data_4M5A # _entry.id 4M5A # _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 4M5A RCSB RCSB081483 WWPDB D_1000081483 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3S9Q _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4M5A _pdbx_database_status.recvd_initial_deposition_date 2013-08-08 _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 'Kushwaha, G.S.' 3 'Sinha, M.' 4 'Bhushan, A.' 5 'Kaur, P.' 6 'Sharma, S.' 7 'Singh, T.P.' 8 # _citation.id primary _citation.title ;Crystal structure of the complex of Ribosome inactivating protein from Momordica balsamina inhibited by asymmetric dimethyl arginine at 1.70 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 'Kushwaha, G.S.' 3 primary 'Sinha, M.' 4 primary 'Bhushan, A.' 5 primary 'Kaur, P.' 6 primary 'Sharma, S.' 7 primary 'Singh, T.P.' 8 # _cell.entry_id 4M5A _cell.length_a 130.257 _cell.length_b 130.257 _cell.length_c 39.740 _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 4M5A _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 ? A ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer syn NG,NG-DIMETHYL-L-ARGININE 202.254 1 ? ? ? ? 4 water nat water 18.015 233 ? ? ? ? # _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 4M5A _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 DA2 'L-peptide linking' n NG,NG-DIMETHYL-L-ARGININE ADMA 'C8 H18 N4 O2' 202.254 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 4M5A _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.39 _exptl_crystal.density_percent_sol 48.64 _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 6.8 _exptl_crystal_grow.pdbx_details '14% PEG 6000, 0.1M Sodium Phosphate, pH 6.7, 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 2013-07-19 _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 4M5A _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 50.0 _reflns.d_resolution_high 1.70 _reflns.number_obs 26101 _reflns.number_all 26101 _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.069 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 23.0 _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 1.70 _reflns_shell.d_res_low 1.79 _reflns_shell.percent_possible_all 99.9 _reflns_shell.Rmerge_I_obs 0.596 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 5.0 _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 4M5A _refine.ls_number_reflns_obs 26101 _refine.ls_number_reflns_all 26101 _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 37.51 _refine.ls_d_res_high 1.70 _refine.ls_percent_reflns_obs 99.39 _refine.ls_R_factor_obs 0.20808 _refine.ls_R_factor_all 0.20808 _refine.ls_R_factor_R_work 0.20146 _refine.ls_R_factor_R_free 0.24084 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1384 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.957 _refine.correlation_coeff_Fo_to_Fc_free 0.946 _refine.B_iso_mean 28.212 _refine.aniso_B[1][1] -0.55 _refine.aniso_B[2][2] -0.55 _refine.aniso_B[3][3] 1.79 _refine.aniso_B[1][2] -0.55 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] -0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 3S9Q _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 0.134 _refine.pdbx_overall_ESU_R_Free 0.125 _refine.overall_SU_ML 0.094 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.863 _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 28 _refine_hist.number_atoms_solvent 233 _refine_hist.number_atoms_total 2172 _refine_hist.d_res_high 1.70 _refine_hist.d_res_low 37.51 # 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 0.006 0.019 ? 1975 ? 'X-RAY DIFFRACTION' r_bond_other_d 0.001 0.020 ? 1910 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.211 1.982 ? 2689 ? 'X-RAY DIFFRACTION' r_angle_other_deg 0.813 3.000 ? 4366 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.366 5.000 ? 245 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 35.787 23.929 ? 84 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 14.941 15.000 ? 322 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 16.656 15.000 ? 13 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.063 0.200 ? 318 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.006 0.021 ? 2246 ? 'X-RAY DIFFRACTION' r_gen_planes_other 0.004 0.020 ? 455 ? 'X-RAY DIFFRACTION' r_mcbond_it 1.069 2.672 ? 985 ? 'X-RAY DIFFRACTION' r_mcbond_other 1.070 2.668 ? 982 ? 'X-RAY DIFFRACTION' r_mcangle_it 1.897 4.001 ? 1228 ? 'X-RAY DIFFRACTION' r_mcangle_other 1.897 4.003 ? 1228 ? 'X-RAY DIFFRACTION' r_scbond_it 1.154 2.847 ? 990 ? 'X-RAY DIFFRACTION' r_scbond_other 1.153 2.847 ? 991 ? 'X-RAY DIFFRACTION' r_scangle_other 1.982 4.204 ? 1462 ? 'X-RAY DIFFRACTION' r_long_range_B_refined 4.997 22.911 ? 2437 ? 'X-RAY DIFFRACTION' r_long_range_B_other 4.749 22.255 ? 2349 ? '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 1.700 _refine_ls_shell.d_res_low 1.744 _refine_ls_shell.number_reflns_R_work 1904 _refine_ls_shell.R_factor_R_work 0.273 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.R_factor_R_free 0.327 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 114 _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 4M5A _struct.title ;Crystal structure of the complex of Ribosome inactivating protein from Momordica balsamina inhibited by asymmetric dimethyl arginine at 1.70 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 4M5A _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Ribosome inactivating protein, Complex hydrolase, Ligand binding, Hydrolase, Asymmetric dimethyl arginine' # 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 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 ? LEU A 25 ? ASP A 10 LEU A 25 1 ? 16 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 ? ALA A 202 ? SER A 182 ALA A 202 1 ? 21 HELX_P HELX_P11 11 GLN A 203 ? ASN A 205 ? GLN A 203 ASN A 205 5 ? 3 HELX_P HELX_P12 12 SER A 230 ? SER A 235 ? SER A 230 SER A 235 1 ? 6 HELX_P HELX_P13 13 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 1.447 _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 THR A 61 ? N THR A 61 O LEU A 75 ? O LEU A 75 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 LEU A 215 ? N LEU A 215 O VAL A 223 ? O VAL A 223 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE DA2 A 302' AC2 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A 301 BOUND TO ASN A 227' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 10 TYR A 70 ? TYR A 70 . ? 1_555 ? 2 AC1 10 ILE A 71 ? ILE A 71 . ? 1_555 ? 3 AC1 10 MET A 72 ? MET A 72 . ? 1_555 ? 4 AC1 10 GLU A 85 ? GLU A 85 . ? 1_555 ? 5 AC1 10 GLY A 109 ? GLY A 109 . ? 1_555 ? 6 AC1 10 TYR A 111 ? TYR A 111 . ? 1_555 ? 7 AC1 10 ILE A 155 ? ILE A 155 . ? 1_555 ? 8 AC1 10 GLU A 160 ? GLU A 160 . ? 1_555 ? 9 AC1 10 ARG A 163 ? ARG A 163 . ? 1_555 ? 10 AC1 10 HOH D . ? HOH A 414 . ? 1_555 ? 11 AC2 6 THR A 226 ? THR A 226 . ? 1_555 ? 12 AC2 6 ASN A 227 ? ASN A 227 . ? 1_555 ? 13 AC2 6 THR A 229 ? THR A 229 . ? 1_555 ? 14 AC2 6 HOH D . ? HOH A 457 . ? 1_555 ? 15 AC2 6 HOH D . ? HOH A 631 . ? 1_555 ? 16 AC2 6 HOH D . ? HOH A 632 . ? 1_555 ? # _database_PDB_matrix.entry_id 4M5A _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 4M5A _atom_sites.fract_transf_matrix[1][1] 0.007677 _atom_sites.fract_transf_matrix[1][2] 0.004432 _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] 0.008865 _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] 0.025164 _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 ? 27.001 10.791 15.207 1.00 44.00 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 25.557 10.569 14.897 1.00 42.74 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 24.843 11.896 14.727 1.00 39.35 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 25.253 12.917 15.283 1.00 41.19 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 24.858 9.759 16.000 1.00 44.76 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 25.519 8.411 16.258 1.00 46.54 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 25.036 7.669 17.140 1.00 48.49 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 26.522 8.092 15.590 1.00 48.40 ? 1 ASP A OD2 1 ATOM 9 N N . VAL A 1 2 ? 23.772 11.869 13.948 1.00 33.86 ? 2 VAL A N 1 ATOM 10 C CA . VAL A 1 2 ? 22.961 13.047 13.709 1.00 30.29 ? 2 VAL A CA 1 ATOM 11 C C . VAL A 1 2 ? 21.508 12.630 13.921 1.00 27.69 ? 2 VAL A C 1 ATOM 12 O O . VAL A 1 2 ? 21.180 11.451 13.791 1.00 27.00 ? 2 VAL A O 1 ATOM 13 C CB . VAL A 1 2 ? 23.218 13.622 12.296 1.00 29.88 ? 2 VAL A CB 1 ATOM 14 C CG1 . VAL A 1 2 ? 24.689 13.988 12.130 1.00 29.34 ? 2 VAL A CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? 22.804 12.640 11.210 1.00 29.90 ? 2 VAL A CG2 1 ATOM 16 N N . SER A 1 3 ? 20.654 13.582 14.283 1.00 25.82 ? 3 SER A N 1 ATOM 17 C CA . SER A 1 3 ? 19.250 13.294 14.554 1.00 25.10 ? 3 SER A CA 1 ATOM 18 C C . SER A 1 3 ? 18.308 14.310 13.926 1.00 24.26 ? 3 SER A C 1 ATOM 19 O O . SER A 1 3 ? 18.678 15.466 13.699 1.00 24.47 ? 3 SER A O 1 ATOM 20 C CB . SER A 1 3 ? 18.995 13.228 16.066 1.00 25.85 ? 3 SER A CB 1 ATOM 21 O OG . SER A 1 3 ? 19.855 12.289 16.688 1.00 26.79 ? 3 SER A OG 1 ATOM 22 N N . PHE A 1 4 ? 17.092 13.857 13.638 1.00 22.65 ? 4 PHE A N 1 ATOM 23 C CA . PHE A 1 4 ? 16.026 14.725 13.159 1.00 22.13 ? 4 PHE A CA 1 ATOM 24 C C . PHE A 1 4 ? 14.678 14.236 13.677 1.00 22.51 ? 4 PHE A C 1 ATOM 25 O O . PHE A 1 4 ? 14.354 13.054 13.573 1.00 21.57 ? 4 PHE A O 1 ATOM 26 C CB . PHE A 1 4 ? 16.013 14.791 11.629 1.00 21.27 ? 4 PHE A CB 1 ATOM 27 C CG . PHE A 1 4 ? 14.990 15.739 11.072 1.00 20.81 ? 4 PHE A CG 1 ATOM 28 C CD1 . PHE A 1 4 ? 14.932 17.047 11.525 1.00 20.52 ? 4 PHE A CD1 1 ATOM 29 C CD2 . PHE A 1 4 ? 14.091 15.335 10.087 1.00 20.98 ? 4 PHE A CD2 1 ATOM 30 C CE1 . PHE A 1 4 ? 13.999 17.929 11.025 1.00 20.58 ? 4 PHE A CE1 1 ATOM 31 C CE2 . PHE A 1 4 ? 13.154 16.223 9.577 1.00 21.23 ? 4 PHE A CE2 1 ATOM 32 C CZ . PHE A 1 4 ? 13.109 17.523 10.054 1.00 20.94 ? 4 PHE A CZ 1 ATOM 33 N N . ARG A 1 5 ? 13.904 15.165 14.231 1.00 23.93 ? 5 ARG A N 1 ATOM 34 C CA . ARG A 1 5 ? 12.590 14.885 14.790 1.00 25.15 ? 5 ARG A CA 1 ATOM 35 C C . ARG A 1 5 ? 11.511 15.568 13.978 1.00 24.79 ? 5 ARG A C 1 ATOM 36 O O . ARG A 1 5 ? 11.506 16.790 13.853 1.00 24.43 ? 5 ARG A O 1 ATOM 37 C CB . ARG A 1 5 ? 12.546 15.379 16.234 1.00 26.97 ? 5 ARG A CB 1 ATOM 38 C CG . ARG A 1 5 ? 13.384 14.502 17.140 1.00 29.07 ? 5 ARG A CG 1 ATOM 39 C CD . ARG A 1 5 ? 13.774 15.136 18.461 1.00 31.17 ? 5 ARG A CD 1 ATOM 40 N NE . ARG A 1 5 ? 14.357 14.102 19.319 1.00 32.91 ? 5 ARG A NE 1 ATOM 41 C CZ . ARG A 1 5 ? 15.649 13.770 19.376 1.00 34.25 ? 5 ARG A CZ 1 ATOM 42 N NH1 . ARG A 1 5 ? 16.567 14.401 18.645 1.00 35.66 ? 5 ARG A NH1 1 ATOM 43 N NH2 . ARG A 1 5 ? 16.032 12.793 20.191 1.00 34.41 ? 5 ARG A NH2 1 ATOM 44 N N . LEU A 1 6 ? 10.589 14.782 13.438 1.00 24.93 ? 6 LEU A N 1 ATOM 45 C CA . LEU A 1 6 ? 9.498 15.333 12.656 1.00 25.52 ? 6 LEU A CA 1 ATOM 46 C C . LEU A 1 6 ? 8.481 16.052 13.541 1.00 26.10 ? 6 LEU A C 1 ATOM 47 O O . LEU A 1 6 ? 7.821 16.984 13.082 1.00 26.84 ? 6 LEU A O 1 ATOM 48 C CB . LEU A 1 6 ? 8.824 14.250 11.806 1.00 25.78 ? 6 LEU A CB 1 ATOM 49 C CG . LEU A 1 6 ? 9.478 13.966 10.442 1.00 26.03 ? 6 LEU A CG 1 ATOM 50 C CD1 . LEU A 1 6 ? 9.320 15.159 9.510 1.00 25.87 ? 6 LEU A CD1 1 ATOM 51 C CD2 . LEU A 1 6 ? 10.946 13.572 10.558 1.00 26.22 ? 6 LEU A CD2 1 ATOM 52 N N . SER A 1 7 ? 8.363 15.637 14.803 1.00 26.78 ? 7 SER A N 1 ATOM 53 C CA . SER A 1 7 ? 7.444 16.306 15.722 1.00 27.50 ? 7 SER A CA 1 ATOM 54 C C . SER A 1 7 ? 7.973 17.698 16.042 1.00 27.66 ? 7 SER A C 1 ATOM 55 O O . SER A 1 7 ? 9.033 17.846 16.650 1.00 27.19 ? 7 SER A O 1 ATOM 56 C CB . SER A 1 7 ? 7.250 15.509 17.013 1.00 28.38 ? 7 SER A CB 1 ATOM 57 O OG . SER A 1 7 ? 6.148 16.026 17.745 1.00 29.40 ? 7 SER A OG 1 ATOM 58 N N . GLY A 1 8 ? 7.230 18.712 15.607 1.00 27.67 ? 8 GLY A N 1 ATOM 59 C CA . GLY A 1 8 ? 7.609 20.105 15.819 1.00 27.35 ? 8 GLY A CA 1 ATOM 60 C C . GLY A 1 8 ? 8.562 20.645 14.774 1.00 27.34 ? 8 GLY A C 1 ATOM 61 O O . GLY A 1 8 ? 9.062 21.765 14.910 1.00 27.60 ? 8 GLY A O 1 ATOM 62 N N . ALA A 1 9 ? 8.804 19.867 13.721 1.00 26.90 ? 9 ALA A N 1 ATOM 63 C CA . ALA A 1 9 ? 9.775 20.252 12.707 1.00 27.34 ? 9 ALA A CA 1 ATOM 64 C C . ALA A 1 9 ? 9.283 21.425 11.870 1.00 27.35 ? 9 ALA A C 1 ATOM 65 O O . ALA A 1 9 ? 8.085 21.579 11.608 1.00 27.16 ? 9 ALA A O 1 ATOM 66 C CB . ALA A 1 9 ? 10.111 19.075 11.805 1.00 27.74 ? 9 ALA A CB 1 ATOM 67 N N . ASP A 1 10 ? 10.234 22.249 11.453 1.00 26.92 ? 10 ASP A N 1 ATOM 68 C CA . ASP A 1 10 ? 9.945 23.382 10.600 1.00 26.85 ? 10 ASP A CA 1 ATOM 69 C C . ASP A 1 10 ? 11.131 23.573 9.655 1.00 25.95 ? 10 ASP A C 1 ATOM 70 O O . ASP A 1 10 ? 12.118 22.831 9.748 1.00 24.81 ? 10 ASP A O 1 ATOM 71 C CB . ASP A 1 10 ? 9.609 24.623 11.458 1.00 27.79 ? 10 ASP A CB 1 ATOM 72 C CG . ASP A 1 10 ? 10.794 25.150 12.268 1.00 29.50 ? 10 ASP A CG 1 ATOM 73 O OD1 . ASP A 1 10 ? 11.860 24.499 12.326 1.00 29.90 ? 10 ASP A OD1 1 ATOM 74 O OD2 . ASP A 1 10 ? 10.644 26.241 12.866 1.00 31.10 ? 10 ASP A OD2 1 ATOM 75 N N . PRO A 1 11 ? 11.031 24.520 8.709 1.00 26.09 ? 11 PRO A N 1 ATOM 76 C CA . PRO A 1 11 ? 12.163 24.715 7.804 1.00 25.96 ? 11 PRO A CA 1 ATOM 77 C C . PRO A 1 11 ? 13.512 24.923 8.504 1.00 26.12 ? 11 PRO A C 1 ATOM 78 O O . PRO A 1 11 ? 14.541 24.462 8.004 1.00 24.69 ? 11 PRO A O 1 ATOM 79 C CB . PRO A 1 11 ? 11.739 25.945 7.011 1.00 26.18 ? 11 PRO A CB 1 ATOM 80 C CG . PRO A 1 11 ? 10.260 25.748 6.875 1.00 25.88 ? 11 PRO A CG 1 ATOM 81 C CD . PRO A 1 11 ? 9.833 25.234 8.226 1.00 25.93 ? 11 PRO A CD 1 ATOM 82 N N . SER A 1 12 ? 13.502 25.597 9.652 1.00 26.62 ? 12 SER A N 1 ATOM 83 C CA . SER A 1 12 ? 14.731 25.865 10.389 1.00 26.62 ? 12 SER A CA 1 ATOM 84 C C . SER A 1 12 ? 15.340 24.583 10.975 1.00 25.37 ? 12 SER A C 1 ATOM 85 O O . SER A 1 12 ? 16.536 24.339 10.817 1.00 24.58 ? 12 SER A O 1 ATOM 86 C CB . SER A 1 12 ? 14.477 26.901 11.488 1.00 27.66 ? 12 SER A CB 1 ATOM 87 O OG . SER A 1 12 ? 15.655 27.158 12.226 1.00 30.13 ? 12 SER A OG 1 ATOM 88 N N . SER A 1 13 ? 14.531 23.760 11.638 1.00 24.12 ? 13 SER A N 1 ATOM 89 C CA . SER A 1 13 ? 15.053 22.531 12.253 1.00 23.41 ? 13 SER A CA 1 ATOM 90 C C . SER A 1 13 ? 15.515 21.507 11.211 1.00 21.92 ? 13 SER A C 1 ATOM 91 O O . SER A 1 13 ? 16.486 20.785 11.441 1.00 21.71 ? 13 SER A O 1 ATOM 92 C CB . SER A 1 13 ? 14.043 21.896 13.217 1.00 23.46 ? 13 SER A CB 1 ATOM 93 O OG . SER A 1 13 ? 12.991 21.247 12.527 1.00 23.91 ? 13 SER A OG 1 ATOM 94 N N . TYR A 1 14 ? 14.829 21.448 10.073 1.00 20.49 ? 14 TYR A N 1 ATOM 95 C CA . TYR A 1 14 ? 15.279 20.593 8.977 1.00 19.45 ? 14 TYR A CA 1 ATOM 96 C C . TYR A 1 14 ? 16.637 21.067 8.450 1.00 19.61 ? 14 TYR A C 1 ATOM 97 O O . TYR A 1 14 ? 17.546 20.259 8.242 1.00 18.99 ? 14 TYR A O 1 ATOM 98 C CB . TYR A 1 14 ? 14.242 20.543 7.856 1.00 18.83 ? 14 TYR A CB 1 ATOM 99 C CG . TYR A 1 14 ? 14.721 19.776 6.654 1.00 17.74 ? 14 TYR A CG 1 ATOM 100 C CD1 . TYR A 1 14 ? 14.827 18.392 6.684 1.00 17.24 ? 14 TYR A CD1 1 ATOM 101 C CD2 . TYR A 1 14 ? 15.075 20.435 5.488 1.00 17.42 ? 14 TYR A CD2 1 ATOM 102 C CE1 . TYR A 1 14 ? 15.268 17.688 5.579 1.00 16.66 ? 14 TYR A CE1 1 ATOM 103 C CE2 . TYR A 1 14 ? 15.520 19.741 4.383 1.00 16.85 ? 14 TYR A CE2 1 ATOM 104 C CZ . TYR A 1 14 ? 15.615 18.371 4.433 1.00 16.74 ? 14 TYR A CZ 1 ATOM 105 O OH . TYR A 1 14 ? 16.052 17.693 3.327 1.00 15.55 ? 14 TYR A OH 1 ATOM 106 N N . GLY A 1 15 ? 16.788 22.373 8.248 1.00 20.29 ? 15 GLY A N 1 ATOM 107 C CA . GLY A 1 15 ? 18.077 22.927 7.831 1.00 20.93 ? 15 GLY A CA 1 ATOM 108 C C . GLY A 1 15 ? 19.198 22.611 8.808 1.00 21.95 ? 15 GLY A C 1 ATOM 109 O O . GLY A 1 15 ? 20.323 22.308 8.399 1.00 21.58 ? 15 GLY A O 1 ATOM 110 N N . MET A 1 16 ? 18.899 22.667 10.104 1.00 22.85 ? 16 MET A N 1 ATOM 111 C CA . MET A 1 16 ? 19.893 22.309 11.115 1.00 23.75 ? 16 MET A CA 1 ATOM 112 C C . MET A 1 16 ? 20.294 20.834 11.018 1.00 21.92 ? 16 MET A C 1 ATOM 113 O O . MET A 1 16 ? 21.457 20.495 11.217 1.00 20.97 ? 16 MET A O 1 ATOM 114 C CB . MET A 1 16 ? 19.388 22.631 12.523 1.00 26.54 ? 16 MET A CB 1 ATOM 115 C CG . MET A 1 16 ? 19.231 24.116 12.804 1.00 29.04 ? 16 MET A CG 1 ATOM 116 S SD . MET A 1 16 ? 18.939 24.412 14.560 1.00 34.42 ? 16 MET A SD 1 ATOM 117 C CE . MET A 1 16 ? 17.187 24.076 14.717 1.00 33.09 ? 16 MET A CE 1 ATOM 118 N N . PHE A 1 17 ? 19.340 19.961 10.695 1.00 19.98 ? 17 PHE A N 1 ATOM 119 C CA . PHE A 1 17 ? 19.643 18.538 10.511 1.00 19.41 ? 17 PHE A CA 1 ATOM 120 C C . PHE A 1 17 ? 20.539 18.321 9.292 1.00 19.01 ? 17 PHE A C 1 ATOM 121 O O . PHE A 1 17 ? 21.502 17.563 9.349 1.00 18.62 ? 17 PHE A O 1 ATOM 122 C CB . PHE A 1 17 ? 18.345 17.732 10.400 1.00 19.54 ? 17 PHE A CB 1 ATOM 123 C CG . PHE A 1 17 ? 18.485 16.419 9.675 1.00 19.25 ? 17 PHE A CG 1 ATOM 124 C CD1 . PHE A 1 17 ? 19.309 15.412 10.159 1.00 19.18 ? 17 PHE A CD1 1 ATOM 125 C CD2 . PHE A 1 17 ? 17.748 16.179 8.526 1.00 19.40 ? 17 PHE A CD2 1 ATOM 126 C CE1 . PHE A 1 17 ? 19.406 14.199 9.498 1.00 19.52 ? 17 PHE A CE1 1 ATOM 127 C CE2 . PHE A 1 17 ? 17.846 14.974 7.859 1.00 19.68 ? 17 PHE A CE2 1 ATOM 128 C CZ . PHE A 1 17 ? 18.675 13.982 8.343 1.00 19.28 ? 17 PHE A CZ 1 ATOM 129 N N . ILE A 1 18 ? 20.225 18.987 8.190 1.00 18.77 ? 18 ILE A N 1 ATOM 130 C CA . ILE A 1 18 ? 21.025 18.830 6.978 1.00 18.96 ? 18 ILE A CA 1 ATOM 131 C C . ILE A 1 18 ? 22.436 19.393 7.178 1.00 19.72 ? 18 ILE A C 1 ATOM 132 O O . ILE A 1 18 ? 23.406 18.809 6.703 1.00 20.00 ? 18 ILE A O 1 ATOM 133 C CB . ILE A 1 18 ? 20.322 19.430 5.744 1.00 18.43 ? 18 ILE A CB 1 ATOM 134 C CG1 . ILE A 1 18 ? 19.015 18.679 5.437 1.00 18.49 ? 18 ILE A CG1 1 ATOM 135 C CG2 . ILE A 1 18 ? 21.228 19.379 4.526 1.00 18.20 ? 18 ILE A CG2 1 ATOM 136 C CD1 . ILE A 1 18 ? 19.141 17.173 5.277 1.00 18.13 ? 18 ILE A CD1 1 ATOM 137 N N . LYS A 1 19 ? 22.548 20.502 7.903 1.00 21.12 ? 19 LYS A N 1 ATOM 138 C CA . LYS A 1 19 ? 23.857 21.037 8.285 1.00 22.63 ? 19 LYS A CA 1 ATOM 139 C C . LYS A 1 19 ? 24.661 20.011 9.096 1.00 22.03 ? 19 LYS A C 1 ATOM 140 O O . LYS A 1 19 ? 25.831 19.751 8.795 1.00 22.01 ? 19 LYS A O 1 ATOM 141 C CB . LYS A 1 19 ? 23.678 22.325 9.094 1.00 24.72 ? 19 LYS A CB 1 ATOM 142 C CG . LYS A 1 19 ? 24.980 22.965 9.552 1.00 27.40 ? 19 LYS A CG 1 ATOM 143 C CD . LYS A 1 19 ? 24.738 24.112 10.527 1.00 29.49 ? 19 LYS A CD 1 ATOM 144 C CE . LYS A 1 19 ? 24.428 25.424 9.827 1.00 31.94 ? 19 LYS A CE 1 ATOM 145 N NZ . LYS A 1 19 ? 24.760 26.584 10.704 1.00 33.39 ? 19 LYS A NZ 1 ATOM 146 N N . ASP A 1 20 ? 24.017 19.435 10.115 1.00 21.88 ? 20 ASP A N 1 ATOM 147 C CA . ASP A 1 20 ? 24.618 18.390 10.956 1.00 22.12 ? 20 ASP A CA 1 ATOM 148 C C . ASP A 1 20 ? 25.092 17.201 10.116 1.00 20.86 ? 20 ASP A C 1 ATOM 149 O O . ASP A 1 20 ? 26.190 16.691 10.312 1.00 20.98 ? 20 ASP A O 1 ATOM 150 C CB . ASP A 1 20 ? 23.617 17.883 12.009 1.00 22.91 ? 20 ASP A CB 1 ATOM 151 C CG . ASP A 1 20 ? 23.307 18.914 13.097 1.00 23.91 ? 20 ASP A CG 1 ATOM 152 O OD1 . ASP A 1 20 ? 24.004 19.949 13.185 1.00 24.68 ? 20 ASP A OD1 1 ATOM 153 O OD2 . ASP A 1 20 ? 22.358 18.679 13.877 1.00 25.71 ? 20 ASP A OD2 1 ATOM 154 N N . LEU A 1 21 ? 24.252 16.767 9.177 1.00 20.42 ? 21 LEU A N 1 ATOM 155 C CA . LEU A 1 21 ? 24.584 15.631 8.320 1.00 19.64 ? 21 LEU A CA 1 ATOM 156 C C . LEU A 1 21 ? 25.832 15.934 7.483 1.00 19.72 ? 21 LEU A C 1 ATOM 157 O O . LEU A 1 21 ? 26.771 15.134 7.443 1.00 18.88 ? 21 LEU A O 1 ATOM 158 C CB . LEU A 1 21 ? 23.385 15.274 7.433 1.00 19.67 ? 21 LEU A CB 1 ATOM 159 C CG . LEU A 1 21 ? 23.530 14.135 6.419 1.00 19.82 ? 21 LEU A CG 1 ATOM 160 C CD1 . LEU A 1 21 ? 24.025 12.842 7.046 1.00 20.05 ? 21 LEU A CD1 1 ATOM 161 C CD2 . LEU A 1 21 ? 22.197 13.910 5.722 1.00 19.77 ? 21 LEU A CD2 1 ATOM 162 N N . ARG A 1 22 ? 25.849 17.094 6.830 1.00 19.91 ? 22 ARG A N 1 ATOM 163 C CA . ARG A 1 22 ? 27.031 17.525 6.076 1.00 20.36 ? 22 ARG A CA 1 ATOM 164 C C . ARG A 1 22 ? 28.275 17.542 6.967 1.00 21.54 ? 22 ARG A C 1 ATOM 165 O O . ARG A 1 22 ? 29.320 17.009 6.598 1.00 22.14 ? 22 ARG A O 1 ATOM 166 C CB . ARG A 1 22 ? 26.819 18.912 5.473 1.00 19.83 ? 22 ARG A CB 1 ATOM 167 C CG . ARG A 1 22 ? 25.837 18.958 4.314 1.00 19.09 ? 22 ARG A CG 1 ATOM 168 C CD . ARG A 1 22 ? 25.488 20.385 3.929 1.00 18.48 ? 22 ARG A CD 1 ATOM 169 N NE . ARG A 1 22 ? 24.422 20.425 2.923 1.00 18.06 ? 22 ARG A NE 1 ATOM 170 C CZ . ARG A 1 22 ? 23.497 21.381 2.809 1.00 18.21 ? 22 ARG A CZ 1 ATOM 171 N NH1 . ARG A 1 22 ? 23.466 22.422 3.641 1.00 18.45 ? 22 ARG A NH1 1 ATOM 172 N NH2 . ARG A 1 22 ? 22.578 21.289 1.857 1.00 17.61 ? 22 ARG A NH2 1 ATOM 173 N N . ASN A 1 23 ? 28.149 18.125 8.152 1.00 23.39 ? 23 ASN A N 1 ATOM 174 C CA . ASN A 1 23 ? 29.294 18.254 9.059 1.00 25.23 ? 23 ASN A CA 1 ATOM 175 C C . ASN A 1 23 ? 29.821 16.934 9.613 1.00 25.09 ? 23 ASN A C 1 ATOM 176 O O . ASN A 1 23 ? 30.985 16.856 10.023 1.00 25.87 ? 23 ASN A O 1 ATOM 177 C CB . ASN A 1 23 ? 28.967 19.230 10.198 1.00 26.60 ? 23 ASN A CB 1 ATOM 178 C CG . ASN A 1 23 ? 28.903 20.685 9.739 1.00 28.30 ? 23 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 23 ? 28.318 21.520 10.423 1.00 30.28 ? 23 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 23 ? 29.500 20.999 8.590 1.00 29.12 ? 23 ASN A ND2 1 ATOM 181 N N . ALA A 1 24 ? 28.991 15.893 9.597 1.00 24.65 ? 24 ALA A N 1 ATOM 182 C CA . ALA A 1 24 ? 29.410 14.568 10.062 1.00 25.08 ? 24 ALA A CA 1 ATOM 183 C C . ALA A 1 24 ? 30.205 13.782 9.012 1.00 25.76 ? 24 ALA A C 1 ATOM 184 O O . ALA A 1 24 ? 30.783 12.745 9.330 1.00 26.72 ? 24 ALA A O 1 ATOM 185 C CB . ALA A 1 24 ? 28.202 13.760 10.513 1.00 24.98 ? 24 ALA A CB 1 ATOM 186 N N . LEU A 1 25 ? 30.236 14.261 7.770 1.00 25.48 ? 25 LEU A N 1 ATOM 187 C CA . LEU A 1 25 ? 30.975 13.581 6.708 1.00 25.60 ? 25 LEU A CA 1 ATOM 188 C C . LEU A 1 25 ? 32.397 14.125 6.691 1.00 26.50 ? 25 LEU A C 1 ATOM 189 O O . LEU A 1 25 ? 32.590 15.338 6.572 1.00 26.36 ? 25 LEU A O 1 ATOM 190 C CB . LEU A 1 25 ? 30.309 13.810 5.354 1.00 25.43 ? 25 LEU A CB 1 ATOM 191 C CG . LEU A 1 25 ? 28.824 13.434 5.298 1.00 25.50 ? 25 LEU A CG 1 ATOM 192 C CD1 . LEU A 1 25 ? 28.127 14.079 4.109 1.00 25.52 ? 25 LEU A CD1 1 ATOM 193 C CD2 . LEU A 1 25 ? 28.642 11.926 5.264 1.00 25.75 ? 25 LEU A CD2 1 ATOM 194 N N . PRO A 1 26 ? 33.397 13.241 6.820 1.00 26.90 ? 26 PRO A N 1 ATOM 195 C CA . PRO A 1 26 ? 34.752 13.756 6.940 1.00 27.34 ? 26 PRO A CA 1 ATOM 196 C C . PRO A 1 26 ? 35.355 14.158 5.603 1.00 28.05 ? 26 PRO A C 1 ATOM 197 O O . PRO A 1 26 ? 34.957 13.657 4.550 1.00 27.41 ? 26 PRO A O 1 ATOM 198 C CB . PRO A 1 26 ? 35.515 12.579 7.541 1.00 27.25 ? 26 PRO A CB 1 ATOM 199 C CG . PRO A 1 26 ? 34.817 11.383 7.007 1.00 27.37 ? 26 PRO A CG 1 ATOM 200 C CD . PRO A 1 26 ? 33.369 11.767 6.847 1.00 27.21 ? 26 PRO A CD 1 ATOM 201 N N . HIS A 1 27 ? 36.310 15.077 5.667 1.00 29.33 ? 27 HIS A N 1 ATOM 202 C CA . HIS A 1 27 ? 37.072 15.487 4.505 1.00 31.08 ? 27 HIS A CA 1 ATOM 203 C C . HIS A 1 27 ? 38.408 16.030 4.993 1.00 31.60 ? 27 HIS A C 1 ATOM 204 O O . HIS A 1 27 ? 38.510 16.508 6.126 1.00 31.10 ? 27 HIS A O 1 ATOM 205 C CB . HIS A 1 27 ? 36.306 16.538 3.684 1.00 31.37 ? 27 HIS A CB 1 ATOM 206 C CG . HIS A 1 27 ? 36.233 17.893 4.323 1.00 32.84 ? 27 HIS A CG 1 ATOM 207 N ND1 . HIS A 1 27 ? 35.250 18.245 5.225 1.00 33.35 ? 27 HIS A ND1 1 ATOM 208 C CD2 . HIS A 1 27 ? 37.006 18.995 4.164 1.00 33.12 ? 27 HIS A CD2 1 ATOM 209 C CE1 . HIS A 1 27 ? 