data_3KU0 # _entry.id 3KU0 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3KU0 RCSB RCSB056445 WWPDB D_1000056445 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3KTZ _pdbx_database_related.details 'Structure of GAP31' _pdbx_database_related.content_type unspecified # _pdbx_database_status.entry_id 3KU0 _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 ? # _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 3KU0 _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 3KU0 _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 RESIDUES 47-297)' ? 2 non-polymer syn ADENINE 135.127 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 4 water nat water 18.015 175 ? ? ? ? # _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 'Gelonium multiflorum' _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 'The enzyme is isolated from seeds of Gelonium multiflorum. The DNA oligo is synthesized by a commercial source.' # _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 3KU0 A 1 ? 251 ? P33186 47 ? 297 ? 1 251 2 1 3KU0 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 ADE non-polymer . ADENINE ? 'C5 H5 N5' 135.127 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 3KU0 _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 3KU0 _reflns.B_iso_Wilson_estimate 11.700 _reflns.observed_criterion_sigma_F 2.0 _reflns.observed_criterion_sigma_I 2.0 _reflns.d_resolution_high 1.9 _reflns.d_resolution_low 47.35 _reflns.number_all 48417 _reflns.number_obs 46674 _reflns.percent_possible_obs 96.4 _reflns.pdbx_Rmerge_I_obs 4.1 _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 1.90 _reflns_shell.d_res_low 2.02 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 71.0 _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 3KU0 _refine.ls_d_res_high 1.900 _refine.ls_d_res_low 47.350 _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF 521827.000 _refine.pdbx_data_cutoff_low_absF 0.000 _refine.ls_percent_reflns_obs 90.700 _refine.ls_number_reflns_obs 41738 _refine.ls_number_reflns_all 46674 _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 0.200 _refine.ls_R_factor_obs 0.200 _refine.ls_R_factor_R_work 0.200 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.242 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 4.900 _refine.ls_number_reflns_R_free 2061 _refine.ls_R_factor_R_free_error 0.005 _refine.B_iso_mean 21.911 _refine.solvent_model_param_bsol 51.488 _refine.solvent_model_param_ksol 0.400 _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.aniso_B[1][1] 6.760 _refine.aniso_B[2][2] 0.580 _refine.aniso_B[3][3] -7.340 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] 2.480 _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 79.66 _refine.B_iso_min 8.59 _refine.occupancy_max 1.00 _refine.occupancy_min 1.00 _refine.pdbx_ls_sigma_I 0.0 _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 3KU0 _refine_analyze.Luzzati_coordinate_error_obs 0.220 _refine_analyze.Luzzati_sigma_a_obs 0.200 _refine_analyze.Luzzati_d_res_low_obs 5.000 _refine_analyze.Luzzati_coordinate_error_free 0.260 _refine_analyze.Luzzati_sigma_a_free 0.120 _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 48 _refine_hist.number_atoms_solvent 175 _refine_hist.number_atoms_total 4199 _refine_hist.d_res_high 1.900 _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 ? 0.007 ? ? 'X-RAY DIFFRACTION' ? c_angle_deg ? 1.300 ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d ? 22.500 ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d ? 0.790 ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it ? 1.190 1.500 ? 'X-RAY DIFFRACTION' ? c_mcangle_it ? 1.970 2.000 ? 'X-RAY DIFFRACTION' ? c_scbond_it ? 2.380 2.000 ? 'X-RAY DIFFRACTION' ? c_scangle_it ? 3.630 2.500 ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.d_res_high 1.900 _refine_ls_shell.d_res_low 2.020 _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.percent_reflns_obs 71.000 _refine_ls_shell.number_reflns_R_work 5132 _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_R_work 0.247 _refine_ls_shell.R_factor_R_free 0.245 _refine_ls_shell.percent_reflns_R_free 5.300 _refine_ls_shell.number_reflns_R_free 288 _refine_ls_shell.R_factor_R_free_error 0.014 _refine_ls_shell.number_reflns_all 5420 _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 carbohydrate.param dna-rna.top 'X-RAY DIFFRACTION' 3 water_rep.param water.top 'X-RAY DIFFRACTION' 4 dna-rna_rep.param carbohydrate.top 'X-RAY DIFFRACTION' # _struct.entry_id 3KU0 _struct.title 'Structure of GAP31 with adenine at its binding pocket' _struct.pdbx_descriptor 'Ribosome-inactivating protein gelonin (E.C.3.2.2.22)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3KU0 _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 3 ? E N N 2 ? F N N 3 ? G N N 4 ? H N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 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 GLY B 129 ? ASN B 143 ? GLY B 129 ASN B 143 1 ? 