 1 HETATM 1673 O O . HOH I 4 . ? 46.003 28.741 16.572 1.00 29.53 ? 1245 HOH A O 1 HETATM 1674 O O . HOH I 4 . ? 37.435 40.536 13.076 1.00 41.26 ? 1246 HOH A O 1 HETATM 1675 O O . HOH I 4 . ? 25.053 23.610 7.494 1.00 31.32 ? 1247 HOH A O 1 HETATM 1676 O O . HOH I 4 . ? 33.742 16.688 28.022 1.00 26.46 ? 1248 HOH A O 1 HETATM 1677 O O . HOH I 4 . ? 35.443 16.383 25.881 1.00 31.26 ? 1249 HOH A O 1 HETATM 1678 O O . HOH I 4 . ? 15.513 16.399 33.653 1.00 28.44 ? 1250 HOH A O 1 HETATM 1679 O O . HOH I 4 . ? 25.338 27.070 35.519 1.00 35.80 ? 1251 HOH A O 1 HETATM 1680 O O . HOH I 4 . ? 36.111 28.461 29.662 1.00 28.85 ? 1252 HOH A O 1 HETATM 1681 O O A HOH I 4 . ? 31.177 12.878 24.119 0.50 24.08 ? 1253 HOH A O 1 HETATM 1682 O O B HOH I 4 . ? 18.188 40.860 6.058 0.50 35.73 ? 1253 HOH A O 1 HETATM 1683 O O . HOH I 4 . ? 10.764 20.315 33.810 1.00 30.38 ? 1254 HOH A O 1 HETATM 1684 O O . HOH I 4 . ? 27.995 14.575 29.793 1.00 30.38 ? 1255 HOH A O 1 HETATM 1685 O O . HOH I 4 . ? 37.545 26.813 28.286 1.00 30.35 ? 1256 HOH A O 1 HETATM 1686 O O . HOH I 4 . ? 43.767 18.571 15.523 1.00 26.15 ? 1257 HOH A O 1 HETATM 1687 O O . HOH I 4 . ? 25.719 12.974 27.397 1.00 32.15 ? 1258 HOH A O 1 HETATM 1688 O O . HOH I 4 . ? 32.635 35.021 4.224 1.00 30.91 ? 1259 HOH A O 1 HETATM 1689 O O . HOH I 4 . ? 44.792 24.695 12.710 1.00 30.61 ? 1260 HOH A O 1 HETATM 1690 O O . HOH I 4 . ? 32.684 28.589 30.555 1.00 41.52 ? 1261 HOH A O 1 HETATM 1691 O O . HOH I 4 . ? 24.455 31.227 31.391 1.00 32.24 ? 1262 HOH A O 1 HETATM 1692 O O . HOH I 4 . ? 18.720 18.456 36.423 1.00 28.00 ? 1263 HOH A O 1 HETATM 1693 O O . HOH I 4 . ? 27.912 12.399 23.952 1.00 38.97 ? 1264 HOH A O 1 HETATM 1694 O O . HOH I 4 . ? 29.009 37.657 23.043 1.00 39.75 ? 1265 HOH A O 1 HETATM 1695 O O . HOH I 4 . ? 41.992 22.457 23.047 1.00 30.43 ? 1266 HOH A O 1 HETATM 1696 O O . HOH I 4 . ? 46.896 32.717 19.184 1.00 29.90 ? 1267 HOH A O 1 HETATM 1697 O O . HOH I 4 . ? 44.655 29.609 7.419 1.00 30.54 ? 1268 HOH A O 1 HETATM 1698 O O . HOH I 4 . ? 28.110 32.805 -3.098 1.00 29.00 ? 1269 HOH A O 1 HETATM 1699 O O . HOH I 4 . ? 20.387 24.569 4.514 1.00 41.39 ? 1270 HOH A O 1 HETATM 1700 O O . HOH I 4 . ? 17.306 14.511 32.564 1.00 27.93 ? 1271 HOH A O 1 HETATM 1701 O O . HOH I 4 . ? 26.089 16.318 15.993 1.00 31.89 ? 1272 HOH A O 1 HETATM 1702 O O . HOH I 4 . ? 25.310 36.597 2.688 1.00 28.48 ? 1273 HOH A O 1 HETATM 1703 O O . HOH I 4 . ? 32.223 30.978 30.868 1.00 35.13 ? 1274 HOH A O 1 HETATM 1704 O O . HOH I 4 . ? 25.031 16.305 13.856 1.00 33.56 ? 1275 HOH A O 1 HETATM 1705 O O . HOH I 4 . ? 30.501 21.624 8.159 1.00 34.20 ? 1276 HOH A O 1 HETATM 1706 O O . HOH I 4 . ? 24.712 17.765 11.324 1.00 34.86 ? 1277 HOH A O 1 HETATM 1707 O O . HOH I 4 . ? 42.106 37.123 19.766 1.00 33.83 ? 1278 HOH A O 1 HETATM 1708 O O . HOH I 4 . ? 19.937 26.074 6.365 1.00 38.55 ? 1279 HOH A O 1 HETATM 1709 O O . HOH I 4 . ? 22.643 31.133 33.338 1.00 35.62 ? 1280 HOH A O 1 HETATM 1710 O O . HOH I 4 . ? 25.340 23.312 5.051 1.00 42.71 ? 1281 HOH A O 1 HETATM 1711 O O . HOH I 4 . ? 38.841 22.407 5.563 1.00 35.94 ? 1282 HOH A O 1 HETATM 1712 O O . HOH I 4 . ? 44.781 18.255 11.861 1.00 40.96 ? 1283 HOH A O 1 HETATM 1713 O O . HOH I 4 . ? 18.218 36.012 34.680 1.00 38.51 ? 1284 HOH A O 1 HETATM 1714 O O . HOH I 4 . ? 43.783 28.111 29.364 1.00 44.82 ? 1285 HOH A O 1 HETATM 1715 O O . HOH I 4 . ? 38.353 37.628 16.353 1.00 36.63 ? 1286 HOH A O 1 HETATM 1716 O O . HOH I 4 . ? 28.388 39.092 19.490 1.00 37.49 ? 1287 HOH A O 1 HETATM 1717 O O . HOH I 4 . ? 32.279 20.461 34.588 1.00 39.70 ? 1288 HOH A O 1 HETATM 1718 O O . HOH I 4 . ? 27.637 16.777 14.422 1.00 36.29 ? 1289 HOH A O 1 HETATM 1719 O O . HOH I 4 . ? 34.831 36.424 7.793 1.00 32.74 ? 1290 HOH A O 1 HETATM 1720 O O . HOH I 4 . ? 18.420 28.713 5.642 1.00 32.44 ? 1291 HOH A O 1 HETATM 1721 O O . HOH I 4 . ? 44.539 21.832 12.952 1.00 40.72 ? 1292 HOH A O 1 HETATM 1722 O O . HOH I 4 . ? 28.710 40.292 17.167 1.00 32.26 ? 1293 HOH A O 1 HETATM 1723 O O . HOH I 4 . ? 31.089 18.696 11.526 1.00 32.98 ? 1294 HOH A O 1 HETATM 1724 O O . HOH I 4 . ? 22.138 25.318 7.205 1.00 36.48 ? 1295 HOH A O 1 HETATM 1725 O O . HOH I 4 . ? 43.165 35.376 24.302 1.00 34.46 ? 1296 HOH A O 1 HETATM 1726 O O . HOH I 4 . ? 9.950 16.601 33.231 1.00 42.27 ? 1297 HOH A O 1 HETATM 1727 O O . HOH I 4 . ? 47.676 26.803 15.174 1.00 32.51 ? 1298 HOH A O 1 HETATM 1728 O O . HOH I 4 . ? 24.497 38.712 24.884 1.00 35.29 ? 1299 HOH A O 1 HETATM 1729 O O . HOH I 4 . ? 26.077 23.475 37.496 1.00 39.84 ? 1300 HOH A O 1 HETATM 1730 O O . HOH I 4 . ? 45.583 39.291 21.124 1.00 42.18 ? 1301 HOH A O 1 HETATM 1731 O O . HOH I 4 . ? 36.208 35.773 26.365 1.00 39.14 ? 1302 HOH A O 1 HETATM 1732 O O . HOH I 4 . ? 41.931 23.159 1.641 1.00 40.61 ? 1303 HOH A O 1 HETATM 1733 O O . HOH I 4 . ? 40.929 38.006 10.984 1.00 42.83 ? 1304 HOH A O 1 HETATM 1734 O O . HOH I 4 . ? 21.309 15.342 33.578 1.00 45.22 ? 1305 HOH A O 1 HETATM 1735 O O . HOH I 4 . ? 46.579 37.296 24.570 1.00 42.72 ? 1306 HOH A O 1 HETATM 1736 O O . HOH I 4 . ? 36.639 33.881 2.663 1.00 43.37 ? 1307 HOH A O 1 HETATM 1737 O O . HOH I 4 . ? 24.975 36.848 8.418 1.00 15.39 ? 1308 HOH A O 1 HETATM 1738 O O . HOH I 4 . ? 45.923 21.928 7.589 1.00 42.77 ? 1309 HOH A O 1 HETATM 1739 O O . HOH I 4 . ? 34.878 23.303 -0.051 1.00 32.26 ? 1310 HOH A O 1 HETATM 1740 O O . HOH I 4 . ? 13.769 37.610 19.371 1.00 31.62 ? 1311 HOH A O 1 HETATM 1741 O O . HOH I 4 . ? 22.704 16.012 12.662 1.00 37.90 ? 1312 HOH A O 1 HETATM 1742 O O . HOH I 4 . ? 44.642 32.978 24.326 1.00 34.43 ? 1313 HOH A O 1 HETATM 1743 O O . HOH I 4 . ? 43.119 24.270 9.372 1.00 28.78 ? 1314 HOH A O 1 HETATM 1744 O O . HOH I 4 . ? 22.451 36.019 20.668 1.00 22.40 ? 1315 HOH A O 1 HETATM 1745 O O . HOH I 4 . ? 28.600 35.812 2.964 1.00 17.57 ? 1316 HOH A O 1 HETATM 1746 O O . HOH I 4 . ? 33.107 18.564 13.765 1.00 17.56 ? 1317 HOH A O 1 HETATM 1747 O O . HOH I 4 . ? 26.425 19.750 9.549 1.00 39.08 ? 1318 HOH A O 1 HETATM 1748 O O . HOH I 4 . ? 33.522 18.357 4.079 1.00 44.77 ? 1319 HOH A O 1 HETATM 1749 O O . HOH I 4 . ? 22.063 41.553 21.585 1.00 47.19 ? 1320 HOH A O 1 HETATM 1750 O O . HOH I 4 . ? 19.608 40.813 19.710 1.00 39.21 ? 1321 HOH A O 1 HETATM 1751 O O . HOH I 4 . ? 30.733 20.588 36.755 1.00 47.94 ? 1322 HOH A O 1 HETATM 1752 O O . HOH I 4 . ? 32.724 23.497 33.263 1.00 40.20 ? 1323 HOH A O 1 HETATM 1753 O O . HOH I 4 . ? 20.727 21.038 40.272 1.00 36.61 ? 1324 HOH A O 1 HETATM 1754 O O . HOH I 4 . ? 32.029 25.530 35.172 1.00 39.36 ? 1325 HOH A O 1 HETATM 1755 O O . HOH I 4 . ? 40.751 22.044 4.169 1.00 43.23 ? 1326 HOH A O 1 HETATM 1756 O O . HOH I 4 . ? 35.055 30.170 31.704 1.00 38.05 ? 1327 HOH A O 1 HETATM 1757 O O . HOH I 4 . ? 26.870 35.574 30.263 1.00 43.47 ? 1328 HOH A O 1 HETATM 1758 O O . HOH I 4 . ? 31.101 33.574 30.326 1.00 48.08 ? 1329 HOH A O 1 HETATM 1759 O O . HOH I 4 . ? 39.572 37.150 21.646 1.00 42.30 ? 1330 HOH A O 1 HETATM 1760 O O . HOH I 4 . ? 46.762 22.551 10.702 1.00 40.74 ? 1331 HOH A O 1 HETATM 1761 O O . HOH I 4 . ? 35.775 17.843 5.329 1.00 44.19 ? 1332 HOH A O 1 HETATM 1762 O O . HOH I 4 . ? 22.630 37.426 18.479 1.00 44.32 ? 1333 HOH A O 1 HETATM 1763 O O . HOH J 4 . ? 20.059 32.352 23.522 1.00 13.80 ? 504 HOH B O 1 HETATM 1764 O O . HOH J 4 . ? 20.507 34.197 21.507 1.00 15.58 ? 505 HOH B O 1 HETATM 1765 O O . HOH J 4 . ? 16.430 20.696 33.775 1.00 23.03 ? 506 HOH B O 1 HETATM 1766 O O . HOH J 4 . ? 4.274 26.896 12.385 1.00 19.03 ? 507 HOH B O 1 HETATM 1767 O O . HOH J 4 . ? 7.331 35.119 26.449 1.00 27.78 ? 508 HOH B O 1 HETATM 1768 O O . HOH J 4 . ? 18.250 34.775 19.403 1.00 19.66 ? 509 HOH B O 1 HETATM 1769 O O . HOH J 4 . ? 11.226 38.582 5.803 1.00 16.85 ? 510 HOH B O 1 HETATM 1770 O O . HOH J 4 . ? 7.083 21.848 32.909 1.00 21.68 ? 511 HOH B O 1 HETATM 1771 O O . HOH J 4 . ? 18.309 15.699 19.458 1.00 22.14 ? 512 HOH B O 1 HETATM 1772 O O . HOH J 4 . ? 13.268 21.368 35.290 1.00 16.39 ? 513 HOH B O 1 HETATM 1773 O O . HOH J 4 . ? 12.879 24.151 35.808 1.00 18.35 ? 514 HOH B O 1 HETATM 1774 O O . HOH J 4 . ? -2.282 25.216 21.978 1.00 21.48 ? 515 HOH B O 1 HETATM 1775 O O . HOH J 4 . ? 14.238 34.890 26.221 1.00 24.98 ? 516 HOH B O 1 HETATM 1776 O O . HOH J 4 . ? 5.459 23.896 32.088 1.00 21.41 ? 517 HOH B O 1 HETATM 1777 O O . HOH J 4 . ? 7.728 29.685 7.373 1.00 16.96 ? 518 HOH B O 1 HETATM 1778 O O . HOH J 4 . ? 9.015 29.148 34.883 1.00 43.32 ? 519 HOH B O 1 HETATM 1779 O O . HOH J 4 . ? 13.623 26.044 33.466 1.00 24.43 ? 520 HOH B O 1 HETATM 1780 O O . HOH J 4 . ? 25.112 9.620 24.647 1.00 24.58 ? 521 HOH B O 1 HETATM 1781 O O . HOH J 4 . ? -0.061 25.407 27.096 1.00 22.33 ? 522 HOH B O 1 HETATM 1782 O O . HOH J 4 . ? 10.236 22.555 12.067 1.00 21.91 ? 523 HOH B O 1 HETATM 1783 O O . HOH J 4 . ? 3.775 36.921 25.815 1.00 24.11 ? 524 HOH B O 1 HETATM 1784 O O . HOH J 4 . ? -2.442 28.288 21.282 1.00 24.81 ? 525 HOH B O 1 HETATM 1785 O O . HOH J 4 . ? 8.878 34.461 21.070 1.00 26.92 ? 526 HOH B O 1 HETATM 1786 O O . HOH J 4 . ? 2.194 26.368 9.454 1.00 28.97 ? 527 HOH B O 1 HETATM 1787 O O . HOH J 4 . ? 20.476 37.082 2.968 1.00 26.68 ? 528 HOH B O 1 HETATM 1788 O O . HOH J 4 . ? 16.194 13.952 19.322 1.00 26.95 ? 529 HOH B O 1 HETATM 1789 O O . HOH J 4 . ? -7.964 25.545 18.326 1.00 23.85 ? 530 HOH B O 1 HETATM 1790 O O . HOH J 4 . ? 20.049 15.903 12.263 1.00 23.87 ? 531 HOH B O 1 HETATM 1791 O O . HOH J 4 . ? 12.163 20.807 10.967 1.00 26.82 ? 532 HOH B O 1 HETATM 1792 O O . HOH J 4 . ? 9.143 39.275 4.185 1.00 20.88 ? 533 HOH B O 1 HETATM 1793 O O . HOH J 4 . ? 20.093 8.373 28.681 1.00 32.60 ? 534 HOH B O 1 HETATM 1794 O O . HOH J 4 . ? 6.030 20.723 11.805 1.00 30.51 ? 535 HOH B O 1 HETATM 1795 O O . HOH J 4 . ? 15.739 14.859 14.844 1.00 22.41 ? 536 HOH B O 1 HETATM 1796 O O . HOH J 4 . ? 9.565 36.985 25.150 1.00 39.25 ? 537 HOH B O 1 HETATM 1797 O O . HOH J 4 . ? 9.010 23.208 34.209 1.00 35.10 ? 538 HOH B O 1 HETATM 1798 O O . HOH J 4 . ? -2.501 43.372 15.143 1.00 27.05 ? 539 HOH B O 1 HETATM 1799 O O . HOH J 4 . ? -0.804 39.254 20.807 1.00 30.39 ? 540 HOH B O 1 HETATM 1800 O O . HOH J 4 . ? 2.375 18.404 22.966 1.00 34.98 ? 541 HOH B O 1 HETATM 1801 O O . HOH J 4 . ? 14.905 20.464 11.029 1.00 32.13 ? 542 HOH B O 1 HETATM 1802 O O . HOH J 4 . ? 6.448 27.696 5.934 1.00 19.77 ? 543 HOH B O 1 HETATM 1803 O O . HOH J 4 . ? 8.935 33.449 29.391 1.00 25.53 ? 544 HOH B O 1 HETATM 1804 O O . HOH J 4 . ? 6.544 38.062 7.813 1.00 25.33 ? 545 HOH B O 1 HETATM 1805 O O . HOH J 4 . ? 16.565 12.122 21.874 1.00 29.60 ? 546 HOH B O 1 HETATM 1806 O O . HOH J 4 . ? 4.396 13.392 17.438 1.00 37.27 ? 547 HOH B O 1 HETATM 1807 O O . HOH J 4 . ? 0.308 21.158 12.000 1.00 39.57 ? 548 HOH B O 1 HETATM 1808 O O . HOH J 4 . ? -0.393 45.321 18.257 1.00 32.29 ? 549 HOH B O 1 HETATM 1809 O O . HOH J 4 . ? 17.386 39.870 16.168 1.00 26.60 ? 550 HOH B O 1 HETATM 1810 O O . HOH J 4 . ? -2.683 35.785 11.621 1.00 37.04 ? 551 HOH B O 1 HETATM 1811 O O . HOH J 4 . ? 12.086 32.851 29.741 1.00 27.50 ? 552 HOH B O 1 HETATM 1812 O O . HOH J 4 . ? 25.957 14.039 15.127 1.00 31.32 ? 553 HOH B O 1 HETATM 1813 O O . HOH J 4 . ? 10.396 24.580 5.830 1.00 32.31 ? 554 HOH B O 1 HETATM 1814 O O . HOH J 4 . ? -2.925 37.102 19.155 1.00 33.59 ? 555 HOH B O 1 HETATM 1815 O O . HOH J 4 . ? 4.351 24.868 8.774 1.00 28.02 ? 556 HOH B O 1 HETATM 1816 O O . HOH J 4 . ? 3.954 16.798 14.667 1.00 33.46 ? 557 HOH B O 1 HETATM 1817 O O . HOH J 4 . ? 30.464 16.088 29.801 1.00 28.82 ? 558 HOH B O 1 HETATM 1818 O O . HOH J 4 . ? 20.575 10.240 27.056 1.00 33.54 ? 559 HOH B O 1 HETATM 1819 O O . HOH J 4 . ? 9.556 41.810 21.114 1.00 38.40 ? 560 HOH B O 1 HETATM 1820 O O . HOH J 4 . ? 15.411 18.004 10.490 1.00 29.83 ? 561 HOH B O 1 HETATM 1821 O O . HOH J 4 . ? 5.893 47.878 10.061 1.00 35.92 ? 562 HOH B O 1 HETATM 1822 O O . HOH J 4 . ? -2.201 28.661 8.649 1.00 29.85 ? 563 HOH B O 1 HETATM 1823 O O . HOH J 4 . ? -0.992 17.924 23.164 1.00 46.28 ? 564 HOH B O 1 HETATM 1824 O O . HOH J 4 . ? 7.688 25.319 6.067 1.00 31.58 ? 565 HOH B O 1 HETATM 1825 O O . HOH J 4 . ? 13.615 43.441 17.686 1.00 42.24 ? 566 HOH B O 1 HETATM 1826 O O . HOH J 4 . ? 21.217 36.675 16.069 1.00 29.55 ? 567 HOH B O 1 HETATM 1827 O O . HOH J 4 . ? 15.299 37.397 25.335 1.00 39.49 ? 568 HOH B O 1 HETATM 1828 O O . HOH J 4 . ? 9.672 39.413 21.198 1.00 34.96 ? 569 HOH B O 1 HETATM 1829 O O . HOH J 4 . ? 13.360 13.966 14.676 1.00 40.67 ? 570 HOH B O 1 HETATM 1830 O O . HOH J 4 . ? -2.420 19.334 14.090 1.00 32.17 ? 571 HOH B O 1 HETATM 1831 O O . HOH J 4 . ? 18.414 10.500 25.086 1.00 28.06 ? 572 HOH B O 1 HETATM 1832 O O . HOH J 4 . ? 8.336 15.094 29.931 1.00 36.46 ? 573 HOH B O 1 HETATM 1833 O O . HOH J 4 . ? 15.859 43.115 16.268 1.00 36.67 ? 574 HOH B O 1 HETATM 1834 O O . HOH J 4 . ? -3.998 33.357 26.145 1.00 40.72 ? 575 HOH B O 1 HETATM 1835 O O . HOH J 4 . ? -4.768 19.887 15.201 1.00 30.33 ? 576 HOH B O 1 HETATM 1836 O O . HOH J 4 . ? 4.627 23.440 11.393 1.00 30.89 ? 577 HOH B O 1 HETATM 1837 O O . HOH J 4 . ? -0.745 18.321 12.691 1.00 43.86 ? 578 HOH B O 1 HETATM 1838 O O . HOH J 4 . ? 13.539 38.539 23.395 1.00 38.02 ? 579 HOH B O 1 HETATM 1839 O O . HOH J 4 . ? 2.196 41.646 20.232 1.00 28.67 ? 580 HOH B O 1 HETATM 1840 O O . HOH J 4 . ? 19.277 36.583 17.288 1.00 31.14 ? 581 HOH B O 1 HETATM 1841 O O . HOH J 4 . ? 5.480 41.755 10.332 1.00 36.06 ? 582 HOH B O 1 HETATM 1842 O O A HOH J 4 . ? -6.758 25.612 15.632 0.50 35.22 ? 583 HOH B O 1 HETATM 1843 O O B HOH J 4 . ? 43.882 26.857 16.886 0.50 27.44 ? 583 HOH B O 1 HETATM 1844 O O . HOH J 4 . ? 23.632 11.006 28.594 1.00 35.39 ? 584 HOH B O 1 HETATM 1845 O O . HOH J 4 . ? 3.731 27.861 6.408 1.00 31.19 ? 585 HOH B O 1 HETATM 1846 O O . HOH J 4 . ? 10.145 27.141 35.000 1.00 32.58 ? 586 HOH B O 1 HETATM 1847 O O . HOH J 4 . ? 16.466 38.778 20.376 1.00 39.28 ? 587 HOH B O 1 HETATM 1848 O O . HOH J 4 . ? 24.244 18.394 35.194 1.00 36.68 ? 588 HOH B O 1 HETATM 1849 O O . HOH J 4 . ? 1.876 34.177 31.837 1.00 39.05 ? 589 HOH B O 1 HETATM 1850 O O . HOH J 4 . ? 14.237 15.403 20.359 1.00 31.39 ? 590 HOH B O 1 HETATM 1851 O O . HOH J 4 . ? -3.904 37.568 13.766 1.00 37.01 ? 591 HOH B O 1 HETATM 1852 O O . HOH J 4 . ? 11.467 12.816 24.176 1.00 53.16 ? 592 HOH B O 1 HETATM 1853 O O . HOH J 4 . ? 30.886 18.101 33.805 1.00 41.22 ? 593 HOH B O 1 HETATM 1854 O O . HOH J 4 . ? 8.305 18.925 10.000 1.00 40.55 ? 594 HOH B O 1 HETATM 1855 O O . HOH J 4 . ? 0.608 42.091 23.682 1.00 41.95 ? 595 HOH B O 1 HETATM 1856 O O . HOH J 4 . ? -2.835 37.043 21.662 1.00 38.49 ? 596 HOH B O 1 HETATM 1857 O O . HOH J 4 . ? 31.877 14.104 28.088 1.00 42.77 ? 597 HOH B O 1 HETATM 1858 O O . HOH J 4 . ? 11.726 22.221 8.513 1.00 37.15 ? 598 HOH B O 1 HETATM 1859 O O . HOH J 4 . ? 4.009 38.970 8.409 1.00 36.03 ? 599 HOH B O 1 HETATM 1860 O O . HOH J 4 . ? 22.873 13.384 12.622 1.00 40.97 ? 600 HOH B O 1 HETATM 1861 O O . HOH J 4 . ? 8.981 14.232 17.795 1.00 44.16 ? 601 HOH B O 1 HETATM 1862 O O . HOH J 4 . ? 10.472 15.549 13.972 1.00 34.62 ? 602 HOH B O 1 HETATM 1863 O O . HOH J 4 . ? 1.667 22.963 11.160 1.00 33.58 ? 603 HOH B O 1 HETATM 1864 O O . HOH J 4 . ? 8.483 32.492 32.082 1.00 35.98 ? 604 HOH B O 1 HETATM 1865 O O . HOH J 4 . ? 17.528 15.097 11.965 1.00 27.88 ? 605 HOH B O 1 HETATM 1866 O O . HOH J 4 . ? 13.150 44.978 20.881 1.00 40.24 ? 606 HOH B O 1 HETATM 1867 O O . HOH J 4 . ? 8.214 38.896 24.913 1.00 44.14 ? 607 HOH B O 1 HETATM 1868 O O . HOH J 4 . ? 16.031 27.056 32.040 1.00 19.14 ? 608 HOH B O 1 HETATM 1869 O O . HOH J 4 . ? 10.056 30.638 32.854 1.00 28.43 ? 609 HOH B O 1 HETATM 1870 O O . HOH J 4 . ? 18.547 11.703 22.884 1.00 31.79 ? 610 HOH B O 1 HETATM 1871 O O . HOH J 4 . ? 5.592 21.384 9.577 1.00 47.06 ? 611 HOH B O 1 HETATM 1872 O O . HOH J 4 . ? -5.144 43.897 19.917 1.00 44.74 ? 612 HOH B O 1 HETATM 1873 O O . HOH J 4 . ? 19.313 8.939 32.071 1.00 41.91 ? 613 HOH B O 1 HETATM 1874 O O . HOH J 4 . ? 22.632 11.763 24.215 1.00 26.98 ? 614 HOH B O 1 HETATM 1875 O O . HOH J 4 . ? 11.544 12.328 9.955 1.00 41.90 ? 615 HOH B O 1 HETATM 1876 O O . HOH J 4 . ? 12.874 8.983 11.202 1.00 38.70 ? 616 HOH B O 1 HETATM 1877 O O . HOH J 4 . ? -5.262 23.446 24.464 1.00 39.61 ? 617 HOH B O 1 HETATM 1878 O O . HOH J 4 . ? -3.348 30.127 18.634 1.00 25.99 ? 618 HOH B O 1 HETATM 1879 O O . HOH J 4 . ? 13.304 14.435 11.295 1.00 37.67 ? 619 HOH B O 1 HETATM 1880 O O . HOH J 4 . ? 9.200 22.233 8.943 1.00 39.37 ? 620 HOH B O 1 HETATM 1881 O O . HOH J 4 . ? -9.978 36.285 17.171 1.00 39.62 ? 621 HOH B O 1 HETATM 1882 O O . HOH J 4 . ? 3.425 39.605 26.787 1.00 42.29 ? 622 HOH B O 1 HETATM 1883 O O . HOH J 4 . ? 6.931 43.326 23.857 1.00 46.08 ? 623 HOH B O 1 HETATM 1884 O O . HOH J 4 . ? 19.394 23.793 7.557 1.00 36.05 ? 624 HOH B O 1 HETATM 1885 O O . HOH J 4 . ? 16.818 22.966 7.539 1.00 43.73 ? 625 HOH B O 1 HETATM 1886 O O . HOH J 4 . ? 1.926 16.063 21.899 1.00 49.70 ? 626 HOH B O 1 HETATM 1887 O O . HOH J 4 . ? 13.147 40.781 5.590 1.00 37.44 ? 627 HOH B O 1 HETATM 1888 O O . HOH J 4 . ? 17.482 36.806 27.827 1.00 40.89 ? 628 HOH B O 1 HETATM 1889 O O . HOH J 4 . ? 7.528 15.609 22.388 1.00 27.69 ? 629 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PRO A 1 ? 0.3228 0.3823 0.2983 0.0326 -0.0022 -0.0139 1 PRO A N 2 C CA . PRO A 1 ? 0.2833 0.3634 0.2950 0.0238 -0.0116 -0.0018 1 PRO A CA 3 C C . PRO A 1 ? 0.2737 0.3064 0.2273 0.0403 -0.0170 0.0013 1 PRO A C 4 O O . PRO A 1 ? 0.3013 0.3254 0.2374 0.0732 -0.0293 -0.0487 1 PRO A O 5 C CB . PRO A 1 ? 0.3630 0.3780 0.3795 0.0173 0.0000 -0.0064 1 PRO A CB 6 C CG . PRO A 1 ? 0.3506 0.4035 0.3514 0.0018 -0.0074 0.0020 1 PRO A CG 7 C CD . PRO A 1 ? 0.3406 0.3822 0.3410 -0.0076 -0.0264 0.0054 1 PRO A CD 8 N N . GLN A 2 ? 0.2911 0.3208 0.1862 0.0453 -0.0246 -0.0092 2 GLN A N 9 C CA . GLN A 2 ? 0.2575 0.2782 0.1411 0.0284 -0.0061 0.0121 2 GLN A CA 10 C C . GLN A 2 ? 0.2783 0.2713 0.1384 0.0344 -0.0136 -0.0147 2 GLN A C 11 O O . GLN A 2 ? 0.3304 0.2912 0.1535 0.0262 -0.0202 0.0008 2 GLN A O 12 C CB . GLN A 2 ? 0.2921 0.2892 0.1444 0.0430 0.0159 0.0273 2 GLN A CB 13 C CG . GLN A 2 ? 0.2848 0.2709 0.1478 0.0305 0.0289 0.0290 2 GLN A CG 14 C CD . GLN A 2 ? 0.3536 0.2808 0.1755 0.0122 0.0192 0.0302 2 GLN A CD 15 O OE1 . GLN A 2 ? 0.3459 0.3395 0.1691 -0.0395 0.0479 0.0368 2 GLN A OE1 16 N NE2 . GLN A 2 ? 0.2979 0.3111 0.1907 0.0347 0.0513 0.0040 2 GLN A NE2 17 N N . ILE A 3 ? 0.2472 0.2473 0.1341 0.0339 0.0018 0.0060 3 ILE A N 18 C CA . ILE A 3 ? 0.2552 0.2337 0.1442 0.0458 -0.0007 -0.0249 3 ILE A CA 19 C C . ILE A 3 ? 0.2477 0.2010 0.1485 0.0376 -0.0005 0.0021 3 ILE A C 20 O O . ILE A 3 ? 0.2515 0.2236 0.1291 0.0504 -0.0013 -0.0201 3 ILE A O 21 C CB . ILE A 3 ? 0.2784 0.2439 0.1761 0.0342 0.0103 0.0077 3 ILE A CB 22 C CG1 . ILE A 3 ? 0.2985 0.2333 0.1701 0.0251 0.0137 0.0376 3 ILE A CG1 23 C CG2 . ILE A 3 ? 0.2860 0.2478 0.2078 0.0630 0.0178 0.0048 3 ILE A CG2 24 C CD1 . ILE A 3 ? 0.3126 0.3115 0.1943 0.0317 0.0107 0.0306 3 ILE A CD1 25 N N . THR A 4 ? 0.2589 0.2347 0.1091 0.0456 -0.0119 -0.0143 4 THR A N 26 C CA . THR A 4 ? 0.2575 0.2027 0.1382 0.0491 0.0029 -0.0180 4 THR A CA 27 C C . THR A 4 ? 0.2468 0.2054 0.1369 0.0336 -0.0099 -0.0229 4 THR A C 28 O O . THR A 4 ? 0.2558 0.2118 0.1547 0.0285 -0.0229 -0.0099 4 THR A O 29 C CB . THR A 4 ? 0.2566 0.2562 0.1276 0.0509 0.0019 -0.0053 4 THR A CB 30 O OG1 . THR A 4 ? 0.3214 0.2740 0.1385 0.0449 -0.0040 -0.0046 4 THR A OG1 31 C CG2 . THR A 4 ? 0.2823 0.2523 0.1719 0.0531 0.0307 -0.0138 4 THR A CG2 32 N N . LEU A 5 ? 0.2625 0.2165 0.1078 0.0453 0.0118 -0.0333 5 LEU A N 33 C CA . LEU A 5 ? 0.2308 0.1907 0.1082 0.0331 0.0097 -0.0220 5 LEU A CA 34 C C . LEU A 5 ? 0.2760 0.1992 0.1339 0.0574 0.0107 -0.0446 5 LEU A C 35 O O . LEU A 5 ? 0.2583 0.2163 0.1228 0.0669 0.0082 -0.0220 5 LEU A O 36 C CB . LEU A 5 ? 0.2125 0.1980 0.0991 0.0348 0.0064 -0.0094 5 LEU A CB 37 C CG . LEU A 5 ? 0.2129 0.1848 0.1135 0.0335 0.0126 -0.0138 5 LEU A CG 38 C CD1 . LEU A 5 ? 0.2127 0.2146 0.1150 0.0187 0.0366 -0.0102 5 LEU A CD1 39 C CD2 . LEU A 5 ? 0.2222 0.2037 0.1095 0.0246 -0.0083 -0.0179 5 LEU A CD2 40 N N . TRP A 6 ? 0.3074 0.2169 0.1159 0.0722 0.0174 -0.0326 6 TRP A N 41 C CA . TRP A 6 ? 0.2845 0.2216 0.1417 0.0514 0.0101 -0.0445 6 TRP A CA 42 C C . TRP A 6 ? 0.2805 0.2206 0.1951 0.0433 0.0112 -0.0820 6 TRP A C 43 O O . TRP A 6 ? 0.2979 0.2194 0.2704 0.0541 0.0114 -0.0236 6 TRP A O 44 C CB . TRP A 6 ? 0.3282 0.2674 0.1756 0.0530 0.0482 -0.0924 6 TRP A CB 45 C CG . TRP A 6 ? 0.3162 0.2816 0.1183 0.0236 0.0264 -0.0555 6 TRP A CG 46 C CD1 . TRP A 6 ? 0.2761 0.3126 0.1688 0.0528 0.0471 -0.0492 6 TRP A CD1 47 C CD2 . TRP A 6 ? 0.3070 0.2639 0.2041 0.0489 0.0034 -0.0613 6 TRP A CD2 48 N NE1 . TRP A 6 ? 0.3094 0.3240 0.1955 0.0369 -0.0165 -0.0339 6 TRP A NE1 49 C CE2 . TRP A 6 ? 0.3332 0.2861 0.1696 0.0267 -0.0221 -0.0230 6 TRP A CE2 50 C CE3 . TRP A 6 ? 0.3064 0.2957 0.1689 0.0692 0.0256 -0.0660 6 TRP A CE3 51 C CZ2 . TRP A 6 ? 0.2917 0.3585 0.1580 0.0512 0.0253 -0.0145 6 TRP A CZ2 52 C CZ3 . TRP A 6 ? 0.3170 0.3374 0.2296 0.0417 0.0261 -0.0242 6 TRP A CZ3 53 C CH2 . TRP A 6 ? 0.3005 0.3133 0.2110 0.0364 0.0135 0.0264 6 TRP A CH2 54 N N . LYS A 7 ? 0.2737 0.2297 0.1807 0.0457 0.0051 -0.0527 7 LYS A N 55 C CA . LYS A 7 ? 0.2899 0.2250 0.1865 0.0354 -0.0194 -0.0724 7 LYS A CA 56 C C . LYS A 7 ? 0.2823 0.2173 0.1421 0.0142 -0.0172 -0.0516 7 LYS A C 57 O O . LYS A 7 ? 0.2656 0.1968 0.1545 0.0314 -0.0046 -0.0329 7 LYS A O 58 C CB . LYS A 7 ? 0.3564 0.3071 0.1750 -0.0210 -0.0021 -0.1190 7 LYS A CB 59 N N . ARG A 8 ? 0.2350 0.1673 0.1735 0.0309 -0.0198 -0.0369 8 ARG A N 60 C CA . ARG A 8 ? 0.2189 0.1788 0.1372 0.0217 -0.0258 -0.0291 8 ARG A CA 61 C C . ARG A 8 ? 0.2373 0.1656 0.1292 0.0157 -0.0309 -0.0472 8 ARG A C 62 O O . ARG A 8 ? 0.2562 0.1734 0.1527 0.0118 -0.0562 -0.0560 8 ARG A O 63 C CB . ARG A 8 ? 0.2299 0.1934 0.1482 0.0027 -0.0365 -0.0398 8 ARG A CB 64 C CG . ARG A 8 ? 0.2276 0.1738 0.2101 0.0022 -0.0371 -0.0147 8 ARG A CG 65 C CD . ARG A 8 ? 0.2387 0.2236 0.2466 -0.0331 -0.0391 0.0053 8 ARG A CD 66 N NE . ARG A 8 ? 0.3371 0.2557 0.4169 0.0056 -0.0417 0.0425 8 ARG A NE 67 C CZ . ARG A 8 ? 0.4006 0.3149 0.3631 -0.0544 -0.0785 0.0471 8 ARG A CZ 68 N NH1 . ARG A 8 ? 0.4183 0.3313 0.4894 -0.0969 -0.0276 0.0320 8 ARG A NH1 69 N NH2 . ARG A 8 ? 0.3546 0.2574 0.4477 -0.0274 -0.0492 0.1381 8 ARG A NH2 70 N N . PRO A 9 ? 0.1991 0.1450 0.1572 0.0105 -0.0140 -0.0365 9 PRO A N 71 C CA . PRO A 9 ? 0.2230 0.1621 0.1016 0.0043 -0.0352 -0.0232 9 PRO A CA 72 C C . PRO A 9 ? 0.2008 0.1794 0.1283 -0.0007 -0.0242 -0.0359 9 PRO A C 73 O O . PRO A 9 ? 0.2044 0.1590 0.1358 0.0080 -0.0393 -0.0228 9 PRO A O 74 C CB . PRO A 9 ? 0.2105 0.1505 0.1251 0.0155 -0.0110 -0.0250 9 PRO A CB 75 C CG . PRO A 9 ? 0.1717 0.1600 0.1188 -0.0155 -0.0120 -0.0315 9 PRO A CG 76 C CD . PRO A 9 ? 0.1750 0.1561 0.1270 -0.0070 -0.0048 -0.0387 9 PRO A CD 77 N N . LEU A 10 ? 0.2387 0.1989 0.1625 -0.0202 -0.0321 -0.0598 10 LEU A N 78 C CA . LEU A 10 ? 0.2194 0.1917 0.1581 -0.0090 -0.0250 -0.0271 10 LEU A CA 79 C C . LEU A 10 ? 0.2367 0.2704 0.1421 -0.0279 -0.0383 -0.0378 10 LEU A C 80 O O . LEU A 10 ? 0.3001 0.4247 0.1387 -0.0311 -0.0330 -0.0468 10 LEU A O 81 C CB . LEU A 10 ? 0.2699 0.2186 0.2301 -0.0538 -0.0251 -0.0730 10 LEU A CB 82 C CG . LEU A 10 ? 0.2503 0.1908 0.3353 -0.0266 0.0088 -0.0169 10 LEU A CG 83 C CD1 . LEU A 10 ? 0.3524 0.1978 0.3572 -0.0280 0.0192 -0.0301 10 LEU A CD1 84 C CD2 . LEU A 10 ? 0.2827 0.2231 0.3008 0.0152 -0.0813 -0.0231 10 LEU A CD2 85 N N . VAL A 11 ? 0.2085 0.2000 0.1552 -0.0168 -0.0746 0.0051 11 VAL A N 86 C CA . VAL A 11 ? 0.2390 0.2079 0.1833 -0.0215 -0.0869 0.0353 11 VAL A CA 87 C C . VAL A 11 ? 0.2325 0.1865 0.1397 -0.0054 -0.0849 -0.0029 11 VAL A C 88 O O . VAL A 11 ? 0.2106 0.2043 0.1770 -0.0331 -0.0977 0.0250 11 VAL A O 89 C CB . VAL A 11 ? 0.2734 0.2264 0.2230 -0.0209 -0.0935 0.0556 11 VAL A CB 90 C CG1 . VAL A 11 ? 0.3030 0.3081 0.2961 -0.0579 -0.0953 0.0960 11 VAL A CG1 91 C CG2 . VAL A 11 ? 0.2707 0.1692 0.3179 -0.0291 -0.0345 0.0076 11 VAL A CG2 92 N N . THR A 12 ? 0.2106 0.2100 0.2138 -0.0320 -0.1140 0.0385 12 THR A N 93 C CA . THR A 12 ? 0.2279 0.2090 0.1931 -0.0287 -0.1005 0.0193 12 THR A CA 94 C C . THR A 12 ? 0.2239 0.1953 0.2222 0.0004 -0.1024 0.0167 12 THR A C 95 O O . THR A 12 ? 0.2615 0.1762 0.2298 -0.0067 -0.1057 0.0519 12 THR A O 96 C CB . THR A 12 ? 0.2514 0.2456 0.2587 -0.0480 -0.1332 0.0051 12 THR A CB 97 O OG1 . THR A 12 ? 0.2804 0.2324 0.2536 -0.0492 -0.1298 0.0042 12 THR A OG1 98 C CG2 . THR A 12 ? 0.2508 0.2528 0.2930 -0.0360 -0.1382 0.0028 12 THR A CG2 99 N N . ILE A 13 ? 0.2121 0.1652 0.2205 -0.0476 -0.0902 0.0290 13 ILE A N 100 C CA . ILE A 13 ? 0.1954 0.1921 0.2258 -0.0305 -0.0830 0.0425 13 ILE A CA 101 C C . ILE A 13 ? 0.1850 0.1844 0.3148 -0.0674 -0.0782 0.0564 13 ILE A C 102 O O . ILE A 13 ? 0.2051 0.1799 0.3196 -0.0487 -0.1307 0.0655 13 ILE A O 103 C CB . ILE A 13 ? 0.1951 0.1727 0.2307 -0.0336 -0.0877 0.0347 13 ILE A CB 104 C CG1 . ILE A 13 ? 0.1828 0.1911 0.2695 -0.0404 -0.1006 0.0513 13 ILE A CG1 105 C CG2 . ILE A 13 ? 0.1798 0.1818 0.2411 -0.0231 -0.1098 0.0361 13 ILE A CG2 106 C CD1 . ILE A 13 ? 0.1730 0.1899 0.2347 -0.0124 -0.0756 0.0454 13 ILE A CD1 107 N N . ARG A 14 ? 0.1923 0.1889 0.3499 -0.0466 -0.0972 0.0416 14 ARG A N 108 C CA . ARG A 14 ? 