35.429 19.500 5.603 1.00 34.40 ? 27 HIS A CE1 1 ATOM 210 N NE2 . HIS A 1 27 ? 36.488 19.977 4.972 1.00 33.92 ? 27 HIS A NE2 1 ATOM 211 N N . THR A 1 28 ? 39.431 15.919 4.151 1.00 34.25 ? 28 THR A N 1 ATOM 212 C CA . THR A 1 28 ? 40.734 16.531 4.433 1.00 35.86 ? 28 THR A CA 1 ATOM 213 C C . THR A 1 28 ? 41.041 17.718 3.519 1.00 36.81 ? 28 THR A C 1 ATOM 214 O O . THR A 1 28 ? 41.926 18.520 3.818 1.00 37.48 ? 28 THR A O 1 ATOM 215 C CB . THR A 1 28 ? 41.877 15.510 4.301 1.00 36.74 ? 28 THR A CB 1 ATOM 216 O OG1 . THR A 1 28 ? 41.774 14.827 3.047 1.00 38.47 ? 28 THR A OG1 1 ATOM 217 C CG2 . THR A 1 28 ? 41.830 14.505 5.442 1.00 37.57 ? 28 THR A CG2 1 ATOM 218 N N . GLU A 1 29 ? 40.291 17.827 2.426 1.00 35.82 ? 29 GLU A N 1 ATOM 219 C CA . GLU A 1 29 ? 40.568 18.756 1.346 1.00 36.11 ? 29 GLU A CA 1 ATOM 220 C C . GLU A 1 29 ? 39.245 19.371 0.927 1.00 35.16 ? 29 GLU A C 1 ATOM 221 O O . GLU A 1 29 ? 38.210 18.694 0.956 1.00 34.68 ? 29 GLU A O 1 ATOM 222 C CB . GLU A 1 29 ? 41.123 17.960 0.164 1.00 37.40 ? 29 GLU A CB 1 ATOM 223 C CG . GLU A 1 29 ? 42.183 18.638 -0.684 1.00 39.11 ? 29 GLU A CG 1 ATOM 224 C CD . GLU A 1 29 ? 42.565 17.790 -1.886 1.00 40.11 ? 29 GLU A CD 1 ATOM 225 O OE1 . GLU A 1 29 ? 42.773 16.567 -1.717 1.00 42.04 ? 29 GLU A OE1 1 ATOM 226 O OE2 . GLU A 1 29 ? 42.656 18.343 -3.003 1.00 42.15 ? 29 GLU A OE2 1 ATOM 227 N N . LYS A 1 30 ? 39.270 20.647 0.549 1.00 33.00 ? 30 LYS A N 1 ATOM 228 C CA . LYS A 1 30 ? 38.204 21.216 -0.268 1.00 32.37 ? 30 LYS A CA 1 ATOM 229 C C . LYS A 1 30 ? 38.747 21.510 -1.652 1.00 32.20 ? 30 LYS A C 1 ATOM 230 O O . LYS A 1 30 ? 39.905 21.904 -1.810 1.00 33.46 ? 30 LYS A O 1 ATOM 231 C CB . LYS A 1 30 ? 37.644 22.502 0.326 1.00 32.28 ? 30 LYS A CB 1 ATOM 232 C CG . LYS A 1 30 ? 37.179 22.371 1.761 1.00 32.45 ? 30 LYS A CG 1 ATOM 233 C CD . LYS A 1 30 ? 36.443 23.621 2.193 1.00 33.00 ? 30 LYS A CD 1 ATOM 234 C CE . LYS A 1 30 ? 36.040 23.531 3.652 1.00 34.09 ? 30 LYS A CE 1 ATOM 235 N NZ . LYS A 1 30 ? 35.493 24.822 4.148 1.00 35.04 ? 30 LYS A NZ 1 ATOM 236 N N . VAL A 1 31 ? 37.895 21.306 -2.648 1.00 30.61 ? 31 VAL A N 1 ATOM 237 C CA . VAL A 1 31 ? 38.200 21.608 -4.034 1.00 30.36 ? 31 VAL A CA 1 ATOM 238 C C . VAL A 1 31 ? 37.216 22.695 -4.430 1.00 30.57 ? 31 VAL A C 1 ATOM 239 O O . VAL A 1 31 ? 35.999 22.493 -4.361 1.00 29.69 ? 31 VAL A O 1 ATOM 240 C CB . VAL A 1 31 ? 38.043 20.352 -4.916 1.00 29.73 ? 31 VAL A CB 1 ATOM 241 C CG1 . VAL A 1 31 ? 38.312 20.662 -6.381 1.00 30.12 ? 31 VAL A CG1 1 ATOM 242 C CG2 . VAL A 1 31 ? 38.977 19.252 -4.430 1.00 29.42 ? 31 VAL A CG2 1 ATOM 243 N N . TYR A 1 32 ? 37.746 23.857 -4.805 1.00 30.13 ? 32 TYR A N 1 ATOM 244 C CA . TYR A 1 32 ? 36.931 25.039 -5.063 1.00 30.69 ? 32 TYR A CA 1 ATOM 245 C C . TYR A 1 32 ? 35.922 25.304 -3.933 1.00 30.26 ? 32 TYR A C 1 ATOM 246 O O . TYR A 1 32 ? 34.736 25.531 -4.178 1.00 30.52 ? 32 TYR A O 1 ATOM 247 C CB . TYR A 1 32 ? 36.234 24.899 -6.414 1.00 31.69 ? 32 TYR A CB 1 ATOM 248 C CG . TYR A 1 32 ? 37.188 24.948 -7.584 1.00 32.55 ? 32 TYR A CG 1 ATOM 249 C CD1 . TYR A 1 32 ? 37.809 26.141 -7.945 1.00 34.04 ? 32 TYR A CD1 1 ATOM 250 C CD2 . TYR A 1 32 ? 37.468 23.811 -8.334 1.00 33.64 ? 32 TYR A CD2 1 ATOM 251 C CE1 . TYR A 1 32 ? 38.683 26.199 -9.019 1.00 33.77 ? 32 TYR A CE1 1 ATOM 252 C CE2 . TYR A 1 32 ? 38.343 23.860 -9.410 1.00 34.47 ? 32 TYR A CE2 1 ATOM 253 C CZ . TYR A 1 32 ? 38.947 25.057 -9.745 1.00 34.01 ? 32 TYR A CZ 1 ATOM 254 O OH . TYR A 1 32 ? 39.813 25.112 -10.814 1.00 35.83 ? 32 TYR A OH 1 ATOM 255 N N . ASN A 1 33 ? 36.419 25.255 -2.698 1.00 29.75 ? 33 ASN A N 1 ATOM 256 C CA . ASN A 1 33 ? 35.649 25.565 -1.488 1.00 29.91 ? 33 ASN A CA 1 ATOM 257 C C . ASN A 1 33 ? 34.510 24.585 -1.152 1.00 28.35 ? 33 ASN A C 1 ATOM 258 O O . ASN A 1 33 ? 33.648 24.898 -0.330 1.00 28.28 ? 33 ASN A O 1 ATOM 259 C CB . ASN A 1 33 ? 35.106 27.002 -1.552 1.00 31.69 ? 33 ASN A CB 1 ATOM 260 C CG . ASN A 1 33 ? 34.982 27.642 -0.181 1.00 33.96 ? 33 ASN A CG 1 ATOM 261 O OD1 . ASN A 1 33 ? 35.803 27.403 0.706 1.00 35.97 ? 33 ASN A OD1 1 ATOM 262 N ND2 . ASN A 1 33 ? 33.954 28.462 0.002 1.00 35.60 ? 33 ASN A ND2 1 ATOM 263 N N . ILE A 1 34 ? 34.533 23.403 -1.767 1.00 26.71 ? 34 ILE A N 1 ATOM 264 C CA . ILE A 1 34 ? 33.530 22.356 -1.531 1.00 25.47 ? 34 ILE A CA 1 ATOM 265 C C . ILE A 1 34 ? 34.240 21.155 -0.922 1.00 25.24 ? 34 ILE A C 1 ATOM 266 O O . ILE A 1 34 ? 35.209 20.664 -1.503 1.00 25.24 ? 34 ILE A O 1 ATOM 267 C CB . ILE A 1 34 ? 32.862 21.871 -2.834 1.00 24.79 ? 34 ILE A CB 1 ATOM 268 C CG1 . ILE A 1 34 ? 32.255 23.035 -3.617 1.00 24.52 ? 34 ILE A CG1 1 ATOM 269 C CG2 . ILE A 1 34 ? 31.773 20.844 -2.527 1.00 24.59 ? 34 ILE A CG2 1 ATOM 270 C CD1 . ILE A 1 34 ? 32.252 22.806 -5.106 1.00 24.53 ? 34 ILE A CD1 1 ATOM 271 N N . PRO A 1 35 ? 33.761 20.669 0.238 1.00 24.69 ? 35 PRO A N 1 ATOM 272 C CA . PRO A 1 35 ? 34.366 19.494 0.855 1.00 24.78 ? 35 PRO A CA 1 ATOM 273 C C . PRO A 1 35 ? 34.448 18.295 -0.093 1.00 24.68 ? 35 PRO A C 1 ATOM 274 O O . PRO A 1 35 ? 33.490 17.970 -0.806 1.00 24.17 ? 35 PRO A O 1 ATOM 275 C CB . PRO A 1 35 ? 33.453 19.215 2.049 1.00 24.76 ? 35 PRO A CB 1 ATOM 276 C CG . PRO A 1 35 ? 32.920 20.556 2.414 1.00 24.43 ? 35 PRO A CG 1 ATOM 277 C CD . PRO A 1 35 ? 32.759 21.292 1.121 1.00 24.71 ? 35 PRO A CD 1 ATOM 278 N N . LEU A 1 36 ? 35.627 17.686 -0.112 1.00 24.86 ? 36 LEU A N 1 ATOM 279 C CA . LEU A 1 36 ? 35.917 16.543 -0.949 1.00 24.91 ? 36 LEU A CA 1 ATOM 280 C C . LEU A 1 36 ? 35.802 15.307 -0.087 1.00 25.03 ? 36 LEU A C 1 ATOM 281 O O . LEU A 1 36 ? 36.591 15.114 0.840 1.00 24.89 ? 36 LEU A O 1 ATOM 282 C CB . LEU A 1 36 ? 37.335 16.643 -1.523 1.00 25.00 ? 36 LEU A CB 1 ATOM 283 C CG . LEU A 1 36 ? 37.835 15.409 -2.287 1.00 25.23 ? 36 LEU A CG 1 ATOM 284 C CD1 . LEU A 1 36 ? 37.040 15.153 -3.561 1.00 25.12 ? 36 LEU A CD1 1 ATOM 285 C CD2 . LEU A 1 36 ? 39.320 15.553 -2.596 1.00 25.03 ? 36 LEU A CD2 1 ATOM 286 N N . LEU A 1 37 ? 34.822 14.460 -0.380 1.00 25.33 ? 37 LEU A N 1 ATOM 287 C CA . LEU A 1 37 ? 34.665 13.242 0.400 1.00 25.89 ? 37 LEU A CA 1 ATOM 288 C C . LEU A 1 37 ? 35.875 12.332 0.212 1.00 27.01 ? 37 LEU A C 1 ATOM 289 O O . LEU A 1 37 ? 36.534 12.357 -0.832 1.00 27.18 ? 37 LEU A O 1 ATOM 290 C CB . LEU A 1 37 ? 33.368 12.516 0.038 1.00 25.46 ? 37 LEU A CB 1 ATOM 291 C CG . LEU A 1 37 ? 32.080 13.253 0.425 1.00 25.13 ? 37 LEU A CG 1 ATOM 292 C CD1 . LEU A 1 37 ? 30.901 12.478 -0.139 1.00 24.78 ? 37 LEU A CD1 1 ATOM 293 C CD2 . LEU A 1 37 ? 31.925 13.446 1.931 1.00 25.11 ? 37 LEU A CD2 1 ATOM 294 N N . LEU A 1 38 ? 36.160 11.539 1.237 1.00 29.50 ? 38 LEU A N 1 ATOM 295 C CA . LEU A 1 38 ? 37.376 10.734 1.265 1.00 30.75 ? 38 LEU A CA 1 ATOM 296 C C . LEU A 1 38 ? 37.306 9.559 0.298 1.00 31.29 ? 38 LEU A C 1 ATOM 297 O O . LEU A 1 38 ? 36.219 9.051 0.013 1.00 30.21 ? 38 LEU A O 1 ATOM 298 C CB . LEU A 1 38 ? 37.642 10.218 2.679 1.00 31.13 ? 38 LEU A CB 1 ATOM 299 C CG . LEU A 1 38 ? 37.792 11.287 3.763 1.00 32.04 ? 38 LEU A CG 1 ATOM 300 C CD1 . LEU A 1 38 ? 38.005 10.634 5.118 1.00 31.97 ? 38 LEU A CD1 1 ATOM 301 C CD2 . LEU A 1 38 ? 38.938 12.238 3.445 1.00 32.19 ? 38 LEU A CD2 1 ATOM 302 N N . PRO A 1 39 ? 38.471 9.114 -0.204 1.00 31.86 ? 39 PRO A N 1 ATOM 303 C CA . PRO A 1 39 ? 38.490 7.985 -1.128 1.00 32.40 ? 39 PRO A CA 1 ATOM 304 C C . PRO A 1 39 ? 38.050 6.687 -0.460 1.00 33.14 ? 39 PRO A C 1 ATOM 305 O O . PRO A 1 39 ? 37.398 5.864 -1.099 1.00 32.84 ? 39 PRO A O 1 ATOM 306 C CB . PRO A 1 39 ? 39.961 7.887 -1.565 1.00 32.66 ? 39 PRO A CB 1 ATOM 307 C CG . PRO A 1 39 ? 40.668 9.046 -0.951 1.00 32.55 ? 39 PRO A CG 1 ATOM 308 C CD . PRO A 1 39 ? 39.829 9.536 0.181 1.00 32.39 ? 39 PRO A CD 1 ATOM 309 N N . SER A 1 40 ? 38.409 6.511 0.810 1.00 34.34 ? 40 SER A N 1 ATOM 310 C CA . SER A 1 40 ? 38.021 5.319 1.559 1.00 35.74 ? 40 SER A CA 1 ATOM 311 C C . SER A 1 40 ? 38.153 5.545 3.061 1.00 35.75 ? 40 SER A C 1 ATOM 312 O O . SER A 1 40 ? 38.878 6.433 3.506 1.00 36.15 ? 40 SER A O 1 ATOM 313 C CB . SER A 1 40 ? 38.872 4.118 1.134 1.00 36.57 ? 40 SER A CB 1 ATOM 314 O OG . SER A 1 40 ? 40.207 4.255 1.591 1.00 37.85 ? 40 SER A OG 1 ATOM 315 N N . VAL A 1 41 ? 37.427 4.736 3.826 1.00 35.99 ? 41 VAL A N 1 ATOM 316 C CA . VAL A 1 41 ? 37.509 4.714 5.285 1.00 36.42 ? 41 VAL A CA 1 ATOM 317 C C . VAL A 1 41 ? 37.361 3.247 5.695 1.00 37.93 ? 41 VAL A C 1 ATOM 318 O O . VAL A 1 41 ? 36.516 2.534 5.146 1.00 38.65 ? 41 VAL A O 1 ATOM 319 C CB . VAL A 1 41 ? 36.388 5.539 5.957 1.00 35.58 ? 41 VAL A CB 1 ATOM 320 C CG1 . VAL A 1 41 ? 36.474 5.430 7.475 1.00 35.04 ? 41 VAL A CG1 1 ATOM 321 C CG2 . VAL A 1 41 ? 36.435 7.002 5.529 1.00 35.49 ? 41 VAL A CG2 1 ATOM 322 N N . SER A 1 42 ? 38.170 2.805 6.655 1.00 39.13 ? 42 SER A N 1 ATOM 323 C CA . SER A 1 42 ? 38.164 1.404 7.077 1.00 40.01 ? 42 SER A CA 1 ATOM 324 C C . SER A 1 42 ? 37.419 1.206 8.384 1.00 40.25 ? 42 SER A C 1 ATOM 325 O O . SER A 1 42 ? 37.432 2.066 9.266 1.00 41.20 ? 42 SER A O 1 ATOM 326 C CB . SER A 1 42 ? 39.592 0.870 7.214 1.00 40.83 ? 42 SER A CB 1 ATOM 327 O OG . SER A 1 42 ? 40.116 0.513 5.947 1.00 42.09 ? 42 SER A OG 1 ATOM 328 N N . GLY A 1 43 ? 36.772 0.052 8.493 1.00 40.29 ? 43 GLY A N 1 ATOM 329 C CA . GLY A 1 43 ? 36.079 -0.329 9.704 1.00 40.00 ? 43 GLY A CA 1 ATOM 330 C C . GLY A 1 43 ? 34.740 0.360 9.837 1.00 39.25 ? 43 GLY A C 1 ATOM 331 O O . GLY A 1 43 ? 34.147 0.805 8.849 1.00 39.19 ? 43 GLY A O 1 ATOM 332 N N . ALA A 1 44 ? 34.283 0.450 11.081 1.00 38.24 ? 44 ALA A N 1 ATOM 333 C CA . ALA A 1 44 ? 32.983 1.019 11.420 1.00 37.71 ? 44 ALA A CA 1 ATOM 334 C C . ALA A 1 44 ? 32.911 2.528 11.180 1.00 36.85 ? 44 ALA A C 1 ATOM 335 O O . ALA A 1 44 ? 31.821 3.079 11.008 1.00 36.26 ? 44 ALA A O 1 ATOM 336 C CB . ALA A 1 44 ? 32.654 0.709 12.871 1.00 38.07 ? 44 ALA A CB 1 ATOM 337 N N . GLY A 1 45 ? 34.070 3.188 11.177 1.00 35.18 ? 45 GLY A N 1 ATOM 338 C CA . GLY A 1 45 ? 34.154 4.623 10.906 1.00 33.90 ? 45 GLY A CA 1 ATOM 339 C C . GLY A 1 45 ? 33.661 5.037 9.529 1.00 32.44 ? 45 GLY A C 1 ATOM 340 O O . GLY A 1 45 ? 33.353 6.207 9.310 1.00 33.02 ? 45 GLY A O 1 ATOM 341 N N . ARG A 1 46 ? 33.595 4.082 8.602 1.00 31.10 ? 46 ARG A N 1 ATOM 342 C CA . ARG A 1 46 ? 33.001 4.314 7.286 1.00 30.38 ? 46 ARG A CA 1 ATOM 343 C C . ARG A 1 46 ? 31.518 4.684 7.347 1.00 28.94 ? 46 ARG A C 1 ATOM 344 O O . ARG A 1 46 ? 31.000 5.259 6.397 1.00 27.52 ? 46 ARG A O 1 ATOM 345 C CB . ARG A 1 46 ? 33.177 3.085 6.387 1.00 31.72 ? 46 ARG A CB 1 ATOM 346 C CG . ARG A 1 46 ? 32.767 3.313 4.942 1.00 33.18 ? 46 ARG A CG 1 ATOM 347 C CD . ARG A 1 46 ? 33.061 2.104 4.076 1.00 35.03 ? 46 ARG A CD 1 ATOM 348 N NE . ARG A 1 46 ? 32.794 2.397 2.670 1.00 37.52 ? 46 ARG A NE 1 ATOM 349 C CZ . ARG A 1 46 ? 33.711 2.727 1.761 1.00 39.04 ? 46 ARG A CZ 1 ATOM 350 N NH1 . ARG A 1 46 ? 35.008 2.790 2.069 1.00 39.65 ? 46 ARG A NH1 1 ATOM 351 N NH2 . ARG A 1 46 ? 33.325 2.984 0.516 1.00 40.56 ? 46 ARG A NH2 1 ATOM 352 N N . TYR A 1 47 ? 30.836 4.359 8.446 1.00 28.21 ? 47 TYR A N 1 ATOM 353 C CA . TYR A 1 47 ? 29.386 4.527 8.508 1.00 27.91 ? 47 TYR A CA 1 ATOM 354 C C . TYR A 1 47 ? 28.936 5.530 9.557 1.00 28.51 ? 47 TYR A C 1 ATOM 355 O O . TYR A 1 47 ? 29.342 5.465 10.718 1.00 30.27 ? 47 TYR A O 1 ATOM 356 C CB . TYR A 1 47 ? 28.716 3.173 8.739 1.00 27.49 ? 47 TYR A CB 1 ATOM 357 C CG . TYR A 1 47 ? 29.296 2.137 7.828 1.00 27.22 ? 47 TYR A CG 1 ATOM 358 C CD1 . TYR A 1 47 ? 28.987 2.132 6.471 1.00 26.71 ? 47 TYR A CD1 1 ATOM 359 C CD2 . TYR A 1 47 ? 30.205 1.200 8.303 1.00 27.59 ? 47 TYR A CD2 1 ATOM 360 C CE1 . TYR A 1 47 ? 29.542 1.197 5.617 1.00 27.19 ? 47 TYR A CE1 1 ATOM 361 C CE2 . TYR A 1 47 ? 30.770 0.266 7.457 1.00 27.62 ? 47 TYR A CE2 1 ATOM 362 C CZ . TYR A 1 47 ? 30.436 0.269 6.117 1.00 27.58 ? 47 TYR A CZ 1 ATOM 363 O OH . TYR A 1 47 ? 30.993 -0.663 5.276 1.00 28.80 ? 47 TYR A OH 1 ATOM 364 N N . LEU A 1 48 ? 28.095 6.461 9.119 1.00 27.77 ? 48 LEU A N 1 ATOM 365 C CA . LEU A 1 48 ? 27.424 7.411 9.997 1.00 28.24 ? 48 LEU A CA 1 ATOM 366 C C . LEU A 1 48 ? 26.022 6.898 10.309 1.00 26.90 ? 48 LEU A C 1 ATOM 367 O O . LEU A 1 48 ? 25.367 6.325 9.436 1.00 26.09 ? 48 LEU A O 1 ATOM 368 C CB . LEU A 1 48 ? 27.325 8.771 9.302 1.00 29.95 ? 48 LEU A CB 1 ATOM 369 C CG . LEU A 1 48 ? 26.318 9.787 9.845 1.00 31.59 ? 48 LEU A CG 1 ATOM 370 C CD1 . LEU A 1 48 ? 26.754 10.287 11.210 1.00 32.52 ? 48 LEU A CD1 1 ATOM 371 C CD2 . LEU A 1 48 ? 26.172 10.946 8.879 1.00 32.25 ? 48 LEU A CD2 1 ATOM 372 N N . LEU A 1 49 ? 25.563 7.130 11.538 1.00 26.12 ? 49 LEU A N 1 ATOM 373 C CA . LEU A 1 49 ? 24.200 6.793 11.942 1.00 26.00 ? 49 LEU A CA 1 ATOM 374 C C . LEU A 1 49 ? 23.325 8.035 12.034 1.00 25.10 ? 49 LEU A C 1 ATOM 375 O O . LEU A 1 49 ? 23.665 8.983 12.744 1.00 25.02 ? 49 LEU A O 1 ATOM 376 C CB . LEU A 1 49 ? 24.206 6.101 13.302 1.00 27.09 ? 49 LEU A CB 1 ATOM 377 C CG . LEU A 1 49 ? 25.067 4.849 13.426 1.00 27.51 ? 49 LEU A CG 1 ATOM 378 C CD1 . LEU A 1 49 ? 24.922 4.293 14.833 1.00 28.27 ? 49 LEU A CD1 1 ATOM 379 C CD2 . LEU A 1 49 ? 24.683 3.808 12.384 1.00 27.85 ? 49 LEU A CD2 1 ATOM 380 N N . MET A 1 50 ? 22.204 8.026 11.316 1.00 23.92 ? 50 MET A N 1 ATOM 381 C CA . MET A 1 50 ? 21.198 9.076 11.435 1.00 23.60 ? 50 MET A CA 1 ATOM 382 C C . MET A 1 50 ? 20.026 8.536 12.223 1.00 23.64 ? 50 MET A C 1 ATOM 383 O O . MET A 1 50 ? 19.444 7.518 11.848 1.00 23.09 ? 50 MET A O 1 ATOM 384 C CB . MET A 1 50 ? 20.647 9.495 10.076 1.00 23.63 ? 50 MET A CB 1 ATOM 385 C CG . MET A 1 50 ? 21.665 9.897 9.038 1.00 23.46 ? 50 MET A CG 1 ATOM 386 S SD . MET A 1 50 ? 20.802 10.668 7.655 1.00 23.46 ? 50 MET A SD 1 ATOM 387 C CE . MET A 1 50 ? 19.955 9.247 6.959 1.00 22.33 ? 50 MET A CE 1 ATOM 388 N N . HIS A 1 51 ? 19.646 9.238 13.280 1.00 23.58 ? 51 HIS A N 1 ATOM 389 C CA . HIS A 1 51 ? 18.469 8.861 14.049 1.00 24.56 ? 51 HIS A CA 1 ATOM 390 C C . HIS A 1 51 ? 17.303 9.730 13.656 1.00 23.69 ? 51 HIS A C 1 ATOM 391 O O . HIS A 1 51 ? 17.317 10.939 13.881 1.00 25.18 ? 51 HIS A O 1 ATOM 392 C CB . HIS A 1 51 ? 18.749 8.991 15.535 1.00 26.23 ? 51 HIS A CB 1 ATOM 393 C CG . HIS A 1 51 ? 19.997 8.293 15.952 1.00 28.42 ? 51 HIS A CG 1 ATOM 394 N ND1 . HIS A 1 51 ? 20.079 6.922 16.059 1.00 29.24 ? 51 HIS A ND1 1 ATOM 395 C CD2 . HIS A 1 51 ? 21.229 8.771 16.241 1.00 29.58 ? 51 HIS A CD2 1 ATOM 396 C CE1 . HIS A 1 51 ? 21.304 6.586 16.419 1.00 30.11 ? 51 HIS A CE1 1 ATOM 397 N NE2 . HIS A 1 51 ? 22.021 7.689 16.538 1.00 30.58 ? 51 HIS A NE2 1 ATOM 398 N N . LEU A 1 52 ? 16.290 9.103 13.074 1.00 22.46 ? 52 LEU A N 1 ATOM 399 C CA . LEU A 1 52 ? 15.117 9.809 12.584 1.00 22.03 ? 52 LEU A CA 1 ATOM 400 C C . LEU A 1 52 ? 13.902 9.397 13.383 1.00 23.17 ? 52 LEU A C 1 ATOM 401 O O . LEU A 1 52 ? 13.664 8.206 13.578 1.00 23.48 ? 52 LEU A O 1 ATOM 402 C CB . LEU A 1 52 ? 14.888 9.485 11.111 1.00 20.90 ? 52 LEU A CB 1 ATOM 403 C CG . LEU A 1 52 ? 16.102 9.690 10.207 1.00 19.98 ? 52 LEU A CG 1 ATOM 404 C CD1 . LEU A 1 52 ? 15.769 9.257 8.787 1.00 19.60 ? 52 LEU A CD1 1 ATOM 405 C CD2 . LEU A 1 52 ? 16.568 11.141 10.248 1.00 20.20 ? 52 LEU A CD2 1 ATOM 406 N N . PHE A 1 53 ? 13.122 10.385 13.817 1.00 23.92 ? 53 PHE A N 1 ATOM 407 C CA . PHE A 1 53 ? 11.924 10.141 14.612 1.00 24.69 ? 53 PHE A CA 1 ATOM 408 C C . PHE A 1 53 ? 10.721 10.670 13.867 1.00 24.57 ? 53 PHE A C 1 ATOM 409 O O . PHE A 1 53 ? 10.720 11.817 13.413 1.00 24.35 ? 53 PHE A O 1 ATOM 410 C CB . PHE A 1 53 ? 12.008 10.842 15.965 1.00 25.32 ? 53 PHE A CB 1 ATOM 411 C CG . PHE A 1 53 ? 13.192 10.437 16.782 1.00 26.04 ? 53 PHE A CG 1 ATOM 412 C CD1 . PHE A 1 53 ? 14.446 10.939 16.486 1.00 26.16 ? 53 PHE A CD1 1 ATOM 413 C CD2 . PHE A 1 53 ? 13.056 9.566 17.856 1.00 26.71 ? 53 PHE A CD2 1 ATOM 414 C CE1 . PHE A 1 53 ? 15.550 10.575 17.229 1.00 26.85 ? 53 PHE A CE1 1 ATOM 415 C CE2 . PHE A 1 53 ? 14.159 9.196 18.608 1.00 26.83 ? 53 PHE A CE2 1 ATOM 416 C CZ . PHE A 1 53 ? 15.407 9.703 18.295 1.00 27.24 ? 53 PHE A CZ 1 ATOM 417 N N . ASN A 1 54 ? 9.691 9.844 13.745 1.00 25.03 ? 54 ASN A N 1 ATOM 418 C CA . ASN A 1 54 ? 8.477 10.298 13.101 1.00 25.70 ? 54 ASN A CA 1 ATOM 419 C C . ASN A 1 54 ? 7.692 11.167 14.078 1.00 26.57 ? 54 ASN A C 1 ATOM 420 O O . ASN A 1 54 ? 8.094 11.343 15.231 1.00 26.49 ? 54 ASN A O 1 ATOM 421 C CB . ASN A 1 54 ? 7.659 9.134 12.514 1.00 25.86 ? 54 ASN A CB 1 ATOM 422 C CG . ASN A 1 54 ? 7.032 8.235 13.565 1.00 25.96 ? 54 ASN A CG 1 ATOM 423 O OD1 . ASN A 1 54 ? 7.084 8.508 14.759 1.00 26.18 ? 54 ASN A OD1 1 ATOM 424 N ND2 . ASN A 1 54 ? 6.434 7.140 13.108 1.00 26.04 ? 54 ASN A ND2 1 ATOM 425 N N . TYR A 1 55 ? 6.592 11.720 13.593 1.00 28.94 ? 55 TYR A N 1 ATOM 426 C CA . TYR A 1 55 ? 5.795 12.665 14.359 1.00 31.86 ? 55 TYR A CA 1 ATOM 427 C C . TYR A 1 55 ? 5.385 12.092 15.728 1.00 32.62 ? 55 TYR A C 1 ATOM 428 O O . TYR A 1 55 ? 5.295 12.827 16.711 1.00 32.64 ? 55 TYR A O 1 ATOM 429 C CB . TYR A 1 55 ? 4.580 13.064 13.529 1.00 33.61 ? 55 TYR A CB 1 ATOM 430 C CG . TYR A 1 55 ? 3.678 14.038 14.213 1.00 36.54 ? 55 TYR A CG 1 ATOM 431 C CD1 . TYR A 1 55 ? 3.920 15.408 14.151 1.00 37.82 ? 55 TYR A CD1 1 ATOM 432 C CD2 . TYR A 1 55 ? 2.581 13.592 14.934 1.00 37.62 ? 55 TYR A CD2 1 ATOM 433 C CE1 . TYR A 1 55 ? 3.080 16.305 14.787 1.00 38.52 ? 55 TYR A CE1 1 ATOM 434 C CE2 . TYR A 1 55 ? 1.742 14.477 15.570 1.00 38.90 ? 55 TYR A CE2 1 ATOM 435 C CZ . TYR A 1 55 ? 1.993 15.829 15.491 1.00 39.29 ? 55 TYR A CZ 1 ATOM 436 O OH . TYR A 1 55 ? 1.147 16.692 16.128 1.00 40.61 ? 55 TYR A OH 1 ATOM 437 N N . ASP A 1 56 ? 5.177 10.776 15.775 1.00 33.67 ? 56 ASP A N 1 ATOM 438 C CA . ASP A 1 56 ? 4.832 10.053 17.011 1.00 34.89 ? 56 ASP A CA 1 ATOM 439 C C . ASP A 1 56 ? 5.995 9.723 17.951 1.00 34.03 ? 56 ASP A C 1 ATOM 440 O O . ASP A 1 56 ? 5.764 9.208 19.046 1.00 34.98 ? 56 ASP A O 1 ATOM 441 C CB . ASP A 1 56 ? 4.123 8.739 16.660 1.00 36.77 ? 56 ASP A CB 1 ATOM 442 C CG . ASP A 1 56 ? 2.626 8.887 16.589 1.00 38.58 ? 56 ASP A CG 1 ATOM 443 O OD1 . ASP A 1 56 ? 2.151 10.013 16.329 1.00 39.81 ? 56 ASP A OD1 1 ATOM 444 O OD2 . ASP A 1 56 ? 1.922 7.875 16.801 1.00 40.63 ? 56 ASP A OD2 1 ATOM 445 N N . GLY A 1 57 ? 7.228 9.997 17.536 1.00 32.32 ? 57 GLY A N 1 ATOM 446 C CA . GLY A 1 57 ? 8.398 9.736 18.377 1.00 31.58 ? 57 GLY A CA 1 ATOM 447 C C . GLY A 1 57 ? 9.019 8.358 18.210 1.00 30.52 ? 57 GLY A C 1 ATOM 448 O O . GLY A 1 57 ? 9.990 8.033 18.893 1.00 31.47 ? 57 GLY A O 1 ATOM 449 N N . ASN A 1 58 ? 8.461 7.544 17.317 1.00 30.25 ? 58 ASN A N 1 ATOM 450 C CA . ASN A 1 58 ? 9.095 6.284 16.918 1.00 30.75 ? 58 ASN A CA 1 ATOM 451 C C . ASN A 1 58 ? 10.273 6.564 16.011 1.00 29.26 ? 58 ASN A C 1 ATOM 452 O O . ASN A 1 58 ? 10.307 7.594 15.335 1.00 29.00 ? 58 ASN A O 1 ATOM 453 C CB . ASN A 1 58 ? 8.111 5.385 16.181 1.00 32.22 ? 58 ASN A CB 1 ATOM 454 C CG . ASN A 1 58 ? 7.051 4.809 17.093 1.00 34.18 ? 58 ASN A CG 1 ATOM 455 O OD1 . ASN A 1 58 ? 7.218 4.751 18.312 1.00 36.09 ? 58 ASN A OD1 1 ATOM 456 N ND2 . ASN A 1 58 ? 5.951 4.368 16.503 1.00 35.19 ? 58 ASN A ND2 1 ATOM 457 N N . THR A 1 59 ? 11.220 5.634 15.970 1.00 27.81 ? 59 THR A N 1 ATOM 458 C CA . THR A 1 59 ? 12.519 5.921 15.385 1.00 26.60 ? 59 THR A CA 1 ATOM 459 C C . THR A 1 59 ? 13.092 4.795 14.539 1.00 24.81 ? 59 THR A C 1 ATOM 460 O O . THR A 1 59 ? 12.855 3.616 14.794 1.00 24.18 ? 59 THR A O 1 ATOM 461 C CB . THR A 1 59 ? 13.538 6.294 16.486 1.00 27.25 ? 59 THR A CB 1 ATOM 462 O OG1 . THR A 1 59 ? 14.780 6.689 15.890 1.00 28.01 ? 59 THR A OG1 1 ATOM 463 C CG2 . THR A 1 59 ? 13.774 5.130 17.466 1.00 27.18 ? 59 THR A CG2 1 ATOM 464 N N . ILE A 1 60 ? 13.834 5.191 13.509 1.00 23.42 ? 60 ILE A N 1 ATOM 465 C CA . ILE A 1 60 ? 14.743 4.294 12.815 1.00 21.99 ? 60 ILE A CA 1 ATOM 466 C C . ILE A 1 60 ? 16.130 4.910 12.886 1.00 21.72 ? 60 ILE A C 1 ATOM 467 O O . ILE A 1 60 ? 16.271 6.127 13.023 1.00 21.77 ? 60 ILE A O 1 ATOM 468 C CB . ILE A 1 60 ? 14.315 4.020 11.347 1.00 22.48 ? 60 ILE A CB 1 ATOM 469 C CG1 . ILE A 1 60 ? 14.352 5.288 10.475 1.00 22.21 ? 60 ILE A CG1 1 ATOM 470 C CG2 . ILE A 1 60 ? 12.929 3.396 11.327 1.00 22.53 ? 60 ILE A CG2 1 ATOM 471 C CD1 . ILE A 1 60 ? 14.154 5.030 8.987 1.00 22.66 ? 60 ILE A CD1 1 ATOM 472 N N . THR A 1 61 ? 17.151 4.065 12.831 1.00 20.71 ? 61 THR A N 1 ATOM 473 C CA . THR A 1 61 ? 18.515 4.522 12.690 1.00 20.96 ? 61 THR A CA 1 ATOM 474 C C . THR A 1 61 ? 18.968 4.096 11.304 1.00 19.50 ? 61 THR A C 1 ATOM 475 O O . THR A 1 61 ? 18.836 2.931 10.938 1.00 18.92 ? 61 THR A O 1 ATOM 476 C CB . THR A 1 61 ? 19.422 3.925 13.775 1.00 22.03 ? 61 THR A CB 1 ATOM 477 O OG1 . THR A 1 61 ? 18.879 4.248 15.063 1.00 23.97 ? 61 THR A OG1 1 ATOM 478 C CG2 . THR A 1 61 ? 20.843 4.469 13.673 1.00 22.37 ? 61 THR A CG2 1 ATOM 479 N N . VAL A 1 62 ? 19.482 5.050 10.537 1.00 18.13 ? 62 VAL A N 1 ATOM 480 C CA . VAL A 1 62 ? 19.905 4.807 9.165 1.00 17.56 ? 62 VAL A CA 1 ATOM 481 C C . VAL A 1 62 ? 21.429 4.868 9.081 1.00 17.46 ? 62 VAL A C 1 ATOM 482 O O . VAL A 1 62 ? 22.045 5.809 9.585 1.00 17.29 ? 62 VAL A O 1 ATOM 483 C CB . VAL A 1 62 ? 19.272 5.853 8.214 1.00 17.02 ? 62 VAL A CB 1 ATOM 484 C CG1 . VAL A 1 62 ? 19.689 5.622 6.767 1.00 16.92 ? 62 VAL A CG1 1 ATOM 485 C CG2 . VAL A 1 62 ? 17.754 5.822 8.320 1.00 17.47 ? 62 VAL A CG2 1 ATOM 486 N N . ALA A 1 63 ? 22.025 3.858 8.448 1.00 17.43 ? 63 ALA A N 1 ATOM 487 C CA . ALA A 1 63 ? 23.476 3.798 8.239 1.00 17.78 ? 63 ALA A CA 1 ATOM 488 C C . ALA A 1 63 ? 23.845 4.362 6.873 1.00 18.04 ? 63 ALA A C 1 ATOM 489 O O . ALA A 1 63 ? 23.319 3.922 5.851 1.00 17.33 ? 63 ALA A O 1 ATOM 490 C CB . ALA A 1 63 ? 23.978 2.366 8.358 1.00 17.74 ? 63 ALA A CB 1 ATOM 491 N N . VAL A 1 64 ? 24.772 5.319 6.870 1.00 18.58 ? 64 VAL A N 1 ATOM 492 C CA . VAL A 1 64 ? 25.176 6.034 5.669 1.00 18.91 ? 64 VAL A CA 1 ATOM 493 C C . VAL A 1 64 ? 26.685 5.891 5.482 1.00 20.08 ? 64 VAL A C 1 ATOM 494 O O . VAL A 1 64 ? 27.444 6.115 6.423 1.00 20.55 ? 64 VAL A O 1 ATOM 495 C CB . VAL A 1 64 ? 24.804 7.533 5.783 1.00 19.39 ? 64 VAL A CB 1 ATOM 496 C CG1 . VAL A 1 64 ? 25.254 8.319 4.561 1.00 19.59 ? 64 VAL A CG1 1 ATOM 497 C CG2 . VAL A 1 64 ? 23.302 7.702 5.981 1.00 19.09 ? 64 VAL A CG2 1 ATOM 498 N N . ASP A 1 65 ? 27.100 5.493 4.280 1.00 20.42 ? 65 ASP A N 1 ATOM 499 C CA . ASP A 1 65 ? 28.510 5.405 3.914 1.00 21.72 ? 65 ASP A CA 1 ATOM 500 C C . ASP A 1 65 ? 29.037 6.836 3.763 1.00 21.81 ? 65 ASP A C 1 ATOM 501 O O . ASP A 1 65 ? 28.519 7.600 2.951 1.00 20.99 ? 65 ASP A O 1 ATOM 502 C CB . ASP A 1 65 ? 28.649 4.602 2.610 1.00 22.61 ? 65 ASP A CB 1 ATOM 503 C CG . ASP A 1 65 ? 30.102 4.420 2.162 1.00 24.13 ? 65 ASP A CG 1 ATOM 504 O OD1 . ASP A 1 65 ? 30.934 5.321 2.388 1.00 25.44 ? 65 ASP A OD1 1 ATOM 505 O OD2 . ASP A 1 65 ? 30.396 3.370 1.553 1.00 26.07 ? 65 ASP A OD2 1 ATOM 506 N N . VAL A 1 66 ? 30.049 7.205 4.556 1.00 22.91 ? 66 VAL A N 1 ATOM 507 C CA . VAL A 1 66 ? 30.497 8.610 4.601 1.00 24.05 ? 66 VAL A CA 1 ATOM 508 C C . VAL A 1 66 ? 31.358 9.005 3.397 1.00 24.74 ? 66 VAL A C 1 ATOM 509 O O . VAL A 1 66 ? 31.618 10.194 3.197 1.00 26.03 ? 66 VAL A O 1 ATOM 510 C CB . VAL A 1 66 ? 31.199 9.003 5.932 1.00 24.04 ? 66 VAL A CB 1 ATOM 511 C CG1 . VAL A 1 66 ? 30.323 8.661 7.128 1.00 24.01 ? 66 VAL A CG1 1 ATOM 512 C CG2 . VAL A 1 66 ? 32.576 8.362 6.076 1.00 24.29 ? 66 VAL A CG2 1 ATOM 513 N N . THR A 1 67 ? 31.768 8.025 2.590 1.00 25.08 ? 67 THR A N 1 ATOM 514 C CA . THR A 1 67 ? 32.519 8.298 1.364 1.00 25.74 ? 67 THR A CA 1 ATOM 515 C C . THR A 1 67 ? 