data_4KWN # _entry.id 4KWN # _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 4KWN RCSB RCSB079887 WWPDB D_1000079887 # _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 4KWN _pdbx_database_status.recvd_initial_deposition_date 2013-05-24 _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 'Singh, A.' 3 'Bhushan, A.' 4 'Sinha, M.' 5 'Kaur, P.' 6 'Sharma, S.' 7 'Singh, T.P.' 8 # _citation.id primary _citation.title ;A new stabilizing water structure at the substrate binding site in ribosome inactivating protein from Momordica balsamina at 1.80 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 'Singh, A.' 3 primary 'Bhushan, A.' 4 primary 'Sinha, M.' 5 primary 'Kaur, P.' 6 primary 'Sharma, S.' 7 primary 'Singh, T.P.' 8 # _cell.entry_id 4KWN _cell.length_a 130.212 _cell.length_b 130.212 _cell.length_c 39.847 _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 4KWN _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'rRNA N-glycosidase' 27093.756 1 3.2.2.22 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 4 water nat water 18.015 268 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Ribosome inactivating protein' # _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 4KWN _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 246 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession D9J2T9 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 246 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 246 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4KWN _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.40 _exptl_crystal.density_percent_sol 48.74 _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 6.7 _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 2013-05-01 _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 4KWN _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 50.00 _reflns.d_resolution_high 1.80 _reflns.number_obs 22146 _reflns.number_all 22146 _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.0630 _reflns.pdbx_netI_over_sigmaI 32.3 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.80 _reflns_shell.d_res_low 1.83 _reflns_shell.percent_possible_all 99.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.429 _reflns_shell.meanI_over_sigI_obs 2.3 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4KWN _refine.ls_number_reflns_obs 22146 _refine.ls_number_reflns_all 22146 _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 37.60 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.84 _refine.ls_R_factor_obs 0.18017 _refine.ls_R_factor_all 0.18171 _refine.ls_R_factor_R_work 0.17839 _refine.ls_R_factor_R_free 0.21389 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1199 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.968 _refine.correlation_coeff_Fo_to_Fc_free 0.956 _refine.B_iso_mean 29.896 _refine.aniso_B[1][1] -0.81 _refine.aniso_B[2][2] -0.81 _refine.aniso_B[3][3] 2.64 _refine.aniso_B[1][2] -0.81 _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 0.133 _refine.pdbx_overall_ESU_R_Free 0.124 _refine.overall_SU_ML 0.092 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.983 _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 26 _refine_hist.number_atoms_solvent 268 _refine_hist.number_atoms_total 2205 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 37.60 # 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 0.005 0.019 ? 1972 ? 'X-RAY DIFFRACTION' r_bond_other_d 0.001 0.020 ? 1905 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.067 1.979 ? 2683 ? 'X-RAY DIFFRACTION' r_angle_other_deg 0.715 3.000 ? 4358 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 4.866 5.000 ? 245 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.599 23.929 ? 84 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 12.394 15.000 ? 322 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 15.634 15.000 ? 13 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.057 0.200 ? 319 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.004 0.021 ? 2229 ? 'X-RAY DIFFRACTION' r_gen_planes_other 0.001 0.020 ? 450 ? '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 1.800 _refine_ls_shell.d_res_low 1.847 _refine_ls_shell.number_reflns_R_work 1612 _refine_ls_shell.R_factor_R_work 0.251 _refine_ls_shell.percent_reflns_obs 98.62 _refine_ls_shell.R_factor_R_free 0.331 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 107 _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 4KWN _struct.title ;A new stabilizing water structure at the substrate binding site in ribosome inactivating protein from Momordica balsamina at 1.80 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 4KWN _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Ribosome inactivating protein, Hydrolase' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 10 ? ALA A 24 ? ASP A 10 ALA A 24 1 ? 15 HELX_P HELX_P2 2 SER A 42 ? GLY A 45 ? SER A 42 GLY A 45 5 ? 4 HELX_P HELX_P3 3 GLU A 85 ? SER A 92 ? GLU A 85 SER A 92 1 ? 8 HELX_P HELX_P4 4 ASN A 110 ? GLY A 119 ? ASN A 110 GLY A 119 1 ? 10 HELX_P HELX_P5 5 PRO A 121 ? ILE A 125 ? PRO A 121 ILE A 125 5 ? 5 HELX_P HELX_P6 6 GLY A 128 ? LEU A 140 ? GLY A 128 LEU A 140 1 ? 13 HELX_P HELX_P7 7 ASP A 143 ? THR A 158 ? ASP A 143 THR A 158 1 ? 16 HELX_P HELX_P8 8 THR A 158 ? PHE A 164 ? THR A 158 PHE A 164 1 ? 7 HELX_P HELX_P9 9 PHE A 164 ? ARG A 174 ? PHE A 164 ARG A 174 1 ? 11 HELX_P HELX_P10 10 SER A 182 ? 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 1.452 _struct_conn.pdbx_value_order ? # _struct_conn_type.id covale _struct_conn_type.criteria ? _struct_conn_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 2 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 VAL A 2 ? ARG A 5 ? VAL A 2 ARG A 5 A 2 TYR A 47 ? PHE A 53 ? TYR A 47 PHE A 53 A 3 THR A 59 ? ASP A 65 ? THR A 59 ASP A 65 A 4 ILE A 71 ? ALA A 76 ? ILE A 71 ALA A 76 A 5 THR A 79 ? PHE A 82 ? THR A 79 PHE A 82 A 6 ARG A 101 ? THR A 104 ? ARG A 101 THR A 104 B 1 LYS A 30 ? VAL A 31 ? LYS A 30 VAL A 31 B 2 ILE A 34 ? PRO A 35 ? ILE A 34 PRO A 35 C 1 VAL A 208 ? VAL A 216 ? VAL A 208 VAL A 216 C 2 ARG A 222 ? ASN A 227 ? ARG A 222 ASN A 227 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N VAL A 2 ? N VAL A 2 O HIS A 51 ? O HIS A 51 A 2 3 N LEU A 48 ? N LEU A 48 O VAL A 64 ? O VAL A 64 A 3 4 N ALA A 63 ? N ALA A 63 O MET A 72 ? O MET A 72 A 4 5 N ALA A 76 ? N ALA A 76 O THR A 79 ? O THR A 79 A 5 6 N SER A 80 ? N SER A 80 O ILE A 103 ? O ILE A 103 B 1 2 N VAL A 31 ? N VAL A 31 O ILE A 34 ? O ILE A 34 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 302' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 303' # 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 5 THR A 226 ? THR A 226 . ? 1_555 ? 2 AC1 5 ASN A 227 ? ASN A 227 . ? 1_555 ? 3 AC1 5 THR A 229 ? THR A 229 . ? 1_555 ? 4 AC1 5 HOH E . ? HOH A 534 . ? 1_555 ? 5 AC1 5 HOH E . ? HOH A 547 . ? 1_555 ? 6 AC2 5 LEU A 6 ? LEU A 6 . ? 1_555 ? 7 AC2 5 ALA A 9 ? ALA A 9 . ? 1_555 ? 8 AC2 5 ARG A 101 ? ARG A 101 . ? 3_555 ? 9 AC2 5 ALA A 175 ? ALA A 175 . ? 1_555 ? 10 AC2 5 HOH E . ? HOH A 488 . ? 1_555 ? 11 AC3 6 VAL A 233 ? VAL A 233 . ? 1_555 ? 12 AC3 6 THR A 234 ? THR A 234 . ? 1_555 ? 13 AC3 6 SER A 235 ? SER A 235 . ? 1_555 ? 14 AC3 6 ASN A 236 ? ASN A 236 . ? 1_555 ? 15 AC3 6 ILE A 237 ? ILE A 237 . ? 1_555 ? 16 AC3 6 GLN A 238 ? GLN A 238 . ? 1_555 ? # _database_PDB_matrix.entry_id 4KWN _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 4KWN _atom_sites.fract_transf_matrix[1][1] 0.007680 _atom_sites.fract_transf_matrix[1][2] 0.004434 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.008868 _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] 0.025096 _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 ? -4.328 28.812 -1.980 1.00 36.73 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -3.782 27.480 -1.578 1.00 36.12 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -2.284 27.577 -1.328 1.00 34.19 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -1.624 28.503 -1.800 1.00 34.76 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -4.040 26.422 -2.659 1.00 37.55 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -5.519 26.265 -3.001 1.00 39.16 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -6.351 27.034 -2.482 1.00 40.55 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -5.848 25.363 -3.800 1.00 41.02 ? 1 ASP A OD2 1 ATOM 9 N N . VAL A 1 2 ? -1.758 26.617 -0.580 1.00 31.56 ? 2 VAL A N 1 ATOM 10 C CA . VAL A 1 2 ? -0.318 26.476 -0.395 1.00 29.77 ? 2 VAL A CA 1 ATOM 11 C C . VAL A 1 2 ? 0.040 25.013 -0.599 1.00 28.13 ? 2 VAL A C 1 ATOM 12 O O . VAL A 1 2 ? -0.817 24.137 -0.464 1.00 26.62 ? 2 VAL A O 1 ATOM 13 C CB . VAL A 1 2 ? 0.144 26.946 1.000 1.00 29.99 ? 2 VAL A CB 1 ATOM 14 C CG1 . VAL A 1 2 ? -0.084 28.442 1.160 1.00 30.22 ? 2 VAL A CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? -0.556 26.169 2.107 1.00 30.08 ? 2 VAL A CG2 1 ATOM 16 N N . SER A 1 3 ? 1.303 24.763 -0.925 1.00 27.61 ? 3 SER A N 1 ATOM 17 C CA . SER A 1 3 ? 1.772 23.422 -1.253 1.00 26.89 ? 3 SER A CA 1 ATOM 18 C C . SER A 1 3 ? 3.118 23.103 -0.611 1.00 26.28 ? 3 SER A C 1 ATOM 19 O O . SER A 1 3 ? 3.935 23.997 -0.375 1.00 26.08 ? 3 SER A O 1 ATOM 20 C CB . SER A 1 3 ? 1.879 23.270 -2.773 1.00 27.51 ? 3 SER A CB 1 ATOM 21 O OG . SER A 1 3 ? 0.593 23.183 -3.359 1.00 28.81 ? 3 SER A OG 1 ATOM 22 N N . PHE A 1 4 ? 3.339 21.820 -0.329 1.00 24.70 ? 4 PHE A N 1 ATOM 23 C CA . PHE A 1 4 ? 4.638 21.334 0.139 1.00 24.06 ? 4 PHE A CA 1 ATOM 24 C C . PHE A 1 4 ? 4.894 19.923 -0.380 1.00 24.53 ? 4 PHE A C 1 ATOM 25 O O . PHE A 1 4 ? 4.040 19.042 -0.264 1.00 23.80 ? 4 PHE A O 1 ATOM 26 C CB . PHE A 1 4 ? 4.725 21.353 1.667 1.00 23.26 ? 4 PHE A CB 1 ATOM 27 C CG . PHE A 1 4 ? 6.065 20.918 2.214 1.00 22.86 ? 4 PHE A CG 1 ATOM 28 C CD1 . PHE A 1 4 ? 7.242 21.526 1.787 1.00 22.35 ? 4 PHE A CD1 1 ATOM 29 C CD2 . PHE A 1 4 ? 6.147 19.920 3.178 1.00 22.61 ? 4 PHE A CD2 1 ATOM 30 C CE1 . PHE A 1 4 ? 8.468 21.129 2.292 1.00 22.33 ? 4 PHE A CE1 1 ATOM 31 C CE2 . PHE A 1 4 ? 7.372 19.522 3.690 1.00 22.55 ? 4 PHE A CE2 1 ATOM 32 C CZ . PHE A 1 4 ? 8.534 20.128 3.247 1.00 22.40 ? 4 PHE A CZ 1 ATOM 33 N N . ARG A 1 5 ? 6.080 19.726 -0.945 1.00 25.39 ? 5 ARG A N 1 ATOM 34 C CA . ARG A 1 5 ? 6.487 18.440 -1.490 1.00 26.48 ? 5 ARG A CA 1 ATOM 35 C C . ARG A 1 5 ? 7.623 17.832 -0.675 1.00 25.59 ? 5 ARG A C 1 ATOM 36 O O . ARG A 1 5 ? 8.669 18.451 -0.499 1.00 24.88 ? 5 ARG A O 1 ATOM 37 C CB . ARG A 1 5 ? 6.897 18.615 -2.954 1.00 28.57 ? 5 ARG A CB 1 ATOM 38 C CG . ARG A 1 5 ? 5.703 18.895 -3.850 1.00 30.78 ? 5 ARG A CG 1 ATOM 39 C CD . ARG A 1 5 ? 6.070 19.395 -5.236 1.00 33.34 ? 5 ARG A CD 1 ATOM 40 N NE . ARG A 1 5 ? 4.882 19.450 -6.093 1.00 35.87 ? 5 ARG A NE 1 ATOM 41 C CZ . ARG A 1 5 ? 3.987 20.440 -6.118 1.00 37.43 ? 5 ARG A CZ 1 ATOM 42 N NH1 . ARG A 1 5 ? 4.113 21.512 -5.338 1.00 38.16 ? 5 ARG A NH1 1 ATOM 43 N NH2 . ARG A 1 5 ? 2.946 20.358 -6.942 1.00 38.56 ? 5 ARG A NH2 1 ATOM 44 N N . LEU A 1 6 ? 7.416 16.616 -0.180 1.00 24.99 ? 6 LEU A N 1 ATOM 45 C CA . LEU A 1 6 ? 8.447 15.932 0.595 1.00 25.23 ? 6 LEU A CA 1 ATOM 46 C C . LEU A 1 6 ? 9.573 15.413 -0.303 1.00 26.26 ? 6 LEU A C 1 ATOM 47 O O . LEU A 1 6 ? 10.701 15.262 0.155 1.00 27.09 ? 6 LEU A O 1 ATOM 48 C CB . LEU A 1 6 ? 7.857 14.796 1.445 1.00 25.06 ? 6 LEU A CB 1 ATOM 49 C CG . LEU A 1 6 ? 7.286 15.197 2.814 1.00 24.68 ? 6 LEU A CG 1 ATOM 50 C CD1 . LEU A 1 6 ? 8.395 15.658 3.750 1.00 24.40 ? 6 LEU A CD1 1 ATOM 51 C CD2 . LEU A 1 6 ? 6.215 16.272 2.704 1.00 24.79 ? 6 LEU A CD2 1 ATOM 52 N N . SER A 1 7 ? 9.272 15.146 -1.572 1.00 27.78 ? 7 SER A N 1 ATOM 53 C CA . SER A 1 7 ? 10.308 14.726 -2.515 1.00 28.75 ? 7 SER A CA 1 ATOM 54 C C . SER A 1 7 ? 11.285 15.870 -2.774 1.00 28.30 ? 7 SER A C 1 ATOM 55 O O . SER A 1 7 ? 10.921 16.895 -3.349 1.00 27.79 ? 7 SER A O 1 ATOM 56 C CB . SER A 1 7 ? 9.711 14.248 -3.837 1.00 29.84 ? 7 SER A CB 1 ATOM 57 O OG . SER A 1 7 ? 10.711 13.610 -4.621 1.00 31.19 ? 7 SER A OG 1 ATOM 58 N N . GLY A 1 8 ? 12.527 15.681 -2.337 1.00 28.06 ? 8 GLY A N 1 ATOM 59 C CA . GLY A 1 8 ? 13.559 16.701 -2.469 1.00 27.89 ? 8 GLY A CA 1 ATOM 60 C C . GLY A 1 8 ? 13.489 17.780 -1.405 1.00 27.90 ? 8 GLY A C 1 ATOM 61 O O . GLY A 1 8 ? 14.208 18.780 -1.488 1.00 28.28 ? 8 GLY A O 1 ATOM 62 N N . ALA A 1 9 ? 12.645 17.585 -0.392 1.00 27.03 ? 9 ALA A N 1 ATOM 63 C CA . ALA A 1 9 ? 12.482 18.586 0.658 1.00 26.89 ? 9 ALA A CA 1 ATOM 64 C C . ALA A 1 9 ? 13.756 18.751 1.474 1.00 26.87 ? 9 ALA A C 1 ATOM 65 O O . ALA A 1 9 ? 14.477 17.785 1.735 1.00 26.84 ? 9 ALA A O 1 ATOM 66 C CB . ALA A 1 9 ? 11.323 18.229 1.577 1.00 26.53 ? 9 ALA A CB 1 ATOM 67 N N . ASP A 1 10 ? 14.028 19.990 1.865 1.00 27.35 ? 10 ASP A N 1 ATOM 68 C CA . ASP A 1 10 ? 15.129 20.293 2.768 1.00 27.71 ? 10 ASP A CA 1 ATOM 69 C C . ASP A 1 10 ? 14.707 21.437 3.690 1.00 27.41 ? 10 ASP A C 1 ATOM 70 O O . ASP A 1 10 ? 13.588 21.947 3.566 1.00 26.65 ? 10 ASP A O 1 ATOM 71 C CB . ASP A 1 10 ? 16.407 20.605 1.970 1.00 28.62 ? 10 ASP A CB 1 ATOM 72 C CG . ASP A 1 10 ? 16.324 21.897 1.173 1.00 30.21 ? 10 ASP A CG 1 ATOM 73 O OD1 . ASP A 1 10 ? 15.237 22.510 1.076 1.00 30.85 ? 10 ASP A OD1 1 ATOM 74 O OD2 . ASP A 1 10 ? 17.373 22.297 0.622 1.00 32.52 ? 10 ASP A OD2 1 ATOM 75 N N . PRO A 1 11 ? 15.579 21.835 4.629 1.00 27.26 ? 11 PRO A N 1 ATOM 76 C CA . PRO A 1 11 ? 15.152 22.902 5.535 1.00 27.42 ? 11 PRO A CA 1 ATOM 77 C C . PRO A 1 11 ? 14.717 24.184 4.829 1.00 27.49 ? 11 PRO A C 1 ATOM 78 O O . PRO A 1 11 ? 13.824 24.881 5.321 1.00 26.21 ? 11 PRO A O 1 ATOM 79 C CB . PRO A 1 11 ? 16.391 23.141 6.393 1.00 27.66 ? 11 PRO A CB 1 ATOM 80 C CG . PRO A 1 11 ? 17.059 21.807 6.440 1.00 27.65 ? 11 PRO A CG 1 ATOM 81 C CD . PRO A 1 11 ? 16.837 21.208 5.079 1.00 27.34 ? 11 PRO A CD 1 ATOM 82 N N . SER A 1 12 ? 15.327 24.480 3.683 1.00 28.34 ? 12 SER A N 1 ATOM 83 C CA . SER A 1 12 ? 14.970 25.668 2.915 1.00 29.16 ? 12 SER A CA 1 ATOM 84 C C . SER A 1 12 ? 13.556 25.568 2.336 1.00 27.86 ? 12 SER A C 1 ATOM 85 O O . SER A 1 12 ? 12.753 26.478 2.525 1.00 27.51 ? 12 SER A O 1 ATOM 86 C CB . SER A 1 12 ? 15.985 25.924 1.798 1.00 30.63 ? 12 SER A CB 1 ATOM 87 O OG . SER A 1 12 ? 15.778 27.202 1.219 1.00 33.99 ? 12 SER A OG 1 ATOM 88 N N . SER A 1 13 ? 13.245 24.475 1.640 1.00 26.47 ? 13 SER A N 1 ATOM 89 C CA . SER A 1 13 ? 11.919 24.332 1.028 1.00 26.08 ? 13 SER A CA 1 ATOM 90 C C . SER A 1 13 ? 10.815 24.250 2.082 1.00 24.70 ? 13 SER A C 1 ATOM 91 O O . SER A 1 13 ? 9.709 24.750 1.874 1.00 24.53 ? 13 SER A O 1 ATOM 92 C CB . SER A 1 13 ? 11.850 23.125 0.088 1.00 26.62 ? 13 SER A CB 1 ATOM 93 O OG . SER A 1 13 ? 11.933 21.902 0.797 1.00 26.74 ? 13 SER A OG 1 ATOM 94 N N . TYR A 1 14 ? 11.118 23.624 3.212 1.00 23.56 ? 14 TYR A N 1 ATOM 95 C CA . TYR A 1 14 ? 10.175 23.588 4.325 1.00 22.76 ? 14 TYR A CA 1 ATOM 96 C C . TYR A 1 14 ? 9.929 25.000 4.861 1.00 23.06 ? 14 TYR A C 1 ATOM 97 O O . TYR A 1 14 ? 8.785 25.386 5.109 1.00 22.71 ? 14 TYR A O 1 ATOM 98 C CB . TYR A 1 14 ? 10.684 22.676 5.440 1.00 22.53 ? 14 TYR A CB 1 ATOM 99 C CG . TYR A 1 14 ? 9.789 22.683 6.653 1.00 21.66 ? 14 TYR A CG 1 ATOM 100 C CD1 . TYR A 1 14 ? 8.540 22.074 6.621 1.00 21.41 ? 14 TYR A CD1 1 ATOM 101 C CD2 . TYR A 1 14 ? 10.180 23.316 7.824 1.00 21.50 ? 14 TYR A CD2 1 ATOM 102 C CE1 . TYR A 1 14 ? 7.713 22.081 7.729 1.00 20.99 ? 14 TYR A CE1 1 ATOM 103 C CE2 . TYR A 1 14 ? 9.359 23.330 8.938 1.00 20.92 ? 14 TYR A CE2 1 ATOM 104 C CZ . TYR A 1 14 ? 8.124 22.715 8.879 1.00 20.75 ? 14 TYR A CZ 1 ATOM 105 O OH . TYR A 1 14 ? 7.310 22.731 9.980 1.00 20.14 ? 14 TYR A OH 1 ATOM 106 N N . GLY A 1 15 ? 11.002 25.769 5.044 1.00 23.31 ? 15 GLY A N 1 ATOM 107 C CA . GLY A 1 15 ? 10.878 27.164 5.471 1.00 23.91 ? 15 GLY A CA 1 ATOM 108 C C . GLY A 1 15 ? 10.010 27.991 4.535 1.00 24.82 ? 15 GLY A C 1 ATOM 109 O O . GLY A 1 15 ? 9.221 28.828 4.979 1.00 24.43 ? 15 GLY A O 1 ATOM 110 N N . MET A 1 16 ? 10.153 27.754 3.233 1.00 26.09 ? 16 MET A N 1 ATOM 111 C CA . MET A 1 16 ? 9.336 28.436 2.227 1.00 27.23 ? 16 MET A CA 1 ATOM 112 C C . MET A 1 16 ? 7.854 28.066 2.348 1.00 25.87 ? 16 MET A C 1 ATOM 113 O O . MET A 1 16 ? 6.983 28.920 2.201 1.00 25.10 ? 16 MET A O 1 ATOM 114 C CB . MET A 1 16 ? 9.842 28.117 0.817 1.00 30.43 ? 16 MET A CB 1 ATOM 115 C CG . MET A 1 16 ? 11.190 28.738 0.488 1.00 33.30 ? 16 MET A CG 1 ATOM 116 S SD . MET A 1 16 ? 11.595 28.620 -1.265 1.00 39.53 ? 16 MET A SD 1 ATOM 117 C CE . MET A 1 16 ? 12.168 26.930 -1.362 1.00 38.20 ? 16 MET A CE 1 ATOM 118 N N . PHE A 1 17 ? 7.575 26.794 2.617 1.00 23.96 ? 17 PHE A N 1 ATOM 119 C CA . PHE A 1 17 ? 6.199 26.331 2.832 1.00 22.83 ? 17 PHE A CA 1 ATOM 120 C C . PHE A 1 17 ? 5.558 26.995 4.056 1.00 22.19 ? 17 PHE A C 1 ATOM 121 O O . PHE A 1 17 ? 4.420 27.458 3.995 1.00 21.66 ? 17 PHE A O 1 ATOM 122 C CB . PHE A 1 17 ? 6.176 24.802 2.962 1.00 22.59 ? 17 PHE A CB 1 ATOM 123 C CG . PHE A 1 17 ? 4.962 24.259 3.670 1.00 22.31 ? 17 PHE A CG 1 ATOM 124 C CD1 . PHE A 1 17 ? 3.690 24.465 3.157 1.00 22.44 ? 17 PHE A CD1 1 ATOM 125 C CD2 . PHE A 1 17 ? 5.100 23.515 4.834 1.00 22.47 ? 17 PHE A CD2 1 ATOM 126 C CE1 . PHE A 1 17 ? 2.574 23.956 3.802 1.00 22.73 ? 17 PHE A CE1 1 ATOM 127 C CE2 . PHE A 1 17 ? 3.989 22.999 5.482 1.00 22.57 ? 17 PHE A CE2 1 ATOM 128 C CZ . PHE A 1 17 ? 2.724 23.222 4.966 1.00 22.61 ? 17 PHE A CZ 1 ATOM 129 N N . ILE A 1 18 ? 6.288 27.038 5.161 1.00 22.04 ? 18 ILE A N 1 ATOM 130 C CA . ILE A 1 18 ? 5.767 27.626 6.390 1.00 22.31 ? 18 ILE A CA 1 ATOM 131 C C . ILE A 1 18 ? 5.559 29.135 6.209 1.00 23.02 ? 18 ILE A C 1 ATOM 132 O O . ILE A 1 18 ? 4.585 29.693 6.721 1.00 22.76 ? 18 ILE A O 1 ATOM 133 C CB . ILE A 1 18 ? 6.672 27.300 7.597 1.00 22.45 ? 18 ILE A CB 1 ATOM 134 C CG1 . ILE A 1 18 ? 6.679 25.783 7.870 1.00 22.47 ? 18 ILE A CG1 1 ATOM 135 C CG2 . ILE A 1 18 ? 6.232 28.062 8.840 1.00 22.36 ? 18 ILE A CG2 1 ATOM 136 C CD1 . ILE A 1 18 ? 5.326 25.161 8.172 1.00 22.41 ? 18 ILE A CD1 1 ATOM 137 N N . LYS A 1 19 ? 6.455 29.783 5.466 1.00 24.04 ? 19 LYS A N 1 ATOM 138 C CA . LYS A 1 19 ? 6.261 31.190 5.092 1.00 25.53 ? 19 LYS A CA 1 ATOM 139 C C . LYS A 1 19 ? 4.974 31.368 4.284 1.00 25.29 ? 19 LYS A C 1 ATOM 140 O O . LYS A 1 19 ? 4.167 32.249 4.588 1.00 25.33 ? 19 LYS A O 1 ATOM 141 C CB . LYS A 1 19 ? 7.456 31.712 4.285 1.00 27.38 ? 19 LYS A CB 1 ATOM 142 C CG . LYS A 1 19 ? 7.329 33.175 3.859 1.00 29.48 ? 19 LYS A CG 1 ATOM 143 C CD . LYS A 1 19 ? 8.145 33.497 2.616 1.00 31.80 ? 19 LYS A CD 1 ATOM 144 C CE . LYS A 1 19 ? 9.638 33.363 2.851 1.00 33.18 ? 19 LYS A CE 1 ATOM 145 N NZ . LYS A 1 19 ? 10.421 33.635 1.611 1.00 34.80 ? 19 LYS A NZ 1 ATOM 146 N N . ASP A 1 20 ? 4.796 30.536 3.258 1.00 25.00 ? 20 ASP A N 1 ATOM 147 C CA . ASP A 1 20 ? 3.578 30.551 2.433 1.00 25.64 ? 20 ASP A CA 1 ATOM 148 C C . ASP A 1 20 ? 2.332 30.335 3.284 1.00 24.54 ? 20 ASP A C 1 ATOM 149 O O . ASP A 1 20 ? 1.316 31.004 3.096 1.00 23.81 ? 20 ASP A O 1 ATOM 150 C CB . ASP A 1 20 ? 3.622 29.454 1.363 1.00 26.61 ? 20 ASP A CB 1 ATOM 151 C CG . ASP A 1 20 ? 4.690 29.687 0.309 1.00 27.68 ? 20 ASP A CG 1 ATOM 152 O OD1 . ASP A 1 20 ? 5.265 30.795 0.238 1.00 28.55 ? 20 ASP A OD1 1 ATOM 153 O OD2 . ASP A 1 20 ? 4.958 28.740 -0.460 1.00 29.21 ? 20 ASP A OD2 1 ATOM 154 N N . LEU A 1 21 ? 2.411 29.383 4.212 1.00 24.31 ? 21 LEU A N 1 ATOM 155 C CA . LEU A 1 21 ? 1.288 29.085 5.095 1.00 23.97 ? 21 LEU A CA 1 ATOM 156 C C . LEU A 1 21 ? 0.903 30.314 5.925 1.00 23.61 ? 21 LEU A C 1 ATOM 157 O O . LEU A 1 21 ? -0.260 30.721 5.940 1.00 23.08 ? 21 LEU A O 1 ATOM 158 C CB . LEU A 1 21 ? 1.621 27.890 5.996 1.00 24.06 ? 21 LEU A CB 1 ATOM 159 C CG . LEU A 1 21 ? 0.607 27.488 7.072 1.00 24.60 ? 21 LEU A CG 1 ATOM 160 C CD1 . LEU A 1 21 ? -0.819 27.427 6.548 1.00 24.96 ? 21 LEU A CD1 1 ATOM 161 C CD2 . LEU A 1 21 ? 1.002 26.145 7.667 1.00 24.38 ? 21 LEU A CD2 1 ATOM 162 N N . ARG A 1 22 ? 1.883 30.914 6.594 1.00 23.90 ? 22 ARG A N 1 ATOM 163 C CA . ARG A 1 22 ? 1.656 32.151 7.350 1.00 24.23 ? 22 ARG A CA 1 ATOM 164 C C . ARG A 1 22 ? 1.042 33.254 6.488 1.00 25.13 ? 22 ARG A C 1 ATOM 165 O O . ARG A 1 22 ? 0.096 33.925 6.900 1.00 25.42 ? 22 ARG A O 1 ATOM 166 C CB . ARG A 1 22 ? 2.970 32.671 7.923 1.00 23.77 ? 22 ARG A CB 1 ATOM 167 C CG . ARG A 1 22 ? 3.501 31.872 9.095 1.00 23.30 ? 22 ARG A CG 1 ATOM 168 C CD . ARG A 1 22 ? 4.947 32.229 9.381 1.00 23.07 ? 22 ARG A CD 1 ATOM 169 N NE . ARG A 1 22 ? 5.499 31.375 10.429 1.00 22.56 ? 22 ARG A NE 1 ATOM 170 C CZ . ARG A 1 22 ? 6.782 31.037 10.543 1.00 22.85 ? 22 ARG A CZ 1 ATOM 171 N NH1 . ARG A 1 22 ? 7.692 31.481 9.676 1.00 23.76 ? 22 ARG A NH1 1 ATOM 172 N NH2 . ARG A 1 22 ? 7.160 30.240 11.535 1.00 22.39 ? 22 ARG A NH2 1 ATOM 173 N N . ASN A 1 23 ? 1.593 33.437 5.294 1.00 27.09 ? 23 ASN A N 1 ATOM 174 C CA . ASN A 1 23 ? 1.170 34.522 4.403 1.00 28.79 ? 23 ASN A CA 1 ATOM 175 C C . ASN A 1 23 ? -0.217 34.319 3.807 1.00 29.04 ? 23 ASN A C 1 ATOM 176 O O . ASN A 1 23 ? -0.856 35.280 3.375 1.00 29.85 ? 23 ASN A O 1 ATOM 177 C CB . ASN A 1 23 ? 2.188 34.722 3.274 1.00 29.81 ? 23 ASN A CB 1 ATOM 178 C CG . ASN A 1 23 ? 3.491 35.363 3.744 1.00 31.06 ? 23 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 23 ? 4.511 35.235 3.074 1.00 32.46 ? 23 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 23 ? 3.469 36.058 4.880 1.00 32.43 ? 23 ASN A ND2 1 ATOM 181 N N . ALA A 1 24 ? -0.682 33.073 3.789 1.00 28.29 ? 24 ALA A N 1 ATOM 182 C CA . ALA A 1 24 ? -2.025 32.759 3.313 1.00 28.21 ? 24 ALA A CA 1 ATOM 183 C C . ALA A 1 24 ? -3.110 33.086 4.347 1.00 28.52 ? 24 ALA A C 1 ATOM 184 O O . ALA A 1 24 ? -4.296 33.093 4.018 1.00 29.25 ? 24 ALA A O 1 ATOM 185 C CB . ALA A 1 24 ? -2.102 31.294 2.911 1.00 28.13 ? 24 ALA A CB 1 ATOM 186 N N . LEU A 1 25 ? -2.717 33.349 5.591 1.00 28.47 ? 25 LEU A N 1 ATOM 187 C CA . LEU A 1 25 ? -3.679 33.678 6.639 1.00 28.31 ? 25 LEU A CA 1 ATOM 188 C C . LEU A 1 25 ? -3.918 35.182 6.640 1.00 29.58 ? 25 LEU A C 1 ATOM 189 O O . LEU A 1 25 ? -2.965 35.952 6.776 1.00 29.00 ? 25 LEU A O 1 ATOM 190 C CB . LEU A 1 25 ? -3.168 33.223 8.004 1.00 28.18 ? 25 LEU A CB 1 ATOM 191 C CG . LEU A 1 25 ? -2.756 31.746 8.056 1.00 27.99 ? 25 LEU A CG 1 ATOM 192 C CD1 . LEU A 1 25 ? -2.026 31.423 9.347 1.00 27.62 ? 25 LEU A CD1 1 ATOM 193 C CD2 . LEU A 1 25 ? -3.964 30.835 7.879 1.00 28.21 ? 25 LEU A CD2 1 ATOM 194 N N . PRO A 1 26 ? -5.185 35.606 6.481 1.00 30.54 ? 26 PRO A N 1 ATOM 195 C CA . PRO A 1 26 ? -5.459 37.033 6.374 1.00 31.49 ? 26 PRO A CA 1 ATOM 196 C C . PRO A 1 26 ? -5.429 37.737 7.725 1.00 32.46 ? 26 PRO A C 1 ATOM 197 O O . PRO A 1 26 ? -5.726 37.129 8.755 1.00 31.92 ? 26 PRO A O 1 ATOM 198 C CB . PRO A 1 26 ? -6.872 37.065 5.792 1.00 31.24 ? 26 PRO A CB 1 ATOM 199 C CG . PRO A 1 26 ? -7.518 35.853 6.363 1.00 31.22 ? 26 PRO A CG 1 ATOM 200 C CD . PRO A 1 26 ? -6.429 34.813 6.458 1.00 30.89 ? 26 PRO A CD 1 ATOM 201 N N . HIS A 1 27 ? -5.059 39.013 7.707 1.00 33.62 ? 27 HIS A N 1 ATOM 202 C CA . HIS A 1 27 ? -5.131 39.862 8.889 1.00 35.22 ? 27 HIS A CA 1 ATOM 203 C C . HIS A 1 27 ? -5.271 41.310 8.436 1.00 35.76 ? 27 HIS A C 1 ATOM 204 O O . HIS A 1 27 ? -4.810 41.664 7.351 1.00 34.32 ? 27 HIS A O 1 ATOM 205 C CB . HIS A 1 27 ? -3.885 39.691 9.764 1.00 35.81 ? 27 HIS A CB 1 ATOM 206 C CG . HIS A 1 27 ? -2.628 40.222 9.147 1.00 37.03 ? 27 HIS A CG 1 ATOM 207 N ND1 . HIS A 1 27 ? -1.870 39.495 8.254 1.00 37.90 ? 27 HIS A ND1 1 ATOM 208 C CD2 . HIS A 1 27 ? -1.994 41.410 9.301 1.00 37.47 ? 27 HIS A CD2 1 ATOM 209 C CE1 . HIS A 1 27 ? -0.822 40.212 7.884 1.00 38.34 ? 27 HIS A CE1 1 ATOM 210 N NE2 . HIS A 1 27 ? -0.875 41.379 8.505 1.00 38.36 ? 27 HIS A NE2 1 ATOM 211 N N . THR A 1 28 ? -5.925 42.132 9.252 1.00 38.00 ? 28 THR A N 1 ATOM 212 C CA . THR A 1 28 ? -6.055 43.565 8.963 1.00 39.22 ? 28 THR A CA 1 ATOM 213 C C . THR A 1 28 ? -5.152 44.421 9.851 1.00 39.42 ? 28 THR A C 1 ATOM 214 O O . THR A 1 28 ? -4.882 45.577 9.521 1.00 39.54 ? 28 THR A O 1 ATOM 215 C CB . THR A 1 28 ? -7.511 44.055 9.102 1.00 40.54 ? 28 THR A CB 1 ATOM 216 O OG1 . THR A 1 28 ? -8.071 43.566 10.325 1.00 42.25 ? 28 THR A OG1 1 ATOM 217 C CG2 . THR A 1 28 ? -8.358 43.576 7.927 1.00 41.24 ? 28 THR A CG2 1 ATOM 218 N N . GLU A 1 29 ? -4.686 43.866 10.968 1.00 38.40 ? 29 GLU A N 1 ATOM 219 C CA . GLU A 1 29 ? -3.748 44.575 11.831 1.00 38.60 ? 29 GLU A CA 1 ATOM 220 C C . GLU A 1 29 ? -2.716 43.650 12.458 1.00 38.01 ? 29 GLU A C 1 ATOM 221 O O . GLU A 1 29 ? -2.903 42.430 12.531 1.00 37.26 ? 29 GLU A O 1 ATOM 222 C CB . GLU A 1 29 ? -4.494 45.325 12.938 1.00 39.42 ? 29 GLU A CB 1 ATOM 223 C CG . GLU A 1 29 ? -5.163 44.420 13.961 1.00 40.71 ? 29 GLU A CG 1 ATOM 224 C CD . GLU A 1 29 ? -6.134 45.162 14.858 1.00 41.97 ? 