0.1845 0.2023 0.3531 -0.0149 -0.0998 0.0564 14 ARG A CA 109 C C . ARG A 14 ? 0.1550 0.2488 0.3665 0.0111 -0.0746 0.0405 14 ARG A C 110 O O . ARG A 14 ? 0.2017 0.1749 0.4316 -0.0146 -0.0720 0.1058 14 ARG A O 111 C CB . ARG A 14 ? 0.2133 0.3121 0.4284 0.0148 -0.1143 0.0376 14 ARG A CB 112 C CG . ARG A 14 ? 0.1978 0.4063 0.3854 0.0268 -0.0745 0.0323 14 ARG A CG 113 C CD . ARG A 14 ? 0.2717 0.4106 0.3912 0.0545 -0.1009 0.0051 14 ARG A CD 114 N NE . ARG A 14 ? 0.2799 0.3645 0.4306 0.0347 -0.0687 0.0672 14 ARG A NE 115 C CZ . ARG A 14 ? 0.2982 0.3757 0.2820 0.0500 -0.0413 0.0435 14 ARG A CZ 116 N NH1 . ARG A 14 ? 0.4540 0.4469 0.3132 0.0401 0.0214 0.0785 14 ARG A NH1 117 N NH2 . ARG A 14 ? 0.2276 0.4004 0.3480 -0.0037 -0.0008 0.0772 14 ARG A NH2 118 N N . ILE A 15 ? 0.1534 0.1745 0.3385 -0.0283 -0.0771 0.0402 15 ILE A N 119 C CA . ILE A 15 ? 0.1883 0.2053 0.3253 -0.0116 -0.0482 0.0584 15 ILE A CA 120 C C . ILE A 15 ? 0.2236 0.2087 0.4071 -0.0105 0.0106 0.0528 15 ILE A C 121 O O . ILE A 15 ? 0.1533 0.2186 0.4986 0.0104 -0.0529 0.0656 15 ILE A O 122 C CB . ILE A 15 ? 0.1863 0.2082 0.3134 -0.0002 -0.0897 0.0700 15 ILE A CB 123 C CG1 . ILE A 15 ? 0.1745 0.2882 0.3173 0.0460 0.0186 0.0759 15 ILE A CG1 124 C CG2 . ILE A 15 ? 0.1856 0.2382 0.4145 0.0413 -0.0431 0.0930 15 ILE A CG2 125 C CD1 . ILE A 15 ? 0.2041 0.3004 0.2947 0.0614 -0.0101 0.1296 15 ILE A CD1 126 N N . GLY A 16 ? 0.2183 0.2166 0.3263 -0.0240 -0.0109 0.0176 16 GLY A N 127 C CA . GLY A 16 ? 0.2402 0.2552 0.3067 -0.0217 -0.0098 0.0018 16 GLY A CA 128 C C . GLY A 16 ? 0.2924 0.2375 0.3147 -0.0208 -0.0153 -0.0110 16 GLY A C 129 O O . GLY A 16 ? 0.2607 0.2706 0.3601 -0.0441 -0.0365 0.0113 16 GLY A O 130 N N . GLY A 17 ? 0.2207 0.2616 0.3046 -0.0076 0.0134 0.0017 17 GLY A N 131 C CA . GLY A 17 ? 0.3543 0.2677 0.3341 -0.0008 -0.0401 -0.0247 17 GLY A CA 132 C C . GLY A 17 ? 0.2286 0.3756 0.3034 0.0346 -0.0429 -0.0409 17 GLY A C 133 O O . GLY A 17 ? 0.3050 0.3550 0.3387 0.0469 -0.0955 -0.0592 17 GLY A O 134 N N . GLN A 18 ? 0.2217 0.2477 0.3629 0.0075 -0.0593 -0.0171 18 GLN A N 135 C CA . GLN A 18 ? 0.2392 0.2618 0.3697 -0.0262 -0.0558 -0.0156 18 GLN A CA 136 C C . GLN A 18 ? 0.2534 0.2591 0.3792 -0.0137 -0.0746 0.0358 18 GLN A C 137 O O . GLN A 18 ? 0.2861 0.2188 0.5021 -0.0809 -0.0776 0.0583 18 GLN A O 138 C CB . GLN A 18 ? 0.2811 0.2588 0.3636 -0.0076 -0.0943 0.0044 18 GLN A CB 139 C CG . GLN A 18 ? 0.3794 0.3332 0.4727 -0.0125 -0.0198 0.0150 18 GLN A CG 140 C CD . GLN A 18 ? 0.3851 0.3143 0.4481 0.0438 0.0191 -0.0702 18 GLN A CD 141 O OE1 . GLN A 18 ? 0.3459 0.2773 0.4085 0.0000 0.1015 -0.0492 18 GLN A OE1 142 N NE2 . GLN A 18 ? 0.3720 0.3330 0.4171 0.0533 -0.0081 -0.0181 18 GLN A NE2 143 N N A LEU A 19 ? 0.2547 0.2245 0.3309 -0.0370 -0.1047 0.0405 19 LEU A N 144 N N B LEU A 19 ? 0.2285 0.1908 0.3064 -0.0426 -0.1268 0.0391 19 LEU A N 145 C CA A LEU A 19 ? 0.2879 0.2841 0.3553 -0.0077 -0.0788 0.0560 19 LEU A CA 146 C CA B LEU A 19 ? 0.2692 0.2479 0.3181 -0.0099 -0.0904 0.0521 19 LEU A CA 147 C C A LEU A 19 ? 0.2436 0.2303 0.3337 -0.0537 -0.0903 0.0678 19 LEU A C 148 C C B LEU A 19 ? 0.2306 0.2130 0.2763 -0.0619 -0.1363 0.0721 19 LEU A C 149 O O A LEU A 19 ? 0.3088 0.2498 0.4408 -0.0720 -0.0859 0.0937 19 LEU A O 150 O O B LEU A 19 ? 0.2472 0.2490 0.3811 -0.1003 -0.1956 0.1190 19 LEU A O 151 C CB A LEU A 19 ? 0.2847 0.2265 0.3652 -0.0248 -0.0603 0.0593 19 LEU A CB 152 C CB B LEU A 19 ? 0.2883 0.1683 0.3330 -0.0237 -0.0692 0.0117 19 LEU A CB 153 C CG A LEU A 19 ? 0.2565 0.3564 0.3658 0.0184 -0.0981 0.0299 19 LEU A CG 154 C CG B LEU A 19 ? 0.2249 0.2007 0.2778 -0.0220 -0.0443 -0.0163 19 LEU A CG 155 C CD1 A LEU A 19 ? 0.3180 0.3271 0.3433 0.0023 -0.0227 -0.0209 19 LEU A CD1 156 C CD1 B LEU A 19 ? 0.2773 0.1784 0.2474 -0.0184 0.0779 -0.0587 19 LEU A CD1 157 C CD2 A LEU A 19 ? 0.2414 0.3269 0.3635 0.0221 -0.0140 0.0672 19 LEU A CD2 158 C CD2 B LEU A 19 ? 0.1613 0.1869 0.2484 -0.0058 -0.1027 0.0473 19 LEU A CD2 159 N N . LYS A 20 ? 0.2308 0.1955 0.3421 -0.0729 -0.1122 0.0789 20 LYS A N 160 C CA . LYS A 20 ? 0.2219 0.1964 0.2607 -0.0365 -0.0938 0.0741 20 LYS A CA 161 C C . LYS A 20 ? 0.2129 0.1797 0.2556 -0.0604 -0.1120 0.0295 20 LYS A C 162 O O . LYS A 20 ? 0.2735 0.1836 0.2778 -0.0439 -0.1127 0.0670 20 LYS A O 163 C CB . LYS A 20 ? 0.2550 0.2667 0.2648 -0.0349 -0.0652 0.0768 20 LYS A CB 164 C CG . LYS A 20 ? 0.2741 0.2886 0.3077 -0.0375 -0.0467 0.0781 20 LYS A CG 165 C CD . LYS A 20 ? 0.2421 0.2431 0.2985 -0.0167 0.0195 0.0316 20 LYS A CD 166 C CE . LYS A 20 ? 0.3121 0.3971 0.3397 -0.0061 0.0120 0.0707 20 LYS A CE 167 N NZ . LYS A 20 ? 0.3438 0.3268 0.3135 -0.0778 -0.0293 0.0690 20 LYS A NZ 168 N N A GLU A 21 ? 0.2188 0.1763 0.2467 -0.0549 -0.1011 0.0522 21 GLU A N 169 N N B GLU A 21 ? 0.2181 0.1862 0.2452 -0.0447 -0.1063 0.0390 21 GLU A N 170 C CA A GLU A 21 ? 0.2119 0.1922 0.2000 -0.0385 -0.0886 0.0251 21 GLU A CA 171 C CA B GLU A 21 ? 0.2280 0.1912 0.1925 -0.0331 -0.0890 0.0262 21 GLU A CA 172 C C A GLU A 21 ? 0.2102 0.1497 0.1695 -0.0325 -0.0790 0.0421 21 GLU A C 173 C C B GLU A 21 ? 0.1480 0.1558 0.1718 -0.0297 -0.0654 0.0195 21 GLU A C 174 O O A GLU A 21 ? 0.1370 0.1380 0.1639 -0.0050 -0.0324 -0.0062 21 GLU A O 175 O O B GLU A 21 ? 0.1359 0.1343 0.1287 0.0129 -0.0248 0.0213 21 GLU A O 176 C CB A GLU A 21 ? 0.2362 0.2116 0.2257 -0.0495 -0.0805 -0.0216 21 GLU A CB 177 C CB B GLU A 21 ? 0.2587 0.2063 0.2386 -0.0429 -0.0719 -0.0123 21 GLU A CB 178 C CG A GLU A 21 ? 0.2367 0.2094 0.2780 -0.0626 -0.1168 -0.0248 21 GLU A CG 179 C CG B GLU A 21 ? 0.2865 0.2331 0.2092 -0.0376 -0.0629 -0.0052 21 GLU A CG 180 C CD A GLU A 21 ? 0.2482 0.2308 0.2771 -0.0294 -0.0808 -0.0307 21 GLU A CD 181 C CD B GLU A 21 ? 0.3313 0.2867 0.3162 -0.0056 -0.0264 -0.0417 21 GLU A CD 182 O OE1 A GLU A 21 ? 0.2810 0.2298 0.1823 -0.0306 -0.1317 0.0370 21 GLU A OE1 183 O OE1 B GLU A 21 ? 0.4446 0.3688 0.3887 -0.0441 -0.0283 0.0601 21 GLU A OE1 184 O OE2 A GLU A 21 ? 0.3113 0.3417 0.1945 -0.0632 -0.0813 -0.0125 21 GLU A OE2 185 O OE2 B GLU A 21 ? 0.3935 0.3297 0.3098 -0.0196 -0.0228 -0.0485 21 GLU A OE2 186 N N . ALA A 22 ? 0.1849 0.1401 0.1531 -0.0194 -0.0380 0.0243 22 ALA A N 187 C CA . ALA A 22 ? 0.1562 0.1226 0.1420 -0.0198 -0.0365 0.0126 22 ALA A CA 188 C C . ALA A 22 ? 0.1691 0.1474 0.1279 -0.0292 -0.0302 0.0329 22 ALA A C 189 O O . ALA A 22 ? 0.1884 0.1884 0.1276 -0.0164 -0.0470 0.0294 22 ALA A O 190 C CB . ALA A 22 ? 0.1541 0.1456 0.1525 -0.0149 -0.0364 0.0196 22 ALA A CB 191 N N . LEU A 23 ? 0.1410 0.1418 0.1213 -0.0129 -0.0357 0.0060 23 LEU A N 192 C CA . LEU A 23 ? 0.1559 0.1343 0.1117 -0.0160 -0.0295 -0.0055 23 LEU A CA 193 C C . LEU A 23 ? 0.1244 0.1202 0.1073 -0.0043 -0.0102 -0.0104 23 LEU A C 194 O O . LEU A 23 ? 0.1614 0.1292 0.1098 -0.0151 -0.0092 -0.0106 23 LEU A O 195 C CB . LEU A 23 ? 0.1475 0.1507 0.1258 0.0053 -0.0244 -0.0001 23 LEU A CB 196 C CG . LEU A 23 ? 0.1647 0.1330 0.1476 -0.0105 -0.0117 -0.0057 23 LEU A CG 197 C CD1 . LEU A 23 ? 0.1903 0.2093 0.1327 0.0127 0.0029 0.0076 23 LEU A CD1 198 C CD2 . LEU A 23 ? 0.1655 0.1627 0.1369 0.0032 -0.0177 0.0178 23 LEU A CD2 199 N N . LEU A 24 ? 0.1546 0.1246 0.0940 -0.0066 -0.0201 -0.0147 24 LEU A N 200 C CA . LEU A 24 ? 0.1327 0.1398 0.0941 0.0075 -0.0060 -0.0057 24 LEU A CA 201 C C . LEU A 24 ? 0.1124 0.1422 0.1215 0.0076 -0.0040 -0.0156 24 LEU A C 202 O O . LEU A 24 ? 0.1416 0.1555 0.1037 0.0013 -0.0073 -0.0245 24 LEU A O 203 C CB . LEU A 24 ? 0.1581 0.1321 0.1040 0.0049 -0.0072 0.0012 24 LEU A CB 204 C CG . LEU A 24 ? 0.1878 0.1448 0.1144 0.0127 -0.0398 0.0110 24 LEU A CG 205 C CD1 . LEU A 24 ? 0.2469 0.1869 0.1399 0.0127 -0.0622 0.0189 24 LEU A CD1 206 C CD2 . LEU A 24 ? 0.1626 0.2034 0.1748 0.0136 -0.0577 -0.0389 24 LEU A CD2 207 N N . ASP A 25 ? 0.1210 0.1133 0.1137 0.0077 -0.0173 -0.0030 25 ASP A N 208 C CA . ASP A 25 ? 0.1218 0.1203 0.0766 0.0039 -0.0019 -0.0018 25 ASP A CA 209 C C . ASP A 25 ? 0.1065 0.1061 0.1037 0.0045 -0.0017 -0.0012 25 ASP A C 210 O O . ASP A 25 ? 0.1219 0.1033 0.1034 0.0082 0.0096 -0.0067 25 ASP A O 211 C CB . ASP A 25 ? 0.1235 0.1253 0.1078 0.0021 0.0082 0.0014 25 ASP A CB 212 C CG . ASP A 25 ? 0.1468 0.1240 0.1232 0.0175 -0.0038 0.0063 25 ASP A CG 213 O OD1 . ASP A 25 ? 0.1268 0.1279 0.1437 0.0101 -0.0103 -0.0106 25 ASP A OD1 214 O OD2 . ASP A 25 ? 0.1433 0.1598 0.1454 0.0125 -0.0055 0.0142 25 ASP A OD2 215 N N . THR A 26 ? 0.1162 0.1085 0.0949 0.0000 0.0096 -0.0101 26 THR A N 216 C CA . THR A 26 ? 0.1083 0.1070 0.0899 -0.0036 0.0035 -0.0040 26 THR A CA 217 C C . THR A 26 ? 0.1111 0.1081 0.0912 0.0004 0.0150 -0.0006 26 THR A C 218 O O . THR A 26 ? 0.1293 0.1046 0.0956 0.0095 -0.0005 -0.0056 26 THR A O 219 C CB . THR A 26 ? 0.1085 0.0970 0.0984 0.0044 0.0001 -0.0056 26 THR A CB 220 O OG1 . THR A 26 ? 0.1158 0.1089 0.1053 0.0115 0.0063 -0.0038 26 THR A OG1 221 C CG2 . THR A 26 ? 0.1250 0.1139 0.1065 0.0174 0.0037 0.0015 26 THR A CG2 222 N N . GLY A 27 ? 0.1093 0.0944 0.0940 -0.0005 0.0096 -0.0007 27 GLY A N 223 C CA . GLY A 27 ? 0.1189 0.1097 0.0999 0.0055 -0.0018 0.0109 27 GLY A CA 224 C C . GLY A 27 ? 0.1145 0.1055 0.0957 0.0128 0.0023 0.0051 27 GLY A C 225 O O . GLY A 27 ? 0.1198 0.1349 0.1006 0.0088 -0.0065 0.0115 27 GLY A O 226 N N . ALA A 28 ? 0.1022 0.1168 0.0928 0.0135 0.0064 0.0010 28 ALA A N 227 C CA . ALA A 28 ? 0.1209 0.1028 0.1027 0.0142 0.0019 0.0067 28 ALA A CA 228 C C . ALA A 28 ? 0.0907 0.1054 0.0968 -0.0017 0.0157 0.0001 28 ALA A C 229 O O . ALA A 28 ? 0.1175 0.1100 0.0945 0.0085 -0.0001 0.0045 28 ALA A O 230 C CB . ALA A 28 ? 0.1092 0.1150 0.0915 0.0151 0.0012 0.0087 28 ALA A CB 231 N N . ASP A 29 ? 0.1231 0.1161 0.0837 0.0130 -0.0001 -0.0096 29 ASP A N 232 C CA . ASP A 29 ? 0.1275 0.1238 0.0995 0.0095 0.0212 -0.0179 29 ASP A CA 233 C C . ASP A 29 ? 0.1317 0.1267 0.1145 0.0228 0.0155 -0.0186 29 ASP A C 234 O O . ASP A 29 ? 0.1393 0.1344 0.1354 0.0284 0.0020 -0.0123 29 ASP A O 235 C CB . ASP A 29 ? 0.1392 0.1320 0.1145 0.0088 0.0213 -0.0234 29 ASP A CB 236 C CG . ASP A 29 ? 0.1568 0.1684 0.1089 0.0068 -0.0006 -0.0116 29 ASP A CG 237 O OD1 . ASP A 29 ? 0.1464 0.1378 0.1466 0.0113 -0.0085 -0.0025 29 ASP A OD1 238 O OD2 . ASP A 29 ? 0.1748 0.2101 0.1407 -0.0124 -0.0113 -0.0178 29 ASP A OD2 239 N N . ASP A 30 ? 0.1222 0.1348 0.1199 0.0145 0.0126 -0.0071 30 ASP A N 240 C CA . ASP A 30 ? 0.1304 0.1484 0.1191 0.0210 0.0186 0.0062 30 ASP A CA 241 C C . ASP A 30 ? 0.1274 0.1301 0.1276 0.0102 0.0068 0.0169 30 ASP A C 242 O O . ASP A 30 ? 0.1136 0.1408 0.1655 0.0139 0.0035 -0.0038 30 ASP A O 243 C CB . ASP A 30 ? 0.1383 0.1933 0.1548 0.0046 0.0268 0.0178 30 ASP A CB 244 C CG . ASP A 30 ? 0.1789 0.2807 0.1695 0.0129 -0.0048 0.0003 30 ASP A CG 245 O OD1 . ASP A 30 ? 0.2666 0.2843 0.2339 0.0023 0.0391 -0.0554 30 ASP A OD1 246 O OD2 . ASP A 30 ? 0.3268 0.5742 0.2075 0.1169 -0.0580 -0.0868 30 ASP A OD2 247 N N . THR A 31 ? 0.1187 0.1462 0.1455 0.0279 -0.0014 -0.0185 31 THR A N 248 C CA . THR A 31 ? 0.1241 0.1267 0.1167 0.0192 0.0088 0.0062 31 THR A CA 249 C C . THR A 31 ? 0.1227 0.1409 0.1309 0.0142 0.0066 0.0235 31 THR A C 250 O O . THR A 31 ? 0.1388 0.1600 0.1395 0.0219 0.0354 0.0176 31 THR A O 251 C CB . THR A 31 ? 0.1036 0.1314 0.1369 0.0113 0.0165 0.0096 31 THR A CB 252 O OG1 . THR A 31 ? 0.1155 0.1290 0.1501 0.0133 0.0030 0.0292 31 THR A OG1 253 C CG2 . THR A 31 ? 0.1106 0.1569 0.1728 0.0000 0.0010 0.0329 31 THR A CG2 254 N N . VAL A 32 ? 0.1147 0.1289 0.1369 0.0101 0.0126 0.0084 32 VAL A N 255 C CA . VAL A 32 ? 0.1187 0.1260 0.1297 0.0093 0.0128 0.0208 32 VAL A CA 256 C C . VAL A 32 ? 0.1443 0.1124 0.1394 0.0031 -0.0020 0.0204 32 VAL A C 257 O O . VAL A 32 ? 0.1323 0.1322 0.1419 -0.0019 0.0061 0.0144 32 VAL A O 258 C CB . VAL A 32 ? 0.1226 0.1391 0.1165 0.0142 0.0078 0.0182 32 VAL A CB 259 C CG1 . VAL A 32 ? 0.1505 0.1679 0.1165 0.0218 -0.0024 0.0188 32 VAL A CG1 260 C CG2 . VAL A 32 ? 0.1199 0.1669 0.1493 0.0289 0.0051 0.0093 32 VAL A CG2 261 N N . LEU A 33 ? 0.1283 0.1262 0.1493 -0.0048 0.0102 0.0183 33 LEU A N 262 C CA . LEU A 33 ? 0.1263 0.1393 0.1305 0.0076 0.0118 0.0298 33 LEU A CA 263 C C . LEU A 33 ? 0.1199 0.1540 0.1434 0.0067 -0.0061 0.0137 33 LEU A C 264 O O . LEU A 33 ? 0.1364 0.1582 0.1380 -0.0011 -0.0035 0.0346 33 LEU A O 265 C CB . LEU A 33 ? 0.1272 0.1483 0.1710 0.0051 -0.0056 0.0462 33 LEU A CB 266 C CG . LEU A 33 ? 0.1540 0.1817 0.1759 0.0310 -0.0077 0.0383 33 LEU A CG 267 C CD1 . LEU A 33 ? 0.1855 0.1648 0.2242 0.0192 -0.0274 0.0549 33 LEU A CD1 268 C CD2 . LEU A 33 ? 0.2129 0.1790 0.1397 -0.0026 -0.0204 0.0390 33 LEU A CD2 269 N N . GLU A 34 ? 0.1540 0.1314 0.1689 -0.0101 -0.0064 0.0221 34 GLU A N 270 C CA . GLU A 34 ? 0.1652 0.1630 0.1872 -0.0022 -0.0190 0.0530 34 GLU A CA 271 C C . GLU A 34 ? 0.1664 0.1672 0.2080 -0.0334 -0.0156 0.0550 34 GLU A C 272 O O . GLU A 34 ? 0.1684 0.1923 0.2461 -0.0260 -0.0268 0.0790 34 GLU A O 273 C CB . GLU A 34 ? 0.2329 0.1791 0.2335 -0.0516 -0.0138 0.0490 34 GLU A CB 274 C CG . GLU A 34 ? 0.2713 0.2115 0.2660 -0.0218 0.0049 0.0232 34 GLU A CG 275 C CD . GLU A 34 ? 0.4464 0.2405 0.3046 -0.0250 0.0021 0.0205 34 GLU A CD 276 O OE1 . GLU A 34 ? 0.4027 0.2351 0.3605 -0.0599 -0.0140 0.0243 34 GLU A OE1 277 O OE2 . GLU A 34 ? 0.5408 0.2603 0.3137 -0.0561 -0.0732 0.0305 34 GLU A OE2 278 N N . GLU A 35 ? 0.1669 0.2015 0.2531 -0.0324 -0.0132 0.0996 35 GLU A N 279 C CA . GLU A 35 ? 0.2129 0.2233 0.2388 -0.0136 -0.0072 0.0817 35 GLU A CA 280 C C . GLU A 35 ? 0.1935 0.2005 0.2409 -0.0341 -0.0130 0.0562 35 GLU A C 281 O O . GLU A 35 ? 0.2119 0.2216 0.3054 -0.0492 -0.0289 0.0377 35 GLU A O 282 C CB . GLU A 35 ? 0.2215 0.2276 0.2923 -0.0295 -0.0046 0.1122 35 GLU A CB 283 C CG . GLU A 35 ? 0.2908 0.3309 0.3797 -0.0477 0.0496 0.1166 35 GLU A CG 284 C CD . GLU A 35 ? 0.4782 0.4590 0.3621 -0.0323 0.0156 0.0159 35 GLU A CD 285 O OE1 . GLU A 35 ? 0.5521 0.4992 0.3703 -0.0713 0.0161 0.0229 35 GLU A OE1 286 O OE2 . GLU A 35 ? 0.5125 0.5852 0.5618 -0.0201 0.0356 -0.0146 35 GLU A OE2 287 N N . MET A 36 ? 0.1903 0.2161 0.2925 -0.0467 -0.0076 0.0494 36 MET A N 288 C CA . MET A 36 ? 0.2029 0.2473 0.2941 -0.0508 -0.0356 0.0319 36 MET A CA 289 C C . MET A 36 ? 0.2186 0.2924 0.2884 -0.0403 -0.0316 0.0346 36 MET A C 290 O O . MET A 36 ? 0.1756 0.3499 0.2669 -0.0093 -0.0090 0.0247 36 MET A O 291 C CB . MET A 36 ? 0.2321 0.2023 0.2831 -0.0415 -0.0355 0.0284 36 MET A CB 292 C CG . MET A 36 ? 0.1765 0.2170 0.2597 -0.0169 -0.0157 0.0625 36 MET A CG 293 S SD . MET A 36 ? 0.2177 0.2364 0.3392 -0.0174 0.0319 0.0551 36 MET A SD 294 C CE . MET A 36 ? 0.2257 0.2640 0.2620 -0.0129 0.0286 0.0651 36 MET A CE 295 N N . ASN A 37 ? 0.2096 0.2869 0.3295 -0.0339 -0.0211 0.0411 37 ASN A N 296 C CA . ASN A 37 ? 0.2469 0.2807 0.2972 -0.0340 0.0084 0.0586 37 ASN A CA 297 C C . ASN A 37 ? 0.2136 0.2806 0.2741 0.0196 -0.0041 0.0481 37 ASN A C 298 O O . ASN A 37 ? 0.2061 0.3246 0.2658 0.0164 0.0407 0.0536 37 ASN A O 299 C CB . ASN A 37 ? 0.2422 0.3566 0.3564 -0.0505 0.0187 0.0693 37 ASN A CB 300 C CG . ASN A 37 ? 0.3322 0.3403 0.3784 -0.0632 0.0159 0.0595 37 ASN A CG 301 O OD1 . ASN A 37 ? 0.4821 0.3589 0.4929 -0.0729 0.0355 0.0269 37 ASN A OD1 302 N ND2 . ASN A 37 ? 0.3348 0.4619 0.3777 -0.0540 0.0123 0.0937 37 ASN A ND2 303 N N . LEU A 38 ? 0.1769 0.3060 0.2417 -0.0013 -0.0240 0.0514 38 LEU A N 304 C CA . LEU A 38 ? 0.2193 0.2897 0.2795 0.0112 -0.0204 0.0158 38 LEU A CA 305 C C . LEU A 38 ? 0.2416 0.3394 0.2133 0.0014 -0.0386 -0.0124 38 LEU A C 306 O O . LEU A 38 ? 0.1682 0.4568 0.2530 0.0174 -0.0314 0.0005 38 LEU A O 307 C CB . LEU A 38 ? 0.2484 0.3196 0.2669 0.0052 0.0055 -0.0059 38 LEU A CB 308 C CG . LEU A 38 ? 0.2430 0.3434 0.2273 -0.0149 -0.0086 -0.0078 38 LEU A CG 309 C CD1 . LEU A 38 ? 0.2965 0.2729 0.2128 -0.0130 -0.0306 0.0592 38 LEU A CD1 310 C CD2 . LEU A 38 ? 0.3179 0.2729 0.2215 -0.0208 0.0008 -0.0343 38 LEU A CD2 311 N N . PRO A 39 ? 0.2598 0.3843 0.3215 0.0347 -0.0437 -0.0318 39 PRO A N 312 C CA . PRO A 39 ? 0.2840 0.3798 0.3422 0.0238 -0.0352 -0.0351 39 PRO A CA 313 C C . PRO A 39 ? 0.2645 0.3447 0.3410 0.0261 -0.0191 -0.0316 39 PRO A C 314 O O . PRO A 39 ? 0.2537 0.4103 0.3698 0.0203 -0.0219 -0.0258 39 PRO A O 315 C CB . PRO A 39 ? 0.2915 0.3806 0.3847 0.0131 -0.0857 -0.0435 39 PRO A CB 316 C CG . PRO A 39 ? 0.3283 0.3816 0.4267 0.0564 -0.0351 -0.0214 39 PRO A CG 317 C CD . PRO A 39 ? 0.3003 0.3292 0.3399 0.0442 -0.0649 -0.0117 39 PRO A CD 318 N N . GLY A 40 ? 0.2544 0.3786 0.3802 -0.0011 -0.0131 -0.0434 40 GLY A N 319 C CA . GLY A 40 ? 0.3076 0.3764 0.3757 0.0099 -0.0009 -0.0439 40 GLY A CA 320 C C . GLY A 40 ? 0.2459 0.3638 0.3550 0.0220 0.0160 -0.0477 40 GLY A C 321 O O . GLY A 40 ? 0.2498 0.3598 0.3785 -0.0206 0.0198 -0.0458 40 GLY A O 322 N N . LYS A 41 ? 0.2300 0.3559 0.3843 0.0444 -0.0029 -0.0379 41 LYS A N 323 C CA . LYS A 41 ? 0.2387 0.3698 0.3332 0.0438 0.0162 -0.0450 41 LYS A CA 324 C C . LYS A 41 ? 0.2003 0.3402 0.3311 0.0519 0.0307 -0.0088 41 LYS A C 325 O O . LYS A 41 ? 0.2789 0.3511 0.3063 0.0344 -0.0235 0.0136 41 LYS A O 326 C CB . LYS A 41 ? 0.2722 0.3694 0.3936 0.0792 -0.0057 -0.0493 41 LYS A CB 327 N N . TRP A 42 ? 0.1868 0.3528 0.2383 -0.0113 0.0299 -0.0034 42 TRP A N 328 C CA . TRP A 42 ? 0.1587 0.2739 0.2285 0.0016 0.0285 0.0131 42 TRP A CA 329 C C . TRP A 42 ? 0.1829 0.2975 0.2086 0.0145 0.0374 0.0031 42 TRP A C 330 O O . TRP A 42 ? 0.2218 0.3467 0.2106 0.0013 0.0632 -0.0142 42 TRP A O 331 C CB . TRP A 42 ? 0.2176 0.2722 0.1862 -0.0284 0.0158 -0.0006 42 TRP A CB 332 C CG . TRP A 42 ? 0.1923 0.3094 0.2025 -0.0059 0.0134 0.0177 42 TRP A CG 333 C CD1 . TRP A 42 ? 0.2500 0.3955 0.2061 -0.0603 -0.0078 0.0196 42 TRP A CD1 334 C CD2 . TRP A 42 ? 0.2215 0.2862 0.1592 -0.0053 0.0833 0.0138 42 TRP A CD2 335 N NE1 . TRP A 42 ? 0.2606 0.3371 0.2583 -0.0732 0.0073 0.0176 42 TRP A NE1 336 C CE2 . TRP A 42 ? 0.2109 0.3119 0.2234 -0.0019 0.0687 0.0268 42 TRP A CE2 337 C CE3 . TRP A 42 ? 0.2207 0.2386 0.1931 0.0123 0.0570 -0.0204 42 TRP A CE3 338 C CZ2 . TRP A 42 ? 0.3246 0.2732 0.2429 -0.0605 0.0216 0.0273 42 TRP A CZ2 339 C CZ3 . TRP A 42 ? 0.2776 0.2749 0.2082 -0.0189 0.0034 0.0069 42 TRP A CZ3 340 C CH2 . TRP A 42 ? 0.3227 0.3110 0.1695 -0.0255 0.0563 0.0178 42 TRP A CH2 341 N N . LYS A 43 ? 0.1730 0.2568 0.1995 0.0295 0.0272 -0.0024 43 LYS A N 342 C CA . LYS A 43 ? 0.2093 0.2902 0.2189 0.0508 0.0112 -0.0057 43 LYS A CA 343 C C . LYS A 43 ? 0.1793 0.2467 0.2191 0.0435 0.0304 -0.0103 43 LYS A C 344 O O . LYS A 43 ? 0.1833 0.2607 0.1840 0.0405 0.0454 0.0000 43 LYS A O 345 C CB . LYS A 43 ? 0.2905 0.3140 0.3146 0.0512 -0.0233 -0.0447 43 LYS A CB 346 N N . PRO A 44 ? 0.1626 0.2822 0.1865 0.0453 0.0273 -0.0160 44 PRO A N 347 C CA . PRO A 44 ? 0.1659 0.2405 0.2059 0.0325 0.0084 -0.0074 44 PRO A CA 348 C C . PRO A 44 ? 0.1886 0.2076 0.2144 0.0261 0.0258 0.0034 44 PRO A C 349 O O . PRO A 44 ? 0.1852 0.2612 0.2647 0.0258 0.0317 -0.0464 44 PRO A O 350 C CB . PRO A 44 ? 0.2178 0.2450 0.2168 0.0171 0.0496 0.0213 44 PRO A CB 351 C CG . PRO A 44 ? 0.2591 0.3625 0.1709 0.0405 0.0524 -0.0044 44 PRO A CG 352 C CD . PRO A 44 ? 0.1844 0.3203 0.1903 0.0343 0.0181 -0.0297 44 PRO A CD 353 N N . LYS A 45 ? 0.1726 0.2039 0.1841 0.0206 0.0005 -0.0377 45 LYS A N 354 C CA . LYS A 45 ? 0.1824 0.2015 0.1700 0.0215 -0.0017 -0.0386 45 LYS A CA 355 C C . LYS A 45 ? 0.1749 0.1819 0.1521 0.0170 -0.0056 -0.0409 45 LYS A C 356 O O . LYS A 45 ? 0.1559 0.1859 0.1952 0.0220 0.0022 -0.0230 45 LYS A O 357 C CB . LYS A 45 ? 0.2280 0.1997 0.2574 0.0391 -0.0186 -0.0028 45 LYS A CB 358 C CG . LYS A 45 ? 0.2673 0.2825 0.3712 0.0498 -0.0366 0.0077 45 LYS A CG 359 C CD . LYS A 45 ? 0.3181 0.3004 0.4277 0.0508 -0.0122 -0.0207 45 LYS A CD 360 C CE . LYS A 45 ? 0.3775 0.2674 0.4279 0.0450 0.0053 -0.0263 45 LYS A CE 361 N NZ . LYS A 45 ? 0.5741 0.4177 0.5215 0.0053 -0.0558 -0.0916 45 LYS A NZ 362 N N . MET A 46 ? 0.1737 0.1829 0.1427 0.0161 -0.0031 -0.0288 46 MET A N 363 C CA . MET A 46 ? 0.1745 0.1681 0.1738 0.0190 0.0114 -0.0146 46 MET A CA 364 C C . MET A 46 ? 0.1737 0.1519 0.1808 0.0141 0.0172 -0.0055 46 MET A C 365 O O . MET A 46 ? 0.2045 0.1608 0.2418 0.0184 0.0519 -0.0220 46 MET A O 366 C CB . MET A 46 ? 0.1650 0.1826 0.1810 0.0325 -0.0105 -0.0249 46 MET A CB 367 C CG . MET A 46 ? 0.2240 0.2473 0.1300 0.0144 -0.0067 -0.0224 46 MET A CG 368 S SD . MET A 46 ? 0.2837 0.2662 0.1754 0.0210 -0.0396 -0.0349 46 MET A SD 369 C CE . MET A 46 ? 0.2870 0.2803 0.1999 0.0797 -0.0306 -0.0124 46 MET A CE 370 N N A ILE A 47 ? 0.1322 0.1568 0.1466 0.0119 0.0037 -0.0016 47 ILE A N 371 N N B ILE A 47 ? 0.1526 0.1581 0.1433 0.0172 0.0138 0.0027 47 ILE A N 372 C CA A ILE A 47 ? 0.1587 0.1489 0.1832 0.0117 0.0146 -0.0136 47 ILE A CA 373 C CA B ILE A 47 ? 0.1575 0.1368 0.1666 0.0160 0.0110 -0.0196 47 ILE A CA 374 C C A ILE A 47 ? 0.1565 0.1636 0.1658 0.0168 0.0049 -0.0015 47 ILE A C 375 C C B ILE A 47 ? 0.1450 0.1594 0.1531 0.0185 -0.0100 -0.0057 47 ILE A C 376 O O A ILE A 47 ? 0.1515 0.1479 0.1829 0.0209 0.0149 0.0027 47 ILE A O 377 O O B ILE A 47 ? 0.1510 0.1464 0.1785 0.0249 0.0187 0.0015 47 ILE A O 378 C CB A ILE A 47 ? 0.1762 0.1698 0.1825 0.0259 0.0231 -0.0090 47 ILE A CB 379 C CB B ILE A 47 ? 0.1425 0.1295 0.1641 0.0338 0.0249 -0.0167 47 ILE A CB 380 C CG1 A ILE A 47 ? 0.1554 0.2103 0.2430 -0.0161 0.0193 0.0002 47 ILE A CG1 381 C CG1 B ILE A 47 ? 0.1438 0.1467 0.1321 0.0270 0.0052 0.0099 47 ILE A CG1 382 C CG2 A ILE A 47 ? 0.2124 0.2055 0.2059 0.0181 0.0071 -0.0045 47 ILE A CG2 383 C CG2 B ILE A 47 ? 0.1260 0.1439 0.2085 0.0219 -0.0022 0.0104 47 ILE A CG2 384 C CD1 A ILE A 47 ? 0.2278 0.2312 0.2331 -0.0155 0.0276 0.0248 47 ILE A CD1 385 C CD1 B ILE A 47 ? 0.1507 0.1619 0.1286 0.0194 0.0000 0.0063 47 ILE A CD1 386 N N . GLY A 48 ? 0.1530 0.1500 0.1530 0.0123 0.0057 -0.0017 48 GLY A N 387 C CA . GLY A 48 ? 0.1436 0.1594 0.1714 0.0056 0.0051 0.0048 48 GLY A CA 388 C C . GLY A 48 ? 0.1510 0.1446 0.1186 0.0103 0.0058 0.0141 48 GLY A C 389 O O . GLY A 48 ? 0.2212 0.1465 0.1509 0.0255 0.0080 0.0106 48 GLY A O 390 N N . GLY A 49 ? 0.1494 0.1649 0.1481 0.0304 0.0028 0.0249 49 GLY A N 391 C CA . GLY A 49 ? 0.1370 0.1496 0.1348 0.0281 0.0043 0.0287 49 GLY A CA 392 C C . GLY A 49 ? 0.1573 0.1586 0.1090 0.0255 -0.0025 0.0257 49 GLY A C 393 O O . GLY A 49 ? 0.1507 0.1835 0.1378 0.0308 -0.0079 -0.0005 49 GLY A O 394 N N . ILE A 50 ? 0.1296 0.1372 0.1204 0.0225 -0.0076 0.0202 50 ILE A N 395 C CA . ILE A 50 ? 0.1388 0.1290 0.1471 0.0189 0.0103 0.0103 50 ILE A CA 396 C C . ILE A 50 ? 0.1373 0.1480 0.1517 0.0240 -0.0090 0.0118 50 ILE A C 397 O O . ILE A 50 ? 0.1286 0.2034 0.1576 0.0315 -0.0147 0.0072 50 ILE A O 398 C CB . ILE A 50 ? 0.1500 0.1744 0.1548 0.0337 -0.0007 0.0158 50 ILE A CB 399 C CG1 . ILE A 50 ? 0.1463 0.2360 0.1417 0.0355 0.0043 0.0359 50 ILE A CG1 400 C CG2 . ILE A 50 ? 0.2009 0.1742 0.1656 0.0538 -0.0159 0.0037 50 ILE A CG2 401 C CD1 . ILE A 50 ? 0.1808 0.2733 0.1667 0.0608 -0.0040 0.0449 50 ILE A CD1 402 N N . GLY A 51 ? 0.1369 0.1495 0.1728 0.0193 -0.0117 0.0311 51 GLY A N 403 C CA . GLY A 51 ? 0.1534 0.1597 0.1711 0.0182 -0.0062 0.0192 51 GLY A CA 404 C C . GLY A 51 ? 0.1570 0.1745 0.1887 0.0188 -0.0112 0.0259 51 GLY A C 405 O O . GLY A 51 ? 0.2647 0.1787 0.1831 0.0414 0.0392 0.0435 51 GLY A O 406 N N . GLY A 52 ? 0.1657 0.1673 0.1591 0.0241 -0.0147 0.0113 52 GLY A N 407 C CA . GLY A 52 ? 0.1764 0.2319 0.1656 0.0119 -0.0157 -0.0011 52 GLY A CA 408 C C . GLY A 52 ? 0.1378 0.1630 0.1340 0.0072 -0.0157 0.0096 52 GLY A C 409 O O . GLY A 52 ? 0.1790 0.1917 0.1362 0.0484 -0.0105 0.0274 52 GLY A O 410 N N . PHE A 53 ? 0.1501 0.1693 0.1125 0.0073 -0.0253 0.0048 53 PHE A N 411 C CA . PHE A 53 ? 0.1484 0.1388 0.1152 0.0016 0.0025 -0.0043 53 PHE A CA 412 C C . PHE A 53 ? 0.1625 0.1361 0.1123 0.0144 0.0111 0.0000 53 PHE A C 413 O O . PHE A 53 ? 0.1673 0.1554 0.1492 0.0032 -0.0279 0.0185 53 PHE A O 414 C CB . PHE A 53 ? 0.2004 0.1620 0.1426 0.0038 -0.0264 -0.0405 53 PHE A CB 415 C CG . PHE A 53 ? 0.2196 0.1904 0.1413 0.0080 -0.0434 -0.0286 53 PHE A CG 416 C CD1 . PHE A 53 ? 0.2140 0.2096 0.1708 -0.0295 -0.0405 -0.0103 53 PHE A CD1 417 C CD2 . PHE A 53 ? 0.2390 0.1834 0.1729 0.0186 -0.0457 -0.0374 53 PHE A CD2 418 C CE1 . PHE A 53 ? 0.2438 0.2455 0.2012 -0.0157 -0.0942 -0.0101 53 PHE A CE1 419 C CE2 . PHE A 53 ? 0.2767 0.1829 0.2534 0.0135 -0.0385 -0.0288 53 PHE A CE2 420 C CZ . PHE A 53 ? 0.2828 0.1837 0.2306 -0.0412 -0.0834 -0.0298 53 PHE A CZ 421 N N . ILE A 54 ? 0.1450 0.1336 0.1273 0.0099 -0.0098 -0.0050 54 ILE A N 422 C CA . ILE A 54 ? 0.1300 0.1547 0.1244 0.0095 -0.0044 -0.0057 54 ILE A CA 423 C C . ILE A 54 ? 0.1431 0.1456 0.1265 0.0136 -0.0052 0.0084 54 ILE A C 424 O O . ILE A 54 ? 0.1458 0.1511 0.1502 0.0104 0.0170 -0.0160 54 ILE A O 425 C CB . ILE A 54 ? 0.1440 0.1225 0.1489 0.0043 -0.0041 -0.0052 54 ILE A CB 426 C CG1 . ILE A 54 ? 0.1374 0.1572 0.1154 -0.0062 0.0199 -0.0071 54 ILE A CG1 427 C CG2 . ILE A 54 ? 0.1735 0.1436 0.1460 0.0188 0.0189 0.0011 54 ILE A CG2 428 C CD1 . ILE A 54 ? 0.1328 0.1659 0.1361 -0.0020 0.0062 -0.0029 54 ILE A CD1 429 N N . LYS A 55 ? 0.1455 0.1484 0.1197 0.0111 0.0141 0.0167 55 LYS A N 430 C CA . LYS A 55 ? 0.1477 0.1615 0.1381 0.0113 -0.0004 0.0044 55 LYS A CA 431 C C . LYS A 55 ? 0.1531 0.1563 0.1192 0.0095 0.0083 0.0009 55 LYS A C 432 O O . LYS A 55 ? 