data_4DWM # _entry.id 4DWM # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4DWM RCSB RCSB070874 WWPDB D_1000070874 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3MRW _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4DWM _pdbx_database_status.recvd_initial_deposition_date 2012-02-25 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Yamini, S.' 1 'Pandey, S.' 2 'Sinha, M.' 3 'Kaur, P.' 4 'Sharma, S.' 5 'Singh, T.P.' 6 # _citation.id primary _citation.title 'Crystal structure of the complex of type I Ribosome inactivating protein with N-acetylglucosamine at 1.62 A resolution' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Yamini, S.' 1 primary 'Pandey, S.' 2 primary 'Sinha, M.' 3 primary 'Kaur, P.' 4 primary 'Sharma, S.' 5 primary 'Singh, T.P.' 6 # _cell.entry_id 4DWM _cell.length_a 130.198 _cell.length_b 130.198 _cell.length_c 40.510 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 9 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4DWM _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 _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 nat 'rRNA N-glycosidase' 27093.756 1 3.2.2.22 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 4 water nat water 18.015 281 ? ? ? ? # _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 ;DVSFRLSGADPSSYGMFIKDLRNALPHTEKVYNIPLLLPSVSGAGRYLLMHLFNYDGNTITVAVDVTNVYIMGYLALTTS YFFNEPAADLASQYVFRSARRKITLPYSGNYERLQIAAGKPREKIPIGLPALDTAISTLLHYDSTAAAGALLVLIQTTAE AARFKYIEQQIQERAYRDEVPSSATISLENSWSGLSKQIQLAQGNNGVFRTPTVLVDSKGNRVQITNVTSNVVTSNIQLL LNTKNI ; _entity_poly.pdbx_seq_one_letter_code_can ;DVSFRLSGADPSSYGMFIKDLRNALPHTEKVYNIPLLLPSVSGAGRYLLMHLFNYDGNTITVAVDVTNVYIMGYLALTTS YFFNEPAADLASQYVFRSARRKITLPYSGNYERLQIAAGKPREKIPIGLPALDTAISTLLHYDSTAAAGALLVLIQTTAE AARFKYIEQQIQERAYRDEVPSSATISLENSWSGLSKQIQLAQGNNGVFRTPTVLVDSKGNRVQITNVTSNVVTSNIQLL LNTKNI ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 VAL n 1 3 SER n 1 4 PHE n 1 5 ARG n 1 6 LEU n 1 7 SER n 1 8 GLY n 1 9 ALA n 1 10 ASP n 1 11 PRO n 1 12 SER n 1 13 SER n 1 14 TYR n 1 15 GLY n 1 16 MET n 1 17 PHE n 1 18 ILE n 1 19 LYS n 1 20 ASP n 1 21 LEU n 1 22 ARG n 1 23 ASN n 1 24 ALA n 1 25 LEU n 1 26 PRO n 1 27 HIS n 1 28 THR n 1 29 GLU n 1 30 LYS n 1 31 VAL n 1 32 TYR n 1 33 ASN n 1 34 ILE n 1 35 PRO n 1 36 LEU n 1 37 LEU n 1 38 LEU n 1 39 PRO n 1 40 SER n 1 41 VAL n 1 42 SER n 1 43 GLY n 1 44 ALA n 1 45 GLY n 1 46 ARG n 1 47 TYR n 1 48 LEU n 1 49 LEU n 1 50 MET n 1 51 HIS n 1 52 LEU n 1 53 PHE n 1 54 ASN n 1 55 TYR n 1 56 ASP n 1 57 GLY n 1 58 ASN n 1 59 THR n 1 60 ILE n 1 61 THR n 1 62 VAL n 1 63 ALA n 1 64 VAL n 1 65 ASP n 1 66 VAL n 1 67 THR n 1 68 ASN n 1 69 VAL n 1 70 TYR n 1 71 ILE n 1 72 MET n 1 73 GLY n 1 74 TYR n 1 75 LEU n 1 76 ALA n 1 77 LEU n 1 78 THR n 1 79 THR n 1 80 SER n 1 81 TYR n 1 82 PHE n 1 83 PHE n 1 84 ASN n 1 85 GLU n 1 86 PRO n 1 87 ALA n 1 88 ALA n 1 89 ASP n 1 90 LEU n 1 91 ALA n 1 92 SER n 1 93 GLN n 1 94 TYR n 1 95 VAL n 1 96 PHE n 1 97 ARG n 1 98 SER n 1 99 ALA n 1 100 ARG n 1 101 ARG n 1 102 LYS n 1 103 ILE n 1 104 THR n 1 105 LEU n 1 106 PRO n 1 107 TYR n 1 108 SER n 1 109 GLY n 1 110 ASN n 1 111 TYR n 1 112 GLU n 1 113 ARG n 1 114 LEU n 1 115 GLN n 1 116 ILE n 1 117 ALA n 1 118 ALA n 1 119 GLY n 1 120 LYS n 1 121 PRO n 1 122 ARG n 1 123 GLU n 1 124 LYS n 1 125 ILE n 1 126 PRO n 1 127 ILE n 1 128 GLY n 1 129 LEU n 1 130 PRO n 1 131 ALA n 1 132 LEU n 1 133 ASP n 1 134 THR n 1 135 ALA n 1 136 ILE n 1 137 SER n 1 138 THR n 1 139 LEU n 1 140 LEU n 1 141 HIS n 1 142 TYR n 1 143 ASP n 1 144 SER n 1 145 THR n 1 146 ALA n 1 147 ALA n 1 148 ALA n 1 149 GLY n 1 150 ALA n 1 151 LEU n 1 152 LEU n 1 153 VAL n 1 154 LEU n 1 155 ILE n 1 156 GLN n 1 157 THR n 1 158 THR n 1 159 ALA n 1 160 GLU n 1 161 ALA n 1 162 ALA n 1 163 ARG n 1 164 PHE n 1 165 LYS n 1 166 TYR n 1 167 ILE n 1 168 GLU n 1 169 GLN n 1 170 GLN n 1 171 ILE n 1 172 GLN n 1 173 GLU n 1 174 ARG n 1 175 ALA n 1 176 TYR n 1 177 ARG n 1 178 ASP n 1 179 GLU n 1 180 VAL n 1 181 PRO n 1 182 SER n 1 183 SER n 1 184 ALA n 1 185 THR n 1 186 ILE n 1 187 SER n 1 188 LEU n 1 189 GLU n 1 190 ASN n 1 191 SER n 1 192 TRP n 1 193 SER n 1 194 GLY n 1 195 LEU n 1 196 SER n 1 197 LYS n 1 198 GLN n 1 199 ILE n 1 200 GLN n 1 201 LEU n 1 202 ALA n 1 203 GLN n 1 204 GLY n 1 205 ASN n 1 206 ASN n 1 207 GLY n 1 208 VAL n 1 209 PHE n 1 210 ARG n 1 211 THR n 1 212 PRO n 1 213 THR n 1 214 VAL n 1 215 LEU n 1 216 VAL n 1 217 ASP n 1 218 SER n 1 219 LYS n 1 220 GLY n 1 221 ASN n 1 222 ARG n 1 223 VAL n 1 224 GLN n 1 225 ILE n 1 226 THR n 1 227 ASN n 1 228 VAL n 1 229 THR n 1 230 SER n 1 231 ASN n 1 232 VAL n 1 233 VAL n 1 234 THR n 1 235 SER n 1 236 ASN n 1 237 ILE n 1 238 GLN n 1 239 LEU n 1 240 LEU n 1 241 LEU n 1 242 ASN n 1 243 THR n 1 244 LYS n 1 245 ASN n 1 246 ILE n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'Bitter gourd' _entity_src_nat.pdbx_organism_scientific 'Momordica balsamina' _entity_src_nat.pdbx_ncbi_taxonomy_id 3672 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code D9J2T9_MOMBA _struct_ref.pdbx_db_accession D9J2T9 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;DVSFRLSGADPSSYGMFIKDLRNALPHTEKVYNIPLLLPSVSGAGRYLLMHLFNYDGNTITVAVDVTNVYIMGYLALTTS YFFNEPAADLASQYVFRSARRKITLPYSGNYERLQIAAGKPREKIPIGLPALDTAISTLLHYDSTAAAGALLVLIQTTAE AARFKYIEQQIQERAYRDEVPSSATISLENSWSGLSKQIQLAQGNNGVFRTPTVLVDSKGNRVQITNVTSNVVTSNIQLL LNTKNI ; _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4DWM _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 246 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession D9J2T9 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 246 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 246 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4DWM _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.44 _exptl_crystal.density_percent_sol 49.57 _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 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.8 _exptl_crystal_grow.pdbx_details '14% PEG 6000, 100mM citrate buffer, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 77 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2011-10-04 _diffrn_detector.details mirror # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator Graphite _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE BM14' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline BM14 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.97 # _reflns.entry_id 4DWM _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 65.10 _reflns.d_resolution_high 1.62 _reflns.number_obs 40774 _reflns.number_all 40774 _reflns.percent_possible_obs 99.2 _reflns.pdbx_Rmerge_I_obs 0.036 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 27.3 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _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 1.62 _reflns_shell.d_res_low 1.65 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.462 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.3 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4DWM _refine.ls_number_reflns_obs 30951 _refine.ls_number_reflns_all 40774 _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 50.00 _refine.ls_d_res_high 1.62 _refine.ls_percent_reflns_obs 100.00 _refine.ls_R_factor_obs 0.15808 _refine.ls_R_factor_all 0.15905 _refine.ls_R_factor_R_work 0.15626 _refine.ls_R_factor_R_free 0.19283 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_free 1604 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.974 _refine.correlation_coeff_Fo_to_Fc_free 0.961 _refine.B_iso_mean 24.226 _refine.aniso_B[1][1] -0.79 _refine.aniso_B[2][2] -0.79 _refine.aniso_B[3][3] 1.19 _refine.aniso_B[1][2] -0.40 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _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 3MRW _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 0.082 _refine.pdbx_overall_ESU_R_Free 0.085 _refine.overall_SU_ML 0.056 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.603 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _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_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1911 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 41 _refine_hist.number_atoms_solvent 281 _refine_hist.number_atoms_total 2233 _refine_hist.d_res_high 1.62 _refine_hist.d_res_low 50.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.022 0.022 ? 1987 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.873 1.987 ? 2704 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.578 5.000 ? 245 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.204 23.929 ? 84 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 14.096 15.000 ? 322 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 18.232 15.000 ? 13 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.188 0.200 ? 322 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.014 0.021 ? 1480 ? 'X-RAY DIFFRACTION' r_mcbond_it 1.521 1.500 ? 1227 ? 'X-RAY DIFFRACTION' r_mcangle_it 2.532 2.000 ? 1988 ? 'X-RAY DIFFRACTION' r_scbond_it 4.061 3.000 ? 760 ? 'X-RAY DIFFRACTION' r_scangle_it 6.286 4.500 ? 716 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.620 _refine_ls_shell.d_res_low 1.662 _refine_ls_shell.number_reflns_R_work 2312 _refine_ls_shell.R_factor_R_work 0.232 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.R_factor_R_free 0.269 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 118 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 4DWM _struct.title 'Crystal structure of the complex of type I Ribosome inactivating protein with N-acetylglucosamine at 1.62 A resolution' _struct.pdbx_descriptor 'rRNA N-glycosidase (E.C.3.2.2.22)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4DWM _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'RIP, Plant protein, N-acetylglucosamine, 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 2 ? C N N 3 ? D N N 3 ? E N N 2 ? F N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 10 ? ALA A 24 ? ASP A 10 ALA A 24 1 ? 15 HELX_P HELX_P2 2 SER A 42 ? GLY A 45 ? SER A 42 GLY A 45 5 ? 4 HELX_P HELX_P3 3 GLU A 85 ? SER A 92 ? GLU A 85 SER A 92 1 ? 8 HELX_P HELX_P4 4 ASN A 110 ? GLY A 119 ? ASN A 110 GLY A 119 1 ? 10 HELX_P HELX_P5 5 PRO A 121 ? ILE A 125 ? PRO A 121 ILE A 125 5 ? 5 HELX_P HELX_P6 6 GLY A 128 ? LEU A 140 ? GLY A 128 LEU A 140 1 ? 13 HELX_P HELX_P7 7 ASP A 143 ? THR A 158 ? ASP A 143 THR A 158 1 ? 16 HELX_P HELX_P8 8 THR A 158 ? PHE A 164 ? THR A 158 PHE A 164 1 ? 7 HELX_P HELX_P9 9 PHE A 164 ? ARG A 174 ? PHE A 164 ARG A 174 1 ? 11 HELX_P HELX_P10 10 SER A 182 ? GLN A 203 ? SER A 182 GLN A 203 1 ? 22 HELX_P HELX_P11 11 SER A 230 ? SER A 235 ? SER A 230 SER A 235 1 ? 6 HELX_P HELX_P12 12 ASN A 242 ? ILE A 246 ? ASN A 242 ILE A 246 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # _struct_conn.id covale1 _struct_conn.conn_type_id covale _struct_conn.pdbx_leaving_atom_flag ? _struct_conn.pdbx_PDB_id ? _struct_conn.ptnr1_label_asym_id A _struct_conn.ptnr1_label_comp_id ASN _struct_conn.ptnr1_label_seq_id 227 _struct_conn.ptnr1_label_atom_id ND2 _struct_conn.pdbx_ptnr1_label_alt_id ? _struct_conn.pdbx_ptnr1_PDB_ins_code ? _struct_conn.pdbx_ptnr1_standard_comp_id ? _struct_conn.ptnr1_symmetry 1_555 _struct_conn.ptnr2_label_asym_id B _struct_conn.ptnr2_label_comp_id NAG _struct_conn.ptnr2_label_seq_id . _struct_conn.ptnr2_label_atom_id C1 _struct_conn.pdbx_ptnr2_label_alt_id ? _struct_conn.pdbx_ptnr2_PDB_ins_code ? _struct_conn.ptnr1_auth_asym_id A _struct_conn.ptnr1_auth_comp_id ASN _struct_conn.ptnr1_auth_seq_id 227 _struct_conn.ptnr2_auth_asym_id A _struct_conn.ptnr2_auth_comp_id NAG _struct_conn.ptnr2_auth_seq_id 301 _struct_conn.ptnr2_symmetry 1_555 _struct_conn.pdbx_ptnr3_label_atom_id ? _struct_conn.pdbx_ptnr3_label_seq_id ? _struct_conn.pdbx_ptnr3_label_comp_id ? _struct_conn.pdbx_ptnr3_label_asym_id ? _struct_conn.pdbx_ptnr3_label_alt_id ? _struct_conn.pdbx_ptnr3_PDB_ins_code ? _struct_conn.details ? _struct_conn.pdbx_dist_value 1.452 _struct_conn.pdbx_value_order ? # _struct_conn_type.id covale _struct_conn_type.criteria ? _struct_conn_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 2 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? parallel B 1 2 ? anti-parallel C 1 2 ? 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 VAL A 2 ? ARG A 5 ? VAL A 2 ARG A 5 A 2 TYR A 47 ? PHE A 53 ? TYR A 47 PHE A 53 A 3 THR A 59 ? ASP A 65 ? THR A 59 ASP A 65 A 4 ILE A 71 ? ALA A 76 ? ILE A 71 ALA A 76 A 5 THR A 79 ? PHE A 82 ? THR A 79 PHE A 82 A 6 ARG A 101 ? THR A 104 ? ARG A 101 THR A 104 B 1 HIS A 27 ? VAL A 31 ? HIS A 27 VAL A 31 B 2 ILE A 34 ? LEU A 37 ? ILE A 34 LEU A 37 C 1 VAL A 208 ? VAL A 216 ? VAL A 208 VAL A 216 C 2 ARG A 222 ? ASN A 227 ? ARG A 222 ASN A 227 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N VAL A 2 ? N VAL A 2 O HIS A 51 ? O HIS A 51 A 2 3 N LEU A 48 ? N LEU A 48 O VAL A 64 ? O VAL A 64 A 3 4 N ALA A 63 ? N ALA A 63 O MET A 72 ? O MET A 72 A 4 5 N ALA A 76 ? N ALA A 76 O THR A 79 ? O THR A 79 A 5 6 N SER A 80 ? N SER A 80 O ILE A 103 ? O ILE A 103 B 1 2 N GLU A 29 ? N GLU A 29 O LEU A 36 ? O LEU A 36 C 1 2 N THR A 213 ? N THR A 213 O ILE A 225 ? O ILE A 225 # 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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 302' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 303' AC4 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE NAG A 304' # 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 6 THR A 226 ? THR A 226 . ? 1_555 ? 2 AC1 6 ASN A 227 ? ASN A 227 . ? 1_555 ? 3 AC1 6 THR A 229 ? THR A 229 . ? 1_555 ? 4 AC1 6 HOH F . ? HOH A 497 . ? 1_555 ? 5 AC1 6 HOH F . ? HOH A 662 . ? 1_555 ? 6 AC1 6 HOH F . ? HOH A 663 . ? 1_555 ? 7 AC2 8 LEU A 6 ? LEU A 6 . ? 1_555 ? 8 AC2 8 ALA A 9 ? ALA A 9 . ? 1_555 ? 9 AC2 8 ARG A 101 ? ARG A 101 . ? 2_555 ? 10 AC2 8 ILE A 103 ? ILE A 103 . ? 2_555 ? 11 AC2 8 PRO A 130 ? PRO A 130 . ? 1_555 ? 12 AC2 8 ALA A 175 ? ALA A 175 . ? 1_555 ? 13 AC2 8 HOH F . ? HOH A 452 . ? 1_555 ? 14 AC2 8 HOH F . ? HOH A 507 . ? 1_555 ? 15 AC3 5 ASN A 33 ? ASN A 33 . ? 1_555 ? 16 AC3 5 THR A 234 ? THR A 234 . ? 1_555 ? 17 AC3 5 SER A 235 ? SER A 235 . ? 1_555 ? 18 AC3 5 GLN A 238 ? GLN A 238 . ? 1_555 ? 19 AC3 5 HOH F . ? HOH A 595 . ? 1_555 ? 20 AC4 12 VAL A 69 ? VAL A 69 . ? 1_555 ? 21 AC4 12 TYR A 70 ? TYR A 70 . ? 1_555 ? 22 AC4 12 ILE A 71 ? ILE A 71 . ? 1_555 ? 23 AC4 12 GLY A 109 ? GLY A 109 . ? 1_555 ? 24 AC4 12 ASN A 110 ? ASN A 110 . ? 1_555 ? 25 AC4 12 TYR A 111 ? TYR A 111 . ? 1_555 ? 26 AC4 12 ILE A 155 ? ILE A 155 . ? 1_555 ? 27 AC4 12 ALA A 159 ? ALA A 159 . ? 1_555 ? 28 AC4 12 ARG A 163 ? ARG A 163 . ? 1_555 ? 29 AC4 12 HOH F . ? HOH A 673 . ? 1_555 ? 30 AC4 12 HOH F . ? HOH A 674 . ? 1_555 ? 31 AC4 12 HOH F . ? HOH A 675 . ? 1_555 ? # _database_PDB_matrix.entry_id 4DWM _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4DWM _atom_sites.fract_transf_matrix[1][1] 0.007681 _atom_sites.fract_transf_matrix[1][2] 0.004434 _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] 0.008869 _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] 0.024685 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 27.162 10.835 28.794 1.00 22.13 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 25.784 10.482 28.126 1.00 22.43 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 25.093 11.807 27.885 1.00 21.99 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 25.508 12.886 28.435 1.00 21.62 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 24.899 9.652 29.081 1.00 21.19 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 25.527 8.320 29.522 1.00 23.35 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 26.691 8.025 29.155 1.00 25.43 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 24.805 7.549 30.258 1.00 22.65 ? 1 ASP A OD2 1 ATOM 9 N N . VAL A 1 2 ? 24.034 11.811 27.062 1.00 17.99 ? 2 VAL A N 1 ATOM 10 C CA . VAL A 1 2 ? 23.189 12.994 26.983 1.00 17.46 ? 2 VAL A CA 1 ATOM 11 C C . VAL A 1 2 ? 21.719 12.585 27.145 1.00 17.75 ? 2 VAL A C 1 ATOM 12 O O . VAL A 1 2 ? 21.430 11.383 27.066 1.00 19.04 ? 2 VAL A O 1 ATOM 13 C CB . VAL A 1 2 ? 23.363 13.613 25.618 1.00 19.46 ? 2 VAL A CB 1 ATOM 14 C CG1 . VAL A 1 2 ? 24.829 14.168 25.428 1.00 20.68 ? 2 VAL A CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? 23.035 12.672 24.461 1.00 19.17 ? 2 VAL A CG2 1 ATOM 16 N N . SER A 1 3 ? 20.890 13.484 27.547 1.00 18.47 ? 3 SER A N 1 ATOM 17 C CA . SER A 1 3 ? 19.489 13.177 27.855 1.00 17.72 ? 3 SER A CA 1 ATOM 18 C C . SER A 1 3 ? 18.573 14.193 27.207 1.00 18.03 ? 3 SER A C 1 ATOM 19 O O . SER A 1 3 ? 18.924 15.348 26.905 1.00 19.15 ? 3 SER A O 1 ATOM 20 C CB . SER A 1 3 ? 19.257 13.237 29.380 1.00 20.35 ? 3 SER A CB 1 ATOM 21 O OG . SER A 1 3 ? 20.000 12.133 29.933 1.00 19.62 ? 3 SER A OG 1 ATOM 22 N N . PHE A 1 4 ? 17.348 13.742 26.920 1.00 16.89 ? 4 PHE A N 1 ATOM 23 C CA . PHE A 1 4 ? 16.309 14.670 26.433 1.00 15.50 ? 4 PHE A CA 1 ATOM 24 C C . PHE A 1 4 ? 14.933 14.194 26.960 1.00 17.31 ? 4 PHE A C 1 ATOM 25 O O . PHE A 1 4 ? 14.606 13.000 26.824 1.00 16.13 ? 4 PHE A O 1 ATOM 26 C CB . PHE A 1 4 ? 16.235 14.737 24.906 1.00 16.12 ? 4 PHE A CB 1 ATOM 27 C CG . PHE A 1 4 ? 15.172 15.756 24.374 1.00 15.98 ? 4 PHE A CG 1 ATOM 28 C CD1 . PHE A 1 4 ? 15.141 17.090 24.860 1.00 15.74 ? 4 PHE A CD1 1 ATOM 29 C CD2 . PHE A 1 4 ? 14.206 15.353 23.433 1.00 16.43 ? 4 PHE A CD2 1 ATOM 30 C CE1 . PHE A 1 4 ? 14.179 17.977 24.403 1.00 14.05 ? 4 PHE A CE1 1 ATOM 31 C CE2 . PHE A 1 4 ? 13.220 16.236 22.922 1.00 17.17 ? 4 PHE A CE2 1 ATOM 32 C CZ . PHE A 1 4 ? 13.249 17.597 23.394 1.00 18.53 ? 4 PHE A CZ 1 ATOM 33 N N . ARG A 1 5 ? 14.188 15.104 27.556 1.00 14.69 ? 5 ARG A N 1 ATOM 34 C CA . ARG A 1 5 ? 12.858 14.835 28.081 1.00 17.27 ? 5 ARG A CA 1 ATOM 35 C C . ARG A 1 5 ? 11.772 15.473 27.257 1.00 17.70 ? 5 ARG A C 1 ATOM 36 O O . ARG A 1 5 ? 11.771 16.715 27.028 1.00 16.71 ? 5 ARG A O 1 ATOM 37 C CB . ARG A 1 5 ? 12.809 15.366 29.538 1.00 19.27 ? 5 ARG A CB 1 ATOM 38 C CG . ARG A 1 5 ? 13.616 14.437 30.455 1.00 25.32 ? 5 ARG A CG 1 ATOM 39 C CD . ARG A 1 5 ? 13.914 14.941 31.818 1.00 32.10 ? 5 ARG A CD 1 ATOM 40 N NE . ARG A 1 5 ? 14.607 13.904 32.674 1.00 34.83 ? 5 ARG A NE 1 ATOM 41 C CZ . ARG A 1 5 ? 15.938 13.653 32.709 1.00 35.87 ? 5 ARG A CZ 1 ATOM 42 N NH1 . ARG A 1 5 ? 16.804 14.302 31.928 1.00 33.35 ? 5 ARG A NH1 1 ATOM 43 N NH2 . ARG A 1 5 ? 16.427 12.710 33.547 1.00 35.23 ? 5 ARG A NH2 1 ATOM 44 N N . LEU A 1 6 ? 10.763 14.691 26.809 1.00 15.98 ? 6 LEU A N 1 ATOM 45 C CA . LEU A 1 6 ? 9.677 15.291 26.108 1.00 15.77 ? 6 LEU A CA 1 ATOM 46 C C . LEU A 1 6 ? 8.694 16.056 27.041 1.00 17.06 ? 6 LEU A C 1 ATOM 47 O O . LEU A 1 6 ? 7.932 16.947 26.559 1.00 18.98 ? 6 LEU A O 1 ATOM 48 C CB . LEU A 1 6 ? 8.888 14.204 25.298 1.00 15.87 ? 6 LEU A CB 1 ATOM 49 C CG . LEU A 1 6 ? 9.469 13.958 23.911 1.00 18.77 ? 6 LEU A CG 1 ATOM 50 C CD1 . LEU A 1 6 ? 9.282 15.164 22.926 1.00 17.59 ? 6 LEU A CD1 1 ATOM 51 C CD2 . LEU A 1 6 ? 10.933 13.567 24.020 1.00 17.64 ? 6 LEU A CD2 1 ATOM 52 N N . SER A 1 7 ? 8.648 15.664 28.326 1.00 17.99 ? 7 SER A N 1 ATOM 53 C CA . SER A 1 7 ? 7.707 16.340 29.202 1.00 19.47 ? 7 SER A CA 1 ATOM 54 C C . SER A 1 7 ? 8.247 17.757 29.467 1.00 18.15 ? 7 SER A C 1 ATOM 55 O O . SER A 1 7 ? 9.359 17.948 29.996 1.00 19.88 ? 7 SER A O 1 ATOM 56 C CB . SER A 1 7 ? 7.583 15.558 30.525 1.00 20.57 ? 7 SER A CB 1 ATOM 57 O OG . SER A 1 7 ? 6.713 16.361 31.388 1.00 22.22 ? 7 SER A OG 1 ATOM 58 N N . GLY A 1 8 ? 7.454 18.750 29.052 1.00 19.06 ? 8 GLY A N 1 ATOM 59 C CA . GLY A 1 8 ? 7.845 20.168 29.179 1.00 19.64 ? 8 GLY A CA 1 ATOM 60 C C . GLY A 1 8 ? 8.787 20.594 28.055 1.00 18.98 ? 8 GLY A C 1 ATOM 61 O O . GLY A 1 8 ? 9.315 21.785 28.063 1.00 19.36 ? 8 GLY A O 1 ATOM 62 N N . ALA A 1 9 ? 8.990 19.745 27.052 1.00 17.17 ? 9 ALA A N 1 ATOM 63 C CA . ALA A 1 9 ? 9.957 20.139 25.999 1.00 17.44 ? 9 ALA A CA 1 ATOM 64 C C . ALA A 1 9 ? 9.467 21.328 25.209 1.00 17.07 ? 9 ALA A C 1 ATOM 65 O O . ALA A 1 9 ? 8.244 21.490 24.927 1.00 18.14 ? 9 ALA A O 1 ATOM 66 C CB . ALA A 1 9 ? 10.275 18.981 25.030 1.00 18.56 ? 9 ALA A CB 1 ATOM 67 N N . ASP A 1 10 ? 10.427 22.148 24.788 1.00 17.30 ? 10 ASP A N 1 ATOM 68 C CA . ASP A 1 10 ? 10.107 23.225 23.878 1.00 17.48 ? 10 ASP A CA 1 ATOM 69 C C . ASP A 1 10 ? 11.290 23.453 22.923 1.00 18.39 ? 10 ASP A C 1 ATOM 70 O O . ASP A 1 10 ? 12.292 22.780 23.044 1.00 18.49 ? 10 ASP A O 1 ATOM 71 C CB . ASP A 1 10 ? 9.735 24.505 24.698 1.00 18.07 ? 10 ASP A CB 1 ATOM 72 C CG . ASP A 1 10 ? 10.928 25.141 25.412 1.00 25.67 ? 10 ASP A CG 1 ATOM 73 O OD1 . ASP A 1 10 ? 12.032 24.551 25.582 1.00 21.63 ? 10 ASP A OD1 1 ATOM 74 O OD2 . ASP A 1 10 ? 10.665 26.284 25.897 1.00 30.92 ? 10 ASP A OD2 1 ATOM 75 N N . PRO A 1 11 ? 11.184 24.440 22.040 1.00 18.36 ? 11 PRO A N 1 ATOM 76 C CA . PRO A 1 11 ? 12.358 24.642 21.143 1.00 17.61 ? 11 PRO A CA 1 ATOM 77 C C . PRO A 1 11 ? 13.676 24.867 21.838 1.00 18.58 ? 11 PRO A C 1 ATOM 78 O O . PRO A 1 11 ? 14.731 24.398 21.353 1.00 18.30 ? 11 PRO A O 1 ATOM 79 C CB . PRO A 1 11 ? 11.959 25.845 20.312 1.00 17.75 ? 11 PRO A CB 1 ATOM 80 C CG . PRO A 1 11 ? 10.369 25.682 20.184 1.00 17.41 ? 11 PRO A CG 1 ATOM 81 C CD . PRO A 1 11 ? 9.985 25.205 21.605 1.00 18.54 ? 11 PRO A CD 1 ATOM 82 N N . SER A 1 12 ? 13.635 25.572 22.956 1.00 20.45 ? 12 SER A N 1 ATOM 83 C CA . SER A 1 12 ? 14.904 25.850 23.650 1.00 21.65 ? 12 SER A CA 1 ATOM 84 C C . SER A 1 12 ? 15.474 24.573 24.253 1.00 20.48 ? 12 SER A C 1 ATOM 85 O O . SER A 1 12 ? 16.682 24.329 24.127 1.00 18.94 ? 12 SER A O 1 ATOM 86 C CB . SER A 1 12 ? 14.656 26.927 24.750 1.00 22.31 ? 12 SER A CB 1 ATOM 87 O OG . SER A 1 12 ? 15.880 27.175 25.493 1.00 36.49 ? 12 SER A OG 1 ATOM 88 N N . SER A 1 13 ? 14.650 23.724 24.893 1.00 18.26 ? 13 SER A N 1 ATOM 89 C CA . SER A 1 13 ? 15.242 22.570 25.544 1.00 18.34 ? 13 SER A CA 1 ATOM 90 C C . SER A 1 13 ? 15.650 21.517 24.518 1.00 17.75 ? 13 SER A C 1 ATOM 91 O O . SER A 1 13 ? 16.634 20.748 24.762 1.00 17.59 ? 13 SER A O 1 ATOM 92 C CB . SER A 1 13 ? 14.288 21.946 26.573 1.00 19.18 ? 13 SER A CB 1 ATOM 93 O OG . SER A 1 13 ? 13.126 21.248 25.972 1.00 18.31 ? 13 SER A OG 1 ATOM 94 N N . TYR A 1 14 ? 14.941 21.511 23.373 1.00 14.99 ? 14 TYR A N 1 ATOM 95 C CA . TYR A 1 14 ? 15.417 20.614 22.314 1.00 15.03 ? 14 TYR A CA 1 ATOM 96 C C . TYR A 1 14 ? 16.742 21.130 21.779 1.00 16.18 ? 14 TYR A C 1 ATOM 97 O O . TYR A 1 14 ? 17.671 20.361 21.489 1.00 17.20 ? 14 TYR A O 1 ATOM 98 C CB . TYR A 1 14 ? 14.351 20.574 21.182 1.00 15.59 ? 14 TYR A CB 1 ATOM 99 C CG . TYR A 1 14 ? 14.786 19.780 19.958 1.00 14.87 ? 14 TYR A CG 1 ATOM 100 C CD1 . TYR A 1 14 ? 14.929 18.406 19.996 1.00 13.70 ? 14 TYR A CD1 1 ATOM 101 C CD2 . TYR A 1 14 ? 15.145 20.462 18.830 1.00 15.61 ? 14 TYR A CD2 1 ATOM 102 C CE1 . TYR A 1 14 ? 15.311 17.686 18.844 1.00 14.17 ? 14 TYR A CE1 1 ATOM 103 C CE2 . TYR A 1 14 ? 15.530 19.800 17.682 1.00 15.89 ? 14 TYR A CE2 1 ATOM 104 C CZ . TYR A 1 14 ? 15.620 18.382 17.680 1.00 14.37 ? 14 TYR A CZ 1 ATOM 105 O OH . TYR A 1 14 ? 16.013 17.732 16.526 1.00 14.81 ? 14 TYR A OH 1 ATOM 106 N N . GLY A 1 15 ? 16.847 22.439 21.554 1.00 16.51 ? 15 GLY A N 1 ATOM 107 C CA . GLY A 1 15 ? 18.160 22.936 21.048 1.00 16.77 ? 15 GLY A CA 1 ATOM 108 C C . GLY A 1 15 ? 19.274 22.685 22.054 1.00 18.95 ? 15 GLY A C 1 ATOM 109 O O . GLY A 1 15 ? 20.399 22.360 21.586 1.00 18.71 ? 15 GLY A O 1 ATOM 110 N N . MET A 1 16 ? 18.990 22.748 23.363 1.00 18.06 ? 16 MET A N 1 ATOM 111 C CA . MET A 1 16 ? 19.995 22.377 24.385 1.00 19.17 ? 16 MET A CA 1 ATOM 112 C C . MET A 1 16 ? 20.432 20.899 24.202 1.00 19.01 ? 16 MET A C 1 ATOM 113 O O . MET A 1 16 ? 21.628 20.551 24.322 1.00 19.31 ? 16 MET A O 1 ATOM 114 C CB . MET A 1 16 ? 19.586 22.647 25.856 1.00 21.21 ? 16 MET A CB 1 ATOM 115 C CG . MET A 1 16 ? 19.210 24.073 26.038 1.00 23.92 ? 16 MET A CG 1 ATOM 116 S SD . MET A 1 16 ? 18.842 24.334 27.791 1.00 37.97 ? 16 MET A SD 1 ATOM 117 C CE . MET A 1 16 ? 17.254 23.562 28.092 1.00 35.07 ? 16 MET A CE 1 ATOM 118 N N . PHE A 1 17 ? 19.463 20.012 23.904 1.00 17.20 ? 17 PHE A N 1 ATOM 119 C CA . PHE A 1 17 ? 19.793 18.620 23.766 1.00 16.12 ? 17 PHE A CA 1 ATOM 120 C C . PHE A 1 17 ? 20.691 18.433 22.515 1.00 14.90 ? 17 PHE A C 1 ATOM 121 O O . PHE A 1 17 ? 21.642 17.652 22.575 1.00 17.47 ? 17 PHE A O 1 ATOM 122 C CB . PHE A 1 17 ? 18.468 17.807 23.653 1.00 16.70 ? 17 PHE A CB 1 ATOM 123 C CG . PHE A 1 17 ? 18.610 16.437 22.956 1.00 16.69 ? 17 PHE A CG 1 ATOM 124 C CD1 . PHE A 1 17 ? 19.440 15.465 23.454 1.00 16.56 ? 17 PHE A CD1 1 ATOM 125 C CD2 . PHE A 1 17 ? 17.885 16.193 21.799 1.00 16.22 ? 17 PHE A CD2 1 ATOM 126 C CE1 . PHE A 1 17 ? 19.558 14.202 22.847 1.00 15.23 ? 17 PHE A CE1 1 ATOM 127 C CE2 . PHE A 1 17 ? 17.981 14.955 21.156 1.00 18.88 ? 17 PHE A CE2 1 ATOM 128 C CZ . PHE A 1 17 ? 18.836 13.951 21.708 1.00 16.89 ? 17 PHE A CZ 1 ATOM 129 N N . ILE A 1 18 ? 20.333 19.088 21.376 1.00 14.85 ? 18 ILE A N 1 ATOM 130 C CA . ILE A 1 18 ? 21.062 18.867 20.164 1.00 15.83 ? 18 ILE A CA 1 ATOM 131 C C . ILE A 1 18 ? 22.482 19.453 20.365 1.00 16.13 ? 18 ILE A C 1 ATOM 132 O O . ILE A 1 18 ? 23.469 18.838 19.899 1.00 18.30 ? 18 ILE A O 1 ATOM 133 C CB . ILE A 1 18 ? 20.340 19.468 18.934 1.00 16.24 ? 18 ILE A CB 1 ATOM 134 C CG1 . ILE A 1 18 ? 19.021 18.728 18.645 1.00 16.24 ? 18 ILE A CG1 1 ATOM 135 C CG2 . ILE A 1 18 ? 21.293 19.494 17.736 1.00 17.59 ? 18 ILE A CG2 1 ATOM 136 C CD1 . ILE A 1 18 ? 19.223 17.164 18.398 1.00 17.12 ? 18 ILE A CD1 1 ATOM 137 N N . LYS A 1 19 ? 22.568 20.603 21.034 1.00 16.29 ? 19 LYS A N 1 ATOM 138 C CA . LYS A 1 19 ? 23.921 21.065 21.436 1.00 18.86 ? 19 LYS A CA 1 ATOM 139 C C . LYS A 1 19 ? 24.728 20.087 22.282 1.00 18.95 ? 19 LYS A C 1 ATOM 140 O O . LYS A 1 19 ? 25.916 19.857 21.964 1.00 18.74 ? 19 LYS A O 1 ATOM 141 C CB . LYS A 1 19 ? 23.735 22.403 22.199 1.00 21.35 ? 19 LYS A CB 1 ATOM 142 C CG . LYS A 1 19 ? 25.110 22.996 22.683 1.00 25.46 ? 19 LYS A CG 1 ATOM 143 C CD . LYS A 1 19 ? 24.748 24.145 23.658 1.00 32.68 ? 19 LYS A CD 1 ATOM 144 C CE . LYS A 1 19 ? 24.802 25.525 22.961 1.00 48.38 ? 