29 GLU A CD 1 ATOM 225 O OE1 . GLU A 1 29 ? -7.356 44.937 14.721 1.00 42.84 ? 29 GLU A OE1 1 ATOM 226 O OE2 . GLU A 1 29 ? -5.679 45.969 15.698 1.00 43.01 ? 29 GLU A OE2 1 ATOM 227 N N . LYS A 1 30 ? -1.622 44.259 12.903 1.00 36.04 ? 30 LYS A N 1 ATOM 228 C CA . LYS A 1 30 ? -0.623 43.583 13.704 1.00 35.53 ? 30 LYS A CA 1 ATOM 229 C C . LYS A 1 30 ? -0.661 44.158 15.105 1.00 35.26 ? 30 LYS A C 1 ATOM 230 O O . LYS A 1 30 ? -0.954 45.341 15.297 1.00 36.53 ? 30 LYS A O 1 ATOM 231 C CB . LYS A 1 30 ? 0.766 43.776 13.112 1.00 35.33 ? 30 LYS A CB 1 ATOM 232 C CG . LYS A 1 30 ? 0.869 43.371 11.655 1.00 35.48 ? 30 LYS A CG 1 ATOM 233 C CD . LYS A 1 30 ? 2.317 43.323 11.211 1.00 36.02 ? 30 LYS A CD 1 ATOM 234 C CE . LYS A 1 30 ? 2.421 42.930 9.751 1.00 36.58 ? 30 LYS A CE 1 ATOM 235 N NZ . LYS A 1 30 ? 3.835 42.886 9.289 1.00 37.11 ? 30 LYS A NZ 1 ATOM 236 N N . VAL A 1 31 ? -0.367 43.310 16.080 1.00 33.68 ? 31 VAL A N 1 ATOM 237 C CA . VAL A 1 31 ? -0.290 43.715 17.468 1.00 32.85 ? 31 VAL A CA 1 ATOM 238 C C . VAL A 1 31 ? 1.122 43.398 17.922 1.00 33.11 ? 31 VAL A C 1 ATOM 239 O O . VAL A 1 31 ? 1.548 42.240 17.886 1.00 31.85 ? 31 VAL A O 1 ATOM 240 C CB . VAL A 1 31 ? -1.325 42.970 18.324 1.00 32.39 ? 31 VAL A CB 1 ATOM 241 C CG1 . VAL A 1 31 ? -1.158 43.314 19.794 1.00 32.28 ? 31 VAL A CG1 1 ATOM 242 C CG2 . VAL A 1 31 ? -2.732 43.298 17.843 1.00 32.51 ? 31 VAL A CG2 1 ATOM 243 N N . TYR A 1 32 ? 1.848 44.440 18.319 1.00 32.55 ? 32 TYR A N 1 ATOM 244 C CA . TYR A 1 32 ? 3.276 44.343 18.597 1.00 32.81 ? 32 TYR A CA 1 ATOM 245 C C . TYR A 1 32 ? 4.019 43.682 17.433 1.00 32.33 ? 32 TYR A C 1 ATOM 246 O O . TYR A 1 32 ? 4.894 42.840 17.624 1.00 33.42 ? 32 TYR A O 1 ATOM 247 C CB . TYR A 1 32 ? 3.511 43.637 19.935 1.00 32.87 ? 32 TYR A CB 1 ATOM 248 C CG . TYR A 1 32 ? 3.028 44.474 21.096 1.00 33.15 ? 32 TYR A CG 1 ATOM 249 C CD1 . TYR A 1 32 ? 3.713 45.627 21.465 1.00 33.63 ? 32 TYR A CD1 1 ATOM 250 C CD2 . TYR A 1 32 ? 1.881 44.135 21.808 1.00 33.19 ? 32 TYR A CD2 1 ATOM 251 C CE1 . TYR A 1 32 ? 3.280 46.416 22.514 1.00 33.41 ? 32 TYR A CE1 1 ATOM 252 C CE2 . TYR A 1 32 ? 1.439 44.920 22.865 1.00 33.99 ? 32 TYR A CE2 1 ATOM 253 C CZ . TYR A 1 32 ? 2.146 46.060 23.210 1.00 33.77 ? 32 TYR A CZ 1 ATOM 254 O OH . TYR A 1 32 ? 1.728 46.850 24.254 1.00 35.19 ? 32 TYR A OH 1 ATOM 255 N N . ASN A 1 33 ? 3.635 44.086 16.223 1.00 31.86 ? 33 ASN A N 1 ATOM 256 C CA . ASN A 1 33 ? 4.251 43.641 14.976 1.00 32.37 ? 33 ASN A CA 1 ATOM 257 C C . ASN A 1 33 ? 3.993 42.170 14.614 1.00 31.32 ? 33 ASN A C 1 ATOM 258 O O . ASN A 1 33 ? 4.650 41.622 13.728 1.00 30.81 ? 33 ASN A O 1 ATOM 259 C CB . ASN A 1 33 ? 5.754 43.937 14.992 1.00 33.81 ? 33 ASN A CB 1 ATOM 260 C CG . ASN A 1 33 ? 6.330 44.105 13.602 1.00 35.46 ? 33 ASN A CG 1 ATOM 261 O OD1 . ASN A 1 33 ? 5.714 44.723 12.732 1.00 36.87 ? 33 ASN A OD1 1 ATOM 262 N ND2 . ASN A 1 33 ? 7.520 43.559 13.384 1.00 37.25 ? 33 ASN A ND2 1 ATOM 263 N N . ILE A 1 34 ? 3.022 41.553 15.287 1.00 30.37 ? 34 ILE A N 1 ATOM 264 C CA . ILE A 1 34 ? 2.611 40.175 15.015 1.00 28.77 ? 34 ILE A CA 1 ATOM 265 C C . ILE A 1 34 ? 1.210 40.197 14.414 1.00 27.97 ? 34 ILE A C 1 ATOM 266 O O . ILE A 1 34 ? 0.299 40.762 15.015 1.00 28.45 ? 34 ILE A O 1 ATOM 267 C CB . ILE A 1 34 ? 2.549 39.335 16.305 1.00 28.76 ? 34 ILE A CB 1 ATOM 268 C CG1 . ILE A 1 34 ? 3.879 39.379 17.052 1.00 28.43 ? 34 ILE A CG1 1 ATOM 269 C CG2 . ILE A 1 34 ? 2.182 37.889 15.992 1.00 28.59 ? 34 ILE A CG2 1 ATOM 270 C CD1 . ILE A 1 34 ? 3.724 39.273 18.550 1.00 28.21 ? 34 ILE A CD1 1 ATOM 271 N N . PRO A 1 35 ? 1.026 39.571 13.237 1.00 26.73 ? 35 PRO A N 1 ATOM 272 C CA . PRO A 1 35 ? -0.296 39.503 12.621 1.00 26.68 ? 35 PRO A CA 1 ATOM 273 C C . PRO A 1 35 ? -1.368 38.973 13.566 1.00 26.73 ? 35 PRO A C 1 ATOM 274 O O . PRO A 1 35 ? -1.162 37.958 14.248 1.00 25.89 ? 35 PRO A O 1 ATOM 275 C CB . PRO A 1 35 ? -0.092 38.539 11.452 1.00 26.73 ? 35 PRO A CB 1 ATOM 276 C CG . PRO A 1 35 ? 1.339 38.684 11.095 1.00 26.66 ? 35 PRO A CG 1 ATOM 277 C CD . PRO A 1 35 ? 2.063 38.977 12.375 1.00 26.62 ? 35 PRO A CD 1 ATOM 278 N N . LEU A 1 36 ? -2.494 39.679 13.600 1.00 26.40 ? 36 LEU A N 1 ATOM 279 C CA . LEU A 1 36 ? -3.639 39.311 14.413 1.00 27.19 ? 36 LEU A CA 1 ATOM 280 C C . LEU A 1 36 ? -4.636 38.603 13.518 1.00 27.23 ? 36 LEU A C 1 ATOM 281 O O . LEU A 1 36 ? -5.169 39.204 12.584 1.00 27.38 ? 36 LEU A O 1 ATOM 282 C CB . LEU A 1 36 ? -4.285 40.562 15.021 1.00 27.54 ? 36 LEU A CB 1 ATOM 283 C CG . LEU A 1 36 ? -5.578 40.342 15.810 1.00 27.49 ? 36 LEU A CG 1 ATOM 284 C CD1 . LEU A 1 36 ? -5.312 39.499 17.044 1.00 27.53 ? 36 LEU A CD1 1 ATOM 285 C CD2 . LEU A 1 36 ? -6.217 41.673 16.188 1.00 27.92 ? 36 LEU A CD2 1 ATOM 286 N N . LEU A 1 37 ? -4.895 37.328 13.790 1.00 27.02 ? 37 LEU A N 1 ATOM 287 C CA . LEU A 1 37 ? -5.868 36.589 12.992 1.00 27.61 ? 37 LEU A CA 1 ATOM 288 C C . LEU A 1 37 ? -7.246 37.201 13.177 1.00 28.77 ? 37 LEU A C 1 ATOM 289 O O . LEU A 1 37 ? -7.536 37.784 14.222 1.00 28.58 ? 37 LEU A O 1 ATOM 290 C CB . LEU A 1 37 ? -5.882 35.104 13.361 1.00 27.25 ? 37 LEU A CB 1 ATOM 291 C CG . LEU A 1 37 ? -4.566 34.381 13.055 1.00 27.18 ? 37 LEU A CG 1 ATOM 292 C CD1 . LEU A 1 37 ? -4.582 32.970 13.621 1.00 27.19 ? 37 LEU A CD1 1 ATOM 293 C CD2 . LEU A 1 37 ? -4.272 34.349 11.562 1.00 27.21 ? 37 LEU A CD2 1 ATOM 294 N N . LEU A 1 38 ? -8.080 37.069 12.151 1.00 30.85 ? 38 LEU A N 1 ATOM 295 C CA . LEU A 1 38 ? -9.389 37.716 12.132 1.00 32.58 ? 38 LEU A CA 1 ATOM 296 C C . LEU A 1 38 ? -10.348 37.059 13.124 1.00 33.65 ? 38 LEU A C 1 ATOM 297 O O . LEU A 1 38 ? -10.231 35.861 13.398 1.00 32.74 ? 38 LEU A O 1 ATOM 298 C CB . LEU A 1 38 ? -9.994 37.666 10.726 1.00 33.00 ? 38 LEU A CB 1 ATOM 299 C CG . LEU A 1 38 ? -9.209 38.344 9.600 1.00 33.92 ? 38 LEU A CG 1 ATOM 300 C CD1 . LEU A 1 38 ? -9.829 38.032 8.247 1.00 34.09 ? 38 LEU A CD1 1 ATOM 301 C CD2 . LEU A 1 38 ? -9.128 39.849 9.811 1.00 34.58 ? 38 LEU A CD2 1 ATOM 302 N N . PRO A 1 39 ? -11.305 37.840 13.663 1.00 34.73 ? 39 PRO A N 1 ATOM 303 C CA . PRO A 1 39 ? -12.323 37.283 14.553 1.00 35.53 ? 39 PRO A CA 1 ATOM 304 C C . PRO A 1 39 ? -13.165 36.221 13.860 1.00 36.10 ? 39 PRO A C 1 ATOM 305 O O . PRO A 1 39 ? -13.506 35.209 14.470 1.00 35.33 ? 39 PRO A O 1 ATOM 306 C CB . PRO A 1 39 ? -13.201 38.494 14.896 1.00 35.41 ? 39 PRO A CB 1 ATOM 307 C CG . PRO A 1 39 ? -12.368 39.683 14.593 1.00 35.25 ? 39 PRO A CG 1 ATOM 308 C CD . PRO A 1 39 ? -11.521 39.279 13.429 1.00 35.20 ? 39 PRO A CD 1 ATOM 309 N N . SER A 1 40 ? -13.499 36.464 12.596 1.00 38.01 ? 40 SER A N 1 ATOM 310 C CA . SER A 1 40 ? -14.284 35.520 11.818 1.00 39.23 ? 40 SER A CA 1 ATOM 311 C C . SER A 1 40 ? -14.186 35.800 10.326 1.00 39.78 ? 40 SER A C 1 ATOM 312 O O . SER A 1 40 ? -13.817 36.898 9.904 1.00 39.86 ? 40 SER A O 1 ATOM 313 C CB . SER A 1 40 ? -15.751 35.553 12.253 1.00 40.15 ? 40 SER A CB 1 ATOM 314 O OG . SER A 1 40 ? -16.312 36.839 12.062 1.00 41.84 ? 40 SER A OG 1 ATOM 315 N N . VAL A 1 41 ? -14.507 34.776 9.544 1.00 39.86 ? 41 VAL A N 1 ATOM 316 C CA . VAL A 1 41 ? -14.587 34.861 8.096 1.00 40.35 ? 41 VAL A CA 1 ATOM 317 C C . VAL A 1 41 ? -15.798 34.033 7.685 1.00 42.00 ? 41 VAL A C 1 ATOM 318 O O . VAL A 1 41 ? -16.005 32.934 8.204 1.00 42.46 ? 41 VAL A O 1 ATOM 319 C CB . VAL A 1 41 ? -13.339 34.271 7.411 1.00 39.89 ? 41 VAL A CB 1 ATOM 320 C CG1 . VAL A 1 41 ? -13.466 34.361 5.896 1.00 39.37 ? 41 VAL A CG1 1 ATOM 321 C CG2 . VAL A 1 41 ? -12.071 34.972 7.884 1.00 39.66 ? 41 VAL A CG2 1 ATOM 322 N N . SER A 1 42 ? -16.592 34.558 6.756 1.00 43.11 ? 42 SER A N 1 ATOM 323 C CA . SER A 1 42 ? -17.822 33.888 6.337 1.00 43.34 ? 42 SER A CA 1 ATOM 324 C C . SER A 1 42 ? -17.614 33.067 5.076 1.00 42.67 ? 42 SER A C 1 ATOM 325 O O . SER A 1 42 ? -16.881 33.467 4.170 1.00 42.77 ? 42 SER A O 1 ATOM 326 C CB . SER A 1 42 ? -18.953 34.898 6.119 1.00 44.12 ? 42 SER A CB 1 ATOM 327 O OG . SER A 1 42 ? -19.692 35.083 7.313 1.00 44.82 ? 42 SER A OG 1 ATOM 328 N N . GLY A 1 43 ? -18.270 31.911 5.038 1.00 41.96 ? 43 GLY A N 1 ATOM 329 C CA . GLY A 1 43 ? -18.288 31.066 3.856 1.00 41.01 ? 43 GLY A CA 1 ATOM 330 C C . GLY A 1 43 ? -16.999 30.303 3.637 1.00 39.95 ? 43 GLY A C 1 ATOM 331 O O . GLY A 1 43 ? -16.244 30.045 4.575 1.00 39.36 ? 43 GLY A O 1 ATOM 332 N N . ALA A 1 44 ? -16.754 29.952 2.378 1.00 39.03 ? 44 ALA A N 1 ATOM 333 C CA . ALA A 1 44 ? -15.601 29.146 1.992 1.00 38.23 ? 44 ALA A CA 1 ATOM 334 C C . ALA A 1 44 ? -14.268 29.854 2.227 1.00 37.56 ? 44 ALA A C 1 ATOM 335 O O . ALA A 1 44 ? -13.247 29.196 2.424 1.00 36.85 ? 44 ALA A O 1 ATOM 336 C CB . ALA A 1 44 ? -15.719 28.732 0.534 1.00 38.63 ? 44 ALA A CB 1 ATOM 337 N N . GLY A 1 45 ? -14.277 31.188 2.213 1.00 36.37 ? 45 GLY A N 1 ATOM 338 C CA . GLY A 1 45 ? -13.072 31.977 2.483 1.00 35.03 ? 45 GLY A CA 1 ATOM 339 C C . GLY A 1 45 ? -12.441 31.721 3.845 1.00 33.87 ? 45 GLY A C 1 ATOM 340 O O . GLY A 1 45 ? -11.284 32.080 4.077 1.00 33.79 ? 45 GLY A O 1 ATOM 341 N N . ARG A 1 46 ? -13.201 31.103 4.745 1.00 32.52 ? 46 ARG A N 1 ATOM 342 C CA . ARG A 1 46 ? -12.700 30.715 6.059 1.00 32.22 ? 46 ARG A CA 1 ATOM 343 C C . ARG A 1 46 ? -11.595 29.653 6.004 1.00 30.94 ? 46 ARG A C 1 ATOM 344 O O . ARG A 1 46 ? -10.779 29.564 6.923 1.00 30.84 ? 46 ARG A O 1 ATOM 345 C CB . ARG A 1 46 ? -13.858 30.198 6.913 1.00 33.54 ? 46 ARG A CB 1 ATOM 346 C CG . ARG A 1 46 ? -13.493 29.924 8.359 1.00 34.82 ? 46 ARG A CG 1 ATOM 347 C CD . ARG A 1 46 ? -14.709 29.561 9.186 1.00 37.01 ? 46 ARG A CD 1 ATOM 348 N NE . ARG A 1 46 ? -14.349 29.511 10.598 1.00 39.71 ? 46 ARG A NE 1 ATOM 349 C CZ . ARG A 1 46 ? -14.474 30.519 11.460 1.00 40.93 ? 46 ARG A CZ 1 ATOM 350 N NH1 . ARG A 1 46 ? -14.998 31.688 11.093 1.00 41.94 ? 46 ARG A NH1 1 ATOM 351 N NH2 . ARG A 1 46 ? -14.086 30.345 12.717 1.00 41.70 ? 46 ARG A NH2 1 ATOM 352 N N . TYR A 1 47 ? -11.569 28.855 4.937 1.00 29.90 ? 47 TYR A N 1 ATOM 353 C CA . TYR A 1 47 ? -10.703 27.675 4.878 1.00 29.05 ? 47 TYR A CA 1 ATOM 354 C C . TYR A 1 47 ? -9.596 27.782 3.837 1.00 29.05 ? 47 TYR A C 1 ATOM 355 O O . TYR A 1 47 ? -9.848 28.063 2.665 1.00 30.89 ? 47 TYR A O 1 ATOM 356 C CB . TYR A 1 47 ? -11.557 26.431 4.633 1.00 28.49 ? 47 TYR A CB 1 ATOM 357 C CG . TYR A 1 47 ? -12.727 26.400 5.573 1.00 27.68 ? 47 TYR A CG 1 ATOM 358 C CD1 . TYR A 1 47 ? -12.543 26.122 6.922 1.00 27.18 ? 47 TYR A CD1 1 ATOM 359 C CD2 . TYR A 1 47 ? -14.011 26.703 5.129 1.00 27.68 ? 47 TYR A CD2 1 ATOM 360 C CE1 . TYR A 1 47 ? -13.611 26.117 7.801 1.00 27.19 ? 47 TYR A CE1 1 ATOM 361 C CE2 . TYR A 1 47 ? -15.084 26.700 6.000 1.00 27.30 ? 47 TYR A CE2 1 ATOM 362 C CZ . TYR A 1 47 ? -14.879 26.411 7.331 1.00 27.36 ? 47 TYR A CZ 1 ATOM 363 O OH . TYR A 1 47 ? -15.949 26.408 8.192 1.00 28.40 ? 47 TYR A OH 1 ATOM 364 N N . LEU A 1 48 ? -8.366 27.564 4.294 1.00 28.19 ? 48 LEU A N 1 ATOM 365 C CA . LEU A 1 48 ? -7.200 27.464 3.430 1.00 28.44 ? 48 LEU A CA 1 ATOM 366 C C . LEU A 1 48 ? -6.976 25.996 3.089 1.00 27.97 ? 48 LEU A C 1 ATOM 367 O O . LEU A 1 48 ? -7.107 25.131 3.959 1.00 27.36 ? 48 LEU A O 1 ATOM 368 C CB . LEU A 1 48 ? -5.970 28.031 4.147 1.00 29.26 ? 48 LEU A CB 1 ATOM 369 C CG . LEU A 1 48 ? -4.572 27.717 3.609 1.00 30.31 ? 48 LEU A CG 1 ATOM 370 C CD1 . LEU A 1 48 ? -4.364 28.251 2.200 1.00 30.75 ? 48 LEU A CD1 1 ATOM 371 C CD2 . LEU A 1 48 ? -3.539 28.302 4.556 1.00 30.71 ? 48 LEU A CD2 1 ATOM 372 N N . LEU A 1 49 ? -6.643 25.724 1.829 1.00 27.65 ? 49 LEU A N 1 ATOM 373 C CA . LEU A 1 49 ? -6.292 24.375 1.397 1.00 27.17 ? 49 LEU A CA 1 ATOM 374 C C . LEU A 1 49 ? -4.780 24.223 1.295 1.00 26.65 ? 49 LEU A C 1 ATOM 375 O O . LEU A 1 49 ? -4.117 24.973 0.572 1.00 26.73 ? 49 LEU A O 1 ATOM 376 C CB . LEU A 1 49 ? -6.939 24.050 0.056 1.00 27.65 ? 49 LEU A CB 1 ATOM 377 C CG . LEU A 1 49 ? -8.453 24.245 -0.005 1.00 28.35 ? 49 LEU A CG 1 ATOM 378 C CD1 . LEU A 1 49 ? -8.946 23.897 -1.399 1.00 28.86 ? 49 LEU A CD1 1 ATOM 379 C CD2 . LEU A 1 49 ? -9.170 23.414 1.052 1.00 28.49 ? 49 LEU A CD2 1 ATOM 380 N N . MET A 1 50 ? -4.249 23.253 2.036 1.00 25.85 ? 50 MET A N 1 ATOM 381 C CA . MET A 1 50 ? -2.838 22.905 1.987 1.00 25.76 ? 50 MET A CA 1 ATOM 382 C C . MET A 1 50 ? -2.681 21.626 1.194 1.00 25.84 ? 50 MET A C 1 ATOM 383 O O . MET A 1 50 ? -3.209 20.587 1.597 1.00 25.28 ? 50 MET A O 1 ATOM 384 C CB . MET A 1 50 ? -2.290 22.616 3.381 1.00 25.93 ? 50 MET A CB 1 ATOM 385 C CG . MET A 1 50 ? -2.334 23.747 4.379 1.00 26.76 ? 50 MET A CG 1 ATOM 386 S SD . MET A 1 50 ? -1.150 23.363 5.687 1.00 27.32 ? 50 MET A SD 1 ATOM 387 C CE . MET A 1 50 ? -1.936 21.970 6.504 1.00 26.26 ? 50 MET A CE 1 ATOM 388 N N . HIS A 1 51 ? -1.929 21.686 0.102 1.00 25.77 ? 51 HIS A N 1 ATOM 389 C CA . HIS A 1 51 ? -1.649 20.502 -0.702 1.00 26.08 ? 51 HIS A CA 1 ATOM 390 C C . HIS A 1 51 ? -0.308 19.920 -0.295 1.00 25.49 ? 51 HIS A C 1 ATOM 391 O O . HIS A 1 51 ? 0.737 20.547 -0.494 1.00 25.43 ? 51 HIS A O 1 ATOM 392 C CB . HIS A 1 51 ? -1.648 20.853 -2.189 1.00 27.59 ? 51 HIS A CB 1 ATOM 393 C CG . HIS A 1 51 ? -2.871 21.593 -2.624 1.00 28.53 ? 51 HIS A CG 1 ATOM 394 N ND1 . HIS A 1 51 ? -4.100 20.984 -2.750 1.00 29.30 ? 51 HIS A ND1 1 ATOM 395 C CD2 . HIS A 1 51 ? -3.060 22.896 -2.936 1.00 29.52 ? 51 HIS A CD2 1 ATOM 396 C CE1 . HIS A 1 51 ? -4.993 21.879 -3.134 1.00 29.93 ? 51 HIS A CE1 1 ATOM 397 N NE2 . HIS A 1 51 ? -4.388 23.047 -3.252 1.00 30.08 ? 51 HIS A NE2 1 ATOM 398 N N . LEU A 1 52 ? -0.348 18.722 0.284 1.00 24.39 ? 52 LEU A N 1 ATOM 399 C CA . LEU A 1 52 ? 0.849 18.044 0.761 1.00 24.17 ? 52 LEU A CA 1 ATOM 400 C C . LEU A 1 52 ? 1.113 16.806 -0.070 1.00 25.02 ? 52 LEU A C 1 ATOM 401 O O . LEU A 1 52 ? 0.196 16.025 -0.333 1.00 25.50 ? 52 LEU A O 1 ATOM 402 C CB . LEU A 1 52 ? 0.678 17.647 2.222 1.00 23.55 ? 52 LEU A CB 1 ATOM 403 C CG . LEU A 1 52 ? 0.330 18.799 3.162 1.00 22.97 ? 52 LEU A CG 1 ATOM 404 C CD1 . LEU A 1 52 ? 0.075 18.266 4.559 1.00 22.66 ? 52 LEU A CD1 1 ATOM 405 C CD2 . LEU A 1 52 ? 1.432 19.852 3.175 1.00 22.98 ? 52 LEU A CD2 1 ATOM 406 N N . PHE A 1 53 ? 2.370 16.629 -0.467 1.00 24.89 ? 53 PHE A N 1 ATOM 407 C CA . PHE A 1 53 ? 2.774 15.502 -1.295 1.00 25.52 ? 53 PHE A CA 1 ATOM 408 C C . PHE A 1 53 ? 3.827 14.691 -0.570 1.00 25.06 ? 53 PHE A C 1 ATOM 409 O O . PHE A 1 53 ? 4.847 15.234 -0.136 1.00 23.80 ? 53 PHE A O 1 ATOM 410 C CB . PHE A 1 53 ? 3.357 15.978 -2.620 1.00 25.83 ? 53 PHE A CB 1 ATOM 411 C CG . PHE A 1 53 ? 2.382 16.717 -3.482 1.00 26.46 ? 53 PHE A CG 1 ATOM 412 C CD1 . PHE A 1 53 ? 2.052 18.034 -3.201 1.00 26.90 ? 53 PHE A CD1 1 ATOM 413 C CD2 . PHE A 1 53 ? 1.804 16.103 -4.586 1.00 27.33 ? 53 PHE A CD2 1 ATOM 414 C CE1 . PHE A 1 53 ? 1.154 18.722 -3.996 1.00 27.37 ? 53 PHE A CE1 1 ATOM 415 C CE2 . PHE A 1 53 ? 0.904 16.787 -5.386 1.00 27.49 ? 53 PHE A CE2 1 ATOM 416 C CZ . PHE A 1 53 ? 0.580 18.098 -5.091 1.00 27.58 ? 53 PHE A CZ 1 ATOM 417 N N . ASN A 1 54 ? 3.585 13.390 -0.446 1.00 24.60 ? 54 ASN A N 1 ATOM 418 C CA . ASN A 1 54 ? 4.574 12.510 0.139 1.00 24.72 ? 54 ASN A CA 1 ATOM 419 C C . ASN A 1 54 ? 5.714 12.299 -0.853 1.00 25.58 ? 54 ASN A C 1 ATOM 420 O O . ASN A 1 54 ? 5.652 12.750 -1.999 1.00 25.34 ? 54 ASN A O 1 ATOM 421 C CB . ASN A 1 54 ? 3.947 11.192 0.635 1.00 24.47 ? 54 ASN A CB 1 ATOM 422 C CG . ASN A 1 54 ? 3.560 10.239 -0.482 1.00 24.39 ? 54 ASN A CG 1 ATOM 423 O OD1 . ASN A 1 54 ? 3.807 10.488 -1.658 1.00 23.79 ? 54 ASN A OD1 1 ATOM 424 N ND2 . ASN A 1 54 ? 2.947 9.121 -0.102 1.00 24.61 ? 54 ASN A ND2 1 ATOM 425 N N . TYR A 1 55 ? 6.759 11.629 -0.397 1.00 27.37 ? 55 TYR A N 1 ATOM 426 C CA . TYR A 1 55 ? 7.958 11.428 -1.198 1.00 29.15 ? 55 TYR A CA 1 ATOM 427 C C . TYR A 1 55 ? 7.667 10.799 -2.569 1.00 29.66 ? 55 TYR A C 1 ATOM 428 O O . TYR A 1 55 ? 8.317 11.137 -3.563 1.00 29.75 ? 55 TYR A O 1 ATOM 429 C CB . TYR A 1 55 ? 8.939 10.573 -0.410 1.00 29.89 ? 55 TYR A CB 1 ATOM 430 C CG . TYR A 1 55 ? 10.200 10.265 -1.157 1.00 31.75 ? 55 TYR A CG 1 ATOM 431 C CD1 . TYR A 1 55 ? 11.257 11.170 -1.181 1.00 32.55 ? 55 TYR A CD1 1 ATOM 432 C CD2 . TYR A 1 55 ? 10.337 9.066 -1.842 1.00 32.37 ? 55 TYR A CD2 1 ATOM 433 C CE1 . TYR A 1 55 ? 12.424 10.881 -1.868 1.00 33.76 ? 55 TYR A CE1 1 ATOM 434 C CE2 . TYR A 1 55 ? 11.493 8.769 -2.530 1.00 33.30 ? 55 TYR A CE2 1 ATOM 435 C CZ . TYR A 1 55 ? 12.532 9.675 -2.538 1.00 33.99 ? 55 TYR A CZ 1 ATOM 436 O OH . TYR A 1 55 ? 13.671 9.360 -3.227 1.00 35.42 ? 55 TYR A OH 1 ATOM 437 N N . ASP A 1 56 ? 6.681 9.905 -2.617 1.00 30.06 ? 56 ASP A N 1 ATOM 438 C CA . ASP A 1 56 ? 6.282 9.245 -3.866 1.00 31.14 ? 56 ASP A CA 1 ATOM 439 C C . ASP A 1 56 ? 5.357 10.082 -4.755 1.00 30.57 ? 56 ASP A C 1 ATOM 440 O O . ASP A 1 56 ? 5.003 9.649 -5.851 1.00 31.00 ? 56 ASP A O 1 ATOM 441 C CB . ASP A 1 56 ? 5.622 7.895 -3.566 1.00 32.55 ? 56 ASP A CB 1 ATOM 442 C CG . ASP A 1 56 ? 6.610 6.862 -3.065 1.00 34.15 ? 56 ASP A CG 1 ATOM 443 O OD1 . ASP A 1 56 ? 7.816 6.993 -3.358 1.00 34.37 ? 56 ASP A OD1 1 ATOM 444 O OD2 . ASP A 1 56 ? 6.178 5.914 -2.376 1.00 36.15 ? 56 ASP A OD2 1 ATOM 445 N N . GLY A 1 57 ? 4.968 11.268 -4.295 1.00 29.35 ? 57 GLY A N 1 ATOM 446 C CA . GLY A 1 57 ? 4.155 12.173 -5.105 1.00 28.95 ? 57 GLY A CA 1 ATOM 447 C C . GLY A 1 57 ? 2.656 12.006 -4.919 1.00 28.81 ? 57 GLY A C 1 ATOM 448 O O . GLY A 1 57 ? 1.870 12.662 -5.607 1.00 29.15 ? 57 GLY A O 1 ATOM 449 N N . ASN A 1 58 ? 2.256 11.120 -4.009 1.00 28.54 ? 58 ASN A N 1 ATOM 450 C CA . ASN A 1 58 ? 0.857 11.014 -3.605 1.00 29.45 ? 58 ASN A CA 1 ATOM 451 C C . ASN A 1 58 ? 0.504 12.195 -2.726 1.00 28.69 ? 58 ASN A C 1 ATOM 452 O O . ASN A 1 58 ? 1.367 12.743 -2.039 1.00 28.43 ? 58 ASN A O 1 ATOM 453 C CB . ASN A 1 58 ? 0.594 9.713 -2.851 1.00 30.90 ? 58 ASN A CB 1 ATOM 454 C CG . ASN A 1 58 ? 0.578 8.500 -3.760 1.00 32.74 ? 58 ASN A CG 1 ATOM 455 O OD1 . ASN A 1 58 ? 0.390 8.611 -4.972 1.00 36.32 ? 58 ASN A OD1 1 ATOM 456 N ND2 . ASN A 1 58 ? 0.758 7.327 -3.172 1.00 34.38 ? 58 ASN A ND2 1 ATOM 457 N N . THR A 1 59 ? -0.764 12.579 -2.735 1.00 28.33 ? 59 THR A N 1 ATOM 458 C CA . THR A 1 59 ? -1.156 13.844 -2.141 1.00 27.99 ? 59 THR A CA 1 ATOM 459 C C . THR A 1 59 ? -2.441 13.788 -1.331 1.00 26.21 ? 59 THR A C 1 ATOM 460 O O . THR A 1 59 ? -3.357 13.022 -1.632 1.00 25.28 ? 59 THR A O 1 ATOM 461 C CB . THR A 1 59 ? -1.299 14.938 -3.225 1.00 29.10 ? 59 THR A CB 1 ATOM 462 O OG1 . THR A 1 59 ? -1.642 16.188 -2.614 1.00 30.16 ? 59 THR A OG1 1 ATOM 463 C CG2 . THR A 1 59 ? -2.355 14.564 -4.268 1.00 29.38 ? 59 THR A CG2 1 ATOM 464 N N . ILE A 1 60 ? -2.475 14.609 -0.288 1.00 24.66 ? 60 ILE A N 1 ATOM 465 C CA . ILE A 1 60 ? -3.707 14.933 0.407 1.00 23.41 ? 60 ILE A CA 1 ATOM 466 C C . ILE A 1 60 ? -3.874 16.447 0.379 1.00 23.32 ? 60 ILE A C 1 ATOM 467 O O . ILE A 1 60 ? -2.899 17.188 0.221 1.00 22.86 ? 60 ILE A O 1 ATOM 468 C CB . ILE A 1 60 ? -3.713 14.396 1.856 1.00 23.37 ? 60 ILE A CB 1 ATOM 469 C CG1 . ILE A 1 60 ? -2.629 15.069 2.717 1.00 22.81 ? 60 ILE A CG1 1 ATOM 470 C CG2 . ILE A 1 60 ? -3.521 12.889 1.838 1.00 23.30 ? 60 ILE A CG2 1 ATOM 471 C CD1 . ILE A 1 60 ? -2.708 14.736 4.195 1.00 23.26 ? 60 ILE A CD1 1 ATOM 472 N N . THR A 1 61 ? -5.115 16.897 0.503 1.00 22.63 ? 61 THR A N 1 ATOM 473 C CA . THR A 1 61 ? -5.399 18.311 0.663 1.00 22.57 ? 61 THR A CA 1 ATOM 474 C C . THR A 1 61 ? -5.992 18.505 2.046 1.00 21.92 ? 61 THR A C 1 ATOM 475 O O . THR A 1 61 ? -6.973 17.857 2.395 1.00 21.32 ? 61 THR A O 1 ATOM 476 C CB . THR A 1 61 ? -6.362 18.820 -0.419 1.00 23.09 ? 61 THR A CB 1 ATOM 477 O OG1 . THR A 1 61 ? -5.783 18.581 -1.707 1.00 23.80 ? 61 THR A OG1 1 ATOM 478 C CG2 . THR A 1 61 ? -6.617 20.315 -0.257 1.00 23.29 ? 61 THR A CG2 1 ATOM 479 N N . VAL A 1 62 ? -5.381 19.388 2.832 1.00 21.09 ? 62 VAL A N 1 ATOM 480 C CA . VAL A 1 62 ? -5.798 19.626 4.208 1.00 20.74 ? 62 VAL A CA 1 ATOM 481 C C . VAL A 1 62 ? -6.520 20.969 4.304 1.00 21.21 ? 62 VAL A C 1 ATOM 482 O O . VAL A 1 62 ? -6.006 21.984 3.832 1.00 21.84 ? 62 VAL A O 1 ATOM 483 C CB . VAL A 1 62 ? -4.583 19.640 5.155 1.00 20.59 ? 62 VAL A CB 1 ATOM 484 C CG1 . VAL A 1 62 ? -5.023 19.792 6.601 1.00 20.51 ? 62 VAL A CG1 1 ATOM 485 C CG2 . VAL A 1 62 ? -3.760 18.370 4.984 1.00 20.35 ? 62 VAL A CG2 1 ATOM 486 N N . ALA A 1 63 ? -7.701 20.967 4.918 1.00 20.66 ? 63 ALA A N 1 ATOM 487 C CA . ALA A 1 63 ? -8.478 22.195 5.114 1.00 20.82 ? 63 ALA A CA 1 ATOM 488 C C . ALA A 1 63 ? -8.160 22.820 6.468 1.00 20.63 ? 63 ALA A C 1 ATOM 489 O O . ALA A 1 63 ? -8.256 22.159 7.504 1.00 19.79 ? 63 ALA A O 1 ATOM 490 C CB . ALA A 1 63 ? -9.968 21.913 4.998 1.00 21.20 ? 63 ALA A CB 1 ATOM 491 N N . VAL A 1 64 ? -7.786 24.099 6.448 1.00 20.48 ? 64 VAL A N 1 ATOM 492 C CA . VAL A 1 64 ? -7.351 24.816 7.642 1.00 20.69 ? 64 VAL A CA 1 ATOM 493 C C . VAL A 1 64 ? -8.210 26.068 7.844 1.00 21.66 ? 64 VAL A C 1 ATOM 494 O O . VAL A 1 64 ? -8.361 26.863 6.921 1.00 22.14 ? 64 VAL A O 1 ATOM 495 C CB . VAL A 1 64 ? -5.877 25.251 7.513 1.00 20.36 ? 64 VAL A CB 1 ATOM 496 C CG1 . VAL A 1 64 ? -5.422 25.985 8.765 1.00 20.59 ? 64 VAL A CG1 1 ATOM 497 C CG2 . VAL A 1 64 ? -4.977 24.049 7.259 1.00 20.28 ? 64 VAL A CG2 1 ATOM 498 N N . ASP A 1 65 ? -8.770 26.224 9.040 1.00 22.56 ? 65 ASP A N 1 ATOM 499 C CA . ASP A 1 65 ? -9.542 27.418 9.401 1.00 23.90 ? 65 ASP A CA 1 ATOM 500 C C . ASP A 1 65 ? -8.562 28.582 9.578 1.00 24.38 ? 65 ASP A C 1 ATOM 501 O O . ASP A 1 65 ? -7.661 28.513 10.415 1.00 24.11 ? 65 ASP A O 1 ATOM 502 C CB . ASP A 1 65 ? -10.336 27.149 10.685 1.00 24.52 ? 65 ASP A CB 1 ATOM 503 C CG . ASP A 1 65 ? -11.192 28.338 11.127 1.00 25.46 ? 65 ASP A CG 1 ATOM 504 O OD1 . ASP A 1 65 ? -10.768 29.502 10.968 1.00 25.66 ? 65 ASP A OD1 1 ATOM 505 O OD2 . ASP A 1 65 ? -12.290 28.096 11.660 1.00 26.66 ? 65 ASP A OD2 1 ATOM 506 N N . VAL A 1 66 ? -8.729 29.644 8.788 1.00 25.60 ? 66 VAL A N 1 ATOM 507 C CA . VAL A 1 66 ? -7.716 30.711 8.745 1.00 26.52 ? 66 VAL A CA 1 ATOM 508 C C . VAL A 1 66 ? -7.777 31.668 9.940 1.00 26.75 ? 66 VAL A C 1 ATOM 509 O O . VAL A 1 66 ? -6.872 32.481 10.117 1.00 28.06 ? 66 VAL A O 1 ATOM 510 C CB . VAL A 1 66 ? -7.722 31.512 7.414 1.00 26.73 ? 66 VAL A CB 1 ATOM 511 C CG1 . VAL A 1 66 ? -7.545 30.581 6.222 1.00 26.69 ? 66 VAL A CG1 1 ATOM 512 C CG2 . VAL A 1 66 ? -8.975 32.369 7.260 1.00 27.12 ? 66 VAL A CG2 1 ATOM 513 N N . THR A 1 67 ? -8.817 31.556 10.763 1.00 26.97 ? 67 THR A N 1 ATOM 514 C CA . THR A 1 67 ? -8.952 32.387 11.957 1.00 27.60 ? 67 THR A CA 1 ATOM 515 C C . THR A 1 67 ? -8.178 31.819 13.149 1.00 26.68 ? 67 THR A C 1 ATOM 516 O O . THR A 1 67 ? -7.847 32.553 14.071 1.00 25.85 ? 67 THR A O 1 ATOM 517 C CB . THR A 1 67 ? -10.433 32.577 12.369 1.00 28.69 ? 67 THR A CB 1 ATOM 518 O OG1 . THR A 1 67 ? -10.967 31.348 12.885 1.00 29.66 ? 67 THR A OG1 1 ATOM 519 C CG2 . THR A 1 67 ? -11.270 33.053 11.185 1.00 29.46 ? 67 THR A CG2 1 ATOM 520 N N . ASN A 1 68 ? -7.897 30.514 13.139 1.00 25.64 ? 68 ASN A N 1 ATOM 521 C CA . ASN A 1 68 ? -7.228 29.872 14.277 1.00 24.32 ? 68 ASN A CA 1 ATOM 522 C C . ASN A 1 68 ? -6.160 28.818 13.925 1.00 23.29 ? 68 ASN A C 1 ATOM 523 O O . ASN A 1 68 ? -5.560 28.233 14.822 1.00 22.35 ? 68 ASN A O 1 ATOM 524 C CB . ASN A 1 68 ? -8.278 29.252 15.204 1.00 24.88 ? 68 ASN A CB 1 ATOM 525 C CG . ASN A 1 68 ? -9.229 28.320 14.472 1.00 25.39 ? 68 ASN A CG 1 ATOM 526 O OD1 . ASN A 1 68 ? -8.886 27.751 13.436 1.00 24.48 ? 68 ASN A OD1 1 ATOM 527 N ND2 . ASN A 1 68 ? -10.431 28.158 15.014 1.00 26.14 ? 68 ASN A ND2 1 ATOM 528 N N . VAL A 1 69 ? -5.924 28.611 12.630 1.00 22.81 ? 69 VAL A N 1 ATOM 529 C CA . VAL A 1 69 ? -4.999 27.585 12.103 1.00 22.82 ? 69 VAL A CA 1 ATOM 530 C C . VAL A 1 69 ? -5.333 26.156 12.569 1.00 23.29 ? 69 VAL A C 1 ATOM 531 O O . VAL A 1 69 ? -4.448 25.290 12.616 1.00 22.44 ? 69 VAL A O 1 ATOM 532 C CB . VAL A 1 69 ? -3.501 27.903 12.393 1.00 22.54 ? 69 VAL A CB 1 ATOM 533 C CG1 . VAL A 1 69 ? -2.647 27.507 11.196 1.00 22.65 ? 69 VAL A CG1 1 ATOM 534 C CG2 . VAL A 1 69 ? -3.276 29.383 12.695 1.00 23.05 ? 69 VAL A CG2 1 ATOM 535 N N . TYR A 1 70 ? -6.603 25.904 12.892 1.00 23.71 ? 70 TYR A N 1 ATOM 536 C CA . TYR A 1 70 ? -7.044 24.556 13.264 1.00 24.63 ? 70 TYR A CA 1 ATOM 537 C C . TYR A 1 70 ? -7.337 23.762 12.000 1.00 23.67 ? 70 TYR A C 1 ATOM 538 O O . TYR A 1 70 ? -8.015 24.242 11.095 1.00 22.78 ? 70 TYR A O 1 ATOM 539 C CB . TYR A 1 70 ? -8.303 24.581 14.145 1.00 26.76 ? 70 TYR A CB 1 ATOM 540 C CG . TYR A 1 70 ? -8.163 25.236 15.511 1.00 29.22 ? 70 TYR A CG 1 ATOM 541 C CD1 . TYR A 1 70 ? -9.296 25.646 16.218 1.00 31.63 ? 70 TYR A CD1 1 ATOM 542 C CD2 . TYR A 1 70 ? -6.917 25.457 16.095 1.00 30.47 ? 70 TYR A CD2 1 ATOM 543 C CE1 . TYR A 1 70 ? -9.190 26.253 17.461 1.00 32.29 ? 70 TYR A CE1 1 ATOM 544 C CE2 . TYR A 1 70 ? -6.801 26.062 17.339 1.00 31.82 ? 70 TYR A CE2 1 ATOM 545 C CZ . TYR A 1 70 ? -7.939 26.459 18.017 1.00 33.08 ? 70 TYR A CZ 1 ATOM 546 O OH . TYR A 1 70 ? -7.831 27.058 19.252 1.00 35.15 ? 