0.1812 0.1717 0.1433 0.0096 -0.0205 -0.0029 55 LYS A O 433 C CB . LYS A 55 ? 0.1578 0.1748 0.1459 0.0085 -0.0027 0.0118 55 LYS A CB 434 C CG . LYS A 55 ? 0.1854 0.2453 0.1509 0.0131 -0.0034 0.0154 55 LYS A CG 435 C CD . LYS A 55 ? 0.2581 0.2797 0.1693 0.0273 0.0446 0.0180 55 LYS A CD 436 C CE . LYS A 55 ? 0.2747 0.3413 0.2186 0.0032 0.0803 0.0633 55 LYS A CE 437 N NZ . LYS A 55 ? 0.3868 0.4362 0.2630 -0.0201 0.1414 0.0732 55 LYS A NZ 438 N N . VAL A 56 ? 0.1476 0.1614 0.1270 0.0101 0.0045 -0.0068 56 VAL A N 439 C CA . VAL A 56 ? 0.1299 0.1617 0.1388 0.0088 -0.0148 0.0110 56 VAL A CA 440 C C . VAL A 56 ? 0.1661 0.1804 0.1700 0.0011 -0.0018 -0.0138 56 VAL A C 441 O O . VAL A 56 ? 0.1550 0.2213 0.1771 0.0238 0.0073 -0.0060 56 VAL A O 442 C CB . VAL A 56 ? 0.1421 0.1879 0.1325 0.0114 0.0109 0.0090 56 VAL A CB 443 C CG1 . VAL A 56 ? 0.1457 0.1976 0.1613 -0.0127 0.0208 0.0298 56 VAL A CG1 444 C CG2 . VAL A 56 ? 0.1665 0.1940 0.1556 -0.0030 0.0229 0.0341 56 VAL A CG2 445 N N . ARG A 57 ? 0.1395 0.1856 0.1445 0.0033 0.0107 0.0041 57 ARG A N 446 C CA . ARG A 57 ? 0.1269 0.2070 0.1426 0.0139 0.0019 0.0139 57 ARG A CA 447 C C . ARG A 57 ? 0.1198 0.1999 0.1802 0.0070 0.0200 0.0123 57 ARG A C 448 O O . ARG A 57 ? 0.1460 0.1904 0.1669 0.0124 0.0369 0.0207 57 ARG A O 449 C CB . ARG A 57 ? 0.1337 0.2270 0.1719 0.0171 0.0315 0.0248 57 ARG A CB 450 C CG . ARG A 57 ? 0.1889 0.2382 0.1885 -0.0102 0.0195 0.0240 57 ARG A CG 451 C CD . ARG A 57 ? 0.1991 0.2607 0.2594 -0.0237 0.0191 -0.0027 57 ARG A CD 452 N NE . ARG A 57 ? 0.2435 0.3179 0.2663 -0.0381 0.0496 0.0424 57 ARG A NE 453 C CZ . ARG A 57 ? 0.2648 0.3669 0.2797 -0.0268 0.0143 0.0246 57 ARG A CZ 454 N NH1 . ARG A 57 ? 0.3640 0.3690 0.4385 0.0044 0.0028 0.0393 57 ARG A NH1 455 N NH2 . ARG A 57 ? 0.2678 0.4236 0.2872 -0.1085 0.0008 0.0012 57 ARG A NH2 456 N N . GLN A 58 ? 0.1525 0.1998 0.1682 0.0227 0.0361 0.0211 58 GLN A N 457 C CA . GLN A 58 ? 0.1477 0.2142 0.1976 0.0342 0.0399 0.0307 58 GLN A CA 458 C C . GLN A 58 ? 0.1545 0.2255 0.2324 0.0383 0.0564 0.0313 58 GLN A C 459 O O . GLN A 58 ? 0.1737 0.2409 0.2022 0.0513 0.0534 0.0318 58 GLN A O 460 C CB . GLN A 58 ? 0.1680 0.2101 0.2287 0.0316 0.0532 -0.0043 58 GLN A CB 461 C CG . GLN A 58 ? 0.2153 0.2334 0.2747 0.0347 0.0998 0.0027 58 GLN A CG 462 C CD . GLN A 58 ? 0.2754 0.2293 0.3505 0.0223 0.0025 -0.0001 58 GLN A CD 463 O OE1 . GLN A 58 ? 0.3481 0.2479 0.4726 0.0131 -0.0512 -0.0123 58 GLN A OE1 464 N NE2 . GLN A 58 ? 0.4402 0.2282 0.4262 0.0216 0.0572 0.0076 58 GLN A NE2 465 N N . TYR A 59 ? 0.1315 0.1914 0.2452 0.0416 0.0588 0.0277 59 TYR A N 466 C CA . TYR A 59 ? 0.1497 0.2301 0.1978 0.0181 0.0537 0.0525 59 TYR A CA 467 C C . TYR A 59 ? 0.1473 0.2222 0.2450 0.0505 0.0482 0.0363 59 TYR A C 468 O O . TYR A 59 ? 0.1592 0.2237 0.2801 0.0587 0.0704 0.0756 59 TYR A O 469 C CB . TYR A 59 ? 0.1145 0.2578 0.1916 0.0626 0.0259 0.0514 59 TYR A CB 470 C CG . TYR A 59 ? 0.1569 0.2338 0.2069 0.0246 0.0328 0.0513 59 TYR A CG 471 C CD1 . TYR A 59 ? 0.1718 0.2262 0.2122 0.0238 0.0230 0.0223 59 TYR A CD1 472 C CD2 . TYR A 59 ? 0.1641 0.2626 0.2020 -0.0014 0.0141 0.0248 59 TYR A CD2 473 C CE1 . TYR A 59 ? 0.2000 0.2106 0.2282 0.0264 0.0059 0.0341 59 TYR A CE1 474 C CE2 . TYR A 59 ? 0.1846 0.2654 0.2265 -0.0422 0.0166 0.0060 59 TYR A CE2 475 C CZ . TYR A 59 ? 0.2628 0.2418 0.2118 -0.0370 0.0045 0.0554 59 TYR A CZ 476 O OH . TYR A 59 ? 0.3455 0.2541 0.3019 -0.1056 -0.0307 0.0716 59 TYR A OH 477 N N . ASP A 60 ? 0.1948 0.2379 0.2982 0.0552 0.0701 0.0464 60 ASP A N 478 C CA . ASP A 60 ? 0.2053 0.2252 0.2955 0.0407 0.0473 0.0164 60 ASP A CA 479 C C . ASP A 60 ? 0.1810 0.2557 0.2546 0.0388 0.0786 0.0309 60 ASP A C 480 O O . ASP A 60 ? 0.1959 0.2468 0.3510 0.0556 0.0732 0.0842 60 ASP A O 481 C CB . ASP A 60 ? 0.2777 0.2668 0.3110 0.0436 0.0436 -0.0007 60 ASP A CB 482 C CG . ASP A 60 ? 0.3115 0.3389 0.3796 0.0704 0.0091 0.0184 60 ASP A CG 483 O OD1 . ASP A 60 ? 0.3533 0.3325 0.3502 0.1389 0.0248 -0.0183 60 ASP A OD1 484 O OD2 . ASP A 60 ? 0.4194 0.4553 0.4249 0.0479 0.0605 -0.0242 60 ASP A OD2 485 N N . GLN A 61 ? 0.2050 0.2175 0.2711 0.0696 0.0691 0.0319 61 GLN A N 486 C CA . GLN A 61 ? 0.1986 0.2824 0.2858 0.0401 0.0289 0.0124 61 GLN A CA 487 C C . GLN A 61 ? 0.1415 0.2256 0.2334 0.0532 0.0353 0.0219 61 GLN A C 488 O O . GLN A 61 ? 0.1910 0.2683 0.3635 0.0503 0.0309 0.0552 61 GLN A O 489 C CB . GLN A 61 ? 0.2260 0.2881 0.3269 0.0814 0.0238 0.0264 61 GLN A CB 490 C CG . GLN A 61 ? 0.3298 0.2129 0.3056 0.0402 -0.0101 -0.0391 61 GLN A CG 491 C CD . GLN A 61 ? 0.3254 0.2547 0.2208 0.0664 -0.0062 -0.0031 61 GLN A CD 492 O OE1 . GLN A 61 ? 0.4576 0.3457 0.2728 0.0497 -0.0432 -0.0362 61 GLN A OE1 493 N NE2 . GLN A 61 ? 0.2893 0.2309 0.2805 0.0051 0.0098 0.0221 61 GLN A NE2 494 N N . ILE A 62 ? 0.1804 0.2208 0.2397 0.0287 0.0338 0.0515 62 ILE A N 495 C CA . ILE A 62 ? 0.1095 0.2098 0.2431 0.0417 0.0120 0.0412 62 ILE A CA 496 C C . ILE A 62 ? 0.1376 0.2450 0.2414 0.0358 0.0081 0.0540 62 ILE A C 497 O O . ILE A 62 ? 0.1089 0.1988 0.2783 0.0151 0.0150 0.0689 62 ILE A O 498 C CB . ILE A 62 ? 0.1866 0.1865 0.2886 0.0379 0.0104 0.0470 62 ILE A CB 499 C CG1 . ILE A 62 ? 0.1732 0.2413 0.3019 0.0293 0.0374 0.0551 62 ILE A CG1 500 C CG2 . ILE A 62 ? 0.1450 0.2118 0.2685 0.0367 0.0054 0.0782 62 ILE A CG2 501 C CD1 . ILE A 62 ? 0.1538 0.3163 0.3316 0.0395 0.0384 0.1066 62 ILE A CD1 502 N N . PRO A 63 ? 0.1296 0.2299 0.2831 0.0010 -0.0028 0.0677 63 PRO A N 503 C CA . PRO A 63 ? 0.1263 0.2326 0.2999 0.0385 -0.0220 0.0474 63 PRO A CA 504 C C . PRO A 63 ? 0.1594 0.2219 0.2695 -0.0249 -0.0125 0.0313 63 PRO A C 505 O O . PRO A 63 ? 0.1474 0.2041 0.3375 -0.0019 -0.0275 0.0701 63 PRO A O 506 C CB . PRO A 63 ? 0.1931 0.2264 0.2822 0.0226 -0.0493 0.0732 63 PRO A CB 507 C CG . PRO A 63 ? 0.1910 0.2433 0.2781 -0.0132 -0.0267 0.0552 63 PRO A CG 508 C CD . PRO A 63 ? 0.1505 0.2482 0.2392 0.0276 0.0283 0.0657 63 PRO A CD 509 N N . VAL A 64 ? 0.1407 0.2183 0.2757 0.0120 -0.0235 0.0584 64 VAL A N 510 C CA . VAL A 64 ? 0.1567 0.1881 0.2198 -0.0361 -0.0292 0.0338 64 VAL A CA 511 C C . VAL A 64 ? 0.1473 0.2305 0.2615 -0.0053 -0.0517 0.0597 64 VAL A C 512 O O . VAL A 64 ? 0.2099 0.2069 0.2444 -0.0501 -0.0150 0.0534 64 VAL A O 513 C CB . VAL A 64 ? 0.1446 0.2058 0.2540 -0.0028 -0.0363 0.0573 64 VAL A CB 514 C CG1 . VAL A 64 ? 0.1778 0.2264 0.2165 -0.0400 -0.0293 0.0498 64 VAL A CG1 515 C CG2 . VAL A 64 ? 0.1586 0.1806 0.2662 -0.0122 -0.0316 0.0839 64 VAL A CG2 516 N N . GLU A 65 ? 0.1895 0.1810 0.2793 -0.0053 -0.0632 0.0526 65 GLU A N 517 C CA . GLU A 65 ? 0.1878 0.2032 0.2837 -0.0455 -0.0810 0.0182 65 GLU A CA 518 C C . GLU A 65 ? 0.2115 0.1897 0.2577 -0.0228 -0.0755 0.0444 65 GLU A C 519 O O . GLU A 65 ? 0.2415 0.1790 0.3803 -0.0366 -0.0820 0.0512 65 GLU A O 520 C CB . GLU A 65 ? 0.2395 0.2306 0.3310 -0.0221 -0.1071 0.0437 65 GLU A CB 521 C CG . GLU A 65 ? 0.2579 0.3113 0.2921 -0.0119 -0.0542 -0.0120 65 GLU A CG 522 C CD . GLU A 65 ? 0.3327 0.4856 0.3974 0.0093 -0.0945 0.0165 65 GLU A CD 523 O OE1 . GLU A 65 ? 0.5567 0.5494 0.4264 0.0571 -0.1078 0.0352 65 GLU A OE1 524 O OE2 . GLU A 65 ? 0.2792 0.5292 0.4239 -0.0542 -0.1478 0.0861 65 GLU A OE2 525 N N . ILE A 66 ? 0.2169 0.1459 0.2719 -0.0259 -0.0684 0.0199 66 ILE A N 526 C CA . ILE A 66 ? 0.2245 0.1623 0.2852 -0.0251 -0.0479 0.0049 66 ILE A CA 527 C C . ILE A 66 ? 0.2320 0.1958 0.2696 -0.0223 -0.0486 -0.0146 66 ILE A C 528 O O . ILE A 66 ? 0.2651 0.2193 0.2336 -0.0333 -0.0582 0.0207 66 ILE A O 529 C CB . ILE A 66 ? 0.2029 0.1492 0.2733 -0.0313 -0.0447 0.0015 66 ILE A CB 530 C CG1 . ILE A 66 ? 0.2250 0.1695 0.2635 -0.0178 -0.0359 0.0149 66 ILE A CG1 531 C CG2 . ILE A 66 ? 0.2045 0.1949 0.3168 -0.0266 -0.0514 0.0173 66 ILE A CG2 532 C CD1 . ILE A 66 ? 0.2275 0.2567 0.2252 -0.0149 -0.0882 0.0255 66 ILE A CD1 533 N N . CYS A 67 ? 0.3108 0.1930 0.3027 -0.0252 -0.0356 -0.0193 67 CYS A N 534 C CA . CYS A 67 ? 0.3519 0.2883 0.3078 -0.0146 -0.0438 -0.0372 67 CYS A CA 535 C C . CYS A 67 ? 0.3678 0.2952 0.2995 -0.0172 -0.0596 -0.0537 67 CYS A C 536 O O . CYS A 67 ? 0.4187 0.3157 0.3103 -0.0378 -0.0251 -0.0786 67 CYS A O 537 C CB . CYS A 67 ? 0.3852 0.3115 0.3111 0.0009 0.0038 -0.0124 67 CYS A CB 538 S SG . CYS A 67 ? 0.5120 0.4201 0.3940 0.0655 -0.0766 0.0399 67 CYS A SG 539 N N . GLY A 68 ? 0.3283 0.2482 0.2421 -0.0346 -0.1004 -0.0379 68 GLY A N 540 C CA . GLY A 68 ? 0.3441 0.2494 0.2687 0.0063 -0.0907 -0.0326 68 GLY A CA 541 C C . GLY A 68 ? 0.3047 0.2430 0.2899 -0.0064 -0.1122 -0.0228 68 GLY A C 542 O O . GLY A 68 ? 0.3501 0.3012 0.3082 0.0399 -0.1440 -0.0299 68 GLY A O 543 N N . HIS A 69 ? 0.2554 0.2196 0.2176 0.0008 -0.0820 -0.0178 69 HIS A N 544 C CA . HIS A 69 ? 0.2185 0.1818 0.2288 -0.0071 -0.0656 0.0372 69 HIS A CA 545 C C . HIS A 69 ? 0.2003 0.1702 0.2273 -0.0194 -0.0582 0.0107 69 HIS A C 546 O O . HIS A 69 ? 0.2667 0.1637 0.2614 0.0029 -0.0458 0.0378 69 HIS A O 547 C CB . HIS A 69 ? 0.2104 0.2055 0.2599 -0.0145 -0.0651 0.0221 69 HIS A CB 548 C CG . HIS A 69 ? 0.2297 0.3275 0.3059 -0.0062 -0.0446 0.0287 69 HIS A CG 549 N ND1 . HIS A 69 ? 0.3699 0.6956 0.5166 -0.0579 0.0703 -0.0654 69 HIS A ND1 550 C CD2 . HIS A 69 ? 0.4403 0.5767 0.3380 0.0085 0.0162 0.0252 69 HIS A CD2 551 C CE1 . HIS A 69 ? 0.4429 0.6574 0.4108 0.0154 -0.0841 -0.0026 69 HIS A CE1 552 N NE2 . HIS A 69 ? 0.3132 0.4991 0.2587 0.0577 -0.0567 0.0159 69 HIS A NE2 553 N N . LYS A 70 ? 0.2267 0.2011 0.2102 0.0199 -0.0327 0.0386 70 LYS A N 554 C CA . LYS A 70 ? 0.2256 0.1958 0.2643 0.0324 -0.0180 0.0463 70 LYS A CA 555 C C . LYS A 70 ? 0.1861 0.1901 0.2327 0.0375 -0.0013 0.0372 70 LYS A C 556 O O . LYS A 70 ? 0.2348 0.1885 0.2387 -0.0104 -0.0087 0.0477 70 LYS A O 557 C CB . LYS A 70 ? 0.2357 0.2861 0.3100 0.0505 -0.0589 0.0625 70 LYS A CB 558 C CG . LYS A 70 ? 0.2890 0.3848 0.3866 -0.0055 -0.0658 0.0477 70 LYS A CG 559 C CD . LYS A 70 ? 0.3645 0.4860 0.5031 0.0488 -0.0263 0.0419 70 LYS A CD 560 C CE . LYS A 70 ? 0.4883 0.5468 0.5334 -0.0144 -0.0380 -0.0080 70 LYS A CE 561 N NZ . LYS A 70 ? 0.5059 0.6602 0.6260 0.0229 0.0015 0.0100 70 LYS A NZ 562 N N . ALA A 71 ? 0.1526 0.1816 0.2125 -0.0025 -0.0013 0.0412 71 ALA A N 563 C CA . ALA A 71 ? 0.1437 0.1644 0.2187 0.0225 0.0213 0.0244 71 ALA A CA 564 C C . ALA A 71 ? 0.1448 0.1589 0.2046 0.0227 0.0091 0.0446 71 ALA A C 565 O O . ALA A 71 ? 0.1453 0.1754 0.3005 0.0211 0.0122 0.0551 71 ALA A O 566 C CB . ALA A 71 ? 0.1541 0.1511 0.2078 0.0313 0.0016 0.0237 71 ALA A CB 567 N N . ILE A 72 ? 0.1640 0.1463 0.2285 0.0379 0.0373 0.0368 72 ILE A N 568 C CA . ILE A 72 ? 0.1696 0.1547 0.2318 0.0491 0.0426 0.0406 72 ILE A CA 569 C C . ILE A 72 ? 0.1446 0.1945 0.2284 0.0394 0.0283 0.0386 72 ILE A C 570 O O . ILE A 72 ? 0.1839 0.1647 0.2561 0.0251 0.0561 0.0394 72 ILE A O 571 C CB . ILE A 72 ? 0.1748 0.1757 0.2433 0.0326 0.0273 0.0421 72 ILE A CB 572 C CG1 . ILE A 72 ? 0.1573 0.1803 0.2282 0.0346 0.0305 0.0384 72 ILE A CG1 573 C CG2 . ILE A 72 ? 0.1733 0.2014 0.2542 0.0336 0.0490 0.0367 72 ILE A CG2 574 C CD1 . ILE A 72 ? 0.1787 0.1740 0.2998 0.0416 0.0299 0.0046 72 ILE A CD1 575 N N . GLY A 73 ? 0.1685 0.1570 0.2206 0.0414 0.0470 0.0460 73 GLY A N 576 C CA . GLY A 73 ? 0.1585 0.1593 0.2533 0.0307 0.0409 0.0257 73 GLY A CA 577 C C . GLY A 73 ? 0.1647 0.1592 0.1884 0.0019 0.0403 0.0348 73 GLY A C 578 O O . GLY A 73 ? 0.1287 0.1821 0.2688 0.0349 0.0216 0.0476 73 GLY A O 579 N N . THR A 74 ? 0.1509 0.1708 0.2281 0.0283 0.0290 0.0389 74 THR A N 580 C CA . THR A 74 ? 0.1360 0.1669 0.2065 0.0214 0.0459 0.0383 74 THR A CA 581 C C . THR A 74 ? 0.1793 0.1506 0.1763 0.0440 0.0372 0.0368 74 THR A C 582 O O . THR A 74 ? 0.1376 0.1587 0.2011 0.0167 0.0530 0.0240 74 THR A O 583 C CB . THR A 74 ? 0.1977 0.1815 0.2234 0.0448 0.0364 0.0025 74 THR A CB 584 O OG1 . THR A 74 ? 0.2522 0.2034 0.3113 0.0771 0.0353 -0.0153 74 THR A OG1 585 C CG2 . THR A 74 ? 0.1761 0.2080 0.2457 0.0340 0.0269 0.0045 74 THR A CG2 586 N N . VAL A 75 ? 0.1249 0.1481 0.1992 0.0387 0.0452 0.0435 75 VAL A N 587 C CA . VAL A 75 ? 0.1333 0.1670 0.1885 0.0106 0.0438 0.0341 75 VAL A CA 588 C C . VAL A 75 ? 0.1213 0.1529 0.1780 0.0228 0.0412 0.0397 75 VAL A C 589 O O . VAL A 75 ? 0.1276 0.1907 0.1976 0.0416 0.0447 0.0454 75 VAL A O 590 C CB . VAL A 75 ? 0.1753 0.1671 0.2022 0.0036 0.0167 0.0337 75 VAL A CB 591 C CG1 . VAL A 75 ? 0.1519 0.2002 0.1763 0.0096 0.0081 0.0207 75 VAL A CG1 592 C CG2 . VAL A 75 ? 0.1713 0.1999 0.2128 0.0238 -0.0056 0.0326 75 VAL A CG2 593 N N . LEU A 76 ? 0.1119 0.1636 0.1660 0.0089 0.0216 0.0260 76 LEU A N 594 C CA . LEU A 76 ? 0.1164 0.1543 0.1729 0.0115 0.0282 0.0199 76 LEU A CA 595 C C . LEU A 76 ? 0.1058 0.1565 0.1547 0.0171 0.0209 0.0164 76 LEU A C 596 O O . LEU A 76 ? 0.1636 0.1708 0.1864 -0.0185 0.0610 0.0035 76 LEU A O 597 C CB . LEU A 76 ? 0.1392 0.1577 0.1491 0.0205 0.0124 0.0217 76 LEU A CB 598 C CG . LEU A 76 ? 0.1385 0.1635 0.1554 0.0242 0.0317 0.0113 76 LEU A CG 599 C CD1 . LEU A 76 ? 0.1378 0.1775 0.1839 0.0114 0.0406 0.0031 76 LEU A CD1 600 C CD2 . LEU A 76 ? 0.1533 0.1586 0.1990 0.0134 0.0249 -0.0126 76 LEU A CD2 601 N N . VAL A 77 ? 0.1228 0.1522 0.1468 0.0105 0.0148 0.0351 77 VAL A N 602 C CA . VAL A 77 ? 0.1241 0.1609 0.1615 -0.0066 -0.0004 0.0428 77 VAL A CA 603 C C . VAL A 77 ? 0.1332 0.1490 0.1493 -0.0237 0.0051 0.0353 77 VAL A C 604 O O . VAL A 77 ? 0.1484 0.1640 0.1518 -0.0114 0.0072 0.0271 77 VAL A O 605 C CB . VAL A 77 ? 0.1389 0.2286 0.1520 -0.0175 -0.0049 0.0298 77 VAL A CB 606 C CG1 . VAL A 77 ? 0.1285 0.2498 0.2036 -0.0311 -0.0229 0.0233 77 VAL A CG1 607 C CG2 . VAL A 77 ? 0.1344 0.2584 0.2177 0.0254 0.0105 0.0371 77 VAL A CG2 608 N N . GLY A 78 ? 0.1592 0.1415 0.1341 -0.0105 -0.0092 0.0325 78 GLY A N 609 C CA . GLY A 78 ? 0.1880 0.1633 0.1548 -0.0174 -0.0159 0.0294 78 GLY A CA 610 C C . GLY A 78 ? 0.1929 0.1322 0.1471 -0.0131 -0.0015 0.0229 78 GLY A C 611 O O . GLY A 78 ? 0.1903 0.1571 0.1571 0.0055 -0.0180 0.0182 78 GLY A O 612 N N . PRO A 79 ? 0.1864 0.1434 0.1639 0.0001 -0.0231 0.0243 79 PRO A N 613 C CA . PRO A 79 ? 0.2109 0.1251 0.1763 0.0171 -0.0574 0.0066 79 PRO A CA 614 C C . PRO A 79 ? 0.1896 0.1766 0.1545 0.0267 -0.0432 -0.0183 79 PRO A C 615 O O . PRO A 79 ? 0.2303 0.2755 0.1940 0.0287 -0.0426 0.0003 79 PRO A O 616 C CB . PRO A 79 ? 0.2437 0.1349 0.1899 -0.0054 -0.0526 0.0261 79 PRO A CB 617 C CG . PRO A 79 ? 0.2256 0.1494 0.1868 0.0047 -0.0306 0.0321 79 PRO A CG 618 C CD . PRO A 79 ? 0.2003 0.1685 0.1670 -0.0098 -0.0294 0.0188 79 PRO A CD 619 N N . THR A 80 ? 0.2189 0.2404 0.2224 -0.0213 -0.0710 0.0613 80 THR A N 620 C CA . THR A 80 ? 0.1967 0.1995 0.2153 -0.0342 -0.0623 0.0542 80 THR A CA 621 C C . THR A 80 ? 0.2033 0.1396 0.2330 -0.0183 -0.0475 0.0740 80 THR A C 622 O O . THR A 80 ? 0.2331 0.1893 0.2704 -0.0548 -0.0769 0.0768 80 THR A O 623 C CB . THR A 80 ? 0.1815 0.1859 0.1949 -0.0164 -0.0440 0.0323 80 THR A CB 624 O OG1 . THR A 80 ? 0.1843 0.1877 0.1978 -0.0327 -0.0349 0.0306 80 THR A OG1 625 C CG2 . THR A 80 ? 0.1687 0.1791 0.1534 -0.0067 -0.0377 0.0383 80 THR A CG2 626 N N . PRO A 81 ? 0.2219 0.1652 0.2326 -0.0015 -0.0642 0.0417 81 PRO A N 627 C CA . PRO A 81 ? 0.2202 0.1453 0.2381 -0.0123 -0.0486 0.0541 81 PRO A CA 628 C C . PRO A 81 ? 0.1867 0.1305 0.2373 -0.0243 -0.0474 0.0535 81 PRO A C 629 O O . PRO A 81 ? 0.2260 0.1385 0.2965 -0.0253 -0.0654 0.0229 81 PRO A O 630 C CB . PRO A 81 ? 0.2353 0.1974 0.2876 -0.0068 -0.0634 0.0550 81 PRO A CB 631 C CG . PRO A 81 ? 0.2097 0.2410 0.3533 -0.0172 -0.0593 -0.0408 81 PRO A CG 632 C CD . PRO A 81 ? 0.2007 0.2004 0.2913 -0.0202 -0.0663 0.0028 81 PRO A CD 633 N N A VAL A 82 ? 0.1703 0.1284 0.2456 -0.0209 -0.0254 0.0582 82 VAL A N 634 N N B VAL A 82 ? 0.1880 0.1219 0.2176 -0.0281 -0.0198 0.0724 82 VAL A N 635 C CA A VAL A 82 ? 0.2095 0.1661 0.2177 0.0117 0.0071 0.0451 82 VAL A CA 636 C CA B VAL A 82 ? 0.1945 0.1246 0.1970 0.0000 0.0036 0.0427 82 VAL A CA 637 C C A VAL A 82 ? 0.1745 0.1365 0.1663 -0.0132 -0.0129 0.0384 82 VAL A C 638 C C B VAL A 82 ? 0.1667 0.1158 0.1514 -0.0158 -0.0127 0.0264 82 VAL A C 639 O O A VAL A 82 ? 0.2053 0.1455 0.1673 -0.0130 -0.0232 0.0584 82 VAL A O 640 O O B VAL A 82 ? 0.1612 0.1286 0.1601 -0.0185 -0.0220 0.0327 82 VAL A O 641 C CB A VAL A 82 ? 0.2262 0.2204 0.2730 0.0208 0.0158 0.0317 82 VAL A CB 642 C CB B VAL A 82 ? 0.1933 0.1087 0.2087 0.0149 -0.0154 0.0258 82 VAL A CB 643 C CG1 A VAL A 82 ? 0.2427 0.2758 0.2631 0.0609 0.0153 0.0177 82 VAL A CG1 644 C CG1 B VAL A 82 ? 0.1863 0.0865 0.2357 -0.0021 0.0130 0.0018 82 VAL A CG1 645 C CG2 A VAL A 82 ? 0.2749 0.2567 0.2795 0.0597 0.0456 0.0393 82 VAL A CG2 646 C CG2 B VAL A 82 ? 0.2644 0.1830 0.2228 0.0212 -0.0090 -0.0447 82 VAL A CG2 647 N N . ASN A 83 ? 0.1625 0.1405 0.1616 -0.0199 -0.0222 0.0202 83 ASN A N 648 C CA . ASN A 83 ? 0.1259 0.1146 0.1462 0.0014 -0.0090 0.0233 83 ASN A CA 649 C C . ASN A 83 ? 0.1305 0.1189 0.1138 0.0011 -0.0080 0.0229 83 ASN A C 650 O O . ASN A 83 ? 0.1615 0.1343 0.1175 -0.0176 -0.0070 0.0010 83 ASN A O 651 C CB . ASN A 83 ? 0.1470 0.1442 0.1553 -0.0156 -0.0112 0.0157 83 ASN A CB 652 C CG . ASN A 83 ? 0.1621 0.1357 0.1887 -0.0019 -0.0020 0.0034 83 ASN A CG 653 O OD1 . ASN A 83 ? 0.1963 0.1765 0.1917 -0.0585 0.0084 0.0164 83 ASN A OD1 654 N ND2 . ASN A 83 ? 0.1718 0.1601 0.2200 -0.0232 -0.0440 0.0201 83 ASN A ND2 655 N N . ILE A 84 ? 0.1313 0.1148 0.1229 0.0035 -0.0074 0.0109 84 ILE A N 656 C CA . ILE A 84 ? 0.1207 0.1142 0.1144 0.0032 0.0100 0.0077 84 ILE A CA 657 C C . ILE A 84 ? 0.1156 0.1055 0.1306 0.0028 -0.0069 -0.0012 84 ILE A C 658 O O . ILE A 84 ? 0.1407 0.1239 0.1212 0.0113 0.0051 0.0164 84 ILE A O 659 C CB . ILE A 84 ? 0.1234 0.1202 0.1246 -0.0026 0.0007 0.0043 84 ILE A CB 660 C CG1 . ILE A 84 ? 0.1488 0.1501 0.1362 0.0000 0.0004 -0.0053 84 ILE A CG1 661 C CG2 . ILE A 84 ? 0.1258 0.1325 0.1337 0.0067 -0.0089 0.0003 84 ILE A CG2 662 C CD1 . ILE A 84 ? 0.1527 0.1651 0.1143 0.0005 -0.0038 0.0198 84 ILE A CD1 663 N N . ILE A 85 ? 0.1197 0.1056 0.1219 -0.0008 0.0000 0.0075 85 ILE A N 664 C CA . ILE A 85 ? 0.1212 0.1079 0.1263 0.0084 0.0030 0.0093 85 ILE A CA 665 C C . ILE A 85 ? 0.1078 0.1029 0.1149 0.0082 -0.0007 0.0031 85 ILE A C 666 O O . ILE A 85 ? 0.1228 0.1281 0.1211 0.0087 -0.0024 -0.0041 85 ILE A O 667 C CB . ILE A 85 ? 0.1178 0.1266 0.1359 -0.0027 -0.0198 0.0066 85 ILE A CB 668 C CG1 . ILE A 85 ? 0.1551 0.1401 0.1481 -0.0115 -0.0225 0.0297 85 ILE A CG1 669 C CG2 . ILE A 85 ? 0.1504 0.1467 0.1254 0.0058 -0.0359 0.0120 85 ILE A CG2 670 C CD1 . ILE A 85 ? 0.1549 0.1694 0.1783 -0.0172 -0.0303 0.0067 85 ILE A CD1 671 N N . GLY A 86 ? 0.1194 0.1061 0.1005 0.0017 0.0072 0.0069 86 GLY A N 672 C CA . GLY A 86 ? 0.1171 0.1046 0.1014 0.0021 -0.0025 0.0073 86 GLY A CA 673 C C . GLY A 86 ? 0.1154 0.1105 0.0979 0.0214 -0.0033 0.0070 86 GLY A C 674 O O . GLY A 86 ? 0.1129 0.1152 0.1099 0.0074 -0.0032 0.0019 86 GLY A O 675 N N . ARG A 87 ? 0.1132 0.1004 0.0909 0.0041 -0.0060 0.0065 87 ARG A N 676 C CA . ARG A 87 ? 0.1113 0.1003 0.1173 0.0034 -0.0027 -0.0001 87 ARG A CA 677 C C . ARG A 87 ? 0.1241 0.1088 0.1168 0.0074 -0.0022 0.0105 87 ARG A C 678 O O . ARG A 87 ? 0.1349 0.1121 0.1226 0.0088 -0.0064 0.0104 87 ARG A O 679 C CB . ARG A 87 ? 0.1181 0.1085 0.1112 0.0048 0.0141 0.0037 87 ARG A CB 680 C CG . ARG A 87 ? 0.1255 0.1003 0.1106 0.0067 -0.0008 0.0068 87 ARG A CG 681 C CD . ARG A 87 ? 0.1134 0.1182 0.1208 0.0072 -0.0023 0.0006 87 ARG A CD 682 N NE . ARG A 87 ? 0.1184 0.1174 0.1247 0.0036 -0.0027 0.0037 87 ARG A NE 683 C CZ . ARG A 87 ? 0.1270 0.1240 0.1312 -0.0013 -0.0007 0.0115 87 ARG A CZ 684 N NH1 . ARG A 87 ? 0.1464 0.1294 0.1205 0.0099 0.0052 -0.0148 87 ARG A NH1 685 N NH2 . ARG A 87 ? 0.1516 0.1376 0.1275 0.0184 -0.0030 0.0013 87 ARG A NH2 686 N N . ASN A 88 ? 0.1122 0.1155 0.1262 0.0131 0.0099 0.0001 88 ASN A N 687 C CA . ASN A 88 ? 0.1207 0.1216 0.1407 0.0034 0.0094 0.0051 88 ASN A CA 688 C C . ASN A 88 ? 0.1232 0.1152 0.1401 0.0144 0.0044 0.0158 88 ASN A C 689 O O . ASN A 88 ? 0.1296 0.1289 0.1999 0.0209 -0.0210 -0.0025 88 ASN A O 690 C CB . ASN A 88 ? 0.1172 0.1403 0.1683 0.0144 0.0295 0.0026 88 ASN A CB 691 C CG . ASN A 88 ? 0.1366 0.1400 0.1429 0.0091 0.0136 0.0074 88 ASN A CG 692 O OD1 . ASN A 88 ? 0.1284 0.1328 0.1546 0.0125 0.0112 -0.0015 88 ASN A OD1 693 N ND2 . ASN A 88 ? 0.1242 0.1409 0.1702 0.0048 0.0269 0.0273 88 ASN A ND2 694 N N . LEU A 89 ? 0.1082 0.1230 0.1385 0.0163 -0.0017 0.0006 89 LEU A N 695 C CA . LEU A 89 ? 0.1178 0.1226 0.1604 0.0043 0.0001 0.0148 89 LEU A CA 696 C C . LEU A 89 ? 0.1207 0.1007 0.1513 0.0139 -0.0029 0.0134 89 LEU A C 697 O O . LEU A 89 ? 0.1341 0.1194 0.1733 0.0081 -0.0194 0.0319 89 LEU A O 698 C CB . LEU A 89 ? 0.1206 0.1188 0.1644 -0.0032 -0.0174 0.0121 89 LEU A CB 699 C CG . LEU A 89 ? 0.1186 0.1384 0.1762 0.0019 0.0212 0.0203 89 LEU A CG 700 C CD1 . LEU A 89 ? 0.1316 0.1493 0.2148 0.0020 -0.0116 0.0402 89 LEU A CD1 701 C CD2 . LEU A 89 ? 0.1267 0.1666 0.1999 0.0199 -0.0060 0.0258 89 LEU A CD2 702 N N . LEU A 90 ? 0.1155 0.1248 0.1299 0.0240 -0.0054 0.0196 90 LEU A N 703 C CA . LEU A 90 ? 0.1235 0.1093 0.1225 0.0095 -0.0043 0.0009 90 LEU A CA 704 C C . LEU A 90 ? 0.1141 0.1335 0.1048 0.0161 0.0090 0.0139 90 LEU A C 705 O O . LEU A 90 ? 0.1365 0.1341 0.1289 0.0093 -0.0058 0.0205 90 LEU A O 706 C CB . LEU A 90 ? 0.1183 0.1121 0.1293 0.0106 0.0051 -0.0003 90 LEU A CB 707 C CG . LEU A 90 ? 0.1465 0.1170 0.1248 0.0117 -0.0001 0.0038 90 LEU A CG 708 C CD1 . LEU A 90 ? 0.1525 0.1223 0.1791 0.0279 -0.0176 -0.0054 90 LEU A CD1 709 C CD2 . LEU A 90 ? 0.1550 0.1402 0.1641 0.0102 -0.0113 -0.0032 90 LEU A CD2 710 N N . THR A 91 ? 0.1252 0.1109 0.1301 0.0102 -0.0028 0.0020 91 THR A N 711 C CA . THR A 91 ? 0.1214 0.1275 0.1439 0.0089 0.0125 0.0143 91 THR A CA 712 C C . THR A 91 ? 0.1375 0.1050 0.1327 0.0108 0.0089 0.0051 91 THR A C 713 O O . THR A 91 ? 0.1482 0.1383 0.1815 0.0133 -0.0015 0.0398 91 THR A O 714 C CB . THR A 91 ? 0.1270 0.1190 0.1656 -0.0021 -0.0009 0.0126 91 THR A CB 715 O OG1 . THR A 91 ? 0.1486 0.1518 0.1751 -0.0001 0.0148 -0.0274 91 THR A OG1 716 C CG2 . THR A 91 ? 0.1418 0.1500 0.1792 0.0040 -0.0015 -0.0038 91 THR A CG2 717 N N . GLN A 92 ? 0.1265 0.1281 0.1536 0.0171 -0.0021 0.0144 92 GLN A N 718 C CA . GLN A 92 ? 0.1264 0.1254 0.1773 0.0244 -0.0154 0.0128 92 GLN A CA 719 C C . GLN A 92 ? 0.1180 0.1527 0.1796 0.0148 -0.0276 0.0078 92 GLN A C 720 O O . GLN A 92 ? 0.1701 0.1905 0.1913 0.0500 -0.0254 0.0316 92 GLN A O 721 C CB . GLN A 92 ? 0.1188 0.1368 0.2141 0.0252 -0.0154 0.0207 92 GLN A CB 722 C CG . GLN A 92 ? 0.1644 0.1205 0.2021 0.0146 0.0043 0.0077 92 GLN A CG 723 C CD . GLN A 92 ? 0.1784 0.1280 0.1927 0.0362 0.0078 0.0180 92 GLN A CD 724 O OE1 . GLN A 92 ? 0.1431 0.1921 0.2109 0.0186 0.0092 0.0436 92 GLN A OE1 725 N NE2 . GLN A 92 ? 0.1641 0.1810 0.1874 0.0424 0.0191 0.0222 92 GLN A NE2 726 N N . ILE A 93 ? 0.1319 0.1482 0.1510 0.0073 -0.0271 0.0060 93 ILE A N 727 C CA . ILE A 93 ? 0.1496 0.1662 0.1627 -0.0002 -0.0239 0.0012 93 ILE A CA 728 C C . ILE A 93 ? 0.1735 0.1664 0.1815 0.0290 -0.0419 0.0076 93 ILE A C 729 O O . ILE A 93 ? 0.2039 0.1958 0.1821 0.0207 -0.0174 0.0264 93 ILE A O 730 C CB . ILE A 93 ? 0.1767 0.2026 0.1599 0.0000 -0.0491 -0.0061 93 ILE A CB 731 C CG1 . ILE A 93 ? 0.1779 0.1581 0.1501 -0.0048 -0.0277 -0.0046 93 ILE A CG1 732 C CG2 . ILE A 93 ? 0.1829 0.1768 0.2076 -0.0061 -0.0205 -0.0180 93 ILE A CG2 733 C CD1 . ILE A 93 ? 0.2061 0.1721 0.1909 0.0030 -0.0252 -0.0079 93 ILE A CD1 734 N N . GLY A 94 ? 0.1557 0.1596 0.1491 0.0205 -0.0094 0.0319 94 GLY A N 735 C CA . GLY A 94 ? 0.1855 0.1569 0.1690 0.0153 -0.0123 0.0499 94 GLY A CA 736 C C . GLY A 94 ? 0.2119 0.1598 0.1465 0.0311 0.0013 0.0345 94 GLY A C 737 O O . GLY A 94 ? 0.2000 0.2035 0.1775 0.0288 0.0168 0.0571 94 GLY A O 738 N N A CYS A 95 ? 0.1735 0.1682 0.1589 0.0281 0.0060 0.0349 95 CYS A N 739 N N B CYS A 95 ? 0.1639 0.1591 0.1611 0.0235 0.0040 0.0335 95 CYS A N 740 C CA A CYS A 95 ? 0.1927 0.1922 0.1240 0.0345 0.0172 0.0161 95 CYS A CA 741 C CA B CYS A 95 ? 0.1716 0.1820 0.1265 0.0422 -0.0059 0.0373 95 CYS A CA 742 C C A CYS A 95 ? 0.1885 0.1882 0.1479 0.0665 -0.0121 0.0231 95 CYS A C 743 C C B CYS A 95 ? 0.1780 0.1958 0.1542 0.0389 0.0047 0.0286 95 CYS A C 744 O O A CYS A 95 ? 0.1987 0.2486 0.1463 0.0236 0.0011 0.0245 95 CYS A O 745 O O B CYS A 95 ? 0.1892 0.2599 0.1454 0.0576 0.0064 0.0306 95 CYS A O 746 C CB A CYS A 95 ? 0.1899 0.1537 0.1610 0.0277 0.0012 0.0090 95 CYS A CB 747 C CB B CYS A 95 ? 0.1645 0.1635 0.1299 0.0107 -0.0084 0.0167 95 CYS A CB 748 S SG A CYS A 95 ? 0.2687 0.2376 0.2329 -0.0036 -0.0336 0.0159 95 CYS A SG 749 S SG B CYS A 95 ? 0.1549 0.1463 0.1365 0.0392 -0.0010 0.0094 95 CYS A SG 750 N N . THR A 96 ? 0.1860 0.2022 0.1412 0.0483 0.0091 0.0332 96 THR A N 751 C CA . THR A 96 ? 0.1925 0.1811 0.1428 0.0442 0.0261 0.0377 96 THR A CA 752 C C . THR A 96 ? 0.1891 0.1456 0.1467 0.0243 0.0121 0.0321 96 THR A C 753 O O . THR A 96 ? 0.1798 0.1931 0.1455 0.0336 -0.0082 0.0301 96 THR A O 754 C CB . THR A 96 ? 0.2142 0.2095 0.2180 0.0677 0.0130 0.0570 96 THR A CB 755 O OG1 . THR A 96 ? 0.2394 0.2420 0.1951 0.0731 0.0368 0.0943 96 THR A OG1 756 C CG2 . THR A 96 ? 0.2613 0.1981 0.2378 0.0707 0.0473 0.0553 96 THR A CG2 757 N N . LEU A 97 ? 0.1868 0.1760 0.1146 0.0266 0.0184 0.0183 97 LEU A N 758 C CA . LEU A 97 ? 