data_3KTZ # _entry.id 3KTZ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3KTZ RCSB RCSB056444 WWPDB D_1000056444 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3KU0 _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.entry_id 3KTZ _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2009-11-26 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # _audit_author.name 'Kong, X.-P.' _audit_author.pdbx_ordinal 1 # _citation.id primary _citation.title ;A new activity of anti-HIV and anti-tumor protein GAP31: DNA adenosine glycosidase--structural and modeling insight into its functions. ; _citation.journal_abbrev Biochem.Biophys.Res.Commun. _citation.journal_volume 391 _citation.page_first 340 _citation.page_last 345 _citation.year 2010 _citation.journal_id_ASTM BBRCA9 _citation.country US _citation.journal_id_ISSN 0006-291X _citation.journal_id_CSD 0146 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19913503 _citation.pdbx_database_id_DOI 10.1016/j.bbrc.2009.11.060 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Li, H.G.' 1 primary 'Huang, P.L.' 2 primary 'Zhang, D.' 3 primary 'Sun, Y.' 4 primary 'Chen, H.C.' 5 primary 'Zhang, J.' 6 primary 'Huang, P.L.' 7 primary 'Kong, X.P.' 8 primary 'Lee-Huang, S.' 9 # _cell.length_a 48.373 _cell.length_b 44.395 _cell.length_c 137.270 _cell.angle_alpha 90.000 _cell.angle_beta 98.380 _cell.angle_gamma 90.000 _cell.entry_id 3KTZ _cell.pdbx_unique_axis ? _cell.Z_PDB 4 _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.space_group_name_H-M 'P 1 21 1' _symmetry.entry_id 3KTZ _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.Int_Tables_number 4 _symmetry.cell_setting ? _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 'Ribosome-inactivating protein gelonin' 28209.184 2 3.2.2.22 ? '(UNP residue 47-297)' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 water nat water 18.015 199 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'rRNA N-glycosidase' # _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 ;GLDTVSFSTKGATYITYVNFLNELRVKLKPEGNSHGIPLLRKKCDDPGKCFVLVALSNDNGQLAEIAIDVTSVYVVGYQV RNRSYFFKDAPDAAYEGLFKNTIKTRLHFGGSYPSLEGEKAYRETTDLGIEPLRIGIKKLDENAIDNYKPTEIASSLLVV IQMVSEAARFTFIENQIRNNFQQRIRPANNTISLENKWGKLSFQIRTSGANGMFSEAVELERANGKKYYVTAVDQVKPKI ALLKFVDKDPK ; _entity_poly.pdbx_seq_one_letter_code_can ;GLDTVSFSTKGATYITYVNFLNELRVKLKPEGNSHGIPLLRKKCDDPGKCFVLVALSNDNGQLAEIAIDVTSVYVVGYQV RNRSYFFKDAPDAAYEGLFKNTIKTRLHFGGSYPSLEGEKAYRETTDLGIEPLRIGIKKLDENAIDNYKPTEIASSLLVV IQMVSEAARFTFIENQIRNNFQQRIRPANNTISLENKWGKLSFQIRTSGANGMFSEAVELERANGKKYYVTAVDQVKPKI ALLKFVDKDPK ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 LEU n 1 3 ASP n 1 4 THR n 1 5 VAL n 1 6 SER n 1 7 PHE n 1 8 SER n 1 9 THR n 1 10 LYS n 1 11 GLY n 1 12 ALA n 1 13 THR n 1 14 TYR n 1 15 ILE n 1 16 THR n 1 17 TYR n 1 18 VAL n 1 19 ASN n 1 20 PHE n 1 21 LEU n 1 22 ASN n 1 23 GLU n 1 24 LEU n 1 25 ARG n 1 26 VAL n 1 27 LYS n 1 28 LEU n 1 29 LYS n 1 30 PRO n 1 31 GLU n 1 32 GLY n 1 33 ASN n 1 34 SER n 1 35 HIS n 1 36 GLY n 1 37 ILE n 1 38 PRO n 1 39 LEU n 1 40 LEU n 1 41 ARG n 1 42 LYS n 1 43 LYS n 1 44 CYS n 1 45 ASP n 1 46 ASP n 1 47 PRO n 1 48 GLY n 1 49 LYS n 1 50 CYS n 1 51 PHE n 1 52 VAL n 1 53 LEU n 1 54 VAL n 1 55 ALA n 1 56 LEU n 1 57 SER n 1 58 ASN n 1 59 ASP n 1 60 ASN n 1 61 GLY n 1 62 GLN n 1 63 LEU n 1 64 ALA n 1 65 GLU n 1 66 ILE n 1 67 ALA n 1 68 ILE n 1 69 ASP n 1 70 VAL n 1 71 THR n 1 72 SER n 1 73 VAL n 1 74 TYR n 1 75 VAL n 1 76 VAL n 1 77 GLY n 1 78 TYR n 1 79 GLN n 1 80 VAL n 1 81 ARG n 1 82 ASN n 1 83 ARG n 1 84 SER n 1 85 TYR n 1 86 PHE n 1 87 PHE n 1 88 LYS n 1 89 ASP n 1 90 ALA n 1 91 PRO n 1 92 ASP n 1 93 ALA n 1 94 ALA n 1 95 TYR n 1 96 GLU n 1 97 GLY n 1 98 LEU n 1 99 PHE n 1 100 LYS n 1 101 ASN n 1 102 THR n 1 103 ILE n 1 104 LYS n 1 105 THR n 1 106 ARG n 1 107 LEU n 1 108 HIS n 1 109 PHE n 1 110 GLY n 1 111 GLY n 1 112 SER n 1 113 TYR n 1 114 PRO n 1 115 SER n 1 116 LEU n 1 117 GLU n 1 118 GLY n 1 119 GLU n 1 120 LYS n 1 121 ALA n 1 122 TYR n 1 123 ARG n 1 124 GLU n 1 125 THR n 1 126 THR n 1 127 ASP n 1 128 LEU n 1 129 GLY n 1 130 ILE n 1 131 GLU n 1 132 PRO n 1 133 LEU n 1 134 ARG n 1 135 ILE n 1 136 GLY n 1 137 ILE n 1 138 LYS n 1 139 LYS n 1 140 LEU n 1 141 ASP n 1 142 GLU n 1 143 ASN n 1 144 ALA n 1 145 ILE n 1 146 ASP n 1 147 ASN n 1 148 TYR n 1 149 LYS n 1 150 PRO n 1 151 THR n 1 152 GLU n 1 153 ILE n 1 154 ALA n 1 155 SER n 1 156 SER n 1 157 LEU n 1 158 LEU n 1 159 VAL n 1 160 VAL n 1 161 ILE n 1 162 GLN n 1 163 MET n 1 164 VAL n 1 165 SER n 1 166 GLU n 1 167 ALA n 1 168 ALA n 1 169 ARG n 1 170 PHE n 1 171 THR n 1 172 PHE n 1 173 ILE n 1 174 GLU n 1 175 ASN n 1 176 GLN n 1 177 ILE n 1 178 ARG n 1 179 ASN n 1 180 ASN n 1 181 PHE n 1 182 GLN n 1 183 GLN n 1 184 ARG n 1 185 ILE n 1 186 ARG n 1 187 PRO n 1 188 ALA n 1 189 ASN n 1 190 ASN n 1 191 THR n 1 192 ILE n 1 193 SER n 1 194 LEU n 1 195 GLU n 1 196 ASN n 1 197 LYS n 1 198 TRP n 1 199 GLY n 1 200 LYS n 1 201 LEU n 1 202 SER n 1 203 PHE n 1 204 GLN n 1 205 ILE n 1 206 ARG n 1 207 THR n 1 208 SER n 1 209 GLY n 1 210 ALA n 1 211 ASN n 1 212 GLY n 1 213 MET n 1 214 PHE n 1 215 SER n 1 216 GLU n 1 217 ALA n 1 218 VAL n 1 219 GLU n 1 220 LEU n 1 221 GLU n 1 222 ARG n 1 223 ALA n 1 224 ASN n 1 225 GLY n 1 226 LYS n 1 227 LYS n 1 228 TYR n 1 229 TYR n 1 230 VAL n 1 231 THR n 1 232 ALA n 1 233 VAL n 1 234 ASP n 1 235 GLN n 1 236 VAL n 1 237 LYS n 1 238 PRO n 1 239 LYS n 1 240 ILE n 1 241 ALA n 1 242 LEU n 1 243 LEU n 1 244 LYS n 1 245 PHE n 1 246 VAL n 1 247 ASP n 1 248 LYS n 1 249 ASP n 1 250 PRO n 1 251 LYS 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 'Euphorbiaceae himalaya' _entity_src_nat.pdbx_organism_scientific 'Gelonium multiflorum' _entity_src_nat.pdbx_ncbi_taxonomy_id 3979 _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 'Isolated from seeds of Gelonium multiflorum' # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code RIPG_GELMU _struct_ref.pdbx_db_accession P33186 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;GLDTVSFSTKGATYITYVNFLNELRVKLKPEGNSHGIPLLRKKCDDPGKCFVLVALSNDNGQLAEIAIDVTSVYVVGYQV RNRSYFFKDAPDAAYEGLFKNTIKTRLHFGGSYPSLEGEKAYRETTDLGIEPLRIGIKKLDENAIDNYKPTEIASSLLVV IQMVSEAARFTFIENQIRNNFQQRIRPANNTISLENKWGKLSFQIRTSGANGMFSEAVELERANGKKYYVTAVDQVKPKI ALLKFVDKDPK ; _struct_ref.pdbx_align_begin 47 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3KTZ A 1 ? 251 ? P33186 47 ? 297 ? 1 251 2 1 3KTZ B 1 ? 251 ? P33186 47 ? 297 ? 1 251 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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.crystals_number 1 _exptl.entry_id 3KTZ _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.58 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 52.41 _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.pH 8.5 _exptl_crystal_grow.temp 300 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '100 mM Tris-HCl, pH 8.5, 2.0 M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 300K' _exptl_crystal_grow.pdbx_pH_range ? # loop_ _diffrn.id _diffrn.ambient_temp _diffrn.ambient_temp_details _diffrn.crystal_id 1 125 ? 1 2 ? ? 1 3 ? ? 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 210' _diffrn_detector.pdbx_collection_date 2003-10-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator CCD _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0 _diffrn_radiation_wavelength.wt 1.0 # loop_ _diffrn_source.diffrn_id _diffrn_source.source _diffrn_source.type _diffrn_source.pdbx_wavelength _diffrn_source.pdbx_wavelength_list _diffrn_source.pdbx_synchrotron_site _diffrn_source.pdbx_synchrotron_beamline 1 SYNCHROTRON 'NSLS BEAMLINE X12B' ? 1.0 NSLS X12B 2 SYNCHROTRON 'NSLS BEAMLINE X26C' ? 1.0 NSLS X26C 3 SYNCHROTRON 'APS BEAMLINE 19-BM' ? 1.0 APS 19-BM # _reflns.entry_id 3KTZ _reflns.B_iso_Wilson_estimate 20.500 _reflns.observed_criterion_sigma_F 2.0 _reflns.observed_criterion_sigma_I 2.0 _reflns.d_resolution_high 1.6 _reflns.d_resolution_low 47.35 _reflns.number_all 65240 _reflns.number_obs 228644 _reflns.percent_possible_obs 99.2 _reflns.pdbx_Rmerge_I_obs .036 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _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_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 1.6 _reflns_shell.d_res_low 1.7 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 90 _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_redundancy ? _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_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 3KTZ _refine.ls_d_res_high 1.600 _refine.ls_d_res_low 47.350 _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF 528379.000 _refine.pdbx_data_cutoff_low_absF 0.000 _refine.ls_percent_reflns_obs 99.2 _refine.ls_number_reflns_obs 69976 _refine.ls_number_reflns_all 65766 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_R_Free_selection_details RANDOM _refine.details 'BULK SOLVENT MODEL USED' _refine.ls_R_factor_all 0.206 _refine.ls_R_factor_obs 0.206 _refine.ls_R_factor_R_work 0.206 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.229 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.100 _refine.ls_number_reflns_R_free 3555 _refine.ls_R_factor_R_free_error 0.004 _refine.B_iso_mean 22.754 _refine.solvent_model_param_bsol 58.545 _refine.solvent_model_param_ksol 0.450 _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.aniso_B[1][1] 4.590 _refine.aniso_B[2][2] 0.540 _refine.aniso_B[3][3] -5.130 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] 0.680 _refine.aniso_B[2][3] 0.000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT MODEL' _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set ? _refine.B_iso_max 77.91 _refine.B_iso_min 8.70 _refine.occupancy_max 1.00 _refine.occupancy_min 1.00 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _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_analyze.entry_id 3KTZ _refine_analyze.Luzzati_coordinate_error_obs 0.200 _refine_analyze.Luzzati_sigma_a_obs 0.190 _refine_analyze.Luzzati_d_res_low_obs 5.000 _refine_analyze.Luzzati_coordinate_error_free 0.220 _refine_analyze.Luzzati_sigma_a_free 0.160 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3976 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 28 _refine_hist.number_atoms_solvent 199 _refine_hist.number_atoms_total 4203 _refine_hist.d_res_high 1.600 _refine_hist.d_res_low 47.350 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d ? 0.006 ? ? 'X-RAY DIFFRACTION' ? c_angle_deg ? 1.300 ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d ? 22.600 ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d ? 0.850 ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it ? 1.210 1.500 ? 'X-RAY DIFFRACTION' ? c_mcangle_it ? 2.020 2.000 ? 'X-RAY DIFFRACTION' ? c_scbond_it ? 2.340 2.000 ? 'X-RAY DIFFRACTION' ? c_scangle_it ? 3.470 2.500 ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.d_res_high 1.600 _refine_ls_shell.d_res_low 1.700 _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.percent_reflns_obs 72.000 _refine_ls_shell.number_reflns_R_work 8607 _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_R_work 0.301 _refine_ls_shell.R_factor_R_free 0.285 _refine_ls_shell.percent_reflns_R_free 5.100 _refine_ls_shell.number_reflns_R_free 466 _refine_ls_shell.R_factor_R_free_error 0.013 _refine_ls_shell.number_reflns_all 9073 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 2 dna-rna_rep.param dna-rna.top 'X-RAY DIFFRACTION' 3 water_rep.param water.top 'X-RAY DIFFRACTION' 4 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' # _struct.entry_id 3KTZ _struct.title 'Structure of GAP31' _struct.pdbx_descriptor 'Gelonium anti-HIV protein, 31 kDa, isolated from seeds of Gelonium multiflorum (E.C.3.2.2.22)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3KTZ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Plant seeds, glycosidase, Disulfide bond, Glycoprotein, Hydrolase, Plant defense, Protein synthesis inhibitor, Toxin' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? # _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 THR A 13 ? LEU A 28 ? THR A 13 LEU A 28 1 ? 16 HELX_P HELX_P2 2 PRO A 91 ? LEU A 98 ? PRO A 91 LEU A 98 1 ? 8 HELX_P HELX_P3 3 SER A 112 ? GLY A 118 ? SER A 112 GLY A 118 1 ? 7 HELX_P HELX_P4 4 TYR A 122 ? THR A 126 ? TYR A 122 THR A 126 5 ? 5 HELX_P HELX_P5 5 GLY A 129 ? ASN A 143 ? GLY A 129 ASN A 143 1 ? 15 HELX_P HELX_P6 6 LYS A 149 ? VAL A 164 ? LYS A 149 VAL A 164 1 ? 16 HELX_P HELX_P7 7 VAL A 164 ? PHE A 170 ? VAL A 164 PHE A 170 1 ? 7 HELX_P HELX_P8 8 PHE A 170 ? ASN A 179 ? PHE A 170 ASN A 179 1 ? 10 HELX_P HELX_P9 9 ALA A 188 ? THR A 207 ? ALA A 188 THR A 207 1 ? 20 HELX_P HELX_P10 10 VAL A 233 ? LYS A 237 ? VAL A 233 LYS A 237 1 ? 5 HELX_P HELX_P11 11 PRO A 238 ? ILE A 240 ? PRO A 238 ILE A 240 5 ? 3 HELX_P HELX_P12 12 THR B 13 ? LEU B 28 ? THR B 13 LEU B 28 1 ? 16 HELX_P HELX_P13 13 PRO B 91 ? LEU B 98 ? PRO B 91 LEU B 98 1 ? 8 HELX_P HELX_P14 14 SER B 112 ? GLY B 118 ? SER B 112 GLY B 118 1 ? 7 HELX_P HELX_P15 15 TYR B 122 ? THR B 126 ? TYR B 122 THR B 126 5 ? 5 HELX_P HELX_P16 16 GLY B 129 ? ASN B 143 ? GLY B 129 ASN B 143 1 ? 15 HELX_P HELX_P17 17 LYS B 149 ? VAL B 164 ? LYS B 149 VAL B 164 1 ? 16 HELX_P HELX_P18 18 VAL B 164 ? PHE B 170 ? VAL B 164 PHE B 170 1 ? 7 HELX_P HELX_P19 19 PHE B 170 ? ASN B 179 ? PHE B 170 ASN B 179 1 ? 10 HELX_P HELX_P20 20 ALA B 188 ? LYS B 197 ? ALA B 188 LYS B 197 1 ? 10 HELX_P HELX_P21 21 LYS B 197 ? SER B 208 ? LYS B 197 SER B 208 1 ? 12 HELX_P HELX_P22 22 VAL B 233 ? LYS B 237 ? VAL B 233 LYS B 237 1 ? 5 HELX_P HELX_P23 23 PRO B 238 ? ILE B 240 ? PRO B 238 ILE B 240 5 ? 3 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 44 SG ? ? ? 1_555 A CYS 50 SG ? ? A CYS 44 A CYS 50 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? B CYS 44 SG ? ? ? 1_555 B CYS 50 SG ? ? B CYS 44 B CYS 50 1_555 ? ? ? ? ? ? ? 2.032 ? covale1 covale ? ? B ASN 189 ND2 ? ? ? 1_555 D NAG . C1 ? ? B ASN 189 B NAG 411 1_555 ? ? ? ? ? ? ? 1.454 ? covale2 covale ? ? A ASN 189 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 189 A NAG 410 1_555 ? ? ? ? ? ? ? 1.457 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 2 ? C ? 2 ? D ? 6 ? E ? 2 ? F ? 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 D 1 2 ? parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? parallel E 1 2 ? anti-parallel F 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 ASP A 3 ? SER A 8 ? ASP A 3 SER A 8 A 2 PHE A 51 ? SER A 57 ? PHE A 51 SER A 57 A 3 LEU A 63 ? ASP A 69 ? LEU A 63 ASP A 69 A 4 VAL A 75 ? VAL A 80 ? VAL A 75 VAL A 80 A 5 ARG A 83 ? PHE A 86 ? ARG A 83 PHE A 86 A 6 ILE A 103 ? ARG A 106 ? ILE A 103 ARG A 106 B 1 ASN A 33 ? SER A 34 ? ASN A 33 SER A 34 B 2 ILE A 37 ? PRO A 38 ? ILE A 37 PRO A 38 C 1 MET A 213 ? GLU A 221 ? MET A 213 GLU A 221 C 2 LYS A 227 ? ALA A 232 ? LYS A 227 ALA A 232 D 1 ASP B 3 ? SER B 8 ? ASP B 3 SER B 8 D 2 PHE B 51 ? SER B 57 ? PHE B 51 SER B 57 D 3 LEU B 63 ? ASP B 69 ? LEU B 63 ASP B 69 D 4 VAL B 75 ? VAL B 80 ? VAL B 75 VAL B 80 D 5 ARG B 83 ? PHE B 86 ? ARG B 83 PHE B 86 D 6 ILE B 103 ? ARG B 106 ? ILE B 103 ARG B 106 E 1 ASN B 33 ? SER B 34 ? ASN B 33 SER B 34 E 2 ILE B 37 ? PRO B 38 ? ILE B 37 PRO B 38 F 1 MET B 213 ? GLU B 221 ? MET B 213 GLU B 221 F 2 LYS B 227 ? ALA B 232 ? LYS B 227 ALA B 232 # 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 5 ? N VAL A 5 O LEU A 53 ? O LEU A 53 A 2 3 N LEU A 56 ? N LEU A 56 O ALA A 64 ? O ALA A 64 A 3 4 N ALA A 67 ? N ALA A 67 O GLY A 77 ? O GLY A 77 A 4 5 N VAL A 80 ? N VAL A 80 O ARG A 83 ? O ARG A 83 A 5 6 N SER A 84 ? N SER A 84 O ILE A 103 ? O ILE A 103 B 1 2 N SER A 34 ? N SER A 34 O ILE A 37 ? O ILE A 37 C 1 2 N PHE A 214 ? N PHE A 214 O THR A 231 ? O THR A 231 D 1 2 N VAL B 5 ? N VAL B 5 O LEU B 53 ? O LEU B 53 D 2 3 N VAL B 54 ? N VAL B 54 O ILE B 66 ? O ILE B 66 D 3 4 N GLU B 65 ? N GLU B 65 O GLN B 79 ? O GLN B 79 D 4 5 N TYR B 78 ? N TYR B 78 O TYR B 85 ? O TYR B 85 D 5 6 N PHE B 86 ? N PHE B 86 O THR B 105 ? O THR B 105 E 1 2 N SER B 34 ? N SER B 34 O ILE B 37 ? O ILE B 37 F 1 2 N VAL B 218 ? N VAL B 218 O VAL B 230 ? O VAL B 230 # 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 410' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 411' # 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 PRO A 187 ? PRO A 187 . ? 1_555 ? 2 AC1 5 ALA A 188 ? ALA A 188 . ? 1_555 ? 3 AC1 5 ASN A 189 ? ASN A 189 . ? 1_555 ? 4 AC1 5 ALA A 223 ? ALA A 223 . ? 1_555 ? 5 AC1 5 ASN A 224 ? ASN A 224 . ? 1_555 ? 6 AC2 4 GLU B 124 ? GLU B 124 . ? 1_555 ? 7 AC2 4 ALA B 188 ? ALA B 188 . ? 1_555 ? 8 AC2 4 ASN B 189 ? ASN B 189 . ? 1_555 ? 9 AC2 4 ASN B 224 ? ASN B 224 . ? 1_555 ? # _database_PDB_matrix.entry_id 3KTZ _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] 0.000000 _database_PDB_matrix.origx_vector[2] 0.000000 _database_PDB_matrix.origx_vector[3] 0.000000 # _atom_sites.entry_id 3KTZ _atom_sites.fract_transf_matrix[1][1] 0.020673 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.003047 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.022525 _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] 0.007364 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # 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 . GLY A 1 1 ? 6.889 -18.065 50.067 1.00 42.34 ? 1 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 6.832 -17.943 48.571 1.00 42.82 ? 1 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 7.230 -16.550 48.137 1.00 41.89 ? 1 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 6.478 -15.846 47.453 1.00 43.79 ? 1 GLY A O 1 ATOM 5 N N . LEU A 1 2 ? 8.434 -16.160 48.533 1.00 38.66 ? 2 LEU A N 1 ATOM 6 C CA . LEU A 1 2 ? 8.948 -14.835 48.237 1.00 35.21 ? 2 LEU A CA 1 ATOM 7 C C . LEU A 1 2 ? 9.925 -14.822 47.069 1.00 32.90 ? 2 LEU A C 1 ATOM 8 O O . LEU A 1 2 ? 10.555 -15.837 46.757 1.00 32.94 ? 2 LEU A O 1 ATOM 9 C CB . LEU A 1 2 ? 9.657 -14.288 49.479 1.00 33.86 ? 2 LEU A CB 1 ATOM 10 C CG . LEU A 1 2 ? 8.936 -14.504 50.810 1.00 31.43 ? 2 LEU A CG 1 ATOM 11 C CD1 . LEU A 1 2 ? 9.896 -14.211 51.947 1.00 32.25 ? 2 LEU A CD1 1 ATOM 12 C CD2 . LEU A 1 2 ? 7.700 -13.620 50.886 1.00 29.09 ? 2 LEU A CD2 1 ATOM 13 N N . ASP A 1 3 ? 10.040 -13.668 46.418 1.00 29.24 ? 3 ASP A N 1 ATOM 14 C CA . ASP A 1 3 ? 10.989 -13.515 45.327 1.00 25.13 ? 3 ASP A CA 1 ATOM 15 C C . ASP A 1 3 ? 12.321 -13.297 46.028 1.00 22.89 ? 3 ASP A C 1 ATOM 16 O O . ASP A 1 3 ? 12.358 -12.857 47.184 1.00 20.26 ? 3 ASP A O 1 ATOM 17 C CB . ASP A 1 3 ? 10.654 -12.294 44.471 1.00 27.59 ? 3 ASP A CB 1 ATOM 18 C CG . ASP A 1 3 ? 9.784 -12.637 43.279 1.00 30.13 ? 3 ASP A CG 1 ATOM 19 O OD1 . ASP A 1 3 ? 10.241 -13.431 42.428 1.00 30.59 ? 3 ASP A OD1 1 ATOM 20 O OD2 . ASP A 1 3 ? 8.649 -12.115 43.191 1.00 30.24 ? 3 ASP A OD2 1 ATOM 21 N N . THR A 1 4 ? 13.412 -13.612 45.347 1.00 19.53 ? 4 THR A N 1 ATOM 22 C CA . THR A 1 4 ? 14.720 -13.434 45.947 1.00 19.62 ? 4 THR A CA 1 ATOM 23 C C . THR A 1 4 ? 15.675 -12.805 44.945 1.00 18.55 ? 4 THR A C 1 ATOM 24 O O . THR A 1 4 ? 15.553 -13.010 43.740 1.00 18.67 ? 4 THR A O 1 ATOM 25 C CB . THR A 1 4 ? 15.301 -14.784 46.444 1.00 20.49 ? 4 THR A CB 1 ATOM 26 O OG1 . THR A 1 4 ? 15.457 -15.674 45.335 1.00 23.29 ? 4 THR A OG1 1 ATOM 27 C CG2 . THR A 1 4 ? 14.365 -15.432 47.466 1.00 20.27 ? 4 THR A CG2 1 ATOM 28 N N . VAL A 1 5 ? 16.617 -12.022 45.451 1.00 17.40 ? 5 VAL A N 1 ATOM 29 C CA . VAL A 1 5 ? 17.596 -11.362 44.604 1.00 17.69 ? 5 VAL A CA 1 ATOM 30 C C . VAL A 1 5 ? 18.948 -11.480 45.301 1.00 17.25 ? 5 VAL A C 1 ATOM 31 O O . VAL A 1 5 ? 19.039 -11.291 46.512 1.00 17.40 ? 5 VAL A O 1 ATOM 32 C CB . VAL A 1 5 ? 17.267 -9.858 44.418 1.00 18.92 ? 5 VAL A CB 1 ATOM 33 C CG1 . VAL A 1 5 ? 18.135 -9.277 43.304 1.00 21.42 ? 5 VAL A CG1 1 ATOM 34 C CG2 . VAL A 1 5 ? 15.797 -9.671 44.112 1.00 20.41 ? 5 VAL A CG2 1 ATOM 35 N N . SER A 1 6 ? 19.994 -11.788 44.548 1.00 15.97 ? 6 SER A N 1 ATOM 36 C CA . SER A 1 6 ? 21.308 -11.925 45.148 1.00 16.71 ? 6 SER A CA 1 ATOM 37 C C . SER A 1 6 ? 22.284 -10.860 44.703 1.00 16.82 ? 6 SER A C 1 ATOM 38 O O . SER A 1 6 ? 22.189 -10.335 43.595 1.00 17.47 ? 6 SER A O 1 ATOM 39 C CB . SER A 1 6 ? 21.922 -13.286 44.801 1.00 18.92 ? 6 SER A CB 1 ATOM 40 O OG . SER A 1 6 ? 21.129 -14.355 45.279 1.00 23.91 ? 6 SER A OG 1 ATOM 41 N N . PHE A 1 7 ? 23.214 -10.531 45.587 1.00 14.88 ? 7 PHE A N 1 ATOM 42 C CA . PHE A 1 7 ? 24.270 -9.605 45.245 1.00 14.91 ? 7 PHE A CA 1 ATOM 43 C C . PHE A 1 7 ? 25.517 -10.036 45.990 1.00 14.97 ? 7 PHE A C 1 ATOM 44 O O . PHE A 1 7 ? 25.543 -10.059 47.221 1.00 14.20 ? 7 PHE A O 1 ATOM 45 C CB . PHE A 1 7 ? 23.965 -8.155 45.608 1.00 14.35 ? 7 PHE A CB 1 ATOM 46 C CG . PHE A 1 7 ? 25.078 -7.214 45.208 1.00 14.68 ? 7 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 7 ? 25.424 -7.067 43.865 1.00 13.94 ? 7 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 7 ? 25.825 -6.536 46.164 1.00 14.80 ? 7 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 7 ? 26.491 -6.265 43.483 1.00 13.18 ? 7 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 7 ? 26.902 -5.727 45.790 1.00 14.39 ? 7 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 7 ? 27.233 -5.594 44.447 1.00 14.10 ? 7 PHE A CZ 1 ATOM 52 N N . SER A 1 8 ? 26.545 -10.393 45.236 1.00 15.54 ? 8 SER A N 1 ATOM 53 C CA . SER A 1 8 ? 27.803 -10.820 45.825 1.00 16.50 ? 8 SER A CA 1 ATOM 54 C C . SER A 1 8 ? 28.824 -9.711 45.642 1.00 16.09 ? 8 SER A C 1 ATOM 55 O O . SER A 1 8 ? 28.881 -9.086 44.588 1.00 17.26 ? 8 SER A O 1 ATOM 56 C CB . SER A 1 8 ? 28.298 -12.102 45.146 1.00 18.46 ? 8 SER A CB 1 ATOM 57 O OG . SER A 1 8 ? 29.574 -12.481 45.637 1.00 21.29 ? 8 SER A OG 1 ATOM 58 N N . THR A 1 9 ? 29.623 -9.459 46.670 1.00 16.68 ? 9 THR A N 1 ATOM 59 C CA . THR A 1 9 ? 30.633 -8.421 46.588 1.00 18.34 ? 9 THR A CA 1 ATOM 60 C C . THR A 1 9 ? 31.893 -8.948 45.898 1.00 20.15 ? 9 THR A C 1 ATOM 61 O O . THR A 1 9 ? 32.735 -8.166 45.449 1.00 19.70 ? 9 THR A O 1 ATOM 62 C CB . THR A 1 9 ? 31.019 -7.902 47.988 1.00 19.84 ? 9 THR A CB 1 ATOM 63 O OG1 . THR A 1 9 ? 31.569 -8.978 48.757 1.00 19.53 ? 9 THR A OG1 1 ATOM 64 C CG2 . THR A 1 9 ? 29.801 -7.331 48.706 1.00 18.46 ? 9 THR A CG2 1 ATOM 65 N N . LYS A 1 10 ? 32.025 -10.269 45.807 1.00 20.47 ? 10 LYS A N 1 ATOM 66 C CA . LYS A 1 10 ? 33.204 -10.848 45.174 1.00 22.38 ? 10 LYS A CA 1 ATOM 67 C C . LYS A 1 10 ? 33.202 -10.581 43.671 1.00 21.46 ? 10 LYS A C 1 ATOM 68 O O . LYS A 1 10 ? 32.326 -11.053 42.947 1.00 21.45 ? 10 LYS A O 1 ATOM 69 C CB . LYS A 1 10 ? 33.272 -12.358 45.418 1.00 25.71 ? 10 LYS A CB 1 ATOM 70 C CG . LYS A 1 10 ? 34.637 -12.944 45.060 1.00 30.78 ? 10 LYS A CG 1 ATOM 71 C CD . LYS A 1 10 ? 34.576 -14.426 44.714 1.00 36.40 ? 10 LYS A CD 1 ATOM 72 C CE . LYS A 1 10 ? 34.150 -15.286 45.895 1.00 40.17 ? 10 LYS A CE 1 ATOM 73 N NZ . LYS A 1 10 ? 34.254 -16.742 45.561 1.00 43.31 ? 10 LYS A NZ 1 ATOM 74 N N . GLY A 1 11 ? 34.191 -9.827 43.205 1.00 20.99 ? 11 GLY A N 1 ATOM 75 C CA . GLY A 1 11 ? 34.268 -9.513 41.791 1.00 19.93 ? 11 GLY A CA 1 ATOM 76 C C . GLY A 1 11 ? 33.159 -8.567 41.373 1.00 19.69 ? 11 GLY A C 1 ATOM 77 O O . GLY A 1 11 ? 32.875 -8.414 40.185 1.00 19.32 ? 11 GLY A O 1 ATOM 78 N N . ALA A 1 12 ? 32.525 -7.931 42.355 1.00 18.41 ? 12 ALA A N 1 ATOM 79 C CA . ALA A 1 12 ? 31.440 -6.996 42.082 1.00 16.50 ? 12 ALA A CA 1 ATOM 80 C C . ALA A 1 12 ? 31.958 -5.775 41.334 1.00 15.82 ? 12 ALA A C 1 ATOM 81 O O . ALA A 1 12 ? 33.097 -5.364 41.526 1.00 16.26 ? 12 ALA A O 1 ATOM 82 C CB . ALA A 1 12 ? 30.785 -6.562 43.386 1.00 15.26 ? 12 ALA A CB 1 ATOM 83 N N . THR A 1 13 ? 31.117 -5.206 40.475 1.00 17.25 ? 13 THR A N 1 ATOM 84 C CA . THR A 1 13 ? 31.473 -4.013 39.709 1.00 15.64 ? 13 THR A CA 1 ATOM 85 C C . THR A 1 13 ? 30.280 -3.075 39.725 1.00 15.80 ? 13 THR A C 1 ATOM 86 O O . THR A 1 13 ? 29.177 -3.470 40.111 1.00 14.80 ? 13 THR A O 1 ATOM 87 C CB . THR A 1 13 ? 31.780 -4.341 38.242 1.00 16.41 ? 13 THR A CB 1 ATOM 88 O OG1 . THR A 1 13 ? 30.567 -4.716 37.580 1.00 16.50 ? 13 THR A OG1 1 ATOM 89 C CG2 . THR A 1 13 ? 32.787 -5.484 38.145 1.00 15.79 ? 13 THR A CG2 1 ATOM 90 N N . TYR A 1 14 ? 30.491 -1.837 39.292 1.00 15.16 ? 14 TYR A N 1 ATOM 91 C CA . TYR A 1 14 ? 29.410 -0.866 39.265 1.00 15.67 ? 14 TYR A CA 1 ATOM 92 C C . TYR A 1 14 ? 28.256 -1.407 38.426 1.00 15.79 ? 14 TYR A C 1 ATOM 93 O O . TYR A 1 14 ? 27.096 -1.076 38.675 1.00 15.66 ? 14 TYR A O 1 ATOM 94 C CB . TYR A 1 14 ? 29.910 0.462 38.696 1.00 16.03 ? 14 TYR A CB 1 ATOM 95 C CG . TYR A 1 14 ? 30.358 0.382 37.255 1.00 18.28 ? 14 TYR A CG 1 ATOM 96 C CD1 . TYR A 1 14 ? 29.512 0.776 36.215 1.00 19.95 ? 14 TYR A CD1 1 ATOM 97 C CD2 . TYR A 1 14 ? 31.631 -0.079 36.932 1.00 19.29 ? 14 TYR A CD2 1 ATOM 98 C CE1 . TYR A 1 14 ? 29.933 0.715 34.886 1.00 21.30 ? 14 TYR A CE1 1 ATOM 99 C CE2 . TYR A 1 14 ? 32.058 -0.145 35.612 1.00 21.09 ? 14 TYR A CE2 1 ATOM 100 C CZ . TYR A 1 14 ? 31.207 0.253 34.598 1.00 20.94 ? 14 TYR A CZ 1 ATOM 101 O OH . TYR A 1 14 ? 31.640 0.186 33.297 1.00 24.58 ? 14 TYR A OH 1 ATOM 102 N N . ILE A 1 15 ? 28.581 -2.246 37.439 1.00 15.34 ? 15 ILE A N 1 ATOM 103 C CA . ILE A 1 15 ? 27.578 -2.853 36.567 1.00 15.70 ? 15 ILE A CA 1 ATOM 104 C C . ILE A 1 15 ? 26.790 -3.967 37.276 1.00 15.69 ? 15 ILE A C 1 ATOM 105 O O . ILE A 1 15 ? 25.561 -4.036 37.156 1.00 15.41 ? 15 ILE A O 1 ATOM 106 C CB . ILE A 1 15 ? 28.235 -3.425 35.279 1.00 18.48 ? 15 ILE A CB 1 ATOM 107 C CG1 . ILE A 1 15 ? 28.645 -2.282 34.349 1.00 18.30 ? 15 ILE A CG1 1 ATOM 108 C CG2 . ILE A 1 15 ? 27.262 -4.347 34.550 1.00 20.00 ? 15 ILE A CG2 1 ATOM 109 C CD1 . ILE A 1 15 ? 27.463 -1.520 33.743 1.00 20.26 ? 15 ILE A CD1 1 ATOM 110 N N . THR A 1 16 ? 27.470 -4.843 38.013 1.00 14.42 ? 16 THR A N 1 ATOM 111 C CA . THR A 1 16 ? 26.736 -5.899 38.702 1.00 16.16 ? 16 THR A CA 1 ATOM 112 C C . THR A 1 16 ? 25.794 -5.268 39.741 1.00 16.36 ? 16 THR A C 1 ATOM 113 O O . THR A 1 16 ? 24.685 -5.755 39.967 1.00 16.47 ? 16 THR A O 1 ATOM 114 C CB . THR A 1 16 ? 27.685 -6.935 39.398 1.00 18.06 ? 16 THR A CB 1 ATOM 115 O OG1 . THR A 1 16 ? 28.445 -6.295 40.431 1.00 19.77 ? 16 THR A OG1 1 ATOM 116 C CG2 . THR A 1 16 ? 28.639 -7.566 38.374 1.00 17.64 ? 16 THR A CG2 1 ATOM 117 N N . TYR A 1 17 ? 26.235 -4.170 40.352 1.00 15.44 ? 17 TYR A N 1 ATOM 118 C CA . TYR A 1 17 ? 25.437 -3.460 41.353 1.00 12.97 ? 17 TYR A CA 1 ATOM 119 C C . TYR A 1 17 ? 24.180 -2.853 40.725 1.00 13.16 ? 17 TYR A C 1 ATOM 120 O O . TYR A 1 17 ? 23.079 -3.000 41.255 1.00 12.50 ? 17 TYR A O 1 ATOM 121 C CB . TYR A 1 17 ? 26.274 -2.348 41.993 1.00 13.11 ? 17 TYR A CB 1 ATOM 122 C CG . TYR A 1 17 ? 25.511 -1.470 42.958 1.00 11.04 ? 17 TYR A CG 1 ATOM 123 C CD1 . TYR A 1 17 ? 25.022 -1.978 44.161 1.00 11.20 ? 17 TYR A CD1 1 ATOM 124 C CD2 . TYR A 1 17 ? 25.285 -0.123 42.670 1.00 11.18 ? 17 TYR A CD2 1 ATOM 125 C CE1 . TYR A 1 17 ? 24.324 -1.159 45.059 1.00 11.31 ? 17 TYR A CE1 1 ATOM 126 C CE2 . TYR A 1 17 ? 24.589 0.705 43.557 1.00 11.11 ? 17 TYR A CE2 1 ATOM 127 C CZ . TYR A 1 17 ? 24.113 0.183 44.748 1.00 12.33 ? 17 TYR A CZ 1 ATOM 128 O OH . TYR A 1 17 ? 23.431 1.002 45.625 1.00 11.02 ? 17 TYR A OH 1 ATOM 129 N N . VAL A 1 18 ? 24.340 -2.166 39.599 1.00 12.11 ? 18 VAL A N 1 ATOM 130 C CA . VAL A 1 18 ? 23.196 -1.559 38.921 1.00 12.28 ? 18 VAL A CA 1 ATOM 131 C C . VAL A 1 18 ? 22.205 -2.615 38.424 1.00 12.81 ? 18 VAL A C 1 ATOM 132 O O . VAL A 1 18 ? 20.984 -2.449 38.551 1.00 12.58 ? 18 VAL A O 1 ATOM 133 C CB . VAL A 1 18 ? 23.666 -0.666 37.747 1.00 12.22 ? 18 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 18 ? 22.484 -0.263 36.863 1.00 14.51 ? 18 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 18 ? 24.355 0.569 38.311 1.00 11.32 ? 18 VAL A CG2 1 ATOM 136 N N . ASN A 1 19 ? 22.717 -3.707 37.869 1.00 13.30 ? 19 ASN A N 1 ATOM 137 C CA . ASN A 1 19 ? 21.836 -4.766 37.392 1.00 13.43 ? 19 ASN A CA 1 ATOM 138 C C . ASN A 1 19 ? 21.065 -5.364 38.567 1.00 12.94 ? 19 ASN A C 1 ATOM 139 O O . ASN A 1 19 ? 19.889 -5.714 38.434 1.00 13.42 ? 19 ASN A O 1 ATOM 140 C CB . ASN A 1 19 ? 22.650 -5.836 36.667 1.00 15.07 ? 19 ASN A CB 1 ATOM 141 C CG . ASN A 1 19 ? 23.049 -5.408 35.265 1.00 17.22 ? 19 ASN A CG 1 ATOM 142 O OD1 . ASN A 1 19 ? 24.037 -5.894 34.715 1.00 21.89 ? 19 ASN A OD1 1 ATOM 143 N ND2 . ASN A 1 19 ? 22.275 -4.507 34.676 1.00 17.08 ? 19 ASN A ND2 1 ATOM 144 N N . PHE A 1 20 ? 21.731 -5.468 39.717 1.00 12.10 ? 20 PHE A N 1 ATOM 145 C CA . PHE A 1 20 ? 21.111 -5.988 40.938 1.00 12.16 ? 20 PHE A CA 1 ATOM 146 C C . PHE A 1 20 ? 19.934 -5.088 41.337 1.00 11.34 ? 20 PHE A C 1 ATOM 147 O O . PHE A 1 20 ? 18.828 -5.572 41.582 1.00 10.81 ? 20 PHE A O 1 ATOM 148 C CB . PHE A 1 20 ? 22.158 -6.054 42.068 1.00 13.17 ? 20 PHE A CB 1 ATOM 149 C CG . PHE A 1 20 ? 21.580 -5.931 43.454 1.00 14.78 ? 20 PHE A CG 1 ATOM 150 C CD1 . PHE A 1 20 ? 20.783 -6.937 43.988 1.00 16.05 ? 20 PHE A CD1 1 ATOM 151 C CD2 . PHE A 1 20 ? 21.821 -4.791 44.217 1.00 15.99 ? 20 PHE A CD2 1 ATOM 152 C CE1 . PHE A 1 20 ? 20.230 -6.810 45.265 1.00 15.84 ? 20 PHE A CE1 1 ATOM 153 C CE2 . PHE A 1 20 ? 21.273 -4.655 45.490 1.00 16.81 ? 20 PHE A CE2 1 ATOM 154 C CZ . PHE A 1 20 ? 20.475 -5.669 46.015 1.00 16.48 ? 20 PHE A CZ 1 ATOM 155 N N . LEU A 1 21 ? 20.166 -3.777 41.390 1.00 11.30 ? 21 LEU A N 1 ATOM 156 C CA . LEU A 1 21 ? 19.102 -2.844 41.751 1.00 11.02 ? 21 LEU A CA 1 ATOM 157 C C . LEU A 1 21 ? 17.907 -2.944 40.810 1.00 10.39 ? 21 LEU A C 1 ATOM 158 O O . LEU A 1 21 ? 16.761 -2.895 41.250 1.00 10.87 ? 21 LEU A O 1 ATOM 159 C CB . LEU A 1 21 ? 19.617 -1.402 41.754 1.00 10.64 ? 21 LEU A CB 1 ATOM 160 C CG . LEU A 1 21 ? 20.624 -1.014 42.835 1.00 11.43 ? 21 LEU A CG 1 ATOM 161 C CD1 . LEU A 1 21 ? 21.038 0.442 42.611 1.00 12.06 ? 21 LEU A CD1 1 ATOM 162 C CD2 . LEU A 1 21 ? 20.018 -1.207 44.230 1.00 10.81 ? 21 LEU A CD2 1 ATOM 163 N N . ASN A 1 22 ? 18.162 -3.083 39.513 1.00 11.86 ? 22 ASN A N 1 ATOM 164 C CA . ASN A 1 22 ? 17.057 -3.177 38.571 1.00 13.38 ? 22 ASN A CA 1 ATOM 165 C C . ASN A 1 22 ? 16.301 -4.498 38.688 1.00 14.19 ? 22 ASN A C 1 ATOM 166 O O . ASN A 1 22 ? 15.110 -4.571 38.385 1.00 14.11 ? 22 ASN A O 1 ATOM 167 C CB . ASN A 1 22 ? 17.555 -2.917 37.147 1.00 13.54 ? 22 ASN A CB 1 ATOM 168 C CG . ASN A 1 22 ? 17.770 -1.433 36.887 1.00 15.49 ? 22 ASN A CG 1 ATOM 169 O OD1 . ASN A 1 22 ? 16.913 -0.612 37.235 1.00 14.43 ? 22 ASN A OD1 1 ATOM 170 N ND2 . ASN A 1 22 ? 18.904 -1.079 36.287 1.00 15.10 ? 22 ASN A ND2 1 ATOM 171 N N . GLU A 1 23 ? 16.988 -5.537 39.147 1.00 15.05 ? 23 GLU A N 1 ATOM 172 C CA . GLU A 1 23 ? 16.331 -6.820 39.347 1.00 15.72 ? 23 GLU A CA 1 ATOM 173 C C . GLU A 1 23 ? 15.426 -6.666 40.576 1.00 13.74 ? 23 GLU A C 1 ATOM 174 O O . GLU A 1 23 ? 14.293 -7.135 40.596 1.00 15.22 ? 23 GLU A O 1 ATOM 175 C CB . GLU A 1 23 ? 17.365 -7.914 39.603 1.00 18.73 ? 23 GLU A CB 1 ATOM 176 C CG . GLU A 1 23 ? 16.762 -9.299 39.650 1.00 24.24 ? 23 GLU A CG 1 ATOM 177 C CD . GLU A 1 23 ? 17.792 -10.368 39.925 1.00 29.80 ? 23 GLU A CD 1 ATOM 178 O OE1 . GLU A 1 23 ? 18.930 -10.243 39.416 1.00 33.62 ? 23 GLU A OE1 1 ATOM 179 O OE2 . GLU A 1 23 ? 17.463 -11.340 40.641 1.00 33.60 ? 23 GLU A OE2 1 ATOM 180 N N . LEU A 1 24 ? 15.938 -6.000 41.601 1.00 12.11 ? 24 LEU A N 1 ATOM 181 C CA . LEU A 1 24 ? 15.171 -5.775 42.817 1.00 11.50 ? 24 LEU A CA 1 ATOM 182 C C . LEU A 1 24 ? 13.938 -4.919 42.516 1.00 12.70 ? 24 LEU A C 1 ATOM 183 O O . LEU A 1 24 ? 12.830 -5.216 42.976 1.00 12.98 ? 24 LEU A O 1 ATOM 184 C CB . LEU A 1 24 ? 16.050 -5.085 43.865 1.00 12.39 ? 24 LEU A CB 1 ATOM 185 C CG . LEU A 1 24 ? 15.372 -4.583 45.146 1.00 13.17 ? 24 LEU A CG 1 ATOM 186 C CD1 . LEU A 1 24 ? 14.603 -5.714 45.831 1.00 13.13 ? 24 LEU A CD1 1 ATOM 187 C CD2 . LEU A 1 24 ? 16.436 -4.004 46.069 1.00 12.34 ? 24 LEU A CD2 1 ATOM 188 N N . ARG A 1 25 ? 14.133 -3.854 41.741 1.00 11.66 ? 25 ARG A N 1 ATOM 189 C CA . ARG A 1 25 ? 13.039 -2.958 41.382 1.00 12.32 ? 25 ARG A CA 1 ATOM 190 C C . ARG A 1 25 ? 11.907 -3.715 40.694 1.00 12.56 ? 25 ARG A C 1 ATOM 191 O O . ARG A 1 25 ? 10.731 -3.406 40.890 1.00 14.49 ? 25 ARG A O 1 ATOM 192 C CB . ARG A 1 25 ? 13.568 -1.840 40.479 1.00 11.84 ? 25 ARG A CB 1 ATOM 193 C CG . ARG A 1 25 ? 14.419 -0.833 41.235 1.00 12.19 ? 25 ARG A CG 1 ATOM 194 C CD . ARG A 1 25 ? 15.281 0.001 40.303 1.00 12.85 ? 25 ARG A CD 1 ATOM 195 N NE . ARG A 1 25 ? 15.949 1.088 41.018 1.00 11.81 ? 25 ARG A NE 1 ATOM 196 C CZ . ARG A 1 25 ? 16.917 1.838 40.499 1.00 11.80 ? 25 ARG A CZ 1 ATOM 197 N NH1 . ARG A 1 25 ? 17.335 1.612 39.257 1.00 8.70 ? 25 ARG A NH1 1 ATOM 198 N NH2 . ARG A 1 25 ? 17.457 2.820 41.215 1.00 9.84 ? 25 ARG A NH2 1 ATOM 199 N N . VAL A 1 26 ? 12.268 -4.714 39.893 1.00 13.78 ? 26 VAL A N 1 ATOM 200 C CA . VAL A 1 26 ? 11.281 -5.525 39.195 1.00 15.08 ? 26 VAL A CA 1 ATOM 201 C C . VAL A 1 26 ? 10.560 -6.469 40.159 1.00 15.03 ? 26 VAL A C 1 ATOM 202 O O . VAL A 1 26 ? 9.330 -6.572 40.145 1.00 15.33 ? 26 VAL A O 1 ATOM 203 C CB . VAL A 1 26 ? 11.939 -6.367 38.079 1.00 14.77 ? 26 VAL A CB 1 ATOM 204 C CG1 . VAL A 1 26 ? 10.950 -7.383 37.540 1.00 16.43 ? 26 VAL A CG1 1 ATOM 205 C CG2 . VAL A 1 26 ? 12.399 -5.460 36.956 1.00 16.10 ? 26 VAL A CG2 1 ATOM 206 N N . LYS A 1 27 ? 11.325 -7.147 41.008 1.00 15.90 ? 27 LYS A N 1 ATOM 207 C CA . LYS A 1 27 ? 10.737 -8.097 41.949 1.00 16.13 ? 27 LYS A CA 1 ATOM 208 C C . LYS A 1 27 ? 9.876 -7.487 43.047 1.00 15.96 ? 27 LYS A C 1 ATOM 209 O O . LYS A 1 27 ? 9.099 -8.186 43.700 1.00 16.18 ? 27 LYS A O 1 ATOM 210 C CB . LYS A 1 27 ? 11.839 -8.993 42.517 1.00 15.47 ? 27 LYS A CB 1 ATOM 211 C CG . LYS A 1 27 ? 12.375 -9.898 41.417 1.00 16.88 ? 27 LYS A CG 1 ATOM 212 C CD . LYS A 1 27 ? 13.414 -10.880 41.857 1.00 18.89 ? 27 LYS A CD 1 ATOM 213 C CE . LYS A 1 27 ? 13.768 -11.795 40.682 1.00 20.22 ? 27 LYS A CE 1 ATOM 214 N NZ . LYS A 1 27 ? 14.827 -12.773 41.033 1.00 19.84 ? 27 LYS A NZ 1 ATOM 215 N N . LEU A 1 28 ? 9.997 -6.179 43.245 1.00 15.83 ? 28 LEU A N 1 ATOM 216 C CA . LEU A 1 28 ? 9.170 -5.501 44.232 1.00 15.12 ? 28 LEU A CA 1 ATOM 217 C C . LEU A 1 28 ? 7.753 -5.435 43.634 1.00 15.80 ? 28 LEU A C 1 ATOM 218 O O . LEU A 1 28 ? 6.774 -5.125 44.319 1.00 14.87 ? 28 LEU A O 1 ATOM 219 C CB . LEU A 1 28 ? 9.718 -4.092 44.497 1.00 13.75 ? 28 LEU A CB 1 ATOM 220 C CG . LEU A 1 28 ? 10.989 -4.003 45.348 1.00 12.25 ? 28 LEU A CG 1 ATOM 221 C CD1 . LEU A 1 28 ? 11.581 -2.602 45.242 1.00 13.09 ? 28 LEU A CD1 1 ATOM 222 C CD2 . LEU A 1 28 ? 10.668 -4.344 46.798 1.00 12.01 ? 28 LEU A CD2 1 ATOM 223 N N . LYS A 1 29 ? 7.674 -5.727 42.337 1.00 16.40 ? 29 LYS A N 1 ATOM 224 C CA . LYS A 1 29 ? 6.424 -5.733 41.584 1.00 17.03 ? 29 LYS A CA 1 ATOM 225 C C . LYS A 1 29 ? 5.498 -4.529 41.785 1.00 16.93 ? 29 LYS A C 1 ATOM 226 O O . LYS A 1 29 ? 4.389 -4.664 42.315 1.00 17.04 ? 29 LYS A O 1 ATOM 227 C CB . LYS A 1 29 ? 5.647 -7.018 41.877 1.00 19.55 ? 29 LYS A CB 1 ATOM 228 C CG . LYS A 1 29 ? 6.291 -8.287 41.343 1.00 23.15 ? 29 LYS A CG 1 ATOM 229 C CD . LYS A 1 29 ? 5.369 -9.476 41.579 1.00 27.98 ? 29 LYS A CD 1 ATOM 230 C CE . LYS A 1 29 ? 5.779 -10.706 40.777 1.00 31.82 ? 29 LYS A CE 1 ATOM 231 N NZ . LYS A 1 29 ? 6.960 -11.410 41.346 1.00 35.28 ? 29 LYS A NZ 1 ATOM 232 N N . PRO A 1 30 ? 5.943 -3.328 41.380 1.00 15.86 ? 30 PRO A N 1 ATOM 233 C CA . PRO A 1 30 ? 5.061 -2.171 41.553 1.00 16.63 ? 30 PRO A CA 1 ATOM 234 C C . PRO A 1 30 ? 3.833 -2.353 40.657 1.00 17.50 ? 30 PRO A C 1 ATOM 235 O O . PRO A 1 30 ? 3.870 -3.121 39.695 1.00 16.12 ? 30 PRO A O 1 ATOM 236 C CB . PRO A 1 30 ? 5.938 -0.994 41.121 1.00 15.23 ? 30 PRO A CB 1 ATOM 237 C CG . PRO A 1 30 ? 6.903 -1.612 40.151 1.00 15.62 ? 30 PRO A CG 1 ATOM 238 C CD . PRO A 1 30 ? 7.243 -2.926 40.815 1.00 15.83 ? 30 PRO A CD 1 ATOM 239 N N . GLU A 1 31 ? 2.744 -1.670 40.980 1.00 18.08 ? 31 GLU A N 1 ATOM 240 C CA . GLU A 1 31 ? 1.535 -1.781 40.172 1.00 21.72 ? 31 GLU A CA 1 ATOM 241 C C . GLU A 1 31 ? 1.122 -0.423 39.644 1.00 20.21 ? 31 GLU A C 1 ATOM 242 O O . GLU A 1 31 ? 0.779 0.480 40.411 1.00 20.70 ? 31 GLU A O 1 ATOM 243 C CB . GLU A 1 31 ? 0.395 -2.396 40.985 1.00 23.94 ? 31 GLU A CB 1 ATOM 244 C CG . GLU A 1 31 ? 0.557 -3.888 41.186 1.00 30.35 ? 31 GLU A CG 1 ATOM 245 C CD . GLU A 1 31 ? -0.535 -4.490 42.044 1.00 33.09 ? 31 GLU A CD 1 ATOM 246 O OE1 . GLU A 1 31 ? -0.488 -5.720 42.276 1.00 34.74 ? 31 GLU A OE1 1 ATOM 247 O OE2 . GLU A 1 31 ? -1.433 -3.738 42.487 1.00 35.34 ? 31 GLU A OE2 1 ATOM 248 N N . GLY A 1 32 ? 1.167 -0.279 38.326 1.00 20.33 ? 32 GLY A N 1 ATOM 249 C CA . GLY A 1 32 ? 0.799 0.985 37.725 1.00 19.15 ? 32 GLY A CA 1 ATOM 250 C C . GLY A 1 32 ? 1.938 1.972 37.855 1.00 19.49 ? 32 GLY A C 1 ATOM 251 O O . GLY A 1 32 ? 3.075 1.602 38.158 1.00 19.11 ? 32 GLY A O 1 ATOM 252 N N . ASN A 1 33 ? 1.627 3.242 37.651 1.00 18.86 ? 33 ASN A N 1 ATOM 253 C CA . ASN A 1 33 ? 2.642 4.273 37.714 1.00 18.58 ? 33 ASN A CA 1 ATOM 254 C C . ASN A 1 33 ? 1.958 5.603 37.927 1.00 18.87 ? 33 ASN A C 1 ATOM 255 O O . ASN A 1 33 ? 0.738 5.707 37.820 1.00 19.91 ? 33 ASN A O 1 ATOM 256 C CB . ASN A 1 33 ? 3.372 4.324 36.378 1.00 18.23 ? 33 ASN A CB 1 ATOM 257 C CG . ASN A 1 33 ? 2.467 4.823 35.248 1.00 19.68 ? 33 ASN A CG 1 ATOM 258 O OD1 . ASN A 1 33 ? 2.180 6.024 35.143 1.00 17.46 ? 33 ASN A OD1 1 ATOM 259 N ND2 . ASN A 1 33 ? 1.999 3.900 34.415 1.00 19.26 ? 33 ASN A ND2 1 ATOM 260 N N . SER A 1 34 ? 2.748 6.621 38.227 1.00 18.23 ? 34 SER A N 1 ATOM 261 C CA . SER A 1 34 ? 2.219 7.964 38.376 1.00 19.07 ? 34 SER A CA 1 ATOM 262 C C . SER A 1 34 ? 3.132 8.824 37.510 1.00 19.09 ? 34 SER A C 1 ATOM 263 O O . SER A 1 34 ? 4.328 8.932 37.780 1.00 18.44 ? 34 SER A O 1 ATOM 264 C CB . SER A 1 34 ? 2.272 8.425 39.833 1.00 19.75 ? 34 SER A CB 1 ATOM 265 O OG . SER A 1 34 ? 1.741 9.734 39.955 1.00 21.09 ? 34 SER A OG 1 ATOM 266 N N . HIS A 1 35 ? 2.577 9.407 36.451 1.00 18.94 ? 35 HIS A N 1 ATOM 267 C CA . HIS A 1 35 ? 3.362 10.243 35.550 1.00 18.53 ? 35 HIS A CA 1 ATOM 268 C C . HIS A 1 35 ? 4.516 9.467 34.925 1.00 17.50 ? 35 HIS A C 1 ATOM 269 O O . HIS A 1 35 ? 5.538 10.050 34.551 1.00 19.80 ? 35 HIS A O 1 ATOM 270 C CB . HIS A 1 35 ? 3.905 11.457 36.305 1.00 19.92 ? 35 HIS A CB 1 ATOM 271 C CG . HIS A 1 35 ? 2.859 12.475 36.642 1.00 22.01 ? 35 HIS A CG 1 ATOM 272 N ND1 . HIS A 1 35 ? 2.433 13.430 35.743 1.00 23.08 ? 35 HIS A ND1 1 ATOM 273 C CD2 . HIS A 1 35 ? 2.155 12.686 37.779 1.00 22.47 ? 35 HIS A CD2 1 ATOM 274 C CE1 . HIS A 1 35 ? 1.514 14.188 36.314 1.00 23.25 ? 35 HIS A CE1 1 ATOM 275 N NE2 . HIS A 1 35 ? 1.327 13.758 37.549 1.00 23.73 ? 35 HIS A NE2 1 ATOM 276 N N . GLY A 1 36 ? 4.353 8.152 34.819 1.00 15.98 ? 36 GLY A N 1 ATOM 277 C CA . GLY A 1 36 ? 5.384 7.319 34.218 1.00 15.61 ? 36 GLY A CA 1 ATOM 278 C C . GLY A 1 36 ? 6.324 6.636 35.194 1.00 15.62 ? 36 GLY A C 1 ATOM 279 O O . GLY A 1 36 ? 7.061 5.724 34.810 1.00 15.33 ? 36 GLY A O 1 ATOM 280 N N . ILE A 1 37 ? 6.307 7.072 36.451 1.00 13.90 ? 37 ILE A N 1 ATOM 281 C CA . ILE A 1 37 ? 7.169 6.491 37.474 1.00 13.91 ? 37 ILE A CA 1 ATOM 282 C C . ILE A 1 37 ? 6.470 5.304 38.129 1.00 13.23 ? 37 ILE A C 1 ATOM 283 O O . ILE A 1 37 ? 5.340 5.432 38.601 1.00 14.69 ? 37 ILE A O 1 ATOM 284 C CB . ILE A 1 37 ? 7.510 7.527 38.576 1.00 14.53 ? 37 ILE A CB 1 ATOM 285 C CG1 . ILE A 1 37 ? 7.975 8.840 37.937 1.00 12.44 ? 37 ILE A CG1 1 ATOM 286 C CG2 . ILE A 1 37 ? 8.593 6.963 39.497 1.00 12.52 ? 37 ILE A CG2 1 ATOM 287 C CD1 . ILE A 1 37 ? 8.077 9.993 38.914 1.00 14.04 ? 37 ILE A CD1 1 ATOM 288 N N . PRO A 1 38 ? 7.130 4.133 38.161 1.00 13.42 ? 38 PRO A N 1 ATOM 289 C CA . PRO A 1 38 ? 6.532 2.944 38.773 1.00 13.42 ? 38 PRO A CA 1 ATOM 290 C C . PRO A 1 38 ? 6.026 3.253 40.175 1.00 14.52 ? 38 PRO A C 1 ATOM 291 O O . PRO A 1 38 ? 6.728 3.868 40.980 1.00 14.57 ? 38 PRO A O 1 ATOM 292 C CB . PRO A 1 38 ? 7.681 1.944 38.779 1.00 13.42 ? 38 PRO A CB 1 ATOM 293 C CG . PRO A 1 38 ? 8.444 2.309 37.537 1.00 13.43 ? 38 PRO A CG 1 ATOM 294 C CD . PRO A 1 38 ? 8.469 3.824 37.621 1.00 13.76 ? 38 PRO A CD 1 ATOM 295 N N . LEU A 1 39 ? 4.803 2.817 40.454 1.00 14.02 ? 39 LEU A N 1 ATOM 296 C CA . LEU A 1 39 ? 4.160 3.044 41.736 1.00 14.12 ? 39 LEU A CA 1 ATOM 297 C C . LEU A 1 39 ? 4.083 1.749 42.554 1.00 14.82 ? 39 LEU A C 1 ATOM 298 O O . LEU A 1 39 ? 3.478 0.762 42.124 1.00 14.09 ? 39 LEU A O 1 ATOM 299 C CB . LEU A 1 39 ? 2.761 3.599 41.485 1.00 14.74 ? 39 LEU A CB 1 ATOM 300 C CG . LEU A 1 39 ? 1.900 4.017 42.664 1.00 16.05 ? 39 LEU A CG 1 ATOM 301 C CD1 . LEU A 1 39 ? 2.585 5.096 43.489 1.00 15.28 ? 39 LEU A CD1 1 ATOM 302 C CD2 . LEU A 1 39 ? 0.581 4.520 42.109 1.00 17.49 ? 39 LEU A CD2 1 ATOM 303 N N . LEU A 1 40 ? 4.692 1.755 43.736 1.00 13.48 ? 40 LEU A N 1 ATOM 304 C CA . LEU A 1 40 ? 4.682 0.564 44.580 1.00 15.37 ? 40 LEU A CA 1 ATOM 305 C C . LEU A 1 40 ? 3.270 0.236 45.060 1.00 16.17 ? 40 LEU A C 1 ATOM 306 O O . LEU A 1 40 ? 2.410 1.111 45.135 1.00 15.18 ? 40 LEU A O 1 ATOM 307 C CB . LEU A 1 40 ? 5.613 0.757 45.782 1.00 14.14 ? 40 LEU A CB 1 ATOM 308 C CG . LEU A 1 40 ? 7.113 0.830 45.450 1.00 12.56 ? 40 LEU A CG 1 ATOM 309 C CD1 . LEU A 1 40 ? 7.883 1.221 46.702 1.00 11.29 ? 40 LEU A CD1 1 ATOM 310 C CD2 . LEU A 1 40 ? 7.605 -0.519 44.899 1.00 13.34 ? 40 LEU A CD2 1 ATOM 311 N N . ARG A 1 41 ? 3.029 -1.031 45.370 1.00 17.67 ? 41 ARG A N 1 ATOM 312 C CA . ARG A 1 41 ? 1.716 -1.441 45.854 1.00 21.71 ? 41 ARG A CA 1 ATOM 313 C C . ARG A 1 41 ? 1.362 -0.738 47.163 1.00 23.01 ? 41 ARG A C 1 ATOM 314 O O . ARG A 1 41 ? 2.204 -0.558 48.043 1.00 23.23 ? 41 ARG A O 1 ATOM 315 C CB . ARG A 1 41 ? 1.672 -2.955 46.047 1.00 20.93 ? 41 ARG A CB 1 ATOM 316 C CG . ARG A 1 41 ? 1.633 -3.719 44.739 1.00 22.89 ? 41 ARG A CG 1 ATOM 317 C CD . ARG A 1 41 ? 1.756 -5.217 44.975 1.00 23.22 ? 41 ARG A CD 1 ATOM 318 N NE . ARG A 1 41 ? 3.146 -5.623 45.141 1.00 23.64 ? 41 ARG A NE 1 ATOM 319 C CZ . ARG A 1 41 ? 3.534 -6.860 45.427 1.00 23.46 ? 41 ARG A CZ 1 ATOM 320 N NH1 . ARG A 1 41 ? 4.824 -7.139 45.554 1.00 23.11 ? 41 ARG A NH1 1 ATOM 321 N NH2 . ARG A 1 41 ? 2.630 -7.816 45.596 1.00 24.30 ? 41 ARG A NH2 1 ATOM 322 N N . LYS A 1 42 ? 0.101 -0.341 47.273 1.00 26.06 ? 42 LYS A N 1 ATOM 323 C CA . LYS A 1 42 ? -0.405 0.356 48.443 1.00 29.37 ? 42 LYS A CA 1 ATOM 324 C C . LYS A 1 42 ? -0.436 -0.539 49.677 1.00 30.00 ? 42 LYS A C 1 ATOM 325 O O . LYS A 1 42 ? -0.004 -0.139 50.756 1.00 29.63 ? 42 LYS A O 1 ATOM 326 C CB . LYS A 1 42 ? -1.810 0.877 48.144 1.00 31.39 ? 42 LYS A CB 1 ATOM 327 C CG . LYS A 1 42 ? -2.506 1.555 49.310 1.00 36.23 ? 42 LYS A CG 1 ATOM 328 C CD . LYS A 1 42 ? -3.948 1.865 48.934 1.00 40.14 ? 42 LYS A CD 1 ATOM 329 C CE . LYS A 1 42 ? -4.716 2.475 50.092 1.00 42.57 ? 42 LYS A CE 1 ATOM 330 N NZ . LYS A 1 42 ? -6.115 2.794 49.688 1.00 45.00 ? 42 LYS A NZ 1 ATOM 331 N N . LYS A 1 43 ? -0.953 -1.750 49.515 1.00 31.64 ? 43 LYS A N 1 ATOM 332 C CA . LYS A 1 43 ? -1.044 -2.679 50.631 1.00 34.83 ? 43 LYS A CA 1 ATOM 333 C C . LYS A 1 43 ? -0.608 -4.082 50.232 1.00 35.14 ? 43 LYS A C 1 ATOM 334 O O . LYS A 1 43 ? -0.788 -4.506 49.091 1.00 34.77 ? 43 LYS A O 1 ATOM 335 C CB . LYS A 1 43 ? -2.480 -2.713 51.179 1.00 37.36 ? 43 LYS A CB 1 ATOM 336 C CG . LYS A 1 43 ? -3.524 -3.205 50.184 1.00 41.96 ? 43 LYS A CG 1 ATOM 337 C CD . LYS A 1 43 ? -4.933 -3.255 50.791 1.00 46.05 ? 43 LYS A CD 1 ATOM 338 C CE . LYS A 1 43 ? -5.503 -1.859 51.061 1.00 48.86 ? 43 LYS A CE 1 ATOM 339 N NZ . LYS A 1 43 ? -6.914 -1.905 51.574 1.00 50.59 ? 43 LYS A NZ 1 ATOM 340 N N . CYS A 1 44 ? -0.028 -4.796 51.187 1.00 36.17 ? 44 CYS A N 1 ATOM 341 C CA . CYS A 1 44 ? 0.442 -6.153 50.958 1.00 38.57 ? 44 CYS A CA 1 ATOM 342 C C . CYS A 1 44 ? 0.747 -6.735 52.340 1.00 41.26 ? 44 CYS A C 1 ATOM 343 O O . CYS A 1 44 ? 1.898 -6.788 52.779 1.00 42.51 ? 44 CYS A O 1 ATOM 344 C CB . CYS A 1 44 ? 1.698 -6.124 50.083 1.00 36.24 ? 44 CYS A CB 1 ATOM 345 S SG . CYS A 1 44 ? 2.161 -7.709 49.316 1.00 33.41 ? 44 CYS A SG 1 ATOM 346 N N . ASP A 1 45 ? -0.317 -7.161 53.011 1.00 43.81 ? 45 ASP A N 1 ATOM 347 C CA . ASP A 1 45 ? -0.276 -7.722 54.360 1.00 46.42 ? 45 ASP A CA 1 ATOM 348 C C . ASP A 1 45 ? 0.440 -9.068 54.548 1.00 45.37 ? 45 ASP A C 1 ATOM 349 O O . ASP A 1 45 ? 1.304 -9.204 55.418 1.00 46.39 ? 45 ASP A O 1 ATOM 350 C CB . ASP A 1 45 ? -1.715 -7.839 54.869 1.00 50.38 ? 45 ASP A CB 1 ATOM 351 C CG . ASP A 1 45 ? -2.638 -8.524 53.857 1.00 54.73 ? 45 ASP A CG 1 ATOM 352 O OD1 . ASP A 1 45 ? -2.729 -8.039 52.701 1.00 54.97 ? 45 ASP A OD1 1 ATOM 353 O OD2 . ASP A 1 45 ? -3.271 -9.545 54.218 1.00 56.79 ? 45 ASP A OD2 1 ATOM 354 N N . ASP A 1 46 ? 0.068 -10.054 53.738 1.00 42.71 ? 46 ASP A N 1 ATOM 355 C CA . ASP A 1 46 ? 0.633 -11.397 53.813 1.00 40.10 ? 46 ASP A CA 1 ATOM 356 C C . ASP A 1 46 ? 2.169 -11.490 53.760 1.00 38.21 ? 46 ASP A C 1 ATOM 357 O O . ASP A 1 46 ? 2.785 -11.306 52.708 1.00 37.09 ? 46 ASP A O 1 ATOM 358 C CB . ASP A 1 46 ? 0.014 -12.256 52.707 1.00 41.09 ? 46 ASP A CB 1 ATOM 359 C CG . ASP A 1 46 ? 0.421 -13.712 52.803 1.00 44.00 ? 46 ASP A CG 1 ATOM 360 O OD1 . ASP A 1 46 ? 0.928 -14.119 53.873 1.00 45.46 ? 46 ASP A OD1 1 ATOM 361 O OD2 . ASP A 1 46 ? 0.223 -14.452 51.813 1.00 45.43 ? 46 ASP A OD2 1 ATOM 362 N N . PRO A 1 47 ? 2.804 -11.791 54.906 1.00 36.37 ? 47 PRO A N 1 ATOM 363 C CA . PRO A 1 47 ? 4.261 -11.911 54.992 1.00 35.46 ? 47 PRO A CA 1 ATOM 364 C C . PRO A 1 47 ? 4.806 -12.966 54.041 1.00 35.83 ? 47 PRO A C 1 ATOM 365 O O . PRO A 1 47 ? 5.995 -12.973 53.729 1.00 36.97 ? 47 PRO A O 1 ATOM 366 C CB . PRO A 1 47 ? 4.487 -12.297 56.448 1.00 34.06 ? 47 PRO A CB 1 ATOM 367 C CG . PRO A 1 47 ? 3.366 -11.622 57.144 1.00 34.73 ? 47 PRO A CG 1 ATOM 368 C CD . PRO A 1 47 ? 2.198 -11.925 56.242 1.00 35.48 ? 47 PRO A CD 1 ATOM 369 N N . GLY A 1 48 ? 3.922 -13.851 53.585 1.00 36.49 ? 48 GLY A N 1 ATOM 370 C CA . GLY A 1 48 ? 4.313 -14.928 52.688 1.00 35.89 ? 48 GLY A CA 1 ATOM 371 C C . GLY A 1 48 ? 4.515 -14.571 51.225 1.00 35.96 ? 48 GLY A C 1 ATOM 372 O O . GLY A 1 48 ? 4.837 -15.437 50.409 1.00 36.49 ? 48 GLY A O 1 ATOM 373 N N . LYS A 1 49 ? 4.328 -13.303 50.879 1.00 35.32 ? 49 LYS A N 1 ATOM 374 C CA . LYS A 1 49 ? 4.518 -12.878 49.497 1.00 34.42 ? 49 LYS A CA 1 ATOM 375 C C . LYS A 1 49 ? 4.676 -11.365 49.389 1.00 31.77 ? 49 LYS A C 1 ATOM 376 O O . LYS A 1 49 ? 4.666 -10.803 48.292 1.00 30.50 ? 49 LYS A O 1 ATOM 377 C CB . LYS A 1 49 ? 3.346 -13.365 48.643 1.00 36.78 ? 49 LYS A CB 1 ATOM 378 C CG . LYS A 1 49 ? 1.972 -13.002 49.186 1.00 38.75 ? 49 LYS A CG 1 ATOM 379 C CD . LYS A 1 49 ? 0.914 -14.010 48.726 1.00 41.33 ? 49 LYS A CD 1 ATOM 380 C CE . LYS A 1 49 ? 0.872 -14.142 47.208 1.00 43.11 ? 49 LYS A CE 1 ATOM 381 N NZ . LYS A 1 49 ? -0.159 -15.121 46.752 1.00 45.28 ? 49 LYS A NZ 1 ATOM 382 N N . CYS A 1 50 ? 4.855 -10.719 50.538 1.00 28.48 ? 50 CYS A N 1 ATOM 383 C CA . CYS A 1 50 ? 5.002 -9.273 50.577 1.00 25.47 ? 50 CYS A CA 1 ATOM 384 C C . CYS A 1 50 ? 6.407 -8.790 50.945 1.00 22.02 ? 50 CYS A C 1 ATOM 385 O O . CYS A 1 50 ? 6.622 -7.624 51.284 1.00 18.78 ? 50 CYS A O 1 ATOM 386 C CB . CYS A 1 50 ? 