19 LYS A CE 1 ATOM 145 N NZ . LYS A 1 19 ? 24.311 26.735 23.805 1.00 52.82 ? 19 LYS A NZ 1 ATOM 146 N N . ASP A 1 20 ? 24.099 19.441 23.254 1.00 17.23 ? 20 ASP A N 1 ATOM 147 C CA . ASP A 1 20 ? 24.784 18.449 24.112 1.00 20.30 ? 20 ASP A CA 1 ATOM 148 C C . ASP A 1 20 ? 25.213 17.233 23.265 1.00 17.54 ? 20 ASP A C 1 ATOM 149 O O . ASP A 1 20 ? 26.297 16.622 23.469 1.00 18.11 ? 20 ASP A O 1 ATOM 150 C CB . ASP A 1 20 ? 23.830 17.921 25.166 1.00 19.44 ? 20 ASP A CB 1 ATOM 151 C CG . ASP A 1 20 ? 23.463 18.940 26.252 1.00 22.70 ? 20 ASP A CG 1 ATOM 152 O OD1 . ASP A 1 20 ? 24.156 19.987 26.403 1.00 24.48 ? 20 ASP A OD1 1 ATOM 153 O OD2 . ASP A 1 20 ? 22.465 18.656 26.941 1.00 24.64 ? 20 ASP A OD2 1 ATOM 154 N N . LEU A 1 21 ? 24.335 16.863 22.304 1.00 17.81 ? 21 LEU A N 1 ATOM 155 C CA . LEU A 1 21 ? 24.607 15.708 21.470 1.00 16.82 ? 21 LEU A CA 1 ATOM 156 C C . LEU A 1 21 ? 25.857 16.022 20.598 1.00 18.10 ? 21 LEU A C 1 ATOM 157 O O . LEU A 1 21 ? 26.824 15.233 20.593 1.00 18.17 ? 21 LEU A O 1 ATOM 158 C CB . LEU A 1 21 ? 23.334 15.386 20.600 1.00 15.17 ? 21 LEU A CB 1 ATOM 159 C CG . LEU A 1 21 ? 23.495 14.254 19.541 1.00 20.43 ? 21 LEU A CG 1 ATOM 160 C CD1 . LEU A 1 21 ? 24.195 12.997 19.914 1.00 22.51 ? 21 LEU A CD1 1 ATOM 161 C CD2 . LEU A 1 21 ? 22.079 14.045 18.979 1.00 16.15 ? 21 LEU A CD2 1 ATOM 162 N N . ARG A 1 22 ? 25.860 17.204 19.971 1.00 17.26 ? 22 ARG A N 1 ATOM 163 C CA . ARG A 1 22 ? 27.042 17.558 19.161 1.00 17.13 ? 22 ARG A CA 1 ATOM 164 C C . ARG A 1 22 ? 28.288 17.585 20.062 1.00 18.88 ? 22 ARG A C 1 ATOM 165 O O . ARG A 1 22 ? 29.386 17.165 19.641 1.00 21.03 ? 22 ARG A O 1 ATOM 166 C CB . ARG A 1 22 ? 26.841 18.967 18.605 1.00 18.52 ? 22 ARG A CB 1 ATOM 167 C CG . ARG A 1 22 ? 25.856 19.041 17.483 1.00 17.52 ? 22 ARG A CG 1 ATOM 168 C CD . ARG A 1 22 ? 25.462 20.454 17.108 1.00 18.26 ? 22 ARG A CD 1 ATOM 169 N NE . ARG A 1 22 ? 24.510 20.497 16.019 1.00 16.92 ? 22 ARG A NE 1 ATOM 170 C CZ . ARG A 1 22 ? 23.540 21.407 15.954 1.00 15.54 ? 22 ARG A CZ 1 ATOM 171 N NH1 . ARG A 1 22 ? 23.505 22.423 16.888 1.00 18.87 ? 22 ARG A NH1 1 ATOM 172 N NH2 . ARG A 1 22 ? 22.604 21.381 15.006 1.00 15.76 ? 22 ARG A NH2 1 ATOM 173 N N . ASN A 1 23 ? 28.127 18.130 21.254 1.00 18.91 ? 23 ASN A N 1 ATOM 174 C CA . ASN A 1 23 ? 29.334 18.341 22.167 1.00 22.06 ? 23 ASN A CA 1 ATOM 175 C C . ASN A 1 23 ? 29.845 17.060 22.727 1.00 23.32 ? 23 ASN A C 1 ATOM 176 O O . ASN A 1 23 ? 30.978 16.972 23.280 1.00 25.01 ? 23 ASN A O 1 ATOM 177 C CB . ASN A 1 23 ? 29.001 19.344 23.299 1.00 22.09 ? 23 ASN A CB 1 ATOM 178 C CG . ASN A 1 23 ? 28.980 20.830 22.840 1.00 27.35 ? 23 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 23 ? 28.367 21.655 23.506 1.00 33.50 ? 23 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 23 ? 29.562 21.150 21.709 1.00 28.20 ? 23 ASN A ND2 1 ATOM 181 N N . ALA A 1 24 ? 29.031 15.981 22.640 1.00 20.99 ? 24 ALA A N 1 ATOM 182 C CA . ALA A 1 24 ? 29.428 14.703 23.261 1.00 20.02 ? 24 ALA A CA 1 ATOM 183 C C . ALA A 1 24 ? 30.295 13.944 22.227 1.00 21.21 ? 24 ALA A C 1 ATOM 184 O O . ALA A 1 24 ? 30.807 12.855 22.532 1.00 23.32 ? 24 ALA A O 1 ATOM 185 C CB . ALA A 1 24 ? 28.224 13.876 23.610 1.00 20.06 ? 24 ALA A CB 1 ATOM 186 N N . LEU A 1 25 ? 30.358 14.411 20.947 1.00 20.26 ? 25 LEU A N 1 ATOM 187 C CA . LEU A 1 25 ? 31.072 13.657 19.901 1.00 20.22 ? 25 LEU A CA 1 ATOM 188 C C . LEU A 1 25 ? 32.534 14.143 19.834 1.00 22.12 ? 25 LEU A C 1 ATOM 189 O O . LEU A 1 25 ? 32.763 15.336 19.766 1.00 23.62 ? 25 LEU A O 1 ATOM 190 C CB . LEU A 1 25 ? 30.446 13.914 18.523 1.00 20.53 ? 25 LEU A CB 1 ATOM 191 C CG . LEU A 1 25 ? 28.930 13.550 18.559 1.00 19.54 ? 25 LEU A CG 1 ATOM 192 C CD1 . LEU A 1 25 ? 28.286 13.939 17.221 1.00 25.34 ? 25 LEU A CD1 1 ATOM 193 C CD2 . LEU A 1 25 ? 28.619 12.082 18.861 1.00 22.79 ? 25 LEU A CD2 1 ATOM 194 N N . PRO A 1 26 ? 33.464 13.230 19.974 1.00 22.58 ? 26 PRO A N 1 ATOM 195 C CA . PRO A 1 26 ? 34.836 13.782 20.041 1.00 24.04 ? 26 PRO A CA 1 ATOM 196 C C . PRO A 1 26 ? 35.438 14.102 18.683 1.00 24.40 ? 26 PRO A C 1 ATOM 197 O O . PRO A 1 26 ? 35.049 13.575 17.648 1.00 24.50 ? 26 PRO A O 1 ATOM 198 C CB . PRO A 1 26 ? 35.619 12.653 20.725 1.00 25.09 ? 26 PRO A CB 1 ATOM 199 C CG . PRO A 1 26 ? 34.889 11.359 20.162 1.00 25.69 ? 26 PRO A CG 1 ATOM 200 C CD . PRO A 1 26 ? 33.414 11.763 20.148 1.00 21.59 ? 26 PRO A CD 1 ATOM 201 N N . HIS A 1 27 ? 36.430 15.018 18.704 1.00 23.93 ? 27 HIS A N 1 ATOM 202 C CA . HIS A 1 27 ? 37.041 15.532 17.468 1.00 26.08 ? 27 HIS A CA 1 ATOM 203 C C . HIS A 1 27 ? 38.378 16.133 17.940 1.00 25.35 ? 27 HIS A C 1 ATOM 204 O O . HIS A 1 27 ? 38.499 16.583 19.114 1.00 25.30 ? 27 HIS A O 1 ATOM 205 C CB . HIS A 1 27 ? 36.174 16.604 16.742 1.00 25.84 ? 27 HIS A CB 1 ATOM 206 C CG . HIS A 1 27 ? 36.055 17.956 17.410 1.00 28.49 ? 27 HIS A CG 1 ATOM 207 N ND1 . HIS A 1 27 ? 35.057 18.287 18.337 1.00 32.99 ? 27 HIS A ND1 1 ATOM 208 C CD2 . HIS A 1 27 ? 36.783 19.110 17.211 1.00 28.03 ? 27 HIS A CD2 1 ATOM 209 C CE1 . HIS A 1 27 ? 35.208 19.567 18.706 1.00 36.11 ? 27 HIS A CE1 1 ATOM 210 N NE2 . HIS A 1 27 ? 36.244 20.091 18.030 1.00 33.02 ? 27 HIS A NE2 1 ATOM 211 N N . THR A 1 28 ? 39.355 16.022 17.070 1.00 27.64 ? 28 THR A N 1 ATOM 212 C CA . THR A 1 28 ? 40.650 16.630 17.380 1.00 29.51 ? 28 THR A CA 1 ATOM 213 C C . THR A 1 28 ? 40.927 17.804 16.509 1.00 30.46 ? 28 THR A C 1 ATOM 214 O O . THR A 1 28 ? 41.797 18.592 16.877 1.00 31.20 ? 28 THR A O 1 ATOM 215 C CB . THR A 1 28 ? 41.809 15.678 17.132 1.00 31.12 ? 28 THR A CB 1 ATOM 216 O OG1 . THR A 1 28 ? 41.726 15.216 15.792 1.00 39.45 ? 28 THR A OG1 1 ATOM 217 C CG2 . THR A 1 28 ? 41.866 14.467 18.071 1.00 34.23 ? 28 THR A CG2 1 ATOM 218 N N . GLU A 1 29 ? 40.276 17.897 15.333 1.00 27.41 ? 29 GLU A N 1 ATOM 219 C CA . GLU A 1 29 ? 40.546 18.915 14.312 1.00 28.78 ? 29 GLU A CA 1 ATOM 220 C C . GLU A 1 29 ? 39.170 19.448 13.822 1.00 28.06 ? 29 GLU A C 1 ATOM 221 O O . GLU A 1 29 ? 38.119 18.716 13.896 1.00 25.42 ? 29 GLU A O 1 ATOM 222 C CB . GLU A 1 29 ? 41.257 18.138 13.207 1.00 29.01 ? 29 GLU A CB 1 ATOM 223 C CG . GLU A 1 29 ? 41.987 18.783 12.114 1.00 41.94 ? 29 GLU A CG 1 ATOM 224 C CD . GLU A 1 29 ? 42.465 17.687 11.138 1.00 47.98 ? 29 GLU A CD 1 ATOM 225 O OE1 . GLU A 1 29 ? 42.761 16.540 11.652 1.00 47.56 ? 29 GLU A OE1 1 ATOM 226 O OE2 . GLU A 1 29 ? 42.459 17.946 9.889 1.00 50.53 ? 29 GLU A OE2 1 ATOM 227 N N . LYS A 1 30 ? 39.164 20.694 13.355 1.00 25.47 ? 30 LYS A N 1 ATOM 228 C CA . LYS A 1 30 ? 38.012 21.291 12.633 1.00 25.82 ? 30 LYS A CA 1 ATOM 229 C C . LYS A 1 30 ? 38.498 21.542 11.207 1.00 27.16 ? 30 LYS A C 1 ATOM 230 O O . LYS A 1 30 ? 39.731 21.907 10.992 1.00 28.69 ? 30 LYS A O 1 ATOM 231 C CB . LYS A 1 30 ? 37.542 22.609 13.253 1.00 25.28 ? 30 LYS A CB 1 ATOM 232 C CG . LYS A 1 30 ? 37.110 22.461 14.697 1.00 26.93 ? 30 LYS A CG 1 ATOM 233 C CD . LYS A 1 30 ? 36.467 23.723 15.168 1.00 32.08 ? 30 LYS A CD 1 ATOM 234 C CE . LYS A 1 30 ? 35.901 23.549 16.496 1.00 32.64 ? 30 LYS A CE 1 ATOM 235 N NZ . LYS A 1 30 ? 35.453 24.921 17.073 1.00 35.32 ? 30 LYS A NZ 1 ATOM 236 N N . VAL A 1 31 ? 37.642 21.333 10.221 1.00 23.83 ? 31 VAL A N 1 ATOM 237 C CA . VAL A 1 31 ? 37.930 21.590 8.824 1.00 22.97 ? 31 VAL A CA 1 ATOM 238 C C . VAL A 1 31 ? 36.953 22.686 8.402 1.00 24.03 ? 31 VAL A C 1 ATOM 239 O O . VAL A 1 31 ? 35.740 22.538 8.569 1.00 21.02 ? 31 VAL A O 1 ATOM 240 C CB . VAL A 1 31 ? 37.832 20.307 7.977 1.00 22.42 ? 31 VAL A CB 1 ATOM 241 C CG1 . VAL A 1 31 ? 37.994 20.602 6.546 1.00 22.22 ? 31 VAL A CG1 1 ATOM 242 C CG2 . VAL A 1 31 ? 38.834 19.205 8.534 1.00 24.51 ? 31 VAL A CG2 1 ATOM 243 N N . TYR A 1 32 ? 37.461 23.836 7.952 1.00 22.11 ? 32 TYR A N 1 ATOM 244 C CA . TYR A 1 32 ? 36.638 24.983 7.652 1.00 22.41 ? 32 TYR A CA 1 ATOM 245 C C . TYR A 1 32 ? 35.713 25.295 8.858 1.00 24.28 ? 32 TYR A C 1 ATOM 246 O O . TYR A 1 32 ? 34.520 25.651 8.633 1.00 24.34 ? 32 TYR A O 1 ATOM 247 C CB . TYR A 1 32 ? 35.922 24.784 6.328 1.00 21.52 ? 32 TYR A CB 1 ATOM 248 C CG . TYR A 1 32 ? 36.887 24.759 5.201 1.00 20.88 ? 32 TYR A CG 1 ATOM 249 C CD1 . TYR A 1 32 ? 37.491 25.972 4.774 1.00 25.53 ? 32 TYR A CD1 1 ATOM 250 C CD2 . TYR A 1 32 ? 37.214 23.594 4.525 1.00 21.91 ? 32 TYR A CD2 1 ATOM 251 C CE1 . TYR A 1 32 ? 38.354 25.977 3.712 1.00 22.58 ? 32 TYR A CE1 1 ATOM 252 C CE2 . TYR A 1 32 ? 38.160 23.619 3.473 1.00 28.16 ? 32 TYR A CE2 1 ATOM 253 C CZ . TYR A 1 32 ? 38.739 24.813 3.143 1.00 24.28 ? 32 TYR A CZ 1 ATOM 254 O OH . TYR A 1 32 ? 39.629 24.928 2.077 1.00 26.02 ? 32 TYR A OH 1 ATOM 255 N N . ASN A 1 33 ? 36.290 25.156 10.083 1.00 22.19 ? 33 ASN A N 1 ATOM 256 C CA . ASN A 1 33 ? 35.633 25.513 11.357 1.00 22.87 ? 33 ASN A CA 1 ATOM 257 C C . ASN A 1 33 ? 34.440 24.538 11.692 1.00 22.44 ? 33 ASN A C 1 ATOM 258 O O . ASN A 1 33 ? 33.742 24.770 12.666 1.00 22.61 ? 33 ASN A O 1 ATOM 259 C CB . ASN A 1 33 ? 35.099 26.941 11.336 1.00 24.61 ? 33 ASN A CB 1 ATOM 260 C CG . ASN A 1 33 ? 34.988 27.537 12.715 1.00 30.54 ? 33 ASN A CG 1 ATOM 261 O OD1 . ASN A 1 33 ? 35.805 27.269 13.603 1.00 36.06 ? 33 ASN A OD1 1 ATOM 262 N ND2 . ASN A 1 33 ? 33.913 28.261 12.936 1.00 37.03 ? 33 ASN A ND2 1 ATOM 263 N N . ILE A 1 34 ? 34.409 23.400 11.003 1.00 20.07 ? 34 ILE A N 1 ATOM 264 C CA . ILE A 1 34 ? 33.368 22.371 11.346 1.00 19.13 ? 34 ILE A CA 1 ATOM 265 C C . ILE A 1 34 ? 34.125 21.201 12.037 1.00 19.08 ? 34 ILE A C 1 ATOM 266 O O . ILE A 1 34 ? 35.063 20.632 11.427 1.00 21.51 ? 34 ILE A O 1 ATOM 267 C CB . ILE A 1 34 ? 32.729 21.861 10.062 1.00 17.64 ? 34 ILE A CB 1 ATOM 268 C CG1 . ILE A 1 34 ? 32.120 23.003 9.292 1.00 18.80 ? 34 ILE A CG1 1 ATOM 269 C CG2 . ILE A 1 34 ? 31.610 20.800 10.454 1.00 18.30 ? 34 ILE A CG2 1 ATOM 270 C CD1 . ILE A 1 34 ? 32.110 22.823 7.833 1.00 19.24 ? 34 ILE A CD1 1 ATOM 271 N N . PRO A 1 35 ? 33.694 20.742 13.244 1.00 19.56 ? 35 PRO A N 1 ATOM 272 C CA . PRO A 1 35 ? 34.276 19.577 13.808 1.00 20.28 ? 35 PRO A CA 1 ATOM 273 C C . PRO A 1 35 ? 34.388 18.343 12.892 1.00 20.10 ? 35 PRO A C 1 ATOM 274 O O . PRO A 1 35 ? 33.426 17.986 12.206 1.00 19.31 ? 35 PRO A O 1 ATOM 275 C CB . PRO A 1 35 ? 33.342 19.249 14.960 1.00 21.12 ? 35 PRO A CB 1 ATOM 276 C CG . PRO A 1 35 ? 32.878 20.552 15.412 1.00 19.75 ? 35 PRO A CG 1 ATOM 277 C CD . PRO A 1 35 ? 32.606 21.271 14.097 1.00 19.57 ? 35 PRO A CD 1 ATOM 278 N N . LEU A 1 36 ? 35.572 17.696 12.864 1.00 18.90 ? 36 LEU A N 1 ATOM 279 C CA . LEU A 1 36 ? 35.778 16.558 11.993 1.00 18.69 ? 36 LEU A CA 1 ATOM 280 C C . LEU A 1 36 ? 35.704 15.294 12.866 1.00 18.71 ? 36 LEU A C 1 ATOM 281 O O . LEU A 1 36 ? 36.554 15.079 13.805 1.00 21.25 ? 36 LEU A O 1 ATOM 282 C CB . LEU A 1 36 ? 37.241 16.591 11.342 1.00 19.55 ? 36 LEU A CB 1 ATOM 283 C CG . LEU A 1 36 ? 37.606 15.351 10.587 1.00 19.27 ? 36 LEU A CG 1 ATOM 284 C CD1 . LEU A 1 36 ? 36.741 15.130 9.350 1.00 19.40 ? 36 LEU A CD1 1 ATOM 285 C CD2 . LEU A 1 36 ? 39.143 15.516 10.221 1.00 21.51 ? 36 LEU A CD2 1 ATOM 286 N N . LEU A 1 37 ? 34.679 14.471 12.684 1.00 18.30 ? 37 LEU A N 1 ATOM 287 C CA . LEU A 1 37 ? 34.604 13.266 13.535 1.00 19.02 ? 37 LEU A CA 1 ATOM 288 C C . LEU A 1 37 ? 35.866 12.356 13.344 1.00 21.37 ? 37 LEU A C 1 ATOM 289 O O . LEU A 1 37 ? 36.504 12.385 12.256 1.00 21.48 ? 37 LEU A O 1 ATOM 290 C CB . LEU A 1 37 ? 33.314 12.418 13.251 1.00 17.59 ? 37 LEU A CB 1 ATOM 291 C CG . LEU A 1 37 ? 32.088 13.366 13.470 1.00 20.03 ? 37 LEU A CG 1 ATOM 292 C CD1 . LEU A 1 37 ? 30.839 12.600 12.817 1.00 20.79 ? 37 LEU A CD1 1 ATOM 293 C CD2 . LEU A 1 37 ? 31.942 13.628 14.949 1.00 21.08 ? 37 LEU A CD2 1 ATOM 294 N N . LEU A 1 38 ? 36.145 11.542 14.369 1.00 23.24 ? 38 LEU A N 1 ATOM 295 C CA . LEU A 1 38 ? 37.357 10.698 14.364 1.00 23.05 ? 38 LEU A CA 1 ATOM 296 C C . LEU A 1 38 ? 37.281 9.556 13.378 1.00 26.19 ? 38 LEU A C 1 ATOM 297 O O . LEU A 1 38 ? 36.167 9.063 13.039 1.00 23.98 ? 38 LEU A O 1 ATOM 298 C CB . LEU A 1 38 ? 37.665 10.174 15.744 1.00 22.08 ? 38 LEU A CB 1 ATOM 299 C CG . LEU A 1 38 ? 37.864 11.211 16.812 1.00 24.62 ? 38 LEU A CG 1 ATOM 300 C CD1 . LEU A 1 38 ? 38.080 10.506 18.144 1.00 28.53 ? 38 LEU A CD1 1 ATOM 301 C CD2 . LEU A 1 38 ? 39.027 12.223 16.392 1.00 28.80 ? 38 LEU A CD2 1 ATOM 302 N N . PRO A 1 39 ? 38.432 9.100 12.855 1.00 26.37 ? 39 PRO A N 1 ATOM 303 C CA . PRO A 1 39 ? 38.431 7.946 11.955 1.00 27.45 ? 39 PRO A CA 1 ATOM 304 C C . PRO A 1 39 ? 37.885 6.692 12.674 1.00 26.98 ? 39 PRO A C 1 ATOM 305 O O . PRO A 1 39 ? 37.126 5.939 12.123 1.00 28.60 ? 39 PRO A O 1 ATOM 306 C CB . PRO A 1 39 ? 39.958 7.695 11.697 1.00 28.71 ? 39 PRO A CB 1 ATOM 307 C CG . PRO A 1 39 ? 40.581 8.964 11.948 1.00 28.10 ? 39 PRO A CG 1 ATOM 308 C CD . PRO A 1 39 ? 39.783 9.732 12.966 1.00 27.83 ? 39 PRO A CD 1 ATOM 309 N N . SER A 1 40 ? 38.247 6.527 13.920 1.00 27.68 ? 40 SER A N 1 ATOM 310 C CA . SER A 1 40 ? 37.815 5.350 14.663 1.00 28.50 ? 40 SER A CA 1 ATOM 311 C C . SER A 1 40 ? 38.056 5.584 16.139 1.00 27.23 ? 40 SER A C 1 ATOM 312 O O . SER A 1 40 ? 38.817 6.477 16.522 1.00 29.32 ? 40 SER A O 1 ATOM 313 C CB . SER A 1 40 ? 38.580 4.105 14.159 1.00 31.59 ? 40 SER A CB 1 ATOM 314 O OG . SER A 1 40 ? 39.907 4.386 14.469 1.00 38.12 ? 40 SER A OG 1 ATOM 315 N N . VAL A 1 41 ? 37.378 4.795 16.976 1.00 27.53 ? 41 VAL A N 1 ATOM 316 C CA . VAL A 1 41 ? 37.502 4.893 18.428 1.00 28.82 ? 41 VAL A CA 1 ATOM 317 C C . VAL A 1 41 ? 37.401 3.439 18.875 1.00 31.66 ? 41 VAL A C 1 ATOM 318 O O . VAL A 1 41 ? 36.551 2.715 18.355 1.00 32.61 ? 41 VAL A O 1 ATOM 319 C CB . VAL A 1 41 ? 36.375 5.711 19.134 1.00 29.09 ? 41 VAL A CB 1 ATOM 320 C CG1 . VAL A 1 41 ? 36.511 5.620 20.663 1.00 25.77 ? 41 VAL A CG1 1 ATOM 321 C CG2 . VAL A 1 41 ? 36.332 7.207 18.676 1.00 24.53 ? 41 VAL A CG2 1 ATOM 322 N N . SER A 1 42 ? 38.295 3.011 19.789 1.00 33.28 ? 42 SER A N 1 ATOM 323 C CA . SER A 1 42 ? 38.317 1.599 20.218 1.00 35.99 ? 42 SER A CA 1 ATOM 324 C C . SER A 1 42 ? 37.545 1.337 21.461 1.00 34.95 ? 42 SER A C 1 ATOM 325 O O . SER A 1 42 ? 37.570 2.143 22.396 1.00 34.33 ? 42 SER A O 1 ATOM 326 C CB . SER A 1 42 ? 39.750 1.076 20.410 1.00 36.97 ? 42 SER A CB 1 ATOM 327 O OG . SER A 1 42 ? 39.971 0.245 19.299 1.00 44.94 ? 42 SER A OG 1 ATOM 328 N N . GLY A 1 43 ? 36.903 0.172 21.475 1.00 33.38 ? 43 GLY A N 1 ATOM 329 C CA . GLY A 1 43 ? 36.207 -0.285 22.679 1.00 33.40 ? 43 GLY A CA 1 ATOM 330 C C . GLY A 1 43 ? 34.893 0.410 22.954 1.00 31.63 ? 43 GLY A C 1 ATOM 331 O O . GLY A 1 43 ? 34.254 0.959 22.028 1.00 31.65 ? 43 GLY A O 1 ATOM 332 N N . ALA A 1 44 ? 34.526 0.445 24.206 1.00 31.17 ? 44 ALA A N 1 ATOM 333 C CA . ALA A 1 44 ? 33.269 1.029 24.568 1.00 30.05 ? 44 ALA A CA 1 ATOM 334 C C . ALA A 1 44 ? 33.148 2.523 24.241 1.00 29.71 ? 44 ALA A C 1 ATOM 335 O O . ALA A 1 44 ? 31.997 3.027 24.165 1.00 27.65 ? 44 ALA A O 1 ATOM 336 C CB . ALA A 1 44 ? 32.973 0.823 26.009 1.00 31.71 ? 44 ALA A CB 1 ATOM 337 N N . GLY A 1 45 ? 34.281 3.248 24.097 1.00 28.30 ? 45 GLY A N 1 ATOM 338 C CA . GLY A 1 45 ? 34.171 4.714 23.973 1.00 26.88 ? 45 GLY A CA 1 ATOM 339 C C . GLY A 1 45 ? 33.689 5.138 22.593 1.00 26.35 ? 45 GLY A C 1 ATOM 340 O O . GLY A 1 45 ? 33.464 6.340 22.348 1.00 26.21 ? 45 GLY A O 1 ATOM 341 N N . ARG A 1 46 ? 33.553 4.161 21.687 1.00 23.53 ? 46 ARG A N 1 ATOM 342 C CA . ARG A 1 46 ? 32.952 4.392 20.400 1.00 20.94 ? 46 ARG A CA 1 ATOM 343 C C . ARG A 1 46 ? 31.485 4.764 20.544 1.00 20.69 ? 46 ARG A C 1 ATOM 344 O O . ARG A 1 46 ? 30.913 5.383 19.612 1.00 20.79 ? 46 ARG A O 1 ATOM 345 C CB . ARG A 1 46 ? 33.067 3.157 19.525 1.00 22.06 ? 46 ARG A CB 1 ATOM 346 C CG . ARG A 1 46 ? 32.514 3.239 18.189 1.00 23.45 ? 46 ARG A CG 1 ATOM 347 C CD . ARG A 1 46 ? 32.857 1.965 17.426 1.00 30.35 ? 46 ARG A CD 1 ATOM 348 N NE . ARG A 1 46 ? 32.944 2.358 16.059 1.00 42.40 ? 46 ARG A NE 1 ATOM 349 C CZ . ARG A 1 46 ? 33.983 2.731 15.292 1.00 37.04 ? 46 ARG A CZ 1 ATOM 350 N NH1 . ARG A 1 46 ? 35.375 2.581 15.468 1.00 33.60 ? 46 ARG A NH1 1 ATOM 351 N NH2 . ARG A 1 46 ? 33.540 3.160 14.136 1.00 36.68 ? 46 ARG A NH2 1 ATOM 352 N N . TYR A 1 47 ? 30.843 4.435 21.655 1.00 21.23 ? 47 TYR A N 1 ATOM 353 C CA . TYR A 1 47 ? 29.337 4.581 21.693 1.00 18.73 ? 47 TYR A CA 1 ATOM 354 C C . TYR A 1 47 ? 28.905 5.609 22.697 1.00 21.28 ? 47 TYR A C 1 ATOM 355 O O . TYR A 1 47 ? 29.303 5.543 23.848 1.00 26.43 ? 47 TYR A O 1 ATOM 356 C CB . TYR A 1 47 ? 28.657 3.214 21.969 1.00 18.60 ? 47 TYR A CB 1 ATOM 357 C CG . TYR A 1 47 ? 29.176 2.203 21.024 1.00 17.52 ? 47 TYR A CG 1 ATOM 358 C CD1 . TYR A 1 47 ? 28.839 2.217 19.671 1.00 18.88 ? 47 TYR A CD1 1 ATOM 359 C CD2 . TYR A 1 47 ? 30.100 1.242 21.482 1.00 21.91 ? 47 TYR A CD2 1 ATOM 360 C CE1 . TYR A 1 47 ? 29.389 1.307 18.808 1.00 19.69 ? 47 TYR A CE1 1 ATOM 361 C CE2 . TYR A 1 47 ? 30.624 0.322 20.630 1.00 20.32 ? 47 TYR A CE2 1 ATOM 362 C CZ . TYR A 1 47 ? 30.317 0.342 19.322 1.00 20.49 ? 47 TYR A CZ 1 ATOM 363 O OH . TYR A 1 47 ? 30.864 -0.609 18.487 1.00 21.98 ? 47 TYR A OH 1 ATOM 364 N N . LEU A 1 48 ? 28.082 6.561 22.249 1.00 18.61 ? 48 LEU A N 1 ATOM 365 C CA . LEU A 1 48 ? 27.431 7.524 23.125 1.00 19.64 ? 48 LEU A CA 1 ATOM 366 C C . LEU A 1 48 ? 26.040 6.983 23.506 1.00 19.87 ? 48 LEU A C 1 ATOM 367 O O . LEU A 1 48 ? 25.342 6.454 22.641 1.00 20.01 ? 48 LEU A O 1 ATOM 368 C CB . LEU A 1 48 ? 27.262 8.910 22.385 1.00 18.87 ? 48 LEU A CB 1 ATOM 369 C CG . LEU A 1 48 ? 26.298 9.928 23.022 1.00 20.38 ? 48 LEU A CG 1 ATOM 370 C CD1 . LEU A 1 48 ? 26.891 10.449 24.313 1.00 24.61 ? 48 LEU A CD1 1 ATOM 371 C CD2 . LEU A 1 48 ? 26.142 11.057 22.015 1.00 22.20 ? 48 LEU A CD2 1 ATOM 372 N N . LEU A 1 49 ? 25.705 7.152 24.768 1.00 18.15 ? 49 LEU A N 1 ATOM 373 C CA . LEU A 1 49 ? 24.315 6.781 25.230 1.00 18.12 ? 49 LEU A CA 1 ATOM 374 C C . LEU A 1 49 ? 23.481 8.018 25.311 1.00 19.51 ? 49 LEU A C 1 ATOM 375 O O . LEU A 1 49 ? 23.877 8.991 25.976 1.00 18.64 ? 49 LEU A O 1 ATOM 376 C CB . LEU A 1 49 ? 24.345 6.131 26.593 1.00 17.19 ? 49 LEU A CB 1 ATOM 377 C CG . LEU A 1 49 ? 25.265 4.888 26.588 1.00 22.47 ? 49 LEU A CG 1 ATOM 378 C CD1 . LEU A 1 49 ? 25.255 4.375 27.984 1.00 23.39 ? 49 LEU A CD1 1 ATOM 379 C CD2 . LEU A 1 49 ? 24.941 3.814 25.426 1.00 20.67 ? 49 LEU A CD2 1 ATOM 380 N N . MET A 1 50 ? 22.287 7.971 24.649 1.00 15.65 ? 50 MET A N 1 ATOM 381 C CA . MET A 1 50 ? 21.304 9.054 24.676 1.00 16.39 ? 50 MET A CA 1 ATOM 382 C C . MET A 1 50 ? 20.089 8.553 25.442 1.00 18.05 ? 50 MET A C 1 ATOM 383 O O . MET A 1 50 ? 19.438 7.565 25.028 1.00 18.38 ? 50 MET A O 1 ATOM 384 C CB . MET A 1 50 ? 20.808 9.476 23.263 1.00 18.50 ? 50 MET A CB 1 ATOM 385 C CG . MET A 1 50 ? 21.879 9.887 22.238 1.00 21.71 ? 50 MET A CG 1 ATOM 386 S SD . MET A 1 50 ? 20.859 10.671 20.890 1.00 23.75 ? 50 MET A SD 1 ATOM 387 C CE . MET A 1 50 ? 19.959 9.231 20.121 1.00 15.31 ? 50 MET A CE 1 ATOM 388 N N . HIS A 1 51 ? 19.769 9.173 26.559 1.00 15.34 ? 51 HIS A N 1 ATOM 389 C CA . HIS A 1 51 ? 18.617 8.772 27.400 1.00 16.85 ? 51 HIS A CA 1 ATOM 390 C C . HIS A 1 51 ? 17.463 9.630 26.956 1.00 18.11 ? 51 HIS A C 1 ATOM 391 O O . HIS A 1 51 ? 17.545 10.888 27.087 1.00 19.46 ? 51 HIS A O 1 ATOM 392 C CB . HIS A 1 51 ? 18.934 9.047 28.868 1.00 16.77 ? 51 HIS A CB 1 ATOM 393 C CG . HIS A 1 51 ? 20.144 8.301 29.337 1.00 17.09 ? 51 HIS A CG 1 ATOM 394 N ND1 . HIS A 1 51 ? 20.142 6.925 29.527 1.00 21.52 ? 51 HIS A ND1 1 ATOM 395 C CD2 . HIS A 1 51 ? 21.426 8.713 29.490 1.00 19.09 ? 51 HIS A CD2 1 ATOM 396 C CE1 . HIS A 1 51 ? 21.373 6.545 29.878 1.00 22.60 ? 51 HIS A CE1 1 ATOM 397 N NE2 . HIS A 1 51 ? 22.141 7.626 29.923 1.00 22.63 ? 51 HIS A NE2 1 ATOM 398 N N . LEU A 1 52 ? 16.415 8.993 26.363 1.00 15.36 ? 52 LEU A N 1 ATOM 399 C CA . LEU A 1 52 ? 15.281 9.744 25.878 1.00 14.08 ? 52 LEU A CA 1 ATOM 400 C C . LEU A 1 52 ? 14.081 9.380 26.719 1.00 16.58 ? 52 LEU A C 1 ATOM 401 O O . LEU A 1 52 ? 13.836 8.198 26.943 1.00 17.81 ? 52 LEU A O 1 ATOM 402 C CB . LEU A 1 52 ? 14.966 9.415 24.405 1.00 14.59 ? 52 LEU A CB 1 ATOM 403 C CG . LEU A 1 52 ? 16.175 9.682 23.520 1.00 14.79 ? 52 LEU A CG 1 ATOM 404 C CD1 . LEU A 1 52 ? 15.861 9.239 22.059 1.00 14.52 ? 52 LEU A CD1 1 ATOM 405 C CD2 . LEU A 1 52 ? 16.615 11.185 23.490 1.00 16.31 ? 52 LEU A CD2 1 ATOM 406 N N . PHE A 1 53 ? 13.305 10.381 27.130 1.00 14.54 ? 53 PHE A N 1 ATOM 407 C CA . PHE A 1 53 ? 12.098 10.159 27.966 1.00 16.68 ? 53 PHE A CA 1 ATOM 408 C C . PHE A 1 53 ? 10.883 10.692 27.272 1.00 16.73 ? 53 PHE A C 1 ATOM 409 O O . PHE A 1 53 ? 10.843 11.822 26.763 1.00 15.28 ? 53 PHE A O 1 ATOM 410 C CB . PHE A 1 53 ? 12.234 10.874 29.368 1.00 16.57 ? 53 PHE A CB 1 ATOM 411 C CG . PHE A 1 53 ? 13.436 10.447 30.160 1.00 15.71 ? 53 PHE A CG 1 ATOM 412 C CD1 . PHE A 1 53 ? 14.688 10.907 29.803 1.00 17.03 ? 53 PHE A CD1 1 ATOM 413 C CD2 . PHE A 1 53 ? 13.276 9.637 31.292 1.00 20.53 ? 53 PHE A CD2 1 ATOM 414 C CE1 . PHE A 1 53 ? 15.787 10.571 30.486 1.00 20.89 ? 53 PHE A CE1 1 ATOM 415 C CE2 . PHE A 1 53 ? 14.439 9.220 32.027 1.00 19.26 ? 53 PHE A CE2 1 ATOM 416 C CZ . PHE A 1 53 ? 15.663 9.734 31.626 1.00 20.46 ? 53 PHE A CZ 1 ATOM 417 N N . ASN A 1 54 ? 9.875 9.792 27.222 1.00 17.33 ? 54 ASN A N 1 ATOM 418 C CA . ASN A 1 54 ? 8.613 10.229 26.617 1.00 16.53 ? 54 ASN A CA 1 ATOM 419 C C . ASN A 1 54 ? 7.854 11.144 27.555 1.00 16.01 ? 54 ASN A C 1 ATOM 420 O O . ASN A 1 54 ? 8.313 11.375 28.720 1.00 16.40 ? 54 ASN A O 1 ATOM 421 C CB . ASN A 1 54 ? 7.775 9.024 26.104 1.00 16.09 ? 54 ASN A CB 1 ATOM 422 C CG . ASN A 1 54 ? 7.094 8.253 27.202 1.00 18.19 ? 54 ASN A CG 1 ATOM 423 O OD1 . ASN A 1 54 ? 7.170 8.567 28.378 1.00 16.33 ? 54 ASN A OD1 1 ATOM 424 N ND2 . ASN A 1 54 ? 6.393 7.178 26.774 1.00 17.01 ? 54 ASN A ND2 1 ATOM 425 N N . TYR A 1 55 ? 6.712 11.636 27.075 1.00 15.95 ? 55 TYR A N 1 ATOM 426 C CA . TYR A 1 55 ? 6.019 12.629 27.903 1.00 19.90 ? 55 TYR A CA 1 ATOM 427 C C . TYR A 1 55 ? 5.627 12.061 29.292 1.00 20.25 ? 55 TYR A C 1 ATOM 428 O O . TYR A 1 55 ? 5.604 12.844 30.285 1.00 19.96 ? 55 TYR A O 1 ATOM 429 C CB . TYR A 1 55 ? 4.764 13.049 27.120 1.00 19.83 ? 55 TYR A CB 1 ATOM 430 C CG . TYR A 1 55 ? 3.907 14.030 27.843 1.00 23.19 ? 55 TYR A CG 1 ATOM 431 C CD1 . TYR A 1 55 ? 4.230 15.403 27.888 1.00 20.13 ? 55 TYR A CD1 1 ATOM 432 C CD2 . TYR A 1 55 ? 2.756 13.569 28.465 1.00 23.01 ? 55 TYR A CD2 1 ATOM 433 C CE1 . TYR A 1 55 ? 3.296 16.281 28.566 1.00 21.83 ? 55 TYR A CE1 1 ATOM 434 C CE2 . TYR A 1 55 ? 1.914 14.403 29.176 1.00 25.06 ? 55 TYR A CE2 1 ATOM 435 C CZ . TYR A 1 55 ? 2.177 15.715 29.214 1.00 23.34 ? 55 TYR A CZ 1 ATOM 436 O OH . TYR A 1 55 ? 1.246 16.475 29.948 1.00 29.61 ? 55 TYR A OH 1 ATOM 437 N N . ASP A 1 56 ? 5.317 10.759 29.364 1.00 19.03 ? 56 ASP A N 1 ATOM 438 C CA . ASP A 1 56 ? 5.048 10.103 30.638 1.00 20.83 ? 56 ASP A CA 1 ATOM 439 C C . ASP A 1 56 ? 6.220 9.738 31.484 1.00 21.14 ? 56 ASP A C 1 ATOM 440 O O . ASP A 1 56 ? 6.062 9.207 32.610 1.00 23.00 ? 56 ASP A O 1 ATOM 441 C CB . ASP A 1 56 ? 4.217 8.835 30.389 1.00 19.85 ? 56 ASP A CB 1 ATOM 442 C CG . ASP A 1 56 ? 2.855 9.124 29.747 1.00 23.12 ? 56 ASP A CG 1 ATOM 443 O OD1 . ASP A 1 56 ? 2.217 10.189 30.000 1.00 23.94 ? 56 ASP A OD1 1 ATOM 444 O OD2 . ASP A 1 56 ? 2.460 8.200 29.034 1.00 28.01 ? 56 ASP A OD2 1 ATOM 445 N N . GLY A 1 57 ? 7.437 10.021 30.978 1.00 18.54 ? 57 GLY A N 1 ATOM 446 C CA . GLY A 1 57 ? 8.576 9.701 31.812 1.00 19.31 ? 57 GLY A CA 1 ATOM 447 C C . GLY A 1 57 ? 9.146 8.315 31.637 1.00 18.30 ? 57 GLY A C 1 ATOM 448 O O . GLY A 1 57 ? 10.159 8.003 32.268 1.00 19.39 ? 57 GLY A O 1 ATOM 449 N N . ASN A 1 58 ? 8.579 7.526 30.718 1.00 18.30 ? 58 ASN A N 1 ATOM 450 C CA . ASN A 1 58 ? 9.228 6.245 30.338 1.00 19.10 ? 58 ASN A CA 1 ATOM 451 C C . ASN A 1 58 ? 10.435 6.471 29.478 1.00 17.82 ? 58 ASN A C 1 ATOM 452 O O . ASN A 1 58 ? 10.498 7.437 28.721 1.00 20.04 ? 58 ASN A O 1 ATOM 453 C CB . ASN A 1 58 ? 8.201 5.394 29.621 1.00 20.68 ? 58 ASN A CB 1 ATOM 454 C CG . ASN A 1 58 ? 7.091 4.869 30.550 1.00 25.10 ? 58 ASN A CG 1 ATOM 455 O OD1 . ASN A 1 58 ? 7.095 5.095 31.744 1.00 41.65 ? 58 ASN A OD1 1 ATOM 456 N ND2 . ASN A 1 58 ? 6.227 3.998 30.001 1.00 33.46 ? 58 ASN A ND2 1 ATOM 457 N N . THR A 1 59 ? 11.420 5.600 29.557 1.00 18.73 ? 59 THR A N 1 ATOM 458 C CA . THR A 1 59 ? 12.684 5.950 28.877 1.00 18.77 ? 59 THR A CA 1 ATOM 459 C C . THR A 1 59 ? 13.213 4.787 28.026 1.00 16.07 ? 59 THR A C 1 ATOM 460 O O . THR A 1 59 ? 13.043 3.557 28.356 1.00 18.04 ? 59 THR A O 1 ATOM 461 C CB . THR A 1 59 ? 13.780 6.430 29.929 1.00 20.85 ? 59 THR A CB 1 ATOM 462 O OG1 . THR A 1 59 ? 14.962 6.778 29.220 1.00 21.35 ? 59 THR A OG1 1 ATOM 463 C CG2 . THR A 1 59 ? 14.077 5.318 30.948 1.00 23.36 ? 59 THR A CG2 1 ATOM 464 N N . ILE A 1 60 ? 13.906 5.179 26.962 1.00 14.67 ? 60 ILE A N 1 ATOM 465 C CA . ILE A 1 60 ? 14.797 4.242 26.272 1.00 13.64 ? 60 ILE A CA 1 ATOM 466 C C . ILE A 1 60 ? 16.236 4.847 26.240 1.00 15.99 ? 60 ILE A C 1 ATOM 467 O O . ILE A 1 60 ? 16.384 6.075 26.450 1.00 17.50 ? 60 ILE A O 1 ATOM 468 C CB . ILE A 1 60 ? 14.386 3.947 24.816 1.00 14.44 ? 60 ILE A CB 1 ATOM 469 C CG1 . ILE A 1 60 ? 14.476 5.223 23.915 1.00 15.66 ? 60 ILE A CG1 1 ATOM 470 C CG2 . ILE A 1 60 ? 13.012 3.359 24.850 1.00 17.70 ? 60 ILE A CG2 1 ATOM 471 C CD1 . ILE A 1 60 ? 14.130 5.022 22.470 1.00 15.52 ? 60 ILE A CD1 1 ATOM 472 N N . THR A 1 61 ? 17.261 3.982 26.116 1.00 14.81 ? 61 THR A N 1 ATOM 473 C CA . THR A 1 61 ? 18.616 4.517 25.994 1.00 14.77 ? 61 THR A CA 1 ATOM 474 C C . THR A 1 61 ? 19.089 4.101 24.616 1.00 15.04 ? 61 THR A C 1 ATOM 475 O O . THR A 1 61 ? 18.978 2.921 24.261 1.00 15.43 ? 61 THR A O 1 ATOM 476 C CB . THR A 1 61 ? 19.569 3.938 27.089 1.00 17.00 ? 61 THR A CB 1 ATOM 477 O OG1 . THR A 1 61 ? 19.018 4.286 28.369 1.00 20.48 ? 61 THR A OG1 1 ATOM 478 C CG2 . THR A 1 61 ? 20.990 4.477 26.875 1.00 17.97 ? 61 THR A CG2 1 ATOM 479 N N . VAL A 1 62 ? 19.584 5.053 23.817 1.00 13.58 ? 62 VAL A N 1 ATOM 480 C CA . VAL A 1 62 ? 19.959 4.800 22.407 1.00 14.25 ? 62 VAL A CA 1 ATOM 481 C C . VAL A 1 62 ? 21.494 4.879 22.286 1.00 16.14 ? 62 VAL A C 1 ATOM 482 O O . VAL A 1 62 ? 22.092 5.842 22.785 1.00 18.04 ? 62 VAL A O 1 ATOM 483 C CB . VAL A 1 62 ? 19.335 5.863 21.492 1.00 14.99 ? 62 VAL A CB 1 ATOM 484 C CG1 . VAL A 1 62 ? 