0.1845 0.1731 0.1346 0.0368 0.0047 0.0369 97 LEU A CA 759 C C . LEU A 97 ? 0.2023 0.1759 0.1449 0.0425 0.0164 0.0193 97 LEU A C 760 O O . LEU A 97 ? 0.2433 0.1890 0.1529 0.0083 0.0533 0.0376 97 LEU A O 761 C CB . LEU A 97 ? 0.1612 0.1529 0.1280 0.0146 0.0104 0.0105 97 LEU A CB 762 C CG . LEU A 97 ? 0.1400 0.1418 0.1274 0.0139 0.0064 0.0158 97 LEU A CG 763 C CD1 . LEU A 97 ? 0.1517 0.2138 0.1650 0.0019 -0.0067 0.0425 97 LEU A CD1 764 C CD2 . LEU A 97 ? 0.2073 0.1879 0.1547 0.0138 0.0219 0.0259 97 LEU A CD2 765 N N . ASN A 98 ? 0.2424 0.1754 0.1331 0.0576 0.0343 0.0607 98 ASN A N 766 C CA . ASN A 98 ? 0.2273 0.2117 0.1537 0.0518 0.0459 0.0512 98 ASN A CA 767 C C . ASN A 98 ? 0.2199 0.2006 0.1705 0.0216 0.0297 0.0370 98 ASN A C 768 O O . ASN A 98 ? 0.2562 0.2420 0.1953 0.0656 0.0546 0.0521 98 ASN A O 769 C CB . ASN A 98 ? 0.2660 0.2227 0.1440 0.0767 0.0459 0.0601 98 ASN A CB 770 C CG . ASN A 98 ? 0.2633 0.2512 0.2257 0.0710 0.0540 0.0873 98 ASN A CG 771 O OD1 . ASN A 98 ? 0.3392 0.2600 0.2433 0.1024 0.0650 0.0890 98 ASN A OD1 772 N ND2 . ASN A 98 ? 0.2621 0.3228 0.1492 0.0809 0.0317 0.0462 98 ASN A ND2 773 N N . PHE A 99 ? 0.2293 0.2165 0.2483 0.0479 0.0599 0.0431 99 PHE A N 774 C CA . PHE A 99 ? 0.2316 0.2335 0.2339 0.0405 0.0542 0.0390 99 PHE A CA 775 C C . PHE A 99 ? 0.2771 0.2766 0.2988 0.0365 0.0879 0.0564 99 PHE A C 776 O O . PHE A 99 ? 0.3011 0.2778 0.3141 -0.0021 0.1157 0.0429 99 PHE A O 777 C CB . PHE A 99 ? 0.2349 0.2488 0.2805 0.0458 0.0472 0.0451 99 PHE A CB 778 C CG . PHE A 99 ? 0.2620 0.2607 0.2467 0.0389 0.0529 0.0658 99 PHE A CG 779 C CD1 . PHE A 99 ? 0.3367 0.3704 0.2518 0.0037 0.0702 0.0350 99 PHE A CD1 780 C CD2 . PHE A 99 ? 0.3101 0.3626 0.4008 -0.0401 0.0126 -0.0219 99 PHE A CD2 781 C CE1 . PHE A 99 ? 0.3344 0.3712 0.2072 0.0243 0.0608 0.0619 99 PHE A CE1 782 C CE2 . PHE A 99 ? 0.3058 0.4144 0.3080 -0.0145 0.0266 0.0407 99 PHE A CE2 783 C CZ . PHE A 99 ? 0.3638 0.4195 0.3476 -0.0004 0.0361 0.0250 99 PHE A CZ 784 O OXT . PHE A 99 ? 0.2967 0.3709 0.3152 0.0515 0.1177 0.0413 99 PHE A OXT 785 N N . PRO B 1 ? 0.3042 0.3350 0.3625 -0.0477 0.0652 0.0252 1 PRO B N 786 C CA . PRO B 1 ? 0.3384 0.3299 0.3624 -0.0425 0.0522 0.0226 1 PRO B CA 787 C C . PRO B 1 ? 0.3223 0.2955 0.2869 -0.0414 0.0900 0.0326 1 PRO B C 788 O O . PRO B 1 ? 0.3459 0.2701 0.3356 -0.0051 0.1089 0.0790 1 PRO B O 789 C CB . PRO B 1 ? 0.3716 0.3921 0.3927 -0.0391 0.0335 0.0067 1 PRO B CB 790 C CG . PRO B 1 ? 0.4015 0.4166 0.4058 -0.0198 -0.0076 -0.0175 1 PRO B CG 791 C CD . PRO B 1 ? 0.3300 0.4055 0.3690 -0.0054 0.0503 0.0177 1 PRO B CD 792 N N . GLN B 2 ? 0.3376 0.2730 0.2815 -0.0292 0.0965 0.0911 2 GLN B N 793 C CA . GLN B 2 ? 0.3099 0.2655 0.2893 0.0033 0.0833 0.0489 2 GLN B CA 794 C C . GLN B 2 ? 0.3311 0.2366 0.3007 -0.0222 0.0721 0.0386 2 GLN B C 795 O O . GLN B 2 ? 0.3552 0.2280 0.2891 -0.0216 0.1041 0.0562 2 GLN B O 796 C CB . GLN B 2 ? 0.3380 0.2907 0.2954 0.0152 0.0831 0.0655 2 GLN B CB 797 C CG . GLN B 2 ? 0.3076 0.2295 0.3414 0.0429 0.0678 0.0649 2 GLN B CG 798 C CD . GLN B 2 ? 0.3692 0.2381 0.3820 0.0860 0.0323 0.0545 2 GLN B CD 799 O OE1 . GLN B 2 ? 0.3730 0.2670 0.4265 0.0726 0.1007 0.0751 2 GLN B OE1 800 N NE2 . GLN B 2 ? 0.3960 0.2922 0.3256 0.0988 0.0268 0.1028 2 GLN B NE2 801 N N . ILE B 3 ? 0.3230 0.2038 0.2480 -0.0290 0.1141 0.0119 3 ILE B N 802 C CA . ILE B 3 ? 0.2973 0.2275 0.2373 -0.0274 0.0668 -0.0250 3 ILE B CA 803 C C . ILE B 3 ? 0.2924 0.1857 0.2080 0.0257 0.0778 -0.0143 3 ILE B C 804 O O . ILE B 3 ? 0.2756 0.2014 0.1634 0.0234 0.0657 0.0189 3 ILE B O 805 C CB . ILE B 3 ? 0.2620 0.2561 0.1940 -0.0243 0.0823 -0.0243 3 ILE B CB 806 C CG1 . ILE B 3 ? 0.2935 0.3525 0.2871 -0.0045 0.0617 -0.0032 3 ILE B CG1 807 C CG2 . ILE B 3 ? 0.3628 0.2687 0.1894 -0.0814 0.1009 0.0039 3 ILE B CG2 808 C CD1 . ILE B 3 ? 0.2452 0.3010 0.2970 0.0135 0.0532 0.0330 3 ILE B CD1 809 N N . THR B 4 ? 0.3890 0.1647 0.2398 0.0068 0.1561 0.0046 4 THR B N 810 C CA . THR B 4 ? 0.3027 0.1726 0.2670 0.0524 0.0834 0.0443 4 THR B CA 811 C C . THR B 4 ? 0.2465 0.1479 0.1618 -0.0123 0.0545 -0.0037 4 THR B C 812 O O . THR B 4 ? 0.2319 0.2372 0.1751 -0.0669 0.0417 -0.0292 4 THR B O 813 C CB . THR B 4 ? 0.2777 0.2358 0.2298 -0.0434 0.0243 -0.0381 4 THR B CB 814 O OG1 . THR B 4 ? 0.3293 0.2181 0.2926 0.0545 -0.0417 -0.0689 4 THR B OG1 815 C CG2 . THR B 4 ? 0.3049 0.1874 0.4674 -0.0354 -0.1219 -0.0573 4 THR B CG2 816 N N . LEU B 5 ? 0.1924 0.1174 0.1450 0.0049 -0.0120 -0.0069 5 LEU B N 817 C CA . LEU B 5 ? 0.1468 0.0972 0.1331 0.0028 0.0079 0.0098 5 LEU B CA 818 C C . LEU B 5 ? 0.1166 0.1139 0.1531 -0.0014 -0.0001 -0.0062 5 LEU B C 819 O O . LEU B 5 ? 0.1406 0.1156 0.1260 0.0025 -0.0002 -0.0080 5 LEU B O 820 C CB . LEU B 5 ? 0.1513 0.1157 0.1291 0.0245 -0.0110 -0.0099 5 LEU B CB 821 C CG . LEU B 5 ? 0.1514 0.1052 0.1472 0.0047 -0.0004 -0.0060 5 LEU B CG 822 C CD1 . LEU B 5 ? 0.1749 0.1282 0.1357 0.0287 -0.0122 -0.0018 5 LEU B CD1 823 C CD2 . LEU B 5 ? 0.1591 0.1387 0.1331 0.0214 0.0088 -0.0074 5 LEU B CD2 824 N N . TRP B 6 ? 0.1397 0.1184 0.1582 0.0132 0.0087 0.0000 6 TRP B N 825 C CA . TRP B 6 ? 0.1414 0.1160 0.1708 0.0261 0.0080 -0.0141 6 TRP B CA 826 C C . TRP B 6 ? 0.1413 0.1413 0.1519 0.0297 -0.0007 -0.0313 6 TRP B C 827 O O . TRP B 6 ? 0.1458 0.2165 0.1745 0.0440 0.0098 -0.0389 6 TRP B O 828 C CB . TRP B 6 ? 0.1304 0.1211 0.2000 0.0144 -0.0073 -0.0218 6 TRP B CB 829 C CG . TRP B 6 ? 0.1629 0.1183 0.1649 0.0147 0.0085 -0.0035 6 TRP B CG 830 C CD1 . TRP B 6 ? 0.2374 0.1880 0.1893 -0.0319 -0.0042 0.0073 6 TRP B CD1 831 C CD2 . TRP B 6 ? 0.1734 0.1152 0.1820 0.0148 -0.0130 0.0131 6 TRP B CD2 832 N NE1 . TRP B 6 ? 0.2824 0.1790 0.2418 -0.0437 -0.0429 0.0799 6 TRP B NE1 833 C CE2 . TRP B 6 ? 0.1913 0.1835 0.2009 0.0028 -0.0431 0.0000 6 TRP B CE2 834 C CE3 . TRP B 6 ? 0.1605 0.1487 0.2355 0.0213 0.0017 0.0045 6 TRP B CE3 835 C CZ2 . TRP B 6 ? 0.2416 0.1974 0.2261 0.0339 -0.0410 0.0088 6 TRP B CZ2 836 C CZ3 . TRP B 6 ? 0.1956 0.2190 0.2595 -0.0023 0.0004 0.0150 6 TRP B CZ3 837 C CH2 . TRP B 6 ? 0.1928 0.2060 0.2908 0.0434 -0.0205 0.0273 6 TRP B CH2 838 N N . LYS B 7 ? 0.1392 0.1242 0.1542 0.0120 0.0048 -0.0121 7 LYS B N 839 C CA . LYS B 7 ? 0.1382 0.1343 0.1437 0.0143 0.0018 -0.0323 7 LYS B CA 840 C C . LYS B 7 ? 0.1204 0.1286 0.1303 0.0050 0.0042 -0.0244 7 LYS B C 841 O O . LYS B 7 ? 0.1483 0.1216 0.1343 0.0144 -0.0045 -0.0228 7 LYS B O 842 C CB . LYS B 7 ? 0.1758 0.1355 0.1952 0.0335 -0.0207 -0.0290 7 LYS B CB 843 C CG . LYS B 7 ? 0.2540 0.1868 0.2498 0.0047 -0.0147 -0.0130 7 LYS B CG 844 C CD . LYS B 7 ? 0.2950 0.2432 0.3743 0.0107 -0.0112 -0.0274 7 LYS B CD 845 C CE . LYS B 7 ? 0.3233 0.2397 0.4419 0.0272 0.0191 -0.0138 7 LYS B CE 846 N NZ . LYS B 7 ? 0.4389 0.4117 0.5385 -0.0092 -0.0799 -0.0592 7 LYS B NZ 847 N N . ARG B 8 ? 0.1339 0.1407 0.1324 0.0077 -0.0128 -0.0232 8 ARG B N 848 C CA . ARG B 8 ? 0.1209 0.1321 0.1279 0.0141 -0.0048 -0.0279 8 ARG B CA 849 C C . ARG B 8 ? 0.1217 0.1205 0.1486 -0.0114 0.0070 -0.0197 8 ARG B C 850 O O . ARG B 8 ? 0.1356 0.1204 0.1861 -0.0025 0.0062 -0.0330 8 ARG B O 851 C CB . ARG B 8 ? 0.1534 0.1404 0.1570 0.0070 0.0003 -0.0029 8 ARG B CB 852 C CG . ARG B 8 ? 0.1602 0.1692 0.1391 -0.0047 -0.0228 -0.0038 8 ARG B CG 853 C CD . ARG B 8 ? 0.2130 0.2944 0.1252 -0.0206 -0.0010 0.0250 8 ARG B CD 854 N NE . ARG B 8 ? 0.2397 0.3729 0.1598 -0.0444 -0.0259 0.0593 8 ARG B NE 855 C CZ . ARG B 8 ? 0.2607 0.2716 0.2374 -0.0015 0.0069 0.0086 8 ARG B CZ 856 N NH1 . ARG B 8 ? 0.2366 0.3661 0.5035 0.0621 0.0008 0.2402 8 ARG B NH1 857 N NH2 . ARG B 8 ? 0.2581 0.2763 0.2126 0.0066 -0.0282 0.0092 8 ARG B NH2 858 N N . PRO B 9 ? 0.1172 0.1112 0.1261 0.0025 0.0086 -0.0043 9 PRO B N 859 C CA . PRO B 9 ? 0.1158 0.1132 0.1672 0.0095 0.0053 0.0127 9 PRO B CA 860 C C . PRO B 9 ? 0.1198 0.1151 0.1369 -0.0013 0.0171 -0.0015 9 PRO B C 861 O O . PRO B 9 ? 0.1304 0.1241 0.1590 0.0082 0.0027 -0.0090 9 PRO B O 862 C CB . PRO B 9 ? 0.1321 0.1352 0.1439 0.0194 0.0085 0.0011 9 PRO B CB 863 C CG . PRO B 9 ? 0.1266 0.1346 0.1367 0.0048 0.0010 -0.0145 9 PRO B CG 864 C CD . PRO B 9 ? 0.1161 0.1267 0.1340 -0.0054 -0.0027 -0.0352 9 PRO B CD 865 N N . LEU B 10 ? 0.1264 0.1487 0.1726 -0.0008 0.0090 -0.0250 10 LEU B N 866 C CA . LEU B 10 ? 0.1145 0.1432 0.1774 -0.0082 -0.0096 -0.0195 10 LEU B CA 867 C C . LEU B 10 ? 0.1487 0.1206 0.2336 0.0031 0.0013 0.0004 10 LEU B C 868 O O . LEU B 10 ? 0.1564 0.1395 0.2942 0.0016 0.0036 0.0104 10 LEU B O 869 C CB . LEU B 10 ? 0.1619 0.1890 0.2256 -0.0022 -0.0348 -0.0391 10 LEU B CB 870 C CG . LEU B 10 ? 0.2048 0.2834 0.1538 0.0147 -0.0140 -0.0465 10 LEU B CG 871 C CD1 . LEU B 10 ? 0.3357 0.3121 0.2283 0.0240 0.0105 -0.0664 10 LEU B CD1 872 C CD2 . LEU B 10 ? 0.2581 0.2319 0.2278 -0.0269 -0.0185 -0.0177 10 LEU B CD2 873 N N . VAL B 11 ? 0.1235 0.1382 0.1961 0.0081 0.0070 0.0159 11 VAL B N 874 C CA . VAL B 11 ? 0.1309 0.1635 0.2032 0.0080 0.0152 0.0194 11 VAL B CA 875 C C . VAL B 11 ? 0.1341 0.1697 0.2224 -0.0208 -0.0062 0.0177 11 VAL B C 876 O O . VAL B 11 ? 0.1386 0.1767 0.2340 -0.0158 -0.0064 0.0361 11 VAL B O 877 C CB . VAL B 11 ? 0.1727 0.2420 0.2018 0.0020 0.0273 0.0220 11 VAL B CB 878 C CG1 . VAL B 11 ? 0.1866 0.2580 0.2762 0.0028 -0.0176 0.0490 11 VAL B CG1 879 C CG2 . VAL B 11 ? 0.1562 0.2843 0.2614 0.0174 0.0223 -0.0510 11 VAL B CG2 880 N N . THR B 12 ? 0.1281 0.1906 0.2438 -0.0166 -0.0014 0.0456 12 THR B N 881 C CA . THR B 12 ? 0.1377 0.2226 0.2537 -0.0304 -0.0124 0.0105 12 THR B CA 882 C C . THR B 12 ? 0.1251 0.2318 0.2339 -0.0105 -0.0025 0.0135 12 THR B C 883 O O . THR B 12 ? 0.1837 0.2432 0.2637 0.0091 0.0232 0.0397 12 THR B O 884 C CB . THR B 12 ? 0.1584 0.2170 0.2994 -0.0375 0.0073 0.0271 12 THR B CB 885 O OG1 . THR B 12 ? 0.2074 0.2646 0.3240 -0.0886 -0.0136 -0.0075 12 THR B OG1 886 C CG2 . THR B 12 ? 0.1747 0.2554 0.3577 -0.0578 -0.0285 0.0131 12 THR B CG2 887 N N . ILE B 13 ? 0.1454 0.2202 0.2918 -0.0142 -0.0005 0.0148 13 ILE B N 888 C CA . ILE B 13 ? 0.1315 0.2047 0.2708 -0.0076 0.0097 0.0082 13 ILE B CA 889 C C . ILE B 13 ? 0.1846 0.2132 0.2989 -0.0377 0.0131 0.0374 13 ILE B C 890 O O . ILE B 13 ? 0.1554 0.2445 0.3606 0.0034 -0.0332 0.0267 13 ILE B O 891 C CB . ILE B 13 ? 0.1497 0.2199 0.2754 0.0289 0.0095 0.0318 13 ILE B CB 892 C CG1 . ILE B 13 ? 0.1433 0.2145 0.2726 0.0023 -0.0078 0.0127 13 ILE B CG1 893 C CG2 . ILE B 13 ? 0.1611 0.2254 0.2575 -0.0030 -0.0141 0.0410 13 ILE B CG2 894 C CD1 . ILE B 13 ? 0.2007 0.2599 0.2716 -0.0007 0.0031 0.0548 13 ILE B CD1 895 N N . ARG B 14 ? 0.1364 0.2230 0.3454 -0.0036 0.0136 0.0235 14 ARG B N 896 C CA . ARG B 14 ? 0.1511 0.2131 0.4017 -0.0137 0.0209 0.0185 14 ARG B CA 897 C C . ARG B 14 ? 0.1203 0.1720 0.2516 0.0024 0.0351 0.0518 14 ARG B C 898 O O . ARG B 14 ? 0.1755 0.2112 0.3395 0.0245 0.0284 0.0523 14 ARG B O 899 C CB . ARG B 14 ? 0.1667 0.2476 0.4631 -0.0212 0.0411 0.0412 14 ARG B CB 900 C CG . ARG B 14 ? 0.1557 0.2831 0.6043 -0.0504 0.0382 0.0626 14 ARG B CG 901 C CD . ARG B 14 ? 0.2115 0.3881 0.5376 -0.0761 0.0302 0.0697 14 ARG B CD 902 N NE . ARG B 14 ? 0.2579 0.4718 0.5380 -0.1075 0.0539 -0.0761 14 ARG B NE 903 C CZ . ARG B 14 ? 0.4391 0.6070 0.5237 0.0448 -0.0515 0.0069 14 ARG B CZ 904 N NH1 . ARG B 14 ? 0.6314 0.6785 0.6110 -0.0148 -0.0357 -0.0633 14 ARG B NH1 905 N NH2 . ARG B 14 ? 0.4309 0.5572 0.5399 -0.0029 -0.0117 0.0226 14 ARG B NH2 906 N N . ILE B 15 ? 0.1643 0.2211 0.3605 0.0003 0.0495 0.0855 15 ILE B N 907 C CA . ILE B 15 ? 0.2019 0.2188 0.3082 0.0254 0.0578 0.0484 15 ILE B CA 908 C C . ILE B 15 ? 0.1807 0.2777 0.3376 -0.0330 0.0438 0.0123 15 ILE B C 909 O O . ILE B 15 ? 0.3630 0.2669 0.3972 0.0956 -0.0076 -0.0038 15 ILE B O 910 C CB . ILE B 15 ? 0.2309 0.2315 0.2957 -0.0268 0.0355 0.0472 15 ILE B CB 911 C CG1 . ILE B 15 ? 0.3504 0.2668 0.3278 -0.0307 -0.0020 -0.0007 15 ILE B CG1 912 C CG2 . ILE B 15 ? 0.2071 0.2372 0.2790 -0.0388 0.0032 0.0327 15 ILE B CG2 913 C CD1 . ILE B 15 ? 0.3549 0.2915 0.3821 0.0697 -0.0005 0.0448 15 ILE B CD1 914 N N . GLY B 16 ? 0.2208 0.2538 0.3130 0.0065 0.0035 0.0005 16 GLY B N 915 C CA . GLY B 16 ? 0.2553 0.2912 0.3261 0.0145 -0.0298 0.0032 16 GLY B CA 916 C C . GLY B 16 ? 0.2682 0.2779 0.3588 -0.0025 -0.0273 0.0242 16 GLY B C 917 O O . GLY B 16 ? 0.3043 0.3398 0.4349 -0.0095 -0.0586 0.0447 16 GLY B O 918 N N . GLY B 17 ? 0.2252 0.2668 0.3371 -0.0073 0.0127 0.0397 17 GLY B N 919 C CA . GLY B 17 ? 0.1566 0.3576 0.3385 -0.0977 0.0261 -0.0033 17 GLY B CA 920 C C . GLY B 17 ? 0.2720 0.3254 0.3902 -0.0897 0.0282 -0.0045 17 GLY B C 921 O O . GLY B 17 ? 0.2627 0.3786 0.4876 -0.1193 0.0234 -0.0442 17 GLY B O 922 N N . GLN B 18 ? 0.1968 0.2889 0.4565 -0.0583 -0.0076 0.0000 18 GLN B N 923 C CA . GLN B 18 ? 0.2784 0.2803 0.3686 0.0055 -0.0169 0.0087 18 GLN B CA 924 C C . GLN B 18 ? 0.2429 0.2751 0.3915 0.0323 -0.0387 -0.0029 18 GLN B C 925 O O . GLN B 18 ? 0.1981 0.2501 0.4903 0.0245 -0.0281 -0.0163 18 GLN B O 926 C CB . GLN B 18 ? 0.1756 0.3078 0.3183 0.0568 -0.0021 -0.0268 18 GLN B CB 927 C CG . GLN B 18 ? 0.2685 0.3236 0.3754 0.0427 -0.0388 -0.0003 18 GLN B CG 928 C CD . GLN B 18 ? 0.2639 0.3803 0.3736 -0.0231 -0.0416 0.0009 18 GLN B CD 929 O OE1 . GLN B 18 ? 0.4604 0.4914 0.3538 -0.0018 -0.0528 -0.0162 18 GLN B OE1 930 N NE2 . GLN B 18 ? 0.2631 0.4117 0.4944 -0.0207 -0.0892 0.0051 18 GLN B NE2 931 N N . LEU B 19 ? 0.1672 0.2418 0.4170 -0.0264 -0.0575 -0.0117 19 LEU B N 932 C CA . LEU B 19 ? 0.1905 0.2374 0.3330 -0.0239 -0.0306 0.0146 19 LEU B CA 933 C C . LEU B 19 ? 0.2138 0.2716 0.3206 -0.0302 -0.0276 0.0375 19 LEU B C 934 O O . LEU B 19 ? 0.2573 0.3166 0.3812 -0.0445 -0.1050 0.0270 19 LEU B O 935 C CB . LEU B 19 ? 0.2597 0.2064 0.3266 -0.0361 -0.0296 -0.0388 19 LEU B CB 936 C CG . LEU B 19 ? 0.2778 0.2578 0.2858 -0.0492 -0.0434 0.0055 19 LEU B CG 937 C CD1 . LEU B 19 ? 0.3283 0.2874 0.4183 -0.0408 -0.0444 -0.0258 19 LEU B CD1 938 C CD2 . LEU B 19 ? 0.3166 0.3116 0.3447 -0.0659 -0.0038 -0.0572 19 LEU B CD2 939 N N . LYS B 20 ? 0.1871 0.2378 0.3184 -0.0061 -0.0449 0.0322 20 LYS B N 940 C CA . LYS B 20 ? 0.2227 0.2344 0.2660 -0.0130 -0.0342 0.0304 20 LYS B CA 941 C C . LYS B 20 ? 0.1899 0.2325 0.2425 -0.0031 -0.0777 0.0179 20 LYS B C 942 O O . LYS B 20 ? 0.2111 0.2651 0.2459 0.0199 -0.0715 0.0017 20 LYS B O 943 C CB . LYS B 20 ? 0.2364 0.2301 0.2738 0.0166 -0.0635 0.0145 20 LYS B CB 944 C CG . LYS B 20 ? 0.2376 0.2153 0.2923 0.0101 -0.0217 0.0327 20 LYS B CG 945 C CD . LYS B 20 ? 0.2498 0.2298 0.3417 0.0270 0.0120 0.0558 20 LYS B CD 946 C CE . LYS B 20 ? 0.1985 0.3092 0.3434 -0.0139 -0.0189 0.0530 20 LYS B CE 947 N NZ . LYS B 20 ? 0.2435 0.3246 0.3386 -0.0239 0.0047 0.0878 20 LYS B NZ 948 N N . GLU B 21 ? 0.2147 0.2013 0.2618 -0.0496 -0.0783 0.0064 21 GLU B N 949 C CA . GLU B 21 ? 0.1897 0.2006 0.2237 -0.0336 -0.0685 0.0030 21 GLU B CA 950 C C . GLU B 21 ? 0.1964 0.1732 0.2208 -0.0175 -0.0533 0.0072 21 GLU B C 951 O O . GLU B 21 ? 0.2282 0.1877 0.2012 -0.0410 -0.0713 0.0062 21 GLU B O 952 C CB . GLU B 21 ? 0.2340 0.2188 0.2478 -0.0612 -0.0439 -0.0075 21 GLU B CB 953 C CG . GLU B 21 ? 0.2643 0.2842 0.3780 -0.0878 -0.0397 -0.0205 21 GLU B CG 954 C CD . GLU B 21 ? 0.3170 0.2813 0.3892 -0.0586 -0.0113 -0.0119 21 GLU B CD 955 O OE1 . GLU B 21 ? 0.3035 0.2798 0.4876 -0.0704 -0.0011 -0.0542 21 GLU B OE1 956 O OE2 . GLU B 21 ? 0.3490 0.2993 0.4940 -0.0347 -0.0488 0.0441 21 GLU B OE2 957 N N . ALA B 22 ? 0.1672 0.1496 0.2009 -0.0132 -0.0406 0.0180 22 ALA B N 958 C CA . ALA B 22 ? 0.1587 0.1293 0.1899 0.0066 -0.0437 0.0008 22 ALA B CA 959 C C . ALA B 22 ? 0.1399 0.1415 0.1299 0.0033 -0.0121 0.0141 22 ALA B C 960 O O . ALA B 22 ? 0.1337 0.1371 0.1920 -0.0014 -0.0087 0.0413 22 ALA B O 961 C CB . ALA B 22 ? 0.1587 0.1549 0.1795 -0.0044 -0.0306 0.0042 22 ALA B CB 962 N N . LEU B 23 ? 0.1484 0.1228 0.1502 -0.0057 -0.0189 0.0198 23 LEU B N 963 C CA . LEU B 23 ? 0.1292 0.1040 0.1451 0.0090 -0.0079 0.0140 23 LEU B CA 964 C C . LEU B 23 ? 0.1018 0.1142 0.1543 0.0068 -0.0067 -0.0184 23 LEU B C 965 O O . LEU B 23 ? 0.1747 0.1299 0.1729 0.0423 -0.0255 -0.0124 23 LEU B O 966 C CB . LEU B 23 ? 0.1708 0.1285 0.1761 0.0120 0.0252 0.0152 23 LEU B CB 967 C CG . LEU B 23 ? 0.2020 0.1696 0.2560 0.0090 0.0454 0.0080 23 LEU B CG 968 C CD1 . LEU B 23 ? 0.2114 0.1809 0.2057 0.0228 0.0700 0.0649 23 LEU B CD1 969 C CD2 . LEU B 23 ? 0.1890 0.1563 0.2648 0.0349 0.0484 0.0265 23 LEU B CD2 970 N N . LEU B 24 ? 0.1240 0.0989 0.1485 0.0133 -0.0037 -0.0007 24 LEU B N 971 C CA . LEU B 24 ? 0.1146 0.1145 0.1667 0.0023 -0.0038 -0.0012 24 LEU B CA 972 C C . LEU B 24 ? 0.1222 0.1123 0.1413 -0.0009 -0.0005 -0.0071 24 LEU B C 973 O O . LEU B 24 ? 0.1114 0.1302 0.1681 0.0146 -0.0026 -0.0135 24 LEU B O 974 C CB . LEU B 24 ? 0.1538 0.1203 0.1664 0.0011 0.0051 0.0130 24 LEU B CB 975 C CG . LEU B 24 ? 0.1579 0.1395 0.1829 0.0013 0.0261 0.0086 24 LEU B CG 976 C CD1 . LEU B 24 ? 0.2337 0.2105 0.1921 -0.0608 -0.0213 0.0521 24 LEU B CD1 977 C CD2 . LEU B 24 ? 0.1703 0.2158 0.2648 -0.0310 0.0446 -0.0511 24 LEU B CD2 978 N N . ASP B 25 ? 0.1287 0.1049 0.1154 0.0062 -0.0030 -0.0012 25 ASP B N 979 C CA . ASP B 25 ? 0.1140 0.1074 0.1219 0.0166 -0.0004 0.0064 25 ASP B CA 980 C C . ASP B 25 ? 0.1279 0.1049 0.1159 0.0082 0.0064 0.0000 25 ASP B C 981 O O . ASP B 25 ? 0.1307 0.1152 0.1270 0.0178 0.0141 -0.0046 25 ASP B O 982 C CB . ASP B 25 ? 0.1143 0.1006 0.1140 0.0098 0.0148 -0.0084 25 ASP B CB 983 C CG . ASP B 25 ? 0.1282 0.1124 0.1034 0.0211 -0.0017 0.0017 25 ASP B CG 984 O OD1 . ASP B 25 ? 0.1341 0.1312 0.1128 0.0018 0.0040 -0.0019 25 ASP B OD1 985 O OD2 . ASP B 25 ? 0.1339 0.1392 0.1207 0.0107 0.0133 0.0154 25 ASP B OD2 986 N N . THR B 26 ? 0.1334 0.1055 0.1124 0.0205 -0.0030 -0.0015 26 THR B N 987 C CA . THR B 26 ? 0.1337 0.1249 0.0989 0.0247 0.0073 -0.0142 26 THR B CA 988 C C . THR B 26 ? 0.1335 0.1131 0.1027 0.0126 0.0006 -0.0169 26 THR B C 989 O O . THR B 26 ? 0.1698 0.1161 0.1162 0.0115 0.0002 -0.0087 26 THR B O 990 C CB . THR B 26 ? 0.1474 0.1322 0.0741 0.0194 0.0186 -0.0219 26 THR B CB 991 O OG1 . THR B 26 ? 0.1437 0.1189 0.1011 0.0108 0.0030 -0.0012 26 THR B OG1 992 C CG2 . THR B 26 ? 0.1549 0.1275 0.0952 0.0085 0.0121 0.0066 26 THR B CG2 993 N N . GLY B 27 ? 0.1322 0.1076 0.1136 0.0124 0.0145 -0.0161 27 GLY B N 994 C CA . GLY B 27 ? 0.1266 0.1360 0.1224 -0.0070 0.0036 -0.0056 27 GLY B CA 995 C C . GLY B 27 ? 0.1426 0.1056 0.1223 0.0073 0.0075 0.0030 27 GLY B C 996 O O . GLY B 27 ? 0.1526 0.1356 0.1431 -0.0068 0.0187 0.0086 27 GLY B O 997 N N . ALA B 28 ? 0.1376 0.1077 0.1172 0.0045 0.0029 0.0031 28 ALA B N 998 C CA . ALA B 28 ? 0.1555 0.1182 0.1314 0.0220 0.0150 0.0114 28 ALA B CA 999 C C . ALA B 28 ? 0.1465 0.1201 0.1380 0.0112 0.0016 0.0042 28 ALA B C 1000 O O . ALA B 28 ? 0.1712 0.1229 0.1108 0.0104 0.0117 -0.0003 28 ALA B O 1001 C CB . ALA B 28 ? 0.1515 0.1245 0.1254 0.0320 0.0076 0.0042 28 ALA B CB 1002 N N . ASP B 29 ? 0.1726 0.1082 0.1217 0.0166 0.0013 0.0054 29 ASP B N 1003 C CA . ASP B 29 ? 0.1847 0.1179 0.1232 0.0250 0.0134 -0.0046 29 ASP B CA 1004 C C . ASP B 29 ? 0.1714 0.1419 0.1521 0.0456 0.0186 -0.0198 29 ASP B C 1005 O O . ASP B 29 ? 0.1830 0.1806 0.1434 0.0382 0.0162 -0.0176 29 ASP B O 1006 C CB . ASP B 29 ? 0.1817 0.1261 0.1904 0.0216 -0.0004 -0.0245 29 ASP B CB 1007 C CG . ASP B 29 ? 0.2054 0.1185 0.2377 0.0179 -0.0142 0.0001 29 ASP B CG 1008 O OD1 . ASP B 29 ? 0.2074 0.1549 0.1783 0.0126 -0.0201 -0.0148 29 ASP B OD1 1009 O OD2 . ASP B 29 ? 0.2570 0.1616 0.3279 -0.0236 -0.0379 0.0601 29 ASP B OD2 1010 N N . ASP B 30 ? 0.1678 0.1467 0.1415 0.0115 0.0079 0.0041 30 ASP B N 1011 C CA . ASP B 30 ? 0.1756 0.1625 0.1348 0.0373 0.0046 0.0089 30 ASP B CA 1012 C C . ASP B 30 ? 0.1236 0.1540 0.1207 0.0364 0.0055 -0.0053 30 ASP B C 1013 O O . ASP B 30 ? 0.1724 0.2651 0.1791 -0.0226 0.0580 -0.0481 30 ASP B O 1014 C CB . ASP B 30 ? 0.2232 0.1561 0.2257 0.0293 -0.0311 -0.0104 30 ASP B CB 1015 C CG . ASP B 30 ? 0.3575 0.2250 0.2042 0.0576 -0.0042 -0.0122 30 ASP B CG 1016 O OD1 . ASP B 30 ? 0.4046 0.2439 0.2587 0.1059 0.0506 -0.0153 30 ASP B OD1 1017 O OD2 . ASP B 30 ? 0.5457 0.2828 0.2608 -0.0648 0.0309 0.0023 30 ASP B OD2 1018 N N . THR B 31 ? 0.1320 0.1462 0.1606 0.0224 0.0158 0.0013 31 THR B N 1019 C CA . THR B 31 ? 0.1411 0.1216 0.1534 0.0428 0.0131 0.0388 31 THR B CA 1020 C C . THR B 31 ? 0.1345 0.1238 0.1392 0.0321 0.0242 0.0315 31 THR B C 1021 O O . THR B 31 ? 0.1476 0.1275 0.1665 0.0314 0.0124 0.0328 31 THR B O 1022 C CB . THR B 31 ? 0.1387 0.1449 0.1289 0.0241 0.0119 0.0198 31 THR B CB 1023 O OG1 . THR B 31 ? 0.1514 0.1650 0.1256 0.0437 0.0306 0.0428 31 THR B OG1 1024 C CG2 . THR B 31 ? 0.1522 0.1715 0.1252 0.0434 0.0347 0.0237 31 THR B CG2 1025 N N A VAL B 32 ? 0.1076 0.1301 0.1294 0.0110 0.0064 0.0187 32 VAL B N 1026 N N B VAL B 32 ? 0.1148 0.1333 0.1301 0.0183 -0.0005 0.0122 32 VAL B N 1027 C CA A VAL B 32 ? 0.1039 0.1455 0.1406 0.0052 -0.0196 0.0185 32 VAL B CA 1028 C CA B VAL B 32 ? 0.1182 0.1368 0.1390 0.0018 -0.0248 0.0147 32 VAL B CA 1029 C C A VAL B 32 ? 0.1471 0.1443 0.1147 0.0054 -0.0048 0.0310 32 VAL B C 1030 C C B VAL B 32 ? 0.1452 0.1500 0.1448 0.0188 -0.0054 0.0219 32 VAL B C 1031 O O A VAL B 32 ? 0.1527 0.1442 0.1594 0.0314 -0.0156 0.0144 32 VAL B O 1032 O O B VAL B 32 ? 0.1355 0.1288 0.1444 0.0232 0.0106 0.0336 32 VAL B O 1033 C CB A VAL B 32 ? 0.1628 0.1899 0.1253 -0.0082 -0.0077 0.0383 32 VAL B CB 1034 C CB B VAL B 32 ? 0.1396 0.1405 0.1327 0.0171 -0.0103 0.0254 32 VAL B CB 1035 C CG1 A VAL B 32 ? 0.1829 0.2135 0.1642 -0.0086 -0.0551 0.0178 32 VAL B CG1 1036 C CG1 B VAL B 32 ? 0.1262 0.1401 0.1000 0.0195 -0.0236 0.0091 32 VAL B CG1 1037 C CG2 A VAL B 32 ? 0.1550 0.1716 0.1359 0.0262 0.0030 0.0080 32 VAL B CG2 1038 C CG2 B VAL B 32 ? 0.1592 0.1535 0.1651 -0.0360 -0.0001 0.0246 32 VAL B CG2 1039 N N . LEU B 33 ? 0.1245 0.1438 0.1858 0.0172 -0.0206 0.0200 33 LEU B N 1040 C CA . LEU B 33 ? 0.1406 0.1489 0.1376 0.0072 0.0015 0.0218 33 LEU B CA 1041 C C . LEU B 33 ? 0.1235 0.1443 0.1545 -0.0178 -0.0117 0.0122 33 LEU B C 1042 O O . LEU B 33 ? 0.1655 0.1492 0.1604 -0.0049 -0.0044 0.0281 33 LEU B O 1043 C CB . LEU B 33 ? 0.1693 0.1802 0.1735 -0.0245 -0.0162 -0.0053 33 LEU B CB 1044 C CG . LEU B 33 ? 0.2294 0.2264 0.1791 -0.0131 0.0099 0.0312 33 LEU B CG 1045 C CD1 . LEU B 33 ? 0.2631 0.2673 0.1885 -0.0637 0.0101 0.0323 33 LEU B CD1 1046 C CD2 . LEU B 33 ? 0.2948 0.2185 0.2089 0.0085 -0.0221 0.0346 33 LEU B CD2 1047 N N . GLU B 34 ? 0.1722 0.1536 0.1501 -0.0115 -0.0018 0.0146 34 GLU B N 1048 C CA . GLU B 34 ? 0.1749 0.1808 0.1600 -0.0196 0.0016 0.0156 34 GLU B CA 1049 C C . GLU B 34 ? 0.1950 0.1997 0.1197 -0.0095 -0.0097 0.0060 34 GLU B C 1050 O O . GLU B 34 ? 0.1782 0.1865 0.1608 -0.0141 -0.0016 0.0418 34 GLU B O 1051 C CB . GLU B 34 ? 0.2040 0.1883 0.1596 0.0072 0.0116 -0.0070 34 GLU B CB 1052 C CG . GLU B 34 ? 0.2193 0.2432 0.2510 0.0112 -0.0225 -0.0197 34 GLU B CG 1053 C CD . GLU B 34 ? 0.2415 0.2349 0.3026 0.0146 0.0205 -0.0054 34 GLU B CD 1054 O OE1 . GLU B 34 ? 0.3766 0.3280 0.3931 0.0115 -0.0858 -0.1109 34 GLU B OE1 1055 O OE2 . GLU B 34 ? 0.2705 0.3342 0.4828 0.0529 -0.0693 -0.0805 34 GLU B OE2 1056 N N . GLU B 35 ? 0.2031 0.2214 0.1087 0.0230 0.0101 0.0110 35 GLU B N 1057 C CA . GLU B 35 ? 0.1929 0.2190 0.1414 0.0077 -0.0230 0.0238 35 GLU B CA 1058 C C . GLU B 35 ? 0.2069 0.2042 0.1674 0.0036 -0.0428 0.0099 35 GLU B C 1059 O O . GLU B 35 ? 0.2225 0.2126 0.2243 -0.0319 -0.0528 0.0018 35 GLU B O 1060 C CB . GLU B 35 ? 0.2435 0.2465 0.1621 0.0322 0.0096 0.0128 35 GLU B CB 1061 C CG . GLU B 35 ? 0.2953 0.2773 0.2245 0.0370 -0.0196 0.0644 35 GLU B CG 1062 C CD . GLU B 35 ? 0.3224 0.2484 0.2921 0.0740 -0.0365 0.0645 35 GLU B CD 1063 O OE1 . GLU B 35 ? 0.3828 0.3495 0.3383 0.0860 0.0574 0.0768 35 GLU B OE1 1064 O OE2 . GLU B 35 ? 0.4444 0.2433 0.2461 0.0301 -0.0225 0.0634 35 GLU B OE2 1065 N N . MET B 36 ? 0.1734 0.2131 0.1730 -0.0182 -0.0359 0.0256 36 MET B N 1066 C CA . MET B 36 ? 0.1988 0.2200 0.2408 -0.0478 -0.0279 0.0146 36 MET B CA 1067 C C . MET B 36 ? 0.1910 0.2701 0.2701 -0.0293 -0.0265 0.0089 36 MET B C 1068 O O . MET B 36 ? 0.1660 0.2221 0.3320 0.0068 -0.0108 0.0456 36 MET B O 1069 C CB . MET B 36 ? 0.2259 0.2658 0.2613 -0.0566 -0.0095 0.0350 36 MET B CB 1070 C CG . MET B 36 ? 0.2509 0.2393 0.2425 -0.0143 0.0231 0.0397 36 MET B CG 1071 S SD . MET B 36 ? 0.2923 0.3116 0.2687 0.0214 0.0131 0.0664 36 MET B SD 1072 C CE . MET B 36 ? 0.2668 0.3729 0.3080 0.0274 0.0556 0.0596 36 MET B CE 1073 N N . ASN B 37 ? 0.1792 0.3083 0.2820 -0.0475 -0.0082 0.0171 37 ASN B N 1074 C CA . ASN B 37 ? 0.2125 0.3453 0.2404 -0.0119 -0.0174 0.0367 37 ASN B CA 1075 C C . ASN B 37 ? 0.2074 0.3548 0.2509 -0.0741 0.0253 0.0672 37 ASN B C 1076 O O . ASN B 37 ? 0.1863 0.4532 0.3012 -0.0644 0.0022 0.0285 37 ASN B O 1077 C CB . ASN B 37 ? 0.2584 0.4030 0.2944 -0.0116 -0.0461 0.0074 37 ASN B CB 1078 C CG . ASN B 37 ? 0.2634 0.4647 0.3681 0.0249 -0.0448 0.0199 37 ASN B CG 1079 O OD1 . ASN B 37 ? 0.3805 0.6512 0.5500 0.0858 -0.1657 0.0166 37 ASN B OD1 1080 N ND2 . ASN B 37 ? 0.3041 0.4164 0.4236 -0.0079 0.0140 0.0419 37 ASN B ND2 1081 N N . LEU B 38 ? 0.1943 0.3411 0.2969 -0.0270 -0.0067 0.0663 38 LEU B N 1082 C CA . LEU B 38 ? 0.2009 0.2797 0.2771 -0.0395 -0.0092 0.0571 38 LEU B CA 1083 C C . LEU B 38 ? 0.2374 0.2696 0.3203 -0.0370 0.0014 0.0686 38 LEU B C 1084 O O . LEU B 38 ? 