3.954 -8.701 51.521 1.00 27.73 ? 50 CYS A CB 1 ATOM 387 S SG . CYS A 1 50 ? 2.264 -8.991 50.888 1.00 31.82 ? 50 CYS A SG 1 ATOM 388 N N . PHE A 1 51 ? 7.364 -9.701 50.853 1.00 18.52 ? 51 PHE A N 1 ATOM 389 C CA . PHE A 1 51 ? 8.747 -9.379 51.137 1.00 17.59 ? 51 PHE A CA 1 ATOM 390 C C . PHE A 1 51 ? 9.632 -9.971 50.053 1.00 18.01 ? 51 PHE A C 1 ATOM 391 O O . PHE A 1 51 ? 9.334 -11.033 49.496 1.00 18.33 ? 51 PHE A O 1 ATOM 392 C CB . PHE A 1 51 ? 9.168 -9.957 52.496 1.00 17.07 ? 51 PHE A CB 1 ATOM 393 C CG . PHE A 1 51 ? 8.541 -9.261 53.673 1.00 17.94 ? 51 PHE A CG 1 ATOM 394 C CD1 . PHE A 1 51 ? 9.091 -8.078 54.175 1.00 16.19 ? 51 PHE A CD1 1 ATOM 395 C CD2 . PHE A 1 51 ? 7.381 -9.771 54.262 1.00 18.53 ? 51 PHE A CD2 1 ATOM 396 C CE1 . PHE A 1 51 ? 8.499 -7.413 55.240 1.00 15.31 ? 51 PHE A CE1 1 ATOM 397 C CE2 . PHE A 1 51 ? 6.778 -9.113 55.331 1.00 16.91 ? 51 PHE A CE2 1 ATOM 398 C CZ . PHE A 1 51 ? 7.340 -7.930 55.820 1.00 17.45 ? 51 PHE A CZ 1 ATOM 399 N N . VAL A 1 52 ? 10.710 -9.265 49.737 1.00 15.78 ? 52 VAL A N 1 ATOM 400 C CA . VAL A 1 52 ? 11.678 -9.755 48.770 1.00 15.38 ? 52 VAL A CA 1 ATOM 401 C C . VAL A 1 52 ? 12.926 -10.014 49.606 1.00 15.74 ? 52 VAL A C 1 ATOM 402 O O . VAL A 1 52 ? 13.330 -9.165 50.409 1.00 14.96 ? 52 VAL A O 1 ATOM 403 C CB . VAL A 1 52 ? 11.990 -8.708 47.664 1.00 13.74 ? 52 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 52 ? 13.178 -9.160 46.826 1.00 15.57 ? 52 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 52 ? 10.783 -8.539 46.765 1.00 13.91 ? 52 VAL A CG2 1 ATOM 406 N N . LEU A 1 53 ? 13.511 -11.196 49.457 1.00 15.34 ? 53 LEU A N 1 ATOM 407 C CA . LEU A 1 53 ? 14.716 -11.510 50.204 1.00 16.77 ? 53 LEU A CA 1 ATOM 408 C C . LEU A 1 53 ? 15.952 -11.173 49.380 1.00 16.40 ? 53 LEU A C 1 ATOM 409 O O . LEU A 1 53 ? 16.115 -11.661 48.257 1.00 15.95 ? 53 LEU A O 1 ATOM 410 C CB . LEU A 1 53 ? 14.762 -12.991 50.583 1.00 19.17 ? 53 LEU A CB 1 ATOM 411 C CG . LEU A 1 53 ? 13.902 -13.496 51.740 1.00 23.99 ? 53 LEU A CG 1 ATOM 412 C CD1 . LEU A 1 53 ? 14.280 -14.948 52.005 1.00 25.23 ? 53 LEU A CD1 1 ATOM 413 C CD2 . LEU A 1 53 ? 14.139 -12.660 52.995 1.00 24.44 ? 53 LEU A CD2 1 ATOM 414 N N . VAL A 1 54 ? 16.817 -10.334 49.943 1.00 14.49 ? 54 VAL A N 1 ATOM 415 C CA . VAL A 1 54 ? 18.053 -9.949 49.272 1.00 13.58 ? 54 VAL A CA 1 ATOM 416 C C . VAL A 1 54 ? 19.212 -10.670 49.955 1.00 13.29 ? 54 VAL A C 1 ATOM 417 O O . VAL A 1 54 ? 19.499 -10.428 51.130 1.00 12.72 ? 54 VAL A O 1 ATOM 418 C CB . VAL A 1 54 ? 18.294 -8.418 49.347 1.00 14.44 ? 54 VAL A CB 1 ATOM 419 C CG1 . VAL A 1 54 ? 19.611 -8.063 48.668 1.00 13.45 ? 54 VAL A CG1 1 ATOM 420 C CG2 . VAL A 1 54 ? 17.138 -7.673 48.685 1.00 15.48 ? 54 VAL A CG2 1 ATOM 421 N N . ALA A 1 55 ? 19.863 -11.566 49.217 1.00 13.01 ? 55 ALA A N 1 ATOM 422 C CA . ALA A 1 55 ? 20.990 -12.329 49.747 1.00 13.65 ? 55 ALA A CA 1 ATOM 423 C C . ALA A 1 55 ? 22.297 -11.586 49.469 1.00 14.48 ? 55 ALA A C 1 ATOM 424 O O . ALA A 1 55 ? 22.771 -11.542 48.333 1.00 13.81 ? 55 ALA A O 1 ATOM 425 C CB . ALA A 1 55 ? 21.027 -13.728 49.114 1.00 13.36 ? 55 ALA A CB 1 ATOM 426 N N . LEU A 1 56 ? 22.852 -10.985 50.518 1.00 14.22 ? 56 LEU A N 1 ATOM 427 C CA . LEU A 1 56 ? 24.097 -10.236 50.432 1.00 14.01 ? 56 LEU A CA 1 ATOM 428 C C . LEU A 1 56 ? 25.220 -11.129 50.933 1.00 15.41 ? 56 LEU A C 1 ATOM 429 O O . LEU A 1 56 ? 25.172 -11.618 52.062 1.00 15.62 ? 56 LEU A O 1 ATOM 430 C CB . LEU A 1 56 ? 24.026 -8.981 51.311 1.00 13.24 ? 56 LEU A CB 1 ATOM 431 C CG . LEU A 1 56 ? 22.914 -7.973 51.003 1.00 13.63 ? 56 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 56 ? 22.967 -6.816 52.002 1.00 11.48 ? 56 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 56 ? 23.078 -7.463 49.572 1.00 15.62 ? 56 LEU A CD2 1 ATOM 434 N N . SER A 1 57 ? 26.225 -11.351 50.095 1.00 15.54 ? 57 SER A N 1 ATOM 435 C CA . SER A 1 57 ? 27.352 -12.184 50.494 1.00 17.94 ? 57 SER A CA 1 ATOM 436 C C . SER A 1 57 ? 28.661 -11.507 50.122 1.00 18.24 ? 57 SER A C 1 ATOM 437 O O . SER A 1 57 ? 28.767 -10.873 49.078 1.00 17.21 ? 57 SER A O 1 ATOM 438 C CB . SER A 1 57 ? 27.259 -13.565 49.831 1.00 17.70 ? 57 SER A CB 1 ATOM 439 O OG . SER A 1 57 ? 27.208 -13.460 48.422 1.00 22.08 ? 57 SER A OG 1 ATOM 440 N N . ASN A 1 58 ? 29.668 -11.624 50.976 1.00 20.06 ? 58 ASN A N 1 ATOM 441 C CA . ASN A 1 58 ? 30.920 -10.980 50.643 1.00 23.39 ? 58 ASN A CA 1 ATOM 442 C C . ASN A 1 58 ? 31.964 -11.958 50.114 1.00 25.25 ? 58 ASN A C 1 ATOM 443 O O . ASN A 1 58 ? 31.682 -13.138 49.886 1.00 25.24 ? 58 ASN A O 1 ATOM 444 C CB . ASN A 1 58 ? 31.460 -10.171 51.839 1.00 23.33 ? 58 ASN A CB 1 ATOM 445 C CG . ASN A 1 58 ? 31.635 -11.005 53.094 1.00 26.02 ? 58 ASN A CG 1 ATOM 446 O OD1 . ASN A 1 58 ? 31.860 -12.217 53.031 1.00 25.75 ? 58 ASN A OD1 1 ATOM 447 N ND2 . ASN A 1 58 ? 31.558 -10.350 54.250 1.00 25.09 ? 58 ASN A ND2 1 ATOM 448 N N . ASP A 1 59 ? 33.170 -11.450 49.899 1.00 27.57 ? 59 ASP A N 1 ATOM 449 C CA . ASP A 1 59 ? 34.264 -12.251 49.377 1.00 29.61 ? 59 ASP A CA 1 ATOM 450 C C . ASP A 1 59 ? 34.589 -13.468 50.246 1.00 30.65 ? 59 ASP A C 1 ATOM 451 O O . ASP A 1 59 ? 34.988 -14.512 49.734 1.00 31.35 ? 59 ASP A O 1 ATOM 452 C CB . ASP A 1 59 ? 35.492 -11.359 49.217 1.00 29.99 ? 59 ASP A CB 1 ATOM 453 C CG . ASP A 1 59 ? 35.235 -10.181 48.288 1.00 31.86 ? 59 ASP A CG 1 ATOM 454 O OD1 . ASP A 1 59 ? 34.122 -9.609 48.339 1.00 29.37 ? 59 ASP A OD1 1 ATOM 455 O OD2 . ASP A 1 59 ? 36.148 -9.822 47.513 1.00 32.70 ? 59 ASP A OD2 1 ATOM 456 N N . ASN A 1 60 ? 34.409 -13.336 51.555 1.00 31.08 ? 60 ASN A N 1 ATOM 457 C CA . ASN A 1 60 ? 34.687 -14.435 52.470 1.00 32.82 ? 60 ASN A CA 1 ATOM 458 C C . ASN A 1 60 ? 33.570 -15.465 52.495 1.00 32.49 ? 60 ASN A C 1 ATOM 459 O O . ASN A 1 60 ? 33.695 -16.506 53.135 1.00 34.07 ? 60 ASN A O 1 ATOM 460 C CB . ASN A 1 60 ? 34.908 -13.906 53.882 1.00 35.47 ? 60 ASN A CB 1 ATOM 461 C CG . ASN A 1 60 ? 36.064 -12.939 53.958 1.00 39.64 ? 60 ASN A CG 1 ATOM 462 O OD1 . ASN A 1 60 ? 37.174 -13.250 53.527 1.00 40.32 ? 60 ASN A OD1 1 ATOM 463 N ND2 . ASN A 1 60 ? 35.813 -11.754 54.513 1.00 42.87 ? 60 ASN A ND2 1 ATOM 464 N N . GLY A 1 61 ? 32.472 -15.172 51.809 1.00 31.72 ? 61 GLY A N 1 ATOM 465 C CA . GLY A 1 61 ? 31.369 -16.113 51.780 1.00 28.97 ? 61 GLY A CA 1 ATOM 466 C C . GLY A 1 61 ? 30.315 -15.857 52.834 1.00 27.89 ? 61 GLY A C 1 ATOM 467 O O . GLY A 1 61 ? 29.272 -16.503 52.826 1.00 29.91 ? 61 GLY A O 1 ATOM 468 N N . GLN A 1 62 ? 30.578 -14.930 53.751 1.00 25.14 ? 62 GLN A N 1 ATOM 469 C CA . GLN A 1 62 ? 29.604 -14.602 54.785 1.00 21.47 ? 62 GLN A CA 1 ATOM 470 C C . GLN A 1 62 ? 28.325 -14.130 54.097 1.00 20.18 ? 62 GLN A C 1 ATOM 471 O O . GLN A 1 62 ? 28.370 -13.352 53.139 1.00 18.65 ? 62 GLN A O 1 ATOM 472 C CB . GLN A 1 62 ? 30.166 -13.524 55.705 1.00 22.06 ? 62 GLN A CB 1 ATOM 473 C CG . GLN A 1 62 ? 31.349 -14.021 56.505 1.00 23.42 ? 62 GLN A CG 1 ATOM 474 C CD . GLN A 1 62 ? 32.076 -12.914 57.216 1.00 24.71 ? 62 GLN A CD 1 ATOM 475 O OE1 . GLN A 1 62 ? 32.641 -12.021 56.583 1.00 24.88 ? 62 GLN A OE1 1 ATOM 476 N NE2 . GLN A 1 62 ? 32.071 -12.962 58.545 1.00 26.00 ? 62 GLN A NE2 1 ATOM 477 N N . LEU A 1 63 ? 27.192 -14.612 54.595 1.00 18.21 ? 63 LEU A N 1 ATOM 478 C CA . LEU A 1 63 ? 25.889 -14.310 54.019 1.00 17.30 ? 63 LEU A CA 1 ATOM 479 C C . LEU A 1 63 ? 24.898 -13.649 54.979 1.00 16.70 ? 63 LEU A C 1 ATOM 480 O O . LEU A 1 63 ? 24.778 -14.040 56.142 1.00 16.46 ? 63 LEU A O 1 ATOM 481 C CB . LEU A 1 63 ? 25.286 -15.613 53.484 1.00 18.06 ? 63 LEU A CB 1 ATOM 482 C CG . LEU A 1 63 ? 23.846 -15.670 52.976 1.00 19.44 ? 63 LEU A CG 1 ATOM 483 C CD1 . LEU A 1 63 ? 23.709 -14.907 51.662 1.00 18.78 ? 63 LEU A CD1 1 ATOM 484 C CD2 . LEU A 1 63 ? 23.452 -17.132 52.791 1.00 19.23 ? 63 LEU A CD2 1 ATOM 485 N N . ALA A 1 64 ? 24.191 -12.642 54.474 1.00 13.90 ? 64 ALA A N 1 ATOM 486 C CA . ALA A 1 64 ? 23.181 -11.938 55.244 1.00 12.90 ? 64 ALA A CA 1 ATOM 487 C C . ALA A 1 64 ? 21.970 -11.808 54.328 1.00 13.96 ? 64 ALA A C 1 ATOM 488 O O . ALA A 1 64 ? 22.055 -11.209 53.255 1.00 14.01 ? 64 ALA A O 1 ATOM 489 C CB . ALA A 1 64 ? 23.687 -10.564 55.659 1.00 13.15 ? 64 ALA A CB 1 ATOM 490 N N . GLU A 1 65 ? 20.851 -12.394 54.738 1.00 14.31 ? 65 GLU A N 1 ATOM 491 C CA . GLU A 1 65 ? 19.628 -12.329 53.948 1.00 14.57 ? 65 GLU A CA 1 ATOM 492 C C . GLU A 1 65 ? 18.667 -11.308 54.538 1.00 13.90 ? 65 GLU A C 1 ATOM 493 O O . GLU A 1 65 ? 18.106 -11.497 55.618 1.00 13.46 ? 65 GLU A O 1 ATOM 494 C CB . GLU A 1 65 ? 19.012 -13.725 53.843 1.00 16.93 ? 65 GLU A CB 1 ATOM 495 C CG . GLU A 1 65 ? 19.839 -14.598 52.893 1.00 20.55 ? 65 GLU A CG 1 ATOM 496 C CD . GLU A 1 65 ? 19.540 -16.085 52.990 1.00 24.73 ? 65 GLU A CD 1 ATOM 497 O OE1 . GLU A 1 65 ? 19.416 -16.726 51.918 1.00 24.63 ? 65 GLU A OE1 1 ATOM 498 O OE2 . GLU A 1 65 ? 19.449 -16.610 54.125 1.00 21.30 ? 65 GLU A OE2 1 ATOM 499 N N . ILE A 1 66 ? 18.507 -10.214 53.798 1.00 13.48 ? 66 ILE A N 1 ATOM 500 C CA . ILE A 1 66 ? 17.686 -9.077 54.187 1.00 12.00 ? 66 ILE A CA 1 ATOM 501 C C . ILE A 1 66 ? 16.248 -9.153 53.680 1.00 12.33 ? 66 ILE A C 1 ATOM 502 O O . ILE A 1 66 ? 16.014 -9.363 52.489 1.00 12.19 ? 66 ILE A O 1 ATOM 503 C CB . ILE A 1 66 ? 18.313 -7.761 53.635 1.00 12.21 ? 66 ILE A CB 1 ATOM 504 C CG1 . ILE A 1 66 ? 19.846 -7.806 53.754 1.00 12.03 ? 66 ILE A CG1 1 ATOM 505 C CG2 . ILE A 1 66 ? 17.734 -6.558 54.360 1.00 12.55 ? 66 ILE A CG2 1 ATOM 506 C CD1 . ILE A 1 66 ? 20.377 -7.938 55.157 1.00 11.91 ? 66 ILE A CD1 1 ATOM 507 N N . ALA A 1 67 ? 15.288 -8.976 54.585 1.00 12.05 ? 67 ALA A N 1 ATOM 508 C CA . ALA A 1 67 ? 13.875 -8.988 54.205 1.00 12.32 ? 67 ALA A CA 1 ATOM 509 C C . ALA A 1 67 ? 13.469 -7.543 53.902 1.00 13.64 ? 67 ALA A C 1 ATOM 510 O O . ALA A 1 67 ? 13.591 -6.655 54.748 1.00 13.45 ? 67 ALA A O 1 ATOM 511 C CB . ALA A 1 67 ? 13.021 -9.546 55.332 1.00 12.53 ? 67 ALA A CB 1 ATOM 512 N N . ILE A 1 68 ? 12.985 -7.314 52.687 1.00 14.50 ? 68 ILE A N 1 ATOM 513 C CA . ILE A 1 68 ? 12.591 -5.981 52.261 1.00 14.63 ? 68 ILE A CA 1 ATOM 514 C C . ILE A 1 68 ? 11.102 -5.901 51.911 1.00 15.25 ? 68 ILE A C 1 ATOM 515 O O . ILE A 1 68 ? 10.595 -6.662 51.077 1.00 14.99 ? 68 ILE A O 1 ATOM 516 C CB . ILE A 1 68 ? 13.484 -5.533 51.065 1.00 16.00 ? 68 ILE A CB 1 ATOM 517 C CG1 . ILE A 1 68 ? 14.917 -5.320 51.580 1.00 16.82 ? 68 ILE A CG1 1 ATOM 518 C CG2 . ILE A 1 68 ? 12.945 -4.255 50.417 1.00 15.81 ? 68 ILE A CG2 1 ATOM 519 C CD1 . ILE A 1 68 ? 15.871 -4.859 50.563 1.00 18.78 ? 68 ILE A CD1 1 ATOM 520 N N . ASP A 1 69 ? 10.417 -4.982 52.587 1.00 14.60 ? 69 ASP A N 1 ATOM 521 C CA . ASP A 1 69 ? 8.987 -4.726 52.414 1.00 16.19 ? 69 ASP A CA 1 ATOM 522 C C . ASP A 1 69 ? 8.701 -4.264 50.971 1.00 14.78 ? 69 ASP A C 1 ATOM 523 O O . ASP A 1 69 ? 9.346 -3.334 50.489 1.00 14.61 ? 69 ASP A O 1 ATOM 524 C CB . ASP A 1 69 ? 8.579 -3.638 53.412 1.00 19.97 ? 69 ASP A CB 1 ATOM 525 C CG . ASP A 1 69 ? 7.085 -3.482 53.537 1.00 26.44 ? 69 ASP A CG 1 ATOM 526 O OD1 . ASP A 1 69 ? 6.422 -3.164 52.529 1.00 28.84 ? 69 ASP A OD1 1 ATOM 527 O OD2 . ASP A 1 69 ? 6.568 -3.673 54.657 1.00 32.22 ? 69 ASP A OD2 1 ATOM 528 N N . VAL A 1 70 ? 7.737 -4.889 50.289 1.00 13.57 ? 70 VAL A N 1 ATOM 529 C CA . VAL A 1 70 ? 7.437 -4.507 48.903 1.00 13.17 ? 70 VAL A CA 1 ATOM 530 C C . VAL A 1 70 ? 6.634 -3.215 48.735 1.00 14.76 ? 70 VAL A C 1 ATOM 531 O O . VAL A 1 70 ? 6.482 -2.715 47.617 1.00 15.44 ? 70 VAL A O 1 ATOM 532 C CB . VAL A 1 70 ? 6.682 -5.627 48.128 1.00 14.21 ? 70 VAL A CB 1 ATOM 533 C CG1 . VAL A 1 70 ? 7.514 -6.908 48.100 1.00 12.10 ? 70 VAL A CG1 1 ATOM 534 C CG2 . VAL A 1 70 ? 5.309 -5.860 48.748 1.00 12.77 ? 70 VAL A CG2 1 ATOM 535 N N . THR A 1 71 ? 6.113 -2.670 49.827 1.00 14.55 ? 71 THR A N 1 ATOM 536 C CA . THR A 1 71 ? 5.342 -1.439 49.719 1.00 15.42 ? 71 THR A CA 1 ATOM 537 C C . THR A 1 71 ? 6.192 -0.212 50.045 1.00 16.23 ? 71 THR A C 1 ATOM 538 O O . THR A 1 71 ? 5.911 0.893 49.575 1.00 17.23 ? 71 THR A O 1 ATOM 539 C CB . THR A 1 71 ? 4.110 -1.457 50.659 1.00 15.63 ? 71 THR A CB 1 ATOM 540 O OG1 . THR A 1 71 ? 4.545 -1.491 52.023 1.00 15.02 ? 71 THR A OG1 1 ATOM 541 C CG2 . THR A 1 71 ? 3.246 -2.675 50.379 1.00 16.41 ? 71 THR A CG2 1 ATOM 542 N N . SER A 1 72 ? 7.252 -0.411 50.824 1.00 15.67 ? 72 SER A N 1 ATOM 543 C CA . SER A 1 72 ? 8.107 0.696 51.235 1.00 16.50 ? 72 SER A CA 1 ATOM 544 C C . SER A 1 72 ? 9.577 0.506 50.890 1.00 16.70 ? 72 SER A C 1 ATOM 545 O O . SER A 1 72 ? 10.357 1.453 50.971 1.00 16.94 ? 72 SER A O 1 ATOM 546 C CB . SER A 1 72 ? 8.001 0.874 52.743 1.00 17.47 ? 72 SER A CB 1 ATOM 547 O OG . SER A 1 72 ? 8.446 -0.311 53.395 1.00 19.58 ? 72 SER A OG 1 ATOM 548 N N . VAL A 1 73 ? 9.942 -0.717 50.515 1.00 16.24 ? 73 VAL A N 1 ATOM 549 C CA . VAL A 1 73 ? 11.322 -1.091 50.197 1.00 16.85 ? 73 VAL A CA 1 ATOM 550 C C . VAL A 1 73 ? 12.181 -0.992 51.461 1.00 18.66 ? 73 VAL A C 1 ATOM 551 O O . VAL A 1 73 ? 13.407 -0.914 51.379 1.00 17.45 ? 73 VAL A O 1 ATOM 552 C CB . VAL A 1 73 ? 11.988 -0.195 49.097 1.00 17.53 ? 73 VAL A CB 1 ATOM 553 C CG1 . VAL A 1 73 ? 13.226 -0.910 48.538 1.00 13.75 ? 73 VAL A CG1 1 ATOM 554 C CG2 . VAL A 1 73 ? 11.010 0.106 47.972 1.00 15.25 ? 73 VAL A CG2 1 ATOM 555 N N . TYR A 1 74 ? 11.555 -0.990 52.635 1.00 18.32 ? 74 TYR A N 1 ATOM 556 C CA . TYR A 1 74 ? 12.378 -0.913 53.826 1.00 21.24 ? 74 TYR A CA 1 ATOM 557 C C . TYR A 1 74 ? 12.745 -2.267 54.410 1.00 17.41 ? 74 TYR A C 1 ATOM 558 O O . TYR A 1 74 ? 12.031 -3.261 54.255 1.00 15.84 ? 74 TYR A O 1 ATOM 559 C CB . TYR A 1 74 ? 11.737 -0.043 54.909 1.00 27.88 ? 74 TYR A CB 1 ATOM 560 C CG . TYR A 1 74 ? 12.760 0.886 55.566 1.00 35.15 ? 74 TYR A CG 1 ATOM 561 C CD1 . TYR A 1 74 ? 13.371 1.915 54.828 1.00 36.79 ? 74 TYR A CD1 1 ATOM 562 C CD2 . TYR A 1 74 ? 13.115 0.743 56.917 1.00 36.69 ? 74 TYR A CD2 1 ATOM 563 C CE1 . TYR A 1 74 ? 14.304 2.784 55.414 1.00 37.43 ? 74 TYR A CE1 1 ATOM 564 C CE2 . TYR A 1 74 ? 14.051 1.605 57.515 1.00 37.98 ? 74 TYR A CE2 1 ATOM 565 C CZ . TYR A 1 74 ? 14.637 2.628 56.756 1.00 38.88 ? 74 TYR A CZ 1 ATOM 566 O OH . TYR A 1 74 ? 15.528 3.514 57.338 1.00 37.68 ? 74 TYR A OH 1 ATOM 567 N N . VAL A 1 75 ? 13.902 -2.282 55.056 1.00 15.34 ? 75 VAL A N 1 ATOM 568 C CA . VAL A 1 75 ? 14.442 -3.461 55.713 1.00 14.87 ? 75 VAL A CA 1 ATOM 569 C C . VAL A 1 75 ? 13.703 -3.657 57.047 1.00 14.58 ? 75 VAL A C 1 ATOM 570 O O . VAL A 1 75 ? 13.636 -2.731 57.862 1.00 13.58 ? 75 VAL A O 1 ATOM 571 C CB . VAL A 1 75 ? 15.953 -3.255 55.989 1.00 13.75 ? 75 VAL A CB 1 ATOM 572 C CG1 . VAL A 1 75 ? 16.511 -4.419 56.793 1.00 14.51 ? 75 VAL A CG1 1 ATOM 573 C CG2 . VAL A 1 75 ? 16.701 -3.080 54.665 1.00 13.14 ? 75 VAL A CG2 1 ATOM 574 N N . VAL A 1 76 ? 13.128 -4.839 57.262 1.00 13.32 ? 76 VAL A N 1 ATOM 575 C CA . VAL A 1 76 ? 12.429 -5.107 58.520 1.00 13.68 ? 76 VAL A CA 1 ATOM 576 C C . VAL A 1 76 ? 13.242 -6.054 59.398 1.00 13.21 ? 76 VAL A C 1 ATOM 577 O O . VAL A 1 76 ? 13.069 -6.087 60.616 1.00 14.04 ? 76 VAL A O 1 ATOM 578 C CB . VAL A 1 76 ? 11.013 -5.723 58.304 1.00 15.22 ? 76 VAL A CB 1 ATOM 579 C CG1 . VAL A 1 76 ? 10.134 -4.758 57.518 1.00 16.66 ? 76 VAL A CG1 1 ATOM 580 C CG2 . VAL A 1 76 ? 11.121 -7.057 57.587 1.00 18.70 ? 76 VAL A CG2 1 ATOM 581 N N . GLY A 1 77 ? 14.138 -6.813 58.776 1.00 12.29 ? 77 GLY A N 1 ATOM 582 C CA . GLY A 1 77 ? 14.954 -7.752 59.524 1.00 11.86 ? 77 GLY A CA 1 ATOM 583 C C . GLY A 1 77 ? 15.846 -8.556 58.602 1.00 11.96 ? 77 GLY A C 1 ATOM 584 O O . GLY A 1 77 ? 15.831 -8.361 57.386 1.00 12.25 ? 77 GLY A O 1 ATOM 585 N N . TYR A 1 78 ? 16.619 -9.471 59.171 1.00 11.71 ? 78 TYR A N 1 ATOM 586 C CA . TYR A 1 78 ? 17.530 -10.272 58.373 1.00 11.49 ? 78 TYR A CA 1 ATOM 587 C C . TYR A 1 78 ? 17.938 -11.566 59.071 1.00 11.63 ? 78 TYR A C 1 ATOM 588 O O . TYR A 1 78 ? 17.783 -11.723 60.287 1.00 11.51 ? 78 TYR A O 1 ATOM 589 C CB . TYR A 1 78 ? 18.796 -9.468 58.079 1.00 11.50 ? 78 TYR A CB 1 ATOM 590 C CG . TYR A 1 78 ? 19.593 -9.139 59.329 1.00 11.59 ? 78 TYR A CG 1 ATOM 591 C CD1 . TYR A 1 78 ? 19.235 -8.074 60.150 1.00 10.34 ? 78 TYR A CD1 1 ATOM 592 C CD2 . TYR A 1 78 ? 20.680 -9.926 59.710 1.00 11.52 ? 78 TYR A CD2 1 ATOM 593 C CE1 . TYR A 1 78 ? 19.937 -7.800 61.322 1.00 11.17 ? 78 TYR A CE1 1 ATOM 594 C CE2 . TYR A 1 78 ? 21.388 -9.662 60.877 1.00 11.93 ? 78 TYR A CE2 1 ATOM 595 C CZ . TYR A 1 78 ? 21.011 -8.599 61.677 1.00 12.06 ? 78 TYR A CZ 1 ATOM 596 O OH . TYR A 1 78 ? 21.712 -8.332 62.829 1.00 13.70 ? 78 TYR A OH 1 ATOM 597 N N . GLN A 1 79 ? 18.475 -12.487 58.281 1.00 12.18 ? 79 GLN A N 1 ATOM 598 C CA . GLN A 1 79 ? 18.954 -13.755 58.801 1.00 12.61 ? 79 GLN A CA 1 ATOM 599 C C . GLN A 1 79 ? 20.438 -13.942 58.514 1.00 13.07 ? 79 GLN A C 1 ATOM 600 O O . GLN A 1 79 ? 20.917 -13.670 57.413 1.00 12.99 ? 79 GLN A O 1 ATOM 601 C CB . GLN A 1 79 ? 18.201 -14.937 58.186 1.00 14.42 ? 79 GLN A CB 1 ATOM 602 C CG . GLN A 1 79 ? 18.765 -16.276 58.658 1.00 15.44 ? 79 GLN A CG 1 ATOM 603 C CD . GLN A 1 79 ? 18.014 -17.470 58.120 1.00 16.44 ? 79 GLN A CD 1 ATOM 604 O OE1 . GLN A 1 79 ? 16.912 -17.345 57.588 1.00 17.91 ? 79 GLN A OE1 1 ATOM 605 N NE2 . GLN A 1 79 ? 18.603 -18.648 58.275 1.00 16.65 ? 79 GLN A NE2 1 ATOM 606 N N . VAL A 1 80 ? 21.157 -14.398 59.529 1.00 13.54 ? 80 VAL A N 1 ATOM 607 C CA . VAL A 1 80 ? 22.573 -14.698 59.413 1.00 14.80 ? 80 VAL A CA 1 ATOM 608 C C . VAL A 1 80 ? 22.718 -16.050 60.099 1.00 16.09 ? 80 VAL A C 1 ATOM 609 O O . VAL A 1 80 ? 22.212 -16.247 61.213 1.00 15.61 ? 80 VAL A O 1 ATOM 610 C CB . VAL A 1 80 ? 23.463 -13.640 60.106 1.00 14.46 ? 80 VAL A CB 1 ATOM 611 C CG1 . VAL A 1 80 ? 23.618 -12.428 59.193 1.00 14.96 ? 80 VAL A CG1 1 ATOM 612 C CG2 . VAL A 1 80 ? 22.856 -13.226 61.456 1.00 17.75 ? 80 VAL A CG2 1 ATOM 613 N N . ARG A 1 81 ? 23.368 -16.992 59.421 1.00 16.60 ? 81 ARG A N 1 ATOM 614 C CA . ARG A 1 81 ? 23.542 -18.331 59.972 1.00 18.61 ? 81 ARG A CA 1 ATOM 615 C C . ARG A 1 81 ? 22.149 -18.895 60.300 1.00 18.61 ? 81 ARG A C 1 ATOM 616 O O . ARG A 1 81 ? 21.273 -18.911 59.432 1.00 19.44 ? 81 ARG A O 1 ATOM 617 C CB . ARG A 1 81 ? 24.451 -18.262 61.209 1.00 20.53 ? 81 ARG A CB 1 ATOM 618 C CG . ARG A 1 81 ? 25.892 -17.837 60.861 1.00 25.08 ? 81 ARG A CG 1 ATOM 619 C CD . ARG A 1 81 ? 26.749 -17.530 62.080 1.00 28.03 ? 81 ARG A CD 1 ATOM 620 N NE . ARG A 1 81 ? 28.070 -17.023 61.700 1.00 33.16 ? 81 ARG A NE 1 ATOM 621 C CZ . ARG A 1 81 ? 28.955 -16.491 62.550 1.00 37.85 ? 81 ARG A CZ 1 ATOM 622 N NH1 . ARG A 1 81 ? 28.676 -16.389 63.846 1.00 38.76 ? 81 ARG A NH1 1 ATOM 623 N NH2 . ARG A 1 81 ? 30.127 -16.042 62.106 1.00 38.62 ? 81 ARG A NH2 1 ATOM 624 N N . ASN A 1 82 ? 21.927 -19.344 61.533 1.00 18.65 ? 82 ASN A N 1 ATOM 625 C CA . ASN A 1 82 ? 20.624 -19.895 61.906 1.00 18.44 ? 82 ASN A CA 1 ATOM 626 C C . ASN A 1 82 ? 19.879 -18.940 62.832 1.00 17.74 ? 82 ASN A C 1 ATOM 627 O O . ASN A 1 82 ? 19.018 -19.352 63.614 1.00 17.55 ? 82 ASN A O 1 ATOM 628 C CB . ASN A 1 82 ? 20.807 -21.250 62.597 1.00 21.05 ? 82 ASN A CB 1 ATOM 629 C CG . ASN A 1 82 ? 21.522 -21.133 63.929 1.00 24.13 ? 82 ASN A CG 1 ATOM 630 O OD1 . ASN A 1 82 ? 22.371 -20.256 64.125 1.00 25.46 ? 82 ASN A OD1 1 ATOM 631 N ND2 . ASN A 1 82 ? 21.193 -22.028 64.851 1.00 27.99 ? 82 ASN A ND2 1 ATOM 632 N N . ARG A 1 83 ? 20.213 -17.659 62.725 1.00 17.03 ? 83 ARG A N 1 ATOM 633 C CA . ARG A 1 83 ? 19.600 -16.628 63.550 1.00 16.29 ? 83 ARG A CA 1 ATOM 634 C C . ARG A 1 83 ? 18.946 -15.546 62.707 1.00 16.04 ? 83 ARG A C 1 ATOM 635 O O . ARG A 1 83 ? 19.321 -15.333 61.553 1.00 15.22 ? 83 ARG A O 1 ATOM 636 C CB . ARG A 1 83 ? 20.656 -15.980 64.438 1.00 17.10 ? 83 ARG A CB 1 ATOM 637 C CG . ARG A 1 83 ? 21.269 -16.921 65.442 1.00 19.38 ? 83 ARG A CG 1 ATOM 638 C CD . ARG A 1 83 ? 22.341 -16.210 66.226 1.00 22.66 ? 83 ARG A CD 1 ATOM 639 N NE . ARG A 1 83 ? 22.725 -16.967 67.410 1.00 28.38 ? 83 ARG A NE 1 ATOM 640 C CZ . ARG A 1 83 ? 22.139 -16.856 68.597 1.00 29.64 ? 83 ARG A CZ 1 ATOM 641 N NH1 . ARG A 1 83 ? 21.130 -16.009 68.778 1.00 28.89 ? 83 ARG A NH1 1 ATOM 642 N NH2 . ARG A 1 83 ? 22.566 -17.600 69.607 1.00 32.00 ? 83 ARG A NH2 1 ATOM 643 N N . SER A 1 84 ? 17.952 -14.878 63.287 1.00 14.14 ? 84 SER A N 1 ATOM 644 C CA . SER A 1 84 ? 17.280 -13.785 62.605 1.00 13.26 ? 84 SER A CA 1 ATOM 645 C C . SER A 1 84 ? 17.091 -12.652 63.598 1.00 13.34 ? 84 SER A C 1 ATOM 646 O O . SER A 1 84 ? 16.895 -12.885 64.796 1.00 12.36 ? 84 SER A O 1 ATOM 647 C CB . SER A 1 84 ? 15.940 -14.236 62.004 1.00 12.44 ? 84 SER A CB 1 ATOM 648 O OG . SER A 1 84 ? 15.025 -14.694 62.976 1.00 13.78 ? 84 SER A OG 1 ATOM 649 N N . TYR A 1 85 ? 17.189 -11.423 63.099 1.00 12.80 ? 85 TYR A N 1 ATOM 650 C CA . TYR A 1 85 ? 17.052 -10.233 63.928 1.00 12.55 ? 85 TYR A CA 1 ATOM 651 C C . TYR A 1 85 ? 16.072 -9.287 63.252 1.00 13.61 ? 85 TYR A C 1 ATOM 652 O O . TYR A 1 85 ? 16.116 -9.116 62.034 1.00 13.12 ? 85 TYR A O 1 ATOM 653 C CB . TYR A 1 85 ? 18.404 -9.538 64.090 1.00 11.67 ? 85 TYR A CB 1 ATOM 654 C CG . TYR A 1 85 ? 19.462 -10.417 64.716 1.00 14.23 ? 85 TYR A CG 1 ATOM 655 C CD1 . TYR A 1 85 ? 20.161 -11.361 63.955 1.00 14.65 ? 85 TYR A CD1 1 ATOM 656 C CD2 . TYR A 1 85 ? 19.722 -10.350 66.082 1.00 13.02 ? 85 TYR A CD2 1 ATOM 657 C CE1 . TYR A 1 85 ? 21.091 -12.222 64.546 1.00 16.19 ? 85 TYR A CE1 1 ATOM 658 C CE2 . TYR A 1 85 ? 20.641 -11.203 66.684 1.00 15.47 ? 85 TYR A CE2 1 ATOM 659 C CZ . TYR A 1 85 ? 21.320 -12.138 65.915 1.00 16.86 ? 85 TYR A CZ 1 ATOM 660 O OH . TYR A 1 85 ? 22.198 -13.007 66.530 1.00 19.50 ? 85 TYR A OH 1 ATOM 661 N N . PHE A 1 86 ? 15.194 -8.681 64.044 1.00 12.55 ? 86 PHE A N 1 ATOM 662 C CA . PHE A 1 86 ? 14.198 -7.754 63.523 1.00 13.42 ? 86 PHE A CA 1 ATOM 663 C C . PHE A 1 86 ? 14.268 -6.404 64.226 1.00 13.19 ? 86 PHE A C 1 ATOM 664 O O . PHE A 1 86 ? 14.574 -6.332 65.413 1.00 13.89 ? 86 PHE A O 1 ATOM 665 C CB . PHE A 1 86 ? 12.796 -8.326 63.727 1.00 13.32 ? 86 PHE A CB 1 ATOM 666 C CG . PHE A 1 86 ? 12.510 -9.545 62.904 1.00 14.30 ? 86 PHE A CG 1 ATOM 667 C CD1 . PHE A 1 86 ? 11.827 -9.436 61.693 1.00 13.54 ? 86 PHE A CD1 1 ATOM 668 C CD2 . PHE A 1 86 ? 12.920 -10.806 63.339 1.00 13.17 ? 86 PHE A CD2 1 ATOM 669 C CE1 . PHE A 1 86 ? 11.550 -10.569 60.920 1.00 13.40 ? 86 PHE A CE1 1 ATOM 670 C CE2 . PHE A 1 86 ? 12.651 -11.947 62.578 1.00 14.98 ? 86 PHE A CE2 1 ATOM 671 C CZ . PHE A 1 86 ? 11.963 -11.829 61.365 1.00 14.34 ? 86 PHE A CZ 1 ATOM 672 N N . PHE A 1 87 ? 13.983 -5.336 63.490 1.00 12.49 ? 87 PHE A N 1 ATOM 673 C CA . PHE A 1 87 ? 13.966 -4.010 64.088 1.00 12.94 ? 87 PHE A CA 1 ATOM 674 C C . PHE A 1 87 ? 12.856 -4.003 65.142 1.00 14.42 ? 87 PHE A C 1 ATOM 675 O O . PHE A 1 87 ? 11.863 -4.727 65.018 1.00 14.55 ? 87 PHE A O 1 ATOM 676 C CB . PHE A 1 87 ? 13.698 -2.949 63.018 1.00 12.81 ? 87 PHE A CB 1 ATOM 677 C CG . PHE A 1 87 ? 14.928 -2.534 62.255 1.00 12.59 ? 87 PHE A CG 1 ATOM 678 C CD1 . PHE A 1 87 ? 14.964 -2.615 60.861 1.00 12.48 ? 87 PHE A CD1 1 ATOM 679 C CD2 . PHE A 1 87 ? 16.043 -2.042 62.927 1.00 11.57 ? 87 PHE A CD2 1 ATOM 680 C CE1 . PHE A 1 87 ? 16.093 -2.210 60.147 1.00 12.43 ? 87 PHE A CE1 1 ATOM 681 C CE2 . PHE A 1 87 ? 17.178 -1.633 62.226 1.00 13.25 ? 87 PHE A CE2 1 ATOM 682 C CZ . PHE A 1 87 ? 17.205 -1.716 60.829 1.00 11.91 ? 87 PHE A CZ 1 ATOM 683 N N . LYS A 1 88 ? 13.022 -3.195 66.181 1.00 14.73 ? 88 LYS A N 1 ATOM 684 C CA . LYS A 1 88 ? 12.033 -3.143 67.247 1.00 15.92 ? 88 LYS A CA 1 ATOM 685 C C . LYS A 1 88 ? 10.643 -2.808 66.714 1.00 17.71 ? 88 LYS A C 1 ATOM 686 O O . LYS A 1 88 ? 9.638 -3.269 67.262 1.00 18.11 ? 88 LYS A O 1 ATOM 687 C CB . LYS A 1 88 ? 12.452 -2.114 68.302 1.00 15.63 ? 88 LYS A CB 1 ATOM 688 C CG . LYS A 1 88 ? 11.525 -2.037 69.499 1.00 15.43 ? 88 LYS A CG 1 ATOM 689 C CD . LYS A 1 88 ? 11.965 -0.944 70.458 1.00 17.01 ? 88 LYS A CD 1 ATOM 690 C CE . LYS A 1 88 ? 11.131 -0.963 71.718 1.00 19.58 ? 88 LYS A CE 1 ATOM 691 N NZ . LYS A 1 88 ? 11.321 -2.232 72.472 1.00 19.88 ? 88 LYS A NZ 1 ATOM 692 N N . ASP A 1 89 ? 10.587 -2.027 65.634 1.00 18.43 ? 89 ASP A N 1 ATOM 693 C CA . ASP A 1 89 ? 9.308 -1.625 65.049 1.00 19.71 ? 89 ASP A CA 1 ATOM 694 C C . ASP A 1 89 ? 8.747 -2.510 63.920 1.00 19.76 ? 89 ASP A C 1 ATOM 695 O O . ASP A 1 89 ? 7.759 -2.150 63.273 1.00 18.89 ? 89 ASP A O 1 ATOM 696 C CB . ASP A 1 89 ? 9.384 -0.153 64.597 1.00 20.65 ? 89 ASP A CB 1 ATOM 697 C CG . ASP A 1 89 ? 10.459 0.098 63.555 1.00 22.60 ? 89 ASP A CG 1 ATOM 698 O OD1 . ASP A 1 89 ? 11.545 -0.516 63.624 1.00 20.94 ? 89 ASP A OD1 1 ATOM 699 O OD2 . ASP A 1 89 ? 10.219 0.940 62.665 1.00 26.97 ? 89 ASP A OD2 1 ATOM 700 N N . ALA A 1 90 ? 9.350 -3.673 63.690 1.00 17.97 ? 90 ALA A N 1 ATOM 701 C CA . ALA A 1 90 ? 8.837 -4.569 62.656 1.00 18.43 ? 90 ALA A CA 1 ATOM 702 C C . ALA A 1 90 ? 7.468 -5.060 63.128 1.00 18.32 ? 90 ALA A C 1 ATOM 703 O O . ALA A 1 90 ? 7.308 -5.435 64.286 1.00 18.83 ? 90 ALA A O 1 ATOM 704 C CB . ALA A 1 90 ? 9.780 -5.753 62.465 1.00 18.98 ? 90 ALA A CB 1 ATOM 705 N N . PRO A 1 91 ? 6.458 -5.058 62.245 1.00 18.80 ? 91 PRO A N 1 ATOM 706 C CA . PRO A 1 91 ? 5.136 -5.525 62.680 1.00 18.73 ? 91 PRO A CA 1 ATOM 707 C C . PRO A 1 91 ? 5.126 -6.995 63.086 1.00 18.47 ? 91 PRO A C 1 ATOM 708 O O . PRO A 1 91 ? 5.969 -7.777 62.637 1.00 17.78 ? 91 PRO A O 1 ATOM 709 C CB . PRO A 1 91 ? 4.248 -5.232 61.472 1.00 19.10 ? 91 PRO A CB 1 ATOM 710 C CG . PRO A 1 91 ? 5.198 -5.291 60.322 1.00 20.75 ? 91 PRO A CG 1 ATOM 711 C CD . PRO A 1 91 ? 6.421 -4.592 60.848 1.00 19.32 ? 91 PRO A CD 1 ATOM 712 N N . ASP A 1 92 ? 4.172 -7.354 63.945 1.00 19.25 ? 92 ASP A N 1 ATOM 713 C CA . ASP A 1 92 ? 4.037 -8.722 64.448 1.00 20.82 ? 92 ASP A CA 1 ATOM 714 C C . ASP A 1 92 ? 3.940 -9.778 63.355 1.00 21.69 ? 92 ASP A C 1 ATOM 715 O O . ASP A 1 92 ? 4.597 -10.819 63.431 1.00 22.24 ? 92 ASP A O 1 ATOM 716 C CB . ASP A 1 92 ? 2.810 -8.843 65.357 1.00 21.29 ? 92 ASP A CB 1 ATOM 717 C CG . ASP A 1 92 ? 3.025 -8.214 66.721 1.00 24.09 ? 92 ASP A CG 1 ATOM 718 O OD1 . ASP A 1 92 ? 4.171 -7.827 67.039 1.00 22.48 ? 92 ASP A OD1 1 ATOM 719 O OD2 . ASP A 1 92 ? 2.041 -8.119 67.485 1.00 27.44 ? 92 ASP A OD2 1 ATOM 720 N N . ALA A 1 93 ? 3.110 -9.520 62.349 1.00 21.02 ? 93 ALA A N 1 ATOM 721 C CA . ALA A 1 93 ? 2.932 -10.460 61.249 1.00 20.73 ? 93 ALA A CA 1 ATOM 722 C C . ALA A 1 93 ? 4.265 -10.803 60.581 1.00 19.77 ? 93 ALA A C 1 ATOM 723 O O . ALA A 1 93 ? 4.514 -11.956 60.231 1.00 20.70 ? 93 ALA A O 1 ATOM 724 C CB . ALA A 1 93 ? 1.970 -9.878 60.230 1.00 21.85 ? 93 ALA A CB 1 ATOM 725 N N . ALA A 1 94 ? 5.119 -9.801 60.405 1.00 18.40 ? 94 ALA A N 1 ATOM 726 C CA . ALA A 1 94 ? 6.423 -10.002 59.781 1.00 16.56 ? 94 ALA A CA 1 ATOM 727 C C . ALA A 1 94 ? 7.364 -10.765 60.708 1.00 16.67 ? 94 ALA A C 1 ATOM 728 O O . ALA A 1 94 ? 8.057 -11.692 60.284 1.00 15.23 ? 94 ALA A O 1 ATOM 729 C CB . ALA A 1 94 ? 7.038 -8.660 59.416 1.00 17.13 ? 94 ALA A CB 1 ATOM 730 N N . TYR A 1 95 ? 7.388 -10.362 61.976 1.00 16.20 ? 95 TYR A N 1 ATOM 731 C CA . TYR A 1 95 ? 8.243 -11.004 62.964 1.00 15.36 ? 95 TYR A CA 1 ATOM 732 C C . TYR A 1 95 ? 7.939 -12.501 63.068 1.00 16.06 ? 95 TYR A C 1 ATOM 733 O O . TYR A 1 95 ? 8.845 -13.328 63.155 1.00 15.79 ? 95 TYR A O 1 ATOM 734 C CB . TYR A 1 95 ? 8.038 -10.357 64.334 1.00 14.89 ? 95 TYR A CB 1 ATOM 735 C CG . TYR A 1 95 ? 8.980 -10.887 65.398 1.00 16.20 ? 95 TYR A CG 1 ATOM 736 C CD1 . TYR A 1 95 ? 10.301 -10.439 65.475 1.00 14.84 ? 95 TYR A CD1 1 ATOM 737 C CD2 . TYR A 1 95 ? 8.560 -11.863 66.304 1.00 15.48 ? 95 TYR A CD2 1 ATOM 738 C CE1 . TYR A 1 95 ? 11.181 -10.950 66.425 1.00 15.08 ? 95 TYR A CE1 1 ATOM 739 C CE2 . TYR A 1 95 ? 9.435 -12.381 67.259 1.00 15.78 ? 95 TYR A CE2 1 ATOM 740 C CZ . TYR A 1 95 ? 10.740 -11.922 67.312 1.00 15.69 ? 95 TYR A CZ 1 ATOM 741 O OH . TYR A 1 95 ? 11.604 -12.445 68.242 1.00 15.03 ? 95 TYR A OH 1 ATOM 742 N N . GLU A 1 96 ? 6.656 -12.843 63.060 1.00 17.06 ? 96 GLU A N 1 ATOM 743 C CA . GLU A 1 96 ? 6.245 -14.238 63.172 1.00 17.88 ? 96 GLU A CA 1 ATOM 744 C C . GLU A 1 96 ? 6.341 -14.993 61.853 1.00 18.01 ? 96 GLU A C 1 ATOM 745 O O . GLU A 1 96 ? 6.731 -16.159 61.833 1.00 18.76 ? 96 GLU A O 1 ATOM 746 C CB . GLU A 1 96 ? 4.807 -14.315 63.697 1.00 18.47 ? 96 GLU A CB 1 ATOM 747 C CG . GLU A 1 96 ? 4.568 -13.472 64.943 1.00 19.54 ? 96 GLU A CG 1 ATOM 748 C CD . GLU A 1 96 ? 3.118 -13.460 65.373 1.00 21.84 ? 96 GLU A CD 1 ATOM 749 O OE1 . GLU A 1 96 ? 2.238 -13.776 64.542 1.00 22.90 ? 96 GLU A OE1 1 ATOM 750 O OE2 . GLU A 1 96 ? 2.851 -13.120 66.543 1.00 24.30 ? 96 GLU A OE2 1 ATOM 751 N N . GLY A 1 97 ? 6.011 -14.316 60.754 1.00 17.33 ? 97 GLY A N 1 ATOM 752 C CA . GLY A 1 97 ? 6.016 -14.956 59.451 1.00 15.70 ? 97 GLY A CA 1 ATOM 753 C C . GLY A 1 97 ? 7.319 -15.142 58.704 1.00 17.35 ? 97 GLY A C 1 ATOM 754 O O . GLY A 1 97 ? 7.441 -16.074 57.913 1.00 19.00 ? 97 GLY A O 1 ATOM 755 N N . LEU A 1 98 ? 8.295 -14.274 58.940 1.00 16.69 ? 98 LEU A N 1 ATOM 756 C CA . LEU A 1 98 ? 9.567 -14.368 58.236 1.00 15.53 ? 98 LEU A CA 1 ATOM 757 C C . LEU A 1 98 ? 10.621 -15.185 58.952 1.00 15.29 ? 98 LEU A C 1 ATOM 758 O O . LEU A 1 98 ? 10.574 -15.364 60.163 1.00 15.62 ? 98 LEU A O 1 ATOM 759 C CB . LEU A 1 98 ? 10.121 -12.966 57.978 1.00 16.56 ? 98 LEU A CB 1 ATOM 760 C CG . LEU A 1 98 ? 9.282 -12.040 57.094 1.00 17.33 ? 98 LEU A CG 1 ATOM 761 C CD1 . LEU A 1 98 ? 9.860 -10.633 57.129 1.00 18.73 ? 98 LEU A CD1 1 ATOM 762 C CD2 . LEU A 1 98 ? 9.252 -12.577 55.677 1.00 18.02 ? 98 LEU A CD2 1 ATOM 763 N N . PHE A 1 99 ? 11.577 -15.677 58.177 1.00 16.23 ? 99 PHE A N 1 ATOM 764 C CA . PHE A 1 99 ? 12.701 -16.449 58.694 1.00 16.56 ? 99 PHE A CA 1 ATOM 765 C C . PHE A 1 99 ? 12.316 -17.506 59.709 1.00 18.13 ? 99 PHE A C 1 ATOM 766 O O . PHE A 1 99 ? 12.839 -17.528 60.825 1.00 17.70 ? 99 PHE A O 1 ATOM 767 C CB . PHE A 1 99 ? 13.743 -15.512 59.318 1.00 15.72 ? 99 PHE A CB 1 ATOM 768 C CG . PHE A 1 99 ? 14.202 -14.419 58.395 1.00 14.66 ? 99 PHE A CG 1 ATOM 769 C CD1 . PHE A 1 99 ? 14.174 -13.088 58.805 1.00 15.03 ? 99 PHE A CD1 1 ATOM 770 C CD2 . PHE A 1 99 ? 14.672 -14.719 57.116 1.00 15.92 ? 99 PHE A CD2 1 ATOM 771 C CE1 . PHE A 1 99 ? 14.608 -12.066 57.953 1.00 14.25 ? 99 PHE A CE1 1 ATOM 772 C CE2 . PHE A 1 99 ? 15.110 -13.704 56.254 1.00 14.93 ? 99 PHE A CE2 1 ATOM 773 C CZ . PHE A 1 99 ? 15.078 -12.376 56.677 1.00 14.96 ? 99 PHE A CZ 1 ATOM 774 N N . LYS A 1 100 ? 11.395 -18.383 59.335 1.00 18.97 ? 100 LYS A N 1 ATOM 775 C CA . LYS A 1 100 ? 11.024 -19.443 60.242 1.00 21.20 ? 100 LYS A CA 1 ATOM 776 C C . LYS A 1 100 ? 12.216 -20.410 60.338 1.00 20.91 ? 100 LYS A C 1 ATOM 777 O O . LYS A 1 100 ? 13.098 -20.418 59.471 1.00 22.54 ? 100 LYS A O 1 ATOM 778 C CB . LYS A 1 100 ? 9.733 -20.114 59.765 1.00 23.10 ? 100 LYS A CB 1 ATOM 779 C CG . LYS A 1 100 ? 8.533 -19.203 60.007 1.00 25.02 ? 100 LYS A CG 1 ATOM 780 C CD . LYS A 1 100 ? 7.206 -19.881 59.772 1.00 27.53 ? 100 LYS A CD 1 ATOM 781 C CE . LYS A 1 100 ? 6.069 -19.038 60.327 1.00 27.06 ? 100 LYS A CE 1 ATOM 782 N NZ . LYS A 1 100 ? 6.227 -18.809 61.796 1.00 27.55 ? 100 LYS A NZ 1 ATOM 783 N N . ASN A 1 101 ? 12.254 -21.191 61.412 1.00 19.69 ? 101 ASN A N 1 ATOM 784 C CA . ASN A 1 101 ? 13.344 -22.120 61.682 1.00 19.11 ? 101 ASN A CA 1 ATOM 785 C C . ASN A 1 101 ? 14.685 -21.405 61.861 1.00 17.61 ? 101 ASN A C 1 ATOM 786 O O . ASN A 1 101 ? 15.694 -21.759 61.251 1.00 19.02 ? 101 ASN A O 1 ATOM 787 C CB . ASN A 1 101 ? 13.462 -23.209 60.605 1.00 20.89 ? 101 ASN A CB 1 ATOM 788 C CG . ASN A 1 101 ? 14.473 -24.297 60.985 1.00 20.88 ? 101 ASN A CG 1 ATOM 789 O OD1 . ASN A 1 101 ? 14.661 -24.608 62.169 1.00 18.65 ? 101 ASN A OD1 1 ATOM 790 N ND2 . ASN A 1 101 ? 15.115 -24.884 59.980 1.00 21.65 ? 101 ASN A ND2 1 ATOM 791 N N . THR A 1 102 ? 14.665 -20.371 62.693 1.00 16.14 ? 102 THR A N 1 ATOM 792 C CA . THR A 1 102 ? 15.861 -19.621 63.056 1.00 14.93 ? 102 THR A CA 1 ATOM 793 C C . THR A 1 102 ? 15.653 -19.283 64.527 1.00 14.66 ? 102 THR A C 1 ATOM 794 O O . THR A 1 102 ? 14.539 -19.377 65.042 1.00 14.81 ? 102 THR A O 1 ATOM 795 C CB . THR A 1 102 ? 16.025 -18.253 62.296 1.00 15.12 ? 102 THR A CB 1 ATOM 796 O OG1 . THR A 1 102 ? 14.888 -17.415 62.540 1.00 13.73 ? 102 THR A OG1 1 ATOM 797 C CG2 . THR A 1 102 ? 16.203 -18.466 60.812 1.00 15.53 ? 102 THR A CG2 1 ATOM 798 N N . ILE A 1 103 ? 16.729 -18.921 65.209 1.00 15.52 ? 103 ILE A N 1 ATOM 799 C CA . ILE A 1 103 ? 16.610 -18.490 66.590 1.00 16.45 ? 103 ILE A CA 1 ATOM 800 C C . ILE A 1 103 ? 16.321 -16.997 66.393 1.00 16.64 ? 103 ILE A C 1 ATOM 801 O O . ILE A 1 103 ? 17.188 -16.261 65.919 1.00 15.86 ? 103 ILE A O 1 ATOM 802 C CB . ILE A 1 103 ? 17.932 -18.699 67.342 1.00 17.52 ? 103 ILE A CB 1 ATOM 803 C CG1 . ILE A 1 103 ? 18.256 -20.196 67.391 1.00 18.66 ? 103 ILE A CG1 1 ATOM 804 C CG2 . ILE A 1 103 ? 17.827 -18.130 68.744 1.00 16.21 ? 103 ILE A CG2 1 ATOM 805 C CD1 . ILE A 1 103 ? 19.696 -20.507 67.725 1.00 21.49 ? 103 ILE A CD1 1 ATOM 806 N N . LYS A 1 104 ? 15.099 -16.571 66.725 1.00 16.33 ? 104 LYS A N 1 ATOM 807 C CA . LYS A 1 104 ? 14.664 -15.181 66.544 1.00 16.38 ? 104 LYS A CA 1 ATOM 808 C C . LYS A 1 104 ? 14.894 -14.211 67.686 1.00 17.02 ? 104 LYS A C 1 ATOM 809 O O . LYS A 1 104 ? 14.703 -14.542 68.854 1.00 17.71 ? 104 LYS A O 1 ATOM 810 C CB . LYS A 1 104 ? 13.172 -15.125 66.201 1.00 17.60 ? 104 LYS A CB 1 ATOM 811 C CG . LYS A 1 104 ? 12.829 -15.596 64.814 1.00 20.80 ? 104 LYS A CG 1 ATOM 812 C CD . LYS A 1 104 ? 11.371 -15.329 64.473 1.00 18.11 ? 104 LYS A CD 1 ATOM 813 C CE . LYS A 1 104 ? 11.070 -15.865 63.092 1.00 16.88 ? 104 LYS A CE 1 ATOM 814 N NZ . LYS A 1 104 ? 9.631 -15.816 62.762 1.00 16.86 ? 104 LYS A NZ 1 ATOM 815 N N . THR A 1 105 ? 15.260 -12.986 67.321 1.00 17.04 ? 105 THR A N 1 ATOM 816 C CA . THR A 1 105 ? 15.501 -11.920 68.285 1.00 18.05 ? 105 THR A CA 1 ATOM 817 C C . THR A 1 105 ? 14.918 -10.613 67.773 1.00 16.85 ? 105 THR A C 1 ATOM 818 O O . THR A 1 105 ? 14.955 -10.338 66.571 1.00 15.87 ? 105 THR A O 1 ATOM 819 C CB . THR A 1 105 ? 16.998 -11.668 68.490 1.00 19.41 ? 105 THR A CB 1 ATOM 820 O OG1 . THR A 1 105 ? 17.642 -12.887 68.863 1.00 25.60 ? 105 THR A OG1 1 ATOM 821 C CG2 . THR A 1 105 ? 17.216 -10.624 69.581 1.00 23.86 ? 105 THR A CG2 1 ATOM 822 N N . ARG A 1 106 ? 14.377 -9.810 68.682 1.00 16.32 ? 106 ARG A N 1 ATOM 823 C CA . ARG A 1 106 ? 13.852 -8.507 68.303 1.00 16.88 ? 106 ARG A CA 1 ATOM 824 C C . ARG A 1 106 ? 14.881 -7.502 68.821 1.00 17.02 ? 106 ARG A C 1 ATOM 825 O O . ARG A 1 106 ? 15.193 -7.491 70.015 1.00 16.47 ? 106 ARG A O 1 ATOM 826 C CB . ARG A 1 106 ? 12.478 -8.250 68.941 1.00 17.09 ? 106 ARG A CB 1 ATOM 827 C CG . ARG A 1 106 ? 11.815 -6.967 68.442 1.00 20.24 ? 106 ARG A CG 1 ATOM 828 C CD . ARG A 1 106 ? 10.410 -6.763 68.999 1.00 22.86 ? 106 ARG A CD 1 ATOM 829 N NE . ARG A 1 106 ? 9.358 -7.489 68.275 1.00 26.06 ? 106 ARG A NE 1 ATOM 830 C CZ . ARG A 1 106 ? 8.916 -7.189 67.048 1.00 28.35 ? 106 ARG A CZ 1 ATOM 831 N NH1 . ARG A 1 106 ? 9.426 -6.167 66.359 1.00 27.77 ? 106 ARG A NH1 1 ATOM 832 N NH2 . ARG A 1 106 ? 7.934 -7.903 66.508 1.00 26.87 ? 106 ARG A NH2 1 ATOM 833 N N . LEU A 1 107 ? 15.435 -6.689 67.922 1.00 15.03 ? 107 LEU A N 1 ATOM 834 C CA . LEU A 1 107 ? 16.430 -5.691 68.306 1.00 15.92 ? 107 LEU A CA 1 ATOM 835 C C . LEU A 1 107 ? 15.781 -4.652 69.224 1.00 16.00 ? 107 LEU A C 1 ATOM 836 O O . LEU A 1 107 ? 14.555 -4.483 69.226 1.00 15.36 ? 107 LEU A O 1 ATOM 837 C CB . LEU A 1 107 ? 17.017 -5.008 67.059 1.00 14.98 ? 107 LEU A CB 1 ATOM 838 C CG . LEU A 1 107 ? 17.790 -5.899 66.068 1.00 15.13 ? 107 LEU A CG 1 ATOM 839 C CD1 . LEU A 1 107 ? 18.064 -5.140 64.762 1.00 13.21 ? 107 LEU A CD1 1 ATOM 840 C CD2 . LEU A 1 107 ? 19.092 -6.350 66.700 1.00 14.51 ? 107 LEU A CD2 1 ATOM 841 N N . HIS A 1 108 ? 16.605 -3.963 70.004 1.00 15.86 ? 108 HIS A N 1 ATOM 842 C CA . HIS A 1 108 ? 16.110 -2.961 70.935 1.00 17.12 ? 108 HIS A CA 1 ATOM 843 C C . HIS A 1 108 ? 16.120 -1.557 70.360 1.00 17.37 ? 108 HIS A C 1 ATOM 844 O O . HIS A 1 108 ? 16.093 -0.572 71.095 1.00 18.80 ? 108 HIS A O 1 ATOM 845 C CB . HIS A 1 108 ? 16.928 -3.016 72.223 1.00 19.70 ? 108 HIS A CB 1 ATOM 846 C CG . HIS A 1 108 ? 16.762 -4.300 72.972 1.00 24.84 ? 108 HIS A CG 1 ATOM 847 N ND1 . HIS A 1 108 ? 17.485 -4.604 74.104 1.00 29.82 ? 108 HIS A ND1 1 ATOM 848 C CD2 . HIS A 1 108 ? 15.940 -5.355 72.756 1.00 27.98 ? 108 HIS A CD2 1 ATOM 849 C CE1 . HIS A 1 108 ? 17.117 -5.792 74.552 1.00 29.58 ? 108 HIS A CE1 1 ATOM 850 N NE2 . HIS A 1 108 ? 16.182 -6.269 73.751 1.00 28.20 ? 108 HIS A NE2 1 ATOM 851 N N . PHE A 1 109 ? 16.169 -1.466 69.039 1.00 15.28 ? 109 PHE A N 1 ATOM 852 C CA . PHE A 1 109 ? 16.146 -0.172 68.377 1.00 14.56 ? 109 PHE A CA 1 ATOM 853 C C . PHE A 1 109 ? 15.365 -0.281 67.072 1.00 13.99 ? 109 PHE A C 1 ATOM 854 O O . PHE A 1 109 ? 15.241 -1.366 66.499 1.00 13.83 ? 109 PHE A O 1 ATOM 855 C CB . PHE A 1 109 ? 17.576 0.346 68.138 1.00 14.27 ? 109 PHE A CB 1 ATOM 856 C CG . PHE A 1 109 ? 18.474 -0.612 67.385 1.00 15.06 ? 109 PHE A CG 1 ATOM 857 C CD1 . PHE A 1 109 ? 18.577 -0.553 65.994 1.00 15.56 ? 109 PHE A CD1 1 ATOM 858 C CD2 . PHE A 1 109 ? 19.261 -1.539 68.074 1.00 15.00 ? 109 PHE A CD2 1 ATOM 859 C CE1 . PHE A 1 109 ? 19.452 -1.393 65.304 1.00 14.66 ? 109 PHE A CE1 1 ATOM 860 C CE2 . PHE A 1 109 ? 20.141 -2.386 67.394 1.00 14.59 ? 109 PHE A CE2 1 ATOM 861 C CZ . PHE A 1 109 ? 20.238 -2.312 66.007 1.00 15.02 ? 109 PHE A CZ 1 ATOM 862 N N . GLY A 1 110 ? 14.812 0.839 66.625 1.00 13.33 ? 110 GLY A N 1 ATOM 863 C CA . GLY A 1 110 ? 14.044 0.836 65.398 1.00 14.47 ? 110 GLY A CA 1 ATOM 864 C C . GLY A 1 110 ? 14.942 1.017 64.197 1.00 14.14 ? 110 GLY A C 1 ATOM 865 O O . GLY A 1 110 ? 16.139 1.259 64.343 1.00 13.42 ? 110 GLY A O 1 ATOM 866 N N . GLY A 1 111 ? 14.357 0.903 63.008 1.00 15.38 ? 111 GLY A N 1 ATOM 867 C CA . GLY A 1 111 ? 15.116 1.052 61.778 1.00 15.21 ? 111 GLY A CA 1 ATOM 868 C C . GLY A 1 111 ? 15.059 2.430 61.141 1.00 14.92 ? 111 GLY A C 1 ATOM 869 O O . GLY A 1 111 ? 15.635 2.635 60.080 1.00 14.79 ? 111 GLY A O 1 ATOM 870 N N . SER A 1 112 ? 14.375 3.383 61.769 1.00 14.78 ? 112 SER A N 1 ATOM 871 C CA . SER A 1 112 ? 14.300 4.726 61.198 1.00 13.59 ? 112 SER A CA 1 ATOM 872 C C . SER A 1 112 ? 15.675 5.349 61.375 1.00 12.84 ? 112 SER A C 1 ATOM 873 O O . SER A 1 112 ? 16.453 4.898 62.219 1.00 12.22 ? 112 SER A O 1 ATOM 874 C CB . SER A 1 112 ? 13.246 5.575 61.928 1.00 14.43 ? 112 SER A CB 1 ATOM 875 O OG . SER A 1 112 ? 13.700 5.985 63.211 1.00 14.56 ? 112 SER A OG 1 ATOM 876 N N . TYR A 1 113 ? 15.985 6.375 60.588 1.00 12.80 ? 113 TYR A N 1 ATOM 877 C CA . TYR A 1 113 ? 17.288 7.025 60.713 1.00 14.00 ? 113 TYR A CA 1 ATOM 878 C C . TYR A 1 113 ? 17.532 7.588 62.120 1.00 14.40 ? 113 TYR A C 1 ATOM 879 O O . TYR A 1 113 ? 18.618 7.412 62.681 1.00 13.96 ? 113 TYR A O 1 ATOM 880 C CB . TYR A 1 113 ? 17.450 8.100 59.633 1.00 13.23 ? 113 TYR A CB 1 ATOM 881 C CG . TYR A 1 113 ? 17.615 7.484 58.262 1.00 14.53 ? 113 TYR A CG 1 ATOM 882 C CD1 . TYR A 1 113 ? 18.605 6.519 58.035 1.00 14.31 ? 113 TYR A CD1 1 ATOM 883 C CD2 . TYR A 1 113 ? 16.764 7.825 57.204 1.00 13.34 ? 113 TYR A CD2 1 ATOM 884 C CE1 . TYR A 1 113 ? 18.745 5.898 56.787 1.00 14.46 ? 113 TYR A CE1 1 ATOM 885 C CE2 . TYR A 1 113 ? 16.894 7.212 55.944 1.00 13.64 ? 113 TYR A CE2 1 ATOM 886 C CZ . TYR A 1 113 ? 17.889 6.249 55.748 1.00 14.62 ? 113 TYR A CZ 1 ATOM 887 O OH . TYR A 1 113 ? 18.042 5.639 54.525 1.00 14.27 ? 113 TYR A OH 1 ATOM 888 N N . PRO A 1 114 ? 16.533 8.272 62.711 1.00 14.67 ? 114 PRO A N 1 ATOM 889 C CA . PRO A 1 114 ? 16.775 8.792 64.062 1.00 15.23 ? 114 PRO A CA 1 ATOM 890 C C . PRO A 1 114 ? 16.944 7.658 65.093 1.00 14.18 ? 114 PRO A C 1 ATOM 891 O O . PRO A 1 114 ? 17.663 7.809 66.083 1.00 14.55 ? 114 PRO A O 1 ATOM 892 C CB . PRO A 1 114 ? 15.555 9.684 64.326 1.00 15.42 ? 114 PRO A CB 1 ATOM 893 C CG . PRO A 1 114 ? 14.510 9.167 63.385 1.00 20.17 ? 114 PRO A CG 1 ATOM 894 C CD . PRO A 1 114 ? 15.287 8.818 62.148 1.00 15.75 ? 114 PRO A CD 1 ATOM 895 N N . SER A 1 115 ? 16.297 6.519 64.863 1.00 13.21 ? 115 SER A N 1 ATOM 896 C CA . SER A 1 115 ? 16.452 5.394 65.783 1.00 13.51 ? 115 SER A CA 1 ATOM 897 C C . SER A 1 115 ? 17.864 4.818 65.636 1.00 14.18 ? 115 SER A C 1 ATOM 898 O O . SER A 1 115 ? 18.497 4.443 66.632 1.00 14.27 ? 115 SER A O 1 ATOM 899 C CB . SER A 1 115 ? 15.414 4.304 65.501 1.00 14.24 ? 115 SER A CB 1 ATOM 900 O OG . SER A 1 115 ? 14.118 4.752 65.851 1.00 18.11 ? 115 SER A OG 1 ATOM 901 N N . LEU A 1 116 ? 18.364 4.749 64.400 1.00 13.07 ? 116 LEU A N 1 ATOM 902 C CA . LEU A 1 116 ? 19.710 4.224 64.172 1.00 13.00 ? 116 LEU A CA 1 ATOM 903 C C . LEU A 1 116 ? 20.743 5.176 64.772 1.00 13.42 ? 116 LEU A C 1 ATOM 904 O O . LEU A 1 116 ? 21.795 4.738 65.235 1.00 14.17 ? 116 LEU A O 1 ATOM 905 C CB . LEU A 1 116 ? 19.975 4.007 62.671 1.00 12.84 ? 116 LEU A CB 1 ATOM 906 C CG . LEU A 1 116 ? 19.219 2.820 62.048 1.00 13.26 ? 116 LEU A CG 1 ATOM 907 C CD1 . LEU A 1 116 ? 19.266 2.885 60.532 1.00 12.68 ? 116 LEU A CD1 1 ATOM 908 C CD2 . LEU A 1 116 ? 19.822 1.506 62.547 1.00 14.46 ? 116 LEU A CD2 1 ATOM 909 N N . GLU A 1 117 ? 20.444 6.474 64.777 1.00 13.64 ? 117 GLU A N 1 ATOM 910 C CA . GLU A 1 117 ? 21.366 7.454 65.358 1.00 14.74 ? 117 GLU A CA 1 ATOM 911 C C . GLU A 1 117 ? 21.466 7.203 66.851 1.00 15.54 ? 117 GLU A C 1 ATOM 912 O O . GLU A 1 117 ? 22.486 7.496 67.477 1.00 16.40 ? 117 GLU A O 1 ATOM 913 C CB . GLU A 1 117 ? 20.873 8.879 65.109 1.00 14.49 ? 117 GLU A CB 1 ATOM 914 C CG . GLU A 1 117 ? 21.012 9.292 63.665 1.00 15.51 ? 117 GLU A CG 1 ATOM 915 C CD . GLU A 1 117 ? 20.485 10.678 63.392 1.00 17.68 ? 117 GLU A CD 1 ATOM 916 O OE1 . GLU A 1 117 ? 19.829 11.251 64.290 1.00 17.97 ? 117 GLU A OE1 1 ATOM 917 O OE2 . GLU A 1 117 ? 20.720 11.187 62.270 1.00 18.73 ? 117 GLU A OE2 1 ATOM 918 N N . GLY A 1 118 ? 20.394 6.659 67.417 1.00 15.32 ? 118 GLY A N 1 ATOM 919 C CA . GLY A 1 118 ? 20.387 6.353 68.835 1.00 16.12 ? 118 GLY A CA 1 ATOM 920 C C . GLY A 1 118 ? 21.424 5.287 69.126 1.00 16.74 ? 118 GLY A C 1 ATOM 921 O O . GLY A 1 118 ? 21.901 5.168 70.258 1.00 16.96 ? 118 GLY A O 1 ATOM 922 N N . GLU A 1 119 ? 21.768 4.506 68.101 1.00 16.29 ? 119 GLU A N 1 ATOM 923 C CA . GLU A 1 119 ? 22.765 3.448 68.235 1.00 16.41 ? 119 GLU A CA 1 ATOM 924 C C . GLU A 1 119 ? 24.083 3.891 67.634 1.00 15.50 ? 119 GLU A C 1 ATOM 925 O O . GLU A 1 119 ? 24.891 3.066 67.213 1.00 15.31 ? 119 GLU A O 1 ATOM 926 C CB . GLU A 1 119 ? 22.302 2.157 67.556 1.00 18.37 ? 119 GLU A CB 1 ATOM 927 C CG . GLU A 1 119 ? 21.085 1.524 68.207 1.00 23.10 ? 119 GLU A CG 1 ATOM 928 C CD . GLU A 1 119 ? 21.180 1.490 69.729 1.00 26.65 ? 119 GLU A CD 1 ATOM 929 O OE1 . GLU A 1 119 ? 22.179 0.945 70.262 1.00 26.57 ? 119 GLU A OE1 1 ATOM 930 O OE2 . GLU A 1 119 ? 20.246 2.014 70.387 1.00 28.42 ? 119 GLU A OE2 1 ATOM 931 N N . LYS A 1 120 ? 24.270 5.207 67.581 1.00 15.09 ? 120 LYS A N 1 ATOM 932 C CA . LYS A 1 120 ? 25.490 5.837 67.075 1.00 15.91 ? 120 LYS A CA 1 ATOM 933 C C . LYS A 1 120 ? 25.750 5.737 65.566 1.00 15.19 ? 120 LYS A C 1 ATOM 934 O O . LYS A 1 120 ? 26.844 6.058 65.101 1.00 14.53 ? 120 LYS A O 1 ATOM 935 C CB . LYS A 1 120 ? 26.706 5.300 67.849 1.00 17.93 ? 120 LYS A CB 1 ATOM 936 C CG . LYS A 1 120 ? 26.539 5.339 69.370 1.00 21.66 ? 120 LYS A CG 1 ATOM 937 C CD . LYS A 1 120 ? 27.829 4.956 70.085 1.00 27.34 ? 120 LYS A CD 1 ATOM 938 C CE . LYS A 1 120 ? 27.588 4.676 71.570 1.00 31.88 ? 120 LYS A CE 1 ATOM 939 N NZ . LYS A 1 120 ? 26.946 5.816 72.299 1.00 36.49 ? 120 LYS A NZ 1 ATOM 940 N N . ALA A 1 121 ? 24.751 5.309 64.799 1.00 14.53 ? 121 ALA A N 1 ATOM 941 C CA . ALA A 1 121 ? 24.912 5.197 63.351 1.00 13.59 ? 121 ALA A CA 1 ATOM 942 C C . ALA A 1 121 ? 24.279 6.416 62.673 1.00 12.65 ? 121 ALA A C 1 ATOM 943 O O . ALA A 1 121 ? 23.057 6.509 62.554 1.00 12.42 ? 121 ALA A O 1 ATOM 944 C CB . ALA A 1 121 ? 24.264 3.899 62.847 1.00 12.75 ? 121 ALA A CB 1 ATOM 945 N N . TYR A 1 122 ? 25.123 7.347 62.243 1.00 12.71 ? 122 TYR A N 1 ATOM 946 C CA . TYR A 1 122 ? 24.678 8.575 61.587 1.00 13.87 ? 122 TYR A CA 1 ATOM 947 C C . TYR A 1 122 ? 24.995 8.556 60.096 1.00 14.48 ? 122 TYR A C 1 ATOM 948 O O . TYR A 1 122 ? 26.108 8.211 59.696 1.00 14.35 ? 122 TYR A O 1 ATOM 949 C CB . TYR A 1 122 ? 25.374 9.786 62.216 1.00 12.83 ? 122 TYR A CB 1 ATOM 950 C CG . TYR A 1 122 ? 25.029 10.005 63.666 1.00 14.58 ? 122 TYR A CG 1 ATOM 951 C CD1 . TYR A 1 122 ? 24.019 10.886 64.029 1.00 15.98 ? 122 TYR A CD1 1 ATOM 952 C CD2 . TYR A 1 122 ? 25.704 9.316 64.680 1.00 16.08 ? 122 TYR A CD2 1 ATOM 953 C CE1 . TYR A 1 122 ? 23.682 11.085 65.365 1.00 16.95 ? 122 TYR A CE1 1 ATOM 954 C CE2 . TYR A 1 122 ? 25.373 9.506 66.026 1.00 16.60 ? 122 TYR A CE2 1 ATOM 955 C CZ . TYR A 1 122 ? 24.359 10.395 66.357 1.00 17.02 ? 122 TYR A CZ 1 ATOM 956 O OH . TYR A 1 122 ? 24.012 10.607 67.674 1.00 18.27 ? 122 TYR A OH 1 ATOM 957 N N . ARG A 1 123 ? 24.027 8.945 59.275 1.00 13.37 ? 123 ARG A N 1 ATOM 958 C CA . ARG A 1 123 ? 24.243 8.972 57.835 1.00 15.80 ? 123 ARG A CA 1 ATOM 959 C C . ARG A 1 123 ? 25.443 9.833 57.448 1.00 15.78 ? 123 ARG A C 1 ATOM 960 O O . ARG A 1 123 ? 26.210 9.479 56.554 1.00 16.07 ? 123 ARG A O 1 ATOM 961 C CB . ARG A 1 123 ? 22.997 9.498 57.120 1.00 14.76 ? 123 ARG A CB 1 ATOM 962 C CG . ARG A 1 123 ? 21.930 8.451 56.903 1.00 12.78 ? 123 ARG A CG 1 ATOM 963 C CD . ARG A 1 123 ? 20.692 9.056 56.277 1.00 12.98 ? 123 ARG A CD 1 ATOM 964 N NE . ARG A 1 123 ? 19.937 9.860 57.232 1.00 11.23 ? 123 ARG A NE 1 ATOM 965 C CZ . ARG A 1 123 ? 18.824 10.520 56.929 1.00 11.52 ? 123 ARG A CZ 1 ATOM 966 N NH1 . ARG A 1 123 ? 18.345 10.474 55.691 1.00 10.65 ? 123 ARG A NH1 1 ATOM 967 N NH2 . ARG A 1 123 ? 18.179 11.208 57.865 1.00 11.39 ? 123 ARG A NH2 1 ATOM 968 N N . GLU A 1 124 ? 25.603 10.963 58.126 1.00 17.50 ? 124 GLU A N 1 ATOM 969 C CA . GLU A 1 124 ? 26.694 11.880 57.822 1.00 19.94 ? 124 GLU A CA 1 ATOM 970 C C . GLU A 1 124 ? 28.097 11.312 58.058 1.00 20.10 ? 124 GLU A C 1 ATOM 971 O O . GLU A 1 124 ? 29.055 11.766 57.434 1.00 20.34 ? 124 GLU A O 1 ATOM 972 C CB . GLU A 1 124 ? 26.522 13.179 58.621 1.00 22.98 ? 124 GLU A CB 1 ATOM 973 C CG . GLU A 1 124 ? 26.213 12.964 60.097 1.00 29.58 ? 124 GLU A CG 1 ATOM 974 C CD . GLU A 1 124 ? 24.716 13.019 60.413 1.00 32.17 ? 124 GLU A CD 1 ATOM 975 O OE1 . GLU A 1 124 ? 23.909 12.418 59.668 1.00 30.62 ? 124 GLU A OE1 1 ATOM 976 O OE2 . GLU A 1 124 ? 24.352 13.663 61.426 1.00 34.70 ? 124 GLU A OE2 1 ATOM 977 N N . THR A 1 125 ? 28.225 10.320 58.937 1.00 18.77 ? 125 THR A N 1 ATOM 978 C CA . THR A 1 125 ? 29.537 9.747 59.229 1.00 18.19 ? 125 THR A CA 1 ATOM 979 C C . THR A 1 125 ? 29.681 8.262 58.901 1.00 18.49 ? 125 THR A C 1 ATOM 980 O O . THR A 1 125 ? 30.598 7.597 59.383 1.00 19.42 ? 125 THR A O 1 ATOM 981 C CB . THR A 1 125 ? 29.896 9.954 60.710 1.00 19.11 ? 125 THR A CB 1 ATOM 982 O OG1 . THR A 1 125 ? 28.879 9.373 61.534 1.00 19.80 ? 125 THR A OG1 1 ATOM 983 C CG2 . THR A 1 125 ? 29.998 11.430 61.027 1.00 19.22 ? 