15 HELX_P HELX_P16 16 LYS B 149 ? VAL B 164 ? LYS B 149 VAL B 164 1 ? 16 HELX_P HELX_P17 17 VAL B 164 ? PHE B 170 ? VAL B 164 PHE B 170 1 ? 7 HELX_P HELX_P18 18 PHE B 170 ? ASN B 179 ? PHE B 170 ASN B 179 1 ? 10 HELX_P HELX_P19 19 ALA B 188 ? LYS B 197 ? ALA B 188 LYS B 197 1 ? 10 HELX_P HELX_P20 20 LYS B 197 ? SER B 208 ? LYS B 197 SER B 208 1 ? 12 HELX_P HELX_P21 21 VAL B 233 ? LYS B 237 ? VAL B 233 LYS B 237 1 ? 5 HELX_P HELX_P22 22 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 ? ? ? ? ? ? ? 2.032 ? disulf2 disulf ? ? B CYS 44 SG ? ? ? 1_555 B CYS 50 SG ? ? B CYS 44 B CYS 50 1_555 ? ? ? ? ? ? ? 2.031 ? covale1 covale ? ? B ASN 189 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 189 B NAG 411 1_555 ? ? ? ? ? ? ? 1.453 ? covale2 covale ? ? A ASN 189 ND2 ? ? ? 1_555 D 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 ALA A 55 ? O ALA A 55 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 TYR A 78 ? N TYR A 78 O TYR A 85 ? O TYR A 85 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 VAL A 218 ? N VAL A 218 O VAL A 230 ? O VAL A 230 D 1 2 N ASP B 3 ? N ASP B 3 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 ? ? ? ? 9 'BINDING SITE FOR RESIDUE ADE A 800' AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ADE B 801' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 410' AC4 Software ? ? ? ? 5 '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 9 VAL A 73 ? VAL A 73 . ? 1_555 ? 2 AC1 9 TYR A 74 ? TYR A 74 . ? 1_555 ? 3 AC1 9 VAL A 75 ? VAL A 75 . ? 1_555 ? 4 AC1 9 PHE A 87 ? PHE A 87 . ? 1_555 ? 5 AC1 9 GLY A 111 ? GLY A 111 . ? 1_555 ? 6 AC1 9 TYR A 113 ? TYR A 113 . ? 1_555 ? 7 AC1 9 ILE A 161 ? ILE A 161 . ? 1_555 ? 8 AC1 9 ARG A 169 ? ARG A 169 . ? 1_555 ? 9 AC1 9 HOH G . ? HOH A 855 . ? 1_555 ? 10 AC2 8 TYR B 74 ? TYR B 74 . ? 1_555 ? 11 AC2 8 VAL B 75 ? VAL B 75 . ? 1_555 ? 12 AC2 8 GLY B 111 ? GLY B 111 . ? 1_555 ? 13 AC2 8 TYR B 113 ? TYR B 113 . ? 1_555 ? 14 AC2 8 ILE B 161 ? ILE B 161 . ? 1_555 ? 15 AC2 8 GLU B 166 ? GLU B 166 . ? 1_555 ? 16 AC2 8 ARG B 169 ? ARG B 169 . ? 1_555 ? 17 AC2 8 HOH H . ? HOH B 911 . ? 1_555 ? 18 AC3 6 GLU A 124 ? GLU A 124 . ? 1_555 ? 19 AC3 6 PRO A 187 ? PRO A 187 . ? 1_555 ? 20 AC3 6 ALA A 188 ? ALA A 188 . ? 1_555 ? 21 AC3 6 ASN A 189 ? ASN A 189 . ? 1_555 ? 22 AC3 6 ALA A 223 ? ALA A 223 . ? 1_555 ? 23 AC3 6 ASN A 224 ? ASN A 224 . ? 1_555 ? 24 AC4 5 PRO B 187 ? PRO B 187 . ? 1_555 ? 25 AC4 5 ALA B 188 ? ALA B 188 . ? 1_555 ? 26 AC4 5 ASN B 189 ? ASN B 189 . ? 1_555 ? 27 AC4 5 ASN B 224 ? ASN B 224 . ? 1_555 ? 28 AC4 5 GLY B 225 ? GLY B 225 . ? 1_555 ? # _database_PDB_matrix.entry_id 3KU0 _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 3KU0 _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 ? 6.903 -18.162 50.531 1.00 45.44 ? 1 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 7.025 -18.143 49.038 1.00 45.82 ? 1 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 7.273 -16.740 48.524 1.00 44.57 ? 1 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 6.418 -16.137 47.871 1.00 46.67 ? 1 GLY A O 1 ATOM 5 N N . LEU A 1 2 ? 8.458 -16.223 48.808 1.00 41.86 ? 2 LEU A N 1 ATOM 6 C CA . LEU A 1 2 ? 8.818 -14.872 48.407 1.00 39.75 ? 2 LEU A CA 1 ATOM 7 C C . LEU A 1 2 ? 9.748 -14.869 47.198 1.00 38.11 ? 2 LEU A C 1 ATOM 8 O O . LEU A 1 2 ? 10.212 -15.920 46.750 1.00 39.91 ? 2 LEU A O 1 ATOM 9 C CB . LEU A 1 2 ? 9.514 -14.179 49.580 1.00 39.10 ? 2 LEU A CB 1 ATOM 10 C CG . LEU A 1 2 ? 8.835 -14.391 50.936 1.00 38.36 ? 2 LEU A CG 1 ATOM 11 C CD1 . LEU A 1 2 ? 9.860 -14.278 52.049 1.00 38.06 ? 2 LEU A CD1 1 ATOM 12 C CD2 . LEU A 1 2 ? 7.700 -13.388 51.107 1.00 36.57 ? 2 LEU A CD2 1 ATOM 13 N N . ASP A 1 3 ? 10.004 -13.679 46.663 1.00 34.34 ? 3 ASP A N 1 ATOM 14 C CA . ASP A 1 3 ? 10.926 -13.532 45.546 1.00 28.37 ? 3 ASP A CA 1 ATOM 15 C C . ASP A 1 3 ? 12.267 -13.288 46.208 1.00 25.15 ? 3 ASP A C 1 ATOM 16 O O . ASP A 1 3 ? 12.322 -12.817 47.349 1.00 21.89 ? 3 ASP A O 1 ATOM 17 C CB . ASP A 1 3 ? 10.560 -12.328 44.686 1.00 29.85 ? 3 ASP A CB 1 ATOM 18 C CG . ASP A 1 3 ? 9.913 -12.726 43.382 1.00 32.16 ? 3 ASP A CG 1 ATOM 19 O OD1 . ASP A 1 3 ? 10.534 -13.513 42.634 1.00 32.61 ? 3 ASP A OD1 1 ATOM 20 O OD2 . ASP A 1 3 ? 8.789 -12.253 43.105 1.00 32.35 ? 3 ASP A OD2 1 ATOM 21 N N . THR A 1 4 ? 13.345 -13.612 45.507 1.00 21.96 ? 4 THR A N 1 ATOM 22 C CA . THR A 1 4 ? 14.674 -13.416 46.066 1.00 20.22 ? 4 THR A CA 1 ATOM 23 C C . THR A 1 4 ? 15.601 -12.777 45.038 1.00 19.07 ? 4 THR A C 1 ATOM 24 O O . THR A 1 4 ? 15.425 -12.962 43.833 1.00 17.93 ? 4 THR A O 1 ATOM 25 C CB . THR A 1 4 ? 15.286 -14.762 46.550 1.00 18.80 ? 4 THR A CB 1 ATOM 26 O OG1 . THR A 1 4 ? 15.356 -15.673 45.452 1.00 21.96 ? 4 THR A OG1 1 ATOM 27 C CG2 . THR A 1 4 ? 