31.634 8.740 0.196 1.00 24.61 ? 67 THR A C 1 ATOM 516 O O . THR A 1 67 ? 32.114 9.414 -0.708 1.00 24.62 ? 67 THR A O 1 ATOM 517 C CB . THR A 1 67 ? 33.358 7.082 0.891 1.00 26.74 ? 67 THR A CB 1 ATOM 518 O OG1 . THR A 1 67 ? 32.504 6.039 0.401 1.00 26.65 ? 67 THR A OG1 1 ATOM 519 C CG2 . THR A 1 67 ? 34.242 6.545 2.009 1.00 27.55 ? 67 THR A CG2 1 ATOM 520 N N . ASN A 1 68 ? 30.355 8.355 0.193 1.00 22.95 ? 68 ASN A N 1 ATOM 521 C CA . ASN A 1 68 ? 29.486 8.658 -0.953 1.00 21.25 ? 68 ASN A CA 1 ATOM 522 C C . ASN A 1 68 ? 28.049 9.065 -0.600 1.00 19.79 ? 68 ASN A C 1 ATOM 523 O O . ASN A 1 68 ? 27.249 9.329 -1.492 1.00 19.99 ? 68 ASN A O 1 ATOM 524 C CB . ASN A 1 68 ? 29.472 7.473 -1.930 1.00 21.68 ? 68 ASN A CB 1 ATOM 525 C CG . ASN A 1 68 ? 29.086 6.170 -1.266 1.00 22.00 ? 68 ASN A CG 1 ATOM 526 O OD1 . ASN A 1 68 ? 28.556 6.154 -0.148 1.00 22.41 ? 68 ASN A OD1 1 ATOM 527 N ND2 . ASN A 1 68 ? 29.357 5.061 -1.946 1.00 22.69 ? 68 ASN A ND2 1 ATOM 528 N N . VAL A 1 69 ? 27.765 9.133 0.701 1.00 19.23 ? 69 VAL A N 1 ATOM 529 C CA . VAL A 1 69 ? 26.439 9.442 1.257 1.00 18.71 ? 69 VAL A CA 1 ATOM 530 C C . VAL A 1 69 ? 25.370 8.432 0.812 1.00 18.95 ? 69 VAL A C 1 ATOM 531 O O . VAL A 1 69 ? 24.188 8.775 0.725 1.00 18.04 ? 69 VAL A O 1 ATOM 532 C CB . VAL A 1 69 ? 25.973 10.888 0.935 1.00 18.50 ? 69 VAL A CB 1 ATOM 533 C CG1 . VAL A 1 69 ? 25.126 11.433 2.080 1.00 18.44 ? 69 VAL A CG1 1 ATOM 534 C CG2 . VAL A 1 69 ? 27.157 11.822 0.694 1.00 18.28 ? 69 VAL A CG2 1 ATOM 535 N N . TYR A 1 70 ? 25.787 7.199 0.530 1.00 19.36 ? 70 TYR A N 1 ATOM 536 C CA . TYR A 1 70 ? 24.856 6.134 0.157 1.00 19.69 ? 70 TYR A CA 1 ATOM 537 C C . TYR A 1 70 ? 24.293 5.521 1.428 1.00 19.15 ? 70 TYR A C 1 ATOM 538 O O . TYR A 1 70 ? 25.040 5.127 2.323 1.00 18.55 ? 70 TYR A O 1 ATOM 539 C CB . TYR A 1 70 ? 25.552 5.030 -0.647 1.00 20.83 ? 70 TYR A CB 1 ATOM 540 C CG . TYR A 1 70 ? 25.901 5.347 -2.096 1.00 22.51 ? 70 TYR A CG 1 ATOM 541 C CD1 . TYR A 1 70 ? 26.359 4.339 -2.935 1.00 24.03 ? 70 TYR A CD1 1 ATOM 542 C CD2 . TYR A 1 70 ? 25.789 6.638 -2.626 1.00 23.13 ? 70 TYR A CD2 1 ATOM 543 C CE1 . TYR A 1 70 ? 26.689 4.592 -4.257 1.00 25.30 ? 70 TYR A CE1 1 ATOM 544 C CE2 . TYR A 1 70 ? 26.118 6.900 -3.951 1.00 24.71 ? 70 TYR A CE2 1 ATOM 545 C CZ . TYR A 1 70 ? 26.565 5.872 -4.761 1.00 25.69 ? 70 TYR A CZ 1 ATOM 546 O OH . TYR A 1 70 ? 26.895 6.122 -6.077 1.00 28.38 ? 70 TYR A OH 1 ATOM 547 N N . ILE A 1 71 ? 22.970 5.438 1.504 1.00 18.95 ? 71 ILE A N 1 ATOM 548 C CA . ILE A 1 71 ? 22.329 4.677 2.564 1.00 19.14 ? 71 ILE A CA 1 ATOM 549 C C . ILE A 1 71 ? 22.597 3.194 2.308 1.00 18.84 ? 71 ILE A C 1 ATOM 550 O O . ILE A 1 71 ? 22.405 2.707 1.190 1.00 18.85 ? 71 ILE A O 1 ATOM 551 C CB . ILE A 1 71 ? 20.818 4.970 2.638 1.00 19.06 ? 71 ILE A CB 1 ATOM 552 C CG1 . ILE A 1 71 ? 20.606 6.402 3.141 1.00 19.66 ? 71 ILE A CG1 1 ATOM 553 C CG2 . ILE A 1 71 ? 20.121 3.995 3.579 1.00 19.28 ? 71 ILE A CG2 1 ATOM 554 C CD1 . ILE A 1 71 ? 19.200 6.938 2.973 1.00 20.10 ? 71 ILE A CD1 1 ATOM 555 N N . MET A 1 72 ? 23.079 2.509 3.343 1.00 19.09 ? 72 MET A N 1 ATOM 556 C CA . MET A 1 72 ? 23.381 1.074 3.304 1.00 19.88 ? 72 MET A CA 1 ATOM 557 C C . MET A 1 72 ? 22.235 0.227 3.845 1.00 19.15 ? 72 MET A C 1 ATOM 558 O O . MET A 1 72 ? 21.969 -0.865 3.346 1.00 18.36 ? 72 MET A O 1 ATOM 559 C CB . MET A 1 72 ? 24.613 0.771 4.165 1.00 21.86 ? 72 MET A CB 1 ATOM 560 C CG . MET A 1 72 ? 25.909 1.429 3.716 1.00 23.11 ? 72 MET A CG 1 ATOM 561 S SD . MET A 1 72 ? 26.560 0.726 2.193 1.00 26.51 ? 72 MET A SD 1 ATOM 562 C CE . MET A 1 72 ? 25.774 1.750 0.954 1.00 24.96 ? 72 MET A CE 1 ATOM 563 N N . GLY A 1 73 ? 21.596 0.724 4.897 1.00 18.69 ? 73 GLY A N 1 ATOM 564 C CA . GLY A 1 73 ? 20.564 -0.023 5.604 1.00 18.10 ? 73 GLY A CA 1 ATOM 565 C C . GLY A 1 73 ? 20.058 0.786 6.772 1.00 18.21 ? 73 GLY A C 1 ATOM 566 O O . GLY A 1 73 ? 20.467 1.929 6.959 1.00 18.42 ? 73 GLY A O 1 ATOM 567 N N . TYR A 1 74 ? 19.172 0.194 7.564 1.00 17.63 ? 74 TYR A N 1 ATOM 568 C CA . TYR A 1 74 ? 18.581 0.885 8.707 1.00 17.93 ? 74 TYR A CA 1 ATOM 569 C C . TYR A 1 74 ? 18.139 -0.127 9.755 1.00 18.74 ? 74 TYR A C 1 ATOM 570 O O . TYR A 1 74 ? 17.978 -1.319 9.457 1.00 19.63 ? 74 TYR A O 1 ATOM 571 C CB . TYR A 1 74 ? 17.392 1.761 8.276 1.00 17.38 ? 74 TYR A CB 1 ATOM 572 C CG . TYR A 1 74 ? 16.349 0.995 7.500 1.00 17.07 ? 74 TYR A CG 1 ATOM 573 C CD1 . TYR A 1 74 ? 16.505 0.765 6.134 1.00 17.07 ? 74 TYR A CD1 1 ATOM 574 C CD2 . TYR A 1 74 ? 15.228 0.463 8.136 1.00 17.16 ? 74 TYR A CD2 1 ATOM 575 C CE1 . TYR A 1 74 ? 15.566 0.041 5.418 1.00 17.12 ? 74 TYR A CE1 1 ATOM 576 C CE2 . TYR A 1 74 ? 14.284 -0.269 7.431 1.00 17.10 ? 74 TYR A CE2 1 ATOM 577 C CZ . TYR A 1 74 ? 14.452 -0.471 6.072 1.00 17.08 ? 74 TYR A CZ 1 ATOM 578 O OH . TYR A 1 74 ? 13.526 -1.202 5.357 1.00 18.17 ? 74 TYR A OH 1 ATOM 579 N N . LEU A 1 75 ? 17.940 0.366 10.971 1.00 20.67 ? 75 LEU A N 1 ATOM 580 C CA . LEU A 1 75 ? 17.491 -0.439 12.097 1.00 22.10 ? 75 LEU A CA 1 ATOM 581 C C . LEU A 1 75 ? 16.117 0.042 12.541 1.00 23.01 ? 75 LEU A C 1 ATOM 582 O O . LEU A 1 75 ? 15.908 1.238 12.760 1.00 23.14 ? 75 LEU A O 1 ATOM 583 C CB . LEU A 1 75 ? 18.470 -0.310 13.263 1.00 22.96 ? 75 LEU A CB 1 ATOM 584 C CG . LEU A 1 75 ? 18.107 -1.044 14.560 1.00 23.67 ? 75 LEU A CG 1 ATOM 585 C CD1 . LEU A 1 75 ? 18.282 -2.541 14.381 1.00 24.00 ? 75 LEU A CD1 1 ATOM 586 C CD2 . LEU A 1 75 ? 18.974 -0.549 15.706 1.00 24.28 ? 75 LEU A CD2 1 ATOM 587 N N . ALA A 1 76 ? 15.195 -0.902 12.690 1.00 23.88 ? 76 ALA A N 1 ATOM 588 C CA . ALA A 1 76 ? 13.853 -0.609 13.175 1.00 25.54 ? 76 ALA A CA 1 ATOM 589 C C . ALA A 1 76 ? 13.552 -1.553 14.331 1.00 28.09 ? 76 ALA A C 1 ATOM 590 O O . ALA A 1 76 ? 13.328 -2.744 14.116 1.00 28.53 ? 76 ALA A O 1 ATOM 591 C CB . ALA A 1 76 ? 12.848 -0.782 12.055 1.00 25.60 ? 76 ALA A CB 1 ATOM 592 N N . LEU A 1 77 ? 13.576 -1.011 15.549 1.00 30.78 ? 77 LEU A N 1 ATOM 593 C CA . LEU A 1 77 ? 13.505 -1.802 16.783 1.00 32.15 ? 77 LEU A CA 1 ATOM 594 C C . LEU A 1 77 ? 14.633 -2.855 16.824 1.00 31.36 ? 77 LEU A C 1 ATOM 595 O O . LEU A 1 77 ? 15.798 -2.499 17.005 1.00 31.70 ? 77 LEU A O 1 ATOM 596 C CB . LEU A 1 77 ? 12.097 -2.399 16.968 1.00 33.99 ? 77 LEU A CB 1 ATOM 597 C CG . LEU A 1 77 ? 11.767 -3.184 18.249 1.00 36.33 ? 77 LEU A CG 1 ATOM 598 C CD1 . LEU A 1 77 ? 12.329 -2.533 19.506 1.00 36.56 ? 77 LEU A CD1 1 ATOM 599 C CD2 . LEU A 1 77 ? 10.260 -3.362 18.370 1.00 37.23 ? 77 LEU A CD2 1 ATOM 600 N N . THR A 1 78 ? 14.314 -4.132 16.632 1.00 30.70 ? 78 THR A N 1 ATOM 601 C CA . THR A 1 78 ? 15.327 -5.186 16.746 1.00 29.46 ? 78 THR A CA 1 ATOM 602 C C . THR A 1 78 ? 15.630 -5.856 15.418 1.00 27.79 ? 78 THR A C 1 ATOM 603 O O . THR A 1 78 ? 16.283 -6.900 15.386 1.00 27.87 ? 78 THR A O 1 ATOM 604 C CB . THR A 1 78 ? 14.884 -6.280 17.728 1.00 30.15 ? 78 THR A CB 1 ATOM 605 O OG1 . THR A 1 78 ? 13.668 -6.879 17.259 1.00 30.52 ? 78 THR A OG1 1 ATOM 606 C CG2 . THR A 1 78 ? 14.668 -5.697 19.109 1.00 30.08 ? 78 THR A CG2 1 ATOM 607 N N . THR A 1 79 ? 15.163 -5.265 14.322 1.00 25.33 ? 79 THR A N 1 ATOM 608 C CA . THR A 1 79 ? 15.428 -5.820 13.012 1.00 23.93 ? 79 THR A CA 1 ATOM 609 C C . THR A 1 79 ? 16.235 -4.844 12.183 1.00 22.86 ? 79 THR A C 1 ATOM 610 O O . THR A 1 79 ? 15.871 -3.669 12.067 1.00 22.96 ? 79 THR A O 1 ATOM 611 C CB . THR A 1 79 ? 14.131 -6.145 12.259 1.00 23.77 ? 79 THR A CB 1 ATOM 612 O OG1 . THR A 1 79 ? 13.314 -7.002 13.063 1.00 23.38 ? 79 THR A OG1 1 ATOM 613 C CG2 . THR A 1 79 ? 14.437 -6.839 10.953 1.00 23.61 ? 79 THR A CG2 1 ATOM 614 N N . SER A 1 80 ? 17.329 -5.334 11.610 1.00 21.67 ? 80 SER A N 1 ATOM 615 C CA . SER A 1 80 ? 18.105 -4.546 10.663 1.00 20.54 ? 80 SER A CA 1 ATOM 616 C C . SER A 1 80 ? 17.704 -4.914 9.242 1.00 20.04 ? 80 SER A C 1 ATOM 617 O O . SER A 1 80 ? 17.271 -6.039 8.966 1.00 19.76 ? 80 SER A O 1 ATOM 618 C CB . SER A 1 80 ? 19.608 -4.743 10.872 1.00 20.57 ? 80 SER A CB 1 ATOM 619 O OG . SER A 1 80 ? 20.016 -6.074 10.593 1.00 20.83 ? 80 SER A OG 1 ATOM 620 N N . TYR A 1 81 ? 17.854 -3.949 8.343 1.00 19.21 ? 81 TYR A N 1 ATOM 621 C CA . TYR A 1 81 ? 17.518 -4.114 6.936 1.00 18.69 ? 81 TYR A CA 1 ATOM 622 C C . TYR A 1 81 ? 18.660 -3.528 6.107 1.00 18.77 ? 81 TYR A C 1 ATOM 623 O O . TYR A 1 81 ? 19.103 -2.414 6.383 1.00 18.07 ? 81 TYR A O 1 ATOM 624 C CB . TYR A 1 81 ? 16.223 -3.353 6.622 1.00 18.84 ? 81 TYR A CB 1 ATOM 625 C CG . TYR A 1 81 ? 15.029 -3.799 7.433 1.00 19.23 ? 81 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 81 ? 14.798 -3.291 8.705 1.00 19.76 ? 81 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 81 ? 14.130 -4.732 6.926 1.00 19.91 ? 81 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 81 ? 13.702 -3.691 9.450 1.00 19.95 ? 81 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 81 ? 13.030 -5.141 7.664 1.00 20.12 ? 81 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 81 ? 12.823 -4.622 8.927 1.00 20.23 ? 81 TYR A CZ 1 ATOM 631 O OH . TYR A 1 81 ? 11.733 -5.034 9.666 1.00 21.40 ? 81 TYR A OH 1 ATOM 632 N N . PHE A 1 82 ? 19.136 -4.272 5.108 1.00 19.21 ? 82 PHE A N 1 ATOM 633 C CA . PHE A 1 82 ? 20.219 -3.807 4.229 1.00 19.36 ? 82 PHE A CA 1 ATOM 634 C C . PHE A 1 82 ? 19.875 -4.013 2.756 1.00 19.87 ? 82 PHE A C 1 ATOM 635 O O . PHE A 1 82 ? 19.189 -4.975 2.397 1.00 20.10 ? 82 PHE A O 1 ATOM 636 C CB . PHE A 1 82 ? 21.528 -4.547 4.548 1.00 19.56 ? 82 PHE A CB 1 ATOM 637 C CG . PHE A 1 82 ? 22.082 -4.242 5.911 1.00 19.15 ? 82 PHE A CG 1 ATOM 638 C CD1 . PHE A 1 82 ? 22.974 -3.196 6.094 1.00 19.21 ? 82 PHE A CD1 1 ATOM 639 C CD2 . PHE A 1 82 ? 21.693 -4.984 7.013 1.00 19.05 ? 82 PHE A CD2 1 ATOM 640 C CE1 . PHE A 1 82 ? 23.477 -2.910 7.358 1.00 19.13 ? 82 PHE A CE1 1 ATOM 641 C CE2 . PHE A 1 82 ? 22.191 -4.702 8.273 1.00 19.40 ? 82 PHE A CE2 1 ATOM 642 C CZ . PHE A 1 82 ? 23.080 -3.657 8.447 1.00 19.50 ? 82 PHE A CZ 1 ATOM 643 N N . PHE A 1 83 ? 20.361 -3.118 1.901 1.00 19.80 ? 83 PHE A N 1 ATOM 644 C CA . PHE A 1 83 ? 20.209 -3.276 0.456 1.00 20.56 ? 83 PHE A CA 1 ATOM 645 C C . PHE A 1 83 ? 20.916 -4.532 -0.026 1.00 21.83 ? 83 PHE A C 1 ATOM 646 O O . PHE A 1 83 ? 21.896 -4.971 0.573 1.00 21.68 ? 83 PHE A O 1 ATOM 647 C CB . PHE A 1 83 ? 20.750 -2.058 -0.296 1.00 20.16 ? 83 PHE A CB 1 ATOM 648 C CG . PHE A 1 83 ? 19.847 -0.859 -0.229 1.00 20.17 ? 83 PHE A CG 1 ATOM 649 C CD1 . PHE A 1 83 ? 18.556 -0.929 -0.732 1.00 20.07 ? 83 PHE A CD1 1 ATOM 650 C CD2 . PHE A 1 83 ? 20.280 0.336 0.337 1.00 20.35 ? 83 PHE A CD2 1 ATOM 651 C CE1 . PHE A 1 83 ? 17.715 0.165 -0.671 1.00 20.27 ? 83 PHE A CE1 1 ATOM 652 C CE2 . PHE A 1 83 ? 19.441 1.438 0.398 1.00 20.41 ? 83 PHE A CE2 1 ATOM 653 C CZ . PHE A 1 83 ? 18.155 1.350 -0.113 1.00 20.15 ? 83 PHE A CZ 1 ATOM 654 N N . ASN A 1 84 ? 20.401 -5.109 -1.105 1.00 23.71 ? 84 ASN A N 1 ATOM 655 C CA . ASN A 1 84 ? 21.000 -6.296 -1.690 1.00 25.49 ? 84 ASN A CA 1 ATOM 656 C C . ASN A 1 84 ? 22.130 -5.883 -2.631 1.00 26.59 ? 84 ASN A C 1 ATOM 657 O O . ASN A 1 84 ? 21.955 -5.804 -3.847 1.00 27.54 ? 84 ASN A O 1 ATOM 658 C CB . ASN A 1 84 ? 19.934 -7.128 -2.412 1.00 25.76 ? 84 ASN A CB 1 ATOM 659 C CG . ASN A 1 84 ? 20.417 -8.517 -2.813 1.00 26.47 ? 84 ASN A CG 1 ATOM 660 O OD1 . ASN A 1 84 ? 19.772 -9.173 -3.628 1.00 28.05 ? 84 ASN A OD1 1 ATOM 661 N ND2 . ASN A 1 84 ? 21.528 -8.979 -2.245 1.00 26.12 ? 84 ASN A ND2 1 ATOM 662 N N . GLU A 1 85 ? 23.304 -5.610 -2.055 1.00 27.59 ? 85 GLU A N 1 ATOM 663 C CA . GLU A 1 85 ? 24.480 -5.190 -2.801 1.00 28.65 ? 85 GLU A CA 1 ATOM 664 C C . GLU A 1 85 ? 25.689 -5.362 -1.898 1.00 25.48 ? 85 GLU A C 1 ATOM 665 O O . GLU A 1 85 ? 25.565 -5.325 -0.674 1.00 27.34 ? 85 GLU A O 1 ATOM 666 C CB . GLU A 1 85 ? 24.347 -3.732 -3.240 1.00 30.54 ? 85 GLU A CB 1 ATOM 667 C CG . GLU A 1 85 ? 24.093 -2.761 -2.099 1.00 30.94 ? 85 GLU A CG 1 ATOM 668 C CD . GLU A 1 85 ? 23.490 -1.453 -2.572 1.00 32.93 ? 85 GLU A CD 1 ATOM 669 O OE1 . GLU A 1 85 ? 23.449 -1.224 -3.799 1.00 40.76 ? 85 GLU A OE1 1 ATOM 670 O OE2 . GLU A 1 85 ? 23.058 -0.652 -1.716 1.00 51.87 ? 85 GLU A OE2 1 ATOM 671 N N . PRO A 1 86 ? 26.880 -5.566 -2.487 1.00 29.09 ? 86 PRO A N 1 ATOM 672 C CA . PRO A 1 86 ? 28.097 -5.882 -1.721 1.00 28.66 ? 86 PRO A CA 1 ATOM 673 C C . PRO A 1 86 ? 28.504 -4.861 -0.652 1.00 27.60 ? 86 PRO A C 1 ATOM 674 O O . PRO A 1 86 ? 28.895 -5.251 0.447 1.00 27.92 ? 86 PRO A O 1 ATOM 675 C CB . PRO A 1 86 ? 29.178 -5.979 -2.802 1.00 29.07 ? 86 PRO A CB 1 ATOM 676 C CG . PRO A 1 86 ? 28.448 -6.305 -4.055 1.00 29.37 ? 86 PRO A CG 1 ATOM 677 C CD . PRO A 1 86 ? 27.094 -5.672 -3.943 1.00 29.37 ? 86 PRO A CD 1 ATOM 678 N N . ALA A 1 87 ? 28.412 -3.576 -0.977 1.00 27.70 ? 87 ALA A N 1 ATOM 679 C CA . ALA A 1 87 ? 28.758 -2.504 -0.040 1.00 27.09 ? 87 ALA A CA 1 ATOM 680 C C . ALA A 1 87 ? 27.882 -2.550 1.206 1.00 26.60 ? 87 ALA A C 1 ATOM 681 O O . ALA A 1 87 ? 28.352 -2.302 2.318 1.00 26.35 ? 87 ALA A O 1 ATOM 682 C CB . ALA A 1 87 ? 28.627 -1.156 -0.725 1.00 27.08 ? 87 ALA A CB 1 ATOM 683 N N . ALA A 1 88 ? 26.606 -2.876 1.019 1.00 25.81 ? 88 ALA A N 1 ATOM 684 C CA . ALA A 1 88 ? 25.686 -2.979 2.143 1.00 25.61 ? 88 ALA A CA 1 ATOM 685 C C . ALA A 1 88 ? 25.920 -4.234 2.980 1.00 26.25 ? 88 ALA A C 1 ATOM 686 O O . ALA A 1 88 ? 25.824 -4.175 4.198 1.00 25.86 ? 88 ALA A O 1 ATOM 687 C CB . ALA A 1 88 ? 24.241 -2.899 1.671 1.00 25.28 ? 88 ALA A CB 1 ATOM 688 N N . ASP A 1 89 ? 26.231 -5.369 2.352 1.00 28.27 ? 89 ASP A N 1 ATOM 689 C CA . ASP A 1 89 ? 26.539 -6.566 3.136 1.00 30.77 ? 89 ASP A CA 1 ATOM 690 C C . ASP A 1 89 ? 27.797 -6.332 3.984 1.00 30.11 ? 89 ASP A C 1 ATOM 691 O O . ASP A 1 89 ? 27.846 -6.734 5.147 1.00 30.61 ? 89 ASP A O 1 ATOM 692 C CB . ASP A 1 89 ? 26.689 -7.803 2.249 1.00 33.16 ? 89 ASP A CB 1 ATOM 693 C CG . ASP A 1 89 ? 26.998 -9.058 3.049 1.00 35.06 ? 89 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 89 ? 26.258 -9.361 4.013 1.00 37.58 ? 89 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 89 ? 27.989 -9.737 2.712 1.00 37.92 ? 89 ASP A OD2 1 ATOM 696 N N . LEU A 1 90 ? 28.796 -5.667 3.405 1.00 31.25 ? 90 LEU A N 1 ATOM 697 C CA . LEU A 1 90 ? 29.992 -5.268 4.154 1.00 31.99 ? 90 LEU A CA 1 ATOM 698 C C . LEU A 1 90 ? 29.615 -4.407 5.355 1.00 30.54 ? 90 LEU A C 1 ATOM 699 O O . LEU A 1 90 ? 30.055 -4.664 6.473 1.00 30.45 ? 90 LEU A O 1 ATOM 700 C CB . LEU A 1 90 ? 30.980 -4.503 3.263 1.00 33.98 ? 90 LEU A CB 1 ATOM 701 C CG . LEU A 1 90 ? 32.178 -3.859 3.985 1.00 35.54 ? 90 LEU A CG 1 ATOM 702 C CD1 . LEU A 1 90 ? 32.986 -4.892 4.754 1.00 36.24 ? 90 LEU A CD1 1 ATOM 703 C CD2 . LEU A 1 90 ? 33.079 -3.124 3.007 1.00 36.33 ? 90 LEU A CD2 1 ATOM 704 N N . ALA A 1 91 ? 28.790 -3.391 5.115 1.00 29.23 ? 91 ALA A N 1 ATOM 705 C CA . ALA A 1 91 ? 28.311 -2.513 6.182 1.00 28.36 ? 91 ALA A CA 1 ATOM 706 C C . ALA A 1 91 ? 27.681 -3.295 7.329 1.00 28.07 ? 91 ALA A C 1 ATOM 707 O O . ALA A 1 91 ? 27.847 -2.943 8.499 1.00 27.34 ? 91 ALA A O 1 ATOM 708 C CB . ALA A 1 91 ? 27.311 -1.509 5.623 1.00 28.22 ? 91 ALA A CB 1 ATOM 709 N N . SER A 1 92 ? 26.970 -4.369 6.990 1.00 28.59 ? 92 SER A N 1 ATOM 710 C CA . SER A 1 92 ? 26.278 -5.180 7.986 1.00 29.39 ? 92 SER A CA 1 ATOM 711 C C . SER A 1 92 ? 27.237 -5.903 8.940 1.00 31.22 ? 92 SER A C 1 ATOM 712 O O . SER A 1 92 ? 26.810 -6.430 9.962 1.00 30.93 ? 92 SER A O 1 ATOM 713 C CB . SER A 1 92 ? 25.321 -6.174 7.308 1.00 28.96 ? 92 SER A CB 1 ATOM 714 O OG . SER A 1 92 ? 25.993 -7.314 6.792 1.00 28.61 ? 92 SER A OG 1 ATOM 715 N N . GLN A 1 93 ? 28.528 -5.915 8.616 1.00 33.69 ? 93 GLN A N 1 ATOM 716 C CA . GLN A 1 93 ? 29.540 -6.431 9.541 1.00 35.62 ? 93 GLN A CA 1 ATOM 717 C C . GLN A 1 93 ? 29.868 -5.483 10.684 1.00 35.44 ? 93 GLN A C 1 ATOM 718 O O . GLN A 1 93 ? 30.434 -5.909 11.695 1.00 36.09 ? 93 GLN A O 1 ATOM 719 C CB . GLN A 1 93 ? 30.841 -6.721 8.806 1.00 37.49 ? 93 GLN A CB 1 ATOM 720 C CG . GLN A 1 93 ? 30.717 -7.789 7.742 1.00 39.15 ? 93 GLN A CG 1 ATOM 721 C CD . GLN A 1 93 ? 32.041 -8.467 7.453 1.00 41.13 ? 93 GLN A CD 1 ATOM 722 O OE1 . GLN A 1 93 ? 32.806 -8.776 8.369 1.00 42.48 ? 93 GLN A OE1 1 ATOM 723 N NE2 . GLN A 1 93 ? 32.318 -8.711 6.178 1.00 41.91 ? 93 GLN A NE2 1 ATOM 724 N N . TYR A 1 94 ? 29.538 -4.204 10.516 1.00 34.08 ? 94 TYR A N 1 ATOM 725 C CA . TYR A 1 94 ? 29.976 -3.159 11.438 1.00 33.46 ? 94 TYR A CA 1 ATOM 726 C C . TYR A 1 94 ? 28.841 -2.431 12.177 1.00 32.18 ? 94 TYR A C 1 ATOM 727 O O . TYR A 1 94 ? 29.052 -1.962 13.297 1.00 32.49 ? 94 TYR A O 1 ATOM 728 C CB . TYR A 1 94 ? 30.847 -2.151 10.679 1.00 34.10 ? 94 TYR A CB 1 ATOM 729 C CG . TYR A 1 94 ? 32.094 -2.759 10.063 1.00 34.74 ? 94 TYR A CG 1 ATOM 730 C CD1 . TYR A 1 94 ? 33.262 -2.907 10.810 1.00 36.37 ? 94 TYR A CD1 1 ATOM 731 C CD2 . TYR A 1 94 ? 32.108 -3.186 8.739 1.00 35.38 ? 94 TYR A CD2 1 ATOM 732 C CE1 . TYR A 1 94 ? 34.403 -3.464 10.255 1.00 36.53 ? 94 TYR A CE1 1 ATOM 733 C CE2 . TYR A 1 94 ? 33.247 -3.744 8.177 1.00 36.22 ? 94 TYR A CE2 1 ATOM 734 C CZ . TYR A 1 94 ? 34.392 -3.878 8.938 1.00 37.24 ? 94 TYR A CZ 1 ATOM 735 O OH . TYR A 1 94 ? 35.525 -4.431 8.385 1.00 38.20 ? 94 TYR A OH 1 ATOM 736 N N . VAL A 1 95 ? 27.653 -2.325 11.574 1.00 29.96 ? 95 VAL A N 1 ATOM 737 C CA . VAL A 1 95 ? 26.533 -1.619 12.226 1.00 29.25 ? 95 VAL A CA 1 ATOM 738 C C . VAL A 1 95 ? 25.347 -2.536 12.520 1.00 28.61 ? 95 VAL A C 1 ATOM 739 O O . VAL A 1 95 ? 25.123 -3.527 11.819 1.00 29.16 ? 95 VAL A O 1 ATOM 740 C CB . VAL A 1 95 ? 26.015 -0.408 11.410 1.00 28.96 ? 95 VAL A CB 1 ATOM 741 C CG1 . VAL A 1 95 ? 27.091 0.659 11.268 1.00 29.37 ? 95 VAL A CG1 1 ATOM 742 C CG2 . VAL A 1 95 ? 25.492 -0.838 10.045 1.00 28.61 ? 95 VAL A CG2 1 ATOM 743 N N . PHE A 1 96 ? 24.596 -2.180 13.560 1.00 29.07 ? 96 PHE A N 1 ATOM 744 C CA . PHE A 1 96 ? 23.373 -2.882 13.952 1.00 29.37 ? 96 PHE A CA 1 ATOM 745 C C . PHE A 1 96 ? 23.662 -4.340 14.287 1.00 33.14 ? 96 PHE A C 1 ATOM 746 O O . PHE A 1 96 ? 22.813 -5.213 14.103 1.00 34.22 ? 96 PHE A O 1 ATOM 747 C CB . PHE A 1 96 ? 22.296 -2.802 12.858 1.00 27.82 ? 96 PHE A CB 1 ATOM 748 C CG . PHE A 1 96 ? 22.086 -1.419 12.289 1.00 26.27 ? 96 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 96 ? 22.128 -0.286 13.102 1.00 25.94 ? 96 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 96 ? 21.804 -1.256 10.938 1.00 25.61 ? 96 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 96 ? 21.926 0.976 12.564 1.00 25.06 ? 96 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 96 ? 21.598 0.004 10.398 1.00 24.83 ? 96 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 96 ? 21.657 1.121 11.214 1.00 24.80 ? 96 PHE A CZ 1 ATOM 754 N N . ARG A 1 97 ? 24.867 -4.590 14.786 1.00 38.25 ? 97 ARG A N 1 ATOM 755 C CA . ARG A 1 97 ? 25.300 -5.938 15.115 1.00 42.53 ? 97 ARG A CA 1 ATOM 756 C C . ARG A 1 97 ? 24.412 -6.589 16.177 1.00 42.54 ? 97 ARG A C 1 ATOM 757 O O . ARG A 1 97 ? 24.201 -7.802 16.144 1.00 43.07 ? 97 ARG A O 1 ATOM 758 C CB . ARG A 1 97 ? 26.768 -5.918 15.550 1.00 45.81 ? 97 ARG A CB 1 ATOM 759 C CG . ARG A 1 97 ? 27.730 -5.573 14.412 1.00 48.71 ? 97 ARG A CG 1 ATOM 760 C CD . ARG A 1 97 ? 27.682 -6.629 13.317 1.00 51.22 ? 97 ARG A CD 1 ATOM 761 N NE . ARG A 1 97 ? 27.831 -7.949 13.918 1.00 54.22 ? 97 ARG A NE 1 ATOM 762 C CZ . ARG A 1 97 ? 28.990 -8.564 14.146 1.00 56.57 ? 97 ARG A CZ 1 ATOM 763 N NH1 . ARG A 1 97 ? 28.980 -9.753 14.730 1.00 57.29 ? 97 ARG A NH1 1 ATOM 764 N NH2 . ARG A 1 97 ? 30.153 -8.016 13.792 1.00 57.17 ? 97 ARG A NH2 1 ATOM 765 N N . SER A 1 98 ? 23.861 -5.785 17.088 1.00 42.26 ? 98 SER A N 1 ATOM 766 C CA . SER A 1 98 ? 23.012 -6.316 18.156 1.00 41.81 ? 98 SER A CA 1 ATOM 767 C C . SER A 1 98 ? 21.513 -6.403 17.797 1.00 39.92 ? 98 SER A C 1 ATOM 768 O O . SER A 1 98 ? 20.680 -6.521 18.693 1.00 39.95 ? 98 SER A O 1 ATOM 769 C CB . SER A 1 98 ? 23.223 -5.519 19.454 1.00 43.32 ? 98 SER A CB 1 ATOM 770 O OG . SER A 1 98 ? 22.327 -4.423 19.562 1.00 44.78 ? 98 SER A OG 1 ATOM 771 N N . ALA A 1 99 ? 21.170 -6.358 16.507 1.00 37.69 ? 99 ALA A N 1 ATOM 772 C CA . ALA A 1 99 ? 19.799 -6.638 16.062 1.00 36.17 ? 99 ALA A CA 1 ATOM 773 C C . ALA A 1 99 ? 19.512 -8.130 16.203 1.00 35.80 ? 99 ALA A C 1 ATOM 774 O O . ALA A 1 99 ? 20.372 -8.959 15.906 1.00 34.81 ? 99 ALA A O 1 ATOM 775 C CB . ALA A 1 99 ? 19.595 -6.207 14.613 1.00 35.73 ? 99 ALA A CB 1 ATOM 776 N N . ARG A 1 100 ? 18.309 -8.471 16.655 1.00 35.83 ? 100 ARG A N 1 ATOM 777 C CA . ARG A 1 100 ? 17.901 -9.877 16.744 1.00 36.48 ? 100 ARG A CA 1 ATOM 778 C C . ARG A 1 100 ? 17.876 -10.568 15.382 1.00 33.26 ? 100 ARG A C 1 ATOM 779 O O . ARG A 1 100 ? 18.129 -11.766 15.291 1.00 32.25 ? 100 ARG A O 1 ATOM 780 C CB . ARG A 1 100 ? 16.516 -10.004 17.371 1.00 39.62 ? 100 ARG A CB 1 ATOM 781 C CG . ARG A 1 100 ? 16.441 -9.656 18.844 1.00 42.68 ? 100 ARG A CG 1 ATOM 782 C CD . ARG A 1 100 ? 15.008 -9.758 19.351 1.00 45.88 ? 100 ARG A CD 1 ATOM 783 N NE . ARG A 1 100 ? 14.775 -10.944 20.180 1.00 48.91 ? 100 ARG A NE 1 ATOM 784 C CZ . ARG A 1 100 ? 14.326 -12.128 19.756 1.00 52.00 ? 100 ARG A CZ 1 ATOM 785 N NH1 . ARG A 1 100 ? 14.041 -12.358 18.474 1.00 53.28 ? 100 ARG A NH1 1 ATOM 786 N NH2 . ARG A 1 100 ? 14.161 -13.109 20.639 1.00 53.16 ? 100 ARG A NH2 1 ATOM 787 N N . ARG A 1 101 ? 17.569 -9.821 14.325 1.00 30.91 ? 101 ARG A N 1 ATOM 788 C CA . ARG A 1 101 ? 17.387 -10.411 13.003 1.00 28.82 ? 101 ARG A CA 1 ATOM 789 C C . ARG A 1 101 ? 17.787 -9.421 11.892 1.00 26.51 ? 101 ARG A C 1 ATOM 790 O O . ARG A 1 101 ? 17.601 -8.213 12.049 1.00 26.95 ? 101 ARG A O 1 ATOM 791 C CB . ARG A 1 101 ? 15.932 -10.928 12.898 1.00 31.53 ? 101 ARG A CB 1 ATOM 792 C CG . ARG A 1 101 ? 15.161 -10.606 11.628 1.00 33.03 ? 101 ARG A CG 1 ATOM 793 C CD . ARG A 1 101 ? 13.680 -10.978 11.718 1.00 34.89 ? 101 ARG A CD 1 ATOM 794 N NE . ARG A 1 101 ? 12.844 -9.778 11.576 1.00 37.10 ? 101 ARG A NE 1 ATOM 795 C CZ . ARG A 1 101 ? 11.609 -9.718 11.063 1.00 39.37 ? 101 ARG A CZ 1 ATOM 796 N NH1 . ARG A 1 101 ? 10.967 -10.796 10.608 1.00 39.41 ? 101 ARG A NH1 1 ATOM 797 N NH2 . ARG A 1 101 ? 11.004 -8.533 11.003 1.00 40.47 ? 101 ARG A NH2 1 ATOM 798 N N . LYS A 1 102 ? 18.381 -9.935 10.812 1.00 23.67 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 18.814 -9.115 9.662 1.00 23.31 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 18.135 -9.531 8.363 1.00 22.72 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 18.325 -10.647 7.875 1.00 22.66 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 20.333 -9.180 9.438 1.00 23.78 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 20.771 -8.495 8.142 1.00 24.67 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 22.276 -8.459 7.956 1.00 25.75 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 22.798 -9.692 7.244 1.00 26.29 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 24.278 -9.592 7.177 1.00 26.87 ? 102 LYS A NZ 1 ATOM 807 N N . ILE A 1 103 ? 17.384 -8.606 7.777 1.00 21.44 ? 103 ILE A N 1 ATOM 808 C CA . ILE A 1 103 ? 16.734 -8.828 6.495 1.00 20.99 ? 103 ILE A CA 1 ATOM 809 C C . ILE A 1 103 ? 17.511 -8.132 5.371 1.00 21.18 ? 103 ILE A C 1 ATOM 810 O O . ILE A 1 103 ? 17.874 -6.959 5.495 1.00 20.90 ? 103 ILE A O 1 ATOM 811 C CB . ILE A 1 103 ? 15.272 -8.313 6.539 1.00 20.77 ? 103 ILE A CB 1 ATOM 812 C CG1 . ILE A 1 103 ? 14.444 -9.168 7.514 1.00 21.09 ? 103 ILE A CG1 1 ATOM 813 C CG2 . ILE A 1 103 ? 14.660 -8.290 5.140 1.00 20.95 ? 