19.715 5.600 20.085 1.00 13.56 ? 62 VAL A CG1 1 ATOM 485 C CG2 . VAL A 1 62 ? 17.773 5.836 21.608 1.00 14.64 ? 62 VAL A CG2 1 ATOM 486 N N . ALA A 1 63 ? 22.079 3.829 21.694 1.00 14.08 ? 63 ALA A N 1 ATOM 487 C CA . ALA A 1 63 ? 23.573 3.845 21.501 1.00 15.73 ? 63 ALA A CA 1 ATOM 488 C C . ALA A 1 63 ? 23.885 4.379 20.126 1.00 16.32 ? 63 ALA A C 1 ATOM 489 O O . ALA A 1 63 ? 23.376 3.897 19.073 1.00 17.32 ? 63 ALA A O 1 ATOM 490 C CB . ALA A 1 63 ? 24.115 2.373 21.645 1.00 15.82 ? 63 ALA A CB 1 ATOM 491 N N . VAL A 1 64 ? 24.786 5.369 20.102 1.00 15.05 ? 64 VAL A N 1 ATOM 492 C CA . VAL A 1 64 ? 25.185 5.990 18.837 1.00 13.77 ? 64 VAL A CA 1 ATOM 493 C C . VAL A 1 64 ? 26.716 5.911 18.653 1.00 16.41 ? 64 VAL A C 1 ATOM 494 O O . VAL A 1 64 ? 27.442 6.229 19.606 1.00 18.04 ? 64 VAL A O 1 ATOM 495 C CB . VAL A 1 64 ? 24.879 7.508 19.036 1.00 15.14 ? 64 VAL A CB 1 ATOM 496 C CG1 . VAL A 1 64 ? 25.251 8.374 17.864 1.00 17.14 ? 64 VAL A CG1 1 ATOM 497 C CG2 . VAL A 1 64 ? 23.354 7.733 19.245 1.00 16.39 ? 64 VAL A CG2 1 ATOM 498 N N . ASP A 1 65 ? 27.126 5.503 17.476 1.00 16.18 ? 65 ASP A N 1 ATOM 499 C CA . ASP A 1 65 ? 28.546 5.395 17.126 1.00 18.86 ? 65 ASP A CA 1 ATOM 500 C C . ASP A 1 65 ? 29.015 6.893 16.959 1.00 19.25 ? 65 ASP A C 1 ATOM 501 O O . ASP A 1 65 ? 28.522 7.629 16.116 1.00 18.61 ? 65 ASP A O 1 ATOM 502 C CB . ASP A 1 65 ? 28.715 4.515 15.874 1.00 17.84 ? 65 ASP A CB 1 ATOM 503 C CG . ASP A 1 65 ? 30.190 4.426 15.438 1.00 23.27 ? 65 ASP A CG 1 ATOM 504 O OD1 . ASP A 1 65 ? 30.886 5.476 15.611 1.00 23.84 ? 65 ASP A OD1 1 ATOM 505 O OD2 . ASP A 1 65 ? 30.541 3.390 14.944 1.00 23.33 ? 65 ASP A OD2 1 ATOM 506 N N . VAL A 1 66 ? 30.016 7.291 17.803 1.00 18.85 ? 66 VAL A N 1 ATOM 507 C CA . VAL A 1 66 ? 30.485 8.705 17.793 1.00 20.16 ? 66 VAL A CA 1 ATOM 508 C C . VAL A 1 66 ? 31.339 9.084 16.522 1.00 20.07 ? 66 VAL A C 1 ATOM 509 O O . VAL A 1 66 ? 31.628 10.276 16.349 1.00 22.50 ? 66 VAL A O 1 ATOM 510 C CB . VAL A 1 66 ? 31.179 9.081 19.117 1.00 20.98 ? 66 VAL A CB 1 ATOM 511 C CG1 . VAL A 1 66 ? 30.294 8.852 20.332 1.00 18.52 ? 66 VAL A CG1 1 ATOM 512 C CG2 . VAL A 1 66 ? 32.560 8.378 19.330 1.00 21.69 ? 66 VAL A CG2 1 ATOM 513 N N . THR A 1 67 ? 31.758 8.109 15.727 1.00 19.29 ? 67 THR A N 1 ATOM 514 C CA . THR A 1 67 ? 32.557 8.418 14.532 1.00 21.34 ? 67 THR A CA 1 ATOM 515 C C . THR A 1 67 ? 31.638 8.787 13.396 1.00 20.01 ? 67 THR A C 1 ATOM 516 O O . THR A 1 67 ? 32.051 9.416 12.408 1.00 20.98 ? 67 THR A O 1 ATOM 517 C CB . THR A 1 67 ? 33.424 7.170 14.104 1.00 21.47 ? 67 THR A CB 1 ATOM 518 O OG1 . THR A 1 67 ? 32.607 6.108 13.528 1.00 23.05 ? 67 THR A OG1 1 ATOM 519 C CG2 . THR A 1 67 ? 34.302 6.729 15.243 1.00 23.65 ? 67 THR A CG2 1 ATOM 520 N N . ASN A 1 68 ? 30.324 8.363 13.470 1.00 19.59 ? 68 ASN A N 1 ATOM 521 C CA . ASN A 1 68 ? 29.536 8.596 12.297 1.00 16.69 ? 68 ASN A CA 1 ATOM 522 C C . ASN A 1 68 ? 28.039 9.010 12.646 1.00 16.28 ? 68 ASN A C 1 ATOM 523 O O . ASN A 1 68 ? 27.288 9.270 11.763 1.00 17.05 ? 68 ASN A O 1 ATOM 524 C CB . ASN A 1 68 ? 29.447 7.380 11.358 1.00 18.27 ? 68 ASN A CB 1 ATOM 525 C CG . ASN A 1 68 ? 29.138 6.124 12.133 1.00 21.78 ? 68 ASN A CG 1 ATOM 526 O OD1 . ASN A 1 68 ? 28.449 6.166 13.177 1.00 18.87 ? 68 ASN A OD1 1 ATOM 527 N ND2 . ASN A 1 68 ? 29.651 4.974 11.649 1.00 28.93 ? 68 ASN A ND2 1 ATOM 528 N N . VAL A 1 69 ? 27.785 9.176 13.930 1.00 16.81 ? 69 VAL A N 1 ATOM 529 C CA . VAL A 1 69 ? 26.402 9.481 14.519 1.00 17.13 ? 69 VAL A CA 1 ATOM 530 C C . VAL A 1 69 ? 25.371 8.435 14.061 1.00 18.13 ? 69 VAL A C 1 ATOM 531 O O . VAL A 1 69 ? 24.152 8.794 13.912 1.00 16.93 ? 69 VAL A O 1 ATOM 532 C CB . VAL A 1 69 ? 25.870 10.929 14.124 1.00 17.92 ? 69 VAL A CB 1 ATOM 533 C CG1 . VAL A 1 69 ? 25.179 11.506 15.322 1.00 18.41 ? 69 VAL A CG1 1 ATOM 534 C CG2 . VAL A 1 69 ? 27.118 11.932 13.741 1.00 18.60 ? 69 VAL A CG2 1 ATOM 535 N N . TYR A 1 70 ? 25.818 7.206 13.768 1.00 18.49 ? 70 TYR A N 1 ATOM 536 C CA . TYR A 1 70 ? 24.830 6.144 13.361 1.00 18.43 ? 70 TYR A CA 1 ATOM 537 C C . TYR A 1 70 ? 24.250 5.520 14.613 1.00 17.78 ? 70 TYR A C 1 ATOM 538 O O . TYR A 1 70 ? 24.971 5.136 15.496 1.00 18.33 ? 70 TYR A O 1 ATOM 539 C CB . TYR A 1 70 ? 25.508 5.080 12.528 1.00 19.96 ? 70 TYR A CB 1 ATOM 540 C CG . TYR A 1 70 ? 25.947 5.550 11.178 1.00 24.76 ? 70 TYR A CG 1 ATOM 541 C CD1 . TYR A 1 70 ? 26.866 4.743 10.442 1.00 35.16 ? 70 TYR A CD1 1 ATOM 542 C CD2 . TYR A 1 70 ? 25.485 6.733 10.590 1.00 30.71 ? 70 TYR A CD2 1 ATOM 543 C CE1 . TYR A 1 70 ? 27.338 5.158 9.194 1.00 34.26 ? 70 TYR A CE1 1 ATOM 544 C CE2 . TYR A 1 70 ? 25.976 7.157 9.309 1.00 31.77 ? 70 TYR A CE2 1 ATOM 545 C CZ . TYR A 1 70 ? 26.867 6.365 8.636 1.00 35.60 ? 70 TYR A CZ 1 ATOM 546 O OH . TYR A 1 70 ? 27.306 6.701 7.359 1.00 40.61 ? 70 TYR A OH 1 ATOM 547 N N . ILE A 1 71 ? 22.905 5.387 14.674 1.00 15.58 ? 71 ILE A N 1 ATOM 548 C CA . ILE A 1 71 ? 22.367 4.662 15.848 1.00 15.56 ? 71 ILE A CA 1 ATOM 549 C C . ILE A 1 71 ? 22.527 3.150 15.635 1.00 15.76 ? 71 ILE A C 1 ATOM 550 O O . ILE A 1 71 ? 22.262 2.656 14.516 1.00 17.58 ? 71 ILE A O 1 ATOM 551 C CB . ILE A 1 71 ? 20.816 5.024 15.904 1.00 15.91 ? 71 ILE A CB 1 ATOM 552 C CG1 . ILE A 1 71 ? 20.719 6.447 16.442 1.00 17.19 ? 71 ILE A CG1 1 ATOM 553 C CG2 . ILE A 1 71 ? 20.047 4.088 16.789 1.00 15.46 ? 71 ILE A CG2 1 ATOM 554 C CD1 . ILE A 1 71 ? 19.268 7.059 16.212 1.00 20.35 ? 71 ILE A CD1 1 ATOM 555 N N . MET A 1 72 ? 23.038 2.476 16.645 1.00 16.21 ? 72 MET A N 1 ATOM 556 C CA . MET A 1 72 ? 23.285 1.036 16.543 1.00 16.42 ? 72 MET A CA 1 ATOM 557 C C . MET A 1 72 ? 22.171 0.190 17.142 1.00 16.68 ? 72 MET A C 1 ATOM 558 O O . MET A 1 72 ? 21.970 -0.902 16.677 1.00 16.18 ? 72 MET A O 1 ATOM 559 C CB . MET A 1 72 ? 24.569 0.708 17.329 1.00 17.86 ? 72 MET A CB 1 ATOM 560 C CG . MET A 1 72 ? 25.879 1.366 16.712 1.00 23.66 ? 72 MET A CG 1 ATOM 561 S SD . MET A 1 72 ? 26.213 0.668 15.054 1.00 29.13 ? 72 MET A SD 1 ATOM 562 C CE . MET A 1 72 ? 25.480 1.949 14.011 1.00 31.66 ? 72 MET A CE 1 ATOM 563 N N . GLY A 1 73 ? 21.540 0.711 18.159 1.00 16.16 ? 73 GLY A N 1 ATOM 564 C CA . GLY A 1 73 ? 20.499 -0.026 18.915 1.00 14.18 ? 73 GLY A CA 1 ATOM 565 C C . GLY A 1 73 ? 20.106 0.733 20.101 1.00 15.34 ? 73 GLY A C 1 ATOM 566 O O . GLY A 1 73 ? 20.487 1.896 20.258 1.00 15.72 ? 73 GLY A O 1 ATOM 567 N N . TYR A 1 74 ? 19.280 0.111 20.929 1.00 14.66 ? 74 TYR A N 1 ATOM 568 C CA . TYR A 1 74 ? 18.711 0.864 22.036 1.00 14.78 ? 74 TYR A CA 1 ATOM 569 C C . TYR A 1 74 ? 18.280 -0.169 23.080 1.00 15.16 ? 74 TYR A C 1 ATOM 570 O O . TYR A 1 74 ? 18.097 -1.381 22.766 1.00 16.00 ? 74 TYR A O 1 ATOM 571 C CB . TYR A 1 74 ? 17.499 1.742 21.658 1.00 14.45 ? 74 TYR A CB 1 ATOM 572 C CG . TYR A 1 74 ? 16.415 1.054 20.911 1.00 13.60 ? 74 TYR A CG 1 ATOM 573 C CD1 . TYR A 1 74 ? 16.504 0.780 19.517 1.00 15.06 ? 74 TYR A CD1 1 ATOM 574 C CD2 . TYR A 1 74 ? 15.310 0.562 21.638 1.00 15.96 ? 74 TYR A CD2 1 ATOM 575 C CE1 . TYR A 1 74 ? 15.555 0.065 18.825 1.00 16.40 ? 74 TYR A CE1 1 ATOM 576 C CE2 . TYR A 1 74 ? 14.351 -0.186 20.953 1.00 16.47 ? 74 TYR A CE2 1 ATOM 577 C CZ . TYR A 1 74 ? 14.461 -0.390 19.581 1.00 17.20 ? 74 TYR A CZ 1 ATOM 578 O OH . TYR A 1 74 ? 13.520 -1.166 18.921 1.00 16.19 ? 74 TYR A OH 1 ATOM 579 N N . LEU A 1 75 ? 18.098 0.307 24.272 1.00 14.12 ? 75 LEU A N 1 ATOM 580 C CA . LEU A 1 75 ? 17.622 -0.493 25.382 1.00 14.95 ? 75 LEU A CA 1 ATOM 581 C C . LEU A 1 75 ? 16.276 0.003 25.853 1.00 15.78 ? 75 LEU A C 1 ATOM 582 O O . LEU A 1 75 ? 16.115 1.217 26.110 1.00 18.01 ? 75 LEU A O 1 ATOM 583 C CB . LEU A 1 75 ? 18.620 -0.355 26.593 1.00 16.06 ? 75 LEU A CB 1 ATOM 584 C CG . LEU A 1 75 ? 18.245 -1.040 27.889 1.00 18.09 ? 75 LEU A CG 1 ATOM 585 C CD1 . LEU A 1 75 ? 18.351 -2.582 27.682 1.00 19.07 ? 75 LEU A CD1 1 ATOM 586 C CD2 . LEU A 1 75 ? 19.230 -0.586 29.027 1.00 19.58 ? 75 LEU A CD2 1 ATOM 587 N N . ALA A 1 76 ? 15.329 -0.892 26.041 1.00 15.50 ? 76 ALA A N 1 ATOM 588 C CA . ALA A 1 76 ? 13.989 -0.473 26.550 1.00 17.24 ? 76 ALA A CA 1 ATOM 589 C C . ALA A 1 76 ? 13.604 -1.462 27.655 1.00 20.26 ? 76 ALA A C 1 ATOM 590 O O . ALA A 1 76 ? 13.409 -2.649 27.357 1.00 19.16 ? 76 ALA A O 1 ATOM 591 C CB . ALA A 1 76 ? 12.974 -0.482 25.425 1.00 17.67 ? 76 ALA A CB 1 ATOM 592 N N . LEU A 1 77 ? 13.674 -0.965 28.902 1.00 23.06 ? 77 LEU A N 1 ATOM 593 C CA . LEU A 1 77 ? 13.490 -1.737 30.168 1.00 22.27 ? 77 LEU A CA 1 ATOM 594 C C . LEU A 1 77 ? 14.579 -2.778 30.278 1.00 20.56 ? 77 LEU A C 1 ATOM 595 O O . LEU A 1 77 ? 15.729 -2.425 30.618 1.00 22.75 ? 77 LEU A O 1 ATOM 596 C CB . LEU A 1 77 ? 12.135 -2.365 30.186 1.00 23.18 ? 77 LEU A CB 1 ATOM 597 C CG . LEU A 1 77 ? 11.752 -2.978 31.569 1.00 25.28 ? 77 LEU A CG 1 ATOM 598 C CD1 . LEU A 1 77 ? 12.560 -2.547 32.759 1.00 23.05 ? 77 LEU A CD1 1 ATOM 599 C CD2 . LEU A 1 77 ? 10.363 -3.072 31.756 1.00 28.58 ? 77 LEU A CD2 1 ATOM 600 N N . THR A 1 78 ? 14.268 -4.040 29.988 1.00 18.67 ? 78 THR A N 1 ATOM 601 C CA . THR A 1 78 ? 15.302 -5.071 30.200 1.00 18.81 ? 78 THR A CA 1 ATOM 602 C C . THR A 1 78 ? 15.629 -5.755 28.857 1.00 16.69 ? 78 THR A C 1 ATOM 603 O O . THR A 1 78 ? 16.295 -6.803 28.825 1.00 18.79 ? 78 THR A O 1 ATOM 604 C CB . THR A 1 78 ? 14.893 -6.128 31.275 1.00 19.15 ? 78 THR A CB 1 ATOM 605 O OG1 . THR A 1 78 ? 13.648 -6.831 30.848 1.00 20.62 ? 78 THR A OG1 1 ATOM 606 C CG2 . THR A 1 78 ? 14.707 -5.398 32.674 1.00 21.91 ? 78 THR A CG2 1 ATOM 607 N N . THR A 1 79 ? 15.155 -5.188 27.710 1.00 15.43 ? 79 THR A N 1 ATOM 608 C CA . THR A 1 79 ? 15.443 -5.782 26.469 1.00 15.14 ? 79 THR A CA 1 ATOM 609 C C . THR A 1 79 ? 16.305 -4.849 25.625 1.00 14.98 ? 79 THR A C 1 ATOM 610 O O . THR A 1 79 ? 15.926 -3.651 25.495 1.00 16.55 ? 79 THR A O 1 ATOM 611 C CB . THR A 1 79 ? 14.132 -6.052 25.693 1.00 14.99 ? 79 THR A CB 1 ATOM 612 O OG1 . THR A 1 79 ? 13.338 -6.966 26.471 1.00 17.68 ? 79 THR A OG1 1 ATOM 613 C CG2 . THR A 1 79 ? 14.398 -6.731 24.418 1.00 15.77 ? 79 THR A CG2 1 ATOM 614 N N . SER A 1 80 ? 17.390 -5.354 25.047 1.00 14.92 ? 80 SER A N 1 ATOM 615 C CA . SER A 1 80 ? 18.120 -4.570 24.040 1.00 15.24 ? 80 SER A CA 1 ATOM 616 C C . SER A 1 80 ? 17.753 -4.951 22.672 1.00 15.79 ? 80 SER A C 1 ATOM 617 O O . SER A 1 80 ? 17.274 -6.067 22.394 1.00 16.04 ? 80 SER A O 1 ATOM 618 C CB . SER A 1 80 ? 19.675 -4.719 24.245 1.00 17.88 ? 80 SER A CB 1 ATOM 619 O OG . SER A 1 80 ? 20.016 -6.080 23.990 1.00 17.44 ? 80 SER A OG 1 ATOM 620 N N . TYR A 1 81 ? 17.888 -3.999 21.741 1.00 14.59 ? 81 TYR A N 1 ATOM 621 C CA . TYR A 1 81 ? 17.536 -4.216 20.358 1.00 13.68 ? 81 TYR A CA 1 ATOM 622 C C . TYR A 1 81 ? 18.643 -3.597 19.504 1.00 15.21 ? 81 TYR A C 1 ATOM 623 O O . TYR A 1 81 ? 19.080 -2.430 19.777 1.00 15.32 ? 81 TYR A O 1 ATOM 624 C CB . TYR A 1 81 ? 16.260 -3.343 20.046 1.00 14.34 ? 81 TYR A CB 1 ATOM 625 C CG . TYR A 1 81 ? 15.048 -3.718 20.876 1.00 10.55 ? 81 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 81 ? 14.865 -3.209 22.135 1.00 12.37 ? 81 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 81 ? 14.143 -4.658 20.392 1.00 13.89 ? 81 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 81 ? 13.759 -3.566 22.953 1.00 13.89 ? 81 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 81 ? 13.005 -5.052 21.176 1.00 16.35 ? 81 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 81 ? 12.839 -4.471 22.409 1.00 14.33 ? 81 TYR A CZ 1 ATOM 631 O OH . TYR A 1 81 ? 11.744 -4.813 23.157 1.00 17.29 ? 81 TYR A OH 1 ATOM 632 N N . PHE A 1 82 ? 19.112 -4.359 18.527 1.00 15.30 ? 82 PHE A N 1 ATOM 633 C CA . PHE A 1 82 ? 20.173 -3.864 17.582 1.00 15.45 ? 82 PHE A CA 1 ATOM 634 C C . PHE A 1 82 ? 19.844 -4.092 16.157 1.00 16.00 ? 82 PHE A C 1 ATOM 635 O O . PHE A 1 82 ? 19.144 -5.068 15.812 1.00 16.98 ? 82 PHE A O 1 ATOM 636 C CB . PHE A 1 82 ? 21.548 -4.636 17.877 1.00 15.76 ? 82 PHE A CB 1 ATOM 637 C CG . PHE A 1 82 ? 22.117 -4.318 19.246 1.00 17.37 ? 82 PHE A CG 1 ATOM 638 C CD1 . PHE A 1 82 ? 22.979 -3.245 19.402 1.00 17.62 ? 82 PHE A CD1 1 ATOM 639 C CD2 . PHE A 1 82 ? 21.704 -5.039 20.381 1.00 13.74 ? 82 PHE A CD2 1 ATOM 640 C CE1 . PHE A 1 82 ? 23.522 -2.935 20.732 1.00 17.34 ? 82 PHE A CE1 1 ATOM 641 C CE2 . PHE A 1 82 ? 22.235 -4.749 21.709 1.00 16.47 ? 82 PHE A CE2 1 ATOM 642 C CZ . PHE A 1 82 ? 23.082 -3.679 21.860 1.00 18.48 ? 82 PHE A CZ 1 ATOM 643 N N . PHE A 1 83 ? 20.296 -3.192 15.264 1.00 15.02 ? 83 PHE A N 1 ATOM 644 C CA . PHE A 1 83 ? 20.066 -3.426 13.821 1.00 14.88 ? 83 PHE A CA 1 ATOM 645 C C . PHE A 1 83 ? 20.811 -4.695 13.430 1.00 15.84 ? 83 PHE A C 1 ATOM 646 O O . PHE A 1 83 ? 21.853 -5.088 14.054 1.00 17.01 ? 83 PHE A O 1 ATOM 647 C CB . PHE A 1 83 ? 20.610 -2.225 13.066 1.00 14.99 ? 83 PHE A CB 1 ATOM 648 C CG . PHE A 1 83 ? 19.696 -0.989 13.208 1.00 14.17 ? 83 PHE A CG 1 ATOM 649 C CD1 . PHE A 1 83 ? 18.330 -1.093 12.753 1.00 14.35 ? 83 PHE A CD1 1 ATOM 650 C CD2 . PHE A 1 83 ? 20.181 0.213 13.752 1.00 15.49 ? 83 PHE A CD2 1 ATOM 651 C CE1 . PHE A 1 83 ? 17.517 0.001 12.888 1.00 14.99 ? 83 PHE A CE1 1 ATOM 652 C CE2 . PHE A 1 83 ? 19.379 1.353 13.794 1.00 14.81 ? 83 PHE A CE2 1 ATOM 653 C CZ . PHE A 1 83 ? 18.007 1.207 13.429 1.00 16.99 ? 83 PHE A CZ 1 ATOM 654 N N . ASN A 1 84 ? 20.315 -5.273 12.370 1.00 17.36 ? 84 ASN A N 1 ATOM 655 C CA . ASN A 1 84 ? 20.912 -6.481 11.814 1.00 18.60 ? 84 ASN A CA 1 ATOM 656 C C . ASN A 1 84 ? 21.988 -6.102 10.811 1.00 17.14 ? 84 ASN A C 1 ATOM 657 O O . ASN A 1 84 ? 21.810 -6.122 9.571 1.00 19.00 ? 84 ASN A O 1 ATOM 658 C CB . ASN A 1 84 ? 19.801 -7.219 11.085 1.00 16.67 ? 84 ASN A CB 1 ATOM 659 C CG . ASN A 1 84 ? 20.219 -8.659 10.680 1.00 18.07 ? 84 ASN A CG 1 ATOM 660 O OD1 . ASN A 1 84 ? 19.628 -9.243 9.716 1.00 24.67 ? 84 ASN A OD1 1 ATOM 661 N ND2 . ASN A 1 84 ? 21.152 -9.211 11.374 1.00 17.63 ? 84 ASN A ND2 1 ATOM 662 N N . GLU A 1 85 ? 23.140 -5.752 11.390 1.00 18.96 ? 85 GLU A N 1 ATOM 663 C CA . GLU A 1 85 ? 24.337 -5.316 10.520 1.00 19.95 ? 85 GLU A CA 1 ATOM 664 C C . GLU A 1 85 ? 25.552 -5.459 11.402 1.00 20.24 ? 85 GLU A C 1 ATOM 665 O O . GLU A 1 85 ? 25.495 -5.367 12.628 1.00 18.83 ? 85 GLU A O 1 ATOM 666 C CB . GLU A 1 85 ? 24.157 -3.925 9.968 1.00 20.68 ? 85 GLU A CB 1 ATOM 667 C CG . GLU A 1 85 ? 24.063 -2.889 11.076 1.00 23.70 ? 85 GLU A CG 1 ATOM 668 C CD . GLU A 1 85 ? 24.010 -1.555 10.433 1.00 31.48 ? 85 GLU A CD 1 ATOM 669 O OE1 . GLU A 1 85 ? 22.889 -1.039 10.275 1.00 23.62 ? 85 GLU A OE1 1 ATOM 670 O OE2 . GLU A 1 85 ? 25.121 -1.067 10.015 1.00 32.89 ? 85 GLU A OE2 1 ATOM 671 N N . PRO A 1 86 ? 26.723 -5.693 10.761 1.00 21.69 ? 86 PRO A N 1 ATOM 672 C CA . PRO A 1 86 ? 27.922 -6.016 11.581 1.00 22.36 ? 86 PRO A CA 1 ATOM 673 C C . PRO A 1 86 ? 28.332 -4.904 12.575 1.00 18.56 ? 86 PRO A C 1 ATOM 674 O O . PRO A 1 86 ? 28.806 -5.213 13.714 1.00 22.25 ? 86 PRO A O 1 ATOM 675 C CB . PRO A 1 86 ? 29.007 -6.292 10.487 1.00 21.26 ? 86 PRO A CB 1 ATOM 676 C CG . PRO A 1 86 ? 28.271 -6.718 9.247 1.00 22.64 ? 86 PRO A CG 1 ATOM 677 C CD . PRO A 1 86 ? 26.875 -5.941 9.318 1.00 22.16 ? 86 PRO A CD 1 ATOM 678 N N . ALA A 1 87 ? 28.173 -3.613 12.226 1.00 19.21 ? 87 ALA A N 1 ATOM 679 C CA . ALA A 1 87 ? 28.553 -2.562 13.167 1.00 19.43 ? 87 ALA A CA 1 ATOM 680 C C . ALA A 1 87 ? 27.684 -2.597 14.376 1.00 20.54 ? 87 ALA A C 1 ATOM 681 O O . ALA A 1 87 ? 28.164 -2.342 15.460 1.00 18.47 ? 87 ALA A O 1 ATOM 682 C CB . ALA A 1 87 ? 28.501 -1.181 12.507 1.00 20.85 ? 87 ALA A CB 1 ATOM 683 N N . ALA A 1 88 ? 26.397 -2.989 14.206 1.00 19.56 ? 88 ALA A N 1 ATOM 684 C CA . ALA A 1 88 ? 25.540 -3.031 15.365 1.00 19.80 ? 88 ALA A CA 1 ATOM 685 C C . ALA A 1 88 ? 25.800 -4.280 16.171 1.00 20.11 ? 88 ALA A C 1 ATOM 686 O O . ALA A 1 88 ? 25.753 -4.232 17.420 1.00 19.64 ? 88 ALA A O 1 ATOM 687 C CB . ALA A 1 88 ? 24.018 -2.939 14.890 1.00 18.37 ? 88 ALA A CB 1 ATOM 688 N N . ASP A 1 89 ? 26.101 -5.420 15.502 1.00 21.04 ? 89 ASP A N 1 ATOM 689 C CA . ASP A 1 89 ? 26.473 -6.586 16.283 1.00 23.11 ? 89 ASP A CA 1 ATOM 690 C C . ASP A 1 89 ? 27.710 -6.306 17.104 1.00 20.92 ? 89 ASP A C 1 ATOM 691 O O . ASP A 1 89 ? 27.762 -6.666 18.255 1.00 21.81 ? 89 ASP A O 1 ATOM 692 C CB . ASP A 1 89 ? 26.633 -7.928 15.471 1.00 24.50 ? 89 ASP A CB 1 ATOM 693 C CG . ASP A 1 89 ? 27.093 -9.076 16.433 1.00 30.70 ? 89 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 89 ? 26.375 -9.526 17.430 1.00 36.46 ? 89 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 89 ? 28.309 -9.350 16.350 1.00 36.45 ? 89 ASP A OD2 1 ATOM 696 N N . LEU A 1 90 ? 28.696 -5.615 16.482 1.00 21.66 ? 90 LEU A N 1 ATOM 697 C CA . LEU A 1 90 ? 29.890 -5.180 17.238 1.00 21.50 ? 90 LEU A CA 1 ATOM 698 C C . LEU A 1 90 ? 29.517 -4.339 18.443 1.00 22.20 ? 90 LEU A C 1 ATOM 699 O O . LEU A 1 90 ? 30.030 -4.550 19.520 1.00 20.96 ? 90 LEU A O 1 ATOM 700 C CB . LEU A 1 90 ? 30.887 -4.400 16.307 1.00 22.44 ? 90 LEU A CB 1 ATOM 701 C CG . LEU A 1 90 ? 32.157 -3.899 17.056 1.00 26.82 ? 90 LEU A CG 1 ATOM 702 C CD1 . LEU A 1 90 ? 32.936 -5.135 17.620 1.00 29.48 ? 90 LEU A CD1 1 ATOM 703 C CD2 . LEU A 1 90 ? 33.026 -2.977 16.212 1.00 28.43 ? 90 LEU A CD2 1 ATOM 704 N N . ALA A 1 91 ? 28.640 -3.367 18.262 1.00 19.99 ? 91 ALA A N 1 ATOM 705 C CA . ALA A 1 91 ? 28.241 -2.508 19.357 1.00 18.24 ? 91 ALA A CA 1 ATOM 706 C C . ALA A 1 91 ? 27.641 -3.340 20.510 1.00 18.00 ? 91 ALA A C 1 ATOM 707 O O . ALA A 1 91 ? 27.810 -3.049 21.721 1.00 18.75 ? 91 ALA A O 1 ATOM 708 C CB . ALA A 1 91 ? 27.217 -1.450 18.898 1.00 17.59 ? 91 ALA A CB 1 ATOM 709 N N . SER A 1 92 ? 26.904 -4.383 20.133 1.00 19.65 ? 92 SER A N 1 ATOM 710 C CA . SER A 1 92 ? 26.279 -5.237 21.185 1.00 18.04 ? 92 SER A CA 1 ATOM 711 C C . SER A 1 92 ? 27.285 -5.995 22.047 1.00 19.73 ? 92 SER A C 1 ATOM 712 O O . SER A 1 92 ? 26.908 -6.515 23.107 1.00 19.18 ? 92 SER A O 1 ATOM 713 C CB . SER A 1 92 ? 25.268 -6.239 20.610 1.00 19.61 ? 92 SER A CB 1 ATOM 714 O OG . SER A 1 92 ? 25.908 -7.405 20.017 1.00 21.00 ? 92 SER A OG 1 ATOM 715 N N . GLN A 1 93 ? 28.559 -5.914 21.658 1.00 21.60 ? 93 GLN A N 1 ATOM 716 C CA . GLN A 1 93 ? 29.630 -6.429 22.519 1.00 22.65 ? 93 GLN A CA 1 ATOM 717 C C . GLN A 1 93 ? 30.018 -5.481 23.618 1.00 23.74 ? 93 GLN A C 1 ATOM 718 O O . GLN A 1 93 ? 30.580 -5.927 24.634 1.00 24.92 ? 93 GLN A O 1 ATOM 719 C CB . GLN A 1 93 ? 30.884 -6.823 21.668 1.00 23.33 ? 93 GLN A CB 1 ATOM 720 C CG . GLN A 1 93 ? 30.543 -7.841 20.631 1.00 28.44 ? 93 GLN A CG 1 ATOM 721 C CD . GLN A 1 93 ? 31.686 -8.223 19.657 1.00 39.73 ? 93 GLN A CD 1 ATOM 722 O OE1 . GLN A 1 93 ? 32.839 -8.190 20.014 1.00 37.42 ? 93 GLN A OE1 1 ATOM 723 N NE2 . GLN A 1 93 ? 31.331 -8.583 18.417 1.00 42.22 ? 93 GLN A NE2 1 ATOM 724 N N . TYR A 1 94 ? 29.581 -4.216 23.500 1.00 23.19 ? 94 TYR A N 1 ATOM 725 C CA . TYR A 1 94 ? 29.933 -3.190 24.457 1.00 22.92 ? 94 TYR A CA 1 ATOM 726 C C . TYR A 1 94 ? 28.799 -2.551 25.277 1.00 24.62 ? 94 TYR A C 1 ATOM 727 O O . TYR A 1 94 ? 29.014 -2.133 26.406 1.00 25.28 ? 94 TYR A O 1 ATOM 728 C CB . TYR A 1 94 ? 30.757 -2.093 23.693 1.00 22.84 ? 94 TYR A CB 1 ATOM 729 C CG . TYR A 1 94 ? 32.026 -2.655 23.135 1.00 24.29 ? 94 TYR A CG 1 ATOM 730 C CD1 . TYR A 1 94 ? 33.156 -2.743 23.947 1.00 25.46 ? 94 TYR A CD1 1 ATOM 731 C CD2 . TYR A 1 94 ? 32.089 -3.110 21.864 1.00 22.59 ? 94 TYR A CD2 1 ATOM 732 C CE1 . TYR A 1 94 ? 34.332 -3.337 23.430 1.00 26.78 ? 94 TYR A CE1 1 ATOM 733 C CE2 . TYR A 1 94 ? 33.264 -3.699 21.309 1.00 29.21 ? 94 TYR A CE2 1 ATOM 734 C CZ . TYR A 1 94 ? 34.369 -3.777 22.118 1.00 32.78 ? 94 TYR A CZ 1 ATOM 735 O OH . TYR A 1 94 ? 35.543 -4.293 21.616 1.00 34.81 ? 94 TYR A OH 1 ATOM 736 N N . VAL A 1 95 ? 27.613 -2.332 24.675 1.00 21.29 ? 95 VAL A N 1 ATOM 737 C CA . VAL A 1 95 ? 26.580 -1.596 25.346 1.00 21.21 ? 95 VAL A CA 1 ATOM 738 C C . VAL A 1 95 ? 25.389 -2.525 25.602 1.00 19.84 ? 95 VAL A C 1 ATOM 739 O O . VAL A 1 95 ? 25.110 -3.512 24.833 1.00 20.06 ? 95 VAL A O 1 ATOM 740 C CB . VAL A 1 95 ? 26.019 -0.398 24.482 1.00 20.21 ? 95 VAL A CB 1 ATOM 741 C CG1 . VAL A 1 95 ? 27.214 0.555 24.248 1.00 24.46 ? 95 VAL A CG1 1 ATOM 742 C CG2 . VAL A 1 95 ? 25.470 -0.874 23.147 1.00 18.91 ? 95 VAL A CG2 1 ATOM 743 N N . PHE A 1 96 ? 24.740 -2.192 26.684 1.00 19.53 ? 96 PHE A N 1 ATOM 744 C CA . PHE A 1 96 ? 23.448 -2.871 27.129 1.00 20.35 ? 96 PHE A CA 1 ATOM 745 C C . PHE A 1 96 ? 23.687 -4.352 27.418 1.00 21.69 ? 96 PHE A C 1 ATOM 746 O O . PHE A 1 96 ? 22.749 -5.150 27.312 1.00 21.29 ? 96 PHE A O 1 ATOM 747 C CB . PHE A 1 96 ? 22.373 -2.739 26.036 1.00 19.78 ? 96 PHE A CB 1 ATOM 748 C CG . PHE A 1 96 ? 22.215 -1.329 25.509 1.00 20.04 ? 96 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 96 ? 22.309 -0.216 26.404 1.00 18.56 ? 96 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 96 ? 21.879 -1.118 24.170 1.00 17.79 ? 96 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 96 ? 22.150 1.118 25.914 1.00 18.43 ? 96 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 96 ? 21.729 0.226 23.639 1.00 19.86 ? 96 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 96 ? 21.891 1.353 24.540 1.00 18.99 ? 96 PHE A CZ 1 ATOM 754 N N . ARG A 1 97 ? 24.927 -4.732 27.744 1.00 21.27 ? 97 ARG A N 1 ATOM 755 C CA . ARG A 1 97 ? 25.137 -6.187 28.083 1.00 22.84 ? 97 ARG A CA 1 ATOM 756 C C . ARG A 1 97 ? 24.358 -6.720 29.276 1.00 24.76 ? 97 ARG A C 1 ATOM 757 O O . ARG A 1 97 ? 24.172 -7.948 29.366 1.00 25.26 ? 97 ARG A O 1 ATOM 758 C CB . ARG A 1 97 ? 26.645 -6.424 28.300 1.00 23.72 ? 97 ARG A CB 1 ATOM 759 C CG . ARG A 1 97 ? 27.455 -6.082 27.071 1.00 27.80 ? 97 ARG A CG 1 ATOM 760 C CD . ARG A 1 97 ? 27.803 -7.184 26.175 1.00 35.22 ? 97 ARG A CD 1 ATOM 761 N NE . ARG A 1 97 ? 28.167 -8.323 27.029 1.00 34.71 ? 97 ARG A NE 1 ATOM 762 C CZ . ARG A 1 97 ? 29.391 -8.578 27.462 1.00 39.16 ? 97 ARG A CZ 1 ATOM 763 N NH1 . ARG A 1 97 ? 29.593 -9.636 28.275 1.00 32.16 ? 97 ARG A NH1 1 ATOM 764 N NH2 . ARG A 1 97 ? 30.385 -7.776 27.124 1.00 41.64 ? 97 ARG A NH2 1 ATOM 765 N N . SER A 1 98 ? 23.894 -5.829 30.153 1.00 22.94 ? 98 SER A N 1 ATOM 766 C CA . SER A 1 98 ? 23.091 -6.191 31.341 1.00 24.23 ? 98 SER A CA 1 ATOM 767 C C . SER A 1 98 ? 21.586 -6.438 31.008 1.00 22.32 ? 98 SER A C 1 ATOM 768 O O . SER A 1 98 ? 20.839 -6.846 31.853 1.00 22.89 ? 98 SER A O 1 ATOM 769 C CB . SER A 1 98 ? 23.145 -5.051 32.352 1.00 25.54 ? 98 SER A CB 1 ATOM 770 O OG . SER A 1 98 ? 22.859 -3.799 31.667 1.00 38.00 ? 98 SER A OG 1 ATOM 771 N N . ALA A 1 99 ? 21.181 -6.214 29.762 1.00 21.68 ? 99 ALA A N 1 ATOM 772 C CA . ALA A 1 99 ? 19.791 -6.557 29.375 1.00 20.15 ? 99 ALA A CA 1 ATOM 773 C C . ALA A 1 99 ? 19.569 -8.033 29.606 1.00 19.75 ? 99 ALA A C 1 ATOM 774 O O . ALA A 1 99 ? 20.427 -8.887 29.327 1.00 20.93 ? 99 ALA A O 1 ATOM 775 C CB . ALA A 1 99 ? 19.516 -6.297 27.920 1.00 18.70 ? 99 ALA A CB 1 ATOM 776 N N . ARG A 1 100 ? 18.358 -8.357 30.037 1.00 20.57 ? 100 ARG A N 1 ATOM 777 C CA . ARG A 1 100 ? 18.004 -9.790 30.180 1.00 19.07 ? 100 ARG A CA 1 ATOM 778 C C . ARG A 1 100 ? 17.860 -10.503 28.880 1.00 19.63 ? 100 ARG A C 1 ATOM 779 O O . ARG A 1 100 ? 18.068 -11.725 28.834 1.00 21.73 ? 100 ARG A O 1 ATOM 780 C CB . ARG A 1 100 ? 16.692 -9.945 30.978 1.00 21.17 ? 100 ARG A CB 1 ATOM 781 C CG . ARG A 1 100 ? 16.780 -9.374 32.404 1.00 24.01 ? 100 ARG A CG 1 ATOM 782 C CD . ARG A 1 100 ? 15.399 -9.708 33.191 1.00 34.26 ? 100 ARG A CD 1 ATOM 783 N NE . ARG A 1 100 ? 14.961 -11.093 32.795 1.00 44.18 ? 100 ARG A NE 1 ATOM 784 C CZ . ARG A 1 100 ? 13.714 -11.489 32.426 1.00 48.56 ? 100 ARG A CZ 1 ATOM 785 N NH1 . ARG A 1 100 ? 12.654 -10.662 32.490 1.00 50.77 ? 100 ARG A NH1 1 ATOM 786 N NH2 . ARG A 1 100 ? 13.510 -12.747 32.028 1.00 44.61 ? 100 ARG A NH2 1 ATOM 787 N N . ARG A 1 101 ? 17.539 -9.811 27.763 1.00 16.59 ? 101 ARG A N 1 ATOM 788 C CA . ARG A 1 101 ? 17.479 -10.478 26.443 1.00 18.27 ? 101 ARG A CA 1 ATOM 789 C C . ARG A 1 101 ? 17.845 -9.480 25.352 1.00 16.76 ? 101 ARG A C 1 ATOM 790 O O . ARG A 1 101 ? 17.716 -8.263 25.623 1.00 17.73 ? 101 ARG A O 1 ATOM 791 C CB . ARG A 1 101 ? 16.105 -11.109 26.037 1.00 18.50 ? 101 ARG A CB 1 ATOM 792 C CG . ARG A 1 101 ? 15.067 -10.052 26.027 1.00 22.77 ? 101 ARG A CG 1 ATOM 793 C CD . ARG A 1 101 ? 13.782 -10.649 25.355 1.00 19.39 ? 101 ARG A CD 1 ATOM 794 N NE . ARG A 1 101 ? 12.770 -9.590 25.369 1.00 19.23 ? 101 ARG A NE 1 ATOM 795 C CZ . ARG A 1 101 ? 11.550 -9.701 24.835 1.00 17.71 ? 101 ARG A CZ 1 ATOM 796 N NH1 . ARG A 1 101 ? 11.078 -10.846 24.322 1.00 18.08 ? 101 ARG A NH1 1 ATOM 797 N NH2 . ARG A 1 101 ? 10.775 -8.610 24.872 1.00 18.95 ? 101 ARG A NH2 1 ATOM 798 N N . LYS A 1 102 ? 18.366 -9.971 24.260 1.00 15.73 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 18.785 -9.097 23.167 1.00 15.02 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 18.023 -9.560 21.938 1.00 15.61 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 18.085 -10.759 21.503 1.00 16.93 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 20.335 -9.227 22.905 1.00 17.28 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 20.736 -8.464 21.633 1.00 14.92 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 22.234 -8.449 21.364 1.00 18.41 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 22.766 -9.792 20.889 1.00 18.67 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 24.342 -9.706 21.052 1.00 25.12 ? 102 LYS A NZ 1 ATOM 807 N N . ILE A 1 103 ? 17.315 -8.591 21.301 1.00 14.98 ? 103 ILE A N 1 ATOM 808 C CA . ILE A 1 103 ? 16.645 -8.909 20.059 1.00 14.59 ? 103 ILE A CA 1 ATOM 809 C C . ILE A 1 103 ? 17.372 -8.238 18.919 1.00 14.92 ? 103 ILE A C 1 ATOM 810 O O . ILE A 1 103 ? 17.712 -7.042 19.016 1.00 15.64 ? 103 ILE A O 1 ATOM 811 C CB . ILE A 1 103 ? 15.166 -8.368 20.149 1.00 12.35 ? 103 ILE A CB 1 ATOM 812 C CG1 . ILE A 1 103 ? 14.365 -9.291 21.086 1.00 14.83 ? 103 ILE A CG1 1 ATOM 813 C CG2 . ILE A 1 103 ? 14.514 -8.360 18.682 1.00 14.26 ? 103 ILE A CG2 1 ATOM 814 C CD1 . ILE A 1 103 ? 12.896 -8.791 21.346 1.00 16.56 ? 103 ILE A CD1 1 ATOM 815 N N . THR A 1 104 ? 17.657 -8.941 17.837 1.00 13.72 ? 104 THR A N 1 ATOM 816 C CA . THR A 1 104 ? 18.245 -8.293 16.682 1.00 14.67 ? 104 THR A CA 1 ATOM 817 C C . THR A 1 104 ? 17.024 -7.927 15.802 1.00 15.32 ? 