14.429 -15.392 47.635 1.00 17.43 ? 4 THR A CG2 1 ATOM 28 N N . VAL A 1 5 ? 16.574 -12.010 45.524 1.00 18.33 ? 5 VAL A N 1 ATOM 29 C CA . VAL A 1 5 ? 17.553 -11.343 44.661 1.00 18.60 ? 5 VAL A CA 1 ATOM 30 C C . VAL A 1 5 ? 18.926 -11.479 45.320 1.00 17.06 ? 5 VAL A C 1 ATOM 31 O O . VAL A 1 5 ? 19.040 -11.380 46.537 1.00 17.34 ? 5 VAL A O 1 ATOM 32 C CB . VAL A 1 5 ? 17.232 -9.827 44.482 1.00 19.44 ? 5 VAL A CB 1 ATOM 33 C CG1 . VAL A 1 5 ? 18.140 -9.229 43.407 1.00 20.45 ? 5 VAL A CG1 1 ATOM 34 C CG2 . VAL A 1 5 ? 15.774 -9.634 44.102 1.00 20.90 ? 5 VAL A CG2 1 ATOM 35 N N . SER A 1 6 ? 19.966 -11.702 44.523 1.00 16.31 ? 6 SER A N 1 ATOM 36 C CA . SER A 1 6 ? 21.308 -11.861 45.075 1.00 18.11 ? 6 SER A CA 1 ATOM 37 C C . SER A 1 6 ? 22.319 -10.837 44.589 1.00 17.65 ? 6 SER A C 1 ATOM 38 O O . SER A 1 6 ? 22.212 -10.316 43.482 1.00 17.38 ? 6 SER A O 1 ATOM 39 C CB . SER A 1 6 ? 21.858 -13.254 44.745 1.00 18.80 ? 6 SER A CB 1 ATOM 40 O OG . SER A 1 6 ? 21.096 -14.268 45.374 1.00 25.18 ? 6 SER A OG 1 ATOM 41 N N . PHE A 1 7 ? 23.294 -10.542 45.440 1.00 15.51 ? 7 PHE A N 1 ATOM 42 C CA . PHE A 1 7 ? 24.372 -9.643 45.079 1.00 15.18 ? 7 PHE A CA 1 ATOM 43 C C . PHE A 1 7 ? 25.614 -10.077 45.827 1.00 16.05 ? 7 PHE A C 1 ATOM 44 O O . PHE A 1 7 ? 25.617 -10.156 47.057 1.00 15.27 ? 7 PHE A O 1 ATOM 45 C CB . PHE A 1 7 ? 24.083 -8.182 45.424 1.00 15.60 ? 7 PHE A CB 1 ATOM 46 C CG . PHE A 1 7 ? 25.209 -7.251 45.039 1.00 14.92 ? 7 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 7 ? 25.555 -7.077 43.701 1.00 13.63 ? 7 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 7 ? 25.964 -6.600 46.010 1.00 16.33 ? 7 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 7 ? 26.636 -6.274 43.332 1.00 12.42 ? 7 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 7 ? 27.053 -5.790 45.648 1.00 15.41 ? 7 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 7 ? 27.385 -5.631 44.305 1.00 13.81 ? 7 PHE A CZ 1 ATOM 52 N N . SER A 1 8 ? 26.667 -10.366 45.076 1.00 16.23 ? 8 SER A N 1 ATOM 53 C CA . SER A 1 8 ? 27.931 -10.783 45.661 1.00 17.83 ? 8 SER A CA 1 ATOM 54 C C . SER A 1 8 ? 28.952 -9.679 45.450 1.00 16.58 ? 8 SER A C 1 ATOM 55 O O . SER A 1 8 ? 29.021 -9.094 44.371 1.00 16.09 ? 8 SER A O 1 ATOM 56 C CB . SER A 1 8 ? 28.424 -12.077 44.996 1.00 20.57 ? 8 SER A CB 1 ATOM 57 O OG . SER A 1 8 ? 29.737 -12.410 45.434 1.00 24.76 ? 8 SER A OG 1 ATOM 58 N N . THR A 1 9 ? 29.743 -9.391 46.478 1.00 15.39 ? 9 THR A N 1 ATOM 59 C CA . THR A 1 9 ? 30.753 -8.354 46.365 1.00 17.56 ? 9 THR A CA 1 ATOM 60 C C . THR A 1 9 ? 32.010 -8.901 45.676 1.00 18.59 ? 9 THR A C 1 ATOM 61 O O . THR A 1 9 ? 32.858 -8.131 45.212 1.00 17.52 ? 9 THR A O 1 ATOM 62 C CB . THR A 1 9 ? 31.147 -7.800 47.753 1.00 19.07 ? 9 THR A CB 1 ATOM 63 O OG1 . THR A 1 9 ? 31.612 -8.874 48.583 1.00 20.13 ? 9 THR A OG1 1 ATOM 64 C CG2 . THR A 1 9 ? 29.955 -7.120 48.421 1.00 18.27 ? 9 THR A CG2 1 ATOM 65 N N . LYS A 1 10 ? 32.123 -10.227 45.599 1.00 19.24 ? 10 LYS A N 1 ATOM 66 C CA . LYS A 1 10 ? 33.292 -10.858 44.982 1.00 20.82 ? 10 LYS A CA 1 ATOM 67 C C . LYS A 1 10 ? 33.357 -10.577 43.480 1.00 20.12 ? 10 LYS A C 1 ATOM 68 O O . LYS A 1 10 ? 32.519 -11.048 42.709 1.00 19.78 ? 10 LYS A O 1 ATOM 69 C CB . LYS A 1 10 ? 33.267 -12.370 45.222 1.00 23.77 ? 10 LYS A CB 1 ATOM 70 C CG . LYS A 1 10 ? 34.619 -13.053 45.025 1.00 27.05 ? 10 LYS A CG 1 ATOM 71 C CD . LYS A 1 10 ? 34.489 -14.576 45.084 1.00 33.94 ? 10 LYS A CD 1 ATOM 72 C CE . LYS A 1 10 ? 33.784 -15.046 46.365 1.00 37.94 ? 10 LYS A CE 1 ATOM 73 N NZ . LYS A 1 10 ? 33.613 -16.535 46.436 1.00 39.63 ? 10 LYS A NZ 1 ATOM 74 N N . GLY A 1 11 ? 34.367 -9.818 43.071 1.00 18.34 ? 11 GLY A N 1 ATOM 75 C CA . GLY A 1 11 ? 34.502 -9.473 41.673 1.00 18.22 ? 11 GLY A CA 1 ATOM 76 C C . GLY A 1 11 ? 33.398 -8.521 41.244 1.00 18.25 ? 11 GLY A C 1 ATOM 77 O O . GLY A 1 11 ? 33.133 -8.356 40.053 1.00 19.17 ? 11 GLY A O 1 ATOM 78 N N . ALA A 1 12 ? 32.745 -7.892 42.216 1.00 17.60 ? 12 ALA A N 1 ATOM 79 C CA . ALA A 1 12 ? 31.659 -6.962 41.925 1.00 16.71 ? 12 ALA A CA 1 ATOM 80 C C . ALA A 1 12 ? 32.158 -5.729 41.186 1.00 16.05 ? 12 ALA A C 1 ATOM 81 O O . ALA A 1 12 ? 33.273 -5.266 41.413 1.00 16.25 ? 12 ALA A O 1 ATOM 82 C CB . ALA A 1 12 ? 30.968 -6.541 43.221 1.00 15.45 ? 12 ALA A CB 1 ATOM 83 N N . THR A 1 13 ? 31.328 -5.207 40.291 1.00 16.88 ? 13 THR A N 1 ATOM 84 C CA . THR A 1 13 ? 31.663 -3.999 39.540 1.00 15.30 ? 13 THR A CA 1 ATOM 85 C C . THR A 1 13 ? 30.455 -3.067 39.600 1.00 15.84 ? 13 THR A C 1 ATOM 86 O O . THR A 1 13 ? 29.375 -3.464 40.049 1.00 15.20 ? 13 THR A O 1 ATOM 87 C CB . THR A 1 13 ? 31.966 -4.312 38.072 1.00 14.94 ? 13 THR A CB 1 ATOM 88 O OG1 . THR A 1 13 ? 30.761 -4.707 37.405 1.00 16.94 ? 13 THR A OG1 1 ATOM 89 C CG2 . THR A 1 13 ? 32.976 -5.436 37.976 1.00 15.70 ? 13 THR A CG2 1 ATOM 90 N N . TYR A 1 14 ? 