0.2841 0.2389 0.3110 -0.0496 -0.0219 0.0816 38 LEU B O 1085 C CB . LEU B 38 ? 0.2604 0.2808 0.3224 -0.0625 -0.0396 0.0729 38 LEU B CB 1086 C CG . LEU B 38 ? 0.2741 0.2572 0.4232 -0.0529 -0.0718 0.0492 38 LEU B CG 1087 C CD1 . LEU B 38 ? 0.2760 0.2575 0.2864 -0.0467 -0.0487 0.0878 38 LEU B CD1 1088 C CD2 . LEU B 38 ? 0.2393 0.2669 0.4081 -0.0233 -0.0599 0.0627 38 LEU B CD2 1089 N N . PRO B 39 ? 0.2268 0.2625 0.3292 -0.0369 -0.0052 0.0309 39 PRO B N 1090 C CA . PRO B 39 ? 0.2471 0.2940 0.3113 -0.0047 -0.0201 0.0266 39 PRO B CA 1091 C C . PRO B 39 ? 0.2190 0.2997 0.2987 -0.0444 0.0186 0.0343 39 PRO B C 1092 O O . PRO B 39 ? 0.2429 0.3611 0.2929 -0.0812 0.0054 0.0736 39 PRO B O 1093 C CB . PRO B 39 ? 0.2585 0.3301 0.3861 -0.0248 -0.0019 0.0091 39 PRO B CB 1094 C CG . PRO B 39 ? 0.2648 0.2971 0.3660 -0.0441 0.0416 0.0084 39 PRO B CG 1095 C CD . PRO B 39 ? 0.2434 0.2995 0.3743 -0.0591 0.0332 0.0369 39 PRO B CD 1096 N N . GLY B 40 ? 0.3225 0.3284 0.2984 -0.0408 0.0218 0.0221 40 GLY B N 1097 C CA . GLY B 40 ? 0.3273 0.3280 0.3192 -0.0731 0.0500 0.0147 40 GLY B CA 1098 C C . GLY B 40 ? 0.2781 0.3194 0.3516 -0.0491 0.0429 0.0160 40 GLY B C 1099 O O . GLY B 40 ? 0.2638 0.3253 0.3597 0.0210 0.0410 0.0323 40 GLY B O 1100 N N . LYS B 41 ? 0.2563 0.2772 0.3253 0.0050 0.0793 0.0138 41 LYS B N 1101 C CA . LYS B 41 ? 0.2118 0.2784 0.3526 0.0164 0.0377 0.0097 41 LYS B CA 1102 C C . LYS B 41 ? 0.2115 0.2402 0.3075 0.0457 0.0642 0.0355 41 LYS B C 1103 O O . LYS B 41 ? 0.2325 0.2479 0.3361 0.0343 0.0927 0.0908 41 LYS B O 1104 C CB . LYS B 41 ? 0.2044 0.3459 0.3725 0.0623 0.0599 -0.0115 41 LYS B CB 1105 N N . TRP B 42 ? 0.1632 0.2520 0.2620 0.0492 0.0396 0.0484 42 TRP B N 1106 C CA . TRP B 42 ? 0.1782 0.2153 0.2434 0.0519 0.0385 0.0416 42 TRP B CA 1107 C C . TRP B 42 ? 0.1959 0.2160 0.3176 0.0666 0.0374 0.0596 42 TRP B C 1108 O O . TRP B 42 ? 0.2220 0.2130 0.2990 0.0730 0.0323 0.0668 42 TRP B O 1109 C CB . TRP B 42 ? 0.1968 0.2287 0.2503 0.0123 0.0252 0.0481 42 TRP B CB 1110 C CG . TRP B 42 ? 0.2091 0.3156 0.2494 0.0667 0.0233 0.0228 42 TRP B CG 1111 C CD1 . TRP B 42 ? 0.2674 0.3744 0.3251 -0.0027 0.0039 0.0562 42 TRP B CD1 1112 C CD2 . TRP B 42 ? 0.2300 0.2580 0.3413 0.0686 0.0128 0.0757 42 TRP B CD2 1113 N NE1 . TRP B 42 ? 0.2867 0.3873 0.3891 0.0507 -0.0435 0.1131 42 TRP B NE1 1114 C CE2 . TRP B 42 ? 0.2263 0.3599 0.3812 0.0944 -0.0098 0.0783 42 TRP B CE2 1115 C CE3 . TRP B 42 ? 0.2780 0.2318 0.2616 0.0089 0.0479 0.0584 42 TRP B CE3 1116 C CZ2 . TRP B 42 ? 0.3756 0.3539 0.3853 0.0242 -0.0268 0.0654 42 TRP B CZ2 1117 C CZ3 . TRP B 42 ? 0.3727 0.3039 0.2504 -0.0016 0.0006 0.0558 42 TRP B CZ3 1118 C CH2 . TRP B 42 ? 0.3990 0.3299 0.2593 -0.0263 -0.0181 0.0749 42 TRP B CH2 1119 N N . LYS B 43 ? 0.1697 0.2112 0.2830 0.0577 0.0645 0.0679 43 LYS B N 1120 C CA . LYS B 43 ? 0.1564 0.2182 0.2712 0.0536 0.0551 0.0372 43 LYS B CA 1121 C C . LYS B 43 ? 0.1641 0.1932 0.2185 0.0600 0.0295 0.0449 43 LYS B C 1122 O O . LYS B 43 ? 0.1781 0.1572 0.2499 0.0631 0.0376 0.0412 43 LYS B O 1123 C CB . LYS B 43 ? 0.2264 0.2652 0.3116 0.0013 0.1159 -0.0364 43 LYS B CB 1124 N N . PRO B 44 ? 0.1682 0.1627 0.2339 0.0386 0.0382 0.0483 44 PRO B N 1125 C CA . PRO B 44 ? 0.1850 0.1879 0.2378 0.0228 0.0227 0.0406 44 PRO B CA 1126 C C . PRO B 44 ? 0.1662 0.1714 0.1970 0.0004 0.0312 0.0075 44 PRO B C 1127 O O . PRO B 44 ? 0.1761 0.1810 0.2301 0.0300 0.0247 0.0053 44 PRO B O 1128 C CB . PRO B 44 ? 0.2055 0.2539 0.2379 0.0201 0.0315 0.0596 44 PRO B CB 1129 C CG . PRO B 44 ? 0.3406 0.1914 0.2513 0.0140 0.0265 0.0528 44 PRO B CG 1130 C CD . PRO B 44 ? 0.1729 0.1651 0.2772 0.0311 0.0055 0.0491 44 PRO B CD 1131 N N . LYS B 45 ? 0.1664 0.1462 0.1718 0.0271 0.0307 0.0083 45 LYS B N 1132 C CA . LYS B 45 ? 0.1638 0.1631 0.1754 0.0306 0.0163 0.0046 45 LYS B CA 1133 C C . LYS B 45 ? 0.1463 0.1311 0.1529 0.0064 0.0043 0.0075 45 LYS B C 1134 O O . LYS B 45 ? 0.1512 0.1558 0.1809 -0.0229 0.0148 -0.0180 45 LYS B O 1135 C CB . LYS B 45 ? 0.1987 0.1807 0.1846 0.0260 0.0442 -0.0002 45 LYS B CB 1136 C CG . LYS B 45 ? 0.2183 0.1898 0.2096 0.0012 0.0353 0.0177 45 LYS B CG 1137 C CD . LYS B 45 ? 0.2892 0.2046 0.2116 0.0085 0.0201 0.0394 45 LYS B CD 1138 C CE . LYS B 45 ? 0.2694 0.3450 0.2976 0.0031 0.0341 0.0097 45 LYS B CE 1139 N NZ . LYS B 45 ? 0.3961 0.3817 0.4136 -0.0645 -0.0183 -0.0226 45 LYS B NZ 1140 N N A MET B 46 ? 0.1552 0.1320 0.1174 -0.0055 0.0085 -0.0138 46 MET B N 1141 N N B MET B 46 ? 0.1559 0.1343 0.1196 -0.0032 0.0117 -0.0120 46 MET B N 1142 C CA A MET B 46 ? 0.1472 0.1202 0.1302 -0.0016 0.0083 -0.0247 46 MET B CA 1143 C CA B MET B 46 ? 0.1512 0.1341 0.1321 0.0096 0.0122 -0.0176 46 MET B CA 1144 C C A MET B 46 ? 0.1539 0.1514 0.1239 -0.0077 -0.0019 -0.0197 46 MET B C 1145 C C B MET B 46 ? 0.1605 0.1611 0.1172 0.0037 0.0019 -0.0176 46 MET B C 1146 O O A MET B 46 ? 0.1911 0.2037 0.1417 0.0312 -0.0194 -0.0420 46 MET B O 1147 O O B MET B 46 ? 0.1842 0.1974 0.1554 0.0243 -0.0320 -0.0424 46 MET B O 1148 C CB A MET B 46 ? 0.1245 0.1571 0.1652 -0.0220 0.0159 -0.0184 46 MET B CB 1149 C CB B MET B 46 ? 0.1541 0.1544 0.1818 -0.0098 0.0374 -0.0173 46 MET B CB 1150 C CG A MET B 46 ? 0.1808 0.1271 0.1893 -0.0072 0.0006 -0.0082 46 MET B CG 1151 C CG B MET B 46 ? 0.1123 0.1023 0.2298 0.0294 0.0853 0.0245 46 MET B CG 1152 S SD A MET B 46 ? 0.2911 0.1698 0.1929 -0.0647 -0.0352 0.0031 46 MET B SD 1153 S SD B MET B 46 ? 0.2042 0.1471 0.1751 -0.0322 0.0063 -0.0016 46 MET B SD 1154 C CE A MET B 46 ? 0.2954 0.2253 0.2014 -0.0142 0.0167 -0.0188 46 MET B CE 1155 C CE B MET B 46 ? 0.1683 0.1763 0.1392 -0.0424 -0.0170 0.0129 46 MET B CE 1156 N N . ILE B 47 ? 0.1302 0.1474 0.1343 0.0042 0.0047 -0.0247 47 ILE B N 1157 C CA . ILE B 47 ? 0.1332 0.1584 0.1293 -0.0057 0.0089 -0.0142 47 ILE B CA 1158 C C . ILE B 47 ? 0.1336 0.1432 0.1296 -0.0030 0.0071 -0.0066 47 ILE B C 1159 O O . ILE B 47 ? 0.1459 0.1480 0.1247 -0.0130 0.0137 -0.0107 47 ILE B O 1160 C CB . ILE B 47 ? 0.1255 0.1855 0.1360 0.0176 0.0123 0.0146 47 ILE B CB 1161 C CG1 . ILE B 47 ? 0.1347 0.1691 0.1483 0.0100 0.0005 0.0270 47 ILE B CG1 1162 C CG2 . ILE B 47 ? 0.1676 0.2061 0.1557 0.0024 0.0267 -0.0111 47 ILE B CG2 1163 C CD1 . ILE B 47 ? 0.1674 0.1731 0.1794 -0.0087 -0.0054 0.0376 47 ILE B CD1 1164 N N . GLY B 48 ? 0.1403 0.1586 0.1364 0.0099 0.0135 -0.0059 48 GLY B N 1165 C CA . GLY B 48 ? 0.1515 0.1521 0.1978 0.0142 0.0177 -0.0070 48 GLY B CA 1166 C C . GLY B 48 ? 0.1325 0.1319 0.1458 0.0000 0.0074 0.0043 48 GLY B C 1167 O O . GLY B 48 ? 0.1568 0.1853 0.1484 0.0190 0.0049 -0.0126 48 GLY B O 1168 N N . GLY B 49 ? 0.1305 0.1355 0.1212 0.0038 0.0121 0.0032 49 GLY B N 1169 C CA . GLY B 49 ? 0.1590 0.1385 0.1410 0.0234 0.0026 0.0197 49 GLY B CA 1170 C C . GLY B 49 ? 0.1576 0.1466 0.1062 0.0093 0.0127 0.0149 49 GLY B C 1171 O O . GLY B 49 ? 0.1339 0.1374 0.1403 0.0029 0.0118 0.0172 49 GLY B O 1172 N N . ILE B 50 ? 0.1450 0.1391 0.1374 0.0311 0.0121 0.0345 50 ILE B N 1173 C CA . ILE B 50 ? 0.1104 0.1567 0.1270 0.0206 0.0145 0.0143 50 ILE B CA 1174 C C . ILE B 50 ? 0.1366 0.1419 0.1258 0.0168 0.0014 0.0064 50 ILE B C 1175 O O . ILE B 50 ? 0.1394 0.1614 0.1542 0.0152 0.0005 0.0049 50 ILE B O 1176 C CB . ILE B 50 ? 0.1324 0.1481 0.1223 0.0180 0.0086 0.0044 50 ILE B CB 1177 C CG1 . ILE B 50 ? 0.1549 0.1625 0.1439 0.0258 -0.0114 0.0103 50 ILE B CG1 1178 C CG2 . ILE B 50 ? 0.1470 0.1672 0.1289 0.0225 0.0117 0.0090 50 ILE B CG2 1179 C CD1 . ILE B 50 ? 0.1511 0.1683 0.1548 0.0309 -0.0244 0.0223 50 ILE B CD1 1180 N N . GLY B 51 ? 0.1193 0.1622 0.1385 0.0216 0.0001 0.0151 51 GLY B N 1181 C CA . GLY B 51 ? 0.1455 0.1657 0.1211 0.0331 0.0122 0.0383 51 GLY B CA 1182 C C . GLY B 51 ? 0.1614 0.1608 0.1545 0.0130 -0.0205 0.0225 51 GLY B C 1183 O O . GLY B 51 ? 0.2565 0.2381 0.1710 0.0686 -0.0457 0.0456 51 GLY B O 1184 N N . GLY B 52 ? 0.1330 0.1448 0.1487 0.0104 0.0145 0.0277 52 GLY B N 1185 C CA . GLY B 52 ? 0.1319 0.1420 0.1783 0.0019 0.0184 0.0369 52 GLY B CA 1186 C C . GLY B 52 ? 0.1343 0.1381 0.1258 -0.0060 -0.0002 0.0136 52 GLY B C 1187 O O . GLY B 52 ? 0.1383 0.1487 0.1410 0.0148 0.0092 0.0232 52 GLY B O 1188 N N . PHE B 53 ? 0.1423 0.1809 0.1403 0.0229 0.0104 0.0451 53 PHE B N 1189 C CA . PHE B 53 ? 0.1218 0.1684 0.1488 0.0120 0.0026 -0.0009 53 PHE B CA 1190 C C . PHE B 53 ? 0.1608 0.1863 0.1089 0.0267 0.0000 -0.0072 53 PHE B C 1191 O O . PHE B 53 ? 0.1686 0.2510 0.1214 0.0407 0.0055 -0.0061 53 PHE B O 1192 C CB . PHE B 53 ? 0.1667 0.1721 0.1508 0.0358 0.0266 0.0338 53 PHE B CB 1193 C CG . PHE B 53 ? 0.1432 0.1268 0.1926 0.0149 0.0060 0.0258 53 PHE B CG 1194 C CD1 . PHE B 53 ? 0.1681 0.1390 0.2457 0.0371 0.0059 0.0319 53 PHE B CD1 1195 C CD2 . PHE B 53 ? 0.1628 0.1350 0.1909 -0.0134 -0.0116 -0.0082 53 PHE B CD2 1196 C CE1 . PHE B 53 ? 0.1518 0.1551 0.2609 -0.0159 -0.0033 0.0159 53 PHE B CE1 1197 C CE2 . PHE B 53 ? 0.1956 0.1226 0.2248 -0.0030 -0.0272 0.0036 53 PHE B CE2 1198 C CZ . PHE B 53 ? 0.1918 0.2006 0.2241 -0.0152 -0.0580 0.0003 53 PHE B CZ 1199 N N . ILE B 54 ? 0.1240 0.1815 0.1451 0.0152 -0.0082 -0.0094 54 ILE B N 1200 C CA . ILE B 54 ? 0.1475 0.1658 0.1513 0.0288 -0.0275 -0.0370 54 ILE B CA 1201 C C . ILE B 54 ? 0.1390 0.1282 0.1502 0.0100 -0.0032 -0.0221 54 ILE B C 1202 O O . ILE B 54 ? 0.1371 0.1648 0.1525 0.0014 -0.0035 -0.0327 54 ILE B O 1203 C CB . ILE B 54 ? 0.1714 0.1794 0.1698 0.0334 -0.0407 -0.0513 54 ILE B CB 1204 C CG1 . ILE B 54 ? 0.1871 0.1385 0.2074 0.0389 -0.0433 -0.0398 54 ILE B CG1 1205 C CG2 . ILE B 54 ? 0.2228 0.2019 0.1666 0.0649 -0.0428 -0.0456 54 ILE B CG2 1206 C CD1 . ILE B 54 ? 0.2111 0.1653 0.2264 0.0315 -0.0620 -0.0256 54 ILE B CD1 1207 N N . LYS B 55 ? 0.1381 0.1332 0.1529 0.0144 -0.0077 -0.0094 55 LYS B N 1208 C CA . LYS B 55 ? 0.1470 0.1319 0.1553 0.0139 -0.0003 0.0180 55 LYS B CA 1209 C C . LYS B 55 ? 0.1203 0.1289 0.1444 0.0066 -0.0189 0.0030 55 LYS B C 1210 O O . LYS B 55 ? 0.1534 0.1575 0.1575 -0.0123 -0.0129 -0.0030 55 LYS B O 1211 C CB . LYS B 55 ? 0.1649 0.1536 0.1911 0.0338 0.0141 0.0156 55 LYS B CB 1212 C CG . LYS B 55 ? 0.2872 0.2013 0.3068 0.0002 0.0165 0.0145 55 LYS B CG 1213 C CD . LYS B 55 ? 0.4481 0.2386 0.2523 0.0065 0.0073 0.0129 55 LYS B CD 1214 C CE . LYS B 55 ? 0.4643 0.1903 0.3831 -0.0365 -0.0131 0.0008 55 LYS B CE 1215 N NZ . LYS B 55 ? 0.4960 0.4001 0.4958 0.0024 0.0719 -0.0235 55 LYS B NZ 1216 N N . VAL B 56 ? 0.1357 0.1225 0.1623 -0.0008 -0.0139 0.0081 56 VAL B N 1217 C CA . VAL B 56 ? 0.1484 0.1255 0.1914 0.0072 0.0111 0.0388 56 VAL B CA 1218 C C . VAL B 56 ? 0.1525 0.1434 0.2026 -0.0041 0.0025 0.0181 56 VAL B C 1219 O O . VAL B 56 ? 0.1495 0.1633 0.2025 -0.0026 0.0195 0.0146 56 VAL B O 1220 C CB . VAL B 56 ? 0.1420 0.1343 0.1693 -0.0123 -0.0060 0.0249 56 VAL B CB 1221 C CG1 . VAL B 56 ? 0.1340 0.1547 0.2277 0.0145 -0.0181 0.0259 56 VAL B CG1 1222 C CG2 . VAL B 56 ? 0.1648 0.1524 0.1959 0.0015 -0.0166 0.0398 56 VAL B CG2 1223 N N . ARG B 57 ? 0.1481 0.1350 0.1918 0.0180 0.0117 0.0302 57 ARG B N 1224 C CA . ARG B 57 ? 0.1257 0.1556 0.2156 0.0194 0.0146 0.0351 57 ARG B CA 1225 C C . ARG B 57 ? 0.1170 0.1510 0.1940 0.0090 0.0082 0.0289 57 ARG B C 1226 O O . ARG B 57 ? 0.1602 0.1325 0.2251 0.0322 0.0142 0.0376 57 ARG B O 1227 C CB . ARG B 57 ? 0.1563 0.1731 0.2000 0.0280 -0.0041 0.0604 57 ARG B CB 1228 C CG . ARG B 57 ? 0.1818 0.2370 0.2191 0.0118 -0.0153 0.0119 57 ARG B CG 1229 C CD . ARG B 57 ? 0.2074 0.2924 0.3087 0.0345 -0.0626 0.0162 57 ARG B CD 1230 N NE . ARG B 57 ? 0.2055 0.3053 0.3392 0.0088 -0.0465 0.0191 57 ARG B NE 1231 C CZ . ARG B 57 ? 0.2646 0.2666 0.2959 -0.0047 -0.0366 0.0668 57 ARG B CZ 1232 N NH1 . ARG B 57 ? 0.3324 0.2778 0.4298 0.0223 0.0578 0.0346 57 ARG B NH1 1233 N NH2 . ARG B 57 ? 0.3222 0.2360 0.4485 0.0158 -0.0218 0.1227 57 ARG B NH2 1234 N N . GLN B 58 ? 0.1610 0.1568 0.1906 0.0403 0.0199 0.0250 58 GLN B N 1235 C CA . GLN B 58 ? 0.1578 0.1698 0.1968 0.0561 0.0430 0.0173 58 GLN B CA 1236 C C . GLN B 58 ? 0.1603 0.1407 0.2188 0.0389 0.0396 0.0361 58 GLN B C 1237 O O . GLN B 58 ? 0.1938 0.1713 0.2400 0.0746 0.0525 0.0522 58 GLN B O 1238 C CB . GLN B 58 ? 0.1849 0.1770 0.1816 0.0572 0.0208 0.0252 58 GLN B CB 1239 C CG . GLN B 58 ? 0.2249 0.2067 0.2256 0.0663 0.0407 0.0274 58 GLN B CG 1240 C CD . GLN B 58 ? 0.2895 0.2342 0.2883 0.0153 0.0338 0.0180 58 GLN B CD 1241 O OE1 . GLN B 58 ? 0.2941 0.2812 0.3312 -0.0235 0.0691 -0.0200 58 GLN B OE1 1242 N NE2 . GLN B 58 ? 0.3956 0.3913 0.3370 -0.0139 0.0937 -0.0274 58 GLN B NE2 1243 N N . TYR B 59 ? 0.1577 0.1530 0.2530 0.0458 0.0527 0.0581 59 TYR B N 1244 C CA . TYR B 59 ? 0.1634 0.2017 0.2231 0.0622 0.0517 0.0535 59 TYR B CA 1245 C C . TYR B 59 ? 0.2246 0.2253 0.2494 0.0693 0.0431 0.0586 59 TYR B C 1246 O O . TYR B 59 ? 0.2291 0.3329 0.2833 0.1272 0.0640 0.1244 59 TYR B O 1247 C CB . TYR B 59 ? 0.1826 0.1958 0.2690 0.0611 0.0714 0.0578 59 TYR B CB 1248 C CG . TYR B 59 ? 0.1367 0.1944 0.2967 0.0014 0.0460 0.0564 59 TYR B CG 1249 C CD1 . TYR B 59 ? 0.2119 0.2254 0.2572 0.0188 0.0442 0.0826 59 TYR B CD1 1250 C CD2 . TYR B 59 ? 0.1425 0.2428 0.3373 0.0284 0.0351 0.0571 59 TYR B CD2 1251 C CE1 . TYR B 59 ? 0.1601 0.2575 0.2855 -0.0235 0.0325 0.0546 59 TYR B CE1 1252 C CE2 . TYR B 59 ? 0.1903 0.2540 0.3943 0.0160 -0.0422 0.0359 59 TYR B CE2 1253 C CZ . TYR B 59 ? 0.2468 0.3065 0.3929 0.0086 -0.0073 0.0493 59 TYR B CZ 1254 O OH . TYR B 59 ? 0.2798 0.3849 0.4603 -0.0472 -0.0325 0.0942 59 TYR B OH 1255 N N . ASP B 60 ? 0.2111 0.2011 0.2666 0.0429 0.0364 0.0436 60 ASP B N 1256 C CA . ASP B 60 ? 0.2552 0.2332 0.2648 0.0238 0.0529 0.0337 60 ASP B CA 1257 C C . ASP B 60 ? 0.2093 0.2121 0.2298 0.0404 0.0340 0.0348 60 ASP B C 1258 O O . ASP B 60 ? 0.1929 0.2181 0.2974 0.0458 0.0378 0.0443 60 ASP B O 1259 C CB . ASP B 60 ? 0.3853 0.2666 0.2384 -0.0180 0.0326 0.0385 60 ASP B CB 1260 C CG . ASP B 60 ? 0.3314 0.2965 0.3639 -0.0041 0.0566 0.0141 60 ASP B CG 1261 O OD1 . ASP B 60 ? 0.3634 0.3028 0.3829 -0.0014 0.0830 0.0278 60 ASP B OD1 1262 O OD2 . ASP B 60 ? 0.4927 0.2884 0.4240 0.0431 -0.0270 0.0183 60 ASP B OD2 1263 N N . GLN B 61 ? 0.2279 0.2035 0.2516 0.0332 0.0518 0.0416 61 GLN B N 1264 C CA . GLN B 61 ? 0.2504 0.2451 0.2375 0.0430 0.0784 0.0418 61 GLN B CA 1265 C C . GLN B 61 ? 0.2168 0.2230 0.2686 0.0480 0.0514 0.0687 61 GLN B C 1266 O O . GLN B 61 ? 0.2144 0.2487 0.3099 0.0475 0.1012 0.0175 61 GLN B O 1267 C CB . GLN B 61 ? 0.2911 0.2708 0.2895 0.0443 0.0745 0.0366 61 GLN B CB 1268 C CG . GLN B 61 ? 0.3209 0.3333 0.3826 0.0353 0.0689 -0.0387 61 GLN B CG 1269 C CD . GLN B 61 ? 0.4434 0.4535 0.4260 0.0216 -0.0093 -0.0139 61 GLN B CD 1270 O OE1 . GLN B 61 ? 0.4738 0.4963 0.4572 0.0860 -0.0082 -0.0331 61 GLN B OE1 1271 N NE2 . GLN B 61 ? 0.5047 0.3624 0.4172 0.0626 0.0077 -0.0150 61 GLN B NE2 1272 N N . ILE B 62 ? 0.1823 0.1762 0.2385 0.0364 0.0372 0.0441 62 ILE B N 1273 C CA . ILE B 62 ? 0.1560 0.1903 0.2141 0.0311 0.0270 0.0539 62 ILE B CA 1274 C C . ILE B 62 ? 0.1712 0.1786 0.2320 0.0433 0.0321 0.0464 62 ILE B C 1275 O O . ILE B 62 ? 0.1480 0.1916 0.2256 0.0368 0.0463 0.0583 62 ILE B O 1276 C CB . ILE B 62 ? 0.1762 0.2013 0.2057 0.0174 0.0193 0.0327 62 ILE B CB 1277 C CG1 . ILE B 62 ? 0.2062 0.1954 0.2143 0.0539 0.0231 0.0664 62 ILE B CG1 1278 C CG2 . ILE B 62 ? 0.2297 0.2108 0.2412 0.0139 0.0001 0.0530 62 ILE B CG2 1279 C CD1 . ILE B 62 ? 0.2100 0.2864 0.3170 0.0774 0.0284 0.1054 62 ILE B CD1 1280 N N . PRO B 63 ? 0.1725 0.2002 0.2271 0.0221 0.0245 0.0539 63 PRO B N 1281 C CA . PRO B 63 ? 0.1830 0.2048 0.2128 0.0266 0.0179 0.0641 63 PRO B CA 1282 C C . PRO B 63 ? 0.2122 0.2034 0.2642 0.0285 -0.0077 0.0423 63 PRO B C 1283 O O . PRO B 63 ? 0.3083 0.2191 0.2395 0.0684 0.0320 0.0500 63 PRO B O 1284 C CB . PRO B 63 ? 0.1997 0.2226 0.2090 -0.0158 0.0068 0.0739 63 PRO B CB 1285 C CG . PRO B 63 ? 0.1928 0.2420 0.3804 0.0172 0.0508 0.0836 63 PRO B CG 1286 C CD . PRO B 63 ? 0.1569 0.2093 0.2522 0.0091 0.0517 0.0494 63 PRO B CD 1287 N N . VAL B 64 ? 0.2311 0.2251 0.2553 0.0567 0.0463 0.0819 64 VAL B N 1288 C CA . VAL B 64 ? 0.2943 0.1840 0.2815 0.0427 0.0482 0.0684 64 VAL B CA 1289 C C . VAL B 64 ? 0.2495 0.2361 0.2939 0.0530 0.0679 0.0760 64 VAL B C 1290 O O . VAL B 64 ? 0.3748 0.2796 0.3088 0.1033 0.0719 0.0964 64 VAL B O 1291 C CB . VAL B 64 ? 0.2717 0.2374 0.3109 0.0539 0.0738 0.0670 64 VAL B CB 1292 C CG1 . VAL B 64 ? 0.2568 0.2346 0.3105 0.0111 0.1020 0.0754 64 VAL B CG1 1293 C CG2 . VAL B 64 ? 0.2577 0.2584 0.2967 0.0513 0.0709 0.0840 64 VAL B CG2 1294 N N A GLU B 65 ? 0.2318 0.2293 0.2674 0.0501 0.0908 0.0738 65 GLU B N 1295 N N B GLU B 65 ? 0.2082 0.2207 0.2802 0.0550 0.0789 0.0827 65 GLU B N 1296 C CA A GLU B 65 ? 0.2293 0.2306 0.2762 0.0555 0.0804 0.0562 65 GLU B CA 1297 C CA B GLU B 65 ? 0.2211 0.1999 0.2952 0.0436 0.0704 0.0597 65 GLU B CA 1298 C C A GLU B 65 ? 0.2256 0.2195 0.2743 0.0599 0.0762 0.0563 65 GLU B C 1299 C C B GLU B 65 ? 0.2297 0.2015 0.2961 0.0350 0.0812 0.0699 65 GLU B C 1300 O O A GLU B 65 ? 0.2481 0.2054 0.2780 0.0790 0.0628 0.0389 65 GLU B O 1301 O O B GLU B 65 ? 0.1734 0.1800 0.3512 0.0323 0.0470 0.0404 65 GLU B O 1302 C CB A GLU B 65 ? 0.2505 0.2023 0.2840 0.0439 0.0384 0.0315 65 GLU B CB 1303 C CB B GLU B 65 ? 0.2333 0.1933 0.3148 0.0510 0.0599 0.0455 65 GLU B CB 1304 C CG A GLU B 65 ? 0.2780 0.2563 0.2423 0.0301 0.0454 0.0197 65 GLU B CG 1305 C CG B GLU B 65 ? 0.2302 0.2496 0.2137 0.0302 0.0567 0.0457 65 GLU B CG 1306 C CD A GLU B 65 ? 0.3298 0.3459 0.3027 -0.0293 0.0319 0.0378 65 GLU B CD 1307 C CD B GLU B 65 ? 0.1755 0.2168 0.2405 0.0454 -0.0188 -0.0181 65 GLU B CD 1308 O OE1 A GLU B 65 ? 0.4465 0.4043 0.3923 0.0098 0.0244 -0.0243 65 GLU B OE1 1309 O OE1 B GLU B 65 ? 0.1691 0.2146 0.2379 -0.0281 0.0130 -0.0071 65 GLU B OE1 1310 O OE2 A GLU B 65 ? 0.3579 0.4162 0.3868 -0.0026 0.0555 -0.0457 65 GLU B OE2 1311 O OE2 B GLU B 65 ? 0.2313 0.2101 0.2288 0.0778 -0.0440 -0.0412 65 GLU B OE2 1312 N N . ILE B 66 ? 0.2349 0.2099 0.2545 0.0718 0.0961 0.0600 66 ILE B N 1313 C CA . ILE B 66 ? 0.2336 0.2447 0.2406 0.0640 0.0877 0.0476 66 ILE B CA 1314 C C . ILE B 66 ? 0.2426 0.2352 0.2722 0.0759 0.0402 0.0493 66 ILE B C 1315 O O . ILE B 66 ? 0.2563 0.2503 0.2728 0.0961 0.0895 0.0624 66 ILE B O 1316 C CB . ILE B 66 ? 0.2295 0.2209 0.2122 0.0726 0.0723 0.0460 66 ILE B CB 1317 C CG1 . ILE B 66 ? 0.2427 0.2436 0.2678 0.0638 0.1017 0.0353 66 ILE B CG1 1318 C CG2 . ILE B 66 ? 0.2461 0.2752 0.2253 0.0710 0.1104 0.0506 66 ILE B CG2 1319 C CD1 . ILE B 66 ? 0.2881 0.2827 0.3127 0.0380 0.0247 0.0774 66 ILE B CD1 1320 N N . CYS B 67 ? 0.2637 0.2627 0.3049 0.0806 0.0517 0.0385 67 CYS B N 1321 C CA . CYS B 67 ? 0.3267 0.2554 0.3403 0.0799 0.0405 0.0313 67 CYS B CA 1322 C C . CYS B 67 ? 0.3571 0.3104 0.3125 0.0759 0.0249 0.0521 67 CYS B C 1323 O O . CYS B 67 ? 0.4135 0.2659 0.3546 0.1135 0.0414 0.0884 67 CYS B O 1324 C CB . CYS B 67 ? 0.3423 0.2549 0.3180 0.1320 0.0563 0.0306 67 CYS B CB 1325 S SG . CYS B 67 ? 0.4058 0.3508 0.4272 0.1244 0.1242 0.1027 67 CYS B SG 1326 N N . GLY B 68 ? 0.3414 0.2873 0.3554 0.0499 0.0689 0.0530 68 GLY B N 1327 C CA . GLY B 68 ? 0.3637 0.3121 0.3517 -0.0175 0.0659 0.0604 68 GLY B CA 1328 C C . GLY B 68 ? 0.3095 0.3319 0.3635 0.0157 0.0831 0.0495 68 GLY B C 1329 O O . GLY B 68 ? 0.4132 0.4253 0.4242 -0.0508 0.1551 0.0923 68 GLY B O 1330 N N . HIS B 69 ? 0.3154 0.2228 0.2605 0.0604 0.0738 0.1037 69 HIS B N 1331 C CA . HIS B 69 ? 0.3153 0.2228 0.2823 0.0631 0.0653 0.0734 69 HIS B CA 1332 C C . HIS B 69 ? 0.3163 0.2137 0.2252 0.0782 0.1145 0.0819 69 HIS B C 1333 O O . HIS B 69 ? 0.3681 0.2466 0.2524 0.1339 0.1604 0.1093 69 HIS B O 1334 C CB . HIS B 69 ? 0.3408 0.2112 0.2814 0.0404 0.0597 0.0647 69 HIS B CB 1335 C CG . HIS B 69 ? 0.2968 0.2657 0.2829 0.0460 0.0620 0.0569 69 HIS B CG 1336 N ND1 . HIS B 69 ? 0.3247 0.2421 0.2694 0.0658 0.0779 0.0576 69 HIS B ND1 1337 C CD2 . HIS B 69 ? 0.3111 0.2729 0.3143 0.0295 0.0723 0.0602 69 HIS B CD2 1338 C CE1 . HIS B 69 ? 0.4315 0.2599 0.3331 0.0493 0.0043 0.0306 69 HIS B CE1 1339 N NE2 . HIS B 69 ? 0.2731 0.2421 0.3208 0.0280 0.0225 0.0424 69 HIS B NE2 1340 N N . LYS B 70 ? 0.2458 0.1999 0.2131 0.0568 0.0997 0.0675 70 LYS B N 1341 C CA . LYS B 70 ? 0.2124 0.2080 0.2253 0.0448 0.0730 0.0424 70 LYS B CA 1342 C C . LYS B 70 ? 0.2076 0.2343 0.2044 0.0493 0.0728 0.0492 70 LYS B C 1343 O O . LYS B 70 ? 0.2310 0.2265 0.2168 0.0410 0.0612 0.0686 70 LYS B O 1344 C CB . LYS B 70 ? 0.2020 0.2156 0.1940 0.0420 0.0592 0.0421 70 LYS B CB 1345 C CG . LYS B 70 ? 0.2521 0.1859 0.2071 0.0296 0.0496 0.0207 70 LYS B CG 1346 C CD . LYS B 70 ? 0.1976 0.2408 0.2399 0.0152 0.0715 0.0215 70 LYS B CD 1347 C CE . LYS B 70 ? 0.2317 0.2725 0.2663 0.0160 0.0246 -0.0002 70 LYS B CE 1348 N NZ . LYS B 70 ? 0.2916 0.2746 0.4263 -0.0006 0.0389 0.0409 70 LYS B NZ 1349 N N . ALA B 71 ? 0.2192 0.2133 0.2578 0.0408 0.0525 0.0841 71 ALA B N 1350 C CA . ALA B 71 ? 0.1820 0.2147 0.2670 0.0477 0.0427 0.0558 71 ALA B CA 1351 C C . ALA B 71 ? 0.1688 0.1606 0.2107 0.0386 0.0489 0.0300 71 ALA B C 1352 O O . ALA B 71 ? 0.1899 0.1981 0.2246 0.0281 0.0564 0.0616 71 ALA B O 1353 C CB . ALA B 71 ? 0.1924 0.2348 0.3045 0.0636 0.0645 0.0850 71 ALA B CB 1354 N N . ILE B 72 ? 0.1637 0.1837 0.2301 0.0337 0.0457 0.0543 72 ILE B N 1355 C CA . ILE B 72 ? 0.1661 0.1733 0.2167 0.0410 0.0516 0.0341 72 ILE B CA 1356 C C . ILE B 72 ? 0.1697 0.1787 0.1684 0.0313 0.0354 0.0385 72 ILE B C 1357 O O . ILE B 72 ? 0.1809 0.2162 0.2069 0.0440 0.0256 0.0417 72 ILE B O 1358 C CB . ILE B 72 ? 0.1727 0.2039 0.2187 0.0392 0.0454 0.0459 72 ILE B CB 1359 C CG1 . ILE B 72 ? 0.1666 0.2208 0.2499 0.0474 0.0614 0.0326 72 ILE B CG1 1360 C CG2 . ILE B 72 ? 0.2168 0.2509 0.2454 0.0372 0.0325 0.0431 72 ILE B CG2 1361 C CD1 . ILE B 72 ? 0.1978 0.2266 0.2644 0.0426 0.0567 0.0361 72 ILE B CD1 1362 N N . GLY B 73 ? 0.1769 0.2042 0.1834 0.0418 0.0410 0.0543 73 GLY B N 1363 C CA . GLY B 73 ? 0.1714 0.1946 0.2308 0.0540 0.0443 0.0265 73 GLY B CA 1364 C C . GLY B 73 ? 0.1448 0.1914 0.1780 0.0333 0.0367 0.0135 73 GLY B C 1365 O O . GLY B 73 ? 0.1806 0.1987 0.2030 0.0205 0.0334 0.0646 73 GLY B O 1366 N N . THR B 74 ? 0.1826 0.1878 0.2203 0.0604 0.0243 0.0372 74 THR B N 1367 C CA . THR B 74 ? 0.1914 0.1773 0.2030 0.0335 0.0324 0.0387 74 THR B CA 1368 C C . THR B 74 ? 0.1626 0.1565 0.1801 0.0141 0.0366 0.0282 74 THR B C 1369 O O . THR B 74 ? 0.1620 0.1909 0.1944 0.0425 0.0338 0.0351 74 THR B O 1370 C CB . THR B 74 ? 0.2493 0.1966 0.2093 -0.0037 0.0337 0.0241 74 THR B CB 1371 O OG1 . THR B 74 ? 0.3665 0.2022 0.2632 0.0054 0.0471 0.0097 74 THR B OG1 1372 C CG2 . THR B 74 ? 0.3095 0.2198 0.2637 -0.0015 0.0574 0.0773 74 THR B CG2 1373 N N . VAL B 75 ? 0.1583 0.1751 0.1903 0.0296 0.0338 0.0503 75 VAL B N 1374 C CA . VAL B 75 ? 0.1530 0.1596 0.1950 0.0315 0.0006 0.0532 75 VAL B CA 1375 C C . VAL B 75 ? 0.1421 0.1562 0.1981 0.0485 0.0092 0.0218 75 VAL B C 1376 O O . VAL B 75 ? 0.1642 0.1777 0.2412 0.0602 0.0356 0.0761 75 VAL B O 1377 C CB . VAL B 75 ? 0.2094 0.1751 0.2665 0.0241 0.0011 0.0607 75 VAL B CB 1378 C CG1 . VAL B 75 ? 0.2526 0.2072 0.2868 0.0013 0.0237 0.0690 75 VAL B CG1 1379 C CG2 . VAL B 75 ? 0.2293 0.1626 0.2220 -0.0048 0.0069 0.0423 75 VAL B CG2 1380 N N . LEU B 76 ? 0.1221 0.1326 0.1865 0.0374 -0.0028 0.0407 76 LEU B N 1381 C CA . LEU B 76 ? 0.1270 0.1314 0.1884 0.0314 -0.0055 0.0269 76 LEU B CA 1382 C C . LEU B 76 ? 0.1745 0.1533 0.1765 0.0304 -0.0080 0.0114 76 LEU B C 1383 O O . LEU B 76 ? 0.2092 0.1521 0.2480 0.0507 -0.0540 -0.0027 76 LEU B O 1384 C CB . LEU B 76 ? 0.1421 0.1239 0.1592 0.0161 0.0125 0.0253 76 LEU B CB 1385 C CG . LEU B 76 ? 0.1300 0.1588 0.1520 0.0212 0.0164 0.0175 76 LEU B CG 1386 C CD1 . LEU B 76 ? 0.1443 0.1532 0.1549 0.0092 0.0038 0.0233 76 LEU B CD1 1387 C CD2 . LEU B 76 ? 0.1317 0.1879 0.1445 0.0367 0.0007 0.0030 76 LEU B CD2 1388 N N . VAL B 77 ? 0.1453 0.1319 0.1782 -0.0013 -0.0266 0.0252 77 VAL B N 1389 C CA . VAL B 77 ? 0.1211 0.1438 0.1652 0.0108 -0.0110 0.0165 77 VAL B CA 1390 C C . VAL B 77 ? 0.1400 0.1588 0.1738 -0.0123 -0.0165 0.0194 77 VAL B C 1391 O O . VAL B 77 ? 0.1517 0.1318 0.1992 0.0075 -0.0179 0.0286 77 VAL B O 1392 C CB . VAL B 77 ? 0.1418 0.1631 0.2255 0.0137 -0.0185 0.0329 77 VAL B CB 1393 C CG1 . VAL B 77 ? 0.1432 0.2036 0.1961 -0.0152 -0.0194 0.0376 77 VAL B CG1 1394 C CG2 . VAL B 77 ? 0.1462 0.1873 0.1946 -0.0172 -0.0167 0.0118 77 VAL B CG2 1395 N N . GLY B 78 ? 0.1449 0.1297 0.1748 -0.0017 0.0049 0.0327 78 GLY B N 1396 C CA . GLY B 78 ? 0.1401 0.1653 0.1655 0.0007 -0.0121 0.0232 78 GLY B CA 1397 C C . GLY B 78 ? 0.1458 0.1676 0.1566 0.0032 -0.0181 0.0218 78 GLY B C 1398 O O . GLY B 78 ? 0.1452 0.1649 0.1873 0.0090 -0.0085 0.0247 78 GLY B O 1399 N N . PRO B 79 ? 0.1657 0.1753 0.1404 0.0196 -0.0215 0.0346 79 PRO B N 1400 C CA . PRO B 79 ? 0.1713 0.1617 0.1449 0.0187 -0.0251 0.0150 79 PRO B CA 1401 C C . PRO B 79 ? 0.1846 0.1598 0.1431 0.0266 0.0040 0.0018 79 PRO B C 1402 O O . PRO B 79 ? 0.1903 0.2275 0.1494 0.0433 0.0054 0.0374 79 PRO B O 1403 C CB . PRO B 79 ? 0.1775 0.2111 0.1596 0.0072 -0.0134 0.0370 79 PRO B CB 1404 C CG . PRO B 79 ? 0.1963 0.1698 0.1537 0.0061 -0.0110 0.0230 79 PRO B CG 1405 C CD . PRO B 79 ? 0.1775 0.1752 0.1810 0.0046 -0.0020 0.0359 79 PRO B CD 1406 N N . THR B 80 ? 0.1513 0.1830 0.1620 0.0208 -0.0013 0.0442 80 THR B N 1407 C CA . THR B 80 ? 0.1455 0.1854 0.1410 0.0109 -0.0041 0.0246 80 THR B CA 1408 C C . THR B 80 ? 