70 TYR A OH 1 ATOM 547 N N . ILE A 1 71 ? -6.813 22.544 11.932 1.00 22.48 ? 71 ILE A N 1 ATOM 548 C CA . ILE A 1 71 ? -7.116 21.659 10.821 1.00 22.33 ? 71 ILE A CA 1 ATOM 549 C C . ILE A 1 71 ? -8.534 21.127 11.028 1.00 21.95 ? 71 ILE A C 1 ATOM 550 O O . ILE A 1 71 ? -8.869 20.672 12.119 1.00 21.59 ? 71 ILE A O 1 ATOM 551 C CB . ILE A 1 71 ? -6.097 20.503 10.729 1.00 22.48 ? 71 ILE A CB 1 ATOM 552 C CG1 . ILE A 1 71 ? -4.735 21.057 10.287 1.00 22.91 ? 71 ILE A CG1 1 ATOM 553 C CG2 . ILE A 1 71 ? -6.592 19.429 9.770 1.00 22.49 ? 71 ILE A CG2 1 ATOM 554 C CD1 . ILE A 1 71 ? -3.598 20.055 10.311 1.00 23.50 ? 71 ILE A CD1 1 ATOM 555 N N . MET A 1 72 ? -9.358 21.212 9.988 1.00 22.03 ? 72 MET A N 1 ATOM 556 C CA . MET A 1 72 ? -10.759 20.784 10.057 1.00 22.89 ? 72 MET A CA 1 ATOM 557 C C . MET A 1 72 ? -10.953 19.382 9.482 1.00 21.93 ? 72 MET A C 1 ATOM 558 O O . MET A 1 72 ? -11.775 18.599 9.971 1.00 21.03 ? 72 MET A O 1 ATOM 559 C CB . MET A 1 72 ? -11.643 21.761 9.277 1.00 24.45 ? 72 MET A CB 1 ATOM 560 C CG . MET A 1 72 ? -11.734 23.163 9.870 1.00 25.71 ? 72 MET A CG 1 ATOM 561 S SD . MET A 1 72 ? -12.587 23.195 11.456 1.00 28.69 ? 72 MET A SD 1 ATOM 562 C CE . MET A 1 72 ? -11.230 23.198 12.620 1.00 28.34 ? 72 MET A CE 1 ATOM 563 N N . GLY A 1 73 ? -10.200 19.083 8.433 1.00 21.29 ? 73 GLY A N 1 ATOM 564 C CA . GLY A 1 73 ? -10.343 17.833 7.707 1.00 20.85 ? 73 GLY A CA 1 ATOM 565 C C . GLY A 1 73 ? -9.372 17.780 6.554 1.00 20.89 ? 73 GLY A C 1 ATOM 566 O O . GLY A 1 73 ? -8.534 18.669 6.394 1.00 20.98 ? 73 GLY A O 1 ATOM 567 N N . TYR A 1 74 ? -9.478 16.734 5.746 1.00 20.69 ? 74 TYR A N 1 ATOM 568 C CA . TYR A 1 74 ? -8.600 16.573 4.606 1.00 20.92 ? 74 TYR A CA 1 ATOM 569 C C . TYR A 1 74 ? -9.251 15.671 3.571 1.00 21.61 ? 74 TYR A C 1 ATOM 570 O O . TYR A 1 74 ? -10.188 14.930 3.874 1.00 21.71 ? 74 TYR A O 1 ATOM 571 C CB . TYR A 1 74 ? -7.239 16.004 5.035 1.00 20.88 ? 74 TYR A CB 1 ATOM 572 C CG . TYR A 1 74 ? -7.360 14.695 5.768 1.00 20.45 ? 74 TYR A CG 1 ATOM 573 C CD1 . TYR A 1 74 ? -7.592 14.671 7.137 1.00 20.60 ? 74 TYR A CD1 1 ATOM 574 C CD2 . TYR A 1 74 ? -7.279 13.480 5.090 1.00 20.68 ? 74 TYR A CD2 1 ATOM 575 C CE1 . TYR A 1 74 ? -7.726 13.479 7.817 1.00 20.30 ? 74 TYR A CE1 1 ATOM 576 C CE2 . TYR A 1 74 ? -7.417 12.280 5.764 1.00 20.44 ? 74 TYR A CE2 1 ATOM 577 C CZ . TYR A 1 74 ? -7.636 12.287 7.128 1.00 20.49 ? 74 TYR A CZ 1 ATOM 578 O OH . TYR A 1 74 ? -7.778 11.112 7.823 1.00 20.46 ? 74 TYR A OH 1 ATOM 579 N N . LEU A 1 75 ? -8.738 15.766 2.353 1.00 22.63 ? 75 LEU A N 1 ATOM 580 C CA . LEU A 1 75 ? -9.188 14.981 1.220 1.00 23.55 ? 75 LEU A CA 1 ATOM 581 C C . LEU A 1 75 ? -8.065 14.063 0.773 1.00 24.31 ? 75 LEU A C 1 ATOM 582 O O . LEU A 1 75 ? -6.938 14.513 0.545 1.00 24.15 ? 75 LEU A O 1 ATOM 583 C CB . LEU A 1 75 ? -9.558 15.912 0.071 1.00 24.34 ? 75 LEU A CB 1 ATOM 584 C CG . LEU A 1 75 ? -9.960 15.278 -1.262 1.00 24.53 ? 75 LEU A CG 1 ATOM 585 C CD1 . LEU A 1 75 ? -11.297 14.571 -1.123 1.00 25.03 ? 75 LEU A CD1 1 ATOM 586 C CD2 . LEU A 1 75 ? -10.027 16.340 -2.345 1.00 25.11 ? 75 LEU A CD2 1 ATOM 587 N N . ALA A 1 76 ? -8.384 12.780 0.642 1.00 24.72 ? 76 ALA A N 1 ATOM 588 C CA . ALA A 1 76 ? -7.441 11.781 0.158 1.00 26.04 ? 76 ALA A CA 1 ATOM 589 C C . ALA A 1 76 ? -8.112 11.012 -0.978 1.00 27.43 ? 76 ALA A C 1 ATOM 590 O O . ALA A 1 76 ? -9.053 10.251 -0.748 1.00 26.56 ? 76 ALA A O 1 ATOM 591 C CB . ALA A 1 76 ? -7.038 10.847 1.286 1.00 26.11 ? 76 ALA A CB 1 ATOM 592 N N . LEU A 1 77 ? -7.624 11.241 -2.199 1.00 29.66 ? 77 LEU A N 1 ATOM 593 C CA . LEU A 1 77 ? -8.251 10.757 -3.438 1.00 31.27 ? 77 LEU A CA 1 ATOM 594 C C . LEU A 1 77 ? -9.708 11.238 -3.568 1.00 30.71 ? 77 LEU A C 1 ATOM 595 O O . LEU A 1 77 ? -9.942 12.410 -3.867 1.00 31.15 ? 77 LEU A O 1 ATOM 596 C CB . LEU A 1 77 ? -8.107 9.230 -3.585 1.00 32.77 ? 77 LEU A CB 1 ATOM 597 C CG . LEU A 1 77 ? -8.684 8.563 -4.847 1.00 34.32 ? 77 LEU A CG 1 ATOM 598 C CD1 . LEU A 1 77 ? -8.426 9.364 -6.118 1.00 34.27 ? 77 LEU A CD1 1 ATOM 599 C CD2 . LEU A 1 77 ? -8.140 7.150 -4.996 1.00 35.05 ? 77 LEU A CD2 1 ATOM 600 N N . THR A 1 78 ? -10.679 10.357 -3.337 1.00 30.14 ? 78 THR A N 1 ATOM 601 C CA . THR A 1 78 ? -12.089 10.706 -3.506 1.00 29.20 ? 78 THR A CA 1 ATOM 602 C C . THR A 1 78 ? -12.839 10.644 -2.180 1.00 27.62 ? 78 THR A C 1 ATOM 603 O O . THR A 1 78 ? -14.068 10.717 -2.158 1.00 28.85 ? 78 THR A O 1 ATOM 604 C CB . THR A 1 78 ? -12.781 9.770 -4.519 1.00 29.34 ? 78 THR A CB 1 ATOM 605 O OG1 . THR A 1 78 ? -12.663 8.411 -4.079 1.00 29.02 ? 78 THR A OG1 1 ATOM 606 C CG2 . THR A 1 78 ? -12.160 9.915 -5.902 1.00 29.65 ? 78 THR A CG2 1 ATOM 607 N N . THR A 1 79 ? -12.108 10.514 -1.075 1.00 26.09 ? 79 THR A N 1 ATOM 608 C CA . THR A 1 79 ? -12.727 10.467 0.239 1.00 24.49 ? 79 THR A CA 1 ATOM 609 C C . THR A 1 79 ? -12.299 11.667 1.064 1.00 23.66 ? 79 THR A C 1 ATOM 610 O O . THR A 1 79 ? -11.103 11.957 1.174 1.00 22.89 ? 79 THR A O 1 ATOM 611 C CB . THR A 1 79 ? -12.358 9.182 0.999 1.00 24.73 ? 79 THR A CB 1 ATOM 612 O OG1 . THR A 1 79 ? -12.720 8.038 0.217 1.00 24.70 ? 79 THR A OG1 1 ATOM 613 C CG2 . THR A 1 79 ? -13.088 9.116 2.337 1.00 24.78 ? 79 THR A CG2 1 ATOM 614 N N . SER A 1 80 ? -13.280 12.355 1.642 1.00 22.57 ? 80 SER A N 1 ATOM 615 C CA . SER A 1 80 ? -13.016 13.426 2.592 1.00 22.01 ? 80 SER A CA 1 ATOM 616 C C . SER A 1 80 ? -13.125 12.892 4.018 1.00 21.62 ? 80 SER A C 1 ATOM 617 O O . SER A 1 80 ? -13.899 11.972 4.295 1.00 21.52 ? 80 SER A O 1 ATOM 618 C CB . SER A 1 80 ? -13.981 14.600 2.375 1.00 22.13 ? 80 SER A CB 1 ATOM 619 O OG . SER A 1 80 ? -15.298 14.284 2.792 1.00 22.27 ? 80 SER A OG 1 ATOM 620 N N . TYR A 1 81 ? -12.333 13.472 4.915 1.00 21.31 ? 81 TYR A N 1 ATOM 621 C CA . TYR A 1 81 ? -12.320 13.104 6.325 1.00 21.08 ? 81 TYR A CA 1 ATOM 622 C C . TYR A 1 81 ? -12.389 14.377 7.170 1.00 20.96 ? 81 TYR A C 1 ATOM 623 O O . TYR A 1 81 ? -11.610 15.299 6.940 1.00 20.79 ? 81 TYR A O 1 ATOM 624 C CB . TYR A 1 81 ? -11.028 12.354 6.661 1.00 21.68 ? 81 TYR A CB 1 ATOM 625 C CG . TYR A 1 81 ? -10.793 11.108 5.833 1.00 22.45 ? 81 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 81 ? -10.226 11.186 4.562 1.00 22.86 ? 81 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 81 ? -11.143 9.856 6.316 1.00 23.11 ? 81 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 81 ? -10.009 10.048 3.802 1.00 23.26 ? 81 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 81 ? -10.933 8.714 5.562 1.00 23.55 ? 81 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 81 ? -10.368 8.815 4.309 1.00 23.34 ? 81 TYR A CZ 1 ATOM 631 O OH . TYR A 1 81 ? -10.161 7.679 3.565 1.00 25.24 ? 81 TYR A OH 1 ATOM 632 N N . PHE A 1 82 ? -13.290 14.418 8.150 1.00 20.98 ? 82 PHE A N 1 ATOM 633 C CA . PHE A 1 82 ? -13.442 15.582 9.035 1.00 21.42 ? 82 PHE A CA 1 ATOM 634 C C . PHE A 1 82 ? -13.462 15.159 10.495 1.00 22.02 ? 82 PHE A C 1 ATOM 635 O O . PHE A 1 82 ? -13.982 14.090 10.829 1.00 23.08 ? 82 PHE A O 1 ATOM 636 C CB . PHE A 1 82 ? -14.736 16.335 8.706 1.00 21.63 ? 82 PHE A CB 1 ATOM 637 C CG . PHE A 1 82 ? -14.728 16.986 7.358 1.00 21.28 ? 82 PHE A CG 1 ATOM 638 C CD1 . PHE A 1 82 ? -14.250 18.280 7.203 1.00 21.73 ? 82 PHE A CD1 1 ATOM 639 C CD2 . PHE A 1 82 ? -15.196 16.312 6.245 1.00 21.38 ? 82 PHE A CD2 1 ATOM 640 C CE1 . PHE A 1 82 ? -14.235 18.882 5.956 1.00 21.79 ? 82 PHE A CE1 1 ATOM 641 C CE2 . PHE A 1 82 ? -15.187 16.908 4.996 1.00 21.39 ? 82 PHE A CE2 1 ATOM 642 C CZ . PHE A 1 82 ? -14.705 18.197 4.851 1.00 21.63 ? 82 PHE A CZ 1 ATOM 643 N N . PHE A 1 83 ? -12.900 15.998 11.364 1.00 22.11 ? 83 PHE A N 1 ATOM 644 C CA . PHE A 1 83 ? -12.966 15.768 12.803 1.00 22.43 ? 83 PHE A CA 1 ATOM 645 C C . PHE A 1 83 ? -14.410 15.784 13.282 1.00 23.61 ? 83 PHE A C 1 ATOM 646 O O . PHE A 1 83 ? -15.264 16.463 12.704 1.00 23.27 ? 83 PHE A O 1 ATOM 647 C CB . PHE A 1 83 ? -12.152 16.813 13.576 1.00 21.98 ? 83 PHE A CB 1 ATOM 648 C CG . PHE A 1 83 ? -10.666 16.606 13.488 1.00 21.88 ? 83 PHE A CG 1 ATOM 649 C CD1 . PHE A 1 83 ? -10.095 15.432 13.963 1.00 21.44 ? 83 PHE A CD1 1 ATOM 650 C CD2 . PHE A 1 83 ? -9.839 17.578 12.943 1.00 21.84 ? 83 PHE A CD2 1 ATOM 651 C CE1 . PHE A 1 83 ? -8.731 15.227 13.884 1.00 21.80 ? 83 PHE A CE1 1 ATOM 652 C CE2 . PHE A 1 83 ? -8.470 17.385 12.872 1.00 21.67 ? 83 PHE A CE2 1 ATOM 653 C CZ . PHE A 1 83 ? -7.915 16.209 13.342 1.00 21.70 ? 83 PHE A CZ 1 ATOM 654 N N . ASN A 1 84 ? -14.668 15.023 14.338 1.00 24.79 ? 84 ASN A N 1 ATOM 655 C CA . ASN A 1 84 ? -15.994 14.930 14.925 1.00 25.99 ? 84 ASN A CA 1 ATOM 656 C C . ASN A 1 84 ? -16.185 16.100 15.890 1.00 26.09 ? 84 ASN A C 1 ATOM 657 O O . ASN A 1 84 ? -16.087 15.947 17.104 1.00 26.24 ? 84 ASN A O 1 ATOM 658 C CB . ASN A 1 84 ? -16.145 13.576 15.629 1.00 26.01 ? 84 ASN A CB 1 ATOM 659 C CG . ASN A 1 84 ? -17.571 13.272 16.056 1.00 26.33 ? 84 ASN A CG 1 ATOM 660 O OD1 . ASN A 1 84 ? -17.787 12.461 16.955 1.00 28.15 ? 84 ASN A OD1 1 ATOM 661 N ND2 . ASN A 1 84 ? -18.545 13.896 15.411 1.00 25.92 ? 84 ASN A ND2 1 ATOM 662 N N . GLU A 1 85 ? -16.421 17.280 15.321 1.00 27.65 ? 85 GLU A N 1 ATOM 663 C CA . GLU A 1 85 ? -16.609 18.511 16.096 1.00 28.15 ? 85 GLU A CA 1 ATOM 664 C C . GLU A 1 85 ? -17.408 19.503 15.238 1.00 27.72 ? 85 GLU A C 1 ATOM 665 O O . GLU A 1 85 ? -17.342 19.446 14.008 1.00 27.04 ? 85 GLU A O 1 ATOM 666 C CB . GLU A 1 85 ? -15.252 19.095 16.525 1.00 29.36 ? 85 GLU A CB 1 ATOM 667 C CG . GLU A 1 85 ? -14.366 19.529 15.362 1.00 31.00 ? 85 GLU A CG 1 ATOM 668 C CD . GLU A 1 85 ? -12.924 19.847 15.741 1.00 32.62 ? 85 GLU A CD 1 ATOM 669 O OE1 . GLU A 1 85 ? -12.420 19.358 16.770 1.00 32.86 ? 85 GLU A OE1 1 ATOM 670 O OE2 . GLU A 1 85 ? -12.272 20.592 14.978 1.00 37.19 ? 85 GLU A OE2 1 ATOM 671 N N . PRO A 1 86 ? -18.187 20.398 15.874 1.00 28.06 ? 86 PRO A N 1 ATOM 672 C CA . PRO A 1 86 ? -19.077 21.266 15.079 1.00 28.17 ? 86 PRO A CA 1 ATOM 673 C C . PRO A 1 86 ? -18.386 22.163 14.046 1.00 27.95 ? 86 PRO A C 1 ATOM 674 O O . PRO A 1 86 ? -18.933 22.381 12.966 1.00 28.51 ? 86 PRO A O 1 ATOM 675 C CB . PRO A 1 86 ? -19.785 22.116 16.138 1.00 28.13 ? 86 PRO A CB 1 ATOM 676 C CG . PRO A 1 86 ? -19.707 21.318 17.389 1.00 28.34 ? 86 PRO A CG 1 ATOM 677 C CD . PRO A 1 86 ? -18.428 20.537 17.321 1.00 27.97 ? 86 PRO A CD 1 ATOM 678 N N . ALA A 1 87 ? -17.207 22.680 14.374 1.00 28.28 ? 87 ALA A N 1 ATOM 679 C CA . ALA A 1 87 ? -16.456 23.523 13.442 1.00 27.94 ? 87 ALA A CA 1 ATOM 680 C C . ALA A 1 87 ? -16.054 22.756 12.182 1.00 27.70 ? 87 ALA A C 1 ATOM 681 O O . ALA A 1 87 ? -16.052 23.314 11.085 1.00 26.80 ? 87 ALA A O 1 ATOM 682 C CB . ALA A 1 87 ? -15.228 24.106 14.122 1.00 28.43 ? 87 ALA A CB 1 ATOM 683 N N . ALA A 1 88 ? -15.717 21.478 12.339 1.00 27.43 ? 88 ALA A N 1 ATOM 684 C CA . ALA A 1 88 ? -15.340 20.647 11.197 1.00 27.88 ? 88 ALA A CA 1 ATOM 685 C C . ALA A 1 88 ? -16.560 20.256 10.371 1.00 28.33 ? 88 ALA A C 1 ATOM 686 O O . ALA A 1 88 ? -16.493 20.245 9.141 1.00 27.91 ? 88 ALA A O 1 ATOM 687 C CB . ALA A 1 88 ? -14.586 19.408 11.655 1.00 27.79 ? 88 ALA A CB 1 ATOM 688 N N . ASP A 1 89 ? -17.671 19.933 11.031 1.00 29.44 ? 89 ASP A N 1 ATOM 689 C CA . ASP A 1 89 ? -18.904 19.650 10.299 1.00 31.05 ? 89 ASP A CA 1 ATOM 690 C C . ASP A 1 89 ? -19.313 20.876 9.485 1.00 30.29 ? 89 ASP A C 1 ATOM 691 O O . ASP A 1 89 ? -19.715 20.747 8.332 1.00 29.92 ? 89 ASP A O 1 ATOM 692 C CB . ASP A 1 89 ? -20.045 19.223 11.225 1.00 32.88 ? 89 ASP A CB 1 ATOM 693 C CG . ASP A 1 89 ? -21.359 19.037 10.475 1.00 34.88 ? 89 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 89 ? -21.418 18.193 9.553 1.00 37.32 ? 89 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 89 ? -22.327 19.755 10.791 1.00 37.55 ? 89 ASP A OD2 1 ATOM 696 N N . LEU A 1 90 ? -19.195 22.062 10.081 1.00 30.88 ? 90 LEU A N 1 ATOM 697 C CA . LEU A 1 90 ? -19.444 23.305 9.348 1.00 30.86 ? 90 LEU A CA 1 ATOM 698 C C . LEU A 1 90 ? -18.508 23.426 8.147 1.00 29.34 ? 90 LEU A C 1 ATOM 699 O O . LEU A 1 90 ? -18.950 23.749 7.047 1.00 29.03 ? 90 LEU A O 1 ATOM 700 C CB . LEU A 1 90 ? -19.293 24.529 10.260 1.00 32.36 ? 90 LEU A CB 1 ATOM 701 C CG . LEU A 1 90 ? -19.336 25.898 9.562 1.00 34.00 ? 90 LEU A CG 1 ATOM 702 C CD1 . LEU A 1 90 ? -20.652 26.112 8.827 1.00 35.12 ? 90 LEU A CD1 1 ATOM 703 C CD2 . LEU A 1 90 ? -19.098 27.015 10.563 1.00 34.45 ? 90 LEU A CD2 1 ATOM 704 N N . ALA A 1 91 ? -17.220 23.164 8.353 1.00 27.97 ? 91 ALA A N 1 ATOM 705 C CA . ALA A 1 91 ? -16.258 23.195 7.250 1.00 27.20 ? 91 ALA A CA 1 ATOM 706 C C . ALA A 1 91 ? -16.670 22.254 6.121 1.00 27.12 ? 91 ALA A C 1 ATOM 707 O O . ALA A 1 91 ? -16.486 22.570 4.944 1.00 26.59 ? 91 ALA A O 1 ATOM 708 C CB . ALA A 1 91 ? -14.860 22.849 7.743 1.00 27.00 ? 91 ALA A CB 1 ATOM 709 N N . SER A 1 92 ? -17.253 21.110 6.477 1.00 27.48 ? 92 SER A N 1 ATOM 710 C CA . SER A 1 92 ? -17.655 20.118 5.476 1.00 28.24 ? 92 SER A CA 1 ATOM 711 C C . SER A 1 92 ? -18.761 20.629 4.542 1.00 30.06 ? 92 SER A C 1 ATOM 712 O O . SER A 1 92 ? -19.016 20.035 3.494 1.00 28.48 ? 92 SER A O 1 ATOM 713 C CB . SER A 1 92 ? -18.072 18.802 6.146 1.00 28.31 ? 92 SER A CB 1 ATOM 714 O OG . SER A 1 92 ? -19.382 18.866 6.689 1.00 27.80 ? 92 SER A OG 1 ATOM 715 N N . GLN A 1 93 ? -19.392 21.740 4.912 1.00 32.29 ? 93 GLN A N 1 ATOM 716 C CA . GLN A 1 93 ? -20.372 22.393 4.048 1.00 34.57 ? 93 GLN A CA 1 ATOM 717 C C . GLN A 1 93 ? -19.710 23.151 2.896 1.00 34.58 ? 93 GLN A C 1 ATOM 718 O O . GLN A 1 93 ? -20.358 23.433 1.886 1.00 35.31 ? 93 GLN A O 1 ATOM 719 C CB . GLN A 1 93 ? -21.245 23.350 4.864 1.00 36.79 ? 93 GLN A CB 1 ATOM 720 C CG . GLN A 1 93 ? -21.876 22.698 6.086 1.00 39.16 ? 93 GLN A CG 1 ATOM 721 C CD . GLN A 1 93 ? -23.166 23.365 6.526 1.00 41.84 ? 93 GLN A CD 1 ATOM 722 O OE1 . GLN A 1 93 ? -24.004 23.730 5.700 1.00 44.78 ? 93 GLN A OE1 1 ATOM 723 N NE2 . GLN A 1 93 ? -23.342 23.508 7.836 1.00 43.32 ? 93 GLN A NE2 1 ATOM 724 N N . TYR A 1 94 ? -18.422 23.462 3.039 1.00 33.90 ? 94 TYR A N 1 ATOM 725 C CA . TYR A 1 94 ? -17.726 24.329 2.090 1.00 33.83 ? 94 TYR A CA 1 ATOM 726 C C . TYR A 1 94 ? -16.566 23.690 1.317 1.00 32.82 ? 94 TYR A C 1 ATOM 727 O O . TYR A 1 94 ? -16.323 24.070 0.171 1.00 33.29 ? 94 TYR A O 1 ATOM 728 C CB . TYR A 1 94 ? -17.240 25.579 2.820 1.00 34.81 ? 94 TYR A CB 1 ATOM 729 C CG . TYR A 1 94 ? -18.377 26.378 3.410 1.00 35.91 ? 94 TYR A CG 1 ATOM 730 C CD1 . TYR A 1 94 ? -19.074 27.302 2.637 1.00 37.13 ? 94 TYR A CD1 1 ATOM 731 C CD2 . TYR A 1 94 ? -18.769 26.198 4.730 1.00 36.53 ? 94 TYR A CD2 1 ATOM 732 C CE1 . TYR A 1 94 ? -20.125 28.030 3.168 1.00 37.43 ? 94 TYR A CE1 1 ATOM 733 C CE2 . TYR A 1 94 ? -19.819 26.922 5.271 1.00 37.64 ? 94 TYR A CE2 1 ATOM 734 C CZ . TYR A 1 94 ? -20.491 27.838 4.487 1.00 38.08 ? 94 TYR A CZ 1 ATOM 735 O OH . TYR A 1 94 ? -21.534 28.561 5.020 1.00 39.82 ? 94 TYR A OH 1 ATOM 736 N N . VAL A 1 95 ? -15.844 22.748 1.924 1.00 30.68 ? 95 VAL A N 1 ATOM 737 C CA . VAL A 1 95 ? -14.676 22.151 1.262 1.00 30.12 ? 95 VAL A CA 1 ATOM 738 C C . VAL A 1 95 ? -14.866 20.668 0.971 1.00 29.37 ? 95 VAL A C 1 ATOM 739 O O . VAL A 1 95 ? -15.566 19.967 1.702 1.00 29.34 ? 95 VAL A O 1 ATOM 740 C CB . VAL A 1 95 ? -13.365 22.333 2.066 1.00 29.82 ? 95 VAL A CB 1 ATOM 741 C CG1 . VAL A 1 95 ? -13.043 23.810 2.242 1.00 30.17 ? 95 VAL A CG1 1 ATOM 742 C CG2 . VAL A 1 95 ? -13.422 21.629 3.417 1.00 29.52 ? 95 VAL A CG2 1 ATOM 743 N N . PHE A 1 96 ? -14.233 20.212 -0.107 1.00 29.07 ? 96 PHE A N 1 ATOM 744 C CA . PHE A 1 96 ? -14.207 18.796 -0.493 1.00 29.47 ? 96 PHE A CA 1 ATOM 745 C C . PHE A 1 96 ? -15.590 18.231 -0.813 1.00 32.02 ? 96 PHE A C 1 ATOM 746 O O . PHE A 1 96 ? -15.803 17.021 -0.733 1.00 32.36 ? 96 PHE A O 1 ATOM 747 C CB . PHE A 1 96 ? -13.544 17.934 0.592 1.00 28.49 ? 96 PHE A CB 1 ATOM 748 C CG . PHE A 1 96 ? -12.243 18.484 1.115 1.00 27.20 ? 96 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 96 ? -11.322 19.093 0.265 1.00 26.99 ? 96 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 96 ? -11.923 18.358 2.460 1.00 26.72 ? 96 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 96 ? -10.125 19.585 0.759 1.00 26.28 ? 96 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 96 ? -10.727 18.846 2.956 1.00 26.34 ? 96 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 96 ? -9.827 19.462 2.105 1.00 26.29 ? 96 PHE A CZ 1 ATOM 754 N N . ARG A 1 97 ? -16.514 19.105 -1.201 1.00 34.58 ? 97 ARG A N 1 ATOM 755 C CA . ARG A 1 97 ? -17.893 18.710 -1.487 1.00 37.15 ? 97 ARG A CA 1 ATOM 756 C C . ARG A 1 97 ? -17.998 17.708 -2.641 1.00 36.70 ? 97 ARG A C 1 ATOM 757 O O . ARG A 1 97 ? -18.947 16.927 -2.706 1.00 37.31 ? 97 ARG A O 1 ATOM 758 C CB . ARG A 1 97 ? -18.726 19.954 -1.791 1.00 39.11 ? 97 ARG A CB 1 ATOM 759 C CG . ARG A 1 97 ? -18.952 20.841 -0.572 1.00 41.28 ? 97 ARG A CG 1 ATOM 760 C CD . ARG A 1 97 ? -20.046 20.276 0.316 1.00 43.55 ? 97 ARG A CD 1 ATOM 761 N NE . ARG A 1 97 ? -21.270 20.105 -0.461 1.00 45.16 ? 97 ARG A NE 1 ATOM 762 C CZ . ARG A 1 97 ? -22.147 21.071 -0.729 1.00 46.70 ? 97 ARG A CZ 1 ATOM 763 N NH1 . ARG A 1 97 ? -23.214 20.793 -1.469 1.00 47.02 ? 97 ARG A NH1 1 ATOM 764 N NH2 . ARG A 1 97 ? -21.977 22.308 -0.266 1.00 47.24 ? 97 ARG A NH2 1 ATOM 765 N N . SER A 1 98 ? -17.013 17.735 -3.537 1.00 36.25 ? 98 SER A N 1 ATOM 766 C CA . SER A 1 98 ? -16.949 16.822 -4.675 1.00 35.94 ? 98 SER A CA 1 ATOM 767 C C . SER A 1 98 ? -16.434 15.416 -4.334 1.00 34.48 ? 98 SER A C 1 ATOM 768 O O . SER A 1 98 ? -16.402 14.556 -5.210 1.00 34.03 ? 98 SER A O 1 ATOM 769 C CB . SER A 1 98 ? -16.058 17.424 -5.761 1.00 36.75 ? 98 SER A CB 1 ATOM 770 O OG . SER A 1 98 ? -14.779 17.741 -5.239 1.00 39.41 ? 98 SER A OG 1 ATOM 771 N N . ALA A 1 99 ? -16.020 15.183 -3.089 1.00 33.45 ? 99 ALA A N 1 ATOM 772 C CA . ALA A 1 99 ? -15.591 13.847 -2.664 1.00 32.90 ? 99 ALA A CA 1 ATOM 773 C C . ALA A 1 99 ? -16.729 12.851 -2.858 1.00 33.26 ? 99 ALA A C 1 ATOM 774 O O . ALA A 1 99 ? -17.889 13.179 -2.611 1.00 32.67 ? 99 ALA A O 1 ATOM 775 C CB . ALA A 1 99 ? -15.155 13.861 -1.206 1.00 32.38 ? 99 ALA A CB 1 ATOM 776 N N . ARG A 1 100 ? -16.400 11.643 -3.308 1.00 33.82 ? 100 ARG A N 1 ATOM 777 C CA . ARG A 1 100 ? -17.414 10.602 -3.489 1.00 34.77 ? 100 ARG A CA 1 ATOM 778 C C . ARG A 1 100 ? -18.040 10.174 -2.156 1.00 32.28 ? 100 ARG A C 1 ATOM 779 O O . ARG A 1 100 ? -19.226 9.854 -2.109 1.00 31.76 ? 100 ARG A O 1 ATOM 780 C CB . ARG A 1 100 ? -16.840 9.397 -4.242 1.00 37.45 ? 100 ARG A CB 1 ATOM 781 C CG . ARG A 1 100 ? -16.548 9.678 -5.711 1.00 40.46 ? 100 ARG A CG 1 ATOM 782 C CD . ARG A 1 100 ? -16.190 8.421 -6.495 1.00 43.26 ? 100 ARG A CD 1 ATOM 783 N NE . ARG A 1 100 ? -17.299 7.461 -6.539 1.00 45.94 ? 100 ARG A NE 1 ATOM 784 C CZ . ARG A 1 100 ? -17.307 6.249 -5.976 1.00 48.92 ? 100 ARG A CZ 1 ATOM 785 N NH1 . ARG A 1 100 ? -16.253 5.785 -5.308 1.00 49.70 ? 100 ARG A NH1 1 ATOM 786 N NH2 . ARG A 1 100 ? -18.388 5.483 -6.091 1.00 50.58 ? 100 ARG A NH2 1 ATOM 787 N N . ARG A 1 101 ? -17.260 10.176 -1.076 1.00 30.54 ? 101 ARG A N 1 ATOM 788 C CA . ARG A 1 101 ? -17.806 9.912 0.261 1.00 29.50 ? 101 ARG A CA 1 ATOM 789 C C . ARG A 1 101 ? -17.102 10.735 1.328 1.00 27.67 ? 101 ARG A C 1 ATOM 790 O O . ARG A 1 101 ? -15.953 11.144 1.155 1.00 27.92 ? 101 ARG A O 1 ATOM 791 C CB . ARG A 1 101 ? -17.723 8.420 0.618 1.00 31.00 ? 101 ARG A CB 1 ATOM 792 C CG . ARG A 1 101 ? -16.329 7.836 0.489 1.00 31.41 ? 101 ARG A CG 1 ATOM 793 C CD . ARG A 1 101 ? -16.141 6.512 1.220 1.00 31.98 ? 101 ARG A CD 1 ATOM 794 N NE . ARG A 1 101 ? -14.711 6.199 1.279 1.00 32.25 ? 101 ARG A NE 1 ATOM 795 C CZ . ARG A 1 101 ? -14.162 5.144 1.881 1.00 32.97 ? 101 ARG A CZ 1 ATOM 796 N NH1 . ARG A 1 101 ? -14.903 4.227 2.501 1.00 32.87 ? 101 ARG A NH1 1 ATOM 797 N NH2 . ARG A 1 101 ? -12.840 5.007 1.854 1.00 33.30 ? 101 ARG A NH2 1 ATOM 798 N N . LYS A 1 102 ? -17.814 10.973 2.422 1.00 26.34 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? -17.293 11.712 3.557 1.00 25.80 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? -17.291 10.826 4.783 1.00 25.16 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? -18.333 10.288 5.165 1.00 25.73 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? -18.154 12.938 3.844 1.00 26.06 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? -17.735 13.674 5.105 1.00 26.28 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? -18.435 15.008 5.242 1.00 26.99 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? -19.809 14.869 5.865 1.00 27.23 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? -20.401 16.228 5.987 1.00 28.00 ? 102 LYS A NZ 1 ATOM 807 N N . ILE A 1 103 ? -16.124 10.695 5.406 1.00 23.33 ? 103 ILE A N 1 ATOM 808 C CA . ILE A 1 103 ? -15.995 9.995 6.672 1.00 22.54 ? 103 ILE A CA 1 ATOM 809 C C . ILE A 1 103 ? -15.752 10.999 7.784 1.00 22.53 ? 103 ILE A C 1 ATOM 810 O O . ILE A 1 103 ? -14.864 11.855 7.684 1.00 22.69 ? 103 ILE A O 1 ATOM 811 C CB . ILE A 1 103 ? -14.842 8.970 6.628 1.00 22.17 ? 103 ILE A CB 1 ATOM 812 C CG1 . ILE A 1 103 ? -15.219 7.830 5.674 1.00 22.43 ? 103 ILE A CG1 1 ATOM 813 C CG2 . ILE A 1 103 ? -14.525 8.459 8.034 1.00 21.98 ? 103 ILE A CG2 1 ATOM 814 C CD1 . ILE A 1 103 ? -14.100 6.856 5.367 1.00 22.48 ? 103 ILE A CD1 1 ATOM 815 N N . THR A 1 104 ? -16.550 10.900 8.841 1.00 22.49 ? 104 THR A N 1 ATOM 816 C CA . THR A 1 104 ? -16.293 11.657 10.052 1.00 22.63 ? 104 THR A CA 1 ATOM 817 C C . THR A 1 104 ? -15.408 10.803 10.942 1.00 22.27 ? 104 THR A C 1 ATOM 818 O O . THR A 1 104 ? -15.794 9.711 11.350 1.00 22.23 ? 104 THR A O 1 ATOM 819 C CB . THR A 1 104 ? -17.588 12.035 10.793 1.00 22.89 ? 104 THR A CB 1 ATOM 820 O OG1 . THR A 1 104 ? -18.443 12.768 9.905 1.00 23.06 ? 104 THR A OG1 1 ATOM 821 C CG2 . THR A 1 104 ? -17.284 12.890 12.015 1.00 22.94 ? 104 THR A CG2 1 ATOM 822 N N . LEU A 1 105 ? -14.218 11.312 11.239 1.00 21.74 ? 105 LEU A N 1 ATOM 823 C CA . LEU A 1 105 ? -13.284 10.625 12.127 1.00 22.65 ? 105 LEU A CA 1 ATOM 824 C C . LEU A 1 105 ? -13.910 10.438 13.509 1.00 23.28 ? 105 LEU A C 1 ATOM 825 O O . LEU A 1 105 ? -14.716 11.262 13.934 1.00 24.36 ? 105 LEU A O 1 ATOM 826 C CB . LEU A 1 105 ? -11.983 11.424 12.242 1.00 22.01 ? 105 LEU A CB 1 ATOM 827 C CG . LEU A 1 105 ? -11.202 11.631 10.943 1.00 22.47 ? 105 LEU A CG 1 ATOM 828 C CD1 . LEU A 1 105 ? -10.122 12.684 11.140 1.00 22.32 ? 105 LEU A CD1 1 ATOM 829 C CD2 . LEU A 1 105 ? -10.602 10.322 10.442 1.00 22.72 ? 105 LEU A CD2 1 ATOM 830 N N . PRO A 1 106 ? -13.549 9.353 14.219 1.00 23.63 ? 106 PRO A N 1 ATOM 831 C CA . PRO A 1 106 ? -14.129 9.072 15.537 1.00 24.11 ? 106 PRO A CA 1 ATOM 832 C C . PRO A 1 106 ? -13.433 9.798 16.701 1.00 24.82 ? 106 PRO A C 1 ATOM 833 O O . PRO A 1 106 ? -13.233 9.218 17.771 1.00 25.56 ? 106 PRO A O 1 ATOM 834 C CB . PRO A 1 106 ? -13.965 7.552 15.659 1.00 23.94 ? 106 PRO A CB 1 ATOM 835 C CG . PRO A 1 106 ? -12.726 7.260 14.891 1.00 23.75 ? 106 PRO A CG 1 ATOM 836 C CD . PRO A 1 106 ? -12.681 8.251 13.759 1.00 23.73 ? 106 PRO A CD 1 ATOM 837 N N . TYR A 1 107 ? -13.068 11.059 16.473 1.00 24.02 ? 107 TYR A N 1 ATOM 838 C CA . TYR A 1 107 ? -12.519 11.931 17.502 1.00 23.61 ? 107 TYR A CA 1 ATOM 839 C C . TYR A 1 107 ? -12.558 13.368 16.994 1.00 23.95 ? 107 TYR A C 1 ATOM 840 O O . TYR A 1 107 ? -12.612 13.610 15.785 1.00 22.84 ? 107 TYR A O 1 ATOM 841 C CB . TYR A 1 107 ? -11.075 11.543 17.867 1.00 23.04 ? 107 TYR A CB 1 ATOM 842 C CG . TYR A 1 107 ? -10.264 10.992 16.711 1.00 22.27 ? 107 TYR A CG 1 ATOM 843 C CD1 . TYR A 1 107 ? -9.740 11.830 15.732 1.00 21.82 ? 107 TYR A CD1 1 ATOM 844 C CD2 . TYR A 1 107 ? -10.024 9.625 16.598 1.00 22.00 ? 107 TYR A CD2 1 ATOM 845 C CE1 . TYR A 1 107 ? -9.004 11.320 14.674 1.00 21.57 ? 107 TYR A CE1 1 ATOM 846 C CE2 . TYR A 1 107 ? -9.288 9.106 15.547 1.00 21.67 ? 107 TYR A CE2 1 ATOM 847 C CZ . TYR A 1 107 ? -8.781 9.954 14.586 1.00 21.18 ? 107 TYR A CZ 1 ATOM 848 O OH . TYR A 1 107 ? -8.055 9.443 13.540 1.00 20.46 ? 107 TYR A OH 1 ATOM 849 N N . SER A 1 108 ? -12.546 14.310 17.927 1.00 24.60 ? 108 SER A N 1 ATOM 850 C CA . SER A 1 108 ? -12.343 15.716 17.607 1.00 25.63 ? 108 SER A CA 1 ATOM 851 C C . SER A 1 108 ? -10.857 15.968 17.350 1.00 25.53 ? 108 SER A C 1 ATOM 852 O O . SER A 1 108 ? -10.030 15.061 17.486 1.00 25.12 ? 108 SER A O 1 ATOM 853 C CB . SER A 1 108 ? -12.824 16.593 18.759 1.00 26.40 ? 108 SER A CB 1 ATOM 854 O OG . SER A 1 108 ? -12.024 16.392 19.909 1.00 27.80 ? 108 SER A OG 1 ATOM 855 N N . GLY A 1 109 ? -10.521 17.202 16.991 1.00 25.65 ? 109 GLY A N 1 ATOM 856 C CA . GLY A 1 109 ? -9.152 17.552 16.626 1.00 26.46 ? 109 GLY A CA 1 ATOM 857 C C . GLY A 1 109 ? -8.257 18.068 17.738 1.00 27.35 ? 109 GLY A C 1 ATOM 858 O O . GLY A 1 109 ? -7.115 18.438 17.482 1.00 27.49 ? 