103 ILE A CG2 1 ATOM 814 C CD1 . ILE A 1 103 ? 13.061 -8.635 7.834 1.00 21.44 ? 103 ILE A CD1 1 ATOM 815 N N . THR A 1 104 ? 17.773 -8.855 4.284 1.00 21.55 ? 104 THR A N 1 ATOM 816 C CA . THR A 1 104 ? 18.307 -8.252 3.065 1.00 22.26 ? 104 THR A CA 1 ATOM 817 C C . THR A 1 104 ? 17.114 -7.915 2.200 1.00 22.09 ? 104 THR A C 1 ATOM 818 O O . THR A 1 104 ? 16.327 -8.791 1.839 1.00 22.00 ? 104 THR A O 1 ATOM 819 C CB . THR A 1 104 ? 19.253 -9.186 2.271 1.00 22.79 ? 104 THR A CB 1 ATOM 820 O OG1 . THR A 1 104 ? 20.335 -9.605 3.106 1.00 23.33 ? 104 THR A OG1 1 ATOM 821 C CG2 . THR A 1 104 ? 19.822 -8.476 1.029 1.00 23.11 ? 104 THR A CG2 1 ATOM 822 N N . LEU A 1 105 ? 16.980 -6.635 1.875 1.00 21.87 ? 105 LEU A N 1 ATOM 823 C CA . LEU A 1 105 ? 15.911 -6.164 1.005 1.00 22.48 ? 105 LEU A CA 1 ATOM 824 C C . LEU A 1 105 ? 16.035 -6.787 -0.384 1.00 23.62 ? 105 LEU A C 1 ATOM 825 O O . LEU A 1 105 ? 17.140 -7.074 -0.833 1.00 24.77 ? 105 LEU A O 1 ATOM 826 C CB . LEU A 1 105 ? 15.955 -4.636 0.921 1.00 21.76 ? 105 LEU A CB 1 ATOM 827 C CG . LEU A 1 105 ? 15.723 -3.929 2.260 1.00 21.90 ? 105 LEU A CG 1 ATOM 828 C CD1 . LEU A 1 105 ? 16.157 -2.473 2.199 1.00 22.11 ? 105 LEU A CD1 1 ATOM 829 C CD2 . LEU A 1 105 ? 14.262 -4.048 2.672 1.00 22.32 ? 105 LEU A CD2 1 ATOM 830 N N . PRO A 1 106 ? 14.899 -7.010 -1.071 1.00 23.96 ? 106 PRO A N 1 ATOM 831 C CA . PRO A 1 106 ? 14.916 -7.640 -2.388 1.00 24.57 ? 106 PRO A CA 1 ATOM 832 C C . PRO A 1 106 ? 15.202 -6.643 -3.531 1.00 25.06 ? 106 PRO A C 1 ATOM 833 O O . PRO A 1 106 ? 14.555 -6.678 -4.580 1.00 25.76 ? 106 PRO A O 1 ATOM 834 C CB . PRO A 1 106 ? 13.511 -8.249 -2.477 1.00 24.04 ? 106 PRO A CB 1 ATOM 835 C CG . PRO A 1 106 ? 12.664 -7.284 -1.732 1.00 24.43 ? 106 PRO A CG 1 ATOM 836 C CD . PRO A 1 106 ? 13.519 -6.828 -0.578 1.00 24.31 ? 106 PRO A CD 1 ATOM 837 N N . TYR A 1 107 ? 16.192 -5.776 -3.309 1.00 23.84 ? 107 TYR A N 1 ATOM 838 C CA . TYR A 1 107 ? 16.678 -4.829 -4.304 1.00 23.23 ? 107 TYR A CA 1 ATOM 839 C C . TYR A 1 107 ? 17.931 -4.144 -3.771 1.00 23.47 ? 107 TYR A C 1 ATOM 840 O O . TYR A 1 107 ? 18.137 -4.060 -2.559 1.00 22.57 ? 107 TYR A O 1 ATOM 841 C CB . TYR A 1 107 ? 15.621 -3.769 -4.644 1.00 22.82 ? 107 TYR A CB 1 ATOM 842 C CG . TYR A 1 107 ? 14.752 -3.351 -3.474 1.00 22.00 ? 107 TYR A CG 1 ATOM 843 C CD1 . TYR A 1 107 ? 15.226 -2.491 -2.487 1.00 21.40 ? 107 TYR A CD1 1 ATOM 844 C CD2 . TYR A 1 107 ? 13.445 -3.828 -3.356 1.00 21.29 ? 107 TYR A CD2 1 ATOM 845 C CE1 . TYR A 1 107 ? 14.423 -2.123 -1.416 1.00 20.88 ? 107 TYR A CE1 1 ATOM 846 C CE2 . TYR A 1 107 ? 12.635 -3.461 -2.297 1.00 21.06 ? 107 TYR A CE2 1 ATOM 847 C CZ . TYR A 1 107 ? 13.129 -2.612 -1.328 1.00 20.67 ? 107 TYR A CZ 1 ATOM 848 O OH . TYR A 1 107 ? 12.329 -2.253 -0.280 1.00 20.85 ? 107 TYR A OH 1 ATOM 849 N N . SER A 1 108 ? 18.767 -3.680 -4.692 1.00 24.49 ? 108 SER A N 1 ATOM 850 C CA . SER A 1 108 ? 19.862 -2.776 -4.369 1.00 25.00 ? 108 SER A CA 1 ATOM 851 C C . SER A 1 108 ? 19.304 -1.385 -4.108 1.00 24.67 ? 108 SER A C 1 ATOM 852 O O . SER A 1 108 ? 18.102 -1.146 -4.233 1.00 24.99 ? 108 SER A O 1 ATOM 853 C CB . SER A 1 108 ? 20.831 -2.688 -5.539 1.00 24.75 ? 108 SER A CB 1 ATOM 854 O OG . SER A 1 108 ? 20.222 -1.990 -6.606 1.00 25.52 ? 108 SER A OG 1 ATOM 855 N N . GLY A 1 109 ? 20.196 -0.457 -3.782 1.00 24.63 ? 109 GLY A N 1 ATOM 856 C CA . GLY A 1 109 ? 19.802 0.906 -3.484 1.00 24.60 ? 109 GLY A CA 1 ATOM 857 C C . GLY A 1 109 ? 19.824 1.864 -4.655 1.00 25.04 ? 109 GLY A C 1 ATOM 858 O O . GLY A 1 109 ? 19.561 3.051 -4.477 1.00 24.79 ? 109 GLY A O 1 ATOM 859 N N . ASN A 1 110 ? 20.129 1.402 -5.862 1.00 25.84 ? 110 ASN A N 1 ATOM 860 C CA . ASN A 1 110 ? 20.134 2.362 -6.957 1.00 27.33 ? 110 ASN A CA 1 ATOM 861 C C . ASN A 1 110 ? 18.729 2.735 -7.401 1.00 26.46 ? 110 ASN A C 1 ATOM 862 O O . ASN A 1 110 ? 17.781 1.949 -7.298 1.00 26.43 ? 110 ASN A O 1 ATOM 863 C CB . ASN A 1 110 ? 20.996 1.935 -8.128 1.00 29.13 ? 110 ASN A CB 1 ATOM 864 C CG . ASN A 1 110 ? 20.423 0.772 -8.872 1.00 30.09 ? 110 ASN A CG 1 ATOM 865 O OD1 . ASN A 1 110 ? 19.682 0.936 -9.847 1.00 31.20 ? 110 ASN A OD1 1 ATOM 866 N ND2 . ASN A 1 110 ? 20.762 -0.421 -8.424 1.00 32.15 ? 110 ASN A ND2 1 ATOM 867 N N . TYR A 1 111 ? 18.615 3.963 -7.879 1.00 25.56 ? 111 TYR A N 1 ATOM 868 C CA . TYR A 1 111 ? 17.321 4.558 -8.140 1.00 25.44 ? 111 TYR A CA 1 ATOM 869 C C . TYR A 1 111 ? 16.460 3.738 -9.075 1.00 26.72 ? 111 TYR A C 1 ATOM 870 O O . TYR A 1 111 ? 15.260 3.616 -8.858 1.00 25.94 ? 111 TYR A O 1 ATOM 871 C CB . TYR A 1 111 ? 17.494 5.951 -8.726 1.00 24.83 ? 111 TYR A CB 1 ATOM 872 C CG . TYR A 1 111 ? 17.656 7.052 -7.707 1.00 24.50 ? 111 TYR A CG 1 ATOM 873 C CD1 . TYR A 1 111 ? 16.936 7.048 -6.511 1.00 24.15 ? 111 TYR A CD1 1 ATOM 874 C CD2 . TYR A 1 111 ? 18.486 8.131 -7.964 1.00 24.32 ? 111 TYR A CD2 1 ATOM 875 C CE1 . TYR A 1 111 ? 17.064 8.076 -5.596 1.00 23.74 ? 111 TYR A CE1 1 ATOM 876 C CE2 . TYR A 1 111 ? 18.619 9.163 -7.054 1.00 24.11 ? 111 TYR A CE2 1 ATOM 877 C CZ . TYR A 1 111 ? 17.905 9.132 -5.872 1.00 23.75 ? 111 TYR A CZ 1 ATOM 878 O OH . TYR A 1 111 ? 18.031 10.152 -4.960 1.00 23.19 ? 111 TYR A OH 1 ATOM 879 N N . GLU A 1 112 ? 17.072 3.175 -10.108 1.00 28.77 ? 112 GLU A N 1 ATOM 880 C CA . GLU A 1 112 ? 16.304 2.506 -11.147 1.00 31.14 ? 112 GLU A CA 1 ATOM 881 C C . GLU A 1 112 ? 15.688 1.222 -10.595 1.00 30.64 ? 112 GLU A C 1 ATOM 882 O O . GLU A 1 112 ? 14.518 0.932 -10.851 1.00 30.35 ? 112 GLU A O 1 ATOM 883 C CB . GLU A 1 112 ? 17.172 2.238 -12.379 1.00 33.02 ? 112 GLU A CB 1 ATOM 884 C CG . GLU A 1 112 ? 17.645 3.508 -13.090 1.00 35.29 ? 112 GLU A CG 1 ATOM 885 C CD . GLU A 1 112 ? 18.760 4.252 -12.360 1.00 36.92 ? 112 GLU A CD 1 ATOM 886 O OE1 . GLU A 1 112 ? 19.526 3.619 -11.600 1.00 39.15 ? 112 GLU A OE1 1 ATOM 887 O OE2 . GLU A 1 112 ? 18.876 5.483 -12.544 1.00 39.81 ? 112 GLU A OE2 1 ATOM 888 N N . ARG A 1 113 ? 16.468 0.476 -9.817 1.00 30.62 ? 113 ARG A N 1 ATOM 889 C CA . ARG A 1 113 ? 15.956 -0.707 -9.118 1.00 31.59 ? 113 ARG A CA 1 ATOM 890 C C . ARG A 1 113 ? 14.862 -0.354 -8.119 1.00 29.41 ? 113 ARG A C 1 ATOM 891 O O . ARG A 1 113 ? 13.852 -1.047 -8.031 1.00 29.01 ? 113 ARG A O 1 ATOM 892 C CB . ARG A 1 113 ? 17.078 -1.426 -8.369 1.00 34.79 ? 113 ARG A CB 1 ATOM 893 C CG . ARG A 1 113 ? 17.959 -2.316 -9.230 1.00 37.59 ? 113 ARG A CG 1 ATOM 894 C CD . ARG A 1 113 ? 17.220 -3.558 -9.718 1.00 40.54 ? 113 ARG A CD 1 ATOM 895 N NE . ARG A 1 113 ? 16.930 -3.538 -11.152 1.00 43.69 ? 113 ARG A NE 1 ATOM 896 C CZ . ARG A 1 113 ? 16.224 -4.470 -11.796 1.00 46.39 ? 113 ARG A CZ 1 ATOM 897 N NH1 . ARG A 1 113 ? 16.027 -4.358 -13.105 1.00 47.62 ? 113 ARG A NH1 1 ATOM 898 N NH2 . ARG A 1 113 ? 15.709 -5.512 -11.145 1.00 46.81 ? 113 ARG A NH2 1 ATOM 899 N N . LEU A 1 114 ? 15.074 0.704 -7.343 1.00 26.86 ? 114 LEU A N 1 ATOM 900 C CA . LEU A 1 114 ? 14.091 1.090 -6.334 1.00 25.12 ? 114 LEU A CA 1 ATOM 901 C C . LEU A 1 114 ? 12.772 1.498 -6.979 1.00 25.15 ? 114 LEU A C 1 ATOM 902 O O . LEU A 1 114 ? 11.706 1.160 -6.473 1.00 25.79 ? 114 LEU A O 1 ATOM 903 C CB . LEU A 1 114 ? 14.611 2.227 -5.451 1.00 23.96 ? 114 LEU A CB 1 ATOM 904 C CG . LEU A 1 114 ? 15.600 1.845 -4.349 1.00 23.02 ? 114 LEU A CG 1 ATOM 905 C CD1 . LEU A 1 114 ? 16.231 3.097 -3.762 1.00 22.14 ? 114 LEU A CD1 1 ATOM 906 C CD2 . LEU A 1 114 ? 14.925 1.059 -3.241 1.00 22.94 ? 114 LEU A CD2 1 ATOM 907 N N . GLN A 1 115 ? 12.850 2.217 -8.095 1.00 26.46 ? 115 GLN A N 1 ATOM 908 C CA . GLN A 1 115 ? 11.656 2.663 -8.811 1.00 26.95 ? 115 GLN A CA 1 ATOM 909 C C . GLN A 1 115 ? 10.869 1.478 -9.359 1.00 27.93 ? 115 GLN A C 1 ATOM 910 O O . GLN A 1 115 ? 9.639 1.479 -9.313 1.00 27.94 ? 115 GLN A O 1 ATOM 911 C CB . GLN A 1 115 ? 12.035 3.621 -9.939 1.00 27.37 ? 115 GLN A CB 1 ATOM 912 C CG . GLN A 1 115 ? 12.597 4.947 -9.435 1.00 27.04 ? 115 GLN A CG 1 ATOM 913 C CD . GLN A 1 115 ? 13.126 5.873 -10.522 1.00 27.63 ? 115 GLN A CD 1 ATOM 914 O OE1 . GLN A 1 115 ? 13.247 7.078 -10.298 1.00 27.55 ? 115 GLN A OE1 1 ATOM 915 N NE2 . GLN A 1 115 ? 13.451 5.329 -11.691 1.00 27.57 ? 115 GLN A NE2 1 ATOM 916 N N . ILE A 1 116 ? 11.582 0.465 -9.853 1.00 29.03 ? 116 ILE A N 1 ATOM 917 C CA . ILE A 1 116 ? 10.951 -0.776 -10.314 1.00 30.27 ? 116 ILE A CA 1 ATOM 918 C C . ILE A 1 116 ? 10.210 -1.449 -9.155 1.00 29.83 ? 116 ILE A C 1 ATOM 919 O O . ILE A 1 116 ? 9.032 -1.778 -9.279 1.00 30.02 ? 116 ILE A O 1 ATOM 920 C CB . ILE A 1 116 ? 11.974 -1.762 -10.932 1.00 31.82 ? 116 ILE A CB 1 ATOM 921 C CG1 . ILE A 1 116 ? 12.453 -1.253 -12.299 1.00 33.26 ? 116 ILE A CG1 1 ATOM 922 C CG2 . ILE A 1 116 ? 11.361 -3.150 -11.093 1.00 32.33 ? 116 ILE A CG2 1 ATOM 923 C CD1 . ILE A 1 116 ? 13.510 -2.116 -12.972 1.00 34.03 ? 116 ILE A CD1 1 ATOM 924 N N . ALA A 1 117 ? 10.902 -1.638 -8.032 1.00 29.30 ? 117 ALA A N 1 ATOM 925 C CA . ALA A 1 117 ? 10.312 -2.281 -6.854 1.00 28.47 ? 117 ALA A CA 1 ATOM 926 C C . ALA A 1 117 ? 9.134 -1.496 -6.279 1.00 28.93 ? 117 ALA A C 1 ATOM 927 O O . ALA A 1 117 ? 8.160 -2.086 -5.811 1.00 29.19 ? 117 ALA A O 1 ATOM 928 C CB . ALA A 1 117 ? 11.370 -2.500 -5.776 1.00 28.39 ? 117 ALA A CB 1 ATOM 929 N N . ALA A 1 118 ? 9.221 -0.169 -6.315 1.00 28.27 ? 118 ALA A N 1 ATOM 930 C CA . ALA A 1 118 ? 8.187 0.682 -5.727 1.00 29.12 ? 118 ALA A CA 1 ATOM 931 C C . ALA A 1 118 ? 6.951 0.775 -6.623 1.00 30.09 ? 118 ALA A C 1 ATOM 932 O O . ALA A 1 118 ? 5.848 1.064 -6.146 1.00 30.70 ? 118 ALA A O 1 ATOM 933 C CB . ALA A 1 118 ? 8.740 2.070 -5.446 1.00 28.45 ? 118 ALA A CB 1 ATOM 934 N N . GLY A 1 119 ? 7.143 0.534 -7.917 1.00 32.10 ? 119 GLY A N 1 ATOM 935 C CA . GLY A 1 119 ? 6.053 0.559 -8.885 1.00 33.06 ? 119 GLY A CA 1 ATOM 936 C C . GLY A 1 119 ? 5.889 1.902 -9.571 1.00 34.78 ? 119 GLY A C 1 ATOM 937 O O . GLY A 1 119 ? 4.944 2.100 -10.336 1.00 34.57 ? 119 GLY A O 1 ATOM 938 N N . LYS A 1 120 ? 6.802 2.830 -9.298 1.00 35.54 ? 120 LYS A N 1 ATOM 939 C CA . LYS A 1 120 ? 6.732 4.154 -9.899 1.00 36.29 ? 120 LYS A CA 1 ATOM 940 C C . LYS A 1 120 ? 8.083 4.863 -9.882 1.00 34.94 ? 120 LYS A C 1 ATOM 941 O O . LYS A 1 120 ? 8.903 4.618 -8.996 1.00 34.28 ? 120 LYS A O 1 ATOM 942 C CB . LYS A 1 120 ? 5.649 5.009 -9.224 1.00 38.20 ? 120 LYS A CB 1 ATOM 943 C CG . LYS A 1 120 ? 5.395 4.730 -7.745 1.00 39.96 ? 120 LYS A CG 1 ATOM 944 C CD . LYS A 1 120 ? 3.999 5.172 -7.319 1.00 41.55 ? 120 LYS A CD 1 ATOM 945 C CE . LYS A 1 120 ? 3.652 6.563 -7.830 1.00 42.81 ? 120 LYS A CE 1 ATOM 946 N NZ . LYS A 1 120 ? 2.549 7.195 -7.055 1.00 43.58 ? 120 LYS A NZ 1 ATOM 947 N N . PRO A 1 121 ? 8.322 5.729 -10.881 1.00 33.76 ? 121 PRO A N 1 ATOM 948 C CA . PRO A 1 121 ? 9.525 6.539 -10.902 1.00 33.05 ? 121 PRO A CA 1 ATOM 949 C C . PRO A 1 121 ? 9.371 7.641 -9.889 1.00 31.72 ? 121 PRO A C 1 ATOM 950 O O . PRO A 1 121 ? 8.249 8.010 -9.543 1.00 32.17 ? 121 PRO A O 1 ATOM 951 C CB . PRO A 1 121 ? 9.516 7.135 -12.306 1.00 33.09 ? 121 PRO A CB 1 ATOM 952 C CG . PRO A 1 121 ? 8.071 7.292 -12.602 1.00 33.26 ? 121 PRO A CG 1 ATOM 953 C CD . PRO A 1 121 ? 7.436 6.063 -12.012 1.00 33.77 ? 121 PRO A CD 1 ATOM 954 N N . ARG A 1 122 ? 10.473 8.204 -9.436 1.00 31.47 ? 122 ARG A N 1 ATOM 955 C CA . ARG A 1 122 ? 10.358 9.153 -8.352 1.00 31.34 ? 122 ARG A CA 1 ATOM 956 C C . ARG A 1 122 ? 9.891 10.541 -8.833 1.00 31.67 ? 122 ARG A C 1 ATOM 957 O O . ARG A 1 122 ? 9.598 11.404 -8.011 1.00 31.41 ? 122 ARG A O 1 ATOM 958 C CB . ARG A 1 122 ? 11.644 9.175 -7.545 1.00 31.18 ? 122 ARG A CB 1 ATOM 959 C CG . ARG A 1 122 ? 12.785 9.840 -8.264 1.00 30.45 ? 122 ARG A CG 1 ATOM 960 C CD . ARG A 1 122 ? 14.102 9.350 -7.714 1.00 29.98 ? 122 ARG A CD 1 ATOM 961 N NE . ARG A 1 122 ? 15.181 10.142 -8.279 1.00 30.20 ? 122 ARG A NE 1 ATOM 962 C CZ . ARG A 1 122 ? 15.877 9.839 -9.375 1.00 30.43 ? 122 ARG A CZ 1 ATOM 963 N NH1 . ARG A 1 122 ? 15.646 8.728 -10.067 1.00 30.90 ? 122 ARG A NH1 1 ATOM 964 N NH2 . ARG A 1 122 ? 16.834 10.668 -9.773 1.00 29.40 ? 122 ARG A NH2 1 ATOM 965 N N . GLU A 1 123 ? 9.772 10.738 -10.152 1.00 32.74 ? 123 GLU A N 1 ATOM 966 C CA . GLU A 1 123 ? 9.041 11.894 -10.701 1.00 33.98 ? 123 GLU A CA 1 ATOM 967 C C . GLU A 1 123 ? 7.605 11.979 -10.189 1.00 32.85 ? 123 GLU A C 1 ATOM 968 O O . GLU A 1 123 ? 7.025 13.058 -10.141 1.00 32.11 ? 123 GLU A O 1 ATOM 969 C CB . GLU A 1 123 ? 8.970 11.843 -12.232 1.00 35.50 ? 123 GLU A CB 1 ATOM 970 C CG . GLU A 1 123 ? 10.204 12.373 -12.941 1.00 37.01 ? 123 GLU A CG 1 ATOM 971 C CD . GLU A 1 123 ? 11.300 11.334 -13.080 1.00 37.73 ? 123 GLU A CD 1 ATOM 972 O OE1 . GLU A 1 123 ? 11.114 10.194 -12.607 1.00 38.20 ? 123 GLU A OE1 1 ATOM 973 O OE2 . GLU A 1 123 ? 12.349 11.660 -13.675 1.00 39.99 ? 123 GLU A OE2 1 ATOM 974 N N . LYS A 1 124 ? 7.037 10.829 -9.839 1.00 32.86 ? 124 LYS A N 1 ATOM 975 C CA . LYS A 1 124 ? 5.638 10.729 -9.426 1.00 33.50 ? 124 LYS A CA 1 ATOM 976 C C . LYS A 1 124 ? 5.456 10.536 -7.933 1.00 30.51 ? 124 LYS A C 1 ATOM 977 O O . LYS A 1 124 ? 4.322 10.456 -7.460 1.00 30.43 ? 124 LYS A O 1 ATOM 978 C CB . LYS A 1 124 ? 4.991 9.545 -10.128 1.00 36.89 ? 124 LYS A CB 1 ATOM 979 C CG . LYS A 1 124 ? 5.241 9.534 -11.620 1.00 39.96 ? 124 LYS A CG 1 ATOM 980 C CD . LYS A 1 124 ? 4.237 10.410 -12.348 1.00 42.97 ? 124 LYS A CD 1 ATOM 981 C CE . LYS A 1 124 ? 3.012 9.610 -12.756 1.00 45.41 ? 124 LYS A CE 1 ATOM 982 N NZ . LYS A 1 124 ? 3.346 8.522 -13.723 1.00 46.05 ? 124 LYS A NZ 1 ATOM 983 N N . ILE A 1 125 ? 6.553 10.435 -7.190 1.00 26.78 ? 125 ILE A N 1 ATOM 984 C CA . ILE A 1 125 ? 6.461 10.222 -5.756 1.00 24.76 ? 125 ILE A CA 1 ATOM 985 C C . ILE A 1 125 ? 6.629 11.561 -5.055 1.00 23.57 ? 125 ILE A C 1 ATOM 986 O O . ILE A 1 125 ? 7.700 12.168 -5.134 1.00 22.64 ? 125 ILE A O 1 ATOM 987 C CB . ILE A 1 125 ? 7.517 9.222 -5.252 1.00 24.31 ? 125 ILE A CB 1 ATOM 988 C CG1 . ILE A 1 125 ? 7.338 7.878 -5.971 1.00 24.24 ? 125 ILE A CG1 1 ATOM 989 C CG2 . ILE A 1 125 ? 7.401 9.052 -3.739 1.00 24.53 ? 125 ILE A CG2 1 ATOM 990 C CD1 . ILE A 1 125 ? 8.405 6.846 -5.667 1.00 23.62 ? 125 ILE A CD1 1 ATOM 991 N N . PRO A 1 126 ? 5.571 12.031 -4.371 1.00 22.57 ? 126 PRO A N 1 ATOM 992 C CA . PRO A 1 126 ? 5.709 13.264 -3.604 1.00 22.02 ? 126 PRO A CA 1 ATOM 993 C C . PRO A 1 126 ? 6.759 13.160 -2.502 1.00 20.70 ? 126 PRO A C 1 ATOM 994 O O . PRO A 1 126 ? 6.852 12.128 -1.831 1.00 21.36 ? 126 PRO A O 1 ATOM 995 C CB . PRO A 1 126 ? 4.324 13.454 -2.979 1.00 22.39 ? 126 PRO A CB 1 ATOM 996 C CG . PRO A 1 126 ? 3.395 12.712 -3.869 1.00 22.67 ? 126 PRO A CG 1 ATOM 997 C CD . PRO A 1 126 ? 4.177 11.543 -4.384 1.00 22.79 ? 126 PRO A CD 1 ATOM 998 N N . ILE A 1 127 ? 7.542 14.225 -2.340 1.00 19.87 ? 127 ILE A N 1 ATOM 999 C CA . ILE A 1 127 ? 8.497 14.324 -1.245 1.00 19.35 ? 127 ILE A CA 1 ATOM 1000 C C . ILE A 1 127 ? 8.241 15.567 -0.401 1.00 18.93 ? 127 ILE A C 1 ATOM 1001 O O . ILE A 1 127 ? 7.507 16.471 -0.797 1.00 18.82 ? 127 ILE A O 1 ATOM 1002 C CB . ILE A 1 127 ? 9.958 14.287 -1.749 1.00 19.81 ? 127 ILE A CB 1 ATOM 1003 C CG1 . ILE A 1 127 ? 10.260 15.442 -2.712 1.00 20.15 ? 127 ILE A CG1 1 ATOM 1004 C CG2 . ILE A 1 127 ? 10.217 12.959 -2.434 1.00 19.88 ? 127 ILE A CG2 1 ATOM 1005 C CD1 . ILE A 1 127 ? 11.706 15.511 -3.169 1.00 20.48 ? 127 ILE A CD1 1 ATOM 1006 N N . GLY A 1 128 ? 8.851 15.590 0.772 1.00 18.12 ? 128 GLY A N 1 ATOM 1007 C CA . GLY A 1 128 ? 8.620 16.640 1.749 1.00 17.92 ? 128 GLY A CA 1 ATOM 1008 C C . GLY A 1 128 ? 8.771 16.077 3.138 1.00 17.90 ? 128 GLY A C 1 ATOM 1009 O O . GLY A 1 128 ? 9.095 14.898 3.310 1.00 17.93 ? 128 GLY A O 1 ATOM 1010 N N . LEU A 1 129 ? 8.529 16.909 4.142 1.00 17.72 ? 129 LEU A N 1 ATOM 1011 C CA . LEU A 1 129 ? 8.638 16.444 5.517 1.00 17.89 ? 129 LEU A CA 1 ATOM 1012 C C . LEU A 1 129 ? 7.478 15.526 5.915 1.00 17.87 ? 129 LEU A C 1 ATOM 1013 O O . LEU A 1 129 ? 7.714 14.529 6.583 1.00 18.12 ? 129 LEU A O 1 ATOM 1014 C CB . LEU A 1 129 ? 8.835 17.603 6.505 1.00 18.08 ? 129 LEU A CB 1 ATOM 1015 C CG . LEU A 1 129 ? 10.111 18.422 6.290 1.00 18.45 ? 129 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 129 ? 10.216 19.494 7.363 1.00 19.01 ? 129 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 129 ? 11.372 17.568 6.282 1.00 18.47 ? 129 LEU A CD2 1 ATOM 1018 N N . PRO A 1 130 ? 6.235 15.827 5.485 1.00 17.93 ? 130 PRO A N 1 ATOM 1019 C CA . PRO A 1 130 ? 5.206 14.814 5.756 1.00 17.87 ? 130 PRO A CA 1 ATOM 1020 C C . PRO A 1 130 ? 5.516 13.456 5.098 1.00 17.61 ? 130 PRO A C 1 ATOM 1021 O O . PRO A 1 130 ? 5.291 12.418 5.720 1.00 17.79 ? 130 PRO A O 1 ATOM 1022 C CB . PRO A 1 130 ? 3.927 15.444 5.184 1.00 18.11 ? 130 PRO A CB 1 ATOM 1023 C CG . PRO A 1 130 ? 4.187 16.917 5.224 1.00 17.99 ? 130 PRO A CG 1 ATOM 1024 C CD . PRO A 1 130 ? 5.655 17.050 4.904 1.00 17.95 ? 130 PRO A CD 1 ATOM 1025 N N . ALA A 1 131 ? 6.051 13.459 3.877 1.00 17.00 ? 131 ALA A N 1 ATOM 1026 C CA . ALA A 1 131 ? 6.424 12.202 3.206 1.00 16.74 ? 131 ALA A CA 1 ATOM 1027 C C . ALA A 1 131 ? 7.523 11.466 3.973 1.00 16.76 ? 131 ALA A C 1 ATOM 1028 O O . ALA A 1 131 ? 7.536 10.234 4.027 1.00 16.11 ? 131 ALA A O 1 ATOM 1029 C CB . ALA A 1 131 ? 6.862 12.453 1.773 1.00 17.10 ? 131 ALA A CB 1 ATOM 1030 N N . LEU A 1 132 ? 8.449 12.218 4.562 1.00 16.50 ? 132 LEU A N 1 ATOM 1031 C CA . LEU A 1 132 ? 9.486 11.603 5.382 1.00 16.97 ? 132 LEU A CA 1 ATOM 1032 C C . LEU A 1 132 ? 8.883 10.970 6.632 1.00 17.77 ? 132 LEU A C 1 ATOM 1033 O O . LEU A 1 132 ? 9.295 9.882 7.023 1.00 18.34 ? 132 LEU A O 1 ATOM 1034 C CB . LEU A 1 132 ? 10.571 12.605 5.755 1.00 16.68 ? 132 LEU A CB 1 ATOM 1035 C CG . LEU A 1 132 ? 11.708 12.068 6.627 1.00 17.09 ? 132 LEU A CG 1 ATOM 1036 C CD1 . LEU A 1 132 ? 12.422 10.886 5.987 1.00 16.97 ? 132 LEU A CD1 1 ATOM 1037 C CD2 . LEU A 1 132 ? 12.688 13.187 6.925 1.00 16.90 ? 132 LEU A CD2 1 ATOM 1038 N N . ASP A 1 133 ? 7.913 11.638 7.261 1.00 19.04 ? 133 ASP A N 1 ATOM 1039 C CA . ASP A 1 133 ? 7.217 11.030 8.407 1.00 19.95 ? 133 ASP A CA 1 ATOM 1040 C C . ASP A 1 133 ? 6.605 9.695 7.984 1.00 19.94 ? 133 ASP A C 1 ATOM 1041 O O . ASP A 1 133 ? 6.754 8.685 8.677 1.00 19.99 ? 133 ASP A O 1 ATOM 1042 C CB . ASP A 1 133 ? 6.127 11.946 8.987 1.00 21.50 ? 133 ASP A CB 1 ATOM 1043 C CG . ASP A 1 133 ? 5.248 11.229 10.019 1.00 22.36 ? 133 ASP A CG 1 ATOM 1044 O OD1 . ASP A 1 133 ? 5.730 10.958 11.130 1.00 24.56 ? 133 ASP A OD1 1 ATOM 1045 O OD2 . ASP A 1 133 ? 4.081 10.919 9.705 1.00 25.14 ? 133 ASP A OD2 1 ATOM 1046 N N . THR A 1 134 ? 5.923 9.701 6.843 1.00 19.91 ? 134 THR A N 1 ATOM 1047 C CA . THR A 1 134 ? 5.315 8.488 6.309 1.00 20.33 ? 134 THR A CA 1 ATOM 1048 C C . THR A 1 134 ? 6.361 7.410 6.056 1.00 19.78 ? 134 THR A C 1 ATOM 1049 O O . THR A 1 134 ? 6.135 6.233 6.360 1.00 19.93 ? 134 THR A O 1 ATOM 1050 C CB . THR A 1 134 ? 4.570 8.761 4.997 1.00 21.23 ? 134 THR A CB 1 ATOM 1051 O OG1 . THR A 1 134 ? 3.607 9.797 5.205 1.00 23.77 ? 134 THR A OG1 1 ATOM 1052 C CG2 . THR A 1 134 ? 3.863 7.528 4.525 1.00 21.76 ? 134 THR A CG2 1 ATOM 1053 N N . ALA A 1 135 ? 7.502 7.817 5.505 1.00 19.00 ? 135 ALA A N 1 ATOM 1054 C CA . ALA A 1 135 ? 8.562 6.875 5.165 1.00 18.72 ? 135 ALA A CA 1 ATOM 1055 C C . ALA A 1 135 ? 9.082 6.161 6.406 1.00 18.81 ? 135 ALA A C 1 ATOM 1056 O O . ALA A 1 135 ? 9.248 4.941 6.396 1.00 18.46 ? 135 ALA A O 1 ATOM 1057 C CB . ALA A 1 135 ? 9.702 7.592 4.450 1.00 18.74 ? 135 ALA A CB 1 ATOM 1058 N N . ILE A 1 136 ? 9.342 6.924 7.465 1.00 19.19 ? 136 ILE A N 1 ATOM 1059 C CA . ILE A 1 136 ? 9.818 6.365 8.730 1.00 19.87 ? 136 ILE A CA 1 ATOM 1060 C C . ILE A 1 136 ? 8.789 5.367 9.240 1.00 21.10 ? 136 ILE A C 1 ATOM 1061 O O . ILE A 1 136 ? 9.136 4.247 9.618 1.00 21.32 ? 136 ILE A O 1 ATOM 1062 C CB . ILE A 1 136 ? 10.069 7.470 9.779 1.00 19.63 ? 136 ILE A CB 1 ATOM 1063 C CG1 . ILE A 1 136 ? 11.241 8.347 9.332 1.00 19.42 ? 136 ILE A CG1 1 ATOM 1064 C CG2 . ILE A 1 136 ? 10.361 6.883 11.154 1.00 19.63 ? 136 ILE A CG2 1 ATOM 1065 C CD1 . ILE A 1 136 ? 11.311 9.688 10.028 1.00 19.56 ? 136 ILE A CD1 1 ATOM 1066 N N . SER A 1 137 ? 7.518 5.763 9.206 1.00 21.22 ? 137 SER A N 1 ATOM 1067 C CA . SER A 1 137 ? 6.447 4.899 9.691 1.00 22.36 ? 137 SER A CA 1 ATOM 1068 C C . SER A 1 137 ? 6.383 3.588 8.914 1.00 21.99 ? 137 SER A C 1 ATOM 1069 O O . SER A 1 137 ? 6.226 2.519 9.508 1.00 23.60 ? 137 SER A O 1 ATOM 1070 C CB . SER A 1 137 ? 5.107 5.625 9.642 1.00 23.16 ? 137 SER A CB 1 ATOM 1071 O OG . SER A 1 137 ? 5.077 6.616 10.650 1.00 23.93 ? 137 SER A OG 1 ATOM 1072 N N . THR A 1 138 ? 6.515 3.683 7.596 1.00 21.43 ? 138 THR A N 1 ATOM 1073 C CA . THR A 1 138 ? 6.541 2.520 6.709 1.00 21.90 ? 138 THR A CA 1 ATOM 1074 C C . THR A 1 138 ? 7.706 1.590 7.032 1.00 21.78 ? 138 THR A C 1 ATOM 1075 O O . THR A 1 138 ? 7.530 0.374 7.128 1.00 22.17 ? 138 THR A O 1 ATOM 1076 C CB . THR A 1 138 ? 6.616 2.958 5.231 1.00 22.21 ? 138 THR A CB 1 ATOM 1077 O OG1 . THR A 1 138 ? 5.371 3.558 4.851 1.00 23.15 ? 138 THR A OG1 1 ATOM 1078 C CG2 . THR A 1 138 ? 6.891 1.779 4.298 1.00 22.44 ? 138 THR A CG2 1 ATOM 1079 N N . LEU A 1 139 ? 8.895 2.150 7.218 1.00 20.93 ? 139 LEU A N 1 ATOM 1080 C CA . LEU A 1 139 ? 10.076 1.310 7.426 1.00 21.12 ? 139 LEU A CA 1 ATOM 1081 C C . LEU A 1 139 ? 10.100 0.599 8.786 1.00 22.55 ? 139 LEU A C 1 ATOM 1082 O O . LEU A 1 139 ? 10.877 -0.335 8.983 1.00 23.05 ? 139 LEU A O 1 ATOM 1083 C CB . LEU A 1 139 ? 11.350 2.129 7.213 1.00 20.22 ? 139 LEU A CB 1 ATOM 1084 C CG . LEU A 1 139 ? 11.503 2.684 5.792 1.00 19.70 ? 139 LEU A CG 1 ATOM 1085 C CD1 . LEU A 1 139 ? 12.679 3.640 5.764 1.00 20.05 ? 139 LEU A CD1 1 ATOM 1086 C CD2 . LEU A 1 139 ? 11.673 1.614 4.718 1.00 19.46 ? 139 LEU A CD2 1 ATOM 1087 N N . LEU A 1 140 ? 9.229 1.011 9.705 1.00 24.07 ? 140 LEU A N 1 ATOM 1088 C CA . LEU A 1 140 ? 9.206 0.445 11.056 1.00 26.73 ? 140 LEU A CA 1 ATOM 1089 C C . LEU A 1 140 ? 8.807 -1.023 11.096 1.00 27.72 ? 140 LEU A C 1 ATOM 1090 O O . LEU A 1 140 ? 9.236 -1.764 11.985 1.00 28.05 ? 140 LEU A O 1 ATOM 1091 C CB . LEU A 1 140 ? 8.274 1.252 11.962 1.00 27.58 ? 140 LEU A CB 1 ATOM 1092 C CG . LEU A 1 140 ? 8.951 2.471 12.586 1.00 28.44 ? 140 LEU A CG 1 ATOM 1093 C CD1 . LEU A 1 140 ? 7.914 3.403 13.189 1.00 28.93 ? 140 LEU A CD1 1 ATOM 1094 C CD2 . LEU A 1 140 ? 9.975 2.043 13.627 1.00 29.09 ? 140 LEU A CD2 1 ATOM 1095 N N . HIS A 1 141 ? 7.968 -1.429 10.149 1.00 28.71 ? 141 HIS A N 1 ATOM 1096 C CA . HIS A 1 141 ? 7.576 -2.825 10.013 1.00 29.41 ? 141 HIS A CA 1 ATOM 1097 C C . HIS A 1 141 ? 7.648 -3.215 8.540 1.00 28.48 ? 141 HIS A C 1 ATOM 1098 O O . HIS A 1 141 ? 7.138 -2.517 7.668 1.00 30.08 ? 141 HIS A O 1 ATOM 1099 C CB . HIS A 1 141 ? 6.173 -3.057 10.581 1.00 30.41 ? 141 HIS A CB 1 ATOM 1100 C CG . HIS A 1 141 ? 6.047 -2.722 12.038 1.00 32.23 ? 141 HIS A CG 1 ATOM 1101 N ND1 . HIS A 1 141 ? 5.530 -1.523 12.483 1.00 32.98 ? 141 HIS A ND1 1 ATOM 1102 C CD2 . HIS A 1 141 ? 6.374 -3.425 13.149 1.00 32.49 ? 141 HIS A CD2 1 ATOM 1103 C CE1 . HIS A 1 141 ? 5.545 -1.503 13.804 1.00 33.38 ? 141 HIS A CE1 1 ATOM 1104 N NE2 . HIS A 1 141 ? 6.049 -2.646 14.233 1.00 33.48 ? 141 HIS A NE2 1 ATOM 1105 N N . TYR A 1 142 ? 8.283 -4.348 8.285 1.00 27.41 ? 142 TYR A N 1 ATOM 1106 C CA . TYR A 1 142 ? 8.681 -4.743 6.942 1.00 25.79 ? 142 TYR A CA 1 ATOM 1107 C C . TYR A 1 142 ? 7.543 -4.873 5.929 1.00 26.32 ? 142 TYR A C 1 ATOM 1108 O O . TYR A 1 142 ? 6.520 -5.502 6.199 1.00 26.71 ? 142 TYR A O 1 ATOM 1109 C CB . TYR A 1 142 ? 9.424 -6.064 7.031 1.00 25.01 ? 142 TYR A CB 1 ATOM 1110 C CG . TYR A 1 142 ? 