0.1641 0.1838 0.1697 0.0335 -0.0159 0.0429 80 THR B C 1409 O O . THR B 80 ? 0.2119 0.1959 0.1629 0.0182 -0.0394 0.0163 80 THR B O 1410 C CB . THR B 80 ? 0.1578 0.1791 0.1336 0.0066 0.0102 0.0292 80 THR B CB 1411 O OG1 . THR B 80 ? 0.1504 0.2002 0.1567 0.0295 -0.0131 0.0371 80 THR B OG1 1412 C CG2 . THR B 80 ? 0.1535 0.1529 0.1850 0.0123 -0.0060 0.0221 80 THR B CG2 1413 N N . PRO B 81 ? 0.2170 0.2475 0.1332 0.0361 -0.0296 0.0049 81 PRO B N 1414 C CA . PRO B 81 ? 0.2549 0.2327 0.1516 0.0624 -0.0283 0.0013 81 PRO B CA 1415 C C . PRO B 81 ? 0.2688 0.2395 0.1633 0.0574 -0.0513 0.0041 81 PRO B C 1416 O O . PRO B 81 ? 0.3076 0.2776 0.1654 0.0547 -0.0722 -0.0132 81 PRO B O 1417 C CB . PRO B 81 ? 0.2578 0.2437 0.1803 0.0342 -0.0135 0.0227 81 PRO B CB 1418 C CG . PRO B 81 ? 0.2240 0.3284 0.2255 0.0678 -0.0334 -0.0196 81 PRO B CG 1419 C CD . PRO B 81 ? 0.1758 0.2754 0.1594 0.0652 0.0318 0.0359 81 PRO B CD 1420 N N A VAL B 82 ? 0.2543 0.2141 0.1358 0.0410 -0.0664 -0.0018 82 VAL B N 1421 N N B VAL B 82 ? 0.2549 0.2110 0.1347 0.0411 -0.0699 0.0026 82 VAL B N 1422 C CA A VAL B 82 ? 0.2267 0.2012 0.1703 0.0438 -0.0396 0.0023 82 VAL B CA 1423 C CA B VAL B 82 ? 0.2321 0.1891 0.1669 0.0405 -0.0477 0.0049 82 VAL B CA 1424 C C A VAL B 82 ? 0.1815 0.1684 0.1362 0.0134 -0.0509 -0.0065 82 VAL B C 1425 C C B VAL B 82 ? 0.1891 0.1629 0.1433 0.0172 -0.0510 -0.0014 82 VAL B C 1426 O O A VAL B 82 ? 0.2410 0.1425 0.1686 0.0042 -0.0199 0.0045 82 VAL B O 1427 O O B VAL B 82 ? 0.2405 0.1419 0.1702 0.0038 -0.0214 0.0046 82 VAL B O 1428 C CB A VAL B 82 ? 0.2388 0.1913 0.1666 0.0446 -0.0469 0.0084 82 VAL B CB 1429 C CB B VAL B 82 ? 0.2503 0.1671 0.1823 0.0381 -0.0536 0.0297 82 VAL B CB 1430 C CG1 A VAL B 82 ? 0.2506 0.2406 0.2485 0.0392 -0.0121 0.0109 82 VAL B CG1 1431 C CG1 B VAL B 82 ? 0.2562 0.1878 0.1483 0.0608 -0.0122 0.0295 82 VAL B CG1 1432 C CG2 A VAL B 82 ? 0.1689 0.2596 0.1584 -0.0075 -0.0166 0.0685 82 VAL B CG2 1433 C CG2 B VAL B 82 ? 0.2035 0.1723 0.2737 -0.0093 -0.0408 0.0231 82 VAL B CG2 1434 N N . ASN B 83 ? 0.1975 0.1565 0.1568 -0.0015 -0.0590 -0.0100 83 ASN B N 1435 C CA . ASN B 83 ? 0.1851 0.1439 0.1659 0.0116 -0.0438 -0.0029 83 ASN B CA 1436 C C . ASN B 83 ? 0.1485 0.1257 0.1435 0.0103 -0.0311 0.0072 83 ASN B C 1437 O O . ASN B 83 ? 0.1941 0.1171 0.1567 0.0091 -0.0254 0.0032 83 ASN B O 1438 C CB . ASN B 83 ? 0.1674 0.1673 0.2057 0.0118 -0.0501 0.0149 83 ASN B CB 1439 C CG . ASN B 83 ? 0.2031 0.1591 0.1695 0.0179 -0.0482 0.0175 83 ASN B CG 1440 O OD1 . ASN B 83 ? 0.1966 0.1724 0.2304 0.0066 -0.0643 0.0209 83 ASN B OD1 1441 N ND2 . ASN B 83 ? 0.2127 0.1966 0.2621 -0.0174 -0.0869 -0.0054 83 ASN B ND2 1442 N N . ILE B 84 ? 0.1544 0.1204 0.1259 0.0159 -0.0275 0.0088 84 ILE B N 1443 C CA . ILE B 84 ? 0.1441 0.1185 0.1286 0.0132 -0.0238 0.0035 84 ILE B CA 1444 C C . ILE B 84 ? 0.1486 0.1138 0.1447 0.0133 -0.0028 -0.0015 84 ILE B C 1445 O O . ILE B 84 ? 0.1621 0.1368 0.1355 0.0457 0.0062 0.0246 84 ILE B O 1446 C CB . ILE B 84 ? 0.1324 0.1383 0.1366 0.0291 -0.0147 0.0092 84 ILE B CB 1447 C CG1 . ILE B 84 ? 0.1434 0.1760 0.1597 0.0037 -0.0208 -0.0020 84 ILE B CG1 1448 C CG2 . ILE B 84 ? 0.1527 0.1621 0.1590 0.0182 -0.0098 -0.0192 84 ILE B CG2 1449 C CD1 . ILE B 84 ? 0.1462 0.1902 0.1814 0.0070 0.0180 -0.0159 84 ILE B CD1 1450 N N . ILE B 85 ? 0.1367 0.1098 0.1412 0.0270 0.0014 0.0002 85 ILE B N 1451 C CA . ILE B 85 ? 0.1419 0.1255 0.1398 0.0246 0.0186 0.0073 85 ILE B CA 1452 C C . ILE B 85 ? 0.1314 0.1379 0.1050 0.0198 0.0294 0.0061 85 ILE B C 1453 O O . ILE B 85 ? 0.1266 0.1395 0.1494 0.0326 0.0132 -0.0060 85 ILE B O 1454 C CB . ILE B 85 ? 0.1633 0.1474 0.1484 0.0095 0.0137 0.0168 85 ILE B CB 1455 C CG1 . ILE B 85 ? 0.2090 0.1412 0.2284 -0.0120 -0.0047 0.0322 85 ILE B CG1 1456 C CG2 . ILE B 85 ? 0.1481 0.1689 0.1649 0.0120 0.0474 0.0429 85 ILE B CG2 1457 C CD1 . ILE B 85 ? 0.2246 0.1857 0.2980 -0.0188 -0.0631 0.0190 85 ILE B CD1 1458 N N . GLY B 86 ? 0.1415 0.1159 0.1248 0.0315 0.0104 0.0026 86 GLY B N 1459 C CA . GLY B 86 ? 0.1661 0.1230 0.0901 0.0271 0.0169 0.0092 86 GLY B CA 1460 C C . GLY B 86 ? 0.1304 0.1351 0.1076 0.0316 0.0192 0.0060 86 GLY B C 1461 O O . GLY B 86 ? 0.1517 0.1370 0.1290 0.0313 0.0162 0.0185 86 GLY B O 1462 N N . ARG B 87 ? 0.1500 0.1486 0.1045 0.0276 0.0144 0.0152 87 ARG B N 1463 C CA . ARG B 87 ? 0.1486 0.1670 0.0872 0.0412 0.0078 -0.0027 87 ARG B CA 1464 C C . ARG B 87 ? 0.1803 0.1745 0.1153 0.0471 0.0062 0.0154 87 ARG B C 1465 O O . ARG B 87 ? 0.1862 0.2188 0.1209 0.0632 0.0313 0.0364 87 ARG B O 1466 C CB . ARG B 87 ? 0.1856 0.1374 0.0801 0.0382 0.0133 -0.0040 87 ARG B CB 1467 C CG . ARG B 87 ? 0.1563 0.1597 0.1257 0.0285 0.0028 -0.0099 87 ARG B CG 1468 C CD . ARG B 87 ? 0.1754 0.1732 0.1189 0.0493 0.0003 0.0067 87 ARG B CD 1469 N NE . ARG B 87 ? 0.1897 0.1676 0.1358 0.0249 -0.0150 -0.0309 87 ARG B NE 1470 C CZ . ARG B 87 ? 0.2167 0.1799 0.1374 0.0377 -0.0048 -0.0054 87 ARG B CZ 1471 N NH1 . ARG B 87 ? 0.2423 0.1653 0.1449 0.0477 -0.0104 -0.0390 87 ARG B NH1 1472 N NH2 . ARG B 87 ? 0.2707 0.1662 0.1411 0.0152 -0.0081 -0.0344 87 ARG B NH2 1473 N N . ASN B 88 ? 0.1733 0.1612 0.0898 0.0497 0.0240 0.0034 88 ASN B N 1474 C CA . ASN B 88 ? 0.1802 0.1709 0.1362 0.0426 0.0377 -0.0222 88 ASN B CA 1475 C C . ASN B 88 ? 0.2034 0.1895 0.1082 0.0587 0.0358 0.0294 88 ASN B C 1476 O O . ASN B 88 ? 0.2168 0.2298 0.1448 0.0667 0.0793 0.0250 88 ASN B O 1477 C CB . ASN B 88 ? 0.1684 0.1461 0.1712 0.0476 0.0432 -0.0024 88 ASN B CB 1478 C CG . ASN B 88 ? 0.1753 0.1619 0.1752 0.0299 0.0338 0.0443 88 ASN B CG 1479 O OD1 . ASN B 88 ? 0.1780 0.1641 0.1361 0.0413 0.0330 0.0158 88 ASN B OD1 1480 N ND2 . ASN B 88 ? 0.1591 0.1843 0.1720 0.0516 0.0315 0.0389 88 ASN B ND2 1481 N N . LEU B 89 ? 0.1677 0.1803 0.1457 0.0518 0.0506 0.0166 89 LEU B N 1482 C CA . LEU B 89 ? 0.1803 0.2000 0.1484 0.0535 0.0568 0.0385 89 LEU B CA 1483 C C . LEU B 89 ? 0.1945 0.1956 0.1333 0.0665 0.0623 0.0311 89 LEU B C 1484 O O . LEU B 89 ? 0.1965 0.2276 0.1525 0.0548 0.0746 0.0612 89 LEU B O 1485 C CB . LEU B 89 ? 0.1615 0.1784 0.1765 0.0482 0.0664 0.0423 89 LEU B CB 1486 C CG . LEU B 89 ? 0.1501 0.1825 0.1787 0.0360 0.0386 0.0289 89 LEU B CG 1487 C CD1 . LEU B 89 ? 0.1678 0.1960 0.2199 0.0145 0.0507 0.0763 89 LEU B CD1 1488 C CD2 . LEU B 89 ? 0.1678 0.2036 0.1988 0.0452 0.0588 0.0520 89 LEU B CD2 1489 N N . LEU B 90 ? 0.1742 0.1651 0.1274 0.0459 0.0438 0.0380 90 LEU B N 1490 C CA . LEU B 90 ? 0.1770 0.1769 0.1200 0.0355 0.0328 0.0375 90 LEU B CA 1491 C C . LEU B 90 ? 0.1879 0.1987 0.1254 0.0491 0.0548 0.0487 90 LEU B C 1492 O O . LEU B 90 ? 0.2232 0.2357 0.1503 0.0902 0.0749 0.0663 90 LEU B O 1493 C CB . LEU B 90 ? 0.1476 0.1638 0.1256 0.0394 0.0316 0.0295 90 LEU B CB 1494 C CG . LEU B 90 ? 0.1586 0.1428 0.1294 0.0344 0.0303 0.0196 90 LEU B CG 1495 C CD1 . LEU B 90 ? 0.1728 0.1777 0.0801 0.0364 0.0218 0.0012 90 LEU B CD1 1496 C CD2 . LEU B 90 ? 0.1530 0.1746 0.1425 0.0306 0.0294 0.0124 90 LEU B CD2 1497 N N . THR B 91 ? 0.2234 0.2117 0.1214 0.0715 0.0276 0.0423 91 THR B N 1498 C CA . THR B 91 ? 0.2097 0.3000 0.1169 0.0869 0.0320 0.0220 91 THR B CA 1499 C C . THR B 91 ? 0.1983 0.3310 0.1231 0.0955 0.0416 0.0170 91 THR B C 1500 O O . THR B 91 ? 0.2387 0.3357 0.1202 0.0944 0.0474 0.0416 91 THR B O 1501 C CB . THR B 91 ? 0.2453 0.3314 0.1408 0.0818 0.0052 -0.0007 91 THR B CB 1502 O OG1 . THR B 91 ? 0.2913 0.2927 0.1732 0.1323 0.0135 -0.0282 91 THR B OG1 1503 C CG2 . THR B 91 ? 0.2958 0.2824 0.1217 0.0709 0.0061 -0.0112 91 THR B CG2 1504 N N . GLN B 92 ? 0.2180 0.2773 0.1403 0.1175 0.0545 0.0511 92 GLN B N 1505 C CA . GLN B 92 ? 0.2286 0.2876 0.1729 0.0894 0.0674 0.0310 92 GLN B CA 1506 C C . GLN B 92 ? 0.2299 0.3023 0.2100 0.0857 0.0860 0.0736 92 GLN B C 1507 O O . GLN B 92 ? 0.2789 0.3456 0.1951 0.1024 0.1129 0.1072 92 GLN B O 1508 C CB . GLN B 92 ? 0.2097 0.2720 0.1722 0.0740 0.0709 0.0735 92 GLN B CB 1509 C CG . GLN B 92 ? 0.2104 0.2700 0.2014 0.0590 0.0709 0.0652 92 GLN B CG 1510 C CD . GLN B 92 ? 0.2444 0.2535 0.1606 0.0342 0.0191 0.0509 92 GLN B CD 1511 O OE1 . GLN B 92 ? 0.2379 0.2625 0.3855 0.0347 -0.0073 0.1046 92 GLN B OE1 1512 N NE2 . GLN B 92 ? 0.3164 0.2507 0.3479 0.0619 -0.0722 -0.0076 92 GLN B NE2 1513 N N . ILE B 93 ? 0.2357 0.2688 0.2201 0.1143 0.1103 0.0788 93 ILE B N 1514 C CA . ILE B 93 ? 0.2331 0.2779 0.2770 0.0675 0.0841 0.0740 93 ILE B CA 1515 C C . ILE B 93 ? 0.2569 0.3049 0.2159 0.0732 0.1071 0.0692 93 ILE B C 1516 O O . ILE B 93 ? 0.3630 0.3150 0.2534 0.1295 0.1299 0.1095 93 ILE B O 1517 C CB . ILE B 93 ? 0.2458 0.2172 0.2863 0.0607 0.0990 0.0763 93 ILE B CB 1518 C CG1 . ILE B 93 ? 0.2528 0.2707 0.2207 0.0561 0.0983 0.0649 93 ILE B CG1 1519 C CG2 . ILE B 93 ? 0.2574 0.2782 0.2479 0.0584 0.0884 0.0579 93 ILE B CG2 1520 C CD1 . ILE B 93 ? 0.2588 0.2252 0.3191 0.0084 0.1058 0.0312 93 ILE B CD1 1521 N N . GLY B 94 ? 0.2380 0.3020 0.1889 0.1028 0.0984 0.0809 94 GLY B N 1522 C CA . GLY B 94 ? 0.2784 0.3149 0.2335 0.1338 0.0723 0.0983 94 GLY B CA 1523 C C . GLY B 94 ? 0.2687 0.3063 0.1797 0.1249 0.0867 0.0866 94 GLY B C 1524 O O . GLY B 94 ? 0.2818 0.3326 0.2177 0.1516 0.1095 0.1426 94 GLY B O 1525 N N . CYS B 95 ? 0.2678 0.2794 0.1582 0.1278 0.0623 0.0687 95 CYS B N 1526 C CA . CYS B 95 ? 0.2586 0.2300 0.1725 0.0914 0.0679 0.0421 95 CYS B CA 1527 C C . CYS B 95 ? 0.2527 0.2284 0.1606 0.0763 0.0732 0.0515 95 CYS B C 1528 O O . CYS B 95 ? 0.3119 0.2412 0.2091 0.0998 0.1096 0.0531 95 CYS B O 1529 C CB . CYS B 95 ? 0.2704 0.2173 0.1704 0.0681 0.0439 0.0767 95 CYS B CB 1530 S SG . CYS B 95 ? 0.2267 0.2733 0.2071 0.0934 0.0704 0.0656 95 CYS B SG 1531 N N . THR B 96 ? 0.2564 0.2249 0.1277 0.0883 0.0528 0.0477 96 THR B N 1532 C CA . THR B 96 ? 0.2701 0.2136 0.1407 0.0669 0.0157 0.0266 96 THR B CA 1533 C C . THR B 96 ? 0.2223 0.1846 0.0933 0.0505 0.0133 0.0199 96 THR B C 1534 O O . THR B 96 ? 0.2240 0.2149 0.1259 0.0489 0.0214 0.0172 96 THR B O 1535 C CB . THR B 96 ? 0.3047 0.2788 0.1192 0.0682 0.0400 0.0271 96 THR B CB 1536 O OG1 . THR B 96 ? 0.2795 0.2664 0.1600 0.0692 0.0367 0.0568 96 THR B OG1 1537 C CG2 . THR B 96 ? 0.3503 0.2904 0.1619 0.0687 0.0459 -0.0063 96 THR B CG2 1538 N N . LEU B 97 ? 0.2391 0.1775 0.1399 0.0515 0.0209 0.0148 97 LEU B N 1539 C CA . LEU B 97 ? 0.2119 0.1810 0.1264 0.0401 0.0163 0.0044 97 LEU B CA 1540 C C . LEU B 97 ? 0.2285 0.1831 0.1519 0.0417 0.0108 0.0072 97 LEU B C 1541 O O . LEU B 97 ? 0.2741 0.1926 0.2056 0.0545 -0.0328 -0.0211 97 LEU B O 1542 C CB . LEU B 97 ? 0.2300 0.1929 0.1861 0.0270 0.0080 0.0178 97 LEU B CB 1543 C CG . LEU B 97 ? 0.1976 0.2223 0.1900 0.0284 -0.0099 -0.0098 97 LEU B CG 1544 C CD1 . LEU B 97 ? 0.2533 0.2486 0.2291 0.0109 0.0063 0.0515 97 LEU B CD1 1545 C CD2 . LEU B 97 ? 0.2559 0.2702 0.1442 0.0409 0.0045 0.0166 97 LEU B CD2 1546 N N . ASN B 98 ? 0.2589 0.1870 0.1250 0.0528 0.0153 0.0208 98 ASN B N 1547 C CA . ASN B 98 ? 0.2654 0.2145 0.1598 0.0619 0.0143 0.0359 98 ASN B CA 1548 C C . ASN B 98 ? 0.2352 0.2055 0.1770 0.0545 0.0111 0.0151 98 ASN B C 1549 O O . ASN B 98 ? 0.2494 0.2205 0.1773 0.0639 -0.0005 0.0223 98 ASN B O 1550 C CB . ASN B 98 ? 0.2131 0.2400 0.1703 0.0612 0.0057 0.0223 98 ASN B CB 1551 C CG . ASN B 98 ? 0.2763 0.2354 0.1463 0.0672 0.0244 0.0260 98 ASN B CG 1552 O OD1 . ASN B 98 ? 0.2948 0.3043 0.2057 0.0974 0.0164 0.0467 98 ASN B OD1 1553 N ND2 . ASN B 98 ? 0.3211 0.3259 0.1510 0.0316 0.0363 0.0506 98 ASN B ND2 1554 N N . PHE B 99 ? 0.2538 0.2503 0.2195 0.0610 -0.0042 0.0184 99 PHE B N 1555 C CA . PHE B 99 ? 0.2428 0.2636 0.2254 0.0497 0.0051 0.0213 99 PHE B CA 1556 C C . PHE B 99 ? 0.2755 0.3459 0.2750 0.0389 -0.0084 0.0119 99 PHE B C 1557 O O . PHE B 99 ? 0.3025 0.3880 0.3110 0.0792 -0.0180 0.0725 99 PHE B O 1558 C CB . PHE B 99 ? 0.2170 0.2672 0.2357 0.0587 -0.0100 0.0132 99 PHE B CB 1559 C CG . PHE B 99 ? 0.2544 0.2764 0.2326 0.0458 -0.0215 0.0229 99 PHE B CG 1560 C CD1 . PHE B 99 ? 0.2842 0.2443 0.2135 0.0467 -0.0389 0.0200 99 PHE B CD1 1561 C CD2 . PHE B 99 ? 0.2672 0.2564 0.3139 0.0206 -0.0244 0.0400 99 PHE B CD2 1562 C CE1 . PHE B 99 ? 0.2856 0.2490 0.2639 0.0510 -0.0248 0.0507 99 PHE B CE1 1563 C CE2 . PHE B 99 ? 0.2734 0.2704 0.3280 0.0029 -0.0455 0.0147 99 PHE B CE2 1564 C CZ . PHE B 99 ? 0.3176 0.2409 0.3382 0.0184 -0.0069 -0.0154 99 PHE B CZ 1565 O OXT . PHE B 99 ? 0.3057 0.3529 0.2544 0.0526 -0.0310 0.0201 99 PHE B OXT 1566 P P . PO4 C . ? 0.7425 0.4338 0.6542 -0.0728 -0.0211 -0.0475 502 PO4 A P 1567 O O1 . PO4 C . ? 0.5708 0.2636 0.2942 0.0169 -0.0226 -0.0847 502 PO4 A O1 1568 O O2 . PO4 C . ? 0.7216 0.5665 0.6553 -0.0804 -0.0686 -0.0322 502 PO4 A O2 1569 O O3 . PO4 C . ? 0.7234 0.5416 0.7680 0.0228 -0.0110 0.0241 502 PO4 A O3 1570 O O4 . PO4 C . ? 0.7180 0.5767 0.6669 -0.0170 -0.0184 0.0195 502 PO4 A O4 1571 P P . PO4 D . ? 0.5222 0.3664 0.6432 -0.0743 -0.0338 0.1127 504 PO4 A P 1572 O O1 . PO4 D . ? 0.3264 0.2652 0.4633 -0.0286 -0.0505 0.0472 504 PO4 A O1 1573 O O2 . PO4 D . ? 0.5823 0.6185 0.6338 -0.0052 -0.0481 -0.0028 504 PO4 A O2 1574 O O3 . PO4 D . ? 0.5603 0.4123 0.7036 0.0370 0.0026 0.0345 504 PO4 A O3 1575 O O4 . PO4 D . ? 0.6722 0.6316 0.6311 -0.0268 0.0083 0.0360 504 PO4 A O4 1576 P P . PO4 E . ? 0.4814 0.5880 0.8055 -0.0096 -0.0819 0.0401 505 PO4 A P 1577 O O1 . PO4 E . ? 0.2836 0.5070 0.5767 0.0113 -0.0781 0.1030 505 PO4 A O1 1578 O O2 . PO4 E . ? 0.6372 0.5473 0.7607 -0.0361 -0.0122 -0.0185 505 PO4 A O2 1579 O O3 . PO4 E . ? 0.5555 0.5214 0.8054 0.0303 -0.0639 -0.0007 505 PO4 A O3 1580 O O4 . PO4 E . ? 0.6207 0.7035 0.7727 -0.0288 0.0310 0.0416 505 PO4 A O4 1581 N N1 . 017 F . ? 0.1726 0.1789 0.2057 0.0346 0.0395 0.0012 1200 017 A N1 1582 C C2 . 017 F . ? 0.1584 0.1675 0.1658 0.0405 0.0179 0.0005 1200 017 A C2 1583 C C3 . 017 F . ? 0.1719 0.1582 0.1495 0.0369 -0.0308 -0.0010 1200 017 A C3 1584 C C4 . 017 F . ? 0.1408 0.1448 0.1645 0.0416 -0.0079 0.0009 1200 017 A C4 1585 C C5 . 017 F . ? 0.1451 0.1355 0.1300 0.0269 -0.0033 -0.0005 1200 017 A C5 1586 C C6 . 017 F . ? 0.1658 0.1686 0.1863 0.0473 0.0126 0.0250 1200 017 A C6 1587 C C7 . 017 F . ? 0.1909 0.1699 0.1726 0.0543 0.0239 0.0297 1200 017 A C7 1588 S S8 . 017 F . ? 0.1418 0.1164 0.1278 0.0192 0.0106 0.0157 1200 017 A S8 1589 O O9 . 017 F . ? 0.1718 0.1349 0.1233 0.0111 0.0239 0.0206 1200 017 A O9 1590 O O10 . 017 F . ? 0.1475 0.1384 0.1478 0.0321 -0.0121 0.0141 1200 017 A O10 1591 N N11 . 017 F . ? 0.1446 0.1137 0.1227 0.0134 0.0029 0.0015 1200 017 A N11 1592 C C12 . 017 F . ? 0.1507 0.1407 0.1538 0.0167 -0.0046 0.0061 1200 017 A C12 1593 C C13 . 017 F . ? 0.1317 0.1365 0.1505 0.0056 -0.0113 0.0167 1200 017 A C13 1594 C C14 . 017 F . ? 0.1555 0.1426 0.1627 -0.0039 0.0102 0.0230 1200 017 A C14 1595 C C15 . 017 F . ? 0.1486 0.1458 0.1645 0.0002 -0.0205 0.0083 1200 017 A C15 1596 C C16 . 017 F . ? 0.1280 0.1120 0.1082 0.0086 0.0053 0.0135 1200 017 A C16 1597 C C17 . 017 F . ? 0.1240 0.1147 0.0861 0.0126 0.0011 0.0147 1200 017 A C17 1598 O O18 . 017 F . ? 0.1295 0.1260 0.1068 0.0195 -0.0097 0.0098 1200 017 A O18 1599 C C19 . 017 F . ? 0.1096 0.1073 0.1034 0.0180 -0.0016 0.0070 1200 017 A C19 1600 N N20 . 017 F . ? 0.1143 0.1204 0.0989 0.0058 0.0000 0.0148 1200 017 A N20 1601 C C21 . 017 F . ? 0.1315 0.1111 0.1118 0.0090 0.0042 0.0188 1200 017 A C21 1602 O O22 . 017 F . ? 0.1302 0.1143 0.1235 0.0184 0.0186 0.0227 1200 017 A O22 1603 O O23 . 017 F . ? 0.1196 0.1329 0.1145 0.0242 0.0168 0.0154 1200 017 A O23 1604 C C24 . 017 F . ? 0.1240 0.1372 0.1232 0.0144 0.0261 0.0278 1200 017 A C24 1605 C C25 . 017 F . ? 0.1165 0.1457 0.1352 0.0090 0.0147 0.0165 1200 017 A C25 1606 O O26 . 017 F . ? 0.1188 0.1459 0.1185 0.0130 -0.0049 0.0122 1200 017 A O26 1607 C C27 . 017 F . ? 0.1408 0.1362 0.1110 0.0288 0.0163 0.0049 1200 017 A C27 1608 O O28 . 017 F . ? 0.1465 0.1407 0.1254 0.0045 -0.0125 0.0071 1200 017 A O28 1609 C C29 . 017 F . ? 0.1203 0.1440 0.1400 0.0120 -0.0093 0.0088 1200 017 A C29 1610 C C30 . 017 F . ? 0.1355 0.1548 0.1202 -0.0004 -0.0129 0.0210 1200 017 A C30 1611 C C31 . 017 F . ? 0.1364 0.1558 0.1144 0.0157 0.0027 0.0206 1200 017 A C31 1612 C C32 . 017 F . ? 0.1009 0.1231 0.1208 0.0103 -0.0058 0.0105 1200 017 A C32 1613 C C33 . 017 F . ? 0.1348 0.1355 0.1333 0.0159 -0.0153 -0.0098 1200 017 A C33 1614 C C34 . 017 F . ? 0.1531 0.1274 0.1438 0.0154 -0.0274 -0.0223 1200 017 A C34 1615 C C35 . 017 F . ? 0.1431 0.1533 0.1408 0.0157 -0.0058 0.0011 1200 017 A C35 1616 C C36 . 017 F . ? 0.1533 0.1506 0.1138 0.0130 -0.0141 0.0045 1200 017 A C36 1617 C C37 . 017 F . ? 0.1570 0.1360 0.0968 0.0029 -0.0078 0.0070 1200 017 A C37 1618 C C38 . 017 F . ? 0.1201 0.1244 0.1096 0.0040 -0.0021 0.0023 1200 017 A C38 1619 P P . PO4 G . ? 0.2912 0.2992 0.2969 -0.0349 -0.0343 0.0492 501 PO4 B P 1620 O O1 . PO4 G . ? 0.3245 0.3580 0.2633 -0.0792 -0.1169 0.0638 501 PO4 B O1 1621 O O2 . PO4 G . ? 0.3311 0.2701 0.4008 -0.0926 0.1056 -0.0313 501 PO4 B O2 1622 O O3 . PO4 G . ? 0.3220 0.4608 0.4010 -0.1522 0.0423 -0.1016 501 PO4 B O3 1623 O O4 . PO4 G . ? 0.2629 0.3651 0.4540 0.0447 0.0625 0.0336 501 PO4 B O4 1624 P P . PO4 H . ? 0.6369 0.4805 0.3597 -0.0929 0.0774 0.0992 503 PO4 B P 1625 O O1 . PO4 H . ? 0.5784 0.4309 0.4799 -0.1573 0.0383 0.1435 503 PO4 B O1 1626 O O2 . PO4 H . ? 0.5744 0.6389 0.6568 -0.0583 0.0094 0.0124 503 PO4 B O2 1627 O O3 . PO4 H . ? 0.5696 0.6200 0.4508 0.0113 0.0220 0.0684 503 PO4 B O3 1628 O O4 . PO4 H . ? 0.7301 0.7162 0.4918 0.0059 0.1055 -0.0122 503 PO4 B O4 1629 O O . HOH I . ? 0.1375 0.1126 0.1189 0.0088 -0.0087 -0.0142 1201 HOH A O 1630 O O . HOH I . ? 0.1590 0.1367 0.1221 0.0061 -0.0042 0.0218 1202 HOH A O 1631 O O . HOH I . ? 0.1577 0.1310 0.1293 0.0166 0.0087 0.0226 1203 HOH A O 1632 O O . HOH I . ? 0.2570 0.2506 0.2139 0.0941 -0.0033 0.0277 1204 HOH A O 1633 O O . HOH I . ? 0.2331 0.2679 0.2841 0.0845 0.0337 0.0046 1205 HOH A O 1634 O O . HOH I . ? 0.1647 0.2270 0.1773 0.0693 0.0514 0.0273 1206 HOH A O 1635 O O . HOH I . ? 0.4176 0.2651 0.1938 0.0803 -0.0645 -0.0498 1207 HOH A O 1636 O O . HOH I . ? 0.2405 0.1867 0.1866 0.0392 0.0391 0.0357 1208 HOH A O 1637 O O . HOH I . ? 0.2149 0.1880 0.3291 0.0076 -0.0131 0.0659 1209 HOH A O 1638 O O . HOH I . ? 0.8978 0.8382 0.7828 -0.0019 -0.0219 -0.0412 1210 HOH A O 1639 O O . HOH I . ? 0.2783 0.3019 0.2854 0.0198 -0.0398 -0.1102 1211 HOH A O 1640 O O . HOH I . ? 0.2278 0.4460 0.2101 -0.0258 -0.0084 -0.0041 1212 HOH A O 1641 O O . HOH I . ? 0.2230 0.1700 0.2979 0.0066 -0.0393 0.0643 1213 HOH A O 1642 O O . HOH I . ? 0.2453 0.2693 0.3839 0.0880 0.0958 0.0164 1214 HOH A O 1643 O O . HOH I . ? 0.3088 0.1953 0.2386 0.0220 -0.0860 -0.0189 1215 HOH A O 1644 O O . HOH I . ? 0.2890 0.2568 0.2288 0.0509 0.0181 0.0193 1216 HOH A O 1645 O O . HOH I . ? 0.3413 0.1901 0.3972 -0.0008 -0.0663 -0.0464 1217 HOH A O 1646 O O . HOH I . ? 0.2412 0.3857 0.3763 0.0478 0.0846 0.0246 1218 HOH A O 1647 O O . HOH I . ? 0.3016 0.2766 0.4702 -0.0976 -0.0109 0.0749 1219 HOH A O 1648 O O . HOH I . ? 0.3138 0.2632 0.4478 0.0219 -0.0146 -0.1635 1220 HOH A O 1649 O O . HOH I . ? 0.3094 0.4525 0.2684 -0.0604 -0.0072 0.0230 1221 HOH A O 1650 O O . HOH I . ? 0.2607 0.4229 0.3673 0.0729 -0.0536 -0.0928 1222 HOH A O 1651 O O . HOH I . ? 0.2577 0.2492 0.3055 0.0821 0.0233 0.0746 1223 HOH A O 1652 O O . HOH I . ? 0.2696 0.2786 0.2803 -0.0658 -0.0771 0.0845 1224 HOH A O 1653 O O . HOH I . ? 0.3973 0.2778 0.3397 -0.0332 -0.0209 -0.1372 1225 HOH A O 1654 O O . HOH I . ? 0.3566 0.2877 0.2965 0.0164 -0.0890 0.0265 1226 HOH A O 1655 O O . HOH I . ? 0.2607 0.2497 0.4423 0.0119 0.0386 0.0193 1227 HOH A O 1656 O O . HOH I . ? 0.2459 0.3479 0.3813 -0.0359 -0.0341 0.1070 1228 HOH A O 1657 O O . HOH I . ? 0.3899 0.3374 0.3277 -0.0680 0.1030 0.0679 1229 HOH A O 1658 O O . HOH I . ? 0.4955 0.3701 0.4266 0.0918 0.0474 0.1212 1230 HOH A O 1659 O O . HOH I . ? 0.5115 0.3454 0.2912 -0.0298 0.0026 -0.0871 1231 HOH A O 1660 O O . HOH I . ? 0.4360 0.6363 0.5210 0.0637 0.0775 -0.0169 1232 HOH A O 1661 O O . HOH I . ? 0.4193 0.5959 0.2155 -0.0574 0.0562 -0.0017 1233 HOH A O 1662 O O . HOH I . ? 0.3757 0.3722 0.3207 0.0577 0.1230 0.0604 1234 HOH A O 1663 O O . HOH I . ? 0.4775 0.3244 0.2618 0.1317 0.0871 0.0530 1235 HOH A O 1664 O O . HOH I . ? 0.5190 0.3691 0.4035 0.1705 -0.0689 -0.1214 1236 HOH A O 1665 O O . HOH I . ? 0.4551 0.3782 0.3070 0.0474 0.1018 0.1060 1237 HOH A O 1666 O O . HOH I . ? 0.4540 0.3366 0.3289 0.0611 -0.1556 -0.0212 1238 HOH A O 1667 O O . HOH I . ? 0.4148 0.4326 0.3266 0.0780 -0.0194 0.0287 1239 HOH A O 1668 O O . HOH I . ? 0.3904 0.3793 0.2430 -0.0204 -0.0494 -0.0843 1240 HOH A O 1669 O O . HOH I . ? 0.3296 0.3301 0.4735 0.1147 -0.0813 -0.0506 1241 HOH A O 1670 O O . HOH I . ? 0.2203 0.2906 0.4235 0.0137 -0.0011 0.1156 1242 HOH A O 1671 O O . HOH I . ? 0.3873 0.4602 0.5017 0.0550 -0.0554 0.1170 1243 HOH A O 1672 O O . HOH I . ? 0.3819 0.4042 0.2482 -0.0623 -0.0114 -0.0284 1244 HOH A O 1673 O O . HOH I . ? 0.3841 0.4245 0.3133 -0.0623 0.0029 -0.0025 1245 HOH A O 1674 O O . HOH I . ? 0.4436 0.5395 0.5844 0.0761 -0.0350 0.0692 1246 HOH A O 1675 O O . HOH I . ? 0.3884 0.4875 0.3141 -0.0850 -0.0530 -0.0233 1247 HOH A O 1676 O O . HOH I . ? 0.3868 0.2978 0.3206 0.0170 -0.0462 0.0539 1248 HOH A O 1677 O O . HOH I . ? 0.4264 0.4481 0.3130 -0.0565 0.0721 0.1030 1249 HOH A O 1678 O O . HOH I . ? 0.4050 0.4163 0.2590 -0.0082 0.0499 0.0831 1250 HOH A O 1679 O O . HOH I . ? 0.5802 0.4431 0.3369 -0.0860 -0.0398 -0.0773 1251 HOH A O 1680 O O . HOH I . ? 0.4595 0.2921 0.3443 -0.0008 -0.1378 0.0585 1252 HOH A O 1681 O O A HOH I . ? 0.4439 0.2318 0.2389 -0.0395 -0.0042 -0.0082 1253 HOH A O 1682 O O B HOH I . ? 0.4555 0.5185 0.3833 0.0105 0.0057 0.1635 1253 HOH A O 1683 O O . HOH I . ? 0.5087 0.3512 0.2942 0.0647 0.1096 0.0863 1254 HOH A O 1684 O O . HOH I . ? 0.3766 0.4299 0.3475 0.0501 -0.0259 0.1274 1255 HOH A O 1685 O O . HOH I . ? 0.3518 0.3012 0.5002 -0.0493 -0.0397 -0.0375 1256 HOH A O 1686 O O . HOH I . ? 0.2598 0.2867 0.4469 0.0272 0.0157 0.0732 1257 HOH A O 1687 O O . HOH I . ? 0.5055 0.3078 0.4080 0.0551 -0.0353 -0.0102 1258 HOH A O 1688 O O . HOH I . ? 0.4455 0.3489 0.3800 -0.1433 0.0926 -0.0445 1259 HOH A O 1689 O O . HOH I . ? 0.2414 0.3839 0.5377 -0.0073 -0.0579 -0.0471 1260 HOH A O 1690 O O . HOH I . ? 0.6500 0.5633 0.3643 0.1384 -0.1889 0.0056 1261 HOH A O 1691 O O . HOH I . ? 0.4609 0.4550 0.3090 -0.0532 -0.0233 -0.0472 1262 HOH A O 1692 O O . HOH I . ? 0.3599 0.3822 0.3215 -0.0361 0.0231 0.0404 1263 HOH A O 1693 O O . HOH I . ? 0.6223 0.1620 0.6962 0.1327 0.1449 -0.0839 1264 HOH A O 1694 O O . HOH I . ? 0.4725 0.5789 0.4589 0.0011 -0.0541 0.0313 1265 HOH A O 1695 O O . HOH I . ? 0.3585 0.3606 0.4368 0.0291 -0.0701 0.0220 1266 HOH A O 1696 O O . HOH I . ? 0.3133 0.4208 0.4017 -0.0763 0.0262 -0.0803 1267 HOH A O 1697 O O . HOH I . ? 0.4032 0.5151 0.2418 -0.1248 0.0386 -0.0212 1268 HOH A O 1698 O O . HOH I . ? 0.3636 0.4827 0.2554 -0.0830 0.0123 -0.0357 1269 HOH A O 1699 O O . HOH I . ? 0.5563 0.4342 0.5818 -0.0293 -0.0013 0.0344 1270 HOH A O 1700 O O . HOH I . ? 0.3812 0.3323 0.3475 0.0449 0.0683 0.0851 1271 HOH A O 1701 O O . HOH I . ? 0.3091 0.4141 0.4886 -0.0068 -0.0167 0.0809 1272 HOH A O 1702 O O . HOH I . ? 0.4392 0.3081 0.3347 -0.0553 -0.0181 0.0022 1273 HOH A O 1703 O O . HOH I . ? 0.5173 0.4798 0.3377 -0.0176 -0.1281 -0.0046 1274 HOH A O 1704 O O . HOH I . ? 0.4413 0.4571 0.3764 0.1187 0.1078 -0.0534 1275 HOH A O 1705 O O . HOH I . ? 0.4910 0.4627 0.3456 0.0246 -0.0139 -0.0699 1276 HOH A O 1706 O O . HOH I . ? 0.5012 0.5053 0.3178 0.0866 -0.0133 -0.0996 1277 HOH A O 1707 O O . HOH I . ? 0.4176 0.3767 0.4910 -0.0262 -0.0986 0.0767 1278 HOH A O 1708 O O . HOH I . ? 0.5898 0.3256 0.5493 -0.1400 0.0032 -0.0288 1279 HOH A O 1709 O O . HOH I . ? 0.4976 0.4258 0.4299 -0.0267 -0.0226 -0.0418 1280 HOH A O 1710 O O . HOH I . ? 0.6433 0.5477 0.4317 -0.0537 -0.0102 -0.0541 1281 HOH A O 1711 O O . HOH I . ? 0.5656 0.3304 0.4692 0.0575 0.1814 0.0198 1282 HOH A O 1712 O O . HOH I . ? 0.3882 0.5394 0.6287 -0.1323 -0.0331 -0.0297 1283 HOH A O 1713 O O . HOH I . ? 0.5701 0.5100 0.3830 0.0048 0.0058 -0.0783 1284 HOH A O 1714 O O . HOH I . ? 0.5344 0.4814 0.6869 0.0621 0.1439 -0.0214 1285 HOH A O 1715 O O . HOH I . ? 0.5419 0.4003 0.4494 0.0403 0.0205 0.0427 1286 HOH A O 1716 O O . HOH I . ? 0.5082 0.3711 0.5452 -0.0051 0.0593 -0.0454 1287 HOH A O 1717 O O . HOH I . ? 0.4630 0.5344 0.5109 0.0603 -0.0792 -0.0231 1288 HOH A O 1718 O O . HOH I . ? 0.5179 0.3745 0.4863 -0.0639 -0.0787 -0.1028 1289 HOH A O 1719 O O . HOH I . ? 0.4505 0.3325 0.4607 -0.0690 -0.0220 0.0211 1290 HOH A O 1720 O O . HOH I . ? 0.3231 0.4835 0.4258 0.0953 -0.0622 -0.1846 1291 HOH A O 1721 O O . HOH I . ? 0.4806 0.4662 0.6000 0.1432 0.0583 -0.0342 1292 HOH A O 1722 O O . HOH I . ? 0.3265 0.4536 0.4454 -0.1210 -0.0364 -0.0120 1293 HOH A O 1723 O O . HOH I . ? 0.4166 0.4527 0.3836 -0.0074 0.0339 -0.0399 1294 HOH A O 1724 O O . HOH I . ? 0.6915 0.3234 0.3708 0.0155 0.0598 -0.0935 1295 HOH A O 1725 O O . HOH I . ? 0.3710 0.4141 0.5242 -0.1698 -0.0710 -0.0297 1296 HOH A O 1726 O O . HOH I . ? 0.4559 0.6389 0.5109 0.0029 0.1494 0.0287 1297 HOH A O 1727 O O . HOH I . ? 0.3158 0.5693 0.3501 -0.0660 0.0422 0.0044 1298 HOH A O 1728 O O . HOH I . ? 0.3929 0.4092 0.5388 -0.0193 -0.0312 -0.0231 1299 HOH A O 1729 O O . HOH I . ? 