109 GLY A O 1 ATOM 859 N N . ASN A 1 110 ? -8.737 18.102 18.975 1.00 28.69 ? 110 ASN A N 1 ATOM 860 C CA . ASN A 1 110 ? -7.890 18.622 20.047 1.00 30.14 ? 110 ASN A CA 1 ATOM 861 C C . ASN A 1 110 ? -6.893 17.582 20.533 1.00 29.12 ? 110 ASN A C 1 ATOM 862 O O . ASN A 1 110 ? -7.132 16.371 20.457 1.00 28.67 ? 110 ASN A O 1 ATOM 863 C CB . ASN A 1 110 ? -8.707 19.166 21.206 1.00 32.03 ? 110 ASN A CB 1 ATOM 864 C CG . ASN A 1 110 ? -9.448 18.086 21.946 1.00 33.30 ? 110 ASN A CG 1 ATOM 865 O OD1 . ASN A 1 110 ? -8.906 17.449 22.852 1.00 34.70 ? 110 ASN A OD1 1 ATOM 866 N ND2 . ASN A 1 110 ? -10.699 17.875 21.569 1.00 35.31 ? 110 ASN A ND2 1 ATOM 867 N N . TYR A 1 111 ? -5.770 18.073 21.037 1.00 27.68 ? 111 TYR A N 1 ATOM 868 C CA . TYR A 1 111 ? -4.640 17.215 21.355 1.00 27.29 ? 111 TYR A CA 1 ATOM 869 C C . TYR A 1 111 ? -4.995 16.072 22.295 1.00 28.69 ? 111 TYR A C 1 ATOM 870 O O . TYR A 1 111 ? -4.536 14.948 22.105 1.00 27.74 ? 111 TYR A O 1 ATOM 871 C CB . TYR A 1 111 ? -3.505 18.038 21.957 1.00 26.37 ? 111 TYR A CB 1 ATOM 872 C CG . TYR A 1 111 ? -2.640 18.761 20.943 1.00 25.88 ? 111 TYR A CG 1 ATOM 873 C CD1 . TYR A 1 111 ? -2.225 18.137 19.769 1.00 25.38 ? 111 TYR A CD1 1 ATOM 874 C CD2 . TYR A 1 111 ? -2.198 20.059 21.184 1.00 25.25 ? 111 TYR A CD2 1 ATOM 875 C CE1 . TYR A 1 111 ? -1.412 18.791 18.856 1.00 25.24 ? 111 TYR A CE1 1 ATOM 876 C CE2 . TYR A 1 111 ? -1.387 20.722 20.277 1.00 24.99 ? 111 TYR A CE2 1 ATOM 877 C CZ . TYR A 1 111 ? -0.997 20.085 19.115 1.00 24.67 ? 111 TYR A CZ 1 ATOM 878 O OH . TYR A 1 111 ? -0.186 20.737 18.216 1.00 23.52 ? 111 TYR A OH 1 ATOM 879 N N . GLU A 1 112 ? -5.821 16.350 23.296 1.00 30.72 ? 112 GLU A N 1 ATOM 880 C CA . GLU A 1 112 ? -6.130 15.343 24.307 1.00 32.97 ? 112 GLU A CA 1 ATOM 881 C C . GLU A 1 112 ? -6.886 14.154 23.696 1.00 32.00 ? 112 GLU A C 1 ATOM 882 O O . GLU A 1 112 ? -6.552 13.002 23.971 1.00 31.76 ? 112 GLU A O 1 ATOM 883 C CB . GLU A 1 112 ? -6.901 15.967 25.475 1.00 35.42 ? 112 GLU A CB 1 ATOM 884 C CG . GLU A 1 112 ? -6.131 17.063 26.209 1.00 38.08 ? 112 GLU A CG 1 ATOM 885 C CD . GLU A 1 112 ? -5.221 16.536 27.309 1.00 41.02 ? 112 GLU A CD 1 ATOM 886 O OE1 . GLU A 1 112 ? -4.221 15.852 26.994 1.00 42.78 ? 112 GLU A OE1 1 ATOM 887 O OE2 . GLU A 1 112 ? -5.496 16.827 28.496 1.00 42.01 ? 112 GLU A OE2 1 ATOM 888 N N . ARG A 1 113 ? -7.871 14.432 22.847 1.00 31.51 ? 113 ARG A N 1 ATOM 889 C CA . ARG A 1 113 ? -8.632 13.373 22.171 1.00 31.47 ? 113 ARG A CA 1 ATOM 890 C C . ARG A 1 113 ? -7.816 12.586 21.153 1.00 29.07 ? 113 ARG A C 1 ATOM 891 O O . ARG A 1 113 ? -7.988 11.379 21.021 1.00 27.64 ? 113 ARG A O 1 ATOM 892 C CB . ARG A 1 113 ? -9.863 13.954 21.473 1.00 33.44 ? 113 ARG A CB 1 ATOM 893 C CG . ARG A 1 113 ? -10.898 14.517 22.426 1.00 36.16 ? 113 ARG A CG 1 ATOM 894 C CD . ARG A 1 113 ? -11.455 13.430 23.326 1.00 39.21 ? 113 ARG A CD 1 ATOM 895 N NE . ARG A 1 113 ? -12.355 13.965 24.339 1.00 42.79 ? 113 ARG A NE 1 ATOM 896 C CZ . ARG A 1 113 ? -12.831 13.266 25.367 1.00 45.04 ? 113 ARG A CZ 1 ATOM 897 N NH1 . ARG A 1 113 ? -13.647 13.850 26.235 1.00 46.20 ? 113 ARG A NH1 1 ATOM 898 N NH2 . ARG A 1 113 ? -12.496 11.988 25.537 1.00 45.83 ? 113 ARG A NH2 1 ATOM 899 N N . LEU A 1 114 ? -6.950 13.276 20.418 1.00 27.00 ? 114 LEU A N 1 ATOM 900 C CA . LEU A 1 114 ? -6.090 12.616 19.437 1.00 25.34 ? 114 LEU A CA 1 ATOM 901 C C . LEU A 1 114 ? -5.100 11.664 20.092 1.00 25.14 ? 114 LEU A C 1 ATOM 902 O O . LEU A 1 114 ? -4.868 10.561 19.597 1.00 25.07 ? 114 LEU A O 1 ATOM 903 C CB . LEU A 1 114 ? -5.330 13.654 18.616 1.00 24.71 ? 114 LEU A CB 1 ATOM 904 C CG . LEU A 1 114 ? -6.168 14.331 17.539 1.00 24.01 ? 114 LEU A CG 1 ATOM 905 C CD1 . LEU A 1 114 ? -5.450 15.572 17.036 1.00 24.02 ? 114 LEU A CD1 1 ATOM 906 C CD2 . LEU A 1 114 ? -6.454 13.373 16.392 1.00 24.36 ? 114 LEU A CD2 1 ATOM 907 N N . GLN A 1 115 ? -4.516 12.112 21.196 1.00 25.81 ? 115 GLN A N 1 ATOM 908 C CA . GLN A 1 115 ? -3.566 11.314 21.970 1.00 26.34 ? 115 GLN A CA 1 ATOM 909 C C . GLN A 1 115 ? -4.223 10.058 22.549 1.00 26.50 ? 115 GLN A C 1 ATOM 910 O O . GLN A 1 115 ? -3.610 8.991 22.576 1.00 26.23 ? 115 GLN A O 1 ATOM 911 C CB . GLN A 1 115 ? -2.965 12.171 23.083 1.00 26.68 ? 115 GLN A CB 1 ATOM 912 C CG . GLN A 1 115 ? -1.986 13.224 22.568 1.00 26.84 ? 115 GLN A CG 1 ATOM 913 C CD . GLN A 1 115 ? -1.422 14.151 23.639 1.00 27.28 ? 115 GLN A CD 1 ATOM 914 O OE1 . GLN A 1 115 ? -0.479 14.895 23.372 1.00 27.58 ? 115 GLN A OE1 1 ATOM 915 N NE2 . GLN A 1 115 ? -1.982 14.116 24.846 1.00 28.08 ? 115 GLN A NE2 1 ATOM 916 N N . ILE A 1 116 ? -5.469 10.194 22.999 1.00 27.35 ? 116 ILE A N 1 ATOM 917 C CA . ILE A 1 116 ? -6.262 9.052 23.466 1.00 28.31 ? 116 ILE A CA 1 ATOM 918 C C . ILE A 1 116 ? -6.482 8.049 22.330 1.00 27.87 ? 116 ILE A C 1 ATOM 919 O O . ILE A 1 116 ? -6.304 6.847 22.516 1.00 27.40 ? 116 ILE A O 1 ATOM 920 C CB . ILE A 1 116 ? -7.614 9.515 24.066 1.00 29.44 ? 116 ILE A CB 1 ATOM 921 C CG1 . ILE A 1 116 ? -7.371 10.214 25.410 1.00 30.61 ? 116 ILE A CG1 1 ATOM 922 C CG2 . ILE A 1 116 ? -8.568 8.340 24.255 1.00 29.94 ? 116 ILE A CG2 1 ATOM 923 C CD1 . ILE A 1 116 ? -8.584 10.913 25.990 1.00 31.08 ? 116 ILE A CD1 1 ATOM 924 N N . ALA A 1 117 ? -6.853 8.550 21.154 1.00 27.58 ? 117 ALA A N 1 ATOM 925 C CA . ALA A 1 117 ? -7.075 7.694 19.986 1.00 27.37 ? 117 ALA A CA 1 ATOM 926 C C . ALA A 1 117 ? -5.785 7.028 19.515 1.00 27.88 ? 117 ALA A C 1 ATOM 927 O O . ALA A 1 117 ? -5.778 5.841 19.189 1.00 27.76 ? 117 ALA A O 1 ATOM 928 C CB . ALA A 1 117 ? -7.707 8.490 18.854 1.00 27.24 ? 117 ALA A CB 1 ATOM 929 N N . ALA A 1 118 ? -4.697 7.793 19.491 1.00 27.60 ? 118 ALA A N 1 ATOM 930 C CA . ALA A 1 118 ? -3.402 7.291 19.033 1.00 27.79 ? 118 ALA A CA 1 ATOM 931 C C . ALA A 1 118 ? -2.779 6.319 20.032 1.00 28.87 ? 118 ALA A C 1 ATOM 932 O O . ALA A 1 118 ? -1.914 5.515 19.670 1.00 28.99 ? 118 ALA A O 1 ATOM 933 C CB . ALA A 1 118 ? -2.454 8.450 18.773 1.00 27.48 ? 118 ALA A CB 1 ATOM 934 N N . GLY A 1 119 ? -3.212 6.403 21.289 1.00 29.97 ? 119 GLY A N 1 ATOM 935 C CA . GLY A 1 119 ? -2.723 5.519 22.339 1.00 31.03 ? 119 GLY A CA 1 ATOM 936 C C . GLY A 1 119 ? -1.410 5.987 22.938 1.00 32.26 ? 119 GLY A C 1 ATOM 937 O O . GLY A 1 119 ? -0.704 5.208 23.575 1.00 32.88 ? 119 GLY A O 1 ATOM 938 N N . LYS A 1 120 ? -1.074 7.258 22.736 1.00 32.70 ? 120 LYS A N 1 ATOM 939 C CA . LYS A 1 120 ? 0.158 7.807 23.288 1.00 33.12 ? 120 LYS A CA 1 ATOM 940 C C . LYS A 1 120 ? 0.174 9.330 23.242 1.00 31.58 ? 120 LYS A C 1 ATOM 941 O O . LYS A 1 120 ? -0.420 9.931 22.347 1.00 29.77 ? 120 LYS A O 1 ATOM 942 C CB . LYS A 1 120 ? 1.381 7.241 22.561 1.00 34.94 ? 120 LYS A CB 1 ATOM 943 C CG . LYS A 1 120 ? 1.315 7.270 21.041 1.00 36.58 ? 120 LYS A CG 1 ATOM 944 C CD . LYS A 1 120 ? 2.354 6.348 20.410 1.00 38.46 ? 120 LYS A CD 1 ATOM 945 C CE . LYS A 1 120 ? 3.726 6.473 21.063 1.00 39.91 ? 120 LYS A CE 1 ATOM 946 N NZ . LYS A 1 120 ? 4.765 5.641 20.393 1.00 41.72 ? 120 LYS A NZ 1 ATOM 947 N N . PRO A 1 121 ? 0.851 9.957 24.218 1.00 31.12 ? 121 PRO A N 1 ATOM 948 C CA . PRO A 1 121 ? 0.960 11.405 24.208 1.00 31.01 ? 121 PRO A CA 1 ATOM 949 C C . PRO A 1 121 ? 1.976 11.812 23.159 1.00 30.69 ? 121 PRO A C 1 ATOM 950 O O . PRO A 1 121 ? 2.833 11.006 22.782 1.00 31.06 ? 121 PRO A O 1 ATOM 951 C CB . PRO A 1 121 ? 1.477 11.721 25.609 1.00 31.24 ? 121 PRO A CB 1 ATOM 952 C CG . PRO A 1 121 ? 2.312 10.541 25.955 1.00 31.28 ? 121 PRO A CG 1 ATOM 953 C CD . PRO A 1 121 ? 1.619 9.360 25.327 1.00 31.25 ? 121 PRO A CD 1 ATOM 954 N N . ARG A 1 122 ? 1.906 13.048 22.694 1.00 30.44 ? 122 ARG A N 1 ATOM 955 C CA . ARG A 1 122 ? 2.793 13.444 21.611 1.00 30.35 ? 122 ARG A CA 1 ATOM 956 C C . ARG A 1 122 ? 4.234 13.692 22.087 1.00 30.68 ? 122 ARG A C 1 ATOM 957 O O . ARG A 1 122 ? 5.141 13.805 21.265 1.00 29.56 ? 122 ARG A O 1 ATOM 958 C CB . ARG A 1 122 ? 2.201 14.608 20.824 1.00 30.97 ? 122 ARG A CB 1 ATOM 959 C CG . ARG A 1 122 ? 2.096 15.897 21.590 1.00 30.33 ? 122 ARG A CG 1 ATOM 960 C CD . ARG A 1 122 ? 1.027 16.776 20.979 1.00 30.29 ? 122 ARG A CD 1 ATOM 961 N NE . ARG A 1 122 ? 1.159 18.123 21.503 1.00 30.58 ? 122 ARG A NE 1 ATOM 962 C CZ . ARG A 1 122 ? 0.621 18.561 22.639 1.00 30.27 ? 122 ARG A CZ 1 ATOM 963 N NH1 . ARG A 1 122 ? -0.129 17.771 23.401 1.00 31.27 ? 122 ARG A NH1 1 ATOM 964 N NH2 . ARG A 1 122 ? 0.832 19.815 23.010 1.00 29.03 ? 122 ARG A NH2 1 ATOM 965 N N . GLU A 1 123 ? 4.451 13.728 23.405 1.00 31.46 ? 123 GLU A N 1 ATOM 966 C CA . GLU A 1 123 ? 5.808 13.662 23.965 1.00 32.75 ? 123 GLU A CA 1 ATOM 967 C C . GLU A 1 123 ? 6.583 12.440 23.463 1.00 31.83 ? 123 GLU A C 1 ATOM 968 O O . GLU A 1 123 ? 7.809 12.467 23.388 1.00 32.18 ? 123 GLU A O 1 ATOM 969 C CB . GLU A 1 123 ? 5.779 13.621 25.499 1.00 34.27 ? 123 GLU A CB 1 ATOM 970 C CG . GLU A 1 123 ? 5.540 14.968 26.167 1.00 35.57 ? 123 GLU A CG 1 ATOM 971 C CD . GLU A 1 123 ? 4.072 15.307 26.354 1.00 35.92 ? 123 GLU A CD 1 ATOM 972 O OE1 . GLU A 1 123 ? 3.211 14.666 25.720 1.00 35.67 ? 123 GLU A OE1 1 ATOM 973 O OE2 . GLU A 1 123 ? 3.782 16.231 27.142 1.00 38.51 ? 123 GLU A OE2 1 ATOM 974 N N . LYS A 1 124 ? 5.859 11.375 23.131 1.00 31.36 ? 124 LYS A N 1 ATOM 975 C CA . LYS A 1 124 ? 6.458 10.113 22.698 1.00 31.61 ? 124 LYS A CA 1 ATOM 976 C C . LYS A 1 124 ? 6.408 9.880 21.184 1.00 29.38 ? 124 LYS A C 1 ATOM 977 O O . LYS A 1 124 ? 6.885 8.846 20.714 1.00 28.27 ? 124 LYS A O 1 ATOM 978 C CB . LYS A 1 124 ? 5.738 8.952 23.387 1.00 33.36 ? 124 LYS A CB 1 ATOM 979 C CG . LYS A 1 124 ? 5.802 8.971 24.907 1.00 35.71 ? 124 LYS A CG 1 ATOM 980 C CD . LYS A 1 124 ? 6.878 8.046 25.460 1.00 37.74 ? 124 LYS A CD 1 ATOM 981 C CE . LYS A 1 124 ? 6.412 7.366 26.740 1.00 39.95 ? 124 LYS A CE 1 ATOM 982 N NZ . LYS A 1 124 ? 6.070 8.325 27.830 1.00 41.11 ? 124 LYS A NZ 1 ATOM 983 N N . ILE A 1 125 ? 5.831 10.814 20.424 1.00 26.49 ? 125 ILE A N 1 ATOM 984 C CA . ILE A 1 125 ? 5.693 10.650 18.970 1.00 24.88 ? 125 ILE A CA 1 ATOM 985 C C . ILE A 1 125 ? 6.749 11.489 18.249 1.00 23.98 ? 125 ILE A C 1 ATOM 986 O O . ILE A 1 125 ? 6.687 12.720 18.282 1.00 22.94 ? 125 ILE A O 1 ATOM 987 C CB . ILE A 1 125 ? 4.285 11.064 18.472 1.00 24.46 ? 125 ILE A CB 1 ATOM 988 C CG1 . ILE A 1 125 ? 3.204 10.303 19.249 1.00 24.62 ? 125 ILE A CG1 1 ATOM 989 C CG2 . ILE A 1 125 ? 4.149 10.813 16.971 1.00 24.58 ? 125 ILE A CG2 1 ATOM 990 C CD1 . ILE A 1 125 ? 1.781 10.728 18.942 1.00 24.46 ? 125 ILE A CD1 1 ATOM 991 N N . PRO A 1 126 ? 7.724 10.827 17.594 1.00 23.24 ? 126 PRO A N 1 ATOM 992 C CA . PRO A 1 126 ? 8.704 11.570 16.806 1.00 22.51 ? 126 PRO A CA 1 ATOM 993 C C . PRO A 1 126 ? 8.057 12.440 15.737 1.00 21.68 ? 126 PRO A C 1 ATOM 994 O O . PRO A 1 126 ? 7.070 12.035 15.118 1.00 21.50 ? 126 PRO A O 1 ATOM 995 C CB . PRO A 1 126 ? 9.544 10.470 16.147 1.00 22.73 ? 126 PRO A CB 1 ATOM 996 C CG . PRO A 1 126 ? 9.387 9.288 17.031 1.00 23.12 ? 126 PRO A CG 1 ATOM 997 C CD . PRO A 1 126 ? 8.006 9.379 17.603 1.00 22.97 ? 126 PRO A CD 1 ATOM 998 N N . ILE A 1 127 ? 8.607 13.633 15.548 1.00 21.33 ? 127 ILE A N 1 ATOM 999 C CA . ILE A 1 127 ? 8.191 14.510 14.466 1.00 20.67 ? 127 ILE A CA 1 ATOM 1000 C C . ILE A 1 127 ? 9.416 14.911 13.660 1.00 20.58 ? 127 ILE A C 1 ATOM 1001 O O . ILE A 1 127 ? 10.555 14.675 14.075 1.00 21.12 ? 127 ILE A O 1 ATOM 1002 C CB . ILE A 1 127 ? 7.401 15.739 14.980 1.00 20.79 ? 127 ILE A CB 1 ATOM 1003 C CG1 . ILE A 1 127 ? 8.241 16.589 15.947 1.00 20.85 ? 127 ILE A CG1 1 ATOM 1004 C CG2 . ILE A 1 127 ? 6.113 15.273 15.644 1.00 20.84 ? 127 ILE A CG2 1 ATOM 1005 C CD1 . ILE A 1 127 ? 7.511 17.803 16.494 1.00 21.03 ? 127 ILE A CD1 1 ATOM 1006 N N . GLY A 1 128 ? 9.164 15.507 12.503 1.00 20.63 ? 128 GLY A N 1 ATOM 1007 C CA . GLY A 1 128 ? 10.193 15.791 11.517 1.00 20.37 ? 128 GLY A CA 1 ATOM 1008 C C . GLY A 1 128 ? 9.595 15.669 10.135 1.00 20.46 ? 128 GLY A C 1 ATOM 1009 O O . GLY A 1 128 ? 8.406 15.353 9.985 1.00 19.96 ? 128 GLY A O 1 ATOM 1010 N N . LEU A 1 129 ? 10.412 15.916 9.117 1.00 20.01 ? 129 LEU A N 1 ATOM 1011 C CA . LEU A 1 129 ? 9.946 15.780 7.746 1.00 20.05 ? 129 LEU A CA 1 ATOM 1012 C C . LEU A 1 129 ? 9.724 14.315 7.363 1.00 19.68 ? 129 LEU A C 1 ATOM 1013 O O . LEU A 1 129 ? 8.747 14.016 6.681 1.00 19.97 ? 129 LEU A O 1 ATOM 1014 C CB . LEU A 1 129 ? 10.885 16.483 6.762 1.00 20.35 ? 129 LEU A CB 1 ATOM 1015 C CG . LEU A 1 129 ? 10.997 17.999 6.957 1.00 20.49 ? 129 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 129 ? 11.862 18.615 5.869 1.00 20.63 ? 129 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 129 ? 9.627 18.663 6.982 1.00 20.72 ? 129 LEU A CD2 1 ATOM 1018 N N . PRO A 1 130 ? 10.605 13.397 7.811 1.00 19.44 ? 130 PRO A N 1 ATOM 1019 C CA . PRO A 1 130 ? 10.275 11.993 7.548 1.00 19.07 ? 130 PRO A CA 1 ATOM 1020 C C . PRO A 1 130 ? 8.940 11.562 8.179 1.00 18.75 ? 130 PRO A C 1 ATOM 1021 O O . PRO A 1 130 ? 8.161 10.864 7.533 1.00 19.10 ? 130 PRO A O 1 ATOM 1022 C CB . PRO A 1 130 ? 11.461 11.234 8.155 1.00 19.23 ? 130 PRO A CB 1 ATOM 1023 C CG . PRO A 1 130 ? 12.597 12.203 8.066 1.00 19.26 ? 130 PRO A CG 1 ATOM 1024 C CD . PRO A 1 130 ? 11.963 13.538 8.370 1.00 19.20 ? 130 PRO A CD 1 ATOM 1025 N N . ALA A 1 131 ? 8.668 11.998 9.406 1.00 18.52 ? 131 ALA A N 1 ATOM 1026 C CA . ALA A 1 131 ? 7.392 11.689 10.057 1.00 18.51 ? 131 ALA A CA 1 ATOM 1027 C C . ALA A 1 131 ? 6.217 12.291 9.285 1.00 18.31 ? 131 ALA A C 1 ATOM 1028 O O . ALA A 1 131 ? 5.160 11.673 9.197 1.00 17.73 ? 131 ALA A O 1 ATOM 1029 C CB . ALA A 1 131 ? 7.379 12.165 11.504 1.00 18.65 ? 131 ALA A CB 1 ATOM 1030 N N . LEU A 1 132 ? 6.402 13.485 8.721 1.00 18.56 ? 132 LEU A N 1 ATOM 1031 C CA . LEU A 1 132 ? 5.354 14.110 7.910 1.00 19.27 ? 132 LEU A CA 1 ATOM 1032 C C . LEU A 1 132 ? 5.079 13.295 6.643 1.00 20.36 ? 132 LEU A C 1 ATOM 1033 O O . LEU A 1 132 ? 3.925 13.082 6.281 1.00 19.95 ? 132 LEU A O 1 ATOM 1034 C CB . LEU A 1 132 ? 5.713 15.556 7.552 1.00 19.31 ? 132 LEU A CB 1 ATOM 1035 C CG . LEU A 1 132 ? 4.706 16.329 6.683 1.00 19.45 ? 132 LEU A CG 1 ATOM 1036 C CD1 . LEU A 1 132 ? 3.294 16.267 7.240 1.00 19.13 ? 132 LEU A CD1 1 ATOM 1037 C CD2 . LEU A 1 132 ? 5.149 17.775 6.533 1.00 19.53 ? 132 LEU A CD2 1 ATOM 1038 N N . ASP A 1 133 ? 6.140 12.846 5.974 1.00 20.87 ? 133 ASP A N 1 ATOM 1039 C CA . ASP A 1 133 ? 6.009 11.938 4.827 1.00 22.22 ? 133 ASP A CA 1 ATOM 1040 C C . ASP A 1 133 ? 5.169 10.709 5.206 1.00 21.64 ? 133 ASP A C 1 ATOM 1041 O O . ASP A 1 133 ? 4.237 10.329 4.484 1.00 20.96 ? 133 ASP A O 1 ATOM 1042 C CB . ASP A 1 133 ? 7.407 11.516 4.347 1.00 23.70 ? 133 ASP A CB 1 ATOM 1043 C CG . ASP A 1 133 ? 7.381 10.690 3.073 1.00 25.37 ? 133 ASP A CG 1 ATOM 1044 O OD1 . ASP A 1 133 ? 6.492 10.897 2.229 1.00 26.57 ? 133 ASP A OD1 1 ATOM 1045 O OD2 . ASP A 1 133 ? 8.282 9.846 2.904 1.00 27.39 ? 133 ASP A OD2 1 ATOM 1046 N N . THR A 1 134 ? 5.482 10.118 6.358 1.00 21.88 ? 134 THR A N 1 ATOM 1047 C CA . THR A 1 134 ? 4.729 8.972 6.881 1.00 22.33 ? 134 THR A CA 1 ATOM 1048 C C . THR A 1 134 ? 3.275 9.326 7.161 1.00 21.44 ? 134 THR A C 1 ATOM 1049 O O . THR A 1 134 ? 2.371 8.536 6.868 1.00 20.99 ? 134 THR A O 1 ATOM 1050 C CB . THR A 1 134 ? 5.347 8.440 8.187 1.00 23.41 ? 134 THR A CB 1 ATOM 1051 O OG1 . THR A 1 134 ? 6.703 8.062 7.954 1.00 26.10 ? 134 THR A OG1 1 ATOM 1052 C CG2 . THR A 1 134 ? 4.595 7.241 8.705 1.00 24.24 ? 134 THR A CG2 1 ATOM 1053 N N . ALA A 1 135 ? 3.051 10.500 7.744 1.00 20.43 ? 135 ALA A N 1 ATOM 1054 C CA . ALA A 1 135 ? 1.698 10.924 8.101 1.00 20.28 ? 135 ALA A CA 1 ATOM 1055 C C . ALA A 1 135 ? 0.826 11.040 6.857 1.00 20.02 ? 135 ALA A C 1 ATOM 1056 O O . ALA A 1 135 ? -0.313 10.567 6.843 1.00 19.65 ? 135 ALA A O 1 ATOM 1057 C CB . ALA A 1 135 ? 1.736 12.251 8.848 1.00 20.16 ? 135 ALA A CB 1 ATOM 1058 N N . ILE A 1 136 ? 1.372 11.660 5.812 1.00 20.03 ? 136 ILE A N 1 ATOM 1059 C CA . ILE A 1 136 ? 0.649 11.838 4.555 1.00 20.48 ? 136 ILE A CA 1 ATOM 1060 C C . ILE A 1 136 ? 0.268 10.469 4.007 1.00 21.40 ? 136 ILE A C 1 ATOM 1061 O O . ILE A 1 136 ? -0.883 10.243 3.629 1.00 21.56 ? 136 ILE A O 1 ATOM 1062 C CB . ILE A 1 136 ? 1.483 12.613 3.507 1.00 20.36 ? 136 ILE A CB 1 ATOM 1063 C CG1 . ILE A 1 136 ? 1.714 14.056 3.966 1.00 20.34 ? 136 ILE A CG1 1 ATOM 1064 C CG2 . ILE A 1 136 ? 0.785 12.611 2.155 1.00 20.41 ? 136 ILE A CG2 1 ATOM 1065 C CD1 . ILE A 1 136 ? 2.893 14.746 3.316 1.00 20.27 ? 136 ILE A CD1 1 ATOM 1066 N N . SER A 1 137 ? 1.239 9.558 3.980 1.00 21.77 ? 137 SER A N 1 ATOM 1067 C CA . SER A 1 137 ? 1.011 8.200 3.488 1.00 22.54 ? 137 SER A CA 1 ATOM 1068 C C . SER A 1 137 ? -0.080 7.485 4.274 1.00 22.51 ? 137 SER A C 1 ATOM 1069 O O . SER A 1 137 ? -0.947 6.839 3.683 1.00 23.38 ? 137 SER A O 1 ATOM 1070 C CB . SER A 1 137 ? 2.306 7.389 3.534 1.00 23.05 ? 137 SER A CB 1 ATOM 1071 O OG . SER A 1 137 ? 3.264 7.954 2.666 1.00 24.21 ? 137 SER A OG 1 ATOM 1072 N N . THR A 1 138 ? -0.042 7.619 5.598 1.00 21.83 ? 138 THR A N 1 ATOM 1073 C CA . THR A 1 138 ? -1.030 7.001 6.483 1.00 22.43 ? 138 THR A CA 1 ATOM 1074 C C . THR A 1 138 ? -2.439 7.513 6.200 1.00 22.36 ? 138 THR A C 1 ATOM 1075 O O . THR A 1 138 ? -3.397 6.738 6.168 1.00 22.31 ? 138 THR A O 1 ATOM 1076 C CB . THR A 1 138 ? -0.694 7.265 7.968 1.00 22.54 ? 138 THR A CB 1 ATOM 1077 O OG1 . THR A 1 138 ? 0.443 6.478 8.351 1.00 22.80 ? 138 THR A OG1 1 ATOM 1078 C CG2 . THR A 1 138 ? -1.874 6.917 8.889 1.00 23.01 ? 138 THR A CG2 1 ATOM 1079 N N . LEU A 1 139 ? -2.566 8.819 5.997 1.00 21.94 ? 139 LEU A N 1 ATOM 1080 C CA . LEU A 1 139 ? -3.886 9.421 5.806 1.00 22.42 ? 139 LEU A CA 1 ATOM 1081 C C . LEU A 1 139 ? -4.495 9.099 4.441 1.00 23.45 ? 139 LEU A C 1 ATOM 1082 O O . LEU A 1 139 ? -5.696 9.282 4.246 1.00 23.97 ? 139 LEU A O 1 ATOM 1083 C CB . LEU A 1 139 ? -3.820 10.935 6.032 1.00 21.93 ? 139 LEU A CB 1 ATOM 1084 C CG . LEU A 1 139 ? -3.411 11.369 7.444 1.00 21.36 ? 139 LEU A CG 1 ATOM 1085 C CD1 . LEU A 1 139 ? -3.291 12.885 7.480 1.00 21.77 ? 139 LEU A CD1 1 ATOM 1086 C CD2 . LEU A 1 139 ? -4.379 10.896 8.525 1.00 21.36 ? 139 LEU A CD2 1 ATOM 1087 N N . LEU A 1 140 ? -3.684 8.597 3.507 1.00 25.19 ? 140 LEU A N 1 ATOM 1088 C CA . LEU A 1 140 ? -4.178 8.236 2.174 1.00 27.56 ? 140 LEU A CA 1 ATOM 1089 C C . LEU A 1 140 ? -5.209 7.107 2.209 1.00 29.02 ? 140 LEU A C 1 ATOM 1090 O O . LEU A 1 140 ? -6.077 7.041 1.335 1.00 29.38 ? 140 LEU A O 1 ATOM 1091 C CB . LEU A 1 140 ? -3.029 7.836 1.238 1.00 28.37 ? 140 LEU A CB 1 ATOM 1092 C CG . LEU A 1 140 ? -2.114 8.951 0.721 1.00 29.32 ? 140 LEU A CG 1 ATOM 1093 C CD1 . LEU A 1 140 ? -0.887 8.355 0.049 1.00 30.11 ? 140 LEU A CD1 1 ATOM 1094 C CD2 . LEU A 1 140 ? -2.852 9.869 -0.238 1.00 29.90 ? 140 LEU A CD2 1 ATOM 1095 N N . HIS A 1 141 ? -5.098 6.214 3.191 1.00 29.56 ? 141 HIS A N 1 ATOM 1096 C CA . HIS A 1 141 ? -6.089 5.151 3.371 1.00 31.31 ? 141 HIS A CA 1 ATOM 1097 C C . HIS A 1 141 ? -6.523 5.036 4.814 1.00 29.82 ? 141 HIS A C 1 ATOM 1098 O O . HIS A 1 141 ? -5.702 4.952 5.725 1.00 31.11 ? 141 HIS A O 1 ATOM 1099 C CB . HIS A 1 141 ? -5.557 3.809 2.890 1.00 32.94 ? 141 HIS A CB 1 ATOM 1100 C CG . HIS A 1 141 ? -5.160 3.817 1.452 1.00 35.17 ? 141 HIS A CG 1 ATOM 1101 N ND1 . HIS A 1 141 ? -3.844 3.866 1.049 1.00 36.51 ? 141 HIS A ND1 1 ATOM 1102 C CD2 . HIS A 1 141 ? -5.905 3.828 0.321 1.00 35.98 ? 141 HIS A CD2 1 ATOM 1103 C CE1 . HIS A 1 141 ? -3.793 3.886 -0.271 1.00 36.85 ? 141 HIS A CE1 1 ATOM 1104 N NE2 . HIS A 1 141 ? -5.030 3.865 -0.736 1.00 36.75 ? 141 HIS A NE2 1 ATOM 1105 N N . TYR A 1 142 ? -7.834 4.986 4.993 1.00 28.14 ? 142 TYR A N 1 ATOM 1106 C CA . TYR A 1 142 ? -8.444 5.134 6.292 1.00 26.24 ? 142 TYR A CA 1 ATOM 1107 C C . TYR A 1 142 ? -8.014 4.067 7.294 1.00 26.04 ? 142 TYR A C 1 ATOM 1108 O O . TYR A 1 142 ? -8.105 2.872 7.029 1.00 25.54 ? 142 TYR A O 1 ATOM 1109 C CB . TYR A 1 142 ? -9.961 5.119 6.144 1.00 25.27 ? 142 TYR A CB 1 ATOM 1110 C CG . TYR A 1 142 ? -10.678 5.290 7.448 1.00 24.09 ? 142 TYR A CG 1 ATOM 1111 C CD1 . TYR A 1 142 ? -10.506 6.437 8.210 1.00 23.67 ? 142 TYR A CD1 1 ATOM 1112 C CD2 . TYR A 1 142 ? -11.526 4.304 7.925 1.00 23.91 ? 142 TYR A CD2 1 ATOM 1113 C CE1 . TYR A 1 142 ? -11.159 6.597 9.414 1.00 23.30 ? 142 TYR A CE1 1 ATOM 1114 C CE2 . TYR A 1 142 ? -12.181 4.449 9.125 1.00 23.63 ? 142 TYR A CE2 1 ATOM 1115 C CZ . TYR A 1 142 ? -12.002 5.603 9.863 1.00 23.25 ? 142 TYR A CZ 1 ATOM 1116 O OH . TYR A 1 142 ? -12.656 5.757 11.054 1.00 22.46 ? 142 TYR A OH 1 ATOM 1117 N N . ASP A 1 143 ? -7.557 4.534 8.446 1.00 25.22 ? 143 ASP A N 1 ATOM 1118 C CA . ASP A 1 143 ? -7.195 3.702 9.579 1.00 25.33 ? 143 ASP A CA 1 ATOM 1119 C C . ASP A 1 143 ? -7.223 4.692 10.748 1.00 24.10 ? 143 ASP A C 1 ATOM 1120 O O . ASP A 1 143 ? -6.283 5.463 10.923 1.00 23.18 ? 143 ASP A O 1 ATOM 1121 C CB . ASP A 1 143 ? -5.806 3.097 9.328 1.00 26.50 ? 143 ASP A CB 1 ATOM 1122 C CG . ASP A 1 143 ? -5.260 2.295 10.505 1.00 28.15 ? 143 ASP A CG 1 ATOM 1123 O OD1 . ASP A 1 143 ? -5.635 2.541 11.670 1.00 27.49 ? 143 ASP A OD1 1 ATOM 1124 O OD2 . ASP A 1 143 ? -4.403 1.418 10.247 1.00 30.55 ? 143 ASP A OD2 1 ATOM 1125 N N . SER A 1 144 ? -8.306 4.696 11.526 1.00 23.26 ? 144 SER A N 1 ATOM 1126 C CA . SER A 1 144 ? -8.543 5.802 12.473 1.00 23.41 ? 144 SER A CA 1 ATOM 1127 C C . SER A 1 144 ? -7.508 5.891 13.591 1.00 23.13 ? 144 SER A C 1 ATOM 1128 O O . SER A 1 144 ? -7.132 6.992 13.997 1.00 22.19 ? 144 SER A O 1 ATOM 1129 C CB . SER A 1 144 ? -9.960 5.764 13.058 1.00 23.53 ? 144 SER A CB 1 ATOM 1130 O OG . SER A 1 144 ? -10.138 4.677 13.939 1.00 24.21 ? 144 SER A OG 1 ATOM 1131 N N . THR A 1 145 ? -7.045 4.746 14.085 1.00 23.08 ? 145 THR A N 1 ATOM 1132 C CA . THR A 1 145 ? -5.983 4.732 15.091 1.00 23.37 ? 145 THR A CA 1 ATOM 1133 C C . THR A 1 145 ? -4.669 5.259 14.522 1.00 22.07 ? 145 THR A C 1 ATOM 1134 O O . THR A 1 145 ? -4.030 6.095 15.150 1.00 23.03 ? 145 THR A O 1 ATOM 1135 C CB . THR A 1 145 ? -5.758 3.326 15.677 1.00 24.42 ? 145 THR A CB 1 ATOM 1136 O OG1 . THR A 1 145 ? -6.987 2.847 16.230 1.00 24.91 ? 145 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 145 ? -4.689 3.354 16.769 1.00 24.64 ? 145 THR A CG2 1 ATOM 1138 N N . ALA A 1 146 ? -4.271 4.772 13.350 1.00 21.47 ? 146 ALA A N 1 ATOM 1139 C CA . ALA A 1 146 ? -3.053 5.255 12.688 1.00 20.86 ? 146 ALA A CA 1 ATOM 1140 C C . ALA A 1 146 ? -3.181 6.741 12.351 1.00 20.33 ? 146 ALA A C 1 ATOM 1141 O O . ALA A 1 146 ? -2.236 7.512 12.514 1.00 20.09 ? 146 ALA A O 1 ATOM 1142 C CB . ALA A 1 146 ? -2.774 4.455 11.426 1.00 20.90 ? 146 ALA A CB 1 ATOM 1143 N N . ALA A 1 147 ? -4.368 7.132 11.897 1.00 19.60 ? 147 ALA A N 1 ATOM 1144 C CA . ALA A 1 147 ? -4.634 8.512 11.506 1.00 19.22 ? 147 ALA A CA 1 ATOM 1145 C C . ALA A 1 147 ? -4.485 9.509 12.658 1.00 19.23 ? 147 ALA A C 1 ATOM 1146 O O . ALA A 1 147 ? -4.026 10.626 12.438 1.00 18.70 ? 147 ALA A O 1 ATOM 1147 C CB . ALA A 1 147 ? -6.018 8.620 10.899 1.00 19.06 ? 147 ALA A CB 1 ATOM 1148 N N . ALA A 1 148 ? -4.877 9.117 13.867 1.00 19.34 ? 148 ALA A N 1 ATOM 1149 C CA . ALA A 1 148 ? -4.730 9.983 15.045 1.00 19.36 ? 148 ALA A CA 1 ATOM 1150 C C . ALA A 1 148 ? -3.272 10.387 15.270 1.00 19.19 ? 148 ALA A C 1 ATOM 1151 O O . ALA A 1 148 ? -2.973 11.561 15.489 1.00 18.66 ? 148 ALA A O 1 ATOM 1152 C CB . ALA A 1 148 ? -5.281 9.301 16.285 1.00 19.85 ? 148 ALA A CB 1 ATOM 1153 N N . GLY A 1 149 ? -2.372 9.409 15.217 1.00 18.57 ? 149 GLY A N 1 ATOM 1154 C CA . GLY A 1 149 ? -0.941 9.677 15.313 1.00 18.42 ? 149 GLY A CA 1 ATOM 1155 C C . GLY A 1 149 ? -0.446 10.525 14.152 1.00 18.23 ? 149 GLY A C 1 ATOM 1156 O O . GLY A 1 149 ? 0.307 11.480 14.354 1.00 18.58 ? 149 GLY A O 1 ATOM 1157 N N . ALA A 1 150 ? -0.875 10.187 12.938 1.00 17.86 ? 150 ALA A N 1 ATOM 1158 C CA . ALA A 1 150 ? -0.489 10.951 11.753 1.00 17.68 ? 150 ALA A CA 1 ATOM 1159 C C . ALA A 1 150 ? -0.939 12.404 11.891 1.00 17.36 ? 150 ALA A C 1 ATOM 1160 O O . ALA A 1 150 ? -0.196 13.322 11.559 1.00 17.26 ? 150 ALA A O 1 ATOM 1161 C CB . ALA A 1 150 ? -1.070 10.335 10.495 1.00 17.58 ? 150 ALA A CB 1 ATOM 1162 N N . LEU A 1 151 ? -2.150 12.607 12.398 1.00 17.50 ? 151 LEU A N 1 ATOM 1163 C CA . LEU A 1 151 ? -2.685 13.956 12.549 1.00 18.04 ? 151 LEU A CA 1 ATOM 1164 C C . LEU A 1 151 ? -1.931 14.761 13.613 1.00 18.32 ? 151 LEU A C 1 ATOM 1165 O O . LEU A 1 151 ? -1.717 15.964 13.430 1.00 18.03 ? 151 LEU A O 1 ATOM 1166 C CB . LEU A 1 151 ? -4.200 13.921 12.809 1.00 18.39 ? 151 LEU A CB 1 ATOM 1167 C CG . LEU A 1 151 ? -5.014 13.508 11.573 1.00 18.49 ? 151 LEU A CG 1 ATOM 1168 C CD1 . LEU A 1 151 ? -6.397 13.005 11.969 1.00 18.90 ? 151 LEU A CD1 1 ATOM 1169 C CD2 . LEU A 1 151 ? -5.136 14.650 10.575 1.00 18.52 ? 151 LEU A CD2 1 ATOM 1170 N N . LEU A 1 152 ? -1.496 14.106 14.694 1.00 18.43 ? 152 LEU A N 1 ATOM 1171 C CA . LEU A 1 152 ? -0.644 14.767 15.691 1.00 18.47 ? 152 LEU A CA 1 ATOM 1172 C C . LEU A 1 152 ? 