30.630 -1.830 39.150 1.00 15.56 ? 14 TYR A N 1 ATOM 91 C CA . TYR A 1 14 ? 29.537 -0.872 39.163 1.00 15.36 ? 14 TYR A CA 1 ATOM 92 C C . TYR A 1 14 ? 28.380 -1.409 38.320 1.00 15.25 ? 14 TYR A C 1 ATOM 93 O O . TYR A 1 14 ? 27.216 -1.069 38.558 1.00 13.53 ? 14 TYR A O 1 ATOM 94 C CB . TYR A 1 14 ? 30.022 0.475 38.624 1.00 17.69 ? 14 TYR A CB 1 ATOM 95 C CG . TYR A 1 14 ? 30.444 0.440 37.173 1.00 19.26 ? 14 TYR A CG 1 ATOM 96 C CD1 . TYR A 1 14 ? 29.534 0.729 36.151 1.00 20.75 ? 14 TYR A CD1 1 ATOM 97 C CD2 . TYR A 1 14 ? 31.743 0.093 36.821 1.00 20.29 ? 14 TYR A CD2 1 ATOM 98 C CE1 . TYR A 1 14 ? 29.917 0.671 34.810 1.00 21.92 ? 14 TYR A CE1 1 ATOM 99 C CE2 . TYR A 1 14 ? 32.135 0.027 35.489 1.00 22.39 ? 14 TYR A CE2 1 ATOM 100 C CZ . TYR A 1 14 ? 31.220 0.316 34.490 1.00 22.31 ? 14 TYR A CZ 1 ATOM 101 O OH . TYR A 1 14 ? 31.617 0.242 33.176 1.00 24.97 ? 14 TYR A OH 1 ATOM 102 N N . ILE A 1 15 ? 28.710 -2.258 37.346 1.00 14.18 ? 15 ILE A N 1 ATOM 103 C CA . ILE A 1 15 ? 27.710 -2.865 36.474 1.00 15.91 ? 15 ILE A CA 1 ATOM 104 C C . ILE A 1 15 ? 26.894 -3.964 37.174 1.00 15.64 ? 15 ILE A C 1 ATOM 105 O O . ILE A 1 15 ? 25.668 -4.006 37.042 1.00 14.05 ? 15 ILE A O 1 ATOM 106 C CB . ILE A 1 15 ? 28.370 -3.435 35.179 1.00 17.68 ? 15 ILE A CB 1 ATOM 107 C CG1 . ILE A 1 15 ? 28.639 -2.297 34.192 1.00 17.35 ? 15 ILE A CG1 1 ATOM 108 C CG2 . ILE A 1 15 ? 27.459 -4.457 34.517 1.00 19.26 ? 15 ILE A CG2 1 ATOM 109 C CD1 . ILE A 1 15 ? 27.365 -1.618 33.660 1.00 18.49 ? 15 ILE A CD1 1 ATOM 110 N N . THR A 1 16 ? 27.553 -4.848 37.920 1.00 14.51 ? 16 THR A N 1 ATOM 111 C CA . THR A 1 16 ? 26.815 -5.902 38.606 1.00 14.84 ? 16 THR A CA 1 ATOM 112 C C . THR A 1 16 ? 25.892 -5.292 39.674 1.00 15.39 ? 16 THR A C 1 ATOM 113 O O . THR A 1 16 ? 24.810 -5.824 39.963 1.00 14.04 ? 16 THR A O 1 ATOM 114 C CB . THR A 1 16 ? 27.770 -6.944 39.260 1.00 16.06 ? 16 THR A CB 1 ATOM 115 O OG1 . THR A 1 16 ? 28.526 -6.328 40.309 1.00 17.58 ? 16 THR A OG1 1 ATOM 116 C CG2 . THR A 1 16 ? 28.730 -7.516 38.217 1.00 17.43 ? 16 THR A CG2 1 ATOM 117 N N . TYR A 1 17 ? 26.317 -4.165 40.242 1.00 14.17 ? 17 TYR A N 1 ATOM 118 C CA . TYR A 1 17 ? 25.535 -3.464 41.263 1.00 12.75 ? 17 TYR A CA 1 ATOM 119 C C . TYR A 1 17 ? 24.259 -2.869 40.663 1.00 12.54 ? 17 TYR A C 1 ATOM 120 O O . TYR A 1 17 ? 23.169 -3.040 41.205 1.00 13.57 ? 17 TYR A O 1 ATOM 121 C CB . TYR A 1 17 ? 26.373 -2.345 41.885 1.00 11.92 ? 17 TYR A CB 1 ATOM 122 C CG . TYR A 1 17 ? 25.608 -1.447 42.836 1.00 10.96 ? 17 TYR A CG 1 ATOM 123 C CD1 . TYR A 1 17 ? 25.113 -1.932 44.045 1.00 11.97 ? 17 TYR A CD1 1 ATOM 124 C CD2 . TYR A 1 17 ? 25.395 -0.106 42.532 1.00 10.20 ? 17 TYR A CD2 1 ATOM 125 C CE1 . TYR A 1 17 ? 24.424 -1.092 44.935 1.00 12.10 ? 17 TYR A CE1 1 ATOM 126 C CE2 . TYR A 1 17 ? 24.711 0.740 43.410 1.00 12.45 ? 17 TYR A CE2 1 ATOM 127 C CZ . TYR A 1 17 ? 24.231 0.242 44.608 1.00 12.34 ? 17 TYR A CZ 1 ATOM 128 O OH . TYR A 1 17 ? 23.576 1.086 45.475 1.00 11.24 ? 17 TYR A OH 1 ATOM 129 N N . VAL A 1 18 ? 24.396 -2.166 39.544 1.00 12.63 ? 18 VAL A N 1 ATOM 130 C CA . VAL A 1 18 ? 23.240 -1.567 38.885 1.00 12.10 ? 18 VAL A CA 1 ATOM 131 C C . VAL A 1 18 ? 22.252 -2.641 38.413 1.00 12.99 ? 18 VAL A C 1 ATOM 132 O O . VAL A 1 18 ? 21.037 -2.496 38.594 1.00 12.37 ? 18 VAL A O 1 ATOM 133 C CB . VAL A 1 18 ? 23.678 -0.702 37.682 1.00 11.79 ? 18 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 18 ? 22.468 -0.291 36.858 1.00 12.10 ? 18 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 18 ? 24.415 0.525 38.187 1.00 10.01 ? 18 VAL A CG2 1 ATOM 136 N N . ASN A 1 19 ? 22.763 -3.720 37.819 1.00 13.11 ? 19 ASN A N 1 ATOM 137 C CA . ASN A 1 19 ? 21.893 -4.803 37.349 1.00 13.80 ? 19 ASN A CA 1 ATOM 138 C C . ASN A 1 19 ? 21.113 -5.398 38.525 1.00 14.00 ? 19 ASN A C 1 ATOM 139 O O . ASN A 1 19 ? 19.934 -5.757 38.394 1.00 13.15 ? 19 ASN A O 1 ATOM 140 C CB . ASN A 1 19 ? 22.725 -5.876 36.641 1.00 15.57 ? 19 ASN A CB 1 ATOM 141 C CG . ASN A 1 19 ? 23.161 -5.447 35.243 1.00 18.36 ? 19 ASN A CG 1 ATOM 142 O OD1 . ASN A 1 19 ? 24.218 -5.858 34.749 1.00 21.15 ? 19 ASN A OD1 1 ATOM 143 N ND2 . ASN A 1 19 ? 22.341 -4.625 34.597 1.00 17.68 ? 19 ASN A ND2 1 ATOM 144 N N . PHE A 1 20 ? 21.781 -5.486 39.674 1.00 14.28 ? 20 PHE A N 1 ATOM 145 C CA . PHE A 1 20 ? 21.177 -5.987 40.909 1.00 13.21 ? 20 PHE A CA 1 ATOM 146 C C . PHE A 1 20 ? 20.004 -5.081 41.316 1.00 12.62 ? 20 PHE A C 1 ATOM 147 O O . PHE A 1 20 ? 18.886 -5.558 41.540 1.00 11.67 ? 20 PHE A O 1 ATOM 148 C CB . PHE A 1 20 ? 22.248 -6.033 42.012 1.00 14.39 ? 20 PHE A CB 1 ATOM 149 C CG . PHE A 1 20 ? 21.699 -5.963 43.408 1.00 14.47 ? 20 PHE A CG 1 ATOM 150 C CD1 . PHE A 1 20 ? 20.882 -6.975 43.907 1.00 15.35 ? 20 PHE A CD1 1 ATOM 151 C CD2 . PHE A 1 20 ? 21.967 -4.856 44.211 1.00 15.29 ? 20 PHE A CD2 1 ATOM 152 C CE1 . PHE A 1 20 ? 