104 THR A C 1 ATOM 818 O O . THR A 1 104 ? 16.231 -8.782 15.433 1.00 16.18 ? 104 THR A O 1 ATOM 819 C CB . THR A 1 104 ? 19.181 -9.221 15.873 1.00 16.60 ? 104 THR A CB 1 ATOM 820 O OG1 . THR A 1 104 ? 20.276 -9.595 16.773 1.00 16.57 ? 104 THR A OG1 1 ATOM 821 C CG2 . THR A 1 104 ? 19.778 -8.472 14.680 1.00 14.86 ? 104 THR A CG2 1 ATOM 822 N N . LEU A 1 105 ? 16.883 -6.633 15.494 1.00 14.45 ? 105 LEU A N 1 ATOM 823 C CA . LEU A 1 105 ? 15.792 -6.220 14.612 1.00 14.27 ? 105 LEU A CA 1 ATOM 824 C C . LEU A 1 105 ? 15.925 -6.841 13.250 1.00 14.73 ? 105 LEU A C 1 ATOM 825 O O . LEU A 1 105 ? 17.043 -7.143 12.809 1.00 18.20 ? 105 LEU A O 1 ATOM 826 C CB . LEU A 1 105 ? 15.888 -4.691 14.420 1.00 12.70 ? 105 LEU A CB 1 ATOM 827 C CG . LEU A 1 105 ? 15.718 -3.979 15.738 1.00 14.93 ? 105 LEU A CG 1 ATOM 828 C CD1 . LEU A 1 105 ? 16.098 -2.477 15.594 1.00 17.95 ? 105 LEU A CD1 1 ATOM 829 C CD2 . LEU A 1 105 ? 14.214 -4.130 16.330 1.00 17.43 ? 105 LEU A CD2 1 ATOM 830 N N . PRO A 1 106 ? 14.837 -6.978 12.506 1.00 14.63 ? 106 PRO A N 1 ATOM 831 C CA . PRO A 1 106 ? 14.903 -7.761 11.246 1.00 16.17 ? 106 PRO A CA 1 ATOM 832 C C . PRO A 1 106 ? 15.210 -6.816 10.032 1.00 18.79 ? 106 PRO A C 1 ATOM 833 O O . PRO A 1 106 ? 14.659 -6.952 8.891 1.00 20.80 ? 106 PRO A O 1 ATOM 834 C CB . PRO A 1 106 ? 13.491 -8.387 11.142 1.00 16.10 ? 106 PRO A CB 1 ATOM 835 C CG . PRO A 1 106 ? 12.597 -7.351 11.815 1.00 16.31 ? 106 PRO A CG 1 ATOM 836 C CD . PRO A 1 106 ? 13.456 -6.843 13.033 1.00 16.31 ? 106 PRO A CD 1 ATOM 837 N N . TYR A 1 107 ? 16.115 -5.857 10.244 1.00 17.01 ? 107 TYR A N 1 ATOM 838 C CA . TYR A 1 107 ? 16.560 -4.967 9.210 1.00 15.92 ? 107 TYR A CA 1 ATOM 839 C C . TYR A 1 107 ? 17.811 -4.279 9.724 1.00 16.54 ? 107 TYR A C 1 ATOM 840 O O . TYR A 1 107 ? 18.066 -4.168 10.946 1.00 16.31 ? 107 TYR A O 1 ATOM 841 C CB . TYR A 1 107 ? 15.472 -3.873 8.810 1.00 18.07 ? 107 TYR A CB 1 ATOM 842 C CG . TYR A 1 107 ? 14.604 -3.447 9.986 1.00 14.33 ? 107 TYR A CG 1 ATOM 843 C CD1 . TYR A 1 107 ? 15.057 -2.498 10.953 1.00 15.33 ? 107 TYR A CD1 1 ATOM 844 C CD2 . TYR A 1 107 ? 13.261 -3.939 10.078 1.00 13.37 ? 107 TYR A CD2 1 ATOM 845 C CE1 . TYR A 1 107 ? 14.255 -2.162 12.062 1.00 15.83 ? 107 TYR A CE1 1 ATOM 846 C CE2 . TYR A 1 107 ? 12.407 -3.500 11.193 1.00 15.50 ? 107 TYR A CE2 1 ATOM 847 C CZ . TYR A 1 107 ? 12.899 -2.626 12.117 1.00 15.45 ? 107 TYR A CZ 1 ATOM 848 O OH . TYR A 1 107 ? 12.176 -2.231 13.183 1.00 15.32 ? 107 TYR A OH 1 ATOM 849 N N . SER A 1 108 ? 18.596 -3.846 8.745 1.00 16.76 ? 108 SER A N 1 ATOM 850 C CA . SER A 1 108 ? 19.686 -2.937 9.106 1.00 19.06 ? 108 SER A CA 1 ATOM 851 C C . SER A 1 108 ? 19.187 -1.490 9.342 1.00 19.60 ? 108 SER A C 1 ATOM 852 O O . SER A 1 108 ? 17.956 -1.189 9.130 1.00 19.80 ? 108 SER A O 1 ATOM 853 C CB . SER A 1 108 ? 20.717 -2.936 7.971 1.00 19.13 ? 108 SER A CB 1 ATOM 854 O OG . SER A 1 108 ? 20.111 -2.326 6.815 1.00 23.67 ? 108 SER A OG 1 ATOM 855 N N . GLY A 1 109 ? 20.117 -0.605 9.712 1.00 17.77 ? 109 GLY A N 1 ATOM 856 C CA . GLY A 1 109 ? 19.709 0.770 10.127 1.00 17.99 ? 109 GLY A CA 1 ATOM 857 C C . GLY A 1 109 ? 19.719 1.732 8.926 1.00 17.89 ? 109 GLY A C 1 ATOM 858 O O . GLY A 1 109 ? 19.500 2.938 9.060 1.00 23.45 ? 109 GLY A O 1 ATOM 859 N N . ASN A 1 110 ? 19.884 1.289 7.701 1.00 20.03 ? 110 ASN A N 1 ATOM 860 C CA . ASN A 1 110 ? 19.832 2.332 6.722 1.00 23.05 ? 110 ASN A CA 1 ATOM 861 C C . ASN A 1 110 ? 18.464 2.697 6.190 1.00 21.36 ? 110 ASN A C 1 ATOM 862 O O . ASN A 1 110 ? 17.479 1.942 6.360 1.00 20.21 ? 110 ASN A O 1 ATOM 863 C CB . ASN A 1 110 ? 20.707 2.078 5.621 1.00 25.30 ? 110 ASN A CB 1 ATOM 864 C CG . ASN A 1 110 ? 20.293 0.951 4.905 1.00 25.12 ? 110 ASN A CG 1 ATOM 865 O OD1 . ASN A 1 110 ? 19.519 1.043 3.885 1.00 33.88 ? 110 ASN A OD1 1 ATOM 866 N ND2 . ASN A 1 110 ? 20.867 -0.157 5.281 1.00 36.58 ? 110 ASN A ND2 1 ATOM 867 N N . TYR A 1 111 ? 18.378 3.944 5.691 1.00 19.57 ? 111 TYR A N 1 ATOM 868 C CA . TYR A 1 111 ? 17.094 4.497 5.380 1.00 18.85 ? 111 TYR A CA 1 ATOM 869 C C . TYR A 1 111 ? 16.319 3.642 4.370 1.00 20.17 ? 111 TYR A C 1 ATOM 870 O O . TYR A 1 111 ? 15.128 3.489 4.525 1.00 20.49 ? 111 TYR A O 1 ATOM 871 C CB . TYR A 1 111 ? 17.266 5.860 4.750 1.00 17.77 ? 111 TYR A CB 1 ATOM 872 C CG . TYR A 1 111 ? 17.463 6.961 5.773 1.00 17.03 ? 111 TYR A CG 1 ATOM 873 C CD1 . TYR A 1 111 ? 16.687 7.034 6.885 1.00 20.04 ? 111 TYR A CD1 1 ATOM 874 C CD2 . TYR A 1 111 ? 18.396 8.003 5.526 1.00 17.35 ? 111 TYR A CD2 1 ATOM 875 C CE1 . TYR A 1 111 ? 16.874 8.131 7.804 1.00 21.36 ? 111 TYR A CE1 1 ATOM 876 C CE2 . TYR A 1 111 ? 18.576 9.091 6.407 1.00 18.19 ? 111 TYR A CE2 1 ATOM 877 C CZ . TYR A 1 111 ? 17.837 9.152 7.522 1.00 17.16 ? 111 TYR A CZ 1 ATOM 878 O OH . TYR A 1 111 ? 17.977 10.217 8.401 1.00 17.33 ? 111 TYR A OH 1 ATOM 879 N N . GLU A 1 112 ? 16.981 3.133 3.345 1.00 21.15 ? 112 GLU A N 1 ATOM 880 C CA . GLU A 1 112 ? 16.311 2.280 2.387 1.00 23.49 ? 112 GLU A CA 1 ATOM 881 C C . GLU A 1 112 ? 15.650 1.044 3.088 1.00 20.54 ? 112 GLU A C 1 ATOM 882 O O . GLU A 1 112 ? 14.463 0.769 2.877 1.00 19.83 ? 112 GLU A O 1 ATOM 883 C CB . GLU A 1 112 ? 17.343 1.837 1.334 1.00 27.18 ? 112 GLU A CB 1 ATOM 884 C CG . GLU A 1 112 ? 16.843 0.633 0.425 1.00 35.96 ? 112 GLU A CG 1 ATOM 885 C CD . GLU A 1 112 ? 17.985 -0.146 -0.400 1.00 49.50 ? 112 GLU A CD 1 ATOM 886 O OE1 . GLU A 1 112 ? 19.233 0.020 -0.145 1.00 51.59 ? 112 GLU A OE1 1 ATOM 887 O OE2 . GLU A 1 112 ? 17.601 -0.991 -1.272 1.00 51.09 ? 112 GLU A OE2 1 ATOM 888 N N . ARG A 1 113 ? 16.398 0.339 3.920 1.00 21.17 ? 113 ARG A N 1 ATOM 889 C CA . ARG A 1 113 ? 15.827 -0.855 4.562 1.00 21.02 ? 113 ARG A CA 1 ATOM 890 C C . ARG A 1 113 ? 14.750 -0.508 5.552 1.00 20.07 ? 113 ARG A C 1 ATOM 891 O O . ARG A 1 113 ? 13.749 -1.234 5.663 1.00 20.56 ? 113 ARG A O 1 ATOM 892 C CB . ARG A 1 113 ? 16.887 -1.691 5.282 1.00 22.93 ? 113 ARG A CB 1 ATOM 893 C CG . ARG A 1 113 ? 17.964 -2.244 4.319 1.00 25.36 ? 113 ARG A CG 1 ATOM 894 C CD . ARG A 1 113 ? 17.272 -3.173 3.282 1.00 31.05 ? 113 ARG A CD 1 ATOM 895 N NE . ARG A 1 113 ? 18.296 -3.767 2.442 1.00 46.51 ? 113 ARG A NE 1 ATOM 896 C CZ . ARG A 1 113 ? 18.051 -4.638 1.458 1.00 52.78 ? 113 ARG A CZ 1 ATOM 897 N NH1 . ARG A 1 113 ? 16.784 -4.992 1.160 1.00 54.13 ? 113 ARG A NH1 1 ATOM 898 N NH2 . ARG A 1 113 ? 19.079 -5.139 0.762 1.00 53.47 ? 113 ARG A NH2 1 ATOM 899 N N . LEU A 1 114 ? 14.960 0.586 6.321 1.00 18.34 ? 114 LEU A N 1 ATOM 900 C CA . LEU A 1 114 ? 13.903 0.951 7.277 1.00 14.64 ? 114 LEU A CA 1 ATOM 901 C C . LEU A 1 114 ? 12.646 1.369 6.590 1.00 16.59 ? 114 LEU A C 1 ATOM 902 O O . LEU A 1 114 ? 11.586 1.093 7.091 1.00 17.03 ? 114 LEU A O 1 ATOM 903 C CB . LEU A 1 114 ? 14.414 2.143 8.159 1.00 15.60 ? 114 LEU A CB 1 ATOM 904 C CG . LEU A 1 114 ? 15.458 1.746 9.170 1.00 15.87 ? 114 LEU A CG 1 ATOM 905 C CD1 . LEU A 1 114 ? 16.023 3.093 9.715 1.00 17.35 ? 114 LEU A CD1 1 ATOM 906 C CD2 . LEU A 1 114 ? 14.763 1.020 10.317 1.00 18.40 ? 114 LEU A CD2 1 ATOM 907 N N . GLN A 1 115 ? 12.724 2.112 5.486 1.00 17.95 ? 115 GLN A N 1 ATOM 908 C CA . GLN A 1 115 ? 11.535 2.521 4.769 1.00 15.75 ? 115 GLN A CA 1 ATOM 909 C C . GLN A 1 115 ? 10.842 1.311 4.184 1.00 19.27 ? 115 GLN A C 1 ATOM 910 O O . GLN A 1 115 ? 9.593 1.314 4.155 1.00 19.18 ? 115 GLN A O 1 ATOM 911 C CB . GLN A 1 115 ? 11.916 3.405 3.602 1.00 17.35 ? 115 GLN A CB 1 ATOM 912 C CG . GLN A 1 115 ? 12.330 4.841 4.125 1.00 16.27 ? 115 GLN A CG 1 ATOM 913 C CD . GLN A 1 115 ? 12.856 5.825 3.016 1.00 19.78 ? 115 GLN A CD 1 ATOM 914 O OE1 . GLN A 1 115 ? 13.062 7.007 3.324 1.00 20.03 ? 115 GLN A OE1 1 ATOM 915 N NE2 . GLN A 1 115 ? 12.860 5.445 1.743 1.00 26.82 ? 115 GLN A NE2 1 ATOM 916 N N . ILE A 1 116 ? 11.584 0.302 3.708 1.00 17.11 ? 116 ILE A N 1 ATOM 917 C CA . ILE A 1 116 ? 10.932 -0.916 3.226 1.00 19.49 ? 116 ILE A CA 1 ATOM 918 C C . ILE A 1 116 ? 10.119 -1.590 4.382 1.00 19.03 ? 116 ILE A C 1 ATOM 919 O O . ILE A 1 116 ? 8.943 -1.987 4.219 1.00 18.77 ? 116 ILE A O 1 ATOM 920 C CB . ILE A 1 116 ? 11.992 -1.837 2.599 1.00 20.10 ? 116 ILE A CB 1 ATOM 921 C CG1 . ILE A 1 116 ? 12.440 -1.281 1.223 1.00 22.70 ? 116 ILE A CG1 1 ATOM 922 C CG2 . ILE A 1 116 ? 11.400 -3.312 2.412 1.00 21.68 ? 116 ILE A CG2 1 ATOM 923 C CD1 . ILE A 1 116 ? 13.705 -2.003 0.598 1.00 22.89 ? 116 ILE A CD1 1 ATOM 924 N N . ALA A 1 117 ? 10.778 -1.706 5.574 1.00 17.86 ? 117 ALA A N 1 ATOM 925 C CA . ALA A 1 117 ? 10.131 -2.290 6.764 1.00 17.20 ? 117 ALA A CA 1 ATOM 926 C C . ALA A 1 117 ? 8.934 -1.520 7.190 1.00 18.69 ? 117 ALA A C 1 ATOM 927 O O . ALA A 1 117 ? 7.942 -2.088 7.562 1.00 19.86 ? 117 ALA A O 1 ATOM 928 C CB . ALA A 1 117 ? 11.116 -2.462 7.878 1.00 16.92 ? 117 ALA A CB 1 ATOM 929 N N . ALA A 1 118 ? 8.994 -0.186 7.104 1.00 17.65 ? 118 ALA A N 1 ATOM 930 C CA . ALA A 1 118 ? 7.903 0.667 7.560 1.00 18.50 ? 118 ALA A CA 1 ATOM 931 C C . ALA A 1 118 ? 6.776 0.711 6.551 1.00 20.67 ? 118 ALA A C 1 ATOM 932 O O . ALA A 1 118 ? 5.641 1.110 6.888 1.00 21.81 ? 118 ALA A O 1 ATOM 933 C CB . ALA A 1 118 ? 8.435 2.105 7.844 1.00 18.09 ? 118 ALA A CB 1 ATOM 934 N N . GLY A 1 119 ? 7.062 0.379 5.320 1.00 20.96 ? 119 GLY A N 1 ATOM 935 C CA . GLY A 1 119 ? 6.017 0.447 4.311 1.00 21.81 ? 119 GLY A CA 1 ATOM 936 C C . GLY A 1 119 ? 5.853 1.827 3.691 1.00 23.60 ? 119 GLY A C 1 ATOM 937 O O . GLY A 1 119 ? 4.861 2.073 2.950 1.00 24.80 ? 119 GLY A O 1 ATOM 938 N N . LYS A 1 120 ? 6.761 2.762 3.988 1.00 22.12 ? 120 LYS A N 1 ATOM 939 C CA . LYS A 1 120 ? 6.573 4.115 3.478 1.00 23.49 ? 120 LYS A CA 1 ATOM 940 C C . LYS A 1 120 ? 7.912 4.877 3.501 1.00 22.13 ? 120 LYS A C 1 ATOM 941 O O . LYS A 1 120 ? 8.796 4.545 4.303 1.00 20.20 ? 120 LYS A O 1 ATOM 942 C CB . LYS A 1 120 ? 5.498 4.849 4.274 1.00 24.05 ? 120 LYS A CB 1 ATOM 943 C CG . LYS A 1 120 ? 5.812 5.007 5.686 1.00 26.48 ? 120 LYS A CG 1 ATOM 944 C CD . LYS A 1 120 ? 4.574 5.360 6.546 1.00 32.57 ? 120 LYS A CD 1 ATOM 945 C CE . LYS A 1 120 ? 3.365 5.637 5.741 1.00 37.67 ? 120 LYS A CE 1 ATOM 946 N NZ . LYS A 1 120 ? 2.303 6.094 6.719 1.00 44.87 ? 120 LYS A NZ 1 ATOM 947 N N . PRO A 1 121 ? 8.070 5.823 2.551 1.00 22.30 ? 121 PRO A N 1 ATOM 948 C CA . PRO A 1 121 ? 9.343 6.572 2.513 1.00 22.38 ? 121 PRO A CA 1 ATOM 949 C C . PRO A 1 121 ? 9.292 7.595 3.595 1.00 21.64 ? 121 PRO A C 1 ATOM 950 O O . PRO A 1 121 ? 8.175 8.029 4.045 1.00 24.04 ? 121 PRO A O 1 ATOM 951 C CB . PRO A 1 121 ? 9.312 7.277 1.125 1.00 22.08 ? 121 PRO A CB 1 ATOM 952 C CG . PRO A 1 121 ? 7.900 7.341 0.738 1.00 22.98 ? 121 PRO A CG 1 ATOM 953 C CD . PRO A 1 121 ? 7.180 6.169 1.421 1.00 24.08 ? 121 PRO A CD 1 ATOM 954 N N . ARG A 1 122 ? 10.454 8.113 3.909 1.00 22.53 ? 122 ARG A N 1 ATOM 955 C CA . ARG A 1 122 ? 10.358 9.103 4.902 1.00 23.09 ? 122 ARG A CA 1 ATOM 956 C C . ARG A 1 122 ? 9.762 10.446 4.487 1.00 22.37 ? 122 ARG A C 1 ATOM 957 O O . ARG A 1 122 ? 9.386 11.249 5.383 1.00 22.42 ? 122 ARG A O 1 ATOM 958 C CB . ARG A 1 122 ? 11.519 9.038 5.845 1.00 27.88 ? 122 ARG A CB 1 ATOM 959 C CG . ARG A 1 122 ? 12.596 9.746 5.201 1.00 21.10 ? 122 ARG A CG 1 ATOM 960 C CD . ARG A 1 122 ? 13.782 9.189 5.767 1.00 19.94 ? 122 ARG A CD 1 ATOM 961 N NE . ARG A 1 122 ? 14.876 9.971 5.212 1.00 22.82 ? 122 ARG A NE 1 ATOM 962 C CZ . ARG A 1 122 ? 15.556 9.682 4.069 1.00 24.73 ? 122 ARG A CZ 1 ATOM 963 N NH1 . ARG A 1 122 ? 15.194 8.719 3.317 1.00 32.00 ? 122 ARG A NH1 1 ATOM 964 N NH2 . ARG A 1 122 ? 16.576 10.519 3.655 1.00 19.48 ? 122 ARG A NH2 1 ATOM 965 N N . GLU A 1 123 ? 9.617 10.681 3.182 1.00 21.93 ? 123 GLU A N 1 ATOM 966 C CA . GLU A 1 123 ? 8.848 11.854 2.672 1.00 22.52 ? 123 GLU A CA 1 ATOM 967 C C . GLU A 1 123 ? 7.430 11.903 3.215 1.00 19.89 ? 123 GLU A C 1 ATOM 968 O O . GLU A 1 123 ? 6.783 12.973 3.228 1.00 21.75 ? 123 GLU A O 1 ATOM 969 C CB . GLU A 1 123 ? 8.705 11.835 1.153 1.00 24.32 ? 123 GLU A CB 1 ATOM 970 C CG . GLU A 1 123 ? 9.990 12.224 0.459 1.00 26.22 ? 123 GLU A CG 1 ATOM 971 C CD . GLU A 1 123 ? 11.040 11.135 0.334 1.00 28.48 ? 123 GLU A CD 1 ATOM 972 O OE1 . GLU A 1 123 ? 11.073 10.033 0.974 1.00 27.88 ? 123 GLU A OE1 1 ATOM 973 O OE2 . GLU A 1 123 ? 11.971 11.416 -0.436 1.00 36.60 ? 123 GLU A OE2 1 ATOM 974 N N . LYS A 1 124 ? 6.891 10.754 3.584 1.00 20.15 ? 124 LYS A N 1 ATOM 975 C CA . LYS A 1 124 ? 5.504 10.663 4.033 1.00 20.74 ? 124 LYS A CA 1 ATOM 976 C C . LYS A 1 124 ? 5.320 10.486 5.523 1.00 19.73 ? 124 LYS A C 1 ATOM 977 O O . LYS A 1 124 ? 4.172 10.326 5.981 1.00 20.83 ? 124 LYS A O 1 ATOM 978 C CB . LYS A 1 124 ? 4.778 9.489 3.268 1.00 20.96 ? 124 LYS A CB 1 ATOM 979 C CG . LYS A 1 124 ? 4.736 9.759 1.741 1.00 24.01 ? 124 LYS A CG 1 ATOM 980 C CD . LYS A 1 124 ? 3.341 9.713 1.141 1.00 40.45 ? 124 LYS A CD 1 ATOM 981 C CE . LYS A 1 124 ? 3.180 8.792 -0.146 1.00 42.87 ? 124 LYS A CE 1 ATOM 982 N NZ . LYS A 1 124 ? 4.154 9.031 -1.303 1.00 50.45 ? 124 LYS A NZ 1 ATOM 983 N N . ILE A 1 125 ? 6.402 10.565 6.335 1.00 17.51 ? 125 ILE A N 1 ATOM 984 C CA . ILE A 1 125 ? 6.276 10.317 7.749 1.00 15.94 ? 125 ILE A CA 1 ATOM 985 C C . ILE A 1 125 ? 6.499 11.651 8.491 1.00 16.42 ? 125 ILE A C 1 ATOM 986 O O . ILE A 1 125 ? 7.624 12.244 8.416 1.00 16.18 ? 125 ILE A O 1 ATOM 987 C CB . ILE A 1 125 ? 7.377 9.316 8.213 1.00 18.24 ? 125 ILE A CB 1 ATOM 988 C CG1 . ILE A 1 125 ? 7.144 7.961 7.535 1.00 18.92 ? 125 ILE A CG1 1 ATOM 989 C CG2 . ILE A 1 125 ? 7.384 9.111 9.759 1.00 17.30 ? 125 ILE A CG2 1 ATOM 990 C CD1 . ILE A 1 125 ? 8.307 6.874 7.842 1.00 20.63 ? 125 ILE A CD1 1 ATOM 991 N N . PRO A 1 126 ? 5.466 12.150 9.169 1.00 16.07 ? 126 PRO A N 1 ATOM 992 C CA . PRO A 1 126 ? 5.691 13.384 9.902 1.00 15.51 ? 126 PRO A CA 1 ATOM 993 C C . PRO A 1 126 ? 6.772 13.241 10.959 1.00 15.08 ? 126 PRO A C 1 ATOM 994 O O . PRO A 1 126 ? 6.926 12.176 11.647 1.00 16.80 ? 126 PRO A O 1 ATOM 995 C CB . PRO A 1 126 ? 4.316 13.645 10.601 1.00 16.10 ? 126 PRO A CB 1 ATOM 996 C CG . PRO A 1 126 ? 3.380 12.849 9.634 1.00 15.65 ? 126 PRO A CG 1 ATOM 997 C CD . PRO A 1 126 ? 4.057 11.605 9.386 1.00 15.78 ? 126 PRO A CD 1 ATOM 998 N N . ILE A 1 127 ? 7.503 14.352 11.146 1.00 15.14 ? 127 ILE A N 1 ATOM 999 C CA . ILE A 1 127 ? 8.473 14.455 12.230 1.00 13.54 ? 127 ILE A CA 1 ATOM 1000 C C . ILE A 1 127 ? 8.260 15.698 13.006 1.00 14.12 ? 127 ILE A C 1 ATOM 1001 O O . ILE A 1 127 ? 7.501 16.587 12.608 1.00 15.31 ? 127 ILE A O 1 ATOM 1002 C CB . ILE A 1 127 ? 9.990 14.383 11.744 1.00 14.68 ? 127 ILE A CB 1 ATOM 1003 C CG1 . ILE A 1 127 ? 10.237 15.515 10.781 1.00 16.07 ? 127 ILE A CG1 1 ATOM 1004 C CG2 . ILE A 1 127 ? 10.212 13.093 10.955 1.00 16.30 ? 127 ILE A CG2 1 ATOM 1005 C CD1 . ILE A 1 127 ? 11.697 15.513 10.128 1.00 19.05 ? 127 ILE A CD1 1 ATOM 1006 N N . GLY A 1 128 ? 8.881 15.721 14.158 1.00 13.84 ? 128 GLY A N 1 ATOM 1007 C CA . GLY A 1 128 ? 8.614 16.821 15.139 1.00 14.52 ? 128 GLY A CA 1 ATOM 1008 C C . GLY A 1 128 ? 8.832 16.266 16.526 1.00 15.47 ? 128 GLY A C 1 ATOM 1009 O O . GLY A 1 128 ? 9.123 15.079 16.724 1.00 15.17 ? 128 GLY A O 1 ATOM 1010 N N . LEU A 1 129 ? 8.589 17.118 17.530 1.00 14.02 ? 129 LEU A N 1 ATOM 1011 C CA . LEU A 1 129 ? 8.617 16.686 18.931 1.00 14.74 ? 129 LEU A CA 1 ATOM 1012 C C . LEU A 1 129 ? 7.460 15.707 19.272 1.00 14.97 ? 129 LEU A C 1 ATOM 1013 O O . LEU A 1 129 ? 7.734 14.730 19.898 1.00 15.04 ? 129 LEU A O 1 ATOM 1014 C CB . LEU A 1 129 ? 8.751 17.857 19.967 1.00 15.37 ? 129 LEU A CB 1 ATOM 1015 C CG . LEU A 1 129 ? 10.091 18.631 19.739 1.00 15.12 ? 129 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 129 ? 10.162 19.697 20.824 1.00 16.72 ? 129 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 129 ? 11.345 17.678 19.762 1.00 16.33 ? 129 LEU A CD2 1 ATOM 1018 N N . PRO A 1 130 ? 6.259 15.978 18.824 1.00 15.08 ? 130 PRO A N 1 ATOM 1019 C CA . PRO A 1 130 ? 5.256 14.934 19.173 1.00 14.00 ? 130 PRO A CA 1 ATOM 1020 C C . PRO A 1 130 ? 5.581 13.569 18.535 1.00 14.76 ? 130 PRO A C 1 ATOM 1021 O O . PRO A 1 130 ? 5.375 12.540 19.141 1.00 14.17 ? 130 PRO A O 1 ATOM 1022 C CB . PRO A 1 130 ? 3.951 15.518 18.515 1.00 13.75 ? 130 PRO A CB 1 ATOM 1023 C CG . PRO A 1 130 ? 4.176 17.131 18.634 1.00 14.77 ? 130 PRO A CG 1 ATOM 1024 C CD . PRO A 1 130 ? 5.663 17.226 18.257 1.00 13.52 ? 130 PRO A CD 1 ATOM 1025 N N . ALA A 1 131 ? 6.118 13.602 17.330 1.00 13.58 ? 131 ALA A N 1 ATOM 1026 C CA . ALA A 1 131 ? 6.425 12.320 16.603 1.00 13.52 ? 131 ALA A CA 1 ATOM 1027 C C . ALA A 1 131 ? 7.545 11.619 17.413 1.00 15.30 ? 131 ALA A C 1 ATOM 1028 O O . ALA A 1 131 ? 7.557 10.396 17.487 1.00 13.22 ? 131 ALA A O 1 ATOM 1029 C CB . ALA A 1 131 ? 6.867 12.594 15.161 1.00 14.10 ? 131 ALA A CB 1 ATOM 1030 N N . LEU A 1 132 ? 8.508 12.386 17.923 1.00 13.95 ? 132 LEU A N 1 ATOM 1031 C CA . LEU A 1 132 ? 9.582 11.751 18.749 1.00 12.65 ? 132 LEU A CA 1 ATOM 1032 C C . LEU A 1 132 ? 9.032 11.156 20.024 1.00 13.99 ? 132 LEU A C 1 ATOM 1033 O O . LEU A 1 132 ? 9.428 10.052 20.400 1.00 14.24 ? 132 LEU A O 1 ATOM 1034 C CB . LEU A 1 132 ? 10.657 12.785 19.087 1.00 13.60 ? 132 LEU A CB 1 ATOM 1035 C CG . LEU A 1 132 ? 11.832 12.249 19.906 1.00 14.87 ? 132 LEU A CG 1 ATOM 1036 C CD1 . LEU A 1 132 ? 12.494 11.049 19.254 1.00 13.77 ? 132 LEU A CD1 1 ATOM 1037 C CD2 . LEU A 1 132 ? 12.856 13.428 20.097 1.00 16.98 ? 132 LEU A CD2 1 ATOM 1038 N N . ASP A 1 133 ? 8.112 11.854 20.665 1.00 13.25 ? 133 ASP A N 1 ATOM 1039 C CA . ASP A 1 133 ? 7.422 11.268 21.831 1.00 14.53 ? 133 ASP A CA 1 ATOM 1040 C C . ASP A 1 133 ? 6.739 9.909 21.435 1.00 12.81 ? 133 ASP A C 1 ATOM 1041 O O . ASP A 1 133 ? 6.899 8.879 22.168 1.00 13.66 ? 133 ASP A O 1 ATOM 1042 C CB . ASP A 1 133 ? 6.362 12.282 22.336 1.00 14.66 ? 133 ASP A CB 1 ATOM 1043 C CG . ASP A 1 133 ? 5.714 11.875 23.622 1.00 21.07 ? 133 ASP A CG 1 ATOM 1044 O OD1 . ASP A 1 133 ? 6.277 11.154 24.477 1.00 18.21 ? 133 ASP A OD1 1 ATOM 1045 O OD2 . ASP A 1 133 ? 4.619 12.395 23.821 1.00 21.94 ? 133 ASP A OD2 1 ATOM 1046 N N . THR A 1 134 ? 6.032 9.937 20.292 1.00 13.25 ? 134 THR A N 1 ATOM 1047 C CA . THR A 1 134 ? 5.395 8.659 19.821 1.00 15.86 ? 134 THR A CA 1 ATOM 1048 C C . THR A 1 134 ? 6.458 7.604 19.557 1.00 16.06 ? 134 THR A C 1 ATOM 1049 O O . THR A 1 134 ? 6.243 6.419 19.837 1.00 14.17 ? 134 THR A O 1 ATOM 1050 C CB . THR A 1 134 ? 4.623 8.870 18.475 1.00 18.63 ? 134 THR A CB 1 ATOM 1051 O OG1 . THR A 1 134 ? 3.630 9.824 18.625 1.00 30.40 ? 134 THR A OG1 1 ATOM 1052 C CG2 . THR A 1 134 ? 3.904 7.750 18.121 1.00 16.63 ? 134 THR A CG2 1 ATOM 1053 N N . ALA A 1 135 ? 7.602 8.026 18.997 1.00 13.27 ? 135 ALA A N 1 ATOM 1054 C CA . ALA A 1 135 ? 8.628 7.010 18.587 1.00 15.20 ? 135 ALA A CA 1 ATOM 1055 C C . ALA A 1 135 ? 9.213 6.329 19.816 1.00 14.51 ? 135 ALA A C 1 ATOM 1056 O O . ALA A 1 135 ? 9.377 5.079 19.858 1.00 13.82 ? 135 ALA A O 1 ATOM 1057 C CB . ALA A 1 135 ? 9.810 7.705 17.846 1.00 16.04 ? 135 ALA A CB 1 ATOM 1058 N N . ILE A 1 136 ? 9.494 7.129 20.843 1.00 14.00 ? 136 ILE A N 1 ATOM 1059 C CA . ILE A 1 136 ? 10.048 6.547 22.067 1.00 15.06 ? 136 ILE A CA 1 ATOM 1060 C C . ILE A 1 136 ? 9.050 5.568 22.624 1.00 15.47 ? 136 ILE A C 1 ATOM 1061 O O . ILE A 1 136 ? 9.388 4.439 23.043 1.00 14.59 ? 136 ILE A O 1 ATOM 1062 C CB . ILE A 1 136 ? 10.289 7.666 23.140 1.00 13.01 ? 136 ILE A CB 1 ATOM 1063 C CG1 . ILE A 1 136 ? 11.396 8.562 22.617 1.00 14.76 ? 136 ILE A CG1 1 ATOM 1064 C CG2 . ILE A 1 136 ? 10.696 7.081 24.512 1.00 17.67 ? 136 ILE A CG2 1 ATOM 1065 C CD1 . ILE A 1 136 ? 11.503 9.929 23.331 1.00 14.46 ? 136 ILE A CD1 1 ATOM 1066 N N . SER A 1 137 ? 7.789 5.976 22.628 1.00 15.75 ? 137 SER A N 1 ATOM 1067 C CA . SER A 1 137 ? 6.765 5.103 23.141 1.00 16.25 ? 137 SER A CA 1 ATOM 1068 C C . SER A 1 137 ? 6.661 3.770 22.399 1.00 14.38 ? 137 SER A C 1 ATOM 1069 O O . SER A 1 137 ? 6.451 2.663 23.036 1.00 16.49 ? 137 SER A O 1 ATOM 1070 C CB . SER A 1 137 ? 5.405 5.830 23.133 1.00 17.51 ? 137 SER A CB 1 ATOM 1071 O OG . SER A 1 137 ? 5.551 6.911 24.054 1.00 20.44 ? 137 SER A OG 1 ATOM 1072 N N . THR A 1 138 ? 6.698 3.847 21.076 1.00 13.45 ? 138 THR A N 1 ATOM 1073 C CA . THR A 1 138 ? 6.614 2.696 20.216 1.00 13.00 ? 138 THR A CA 1 ATOM 1074 C C . THR A 1 138 ? 7.750 1.741 20.606 1.00 14.90 ? 138 THR A C 1 ATOM 1075 O O . THR A 1 138 ? 7.572 0.494 20.648 1.00 16.27 ? 138 THR A O 1 ATOM 1076 C CB . THR A 1 138 ? 6.679 3.093 18.732 1.00 14.28 ? 138 THR A CB 1 ATOM 1077 O OG1 . THR A 1 138 ? 5.324 3.669 18.467 1.00 15.68 ? 138 THR A OG1 1 ATOM 1078 C CG2 . THR A 1 138 ? 6.917 1.880 17.786 1.00 15.78 ? 138 THR A CG2 1 ATOM 1079 N N . LEU A 1 139 ? 8.954 2.327 20.769 1.00 13.65 ? 139 LEU A N 1 ATOM 1080 C CA . LEU A 1 139 ? 10.116 1.443 20.966 1.00 13.61 ? 139 LEU A CA 1 ATOM 1081 C C . LEU A 1 139 ? 10.135 0.768 22.299 1.00 15.26 ? 139 LEU A C 1 ATOM 1082 O O . LEU A 1 139 ? 10.865 -0.239 22.497 1.00 17.27 ? 139 LEU A O 1 ATOM 1083 C CB . LEU A 1 139 ? 11.413 2.268 20.692 1.00 15.04 ? 139 LEU A CB 1 ATOM 1084 C CG . LEU A 1 139 ? 11.539 2.783 19.302 1.00 15.15 ? 139 LEU A CG 1 ATOM 1085 C CD1 . LEU A 1 139 ? 12.877 3.682 19.205 1.00 17.79 ? 139 LEU A CD1 1 ATOM 1086 C CD2 . LEU A 1 139 ? 11.560 1.666 18.183 1.00 13.81 ? 139 LEU A CD2 1 ATOM 1087 N N . LEU A 1 140 ? 9.260 1.198 23.246 1.00 13.75 ? 140 LEU A N 1 ATOM 1088 C CA . LEU A 1 140 ? 9.239 0.544 24.565 1.00 16.63 ? 140 LEU A CA 1 ATOM 1089 C C . LEU A 1 140 ? 8.792 -0.898 24.459 1.00 20.61 ? 140 LEU A C 1 ATOM 1090 O O . LEU A 1 140 ? 9.208 -1.687 25.355 1.00 22.75 ? 140 LEU A O 1 ATOM 1091 C CB . LEU A 1 140 ? 8.268 1.270 25.506 1.00 16.87 ? 140 LEU A CB 1 ATOM 1092 C CG . LEU A 1 140 ? 8.679 2.718 25.825 1.00 24.07 ? 140 LEU A CG 1 ATOM 1093 C CD1 . LEU A 1 140 ? 7.447 3.390 26.537 1.00 23.15 ? 140 LEU A CD1 1 ATOM 1094 C CD2 . LEU A 1 140 ? 9.824 2.818 26.785 1.00 28.44 ? 140 LEU A CD2 1 ATOM 1095 N N . HIS A 1 141 ? 7.982 -1.219 23.438 1.00 20.37 ? 141 HIS A N 1 ATOM 1096 C CA . HIS A 1 141 ? 7.573 -2.620 23.321 1.00 22.88 ? 141 HIS A CA 1 ATOM 1097 C C . HIS A 1 141 ? 7.718 -3.098 21.911 1.00 21.22 ? 141 HIS A C 1 ATOM 1098 O O . HIS A 1 141 ? 7.281 -2.454 20.984 1.00 24.60 ? 141 HIS A O 1 ATOM 1099 C CB . HIS A 1 141 ? 6.114 -2.749 23.672 1.00 24.94 ? 141 HIS A CB 1 ATOM 1100 C CG . HIS A 1 141 ? 5.851 -2.404 25.103 1.00 30.23 ? 141 HIS A CG 1 ATOM 1101 N ND1 . HIS A 1 141 ? 5.238 -1.222 25.467 1.00 36.95 ? 141 HIS A ND1 1 ATOM 1102 C CD2 . HIS A 1 141 ? 6.228 -3.020 26.255 1.00 33.80 ? 141 HIS A CD2 1 ATOM 1103 C CE1 . HIS A 1 141 ? 5.200 -1.142 26.789 1.00 35.53 ? 141 HIS A CE1 1 ATOM 1104 N NE2 . HIS A 1 141 ? 5.804 -2.208 27.292 1.00 34.61 ? 141 HIS A NE2 1 ATOM 1105 N N . TYR A 1 142 ? 8.220 -4.288 21.800 1.00 17.65 ? 142 TYR A N 1 ATOM 1106 C CA . TYR A 1 142 ? 8.672 -4.707 20.506 1.00 16.40 ? 142 TYR A CA 1 ATOM 1107 C C . TYR A 1 142 ? 7.532 -4.868 19.502 1.00 18.95 ? 142 TYR A C 1 ATOM 1108 O O . TYR A 1 142 ? 6.552 -5.631 19.713 1.00 16.95 ? 142 TYR A O 1 ATOM 1109 C CB . TYR A 1 142 ? 9.445 -5.992 20.661 1.00 16.49 ? 142 TYR A CB 1 ATOM 1110 C CG . TYR A 1 142 ? 9.915 -6.556 19.331 1.00 14.53 ? 142 TYR A CG 1 ATOM 1111 C CD1 . TYR A 1 142 ? 10.803 -5.827 18.487 1.00 15.59 ? 142 TYR A CD1 1 ATOM 1112 C CD2 . TYR A 1 142 ? 9.536 -7.840 18.911 1.00 14.42 ? 142 TYR A CD2 1 ATOM 1113 C CE1 . TYR A 1 142 ? 11.295 -6.359 17.281 1.00 14.39 ? 142 TYR A CE1 1 ATOM 1114 C CE2 . TYR A 1 142 ? 9.948 -8.303 17.708 1.00 14.97 ? 142 TYR A CE2 1 ATOM 1115 C CZ . TYR A 1 142 ? 10.877 -7.578 16.853 1.00 13.10 ? 142 TYR A CZ 1 ATOM 1116 O OH . TYR A 1 142 ? 11.296 -8.158 15.701 1.00 15.96 ? 142 TYR A OH 1 ATOM 1117 N N . ASP A 1 143 ? 7.684 -4.238 18.352 1.00 15.66 ? 143 ASP A N 1 ATOM 1118 C CA . ASP A 1 143 ? 6.850 -4.435 17.191 1.00 15.11 ? 143 ASP A CA 1 ATOM 1119 C C . ASP A 1 143 ? 7.677 -4.004 16.004 1.00 16.24 ? 143 ASP A C 1 ATOM 1120 O O . ASP A 1 143 ? 7.916 -2.805 15.772 1.00 16.71 ? 143 ASP A O 1 ATOM 1121 C CB . ASP A 1 143 ? 5.564 -3.621 17.343 1.00 17.34 ? 143 ASP A CB 1 ATOM 1122 C CG . ASP A 1 143 ? 4.678 -3.578 16.126 1.00 21.74 ? 143 ASP A CG 1 ATOM 1123 O OD1 . ASP A 1 143 ? 4.950 -3.666 14.918 1.00 19.79 ? 143 ASP A OD1 1 ATOM 1124 O OD2 . ASP A 1 143 ? 3.505 -3.195 16.472 1.00 31.16 ? 143 ASP A OD2 1 ATOM 1125 N N . SER A 1 144 ? 8.154 -4.965 15.205 1.00 15.58 ? 144 SER A N 1 ATOM 1126 C CA . SER A 1 144 ? 9.247 -4.556 14.266 1.00 15.95 ? 144 SER A CA 1 ATOM 1127 C C . SER A 1 144 ? 8.748 -3.605 13.160 1.00 16.32 ? 144 SER A C 1 ATOM 1128 O O . SER A 1 144 ? 9.540 -2.707 12.713 1.00 14.22 ? 144 SER A O 1 ATOM 1129 C CB . SER A 1 144 ? 9.990 -5.766 13.703 1.00 18.20 ? 144 SER A CB 1 ATOM 1130 O OG . SER A 1 144 ? 9.134 -6.470 12.786 1.00 18.12 ? 144 SER A OG 1 ATOM 1131 N N . THR A 1 145 ? 7.518 -3.803 12.642 1.00 15.24 ? 145 THR A N 1 ATOM 1132 C CA . THR A 1 145 ? 7.032 -2.892 11.629 1.00 15.93 ? 145 THR A CA 1 ATOM 1133 C C . THR A 1 145 ? 6.818 -1.461 12.174 1.00 14.60 ? 145 THR A C 1 ATOM 1134 O O . THR A 1 145 ? 7.252 -0.494 11.578 1.00 16.17 ? 145 THR A O 1 ATOM 1135 C CB . THR A 1 145 ? 5.670 -3.380 11.004 1.00 16.98 ? 145 THR A CB 1 ATOM 1136 O OG1 . THR A 1 145 ? 5.994 -4.624 10.400 1.00 19.30 ? 145 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 145 ? 5.163 -2.312 9.997 1.00 17.37 ? 145 THR A CG2 1 ATOM 1138 N N . ALA A 1 146 ? 6.242 -1.369 13.345 1.00 14.03 ? 146 ALA A N 1 ATOM 1139 C CA . ALA A 1 146 ? 6.003 -0.033 13.999 1.00 13.15 ? 146 ALA A CA 1 ATOM 1140 C C . ALA A 1 146 ? 7.385 0.585 14.329 1.00 15.21 ? 146 ALA A C 1 ATOM 1141 O O . ALA A 1 146 ? 7.589 1.790 14.204 1.00 15.62 ? 146 ALA A O 1 ATOM 1142 C CB . ALA A 1 146 ? 5.199 -0.209 15.296 1.00 13.54 ? 146 ALA A CB 1 ATOM 1143 N N . ALA A 1 147 ? 8.298 -0.280 14.832 1.00 13.56 ? 147 ALA A N 1 ATOM 1144 C CA . ALA A 1 147 ? 9.618 0.258 15.230 1.00 12.05 ? 147 ALA A CA 1 ATOM 1145 C C . ALA A 1 147 ? 10.339 0.874 14.031 1.00 13.30 ? 147 ALA A C 1 ATOM 1146 O O . ALA A 1 147 ? 11.142 1.808 14.222 1.00 13.02 ? 147 ALA A O 1 ATOM 1147 C CB . ALA A 1 147 ? 10.468 -0.850 15.837 1.00 13.97 ? 147 ALA A CB 1 ATOM 1148 N N . ALA A 1 148 ? 10.179 0.351 12.789 1.00 13.99 ? 148 ALA A N 1 ATOM 1149 C CA . ALA A 1 148 ? 10.935 0.910 11.677 1.00 13.97 ? 148 ALA A CA 1 ATOM 1150 C C . ALA A 1 148 ? 