0.639 15.258 15.045 1.00 18.21 ? 152 LEU A C 1 ATOM 1173 O O . LEU A 1 152 ? 1.080 16.377 15.304 1.00 18.04 ? 152 LEU A O 1 ATOM 1174 C CB . LEU A 1 152 ? -0.322 13.836 16.867 1.00 18.60 ? 152 LEU A CB 1 ATOM 1175 C CG . LEU A 1 152 ? -1.514 13.572 17.791 1.00 18.80 ? 152 LEU A CG 1 ATOM 1176 C CD1 . LEU A 1 152 ? -1.252 12.408 18.732 1.00 19.46 ? 152 LEU A CD1 1 ATOM 1177 C CD2 . LEU A 1 152 ? -1.880 14.814 18.583 1.00 18.99 ? 152 LEU A CD2 1 ATOM 1178 N N . VAL A 1 153 ? 1.219 14.433 14.178 1.00 17.77 ? 153 VAL A N 1 ATOM 1179 C CA . VAL A 1 153 ? 2.411 14.832 13.436 1.00 18.08 ? 153 VAL A CA 1 ATOM 1180 C C . VAL A 1 153 ? 2.101 15.988 12.484 1.00 18.05 ? 153 VAL A C 1 ATOM 1181 O O . VAL A 1 153 ? 2.843 16.973 12.427 1.00 18.36 ? 153 VAL A O 1 ATOM 1182 C CB . VAL A 1 153 ? 3.016 13.650 12.651 1.00 17.81 ? 153 VAL A CB 1 ATOM 1183 C CG1 . VAL A 1 153 ? 4.153 14.119 11.756 1.00 17.68 ? 153 VAL A CG1 1 ATOM 1184 C CG2 . VAL A 1 153 ? 3.506 12.577 13.616 1.00 18.23 ? 153 VAL A CG2 1 ATOM 1185 N N . LEU A 1 154 ? 1.005 15.864 11.745 1.00 17.97 ? 154 LEU A N 1 ATOM 1186 C CA . LEU A 1 154 ? 0.629 16.854 10.739 1.00 18.72 ? 154 LEU A CA 1 ATOM 1187 C C . LEU A 1 154 ? 0.398 18.232 11.356 1.00 18.83 ? 154 LEU A C 1 ATOM 1188 O O . LEU A 1 154 ? 0.905 19.242 10.857 1.00 18.05 ? 154 LEU A O 1 ATOM 1189 C CB . LEU A 1 154 ? -0.637 16.397 10.013 1.00 19.48 ? 154 LEU A CB 1 ATOM 1190 C CG . LEU A 1 154 ? -1.271 17.366 9.016 1.00 20.13 ? 154 LEU A CG 1 ATOM 1191 C CD1 . LEU A 1 154 ? -0.346 17.593 7.837 1.00 20.63 ? 154 LEU A CD1 1 ATOM 1192 C CD2 . LEU A 1 154 ? -2.616 16.818 8.555 1.00 20.98 ? 154 LEU A CD2 1 ATOM 1193 N N . ILE A 1 155 ? -0.363 18.259 12.447 1.00 18.73 ? 155 ILE A N 1 ATOM 1194 C CA . ILE A 1 155 ? -0.715 19.518 13.114 1.00 19.18 ? 155 ILE A CA 1 ATOM 1195 C C . ILE A 1 155 ? 0.540 20.243 13.583 1.00 18.98 ? 155 ILE A C 1 ATOM 1196 O O . ILE A 1 155 ? 0.672 21.453 13.402 1.00 18.85 ? 155 ILE A O 1 ATOM 1197 C CB . ILE A 1 155 ? -1.662 19.273 14.309 1.00 19.65 ? 155 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 155 ? -3.046 18.859 13.800 1.00 20.41 ? 155 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 155 ? -1.781 20.514 15.185 1.00 19.91 ? 155 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 155 ? -3.879 18.137 14.833 1.00 20.63 ? 155 ILE A CD1 1 ATOM 1201 N N . GLN A 1 156 ? 1.466 19.495 14.175 1.00 18.59 ? 156 GLN A N 1 ATOM 1202 C CA . GLN A 1 156 ? 2.679 20.088 14.726 1.00 18.61 ? 156 GLN A CA 1 ATOM 1203 C C . GLN A 1 156 ? 3.669 20.560 13.669 1.00 18.61 ? 156 GLN A C 1 ATOM 1204 O O . GLN A 1 156 ? 4.365 21.558 13.879 1.00 18.64 ? 156 GLN A O 1 ATOM 1205 C CB . GLN A 1 156 ? 3.358 19.106 15.666 1.00 18.92 ? 156 GLN A CB 1 ATOM 1206 C CG . GLN A 1 156 ? 2.526 18.784 16.891 1.00 18.86 ? 156 GLN A CG 1 ATOM 1207 C CD . GLN A 1 156 ? 3.231 17.804 17.786 1.00 19.07 ? 156 GLN A CD 1 ATOM 1208 O OE1 . GLN A 1 156 ? 3.107 16.586 17.617 1.00 19.58 ? 156 GLN A OE1 1 ATOM 1209 N NE2 . GLN A 1 156 ? 3.994 18.320 18.732 1.00 18.63 ? 156 GLN A NE2 1 ATOM 1210 N N . THR A 1 157 ? 3.749 19.853 12.545 1.00 18.00 ? 157 THR A N 1 ATOM 1211 C CA . THR A 1 157 ? 4.712 20.204 11.501 1.00 18.07 ? 157 THR A CA 1 ATOM 1212 C C . THR A 1 157 ? 4.163 21.237 10.516 1.00 18.29 ? 157 THR A C 1 ATOM 1213 O O . THR A 1 157 ? 4.896 21.696 9.645 1.00 19.16 ? 157 THR A O 1 ATOM 1214 C CB . THR A 1 157 ? 5.194 18.968 10.707 1.00 17.81 ? 157 THR A CB 1 ATOM 1215 O OG1 . THR A 1 157 ? 4.072 18.300 10.123 1.00 18.55 ? 157 THR A OG1 1 ATOM 1216 C CG2 . THR A 1 157 ? 5.957 18.002 11.603 1.00 17.82 ? 157 THR A CG2 1 ATOM 1217 N N . THR A 1 158 ? 2.885 21.593 10.641 1.00 18.52 ? 158 THR A N 1 ATOM 1218 C CA . THR A 1 158 ? 2.285 22.615 9.784 1.00 19.23 ? 158 THR A CA 1 ATOM 1219 C C . THR A 1 158 ? 1.812 23.788 10.652 1.00 19.22 ? 158 THR A C 1 ATOM 1220 O O . THR A 1 158 ? 2.526 24.783 10.783 1.00 19.95 ? 158 THR A O 1 ATOM 1221 C CB . THR A 1 158 ? 1.144 22.038 8.916 1.00 18.95 ? 158 THR A CB 1 ATOM 1222 O OG1 . THR A 1 158 ? 0.077 21.569 9.751 1.00 18.75 ? 158 THR A OG1 1 ATOM 1223 C CG2 . THR A 1 158 ? 1.660 20.887 8.050 1.00 19.20 ? 158 THR A CG2 1 ATOM 1224 N N . ALA A 1 159 ? 0.645 23.651 11.277 1.00 19.38 ? 159 ALA A N 1 ATOM 1225 C CA . ALA A 1 159 ? 0.053 24.731 12.082 1.00 19.27 ? 159 ALA A CA 1 ATOM 1226 C C . ALA A 1 159 ? 0.973 25.280 13.177 1.00 19.39 ? 159 ALA A C 1 ATOM 1227 O O . ALA A 1 159 ? 1.170 26.493 13.270 1.00 19.23 ? 159 ALA A O 1 ATOM 1228 C CB . ALA A 1 159 ? -1.268 24.276 12.687 1.00 19.13 ? 159 ALA A CB 1 ATOM 1229 N N . GLU A 1 160 ? 1.543 24.400 13.998 1.00 18.83 ? 160 GLU A N 1 ATOM 1230 C CA . GLU A 1 160 ? 2.343 24.847 15.136 1.00 19.30 ? 160 GLU A CA 1 ATOM 1231 C C . GLU A 1 160 ? 3.634 25.526 14.672 1.00 18.85 ? 160 GLU A C 1 ATOM 1232 O O . GLU A 1 160 ? 4.060 26.519 15.264 1.00 18.86 ? 160 GLU A O 1 ATOM 1233 C CB . GLU A 1 160 ? 2.641 23.694 16.111 1.00 19.49 ? 160 GLU A CB 1 ATOM 1234 C CG . GLU A 1 160 ? 1.404 23.003 16.683 1.00 20.10 ? 160 GLU A CG 1 ATOM 1235 C CD . GLU A 1 160 ? 0.627 23.839 17.693 1.00 20.48 ? 160 GLU A CD 1 ATOM 1236 O OE1 . GLU A 1 160 ? 0.841 25.070 17.773 1.00 21.17 ? 160 GLU A OE1 1 ATOM 1237 O OE2 . GLU A 1 160 ? -0.208 23.260 18.422 1.00 20.09 ? 160 GLU A OE2 1 ATOM 1238 N N . ALA A 1 161 ? 4.234 25.006 13.602 1.00 18.67 ? 161 ALA A N 1 ATOM 1239 C CA . ALA A 1 161 ? 5.401 25.648 12.982 1.00 18.83 ? 161 ALA A CA 1 ATOM 1240 C C . ALA A 1 161 ? 5.052 27.012 12.393 1.00 18.87 ? 161 ALA A C 1 ATOM 1241 O O . ALA A 1 161 ? 5.864 27.939 12.458 1.00 19.71 ? 161 ALA A O 1 ATOM 1242 C CB . ALA A 1 161 ? 6.002 24.757 11.906 1.00 18.95 ? 161 ALA A CB 1 ATOM 1243 N N . ALA A 1 162 ? 3.862 27.142 11.811 1.00 18.89 ? 162 ALA A N 1 ATOM 1244 C CA . ALA A 1 162 ? 3.407 28.453 11.331 1.00 19.28 ? 162 ALA A CA 1 ATOM 1245 C C . ALA A 1 162 ? 3.274 29.444 12.493 1.00 19.81 ? 162 ALA A C 1 ATOM 1246 O O . ALA A 1 162 ? 3.628 30.614 12.352 1.00 20.66 ? 162 ALA A O 1 ATOM 1247 C CB . ALA A 1 162 ? 2.095 28.341 10.579 1.00 18.82 ? 162 ALA A CB 1 ATOM 1248 N N . ARG A 1 163 ? 2.787 28.971 13.635 1.00 20.31 ? 163 ARG A N 1 ATOM 1249 C CA . ARG A 1 163 ? 2.570 29.831 14.807 1.00 20.77 ? 163 ARG A CA 1 ATOM 1250 C C . ARG A 1 163 ? 3.840 30.274 15.529 1.00 21.01 ? 163 ARG A C 1 ATOM 1251 O O . ARG A 1 163 ? 3.868 31.361 16.116 1.00 21.25 ? 163 ARG A O 1 ATOM 1252 C CB . ARG A 1 163 ? 1.682 29.120 15.824 1.00 20.95 ? 163 ARG A CB 1 ATOM 1253 C CG . ARG A 1 163 ? 0.260 28.893 15.360 1.00 20.99 ? 163 ARG A CG 1 ATOM 1254 C CD . ARG A 1 163 ? -0.417 27.895 16.273 1.00 21.87 ? 163 ARG A CD 1 ATOM 1255 N NE . ARG A 1 163 ? -1.811 27.660 15.913 1.00 22.56 ? 163 ARG A NE 1 ATOM 1256 C CZ . ARG A 1 163 ? -2.500 26.568 16.246 1.00 24.25 ? 163 ARG A CZ 1 ATOM 1257 N NH1 . ARG A 1 163 ? -1.925 25.592 16.940 1.00 24.92 ? 163 ARG A NH1 1 ATOM 1258 N NH2 . ARG A 1 163 ? -3.764 26.436 15.873 1.00 23.81 ? 163 ARG A NH2 1 ATOM 1259 N N . PHE A 1 164 ? 4.870 29.431 15.522 1.00 20.66 ? 164 PHE A N 1 ATOM 1260 C CA . PHE A 1 164 ? 6.082 29.695 16.295 1.00 21.26 ? 164 PHE A CA 1 ATOM 1261 C C . PHE A 1 164 ? 7.332 29.413 15.482 1.00 22.34 ? 164 PHE A C 1 ATOM 1262 O O . PHE A 1 164 ? 7.529 28.293 15.008 1.00 21.43 ? 164 PHE A O 1 ATOM 1263 C CB . PHE A 1 164 ? 6.133 28.812 17.538 1.00 21.32 ? 164 PHE A CB 1 ATOM 1264 C CG . PHE A 1 164 ? 5.047 29.077 18.535 1.00 21.51 ? 164 PHE A CG 1 ATOM 1265 C CD1 . PHE A 1 164 ? 5.145 30.138 19.429 1.00 21.71 ? 164 PHE A CD1 1 ATOM 1266 C CD2 . PHE A 1 164 ? 3.946 28.233 18.618 1.00 21.73 ? 164 PHE A CD2 1 ATOM 1267 C CE1 . PHE A 1 164 ? 4.150 30.364 20.368 1.00 21.70 ? 164 PHE A CE1 1 ATOM 1268 C CE2 . PHE A 1 164 ? 2.948 28.456 19.551 1.00 21.96 ? 164 PHE A CE2 1 ATOM 1269 C CZ . PHE A 1 164 ? 3.051 29.522 20.432 1.00 21.83 ? 164 PHE A CZ 1 ATOM 1270 N N . LYS A 1 165 ? 8.191 30.419 15.355 1.00 22.94 ? 165 LYS A N 1 ATOM 1271 C CA . LYS A 1 165 ? 9.459 30.258 14.654 1.00 24.64 ? 165 LYS A CA 1 ATOM 1272 C C . LYS A 1 165 ? 10.341 29.175 15.285 1.00 23.55 ? 165 LYS A C 1 ATOM 1273 O O . LYS A 1 165 ? 11.024 28.439 14.571 1.00 23.64 ? 165 LYS A O 1 ATOM 1274 C CB . LYS A 1 165 ? 10.206 31.593 14.595 1.00 26.35 ? 165 LYS A CB 1 ATOM 1275 C CG . LYS A 1 165 ? 11.455 31.561 13.724 1.00 28.98 ? 165 LYS A CG 1 ATOM 1276 C CD . LYS A 1 165 ? 11.417 32.636 12.645 1.00 31.13 ? 165 LYS A CD 1 ATOM 1277 C CE . LYS A 1 165 ? 10.619 32.188 11.428 1.00 31.82 ? 165 LYS A CE 1 ATOM 1278 N NZ . LYS A 1 165 ? 11.490 31.781 10.284 1.00 32.03 ? 165 LYS A NZ 1 ATOM 1279 N N . TYR A 1 166 ? 10.321 29.074 16.611 1.00 23.63 ? 166 TYR A N 1 ATOM 1280 C CA . TYR A 1 166 ? 11.064 28.026 17.309 1.00 23.51 ? 166 TYR A CA 1 ATOM 1281 C C . TYR A 1 166 ? 10.651 26.630 16.820 1.00 22.39 ? 166 TYR A C 1 ATOM 1282 O O . TYR A 1 166 ? 11.503 25.767 16.607 1.00 21.62 ? 166 TYR A O 1 ATOM 1283 C CB . TYR A 1 166 ? 10.870 28.131 18.826 1.00 24.89 ? 166 TYR A CB 1 ATOM 1284 C CG . TYR A 1 166 ? 11.493 26.981 19.593 1.00 26.15 ? 166 TYR A CG 1 ATOM 1285 C CD1 . TYR A 1 166 ? 12.848 26.987 19.924 1.00 27.12 ? 166 TYR A CD1 1 ATOM 1286 C CD2 . TYR A 1 166 ? 10.730 25.881 19.973 1.00 26.58 ? 166 TYR A CD2 1 ATOM 1287 C CE1 . TYR A 1 166 ? 13.423 25.930 20.615 1.00 27.50 ? 166 TYR A CE1 1 ATOM 1288 C CE2 . TYR A 1 166 ? 11.295 24.823 20.662 1.00 27.17 ? 166 TYR A CE2 1 ATOM 1289 C CZ . TYR A 1 166 ? 12.642 24.850 20.981 1.00 27.66 ? 166 TYR A CZ 1 ATOM 1290 O OH . TYR A 1 166 ? 13.197 23.795 21.672 1.00 28.67 ? 166 TYR A OH 1 ATOM 1291 N N . ILE A 1 167 ? 9.350 26.411 16.642 1.00 21.38 ? 167 ILE A N 1 ATOM 1292 C CA . ILE A 1 167 ? 8.859 25.102 16.201 1.00 21.00 ? 167 ILE A CA 1 ATOM 1293 C C . ILE A 1 167 ? 9.246 24.833 14.741 1.00 21.10 ? 167 ILE A C 1 ATOM 1294 O O . ILE A 1 167 ? 9.693 23.731 14.411 1.00 21.43 ? 167 ILE A O 1 ATOM 1295 C CB . ILE A 1 167 ? 7.341 24.943 16.453 1.00 20.94 ? 167 ILE A CB 1 ATOM 1296 C CG1 . ILE A 1 167 ? 7.079 24.967 17.965 1.00 20.75 ? 167 ILE A CG1 1 ATOM 1297 C CG2 . ILE A 1 167 ? 6.826 23.646 15.833 1.00 20.80 ? 167 ILE A CG2 1 ATOM 1298 C CD1 . ILE A 1 167 ? 5.631 24.817 18.391 1.00 20.39 ? 167 ILE A CD1 1 ATOM 1299 N N . GLU A 1 168 ? 9.112 25.839 13.879 1.00 21.07 ? 168 GLU A N 1 ATOM 1300 C CA . GLU A 1 168 ? 9.608 25.740 12.505 1.00 21.80 ? 168 GLU A CA 1 ATOM 1301 C C . GLU A 1 168 ? 11.070 25.295 12.482 1.00 22.06 ? 168 GLU A C 1 ATOM 1302 O O . GLU A 1 168 ? 11.442 24.399 11.725 1.00 21.82 ? 168 GLU A O 1 ATOM 1303 C CB . GLU A 1 168 ? 9.461 27.078 11.771 1.00 22.20 ? 168 GLU A CB 1 ATOM 1304 C CG . GLU A 1 168 ? 10.112 27.116 10.394 1.00 23.03 ? 168 GLU A CG 1 ATOM 1305 C CD . GLU A 1 168 ? 10.112 28.498 9.767 1.00 23.88 ? 168 GLU A CD 1 ATOM 1306 O OE1 . GLU A 1 168 ? 9.657 29.466 10.414 1.00 24.11 ? 168 GLU A OE1 1 ATOM 1307 O OE2 . GLU A 1 168 ? 10.585 28.612 8.622 1.00 25.56 ? 168 GLU A OE2 1 ATOM 1308 N N . GLN A 1 169 ? 11.891 25.928 13.313 1.00 22.71 ? 169 GLN A N 1 ATOM 1309 C CA . GLN A 1 169 ? 13.310 25.589 13.395 1.00 23.90 ? 169 GLN A CA 1 ATOM 1310 C C . GLN A 1 169 ? 13.543 24.166 13.909 1.00 23.48 ? 169 GLN A C 1 ATOM 1311 O O . GLN A 1 169 ? 14.423 23.465 13.414 1.00 23.30 ? 169 GLN A O 1 ATOM 1312 C CB . GLN A 1 169 ? 14.047 26.619 14.250 1.00 25.81 ? 169 GLN A CB 1 ATOM 1313 C CG . GLN A 1 169 ? 14.082 27.987 13.579 1.00 27.65 ? 169 GLN A CG 1 ATOM 1314 C CD . GLN A 1 169 ? 14.574 29.098 14.487 1.00 29.95 ? 169 GLN A CD 1 ATOM 1315 O OE1 . GLN A 1 169 ? 14.434 29.034 15.708 1.00 32.56 ? 169 GLN A OE1 1 ATOM 1316 N NE2 . GLN A 1 169 ? 15.139 30.137 13.887 1.00 32.22 ? 169 GLN A NE2 1 ATOM 1317 N N . GLN A 1 170 ? 12.739 23.737 14.877 1.00 22.97 ? 170 GLN A N 1 ATOM 1318 C CA . GLN A 1 170 ? 12.828 22.378 15.403 1.00 23.52 ? 170 GLN A CA 1 ATOM 1319 C C . GLN A 1 170 ? 12.557 21.339 14.316 1.00 22.47 ? 170 GLN A C 1 ATOM 1320 O O . GLN A 1 170 ? 13.239 20.317 14.251 1.00 21.88 ? 170 GLN A O 1 ATOM 1321 C CB . GLN A 1 170 ? 11.862 22.184 16.578 1.00 24.33 ? 170 GLN A CB 1 ATOM 1322 C CG . GLN A 1 170 ? 12.273 22.931 17.835 1.00 25.87 ? 170 GLN A CG 1 ATOM 1323 C CD . GLN A 1 170 ? 13.524 22.357 18.470 1.00 27.41 ? 170 GLN A CD 1 ATOM 1324 O OE1 . GLN A 1 170 ? 14.589 22.986 18.462 1.00 29.72 ? 170 GLN A OE1 1 ATOM 1325 N NE2 . GLN A 1 170 ? 13.408 21.153 19.014 1.00 27.09 ? 170 GLN A NE2 1 ATOM 1326 N N . ILE A 1 171 ? 11.578 21.608 13.459 1.00 21.99 ? 171 ILE A N 1 ATOM 1327 C CA . ILE A 1 171 ? 11.266 20.703 12.356 1.00 21.89 ? 171 ILE A CA 1 ATOM 1328 C C . ILE A 1 171 ? 12.384 20.729 11.314 1.00 22.63 ? 171 ILE A C 1 ATOM 1329 O O . ILE A 1 171 ? 12.759 19.684 10.789 1.00 22.61 ? 171 ILE A O 1 ATOM 1330 C CB . ILE A 1 171 ? 9.893 21.017 11.719 1.00 21.46 ? 171 ILE A CB 1 ATOM 1331 C CG1 . ILE A 1 171 ? 8.785 20.989 12.781 1.00 21.28 ? 171 ILE A CG1 1 ATOM 1332 C CG2 . ILE A 1 171 ? 9.570 20.033 10.600 1.00 21.45 ? 171 ILE A CG2 1 ATOM 1333 C CD1 . ILE A 1 171 ? 8.773 19.763 13.674 1.00 21.17 ? 171 ILE A CD1 1 ATOM 1334 N N . GLN A 1 172 ? 12.935 21.908 11.035 1.00 22.98 ? 172 GLN A N 1 ATOM 1335 C CA . GLN A 1 172 ? 14.079 22.020 10.121 1.00 23.66 ? 172 GLN A CA 1 ATOM 1336 C C . GLN A 1 172 ? 15.274 21.187 10.591 1.00 23.95 ? 172 GLN A C 1 ATOM 1337 O O . GLN A 1 172 ? 15.972 20.589 9.776 1.00 24.04 ? 172 GLN A O 1 ATOM 1338 C CB . GLN A 1 172 ? 14.496 23.483 9.947 1.00 23.94 ? 172 GLN A CB 1 ATOM 1339 C CG . GLN A 1 172 ? 13.506 24.294 9.133 1.00 24.42 ? 172 GLN A CG 1 ATOM 1340 C CD . GLN A 1 172 ? 13.797 25.784 9.152 1.00 25.00 ? 172 GLN A CD 1 ATOM 1341 O OE1 . GLN A 1 172 ? 14.137 26.355 10.192 1.00 25.55 ? 172 GLN A OE1 1 ATOM 1342 N NE2 . GLN A 1 172 ? 13.660 26.425 7.998 1.00 25.50 ? 172 GLN A NE2 1 ATOM 1343 N N . GLU A 1 173 ? 15.495 21.144 11.901 1.00 24.80 ? 173 GLU A N 1 ATOM 1344 C CA . GLU A 1 173 ? 16.559 20.324 12.483 1.00 25.71 ? 173 GLU A CA 1 ATOM 1345 C C . GLU A 1 173 ? 16.269 18.832 12.310 1.00 24.82 ? 173 GLU A C 1 ATOM 1346 O O . GLU A 1 173 ? 17.191 18.009 12.311 1.00 23.87 ? 173 GLU A O 1 ATOM 1347 C CB . GLU A 1 173 ? 16.730 20.650 13.967 1.00 28.16 ? 173 GLU A CB 1 ATOM 1348 C CG . GLU A 1 173 ? 17.176 22.082 14.221 1.00 30.26 ? 173 GLU A CG 1 ATOM 1349 C CD . GLU A 1 173 ? 17.411 22.393 15.688 1.00 32.74 ? 173 GLU A CD 1 ATOM 1350 O OE1 . GLU A 1 173 ? 17.872 23.519 15.980 1.00 35.67 ? 173 GLU A OE1 1 ATOM 1351 O OE2 . GLU A 1 173 ? 17.142 21.524 16.549 1.00 34.47 ? 173 GLU A OE2 1 ATOM 1352 N N . ARG A 1 174 ? 14.985 18.503 12.161 1.00 22.86 ? 174 ARG A N 1 ATOM 1353 C CA . ARG A 1 174 ? 14.523 17.136 11.960 1.00 22.41 ? 174 ARG A CA 1 ATOM 1354 C C . ARG A 1 174 ? 14.166 16.872 10.497 1.00 22.20 ? 174 ARG A C 1 ATOM 1355 O O . ARG A 1 174 ? 13.248 16.093 10.205 1.00 22.30 ? 174 ARG A O 1 ATOM 1356 C CB . ARG A 1 174 ? 13.291 16.880 12.840 1.00 22.31 ? 174 ARG A CB 1 ATOM 1357 C CG . ARG A 1 174 ? 13.538 16.934 14.338 1.00 22.92 ? 174 ARG A CG 1 ATOM 1358 C CD . ARG A 1 174 ? 12.266 17.314 15.091 1.00 23.09 ? 174 ARG A CD 1 ATOM 1359 N NE . ARG A 1 174 ? 12.368 17.108 16.532 1.00 23.69 ? 174 ARG A NE 1 ATOM 1360 C CZ . ARG A 1 174 ? 13.092 17.860 17.362 1.00 24.29 ? 174 ARG A CZ 1 ATOM 1361 N NH1 . ARG A 1 174 ? 13.802 18.891 16.912 1.00 24.26 ? 174 ARG A NH1 1 ATOM 1362 N NH2 . ARG A 1 174 ? 13.110 17.574 18.657 1.00 25.23 ? 174 ARG A NH2 1 ATOM 1363 N N . ALA A 1 175 ? 14.889 17.501 9.571 1.00 22.08 ? 175 ALA A N 1 ATOM 1364 C CA . ALA A 1 175 ? 14.593 17.343 8.147 1.00 21.85 ? 175 ALA A CA 1 ATOM 1365 C C . ALA A 1 175 ? 14.890 15.931 7.652 1.00 21.79 ? 175 ALA A C 1 ATOM 1366 O O . ALA A 1 175 ? 14.236 15.466 6.734 1.00 21.70 ? 175 ALA A O 1 ATOM 1367 C CB . ALA A 1 175 ? 15.366 18.353 7.314 1.00 22.06 ? 175 ALA A CB 1 ATOM 1368 N N . TYR A 1 176 ? 15.883 15.268 8.245 1.00 22.12 ? 176 TYR A N 1 ATOM 1369 C CA . TYR A 1 176 ? 16.317 13.943 7.774 1.00 23.21 ? 176 TYR A CA 1 ATOM 1370 C C . TYR A 1 176 ? 16.368 12.884 8.886 1.00 23.26 ? 176 TYR A C 1 ATOM 1371 O O . TYR A 1 176 ? 16.799 11.746 8.653 1.00 22.36 ? 176 TYR A O 1 ATOM 1372 C CB . TYR A 1 176 ? 17.689 14.052 7.088 1.00 23.93 ? 176 TYR A CB 1 ATOM 1373 C CG . TYR A 1 176 ? 17.828 15.224 6.130 1.00 24.41 ? 176 TYR A CG 1 ATOM 1374 C CD1 . TYR A 1 176 ? 17.045 15.313 4.982 1.00 25.23 ? 176 TYR A CD1 1 ATOM 1375 C CD2 . TYR A 1 176 ? 18.756 16.236 6.365 1.00 25.59 ? 176 TYR A CD2 1 ATOM 1376 C CE1 . TYR A 1 176 ? 17.175 16.377 4.103 1.00 25.69 ? 176 TYR A CE1 1 ATOM 1377 C CE2 . TYR A 1 176 ? 18.891 17.303 5.492 1.00 26.24 ? 176 TYR A CE2 1 ATOM 1378 C CZ . TYR A 1 176 ? 18.100 17.369 4.365 1.00 26.17 ? 176 TYR A CZ 1 ATOM 1379 O OH . TYR A 1 176 ? 18.230 18.422 3.494 1.00 27.91 ? 176 TYR A OH 1 ATOM 1380 N N . ARG A 1 177 ? 15.921 13.267 10.079 1.00 23.87 ? 177 ARG A N 1 ATOM 1381 C CA . ARG A 1 177 ? 15.862 12.390 11.244 1.00 25.32 ? 177 ARG A CA 1 ATOM 1382 C C . ARG A 1 177 ? 14.771 12.900 12.173 1.00 24.78 ? 177 ARG A C 1 ATOM 1383 O O . ARG A 1 177 ? 14.861 14.026 12.677 1.00 24.99 ? 177 ARG A O 1 ATOM 1384 C CB . ARG A 1 177 ? 17.195 12.386 12.003 1.00 27.04 ? 177 ARG A CB 1 ATOM 1385 C CG . ARG A 1 177 ? 17.167 11.542 13.274 1.00 29.37 ? 177 ARG A CG 1 ATOM 1386 C CD . ARG A 1 177 ? 18.512 11.504 13.979 1.00 31.49 ? 177 ARG A CD 1 ATOM 1387 N NE . ARG A 1 177 ? 18.925 12.826 14.450 1.00 33.28 ? 177 ARG A NE 1 ATOM 1388 C CZ . ARG A 1 177 ? 20.109 13.098 14.998 1.00 35.13 ? 177 ARG A CZ 1 ATOM 1389 N NH1 . ARG A 1 177 ? 21.018 12.142 15.152 1.00 36.27 ? 177 ARG A NH1 1 ATOM 1390 N NH2 . ARG A 1 177 ? 20.390 14.335 15.394 1.00 35.95 ? 177 ARG A NH2 1 ATOM 1391 N N . ASP A 1 178 ? 13.756 12.071 12.415 1.00 23.85 ? 178 ASP A N 1 ATOM 1392 C CA . ASP A 1 178 ? 12.703 12.410 13.365 1.00 23.28 ? 178 ASP A CA 1 ATOM 1393 C C . ASP A 1 178 ? 13.213 12.392 14.799 1.00 24.06 ? 178 ASP A C 1 ATOM 1394 O O . ASP A 1 178 ? 14.139 11.652 15.144 1.00 23.78 ? 178 ASP A O 1 ATOM 1395 C CB . ASP A 1 178 ? 11.519 11.433 13.273 1.00 22.65 ? 178 ASP A CB 1 ATOM 1396 C CG . ASP A 1 178 ? 10.813 11.477 11.937 1.00 22.23 ? 178 ASP A CG 1 ATOM 1397 O OD1 . ASP A 1 178 ? 10.763 12.551 11.304 1.00 21.55 ? 178 ASP A OD1 1 ATOM 1398 O OD2 . ASP A 1 178 ? 10.286 10.424 11.519 1.00 21.59 ? 178 ASP A OD2 1 ATOM 1399 N N . GLU A 1 179 ? 12.582 13.203 15.637 1.00 23.78 ? 179 GLU A N 1 ATOM 1400 C CA . GLU A 1 179 ? 12.843 13.190 17.062 1.00 24.76 ? 179 GLU A CA 1 ATOM 1401 C C . GLU A 1 179 ? 11.612 13.718 17.769 1.00 24.36 ? 179 GLU A C 1 ATOM 1402 O O . GLU A 1 179 ? 10.935 14.611 17.256 1.00 23.42 ? 179 GLU A O 1 ATOM 1403 C CB . GLU A 1 179 ? 14.070 14.046 17.386 1.00 26.21 ? 179 GLU A CB 1 ATOM 1404 C CG . GLU A 1 179 ? 14.446 14.097 18.862 1.00 27.89 ? 179 GLU A CG 1 ATOM 1405 C CD . GLU A 1 179 ? 15.688 14.930 19.125 1.00 29.71 ? 179 GLU A CD 1 ATOM 1406 O OE1 . GLU A 1 179 ? 16.545 15.044 18.221 1.00 31.76 ? 179 GLU A OE1 1 ATOM 1407 O OE2 . GLU A 1 179 ? 15.814 15.467 20.243 1.00 31.52 ? 179 GLU A OE2 1 ATOM 1408 N N . VAL A 1 180 ? 11.306 13.159 18.935 1.00 24.08 ? 180 VAL A N 1 ATOM 1409 C CA . VAL A 1 180 ? 10.167 13.650 19.707 1.00 24.57 ? 180 VAL A CA 1 ATOM 1410 C C . VAL A 1 180 ? 10.344 15.151 19.975 1.00 24.40 ? 180 VAL A C 1 ATOM 1411 O O . VAL A 1 180 ? 11.474 15.644 20.048 1.00 23.36 ? 180 VAL A O 1 ATOM 1412 C CB . VAL A 1 180 ? 9.950 12.871 21.025 1.00 24.84 ? 180 VAL A CB 1 ATOM 1413 C CG1 . VAL A 1 180 ? 9.555 11.426 20.736 1.00 25.08 ? 180 VAL A CG1 1 ATOM 1414 C CG2 . VAL A 1 180 ? 11.177 12.934 21.932 1.00 25.10 ? 180 VAL A CG2 1 ATOM 1415 N N . PRO A 1 181 ? 9.231 15.890 20.083 1.00 24.84 ? 181 PRO A N 1 ATOM 1416 C CA . PRO A 1 181 ? 9.335 17.337 20.294 1.00 25.34 ? 181 PRO A CA 1 ATOM 1417 C C . PRO A 1 181 ? 10.026 17.696 21.607 1.00 26.07 ? 181 PRO A C 1 ATOM 1418 O O . PRO A 1 181 ? 9.895 16.968 22.590 1.00 26.47 ? 181 PRO A O 1 ATOM 1419 C CB . PRO A 1 181 ? 7.871 17.801 20.320 1.00 25.18 ? 181 PRO A CB 1 ATOM 1420 C CG . PRO A 1 181 ? 7.073 16.578 20.604 1.00 25.09 ? 181 PRO A CG 1 ATOM 1421 C CD . PRO A 1 181 ? 7.832 15.442 19.995 1.00 24.96 ? 181 PRO A CD 1 ATOM 1422 N N . SER A 1 182 ? 10.761 18.806 21.620 1.00 26.81 ? 182 SER A N 1 ATOM 1423 C CA . SER A 1 182 ? 11.346 19.314 22.858 1.00 27.69 ? 182 SER A CA 1 ATOM 1424 C C . SER A 1 182 ? 10.233 19.702 23.837 1.00 28.32 ? 182 SER A C 1 ATOM 1425 O O . SER A 1 182 ? 9.105 19.979 23.428 1.00 27.54 ? 182 SER A O 1 ATOM 1426 C CB . SER A 1 182 ? 12.257 20.512 22.573 1.00 27.79 ? 182 SER A CB 1 ATOM 1427 O OG . SER A 1 182 ? 11.530 21.621 22.064 1.00 28.41 ? 182 SER A OG 1 ATOM 1428 N N . SER A 1 183 ? 10.543 19.705 25.130 1.00 29.43 ? 183 SER A N 1 ATOM 1429 C CA . SER A 1 183 ? 9.571 20.131 26.139 1.00 30.08 ? 183 SER A CA 1 ATOM 1430 C C . SER A 1 183 ? 9.116 21.573 25.883 1.00 28.93 ? 183 SER A C 1 ATOM 1431 O O . SER A 1 183 ? 7.960 21.914 26.126 1.00 28.95 ? 183 SER A O 1 ATOM 1432 C CB . SER A 1 183 ? 10.152 19.997 27.549 1.00 32.30 ? 183 SER A CB 1 ATOM 1433 O OG . SER A 1 183 ? 10.439 18.638 27.851 1.00 35.16 ? 183 SER A OG 1 ATOM 1434 N N . ALA A 1 184 ? 10.026 22.405 25.381 1.00 28.37 ? 184 ALA A N 1 ATOM 1435 C CA . ALA A 1 184 ? 9.699 23.780 24.985 1.00 27.86 ? 184 ALA A CA 1 ATOM 1436 C C . ALA A 1 184 ? 8.652 23.818 23.871 1.00 27.15 ? 184 ALA A C 1 ATOM 1437 O O . ALA A 1 184 ? 7.726 24.636 23.898 1.00 26.24 ? 184 ALA A O 1 ATOM 1438 C CB . ALA A 1 184 ? 10.956 24.511 24.539 1.00 28.17 ? 184 ALA A CB 1 ATOM 1439 N N . THR A 1 185 ? 8.810 22.935 22.889 1.00 25.78 ? 185 THR A N 1 ATOM 1440 C CA . THR A 1 185 ? 7.856 22.824 21.786 1.00 25.24 ? 185 THR A CA 1 ATOM 1441 C C . THR A 1 185 ? 6.461 22.544 22.327 1.00 24.86 ? 185 THR A C 1 ATOM 1442 O O . THR A 1 185 ? 5.508 23.237 21.986 1.00 24.96 ? 185 THR A O 1 ATOM 1443 C CB . THR A 1 185 ? 8.264 21.698 20.809 1.00 24.52 ? 185 THR A CB 1 ATOM 1444 O OG1 . THR A 1 185 ? 9.473 22.065 20.137 1.00 24.53 ? 185 THR A OG1 1 ATOM 1445 C CG2 . THR A 1 185 ? 7.174 21.437 19.777 1.00 24.17 ? 185 THR A CG2 1 ATOM 1446 N N . ILE A 1 186 ? 6.353 21.534 23.185 1.00 25.07 ? 186 ILE A N 1 ATOM 1447 C CA . ILE A 1 186 ? 5.071 21.166 23.785 1.00 25.49 ? 186 ILE A CA 1 ATOM 1448 C C . ILE A 1 186 ? 4.485 22.346 24.567 1.00 25.33 ? 186 ILE A C 1 ATOM 1449 O O . ILE A 1 186 ? 3.285 22.631 24.477 1.00 24.04 ? 186 ILE A O 1 ATOM 1450 C CB . ILE A 1 186 ? 5.210 19.948 24.727 1.00 26.15 ? 186 ILE A CB 1 ATOM 1451 C CG1 . ILE A 1 186 ? 5.691 18.706 23.956 1.00 26.60 ? 186 ILE A CG1 1 ATOM 1452 C CG2 . ILE A 1 186 ? 3.889 19.653 25.427 1.00 26.48 ? 186 ILE A CG2 1 ATOM 1453 C CD1 . ILE A 1 186 ? 4.683 18.130 22.984 1.00 27.06 ? 186 ILE A CD1 1 ATOM 1454 N N . SER A 1 187 ? 5.346 23.028 25.316 1.00 25.48 ? 187 SER A N 1 ATOM 1455 C CA . SER A 1 187 ? 4.935 24.168 26.134 1.00 26.04 ? 187 SER A CA 1 ATOM 1456 C C . SER A 1 187 ? 4.330 25.279 25.278 1.00 25.04 ? 187 SER A C 1 ATOM 1457 O O . SER A 1 187 ? 3.265 25.813 25.602 1.00 25.75 ? 187 SER A O 1 ATOM 1458 C CB . SER A 1 187 ? 6.129 24.710 26.921 1.00 26.75 ? 187 SER A CB 1 ATOM 1459 O OG . SER A 1 187 ? 5.733 25.778 27.764 1.00 28.17 ? 187 SER A OG 1 ATOM 1460 N N . LEU A 1 188 ? 5.008 25.615 24.185 1.00 24.37 ? 188 LEU A N 1 ATOM 1461 C CA . LEU A 1 188 ? 4.533 26.649 23.265 1.00 23.84 ? 188 LEU A CA 1 ATOM 1462 C C . LEU A 1 188 ? 3.202 26.278 22.623 1.00 22.99 ? 188 LEU A C 1 ATOM 1463 O O . LEU A 1 188 ? 2.299 27.108 22.545 1.00 21.76 ? 188 LEU A O 1 ATOM 1464 C CB . LEU A 1 188 ? 5.562 26.914 22.169 1.00 24.23 ? 188 LEU A CB 1 ATOM 1465 C CG . LEU A 1 188 ? 6.873 27.545 22.626 1.00 24.41 ? 188 LEU A CG 1 ATOM 1466 C CD1 . LEU A 1 188 ? 7.910 27.397 21.530 1.00 24.58 ? 188 LEU A CD1 1 ATOM 1467 C CD2 . LEU A 1 188 ? 6.670 29.006 23.008 1.00 24.38 ? 188 LEU A CD2 1 ATOM 1468 N N . GLU A 1 189 ? 3.084 25.037 22.155 1.00 22.38 ? 189 GLU A N 1 ATOM 1469 C CA . GLU A 1 189 ? 1.825 24.555 21.578 1.00 22.40 ? 189 GLU A CA 1 ATOM 1470 C C . GLU A 1 189 ? 0.686 24.767 22.565 1.00 22.83 ? 189 GLU A C 1 ATOM 1471 O O . GLU A 1 189 ? -0.370 25.298 22.219 1.00 22.65 ? 189 GLU A O 1 ATOM 1472 C CB . GLU A 1 189 ? 1.921 23.065 21.241 1.00 22.27 ? 189 GLU A CB 1 ATOM 1473 C CG . GLU A 1 189 ? 2.886 22.739 20.109 1.00 22.11 ? 189 GLU A CG 1 ATOM 1474 C CD . GLU A 1 189 ? 3.126 21.247 19.944 1.00 22.20 ? 189 GLU A CD 1 ATOM 1475 O OE1 . GLU A 1 189 ? 2.579 20.451 20.735 1.00 22.47 ? 189 GLU A OE1 1 ATOM 1476 O OE2 . GLU A 1 189 ? 3.874 20.874 19.016 1.00 21.62 ? 189 GLU A OE2 1 ATOM 1477 N N . ASN A 1 190 ? 0.925 24.357 23.807 1.00 23.89 ? 190 ASN A N 1 ATOM 1478 C CA . ASN A 1 190 ? -0.071 24.457 24.871 1.00 24.93 ? 190 ASN A CA 1 ATOM 1479 C C . ASN A 1 190 ? -0.398 25.894 25.286 1.00 25.58 ? 190 ASN A C 1 ATOM 1480 O O . ASN A 1 190 ? -1.453 26.137 25.867 1.00 26.35 ? 