125 THR A CG2 1 ATOM 984 N N . THR A 1 126 ? 28.777 7.739 58.083 1.00 17.34 ? 126 THR A N 1 ATOM 985 C CA . THR A 1 126 ? 28.822 6.333 57.704 1.00 16.91 ? 126 THR A CA 1 ATOM 986 C C . THR A 1 126 ? 29.195 6.189 56.225 1.00 16.70 ? 126 THR A C 1 ATOM 987 O O . THR A 1 126 ? 28.448 6.593 55.335 1.00 14.46 ? 126 THR A O 1 ATOM 988 C CB . THR A 1 126 ? 27.453 5.642 57.991 1.00 17.56 ? 126 THR A CB 1 ATOM 989 O OG1 . THR A 1 126 ? 27.213 5.640 59.404 1.00 17.61 ? 126 THR A OG1 1 ATOM 990 C CG2 . THR A 1 126 ? 27.449 4.196 57.493 1.00 17.27 ? 126 THR A CG2 1 ATOM 991 N N . ASP A 1 127 ? 30.376 5.630 55.978 1.00 16.79 ? 127 ASP A N 1 ATOM 992 C CA . ASP A 1 127 ? 30.870 5.415 54.625 1.00 17.53 ? 127 ASP A CA 1 ATOM 993 C C . ASP A 1 127 ? 29.995 4.441 53.849 1.00 16.44 ? 127 ASP A C 1 ATOM 994 O O . ASP A 1 127 ? 29.462 3.484 54.417 1.00 16.91 ? 127 ASP A O 1 ATOM 995 C CB . ASP A 1 127 ? 32.285 4.837 54.665 1.00 18.46 ? 127 ASP A CB 1 ATOM 996 C CG . ASP A 1 127 ? 33.318 5.848 55.093 1.00 22.68 ? 127 ASP A CG 1 ATOM 997 O OD1 . ASP A 1 127 ? 34.462 5.433 55.390 1.00 23.18 ? 127 ASP A OD1 1 ATOM 998 O OD2 . ASP A 1 127 ? 32.989 7.053 55.121 1.00 23.47 ? 127 ASP A OD2 1 ATOM 999 N N . LEU A 1 128 ? 29.867 4.684 52.548 1.00 15.73 ? 128 LEU A N 1 ATOM 1000 C CA . LEU A 1 128 ? 29.105 3.813 51.665 1.00 14.54 ? 128 LEU A CA 1 ATOM 1001 C C . LEU A 1 128 ? 30.033 3.433 50.515 1.00 14.78 ? 128 LEU A C 1 ATOM 1002 O O . LEU A 1 128 ? 30.923 4.204 50.148 1.00 15.02 ? 128 LEU A O 1 ATOM 1003 C CB . LEU A 1 128 ? 27.867 4.530 51.117 1.00 15.48 ? 128 LEU A CB 1 ATOM 1004 C CG . LEU A 1 128 ? 26.844 5.066 52.130 1.00 17.04 ? 128 LEU A CG 1 ATOM 1005 C CD1 . LEU A 1 128 ? 25.740 5.792 51.379 1.00 14.87 ? 128 LEU A CD1 1 ATOM 1006 C CD2 . LEU A 1 128 ? 26.271 3.926 52.971 1.00 13.97 ? 128 LEU A CD2 1 ATOM 1007 N N . GLY A 1 129 ? 29.822 2.248 49.951 1.00 13.95 ? 129 GLY A N 1 ATOM 1008 C CA . GLY A 1 129 ? 30.656 1.781 48.858 1.00 14.15 ? 129 GLY A CA 1 ATOM 1009 C C . GLY A 1 129 ? 30.774 0.274 48.945 1.00 15.29 ? 129 GLY A C 1 ATOM 1010 O O . GLY A 1 129 ? 30.199 -0.333 49.847 1.00 14.83 ? 129 GLY A O 1 ATOM 1011 N N . ILE A 1 130 ? 31.515 -0.343 48.030 1.00 14.70 ? 130 ILE A N 1 ATOM 1012 C CA . ILE A 1 130 ? 31.640 -1.795 48.065 1.00 15.18 ? 130 ILE A CA 1 ATOM 1013 C C . ILE A 1 130 ? 32.393 -2.302 49.306 1.00 15.52 ? 130 ILE A C 1 ATOM 1014 O O . ILE A 1 130 ? 32.019 -3.330 49.869 1.00 16.18 ? 130 ILE A O 1 ATOM 1015 C CB . ILE A 1 130 ? 32.297 -2.348 46.757 1.00 14.98 ? 130 ILE A CB 1 ATOM 1016 C CG1 . ILE A 1 130 ? 32.155 -3.870 46.715 1.00 14.70 ? 130 ILE A CG1 1 ATOM 1017 C CG2 . ILE A 1 130 ? 33.753 -1.945 46.673 1.00 14.29 ? 130 ILE A CG2 1 ATOM 1018 C CD1 . ILE A 1 130 ? 30.711 -4.345 46.764 1.00 15.30 ? 130 ILE A CD1 1 ATOM 1019 N N . GLU A 1 131 ? 33.433 -1.595 49.746 1.00 15.27 ? 131 GLU A N 1 ATOM 1020 C CA . GLU A 1 131 ? 34.157 -2.040 50.941 1.00 17.35 ? 131 GLU A CA 1 ATOM 1021 C C . GLU A 1 131 ? 33.266 -1.922 52.174 1.00 16.91 ? 131 GLU A C 1 ATOM 1022 O O . GLU A 1 131 ? 33.176 -2.855 52.973 1.00 16.11 ? 131 GLU A O 1 ATOM 1023 C CB . GLU A 1 131 ? 35.438 -1.241 51.145 1.00 19.60 ? 131 GLU A CB 1 ATOM 1024 C CG . GLU A 1 131 ? 36.657 -1.959 50.640 1.00 26.24 ? 131 GLU A CG 1 ATOM 1025 C CD . GLU A 1 131 ? 36.796 -3.346 51.244 1.00 29.18 ? 131 GLU A CD 1 ATOM 1026 O OE1 . GLU A 1 131 ? 36.976 -3.447 52.478 1.00 31.26 ? 131 GLU A OE1 1 ATOM 1027 O OE2 . GLU A 1 131 ? 36.719 -4.334 50.481 1.00 30.03 ? 131 GLU A OE2 1 ATOM 1028 N N . PRO A 1 132 ? 32.617 -0.759 52.365 1.00 17.00 ? 132 PRO A N 1 ATOM 1029 C CA . PRO A 1 132 ? 31.735 -0.607 53.525 1.00 15.22 ? 132 PRO A CA 1 ATOM 1030 C C . PRO A 1 132 ? 30.652 -1.694 53.516 1.00 13.89 ? 132 PRO A C 1 ATOM 1031 O O . PRO A 1 132 ? 30.199 -2.134 54.571 1.00 13.57 ? 132 PRO A O 1 ATOM 1032 C CB . PRO A 1 132 ? 31.163 0.789 53.327 1.00 15.27 ? 132 PRO A CB 1 ATOM 1033 C CG . PRO A 1 132 ? 32.340 1.524 52.769 1.00 15.60 ? 132 PRO A CG 1 ATOM 1034 C CD . PRO A 1 132 ? 32.874 0.553 51.735 1.00 16.97 ? 132 PRO A CD 1 ATOM 1035 N N . LEU A 1 133 ? 30.248 -2.131 52.323 1.00 13.70 ? 133 LEU A N 1 ATOM 1036 C CA . LEU A 1 133 ? 29.231 -3.172 52.211 1.00 13.71 ? 133 LEU A CA 1 ATOM 1037 C C . LEU A 1 133 ? 29.805 -4.523 52.638 1.00 14.65 ? 133 LEU A C 1 ATOM 1038 O O . LEU A 1 133 ? 29.149 -5.280 53.351 1.00 15.00 ? 133 LEU A O 1 ATOM 1039 C CB . LEU A 1 133 ? 28.684 -3.259 50.782 1.00 12.74 ? 133 LEU A CB 1 ATOM 1040 C CG . LEU A 1 133 ? 27.562 -4.298 50.597 1.00 12.52 ? 133 LEU A CG 1 ATOM 1041 C CD1 . LEU A 1 133 ? 26.383 -3.980 51.508 1.00 14.17 ? 133 LEU A CD1 1 ATOM 1042 C CD2 . LEU A 1 133 ? 27.106 -4.314 49.150 1.00 14.84 ? 133 LEU A CD2 1 ATOM 1043 N N . ARG A 1 134 ? 31.026 -4.826 52.202 1.00 15.38 ? 134 ARG A N 1 ATOM 1044 C CA . ARG A 1 134 ? 31.686 -6.084 52.577 1.00 16.27 ? 134 ARG A CA 1 ATOM 1045 C C . ARG A 1 134 ? 31.845 -6.168 54.096 1.00 15.49 ? 134 ARG A C 1 ATOM 1046 O O . ARG A 1 134 ? 31.607 -7.211 54.703 1.00 15.40 ? 134 ARG A O 1 ATOM 1047 C CB . ARG A 1 134 ? 33.078 -6.178 51.939 1.00 16.38 ? 134 ARG A CB 1 ATOM 1048 C CG . ARG A 1 134 ? 33.066 -6.323 50.440 1.00 17.80 ? 134 ARG A CG 1 ATOM 1049 C CD . ARG A 1 134 ? 34.471 -6.495 49.901 1.00 19.66 ? 134 ARG A CD 1 ATOM 1050 N NE . ARG A 1 134 ? 34.442 -6.880 48.493 1.00 22.12 ? 134 ARG A NE 1 ATOM 1051 C CZ . ARG A 1 134 ? 34.929 -6.141 47.503 1.00 22.80 ? 134 ARG A CZ 1 ATOM 1052 N NH1 . ARG A 1 134 ? 35.495 -4.969 47.764 1.00 21.29 ? 134 ARG A NH1 1 ATOM 1053 N NH2 . ARG A 1 134 ? 34.832 -6.570 46.249 1.00 22.54 ? 134 ARG A NH2 1 ATOM 1054 N N . ILE A 1 135 ? 32.267 -5.061 54.696 1.00 14.87 ? 135 ILE A N 1 ATOM 1055 C CA . ILE A 1 135 ? 32.468 -4.989 56.137 1.00 15.66 ? 135 ILE A CA 1 ATOM 1056 C C . ILE A 1 135 ? 31.135 -5.096 56.884 1.00 15.77 ? 135 ILE A C 1 ATOM 1057 O O . ILE A 1 135 ? 31.050 -5.735 57.935 1.00 15.70 ? 135 ILE A O 1 ATOM 1058 C CB . ILE A 1 135 ? 33.182 -3.670 56.510 1.00 15.47 ? 135 ILE A CB 1 ATOM 1059 C CG1 . ILE A 1 135 ? 34.579 -3.659 55.882 1.00 16.09 ? 135 ILE A CG1 1 ATOM 1060 C CG2 . ILE A 1 135 ? 33.266 -3.519 58.020 1.00 14.15 ? 135 ILE A CG2 1 ATOM 1061 C CD1 . ILE A 1 135 ? 35.266 -2.315 55.930 1.00 17.72 ? 135 ILE A CD1 1 ATOM 1062 N N . GLY A 1 136 ? 30.098 -4.466 56.338 1.00 15.85 ? 136 GLY A N 1 ATOM 1063 C CA . GLY A 1 136 ? 28.784 -4.529 56.957 1.00 14.37 ? 136 GLY A CA 1 ATOM 1064 C C . GLY A 1 136 ? 28.275 -5.959 56.995 1.00 14.27 ? 136 GLY A C 1 ATOM 1065 O O . GLY A 1 136 ? 27.754 -6.414 58.013 1.00 14.60 ? 136 GLY A O 1 ATOM 1066 N N . ILE A 1 137 ? 28.414 -6.669 55.879 1.00 13.34 ? 137 ILE A N 1 ATOM 1067 C CA . ILE A 1 137 ? 27.986 -8.059 55.811 1.00 14.11 ? 137 ILE A CA 1 ATOM 1068 C C . ILE A 1 137 ? 28.779 -8.849 56.852 1.00 16.07 ? 137 ILE A C 1 ATOM 1069 O O . ILE A 1 137 ? 28.211 -9.611 57.642 1.00 16.63 ? 137 ILE A O 1 ATOM 1070 C CB . ILE A 1 137 ? 28.244 -8.666 54.406 1.00 12.63 ? 137 ILE A CB 1 ATOM 1071 C CG1 . ILE A 1 137 ? 27.362 -7.968 53.365 1.00 12.06 ? 137 ILE A CG1 1 ATOM 1072 C CG2 . ILE A 1 137 ? 27.960 -10.165 54.427 1.00 12.67 ? 137 ILE A CG2 1 ATOM 1073 C CD1 . ILE A 1 137 ? 27.767 -8.230 51.922 1.00 13.20 ? 137 ILE A CD1 1 ATOM 1074 N N . LYS A 1 138 ? 30.094 -8.648 56.858 1.00 16.51 ? 138 LYS A N 1 ATOM 1075 C CA . LYS A 1 138 ? 30.962 -9.340 57.794 1.00 17.20 ? 138 LYS A CA 1 ATOM 1076 C C . LYS A 1 138 ? 30.506 -9.123 59.228 1.00 17.11 ? 138 LYS A C 1 ATOM 1077 O O . LYS A 1 138 ? 30.409 -10.073 60.005 1.00 17.71 ? 138 LYS A O 1 ATOM 1078 C CB . LYS A 1 138 ? 32.399 -8.849 57.639 1.00 20.04 ? 138 LYS A CB 1 ATOM 1079 C CG . LYS A 1 138 ? 33.378 -9.487 58.608 1.00 23.65 ? 138 LYS A CG 1 ATOM 1080 C CD . LYS A 1 138 ? 34.724 -8.798 58.537 1.00 25.67 ? 138 LYS A CD 1 ATOM 1081 C CE . LYS A 1 138 ? 35.705 -9.420 59.503 1.00 29.20 ? 138 LYS A CE 1 ATOM 1082 N NZ . LYS A 1 138 ? 36.908 -8.564 59.634 1.00 32.23 ? 138 LYS A NZ 1 ATOM 1083 N N . LYS A 1 139 ? 30.224 -7.874 59.579 1.00 16.27 ? 139 LYS A N 1 ATOM 1084 C CA . LYS A 1 139 ? 29.793 -7.560 60.933 1.00 18.20 ? 139 LYS A CA 1 ATOM 1085 C C . LYS A 1 139 ? 28.445 -8.175 61.300 1.00 17.85 ? 139 LYS A C 1 ATOM 1086 O O . LYS A 1 139 ? 28.240 -8.575 62.449 1.00 18.87 ? 139 LYS A O 1 ATOM 1087 C CB . LYS A 1 139 ? 29.741 -6.045 61.148 1.00 18.79 ? 139 LYS A CB 1 ATOM 1088 C CG . LYS A 1 139 ? 31.102 -5.379 61.166 1.00 22.55 ? 139 LYS A CG 1 ATOM 1089 C CD . LYS A 1 139 ? 30.958 -3.926 61.571 1.00 28.94 ? 139 LYS A CD 1 ATOM 1090 C CE . LYS A 1 139 ? 32.292 -3.207 61.598 1.00 31.83 ? 139 LYS A CE 1 ATOM 1091 N NZ . LYS A 1 139 ? 32.105 -1.755 61.912 1.00 36.48 ? 139 LYS A NZ 1 ATOM 1092 N N . LEU A 1 140 ? 27.523 -8.249 60.345 1.00 16.44 ? 140 LEU A N 1 ATOM 1093 C CA . LEU A 1 140 ? 26.220 -8.832 60.646 1.00 15.40 ? 140 LEU A CA 1 ATOM 1094 C C . LEU A 1 140 ? 26.411 -10.312 60.963 1.00 16.66 ? 140 LEU A C 1 ATOM 1095 O O . LEU A 1 140 ? 25.757 -10.865 61.852 1.00 16.24 ? 140 LEU A O 1 ATOM 1096 C CB . LEU A 1 140 ? 25.253 -8.661 59.464 1.00 13.47 ? 140 LEU A CB 1 ATOM 1097 C CG . LEU A 1 140 ? 24.756 -7.236 59.193 1.00 13.66 ? 140 LEU A CG 1 ATOM 1098 C CD1 . LEU A 1 140 ? 23.828 -7.252 57.994 1.00 14.25 ? 140 LEU A CD1 1 ATOM 1099 C CD2 . LEU A 1 140 ? 24.026 -6.688 60.410 1.00 12.18 ? 140 LEU A CD2 1 ATOM 1100 N N . ASP A 1 141 ? 27.325 -10.949 60.240 1.00 17.07 ? 141 ASP A N 1 ATOM 1101 C CA . ASP A 1 141 ? 27.585 -12.362 60.463 1.00 18.27 ? 141 ASP A CA 1 ATOM 1102 C C . ASP A 1 141 ? 28.300 -12.575 61.788 1.00 19.22 ? 141 ASP A C 1 ATOM 1103 O O . ASP A 1 141 ? 27.958 -13.484 62.544 1.00 20.86 ? 141 ASP A O 1 ATOM 1104 C CB . ASP A 1 141 ? 28.424 -12.937 59.329 1.00 18.33 ? 141 ASP A CB 1 ATOM 1105 C CG . ASP A 1 141 ? 28.706 -14.410 59.516 1.00 20.01 ? 141 ASP A CG 1 ATOM 1106 O OD1 . ASP A 1 141 ? 29.893 -14.773 59.679 1.00 22.37 ? 141 ASP A OD1 1 ATOM 1107 O OD2 . ASP A 1 141 ? 27.739 -15.201 59.507 1.00 18.46 ? 141 ASP A OD2 1 ATOM 1108 N N . GLU A 1 142 ? 29.293 -11.736 62.068 1.00 19.56 ? 142 GLU A N 1 ATOM 1109 C CA . GLU A 1 142 ? 30.054 -11.831 63.311 1.00 20.63 ? 142 GLU A CA 1 ATOM 1110 C C . GLU A 1 142 ? 29.172 -11.628 64.533 1.00 20.89 ? 142 GLU A C 1 ATOM 1111 O O . GLU A 1 142 ? 29.461 -12.142 65.612 1.00 22.14 ? 142 GLU A O 1 ATOM 1112 C CB . GLU A 1 142 ? 31.170 -10.792 63.334 1.00 21.13 ? 142 GLU A CB 1 ATOM 1113 C CG . GLU A 1 142 ? 32.341 -11.117 62.446 1.00 26.21 ? 142 GLU A CG 1 ATOM 1114 C CD . GLU A 1 142 ? 33.438 -10.073 62.552 1.00 30.04 ? 142 GLU A CD 1 ATOM 1115 O OE1 . GLU A 1 142 ? 34.529 -10.291 61.979 1.00 32.39 ? 142 GLU A OE1 1 ATOM 1116 O OE2 . GLU A 1 142 ? 33.203 -9.030 63.208 1.00 32.58 ? 142 GLU A OE2 1 ATOM 1117 N N . ASN A 1 143 ? 28.101 -10.865 64.371 1.00 20.30 ? 143 ASN A N 1 ATOM 1118 C CA . ASN A 1 143 ? 27.192 -10.614 65.479 1.00 20.44 ? 143 ASN A CA 1 ATOM 1119 C C . ASN A 1 143 ? 25.998 -11.575 65.509 1.00 19.79 ? 143 ASN A C 1 ATOM 1120 O O . ASN A 1 143 ? 24.962 -11.268 66.098 1.00 20.53 ? 143 ASN A O 1 ATOM 1121 C CB . ASN A 1 143 ? 26.716 -9.159 65.435 1.00 20.33 ? 143 ASN A CB 1 ATOM 1122 C CG . ASN A 1 143 ? 27.767 -8.191 65.954 1.00 21.15 ? 143 ASN A CG 1 ATOM 1123 O OD1 . ASN A 1 143 ? 27.970 -8.067 67.165 1.00 21.41 ? 143 ASN A OD1 1 ATOM 1124 N ND2 . ASN A 1 143 ? 28.454 -7.514 65.041 1.00 19.58 ? 143 ASN A ND2 1 ATOM 1125 N N . ALA A 1 144 ? 26.144 -12.734 64.871 1.00 20.22 ? 144 ALA A N 1 ATOM 1126 C CA . ALA A 1 144 ? 25.076 -13.736 64.866 1.00 21.40 ? 144 ALA A CA 1 ATOM 1127 C C . ALA A 1 144 ? 25.275 -14.541 66.140 1.00 22.59 ? 144 ALA A C 1 ATOM 1128 O O . ALA A 1 144 ? 25.540 -15.745 66.095 1.00 21.60 ? 144 ALA A O 1 ATOM 1129 C CB . ALA A 1 144 ? 25.186 -14.644 63.638 1.00 20.96 ? 144 ALA A CB 1 ATOM 1130 N N . ILE A 1 145 ? 25.157 -13.845 67.272 1.00 22.59 ? 145 ILE A N 1 ATOM 1131 C CA . ILE A 1 145 ? 25.339 -14.429 68.596 1.00 24.85 ? 145 ILE A CA 1 ATOM 1132 C C . ILE A 1 145 ? 24.354 -13.815 69.586 1.00 25.95 ? 145 ILE A C 1 ATOM 1133 O O . ILE A 1 145 ? 23.611 -12.895 69.241 1.00 26.76 ? 145 ILE A O 1 ATOM 1134 C CB . ILE A 1 145 ? 26.768 -14.156 69.116 1.00 23.68 ? 145 ILE A CB 1 ATOM 1135 C CG1 . ILE A 1 145 ? 26.986 -12.642 69.222 1.00 23.12 ? 145 ILE A CG1 1 ATOM 1136 C CG2 . ILE A 1 145 ? 27.796 -14.796 68.186 1.00 23.01 ? 145 ILE A CG2 1 ATOM 1137 C CD1 . ILE A 1 145 ? 28.389 -12.229 69.561 1.00 23.01 ? 145 ILE A CD1 1 ATOM 1138 N N . ASP A 1 146 ? 24.364 -14.321 70.817 1.00 28.18 ? 146 ASP A N 1 ATOM 1139 C CA . ASP A 1 146 ? 23.489 -13.823 71.879 1.00 30.38 ? 146 ASP A CA 1 ATOM 1140 C C . ASP A 1 146 ? 23.922 -12.431 72.347 1.00 30.01 ? 146 ASP A C 1 ATOM 1141 O O . ASP A 1 146 ? 23.105 -11.520 72.463 1.00 29.50 ? 146 ASP A O 1 ATOM 1142 C CB . ASP A 1 146 ? 23.515 -14.770 73.084 1.00 35.24 ? 146 ASP A CB 1 ATOM 1143 C CG . ASP A 1 146 ? 23.023 -16.163 72.748 1.00 41.40 ? 146 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 146 ? 21.863 -16.298 72.297 1.00 43.88 ? 146 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 146 ? 23.797 -17.129 72.943 1.00 46.14 ? 146 ASP A OD2 1 ATOM 1146 N N . ASN A 1 147 ? 25.211 -12.283 72.635 1.00 30.08 ? 147 ASN A N 1 ATOM 1147 C CA . ASN A 1 147 ? 25.761 -11.012 73.093 1.00 30.79 ? 147 ASN A CA 1 ATOM 1148 C C . ASN A 1 147 ? 26.285 -10.192 71.920 1.00 28.48 ? 147 ASN A C 1 ATOM 1149 O O . ASN A 1 147 ? 27.480 -9.906 71.823 1.00 28.15 ? 147 ASN A O 1 ATOM 1150 C CB . ASN A 1 147 ? 26.886 -11.265 74.094 1.00 35.02 ? 147 ASN A CB 1 ATOM 1151 C CG . ASN A 1 147 ? 26.376 -11.834 75.403 1.00 40.85 ? 147 ASN A CG 1 ATOM 1152 O OD1 . ASN A 1 147 ? 25.723 -11.135 76.186 1.00 43.57 ? 147 ASN A OD1 1 ATOM 1153 N ND2 . ASN A 1 147 ? 26.661 -13.113 75.645 1.00 42.56 ? 147 ASN A ND2 1 ATOM 1154 N N . TYR A 1 148 ? 25.375 -9.813 71.033 1.00 25.62 ? 148 TYR A N 1 ATOM 1155 C CA . TYR A 1 148 ? 25.734 -9.038 69.861 1.00 23.61 ? 148 TYR A CA 1 ATOM 1156 C C . TYR A 1 148 ? 25.917 -7.566 70.228 1.00 23.25 ? 148 TYR A C 1 ATOM 1157 O O . TYR A 1 148 ? 25.401 -7.099 71.247 1.00 22.49 ? 148 TYR A O 1 ATOM 1158 C CB . TYR A 1 148 ? 24.647 -9.201 68.800 1.00 22.77 ? 148 TYR A CB 1 ATOM 1159 C CG . TYR A 1 148 ? 23.298 -8.686 69.235 1.00 22.31 ? 148 TYR A CG 1 ATOM 1160 C CD1 . TYR A 1 148 ? 23.023 -7.317 69.244 1.00 22.58 ? 148 TYR A CD1 1 ATOM 1161 C CD2 . TYR A 1 148 ? 22.297 -9.562 69.647 1.00 22.53 ? 148 TYR A CD2 1 ATOM 1162 C CE1 . TYR A 1 148 ? 21.785 -6.829 69.651 1.00 23.12 ? 148 TYR A CE1 1 ATOM 1163 C CE2 . TYR A 1 148 ? 21.047 -9.086 70.058 1.00 23.13 ? 148 TYR A CE2 1 ATOM 1164 C CZ . TYR A 1 148 ? 20.800 -7.717 70.057 1.00 24.14 ? 148 TYR A CZ 1 ATOM 1165 O OH . TYR A 1 148 ? 19.572 -7.234 70.459 1.00 25.56 ? 148 TYR A OH 1 ATOM 1166 N N . LYS A 1 149 ? 26.664 -6.844 69.398 1.00 22.09 ? 149 LYS A N 1 ATOM 1167 C CA . LYS A 1 149 ? 26.919 -5.431 69.618 1.00 21.88 ? 149 LYS A CA 1 ATOM 1168 C C . LYS A 1 149 ? 25.959 -4.618 68.761 1.00 21.67 ? 149 LYS A C 1 ATOM 1169 O O . LYS A 1 149 ? 26.108 -4.551 67.545 1.00 21.87 ? 149 LYS A O 1 ATOM 1170 C CB . LYS A 1 149 ? 28.365 -5.095 69.241 1.00 23.38 ? 149 LYS A CB 1 ATOM 1171 C CG . LYS A 1 149 ? 29.386 -5.878 70.034 1.00 26.73 ? 149 LYS A CG 1 ATOM 1172 C CD . LYS A 1 149 ? 30.801 -5.479 69.669 1.00 31.68 ? 149 LYS A CD 1 ATOM 1173 C CE . LYS A 1 149 ? 31.810 -6.329 70.430 1.00 34.68 ? 149 LYS A CE 1 ATOM 1174 N NZ . LYS A 1 149 ? 33.218 -5.983 70.081 1.00 37.97 ? 149 LYS A NZ 1 ATOM 1175 N N . PRO A 1 150 ? 24.956 -3.987 69.386 1.00 21.58 ? 150 PRO A N 1 ATOM 1176 C CA . PRO A 1 150 ? 23.990 -3.187 68.623 1.00 20.66 ? 150 PRO A CA 1 ATOM 1177 C C . PRO A 1 150 ? 24.598 -2.069 67.769 1.00 19.89 ? 150 PRO A C 1 ATOM 1178 O O . PRO A 1 150 ? 24.069 -1.733 66.708 1.00 19.79 ? 150 PRO A O 1 ATOM 1179 C CB . PRO A 1 150 ? 23.045 -2.656 69.707 1.00 20.74 ? 150 PRO A CB 1 ATOM 1180 C CG . PRO A 1 150 ? 23.911 -2.616 70.930 1.00 21.73 ? 150 PRO A CG 1 ATOM 1181 C CD . PRO A 1 150 ? 24.676 -3.914 70.829 1.00 21.31 ? 150 PRO A CD 1 ATOM 1182 N N . THR A 1 151 ? 25.704 -1.489 68.218 1.00 18.14 ? 151 THR A N 1 ATOM 1183 C CA . THR A 1 151 ? 26.322 -0.419 67.450 1.00 17.54 ? 151 THR A CA 1 ATOM 1184 C C . THR A 1 151 ? 26.832 -0.939 66.108 1.00 16.91 ? 151 THR A C 1 ATOM 1185 O O . THR A 1 151 ? 26.755 -0.246 65.098 1.00 17.50 ? 151 THR A O 1 ATOM 1186 C CB . THR A 1 151 ? 27.489 0.226 68.219 1.00 18.85 ? 151 THR A CB 1 ATOM 1187 O OG1 . THR A 1 151 ? 28.478 -0.768 68.513 1.00 22.58 ? 151 THR A OG1 1 ATOM 1188 C CG2 . THR A 1 151 ? 26.988 0.839 69.516 1.00 19.05 ? 151 THR A CG2 1 ATOM 1189 N N . GLU A 1 152 ? 27.342 -2.163 66.092 1.00 15.56 ? 152 GLU A N 1 ATOM 1190 C CA . GLU A 1 152 ? 27.858 -2.734 64.857 1.00 15.97 ? 152 GLU A CA 1 ATOM 1191 C C . GLU A 1 152 ? 26.727 -3.126 63.918 1.00 16.13 ? 152 GLU A C 1 ATOM 1192 O O . GLU A 1 152 ? 26.831 -2.953 62.701 1.00 16.54 ? 152 GLU A O 1 ATOM 1193 C CB . GLU A 1 152 ? 28.753 -3.935 65.163 1.00 15.68 ? 152 GLU A CB 1 ATOM 1194 C CG . GLU A 1 152 ? 30.012 -3.532 65.911 1.00 20.44 ? 152 GLU A CG 1 ATOM 1195 C CD . GLU A 1 152 ? 31.027 -4.650 66.043 1.00 23.49 ? 152 GLU A CD 1 ATOM 1196 O OE1 . GLU A 1 152 ? 32.175 -4.351 66.443 1.00 26.65 ? 152 GLU A OE1 1 ATOM 1197 O OE2 . GLU A 1 152 ? 30.690 -5.819 65.755 1.00 24.38 ? 152 GLU A OE2 1 ATOM 1198 N N . ILE A 1 153 ? 25.641 -3.650 64.481 1.00 15.71 ? 153 ILE A N 1 ATOM 1199 C CA . ILE A 1 153 ? 24.493 -4.036 63.666 1.00 13.86 ? 153 ILE A CA 1 ATOM 1200 C C . ILE A 1 153 ? 23.854 -2.768 63.084 1.00 13.70 ? 153 ILE A C 1 ATOM 1201 O O . ILE A 1 153 ? 23.511 -2.723 61.904 1.00 12.77 ? 153 ILE A O 1 ATOM 1202 C CB . ILE A 1 153 ? 23.463 -4.828 64.499 1.00 13.37 ? 153 ILE A CB 1 ATOM 1203 C CG1 . ILE A 1 153 ? 24.040 -6.203 64.854 1.00 12.47 ? 153 ILE A CG1 1 ATOM 1204 C CG2 . ILE A 1 153 ? 22.161 -4.979 63.728 1.00 12.67 ? 153 ILE A CG2 1 ATOM 1205 C CD1 . ILE A 1 153 ? 23.136 -7.044 65.743 1.00 12.43 ? 153 ILE A CD1 1 ATOM 1206 N N . ALA A 1 154 ? 23.731 -1.733 63.912 1.00 13.12 ? 154 ALA A N 1 ATOM 1207 C CA . ALA A 1 154 ? 23.142 -0.466 63.479 1.00 13.68 ? 154 ALA A CA 1 ATOM 1208 C C . ALA A 1 154 ? 23.920 0.183 62.330 1.00 13.09 ? 154 ALA A C 1 ATOM 1209 O O . ALA A 1 154 ? 23.326 0.597 61.334 1.00 14.29 ? 154 ALA A O 1 ATOM 1210 C CB . ALA A 1 154 ? 23.047 0.503 64.660 1.00 12.16 ? 154 ALA A CB 1 ATOM 1211 N N . SER A 1 155 ? 25.241 0.275 62.448 1.00 13.09 ? 155 SER A N 1 ATOM 1212 C CA . SER A 1 155 ? 26.015 0.892 61.375 1.00 15.04 ? 155 SER A CA 1 ATOM 1213 C C . SER A 1 155 ? 25.993 0.019 60.122 1.00 14.85 ? 155 SER A C 1 ATOM 1214 O O . SER A 1 155 ? 25.919 0.537 59.003 1.00 14.81 ? 155 SER A O 1 ATOM 1215 C CB . SER A 1 155 ? 27.461 1.149 61.807 1.00 17.52 ? 155 SER A CB 1 ATOM 1216 O OG . SER A 1 155 ? 28.123 -0.063 62.101 1.00 26.62 ? 155 SER A OG 1 ATOM 1217 N N . SER A 1 156 ? 26.047 -1.300 60.307 1.00 12.99 ? 156 SER A N 1 ATOM 1218 C CA . SER A 1 156 ? 26.012 -2.217 59.169 1.00 12.40 ? 156 SER A CA 1 ATOM 1219 C C . SER A 1 156 ? 24.665 -2.145 58.438 1.00 11.82 ? 156 SER A C 1 ATOM 1220 O O . SER A 1 156 ? 24.616 -2.146 57.210 1.00 12.46 ? 156 SER A O 1 ATOM 1221 C CB . SER A 1 156 ? 26.289 -3.649 59.636 1.00 13.74 ? 156 SER A CB 1 ATOM 1222 O OG . SER A 1 156 ? 27.613 -3.767 60.142 1.00 14.98 ? 156 SER A OG 1 ATOM 1223 N N . LEU A 1 157 ? 23.568 -2.079 59.182 1.00 11.42 ? 157 LEU A N 1 ATOM 1224 C CA . LEU A 1 157 ? 22.260 -1.988 58.540 1.00 10.88 ? 157 LEU A CA 1 ATOM 1225 C C . LEU A 1 157 ? 22.081 -0.612 57.893 1.00 11.18 ? 157 LEU A C 1 ATOM 1226 O O . LEU A 1 157 ? 21.372 -0.478 56.889 1.00 10.60 ? 157 LEU A O 1 ATOM 1227 C CB . LEU A 1 157 ? 21.139 -2.253 59.552 1.00 11.91 ? 157 LEU A CB 1 ATOM 1228 C CG . LEU A 1 157 ? 21.040 -3.706 60.048 1.00 12.32 ? 157 LEU A CG 1 ATOM 1229 C CD1 . LEU A 1 157 ? 19.933 -3.815 61.081 1.00 12.22 ? 157 LEU A CD1 1 ATOM 1230 C CD2 . LEU A 1 157 ? 20.788 -4.653 58.860 1.00 11.95 ? 157 LEU A CD2 1 ATOM 1231 N N . LEU A 1 158 ? 22.716 0.414 58.463 1.00 10.85 ? 158 LEU A N 1 ATOM 1232 C CA . LEU A 1 158 ? 22.622 1.750 57.880 1.00 11.23 ? 158 LEU A CA 1 ATOM 1233 C C . LEU A 1 158 ? 23.244 1.728 56.465 1.00 11.98 ? 158 LEU A C 1 ATOM 1234 O O . LEU A 1 158 ? 22.731 2.360 55.533 1.00 11.50 ? 158 LEU A O 1 ATOM 1235 C CB . LEU A 1 158 ? 23.326 2.785 58.774 1.00 10.91 ? 158 LEU A CB 1 ATOM 1236 C CG . LEU A 1 158 ? 23.279 4.234 58.256 1.00 11.37 ? 158 LEU A CG 1 ATOM 1237 C CD1 . LEU A 1 158 ? 21.836 4.625 57.902 1.00 11.35 ? 158 LEU A CD1 1 ATOM 1238 C CD2 . LEU A 1 158 ? 23.860 5.172 59.298 1.00 10.40 ? 158 LEU A CD2 1 ATOM 1239 N N . VAL A 1 159 ? 24.335 0.984 56.304 1.00 10.63 ? 159 VAL A N 1 ATOM 1240 C CA . VAL A 1 159 ? 24.990 0.859 55.009 1.00 11.55 ? 159 VAL A CA 1 ATOM 1241 C C . VAL A 1 159 ? 24.076 0.099 54.038 1.00 12.60 ? 159 VAL A C 1 ATOM 1242 O O . VAL A 1 159 ? 23.877 0.519 52.892 1.00 12.35 ? 159 VAL A O 1 ATOM 1243 C CB . VAL A 1 159 ? 26.343 0.102 55.141 1.00 12.45 ? 159 VAL A CB 1 ATOM 1244 C CG1 . VAL A 1 159 ? 26.943 -0.165 53.755 1.00 12.79 ? 159 VAL A CG1 1 ATOM 1245 C CG2 . VAL A 1 159 ? 27.313 0.927 55.979 1.00 11.49 ? 159 VAL A CG2 1 ATOM 1246 N N . VAL A 1 160 ? 23.518 -1.016 54.505 1.00 12.46 ? 160 VAL A N 1 ATOM 1247 C CA . VAL A 1 160 ? 22.623 -1.844 53.695 1.00 12.38 ? 160 VAL A CA 1 ATOM 1248 C C . VAL A 1 160 ? 21.362 -1.072 53.287 1.00 12.10 ? 160 VAL A C 1 ATOM 1249 O O . VAL A 1 160 ? 20.942 -1.110 52.128 1.00 10.91 ? 160 VAL A O 1 ATOM 1250 C CB . VAL A 1 160 ? 22.195 -3.127 54.472 1.00 13.43 ? 160 VAL A CB 1 ATOM 1251 C CG1 . VAL A 1 160 ? 21.081 -3.842 53.730 1.00 13.01 ? 160 VAL A CG1 1 ATOM 1252 C CG2 . VAL A 1 160 ? 23.384 -4.051 54.649 1.00 12.46 ? 160 VAL A CG2 1 ATOM 1253 N N . ILE A 1 161 ? 20.758 -0.379 54.248 1.00 11.02 ? 161 ILE A N 1 ATOM 1254 C CA . ILE A 1 161 ? 19.552 0.393 53.979 1.00 11.49 ? 161 ILE A CA 1 ATOM 1255 C C . ILE A 1 161 ? 19.767 1.417 52.856 1.00 11.64 ? 161 ILE A C 1 ATOM 1256 O O . ILE A 1 161 ? 18.926 1.557 51.961 1.00 11.95 ? 161 ILE A O 1 ATOM 1257 C CB . ILE A 1 161 ? 19.065 1.107 55.265 1.00 10.61 ? 161 ILE A CB 1 ATOM 1258 C CG1 . ILE A 1 161 ? 18.476 0.071 56.228 1.00 11.68 ? 161 ILE A CG1 1 ATOM 1259 C CG2 . ILE A 1 161 ? 18.037 2.181 54.922 1.00 12.77 ? 161 ILE A CG2 1 ATOM 1260 C CD1 . ILE A 1 161 ? 18.118 0.620 57.597 1.00 13.42 ? 161 ILE A CD1 1 ATOM 1261 N N . GLN A 1 162 ? 20.896 2.116 52.872 1.00 9.76 ? 162 GLN A N 1 ATOM 1262 C CA . GLN A 1 162 ? 21.122 3.108 51.830 1.00 11.47 ? 162 GLN A CA 1 ATOM 1263 C C . GLN A 1 162 ? 21.572 2.524 50.499 1.00 11.14 ? 162 GLN A C 1 ATOM 1264 O O . GLN A 1 162 ? 21.135 2.983 49.445 1.00 12.79 ? 162 GLN A O 1 ATOM 1265 C CB . GLN A 1 162 ? 22.118 4.154 52.308 1.00 12.55 ? 162 GLN A CB 1 ATOM 1266 C CG . GLN A 1 162 ? 21.630 4.889 53.535 1.00 14.63 ? 162 GLN A CG 1 ATOM 1267 C CD . GLN A 1 162 ? 22.517 6.045 53.896 1.00 17.03 ? 162 GLN A CD 1 ATOM 1268 O OE1 . GLN A 1 162 ? 22.352 7.151 53.381 1.00 17.79 ? 162 GLN A OE1 1 ATOM 1269 N NE2 . GLN A 1 162 ? 23.486 5.795 54.772 1.00 17.32 ? 162 GLN A NE2 1 ATOM 1270 N N . MET A 1 163 ? 22.422 1.501 50.533 1.00 10.87 ? 163 MET A N 1 ATOM 1271 C CA . MET A 1 163 ? 22.902 0.905 49.289 1.00 10.48 ? 163 MET A CA 1 ATOM 1272 C C . MET A 1 163 ? 21.887 -0.012 48.624 1.00 11.14 ? 163 MET A C 1 ATOM 1273 O O . MET A 1 163 ? 22.017 -0.334 47.440 1.00 11.86 ? 163 MET A O 1 ATOM 1274 C CB . MET A 1 163 ? 24.209 0.149 49.530 1.00 11.89 ? 163 MET A CB 1 ATOM 1275 C CG . MET A 1 163 ? 25.351 1.061 49.958 1.00 12.67 ? 163 MET A CG 1 ATOM 1276 S SD . MET A 1 163 ? 26.945 0.234 50.037 1.00 14.36 ? 163 MET A SD 1 ATOM 1277 C CE . MET A 1 163 ? 27.326 0.027 48.256 1.00 14.29 ? 163 MET A CE 1 ATOM 1278 N N . VAL A 1 164 ? 20.870 -0.428 49.372 1.00 10.99 ? 164 VAL A N 1 ATOM 1279 C CA . VAL A 1 164 ? 19.847 -1.300 48.812 1.00 11.37 ? 164 VAL A CA 1 ATOM 1280 C C . VAL A 1 164 ? 18.497 -0.591 48.731 1.00 10.96 ? 164 VAL A C 1 ATOM 1281 O O . VAL A 1 164 ? 18.006 -0.343 47.632 1.00 12.04 ? 164 VAL A O 1 ATOM 1282 C CB . VAL A 1 164 ? 19.704 -2.618 49.631 1.00 11.83 ? 164 VAL A CB 1 ATOM 1283 C CG1 . VAL A 1 164 ? 18.620 -3.498 49.024 1.00 10.75 ? 164 VAL A CG1 1 ATOM 1284 C CG2 . VAL A 1 164 ? 21.032 -3.374 49.639 1.00 10.46 ? 164 VAL A CG2 1 ATOM 1285 N N . SER A 1 165 ? 17.917 -0.242 49.881 1.00 10.66 ? 165 SER A N 1 ATOM 1286 C CA . SER A 1 165 ? 16.610 0.424 49.910 1.00 11.09 ? 165 SER A CA 1 ATOM 1287 C C . SER A 1 165 ? 16.565 1.800 49.252 1.00 11.72 ? 165 SER A C 1 ATOM 1288 O O . SER A 1 165 ? 15.746 2.035 48.363 1.00 10.53 ? 165 SER A O 1 ATOM 1289 C CB . SER A 1 165 ? 16.096 0.567 51.346 1.00 11.24 ? 165 SER A CB 1 ATOM 1290 O OG . SER A 1 165 ? 15.898 -0.699 51.944 1.00 16.23 ? 165 SER A OG 1 ATOM 1291 N N . GLU A 1 166 ? 17.422 2.716 49.700 1.00 10.98 ? 166 GLU A N 1 ATOM 1292 C CA . GLU A 1 166 ? 17.424 4.068 49.148 1.00 10.56 ? 166 GLU A CA 1 ATOM 1293 C C . GLU A 1 166 ? 17.882 4.088 47.689 1.00 11.04 ? 166 GLU A C 1 ATOM 1294 O O . GLU A 1 166 ? 17.301 4.800 46.868 1.00 10.64 ? 166 GLU A O 1 ATOM 1295 C CB . GLU A 1 166 ? 18.294 4.994 50.009 1.00 12.17 ? 166 GLU A CB 1 ATOM 1296 C CG . GLU A 1 166 ? 17.852 5.080 51.480 1.00 10.75 ? 166 GLU A CG 1 ATOM 1297 C CD . GLU A 1 166 ? 16.519 5.795 51.688 1.00 11.58 ? 166 GLU A CD 1 ATOM 1298 O OE1 . GLU A 1 166 ? 15.806 6.081 50.703 1.00 11.40 ? 166 GLU A OE1 1 ATOM 1299 O OE2 . GLU A 1 166 ? 16.174 6.068 52.859 1.00 13.82 ? 166 GLU A OE2 1 ATOM 1300 N N . ALA A 1 167 ? 18.911 3.307 47.361 1.00 10.93 ? 167 ALA A N 1 ATOM 1301 C CA . ALA A 1 167 ? 19.388 3.249 45.981 1.00 11.54 ? 167 ALA A CA 1 ATOM 1302 C C . ALA A 1 167 ? 18.302 2.674 45.066 1.00 10.59 ? 167 ALA A C 1 ATOM 1303 O O . ALA A 1 167 ? 18.162 3.101 43.922 1.00 11.61 ? 167 ALA A O 1 ATOM 1304 C CB . ALA A 1 167 ? 20.653 2.402 45.886 1.00 11.23 ? 167 ALA A CB 1 ATOM 1305 N N . ALA A 1 168 ? 17.531 1.710 45.566 1.00 10.10 ? 168 ALA A N 1 ATOM 1306 C CA . ALA A 1 168 ? 16.468 1.110 44.763 1.00 10.02 ? 168 ALA A CA 1 ATOM 1307 C C . ALA A 1 168 ? 15.357 2.129 44.502 1.00 10.15 ? 168 ALA A C 1 ATOM 1308 O O . ALA A 1 168 ? 14.771 2.154 43.423 1.00 10.94 ? 168 ALA A O 1 ATOM 1309 C CB . ALA A 1 168 ? 15.900 -0.121 45.467 1.00 9.93 ? 168 ALA A CB 1 ATOM 1310 N N . ARG A 1 169 ? 15.071 2.970 45.493 1.00 10.10 ? 169 ARG A N 1 ATOM 1311 C CA . ARG A 1 169 ? 14.032 3.995 45.361 1.00 9.38 ? 169 ARG A CA 1 ATOM 1312 C C . ARG A 1 169 ? 14.440 5.157 44.444 1.00 10.91 ? 169 ARG A C 1 ATOM 1313 O O . ARG A 1 169 ? 13.621 5.663 43.668 1.00 11.29 ? 169 ARG A O 1 ATOM 1314 C CB . ARG A 1 169 ? 13.716 4.612 46.723 1.00 9.83 ? 169 ARG A CB 1 ATOM 1315 C CG . ARG A 1 169 ? 13.090 3.703 47.758 1.00 10.10 ? 169 ARG A CG 1 ATOM 1316 C CD . ARG A 1 169 ? 13.173 4.396 49.110 1.00 10.24 ? 169 ARG A CD 1 ATOM 1317 N NE . ARG A 1 169 ? 12.512 3.636 50.165 1.00 13.30 ? 169 ARG A NE 1 ATOM 1318 C CZ . ARG A 1 169 ? 12.520 3.978 51.448 1.00 17.14 ? 169 ARG A CZ 1 ATOM 1319 N NH1 . ARG A 1 169 ? 13.160 5.072 51.843 1.00 19.05 ? 169 ARG A NH1 1 ATOM 1320 N NH2 . ARG A 1 169 ? 11.884 3.230 52.339 1.00 17.95 ? 169 ARG A NH2 1 ATOM 1321 N N . PHE A 1 170 ? 15.705 5.578 44.559 1.00 10.15 ? 170 PHE A N 1 ATOM 1322 C CA . PHE A 1 170 ? 16.225 6.729 43.825 1.00 10.05 ? 170 PHE A CA 1 ATOM 1323 C C . PHE A 1 170 ? 17.357 6.458 42.859 1.00 10.31 ? 170 PHE A C 1 ATOM 1324 O O . PHE A 1 170 ? 18.417 5.974 43.247 1.00 11.29 ? 170 PHE A O 1 ATOM 1325 C CB . PHE A 1 170 ? 16.737 7.791 44.811 1.00 11.66 ? 170 PHE A CB 1 ATOM 1326 C CG . PHE A 1 170 ? 15.669 8.418 45.671 1.00 11.61 ? 170 PHE A CG 1 ATOM 1327 C CD1 . PHE A 1 170 ? 14.888 9.466 45.184 1.00 12.05 ? 170 PHE A CD1 1 ATOM 1328 C CD2 . PHE A 1 170 ? 15.464 7.979 46.978 1.00 10.78 ? 170 PHE A CD2 1 ATOM 1329 C CE1 . PHE A 1 170 ? 13.917 10.073 45.986 1.00 11.14 ? 170 PHE A CE1 1 ATOM 1330 C CE2 . PHE A 1 170 ? 14.495 8.577 47.790 1.00 11.66 ? 170 PHE A CE2 1 ATOM 1331 C CZ . PHE A 1 170 ? 13.720 9.627 47.291 1.00 11.81 ? 170 PHE A CZ 1 ATOM 1332 N N . THR A 1 171 ? 17.146 6.814 41.600 1.00 11.28 ? 171 THR A N 1 ATOM 1333 C CA . THR A 1 171 ? 18.185 6.659 40.603 1.00 12.02 ? 171 THR A CA 1 ATOM 1334 C C . THR A 1 171 ? 19.336 7.604 40.991 1.00 12.35 ? 171 THR A C 1 ATOM 1335 O O . THR A 1 171 ? 20.506 7.335 40.708 1.00 12.60 ? 171 THR A O 1 ATOM 1336 C CB . THR A 1 171 ? 17.666 7.037 39.200 1.00 14.25 ? 171 THR A CB 1 ATOM 1337 O OG1 . THR A 1 171 ? 17.078 8.345 39.250 1.00 16.14 ? 171 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 171 ? 16.626 6.023 38.709 1.00 13.96 ? 171 THR A CG2 1 ATOM 1339 N N . PHE A 1 172 ? 19.005 8.713 41.649 1.00 12.61 ? 172 PHE A N 1 ATOM 1340 C CA . PHE A 1 172 ? 20.033 9.664 42.070 1.00 13.23 ? 172 PHE A CA 1 ATOM 1341 C C . PHE A 1 172 ? 21.032 9.021 43.039 1.00 13.13 ? 172 PHE A C 1 ATOM 1342 O O . PHE A 1 172 ? 22.249 9.174 42.889 1.00 12.53 ? 172 PHE A O 1 ATOM 1343 C CB . PHE A 1 172 ? 19.394 10.877 42.748 1.00 12.88 ? 172 PHE A CB 1 ATOM 1344 C CG . PHE A 1 172 ? 20.381 11.937 43.146 1.00 15.93 ? 172 PHE A CG 1 ATOM 1345 C CD1 . PHE A 1 172 ? 20.882 12.833 42.201 1.00 16.47 ? 172 PHE A CD1 1 ATOM 1346 C CD2 . PHE A 1 172 ? 20.829 12.030 44.464 1.00 15.71 ? 172 PHE A CD2 1 ATOM 1347 C CE1 . PHE A 1 172 ? 21.817 13.808 42.566 1.00 17.36 ? 172 PHE A CE1 1 ATOM 1348 C CE2 . PHE A 1 172 ? 21.761 13.000 44.836 1.00 17.57 ? 172 PHE A CE2 1 ATOM 1349 C CZ . PHE A 1 172 ? 22.254 13.889 43.881 1.00 16.29 ? 172 PHE A CZ 1 ATOM 1350 N N . ILE A 1 173 ? 20.513 8.306 44.036 1.00 12.42 ? 173 ILE A N 1 ATOM 1351 C CA . ILE A 1 173 ? 21.357 7.655 45.034 1.00 12.50 ? 173 ILE A CA 1 ATOM 1352 C C . ILE A 1 173 ? 22.083 6.474 44.396 1.00 13.92 ? 173 ILE A C 1 ATOM 1353 O O . ILE A 1 173 ? 23.257 6.217 44.685 1.00 12.58 ? 173 ILE A O 1 ATOM 1354 C CB . ILE A 1 173 ? 20.508 7.225 46.258 1.00 12.45 ? 173 ILE A CB 1 ATOM 1355 C CG1 . ILE A 1 173 ? 19.921 8.483 46.915 1.00 11.84 ? 173 ILE A CG1 1 ATOM 1356 C CG2 . ILE A 1 173 ? 21.361 6.462 47.263 1.00 11.59 ? 173 ILE A CG2 1 ATOM 1357 C CD1 . ILE A 1 173 ? 19.024 8.227 48.115 1.00 11.12 ? 173 ILE A CD1 1 ATOM 1358 N N . GLU A 1 174 ? 21.379 5.773 43.512 1.00 13.61 ? 174 GLU A N 1 ATOM 1359 C CA . GLU A 1 174 ? 21.955 4.655 42.766 1.00 13.10 ? 174 GLU A CA 1 ATOM 1360 C C . GLU A 1 174 ? 23.220 5.139 42.058 1.00 13.28 ? 174 GLU A C 1 ATOM 1361 O O . GLU A 1 174 ? 24.265 4.485 42.101 1.00 13.43 ? 174 GLU A O 1 ATOM 1362 C CB . GLU A 1 174 ? 20.968 4.162 41.699 1.00 12.59 ? 174 GLU A CB 1 ATOM 1363 C CG . GLU A 1 174 ? 21.599 3.279 40.616 1.00 13.54 ? 174 GLU A CG 1 ATOM 1364 C CD . GLU A 1 174 ? 20.676 3.031 39.422 1.00 15.25 ? 174 GLU A CD 1 ATOM 1365 O OE1 . GLU A 1 174 ? 19.518 3.498 39.429 1.00 15.43 ? 174 GLU A OE1 1 ATOM 1366 O OE2 . GLU A 1 174 ? 21.112 2.361 38.464 1.00 17.70 ? 174 GLU A OE2 1 ATOM 1367 N N . ASN A 1 175 ? 23.118 6.291 41.405 1.00 12.83 ? 175 ASN A N 1 ATOM 1368 C CA . ASN A 1 175 ? 24.251 6.821 40.668 1.00 15.61 ? 175 ASN A CA 1 ATOM 1369 C C . ASN A 1 175 ? 25.351 7.467 41.498 1.00 16.79 ? 175 ASN A C 1 ATOM 1370 O O . ASN A 1 175 ? 26.503 7.526 41.057 1.00 17.14 ? 175 ASN A O 1 ATOM 1371 C CB . ASN A 1 175 ? 23.746 7.746 39.569 1.00 15.63 ? 175 ASN A CB 1 ATOM 1372 C CG . ASN A 1 175 ? 23.022 6.973 38.488 1.00 18.09 ? 175 ASN A CG 1 ATOM 1373 O OD1 . ASN A 1 175 ? 23.511 5.932 38.047 1.00 19.72 ? 175 ASN A OD1 1 ATOM 1374 N ND2 . ASN A 1 175 ? 21.856 7.459 38.065 1.00 16.40 ? 175 ASN A ND2 1 ATOM 1375 N N . GLN A 1 176 ? 25.014 7.936 42.697 1.00 17.08 ? 176 GLN A N 1 ATOM 1376 C CA . GLN A 1 176 ? 26.030 8.504 43.578 1.00 18.34 ? 176 GLN A CA 1 ATOM 1377 C C . GLN A 1 176 ? 26.941 7.328 43.932 1.00 18.29 ? 176 GLN A C 1 ATOM 1378 O O . GLN A 1 176 ? 28.164 7.465 44.020 1.00 20.78 ? 176 GLN A O 1 ATOM 1379 C CB . GLN A 1 176 ? 25.397 9.068 44.855 1.00 21.80 ? 176 GLN A CB 1 ATOM 1380 C CG . GLN A 1 176 ? 24.578 10.331 44.641 1.00 28.83 ? 176 GLN A CG 1 ATOM 1381 C CD . GLN A 1 176 ? 25.428 11.586 44.666 1.00 32.82 ? 176 GLN A CD 1 ATOM 1382 O OE1 . GLN A 1 176 ? 26.560 11.591 44.183 1.00 36.32 ? 176 GLN A OE1 1 ATOM 1383 N NE2 . GLN A 1 176 ? 24.882 12.664 45.227 1.00 34.73 ? 176 GLN A NE2 1 ATOM 1384 N N . ILE A 1 177 ? 26.334 6.161 44.119 1.00 15.04 ? 177 ILE A N 1 ATOM 1385 C CA . ILE A 1 177 ? 27.086 4.962 44.449 1.00 15.07 ? 177 ILE A CA 1 ATOM 1386 C C . ILE A 1 177 ? 27.756 4.341 43.216 1.00 15.24 ? 177 ILE A C 1 ATOM 1387 O O . ILE A 1 177 ? 28.919 3.925 43.279 1.00 15.31 ? 177 ILE A O 1 ATOM 1388 C CB . ILE A 1 177 ? 26.163 3.939 45.139 1.00 16.73 ? 177 ILE A CB 1 ATOM 1389 C CG1 . ILE A 1 177 ? 25.711 4.519 46.482 1.00 18.04 ? 177 ILE A CG1 1 ATOM 1390 C CG2 . ILE A 1 177 ? 26.883 2.608 45.357 1.00 14.60 ? 177 ILE A CG2 1 ATOM 1391 C CD1 . ILE A 1 177 ? 24.632 3.729 47.155 1.00 22.60 ? 177 ILE A CD1 1 ATOM 1392 N N . ARG A 1 178 ? 27.034 4.300 42.095 1.00 13.86 ? 178 ARG A N 1 ATOM 1393 C CA . ARG A 1 178 ? 27.562 3.725 40.859 1.00 13.51 ? 178 ARG A CA 1 ATOM 1394 C C . ARG A 1 178 ? 28.931 4.289 40.469 1.00 13.82 ? 178 ARG A C 1 ATOM 1395 O O . ARG A 1 178 ? 29.855 3.530 40.176 1.00 12.43 ? 178 ARG A O 1 ATOM 1396 C CB . ARG A 1 178 ? 26.576 3.946 39.698 1.00 14.79 ? 178 ARG A CB 1 ATOM 1397 C CG . ARG A 1 178 ? 27.138 3.537 38.327 1.00 15.69 ? 178 ARG A CG 1 ATOM 1398 C CD . ARG A 1 178 ? 26.162 3.786 37.189 1.00 18.43 ? 178 ARG A CD 1 ATOM 1399 N NE . ARG A 1 178 ? 26.733 3.437 35.885 1.00 20.67 ? 178 ARG A NE 1 ATOM 1400 C CZ . ARG A 1 178 ? 26.097 2.739 34.938 1.00 25.24 ? 178 ARG A CZ 1 ATOM 1401 N NH1 . ARG A 1 178 ? 24.853 2.293 35.132 1.00 20.85 ? 178 ARG A NH1 1 ATOM 1402 N NH2 . ARG A 1 178 ? 26.702 2.492 33.780 1.00 23.76 ? 178 ARG A NH2 1 ATOM 1403 N N . ASN A 1 179 ? 29.054 5.618 40.461 1.00 14.17 ? 179 ASN A N 1 ATOM 1404 C CA . ASN A 1 179 ? 30.304 6.272 40.080 1.00 13.97 ? 179 ASN A CA 1 ATOM 1405 C C . ASN A 1 179 ? 31.289 6.519 41.228 1.00 14.98 ? 179 ASN A C 1 ATOM 1406 O O . ASN A 1 179 ? 32.251 7.271 41.078 1.00 15.83 ? 179 ASN A O 1 ATOM 1407 C CB . ASN A 1 179 ? 30.006 7.585 39.349 1.00 14.92 ? 179 ASN A CB 1 ATOM 1408 C CG . ASN A 1 179 ? 29.400 7.359 37.973 1.00 15.92 ? 179 ASN A CG 1 ATOM 1409 O OD1 . ASN A 1 179 ? 29.738 6.389 37.298 1.00 16.61 ? 179 ASN A OD1 1 ATOM 1410 N ND2 . ASN A 1 179 ? 28.518 8.260 37.543 1.00 15.35 ? 179 ASN A ND2 1 ATOM 1411 N N . ASN A 1 180 ? 31.037 5.882 42.369 1.00 14.83 ? 180 ASN A N 1 ATOM 1412 C CA . ASN A 1 180 ? 31.903 5.970 43.548 1.00 15.25 ? 180 ASN A CA 1 ATOM 1413 C C . ASN A 1 180 ? 31.968 4.563 44.135 1.00 16.19 ? 180 ASN A C 1 ATOM 1414 O O . ASN A 1 180 ? 32.356 4.368 45.287 1.00 15.93 ? 180 ASN A O 1 ATOM 1415 C CB . ASN A 1 180 ? 31.308 6.916 44.595 1.00 15.02 ? 180 ASN A CB 1 ATOM 1416 C CG . ASN A 1 180 ? 31.464 8.379 44.224 1.00 15.55 ? 180 ASN A CG 1 ATOM 1417 O OD1 . ASN A 1 180 ? 32.578 8.899 44.129 1.00 16.42 ? 180 ASN A OD1 1 ATOM 1418 N ND2 . ASN A 1 180 ? 30.344 9.054 44.020 1.00 15.91 ? 180 ASN A ND2 1 ATOM 1419 N N . PHE A 1 181 ? 31.595 3.584 43.320 1.00 16.39 ? 181 PHE A N 1 ATOM 1420 C CA . PHE A 1 181 ? 31.534 2.192 43.747 1.00 17.44 ? 181 PHE A CA 1 ATOM 1421 C C . PHE A 1 181 ? 32.764 1.641 44.472 1.00 19.15 ? 181 PHE A C 1 ATOM 1422 O O . PHE A 1 181 ? 32.643 1.042 45.553 1.00 18.14 ? 181 PHE A O 1 ATOM 1423 C CB . PHE A 1 181 ? 31.209 1.300 42.547 1.00 16.42 ? 181 PHE A CB 1 ATOM 1424 C CG . PHE A 1 181 ? 30.741 -0.069 42.929 1.00 16.59 ? 181 PHE A CG 1 ATOM 1425 C CD1 . PHE A 1 181 ? 29.546 -0.238 43.620 1.00 16.81 ? 181 PHE A CD1 1 ATOM 1426 C CD2 . PHE A 1 181 ? 31.498 -1.192 42.611 1.00 17.59 ? 181 PHE A CD2 1 ATOM 1427 C CE1 . PHE A 1 181 ? 29.108 -1.511 43.990 1.00 18.35 ? 181 PHE A CE1 1 ATOM 1428 C CE2 . PHE A 1 181 ? 31.069 -2.470 42.977 1.00 18.20 ? 181 PHE A CE2 1 ATOM 1429 C CZ . PHE A 1 181 ? 29.872 -2.629 43.667 1.00 17.40 ? 181 PHE A CZ 1 ATOM 1430 N N . GLN A 1 182 ? 33.938 1.831 43.878 1.00 18.49 ? 182 GLN A N 1 ATOM 1431 C CA . GLN A 1 182 ? 35.170 1.331 44.470 1.00 20.23 ? 182 GLN A CA 1 ATOM 1432 C C . GLN A 1 182 ? 35.772 2.294 45.491 1.00 21.81 ? 182 GLN A C 1 ATOM 1433 O O . GLN A 1 182 ? 36.918 2.134 45.896 1.00 23.74 ? 182 GLN A O 1 ATOM 1434 C CB . GLN A 1 182 ? 36.196 1.049 43.373 1.00 19.82 ? 182 GLN A CB 1 ATOM 1435 C CG . GLN A 1 182 ? 35.768 -0.014 42.375 1.00 21.02 ? 182 GLN A CG 1 ATOM 1436 C CD . GLN A 1 182 ? 35.502 -1.346 43.037 1.00 24.37 ? 182 GLN A CD 1 ATOM 1437 O OE1 . GLN A 1 182 ? 36.127 -1.681 44.045 1.00 24.06 ? 182 GLN A OE1 1 ATOM 1438 N NE2 . GLN A 1 182 ? 34.584 -2.125 42.468 1.00 26.26 ? 182 GLN A NE2 1 ATOM 1439 N N . GLN A 1 183 ? 35.001 3.289 45.910 1.00 21.63 ? 183 GLN A N 1 ATOM 1440 C CA . GLN A 1 183 ? 35.492 4.265 46.873 1.00 22.39 ? 183 GLN A CA 1 ATOM 1441 C C . GLN A 1 183 ? 34.625 4.288 48.131 1.00 22.54 ? 183 GLN A C 1 ATOM 1442 O O . GLN A 1 183 ? 33.668 3.520 48.266 1.00 23.02 ? 183 GLN A O 1 ATOM 1443 C CB . GLN A 1 183 ? 35.505 5.655 46.231 1.00 24.01 ? 183 GLN A CB 1 ATOM 1444 C CG . GLN A 1 183 ? 36.299 5.730 44.940 1.00 27.27 ? 183 GLN A CG 1 ATOM 1445 C CD . GLN A 1 183 ? 35.820 6.845 44.023 1.00 30.51 ? 183 GLN A CD 1 ATOM 1446 O OE1 . GLN A 1 183 ? 35.896 8.028 44.368 1.00 32.68 ? 183 GLN A OE1 1 ATOM 1447 N NE2 . GLN A 1 183 ? 35.319 6.470 42.843 1.00 29.88 ? 183 GLN A NE2 1 ATOM 1448 N N . ARG A 1 184 ? 34.986 5.162 49.061 1.00 20.99 ? 184 ARG A N 1 ATOM 1449 C CA . ARG A 1 184 ? 34.239 5.319 50.294 1.00 21.77 ? 184 ARG A CA 1 ATOM 1450 C C . ARG A 1 184 ? 33.704 6.736 50.273 1.00 23.53 ? 184 ARG A C 1 ATOM 1451 O O . ARG A 1 184 ? 34.477 7.693 50.240 1.00 25.22 ? 184 ARG A O 1 ATOM 1452 C CB . ARG A 1 184 ? 35.144 5.125 51.506 1.00 20.75 ? 184 ARG A CB 1 ATOM 1453 C CG . ARG A 1 184 ? 35.396 3.679 51.862 1.00 22.93 ? 184 ARG A CG 1 ATOM 1454 C CD . ARG A 1 184 ? 36.632 3.563 52.716 1.00 26.75 ? 184 ARG A CD 1 ATOM 1455 N NE . ARG A 1 184 ? 36.808 2.219 53.249 1.00 30.47 ? 184 ARG A NE 1 ATOM 1456 C CZ . ARG A 1 184 ? 36.116 1.724 54.272 1.00 33.80 ? 184 ARG A CZ 1 ATOM 1457 N NH1 . ARG A 1 184 ? 35.192 2.463 54.885 1.00 32.64 ? 184 ARG A NH1 1 ATOM 1458 N NH2 . ARG A 1 184 ? 36.351 0.484 54.687 1.00 34.64 ? 184 ARG A NH2 1 ATOM 1459 N N . ILE A 1 185 ? 32.383 6.873 50.270 1.00 21.43 ? 185 ILE A N 1 ATOM 1460 C CA . ILE A 1 185 ? 31.771 8.193 50.251 1.00 21.11 ? 185 ILE A CA 1 ATOM 1461 C C . ILE A 1 185 ? 30.693 8.264 51.313 1.00 19.02 ? 185 ILE A C 1 ATOM 1462 O O . ILE A 1 185 ? 30.102 7.257 51.680 1.00 19.50 ? 185 ILE A O 1 ATOM 1463 C CB . ILE A 1 185 ? 31.105 8.494 48.889 1.00 22.14 ? 185 ILE A CB 1 ATOM 1464 C CG1 . ILE A 1 185 ? 29.878 7.586 48.707 1.00 23.72 ? 185 ILE A CG1 1 ATOM 1465 C CG2 . ILE A 1 185 ? 32.110 8.282 47.764 1.00 22.88 ? 185 ILE A CG2 1 ATOM 1466 C CD1 . ILE A 1 185 ? 28.967 7.956 47.553 1.00 23.49 ? 185 ILE A CD1 1 ATOM 1467 N N . ARG A 1 186 ? 30.452 9.463 51.813 1.00 18.66 ? 186 ARG A N 1 ATOM 1468 C CA . ARG A 1 186 ? 29.412 9.665 52.799 1.00 18.67 ? 186 ARG A CA 1 ATOM 1469 C C . ARG A 1 186 ? 28.379 10.550 52.127 1.00 18.67 ? 186 ARG A C 1 ATOM 1470 O O . ARG A 1 186 ? 28.732 11.504 51.429 1.00 19.08 ? 186 ARG A O 1 ATOM 1471 C CB . ARG A 1 186 ? 29.980 10.346 54.039 1.00 18.47 ? 186 ARG A CB 1 ATOM 1472 C CG . ARG A 1 186 ? 30.846 9.426 54.865 1.00 21.00 ? 186 ARG A CG 1 ATOM 1473 C CD . ARG A 1 186 ? 31.554 10.175 55.973 1.00 22.49 ? 186 ARG A CD 1 ATOM 1474 N NE . ARG A 1 186 ? 32.426 9.292 56.739 1.00 24.54 ? 186 ARG A NE 1 ATOM 1475 C CZ . ARG A 1 186 ? 33.039 9.635 57.868 1.00 25.41 ? 186 ARG A CZ 1 ATOM 1476 N NH1 . ARG A 1 186 ? 32.882 10.851 58.366 1.00 23.53 ? 186 ARG A NH1 1 ATOM 1477 N NH2 . ARG A 1 186 ? 33.790 8.749 58.510 1.00 28.11 ? 186 ARG A NH2 1 ATOM 1478 N N . PRO A 1 187 ? 27.089 10.235 52.305 1.00 18.19 ? 187 PRO A N 1 ATOM 1479 C CA . PRO A 1 187 ? 26.040 11.046 51.684 1.00 17.93 ? 187 PRO A CA 1 ATOM 1480 C C . PRO A 1 187 ? 26.138 12.499 52.106 1.00 17.87 ? 187 PRO A C 1 ATOM 1481 O O . PRO A 1 187 ? 26.521 12.789 53.237 1.00 18.85 ? 187 PRO A O 1 ATOM 1482 C CB . PRO A 1 187 ? 24.754 10.391 52.177 1.00 17.83 ? 187 PRO A CB 1 ATOM 1483 C CG . PRO A 1 187 ? 25.148 9.818 53.500 1.00 19.88 ? 187 PRO A CG 1 ATOM 1484 C CD . PRO A 1 187 ? 26.506 9.218 53.195 1.00 18.37 ? 187 PRO A CD 1 ATOM 1485 N N . ALA A 1 188 ? 25.811 13.405 51.188 1.00 17.71 ? 188 ALA A N 1 ATOM 1486 C CA . ALA A 1 188 ? 25.837 14.833 51.480 1.00 17.21 ? 188 ALA A CA 1 ATOM 1487 C C . ALA A 1 188 ? 24.400 15.263 51.766 1.00 16.78 ? 188 ALA A C 1 ATOM 1488 O O . ALA A 1 188 ? 23.508 14.418 51.836 1.00 15.42 ? 188 ALA A O 1 ATOM 1489 C CB . ALA A 1 188 ? 26.407 15.611 50.294 1.00 17.19 ? 188 ALA A CB 1 ATOM 1490 N N . ASN A 1 189 ? 24.179 16.565 51.925 1.00 16.56 ? 189 ASN A N 1 ATOM 1491 C CA . ASN A 1 189 ? 22.846 17.097 52.211 1.00 17.32 ? 189 ASN A CA 1 ATOM 1492 C C . ASN A 1 189 ? 21.801 16.803 51.129 1.00 15.96 ? 189 ASN A C 1 ATOM 1493 O O . ASN A 1 189 ? 20.604 16.719 51.416 1.00 15.03 ? 189 ASN A O 1 ATOM 1494 C CB . ASN A 1 189 ? 22.932 18.612 52.451 1.00 20.20 ? 189 ASN A CB 1 ATOM 1495 C CG . ASN A 1 189 ? 23.820 18.965 53.642 1.00 25.21 ? 189 ASN A CG 1 ATOM 1496 O OD1 . ASN A 1 189 ? 23.495 18.641 54.784 1.00 23.48 ? 189 ASN A OD1 1 ATOM 1497 N ND2 . ASN A 1 189 ? 24.943 19.622 53.362 1.00 31.31 ? 189 ASN A ND2 1 ATOM 1498 N N . ASN A 1 190 ? 22.242 16.651 49.887 1.00 15.56 ? 190 ASN A N 1 ATOM 1499 C CA . ASN A 1 190 ? 21.302 16.360 48.816 1.00 16.47 ? 190 ASN A CA 1 ATOM 1500 C C . ASN A 1 190 ? 20.729 14.946 48.951 1.00 16.96 ? 190 ASN A C 1 ATOM 1501 O O . ASN A 1 190 ? 19.513 14.752 48.904 1.00 16.15 ? 190 ASN A O 1 ATOM 1502 C CB . ASN A 1 190 ? 21.960 16.551 47.440 1.00 17.74 ? 190 ASN A CB 1 ATOM 1503 C CG . ASN A 1 190 ? 23.365 15.975 47.361 1.00 18.82 ? 190 ASN A CG 1 ATOM 1504 O OD1 . ASN A 1 190 ? 23.858 15.337 48.296 1.00 20.30 ? 190 ASN A OD1 1 ATOM 1505 N ND2 . ASN A 1 190 ? 24.016 16.199 46.228 1.00 20.14 ? 190 ASN A ND2 1 ATOM 1506 N N . THR A 1 191 ? 21.608 13.964 49.130 1.00 15.96 ? 191 THR A N 1 ATOM 1507 C CA . THR A 1 191 ? 21.186 12.576 49.297 1.00 15.28 ? 191 THR A CA 1 ATOM 1508 C C . THR A 1 191 ? 20.288 12.410 50.531 1.00 14.57 ? 191 THR A C 1 ATOM 1509 O O . THR A 1 191 ? 19.217 11.792 50.466 1.00 13.19 ? 191 THR A O 1 ATOM 1510 C CB . THR A 1 191 ? 22.421 11.675 49.433 1.00 16.58 ? 191 THR A CB 1 ATOM 1511 O OG1 . THR A 1 191 ? 23.144 11.704 48.200 1.00 21.77 ? 191 THR A OG1 1 ATOM 1512 C CG2 . THR A 1 191 ? 22.028 10.241 49.757 1.00 16.64 ? 191 THR A CG2 1 ATOM 1513 N N . ILE A 1 192 ? 20.726 12.976 51.651 1.00 12.48 ? 192 ILE A N 1 ATOM 1514 C CA . ILE A 1 192 ? 19.982 12.895 52.898 1.00 13.00 ? 192 ILE A CA 1 ATOM 1515 C C . ILE A 1 192 ? 18.594 13.540 52.782 1.00 12.69 ? 192 ILE A C 1 ATOM 1516 O O . ILE A 1 192 ? 17.602 12.971 53.241 1.00 11.89 ? 192 ILE A O 1 ATOM 1517 C CB . ILE A 1 192 ? 20.807 13.533 54.054 1.00 13.28 ? 192 ILE A CB 1 ATOM 1518 C CG1 . ILE A 1 192 ? 22.089 12.706 54.261 1.00 15.37 ? 192 ILE A CG1 1 ATOM 1519 C CG2 . ILE A 1 192 ? 19.980 13.614 55.325 1.00 13.32 ? 192 ILE A CG2 1 ATOM 1520 C CD1 . ILE A 1 192 ? 23.048 13.207 55.350 1.00 16.25 ? 192 ILE A CD1 1 ATOM 1521 N N . SER A 1 193 ? 18.505 14.706 52.148 1.00 12.89 ? 193 SER A N 1 ATOM 1522 C CA . SER A 1 193 ? 17.196 15.345 52.021 1.00 14.03 ? 193 SER A CA 1 ATOM 1523 C C . SER A 1 193 ? 16.288 14.517 51.110 1.00 12.93 ? 193 SER A C 1 ATOM 1524 O O . SER A 1 193 ? 15.083 14.438 51.348 1.00 12.95 ? 193 SER A O 1 ATOM 1525 C CB . SER A 1 193 ? 17.318 16.793 51.500 1.00 14.24 ? 193 SER A CB 1 ATOM 1526 O OG . SER A 1 193 ? 17.825 16.849 50.177 1.00 16.83 ? 193 SER A OG 1 ATOM 1527 N N . LEU A 1 194 ? 16.856 13.896 50.077 1.00 13.05 ? 194 LEU A N 1 ATOM 1528 C CA . LEU A 1 194 ? 16.056 13.061 49.175 1.00 14.14 ? 194 LEU A CA 1 ATOM 1529 C C . LEU A 1 194 ? 15.463 11.895 49.955 1.00 13.39 ? 194 LEU A C 1 ATOM 1530 O O . LEU A 1 194 ? 14.268 11.625 49.875 1.00 12.61 ? 194 LEU A O 1 ATOM 1531 C CB . LEU A 1 194 ? 16.912 12.487 48.044 1.00 16.69 ? 194 LEU A CB 1 ATOM 1532 C CG . LEU A 1 194 ? 16.793 13.076 46.642 1.00 20.28 ? 194 LEU A CG 1 ATOM 1533 C CD1 . LEU A 1 194 ? 17.567 12.181 45.680 1.00 20.77 ? 194 LEU A CD1 1 ATOM 1534 C CD2 . LEU A 1 194 ? 15.332 13.169 46.225 1.00 19.09 ? 194 LEU A CD2 1 ATOM 1535 N N . GLU A 1 195 ? 16.318 11.202 50.700 1.00 12.74 ? 195 GLU A N 1 ATOM 1536 C CA . GLU A 1 195 ? 15.889 10.064 51.505 1.00 12.44 ? 195 GLU A CA 1 ATOM 1537 C C . GLU A 1 195 ? 14.782 10.495 52.456 1.00 14.29 ? 195 GLU A C 1 ATOM 1538 O O . GLU A 1 195 ? 13.762 9.808 52.589 1.00 15.79 ? 195 GLU A O 1 ATOM 1539 C CB . GLU A 1 195 ? 17.067 9.508 52.312 1.00 13.12 ? 195 GLU A CB 1 ATOM 1540 C CG . GLU A 1 195 ? 18.243 9.012 51.458 1.00 13.31 ? 195 GLU A CG 1 ATOM 1541 C CD . GLU A 1 195 ? 19.448 8.599 52.290 1.00 14.74 ? 195 GLU A CD 1 ATOM 1542 O OE1 . GLU A 1 195 ? 19.619 9.133 53.407 1.00 15.92 ? 195 GLU A OE1 1 ATOM 1543 O OE2 . GLU A 1 195 ? 20.242 7.755 51.819 1.00 14.56 ? 195 GLU A OE2 1 ATOM 1544 N N . ASN A 1 196 ? 14.974 11.640 53.110 1.00 13.58 ? 196 ASN A N 1 ATOM 1545 C CA . ASN A 1 196 ? 13.984 12.136 54.059 1.00 13.54 ? 196 ASN A CA 1 ATOM 1546 C C . ASN A 1 196 ? 12.637 12.460 53.418 1.00 14.88 ? 196 ASN A C 1 ATOM 1547 O O . ASN A 1 196 ? 11.586 12.316 54.052 1.00 14.98 ? 196 ASN A O 1 ATOM 1548 C CB . ASN A 1 196 ? 14.489 13.406 54.754 1.00 13.20 ? 196 ASN A CB 1 ATOM 1549 C CG . ASN A 1 196 ? 15.677 13.150 55.666 1.00 16.84 ? 196 ASN A CG 1 ATOM 1550 O OD1 . ASN A 1 196 ? 15.946 12.014 56.049 1.00 15.66 ? 196 ASN A OD1 1 ATOM 1551 N ND2 . ASN A 1 196 ? 16.381 14.217 56.035 1.00 16.30 ? 196 ASN A ND2 1 ATOM 1552 N N . LYS A 1 197 ? 12.678 12.893 52.160 1.00 14.10 ? 197 LYS A N 1 ATOM 1553 C CA . LYS A 1 197 ? 11.476 13.318 51.451 1.00 13.71 ? 197 LYS A CA 1 ATOM 1554 C C . LYS A 1 197 ? 10.809 12.349 50.482 1.00 13.78 ? 197 LYS A C 1 ATOM 1555 O O . LYS A 1 197 ? 9.899 12.742 49.751 1.00 14.78 ? 197 LYS A O 1 ATOM 1556 C CB . LYS A 1 197 ? 11.778 14.635 50.725 1.00 13.44 ? 197 LYS A CB 1 ATOM 1557 C CG . LYS A 1 197 ? 12.041 15.808 51.667 1.00 15.25 ? 197 LYS A CG 1 ATOM 1558 C CD . LYS A 1 197 ? 10.850 16.002 52.606 1.00 17.55 ? 197 LYS A CD 1 ATOM 1559 C CE . LYS A 1 197 ? 10.788 17.396 53.208 1.00 21.85 ? 197 LYS A CE 1 ATOM 1560 N NZ . LYS A 1 197 ? 11.946 17.715 54.067 1.00 24.76 ? 197 LYS A NZ 1 ATOM 1561 N N . TRP A 1 198 ? 11.233 11.091 50.478 1.00 12.41 ? 198 TRP A N 1 ATOM 1562 C CA . TRP A 1 198 ? 10.640 10.120 49.565 1.00 12.44 ? 198 TRP A CA 1 ATOM 1563 C C . TRP A 1 198 ? 9.114 10.032 49.688 1.00 11.52 ? 198 TRP A C 1 ATOM 1564 O O . TRP A 1 198 ? 8.409 9.957 48.685 1.00 12.78 ? 198 TRP A O 1 ATOM 1565 C CB . TRP A 1 198 ? 11.257 8.734 49.780 1.00 12.13 ? 198 TRP A CB 1 ATOM 1566 C CG . TRP A 1 198 ? 10.783 7.717 48.771 1.00 13.16 ? 198 TRP A CG 1 ATOM 1567 C CD1 . TRP A 1 198 ? 10.861 7.816 47.407 1.00 13.80 ? 198 TRP A CD1 1 ATOM 1568 C CD2 . TRP A 1 198 ? 