20.331 -6.887 45.190 1.00 14.81 ? 20 PHE A CE1 1 ATOM 153 C CE2 . PHE A 1 20 ? 21.422 -4.755 45.493 1.00 15.75 ? 20 PHE A CE2 1 ATOM 154 C CZ . PHE A 1 20 ? 20.600 -5.776 45.983 1.00 15.75 ? 20 PHE A CZ 1 ATOM 155 N N . LEU A 1 21 ? 20.255 -3.776 41.398 1.00 11.80 ? 21 LEU A N 1 ATOM 156 C CA . LEU A 1 21 ? 19.205 -2.832 41.767 1.00 12.32 ? 21 LEU A CA 1 ATOM 157 C C . LEU A 1 21 ? 17.986 -2.940 40.858 1.00 11.63 ? 21 LEU A C 1 ATOM 158 O O . LEU A 1 21 ? 16.851 -2.896 41.335 1.00 11.91 ? 21 LEU A O 1 ATOM 159 C CB . LEU A 1 21 ? 19.725 -1.390 41.731 1.00 11.66 ? 21 LEU A CB 1 ATOM 160 C CG . LEU A 1 21 ? 20.724 -0.970 42.805 1.00 12.24 ? 21 LEU A CG 1 ATOM 161 C CD1 . LEU A 1 21 ? 21.161 0.463 42.547 1.00 12.10 ? 21 LEU A CD1 1 ATOM 162 C CD2 . LEU A 1 21 ? 20.087 -1.100 44.177 1.00 11.25 ? 21 LEU A CD2 1 ATOM 163 N N . ASN A 1 22 ? 18.210 -3.074 39.553 1.00 11.91 ? 22 ASN A N 1 ATOM 164 C CA . ASN A 1 22 ? 17.084 -3.174 38.630 1.00 13.67 ? 22 ASN A CA 1 ATOM 165 C C . ASN A 1 22 ? 16.331 -4.498 38.735 1.00 14.21 ? 22 ASN A C 1 ATOM 166 O O . ASN A 1 22 ? 15.157 -4.585 38.379 1.00 12.85 ? 22 ASN A O 1 ATOM 167 C CB . ASN A 1 22 ? 17.548 -2.909 37.201 1.00 13.58 ? 22 ASN A CB 1 ATOM 168 C CG . ASN A 1 22 ? 17.771 -1.436 36.946 1.00 15.78 ? 22 ASN A CG 1 ATOM 169 O OD1 . ASN A 1 22 ? 16.931 -0.606 37.303 1.00 14.66 ? 22 ASN A OD1 1 ATOM 170 N ND2 . ASN A 1 22 ? 18.900 -1.097 36.332 1.00 17.69 ? 22 ASN A ND2 1 ATOM 171 N N . GLU A 1 23 ? 17.006 -5.524 39.240 1.00 15.20 ? 23 GLU A N 1 ATOM 172 C CA . GLU A 1 23 ? 16.358 -6.812 39.423 1.00 16.09 ? 23 GLU A CA 1 ATOM 173 C C . GLU A 1 23 ? 15.438 -6.666 40.633 1.00 14.07 ? 23 GLU A C 1 ATOM 174 O O . GLU A 1 23 ? 14.311 -7.158 40.645 1.00 14.76 ? 23 GLU A O 1 ATOM 175 C CB . GLU A 1 23 ? 17.394 -7.898 39.693 1.00 19.36 ? 23 GLU A CB 1 ATOM 176 C CG . GLU A 1 23 ? 16.808 -9.295 39.658 1.00 24.77 ? 23 GLU A CG 1 ATOM 177 C CD . GLU A 1 23 ? 17.838 -10.371 39.936 1.00 30.06 ? 23 GLU A CD 1 ATOM 178 O OE1 . GLU A 1 23 ? 18.987 -10.253 39.433 1.00 31.34 ? 23 GLU A OE1 1 ATOM 179 O OE2 . GLU A 1 23 ? 17.490 -11.338 40.652 1.00 32.31 ? 23 GLU A OE2 1 ATOM 180 N N . LEU A 1 24 ? 15.929 -5.979 41.654 1.00 12.76 ? 24 LEU A N 1 ATOM 181 C CA . LEU A 1 24 ? 15.143 -5.752 42.860 1.00 12.83 ? 24 LEU A CA 1 ATOM 182 C C . LEU A 1 24 ? 13.912 -4.891 42.553 1.00 13.82 ? 24 LEU A C 1 ATOM 183 O O . LEU A 1 24 ? 12.806 -5.175 43.025 1.00 15.36 ? 24 LEU A O 1 ATOM 184 C CB . LEU A 1 24 ? 16.004 -5.057 43.914 1.00 12.14 ? 24 LEU A CB 1 ATOM 185 C CG . LEU A 1 24 ? 15.299 -4.590 45.188 1.00 12.60 ? 24 LEU A CG 1 ATOM 186 C CD1 . LEU A 1 24 ? 14.666 -5.774 45.907 1.00 11.89 ? 24 LEU A CD1 1 ATOM 187 C CD2 . LEU A 1 24 ? 16.312 -3.888 46.080 1.00 11.90 ? 24 LEU A CD2 1 ATOM 188 N N . ARG A 1 25 ? 14.109 -3.838 41.766 1.00 12.74 ? 25 ARG A N 1 ATOM 189 C CA . ARG A 1 25 ? 13.020 -2.936 41.404 1.00 13.47 ? 25 ARG A CA 1 ATOM 190 C C . ARG A 1 25 ? 11.885 -3.685 40.720 1.00 12.89 ? 25 ARG A C 1 ATOM 191 O O . ARG A 1 25 ? 10.718 -3.318 40.847 1.00 13.87 ? 25 ARG A O 1 ATOM 192 C CB . ARG A 1 25 ? 13.551 -1.819 40.499 1.00 12.08 ? 25 ARG A CB 1 ATOM 193 C CG . ARG A 1 25 ? 14.372 -0.786 41.253 1.00 12.74 ? 25 ARG A CG 1 ATOM 194 C CD . ARG A 1 25 ? 15.233 0.045 40.315 1.00 13.00 ? 25 ARG A CD 1 ATOM 195 N NE . ARG A 1 25 ? 15.897 1.142 41.017 1.00 11.81 ? 25 ARG A NE 1 ATOM 196 C CZ . ARG A 1 25 ? 16.894 1.859 40.510 1.00 11.14 ? 25 ARG A CZ 1 ATOM 197 N NH1 . ARG A 1 25 ? 17.347 1.589 39.296 1.00 10.87 ? 25 ARG A NH1 1 ATOM 198 N NH2 . ARG A 1 25 ? 17.431 2.851 41.210 1.00 9.37 ? 25 ARG A NH2 1 ATOM 199 N N . VAL A 1 26 ? 12.238 -4.739 39.996 1.00 13.75 ? 26 VAL A N 1 ATOM 200 C CA . VAL A 1 26 ? 11.261 -5.561 39.301 1.00 15.32 ? 26 VAL A CA 1 ATOM 201 C C . VAL A 1 26 ? 10.530 -6.492 40.270 1.00 15.90 ? 26 VAL A C 1 ATOM 202 O O . VAL A 1 26 ? 9.300 -6.590 40.246 1.00 15.70 ? 26 VAL A O 1 ATOM 203 C CB . VAL A 1 26 ? 11.946 -6.421 38.220 1.00 16.35 ? 26 VAL A CB 1 ATOM 204 C CG1 . VAL A 1 26 ? 10.949 -7.393 37.610 1.00 16.38 ? 26 VAL A CG1 1 ATOM 205 C CG2 . VAL A 1 26 ? 12.534 -5.521 37.153 1.00 18.39 ? 26 VAL A CG2 1 ATOM 206 N N . LYS A 1 27 ? 11.288 -7.163 41.134 1.00 15.64 ? 27 LYS A N 1 ATOM 207 C CA . LYS A 1 27 ? 10.701 -8.103 42.082 1.00 15.78 ? 27 LYS A CA 1 ATOM 208 C C . LYS A 1 27 ? 9.848 -7.488 43.183 1.00 16.72 ? 27 LYS A C 1 ATOM 209 O O . LYS A 1 27 ? 9.099 -8.197 43.864 1.00 15.84 ? 27 LYS A O 1 ATOM 210 C CB . LYS A 1 27 ? 11.800 -8.999 42.654 1.00 16.16 ? 27 LYS A CB 1 ATOM 211 C CG . LYS A 1 27 ? 12.406 -9.882 41.558 1.00 18.84 ? 27 LYS A CG 1 ATOM 212 C CD . LYS A 1 27 ? 13.351 -10.951 42.063 1.00 21.55 ? 27 LYS A CD 1 ATOM 213 C CE . LYS A 1 27 ? 13.801 -11.826 40.897 1.00 23.68 ? 27 LYS A CE 1 ATOM 214 N NZ . LYS A 1 27 ? 14.766 -12.886 41.296 1.00 25.08 ? 27 LYS A NZ 1 ATOM 215 N N . LEU A 1 28 ? 