10.529 2.397 11.494 1.00 14.47 ? 148 ALA A C 1 ATOM 1151 O O . ALA A 1 148 ? 11.390 3.250 11.243 1.00 13.75 ? 148 ALA A O 1 ATOM 1152 C CB . ALA A 1 148 ? 10.653 0.152 10.472 1.00 14.44 ? 148 ALA A CB 1 ATOM 1153 N N . GLY A 1 149 ? 9.231 2.695 11.505 1.00 13.41 ? 149 GLY A N 1 ATOM 1154 C CA . GLY A 1 149 ? 8.821 4.107 11.361 1.00 14.20 ? 149 GLY A CA 1 ATOM 1155 C C . GLY A 1 149 ? 9.307 4.930 12.567 1.00 15.24 ? 149 GLY A C 1 ATOM 1156 O O . GLY A 1 149 ? 9.780 6.059 12.381 1.00 14.41 ? 149 GLY A O 1 ATOM 1157 N N . ALA A 1 150 ? 9.232 4.391 13.775 1.00 12.97 ? 150 ALA A N 1 ATOM 1158 C CA . ALA A 1 150 ? 9.695 5.092 14.987 1.00 12.35 ? 150 ALA A CA 1 ATOM 1159 C C . ALA A 1 150 ? 11.193 5.423 14.775 1.00 13.30 ? 150 ALA A C 1 ATOM 1160 O O . ALA A 1 150 ? 11.615 6.469 15.143 1.00 14.39 ? 150 ALA A O 1 ATOM 1161 C CB . ALA A 1 150 ? 9.461 4.208 16.274 1.00 12.14 ? 150 ALA A CB 1 ATOM 1162 N N . LEU A 1 151 ? 11.980 4.443 14.321 1.00 13.62 ? 151 LEU A N 1 ATOM 1163 C CA . LEU A 1 151 ? 13.428 4.658 14.137 1.00 13.07 ? 151 LEU A CA 1 ATOM 1164 C C . LEU A 1 151 ? 13.696 5.680 13.013 1.00 15.26 ? 151 LEU A C 1 ATOM 1165 O O . LEU A 1 151 ? 14.636 6.479 13.202 1.00 14.60 ? 151 LEU A O 1 ATOM 1166 C CB . LEU A 1 151 ? 14.107 3.291 13.825 1.00 13.17 ? 151 LEU A CB 1 ATOM 1167 C CG . LEU A 1 151 ? 14.114 2.464 15.125 1.00 11.76 ? 151 LEU A CG 1 ATOM 1168 C CD1 . LEU A 1 151 ? 14.360 0.982 14.700 1.00 14.68 ? 151 LEU A CD1 1 ATOM 1169 C CD2 . LEU A 1 151 ? 15.186 2.927 16.061 1.00 16.04 ? 151 LEU A CD2 1 ATOM 1170 N N . LEU A 1 152 ? 12.871 5.763 11.942 1.00 13.04 ? 152 LEU A N 1 ATOM 1171 C CA . LEU A 1 152 ? 13.014 6.832 10.930 1.00 12.72 ? 152 LEU A CA 1 ATOM 1172 C C . LEU A 1 152 ? 12.778 8.151 11.623 1.00 13.89 ? 152 LEU A C 1 ATOM 1173 O O . LEU A 1 152 ? 13.546 9.124 11.329 1.00 13.92 ? 152 LEU A O 1 ATOM 1174 C CB . LEU A 1 152 ? 12.043 6.662 9.773 1.00 12.69 ? 152 LEU A CB 1 ATOM 1175 C CG . LEU A 1 152 ? 12.462 5.457 8.922 1.00 12.76 ? 152 LEU A CG 1 ATOM 1176 C CD1 . LEU A 1 152 ? 11.347 5.034 7.983 1.00 15.73 ? 152 LEU A CD1 1 ATOM 1177 C CD2 . LEU A 1 152 ? 13.715 5.839 8.141 1.00 13.91 ? 152 LEU A CD2 1 ATOM 1178 N N . VAL A 1 153 ? 11.784 8.271 12.567 1.00 12.18 ? 153 VAL A N 1 ATOM 1179 C CA . VAL A 1 153 ? 11.623 9.548 13.236 1.00 11.73 ? 153 VAL A CA 1 ATOM 1180 C C . VAL A 1 153 ? 12.785 9.796 14.184 1.00 13.12 ? 153 VAL A C 1 ATOM 1181 O O . VAL A 1 153 ? 13.286 10.949 14.217 1.00 14.49 ? 153 VAL A O 1 ATOM 1182 C CB . VAL A 1 153 ? 10.285 9.506 14.073 1.00 13.16 ? 153 VAL A CB 1 ATOM 1183 C CG1 . VAL A 1 153 ? 10.165 10.733 15.059 1.00 13.89 ? 153 VAL A CG1 1 ATOM 1184 C CG2 . VAL A 1 153 ? 9.108 9.370 13.111 1.00 13.48 ? 153 VAL A CG2 1 ATOM 1185 N N . LEU A 1 154 ? 13.198 8.788 14.985 1.00 12.48 ? 154 LEU A N 1 ATOM 1186 C CA . LEU A 1 154 ? 14.275 8.997 15.950 1.00 12.54 ? 154 LEU A CA 1 ATOM 1187 C C . LEU A 1 154 ? 15.618 9.448 15.243 1.00 13.69 ? 154 LEU A C 1 ATOM 1188 O O . LEU A 1 154 ? 16.287 10.394 15.760 1.00 13.95 ? 154 LEU A O 1 ATOM 1189 C CB . LEU A 1 154 ? 14.492 7.642 16.644 1.00 13.76 ? 154 LEU A CB 1 ATOM 1190 C CG . LEU A 1 154 ? 15.725 7.609 17.570 1.00 15.77 ? 154 LEU A CG 1 ATOM 1191 C CD1 . LEU A 1 154 ? 15.374 8.448 18.673 1.00 19.21 ? 154 LEU A CD1 1 ATOM 1192 C CD2 . LEU A 1 154 ? 15.808 6.116 18.099 1.00 21.11 ? 154 LEU A CD2 1 ATOM 1193 N N . ILE A 1 155 ? 15.956 8.769 14.126 1.00 12.64 ? 155 ILE A N 1 ATOM 1194 C CA . ILE A 1 155 ? 17.265 9.093 13.469 1.00 13.20 ? 155 ILE A CA 1 ATOM 1195 C C . ILE A 1 155 ? 17.228 10.567 13.006 1.00 15.31 ? 155 ILE A C 1 ATOM 1196 O O . ILE A 1 155 ? 18.226 11.314 13.201 1.00 15.11 ? 155 ILE A O 1 ATOM 1197 C CB . ILE A 1 155 ? 17.516 8.186 12.290 1.00 13.06 ? 155 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 155 ? 17.808 6.822 12.932 1.00 16.34 ? 155 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 155 ? 18.608 8.799 11.306 1.00 13.82 ? 155 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 155 ? 17.617 5.685 11.813 1.00 17.41 ? 155 ILE A CD1 1 ATOM 1201 N N . GLN A 1 156 ? 16.071 11.008 12.466 1.00 13.07 ? 156 GLN A N 1 ATOM 1202 C CA . GLN A 1 156 ? 16.018 12.368 11.887 1.00 16.08 ? 156 GLN A CA 1 ATOM 1203 C C . GLN A 1 156 ? 15.966 13.437 12.950 1.00 16.57 ? 156 GLN A C 1 ATOM 1204 O O . GLN A 1 156 ? 16.574 14.540 12.771 1.00 16.85 ? 156 GLN A O 1 ATOM 1205 C CB . GLN A 1 156 ? 14.852 12.503 10.946 1.00 17.07 ? 156 GLN A CB 1 ATOM 1206 C CG . GLN A 1 156 ? 15.038 11.582 9.702 1.00 13.11 ? 156 GLN A CG 1 ATOM 1207 C CD . GLN A 1 156 ? 13.852 11.777 8.841 1.00 12.47 ? 156 GLN A CD 1 ATOM 1208 O OE1 . GLN A 1 156 ? 12.779 11.000 9.068 1.00 16.05 ? 156 GLN A OE1 1 ATOM 1209 N NE2 . GLN A 1 156 ? 13.863 12.698 8.002 1.00 11.91 ? 156 GLN A NE2 1 ATOM 1210 N N . THR A 1 157 ? 15.316 13.157 14.082 1.00 13.06 ? 157 THR A N 1 ATOM 1211 C CA . THR A 1 157 ? 15.129 14.185 15.112 1.00 13.48 ? 157 THR A CA 1 ATOM 1212 C C . THR A 1 157 ? 16.346 14.180 16.080 1.00 13.29 ? 157 THR A C 1 ATOM 1213 O O . THR A 1 157 ? 16.408 15.076 17.005 1.00 14.66 ? 157 THR A O 1 ATOM 1214 C CB . THR A 1 157 ? 13.820 13.966 15.934 1.00 13.07 ? 157 THR A CB 1 ATOM 1215 O OG1 . THR A 1 157 ? 13.834 12.632 16.535 1.00 14.42 ? 157 THR A OG1 1 ATOM 1216 C CG2 . THR A 1 157 ? 12.661 14.131 15.030 1.00 16.12 ? 157 THR A CG2 1 ATOM 1217 N N . THR A 1 158 ? 17.339 13.282 15.947 1.00 14.35 ? 158 THR A N 1 ATOM 1218 C CA . THR A 1 158 ? 18.488 13.264 16.901 1.00 14.54 ? 158 THR A CA 1 ATOM 1219 C C . THR A 1 158 ? 19.758 13.446 15.980 1.00 15.90 ? 158 THR A C 1 ATOM 1220 O O . THR A 1 158 ? 20.266 14.576 15.804 1.00 17.04 ? 158 THR A O 1 ATOM 1221 C CB . THR A 1 158 ? 18.565 12.008 17.794 1.00 15.46 ? 158 THR A CB 1 ATOM 1222 O OG1 . THR A 1 158 ? 18.652 10.815 16.962 1.00 14.85 ? 158 THR A OG1 1 ATOM 1223 C CG2 . THR A 1 158 ? 17.261 11.912 18.627 1.00 14.61 ? 158 THR A CG2 1 ATOM 1224 N N . ALA A 1 159 ? 20.158 12.373 15.330 1.00 14.82 ? 159 ALA A N 1 ATOM 1225 C CA . ALA A 1 159 ? 21.395 12.433 14.489 1.00 16.79 ? 159 ALA A CA 1 ATOM 1226 C C . ALA A 1 159 ? 21.336 13.461 13.412 1.00 17.11 ? 159 ALA A C 1 ATOM 1227 O O . ALA A 1 159 ? 22.331 14.245 13.231 1.00 15.16 ? 159 ALA A O 1 ATOM 1228 C CB . ALA A 1 159 ? 21.696 11.023 13.859 1.00 18.14 ? 159 ALA A CB 1 ATOM 1229 N N . GLU A 1 160 ? 20.271 13.493 12.612 1.00 14.11 ? 160 GLU A N 1 ATOM 1230 C CA . GLU A 1 160 ? 20.296 14.401 11.472 1.00 14.76 ? 160 GLU A CA 1 ATOM 1231 C C . GLU A 1 160 ? 20.281 15.882 11.931 1.00 15.67 ? 160 GLU A C 1 ATOM 1232 O O . GLU A 1 160 ? 20.927 16.719 11.327 1.00 15.56 ? 160 GLU A O 1 ATOM 1233 C CB . GLU A 1 160 ? 19.121 14.138 10.465 1.00 15.28 ? 160 GLU A CB 1 ATOM 1234 C CG . GLU A 1 160 ? 19.136 12.674 9.873 1.00 16.40 ? 160 GLU A CG 1 ATOM 1235 C CD . GLU A 1 160 ? 20.266 12.418 8.896 1.00 18.59 ? 160 GLU A CD 1 ATOM 1236 O OE1 . GLU A 1 160 ? 21.248 13.240 8.785 1.00 18.50 ? 160 GLU A OE1 1 ATOM 1237 O OE2 . GLU A 1 160 ? 20.199 11.346 8.229 1.00 17.69 ? 160 GLU A OE2 1 ATOM 1238 N N . ALA A 1 161 ? 19.511 16.156 12.981 1.00 14.40 ? 161 ALA A N 1 ATOM 1239 C CA . ALA A 1 161 ? 19.508 17.494 13.596 1.00 15.30 ? 161 ALA A CA 1 ATOM 1240 C C . ALA A 1 161 ? 20.875 17.863 14.183 1.00 15.88 ? 161 ALA A C 1 ATOM 1241 O O . ALA A 1 161 ? 21.292 19.082 14.118 1.00 17.17 ? 161 ALA A O 1 ATOM 1242 C CB . ALA A 1 161 ? 18.423 17.551 14.727 1.00 15.15 ? 161 ALA A CB 1 ATOM 1243 N N . ALA A 1 162 ? 21.565 16.872 14.715 1.00 14.69 ? 162 ALA A N 1 ATOM 1244 C CA . ALA A 1 162 ? 22.974 17.166 15.186 1.00 14.52 ? 162 ALA A CA 1 ATOM 1245 C C . ALA A 1 162 ? 23.825 17.556 13.974 1.00 16.45 ? 162 ALA A C 1 ATOM 1246 O O . ALA A 1 162 ? 24.679 18.480 14.109 1.00 18.30 ? 162 ALA A O 1 ATOM 1247 C CB . ALA A 1 162 ? 23.599 15.997 15.933 1.00 15.68 ? 162 ALA A CB 1 ATOM 1248 N N . ARG A 1 163 ? 23.692 16.874 12.845 1.00 13.33 ? 163 ARG A N 1 ATOM 1249 C CA . ARG A 1 163 ? 24.565 17.120 11.685 1.00 14.32 ? 163 ARG A CA 1 ATOM 1250 C C . ARG A 1 163 ? 24.266 18.457 11.069 1.00 16.04 ? 163 ARG A C 1 ATOM 1251 O O . ARG A 1 163 ? 25.194 18.987 10.426 1.00 17.10 ? 163 ARG A O 1 ATOM 1252 C CB . ARG A 1 163 ? 24.365 15.973 10.670 1.00 16.63 ? 163 ARG A CB 1 ATOM 1253 C CG . ARG A 1 163 ? 24.859 14.630 11.176 1.00 14.95 ? 163 ARG A CG 1 ATOM 1254 C CD . ARG A 1 163 ? 24.376 13.580 10.210 1.00 16.25 ? 163 ARG A CD 1 ATOM 1255 N NE . ARG A 1 163 ? 24.914 12.252 10.587 1.00 15.57 ? 163 ARG A NE 1 ATOM 1256 C CZ . ARG A 1 163 ? 24.271 11.104 10.293 1.00 21.88 ? 163 ARG A CZ 1 ATOM 1257 N NH1 . ARG A 1 163 ? 23.105 11.168 9.656 1.00 21.31 ? 163 ARG A NH1 1 ATOM 1258 N NH2 . ARG A 1 163 ? 24.762 9.923 10.588 1.00 18.99 ? 163 ARG A NH2 1 ATOM 1259 N N . PHE A 1 164 ? 22.997 18.953 11.068 1.00 13.93 ? 164 PHE A N 1 ATOM 1260 C CA . PHE A 1 164 ? 22.629 20.096 10.238 1.00 14.84 ? 164 PHE A CA 1 ATOM 1261 C C . PHE A 1 164 ? 21.751 21.079 11.000 1.00 16.67 ? 164 PHE A C 1 ATOM 1262 O O . PHE A 1 164 ? 20.679 20.707 11.469 1.00 16.49 ? 164 PHE A O 1 ATOM 1263 C CB . PHE A 1 164 ? 21.830 19.659 9.014 1.00 15.86 ? 164 PHE A CB 1 ATOM 1264 C CG . PHE A 1 164 ? 22.589 18.878 8.036 1.00 17.91 ? 164 PHE A CG 1 ATOM 1265 C CD1 . PHE A 1 164 ? 23.452 19.556 7.168 1.00 18.53 ? 164 PHE A CD1 1 ATOM 1266 C CD2 . PHE A 1 164 ? 22.504 17.473 8.017 1.00 15.48 ? 164 PHE A CD2 1 ATOM 1267 C CE1 . PHE A 1 164 ? 24.148 18.816 6.168 1.00 17.59 ? 164 PHE A CE1 1 ATOM 1268 C CE2 . PHE A 1 164 ? 23.165 16.722 7.007 1.00 17.74 ? 164 PHE A CE2 1 ATOM 1269 C CZ . PHE A 1 164 ? 24.051 17.443 6.050 1.00 18.41 ? 164 PHE A CZ 1 ATOM 1270 N N . LYS A 1 165 ? 22.235 22.294 11.234 1.00 16.05 ? 165 LYS A N 1 ATOM 1271 C CA . LYS A 1 165 ? 21.440 23.295 11.923 1.00 16.38 ? 165 LYS A CA 1 ATOM 1272 C C . LYS A 1 165 ? 20.057 23.529 11.246 1.00 15.64 ? 165 LYS A C 1 ATOM 1273 O O . LYS A 1 165 ? 19.033 23.691 11.981 1.00 16.08 ? 165 LYS A O 1 ATOM 1274 C CB . LYS A 1 165 ? 22.271 24.614 12.003 1.00 18.88 ? 165 LYS A CB 1 ATOM 1275 C CG . LYS A 1 165 ? 21.482 25.797 12.484 1.00 28.17 ? 165 LYS A CG 1 ATOM 1276 C CD . LYS A 1 165 ? 22.521 26.952 12.833 1.00 42.16 ? 165 LYS A CD 1 ATOM 1277 C CE . LYS A 1 165 ? 23.545 26.388 13.916 1.00 45.70 ? 165 LYS A CE 1 ATOM 1278 N NZ . LYS A 1 165 ? 24.568 27.399 14.502 1.00 53.46 ? 165 LYS A NZ 1 ATOM 1279 N N . TYR A 1 166 ? 19.971 23.398 9.923 1.00 14.96 ? 166 TYR A N 1 ATOM 1280 C CA . TYR A 1 166 ? 18.697 23.542 9.210 1.00 15.69 ? 166 TYR A CA 1 ATOM 1281 C C . TYR A 1 166 ? 17.710 22.464 9.768 1.00 16.37 ? 166 TYR A C 1 ATOM 1282 O O . TYR A 1 166 ? 16.511 22.776 9.980 1.00 15.57 ? 166 TYR A O 1 ATOM 1283 C CB . TYR A 1 166 ? 18.897 23.407 7.685 1.00 19.04 ? 166 TYR A CB 1 ATOM 1284 C CG . TYR A 1 166 ? 17.561 23.392 6.928 1.00 18.99 ? 166 TYR A CG 1 ATOM 1285 C CD1 . TYR A 1 166 ? 16.989 24.567 6.461 1.00 19.64 ? 166 TYR A CD1 1 ATOM 1286 C CD2 . TYR A 1 166 ? 16.932 22.194 6.647 1.00 16.50 ? 166 TYR A CD2 1 ATOM 1287 C CE1 . TYR A 1 166 ? 15.722 24.570 5.754 1.00 21.52 ? 166 TYR A CE1 1 ATOM 1288 C CE2 . TYR A 1 166 ? 15.778 22.165 5.960 1.00 20.02 ? 166 TYR A CE2 1 ATOM 1289 C CZ . TYR A 1 166 ? 15.148 23.342 5.524 1.00 20.09 ? 166 TYR A CZ 1 ATOM 1290 O OH . TYR A 1 166 ? 13.984 23.273 4.821 1.00 20.85 ? 166 TYR A OH 1 ATOM 1291 N N . ILE A 1 167 ? 18.212 21.219 9.934 1.00 13.46 ? 167 ILE A N 1 ATOM 1292 C CA . ILE A 1 167 ? 17.252 20.171 10.395 1.00 14.33 ? 167 ILE A CA 1 ATOM 1293 C C . ILE A 1 167 ? 16.859 20.372 11.852 1.00 16.58 ? 167 ILE A C 1 ATOM 1294 O O . ILE A 1 167 ? 15.693 20.264 12.203 1.00 15.16 ? 167 ILE A O 1 ATOM 1295 C CB . ILE A 1 167 ? 17.845 18.769 10.126 1.00 14.08 ? 167 ILE A CB 1 ATOM 1296 C CG1 . ILE A 1 167 ? 18.048 18.600 8.623 1.00 14.16 ? 167 ILE A CG1 1 ATOM 1297 C CG2 . ILE A 1 167 ? 16.932 17.669 10.728 1.00 14.62 ? 167 ILE A CG2 1 ATOM 1298 C CD1 . ILE A 1 167 ? 18.710 17.237 8.271 1.00 14.29 ? 167 ILE A CD1 1 ATOM 1299 N N . GLU A 1 168 ? 17.803 20.720 12.728 1.00 14.51 ? 168 GLU A N 1 ATOM 1300 C CA . GLU A 1 168 ? 17.487 21.136 14.064 1.00 15.07 ? 168 GLU A CA 1 ATOM 1301 C C . GLU A 1 168 ? 16.369 22.206 14.053 1.00 16.43 ? 168 GLU A C 1 ATOM 1302 O O . GLU A 1 168 ? 15.400 22.101 14.851 1.00 15.54 ? 168 GLU A O 1 ATOM 1303 C CB . GLU A 1 168 ? 18.787 21.696 14.752 1.00 16.31 ? 168 GLU A CB 1 ATOM 1304 C CG . GLU A 1 168 ? 18.441 22.256 16.112 1.00 14.88 ? 168 GLU A CG 1 ATOM 1305 C CD . GLU A 1 168 ? 19.651 22.975 16.800 1.00 19.89 ? 168 GLU A CD 1 ATOM 1306 O OE1 . GLU A 1 168 ? 20.686 23.152 16.124 1.00 18.05 ? 168 GLU A OE1 1 ATOM 1307 O OE2 . GLU A 1 168 ? 19.561 23.355 17.996 1.00 22.37 ? 168 GLU A OE2 1 ATOM 1308 N N . GLN A 1 169 ? 16.530 23.255 13.260 1.00 15.59 ? 169 GLN A N 1 ATOM 1309 C CA . GLN A 1 169 ? 15.497 24.330 13.167 1.00 16.48 ? 169 GLN A CA 1 ATOM 1310 C C . GLN A 1 169 ? 14.133 23.811 12.642 1.00 17.86 ? 169 GLN A C 1 ATOM 1311 O O . GLN A 1 169 ? 13.111 24.213 13.160 1.00 17.76 ? 169 GLN A O 1 ATOM 1312 C CB . GLN A 1 169 ? 16.002 25.451 12.254 1.00 17.69 ? 169 GLN A CB 1 ATOM 1313 C CG . GLN A 1 169 ? 17.213 26.158 12.941 1.00 20.70 ? 169 GLN A CG 1 ATOM 1314 C CD . GLN A 1 169 ? 17.847 27.172 11.975 1.00 29.42 ? 169 GLN A CD 1 ATOM 1315 O OE1 . GLN A 1 169 ? 17.800 27.016 10.719 1.00 35.31 ? 169 GLN A OE1 1 ATOM 1316 N NE2 . GLN A 1 169 ? 18.389 28.218 12.541 1.00 38.03 ? 169 GLN A NE2 1 ATOM 1317 N N . GLN A 1 170 ? 14.182 22.906 11.677 1.00 15.05 ? 170 GLN A N 1 ATOM 1318 C CA . GLN A 1 170 ? 12.944 22.270 11.149 1.00 16.70 ? 170 GLN A CA 1 ATOM 1319 C C . GLN A 1 170 ? 12.229 21.564 12.343 1.00 15.58 ? 170 GLN A C 1 ATOM 1320 O O . GLN A 1 170 ? 11.003 21.636 12.469 1.00 15.48 ? 170 GLN A O 1 ATOM 1321 C CB . GLN A 1 170 ? 13.276 21.202 10.120 1.00 17.64 ? 170 GLN A CB 1 ATOM 1322 C CG . GLN A 1 170 ? 13.570 21.703 8.725 1.00 21.89 ? 170 GLN A CG 1 ATOM 1323 C CD . GLN A 1 170 ? 12.341 21.183 7.846 1.00 31.71 ? 170 GLN A CD 1 ATOM 1324 O OE1 . GLN A 1 170 ? 11.969 19.862 7.560 1.00 28.06 ? 170 GLN A OE1 1 ATOM 1325 N NE2 . GLN A 1 170 ? 11.604 22.217 7.534 1.00 21.62 ? 170 GLN A NE2 1 ATOM 1326 N N . ILE A 1 171 ? 12.969 20.819 13.141 1.00 15.77 ? 171 ILE A N 1 ATOM 1327 C CA . ILE A 1 171 ? 12.315 20.134 14.271 1.00 14.54 ? 171 ILE A CA 1 ATOM 1328 C C . ILE A 1 171 ? 11.803 21.150 15.315 1.00 15.55 ? 171 ILE A C 1 ATOM 1329 O O . ILE A 1 171 ? 10.737 21.033 15.873 1.00 16.19 ? 171 ILE A O 1 ATOM 1330 C CB . ILE A 1 171 ? 13.208 19.098 14.949 1.00 12.27 ? 171 ILE A CB 1 ATOM 1331 C CG1 . ILE A 1 171 ? 13.670 18.085 13.895 1.00 16.00 ? 171 ILE A CG1 1 ATOM 1332 C CG2 . ILE A 1 171 ? 12.486 18.341 16.109 1.00 15.81 ? 171 ILE A CG2 1 ATOM 1333 C CD1 . ILE A 1 171 ? 12.577 17.519 13.018 1.00 17.65 ? 171 ILE A CD1 1 ATOM 1334 N N . GLN A 1 172 ? 12.579 22.198 15.565 1.00 16.59 ? 172 GLN A N 1 ATOM 1335 C CA . GLN A 1 172 ? 12.066 23.232 16.499 1.00 15.68 ? 172 GLN A CA 1 ATOM 1336 C C . GLN A 1 172 ? 10.760 23.860 15.990 1.00 17.46 ? 172 GLN A C 1 ATOM 1337 O O . GLN A 1 172 ? 9.880 24.226 16.846 1.00 17.43 ? 172 GLN A O 1 ATOM 1338 C CB . GLN A 1 172 ? 13.122 24.377 16.648 1.00 16.55 ? 172 GLN A CB 1 ATOM 1339 C CG . GLN A 1 172 ? 14.263 23.907 17.543 1.00 16.84 ? 172 GLN A CG 1 ATOM 1340 C CD . GLN A 1 172 ? 15.478 24.836 17.533 1.00 17.90 ? 172 GLN A CD 1 ATOM 1341 O OE1 . GLN A 1 172 ? 15.891 25.357 16.469 1.00 19.91 ? 172 GLN A OE1 1 ATOM 1342 N NE2 . GLN A 1 172 ? 16.030 25.055 18.724 1.00 20.19 ? 172 GLN A NE2 1 ATOM 1343 N N . GLU A 1 173 ? 10.630 24.056 14.664 1.00 14.61 ? 173 GLU A N 1 ATOM 1344 C CA . GLU A 1 173 ? 9.396 24.592 14.041 1.00 16.50 ? 173 GLU A CA 1 ATOM 1345 C C . GLU A 1 173 ? 8.227 23.549 14.242 1.00 18.96 ? 173 GLU A C 1 ATOM 1346 O O . GLU A 1 173 ? 7.054 23.918 14.226 1.00 21.32 ? 173 GLU A O 1 ATOM 1347 C CB . GLU A 1 173 ? 9.599 24.846 12.586 1.00 17.89 ? 173 GLU A CB 1 ATOM 1348 C CG . GLU A 1 173 ? 10.451 26.163 12.453 1.00 23.01 ? 173 GLU A CG 1 ATOM 1349 C CD . GLU A 1 173 ? 10.960 26.409 11.018 1.00 35.72 ? 173 GLU A CD 1 ATOM 1350 O OE1 . GLU A 1 173 ? 11.856 27.286 10.867 1.00 36.96 ? 173 GLU A OE1 1 ATOM 1351 O OE2 . GLU A 1 173 ? 10.512 25.735 10.069 1.00 39.62 ? 173 GLU A OE2 1 ATOM 1352 N N . ARG A 1 174 ? 8.577 22.300 14.553 1.00 14.69 ? 174 ARG A N 1 ATOM 1353 C CA . ARG A 1 174 ? 7.617 21.218 14.732 1.00 14.69 ? 174 ARG A CA 1 ATOM 1354 C C . ARG A 1 174 ? 7.568 20.808 16.171 1.00 15.95 ? 174 ARG A C 1 ATOM 1355 O O . ARG A 1 174 ? 7.289 19.631 16.531 1.00 15.93 ? 174 ARG A O 1 ATOM 1356 C CB . ARG A 1 174 ? 8.025 20.051 13.802 1.00 13.44 ? 174 ARG A CB 1 ATOM 1357 C CG . ARG A 1 174 ? 7.949 20.267 12.267 1.00 16.05 ? 174 ARG A CG 1 ATOM 1358 C CD . ARG A 1 174 ? 8.890 19.262 11.471 1.00 16.79 ? 174 ARG A CD 1 ATOM 1359 N NE . ARG A 1 174 ? 8.663 19.291 10.070 1.00 18.19 ? 174 ARG A NE 1 ATOM 1360 C CZ . ARG A 1 174 ? 8.934 20.336 9.289 1.00 17.81 ? 174 ARG A CZ 1 ATOM 1361 N NH1 . ARG A 1 174 ? 9.519 21.449 9.829 1.00 17.94 ? 174 ARG A NH1 1 ATOM 1362 N NH2 . ARG A 1 174 ? 8.573 20.289 8.027 1.00 19.38 ? 174 ARG A NH2 1 ATOM 1363 N N . ALA A 1 175 ? 7.703 21.779 17.081 1.00 15.29 ? 175 ALA A N 1 ATOM 1364 C CA . ALA A 1 175 ? 7.732 21.381 18.489 1.00 14.87 ? 175 ALA A CA 1 ATOM 1365 C C . ALA A 1 175 ? 6.378 20.923 18.960 1.00 14.88 ? 175 ALA A C 1 ATOM 1366 O O . ALA A 1 175 ? 6.315 20.135 19.863 1.00 15.06 ? 175 ALA A O 1 ATOM 1367 C CB . ALA A 1 175 ? 8.181 22.595 19.435 1.00 17.43 ? 175 ALA A CB 1 ATOM 1368 N N . TYR A 1 176 ? 5.331 21.500 18.341 1.00 14.62 ? 176 TYR A N 1 ATOM 1369 C CA . TYR A 1 176 ? 3.976 21.181 18.877 1.00 15.15 ? 176 TYR A CA 1 ATOM 1370 C C . TYR A 1 176 ? 3.046 20.688 17.812 1.00 15.66 ? 176 TYR A C 1 ATOM 1371 O O . TYR A 1 176 ? 1.840 20.491 18.103 1.00 17.20 ? 176 TYR A O 1 ATOM 1372 C CB . TYR A 1 176 ? 3.336 22.426 19.577 1.00 15.50 ? 176 TYR A CB 1 ATOM 1373 C CG . TYR A 1 176 ? 4.256 23.119 20.531 1.00 14.91 ? 176 TYR A CG 1 ATOM 1374 C CD1 . TYR A 1 176 ? 4.865 22.441 21.617 1.00 17.55 ? 176 TYR A CD1 1 ATOM 1375 C CD2 . TYR A 1 176 ? 4.606 24.471 20.291 1.00 23.54 ? 176 TYR A CD2 1 ATOM 1376 C CE1 . TYR A 1 176 ? 5.757 23.133 22.509 1.00 19.55 ? 176 TYR A CE1 1 ATOM 1377 C CE2 . TYR A 1 176 ? 5.442 25.137 21.199 1.00 21.02 ? 176 TYR A CE2 1 ATOM 1378 C CZ . TYR A 1 176 ? 6.048 24.451 22.262 1.00 22.12 ? 176 TYR A CZ 1 ATOM 1379 O OH . TYR A 1 176 ? 6.906 25.081 23.119 1.00 21.42 ? 176 TYR A OH 1 ATOM 1380 N N . ARG A 1 177 ? 3.569 20.460 16.627 1.00 14.08 ? 177 ARG A N 1 ATOM 1381 C CA . ARG A 1 177 ? 2.852 19.993 15.428 1.00 15.81 ? 177 ARG A CA 1 ATOM 1382 C C . ARG A 1 177 ? 3.807 19.296 14.488 1.00 15.75 ? 177 ARG A C 1 ATOM 1383 O O . ARG A 1 177 ? 4.769 19.943 14.019 1.00 16.70 ? 177 ARG A O 1 ATOM 1384 C CB . ARG A 1 177 ? 2.132 21.164 14.700 1.00 14.36 ? 177 ARG A CB 1 ATOM 1385 C CG . ARG A 1 177 ? 1.329 20.726 13.492 1.00 17.21 ? 177 ARG A CG 1 ATOM 1386 C CD . ARG A 1 177 ? 0.620 21.852 12.732 1.00 21.84 ? 177 ARG A CD 1 ATOM 1387 N NE . ARG A 1 177 ? 1.658 22.837 12.310 1.00 25.47 ? 177 ARG A NE 1 ATOM 1388 C CZ . ARG A 1 177 ? 1.332 23.974 11.692 1.00 34.01 ? 177 ARG A CZ 1 ATOM 1389 N NH1 . ARG A 1 177 ? 0.064 24.266 11.511 1.00 34.63 ? 177 ARG A NH1 1 ATOM 1390 N NH2 . ARG A 1 177 ? 2.243 24.828 11.285 1.00 36.47 ? 177 ARG A NH2 1 ATOM 1391 N N . ASP A 1 178 ? 3.607 17.991 14.302 1.00 14.66 ? 178 ASP A N 1 ATOM 1392 C CA . ASP A 1 178 ? 4.443 17.340 13.317 1.00 13.84 ? 178 ASP A CA 1 ATOM 1393 C C . ASP A 1 178 ? 4.138 17.716 11.894 1.00 15.38 ? 178 ASP A C 1 ATOM 1394 O O . ASP A 1 178 ? 2.996 18.180 11.554 1.00 15.91 ? 178 ASP A O 1 ATOM 1395 C CB . ASP A 1 178 ? 4.171 15.818 13.405 1.00 14.27 ? 178 ASP A CB 1 ATOM 1396 C CG . ASP A 1 178 ? 4.606 15.186 14.721 1.00 15.42 ? 178 ASP A CG 1 ATOM 1397 O OD1 . ASP A 1 178 ? 5.557 15.631 15.407 1.00 14.81 ? 178 ASP A OD1 1 ATOM 1398 O OD2 . ASP A 1 178 ? 3.899 14.165 15.152 1.00 15.09 ? 178 ASP A OD2 1 ATOM 1399 N N . GLU A 1 179 ? 5.189 17.567 11.045 1.00 14.37 ? 179 GLU A N 1 ATOM 1400 C CA . GLU A 1 179 ? 4.992 17.814 9.652 1.00 16.03 ? 179 GLU A CA 1 ATOM 1401 C C . GLU A 1 179 ? 6.049 16.982 8.918 1.00 15.09 ? 179 GLU A C 1 ATOM 1402 O O . GLU A 1 179 ? 7.153 16.800 9.420 1.00 15.22 ? 179 GLU A O 1 ATOM 1403 C CB . GLU A 1 179 ? 5.120 19.310 9.345 1.00 16.83 ? 179 GLU A CB 1 ATOM 1404 C CG . GLU A 1 179 ? 4.841 19.590 7.804 1.00 18.81 ? 179 GLU A CG 1 ATOM 1405 C CD . GLU A 1 179 ? 5.057 21.072 7.448 1.00 26.09 ? 179 GLU A CD 1 ATOM 1406 O OE1 . GLU A 1 179 ? 4.843 21.911 8.351 1.00 29.80 ? 179 GLU A OE1 1 ATOM 1407 O OE2 . GLU A 1 179 ? 5.445 21.313 6.241 1.00 32.87 ? 179 GLU A OE2 1 ATOM 1408 N N . VAL A 1 180 ? 5.691 16.407 7.755 1.00 15.91 ? 180 VAL A N 1 ATOM 1409 C CA . VAL A 1 180 ? 6.753 15.652 7.003 1.00 15.69 ? 180 VAL A CA 1 ATOM 1410 C C . VAL A 1 180 ? 7.944 16.589 6.734 1.00 16.70 ? 180 VAL A C 1 ATOM 1411 O O . VAL A 1 180 ? 7.801 17.826 6.709 1.00 16.35 ? 180 VAL A O 1 ATOM 1412 C CB . VAL A 1 180 ? 6.216 15.128 5.647 1.00 18.64 ? 180 VAL A CB 1 ATOM 1413 C CG1 . VAL A 1 180 ? 5.045 14.074 5.836 1.00 18.81 ? 180 VAL A CG1 1 ATOM 1414 C CG2 . VAL A 1 180 ? 5.654 16.326 4.765 1.00 18.67 ? 180 VAL A CG2 1 ATOM 1415 N N . PRO A 1 181 ? 9.127 15.976 6.627 1.00 18.54 ? 181 PRO A N 1 ATOM 1416 C CA . PRO A 1 181 ? 10.336 16.817 6.386 1.00 18.52 ? 181 PRO A CA 1 ATOM 1417 C C . PRO A 1 181 ? 10.239 17.530 5.059 1.00 18.40 ? 181 PRO A C 1 ATOM 1418 O O . PRO A 1 181 ? 9.641 17.026 4.081 1.00 17.75 ? 181 PRO A O 1 ATOM 1419 C CB . PRO A 1 181 ? 11.485 15.750 6.356 1.00 19.33 ? 181 PRO A CB 1 ATOM 1420 C CG . PRO A 1 181 ? 10.852 14.449 6.088 1.00 19.26 ? 181 PRO A CG 1 ATOM 1421 C CD . PRO A 1 181 ? 9.395 14.546 6.651 1.00 17.58 ? 181 PRO A CD 1 ATOM 1422 N N . SER A 1 182 ? 10.880 18.713 5.017 1.00 18.71 ? 182 SER A N 1 ATOM 1423 C CA . SER A 1 182 ? 10.935 19.408 3.733 1.00 17.45 ? 182 SER A CA 1 ATOM 1424 C C . SER A 1 182 ? 11.865 18.624 2.784 1.00 18.72 ? 182 SER A C 1 ATOM 1425 O O . SER A 1 182 ? 12.719 17.809 3.246 1.00 18.24 ? 182 SER A O 1 ATOM 1426 C CB . SER A 1 182 ? 11.486 20.796 3.955 1.00 18.72 ? 182 SER A CB 1 ATOM 1427 O OG . SER A 1 182 ? 12.891 20.815 4.366 1.00 20.86 ? 182 SER A OG 1 ATOM 1428 N N . SER A 1 183 ? 11.727 18.866 1.453 1.00 20.08 ? 183 SER A N 1 ATOM 1429 C CA . SER A 1 183 ? 12.666 18.185 0.600 1.00 22.05 ? 183 SER A CA 1 ATOM 1430 C C . SER A 1 183 ? 14.114 18.647 0.798 1.00 19.97 ? 183 SER A C 1 ATOM 1431 O O . SER A 1 183 ? 14.979 17.813 0.630 1.00 21.14 ? 183 SER A O 1 ATOM 1432 C CB . SER A 1 183 ? 12.363 18.252 -0.842 1.00 26.66 ? 183 SER A CB 1 ATOM 1433 O OG . SER A 1 183 ? 11.715 19.463 -1.137 1.00 38.02 ? 183 SER A OG 1 ATOM 1434 N N . ALA A 1 184 ? 14.300 19.863 1.323 1.00 19.33 ? 184 ALA A N 1 ATOM 1435 C CA . ALA A 1 184 ? 15.656 20.284 1.690 1.00 20.46 ? 184 ALA A CA 1 ATOM 1436 C C . ALA A 1 184 ? 16.214 19.357 2.759 1.00 19.48 ? 184 ALA A C 1 ATOM 1437 O O . ALA A 1 184 ? 17.395 18.949 2.730 1.00 20.15 ? 184 ALA A O 1 ATOM 1438 C CB . ALA A 1 184 ? 15.674 21.782 2.184 1.00 19.37 ? 184 ALA A CB 1 ATOM 1439 N N . THR A 1 185 ? 15.383 19.090 3.771 1.00 16.83 ? 185 THR A N 1 ATOM 1440 C CA . THR A 1 185 ? 15.835 18.202 4.846 1.00 17.22 ? 185 THR A CA 1 ATOM 1441 C C . THR A 1 185 ? 16.252 16.823 4.302 1.00 16.58 ? 185 THR A C 1 ATOM 1442 O O . THR A 1 185 ? 17.317 16.270 4.722 1.00 16.23 ? 185 THR A O 1 ATOM 1443 C CB . THR A 1 185 ? 14.635 17.973 5.846 1.00 16.02 ? 185 THR A CB 1 ATOM 1444 O OG1 . THR A 1 185 ? 14.482 19.176 6.617 1.00 20.33 ? 185 THR A OG1 1 ATOM 1445 C CG2 . THR A 1 185 ? 15.022 16.889 6.798 1.00 16.01 ? 185 THR A CG2 1 ATOM 1446 N N . ILE A 1 186 ? 15.390 16.222 3.435 1.00 15.04 ? 186 ILE A N 1 ATOM 1447 C CA . ILE A 1 186 ? 15.739 14.931 2.840 1.00 17.54 ? 186 ILE A CA 1 ATOM 1448 C C . ILE A 1 186 ? 17.083 14.972 2.060 1.00 16.65 ? 186 ILE A C 1 ATOM 1449 O O . ILE A 1 186 ? 17.943 14.076 2.182 1.00 17.70 ? 186 ILE A O 1 ATOM 1450 C CB . ILE A 1 186 ? 14.547 14.448 1.905 1.00 17.44 ? 186 ILE A CB 1 ATOM 1451 C CG1 . ILE A 1 186 ? 13.235 14.192 2.729 1.00 22.08 ? 186 ILE A CG1 1 ATOM 1452 C CG2 . ILE A 1 186 ? 14.961 13.121 1.158 1.00 21.77 ? 186 ILE A CG2 1 ATOM 1453 C CD1 . ILE A 1 186 ? 13.355 13.058 3.637 1.00 23.45 ? 186 ILE A CD1 1 ATOM 1454 N N . SER A 1 187 ? 17.222 16.045 1.332 1.00 20.02 ? 187 SER A N 1 ATOM 1455 C CA . SER A 1 187 ? 18.424 16.276 0.490 1.00 19.99 ? 187 SER A CA 1 ATOM 1456 C C . SER A 1 187 ? 19.678 16.331 1.377 1.00 19.38 ? 187 SER A C 1 ATOM 1457 O O . SER A 1 187 ? 20.735 15.684 1.059 1.00 19.24 ? 187 SER A O 1 ATOM 1458 C CB . SER A 1 187 ? 18.251 17.565 -0.289 1.00 21.61 ? 187 SER A CB 1 ATOM 1459 O OG . SER A 1 187 ? 19.423 17.698 -1.142 1.00 30.45 ? 187 SER A OG 1 ATOM 1460 N N . LEU A 1 188 ? 19.623 17.103 2.439 1.00 17.33 ? 188 LEU A N 1 ATOM 1461 C CA . LEU A 1 188 ? 20.786 17.205 3.358 1.00 17.16 ? 188 LEU A CA 1 ATOM 1462 C C . LEU A 1 188 ? 21.121 15.841 3.970 1.00 17.01 ? 188 LEU A C 1 ATOM 1463 O O . LEU A 1 188 ? 22.284 15.404 4.001 1.00 19.25 ? 188 LEU A O 1 ATOM 1464 C CB . LEU A 1 188 ? 20.500 18.221 4.463 1.00 17.15 ? 188 LEU A CB 1 ATOM 1465 C CG . LEU A 1 188 ? 20.290 19.650 4.065 1.00 16.15 ? 188 LEU A CG 1 ATOM 1466 C CD1 . LEU A 1 188 ? 19.713 20.465 5.203 1.00 20.83 ? 188 LEU A CD1 1 ATOM 1467 C CD2 . LEU A 1 188 ? 21.750 20.142 3.516 1.00 17.37 ? 188 LEU A CD2 1 ATOM 1468 N N . GLU A 1 189 ? 20.070 15.123 4.485 1.00 18.01 ? 189 GLU A N 1 ATOM 1469 C CA . GLU A 1 189 ? 20.297 13.782 4.988 1.00 17.21 ? 189 GLU A CA 1 ATOM 1470 C C . GLU A 1 189 ? 21.068 12.879 4.002 1.00 16.83 ? 189 GLU A C 1 ATOM 1471 O O . GLU A 1 189 ? 22.025 12.168 4.370 1.00 18.03 ? 189 GLU A O 1 ATOM 1472 C CB . GLU A 1 189 ? 18.955 13.119 5.334 1.00 15.19 ? 189 GLU A CB 1 ATOM 1473 C CG . GLU A 1 189 ? 18.283 13.832 6.548 1.00 16.06 ? 189 GLU A CG 1 ATOM 1474 C CD . GLU A 1 189 ? 16.812 13.310 6.719 1.00 19.31 ? 189 GLU A CD 1 ATOM 1475 O OE1 . GLU A 1 189 ? 16.407 12.461 5.888 1.00 17.35 ? 189 GLU A OE1 1 ATOM 1476 O OE2 . GLU A 1 189 ? 16.151 13.761 7.654 1.00 17.08 ? 189 GLU A OE2 1 ATOM 1477 N N . ASN A 1 190 ? 20.597 12.882 2.785 1.00 17.45 ? 