190 ASN A O 1 ATOM 1481 C CB . ASN A 1 190 ? 0.398 23.673 26.103 1.00 25.35 ? 190 ASN A CB 1 ATOM 1482 C CG . ASN A 1 190 ? 0.354 22.168 25.897 1.00 25.98 ? 190 ASN A CG 1 ATOM 1483 O OD1 . ASN A 1 190 ? -0.306 21.670 24.985 1.00 26.20 ? 190 ASN A OD1 1 ATOM 1484 N ND2 . ASN A 1 190 ? 1.056 21.434 26.756 1.00 25.95 ? 190 ASN A ND2 1 ATOM 1485 N N . SER A 1 191 ? 0.502 26.831 24.989 1.00 26.16 ? 191 SER A N 1 ATOM 1486 C CA . SER A 1 191 ? 0.379 28.223 25.444 1.00 26.21 ? 191 SER A CA 1 ATOM 1487 C C . SER A 1 191 ? -0.031 29.230 24.364 1.00 25.72 ? 191 SER A C 1 ATOM 1488 O O . SER A 1 191 ? -0.093 30.435 24.640 1.00 25.49 ? 191 SER A O 1 ATOM 1489 C CB . SER A 1 191 ? 1.714 28.674 26.037 1.00 26.63 ? 191 SER A CB 1 ATOM 1490 O OG . SER A 1 191 ? 2.153 27.777 27.043 1.00 27.98 ? 191 SER A OG 1 ATOM 1491 N N . TRP A 1 192 ? -0.307 28.763 23.150 1.00 24.27 ? 192 TRP A N 1 ATOM 1492 C CA . TRP A 1 192 ? -0.553 29.678 22.038 1.00 23.92 ? 192 TRP A CA 1 ATOM 1493 C C . TRP A 1 192 ? -1.757 30.578 22.300 1.00 24.98 ? 192 TRP A C 1 ATOM 1494 O O . TRP A 1 192 ? -1.686 31.789 22.081 1.00 24.91 ? 192 TRP A O 1 ATOM 1495 C CB . TRP A 1 192 ? -0.741 28.927 20.722 1.00 22.64 ? 192 TRP A CB 1 ATOM 1496 C CG . TRP A 1 192 ? -0.919 29.845 19.544 1.00 21.69 ? 192 TRP A CG 1 ATOM 1497 C CD1 . TRP A 1 192 ? -0.035 30.784 19.097 1.00 21.13 ? 192 TRP A CD1 1 ATOM 1498 C CD2 . TRP A 1 192 ? -2.050 29.910 18.666 1.00 20.96 ? 192 TRP A CD2 1 ATOM 1499 N NE1 . TRP A 1 192 ? -0.548 31.433 17.998 1.00 20.90 ? 192 TRP A NE1 1 ATOM 1500 C CE2 . TRP A 1 192 ? -1.782 30.915 17.711 1.00 20.46 ? 192 TRP A CE2 1 ATOM 1501 C CE3 . TRP A 1 192 ? -3.265 29.218 18.594 1.00 20.82 ? 192 TRP A CE3 1 ATOM 1502 C CZ2 . TRP A 1 192 ? -2.682 31.241 16.692 1.00 20.55 ? 192 TRP A CZ2 1 ATOM 1503 C CZ3 . TRP A 1 192 ? -4.155 29.543 17.586 1.00 20.55 ? 192 TRP A CZ3 1 ATOM 1504 C CH2 . TRP A 1 192 ? -3.859 30.541 16.645 1.00 20.33 ? 192 TRP A CH2 1 ATOM 1505 N N . SER A 1 193 ? -2.852 29.985 22.767 1.00 25.66 ? 193 SER A N 1 ATOM 1506 C CA . SER A 1 193 ? -4.053 30.753 23.089 1.00 27.51 ? 193 SER A CA 1 ATOM 1507 C C . SER A 1 193 ? -3.780 31.763 24.203 1.00 27.32 ? 193 SER A C 1 ATOM 1508 O O . SER A 1 193 ? -4.107 32.947 24.072 1.00 26.98 ? 193 SER A O 1 ATOM 1509 C CB . SER A 1 193 ? -5.193 29.822 23.504 1.00 28.78 ? 193 SER A CB 1 ATOM 1510 O OG . SER A 1 193 ? -6.408 30.542 23.617 1.00 30.37 ? 193 SER A OG 1 ATOM 1511 N N . GLY A 1 194 ? -3.183 31.282 25.291 1.00 27.40 ? 194 GLY A N 1 ATOM 1512 C CA . GLY A 1 194 ? -2.807 32.127 26.421 1.00 28.45 ? 194 GLY A CA 1 ATOM 1513 C C . GLY A 1 194 ? -1.910 33.285 26.024 1.00 28.34 ? 194 GLY A C 1 ATOM 1514 O O . GLY A 1 194 ? -2.175 34.428 26.390 1.00 28.28 ? 194 GLY A O 1 ATOM 1515 N N . LEU A 1 195 ? -0.852 32.993 25.269 1.00 28.19 ? 195 LEU A N 1 ATOM 1516 C CA . LEU A 1 195 ? 0.069 34.034 24.795 1.00 28.02 ? 195 LEU A CA 1 ATOM 1517 C C . LEU A 1 195 ? -0.610 35.045 23.886 1.00 27.83 ? 195 LEU A C 1 ATOM 1518 O O . LEU A 1 195 ? -0.366 36.253 23.994 1.00 26.54 ? 195 LEU A O 1 ATOM 1519 C CB . LEU A 1 195 ? 1.240 33.424 24.026 1.00 28.63 ? 195 LEU A CB 1 ATOM 1520 C CG . LEU A 1 195 ? 2.348 32.763 24.838 1.00 29.23 ? 195 LEU A CG 1 ATOM 1521 C CD1 . LEU A 1 195 ? 3.240 31.958 23.902 1.00 29.73 ? 195 LEU A CD1 1 ATOM 1522 C CD2 . LEU A 1 195 ? 3.161 33.798 25.606 1.00 29.47 ? 195 LEU A CD2 1 ATOM 1523 N N . SER A 1 196 ? -1.428 34.541 22.967 1.00 26.78 ? 196 SER A N 1 ATOM 1524 C CA . SER A 1 196 ? -2.162 35.388 22.037 1.00 27.29 ? 196 SER A CA 1 ATOM 1525 C C . SER A 1 196 ? -3.033 36.371 22.813 1.00 28.05 ? 196 SER A C 1 ATOM 1526 O O . SER A 1 196 ? -3.061 37.567 22.508 1.00 27.30 ? 196 SER A O 1 ATOM 1527 C CB . SER A 1 196 ? -3.018 34.532 21.097 1.00 26.86 ? 196 SER A CB 1 ATOM 1528 O OG . SER A 1 196 ? -2.205 33.807 20.185 1.00 26.23 ? 196 SER A OG 1 ATOM 1529 N N . LYS A 1 197 ? -3.722 35.860 23.829 1.00 28.71 ? 197 LYS A N 1 ATOM 1530 C CA . LYS A 1 197 ? -4.562 36.684 24.692 1.00 30.01 ? 197 LYS A CA 1 ATOM 1531 C C . LYS A 1 197 ? -3.760 37.774 25.409 1.00 29.67 ? 197 LYS A C 1 ATOM 1532 O O . LYS A 1 197 ? -4.109 38.952 25.333 1.00 28.54 ? 197 LYS A O 1 ATOM 1533 C CB . LYS A 1 197 ? -5.273 35.809 25.724 1.00 31.77 ? 197 LYS A CB 1 ATOM 1534 C CG . LYS A 1 197 ? -6.317 36.542 26.551 1.00 33.63 ? 197 LYS A CG 1 ATOM 1535 C CD . LYS A 1 197 ? -6.996 35.599 27.529 1.00 35.24 ? 197 LYS A CD 1 ATOM 1536 C CE . LYS A 1 197 ? -7.975 36.338 28.425 1.00 37.13 ? 197 LYS A CE 1 ATOM 1537 N NZ . LYS A 1 197 ? -8.684 35.409 29.349 1.00 38.25 ? 197 LYS A NZ 1 ATOM 1538 N N . GLN A 1 198 ? -2.691 37.378 26.097 1.00 29.46 ? 198 GLN A N 1 ATOM 1539 C CA . GLN A 1 198 ? -1.906 38.312 26.913 1.00 29.49 ? 198 GLN A CA 1 ATOM 1540 C C . GLN A 1 198 ? -1.202 39.386 26.089 1.00 28.95 ? 198 GLN A C 1 ATOM 1541 O O . GLN A 1 198 ? -1.060 40.528 26.540 1.00 28.41 ? 198 GLN A O 1 ATOM 1542 C CB . GLN A 1 198 ? -0.886 37.558 27.775 1.00 30.33 ? 198 GLN A CB 1 ATOM 1543 C CG . GLN A 1 198 ? -1.509 36.678 28.844 1.00 31.17 ? 198 GLN A CG 1 ATOM 1544 C CD . GLN A 1 198 ? -2.411 37.461 29.779 1.00 32.51 ? 198 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 198 ? -2.040 38.540 30.250 1.00 33.12 ? 198 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 198 ? -3.604 36.934 30.044 1.00 33.14 ? 198 GLN A NE2 1 ATOM 1547 N N . ILE A 1 199 ? -0.765 39.024 24.886 1.00 27.72 ? 199 ILE A N 1 ATOM 1548 C CA . ILE A 1 199 ? -0.156 39.984 23.972 1.00 27.29 ? 199 ILE A CA 1 ATOM 1549 C C . ILE A 1 199 ? -1.184 41.042 23.558 1.00 27.82 ? 199 ILE A C 1 ATOM 1550 O O . ILE A 1 199 ? -0.862 42.227 23.482 1.00 27.59 ? 199 ILE A O 1 ATOM 1551 C CB . ILE A 1 199 ? 0.450 39.282 22.734 1.00 26.66 ? 199 ILE A CB 1 ATOM 1552 C CG1 . ILE A 1 199 ? 1.679 38.471 23.149 1.00 26.42 ? 199 ILE A CG1 1 ATOM 1553 C CG2 . ILE A 1 199 ? 0.864 40.294 21.673 1.00 26.66 ? 199 ILE A CG2 1 ATOM 1554 C CD1 . ILE A 1 199 ? 2.166 37.499 22.094 1.00 25.89 ? 199 ILE A CD1 1 ATOM 1555 N N . GLN A 1 200 ? -2.418 40.613 23.304 1.00 28.21 ? 200 GLN A N 1 ATOM 1556 C CA . GLN A 1 200 ? -3.492 41.548 22.985 1.00 28.84 ? 200 GLN A CA 1 ATOM 1557 C C . GLN A 1 200 ? -3.895 42.392 24.199 1.00 29.95 ? 200 GLN A C 1 ATOM 1558 O O . GLN A 1 200 ? -4.150 43.585 24.058 1.00 30.70 ? 200 GLN A O 1 ATOM 1559 C CB . GLN A 1 200 ? -4.702 40.815 22.404 1.00 28.57 ? 200 GLN A CB 1 ATOM 1560 C CG . GLN A 1 200 ? -4.530 40.448 20.941 1.00 28.52 ? 200 GLN A CG 1 ATOM 1561 C CD . GLN A 1 200 ? -5.484 39.357 20.501 1.00 28.58 ? 200 GLN A CD 1 ATOM 1562 O OE1 . GLN A 1 200 ? -6.587 39.636 20.045 1.00 29.37 ? 200 GLN A OE1 1 ATOM 1563 N NE2 . GLN A 1 200 ? -5.069 38.106 20.655 1.00 28.45 ? 200 GLN A NE2 1 ATOM 1564 N N . LEU A 1 201 ? -3.934 41.783 25.383 1.00 30.67 ? 201 LEU A N 1 ATOM 1565 C CA . LEU A 1 201 ? -4.250 42.520 26.616 1.00 32.43 ? 201 LEU A CA 1 ATOM 1566 C C . LEU A 1 201 ? -3.184 43.554 26.960 1.00 32.90 ? 201 LEU A C 1 ATOM 1567 O O . LEU A 1 201 ? -3.469 44.554 27.615 1.00 33.12 ? 201 LEU A O 1 ATOM 1568 C CB . LEU A 1 201 ? -4.421 41.565 27.800 1.00 33.00 ? 201 LEU A CB 1 ATOM 1569 C CG . LEU A 1 201 ? -5.665 40.676 27.788 1.00 33.84 ? 201 LEU A CG 1 ATOM 1570 C CD1 . LEU A 1 201 ? -5.615 39.687 28.939 1.00 34.29 ? 201 LEU A CD1 1 ATOM 1571 C CD2 . LEU A 1 201 ? -6.924 41.516 27.876 1.00 34.63 ? 201 LEU A CD2 1 ATOM 1572 N N . ALA A 1 202 ? -1.958 43.305 26.515 1.00 32.59 ? 202 ALA A N 1 ATOM 1573 C CA . ALA A 1 202 ? -0.846 44.210 26.770 1.00 33.57 ? 202 ALA A CA 1 ATOM 1574 C C . ALA A 1 202 ? -0.947 45.539 25.998 1.00 34.54 ? 202 ALA A C 1 ATOM 1575 O O . ALA A 1 202 ? -0.291 46.512 26.378 1.00 34.05 ? 202 ALA A O 1 ATOM 1576 C CB . ALA A 1 202 ? 0.468 43.507 26.460 1.00 33.37 ? 202 ALA A CB 1 ATOM 1577 N N . GLN A 1 203 ? -1.763 45.584 24.939 1.00 35.91 ? 203 GLN A N 1 ATOM 1578 C CA . GLN A 1 203 ? -1.926 46.795 24.108 1.00 37.85 ? 203 GLN A CA 1 ATOM 1579 C C . GLN A 1 203 ? -2.323 48.034 24.911 1.00 37.97 ? 203 GLN A C 1 ATOM 1580 O O . GLN A 1 203 ? -1.887 49.145 24.593 1.00 40.50 ? 203 GLN A O 1 ATOM 1581 C CB . GLN A 1 203 ? -3.002 46.604 23.030 1.00 39.63 ? 203 GLN A CB 1 ATOM 1582 C CG . GLN A 1 203 ? -2.730 45.564 21.955 1.00 41.67 ? 203 GLN A CG 1 ATOM 1583 C CD . GLN A 1 203 ? -3.865 45.502 20.942 1.00 42.82 ? 203 GLN A CD 1 ATOM 1584 O OE1 . GLN A 1 203 ? -3.912 46.300 20.003 1.00 44.30 ? 203 GLN A OE1 1 ATOM 1585 N NE2 . GLN A 1 203 ? -4.794 44.564 21.135 1.00 43.24 ? 203 GLN A NE2 1 ATOM 1586 N N . GLY A 1 204 ? -3.180 47.844 25.913 1.00 36.14 ? 204 GLY A N 1 ATOM 1587 C CA . GLY A 1 204 ? -3.639 48.936 26.778 1.00 34.14 ? 204 GLY A CA 1 ATOM 1588 C C . GLY A 1 204 ? -3.139 48.805 28.205 1.00 32.89 ? 204 GLY A C 1 ATOM 1589 O O . GLY A 1 204 ? -3.719 49.370 29.131 1.00 32.86 ? 204 GLY A O 1 ATOM 1590 N N . ASN A 1 205 ? -2.054 48.058 28.379 1.00 30.79 ? 205 ASN A N 1 ATOM 1591 C CA . ASN A 1 205 ? -1.473 47.819 29.690 1.00 29.70 ? 205 ASN A CA 1 ATOM 1592 C C . ASN A 1 205 ? 0.046 48.022 29.627 1.00 28.19 ? 205 ASN A C 1 ATOM 1593 O O . ASN A 1 205 ? 0.798 47.384 30.363 1.00 27.82 ? 205 ASN A O 1 ATOM 1594 C CB . ASN A 1 205 ? -1.859 46.405 30.163 1.00 30.43 ? 205 ASN A CB 1 ATOM 1595 C CG . ASN A 1 205 ? -1.520 46.129 31.626 1.00 31.28 ? 205 ASN A CG 1 ATOM 1596 O OD1 . ASN A 1 205 ? -0.998 45.066 31.951 1.00 32.80 ? 205 ASN A OD1 1 ATOM 1597 N ND2 . ASN A 1 205 ? -1.837 47.059 32.512 1.00 31.57 ? 205 ASN A ND2 1 ATOM 1598 N N . ASN A 1 206 ? 0.479 48.923 28.742 1.00 27.41 ? 206 ASN A N 1 ATOM 1599 C CA . ASN A 1 206 ? 1.885 49.314 28.610 1.00 27.23 ? 206 ASN A CA 1 ATOM 1600 C C . ASN A 1 206 ? 2.825 48.153 28.289 1.00 27.80 ? 206 ASN A C 1 ATOM 1601 O O . ASN A 1 206 ? 3.972 48.134 28.734 1.00 27.35 ? 206 ASN A O 1 ATOM 1602 C CB . ASN A 1 206 ? 2.359 50.031 29.883 1.00 27.22 ? 206 ASN A CB 1 ATOM 1603 C CG . ASN A 1 206 ? 1.640 51.344 30.109 1.00 26.41 ? 206 ASN A CG 1 ATOM 1604 O OD1 . ASN A 1 206 ? 1.553 52.169 29.203 1.00 27.23 ? 206 ASN A OD1 1 ATOM 1605 N ND2 . ASN A 1 206 ? 1.124 51.545 31.314 1.00 26.70 ? 206 ASN A ND2 1 ATOM 1606 N N . GLY A 1 207 ? 2.338 47.189 27.513 1.00 28.10 ? 207 GLY A N 1 ATOM 1607 C CA . GLY A 1 207 ? 3.156 46.039 27.124 1.00 28.88 ? 207 GLY A CA 1 ATOM 1608 C C . GLY A 1 207 ? 3.273 44.954 28.182 1.00 29.35 ? 207 GLY A C 1 ATOM 1609 O O . GLY A 1 207 ? 4.001 43.979 27.985 1.00 29.19 ? 207 GLY A O 1 ATOM 1610 N N . VAL A 1 208 ? 2.542 45.103 29.288 1.00 29.73 ? 208 VAL A N 1 ATOM 1611 C CA . VAL A 1 208 ? 2.604 44.174 30.416 1.00 30.29 ? 208 VAL A CA 1 ATOM 1612 C C . VAL A 1 208 ? 1.440 43.181 30.346 1.00 31.09 ? 208 VAL A C 1 ATOM 1613 O O . VAL A 1 208 ? 0.295 43.573 30.114 1.00 31.03 ? 208 VAL A O 1 ATOM 1614 C CB . VAL A 1 208 ? 2.557 44.941 31.761 1.00 30.28 ? 208 VAL A CB 1 ATOM 1615 C CG1 . VAL A 1 208 ? 2.500 43.990 32.951 1.00 30.45 ? 208 VAL A CG1 1 ATOM 1616 C CG2 . VAL A 1 208 ? 3.757 45.869 31.885 1.00 30.53 ? 208 VAL A CG2 1 ATOM 1617 N N . PHE A 1 209 ? 1.742 41.898 30.541 1.00 31.74 ? 209 PHE A N 1 ATOM 1618 C CA . PHE A 1 209 ? 0.714 40.856 30.595 1.00 32.12 ? 209 PHE A CA 1 ATOM 1619 C C . PHE A 1 209 ? -0.138 41.028 31.850 1.00 33.85 ? 209 PHE A C 1 ATOM 1620 O O . PHE A 1 209 ? 0.396 41.242 32.939 1.00 33.71 ? 209 PHE A O 1 ATOM 1621 C CB . PHE A 1 209 ? 1.357 39.461 30.643 1.00 31.73 ? 209 PHE A CB 1 ATOM 1622 C CG . PHE A 1 209 ? 1.950 38.986 29.334 1.00 30.39 ? 209 PHE A CG 1 ATOM 1623 C CD1 . PHE A 1 209 ? 2.124 39.831 28.238 1.00 29.66 ? 209 PHE A CD1 1 ATOM 1624 C CD2 . PHE A 1 209 ? 2.356 37.664 29.216 1.00 30.25 ? 209 PHE A CD2 1 ATOM 1625 C CE1 . PHE A 1 209 ? 2.671 39.354 27.056 1.00 29.53 ? 209 PHE A CE1 1 ATOM 1626 C CE2 . PHE A 1 209 ? 2.909 37.188 28.040 1.00 29.46 ? 209 PHE A CE2 1 ATOM 1627 C CZ . PHE A 1 209 ? 3.066 38.031 26.960 1.00 29.36 ? 209 PHE A CZ 1 ATOM 1628 N N . ARG A 1 210 ? -1.455 40.917 31.699 1.00 35.45 ? 210 ARG A N 1 ATOM 1629 C CA . ARG A 1 210 ? -2.361 40.919 32.850 1.00 36.94 ? 210 ARG A CA 1 ATOM 1630 C C . ARG A 1 210 ? -2.131 39.676 33.713 1.00 37.75 ? 210 ARG A C 1 ATOM 1631 O O . ARG A 1 210 ? -2.216 39.743 34.938 1.00 37.34 ? 210 ARG A O 1 ATOM 1632 C CB . ARG A 1 210 ? -3.822 40.965 32.395 1.00 37.33 ? 210 ARG A CB 1 ATOM 1633 C CG . ARG A 1 210 ? -4.202 42.221 31.625 1.00 38.08 ? 210 ARG A CG 1 ATOM 1634 C CD . ARG A 1 210 ? -4.622 43.354 32.544 1.00 38.39 ? 210 ARG A CD 1 ATOM 1635 N NE . ARG A 1 210 ? -4.909 44.569 31.787 1.00 38.14 ? 210 ARG A NE 1 ATOM 1636 C CZ . ARG A 1 210 ? -5.169 45.758 32.326 1.00 37.56 ? 210 ARG A CZ 1 ATOM 1637 N NH1 . ARG A 1 210 ? -5.186 45.915 33.646 1.00 37.00 ? 210 ARG A NH1 1 ATOM 1638 N NH2 . ARG A 1 210 ? -5.419 46.795 31.536 1.00 36.84 ? 210 ARG A NH2 1 ATOM 1639 N N . THR A 1 211 ? -1.834 38.551 33.059 1.00 38.12 ? 211 THR A N 1 ATOM 1640 C CA . THR A 1 211 ? -1.544 37.286 33.734 1.00 38.55 ? 211 THR A CA 1 ATOM 1641 C C . THR A 1 211 ? -0.284 36.674 33.116 1.00 38.49 ? 211 THR A C 1 ATOM 1642 O O . THR A 1 211 ? -0.241 36.466 31.904 1.00 37.27 ? 211 THR A O 1 ATOM 1643 C CB . THR A 1 211 ? -2.707 36.288 33.572 1.00 39.41 ? 211 THR A CB 1 ATOM 1644 O OG1 . THR A 1 211 ? -3.942 36.918 33.936 1.00 40.18 ? 211 THR A OG1 1 ATOM 1645 C CG2 . THR A 1 211 ? -2.495 35.055 34.445 1.00 39.50 ? 211 THR A CG2 1 ATOM 1646 N N . PRO A 1 212 ? 0.749 36.394 33.934 1.00 38.04 ? 212 PRO A N 1 ATOM 1647 C CA . PRO A 1 212 ? 1.961 35.830 33.336 1.00 38.17 ? 212 PRO A CA 1 ATOM 1648 C C . PRO A 1 212 ? 1.763 34.433 32.753 1.00 37.75 ? 212 PRO A C 1 ATOM 1649 O O . PRO A 1 212 ? 0.963 33.653 33.270 1.00 38.94 ? 212 PRO A O 1 ATOM 1650 C CB . PRO A 1 212 ? 2.947 35.789 34.508 1.00 38.79 ? 212 PRO A CB 1 ATOM 1651 C CG . PRO A 1 212 ? 2.459 36.842 35.445 1.00 38.94 ? 212 PRO A CG 1 ATOM 1652 C CD . PRO A 1 212 ? 0.965 36.756 35.347 1.00 38.92 ? 212 PRO A CD 1 ATOM 1653 N N . THR A 1 213 ? 2.487 34.142 31.676 1.00 37.44 ? 213 THR A N 1 ATOM 1654 C CA . THR A 1 213 ? 2.424 32.848 31.000 1.00 37.04 ? 213 THR A CA 1 ATOM 1655 C C . THR A 1 213 ? 3.672 32.049 31.359 1.00 37.29 ? 213 THR A C 1 ATOM 1656 O O . THR A 1 213 ? 4.790 32.521 31.154 1.00 35.85 ? 213 THR A O 1 ATOM 1657 C CB . THR A 1 213 ? 2.341 33.034 29.468 1.00 36.95 ? 213 THR A CB 1 ATOM 1658 O OG1 . THR A 1 213 ? 1.058 33.573 29.115 1.00 36.90 ? 213 THR A OG1 1 ATOM 1659 C CG2 . THR A 1 213 ? 2.550 31.707 28.730 1.00 37.04 ? 213 THR A CG2 1 ATOM 1660 N N . VAL A 1 214 ? 3.485 30.844 31.896 1.00 38.24 ? 214 VAL A N 1 ATOM 1661 C CA . VAL A 1 214 ? 4.614 29.978 32.236 1.00 38.49 ? 214 VAL A CA 1 ATOM 1662 C C . VAL A 1 214 ? 4.958 29.058 31.060 1.00 37.67 ? 214 VAL A C 1 ATOM 1663 O O . VAL A 1 214 ? 4.092 28.354 30.537 1.00 36.98 ? 214 VAL A O 1 ATOM 1664 C CB . VAL A 1 214 ? 4.343 29.137 33.503 1.00 39.27 ? 214 VAL A CB 1 ATOM 1665 C CG1 . VAL A 1 214 ? 5.515 28.212 33.796 1.00 39.94 ? 214 VAL A CG1 1 ATOM 1666 C CG2 . VAL A 1 214 ? 4.090 30.047 34.697 1.00 39.89 ? 214 VAL A CG2 1 ATOM 1667 N N . LEU A 1 215 ? 6.229 29.076 30.664 1.00 37.43 ? 215 LEU A N 1 ATOM 1668 C CA . LEU A 1 215 ? 6.744 28.252 29.571 1.00 37.42 ? 215 LEU A CA 1 ATOM 1669 C C . LEU A 1 215 ? 7.971 27.462 30.011 1.00 39.38 ? 215 LEU A C 1 ATOM 1670 O O . LEU A 1 215 ? 8.586 27.772 31.029 1.00 39.94 ? 215 LEU A O 1 ATOM 1671 C CB . LEU A 1 215 ? 7.161 29.131 28.393 1.00 36.40 ? 215 LEU A CB 1 ATOM 1672 C CG . LEU A 1 215 ? 6.117 29.967 27.660 1.00 35.88 ? 215 LEU A CG 1 ATOM 1673 C CD1 . LEU A 1 215 ? 6.814 30.723 26.544 1.00 36.14 ? 215 LEU A CD1 1 ATOM 1674 C CD2 . LEU A 1 215 ? 4.996 29.106 27.107 1.00 35.50 ? 215 LEU A CD2 1 ATOM 1675 N N . VAL A 1 216 ? 8.329 26.451 29.223 1.00 40.58 ? 216 VAL A N 1 ATOM 1676 C CA . VAL A 1 216 ? 9.610 25.756 29.364 1.00 42.16 ? 216 VAL A CA 1 ATOM 1677 C C . VAL A 1 216 ? 10.533 26.255 28.254 1.00 43.92 ? 216 VAL A C 1 ATOM 1678 O O . VAL A 1 216 ? 10.118 26.328 27.097 1.00 42.07 ? 216 VAL A O 1 ATOM 1679 C CB . VAL A 1 216 ? 9.436 24.228 29.257 1.00 42.32 ? 216 VAL A CB 1 ATOM 1680 C CG1 . VAL A 1 216 ? 10.786 23.520 29.285 1.00 42.87 ? 216 VAL A CG1 1 ATOM 1681 C CG2 . VAL A 1 216 ? 8.545 23.718 30.380 1.00 42.19 ? 216 VAL A CG2 1 ATOM 1682 N N . ASP A 1 217 ? 11.774 26.603 28.597 1.00 46.22 ? 217 ASP A N 1 ATOM 1683 C CA . ASP A 1 217 ? 12.721 27.117 27.596 1.00 49.37 ? 217 ASP A CA 1 ATOM 1684 C C . ASP A 1 217 ? 13.539 25.994 26.940 1.00 51.32 ? 217 ASP A C 1 ATOM 1685 O O . ASP A 1 217 ? 13.400 24.820 27.295 1.00 50.62 ? 217 ASP A O 1 ATOM 1686 C CB . ASP A 1 217 ? 13.626 28.224 28.182 1.00 50.08 ? 217 ASP A CB 1 ATOM 1687 C CG . ASP A 1 217 ? 14.675 27.701 29.162 1.00 50.71 ? 217 ASP A CG 1 ATOM 1688 O OD1 . ASP A 1 217 ? 14.844 26.471 29.298 1.00 50.74 ? 217 ASP A OD1 1 ATOM 1689 O OD2 . ASP A 1 217 ? 15.342 28.544 29.802 1.00 51.91 ? 217 ASP A OD2 1 ATOM 1690 N N . SER A 1 218 ? 14.385 26.375 25.985 1.00 55.14 ? 218 SER A N 1 ATOM 1691 C CA . SER A 1 218 ? 15.196 25.436 25.197 1.00 58.59 ? 218 SER A CA 1 ATOM 1692 C C . SER A 1 218 ? 16.030 24.439 26.013 1.00 60.62 ? 218 SER A C 1 ATOM 1693 O O . SER A 1 218 ? 16.346 23.354 25.524 1.00 61.76 ? 218 SER A O 1 ATOM 1694 C CB . SER A 1 218 ? 16.131 26.220 24.269 1.00 59.55 ? 218 SER A CB 1 ATOM 1695 O OG . SER A 1 218 ? 16.963 27.100 25.008 1.00 61.00 ? 218 SER A OG 1 ATOM 1696 N N . LYS A 1 219 ? 16.390 24.807 27.241 1.00 62.95 ? 219 LYS A N 1 ATOM 1697 C CA . LYS A 1 219 ? 17.240 23.963 28.088 1.00 64.04 ? 219 LYS A CA 1 ATOM 1698 C C . LYS A 1 219 ? 16.435 23.199 29.144 1.00 62.82 ? 219 LYS A C 1 ATOM 1699 O O . LYS A 1 219 ? 16.999 22.710 30.125 1.00 63.23 ? 219 LYS A O 1 ATOM 1700 C CB . LYS A 1 219 ? 18.326 24.813 28.762 1.00 66.32 ? 219 LYS A CB 1 ATOM 1701 C CG . LYS A 1 219 ? 18.854 25.938 27.883 1.00 68.19 ? 219 LYS A CG 1 ATOM 1702 C CD . LYS A 1 219 ? 20.310 26.271 28.159 1.00 69.84 ? 219 LYS A CD 1 ATOM 1703 C CE . LYS A 1 219 ? 20.802 27.358 27.215 1.00 71.10 ? 219 LYS A CE 1 ATOM 1704 N NZ . LYS A 1 219 ? 22.175 27.089 26.707 1.00 71.85 ? 219 LYS A NZ 1 ATOM 1705 N N . GLY A 1 220 ? 15.122 23.095 28.939 1.00 60.76 ? 220 GLY A N 1 ATOM 1706 C CA . GLY A 1 220 ? 14.248 22.384 29.866 1.00 59.63 ? 220 GLY A CA 1 ATOM 1707 C C . GLY A 1 220 ? 13.924 23.154 31.134 1.00 58.92 ? 220 GLY A C 1 ATOM 1708 O O . GLY A 1 220 ? 13.339 22.594 32.060 1.00 59.08 ? 220 GLY A O 1 ATOM 1709 N N . ASN A 1 221 ? 14.293 24.435 31.179 1.00 58.37 ? 221 ASN A N 1 ATOM 1710 C CA . ASN A 1 221 ? 14.048 25.272 32.352 1.00 58.36 ? 221 ASN A CA 1 ATOM 1711 C C . ASN A 1 221 ? 12.750 26.059 32.214 1.00 58.22 ? 221 ASN A C 1 ATOM 1712 O O . ASN A 1 221 ? 12.512 26.712 31.197 1.00 57.04 ? 221 ASN A O 1 ATOM 1713 C CB . ASN A 1 221 ? 15.222 26.223 32.593 1.00 58.16 ? 221 ASN A CB 1 ATOM 1714 C CG . ASN A 1 221 ? 16.479 25.495 33.029 1.00 57.76 ? 221 ASN A CG 1 ATOM 1715 O OD1 . ASN A 1 221 ? 16.460 24.736 33.998 1.00 57.22 ? 221 ASN A OD1 1 ATOM 1716 N ND2 . ASN A 1 221 ? 17.580 25.720 32.317 1.00 57.53 ? 221 ASN A ND2 1 ATOM 1717 N N . ARG A 1 222 ? 11.925 25.991 33.254 1.00 58.53 ? 222 ARG A N 1 ATOM 1718 C CA . ARG A 1 222 ? 10.601 26.611 33.260 1.00 58.84 ? 222 ARG A CA 1 ATOM 1719 C C . ARG A 1 222 ? 10.737 28.110 33.572 1.00 57.52 ? 222 ARG A C 1 ATOM 1720 O O . ARG A 1 222 ? 11.489 28.491 34.472 1.00 58.35 ? 222 ARG A O 1 ATOM 1721 C CB . ARG A 1 222 ? 9.693 25.854 34.253 1.00 60.04 ? 222 ARG A CB 1 ATOM 1722 C CG . ARG A 1 222 ? 8.488 26.599 34.813 1.00 61.28 ? 222 ARG A CG 1 ATOM 1723 C CD . ARG A 1 222 ? 8.907 27.538 35.933 1.00 62.14 ? 222 ARG A CD 1 ATOM 1724 N NE . ARG A 1 222 ? 7.794 28.152 36.646 1.00 62.35 ? 222 ARG A NE 1 ATOM 1725 C CZ . ARG A 1 222 ? 7.877 29.305 37.310 1.00 62.26 ? 222 ARG A CZ 1 ATOM 1726 N NH1 . ARG A 1 222 ? 6.808 29.782 37.927 1.00 61.54 ? 222 ARG A NH1 1 ATOM 1727 N NH2 . ARG A 1 222 ? 9.017 29.996 37.356 1.00 61.74 ? 222 ARG A NH2 1 ATOM 1728 N N . VAL A 1 223 ? 10.028 28.951 32.812 1.00 55.10 ? 223 VAL A N 1 ATOM 1729 C CA . VAL A 1 223 ? 10.135 30.415 32.937 1.00 52.89 ? 223 VAL A CA 1 ATOM 1730 C C . VAL A 1 223 ? 8.781 31.125 32.871 1.00 49.86 ? 223 VAL A C 1 ATOM 1731 O O . VAL A 1 223 ? 7.806 30.573 32.364 1.00 49.39 ? 223 VAL A O 1 ATOM 1732 C CB . VAL A 1 223 ? 11.054 31.016 31.846 1.00 53.19 ? 223 VAL A CB 1 ATOM 1733 C CG1 . VAL A 1 223 ? 12.444 30.404 31.926 1.00 54.38 ? 223 VAL A CG1 1 ATOM 1734 C CG2 . VAL A 1 223 ? 10.465 30.823 30.451 1.00 53.71 ? 223 VAL A CG2 1 ATOM 1735 N N . GLN A 1 224 ? 8.746 32.357 33.381 1.00 46.64 ? 224 GLN A N 1 ATOM 1736 C CA . GLN A 1 224 ? 7.554 33.203 33.347 1.00 44.13 ? 224 GLN A CA 1 ATOM 1737 C C . GLN A 1 224 ? 7.709 34.307 32.308 1.00 40.37 ? 224 GLN A C 1 ATOM 1738 O O . GLN A 1 224 ? 8.722 35.002 32.283 1.00 38.86 ? 224 GLN A O 1 ATOM 1739 C CB . GLN A 1 224 ? 7.313 33.857 34.709 1.00 45.35 ? 224 GLN A CB 1 ATOM 1740 C CG . GLN A 1 224 ? 6.879 32.897 35.803 1.00 46.68 ? 224 GLN A CG 1 ATOM 1741 C CD . GLN A 1 224 ? 5.840 33.504 36.732 1.00 48.01 ? 224 GLN A CD 1 ATOM 1742 O OE1 . GLN A 1 224 ? 5.971 34.651 37.165 1.00 48.69 ? 224 GLN A OE1 1 ATOM 1743 N NE2 . GLN A 1 224 ? 4.798 32.734 37.044 1.00 48.74 ? 224 GLN A NE2 1 ATOM 1744 N N . ILE A 1 225 ? 6.693 34.470 31.467 1.00 37.42 ? 225 ILE A N 1 ATOM 1745 C CA . ILE A 1 225 ? 6.659 35.549 30.485 1.00 35.57 ? 225 ILE A CA 1 ATOM 1746 C C . ILE A 1 225 ? 5.679 36.581 31.030 1.00 34.68 ? 225 ILE A C 1 ATOM 1747 O O . ILE A 1 225 ? 4.519 36.261 31.274 1.00 34.43 ? 225 ILE A O 1 ATOM 1748 C CB . ILE A 1 225 ? 6.202 35.042 29.102 1.00 34.92 ? 225 ILE A CB 1 ATOM 1749 C CG1 . ILE A 1 225 ? 6.932 33.741 28.730 1.00 34.64 ? 225 ILE A CG1 1 ATOM 1750 C CG2 . ILE A 1 225 ? 6.425 36.105 28.035 1.00 34.56 ? 225 ILE A CG2 1 ATOM 1751 C CD1 . ILE A 1 225 ? 8.442 33.857 28.652 1.00 34.79 ? 225 ILE A CD1 1 ATOM 1752 N N . THR A 1 226 ? 6.154 37.804 31.254 1.00 35.03 ? 226 THR A N 1 ATOM 1753 C CA . THR A 1 226 ? 5.341 38.835 31.909 1.00 34.51 ? 226 THR A CA 1 ATOM 1754 C C . THR A 1 226 ? 5.059 40.062 31.050 1.00 34.61 ? 226 THR A C 1 ATOM 1755 O O . THR A 1 226 ? 4.187 40.862 31.392 1.00 34.86 ? 226 THR A O 1 ATOM 1756 C CB . THR A 1 226 ? 6.002 39.308 33.216 1.00 34.41 ? 226 THR A CB 1 ATOM 1757 O OG1 . THR A 1 226 ? 7.343 39.740 32.952 1.00 33.73 ? 226 THR A OG1 1 ATOM 1758 C CG2 . THR A 1 226 ? 6.013 38.182 34.243 1.00 34.94 ? 226 THR A CG2 1 ATOM 1759 N N . ASN A 1 227 ? 5.788 40.220 29.949 1.00 34.15 ? 227 ASN A N 1 ATOM 1760 C CA . ASN A 1 227 ? 5.627 41.391 29.097 1.00 35.14 ? 227 ASN A CA 1 ATOM 1761 C C . ASN A 1 227 ? 6.119 41.160 27.667 1.00 33.07 ? 227 ASN A C 1 ATOM 1762 O O . ASN A 1 227 ? 6.752 40.142 27.373 1.00 32.82 ? 227 ASN A O 1 ATOM 1763 C CB . ASN A 1 227 ? 6.298 42.618 29.745 1.00 37.42 ? 227 ASN A CB 1 ATOM 1764 C CG . ASN A 1 227 ? 7.805 42.467 29.914 1.00 40.31 ? 227 ASN A CG 1 ATOM 1765 O OD1 . ASN A 1 227 ? 8.557 42.562 28.945 1.00 39.96 ? 227 ASN A OD1 1 ATOM 1766 N ND2 . ASN A 1 227 ? 8.252 42.257 31.158 1.00 44.97 ? 227 ASN A ND2 1 ATOM 1767 N N . VAL A 1 228 ? 5.816 42.110 26.786 1.00 31.07 ? 228 VAL A N 1 ATOM 1768 C CA . VAL A 1 228 ? 6.104 41.971 25.351 1.00 30.49 ? 228 VAL A CA 1 ATOM 1769 C C . VAL A 1 228 ? 7.581 42.073 24.954 1.00 30.40 ? 228 VAL A C 1 ATOM 1770 O O . VAL A 1 228 ? 7.904 41.889 23.780 1.00 29.88 ? 228 VAL A O 1 ATOM 1771 C CB . VAL A 1 228 ? 5.301 42.978 24.490 1.00 30.30 ? 228 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 228 ? 3.806 42.720 24.618 1.00 29.76 ? 228 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 228 ? 5.647 44.423 24.847 1.00 30.20 ? 228 VAL A CG2 1 ATOM 1774 N N . THR A 1 229 ? 8.470 42.379 25.900 1.00 31.30 ? 229 THR A N 1 ATOM 1775 C CA . THR A 1 229 ? 9.909 42.430 25.590 1.00 32.11 ? 229 THR A CA 1 ATOM 1776 C C . THR A 1 229 ? 10.546 41.040 25.604 1.00 32.13 ? 229 THR A C 1 ATOM 1777 O O . THR A 1 229 ? 11.703 40.892 25.222 1.00 32.36 ? 229 THR A O 1 ATOM 1778 C CB . THR A 1 229 ? 10.715 43.346 26.548 1.00 32.96 ? 229 THR A CB 1 ATOM 1779 O OG1 . THR A 1 229 ? 10.815 42.747 27.848 1.00 33.98 ? 229 THR A OG1 1 ATOM 1780 C CG2 . THR A 1 229 ? 10.079 44.728 26.658 1.00 33.60 ? 229 THR A CG2 1 ATOM 1781 N N . SER A 1 230 ? 9.800 40.031 26.049 1.00 32.00 ? 230 SER A N 1 ATOM 1782 C CA . SER A 1 230 ? 10.302 38.661 26.063 1.00 32.44 ? 230 SER A CA 1 ATOM 1783 C C . SER A 1 230 ? 10.585 38.172 24.642 1.00 31.59 ? 230 SER A C 1 ATOM 1784 O O . SER A 1 230 ? 9.894 38.549 23.695 1.00 29.19 ? 230 SER A O 1 ATOM 1785 C CB . SER A 1 230 ? 9.308 37.732 26.761 1.00 33.86 ? 230 SER A CB 1 ATOM 1786 O OG . SER A 1 230 ? 9.461 36.391 26.330 1.00 35.88 ? 230 SER A OG 1 ATOM 1787 N N . ASN A 1 231 ? 11.613 37.337 24.506 1.00 31.87 ? 231 ASN A N 1 ATOM 1788 C CA . ASN A 1 231 ? 11.984 36.758 23.213 1.00 32.66 ? 231 ASN A CA 1 ATOM 1789 C C . ASN A 1 231 ? 