9.924 -6.584 5.719 1.00 23.78 ? 142 TYR A CG 1 ATOM 1111 C CD1 . TYR A 1 142 ? 10.841 -5.865 4.962 1.00 23.33 ? 142 TYR A CD1 1 ATOM 1112 C CD2 . TYR A 1 142 ? 9.500 -7.809 5.244 1.00 23.43 ? 142 TYR A CD2 1 ATOM 1113 C CE1 . TYR A 1 142 ? 11.310 -6.356 3.755 1.00 22.86 ? 142 TYR A CE1 1 ATOM 1114 C CE2 . TYR A 1 142 ? 9.955 -8.307 4.044 1.00 23.26 ? 142 TYR A CE2 1 ATOM 1115 C CZ . TYR A 1 142 ? 10.869 -7.582 3.305 1.00 22.65 ? 142 TYR A CZ 1 ATOM 1116 O OH . TYR A 1 142 ? 11.333 -8.081 2.113 1.00 22.08 ? 142 TYR A OH 1 ATOM 1117 N N . ASP A 1 143 ? 7.761 -4.293 4.755 1.00 26.53 ? 143 ASP A N 1 ATOM 1118 C CA . ASP A 1 143 ? 6.855 -4.400 3.626 1.00 26.51 ? 143 ASP A CA 1 ATOM 1119 C C . ASP A 1 143 ? 7.698 -3.945 2.424 1.00 25.71 ? 143 ASP A C 1 ATOM 1120 O O . ASP A 1 143 ? 7.893 -2.752 2.225 1.00 24.05 ? 143 ASP A O 1 ATOM 1121 C CB . ASP A 1 143 ? 5.628 -3.516 3.923 1.00 28.36 ? 143 ASP A CB 1 ATOM 1122 C CG . ASP A 1 143 ? 4.707 -3.304 2.732 1.00 29.90 ? 143 ASP A CG 1 ATOM 1123 O OD1 . ASP A 1 143 ? 5.093 -3.527 1.565 1.00 29.72 ? 143 ASP A OD1 1 ATOM 1124 O OD2 . ASP A 1 143 ? 3.560 -2.871 2.988 1.00 32.48 ? 143 ASP A OD2 1 ATOM 1125 N N . SER A 1 144 ? 8.243 -4.890 1.655 1.00 24.55 ? 144 SER A N 1 ATOM 1126 C CA . SER A 1 144 ? 9.313 -4.541 0.699 1.00 25.04 ? 144 SER A CA 1 ATOM 1127 C C . SER A 1 144 ? 8.885 -3.564 -0.408 1.00 25.23 ? 144 SER A C 1 ATOM 1128 O O . SER A 1 144 ? 9.669 -2.699 -0.802 1.00 24.31 ? 144 SER A O 1 ATOM 1129 C CB . SER A 1 144 ? 9.958 -5.786 0.089 1.00 25.11 ? 144 SER A CB 1 ATOM 1130 O OG . SER A 1 144 ? 9.085 -6.432 -0.814 1.00 25.79 ? 144 SER A OG 1 ATOM 1131 N N . THR A 1 145 ? 7.657 -3.695 -0.911 1.00 25.71 ? 145 THR A N 1 ATOM 1132 C CA . THR A 1 145 ? 7.137 -2.750 -1.914 1.00 26.50 ? 145 THR A CA 1 ATOM 1133 C C . THR A 1 145 ? 6.968 -1.353 -1.323 1.00 25.17 ? 145 THR A C 1 ATOM 1134 O O . THR A 1 145 ? 7.411 -0.375 -1.923 1.00 26.16 ? 145 THR A O 1 ATOM 1135 C CB . THR A 1 145 ? 5.789 -3.217 -2.512 1.00 27.70 ? 145 THR A CB 1 ATOM 1136 O OG1 . THR A 1 145 ? 5.970 -4.479 -3.158 1.00 28.49 ? 145 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 145 ? 5.246 -2.214 -3.538 1.00 28.23 ? 145 THR A CG2 1 ATOM 1138 N N . ALA A 1 146 ? 6.328 -1.262 -0.158 1.00 23.74 ? 146 ALA A N 1 ATOM 1139 C CA . ALA A 1 146 ? 6.159 0.021 0.516 1.00 22.66 ? 146 ALA A CA 1 ATOM 1140 C C . ALA A 1 146 ? 7.521 0.602 0.864 1.00 21.25 ? 146 ALA A C 1 ATOM 1141 O O . ALA A 1 146 ? 7.735 1.803 0.735 1.00 20.88 ? 146 ALA A O 1 ATOM 1142 C CB . ALA A 1 146 ? 5.317 -0.126 1.773 1.00 22.79 ? 146 ALA A CB 1 ATOM 1143 N N . ALA A 1 147 ? 8.435 -0.260 1.302 1.00 20.43 ? 147 ALA A N 1 ATOM 1144 C CA . ALA A 1 147 ? 9.772 0.171 1.694 1.00 19.73 ? 147 ALA A CA 1 ATOM 1145 C C . ALA A 1 147 ? 10.524 0.831 0.543 1.00 19.31 ? 147 ALA A C 1 ATOM 1146 O O . ALA A 1 147 ? 11.215 1.816 0.756 1.00 18.86 ? 147 ALA A O 1 ATOM 1147 C CB . ALA A 1 147 ? 10.569 -0.998 2.231 1.00 19.78 ? 147 ALA A CB 1 ATOM 1148 N N . ALA A 1 148 ? 10.399 0.290 -0.666 1.00 19.26 ? 148 ALA A N 1 ATOM 1149 C CA . ALA A 1 148 ? 11.080 0.868 -1.834 1.00 19.19 ? 148 ALA A CA 1 ATOM 1150 C C . ALA A 1 148 ? 10.704 2.335 -2.021 1.00 18.92 ? 148 ALA A C 1 ATOM 1151 O O . ALA A 1 148 ? 11.569 3.196 -2.196 1.00 18.18 ? 148 ALA A O 1 ATOM 1152 C CB . ALA A 1 148 ? 10.745 0.083 -3.088 1.00 19.82 ? 148 ALA A CB 1 ATOM 1153 N N . GLY A 1 149 ? 9.407 2.617 -1.989 1.00 18.56 ? 149 GLY A N 1 ATOM 1154 C CA . GLY A 1 149 ? 8.925 3.989 -2.084 1.00 18.29 ? 149 GLY A CA 1 ATOM 1155 C C . GLY A 1 149 ? 9.395 4.849 -0.922 1.00 18.01 ? 149 GLY A C 1 ATOM 1156 O O . GLY A 1 149 ? 9.809 5.997 -1.118 1.00 18.55 ? 149 GLY A O 1 ATOM 1157 N N . ALA A 1 150 ? 9.326 4.299 0.291 1.00 17.37 ? 150 ALA A N 1 ATOM 1158 C CA . ALA A 1 150 ? 9.769 5.015 1.489 1.00 17.12 ? 150 ALA A CA 1 ATOM 1159 C C . ALA A 1 150 ? 11.250 5.358 1.382 1.00 16.60 ? 150 ALA A C 1 ATOM 1160 O O . ALA A 1 150 ? 11.672 6.439 1.774 1.00 16.88 ? 150 ALA A O 1 ATOM 1161 C CB . ALA A 1 150 ? 9.518 4.190 2.738 1.00 17.28 ? 150 ALA A CB 1 ATOM 1162 N N . LEU A 1 151 ? 12.031 4.423 0.850 1.00 16.43 ? 151 LEU A N 1 ATOM 1163 C CA . LEU A 1 151 ? 13.467 4.630 0.701 1.00 16.30 ? 151 LEU A CA 1 ATOM 1164 C C . LEU A 1 151 ? 13.784 5.700 -0.337 1.00 16.29 ? 151 LEU A C 1 ATOM 1165 O O . LEU A 1 151 ? 14.710 6.478 -0.136 1.00 16.34 ? 151 LEU A O 1 ATOM 1166 C CB . LEU A 1 151 ? 14.185 3.313 0.399 1.00 16.48 ? 151 LEU A CB 1 ATOM 1167 C CG . LEU A 1 151 ? 14.242 2.392 1.623 1.00 16.61 ? 151 LEU A CG 1 ATOM 1168 C CD1 . LEU A 1 151 ? 14.496 0.942 1.219 1.00 16.80 ? 151 LEU A CD1 1 ATOM 1169 C CD2 . LEU A 1 151 ? 15.290 2.849 2.627 1.00 16.96 ? 151 LEU A CD2 1 ATOM 1170 N N . LEU A 1 152 ? 13.015 5.762 -1.424 1.00 16.68 ? 152 LEU A N 1 ATOM 1171 C CA . LEU A 1 152 ? 13.163 6.857 -2.383 1.00 16.59 ? 152 LEU A CA 1 ATOM 1172 C C . LEU A 1 152 ? 12.923 8.204 -1.725 1.00 16.03 ? 152 LEU A C 1 ATOM 1173 O O . LEU A 1 152 ? 13.638 9.163 -2.003 1.00 15.96 ? 152 LEU A O 1 ATOM 1174 C CB . LEU A 1 152 ? 12.229 6.681 -3.583 1.00 17.09 ? 152 LEU A CB 1 ATOM 1175 C CG . LEU A 1 152 ? 12.633 5.527 -4.493 1.00 17.53 ? 152 LEU A CG 1 ATOM 1176 C CD1 . LEU A 1 152 ? 11.510 5.192 -5.467 1.00 18.12 ? 152 LEU A CD1 1 ATOM 1177 C CD2 . LEU A 1 152 ? 13.924 5.854 -5.233 1.00 17.85 ? 152 LEU A CD2 1 ATOM 1178 N N . VAL A 1 153 ? 11.937 8.281 -0.836 1.00 15.61 ? 153 VAL A N 1 ATOM 1179 C CA . VAL A 1 153 ? 11.687 9.525 -0.118 1.00 15.65 ? 153 VAL A CA 1 ATOM 1180 C C . VAL A 1 153 ? 12.855 9.820 0.821 1.00 15.49 ? 153 VAL A C 1 ATOM 1181 O O . VAL A 1 153 ? 13.354 10.948 0.880 1.00 15.75 ? 153 VAL A O 1 ATOM 1182 C CB . VAL A 1 153 ? 10.374 9.466 0.684 1.00 15.80 ? 153 VAL A CB 1 ATOM 1183 C CG1 . VAL A 1 153 ? 10.225 10.699 1.567 1.00 15.62 ? 153 VAL A CG1 1 ATOM 1184 C CG2 . VAL A 1 153 ? 9.185 9.325 -0.261 1.00 16.22 ? 153 VAL A CG2 1 ATOM 1185 N N . LEU A 1 154 ? 13.292 8.795 1.543 1.00 14.85 ? 154 LEU A N 1 ATOM 1186 C CA . LEU A 1 154 ? 14.338 8.951 2.545 1.00 15.21 ? 154 LEU A CA 1 ATOM 1187 C C . LEU A 1 154 ? 15.635 9.424 1.909 1.00 14.89 ? 154 LEU A C 1 ATOM 1188 O O . LEU A 1 154 ? 16.266 10.355 2.410 1.00 14.97 ? 154 LEU A O 1 ATOM 1189 C CB . LEU A 1 154 ? 14.581 7.629 3.269 1.00 15.82 ? 154 LEU A CB 1 ATOM 1190 C CG . LEU A 1 154 ? 15.733 7.545 4.274 1.00 16.36 ? 154 LEU A CG 1 ATOM 1191 C CD1 . LEU A 1 154 ? 15.480 8.433 5.483 1.00 16.88 ? 154 LEU A CD1 1 ATOM 1192 C CD2 . LEU A 1 154 ? 15.921 6.096 4.699 1.00 17.17 ? 154 LEU A CD2 1 ATOM 1193 N N . ILE A 1 155 ? 16.022 8.787 0.805 1.00 14.90 ? 155 ILE A N 1 ATOM 1194 C CA . ILE A 1 155 ? 17.270 9.147 0.116 1.00 15.27 ? 155 ILE A CA 1 ATOM 1195 C C . ILE A 1 155 ? 17.265 10.616 -0.318 1.00 15.09 ? 155 ILE A C 1 ATOM 1196 O O . ILE A 1 155 ? 18.258 11.329 -0.135 1.00 15.07 ? 155 ILE A O 1 ATOM 1197 C CB . ILE A 1 155 ? 17.531 8.219 -1.093 1.00 15.76 ? 155 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 155 ? 17.875 6.809 -0.601 1.00 16.33 ? 155 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 155 ? 18.655 8.757 -1.980 1.00 16.04 ? 155 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 155 ? 17.567 5.731 -1.613 1.00 16.55 ? 155 ILE A CD1 1 ATOM 1201 N N . GLN A 1 156 ? 16.145 11.077 -0.863 1.00 14.94 ? 156 GLN A N 1 ATOM 1202 C CA . GLN A 1 156 ? 16.088 12.414 -1.430 1.00 15.59 ? 156 GLN A CA 1 ATOM 1203 C C . GLN A 1 156 ? 15.980 13.493 -0.373 1.00 15.54 ? 156 GLN A C 1 ATOM 1204 O O . GLN A 1 156 ? 16.477 14.606 -0.568 1.00 16.26 ? 156 GLN A O 1 ATOM 1205 C CB . GLN A 1 156 ? 14.936 12.521 -2.411 1.00 16.06 ? 156 GLN A CB 1 ATOM 1206 C CG . GLN A 1 156 ? 15.070 11.588 -3.595 1.00 16.40 ? 156 GLN A CG 1 ATOM 1207 C CD . GLN A 1 156 ? 13.885 11.716 -4.511 1.00 16.97 ? 156 GLN A CD 1 ATOM 1208 O OE1 . GLN A 1 156 ? 12.899 10.978 -4.384 1.00 18.80 ? 156 GLN A OE1 1 ATOM 1209 N NE2 . GLN A 1 156 ? 13.939 12.686 -5.402 1.00 16.88 ? 156 GLN A NE2 1 ATOM 1210 N N . THR A 1 157 ? 15.350 13.173 0.752 1.00 15.26 ? 157 THR A N 1 ATOM 1211 C CA . THR A 1 157 ? 15.182 14.155 1.817 1.00 15.42 ? 157 THR A CA 1 ATOM 1212 C C . THR A 1 157 ? 16.359 14.191 2.801 1.00 15.20 ? 157 THR A C 1 ATOM 1213 O O . THR A 1 157 ? 16.378 15.043 3.694 1.00 16.03 ? 157 THR A O 1 ATOM 1214 C CB . THR A 1 157 ? 13.876 13.942 2.616 1.00 15.30 ? 157 THR A CB 1 ATOM 1215 O OG1 . THR A 1 157 ? 13.838 12.616 3.159 1.00 16.00 ? 157 THR A OG1 1 ATOM 1216 C CG2 . THR A 1 157 ? 12.654 14.178 1.736 1.00 15.53 ? 157 THR A CG2 1 ATOM 1217 N N . THR A 1 158 ? 17.318 13.275 2.663 1.00 14.99 ? 158 THR A N 1 ATOM 1218 C CA . THR A 1 158 ? 18.498 13.261 3.525 1.00 15.16 ? 158 THR A CA 1 ATOM 1219 C C . THR A 1 158 ? 19.739 13.426 2.649 1.00 15.33 ? 158 THR A C 1 ATOM 1220 O O . THR A 1 158 ? 20.247 14.532 2.521 1.00 15.10 ? 158 THR A O 1 ATOM 1221 C CB . THR A 1 158 ? 18.558 11.997 4.416 1.00 15.35 ? 158 THR A CB 1 ATOM 1222 O OG1 . THR A 1 158 ? 18.631 10.809 3.610 1.00 15.16 ? 158 THR A OG1 1 ATOM 1223 C CG2 . THR A 1 158 ? 17.322 11.941 5.307 1.00 15.22 ? 158 THR A CG2 1 ATOM 1224 N N . ALA A 1 159 ? 20.175 12.346 2.013 1.00 15.40 ? 159 ALA A N 1 ATOM 1225 C CA . ALA A 1 159 ? 21.405 12.343 1.218 1.00 15.81 ? 159 ALA A CA 1 ATOM 1226 C C . ALA A 1 159 ? 21.412 13.381 0.095 1.00 15.88 ? 159 ALA A C 1 ATOM 1227 O O . ALA A 1 159 ? 22.384 14.125 -0.043 1.00 15.64 ? 159 ALA A O 1 ATOM 1228 C CB . ALA A 1 159 ? 21.672 10.953 0.661 1.00 16.20 ? 159 ALA A CB 1 ATOM 1229 N N . GLU A 1 160 ? 20.338 13.478 -0.688 1.00 15.90 ? 160 GLU A N 1 ATOM 1230 C CA . GLU A 1 160 ? 20.366 14.409 -1.828 1.00 15.85 ? 160 GLU A CA 1 ATOM 1231 C C . GLU A 1 160 ? 20.338 15.860 -1.358 1.00 15.65 ? 160 GLU A C 1 ATOM 1232 O O . GLU A 1 160 ? 20.979 16.729 -1.954 1.00 15.31 ? 160 GLU A O 1 ATOM 1233 C CB . GLU A 1 160 ? 19.223 14.145 -2.820 1.00 16.17 ? 160 GLU A CB 1 ATOM 1234 C CG . GLU A 1 160 ? 19.198 12.733 -3.377 1.00 16.77 ? 160 GLU A CG 1 ATOM 1235 C CD . GLU A 1 160 ? 20.305 12.435 -4.373 1.00 17.35 ? 160 GLU A CD 1 ATOM 1236 O OE1 . GLU A 1 160 ? 21.294 13.198 -4.462 1.00 18.11 ? 160 GLU A OE1 1 ATOM 1237 O OE2 . GLU A 1 160 ? 20.178 11.416 -5.078 1.00 18.57 ? 160 GLU A OE2 1 ATOM 1238 N N . ALA A 1 161 ? 19.598 16.125 -0.285 1.00 14.98 ? 161 ALA A N 1 ATOM 1239 C CA . ALA A 1 161 ? 19.584 17.463 0.318 1.00 15.41 ? 161 ALA A CA 1 ATOM 1240 C C . ALA A 1 161 ? 20.948 17.838 0.891 1.00 15.78 ? 161 ALA A C 1 ATOM 1241 O O . ALA A 1 161 ? 21.355 18.997 0.825 1.00 16.03 ? 161 ALA A O 1 ATOM 1242 C CB . ALA A 1 161 ? 18.522 17.553 1.401 1.00 15.55 ? 161 ALA A CB 1 ATOM 1243 N N . ALA A 1 162 ? 21.640 16.865 1.474 1.00 15.83 ? 162 ALA A N 1 ATOM 1244 C CA . ALA A 1 162 ? 23.000 17.097 1.963 1.00 16.22 ? 162 ALA A CA 1 ATOM 1245 C C . ALA A 1 162 ? 23.918 17.523 0.818 1.00 16.51 ? 162 ALA A C 1 ATOM 1246 O O . ALA A 1 162 ? 24.761 18.410 0.985 1.00 17.16 ? 162 ALA A O 1 ATOM 1247 C CB . ALA A 1 162 ? 23.543 15.859 2.638 1.00 16.23 ? 162 ALA A CB 1 ATOM 1248 N N . ARG A 1 163 ? 23.740 16.916 -0.348 1.00 16.32 ? 163 ARG A N 1 ATOM 1249 C CA . ARG A 1 163 ? 24.615 17.199 -1.487 1.00 17.00 ? 163 ARG A CA 1 ATOM 1250 C C . ARG A 1 163 ? 24.346 18.503 -2.203 1.00 17.05 ? 163 ARG A C 1 ATOM 1251 O O . ARG A 1 163 ? 25.273 19.078 -2.772 1.00 17.26 ? 163 ARG A O 1 ATOM 1252 C CB . ARG A 1 163 ? 24.508 16.096 -2.521 1.00 17.06 ? 163 ARG A CB 1 ATOM 1253 C CG . ARG A 1 163 ? 25.061 14.778 -2.051 1.00 17.37 ? 163 ARG A CG 1 ATOM 1254 C CD . ARG A 1 163 ? 24.507 13.718 -2.953 1.00 17.94 ? 163 ARG A CD 1 ATOM 1255 N NE . ARG A 1 163 ? 25.008 12.394 -2.631 1.00 18.62 ? 163 ARG A NE 1 ATOM 1256 C CZ . ARG A 1 163 ? 24.283 11.294 -2.740 1.00 19.55 ? 163 ARG A CZ 1 ATOM 1257 N NH1 . ARG A 1 163 ? 23.020 11.393 -3.133 1.00 20.18 ? 163 ARG A NH1 1 ATOM 1258 N NH2 . ARG A 1 163 ? 24.815 10.116 -2.442 1.00 19.56 ? 163 ARG A NH2 1 ATOM 1259 N N . PHE A 1 164 ? 23.092 18.948 -2.228 1.00 17.21 ? 164 PHE A N 1 ATOM 1260 C CA . PHE A 1 164 ? 22.727 20.152 -2.964 1.00 17.80 ? 164 PHE A CA 1 ATOM 1261 C C . PHE A 1 164 ? 21.870 21.098 -2.146 1.00 18.56 ? 164 PHE A C 1 ATOM 1262 O O . PHE A 1 164 ? 20.795 20.717 -1.697 1.00 18.30 ? 164 PHE A O 1 ATOM 1263 C CB . PHE A 1 164 ? 21.941 19.776 -4.211 1.00 17.68 ? 164 PHE A CB 1 ATOM 1264 C CG . PHE A 1 164 ? 22.726 18.994 -5.208 1.00 18.18 ? 164 PHE A CG 1 ATOM 1265 C CD1 . PHE A 1 164 ? 23.590 19.638 -6.074 1.00 18.54 ? 164 PHE A CD1 1 ATOM 1266 C CD2 . PHE A 1 164 ? 22.588 17.621 -5.299 1.00 18.54 ? 164 PHE A CD2 1 ATOM 1267 C CE1 . PHE A 1 164 ? 24.305 18.922 -7.016 1.00 18.56 ? 164 PHE A CE1 1 ATOM 1268 C CE2 . PHE A 1 164 ? 23.302 16.895 -6.236 1.00 18.74 ? 164 PHE A CE2 1 ATOM 1269 C CZ . PHE A 1 164 ? 24.164 17.550 -7.100 1.00 18.63 ? 164 PHE A CZ 1 ATOM 1270 N N . LYS A 1 165 ? 22.331 22.336 -1.989 1.00 19.70 ? 165 LYS A N 1 ATOM 1271 C CA . LYS A 1 165 ? 21.564 23.379 -1.305 1.00 21.02 ? 165 LYS A CA 1 ATOM 1272 C C . LYS A 1 165 ? 20.179 23.567 -1.924 1.00 19.86 ? 165 LYS A C 1 ATOM 1273 O O . LYS A 1 165 ? 19.195 23.742 -1.206 1.00 19.37 ? 165 LYS A O 1 ATOM 1274 C CB . LYS A 1 165 ? 22.322 24.711 -1.335 1.00 23.84 ? 165 LYS A CB 1 ATOM 1275 C CG . LYS A 1 165 ? 21.709 25.800 -0.461 1.00 26.76 ? 165 LYS A CG 1 ATOM 1276 C CD . LYS A 1 165 ? 22.484 27.113 -0.537 1.00 29.41 ? 165 LYS A CD 1 ATOM 1277 C CE . LYS A 1 165 ? 22.298 27.833 -1.871 1.00 31.29 ? 165 LYS A CE 1 ATOM 1278 N NZ . LYS A 1 165 ? 22.170 29.314 -1.722 1.00 33.33 ? 165 LYS A NZ 1 ATOM 1279 N N . TYR A 1 166 ? 20.101 23.540 -3.251 1.00 19.40 ? 166 TYR A N 1 ATOM 1280 C CA . TYR A 1 166 ? 18.812 23.668 -3.930 1.00 19.53 ? 166 TYR A CA 1 ATOM 1281 C C . TYR A 1 166 ? 17.825 22.599 -3.455 1.00 18.59 ? 166 TYR A C 1 ATOM 1282 O O . TYR A 1 166 ? 16.649 22.894 -3.215 1.00 18.71 ? 166 TYR A O 1 ATOM 1283 C CB . TYR A 1 166 ? 18.978 23.589 -5.446 1.00 20.28 ? 166 TYR A CB 1 ATOM 1284 C CG . TYR A 1 166 ? 17.667 23.484 -6.197 1.00 21.08 ? 166 TYR A CG 1 ATOM 1285 C CD1 . TYR A 1 166 ? 16.874 24.611 -6.427 1.00 21.65 ? 166 TYR A CD1 1 ATOM 1286 C CD2 . TYR A 1 166 ? 17.215 22.257 -6.673 1.00 21.36 ? 166 TYR A CD2 1 ATOM 1287 C CE1 . TYR A 1 166 ? 15.672 24.512 -7.113 1.00 21.96 ? 166 TYR A CE1 1 ATOM 1288 C CE2 . TYR A 1 166 ? 16.019 22.152 -7.366 1.00 21.87 ? 166 TYR A CE2 1 ATOM 1289 C CZ . TYR A 1 166 ? 15.251 23.284 -7.581 1.00 22.24 ? 166 TYR A CZ 1 ATOM 1290 O OH . TYR A 1 166 ? 14.055 23.200 -8.266 1.00 24.17 ? 166 TYR A OH 1 ATOM 1291 N N . ILE A 1 167 ? 18.301 21.369 -3.295 1.00 17.84 ? 167 ILE A N 1 ATOM 1292 C CA . ILE A 1 167 ? 17.412 20.276 -2.889 1.00 17.60 ? 167 ILE A CA 1 ATOM 1293 C C . ILE A 1 167 ? 16.969 20.443 -1.430 1.00 17.90 ? 167 ILE A C 1 ATOM 1294 O O . ILE A 1 167 ? 15.792 20.254 -1.109 1.00 17.62 ? 167 ILE A O 1 ATOM 1295 C CB . ILE A 1 167 ? 18.025 18.885 -3.176 1.00 17.40 ? 167 ILE A CB 1 ATOM 1296 C CG1 . ILE A 1 167 ? 18.190 18.714 -4.697 1.00 17.48 ? 167 ILE A CG1 1 ATOM 1297 C CG2 . ILE A 1 167 ? 17.135 17.784 -2.602 1.00 17.58 ? 167 ILE A CG2 1 ATOM 1298 C CD1 . ILE A 1 167 ? 18.749 17.386 -5.165 1.00 17.00 ? 167 ILE A CD1 1 ATOM 1299 N N . GLU A 1 168 ? 17.894 20.822 -0.552 1.00 18.02 ? 168 GLU A N 1 ATOM 1300 C CA . GLU A 1 168 ? 17.542 21.189 0.819 1.00 18.80 ? 168 GLU A CA 1 ATOM 1301 C C . GLU A 1 168 ? 16.408 22.226 0.843 1.00 19.05 ? 168 GLU A C 1 ATOM 1302 O O . GLU A 1 168 ? 15.425 22.069 1.570 1.00 18.49 ? 168 GLU A O 1 ATOM 1303 C CB . GLU A 1 168 ? 18.766 21.738 1.560 1.00 19.83 ? 168 GLU A CB 1 ATOM 1304 C CG . GLU A 1 168 ? 18.464 22.247 2.961 1.00 20.61 ? 168 GLU A CG 1 ATOM 1305 C CD . GLU A 1 168 ? 19.618 22.991 3.611 1.00 21.74 ? 168 GLU A CD 1 ATOM 1306 O OE1 . GLU A 1 168 ? 20.702 23.125 2.999 1.00 22.16 ? 168 GLU A OE1 1 ATOM 1307 O OE2 . GLU A 1 168 ? 19.428 23.461 4.754 1.00 23.32 ? 168 GLU A OE2 1 ATOM 1308 N N . GLN A 1 169 ? 16.549 23.276 0.040 1.00 19.33 ? 169 GLN A N 1 ATOM 1309 C CA . GLN A 1 169 ? 15.542 24.334 -0.027 1.00 20.48 ? 169 GLN A CA 1 ATOM 1310 C C . GLN A 1 169 ? 14.204 23.835 -0.566 1.00 20.28 ? 169 GLN A C 1 ATOM 1311 O O . GLN A 1 169 ? 13.148 24.262 -0.097 1.00 21.24 ? 169 GLN A O 1 ATOM 1312 C CB . GLN A 1 169 ? 16.050 25.493 -0.883 1.00 22.31 ? 169 GLN A CB 1 ATOM 1313 C CG . GLN A 1 169 ? 17.181 26.286 -0.250 1.00 24.34 ? 169 GLN A CG 1 ATOM 1314 C CD . GLN A 1 169 ? 17.932 27.146 -1.252 1.00 26.61 ? 169 GLN A CD 1 ATOM 1315 O OE1 . GLN A 1 169 ? 17.758 27.012 -2.465 1.00 29.36 ? 169 GLN A OE1 1 ATOM 1316 N NE2 . GLN A 1 169 ? 18.775 28.031 -0.749 1.00 28.40 ? 169 GLN A NE2 1 ATOM 1317 N N . GLN A 1 170 ? 14.252 22.941 -1.547 1.00 19.61 ? 170 GLN A N 1 ATOM 1318 C CA . GLN A 1 170 ? 13.042 22.320 -2.083 1.00 20.02 ? 170 GLN A CA 1 ATOM 1319 C C . GLN A 1 170 ? 12.278 21.563 -0.998 1.00 19.41 ? 170 GLN A C 1 ATOM 1320 O O . GLN A 1 170 ? 11.051 21.636 -0.937 1.00 18.95 ? 170 GLN A O 1 ATOM 1321 C CB . GLN A 1 170 ? 13.386 21.381 -3.241 1.00 21.11 ? 170 GLN A CB 1 ATOM 1322 C CG . GLN A 1 170 ? 13.780 22.115 -4.510 1.00 22.23 ? 170 GLN A CG 1 ATOM 1323 C CD . GLN A 1 170 ? 12.634 22.910 -5.096 1.00 23.32 ? 170 GLN A CD 1 ATOM 1324 O OE1 . GLN A 1 170 ? 12.643 24.148 -5.088 1.00 25.69 ? 170 GLN A OE1 1 ATOM 1325 N NE2 . GLN A 1 170 ? 11.629 22.206 -5.595 1.00 23.84 ? 170 GLN A NE2 1 ATOM 1326 N N . ILE A 1 171 ? 13.003 20.844 -0.148 1.00 19.00 ? 171 ILE A N 1 ATOM 1327 C CA . ILE A 1 171 ? 12.365 20.112 0.954 1.00 18.91 ? 171 ILE A CA 1 ATOM 1328 C C . ILE A 1 171 ? 11.816 21.087 2.005 1.00 19.79 ? 171 ILE A C 1 ATOM 1329 O O . ILE A 1 171 ? 10.741 20.857 2.563 1.00 19.18 ? 171 ILE A O 1 ATOM 1330 C CB . ILE A 1 171 ? 13.314 19.061 1.586 1.00 18.14 ? 171 ILE A CB 1 ATOM 1331 C CG1 . ILE A 1 171 ? 13.835 18.077 0.527 1.00 18.30 ? 171 ILE A CG1 1 ATOM 1332 C CG2 . ILE A 1 171 ? 12.617 18.278 2.695 1.00 17.91 ? 171 ILE A CG2 1 ATOM 1333 C CD1 . ILE A 1 171 ? 12.787 17.439 -0.360 1.00 18.53 ? 171 ILE A CD1 1 ATOM 1334 N N . GLN A 1 172 ? 12.529 22.181 2.262 1.00 20.61 ? 172 GLN A N 1 ATOM 1335 C CA . GLN A 1 172 ? 12.037 23.212 3.188 1.00 21.65 ? 172 GLN A CA 1 ATOM 1336 C C . GLN A 1 172 ? 10.715 23.821 2.741 1.00 22.84 ? 172 GLN A C 1 ATOM 1337 O O . GLN A 1 172 ? 9.854 24.123 3.569 1.00 23.59 ? 172 GLN A O 1 ATOM 1338 C CB . GLN A 1 172 ? 13.078 24.316 3.382 1.00 22.30 ? 172 GLN A CB 1 ATOM 1339 C CG . GLN A 1 172 ? 14.246 23.860 4.234 1.00 23.04 ? 172 GLN A CG 1 ATOM 1340 C CD . GLN A 1 172 ? 15.373 24.876 4.306 1.00 23.95 ? 172 GLN A CD 1 ATOM 1341 O OE1 . GLN A 1 172 ? 15.831 25.391 3.287 1.00 24.54 ? 172 GLN A OE1 1 ATOM 1342 N NE2 . GLN A 1 172 ? 15.831 25.160 5.517 1.00 24.75 ? 172 GLN A NE2 1 ATOM 1343 N N . GLU A 1 173 ? 10.565 24.001 1.432 1.00 23.65 ? 173 GLU A N 1 ATOM 1344 C CA . GLU A 1 173 ? 9.304 24.463 0.852 1.00 25.28 ? 173 GLU A CA 1 ATOM 1345 C C . GLU A 1 173 ? 8.174 23.463 1.089 1.00 24.14 ? 173 GLU A C 1 ATOM 1346 O O . GLU A 1 173 ? 7.004 23.844 1.133 1.00 24.13 ? 173 GLU A O 1 ATOM 1347 C CB . GLU A 1 173 ? 9.464 24.691 -0.648 1.00 28.11 ? 173 GLU A CB 1 ATOM 1348 C CG . GLU A 1 173 ? 10.359 25.874 -0.970 1.00 30.88 ? 173 GLU A CG 1 ATOM 1349 C CD . GLU A 1 173 ? 10.418 26.204 -2.447 1.00 33.27 ? 173 GLU A CD 1 ATOM 1350 O OE1 . GLU A 1 173 ? 11.214 27.095 -2.815 1.00 36.61 ? 173 GLU A OE1 1 ATOM 1351 O OE2 . GLU A 1 173 ? 9.681 25.578 -3.242 1.00 35.52 ? 173 GLU A OE2 1 ATOM 1352 N N . ARG A 1 174 ? 8.545 22.191 1.239 1.00 22.04 ? 174 ARG A N 1 ATOM 1353 C CA . ARG A 1 174 ? 7.602 21.096 1.439 1.00 21.14 ? 174 ARG A CA 1 ATOM 1354 C C . ARG A 1 174 ? 7.555 20.651 2.911 1.00 20.88 ? 174 ARG A C 1 ATOM 1355 O O . ARG A 1 174 ? 7.322 19.476 3.207 1.00 20.81 ? 174 ARG A O 1 ATOM 1356 C CB . ARG A 1 174 ? 7.994 19.912 0.537 1.00 21.14 ? 174 ARG A CB 1 ATOM 1357 C CG . ARG A 1 174 ? 7.959 20.168 -0.967 1.00 21.38 ? 174 ARG A CG 1 ATOM 1358 C CD . ARG A 1 174 ? 8.932 19.255 -1.716 1.00 21.49 ? 174 ARG A CD 1 ATOM 1359 N NE . ARG A 1 174 ? 8.679 19.219 -3.155 1.00 21.29 ? 174 ARG A NE 1 ATOM 1360 C CZ . ARG A 1 174 ? 8.980 20.206 -4.000 1.00 22.04 ? 174 ARG A CZ 1 ATOM 1361 N NH1 . ARG A 1 174 ? 9.562 21.319 -3.558 1.00 21.95 ? 174 ARG A NH1 1 ATOM 1362 N NH2 . ARG A 1 174 ? 8.701 20.084 -5.293 1.00 22.75 ? 174 ARG A NH2 1 ATOM 1363 N N . ALA A 1 175 ? 7.757 21.588 3.834 1.00 20.31 ? 175 ALA A N 1 ATOM 1364 C CA . ALA A 1 175 ? 7.734 21.283 5.264 1.00 20.24 ? 175 ALA A CA 1 ATOM 1365 C C . ALA A 1 175 ? 6.364 20.785 5.730 1.00 20.94 ? 175 ALA A C 1 ATOM 1366 O O . ALA A 1 175 ? 6.280 19.991 6.664 1.00 21.61 ? 175 ALA A O 1 ATOM 1367 C CB . ALA A 1 175 ? 8.145 22.504 6.077 1.00 20.71 ? 175 ALA A CB 1 ATOM 1368 N N . TYR A 1 176 ? 5.301 21.279 5.093 1.00 21.73 ? 176 TYR A N 1 ATOM 1369 C CA . TYR A 1 176 ? 3.927 20.984 5.523 1.00 22.31 ? 176 TYR A CA 1 ATOM 1370 C C . TYR A 1 176 ? 3.001 20.522 4.377 1.00 22.56 ? 176 TYR A C 1 ATOM 1371 O O . TYR A 1 176 ? 1.803 20.319 4.591 1.00 22.48 ? 176 TYR A O 1 ATOM 1372 C CB . TYR A 1 176 ? 3.326 22.215 6.236 1.00 23.07 ? 176 TYR A CB 1 ATOM 1373 C CG . TYR A 1 176 ? 4.273 22.934 7.194 1.00 23.62 ? 176 TYR A CG 1 ATOM 1374 C CD1 . TYR A 1 176 ? 4.674 22.350 8.395 1.00 24.27 ? 176 TYR A CD1 1 ATOM 1375 C CD2 . TYR A 1 176 ? 4.756 24.208 6.898 1.00 24.83 ? 176 TYR A CD2 1 ATOM 1376 C CE1 . TYR A 1 176 ? 5.534 23.012 9.265 1.00 24.73 ? 176 TYR A CE1 1 ATOM 1377 C CE2 . TYR A 1 176 ? 5.613 24.873 7.759 1.00 24.90 ? 176 TYR A CE2 1 ATOM 1378 C CZ . TYR A 1 176 ? 6.001 24.275 8.939 1.00 25.66 ? 176 TYR A CZ 1 ATOM 1379 O OH . TYR A 1 176 ? 6.854 24.950 9.784 1.00 26.74 ? 176 TYR A OH 1 ATOM 1380 N N . ARG A 1 177 ? 3.552 20.349 3.175 1.00 22.96 ? 177 ARG A N 1 ATOM 1381 C CA . ARG A 1 177 ? 2.808 19.853 2.011 1.00 24.93 ? 177 ARG A CA 1 ATOM 1382 C C . ARG A 1 177 ? 3.758 19.170 1.037 1.00 24.68 ? 177 ARG A C 1 ATOM 1383 O O . ARG A 1 177 ? 4.642 19.821 0.464 1.00 24.90 ? 177 ARG A O 1 ATOM 1384 C CB . ARG A 1 177 ? 2.104 20.992 1.266 1.00 27.31 ? 177 ARG A CB 1 ATOM 1385 C CG . ARG A 1 177 ? 1.402 20.533 -0.011 1.00 30.62 ? 177 ARG A CG 1 ATOM 1386 C CD . ARG A 1 177 ? 0.783 21.665 -0.815 1.00 33.81 ? 177 ARG A CD 1 ATOM 1387 N NE . ARG A 1 177 ? 1.748 22.699 -1.185 1.00 36.73 ? 177 ARG A NE 1 ATOM 1388 C CZ . ARG A 1 177 ? 1.447 23.785 -1.897 1.00 40.02 ? 177 ARG A CZ 1 ATOM 1389 N NH1 . ARG A 1 177 ? 0.205 23.986 -2.324 1.00 41.00 ? 177 ARG A NH1 1 ATOM 1390 N NH2 . ARG A 1 177 ? 2.390 24.675 -2.184 1.00 40.98 ? 177 ARG A NH2 1 ATOM 1391 N N . ASP A 1 178 ? 3.557 17.872 0.818 1.00 23.21 ? 178 ASP A N 1 ATOM 1392 C CA . ASP A 1 178 ? 4.371 17.139 -0.142 1.00 22.92 ? 178 ASP A CA 1 ATOM 1393 C C . ASP A 1 178 ? 4.119 17.586 -1.578 1.00 23.61 ? 178 ASP A C 1 ATOM 1394 O O . ASP A 1 178 ? 3.024 18.027 -1.932 1.00 23.28 ? 178 ASP A O 1 ATOM 1395 C CB . ASP A 1 178 ? 4.117 15.628 -0.054 1.00 22.10 ? 178 ASP A CB 1 ATOM 1396 C CG . ASP A 1 178 ? 4.524 15.031 1.284 1.00 21.74 ? 178 ASP A CG 1 ATOM 1397 O OD1 . ASP A 1 178 ? 5.481 15.522 1.915 1.00 21.62 ? 178 ASP A OD1 1 ATOM 1398 O OD2 . ASP A 1 178 ? 3.883 14.043 1.706 1.00 21.26 ? 178 ASP A OD2 1 ATOM 1399 N N . GLU A 1 179 ? 5.152 17.448 -2.399 1.00 24.10 ? 179 GLU A N 1 ATOM 1400 C CA . GLU A 1 179 ? 5.055 17.696 -3.829 1.00 24.76 ? 179 GLU A CA 1 ATOM 1401 C C . GLU A 1 179 ? 6.123 16.889 -4.549 1.00 24.08 ? 179 GLU A C 1 ATOM 1402 O O . GLU A 1 179 ? 7.237 16.730 -4.030 1.00 22.44 ? 