190 ASN A N 1 ATOM 1478 C CA . ASN A 1 190 ? 21.122 11.990 1.735 1.00 16.44 ? 190 ASN A CA 1 ATOM 1479 C C . ASN A 1 190 ? 22.524 12.448 1.294 1.00 19.07 ? 190 ASN A C 1 ATOM 1480 O O . ASN A 1 190 ? 23.268 11.611 0.756 1.00 22.16 ? 190 ASN A O 1 ATOM 1481 C CB . ASN A 1 190 ? 20.203 12.103 0.556 1.00 16.20 ? 190 ASN A CB 1 ATOM 1482 C CG . ASN A 1 190 ? 18.891 11.294 0.735 1.00 18.48 ? 190 ASN A CG 1 ATOM 1483 O OD1 . ASN A 1 190 ? 18.791 10.495 1.645 1.00 22.59 ? 190 ASN A OD1 1 ATOM 1484 N ND2 . ASN A 1 190 ? 17.901 11.562 -0.163 1.00 20.00 ? 190 ASN A ND2 1 ATOM 1485 N N . SER A 1 191 ? 22.829 13.704 1.642 1.00 19.42 ? 191 SER A N 1 ATOM 1486 C CA . SER A 1 191 ? 24.073 14.344 1.161 1.00 19.61 ? 191 SER A CA 1 ATOM 1487 C C . SER A 1 191 ? 25.151 14.452 2.187 1.00 20.20 ? 191 SER A C 1 ATOM 1488 O O . SER A 1 191 ? 26.227 14.994 1.840 1.00 19.14 ? 191 SER A O 1 ATOM 1489 C CB . SER A 1 191 ? 23.794 15.727 0.557 1.00 21.54 ? 191 SER A CB 1 ATOM 1490 O OG . SER A 1 191 ? 22.966 15.541 -0.635 1.00 22.79 ? 191 SER A OG 1 ATOM 1491 N N . TRP A 1 192 ? 24.959 13.925 3.382 1.00 16.45 ? 192 TRP A N 1 ATOM 1492 C CA . TRP A 1 192 ? 25.873 14.274 4.481 1.00 16.87 ? 192 TRP A CA 1 ATOM 1493 C C . TRP A 1 192 ? 27.274 13.692 4.157 1.00 18.66 ? 192 TRP A C 1 ATOM 1494 O O . TRP A 1 192 ? 28.323 14.348 4.370 1.00 19.00 ? 192 TRP A O 1 ATOM 1495 C CB . TRP A 1 192 ? 25.384 13.697 5.806 1.00 17.66 ? 192 TRP A CB 1 ATOM 1496 C CG . TRP A 1 192 ? 26.314 14.034 6.950 1.00 17.81 ? 192 TRP A CG 1 ATOM 1497 C CD1 . TRP A 1 192 ? 26.694 15.313 7.385 1.00 17.91 ? 192 TRP A CD1 1 ATOM 1498 C CD2 . TRP A 1 192 ? 26.914 13.118 7.860 1.00 16.79 ? 192 TRP A CD2 1 ATOM 1499 N NE1 . TRP A 1 192 ? 27.468 15.193 8.528 1.00 16.12 ? 192 TRP A NE1 1 ATOM 1500 C CE2 . TRP A 1 192 ? 27.645 13.876 8.830 1.00 15.55 ? 192 TRP A CE2 1 ATOM 1501 C CE3 . TRP A 1 192 ? 26.932 11.712 7.959 1.00 17.45 ? 192 TRP A CE3 1 ATOM 1502 C CZ2 . TRP A 1 192 ? 28.346 13.271 9.900 1.00 17.11 ? 192 TRP A CZ2 1 ATOM 1503 C CZ3 . TRP A 1 192 ? 27.652 11.127 8.972 1.00 14.42 ? 192 TRP A CZ3 1 ATOM 1504 C CH2 . TRP A 1 192 ? 28.315 11.904 9.978 1.00 16.44 ? 192 TRP A CH2 1 ATOM 1505 N N . SER A 1 193 ? 27.301 12.446 3.711 1.00 18.88 ? 193 SER A N 1 ATOM 1506 C CA . SER A 1 193 ? 28.598 11.824 3.393 1.00 20.41 ? 193 SER A CA 1 ATOM 1507 C C . SER A 1 193 ? 29.336 12.588 2.264 1.00 19.82 ? 193 SER A C 1 ATOM 1508 O O . SER A 1 193 ? 30.568 12.859 2.408 1.00 20.39 ? 193 SER A O 1 ATOM 1509 C CB . SER A 1 193 ? 28.324 10.347 3.016 1.00 21.66 ? 193 SER A CB 1 ATOM 1510 O OG . SER A 1 193 ? 29.606 9.730 2.873 1.00 28.57 ? 193 SER A OG 1 ATOM 1511 N N . GLY A 1 194 ? 28.593 12.893 1.217 1.00 19.56 ? 194 GLY A N 1 ATOM 1512 C CA . GLY A 1 194 ? 29.139 13.636 0.037 1.00 20.86 ? 194 GLY A CA 1 ATOM 1513 C C . GLY A 1 194 ? 29.631 14.992 0.472 1.00 21.69 ? 194 GLY A C 1 ATOM 1514 O O . GLY A 1 194 ? 30.754 15.384 0.086 1.00 21.36 ? 194 GLY A O 1 ATOM 1515 N N . LEU A 1 195 ? 28.856 15.743 1.253 1.00 19.39 ? 195 LEU A N 1 ATOM 1516 C CA . LEU A 1 195 ? 29.291 17.081 1.698 1.00 17.47 ? 195 LEU A CA 1 ATOM 1517 C C . LEU A 1 195 ? 30.499 16.919 2.581 1.00 19.63 ? 195 LEU A C 1 ATOM 1518 O O . LEU A 1 195 ? 31.480 17.727 2.452 1.00 20.35 ? 195 LEU A O 1 ATOM 1519 C CB . LEU A 1 195 ? 28.164 17.774 2.502 1.00 18.17 ? 195 LEU A CB 1 ATOM 1520 C CG . LEU A 1 195 ? 27.051 18.290 1.625 1.00 22.96 ? 195 LEU A CG 1 ATOM 1521 C CD1 . LEU A 1 195 ? 25.742 18.652 2.509 1.00 24.69 ? 195 LEU A CD1 1 ATOM 1522 C CD2 . LEU A 1 195 ? 27.580 19.631 0.898 1.00 22.77 ? 195 LEU A CD2 1 ATOM 1523 N N . SER A 1 196 ? 30.471 15.963 3.503 1.00 17.63 ? 196 SER A N 1 ATOM 1524 C CA . SER A 1 196 ? 31.579 15.802 4.458 1.00 18.25 ? 196 SER A CA 1 ATOM 1525 C C . SER A 1 196 ? 32.862 15.519 3.646 1.00 20.73 ? 196 SER A C 1 ATOM 1526 O O . SER A 1 196 ? 33.920 16.161 3.878 1.00 20.25 ? 196 SER A O 1 ATOM 1527 C CB . SER A 1 196 ? 31.306 14.540 5.311 1.00 18.19 ? 196 SER A CB 1 ATOM 1528 O OG . SER A 1 196 ? 30.344 14.918 6.309 1.00 16.66 ? 196 SER A OG 1 ATOM 1529 N N . LYS A 1 197 ? 32.752 14.656 2.646 1.00 18.59 ? 197 LYS A N 1 ATOM 1530 C CA . LYS A 1 197 ? 33.939 14.364 1.840 1.00 20.05 ? 197 LYS A CA 1 ATOM 1531 C C . LYS A 1 197 ? 34.442 15.597 1.036 1.00 20.76 ? 197 LYS A C 1 ATOM 1532 O O . LYS A 1 197 ? 35.672 15.864 1.023 1.00 19.73 ? 197 LYS A O 1 ATOM 1533 C CB . LYS A 1 197 ? 33.612 13.253 0.900 1.00 21.16 ? 197 LYS A CB 1 ATOM 1534 C CG . LYS A 1 197 ? 34.850 12.814 -0.025 1.00 24.49 ? 197 LYS A CG 1 ATOM 1535 C CD . LYS A 1 197 ? 34.365 11.685 -0.957 1.00 30.73 ? 197 LYS A CD 1 ATOM 1536 C CE . LYS A 1 197 ? 35.481 11.128 -1.817 1.00 40.67 ? 197 LYS A CE 1 ATOM 1537 N NZ . LYS A 1 197 ? 34.842 9.956 -2.619 1.00 43.73 ? 197 LYS A NZ 1 ATOM 1538 N N . GLN A 1 198 ? 33.514 16.311 0.396 1.00 18.71 ? 198 GLN A N 1 ATOM 1539 C CA . GLN A 1 198 ? 33.931 17.449 -0.439 1.00 18.30 ? 198 GLN A CA 1 ATOM 1540 C C . GLN A 1 198 ? 34.512 18.577 0.390 1.00 19.27 ? 198 GLN A C 1 ATOM 1541 O O . GLN A 1 198 ? 35.481 19.256 -0.062 1.00 19.04 ? 198 GLN A O 1 ATOM 1542 C CB . GLN A 1 198 ? 32.786 17.957 -1.364 1.00 18.11 ? 198 GLN A CB 1 ATOM 1543 C CG . GLN A 1 198 ? 32.365 16.908 -2.445 1.00 19.09 ? 198 GLN A CG 1 ATOM 1544 C CD . GLN A 1 198 ? 33.550 16.406 -3.264 1.00 26.06 ? 198 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 198 ? 34.347 17.225 -3.705 1.00 27.63 ? 198 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 198 ? 33.676 15.092 -3.486 1.00 28.62 ? 198 GLN A NE2 1 ATOM 1547 N N . ILE A 1 199 ? 33.986 18.837 1.563 1.00 18.85 ? 199 ILE A N 1 ATOM 1548 C CA . ILE A 1 199 ? 34.559 19.849 2.432 1.00 17.49 ? 199 ILE A CA 1 ATOM 1549 C C . ILE A 1 199 ? 36.001 19.453 2.840 1.00 19.49 ? 199 ILE A C 1 ATOM 1550 O O . ILE A 1 199 ? 36.898 20.322 2.867 1.00 18.47 ? 199 ILE A O 1 ATOM 1551 C CB . ILE A 1 199 ? 33.660 20.015 3.688 1.00 16.99 ? 199 ILE A CB 1 ATOM 1552 C CG1 . ILE A 1 199 ? 32.336 20.625 3.210 1.00 17.91 ? 199 ILE A CG1 1 ATOM 1553 C CG2 . ILE A 1 199 ? 34.300 20.964 4.737 1.00 20.32 ? 199 ILE A CG2 1 ATOM 1554 C CD1 . ILE A 1 199 ? 31.252 20.539 4.272 1.00 16.05 ? 199 ILE A CD1 1 ATOM 1555 N N . GLN A 1 200 ? 36.241 18.172 3.082 1.00 19.36 ? 200 GLN A N 1 ATOM 1556 C CA . GLN A 1 200 ? 37.613 17.697 3.376 1.00 18.81 ? 200 GLN A CA 1 ATOM 1557 C C . GLN A 1 200 ? 38.500 17.791 2.080 1.00 19.23 ? 200 GLN A C 1 ATOM 1558 O O . GLN A 1 200 ? 39.672 18.203 2.205 1.00 21.08 ? 200 GLN A O 1 ATOM 1559 C CB . GLN A 1 200 ? 37.561 16.288 3.958 1.00 18.30 ? 200 GLN A CB 1 ATOM 1560 C CG . GLN A 1 200 ? 37.150 16.347 5.417 1.00 17.25 ? 200 GLN A CG 1 ATOM 1561 C CD . GLN A 1 200 ? 36.743 14.971 5.892 1.00 20.00 ? 200 GLN A CD 1 ATOM 1562 O OE1 . GLN A 1 200 ? 37.589 14.223 6.326 1.00 23.22 ? 200 GLN A OE1 1 ATOM 1563 N NE2 . GLN A 1 200 ? 35.439 14.643 5.785 1.00 20.06 ? 200 GLN A NE2 1 ATOM 1564 N N . LEU A 1 201 ? 37.967 17.451 0.915 1.00 19.65 ? 201 LEU A N 1 ATOM 1565 C CA . LEU A 1 201 ? 38.845 17.500 -0.310 1.00 20.80 ? 201 LEU A CA 1 ATOM 1566 C C . LEU A 1 201 ? 39.129 18.970 -0.667 1.00 21.54 ? 201 LEU A C 1 ATOM 1567 O O . LEU A 1 201 ? 40.157 19.257 -1.346 1.00 22.34 ? 201 LEU A O 1 ATOM 1568 C CB . LEU A 1 201 ? 38.219 16.823 -1.505 1.00 22.05 ? 201 LEU A CB 1 ATOM 1569 C CG . LEU A 1 201 ? 37.833 15.362 -1.368 1.00 25.92 ? 201 LEU A CG 1 ATOM 1570 C CD1 . LEU A 1 201 ? 37.188 14.787 -2.568 1.00 27.06 ? 201 LEU A CD1 1 ATOM 1571 C CD2 . LEU A 1 201 ? 38.984 14.473 -0.810 1.00 30.39 ? 201 LEU A CD2 1 ATOM 1572 N N . ALA A 1 202 ? 38.300 19.908 -0.230 1.00 19.48 ? 202 ALA A N 1 ATOM 1573 C CA . ALA A 1 202 ? 38.527 21.330 -0.555 1.00 20.98 ? 202 ALA A CA 1 ATOM 1574 C C . ALA A 1 202 ? 39.777 21.857 0.183 1.00 22.77 ? 202 ALA A C 1 ATOM 1575 O O . ALA A 1 202 ? 40.388 22.825 -0.341 1.00 21.21 ? 202 ALA A O 1 ATOM 1576 C CB . ALA A 1 202 ? 37.247 22.177 -0.164 1.00 20.07 ? 202 ALA A CB 1 ATOM 1577 N N . GLN A 1 203 ? 40.210 21.204 1.290 1.00 22.31 ? 203 GLN A N 1 ATOM 1578 C CA . GLN A 1 203 ? 41.345 21.718 2.139 1.00 28.51 ? 203 GLN A CA 1 ATOM 1579 C C . GLN A 1 203 ? 42.585 21.776 1.295 1.00 31.53 ? 203 GLN A C 1 ATOM 1580 O O . GLN A 1 203 ? 43.305 22.805 1.313 1.00 37.07 ? 203 GLN A O 1 ATOM 1581 C CB . GLN A 1 203 ? 41.641 20.934 3.441 1.00 29.18 ? 203 GLN A CB 1 ATOM 1582 C CG . GLN A 1 203 ? 40.501 20.221 4.227 1.00 37.65 ? 203 GLN A CG 1 ATOM 1583 C CD . GLN A 1 203 ? 41.036 19.036 5.145 1.00 41.06 ? 203 GLN A CD 1 ATOM 1584 O OE1 . GLN A 1 203 ? 41.808 19.300 6.082 1.00 47.56 ? 203 GLN A OE1 1 ATOM 1585 N NE2 . GLN A 1 203 ? 40.669 17.738 4.825 1.00 38.84 ? 203 GLN A NE2 1 ATOM 1586 N N . GLY A 1 204 ? 42.908 20.794 0.508 1.00 31.62 ? 204 GLY A N 1 ATOM 1587 C CA . GLY A 1 204 ? 44.067 21.163 -0.439 1.00 24.43 ? 204 GLY A CA 1 ATOM 1588 C C . GLY A 1 204 ? 43.752 21.591 -1.891 1.00 22.37 ? 204 GLY A C 1 ATOM 1589 O O . GLY A 1 204 ? 44.556 21.450 -2.872 1.00 23.20 ? 204 GLY A O 1 ATOM 1590 N N . ASN A 1 205 ? 42.577 22.155 -2.101 1.00 16.59 ? 205 ASN A N 1 ATOM 1591 C CA . ASN A 1 205 ? 42.046 22.509 -3.376 1.00 17.76 ? 205 ASN A CA 1 ATOM 1592 C C . ASN A 1 205 ? 41.463 23.936 -3.306 1.00 16.96 ? 205 ASN A C 1 ATOM 1593 O O . ASN A 1 205 ? 40.555 24.297 -4.094 1.00 18.49 ? 205 ASN A O 1 ATOM 1594 C CB . ASN A 1 205 ? 40.968 21.524 -3.835 1.00 21.67 ? 205 ASN A CB 1 ATOM 1595 C CG . ASN A 1 205 ? 40.673 21.608 -5.324 1.00 23.24 ? 205 ASN A CG 1 ATOM 1596 O OD1 . ASN A 1 205 ? 39.464 21.538 -5.770 1.00 28.32 ? 205 ASN A OD1 1 ATOM 1597 N ND2 . ASN A 1 205 ? 41.757 21.730 -6.193 1.00 22.02 ? 205 ASN A ND2 1 ATOM 1598 N N . ASN A 1 206 ? 42.085 24.784 -2.484 1.00 18.50 ? 206 ASN A N 1 ATOM 1599 C CA . ASN A 1 206 ? 41.696 26.230 -2.376 1.00 18.58 ? 206 ASN A CA 1 ATOM 1600 C C . ASN A 1 206 ? 40.232 26.441 -2.064 1.00 18.16 ? 206 ASN A C 1 ATOM 1601 O O . ASN A 1 206 ? 39.640 27.418 -2.510 1.00 19.97 ? 206 ASN A O 1 ATOM 1602 C CB . ASN A 1 206 ? 42.064 26.974 -3.648 1.00 17.94 ? 206 ASN A CB 1 ATOM 1603 C CG . ASN A 1 206 ? 43.579 27.004 -3.840 1.00 15.85 ? 206 ASN A CG 1 ATOM 1604 O OD1 . ASN A 1 206 ? 44.310 27.316 -2.844 1.00 20.11 ? 206 ASN A OD1 1 ATOM 1605 N ND2 . ASN A 1 206 ? 44.022 26.661 -5.052 1.00 17.31 ? 206 ASN A ND2 1 ATOM 1606 N N . GLY A 1 207 ? 39.684 25.534 -1.265 1.00 16.59 ? 207 GLY A N 1 ATOM 1607 C CA . GLY A 1 207 ? 38.254 25.769 -0.821 1.00 18.38 ? 207 GLY A CA 1 ATOM 1608 C C . GLY A 1 207 ? 37.254 25.241 -1.858 1.00 21.47 ? 207 GLY A C 1 ATOM 1609 O O . GLY A 1 207 ? 36.057 25.382 -1.628 1.00 21.91 ? 207 GLY A O 1 ATOM 1610 N N . VAL A 1 208 ? 37.721 24.669 -2.974 1.00 20.40 ? 208 VAL A N 1 ATOM 1611 C CA . VAL A 1 208 ? 36.844 24.237 -4.066 1.00 22.14 ? 208 VAL A CA 1 ATOM 1612 C C . VAL A 1 208 ? 36.545 22.732 -3.994 1.00 23.04 ? 208 VAL A C 1 ATOM 1613 O O . VAL A 1 208 ? 37.452 21.940 -3.780 1.00 21.22 ? 208 VAL A O 1 ATOM 1614 C CB . VAL A 1 208 ? 37.509 24.585 -5.501 1.00 23.38 ? 208 VAL A CB 1 ATOM 1615 C CG1 . VAL A 1 208 ? 36.682 24.012 -6.654 1.00 26.43 ? 208 VAL A CG1 1 ATOM 1616 C CG2 . VAL A 1 208 ? 37.628 26.130 -5.649 1.00 25.03 ? 208 VAL A CG2 1 ATOM 1617 N N . PHE A 1 209 ? 35.237 22.339 -4.094 1.00 22.55 ? 209 PHE A N 1 ATOM 1618 C CA . PHE A 1 209 ? 34.943 20.925 -4.115 1.00 23.51 ? 209 PHE A CA 1 ATOM 1619 C C . PHE A 1 209 ? 35.541 20.249 -5.366 1.00 24.95 ? 209 PHE A C 1 ATOM 1620 O O . PHE A 1 209 ? 35.435 20.771 -6.492 1.00 25.78 ? 209 PHE A O 1 ATOM 1621 C CB . PHE A 1 209 ? 33.408 20.699 -4.206 1.00 22.04 ? 209 PHE A CB 1 ATOM 1622 C CG . PHE A 1 209 ? 32.665 20.995 -2.930 1.00 22.78 ? 209 PHE A CG 1 ATOM 1623 C CD1 . PHE A 1 209 ? 33.293 21.631 -1.864 1.00 19.57 ? 209 PHE A CD1 1 ATOM 1624 C CD2 . PHE A 1 209 ? 31.282 20.730 -2.842 1.00 20.68 ? 209 PHE A CD2 1 ATOM 1625 C CE1 . PHE A 1 209 ? 32.607 21.949 -0.645 1.00 22.10 ? 209 PHE A CE1 1 ATOM 1626 C CE2 . PHE A 1 209 ? 30.589 21.075 -1.648 1.00 19.99 ? 209 PHE A CE2 1 ATOM 1627 C CZ . PHE A 1 209 ? 31.177 21.633 -0.564 1.00 19.82 ? 209 PHE A CZ 1 ATOM 1628 N N . ARG A 1 210 ? 36.091 19.062 -5.167 1.00 26.29 ? 210 ARG A N 1 ATOM 1629 C CA . ARG A 1 210 ? 36.483 18.241 -6.362 1.00 27.53 ? 210 ARG A CA 1 ATOM 1630 C C . ARG A 1 210 ? 35.275 17.838 -7.200 1.00 28.36 ? 210 ARG A C 1 ATOM 1631 O O . ARG A 1 210 ? 35.387 17.787 -8.410 1.00 28.82 ? 210 ARG A O 1 ATOM 1632 C CB . ARG A 1 210 ? 37.281 16.990 -6.015 1.00 26.87 ? 210 ARG A CB 1 ATOM 1633 C CG . ARG A 1 210 ? 38.635 17.269 -5.260 1.00 29.54 ? 210 ARG A CG 1 ATOM 1634 C CD . ARG A 1 210 ? 39.829 17.543 -6.248 1.00 34.48 ? 210 ARG A CD 1 ATOM 1635 N NE . ARG A 1 210 ? 41.002 17.982 -5.487 1.00 34.03 ? 210 ARG A NE 1 ATOM 1636 C CZ . ARG A 1 210 ? 42.140 18.443 -6.031 1.00 29.57 ? 210 ARG A CZ 1 ATOM 1637 N NH1 . ARG A 1 210 ? 42.242 18.507 -7.338 1.00 26.22 ? 210 ARG A NH1 1 ATOM 1638 N NH2 . ARG A 1 210 ? 43.137 18.807 -5.237 1.00 27.84 ? 210 ARG A NH2 1 ATOM 1639 N N . THR A 1 211 ? 34.114 17.611 -6.576 1.00 27.30 ? 211 THR A N 1 ATOM 1640 C CA . THR A 1 211 ? 32.870 17.246 -7.284 1.00 28.75 ? 211 THR A CA 1 ATOM 1641 C C . THR A 1 211 ? 31.689 18.010 -6.645 1.00 27.97 ? 211 THR A C 1 ATOM 1642 O O . THR A 1 211 ? 31.546 17.950 -5.450 1.00 26.38 ? 211 THR A O 1 ATOM 1643 C CB . THR A 1 211 ? 32.576 15.727 -7.150 1.00 29.85 ? 211 THR A CB 1 ATOM 1644 O OG1 . THR A 1 211 ? 33.701 14.945 -7.592 1.00 34.84 ? 211 THR A OG1 1 ATOM 1645 C CG2 . THR A 1 211 ? 31.330 15.263 -7.897 1.00 29.90 ? 211 THR A CG2 1 ATOM 1646 N N . PRO A 1 212 ? 30.881 18.700 -7.433 1.00 29.15 ? 212 PRO A N 1 ATOM 1647 C CA . PRO A 1 212 ? 29.781 19.487 -6.863 1.00 29.08 ? 212 PRO A CA 1 ATOM 1648 C C . PRO A 1 212 ? 28.792 18.537 -6.215 1.00 28.04 ? 212 PRO A C 1 ATOM 1649 O O . PRO A 1 212 ? 28.636 17.326 -6.614 1.00 28.85 ? 212 PRO A O 1 ATOM 1650 C CB . PRO A 1 212 ? 29.146 20.137 -8.082 1.00 30.88 ? 212 PRO A CB 1 ATOM 1651 C CG . PRO A 1 212 ? 30.379 20.344 -9.001 1.00 32.54 ? 212 PRO A CG 1 ATOM 1652 C CD . PRO A 1 212 ? 31.071 19.005 -8.881 1.00 31.60 ? 212 PRO A CD 1 ATOM 1653 N N . THR A 1 213 ? 28.195 19.062 -5.182 1.00 25.74 ? 213 THR A N 1 ATOM 1654 C CA . THR A 1 213 ? 27.101 18.394 -4.496 1.00 26.70 ? 213 THR A CA 1 ATOM 1655 C C . THR A 1 213 ? 25.793 19.077 -4.885 1.00 26.03 ? 213 THR A C 1 ATOM 1656 O O . THR A 1 213 ? 25.608 20.315 -4.814 1.00 25.64 ? 213 THR A O 1 ATOM 1657 C CB . THR A 1 213 ? 27.276 18.455 -2.966 1.00 27.04 ? 213 THR A CB 1 ATOM 1658 O OG1 . THR A 1 213 ? 28.442 17.702 -2.567 1.00 29.87 ? 213 THR A OG1 1 ATOM 1659 C CG2 . THR A 1 213 ? 25.921 17.959 -2.196 1.00 26.95 ? 213 THR A CG2 1 ATOM 1660 N N . VAL A 1 214 ? 24.805 18.260 -5.249 1.00 24.56 ? 214 VAL A N 1 ATOM 1661 C CA . VAL A 1 214 ? 23.467 18.831 -5.643 1.00 25.15 ? 214 VAL A CA 1 ATOM 1662 C C . VAL A 1 214 ? 22.530 18.702 -4.437 1.00 21.84 ? 214 VAL A C 1 ATOM 1663 O O . VAL A 1 214 ? 22.390 17.601 -3.880 1.00 25.56 ? 214 VAL A O 1 ATOM 1664 C CB . VAL A 1 214 ? 22.845 18.050 -6.894 1.00 25.08 ? 214 VAL A CB 1 ATOM 1665 C CG1 . VAL A 1 214 ? 21.382 18.439 -7.114 1.00 27.94 ? 214 VAL A CG1 1 ATOM 1666 C CG2 . VAL A 1 214 ? 23.724 18.396 -8.116 1.00 30.47 ? 214 VAL A CG2 1 ATOM 1667 N N . LEU A 1 215 ? 21.965 19.829 -4.038 1.00 24.02 ? 215 LEU A N 1 ATOM 1668 C CA . LEU A 1 215 ? 20.970 19.872 -2.949 1.00 23.85 ? 215 LEU A CA 1 ATOM 1669 C C . LEU A 1 215 ? 19.661 20.499 -3.428 1.00 26.69 ? 215 LEU A C 1 ATOM 1670 O O . LEU A 1 215 ? 19.614 21.270 -4.396 1.00 28.22 ? 215 LEU A O 1 ATOM 1671 C CB . LEU A 1 215 ? 21.487 20.663 -1.754 1.00 23.25 ? 215 LEU A CB 1 ATOM 1672 C CG . LEU A 1 215 ? 22.790 20.219 -1.116 1.00 22.88 ? 215 LEU A CG 1 ATOM 1673 C CD1 . LEU A 1 215 ? 23.027 21.221 0.052 1.00 23.07 ? 215 LEU A CD1 1 ATOM 1674 C CD2 . LEU A 1 215 ? 22.659 18.836 -0.596 1.00 27.18 ? 215 LEU A CD2 1 ATOM 1675 N N . VAL A 1 216 ? 18.580 20.194 -2.703 1.00 26.39 ? 216 VAL A N 1 ATOM 1676 C CA . VAL A 1 216 ? 17.329 20.926 -2.846 1.00 26.99 ? 216 VAL A CA 1 ATOM 1677 C C . VAL A 1 216 ? 17.318 22.041 -1.792 1.00 28.17 ? 216 VAL A C 1 ATOM 1678 O O . VAL A 1 216 ? 17.546 21.806 -0.602 1.00 27.38 ? 216 VAL A O 1 ATOM 1679 C CB . VAL A 1 216 ? 16.166 19.976 -2.637 1.00 27.32 ? 216 VAL A CB 1 ATOM 1680 C CG1 . VAL A 1 216 ? 14.816 20.778 -2.850 1.00 30.69 ? 216 VAL A CG1 1 ATOM 1681 C CG2 . VAL A 1 216 ? 16.332 18.651 -3.501 1.00 26.87 ? 216 VAL A CG2 1 ATOM 1682 N N . ASP A 1 217 ? 17.056 23.268 -2.224 1.00 29.95 ? 217 ASP A N 1 ATOM 1683 C CA . ASP A 1 217 ? 16.992 24.375 -1.291 1.00 33.81 ? 217 ASP A CA 1 ATOM 1684 C C . ASP A 1 217 ? 15.597 24.502 -0.642 1.00 34.61 ? 217 ASP A C 1 ATOM 1685 O O . ASP A 1 217 ? 14.674 23.726 -0.944 1.00 32.35 ? 217 ASP A O 1 ATOM 1686 C CB . ASP A 1 217 ? 17.436 25.727 -1.968 1.00 35.09 ? 217 ASP A CB 1 ATOM 1687 C CG . ASP A 1 217 ? 16.462 26.186 -3.071 1.00 41.40 ? 217 ASP A CG 1 ATOM 1688 O OD1 . ASP A 1 217 ? 15.226 25.858 -3.069 1.00 41.50 ? 217 ASP A OD1 1 ATOM 1689 O OD2 . ASP A 1 217 ? 16.943 26.904 -3.994 1.00 47.46 ? 217 ASP A OD2 1 ATOM 1690 N N . SER A 1 218 ? 15.484 25.492 0.236 1.00 37.67 ? 218 SER A N 1 ATOM 1691 C CA . SER A 1 218 ? 14.257 25.789 1.017 1.00 42.38 ? 218 SER A CA 1 ATOM 1692 C C . SER A 1 218 ? 13.015 26.074 0.149 1.00 43.28 ? 218 SER A C 1 ATOM 1693 O O . SER A 1 218 ? 11.903 26.116 0.644 1.00 43.65 ? 218 SER A O 1 ATOM 1694 C CB . SER A 1 218 ? 14.542 27.004 1.883 1.00 44.08 ? 218 SER A CB 1 ATOM 1695 O OG . SER A 1 218 ? 14.189 26.760 3.238 1.00 48.87 ? 218 SER A OG 1 ATOM 1696 N N . LYS A 1 219 ? 13.205 26.244 -1.160 1.00 44.42 ? 219 LYS A N 1 ATOM 1697 C CA . LYS A 1 219 ? 12.086 26.562 -2.064 1.00 45.52 ? 219 LYS A CA 1 ATOM 1698 C C . LYS A 1 219 ? 11.737 25.411 -2.964 1.00 44.96 ? 219 LYS A C 1 ATOM 1699 O O . LYS A 1 219 ? 10.826 25.532 -3.774 1.00 46.68 ? 219 LYS A O 1 ATOM 1700 C CB . LYS A 1 219 ? 12.382 27.844 -2.901 1.00 46.71 ? 219 LYS A CB 1 ATOM 1701 C CG . LYS A 1 219 ? 12.530 29.091 -2.026 1.00 50.43 ? 219 LYS A CG 1 ATOM 1702 C CD . LYS A 1 219 ? 12.276 30.350 -2.788 1.00 56.03 ? 219 LYS A CD 1 ATOM 1703 C CE . LYS A 1 219 ? 11.330 31.270 -2.021 1.00 58.52 ? 219 LYS A CE 1 ATOM 1704 N NZ . LYS A 1 219 ? 11.917 31.711 -0.712 1.00 58.91 ? 219 LYS A NZ 1 ATOM 1705 N N . GLY A 1 220 ? 12.447 24.293 -2.843 1.00 42.21 ? 220 GLY A N 1 ATOM 1706 C CA . GLY A 1 220 ? 12.170 23.155 -3.685 1.00 42.32 ? 220 GLY A CA 1 ATOM 1707 C C . GLY A 1 220 ? 13.028 23.070 -4.940 1.00 42.00 ? 220 GLY A C 1 ATOM 1708 O O . GLY A 1 220 ? 12.957 22.046 -5.691 1.00 41.46 ? 220 GLY A O 1 ATOM 1709 N N . ASN A 1 221 ? 13.876 24.108 -5.088 1.00 42.47 ? 221 ASN A N 1 ATOM 1710 C CA . ASN A 1 221 ? 14.828 24.320 -6.238 1.00 42.86 ? 221 ASN A CA 1 ATOM 1711 C C . ASN A 1 221 ? 16.133 23.498 -6.047 1.00 41.38 ? 221 ASN A C 1 ATOM 1712 O O . ASN A 1 221 ? 16.728 23.613 -4.970 1.00 40.40 ? 221 ASN A O 1 ATOM 1713 C CB . ASN A 1 221 ? 15.170 25.842 -6.302 1.00 42.96 ? 221 ASN A CB 1 ATOM 1714 C CG . ASN A 1 221 ? 13.982 26.702 -6.731 1.00 44.78 ? 221 ASN A CG 1 ATOM 1715 O OD1 . ASN A 1 221 ? 13.246 26.306 -7.606 1.00 46.75 ? 221 ASN A OD1 1 ATOM 1716 N ND2 . ASN A 1 221 ? 13.789 27.865 -6.095 1.00 46.50 ? 221 ASN A ND2 1 ATOM 1717 N N . ARG A 1 222 ? 16.531 22.671 -7.037 1.00 41.00 ? 222 ARG A N 1 ATOM 1718 C CA . ARG A 1 222 ? 17.768 21.870 -6.978 1.00 41.23 ? 222 ARG A CA 1 ATOM 1719 C C . ARG A 1 222 ? 18.969 22.810 -7.285 1.00 40.17 ? 222 ARG A C 1 ATOM 1720 O O . ARG A 1 222 ? 18.905 23.626 -8.224 1.00 40.05 ? 222 ARG A O 1 ATOM 1721 C CB . ARG A 1 222 ? 17.756 20.674 -7.950 1.00 42.36 ? 222 ARG A CB 1 ATOM 1722 C CG . ARG A 1 222 ? 18.672 20.977 -9.206 1.00 47.74 ? 222 ARG A CG 1 ATOM 1723 C CD . ARG A 1 222 ? 19.045 19.784 -10.147 1.00 50.75 ? 222 ARG A CD 1 ATOM 1724 N NE . ARG A 1 222 ? 20.421 19.802 -10.726 1.00 55.42 ? 222 ARG A NE 1 ATOM 1725 C CZ . ARG A 1 222 ? 21.275 20.847 -10.850 1.00 56.33 ? 222 ARG A CZ 1 ATOM 1726 N NH1 . ARG A 1 222 ? 22.452 20.639 -11.412 1.00 53.16 ? 222 ARG A NH1 1 ATOM 1727 N NH2 . ARG A 1 222 ? 20.980 22.097 -10.459 1.00 58.85 ? 222 ARG A NH2 1 ATOM 1728 N N . VAL A 1 223 ? 20.046 22.720 -6.485 1.00 37.19 ? 223 VAL A N 1 ATOM 1729 C CA . VAL A 1 223 ? 21.134 23.736 -6.555 1.00 35.87 ? 223 VAL A CA 1 ATOM 1730 C C . VAL A 1 223 ? 22.465 22.978 -6.428 1.00 34.21 ? 223 VAL A C 1 ATOM 1731 O O . VAL A 1 223 ? 22.503 21.973 -5.746 1.00 32.08 ? 223 VAL A O 1 ATOM 1732 C CB . VAL A 1 223 ? 20.966 24.849 -5.493 1.00 34.65 ? 223 VAL A CB 1 ATOM 1733 C CG1 . VAL A 1 223 ? 21.180 24.342 -4.095 1.00 35.25 ? 223 VAL A CG1 1 ATOM 1734 C CG2 . VAL A 1 223 ? 21.981 25.884 -5.662 1.00 41.26 ? 223 VAL A CG2 1 ATOM 1735 N N . GLN A 1 224 ? 23.533 23.462 -7.073 1.00 31.37 ? 224 GLN A N 1 ATOM 1736 C CA . GLN A 1 224 ? 24.865 22.874 -6.981 1.00 31.58 ? 224 GLN A CA 1 ATOM 1737 C C . GLN A 1 224 ? 25.731 23.573 -5.914 1.00 29.26 ? 224 GLN A C 1 ATOM 1738 O O . GLN A 1 224 ? 25.888 24.822 -5.909 1.00 30.30 ? 224 GLN A O 1 ATOM 1739 C CB . GLN A 1 224 ? 25.625 22.968 -8.325 1.00 33.14 ? 224 GLN A CB 1 ATOM 1740 C CG . GLN A 1 224 ? 24.958 22.252 -9.442 1.00 38.43 ? 224 GLN A CG 1 ATOM 1741 C CD . GLN A 1 224 ? 25.986 21.495 -10.294 1.00 45.45 ? 224 GLN A CD 1 ATOM 1742 O OE1 . GLN A 1 224 ? 27.083 22.031 -10.565 1.00 47.85 ? 224 GLN A OE1 1 ATOM 1743 N NE2 . GLN A 1 224 ? 25.638 20.231 -10.718 1.00 48.53 ? 224 GLN A NE2 1 ATOM 1744 N N . ILE A 1 225 ? 26.300 22.778 -5.007 1.00 26.50 ? 225 ILE A N 1 ATOM 1745 C CA . ILE A 1 225 ? 27.239 23.394 -3.968 1.00 24.39 ? 225 ILE A CA 1 ATOM 1746 C C . ILE A 1 225 ? 28.636 23.080 -4.535 1.00 25.06 ? 225 ILE A C 1 ATOM 1747 O O . ILE A 1 225 ? 28.903 21.968 -4.880 1.00 24.55 ? 225 ILE A O 1 ATOM 1748 C CB . ILE A 1 225 ? 27.015 22.796 -2.579 1.00 23.12 ? 225 ILE A CB 1 ATOM 1749 C CG1 . ILE A 1 225 ? 25.480 22.849 -2.245 1.00 24.51 ? 225 ILE A CG1 1 ATOM 1750 C CG2 . ILE A 1 225 ? 27.930 23.441 -1.483 1.00 24.60 ? 225 ILE A CG2 1 ATOM 1751 C CD1 . ILE A 1 225 ? 24.926 24.236 -2.177 1.00 26.95 ? 225 ILE A CD1 1 ATOM 1752 N N . THR A 1 226 ? 29.493 24.097 -4.709 1.00 24.69 ? 226 THR A N 1 ATOM 1753 C CA . THR A 1 226 ? 30.754 23.859 -5.461 1.00 25.40 ? 226 THR A CA 1 ATOM 1754 C C . THR A 1 226 ? 31.980 24.221 -4.637 1.00 24.48 ? 226 THR A C 1 ATOM 1755 O O . THR A 1 226 ? 33.074 23.837 -5.010 1.00 25.08 ? 226 THR A O 1 ATOM 1756 C CB . THR A 1 226 ? 30.843 24.664 -6.805 1.00 26.79 ? 226 THR A CB 1 ATOM 1757 O OG1 . THR A 1 226 ? 30.655 26.067 -6.545 1.00 27.30 ? 226 THR A OG1 1 ATOM 1758 C CG2 . THR A 1 226 ? 29.783 24.118 -7.841 1.00 27.69 ? 226 THR A CG2 1 ATOM 1759 N N . ASN A 1 227 ? 31.795 24.954 -3.565 1.00 22.08 ? 227 ASN A N 1 ATOM 1760 C CA . ASN A 1 227 ? 32.912 25.395 -2.721 1.00 22.19 ? 227 ASN A CA 1 ATOM 1761 C C . ASN A 1 227 ? 32.478 25.786 -1.312 1.00 21.73 ? 227 ASN A C 1 ATOM 1762 O O . ASN A 1 227 ? 31.235 25.805 -1.014 1.00 22.89 ? 227 ASN A O 1 ATOM 1763 C CB . ASN A 1 227 ? 33.641 26.569 -3.464 1.00 21.65 ? 227 ASN A CB 1 ATOM 1764 C CG . ASN A 1 227 ? 32.798 27.864 -3.524 1.00 22.83 ? 227 ASN A CG 1 ATOM 1765 O OD1 . ASN A 1 227 ? 32.663 28.569 -2.518 1.00 23.68 ? 227 ASN A OD1 1 ATOM 1766 N ND2 . ASN A 1 227 ? 32.266 28.169 -4.703 1.00 29.92 ? 227 ASN A ND2 1 ATOM 1767 N N . VAL A 1 228 ? 33.446 26.056 -0.435 1.00 18.96 ? 228 VAL A N 1 ATOM 1768 C CA . VAL A 1 228 ? 33.211 26.224 1.030 1.00 19.89 ? 228 VAL A CA 1 ATOM 1769 C C . VAL A 1 228 ? 32.564 27.573 1.411 1.00 19.96 ? 228 VAL A C 1 ATOM 1770 O O . VAL A 1 228 ? 32.337 27.819 2.604 1.00 22.82 ? 228 VAL A O 1 ATOM 1771 C CB . VAL A 1 228 ? 34.463 26.035 1.853 1.00 21.49 ? 228 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 228 ? 34.961 24.526 1.784 1.00 21.16 ? 228 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 228 ? 35.575 27.076 1.356 1.00 19.47 ? 228 VAL A CG2 1 ATOM 1774 N N . THR A 1 229 ? 32.433 28.461 0.408 1.00 21.33 ? 229 THR A N 1 ATOM 1775 C CA . THR A 1 229 ? 31.721 29.716 0.684 1.00 23.52 ? 229 THR A CA 1 ATOM 1776 C C . THR A 1 229 ? 30.197 29.516 0.705 1.00 23.60 ? 229 THR A C 1 ATOM 1777 O O . THR A 1 229 ? 29.510 30.452 1.088 1.00 24.90 ? 229 THR A O 1 ATOM 1778 C CB . THR A 1 229 ? 32.003 30.891 -0.298 1.00 21.88 ? 229 THR A CB 1 ATOM 1779 O OG1 . THR A 1 229 ? 31.359 30.696 -1.592 1.00 26.99 ? 229 THR A OG1 1 ATOM 1780 C CG2 . THR A 1 229 ? 33.519 31.092 -0.428 1.00 25.33 ? 229 THR A CG2 1 ATOM 1781 N N . SER A 1 230 ? 29.693 28.343 0.272 1.00 23.13 ? 230 SER A N 1 ATOM 1782 C CA . SER A 1 230 ? 28.254 28.161 0.277 1.00 24.23 ? 230 SER A CA 1 ATOM 1783 C C . SER A 1 230 ? 27.660 28.135 1.719 1.00 22.88 ? 230 SER A C 1 ATOM 1784 O O . SER A 1 230 ? 28.352 27.776 2.747 1.00 19.95 ? 230 SER A O 1 ATOM 1785 C CB . SER A 1 230 ? 27.851 26.933 -0.534 1.00 27.58 ? 230 SER A CB 1 ATOM 1786 O OG . SER A 1 230 ? 26.768 26.272 0.159 1.00 33.69 ? 230 SER A OG 1 ATOM 1787 N N . ASN A 1 231 ? 26.374 28.621 1.836 1.00 23.18 ? 231 ASN A N 1 ATOM 1788 C CA . ASN A 1 231 ? 25.787 28.751 3.170 1.00 23.40 ? 231 ASN A CA 1 ATOM 1789 C C . ASN A 1 231 ? 25.665 27.325 3.889 1.00 18.75 ? 231 ASN A C 1 ATOM 1790 O O . ASN A 1 231 ? 25.726 27.230 5.133 1.00 20.94 ? 231 ASN A O 1 ATOM 1791 C CB . ASN A 1 231 ? 24.361 29.396 3.059 1.00 24.27 ? 231 ASN A CB 1 ATOM 1792 C CG . ASN A 1 231 ? 24.426 30.984 3.025 1.00 35.97 ? 231 ASN A CG 1 ATOM 1793 O OD1 . ASN A 1 231 ? 25.422 31.613 3.451 1.00 48.33 ? 231 ASN A OD1 1 ATOM 1794 N ND2 . ASN A 1 231 ? 23.326 31.625 2.548 1.00 41.21 ? 231 ASN A ND2 1 ATOM 1795 N N . VAL A 1 232 ? 25.545 26.312 3.070 1.00 21.31 ? 232 VAL A N 1 ATOM 1796 C CA . VAL A 1 232 ? 25.508 24.918 3.610 1.00 19.61 ? 232 VAL A CA 1 ATOM 1797 C C . VAL A 1 232 ? 26.735 24.614 4.418 1.00 19.36 ? 232 VAL A C 1 ATOM 1798 O O . VAL A 1 232 ? 26.705 23.997 5.495 1.00 18.04 ? 232 VAL A O 1 ATOM 1799 C CB . VAL A 1 232 ? 25.348 23.853 2.552 1.00 23.12 ? 232 VAL A CB 1 ATOM 1800 C CG1 . VAL A 1 232 ? 25.035 22.502 3.264 1.00 24.11 ? 232 VAL A CG1 1 ATOM 1801 C CG2 . VAL A 1 232 ? 24.208 24.233 1.607 1.00 29.32 ? 232 VAL A CG2 1 ATOM 1802 N N . VAL A 1 233 ? 27.887 25.148 3.953 1.00 17.62 ? 