10.849 35.980 22.549 1.00 30.24 ? 231 ASN A C 1 ATOM 1790 O O . ASN A 1 231 ? 10.753 35.948 21.324 1.00 29.65 ? 231 ASN A O 1 ATOM 1791 C CB . ASN A 1 231 ? 13.211 35.845 23.366 1.00 34.96 ? 231 ASN A CB 1 ATOM 1792 C CG . ASN A 1 231 ? 14.515 36.622 23.446 1.00 38.05 ? 231 ASN A CG 1 ATOM 1793 O OD1 . ASN A 1 231 ? 14.634 37.720 22.901 1.00 40.62 ? 231 ASN A OD1 1 ATOM 1794 N ND2 . ASN A 1 231 ? 15.509 36.046 24.118 1.00 39.84 ? 231 ASN A ND2 1 ATOM 1795 N N . VAL A 1 232 ? 9.989 35.364 23.356 1.00 29.78 ? 232 VAL A N 1 ATOM 1796 C CA . VAL A 1 232 ? 8.837 34.624 22.822 1.00 28.76 ? 232 VAL A CA 1 ATOM 1797 C C . VAL A 1 232 ? 7.957 35.566 21.993 1.00 27.83 ? 232 VAL A C 1 ATOM 1798 O O . VAL A 1 232 ? 7.416 35.178 20.959 1.00 26.12 ? 232 VAL A O 1 ATOM 1799 C CB . VAL A 1 232 ? 7.994 33.951 23.934 1.00 29.49 ? 232 VAL A CB 1 ATOM 1800 C CG1 . VAL A 1 232 ? 6.925 33.049 23.331 1.00 29.15 ? 232 VAL A CG1 1 ATOM 1801 C CG2 . VAL A 1 232 ? 8.871 33.128 24.867 1.00 30.00 ? 232 VAL A CG2 1 ATOM 1802 N N . VAL A 1 233 ? 7.845 36.818 22.437 1.00 27.23 ? 233 VAL A N 1 ATOM 1803 C CA . VAL A 1 233 ? 6.996 37.804 21.767 1.00 26.83 ? 233 VAL A CA 1 ATOM 1804 C C . VAL A 1 233 ? 7.711 38.520 20.619 1.00 26.63 ? 233 VAL A C 1 ATOM 1805 O O . VAL A 1 233 ? 7.128 38.712 19.557 1.00 26.94 ? 233 VAL A O 1 ATOM 1806 C CB . VAL A 1 233 ? 6.444 38.841 22.774 1.00 26.75 ? 233 VAL A CB 1 ATOM 1807 C CG1 . VAL A 1 233 ? 5.509 39.819 22.079 1.00 26.92 ? 233 VAL A CG1 1 ATOM 1808 C CG2 . VAL A 1 233 ? 5.712 38.136 23.905 1.00 26.85 ? 233 VAL A CG2 1 ATOM 1809 N N . THR A 1 234 ? 8.965 38.917 20.824 1.00 27.28 ? 234 THR A N 1 ATOM 1810 C CA . THR A 1 234 ? 9.684 39.713 19.821 1.00 27.96 ? 234 THR A CA 1 ATOM 1811 C C . THR A 1 234 ? 10.200 38.887 18.642 1.00 28.58 ? 234 THR A C 1 ATOM 1812 O O . THR A 1 234 ? 10.309 39.399 17.525 1.00 29.19 ? 234 THR A O 1 ATOM 1813 C CB . THR A 1 234 ? 10.863 40.493 20.446 1.00 27.85 ? 234 THR A CB 1 ATOM 1814 O OG1 . THR A 1 234 ? 11.760 39.587 21.100 1.00 27.60 ? 234 THR A OG1 1 ATOM 1815 C CG2 . THR A 1 234 ? 10.350 41.509 21.456 1.00 28.01 ? 234 THR A CG2 1 ATOM 1816 N N . SER A 1 235 ? 10.488 37.610 18.882 1.00 29.59 ? 235 SER A N 1 ATOM 1817 C CA . SER A 1 235 ? 11.213 36.786 17.909 1.00 30.02 ? 235 SER A CA 1 ATOM 1818 C C . SER A 1 235 ? 10.483 35.509 17.457 1.00 29.74 ? 235 SER A C 1 ATOM 1819 O O . SER A 1 235 ? 10.647 35.068 16.312 1.00 32.87 ? 235 SER A O 1 ATOM 1820 C CB . SER A 1 235 ? 12.577 36.417 18.496 1.00 30.85 ? 235 SER A CB 1 ATOM 1821 O OG . SER A 1 235 ? 13.228 37.568 19.016 1.00 33.03 ? 235 SER A OG 1 ATOM 1822 N N . ASN A 1 236 ? 9.654 34.947 18.326 1.00 27.27 ? 236 ASN A N 1 ATOM 1823 C CA . ASN A 1 236 ? 9.181 33.569 18.180 1.00 26.05 ? 236 ASN A CA 1 ATOM 1824 C C . ASN A 1 236 ? 7.756 33.479 17.615 1.00 24.89 ? 236 ASN A C 1 ATOM 1825 O O . ASN A 1 236 ? 7.565 33.008 16.494 1.00 24.13 ? 236 ASN A O 1 ATOM 1826 C CB . ASN A 1 236 ? 9.301 32.881 19.543 1.00 25.80 ? 236 ASN A CB 1 ATOM 1827 C CG . ASN A 1 236 ? 9.100 31.378 19.485 1.00 25.48 ? 236 ASN A CG 1 ATOM 1828 O OD1 . ASN A 1 236 ? 8.742 30.810 18.457 1.00 25.49 ? 236 ASN A OD1 1 ATOM 1829 N ND2 . ASN A 1 236 ? 9.334 30.728 20.610 1.00 26.23 ? 236 ASN A ND2 1 ATOM 1830 N N . ILE A 1 237 ? 6.764 33.940 18.376 1.00 24.65 ? 237 ILE A N 1 ATOM 1831 C CA . ILE A 1 237 ? 5.363 33.843 17.947 1.00 23.87 ? 237 ILE A CA 1 ATOM 1832 C C . ILE A 1 237 ? 5.140 34.640 16.652 1.00 24.21 ? 237 ILE A C 1 ATOM 1833 O O . ILE A 1 237 ? 5.638 35.758 16.516 1.00 24.32 ? 237 ILE A O 1 ATOM 1834 C CB . ILE A 1 237 ? 4.386 34.282 19.069 1.00 23.62 ? 237 ILE A CB 1 ATOM 1835 C CG1 . ILE A 1 237 ? 2.951 33.857 18.734 1.00 23.23 ? 237 ILE A CG1 1 ATOM 1836 C CG2 . ILE A 1 237 ? 4.460 35.786 19.324 1.00 23.49 ? 237 ILE A CG2 1 ATOM 1837 C CD1 . ILE A 1 237 ? 2.029 33.838 19.933 1.00 23.43 ? 237 ILE A CD1 1 ATOM 1838 N N . GLN A 1 238 ? 4.418 34.050 15.698 1.00 23.91 ? 238 GLN A N 1 ATOM 1839 C CA . GLN A 1 238 ? 4.227 34.647 14.367 1.00 24.39 ? 238 GLN A CA 1 ATOM 1840 C C . GLN A 1 238 ? 2.778 34.973 14.018 1.00 23.45 ? 238 GLN A C 1 ATOM 1841 O O . GLN A 1 238 ? 2.517 35.651 13.022 1.00 23.88 ? 238 GLN A O 1 ATOM 1842 C CB . GLN A 1 238 ? 4.784 33.704 13.301 1.00 25.30 ? 238 GLN A CB 1 ATOM 1843 C CG . GLN A 1 238 ? 6.254 33.376 13.481 1.00 26.39 ? 238 GLN A CG 1 ATOM 1844 C CD . GLN A 1 238 ? 7.147 34.584 13.277 1.00 27.77 ? 238 GLN A CD 1 ATOM 1845 O OE1 . GLN A 1 238 ? 6.984 35.328 12.311 1.00 29.76 ? 238 GLN A OE1 1 ATOM 1846 N NE2 . GLN A 1 238 ? 8.107 34.775 14.174 1.00 28.15 ? 238 GLN A NE2 1 ATOM 1847 N N . LEU A 1 239 ? 1.846 34.473 14.825 1.00 22.98 ? 239 LEU A N 1 ATOM 1848 C CA . LEU A 1 239 ? 0.414 34.623 14.584 1.00 22.77 ? 239 LEU A CA 1 ATOM 1849 C C . LEU A 1 239 ? -0.307 34.689 15.928 1.00 22.75 ? 239 LEU A C 1 ATOM 1850 O O . LEU A 1 239 ? 0.029 33.942 16.855 1.00 22.47 ? 239 LEU A O 1 ATOM 1851 C CB . LEU A 1 239 ? -0.126 33.429 13.791 1.00 22.33 ? 239 LEU A CB 1 ATOM 1852 C CG . LEU A 1 239 ? 0.495 33.063 12.441 1.00 22.23 ? 239 LEU A CG 1 ATOM 1853 C CD1 . LEU A 1 239 ? 0.046 31.664 12.037 1.00 22.07 ? 239 LEU A CD1 1 ATOM 1854 C CD2 . LEU A 1 239 ? 0.117 34.076 11.370 1.00 22.58 ? 239 LEU A CD2 1 ATOM 1855 N N . LEU A 1 240 ? -1.295 35.577 16.037 1.00 23.23 ? 240 LEU A N 1 ATOM 1856 C CA . LEU A 1 240 ? -2.096 35.687 17.255 1.00 24.10 ? 240 LEU A CA 1 ATOM 1857 C C . LEU A 1 240 ? -3.531 35.243 17.023 1.00 24.43 ? 240 LEU A C 1 ATOM 1858 O O . LEU A 1 240 ? -4.200 35.711 16.101 1.00 25.10 ? 240 LEU A O 1 ATOM 1859 C CB . LEU A 1 240 ? -2.103 37.127 17.793 1.00 24.41 ? 240 LEU A CB 1 ATOM 1860 C CG . LEU A 1 240 ? -0.739 37.766 18.043 1.00 24.57 ? 240 LEU A CG 1 ATOM 1861 C CD1 . LEU A 1 240 ? -0.905 39.239 18.401 1.00 25.17 ? 240 LEU A CD1 1 ATOM 1862 C CD2 . LEU A 1 240 ? 0.032 37.032 19.130 1.00 24.72 ? 240 LEU A CD2 1 ATOM 1863 N N . LEU A 1 241 ? -3.981 34.320 17.864 1.00 25.45 ? 241 LEU A N 1 ATOM 1864 C CA . LEU A 1 241 ? -5.385 33.973 17.954 1.00 26.29 ? 241 LEU A CA 1 ATOM 1865 C C . LEU A 1 241 ? -6.126 35.191 18.478 1.00 27.08 ? 241 LEU A C 1 ATOM 1866 O O . LEU A 1 241 ? -5.791 35.705 19.548 1.00 26.82 ? 241 LEU A O 1 ATOM 1867 C CB . LEU A 1 241 ? -5.577 32.806 18.922 1.00 26.00 ? 241 LEU A CB 1 ATOM 1868 C CG . LEU A 1 241 ? -6.990 32.238 19.047 1.00 26.21 ? 241 LEU A CG 1 ATOM 1869 C CD1 . LEU A 1 241 ? -7.491 31.747 17.699 1.00 26.56 ? 241 LEU A CD1 1 ATOM 1870 C CD2 . LEU A 1 241 ? -7.001 31.117 20.075 1.00 26.31 ? 241 LEU A CD2 1 ATOM 1871 N N . ASN A 1 242 ? -7.113 35.657 17.720 1.00 28.83 ? 242 ASN A N 1 ATOM 1872 C CA . ASN A 1 242 ? -7.905 36.817 18.122 1.00 30.13 ? 242 ASN A CA 1 ATOM 1873 C C . ASN A 1 242 ? -8.597 36.536 19.449 1.00 32.18 ? 242 ASN A C 1 ATOM 1874 O O . ASN A 1 242 ? -9.198 35.475 19.632 1.00 32.10 ? 242 ASN A O 1 ATOM 1875 C CB . ASN A 1 242 ? -8.940 37.165 17.047 1.00 30.25 ? 242 ASN A CB 1 ATOM 1876 C CG . ASN A 1 242 ? -9.446 38.597 17.155 1.00 30.25 ? 242 ASN A CG 1 ATOM 1877 O OD1 . ASN A 1 242 ? -10.098 38.961 18.132 1.00 30.31 ? 242 ASN A OD1 1 ATOM 1878 N ND2 . ASN A 1 242 ? -9.155 39.410 16.145 1.00 30.25 ? 242 ASN A ND2 1 ATOM 1879 N N . THR A 1 243 ? -8.506 37.489 20.373 1.00 34.35 ? 243 THR A N 1 ATOM 1880 C CA . THR A 1 243 ? -9.109 37.343 21.698 1.00 36.81 ? 243 THR A CA 1 ATOM 1881 C C . THR A 1 243 ? -10.630 37.132 21.650 1.00 39.14 ? 243 THR A C 1 ATOM 1882 O O . THR A 1 243 ? -11.214 36.590 22.589 1.00 39.19 ? 243 THR A O 1 ATOM 1883 C CB . THR A 1 243 ? -8.777 38.551 22.599 1.00 37.40 ? 243 THR A CB 1 ATOM 1884 O OG1 . THR A 1 243 ? -9.202 38.278 23.938 1.00 38.92 ? 243 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 243 ? -9.450 39.830 22.091 1.00 36.98 ? 243 THR A CG2 1 ATOM 1886 N N . LYS A 1 244 ? -11.261 37.546 20.555 1.00 42.25 ? 244 LYS A N 1 ATOM 1887 C CA . LYS A 1 244 ? -12.686 37.291 20.345 1.00 45.33 ? 244 LYS A CA 1 ATOM 1888 C C . LYS A 1 244 ? -12.999 35.795 20.183 1.00 46.94 ? 244 LYS A C 1 ATOM 1889 O O . LYS A 1 244 ? -14.153 35.382 20.328 1.00 46.91 ? 244 LYS A O 1 ATOM 1890 C CB . LYS A 1 244 ? -13.190 38.088 19.140 1.00 47.21 ? 244 LYS A CB 1 ATOM 1891 C CG . LYS A 1 244 ? -13.093 39.596 19.348 1.00 49.04 ? 244 LYS A CG 1 ATOM 1892 C CD . LYS A 1 244 ? -13.576 40.396 18.148 1.00 50.89 ? 244 LYS A CD 1 ATOM 1893 C CE . LYS A 1 244 ? -15.085 40.317 17.976 1.00 52.34 ? 244 LYS A CE 1 ATOM 1894 N NZ . LYS A 1 244 ? -15.523 40.953 16.702 1.00 53.41 ? 244 LYS A NZ 1 ATOM 1895 N N . ASN A 1 245 ? -11.971 34.996 19.892 1.00 47.26 ? 245 ASN A N 1 ATOM 1896 C CA . ASN A 1 245 ? -12.098 33.540 19.800 1.00 48.48 ? 245 ASN A CA 1 ATOM 1897 C C . ASN A 1 245 ? -11.491 32.790 20.995 1.00 49.53 ? 245 ASN A C 1 ATOM 1898 O O . ASN A 1 245 ? -11.332 31.568 20.946 1.00 49.92 ? 245 ASN A O 1 ATOM 1899 C CB . ASN A 1 245 ? -11.458 33.054 18.494 1.00 48.01 ? 245 ASN A CB 1 ATOM 1900 C CG . ASN A 1 245 ? -12.207 33.536 17.265 1.00 47.84 ? 245 ASN A CG 1 ATOM 1901 O OD1 . ASN A 1 245 ? -13.433 33.438 17.198 1.00 48.63 ? 245 ASN A OD1 1 ATOM 1902 N ND2 . ASN A 1 245 ? -11.476 34.051 16.284 1.00 46.94 ? 245 ASN A ND2 1 ATOM 1903 N N . ILE A 1 246 ? -11.163 33.516 22.064 1.00 50.76 ? 246 ILE A N 1 ATOM 1904 C CA . ILE A 1 246 ? -10.591 32.915 23.272 1.00 51.68 ? 246 ILE A CA 1 ATOM 1905 C C . ILE A 1 246 ? -11.582 33.055 24.427 1.00 53.35 ? 246 ILE A C 1 ATOM 1906 O O . ILE A 1 246 ? -11.983 32.064 25.038 1.00 54.33 ? 246 ILE A O 1 ATOM 1907 C CB . ILE A 1 246 ? -9.239 33.565 23.655 1.00 51.19 ? 246 ILE A CB 1 ATOM 1908 C CG1 . ILE A 1 246 ? -8.295 33.587 22.446 1.00 50.80 ? 246 ILE A CG1 1 ATOM 1909 C CG2 . ILE A 1 246 ? -8.593 32.812 24.813 1.00 51.25 ? 246 ILE A CG2 1 ATOM 1910 C CD1 . ILE A 1 246 ? -6.998 34.341 22.664 1.00 50.05 ? 246 ILE A CD1 1 ATOM 1911 O OXT . ILE A 1 246 ? -12.013 34.156 24.776 1.00 54.23 ? 246 ILE A OXT 1 HETATM 1912 C C1 . NAG B 2 . ? 9.647 42.123 31.538 1.00 55.15 ? 301 NAG A C1 1 HETATM 1913 C C2 . NAG B 2 . ? 10.126 42.441 32.959 1.00 60.00 ? 301 NAG A C2 1 HETATM 1914 C C3 . NAG B 2 . ? 11.631 42.247 33.200 1.00 61.19 ? 301 NAG A C3 1 HETATM 1915 C C4 . NAG B 2 . ? 12.232 41.137 32.343 1.00 61.67 ? 301 NAG A C4 1 HETATM 1916 C C5 . NAG B 2 . ? 11.745 41.321 30.910 1.00 61.01 ? 301 NAG A C5 1 HETATM 1917 C C6 . NAG B 2 . ? 12.433 40.397 29.909 1.00 61.69 ? 301 NAG A C6 1 HETATM 1918 C C7 . NAG B 2 . ? 8.504 44.187 33.524 1.00 63.04 ? 301 NAG A C7 1 HETATM 1919 C C8 . NAG B 2 . ? 8.235 45.652 33.715 1.00 63.64 ? 301 NAG A C8 1 HETATM 1920 N N2 . NAG B 2 . ? 9.749 43.827 33.196 1.00 61.44 ? 301 NAG A N2 1 HETATM 1921 O O3 . NAG B 2 . ? 11.869 41.970 34.564 1.00 61.92 ? 301 NAG A O3 1 HETATM 1922 O O4 . NAG B 2 . ? 13.640 41.190 32.419 1.00 62.53 ? 301 NAG A O4 1 HETATM 1923 O O5 . NAG B 2 . ? 10.355 41.068 30.922 1.00 57.96 ? 301 NAG A O5 1 HETATM 1924 O O6 . NAG B 2 . ? 12.094 39.055 30.181 1.00 61.97 ? 301 NAG A O6 1 HETATM 1925 O O7 . NAG B 2 . ? 7.585 43.379 33.669 1.00 63.90 ? 301 NAG A O7 1 HETATM 1926 C C1 . GOL C 3 . ? 12.411 13.786 4.514 1.00 36.26 ? 302 GOL A C1 1 HETATM 1927 O O1 . GOL C 3 . ? 12.746 12.411 4.298 1.00 36.62 ? 302 GOL A O1 1 HETATM 1928 C C2 . GOL C 3 . ? 12.286 14.503 3.176 1.00 35.99 ? 302 GOL A C2 1 HETATM 1929 O O2 . GOL C 3 . ? 11.619 13.656 2.224 1.00 34.58 ? 302 GOL A O2 1 HETATM 1930 C C3 . GOL C 3 . ? 13.692 14.881 2.712 1.00 35.45 ? 302 GOL A C3 1 HETATM 1931 O O3 . GOL C 3 . ? 13.718 15.257 1.332 1.00 34.93 ? 302 GOL A O3 1 HETATM 1932 C C1 . GOL D 3 . ? 7.300 38.499 13.819 1.00 43.25 ? 303 GOL A C1 1 HETATM 1933 O O1 . GOL D 3 . ? 7.916 38.975 12.615 1.00 44.79 ? 303 GOL A O1 1 HETATM 1934 C C2 . GOL D 3 . ? 8.252 38.707 14.996 1.00 42.02 ? 303 GOL A C2 1 HETATM 1935 O O2 . GOL D 3 . ? 7.827 39.852 15.750 1.00 44.07 ? 303 GOL A O2 1 HETATM 1936 C C3 . GOL D 3 . ? 8.327 37.462 15.882 1.00 40.79 ? 303 GOL A C3 1 HETATM 1937 O O3 . GOL D 3 . ? 7.715 37.593 17.177 1.00 37.99 ? 303 GOL A O3 1 HETATM 1938 O O . HOH E 4 . ? -0.945 12.868 -6.889 1.00 56.70 ? 401 HOH A O 1 HETATM 1939 O O . HOH E 4 . ? 19.717 21.396 1.831 1.00 48.10 ? 402 HOH A O 1 HETATM 1940 O O . HOH E 4 . ? 14.977 25.943 -1.963 1.00 51.15 ? 403 HOH A O 1 HETATM 1941 O O . HOH E 4 . ? -16.029 14.546 19.548 1.00 50.64 ? 404 HOH A O 1 HETATM 1942 O O . HOH E 4 . ? 0.774 16.016 25.659 1.00 49.53 ? 405 HOH A O 1 HETATM 1943 O O . HOH E 4 . ? 6.333 46.238 28.431 1.00 44.73 ? 406 HOH A O 1 HETATM 1944 O O . HOH E 4 . ? -17.735 16.657 11.475 1.00 23.25 ? 407 HOH A O 1 HETATM 1945 O O . HOH E 4 . ? -11.931 3.069 12.842 1.00 24.56 ? 408 HOH A O 1 HETATM 1946 O O . HOH E 4 . ? 2.809 35.445 10.180 1.00 46.05 ? 409 HOH A O 1 HETATM 1947 O O . HOH E 4 . ? 10.586 10.575 -5.401 1.00 48.62 ? 410 HOH A O 1 HETATM 1948 O O . HOH E 4 . ? 14.487 29.049 6.888 1.00 54.63 ? 411 HOH A O 1 HETATM 1949 O O . HOH E 4 . ? 9.864 28.382 24.993 1.00 45.25 ? 412 HOH A O 1 HETATM 1950 O O . HOH E 4 . ? -3.761 23.589 17.168 1.00 39.24 ? 413 HOH A O 1 HETATM 1951 O O . HOH E 4 . ? 15.846 38.766 32.233 1.00 57.35 ? 414 HOH A O 1 HETATM 1952 O O . HOH E 4 . ? -8.341 43.924 28.797 1.00 44.36 ? 415 HOH A O 1 HETATM 1953 O O . HOH E 4 . ? -23.786 25.671 3.434 1.00 54.33 ? 416 HOH A O 1 HETATM 1954 O O . HOH E 4 . ? -22.898 25.846 0.674 1.00 50.42 ? 417 HOH A O 1 HETATM 1955 O O . HOH E 4 . ? 9.491 42.586 17.141 1.00 61.50 ? 418 HOH A O 1 HETATM 1956 O O . HOH E 4 . ? -6.227 32.253 28.203 1.00 48.12 ? 419 HOH A O 1 HETATM 1957 O O . HOH E 4 . ? -5.594 29.487 27.171 1.00 59.31 ? 420 HOH A O 1 HETATM 1958 O O . HOH E 4 . ? -4.952 21.150 18.250 1.00 46.95 ? 421 HOH A O 1 HETATM 1959 O O . HOH E 4 . ? -8.445 23.119 21.259 1.00 48.21 ? 422 HOH A O 1 HETATM 1960 O O . HOH E 4 . ? -9.893 42.077 15.801 1.00 33.25 ? 423 HOH A O 1 HETATM 1961 O O . HOH E 4 . ? -8.647 42.599 13.392 1.00 43.09 ? 424 HOH A O 1 HETATM 1962 O O . HOH E 4 . ? 10.910 22.713 33.388 1.00 57.53 ? 425 HOH A O 1 HETATM 1963 O O . HOH E 4 . ? 3.729 52.991 27.625 1.00 48.66 ? 426 HOH A O 1 HETATM 1964 O O . HOH E 4 . ? 0.932 50.553 24.060 1.00 51.53 ? 427 HOH A O 1 HETATM 1965 O O . HOH E 4 . ? -16.262 40.202 12.742 1.00 60.81 ? 428 HOH A O 1 HETATM 1966 O O . HOH E 4 . ? -6.098 44.921 18.443 1.00 50.97 ? 429 HOH A O 1 HETATM 1967 O O . HOH E 4 . ? -16.394 37.198 21.808 1.00 55.49 ? 430 HOH A O 1 HETATM 1968 O O . HOH E 4 . ? -2.138 20.257 -5.561 1.00 56.62 ? 431 HOH A O 1 HETATM 1969 O O . HOH E 4 . ? -3.780 22.307 -6.953 1.00 57.07 ? 432 HOH A O 1 HETATM 1970 O O . HOH E 4 . ? -10.406 20.919 -2.983 1.00 45.66 ? 433 HOH A O 1 HETATM 1971 O O . HOH E 4 . ? -12.161 18.844 -3.464 1.00 49.12 ? 434 HOH A O 1 HETATM 1972 O O . HOH E 4 . ? -6.118 36.132 2.377 1.00 57.93 ? 435 HOH A O 1 HETATM 1973 O O . HOH E 4 . ? 1.961 47.682 18.633 1.00 60.58 ? 436 HOH A O 1 HETATM 1974 O O . HOH E 4 . ? -2.720 42.525 4.537 1.00 59.07 ? 437 HOH A O 1 HETATM 1975 O O . HOH E 4 . ? 2.344 34.220 -0.695 1.00 50.50 ? 438 HOH A O 1 HETATM 1976 O O . HOH E 4 . ? 20.247 14.645 11.018 1.00 45.02 ? 439 HOH A O 1 HETATM 1977 O O . HOH E 4 . ? 20.233 11.824 18.156 1.00 42.72 ? 440 HOH A O 1 HETATM 1978 O O . HOH E 4 . ? 14.965 12.339 21.825 1.00 52.75 ? 441 HOH A O 1 HETATM 1979 O O . HOH E 4 . ? 13.008 15.169 24.494 1.00 50.39 ? 442 HOH A O 1 HETATM 1980 O O . HOH E 4 . ? 10.737 14.078 25.940 1.00 46.63 ? 443 HOH A O 1 HETATM 1981 O O . HOH E 4 . ? -6.219 46.835 6.880 1.00 53.73 ? 444 HOH A O 1 HETATM 1982 O O . HOH E 4 . ? 8.449 31.259 39.767 1.00 66.11 ? 445 HOH A O 1 HETATM 1983 O O . HOH E 4 . ? 2.856 27.062 -1.581 1.00 31.03 ? 446 HOH A O 1 HETATM 1984 O O . HOH E 4 . ? 15.851 23.522 -1.571 1.00 59.20 ? 447 HOH A O 1 HETATM 1985 O O . HOH E 4 . ? 4.816 25.696 36.212 1.00 40.73 ? 448 HOH A O 1 HETATM 1986 O O . HOH E 4 . ? 18.477 23.638 3.123 1.00 39.53 ? 449 HOH A O 1 HETATM 1987 O O . HOH E 4 . ? 19.088 23.130 9.080 1.00 52.96 ? 450 HOH A O 1 HETATM 1988 O O . HOH E 4 . ? -7.533 8.867 6.189 1.00 25.47 ? 451 HOH A O 1 HETATM 1989 O O . HOH E 4 . ? -17.117 15.613 1.355 1.00 24.52 ? 452 HOH A O 1 HETATM 1990 O O . HOH E 4 . ? -17.637 18.055 2.313 1.00 30.04 ? 453 HOH A O 1 HETATM 1991 O O . HOH E 4 . ? 6.201 8.410 0.050 1.00 37.14 ? 454 HOH A O 1 HETATM 1992 O O . HOH E 4 . ? 17.074 14.829 14.454 1.00 36.55 ? 455 HOH A O 1 HETATM 1993 O O . HOH E 4 . ? 14.819 19.074 20.453 1.00 33.93 ? 456 HOH A O 1 HETATM 1994 O O . HOH E 4 . ? -15.028 7.081 11.324 1.00 24.88 ? 457 HOH A O 1 HETATM 1995 O O . HOH E 4 . ? -16.094 21.946 -1.986 1.00 35.05 ? 458 HOH A O 1 HETATM 1996 O O . HOH E 4 . ? 10.091 20.641 -0.977 1.00 24.72 ? 459 HOH A O 1 HETATM 1997 O O . HOH E 4 . ? -19.662 11.462 7.985 1.00 23.60 ? 460 HOH A O 1 HETATM 1998 O O . HOH E 4 . ? -15.456 26.003 10.629 1.00 31.32 ? 461 HOH A O 1 HETATM 1999 O O . HOH E 4 . ? 7.495 33.635 7.836 1.00 31.05 ? 462 HOH A O 1 HETATM 2000 O O . HOH E 4 . ? 6.910 7.496 11.144 1.00 23.93 ? 463 HOH A O 1 HETATM 2001 O O . HOH E 4 . ? -0.723 14.910 27.829 1.00 59.57 ? 464 HOH A O 1 HETATM 2002 O O . HOH E 4 . ? 5.243 36.224 10.437 1.00 45.90 ? 465 HOH A O 1 HETATM 2003 O O . HOH E 4 . ? 4.743 14.563 18.754 1.00 22.51 ? 466 HOH A O 1 HETATM 2004 O O . HOH E 4 . ? 0.365 6.748 12.506 1.00 34.15 ? 467 HOH A O 1 HETATM 2005 O O . HOH E 4 . ? -2.356 10.878 -4.402 1.00 33.18 ? 468 HOH A O 1 HETATM 2006 O O . HOH E 4 . ? 8.272 24.574 -0.320 1.00 29.01 ? 469 HOH A O 1 HETATM 2007 O O . HOH E 4 . ? -5.889 13.353 -2.968 1.00 33.73 ? 470 HOH A O 1 HETATM 2008 O O . HOH E 4 . ? 17.744 16.018 10.227 1.00 28.02 ? 471 HOH A O 1 HETATM 2009 O O . HOH E 4 . ? -7.299 35.270 9.928 1.00 27.61 ? 472 HOH A O 1 HETATM 2010 O O . HOH E 4 . ? -5.975 7.090 7.870 1.00 25.54 ? 473 HOH A O 1 HETATM 2011 O O . HOH E 4 . ? -1.449 6.389 15.967 1.00 30.04 ? 474 HOH A O 1 HETATM 2012 O O . HOH E 4 . ? -7.824 1.867 13.128 1.00 27.63 ? 475 HOH A O 1 HETATM 2013 O O . HOH E 4 . ? 2.041 46.389 15.877 1.00 37.00 ? 476 HOH A O 1 HETATM 2014 O O . HOH E 4 . ? -2.757 3.092 8.514 1.00 45.40 ? 477 HOH A O 1 HETATM 2015 O O . HOH E 4 . ? 6.287 9.593 14.070 1.00 21.76 ? 478 HOH A O 1 HETATM 2016 O O . HOH E 4 . ? -15.669 11.646 18.883 1.00 46.39 ? 479 HOH A O 1 HETATM 2017 O O . HOH E 4 . ? 7.701 22.083 -1.694 1.00 25.70 ? 480 HOH A O 1 HETATM 2018 O O . HOH E 4 . ? 11.138 19.763 -3.398 1.00 32.30 ? 481 HOH A O 1 HETATM 2019 O O . HOH E 4 . ? -19.275 15.905 13.653 1.00 33.38 ? 482 HOH A O 1 HETATM 2020 O O . HOH E 4 . ? 5.861 26.015 -0.373 1.00 32.46 ? 483 HOH A O 1 HETATM 2021 O O . HOH E 4 . ? -15.725 22.718 16.975 1.00 34.63 ? 484 HOH A O 1 HETATM 2022 O O . HOH E 4 . ? 13.493 16.007 21.915 1.00 34.38 ? 485 HOH A O 1 HETATM 2023 O O . HOH E 4 . ? 1.153 29.172 -2.508 1.00 45.85 ? 486 HOH A O 1 HETATM 2024 O O . HOH E 4 . ? -8.749 7.886 1.069 1.00 32.31 ? 487 HOH A O 1 HETATM 2025 O O . HOH E 4 . ? 13.695 13.839 -0.760 1.00 33.39 ? 488 HOH A O 1 HETATM 2026 O O . HOH E 4 . ? -6.516 41.505 11.995 1.00 34.66 ? 489 HOH A O 1 HETATM 2027 O O . HOH E 4 . ? -3.167 26.944 22.821 1.00 33.70 ? 490 HOH A O 1 HETATM 2028 O O . HOH E 4 . ? -9.855 5.769 16.532 1.00 30.47 ? 491 HOH A O 1 HETATM 2029 O O . HOH E 4 . ? -9.604 4.208 2.816 1.00 39.05 ? 492 HOH A O 1 HETATM 2030 O O . HOH E 4 . ? 3.654 10.032 11.056 1.00 37.15 ? 493 HOH A O 1 HETATM 2031 O O . HOH E 4 . ? -11.657 6.824 18.479 1.00 33.55 ? 494 HOH A O 1 HETATM 2032 O O . HOH E 4 . ? 9.742 30.553 7.059 1.00 25.51 ? 495 HOH A O 1 HETATM 2033 O O . HOH E 4 . ? -4.274 34.088 29.401 1.00 37.06 ? 496 HOH A O 1 HETATM 2034 O O . HOH E 4 . ? -13.315 13.299 20.572 1.00 35.23 ? 497 HOH A O 1 HETATM 2035 O O . HOH E 4 . ? -20.060 17.984 15.408 1.00 35.73 ? 498 HOH A O 1 HETATM 2036 O O . HOH E 4 . ? 6.764 15.234 -2.939 1.00 25.02 ? 499 HOH A O 1 HETATM 2037 O O . HOH E 4 . ? 9.410 5.248 -2.114 1.00 32.95 ? 500 HOH A O 1 HETATM 2038 O O . HOH E 4 . ? -14.862 32.682 14.181 1.00 44.16 ? 501 HOH A O 1 HETATM 2039 O O . HOH E 4 . ? -1.106 47.260 12.143 1.00 33.31 ? 502 HOH A O 1 HETATM 2040 O O . HOH E 4 . ? 13.510 36.964 26.742 1.00 36.27 ? 503 HOH A O 1 HETATM 2041 O O . HOH E 4 . ? -7.736 42.235 19.967 1.00 40.52 ? 504 HOH A O 1 HETATM 2042 O O . HOH E 4 . ? 13.449 29.201 3.436 1.00 38.45 ? 505 HOH A O 1 HETATM 2043 O O . HOH E 4 . ? 6.767 41.499 18.904 1.00 32.23 ? 506 HOH A O 1 HETATM 2044 O O . HOH E 4 . ? -2.963 28.591 26.158 1.00 28.92 ? 507 HOH A O 1 HETATM 2045 O O . HOH E 4 . ? 0.807 32.144 0.681 1.00 30.15 ? 508 HOH A O 1 HETATM 2046 O O . HOH E 4 . ? -3.869 30.439 -0.116 1.00 52.25 ? 509 HOH A O 1 HETATM 2047 O O . HOH E 4 . ? -6.190 16.156 -2.851 1.00 47.80 ? 510 HOH A O 1 HETATM 2048 O O . HOH E 4 . ? -5.662 45.230 29.265 1.00 37.91 ? 511 HOH A O 1 HETATM 2049 O O . HOH E 4 . ? 16.660 17.010 16.325 1.00 43.67 ? 512 HOH A O 1 HETATM 2050 O O . HOH E 4 . ? -18.583 13.441 0.145 1.00 36.23 ? 513 HOH A O 1 HETATM 2051 O O . HOH E 4 . ? 12.942 22.114 25.898 1.00 44.75 ? 514 HOH A O 1 HETATM 2052 O O . HOH E 4 . ? -8.005 4.439 18.302 1.00 27.96 ? 515 HOH A O 1 HETATM 2053 O O . HOH E 4 . ? 14.936 18.093 23.278 1.00 41.17 ? 516 HOH A O 1 HETATM 2054 O O . HOH E 4 . ? -14.284 12.615 -5.704 1.00 44.19 ? 517 HOH A O 1 HETATM 2055 O O . HOH E 4 . ? -8.709 34.571 15.319 1.00 26.95 ? 518 HOH A O 1 HETATM 2056 O O . HOH E 4 . ? 13.162 18.722 25.629 1.00 39.79 ? 519 HOH A O 1 HETATM 2057 O O . HOH E 4 . ? -6.953 27.893 -0.103 1.00 31.52 ? 520 HOH A O 1 HETATM 2058 O O . HOH E 4 . ? 2.943 6.354 -1.317 1.00 39.78 ? 521 HOH A O 1 HETATM 2059 O O . HOH E 4 . ? -12.658 22.210 -1.626 1.00 35.87 ? 522 HOH A O 1 HETATM 2060 O O . HOH E 4 . ? 2.015 7.969 14.498 1.00 37.65 ? 523 HOH A O 1 HETATM 2061 O O . HOH E 4 . ? 12.990 10.815 19.538 1.00 27.94 ? 524 HOH A O 1 HETATM 2062 O O . HOH E 4 . ? 11.164 32.202 22.399 1.00 37.63 ? 525 HOH A O 1 HETATM 2063 O O . HOH E 4 . ? 3.020 22.644 28.810 1.00 52.73 ? 526 HOH A O 1 HETATM 2064 O O . HOH E 4 . ? -4.214 0.952 13.608 1.00 36.55 ? 527 HOH A O 1 HETATM 2065 O O . HOH E 4 . ? -9.100 31.356 1.904 1.00 54.01 ? 528 HOH A O 1 HETATM 2066 O O . HOH E 4 . ? -7.492 1.405 4.853 1.00 36.09 ? 529 HOH A O 1 HETATM 2067 O O . HOH E 4 . ? 5.693 35.469 6.842 1.00 40.62 ? 530 HOH A O 1 HETATM 2068 O O . HOH E 4 . ? -12.815 32.409 27.758 1.00 68.40 ? 531 HOH A O 1 HETATM 2069 O O . HOH E 4 . ? -4.605 13.077 26.210 1.00 42.97 ? 532 HOH A O 1 HETATM 2070 O O . HOH E 4 . ? -8.402 28.781 22.960 1.00 45.05 ? 533 HOH A O 1 HETATM 2071 O O . HOH E 4 . ? 8.627 38.673 30.091 1.00 37.38 ? 534 HOH A O 1 HETATM 2072 O O . HOH E 4 . ? -1.742 24.658 20.137 1.00 32.81 ? 535 HOH A O 1 HETATM 2073 O O . HOH E 4 . ? 6.562 15.145 -5.733 1.00 40.09 ? 536 HOH A O 1 HETATM 2074 O O . HOH E 4 . ? -3.494 -1.478 12.345 1.00 51.70 ? 537 HOH A O 1 HETATM 2075 O O . HOH E 4 . ? -5.642 32.116 1.547 1.00 44.34 ? 538 HOH A O 1 HETATM 2076 O O . HOH E 4 . ? 0.964 49.853 33.856 1.00 34.01 ? 539 HOH A O 1 HETATM 2077 O O . HOH E 4 . ? -10.234 10.012 21.668 1.00 33.57 ? 540 HOH A O 1 HETATM 2078 O O . HOH E 4 . ? -24.645 23.180 -2.268 1.00 38.13 ? 541 HOH A O 1 HETATM 2079 O O . HOH E 4 . ? 7.160 43.140 21.223 1.00 38.10 ? 542 HOH A O 1 HETATM 2080 O O . HOH E 4 . ? -10.853 7.834 -1.756 1.00 36.30 ? 543 HOH A O 1 HETATM 2081 O O . HOH E 4 . ? 15.859 12.347 4.067 1.00 40.83 ? 544 HOH A O 1 HETATM 2082 O O . HOH E 4 . ? -1.406 25.245 29.518 1.00 53.21 ? 545 HOH A O 1 HETATM 2083 O O . HOH E 4 . ? 0.242 22.035 -5.799 1.00 56.38 ? 546 HOH A O 1 HETATM 2084 O O . HOH E 4 . ? 14.313 42.059 35.612 1.00 58.93 ? 547 HOH A O 1 HETATM 2085 O O . HOH E 4 . ? -0.696 25.543 -3.785 1.00 46.77 ? 548 HOH A O 1 HETATM 2086 O O . HOH E 4 . ? 8.820 21.378 -5.137 1.00 56.58 ? 549 HOH A O 1 HETATM 2087 O O . HOH E 4 . ? -6.145 7.689 -1.489 1.00 42.32 ? 550 HOH A O 1 HETATM 2088 O O . HOH E 4 . ? 5.234 2.781 20.205 1.00 42.26 ? 551 HOH A O 1 HETATM 2089 O O . HOH E 4 . ? -1.873 32.404 32.217 1.00 55.67 ? 552 HOH A O 1 HETATM 2090 O O . HOH E 4 . ? 2.603 14.416 -7.858 1.00 41.61 ? 553 HOH A O 1 HETATM 2091 O O . HOH E 4 . ? -3.335 18.097 -3.525 1.00 48.88 ? 554 HOH A O 1 HETATM 2092 O O . HOH E 4 . ? -2.933 10.900 26.553 1.00 46.42 ? 555 HOH A O 1 HETATM 2093 O O . HOH E 4 . ? -7.887 19.464 -3.314 1.00 47.33 ? 556 HOH A O 1 HETATM 2094 O O . HOH E 4 . ? 1.841 8.098 10.330 1.00 37.71 ? 557 HOH A O 1 HETATM 2095 O O . HOH E 4 . ? -3.358 44.165 6.842 1.00 53.78 ? 558 HOH A O 1 HETATM 2096 O O . HOH E 4 . ? 0.739 18.470 27.052 1.00 38.09 ? 559 HOH A O 1 HETATM 2097 O O . HOH E 4 . ? -0.205 3.768 8.774 1.00 33.84 ? 560 HOH A O 1 HETATM 2098 O O . HOH E 4 . ? -1.868 4.089 3.559 1.00 53.40 ? 561 HOH A O 1 HETATM 2099 O O . HOH E 4 . ? 15.788 23.968 21.981 1.00 48.41 ? 562 HOH A O 1 HETATM 2100 O O . HOH E 4 . ? 1.096 29.624 31.670 1.00 48.12 ? 