179 GLU A O 1 ATOM 1403 C CB . GLU A 1 179 ? 5.243 19.186 -4.123 1.00 26.67 ? 179 GLU A CB 1 ATOM 1404 C CG . GLU A 1 179 ? 4.985 19.572 -5.572 1.00 28.27 ? 179 GLU A CG 1 ATOM 1405 C CD . GLU A 1 179 ? 5.132 21.062 -5.829 1.00 29.93 ? 179 GLU A CD 1 ATOM 1406 O OE1 . GLU A 1 179 ? 4.780 21.868 -4.944 1.00 31.87 ? 179 GLU A OE1 1 ATOM 1407 O OE2 . GLU A 1 179 ? 5.592 21.432 -6.926 1.00 30.75 ? 179 GLU A OE2 1 ATOM 1408 N N . VAL A 1 180 ? 5.794 16.378 -5.734 1.00 24.08 ? 180 VAL A N 1 ATOM 1409 C CA . VAL A 1 180 ? 6.791 15.670 -6.543 1.00 24.42 ? 180 VAL A CA 1 ATOM 1410 C C . VAL A 1 180 ? 8.023 16.556 -6.746 1.00 24.71 ? 180 VAL A C 1 ATOM 1411 O O . VAL A 1 180 ? 7.916 17.787 -6.748 1.00 24.77 ? 180 VAL A O 1 ATOM 1412 C CB . VAL A 1 180 ? 6.263 15.212 -7.927 1.00 25.11 ? 180 VAL A CB 1 ATOM 1413 C CG1 . VAL A 1 180 ? 5.204 14.131 -7.772 1.00 25.38 ? 180 VAL A CG1 1 ATOM 1414 C CG2 . VAL A 1 180 ? 5.733 16.385 -8.748 1.00 25.44 ? 180 VAL A CG2 1 ATOM 1415 N N . PRO A 1 181 ? 9.197 15.930 -6.896 1.00 24.60 ? 181 PRO A N 1 ATOM 1416 C CA . PRO A 1 181 ? 10.412 16.723 -7.074 1.00 25.15 ? 181 PRO A CA 1 ATOM 1417 C C . PRO A 1 181 ? 10.403 17.531 -8.363 1.00 25.42 ? 181 PRO A C 1 ATOM 1418 O O . PRO A 1 181 ? 9.899 17.063 -9.386 1.00 26.06 ? 181 PRO A O 1 ATOM 1419 C CB . PRO A 1 181 ? 11.539 15.682 -7.108 1.00 24.96 ? 181 PRO A CB 1 ATOM 1420 C CG . PRO A 1 181 ? 10.893 14.351 -7.187 1.00 24.91 ? 181 PRO A CG 1 ATOM 1421 C CD . PRO A 1 181 ? 9.457 14.484 -6.809 1.00 24.45 ? 181 PRO A CD 1 ATOM 1422 N N . SER A 1 182 ? 10.961 18.737 -8.295 1.00 25.48 ? 182 SER A N 1 ATOM 1423 C CA . SER A 1 182 ? 11.122 19.586 -9.466 1.00 25.66 ? 182 SER A CA 1 ATOM 1424 C C . SER A 1 182 ? 12.043 18.893 -10.466 1.00 26.02 ? 182 SER A C 1 ATOM 1425 O O . SER A 1 182 ? 12.816 18.001 -10.102 1.00 25.44 ? 182 SER A O 1 ATOM 1426 C CB . SER A 1 182 ? 11.698 20.947 -9.062 1.00 25.45 ? 182 SER A CB 1 ATOM 1427 O OG . SER A 1 182 ? 13.070 20.842 -8.703 1.00 25.20 ? 182 SER A OG 1 ATOM 1428 N N . SER A 1 183 ? 11.953 19.285 -11.732 1.00 27.22 ? 183 SER A N 1 ATOM 1429 C CA . SER A 1 183 ? 12.819 18.710 -12.761 1.00 28.12 ? 183 SER A CA 1 ATOM 1430 C C . SER A 1 183 ? 14.303 18.953 -12.442 1.00 26.77 ? 183 SER A C 1 ATOM 1431 O O . SER A 1 183 ? 15.135 18.074 -12.670 1.00 27.04 ? 183 SER A O 1 ATOM 1432 C CB . SER A 1 183 ? 12.469 19.265 -14.147 1.00 29.49 ? 183 SER A CB 1 ATOM 1433 O OG . SER A 1 183 ? 11.201 18.792 -14.589 1.00 32.37 ? 183 SER A OG 1 ATOM 1434 N N . ALA A 1 184 ? 14.624 20.130 -11.902 1.00 26.18 ? 184 ALA A N 1 ATOM 1435 C CA . ALA A 1 184 ? 16.002 20.439 -11.500 1.00 25.29 ? 184 ALA A CA 1 ATOM 1436 C C . ALA A 1 184 ? 16.476 19.491 -10.405 1.00 24.53 ? 184 ALA A C 1 ATOM 1437 O O . ALA A 1 184 ? 17.622 19.041 -10.421 1.00 24.35 ? 184 ALA A O 1 ATOM 1438 C CB . ALA A 1 184 ? 16.131 21.881 -11.033 1.00 25.60 ? 184 ALA A CB 1 ATOM 1439 N N . THR A 1 185 ? 15.592 19.189 -9.455 1.00 23.16 ? 185 THR A N 1 ATOM 1440 C CA . THR A 1 185 ? 15.922 18.239 -8.392 1.00 22.57 ? 185 THR A CA 1 ATOM 1441 C C . THR A 1 185 ? 16.371 16.899 -8.982 1.00 22.48 ? 185 THR A C 1 ATOM 1442 O O . THR A 1 185 ? 17.438 16.395 -8.641 1.00 22.07 ? 185 THR A O 1 ATOM 1443 C CB . THR A 1 185 ? 14.726 18.015 -7.438 1.00 21.86 ? 185 THR A CB 1 ATOM 1444 O OG1 . THR A 1 185 ? 14.399 19.243 -6.774 1.00 22.24 ? 185 THR A OG1 1 ATOM 1445 C CG2 . THR A 1 185 ? 15.054 16.940 -6.401 1.00 21.25 ? 185 THR A CG2 1 ATOM 1446 N N . ILE A 1 186 ? 15.567 16.329 -9.875 1.00 22.87 ? 186 ILE A N 1 ATOM 1447 C CA . ILE A 1 186 ? 15.904 15.038 -10.488 1.00 23.32 ? 186 ILE A CA 1 ATOM 1448 C C . ILE A 1 186 ? 17.223 15.131 -11.267 1.00 22.84 ? 186 ILE A C 1 ATOM 1449 O O . ILE A 1 186 ? 18.068 14.237 -11.180 1.00 21.55 ? 186 ILE A O 1 ATOM 1450 C CB . ILE A 1 186 ? 14.770 14.534 -11.415 1.00 24.54 ? 186 ILE A CB 1 ATOM 1451 C CG1 . ILE A 1 186 ? 13.489 14.262 -10.609 1.00 25.45 ? 186 ILE A CG1 1 ATOM 1452 C CG2 . ILE A 1 186 ? 15.195 13.279 -12.170 1.00 24.76 ? 186 ILE A CG2 1 ATOM 1453 C CD1 . ILE A 1 186 ? 13.575 13.099 -9.642 1.00 26.06 ? 186 ILE A CD1 1 ATOM 1454 N N . SER A 1 187 ? 17.382 16.222 -12.014 1.00 23.24 ? 187 SER A N 1 ATOM 1455 C CA . SER A 1 187 ? 18.607 16.496 -12.778 1.00 23.42 ? 187 SER A CA 1 ATOM 1456 C C . SER A 1 187 ? 19.862 16.500 -11.890 1.00 22.10 ? 187 SER A C 1 ATOM 1457 O O . SER A 1 187 ? 20.847 15.816 -12.191 1.00 21.35 ? 187 SER A O 1 ATOM 1458 C CB . SER A 1 187 ? 18.465 17.829 -13.525 1.00 24.67 ? 187 SER A CB 1 ATOM 1459 O OG . SER A 1 187 ? 19.649 18.167 -14.226 1.00 26.77 ? 187 SER A OG 1 ATOM 1460 N N . LEU A 1 188 ? 19.810 17.244 -10.786 1.00 21.30 ? 188 LEU A N 1 ATOM 1461 C CA . LEU A 1 188 ? 20.945 17.335 -9.861 1.00 20.38 ? 188 LEU A CA 1 ATOM 1462 C C . LEU A 1 188 ? 21.278 15.973 -9.256 1.00 19.42 ? 188 LEU A C 1 ATOM 1463 O O . LEU A 1 188 ? 22.448 15.594 -9.185 1.00 18.85 ? 188 LEU A O 1 ATOM 1464 C CB . LEU A 1 188 ? 20.680 18.367 -8.753 1.00 20.81 ? 188 LEU A CB 1 ATOM 1465 C CG . LEU A 1 188 ? 20.567 19.816 -9.246 1.00 21.19 ? 188 LEU A CG 1 ATOM 1466 C CD1 . LEU A 1 188 ? 19.947 20.713 -8.188 1.00 21.21 ? 188 LEU A CD1 1 ATOM 1467 C CD2 . LEU A 1 188 ? 21.913 20.368 -9.712 1.00 21.16 ? 188 LEU A CD2 1 ATOM 1468 N N . GLU A 1 189 ? 20.254 15.231 -8.835 1.00 19.24 ? 189 GLU A N 1 ATOM 1469 C CA . GLU A 1 189 ? 20.469 13.898 -8.259 1.00 19.48 ? 189 GLU A CA 1 ATOM 1470 C C . GLU A 1 189 ? 21.227 13.015 -9.226 1.00 20.23 ? 189 GLU A C 1 ATOM 1471 O O . GLU A 1 189 ? 22.185 12.335 -8.862 1.00 20.33 ? 189 GLU A O 1 ATOM 1472 C CB . GLU A 1 189 ? 19.135 13.224 -7.926 1.00 19.67 ? 189 GLU A CB 1 ATOM 1473 C CG . GLU A 1 189 ? 18.351 13.927 -6.832 1.00 19.54 ? 189 GLU A CG 1 ATOM 1474 C CD . GLU A 1 189 ? 16.948 13.380 -6.657 1.00 19.85 ? 189 GLU A CD 1 ATOM 1475 O OE1 . GLU A 1 189 ? 16.521 12.539 -7.474 1.00 20.64 ? 189 GLU A OE1 1 ATOM 1476 O OE2 . GLU A 1 189 ? 16.270 13.809 -5.699 1.00 19.22 ? 189 GLU A OE2 1 ATOM 1477 N N . ASN A 1 190 ? 20.772 13.047 -10.469 1.00 21.31 ? 190 ASN A N 1 ATOM 1478 C CA . ASN A 1 190 ? 21.364 12.274 -11.547 1.00 22.70 ? 190 ASN A CA 1 ATOM 1479 C C . ASN A 1 190 ? 22.782 12.725 -11.920 1.00 23.20 ? 190 ASN A C 1 ATOM 1480 O O . ASN A 1 190 ? 23.575 11.917 -12.410 1.00 24.91 ? 190 ASN A O 1 ATOM 1481 C CB . ASN A 1 190 ? 20.449 12.342 -12.778 1.00 23.12 ? 190 ASN A CB 1 ATOM 1482 C CG . ASN A 1 190 ? 19.166 11.540 -12.603 1.00 23.90 ? 190 ASN A CG 1 ATOM 1483 O OD1 . ASN A 1 190 ? 19.066 10.683 -11.720 1.00 24.82 ? 190 ASN A OD1 1 ATOM 1484 N ND2 . ASN A 1 190 ? 18.176 11.810 -13.453 1.00 24.08 ? 190 ASN A ND2 1 ATOM 1485 N N . SER A 1 191 ? 23.104 13.992 -11.664 1.00 23.57 ? 191 SER A N 1 ATOM 1486 C CA . SER A 1 191 ? 24.370 14.596 -12.116 1.00 23.80 ? 191 SER A CA 1 ATOM 1487 C C . SER A 1 191 ? 25.468 14.717 -11.054 1.00 23.34 ? 191 SER A C 1 ATOM 1488 O O . SER A 1 191 ? 26.563 15.211 -11.347 1.00 22.96 ? 191 SER A O 1 ATOM 1489 C CB . SER A 1 191 ? 24.085 15.991 -12.670 1.00 24.25 ? 191 SER A CB 1 ATOM 1490 O OG . SER A 1 191 ? 23.070 15.940 -13.662 1.00 25.15 ? 191 SER A OG 1 ATOM 1491 N N . TRP A 1 192 ? 25.195 14.280 -9.829 1.00 21.65 ? 192 TRP A N 1 ATOM 1492 C CA . TRP A 1 192 ? 26.139 14.506 -8.740 1.00 21.28 ? 192 TRP A CA 1 ATOM 1493 C C . TRP A 1 192 ? 27.513 13.905 -9.034 1.00 22.22 ? 192 TRP A C 1 ATOM 1494 O O . TRP A 1 192 ? 28.533 14.569 -8.854 1.00 22.61 ? 192 TRP A O 1 ATOM 1495 C CB . TRP A 1 192 ? 25.596 13.951 -7.429 1.00 20.12 ? 192 TRP A CB 1 ATOM 1496 C CG . TRP A 1 192 ? 26.475 14.222 -6.254 1.00 18.56 ? 192 TRP A CG 1 ATOM 1497 C CD1 . TRP A 1 192 ? 26.859 15.439 -5.778 1.00 18.11 ? 192 TRP A CD1 1 ATOM 1498 C CD2 . TRP A 1 192 ? 27.071 13.247 -5.399 1.00 17.95 ? 192 TRP A CD2 1 ATOM 1499 N NE1 . TRP A 1 192 ? 27.660 15.285 -4.673 1.00 17.55 ? 192 TRP A NE1 1 ATOM 1500 C CE2 . TRP A 1 192 ? 27.811 13.947 -4.420 1.00 17.76 ? 192 TRP A CE2 1 ATOM 1501 C CE3 . TRP A 1 192 ? 27.048 11.847 -5.359 1.00 18.17 ? 192 TRP A CE3 1 ATOM 1502 C CZ2 . TRP A 1 192 ? 28.521 13.295 -3.415 1.00 17.38 ? 192 TRP A CZ2 1 ATOM 1503 C CZ3 . TRP A 1 192 ? 27.755 11.197 -4.356 1.00 17.51 ? 192 TRP A CZ3 1 ATOM 1504 C CH2 . TRP A 1 192 ? 28.477 11.919 -3.396 1.00 17.52 ? 192 TRP A CH2 1 ATOM 1505 N N . SER A 1 193 ? 27.530 12.656 -9.491 1.00 23.35 ? 193 SER A N 1 ATOM 1506 C CA . SER A 1 193 ? 28.783 11.974 -9.794 1.00 25.19 ? 193 SER A CA 1 ATOM 1507 C C . SER A 1 193 ? 29.518 12.695 -10.923 1.00 25.00 ? 193 SER A C 1 ATOM 1508 O O . SER A 1 193 ? 30.711 12.977 -10.805 1.00 25.80 ? 193 SER A O 1 ATOM 1509 C CB . SER A 1 193 ? 28.529 10.519 -10.182 1.00 26.01 ? 193 SER A CB 1 ATOM 1510 O OG . SER A 1 193 ? 29.754 9.812 -10.269 1.00 28.45 ? 193 SER A OG 1 ATOM 1511 N N . GLY A 1 194 ? 28.791 13.001 -11.996 1.00 26.02 ? 194 GLY A N 1 ATOM 1512 C CA . GLY A 1 194 ? 29.335 13.776 -13.122 1.00 26.48 ? 194 GLY A CA 1 ATOM 1513 C C . GLY A 1 194 ? 29.949 15.092 -12.674 1.00 26.75 ? 194 GLY A C 1 ATOM 1514 O O . GLY A 1 194 ? 31.101 15.399 -12.999 1.00 26.82 ? 194 GLY A O 1 ATOM 1515 N N . LEU A 1 195 ? 29.179 15.861 -11.907 1.00 26.18 ? 195 LEU A N 1 ATOM 1516 C CA . LEU A 1 195 ? 29.624 17.164 -11.404 1.00 25.51 ? 195 LEU A CA 1 ATOM 1517 C C . LEU A 1 195 ? 30.830 17.056 -10.479 1.00 25.51 ? 195 LEU A C 1 ATOM 1518 O O . LEU A 1 195 ? 31.768 17.855 -10.579 1.00 24.61 ? 195 LEU A O 1 ATOM 1519 C CB . LEU A 1 195 ? 28.486 17.875 -10.661 1.00 25.40 ? 195 LEU A CB 1 ATOM 1520 C CG . LEU A 1 195 ? 27.386 18.543 -11.490 1.00 25.86 ? 195 LEU A CG 1 ATOM 1521 C CD1 . LEU A 1 195 ? 26.200 18.870 -10.588 1.00 26.11 ? 195 LEU A CD1 1 ATOM 1522 C CD2 . LEU A 1 195 ? 27.877 19.799 -12.203 1.00 26.12 ? 195 LEU A CD2 1 ATOM 1523 N N . SER A 1 196 ? 30.800 16.083 -9.570 1.00 24.30 ? 196 SER A N 1 ATOM 1524 C CA . SER A 1 196 ? 31.900 15.881 -8.639 1.00 24.81 ? 196 SER A CA 1 ATOM 1525 C C . SER A 1 196 ? 33.178 15.637 -9.423 1.00 25.98 ? 196 SER A C 1 ATOM 1526 O O . SER A 1 196 ? 34.226 16.182 -9.094 1.00 25.45 ? 196 SER A O 1 ATOM 1527 C CB . SER A 1 196 ? 31.618 14.707 -7.705 1.00 25.00 ? 196 SER A CB 1 ATOM 1528 O OG . SER A 1 196 ? 30.584 15.037 -6.794 1.00 23.32 ? 196 SER A OG 1 ATOM 1529 N N . LYS A 1 197 ? 33.073 14.842 -10.481 1.00 27.25 ? 197 LYS A N 1 ATOM 1530 C CA . LYS A 1 197 ? 34.227 14.529 -11.314 1.00 28.53 ? 197 LYS A CA 1 ATOM 1531 C C . LYS A 1 197 ? 34.753 15.742 -12.089 1.00 28.33 ? 197 LYS A C 1 ATOM 1532 O O . LYS A 1 197 ? 35.958 15.992 -12.091 1.00 27.49 ? 197 LYS A O 1 ATOM 1533 C CB . LYS A 1 197 ? 33.893 13.399 -12.279 1.00 30.24 ? 197 LYS A CB 1 ATOM 1534 C CG . LYS A 1 197 ? 35.011 13.082 -13.258 1.00 32.07 ? 197 LYS A CG 1 ATOM 1535 C CD . LYS A 1 197 ? 34.639 11.909 -14.143 1.00 33.31 ? 197 LYS A CD 1 ATOM 1536 C CE . LYS A 1 197 ? 35.875 11.242 -14.723 1.00 34.75 ? 197 LYS A CE 1 ATOM 1537 N NZ . LYS A 1 197 ? 35.601 9.823 -15.072 1.00 35.72 ? 197 LYS A NZ 1 ATOM 1538 N N . GLN A 1 198 ? 33.865 16.481 -12.753 1.00 28.40 ? 198 GLN A N 1 ATOM 1539 C CA . GLN A 1 198 ? 34.286 17.639 -13.562 1.00 29.02 ? 198 GLN A CA 1 ATOM 1540 C C . GLN A 1 198 ? 34.880 18.782 -12.727 1.00 29.21 ? 198 GLN A C 1 ATOM 1541 O O . GLN A 1 198 ? 35.744 19.524 -13.204 1.00 30.09 ? 198 GLN A O 1 ATOM 1542 C CB . GLN A 1 198 ? 33.131 18.144 -14.441 1.00 29.56 ? 198 GLN A CB 1 ATOM 1543 C CG . GLN A 1 198 ? 32.709 17.157 -15.517 1.00 30.57 ? 198 GLN A CG 1 ATOM 1544 C CD . GLN A 1 198 ? 33.882 16.713 -16.369 1.00 32.18 ? 198 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 198 ? 34.699 17.540 -16.790 1.00 32.96 ? 198 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 198 ? 33.995 15.407 -16.603 1.00 32.40 ? 198 GLN A NE2 1 ATOM 1547 N N . ILE A 1 199 ? 34.427 18.914 -11.483 1.00 28.32 ? 199 ILE A N 1 ATOM 1548 C CA . ILE A 1 199 ? 34.958 19.916 -10.556 1.00 27.51 ? 199 ILE A CA 1 ATOM 1549 C C . ILE A 1 199 ? 36.376 19.552 -10.114 1.00 28.60 ? 199 ILE A C 1 ATOM 1550 O O . ILE A 1 199 ? 37.251 20.420 -10.035 1.00 28.70 ? 199 ILE A O 1 ATOM 1551 C CB . ILE A 1 199 ? 34.019 20.069 -9.341 1.00 26.43 ? 199 ILE A CB 1 ATOM 1552 C CG1 . ILE A 1 199 ? 32.701 20.694 -9.799 1.00 25.48 ? 199 ILE A CG1 1 ATOM 1553 C CG2 . ILE A 1 199 ? 34.648 20.924 -8.246 1.00 26.46 ? 199 ILE A CG2 1 ATOM 1554 C CD1 . ILE A 1 199 ? 31.573 20.533 -8.800 1.00 24.87 ? 199 ILE A CD1 1 ATOM 1555 N N . GLN A 1 200 ? 36.597 18.272 -9.831 1.00 29.14 ? 200 GLN A N 1 ATOM 1556 C CA . GLN A 1 200 ? 37.933 17.779 -9.505 1.00 29.95 ? 200 GLN A CA 1 ATOM 1557 C C . GLN A 1 200 ? 38.887 17.878 -10.699 1.00 30.53 ? 200 GLN A C 1 ATOM 1558 O O . GLN A 1 200 ? 40.032 18.289 -10.533 1.00 31.01 ? 200 GLN A O 1 ATOM 1559 C CB . GLN A 1 200 ? 37.864 16.349 -8.971 1.00 30.24 ? 200 GLN A CB 1 ATOM 1560 C CG . GLN A 1 200 ? 37.498 16.314 -7.500 1.00 30.21 ? 200 GLN A CG 1 ATOM 1561 C CD . GLN A 1 200 ? 37.020 14.955 -7.043 1.00 30.16 ? 200 GLN A CD 1 ATOM 1562 O OE1 . GLN A 1 200 ? 37.807 14.140 -6.570 1.00 29.64 ? 200 GLN A OE1 1 ATOM 1563 N NE2 . GLN A 1 200 ? 35.725 14.704 -7.183 1.00 30.52 ? 200 GLN A NE2 1 ATOM 1564 N N . LEU A 1 201 ? 38.407 17.530 -11.890 1.00 31.07 ? 201 LEU A N 1 ATOM 1565 C CA . LEU A 1 201 ? 39.208 17.654 -13.121 1.00 32.50 ? 201 LEU A CA 1 ATOM 1566 C C . LEU A 1 201 ? 39.524 19.100 -13.491 1.00 33.29 ? 201 LEU A C 1 ATOM 1567 O O . LEU A 1 201 ? 40.491 19.365 -14.212 1.00 33.23 ? 201 LEU A O 1 ATOM 1568 C CB . LEU A 1 201 ? 38.499 16.997 -14.303 1.00 33.05 ? 201 LEU A CB 1 ATOM 1569 C CG . LEU A 1 201 ? 38.520 15.472 -14.369 1.00 33.59 ? 201 LEU A CG 1 ATOM 1570 C CD1 . LEU A 1 201 ? 37.581 15.009 -15.466 1.00 33.99 ? 201 LEU A CD1 1 ATOM 1571 C CD2 . LEU A 1 201 ? 39.926 14.948 -14.624 1.00 34.09 ? 201 LEU A CD2 1 ATOM 1572 N N . ALA A 1 202 ? 38.701 20.028 -13.019 1.00 33.67 ? 202 ALA A N 1 ATOM 1573 C CA . ALA A 1 202 ? 38.904 21.444 -13.291 1.00 34.27 ? 202 ALA A CA 1 ATOM 1574 C C . ALA A 1 202 ? 40.087 22.047 -12.509 1.00 35.69 ? 202 ALA A C 1 ATOM 1575 O O . ALA A 1 202 ? 40.581 23.117 -12.874 1.00 35.92 ? 202 ALA A O 1 ATOM 1576 C CB . ALA A 1 202 ? 37.624 22.209 -13.003 1.00 33.69 ? 202 ALA A CB 1 ATOM 1577 N N . GLN A 1 203 ? 40.532 21.371 -11.443 1.00 38.01 ? 203 GLN A N 1 ATOM 1578 C CA . GLN A 1 203 ? 41.713 21.799 -10.658 1.00 39.63 ? 203 GLN A CA 1 ATOM 1579 C C . GLN A 1 203 ? 42.978 22.039 -11.488 1.00 39.43 ? 203 GLN A C 1 ATOM 1580 O O . GLN A 1 203 ? 43.813 22.862 -11.103 1.00 41.22 ? 203 GLN A O 1 ATOM 1581 C CB . GLN A 1 203 ? 42.052 20.787 -9.548 1.00 41.29 ? 203 GLN A CB 1 ATOM 1582 C CG . GLN A 1 203 ? 41.567 21.188 -8.160 1.00 42.78 ? 203 GLN A CG 1 ATOM 1583 C CD . GLN A 1 203 ? 41.922 20.183 -7.065 1.00 44.00 ? 203 GLN A CD 1 ATOM 1584 O OE1 . GLN A 1 203 ? 42.414 20.565 -6.001 1.00 44.31 ? 203 GLN A OE1 1 ATOM 1585 N NE2 . GLN A 1 203 ? 41.668 18.896 -7.317 1.00 44.51 ? 203 GLN A NE2 1 ATOM 1586 N N . GLY A 1 204 ? 43.129 21.306 -12.594 1.00 37.75 ? 204 GLY A N 1 ATOM 1587 C CA . GLY A 1 204 ? 44.263 21.482 -13.514 1.00 35.95 ? 204 GLY A CA 1 ATOM 1588 C C . GLY A 1 204 ? 43.872 21.794 -14.952 1.00 34.01 ? 204 GLY A C 1 ATOM 1589 O O . GLY A 1 204 ? 44.617 21.491 -15.886 1.00 34.29 ? 204 GLY A O 1 ATOM 1590 N N . ASN A 1 205 ? 42.698 22.395 -15.128 1.00 31.23 ? 205 ASN A N 1 ATOM 1591 C CA . ASN A 1 205 ? 42.206 22.807 -16.441 1.00 30.46 ? 205 ASN A CA 1 ATOM 1592 C C . ASN A 1 205 ? 41.599 24.209 -16.336 1.00 28.00 ? 205 ASN A C 1 ATOM 1593 O O . ASN A 1 205 ? 40.667 24.555 -17.063 1.00 28.23 ? 205 ASN A O 1 ATOM 1594 C CB . ASN A 1 205 ? 41.200 21.768 -16.968 1.00 31.39 ? 205 ASN A CB 1 ATOM 1595 C CG . ASN A 1 205 ? 40.775 22.004 -18.415 1.00 32.19 ? 205 ASN A CG 1 ATOM 1596 O OD1 . ASN A 1 205 ? 39.587 21.939 -18.727 1.00 34.43 ? 205 ASN A OD1 1 ATOM 1597 N ND2 . ASN A 1 205 ? 41.732 22.249 -19.306 1.00 32.93 ? 205 ASN A ND2 1 ATOM 1598 N N . ASN A 1 206 ? 42.155 25.005 -15.419 1.00 26.54 ? 206 ASN A N 1 ATOM 1599 C CA . ASN A 1 206 ? 41.821 26.419 -15.257 1.00 26.23 ? 206 ASN A CA 1 ATOM 1600 C C . ASN A 1 206 ? 40.368 26.664 -14.852 1.00 26.95 ? 206 ASN A C 1 ATOM 1601 O O . ASN A 1 206 ? 39.783 27.687 -15.199 1.00 26.63 ? 206 ASN A O 1 ATOM 1602 C CB . ASN A 1 206 ? 42.174 27.194 -16.535 1.00 25.38 ? 206 ASN A CB 1 ATOM 1603 C CG . ASN A 1 206 ? 43.665 27.197 -16.814 1.00 24.09 ? 206 ASN A CG 1 ATOM 1604 O OD1 . ASN A 1 206 ? 44.459 27.553 -15.946 1.00 24.24 ? 206 ASN A OD1 1 ATOM 1605 N ND2 . ASN A 1 206 ? 44.052 26.805 -18.018 1.00 23.82 ? 206 ASN A ND2 1 ATOM 1606 N N . GLY A 1 207 ? 39.799 25.724 -14.100 1.00 28.31 ? 207 GLY A N 1 ATOM 1607 C CA . GLY A 1 207 ? 38.388 25.790 -13.721 1.00 28.88 ? 207 GLY A CA 1 ATOM 1608 C C . GLY A 1 207 ? 37.419 25.361 -14.815 1.00 30.38 ? 207 GLY A C 1 ATOM 1609 O O . GLY A 1 207 ? 36.206 25.456 -14.631 1.00 31.03 ? 207 GLY A O 1 ATOM 1610 N N . VAL A 1 208 ? 37.944 24.883 -15.945 1.00 30.59 ? 208 VAL A N 1 ATOM 1611 C CA . VAL A 1 208 ? 37.119 24.477 -17.082 1.00 30.70 ? 208 VAL A CA 1 ATOM 1612 C C . VAL A 1 208 ? 36.818 22.985 -16.979 1.00 31.33 ? 208 VAL A C 1 ATOM 1613 O O . VAL A 1 208 ? 37.700 22.181 -16.668 1.00 31.65 ? 208 VAL A O 1 ATOM 1614 C CB . VAL A 1 208 ? 37.816 24.795 -18.428 1.00 30.41 ? 208 VAL A CB 1 ATOM 1615 C CG1 . VAL A 1 208 ? 37.027 24.255 -19.618 1.00 30.48 ? 208 VAL A CG1 1 ATOM 1616 C CG2 . VAL A 1 208 ? 38.020 26.295 -18.566 1.00 30.72 ? 208 VAL A CG2 1 ATOM 1617 N N . PHE A 1 209 ? 35.563 22.629 -17.230 1.00 32.24 ? 209 PHE A N 1 ATOM 1618 C CA . PHE A 1 209 ? 35.147 21.231 -17.296 1.00 33.29 ? 209 PHE A CA 1 ATOM 1619 C C . PHE A 1 209 ? 35.715 20.582 -18.562 1.00 34.98 ? 209 PHE A C 1 ATOM 1620 O O . PHE A 1 209 ? 35.593 21.139 -19.651 1.00 36.01 ? 209 PHE A O 1 ATOM 1621 C CB . PHE A 1 209 ? 33.614 21.134 -17.346 1.00 32.83 ? 209 PHE A CB 1 ATOM 1622 C CG . PHE A 1 209 ? 32.915 21.360 -16.019 1.00 31.98 ? 209 PHE A CG 1 ATOM 1623 C CD1 . PHE A 1 209 ? 33.561 21.921 -14.914 1.00 31.59 ? 209 PHE A CD1 1 ATOM 1624 C CD2 . PHE A 1 209 ? 31.573 21.022 -15.897 1.00 31.93 ? 209 PHE A CD2 1 ATOM 1625 C CE1 . PHE A 1 209 ? 32.877 22.117 -13.720 1.00 31.40 ? 209 PHE A CE1 1 ATOM 1626 C CE2 . PHE A 1 209 ? 30.888 21.218 -14.709 1.00 31.39 ? 209 PHE A CE2 1 ATOM 1627 C CZ . PHE A 1 209 ? 31.539 21.764 -13.620 1.00 31.20 ? 209 PHE A CZ 1 ATOM 1628 N N . ARG A 1 210 ? 36.319 19.404 -18.423 1.00 36.35 ? 210 ARG A N 1 ATOM 1629 C CA . ARG A 1 210 ? 36.750 18.618 -19.590 1.00 38.01 ? 210 ARG A CA 1 ATOM 1630 C C . ARG A 1 210 ? 35.547 18.208 -20.434 1.00 38.50 ? 210 ARG A C 1 ATOM 1631 O O . ARG A 1 210 ? 35.612 18.193 -21.665 1.00 36.95 ? 210 ARG A O 1 ATOM 1632 C CB . ARG A 1 210 ? 37.485 17.346 -19.162 1.00 39.19 ? 210 ARG A CB 1 ATOM 1633 C CG . ARG A 1 210 ? 38.735 17.564 -18.330 1.00 40.14 ? 210 ARG A CG 1 ATOM 1634 C CD . ARG A 1 210 ? 39.938 17.858 -19.205 1.00 40.97 ? 210 ARG A CD 1 ATOM 1635 N NE . ARG A 1 210 ? 41.117 18.173 -18.405 1.00 41.44 ? 210 ARG A NE 1 ATOM 1636 C CZ . ARG A 1 210 ? 42.305 18.494 -18.910 1.00 41.16 ? 210 ARG A CZ 1 ATOM 1637 N NH1 . ARG A 1 210 ? 42.486 18.546 -20.227 1.00 40.66 ? 210 ARG A NH1 1 ATOM 1638 N NH2 . ARG A 1 210 ? 43.318 18.760 -18.093 1.00 40.74 ? 210 ARG A NH2 1 ATOM 1639 N N . THR A 1 211 ? 34.457 17.864 -19.751 1.00 38.42 ? 211 THR A N 1 ATOM 1640 C CA . THR A 1 211 ? 33.204 17.479 -20.385 1.00 39.07 ? 211 THR A CA 1 ATOM 1641 C C . THR A 1 211 ? 32.072 18.266 -19.729 1.00 38.77 ? 211 THR A C 1 ATOM 1642 O O . THR A 1 211 ? 31.884 18.166 -18.516 1.00 38.64 ? 211 THR A O 1 ATOM 1643 C CB . THR A 1 211 ? 32.933 15.975 -20.207 1.00 39.58 ? 211 THR A CB 1 ATOM 1644 O OG1 . THR A 1 211 ? 34.110 15.229 -20.543 1.00 40.75 ? 211 THR A OG1 1 ATOM 1645 C CG2 . THR A 1 211 ? 31.778 15.527 -21.092 1.00 39.74 ? 211 THR A CG2 1 ATOM 1646 N N . PRO A 1 212 ? 31.329 19.066 -20.515 1.00 38.30 ? 212 PRO A N 1 ATOM 1647 C CA . PRO A 1 212 ? 30.236 19.840 -19.924 1.00 37.85 ? 212 PRO A CA 1 ATOM 1648 C C . PRO A 1 212 ? 29.090 18.975 -19.412 1.00 36.70 ? 212 PRO A C 1 ATOM 1649 O O . PRO A 1 212 ? 28.781 17.947 -20.010 1.00 36.51 ? 212 PRO A O 1 ATOM 1650 C CB . PRO A 1 212 ? 29.768 20.725 -21.085 1.00 38.71 ? 212 PRO A CB 1 ATOM 1651 C CG . PRO A 1 212 ? 30.969 20.850 -21.956 1.00 38.68 ? 212 PRO A CG 1 ATOM 1652 C CD . PRO A 1 212 ? 31.601 19.494 -21.899 1.00 38.70 ? 212 PRO A CD 1 ATOM 1653 N N . THR A 1 213 ? 28.489 19.401 -18.302 1.00 35.37 ? 213 THR A N 1 ATOM 1654 C CA . THR A 1 213 ? 27.366 18.701 -17.680 1.00 34.23 ? 213 THR A CA 1 ATOM 1655 C C . THR A 1 213 ? 26.073 19.425 -18.045 1.00 33.68 ? 213 THR A C 1 ATOM 1656 O O . THR A 1 213 ? 25.951 20.629 -17.822 1.00 34.23 ? 213 THR A O 1 ATOM 1657 C CB . THR A 1 213 ? 27.532 18.662 -16.142 1.00 34.19 ? 213 THR A CB 1 ATOM 1658 O OG1 . THR A 1 213 ? 28.694 17.894 -15.798 1.00 34.52 ? 213 THR A OG1 1 ATOM 1659 C CG2 . THR A 1 213 ? 26.305 18.046 -15.459 1.00 33.65 ? 213 THR A CG2 1 ATOM 1660 N N . VAL A 1 214 ? 25.112 18.692 -18.606 1.00 33.22 ? 214 VAL A N 1 ATOM 1661 C CA . VAL A 1 214 ? 23.813 19.264 -18.952 1.00 33.48 ? 214 VAL A CA 1 ATOM 1662 C C . VAL A 1 214 ? 22.855 19.138 -17.764 1.00 32.10 ? 214 VAL A C 1 ATOM 1663 O O . VAL A 1 214 ? 22.684 18.045 -17.229 1.00 32.47 ? 214 VAL A O 1 ATOM 1664 C CB . VAL A 1 214 ? 23.174 18.568 -20.176 1.00 34.63 ? 214 VAL A CB 1 ATOM 1665 C CG1 . VAL A 1 214 ? 21.883 19.272 -20.561 1.00 34.97 ? 214 VAL A CG1 1 ATOM 1666 C CG2 . VAL A 1 214 ? 24.130 18.562 -21.361 1.00 35.67 ? 214 VAL A CG2 1 ATOM 1667 N N . LEU A 1 215 ? 22.237 20.252 -17.366 1.00 31.95 ? 215 LEU A N 1 ATOM 1668 C CA . LEU A 1 215 ? 21.244 20.263 -16.279 1.00 30.75 ? 215 LEU A CA 1 ATOM 1669 C C . LEU A 1 215 ? 19.936 20.955 -16.637 1.00 31.81 ? 215 LEU A C 1 ATOM 1670 O O . LEU A 1 215 ? 19.832 21.641 -17.652 1.00 30.66 ? 215 LEU A O 1 ATOM 1671 C CB . LEU A 1 215 ? 21.789 21.009 -15.070 1.00 29.86 ? 215 LEU A CB 1 ATOM 1672 C CG . LEU A 1 215 ? 23.042 20.502 -14.383 1.00 29.15 ? 215 LEU A CG 1 ATOM 1673 C CD1 . LEU A 1 215 ? 23.359 21.482 -13.269 1.00 29.28 ? 215 LEU A CD1 1 ATOM 1674 C CD2 . LEU A 1 215 ? 22.875 19.088 -13.845 1.00 29.15 ? 215 LEU A CD2 1 ATOM 1675 N N . VAL A 1 216 ? 18.953 20.784 -15.754 1.00 32.66 ? 216 VAL A N 1 ATOM 1676 C CA . VAL A 1 216 ? 17.725 21.568 -15.756 1.00 33.96 ? 216 VAL A CA 1 ATOM 1677 C C . VAL A 1 216 ? 17.783 22.559 -14.592 1.00 35.86 ? 216 VAL A C 1 ATOM 1678 O O . VAL A 1 216 ? 18.083 22.173 -13.461 1.00 34.28 ? 216 VAL A O 1 ATOM 1679 C CB . VAL A 1 216 ? 16.494 20.658 -15.600 1.00 34.00 ? 216 VAL A CB 1 ATOM 1680 C CG1 . VAL A 1 216 ? 15.211 21.476 -15.618 1.00 34.46 ? 216 VAL A CG1 1 ATOM 1681 C CG2 . VAL A 1 216 ? 16.472 19.616 -16.707 1.00 33.44 ? 216 VAL A CG2 1 ATOM 1682 N N . ASP A 1 217 ? 17.500 23.831 -14.871 1.00 38.29 ? 217 ASP A N 1 ATOM 1683 C CA . ASP A 1 217 ? 17.529 24.876 -13.837 1.00 41.39 ? 217 ASP A CA 1 ATOM 1684 C C . ASP A 1 217 ? 16.171 25.010 -13.148 1.00 42.79 ? 217 ASP A C 1 ATOM 1685 O O . ASP A 1 217 ? 15.236 24.267 -13.451 1.00 42.29 ? 217 ASP A O 1 ATOM 1686 C CB . ASP A 1 217 ? 17.989 26.225 -14.425 1.00 42.39 ? 217 ASP A CB 1 ATOM 1687 C CG . ASP A 1 217 ? 17.064 26.752 -15.518 1.00 44.02 ? 217 ASP A CG 1 ATOM 1688 O OD1 . ASP A 1 217 ? 15.825 26.705 -15.352 1.00 43.83 ? 217 ASP A OD1 1 ATOM 1689 O OD2 . ASP A 1 217 ? 17.588 27.229 -16.550 1.00 46.44 ? 217 ASP A OD2 1 ATOM 1690 N N . SER A 1 218 ? 