0.4840 0.7383 0.2914 0.0172 -0.0836 -0.1032 1300 HOH A O 1730 O O . HOH I . ? 0.4339 0.5985 0.5702 -0.0446 0.0183 -0.0202 1301 HOH A O 1731 O O . HOH I . ? 0.4346 0.4878 0.5646 -0.0328 -0.1089 -0.0314 1302 HOH A O 1732 O O . HOH I . ? 0.4660 0.4994 0.5776 0.0092 0.0845 0.0439 1303 HOH A O 1733 O O . HOH I . ? 0.3860 0.6268 0.6144 -0.0947 0.0272 0.1001 1304 HOH A O 1734 O O . HOH I . ? 0.5988 0.5651 0.5541 0.0361 -0.1157 0.0843 1305 HOH A O 1735 O O . HOH I . ? 0.5358 0.4744 0.6127 -0.0779 0.0129 0.0776 1306 HOH A O 1736 O O . HOH I . ? 0.6399 0.4186 0.5893 0.0043 -0.0186 0.0966 1307 HOH A O 1737 O O . HOH I . ? 0.2102 0.2177 0.1568 0.0221 -0.0038 -0.0356 1308 HOH A O 1738 O O . HOH I . ? 0.5852 0.5104 0.5293 -0.0202 -0.0570 -0.0899 1309 HOH A O 1739 O O . HOH I . ? 0.4519 0.3025 0.4713 0.0524 0.0724 0.0234 1310 HOH A O 1740 O O . HOH I . ? 0.4348 0.3054 0.4611 0.1299 -0.0825 -0.0942 1311 HOH A O 1741 O O . HOH I . ? 0.7779 0.3030 0.3590 0.0290 0.1264 -0.1233 1312 HOH A O 1742 O O . HOH I . ? 0.2991 0.5138 0.4951 0.0841 0.0647 0.0048 1313 HOH A O 1743 O O . HOH I . ? 0.3499 0.3775 0.3658 -0.0064 -0.0509 -0.0462 1314 HOH A O 1744 O O . HOH I . ? 0.2973 0.2949 0.2588 -0.0618 0.0754 -0.0250 1315 HOH A O 1745 O O . HOH I . ? 0.2534 0.1887 0.2252 -0.0123 0.0138 0.0444 1316 HOH A O 1746 O O . HOH I . ? 0.1421 0.2326 0.2925 0.0370 0.0669 0.0021 1317 HOH A O 1747 O O . HOH I . ? 0.4618 0.5214 0.5014 0.0056 0.0834 -0.2297 1318 HOH A O 1748 O O . HOH I . ? 0.6330 0.4799 0.5881 0.0991 0.0168 0.0001 1319 HOH A O 1749 O O . HOH I . ? 0.6058 0.4796 0.7072 -0.0137 0.0402 0.0299 1320 HOH A O 1750 O O . HOH I . ? 0.5887 0.4626 0.4385 -0.0641 0.0002 -0.0359 1321 HOH A O 1751 O O . HOH I . ? 0.5188 0.6224 0.6802 0.0184 0.0206 0.0047 1322 HOH A O 1752 O O . HOH I . ? 0.5334 0.4929 0.5008 -0.0208 -0.0189 -0.0143 1323 HOH A O 1753 O O . HOH I . ? 0.4855 0.4269 0.4785 0.0755 0.0725 -0.0450 1324 HOH A O 1754 O O . HOH I . ? 0.4394 0.4484 0.6076 -0.0332 -0.0674 -0.0747 1325 HOH A O 1755 O O . HOH I . ? 0.6176 0.5901 0.4347 -0.0410 -0.0577 0.0137 1326 HOH A O 1756 O O . HOH I . ? 0.5614 0.5239 0.3603 0.1297 -0.1587 0.0499 1327 HOH A O 1757 O O . HOH I . ? 0.5210 0.5791 0.5515 0.0064 -0.0389 -0.0456 1328 HOH A O 1758 O O . HOH I . ? 0.7009 0.5814 0.5442 0.0286 -0.0127 -0.0286 1329 HOH A O 1759 O O . HOH I . ? 0.6553 0.3087 0.6431 -0.0318 0.0118 0.0469 1330 HOH A O 1760 O O . HOH I . ? 0.4384 0.5898 0.5194 0.0013 0.0884 0.0845 1331 HOH A O 1761 O O . HOH I . ? 0.6412 0.5111 0.5266 0.0132 0.0034 0.0053 1332 HOH A O 1762 O O . HOH I . ? 0.6025 0.4330 0.6482 0.0120 0.0216 0.0456 1333 HOH A O 1763 O O . HOH J . ? 0.2205 0.1382 0.1654 0.0097 0.0215 -0.0199 504 HOH B O 1764 O O . HOH J . ? 0.2051 0.2003 0.1863 0.0064 0.0012 0.0272 505 HOH B O 1765 O O . HOH J . ? 0.2894 0.3631 0.2226 0.1097 0.0912 0.1031 506 HOH B O 1766 O O . HOH J . ? 0.2115 0.2300 0.2813 -0.0105 -0.0241 0.0506 507 HOH B O 1767 O O . HOH J . ? 0.1916 0.3439 0.5200 0.0564 0.0599 0.2096 508 HOH B O 1768 O O . HOH J . ? 0.3078 0.2854 0.1537 -0.0987 -0.0147 0.0459 509 HOH B O 1769 O O . HOH J . ? 0.2428 0.2169 0.1805 0.0427 -0.0501 -0.0352 510 HOH B O 1770 O O . HOH J . ? 0.3430 0.3033 0.1772 0.0680 0.0652 0.0353 511 HOH B O 1771 O O . HOH J . ? 0.2786 0.3613 0.2012 0.1029 0.0152 0.0557 512 HOH B O 1772 O O . HOH J . ? 0.2248 0.2271 0.1707 0.0005 0.0221 0.0335 513 HOH B O 1773 O O . HOH J . ? 0.2318 0.2532 0.2119 0.0269 -0.0233 -0.0159 514 HOH B O 1774 O O . HOH J . ? 0.2665 0.2895 0.2598 0.0502 0.0469 0.0248 515 HOH B O 1775 O O . HOH J . ? 0.3612 0.3458 0.2418 0.0103 -0.0086 -0.0857 516 HOH B O 1776 O O . HOH J . ? 0.3376 0.3312 0.1445 0.1316 0.0425 -0.0074 517 HOH B O 1777 O O . HOH J . ? 0.2202 0.2301 0.1937 0.0090 0.0056 0.0491 518 HOH B O 1778 O O . HOH J . ? 0.5159 0.6251 0.5049 0.0022 -0.0653 0.0190 519 HOH B O 1779 O O . HOH J . ? 0.2829 0.4366 0.2084 0.0938 0.0500 0.0862 520 HOH B O 1780 O O . HOH J . ? 0.3315 0.2355 0.3668 0.0250 -0.0082 -0.0848 521 HOH B O 1781 O O . HOH J . ? 0.3494 0.2715 0.2275 0.0011 0.0071 0.0305 522 HOH B O 1782 O O . HOH J . ? 0.2677 0.2242 0.3403 -0.0020 -0.0329 -0.0577 523 HOH B O 1783 O O . HOH J . ? 0.3201 0.2669 0.3290 0.0595 -0.0069 0.0130 524 HOH B O 1784 O O . HOH J . ? 0.2446 0.2824 0.4154 -0.0142 0.1464 -0.0501 525 HOH B O 1785 O O . HOH J . ? 0.3729 0.3369 0.3130 0.0236 0.0759 -0.0237 526 HOH B O 1786 O O . HOH J . ? 0.4441 0.3240 0.3325 -0.0018 -0.0254 0.0512 527 HOH B O 1787 O O . HOH J . ? 0.3695 0.3941 0.2500 0.0324 0.0408 0.0750 528 HOH B O 1788 O O . HOH J . ? 0.3007 0.3901 0.3331 0.0625 -0.0472 -0.0085 529 HOH B O 1789 O O . HOH J . ? 0.1852 0.2040 0.5167 0.0187 0.0181 0.0722 530 HOH B O 1790 O O . HOH J . ? 0.4650 0.2462 0.1956 0.0093 -0.0561 -0.0664 531 HOH B O 1791 O O . HOH J . ? 0.2793 0.3698 0.3698 0.0358 -0.1144 -0.0432 532 HOH B O 1792 O O . HOH J . ? 0.2601 0.2708 0.2624 0.0330 -0.0607 -0.0448 533 HOH B O 1793 O O . HOH J . ? 0.3790 0.3875 0.4721 0.0520 0.1145 0.0750 534 HOH B O 1794 O O . HOH J . ? 0.3332 0.4437 0.3822 -0.0207 -0.1155 0.1504 535 HOH B O 1795 O O . HOH J . ? 0.3274 0.2593 0.2645 -0.0383 -0.0540 -0.0872 536 HOH B O 1796 O O . HOH J . ? 0.5575 0.4020 0.5317 0.0947 0.0386 -0.0560 537 HOH B O 1797 O O . HOH J . ? 0.3560 0.5872 0.3902 -0.0051 0.1652 -0.0357 538 HOH B O 1798 O O . HOH J . ? 0.2521 0.3119 0.4635 0.0768 -0.0770 0.0658 539 HOH B O 1799 O O . HOH J . ? 0.3340 0.4511 0.3693 0.2147 0.0086 -0.0457 540 HOH B O 1800 O O . HOH J . ? 0.3201 0.2788 0.7300 0.0640 0.0071 0.0611 541 HOH B O 1801 O O . HOH J . ? 0.2431 0.4163 0.5613 0.0560 -0.0039 0.0981 542 HOH B O 1802 O O . HOH J . ? 0.3544 0.2230 0.1735 -0.0011 -0.0033 0.0221 543 HOH B O 1803 O O . HOH J . ? 0.3264 0.2747 0.3688 0.0248 0.1075 -0.0453 544 HOH B O 1804 O O . HOH J . ? 0.3052 0.3176 0.3393 0.0273 -0.1185 -0.0305 545 HOH B O 1805 O O . HOH J . ? 0.2969 0.2812 0.5462 -0.0175 -0.0181 0.0604 546 HOH B O 1806 O O . HOH J . ? 0.4239 0.3734 0.6186 -0.1381 -0.0948 0.0405 547 HOH B O 1807 O O . HOH J . ? 0.5833 0.3704 0.5495 0.0606 -0.0618 0.0568 548 HOH B O 1808 O O . HOH J . ? 0.4718 0.3652 0.3898 0.1594 0.0196 -0.0323 549 HOH B O 1809 O O . HOH J . ? 0.3264 0.4994 0.1849 0.0710 -0.0779 -0.1094 550 HOH B O 1810 O O . HOH J . ? 0.4445 0.5690 0.3939 -0.1327 -0.0441 0.1761 551 HOH B O 1811 O O . HOH J . ? 0.4155 0.3559 0.2734 0.0849 0.0313 0.0478 552 HOH B O 1812 O O . HOH J . ? 0.3931 0.3865 0.4103 0.0328 0.0069 0.0411 553 HOH B O 1813 O O . HOH J . ? 0.5231 0.4091 0.2954 -0.0252 -0.1555 0.0539 554 HOH B O 1814 O O . HOH J . ? 0.4263 0.3511 0.4988 -0.0185 0.1265 0.1023 555 HOH B O 1815 O O . HOH J . ? 0.3617 0.3137 0.3892 0.0075 -0.0251 0.0319 556 HOH B O 1816 O O . HOH J . ? 0.3716 0.3692 0.5303 -0.1114 -0.0225 -0.0235 557 HOH B O 1817 O O . HOH J . ? 0.4479 0.3861 0.2609 0.0283 -0.0166 0.0714 558 HOH B O 1818 O O . HOH J . ? 0.5838 0.3285 0.3618 0.0982 0.0377 0.0506 559 HOH B O 1819 O O . HOH J . ? 0.5335 0.5825 0.3429 0.0141 0.0558 -0.0413 560 HOH B O 1820 O O . HOH J . ? 0.3495 0.4219 0.3619 -0.0530 0.0019 -0.0062 561 HOH B O 1821 O O . HOH J . ? 0.4482 0.5504 0.3660 -0.0247 0.0012 -0.0910 562 HOH B O 1822 O O . HOH J . ? 0.2088 0.5250 0.4004 -0.0527 -0.0306 -0.1032 563 HOH B O 1823 O O . HOH J . ? 0.4652 0.6199 0.6730 0.0906 -0.1493 0.0745 564 HOH B O 1824 O O . HOH J . ? 0.3873 0.3629 0.4495 0.0098 -0.0553 0.0844 565 HOH B O 1825 O O . HOH J . ? 0.5342 0.6448 0.4259 0.0229 -0.1367 0.0918 566 HOH B O 1826 O O . HOH J . ? 0.3379 0.4224 0.3624 0.0241 -0.0514 0.0628 567 HOH B O 1827 O O . HOH J . ? 0.5895 0.4269 0.4841 0.0847 0.0801 -0.0306 568 HOH B O 1828 O O . HOH J . ? 0.3726 0.4371 0.5186 -0.0176 0.0121 -0.0637 569 HOH B O 1829 O O . HOH J . ? 0.5473 0.3842 0.6135 -0.0487 -0.0096 -0.0106 570 HOH B O 1830 O O . HOH J . ? 0.2791 0.3447 0.5985 -0.0673 -0.1320 -0.0617 571 HOH B O 1831 O O . HOH J . ? 0.3579 0.2524 0.4556 0.0361 -0.0001 0.0195 572 HOH B O 1832 O O . HOH J . ? 0.4152 0.3893 0.5806 0.1305 0.0727 -0.0424 573 HOH B O 1833 O O . HOH J . ? 0.3175 0.5961 0.4797 -0.0488 -0.0463 0.0319 574 HOH B O 1834 O O . HOH J . ? 0.4712 0.5064 0.5694 0.0558 0.1119 -0.0242 575 HOH B O 1835 O O . HOH J . ? 0.3418 0.4355 0.3748 -0.1190 0.0055 0.0017 576 HOH B O 1836 O O . HOH J . ? 0.3224 0.4353 0.4157 -0.0053 -0.1529 -0.0177 577 HOH B O 1837 O O . HOH J . ? 0.5823 0.6338 0.4504 -0.0962 0.0069 -0.0417 578 HOH B O 1838 O O . HOH J . ? 0.5086 0.4717 0.4641 0.0113 0.0565 -0.0575 579 HOH B O 1839 O O . HOH J . ? 0.4634 0.3081 0.3176 0.0589 0.0400 0.0041 580 HOH B O 1840 O O . HOH J . ? 0.4561 0.3572 0.3696 -0.0442 -0.0499 0.0662 581 HOH B O 1841 O O . HOH J . ? 0.4819 0.4098 0.4782 0.0729 0.0061 0.1129 582 HOH B O 1842 O O A HOH J . ? 0.4940 0.4199 0.4242 0.0018 -0.0796 -0.0158 583 HOH B O 1843 O O B HOH J . ? 0.3203 0.3375 0.3848 -0.0591 -0.0426 0.0159 583 HOH B O 1844 O O . HOH J . ? 0.5406 0.3736 0.4303 0.0819 0.0206 -0.0760 584 HOH B O 1845 O O . HOH J . ? 0.3431 0.4043 0.4373 -0.0396 0.0557 -0.1371 585 HOH B O 1846 O O . HOH J . ? 0.3978 0.5681 0.2716 0.0910 0.0929 -0.0157 586 HOH B O 1847 O O . HOH J . ? 0.5254 0.5308 0.4361 0.0470 -0.0842 0.1218 587 HOH B O 1848 O O . HOH J . ? 0.5152 0.5584 0.3198 0.0409 -0.0939 0.0839 588 HOH B O 1849 O O . HOH J . ? 0.5691 0.4368 0.4779 0.0041 0.0929 -0.0252 589 HOH B O 1850 O O . HOH J . ? 0.3039 0.3737 0.5148 -0.0010 -0.0711 0.0804 590 HOH B O 1851 O O . HOH J . ? 0.6016 0.4724 0.3320 -0.0310 -0.0459 0.0878 591 HOH B O 1852 O O . HOH J . ? 0.6875 0.6280 0.7043 -0.0252 0.0247 0.0360 592 HOH B O 1853 O O . HOH J . ? 0.4524 0.6591 0.4545 0.0497 -0.0979 0.0578 593 HOH B O 1854 O O . HOH J . ? 0.4855 0.6205 0.4347 -0.0470 -0.0606 -0.0770 594 HOH B O 1855 O O . HOH J . ? 0.6257 0.4317 0.5364 0.0437 0.0169 0.0368 595 HOH B O 1856 O O . HOH J . ? 0.4161 0.5365 0.5097 0.0466 0.0108 -0.0423 596 HOH B O 1857 O O . HOH J . ? 0.5466 0.4601 0.6184 0.1003 -0.0900 -0.0522 597 HOH B O 1858 O O . HOH J . ? 0.5349 0.5190 0.3574 -0.0264 -0.0521 -0.0222 598 HOH B O 1859 O O . HOH J . ? 0.4655 0.5122 0.3913 0.0152 0.0385 -0.0237 599 HOH B O 1860 O O . HOH J . ? 0.7104 0.5648 0.2814 0.0267 -0.0711 -0.1293 600 HOH B O 1861 O O . HOH J . ? 0.6358 0.4024 0.6395 0.0721 -0.0239 0.0188 601 HOH B O 1862 O O . HOH J . ? 0.4601 0.4959 0.3593 -0.0586 0.0083 -0.0961 602 HOH B O 1863 O O . HOH J . ? 0.4330 0.4668 0.3760 0.0933 -0.0390 -0.0212 603 HOH B O 1864 O O . HOH J . ? 0.5920 0.3923 0.3828 0.0388 0.1780 -0.0142 604 HOH B O 1865 O O . HOH J . ? 0.4305 0.3876 0.2410 -0.0431 -0.0914 -0.0667 605 HOH B O 1866 O O . HOH J . ? 0.5280 0.4683 0.5324 -0.1207 -0.0021 0.0432 606 HOH B O 1867 O O . HOH J . ? 0.5501 0.4960 0.6309 -0.0021 -0.0653 -0.0411 607 HOH B O 1868 O O . HOH J . ? 0.2437 0.3120 0.1716 0.0691 0.0430 0.0018 608 HOH B O 1869 O O . HOH J . ? 0.3406 0.4263 0.3130 0.0440 0.1140 -0.0332 609 HOH B O 1870 O O . HOH J . ? 0.5336 0.2397 0.4342 0.0048 0.0133 -0.0196 610 HOH B O 1871 O O . HOH J . ? 0.5970 0.6075 0.5836 -0.0223 -0.0577 -0.0450 611 HOH B O 1872 O O . HOH J . ? 0.5254 0.5646 0.6099 0.0046 -0.0010 0.0212 612 HOH B O 1873 O O . HOH J . ? 0.4338 0.5731 0.5853 0.1452 0.1344 -0.0168 613 HOH B O 1874 O O . HOH J . ? 0.5643 0.2113 0.2492 -0.0930 -0.1142 0.0670 614 HOH B O 1875 O O . HOH J . ? 0.6118 0.3938 0.5862 -0.0108 0.0066 -0.0107 615 HOH B O 1876 O O . HOH J . ? 0.5156 0.4108 0.5439 -0.0178 0.0170 -0.0396 616 HOH B O 1877 O O . HOH J . ? 0.4794 0.5790 0.4463 -0.0407 0.0411 -0.0806 617 HOH B O 1878 O O . HOH J . ? 0.2940 0.3436 0.3497 -0.0304 0.0050 0.0185 618 HOH B O 1879 O O . HOH J . ? 0.4783 0.4676 0.4851 0.0501 -0.0278 -0.1021 619 HOH B O 1880 O O . HOH J . ? 0.5001 0.3369 0.6587 0.0112 -0.0093 -0.0651 620 HOH B O 1881 O O . HOH J . ? 0.5501 0.3915 0.5638 -0.0572 0.0611 -0.0111 621 HOH B O 1882 O O . HOH J . ? 0.6190 0.3995 0.5881 0.0265 -0.0402 -0.1043 622 HOH B O 1883 O O . HOH J . ? 0.6081 0.4712 0.6714 0.0009 -0.0226 -0.0328 623 HOH B O 1884 O O . HOH J . ? 0.5358 0.4321 0.4015 0.0007 -0.1187 0.1434 624 HOH B O 1885 O O . HOH J . ? 0.5706 0.5875 0.5034 0.0129 -0.0232 0.0564 625 HOH B O 1886 O O . HOH J . ? 0.6715 0.6529 0.5638 -0.0328 0.0256 -0.0269 626 HOH B O 1887 O O . HOH J . ? 0.4743 0.5073 0.4409 -0.1260 0.0344 0.1079 627 HOH B O 1888 O O . HOH J . ? 0.8112 0.3503 0.3921 0.1512 -0.0323 -0.1429 628 HOH B O 1889 O O . HOH J . ? 0.3750 0.2732 0.4036 -0.0102 0.1098 0.0502 629 HOH B O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PRO 1 1 1 PRO PRO A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 LEU 5 5 5 LEU LEU A . n A 1 6 TRP 6 6 6 TRP TRP A . n A 1 7 LYS 7 7 7 LYS LYS A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 LEU 10 10 10 LEU LEU A . n A 1 11 VAL 11 11 11 VAL VAL A . n A 1 12 THR 12 12 12 THR THR A . n A 1 13 ILE 13 13 13 ILE ILE A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 ILE 15 15 15 ILE ILE A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 GLY 17 17 17 GLY GLY A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LYS 20 20 20 LYS LYS A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 LEU 23 23 23 LEU LEU A . n A 1 24 LEU 24 24 24 LEU LEU A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 GLY 27 27 27 GLY GLY A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 ASP 30 30 30 ASP ASP A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 ASN 37 37 37 ASN ASN A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 GLY 40 40 40 GLY GLY A . n A 1 41 LYS 41 41 41 LYS LYS A . n A 1 42 TRP 42 42 42 TRP TRP A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 PRO 44 44 44 PRO PRO A . n A 1 45 LYS 45 45 45 LYS LYS A . n A 1 46 MET 46 46 46 MET MET A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 GLY 48 48 48 GLY GLY A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 GLY 51 51 51 GLY GLY A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 PHE 53 53 53 PHE PHE A . n A 1 54 ILE 54 54 54 ILE ILE A . n A 1 55 LYS 55 55 55 LYS LYS A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 ARG 57 57 57 ARG ARG A . n A 1 58 GLN 58 58 58 GLN GLN A . n A 1 59 TYR 59 59 59 TYR TYR A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 GLN 61 61 61 GLN GLN A . n A 1 62 ILE 62 62 62 ILE ILE A . n A 1 63 PRO 63 63 63 PRO PRO A . n A 1 64 VAL 64 64 64 VAL VAL A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 GLY 68 68 68 GLY GLY A . n A 1 69 HIS 69 69 69 HIS HIS A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 ALA 71 71 71 ALA ALA A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 LEU 76 76 76 LEU LEU A . n A 1 77 VAL 77 77 77 VAL VAL A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 PRO 79 79 79 PRO PRO A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 VAL 82 82 82 VAL VAL A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 ILE 84 84 84 ILE ILE A . n A 1 85 ILE 85 85 85 ILE ILE A . n A 1 86 GLY 86 86 86 GLY GLY A . n A 1 87 ARG 87 87 87 ARG ARG A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 THR 91 91 91 THR THR A . n A 1 92 GLN 92 92 92 GLN GLN A . n A 1 93 ILE 93 93 93 ILE ILE A . n A 1 94 GLY 94 94 94 GLY GLY A . n A 1 95 CYS 95 95 95 CYS CYS A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 PHE 99 99 99 PHE PHE A . n B 1 1 PRO 1 1 1 PRO PRO B . n B 1 2 GLN 2 2 2 GLN GLN B . n B 1 3 ILE 3 3 3 ILE ILE B . n B 1 4 THR 4 4 4 THR THR B . n B 1 5 LEU 5 5 5 LEU LEU B . n B 1 6 TRP 6 6 6 TRP TRP B . n B 1 7 LYS 7 7 7 LYS LYS B . n B 1 8 ARG 8 8 8 ARG ARG B . n B 1 9 PRO 9 9 9 PRO PRO B . n B 1 10 LEU 10 10 10 LEU LEU B . n B 1 11 VAL 11 11 11 VAL VAL B . n B 1 12 THR 12 12 12 THR THR B . n B 1 13 ILE 13 13 13 ILE ILE B . n B 1 14 ARG 14 14 14 ARG ARG B . n B 1 15 ILE 15 15 15 ILE ILE B . n B 1 16 GLY 16 16 16 GLY GLY B . n B 1 17 GLY 17 17 17 GLY GLY B . n B 1 18 GLN 18 18 18 GLN GLN B . n B 1 19 LEU 19 19 19 LEU LEU B . n B 1 20 LYS 20 20 20 LYS LYS B . n B 1 21 GLU 21 21 21 GLU GLU B . n B 1 22 ALA 22 22 22 ALA ALA B . n B 1 23 LEU 23 23 23 LEU LEU B . n B 1 24 LEU 24 24 24 LEU LEU B . n B 1 25 ASP 25 25 25 ASP ASP B . n B 1 26 THR 26 26 26 THR THR B . n B 1 27 GLY 27 27 27 GLY GLY B . n B 1 28 ALA 28 28 28 ALA ALA B . n B 1 29 ASP 29 29 29 ASP ASP B . n B 1 30 ASP 30 30 30 ASP ASP B . n B 1 31 THR 31 31 31 THR THR B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 LEU 33 33 33 LEU LEU B . n B 1 34 GLU 34 34 34 GLU GLU B . n B 1 35 GLU 35 35 35 GLU GLU B . n B 1 36 MET 36 36 36 MET MET B . n B 1 37 ASN 37 37 37 ASN ASN B . n B 1 38 LEU 38 38 38 LEU LEU B . n B 1 39 PRO 39 39 39 PRO PRO B . n B 1 40 GLY 40 40 40 GLY GLY B . n B 1 41 LYS 41 41 41 LYS LYS B . n B 1 42 TRP 42 42 42 TRP TRP B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 PRO 44 44 44 PRO PRO B . n B 1 45 LYS 45 45 45 LYS LYS B . n B 1 46 MET 46 46 46 MET MET B . n B 1 47 ILE 47 47 47 ILE ILE B . n B 1 48 GLY 48 48 48 GLY GLY B . n B 1 49 GLY 49 49 49 GLY GLY B . n B 1 50 ILE 50 50 50 ILE ILE B . n B 1 51 GLY 51 51 51 GLY GLY B . n B 1 52 GLY 52 52 52 GLY GLY B . n B 1 53 PHE 53 53 53 PHE PHE B . n B 1 54 ILE 54 54 54 ILE ILE B . n B 1 55 LYS 55 55 55 LYS LYS B . n B 1 56 VAL 56 56 56 VAL VAL B . n B 1 57 ARG 57 57 57 ARG ARG B . n B 1 58 GLN 58 58 58 GLN GLN B . n B 1 59 TYR 59 59 59 TYR TYR B . n B 1 60 ASP 60 60 60 ASP ASP B . n B 1 61 GLN 61 61 61 GLN GLN B . n B 1 62 ILE 62 62 62 ILE ILE B . n B 1 63 PRO 63 63 63 PRO PRO B . n B 1 64 VAL 64 64 64 VAL VAL B . n B 1 65 GLU 65 65 65 GLU GLU B . n B 1 66 ILE 66 66 66 ILE ILE B . n B 1 67 CYS 67 67 67 CYS CYS B . n B 1 68 GLY 68 68 68 GLY GLY B . n B 1 69 HIS 69 69 69 HIS HIS B . n B 1 70 LYS 70 70 70 LYS LYS B . n B 1 71 ALA 71 71 71 ALA ALA B . n B 1 72 ILE 72 72 72 ILE ILE B . n B 1 73 GLY 73 73 73 GLY GLY B . n B 1 74 THR 74 74 74 THR THR B . n B 1 75 VAL 75 75 75 VAL VAL B . n B 1 76 LEU 76 76 76 LEU LEU B . n B 1 77 VAL 77 77 77 VAL VAL B . n B 1 78 GLY 78 78 78 GLY GLY B . n B 1 79 PRO 79 79 79 PRO PRO B . n B 1 80 THR 80 80 80 THR THR B . n B 1 81 PRO 81 81 81 PRO PRO B . n B 1 82 VAL 82 82 82 VAL VAL B . n B 1 83 ASN 83 83 83 ASN ASN B . n B 1 84 ILE 84 84 84 ILE ILE B . n B 1 85 ILE 85 85 85 ILE ILE B . n B 1 86 GLY 86 86 86 GLY GLY B . n B 1 87 ARG 87 87 87 ARG ARG B . n B 1 88 ASN 88 88 88 ASN ASN B . n B 1 89 LEU 89 89 89 LEU LEU B . n B 1 90 LEU 90 90 90 LEU LEU B . n B 1 91 THR 91 91 91 THR THR B . n B 1 92 GLN 92 92 92 GLN GLN B . n B 1 93 ILE 93 93 93 ILE ILE B . n B 1 94 GLY 94 94 94 GLY GLY B . n B 1 95 CYS 95 95 95 CYS CYS B . n B 1 96 THR 96 96 96 THR THR B . n B 1 97 LEU 97 97 97 LEU LEU B . n B 1 98 ASN 98 98 98 ASN ASN B . n B 1 99 PHE 99 99 99 PHE PHE 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 PO4 1 502 502 PO4 PO4 A . D 2 PO4 1 504 504 PO4 PO4 A . E 2 PO4 1 505 505 PO4 PO4 A . F 3 017 1 1200 1200 017 017 A . G 2 PO4 1 501 501 PO4 PO4 B . H 2 PO4 1 503 503 PO4 PO4 B . I 4 HOH 1 1201 1 HOH HOH A . I 4 HOH 2 1202 2 HOH HOH A . I 4 HOH 3 1203 4 HOH HOH A . I 4 HOH 4 1204 6 HOH HOH A . I 4 HOH 5 1205 7 HOH HOH A . I 4 HOH 6 1206 8 HOH HOH A . I 4 HOH 7 1207 11 HOH HOH A . I 4 HOH 8 1208 14 HOH HOH A . I 4 HOH 9 1209 16 HOH HOH A . I 4 HOH 10 1210 20 HOH HOH A . I 4 HOH 11 1211 21 HOH HOH A . I 4 HOH 12 1212 22 HOH HOH A . I 4 HOH 13 1213 24 HOH HOH A . I 4 HOH 14 1214 25 HOH HOH A . I 4 HOH 15 1215 27 HOH HOH A . I 4 HOH 16 1216 30 HOH HOH A . I 4 HOH 17 1217 31 HOH HOH A . I 4 HOH 18 1218 36 HOH HOH A . I 4 HOH 19 1219 44 HOH HOH A . I 4 HOH 20 1220 46 HOH HOH A . I 4 HOH 21 1221 47 HOH HOH A . I 4 HOH 22 1222 48 HOH HOH A . I 4 HOH 23 1223 50 HOH HOH A . I 4 HOH 24 1224 54 HOH HOH A . I 4 HOH 25 1225 59 HOH HOH A . I 4 HOH 26 1226 65 HOH HOH A . I 4 HOH 27 1227 67 HOH HOH A . I 4 HOH 28 1228 73 HOH HOH A . I 4 HOH 29 1229 74 HOH HOH A . I 4 HOH 30 1230 76 HOH HOH A . I 4 HOH 31 1231 77 HOH HOH A . I 4 HOH 32 1232 78 HOH HOH A . I 4 HOH 33 1233 79 HOH HOH A . I 4 HOH 34 1234 81 HOH HOH A . I 4 HOH 35 1235 82 HOH HOH A . I 4 HOH 36 1236 83 HOH HOH A . I 4 HOH 37 1237 84 HOH HOH A . I 4 HOH 38 1238 85 HOH HOH A . I 4 HOH 39 1239 86 HOH HOH A . I 4 HOH 40 1240 88 HOH HOH A . I 4 HOH 41 1241 90 HOH HOH A . I 4 HOH 42 1242 92 HOH HOH A . I 4 HOH 43 1243 93 HOH HOH A . I 4 HOH 44 1244 94 HOH HOH A . I 4 HOH 45 1245 97 HOH HOH A . I 4 HOH 46 1246 98 HOH HOH A . I 4 HOH 47 1247 99 HOH HOH A . I 4 HOH 48 1248 100 HOH HOH A . I 4 HOH 49 1249 101 HOH HOH A . I 4 HOH 50 1250 102 HOH HOH A . I 4 HOH 51 1251 103 HOH HOH A . I 4 HOH 52 1252 105 HOH HOH A . I 4 HOH 53 1253 106 HOH HOH A . I 4 HOH 54 1254 111 HOH HOH A . I 4 HOH 55 1255 114 HOH HOH A . I 4 HOH 56 1256 116 HOH HOH A . I 4 HOH 57 1257 118 HOH HOH A . I 4 HOH 58 1258 123 HOH HOH A . I 4 HOH 59 1259 125 HOH HOH A . I 4 HOH 60 1260 127 HOH HOH A . I 4 HOH 61 1261 128 HOH HOH A . I 4 HOH 62 1262 129 HOH HOH A . I 4 HOH 63 1263 130 HOH HOH A . I 4 HOH 64 1264 133 HOH HOH A . I 4 HOH 65 1265 135 HOH HOH A . I 4 HOH 66 1266 138 HOH HOH A . I 4 HOH 67 1267 139 HOH HOH A . I 4 HOH 68 1268 141 HOH HOH A . I 4 HOH 69 1269 144 HOH HOH A . I 4 HOH 70 1270 145 HOH HOH A . I 4 HOH 71 1271 149 HOH HOH A . I 4 HOH 72 1272 152 HOH HOH A . I 4 HOH 73 1273 153 HOH HOH A . I 4 HOH 74 1274 154 HOH HOH A . I 4 HOH 75 1275 155 HOH HOH A . I 4 HOH 76 1276 157 HOH HOH A . I 4 HOH 77 1277 159 HOH HOH A . I 4 HOH 78 1278 164 HOH HOH A . I 4 HOH 79 1279 167 HOH HOH A . I 4 HOH 80 1280 169 HOH HOH A . I 4 HOH 81 1281 170 HOH HOH A . I 4 HOH 82 1282 173 HOH HOH A . I 4 HOH 83 1283 176 HOH HOH A . I 4 HOH 84 1284 177 HOH HOH A . I 4 HOH 85 1285 179 HOH HOH A . I 4 HOH 86 1286 180 HOH HOH A . I 4 HOH 87 1287 182 HOH HOH A . I 4 HOH 88 1288 183 HOH HOH A . I 4 HOH 89 1289 184 HOH HOH A . I 4 HOH 90 1290 185 HOH HOH A . I 4 HOH 91 1291 187 HOH HOH A . I 4 HOH 92 1292 188 HOH HOH A . I 4 HOH 93 1293 195 HOH HOH A . I 4 HOH 94 1294 197 HOH HOH A . I 4 HOH 95 1295 199 HOH HOH A . I 4 HOH 96 1296 202 HOH HOH A . I 4 HOH 97 1297 208 HOH HOH A . I 4 HOH 98 1298 209 HOH HOH A . I 4 HOH 99 1299 211 HOH HOH A . I 4 HOH 100 1300 215 HOH HOH A . I 4 HOH 101 1301 216 HOH HOH A . I 4 HOH 102 1302 217 HOH HOH A . I 4 HOH 103 1303 218 HOH HOH A . I 4 HOH 104 1304 219 HOH HOH A . I 4 HOH 105 1305 222 HOH HOH A . I 4 HOH 106 1306 223 HOH HOH A . I 4 HOH 107 1307 224 HOH HOH A . I 4 HOH 108 1308 228 HOH HOH A . I 4 HOH 109 1309 231 HOH HOH A . I 4 HOH 110 1310 233 HOH HOH A . I 4 HOH 111 1311 234 HOH HOH A . I 4 HOH 112 1312 238 HOH HOH A . I 4 HOH 113 1313 248 HOH HOH A . I 4 HOH 114 1314 251 HOH HOH A . I 4 HOH 115 1315 253 HOH HOH A . I 4 HOH 116 1316 254 HOH HOH A . I 4 HOH 117 1317 258 HOH HOH A . I 4 HOH 118 1318 259 HOH HOH A . I 4 HOH 119 1319 260 HOH HOH A . I 4 HOH 120 1320 263 HOH HOH A . I 4 HOH 121 1321 264 HOH HOH A . I 4 HOH 122 1322 268 HOH HOH A . I 4 HOH 123 1323 269 HOH HOH A . I 4 HOH 124 1324 270 HOH HOH A . I 4 HOH 125 1325 285 HOH HOH A . I 4 HOH 126 1326 288 HOH HOH A . I 4 HOH 127 1327 289 HOH HOH A . I 4 HOH 128 1328 296 HOH HOH A . I 4 HOH 129 1329 297 HOH HOH A . I 4 HOH 130 1330 298 HOH HOH A . I 4 HOH 131 1331 299 HOH HOH A . I 4 HOH 132 1332 302 HOH HOH A . I 4 HOH 133 1333 303 HOH HOH A . J 4 HOH 1 504 3 HOH HOH B . J 4 HOH 2 505 5 HOH HOH B . J 4 HOH 3 506 9 HOH HOH B . J 4 HOH 4 507 10 HOH HOH B . J 4 HOH 5 508 12 HOH HOH B . J 4 HOH 6 509 13 HOH HOH B . J 4 HOH 7 510 17 HOH HOH B . J 4 HOH 8 511 18 HOH HOH B . J 4 HOH 9 512 19 HOH HOH B . J 4 HOH 10 513 23 HOH HOH B . J 4 HOH 11 514 26 HOH HOH B . J 4 HOH 12 515 28 HOH HOH B . J 4 HOH 13 516 29 HOH HOH B . J 4 HOH 14 517 32 HOH HOH B . J 4 HOH 15 518 33 HOH HOH B . J 4 HOH 16 519 34 HOH HOH B . J 4 HOH 17 520 35 HOH HOH B . J 4 HOH 18 521 37 HOH HOH B . J 4 HOH 19 522 38 HOH HOH B . J 4 HOH 20 523 39 HOH HOH B . J 4 HOH 21 524 40 HOH HOH B . J 4 HOH 22 525 41 HOH HOH B . J 4 HOH 23 526 42 HOH HOH B . J 4 HOH 24 527 43 HOH HOH B . J 4 HOH 25 528 45 HOH HOH B . J 4 HOH 26 529 49 HOH HOH B . J 4 HOH 27 530 51 HOH HOH B . J 4 HOH 28 531 53 HOH HOH B . J 4 HOH 29 532 57 HOH HOH B . J 4 HOH 30 533 58 HOH HOH B . J 4 HOH 31 534 62 HOH HOH B . J 4 HOH 32 535 64 HOH HOH B . J 4 HOH 33 536 66 HOH HOH B . J 4 HOH 34 537 68 HOH HOH B . J 4 HOH 35 538 69 HOH HOH B . J 4 HOH 36 539 70 HOH HOH B . J 4 HOH 37 540 71 HOH HOH B . J 4 HOH 38 541 75 HOH HOH B . J 4 HOH 39 542 87 HOH HOH B . J 4 HOH 40 543 89 HOH HOH B . J 4 HOH 41 544 91 HOH HOH B . J 4 HOH 42 545 96 HOH HOH B . J 4 HOH 43 546 104 HOH HOH B . J 4 HOH 44 547 108 HOH HOH B . J 4 HOH 45 548 110 HOH HOH B . J 4 HOH 46 549 112 HOH HOH B . J 4 HOH 47 550 115 HOH HOH B . J 4 HOH 48 551 117 HOH HOH B . J 4 HOH 49 552 119 HOH HOH B . J 4 HOH 50 553 121 HOH HOH B . J 4 HOH 51 554 122 HOH HOH B . J 4 HOH 52 555 124 HOH HOH B . J 4 HOH 53 556 126 HOH HOH B . J 4 HOH 54 557 131 HOH HOH B . J 4 HOH 55 558 132 HOH HOH B . J 4 HOH 56 559 134 HOH HOH B . J 4 HOH 57 560 136 HOH HOH B . J 4 HOH 58 561 137 HOH HOH B . J 4 HOH 59 562 140 HOH HOH B . J 4 HOH 60 563 142 HOH HOH B . J 4 HOH 61 564 143 HOH HOH B . J 4 HOH 62 565 1145 HOH HOH B . J 4 HOH 63 566 146 HOH HOH B . J 4 HOH 64 567 147 HOH HOH B . J 4 HOH 65 568 148 HOH HOH B . J 4 HOH 66 569 150 HOH HOH B . J 4 HOH 67 570 151 HOH HOH B . J 4 HOH 68 571 158 HOH HOH B . J 4 HOH 69 572 160 HOH HOH B . J 4 HOH 70 573 161 HOH HOH B . J 4 HOH 71 574 162 HOH HOH B . J 4 HOH 72 575 163 HOH HOH B . J 4 HOH 73 576 166 HOH HOH B . J 4 HOH 74 577 168 HOH HOH B . J 4 HOH 75 578 172 HOH HOH B . J 4 HOH 76 579 174 HOH HOH B . J 4 HOH 77 580 175 HOH HOH B . J 4 HOH 78 581 178 HOH HOH B . J 4 HOH 79 582 181 HOH HOH B . J 4 HOH 80 583 186 HOH HOH B . J 4 HOH 81 584 189 HOH HOH B . J 4 HOH 82 585 191 HOH HOH B . J 4 HOH 83 586 193 HOH HOH B . J 4 HOH 84 587 194 HOH HOH B . J 4 HOH 85 588 196 HOH HOH B . J 4 HOH 86 589 198 HOH HOH B . J 4 HOH 87 590 201 HOH HOH B . J 4 HOH 88 591 203 HOH HOH B . J 4 HOH 89 592 204 HOH HOH B . J 4 HOH 90 593 205 HOH HOH B . J 4 HOH 91 594 206 HOH HOH B . J 4 HOH 92 595 207 HOH HOH B . J 4 HOH 93 596 210 HOH HOH B . J 4 HOH 94 597 212 HOH HOH B . J 4 HOH 95 598 213 HOH HOH B . J 4 HOH 96 599 220 HOH HOH B . J 4 HOH 97 600 221 HOH HOH B . J 4 HOH 98 601 225 HOH HOH B . J 4 HOH 99 602 226 HOH HOH B . J 4 HOH 100 603 227 HOH HOH B . J 4 HOH 101 604 235 HOH HOH B . J 4 HOH 102 605 237 HOH HOH B . J 4 HOH 103 606 239 HOH HOH B . J 4 HOH 104 607 249 HOH HOH B . J 4 HOH 105 608 255 HOH HOH B . J 4 HOH 106 609 256 HOH HOH B . J 4 HOH 107 610 257 HOH HOH B . J 4 HOH 108 611 265 HOH HOH B . J 4 HOH 109 612 267 HOH HOH B . J 4 HOH 110 613 271 HOH HOH B . J 4 HOH 111 614 272 HOH HOH B . J 4 HOH 112 615 274 HOH HOH B . J 4 HOH 113 616 276 HOH HOH B . J 4 HOH 114 617 277 HOH HOH B . J 4 HOH 115 618 278 HOH HOH B . J 4 HOH 116 619 279 HOH HOH B . J 4 HOH 117 620 280 HOH HOH B . J 4 HOH 118 621 282 HOH HOH B . J 4 HOH 119 622 283 HOH HOH B . J 4 HOH 120 623 284 HOH HOH B . J 4 HOH 121 624 286 HOH HOH B . J 4 HOH 122 625 287 HOH HOH B . J 4 HOH 123 626 291 HOH HOH B . J 4 HOH 124 627 292 HOH HOH B . J 4 HOH 125 628 295 HOH HOH B . J 4 HOH 126 629 400 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 5530 ? 