10.183 6.442 49.045 1.00 12.10 ? 198 TRP A CD2 1 ATOM 1569 N NE1 . TRP A 1 198 ? 10.349 6.682 46.819 1.00 13.29 ? 198 TRP A NE1 1 ATOM 1570 C CE2 . TRP A 1 198 ? 9.928 5.823 47.799 1.00 11.18 ? 198 TRP A CE2 1 ATOM 1571 C CE3 . TRP A 1 198 ? 9.837 5.761 50.222 1.00 13.14 ? 198 TRP A CE3 1 ATOM 1572 C CZ2 . TRP A 1 198 ? 9.344 4.557 47.696 1.00 11.69 ? 198 TRP A CZ2 1 ATOM 1573 C CZ3 . TRP A 1 198 ? 9.255 4.498 50.119 1.00 13.23 ? 198 TRP A CZ3 1 ATOM 1574 C CH2 . TRP A 1 198 ? 9.015 3.912 48.861 1.00 12.17 ? 198 TRP A CH2 1 ATOM 1575 N N . GLY A 1 199 ? 8.605 10.035 50.912 1.00 12.37 ? 199 GLY A N 1 ATOM 1576 C CA . GLY A 1 199 ? 7.169 9.958 51.109 1.00 11.62 ? 199 GLY A CA 1 ATOM 1577 C C . GLY A 1 199 ? 6.452 11.205 50.625 1.00 12.75 ? 199 GLY A C 1 ATOM 1578 O O . GLY A 1 199 ? 5.437 11.105 49.930 1.00 13.39 ? 199 GLY A O 1 ATOM 1579 N N . LYS A 1 200 ? 6.964 12.380 50.986 1.00 13.29 ? 200 LYS A N 1 ATOM 1580 C CA . LYS A 1 200 ? 6.350 13.640 50.567 1.00 14.61 ? 200 LYS A CA 1 ATOM 1581 C C . LYS A 1 200 ? 6.359 13.796 49.050 1.00 15.19 ? 200 LYS A C 1 ATOM 1582 O O . LYS A 1 200 ? 5.351 14.182 48.453 1.00 15.11 ? 200 LYS A O 1 ATOM 1583 C CB . LYS A 1 200 ? 7.067 14.822 51.223 1.00 16.81 ? 200 LYS A CB 1 ATOM 1584 C CG . LYS A 1 200 ? 6.737 14.959 52.701 1.00 24.08 ? 200 LYS A CG 1 ATOM 1585 C CD . LYS A 1 200 ? 7.512 16.082 53.375 1.00 28.52 ? 200 LYS A CD 1 ATOM 1586 C CE . LYS A 1 200 ? 7.050 16.275 54.821 1.00 31.53 ? 200 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 200 ? 7.086 14.993 55.595 1.00 35.39 ? 200 LYS A NZ 1 ATOM 1588 N N . LEU A 1 201 ? 7.497 13.497 48.427 1.00 14.24 ? 201 LEU A N 1 ATOM 1589 C CA . LEU A 1 201 ? 7.610 13.581 46.976 1.00 13.14 ? 201 LEU A CA 1 ATOM 1590 C C . LEU A 1 201 ? 6.626 12.610 46.338 1.00 14.37 ? 201 LEU A C 1 ATOM 1591 O O . LEU A 1 201 ? 5.934 12.964 45.383 1.00 15.13 ? 201 LEU A O 1 ATOM 1592 C CB . LEU A 1 201 ? 9.033 13.239 46.523 1.00 12.18 ? 201 LEU A CB 1 ATOM 1593 C CG . LEU A 1 201 ? 10.145 14.243 46.849 1.00 14.16 ? 201 LEU A CG 1 ATOM 1594 C CD1 . LEU A 1 201 ? 11.495 13.635 46.468 1.00 12.72 ? 201 LEU A CD1 1 ATOM 1595 C CD2 . LEU A 1 201 ? 9.917 15.563 46.098 1.00 12.33 ? 201 LEU A CD2 1 ATOM 1596 N N . SER A 1 202 ? 6.562 11.388 46.867 1.00 12.60 ? 202 SER A N 1 ATOM 1597 C CA . SER A 1 202 ? 5.652 10.377 46.337 1.00 13.59 ? 202 SER A CA 1 ATOM 1598 C C . SER A 1 202 ? 4.197 10.830 46.409 1.00 14.30 ? 202 SER A C 1 ATOM 1599 O O . SER A 1 202 ? 3.425 10.606 45.474 1.00 13.77 ? 202 SER A O 1 ATOM 1600 C CB . SER A 1 202 ? 5.802 9.053 47.097 1.00 13.14 ? 202 SER A CB 1 ATOM 1601 O OG . SER A 1 202 ? 7.037 8.430 46.798 1.00 13.39 ? 202 SER A OG 1 ATOM 1602 N N . PHE A 1 203 ? 3.824 11.462 47.519 1.00 15.07 ? 203 PHE A N 1 ATOM 1603 C CA . PHE A 1 203 ? 2.453 11.927 47.682 1.00 15.86 ? 203 PHE A CA 1 ATOM 1604 C C . PHE A 1 203 ? 2.120 13.060 46.722 1.00 15.44 ? 203 PHE A C 1 ATOM 1605 O O . PHE A 1 203 ? 1.093 13.017 46.050 1.00 16.89 ? 203 PHE A O 1 ATOM 1606 C CB . PHE A 1 203 ? 2.190 12.382 49.121 1.00 15.87 ? 203 PHE A CB 1 ATOM 1607 C CG . PHE A 1 203 ? 0.807 12.940 49.325 1.00 18.16 ? 203 PHE A CG 1 ATOM 1608 C CD1 . PHE A 1 203 ? 0.602 14.315 49.412 1.00 20.41 ? 203 PHE A CD1 1 ATOM 1609 C CD2 . PHE A 1 203 ? -0.298 12.094 49.370 1.00 17.94 ? 203 PHE A CD2 1 ATOM 1610 C CE1 . PHE A 1 203 ? -0.691 14.840 49.536 1.00 21.28 ? 203 PHE A CE1 1 ATOM 1611 C CE2 . PHE A 1 203 ? -1.586 12.606 49.493 1.00 18.82 ? 203 PHE A CE2 1 ATOM 1612 C CZ . PHE A 1 203 ? -1.783 13.981 49.576 1.00 20.28 ? 203 PHE A CZ 1 ATOM 1613 N N . GLN A 1 204 ? 2.986 14.066 46.647 1.00 15.22 ? 204 GLN A N 1 ATOM 1614 C CA . GLN A 1 204 ? 2.739 15.203 45.759 1.00 15.97 ? 204 GLN A CA 1 ATOM 1615 C C . GLN A 1 204 ? 2.696 14.802 44.287 1.00 16.78 ? 204 GLN A C 1 ATOM 1616 O O . GLN A 1 204 ? 1.914 15.353 43.507 1.00 17.51 ? 204 GLN A O 1 ATOM 1617 C CB . GLN A 1 204 ? 3.810 16.279 45.959 1.00 15.83 ? 204 GLN A CB 1 ATOM 1618 C CG . GLN A 1 204 ? 3.746 16.997 47.294 1.00 14.76 ? 204 GLN A CG 1 ATOM 1619 C CD . GLN A 1 204 ? 2.425 17.702 47.498 1.00 16.94 ? 204 GLN A CD 1 ATOM 1620 O OE1 . GLN A 1 204 ? 1.882 18.301 46.570 1.00 18.10 ? 204 GLN A OE1 1 ATOM 1621 N NE2 . GLN A 1 204 ? 1.905 17.646 48.719 1.00 17.99 ? 204 GLN A NE2 1 ATOM 1622 N N . ILE A 1 205 ? 3.539 13.849 43.902 1.00 14.49 ? 205 ILE A N 1 ATOM 1623 C CA . ILE A 1 205 ? 3.581 13.403 42.516 1.00 14.66 ? 205 ILE A CA 1 ATOM 1624 C C . ILE A 1 205 ? 2.318 12.643 42.164 1.00 15.56 ? 205 ILE A C 1 ATOM 1625 O O . ILE A 1 205 ? 1.643 12.965 41.188 1.00 16.81 ? 205 ILE A O 1 ATOM 1626 C CB . ILE A 1 205 ? 4.811 12.492 42.245 1.00 14.01 ? 205 ILE A CB 1 ATOM 1627 C CG1 . ILE A 1 205 ? 6.100 13.316 42.358 1.00 13.34 ? 205 ILE A CG1 1 ATOM 1628 C CG2 . ILE A 1 205 ? 4.696 11.848 40.863 1.00 12.78 ? 205 ILE A CG2 1 ATOM 1629 C CD1 . ILE A 1 205 ? 7.374 12.500 42.300 1.00 13.68 ? 205 ILE A CD1 1 ATOM 1630 N N . ARG A 1 206 ? 1.993 11.635 42.964 1.00 15.42 ? 206 ARG A N 1 ATOM 1631 C CA . ARG A 1 206 ? 0.807 10.827 42.710 1.00 16.38 ? 206 ARG A CA 1 ATOM 1632 C C . ARG A 1 206 ? -0.509 11.625 42.685 1.00 15.94 ? 206 ARG A C 1 ATOM 1633 O O . ARG A 1 206 ? -1.402 11.312 41.905 1.00 15.67 ? 206 ARG A O 1 ATOM 1634 C CB . ARG A 1 206 ? 0.703 9.702 43.751 1.00 17.46 ? 206 ARG A CB 1 ATOM 1635 C CG . ARG A 1 206 ? -0.365 8.656 43.418 1.00 18.36 ? 206 ARG A CG 1 ATOM 1636 C CD . ARG A 1 206 ? -0.500 7.618 44.519 1.00 21.62 ? 206 ARG A CD 1 ATOM 1637 N NE . ARG A 1 206 ? -0.981 8.227 45.755 1.00 23.23 ? 206 ARG A NE 1 ATOM 1638 C CZ . ARG A 1 206 ? -2.235 8.620 45.958 1.00 24.93 ? 206 ARG A CZ 1 ATOM 1639 N NH1 . ARG A 1 206 ? -3.150 8.460 45.010 1.00 23.84 ? 206 ARG A NH1 1 ATOM 1640 N NH2 . ARG A 1 206 ? -2.569 9.195 47.104 1.00 24.65 ? 206 ARG A NH2 1 ATOM 1641 N N . THR A 1 207 ? -0.625 12.652 43.524 1.00 16.09 ? 207 THR A N 1 ATOM 1642 C CA . THR A 1 207 ? -1.851 13.448 43.591 1.00 17.47 ? 207 THR A CA 1 ATOM 1643 C C . THR A 1 207 ? -1.891 14.656 42.657 1.00 18.83 ? 207 THR A C 1 ATOM 1644 O O . THR A 1 207 ? -2.876 15.397 42.640 1.00 19.48 ? 207 THR A O 1 ATOM 1645 C CB . THR A 1 207 ? -2.134 13.940 45.039 1.00 17.46 ? 207 THR A CB 1 ATOM 1646 O OG1 . THR A 1 207 ? -1.044 14.746 45.505 1.00 19.11 ? 207 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 207 ? -2.325 12.757 45.977 1.00 17.60 ? 207 THR A CG2 1 ATOM 1648 N N . SER A 1 208 ? -0.833 14.858 41.878 1.00 18.55 ? 208 SER A N 1 ATOM 1649 C CA . SER A 1 208 ? -0.793 15.990 40.947 1.00 19.68 ? 208 SER A CA 1 ATOM 1650 C C . SER A 1 208 ? -1.637 15.699 39.701 1.00 18.74 ? 208 SER A C 1 ATOM 1651 O O . SER A 1 208 ? -1.920 14.540 39.392 1.00 17.98 ? 208 SER A O 1 ATOM 1652 C CB . SER A 1 208 ? 0.656 16.294 40.523 1.00 19.71 ? 208 SER A CB 1 ATOM 1653 O OG . SER A 1 208 ? 1.200 15.244 39.734 1.00 21.16 ? 208 SER A OG 1 ATOM 1654 N N . GLY A 1 209 ? -2.046 16.754 39.000 1.00 17.40 ? 209 GLY A N 1 ATOM 1655 C CA . GLY A 1 209 ? -2.827 16.571 37.790 1.00 18.37 ? 209 GLY A CA 1 ATOM 1656 C C . GLY A 1 209 ? -1.915 16.343 36.599 1.00 19.85 ? 209 GLY A C 1 ATOM 1657 O O . GLY A 1 209 ? -0.713 16.142 36.767 1.00 21.26 ? 209 GLY A O 1 ATOM 1658 N N . ALA A 1 210 ? -2.468 16.384 35.392 1.00 20.81 ? 210 ALA A N 1 ATOM 1659 C CA . ALA A 1 210 ? -1.674 16.173 34.186 1.00 21.72 ? 210 ALA A CA 1 ATOM 1660 C C . ALA A 1 210 ? -0.516 17.167 34.036 1.00 22.94 ? 210 ALA A C 1 ATOM 1661 O O . ALA A 1 210 ? 0.507 16.843 33.433 1.00 23.31 ? 210 ALA A O 1 ATOM 1662 C CB . ALA A 1 210 ? -2.573 16.229 32.958 1.00 22.22 ? 210 ALA A CB 1 ATOM 1663 N N . ASN A 1 211 ? -0.660 18.372 34.580 1.00 22.75 ? 211 ASN A N 1 ATOM 1664 C CA . ASN A 1 211 ? 0.413 19.349 34.466 1.00 24.51 ? 211 ASN A CA 1 ATOM 1665 C C . ASN A 1 211 ? 1.572 19.093 35.443 1.00 24.73 ? 211 ASN A C 1 ATOM 1666 O O . ASN A 1 211 ? 2.564 19.820 35.433 1.00 25.44 ? 211 ASN A O 1 ATOM 1667 C CB . ASN A 1 211 ? -0.125 20.775 34.651 1.00 24.96 ? 211 ASN A CB 1 ATOM 1668 C CG . ASN A 1 211 ? -0.695 21.020 36.037 1.00 26.70 ? 211 ASN A CG 1 ATOM 1669 O OD1 . ASN A 1 211 ? -0.452 20.258 36.974 1.00 27.80 ? 211 ASN A OD1 1 ATOM 1670 N ND2 . ASN A 1 211 ? -1.446 22.105 36.176 1.00 27.09 ? 211 ASN A ND2 1 ATOM 1671 N N . GLY A 1 212 ? 1.439 18.068 36.283 1.00 23.02 ? 212 GLY A N 1 ATOM 1672 C CA . GLY A 1 212 ? 2.489 17.729 37.232 1.00 22.71 ? 212 GLY A CA 1 ATOM 1673 C C . GLY A 1 212 ? 2.765 18.704 38.367 1.00 22.89 ? 212 GLY A C 1 ATOM 1674 O O . GLY A 1 212 ? 3.714 18.510 39.133 1.00 22.91 ? 212 GLY A O 1 ATOM 1675 N N . MET A 1 213 ? 1.950 19.749 38.490 1.00 23.03 ? 213 MET A N 1 ATOM 1676 C CA . MET A 1 213 ? 2.137 20.747 39.546 1.00 24.30 ? 213 MET A CA 1 ATOM 1677 C C . MET A 1 213 ? 1.788 20.209 40.932 1.00 23.32 ? 213 MET A C 1 ATOM 1678 O O . MET A 1 213 ? 0.697 19.681 41.133 1.00 23.17 ? 213 MET A O 1 ATOM 1679 C CB . MET A 1 213 ? 1.275 21.984 39.266 1.00 26.85 ? 213 MET A CB 1 ATOM 1680 C CG . MET A 1 213 ? 1.645 22.740 38.005 1.00 32.81 ? 213 MET A CG 1 ATOM 1681 S SD . MET A 1 213 ? 3.342 23.348 38.047 1.00 40.14 ? 213 MET A SD 1 ATOM 1682 C CE . MET A 1 213 ? 3.218 24.632 39.320 1.00 37.77 ? 213 MET A CE 1 ATOM 1683 N N . PHE A 1 214 ? 2.712 20.352 41.881 1.00 22.19 ? 214 PHE A N 1 ATOM 1684 C CA . PHE A 1 214 ? 2.496 19.901 43.259 1.00 22.38 ? 214 PHE A CA 1 ATOM 1685 C C . PHE A 1 214 ? 1.523 20.842 43.953 1.00 24.23 ? 214 PHE A C 1 ATOM 1686 O O . PHE A 1 214 ? 1.575 22.050 43.743 1.00 24.48 ? 214 PHE A O 1 ATOM 1687 C CB . PHE A 1 214 ? 3.804 19.934 44.055 1.00 21.34 ? 214 PHE A CB 1 ATOM 1688 C CG . PHE A 1 214 ? 4.769 18.834 43.715 1.00 18.85 ? 214 PHE A CG 1 ATOM 1689 C CD1 . PHE A 1 214 ? 4.562 18.007 42.618 1.00 18.61 ? 214 PHE A CD1 1 ATOM 1690 C CD2 . PHE A 1 214 ? 5.903 18.635 44.498 1.00 18.98 ? 214 PHE A CD2 1 ATOM 1691 C CE1 . PHE A 1 214 ? 5.472 16.997 42.307 1.00 18.71 ? 214 PHE A CE1 1 ATOM 1692 C CE2 . PHE A 1 214 ? 6.815 17.631 44.195 1.00 18.28 ? 214 PHE A CE2 1 ATOM 1693 C CZ . PHE A 1 214 ? 6.599 16.811 43.098 1.00 17.30 ? 214 PHE A CZ 1 ATOM 1694 N N . SER A 1 215 ? 0.649 20.298 44.792 1.00 25.84 ? 215 SER A N 1 ATOM 1695 C CA . SER A 1 215 ? -0.297 21.136 45.521 1.00 27.24 ? 215 SER A CA 1 ATOM 1696 C C . SER A 1 215 ? 0.480 21.874 46.610 1.00 28.53 ? 215 SER A C 1 ATOM 1697 O O . SER A 1 215 ? 0.083 22.948 47.062 1.00 28.78 ? 215 SER A O 1 ATOM 1698 C CB . SER A 1 215 ? -1.408 20.281 46.131 1.00 27.35 ? 215 SER A CB 1 ATOM 1699 O OG . SER A 1 215 ? -0.868 19.259 46.941 1.00 32.69 ? 215 SER A OG 1 ATOM 1700 N N . GLU A 1 216 ? 1.599 21.286 47.021 1.00 28.83 ? 216 GLU A N 1 ATOM 1701 C CA . GLU A 1 216 ? 2.474 21.877 48.030 1.00 29.65 ? 216 GLU A CA 1 ATOM 1702 C C . GLU A 1 216 ? 3.903 21.528 47.641 1.00 27.18 ? 216 GLU A C 1 ATOM 1703 O O . GLU A 1 216 ? 4.216 20.370 47.372 1.00 26.70 ? 216 GLU A O 1 ATOM 1704 C CB . GLU A 1 216 ? 2.167 21.320 49.426 1.00 33.58 ? 216 GLU A CB 1 ATOM 1705 C CG . GLU A 1 216 ? 0.746 21.599 49.919 1.00 42.61 ? 216 GLU A CG 1 ATOM 1706 C CD . GLU A 1 216 ? 0.485 21.043 51.314 1.00 47.39 ? 216 GLU A CD 1 ATOM 1707 O OE1 . GLU A 1 216 ? 1.153 21.491 52.275 1.00 49.58 ? 216 GLU A OE1 1 ATOM 1708 O OE2 . GLU A 1 216 ? -0.387 20.154 51.449 1.00 50.85 ? 216 GLU A OE2 1 ATOM 1709 N N . ALA A 1 217 ? 4.764 22.535 47.597 1.00 25.47 ? 217 ALA A N 1 ATOM 1710 C CA . ALA A 1 217 ? 6.156 22.330 47.236 1.00 23.25 ? 217 ALA A CA 1 ATOM 1711 C C . ALA A 1 217 ? 6.864 21.481 48.284 1.00 22.31 ? 217 ALA A C 1 ATOM 1712 O O . ALA A 1 217 ? 6.484 21.479 49.461 1.00 23.09 ? 217 ALA A O 1 ATOM 1713 C CB . ALA A 1 217 ? 6.858 23.672 47.100 1.00 22.35 ? 217 ALA A CB 1 ATOM 1714 N N . VAL A 1 218 ? 7.892 20.759 47.845 1.00 20.06 ? 218 VAL A N 1 ATOM 1715 C CA . VAL A 1 218 ? 8.680 19.916 48.730 1.00 18.20 ? 218 VAL A CA 1 ATOM 1716 C C . VAL A 1 218 ? 10.094 20.482 48.823 1.00 17.19 ? 218 VAL A C 1 ATOM 1717 O O . VAL A 1 218 ? 10.748 20.745 47.811 1.00 17.33 ? 218 VAL A O 1 ATOM 1718 C CB . VAL A 1 218 ? 8.753 18.468 48.214 1.00 18.24 ? 218 VAL A CB 1 ATOM 1719 C CG1 . VAL A 1 218 ? 9.578 17.609 49.184 1.00 16.49 ? 218 VAL A CG1 1 ATOM 1720 C CG2 . VAL A 1 218 ? 7.347 17.906 48.062 1.00 16.08 ? 218 VAL A CG2 1 ATOM 1721 N N . GLU A 1 219 ? 10.567 20.671 50.045 1.00 17.42 ? 219 GLU A N 1 ATOM 1722 C CA . GLU A 1 219 ? 11.893 21.225 50.238 1.00 18.34 ? 219 GLU A CA 1 ATOM 1723 C C . GLU A 1 219 ? 12.999 20.182 50.194 1.00 18.24 ? 219 GLU A C 1 ATOM 1724 O O . GLU A 1 219 ? 12.954 19.168 50.894 1.00 18.18 ? 219 GLU A O 1 ATOM 1725 C CB . GLU A 1 219 ? 11.957 21.973 51.568 1.00 20.16 ? 219 GLU A CB 1 ATOM 1726 C CG . GLU A 1 219 ? 13.301 22.613 51.864 1.00 22.85 ? 219 GLU A CG 1 ATOM 1727 C CD . GLU A 1 219 ? 13.316 23.291 53.221 1.00 26.81 ? 219 GLU A CD 1 ATOM 1728 O OE1 . GLU A 1 219 ? 12.606 24.306 53.395 1.00 28.95 ? 219 GLU A OE1 1 ATOM 1729 O OE2 . GLU A 1 219 ? 14.031 22.803 54.120 1.00 28.35 ? 219 GLU A OE2 1 ATOM 1730 N N . LEU A 1 220 ? 13.987 20.438 49.347 1.00 17.74 ? 220 LEU A N 1 ATOM 1731 C CA . LEU A 1 220 ? 15.140 19.564 49.232 1.00 18.10 ? 220 LEU A CA 1 ATOM 1732 C C . LEU A 1 220 ? 16.369 20.429 49.495 1.00 18.80 ? 220 LEU A C 1 ATOM 1733 O O . LEU A 1 220 ? 16.248 21.643 49.711 1.00 18.70 ? 220 LEU A O 1 ATOM 1734 C CB . LEU A 1 220 ? 15.211 18.924 47.842 1.00 16.67 ? 220 LEU A CB 1 ATOM 1735 C CG . LEU A 1 220 ? 14.186 17.807 47.608 1.00 17.77 ? 220 LEU A CG 1 ATOM 1736 C CD1 . LEU A 1 220 ? 14.330 17.276 46.188 1.00 15.43 ? 220 LEU A CD1 1 ATOM 1737 C CD2 . LEU A 1 220 ? 14.392 16.682 48.642 1.00 16.61 ? 220 LEU A CD2 1 ATOM 1738 N N . GLU A 1 221 ? 17.542 19.811 49.496 1.00 17.43 ? 221 GLU A N 1 ATOM 1739 C CA . GLU A 1 221 ? 18.770 20.543 49.742 1.00 17.34 ? 221 GLU A CA 1 ATOM 1740 C C . GLU A 1 221 ? 19.846 20.150 48.756 1.00 18.31 ? 221 GLU A C 1 ATOM 1741 O O . GLU A 1 221 ? 19.890 19.013 48.287 1.00 17.39 ? 221 GLU A O 1 ATOM 1742 C CB . GLU A 1 221 ? 19.279 20.271 51.160 1.00 17.89 ? 221 GLU A CB 1 ATOM 1743 C CG . GLU A 1 221 ? 18.324 20.700 52.254 1.00 20.37 ? 221 GLU A CG 1 ATOM 1744 C CD . GLU A 1 221 ? 18.929 20.598 53.641 1.00 20.99 ? 221 GLU A CD 1 ATOM 1745 O OE1 . GLU A 1 221 ? 20.127 20.260 53.763 1.00 22.06 ? 221 GLU A OE1 1 ATOM 1746 O OE2 . GLU A 1 221 ? 18.199 20.864 54.615 1.00 22.44 ? 221 GLU A OE2 1 ATOM 1747 N N . ARG A 1 222 ? 20.698 21.112 48.426 1.00 18.48 ? 222 ARG A N 1 ATOM 1748 C CA . ARG A 1 222 ? 21.813 20.860 47.539 1.00 18.98 ? 222 ARG A CA 1 ATOM 1749 C C . ARG A 1 222 ? 22.862 20.231 48.449 1.00 19.53 ? 222 ARG A C 1 ATOM 1750 O O . ARG A 1 222 ? 22.662 20.157 49.661 1.00 19.11 ? 222 ARG A O 1 ATOM 1751 C CB . ARG A 1 222 ? 22.333 22.174 46.943 1.00 20.63 ? 222 ARG A CB 1 ATOM 1752 C CG . ARG A 1 222 ? 21.369 22.845 45.974 1.00 21.57 ? 222 ARG A CG 1 ATOM 1753 C CD . ARG A 1 222 ? 21.092 21.952 44.784 1.00 21.75 ? 222 ARG A CD 1 ATOM 1754 N NE . ARG A 1 222 ? 20.119 22.547 43.875 1.00 24.87 ? 222 ARG A NE 1 ATOM 1755 C CZ . ARG A 1 222 ? 19.527 21.889 42.881 1.00 26.99 ? 222 ARG A CZ 1 ATOM 1756 N NH1 . ARG A 1 222 ? 19.807 20.607 42.663 1.00 25.65 ? 222 ARG A NH1 1 ATOM 1757 N NH2 . ARG A 1 222 ? 18.650 22.512 42.105 1.00 27.11 ? 222 ARG A NH2 1 ATOM 1758 N N . ALA A 1 223 ? 23.972 19.780 47.874 1.00 21.83 ? 223 ALA A N 1 ATOM 1759 C CA . ALA A 1 223 ? 25.037 19.151 48.653 1.00 23.37 ? 223 ALA A CA 1 ATOM 1760 C C . ALA A 1 223 ? 25.514 20.056 49.783 1.00 25.12 ? 223 ALA A C 1 ATOM 1761 O O . ALA A 1 223 ? 25.741 19.600 50.901 1.00 25.63 ? 223 ALA A O 1 ATOM 1762 C CB . ALA A 1 223 ? 26.208 18.790 47.741 1.00 21.74 ? 223 ALA A CB 1 ATOM 1763 N N . ASN A 1 224 ? 25.647 21.343 49.481 1.00 27.57 ? 224 ASN A N 1 ATOM 1764 C CA . ASN A 1 224 ? 26.107 22.330 50.450 1.00 29.78 ? 224 ASN A CA 1 ATOM 1765 C C . ASN A 1 224 ? 25.068 22.679 51.506 1.00 29.51 ? 224 ASN A C 1 ATOM 1766 O O . ASN A 1 224 ? 25.363 23.419 52.439 1.00 32.14 ? 224 ASN A O 1 ATOM 1767 C CB . ASN A 1 224 ? 26.531 23.605 49.721 1.00 32.62 ? 224 ASN A CB 1 ATOM 1768 C CG . ASN A 1 224 ? 25.426 24.162 48.845 1.00 35.61 ? 224 ASN A CG 1 ATOM 1769 O OD1 . ASN A 1 224 ? 24.342 24.474 49.328 1.00 37.03 ? 224 ASN A OD1 1 ATOM 1770 N ND2 . ASN A 1 224 ? 25.692 24.280 47.547 1.00 38.49 ? 224 ASN A ND2 1 ATOM 1771 N N . GLY A 1 225 ? 23.852 22.165 51.363 1.00 28.24 ? 225 GLY A N 1 ATOM 1772 C CA . GLY A 1 225 ? 22.821 22.462 52.343 1.00 26.78 ? 225 GLY A CA 1 ATOM 1773 C C . GLY A 1 225 ? 21.815 23.522 51.918 1.00 26.70 ? 225 GLY A C 1 ATOM 1774 O O . GLY A 1 225 ? 20.783 23.698 52.572 1.00 25.65 ? 225 GLY A O 1 ATOM 1775 N N . LYS A 1 226 ? 22.108 24.235 50.833 1.00 25.43 ? 226 LYS A N 1 ATOM 1776 C CA . LYS A 1 226 ? 21.202 25.268 50.332 1.00 25.21 ? 226 LYS A CA 1 ATOM 1777 C C . LYS A 1 226 ? 19.848 24.645 50.002 1.00 24.44 ? 226 LYS A C 1 ATOM 1778 O O . LYS A 1 226 ? 19.771 23.627 49.311 1.00 23.75 ? 226 LYS A O 1 ATOM 1779 C CB . LYS A 1 226 ? 21.774 25.920 49.069 1.00 26.94 ? 226 LYS A CB 1 ATOM 1780 C CG . LYS A 1 226 ? 20.857 26.963 48.438 1.00 29.43 ? 226 LYS A CG 1 ATOM 1781 C CD . LYS A 1 226 ? 21.290 27.326 47.019 1.00 33.01 ? 226 LYS A CD 1 ATOM 1782 C CE . LYS A 1 226 ? 22.561 28.165 46.996 1.00 36.95 ? 226 LYS A CE 1 ATOM 1783 N NZ . LYS A 1 226 ? 23.778 27.434 47.445 1.00 40.06 ? 226 LYS A NZ 1 ATOM 1784 N N . LYS A 1 227 ? 18.781 25.266 50.485 1.00 22.51 ? 227 LYS A N 1 ATOM 1785 C CA . LYS A 1 227 ? 17.440 24.754 50.242 1.00 23.42 ? 227 LYS A CA 1 ATOM 1786 C C . LYS A 1 227 ? 16.857 25.182 48.905 1.00 22.54 ? 227 LYS A C 1 ATOM 1787 O O . LYS A 1 227 ? 17.176 26.246 48.386 1.00 21.95 ? 227 LYS A O 1 ATOM 1788 C CB . LYS A 1 227 ? 16.492 25.216 51.353 1.00 24.91 ? 227 LYS A CB 1 ATOM 1789 C CG . LYS A 1 227 ? 17.011 24.932 52.751 1.00 29.78 ? 227 LYS A CG 1 ATOM 1790 C CD . LYS A 1 227 ? 15.992 25.281 53.815 1.00 33.16 ? 227 LYS A CD 1 ATOM 1791 C CE . LYS A 1 227 ? 16.564 25.065 55.210 1.00 34.65 ? 227 LYS A CE 1 ATOM 1792 N NZ . LYS A 1 227 ? 17.086 23.683 55.421 1.00 35.39 ? 227 LYS A NZ 1 ATOM 1793 N N . TYR A 1 228 ? 16.017 24.321 48.342 1.00 22.45 ? 228 TYR A N 1 ATOM 1794 C CA . TYR A 1 228 ? 15.304 24.623 47.108 1.00 22.51 ? 228 TYR A CA 1 ATOM 1795 C C . TYR A 1 228 ? 13.977 23.889 47.187 1.00 23.23 ? 228 TYR A C 1 ATOM 1796 O O . TYR A 1 228 ? 13.802 22.987 48.014 1.00 22.21 ? 228 TYR A O 1 ATOM 1797 C CB . TYR A 1 228 ? 16.083 24.234 45.842 1.00 22.76 ? 228 TYR A CB 1 ATOM 1798 C CG . TYR A 1 228 ? 16.314 22.759 45.593 1.00 23.53 ? 228 TYR A CG 1 ATOM 1799 C CD1 . TYR A 1 228 ? 17.385 22.091 46.184 1.00 22.23 ? 228 TYR A CD1 1 ATOM 1800 C CD2 . TYR A 1 228 ? 15.520 22.058 44.682 1.00 23.08 ? 228 TYR A CD2 1 ATOM 1801 C CE1 . TYR A 1 228 ? 17.672 20.767 45.864 1.00 22.34 ? 228 TYR A CE1 1 ATOM 1802 C CE2 . TYR A 1 228 ? 15.798 20.734 44.355 1.00 21.86 ? 228 TYR A CE2 1 ATOM 1803 C CZ . TYR A 1 228 ? 16.878 20.098 44.948 1.00 22.15 ? 228 TYR A CZ 1 ATOM 1804 O OH . TYR A 1 228 ? 17.185 18.802 44.604 1.00 21.59 ? 228 TYR A OH 1 ATOM 1805 N N . TYR A 1 229 ? 13.032 24.283 46.348 1.00 22.94 ? 229 TYR A N 1 ATOM 1806 C CA . TYR A 1 229 ? 11.728 23.666 46.398 1.00 22.72 ? 229 TYR A CA 1 ATOM 1807 C C . TYR A 1 229 ? 11.317 23.024 45.099 1.00 22.67 ? 229 TYR A C 1 ATOM 1808 O O . TYR A 1 229 ? 11.491 23.596 44.020 1.00 23.74 ? 229 TYR A O 1 ATOM 1809 C CB . TYR A 1 229 ? 10.686 24.698 46.836 1.00 23.56 ? 229 TYR A CB 1 ATOM 1810 C CG . TYR A 1 229 ? 10.983 25.253 48.204 1.00 25.20 ? 229 TYR A CG 1 ATOM 1811 C CD1 . TYR A 1 229 ? 12.017 26.173 48.394 1.00 26.94 ? 229 TYR A CD1 1 ATOM 1812 C CD2 . TYR A 1 229 ? 10.293 24.797 49.328 1.00 26.42 ? 229 TYR A CD2 1 ATOM 1813 C CE1 . TYR A 1 229 ? 12.365 26.619 49.668 1.00 27.88 ? 229 TYR A CE1 1 ATOM 1814 C CE2 . TYR A 1 229 ? 10.632 25.238 50.607 1.00 27.98 ? 229 TYR A CE2 1 ATOM 1815 C CZ . TYR A 1 229 ? 11.670 26.145 50.768 1.00 28.95 ? 229 TYR A CZ 1 ATOM 1816 O OH . TYR A 1 229 ? 12.027 26.557 52.031 1.00 32.49 ? 229 TYR A OH 1 ATOM 1817 N N . VAL A 1 230 ? 10.799 21.807 45.221 1.00 20.22 ? 230 VAL A N 1 ATOM 1818 C CA . VAL A 1 230 ? 10.316 21.054 44.080 1.00 19.34 ? 230 VAL A CA 1 ATOM 1819 C C . VAL A 1 230 ? 8.821 21.361 44.002 1.00 19.05 ? 230 VAL A C 1 ATOM 1820 O O . VAL A 1 230 ? 8.077 21.112 44.951 1.00 17.52 ? 230 VAL A O 1 ATOM 1821 C CB . VAL A 1 230 ? 10.530 19.545 44.279 1.00 17.70 ? 230 VAL A CB 1 ATOM 1822 C CG1 . VAL A 1 230 ? 10.009 18.788 43.068 1.00 17.15 ? 230 VAL A CG1 1 ATOM 1823 C CG2 . VAL A 1 230 ? 12.008 19.259 44.495 1.00 17.33 ? 230 VAL A CG2 1 ATOM 1824 N N . THR A 1 231 ? 8.393 21.918 42.875 1.00 19.38 ? 231 THR A N 1 ATOM 1825 C CA . THR A 1 231 ? 6.997 22.284 42.690 1.00 20.17 ? 231 THR A CA 1 ATOM 1826 C C . THR A 1 231 ? 6.321 21.502 41.571 1.00 20.59 ? 231 THR A C 1 ATOM 1827 O O . THR A 1 231 ? 5.112 21.624 41.362 1.00 22.06 ? 231 THR A O 1 ATOM 1828 C CB . THR A 1 231 ? 6.879 23.777 42.380 1.00 20.69 ? 231 THR A CB 1 ATOM 1829 O OG1 . THR A 1 231 ? 7.673 24.082 41.227 1.00 22.12 ? 231 THR A OG1 1 ATOM 1830 C CG2 . THR A 1 231 ? 7.365 24.603 43.567 1.00 20.38 ? 231 THR A CG2 1 ATOM 1831 N N . ALA A 1 232 ? 7.096 20.697 40.853 1.00 19.78 ? 232 ALA A N 1 ATOM 1832 C CA . ALA A 1 232 ? 6.544 19.907 39.762 1.00 19.32 ? 232 ALA A CA 1 ATOM 1833 C C . ALA A 1 232 ? 7.258 18.567 39.611 1.00 18.87 ? 232 ALA A C 1 ATOM 1834 O O . ALA A 1 232 ? 8.436 18.436 39.940 1.00 19.05 ? 232 ALA A O 1 ATOM 1835 C CB . ALA A 1 232 ? 6.630 20.692 38.457 1.00 20.12 ? 232 ALA A CB 1 ATOM 1836 N N . VAL A 1 233 ? 6.527 17.583 39.102 1.00 18.65 ? 233 VAL A N 1 ATOM 1837 C CA . VAL A 1 233 ? 7.046 16.235 38.891 1.00 18.42 ? 233 VAL A CA 1 ATOM 1838 C C . VAL A 1 233 ? 8.341 16.243 38.081 1.00 20.51 ? 233 VAL A C 1 ATOM 1839 O O . VAL A 1 233 ? 9.346 15.656 38.478 1.00 19.00 ? 233 VAL A O 1 ATOM 1840 C CB . VAL A 1 233 ? 6.009 15.373 38.137 1.00 17.90 ? 233 VAL A CB 1 ATOM 1841 C CG1 . VAL A 1 233 ? 6.593 14.004 37.820 1.00 16.33 ? 233 VAL A CG1 1 ATOM 1842 C CG2 . VAL A 1 233 ? 4.729 15.247 38.974 1.00 18.59 ? 233 VAL A CG2 1 ATOM 1843 N N . ASP A 1 234 ? 8.294 16.912 36.935 1.00 21.31 ? 234 ASP A N 1 ATOM 1844 C CA . ASP A 1 234 ? 9.432 17.010 36.030 1.00 23.58 ? 234 ASP A CA 1 ATOM 1845 C C . ASP A 1 234 ? 10.749 17.408 36.679 1.00 22.59 ? 234 ASP A C 1 ATOM 1846 O O . ASP A 1 234 ? 11.811 16.991 36.231 1.00 24.37 ? 234 ASP A O 1 ATOM 1847 C CB . ASP A 1 234 ? 9.103 17.993 34.909 1.00 27.74 ? 234 ASP A CB 1 ATOM 1848 C CG . ASP A 1 234 ? 8.549 17.307 33.683 1.00 32.01 ? 234 ASP A CG 1 ATOM 1849 O OD1 . ASP A 1 234 ? 7.952 16.212 33.824 1.00 33.90 ? 234 ASP A OD1 1 ATOM 1850 O OD2 . ASP A 1 234 ? 8.708 17.871 32.576 1.00 36.30 ? 234 ASP A OD2 1 ATOM 1851 N N . GLN A 1 235 ? 10.682 18.219 37.725 1.00 21.04 ? 235 GLN A N 1 ATOM 1852 C CA . GLN A 1 235 ? 11.884 18.667 38.412 1.00 20.75 ? 235 GLN A CA 1 ATOM 1853 C C . GLN A 1 235 ? 12.629 17.540 39.123 1.00 20.77 ? 235 GLN A C 1 ATOM 1854 O O . GLN A 1 235 ? 13.845 17.598 39.285 1.00 22.53 ? 235 GLN A O 1 ATOM 1855 C CB . GLN A 1 235 ? 11.522 19.730 39.446 1.00 20.42 ? 235 GLN A CB 1 ATOM 1856 C CG . GLN A 1 235 ? 10.986 21.017 38.867 1.00 22.83 ? 235 GLN A CG 1 ATOM 1857 C CD . GLN A 1 235 ? 10.340 21.887 39.924 1.00 24.71 ? 235 GLN A CD 1 ATOM 1858 O OE1 . GLN A 1 235 ? 10.797 21.946 41.063 1.00 25.47 ? 235 GLN A OE1 1 ATOM 1859 N NE2 . GLN A 1 235 ? 9.273 22.579 39.546 1.00 29.85 ? 235 GLN A NE2 1 ATOM 1860 N N . VAL A 1 236 ? 11.899 16.510 39.533 1.00 19.05 ? 236 VAL A N 1 ATOM 1861 C CA . VAL A 1 236 ? 12.492 15.420 40.294 1.00 17.99 ? 236 VAL A CA 1 ATOM 1862 C C . VAL A 1 236 ? 12.359 14.026 39.657 1.00 17.25 ? 236 VAL A C 1 ATOM 1863 O O . VAL A 1 236 ? 12.983 13.066 40.105 1.00 15.59 ? 236 VAL A O 1 ATOM 1864 C CB . VAL A 1 236 ? 11.866 15.431 41.722 1.00 19.38 ? 236 VAL A CB 1 ATOM 1865 C CG1 . VAL A 1 236 ? 10.417 14.943 41.662 1.00 16.66 ? 236 VAL A CG1 1 ATOM 1866 C CG2 . VAL A 1 236 ? 12.696 14.620 42.677 1.00 20.68 ? 236 VAL A CG2 1 ATOM 1867 N N . LYS A 1 237 ? 11.565 13.925 38.597 1.00 17.51 ? 237 LYS A N 1 ATOM 1868 C CA . LYS A 1 237 ? 11.346 12.649 37.927 1.00 17.82 ? 237 LYS A CA 1 ATOM 1869 C C . LYS A 1 237 ? 12.608 11.855 37.564 1.00 18.31 ? 237 LYS A C 1 ATOM 1870 O O . LYS A 1 237 ? 12.673 10.651 37.810 1.00 18.99 ? 237 LYS A O 1 ATOM 1871 C CB . LYS A 1 237 ? 10.487 12.852 36.671 1.00 18.66 ? 237 LYS A CB 1 ATOM 1872 C CG . LYS A 1 237 ? 10.190 11.555 35.932 1.00 21.65 ? 237 LYS A CG 1 ATOM 1873 C CD . LYS A 1 237 ? 9.396 11.760 34.645 1.00 21.40 ? 237 LYS A CD 1 ATOM 1874 C CE . LYS A 1 237 ? 7.917 11.960 34.911 1.00 21.50 ? 237 LYS A CE 1 ATOM 1875 N NZ . LYS A 1 237 ? 7.133 11.942 33.638 1.00 17.79 ? 237 LYS A NZ 1 ATOM 1876 N N . PRO A 1 238 ? 13.629 12.503 36.974 1.00 17.88 ? 238 PRO A N 1 ATOM 1877 C CA . PRO A 1 238 ? 14.820 11.717 36.633 1.00 17.62 ? 238 PRO A CA 1 ATOM 1878 C C . PRO A 1 238 ? 15.608 11.169 37.822 1.00 16.27 ? 238 PRO A C 1 ATOM 1879 O O . PRO A 1 238 ? 16.500 10.346 37.643 1.00 16.18 ? 238 PRO A O 1 ATOM 1880 C CB . PRO A 1 238 ? 15.642 12.679 35.770 1.00 17.33 ? 238 PRO A CB 1 ATOM 1881 C CG . PRO A 1 238 ? 15.260 14.006 36.284 1.00 20.63 ? 238 PRO A CG 1 ATOM 1882 C CD . PRO A 1 238 ? 13.767 13.893 36.505 1.00 19.11 ? 238 PRO A CD 1 ATOM 1883 N N . LYS A 1 239 ? 15.264 11.614 39.029 1.00 14.85 ? 239 LYS A N 1 ATOM 1884 C CA . LYS A 1 239 ? 15.943 11.167 40.248 1.00 13.34 ? 239 LYS A CA 1 ATOM 1885 C C . LYS A 1 239 ? 15.252 10.013 40.964 1.00 12.84 ? 239 LYS A C 1 ATOM 1886 O O . LYS A 1 239 ? 15.839 9.392 41.844 1.00 11.58 ? 239 LYS A O 1 ATOM 1887 C CB . LYS A 1 239 ? 16.055 12.321 41.239 1.00 13.31 ? 239 LYS A CB 1 ATOM 1888 C CG . LYS A 1 239 ? 16.911 13.463 40.762 1.00 14.56 ? 239 LYS A CG 1 ATOM 1889 C CD . LYS A 1 239 ? 17.045 14.529 41.839 1.00 17.51 ? 239 LYS A CD 1 ATOM 1890 C CE . LYS A 1 239 ? 17.884 15.692 41.339 1.00 19.81 ? 239 LYS A CE 1 ATOM 1891 N NZ . LYS A 1 239 ? 17.980 16.758 42.351 1.00 23.38 ? 239 LYS A NZ 1 ATOM 1892 N N . ILE A 1 240 ? 14.008 9.733 40.586 1.00 12.64 ? 240 ILE A N 1 ATOM 1893 C CA . ILE A 1 240 ? 13.218 8.699 41.241 1.00 12.99 ? 240 ILE A CA 1 ATOM 1894 C C . ILE A 1 240 ? 12.987 7.449 40.403 1.00 13.00 ? 240 ILE A C 1 ATOM 1895 O O . ILE A 1 240 ? 12.635 7.543 39.232 1.00 13.18 ? 240 ILE A O 1 ATOM 1896 C CB . ILE A 1 240 ? 11.841 9.272 41.653 1.00 14.05 ? 240 ILE A CB 1 ATOM 1897 C CG1 . ILE A 1 240 ? 12.039 10.541 42.490 1.00 13.34 ? 240 ILE A CG1 1 ATOM 1898 C CG2 . ILE A 1 240 ? 11.044 8.219 42.432 1.00 14.02 ? 240 ILE A CG2 1 ATOM 1899 C CD1 . ILE A 1 240 ? 10.759 11.307 42.764 1.00 14.39 ? 240 ILE A CD1 1 ATOM 1900 N N . ALA A 1 241 ? 13.170 6.279 41.017 1.00 12.72 ? 241 ALA A N 1 ATOM 1901 C CA . ALA A 1 241 ? 12.970 5.002 40.327 1.00 11.70 ? 241 ALA A CA 1 ATOM 1902 C C . ALA A 1 241 ? 11.649 4.348 40.726 1.00 11.97 ? 241 ALA A C 1 ATOM 1903 O O . ALA A 1 241 ? 11.037 3.643 39.928 1.00 10.96 ? 241 ALA A O 1 ATOM 1904 C CB . ALA A 1 241 ? 14.125 4.044 40.631 1.00 11.67 ? 241 ALA A CB 1 ATOM 1905 N N . LEU A 1 242 ? 11.224 4.586 41.967 1.00 11.56 ? 242 LEU A N 1 ATOM 1906 C CA . LEU A 1 242 ? 9.989 4.012 42.503 1.00 11.35 ? 242 LEU A CA 1 ATOM 1907 C C . LEU A 1 242 ? 9.268 5.023 43.371 1.00 12.56 ? 242 LEU A C 1 ATOM 1908 O O . LEU A 1 242 ? 9.906 5.800 44.082 1.00 12.67 ? 242 LEU A O 1 ATOM 1909 C CB . LEU A 1 242 ? 10.304 2.797 43.376 1.00 10.70 ? 242 LEU A CB 1 ATOM 1910 C CG . LEU A 1 242 ? 11.004 1.587 42.765 1.00 10.47 ? 242 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 242 ? 11.522 0.681 43.867 1.00 10.59 ? 242 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 242 ? 10.028 0.855 41.861 1.00 11.05 ? 242 LEU A CD2 1 ATOM 1913 N N . LEU A 1 243 ? 7.939 4.994 43.326 1.00 12.37 ? 243 LEU A N 1 ATOM 1914 C CA . LEU A 1 243 ? 7.122 5.886 44.142 1.00 12.99 ? 243 LEU A CA 1 ATOM 1915 C C . LEU A 1 243 ? 6.424 5.080 45.222 1.00 12.89 ? 243 LEU A C 1 ATOM 1916 O O . LEU A 1 243 ? 5.986 3.951 44.983 1.00 12.29 ? 243 LEU A O 1 ATOM 1917 C CB . LEU A 1 243 ? 6.044 6.584 43.308 1.00 14.13 ? 243 LEU A CB 1 ATOM 1918 C CG . LEU A 1 243 ? 6.448 7.641 42.280 1.00 15.41 ? 243 LEU A CG 1 ATOM 1919 C CD1 . LEU A 1 243 ? 5.187 8.127 41.560 1.00 16.71 ? 243 LEU A CD1 1 ATOM 1920 C CD2 . LEU A 1 243 ? 7.160 8.794 42.968 1.00 12.53 ? 243 LEU A CD2 1 ATOM 1921 N N . LYS A 1 244 ? 6.329 5.659 46.411 1.00 12.35 ? 244 LYS A N 1 ATOM 1922 C CA . LYS A 1 244 ? 5.633 4.994 47.491 1.00 14.00 ? 244 LYS A CA 1 ATOM 1923 C C . LYS A 1 244 ? 4.176 5.367 47.271 1.00 15.44 ? 244 LYS A C 1 ATOM 1924 O O . LYS A 1 244 ? 3.887 6.438 46.749 1.00 16.51 ? 244 LYS A O 1 ATOM 1925 C CB . LYS A 1 244 ? 6.085 5.525 48.848 1.00 15.91 ? 244 LYS A CB 1 ATOM 1926 C CG . LYS A 1 244 ? 5.387 4.842 50.010 1.00 16.41 ? 244 LYS A CG 1 ATOM 1927 C CD . LYS A 1 244 ? 5.899 5.338 51.336 1.00 19.97 ? 244 LYS A CD 1 ATOM 1928 C CE . LYS A 1 244 ? 5.257 4.560 52.478 1.00 22.17 ? 244 LYS A CE 1 ATOM 1929 N NZ . LYS A 1 244 ? 5.686 5.071 53.817 1.00 24.89 ? 244 LYS A NZ 1 ATOM 1930 N N . PHE A 1 245 ? 3.255 4.489 47.625 1.00 15.85 ? 245 PHE A N 1 ATOM 1931 C CA . PHE A 1 245 ? 1.858 4.839 47.465 1.00 18.70 ? 245 PHE A CA 1 ATOM 1932 C C . PHE A 1 245 ? 1.460 5.472 48.793 1.00 20.18 ? 245 PHE A C 1 ATOM 1933 O O . PHE A 1 245 ? 1.292 4.777 49.789 1.00 20.59 ? 245 PHE A O 1 ATOM 1934 C CB . PHE A 1 245 ? 1.016 3.596 47.182 1.00 19.01 ? 245 PHE A CB 1 ATOM 1935 C CG . PHE A 1 245 ? -0.363 3.907 46.667 1.00 21.85 ? 245 PHE A CG 1 ATOM 1936 C CD1 . PHE A 1 245 ? -1.267 4.628 47.443 1.00 23.69 ? 245 PHE A CD1 1 ATOM 1937 C CD2 . PHE A 1 245 ? -0.750 3.499 45.394 1.00 22.71 ? 245 PHE A CD2 1 ATOM 1938 C CE1 . PHE A 1 245 ? -2.537 4.942 46.957 1.00 23.47 ? 245 PHE A CE1 1 ATOM 1939 C CE2 . PHE A 1 245 ? -2.015 3.806 44.898 1.00 22.36 ? 245 PHE A CE2 1 ATOM 1940 C CZ . PHE A 1 245 ? -2.908 4.529 45.682 1.00 23.23 ? 245 PHE A CZ 1 ATOM 1941 N N . VAL A 1 246 ? 1.344 6.795 48.811 1.00 22.51 ? 246 VAL A N 1 ATOM 1942 C CA . VAL A 1 246 ? 0.979 7.516 50.029 1.00 25.83 ? 246 VAL A CA 1 ATOM 1943 C C . VAL A 1 246 ? -0.465 8.028 49.944 1.00 29.64 ? 246 VAL A C 1 ATOM 1944 O O . VAL A 1 246 ? -0.811 8.774 49.029 1.00 28.24 ? 246 VAL A O 1 ATOM 1945 C CB . VAL A 1 246 ? 1.939 8.712 50.264 1.00 23.45 ? 246 VAL A CB 1 ATOM 1946 C CG1 . VAL A 1 246 ? 1.564 9.450 51.546 1.00 22.92 ? 246 VAL A CG1 1 ATOM 1947 C CG2 . VAL A 1 246 ? 3.368 8.218 50.352 1.00 21.94 ? 246 VAL A CG2 1 ATOM 1948 N N . ASP A 1 247 ? -1.301 7.623 50.901 1.00 35.55 ? 247 ASP A N 1 ATOM 1949 C CA . ASP A 1 247 ? -2.708 8.032 50.926 1.00 42.12 ? 247 ASP A CA 1 ATOM 1950 C C . ASP A 1 247 ? -2.934 9.499 51.258 1.00 45.29 ? 247 ASP A C 1 ATOM 1951 O O . ASP A 1 247 ? -3.469 10.250 50.445 1.00 46.46 ? 247 ASP A O 1 ATOM 1952 C CB . ASP A 1 247 ? -3.505 7.188 51.925 1.00 44.50 ? 247 ASP A CB 1 ATOM 1953 C CG . ASP A 1 247 ? -4.262 6.054 51.261 1.00 48.28 ? 247 ASP A CG 1 ATOM 1954 O OD1 . ASP A 1 247 ? -4.863 6.285 50.190 1.00 51.02 ? 247 ASP A OD1 1 ATOM 1955 O OD2 . ASP A 1 247 ? -4.272 4.934 51.818 1.00 51.60 ? 247 ASP A OD2 1 ATOM 1956 N N . LYS A 1 248 ? -2.546 9.897 52.464 1.00 49.74 ? 248 LYS A N 1 ATOM 1957 C CA . LYS A 1 248 ? -2.719 11.277 52.906 1.00 54.58 ? 248 LYS A CA 1 ATOM 1958 C C . LYS A 1 248 ? -1.371 11.990 52.978 1.00 56.99 ? 248 LYS A C 1 ATOM 1959 O O . LYS A 1 248 ? -0.332 11.355 53.176 1.00 56.49 ? 248 LYS A O 1 ATOM 1960 C CB . LYS A 1 248 ? -3.408 11.302 54.276 1.00 55.70 ? 248 LYS A CB 1 ATOM 1961 C CG . LYS A 1 248 ? -4.749 10.581 54.297 1.00 57.30 ? 248 LYS A CG 1 ATOM 1962 C CD . LYS A 1 248 ? -5.318 10.497 55.702 1.00 60.09 ? 248 LYS A CD 1 ATOM 1963 C CE . LYS A 1 248 ? -6.661 9.774 55.703 1.00 62.38 ? 248 LYS A CE 1 ATOM 1964 N NZ . LYS A 1 248 ? -7.254 9.654 57.072 1.00 63.31 ? 248 LYS A NZ 1 ATOM 1965 N N . ASP A 1 249 ? -1.392 13.309 52.811 1.00 60.32 ? 249 ASP A N 1 ATOM 1966 C CA . ASP A 1 249 ? -0.165 14.095 52.844 1.00 63.83 ? 249 ASP A CA 1 ATOM 1967 C C . ASP A 1 249 ? 0.627 13.825 54.114 1.00 64.94 ? 249 ASP A C 1 ATOM 1968 O O . ASP A 1 249 ? 0.153 14.076 55.224 1.00 64.71 ? 249 ASP A O 1 ATOM 1969 C CB . ASP A 1 249 ? -0.481 15.590 52.717 1.00 66.19 ? 249 ASP A CB 1 ATOM 1970 C CG . ASP A 1 249 ? -1.493 16.064 53.737 1.00 68.97 ? 249 ASP A CG 1 ATOM 1971 O OD1 . ASP A 1 249 ? -2.569 15.433 53.849 1.00 70.42 ? 249 ASP A OD1 1 ATOM 1972 O OD2 . ASP A 1 249 ? -1.213 17.075 54.419 1.00 70.48 ? 249 ASP A OD2 1 ATOM 1973 N N . PRO A 1 250 ? 1.849 13.290 53.959 1.00 66.15 ? 250 PRO A N 1 ATOM 1974 C CA . PRO A 1 250 ? 2.741 12.965 55.074 1.00 67.70 ? 250 PRO A CA 1 ATOM 1975 C C . PRO A 1 250 ? 3.379 14.192 55.722 1.00 69.39 ? 250 PRO A C 1 ATOM 1976 O O . PRO A 1 250 ? 3.657 15.190 55.053 1.00 69.89 ? 250 PRO A O 1 ATOM 1977 C CB . PRO A 1 250 ? 3.775 12.053 54.422 1.00 67.21 ? 250 PRO A CB 1 ATOM 1978 C CG . PRO A 1 250 ? 3.897 12.642 53.055 1.00 66.30 ? 250 PRO A CG 1 ATOM 1979 C CD . PRO A 1 250 ? 2.452 12.886 52.676 1.00 65.89 ? 250 PRO A CD 1 ATOM 1980 N N . LYS A 1 251 ? 3.599 14.099 57.031 1.00 70.87 ? 251 LYS A N 1 ATOM 1981 C CA . LYS A 1 251 ? 4.214 15.168 57.814 1.00 71.83 ? 251 LYS A CA 1 ATOM 1982 C C . LYS A 1 251 ? 3.994 14.900 59.300 1.00 72.44 ? 251 LYS A C 1 ATOM 1983 O O . LYS A 1 251 ? 3.157 14.019 59.600 1.00 72.64 ? 251 LYS A O 1 ATOM 1984 C CB . LYS A 1 251 ? 3.619 16.532 57.451 1.00 71.62 ? 251 LYS A CB 1 ATOM 1985 C CG . LYS A 1 251 ? 4.377 17.695 58.062 1.00 71.78 ? 251 LYS A CG 1 ATOM 1986 C CD . LYS A 1 251 ? 3.703 19.025 57.778 1.00 72.18 ? 251 LYS A CD 1 ATOM 1987 C CE . LYS A 1 251 ? 4.460 20.165 58.445 1.00 71.96 ? 251 LYS A CE 1 ATOM 1988 N NZ . LYS A 1 251 ? 3.770 21.472 58.279 1.00 72.14 ? 251 LYS A NZ 1 ATOM 1989 N N . GLY B 1 1 ? 35.756 -10.529 15.630 1.00 47.43 ? 1 GLY B N 1 ATOM 1990 C CA . GLY B 1 1 ? 34.464 -9.943 15.137 1.00 45.91 ? 1 GLY B CA 1 ATOM 1991 C C . GLY B 1 1 ? 33.954 -8.805 16.008 1.00 44.07 ? 1 GLY B C 1 ATOM 1992 O O . GLY B 1 1 ? 34.587 -8.443 17.006 1.00 45.23 ? 1 GLY B O 1 ATOM 1993 N N . LEU B 1 2 ? 32.812 -8.237 15.630 1.00 40.18 ? 2 LEU B N 1 ATOM 1994 C CA . LEU B 1 2 ? 32.221 -7.138 16.385 1.00 35.89 ? 2 LEU B CA 1 ATOM 1995 C C . LEU B 1 2 ? 31.162 -7.662 17.347 1.00 34.25 ? 2 LEU B C 1 ATOM 1996 O O . LEU B 1 2 ? 30.492 -8.651 17.055 1.00 33.26 ? 2 LEU B O 1 ATOM 1997 C CB . LEU B 1 2 ? 31.559 -6.134 15.438 1.00 33.90 ? 2 LEU B CB 1 ATOM 1998 C CG . LEU B 1 2 ? 32.388 -5.368 14.411 1.00 32.78 ? 2 LEU B CG 1 ATOM 1999 C CD1 . LEU B 1 2 ? 31.463 -4.455 13.631 1.00 31.45 ? 2 LEU B CD1 1 ATOM 2000 C CD2 . LEU B 1 2 ? 33.476 -4.561 15.098 1.00 31.30 ? 2 LEU B CD2 1 ATOM 2001 N N . ASP B 1 3 ? 31.009 -7.005 18.493 1.00 32.72 ? 3 ASP B N 1 ATOM 2002 C CA . ASP B 1 3 ? 29.981 -7.412 19.448 1.00 32.43 ? 3 ASP B CA 1 ATOM 2003 C C . ASP B 1 3 ? 28.654 -6.814 18.996 1.00 30.22 ? 3 ASP B C 1 ATOM 2004 O O . ASP B 1 3 ? 28.616 -5.754 18.368 1.00 30.18 ? 3 ASP B O 1 ATOM 2005 C CB . ASP B 1 3 ? 30.311 -6.929 20.867 1.00 34.73 ? 3 ASP B CB 1 ATOM 2006 C CG . ASP B 1 3 ? 31.435 -7.729 21.509 1.00 38.05 ? 3 ASP B CG 1 ATOM 2007 O OD1 . ASP B 1 3 ? 31.284 -8.964 21.639 1.00 39.09 ? 3 ASP B OD1 1 ATOM 2008 O OD2 . ASP B 1 3 ? 32.468 -7.127 21.880 1.00 39.10 ? 3 ASP B OD2 1 ATOM 2009 N N . THR B 1 4 ? 27.567 -7.504 19.298 1.00 27.93 ? 4 THR B N 1 ATOM 2010 C CA . THR B 1 4 ? 26.257 -7.027 18.915 1.00 27.57 ? 4 THR B CA 1 ATOM 2011 C C . THR B 1 4 ? 25.335 -7.005 20.120 1.00 26.61 ? 4 THR B C 1 ATOM 2012 O O . THR B 1 4 ? 25.293 -7.954 20.900 1.00 27.88 ? 4 THR B O 1 ATOM 2013 C CB . THR B 1 4 ? 25.634 -7.927 17.838 1.00 29.21 ? 4 THR B CB 1 ATOM 2014 O OG1 . THR B 1 4 ? 26.518 -8.000 16.714 1.00 31.98 ? 4 THR B OG1 1 ATOM 2015 C CG2 . THR B 1 4 ? 24.286 -7.368 17.380 1.00 29.96 ? 4 THR B CG2 1 ATOM 2016 N N . VAL B 1 5 ? 24.611 -5.906 20.280 1.00 24.48 ? 5 VAL B N 1 ATOM 2017 C CA . VAL B 1 5 ? 23.666 -5.775 21.376 1.00 23.08 ? 5 VAL B CA 1 ATOM 2018 C C . VAL B 1 5 ? 22.306 -5.613 20.712 1.00 22.67 ? 5 VAL B C 1 ATOM 2019 O O . VAL B 1 5 ? 22.132 -4.772 19.828 1.00 23.11 ? 5 VAL B O 1 ATOM 2020 C CB . VAL B 1 5 ? 23.987 -4.539 22.269 1.00 22.25 ? 5 VAL B CB 1 ATOM 2021 C CG1 . VAL B 1 5 ? 22.980 -4.431 23.409 1.00 21.58 ? 5 VAL B CG1 1 ATOM 2022 C CG2 . VAL B 1 5 ? 25.389 -4.669 22.843 1.00 23.34 ? 5 VAL B CG2 1 ATOM 2023 N N . SER B 1 6 ? 21.350 -6.435 21.123 1.00 21.21 ? 6 SER B N 1 ATOM 2024 C CA . SER B 1 6 ? 20.021 -6.381 20.541 1.00 22.05 ? 6 SER B CA 1 ATOM 2025 C C . SER B 1 6 ? 18.998 -5.772 21.473 1.00 21.31 ? 6 SER B C 1 ATOM 2026 O O . SER B 1 6 ? 19.129 -5.841 22.692 1.00 21.14 ? 6 SER B O 1 ATOM 2027 C CB . SER B 1 6 ? 19.557 -7.787 20.163 1.00 23.75 ? 6 SER B CB 1 ATOM 2028 O OG . SER B 1 6 ? 20.503 -8.419 19.323 1.00 28.07 ? 6 SER B OG 1 ATOM 2029 N N . PHE B 1 7 ? 17.979 -5.167 20.877 1.00 20.67 ? 7 PHE B N 1 ATOM 2030 C CA . PHE B 1 7 ? 16.881 -4.575 21.624 1.00 20.38 ? 7 PHE B CA 1 ATOM 2031 C C . PHE B 1 7 ? 15.644 -4.655 20.744 1.00 20.88 ? 7 PHE B C 1 ATOM 2032 O O . PHE B 1 7 ? 15.673 -4.232 19.584 1.00 21.57 ? 7 PHE B O 1 ATOM 2033 C CB . PHE B 1 7 ? 17.151 -3.106 21.977 1.00 19.16 ? 7 PHE B CB 1 ATOM 2034 C CG . PHE B 1 7 ? 16.015 -2.455 22.733 1.00 19.40 ? 7 PHE B CG 1 ATOM 2035 C CD1 . PHE B 1 7 ? 15.727 -2.830 24.046 1.00 18.76 ? 7 PHE B CD1 1 ATOM 2036 C CD2 . PHE B 1 7 ? 15.196 -1.509 22.117 1.00 19.21 ? 7 PHE B CD2 1 ATOM 2037 C CE1 . PHE B 1 7 ? 14.634 -2.272 24.732 1.00 18.07 ? 7 PHE B CE1 1 ATOM 2038 C CE2 . PHE B 1 7 ? 14.097 -0.947 22.799 1.00 19.07 ? 7 PHE B CE2 1 ATOM 2039 C CZ . PHE B 1 7 ? 13.821 -1.333 24.105 1.00 16.46 ? 7 PHE B CZ 1 ATOM 2040 N N . SER B 1 8 ? 14.569 -5.214 21.287 1.00 20.58 ? 8 SER B N 1 ATOM 2041 C CA . SER B 1 8 ? 13.318 -5.322 20.550 1.00 22.21 ? 8 SER B CA 1 ATOM 2042 C C . SER B 1 8 ? 12.282 -4.411 21.186 1.00 21.84 ? 8 SER B C 1 ATOM 2043 O O . SER B 1 8 ? 12.207 -4.304 22.412 1.00 21.30 ? 8 SER B O 1 ATOM 2044 C CB . SER B 1 8 ? 12.795 -6.759 20.558 1.00 23.51 ? 8 SER B CB 1 ATOM 2045 O OG . SER B 1 8 ? 11.503 -6.809 19.971 1.00 25.99 ? 8 SER B OG 1 ATOM 2046 N N . THR B 1 9 ? 11.489 -3.754 20.348 1.00 22.27 ? 9 THR B N 1 ATOM 2047 C CA . THR B 1 9 ? 10.456 -2.848 20.832 1.00 23.18 ? 9 THR B CA 1 ATOM 2048 C C . THR B 1 9 ? 9.187 -3.626 21.162 1.00 24.42 ? 9 THR B C 1 ATOM 2049 O O . THR B 1 9 ? 8.295 -3.117 21.839 1.00 24.16 ? 9 THR B O 1 ATOM 2050 C CB . THR B 1 9 ? 10.119 -1.763 19.785 1.00 23.38 ? 9 THR B CB 1 ATOM 2051 O OG1 . THR B 1 9 ? 9.557 -2.379 18.623 1.00 22.17 ? 9 THR B OG1 1 ATOM 2052 C CG2 . THR B 1 9 ? 11.375 -0.992 19.381 1.00 22.66 ? 9 THR B CG2 1 ATOM 2053 N N . LYS B 1 10 ? 9.114 -4.865 20.686 1.00 25.47 ? 10 LYS B N 1 ATOM 2054 C CA . LYS B 1 10 ? 7.953 -5.709 20.939 1.00 26.03 ? 10 LYS B CA 1 ATOM 2055 C C . LYS B 1 10 ? 7.917 -6.115 22.412 1.00 24.84 ? 10 LYS B C 1 ATOM 2056 O O . LYS B 1 10 ? 8.768 -6.877 22.875 1.00 25.36 ? 10 LYS B O 1 ATOM 2057 C CB . LYS B 1 10 ? 8.021 -6.955 20.057 1.00 28.48 ? 10 LYS B CB 1 ATOM 2058 C CG . LYS B 1 10 ? 6.695 -7.683 19.898 1.00 33.76 ? 10 LYS B CG 1 ATOM 2059 C CD . LYS B 1 10 ? 6.799 -8.709 18.775 1.00 39.49 ? 10 LYS B CD 1 ATOM 2060 C CE . LYS B 1 10 ? 5.447 -8.983 18.116 1.00 42.71 ? 10 LYS B CE 1 ATOM 2061 N NZ . LYS B 1 10 ? 5.596 -9.767 16.845 1.00 44.29 ? 10 LYS B NZ 1 ATOM 2062 N N . GLY B 1 11 ? 6.936 -5.599 23.146 1.00 24.39 ? 11 GLY B N 1 ATOM 2063 C CA . GLY B 1 11 ? 6.818 -5.922 24.559 1.00 23.51 ? 11 GLY B CA 1 ATOM 2064 C C . GLY B 1 11 ? 7.867 -5.244 25.420 1.00 23.26 ? 11 GLY B C 1 ATOM 2065 O O . GLY B 1 11 ? 8.065 -5.602 26.582 1.00 23.26 ? 11 GLY B O 1 ATOM 2066 N N . ALA B 1 12 ? 8.543 -4.252 24.852 1.00 22.46 ? 12 ALA B N 1 ATOM 2067 C CA . ALA B 1 12 ? 9.580 -3.533 25.578 1.00 21.61 ? 12 ALA B CA 1 ATOM 2068 C C . ALA B 1 12 ? 9.019 -2.779 26.777 1.00 20.68 ? 12 ALA B C 1 ATOM 2069 O O . ALA B 1 12 ? 7.881 -2.306 26.758 1.00 20.25 ? 12 ALA B O 1 ATOM 2070 C CB . ALA B 1 12 ? 10.292 -2.559 24.639 1.00 21.33 ? 12 ALA B CB 1 ATOM 2071 N N . THR B 1 13 ? 9.830 -2.675 27.823 1.00 19.97 ? 13 THR B N 1 ATOM 2072 C CA . THR B 1 13 ? 9.445 -1.954 29.036 1.00 18.53 ? 13 THR B CA 1 ATOM 2073 C C . THR B 1 13 ? 10.608 -1.059 29.434 1.00 17.44 ? 13 THR B C 1 ATOM 2074 O O . THR B 1 13 ? 11.702 -1.166 28.871 1.00 16.56 ? 13 THR B O 1 ATOM 2075 C CB . THR B 1 13 ? 9.154 -2.906 30.221 1.00 19.18 ? 13 THR B CB 1 ATOM 2076 O OG1 . THR B 1 13 ? 10.366 -3.565 30.613 1.00 18.16 ? 13 THR B OG1 1 ATOM 2077 C CG2 . THR B 1 13 ? 8.094 -3.944 29.834 1.00 17.16 ? 13 THR B CG2 1 ATOM 2078 N N . TYR B 1 14 ? 10.376 -0.184 30.406 1.00 16.35 ? 14 TYR B N 1 ATOM 2079 C CA . TYR B 1 14 ? 11.418 0.721 30.862 1.00 16.76 ? 14 TYR B CA 1 ATOM 2080 C C . TYR B 1 14 ? 12.602 -0.089 31.379 1.00 16.82 ? 14 TYR B C 1 ATOM 2081 O O . TYR B 1 14 ? 13.752 0.352 31.321 1.00 16.62 ? 14 TYR B O 1 ATOM 2082 C CB . TYR B 1 14 ? 10.874 1.637 31.957 1.00 16.37 ? 14 TYR B CB 1 ATOM 2083 C CG . TYR B 1 14 ? 10.424 0.911 33.201 1.00 18.10 ? 14 TYR B CG 1 ATOM 2084 C CD1 . TYR B 1 14 ? 11.174 0.969 34.375 1.00 19.05 ? 14 TYR B CD1 1 ATOM 2085 C CD2 . TYR B 1 14 ? 9.235 0.182 33.213 1.00 19.11 ? 14 TYR B CD2 1 ATOM 2086 C CE1 . TYR B 1 14 ? 10.745 0.324 35.536 1.00 19.13 ? 14 TYR B CE1 1 ATOM 2087 C CE2 . TYR B 1 14 ? 8.798 -0.467 34.364 1.00 18.81 ? 14 TYR B CE2 1 ATOM 2088 C CZ . TYR B 1 14 ? 9.556 -0.391 35.523 1.00 20.04 ? 14 TYR B CZ 1 ATOM 2089 O OH . TYR B 1 14 ? 9.120 -1.023 36.668 1.00 19.49 ? 14 TYR B OH 1 ATOM 2090 N N . ILE B 1 15 ? 12.313 -1.284 31.878 1.00 16.11 ? 15 ILE B N 1 ATOM 2091 C CA . ILE B 1 15 ? 13.353 -2.157 32.384 1.00 15.38 ? 15 ILE B CA 1 ATOM 2092 C C . ILE B 1 15 ? 14.158 -2.815 31.264 1.00 15.09 ? 15 ILE B C 1 ATOM 2093 O O . ILE B 1 15 ? 15.386 -2.875 31.348 1.00 15.95 ? 15 ILE B O 1 ATOM 2094 C CB . ILE B 1 15 ? 12.758 -3.236 33.319 1.00 15.99 ? 15 ILE B CB 1 ATOM 2095 C CG1 . ILE B 1 15 ? 12.482 -2.621 34.692 1.00 16.78 ? 15 ILE B CG1 1 ATOM 2096 C CG2 . ILE B 1 15 ? 13.707 -4.411 33.443 1.00 17.63 ? 15 ILE B CG2 1 ATOM 2097 C CD1 . ILE B 1 15 ? 13.733 -2.070 35.380 1.00 17.76 ? 15 ILE B CD1 1 ATOM 2098 N N . THR B 1 16 ? 13.503 -3.309 30.213 1.00 14.81 ? 16 THR B N 1 ATOM 2099 C CA . THR B 1 16 ? 14.283 -3.929 29.136 1.00 15.80 ? 16 THR B CA 1 ATOM 2100 C C . THR B 1 16 ? 15.162 -2.870 28.462 1.00 14.95 ? 16 THR B C 1 ATOM 2101 O O . THR B 1 16 ? 16.272 -3.164 28.031 1.00 16.05 ? 16 THR B O 1 ATOM 2102 C CB . THR B 1 16 ? 13.395 -4.634 28.067 1.00 16.88 ? 16 THR B CB 1 ATOM 2103 O OG1 . THR B 1 16 ? 12.658 -3.666 27.308 1.00 17.66 ? 16 THR B OG1 1 ATOM 2104 C CG2 . THR B 1 16 ? 12.429 -5.599 28.742 1.00 17.74 ? 16 THR B CG2 1 ATOM 2105 N N . TYR B 1 17 ? 14.668 -1.634 28.404 1.00 14.16 ? 17 TYR B N 1 ATOM 2106 C CA . TYR B 1 17 ? 15.412 -0.523 27.808 1.00 13.57 ? 17 TYR B CA 1 ATOM 2107 C C . TYR B 1 17 ? 16.667 -0.224 28.636 1.00 13.57 ? 17 TYR B C 1 ATOM 2108 O O . TYR B 1 17 ? 17.765 -0.118 28.097 1.00 13.88 ? 17 TYR B O 1 ATOM 2109 C CB . TYR B 1 17 ? 14.526 0.725 27.752 1.00 14.14 ? 17 TYR B CB 1 ATOM 2110 C CG . TYR B 1 17 ? 15.248 1.982 27.311 1.00 14.50 ? 17 TYR B CG 1 ATOM 2111 C CD1 . TYR B 1 17 ? 15.701 2.127 25.999 1.00 13.78 ? 17 TYR B CD1 1 ATOM 2112 C CD2 . TYR B 1 17 ? 15.480 3.026 28.209 1.00 13.96 ? 17 TYR B CD2 1 ATOM 2113 C CE1 . TYR B 1 17 ? 16.369 3.286 25.587 1.00 12.37 ? 17 TYR B CE1 1 ATOM 2114 C CE2 . TYR B 1 17 ? 16.147 4.186 27.807 1.00 13.62 ? 17 TYR B CE2 1 ATOM 2115 C CZ . TYR B 1 17 ? 16.586 4.305 26.494 1.00 12.73 ? 17 TYR B CZ 1 ATOM 2116 O OH . TYR B 1 17 ? 17.237 5.442 26.089 1.00 14.29 ? 17 TYR B OH 1 ATOM 2117 N N . VAL B 1 18 ? 16.493 -0.083 29.947 1.00 13.06 ? 18 VAL B N 1 ATOM 2118 C CA . VAL B 1 18 ? 17.609 0.199 30.842 1.00 14.04 ? 18 VAL B CA 1 ATOM 2119 C C . VAL B 1 18 ? 18.611 -0.954 30.857 1.00 14.56 ? 18 VAL B C 1 ATOM 2120 O O . VAL B 1 18 ? 19.818 -0.726 30.849 1.00 14.25 ? 18 VAL B O 1 ATOM 2121 C CB . VAL B 1 18 ? 17.102 0.498 32.275 1.00 15.17 ? 18 VAL B CB 1 ATOM 2122 C CG1 . VAL B 1 18 ? 18.256 0.459 33.273 1.00 17.87 ? 18 VAL B CG1 1 ATOM 2123 C CG2 . VAL B 1 18 ? 16.438 1.881 32.297 1.00 14.75 ? 18 VAL B CG2 1 ATOM 2124 N N . ASN B 1 19 ? 18.120 -2.190 30.870 1.00 15.23 ? 19 ASN B N 1 ATOM 2125 C CA . ASN B 1 19 ? 19.020 -3.341 30.852 1.00 16.09 ? 19 ASN B CA 1 ATOM 2126 C C . ASN B 1 19 ? 19.814 -3.330 29.542 1.00 15.86 ? 19 ASN B C 1 ATOM 2127 O O . ASN B 1 19 ? 20.997 -3.661 29.518 1.00 17.27 ? 19 ASN B O 1 ATOM 2128 C CB . ASN B 1 19 ? 18.224 -4.638 31.000 1.00 17.04 ? 19 ASN B CB 1 ATOM 2129 C CG . ASN B 1 19 ? 17.707 -4.847 32.417 1.00 19.67 ? 19 ASN B CG 1 ATOM 2130 O OD1 . ASN B 1 19 ? 16.733 -5.573 32.632 1.00 24.18 ? 19 ASN B OD1 1 ATOM 2131 N ND2 . ASN B 1 19 ? 18.362 -4.223 33.391 1.00 18.53 ? 19 ASN B ND2 1 ATOM 2132 N N . PHE B 1 20 ? 19.161 -2.928 28.455 1.00 16.43 ? 20 PHE B N 1 ATOM 2133 C CA . PHE B 1 20 ? 19.812 -2.830 27.147 1.00 15.64 ? 20 PHE B CA 1 ATOM 2134 C C . PHE B 1 20 ? 20.958 -1.810 27.202 1.00 15.36 ? 20 PHE B C 1 ATOM 2135 O O . PHE B 1 20 ? 22.076 -2.103 26.776 1.00 14.96 ? 20 PHE B O 1 ATOM 2136 C CB . PHE B 1 20 ? 18.785 -2.402 26.094 1.00 17.43 ? 20 PHE B CB 1 ATOM 2137 C CG . PHE B 1 20 ? 19.381 -1.698 24.901 1.00 19.31 ? 20 PHE B CG 1 ATOM 2138 C CD1 . PHE B 1 20 ? 20.227 -2.370 24.020 1.00 20.04 ? 20 PHE B CD1 1 ATOM 2139 C CD2 . PHE B 1 20 ? 19.102 -0.355 24.666 1.00 19.96 ? 20 PHE B CD2 1 ATOM 2140 C CE1 . PHE B 1 20 ? 20.786 -1.709 22.921 1.00 19.57 ? 20 PHE B CE1 1 ATOM 2141 C CE2 . PHE B 1 20 ? 19.656 0.312 23.571 1.00 19.97 ? 20 PHE B CE2 1 ATOM 2142 C CZ . PHE B 1 20 ? 20.500 -0.369 22.698 1.00 18.85 ? 20 PHE B CZ 1 ATOM 2143 N N . LEU B 1 21 ? 20.679 -0.613 27.725 1.00 14.66 ? 21 LEU B N 1 ATOM 2144 C CA . LEU B 1 21 ? 21.705 0.424 27.832 1.00 14.24 ? 21 LEU B CA 1 ATOM 2145 C C . LEU B 1 21 ? 22.913 -0.049 28.632 1.00 14.03 ? 21 LEU B C 1 ATOM 2146 O O . LEU B 1 21 ? 24.051 0.220 28.260 1.00 14.17 ? 21 LEU B O 1 ATOM 2147 C CB . LEU B 1 21 ? 21.144 1.690 28.490 1.00 14.55 ? 21 LEU B CB 1 ATOM 2148 C CG . LEU B 1 21 ? 20.115 2.510 27.708 1.00 15.76 ? 21 LEU B CG 1 ATOM 2149 C CD1 . LEU B 1 21 ? 19.714 3.737 28.537 1.00 15.34 ? 21 LEU B CD1 1 ATOM 2150 C CD2 . LEU B 1 21 ? 20.702 2.936 26.358 1.00 15.05 ? 21 LEU B CD2 1 ATOM 2151 N N . ASN B 1 22 ? 22.680 -0.752 29.735 1.00 13.98 ? 22 ASN B N 1 ATOM 2152 C CA . ASN B 1 22 ? 23.807 -1.209 30.528 1.00 15.44 ? 22 ASN B CA 1 ATOM 2153 C C . ASN B 1 22 ? 24.568 -2.330 29.847 1.00 16.06 ? 22 ASN B C 1 ATOM 2154 O O . ASN B 1 22 ? 25.752 -2.536 30.103 1.00 16.70 ? 22 ASN B O 1 ATOM 2155 C CB . ASN B 1 22 ? 23.349 -1.617 31.923 1.00 16.06 ? 22 ASN B CB 1 ATOM 2156 C CG . ASN B 1 22 ? 23.089 -0.417 32.802 1.00 15.33 ? 22 ASN B CG 1 ATOM 2157 O OD1 . ASN B 1 22 ? 23.927 0.489 32.884 1.00 15.56 ? 22 ASN B OD1 1 ATOM 2158 N ND2 . ASN B 1 22 ? 21.932 -0.394 33.465 1.00 15.83 ? 22 ASN B ND2 1 ATOM 2159 N N . GLU B 1 23 ? 