16.066 25.971 -12.234 1.00 47.58 ? 218 SER A N 1 ATOM 1691 C CA . SER A 1 218 ? 14.824 26.231 -11.496 1.00 51.74 ? 218 SER A CA 1 ATOM 1692 C C . SER A 1 218 ? 13.545 26.476 -12.344 1.00 54.85 ? 218 SER A C 1 ATOM 1693 O O . SER A 1 218 ? 12.489 26.749 -11.767 1.00 56.53 ? 218 SER A O 1 ATOM 1694 C CB . SER A 1 218 ? 15.046 27.408 -10.529 1.00 52.28 ? 218 SER A CB 1 ATOM 1695 O OG . SER A 1 218 ? 15.439 28.584 -11.221 1.00 52.51 ? 218 SER A OG 1 ATOM 1696 N N . LYS A 1 219 ? 13.621 26.367 -13.681 1.00 58.01 ? 219 LYS A N 1 ATOM 1697 C CA . LYS A 1 219 ? 12.453 26.620 -14.562 1.00 59.84 ? 219 LYS A CA 1 ATOM 1698 C C . LYS A 1 219 ? 12.260 25.644 -15.742 1.00 59.93 ? 219 LYS A C 1 ATOM 1699 O O . LYS A 1 219 ? 11.577 25.983 -16.714 1.00 60.78 ? 219 LYS A O 1 ATOM 1700 C CB . LYS A 1 219 ? 12.490 28.051 -15.133 1.00 61.94 ? 219 LYS A CB 1 ATOM 1701 C CG . LYS A 1 219 ? 13.575 28.966 -14.585 1.00 63.12 ? 219 LYS A CG 1 ATOM 1702 C CD . LYS A 1 219 ? 13.142 30.422 -14.607 1.00 64.83 ? 219 LYS A CD 1 ATOM 1703 C CE . LYS A 1 219 ? 13.462 31.104 -13.289 1.00 65.97 ? 219 LYS A CE 1 ATOM 1704 N NZ . LYS A 1 219 ? 12.746 32.400 -13.169 1.00 66.75 ? 219 LYS A NZ 1 ATOM 1705 N N . GLY A 1 220 ? 12.836 24.447 -15.667 1.00 58.15 ? 220 GLY A N 1 ATOM 1706 C CA . GLY A 1 220 ? 12.642 23.440 -16.716 1.00 58.14 ? 220 GLY A CA 1 ATOM 1707 C C . GLY A 1 220 ? 13.524 23.586 -17.947 1.00 58.28 ? 220 GLY A C 1 ATOM 1708 O O . GLY A 1 220 ? 13.385 22.814 -18.899 1.00 59.65 ? 220 GLY A O 1 ATOM 1709 N N . ASN A 1 221 ? 14.444 24.551 -17.928 1.00 58.60 ? 221 ASN A N 1 ATOM 1710 C CA . ASN A 1 221 ? 15.259 24.863 -19.106 1.00 58.58 ? 221 ASN A CA 1 ATOM 1711 C C . ASN A 1 221 ? 16.641 24.180 -19.075 1.00 57.11 ? 221 ASN A C 1 ATOM 1712 O O . ASN A 1 221 ? 17.357 24.265 -18.076 1.00 58.00 ? 221 ASN A O 1 ATOM 1713 C CB . ASN A 1 221 ? 15.347 26.386 -19.272 1.00 59.40 ? 221 ASN A CB 1 ATOM 1714 C CG . ASN A 1 221 ? 14.001 27.001 -19.649 1.00 59.85 ? 221 ASN A CG 1 ATOM 1715 O OD1 . ASN A 1 221 ? 13.432 26.666 -20.689 1.00 60.26 ? 221 ASN A OD1 1 ATOM 1716 N ND2 . ASN A 1 221 ? 13.482 27.892 -18.804 1.00 59.30 ? 221 ASN A ND2 1 ATOM 1717 N N . ARG A 1 222 ? 16.988 23.505 -20.179 1.00 54.82 ? 222 ARG A N 1 ATOM 1718 C CA . ARG A 1 222 ? 18.133 22.565 -20.253 1.00 52.67 ? 222 ARG A CA 1 ATOM 1719 C C . ARG A 1 222 ? 19.465 23.268 -20.510 1.00 51.68 ? 222 ARG A C 1 ATOM 1720 O O . ARG A 1 222 ? 19.754 23.665 -21.643 1.00 49.23 ? 222 ARG A O 1 ATOM 1721 C CB . ARG A 1 222 ? 17.882 21.490 -21.337 1.00 51.48 ? 222 ARG A CB 1 ATOM 1722 C CG . ARG A 1 222 ? 19.109 20.707 -21.851 1.00 50.86 ? 222 ARG A CG 1 ATOM 1723 C CD . ARG A 1 222 ? 19.350 20.918 -23.351 1.00 49.92 ? 222 ARG A CD 1 ATOM 1724 N NE . ARG A 1 222 ? 20.736 20.758 -23.825 1.00 48.57 ? 222 ARG A NE 1 ATOM 1725 C CZ . ARG A 1 222 ? 21.600 21.755 -24.051 1.00 48.20 ? 222 ARG A CZ 1 ATOM 1726 N NH1 . ARG A 1 222 ? 22.818 21.482 -24.506 1.00 47.90 ? 222 ARG A NH1 1 ATOM 1727 N NH2 . ARG A 1 222 ? 21.274 23.026 -23.816 1.00 47.43 ? 222 ARG A NH2 1 ATOM 1728 N N . VAL A 1 223 ? 20.286 23.381 -19.465 1.00 50.89 ? 223 VAL A N 1 ATOM 1729 C CA . VAL A 1 223 ? 21.514 24.177 -19.537 1.00 49.65 ? 223 VAL A CA 1 ATOM 1730 C C . VAL A 1 223 ? 22.798 23.367 -19.411 1.00 47.57 ? 223 VAL A C 1 ATOM 1731 O O . VAL A 1 223 ? 22.805 22.264 -18.870 1.00 47.45 ? 223 VAL A O 1 ATOM 1732 C CB . VAL A 1 223 ? 21.495 25.319 -18.503 1.00 49.41 ? 223 VAL A CB 1 ATOM 1733 C CG1 . VAL A 1 223 ? 20.182 26.075 -18.629 1.00 50.20 ? 223 VAL A CG1 1 ATOM 1734 C CG2 . VAL A 1 223 ? 21.685 24.806 -17.078 1.00 50.00 ? 223 VAL A CG2 1 ATOM 1735 N N . GLN A 1 224 ? 23.880 23.947 -19.924 1.00 44.90 ? 224 GLN A N 1 ATOM 1736 C CA . GLN A 1 224 ? 25.178 23.299 -19.963 1.00 42.94 ? 224 GLN A CA 1 ATOM 1737 C C . GLN A 1 224 ? 26.088 23.988 -18.964 1.00 39.32 ? 224 GLN A C 1 ATOM 1738 O O . GLN A 1 224 ? 26.267 25.203 -19.015 1.00 38.16 ? 224 GLN A O 1 ATOM 1739 C CB . GLN A 1 224 ? 25.787 23.384 -21.365 1.00 44.20 ? 224 GLN A CB 1 ATOM 1740 C CG . GLN A 1 224 ? 25.142 22.448 -22.381 1.00 46.22 ? 224 GLN A CG 1 ATOM 1741 C CD . GLN A 1 224 ? 26.151 21.749 -23.284 1.00 47.45 ? 224 GLN A CD 1 ATOM 1742 O OE1 . GLN A 1 224 ? 27.189 22.316 -23.632 1.00 48.59 ? 224 GLN A OE1 1 ATOM 1743 N NE2 . GLN A 1 224 ? 25.845 20.511 -23.673 1.00 48.35 ? 224 GLN A NE2 1 ATOM 1744 N N . ILE A 1 225 ? 26.637 23.199 -18.045 1.00 36.04 ? 225 ILE A N 1 ATOM 1745 C CA . ILE A 1 225 ? 27.604 23.677 -17.066 1.00 33.74 ? 225 ILE A CA 1 ATOM 1746 C C . ILE A 1 225 ? 28.998 23.347 -17.602 1.00 33.43 ? 225 ILE A C 1 ATOM 1747 O O . ILE A 1 225 ? 29.317 22.182 -17.843 1.00 32.94 ? 225 ILE A O 1 ATOM 1748 C CB . ILE A 1 225 ? 27.371 23.017 -15.690 1.00 32.04 ? 225 ILE A CB 1 ATOM 1749 C CG1 . ILE A 1 225 ? 25.881 23.073 -15.307 1.00 31.27 ? 225 ILE A CG1 1 ATOM 1750 C CG2 . ILE A 1 225 ? 28.226 23.673 -14.614 1.00 31.90 ? 225 ILE A CG2 1 ATOM 1751 C CD1 . ILE A 1 225 ? 25.263 24.459 -15.319 1.00 31.14 ? 225 ILE A CD1 1 ATOM 1752 N N . THR A 1 226 ? 29.810 24.385 -17.797 1.00 34.07 ? 226 THR A N 1 ATOM 1753 C CA . THR A 1 226 ? 31.100 24.268 -18.488 1.00 34.16 ? 226 THR A CA 1 ATOM 1754 C C . THR A 1 226 ? 32.301 24.628 -17.615 1.00 34.07 ? 226 THR A C 1 ATOM 1755 O O . THR A 1 226 ? 33.434 24.277 -17.951 1.00 34.50 ? 226 THR A O 1 ATOM 1756 C CB . THR A 1 226 ? 31.152 25.178 -19.738 1.00 34.34 ? 226 THR A CB 1 ATOM 1757 O OG1 . THR A 1 226 ? 31.069 26.554 -19.346 1.00 34.84 ? 226 THR A OG1 1 ATOM 1758 C CG2 . THR A 1 226 ? 30.012 24.854 -20.705 1.00 34.59 ? 226 THR A CG2 1 ATOM 1759 N N . ASN A 1 227 ? 32.067 25.341 -16.515 1.00 33.40 ? 227 ASN A N 1 ATOM 1760 C CA . ASN A 1 227 ? 33.157 25.764 -15.641 1.00 33.51 ? 227 ASN A CA 1 ATOM 1761 C C . ASN A 1 227 ? 32.713 26.031 -14.206 1.00 32.06 ? 227 ASN A C 1 ATOM 1762 O O . ASN A 1 227 ? 31.513 26.053 -13.907 1.00 31.04 ? 227 ASN A O 1 ATOM 1763 C CB . ASN A 1 227 ? 33.908 26.974 -16.242 1.00 35.13 ? 227 ASN A CB 1 ATOM 1764 C CG . ASN A 1 227 ? 33.084 28.256 -16.261 1.00 37.01 ? 227 ASN A CG 1 ATOM 1765 O OD1 . ASN A 1 227 ? 32.970 28.940 -15.246 1.00 38.09 ? 227 ASN A OD1 1 ATOM 1766 N ND2 . ASN A 1 227 ? 32.530 28.599 -17.425 1.00 39.74 ? 227 ASN A ND2 1 ATOM 1767 N N . VAL A 1 228 ? 33.695 26.220 -13.326 1.00 30.40 ? 228 VAL A N 1 ATOM 1768 C CA . VAL A 1 228 ? 33.450 26.390 -11.888 1.00 30.08 ? 228 VAL A CA 1 ATOM 1769 C C . VAL A 1 228 ? 32.819 27.718 -11.476 1.00 30.16 ? 228 VAL A C 1 ATOM 1770 O O . VAL A 1 228 ? 32.463 27.883 -10.308 1.00 30.38 ? 228 VAL A O 1 ATOM 1771 C CB . VAL A 1 228 ? 34.737 26.209 -11.047 1.00 30.17 ? 228 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 228 ? 35.257 24.784 -11.165 1.00 29.80 ? 228 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 228 ? 35.803 27.240 -11.423 1.00 30.32 ? 228 VAL A CG2 1 ATOM 1774 N N . THR A 1 229 ? 32.683 28.668 -12.398 1.00 30.66 ? 229 THR A N 1 ATOM 1775 C CA . THR A 1 229 ? 32.027 29.937 -12.057 1.00 31.09 ? 229 THR A CA 1 ATOM 1776 C C . THR A 1 229 ? 30.509 29.802 -12.107 1.00 30.38 ? 229 THR A C 1 ATOM 1777 O O . THR A 1 229 ? 29.790 30.739 -11.768 1.00 30.57 ? 229 THR A O 1 ATOM 1778 C CB . THR A 1 229 ? 32.481 31.115 -12.948 1.00 31.57 ? 229 THR A CB 1 ATOM 1779 O OG1 . THR A 1 229 ? 31.973 30.963 -14.281 1.00 33.09 ? 229 THR A OG1 1 ATOM 1780 C CG2 . THR A 1 229 ? 34.004 31.211 -12.969 1.00 31.68 ? 229 THR A CG2 1 ATOM 1781 N N . SER A 1 230 ? 30.031 28.635 -12.528 1.00 29.69 ? 230 SER A N 1 ATOM 1782 C CA . SER A 1 230 ? 28.609 28.349 -12.533 1.00 29.63 ? 230 SER A CA 1 ATOM 1783 C C . SER A 1 230 ? 28.031 28.353 -11.116 1.00 29.31 ? 230 SER A C 1 ATOM 1784 O O . SER A 1 230 ? 28.663 27.895 -10.166 1.00 28.21 ? 230 SER A O 1 ATOM 1785 C CB . SER A 1 230 ? 28.342 26.996 -13.187 1.00 29.60 ? 230 SER A CB 1 ATOM 1786 O OG . SER A 1 230 ? 27.037 26.538 -12.889 1.00 31.11 ? 230 SER A OG 1 ATOM 1787 N N . ASN A 1 231 ? 26.833 28.916 -11.005 1.00 29.97 ? 231 ASN A N 1 ATOM 1788 C CA . ASN A 1 231 ? 25.972 28.808 -9.826 1.00 30.73 ? 231 ASN A CA 1 ATOM 1789 C C . ASN A 1 231 ? 25.990 27.450 -9.143 1.00 27.85 ? 231 ASN A C 1 ATOM 1790 O O . ASN A 1 231 ? 26.075 27.349 -7.922 1.00 26.94 ? 231 ASN A O 1 ATOM 1791 C CB . ASN A 1 231 ? 24.527 29.039 -10.270 1.00 33.33 ? 231 ASN A CB 1 ATOM 1792 C CG . ASN A 1 231 ? 23.950 30.334 -9.766 1.00 36.76 ? 231 ASN A CG 1 ATOM 1793 O OD1 . ASN A 1 231 ? 24.671 31.257 -9.377 1.00 39.39 ? 231 ASN A OD1 1 ATOM 1794 N ND2 . ASN A 1 231 ? 22.622 30.413 -9.775 1.00 38.49 ? 231 ASN A ND2 1 ATOM 1795 N N . VAL A 1 232 ? 25.865 26.413 -9.957 1.00 27.09 ? 232 VAL A N 1 ATOM 1796 C CA . VAL A 1 232 ? 25.768 25.045 -9.461 1.00 25.95 ? 232 VAL A CA 1 ATOM 1797 C C . VAL A 1 232 ? 27.003 24.723 -8.609 1.00 24.46 ? 232 VAL A C 1 ATOM 1798 O O . VAL A 1 232 ? 26.909 24.043 -7.590 1.00 23.70 ? 232 VAL A O 1 ATOM 1799 C CB . VAL A 1 232 ? 25.602 24.038 -10.623 1.00 26.78 ? 232 VAL A CB 1 ATOM 1800 C CG1 . VAL A 1 232 ? 25.344 22.637 -10.093 1.00 27.10 ? 232 VAL A CG1 1 ATOM 1801 C CG2 . VAL A 1 232 ? 24.443 24.441 -11.526 1.00 27.15 ? 232 VAL A CG2 1 ATOM 1802 N N . VAL A 1 233 ? 28.155 25.258 -9.012 1.00 23.47 ? 233 VAL A N 1 ATOM 1803 C CA . VAL A 1 233 ? 29.419 25.007 -8.316 1.00 22.86 ? 233 VAL A CA 1 ATOM 1804 C C . VAL A 1 233 ? 29.661 25.990 -7.159 1.00 23.02 ? 233 VAL A C 1 ATOM 1805 O O . VAL A 1 233 ? 30.130 25.590 -6.096 1.00 23.30 ? 233 VAL A O 1 ATOM 1806 C CB . VAL A 1 233 ? 30.610 25.054 -9.305 1.00 22.53 ? 233 VAL A CB 1 ATOM 1807 C CG1 . VAL A 1 233 ? 31.908 24.693 -8.604 1.00 22.46 ? 233 VAL A CG1 1 ATOM 1808 C CG2 . VAL A 1 233 ? 30.367 24.108 -10.476 1.00 22.45 ? 233 VAL A CG2 1 ATOM 1809 N N . THR A 1 234 ? 29.351 27.269 -7.367 1.00 23.73 ? 234 THR A N 1 ATOM 1810 C CA . THR A 1 234 ? 29.641 28.302 -6.364 1.00 24.91 ? 234 THR A CA 1 ATOM 1811 C C . THR A 1 234 ? 28.649 28.327 -5.204 1.00 25.35 ? 234 THR A C 1 ATOM 1812 O O . THR A 1 234 ? 29.011 28.683 -4.082 1.00 26.50 ? 234 THR A O 1 ATOM 1813 C CB . THR A 1 234 ? 29.689 29.719 -6.987 1.00 25.21 ? 234 THR A CB 1 ATOM 1814 O OG1 . THR A 1 234 ? 28.459 30.006 -7.666 1.00 25.69 ? 234 THR A OG1 1 ATOM 1815 C CG2 . THR A 1 234 ? 30.844 29.832 -7.965 1.00 25.16 ? 234 THR A CG2 1 ATOM 1816 N N . SER A 1 235 ? 27.410 27.929 -5.473 1.00 26.37 ? 235 SER A N 1 ATOM 1817 C CA . SER A 1 235 ? 26.309 28.147 -4.536 1.00 27.30 ? 235 SER A CA 1 ATOM 1818 C C . SER A 1 235 ? 25.636 26.847 -4.082 1.00 26.64 ? 235 SER A C 1 ATOM 1819 O O . SER A 1 235 ? 25.287 26.697 -2.908 1.00 28.59 ? 235 SER A O 1 ATOM 1820 C CB . SER A 1 235 ? 25.275 29.071 -5.190 1.00 28.69 ? 235 SER A CB 1 ATOM 1821 O OG . SER A 1 235 ? 25.877 30.290 -5.604 1.00 31.44 ? 235 SER A OG 1 ATOM 1822 N N . ASN A 1 236 ? 25.497 25.902 -5.004 1.00 23.96 ? 236 ASN A N 1 ATOM 1823 C CA . ASN A 1 236 ? 24.582 24.773 -4.853 1.00 22.62 ? 236 ASN A CA 1 ATOM 1824 C C . ASN A 1 236 ? 25.232 23.503 -4.276 1.00 21.37 ? 236 ASN A C 1 ATOM 1825 O O . ASN A 1 236 ? 24.912 23.086 -3.157 1.00 20.65 ? 236 ASN A O 1 ATOM 1826 C CB . ASN A 1 236 ? 23.948 24.511 -6.225 1.00 22.17 ? 236 ASN A CB 1 ATOM 1827 C CG . ASN A 1 236 ? 22.721 23.624 -6.166 1.00 22.23 ? 236 ASN A CG 1 ATOM 1828 O OD1 . ASN A 1 236 ? 22.427 22.998 -5.153 1.00 22.32 ? 236 ASN A OD1 1 ATOM 1829 N ND2 . ASN A 1 236 ? 22.005 23.555 -7.277 1.00 22.78 ? 236 ASN A ND2 1 ATOM 1830 N N . ILE A 1 237 ? 26.146 22.889 -5.026 1.00 20.65 ? 237 ILE A N 1 ATOM 1831 C CA . ILE A 1 237 ? 26.740 21.613 -4.607 1.00 20.08 ? 237 ILE A CA 1 ATOM 1832 C C . ILE A 1 237 ? 27.513 21.795 -3.296 1.00 20.02 ? 237 ILE A C 1 ATOM 1833 O O . ILE A 1 237 ? 28.234 22.775 -3.126 1.00 20.32 ? 237 ILE A O 1 ATOM 1834 C CB . ILE A 1 237 ? 27.608 20.985 -5.728 1.00 19.51 ? 237 ILE A CB 1 ATOM 1835 C CG1 . ILE A 1 237 ? 27.944 19.522 -5.419 1.00 19.56 ? 237 ILE A CG1 1 ATOM 1836 C CG2 . ILE A 1 237 ? 28.890 21.782 -5.959 1.00 19.52 ? 237 ILE A CG2 1 ATOM 1837 C CD1 . ILE A 1 237 ? 28.547 18.763 -6.585 1.00 19.54 ? 237 ILE A CD1 1 ATOM 1838 N N . GLN A 1 238 ? 27.332 20.861 -2.360 1.00 19.65 ? 238 GLN A N 1 ATOM 1839 C CA . GLN A 1 238 ? 27.902 20.981 -1.014 1.00 19.74 ? 238 GLN A CA 1 ATOM 1840 C C . GLN A 1 238 ? 28.916 19.900 -0.650 1.00 18.99 ? 238 GLN A C 1 ATOM 1841 O O . GLN A 1 238 ? 29.624 20.031 0.354 1.00 19.27 ? 238 GLN A O 1 ATOM 1842 C CB . GLN A 1 238 ? 26.778 20.975 0.022 1.00 20.55 ? 238 GLN A CB 1 ATOM 1843 C CG . GLN A 1 238 ? 25.764 22.091 -0.158 1.00 21.37 ? 238 GLN A CG 1 ATOM 1844 C CD . GLN A 1 238 ? 26.364 23.460 0.099 1.00 22.82 ? 238 GLN A CD 1 ATOM 1845 O OE1 . GLN A 1 238 ? 26.967 23.688 1.149 1.00 25.06 ? 238 GLN A OE1 1 ATOM 1846 N NE2 . GLN A 1 238 ? 26.205 24.378 -0.849 1.00 23.23 ? 238 GLN A NE2 1 ATOM 1847 N N . LEU A 1 239 ? 28.974 18.837 -1.445 1.00 18.43 ? 239 LEU A N 1 ATOM 1848 C CA . LEU A 1 239 ? 29.864 17.706 -1.199 1.00 18.83 ? 239 LEU A CA 1 ATOM 1849 C C . LEU A 1 239 ? 30.325 17.150 -2.546 1.00 19.28 ? 239 LEU A C 1 ATOM 1850 O O . LEU A 1 239 ? 29.561 17.142 -3.515 1.00 18.94 ? 239 LEU A O 1 ATOM 1851 C CB . LEU A 1 239 ? 29.132 16.609 -0.419 1.00 18.68 ? 239 LEU A CB 1 ATOM 1852 C CG . LEU A 1 239 ? 28.497 16.913 0.944 1.00 18.81 ? 239 LEU A CG 1 ATOM 1853 C CD1 . LEU A 1 239 ? 27.450 15.858 1.274 1.00 18.66 ? 239 LEU A CD1 1 ATOM 1854 C CD2 . LEU A 1 239 ? 29.546 16.964 2.043 1.00 18.98 ? 239 LEU A CD2 1 ATOM 1855 N N . LEU A 1 240 ? 31.571 16.687 -2.617 1.00 20.44 ? 240 LEU A N 1 ATOM 1856 C CA . LEU A 1 240 ? 32.089 16.100 -3.848 1.00 21.96 ? 240 LEU A CA 1 ATOM 1857 C C . LEU A 1 240 ? 32.417 14.634 -3.653 1.00 22.43 ? 240 LEU A C 1 ATOM 1858 O O . LEU A 1 240 ? 33.143 14.273 -2.732 1.00 22.80 ? 240 LEU A O 1 ATOM 1859 C CB . LEU A 1 240 ? 33.352 16.829 -4.328 1.00 22.31 ? 240 LEU A CB 1 ATOM 1860 C CG . LEU A 1 240 ? 33.239 18.337 -4.539 1.00 22.83 ? 240 LEU A CG 1 ATOM 1861 C CD1 . LEU A 1 240 ? 34.611 18.925 -4.838 1.00 23.10 ? 240 LEU A CD1 1 ATOM 1862 C CD2 . LEU A 1 240 ? 32.246 18.676 -5.639 1.00 23.07 ? 240 LEU A CD2 1 ATOM 1863 N N . LEU A 1 241 ? 31.869 13.797 -4.526 1.00 23.07 ? 241 LEU A N 1 ATOM 1864 C CA . LEU A 1 241 ? 32.237 12.392 -4.591 1.00 24.39 ? 241 LEU A CA 1 ATOM 1865 C C . LEU A 1 241 ? 33.669 12.317 -5.078 1.00 25.57 ? 241 LEU A C 1 ATOM 1866 O O . LEU A 1 241 ? 33.987 12.891 -6.114 1.00 25.83 ? 241 LEU A O 1 ATOM 1867 C CB . LEU A 1 241 ? 31.330 11.657 -5.577 1.00 24.33 ? 241 LEU A CB 1 ATOM 1868 C CG . LEU A 1 241 ? 31.506 10.147 -5.729 1.00 24.65 ? 241 LEU A CG 1 ATOM 1869 C CD1 . LEU A 1 241 ? 31.296 9.441 -4.398 1.00 25.18 ? 241 LEU A CD1 1 ATOM 1870 C CD2 . LEU A 1 241 ? 30.534 9.633 -6.781 1.00 24.96 ? 241 LEU A CD2 1 ATOM 1871 N N . ASN A 1 242 ? 34.530 11.631 -4.335 1.00 26.96 ? 242 ASN A N 1 ATOM 1872 C CA . ASN A 1 242 ? 35.930 11.516 -4.734 1.00 28.10 ? 242 ASN A CA 1 ATOM 1873 C C . ASN A 1 242 ? 36.040 10.784 -6.059 1.00 30.08 ? 242 ASN A C 1 ATOM 1874 O O . ASN A 1 242 ? 35.407 9.744 -6.261 1.00 30.04 ? 242 ASN A O 1 ATOM 1875 C CB . ASN A 1 242 ? 36.755 10.791 -3.672 1.00 28.10 ? 242 ASN A CB 1 ATOM 1876 C CG . ASN A 1 242 ? 38.230 11.147 -3.732 1.00 28.33 ? 242 ASN A CG 1 ATOM 1877 O OD1 . ASN A 1 242 ? 38.940 10.756 -4.662 1.00 29.87 ? 242 ASN A OD1 1 ATOM 1878 N ND2 . ASN A 1 242 ? 38.698 11.892 -2.738 1.00 28.02 ? 242 ASN A ND2 1 ATOM 1879 N N . THR A 1 243 ? 36.846 11.336 -6.958 1.00 32.28 ? 243 THR A N 1 ATOM 1880 C CA . THR A 1 243 ? 37.020 10.766 -8.288 1.00 34.87 ? 243 THR A CA 1 ATOM 1881 C C . THR A 1 243 ? 37.610 9.345 -8.240 1.00 37.29 ? 243 THR A C 1 ATOM 1882 O O . THR A 1 243 ? 37.443 8.570 -9.183 1.00 37.28 ? 243 THR A O 1 ATOM 1883 C CB . THR A 1 243 ? 37.867 11.702 -9.182 1.00 35.74 ? 243 THR A CB 1 ATOM 1884 O OG1 . THR A 1 243 ? 37.848 11.229 -10.533 1.00 36.69 ? 243 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 243 ? 39.307 11.797 -8.683 1.00 35.64 ? 243 THR A CG2 1 ATOM 1886 N N . LYS A 1 244 ? 38.273 8.999 -7.137 1.00 40.45 ? 244 LYS A N 1 ATOM 1887 C CA . LYS A 1 244 ? 38.715 7.620 -6.909 1.00 44.34 ? 244 LYS A CA 1 ATOM 1888 C C . LYS A 1 244 ? 37.536 6.631 -6.775 1.00 46.30 ? 244 LYS A C 1 ATOM 1889 O O . LYS A 1 244 ? 37.717 5.422 -6.948 1.00 47.29 ? 244 LYS A O 1 ATOM 1890 C CB . LYS A 1 244 ? 39.660 7.553 -5.697 1.00 46.14 ? 244 LYS A CB 1 ATOM 1891 C CG . LYS A 1 244 ? 40.998 8.235 -5.982 1.00 47.68 ? 244 LYS A CG 1 ATOM 1892 C CD . LYS A 1 244 ? 41.839 8.525 -4.745 1.00 48.79 ? 244 LYS A CD 1 ATOM 1893 C CE . LYS A 1 244 ? 42.669 7.322 -4.318 1.00 49.63 ? 244 LYS A CE 1 ATOM 1894 N NZ . LYS A 1 244 ? 43.392 7.559 -3.036 1.00 49.85 ? 244 LYS A NZ 1 ATOM 1895 N N . ASN A 1 245 ? 36.338 7.148 -6.490 1.00 46.88 ? 245 ASN A N 1 ATOM 1896 C CA . ASN A 1 245 ? 35.116 6.334 -6.416 1.00 47.31 ? 245 ASN A CA 1 ATOM 1897 C C . ASN A 1 245 ? 34.155 6.515 -7.608 1.00 47.82 ? 245 ASN A C 1 ATOM 1898 O O . ASN A 1 245 ? 32.983 6.138 -7.530 1.00 48.20 ? 245 ASN A O 1 ATOM 1899 C CB . ASN A 1 245 ? 34.397 6.621 -5.090 1.00 47.20 ? 245 ASN A CB 1 ATOM 1900 C CG . ASN A 1 245 ? 35.147 6.061 -3.893 1.00 47.32 ? 245 ASN A CG 1 ATOM 1901 O OD1 . ASN A 1 245 ? 35.645 4.935 -3.935 1.00 48.09 ? 245 ASN A OD1 1 ATOM 1902 N ND2 . ASN A 1 245 ? 35.230 6.838 -2.819 1.00 46.31 ? 245 ASN A ND2 1 ATOM 1903 N N . ILE A 1 246 ? 34.660 7.069 -8.710 1.00 47.85 ? 246 ILE A N 1 ATOM 1904 C CA . ILE A 1 246 ? 33.860 7.290 -9.919 1.00 48.43 ? 246 ILE A CA 1 ATOM 1905 C C . ILE A 1 246 ? 34.420 6.446 -11.065 1.00 49.49 ? 246 ILE A C 1 ATOM 1906 O O . ILE A 1 246 ? 33.677 5.943 -11.911 1.00 49.78 ? 246 ILE A O 1 ATOM 1907 C CB . ILE A 1 246 ? 33.834 8.790 -10.308 1.00 47.64 ? 246 ILE A CB 1 ATOM 1908 C CG1 . ILE A 1 246 ? 33.265 9.621 -9.149 1.00 47.29 ? 246 ILE A CG1 1 ATOM 1909 C CG2 . ILE A 1 246 ? 33.000 9.016 -11.564 1.00 47.53 ? 246 ILE A CG2 1 ATOM 1910 C CD1 . ILE A 1 246 ? 33.260 11.121 -9.374 1.00 46.44 ? 246 ILE A CD1 1 ATOM 1911 O OXT . ILE A 1 246 ? 35.630 6.239 -11.171 1.00 50.77 ? 246 ILE A OXT 1 HETATM 1912 C C1 . NAG B 2 . ? 31.743 29.801 -17.597 1.00 47.95 ? 301 NAG A C1 1 HETATM 1913 C C2 . NAG B 2 . ? 31.549 30.286 -19.037 1.00 51.90 ? 301 NAG A C2 1 HETATM 1914 C C3 . NAG B 2 . ? 30.594 31.481 -19.154 1.00 52.95 ? 301 NAG A C3 1 HETATM 1915 C C4 . NAG B 2 . ? 29.420 31.415 -18.184 1.00 53.03 ? 301 NAG A C4 1 HETATM 1916 C C5 . NAG B 2 . ? 29.916 31.041 -16.792 1.00 52.18 ? 301 NAG A C5 1 HETATM 1917 C C6 . NAG B 2 . ? 28.792 30.972 -15.764 1.00 52.76 ? 301 NAG A C6 1 HETATM 1918 C C7 . NAG B 2 . ? 33.732 29.789 -20.055 1.00 54.03 ? 301 NAG A C7 1 HETATM 1919 C C8 . NAG B 2 . ? 35.051 30.344 -20.514 1.00 54.16 ? 301 NAG A C8 1 HETATM 1920 N N2 . NAG B 2 . ? 32.860 30.663 -19.542 1.00 53.00 ? 301 NAG A N2 1 HETATM 1921 O O3 . NAG B 2 . ? 30.105 31.588 -20.476 1.00 53.68 ? 301 NAG A O3 1 HETATM 1922 O O4 . NAG B 2 . ? 28.780 32.672 -18.162 1.00 54.61 ? 301 NAG A O4 1 HETATM 1923 O O5 . NAG B 2 . ? 30.529 29.774 -16.877 1.00 49.72 ? 301 NAG A O5 1 HETATM 1924 O O6 . NAG B 2 . ? 27.839 30.012 -16.164 1.00 53.06 ? 301 NAG A O6 1 HETATM 1925 O O7 . NAG B 2 . ? 33.510 28.581 -20.162 1.00 54.31 ? 301 NAG A O7 1 HETATM 1926 C C1 . DA2 C 3 . ? 21.161 6.443 -2.560 1.00 22.97 ? 302 DA2 A C1 1 HETATM 1927 C C2 . DA2 C 3 . ? 22.087 8.580 -2.645 1.00 22.52 ? 302 DA2 A C2 1 HETATM 1928 N N . DA2 C 3 . ? 23.575 1.736 -4.359 1.00 33.27 ? 302 DA2 A N 1 HETATM 1929 C CA . DA2 C 3 . ? 23.499 2.981 -3.693 1.00 30.97 ? 302 DA2 A CA 1 HETATM 1930 C CB . DA2 C 3 . ? 22.658 3.994 -4.441 1.00 30.92 ? 302 DA2 A CB 1 HETATM 1931 C CG . DA2 C 3 . ? 23.293 4.658 -5.581 1.00 28.56 ? 302 DA2 A CG 1 HETATM 1932 C CD . DA2 C 3 . ? 23.062 6.183 -5.542 1.00 27.06 ? 302 DA2 A CD 1 HETATM 1933 N NE . DA2 C 3 . ? 21.648 6.620 -5.538 1.00 32.25 ? 302 DA2 A NE 1 HETATM 1934 C CZ . DA2 C 3 . ? 21.320 7.622 -4.704 1.00 30.00 ? 302 DA2 A CZ 1 HETATM 1935 N NH2 . DA2 C 3 . ? 21.223 8.815 -5.279 1.00 32.97 ? 302 DA2 A NH2 1 HETATM 1936 N NH1 . DA2 C 3 . ? 21.522 7.533 -3.354 1.00 31.75 ? 302 DA2 A NH1 1 HETATM 1937 C C . DA2 C 3 . ? 23.040 2.767 -2.277 1.00 28.40 ? 302 DA2 A C 1 HETATM 1938 O O . DA2 C 3 . ? 22.353 3.675 -1.686 1.00 33.13 ? 302 DA2 A O 1 HETATM 1939 O OXT . DA2 C 3 . ? 23.520 1.857 -1.607 1.00 35.90 ? 302 DA2 A OXT 1 HETATM 1940 O O . HOH D 4 . ? 23.408 -7.029 1.794 1.00 27.77 ? 401 HOH A O 1 HETATM 1941 O O . HOH D 4 . ? 3.567 -0.848 5.062 1.00 44.83 ? 402 HOH A O 1 HETATM 1942 O O . HOH D 4 . ? 11.449 -2.225 7.110 1.00 24.83 ? 403 HOH A O 1 HETATM 1943 O O . HOH D 4 . ? 20.015 23.076 -11.423 1.00 34.31 ? 404 HOH A O 1 HETATM 1944 O O . HOH D 4 . ? 15.041 1.745 15.817 1.00 42.50 ? 405 HOH A O 1 HETATM 1945 O O . HOH D 4 . ? 25.538 30.061 -13.517 1.00 34.76 ? 406 HOH A O 1 HETATM 1946 O O . HOH D 4 . ? 12.733 19.160 14.272 1.00 26.77 ? 407 HOH A O 1 HETATM 1947 O O . HOH D 4 . ? 13.704 -9.413 1.828 1.00 22.41 ? 408 HOH A O 1 HETATM 1948 O O . HOH D 4 . ? 19.824 -11.260 5.138 1.00 28.74 ? 409 HOH A O 1 HETATM 1949 O O . HOH D 4 . ? 18.570 -5.005 -7.208 1.00 36.50 ? 410 HOH A O 1 HETATM 1950 O O . HOH D 4 . ? 21.822 16.179 15.138 1.00 30.42 ? 411 HOH A O 1 HETATM 1951 O O . HOH D 4 . ? 15.254 17.842 14.954 1.00 30.02 ? 412 HOH A O 1 HETATM 1952 O O . HOH D 4 . ? 10.291 11.422 -5.460 1.00 22.00 ? 413 HOH A O 1 HETATM 1953 O O . HOH D 4 . ? 21.704 7.542 0.178 1.00 24.62 ? 414 HOH A O 1 HETATM 1954 O O . HOH D 4 . ? 26.704 -2.639 15.715 1.00 45.63 ? 415 HOH A O 1 HETATM 1955 O O . HOH D 4 . ? 29.238 21.978 2.414 1.00 35.19 ? 416 HOH A O 1 HETATM 1956 O O . HOH D 4 . ? 40.135 25.312 -5.023 1.00 44.92 ? 417 HOH A O 1 HETATM 1957 O O . HOH D 4 . ? 11.910 19.470 -5.707 1.00 24.19 ? 418 HOH A O 1 HETATM 1958 O O . HOH D 4 . ? 22.092 -7.012 11.880 1.00 26.11 ? 419 HOH A O 1 HETATM 1959 O O . HOH D 4 . ? 12.818 27.175 0.437 1.00 36.12 ? 420 HOH A O 1 HETATM 1960 O O . HOH D 4 . ? 8.622 -8.762 0.334 1.00 26.72 ? 421 HOH A O 1 HETATM 1961 O O . HOH D 4 . ? 30.465 -0.553 2.812 1.00 32.03 ? 422 HOH A O 1 HETATM 1962 O O . HOH D 4 . ? 5.577 -5.781 0.040 1.00 34.41 ? 423 HOH A O 1 HETATM 1963 O O . HOH D 4 . ? 26.392 11.836 -12.851 1.00 29.62 ? 424 HOH A O 1 HETATM 1964 O O . HOH D 4 . ? 34.173 11.240 3.429 1.00 25.83 ? 425 HOH A O 1 HETATM 1965 O O . HOH D 4 . ? 9.203 22.494 -6.926 1.00 32.52 ? 426 HOH A O 1 HETATM 1966 O O . HOH D 4 . ? 39.194 24.933 -2.320 1.00 38.10 ? 427 HOH A O 1 HETATM 1967 O O . HOH D 4 . ? 34.352 9.763 -2.102 1.00 25.26 ? 428 HOH A O 1 HETATM 1968 O O . HOH D 4 . ? 7.869 -4.669 -5.029 1.00 32.98 ? 429 HOH A O 1 HETATM 1969 O O . HOH D 4 . ? 5.222 10.199 -0.941 1.00 25.41 ? 430 HOH A O 1 HETATM 1970 O O . HOH D 4 . ? 25.390 0.253 15.124 1.00 36.92 ? 431 HOH A O 1 HETATM 1971 O O . HOH D 4 . ? 43.696 24.653 -13.410 1.00 47.89 ? 432 HOH A O 1 HETATM 1972 O O . HOH D 4 . ? 6.927 -7.425 2.141 1.00 30.81 ? 433 HOH A O 1 HETATM 1973 O O . HOH D 4 . ? 11.256 19.672 16.672 1.00 38.93 ? 434 HOH A O 1 HETATM 1974 O O . HOH D 4 . ? 11.089 -4.007 11.964 1.00 33.24 ? 435 HOH A O 1 HETATM 1975 O O . HOH D 4 . ? 27.633 7.885 13.428 1.00 34.96 ? 436 HOH A O 1 HETATM 1976 O O . HOH D 4 . ? 9.921 -5.643 -3.321 1.00 34.01 ? 437 HOH A O 1 HETATM 1977 O O . HOH D 4 . ? 24.473 -6.285 11.057 1.00 43.66 ? 438 HOH A O 1 HETATM 1978 O O . HOH D 4 . ? 9.727 13.551 16.087 1.00 28.28 ? 439 HOH A O 1 HETATM 1979 O O . HOH D 4 . ? 