1 MORE -56 ? 1 'SSA (A^2)' 9340 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2005-05-03 2 'Structure model' 1 1 2008-04-30 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2021-10-27 5 'Structure model' 1 4 2023-08-23 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? _pdbx_audit_revision_details.details ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' 4 4 'Structure model' 'Database references' 5 4 'Structure model' 'Derived calculations' 6 4 'Structure model' 'Structure summary' 7 5 'Structure model' 'Data collection' 8 5 'Structure model' 'Refinement description' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' chem_comp 2 4 'Structure model' database_2 3 4 'Structure model' struct_ref_seq_dif 4 4 'Structure model' struct_site 5 5 'Structure model' chem_comp_atom 6 5 'Structure model' chem_comp_bond 7 5 'Structure model' pdbx_initial_refinement_model # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 4 'Structure model' '_chem_comp.pdbx_synonyms' 2 4 'Structure model' '_database_2.pdbx_DOI' 3 4 'Structure model' '_database_2.pdbx_database_accession' 4 4 'Structure model' '_struct_ref_seq_dif.details' 5 4 'Structure model' '_struct_site.pdbx_auth_asym_id' 6 4 'Structure model' '_struct_site.pdbx_auth_comp_id' 7 4 'Structure model' '_struct_site.pdbx_auth_seq_id' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 AMoRE phasing . ? 3 REFMAC refinement 5.1.19 ? 4 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 GLY _pdbx_validate_symm_contact.auth_seq_id_1 16 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 B _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 618 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 1_655 _pdbx_validate_symm_contact.dist 1.94 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CB A ARG 14 ? ? CG A ARG 14 ? ? 1.348 1.521 -0.173 0.027 N 2 1 CD A GLU 21 ? B OE2 A GLU 21 ? B 1.335 1.252 0.083 0.011 N 3 1 CD A GLU 34 ? ? OE1 A GLU 34 ? ? 1.396 1.252 0.144 0.011 N 4 1 CD A GLU 35 ? ? OE2 A GLU 35 ? ? 1.321 1.252 0.069 0.011 N 5 1 CD A GLU 65 ? ? OE2 A GLU 65 ? ? 1.122 1.252 -0.130 0.011 N 6 1 CB A CYS 67 ? ? SG A CYS 67 ? ? 1.624 1.812 -0.188 0.016 N 7 1 CB A CYS 95 ? A SG A CYS 95 ? A 1.673 1.812 -0.139 0.016 N 8 1 CA B THR 4 ? ? CB B THR 4 ? ? 1.777 1.529 0.248 0.026 N 9 1 CB B THR 4 ? ? OG1 B THR 4 ? ? 1.213 1.428 -0.215 0.020 N 10 1 NE B ARG 8 ? ? CZ B ARG 8 ? ? 1.412 1.326 0.086 0.013 N 11 1 NE B ARG 14 ? ? CZ B ARG 14 ? ? 1.228 1.326 -0.098 0.013 N 12 1 CA B GLN 18 ? ? CB B GLN 18 ? ? 1.667 1.535 0.132 0.022 N 13 1 CD B LYS 45 ? ? CE B LYS 45 ? ? 1.332 1.508 -0.176 0.025 N 14 1 CE B LYS 45 ? ? NZ B LYS 45 ? ? 1.290 1.486 -0.196 0.025 N 15 1 CB B MET 46 ? B CG B MET 46 ? B 1.729 1.509 0.220 0.032 N 16 1 CD1 B TYR 59 ? ? CE1 B TYR 59 ? ? 1.289 1.389 -0.100 0.015 N 17 1 CB B CYS 67 ? ? SG B CYS 67 ? ? 1.627 1.812 -0.185 0.016 N # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 87 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 87 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 87 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 117.02 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.28 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 7 ? CG ? A LYS 7 CG 2 1 Y 1 A LYS 7 ? CD ? A LYS 7 CD 3 1 Y 1 A LYS 7 ? CE ? A LYS 7 CE 4 1 Y 1 A LYS 7 ? NZ ? A LYS 7 NZ 5 1 Y 1 A LYS 41 ? CG ? A LYS 41 CG 6 1 Y 1 A LYS 41 ? CD ? A LYS 41 CD 7 1 Y 1 A LYS 41 ? CE ? A LYS 41 CE 8 1 Y 1 A LYS 41 ? NZ ? A LYS 41 NZ 9 1 Y 1 A LYS 43 ? CG ? A LYS 43 CG 10 1 Y 1 A LYS 43 ? CD ? A LYS 43 CD 11 1 Y 1 A LYS 43 ? CE ? A LYS 43 CE 12 1 Y 1 A LYS 43 ? NZ ? A LYS 43 NZ 13 1 Y 1 B LYS 41 ? CG ? B LYS 41 CG 14 1 Y 1 B LYS 41 ? CD ? B LYS 41 CD 15 1 Y 1 B LYS 41 ? CE ? B LYS 41 CE 16 1 Y 1 B LYS 41 ? NZ ? B LYS 41 NZ 17 1 Y 1 B LYS 43 ? CG ? B LYS 43 CG 18 1 Y 1 B LYS 43 ? CD ? B LYS 43 CD 19 1 Y 1 B LYS 43 ? CE ? B LYS 43 CE 20 1 Y 1 B LYS 43 ? NZ ? B LYS 43 NZ # loop_ _chem_comp_atom.comp_id _chem_comp_atom.atom_id _chem_comp_atom.type_symbol _chem_comp_atom.pdbx_aromatic_flag _chem_comp_atom.pdbx_stereo_config _chem_comp_atom.pdbx_ordinal 017 N1 N N N 1 017 C2 C Y N 2 017 C3 C Y N 3 017 C4 C Y N 4 017 C5 C Y N 5 017 C6 C Y N 6 017 C7 C Y N 7 017 S8 S N N 8 017 O9 O N N 9 017 O10 O N N 10 017 N11 N N N 11 017 C12 C N N 12 017 C13 C N N 13 017 C14 C N N 14 017 C15 C N N 15 017 C16 C N N 16 017 C17 C N R 17 017 O18 O N N 18 017 C19 C N S 19 017 N20 N N N 20 017 C21 C N N 21 017 O22 O N N 22 017 O23 O N N 23 017 C24 C N R 24 017 C25 C N N 25 017 O26 O N N 26 017 C27 C N R 27 017 O28 O N N 28 017 C29 C N N 29 017 C30 C N N 30 017 C31 C N S 31 017 C32 C N N 32 017 C33 C Y N 33 017 C34 C Y N 34 017 C35 C Y N 35 017 C36 C Y N 36 017 C37 C Y N 37 017 C38 C Y N 38 017 H11 H N N 39 017 H12 H N N 40 017 H3 H N N 41 017 H4 H N N 42 017 H6 H N N 43 017 H7 H N N 44 017 H121 H N N 45 017 H122 H N N 46 017 H13 H N N 47 017 H141 H N N 48 017 H142 H N N 49 017 H143 H N N 50 017 H151 H N N 51 017 H152 H N N 52 017 H153 H N N 53 017 H161 H N N 54 017 H162 H N N 55 017 H17 H N N 56 017 H18 H N N 57 017 H19 H N N 58 017 H20 H N N 59 017 H24 H N N 60 017 H251 H N N 61 017 H252 H N N 62 017 H27 H N N 63 017 H291 H N N 64 017 H292 H N N 65 017 H301 H N N 66 017 H302 H N N 67 017 H31 H N N 68 017 H321 H N N 69 017 H322 H N N 70 017 H33 H N N 71 017 H34 H N N 72 017 H35 H N N 73 017 H36 H N N 74 017 H37 H N N 75 ALA N N N N 76 ALA CA C N S 77 ALA C C N N 78 ALA O O N N 79 ALA CB C N N 80 ALA OXT O N N 81 ALA H H N N 82 ALA H2 H N N 83 ALA HA H N N 84 ALA HB1 H N N 85 ALA HB2 H N N 86 ALA HB3 H N N 87 ALA HXT H N N 88 ARG N N N N 89 ARG CA C N S 90 ARG C C N N 91 ARG O O N N 92 ARG CB C N N 93 ARG CG C N N 94 ARG CD C N N 95 ARG NE N N N 96 ARG CZ C N N 97 ARG NH1 N N N 98 ARG NH2 N N N 99 ARG OXT O N N 100 ARG H H N N 101 ARG H2 H N N 102 ARG HA H N N 103 ARG HB2 H N N 104 ARG HB3 H N N 105 ARG HG2 H N N 106 ARG HG3 H N N 107 ARG HD2 H N N 108 ARG HD3 H N N 109 ARG HE H N N 110 ARG HH11 H N N 111 ARG HH12 H N N 112 ARG HH21 H N N 113 ARG HH22 H N N 114 ARG HXT H N N 115 ASN N N N N 116 ASN CA C N S 117 ASN C C N N 118 ASN O O N N 119 ASN CB C N N 120 ASN CG C N N 121 ASN OD1 O N N 122 ASN ND2 N N N 123 ASN OXT O N N 124 ASN H H N N 125 ASN H2 H N N 126 ASN HA H N N 127 ASN HB2 H N N 128 ASN HB3 H N N 129 ASN HD21 H N N 130 ASN HD22 H N N 131 ASN HXT H N N 132 ASP N N N N 133 ASP CA C N S 134 ASP C C N N 135 ASP O O N N 136 ASP CB C N N 137 ASP CG C N N 138 ASP OD1 O N N 139 ASP OD2 O N N 140 ASP OXT O N N 141 ASP H H N N 142 ASP H2 H N N 143 ASP HA H N N 144 ASP HB2 H N N 145 ASP HB3 H N N 146 ASP HD2 H N N 147 ASP HXT H N N 148 CYS N N N N 149 CYS CA C N R 150 CYS C C N N 151 CYS O O N N 152 CYS CB C N N 153 CYS SG S N N 154 CYS OXT O N N 155 CYS H H N N 156 CYS H2 H N N 157 CYS HA H N N 158 CYS HB2 H N N 159 CYS HB3 H N N 160 CYS HG H N N 161 CYS HXT H N N 162 GLN N N N N 163 GLN CA C N S 164 GLN C C N N 165 GLN O O N N 166 GLN CB C N N 167 GLN CG C N N 168 GLN CD C N N 169 GLN OE1 O N N 170 GLN NE2 N N N 171 GLN OXT O N N 172 GLN H H N N 173 GLN H2 H N N 174 GLN HA H N N 175 GLN HB2 H N N 176 GLN HB3 H N N 177 GLN HG2 H N N 178 GLN HG3 H N N 179 GLN HE21 H N N 180 GLN HE22 H N N 181 GLN HXT H N N 182 GLU N N N N 183 GLU CA C N S 184 GLU C C N N 185 GLU O O N N 186 GLU CB C N N 187 GLU CG C N N 188 GLU CD C N N 189 GLU OE1 O N N 190 GLU OE2 O N N 191 GLU OXT O N N 192 GLU H H N N 193 GLU H2 H N N 194 GLU HA H N N 195 GLU HB2 H N N 196 GLU HB3 H N N 197 GLU HG2 H N N 198 GLU HG3 H N N 199 GLU HE2 H N N 200 GLU HXT H N N 201 GLY N N N N 202 GLY CA C N N 203 GLY C C N N 204 GLY O O N N 205 GLY OXT O N N 206 GLY H H N N 207 GLY H2 H N N 208 GLY HA2 H N N 209 GLY HA3 H N N 210 GLY HXT H N N 211 HIS N N N N 212 HIS CA C N S 213 HIS C C N N 214 HIS O O N N 215 HIS CB C N N 216 HIS CG C Y N 217 HIS ND1 N Y N 218 HIS CD2 C Y N 219 HIS CE1 C Y N 220 HIS NE2 N Y N 221 HIS OXT O N N 222 HIS H H N N 223 HIS H2 H N N 224 HIS HA H N N 225 HIS HB2 H N N 226 HIS HB3 H N N 227 HIS HD1 H N N 228 HIS HD2 H N N 229 HIS HE1 H N N 230 HIS HE2 H N N 231 HIS HXT H N N 232 HOH O O N N 233 HOH H1 H N N 234 HOH H2 H N N 235 ILE N N N N 236 ILE CA C N S 237 ILE C C N N 238 ILE O O N N 239 ILE CB C N S 240 ILE CG1 C N N 241 ILE CG2 C N N 242 ILE CD1 C N N 243 ILE OXT O N N 244 ILE H H N N 245 ILE H2 H N N 246 ILE HA H N N 247 ILE HB H N N 248 ILE HG12 H N N 249 ILE HG13 H N N 250 ILE HG21 H N N 251 ILE HG22 H N N 252 ILE HG23 H N N 253 ILE HD11 H N N 254 ILE HD12 H N N 255 ILE HD13 H N N 256 ILE HXT H N N 257 LEU N N N N 258 LEU CA C N S 259 LEU C C N N 260 LEU O O N N 261 LEU CB C N N 262 LEU CG C N N 263 LEU CD1 C N N 264 LEU CD2 C N N 265 LEU OXT O N N 266 LEU H H N N 267 LEU H2 H N N 268 LEU HA H N N 269 LEU HB2 H N N 270 LEU HB3 H N N 271 LEU HG H N N 272 LEU HD11 H N N 273 LEU HD12 H N N 274 LEU HD13 H N N 275 LEU HD21 H N N 276 LEU HD22 H N N 277 LEU HD23 H N N 278 LEU HXT H N N 279 LYS N N N N 280 LYS CA C N S 281 LYS C C N N 282 LYS O O N N 283 LYS CB C N N 284 LYS CG C N N 285 LYS CD C N N 286 LYS CE C N N 287 LYS NZ N N N 288 LYS OXT O N N 289 LYS H H N N 290 LYS H2 H N N 291 LYS HA H N N 292 LYS HB2 H N N 293 LYS HB3 H N N 294 LYS HG2 H N N 295 LYS HG3 H N N 296 LYS HD2 H N N 297 LYS HD3 H N N 298 LYS HE2 H N N 299 LYS HE3 H N N 300 LYS HZ1 H N N 301 LYS HZ2 H N N 302 LYS HZ3 H N N 303 LYS HXT H N N 304 MET N N N N 305 MET CA C N S 306 MET C C N N 307 MET O O N N 308 MET CB C N N 309 MET CG C N N 310 MET SD S N N 311 MET CE C N N 312 MET OXT O N N 313 MET H H N N 314 MET H2 H N N 315 MET HA H N N 316 MET HB2 H N N 317 MET HB3 H N N 318 MET HG2 H N N 319 MET HG3 H N N 320 MET HE1 H N N 321 MET HE2 H N N 322 MET HE3 H N N 323 MET HXT H N N 324 PHE N N N N 325 PHE CA C N S 326 PHE C C N N 327 PHE O O N N 328 PHE CB C N N 329 PHE CG C Y N 330 PHE CD1 C Y N 331 PHE CD2 C Y N 332 PHE CE1 C Y N 333 PHE CE2 C Y N 334 PHE CZ C Y N 335 PHE OXT O N N 336 PHE H H N N 337 PHE H2 H N N 338 PHE HA H N N 339 PHE HB2 H N N 340 PHE HB3 H N N 341 PHE HD1 H N N 342 PHE HD2 H N N 343 PHE HE1 H N N 344 PHE HE2 H N N 345 PHE HZ H N N 346 PHE HXT H N N 347 PO4 P P N N 348 PO4 O1 O N N 349 PO4 O2 O N N 350 PO4 O3 O N N 351 PO4 O4 O N N 352 PRO N N N N 353 PRO CA C N S 354 PRO C C N N 355 PRO O O N N 356 PRO CB C N N 357 PRO CG C N N 358 PRO CD C N N 359 PRO OXT O N N 360 PRO H H N N 361 PRO HA H N N 362 PRO HB2 H N N 363 PRO HB3 H N N 364 PRO HG2 H N N 365 PRO HG3 H N N 366 PRO HD2 H N N 367 PRO HD3 H N N 368 PRO HXT H N N 369 THR N N N N 370 THR CA C N S 371 THR C C N N 372 THR O O N N 373 THR CB C N R 374 THR OG1 O N N 375 THR CG2 C N N 376 THR OXT O N N 377 THR H H N N 378 THR H2 H N N 379 THR HA H N N 380 THR HB H N N 381 THR HG1 H N N 382 THR HG21 H N N 383 THR HG22 H N N 384 THR HG23 H N N 385 THR HXT H N N 386 TRP N N N N 387 TRP CA C N S 388 TRP C C N N 389 TRP O O N N 390 TRP CB C N N 391 TRP CG C Y N 392 TRP CD1 C Y N 393 TRP CD2 C Y N 394 TRP NE1 N Y N 395 TRP CE2 C Y N 396 TRP CE3 C Y N 397 TRP CZ2 C Y N 398 TRP CZ3 C Y N 399 TRP CH2 C Y N 400 TRP OXT O N N 401 TRP H H N N 402 TRP H2 H N N 403 TRP HA H N N 404 TRP HB2 H N N 405 TRP HB3 H N N 406 TRP HD1 H N N 407 TRP HE1 H N N 408 TRP HE3 H N N 409 TRP HZ2 H N N 410 TRP HZ3 H N N 411 TRP HH2 H N N 412 TRP HXT H N N 413 TYR N N N N 414 TYR CA C N S 415 TYR C C N N 416 TYR O O N N 417 TYR CB C N N 418 TYR CG C Y N 419 TYR CD1 C Y N 420 TYR CD2 C Y N 421 TYR CE1 C Y N 422 TYR CE2 C Y N 423 TYR CZ C Y N 424 TYR OH O N N 425 TYR OXT O N N 426 TYR H H N N 427 TYR H2 H N N 428 TYR HA H N N 429 TYR HB2 H N N 430 TYR HB3 H N N 431 TYR HD1 H N N 432 TYR HD2 H N N 433 TYR HE1 H N N 434 TYR HE2 H N N 435 TYR HH H N N 436 TYR HXT H N N 437 VAL N N N N 438 VAL CA C N S 439 VAL C C N N 440 VAL O O N N 441 VAL CB C N N 442 VAL CG1 C N N 443 VAL CG2 C N N 444 VAL OXT O N N 445 VAL H H N N 446 VAL H2 H N N 447 VAL HA H N N 448 VAL HB H N N 449 VAL HG11 H N N 450 VAL HG12 H N N 451 VAL HG13 H N N 452 VAL HG21 H N N 453 VAL HG22 H N N 454 VAL HG23 H N N 455 VAL HXT H N N 456 # loop_ _chem_comp_bond.comp_id _chem_comp_bond.atom_id_1 _chem_comp_bond.atom_id_2 _chem_comp_bond.value_order _chem_comp_bond.pdbx_aromatic_flag _chem_comp_bond.pdbx_stereo_config _chem_comp_bond.pdbx_ordinal 017 N1 C2 sing N N 1 017 N1 H11 sing N N 2 017 N1 H12 sing N N 3 017 C2 C3 doub Y N 4 017 C2 C7 sing Y N 5 017 C3 C4 sing Y N 6 017 C3 H3 sing N N 7 017 C4 C5 doub Y N 8 017 C4 H4 sing N N 9 017 C5 C6 sing Y N 10 017 C5 S8 sing N N 11 017 C6 C7 doub Y N 12 017 C6 H6 sing N N 13 017 C7 H7 sing N N 14 017 S8 O9 doub N N 15 017 S8 O10 doub N N 16 017 S8 N11 sing N N 17 017 N11 C12 sing N N 18 017 N11 C16 sing N N 19 017 C12 C13 sing N N 20 017 C12 H121 sing N N 21 017 C12 H122 sing N N 22 017 C13 C14 sing N N 23 017 C13 C15 sing N N 24 017 C13 H13 sing N N 25 017 C14 H141 sing N N 26 017 C14 H142 sing N N 27 017 C14 H143 sing N N 28 017 C15 H151 sing N N 29 017 C15 H152 sing N N 30 017 C15 H153 sing N N 31 017 C16 C17 sing N N 32 017 C16 H161 sing N N 33 017 C16 H162 sing N N 34 017 C17 O18 sing N N 35 017 C17 C19 sing N N 36 017 C17 H17 sing N N 37 017 O18 H18 sing N N 38 017 C19 N20 sing N N 39 017 C19 C32 sing N N 40 017 C19 H19 sing N N 41 017 N20 C21 sing N N 42 017 N20 H20 sing N N 43 017 C21 O22 doub N N 44 017 C21 O23 sing N N 45 017 O23 C24 sing N N 46 017 C24 C25 sing N N 47 017 C24 C31 sing N N 48 017 C24 H24 sing N N 49 017 C25 O26 sing N N 50 017 C25 H251 sing N N 51 017 C25 H252 sing N N 52 017 O26 C27 sing N N 53 017 C27 O28 sing N N 54 017 C27 C31 sing N N 55 017 C27 H27 sing N N 56 017 O28 C29 sing N N 57 017 C29 C30 sing N N 58 017 C29 H291 sing N N 59 017 C29 H292 sing N N 60 017 C30 C31 sing N N 61 017 C30 H301 sing N N 62 017 C30 H302 sing N N 63 017 C31 H31 sing N N 64 017 C32 C38 sing N N 65 017 C32 H321 sing N N 66 017 C32 H322 sing N N 67 017 C33 C34 doub Y N 68 017 C33 C38 sing Y N 69 017 C33 H33 sing N N 70 017 C34 C35 sing Y N 71 017 C34 H34 sing N N 72 017 C35 C36 doub Y N 73 017 C35 H35 sing N N 74 017 C36 C37 sing Y N 75 017 C36 H36 sing N N 76 017 C37 C38 doub Y N 77 017 C37 H37 sing N N 78 ALA N CA sing N N 79 ALA N H sing N N 80 ALA N H2 sing N N 81 ALA CA C sing N N 82 ALA CA CB sing N N 83 ALA CA HA sing N N 84 ALA C O doub N N 85 ALA C OXT sing N N 86 ALA CB HB1 sing N N 87 ALA CB HB2 sing N N 88 ALA CB HB3 sing N N 89 ALA OXT HXT sing N N 90 ARG N CA sing N N 91 ARG N H sing N N 92 ARG N H2 sing N N 93 ARG CA C sing N N 94 ARG CA CB sing N N 95 ARG CA HA sing N N 96 ARG C O doub N N 97 ARG C OXT sing N N 98 ARG CB CG sing N N 99 ARG CB HB2 sing N N 100 ARG CB HB3 sing N N 101 ARG CG CD sing N N 102 ARG CG HG2 sing N N 103 ARG CG HG3 sing N N 104 ARG CD NE sing N N 105 ARG CD HD2 sing N N 106 ARG CD HD3 sing N N 107 ARG NE CZ sing N N 108 ARG NE HE sing N N 109 ARG CZ NH1 sing N N 110 ARG CZ NH2 doub N N 111 ARG NH1 HH11 sing N N 112 ARG NH1 HH12 sing N N 113 ARG NH2 HH21 sing N N 114 ARG NH2 HH22 sing N N 115 ARG OXT HXT sing N N 116 ASN N CA sing N N 117 ASN N H sing N N 118 ASN N H2 sing N N 119 ASN CA C sing N N 120 ASN CA CB sing N N 121 ASN CA HA sing N N 122 ASN C O doub N N 123 ASN C OXT sing N N 124 ASN CB CG sing N N 125 ASN CB HB2 sing N N 126 ASN CB HB3 sing N N 127 ASN CG OD1 doub N N 128 ASN CG ND2 sing N N 129 ASN ND2 HD21 sing N N 130 ASN ND2 HD22 sing N N 131 ASN OXT HXT sing N N 132 ASP N CA sing N N 133 ASP N H sing N N 134 ASP N H2 sing N N 135 ASP CA C sing N N 136 ASP CA CB sing N N 137 ASP CA HA sing N N 138 ASP C O doub N N 139 ASP C OXT sing N N 140 ASP CB CG sing N N 141 ASP CB HB2 sing N N 142 ASP CB HB3 sing N N 143 ASP CG OD1 doub N N 144 ASP CG OD2 sing N N 145 ASP OD2 HD2 sing N N 146 ASP OXT HXT sing N N 147 CYS N CA sing N N 148 CYS N H sing N N 149 CYS N H2 sing N N 150 CYS CA C sing N N 151 CYS CA CB sing N N 152 CYS CA HA sing N N 153 CYS C O doub N N 154 CYS C OXT sing N N 155 CYS CB SG sing N N 156 CYS CB HB2 sing N N 157 CYS CB HB3 sing N N 158 CYS SG HG sing N N 159 CYS OXT HXT sing N N 160 GLN N CA sing N N 161 GLN N H sing N N 162 GLN N H2 sing N N 163 GLN CA C sing N N 164 GLN CA CB sing N N 165 GLN CA HA sing N N 166 GLN C O doub N N 167 GLN C OXT sing N N 168 GLN CB CG sing N N 169 GLN CB HB2 sing N N 170 GLN CB HB3 sing N N 171 GLN CG CD sing N N 172 GLN CG HG2 sing N N 173 GLN CG HG3 sing N N 174 GLN CD OE1 doub N N 175 GLN CD NE2 sing N N 176 GLN NE2 HE21 sing N N 177 GLN NE2 HE22 sing N N 178 GLN OXT HXT sing N N 179 GLU N CA sing N N 180 GLU N H sing N N 181 GLU N H2 sing N N 182 GLU CA C sing N N 183 GLU CA CB sing N N 184 GLU CA HA sing N N 185 GLU C O doub N N 186 GLU C OXT sing N N 187 GLU CB CG sing N N 188 GLU CB HB2 sing N N 189 GLU CB HB3 sing N N 190 GLU CG CD sing N N 191 GLU CG HG2 sing N N 192 GLU CG HG3 sing N N 193 GLU CD OE1 doub N N 194 GLU CD OE2 sing N N 195 GLU OE2 HE2 sing N N 196 GLU OXT HXT sing N N 197 GLY N CA sing N N 198 GLY N H sing N N 199 GLY N H2 sing N N 200 GLY CA C sing N N 201 GLY CA HA2 sing N N 202 GLY CA HA3 sing N N 203 GLY C O doub N N 204 GLY C OXT sing N N 205 GLY OXT HXT sing N N 206 HIS N CA sing N N 207 HIS N H sing N N 208 HIS N H2 sing N N 209 HIS CA C sing N N 210 HIS CA CB sing N N 211 HIS CA HA sing N N 212 HIS C O doub N N 213 HIS C OXT sing N N 214 HIS CB CG sing N N 215 HIS CB HB2 sing N N 216 HIS CB HB3 sing N N 217 HIS CG ND1 sing Y N 218 HIS CG CD2 doub Y N 219 HIS ND1 CE1 doub Y N 220 HIS ND1 HD1 sing N N 221 HIS CD2 NE2 sing Y N 222 HIS CD2 HD2 sing N N 223 HIS CE1 NE2 sing Y N 224 HIS CE1 HE1 sing N N 225 HIS NE2 HE2 sing N N 226 HIS OXT HXT sing N N 227 HOH O H1 sing N N 228 HOH O H2 sing N N 229 ILE N CA sing N N 230 ILE N H sing N N 231 ILE N H2 sing N N 232 ILE CA C sing N N 233 ILE CA CB sing N N 234 ILE CA HA sing N N 235 ILE C O doub N N 236 ILE C OXT sing N N 237 ILE CB CG1 sing N N 238 ILE CB CG2 sing N N 239 ILE CB HB sing N N 240 ILE CG1 CD1 sing N N 241 ILE CG1 HG12 sing N N 242 ILE CG1 HG13 sing N N 243 ILE CG2 HG21 sing N N 244 ILE CG2 HG22 sing N N 245 ILE CG2 HG23 sing N N 246 ILE CD1 HD11 sing N N 247 ILE CD1 HD12 sing N N 248 ILE CD1 HD13 sing N N 249 ILE OXT HXT sing N N 250 LEU N CA sing N N 251 LEU N H sing N N 252 LEU N H2 sing N N 253 LEU CA C sing N N 254 LEU CA CB sing N N 255 LEU CA HA sing N N 256 LEU C O doub N N 257 LEU C OXT sing N N 258 LEU CB CG sing N N 259 LEU CB HB2 sing N N 260 LEU CB HB3 sing N N 261 LEU CG CD1 sing N N 262 LEU CG CD2 sing N N 263 LEU CG HG sing N N 264 LEU CD1 HD11 sing N N 265 LEU CD1 HD12 sing N N 266 LEU CD1 HD13 sing N N 267 LEU CD2 HD21 sing N N 268 LEU CD2 HD22 sing N N 269 LEU CD2 HD23 sing N N 270 LEU OXT HXT sing N N 271 LYS N CA sing N N 272 LYS N H sing N N 273 LYS N H2 sing N N 274 LYS CA C sing N N 275 LYS CA CB sing N N 276 LYS CA HA sing N N 277 LYS C O doub N N 278 LYS C OXT sing N N 279 LYS CB CG sing N N 280 LYS CB HB2 sing N N 281 LYS CB HB3 sing N N 282 LYS CG CD sing N N 283 LYS CG HG2 sing N N 284 LYS CG HG3 sing N N 285 LYS CD CE sing N N 286 LYS CD HD2 sing N N 287 LYS CD HD3 sing N N 288 LYS CE NZ sing N N 289 LYS CE HE2 sing N N 290 LYS CE HE3 sing N N 291 LYS NZ HZ1 sing N N 292 LYS NZ HZ2 sing N N 293 LYS NZ HZ3 sing N N 294 LYS OXT HXT sing N N 295 MET N CA sing N N 296 MET N H sing N N 297 MET N H2 sing N N 298 MET CA C sing N N 299 MET CA CB sing N N 300 MET CA HA sing N N 301 MET C O doub N N 302 MET C OXT sing N N 303 MET CB CG sing N N 304 MET CB HB2 sing N N 305 MET CB HB3 sing N N 306 MET CG SD sing N N 307 MET CG HG2 sing N N 308 MET CG HG3 sing N N 309 MET SD CE sing N N 310 MET CE HE1 sing N N 311 MET CE HE2 sing N N 312 MET CE HE3 sing N N 313 MET OXT HXT sing N N 314 PHE N CA sing N N 315 PHE N H sing N N 316 PHE N H2 sing N N 317 PHE CA C sing N N 318 PHE CA CB sing N N 319 PHE CA HA sing N N 320 PHE C O doub N N 321 PHE C OXT sing N N 322 PHE CB CG sing N N 323 PHE CB HB2 sing N N 324 PHE CB HB3 sing N N 325 PHE CG CD1 doub Y N 326 PHE CG CD2 sing Y N 327 PHE CD1 CE1 sing Y N 328 PHE CD1 HD1 sing N N 329 PHE CD2 CE2 doub Y N 330 PHE CD2 HD2 sing N N 331 PHE CE1 CZ doub Y N 332 PHE CE1 HE1 sing N N 333 PHE CE2 CZ sing Y N 334 PHE CE2 HE2 sing N N 335 PHE CZ HZ sing N N 336 PHE OXT HXT sing N N 337 PO4 P O1 doub N N 338 PO4 P O2 sing N N 339 PO4 P O3 sing N N 340 PO4 P O4 sing N N 341 PRO N CA sing N N 342 PRO N CD sing N N 343 PRO N H sing N N 344 PRO CA C sing N N 345 PRO CA CB sing N N 346 PRO CA HA sing N N 347 PRO C O doub N N 348 PRO C OXT sing N N 349 PRO CB CG sing N N 350 PRO CB HB2 sing N N 351 PRO CB HB3 sing N N 352 PRO CG CD sing N N 353 PRO CG HG2 sing N N 354 PRO CG HG3 sing N N 355 PRO CD HD2 sing N N 356 PRO CD HD3 sing N N 357 PRO OXT HXT sing N N 358 THR N CA sing N N 359 THR N H sing N N 360 THR N H2 sing N N 361 THR CA C sing N N 362 THR CA CB sing N N 363 THR CA HA sing N N 364 THR C O doub N N 365 THR C OXT sing N N 366 THR CB OG1 sing N N 367 THR CB CG2 sing N N 368 THR CB HB sing N N 369 THR OG1 HG1 sing N N 370 THR CG2 HG21 sing N N 371 THR CG2 HG22 sing N N 372 THR CG2 HG23 sing N N 373 THR OXT HXT sing N N 374 TRP N CA sing N N 375 TRP N H sing N N 376 TRP N H2 sing N N 377 TRP CA C sing N N 378 TRP CA CB sing N N 379 TRP CA HA sing N N 380 TRP C O doub N N 381 TRP C OXT sing N N 382 TRP CB CG sing N N 383 TRP CB HB2 sing N N 384 TRP CB HB3 sing N N 385 TRP CG CD1 doub Y N 386 TRP CG CD2 sing Y N 387 TRP CD1 NE1 sing Y N 388 TRP CD1 HD1 sing N N 389 TRP CD2 CE2 doub Y N 390 TRP CD2 CE3 sing Y N 391 TRP NE1 CE2 sing Y N 392 TRP NE1 HE1 sing N N 393 TRP CE2 CZ2 sing Y N 394 TRP CE3 CZ3 doub Y N 395 TRP CE3 HE3 sing N N 396 TRP CZ2 CH2 doub Y N 397 TRP CZ2 HZ2 sing N N 398 TRP CZ3 CH2 sing Y N 399 TRP CZ3 HZ3 sing N N 400 TRP CH2 HH2 sing N N 401 TRP OXT HXT sing N N 402 TYR N CA sing N N 403 TYR N H sing N N 404 TYR N H2 sing N N 405 TYR CA C sing N N 406 TYR CA CB sing N N 407 TYR CA HA sing N N 408 TYR C O doub N N 409 TYR C OXT sing N N 410 TYR CB CG sing N N 411 TYR CB HB2 sing N N 412 TYR CB HB3 sing N N 413 TYR CG CD1 doub Y N 414 TYR CG CD2 sing Y N 415 TYR CD1 CE1 sing Y N 416 TYR CD1 HD1 sing N N 417 TYR CD2 CE2 doub Y N 418 TYR CD2 HD2 sing N N 419 TYR CE1 CZ doub Y N 420 TYR CE1 HE1 sing N N 421 TYR CE2 CZ sing Y N 422 TYR CE2 HE2 sing N N 423 TYR CZ OH sing N N 424 TYR OH HH sing N N 425 TYR OXT HXT sing N N 426 VAL N CA sing N N 427 VAL N H sing N N 428 VAL N H2 sing N N 429 VAL CA C sing N N 430 VAL CA CB sing N N 431 VAL CA HA sing N N 432 VAL C O doub N N 433 VAL C OXT sing N N 434 VAL CB CG1 sing N N 435 VAL CB CG2 sing N N 436 VAL CB HB sing N N 437 VAL CG1 HG11 sing N N 438 VAL CG1 HG12 sing N N 439 VAL CG1 HG13 sing N N 440 VAL CG2 HG21 sing N N 441 VAL CG2 HG22 sing N N 442 VAL CG2 HG23 sing N N 443 VAL OXT HXT sing N N 444 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'PHOSPHATE ION' PO4 3 '(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE' 017 4 water HOH # _pdbx_initial_refinement_model.id 1 _pdbx_initial_refinement_model.entity_id_list ? _pdbx_initial_refinement_model.type 'experimental model' _pdbx_initial_refinement_model.source_name PDB _pdbx_initial_refinement_model.accession_code 1F7A _pdbx_initial_refinement_model.details ? # If you find results from this site helpful for your research, please cite one of our papers:
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