23.888 -3.039 28.961 1.00 16.83 ? 23 GLU B N 1 ATOM 2160 C CA . GLU B 1 23 ? 24.523 -4.111 28.212 1.00 19.66 ? 23 GLU B CA 1 ATOM 2161 C C . GLU B 1 23 ? 25.460 -3.438 27.197 1.00 17.66 ? 23 GLU B C 1 ATOM 2162 O O . GLU B 1 23 ? 26.592 -3.870 26.987 1.00 16.90 ? 23 GLU B O 1 ATOM 2163 C CB . GLU B 1 23 ? 23.450 -4.922 27.499 1.00 23.43 ? 23 GLU B CB 1 ATOM 2164 C CG . GLU B 1 23 ? 23.918 -6.223 26.906 1.00 32.21 ? 23 GLU B CG 1 ATOM 2165 C CD . GLU B 1 23 ? 22.792 -6.940 26.180 1.00 36.92 ? 23 GLU B CD 1 ATOM 2166 O OE1 . GLU B 1 23 ? 21.719 -7.143 26.798 1.00 37.23 ? 23 GLU B OE1 1 ATOM 2167 O OE2 . GLU B 1 23 ? 22.981 -7.295 24.994 1.00 40.46 ? 23 GLU B OE2 1 ATOM 2168 N N . LEU B 1 24 ? 24.980 -2.357 26.589 1.00 15.82 ? 24 LEU B N 1 ATOM 2169 C CA . LEU B 1 24 ? 25.764 -1.614 25.608 1.00 14.86 ? 24 LEU B CA 1 ATOM 2170 C C . LEU B 1 24 ? 26.968 -0.951 26.264 1.00 15.35 ? 24 LEU B C 1 ATOM 2171 O O . LEU B 1 24 ? 28.064 -0.958 25.709 1.00 16.09 ? 24 LEU B O 1 ATOM 2172 C CB . LEU B 1 24 ? 24.894 -0.543 24.926 1.00 14.82 ? 24 LEU B CB 1 ATOM 2173 C CG . LEU B 1 24 ? 25.610 0.465 24.012 1.00 14.55 ? 24 LEU B CG 1 ATOM 2174 C CD1 . LEU B 1 24 ? 26.358 -0.274 22.894 1.00 15.28 ? 24 LEU B CD1 1 ATOM 2175 C CD2 . LEU B 1 24 ? 24.599 1.447 23.431 1.00 14.77 ? 24 LEU B CD2 1 ATOM 2176 N N . ARG B 1 25 ? 26.758 -0.372 27.443 1.00 15.09 ? 25 ARG B N 1 ATOM 2177 C CA . ARG B 1 25 ? 27.824 0.301 28.172 1.00 15.73 ? 25 ARG B CA 1 ATOM 2178 C C . ARG B 1 25 ? 28.972 -0.651 28.473 1.00 16.85 ? 25 ARG B C 1 ATOM 2179 O O . ARG B 1 25 ? 30.134 -0.252 28.484 1.00 17.87 ? 25 ARG B O 1 ATOM 2180 C CB . ARG B 1 25 ? 27.274 0.894 29.476 1.00 15.79 ? 25 ARG B CB 1 ATOM 2181 C CG . ARG B 1 25 ? 26.419 2.136 29.261 1.00 16.10 ? 25 ARG B CG 1 ATOM 2182 C CD . ARG B 1 25 ? 25.566 2.469 30.476 1.00 15.52 ? 25 ARG B CD 1 ATOM 2183 N NE . ARG B 1 25 ? 24.797 3.695 30.259 1.00 15.76 ? 25 ARG B NE 1 ATOM 2184 C CZ . ARG B 1 25 ? 23.796 4.098 31.037 1.00 15.36 ? 25 ARG B CZ 1 ATOM 2185 N NH1 . ARG B 1 25 ? 23.436 3.369 32.085 1.00 14.03 ? 25 ARG B NH1 1 ATOM 2186 N NH2 . ARG B 1 25 ? 23.163 5.232 30.776 1.00 13.17 ? 25 ARG B NH2 1 ATOM 2187 N N . VAL B 1 26 ? 28.641 -1.912 28.720 1.00 18.07 ? 26 VAL B N 1 ATOM 2188 C CA . VAL B 1 26 ? 29.660 -2.912 29.006 1.00 18.85 ? 26 VAL B CA 1 ATOM 2189 C C . VAL B 1 26 ? 30.419 -3.261 27.732 1.00 19.78 ? 26 VAL B C 1 ATOM 2190 O O . VAL B 1 26 ? 31.656 -3.287 27.722 1.00 18.66 ? 26 VAL B O 1 ATOM 2191 C CB . VAL B 1 26 ? 29.045 -4.214 29.580 1.00 19.28 ? 26 VAL B CB 1 ATOM 2192 C CG1 . VAL B 1 26 ? 30.093 -5.325 29.589 1.00 18.70 ? 26 VAL B CG1 1 ATOM 2193 C CG2 . VAL B 1 26 ? 28.535 -3.972 30.993 1.00 18.21 ? 26 VAL B CG2 1 ATOM 2194 N N . LYS B 1 27 ? 29.680 -3.515 26.653 1.00 19.95 ? 27 LYS B N 1 ATOM 2195 C CA . LYS B 1 27 ? 30.315 -3.883 25.393 1.00 20.42 ? 27 LYS B CA 1 ATOM 2196 C C . LYS B 1 27 ? 31.106 -2.774 24.715 1.00 20.30 ? 27 LYS B C 1 ATOM 2197 O O . LYS B 1 27 ? 31.866 -3.032 23.784 1.00 20.54 ? 27 LYS B O 1 ATOM 2198 C CB . LYS B 1 27 ? 29.285 -4.486 24.443 1.00 21.39 ? 27 LYS B CB 1 ATOM 2199 C CG . LYS B 1 27 ? 28.798 -5.833 24.950 1.00 24.92 ? 27 LYS B CG 1 ATOM 2200 C CD . LYS B 1 27 ? 28.003 -6.581 23.906 1.00 31.37 ? 27 LYS B CD 1 ATOM 2201 C CE . LYS B 1 27 ? 27.584 -7.958 24.409 1.00 31.77 ? 27 LYS B CE 1 ATOM 2202 N NZ . LYS B 1 27 ? 26.811 -8.697 23.366 1.00 33.39 ? 27 LYS B NZ 1 ATOM 2203 N N . LEU B 1 28 ? 30.942 -1.539 25.178 1.00 18.81 ? 28 LEU B N 1 ATOM 2204 C CA . LEU B 1 28 ? 31.717 -0.440 24.618 1.00 19.57 ? 28 LEU B CA 1 ATOM 2205 C C . LEU B 1 28 ? 33.138 -0.614 25.165 1.00 20.85 ? 28 LEU B C 1 ATOM 2206 O O . LEU B 1 28 ? 34.100 -0.006 24.681 1.00 21.95 ? 28 LEU B O 1 ATOM 2207 C CB . LEU B 1 28 ? 31.130 0.903 25.056 1.00 17.42 ? 28 LEU B CB 1 ATOM 2208 C CG . LEU B 1 28 ? 29.833 1.290 24.343 1.00 17.16 ? 28 LEU B CG 1 ATOM 2209 C CD1 . LEU B 1 28 ? 29.176 2.445 25.077 1.00 17.44 ? 28 LEU B CD1 1 ATOM 2210 C CD2 . LEU B 1 28 ? 30.133 1.665 22.894 1.00 15.43 ? 28 LEU B CD2 1 ATOM 2211 N N . LYS B 1 29 ? 33.246 -1.460 26.188 1.00 20.61 ? 29 LYS B N 1 ATOM 2212 C CA . LYS B 1 29 ? 34.513 -1.770 26.834 1.00 20.87 ? 29 LYS B CA 1 ATOM 2213 C C . LYS B 1 29 ? 35.399 -0.579 27.160 1.00 21.52 ? 29 LYS B C 1 ATOM 2214 O O . LYS B 1 29 ? 36.500 -0.445 26.620 1.00 21.88 ? 29 LYS B O 1 ATOM 2215 C CB . LYS B 1 29 ? 35.305 -2.768 25.988 1.00 21.27 ? 29 LYS B CB 1 ATOM 2216 C CG . LYS B 1 29 ? 34.692 -4.150 25.973 1.00 24.43 ? 29 LYS B CG 1 ATOM 2217 C CD . LYS B 1 29 ? 35.447 -5.086 25.061 1.00 28.30 ? 29 LYS B CD 1 ATOM 2218 C CE . LYS B 1 29 ? 34.758 -6.434 24.990 1.00 30.75 ? 29 LYS B CE 1 ATOM 2219 N NZ . LYS B 1 29 ? 35.477 -7.353 24.066 1.00 35.43 ? 29 LYS B NZ 1 ATOM 2220 N N . PRO B 1 30 ? 34.932 0.310 28.050 1.00 21.31 ? 30 PRO B N 1 ATOM 2221 C CA . PRO B 1 30 ? 35.753 1.470 28.410 1.00 22.48 ? 30 PRO B CA 1 ATOM 2222 C C . PRO B 1 30 ? 36.999 0.957 29.142 1.00 23.39 ? 30 PRO B C 1 ATOM 2223 O O . PRO B 1 30 ? 36.992 -0.152 29.681 1.00 23.70 ? 30 PRO B O 1 ATOM 2224 C CB . PRO B 1 30 ? 34.830 2.274 29.327 1.00 21.42 ? 30 PRO B CB 1 ATOM 2225 C CG . PRO B 1 30 ? 33.999 1.222 29.968 1.00 22.04 ? 30 PRO B CG 1 ATOM 2226 C CD . PRO B 1 30 ? 33.671 0.303 28.808 1.00 20.95 ? 30 PRO B CD 1 ATOM 2227 N N . GLU B 1 31 ? 38.069 1.740 29.152 1.00 23.09 ? 31 GLU B N 1 ATOM 2228 C CA . GLU B 1 31 ? 39.275 1.302 29.845 1.00 24.88 ? 31 GLU B CA 1 ATOM 2229 C C . GLU B 1 31 ? 39.650 2.270 30.955 1.00 23.45 ? 31 GLU B C 1 ATOM 2230 O O . GLU B 1 31 ? 40.044 3.409 30.698 1.00 23.43 ? 31 GLU B O 1 ATOM 2231 C CB . GLU B 1 31 ? 40.446 1.167 28.870 1.00 27.93 ? 31 GLU B CB 1 ATOM 2232 C CG . GLU B 1 31 ? 40.187 0.235 27.698 1.00 32.86 ? 31 GLU B CG 1 ATOM 2233 C CD . GLU B 1 31 ? 41.441 -0.016 26.881 1.00 35.67 ? 31 GLU B CD 1 ATOM 2234 O OE1 . GLU B 1 31 ? 42.338 0.856 26.883 1.00 37.70 ? 31 GLU B OE1 1 ATOM 2235 O OE2 . GLU B 1 31 ? 41.526 -1.077 26.225 1.00 38.57 ? 31 GLU B OE2 1 ATOM 2236 N N . GLY B 1 32 ? 39.526 1.809 32.193 1.00 22.10 ? 32 GLY B N 1 ATOM 2237 C CA . GLY B 1 32 ? 39.858 2.661 33.315 1.00 22.49 ? 32 GLY B CA 1 ATOM 2238 C C . GLY B 1 32 ? 38.715 3.598 33.640 1.00 22.18 ? 32 GLY B C 1 ATOM 2239 O O . GLY B 1 32 ? 37.586 3.402 33.183 1.00 22.09 ? 32 GLY B O 1 ATOM 2240 N N . ASN B 1 33 ? 39.008 4.631 34.416 1.00 20.85 ? 33 ASN B N 1 ATOM 2241 C CA . ASN B 1 33 ? 37.982 5.575 34.806 1.00 20.00 ? 33 ASN B CA 1 ATOM 2242 C C . ASN B 1 33 ? 38.632 6.874 35.217 1.00 19.49 ? 33 ASN B C 1 ATOM 2243 O O . ASN B 1 33 ? 39.850 6.974 35.295 1.00 21.53 ? 33 ASN B O 1 ATOM 2244 C CB . ASN B 1 33 ? 37.221 5.019 36.004 1.00 20.77 ? 33 ASN B CB 1 ATOM 2245 C CG . ASN B 1 33 ? 38.072 5.008 37.270 1.00 21.23 ? 33 ASN B CG 1 ATOM 2246 O OD1 . ASN B 1 33 ? 38.124 5.992 38.010 1.00 21.91 ? 33 ASN B OD1 1 ATOM 2247 N ND2 . ASN B 1 33 ? 38.767 3.905 37.505 1.00 22.22 ? 33 ASN B ND2 1 ATOM 2248 N N . SER B 1 34 ? 37.800 7.870 35.475 1.00 18.41 ? 34 SER B N 1 ATOM 2249 C CA . SER B 1 34 ? 38.258 9.158 35.950 1.00 18.28 ? 34 SER B CA 1 ATOM 2250 C C . SER B 1 34 ? 37.250 9.490 37.046 1.00 19.38 ? 34 SER B C 1 ATOM 2251 O O . SER B 1 34 ? 36.053 9.639 36.781 1.00 18.34 ? 34 SER B O 1 ATOM 2252 C CB . SER B 1 34 ? 38.222 10.205 34.838 1.00 19.86 ? 34 SER B CB 1 ATOM 2253 O OG . SER B 1 34 ? 38.671 11.463 35.318 1.00 22.84 ? 34 SER B OG 1 ATOM 2254 N N . HIS B 1 35 ? 37.736 9.568 38.280 1.00 19.24 ? 35 HIS B N 1 ATOM 2255 C CA . HIS B 1 35 ? 36.894 9.849 39.431 1.00 19.50 ? 35 HIS B CA 1 ATOM 2256 C C . HIS B 1 35 ? 35.760 8.844 39.591 1.00 19.55 ? 35 HIS B C 1 ATOM 2257 O O . HIS B 1 35 ? 34.674 9.188 40.070 1.00 21.99 ? 35 HIS B O 1 ATOM 2258 C CB . HIS B 1 35 ? 36.322 11.259 39.350 1.00 21.01 ? 35 HIS B CB 1 ATOM 2259 C CG . HIS B 1 35 ? 37.335 12.329 39.594 1.00 23.51 ? 35 HIS B CG 1 ATOM 2260 N ND1 . HIS B 1 35 ? 38.160 12.813 38.602 1.00 25.97 ? 35 HIS B ND1 1 ATOM 2261 C CD2 . HIS B 1 35 ? 37.684 12.980 40.728 1.00 23.79 ? 35 HIS B CD2 1 ATOM 2262 C CE1 . HIS B 1 35 ? 38.975 13.717 39.115 1.00 26.23 ? 35 HIS B CE1 1 ATOM 2263 N NE2 . HIS B 1 35 ? 38.707 13.837 40.403 1.00 26.25 ? 35 HIS B NE2 1 ATOM 2264 N N . GLY B 1 36 ? 36.014 7.604 39.185 1.00 18.06 ? 36 GLY B N 1 ATOM 2265 C CA . GLY B 1 36 ? 35.009 6.565 39.320 1.00 16.77 ? 36 GLY B CA 1 ATOM 2266 C C . GLY B 1 36 ? 34.107 6.389 38.119 1.00 16.37 ? 36 GLY B C 1 ATOM 2267 O O . GLY B 1 36 ? 33.391 5.398 38.031 1.00 16.95 ? 36 GLY B O 1 ATOM 2268 N N . ILE B 1 37 ? 34.133 7.341 37.194 1.00 15.69 ? 37 ILE B N 1 ATOM 2269 C CA . ILE B 1 37 ? 33.296 7.257 36.001 1.00 16.00 ? 37 ILE B CA 1 ATOM 2270 C C . ILE B 1 37 ? 34.063 6.523 34.903 1.00 16.80 ? 37 ILE B C 1 ATOM 2271 O O . ILE B 1 37 ? 35.191 6.904 34.564 1.00 17.75 ? 37 ILE B O 1 ATOM 2272 C CB . ILE B 1 37 ? 32.913 8.664 35.499 1.00 16.34 ? 37 ILE B CB 1 ATOM 2273 C CG1 . ILE B 1 37 ? 32.336 9.482 36.656 1.00 16.80 ? 37 ILE B CG1 1 ATOM 2274 C CG2 . ILE B 1 37 ? 31.898 8.558 34.368 1.00 14.00 ? 37 ILE B CG2 1 ATOM 2275 C CD1 . ILE B 1 37 ? 32.110 10.946 36.325 1.00 18.28 ? 37 ILE B CD1 1 ATOM 2276 N N . PRO B 1 38 ? 33.474 5.452 34.341 1.00 17.30 ? 38 PRO B N 1 ATOM 2277 C CA . PRO B 1 38 ? 34.167 4.711 33.283 1.00 18.33 ? 38 PRO B CA 1 ATOM 2278 C C . PRO B 1 38 ? 34.599 5.598 32.108 1.00 19.90 ? 38 PRO B C 1 ATOM 2279 O O . PRO B 1 38 ? 33.829 6.432 31.618 1.00 19.15 ? 38 PRO B O 1 ATOM 2280 C CB . PRO B 1 38 ? 33.167 3.611 32.900 1.00 19.15 ? 38 PRO B CB 1 ATOM 2281 C CG . PRO B 1 38 ? 31.856 4.068 33.468 1.00 20.41 ? 38 PRO B CG 1 ATOM 2282 C CD . PRO B 1 38 ? 32.215 4.788 34.718 1.00 17.72 ? 38 PRO B CD 1 ATOM 2283 N N . LEU B 1 39 ? 35.848 5.415 31.681 1.00 18.27 ? 39 LEU B N 1 ATOM 2284 C CA . LEU B 1 39 ? 36.434 6.196 30.598 1.00 18.54 ? 39 LEU B CA 1 ATOM 2285 C C . LEU B 1 39 ? 36.561 5.395 29.306 1.00 18.49 ? 39 LEU B C 1 ATOM 2286 O O . LEU B 1 39 ? 37.230 4.358 29.256 1.00 17.61 ? 39 LEU B O 1 ATOM 2287 C CB . LEU B 1 39 ? 37.813 6.703 31.034 1.00 19.10 ? 39 LEU B CB 1 ATOM 2288 C CG . LEU B 1 39 ? 38.607 7.657 30.134 1.00 19.74 ? 39 LEU B CG 1 ATOM 2289 C CD1 . LEU B 1 39 ? 37.842 8.951 29.899 1.00 18.17 ? 39 LEU B CD1 1 ATOM 2290 C CD2 . LEU B 1 39 ? 39.941 7.958 30.809 1.00 20.74 ? 39 LEU B CD2 1 ATOM 2291 N N . LEU B 1 40 ? 35.912 5.882 28.254 1.00 18.39 ? 40 LEU B N 1 ATOM 2292 C CA . LEU B 1 40 ? 35.964 5.206 26.961 1.00 19.82 ? 40 LEU B CA 1 ATOM 2293 C C . LEU B 1 40 ? 37.381 5.186 26.404 1.00 20.13 ? 40 LEU B C 1 ATOM 2294 O O . LEU B 1 40 ? 38.207 6.035 26.738 1.00 19.41 ? 40 LEU B O 1 ATOM 2295 C CB . LEU B 1 40 ? 35.041 5.902 25.956 1.00 17.70 ? 40 LEU B CB 1 ATOM 2296 C CG . LEU B 1 40 ? 33.543 5.839 26.255 1.00 16.96 ? 40 LEU B CG 1 ATOM 2297 C CD1 . LEU B 1 40 ? 32.797 6.786 25.311 1.00 14.85 ? 40 LEU B CD1 1 ATOM 2298 C CD2 . LEU B 1 40 ? 33.056 4.398 26.101 1.00 15.51 ? 40 LEU B CD2 1 ATOM 2299 N N . ARG B 1 41 ? 37.652 4.211 25.546 1.00 23.46 ? 41 ARG B N 1 ATOM 2300 C CA . ARG B 1 41 ? 38.963 4.093 24.931 1.00 25.23 ? 41 ARG B CA 1 ATOM 2301 C C . ARG B 1 41 ? 39.280 5.341 24.124 1.00 28.76 ? 41 ARG B C 1 ATOM 2302 O O . ARG B 1 41 ? 38.389 5.959 23.538 1.00 27.82 ? 41 ARG B O 1 ATOM 2303 C CB . ARG B 1 41 ? 39.013 2.862 24.034 1.00 24.23 ? 41 ARG B CB 1 ATOM 2304 C CG . ARG B 1 41 ? 39.246 1.574 24.797 1.00 24.40 ? 41 ARG B CG 1 ATOM 2305 C CD . ARG B 1 41 ? 39.118 0.370 23.894 1.00 25.88 ? 41 ARG B CD 1 ATOM 2306 N NE . ARG B 1 41 ? 37.720 0.057 23.623 1.00 26.45 ? 41 ARG B NE 1 ATOM 2307 C CZ . ARG B 1 41 ? 37.315 -0.927 22.830 1.00 26.53 ? 41 ARG B CZ 1 ATOM 2308 N NH1 . ARG B 1 41 ? 36.016 -1.143 22.651 1.00 26.15 ? 41 ARG B NH1 1 ATOM 2309 N NH2 . ARG B 1 41 ? 38.209 -1.687 22.208 1.00 26.02 ? 41 ARG B NH2 1 ATOM 2310 N N . LYS B 1 42 ? 40.557 5.709 24.111 1.00 33.46 ? 42 LYS B N 1 ATOM 2311 C CA . LYS B 1 42 ? 41.015 6.886 23.387 1.00 38.52 ? 42 LYS B CA 1 ATOM 2312 C C . LYS B 1 42 ? 41.098 6.539 21.911 1.00 41.22 ? 42 LYS B C 1 ATOM 2313 O O . LYS B 1 42 ? 40.330 7.043 21.092 1.00 41.56 ? 42 LYS B O 1 ATOM 2314 C CB . LYS B 1 42 ? 42.397 7.305 23.890 1.00 39.73 ? 42 LYS B CB 1 ATOM 2315 C CG . LYS B 1 42 ? 42.813 8.719 23.495 1.00 42.44 ? 42 LYS B CG 1 ATOM 2316 C CD . LYS B 1 42 ? 44.288 8.974 23.807 1.00 45.46 ? 42 LYS B CD 1 ATOM 2317 C CE . LYS B 1 42 ? 44.663 8.491 25.209 1.00 46.96 ? 42 LYS B CE 1 ATOM 2318 N NZ . LYS B 1 42 ? 46.095 8.727 25.553 1.00 47.57 ? 42 LYS B NZ 1 ATOM 2319 N N . LYS B 1 43 ? 42.042 5.668 21.579 1.00 45.27 ? 43 LYS B N 1 ATOM 2320 C CA . LYS B 1 43 ? 42.227 5.252 20.202 1.00 48.16 ? 43 LYS B CA 1 ATOM 2321 C C . LYS B 1 43 ? 41.656 3.868 19.976 1.00 49.22 ? 43 LYS B C 1 ATOM 2322 O O . LYS B 1 43 ? 41.526 3.063 20.899 1.00 48.19 ? 43 LYS B O 1 ATOM 2323 C CB . LYS B 1 43 ? 43.716 5.277 19.816 1.00 49.77 ? 43 LYS B CB 1 ATOM 2324 C CG . LYS B 1 43 ? 44.635 4.401 20.674 1.00 53.12 ? 43 LYS B CG 1 ATOM 2325 C CD . LYS B 1 43 ? 46.099 4.531 20.224 1.00 54.95 ? 43 LYS B CD 1 ATOM 2326 C CE . LYS B 1 43 ? 47.057 3.705 21.089 1.00 55.33 ? 43 LYS B CE 1 ATOM 2327 N NZ . LYS B 1 43 ? 48.486 3.850 20.656 1.00 54.13 ? 43 LYS B NZ 1 ATOM 2328 N N . CYS B 1 44 ? 41.310 3.614 18.724 1.00 51.73 ? 44 CYS B N 1 ATOM 2329 C CA . CYS B 1 44 ? 40.744 2.349 18.297 1.00 53.66 ? 44 CYS B CA 1 ATOM 2330 C C . CYS B 1 44 ? 40.418 2.584 16.825 1.00 56.79 ? 44 CYS B C 1 ATOM 2331 O O . CYS B 1 44 ? 39.400 3.194 16.486 1.00 57.76 ? 44 CYS B O 1 ATOM 2332 C CB . CYS B 1 44 ? 39.472 2.042 19.088 1.00 52.08 ? 44 CYS B CB 1 ATOM 2333 S SG . CYS B 1 44 ? 38.941 0.301 19.024 1.00 47.39 ? 44 CYS B SG 1 ATOM 2334 N N . ASP B 1 45 ? 41.309 2.109 15.960 1.00 59.18 ? 45 ASP B N 1 ATOM 2335 C CA . ASP B 1 45 ? 41.177 2.267 14.516 1.00 60.00 ? 45 ASP B CA 1 ATOM 2336 C C . ASP B 1 45 ? 40.501 1.078 13.837 1.00 58.90 ? 45 ASP B C 1 ATOM 2337 O O . ASP B 1 45 ? 39.509 1.232 13.129 1.00 58.96 ? 45 ASP B O 1 ATOM 2338 C CB . ASP B 1 45 ? 42.567 2.453 13.915 1.00 62.57 ? 45 ASP B CB 1 ATOM 2339 C CG . ASP B 1 45 ? 43.492 1.290 14.239 1.00 64.96 ? 45 ASP B CG 1 ATOM 2340 O OD1 . ASP B 1 45 ? 43.662 0.979 15.444 1.00 65.74 ? 45 ASP B OD1 1 ATOM 2341 O OD2 . ASP B 1 45 ? 44.042 0.686 13.291 1.00 66.37 ? 45 ASP B OD2 1 ATOM 2342 N N . ASP B 1 46 ? 41.059 -0.106 14.057 1.00 57.52 ? 46 ASP B N 1 ATOM 2343 C CA . ASP B 1 46 ? 40.550 -1.327 13.457 1.00 57.37 ? 46 ASP B CA 1 ATOM 2344 C C . ASP B 1 46 ? 39.025 -1.469 13.531 1.00 56.99 ? 46 ASP B C 1 ATOM 2345 O O . ASP B 1 46 ? 38.459 -1.735 14.594 1.00 57.34 ? 46 ASP B O 1 ATOM 2346 C CB . ASP B 1 46 ? 41.236 -2.532 14.109 1.00 57.57 ? 46 ASP B CB 1 ATOM 2347 C CG . ASP B 1 46 ? 41.006 -3.816 13.343 1.00 58.12 ? 46 ASP B CG 1 ATOM 2348 O OD1 . ASP B 1 46 ? 41.131 -3.790 12.101 1.00 57.90 ? 46 ASP B OD1 1 ATOM 2349 O OD2 . ASP B 1 46 ? 40.712 -4.851 13.980 1.00 58.10 ? 46 ASP B OD2 1 ATOM 2350 N N . PRO B 1 47 ? 38.337 -1.290 12.389 1.00 56.07 ? 47 PRO B N 1 ATOM 2351 C CA . PRO B 1 47 ? 36.876 -1.403 12.332 1.00 55.59 ? 47 PRO B CA 1 ATOM 2352 C C . PRO B 1 47 ? 36.461 -2.820 12.690 1.00 55.48 ? 47 PRO B C 1 ATOM 2353 O O . PRO B 1 47 ? 35.274 -3.122 12.829 1.00 55.41 ? 47 PRO B O 1 ATOM 2354 C CB . PRO B 1 47 ? 36.556 -1.077 10.875 1.00 55.42 ? 47 PRO B CB 1 ATOM 2355 C CG . PRO B 1 47 ? 37.697 -0.212 10.454 1.00 56.59 ? 47 PRO B CG 1 ATOM 2356 C CD . PRO B 1 47 ? 38.878 -0.898 11.079 1.00 56.08 ? 47 PRO B CD 1 ATOM 2357 N N . GLY B 1 48 ? 37.462 -3.686 12.823 1.00 55.18 ? 48 GLY B N 1 ATOM 2358 C CA . GLY B 1 48 ? 37.216 -5.075 13.155 1.00 54.70 ? 48 GLY B CA 1 ATOM 2359 C C . GLY B 1 48 ? 36.949 -5.285 14.631 1.00 54.20 ? 48 GLY B C 1 ATOM 2360 O O . GLY B 1 48 ? 36.803 -6.424 15.084 1.00 54.77 ? 48 GLY B O 1 ATOM 2361 N N . LYS B 1 49 ? 36.884 -4.191 15.386 1.00 52.56 ? 49 LYS B N 1 ATOM 2362 C CA . LYS B 1 49 ? 36.623 -4.281 16.819 1.00 50.72 ? 49 LYS B CA 1 ATOM 2363 C C . LYS B 1 49 ? 36.362 -2.923 17.462 1.00 47.32 ? 49 LYS B C 1 ATOM 2364 O O . LYS B 1 49 ? 36.193 -2.838 18.683 1.00 47.59 ? 49 LYS B O 1 ATOM 2365 C CB . LYS B 1 49 ? 37.804 -4.949 17.534 1.00 53.67 ? 49 LYS B CB 1 ATOM 2366 C CG . LYS B 1 49 ? 39.140 -4.234 17.330 1.00 56.44 ? 49 LYS B CG 1 ATOM 2367 C CD . LYS B 1 49 ? 40.195 -4.689 18.339 1.00 58.69 ? 49 LYS B CD 1 ATOM 2368 C CE . LYS B 1 49 ? 39.828 -4.265 19.761 1.00 59.70 ? 49 LYS B CE 1 ATOM 2369 N NZ . LYS B 1 49 ? 40.898 -4.612 20.740 1.00 60.68 ? 49 LYS B NZ 1 ATOM 2370 N N . CYS B 1 50 ? 36.322 -1.866 16.654 1.00 41.74 ? 50 CYS B N 1 ATOM 2371 C CA . CYS B 1 50 ? 36.105 -0.530 17.197 1.00 37.90 ? 50 CYS B CA 1 ATOM 2372 C C . CYS B 1 50 ? 34.698 0.023 17.053 1.00 32.51 ? 50 CYS B C 1 ATOM 2373 O O . CYS B 1 50 ? 34.468 1.227 17.182 1.00 28.86 ? 50 CYS B O 1 ATOM 2374 C CB . CYS B 1 50 ? 37.119 0.425 16.594 1.00 41.40 ? 50 CYS B CB 1 ATOM 2375 S SG . CYS B 1 50 ? 38.813 -0.087 17.034 1.00 49.86 ? 50 CYS B SG 1 ATOM 2376 N N . PHE B 1 51 ? 33.761 -0.880 16.798 1.00 27.85 ? 51 PHE B N 1 ATOM 2377 C CA . PHE B 1 51 ? 32.357 -0.535 16.658 1.00 25.29 ? 51 PHE B CA 1 ATOM 2378 C C . PHE B 1 51 ? 31.576 -1.628 17.347 1.00 23.74 ? 51 PHE B C 1 ATOM 2379 O O . PHE B 1 51 ? 32.033 -2.768 17.435 1.00 23.94 ? 51 PHE B O 1 ATOM 2380 C CB . PHE B 1 51 ? 31.945 -0.500 15.186 1.00 23.18 ? 51 PHE B CB 1 ATOM 2381 C CG . PHE B 1 51 ? 32.652 0.545 14.389 1.00 24.26 ? 51 PHE B CG 1 ATOM 2382 C CD1 . PHE B 1 51 ? 32.260 1.878 14.465 1.00 23.30 ? 51 PHE B CD1 1 ATOM 2383 C CD2 . PHE B 1 51 ? 33.740 0.205 13.587 1.00 23.63 ? 51 PHE B CD2 1 ATOM 2384 C CE1 . PHE B 1 51 ? 32.941 2.861 13.758 1.00 23.05 ? 51 PHE B CE1 1 ATOM 2385 C CE2 . PHE B 1 51 ? 34.427 1.179 12.876 1.00 24.39 ? 51 PHE B CE2 1 ATOM 2386 C CZ . PHE B 1 51 ? 34.028 2.512 12.963 1.00 23.39 ? 51 PHE B CZ 1 ATOM 2387 N N . VAL B 1 52 ? 30.406 -1.272 17.856 1.00 21.69 ? 52 VAL B N 1 ATOM 2388 C CA . VAL B 1 52 ? 29.530 -2.243 18.488 1.00 21.29 ? 52 VAL B CA 1 ATOM 2389 C C . VAL B 1 52 ? 28.289 -2.173 17.615 1.00 20.70 ? 52 VAL B C 1 ATOM 2390 O O . VAL B 1 52 ? 27.916 -1.090 17.171 1.00 19.36 ? 52 VAL B O 1 ATOM 2391 C CB . VAL B 1 52 ? 29.169 -1.847 19.940 1.00 21.16 ? 52 VAL B CB 1 ATOM 2392 C CG1 . VAL B 1 52 ? 28.093 -2.777 20.485 1.00 21.65 ? 52 VAL B CG1 1 ATOM 2393 C CG2 . VAL B 1 52 ? 30.403 -1.928 20.818 1.00 23.57 ? 52 VAL B CG2 1 ATOM 2394 N N . LEU B 1 53 ? 27.671 -3.312 17.331 1.00 20.10 ? 53 LEU B N 1 ATOM 2395 C CA . LEU B 1 53 ? 26.474 -3.290 16.508 1.00 21.29 ? 53 LEU B CA 1 ATOM 2396 C C . LEU B 1 53 ? 25.253 -3.373 17.401 1.00 20.63 ? 53 LEU B C 1 ATOM 2397 O O . LEU B 1 53 ? 25.175 -4.232 18.285 1.00 21.95 ? 53 LEU B O 1 ATOM 2398 C CB . LEU B 1 53 ? 26.473 -4.453 15.513 1.00 22.59 ? 53 LEU B CB 1 ATOM 2399 C CG . LEU B 1 53 ? 27.656 -4.490 14.535 1.00 25.21 ? 53 LEU B CG 1 ATOM 2400 C CD1 . LEU B 1 53 ? 27.534 -5.715 13.648 1.00 26.04 ? 53 LEU B CD1 1 ATOM 2401 C CD2 . LEU B 1 53 ? 27.685 -3.219 13.687 1.00 24.88 ? 53 LEU B CD2 1 ATOM 2402 N N . VAL B 1 54 ? 24.316 -2.456 17.188 1.00 17.70 ? 54 VAL B N 1 ATOM 2403 C CA . VAL B 1 54 ? 23.080 -2.434 17.956 1.00 17.54 ? 54 VAL B CA 1 ATOM 2404 C C . VAL B 1 54 ? 21.972 -2.831 16.997 1.00 17.54 ? 54 VAL B C 1 ATOM 2405 O O . VAL B 1 54 ? 21.632 -2.089 16.074 1.00 17.69 ? 54 VAL B O 1 ATOM 2406 C CB . VAL B 1 54 ? 22.787 -1.026 18.546 1.00 17.38 ? 54 VAL B CB 1 ATOM 2407 C CG1 . VAL B 1 54 ? 21.394 -0.991 19.171 1.00 17.09 ? 54 VAL B CG1 1 ATOM 2408 C CG2 . VAL B 1 54 ? 23.830 -0.678 19.594 1.00 16.76 ? 54 VAL B CG2 1 ATOM 2409 N N . ALA B 1 55 ? 21.430 -4.024 17.205 1.00 19.07 ? 55 ALA B N 1 ATOM 2410 C CA . ALA B 1 55 ? 20.364 -4.536 16.356 1.00 19.28 ? 55 ALA B CA 1 ATOM 2411 C C . ALA B 1 55 ? 19.000 -4.135 16.908 1.00 19.54 ? 55 ALA B C 1 ATOM 2412 O O . ALA B 1 55 ? 18.515 -4.703 17.892 1.00 20.28 ? 55 ALA B O 1 ATOM 2413 C CB . ALA B 1 55 ? 20.469 -6.056 16.247 1.00 19.66 ? 55 ALA B CB 1 ATOM 2414 N N . LEU B 1 56 ? 18.391 -3.148 16.264 1.00 19.76 ? 56 LEU B N 1 ATOM 2415 C CA . LEU B 1 56 ? 17.085 -2.648 16.661 1.00 20.68 ? 56 LEU B CA 1 ATOM 2416 C C . LEU B 1 56 ? 15.998 -3.286 15.800 1.00 22.43 ? 56 LEU B C 1 ATOM 2417 O O . LEU B 1 56 ? 16.087 -3.271 14.579 1.00 23.46 ? 56 LEU B O 1 ATOM 2418 C CB . LEU B 1 56 ? 17.030 -1.133 16.470 1.00 19.82 ? 56 LEU B CB 1 ATOM 2419 C CG . LEU B 1 56 ? 18.049 -0.271 17.206 1.00 20.21 ? 56 LEU B CG 1 ATOM 2420 C CD1 . LEU B 1 56 ? 17.834 1.187 16.817 1.00 19.86 ? 56 LEU B CD1 1 ATOM 2421 C CD2 . LEU B 1 56 ? 17.892 -0.471 18.710 1.00 19.89 ? 56 LEU B CD2 1 ATOM 2422 N N . SER B 1 57 ? 14.973 -3.839 16.435 1.00 23.30 ? 57 SER B N 1 ATOM 2423 C CA . SER B 1 57 ? 13.872 -4.453 15.702 1.00 25.63 ? 57 SER B CA 1 ATOM 2424 C C . SER B 1 57 ? 12.548 -4.018 16.319 1.00 26.68 ? 57 SER B C 1 ATOM 2425 O O . SER B 1 57 ? 12.444 -3.900 17.542 1.00 26.26 ? 57 SER B O 1 ATOM 2426 C CB . SER B 1 57 ? 13.992 -5.980 15.743 1.00 26.67 ? 57 SER B CB 1 ATOM 2427 O OG . SER B 1 57 ? 14.037 -6.466 17.077 1.00 29.67 ? 57 SER B OG 1 ATOM 2428 N N . ASN B 1 58 ? 11.539 -3.757 15.490 1.00 27.23 ? 58 ASN B N 1 ATOM 2429 C CA . ASN B 1 58 ? 10.261 -3.351 16.054 1.00 29.47 ? 58 ASN B CA 1 ATOM 2430 C C . ASN B 1 58 ? 9.235 -4.486 16.103 1.00 30.61 ? 58 ASN B C 1 ATOM 2431 O O . ASN B 1 58 ? 9.565 -5.656 15.868 1.00 28.72 ? 58 ASN B O 1 ATOM 2432 C CB . ASN B 1 58 ? 9.690 -2.101 15.344 1.00 28.23 ? 58 ASN B CB 1 ATOM 2433 C CG . ASN B 1 58 ? 9.374 -2.330 13.877 1.00 30.81 ? 58 ASN B CG 1 ATOM 2434 O OD1 . ASN B 1 58 ? 9.163 -3.462 13.434 1.00 30.83 ? 58 ASN B OD1 1 ATOM 2435 N ND2 . ASN B 1 58 ? 9.314 -1.240 13.115 1.00 28.35 ? 58 ASN B ND2 1 ATOM 2436 N N . ASP B 1 59 ? 7.997 -4.127 16.435 1.00 33.19 ? 59 ASP B N 1 ATOM 2437 C CA . ASP B 1 59 ? 6.901 -5.079 16.571 1.00 35.78 ? 59 ASP B CA 1 ATOM 2438 C C . ASP B 1 59 ? 6.566 -5.850 15.307 1.00 37.56 ? 59 ASP B C 1 ATOM 2439 O O . ASP B 1 59 ? 6.119 -6.996 15.378 1.00 38.29 ? 59 ASP B O 1 ATOM 2440 C CB . ASP B 1 59 ? 5.656 -4.347 17.067 1.00 36.19 ? 59 ASP B CB 1 ATOM 2441 C CG . ASP B 1 59 ? 5.845 -3.749 18.452 1.00 39.05 ? 59 ASP B CG 1 ATOM 2442 O OD1 . ASP B 1 59 ? 6.937 -3.200 18.722 1.00 36.95 ? 59 ASP B OD1 1 ATOM 2443 O OD2 . ASP B 1 59 ? 4.898 -3.817 19.269 1.00 40.09 ? 59 ASP B OD2 1 ATOM 2444 N N . ASN B 1 60 ? 6.784 -5.226 14.154 1.00 38.83 ? 60 ASN B N 1 ATOM 2445 C CA . ASN B 1 60 ? 6.480 -5.865 12.880 1.00 40.35 ? 60 ASN B CA 1 ATOM 2446 C C . ASN B 1 60 ? 7.660 -6.562 12.204 1.00 40.58 ? 60 ASN B C 1 ATOM 2447 O O . ASN B 1 60 ? 7.629 -6.807 11.001 1.00 41.88 ? 60 ASN B O 1 ATOM 2448 C CB . ASN B 1 60 ? 5.862 -4.844 11.919 1.00 41.72 ? 60 ASN B CB 1 ATOM 2449 C CG . ASN B 1 60 ? 4.468 -4.412 12.348 1.00 43.69 ? 60 ASN B CG 1 ATOM 2450 O OD1 . ASN B 1 60 ? 3.609 -5.250 12.623 1.00 45.49 ? 60 ASN B OD1 1 ATOM 2451 N ND2 . ASN B 1 60 ? 4.236 -3.103 12.401 1.00 44.42 ? 60 ASN B ND2 1 ATOM 2452 N N . GLY B 1 61 ? 8.699 -6.877 12.970 1.00 40.17 ? 61 GLY B N 1 ATOM 2453 C CA . GLY B 1 61 ? 9.847 -7.565 12.400 1.00 39.47 ? 61 GLY B CA 1 ATOM 2454 C C . GLY B 1 61 ? 10.885 -6.750 11.635 1.00 38.69 ? 61 GLY B C 1 ATOM 2455 O O . GLY B 1 61 ? 11.883 -7.311 11.168 1.00 39.51 ? 61 GLY B O 1 ATOM 2456 N N . GLN B 1 62 ? 10.668 -5.444 11.491 1.00 35.87 ? 62 GLN B N 1 ATOM 2457 C CA . GLN B 1 62 ? 11.621 -4.597 10.778 1.00 32.12 ? 62 GLN B CA 1 ATOM 2458 C C . GLN B 1 62 ? 12.896 -4.433 11.599 1.00 30.57 ? 62 GLN B C 1 ATOM 2459 O O . GLN B 1 62 ? 12.834 -4.199 12.805 1.00 29.97 ? 62 GLN B O 1 ATOM 2460 C CB . GLN B 1 62 ? 10.994 -3.241 10.500 1.00 31.57 ? 62 GLN B CB 1 ATOM 2461 C CG . GLN B 1 62 ? 9.843 -3.334 9.542 1.00 33.20 ? 62 GLN B CG 1 ATOM 2462 C CD . GLN B 1 62 ? 9.022 -2.078 9.517 1.00 34.15 ? 62 GLN B CD 1 ATOM 2463 O OE1 . GLN B 1 62 ? 8.433 -1.690 10.528 1.00 34.46 ? 62 GLN B OE1 1 ATOM 2464 N NE2 . GLN B 1 62 ? 8.973 -1.428 8.360 1.00 36.00 ? 62 GLN B NE2 1 ATOM 2465 N N . LEU B 1 63 ? 14.046 -4.560 10.939 1.00 28.29 ? 63 LEU B N 1 ATOM 2466 C CA . LEU B 1 63 ? 15.342 -4.460 11.604 1.00 26.91 ? 63 LEU B CA 1 ATOM 2467 C C . LEU B 1 63 ? 16.310 -3.434 11.016 1.00 25.78 ? 63 LEU B C 1 ATOM 2468 O O . LEU B 1 63 ? 16.471 -3.320 9.799 1.00 25.24 ? 63 LEU B O 1 ATOM 2469 C CB . LEU B 1 63 ? 16.034 -5.828 11.614 1.00 27.77 ? 63 LEU B CB 1 ATOM 2470 C CG . LEU B 1 63 ? 17.486 -5.861 12.119 1.00 30.02 ? 63 LEU B CG 1 ATOM 2471 C CD1 . LEU B 1 63 ? 17.544 -5.648 13.629 1.00 28.93 ? 63 LEU B CD1 1 ATOM 2472 C CD2 . LEU B 1 63 ? 18.109 -7.198 11.766 1.00 31.19 ? 63 LEU B CD2 1 ATOM 2473 N N . ALA B 1 64 ? 16.954 -2.695 11.912 1.00 23.43 ? 64 ALA B N 1 ATOM 2474 C CA . ALA B 1 64 ? 17.944 -1.692 11.551 1.00 22.19 ? 64 ALA B CA 1 ATOM 2475 C C . ALA B 1 64 ? 19.123 -2.001 12.456 1.00 21.74 ? 64 ALA B C 1 ATOM 2476 O O . ALA B 1 64 ? 18.987 -1.987 13.682 1.00 21.42 ? 64 ALA B O 1 ATOM 2477 C CB . ALA B 1 64 ? 17.414 -0.284 11.830 1.00 20.81 ? 64 ALA B CB 1 ATOM 2478 N N . GLU B 1 65 ? 20.268 -2.314 11.861 1.00 21.69 ? 65 GLU B N 1 ATOM 2479 C CA . GLU B 1 65 ? 21.455 -2.625 12.647 1.00 22.54 ? 65 GLU B CA 1 ATOM 2480 C C . GLU B 1 65 ? 22.336 -1.378 12.661 1.00 20.97 ? 65 GLU B C 1 ATOM 2481 O O . GLU B 1 65 ? 22.840 -0.956 11.621 1.00 19.82 ? 65 GLU B O 1 ATOM 2482 C CB . GLU B 1 65 ? 22.192 -3.815 12.034 1.00 25.68 ? 65 GLU B CB 1 ATOM 2483 C CG . GLU B 1 65 ? 23.174 -4.469 12.987 1.00 34.54 ? 65 GLU B CG 1 ATOM 2484 C CD . GLU B 1 65 ? 23.859 -5.691 12.392 1.00 39.68 ? 65 GLU B CD 1 ATOM 2485 O OE1 . GLU B 1 65 ? 24.698 -6.294 13.098 1.00 43.41 ? 65 GLU B OE1 1 ATOM 2486 O OE2 . GLU B 1 65 ? 23.560 -6.046 11.228 1.00 42.30 ? 65 GLU B OE2 1 ATOM 2487 N N . ILE B 1 66 ? 22.510 -0.797 13.850 1.00 19.37 ? 66 ILE B N 1 ATOM 2488 C CA . ILE B 1 66 ? 23.276 0.440 14.034 1.00 16.81 ? 66 ILE B CA 1 ATOM 2489 C C . ILE B 1 66 ? 24.743 0.232 14.422 1.00 16.28 ? 66 ILE B C 1 ATOM 2490 O O . ILE B 1 66 ? 25.045 -0.524 15.340 1.00 16.52 ? 66 ILE B O 1 ATOM 2491 C CB . ILE B 1 66 ? 22.624 1.327 15.138 1.00 14.12 ? 66 ILE B CB 1 ATOM 2492 C CG1 . ILE B 1 66 ? 21.101 1.373 14.958 1.00 14.56 ? 66 ILE B CG1 1 ATOM 2493 C CG2 . ILE B 1 66 ? 23.215 2.723 15.101 1.00 14.60 ? 66 ILE B CG2 1 ATOM 2494 C CD1 . ILE B 1 66 ? 20.618 2.074 13.691 1.00 13.91 ? 66 ILE B CD1 1 ATOM 2495 N N . ALA B 1 67 ? 25.645 0.916 13.719 1.00 15.88 ? 67 ALA B N 1 ATOM 2496 C CA . ALA B 1 67 ? 27.075 0.835 14.012 1.00 16.12 ? 67 ALA B CA 1 ATOM 2497 C C . ALA B 1 67 ? 27.416 1.976 14.980 1.00 16.77 ? 67 ALA B C 1 ATOM 2498 O O . ALA B 1 67 ? 27.262 3.159 14.648 1.00 16.67 ? 67 ALA B O 1 ATOM 2499 C CB . ALA B 1 67 ? 27.901 0.966 12.720 1.00 14.70 ? 67 ALA B CB 1 ATOM 2500 N N . ILE B 1 68 ? 27.860 1.610 16.182 1.00 16.53 ? 68 ILE B N 1 ATOM 2501 C CA . ILE B 1 68 ? 28.212 2.585 17.215 1.00 16.05 ? 68 ILE B CA 1 ATOM 2502 C C . ILE B 1 68 ? 29.720 2.575 17.462 1.00 16.64 ? 68 ILE B C 1 ATOM 2503 O O . ILE B 1 68 ? 30.310 1.530 17.731 1.00 16.57 ? 68 ILE B O 1 ATOM 2504 C CB . ILE B 1 68 ? 27.479 2.268 18.560 1.00 16.56 ? 68 ILE B CB 1 ATOM 2505 C CG1 . ILE B 1 68 ? 25.961 2.411 18.386 1.00 16.06 ? 68 ILE B CG1 1 ATOM 2506 C CG2 . ILE B 1 68 ? 27.981 3.196 19.678 1.00 13.89 ? 68 ILE B CG2 1 ATOM 2507 C CD1 . ILE B 1 68 ? 25.503 3.834 18.152 1.00 18.19 ? 68 ILE B CD1 1 ATOM 2508 N N . ASP B 1 69 ? 30.328 3.751 17.361 1.00 17.98 ? 69 ASP B N 1 ATOM 2509 C CA . ASP B 1 69 ? 31.764 3.941 17.574 1.00 19.27 ? 69 ASP B CA 1 ATOM 2510 C C . ASP B 1 69 ? 32.047 3.755 19.067 1.00 19.16 ? 69 ASP B C 1 ATOM 2511 O O . ASP B 1 69 ? 31.380 4.373 19.895 1.00 19.40 ? 69 ASP B O 1 ATOM 2512 C CB . ASP B 1 69 ? 32.131 5.360 17.136 1.00 22.99 ? 69 ASP B CB 1 ATOM 2513 C CG . ASP B 1 69 ? 33.597 5.659 17.284 1.00 27.90 ? 69 ASP B CG 1 ATOM 2514 O OD1 . ASP B 1 69 ? 34.124 5.545 18.408 1.00 31.06 ? 69 ASP B OD1 1 ATOM 2515 O OD2 . ASP B 1 69 ? 34.226 6.019 16.269 1.00 30.96 ? 69 ASP B OD2 1 ATOM 2516 N N . VAL B 1 70 ? 33.029 2.924 19.420 1.00 17.77 ? 70 VAL B N 1 ATOM 2517 C CA . VAL B 1 70 ? 33.315 2.683 20.838 1.00 18.38 ? 70 VAL B CA 1 ATOM 2518 C C . VAL B 1 70 ? 34.069 3.790 21.559 1.00 18.60 ? 70 VAL B C 1 ATOM 2519 O O . VAL B 1 70 ? 34.245 3.729 22.770 1.00 19.60 ? 70 VAL B O 1 ATOM 2520 C CB . VAL B 1 70 ? 34.095 1.366 21.065 1.00 18.26 ? 70 VAL B CB 1 ATOM 2521 C CG1 . VAL B 1 70 ? 33.315 0.197 20.496 1.00 17.53 ? 70 VAL B CG1 1 ATOM 2522 C CG2 . VAL B 1 70 ? 35.491 1.468 20.460 1.00 18.94 ? 70 VAL B CG2 1 ATOM 2523 N N . THR B 1 71 ? 34.516 4.803 20.830 1.00 18.38 ? 71 THR B N 1 ATOM 2524 C CA . THR B 1 71 ? 35.244 5.896 21.462 1.00 19.55 ? 71 THR B CA 1 ATOM 2525 C C . THR B 1 71 ? 34.349 7.104 21.746 1.00 19.85 ? 71 THR B C 1 ATOM 2526 O O . THR B 1 71 ? 34.651 7.910 22.625 1.00 20.09 ? 71 THR B O 1 ATOM 2527 C CB . THR B 1 71 ? 36.446 6.357 20.590 1.00 20.33 ? 71 THR B CB 1 ATOM 2528 O OG1 . THR B 1 71 ? 35.966 6.950 19.377 1.00 18.71 ? 71 THR B OG1 1 ATOM 2529 C CG2 . THR B 1 71 ? 37.351 5.166 20.258 1.00 19.73 ? 71 THR B CG2 1 ATOM 2530 N N . SER B 1 72 ? 33.239 7.222 21.019 1.00 19.92 ? 72 SER B N 1 ATOM 2531 C CA . SER B 1 72 ? 32.333 8.360 21.208 1.00 19.97 ? 72 SER B CA 1 ATOM 2532 C C . SER B 1 72 ? 30.883 7.933 21.418 1.00 18.75 ? 72 SER B C 1 ATOM 2533 O O . SER B 1 72 ? 30.030 8.757 21.749 1.00 17.16 ? 72 SER B O 1 ATOM 2534 C CB . SER B 1 72 ? 32.392 9.267 19.985 1.00 20.49 ? 72 SER B CB 1 ATOM 2535 O OG . SER B 1 72 ? 31.801 8.604 18.878 1.00 23.52 ? 72 SER B OG 1 ATOM 2536 N N . VAL B 1 73 ? 30.624 6.644 21.208 1.00 18.98 ? 73 VAL B N 1 ATOM 2537 C CA . VAL B 1 73 ? 29.298 6.048 21.327 1.00 18.38 ? 73 VAL B CA 1 ATOM 2538 C C . VAL B 1 73 ? 28.344 6.615 20.281 1.00 19.86 ? 73 VAL B C 1 ATOM 2539 O O . VAL B 1 73 ? 27.137 6.418 20.370 1.00 20.93 ? 73 VAL B O 1 ATOM 2540 C CB . VAL B 1 73 ? 28.659 6.290 22.711 1.00 19.51 ? 73 VAL B CB 1 ATOM 2541 C CG1 . VAL B 1 73 ? 27.456 5.365 22.879 1.00 19.84 ? 73 VAL B CG1 1 ATOM 2542 C CG2 . VAL B 1 73 ? 29.674 6.061 23.822 1.00 18.04 ? 73 VAL B CG2 1 ATOM 2543 N N . TYR B 1 74 ? 28.873 7.307 19.279 1.00 20.38 ? 74 TYR B N 1 ATOM 2544 C CA . TYR B 1 74 ? 27.988 7.885 18.273 1.00 21.76 ? 74 TYR B CA 1 ATOM 2545 C C . TYR B 1 74 ? 27.746 6.970 17.071 1.00 19.97 ? 74 TYR B C 1 ATOM 2546 O O . TYR B 1 74 ? 28.573 6.123 16.728 1.00 18.52 ? 74 TYR B O 1 ATOM 2547 C CB . TYR B 1 74 ? 28.531 9.235 17.790 1.00 24.61 ? 74 TYR B CB 1 ATOM 2548 C CG . TYR B 1 74 ? 27.457 10.300 17.549 1.00 27.18 ? 74 TYR B CG 1 ATOM 2549 C CD1 . TYR B 1 74 ? 26.809 10.934 18.624 1.00 26.81 ? 74 TYR B CD1 1 ATOM 2550 C CD2 . TYR B 1 74 ? 27.134 10.714 16.251 1.00 26.94 ? 74 TYR B CD2 1 ATOM 2551 C CE1 . TYR B 1 74 ? 25.882 11.958 18.408 1.00 26.25 ? 74 TYR B CE1 1 ATOM 2552 C CE2 . TYR B 1 74 ? 26.207 11.730 16.026 1.00 26.49 ? 74 TYR B CE2 1 ATOM 2553 C CZ . TYR B 1 74 ? 25.589 12.351 17.104 1.00 26.63 ? 74 TYR B CZ 1 ATOM 2554 O OH . TYR B 1 74 ? 24.702 13.383 16.873 1.00 28.67 ? 74 TYR B OH 1 ATOM 2555 N N . VAL B 1 75 ? 26.589 7.160 16.444 1.00 18.49 ? 75 VAL B N 1 ATOM 2556 C CA . VAL B 1 75 ? 26.178 6.393 15.275 1.00 17.93 ? 75 VAL B CA 1 ATOM 2557 C C . VAL B 1 75 ? 26.996 6.808 14.041 1.00 18.04 ? 75 VAL B C 1 ATOM 2558 O O . VAL B 1 75 ? 27.073 7.994 13.722 1.00 18.27 ? 75 VAL B O 1 ATOM 2559 C CB . VAL B 1 75 ? 24.669 6.635 14.988 1.00 17.94 ? 75 VAL B CB 1 ATOM 2560 C CG1 . VAL B 1 75 ? 24.219 5.814 13.805 1.00 15.77 ? 75 VAL B CG1 1 ATOM 2561 C CG2 . VAL B 1 75 ? 23.844 6.298 16.225 1.00 16.81 ? 75 VAL B CG2 1 ATOM 2562 N N . VAL B 1 76 ? 27.605 5.840 13.357 1.00 17.46 ? 76 VAL B N 1 ATOM 2563 C CA . VAL B 1 76 ? 28.389 6.135 12.157 1.00 17.47 ? 76 VAL B CA 1 ATOM 2564 C C . VAL B 1 76 ? 27.642 5.716 10.882 1.00 17.35 ? 76 VAL B C 1 ATOM 2565 O O . VAL B 1 76 ? 27.861 6.277 9.805 1.00 16.04 ? 76 VAL B O 1 ATOM 2566 C CB . VAL B 1 76 ? 29.762 5.417 12.179 1.00 18.32 ? 76 VAL B CB 1 ATOM 2567 C CG1 . VAL B 1 76 ? 30.594 5.924 13.342 1.00 19.31 ? 76 VAL B CG1 1 ATOM 2568 C CG2 . VAL B 1 76 ? 29.560 3.921 12.285 1.00 19.35 ? 76 VAL B CG2 1 ATOM 2569 N N . GLY B 1 77 ? 26.764 4.726 11.016 1.00 16.09 ? 77 GLY B N 1 ATOM 2570 C CA . GLY B 1 77 ? 25.994 4.246 9.882 1.00 14.95 ? 77 GLY B CA 1 ATOM 2571 C C . GLY B 1 77 ? 25.095 3.111 10.326 1.00 16.58 ? 77 GLY B C 1 ATOM 2572 O O . GLY B 1 77 ? 25.068 2.766 11.510 1.00 17.07 ? 77 GLY B O 1 ATOM 2573 N N . TYR B 1 78 ? 24.355 2.522 9.396 1.00 15.57 ? 78 TYR B N 1 ATOM 2574 C CA . TYR B 1 78 ? 23.470 1.418 9.748 1.00 16.60 ? 78 TYR B CA 1 ATOM 2575 C C . TYR B 1 78 ? 23.133 0.556 8.539 1.00 18.50 ? 78 TYR B C 1 ATOM 2576 O O . TYR B 1 78 ? 23.326 0.964 7.387 1.00 17.79 ? 78 TYR B O 1 ATOM 2577 C CB . TYR B 1 78 ? 22.165 1.942 10.359 1.00 15.44 ? 78 TYR B CB 1 ATOM 2578 C CG . TYR B 1 78 ? 21.335 2.765 9.402 1.00 16.73 ? 78 TYR B CG 1 ATOM 2579 C CD1 . TYR B 1 78 ? 21.670 4.088 9.122 1.00 15.77 ? 78 TYR B CD1 1 ATOM 2580 C CD2 . TYR B 1 78 ? 20.251 2.202 8.724 1.00 16.43 ? 78 TYR B CD2 1 ATOM 2581 C CE1 . TYR B 1 78 ? 20.956 4.827 8.186 1.00 16.51 ? 78 TYR B CE1 1 ATOM 2582 C CE2 . TYR B 1 78 ? 19.529 2.939 7.781 1.00 16.30 ? 78 TYR B CE2 1 ATOM 2583 C CZ . TYR B 1 78 ? 19.893 4.248 7.518 1.00 15.86 ? 78 TYR B CZ 1 ATOM 2584 O OH . TYR B 1 78 ? 19.222 4.978 6.571 1.00 16.80 ? 78 TYR B OH 1 ATOM 2585 N N . GLN B 1 79 ? 22.628 -0.642 8.810 1.00 19.61 ? 79 GLN B N 1 ATOM 2586 C CA . GLN B 1 79 ? 22.235 -1.546 7.747 1.00 20.53 ? 79 GLN B CA 1 ATOM 2587 C C . GLN B 1 79 ? 20.768 -1.950 7.877 1.00 20.82 ? 79 GLN B C 1 ATOM 2588 O O . GLN B 1 79 ? 20.288 -2.284 8.968 1.00 20.21 ? 79 GLN B O 1 ATOM 2589 C CB . GLN B 1 79 ? 23.094 -2.809 7.756 1.00 22.04 ? 79 GLN B CB 1 ATOM 2590 C CG . GLN B 1 79 ? 22.837 -3.690 6.541 1.00 26.00 ? 79 GLN B CG 1 ATOM 2591 C CD . GLN B 1 79 ? 23.306 -5.113 6.723 1.00 26.90 ? 79 GLN B CD 1 ATOM 2592 O OE1 . GLN B 1 79 ? 24.338 -5.365 7.343 1.00 27.73 ? 79 GLN B OE1 1 ATOM 2593 N NE2 . GLN B 1 79 ? 22.554 -6.058 6.164 1.00 28.67 ? 79 GLN B NE2 1 ATOM 2594 N N . VAL B 1 80 ? 20.063 -1.894 6.753 1.00 20.16 ? 80 VAL B N 1 ATOM 2595 C CA . VAL B 1 80 ? 18.667 -2.298 6.676 1.00 22.12 ? 80 VAL B CA 1 ATOM 2596 C C . VAL B 1 80 ? 18.588 -3.167 5.420 1.00 23.77 ? 80 VAL B C 1 ATOM 2597 O O . VAL B 1 80 ? 19.066 -2.768 4.357 1.00 23.23 ? 80 VAL B O 1 ATOM 2598 C CB . VAL B 1 80 ? 17.703 -1.084 6.549 1.00 21.78 ? 80 VAL B CB 1 ATOM 2599 C CG1 . VAL B 1 80 ? 17.409 -0.503 7.931 1.00 20.31 ? 80 VAL B CG1 1 ATOM 2600 C CG2 . VAL B 1 80 ? 18.315 -0.014 5.655 1.00 21.69 ? 80 VAL B CG2 1 ATOM 2601 N N . ARG B 1 81 ? 18.013 -4.361 5.553 1.00 25.36 ? 81 ARG B N 1 ATOM 2602 C CA . ARG B 1 81 ? 17.898 -5.292 4.430 1.00 26.51 ? 81 ARG B CA 1 ATOM 2603 C C . ARG B 1 81 ? 19.286 -5.547 3.839 1.00 26.57 ? 81 ARG B C 1 ATOM 2604 O O . ARG B 1 81 ? 20.235 -5.817 4.582 1.00 26.77 ? 81 ARG B O 1 ATOM 2605 C CB . ARG B 1 81 ? 16.947 -4.723 3.376 1.00 27.45 ? 81 ARG B CB 1 ATOM 2606 C CG . ARG B 1 81 ? 15.530 -4.526 3.904 1.00 32.55 ? 81 ARG B CG 1 ATOM 2607 C CD . ARG B 1 81 ? 14.672 -3.737 2.934 1.00 36.33 ? 81 ARG B CD 1 ATOM 2608 N NE . ARG B 1 81 ? 13.313 -3.549 3.436 1.00 40.43 ? 81 ARG B NE 1 ATOM 2609 C CZ . ARG B 1 81 ? 12.367 -2.857 2.804 1.00 42.65 ? 81 ARG B CZ 1 ATOM 2610 N NH1 . ARG B 1 81 ? 12.622 -2.279 1.635 1.00 43.98 ? 81 ARG B NH1 1 ATOM 2611 N NH2 . ARG B 1 81 ? 11.163 -2.732 3.347 1.00 43.40 ? 81 ARG B NH2 1 ATOM 2612 N N . ASN B 1 82 ? 19.415 -5.453 2.518 1.00 26.36 ? 82 ASN B N 1 ATOM 2613 C CA . ASN B 1 82 ? 20.702 -5.695 1.859 1.00 26.54 ? 82 ASN B CA 1 ATOM 2614 C C . ASN B 1 82 ? 21.483 -4.408 1.608 1.00 25.50 ? 82 ASN B C 1 ATOM 2615 O O . ASN B 1 82 ? 22.416 -4.390 0.807 1.00 25.41 ? 82 ASN B O 1 ATOM 2616 C CB . ASN B 1 82 ? 20.492 -6.413 0.517 1.00 27.83 ? 82 ASN B CB 1 ATOM 2617 C CG . ASN B 1 82 ? 19.717 -5.564 -0.487 1.00 28.86 ? 82 ASN B CG 1 ATOM 2618 O OD1 . ASN B 1 82 ? 19.913 -5.680 -1.698 1.00 28.73 ? 82 ASN B OD1 1 ATOM 2619 N ND2 . ASN B 1 82 ? 18.824 -4.713 0.016 1.00 28.26 ? 82 ASN B ND2 1 ATOM 2620 N N . ARG B 1 83 ? 21.108 -3.335 2.298 1.00 24.47 ? 83 ARG B N 1 ATOM 2621 C CA . ARG B 1 83 ? 21.772 -2.051 2.113 1.00 24.31 ? 83 ARG B CA 1 ATOM 2622 C C . ARG B 1 83 ? 22.303 -1.454 3.408 1.00 23.45 ? 83 ARG B C 1 ATOM 2623 O O . ARG B 1 83 ? 21.916 -1.866 4.501 1.00 23.60 ? 83 ARG B O 1 ATOM 2624 C CB . ARG B 1 83 ? 20.798 -1.056 1.489 1.00 26.54 ? 83 ARG B CB 1 ATOM 2625 C CG . ARG B 1 83 ? 20.318 -1.440 0.103 1.00 31.30 ? 83 ARG B CG 1 ATOM 2626 C CD . ARG B 1 83 ? 18.993 -0.777 -0.188 1.00 34.34 ? 83 ARG B CD 1 ATOM 2627 N NE . ARG B 1 83 ? 18.554 -1.003 -1.562 1.00 39.43 ? 83 ARG B NE 1 ATOM 2628 C CZ . ARG B 1 83 ? 19.096 -0.420 -2.626 1.00 41.28 ? 83 ARG B CZ 1 ATOM 2629 N NH1 . ARG B 1 83 ? 20.109 0.432 -2.480 1.00 42.08 ? 83 ARG B NH1 1 ATOM 2630 N NH2 . ARG B 1 83 ? 18.620 -0.684 -3.837 1.00 42.38 ? 83 ARG B NH2 1 ATOM 2631 N N . SER B 1 84 ? 23.196 -0.481 3.271 1.00 21.23 ? 84 SER B N 1 ATOM 2632 C CA . SER B 1 84 ? 23.754 0.217 4.419 1.00 20.47 ? 84 SER B CA 1 ATOM 2633 C C . SER B 1 84 ? 23.956 1.680 4.037 1.00 19.78 ? 84 SER B C 1 ATOM 2634 O O . SER B 1 84 ? 24.137 2.003 2.860 1.00 18.67 ? 84 SER B O 1 ATOM 2635 C CB . SER B 1 84 ? 25.076 -0.425 4.875 1.00 20.70 ? 84 SER B CB 1 ATOM 2636 O OG . SER B 1 84 ? 26.088 -0.358 3.890 1.00 22.64 ? 84 SER B OG 1 ATOM 2637 N N . TYR B 1 85 ? 23.882 2.561 5.031 1.00 19.30 ? 85 TYR B N 1 ATOM 2638 C CA . TYR B 1 85 ? 24.054 3.997 4.821 1.00 19.06 ? 85 TYR B CA 1 ATOM 2639 C C . TYR B 1 85 ? 25.007 4.527 5.881 1.00 18.64 ? 85 TYR B C 1 ATOM 2640 O O . TYR B 1 85 ? 24.927 4.128 7.042 1.00 18.01 ? 85 TYR B O 1 ATOM 2641 C CB . TYR B 1 85 ? 22.708 4.724 4.927 1.00 20.35 ? 85 TYR B CB 1 ATOM 2642 C CG . TYR B 1 85 ? 21.672 4.198 3.963 1.00 22.37 ? 85 TYR B CG 1 ATOM 2643 C CD1 . TYR B 1 85 ? 21.012 2.992 4.213 1.00 22.48 ? 85 TYR B CD1 1 ATOM 2644 C CD2 . TYR B 1 85 ? 21.403 4.866 2.761 1.00 22.30 ? 85 TYR B CD2 1 ATOM 2645 C CE1 . TYR B 1 85 ? 20.113 2.456 3.287 1.00 25.05 ? 85 TYR B CE1 1 ATOM 2646 C CE2 . TYR B 1 85 ? 20.505 4.338 1.826 1.00 23.52 ? 85 TYR B CE2 1 ATOM 2647 C CZ . TYR B 1 85 ? 19.868 3.133 2.096 1.00 23.75 ? 85 TYR B CZ 1 ATOM 2648 O OH . TYR B 1 85 ? 19.005 2.584 1.180 1.00 24.63 ? 85 TYR B OH 1 ATOM 2649 N N . PHE B 1 86 ? 25.905 5.421 5.478 1.00 17.40 ? 86 PHE B N 1 ATOM 2650 C CA . PHE B 1 86 ? 26.886 5.991 6.391 1.00 16.58 ? 86 PHE B CA 1 ATOM 2651 C C . PHE B 1 86 ? 26.816 7.502 6.362 1.00 18.31 ? 86 PHE B C 1 ATOM 2652 O O . PHE B 1 86 ? 26.600 8.099 5.305 1.00 19.15 ? 86 PHE B O 1 ATOM 2653 C CB . PHE B 1 86 ? 28.296 5.554 5.988 1.00 16.12 ? 86 PHE B CB 1 ATOM 2654 C CG . PHE B 1 86 ? 28.547 4.088 6.155 1.00 16.98 ? 86 PHE B CG 1 ATOM 2655 C CD1 . PHE B 1 86 ? 29.120 3.597 7.323 1.00 18.23 ? 86 PHE B CD1 1 ATOM 2656 C CD2 . PHE B 1 86 ? 28.176 3.189 5.161 1.00 17.86 ? 86 PHE B CD2 1 ATOM 2657 C CE1 . PHE B 1 86 ? 29.321 2.229 7.503 1.00 19.99 ? 86 PHE B CE1 1 ATOM 2658 C CE2 . PHE B 1 86 ? 28.370 1.816 5.328 1.00 19.50 ? 86 PHE B CE2 1 ATOM 2659 C CZ . PHE B 1 86 ? 28.944 1.335 6.504 1.00 19.94 ? 86 PHE B CZ 1 ATOM 2660 N N . PHE B 1 87 ? 26.988 8.120 7.527 1.00 17.83 ? 87 PHE B N 1 ATOM 2661 C CA . PHE B 1 87 ? 26.977 9.572 7.622 1.00 18.35 ? 87 PHE B CA 1 ATOM 2662 C C . PHE B 1 87 ? 28.125 10.070 6.759 1.00 19.59 ? 87 PHE B C 1 ATOM 2663 O O . PHE B 1 87 ? 29.120 9.364 6.577 1.00 19.19 ? 87 PHE B O 1 ATOM 2664 C CB . PHE B 1 87 ? 27.177 10.012 9.078 1.00 17.45 ? 87 PHE B CB 1 ATOM 2665 C CG . PHE B 1 87 ? 25.903 10.048 9.886 1.00 18.12 ? 87 PHE B CG 1 ATOM 2666 C CD1 . PHE B 1 87 ? 25.892 9.612 11.211 1.00 18.77 ? 87 PHE B CD1 1 ATOM 2667 C CD2 . PHE B 1 87 ? 24.726 10.558 9.337 1.00 17.01 ? 87 PHE B CD2 1 ATOM 2668 C CE1 . PHE B 1 87 ? 24.730 9.684 11.981 1.00 18.89 ? 87 PHE B CE1 1 ATOM 2669 C CE2 . PHE B 1 87 ? 23.553 10.638 10.093 1.00 18.02 ? 87 PHE B CE2 1 ATOM 2670 C CZ . PHE B 1 87 ? 23.552 10.201 11.419 1.00 19.83 ? 87 PHE B CZ 1 ATOM 2671 N N . LYS B 1 88 ? 27.983 11.280 6.234 1.00 21.16 ? 88 LYS B N 1 ATOM 2672 C CA . LYS B 1 88 ? 29.001 11.872 5.377 1.00 25.52 ? 88 LYS B CA 1 ATOM 2673 C C . LYS B 1 88 ? 30.370 11.897 6.045 1.00 26.74 ? 88 LYS B C 1 ATOM 2674 O O . LYS B 1 88 ? 31.390 11.635 5.408 1.00 27.25 ? 88 LYS B O 1 ATOM 2675 C CB . LYS B 1 88 ? 28.598 13.303 4.990 1.00 28.25 ? 88 LYS B CB 1 ATOM 2676 C CG . LYS B 1 88 ? 29.520 13.955 3.955 1.00 32.00 ? 88 LYS B CG 1 ATOM 2677 C CD . LYS B 1 88 ? 29.508 13.175 2.635 1.00 36.25 ? 88 LYS B CD 1 ATOM 2678 C CE . LYS B 1 88 ? 30.469 13.768 1.610 1.00 38.02 ? 88 LYS B CE 1 ATOM 2679 N NZ . LYS B 1 88 ? 31.886 13.733 2.081 1.00 40.10 ? 88 LYS B NZ 1 ATOM 2680 N N . ASP B 1 89 ? 30.385 12.207 7.335 1.00 28.25 ? 89 ASP B N 1 ATOM 2681 C CA . ASP B 1 89 ? 31.628 12.293 8.087 1.00 30.64 ? 89 ASP B CA 1 ATOM 2682 C C . ASP B 1 89 ? 32.094 10.985 8.727 1.00 31.83 ? 89 ASP B C 1 ATOM 2683 O O . ASP B 1 89 ? 32.985 10.995 9.571 1.00 32.69 ? 89 ASP B O 1 ATOM 2684 C CB . ASP B 1 89 ? 31.499 13.386 9.154 1.00 31.28 ? 89 ASP B CB 1 ATOM 2685 C CG . ASP B 1 89 ? 30.299 13.183 10.064 1.00 32.94 ? 89 ASP B CG 1 ATOM 2686 O OD1 . ASP B 1 89 ? 29.350 12.476 9.670 1.00 31.81 ? 89 ASP B OD1 1 ATOM 2687 O OD2 . ASP B 1 89 ? 30.296 13.748 11.176 1.00 36.19 ? 89 ASP B OD2 1 ATOM 2688 N N . ALA B 1 90 ? 31.504 9.863 8.327 1.00 32.56 ? 90 ALA B N 1 ATOM 2689 C CA . ALA B 1 90 ? 31.906 8.569 8.875 1.00 34.23 ? 90 ALA B CA 1 ATOM 2690 C C . ALA B 1 90 ? 33.306 8.218 8.361 1.00 35.38 ? 90 ALA B C 1 ATOM 2691 O O . ALA B 1 90 ? 33.563 8.280 7.159 1.00 35.40 ? 90 ALA B O 1 ATOM 2692 C CB . ALA B 1 90 ? 30.908 7.481 8.456 1.00 33.70 ? 90 ALA B CB 1 ATOM 2693 N N . PRO B 1 91 ? 34.229 7.843 9.267 1.00 36.57 ? 91 PRO B N 1 ATOM 2694 C CA . PRO B 1 91 ? 35.594 7.487 8.863 1.00 37.29 ? 91 PRO B CA 1 ATOM 2695 C C . PRO B 1 91 ? 35.617 6.402 7.784 1.00 39.03 ? 91 PRO B C 1 ATOM 2696 O O . PRO B 1 91 ? 34.859 5.434 7.845 1.00 40.00 ? 91 PRO B O 1 ATOM 2697 C CB . PRO B 1 91 ? 36.235 7.038 10.176 1.00 36.12 ? 91 PRO B CB 1 ATOM 2698 C CG . PRO B 1 91 ? 35.072 6.560 10.990 1.00 36.13 ? 91 PRO B CG 1 ATOM 2699 C CD . PRO B 1 91 ? 34.034 7.606 10.707 1.00 36.12 ? 91 PRO B CD 1 ATOM 2700 N N . ASP B 1 92 ? 36.491 6.568 6.797 1.00 40.66 ? 92 ASP B N 1 ATOM 2701 C CA . ASP B 1 92 ? 36.591 5.621 5.691 1.00 42.53 ? 92 ASP B CA 1 ATOM 2702 C C . ASP B 1 92 ? 36.788 4.168 6.098 1.00 42.22 ? 92 ASP B C 1 ATOM 2703 O O . ASP B 1 92 ? 36.407 3.259 5.358 1.00 42.86 ? 92 ASP B O 1 ATOM 2704 C CB . ASP B 1 92 ? 37.711 6.041 4.741 1.00 45.51 ? 92 ASP B CB 1 ATOM 2705 C CG . ASP B 1 92 ? 37.521 7.449 4.215 1.00 49.03 ? 92 ASP B CG 1 ATOM 2706 O OD1 . ASP B 1 92 ? 36.367 7.802 3.883 1.00 49.68 ? 92 ASP B OD1 1 ATOM 2707 O OD2 . ASP B 1 92 ? 38.519 8.199 4.129 1.00 51.32 ? 92 ASP B OD2 1 ATOM 2708 N N . ALA B 1 93 ? 37.384 3.944 7.265 1.00 40.85 ? 93 ALA B N 1 ATOM 2709 C CA . ALA B 1 93 ? 37.609 2.582 7.743 1.00 38.72 ? 93 ALA B CA 1 ATOM 2710 C C . ALA B 1 93 ? 36.274 1.959 8.128 1.00 36.28 ? 93 ALA B C 1 ATOM 2711 O O . ALA B 1 93 ? 36.079 0.751 7.999 1.00 36.14 ? 93 ALA B O 1 ATOM 2712 C CB . ALA B 1 93 ? 38.552 2.590 8.940 1.00 38.90 ? 93 ALA B CB 1 ATOM 2713 N N . ALA B 1 94 ? 35.359 2.795 8.610 1.00 34.15 ? 94 ALA B N 1 ATOM 2714 C CA . ALA B 1 94 ? 34.035 2.330 8.994 1.00 31.12 ? 94 ALA B CA 1 ATOM 2715 C C . ALA B 1 94 ? 33.277 2.030 7.712 1.00 29.42 ? 94 ALA B C 1 ATOM 2716 O O . ALA B 1 94 ? 32.671 0.969 7.567 1.00 28.60 ? 94 ALA B O 1 ATOM 2717 C CB . ALA B 1 94 ? 33.305 3.401 9.795 1.00 29.70 ? 94 ALA B CB 1 ATOM 2718 N N . TYR B 1 95 ? 33.335 2.969 6.775 1.00 27.72 ? 95 TYR B N 1 ATOM 2719 C CA . TYR B 1 95 ? 32.653 2.813 5.502 1.00 28.72 ? 95 TYR B CA 1 ATOM 2720 C C . TYR B 1 95 ? 33.081 1.528 4.812 1.00 29.05 ? 95 TYR B C 1 ATOM 2721 O O . TYR B 1 95 ? 32.253 0.788 4.293 1.00 28.26 ? 95 TYR B O 1 ATOM 2722 C CB . TYR B 1 95 ? 32.957 3.995 4.580 1.00 28.94 ? 95 TYR B CB 1 ATOM 2723 C CG . TYR B 1 95 ? 32.145 3.977 3.306 1.00 30.45 ? 95 TYR B CG 1 ATOM 2724 C CD1 . TYR B 1 95 ? 30.787 4.309 3.317 1.00 30.97 ? 95 TYR B CD1 1 ATOM 2725 C CD2 . TYR B 1 95 ? 32.720 3.601 2.094 1.00 31.36 ? 95 TYR B CD2 1 ATOM 2726 C CE1 . TYR B 1 95 ? 30.020 4.268 2.152 1.00 31.52 ? 95 TYR B CE1 1 ATOM 2727 C CE2 . TYR B 1 95 ? 31.962 3.553 0.922 1.00 32.89 ? 95 TYR B CE2 1 ATOM 2728 C CZ . TYR B 1 95 ? 30.613 3.890 0.958 1.00 32.91 ? 95 TYR B CZ 1 ATOM 2729 O OH . TYR B 1 95 ? 29.865 3.859 -0.202 1.00 35.69 ? 95 TYR B OH 1 ATOM 2730 N N . GLU B 1 96 ? 34.383 1.268 4.816 1.00 30.47 ? 96 GLU B N 1 ATOM 2731 C CA . GLU B 1 96 ? 34.931 0.081 4.172 1.00 31.95 ? 96 GLU B CA 1 ATOM 2732 C C . GLU B 1 96 ? 34.832 -1.202 4.993 1.00 30.43 ? 96 GLU B C 1 ATOM 2733 O O . GLU B 1 96 ? 34.549 -2.268 4.451 1.00 31.01 ? 96 GLU B O 1 ATOM 2734 C CB . GLU B 1 96 ? 36.399 0.324 3.803 1.00 34.94 ? 96 GLU B CB 1 ATOM 2735 C CG . GLU B 1 96 ? 36.677 0.484 2.305 1.00 41.39 ? 96 GLU B CG 1 ATOM 2736 C CD . GLU B 1 96 ? 36.100 1.763 1.712 1.00 44.85 ? 96 GLU B CD 1 ATOM 2737 O OE1 . GLU B 1 96 ? 36.450 2.861 2.204 1.00 47.44 ? 96 GLU B OE1 1 ATOM 2738 O OE2 . GLU B 1 96 ? 35.304 1.671 0.748 1.00 46.51 ? 96 GLU B OE2 1 ATOM 2739 N N . GLY B 1 97 ? 35.054 -1.103 6.299 1.00 29.08 ? 97 GLY B N 1 ATOM 2740 C CA . GLY B 1 97 ? 35.025 -2.290 7.135 1.00 27.30 ? 97 GLY B CA 1 ATOM 2741 C C . GLY B 1 97 ? 33.690 -2.809 7.634 1.00 27.18 ? 97 GLY B C 1 ATOM 2742 O O . GLY B 1 97 ? 33.576 -3.988 7.977 1.00 27.13 ? 97 GLY B O 1 ATOM 2743 N N . LEU B 1 98 ? 32.678 -1.950 7.677 1.00 25.40 ? 98 LEU B N 1 ATOM 2744 C CA . LEU B 1 98 ? 31.366 -2.355 8.179 1.00 25.32 ? 98 LEU B CA 1 ATOM 2745 C C . LEU B 1 98 ? 30.364 -2.768 7.105 1.00 24.92 ? 98 LEU B C 1 ATOM 2746 O O . LEU B 1 98 ? 30.427 -2.289 5.975 1.00 25.42 ? 98 LEU B O 1 ATOM 2747 C CB . LEU B 1 98 ? 30.761 -1.216 9.006 1.00 23.66 ? 98 LEU B CB 1 ATOM 2748 C CG . LEU B 1 98 ? 31.478 -0.871 10.306 1.00 22.74 ? 98 LEU B CG 1 ATOM 2749 C CD1 . LEU B 1 98 ? 31.056 0.510 10.783 1.00 21.42 ? 98 LEU B CD1 1 ATOM 2750 C CD2 . LEU B 1 98 ? 31.162 -1.943 11.335 1.00 23.00 ? 98 LEU B CD2 1 ATOM 2751 N N . PHE B 1 99 ? 29.443 -3.655 7.479 1.00 24.26 ? 99 PHE B N 1 ATOM 2752 C CA . PHE B 1 99 ? 28.388 -4.120 6.585 1.00 25.89 ? 99 PHE B CA 1 ATOM 2753 C C . PHE B 1 99 ? 28.931 -4.368 5.181 1.00 27.74 ? 99 PHE B C 1 ATOM 2754 O O . PHE B 1 99 ? 28.451 -3.774 4.209 1.00 27.85 ? 99 PHE B O 1 ATOM 2755 C CB . PHE B 1 99 ? 27.285 -3.061 6.512 1.00 24.74 ? 99 PHE B CB 1 ATOM 2756 C CG . PHE B 1 99 ? 26.886 -2.499 7.847 1.00 23.74 ? 99 PHE B CG 1 ATOM 2757 C CD1 . PHE B 1 99 ? 26.884 -1.121 8.061 1.00 22.17 ? 99 PHE B CD1 1 ATOM 2758 C CD2 . PHE B 1 99 ? 26.492 -3.339 8.886 1.00 23.85 ? 99 PHE B CD2 1 ATOM 2759 C CE1 . PHE B 1 99 ? 26.491 -0.587 9.291 1.00 23.16 ? 99 PHE B CE1 1 ATOM 2760 C CE2 . PHE B 1 99 ? 26.095 -2.813 10.124 1.00 24.74 ? 99 PHE B CE2 1 ATOM 2761 C CZ . PHE B 1 99 ? 26.095 -1.433 10.323 1.00 22.25 ? 99 PHE B CZ 1 ATOM 2762 N N . LYS B 1 100 ? 29.923 -5.245 5.073 1.00 29.46 ? 