233 VAL A N 1 ATOM 1803 C CA . VAL A 1 233 ? 29.164 24.910 4.637 1.00 18.15 ? 233 VAL A CA 1 ATOM 1804 C C . VAL A 1 233 ? 29.450 25.920 5.779 1.00 17.93 ? 233 VAL A C 1 ATOM 1805 O O . VAL A 1 233 ? 29.954 25.577 6.824 1.00 18.53 ? 233 VAL A O 1 ATOM 1806 C CB . VAL A 1 233 ? 30.355 24.922 3.556 1.00 17.63 ? 233 VAL A CB 1 ATOM 1807 C CG1 . VAL A 1 233 ? 31.647 24.607 4.264 1.00 19.77 ? 233 VAL A CG1 1 ATOM 1808 C CG2 . VAL A 1 233 ? 30.070 23.949 2.374 1.00 18.67 ? 233 VAL A CG2 1 ATOM 1809 N N . THR A 1 234 ? 29.082 27.207 5.565 1.00 19.27 ? 234 THR A N 1 ATOM 1810 C CA . THR A 1 234 ? 29.503 28.212 6.568 1.00 21.65 ? 234 THR A CA 1 ATOM 1811 C C . THR A 1 234 ? 28.522 28.260 7.696 1.00 20.08 ? 234 THR A C 1 ATOM 1812 O O . THR A 1 234 ? 28.881 28.675 8.766 1.00 23.70 ? 234 THR A O 1 ATOM 1813 C CB . THR A 1 234 ? 29.574 29.643 5.992 1.00 21.12 ? 234 THR A CB 1 ATOM 1814 O OG1 . THR A 1 234 ? 28.301 29.969 5.439 1.00 21.96 ? 234 THR A OG1 1 ATOM 1815 C CG2 . THR A 1 234 ? 30.477 29.672 4.812 1.00 23.94 ? 234 THR A CG2 1 ATOM 1816 N N . SER A 1 235 ? 27.284 27.794 7.456 1.00 22.72 ? 235 SER A N 1 ATOM 1817 C CA . SER A 1 235 ? 26.219 28.032 8.464 1.00 24.27 ? 235 SER A CA 1 ATOM 1818 C C . SER A 1 235 ? 25.537 26.708 8.976 1.00 27.18 ? 235 SER A C 1 ATOM 1819 O O . SER A 1 235 ? 25.346 26.491 10.226 1.00 31.08 ? 235 SER A O 1 ATOM 1820 C CB . SER A 1 235 ? 25.238 29.128 7.888 1.00 25.83 ? 235 SER A CB 1 ATOM 1821 O OG . SER A 1 235 ? 26.031 30.234 7.379 1.00 37.11 ? 235 SER A OG 1 ATOM 1822 N N . ASN A 1 236 ? 25.319 25.822 8.062 1.00 20.92 ? 236 ASN A N 1 ATOM 1823 C CA . ASN A 1 236 ? 24.377 24.695 8.269 1.00 19.51 ? 236 ASN A CA 1 ATOM 1824 C C . ASN A 1 236 ? 25.049 23.431 8.833 1.00 16.54 ? 236 ASN A C 1 ATOM 1825 O O . ASN A 1 236 ? 24.794 23.045 9.961 1.00 17.47 ? 236 ASN A O 1 ATOM 1826 C CB . ASN A 1 236 ? 23.733 24.471 6.911 1.00 18.43 ? 236 ASN A CB 1 ATOM 1827 C CG . ASN A 1 236 ? 22.534 23.525 6.964 1.00 20.54 ? 236 ASN A CG 1 ATOM 1828 O OD1 . ASN A 1 236 ? 22.292 22.869 7.941 1.00 19.80 ? 236 ASN A OD1 1 ATOM 1829 N ND2 . ASN A 1 236 ? 21.859 23.389 5.838 1.00 20.87 ? 236 ASN A ND2 1 ATOM 1830 N N . ILE A 1 237 ? 25.887 22.773 8.046 1.00 16.92 ? 237 ILE A N 1 ATOM 1831 C CA . ILE A 1 237 ? 26.549 21.559 8.550 1.00 15.88 ? 237 ILE A CA 1 ATOM 1832 C C . ILE A 1 237 ? 27.336 21.772 9.818 1.00 17.84 ? 237 ILE A C 1 ATOM 1833 O O . ILE A 1 237 ? 28.100 22.776 9.914 1.00 18.50 ? 237 ILE A O 1 ATOM 1834 C CB . ILE A 1 237 ? 27.359 20.869 7.426 1.00 15.99 ? 237 ILE A CB 1 ATOM 1835 C CG1 . ILE A 1 237 ? 27.767 19.406 7.773 1.00 14.70 ? 237 ILE A CG1 1 ATOM 1836 C CG2 . ILE A 1 237 ? 28.672 21.692 7.121 1.00 16.40 ? 237 ILE A CG2 1 ATOM 1837 C CD1 . ILE A 1 237 ? 28.189 18.583 6.497 1.00 19.04 ? 237 ILE A CD1 1 ATOM 1838 N N . GLN A 1 238 ? 27.222 20.824 10.793 1.00 15.73 ? 238 GLN A N 1 ATOM 1839 C CA . GLN A 1 238 ? 27.856 20.948 12.101 1.00 16.10 ? 238 GLN A CA 1 ATOM 1840 C C . GLN A 1 238 ? 28.848 19.880 12.419 1.00 16.84 ? 238 GLN A C 1 ATOM 1841 O O . GLN A 1 238 ? 29.580 20.020 13.469 1.00 18.10 ? 238 GLN A O 1 ATOM 1842 C CB . GLN A 1 238 ? 26.732 20.992 13.194 1.00 17.06 ? 238 GLN A CB 1 ATOM 1843 C CG . GLN A 1 238 ? 25.716 22.189 13.040 1.00 17.51 ? 238 GLN A CG 1 ATOM 1844 C CD . GLN A 1 238 ? 26.434 23.527 13.209 1.00 20.32 ? 238 GLN A CD 1 ATOM 1845 O OE1 . GLN A 1 238 ? 27.154 23.738 14.196 1.00 28.17 ? 238 GLN A OE1 1 ATOM 1846 N NE2 . GLN A 1 238 ? 26.234 24.419 12.267 1.00 21.32 ? 238 GLN A NE2 1 ATOM 1847 N N . LEU A 1 239 ? 28.913 18.799 11.608 1.00 15.41 ? 239 LEU A N 1 ATOM 1848 C CA . LEU A 1 239 ? 29.791 17.618 11.951 1.00 15.31 ? 239 LEU A CA 1 ATOM 1849 C C . LEU A 1 239 ? 30.168 17.082 10.566 1.00 15.13 ? 239 LEU A C 1 ATOM 1850 O O . LEU A 1 239 ? 29.361 17.044 9.594 1.00 17.07 ? 239 LEU A O 1 ATOM 1851 C CB . LEU A 1 239 ? 28.963 16.537 12.732 1.00 14.91 ? 239 LEU A CB 1 ATOM 1852 C CG . LEU A 1 239 ? 28.436 17.016 14.026 1.00 15.16 ? 239 LEU A CG 1 ATOM 1853 C CD1 . LEU A 1 239 ? 27.389 15.879 14.443 1.00 15.63 ? 239 LEU A CD1 1 ATOM 1854 C CD2 . LEU A 1 239 ? 29.492 17.072 15.108 1.00 16.87 ? 239 LEU A CD2 1 ATOM 1855 N N . LEU A 1 240 ? 31.439 16.751 10.423 1.00 16.70 ? 240 LEU A N 1 ATOM 1856 C CA . LEU A 1 240 ? 31.894 16.094 9.243 1.00 16.57 ? 240 LEU A CA 1 ATOM 1857 C C . LEU A 1 240 ? 32.236 14.595 9.440 1.00 17.44 ? 240 LEU A C 1 ATOM 1858 O O . LEU A 1 240 ? 33.044 14.248 10.326 1.00 18.63 ? 240 LEU A O 1 ATOM 1859 C CB . LEU A 1 240 ? 33.197 16.810 8.700 1.00 16.26 ? 240 LEU A CB 1 ATOM 1860 C CG . LEU A 1 240 ? 33.002 18.289 8.453 1.00 17.04 ? 240 LEU A CG 1 ATOM 1861 C CD1 . LEU A 1 240 ? 34.491 18.752 8.069 1.00 20.91 ? 240 LEU A CD1 1 ATOM 1862 C CD2 . LEU A 1 240 ? 32.001 18.637 7.318 1.00 17.03 ? 240 LEU A CD2 1 ATOM 1863 N N . LEU A 1 241 ? 31.639 13.752 8.604 1.00 17.38 ? 241 LEU A N 1 ATOM 1864 C CA . LEU A 1 241 ? 32.049 12.338 8.545 1.00 18.30 ? 241 LEU A CA 1 ATOM 1865 C C . LEU A 1 241 ? 33.528 12.293 8.058 1.00 17.34 ? 241 LEU A C 1 ATOM 1866 O O . LEU A 1 241 ? 33.780 12.863 6.982 1.00 19.76 ? 241 LEU A O 1 ATOM 1867 C CB . LEU A 1 241 ? 31.159 11.532 7.613 1.00 19.05 ? 241 LEU A CB 1 ATOM 1868 C CG . LEU A 1 241 ? 31.364 10.031 7.458 1.00 18.43 ? 241 LEU A CG 1 ATOM 1869 C CD1 . LEU A 1 241 ? 31.230 9.409 8.848 1.00 19.22 ? 241 LEU A CD1 1 ATOM 1870 C CD2 . LEU A 1 241 ? 30.354 9.456 6.407 1.00 21.29 ? 241 LEU A CD2 1 ATOM 1871 N N . ASN A 1 242 ? 34.400 11.589 8.785 1.00 20.15 ? 242 ASN A N 1 ATOM 1872 C CA . ASN A 1 242 ? 35.846 11.571 8.345 1.00 20.81 ? 242 ASN A CA 1 ATOM 1873 C C . ASN A 1 242 ? 35.967 10.817 7.008 1.00 22.36 ? 242 ASN A C 1 ATOM 1874 O O . ASN A 1 242 ? 35.322 9.806 6.838 1.00 23.17 ? 242 ASN A O 1 ATOM 1875 C CB . ASN A 1 242 ? 36.651 10.855 9.432 1.00 20.43 ? 242 ASN A CB 1 ATOM 1876 C CG . ASN A 1 242 ? 38.155 11.173 9.342 1.00 18.50 ? 242 ASN A CG 1 ATOM 1877 O OD1 . ASN A 1 242 ? 38.793 10.677 8.408 1.00 25.67 ? 242 ASN A OD1 1 ATOM 1878 N ND2 . ASN A 1 242 ? 38.661 11.857 10.303 1.00 23.09 ? 242 ASN A ND2 1 ATOM 1879 N N . THR A 1 243 ? 36.711 11.362 5.987 1.00 23.67 ? 243 THR A N 1 ATOM 1880 C CA . THR A 1 243 ? 36.852 10.634 4.697 1.00 26.07 ? 243 THR A CA 1 ATOM 1881 C C . THR A 1 243 ? 37.392 9.192 4.848 1.00 26.22 ? 243 THR A C 1 ATOM 1882 O O . THR A 1 243 ? 37.143 8.372 3.974 1.00 28.00 ? 243 THR A O 1 ATOM 1883 C CB . THR A 1 243 ? 37.780 11.344 3.636 1.00 26.77 ? 243 THR A CB 1 ATOM 1884 O OG1 . THR A 1 243 ? 39.002 11.600 4.338 1.00 31.19 ? 243 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 243 ? 37.118 12.606 3.234 1.00 30.67 ? 243 THR A CG2 1 ATOM 1886 N N . LYS A 1 244 ? 38.123 8.932 5.930 1.00 27.10 ? 244 LYS A N 1 ATOM 1887 C CA . LYS A 1 244 ? 38.596 7.555 6.248 1.00 30.67 ? 244 LYS A CA 1 ATOM 1888 C C . LYS A 1 244 ? 37.409 6.555 6.378 1.00 32.04 ? 244 LYS A C 1 ATOM 1889 O O . LYS A 1 244 ? 37.578 5.350 6.164 1.00 33.42 ? 244 LYS A O 1 ATOM 1890 C CB . LYS A 1 244 ? 39.543 7.524 7.460 1.00 30.01 ? 244 LYS A CB 1 ATOM 1891 C CG . LYS A 1 244 ? 40.936 8.147 7.125 1.00 38.09 ? 244 LYS A CG 1 ATOM 1892 C CD . LYS A 1 244 ? 42.019 8.180 8.264 1.00 45.56 ? 244 LYS A CD 1 ATOM 1893 C CE . LYS A 1 244 ? 42.675 6.774 8.619 1.00 48.55 ? 244 LYS A CE 1 ATOM 1894 N NZ . LYS A 1 244 ? 43.379 6.870 10.001 1.00 51.37 ? 244 LYS A NZ 1 ATOM 1895 N N . ASN A 1 245 ? 36.186 7.081 6.579 1.00 30.03 ? 245 ASN A N 1 ATOM 1896 C CA . ASN A 1 245 ? 34.955 6.279 6.715 1.00 31.74 ? 245 ASN A CA 1 ATOM 1897 C C . ASN A 1 245 ? 34.035 6.413 5.516 1.00 32.37 ? 245 ASN A C 1 ATOM 1898 O O . ASN A 1 245 ? 32.875 6.001 5.575 1.00 33.39 ? 245 ASN A O 1 ATOM 1899 C CB . ASN A 1 245 ? 34.270 6.638 8.053 1.00 30.66 ? 245 ASN A CB 1 ATOM 1900 C CG . ASN A 1 245 ? 35.102 6.216 9.238 1.00 29.93 ? 245 ASN A CG 1 ATOM 1901 O OD1 . ASN A 1 245 ? 35.646 5.082 9.243 1.00 34.16 ? 245 ASN A OD1 1 ATOM 1902 N ND2 . ASN A 1 245 ? 35.244 7.063 10.217 1.00 29.07 ? 245 ASN A ND2 1 ATOM 1903 N N . ILE A 1 246 ? 34.554 6.960 4.414 1.00 32.73 ? 246 ILE A N 1 ATOM 1904 C CA . ILE A 1 246 ? 33.738 7.208 3.268 1.00 32.70 ? 246 ILE A CA 1 ATOM 1905 C C . ILE A 1 246 ? 34.319 6.457 2.069 1.00 35.49 ? 246 ILE A C 1 ATOM 1906 O O . ILE A 1 246 ? 33.544 5.730 1.424 1.00 38.08 ? 246 ILE A O 1 ATOM 1907 C CB . ILE A 1 246 ? 33.632 8.708 2.930 1.00 32.40 ? 246 ILE A CB 1 ATOM 1908 C CG1 . ILE A 1 246 ? 33.142 9.527 4.157 1.00 28.31 ? 246 ILE A CG1 1 ATOM 1909 C CG2 . ILE A 1 246 ? 32.749 8.924 1.725 1.00 29.25 ? 246 ILE A CG2 1 ATOM 1910 C CD1 . ILE A 1 246 ? 33.073 11.073 3.931 1.00 25.07 ? 246 ILE A CD1 1 ATOM 1911 O OXT . ILE A 1 246 ? 35.517 6.607 1.702 1.00 36.06 ? 246 ILE A OXT 1 HETATM 1912 C C1 . NAG B 2 . ? 31.452 29.328 -5.024 1.00 41.93 ? 301 NAG A C1 1 HETATM 1913 C C2 . NAG B 2 . ? 31.511 29.789 -6.482 1.00 41.46 ? 301 NAG A C2 1 HETATM 1914 C C3 . NAG B 2 . ? 30.719 31.103 -6.645 1.00 43.29 ? 301 NAG A C3 1 HETATM 1915 C C4 . NAG B 2 . ? 29.301 30.727 -6.268 1.00 43.72 ? 301 NAG A C4 1 HETATM 1916 C C5 . NAG B 2 . ? 29.229 30.383 -4.779 1.00 41.14 ? 301 NAG A C5 1 HETATM 1917 C C6 . NAG B 2 . ? 27.822 29.849 -4.516 1.00 40.99 ? 301 NAG A C6 1 HETATM 1918 C C7 . NAG B 2 . ? 33.731 28.918 -7.179 1.00 46.40 ? 301 NAG A C7 1 HETATM 1919 C C8 . NAG B 2 . ? 35.182 29.329 -7.357 1.00 45.02 ? 301 NAG A C8 1 HETATM 1920 N N2 . NAG B 2 . ? 32.942 29.925 -6.755 1.00 40.35 ? 301 NAG A N2 1 HETATM 1921 O O3 . NAG B 2 . ? 30.774 31.807 -7.902 1.00 47.61 ? 301 NAG A O3 1 HETATM 1922 O O4 . NAG B 2 . ? 28.455 31.826 -6.557 1.00 49.60 ? 301 NAG A O4 1 HETATM 1923 O O5 . NAG B 2 . ? 30.180 29.391 -4.363 1.00 45.58 ? 301 NAG A O5 1 HETATM 1924 O O6 . NAG B 2 . ? 27.643 29.790 -3.138 1.00 40.06 ? 301 NAG A O6 1 HETATM 1925 O O7 . NAG B 2 . ? 33.338 27.727 -7.392 1.00 45.96 ? 301 NAG A O7 1 HETATM 1926 C C1 . GOL C 3 . ? 5.614 17.543 22.084 1.00 27.83 ? 302 GOL A C1 1 HETATM 1927 O O1 . GOL C 3 . ? 4.228 17.564 22.329 1.00 26.15 ? 302 GOL A O1 1 HETATM 1928 C C2 . GOL C 3 . ? 6.324 17.891 23.420 1.00 24.62 ? 302 GOL A C2 1 HETATM 1929 O O2 . GOL C 3 . ? 6.096 16.850 24.386 1.00 20.18 ? 302 GOL A O2 1 HETATM 1930 C C3 . GOL C 3 . ? 5.875 19.288 23.893 1.00 25.67 ? 302 GOL A C3 1 HETATM 1931 O O3 . GOL C 3 . ? 6.404 19.583 25.178 1.00 20.69 ? 302 GOL A O3 1 HETATM 1932 C C1 . GOL D 3 . ? 29.829 25.248 12.958 1.00 30.23 ? 303 GOL A C1 1 HETATM 1933 O O1 . GOL D 3 . ? 29.047 26.099 13.820 1.00 31.55 ? 303 GOL A O1 1 HETATM 1934 C C2 . GOL D 3 . ? 29.939 25.964 11.626 1.00 35.08 ? 303 GOL A C2 1 HETATM 1935 O O2 . GOL D 3 . ? 28.688 26.544 11.357 1.00 29.89 ? 303 GOL A O2 1 HETATM 1936 C C3 . GOL D 3 . ? 31.094 26.987 11.719 1.00 30.40 ? 303 GOL A C3 1 HETATM 1937 O O3 . GOL D 3 . ? 31.341 27.853 10.603 1.00 34.86 ? 303 GOL A O3 1 HETATM 1938 C C1 . NAG E 2 . ? 20.435 5.632 9.288 0.50 39.33 ? 304 NAG A C1 1 HETATM 1939 C C2 . NAG E 2 . ? 21.523 6.571 9.591 0.50 34.95 ? 304 NAG A C2 1 HETATM 1940 C C3 . NAG E 2 . ? 21.649 7.765 8.687 0.50 34.00 ? 304 NAG A C3 1 HETATM 1941 C C4 . NAG E 2 . ? 21.954 7.166 7.307 0.50 38.08 ? 304 NAG A C4 1 HETATM 1942 C C5 . NAG E 2 . ? 20.880 6.147 7.005 0.50 35.01 ? 304 NAG A C5 1 HETATM 1943 C C6 . NAG E 2 . ? 21.431 5.357 5.869 0.50 29.36 ? 304 NAG A C6 1 HETATM 1944 C C7 . NAG E 2 . ? 21.489 6.471 12.105 0.50 27.62 ? 304 NAG A C7 1 HETATM 1945 C C8 . NAG E 2 . ? 21.627 7.482 13.243 0.50 14.82 ? 304 NAG A C8 1 HETATM 1946 N N2 . NAG E 2 . ? 21.530 7.050 10.933 0.50 33.70 ? 304 NAG A N2 1 HETATM 1947 O O1 . NAG E 2 . ? 20.724 4.599 10.227 0.50 43.04 ? 304 NAG A O1 1 HETATM 1948 O O3 . NAG E 2 . ? 22.793 8.293 9.305 0.50 24.46 ? 304 NAG A O3 1 HETATM 1949 O O4 . NAG E 2 . ? 22.024 8.018 6.148 0.50 38.67 ? 304 NAG A O4 1 HETATM 1950 O O5 . NAG E 2 . ? 20.855 5.217 8.028 0.50 41.38 ? 304 NAG A O5 1 HETATM 1951 O O6 . NAG E 2 . ? 20.617 5.392 4.783 0.50 29.87 ? 304 NAG A O6 1 HETATM 1952 O O7 . NAG E 2 . ? 21.410 5.306 12.253 0.50 30.71 ? 304 NAG A O7 1 HETATM 1953 O O . HOH F 4 . ? 11.513 5.723 33.707 1.00 53.50 ? 401 HOH A O 1 HETATM 1954 O O . HOH F 4 . ? 20.254 -6.748 7.038 1.00 56.48 ? 402 HOH A O 1 HETATM 1955 O O . HOH F 4 . ? 13.229 8.622 1.099 1.00 43.15 ? 403 HOH A O 1 HETATM 1956 O O . HOH F 4 . ? 37.826 29.162 -3.629 1.00 35.86 ? 404 HOH A O 1 HETATM 1957 O O . HOH F 4 . ? 20.788 -13.050 29.477 1.00 49.49 ? 405 HOH A O 1 HETATM 1958 O O . HOH F 4 . ? 29.259 19.966 16.045 1.00 30.43 ? 406 HOH A O 1 HETATM 1959 O O . HOH F 4 . ? 4.571 13.923 32.493 1.00 51.50 ? 407 HOH A O 1 HETATM 1960 O O . HOH F 4 . ? 17.729 27.043 20.686 1.00 42.47 ? 408 HOH A O 1 HETATM 1961 O O . HOH F 4 . ? 19.494 22.498 1.462 1.00 41.20 ? 409 HOH A O 1 HETATM 1962 O O . HOH F 4 . ? 23.232 -7.147 15.166 1.00 19.54 ? 410 HOH A O 1 HETATM 1963 O O . HOH F 4 . ? 8.535 -8.897 13.862 1.00 20.48 ? 411 HOH A O 1 HETATM 1964 O O . HOH F 4 . ? 40.338 24.294 7.472 1.00 31.04 ? 412 HOH A O 1 HETATM 1965 O O . HOH F 4 . ? 22.161 16.023 28.117 1.00 24.39 ? 413 HOH A O 1 HETATM 1966 O O . HOH F 4 . ? 11.471 -2.118 20.555 1.00 18.05 ? 414 HOH A O 1 HETATM 1967 O O . HOH F 4 . ? 22.186 -7.016 25.368 1.00 17.81 ? 415 HOH A O 1 HETATM 1968 O O . HOH F 4 . ? 24.552 -6.188 24.475 1.00 23.81 ? 416 HOH A O 1 HETATM 1969 O O . HOH F 4 . ? 4.128 9.763 26.267 1.00 37.14 ? 417 HOH A O 1 HETATM 1970 O O . HOH F 4 . ? 4.497 22.161 12.258 1.00 25.32 ? 418 HOH A O 1 HETATM 1971 O O . HOH F 4 . ? 9.133 22.396 6.253 1.00 28.27 ? 419 HOH A O 1 HETATM 1972 O O . HOH F 4 . ? 13.682 -9.569 15.422 1.00 17.58 ? 420 HOH A O 1 HETATM 1973 O O . HOH F 4 . ? 27.101 -3.066 28.657 1.00 23.95 ? 421 HOH A O 1 HETATM 1974 O O . HOH F 4 . ? 12.917 19.076 27.636 1.00 18.05 ? 422 HOH A O 1 HETATM 1975 O O . HOH F 4 . ? 19.797 -11.273 18.896 1.00 20.18 ? 423 HOH A O 1 HETATM 1976 O O . HOH F 4 . ? 30.094 -0.445 15.966 1.00 27.72 ? 424 HOH A O 1 HETATM 1977 O O . HOH F 4 . ? 25.316 23.417 18.757 1.00 28.00 ? 425 HOH A O 1 HETATM 1978 O O . HOH F 4 . ? 3.077 9.770 15.638 1.00 17.25 ? 426 HOH A O 1 HETATM 1979 O O . HOH F 4 . ? 13.253 7.327 -1.182 1.00 44.95 ? 427 HOH A O 1 HETATM 1980 O O . HOH F 4 . ? 29.128 22.420 15.334 1.00 44.33 ? 428 HOH A O 1 HETATM 1981 O O . HOH F 4 . ? 10.194 11.412 7.834 1.00 18.11 ? 429 HOH A O 1 HETATM 1982 O O . HOH F 4 . ? 5.575 3.681 14.284 1.00 26.50 ? 430 HOH A O 1 HETATM 1983 O O . HOH F 4 . ? 10.909 3.489 31.415 1.00 32.41 ? 431 HOH A O 1 HETATM 1984 O O . HOH F 4 . ? 17.291 19.489 27.026 1.00 20.39 ? 432 HOH A O 1 HETATM 1985 O O . HOH F 4 . ? 14.616 1.649 29.551 1.00 24.65 ? 433 HOH A O 1 HETATM 1986 O O . HOH F 4 . ? 4.985 23.513 16.323 1.00 22.52 ? 434 HOH A O 1 HETATM 1987 O O . HOH F 4 . ? 34.216 11.244 16.561 1.00 19.87 ? 435 HOH A O 1 HETATM 1988 O O . HOH F 4 . ? 9.172 -1.680 18.883 1.00 18.21 ? 436 HOH A O 1 HETATM 1989 O O . HOH F 4 . ? 6.194 1.891 10.720 1.00 27.60 ? 437 HOH A O 1 HETATM 1990 O O . HOH F 4 . ? 5.591 -5.921 13.451 1.00 20.52 ? 438 HOH A O 1 HETATM 1991 O O . HOH F 4 . ? 39.021 24.981 10.636 1.00 26.27 ? 439 HOH A O 1 HETATM 1992 O O . HOH F 4 . ? 5.034 -0.831 20.526 1.00 31.77 ? 440 HOH A O 1 HETATM 1993 O O . HOH F 4 . ? 5.265 10.422 12.651 1.00 19.25 ? 441 HOH A O 1 HETATM 1994 O O . HOH F 4 . ? 18.021 -7.741 7.872 1.00 36.56 ? 442 HOH A O 1 HETATM 1995 O O . HOH F 4 . ? 15.461 17.770 28.257 1.00 18.96 ? 443 HOH A O 1 HETATM 1996 O O . HOH F 4 . ? 11.678 19.607 29.890 1.00 28.91 ? 444 HOH A O 1 HETATM 1997 O O . HOH F 4 . ? 23.401 -8.926 13.191 1.00 25.71 ? 445 HOH A O 1 HETATM 1998 O O . HOH F 4 . ? 19.652 18.056 26.932 1.00 24.08 ? 446 HOH A O 1 HETATM 1999 O O . HOH F 4 . ? 27.403 -2.431 9.577 1.00 25.58 ? 447 HOH A O 1 HETATM 2000 O O . HOH F 4 . ? 7.293 19.860 4.844 1.00 32.08 ? 448 HOH A O 1 HETATM 2001 O O . HOH F 4 . ? 17.925 27.176 16.303 1.00 36.10 ? 449 HOH A O 1 HETATM 2002 O O . HOH F 4 . ? 24.731 15.465 29.215 1.00 41.37 ? 450 HOH A O 1 HETATM 2003 O O . HOH F 4 . ? 11.373 -3.615 25.718 1.00 19.96 ? 451 HOH A O 1 HETATM 2004 O O . HOH F 4 . ? 5.123 18.902 27.446 1.00 22.67 ? 452 HOH A O 1 HETATM 2005 O O . HOH F 4 . ? 39.112 15.300 14.320 1.00 28.19 ? 453 HOH A O 1 HETATM 2006 O O . HOH F 4 . ? 9.815 -5.661 10.132 1.00 21.13 ? 454 HOH A O 1 HETATM 2007 O O . HOH F 4 . ? 8.210 -5.950 24.076 1.00 26.69 ? 455 HOH A O 1 HETATM 2008 O O . HOH F 4 . ? 6.286 8.981 15.442 1.00 31.96 ? 456 HOH A O 1 HETATM 2009 O O . HOH F 4 . ? 11.534 -6.611 8.182 1.00 30.64 ? 457 HOH A O 1 HETATM 2010 O O . HOH F 4 . ? 21.632 23.722 19.409 1.00 26.33 ? 458 HOH A O 1 HETATM 2011 O O . HOH F 4 . ? 31.369 13.255 -2.920 1.00 38.88 ? 459 HOH A O 1 HETATM 2012 O O . HOH F 4 . ? 18.157 -5.252 6.133 1.00 30.71 ? 460 HOH A O 1 HETATM 2013 O O . HOH F 4 . ? 25.605 -8.494 11.322 1.00 30.79 ? 461 HOH A O 1 HETATM 2014 O O . HOH F 4 . ? 10.000 13.508 29.642 1.00 17.01 ? 462 HOH A O 1 HETATM 2015 O O . HOH F 4 . ? 0.009 10.895 28.794 1.00 22.27 ? 463 HOH A O 1 HETATM 2016 O O . HOH F 4 . ? 35.699 3.506 12.183 1.00 35.11 ? 464 HOH A O 1 HETATM 2017 O O . HOH F 4 . ? 41.508 22.338 14.033 1.00 31.12 ? 465 HOH A O 1 HETATM 2018 O O . HOH F 4 . ? 25.119 29.981 -0.459 1.00 32.22 ? 466 HOH A O 1 HETATM 2019 O O . HOH F 4 . ? 40.237 14.542 6.389 1.00 31.36 ? 467 HOH A O 1 HETATM 2020 O O . HOH F 4 . ? 18.643 26.153 22.934 1.00 35.66 ? 468 HOH A O 1 HETATM 2021 O O . HOH F 4 . ? 32.525 26.638 7.376 1.00 25.85 ? 469 HOH A O 1 HETATM 2022 O O . HOH F 4 . ? 26.090 11.600 0.353 1.00 22.67 ? 470 HOH A O 1 HETATM 2023 O O . HOH F 4 . ? 27.585 16.865 25.942 1.00 24.46 ? 471 HOH A O 1 HETATM 2024 O O . HOH F 4 . ? 28.598 12.261 26.912 1.00 30.20 ? 472 HOH A O 1 HETATM 2025 O O . HOH F 4 . ? 16.888 3.048 29.476 1.00 36.57 ? 473 HOH A O 1 HETATM 2026 O O . HOH F 4 . ? 41.775 17.761 -2.801 1.00 25.92 ? 474 HOH A O 1 HETATM 2027 O O . HOH F 4 . ? 6.081 22.862 10.196 1.00 48.44 ? 475 HOH A O 1 HETATM 2028 O O . HOH F 4 . ? 21.035 -9.402 26.669 1.00 24.45 ? 476 HOH A O 1 HETATM 2029 O O . HOH F 4 . ? 12.666 22.196 0.663 1.00 30.29 ? 477 HOH A O 1 HETATM 2030 O O . HOH F 4 . ? 7.793 -4.648 8.362 1.00 23.09 ? 478 HOH A O 1 HETATM 2031 O O . HOH F 4 . ? 8.251 21.756 3.274 1.00 41.45 ? 479 HOH A O 1 HETATM 2032 O O . HOH F 4 . ? 18.225 -5.904 32.437 1.00 29.24 ? 480 HOH A O 1 HETATM 2033 O O . HOH F 4 . ? 34.253 9.731 11.160 1.00 22.39 ? 481 HOH A O 1 HETATM 2034 O O . HOH F 4 . ? 9.508 20.604 0.863 1.00 30.69 ? 482 HOH A O 1 HETATM 2035 O O . HOH F 4 . ? 27.743 7.883 26.770 1.00 21.61 ? 483 HOH A O 1 HETATM 2036 O O . HOH F 4 . ? 3.935 6.056 28.203 1.00 25.37 ? 484 HOH A O 1 HETATM 2037 O O . HOH F 4 . ? 25.647 0.062 28.314 1.00 27.40 ? 485 HOH A O 1 HETATM 2038 O O . HOH F 4 . ? 5.818 5.729 12.261 1.00 35.23 ? 486 HOH A O 1 HETATM 2039 O O . HOH F 4 . ? 2.884 16.825 7.068 1.00 25.76 ? 487 HOH A O 1 HETATM 2040 O O . HOH F 4 . ? 22.156 25.664 4.012 1.00 30.56 ? 488 HOH A O 1 HETATM 2041 O O . HOH F 4 . ? 18.225 13.766 -2.086 1.00 39.31 ? 489 HOH A O 1 HETATM 2042 O O . HOH F 4 . ? 2.909 -2.872 13.226 1.00 32.33 ? 490 HOH A O 1 HETATM 2043 O O . HOH F 4 . ? 33.115 8.491 23.657 1.00 54.55 ? 491 HOH A O 1 HETATM 2044 O O . HOH F 4 . ? 4.935 -5.646 21.808 1.00 33.17 ? 492 HOH A O 1 HETATM 2045 O O . HOH F 4 . ? 27.900 22.855 19.612 1.00 47.02 ? 493 HOH A O 1 HETATM 2046 O O . HOH F 4 . ? 34.068 6.131 -1.057 1.00 53.75 ? 494 HOH A O 1 HETATM 2047 O O . HOH F 4 . ? 13.408 2.647 0.402 1.00 38.03 ? 495 HOH A O 1 HETATM 2048 O O . HOH F 4 . ? 29.216 6.936 3.462 1.00 36.66 ? 496 HOH A O 1 HETATM 2049 O O . HOH F 4 . ? 28.951 26.711 -3.708 1.00 29.54 ? 497 HOH A O 1 HETATM 2050 O O . HOH F 4 . ? 7.961 17.193 33.922 1.00 52.89 ? 498 HOH A O 1 HETATM 2051 O O . HOH F 4 . ? 0.671 -3.607 14.061 1.00 42.48 ? 499 HOH A O 1 HETATM 2052 O O . HOH F 4 . ? 30.620 11.452 24.984 1.00 39.50 ? 500 HOH A O 1 HETATM 2053 O O . HOH F 4 . ? 42.751 25.740 -7.702 1.00 28.23 ? 501 HOH A O 1 HETATM 2054 O O . HOH F 4 . ? 13.737 -3.979 5.161 1.00 27.19 ? 502 HOH A O 1 HETATM 2055 O O . HOH F 4 . ? 32.452 -9.809 28.914 1.00 40.04 ? 503 HOH A O 1 HETATM 2056 O O . HOH F 4 . ? 33.628 27.829 4.983 1.00 33.45 ? 504 HOH A O 1 HETATM 2057 O O . HOH F 4 . ? 12.051 -5.517 28.475 1.00 26.75 ? 505 HOH A O 1 HETATM 2058 O O . HOH F 4 . ? 22.708 -9.901 30.267 1.00 33.76 ? 506 HOH A O 1 HETATM 2059 O O . HOH F 4 . ? 2.874 19.938 22.478 1.00 25.39 ? 507 HOH A O 1 HETATM 2060 O O . HOH F 4 . ? 20.377 15.785 -2.465 1.00 45.43 ? 508 HOH A O 1 HETATM 2061 O O . HOH F 4 . ? 19.201 11.109 32.155 1.00 40.31 ? 509 HOH A O 1 HETATM 2062 O O . HOH F 4 . ? 22.610 12.071 30.283 1.00 29.52 ? 510 HOH A O 1 HETATM 2063 O O . HOH F 4 . ? 13.927 19.011 30.569 1.00 43.47 ? 511 HOH A O 1 HETATM 2064 O O . HOH F 4 . ? 9.637 -1.086 28.189 1.00 34.51 ? 512 HOH A O 1 HETATM 2065 O O . HOH F 4 . ? -0.177 5.946 6.360 1.00 39.20 ? 513 HOH A O 1 HETATM 2066 O O . HOH F 4 . ? 41.002 13.772 12.948 1.00 39.14 ? 514 HOH A O 1 HETATM 2067 O O . HOH F 4 . ? 11.342 9.831 34.129 1.00 36.60 ? 515 HOH A O 1 HETATM 2068 O O . HOH F 4 . ? 17.370 6.146 30.091 1.00 28.54 ? 516 HOH A O 1 HETATM 2069 O O . HOH F 4 . ? 11.071 2.804 0.179 1.00 46.79 ? 517 HOH A O 1 HETATM 2070 O O . HOH F 4 . ? 21.389 2.940 30.225 1.00 52.59 ? 518 HOH A O 1 HETATM 2071 O O . HOH F 4 . ? 6.119 5.709 16.522 1.00 30.22 ? 519 HOH A O 1 HETATM 2072 O O . HOH F 4 . ? 39.316 19.312 20.183 1.00 54.75 ? 520 HOH A O 1 HETATM 2073 O O . HOH F 4 . ? 15.287 10.064 -0.438 1.00 31.85 ? 521 HOH A O 1 HETATM 2074 O O . HOH F 4 . ? 3.376 1.619 17.968 1.00 32.35 ? 522 HOH A O 1 HETATM 2075 O O . HOH F 4 . ? 4.936 0.450 22.906 1.00 38.31 ? 523 HOH A O 1 HETATM 2076 O O . HOH F 4 . ? 12.753 25.339 4.338 1.00 36.77 ? 524 HOH A O 1 HETATM 2077 O O . HOH F 4 . ? 24.998 15.500 -5.306 1.00 32.25 ? 525 HOH A O 1 HETATM 2078 O O . HOH F 4 . ? 3.614 7.606 8.932 1.00 36.12 ? 526 HOH A O 1 HETATM 2079 O O . HOH F 4 . ? 23.026 25.650 -8.827 1.00 48.39 ? 527 HOH A O 1 HETATM 2080 O O . HOH F 4 . ? 26.393 13.378 -2.218 1.00 41.67 ? 528 HOH A O 1 HETATM 2081 O O . HOH F 4 . ? 15.707 26.906 8.788 1.00 45.82 ? 529 HOH A O 1 HETATM 2082 O O . HOH F 4 . ? 8.708 15.256 2.360 1.00 34.22 ? 530 HOH A O 1 HETATM 2083 O O . HOH F 4 . ? 13.887 1.797 32.446 1.00 38.94 ? 531 HOH A O 1 HETATM 2084 O O . HOH F 4 . ? 11.238 -5.506 5.647 1.00 32.86 ? 532 HOH A O 1 HETATM 2085 O O . HOH F 4 . ? 2.894 -0.221 12.439 1.00 33.38 ? 533 HOH A O 1 HETATM 2086 O O . HOH F 4 . ? 21.753 -2.464 4.705 1.00 41.14 ? 534 HOH A O 1 HETATM 2087 O O . HOH F 4 . ? 3.332 5.322 20.167 1.00 38.17 ? 535 HOH A O 1 HETATM 2088 O O . HOH F 4 . ? 16.996 16.106 29.924 1.00 29.77 ? 536 HOH A O 1 HETATM 2089 O O . HOH F 4 . ? 30.364 -7.704 13.725 1.00 45.90 ? 537 HOH A O 1 HETATM 2090 O O . HOH F 4 . ? -0.493 27.575 11.584 1.00 48.13 ? 538 HOH A O 1 HETATM 2091 O O . HOH F 4 . ? 38.880 21.395 -8.678 1.00 43.61 ? 539 HOH A O 1 HETATM 2092 O O . HOH F 4 . ? 41.998 20.577 9.671 1.00 46.38 ? 540 HOH A O 1 HETATM 2093 O O . HOH F 4 . ? 35.332 13.830 -5.549 1.00 34.16 ? 541 HOH A O 1 HETATM 2094 O O . HOH F 4 . ? 12.568 24.447 8.121 1.00 33.08 ? 542 HOH A O 1 HETATM 2095 O O . HOH F 4 . ? 25.120 27.890 -1.850 1.00 41.50 ? 543 HOH A O 1 HETATM 2096 O O . HOH F 4 . ? 8.585 2.413 0.974 1.00 37.52 ? 544 HOH A O 1 HETATM 2097 O O . HOH F 4 . ? 37.057 2.861 24.407 1.00 40.63 ? 545 HOH A O 1 HETATM 2098 O O . HOH F 4 . ? 26.578 21.041 25.842 1.00 37.80 ? 546 HOH A O 1 HETATM 2099 O O . HOH F 4 . ? 29.489 3.052 25.640 1.00 35.28 ? 547 HOH A O 1 HETATM 2100 O O . HOH F 4 . ? 13.344 27.378 13.923 1.00 51.21 ? 548 HOH A O 1 HETATM 2101 O O . HOH F 4 . ? 12.820 12.856 -2.359 1.00 52.49 ? 549 HOH A O 1 HETATM 2102 O O . HOH F 4 . ? 37.957 18.403 -9.894 1.00 58.72 ? 550 HOH A O 1 HETATM 2103 O O . HOH F 4 . ? 29.150 4.956 27.081 1.00 47.77 ? 551 HOH A O 1 HETATM 2104 O O . HOH F 4 . ? 33.263 17.408 21.469 1.00 34.89 ? 552 HOH A O 1 HETATM 2105 O O . HOH F 4 . ? 16.395 -13.946 28.480 1.00 33.43 ? 553 HOH A O 1 HETATM 2106 O O . HOH F 4 . ? 11.553 23.367 28.344 1.00 36.90 ? 554 HOH A O 1 HETATM 2107 O O . HOH F 4 . ? 30.942 5.795 1.878 1.00 53.13 ? 555 HOH A O 1 HETATM 2108 O O . HOH F 4 . ? 10.101 -5.980 26.042 1.00 26.77 ? 556 HOH A O 1 HETATM 2109 O O . HOH F 4 . ? 1.583 19.007 9.509 1.00 32.18 ? 557 HOH A O 1 HETATM 2110 O O . HOH F 4 . ? 24.605 -8.903 8.774 1.00 56.40 ? 558 HOH A O 1 HETATM 2111 O O . HOH F 4 . ? 32.185 28.345 15.545 1.00 51.60 ? 559 HOH A O 1 HETATM 2112 O O . HOH F 4 . ? 23.122 10.285 32.550 1.00 43.80 ? 560 HOH A O 1 HETATM 2113 O O . HOH F 4 . ? 28.791 2.146 12.010 1.00 48.94 ? 561 HOH A O 1 HETATM 2114 O O . HOH F 4 . ? 14.665 -5.046 2.528 1.00 34.02 ? 562 HOH A O 1 HETATM 2115 O O . HOH F 4 . ? 33.820 -0.500 19.290 1.00 32.30 ? 563 HOH A O 1 HETATM 2116 O O . HOH F 4 . ? 24.784 5.295 31.577 1.00 47.97 ? 564 HOH A O 1 HETATM 2117 O O . HOH F 4 . ? 32.570 7.459 -3.855 1.00 51.47 ? 565 HOH A O 1 HETATM 2118 O O . HOH F 4 . ? 17.814 4.331 32.185 1.00 51.44 ? 566 HOH A O 1 HETATM 2119 O O . HOH F 4 . ? 40.156 1.844 16.895 1.00 57.77 ? 567 HOH A O 1 HETATM 2120 O O . HOH F 4 . ? 33.299 4.257 11.689 1.00 38.60 ? 568 HOH A O 1 HETATM 2121 O O . HOH F 4 . ? 33.486 22.357 -7.464 1.00 33.76 ? 569 HOH A O 1 HETATM 2122 O O . HOH F 4 . ? 40.513 27.532 1.461 1.00 33.84 ? 570 HOH A O 1 HETATM 2123 O O . HOH F 4 . ? 23.193 -6.488 7.126 1.00 39.80 ? 571 HOH A O 1 HETATM 2124 O O . HOH F 4 . ? 28.101 5.873 30.068 1.00 38.53 ? 572 HOH A O 1 HETATM 2125 O O . HOH F 4 . ? 13.849 27.587 17.087 1.00 45.56 ? 573 HOH A O 1 HETATM 2126 O O . HOH F 4 . ? 21.600 25.910 16.313 1.00 49.69 ? 574 HOH A O 1 HETATM 2127 O O . HOH F 4 . ? 36.109 -0.592 26.271 1.00 40.59 ? 575 HOH A O 1 HETATM 2128 O O . HOH F 4 . ? 6.625 -3.401 29.465 1.00 55.56 ? 576 HOH A O 1 HETATM 2129 O O . HOH F 4 . ? 26.724 11.505 31.607 1.00 41.06 ? 577 HOH A O 1 HETATM 2130 O O . HOH F 4 . ? 6.024 23.659 26.319 1.00 53.02 ? 578 HOH A O 1 HETATM 2131 O O . HOH F 4 . ? 40.123 5.225 20.741 1.00 54.34 ? 579 HOH A O 1 HETATM 2132 O O . HOH F 4 . ? 3.100 3.794 1.486 1.00 53.32 ? 580 HOH A O 1 HETATM 2133 O O . HOH F 4 . ? 23.884 14.457 -2.867 1.00 35.79 ? 581 HOH A O 1 HETATM 2134 O O . HOH F 4 . ? 