9.945 -6.172 43.361 1.00 16.62 ? 28 LEU A N 1 ATOM 216 C CA . LEU A 1 28 ? 9.110 -5.501 44.353 1.00 16.88 ? 28 LEU A CA 1 ATOM 217 C C . LEU A 1 28 ? 7.687 -5.444 43.769 1.00 17.72 ? 28 LEU A C 1 ATOM 218 O O . LEU A 1 28 ? 6.721 -5.128 44.464 1.00 17.51 ? 28 LEU A O 1 ATOM 219 C CB . LEU A 1 28 ? 9.630 -4.085 44.631 1.00 15.73 ? 28 LEU A CB 1 ATOM 220 C CG . LEU A 1 28 ? 10.901 -3.959 45.475 1.00 13.86 ? 28 LEU A CG 1 ATOM 221 C CD1 . LEU A 1 28 ? 11.413 -2.532 45.393 1.00 14.58 ? 28 LEU A CD1 1 ATOM 222 C CD2 . LEU A 1 28 ? 10.622 -4.342 46.921 1.00 12.15 ? 28 LEU A CD2 1 ATOM 223 N N . LYS A 1 29 ? 7.588 -5.749 42.476 1.00 18.12 ? 29 LYS A N 1 ATOM 224 C CA . LYS A 1 29 ? 6.325 -5.776 41.745 1.00 18.04 ? 29 LYS A CA 1 ATOM 225 C C . LYS A 1 29 ? 5.395 -4.581 41.930 1.00 18.19 ? 29 LYS A C 1 ATOM 226 O O . LYS A 1 29 ? 4.273 -4.727 42.422 1.00 18.33 ? 29 LYS A O 1 ATOM 227 C CB . LYS A 1 29 ? 5.555 -7.049 42.092 1.00 20.68 ? 29 LYS A CB 1 ATOM 228 C CG . LYS A 1 29 ? 6.140 -8.338 41.530 1.00 23.72 ? 29 LYS A CG 1 ATOM 229 C CD . LYS A 1 29 ? 5.302 -9.524 41.991 1.00 28.04 ? 29 LYS A CD 1 ATOM 230 C CE . LYS A 1 29 ? 5.555 -10.776 41.160 1.00 31.94 ? 29 LYS A CE 1 ATOM 231 N NZ . LYS A 1 29 ? 6.933 -11.310 41.315 1.00 34.94 ? 29 LYS A NZ 1 ATOM 232 N N . PRO A 1 30 ? 5.839 -3.381 41.538 1.00 17.59 ? 30 PRO A N 1 ATOM 233 C CA . PRO A 1 30 ? 4.949 -2.226 41.704 1.00 17.93 ? 30 PRO A CA 1 ATOM 234 C C . PRO A 1 30 ? 3.707 -2.396 40.820 1.00 19.08 ? 30 PRO A C 1 ATOM 235 O O . PRO A 1 30 ? 3.727 -3.179 39.870 1.00 17.52 ? 30 PRO A O 1 ATOM 236 C CB . PRO A 1 30 ? 5.825 -1.051 41.275 1.00 15.83 ? 30 PRO A CB 1 ATOM 237 C CG . PRO A 1 30 ? 6.756 -1.666 40.270 1.00 16.85 ? 30 PRO A CG 1 ATOM 238 C CD . PRO A 1 30 ? 7.112 -2.992 40.903 1.00 16.68 ? 30 PRO A CD 1 ATOM 239 N N . GLU A 1 31 ? 2.625 -1.692 41.134 1.00 19.98 ? 31 GLU A N 1 ATOM 240 C CA . GLU A 1 31 ? 1.410 -1.802 40.325 1.00 22.55 ? 31 GLU A CA 1 ATOM 241 C C . GLU A 1 31 ? 1.031 -0.473 39.709 1.00 21.82 ? 31 GLU A C 1 ATOM 242 O O . GLU A 1 31 ? 0.639 0.463 40.408 1.00 21.54 ? 31 GLU A O 1 ATOM 243 C CB . GLU A 1 31 ? 0.237 -2.317 41.156 1.00 24.76 ? 31 GLU A CB 1 ATOM 244 C CG . GLU A 1 31 ? 0.246 -3.813 41.335 1.00 31.54 ? 31 GLU A CG 1 ATOM 245 C CD . GLU A 1 31 ? -0.882 -4.303 42.216 1.00 35.43 ? 31 GLU A CD 1 ATOM 246 O OE1 . GLU A 1 31 ? -0.981 -5.536 42.411 1.00 38.17 ? 31 GLU A OE1 1 ATOM 247 O OE2 . GLU A 1 31 ? -1.666 -3.461 42.714 1.00 37.61 ? 31 GLU A OE2 1 ATOM 248 N N . GLY A 1 32 ? 1.146 -0.392 38.392 1.00 20.40 ? 32 GLY A N 1 ATOM 249 C CA . GLY A 1 32 ? 0.808 0.843 37.724 1.00 20.09 ? 32 GLY A CA 1 ATOM 250 C C . GLY A 1 32 ? 1.913 1.859 37.899 1.00 20.22 ? 32 GLY A C 1 ATOM 251 O O . GLY A 1 32 ? 3.054 1.508 38.202 1.00 20.46 ? 32 GLY A O 1 ATOM 252 N N . ASN A 1 33 ? 1.566 3.128 37.737 1.00 19.25 ? 33 ASN A N 1 ATOM 253 C CA . ASN A 1 33 ? 2.548 4.194 37.833 1.00 20.01 ? 33 ASN A CA 1 ATOM 254 C C . ASN A 1 33 ? 1.833 5.515 38.023 1.00 20.44 ? 33 ASN A C 1 ATOM 255 O O . ASN A 1 33 ? 0.612 5.595 37.902 1.00 21.06 ? 33 ASN A O 1 ATOM 256 C CB . ASN A 1 33 ? 3.328 4.273 36.522 1.00 18.73 ? 33 ASN A CB 1 ATOM 257 C CG . ASN A 1 33 ? 2.450 4.743 35.355 1.00 19.87 ? 33 ASN A CG 1 ATOM 258 O OD1 . ASN A 1 33 ? 2.128 5.932 35.235 1.00 18.07 ? 33 ASN A OD1 1 ATOM 259 N ND2 . ASN A 1 33 ? 2.042 3.806 34.507 1.00 18.67 ? 33 ASN A ND2 1 ATOM 260 N N . SER A 1 34 ? 2.604 6.551 38.318 1.00 19.46 ? 34 SER A N 1 ATOM 261 C CA . SER A 1 34 ? 2.054 7.887 38.442 1.00 18.81 ? 34 SER A CA 1 ATOM 262 C C . SER A 1 34 ? 2.964 8.755 37.578 1.00 18.85 ? 34 SER A C 1 ATOM 263 O O . SER A 1 34 ? 4.168 8.836 37.822 1.00 18.40 ? 34 SER A O 1 ATOM 264 C CB . SER A 1 34 ? 2.075 8.374 39.889 1.00 18.60 ? 34 SER A CB 1 ATOM 265 O OG . SER A 1 34 ? 1.484 9.664 39.975 1.00 18.36 ? 34 SER A OG 1 ATOM 266 N N . HIS A 1 35 ? 2.394 9.375 36.550 1.00 18.34 ? 35 HIS A N 1 ATOM 267 C CA . HIS A 1 35 ? 3.170 10.226 35.653 1.00 19.44 ? 35 HIS A CA 1 ATOM 268 C C . HIS A 1 35 ? 4.335 9.462 35.029 1.00 17.58 ? 35 HIS A C 1 ATOM 269 O O . HIS A 1 35 ? 5.371 10.047 34.714 1.00 18.69 ? 35 HIS A O 1 ATOM 270 C CB . HIS A 1 35 ? 3.698 11.447 36.415 1.00 21.65 ? 35 HIS A CB 1 ATOM 271 C CG . HIS A 1 35 ? 2.620 12.357 36.921 1.00 24.14 ? 35 HIS A CG 1 ATOM 272 N ND1 . HIS A 1 35 ? 2.165 13.445 36.204 1.00 25.01 ? 35 HIS A ND1 1 ATOM 273 C CD2 . HIS A 1 35 ? 1.897 12.332 38.067 1.00 23.59 ? 35 HIS A CD2 1 ATOM 274 C CE1 . HIS A 1 35 ? 1.211 14.052 36.888 1.00 24.61 ? 35 HIS A CE1 1 ATOM 275 N NE2 . HIS A 1 35 ? 1.029 13.397 38.021 1.00 24.81 ? 35 HIS A NE2 1 ATOM 276 N N . GLY A 1 36 ? 4.157 8.155 34.863 1.00 15.53 ? 36 GLY A N 1 ATOM 277 C CA . GLY A 1 36 ? 5.185 7.325 34.260 1.00 15.17 ? 36 GLY A CA 1 ATOM 278 C C . GLY A 1 36 ? 6.154 6.665 35.224 1.00 16.39 ? 36 GLY A C 1 ATOM 279 O O . GLY A 1 36 ? 