100 LYS B N 1 ATOM 2763 C CA . LYS B 1 100 ? 30.543 -5.534 3.783 1.00 30.02 ? 100 LYS B CA 1 ATOM 2764 C C . LYS B 1 100 ? 29.636 -6.089 2.685 1.00 28.64 ? 100 LYS B C 1 ATOM 2765 O O . LYS B 1 100 ? 29.758 -5.686 1.525 1.00 28.60 ? 100 LYS B O 1 ATOM 2766 C CB . LYS B 1 100 ? 31.751 -6.455 3.979 1.00 32.31 ? 100 LYS B CB 1 ATOM 2767 C CG . LYS B 1 100 ? 32.953 -5.753 4.593 1.00 35.18 ? 100 LYS B CG 1 ATOM 2768 C CD . LYS B 1 100 ? 34.114 -6.714 4.758 1.00 39.21 ? 100 LYS B CD 1 ATOM 2769 C CE . LYS B 1 100 ? 35.335 -6.016 5.324 1.00 41.76 ? 100 LYS B CE 1 ATOM 2770 N NZ . LYS B 1 100 ? 35.826 -4.952 4.405 1.00 44.61 ? 100 LYS B NZ 1 ATOM 2771 N N . ASN B 1 101 ? 28.732 -7.003 3.024 1.00 26.90 ? 101 ASN B N 1 ATOM 2772 C CA . ASN B 1 101 ? 27.856 -7.548 1.998 1.00 25.53 ? 101 ASN B CA 1 ATOM 2773 C C . ASN B 1 101 ? 26.539 -6.808 1.922 1.00 24.81 ? 101 ASN B C 1 ATOM 2774 O O . ASN B 1 101 ? 25.491 -7.340 2.271 1.00 25.99 ? 101 ASN B O 1 ATOM 2775 C CB . ASN B 1 101 ? 27.598 -9.039 2.220 1.00 27.48 ? 101 ASN B CB 1 ATOM 2776 C CG . ASN B 1 101 ? 28.854 -9.877 2.060 1.00 28.42 ? 101 ASN B CG 1 ATOM 2777 O OD1 . ASN B 1 101 ? 29.798 -9.488 1.369 1.00 28.19 ? 101 ASN B OD1 1 ATOM 2778 N ND2 . ASN B 1 101 ? 28.865 -11.041 2.690 1.00 31.34 ? 101 ASN B ND2 1 ATOM 2779 N N . THR B 1 102 ? 26.608 -5.568 1.456 1.00 23.62 ? 102 THR B N 1 ATOM 2780 C CA . THR B 1 102 ? 25.435 -4.723 1.302 1.00 23.21 ? 102 THR B CA 1 ATOM 2781 C C . THR B 1 102 ? 25.736 -3.711 0.205 1.00 23.94 ? 102 THR B C 1 ATOM 2782 O O . THR B 1 102 ? 26.892 -3.532 -0.181 1.00 23.26 ? 102 THR B O 1 ATOM 2783 C CB . THR B 1 102 ? 25.133 -3.914 2.587 1.00 22.99 ? 102 THR B CB 1 ATOM 2784 O OG1 . THR B 1 102 ? 26.214 -3.005 2.838 1.00 21.98 ? 102 THR B OG1 1 ATOM 2785 C CG2 . THR B 1 102 ? 24.963 -4.832 3.785 1.00 21.64 ? 102 THR B CG2 1 ATOM 2786 N N . ILE B 1 103 ? 24.689 -3.066 -0.303 1.00 24.55 ? 103 ILE B N 1 ATOM 2787 C CA . ILE B 1 103 ? 24.838 -2.013 -1.305 1.00 24.92 ? 103 ILE B CA 1 ATOM 2788 C C . ILE B 1 103 ? 25.049 -0.761 -0.438 1.00 24.81 ? 103 ILE B C 1 ATOM 2789 O O . ILE B 1 103 ? 24.106 -0.269 0.189 1.00 25.64 ? 103 ILE B O 1 ATOM 2790 C CB . ILE B 1 103 ? 23.545 -1.849 -2.146 1.00 25.76 ? 103 ILE B CB 1 ATOM 2791 C CG1 . ILE B 1 103 ? 23.240 -3.149 -2.899 1.00 25.24 ? 103 ILE B CG1 1 ATOM 2792 C CG2 . ILE B 1 103 ? 23.698 -0.687 -3.117 1.00 23.73 ? 103 ILE B CG2 1 ATOM 2793 C CD1 . ILE B 1 103 ? 21.889 -3.151 -3.598 1.00 24.87 ? 103 ILE B CD1 1 ATOM 2794 N N . LYS B 1 104 ? 26.283 -0.268 -0.385 1.00 24.07 ? 104 LYS B N 1 ATOM 2795 C CA . LYS B 1 104 ? 26.616 0.888 0.447 1.00 24.83 ? 104 LYS B CA 1 ATOM 2796 C C . LYS B 1 104 ? 26.350 2.263 -0.132 1.00 25.37 ? 104 LYS B C 1 ATOM 2797 O O . LYS B 1 104 ? 26.524 2.505 -1.326 1.00 26.07 ? 104 LYS B O 1 ATOM 2798 C CB . LYS B 1 104 ? 28.082 0.831 0.881 1.00 23.96 ? 104 LYS B CB 1 ATOM 2799 C CG . LYS B 1 104 ? 28.382 -0.241 1.899 1.00 26.25 ? 104 LYS B CG 1 ATOM 2800 C CD . LYS B 1 104 ? 29.831 -0.196 2.345 1.00 25.35 ? 104 LYS B CD 1 ATOM 2801 C CE . LYS B 1 104 ? 30.114 -1.326 3.309 1.00 25.09 ? 104 LYS B CE 1 ATOM 2802 N NZ . LYS B 1 104 ? 31.554 -1.446 3.638 1.00 26.55 ? 104 LYS B NZ 1 ATOM 2803 N N . THR B 1 105 ? 25.952 3.174 0.749 1.00 24.36 ? 105 THR B N 1 ATOM 2804 C CA . THR B 1 105 ? 25.662 4.545 0.368 1.00 24.06 ? 105 THR B CA 1 ATOM 2805 C C . THR B 1 105 ? 26.214 5.487 1.420 1.00 24.88 ? 105 THR B C 1 ATOM 2806 O O . THR B 1 105 ? 25.986 5.286 2.617 1.00 23.21 ? 105 THR B O 1 ATOM 2807 C CB . THR B 1 105 ? 24.143 4.800 0.279 1.00 24.65 ? 105 THR B CB 1 ATOM 2808 O OG1 . THR B 1 105 ? 23.570 3.954 -0.725 1.00 25.98 ? 105 THR B OG1 1 ATOM 2809 C CG2 . THR B 1 105 ? 23.863 6.255 -0.064 1.00 23.86 ? 105 THR B CG2 1 ATOM 2810 N N . ARG B 1 106 ? 26.964 6.497 0.986 1.00 24.58 ? 106 ARG B N 1 ATOM 2811 C CA . ARG B 1 106 ? 27.461 7.481 1.930 1.00 24.46 ? 106 ARG B CA 1 ATOM 2812 C C . ARG B 1 106 ? 26.481 8.645 1.813 1.00 23.98 ? 106 ARG B C 1 ATOM 2813 O O . ARG B 1 106 ? 26.367 9.267 0.750 1.00 23.85 ? 106 ARG B O 1 ATOM 2814 C CB . ARG B 1 106 ? 28.877 7.947 1.585 1.00 24.82 ? 106 ARG B CB 1 ATOM 2815 C CG . ARG B 1 106 ? 29.453 8.881 2.657 1.00 26.93 ? 106 ARG B CG 1 ATOM 2816 C CD . ARG B 1 106 ? 30.857 9.341 2.330 1.00 29.10 ? 106 ARG B CD 1 ATOM 2817 N NE . ARG B 1 106 ? 31.880 8.331 2.609 1.00 31.37 ? 106 ARG B NE 1 ATOM 2818 C CZ . ARG B 1 106 ? 32.288 7.986 3.829 1.00 31.48 ? 106 ARG B CZ 1 ATOM 2819 N NH1 . ARG B 1 106 ? 33.227 7.061 3.982 1.00 31.16 ? 106 ARG B NH1 1 ATOM 2820 N NH2 . ARG B 1 106 ? 31.758 8.564 4.897 1.00 31.60 ? 106 ARG B NH2 1 ATOM 2821 N N . LEU B 1 107 ? 25.747 8.910 2.891 1.00 21.57 ? 107 LEU B N 1 ATOM 2822 C CA . LEU B 1 107 ? 24.772 9.995 2.901 1.00 22.14 ? 107 LEU B CA 1 ATOM 2823 C C . LEU B 1 107 ? 25.453 11.341 2.662 1.00 21.77 ? 107 LEU B C 1 ATOM 2824 O O . LEU B 1 107 ? 26.634 11.523 2.982 1.00 20.99 ? 107 LEU B O 1 ATOM 2825 C CB . LEU B 1 107 ? 24.015 10.013 4.231 1.00 21.81 ? 107 LEU B CB 1 ATOM 2826 C CG . LEU B 1 107 ? 23.189 8.756 4.534 1.00 23.31 ? 107 LEU B CG 1 ATOM 2827 C CD1 . LEU B 1 107 ? 22.657 8.827 5.958 1.00 21.31 ? 107 LEU B CD1 1 ATOM 2828 C CD2 . LEU B 1 107 ? 22.038 8.630 3.533 1.00 21.56 ? 107 LEU B CD2 1 ATOM 2829 N N . HIS B 1 108 ? 24.705 12.281 2.091 1.00 22.21 ? 108 HIS B N 1 ATOM 2830 C CA . HIS B 1 108 ? 25.252 13.597 1.799 1.00 21.45 ? 108 HIS B CA 1 ATOM 2831 C C . HIS B 1 108 ? 25.370 14.470 3.041 1.00 21.59 ? 108 HIS B C 1 ATOM 2832 O O . HIS B 1 108 ? 25.992 15.532 3.008 1.00 21.33 ? 108 HIS B O 1 ATOM 2833 C CB . HIS B 1 108 ? 24.408 14.299 0.723 1.00 20.31 ? 108 HIS B CB 1 ATOM 2834 C CG . HIS B 1 108 ? 22.994 14.578 1.129 1.00 18.79 ? 108 HIS B CG 1 ATOM 2835 N ND1 . HIS B 1 108 ? 22.618 15.737 1.776 1.00 20.84 ? 108 HIS B ND1 1 ATOM 2836 C CD2 . HIS B 1 108 ? 21.857 13.864 0.948 1.00 18.05 ? 108 HIS B CD2 1 ATOM 2837 C CE1 . HIS B 1 108 ? 21.311 15.727 1.972 1.00 17.55 ? 108 HIS B CE1 1 ATOM 2838 N NE2 . HIS B 1 108 ? 20.825 14.601 1.479 1.00 19.62 ? 108 HIS B NE2 1 ATOM 2839 N N . PHE B 1 109 ? 24.788 14.008 4.143 1.00 21.70 ? 109 PHE B N 1 ATOM 2840 C CA . PHE B 1 109 ? 24.832 14.760 5.387 1.00 20.54 ? 109 PHE B CA 1 ATOM 2841 C C . PHE B 1 109 ? 25.534 13.992 6.514 1.00 20.30 ? 109 PHE B C 1 ATOM 2842 O O . PHE B 1 109 ? 25.594 12.762 6.500 1.00 20.39 ? 109 PHE B O 1 ATOM 2843 C CB . PHE B 1 109 ? 23.401 15.172 5.801 1.00 20.94 ? 109 PHE B CB 1 ATOM 2844 C CG . PHE B 1 109 ? 22.441 14.017 5.975 1.00 19.36 ? 109 PHE B CG 1 ATOM 2845 C CD1 . PHE B 1 109 ? 22.219 13.457 7.235 1.00 20.03 ? 109 PHE B CD1 1 ATOM 2846 C CD2 . PHE B 1 109 ? 21.746 13.502 4.884 1.00 19.95 ? 109 PHE B CD2 1 ATOM 2847 C CE1 . PHE B 1 109 ? 21.314 12.400 7.406 1.00 20.80 ? 109 PHE B CE1 1 ATOM 2848 C CE2 . PHE B 1 109 ? 20.838 12.445 5.036 1.00 19.65 ? 109 PHE B CE2 1 ATOM 2849 C CZ . PHE B 1 109 ? 20.620 11.892 6.301 1.00 20.22 ? 109 PHE B CZ 1 ATOM 2850 N N . GLY B 1 110 ? 26.084 14.737 7.470 1.00 19.25 ? 110 GLY B N 1 ATOM 2851 C CA . GLY B 1 110 ? 26.766 14.132 8.601 1.00 18.67 ? 110 GLY B CA 1 ATOM 2852 C C . GLY B 1 110 ? 25.814 13.865 9.753 1.00 18.31 ? 110 GLY B C 1 ATOM 2853 O O . GLY B 1 110 ? 24.617 14.125 9.641 1.00 16.94 ? 110 GLY B O 1 ATOM 2854 N N . GLY B 1 111 ? 26.348 13.363 10.866 1.00 19.21 ? 111 GLY B N 1 ATOM 2855 C CA . GLY B 1 111 ? 25.518 13.044 12.018 1.00 18.45 ? 111 GLY B CA 1 ATOM 2856 C C . GLY B 1 111 ? 25.465 14.057 13.150 1.00 18.77 ? 111 GLY B C 1 ATOM 2857 O O . GLY B 1 111 ? 24.795 13.825 14.161 1.00 18.35 ? 111 GLY B O 1 ATOM 2858 N N . SER B 1 112 ? 26.163 15.178 13.001 1.00 17.37 ? 112 SER B N 1 ATOM 2859 C CA . SER B 1 112 ? 26.144 16.199 14.038 1.00 18.38 ? 112 SER B CA 1 ATOM 2860 C C . SER B 1 112 ? 24.725 16.742 14.119 1.00 19.33 ? 112 SER B C 1 ATOM 2861 O O . SER B 1 112 ? 23.935 16.596 13.185 1.00 19.47 ? 112 SER B O 1 ATOM 2862 C CB . SER B 1 112 ? 27.105 17.342 13.701 1.00 18.10 ? 112 SER B CB 1 ATOM 2863 O OG . SER B 1 112 ? 26.679 18.032 12.541 1.00 20.29 ? 112 SER B OG 1 ATOM 2864 N N . TYR B 1 113 ? 24.395 17.378 15.231 1.00 18.44 ? 113 TYR B N 1 ATOM 2865 C CA . TYR B 1 113 ? 23.062 17.914 15.369 1.00 18.26 ? 113 TYR B CA 1 ATOM 2866 C C . TYR B 1 113 ? 22.799 19.001 14.331 1.00 18.30 ? 113 TYR B C 1 ATOM 2867 O O . TYR B 1 113 ? 21.731 19.042 13.726 1.00 17.55 ? 113 TYR B O 1 ATOM 2868 C CB . TYR B 1 113 ? 22.859 18.385 16.809 1.00 18.49 ? 113 TYR B CB 1 ATOM 2869 C CG . TYR B 1 113 ? 22.760 17.195 17.742 1.00 18.47 ? 113 TYR B CG 1 ATOM 2870 C CD1 . TYR B 1 113 ? 21.838 16.177 17.488 1.00 17.95 ? 113 TYR B CD1 1 ATOM 2871 C CD2 . TYR B 1 113 ? 23.601 17.061 18.848 1.00 16.01 ? 113 TYR B CD2 1 ATOM 2872 C CE1 . TYR B 1 113 ? 21.753 15.054 18.304 1.00 17.93 ? 113 TYR B CE1 1 ATOM 2873 C CE2 . TYR B 1 113 ? 23.522 15.934 19.677 1.00 16.66 ? 113 TYR B CE2 1 ATOM 2874 C CZ . TYR B 1 113 ? 22.593 14.938 19.393 1.00 17.80 ? 113 TYR B CZ 1 ATOM 2875 O OH . TYR B 1 113 ? 22.480 13.825 20.191 1.00 18.25 ? 113 TYR B OH 1 ATOM 2876 N N . PRO B 1 114 ? 23.770 19.893 14.099 1.00 20.35 ? 114 PRO B N 1 ATOM 2877 C CA . PRO B 1 114 ? 23.461 20.903 13.080 1.00 20.86 ? 114 PRO B CA 1 ATOM 2878 C C . PRO B 1 114 ? 23.321 20.293 11.670 1.00 20.82 ? 114 PRO B C 1 ATOM 2879 O O . PRO B 1 114 ? 22.538 20.785 10.843 1.00 18.92 ? 114 PRO B O 1 ATOM 2880 C CB . PRO B 1 114 ? 24.611 21.913 13.215 1.00 20.76 ? 114 PRO B CB 1 ATOM 2881 C CG . PRO B 1 114 ? 25.669 21.196 13.990 1.00 22.72 ? 114 PRO B CG 1 ATOM 2882 C CD . PRO B 1 114 ? 24.913 20.310 14.929 1.00 20.41 ? 114 PRO B CD 1 ATOM 2883 N N . SER B 1 115 ? 24.061 19.215 11.402 1.00 19.90 ? 115 SER B N 1 ATOM 2884 C CA . SER B 1 115 ? 23.969 18.550 10.101 1.00 19.79 ? 115 SER B CA 1 ATOM 2885 C C . SER B 1 115 ? 22.574 17.948 9.947 1.00 19.57 ? 115 SER B C 1 ATOM 2886 O O . SER B 1 115 ? 21.975 18.026 8.877 1.00 20.17 ? 115 SER B O 1 ATOM 2887 C CB . SER B 1 115 ? 25.008 17.428 9.964 1.00 19.81 ? 115 SER B CB 1 ATOM 2888 O OG . SER B 1 115 ? 26.328 17.938 9.913 1.00 22.20 ? 115 SER B OG 1 ATOM 2889 N N . LEU B 1 116 ? 22.059 17.352 11.019 1.00 17.32 ? 116 LEU B N 1 ATOM 2890 C CA . LEU B 1 116 ? 20.737 16.746 10.971 1.00 16.96 ? 116 LEU B CA 1 ATOM 2891 C C . LEU B 1 116 ? 19.640 17.802 10.839 1.00 18.13 ? 116 LEU B C 1 ATOM 2892 O O . LEU B 1 116 ? 18.596 17.537 10.237 1.00 19.11 ? 116 LEU B O 1 ATOM 2893 C CB . LEU B 1 116 ? 20.509 15.864 12.204 1.00 16.04 ? 116 LEU B CB 1 ATOM 2894 C CG . LEU B 1 116 ? 21.458 14.655 12.282 1.00 15.80 ? 116 LEU B CG 1 ATOM 2895 C CD1 . LEU B 1 116 ? 21.317 13.953 13.626 1.00 16.62 ? 116 LEU B CD1 1 ATOM 2896 C CD2 . LEU B 1 116 ? 21.163 13.693 11.150 1.00 15.29 ? 116 LEU B CD2 1 ATOM 2897 N N . GLU B 1 117 ? 19.866 18.996 11.384 1.00 17.78 ? 117 GLU B N 1 ATOM 2898 C CA . GLU B 1 117 ? 18.871 20.060 11.270 1.00 20.13 ? 117 GLU B CA 1 ATOM 2899 C C . GLU B 1 117 ? 18.788 20.502 9.808 1.00 21.34 ? 117 GLU B C 1 ATOM 2900 O O . GLU B 1 117 ? 17.743 20.964 9.337 1.00 22.12 ? 117 GLU B O 1 ATOM 2901 C CB . GLU B 1 117 ? 19.238 21.243 12.163 1.00 20.19 ? 117 GLU B CB 1 ATOM 2902 C CG . GLU B 1 117 ? 19.147 20.924 13.638 1.00 22.99 ? 117 GLU B CG 1 ATOM 2903 C CD . GLU B 1 117 ? 19.513 22.103 14.518 1.00 26.33 ? 117 GLU B CD 1 ATOM 2904 O OE1 . GLU B 1 117 ? 20.166 23.046 14.015 1.00 28.02 ? 117 GLU B OE1 1 ATOM 2905 O OE2 . GLU B 1 117 ? 19.161 22.078 15.719 1.00 26.81 ? 117 GLU B OE2 1 ATOM 2906 N N . GLY B 1 118 ? 19.900 20.346 9.096 1.00 21.57 ? 118 GLY B N 1 ATOM 2907 C CA . GLY B 1 118 ? 19.939 20.699 7.692 1.00 21.59 ? 118 GLY B CA 1 ATOM 2908 C C . GLY B 1 118 ? 18.960 19.824 6.941 1.00 22.80 ? 118 GLY B C 1 ATOM 2909 O O . GLY B 1 118 ? 18.506 20.184 5.855 1.00 24.26 ? 118 GLY B O 1 ATOM 2910 N N . GLU B 1 119 ? 18.648 18.664 7.516 1.00 21.46 ? 119 GLU B N 1 ATOM 2911 C CA . GLU B 1 119 ? 17.689 17.741 6.922 1.00 21.72 ? 119 GLU B CA 1 ATOM 2912 C C . GLU B 1 119 ? 16.380 17.845 7.680 1.00 20.49 ? 119 GLU B C 1 ATOM 2913 O O . GLU B 1 119 ? 15.581 16.915 7.690 1.00 20.99 ? 119 GLU B O 1 ATOM 2914 C CB . GLU B 1 119 ? 18.200 16.301 6.964 1.00 24.93 ? 119 GLU B CB 1 ATOM 2915 C CG . GLU B 1 119 ? 19.279 16.006 5.941 1.00 28.31 ? 119 GLU B CG 1 ATOM 2916 C CD . GLU B 1 119 ? 18.856 16.389 4.531 1.00 31.96 ? 119 GLU B CD 1 ATOM 2917 O OE1 . GLU B 1 119 ? 17.768 15.953 4.094 1.00 34.38 ? 119 GLU B OE1 1 ATOM 2918 O OE2 . GLU B 1 119 ? 19.612 17.124 3.857 1.00 32.77 ? 119 GLU B OE2 1 ATOM 2919 N N . LYS B 1 120 ? 16.194 18.986 8.333 1.00 20.01 ? 120 LYS B N 1 ATOM 2920 C CA . LYS B 1 120 ? 14.984 19.291 9.079 1.00 22.45 ? 120 LYS B CA 1 ATOM 2921 C C . LYS B 1 120 ? 14.698 18.471 10.337 1.00 22.09 ? 120 LYS B C 1 ATOM 2922 O O . LYS B 1 120 ? 13.549 18.412 10.799 1.00 20.58 ? 120 LYS B O 1 ATOM 2923 C CB . LYS B 1 120 ? 13.783 19.230 8.133 1.00 24.76 ? 120 LYS B CB 1 ATOM 2924 C CG . LYS B 1 120 ? 13.934 20.149 6.921 1.00 28.36 ? 120 LYS B CG 1 ATOM 2925 C CD . LYS B 1 120 ? 12.637 20.284 6.130 1.00 32.67 ? 120 LYS B CD 1 ATOM 2926 C CE . LYS B 1 120 ? 12.177 18.947 5.576 1.00 35.26 ? 120 LYS B CE 1 ATOM 2927 N NZ . LYS B 1 120 ? 11.019 19.091 4.643 1.00 39.62 ? 120 LYS B NZ 1 ATOM 2928 N N . ALA B 1 121 ? 15.735 17.856 10.897 1.00 20.31 ? 121 ALA B N 1 ATOM 2929 C CA . ALA B 1 121 ? 15.587 17.068 12.119 1.00 20.11 ? 121 ALA B CA 1 ATOM 2930 C C . ALA B 1 121 ? 16.140 17.873 13.309 1.00 20.69 ? 121 ALA B C 1 ATOM 2931 O O . ALA B 1 121 ? 17.358 17.989 13.484 1.00 21.23 ? 121 ALA B O 1 ATOM 2932 C CB . ALA B 1 121 ? 16.330 15.748 11.977 1.00 19.46 ? 121 ALA B CB 1 ATOM 2933 N N . TYR B 1 122 ? 15.235 18.427 14.115 1.00 19.25 ? 122 TYR B N 1 ATOM 2934 C CA . TYR B 1 122 ? 15.597 19.240 15.276 1.00 19.78 ? 122 TYR B CA 1 ATOM 2935 C C . TYR B 1 122 ? 15.283 18.516 16.579 1.00 19.88 ? 122 TYR B C 1 ATOM 2936 O O . TYR B 1 122 ? 14.221 17.900 16.715 1.00 20.16 ? 122 TYR B O 1 ATOM 2937 C CB . TYR B 1 122 ? 14.818 20.557 15.252 1.00 22.33 ? 122 TYR B CB 1 ATOM 2938 C CG . TYR B 1 122 ? 15.084 21.407 14.034 1.00 25.14 ? 122 TYR B CG 1 ATOM 2939 C CD1 . TYR B 1 122 ? 16.052 22.409 14.055 1.00 26.36 ? 122 TYR B CD1 1 ATOM 2940 C CD2 . TYR B 1 122 ? 14.385 21.189 12.847 1.00 26.92 ? 122 TYR B CD2 1 ATOM 2941 C CE1 . TYR B 1 122 ? 16.318 23.174 12.918 1.00 28.24 ? 122 TYR B CE1 1 ATOM 2942 C CE2 . TYR B 1 122 ? 14.644 21.943 11.708 1.00 27.92 ? 122 TYR B CE2 1 ATOM 2943 C CZ . TYR B 1 122 ? 15.609 22.933 11.748 1.00 28.68 ? 122 TYR B CZ 1 ATOM 2944 O OH . TYR B 1 122 ? 15.872 23.673 10.613 1.00 31.35 ? 122 TYR B OH 1 ATOM 2945 N N . ARG B 1 123 ? 16.190 18.615 17.547 1.00 18.70 ? 123 ARG B N 1 ATOM 2946 C CA . ARG B 1 123 ? 15.991 17.962 18.837 1.00 18.96 ? 123 ARG B CA 1 ATOM 2947 C C . ARG B 1 123 ? 14.746 18.449 19.573 1.00 21.14 ? 123 ARG B C 1 ATOM 2948 O O . ARG B 1 123 ? 14.018 17.655 20.160 1.00 21.16 ? 123 ARG B O 1 ATOM 2949 C CB . ARG B 1 123 ? 17.226 18.156 19.718 1.00 17.62 ? 123 ARG B CB 1 ATOM 2950 C CG . ARG B 1 123 ? 18.404 17.246 19.343 1.00 16.49 ? 123 ARG B CG 1 ATOM 2951 C CD . ARG B 1 123 ? 19.638 17.533 20.186 1.00 16.55 ? 123 ARG B CD 1 ATOM 2952 N NE . ARG B 1 123 ? 20.297 18.772 19.781 1.00 16.76 ? 123 ARG B NE 1 ATOM 2953 C CZ . ARG B 1 123 ? 21.402 19.251 20.344 1.00 18.31 ? 123 ARG B CZ 1 ATOM 2954 N NH1 . ARG B 1 123 ? 21.975 18.596 21.346 1.00 18.18 ? 123 ARG B NH1 1 ATOM 2955 N NH2 . ARG B 1 123 ? 21.942 20.380 19.902 1.00 17.77 ? 123 ARG B NH2 1 ATOM 2956 N N . GLU B 1 124 ? 14.494 19.752 19.521 1.00 24.34 ? 124 GLU B N 1 ATOM 2957 C CA . GLU B 1 124 ? 13.344 20.348 20.201 1.00 27.17 ? 124 GLU B CA 1 ATOM 2958 C C . GLU B 1 124 ? 11.994 19.878 19.680 1.00 26.00 ? 124 GLU B C 1 ATOM 2959 O O . GLU B 1 124 ? 11.005 19.911 20.409 1.00 26.68 ? 124 GLU B O 1 ATOM 2960 C CB . GLU B 1 124 ? 13.389 21.869 20.074 1.00 31.70 ? 124 GLU B CB 1 ATOM 2961 C CG . GLU B 1 124 ? 14.728 22.471 20.383 1.00 39.92 ? 124 GLU B CG 1 ATOM 2962 C CD . GLU B 1 124 ? 14.970 23.732 19.589 1.00 45.68 ? 124 GLU B CD 1 ATOM 2963 O OE1 . GLU B 1 124 ? 16.150 24.125 19.444 1.00 49.86 ? 124 GLU B OE1 1 ATOM 2964 O OE2 . GLU B 1 124 ? 13.981 24.331 19.108 1.00 49.43 ? 124 GLU B OE2 1 ATOM 2965 N N . THR B 1 125 ? 11.940 19.452 18.425 1.00 23.72 ? 125 THR B N 1 ATOM 2966 C CA . THR B 1 125 ? 10.671 19.022 17.852 1.00 23.51 ? 125 THR B CA 1 ATOM 2967 C C . THR B 1 125 ? 10.614 17.545 17.491 1.00 23.32 ? 125 THR B C 1 ATOM 2968 O O . THR B 1 125 ? 9.748 17.119 16.734 1.00 24.96 ? 125 THR B O 1 ATOM 2969 C CB . THR B 1 125 ? 10.333 19.855 16.599 1.00 22.16 ? 125 THR B CB 1 ATOM 2970 O OG1 . THR B 1 125 ? 11.386 19.732 15.635 1.00 23.26 ? 125 THR B OG1 1 ATOM 2971 C CG2 . THR B 1 125 ? 10.177 21.316 16.973 1.00 23.25 ? 125 THR B CG2 1 ATOM 2972 N N . THR B 1 126 ? 11.531 16.759 18.033 1.00 23.17 ? 126 THR B N 1 ATOM 2973 C CA . THR B 1 126 ? 11.546 15.335 17.738 1.00 22.02 ? 126 THR B CA 1 ATOM 2974 C C . THR B 1 126 ? 11.186 14.525 18.967 1.00 21.10 ? 126 THR B C 1 ATOM 2975 O O . THR B 1 126 ? 11.920 14.511 19.957 1.00 20.86 ? 126 THR B O 1 ATOM 2976 C CB . THR B 1 126 ? 12.923 14.893 17.217 1.00 22.24 ? 126 THR B CB 1 ATOM 2977 O OG1 . THR B 1 126 ? 13.134 15.458 15.914 1.00 24.00 ? 126 THR B OG1 1 ATOM 2978 C CG2 . THR B 1 126 ? 13.004 13.370 17.139 1.00 21.64 ? 126 THR B CG2 1 ATOM 2979 N N . ASP B 1 127 ? 10.041 13.857 18.898 1.00 20.22 ? 127 ASP B N 1 ATOM 2980 C CA . ASP B 1 127 ? 9.568 13.039 20.003 1.00 20.59 ? 127 ASP B CA 1 ATOM 2981 C C . ASP B 1 127 ? 10.501 11.863 20.260 1.00 19.55 ? 127 ASP B C 1 ATOM 2982 O O . ASP B 1 127 ? 11.093 11.309 19.330 1.00 17.89 ? 127 ASP B O 1 ATOM 2983 C CB . ASP B 1 127 ? 8.173 12.486 19.700 1.00 21.73 ? 127 ASP B CB 1 ATOM 2984 C CG . ASP B 1 127 ? 7.091 13.545 19.760 1.00 25.63 ? 127 ASP B CG 1 ATOM 2985 O OD1 . ASP B 1 127 ? 5.960 13.242 19.319 1.00 26.81 ? 127 ASP B OD1 1 ATOM 2986 O OD2 . ASP B 1 127 ? 7.357 14.666 20.253 1.00 25.59 ? 127 ASP B OD2 1 ATOM 2987 N N . LEU B 1 128 ? 10.623 11.494 21.532 1.00 17.54 ? 128 LEU B N 1 ATOM 2988 C CA . LEU B 1 128 ? 11.433 10.356 21.943 1.00 16.74 ? 128 LEU B CA 1 ATOM 2989 C C . LEU B 1 128 ? 10.500 9.483 22.771 1.00 15.66 ? 128 LEU B C 1 ATOM 2990 O O . LEU B 1 128 ? 9.548 9.977 23.364 1.00 15.26 ? 128 LEU B O 1 ATOM 2991 C CB . LEU B 1 128 ? 12.631 10.799 22.798 1.00 15.86 ? 128 LEU B CB 1 ATOM 2992 C CG . LEU B 1 128 ? 13.620 11.763 22.151 1.00 14.69 ? 128 LEU B CG 1 ATOM 2993 C CD1 . LEU B 1 128 ? 14.714 12.090 23.149 1.00 13.84 ? 128 LEU B CD1 1 ATOM 2994 C CD2 . LEU B 1 128 ? 14.199 11.147 20.884 1.00 11.82 ? 128 LEU B CD2 1 ATOM 2995 N N . GLY B 1 129 ? 10.783 8.188 22.807 1.00 16.77 ? 129 GLY B N 1 ATOM 2996 C CA . GLY B 1 129 ? 9.952 7.255 23.544 1.00 16.95 ? 129 GLY B CA 1 ATOM 2997 C C . GLY B 1 129 ? 9.909 5.958 22.761 1.00 18.33 ? 129 GLY B C 1 ATOM 2998 O O . GLY B 1 129 ? 10.488 5.870 21.673 1.00 17.48 ? 129 GLY B O 1 ATOM 2999 N N . ILE B 1 130 ? 9.219 4.952 23.287 1.00 18.18 ? 130 ILE B N 1 ATOM 3000 C CA . ILE B 1 130 ? 9.156 3.671 22.603 1.00 18.65 ? 130 ILE B CA 1 ATOM 3001 C C . ILE B 1 130 ? 8.416 3.710 21.259 1.00 18.96 ? 130 ILE B C 1 ATOM 3002 O O . ILE B 1 130 ? 8.857 3.078 20.295 1.00 19.61 ? 130 ILE B O 1 ATOM 3003 C CB . ILE B 1 130 ? 8.543 2.573 23.523 1.00 19.66 ? 130 ILE B CB 1 ATOM 3004 C CG1 . ILE B 1 130 ? 8.693 1.201 22.855 1.00 19.24 ? 130 ILE B CG1 1 ATOM 3005 C CG2 . ILE B 1 130 ? 7.077 2.891 23.844 1.00 18.53 ? 130 ILE B CG2 1 ATOM 3006 C CD1 . ILE B 1 130 ? 10.129 0.858 22.475 1.00 18.25 ? 130 ILE B CD1 1 ATOM 3007 N N . GLU B 1 131 ? 7.312 4.451 21.173 1.00 19.12 ? 131 GLU B N 1 ATOM 3008 C CA . GLU B 1 131 ? 6.575 4.523 19.911 1.00 20.93 ? 131 GLU B CA 1 ATOM 3009 C C . GLU B 1 131 ? 7.425 5.257 18.850 1.00 20.88 ? 131 GLU B C 1 ATOM 3010 O O . GLU B 1 131 ? 7.526 4.805 17.700 1.00 20.63 ? 131 GLU B O 1 ATOM 3011 C CB . GLU B 1 131 ? 5.211 5.194 20.129 1.00 23.27 ? 131 GLU B CB 1 ATOM 3012 C CG . GLU B 1 131 ? 4.220 5.068 18.957 1.00 28.53 ? 131 GLU B CG 1 ATOM 3013 C CD . GLU B 1 131 ? 3.978 3.625 18.493 1.00 31.17 ? 131 GLU B CD 1 ATOM 3014 O OE1 . GLU B 1 131 ? 3.877 2.716 19.350 1.00 31.75 ? 131 GLU B OE1 1 ATOM 3015 O OE2 . GLU B 1 131 ? 3.872 3.404 17.262 1.00 33.02 ? 131 GLU B OE2 1 ATOM 3016 N N . PRO B 1 132 ? 8.034 6.406 19.210 1.00 20.63 ? 132 PRO B N 1 ATOM 3017 C CA . PRO B 1 132 ? 8.852 7.069 18.186 1.00 20.16 ? 132 PRO B CA 1 ATOM 3018 C C . PRO B 1 132 ? 10.022 6.191 17.726 1.00 18.68 ? 132 PRO B C 1 ATOM 3019 O O . PRO B 1 132 ? 10.472 6.297 16.586 1.00 18.41 ? 132 PRO B O 1 ATOM 3020 C CB . PRO B 1 132 ? 9.316 8.367 18.865 1.00 21.23 ? 132 PRO B CB 1 ATOM 3021 C CG . PRO B 1 132 ? 8.813 8.283 20.291 1.00 23.55 ? 132 PRO B CG 1 ATOM 3022 C CD . PRO B 1 132 ? 7.649 7.358 20.265 1.00 20.50 ? 132 PRO B CD 1 ATOM 3023 N N . LEU B 1 133 ? 10.503 5.317 18.608 1.00 17.61 ? 133 LEU B N 1 ATOM 3024 C CA . LEU B 1 133 ? 11.597 4.412 18.263 1.00 16.34 ? 133 LEU B CA 1 ATOM 3025 C C . LEU B 1 133 ? 11.099 3.355 17.276 1.00 17.55 ? 133 LEU B C 1 ATOM 3026 O O . LEU B 1 133 ? 11.802 2.995 16.332 1.00 16.93 ? 133 LEU B O 1 ATOM 3027 C CB . LEU B 1 133 ? 12.138 3.729 19.513 1.00 16.11 ? 133 LEU B CB 1 ATOM 3028 C CG . LEU B 1 133 ? 13.282 2.743 19.272 1.00 17.94 ? 133 LEU B CG 1 ATOM 3029 C CD1 . LEU B 1 133 ? 14.403 3.424 18.485 1.00 16.53 ? 133 LEU B CD1 1 ATOM 3030 C CD2 . LEU B 1 133 ? 13.791 2.228 20.617 1.00 17.70 ? 133 LEU B CD2 1 ATOM 3031 N N . ARG B 1 134 ? 9.884 2.856 17.506 1.00 18.51 ? 134 ARG B N 1 ATOM 3032 C CA . ARG B 1 134 ? 9.277 1.856 16.622 1.00 19.09 ? 134 ARG B CA 1 ATOM 3033 C C . ARG B 1 134 ? 9.131 2.457 15.229 1.00 18.66 ? 134 ARG B C 1 ATOM 3034 O O . ARG B 1 134 ? 9.476 1.829 14.227 1.00 19.97 ? 134 ARG B O 1 ATOM 3035 C CB . ARG B 1 134 ? 7.891 1.441 17.133 1.00 17.42 ? 134 ARG B CB 1 ATOM 3036 C CG . ARG B 1 134 ? 7.915 0.577 18.374 1.00 18.65 ? 134 ARG B CG 1 ATOM 3037 C CD . ARG B 1 134 ? 6.525 0.049 18.712 1.00 20.36 ? 134 ARG B CD 1 ATOM 3038 N NE . ARG B 1 134 ? 6.544 -0.803 19.902 1.00 22.43 ? 134 ARG B NE 1 ATOM 3039 C CZ . ARG B 1 134 ? 5.965 -0.493 21.062 1.00 22.51 ? 134 ARG B CZ 1 ATOM 3040 N NH1 . ARG B 1 134 ? 5.307 0.653 21.198 1.00 21.10 ? 134 ARG B NH1 1 ATOM 3041 N NH2 . ARG B 1 134 ? 6.054 -1.324 22.093 1.00 22.41 ? 134 ARG B NH2 1 ATOM 3042 N N . ILE B 1 135 ? 8.618 3.681 15.188 1.00 18.41 ? 135 ILE B N 1 ATOM 3043 C CA . ILE B 1 135 ? 8.416 4.408 13.945 1.00 18.20 ? 135 ILE B CA 1 ATOM 3044 C C . ILE B 1 135 ? 9.735 4.719 13.256 1.00 18.63 ? 135 ILE B C 1 ATOM 3045 O O . ILE B 1 135 ? 9.827 4.637 12.035 1.00 19.86 ? 135 ILE B O 1 ATOM 3046 C CB . ILE B 1 135 ? 7.673 5.717 14.207 1.00 19.37 ? 135 ILE B CB 1 ATOM 3047 C CG1 . ILE B 1 135 ? 6.252 5.405 14.679 1.00 20.23 ? 135 ILE B CG1 1 ATOM 3048 C CG2 . ILE B 1 135 ? 7.671 6.576 12.958 1.00 20.42 ? 135 ILE B CG2 1 ATOM 3049 C CD1 . ILE B 1 135 ? 5.489 6.621 15.175 1.00 22.63 ? 135 ILE B CD1 1 ATOM 3050 N N . GLY B 1 136 ? 10.748 5.086 14.037 1.00 17.64 ? 136 GLY B N 1 ATOM 3051 C CA . GLY B 1 136 ? 12.050 5.386 13.466 1.00 16.48 ? 136 GLY B CA 1 ATOM 3052 C C . GLY B 1 136 ? 12.635 4.164 12.781 1.00 16.64 ? 136 GLY B C 1 ATOM 3053 O O . GLY B 1 136 ? 13.193 4.255 11.686 1.00 17.17 ? 136 GLY B O 1 ATOM 3054 N N . ILE B 1 137 ? 12.509 3.012 13.431 1.00 16.71 ? 137 ILE B N 1 ATOM 3055 C CA . ILE B 1 137 ? 13.011 1.761 12.875 1.00 18.68 ? 137 ILE B CA 1 ATOM 3056 C C . ILE B 1 137 ? 12.256 1.434 11.585 1.00 20.65 ? 137 ILE B C 1 ATOM 3057 O O . ILE B 1 137 ? 12.840 0.994 10.593 1.00 20.53 ? 137 ILE B O 1 ATOM 3058 C CB . ILE B 1 137 ? 12.825 0.604 13.877 1.00 19.18 ? 137 ILE B CB 1 ATOM 3059 C CG1 . ILE B 1 137 ? 13.697 0.861 15.116 1.00 18.88 ? 137 ILE B CG1 1 ATOM 3060 C CG2 . ILE B 1 137 ? 13.161 -0.728 13.204 1.00 17.53 ? 137 ILE B CG2 1 ATOM 3061 C CD1 . ILE B 1 137 ? 13.462 -0.101 16.275 1.00 18.04 ? 137 ILE B CD1 1 ATOM 3062 N N . LYS B 1 138 ? 10.949 1.659 11.616 1.00 21.39 ? 138 LYS B N 1 ATOM 3063 C CA . LYS B 1 138 ? 10.093 1.404 10.469 1.00 22.57 ? 138 LYS B CA 1 ATOM 3064 C C . LYS B 1 138 ? 10.554 2.238 9.281 1.00 21.38 ? 138 LYS B C 1 ATOM 3065 O O . LYS B 1 138 ? 10.742 1.718 8.185 1.00 22.38 ? 138 LYS B O 1 ATOM 3066 C CB . LYS B 1 138 ? 8.639 1.762 10.811 1.00 23.29 ? 138 LYS B CB 1 ATOM 3067 C CG . LYS B 1 138 ? 7.627 1.330 9.756 1.00 26.70 ? 138 LYS B CG 1 ATOM 3068 C CD . LYS B 1 138 ? 6.241 1.876 10.048 1.00 29.83 ? 138 LYS B CD 1 ATOM 3069 C CE . LYS B 1 138 ? 6.193 3.382 9.834 1.00 34.07 ? 138 LYS B CE 1 ATOM 3070 N NZ . LYS B 1 138 ? 4.847 3.967 10.112 1.00 37.28 ? 138 LYS B NZ 1 ATOM 3071 N N . LYS B 1 139 ? 10.736 3.534 9.508 1.00 20.73 ? 139 LYS B N 1 ATOM 3072 C CA . LYS B 1 139 ? 11.152 4.443 8.452 1.00 21.76 ? 139 LYS B CA 1 ATOM 3073 C C . LYS B 1 139 ? 12.538 4.147 7.894 1.00 21.50 ? 139 LYS B C 1 ATOM 3074 O O . LYS B 1 139 ? 12.780 4.339 6.699 1.00 20.89 ? 139 LYS B O 1 ATOM 3075 C CB . LYS B 1 139 ? 11.073 5.888 8.942 1.00 22.27 ? 139 LYS B CB 1 ATOM 3076 C CG . LYS B 1 139 ? 9.652 6.370 9.134 1.00 24.78 ? 139 LYS B CG 1 ATOM 3077 C CD . LYS B 1 139 ? 9.631 7.808 9.590 1.00 29.32 ? 139 LYS B CD 1 ATOM 3078 C CE . LYS B 1 139 ? 8.204 8.300 9.809 1.00 33.10 ? 139 LYS B CE 1 ATOM 3079 N NZ . LYS B 1 139 ? 8.180 9.703 10.337 1.00 36.12 ? 139 LYS B NZ 1 ATOM 3080 N N . LEU B 1 140 ? 13.449 3.684 8.742 1.00 19.47 ? 140 LEU B N 1 ATOM 3081 C CA . LEU B 1 140 ? 14.782 3.360 8.263 1.00 20.30 ? 140 LEU B CA 1 ATOM 3082 C C . LEU B 1 140 ? 14.676 2.170 7.329 1.00 21.43 ? 140 LEU B C 1 ATOM 3083 O O . LEU B 1 140 ? 15.361 2.110 6.309 1.00 22.10 ? 140 LEU B O 1 ATOM 3084 C CB . LEU B 1 140 ? 15.720 3.028 9.423 1.00 18.81 ? 140 LEU B CB 1 ATOM 3085 C CG . LEU B 1 140 ? 16.177 4.228 10.257 1.00 18.19 ? 140 LEU B CG 1 ATOM 3086 C CD1 . LEU B 1 140 ? 17.146 3.746 11.334 1.00 18.02 ? 140 LEU B CD1 1 ATOM 3087 C CD2 . LEU B 1 140 ? 16.845 5.272 9.361 1.00 16.78 ? 140 LEU B CD2 1 ATOM 3088 N N . ASP B 1 141 ? 13.803 1.230 7.675 1.00 22.57 ? 141 ASP B N 1 ATOM 3089 C CA . ASP B 1 141 ? 13.608 0.041 6.854 1.00 24.57 ? 141 ASP B CA 1 ATOM 3090 C C . ASP B 1 141 ? 12.870 0.354 5.548 1.00 25.37 ? 141 ASP B C 1 ATOM 3091 O O . ASP B 1 141 ? 13.215 -0.177 4.496 1.00 25.64 ? 141 ASP B O 1 ATOM 3092 C CB . ASP B 1 141 ? 12.853 -1.032 7.645 1.00 26.83 ? 141 ASP B CB 1 ATOM 3093 C CG . ASP B 1 141 ? 12.569 -2.276 6.813 1.00 30.10 ? 141 ASP B CG 1 ATOM 3094 O OD1 . ASP B 1 141 ? 11.439 -2.401 6.292 1.00 31.08 ? 141 ASP B OD1 1 ATOM 3095 O OD2 . ASP B 1 141 ? 13.482 -3.121 6.670 1.00 31.16 ? 141 ASP B OD2 1 ATOM 3096 N N . GLU B 1 142 ? 11.863 1.218 5.609 1.00 25.49 ? 142 GLU B N 1 ATOM 3097 C CA . GLU B 1 142 ? 11.121 1.583 4.409 1.00 27.04 ? 142 GLU B CA 1 ATOM 3098 C C . GLU B 1 142 ? 12.003 2.334 3.409 1.00 27.50 ? 142 GLU B C 1 ATOM 3099 O O . GLU B 1 142 ? 11.801 2.243 2.195 1.00 27.52 ? 142 GLU B O 1 ATOM 3100 C CB . GLU B 1 142 ? 9.918 2.450 4.774 1.00 29.75 ? 142 GLU B CB 1 ATOM 3101 C CG . GLU B 1 142 ? 8.788 1.700 5.453 1.00 33.39 ? 142 GLU B CG 1 ATOM 3102 C CD . GLU B 1 142 ? 7.670 2.625 5.899 1.00 36.78 ? 142 GLU B CD 1 ATOM 3103 O OE1 . GLU B 1 142 ? 6.624 2.111 6.355 1.00 39.50 ? 142 GLU B OE1 1 ATOM 3104 O OE2 . GLU B 1 142 ? 7.838 3.864 5.802 1.00 37.36 ? 142 GLU B OE2 1 ATOM 3105 N N . ASN B 1 143 ? 12.977 3.084 3.920 1.00 26.82 ? 143 ASN B N 1 ATOM 3106 C CA . ASN B 1 143 ? 13.883 3.843 3.063 1.00 25.70 ? 143 ASN B CA 1 ATOM 3107 C C . ASN B 1 143 ? 15.133 3.067 2.653 1.00 25.58 ? 143 ASN B C 1 ATOM 3108 O O . ASN B 1 143 ? 16.127 3.655 2.218 1.00 25.27 ? 143 ASN B O 1 ATOM 3109 C CB . ASN B 1 143 ? 14.270 5.152 3.743 1.00 24.52 ? 143 ASN B CB 1 ATOM 3110 C CG . ASN B 1 143 ? 13.182 6.190 3.642 1.00 23.97 ? 143 ASN B CG 1 ATOM 3111 O OD1 . ASN B 1 143 ? 13.052 6.867 2.624 1.00 24.04 ? 143 ASN B OD1 1 ATOM 3112 N ND2 . ASN B 1 143 ? 12.376 6.310 4.691 1.00 22.26 ? 143 ASN B ND2 1 ATOM 3113 N N . ALA B 1 144 ? 15.083 1.747 2.811 1.00 25.88 ? 144 ALA B N 1 ATOM 3114 C CA . ALA B 1 144 ? 16.186 0.884 2.403 1.00 28.23 ? 144 ALA B CA 1 ATOM 3115 C C . ALA B 1 144 ? 15.908 0.688 0.918 1.00 30.85 ? 144 ALA B C 1 ATOM 3116 O O . ALA B 1 144 ? 15.627 -0.420 0.454 1.00 31.04 ? 144 ALA B O 1 ATOM 3117 C CB . ALA B 1 144 ? 16.125 -0.451 3.135 1.00 27.98 ? 144 ALA B CB 1 ATOM 3118 N N . ILE B 1 145 ? 15.958 1.797 0.188 1.00 32.42 ? 145 ILE B N 1 ATOM 3119 C CA . ILE B 1 145 ? 15.692 1.809 -1.240 1.00 33.86 ? 145 ILE B CA 1 ATOM 3120 C C . ILE B 1 145 ? 16.595 2.847 -1.906 1.00 36.33 ? 145 ILE B C 1 ATOM 3121 O O . ILE B 1 145 ? 17.225 3.655 -1.224 1.00 36.57 ? 145 ILE B O 1 ATOM 3122 C CB . ILE B 1 145 ? 14.216 2.170 -1.501 1.00 32.93 ? 145 ILE B CB 1 ATOM 3123 C CG1 . ILE B 1 145 ? 13.890 3.514 -0.845 1.00 32.00 ? 145 ILE B CG1 1 ATOM 3124 C CG2 . ILE B 1 145 ? 13.308 1.085 -0.938 1.00 31.97 ? 145 ILE B CG2 1 ATOM 3125 C CD1 . ILE B 1 145 ? 12.446 3.941 -0.991 1.00 31.32 ? 145 ILE B CD1 1 ATOM 3126 N N . ASP B 1 146 ? 16.653 2.825 -3.234 1.00 37.76 ? 146 ASP B N 1 ATOM 3127 C CA . ASP B 1 146 ? 17.484 3.762 -3.981 1.00 38.83 ? 146 ASP B CA 1 ATOM 3128 C C . ASP B 1 146 ? 17.005 5.201 -3.847 1.00 37.15 ? 146 ASP B C 1 ATOM 3129 O O . ASP B 1 146 ? 17.807 6.116 -3.651 1.00 35.85 ? 146 ASP B O 1 ATOM 3130 C CB . ASP B 1 146 ? 17.506 3.371 -5.459 1.00 44.07 ? 146 ASP B CB 1 ATOM 3131 C CG . ASP B 1 146 ? 18.092 1.993 -5.682 1.00 49.58 ? 146 ASP B CG 1 ATOM 3132 O OD1 . ASP B 1 146 ? 19.319 1.827 -5.480 1.00 52.36 ? 146 ASP B OD1 1 ATOM 3133 O OD2 . ASP B 1 146 ? 17.322 1.074 -6.049 1.00 52.82 ? 146 ASP B OD2 1 ATOM 3134 N N . ASN B 1 147 ? 15.697 5.402 -3.962 1.00 35.56 ? 147 ASN B N 1 ATOM 3135 C CA . ASN B 1 147 ? 15.134 6.741 -3.858 1.00 35.85 ? 147 ASN B CA 1 ATOM 3136 C C . ASN B 1 147 ? 14.678 7.006 -2.420 1.00 34.42 ? 147 ASN B C 1 ATOM 3137 O O . ASN B 1 147 ? 13.510 7.319 -2.170 1.00 34.66 ? 147 ASN B O 1 ATOM 3138 C CB . ASN B 1 147 ? 13.956 6.895 -4.830 1.00 37.87 ? 147 ASN B CB 1 ATOM 3139 C CG . ASN B 1 147 ? 13.632 8.353 -5.132 1.00 41.06 ? 147 ASN B CG 1 ATOM 3140 O OD1 . ASN B 1 147 ? 12.700 8.655 -5.885 1.00 44.34 ? 147 ASN B OD1 1 ATOM 3141 N ND2 . ASN B 1 147 ? 14.407 9.266 -4.552 1.00 42.57 ? 147 ASN B ND2 1 ATOM 3142 N N . TYR B 1 148 ? 15.612 6.875 -1.481 1.00 31.92 ? 148 TYR B N 1 ATOM 3143 C CA . TYR B 1 148 ? 15.333 7.093 -0.066 1.00 29.05 ? 148 TYR B CA 1 ATOM 3144 C C . TYR B 1 148 ? 15.077 8.567 0.217 1.00 27.37 ? 148 TYR B C 1 ATOM 3145 O O . TYR B 1 148 ? 15.571 9.435 -0.500 1.00 25.53 ? 148 TYR B O 1 ATOM 3146 C CB . TYR B 1 148 ? 16.517 6.599 0.781 1.00 29.42 ? 148 TYR B CB 1 ATOM 3147 C CG . TYR B 1 148 ? 17.851 7.252 0.446 1.00 29.24 ? 148 TYR B CG 1 ATOM 3148 C CD1 . TYR B 1 148 ? 18.141 8.562 0.850 1.00 27.79 ? 148 TYR B CD1 1 ATOM 3149 C CD2 . TYR B 1 148 ? 18.811 6.571 -0.310 1.00 28.14 ? 148 TYR B CD2 1 ATOM 3150 C CE1 . TYR B 1 148 ? 19.350 9.174 0.506 1.00 26.34 ? 148 TYR B CE1 1 ATOM 3151 C CE2 . TYR B 1 148 ? 20.022 7.176 -0.661 1.00 25.88 ? 148 TYR B CE2 1 ATOM 3152 C CZ . TYR B 1 148 ? 20.282 8.472 -0.251 1.00 26.63 ? 148 TYR B CZ 1 ATOM 3153 O OH . TYR B 1 148 ? 21.473 9.065 -0.608 1.00 27.96 ? 148 TYR B OH 1 ATOM 3154 N N . LYS B 1 149 ? 14.296 8.847 1.257 1.00 26.11 ? 149 LYS B N 1 ATOM 3155 C CA . LYS B 1 149 ? 14.013 10.225 1.635 1.00 26.43 ? 149 LYS B CA 1 ATOM 3156 C C . LYS B 1 149 ? 14.963 10.594 2.772 1.00 26.24 ? 149 LYS B C 1 ATOM 3157 O O . LYS B 1 149 ? 14.826 10.105 3.896 1.00 25.02 ? 149 LYS B O 1 ATOM 3158 C CB . LYS B 1 149 ? 12.561 10.381 2.097 1.00 27.98 ? 149 LYS B CB 1 ATOM 3159 C CG . LYS B 1 149 ? 11.531 9.922 1.077 1.00 32.31 ? 149 LYS B CG 1 ATOM 3160 C CD . LYS B 1 149 ? 10.118 10.379 1.436 1.00 36.69 ? 149 LYS B CD 1 ATOM 3161 C CE . LYS B 1 149 ? 9.874 11.840 1.045 1.00 40.42 ? 149 LYS B CE 1 ATOM 3162 N NZ . LYS B 1 149 ? 10.874 12.799 1.625 1.00 44.17 ? 149 LYS B NZ 1 ATOM 3163 N N . PRO B 1 150 ? 15.946 11.459 2.490 1.00 25.61 ? 150 PRO B N 1 ATOM 3164 C CA . PRO B 1 150 ? 16.916 11.883 3.499 1.00 24.98 ? 150 PRO B CA 1 ATOM 3165 C C . PRO B 1 150 ? 16.302 12.493 4.752 1.00 24.11 ? 150 PRO B C 1 ATOM 3166 O O . PRO B 1 150 ? 16.840 12.336 5.843 1.00 24.10 ? 150 PRO B O 1 ATOM 3167 C CB . PRO B 1 150 ? 17.800 12.870 2.736 1.00 25.58 ? 150 PRO B CB 1 ATOM 3168 C CG . PRO B 1 150 ? 16.885 13.413 1.696 1.00 26.11 ? 150 PRO B CG 1 ATOM 3169 C CD . PRO B 1 150 ? 16.174 12.175 1.224 1.00 25.73 ? 150 PRO B CD 1 ATOM 3170 N N . THR B 1 151 ? 15.178 13.182 4.610 1.00 23.20 ? 151 THR B N 1 ATOM 3171 C CA . THR B 1 151 ? 14.557 13.790 5.776 1.00 23.17 ? 151 THR B CA 1 ATOM 3172 C C . THR B 1 151 ? 14.019 12.730 6.743 1.00 22.22 ? 151 THR B C 1 ATOM 3173 O O . THR B 1 151 ? 14.083 12.904 7.963 1.00 21.61 ? 151 THR B O 1 ATOM 3174 C CB . THR B 1 151 ? 13.416 14.779 5.380 1.00 22.97 ? 151 THR B CB 1 ATOM 3175 O OG1 . THR B 1 151 ? 12.394 14.092 4.649 1.00 24.91 ? 151 THR B OG1 1 ATOM 3176 C CG2 . THR B 1 151 ? 13.972 15.911 4.539 1.00 22.43 ? 151 THR B CG2 1 ATOM 3177 N N . GLU B 1 152 ? 13.505 11.628 6.201 1.00 21.34 ? 152 GLU B N 1 ATOM 3178 C CA . GLU B 1 152 ? 12.970 10.557 7.037 1.00 21.63 ? 152 GLU B CA 1 ATOM 3179 C C . GLU B 1 152 ? 14.089 9.778 7.720 1.00 20.12 ? 152 GLU B C 1 ATOM 3180 O O . GLU B 1 152 ? 13.937 9.324 8.852 1.00 19.63 ? 152 GLU B O 1 ATOM 3181 C CB . GLU B 1 152 ? 12.094 9.611 6.210 1.00 21.81 ? 152 GLU B CB 1 ATOM 3182 C CG . GLU B 1 152 ? 10.740 10.201 5.854 1.00 24.86 ? 152 GLU B CG 1 ATOM 3183 C CD . GLU B 1 152 ? 9.823 9.213 5.153 1.00 27.23 ? 152 GLU B CD 1 ATOM 3184 O OE1 . GLU B 1 152 ? 8.665 9.585 4.856 1.00 30.48 ? 152 GLU B OE1 1 ATOM 3185 O OE2 . GLU B 1 152 ? 10.251 8.068 4.899 1.00 27.22 ? 152 GLU B OE2 1 ATOM 3186 N N . ILE B 1 153 ? 15.212 9.625 7.031 1.00 18.75 ? 153 ILE B N 1 ATOM 3187 C CA . ILE B 1 153 ? 16.348 8.923 7.607 1.00 17.74 ? 153 ILE B CA 1 ATOM 3188 C C . ILE B 1 153 ? 16.919 9.791 8.720 1.00 17.31 ? 153 ILE B C 1 ATOM 3189 O O . ILE B 1 153 ? 17.208 9.304 9.814 1.00 17.34 ? 153 ILE B O 1 ATOM 3190 C CB . ILE B 1 153 ? 17.438 8.661 6.552 1.00 18.62 ? 153 ILE B CB 1 ATOM 3191 C CG1 . ILE B 1 153 ? 16.937 7.604 5.559 1.00 18.03 ? 153 ILE B CG1 1 ATOM 3192 C CG2 . ILE B 1 153 ? 18.746 8.229 7.237 1.00 18.58 ? 153 ILE B CG2 1 ATOM 3193 C CD1 . ILE B 1 153 ? 17.899 7.281 4.436 1.00 17.74 ? 153 ILE B CD1 1 ATOM 3194 N N . ALA B 1 154 ? 17.064 11.082 8.441 1.00 15.19 ? 154 ALA B N 1 ATOM 3195 C CA . ALA B 1 154 ? 17.603 12.017 9.421 1.00 15.59 ? 154 ALA B CA 1 ATOM 3196 C C . ALA B 1 154 ? 16.763 12.028 10.697 1.00 16.62 ? 154 ALA B C 1 ATOM 3197 O O . ALA B 1 154 ? 17.287 11.940 11.809 1.00 16.13 ? 154 ALA B O 1 ATOM 3198 C CB . ALA B 1 154 ? 17.663 13.413 8.823 1.00 16.22 ? 154 ALA B CB 1 ATOM 3199 N N . SER B 1 155 ? 15.454 12.141 10.527 1.00 16.88 ? 155 SER B N 1 ATOM 3200 C CA . SER B 1 155 ? 14.536 12.165 11.653 1.00 17.91 ? 155 SER B CA 1 ATOM 3201 C C . SER B 1 155 ? 14.641 10.876 12.472 1.00 17.73 ? 155 SER B C 1 ATOM 3202 O O . SER B 1 155 ? 14.706 10.910 13.702 1.00 19.50 ? 155 SER B O 1 ATOM 3203 C CB . SER B 1 155 ? 13.102 12.345 11.144 1.00 18.70 ? 155 SER B CB 1 ATOM 3204 O OG . SER B 1 155 ? 12.192 12.351 12.225 1.00 25.20 ? 155 SER B OG 1 ATOM 3205 N N . SER B 1 156 ? 14.657 9.737 11.788 1.00 17.75 ? 156 SER B N 1 ATOM 3206 C CA . SER B 1 156 ? 14.753 8.451 12.465 1.00 18.42 ? 156 SER B CA 1 ATOM 3207 C C . SER B 1 156 ? 16.086 8.269 13.199 1.00 18.30 ? 156 SER B C 1 ATOM 3208 O O . SER B 1 156 ? 16.123 7.753 14.319 1.00 18.18 ? 156 SER B O 1 ATOM 3209 C CB . SER B 1 156 ? 14.544 7.316 11.460 1.00 19.12 ? 156 SER B CB 1 ATOM 3210 O OG . SER B 1 156 ? 13.232 7.369 10.923 1.00 19.77 ? 156 SER B OG 1 ATOM 3211 N N . LEU B 1 157 ? 17.179 8.693 12.576 1.00 16.92 ? 157 LEU B N 1 ATOM 3212 C CA . LEU B 1 157 ? 18.477 8.561 13.217 1.00 15.61 ? 157 LEU B CA 1 ATOM 3213 C C . LEU B 1 157 ? 18.592 9.492 14.424 1.00 16.32 ? 157 LEU B C 1 ATOM 3214 O O . LEU B 1 157 ? 19.284 9.168 15.393 1.00 16.75 ? 157 LEU B O 1 ATOM 3215 C CB . LEU B 1 157 ? 19.597 8.847 12.215 1.00 15.14 ? 157 LEU B CB 1 ATOM 3216 C CG . LEU B 1 157 ? 19.815 7.760 11.158 1.00 15.12 ? 157 LEU B CG 1 ATOM 3217 C CD1 . LEU B 1 157 ? 20.993 8.149 10.284 1.00 15.37 ? 157 LEU B CD1 1 ATOM 3218 C CD2 . LEU B 1 157 ? 20.068 6.409 11.821 1.00 13.29 ? 157 LEU B CD2 1 ATOM 3219 N N . LEU B 1 158 ? 17.927 10.647 14.378 1.00 14.96 ? 158 LEU B N 1 ATOM 3220 C CA . LEU B 1 158 ? 17.984 11.568 15.513 1.00 15.33 ? 158 LEU B CA 1 ATOM 3221 C C . LEU B 1 158 ? 17.352 10.893 16.740 1.00 15.41 ? 158 LEU B C 1 ATOM 3222 O O . LEU B 1 158 ? 17.836 11.047 17.862 1.00 15.20 ? 158 LEU B O 1 ATOM 3223 C CB . LEU B 1 158 ? 17.260 12.883 15.194 1.00 15.15 ? 158 LEU B CB 1 ATOM 3224 C CG . LEU B 1 158 ? 17.270 13.951 16.302 1.00 15.72 ? 158 LEU B CG 1 ATOM 3225 C CD1 . LEU B 1 158 ? 18.702 14.183 16.805 1.00 15.68 ? 158 LEU B CD1 1 ATOM 3226 C CD2 . LEU B 1 158 ? 16.677 15.246 15.765 1.00 14.62 ? 158 LEU B CD2 1 ATOM 3227 N N . VAL B 1 159 ? 16.274 10.143 16.518 1.00 14.59 ? 159 VAL B N 1 ATOM 3228 C CA . VAL B 1 159 ? 15.613 9.426 17.603 1.00 14.16 ? 159 VAL B CA 1 ATOM 3229 C C . VAL B 1 159 ? 16.569 8.353 18.128 1.00 15.28 ? 159 VAL B C 1 ATOM 3230 O O . VAL B 1 159 ? 16.751 8.202 19.337 1.00 15.41 ? 159 VAL B O 1 ATOM 3231 C CB . VAL B 1 159 ? 14.311 8.744 17.113 1.00 13.87 ? 159 VAL B CB 1 ATOM 3232 C CG1 . VAL B 1 159 ? 13.732 7.846 18.214 1.00 13.43 ? 159 VAL B CG1 1 ATOM 3233 C CG2 . VAL B 1 159 ? 13.296 9.804 16.712 1.00 13.58 ? 159 VAL B CG2 1 ATOM 3234 N N . VAL B 1 160 ? 17.179 7.609 17.210 1.00 14.37 ? 160 VAL B N 1 ATOM 3235 C CA . VAL B 1 160 ? 18.118 6.554 17.573 1.00 14.63 ? 160 VAL B CA 1 ATOM 3236 C C . VAL B 1 160 ? 19.331 7.121 18.321 1.00 14.24 ? 160 VAL B C 1 ATOM 3237 O O . VAL B 1 160 ? 19.754 6.584 19.348 1.00 12.62 ? 160 VAL B O 1 ATOM 3238 C CB . VAL B 1 160 ? 18.587 5.796 16.303 1.00 14.96 ? 160 VAL B CB 1 ATOM 3239 C CG1 . VAL B 1 160 ? 19.729 4.848 16.641 1.00 15.30 ? 160 VAL B CG1 1 ATOM 3240 C CG2 . VAL B 1 160 ? 17.414 5.019 15.714 1.00 14.38 ? 160 VAL B CG2 1 ATOM 3241 N N . ILE B 1 161 ? 19.882 8.215 17.808 1.00 13.88 ? 161 ILE B N 1 ATOM 3242 C CA . ILE B 1 161 ? 21.041 8.842 18.431 1.00 15.22 ? 161 ILE B CA 1 ATOM 3243 C C . ILE B 1 161 ? 20.789 9.247 19.887 1.00 15.12 ? 161 ILE B C 1 ATOM 3244 O O . ILE B 1 161 ? 21.641 9.053 20.751 1.00 14.34 ? 161 ILE B O 1 ATOM 3245 C CB . ILE B 1 161 ? 21.500 10.079 17.611 1.00 15.21 ? 161 ILE B CB 1 ATOM 3246 C CG1 . ILE B 1 161 ? 22.199 9.600 16.327 1.00 15.21 ? 161 ILE B CG1 1 ATOM 3247 C CG2 . ILE B 1 161 ? 22.402 10.982 18.465 1.00 14.34 ? 161 ILE B CG2 1 ATOM 3248 C CD1 . ILE B 1 161 ? 22.430 10.690 15.293 1.00 14.35 ? 161 ILE B CD1 1 ATOM 3249 N N . GLN B 1 162 ? 19.619 9.793 20.174 1.00 15.12 ? 162 GLN B N 1 ATOM 3250 C CA . GLN B 1 162 ? 19.356 10.201 21.546 1.00 16.35 ? 162 GLN B CA 1 ATOM 3251 C C . GLN B 1 162 ? 18.933 9.076 22.474 1.00 14.67 ? 162 GLN B C 1 ATOM 3252 O O . GLN B 1 162 ? 19.325 9.058 23.639 1.00 14.82 ? 162 GLN B O 1 ATOM 3253 C CB . GLN B 1 162 ? 18.333 11.324 21.561 1.00 17.45 ? 162 GLN B CB 1 ATOM 3254 C CG . GLN B 1 162 ? 18.933 12.595 21.019 1.00 21.66 ? 162 GLN B CG 1 ATOM 3255 C CD . GLN B 1 162 ? 17.953 13.707 20.977 1.00 24.09 ? 162 GLN B CD 1 ATOM 3256 O OE1 . GLN B 1 162 ? 17.060 13.730 20.129 1.00 27.68 ? 162 GLN B OE1 1 ATOM 3257 N NE2 . GLN B 1 162 ? 18.091 14.645 21.900 1.00 23.48 ? 162 GLN B NE2 1 ATOM 3258 N N . MET B 1 163 ? 18.159 8.125 21.964 1.00 14.03 ? 163 MET B N 1 ATOM 3259 C CA . MET B 1 163 ? 17.704 7.019 22.801 1.00 13.64 ? 163 MET B CA 1 ATOM 3260 C C . MET B 1 163 ? 18.757 5.948 22.992 1.00 13.64 ? 163 MET B C 1 ATOM 3261 O O . MET B 1 163 ? 18.654 5.130 23.910 1.00 14.05 ? 163 MET B O 1 ATOM 3262 C CB . MET B 1 163 ? 16.430 6.400 22.229 1.00 14.33 ? 163 MET B CB 1 ATOM 3263 C CG . MET B 1 163 ? 15.228 7.326 22.315 1.00 14.57 ? 163 MET B CG 1 ATOM 3264 S SD . MET B 1 163 ? 13.706 6.500 21.839 1.00 15.45 ? 163 MET B SD 1 ATOM 3265 C CE . MET B 1 163 ? 13.438 5.441 23.253 1.00 12.70 ? 163 MET B CE 1 ATOM 3266 N N . VAL B 1 164 ? 19.768 5.946 22.130 1.00 13.75 ? 164 VAL B N 1 ATOM 3267 C CA . VAL B 1 164 ? 20.849 4.975 22.245 1.00 13.86 ? 164 VAL B CA 1 ATOM 3268 C C . VAL B 1 164 ? 22.157 5.657 22.639 1.00 14.46 ? 164 VAL B C 1 ATOM 3269 O O . VAL B 1 164 ? 22.665 5.431 23.734 1.00 16.29 ? 164 VAL B O 1 ATOM 3270 C CB . VAL B 1 164 ? 21.057 4.203 20.935 1.00 14.32 ? 164 VAL B CB 1 ATOM 3271 C CG1 . VAL B 1 164 ? 22.238 3.233 21.078 1.00 15.17 ? 164 VAL B CG1 1 ATOM 3272 C CG2 . VAL B 1 164 ? 19.780 3.451 20.584 1.00 13.34 ? 164 VAL B CG2 1 ATOM 3273 N N . SER B 1 165 ? 22.686 6.509 21.764 1.00 14.11 ? 165 SER B N 1 ATOM 3274 C CA . SER B 1 165 ? 23.945 7.203 22.039 1.00 13.94 ? 165 SER B CA 1 ATOM 3275 C C . SER B 1 165 ? 23.955 8.113 23.273 1.00 13.73 ? 165 SER B C 1 ATOM 3276 O O . SER B 1 165 ? 24.755 7.910 24.188 1.00 13.71 ? 165 SER B O 1 ATOM 3277 C CB . SER B 1 165 ? 24.373 8.030 20.820 1.00 14.73 ? 165 SER B CB 1 ATOM 3278 O OG . SER B 1 165 ? 24.571 7.205 19.687 1.00 16.82 ? 165 SER B OG 1 ATOM 3279 N N . GLU B 1 166 ? 23.084 9.117 23.302 1.00 12.36 ? 166 GLU B N 1 ATOM 3280 C CA . GLU B 1 166 ? 23.073 10.046 24.425 1.00 12.99 ? 166 GLU B CA 1 ATOM 3281 C C . GLU B 1 166 ? 22.618 9.382 25.714 1.00 12.60 ? 166 GLU B C 1 ATOM 3282 O O . GLU B 1 166 ? 23.160 9.668 26.780 1.00 13.27 ? 166 GLU B O 1 ATOM 3283 C CB . GLU B 1 166 ? 22.203 11.271 24.110 1.00 12.50 ? 166 GLU B CB 1 ATOM 3284 C CG . GLU B 1 166 ? 22.620 12.036 22.844 1.00 14.73 ? 166 GLU B CG 1 ATOM 3285 C CD . GLU B 1 166 ? 23.955 12.769 22.964 1.00 13.57 ? 166 GLU B CD 1 ATOM 3286 O OE1 . GLU B 1 166 ? 24.650 12.619 23.989 1.00 14.03 ? 166 GLU B OE1 1 ATOM 3287 O OE2 . GLU B 1 166 ? 24.308 13.503 22.013 1.00 13.90 ? 166 GLU B OE2 1 ATOM 3288 N N . ALA B 1 167 ? 21.629 8.497 25.624 1.00 12.23 ? 167 ALA B N 1 ATOM 3289 C CA . ALA B 1 167 ? 21.153 7.789 26.811 1.00 11.94 ? 167 ALA B CA 1 ATOM 3290 C C . ALA B 1 167 ? 22.276 6.910 27.395 1.00 12.68 ? 167 ALA B C 1 ATOM 3291 O O . ALA B 1 167 ? 22.409 6.783 28.610 1.00 13.15 ? 167 ALA B O 1 ATOM 3292 C CB . ALA B 1 167 ? 19.947 6.933 26.464 1.00 10.13 ? 167 ALA B CB 1 ATOM 3293 N N . ALA B 1 168 ? 23.079 6.300 26.526 1.00 13.10 ? 168 ALA B N 1 ATOM 3294 C CA . ALA B 1 168 ? 24.179 5.453 26.985 1.00 12.52 ? 168 ALA B CA 1 ATOM 3295 C C . ALA B 1 168 ? 25.229 6.317 27.687 1.00 13.21 ? 168 ALA B C 1 ATOM 3296 O O . ALA B 1 168 ? 25.827 5.899 28.681 1.00 12.47 ? 168 ALA B O 1 ATOM 3297 C CB . ALA B 1 168 ? 24.803 4.715 25.804 1.00 12.67 ? 168 ALA B CB 1 ATOM 3298 N N . ARG B 1 169 ? 25.437 7.528 27.176 1.00 11.70 ? 169 ARG B N 1 ATOM 3299 C CA . ARG B 1 169 ? 26.417 8.449 27.754 1.00 11.94 ? 169 ARG B CA 1 ATOM 3300 C C . ARG B 1 169 ? 26.002 9.053 29.092 1.00 12.25 ? 169 ARG B C 1 ATOM 3301 O O . ARG B 1 169 ? 26.822 9.170 30.001 1.00 12.86 ? 169 ARG B O 1 ATOM 3302 C CB . ARG B 1 169 ? 26.688 9.620 26.808 1.00 11.22 ? 169 ARG B CB 1 ATOM 3303 C CG . ARG B 1 169 ? 27.384 9.282 25.511 1.00 10.85 ? 169 ARG B CG 1 ATOM 3304 C CD . ARG B 1 169 ? 27.275 10.493 24.621 1.00 12.82 ? 169 ARG B CD 1 ATOM 3305 N NE . ARG B 1 169 ? 27.955 10.336 23.348 1.00 15.83 ? 169 ARG B NE 1 ATOM 3306 C CZ . ARG B 1 169 ? 27.979 11.281 22.419 1.00 18.23 ? 169 ARG B CZ 1 ATOM 3307 N NH1 . ARG B 1 169 ? 27.355 12.431 22.638 1.00 19.18 ? 169 ARG B NH1 1 ATOM 3308 N NH2 . ARG B 1 169 ? 28.638 11.088 21.285 1.00 21.24 ? 169 ARG B NH2 1 ATOM 3309 N N . PHE B 1 170 ? 24.731 9.438 29.198 1.00 11.92 ? 170 PHE B N 1 ATOM 3310 C CA . PHE B 1 170 ? 24.204 10.108 30.381 1.00 11.07 ? 170 PHE B CA 1 ATOM 3311 C C . PHE B 1 170 ? 23.101 9.362 31.109 1.00 12.35 ? 170 PHE B C 1 ATOM 3312 O O . PHE B 1 170 ? 22.056 9.080 30.522 1.00 12.73 ? 170 PHE B O 1 ATOM 3313 C CB . PHE B 1 170 ? 23.640 11.476 29.978 1.00 11.16 ? 170 PHE B CB 1 ATOM 3314 C CG . PHE B 1 170 ? 24.670 12.441 29.460 1.00 13.86 ? 170 PHE B CG 1 ATOM 3315 C CD1 . PHE B 1 170 ? 25.426 13.212 30.342 1.00 13.17 ? 170 PHE B CD1 1 ATOM 3316 C CD2 . PHE B 1 170 ? 24.884 12.582 28.088 1.00 13.21 ? 170 PHE B CD2 1 ATOM 3317 C CE1 . PHE B 1 170 ? 26.381 14.113 29.866 1.00 14.67 ? 170 PHE B CE1 1 ATOM 3318 C CE2 . PHE B 1 170 ? 25.838 13.480 27.599 1.00 13.96 ? 170 PHE B CE2 1 ATOM 3319 C CZ . PHE B 1 170 ? 26.587 14.246 28.487 1.00 14.66 ? 170 PHE B CZ 1 ATOM 3320 N N . THR B 1 171 ? 23.317 9.063 32.389 1.00 13.25 ? 171 THR B N 1 ATOM 3321 C CA . THR B 1 171 ? 22.281 8.399 33.183 1.00 13.26 ? 171 THR B CA 1 ATOM 3322 C C . THR B 1 171 ? 21.102 9.367 33.273 1.00 13.18 ? 171 THR B C 1 ATOM 3323 O O . THR B 1 171 ? 19.954 8.953 33.388 1.00 13.40 ? 171 THR B O 1 ATOM 3324 C CB . THR B 1 171 ? 22.754 8.085 34.619 1.00 14.35 ? 171 THR B CB 1 ATOM 3325 O OG1 . THR B 1 171 ? 23.284 9.274 35.213 1.00 16.00 ? 171 THR B OG1 1 ATOM 3326 C CG2 . THR B 1 171 ? 23.824 7.004 34.615 1.00 14.58 ? 171 THR B CG2 1 ATOM 3327 N N . PHE B 1 172 ? 21.393 10.664 33.208 1.00 13.11 ? 172 PHE B N 1 ATOM 3328 C CA . PHE B 1 172 ? 20.349 11.682 33.274 1.00 14.78 ? 172 PHE B CA 1 ATOM 3329 C C . PHE B 1 172 ? 19.368 11.561 32.103 1.00 14.38 ? 172 PHE B C 1 ATOM 3330 O O . PHE B 1 172 ? 18.152 11.621 32.288 1.00 15.20 ? 172 PHE B O 1 ATOM 3331 C CB . PHE B 1 172 ? 20.965 13.080 33.264 1.00 17.02 ? 172 PHE B CB 1 ATOM 3332 C CG . PHE B 1 172 ? 19.948 14.182 33.358 1.00 20.63 ? 172 PHE B CG 1 ATOM 3333 C CD1 . PHE B 1 172 ? 19.375 14.517 34.586 1.00 21.52 ? 172 PHE B CD1 1 ATOM 3334 C CD2 . PHE B 1 172 ? 19.540 14.870 32.213 1.00 20.96 ? 172 PHE B CD2 1 ATOM 3335 C CE1 . PHE B 1 172 ? 18.406 15.526 34.673 1.00 22.41 ? 172 PHE B CE1 1 ATOM 3336 C CE2 . PHE B 1 172 ? 18.574 15.879 32.288 1.00 22.29 ? 172 PHE B CE2 1 ATOM 3337 C CZ . PHE B 1 172 ? 18.006 16.207 33.520 1.00 22.10 ? 172 PHE B CZ 1 ATOM 3338 N N . ILE B 1 173 ? 19.900 11.391 30.899 1.00 13.67 ? 173 ILE B N 1 ATOM 3339 C CA . ILE B 1 173 ? 19.069 11.265 29.708 1.00 13.74 ? 173 ILE B CA 1 ATOM 3340 C C . ILE B 1 173 ? 18.388 9.898 29.703 1.00 14.18 ? 173 ILE B C 1 ATOM 3341 O O . ILE B 1 173 ? 17.230 9.770 29.304 1.00 13.52 ? 173 ILE B O 1 ATOM 3342 C CB . ILE B 1 173 ? 19.924 11.505 28.433 1.00 13.71 ? 173 ILE B CB 1 ATOM 3343 C CG1 . ILE B 1 173 ? 20.434 12.956 28.464 1.00 12.86 ? 173 ILE B CG1 1 ATOM 3344 C CG2 . ILE B 1 173 ? 19.115 11.210 27.167 1.00 11.87 ? 173 ILE B CG2 1 ATOM 3345 C CD1 . ILE B 1 173 ? 21.225 13.392 27.258 1.00 12.66 ? 173 ILE B CD1 1 ATOM 3346 N N . GLU B 1 174 ? 19.104 8.884 30.176 1.00 14.12 ? 174 GLU B N 1 ATOM 3347 C CA . GLU B 1 174 ? 18.560 7.531 30.284 1.00 14.08 ? 174 GLU B CA 1 ATOM 3348 C C . GLU B 1 174 ? 17.294 7.571 31.144 1.00 14.25 ? 174 GLU B C 1 ATOM 3349 O O . GLU B 1 174 ? 16.266 7.004 30.790 1.00 13.96 ? 174 GLU B O 1 ATOM 3350 C CB . GLU B 1 174 ? 19.588 6.613 30.959 1.00 13.97 ? 174 GLU B CB 1 ATOM 3351 C CG . GLU B 1 174 ? 19.026 5.302 31.515 1.00 15.64 ? 