24.218 26.958 0.366 1.00 36.43 ? 582 HOH A O 1 HETATM 2135 O O . HOH F 4 . ? 21.356 25.742 23.148 1.00 46.40 ? 583 HOH A O 1 HETATM 2136 O O . HOH F 4 . ? 36.855 9.168 0.769 1.00 42.34 ? 584 HOH A O 1 HETATM 2137 O O . HOH F 4 . ? 36.113 20.914 -9.123 1.00 44.41 ? 585 HOH A O 1 HETATM 2138 O O . HOH F 4 . ? 25.353 26.368 16.657 1.00 56.11 ? 586 HOH A O 1 HETATM 2139 O O . HOH F 4 . ? 9.058 27.880 -0.003 1.00 58.14 ? 587 HOH A O 1 HETATM 2140 O O . HOH F 4 . ? 41.419 21.825 6.775 1.00 48.25 ? 588 HOH A O 1 HETATM 2141 O O . HOH F 4 . ? 19.101 8.418 32.972 1.00 43.22 ? 589 HOH A O 1 HETATM 2142 O O . HOH F 4 . ? 36.014 -1.376 18.351 1.00 45.26 ? 590 HOH A O 1 HETATM 2143 O O . HOH F 4 . ? 42.007 16.817 7.733 1.00 51.25 ? 591 HOH A O 1 HETATM 2144 O O . HOH F 4 . ? 27.890 29.794 11.453 1.00 50.13 ? 592 HOH A O 1 HETATM 2145 O O . HOH F 4 . ? 21.246 -9.118 33.959 1.00 54.25 ? 593 HOH A O 1 HETATM 2146 O O . HOH F 4 . ? 33.405 15.276 24.139 1.00 52.15 ? 594 HOH A O 1 HETATM 2147 O O . HOH F 4 . ? 28.286 25.274 9.114 1.00 23.01 ? 595 HOH A O 1 HETATM 2148 O O . HOH F 4 . ? 1.827 11.612 32.011 1.00 36.15 ? 596 HOH A O 1 HETATM 2149 O O . HOH F 4 . ? 15.222 -6.174 6.273 1.00 34.54 ? 597 HOH A O 1 HETATM 2150 O O . HOH F 4 . ? 34.280 15.058 -10.331 1.00 50.96 ? 598 HOH A O 1 HETATM 2151 O O . HOH F 4 . ? 25.818 27.763 12.259 1.00 47.65 ? 599 HOH A O 1 HETATM 2152 O O . HOH F 4 . ? 5.341 23.856 5.272 1.00 50.63 ? 600 HOH A O 1 HETATM 2153 O O . HOH F 4 . ? 24.251 32.378 6.846 1.00 50.94 ? 601 HOH A O 1 HETATM 2154 O O . HOH F 4 . ? 34.091 23.957 19.983 1.00 52.03 ? 602 HOH A O 1 HETATM 2155 O O . HOH F 4 . ? 30.832 -9.048 15.971 1.00 51.49 ? 603 HOH A O 1 HETATM 2156 O O . HOH F 4 . ? 18.468 -3.612 31.783 1.00 45.13 ? 604 HOH A O 1 HETATM 2157 O O . HOH F 4 . ? 43.955 24.574 -0.333 1.00 24.27 ? 605 HOH A O 1 HETATM 2158 O O . HOH F 4 . ? 18.979 24.009 3.389 1.00 48.54 ? 606 HOH A O 1 HETATM 2159 O O . HOH F 4 . ? 31.118 -3.200 11.687 1.00 49.49 ? 607 HOH A O 1 HETATM 2160 O O . HOH F 4 . ? 10.619 16.107 33.507 1.00 51.81 ? 608 HOH A O 1 HETATM 2161 O O . HOH F 4 . ? 19.341 27.114 8.489 1.00 42.65 ? 609 HOH A O 1 HETATM 2162 O O . HOH F 4 . ? 12.328 12.421 33.684 1.00 38.67 ? 610 HOH A O 1 HETATM 2163 O O . HOH F 4 . ? 10.150 13.363 32.317 1.00 29.30 ? 611 HOH A O 1 HETATM 2164 O O . HOH F 4 . ? 22.600 -8.143 17.656 1.00 26.36 ? 612 HOH A O 1 HETATM 2165 O O . HOH F 4 . ? 3.005 8.970 23.681 1.00 53.56 ? 613 HOH A O 1 HETATM 2166 O O . HOH F 4 . ? 41.927 23.310 -8.449 1.00 33.09 ? 614 HOH A O 1 HETATM 2167 O O . HOH F 4 . ? 43.638 29.445 -1.098 1.00 45.79 ? 615 HOH A O 1 HETATM 2168 O O . HOH F 4 . ? 11.185 27.907 23.524 1.00 38.52 ? 616 HOH A O 1 HETATM 2169 O O . HOH F 4 . ? 8.050 26.491 17.485 1.00 45.35 ? 617 HOH A O 1 HETATM 2170 O O . HOH F 4 . ? 31.687 4.725 9.503 1.00 45.76 ? 618 HOH A O 1 HETATM 2171 O O . HOH F 4 . ? 0.272 23.491 8.553 1.00 38.42 ? 619 HOH A O 1 HETATM 2172 O O . HOH F 4 . ? 13.236 26.865 8.395 1.00 47.94 ? 620 HOH A O 1 HETATM 2173 O O . HOH F 4 . ? 29.956 9.621 29.203 1.00 43.64 ? 621 HOH A O 1 HETATM 2174 O O . HOH F 4 . ? 31.230 -8.773 24.317 1.00 33.85 ? 622 HOH A O 1 HETATM 2175 O O . HOH F 4 . ? 1.764 8.931 26.332 1.00 46.44 ? 623 HOH A O 1 HETATM 2176 O O . HOH F 4 . ? 19.769 17.049 -10.260 1.00 36.09 ? 624 HOH A O 1 HETATM 2177 O O . HOH F 4 . ? 7.552 -2.130 1.850 1.00 39.16 ? 625 HOH A O 1 HETATM 2178 O O . HOH F 4 . ? 27.342 14.870 -6.244 1.00 45.38 ? 626 HOH A O 1 HETATM 2179 O O . HOH F 4 . ? 33.254 25.701 15.279 1.00 37.87 ? 627 HOH A O 1 HETATM 2180 O O . HOH F 4 . ? 18.713 26.294 18.736 1.00 42.58 ? 628 HOH A O 1 HETATM 2181 O O . HOH F 4 . ? 31.090 23.957 16.268 1.00 48.72 ? 629 HOH A O 1 HETATM 2182 O O . HOH F 4 . ? 33.608 -9.086 22.493 1.00 46.11 ? 630 HOH A O 1 HETATM 2183 O O . HOH F 4 . ? 17.886 29.086 26.316 1.00 55.90 ? 631 HOH A O 1 HETATM 2184 O O . HOH F 4 . ? 12.397 28.177 26.982 1.00 40.46 ? 632 HOH A O 1 HETATM 2185 O O . HOH F 4 . ? 13.175 25.211 27.941 1.00 41.63 ? 633 HOH A O 1 HETATM 2186 O O . HOH F 4 . ? 8.722 28.014 24.319 1.00 41.08 ? 634 HOH A O 1 HETATM 2187 O O . HOH F 4 . ? 7.125 10.302 -1.461 1.00 43.83 ? 635 HOH A O 1 HETATM 2188 O O . HOH F 4 . ? 32.527 23.035 18.219 1.00 47.37 ? 636 HOH A O 1 HETATM 2189 O O . HOH F 4 . ? 4.581 2.654 9.077 1.00 39.89 ? 637 HOH A O 1 HETATM 2190 O O . HOH F 4 . ? 23.161 22.624 26.642 1.00 49.36 ? 638 HOH A O 1 HETATM 2191 O O . HOH F 4 . ? 41.483 7.440 14.903 1.00 51.55 ? 639 HOH A O 1 HETATM 2192 O O . HOH F 4 . ? 4.897 5.214 9.567 1.00 48.14 ? 640 HOH A O 1 HETATM 2193 O O . HOH F 4 . ? 8.904 24.081 9.096 1.00 43.96 ? 641 HOH A O 1 HETATM 2194 O O . HOH F 4 . ? 2.134 6.825 32.149 1.00 52.94 ? 642 HOH A O 1 HETATM 2195 O O . HOH F 4 . ? 41.700 11.224 7.812 1.00 52.07 ? 643 HOH A O 1 HETATM 2196 O O . HOH F 4 . ? 30.722 19.169 17.919 1.00 43.78 ? 644 HOH A O 1 HETATM 2197 O O . HOH F 4 . ? 11.184 23.870 2.001 1.00 43.55 ? 645 HOH A O 1 HETATM 2198 O O . HOH F 4 . ? 28.573 31.847 3.606 1.00 51.64 ? 646 HOH A O 1 HETATM 2199 O O . HOH F 4 . ? 43.347 10.397 10.881 1.00 49.43 ? 647 HOH A O 1 HETATM 2200 O O . HOH F 4 . ? 27.656 26.949 -6.450 1.00 49.49 ? 648 HOH A O 1 HETATM 2201 O O . HOH F 4 . ? 2.357 27.037 9.483 1.00 52.31 ? 649 HOH A O 1 HETATM 2202 O O . HOH F 4 . ? 37.771 -3.937 23.507 1.00 47.04 ? 650 HOH A O 1 HETATM 2203 O O . HOH F 4 . ? 16.308 6.197 1.200 1.00 49.52 ? 651 HOH A O 1 HETATM 2204 O O . HOH F 4 . ? 5.861 25.998 12.868 1.00 47.97 ? 652 HOH A O 1 HETATM 2205 O O . HOH F 4 . ? 4.416 -0.052 0.899 1.00 55.97 ? 653 HOH A O 1 HETATM 2206 O O . HOH F 4 . ? 29.874 10.076 -0.334 1.00 60.44 ? 654 HOH A O 1 HETATM 2207 O O . HOH F 4 . ? 38.022 5.548 2.565 1.00 55.61 ? 655 HOH A O 1 HETATM 2208 O O . HOH F 4 . ? 7.818 24.190 28.117 1.00 44.01 ? 656 HOH A O 1 HETATM 2209 O O . HOH F 4 . ? 31.795 10.196 -2.271 1.00 51.12 ? 657 HOH A O 1 HETATM 2210 O O . HOH F 4 . ? 10.204 23.186 -0.641 1.00 63.64 ? 658 HOH A O 1 HETATM 2211 O O . HOH F 4 . ? 27.139 10.089 -0.950 1.00 50.33 ? 659 HOH A O 1 HETATM 2212 O O . HOH F 4 . ? 28.088 19.294 27.148 1.00 45.36 ? 660 HOH A O 1 HETATM 2213 O O . HOH F 4 . ? 26.150 17.433 28.315 1.00 57.11 ? 661 HOH A O 1 HETATM 2214 O O . HOH F 4 . ? 25.960 32.043 -7.038 1.00 63.37 ? 662 HOH A O 1 HETATM 2215 O O . HOH F 4 . ? 29.854 33.215 -10.161 1.00 59.31 ? 663 HOH A O 1 HETATM 2216 O O . HOH F 4 . ? 27.478 34.296 -4.288 1.00 47.17 ? 664 HOH A O 1 HETATM 2217 O O . HOH F 4 . ? 41.416 12.476 10.604 1.00 34.45 ? 665 HOH A O 1 HETATM 2218 O O . HOH F 4 . ? 24.799 10.622 3.701 1.00 28.03 ? 666 HOH A O 1 HETATM 2219 O O . HOH F 4 . ? 18.380 16.484 34.544 1.00 46.36 ? 667 HOH A O 1 HETATM 2220 O O . HOH F 4 . ? 16.036 16.989 33.732 1.00 49.27 ? 668 HOH A O 1 HETATM 2221 O O . HOH F 4 . ? 22.743 -0.941 30.123 1.00 40.52 ? 669 HOH A O 1 HETATM 2222 O O . HOH F 4 . ? 23.350 1.262 29.718 1.00 43.44 ? 670 HOH A O 1 HETATM 2223 O O . HOH F 4 . ? 3.648 19.332 4.617 1.00 50.31 ? 671 HOH A O 1 HETATM 2224 O O . HOH F 4 . ? 7.001 13.079 33.343 1.00 47.63 ? 672 HOH A O 1 HETATM 2225 O O . HOH F 4 . ? 24.520 9.457 6.646 1.00 39.33 ? 673 HOH A O 1 HETATM 2226 O O . HOH F 4 . ? 22.049 10.626 6.426 1.00 26.61 ? 674 HOH A O 1 HETATM 2227 O O . HOH F 4 . ? 19.934 4.125 2.623 1.00 38.23 ? 675 HOH A O 1 HETATM 2228 O O . HOH F 4 . ? 23.490 -0.189 6.539 1.00 63.72 ? 676 HOH A O 1 HETATM 2229 O O . HOH F 4 . ? 22.694 2.502 11.583 1.00 47.69 ? 677 HOH A O 1 HETATM 2230 O O . HOH F 4 . ? 27.242 1.473 9.390 1.00 50.15 ? 678 HOH A O 1 HETATM 2231 O O . HOH F 4 . ? 20.305 8.478 2.383 1.00 43.29 ? 679 HOH A O 1 HETATM 2232 O O . HOH F 4 . ? 18.899 6.256 1.198 1.00 50.16 ? 680 HOH A O 1 HETATM 2233 O O . HOH F 4 . ? 23.144 1.654 9.495 1.00 43.59 ? 681 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 PHE 4 4 4 PHE PHE A . n A 1 5 ARG 5 5 5 ARG ARG A . n A 1 6 LEU 6 6 6 LEU LEU A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 GLY 8 8 8 GLY GLY A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASP 10 10 10 ASP ASP A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 SER 13 13 13 SER SER A . n A 1 14 TYR 14 14 14 TYR TYR A . n A 1 15 GLY 15 15 15 GLY GLY A . n A 1 16 MET 16 16 16 MET MET A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ILE 18 18 18 ILE ILE A . n A 1 19 LYS 19 19 19 LYS LYS A . n A 1 20 ASP 20 20 20 ASP ASP A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 PRO 26 26 26 PRO PRO A . n A 1 27 HIS 27 27 27 HIS HIS A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 GLU 29 29 29 GLU GLU A . n A 1 30 LYS 30 30 30 LYS LYS A . n A 1 31 VAL 31 31 31 VAL VAL A . n A 1 32 TYR 32 32 32 TYR TYR A . n A 1 33 ASN 33 33 33 ASN ASN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 PRO 35 35 35 PRO PRO A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 LEU 37 37 37 LEU LEU 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 SER 40 40 40 SER SER A . n A 1 41 VAL 41 41 41 VAL VAL A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 GLY 43 43 43 GLY GLY A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 TYR 47 47 47 TYR TYR A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 LEU 49 49 49 LEU LEU A . n A 1 50 MET 50 50 50 MET MET A . n A 1 51 HIS 51 51 51 HIS HIS A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 PHE 53 53 53 PHE PHE A . n A 1 54 ASN 54 54 54 ASN ASN A . n A 1 55 TYR 55 55 55 TYR TYR A . n A 1 56 ASP 56 56 56 ASP ASP A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 ASN 58 58 58 ASN ASN A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 VAL 62 62 62 VAL VAL A . n A 1 63 ALA 63 63 63 ALA ALA A . n A 1 64 VAL 64 64 64 VAL VAL A . n A 1 65 ASP 65 65 65 ASP ASP A . n A 1 66 VAL 66 66 66 VAL VAL A . n A 1 67 THR 67 67 67 THR THR A . n A 1 68 ASN 68 68 68 ASN ASN A . n A 1 69 VAL 69 69 69 VAL VAL A . n A 1 70 TYR 70 70 70 TYR TYR A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 MET 72 72 72 MET MET A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 TYR 74 74 74 TYR TYR A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 THR 78 78 78 THR THR A . n A 1 79 THR 79 79 79 THR THR A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 TYR 81 81 81 TYR TYR A . n A 1 82 PHE 82 82 82 PHE PHE A . n A 1 83 PHE 83 83 83 PHE PHE A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 GLU 85 85 85 GLU GLU A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 ALA 87 87 87 ALA ALA A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 ASP 89 89 89 ASP ASP A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 ALA 91 91 91 ALA ALA A . n A 1 92 SER 92 92 92 SER SER A . n A 1 93 GLN 93 93 93 GLN GLN A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 VAL 95 95 95 VAL VAL A . n A 1 96 PHE 96 96 96 PHE PHE A . n A 1 97 ARG 97 97 97 ARG ARG A . n A 1 98 SER 98 98 98 SER SER A . n A 1 99 ALA 99 99 99 ALA ALA A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 ARG 101 101 101 ARG ARG A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 ILE 103 103 103 ILE ILE A . n A 1 104 THR 104 104 104 THR THR A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 TYR 107 107 107 TYR TYR A . n A 1 108 SER 108 108 108 SER SER A . n A 1 109 GLY 109 109 109 GLY GLY A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 TYR 111 111 111 TYR TYR A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 LYS 120 120 120 LYS LYS A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 LYS 124 124 124 LYS LYS A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 PRO 126 126 126 PRO PRO A . n A 1 127 ILE 127 127 127 ILE ILE A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 ASP 133 133 133 ASP ASP A . n A 1 134 THR 134 134 134 THR THR A . n A 1 135 ALA 135 135 135 ALA ALA A . n A 1 136 ILE 136 136 136 ILE ILE A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 HIS 141 141 141 HIS HIS A . n A 1 142 TYR 142 142 142 TYR TYR A . n A 1 143 ASP 143 143 143 ASP ASP A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 THR 145 145 145 THR THR A . n A 1 146 ALA 146 146 146 ALA ALA A . n A 1 147 ALA 147 147 147 ALA ALA A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 VAL 153 153 153 VAL VAL A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 ALA 159 159 159 ALA ALA A . n A 1 160 GLU 160 160 160 GLU GLU A . n A 1 161 ALA 161 161 161 ALA ALA A . n A 1 162 ALA 162 162 162 ALA ALA A . n A 1 163 ARG 163 163 163 ARG ARG A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 LYS 165 165 165 LYS LYS A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 ILE 167 167 167 ILE ILE A . n A 1 168 GLU 168 168 168 GLU GLU A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLN 170 170 170 GLN GLN A . n A 1 171 ILE 171 171 171 ILE ILE A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 GLU 173 173 173 GLU GLU A . n A 1 174 ARG 174 174 174 ARG ARG A . n A 1 175 ALA 175 175 175 ALA ALA A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 ARG 177 177 177 ARG ARG A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 SER 182 182 182 SER SER A . n A 1 183 SER 183 183 183 SER SER A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 THR 185 185 185 THR THR A . n A 1 186 ILE 186 186 186 ILE ILE A . n A 1 187 SER 187 187 187 SER SER A . n A 1 188 LEU 188 188 188 LEU LEU A . n A 1 189 GLU 189 189 189 GLU GLU A . n A 1 190 ASN 190 190 190 ASN ASN A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 TRP 192 192 192 TRP TRP A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 LEU 195 195 195 LEU LEU A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 LYS 197 197 197 LYS LYS A . n A 1 198 GLN 198 198 198 GLN GLN A . n A 1 199 ILE 199 199 199 ILE ILE A . n A 1 200 GLN 200 200 200 GLN GLN A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 ALA 202 202 202 ALA ALA A . n A 1 203 GLN 203 203 203 GLN GLN A . n A 1 204 GLY 204 204 204 GLY GLY A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 PHE 209 209 209 PHE PHE A . n A 1 210 ARG 210 210 210 ARG ARG A . n A 1 211 THR 211 211 211 THR THR A . n A 1 212 PRO 212 212 212 PRO PRO A . n A 1 213 THR 213 213 213 THR THR A . n A 1 214 VAL 214 214 214 VAL VAL A . n A 1 215 LEU 215 215 215 LEU LEU A . n A 1 216 VAL 216 216 216 VAL VAL A . n A 1 217 ASP 217 217 217 ASP ASP A . n A 1 218 SER 218 218 218 SER SER A . n A 1 219 LYS 219 219 219 LYS LYS A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 ASN 221 221 221 ASN ASN A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 VAL 223 223 223 VAL VAL A . n A 1 224 GLN 224 224 224 GLN GLN A . n A 1 225 ILE 225 225 225 ILE ILE A . n A 1 226 THR 226 226 226 THR THR A . n A 1 227 ASN 227 227 227 ASN ASN A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 THR 229 229 229 THR THR A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 VAL 232 232 232 VAL VAL A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ILE 237 237 237 ILE ILE A . n A 1 238 GLN 238 238 238 GLN GLN A . n A 1 239 LEU 239 239 239 LEU LEU A . n A 1 240 LEU 240 240 240 LEU LEU A . n A 1 241 LEU 241 241 241 LEU LEU A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 ASN 245 245 245 ASN ASN A . n A 1 246 ILE 246 246 246 ILE ILE A . n # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 227 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 227 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _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 monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F # _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 # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2012-03-07 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal HKL-2000 'data collection' . ? 1 AMoRE phasing . ? 2 REFMAC refinement 5.5.0109 ? 3 DENZO 'data reduction' . ? 4 SCALEPACK 'data scaling' . ? 5 # 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 CZ A ARG 46 ? ? NH1 A ARG 46 ? ? 1.411 1.326 0.085 0.013 N 2 1 CG A GLU 112 ? ? CD A GLU 112 ? ? 1.610 1.515 0.095 0.015 N 3 1 CZ A PHE 164 ? ? CE2 A PHE 164 ? ? 1.490 1.369 0.121 0.019 N 4 1 CD A GLN 170 ? ? OE1 A GLN 170 ? ? 1.402 1.235 0.167 0.022 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CD A ARG 46 ? ? NE A ARG 46 ? ? CZ A ARG 46 ? ? 132.15 123.60 8.55 1.40 N 2 1 NE A ARG 46 ? ? CZ A ARG 46 ? ? NH1 A ARG 46 ? ? 131.44 120.30 11.14 0.50 N 3 1 NE A ARG 46 ? ? CZ A ARG 46 ? ? NH2 A ARG 46 ? ? 109.45 120.30 -10.85 0.50 N 4 1 CB A ASP 56 ? ? CG A ASP 56 ? ? OD2 A ASP 56 ? ? 112.69 118.30 -5.61 0.90 N 5 1 CB A ASP 89 ? ? CG A ASP 89 ? ? OD1 A ASP 89 ? ? 123.97 118.30 5.67 0.90 N 6 1 NE A ARG 101 ? ? CZ A ARG 101 ? ? NH2 A ARG 101 ? ? 116.73 120.30 -3.57 0.50 N 7 1 CB A ASP 143 ? ? CG A ASP 143 ? ? OD1 A ASP 143 ? ? 130.95 118.30 12.65 0.90 N 8 1 CB A ASP 143 ? ? CG A ASP 143 ? ? OD2 A ASP 143 ? ? 109.20 118.30 -9.10 0.90 N 9 1 NE A ARG 222 ? ? CZ A ARG 222 ? ? NH2 A ARG 222 ? ? 123.56 120.30 3.26 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 LEU A 77 ? ? 63.27 -102.44 2 1 PRO A 106 ? ? -92.79 40.75 3 1 THR A 158 ? ? -122.62 -78.14 4 1 ASN A 236 ? ? -91.45 -68.84 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 GLYCEROL GOL 4 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 301 247 NAG NAG A . C 3 GOL 1 302 249 GOL GOL A . D 3 GOL 1 303 250 GOL GOL A . E 2 NAG 1 304 1 NAG NAG A . F 4 HOH 1 401 1 HOH HOH A . F 4 HOH 2 402 3 HOH HOH A . F 4 HOH 3 403 4 HOH HOH A . F 4 HOH 4 404 5 HOH HOH A . F 4 HOH 5 405 6 HOH HOH A . F 4 HOH 6 406 8 HOH HOH A . F 4 HOH 7 407 9 HOH HOH A . F 4 HOH 8 408 10 HOH HOH A . F 4 HOH 9 409 11 HOH HOH A . F 4 HOH 10 410 12 HOH HOH A . F 4 HOH 11 411 13 HOH HOH A . F 4 HOH 12 412 14 HOH HOH A . F 4 HOH 13 413 15 HOH HOH A . F 4 HOH 14 414 16 HOH HOH A . F 4 HOH 15 415 17 HOH HOH A . F 4 HOH 16 416 18 HOH HOH A . F 4 HOH 17 417 19 HOH HOH A . F 4 HOH 18 418 20 HOH HOH A . F 4 HOH 19 419 21 HOH HOH A . F 4 HOH 20 420 22 HOH HOH A . F 4 HOH 21 421 23 HOH HOH A . F 4 HOH 22 422 24 HOH HOH A . F 4 HOH 23 423 25 HOH HOH A . F 4 HOH 24 424 26 HOH HOH A . F 4 HOH 25 425 27 HOH HOH A . F 4 HOH 26 426 28 HOH HOH A . F 4 HOH 27 427 29 HOH HOH A . F 4 HOH 28 428 30 HOH HOH A . F 4 HOH 29 429 31 HOH HOH A . F 4 HOH 30 430 32 HOH HOH A . F 4 HOH 31 431 33 HOH HOH A . F 4 HOH 32 432 34 HOH HOH A . F 4 HOH 33 433 35 HOH HOH A . F 4 HOH 34 434 36 HOH HOH A . F 4 HOH 35 435 37 HOH HOH A . F 4 HOH 36 436 38 HOH HOH A . F 4 HOH 37 437 39 HOH HOH A . F 4 HOH 38 438 40 HOH HOH A . F 4 HOH 39 439 41 HOH HOH A . F 4 HOH 40 440 42 HOH HOH A . F 4 HOH 41 441 43 HOH HOH A . F 4 HOH 42 442 44 HOH HOH A . F 4 HOH 43 443 45 HOH HOH A . F 4 HOH 44 444 46 HOH HOH A . F 4 HOH 45 445 47 HOH HOH A . F 4 HOH 46 446 48 HOH HOH A . F 4 HOH 47 447 49 HOH HOH A . F 4 HOH 48 448 50 HOH HOH A . F 4 HOH 49 449 51 HOH HOH A . F 4 HOH 50 450 52 HOH HOH A . F 4 HOH 51 451 53 HOH HOH A . F 4 HOH 52 452 54 HOH HOH A . F 4 HOH 53 453 55 HOH HOH A . F 4 HOH 54 454 56 HOH HOH A . F 4 HOH 55 455 57 HOH HOH A . F 4 HOH 56 456 58 HOH HOH A . F 4 HOH 57 457 59 HOH HOH A . F 4 HOH 58 458 60 HOH HOH A . F 4 HOH 59 459 61 HOH HOH A . F 4 HOH 60 460 62 HOH HOH A . F 4 HOH 61 461 63 HOH HOH A . F 4 HOH 62 462 64 HOH HOH A . F 4 HOH 63 463 65 HOH HOH A . F 4 HOH 64 464 66 HOH HOH A . F 4 HOH 65 465 67 HOH HOH A . F 4 HOH 66 466 68 HOH HOH A . F 4 HOH 67 467 69 HOH HOH A . F 4 HOH 68 468 70 HOH HOH A . F 4 HOH 69 469 71 HOH HOH A . F 4 HOH 70 470 72 HOH HOH A . F 4 HOH 71 471 73 HOH HOH A . F 4 HOH 72 472 74 HOH HOH A . F 4 HOH 73 473 75 HOH HOH A . F 4 HOH 74 474 76 HOH HOH A . F 4 HOH 75 475 77 HOH HOH A . F 4 HOH 76 476 78 HOH HOH A . F 4 HOH 77 477 79 HOH HOH A . F 4 HOH 78 478 80 HOH HOH A . F 4 HOH 79 479 81 HOH HOH A . F 4 HOH 80 480 82 HOH HOH A . F 4 HOH 81 481 83 HOH HOH A . F 4 HOH 82 482 84 HOH HOH A . F 4 HOH 83 483 85 HOH HOH A . F 4 HOH 84 484 86 HOH HOH A . F 4 HOH 85 485 87 HOH HOH A . F 4 HOH 86 486 88 HOH HOH A . F 4 HOH 87 487 89 HOH HOH A . F 4 HOH 88 488 90 HOH HOH A . F 4 HOH 89 489 91 HOH HOH A . F 4 HOH 90 490 92 HOH HOH A . F 4 HOH 91 491 93 HOH HOH A . F 4 HOH 92 492 94 HOH HOH A . F 4 HOH 93 493 95 HOH HOH A . F 4 HOH 94 494 96 HOH HOH A . F 4 HOH 95 495 97 HOH HOH A . F 4 HOH 96 496 98 HOH HOH A . F 4 HOH 97 497 99 HOH HOH A . F 4 HOH 98 498 100 HOH HOH A . F 4 HOH 99 499 101 HOH HOH A . F 4 HOH 100 500 102 HOH HOH A . F 4 HOH 101 501 103 HOH HOH A . F 4 HOH 102 502 104 HOH HOH A . F 4 HOH 103 503 105 HOH HOH A . F 4 HOH 104 504 106 HOH HOH A . F 4 HOH 105 505 107 HOH HOH A . F 4 HOH 106 506 108 HOH HOH A . F 4 HOH 107 507 109 HOH HOH A . F 4 HOH 108 508 110 HOH HOH A . F 4 HOH 109 509 111 HOH HOH A . F 4 HOH 110 510 112 HOH HOH A . F 4 HOH 111 511 113 HOH HOH A . F 4 HOH 112 512 114 HOH HOH A . F 4 HOH 113 513 115 HOH HOH A . F 4 HOH 114 514 117 HOH HOH A . F 4 HOH 115 515 118 HOH HOH A . F 4 HOH 116 516 119 HOH HOH A . F 4 HOH 117 517 120 HOH HOH A . F 4 HOH 118 518 121 HOH HOH A . F 4 HOH 119 519 122 HOH HOH A . F 4 HOH 120 520 123 HOH HOH A . F 4 HOH 121 521 124 HOH HOH A . F 4 HOH 122 522 125 HOH HOH A . F 4 HOH 123 523 126 HOH HOH A . F 4 HOH 124 524 127 HOH HOH A . F 4 HOH 125 525 128 HOH HOH A . F 4 HOH 126 526 129 HOH HOH A . F 4 HOH 127 527 130 HOH HOH A . F 4 HOH 128 528 131 HOH HOH A . F 4 HOH 129 529 132 HOH HOH A . F 4 HOH 130 530 133 HOH HOH A . F 4 HOH 131 531 134 HOH HOH A . F 4 HOH 132 532 135 HOH HOH A . F 4 HOH 133 533 136 HOH HOH A . F 4 HOH 134 534 137 HOH HOH A . F 4 HOH 135 535 138 HOH HOH A . F 4 HOH 136 536 139 HOH HOH A . F 4 HOH 137 537 140 HOH HOH A . F 4 HOH 138 538 141 HOH HOH A . F 4 HOH 139 539 142 HOH HOH A . F 4 HOH 140 540 143 HOH HOH A . F 4 HOH 141 541 144 HOH HOH A . F 4 HOH 142 542 145 HOH HOH A . F 4 HOH 143 543 146 HOH HOH A . F 4 HOH 144 544 147 HOH HOH A . F 4 HOH 145 545 148 HOH HOH A . F 4 HOH 146 546 149 HOH HOH A . F 4 HOH 147 547 150 HOH HOH A . F 4 HOH 148 548 151 HOH HOH A . F 4 HOH 149 549 152 HOH HOH A . F 4 HOH 150 550 153 HOH HOH A . F 4 HOH 151 551 154 HOH HOH A . F 4 HOH 152 552 155 HOH HOH A . F 4 HOH 153 553 156 HOH HOH A . F 4 HOH 154 554 157 HOH HOH A . F 4 HOH 155 555 159 HOH HOH A . F 4 HOH 156 556 160 HOH HOH A . F 4 HOH 157 557 161 HOH HOH A . F 4 HOH 158 558 162 HOH HOH A . F 4 HOH 159 559 163 HOH HOH A . F 4 HOH 160 560 164 HOH HOH A . F 4 HOH 161 561 165 HOH HOH A . F 4 HOH 162 562 166 HOH HOH A . F 4 HOH 163 563 167 HOH HOH A . F 4 HOH 164 564 168 HOH HOH A . F 4 HOH 165 565 169 HOH HOH A . F 4 HOH 166 566 170 HOH HOH A . F 4 HOH 167 567 171 HOH HOH A . F 4 HOH 168 568 173 HOH HOH A . F 4 HOH 169 569 174 HOH HOH A . F 4 HOH 170 570 176 HOH HOH A . F 4 HOH 171 571 177 HOH HOH A . F 4 HOH 172 572 178 HOH HOH A . F 4 HOH 173 573 179 HOH HOH A . F 4 HOH 174 574 180 HOH HOH A . F 4 HOH 175 575 181 HOH HOH A . F 4 HOH 176 576 182 HOH HOH A . F 4 HOH 177 577 183 HOH HOH A . F 4 HOH 178 578 184 HOH HOH A . F 4 HOH 179 579 185 HOH HOH A . F 4 HOH 180 580 186 HOH HOH A . F 4 HOH 181 581 187 HOH HOH A . F 4 HOH 182 582 188 HOH HOH A . F 4 HOH 183 583 189 HOH HOH A . F 4 HOH 184 584 190 HOH HOH A . F 4 HOH 185 585 191 HOH HOH A . F 4 HOH 186 586 192 HOH HOH A . F 4 HOH 187 587 193 HOH HOH A . F 4 HOH 188 588 194 HOH HOH A . F 4 HOH 189 589 195 HOH HOH A . F 4 HOH 190 590 196 HOH HOH A . F 4 HOH 191 591 197 HOH HOH A . F 4 HOH 192 592 198 HOH HOH A . F 4 HOH 193 593 199 HOH HOH A . F 4 HOH 194 594 200 HOH HOH A . F 4 HOH 195 595 201 HOH HOH A . F 4 HOH 196 596 202 HOH HOH A . F 4 HOH 197 597 203 HOH HOH A . F 4 HOH 198 598 204 HOH HOH A . F 4 HOH 199 599 205 HOH HOH A . F 4 HOH 200 600 206 HOH HOH A . F 4 HOH 201 601 207 HOH HOH A . F 4 HOH 202 602 208 HOH HOH A . F 4 HOH 203 603 209 HOH HOH A . F 4 HOH 204 604 210 HOH HOH A . F 4 HOH 205 605 211 HOH HOH A . F 4 HOH 206 606 212 HOH HOH A . F 4 HOH 207 607 213 HOH HOH A . F 4 HOH 208 608 214 HOH HOH A . F 4 HOH 209 609 215 HOH HOH A . F 4 HOH 210 610 216 HOH HOH A . F 4 HOH 211 611 217 HOH HOH A . F 4 HOH 212 612 218 HOH HOH A . F 4 HOH 213 613 219 HOH HOH A . F 4 HOH 214 614 220 HOH HOH A . F 4 HOH 215 615 221 HOH HOH A . F 4 HOH 216 616 222 HOH HOH A . F 4 HOH 217 617 223 HOH HOH A . F 4 HOH 218 618 224 HOH HOH A . F 4 HOH 219 619 225 HOH HOH A . F 4 HOH 220 620 226 HOH HOH A . F 4 HOH 221 621 227 HOH HOH A . F 4 HOH 222 622 228 HOH HOH A . F 4 HOH 223 623 229 HOH HOH A . F 4 HOH 224 624 230 HOH HOH A . F 4 HOH 225 625 231 HOH HOH A . F 4 HOH 226 626 232 HOH HOH A . F 4 HOH 227 627 233 HOH HOH A . F 4 HOH 228 628 234 HOH HOH A . F 4 HOH 229 629 235 HOH HOH A . F 4 HOH 230 630 236 HOH HOH A . F 4 HOH 231 631 237 HOH HOH A . F 4 HOH 232 632 238 HOH HOH A . F 4 HOH 233 633 239 HOH HOH A . F 4 HOH 234 634 240 HOH HOH A . F 4 HOH 235 635 241 HOH HOH A . F 4 HOH 236 636 242 HOH HOH A . F 4 HOH 237 637 243 HOH HOH A . F 4 HOH 238 638 244 HOH HOH A . F 4 HOH 239 639 245 HOH HOH A . F 4 HOH 240 640 246 HOH HOH A . F 4 HOH 241 641 247 HOH HOH A . F 4 HOH 242 642 248 HOH HOH A . F 4 HOH 243 643 249 HOH HOH A . F 4 HOH 244 644 250 HOH HOH A . F 4 HOH 245 645 251 HOH HOH A . F 4 HOH 246 646 252 HOH HOH A . F 4 HOH 247 647 253 HOH HOH A . F 4 HOH 248 648 254 HOH HOH A . F 4 HOH 249 649 255 HOH HOH A . F 4 HOH 250 650 256 HOH HOH A . F 4 HOH 251 651 257 HOH HOH A . F 4 HOH 252 652 259 HOH HOH A . F 4 HOH 253 653 260 HOH HOH A . F 4 HOH 254 654 261 HOH HOH A . F 4 HOH 255 655 262 HOH HOH A . F 4 HOH 256 656 263 HOH HOH A . F 4 HOH 257 657 265 HOH HOH A . F 4 HOH 258 658 266 HOH HOH A . F 4 HOH 259 659 267 HOH HOH A . F 4 HOH 260 660 268 HOH HOH A . F 4 HOH 261 661 269 HOH HOH A . F 4 HOH 262 662 270 HOH HOH A . F 4 HOH 263 663 271 HOH HOH A . F 4 HOH 264 664 272 HOH HOH A . F 4 HOH 265 665 273 HOH HOH A . F 4 HOH 266 666 274 HOH HOH A . F 4 HOH 267 667 275 HOH HOH A . F 4 HOH 268 668 276 HOH HOH A . F 4 HOH 269 669 277 HOH HOH A . F 4 HOH 270 670 278 HOH HOH A . F 4 HOH 271 671 279 HOH HOH A . F 4 HOH 272 672 280 HOH HOH A . F 4 HOH 273 673 281 HOH HOH A . F 4 HOH 274 674 282 HOH HOH A . F 4 HOH 275 675 283 HOH HOH A . F 4 HOH 276 676 284 HOH HOH A . F 4 HOH 277 677 285 HOH HOH A . F 4 HOH 278 678 286 HOH HOH A . F 4 HOH 279 679 287 HOH HOH A . F 4 HOH 280 680 288 HOH HOH A . F 4 HOH 281 681 289 HOH HOH A . #