563 HOH A O 1 HETATM 2101 O O . HOH E 4 . ? 4.773 6.925 17.621 1.00 36.71 ? 564 HOH A O 1 HETATM 2102 O O . HOH E 4 . ? 11.162 33.092 34.772 1.00 55.50 ? 565 HOH A O 1 HETATM 2103 O O . HOH E 4 . ? -1.520 29.699 28.626 1.00 42.92 ? 566 HOH A O 1 HETATM 2104 O O . HOH E 4 . ? 14.936 25.882 17.555 1.00 49.19 ? 567 HOH A O 1 HETATM 2105 O O . HOH E 4 . ? 8.682 15.183 24.270 1.00 43.28 ? 568 HOH A O 1 HETATM 2106 O O . HOH E 4 . ? -5.233 12.989 -5.858 1.00 48.91 ? 569 HOH A O 1 HETATM 2107 O O . HOH E 4 . ? -10.140 7.065 21.131 1.00 41.52 ? 570 HOH A O 1 HETATM 2108 O O . HOH E 4 . ? -3.583 23.055 21.714 1.00 39.63 ? 571 HOH A O 1 HETATM 2109 O O . HOH E 4 . ? -1.635 2.017 14.377 1.00 45.22 ? 572 HOH A O 1 HETATM 2110 O O . HOH E 4 . ? -13.314 17.709 21.869 1.00 45.73 ? 573 HOH A O 1 HETATM 2111 O O . HOH E 4 . ? 2.836 5.435 6.778 1.00 34.82 ? 574 HOH A O 1 HETATM 2112 O O . HOH E 4 . ? 5.360 22.717 -3.336 1.00 42.44 ? 575 HOH A O 1 HETATM 2113 O O . HOH E 4 . ? -21.884 22.512 12.954 1.00 44.99 ? 576 HOH A O 1 HETATM 2114 O O . HOH E 4 . ? 21.201 11.923 11.617 1.00 36.31 ? 577 HOH A O 1 HETATM 2115 O O . HOH E 4 . ? -0.935 44.817 34.904 1.00 48.72 ? 578 HOH A O 1 HETATM 2116 O O . HOH E 4 . ? -3.023 46.815 16.654 1.00 45.01 ? 579 HOH A O 1 HETATM 2117 O O . HOH E 4 . ? -5.499 37.736 31.910 1.00 40.75 ? 580 HOH A O 1 HETATM 2118 O O . HOH E 4 . ? 18.873 20.132 9.483 1.00 56.85 ? 581 HOH A O 1 HETATM 2119 O O . HOH E 4 . ? 11.319 36.007 28.515 1.00 53.76 ? 582 HOH A O 1 HETATM 2120 O O . HOH E 4 . ? 5.478 22.264 -8.258 1.00 56.16 ? 583 HOH A O 1 HETATM 2121 O O . HOH E 4 . ? -2.118 8.486 25.386 1.00 46.89 ? 584 HOH A O 1 HETATM 2122 O O . HOH E 4 . ? -9.661 38.286 30.779 1.00 55.91 ? 585 HOH A O 1 HETATM 2123 O O . HOH E 4 . ? 5.111 33.566 0.827 1.00 43.45 ? 586 HOH A O 1 HETATM 2124 O O . HOH E 4 . ? -11.914 27.012 1.030 1.00 42.82 ? 587 HOH A O 1 HETATM 2125 O O . HOH E 4 . ? 16.975 25.124 12.506 1.00 43.17 ? 588 HOH A O 1 HETATM 2126 O O . HOH E 4 . ? 6.592 15.510 29.616 1.00 54.58 ? 589 HOH A O 1 HETATM 2127 O O . HOH E 4 . ? -7.336 39.808 32.800 1.00 56.44 ? 590 HOH A O 1 HETATM 2128 O O . HOH E 4 . ? -3.751 39.789 5.031 1.00 54.06 ? 591 HOH A O 1 HETATM 2129 O O . HOH E 4 . ? -1.699 37.593 4.841 1.00 41.91 ? 592 HOH A O 1 HETATM 2130 O O . HOH E 4 . ? -20.366 7.226 -1.714 1.00 33.81 ? 593 HOH A O 1 HETATM 2131 O O . HOH E 4 . ? 13.949 21.537 -1.981 1.00 52.45 ? 594 HOH A O 1 HETATM 2132 O O . HOH E 4 . ? -6.423 19.429 23.824 1.00 51.13 ? 595 HOH A O 1 HETATM 2133 O O . HOH E 4 . ? -10.606 29.595 24.714 1.00 55.09 ? 596 HOH A O 1 HETATM 2134 O O . HOH E 4 . ? -10.529 5.844 0.463 1.00 46.38 ? 597 HOH A O 1 HETATM 2135 O O . HOH E 4 . ? 15.687 10.728 17.463 1.00 37.14 ? 598 HOH A O 1 HETATM 2136 O O . HOH E 4 . ? -20.902 15.274 17.794 1.00 54.70 ? 599 HOH A O 1 HETATM 2137 O O . HOH E 4 . ? 9.471 44.529 10.988 1.00 62.76 ? 600 HOH A O 1 HETATM 2138 O O . HOH E 4 . ? -2.527 24.856 -6.101 1.00 47.35 ? 601 HOH A O 1 HETATM 2139 O O . HOH E 4 . ? -12.432 26.085 14.265 1.00 43.93 ? 602 HOH A O 1 HETATM 2140 O O . HOH E 4 . ? 12.308 31.843 18.163 1.00 54.18 ? 603 HOH A O 1 HETATM 2141 O O . HOH E 4 . ? -9.932 15.203 26.987 1.00 56.94 ? 604 HOH A O 1 HETATM 2142 O O . HOH E 4 . ? -17.152 29.050 7.262 1.00 42.20 ? 605 HOH A O 1 HETATM 2143 O O . HOH E 4 . ? -5.629 20.064 -5.890 1.00 49.87 ? 606 HOH A O 1 HETATM 2144 O O . HOH E 4 . ? -1.588 32.075 -0.699 1.00 48.39 ? 607 HOH A O 1 HETATM 2145 O O . HOH E 4 . ? -3.072 22.121 24.452 1.00 50.86 ? 608 HOH A O 1 HETATM 2146 O O . HOH E 4 . ? 17.597 28.186 7.608 1.00 50.86 ? 609 HOH A O 1 HETATM 2147 O O . HOH E 4 . ? -12.661 30.900 15.102 1.00 55.01 ? 610 HOH A O 1 HETATM 2148 O O . HOH E 4 . ? -4.297 25.737 19.774 1.00 45.72 ? 611 HOH A O 1 HETATM 2149 O O . HOH E 4 . ? 2.763 40.182 33.990 1.00 41.45 ? 612 HOH A O 1 HETATM 2150 O O . HOH E 4 . ? 11.427 34.562 -0.793 1.00 64.45 ? 613 HOH A O 1 HETATM 2151 O O . HOH E 4 . ? 3.549 48.859 24.838 1.00 46.95 ? 614 HOH A O 1 HETATM 2152 O O . HOH E 4 . ? -15.908 13.150 24.805 1.00 58.97 ? 615 HOH A O 1 HETATM 2153 O O . HOH E 4 . ? -9.060 27.104 -3.589 1.00 51.20 ? 616 HOH A O 1 HETATM 2154 O O . HOH E 4 . ? 17.690 25.797 9.263 1.00 56.91 ? 617 HOH A O 1 HETATM 2155 O O . HOH E 4 . ? -19.476 30.493 8.169 1.00 62.88 ? 618 HOH A O 1 HETATM 2156 O O . HOH E 4 . ? -16.623 27.705 12.740 1.00 48.28 ? 619 HOH A O 1 HETATM 2157 O O . HOH E 4 . ? -3.435 28.501 -5.345 1.00 54.69 ? 620 HOH A O 1 HETATM 2158 O O . HOH E 4 . ? 17.241 17.157 0.599 1.00 52.87 ? 621 HOH A O 1 HETATM 2159 O O . HOH E 4 . ? -14.351 38.382 6.851 1.00 52.71 ? 622 HOH A O 1 HETATM 2160 O O . HOH E 4 . ? -4.557 7.247 26.498 1.00 53.88 ? 623 HOH A O 1 HETATM 2161 O O . HOH E 4 . ? 0.626 27.915 29.390 1.00 44.11 ? 624 HOH A O 1 HETATM 2162 O O . HOH E 4 . ? 11.730 34.197 26.293 1.00 55.96 ? 625 HOH A O 1 HETATM 2163 O O . HOH E 4 . ? -10.577 36.650 25.538 1.00 61.95 ? 626 HOH A O 1 HETATM 2164 O O . HOH E 4 . ? 4.540 42.209 35.124 1.00 56.46 ? 627 HOH A O 1 HETATM 2165 O O . HOH E 4 . ? 3.541 39.849 8.132 1.00 49.89 ? 628 HOH A O 1 HETATM 2166 O O . HOH E 4 . ? -0.845 47.128 19.260 1.00 50.29 ? 629 HOH A O 1 HETATM 2167 O O . HOH E 4 . ? 10.062 24.845 -2.422 1.00 45.60 ? 630 HOH A O 1 HETATM 2168 O O . HOH E 4 . ? -16.981 37.639 8.145 1.00 54.80 ? 631 HOH A O 1 HETATM 2169 O O . HOH E 4 . ? -11.772 29.491 17.576 1.00 64.87 ? 632 HOH A O 1 HETATM 2170 O O . HOH E 4 . ? 5.253 38.963 10.442 1.00 41.59 ? 633 HOH A O 1 HETATM 2171 O O . HOH E 4 . ? -18.807 13.749 -7.064 1.00 60.99 ? 634 HOH A O 1 HETATM 2172 O O . HOH E 4 . ? -3.305 36.688 2.481 1.00 52.95 ? 635 HOH A O 1 HETATM 2173 O O . HOH E 4 . ? -12.949 10.330 20.541 1.00 45.01 ? 636 HOH A O 1 HETATM 2174 O O . HOH E 4 . ? -4.643 37.167 36.659 1.00 49.88 ? 637 HOH A O 1 HETATM 2175 O O . HOH E 4 . ? 11.440 36.011 13.666 1.00 56.06 ? 638 HOH A O 1 HETATM 2176 O O . HOH E 4 . ? 18.894 16.244 19.923 1.00 52.86 ? 639 HOH A O 1 HETATM 2177 O O . HOH E 4 . ? 15.896 37.118 20.243 1.00 57.80 ? 640 HOH A O 1 HETATM 2178 O O . HOH E 4 . ? 5.672 41.733 11.009 1.00 45.00 ? 641 HOH A O 1 HETATM 2179 O O . HOH E 4 . ? -12.143 20.379 20.507 1.00 54.37 ? 642 HOH A O 1 HETATM 2180 O O . HOH E 4 . ? -12.247 16.824 -5.583 1.00 53.39 ? 643 HOH A O 1 HETATM 2181 O O . HOH E 4 . ? -0.538 50.324 26.662 1.00 33.40 ? 644 HOH A O 1 HETATM 2182 O O . HOH E 4 . ? 11.476 28.534 22.685 1.00 53.79 ? 645 HOH A O 1 HETATM 2183 O O . HOH E 4 . ? 8.882 16.982 -6.362 1.00 47.67 ? 646 HOH A O 1 HETATM 2184 O O . HOH E 4 . ? 4.661 16.878 -6.959 1.00 42.47 ? 647 HOH A O 1 HETATM 2185 O O . HOH E 4 . ? -4.045 19.631 25.528 1.00 48.48 ? 648 HOH A O 1 HETATM 2186 O O . HOH E 4 . ? 19.446 21.990 25.302 1.00 58.32 ? 649 HOH A O 1 HETATM 2187 O O . HOH E 4 . ? 2.168 32.822 36.378 1.00 60.55 ? 650 HOH A O 1 HETATM 2188 O O . HOH E 4 . ? -1.907 17.546 25.870 1.00 67.26 ? 651 HOH A O 1 HETATM 2189 O O . HOH E 4 . ? -5.785 20.957 21.187 1.00 33.78 ? 652 HOH A O 1 HETATM 2190 O O . HOH E 4 . ? -18.264 15.652 8.901 1.00 35.31 ? 653 HOH A O 1 HETATM 2191 O O . HOH E 4 . ? 5.934 7.679 2.899 1.00 54.72 ? 654 HOH A O 1 HETATM 2192 O O . HOH E 4 . ? -1.077 47.985 35.107 1.00 48.42 ? 655 HOH A O 1 HETATM 2193 O O . HOH E 4 . ? -3.711 23.240 14.314 1.00 32.89 ? 656 HOH A O 1 HETATM 2194 O O . HOH E 4 . ? -5.688 21.357 14.474 1.00 34.78 ? 657 HOH A O 1 HETATM 2195 O O . HOH E 4 . ? -9.070 20.956 14.981 1.00 36.30 ? 658 HOH A O 1 HETATM 2196 O O . HOH E 4 . ? -10.094 21.069 17.671 1.00 53.64 ? 659 HOH A O 1 HETATM 2197 O O . HOH E 4 . ? 8.808 13.898 28.433 1.00 54.91 ? 660 HOH A O 1 HETATM 2198 O O . HOH E 4 . ? 7.443 11.376 27.659 1.00 55.37 ? 661 HOH A O 1 HETATM 2199 O O . HOH E 4 . ? -3.411 3.746 5.962 1.00 38.67 ? 662 HOH A O 1 HETATM 2200 O O . HOH E 4 . ? 7.971 12.247 -6.526 1.00 45.07 ? 663 HOH A O 1 HETATM 2201 O O . HOH E 4 . ? 10.944 20.053 19.103 1.00 32.49 ? 664 HOH A O 1 HETATM 2202 O O . HOH E 4 . ? 10.265 33.242 6.935 1.00 38.83 ? 665 HOH A O 1 HETATM 2203 O O . HOH E 4 . ? 15.400 20.672 25.432 1.00 46.06 ? 666 HOH A O 1 HETATM 2204 O O . HOH E 4 . ? -11.651 10.014 24.232 1.00 38.64 ? 667 HOH A O 1 HETATM 2205 O O . HOH E 4 . ? -11.903 14.076 -5.278 1.00 45.58 ? 668 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 PHE 4 4 4 PHE PHE A . n A 1 5 ARG 5 5 5 ARG ARG A . n A 1 6 LEU 6 6 6 LEU LEU A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 GLY 8 8 8 GLY GLY A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASP 10 10 10 ASP ASP A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 SER 13 13 13 SER SER A . n A 1 14 TYR 14 14 14 TYR TYR A . n A 1 15 GLY 15 15 15 GLY GLY A . n A 1 16 MET 16 16 16 MET MET A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ILE 18 18 18 ILE ILE A . n A 1 19 LYS 19 19 19 LYS LYS A . n A 1 20 ASP 20 20 20 ASP ASP A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 PRO 26 26 26 PRO PRO A . n A 1 27 HIS 27 27 27 HIS HIS A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 GLU 29 29 29 GLU GLU A . n A 1 30 LYS 30 30 30 LYS LYS A . n A 1 31 VAL 31 31 31 VAL VAL A . n A 1 32 TYR 32 32 32 TYR TYR A . n A 1 33 ASN 33 33 33 ASN ASN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 PRO 35 35 35 PRO PRO A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 VAL 41 41 41 VAL VAL A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 GLY 43 43 43 GLY GLY A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 TYR 47 47 47 TYR TYR A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 LEU 49 49 49 LEU LEU A . n A 1 50 MET 50 50 50 MET MET A . n A 1 51 HIS 51 51 51 HIS HIS A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 PHE 53 53 53 PHE PHE A . n A 1 54 ASN 54 54 54 ASN ASN A . n A 1 55 TYR 55 55 55 TYR TYR A . n A 1 56 ASP 56 56 56 ASP ASP A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 ASN 58 58 58 ASN ASN A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 VAL 62 62 62 VAL VAL A . n A 1 63 ALA 63 63 63 ALA ALA A . n A 1 64 VAL 64 64 64 VAL VAL A . n A 1 65 ASP 65 65 65 ASP ASP A . n A 1 66 VAL 66 66 66 VAL VAL A . n A 1 67 THR 67 67 67 THR THR A . n A 1 68 ASN 68 68 68 ASN ASN A . n A 1 69 VAL 69 69 69 VAL VAL A . n A 1 70 TYR 70 70 70 TYR TYR A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 MET 72 72 72 MET MET A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 TYR 74 74 74 TYR TYR A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 THR 78 78 78 THR THR A . n A 1 79 THR 79 79 79 THR THR A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 TYR 81 81 81 TYR TYR A . n A 1 82 PHE 82 82 82 PHE PHE A . n A 1 83 PHE 83 83 83 PHE PHE A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 GLU 85 85 85 GLU GLU A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 ALA 87 87 87 ALA ALA A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 ASP 89 89 89 ASP ASP A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 ALA 91 91 91 ALA ALA A . n A 1 92 SER 92 92 92 SER SER A . n A 1 93 GLN 93 93 93 GLN GLN A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 VAL 95 95 95 VAL VAL A . n A 1 96 PHE 96 96 96 PHE PHE A . n A 1 97 ARG 97 97 97 ARG ARG A . n A 1 98 SER 98 98 98 SER SER A . n A 1 99 ALA 99 99 99 ALA ALA A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 ARG 101 101 101 ARG ARG A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 ILE 103 103 103 ILE ILE A . n A 1 104 THR 104 104 104 THR THR A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 TYR 107 107 107 TYR TYR A . n A 1 108 SER 108 108 108 SER SER A . n A 1 109 GLY 109 109 109 GLY GLY A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 TYR 111 111 111 TYR TYR A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 LYS 120 120 120 LYS LYS A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 LYS 124 124 124 LYS LYS A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 PRO 126 126 126 PRO PRO A . n A 1 127 ILE 127 127 127 ILE ILE A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 ASP 133 133 133 ASP ASP A . n A 1 134 THR 134 134 134 THR THR A . n A 1 135 ALA 135 135 135 ALA ALA A . n A 1 136 ILE 136 136 136 ILE ILE A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 HIS 141 141 141 HIS HIS A . n A 1 142 TYR 142 142 142 TYR TYR A . n A 1 143 ASP 143 143 143 ASP ASP A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 THR 145 145 145 THR THR A . n A 1 146 ALA 146 146 146 ALA ALA A . n A 1 147 ALA 147 147 147 ALA ALA A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 VAL 153 153 153 VAL VAL A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 ALA 159 159 159 ALA ALA A . n A 1 160 GLU 160 160 160 GLU GLU A . n A 1 161 ALA 161 161 161 ALA ALA A . n A 1 162 ALA 162 162 162 ALA ALA A . n A 1 163 ARG 163 163 163 ARG ARG A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 LYS 165 165 165 LYS LYS A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 ILE 167 167 167 ILE ILE A . n A 1 168 GLU 168 168 168 GLU GLU A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLN 170 170 170 GLN GLN A . n A 1 171 ILE 171 171 171 ILE ILE A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 GLU 173 173 173 GLU GLU A . n A 1 174 ARG 174 174 174 ARG ARG A . n A 1 175 ALA 175 175 175 ALA ALA A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 ARG 177 177 177 ARG ARG A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 SER 182 182 182 SER SER A . n A 1 183 SER 183 183 183 SER SER A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 THR 185 185 185 THR THR A . n A 1 186 ILE 186 186 186 ILE ILE A . n A 1 187 SER 187 187 187 SER SER A . n A 1 188 LEU 188 188 188 LEU LEU A . n A 1 189 GLU 189 189 189 GLU GLU A . n A 1 190 ASN 190 190 190 ASN ASN A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 TRP 192 192 192 TRP TRP A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 LEU 195 195 195 LEU LEU A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 LYS 197 197 197 LYS LYS A . n A 1 198 GLN 198 198 198 GLN GLN A . n A 1 199 ILE 199 199 199 ILE ILE A . n A 1 200 GLN 200 200 200 GLN GLN A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 ALA 202 202 202 ALA ALA A . n A 1 203 GLN 203 203 203 GLN GLN A . n A 1 204 GLY 204 204 204 GLY GLY A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 PHE 209 209 209 PHE PHE A . n A 1 210 ARG 210 210 210 ARG ARG A . n A 1 211 THR 211 211 211 THR THR A . n A 1 212 PRO 212 212 212 PRO PRO A . n A 1 213 THR 213 213 213 THR THR A . n A 1 214 VAL 214 214 214 VAL VAL A . n A 1 215 LEU 215 215 215 LEU LEU A . n A 1 216 VAL 216 216 216 VAL VAL A . n A 1 217 ASP 217 217 217 ASP ASP A . n A 1 218 SER 218 218 218 SER SER A . n A 1 219 LYS 219 219 219 LYS LYS A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 ASN 221 221 221 ASN ASN A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 VAL 223 223 223 VAL VAL A . n A 1 224 GLN 224 224 224 GLN GLN A . n A 1 225 ILE 225 225 225 ILE ILE A . n A 1 226 THR 226 226 226 THR THR A . n A 1 227 ASN 227 227 227 ASN ASN A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 THR 229 229 229 THR THR A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 VAL 232 232 232 VAL VAL A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ILE 237 237 237 ILE ILE A . n A 1 238 GLN 238 238 238 GLN GLN A . n A 1 239 LEU 239 239 239 LEU LEU A . n A 1 240 LEU 240 240 240 LEU LEU A . n A 1 241 LEU 241 241 241 LEU LEU A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 ASN 245 245 245 ASN ASN A . n A 1 246 ILE 246 246 246 ILE ILE A . n # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 227 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 227 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # _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 2013-06-12 2 'Structure model' 1 1 2013-07-17 # _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 'Structure summary' # 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 ? ? 56.71 -104.72 2 1 PRO A 106 ? ? -84.52 40.27 3 1 ASP A 143 ? ? -160.73 99.93 4 1 THR A 158 ? ? -118.24 -80.54 5 1 ASN A 236 ? ? -101.44 -66.75 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 GLYCEROL GOL 4 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 301 301 NAG NAG A . C 3 GOL 1 302 247 GOL GOL A . D 3 GOL 1 303 248 GOL GOL A . E 4 HOH 1 401 2 HOH HOH A . E 4 HOH 2 402 3 HOH HOH A . E 4 HOH 3 403 4 HOH HOH A . E 4 HOH 4 404 5 HOH HOH A . E 4 HOH 5 405 6 HOH HOH A . E 4 HOH 6 406 7 HOH HOH A . E 4 HOH 7 407 8 HOH HOH A . E 4 HOH 8 408 9 HOH HOH A . E 4 HOH 9 409 10 HOH HOH A . E 4 HOH 10 410 11 HOH HOH A . E 4 HOH 11 411 12 HOH HOH A . E 4 HOH 12 412 13 HOH HOH A . E 4 HOH 13 413 14 HOH HOH A . E 4 HOH 14 414 15 HOH HOH A . E 4 HOH 15 415 16 HOH HOH A . E 4 HOH 16 416 18 HOH HOH A . E 4 HOH 17 417 19 HOH HOH A . E 4 HOH 18 418 20 HOH HOH A . E 4 HOH 19 419 21 HOH HOH A . E 4 HOH 20 420 22 HOH HOH A . E 4 HOH 21 421 23 HOH HOH A . E 4 HOH 22 422 24 HOH HOH A . E 4 HOH 23 423 25 HOH HOH A . E 4 HOH 24 424 26 HOH HOH A . E 4 HOH 25 425 28 HOH HOH A . E 4 HOH 26 426 29 HOH HOH A . E 4 HOH 27 427 30 HOH HOH A . E 4 HOH 28 428 31 HOH HOH A . E 4 HOH 29 429 32 HOH HOH A . E 4 HOH 30 430 33 HOH HOH A . E 4 HOH 31 431 34 HOH HOH A . E 4 HOH 32 432 35 HOH HOH A . E 4 HOH 33 433 36 HOH HOH A . E 4 HOH 34 434 37 HOH HOH A . E 4 HOH 35 435 38 HOH HOH A . E 4 HOH 36 436 39 HOH HOH A . E 4 HOH 37 437 40 HOH HOH A . E 4 HOH 38 438 42 HOH HOH A . E 4 HOH 39 439 43 HOH HOH A . E 4 HOH 40 440 44 HOH HOH A . E 4 HOH 41 441 45 HOH HOH A . E 4 HOH 42 442 46 HOH HOH A . E 4 HOH 43 443 47 HOH HOH A . E 4 HOH 44 444 49 HOH HOH A . E 4 HOH 45 445 50 HOH HOH A . E 4 HOH 46 446 51 HOH HOH A . E 4 HOH 47 447 52 HOH HOH A . E 4 HOH 48 448 53 HOH HOH A . E 4 HOH 49 449 54 HOH HOH A . E 4 HOH 50 450 55 HOH HOH A . E 4 HOH 51 451 56 HOH HOH A . E 4 HOH 52 452 57 HOH HOH A . E 4 HOH 53 453 58 HOH HOH A . E 4 HOH 54 454 59 HOH HOH A . E 4 HOH 55 455 60 HOH HOH A . E 4 HOH 56 456 61 HOH HOH A . E 4 HOH 57 457 62 HOH HOH A . E 4 HOH 58 458 63 HOH HOH A . E 4 HOH 59 459 64 HOH HOH A . E 4 HOH 60 460 65 HOH HOH A . E 4 HOH 61 461 66 HOH HOH A . E 4 HOH 62 462 67 HOH HOH A . E 4 HOH 63 463 68 HOH HOH A . E 4 HOH 64 464 69 HOH HOH A . E 4 HOH 65 465 70 HOH HOH A . E 4 HOH 66 466 71 HOH HOH A . E 4 HOH 67 467 72 HOH HOH A . E 4 HOH 68 468 73 HOH HOH A . E 4 HOH 69 469 74 HOH HOH A . E 4 HOH 70 470 75 HOH HOH A . E 4 HOH 71 471 76 HOH HOH A . E 4 HOH 72 472 77 HOH HOH A . E 4 HOH 73 473 78 HOH HOH A . E 4 HOH 74 474 79 HOH HOH A . E 4 HOH 75 475 80 HOH HOH A . E 4 HOH 76 476 81 HOH HOH A . E 4 HOH 77 477 82 HOH HOH A . E 4 HOH 78 478 83 HOH HOH A . E 4 HOH 79 479 84 HOH HOH A . E 4 HOH 80 480 85 HOH HOH A . E 4 HOH 81 481 86 HOH HOH A . E 4 HOH 82 482 87 HOH HOH A . E 4 HOH 83 483 88 HOH HOH A . E 4 HOH 84 484 89 HOH HOH A . E 4 HOH 85 485 90 HOH HOH A . E 4 HOH 86 486 92 HOH HOH A . E 4 HOH 87 487 93 HOH HOH A . E 4 HOH 88 488 94 HOH HOH A . E 4 HOH 89 489 95 HOH HOH A . E 4 HOH 90 490 96 HOH HOH A . E 4 HOH 91 491 97 HOH HOH A . E 4 HOH 92 492 98 HOH HOH A . E 4 HOH 93 493 99 HOH HOH A . E 4 HOH 94 494 100 HOH HOH A . E 4 HOH 95 495 101 HOH HOH A . E 4 HOH 96 496 102 HOH HOH A . E 4 HOH 97 497 103 HOH HOH A . E 4 HOH 98 498 104 HOH HOH A . E 4 HOH 99 499 105 HOH HOH A . E 4 HOH 100 500 106 HOH HOH A . E 4 HOH 101 501 107 HOH HOH A . E 4 HOH 102 502 108 HOH HOH A . E 4 HOH 103 503 109 HOH HOH A . E 4 HOH 104 504 110 HOH HOH A . E 4 HOH 105 505 111 HOH HOH A . E 4 HOH 106 506 112 HOH HOH A . E 4 HOH 107 507 113 HOH HOH A . E 4 HOH 108 508 114 HOH HOH A . E 4 HOH 109 509 115 HOH HOH A . E 4 HOH 110 510 116 HOH HOH A . E 4 HOH 111 511 117 HOH HOH A . E 4 HOH 112 512 118 HOH HOH A . E 4 HOH 113 513 119 HOH HOH A . E 4 HOH 114 514 120 HOH HOH A . E 4 HOH 115 515 121 HOH HOH A . E 4 HOH 116 516 122 HOH HOH A . E 4 HOH 117 517 123 HOH HOH A . E 4 HOH 118 518 124 HOH HOH A . E 4 HOH 119 519 125 HOH HOH A . E 4 HOH 120 520 126 HOH HOH A . E 4 HOH 121 521 127 HOH HOH A . E 4 HOH 122 522 128 HOH HOH A . E 4 HOH 123 523 129 HOH HOH A . E 4 HOH 124 524 130 HOH HOH A . E 4 HOH 125 525 131 HOH HOH A . E 4 HOH 126 526 132 HOH HOH A . E 4 HOH 127 527 133 HOH HOH A . E 4 HOH 128 528 134 HOH HOH A . E 4 HOH 129 529 135 HOH HOH A . E 4 HOH 130 530 136 HOH HOH A . E 4 HOH 131 531 137 HOH HOH A . E 4 HOH 132 532 138 HOH HOH A . E 4 HOH 133 533 139 HOH HOH A . E 4 HOH 134 534 140 HOH HOH A . E 4 HOH 135 535 141 HOH HOH A . E 4 HOH 136 536 142 HOH HOH A . E 4 HOH 137 537 143 HOH HOH A . E 4 HOH 138 538 144 HOH HOH A . E 4 HOH 139 539 145 HOH HOH A . E 4 HOH 140 540 146 HOH HOH A . E 4 HOH 141 541 147 HOH HOH A . E 4 HOH 142 542 148 HOH HOH A . E 4 HOH 143 543 149 HOH HOH A . E 4 HOH 144 544 150 HOH HOH A . E 4 HOH 145 545 151 HOH HOH A . E 4 HOH 146 546 152 HOH HOH A . E 4 HOH 147 547 153 HOH HOH A . E 4 HOH 148 548 154 HOH HOH A . E 4 HOH 149 549 155 HOH HOH A . E 4 HOH 150 550 156 HOH HOH A . E 4 HOH 151 551 157 HOH HOH A . E 4 HOH 152 552 159 HOH HOH A . E 4 HOH 153 553 160 HOH HOH A . E 4 HOH 154 554 161 HOH HOH A . E 4 HOH 155 555 162 HOH HOH A . E 4 HOH 156 556 163 HOH HOH A . E 4 HOH 157 557 164 HOH HOH A . E 4 HOH 158 558 165 HOH HOH A . E 4 HOH 159 559 166 HOH HOH A . E 4 HOH 160 560 167 HOH HOH A . E 4 HOH 161 561 168 HOH HOH A . E 4 HOH 162 562 169 HOH HOH A . E 4 HOH 163 563 170 HOH HOH A . E 4 HOH 164 564 171 HOH HOH A . E 4 HOH 165 565 172 HOH HOH A . E 4 HOH 166 566 173 HOH HOH A . E 4 HOH 167 567 174 HOH HOH A . E 4 HOH 168 568 175 HOH HOH A . E 4 HOH 169 569 176 HOH HOH A . E 4 HOH 170 570 177 HOH HOH A . E 4 HOH 171 571 178 HOH HOH A . E 4 HOH 172 572 179 HOH HOH A . E 4 HOH 173 573 180 HOH HOH A . E 4 HOH 174 574 181 HOH HOH A . E 4 HOH 175 575 183 HOH HOH A . E 4 HOH 176 576 184 HOH HOH A . E 4 HOH 177 577 185 HOH HOH A . E 4 HOH 178 578 186 HOH HOH A . E 4 HOH 179 579 187 HOH HOH A . E 4 HOH 180 580 188 HOH HOH A . E 4 HOH 181 581 189 HOH HOH A . E 4 HOH 182 582 190 HOH HOH A . E 4 HOH 183 583 191 HOH HOH A . E 4 HOH 184 584 192 HOH HOH A . E 4 HOH 185 585 194 HOH HOH A . E 4 HOH 186 586 195 HOH HOH A . E 4 HOH 187 587 196 HOH HOH A . E 4 HOH 188 588 197 HOH HOH A . E 4 HOH 189 589 198 HOH HOH A . E 4 HOH 190 590 199 HOH HOH A . E 4 HOH 191 591 200 HOH HOH A . E 4 HOH 192 592 201 HOH HOH A . E 4 HOH 193 593 202 HOH HOH A . E 4 HOH 194 594 203 HOH HOH A . E 4 HOH 195 595 204 HOH HOH A . E 4 HOH 196 596 205 HOH HOH A . E 4 HOH 197 597 206 HOH HOH A . E 4 HOH 198 598 207 HOH HOH A . E 4 HOH 199 599 208 HOH HOH A . E 4 HOH 200 600 209 HOH HOH A . E 4 HOH 201 601 210 HOH HOH A . E 4 HOH 202 602 211 HOH HOH A . E 4 HOH 203 603 212 HOH HOH A . E 4 HOH 204 604 213 HOH HOH A . E 4 HOH 205 605 214 HOH HOH A . E 4 HOH 206 606 217 HOH HOH A . E 4 HOH 207 607 219 HOH HOH A . E 4 HOH 208 608 220 HOH HOH A . E 4 HOH 209 609 221 HOH HOH A . E 4 HOH 210 610 222 HOH HOH A . E 4 HOH 211 611 223 HOH HOH A . E 4 HOH 212 612 224 HOH HOH A . E 4 HOH 213 613 225 HOH HOH A . E 4 HOH 214 614 226 HOH HOH A . E 4 HOH 215 615 227 HOH HOH A . E 4 HOH 216 616 228 HOH HOH A . E 4 HOH 217 617 229 HOH HOH A . E 4 HOH 218 618 231 HOH HOH A . E 4 HOH 219 619 232 HOH HOH A . E 4 HOH 220 620 233 HOH HOH A . E 4 HOH 221 621 234 HOH HOH A . E 4 HOH 222 622 235 HOH HOH A . E 4 HOH 223 623 236 HOH HOH A . E 4 HOH 224 624 237 HOH HOH A . E 4 HOH 225 625 238 HOH HOH A . E 4 HOH 226 626 240 HOH HOH A . E 4 HOH 227 627 241 HOH HOH A . E 4 HOH 228 628 242 HOH HOH A . E 4 HOH 229 629 243 HOH HOH A . E 4 HOH 230 630 244 HOH HOH A . E 4 HOH 231 631 245 HOH HOH A . E 4 HOH 232 632 246 HOH HOH A . E 4 HOH 233 633 247 HOH HOH A . E 4 HOH 234 634 248 HOH HOH A . E 4 HOH 235 635 249 HOH HOH A . E 4 HOH 236 636 252 HOH HOH A . E 4 HOH 237 637 253 HOH HOH A . E 4 HOH 238 638 254 HOH HOH A . E 4 HOH 239 639 255 HOH HOH A . E 4 HOH 240 640 256 HOH HOH A . E 4 HOH 241 641 257 HOH HOH A . E 4 HOH 242 642 258 HOH HOH A . E 4 HOH 243 643 259 HOH HOH A . E 4 HOH 244 644 260 HOH HOH A . E 4 HOH 245 645 261 HOH HOH A . E 4 HOH 246 646 263 HOH HOH A . E 4 HOH 247 647 265 HOH HOH A . E 4 HOH 248 648 266 HOH HOH A . E 4 HOH 249 649 268 HOH HOH A . E 4 HOH 250 650 269 HOH HOH A . E 4 HOH 251 651 270 HOH HOH A . E 4 HOH 252 652 271 HOH HOH A . E 4 HOH 253 653 272 HOH HOH A . E 4 HOH 254 654 273 HOH HOH A . E 4 HOH 255 655 274 HOH HOH A . E 4 HOH 256 656 275 HOH HOH A . E 4 HOH 257 657 276 HOH HOH A . E 4 HOH 258 658 277 HOH HOH A . E 4 HOH 259 659 278 HOH HOH A . E 4 HOH 260 660 281 HOH HOH A . E 4 HOH 261 661 282 HOH HOH A . E 4 HOH 262 662 283 HOH HOH A . E 4 HOH 263 663 284 HOH HOH A . E 4 HOH 264 664 285 HOH HOH A . E 4 HOH 265 665 286 HOH HOH A . E 4 HOH 266 666 287 HOH HOH A . E 4 HOH 267 667 288 HOH HOH A . E 4 HOH 268 668 289 HOH HOH A . #