174 GLU B CG 1 ATOM 3352 C CD . GLU B 1 174 ? 19.988 4.594 32.489 1.00 18.46 ? 174 GLU B CD 1 ATOM 3353 O OE1 . GLU B 1 174 ? 21.153 5.029 32.648 1.00 17.77 ? 174 GLU B OE1 1 ATOM 3354 O OE2 . GLU B 1 174 ? 19.573 3.587 33.099 1.00 20.72 ? 174 GLU B OE2 1 ATOM 3355 N N . ASN B 1 175 ? 17.373 8.255 32.280 1.00 14.25 ? 175 ASN B N 1 ATOM 3356 C CA . ASN B 1 175 ? 16.235 8.322 33.186 1.00 16.24 ? 175 ASN B CA 1 ATOM 3357 C C . ASN B 1 175 ? 15.088 9.209 32.732 1.00 18.21 ? 175 ASN B C 1 ATOM 3358 O O . ASN B 1 175 ? 13.942 9.005 33.143 1.00 18.40 ? 175 ASN B O 1 ATOM 3359 C CB . ASN B 1 175 ? 16.710 8.696 34.588 1.00 15.26 ? 175 ASN B CB 1 ATOM 3360 C CG . ASN B 1 175 ? 17.462 7.556 35.245 1.00 15.92 ? 175 ASN B CG 1 ATOM 3361 O OD1 . ASN B 1 175 ? 17.026 6.408 35.178 1.00 17.25 ? 175 ASN B OD1 1 ATOM 3362 N ND2 . ASN B 1 175 ? 18.588 7.858 35.874 1.00 15.35 ? 175 ASN B ND2 1 ATOM 3363 N N . GLN B 1 176 ? 15.380 10.189 31.886 1.00 17.95 ? 176 GLN B N 1 ATOM 3364 C CA . GLN B 1 176 ? 14.319 11.038 31.371 1.00 18.99 ? 176 GLN B CA 1 ATOM 3365 C C . GLN B 1 176 ? 13.462 10.177 30.456 1.00 18.21 ? 176 GLN B C 1 ATOM 3366 O O . GLN B 1 176 ? 12.249 10.363 30.349 1.00 19.30 ? 176 GLN B O 1 ATOM 3367 C CB . GLN B 1 176 ? 14.904 12.214 30.596 1.00 22.02 ? 176 GLN B CB 1 ATOM 3368 C CG . GLN B 1 176 ? 15.337 13.356 31.479 1.00 26.19 ? 176 GLN B CG 1 ATOM 3369 C CD . GLN B 1 176 ? 15.916 14.489 30.679 1.00 32.80 ? 176 GLN B CD 1 ATOM 3370 O OE1 . GLN B 1 176 ? 15.855 15.650 31.089 1.00 36.78 ? 176 GLN B OE1 1 ATOM 3371 N NE2 . GLN B 1 176 ? 16.495 14.163 29.526 1.00 33.88 ? 176 GLN B NE2 1 ATOM 3372 N N . ILE B 1 177 ? 14.104 9.216 29.802 1.00 17.73 ? 177 ILE B N 1 ATOM 3373 C CA . ILE B 1 177 ? 13.396 8.307 28.901 1.00 17.79 ? 177 ILE B CA 1 ATOM 3374 C C . ILE B 1 177 ? 12.753 7.178 29.707 1.00 16.80 ? 177 ILE B C 1 ATOM 3375 O O . ILE B 1 177 ? 11.606 6.804 29.457 1.00 15.81 ? 177 ILE B O 1 ATOM 3376 C CB . ILE B 1 177 ? 14.363 7.717 27.827 1.00 17.11 ? 177 ILE B CB 1 ATOM 3377 C CG1 . ILE B 1 177 ? 14.774 8.827 26.851 1.00 17.02 ? 177 ILE B CG1 1 ATOM 3378 C CG2 . ILE B 1 177 ? 13.699 6.566 27.071 1.00 16.68 ? 177 ILE B CG2 1 ATOM 3379 C CD1 . ILE B 1 177 ? 15.972 8.491 26.004 1.00 16.39 ? 177 ILE B CD1 1 ATOM 3380 N N . ARG B 1 178 ? 13.488 6.657 30.689 1.00 16.37 ? 178 ARG B N 1 ATOM 3381 C CA . ARG B 1 178 ? 12.983 5.568 31.528 1.00 15.27 ? 178 ARG B CA 1 ATOM 3382 C C . ARG B 1 178 ? 11.600 5.895 32.091 1.00 14.22 ? 178 ARG B C 1 ATOM 3383 O O . ARG B 1 178 ? 10.659 5.117 31.928 1.00 14.83 ? 178 ARG B O 1 ATOM 3384 C CB . ARG B 1 178 ? 13.962 5.289 32.681 1.00 15.30 ? 178 ARG B CB 1 ATOM 3385 C CG . ARG B 1 178 ? 13.516 4.201 33.663 1.00 15.08 ? 178 ARG B CG 1 ATOM 3386 C CD . ARG B 1 178 ? 14.391 4.174 34.934 1.00 16.02 ? 178 ARG B CD 1 ATOM 3387 N NE . ARG B 1 178 ? 13.950 3.146 35.885 1.00 17.62 ? 178 ARG B NE 1 ATOM 3388 C CZ . ARG B 1 178 ? 14.698 2.127 36.316 1.00 17.08 ? 178 ARG B CZ 1 ATOM 3389 N NH1 . ARG B 1 178 ? 15.951 1.972 35.901 1.00 14.51 ? 178 ARG B NH1 1 ATOM 3390 N NH2 . ARG B 1 178 ? 14.180 1.242 37.156 1.00 17.08 ? 178 ARG B NH2 1 ATOM 3391 N N . ASN B 1 179 ? 11.471 7.053 32.736 1.00 13.54 ? 179 ASN B N 1 ATOM 3392 C CA . ASN B 1 179 ? 10.196 7.442 33.334 1.00 14.03 ? 179 ASN B CA 1 ATOM 3393 C C . ASN B 1 179 ? 9.184 8.097 32.401 1.00 13.99 ? 179 ASN B C 1 ATOM 3394 O O . ASN B 1 179 ? 8.180 8.644 32.854 1.00 15.24 ? 179 ASN B O 1 ATOM 3395 C CB . ASN B 1 179 ? 10.436 8.331 34.555 1.00 14.91 ? 179 ASN B CB 1 ATOM 3396 C CG . ASN B 1 179 ? 11.019 7.558 35.727 1.00 16.37 ? 179 ASN B CG 1 ATOM 3397 O OD1 . ASN B 1 179 ? 10.742 6.369 35.900 1.00 15.96 ? 179 ASN B OD1 1 ATOM 3398 N ND2 . ASN B 1 179 ? 11.815 8.232 36.547 1.00 16.29 ? 179 ASN B ND2 1 ATOM 3399 N N . ASN B 1 180 ? 9.451 8.032 31.102 1.00 14.22 ? 180 ASN B N 1 ATOM 3400 C CA . ASN B 1 180 ? 8.549 8.575 30.076 1.00 16.50 ? 180 ASN B CA 1 ATOM 3401 C C . ASN B 1 180 ? 8.517 7.571 28.919 1.00 16.94 ? 180 ASN B C 1 ATOM 3402 O O . ASN B 1 180 ? 8.072 7.890 27.814 1.00 17.00 ? 180 ASN B O 1 ATOM 3403 C CB . ASN B 1 180 ? 9.071 9.916 29.529 1.00 16.92 ? 180 ASN B CB 1 ATOM 3404 C CG . ASN B 1 180 ? 8.882 11.068 30.497 1.00 18.16 ? 180 ASN B CG 1 ATOM 3405 O OD1 . ASN B 1 180 ? 7.758 11.388 30.881 1.00 17.06 ? 180 ASN B OD1 1 ATOM 3406 N ND2 . ASN B 1 180 ? 9.985 11.707 30.886 1.00 15.14 ? 180 ASN B ND2 1 ATOM 3407 N N . PHE B 1 181 ? 8.991 6.358 29.185 1.00 17.99 ? 181 PHE B N 1 ATOM 3408 C CA . PHE B 1 181 ? 9.092 5.324 28.160 1.00 17.98 ? 181 PHE B CA 1 ATOM 3409 C C . PHE B 1 181 ? 7.862 5.095 27.288 1.00 18.92 ? 181 PHE B C 1 ATOM 3410 O O . PHE B 1 181 ? 7.990 4.988 26.066 1.00 18.31 ? 181 PHE B O 1 ATOM 3411 C CB . PHE B 1 181 ? 9.516 4.000 28.789 1.00 17.67 ? 181 PHE B CB 1 ATOM 3412 C CG . PHE B 1 181 ? 10.031 2.996 27.794 1.00 18.31 ? 181 PHE B CG 1 ATOM 3413 C CD1 . PHE B 1 181 ? 11.222 3.229 27.106 1.00 18.88 ? 181 PHE B CD1 1 ATOM 3414 C CD2 . PHE B 1 181 ? 9.339 1.810 27.556 1.00 18.11 ? 181 PHE B CD2 1 ATOM 3415 C CE1 . PHE B 1 181 ? 11.718 2.293 26.200 1.00 16.97 ? 181 PHE B CE1 1 ATOM 3416 C CE2 . PHE B 1 181 ? 9.828 0.866 26.650 1.00 17.07 ? 181 PHE B CE2 1 ATOM 3417 C CZ . PHE B 1 181 ? 11.018 1.109 25.973 1.00 17.58 ? 181 PHE B CZ 1 ATOM 3418 N N . GLN B 1 182 ? 6.683 5.012 27.900 1.00 18.91 ? 182 GLN B N 1 ATOM 3419 C CA . GLN B 1 182 ? 5.456 4.778 27.140 1.00 21.15 ? 182 GLN B CA 1 ATOM 3420 C C . GLN B 1 182 ? 4.806 6.072 26.657 1.00 23.59 ? 182 GLN B C 1 ATOM 3421 O O . GLN B 1 182 ? 3.664 6.067 26.197 1.00 25.32 ? 182 GLN B O 1 ATOM 3422 C CB . GLN B 1 182 ? 4.441 3.996 27.979 1.00 19.49 ? 182 GLN B CB 1 ATOM 3423 C CG . GLN B 1 182 ? 4.874 2.591 28.396 1.00 20.47 ? 182 GLN B CG 1 ATOM 3424 C CD . GLN B 1 182 ? 5.137 1.659 27.221 1.00 23.75 ? 182 GLN B CD 1 ATOM 3425 O OE1 . GLN B 1 182 ? 4.453 1.718 26.196 1.00 25.14 ? 182 GLN B OE1 1 ATOM 3426 N NE2 . GLN B 1 182 ? 6.121 0.775 27.376 1.00 23.14 ? 182 GLN B NE2 1 ATOM 3427 N N . GLN B 1 183 ? 5.530 7.180 26.760 1.00 24.69 ? 183 GLN B N 1 ATOM 3428 C CA . GLN B 1 183 ? 5.009 8.469 26.325 1.00 25.17 ? 183 GLN B CA 1 ATOM 3429 C C . GLN B 1 183 ? 5.891 9.036 25.221 1.00 26.14 ? 183 GLN B C 1 ATOM 3430 O O . GLN B 1 183 ? 6.856 8.403 24.791 1.00 25.71 ? 183 GLN B O 1 ATOM 3431 C CB . GLN B 1 183 ? 4.983 9.442 27.499 1.00 26.03 ? 183 GLN B CB 1 ATOM 3432 C CG . GLN B 1 183 ? 4.325 8.883 28.744 1.00 29.96 ? 183 GLN B CG 1 ATOM 3433 C CD . GLN B 1 183 ? 4.617 9.726 29.973 1.00 32.99 ? 183 GLN B CD 1 ATOM 3434 O OE1 . GLN B 1 183 ? 4.272 10.909 30.021 1.00 35.48 ? 183 GLN B OE1 1 ATOM 3435 N NE2 . GLN B 1 183 ? 5.261 9.122 30.974 1.00 31.82 ? 183 GLN B NE2 1 ATOM 3436 N N . ARG B 1 184 ? 5.544 10.231 24.760 1.00 26.48 ? 184 ARG B N 1 ATOM 3437 C CA . ARG B 1 184 ? 6.296 10.912 23.716 1.00 27.11 ? 184 ARG B CA 1 ATOM 3438 C C . ARG B 1 184 ? 6.813 12.217 24.306 1.00 28.38 ? 184 ARG B C 1 ATOM 3439 O O . ARG B 1 184 ? 6.043 13.145 24.546 1.00 31.14 ? 184 ARG B O 1 ATOM 3440 C CB . ARG B 1 184 ? 5.389 11.211 22.523 1.00 27.99 ? 184 ARG B CB 1 ATOM 3441 C CG . ARG B 1 184 ? 5.003 9.996 21.705 1.00 30.51 ? 184 ARG B CG 1 ATOM 3442 C CD . ARG B 1 184 ? 3.867 10.341 20.767 1.00 34.70 ? 184 ARG B CD 1 ATOM 3443 N NE . ARG B 1 184 ? 3.663 9.336 19.729 1.00 39.48 ? 184 ARG B NE 1 ATOM 3444 C CZ . ARG B 1 184 ? 4.335 9.300 18.580 1.00 43.24 ? 184 ARG B CZ 1 ATOM 3445 N NH1 . ARG B 1 184 ? 5.264 10.216 18.315 1.00 43.81 ? 184 ARG B NH1 1 ATOM 3446 N NH2 . ARG B 1 184 ? 4.069 8.354 17.686 1.00 45.27 ? 184 ARG B NH2 1 ATOM 3447 N N . ILE B 1 185 ? 8.112 12.294 24.551 1.00 26.80 ? 185 ILE B N 1 ATOM 3448 C CA . ILE B 1 185 ? 8.677 13.503 25.125 1.00 26.43 ? 185 ILE B CA 1 ATOM 3449 C C . ILE B 1 185 ? 9.739 14.092 24.217 1.00 25.51 ? 185 ILE B C 1 ATOM 3450 O O . ILE B 1 185 ? 10.379 13.383 23.446 1.00 26.65 ? 185 ILE B O 1 ATOM 3451 C CB . ILE B 1 185 ? 9.326 13.222 26.485 1.00 26.89 ? 185 ILE B CB 1 ATOM 3452 C CG1 . ILE B 1 185 ? 10.487 12.239 26.294 1.00 29.14 ? 185 ILE B CG1 1 ATOM 3453 C CG2 . ILE B 1 185 ? 8.278 12.676 27.452 1.00 27.68 ? 185 ILE B CG2 1 ATOM 3454 C CD1 . ILE B 1 185 ? 11.376 12.062 27.494 1.00 28.79 ? 185 ILE B CD1 1 ATOM 3455 N N . ARG B 1 186 ? 9.915 15.400 24.313 1.00 24.88 ? 186 ARG B N 1 ATOM 3456 C CA . ARG B 1 186 ? 10.918 16.092 23.528 1.00 24.16 ? 186 ARG B CA 1 ATOM 3457 C C . ARG B 1 186 ? 11.961 16.582 24.505 1.00 24.06 ? 186 ARG B C 1 ATOM 3458 O O . ARG B 1 186 ? 11.626 17.028 25.598 1.00 25.21 ? 186 ARG B O 1 ATOM 3459 C CB . ARG B 1 186 ? 10.285 17.264 22.788 1.00 22.98 ? 186 ARG B CB 1 ATOM 3460 C CG . ARG B 1 186 ? 9.278 16.785 21.797 1.00 23.61 ? 186 ARG B CG 1 ATOM 3461 C CD . ARG B 1 186 ? 8.642 17.892 21.016 1.00 24.24 ? 186 ARG B CD 1 ATOM 3462 N NE . ARG B 1 186 ? 7.859 17.315 19.933 1.00 25.30 ? 186 ARG B NE 1 ATOM 3463 C CZ . ARG B 1 186 ? 7.249 18.019 18.990 1.00 26.47 ? 186 ARG B CZ 1 ATOM 3464 N NH1 . ARG B 1 186 ? 7.325 19.342 18.995 1.00 26.15 ? 186 ARG B NH1 1 ATOM 3465 N NH2 . ARG B 1 186 ? 6.582 17.394 18.031 1.00 27.26 ? 186 ARG B NH2 1 ATOM 3466 N N . PRO B 1 187 ? 13.245 16.479 24.146 1.00 23.84 ? 187 PRO B N 1 ATOM 3467 C CA . PRO B 1 187 ? 14.270 16.950 25.080 1.00 24.09 ? 187 PRO B CA 1 ATOM 3468 C C . PRO B 1 187 ? 14.117 18.431 25.438 1.00 24.33 ? 187 PRO B C 1 ATOM 3469 O O . PRO B 1 187 ? 13.701 19.245 24.606 1.00 24.23 ? 187 PRO B O 1 ATOM 3470 C CB . PRO B 1 187 ? 15.576 16.645 24.347 1.00 23.88 ? 187 PRO B CB 1 ATOM 3471 C CG . PRO B 1 187 ? 15.172 16.614 22.901 1.00 24.39 ? 187 PRO B CG 1 ATOM 3472 C CD . PRO B 1 187 ? 13.850 15.907 22.935 1.00 22.48 ? 187 PRO B CD 1 ATOM 3473 N N . ALA B 1 188 ? 14.439 18.759 26.688 1.00 23.71 ? 188 ALA B N 1 ATOM 3474 C CA . ALA B 1 188 ? 14.359 20.127 27.187 1.00 23.83 ? 188 ALA B CA 1 ATOM 3475 C C . ALA B 1 188 ? 15.739 20.778 27.143 1.00 23.86 ? 188 ALA B C 1 ATOM 3476 O O . ALA B 1 188 ? 16.703 20.172 26.674 1.00 23.09 ? 188 ALA B O 1 ATOM 3477 C CB . ALA B 1 188 ? 13.825 20.131 28.609 1.00 24.84 ? 188 ALA B CB 1 ATOM 3478 N N . ASN B 1 189 ? 15.839 22.005 27.641 1.00 23.62 ? 189 ASN B N 1 ATOM 3479 C CA . ASN B 1 189 ? 17.113 22.713 27.623 1.00 24.24 ? 189 ASN B CA 1 ATOM 3480 C C . ASN B 1 189 ? 18.204 22.021 28.426 1.00 22.46 ? 189 ASN B C 1 ATOM 3481 O O . ASN B 1 189 ? 19.386 22.184 28.130 1.00 22.04 ? 189 ASN B O 1 ATOM 3482 C CB . ASN B 1 189 ? 16.935 24.157 28.113 1.00 27.25 ? 189 ASN B CB 1 ATOM 3483 C CG . ASN B 1 189 ? 16.135 25.011 27.137 1.00 30.36 ? 189 ASN B CG 1 ATOM 3484 O OD1 . ASN B 1 189 ? 16.550 25.217 25.998 1.00 28.81 ? 189 ASN B OD1 1 ATOM 3485 N ND2 . ASN B 1 189 ? 14.982 25.491 27.594 1.00 36.23 ? 189 ASN B ND2 1 ATOM 3486 N N . ASN B 1 190 ? 17.821 21.251 29.440 1.00 21.18 ? 190 ASN B N 1 ATOM 3487 C CA . ASN B 1 190 ? 18.820 20.551 30.244 1.00 20.29 ? 190 ASN B CA 1 ATOM 3488 C C . ASN B 1 190 ? 19.426 19.389 29.457 1.00 18.55 ? 190 ASN B C 1 ATOM 3489 O O . ASN B 1 190 ? 20.647 19.252 29.369 1.00 17.08 ? 190 ASN B O 1 ATOM 3490 C CB . ASN B 1 190 ? 18.209 20.052 31.563 1.00 21.36 ? 190 ASN B CB 1 ATOM 3491 C CG . ASN B 1 190 ? 16.830 19.438 31.388 1.00 23.07 ? 190 ASN B CG 1 ATOM 3492 O OD1 . ASN B 1 190 ? 16.393 19.150 30.270 1.00 25.70 ? 190 ASN B OD1 1 ATOM 3493 N ND2 . ASN B 1 190 ? 16.141 19.222 32.504 1.00 23.14 ? 190 ASN B ND2 1 ATOM 3494 N N . THR B 1 191 ? 18.562 18.566 28.873 1.00 17.62 ? 191 THR B N 1 ATOM 3495 C CA . THR B 1 191 ? 18.999 17.430 28.070 1.00 17.81 ? 191 THR B CA 1 ATOM 3496 C C . THR B 1 191 ? 19.878 17.906 26.920 1.00 17.56 ? 191 THR B C 1 ATOM 3497 O O . THR B 1 191 ? 20.965 17.382 26.688 1.00 17.54 ? 191 THR B O 1 ATOM 3498 C CB . THR B 1 191 ? 17.796 16.698 27.471 1.00 18.39 ? 191 THR B CB 1 ATOM 3499 O OG1 . THR B 1 191 ? 16.925 16.292 28.529 1.00 21.39 ? 191 THR B OG1 1 ATOM 3500 C CG2 . THR B 1 191 ? 18.245 15.473 26.673 1.00 17.41 ? 191 THR B CG2 1 ATOM 3501 N N . ILE B 1 192 ? 19.406 18.911 26.196 1.00 16.81 ? 192 ILE B N 1 ATOM 3502 C CA . ILE B 1 192 ? 20.160 19.424 25.064 1.00 17.10 ? 192 ILE B CA 1 ATOM 3503 C C . ILE B 1 192 ? 21.515 20.023 25.450 1.00 16.73 ? 192 ILE B C 1 ATOM 3504 O O . ILE B 1 192 ? 22.502 19.815 24.742 1.00 17.17 ? 192 ILE B O 1 ATOM 3505 C CB . ILE B 1 192 ? 19.314 20.455 24.274 1.00 17.02 ? 192 ILE B CB 1 ATOM 3506 C CG1 . ILE B 1 192 ? 18.112 19.745 23.643 1.00 17.48 ? 192 ILE B CG1 1 ATOM 3507 C CG2 . ILE B 1 192 ? 20.154 21.119 23.198 1.00 16.84 ? 192 ILE B CG2 1 ATOM 3508 C CD1 . ILE B 1 192 ? 17.163 20.659 22.897 1.00 18.11 ? 192 ILE B CD1 1 ATOM 3509 N N . SER B 1 193 ? 21.579 20.748 26.566 1.00 17.67 ? 193 SER B N 1 ATOM 3510 C CA . SER B 1 193 ? 22.852 21.352 26.981 1.00 18.73 ? 193 SER B CA 1 ATOM 3511 C C . SER B 1 193 ? 23.837 20.259 27.389 1.00 18.60 ? 193 SER B C 1 ATOM 3512 O O . SER B 1 193 ? 25.038 20.363 27.121 1.00 17.93 ? 193 SER B O 1 ATOM 3513 C CB . SER B 1 193 ? 22.649 22.370 28.126 1.00 18.25 ? 193 SER B CB 1 ATOM 3514 O OG . SER B 1 193 ? 22.301 21.757 29.354 1.00 20.43 ? 193 SER B OG 1 ATOM 3515 N N . LEU B 1 194 ? 23.325 19.205 28.023 1.00 18.26 ? 194 LEU B N 1 ATOM 3516 C CA . LEU B 1 194 ? 24.167 18.083 28.429 1.00 17.12 ? 194 LEU B CA 1 ATOM 3517 C C . LEU B 1 194 ? 24.794 17.437 27.207 1.00 15.77 ? 194 LEU B C 1 ATOM 3518 O O . LEU B 1 194 ? 25.999 17.190 27.176 1.00 16.18 ? 194 LEU B O 1 ATOM 3519 C CB . LEU B 1 194 ? 23.349 17.033 29.177 1.00 18.13 ? 194 LEU B CB 1 ATOM 3520 C CG . LEU B 1 194 ? 23.230 17.241 30.680 1.00 20.99 ? 194 LEU B CG 1 ATOM 3521 C CD1 . LEU B 1 194 ? 22.355 16.144 31.262 1.00 21.39 ? 194 LEU B CD1 1 ATOM 3522 C CD2 . LEU B 1 194 ? 24.630 17.223 31.317 1.00 20.47 ? 194 LEU B CD2 1 ATOM 3523 N N . GLU B 1 195 ? 23.965 17.159 26.204 1.00 15.85 ? 195 GLU B N 1 ATOM 3524 C CA . GLU B 1 195 ? 24.431 16.535 24.967 1.00 15.72 ? 195 GLU B CA 1 ATOM 3525 C C . GLU B 1 195 ? 25.509 17.396 24.331 1.00 15.63 ? 195 GLU B C 1 ATOM 3526 O O . GLU B 1 195 ? 26.529 16.889 23.878 1.00 15.57 ? 195 GLU B O 1 ATOM 3527 C CB . GLU B 1 195 ? 23.273 16.355 23.981 1.00 16.33 ? 195 GLU B CB 1 ATOM 3528 C CG . GLU B 1 195 ? 22.126 15.515 24.520 1.00 18.67 ? 195 GLU B CG 1 ATOM 3529 C CD . GLU B 1 195 ? 20.960 15.404 23.553 1.00 20.21 ? 195 GLU B CD 1 ATOM 3530 O OE1 . GLU B 1 195 ? 20.700 16.375 22.806 1.00 21.65 ? 195 GLU B OE1 1 ATOM 3531 O OE2 . GLU B 1 195 ? 20.284 14.352 23.555 1.00 19.80 ? 195 GLU B OE2 1 ATOM 3532 N N . ASN B 1 196 ? 25.280 18.704 24.314 1.00 15.91 ? 196 ASN B N 1 ATOM 3533 C CA . ASN B 1 196 ? 26.233 19.632 23.727 1.00 16.90 ? 196 ASN B CA 1 ATOM 3534 C C . ASN B 1 196 ? 27.566 19.670 24.474 1.00 16.74 ? 196 ASN B C 1 ATOM 3535 O O . ASN B 1 196 ? 28.619 19.800 23.853 1.00 18.30 ? 196 ASN B O 1 ATOM 3536 C CB . ASN B 1 196 ? 25.653 21.053 23.696 1.00 18.57 ? 196 ASN B CB 1 ATOM 3537 C CG . ASN B 1 196 ? 24.455 21.190 22.768 1.00 17.50 ? 196 ASN B CG 1 ATOM 3538 O OD1 . ASN B 1 196 ? 24.242 20.376 21.870 1.00 18.00 ? 196 ASN B OD1 1 ATOM 3539 N ND2 . ASN B 1 196 ? 23.679 22.244 22.973 1.00 18.43 ? 196 ASN B ND2 1 ATOM 3540 N N . LYS B 1 197 ? 27.518 19.542 25.798 1.00 16.10 ? 197 LYS B N 1 ATOM 3541 C CA . LYS B 1 197 ? 28.721 19.620 26.624 1.00 16.22 ? 197 LYS B CA 1 ATOM 3542 C C . LYS B 1 197 ? 29.393 18.321 27.049 1.00 16.77 ? 197 LYS B C 1 ATOM 3543 O O . LYS B 1 197 ? 30.242 18.344 27.942 1.00 17.09 ? 197 LYS B O 1 ATOM 3544 C CB . LYS B 1 197 ? 28.419 20.422 27.889 1.00 17.25 ? 197 LYS B CB 1 ATOM 3545 C CG . LYS B 1 197 ? 27.859 21.807 27.638 1.00 19.84 ? 197 LYS B CG 1 ATOM 3546 C CD . LYS B 1 197 ? 28.831 22.660 26.846 1.00 22.63 ? 197 LYS B CD 1 ATOM 3547 C CE . LYS B 1 197 ? 28.303 24.077 26.689 1.00 25.63 ? 197 LYS B CE 1 ATOM 3548 N NZ . LYS B 1 197 ? 29.180 24.875 25.799 1.00 28.56 ? 197 LYS B NZ 1 ATOM 3549 N N . TRP B 1 198 ? 29.043 17.197 26.432 1.00 15.17 ? 198 TRP B N 1 ATOM 3550 C CA . TRP B 1 198 ? 29.659 15.935 26.830 1.00 15.33 ? 198 TRP B CA 1 ATOM 3551 C C . TRP B 1 198 ? 31.184 15.965 26.698 1.00 16.10 ? 198 TRP B C 1 ATOM 3552 O O . TRP B 1 198 ? 31.905 15.555 27.615 1.00 14.63 ? 198 TRP B O 1 ATOM 3553 C CB . TRP B 1 198 ? 29.096 14.773 26.006 1.00 13.92 ? 198 TRP B CB 1 ATOM 3554 C CG . TRP B 1 198 ? 29.610 13.425 26.442 1.00 12.84 ? 198 TRP B CG 1 ATOM 3555 C CD1 . TRP B 1 198 ? 29.532 12.876 27.698 1.00 12.37 ? 198 TRP B CD1 1 ATOM 3556 C CD2 . TRP B 1 198 ? 30.240 12.437 25.613 1.00 12.98 ? 198 TRP B CD2 1 ATOM 3557 N NE1 . TRP B 1 198 ? 30.069 11.605 27.698 1.00 12.31 ? 198 TRP B NE1 1 ATOM 3558 C CE2 . TRP B 1 198 ? 30.511 11.311 26.432 1.00 12.74 ? 198 TRP B CE2 1 ATOM 3559 C CE3 . TRP B 1 198 ? 30.599 12.392 24.257 1.00 12.33 ? 198 TRP B CE3 1 ATOM 3560 C CZ2 . TRP B 1 198 ? 31.126 10.148 25.934 1.00 13.94 ? 198 TRP B CZ2 1 ATOM 3561 C CZ3 . TRP B 1 198 ? 31.211 11.232 23.760 1.00 13.50 ? 198 TRP B CZ3 1 ATOM 3562 C CH2 . TRP B 1 198 ? 31.467 10.127 24.600 1.00 12.22 ? 198 TRP B CH2 1 ATOM 3563 N N . GLY B 1 199 ? 31.669 16.451 25.558 1.00 16.67 ? 199 GLY B N 1 ATOM 3564 C CA . GLY B 1 199 ? 33.103 16.519 25.330 1.00 17.95 ? 199 GLY B CA 1 ATOM 3565 C C . GLY B 1 199 ? 33.812 17.417 26.327 1.00 19.15 ? 199 GLY B C 1 ATOM 3566 O O . GLY B 1 199 ? 34.840 17.034 26.891 1.00 19.85 ? 199 GLY B O 1 ATOM 3567 N N . LYS B 1 200 ? 33.265 18.610 26.552 1.00 20.02 ? 200 LYS B N 1 ATOM 3568 C CA . LYS B 1 200 ? 33.860 19.555 27.491 1.00 21.23 ? 200 LYS B CA 1 ATOM 3569 C C . LYS B 1 200 ? 33.848 19.021 28.920 1.00 20.42 ? 200 LYS B C 1 ATOM 3570 O O . LYS B 1 200 ? 34.835 19.145 29.642 1.00 20.65 ? 200 LYS B O 1 ATOM 3571 C CB . LYS B 1 200 ? 33.126 20.895 27.437 1.00 24.05 ? 200 LYS B CB 1 ATOM 3572 C CG . LYS B 1 200 ? 33.350 21.658 26.143 1.00 28.67 ? 200 LYS B CG 1 ATOM 3573 C CD . LYS B 1 200 ? 32.955 23.119 26.301 1.00 33.95 ? 200 LYS B CD 1 ATOM 3574 C CE . LYS B 1 200 ? 33.254 23.934 25.044 1.00 36.08 ? 200 LYS B CE 1 ATOM 3575 N NZ . LYS B 1 200 ? 32.404 23.514 23.892 1.00 40.18 ? 200 LYS B NZ 1 ATOM 3576 N N . LEU B 1 201 ? 32.727 18.438 29.333 1.00 18.28 ? 201 LEU B N 1 ATOM 3577 C CA . LEU B 1 201 ? 32.630 17.879 30.675 1.00 17.34 ? 201 LEU B CA 1 ATOM 3578 C C . LEU B 1 201 ? 33.639 16.748 30.812 1.00 17.26 ? 201 LEU B C 1 ATOM 3579 O O . LEU B 1 201 ? 34.322 16.634 31.829 1.00 17.90 ? 201 LEU B O 1 ATOM 3580 C CB . LEU B 1 201 ? 31.222 17.336 30.930 1.00 17.12 ? 201 LEU B CB 1 ATOM 3581 C CG . LEU B 1 201 ? 30.094 18.357 31.067 1.00 17.44 ? 201 LEU B CG 1 ATOM 3582 C CD1 . LEU B 1 201 ? 28.753 17.627 30.990 1.00 18.71 ? 201 LEU B CD1 1 ATOM 3583 C CD2 . LEU B 1 201 ? 30.227 19.116 32.383 1.00 17.86 ? 201 LEU B CD2 1 ATOM 3584 N N . SER B 1 202 ? 33.730 15.912 29.781 1.00 15.78 ? 202 SER B N 1 ATOM 3585 C CA . SER B 1 202 ? 34.652 14.786 29.799 1.00 15.67 ? 202 SER B CA 1 ATOM 3586 C C . SER B 1 202 ? 36.092 15.272 29.945 1.00 17.46 ? 202 SER B C 1 ATOM 3587 O O . SER B 1 202 ? 36.877 14.696 30.700 1.00 16.60 ? 202 SER B O 1 ATOM 3588 C CB . SER B 1 202 ? 34.504 13.954 28.521 1.00 15.45 ? 202 SER B CB 1 ATOM 3589 O OG . SER B 1 202 ? 33.233 13.328 28.462 1.00 14.41 ? 202 SER B OG 1 ATOM 3590 N N . PHE B 1 203 ? 36.437 16.337 29.230 1.00 16.93 ? 203 PHE B N 1 ATOM 3591 C CA . PHE B 1 203 ? 37.790 16.869 29.304 1.00 17.28 ? 203 PHE B CA 1 ATOM 3592 C C . PHE B 1 203 ? 38.094 17.450 30.686 1.00 18.28 ? 203 PHE B C 1 ATOM 3593 O O . PHE B 1 203 ? 39.123 17.129 31.286 1.00 18.76 ? 203 PHE B O 1 ATOM 3594 C CB . PHE B 1 203 ? 38.011 17.935 28.226 1.00 16.48 ? 203 PHE B CB 1 ATOM 3595 C CG . PHE B 1 203 ? 39.339 18.626 28.328 1.00 16.99 ? 203 PHE B CG 1 ATOM 3596 C CD1 . PHE B 1 203 ? 39.436 19.888 28.901 1.00 18.07 ? 203 PHE B CD1 1 ATOM 3597 C CD2 . PHE B 1 203 ? 40.496 17.993 27.895 1.00 17.89 ? 203 PHE B CD2 1 ATOM 3598 C CE1 . PHE B 1 203 ? 40.668 20.509 29.043 1.00 19.54 ? 203 PHE B CE1 1 ATOM 3599 C CE2 . PHE B 1 203 ? 41.736 18.601 28.032 1.00 18.25 ? 203 PHE B CE2 1 ATOM 3600 C CZ . PHE B 1 203 ? 41.824 19.862 28.608 1.00 19.90 ? 203 PHE B CZ 1 ATOM 3601 N N . GLN B 1 204 ? 37.205 18.294 31.200 1.00 17.67 ? 204 GLN B N 1 ATOM 3602 C CA . GLN B 1 204 ? 37.429 18.892 32.509 1.00 17.69 ? 204 GLN B CA 1 ATOM 3603 C C . GLN B 1 204 ? 37.498 17.835 33.614 1.00 18.65 ? 204 GLN B C 1 ATOM 3604 O O . GLN B 1 204 ? 38.335 17.918 34.518 1.00 19.15 ? 204 GLN B O 1 ATOM 3605 C CB . GLN B 1 204 ? 36.328 19.907 32.828 1.00 19.16 ? 204 GLN B CB 1 ATOM 3606 C CG . GLN B 1 204 ? 36.350 21.179 31.975 1.00 20.48 ? 204 GLN B CG 1 ATOM 3607 C CD . GLN B 1 204 ? 37.643 21.980 32.130 1.00 22.96 ? 204 GLN B CD 1 ATOM 3608 O OE1 . GLN B 1 204 ? 38.208 22.068 33.220 1.00 23.09 ? 204 GLN B OE1 1 ATOM 3609 N NE2 . GLN B 1 204 ? 38.104 22.579 31.037 1.00 24.38 ? 204 GLN B NE2 1 ATOM 3610 N N . ILE B 1 205 ? 36.628 16.834 33.543 1.00 17.97 ? 205 ILE B N 1 ATOM 3611 C CA . ILE B 1 205 ? 36.621 15.790 34.564 1.00 17.39 ? 205 ILE B CA 1 ATOM 3612 C C . ILE B 1 205 ? 37.904 14.953 34.527 1.00 17.39 ? 205 ILE B C 1 ATOM 3613 O O . ILE B 1 205 ? 38.574 14.784 35.546 1.00 17.75 ? 205 ILE B O 1 ATOM 3614 C CB . ILE B 1 205 ? 35.386 14.860 34.405 1.00 15.33 ? 205 ILE B CB 1 ATOM 3615 C CG1 . ILE B 1 205 ? 34.110 15.639 34.742 1.00 15.33 ? 205 ILE B CG1 1 ATOM 3616 C CG2 . ILE B 1 205 ? 35.522 13.635 35.306 1.00 15.08 ? 205 ILE B CG2 1 ATOM 3617 C CD1 . ILE B 1 205 ? 32.810 14.881 34.462 1.00 14.00 ? 205 ILE B CD1 1 ATOM 3618 N N . ARG B 1 206 ? 38.255 14.449 33.349 1.00 17.64 ? 206 ARG B N 1 ATOM 3619 C CA . ARG B 1 206 ? 39.438 13.612 33.215 1.00 17.37 ? 206 ARG B CA 1 ATOM 3620 C C . ARG B 1 206 ? 40.730 14.305 33.620 1.00 18.31 ? 206 ARG B C 1 ATOM 3621 O O . ARG B 1 206 ? 41.601 13.688 34.235 1.00 17.31 ? 206 ARG B O 1 ATOM 3622 C CB . ARG B 1 206 ? 39.582 13.108 31.782 1.00 17.45 ? 206 ARG B CB 1 ATOM 3623 C CG . ARG B 1 206 ? 40.746 12.149 31.602 1.00 19.66 ? 206 ARG B CG 1 ATOM 3624 C CD . ARG B 1 206 ? 40.913 11.724 30.151 1.00 21.40 ? 206 ARG B CD 1 ATOM 3625 N NE . ARG B 1 206 ? 41.400 12.806 29.293 1.00 24.17 ? 206 ARG B NE 1 ATOM 3626 C CZ . ARG B 1 206 ? 42.630 13.321 29.337 1.00 24.85 ? 206 ARG B CZ 1 ATOM 3627 N NH1 . ARG B 1 206 ? 43.529 12.864 30.203 1.00 26.65 ? 206 ARG B NH1 1 ATOM 3628 N NH2 . ARG B 1 206 ? 42.969 14.289 28.501 1.00 23.78 ? 206 ARG B NH2 1 ATOM 3629 N N . THR B 1 207 ? 40.858 15.584 33.289 1.00 17.29 ? 207 THR B N 1 ATOM 3630 C CA . THR B 1 207 ? 42.087 16.301 33.610 1.00 19.40 ? 207 THR B CA 1 ATOM 3631 C C . THR B 1 207 ? 42.145 16.907 35.008 1.00 20.00 ? 207 THR B C 1 ATOM 3632 O O . THR B 1 207 ? 43.205 17.376 35.431 1.00 21.14 ? 207 THR B O 1 ATOM 3633 C CB . THR B 1 207 ? 42.382 17.424 32.574 1.00 17.42 ? 207 THR B CB 1 ATOM 3634 O OG1 . THR B 1 207 ? 41.327 18.390 32.598 1.00 19.81 ? 207 THR B OG1 1 ATOM 3635 C CG2 . THR B 1 207 ? 42.519 16.843 31.179 1.00 16.12 ? 207 THR B CG2 1 ATOM 3636 N N . SER B 1 208 ? 41.028 16.898 35.731 1.00 20.31 ? 208 SER B N 1 ATOM 3637 C CA . SER B 1 208 ? 41.012 17.463 37.080 1.00 20.78 ? 208 SER B CA 1 ATOM 3638 C C . SER B 1 208 ? 41.812 16.585 38.045 1.00 20.67 ? 208 SER B C 1 ATOM 3639 O O . SER B 1 208 ? 42.055 15.407 37.772 1.00 20.75 ? 208 SER B O 1 ATOM 3640 C CB . SER B 1 208 ? 39.570 17.611 37.592 1.00 20.83 ? 208 SER B CB 1 ATOM 3641 O OG . SER B 1 208 ? 39.001 16.347 37.888 1.00 23.21 ? 208 SER B OG 1 ATOM 3642 N N . GLY B 1 209 ? 42.232 17.171 39.163 1.00 20.61 ? 209 GLY B N 1 ATOM 3643 C CA . GLY B 1 209 ? 42.988 16.431 40.155 1.00 21.41 ? 209 GLY B CA 1 ATOM 3644 C C . GLY B 1 209 ? 42.055 15.719 41.115 1.00 23.24 ? 209 GLY B C 1 ATOM 3645 O O . GLY B 1 209 ? 40.845 15.663 40.882 1.00 23.47 ? 209 GLY B O 1 ATOM 3646 N N . ALA B 1 210 ? 42.606 15.185 42.202 1.00 23.59 ? 210 ALA B N 1 ATOM 3647 C CA . ALA B 1 210 ? 41.810 14.457 43.188 1.00 24.42 ? 210 ALA B CA 1 ATOM 3648 C C . ALA B 1 210 ? 40.635 15.251 43.760 1.00 25.23 ? 210 ALA B C 1 ATOM 3649 O O . ALA B 1 210 ? 39.609 14.666 44.119 1.00 25.92 ? 210 ALA B O 1 ATOM 3650 C CB . ALA B 1 210 ? 42.709 13.960 44.327 1.00 23.90 ? 210 ALA B CB 1 ATOM 3651 N N . ASN B 1 211 ? 40.775 16.571 43.848 1.00 25.88 ? 211 ASN B N 1 ATOM 3652 C CA . ASN B 1 211 ? 39.696 17.395 44.385 1.00 27.92 ? 211 ASN B CA 1 ATOM 3653 C C . ASN B 1 211 ? 38.542 17.568 43.398 1.00 28.14 ? 211 ASN B C 1 ATOM 3654 O O . ASN B 1 211 ? 37.493 18.104 43.749 1.00 29.81 ? 211 ASN B O 1 ATOM 3655 C CB . ASN B 1 211 ? 40.218 18.770 44.815 1.00 29.42 ? 211 ASN B CB 1 ATOM 3656 C CG . ASN B 1 211 ? 40.982 19.479 43.717 1.00 32.10 ? 211 ASN B CG 1 ATOM 3657 O OD1 . ASN B 1 211 ? 40.523 19.581 42.581 1.00 35.33 ? 211 ASN B OD1 1 ATOM 3658 N ND2 . ASN B 1 211 ? 42.155 19.988 44.058 1.00 34.60 ? 211 ASN B ND2 1 ATOM 3659 N N . GLY B 1 212 ? 38.739 17.110 42.167 1.00 27.16 ? 212 GLY B N 1 ATOM 3660 C CA . GLY B 1 212 ? 37.693 17.215 41.168 1.00 27.36 ? 212 GLY B CA 1 ATOM 3661 C C . GLY B 1 212 ? 37.372 18.624 40.705 1.00 27.77 ? 212 GLY B C 1 ATOM 3662 O O . GLY B 1 212 ? 36.343 18.850 40.056 1.00 28.72 ? 212 GLY B O 1 ATOM 3663 N N . MET B 1 213 ? 38.236 19.579 41.024 1.00 26.76 ? 213 MET B N 1 ATOM 3664 C CA . MET B 1 213 ? 38.000 20.954 40.604 1.00 28.05 ? 213 MET B CA 1 ATOM 3665 C C . MET B 1 213 ? 38.347 21.133 39.126 1.00 27.24 ? 213 MET B C 1 ATOM 3666 O O . MET B 1 213 ? 39.439 20.763 38.687 1.00 25.50 ? 213 MET B O 1 ATOM 3667 C CB . MET B 1 213 ? 38.827 21.921 41.458 1.00 31.12 ? 213 MET B CB 1 ATOM 3668 C CG . MET B 1 213 ? 38.459 21.909 42.936 1.00 36.41 ? 213 MET B CG 1 ATOM 3669 S SD . MET B 1 213 ? 36.677 22.165 43.223 1.00 43.72 ? 213 MET B SD 1 ATOM 3670 C CE . MET B 1 213 ? 36.216 20.634 44.096 1.00 39.15 ? 213 MET B CE 1 ATOM 3671 N N . PHE B 1 214 ? 37.406 21.687 38.363 1.00 26.41 ? 214 PHE B N 1 ATOM 3672 C CA . PHE B 1 214 ? 37.600 21.929 36.931 1.00 26.81 ? 214 PHE B CA 1 ATOM 3673 C C . PHE B 1 214 ? 38.578 23.079 36.729 1.00 27.78 ? 214 PHE B C 1 ATOM 3674 O O . PHE B 1 214 ? 38.567 24.043 37.491 1.00 28.94 ? 214 PHE B O 1 ATOM 3675 C CB . PHE B 1 214 ? 36.277 22.332 36.261 1.00 25.26 ? 214 PHE B CB 1 ATOM 3676 C CG . PHE B 1 214 ? 35.313 21.201 36.044 1.00 23.61 ? 214 PHE B CG 1 ATOM 3677 C CD1 . PHE B 1 214 ? 35.520 19.954 36.619 1.00 20.95 ? 214 PHE B CD1 1 ATOM 3678 C CD2 . PHE B 1 214 ? 34.167 21.406 35.274 1.00 23.30 ? 214 PHE B CD2 1 ATOM 3679 C CE1 . PHE B 1 214 ? 34.597 18.926 36.431 1.00 21.57 ? 214 PHE B CE1 1 ATOM 3680 C CE2 . PHE B 1 214 ? 33.241 20.387 35.081 1.00 22.27 ? 214 PHE B CE2 1 ATOM 3681 C CZ . PHE B 1 214 ? 33.457 19.144 35.661 1.00 20.79 ? 214 PHE B CZ 1 ATOM 3682 N N . SER B 1 215 ? 39.416 22.998 35.704 1.00 28.77 ? 215 SER B N 1 ATOM 3683 C CA . SER B 1 215 ? 40.333 24.099 35.452 1.00 31.33 ? 215 SER B CA 1 ATOM 3684 C C . SER B 1 215 ? 39.484 25.238 34.876 1.00 32.03 ? 215 SER B C 1 ATOM 3685 O O . SER B 1 215 ? 39.809 26.417 35.037 1.00 32.97 ? 215 SER B O 1 ATOM 3686 C CB . SER B 1 215 ? 41.428 23.686 34.467 1.00 30.81 ? 215 SER B CB 1 ATOM 3687 O OG . SER B 1 215 ? 40.887 23.398 33.194 1.00 36.70 ? 215 SER B OG 1 ATOM 3688 N N . GLU B 1 216 ? 38.384 24.872 34.218 1.00 32.13 ? 216 GLU B N 1 ATOM 3689 C CA . GLU B 1 216 ? 37.460 25.842 33.630 1.00 31.84 ? 216 GLU B CA 1 ATOM 3690 C C . GLU B 1 216 ? 36.026 25.348 33.782 1.00 30.36 ? 216 GLU B C 1 ATOM 3691 O O . GLU B 1 216 ? 35.739 24.177 33.546 1.00 28.96 ? 216 GLU B O 1 ATOM 3692 C CB . GLU B 1 216 ? 37.783 26.048 32.156 1.00 34.47 ? 216 GLU B CB 1 ATOM 3693 C CG . GLU B 1 216 ? 39.145 26.669 31.929 1.00 41.54 ? 216 GLU B CG 1 ATOM 3694 C CD . GLU B 1 216 ? 39.787 26.198 30.639 1.00 46.69 ? 216 GLU B CD 1 ATOM 3695 O OE1 . GLU B 1 216 ? 40.070 24.981 30.523 1.00 48.97 ? 216 GLU B OE1 1 ATOM 3696 O OE2 . GLU B 1 216 ? 40.007 27.041 29.740 1.00 49.14 ? 216 GLU B OE2 1 ATOM 3697 N N . ALA B 1 217 ? 35.132 26.244 34.184 1.00 28.32 ? 217 ALA B N 1 ATOM 3698 C CA . ALA B 1 217 ? 33.733 25.891 34.374 1.00 27.48 ? 217 ALA B CA 1 ATOM 3699 C C . ALA B 1 217 ? 33.056 25.536 33.064 1.00 27.39 ? 217 ALA B C 1 ATOM 3700 O O . ALA B 1 217 ? 33.440 26.013 31.997 1.00 26.98 ? 217 ALA B O 1 ATOM 3701 C CB . ALA B 1 217 ? 32.981 27.043 35.038 1.00 27.63 ? 217 ALA B CB 1 ATOM 3702 N N . VAL B 1 218 ? 32.044 24.684 33.154 1.00 26.24 ? 218 VAL B N 1 ATOM 3703 C CA . VAL B 1 218 ? 31.279 24.288 31.985 1.00 25.25 ? 218 VAL B CA 1 ATOM 3704 C C . VAL B 1 218 ? 29.863 24.772 32.248 1.00 24.42 ? 218 VAL B C 1 ATOM 3705 O O . VAL B 1 218 ? 29.303 24.537 33.316 1.00 24.16 ? 218 VAL B O 1 ATOM 3706 C CB . VAL B 1 218 ? 31.261 22.762 31.797 1.00 24.79 ? 218 VAL B CB 1 ATOM 3707 C CG1 . VAL B 1 218 ? 30.455 22.410 30.553 1.00 25.11 ? 218 VAL B CG1 1 ATOM 3708 C CG2 . VAL B 1 218 ? 32.685 22.233 31.682 1.00 23.90 ? 218 VAL B CG2 1 ATOM 3709 N N . GLU B 1 219 ? 29.290 25.462 31.275 1.00 25.06 ? 219 GLU B N 1 ATOM 3710 C CA . GLU B 1 219 ? 27.947 25.986 31.427 1.00 25.58 ? 219 GLU B CA 1 ATOM 3711 C C . GLU B 1 219 ? 26.871 25.032 30.935 1.00 24.07 ? 219 GLU B C 1 ATOM 3712 O O . GLU B 1 219 ? 26.937 24.516 29.818 1.00 22.70 ? 219 GLU B O 1 ATOM 3713 C CB . GLU B 1 219 ? 27.829 27.312 30.687 1.00 28.43 ? 219 GLU B CB 1 ATOM 3714 C CG . GLU B 1 219 ? 26.420 27.838 30.596 1.00 31.74 ? 219 GLU B CG 1 ATOM 3715 C CD . GLU B 1 219 ? 26.372 29.178 29.913 1.00 33.92 ? 219 GLU B CD 1 ATOM 3716 O OE1 . GLU B 1 219 ? 26.624 30.193 30.594 1.00 36.53 ? 219 GLU B OE1 1 ATOM 3717 O OE2 . GLU B 1 219 ? 26.099 29.214 28.694 1.00 35.24 ? 219 GLU B OE2 1 ATOM 3718 N N . LEU B 1 220 ? 25.883 24.799 31.787 1.00 23.06 ? 220 LEU B N 1 ATOM 3719 C CA . LEU B 1 220 ? 24.772 23.927 31.445 1.00 24.09 ? 220 LEU B CA 1 ATOM 3720 C C . LEU B 1 220 ? 23.486 24.722 31.649 1.00 25.07 ? 220 LEU B C 1 ATOM 3721 O O . LEU B 1 220 ? 23.528 25.877 32.073 1.00 25.71 ? 220 LEU B O 1 ATOM 3722 C CB . LEU B 1 220 ? 24.781 22.671 32.328 1.00 21.40 ? 220 LEU B CB 1 ATOM 3723 C CG . LEU B 1 220 ? 25.924 21.679 32.071 1.00 19.58 ? 220 LEU B CG 1 ATOM 3724 C CD1 . LEU B 1 220 ? 25.846 20.537 33.071 1.00 17.35 ? 220 LEU B CD1 1 ATOM 3725 C CD2 . LEU B 1 220 ? 25.833 21.148 30.644 1.00 17.79 ? 220 LEU B CD2 1 ATOM 3726 N N . GLU B 1 221 ? 22.348 24.112 31.341 1.00 24.96 ? 221 GLU B N 1 ATOM 3727 C CA . GLU B 1 221 ? 21.073 24.794 31.494 1.00 25.48 ? 221 GLU B CA 1 ATOM 3728 C C . GLU B 1 221 ? 20.002 23.934 32.129 1.00 26.29 ? 221 GLU B C 1 ATOM 3729 O O . GLU B 1 221 ? 19.937 22.726 31.893 1.00 25.13 ? 221 GLU B O 1 ATOM 3730 C CB . GLU B 1 221 ? 20.565 25.275 30.137 1.00 25.91 ? 221 GLU B CB 1 ATOM 3731 C CG . GLU B 1 221 ? 21.353 26.425 29.562 1.00 29.02 ? 221 GLU B CG 1 ATOM 3732 C CD . GLU B 1 221 ? 20.798 26.892 28.242 1.00 30.24 ? 221 GLU B CD 1 ATOM 3733 O OE1 . GLU B 1 221 ? 19.596 26.656 27.989 1.00 30.39 ? 221 GLU B OE1 1 ATOM 3734 O OE2 . GLU B 1 221 ? 21.558 27.505 27.463 1.00 31.37 ? 221 GLU B OE2 1 ATOM 3735 N N . ARG B 1 222 ? 19.166 24.570 32.945 1.00 27.01 ? 222 ARG B N 1 ATOM 3736 C CA . ARG B 1 222 ? 18.054 23.886 33.587 1.00 27.56 ? 222 ARG B CA 1 ATOM 3737 C C . ARG B 1 222 ? 16.996 23.735 32.489 1.00 27.18 ? 222 ARG B C 1 ATOM 3738 O O . ARG B 1 222 ? 17.119 24.331 31.414 1.00 26.54 ? 222 ARG B O 1 ATOM 3739 C CB . ARG B 1 222 ? 17.507 24.727 34.748 1.00 27.18 ? 222 ARG B CB 1 ATOM 3740 C CG . ARG B 1 222 ? 18.499 24.946 35.882 1.00 28.82 ? 222 ARG B CG 1 ATOM 3741 C CD . ARG B 1 222 ? 18.884 23.625 36.545 1.00 31.05 ? 222 ARG B CD 1 ATOM 3742 N NE . ARG B 1 222 ? 19.814 23.805 37.661 1.00 32.98 ? 222 ARG B NE 1 ATOM 3743 C CZ . ARG B 1 222 ? 20.393 22.810 38.332 1.00 33.45 ? 222 ARG B CZ 1 ATOM 3744 N NH1 . ARG B 1 222 ? 20.148 21.546 38.007 1.00 33.42 ? 222 ARG B NH1 1 ATOM 3745 N NH2 . ARG B 1 222 ? 21.221 23.078 39.334 1.00 32.82 ? 222 ARG B NH2 1 ATOM 3746 N N . ALA B 1 223 ? 15.966 22.939 32.746 1.00 27.53 ? 223 ALA B N 1 ATOM 3747 C CA . ALA B 1 223 ? 14.921 22.734 31.750 1.00 28.47 ? 223 ALA B CA 1 ATOM 3748 C C . ALA B 1 223 ? 14.435 24.069 31.194 1.00 29.18 ? 223 ALA B C 1 ATOM 3749 O O . ALA B 1 223 ? 14.373 24.256 29.981 1.00 29.27 ? 223 ALA B O 1 ATOM 3750 C CB . ALA B 1 223 ? 13.754 21.956 32.361 1.00 27.79 ? 223 ALA B CB 1 ATOM 3751 N N . ASN B 1 224 ? 14.113 24.995 32.095 1.00 31.13 ? 224 ASN B N 1 ATOM 3752 C CA . ASN B 1 224 ? 13.615 26.325 31.738 1.00 31.54 ? 224 ASN B CA 1 ATOM 3753 C C . ASN B 1 224 ? 14.622 27.167 30.969 1.00 31.31 ? 224 ASN B C 1 ATOM 3754 O O . ASN B 1 224 ? 14.308 28.280 30.558 1.00 31.52 ? 224 ASN B O 1 ATOM 3755 C CB . ASN B 1 224 ? 13.210 27.082 33.000 1.00 32.77 ? 224 ASN B CB 1 ATOM 3756 C CG . ASN B 1 224 ? 14.373 27.283 33.943 1.00 34.85 ? 224 ASN B CG 1 ATOM 3757 O OD1 . ASN B 1 224 ? 15.416 27.791 33.547 1.00 37.33 ? 224 ASN B OD1 1 ATOM 3758 N ND2 . ASN B 1 224 ? 14.204 26.883 35.197 1.00 37.16 ? 224 ASN B ND2 1 ATOM 3759 N N . GLY B 1 225 ? 15.835 26.651 30.792 1.00 31.54 ? 225 GLY B N 1 ATOM 3760 C CA . GLY B 1 225 ? 16.847 27.391 30.058 1.00 31.80 ? 225 GLY B CA 1 ATOM 3761 C C . GLY B 1 225 ? 17.796 28.212 30.916 1.00 32.26 ? 225 GLY B C 1 ATOM 3762 O O . GLY B 1 225 ? 18.726 28.834 30.397 1.00 31.00 ? 225 GLY B O 1 ATOM 3763 N N . LYS B 1 226 ? 17.578 28.220 32.227 1.00 33.28 ? 226 LYS B N 1 ATOM 3764 C CA . LYS B 1 226 ? 18.445 28.986 33.109 1.00 33.56 ? 226 LYS B CA 1 ATOM 3765 C C . LYS B 1 226 ? 19.840 28.377 33.154 1.00 33.93 ? 226 LYS B C 1 ATOM 3766 O O . LYS B 1 226 ? 20.019 27.204 33.497 1.00 32.63 ? 226 LYS B O 1 ATOM 3767 C CB . LYS B 1 226 ? 17.879 29.058 34.523 1.00 34.65 ? 226 LYS B CB 1 ATOM 3768 C CG . LYS B 1 226 ? 18.680 29.995 35.402 1.00 35.97 ? 226 LYS B CG 1 ATOM 3769 C CD . LYS B 1 226 ? 18.244 29.934 36.840 1.00 39.24 ? 226 LYS B CD 1 ATOM 3770 C CE . LYS B 1 226 ? 19.118 30.834 37.697 1.00 40.55 ? 226 LYS B CE 1 ATOM 3771 N NZ . LYS B 1 226 ? 18.724 30.753 39.127 1.00 43.64 ? 226 LYS B NZ 1 ATOM 3772 N N . LYS B 1 227 ? 20.826 29.194 32.808 1.00 33.80 ? 227 LYS B N 1 ATOM 3773 C CA . LYS B 1 227 ? 22.208 28.755 32.781 1.00 34.87 ? 227 LYS B CA 1 ATOM 3774 C C . LYS B 1 227 ? 22.880 28.739 34.146 1.00 35.19 ? 227 LYS B C 1 ATOM 3775 O O . LYS B 1 227 ? 22.635 29.604 34.990 1.00 35.51 ? 227 LYS B O 1 ATOM 3776 C CB . LYS B 1 227 ? 23.011 29.634 31.814 1.00 35.25 ? 227 LYS B CB 1 ATOM 3777 C CG . LYS B 1 227 ? 22.585 29.473 30.361 1.00 36.33 ? 227 LYS B CG 1 ATOM 3778 C CD . LYS B 1 227 ? 23.501 30.210 29.414 1.00 36.63 ? 227 LYS B CD 1 ATOM 3779 C CE . LYS B 1 227 ? 23.276 31.700 29.473 1.00 38.23 ? 227 LYS B CE 1 ATOM 3780 N NZ . LYS B 1 227 ? 21.915 32.045 28.982 1.00 40.65 ? 227 LYS B NZ 1 ATOM 3781 N N . TYR B 1 228 ? 23.714 27.723 34.357 1.00 34.44 ? 228 TYR B N 1 ATOM 3782 C CA . TYR B 1 228 ? 24.475 27.575 35.588 1.00 33.11 ? 228 TYR B CA 1 ATOM 3783 C C . TYR B 1 228 ? 25.810 26.969 35.195 1.00 33.93 ? 228 TYR B C 1 ATOM 3784 O O . TYR B 1 228 ? 25.969 26.491 34.064 1.00 33.84 ? 228 TYR B O 1 ATOM 3785 C CB . TYR B 1 228 ? 23.753 26.680 36.604 1.00 32.79 ? 228 TYR B CB 1 ATOM 3786 C CG . TYR B 1 228 ? 23.552 25.239 36.190 1.00 33.58 ? 228 TYR B CG 1 ATOM 3787 C CD1 . TYR B 1 228 ? 22.520 24.875 35.319 1.00 32.35 ? 228 TYR B CD1 1 ATOM 3788 C CD2 . TYR B 1 228 ? 24.376 24.232 36.698 1.00 32.20 ? 228 TYR B CD2 1 ATOM 3789 C CE1 . TYR B 1 228 ? 22.311 23.541 34.971 1.00 31.79 ? 228 TYR B CE1 1 ATOM 3790 C CE2 . TYR B 1 228 ? 24.177 22.901 36.355 1.00 31.14 ? 228 TYR B CE2 1 ATOM 3791 C CZ . TYR B 1 228 ? 23.144 22.562 35.494 1.00 32.09 ? 228 TYR B CZ 1 ATOM 3792 O OH . TYR B 1 228 ? 22.940 21.240 35.171 1.00 32.06 ? 228 TYR B OH 1 ATOM 3793 N N . TYR B 1 229 ? 26.772 26.989 36.113 1.00 32.98 ? 229 TYR B N 1 ATOM 3794 C CA . TYR B 1 229 ? 28.086 26.461 35.799 1.00 31.83 ? 229 TYR B CA 1 ATOM 3795 C C . TYR B 1 229 ? 28.504 25.302 36.662 1.00 30.09 ? 229 TYR B C 1 ATOM 3796 O O . TYR B 1 229 ? 28.260 25.282 37.868 1.00 29.82 ? 229 TYR B O 1 ATOM 3797 C CB . TYR B 1 229 ? 29.132 27.573 35.888 1.00 34.71 ? 229 TYR B CB 1 ATOM 3798 C CG . TYR B 1 229 ? 28.781 28.748 35.017 1.00 37.96 ? 229 TYR B CG 1 ATOM 3799 C CD1 . TYR B 1 229 ? 27.696 29.565 35.335 1.00 40.32 ? 229 TYR B CD1 1 ATOM 3800 C CD2 . TYR B 1 229 ? 29.466 28.991 33.830 1.00 38.66 ? 229 TYR B CD2 1 ATOM 3801 C CE1 . TYR B 1 229 ? 27.290 30.586 34.491 1.00 43.14 ? 229 TYR B CE1 1 ATOM 3802 C CE2 . TYR B 1 229 ? 29.071 30.018 32.973 1.00 42.89 ? 229 TYR B CE2 1 ATOM 3803 C CZ . TYR B 1 229 ? 27.975 30.809 33.311 1.00 44.40 ? 229 TYR B CZ 1 ATOM 3804 O OH . TYR B 1 229 ? 27.538 31.807 32.465 1.00 47.43 ? 229 TYR B OH 1 ATOM 3805 N N . VAL B 1 230 ? 29.119 24.322 36.017 1.00 28.16 ? 230 VAL B N 1 ATOM 3806 C CA . VAL B 1 230 ? 29.626 23.148 36.703 1.00 27.56 ? 230 VAL B CA 1 ATOM 3807 C C . VAL B 1 230 ? 31.114 23.428 36.877 1.00 26.36 ? 230 VAL B C 1 ATOM 3808 O O . VAL B 1 230 ? 31.823 23.659 35.896 1.00 26.67 ? 230 VAL B O 1 ATOM 3809 C CB . VAL B 1 230 ? 29.433 21.872 35.854 1.00 27.23 ? 230 VAL B CB 1 ATOM 3810 C CG1 . VAL B 1 230 ? 30.216 20.718 36.460 1.00 26.83 ? 230 VAL B CG1 1 ATOM 3811 C CG2 . VAL B 1 230 ? 27.955 21.524 35.780 1.00 26.60 ? 230 VAL B CG2 1 ATOM 3812 N N . THR B 1 231 ? 31.582 23.427 38.121 1.00 25.81 ? 231 THR B N 1 ATOM 3813 C CA . THR B 1 231 ? 32.990 23.706 38.384 1.00 24.41 ? 231 THR B CA 1 ATOM 3814 C C . THR B 1 231 ? 33.720 22.555 39.069 1.00 24.36 ? 231 THR B C 1 ATOM 3815 O O . THR B 1 231 ? 34.939 22.614 39.250 1.00 25.45 ? 231 THR B O 1 ATOM 3816 C CB . THR B 1 231 ? 33.146 24.987 39.235 1.00 23.74 ? 231 THR B CB 1 ATOM 3817 O OG1 . THR B 1 231 ? 32.423 24.839 40.463 1.00 23.43 ? 231 THR B OG1 1 ATOM 3818 C CG2 . THR B 1 231 ? 32.609 26.199 38.478 1.00 22.73 ? 231 THR B CG2 1 ATOM 3819 N N . ALA B 1 232 ? 32.980 21.513 39.442 1.00 22.79 ? 232 ALA B N 1 ATOM 3820 C CA . ALA B 1 232 ? 33.573 20.342 40.093 1.00 23.18 ? 232 ALA B CA 1 ATOM 3821 C C . ALA B 1 232 ? 32.922 19.042 39.611 1.00 22.92 ? 232 ALA B C 1 ATOM 3822 O O . ALA B 1 232 ? 31.735 19.019 39.259 1.00 22.26 ? 232 ALA B O 1 ATOM 3823 C CB . ALA B 1 232 ? 33.445 20.457 41.616 1.00 20.91 ? 232 ALA B CB 1 ATOM 3824 N N . VAL B 1 233 ? 33.709 17.967 39.599 1.00 22.81 ? 233 VAL B N 1 ATOM 3825 C CA . VAL B 1 233 ? 33.236 16.650 39.165 1.00 22.30 ? 233 VAL B CA 1 ATOM 3826 C C . VAL B 1 233 ? 31.965 16.186 39.882 1.00 24.09 ? 233 VAL B C 1 ATOM 3827 O O . VAL B 1 233 ? 31.008 15.748 39.241 1.00 23.08 ? 233 VAL B O 1 ATOM 3828 C CB . VAL B 1 233 ? 34.322 15.561 39.377 1.00 21.21 ? 233 VAL B CB 1 ATOM 3829 C CG1 . VAL B 1 233 ? 33.763 14.179 39.026 1.00 18.41 ? 233 VAL B CG1 1 ATOM 3830 C CG2 . VAL B 1 233 ? 35.544 15.874 38.525 1.00 20.27 ? 233 VAL B CG2 1 ATOM 3831 N N . ASP B 1 234 ? 31.961 16.277 41.210 1.00 24.45 ? 234 ASP B N 1 ATOM 3832 C CA . ASP B 1 234 ? 30.816 15.844 42.006 1.00 26.53 ? 234 ASP B CA 1 ATOM 3833 C C . ASP B 1 234 ? 29.483 16.497 41.626 1.00 26.36 ? 234 ASP B C 1 ATOM 3834 O O . ASP B 1 234 ? 28.423 15.905 41.814 1.00 26.87 ? 234 ASP B O 1 ATOM 3835 C CB . ASP B 1 234 ? 31.114 16.063 43.494 1.00 30.19 ? 234 ASP B CB 1 ATOM 3836 C CG . ASP B 1 234 ? 31.770 14.847 44.145 1.00 34.45 ? 234 ASP B CG 1 ATOM 3837 O OD1 . ASP B 1 234 ? 32.439 14.062 43.432 1.00 37.97 ? 234 ASP B OD1 1 ATOM 3838 O OD2 . ASP B 1 234 ? 31.624 14.679 45.377 1.00 37.59 ? 234 ASP B OD2 1 ATOM 3839 N N . GLN B 1 235 ? 29.531 17.705 41.083 1.00 25.98 ? 235 GLN B N 1 ATOM 3840 C CA . GLN B 1 235 ? 28.314 18.408 40.686 1.00 26.29 ? 235 GLN B CA 1 ATOM 3841 C C . GLN B 1 235 ? 27.568 17.707 39.555 1.00 26.38 ? 235 GLN B C 1 ATOM 3842 O O . GLN B 1 235 ? 26.341 17.722 39.506 1.00 28.09 ? 235 GLN B O 1 ATOM 3843 C CB . GLN B 1 235 ? 28.650 19.822 40.215 1.00 28.04 ? 235 GLN B CB 1 ATOM 3844 C CG . GLN B 1 235 ? 29.060 20.789 41.303 1.00 29.73 ? 235 GLN B CG 1 ATOM 3845 C CD . GLN B 1 235 ? 29.846 21.958 40.753 1.00 30.34 ? 235 GLN B CD 1 ATOM 3846 O OE1 . GLN B 1 235 ? 29.473 22.561 39.747 1.00 29.60 ? 235 GLN B OE1 1 ATOM 3847 N NE2 . GLN B 1 235 ? 30.947 22.288 41.417 1.00 34.52 ? 235 GLN B NE2 1 ATOM 3848 N N . VAL B 1 236 ? 28.315 17.094 38.646 1.00 24.57 ? 236 VAL B N 1 ATOM 3849 C CA . VAL B 1 236 ? 27.715 16.448 37.488 1.00 22.20 ? 236 VAL B CA 1 ATOM 3850 C C . VAL B 1 236 ? 27.883 14.925 37.458 1.00 21.30 ? 236 VAL B C 1 ATOM 3851 O O . VAL B 1 236 ? 27.247 14.235 36.659 1.00 19.30 ? 236 VAL B O 1 ATOM 3852 C CB . VAL B 1 236 ? 28.315 17.081 36.186 1.00 21.82 ? 236 VAL B CB 1 ATOM 3853 C CG1 . VAL B 1 236 ? 29.782 16.683 36.029 1.00 19.21 ? 236 VAL B CG1 1 ATOM 3854 C CG2 . VAL B 1 236 ? 27.514 16.672 34.976 1.00 23.08 ? 236 VAL B CG2 1 ATOM 3855 N N . LYS B 1 237 ? 28.720 14.398 38.344 1.00 20.06 ? 237 LYS B N 1 ATOM 3856 C CA . LYS B 1 237 ? 28.990 12.970 38.362 1.00 19.49 ? 237 LYS B CA 1 ATOM 3857 C C . LYS B 1 237 ? 27.774 12.041 38.302 1.00 19.15 ? 237 LYS B C 1 ATOM 3858 O O . LYS B 1 237 ? 27.785 11.049 37.570 1.00 20.55 ? 237 LYS B O 1 ATOM 3859 C CB . LYS B 1 237 ? 29.856 12.606 39.574 1.00 20.87 ? 237 LYS B CB 1 ATOM 3860 C CG . LYS B 1 237 ? 30.290 11.143 39.572 1.00 23.61 ? 237 LYS B CG 1 ATOM 3861 C CD . LYS B 1 237 ? 31.007 10.719 40.864 1.00 25.21 ? 237 LYS B CD 1 ATOM 3862 C CE . LYS B 1 237 ? 32.474 11.089 40.851 1.00 26.81 ? 237 LYS B CE 1 ATOM 3863 N NZ . LYS B 1 237 ? 33.234 10.352 41.908 1.00 25.17 ? 237 LYS B NZ 1 ATOM 3864 N N . PRO B 1 238 ? 26.708 12.340 39.059 1.00 18.33 ? 238 PRO B N 1 ATOM 3865 C CA . PRO B 1 238 ? 25.550 11.441 38.997 1.00 18.47 ? 238 PRO B CA 1 ATOM 3866 C C . PRO B 1 238 ? 24.747 11.419 37.683 1.00 18.46 ? 238 PRO B C 1 ATOM 3867 O O . PRO B 1 238 ? 23.876 10.562 37.503 1.00 19.32 ? 238 PRO B O 1 ATOM 3868 C CB . PRO B 1 238 ? 24.715 11.875 40.200 1.00 19.13 ? 238 PRO B CB 1 ATOM 3869 C CG . PRO B 1 238 ? 25.042 13.315 40.332 1.00 21.20 ? 238 PRO B CG 1 ATOM 3870 C CD . PRO B 1 238 ? 26.526 13.364 40.098 1.00 18.02 ? 238 PRO B CD 1 ATOM 3871 N N . LYS B 1 239 ? 25.045 12.335 36.765 1.00 16.38 ? 239 LYS B N 1 ATOM 3872 C CA . LYS B 1 239 ? 24.336 12.407 35.482 1.00 15.61 ? 239 LYS B CA 1 ATOM 3873 C C . LYS B 1 239 ? 25.085 11.740 34.331 1.00 14.62 ? 239 LYS B C 1 ATOM 3874 O O . LYS B 1 239 ? 24.537 11.558 33.248 1.00 12.91 ? 239 LYS B O 1 ATOM 3875 C CB . LYS B 1 239 ? 24.106 13.866 35.089 1.00 16.29 ? 239 LYS B CB 1 ATOM 3876 C CG . LYS B 1 239 ? 23.379 14.686 36.114 1.00 17.73 ? 239 LYS B CG 1 ATOM 3877 C CD . LYS B 1 239 ? 23.029 16.043 35.560 1.00 21.97 ? 239 LYS B CD 1 ATOM 3878 C CE . LYS B 1 239 ? 22.262 16.867 36.588 1.00 24.26 ? 239 LYS B CE 1 ATOM 3879 N NZ . LYS B 1 239 ? 21.710 18.099 35.970 1.00 27.74 ? 239 LYS B NZ 1 ATOM 3880 N N . ILE B 1 240 ? 26.344 11.393 34.571 1.00 15.07 ? 240 ILE B N 1 ATOM 3881 C CA . ILE B 1 240 ? 27.206 10.807 33.546 1.00 15.07 ? 240 ILE B CA 1 ATOM 3882 C C . ILE B 1 240 ? 27.481 9.320 33.743 1.00 14.90 ? 240 ILE B C 1 ATOM 3883 O O . ILE B 1 240 ? 27.876 8.901 34.831 1.00 16.09 ? 240 ILE B O 1 ATOM 3884 C CB . ILE B 1 240 ? 28.570 11.544 33.519 1.00 14.71 ? 240 ILE B CB 1 ATOM 3885 C CG1 . ILE B 1 240 ? 28.348 13.049 33.359 1.00 14.74 ? 240 ILE B CG1 1 ATOM 3886 C CG2 . ILE B 1 240 ? 29.434 11.013 32.389 1.00 14.47 ? 240 ILE B CG2 1 ATOM 3887 C CD1 . ILE B 1 240 ? 29.615 13.865 33.516 1.00 15.76 ? 240 ILE B CD1 1 ATOM 3888 N N . ALA B 1 241 ? 27.287 8.531 32.684 1.00 13.17 ? 241 ALA B N 1 ATOM 3889 C CA . ALA B 1 241 ? 27.534 7.091 32.738 1.00 12.22 ? 241 ALA B CA 1 ATOM 3890 C C . ALA B 1 241 ? 28.875 6.742 32.086 1.00 12.59 ? 241 ALA B C 1 ATOM 3891 O O . ALA B 1 241 ? 29.542 5.791 32.492 1.00 11.98 ? 241 ALA B O 1 ATOM 3892 C CB . ALA B 1 241 ? 26.404 6.338 32.031 1.00 12.29 ? 241 ALA B CB 1 ATOM 3893 N N . LEU B 1 242 ? 29.255 7.528 31.079 1.00 12.52 ? 242 LEU B N 1 ATOM 3894 C CA . LEU B 1 242 ? 30.490 7.317 30.328 1.00 13.52 ? 242 LEU B CA 1 ATOM 3895 C C . LEU B 1 242 ? 31.203 8.630 30.028 1.00 14.51 ? 242 LEU B C 1 ATOM 3896 O O . LEU B 1 242 ? 30.563 9.639 29.727 1.00 14.70 ? 242 LEU B O 1 ATOM 3897 C CB . LEU B 1 242 ? 30.178 6.625 28.995 1.00 11.55 ? 242 LEU B CB 1 ATOM 3898 C CG . LEU B 1 242 ? 29.566 5.221 28.993 1.00 12.66 ? 242 LEU B CG 1 ATOM 3899 C CD1 . LEU B 1 242 ? 29.019 4.928 27.603 1.00 12.67 ? 242 LEU B CD1 1 ATOM 3900 C CD2 . LEU B 1 242 ? 30.607 4.177 29.391 1.00 11.27 ? 242 LEU B CD2 1 ATOM 3901 N N . LEU B 1 243 ? 32.533 8.611 30.099 1.00 14.62 ? 243 LEU B N 1 ATOM 3902 C CA . LEU B 1 243 ? 33.334 9.794 29.801 1.00 14.79 ? 243 LEU B CA 1 ATOM 3903 C C . LEU B 1 243 ? 34.071 9.594 28.493 1.00 14.79 ? 243 LEU B C 1 ATOM 3904 O O . LEU B 1 243 ? 34.590 8.515 28.221 1.00 15.38 ? 243 LEU B O 1 ATOM 3905 C CB . LEU B 1 243 ? 34.386 10.056 30.885 1.00 15.43 ? 243 LEU B CB 1 ATOM 3906 C CG . LEU B 1 243 ? 34.009 10.678 32.227 1.00 17.13 ? 243 LEU B CG 1 ATOM 3907 C CD1 . LEU B 1 243 ? 35.274 10.782 33.073 1.00 16.89 ? 243 LEU B CD1 1 ATOM 3908 C CD2 . LEU B 1 243 ? 33.380 12.049 32.032 1.00 15.67 ? 243 LEU B CD2 1 ATOM 3909 N N . LYS B 1 244 ? 34.115 10.639 27.681 1.00 16.29 ? 244 LYS B N 1 ATOM 3910 C CA . LYS B 1 244 ? 34.843 10.576 26.424 1.00 17.97 ? 244 LYS B CA 1 ATOM 3911 C C . LYS B 1 244 ? 36.307 10.843 26.780 1.00 19.50 ? 244 LYS B C 1 ATOM 3912 O O . LYS B 1 244 ? 36.593 11.569 27.739 1.00 18.05 ? 244 LYS B O 1 ATOM 3913 C CB . LYS B 1 244 ? 34.359 11.668 25.465 1.00 17.77 ? 244 LYS B CB 1 ATOM 3914 C CG . LYS B 1 244 ? 34.996 11.603 24.086 1.00 18.24 ? 244 LYS B CG 1 ATOM 3915 C CD . LYS B 1 244 ? 34.441 12.681 23.182 1.00 20.45 ? 244 LYS B CD 1 ATOM 3916 C CE . LYS B 1 244 ? 34.827 12.427 21.737 1.00 24.14 ? 244 LYS B CE 1 ATOM 3917 N NZ . LYS B 1 244 ? 34.202 13.431 20.822 1.00 26.73 ? 244 LYS B NZ 1 ATOM 3918 N N . PHE B 1 245 ? 37.233 10.246 26.038 1.00 20.03 ? 245 PHE B N 1 ATOM 3919 C CA . PHE B 1 245 ? 38.634 10.511 26.304 1.00 22.37 ? 245 PHE B CA 1 ATOM 3920 C C . PHE B 1 245 ? 39.049 11.631 25.356 1.00 23.71 ? 245 PHE B C 1 ATOM 3921 O O . PHE B 1 245 ? 39.284 11.399 24.171 1.00 23.34 ? 245 PHE B O 1 ATOM 3922 C CB . PHE B 1 245 ? 39.500 9.276 26.058 1.00 22.89 ? 245 PHE B CB 1 ATOM 3923 C CG . PHE B 1 245 ? 40.870 9.383 26.673 1.00 25.19 ? 245 PHE B CG 1 ATOM 3924 C CD1 . PHE B 1 245 ? 41.678 10.487 26.414 1.00 26.38 ? 245 PHE B CD1 1 ATOM 3925 C CD2 . PHE B 1 245 ? 41.334 8.412 27.547 1.00 25.68 ? 245 PHE B CD2 1 ATOM 3926 C CE1 . PHE B 1 245 ? 42.925 10.623 27.021 1.00 27.15 ? 245 PHE B CE1 1 ATOM 3927 C CE2 . PHE B 1 245 ? 42.581 8.542 28.159 1.00 26.38 ? 245 PHE B CE2 1 ATOM 3928 C CZ . PHE B 1 245 ? 43.373 9.649 27.895 1.00 26.12 ? 245 PHE B CZ 1 ATOM 3929 N N . VAL B 1 246 ? 39.107 12.848 25.884 1.00 26.10 ? 246 VAL B N 1 ATOM 3930 C CA . VAL B 1 246 ? 39.486 14.025 25.109 1.00 29.83 ? 246 VAL B CA 1 ATOM 3931 C C . VAL B 1 246 ? 40.897 14.452 25.532 1.00 33.24 ? 246 VAL B C 1 ATOM 3932 O O . VAL B 1 246 ? 41.155 14.648 26.718 1.00 32.71 ? 246 VAL B O 1 ATOM 3933 C CB . VAL B 1 246 ? 38.509 15.188 25.382 1.00 28.86 ? 246 VAL B CB 1 ATOM 3934 C CG1 . VAL B 1 246 ? 38.840 16.373 24.491 1.00 27.94 ? 246 VAL B CG1 1 ATOM 3935 C CG2 . VAL B 1 246 ? 37.068 14.722 25.164 1.00 29.39 ? 