6.944 5.794 34.828 1.00 17.85 ? 36 GLY A O 1 ATOM 280 N N . ILE A 1 37 ? 6.113 7.077 36.487 1.00 14.42 ? 37 ILE A N 1 ATOM 281 C CA . ILE A 1 37 ? 7.001 6.517 37.493 1.00 13.74 ? 37 ILE A CA 1 ATOM 282 C C . ILE A 1 37 ? 6.328 5.324 38.158 1.00 14.24 ? 37 ILE A C 1 ATOM 283 O O . ILE A 1 37 ? 5.186 5.423 38.605 1.00 15.74 ? 37 ILE A O 1 ATOM 284 C CB . ILE A 1 37 ? 7.340 7.567 38.567 1.00 14.48 ? 37 ILE A CB 1 ATOM 285 C CG1 . ILE A 1 37 ? 7.854 8.843 37.890 1.00 12.24 ? 37 ILE A CG1 1 ATOM 286 C CG2 . ILE A 1 37 ? 8.370 6.998 39.549 1.00 10.31 ? 37 ILE A CG2 1 ATOM 287 C CD1 . ILE A 1 37 ? 7.924 10.035 38.816 1.00 13.88 ? 37 ILE A CD1 1 ATOM 288 N N . PRO A 1 38 ? 7.021 4.173 38.219 1.00 14.04 ? 38 PRO A N 1 ATOM 289 C CA . PRO A 1 38 ? 6.451 2.976 38.843 1.00 14.28 ? 38 PRO A CA 1 ATOM 290 C C . PRO A 1 38 ? 5.920 3.277 40.245 1.00 15.39 ? 38 PRO A C 1 ATOM 291 O O . PRO A 1 38 ? 6.575 3.951 41.040 1.00 16.22 ? 38 PRO A O 1 ATOM 292 C CB . PRO A 1 38 ? 7.627 2.000 38.850 1.00 14.93 ? 38 PRO A CB 1 ATOM 293 C CG . PRO A 1 38 ? 8.371 2.370 37.595 1.00 13.71 ? 38 PRO A CG 1 ATOM 294 C CD . PRO A 1 38 ? 8.362 3.891 37.668 1.00 14.21 ? 38 PRO A CD 1 ATOM 295 N N . LEU A 1 39 ? 4.726 2.771 40.532 1.00 14.94 ? 39 LEU A N 1 ATOM 296 C CA . LEU A 1 39 ? 4.060 2.988 41.810 1.00 15.22 ? 39 LEU A CA 1 ATOM 297 C C . LEU A 1 39 ? 3.941 1.686 42.616 1.00 15.07 ? 39 LEU A C 1 ATOM 298 O O . LEU A 1 39 ? 3.293 0.721 42.183 1.00 14.10 ? 39 LEU A O 1 ATOM 299 C CB . LEU A 1 39 ? 2.674 3.577 41.544 1.00 15.53 ? 39 LEU A CB 1 ATOM 300 C CG . LEU A 1 39 ? 1.774 3.969 42.708 1.00 16.39 ? 39 LEU A CG 1 ATOM 301 C CD1 . LEU A 1 39 ? 2.426 5.047 43.561 1.00 16.45 ? 39 LEU A CD1 1 ATOM 302 C CD2 . LEU A 1 39 ? 0.466 4.473 42.129 1.00 16.38 ? 39 LEU A CD2 1 ATOM 303 N N . LEU A 1 40 ? 4.572 1.666 43.788 1.00 13.95 ? 40 LEU A N 1 ATOM 304 C CA . LEU A 1 40 ? 4.546 0.484 44.644 1.00 16.05 ? 40 LEU A CA 1 ATOM 305 C C . LEU A 1 40 ? 3.121 0.175 45.103 1.00 18.21 ? 40 LEU A C 1 ATOM 306 O O . LEU A 1 40 ? 2.290 1.079 45.256 1.00 17.30 ? 40 LEU A O 1 ATOM 307 C CB . LEU A 1 40 ? 5.467 0.683 45.859 1.00 13.65 ? 40 LEU A CB 1 ATOM 308 C CG . LEU A 1 40 ? 6.962 0.859 45.547 1.00 12.38 ? 40 LEU A CG 1 ATOM 309 C CD1 . LEU A 1 40 ? 7.717 1.245 46.810 1.00 10.78 ? 40 LEU A CD1 1 ATOM 310 C CD2 . LEU A 1 40 ? 7.519 -0.435 44.960 1.00 11.68 ? 40 LEU A CD2 1 ATOM 311 N N . ARG A 1 41 ? 2.838 -1.108 45.297 1.00 20.95 ? 41 ARG A N 1 ATOM 312 C CA . ARG A 1 41 ? 1.518 -1.536 45.743 1.00 23.36 ? 41 ARG A CA 1 ATOM 313 C C . ARG A 1 41 ? 1.138 -0.812 47.026 1.00 24.62 ? 41 ARG A C 1 ATOM 314 O O . ARG A 1 41 ? 1.971 -0.589 47.902 1.00 24.05 ? 41 ARG A O 1 ATOM 315 C CB . ARG A 1 41 ? 1.500 -3.049 45.975 1.00 23.77 ? 41 ARG A CB 1 ATOM 316 C CG . ARG A 1 41 ? 1.451 -3.869 44.692 1.00 26.52 ? 41 ARG A CG 1 ATOM 317 C CD . ARG A 1 41 ? 1.606 -5.368 44.972 1.00 27.85 ? 41 ARG A CD 1 ATOM 318 N NE . ARG A 1 41 ? 2.993 -5.745 45.242 1.00 27.95 ? 41 ARG A NE 1 ATOM 319 C CZ . ARG A 1 41 ? 3.392 -6.984 45.518 1.00 28.16 ? 41 ARG A CZ 1 ATOM 320 N NH1 . ARG A 1 41 ? 4.673 -7.236 45.742 1.00 27.63 ? 41 ARG A NH1 1 ATOM 321 N NH2 . ARG A 1 41 ? 2.510 -7.971 45.578 1.00 29.30 ? 41 ARG A NH2 1 ATOM 322 N N . LYS A 1 42 ? -0.130 -0.436 47.121 1.00 27.07 ? 42 LYS A N 1 ATOM 323 C CA . LYS A 1 42 ? -0.635 0.267 48.288 1.00 30.08 ? 42 LYS A CA 1 ATOM 324 C C . LYS A 1 42 ? -0.667 -0.661 49.500 1.00 31.18 ? 42 LYS A C 1 ATOM 325 O O . LYS A 1 42 ? -0.191 -0.305 50.579 1.00 30.87 ? 42 LYS A O 1 ATOM 326 C CB . LYS A 1 42 ? -2.036 0.791 47.990 1.00 30.63 ? 42 LYS A CB 1 ATOM 327 C CG . LYS A 1 42 ? -2.652 1.634 49.085 1.00 34.93 ? 42 LYS A CG 1 ATOM 328 C CD . LYS A 1 42 ? -3.982 2.194 48.595 1.00 38.79 ? 42 LYS A CD 1 ATOM 329 C CE . LYS A 1 42 ? -4.593 3.166 49.583 1.00 40.38 ? 42 LYS A CE 1 ATOM 330 N NZ . LYS A 1 42 ? -5.653 3.991 48.926 1.00 41.63 ? 42 LYS A NZ 1 ATOM 331 N N . LYS A 1 43 ? -1.224 -1.853 49.312 1.00 32.58 ? 43 LYS A N 1 ATOM 332 C CA . LYS A 1 43 ? -1.321 -2.827 50.394 1.00 35.61 ? 43 LYS A CA 1 ATOM 333 C C . LYS A 1 43 ? -0.825 -4.212 50.017 1.00 35.73 ? 43 LYS A C 1 ATOM 334 O O . LYS A 1 43 ? -0.941 -4.651 48.873 1.00 36.19 ? 43 LYS A O 1 ATOM 335 C CB . LYS A 1 43 ? -2.767 -2.938 50.902 1.00 37.55 ? 43 LYS A CB 1 ATOM 336 C CG . LYS A 1 43 ? -3.183 -1.819 51.841 1.00 41.25 ? 43 LYS A CG 1 ATOM 337 C CD . LYS A 1 43 ? -4.479 -2.152 52.559 1.00 45.01 ? 43 LYS A CD 1 ATOM 338 C CE . LYS A 1 43 ? -4.783 -1.122 53.645 1.00 47.89 ? 43 LYS A CE 1 ATOM 339 N NZ . LYS A 1 43 ? -5.977 -1.480 54.475 1.00 48.23 ? 43 LYS A NZ 1 ATOM 340 N N . CYS A 1 44 ? -0.275 -4.896 51.008 1.00 36.18 ? 44 CYS A N 1 ATOM 341 C CA . CYS A 1 44 ? 0.253 -6.239 50.841 1.00 37.10 ? 44 CYS A CA 1 ATOM 342 C C . CYS A 1 44 ? 0.622 -6.629 52.259 1.00 38.86 ? 