5.812 5.362 2.975 1.00 44.20 ? 440 HOH A O 1 HETATM 1980 O O . HOH D 4 . ? 13.873 -3.734 -8.624 1.00 32.18 ? 441 HOH A O 1 HETATM 1981 O O . HOH D 4 . ? 4.019 9.532 13.010 1.00 33.98 ? 442 HOH A O 1 HETATM 1982 O O . HOH D 4 . ? 10.468 3.362 17.696 1.00 33.47 ? 443 HOH A O 1 HETATM 1983 O O . HOH D 4 . ? 25.442 23.283 5.637 1.00 28.64 ? 444 HOH A O 1 HETATM 1984 O O . HOH D 4 . ? 12.554 25.395 -8.632 1.00 37.51 ? 445 HOH A O 1 HETATM 1985 O O . HOH D 4 . ? 39.534 19.193 6.633 1.00 43.95 ? 446 HOH A O 1 HETATM 1986 O O . HOH D 4 . ? 41.560 22.449 1.146 1.00 34.62 ? 447 HOH A O 1 HETATM 1987 O O . HOH D 4 . ? 6.095 1.979 -2.870 1.00 39.16 ? 448 HOH A O 1 HETATM 1988 O O . HOH D 4 . ? 32.644 26.783 -5.283 1.00 35.16 ? 449 HOH A O 1 HETATM 1989 O O . HOH D 4 . ? 4.351 22.161 -1.315 1.00 35.13 ? 450 HOH A O 1 HETATM 1990 O O . HOH D 4 . ? 39.307 15.116 1.390 1.00 37.53 ? 451 HOH A O 1 HETATM 1991 O O . HOH D 4 . ? 27.358 16.730 12.806 1.00 28.40 ? 452 HOH A O 1 HETATM 1992 O O . HOH D 4 . ? 19.537 18.105 13.841 1.00 28.97 ? 453 HOH A O 1 HETATM 1993 O O . HOH D 4 . ? 24.934 10.957 -9.626 1.00 28.82 ? 454 HOH A O 1 HETATM 1994 O O . HOH D 4 . ? 9.140 -1.636 5.382 1.00 23.58 ? 455 HOH A O 1 HETATM 1995 O O . HOH D 4 . ? 7.188 19.851 -8.677 1.00 33.21 ? 456 HOH A O 1 HETATM 1996 O O . HOH D 4 . ? 29.308 27.040 -16.582 1.00 33.61 ? 457 HOH A O 1 HETATM 1997 O O . HOH D 4 . ? 19.240 -3.255 18.088 1.00 45.06 ? 458 HOH A O 1 HETATM 1998 O O . HOH D 4 . ? 33.775 -0.718 6.336 1.00 36.90 ? 459 HOH A O 1 HETATM 1999 O O . HOH D 4 . ? 17.192 19.582 13.716 1.00 24.73 ? 460 HOH A O 1 HETATM 2000 O O . HOH D 4 . ? 41.473 12.462 -2.554 1.00 36.50 ? 461 HOH A O 1 HETATM 2001 O O . HOH D 4 . ? 20.917 -9.416 13.104 1.00 39.53 ? 462 HOH A O 1 HETATM 2002 O O . HOH D 4 . ? 5.066 23.408 3.196 1.00 30.12 ? 463 HOH A O 1 HETATM 2003 O O . HOH D 4 . ? 31.705 13.594 -16.044 1.00 38.08 ? 464 HOH A O 1 HETATM 2004 O O . HOH D 4 . ? 15.923 9.998 -13.684 1.00 38.82 ? 465 HOH A O 1 HETATM 2005 O O . HOH D 4 . ? 13.195 22.899 -11.709 1.00 39.70 ? 466 HOH A O 1 HETATM 2006 O O . HOH D 4 . ? 28.691 11.526 13.438 1.00 55.07 ? 467 HOH A O 1 HETATM 2007 O O . HOH D 4 . ? 4.996 18.890 13.830 1.00 36.53 ? 468 HOH A O 1 HETATM 2008 O O . HOH D 4 . ? 14.741 6.868 -13.476 1.00 51.24 ? 469 HOH A O 1 HETATM 2009 O O . HOH D 4 . ? 11.724 -6.562 -5.261 1.00 36.75 ? 470 HOH A O 1 HETATM 2010 O O . HOH D 4 . ? 42.486 18.125 -15.711 1.00 38.33 ? 471 HOH A O 1 HETATM 2011 O O . HOH D 4 . ? 3.650 7.830 -4.163 1.00 39.00 ? 472 HOH A O 1 HETATM 2012 O O . HOH D 4 . ? 16.343 -14.116 15.128 1.00 37.26 ? 473 HOH A O 1 HETATM 2013 O O . HOH D 4 . ? 27.816 -2.576 -3.399 1.00 44.51 ? 474 HOH A O 1 HETATM 2014 O O . HOH D 4 . ? 13.467 2.474 -12.931 1.00 42.25 ? 475 HOH A O 1 HETATM 2015 O O . HOH D 4 . ? 5.461 -6.368 8.743 1.00 40.34 ? 476 HOH A O 1 HETATM 2016 O O . HOH D 4 . ? 30.292 -7.715 0.651 1.00 42.38 ? 477 HOH A O 1 HETATM 2017 O O . HOH D 4 . ? 5.799 3.713 0.554 1.00 36.09 ? 478 HOH A O 1 HETATM 2018 O O . HOH D 4 . ? 17.290 6.107 16.635 1.00 44.66 ? 479 HOH A O 1 HETATM 2019 O O . HOH D 4 . ? 28.780 2.346 -0.812 1.00 35.36 ? 480 HOH A O 1 HETATM 2020 O O . HOH D 4 . ? 25.747 -8.432 -2.055 1.00 35.28 ? 481 HOH A O 1 HETATM 2021 O O . HOH D 4 . ? 18.434 26.116 9.569 1.00 34.70 ? 482 HOH A O 1 HETATM 2022 O O . HOH D 4 . ? 27.404 22.101 7.257 1.00 38.61 ? 483 HOH A O 1 HETATM 2023 O O . HOH D 4 . ? 2.878 16.620 -6.232 1.00 33.63 ? 484 HOH A O 1 HETATM 2024 O O . HOH D 4 . ? 36.744 28.681 -14.758 1.00 39.97 ? 485 HOH A O 1 HETATM 2025 O O . HOH D 4 . ? 8.699 -6.529 10.367 1.00 30.04 ? 486 HOH A O 1 HETATM 2026 O O . HOH D 4 . ? 40.443 7.459 5.771 1.00 51.59 ? 487 HOH A O 1 HETATM 2027 O O . HOH D 4 . ? 11.311 27.780 10.473 1.00 34.97 ? 488 HOH A O 1 HETATM 2028 O O . HOH D 4 . ? 18.971 -6.006 -11.656 1.00 53.27 ? 489 HOH A O 1 HETATM 2029 O O . HOH D 4 . ? 24.851 15.875 15.380 1.00 46.10 ? 490 HOH A O 1 HETATM 2030 O O . HOH D 4 . ? 11.342 -5.058 -7.997 1.00 36.18 ? 491 HOH A O 1 HETATM 2031 O O . HOH D 4 . ? 17.949 -5.671 19.032 1.00 54.71 ? 492 HOH A O 1 HETATM 2032 O O . HOH D 4 . ? 41.403 13.956 -0.134 1.00 40.90 ? 493 HOH A O 1 HETATM 2033 O O . HOH D 4 . ? 34.177 29.897 -8.760 1.00 39.61 ? 494 HOH A O 1 HETATM 2034 O O . HOH D 4 . ? 3.254 5.091 6.406 1.00 37.06 ? 495 HOH A O 1 HETATM 2035 O O . HOH D 4 . ? 8.684 22.142 -9.689 1.00 41.04 ? 496 HOH A O 1 HETATM 2036 O O . HOH D 4 . ? 9.833 20.978 -12.359 1.00 43.81 ? 497 HOH A O 1 HETATM 2037 O O . HOH D 4 . ? 23.158 12.166 -6.282 1.00 24.29 ? 498 HOH A O 1 HETATM 2038 O O . HOH D 4 . ? 25.715 28.193 -0.591 1.00 48.17 ? 499 HOH A O 1 HETATM 2039 O O . HOH D 4 . ? 16.784 16.283 16.826 1.00 40.67 ? 500 HOH A O 1 HETATM 2040 O O . HOH D 4 . ? 12.074 -5.467 14.826 1.00 35.89 ? 501 HOH A O 1 HETATM 2041 O O . HOH D 4 . ? 33.618 22.772 -20.521 1.00 41.62 ? 502 HOH A O 1 HETATM 2042 O O . HOH D 4 . ? 2.939 -3.241 -0.466 1.00 46.83 ? 503 HOH A O 1 HETATM 2043 O O . HOH D 4 . ? 6.305 6.052 -1.282 1.00 41.64 ? 504 HOH A O 1 HETATM 2044 O O . HOH D 4 . ? 12.249 12.418 19.953 1.00 46.75 ? 505 HOH A O 1 HETATM 2045 O O . HOH D 4 . ? 29.345 7.389 -9.304 1.00 39.26 ? 506 HOH A O 1 HETATM 2046 O O . HOH D 4 . ? 8.630 2.413 -11.765 1.00 40.26 ? 507 HOH A O 1 HETATM 2047 O O . HOH D 4 . ? 15.058 25.673 -3.920 1.00 41.05 ? 508 HOH A O 1 HETATM 2048 O O . HOH D 4 . ? 25.080 12.996 17.989 1.00 50.31 ? 509 HOH A O 1 HETATM 2049 O O . HOH D 4 . ? 5.954 26.526 0.779 1.00 37.36 ? 510 HOH A O 1 HETATM 2050 O O . HOH D 4 . ? 43.887 29.819 -14.358 1.00 35.02 ? 511 HOH A O 1 HETATM 2051 O O . HOH D 4 . ? 23.815 25.447 6.551 1.00 39.47 ? 512 HOH A O 1 HETATM 2052 O O . HOH D 4 . ? 29.346 3.132 12.524 1.00 41.42 ? 513 HOH A O 1 HETATM 2053 O O . HOH D 4 . ? -0.154 10.808 15.396 1.00 42.58 ? 514 HOH A O 1 HETATM 2054 O O . HOH D 4 . ? 28.766 28.362 -19.911 1.00 57.02 ? 515 HOH A O 1 HETATM 2055 O O . HOH D 4 . ? 18.321 26.447 6.087 1.00 45.92 ? 516 HOH A O 1 HETATM 2056 O O . HOH D 4 . ? 22.499 25.922 -9.092 1.00 32.41 ? 517 HOH A O 1 HETATM 2057 O O . HOH D 4 . ? 31.531 17.706 4.815 1.00 41.13 ? 518 HOH A O 1 HETATM 2058 O O . HOH D 4 . ? 4.423 0.428 9.670 1.00 45.42 ? 519 HOH A O 1 HETATM 2059 O O . HOH D 4 . ? 42.785 25.670 -20.176 1.00 39.94 ? 520 HOH A O 1 HETATM 2060 O O . HOH D 4 . ? 28.546 25.377 -3.892 1.00 25.40 ? 521 HOH A O 1 HETATM 2061 O O . HOH D 4 . ? 28.240 14.331 13.939 1.00 53.29 ? 522 HOH A O 1 HETATM 2062 O O . HOH D 4 . ? 24.147 15.033 -16.111 1.00 56.65 ? 523 HOH A O 1 HETATM 2063 O O . HOH D 4 . ? 27.248 1.299 -6.205 1.00 42.34 ? 524 HOH A O 1 HETATM 2064 O O . HOH D 4 . ? 35.702 3.623 -0.734 1.00 40.21 ? 525 HOH A O 1 HETATM 2065 O O . HOH D 4 . ? 4.528 5.351 14.435 1.00 44.30 ? 526 HOH A O 1 HETATM 2066 O O . HOH D 4 . ? 41.764 16.512 -5.151 1.00 49.36 ? 527 HOH A O 1 HETATM 2067 O O . HOH D 4 . ? 26.858 0.491 -3.380 1.00 52.57 ? 528 HOH A O 1 HETATM 2068 O O . HOH D 4 . ? 33.365 25.653 2.404 1.00 40.02 ? 529 HOH A O 1 HETATM 2069 O O . HOH D 4 . ? 11.430 -8.529 -7.289 1.00 35.65 ? 530 HOH A O 1 HETATM 2070 O O . HOH D 4 . ? 5.876 24.739 12.256 1.00 43.38 ? 531 HOH A O 1 HETATM 2071 O O . HOH D 4 . ? 33.512 17.304 8.640 1.00 46.28 ? 532 HOH A O 1 HETATM 2072 O O . HOH D 4 . ? 25.035 16.121 -18.750 1.00 49.92 ? 533 HOH A O 1 HETATM 2073 O O . HOH D 4 . ? 8.252 1.128 16.576 1.00 39.26 ? 534 HOH A O 1 HETATM 2074 O O . HOH D 4 . ? 39.861 2.177 3.842 1.00 58.21 ? 535 HOH A O 1 HETATM 2075 O O . HOH D 4 . ? 37.282 9.105 -12.011 1.00 47.99 ? 536 HOH A O 1 HETATM 2076 O O . HOH D 4 . ? 40.931 23.057 -5.919 1.00 48.33 ? 537 HOH A O 1 HETATM 2077 O O . HOH D 4 . ? 6.347 22.964 -2.963 1.00 44.32 ? 538 HOH A O 1 HETATM 2078 O O . HOH D 4 . ? 24.243 1.512 -8.332 1.00 58.42 ? 539 HOH A O 1 HETATM 2079 O O . HOH D 4 . ? 27.089 10.659 18.522 1.00 49.67 ? 540 HOH A O 1 HETATM 2080 O O . HOH D 4 . ? 21.930 25.726 3.072 1.00 34.92 ? 541 HOH A O 1 HETATM 2081 O O . HOH D 4 . ? 20.525 -9.576 19.458 1.00 55.12 ? 542 HOH A O 1 HETATM 2082 O O . HOH D 4 . ? 38.876 21.823 -21.613 1.00 48.43 ? 543 HOH A O 1 HETATM 2083 O O . HOH D 4 . ? 40.312 4.409 -8.737 1.00 52.11 ? 544 HOH A O 1 HETATM 2084 O O . HOH D 4 . ? 3.289 2.161 0.016 1.00 48.16 ? 545 HOH A O 1 HETATM 2085 O O . HOH D 4 . ? 30.652 10.812 11.420 1.00 49.96 ? 546 HOH A O 1 HETATM 2086 O O . HOH D 4 . ? -0.730 24.877 -4.746 1.00 61.73 ? 547 HOH A O 1 HETATM 2087 O O . HOH D 4 . ? 15.777 -5.858 -7.880 1.00 47.66 ? 548 HOH A O 1 HETATM 2088 O O . HOH D 4 . ? 8.804 15.126 -10.988 1.00 49.22 ? 549 HOH A O 1 HETATM 2089 O O . HOH D 4 . ? 7.852 24.242 -4.912 1.00 52.41 ? 550 HOH A O 1 HETATM 2090 O O . HOH D 4 . ? 23.114 15.001 17.505 1.00 57.42 ? 551 HOH A O 1 HETATM 2091 O O . HOH D 4 . ? 5.317 13.677 -12.338 1.00 40.36 ? 552 HOH A O 1 HETATM 2092 O O . HOH D 4 . ? 20.952 -7.188 -6.158 1.00 49.98 ? 553 HOH A O 1 HETATM 2093 O O . HOH D 4 . ? 24.188 27.391 -13.168 1.00 47.80 ? 554 HOH A O 1 HETATM 2094 O O . HOH D 4 . ? 10.761 3.042 -13.426 1.00 44.37 ? 555 HOH A O 1 HETATM 2095 O O . HOH D 4 . ? 21.535 23.739 6.344 1.00 28.19 ? 556 HOH A O 1 HETATM 2096 O O . HOH D 4 . ? 26.504 8.623 -7.130 1.00 33.22 ? 557 HOH A O 1 HETATM 2097 O O . HOH D 4 . ? 14.854 27.848 2.260 1.00 41.61 ? 558 HOH A O 1 HETATM 2098 O O . HOH D 4 . ? 20.568 2.970 16.931 1.00 40.01 ? 559 HOH A O 1 HETATM 2099 O O . HOH D 4 . ? 22.537 -8.130 4.204 1.00 35.18 ? 560 HOH A O 1 HETATM 2100 O O . HOH D 4 . ? 23.470 -8.765 -0.367 1.00 30.62 ? 561 HOH A O 1 HETATM 2101 O O . HOH D 4 . ? 3.337 1.667 4.513 1.00 32.36 ? 562 HOH A O 1 HETATM 2102 O O . HOH D 4 . ? 1.503 18.835 -4.369 1.00 36.01 ? 563 HOH A O 1 HETATM 2103 O O . HOH D 4 . ? 2.647 24.889 3.370 1.00 44.45 ? 564 HOH A O 1 HETATM 2104 O O . HOH D 4 . ? -0.253 24.409 1.708 1.00 36.96 ? 565 HOH A O 1 HETATM 2105 O O . HOH D 4 . ? 32.145 -9.525 16.202 1.00 42.36 ? 566 HOH A O 1 HETATM 2106 O O . HOH D 4 . ? 19.550 17.124 16.926 1.00 36.42 ? 567 HOH A O 1 HETATM 2107 O O . HOH D 4 . ? 31.239 23.947 3.031 1.00 45.00 ? 568 HOH A O 1 HETATM 2108 O O . HOH D 4 . ? 21.723 26.628 -4.927 1.00 43.80 ? 569 HOH A O 1 HETATM 2109 O O . HOH D 4 . ? 19.137 27.630 -4.639 1.00 44.12 ? 570 HOH A O 1 HETATM 2110 O O . HOH D 4 . ? 13.662 9.229 -12.208 1.00 50.42 ? 571 HOH A O 1 HETATM 2111 O O . HOH D 4 . ? 31.212 11.081 -14.822 1.00 43.44 ? 572 HOH A O 1 HETATM 2112 O O . HOH D 4 . ? 7.109 7.766 2.233 1.00 37.67 ? 573 HOH A O 1 HETATM 2113 O O . HOH D 4 . ? 26.573 13.714 -15.225 1.00 44.02 ? 574 HOH A O 1 HETATM 2114 O O . HOH D 4 . ? 14.320 -15.079 18.725 1.00 56.54 ? 575 HOH A O 1 HETATM 2115 O O . HOH D 4 . ? 9.845 13.357 18.809 1.00 35.17 ? 576 HOH A O 1 HETATM 2116 O O . HOH D 4 . ? 7.471 12.874 20.110 1.00 41.04 ? 577 HOH A O 1 HETATM 2117 O O . HOH D 4 . ? 30.992 5.554 -10.818 1.00 53.54 ? 578 HOH A O 1 HETATM 2118 O O . HOH D 4 . ? 24.180 -10.579 2.379 1.00 53.89 ? 579 HOH A O 1 HETATM 2119 O O . HOH D 4 . ? 34.663 -7.114 9.652 1.00 54.48 ? 580 HOH A O 1 HETATM 2120 O O . HOH D 4 . ? 21.766 -2.929 -8.622 1.00 47.61 ? 581 HOH A O 1 HETATM 2121 O O . HOH D 4 . ? 7.461 -1.559 -11.756 1.00 50.88 ? 582 HOH A O 1 HETATM 2122 O O . HOH D 4 . ? 35.862 14.190 -18.281 1.00 42.07 ? 583 HOH A O 1 HETATM 2123 O O . HOH D 4 . ? 18.857 10.650 18.839 1.00 51.04 ? 584 HOH A O 1 HETATM 2124 O O . HOH D 4 . ? 26.631 21.188 12.567 1.00 37.74 ? 585 HOH A O 1 HETATM 2125 O O . HOH D 4 . ? 16.383 21.291 15.709 1.00 35.54 ? 586 HOH A O 1 HETATM 2126 O O . HOH D 4 . ? 17.217 -8.280 -4.675 1.00 42.71 ? 587 HOH A O 1 HETATM 2127 O O . HOH D 4 . ? 44.567 18.332 -8.109 1.00 47.85 ? 588 HOH A O 1 HETATM 2128 O O . HOH D 4 . ? 33.880 27.421 -7.794 1.00 45.55 ? 589 HOH A O 1 HETATM 2129 O O . HOH D 4 . ? 7.522 25.599 4.392 1.00 47.78 ? 590 HOH A O 1 HETATM 2130 O O . HOH D 4 . ? 18.981 27.372 -10.973 1.00 37.20 ? 591 HOH A O 1 HETATM 2131 O O . HOH D 4 . ? 18.608 24.128 -9.227 1.00 38.64 ? 592 HOH A O 1 HETATM 2132 O O . HOH D 4 . ? 32.487 20.205 8.907 1.00 51.64 ? 593 HOH A O 1 HETATM 2133 O O . HOH D 4 . ? 33.399 14.756 10.260 1.00 64.92 ? 594 HOH A O 1 HETATM 2134 O O . HOH D 4 . ? 36.301 16.407 8.256 1.00 45.39 ? 595 HOH A O 1 HETATM 2135 O O . HOH D 4 . ? 21.376 25.546 -11.881 1.00 39.73 ? 596 HOH A O 1 HETATM 2136 O O . HOH D 4 . ? 13.260 25.385 14.678 1.00 45.72 ? 597 HOH A O 1 HETATM 2137 O O . HOH D 4 . ? 5.072 -1.189 7.332 1.00 38.38 ? 598 HOH A O 1 HETATM 2138 O O . HOH D 4 . ? 21.883 8.314 -8.432 1.00 32.19 ? 599 HOH A O 1 HETATM 2139 O O . HOH D 4 . ? 33.250 3.922 -14.003 1.00 57.58 ? 600 HOH A O 1 HETATM 2140 O O . HOH D 4 . ? 42.580 11.848 3.965 1.00 50.25 ? 601 HOH A O 1 HETATM 2141 O O . HOH D 4 . ? 17.375 28.221 -6.910 1.00 52.75 ? 602 HOH A O 1 HETATM 2142 O O . HOH D 4 . ? 33.260 -6.763 12.201 1.00 50.56 ? 603 HOH A O 1 HETATM 2143 O O . HOH D 4 . ? 5.582 -2.889 -7.041 1.00 46.26 ? 604 HOH A O 1 HETATM 2144 O O . HOH D 4 . ? 6.186 6.739 20.614 1.00 51.64 ? 605 HOH A O 1 HETATM 2145 O O . HOH D 4 . ? 1.508 -1.516 1.560 1.00 63.24 ? 606 HOH A O 1 HETATM 2146 O O . HOH D 4 . ? 30.805 5.469 -4.851 1.00 53.69 ? 607 HOH A O 1 HETATM 2147 O O . HOH D 4 . ? 8.082 27.349 13.306 1.00 46.21 ? 608 HOH A O 1 HETATM 2148 O O . HOH D 4 . ? 27.709 15.320 -19.694 1.00 52.58 ? 609 HOH A O 1 HETATM 2149 O O . HOH D 4 . ? 34.987 19.826 -24.068 1.00 51.35 ? 610 HOH A O 1 HETATM 2150 O O . HOH D 4 . ? 11.170 9.698 21.071 1.00 40.93 ? 611 HOH A O 1 HETATM 2151 O O . HOH D 4 . ? 10.322 23.997 -12.768 1.00 53.48 ? 612 HOH A O 1 HETATM 2152 O O . HOH D 4 . ? 2.413 11.873 -8.943 1.00 46.98 ? 613 HOH A O 1 HETATM 2153 O O . HOH D 4 . ? 32.970 4.729 -1.870 1.00 43.77 ? 614 HOH A O 1 HETATM 2154 O O . HOH D 4 . ? 10.668 26.753 -19.442 1.00 57.67 ? 615 HOH A O 1 HETATM 2155 O O . HOH D 4 . ? 31.022 -8.572 3.833 1.00 52.19 ? 616 HOH A O 1 HETATM 2156 O O . HOH D 4 . ? 28.449 1.091 14.511 1.00 48.93 ? 617 HOH A O 1 HETATM 2157 O O . HOH D 4 . ? 9.640 -1.310 14.918 1.00 41.31 ? 618 HOH A O 1 HETATM 2158 O O . HOH D 4 . ? 4.843 12.670 19.263 1.00 46.59 ? 619 HOH A O 1 HETATM 2159 O O . HOH D 4 . ? 21.112 5.297 -8.671 1.00 29.95 ? 620 HOH A O 1 HETATM 2160 O O . HOH D 4 . ? 27.950 3.846 -7.512 1.00 40.10 ? 621 HOH A O 1 HETATM 2161 O O . HOH D 4 . ? 25.119 4.191 -8.114 1.00 48.00 ? 622 HOH A O 1 HETATM 2162 O O . HOH D 4 . ? 24.323 9.684 -5.701 1.00 32.98 ? 623 HOH A O 1 HETATM 2163 O O . HOH D 4 . ? 20.633 8.624 -10.974 1.00 40.28 ? 624 HOH A O 1 HETATM 2164 O O . HOH D 4 . ? 30.006 8.811 -12.725 1.00 54.54 ? 625 HOH A O 1 HETATM 2165 O O . HOH D 4 . ? 16.270 0.040 17.837 1.00 50.14 ? 626 HOH A O 1 HETATM 2166 O O . HOH D 4 . ? 21.993 -3.042 17.071 1.00 41.95 ? 627 HOH A O 1 HETATM 2167 O O . HOH D 4 . ? 35.751 -0.209 4.412 1.00 44.06 ? 628 HOH A O 1 HETATM 2168 O O . HOH D 4 . ? 37.939 -1.872 7.208 1.00 44.24 ? 629 HOH A O 1 HETATM 2169 O O . HOH D 4 . ? 6.184 15.655 20.346 1.00 42.75 ? 630 HOH A O 1 HETATM 2170 O O . HOH D 4 . ? 31.377 33.801 -21.070 1.00 42.36 ? 631 HOH A O 1 HETATM 2171 O O . HOH D 4 . ? 27.328 34.479 -17.062 1.00 45.95 ? 632 HOH A O 1 HETATM 2172 O O . HOH D 4 . ? 34.275 16.941 -24.089 1.00 46.95 ? 633 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 # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-08-28 2 'Structure model' 1 1 2013-11-06 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Non-polymer description' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal HKL-2000 'data collection' . ? 1 AMoRE phasing . ? 2 REFMAC refinement 5.7.0032 ? 3 DENZO 'data reduction' . ? 4 SCALEPACK 'data scaling' . ? 5 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 LEU A 77 ? ? 56.26 -106.89 2 1 PRO A 106 ? ? -83.43 44.48 3 1 ASP A 143 ? ? -163.85 98.84 4 1 THR A 158 ? ? -119.95 -79.55 5 1 SER A 218 ? ? -54.25 3.58 6 1 ASN A 236 ? ? -94.41 -66.66 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 NG,NG-DIMETHYL-L-ARGININE DA2 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 1 301 301 NAG NAG A . C 3 DA2 1 302 1 DA2 DA2 A . D 4 HOH 1 401 1 HOH HOH A . D 4 HOH 2 402 2 HOH HOH A . D 4 HOH 3 403 3 HOH HOH A . D 4 HOH 4 404 4 HOH HOH A . D 4 HOH 5 405 5 HOH HOH A . D 4 HOH 6 406 6 HOH HOH A . D 4 HOH 7 407 7 HOH HOH A . D 4 HOH 8 408 8 HOH HOH A . D 4 HOH 9 409 9 HOH HOH A . D 4 HOH 10 410 10 HOH HOH A . D 4 HOH 11 411 11 HOH HOH A . D 4 HOH 12 412 12 HOH HOH A . D 4 HOH 13 413 13 HOH HOH A . D 4 HOH 14 414 14 HOH HOH A . D 4 HOH 15 415 15 HOH HOH A . D 4 HOH 16 416 16 HOH HOH A . D 4 HOH 17 417 17 HOH HOH A . D 4 HOH 18 418 18 HOH HOH A . D 4 HOH 19 419 19 HOH HOH A . D 4 HOH 20 420 20 HOH HOH A . D 4 HOH 21 421 21 HOH HOH A . D 4 HOH 22 422 22 HOH HOH A . D 4 HOH 23 423 23 HOH HOH A . D 4 HOH 24 424 24 HOH HOH A . D 4 HOH 25 425 25 HOH HOH A . D 4 HOH 26 426 26 HOH HOH A . D 4 HOH 27 427 27 HOH HOH A . D 4 HOH 28 428 28 HOH HOH A . D 4 HOH 29 429 29 HOH HOH A . D 4 HOH 30 430 30 HOH HOH A . D 4 HOH 31 431 31 HOH HOH A . D 4 HOH 32 432 32 HOH HOH A . D 4 HOH 33 433 33 HOH HOH A . D 4 HOH 34 434 34 HOH HOH A . D 4 HOH 35 435 35 HOH HOH A . D 4 HOH 36 436 36 HOH HOH A . D 4 HOH 37 437 37 HOH HOH A . D 4 HOH 38 438 38 HOH HOH A . D 4 HOH 39 439 39 HOH HOH A . D 4 HOH 40 440 40 HOH HOH A . D 4 HOH 41 441 41 HOH HOH A . D 4 HOH 42 442 42 HOH HOH A . D 4 HOH 43 443 43 HOH HOH A . D 4 HOH 44 444 44 HOH HOH A . D 4 HOH 45 445 45 HOH HOH A . D 4 HOH 46 446 46 HOH HOH A . D 4 HOH 47 447 47 HOH HOH A . D 4 HOH 48 448 48 HOH HOH A . D 4 HOH 49 449 49 HOH HOH A . D 4 HOH 50 450 50 HOH HOH A . D 4 HOH 51 451 51 HOH HOH A . D 4 HOH 52 452 52 HOH HOH A . D 4 HOH 53 453 53 HOH HOH A . D 4 HOH 54 454 54 HOH HOH A . D 4 HOH 55 455 55 HOH HOH A . D 4 HOH 56 456 56 HOH HOH A . D 4 HOH 57 457 57 HOH HOH A . D 4 HOH 58 458 58 HOH HOH A . D 4 HOH 59 459 59 HOH HOH A . D 4 HOH 60 460 60 HOH HOH A . D 4 HOH 61 461 61 HOH HOH A . D 4 HOH 62 462 62 HOH HOH A . D 4 HOH 63 463 63 HOH HOH A . D 4 HOH 64 464 64 HOH HOH A . D 4 HOH 65 465 65 HOH HOH A . D 4 HOH 66 466 66 HOH HOH A . D 4 HOH 67 467 67 HOH HOH A . D 4 HOH 68 468 68 HOH HOH A . D 4 HOH 69 469 69 HOH HOH A . D 4 HOH 70 470 70 HOH HOH A . D 4 HOH 71 471 71 HOH HOH A . D 4 HOH 72 472 72 HOH HOH A . D 4 HOH 73 473 73 HOH HOH A . D 4 HOH 74 474 74 HOH HOH A . D 4 HOH 75 475 75 HOH HOH A . D 4 HOH 76 476 77 HOH HOH A . D 4 HOH 77 477 78 HOH HOH A . D 4 HOH 78 478 79 HOH HOH A . D 4 HOH 79 479 80 HOH HOH A . D 4 HOH 80 480 81 HOH HOH A . D 4 HOH 81 481 82 HOH HOH A . D 4 HOH 82 482 83 HOH HOH A . D 4 HOH 83 483 84 HOH HOH A . D 4 HOH 84 484 85 HOH HOH A . D 4 HOH 85 485 86 HOH HOH A . D 4 HOH 86 486 87 HOH HOH A . D 4 HOH 87 487 88 HOH HOH A . D 4 HOH 88 488 89 HOH HOH A . D 4 HOH 89 489 90 HOH HOH A . D 4 HOH 90 490 91 HOH HOH A . D 4 HOH 91 491 92 HOH HOH A . D 4 HOH 92 492 93 HOH HOH A . D 4 HOH 93 493 94 HOH HOH A . D 4 HOH 94 494 95 HOH HOH A . D 4 HOH 95 495 96 HOH HOH A . D 4 HOH 96 496 97 HOH HOH A . D 4 HOH 97 497 98 HOH HOH A . D 4 HOH 98 498 99 HOH HOH A . D 4 HOH 99 499 100 HOH HOH A . D 4 HOH 100 500 101 HOH HOH A . D 4 HOH 101 501 102 HOH HOH A . D 4 HOH 102 502 103 HOH HOH A . D 4 HOH 103 503 104 HOH HOH A . D 4 HOH 104 504 105 HOH HOH A . D 4 HOH 105 505 106 HOH HOH A . D 4 HOH 106 506 107 HOH HOH A . D 4 HOH 107 507 108 HOH HOH A . D 4 HOH 108 508 109 HOH HOH A . D 4 HOH 109 509 111 HOH HOH A . D 4 HOH 110 510 112 HOH HOH A . D 4 HOH 111 511 114 HOH HOH A . D 4 HOH 112 512 115 HOH HOH A . D 4 HOH 113 513 116 HOH HOH A . D 4 HOH 114 514 117 HOH HOH A . D 4 HOH 115 515 118 HOH HOH A . D 4 HOH 116 516 119 HOH HOH A . D 4 HOH 117 517 121 HOH HOH A . D 4 HOH 118 518 122 HOH HOH A . D 4 HOH 119 519 123 HOH HOH A . D 4 HOH 120 520 124 HOH HOH A . D 4 HOH 121 521 125 HOH HOH A . D 4 HOH 122 522 128 HOH HOH A . D 4 HOH 123 523 129 HOH HOH A . D 4 HOH 124 524 130 HOH HOH A . D 4 HOH 125 525 131 HOH HOH A . D 4 HOH 126 526 132 HOH HOH A . D 4 HOH 127 527 133 HOH HOH A . D 4 HOH 128 528 134 HOH HOH A . D 4 HOH 129 529 135 HOH HOH A . D 4 HOH 130 530 136 HOH HOH A . D 4 HOH 131 531 137 HOH HOH A . D 4 HOH 132 532 138 HOH HOH A . D 4 HOH 133 533 140 HOH HOH A . D 4 HOH 134 534 141 HOH HOH A . D 4 HOH 135 535 142 HOH HOH A . D 4 HOH 136 536 143 HOH HOH A . D 4 HOH 137 537 144 HOH HOH A . D 4 HOH 138 538 145 HOH HOH A . D 4 HOH 139 539 146 HOH HOH A . D 4 HOH 140 540 149 HOH HOH A . D 4 HOH 141 541 150 HOH HOH A . D 4 HOH 142 542 151 HOH HOH A . D 4 HOH 143 543 152 HOH HOH A . D 4 HOH 144 544 153 HOH HOH A . D 4 HOH 145 545 156 HOH HOH A . D 4 HOH 146 546 157 HOH HOH A . D 4 HOH 147 547 158 HOH HOH A . D 4 HOH 148 548 159 HOH HOH A . D 4 HOH 149 549 160 HOH HOH A . D 4 HOH 150 550 161 HOH HOH A . D 4 HOH 151 551 162 HOH HOH A . D 4 HOH 152 552 163 HOH HOH A . D 4 HOH 153 553 164 HOH HOH A . D 4 HOH 154 554 166 HOH HOH A . D 4 HOH 155 555 168 HOH HOH A . D 4 HOH 156 556 169 HOH HOH A . D 4 HOH 157 557 170 HOH HOH A . D 4 HOH 158 558 173 HOH HOH A . D 4 HOH 159 559 174 HOH HOH A . D 4 HOH 160 560 175 HOH HOH A . D 4 HOH 161 561 176 HOH HOH A . D 4 HOH 162 562 177 HOH HOH A . D 4 HOH 163 563 178 HOH HOH A . D 4 HOH 164 564 179 HOH HOH A . D 4 HOH 165 565 180 HOH HOH A . D 4 HOH 166 566 181 HOH HOH A . D 4 HOH 167 567 184 HOH HOH A . D 4 HOH 168 568 185 HOH HOH A . D 4 HOH 169 569 186 HOH HOH A . D 4 HOH 170 570 187 HOH HOH A . D 4 HOH 171 571 188 HOH HOH A . D 4 HOH 172 572 189 HOH HOH A . D 4 HOH 173 573 190 HOH HOH A . D 4 HOH 174 574 192 HOH HOH A . D 4 HOH 175 575 194 HOH HOH A . D 4 HOH 176 576 195 HOH HOH A . D 4 HOH 177 577 196 HOH HOH A . D 4 HOH 178 578 197 HOH HOH A . D 4 HOH 179 579 198 HOH HOH A . D 4 HOH 180 580 199 HOH HOH A . D 4 HOH 181 581 200 HOH HOH A . D 4 HOH 182 582 202 HOH HOH A . D 4 HOH 183 583 204 HOH HOH A . D 4 HOH 184 584 205 HOH HOH A . D 4 HOH 185 585 206 HOH HOH A . D 4 HOH 186 586 207 HOH HOH A . D 4 HOH 187 587 208 HOH HOH A . D 4 HOH 188 588 209 HOH HOH A . D 4 HOH 189 589 210 HOH HOH A . D 4 HOH 190 590 213 HOH HOH A . D 4 HOH 191 591 214 HOH HOH A . D 4 HOH 192 592 215 HOH HOH A . D 4 HOH 193 593 217 HOH HOH A . D 4 HOH 194 594 218 HOH HOH A . D 4 HOH 195 595 219 HOH HOH A . D 4 HOH 196 596 220 HOH HOH A . D 4 HOH 197 597 221 HOH HOH A . D 4 HOH 198 598 223 HOH HOH A . D 4 HOH 199 599 226 HOH HOH A . D 4 HOH 200 600 227 HOH HOH A . D 4 HOH 201 601 228 HOH HOH A . D 4 HOH 202 602 229 HOH HOH A . D 4 HOH 203 603 230 HOH HOH A . D 4 HOH 204 604 231 HOH HOH A . D 4 HOH 205 605 233 HOH HOH A . D 4 HOH 206 606 234 HOH HOH A . D 4 HOH 207 607 235 HOH HOH A . D 4 HOH 208 608 236 HOH HOH A . D 4 HOH 209 609 237 HOH HOH A . D 4 HOH 210 610 238 HOH HOH A . D 4 HOH 211 611 240 HOH HOH A . D 4 HOH 212 612 241 HOH HOH A . D 4 HOH 213 613 243 HOH HOH A . D 4 HOH 214 614 244 HOH HOH A . D 4 HOH 215 615 245 HOH HOH A . D 4 HOH 216 616 246 HOH HOH A . D 4 HOH 217 617 247 HOH HOH A . D 4 HOH 218 618 248 HOH HOH A . D 4 HOH 219 619 250 HOH HOH A . D 4 HOH 220 620 251 HOH HOH A . D 4 HOH 221 621 252 HOH HOH A . D 4 HOH 222 622 253 HOH HOH A . D 4 HOH 223 623 254 HOH HOH A . D 4 HOH 224 624 255 HOH HOH A . D 4 HOH 225 625 256 HOH HOH A . D 4 HOH 226 626 257 HOH HOH A . D 4 HOH 227 627 258 HOH HOH A . D 4 HOH 228 628 259 HOH HOH A . D 4 HOH 229 629 260 HOH HOH A . D 4 HOH 230 630 261 HOH HOH A . D 4 HOH 231 631 262 HOH HOH A . D 4 HOH 232 632 263 HOH HOH A . D 4 HOH 233 633 264 HOH HOH A . #