246 VAL B CG2 1 ATOM 3936 N N . ASP B 1 247 ? 41.808 14.593 24.571 1.00 37.77 ? 247 ASP B N 1 ATOM 3937 C CA . ASP B 1 247 ? 43.177 14.989 24.891 1.00 43.06 ? 247 ASP B CA 1 ATOM 3938 C C . ASP B 1 247 ? 43.375 16.485 25.071 1.00 44.76 ? 247 ASP B C 1 ATOM 3939 O O . ASP B 1 247 ? 44.094 16.917 25.975 1.00 44.90 ? 247 ASP B O 1 ATOM 3940 C CB . ASP B 1 247 ? 44.146 14.476 23.826 1.00 46.17 ? 247 ASP B CB 1 ATOM 3941 C CG . ASP B 1 247 ? 44.683 13.098 24.150 1.00 50.63 ? 247 ASP B CG 1 ATOM 3942 O OD1 . ASP B 1 247 ? 45.356 12.954 25.196 1.00 52.92 ? 247 ASP B OD1 1 ATOM 3943 O OD2 . ASP B 1 247 ? 44.429 12.156 23.368 1.00 54.33 ? 247 ASP B OD2 1 ATOM 3944 N N . LYS B 1 248 ? 42.743 17.274 24.212 1.00 47.36 ? 248 LYS B N 1 ATOM 3945 C CA . LYS B 1 248 ? 42.866 18.723 24.287 1.00 51.39 ? 248 LYS B CA 1 ATOM 3946 C C . LYS B 1 248 ? 41.512 19.351 24.587 1.00 53.09 ? 248 LYS B C 1 ATOM 3947 O O . LYS B 1 248 ? 40.476 18.711 24.414 1.00 53.05 ? 248 LYS B O 1 ATOM 3948 C CB . LYS B 1 248 ? 43.431 19.261 22.969 1.00 53.18 ? 248 LYS B CB 1 ATOM 3949 C CG . LYS B 1 248 ? 44.794 18.667 22.619 1.00 55.59 ? 248 LYS B CG 1 ATOM 3950 C CD . LYS B 1 248 ? 45.189 18.938 21.177 1.00 57.73 ? 248 LYS B CD 1 ATOM 3951 C CE . LYS B 1 248 ? 46.470 18.195 20.816 1.00 59.13 ? 248 LYS B CE 1 ATOM 3952 N NZ . LYS B 1 248 ? 46.815 18.334 19.371 1.00 60.51 ? 248 LYS B NZ 1 ATOM 3953 N N . ASP B 1 249 ? 41.522 20.601 25.041 1.00 55.54 ? 249 ASP B N 1 ATOM 3954 C CA . ASP B 1 249 ? 40.284 21.290 25.377 1.00 58.52 ? 249 ASP B CA 1 ATOM 3955 C C . ASP B 1 249 ? 39.398 21.464 24.149 1.00 60.67 ? 249 ASP B C 1 ATOM 3956 O O . ASP B 1 249 ? 39.800 22.079 23.162 1.00 60.66 ? 249 ASP B O 1 ATOM 3957 C CB . ASP B 1 249 ? 40.580 22.659 25.986 1.00 59.19 ? 249 ASP B CB 1 ATOM 3958 C CG . ASP B 1 249 ? 39.399 23.216 26.757 1.00 60.49 ? 249 ASP B CG 1 ATOM 3959 O OD1 . ASP B 1 249 ? 38.258 23.108 26.258 1.00 60.87 ? 249 ASP B OD1 1 ATOM 3960 O OD2 . ASP B 1 249 ? 39.610 23.763 27.861 1.00 61.51 ? 249 ASP B OD2 1 ATOM 3961 N N . PRO B 1 250 ? 38.174 20.919 24.197 1.00 63.14 ? 250 PRO B N 1 ATOM 3962 C CA . PRO B 1 250 ? 37.233 21.020 23.078 1.00 65.68 ? 250 PRO B CA 1 ATOM 3963 C C . PRO B 1 250 ? 36.457 22.340 23.055 1.00 67.99 ? 250 PRO B C 1 ATOM 3964 O O . PRO B 1 250 ? 36.233 22.964 24.097 1.00 68.26 ? 250 PRO B O 1 ATOM 3965 C CB . PRO B 1 250 ? 36.321 19.820 23.300 1.00 64.99 ? 250 PRO B CB 1 ATOM 3966 C CG . PRO B 1 250 ? 36.214 19.787 24.791 1.00 64.45 ? 250 PRO B CG 1 ATOM 3967 C CD . PRO B 1 250 ? 37.650 20.020 25.242 1.00 63.64 ? 250 PRO B CD 1 ATOM 3968 N N . LYS B 1 251 ? 36.053 22.755 21.857 1.00 70.14 ? 251 LYS B N 1 ATOM 3969 C CA . LYS B 1 251 ? 35.290 23.987 21.673 1.00 71.89 ? 251 LYS B CA 1 ATOM 3970 C C . LYS B 1 251 ? 35.095 24.266 20.188 1.00 72.15 ? 251 LYS B C 1 ATOM 3971 O O . LYS B 1 251 ? 36.023 23.915 19.428 1.00 72.44 ? 251 LYS B O 1 ATOM 3972 C CB . LYS B 1 251 ? 36.008 25.173 22.323 1.00 73.13 ? 251 LYS B CB 1 ATOM 3973 C CG . LYS B 1 251 ? 35.229 26.473 22.235 1.00 74.44 ? 251 LYS B CG 1 ATOM 3974 C CD . LYS B 1 251 ? 36.013 27.622 22.836 1.00 76.30 ? 251 LYS B CD 1 ATOM 3975 C CE . LYS B 1 251 ? 35.253 28.929 22.695 1.00 77.23 ? 251 LYS B CE 1 ATOM 3976 N NZ . LYS B 1 251 ? 36.030 30.074 23.244 1.00 77.91 ? 251 LYS B NZ 1 HETATM 3977 C C1 . NAG C 2 . ? 25.802 20.134 54.421 1.00 38.77 ? 410 NAG A C1 1 HETATM 3978 C C2 . NAG C 2 . ? 26.888 19.096 54.754 1.00 40.12 ? 410 NAG A C2 1 HETATM 3979 C C3 . NAG C 2 . ? 27.892 19.654 55.769 1.00 42.77 ? 410 NAG A C3 1 HETATM 3980 C C4 . NAG C 2 . ? 28.460 20.980 55.265 1.00 44.02 ? 410 NAG A C4 1 HETATM 3981 C C5 . NAG C 2 . ? 27.304 21.941 54.987 1.00 43.35 ? 410 NAG A C5 1 HETATM 3982 C C6 . NAG C 2 . ? 27.786 23.272 54.437 1.00 43.96 ? 410 NAG A C6 1 HETATM 3983 C C7 . NAG C 2 . ? 26.404 16.753 54.627 1.00 40.14 ? 410 NAG A C7 1 HETATM 3984 C C8 . NAG C 2 . ? 26.088 15.469 55.382 1.00 39.28 ? 410 NAG A C8 1 HETATM 3985 N N2 . NAG C 2 . ? 26.272 17.898 55.285 1.00 40.36 ? 410 NAG A N2 1 HETATM 3986 O O3 . NAG C 2 . ? 28.951 18.726 55.965 1.00 43.80 ? 410 NAG A O3 1 HETATM 3987 O O4 . NAG C 2 . ? 29.337 21.534 56.240 1.00 46.75 ? 410 NAG A O4 1 HETATM 3988 O O5 . NAG C 2 . ? 26.410 21.371 54.001 1.00 42.09 ? 410 NAG A O5 1 HETATM 3989 O O6 . NAG C 2 . ? 26.789 24.277 54.573 1.00 45.23 ? 410 NAG A O6 1 HETATM 3990 O O7 . NAG C 2 . ? 26.772 16.704 53.455 1.00 39.93 ? 410 NAG A O7 1 HETATM 3991 C C1 . NAG D 2 . ? 14.244 26.519 26.877 1.00 40.86 ? 411 NAG B C1 1 HETATM 3992 C C2 . NAG D 2 . ? 13.038 25.860 26.165 1.00 42.15 ? 411 NAG B C2 1 HETATM 3993 C C3 . NAG D 2 . ? 12.036 26.897 25.632 1.00 43.36 ? 411 NAG B C3 1 HETATM 3994 C C4 . NAG D 2 . ? 11.656 27.874 26.738 1.00 44.58 ? 411 NAG B C4 1 HETATM 3995 C C5 . NAG D 2 . ? 12.936 28.527 27.253 1.00 45.62 ? 411 NAG B C5 1 HETATM 3996 C C6 . NAG D 2 . ? 12.668 29.541 28.347 1.00 46.57 ? 411 NAG B C6 1 HETATM 3997 C C7 . NAG D 2 . ? 13.577 23.726 25.181 1.00 41.72 ? 411 NAG B C7 1 HETATM 3998 C C8 . NAG D 2 . ? 14.048 22.943 23.965 1.00 41.40 ? 411 NAG B C8 1 HETATM 3999 N N2 . NAG D 2 . ? 13.514 25.048 25.061 1.00 42.51 ? 411 NAG B N2 1 HETATM 4000 O O3 . NAG D 2 . ? 10.872 26.238 25.160 1.00 43.36 ? 411 NAG B O3 1 HETATM 4001 O O4 . NAG D 2 . ? 10.760 28.861 26.240 1.00 45.55 ? 411 NAG B O4 1 HETATM 4002 O O5 . NAG D 2 . ? 13.810 27.521 27.819 1.00 44.14 ? 411 NAG B O5 1 HETATM 4003 O O6 . NAG D 2 . ? 13.878 30.135 28.796 1.00 48.53 ? 411 NAG B O6 1 HETATM 4004 O O7 . NAG D 2 . ? 13.272 23.132 26.217 1.00 41.63 ? 411 NAG B O7 1 HETATM 4005 O O . HOH E 3 . ? 20.769 6.954 60.969 1.00 12.13 ? 801 HOH A O 1 HETATM 4006 O O . HOH E 3 . ? 21.234 9.619 60.022 1.00 12.27 ? 802 HOH A O 1 HETATM 4007 O O . HOH E 3 . ? 20.401 -2.705 34.492 1.00 13.16 ? 804 HOH A O 1 HETATM 4008 O O . HOH E 3 . ? 3.596 1.949 48.648 1.00 13.28 ? 805 HOH A O 1 HETATM 4009 O O . HOH E 3 . ? 28.707 3.078 32.145 1.00 14.60 ? 806 HOH A O 1 HETATM 4010 O O . HOH E 3 . ? 26.525 2.554 65.136 1.00 14.64 ? 807 HOH A O 1 HETATM 4011 O O . HOH E 3 . ? 7.748 4.960 32.278 1.00 14.76 ? 809 HOH A O 1 HETATM 4012 O O . HOH E 3 . ? 23.817 -10.074 63.464 1.00 14.98 ? 811 HOH A O 1 HETATM 4013 O O . HOH E 3 . ? 18.660 -14.162 66.836 1.00 14.98 ? 812 HOH A O 1 HETATM 4014 O O . HOH E 3 . ? 13.198 -18.997 67.330 1.00 15.17 ? 813 HOH A O 1 HETATM 4015 O O . HOH E 3 . ? 5.137 -3.118 45.386 1.00 15.49 ? 816 HOH A O 1 HETATM 4016 O O . HOH E 3 . ? 25.772 7.014 55.312 1.00 15.63 ? 817 HOH A O 1 HETATM 4017 O O . HOH E 3 . ? 19.345 1.779 36.529 1.00 15.89 ? 818 HOH A O 1 HETATM 4018 O O . HOH E 3 . ? 1.841 8.334 46.507 1.00 15.93 ? 819 HOH A O 1 HETATM 4019 O O . HOH E 3 . ? 30.525 2.238 56.733 1.00 16.16 ? 820 HOH A O 1 HETATM 4020 O O . HOH E 3 . ? 27.966 6.970 62.103 1.00 16.31 ? 821 HOH A O 1 HETATM 4021 O O . HOH E 3 . ? 23.089 3.601 36.856 1.00 16.89 ? 824 HOH A O 1 HETATM 4022 O O . HOH E 3 . ? 21.501 -15.848 56.000 1.00 16.95 ? 825 HOH A O 1 HETATM 4023 O O . HOH E 3 . ? 28.848 4.762 35.034 1.00 17.76 ? 828 HOH A O 1 HETATM 4024 O O . HOH E 3 . ? 19.246 -4.496 70.333 1.00 17.98 ? 829 HOH A O 1 HETATM 4025 O O . HOH E 3 . ? 33.451 -1.301 39.628 1.00 18.07 ? 830 HOH A O 1 HETATM 4026 O O . HOH E 3 . ? 34.583 0.928 48.726 1.00 18.30 ? 832 HOH A O 1 HETATM 4027 O O . HOH E 3 . ? 12.312 3.260 64.012 1.00 18.37 ? 833 HOH A O 1 HETATM 4028 O O . HOH E 3 . ? 28.429 -8.748 41.862 1.00 18.83 ? 835 HOH A O 1 HETATM 4029 O O . HOH E 3 . ? 17.726 3.966 69.137 1.00 19.04 ? 836 HOH A O 1 HETATM 4030 O O . HOH E 3 . ? 29.403 9.895 64.152 1.00 19.30 ? 837 HOH A O 1 HETATM 4031 O O . HOH E 3 . ? 0.397 0.581 43.041 1.00 19.53 ? 841 HOH A O 1 HETATM 4032 O O . HOH E 3 . ? 8.868 12.156 53.436 1.00 19.94 ? 843 HOH A O 1 HETATM 4033 O O . HOH E 3 . ? 13.945 7.613 58.898 1.00 20.30 ? 846 HOH A O 1 HETATM 4034 O O . HOH E 3 . ? 20.290 12.574 66.707 1.00 20.66 ? 847 HOH A O 1 HETATM 4035 O O . HOH E 3 . ? 14.568 -9.401 71.760 1.00 20.55 ? 848 HOH A O 1 HETATM 4036 O O . HOH E 3 . ? 0.156 17.405 44.112 1.00 20.91 ? 849 HOH A O 1 HETATM 4037 O O . HOH E 3 . ? 17.779 28.540 49.678 1.00 20.96 ? 850 HOH A O 1 HETATM 4038 O O . HOH E 3 . ? 19.968 5.341 36.932 1.00 21.14 ? 851 HOH A O 1 HETATM 4039 O O . HOH E 3 . ? 18.714 -6.282 35.941 1.00 21.39 ? 853 HOH A O 1 HETATM 4040 O O . HOH E 3 . ? 30.435 1.076 30.986 1.00 21.89 ? 857 HOH A O 1 HETATM 4041 O O . HOH E 3 . ? -1.478 19.355 39.537 1.00 21.90 ? 859 HOH A O 1 HETATM 4042 O O . HOH E 3 . ? 8.788 19.668 52.808 1.00 21.91 ? 860 HOH A O 1 HETATM 4043 O O . HOH E 3 . ? 8.065 -11.601 47.238 1.00 22.17 ? 862 HOH A O 1 HETATM 4044 O O . HOH E 3 . ? 14.817 18.600 52.867 1.00 22.17 ? 863 HOH A O 1 HETATM 4045 O O . HOH E 3 . ? 7.726 -5.930 38.184 1.00 22.72 ? 865 HOH A O 1 HETATM 4046 O O . HOH E 3 . ? 7.517 -9.921 45.026 1.00 22.84 ? 867 HOH A O 1 HETATM 4047 O O . HOH E 3 . ? 6.134 18.404 35.775 1.00 23.12 ? 868 HOH A O 1 HETATM 4048 O O . HOH E 3 . ? 13.172 -17.713 44.846 1.00 23.28 ? 869 HOH A O 1 HETATM 4049 O O . HOH E 3 . ? 24.540 -13.541 47.229 1.00 23.18 ? 870 HOH A O 1 HETATM 4050 O O . HOH E 3 . ? 30.656 -0.869 56.920 1.00 23.30 ? 871 HOH A O 1 HETATM 4051 O O . HOH E 3 . ? 15.818 16.930 54.883 1.00 23.58 ? 876 HOH A O 1 HETATM 4052 O O . HOH E 3 . ? 13.955 7.354 53.671 1.00 24.01 ? 878 HOH A O 1 HETATM 4053 O O . HOH E 3 . ? 28.667 7.937 65.759 1.00 24.02 ? 881 HOH A O 1 HETATM 4054 O O . HOH E 3 . ? 34.556 3.850 41.858 1.00 24.22 ? 882 HOH A O 1 HETATM 4055 O O . HOH E 3 . ? -0.989 9.801 39.560 1.00 24.45 ? 883 HOH A O 1 HETATM 4056 O O . HOH E 3 . ? 25.374 13.083 48.267 1.00 24.47 ? 884 HOH A O 1 HETATM 4057 O O . HOH E 3 . ? 19.493 -12.654 41.993 1.00 24.88 ? 885 HOH A O 1 HETATM 4058 O O . HOH E 3 . ? 36.272 -9.004 44.867 1.00 24.79 ? 888 HOH A O 1 HETATM 4059 O O . HOH E 3 . ? 1.234 -7.104 62.344 1.00 25.01 ? 890 HOH A O 1 HETATM 4060 O O . HOH E 3 . ? 30.658 -9.260 67.799 1.00 25.02 ? 891 HOH A O 1 HETATM 4061 O O . HOH E 3 . ? 24.945 -5.295 31.876 1.00 25.22 ? 892 HOH A O 1 HETATM 4062 O O . HOH E 3 . ? 10.189 -18.481 56.186 1.00 25.50 ? 893 HOH A O 1 HETATM 4063 O O . HOH E 3 . ? 0.389 -12.841 67.459 1.00 25.49 ? 895 HOH A O 1 HETATM 4064 O O . HOH E 3 . ? 14.536 -19.149 57.552 1.00 25.96 ? 897 HOH A O 1 HETATM 4065 O O . HOH E 3 . ? 30.826 -6.218 35.413 1.00 26.50 ? 898 HOH A O 1 HETATM 4066 O O . HOH E 3 . ? 30.558 4.882 47.263 1.00 26.61 ? 901 HOH A O 1 HETATM 4067 O O . HOH E 3 . ? 28.614 4.393 61.237 1.00 27.05 ? 902 HOH A O 1 HETATM 4068 O O . HOH E 3 . ? 27.894 -2.159 71.096 1.00 27.56 ? 904 HOH A O 1 HETATM 4069 O O . HOH E 3 . ? 2.476 2.147 51.334 1.00 27.56 ? 905 HOH A O 1 HETATM 4070 O O . HOH E 3 . ? 12.484 -14.617 42.815 1.00 27.68 ? 906 HOH A O 1 HETATM 4071 O O . HOH E 3 . ? 14.991 17.519 36.006 1.00 27.53 ? 907 HOH A O 1 HETATM 4072 O O . HOH E 3 . ? 34.434 -12.257 60.341 1.00 28.30 ? 909 HOH A O 1 HETATM 4073 O O . HOH E 3 . ? 11.853 7.185 64.465 1.00 28.27 ? 910 HOH A O 1 HETATM 4074 O O . HOH E 3 . ? 2.636 -13.839 60.235 1.00 28.14 ? 911 HOH A O 1 HETATM 4075 O O . HOH E 3 . ? 11.211 -15.866 55.365 1.00 28.23 ? 913 HOH A O 1 HETATM 4076 O O . HOH E 3 . ? 15.630 20.686 54.008 1.00 28.93 ? 917 HOH A O 1 HETATM 4077 O O . HOH E 3 . ? 12.862 -5.038 71.346 1.00 29.67 ? 918 HOH A O 1 HETATM 4078 O O . HOH E 3 . ? 10.208 9.147 53.532 1.00 29.24 ? 920 HOH A O 1 HETATM 4079 O O . HOH E 3 . ? 26.013 -10.411 42.451 1.00 29.14 ? 922 HOH A O 1 HETATM 4080 O O . HOH E 3 . ? 2.016 -5.146 64.913 1.00 29.63 ? 924 HOH A O 1 HETATM 4081 O O . HOH E 3 . ? 18.109 14.522 58.347 1.00 29.65 ? 925 HOH A O 1 HETATM 4082 O O . HOH E 3 . ? -1.144 3.041 36.531 1.00 29.74 ? 926 HOH A O 1 HETATM 4083 O O . HOH E 3 . ? 18.015 30.479 48.193 1.00 29.90 ? 927 HOH A O 1 HETATM 4084 O O . HOH E 3 . ? 37.966 6.275 49.169 1.00 30.21 ? 930 HOH A O 1 HETATM 4085 O O . HOH E 3 . ? 8.502 -18.067 63.697 1.00 30.25 ? 931 HOH A O 1 HETATM 4086 O O . HOH E 3 . ? 32.427 5.287 58.172 1.00 30.24 ? 933 HOH A O 1 HETATM 4087 O O . HOH E 3 . ? 26.821 15.314 45.632 1.00 30.49 ? 935 HOH A O 1 HETATM 4088 O O . HOH E 3 . ? 21.970 13.503 62.336 1.00 30.88 ? 936 HOH A O 1 HETATM 4089 O O . HOH E 3 . ? 34.138 1.295 39.613 1.00 30.62 ? 938 HOH A O 1 HETATM 4090 O O . HOH E 3 . ? 29.883 -13.600 47.881 1.00 30.67 ? 939 HOH A O 1 HETATM 4091 O O . HOH E 3 . ? 18.415 27.045 45.880 1.00 30.82 ? 940 HOH A O 1 HETATM 4092 O O . HOH E 3 . ? 30.096 -10.627 41.157 1.00 31.68 ? 941 HOH A O 1 HETATM 4093 O O . HOH E 3 . ? -0.120 9.414 35.496 1.00 31.86 ? 943 HOH A O 1 HETATM 4094 O O . HOH E 3 . ? 29.679 -1.515 59.424 1.00 31.72 ? 945 HOH A O 1 HETATM 4095 O O . HOH E 3 . ? 24.031 -8.397 39.999 1.00 32.19 ? 946 HOH A O 1 HETATM 4096 O O . HOH E 3 . ? 21.393 -9.570 41.063 1.00 31.98 ? 948 HOH A O 1 HETATM 4097 O O . HOH E 3 . ? 25.887 -17.105 71.181 1.00 32.26 ? 951 HOH A O 1 HETATM 4098 O O . HOH E 3 . ? 18.781 -14.784 45.651 1.00 32.04 ? 952 HOH A O 1 HETATM 4099 O O . HOH E 3 . ? 32.506 11.325 50.982 1.00 33.24 ? 955 HOH A O 1 HETATM 4100 O O . HOH E 3 . ? -4.512 17.647 43.127 1.00 32.94 ? 957 HOH A O 1 HETATM 4101 O O . HOH E 3 . ? 35.068 -5.469 43.370 1.00 33.90 ? 959 HOH A O 1 HETATM 4102 O O . HOH E 3 . ? -4.097 20.582 38.161 1.00 33.66 ? 960 HOH A O 1 HETATM 4103 O O . HOH E 3 . ? 30.354 -0.344 63.839 1.00 34.05 ? 962 HOH A O 1 HETATM 4104 O O . HOH E 3 . ? -0.881 18.384 49.647 1.00 34.19 ? 963 HOH A O 1 HETATM 4105 O O . HOH E 3 . ? 23.204 -8.118 73.435 1.00 35.55 ? 966 HOH A O 1 HETATM 4106 O O . HOH E 3 . ? -2.164 16.821 46.750 1.00 35.06 ? 967 HOH A O 1 HETATM 4107 O O . HOH E 3 . ? 30.753 11.880 44.271 1.00 35.48 ? 969 HOH A O 1 HETATM 4108 O O . HOH E 3 . ? 24.774 -16.525 57.122 1.00 36.44 ? 973 HOH A O 1 HETATM 4109 O O . HOH E 3 . ? 5.283 -4.833 38.481 1.00 36.90 ? 974 HOH A O 1 HETATM 4110 O O . HOH E 3 . ? 5.073 -0.105 37.160 1.00 37.03 ? 976 HOH A O 1 HETATM 4111 O O . HOH E 3 . ? 28.116 9.597 40.814 1.00 38.51 ? 982 HOH A O 1 HETATM 4112 O O . HOH E 3 . ? 0.062 -11.938 63.392 1.00 39.66 ? 984 HOH A O 1 HETATM 4113 O O . HOH E 3 . ? 17.433 13.432 63.461 1.00 40.18 ? 985 HOH A O 1 HETATM 4114 O O . HOH E 3 . ? -2.266 22.810 38.611 1.00 41.15 ? 988 HOH A O 1 HETATM 4115 O O . HOH E 3 . ? 17.069 23.084 58.617 1.00 39.93 ? 989 HOH A O 1 HETATM 4116 O O . HOH E 3 . ? -2.040 19.247 42.615 1.00 41.72 ? 990 HOH A O 1 HETATM 4117 O O . HOH E 3 . ? 17.715 -15.091 42.966 1.00 44.40 ? 995 HOH A O 1 HETATM 4118 O O . HOH E 3 . ? 24.184 3.716 71.791 1.00 45.57 ? 996 HOH A O 1 HETATM 4119 O O . HOH E 3 . ? 13.248 8.479 55.927 1.00 45.90 ? 997 HOH A O 1 HETATM 4120 O O . HOH E 3 . ? 20.873 -18.987 71.947 1.00 46.73 ? 999 HOH A O 1 HETATM 4121 O O . HOH F 3 . ? 12.027 1.096 38.936 1.00 12.42 ? 803 HOH B O 1 HETATM 4122 O O . HOH F 3 . ? 11.715 4.034 37.091 1.00 14.77 ? 808 HOH B O 1 HETATM 4123 O O . HOH F 3 . ? 21.253 2.204 34.526 1.00 14.72 ? 810 HOH B O 1 HETATM 4124 O O . HOH F 3 . ? 19.579 17.771 15.134 1.00 15.35 ? 814 HOH B O 1 HETATM 4125 O O . HOH F 3 . ? 7.249 0.262 30.295 1.00 15.41 ? 815 HOH B O 1 HETATM 4126 O O . HOH F 3 . ? 17.747 3.751 35.007 1.00 16.48 ? 822 HOH B O 1 HETATM 4127 O O . HOH F 3 . ? 32.705 3.602 39.885 1.00 16.87 ? 823 HOH B O 1 HETATM 4128 O O . HOH F 3 . ? 10.384 -1.072 39.081 1.00 17.35 ? 826 HOH B O 1 HETATM 4129 O O . HOH F 3 . ? 35.675 2.133 24.673 1.00 17.62 ? 827 HOH B O 1 HETATM 4130 O O . HOH F 3 . ? 18.932 19.571 16.974 1.00 18.21 ? 831 HOH B O 1 HETATM 4131 O O . HOH F 3 . ? 17.077 3.669 5.262 1.00 18.84 ? 834 HOH B O 1 HETATM 4132 O O . HOH F 3 . ? 37.028 8.246 23.901 1.00 19.59 ? 838 HOH B O 1 HETATM 4133 O O . HOH F 3 . ? 38.503 13.166 28.688 1.00 19.44 ? 839 HOH B O 1 HETATM 4134 O O . HOH F 3 . ? 22.612 1.827 0.433 1.00 19.60 ? 840 HOH B O 1 HETATM 4135 O O . HOH F 3 . ? 40.336 4.858 28.437 1.00 19.69 ? 842 HOH B O 1 HETATM 4136 O O . HOH F 3 . ? 24.410 24.131 25.185 1.00 20.20 ? 844 HOH B O 1 HETATM 4137 O O . HOH F 3 . ? 16.041 -6.105 35.678 1.00 20.37 ? 845 HOH B O 1 HETATM 4138 O O . HOH F 3 . ? 45.058 19.390 35.273 1.00 21.47 ? 852 HOH B O 1 HETATM 4139 O O . HOH F 3 . ? 25.727 17.915 6.958 1.00 21.70 ? 854 HOH B O 1 HETATM 4140 O O . HOH F 3 . ? 14.469 15.112 20.254 1.00 21.85 ? 855 HOH B O 1 HETATM 4141 O O . HOH F 3 . ? 9.998 11.149 16.633 1.00 21.77 ? 856 HOH B O 1 HETATM 4142 O O . HOH F 3 . ? 6.094 6.279 30.548 1.00 21.75 ? 858 HOH B O 1 HETATM 4143 O O . HOH F 3 . ? 12.228 17.702 13.995 1.00 22.27 ? 861 HOH B O 1 HETATM 4144 O O . HOH F 3 . ? 6.114 6.149 23.172 1.00 22.51 ? 864 HOH B O 1 HETATM 4145 O O . HOH F 3 . ? 25.217 24.735 27.717 1.00 22.87 ? 866 HOH B O 1 HETATM 4146 O O . HOH F 3 . ? 13.580 15.339 9.205 1.00 23.41 ? 872 HOH B O 1 HETATM 4147 O O . HOH F 3 . ? 30.879 26.017 28.518 1.00 23.38 ? 873 HOH B O 1 HETATM 4148 O O . HOH F 3 . ? 26.503 15.226 21.942 1.00 23.66 ? 874 HOH B O 1 HETATM 4149 O O . HOH F 3 . ? 23.101 18.829 6.643 1.00 23.52 ? 875 HOH B O 1 HETATM 4150 O O . HOH F 3 . ? 40.250 19.997 34.677 1.00 23.82 ? 877 HOH B O 1 HETATM 4151 O O . HOH F 3 . ? 26.355 17.756 17.215 1.00 23.94 ? 879 HOH B O 1 HETATM 4152 O O . HOH F 3 . ? 12.801 -5.218 24.926 1.00 24.12 ? 880 HOH B O 1 HETATM 4153 O O . HOH F 3 . ? 22.193 -5.241 31.610 1.00 24.64 ? 886 HOH B O 1 HETATM 4154 O O . HOH F 3 . ? 16.677 -6.927 17.699 1.00 24.80 ? 887 HOH B O 1 HETATM 4155 O O . HOH F 3 . ? 41.687 19.516 39.770 1.00 25.09 ? 889 HOH B O 1 HETATM 4156 O O . HOH F 3 . ? 16.198 21.802 18.129 1.00 25.24 ? 894 HOH B O 1 HETATM 4157 O O . HOH F 3 . ? 31.286 19.528 24.591 1.00 25.42 ? 896 HOH B O 1 HETATM 4158 O O . HOH F 3 . ? 10.133 8.454 14.953 1.00 26.88 ? 899 HOH B O 1 HETATM 4159 O O . HOH F 3 . ? 34.389 17.008 42.825 1.00 26.63 ? 900 HOH B O 1 HETATM 4160 O O . HOH F 3 . ? 21.975 23.642 20.926 1.00 27.36 ? 903 HOH B O 1 HETATM 4161 O O . HOH F 3 . ? 8.212 -3.740 36.474 1.00 27.99 ? 908 HOH B O 1 HETATM 4162 O O . HOH F 3 . ? 21.814 -8.435 23.134 1.00 28.63 ? 912 HOH B O 1 HETATM 4163 O O . HOH F 3 . ? 32.685 -4.971 19.117 1.00 28.70 ? 914 HOH B O 1 HETATM 4164 O O . HOH F 3 . ? 6.514 -1.743 15.252 1.00 28.71 ? 915 HOH B O 1 HETATM 4165 O O . HOH F 3 . ? 11.744 15.046 13.754 1.00 28.73 ? 916 HOH B O 1 HETATM 4166 O O . HOH F 3 . ? 28.480 16.335 10.937 1.00 29.31 ? 919 HOH B O 1 HETATM 4167 O O . HOH F 3 . ? 11.478 20.227 10.814 1.00 29.58 ? 921 HOH B O 1 HETATM 4168 O O . HOH F 3 . ? 33.176 -3.510 29.982 1.00 29.22 ? 923 HOH B O 1 HETATM 4169 O O . HOH F 3 . ? 24.114 27.409 27.977 1.00 29.94 ? 928 HOH B O 1 HETATM 4170 O O . HOH F 3 . ? 43.955 14.073 35.747 1.00 29.82 ? 929 HOH B O 1 HETATM 4171 O O . HOH F 3 . ? 3.174 6.858 22.932 1.00 30.06 ? 932 HOH B O 1 HETATM 4172 O O . HOH F 3 . ? 21.646 18.612 4.374 1.00 30.41 ? 934 HOH B O 1 HETATM 4173 O O . HOH F 3 . ? 27.017 17.033 20.086 1.00 31.26 ? 937 HOH B O 1 HETATM 4174 O O . HOH F 3 . ? 19.951 -5.024 9.322 1.00 32.04 ? 942 HOH B O 1 HETATM 4175 O O . HOH F 3 . ? 14.956 -6.599 23.724 1.00 31.90 ? 944 HOH B O 1 HETATM 4176 O O . HOH F 3 . ? 33.200 -4.480 21.824 1.00 32.09 ? 947 HOH B O 1 HETATM 4177 O O . HOH F 3 . ? 3.833 0.855 23.961 1.00 32.03 ? 949 HOH B O 1 HETATM 4178 O O . HOH F 3 . ? 42.358 4.545 26.359 1.00 32.39 ? 950 HOH B O 1 HETATM 4179 O O . HOH F 3 . ? 16.901 -5.716 26.731 1.00 32.99 ? 953 HOH B O 1 HETATM 4180 O O . HOH F 3 . ? 5.796 -1.568 24.800 1.00 33.04 ? 954 HOH B O 1 HETATM 4181 O O . HOH F 3 . ? 13.948 24.444 34.849 1.00 33.33 ? 956 HOH B O 1 HETATM 4182 O O . HOH F 3 . ? 8.553 14.073 16.472 1.00 33.62 ? 958 HOH B O 1 HETATM 4183 O O . HOH F 3 . ? 11.131 21.434 13.681 1.00 34.24 ? 961 HOH B O 1 HETATM 4184 O O . HOH F 3 . ? 35.505 -3.524 21.577 1.00 34.16 ? 964 HOH B O 1 HETATM 4185 O O . HOH F 3 . ? 24.061 16.070 40.073 1.00 34.56 ? 965 HOH B O 1 HETATM 4186 O O . HOH F 3 . ? 19.686 -5.935 25.386 1.00 35.29 ? 968 HOH B O 1 HETATM 4187 O O . HOH F 3 . ? 27.616 6.300 -1.958 1.00 35.27 ? 970 HOH B O 1 HETATM 4188 O O . HOH F 3 . ? 9.955 14.325 31.887 1.00 35.76 ? 971 HOH B O 1 HETATM 4189 O O . HOH F 3 . ? 15.684 -6.896 30.555 1.00 36.20 ? 972 HOH B O 1 HETATM 4190 O O . HOH F 3 . ? 24.450 19.262 36.727 1.00 37.39 ? 975 HOH B O 1 HETATM 4191 O O . HOH F 3 . ? 26.623 28.472 38.567 1.00 37.63 ? 977 HOH B O 1 HETATM 4192 O O . HOH F 3 . ? 30.871 -6.833 7.083 1.00 37.80 ? 978 HOH B O 1 HETATM 4193 O O . HOH F 3 . ? 8.042 16.900 26.348 1.00 38.28 ? 979 HOH B O 1 HETATM 4194 O O . HOH F 3 . ? 10.970 -7.189 24.838 1.00 37.91 ? 980 HOH B O 1 HETATM 4195 O O . HOH F 3 . ? 36.001 1.148 32.632 1.00 38.02 ? 981 HOH B O 1 HETATM 4196 O O . HOH F 3 . ? 29.549 -5.449 10.150 1.00 39.48 ? 983 HOH B O 1 HETATM 4197 O O . HOH F 3 . ? 11.438 -7.847 17.571 1.00 39.76 ? 986 HOH B O 1 HETATM 4198 O O . HOH F 3 . ? 41.843 3.955 35.432 1.00 39.84 ? 987 HOH B O 1 HETATM 4199 O O . HOH F 3 . ? 5.401 15.782 22.236 1.00 42.58 ? 991 HOH B O 1 HETATM 4200 O O . HOH F 3 . ? 28.751 19.738 20.823 1.00 42.98 ? 992 HOH B O 1 HETATM 4201 O O . HOH F 3 . ? 41.651 21.183 37.235 1.00 43.28 ? 993 HOH B O 1 HETATM 4202 O O . HOH F 3 . ? 16.118 -8.434 22.386 1.00 43.05 ? 994 HOH B O 1 HETATM 4203 O O . HOH F 3 . ? 11.490 20.920 22.773 1.00 46.89 ? 998 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLY 1 1 1 GLY GLY A . n A 1 2 LEU 2 2 2 LEU LEU A . n A 1 3 ASP 3 3 3 ASP ASP A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 VAL 5 5 5 VAL VAL A . n A 1 6 SER 6 6 6 SER SER A . n A 1 7 PHE 7 7 7 PHE PHE A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 LYS 10 10 10 LYS LYS A . n A 1 11 GLY 11 11 11 GLY GLY A . n A 1 12 ALA 12 12 12 ALA ALA A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 TYR 14 14 14 TYR TYR A . n A 1 15 ILE 15 15 15 ILE ILE A . n A 1 16 THR 16 16 16 THR THR A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 VAL 18 18 18 VAL VAL A . n A 1 19 ASN 19 19 19 ASN ASN A . n A 1 20 PHE 20 20 20 PHE PHE A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 GLU 23 23 23 GLU GLU A . n A 1 24 LEU 24 24 24 LEU LEU A . n A 1 25 ARG 25 25 25 ARG ARG A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 LYS 27 27 27 LYS LYS A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 LYS 29 29 29 LYS LYS A . n A 1 30 PRO 30 30 30 PRO PRO A . n A 1 31 GLU 31 31 31 GLU GLU A . n A 1 32 GLY 32 32 32 GLY GLY A . n A 1 33 ASN 33 33 33 ASN ASN A . n A 1 34 SER 34 34 34 SER SER A . n A 1 35 HIS 35 35 35 HIS HIS A . n A 1 36 GLY 36 36 36 GLY GLY A . n A 1 37 ILE 37 37 37 ILE ILE A . n A 1 38 PRO 38 38 38 PRO PRO A . n A 1 39 LEU 39 39 39 LEU LEU A . n A 1 40 LEU 40 40 40 LEU LEU A . n A 1 41 ARG 41 41 41 ARG ARG A . n A 1 42 LYS 42 42 42 LYS LYS A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 CYS 44 44 44 CYS CYS A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 PRO 47 47 47 PRO PRO A . n A 1 48 GLY 48 48 48 GLY GLY A . n A 1 49 LYS 49 49 49 LYS LYS A . n A 1 50 CYS 50 50 50 CYS CYS A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 VAL 52 52 52 VAL VAL A . n A 1 53 LEU 53 53 53 LEU LEU A . n A 1 54 VAL 54 54 54 VAL VAL A . n A 1 55 ALA 55 55 55 ALA ALA A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 ASN 58 58 58 ASN ASN A . n A 1 59 ASP 59 59 59 ASP ASP A . n A 1 60 ASN 60 60 60 ASN ASN A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLN 62 62 62 GLN GLN A . n A 1 63 LEU 63 63 63 LEU LEU A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 ALA 67 67 67 ALA ALA A . n A 1 68 ILE 68 68 68 ILE ILE A . n A 1 69 ASP 69 69 69 ASP ASP A . n A 1 70 VAL 70 70 70 VAL VAL A . n A 1 71 THR 71 71 71 THR THR A . n A 1 72 SER 72 72 72 SER SER A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 TYR 74 74 74 TYR TYR A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 VAL 76 76 76 VAL VAL A . n A 1 77 GLY 77 77 77 GLY GLY A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 GLN 79 79 79 GLN GLN A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 ASN 82 82 82 ASN ASN A . n A 1 83 ARG 83 83 83 ARG ARG A . n A 1 84 SER 84 84 84 SER SER A . n A 1 85 TYR 85 85 85 TYR TYR A . n A 1 86 PHE 86 86 86 PHE PHE A . n A 1 87 PHE 87 87 87 PHE PHE A . n A 1 88 LYS 88 88 88 LYS LYS A . n A 1 89 ASP 89 89 89 ASP ASP A . n A 1 90 ALA 90 90 90 ALA ALA A . n A 1 91 PRO 91 91 91 PRO PRO A . n A 1 92 ASP 92 92 92 ASP ASP A . n A 1 93 ALA 93 93 93 ALA ALA A . n A 1 94 ALA 94 94 94 ALA ALA A . n A 1 95 TYR 95 95 95 TYR TYR A . n A 1 96 GLU 96 96 96 GLU GLU A . n A 1 97 GLY 97 97 97 GLY GLY A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 PHE 99 99 99 PHE PHE A . n A 1 100 LYS 100 100 100 LYS LYS A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 THR 102 102 102 THR THR A . n A 1 103 ILE 103 103 103 ILE ILE A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 THR 105 105 105 THR THR A . n A 1 106 ARG 106 106 106 ARG ARG A . n A 1 107 LEU 107 107 107 LEU LEU A . n A 1 108 HIS 108 108 108 HIS HIS A . n A 1 109 PHE 109 109 109 PHE PHE A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 GLY 111 111 111 GLY GLY A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 TYR 113 113 113 TYR TYR A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 LEU 116 116 116 LEU LEU A . n A 1 117 GLU 117 117 117 GLU GLU A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 LYS 120 120 120 LYS LYS A . n A 1 121 ALA 121 121 121 ALA ALA A . n A 1 122 TYR 122 122 122 TYR TYR A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 THR 125 125 125 THR THR A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 ASP 127 127 127 ASP ASP A . n A 1 128 LEU 128 128 128 LEU LEU A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 ILE 130 130 130 ILE ILE A . n A 1 131 GLU 131 131 131 GLU GLU A . n A 1 132 PRO 132 132 132 PRO PRO A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 ARG 134 134 134 ARG ARG A . n A 1 135 ILE 135 135 135 ILE ILE A . n A 1 136 GLY 136 136 136 GLY GLY A . n A 1 137 ILE 137 137 137 ILE ILE A . n A 1 138 LYS 138 138 138 LYS LYS A . n A 1 139 LYS 139 139 139 LYS LYS A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 ASP 141 141 141 ASP ASP A . n A 1 142 GLU 142 142 142 GLU GLU A . n A 1 143 ASN 143 143 143 ASN ASN A . n A 1 144 ALA 144 144 144 ALA ALA A . n A 1 145 ILE 145 145 145 ILE ILE A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 TYR 148 148 148 TYR TYR A . n A 1 149 LYS 149 149 149 LYS LYS A . n A 1 150 PRO 150 150 150 PRO PRO A . n A 1 151 THR 151 151 151 THR THR A . n A 1 152 GLU 152 152 152 GLU GLU A . n A 1 153 ILE 153 153 153 ILE ILE A . n A 1 154 ALA 154 154 154 ALA ALA A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 LEU 157 157 157 LEU LEU A . n A 1 158 LEU 158 158 158 LEU LEU A . n A 1 159 VAL 159 159 159 VAL VAL A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 GLN 162 162 162 GLN GLN A . n A 1 163 MET 163 163 163 MET MET A . n A 1 164 VAL 164 164 164 VAL VAL A . n A 1 165 SER 165 165 165 SER SER A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 ALA 167 167 167 ALA ALA A . n A 1 168 ALA 168 168 168 ALA ALA A . n A 1 169 ARG 169 169 169 ARG ARG A . n A 1 170 PHE 170 170 170 PHE PHE A . n A 1 171 THR 171 171 171 THR THR A . n A 1 172 PHE 172 172 172 PHE PHE A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 GLU 174 174 174 GLU GLU A . n A 1 175 ASN 175 175 175 ASN ASN A . n A 1 176 GLN 176 176 176 GLN GLN A . n A 1 177 ILE 177 177 177 ILE ILE A . n A 1 178 ARG 178 178 178 ARG ARG A . n A 1 179 ASN 179 179 179 ASN ASN A . n A 1 180 ASN 180 180 180 ASN ASN A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 GLN 183 183 183 GLN GLN A . n A 1 184 ARG 184 184 184 ARG ARG A . n A 1 185 ILE 185 185 185 ILE ILE A . n A 1 186 ARG 186 186 186 ARG ARG A . n A 1 187 PRO 187 187 187 PRO PRO A . n A 1 188 ALA 188 188 188 ALA ALA A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ASN 190 190 190 ASN ASN A . n A 1 191 THR 191 191 191 THR THR A . n A 1 192 ILE 192 192 192 ILE ILE A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 GLU 195 195 195 GLU GLU A . n A 1 196 ASN 196 196 196 ASN ASN A . n A 1 197 LYS 197 197 197 LYS LYS A . n A 1 198 TRP 198 198 198 TRP TRP A . n A 1 199 GLY 199 199 199 GLY GLY A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 SER 202 202 202 SER SER A . n A 1 203 PHE 203 203 203 PHE PHE A . n A 1 204 GLN 204 204 204 GLN GLN A . n A 1 205 ILE 205 205 205 ILE ILE A . n A 1 206 ARG 206 206 206 ARG ARG A . n A 1 207 THR 207 207 207 THR THR A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 GLY 209 209 209 GLY GLY A . n A 1 210 ALA 210 210 210 ALA ALA A . n A 1 211 ASN 211 211 211 ASN ASN A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 MET 213 213 213 MET MET A . n A 1 214 PHE 214 214 214 PHE PHE A . n A 1 215 SER 215 215 215 SER SER A . n A 1 216 GLU 216 216 216 GLU GLU A . n A 1 217 ALA 217 217 217 ALA ALA A . n A 1 218 VAL 218 218 218 VAL VAL A . n A 1 219 GLU 219 219 219 GLU GLU A . n A 1 220 LEU 220 220 220 LEU LEU A . n A 1 221 GLU 221 221 221 GLU GLU A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 ASN 224 224 224 ASN ASN A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 LYS 226 226 226 LYS LYS A . n A 1 227 LYS 227 227 227 LYS LYS A . n A 1 228 TYR 228 228 228 TYR TYR A . n A 1 229 TYR 229 229 229 TYR TYR A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ALA 232 232 232 ALA ALA A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 ASP 234 234 234 ASP ASP A . n A 1 235 GLN 235 235 235 GLN GLN A . n A 1 236 VAL 236 236 236 VAL VAL A . n A 1 237 LYS 237 237 237 LYS LYS A . n A 1 238 PRO 238 238 238 PRO PRO A . n A 1 239 LYS 239 239 239 LYS LYS A . n A 1 240 ILE 240 240 240 ILE ILE A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 LEU 243 243 243 LEU LEU A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 PHE 245 245 245 PHE PHE A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 ASP 247 247 247 ASP ASP A . n A 1 248 LYS 248 248 248 LYS LYS A . n A 1 249 ASP 249 249 249 ASP ASP A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 LYS 251 251 251 LYS LYS A . n B 1 1 GLY 1 1 1 GLY GLY B . n B 1 2 LEU 2 2 2 LEU LEU B . n B 1 3 ASP 3 3 3 ASP ASP B . n B 1 4 THR 4 4 4 THR THR B . n B 1 5 VAL 5 5 5 VAL VAL B . n B 1 6 SER 6 6 6 SER SER B . n B 1 7 PHE 7 7 7 PHE PHE B . n B 1 8 SER 8 8 8 SER SER B . n B 1 9 THR 9 9 9 THR THR B . n B 1 10 LYS 10 10 10 LYS LYS B . n B 1 11 GLY 11 11 11 GLY GLY B . n B 1 12 ALA 12 12 12 ALA ALA B . n B 1 13 THR 13 13 13 THR THR B . n B 1 14 TYR 14 14 14 TYR TYR B . n B 1 15 ILE 15 15 15 ILE ILE B . n B 1 16 THR 16 16 16 THR THR B . n B 1 17 TYR 17 17 17 TYR TYR B . n B 1 18 VAL 18 18 18 VAL VAL B . n B 1 19 ASN 19 19 19 ASN ASN B . n B 1 20 PHE 20 20 20 PHE PHE B . n B 1 21 LEU 21 21 21 LEU LEU B . n B 1 22 ASN 22 22 22 ASN ASN B . n B 1 23 GLU 23 23 23 GLU GLU B . n B 1 24 LEU 24 24 24 LEU LEU B . n B 1 25 ARG 25 25 25 ARG ARG B . n B 1 26 VAL 26 26 26 VAL VAL B . n B 1 27 LYS 27 27 27 LYS LYS B . n B 1 28 LEU 28 28 28 LEU LEU B . n B 1 29 LYS 29 29 29 LYS LYS B . n B 1 30 PRO 30 30 30 PRO PRO B . n B 1 31 GLU 31 31 31 GLU GLU B . n B 1 32 GLY 32 32 32 GLY GLY B . n B 1 33 ASN 33 33 33 ASN ASN B . n B 1 34 SER 34 34 34 SER SER B . n B 1 35 HIS 35 35 35 HIS HIS B . n B 1 36 GLY 36 36 36 GLY GLY B . n B 1 37 ILE 37 37 37 ILE ILE B . n B 1 38 PRO 38 38 38 PRO PRO B . n B 1 39 LEU 39 39 39 LEU LEU B . n B 1 40 LEU 40 40 40 LEU LEU B . n B 1 41 ARG 41 41 41 ARG ARG B . n B 1 42 LYS 42 42 42 LYS LYS B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 CYS 44 44 44 CYS CYS B . n B 1 45 ASP 45 45 45 ASP ASP B . n B 1 46 ASP 46 46 46 ASP ASP B . n B 1 47 PRO 47 47 47 PRO PRO B . n B 1 48 GLY 48 48 48 GLY GLY B . n B 1 49 LYS 49 49 49 LYS LYS B . n B 1 50 CYS 50 50 50 CYS CYS B . n B 1 51 PHE 51 51 51 PHE PHE B . n B 1 52 VAL 52 52 52 VAL VAL B . n B 1 53 LEU 53 53 53 LEU LEU B . n B 1 54 VAL 54 54 54 VAL VAL B . n B 1 55 ALA 55 55 55 ALA ALA B . n B 1 56 LEU 56 56 56 LEU LEU B . n B 1 57 SER 57 57 57 SER SER B . n B 1 58 ASN 58 58 58 ASN ASN B . n B 1 59 ASP 59 59 59 ASP ASP B . n B 1 60 ASN 60 60 60 ASN ASN B . n B 1 61 GLY 61 61 61 GLY GLY B . n B 1 62 GLN 62 62 62 GLN GLN B . n B 1 63 LEU 63 63 63 LEU LEU B . n B 1 64 ALA 64 64 64 ALA ALA B . n B 1 65 GLU 65 65 65 GLU GLU B . n B 1 66 ILE 66 66 66 ILE ILE B . n B 1 67 ALA 67 67 67 ALA ALA B . n B 1 68 ILE 68 68 68 ILE ILE B . n B 1 69 ASP 69 69 69 ASP ASP B . n B 1 70 VAL 70 70 70 VAL VAL B . n B 1 71 THR 71 71 71 THR THR B . n B 1 72 SER 72 72 72 SER SER B . n B 1 73 VAL 73 73 73 VAL VAL B . n B 1 74 TYR 74 74 74 TYR TYR B . n B 1 75 VAL 75 75 75 VAL VAL B . n B 1 76 VAL 76 76 76 VAL VAL B . n B 1 77 GLY 77 77 77 GLY GLY B . n B 1 78 TYR 78 78 78 TYR TYR B . n B 1 79 GLN 79 79 79 GLN GLN B . n B 1 80 VAL 80 80 80 VAL VAL B . n B 1 81 ARG 81 81 81 ARG ARG B . n B 1 82 ASN 82 82 82 ASN ASN B . n B 1 83 ARG 83 83 83 ARG ARG B . n B 1 84 SER 84 84 84 SER SER B . n B 1 85 TYR 85 85 85 TYR TYR B . n B 1 86 PHE 86 86 86 PHE PHE B . n B 1 87 PHE 87 87 87 PHE PHE B . n B 1 88 LYS 88 88 88 LYS LYS B . n B 1 89 ASP 89 89 89 ASP ASP B . n B 1 90 ALA 90 90 90 ALA ALA B . n B 1 91 PRO 91 91 91 PRO PRO B . n B 1 92 ASP 92 92 92 ASP ASP B . n B 1 93 ALA 93 93 93 ALA ALA B . n B 1 94 ALA 94 94 94 ALA ALA B . n B 1 95 TYR 95 95 95 TYR TYR B . n B 1 96 GLU 96 96 96 GLU GLU B . n B 1 97 GLY 97 97 97 GLY GLY B . n B 1 98 LEU 98 98 98 LEU LEU B . n B 1 99 PHE 99 99 99 PHE PHE B . n B 1 100 LYS 100 100 100 LYS LYS B . n B 1 101 ASN 101 101 101 ASN ASN B . n B 1 102 THR 102 102 102 THR THR B . n B 1 103 ILE 103 103 103 ILE ILE B . n B 1 104 LYS 104 104 104 LYS LYS B . n B 1 105 THR 105 105 105 THR THR B . n B 1 106 ARG 106 106 106 ARG ARG B . n B 1 107 LEU 107 107 107 LEU LEU B . n B 1 108 HIS 108 108 108 HIS HIS B . n B 1 109 PHE 109 109 109 PHE PHE B . n B 1 110 GLY 110 110 110 GLY GLY B . n B 1 111 GLY 111 111 111 GLY GLY B . n B 1 112 SER 112 112 112 SER SER B . n B 1 113 TYR 113 113 113 TYR TYR B . n B 1 114 PRO 114 114 114 PRO PRO B . n B 1 115 SER 115 115 115 SER SER B . n B 1 116 LEU 116 116 116 LEU LEU B . n B 1 117 GLU 117 117 117 GLU GLU B . n B 1 118 GLY 118 118 118 GLY GLY B . n B 1 119 GLU 119 119 119 GLU GLU B . n B 1 120 LYS 120 120 120 LYS LYS B . n B 1 121 ALA 121 121 121 ALA ALA B . n B 1 122 TYR 122 122 122 TYR TYR B . n B 1 123 ARG 123 123 123 ARG ARG B . n B 1 124 GLU 124 124 124 GLU GLU B . n B 1 125 THR 125 125 125 THR THR B . n B 1 126 THR 126 126 126 THR THR B . n B 1 127 ASP 127 127 127 ASP ASP B . n B 1 128 LEU 128 128 128 LEU LEU B . n B 1 129 GLY 129 129 129 GLY GLY B . n B 1 130 ILE 130 130 130 ILE ILE B . n B 1 131 GLU 131 131 131 GLU GLU B . n B 1 132 PRO 132 132 132 PRO PRO B . n B 1 133 LEU 133 133 133 LEU LEU B . n B 1 134 ARG 134 134 134 ARG ARG B . n B 1 135 ILE 135 135 135 ILE ILE B . n B 1 136 GLY 136 136 136 GLY GLY B . n B 1 137 ILE 137 137 137 ILE ILE B . n B 1 138 LYS 138 138 138 LYS LYS B . n B 1 139 LYS 139 139 139 LYS LYS B . n B 1 140 LEU 140 140 140 LEU LEU B . n B 1 141 ASP 141 141 141 ASP ASP B . n B 1 142 GLU 142 142 142 GLU GLU B . n B 1 143 ASN 143 143 143 ASN ASN B . n B 1 144 ALA 144 144 144 ALA ALA B . n B 1 145 ILE 145 145 145 ILE ILE B . n B 1 146 ASP 146 146 146 ASP ASP B . n B 1 147 ASN 147 147 147 ASN ASN B . n B 1 148 TYR 148 148 148 TYR TYR B . n B 1 149 LYS 149 149 149 LYS LYS B . n B 1 150 PRO 150 150 150 PRO PRO B . n B 1 151 THR 151 151 151 THR THR B . n B 1 152 GLU 152 152 152 GLU GLU B . n B 1 153 ILE 153 153 153 ILE ILE B . n B 1 154 ALA 154 154 154 ALA ALA B . n B 1 155 SER 155 155 155 SER SER B . n B 1 156 SER 156 156 156 SER SER B . n B 1 157 LEU 157 157 157 LEU LEU B . n B 1 158 LEU 158 158 158 LEU LEU B . n B 1 159 VAL 159 159 159 VAL VAL B . n B 1 160 VAL 160 160 160 VAL VAL B . n B 1 161 ILE 161 161 161 ILE ILE B . n B 1 162 GLN 162 162 162 GLN GLN B . n B 1 163 MET 163 163 163 MET MET B . n B 1 164 VAL 164 164 164 VAL VAL B . n B 1 165 SER 165 165 165 SER SER B . n B 1 166 GLU 166 166 166 GLU GLU B . n B 1 167 ALA 167 167 167 ALA ALA B . n B 1 168 ALA 168 168 168 ALA ALA B . n B 1 169 ARG 169 169 169 ARG ARG B . n B 1 170 PHE 170 170 170 PHE PHE B . n B 1 171 THR 171 171 171 THR THR B . n B 1 172 PHE 172 172 172 PHE PHE B . n B 1 173 ILE 173 173 173 ILE ILE B . n B 1 174 GLU 174 174 174 GLU GLU B . n B 1 175 ASN 175 175 175 ASN ASN B . n B 1 176 GLN 176 176 176 GLN GLN B . n B 1 177 ILE 177 177 177 ILE ILE B . n B 1 178 ARG 178 178 178 ARG ARG B . n B 1 179 ASN 179 179 179 ASN ASN B . n B 1 180 ASN 180 180 180 ASN ASN B . n B 1 181 PHE 181 181 181 PHE PHE B . n B 1 182 GLN 182 182 182 GLN GLN B . n B 1 183 GLN 183 183 183 GLN GLN B . n B 1 184 ARG 184 184 184 ARG ARG B . n B 1 185 ILE 185 185 185 ILE ILE B . n B 1 186 ARG 186 186 186 ARG ARG B . n B 1 187 PRO 187 187 187 PRO PRO B . n B 1 188 ALA 188 188 188 ALA ALA B . n B 1 189 ASN 189 189 189 ASN ASN B . n B 1 190 ASN 190 190 190 ASN ASN B . n B 1 191 THR 191 191 191 THR THR B . n B 1 192 ILE 192 192 192 ILE ILE B . n B 1 193 SER 193 193 193 SER SER B . n B 1 194 LEU 194 194 194 LEU LEU B . n B 1 195 GLU 195 195 195 GLU GLU B . n B 1 196 ASN 196 196 196 ASN ASN B . n B 1 197 LYS 197 197 197 LYS LYS B . n B 1 198 TRP 198 198 198 TRP TRP B . n B 1 199 GLY 199 199 199 GLY GLY B . n B 1 200 LYS 200 200 200 LYS LYS B . n B 1 201 LEU 201 201 201 LEU LEU B . n B 1 202 SER 202 202 202 SER SER B . n B 1 203 PHE 203 203 203 PHE PHE B . n B 1 204 GLN 204 204 204 GLN GLN B . n B 1 205 ILE 205 205 205 ILE ILE B . n B 1 206 ARG 206 206 206 ARG ARG B . n B 1 207 THR 207 207 207 THR THR B . n B 1 208 SER 208 208 208 SER SER B . n B 1 209 GLY 209 209 209 GLY GLY B . n B 1 210 ALA 210 210 210 ALA ALA B . n B 1 211 ASN 211 211 211 ASN ASN B . n B 1 212 GLY 212 212 212 GLY GLY B . n B 1 213 MET 213 213 213 MET MET B . n B 1 214 PHE 214 214 214 PHE PHE B . n B 1 215 SER 215 215 215 SER SER B . n B 1 216 GLU 216 216 216 GLU GLU B . n B 1 217 ALA 217 217 217 ALA ALA B . n B 1 218 VAL 218 218 218 VAL VAL B . n B 1 219 GLU 219 219 219 GLU GLU B . n B 1 220 LEU 220 220 220 LEU LEU B . n B 1 221 GLU 221 221 221 GLU GLU B . n B 1 222 ARG 222 222 222 ARG ARG B . n B 1 223 ALA 223 223 223 ALA ALA B . n B 1 224 ASN 224 224 224 ASN ASN B . n B 1 225 GLY 225 225 225 GLY GLY B . n B 1 226 LYS 226 226 226 LYS LYS B . n B 1 227 LYS 227 227 227 LYS LYS B . n B 1 228 TYR 228 228 228 TYR TYR B . n B 1 229 TYR 229 229 229 TYR TYR B . n B 1 230 VAL 230 230 230 VAL VAL B . n B 1 231 THR 231 231 231 THR THR B . n B 1 232 ALA 232 232 232 ALA ALA B . n B 1 233 VAL 233 233 233 VAL VAL B . n B 1 234 ASP 234 234 234 ASP ASP B . n B 1 235 GLN 235 235 235 GLN GLN B . n B 1 236 VAL 236 236 236 VAL VAL B . n B 1 237 LYS 237 237 237 LYS LYS B . n B 1 238 PRO 238 238 238 PRO PRO B . n B 1 239 LYS 239 239 239 LYS LYS B . n B 1 240 ILE 240 240 240 ILE ILE B . n B 1 241 ALA 241 241 241 ALA ALA B . n B 1 242 LEU 242 242 242 LEU LEU B . n B 1 243 LEU 243 243 243 LEU LEU B . n B 1 244 LYS 244 244 244 LYS LYS B . n B 1 245 PHE 245 245 245 PHE PHE B . n B 1 246 VAL 246 246 246 VAL VAL B . n B 1 247 ASP 247 247 247 ASP ASP B . n B 1 248 LYS 248 248 248 LYS LYS B . n B 1 249 ASP 249 249 249 ASP ASP B . n B 1 250 PRO 250 250 250 PRO PRO B . n B 1 251 LYS 251 251 251 LYS LYS B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 410 410 NAG NAG A . D 2 NAG 1 411 411 NAG NAG B . E 3 HOH 1 801 801 HOH TIP A . E 3 HOH 2 802 802 HOH TIP A . E 3 HOH 3 804 804 HOH TIP A . E 3 HOH 4 805 805 HOH TIP A . E 3 HOH 5 806 806 HOH TIP A . E 3 HOH 6 807 807 HOH TIP A . E 3 HOH 7 809 809 HOH TIP A . E 3 HOH 8 811 811 HOH TIP A . E 3 HOH 9 812 812 HOH TIP A . E 3 HOH 10 813 813 HOH TIP A . E 3 HOH 11 816 816 HOH TIP A . E 3 HOH 12 817 817 HOH TIP A . E 3 HOH 13 818 818 HOH TIP A . E 3 HOH 14 819 819 HOH TIP A . E 3 HOH 15 820 820 HOH TIP A . E 3 HOH 16 821 821 HOH TIP A . E 3 HOH 17 824 824 HOH TIP A . E 3 HOH 18 825 825 HOH TIP A . E 3 HOH 19 828 828 HOH TIP A . E 3 HOH 20 829 829 HOH TIP A . E 3 HOH 21 830 830 HOH TIP A . E 3 HOH 22 832 832 HOH TIP A . E 3 HOH 23 833 833 HOH TIP A . E 3 HOH 24 835 835 HOH TIP A . E 3 HOH 25 836 836 HOH TIP A . E 3 HOH 26 837 837 HOH TIP A . E 3 HOH 27 841 841 HOH TIP A . E 3 HOH 28 843 843 HOH TIP A . E 3 HOH 29 846 846 HOH TIP A . E 3 HOH 30 847 847 HOH TIP A . E 3 HOH 31 848 848 HOH TIP A . E 3 HOH 32 849 849 HOH TIP A . E 3 HOH 33 850 850 HOH TIP A . E 3 HOH 34 851 851 HOH TIP A . E 3 HOH 35 853 853 HOH TIP A . E 3 HOH 36 857 857 HOH TIP A . E 3 HOH 37 859 859 HOH TIP A . E 3 HOH 38 860 860 HOH TIP A . E 3 HOH 39 862 862 HOH TIP A . E 3 HOH 40 863 863 HOH TIP A . E 3 HOH 41 865 865 HOH TIP A . E 3 HOH 42 867 867 HOH TIP A . E 3 HOH 43 868 868 HOH TIP A . E 3 HOH 44 869 869 HOH TIP A . E 3 HOH 45 870 870 HOH TIP A . E 3 HOH 46 871 871 HOH TIP A . E 3 HOH 47 876 876 HOH TIP A . E 3 HOH 48 878 878 HOH TIP A . E 3 HOH 49 881 881 HOH TIP A . E 3 HOH 50 882 882 HOH TIP A . E 3 HOH 51 883 883 HOH TIP A . E 3 HOH 52 884 884 HOH TIP A . E 3 HOH 53 885 885 HOH TIP A . E 3 HOH 54 888 888 HOH TIP A . E 3 HOH 55 890 890 HOH TIP A . E 3 HOH 56 891 891 HOH TIP A . E 3 HOH 57 892 892 HOH TIP A . E 3 HOH 58 893 893 HOH TIP A . E 3 HOH 59 895 895 HOH TIP A . E 3 HOH 60 897 897 HOH TIP A . E 3 HOH 61 898 898 HOH TIP A . E 3 HOH 62 901 901 HOH TIP A . E 3 HOH 63 902 902 HOH TIP A . E 3 HOH 64 904 904 HOH TIP A . E 3 HOH 65 905 905 HOH TIP A . E 3 HOH 66 906 906 HOH TIP A . E 3 HOH 67 907 907 HOH TIP A . E 3 HOH 68 909 909 HOH TIP A . E 3 HOH 69 910 910 HOH TIP A . E 3 HOH 70 911 911 HOH TIP A . E 3 HOH 71 913 913 HOH TIP A . E 3 HOH 72 917 917 HOH TIP A . E 3 HOH 73 918 918 HOH TIP A . E 3 HOH 74 920 920 HOH TIP A . E 3 HOH 75 922 922 HOH TIP A . E 3 HOH 76 924 924 HOH TIP A . E 3 HOH 77 925 925 HOH TIP A . E 3 HOH 78 926 926 HOH TIP A . E 3 HOH 79 927 927 HOH TIP A . E 3 HOH 80 930 930 HOH TIP A . E 3 HOH 81 931 931 HOH TIP A . E 3 HOH 82 933 933 HOH TIP A . E 3 HOH 83 935 935 HOH TIP A . E 3 HOH 84 936 936 HOH TIP A . E 3 HOH 85 938 938 HOH TIP A . E 3 HOH 86 939 939 HOH TIP A . E 3 HOH 87 940 940 HOH TIP A . E 3 HOH 88 941 941 HOH TIP A . E 3 HOH 89 943 943 HOH TIP A . E 3 HOH 90 945 945 HOH TIP A . E 3 HOH 91 946 946 HOH TIP A . E 3 HOH 92 948 948 HOH TIP A . E 3 HOH 93 951 951 HOH TIP A . E 3 HOH 94 952 952 HOH TIP A . E 3 HOH 95 955 955 HOH TIP A . E 3 HOH 96 957 957 HOH TIP A . E 3 HOH 97 959 959 HOH TIP A . E 3 HOH 98 960 960 HOH TIP A . E 3 HOH 99 962 962 HOH TIP A . E 3 HOH 100 963 963 HOH TIP A . E 3 HOH 101 966 966 HOH TIP A . E 3 HOH 102 967 967 HOH TIP A . E 3 HOH 103 969 969 HOH TIP A . E 3 HOH 104 973 973 HOH TIP A . E 3 HOH 105 974 974 HOH TIP A . E 3 HOH 106 976 976 HOH TIP A . E 3 HOH 107 982 982 HOH TIP A . E 3 HOH 108 984 984 HOH TIP A . E 3 HOH 109 985 985 HOH TIP A . E 3 HOH 110 988 988 HOH TIP A . E 3 HOH 111 989 989 HOH TIP A . E 3 HOH 112 990 990 HOH TIP A . E 3 HOH 113 995 995 HOH TIP A . E 3 HOH 114 996 996 HOH TIP A . E 3 HOH 115 997 997 HOH TIP A . E 3 HOH 116 999 999 HOH TIP A . F 3 HOH 1 803 803 HOH TIP B . F 3 HOH 2 808 808 HOH TIP B . F 3 HOH 3 810 810 HOH TIP B . F 3 HOH 4 814 814 HOH TIP B . F 3 HOH 5 815 815 HOH TIP B . F 3 HOH 6 822 822 HOH TIP B . F 3 HOH 7 823 823 HOH TIP B . F 3 HOH 8 826 826 HOH TIP B . F 3 HOH 9 827 827 HOH TIP B . F 3 HOH 10 831 831 HOH TIP B . F 3 HOH 11 834 834 HOH TIP B . F 3 HOH 12 838 838 HOH TIP B . F 3 HOH 13 839 839 HOH TIP B . F 3 HOH 14 840 840 HOH TIP B . F 3 HOH 15 842 842 HOH TIP B . F 3 HOH 16 844 844 HOH TIP B . F 3 HOH 17 845 845 HOH TIP B . F 3 HOH 18 852 852 HOH TIP B . F 3 HOH 19 854 854 HOH TIP B . F 3 HOH 20 855 855 HOH TIP B . F 3 HOH 21 856 856 HOH TIP B . F 3 HOH 22 858 858 HOH TIP B . F 3 HOH 23 861 861 HOH TIP B . F 3 HOH 24 864 864 HOH TIP B . F 3 HOH 25 866 866 HOH TIP B . F 3 HOH 26 872 872 HOH TIP B . F 3 HOH 27 873 873 HOH TIP B . F 3 HOH 28 874 874 HOH TIP B . F 3 HOH 29 875 875 HOH TIP B . F 3 HOH 30 877 877 HOH TIP B . F 3 HOH 31 879 879 HOH TIP B . F 3 HOH 32 880 880 HOH TIP B . F 3 HOH 33 886 886 HOH TIP B . F 3 HOH 34 887 887 HOH TIP B . F 3 HOH 35 889 889 HOH TIP B . F 3 HOH 36 894 894 HOH TIP B . F 3 HOH 37 896 896 HOH TIP B . F 3 HOH 38 899 899 HOH TIP B . F 3 HOH 39 900 900 HOH TIP B . F 3 HOH 40 903 903 HOH TIP B . F 3 HOH 41 908 908 HOH TIP B . F 3 HOH 42 912 912 HOH TIP B . F 3 HOH 43 914 914 HOH TIP B . F 3 HOH 44 915 915 HOH TIP B . F 3 HOH 45 916 916 HOH TIP B . F 3 HOH 46 919 919 HOH TIP B . F 3 HOH 47 921 921 HOH TIP B . F 3 HOH 48 923 923 HOH TIP B . F 3 HOH 49 928 928 HOH TIP B . F 3 HOH 50 929 929 HOH TIP B . F 3 HOH 51 932 932 HOH TIP B . F 3 HOH 52 934 934 HOH TIP B . F 3 HOH 53 937 937 HOH TIP B . F 3 HOH 54 942 942 HOH TIP B . F 3 HOH 55 944 944 HOH TIP B . F 3 HOH 56 947 947 HOH TIP B . F 3 HOH 57 949 949 HOH TIP B . F 3 HOH 58 950 950 HOH TIP B . F 3 HOH 59 953 953 HOH TIP B . F 3 HOH 60 954 954 HOH TIP B . F 3 HOH 61 956 956 HOH TIP B . F 3 HOH 62 958 958 HOH TIP B . F 3 HOH 63 961 961 HOH TIP B . F 3 HOH 64 964 964 HOH TIP B . F 3 HOH 65 965 965 HOH TIP B . F 3 HOH 66 968 968 HOH TIP B . F 3 HOH 67 970 970 HOH TIP B . F 3 HOH 68 971 971 HOH TIP B . F 3 HOH 69 972 972 HOH TIP B . F 3 HOH 70 975 975 HOH TIP B . F 3 HOH 71 977 977 HOH TIP B . F 3 HOH 72 978 978 HOH TIP B . F 3 HOH 73 979 979 HOH TIP B . F 3 HOH 74 980 980 HOH TIP B . F 3 HOH 75 981 981 HOH TIP B . F 3 HOH 76 983 983 HOH TIP B . F 3 HOH 77 986 986 HOH TIP B . F 3 HOH 78 987 987 HOH TIP B . F 3 HOH 79 991 991 HOH TIP B . F 3 HOH 80 992 992 HOH TIP B . F 3 HOH 81 993 993 HOH TIP B . F 3 HOH 82 994 994 HOH TIP B . F 3 HOH 83 998 998 HOH TIP B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 B ASN 189 B ASN 189 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 189 A ASN 189 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA monomeric 1 2 author_and_software_defined_assembly PISA monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,E 2 1 B,D,F # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # 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 2010-01-26 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-01 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 CNS 1.2 ? package 'Axel T. Brunger' axel.brunger@yale.edu refinement http://cns-online.org/ Fortran_77 ? 2 PDB_EXTRACT 3.005 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 3 ADSC Quantum ? ? ? ? 'data collection' ? ? ? 4 DENZO . ? ? ? ? 'data reduction' ? ? ? 5 SCALEPACK . ? ? ? ? 'data scaling' ? ? ? 6 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? 7 CNS . ? ? ? ? phasing ? ? ? # 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 CYS A 44 ? ? -167.57 79.76 2 1 ASP A 46 ? ? -53.12 106.90 3 1 LYS A 49 ? ? -162.54 11.45 4 1 ARG A 81 ? ? 56.38 -126.10 5 1 CYS B 44 ? ? 175.66 99.28 6 1 ASP B 46 ? ? -45.17 106.64 7 1 LYS B 49 ? ? -170.63 3.96 8 1 ARG B 81 ? ? 55.36 -131.67 9 1 ASN B 147 ? ? -94.47 57.02 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 water HOH #