44 CYS A C 1 ATOM 343 O O . CYS A 1 44 ? 1.755 -6.419 52.696 1.00 39.10 ? 44 CYS A O 1 ATOM 344 C CB . CYS A 1 44 ? 1.498 -6.212 49.956 1.00 35.18 ? 44 CYS A CB 1 ATOM 345 S SG . CYS A 1 44 ? 2.016 -7.840 49.331 1.00 33.78 ? 44 CYS A SG 1 ATOM 346 N N . ASP A 1 45 ? -0.340 -7.197 52.976 1.00 40.79 ? 45 ASP A N 1 ATOM 347 C CA . ASP A 1 45 ? -0.124 -7.564 54.366 1.00 43.51 ? 45 ASP A CA 1 ATOM 348 C C . ASP A 1 45 ? 0.278 -9.010 54.666 1.00 42.35 ? 45 ASP A C 1 ATOM 349 O O . ASP A 1 45 ? 0.779 -9.293 55.750 1.00 42.85 ? 45 ASP A O 1 ATOM 350 C CB . ASP A 1 45 ? -1.366 -7.180 55.172 1.00 46.88 ? 45 ASP A CB 1 ATOM 351 C CG . ASP A 1 45 ? -1.868 -5.784 54.824 1.00 50.08 ? 45 ASP A CG 1 ATOM 352 O OD1 . ASP A 1 45 ? -1.029 -4.861 54.706 1.00 51.46 ? 45 ASP A OD1 1 ATOM 353 O OD2 . ASP A 1 45 ? -3.100 -5.609 54.671 1.00 52.41 ? 45 ASP A OD2 1 ATOM 354 N N . ASP A 1 46 ? 0.073 -9.919 53.719 1.00 40.56 ? 46 ASP A N 1 ATOM 355 C CA . ASP A 1 46 ? 0.445 -11.315 53.929 1.00 39.02 ? 46 ASP A CA 1 ATOM 356 C C . ASP A 1 46 ? 1.976 -11.503 53.877 1.00 37.99 ? 46 ASP A C 1 ATOM 357 O O . ASP A 1 46 ? 2.588 -11.460 52.806 1.00 37.08 ? 46 ASP A O 1 ATOM 358 C CB . ASP A 1 46 ? -0.253 -12.193 52.882 1.00 40.01 ? 46 ASP A CB 1 ATOM 359 C CG . ASP A 1 46 ? 0.093 -13.666 53.025 1.00 43.12 ? 46 ASP A CG 1 ATOM 360 O OD1 . ASP A 1 46 ? 0.383 -14.107 54.158 1.00 44.16 ? 46 ASP A OD1 1 ATOM 361 O OD2 . ASP A 1 46 ? 0.063 -14.390 52.006 1.00 45.59 ? 46 ASP A OD2 1 ATOM 362 N N . PRO A 1 47 ? 2.614 -11.718 55.043 1.00 36.38 ? 47 PRO A N 1 ATOM 363 C CA . PRO A 1 47 ? 4.068 -11.904 55.104 1.00 35.22 ? 47 PRO A CA 1 ATOM 364 C C . PRO A 1 47 ? 4.558 -12.970 54.140 1.00 35.09 ? 47 PRO A C 1 ATOM 365 O O . PRO A 1 47 ? 5.706 -12.938 53.702 1.00 35.84 ? 47 PRO A O 1 ATOM 366 C CB . PRO A 1 47 ? 4.304 -12.308 56.556 1.00 34.39 ? 47 PRO A CB 1 ATOM 367 C CG . PRO A 1 47 ? 3.197 -11.629 57.277 1.00 35.16 ? 47 PRO A CG 1 ATOM 368 C CD . PRO A 1 47 ? 2.018 -11.882 56.378 1.00 34.93 ? 47 PRO A CD 1 ATOM 369 N N . GLY A 1 48 ? 3.675 -13.911 53.819 1.00 35.58 ? 48 GLY A N 1 ATOM 370 C CA . GLY A 1 48 ? 4.014 -15.004 52.922 1.00 35.05 ? 48 GLY A CA 1 ATOM 371 C C . GLY A 1 48 ? 4.308 -14.622 51.482 1.00 35.54 ? 48 GLY A C 1 ATOM 372 O O . GLY A 1 48 ? 4.831 -15.435 50.720 1.00 36.84 ? 48 GLY A O 1 ATOM 373 N N . LYS A 1 49 ? 3.974 -13.397 51.095 1.00 35.53 ? 49 LYS A N 1 ATOM 374 C CA . LYS A 1 49 ? 4.237 -12.956 49.729 1.00 35.43 ? 49 LYS A CA 1 ATOM 375 C C . LYS A 1 49 ? 4.355 -11.439 49.590 1.00 32.84 ? 49 LYS A C 1 ATOM 376 O O . LYS A 1 49 ? 4.165 -10.881 48.502 1.00 31.62 ? 49 LYS A O 1 ATOM 377 C CB . LYS A 1 49 ? 3.157 -13.502 48.792 1.00 38.64 ? 49 LYS A CB 1 ATOM 378 C CG . LYS A 1 49 ? 1.740 -13.416 49.328 1.00 40.95 ? 49 LYS A CG 1 ATOM 379 C CD . LYS A 1 49 ? 0.787 -14.114 48.374 1.00 44.19 ? 49 LYS A CD 1 ATOM 380 C CE . LYS A 1 49 ? -0.660 -13.958 48.812 1.00 46.48 ? 49 LYS A CE 1 ATOM 381 N NZ . LYS A 1 49 ? -1.592 -14.505 47.780 1.00 48.70 ? 49 LYS A NZ 1 ATOM 382 N N . CYS A 1 50 ? 4.696 -10.780 50.693 1.00 29.33 ? 50 CYS A N 1 ATOM 383 C CA . CYS A 1 50 ? 4.839 -9.332 50.691 1.00 26.80 ? 50 CYS A CA 1 ATOM 384 C C . CYS A 1 50 ? 6.234 -8.866 51.073 1.00 23.57 ? 50 CYS A C 1 ATOM 385 O O . CYS A 1 50 ? 6.431 -7.726 51.494 1.00 21.43 ? 50 CYS A O 1 ATOM 386 C CB . CYS A 1 50 ? 3.797 -8.712 51.612 1.00 28.29 ? 50 CYS A CB 1 ATOM 387 S SG . CYS A 1 50 ? 2.106 -8.998 50.998 1.00 31.55 ? 50 CYS A SG 1 ATOM 388 N N . PHE A 1 51 ? 7.203 -9.758 50.906 1.00 21.02 ? 51 PHE A N 1 ATOM 389 C CA . PHE A 1 51 ? 8.592 -9.449 51.205 1.00 18.67 ? 51 PHE A CA 1 ATOM 390 C C . PHE A 1 51 ? 9.503 -10.036 50.136 1.00 18.17 ? 51 PHE A C 1 ATOM 391 O O . PHE A 1 51 ? 9.209 -11.087 49.561 1.00 19.57 ? 51 PHE A O 1 ATOM 392 C CB . PHE A 1 51 ? 8.979 -10.022 52.573 1.00 17.55 ? 51 PHE A CB 1 ATOM 393 C CG . PHE A 1 51 ? 8.397 -9.268 53.731 1.00 17.18 ? 51 PHE A CG 1 ATOM 394 C CD1 . PHE A 1 51 ? 8.981 -8.079 54.170 1.00 15.96 ? 51 PHE A CD1 1 ATOM 395 C CD2 . PHE A 1 51 ? 7.243 -9.727 54.366 1.00 17.72 ? 51 PHE A CD2 1 ATOM 396 C CE1 . PHE A 1 51 ? 8.424 -7.352 55.225 1.00 14.13 ? 51 PHE A CE1 1 ATOM 397 C CE2 . PHE A 1 51 ? 6.677 -9.009 55.421 1.00 17.19 ? 51 PHE A CE2 1 ATOM 398 C CZ . PHE A 1 51 ? 7.272 -7.816 55.849 1.00 15.14 ? 51 PHE A CZ 1 ATOM 399 N N . VAL A 1 52 ? 10.604 -9.342 49.864 1.00 17.20 ? 52 VAL A N 1 ATOM 400 C CA . VAL A 1 52 ? 11.590 -9.812 48.899 1.00 16.37 ? 52 VAL A CA 1 ATOM 401 C C . VAL A 1 52 ? 12.877 -10.032 49.697 1.00 17.00 ? 52 VAL A C 1 ATOM 402 O O . VAL A 1 52 ? 13.277 -9.165 50.485 1.00 16.51 ? 52 VAL A O 1 ATOM 403 C CB . VAL A 1 52 ? 11.848 -8.762 47.782 1.00 15.28 ? 52 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 52 ? 13.041 -9.170 46.940 1.00 15.17 ? 52 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 52 ? 10.632 -8.632 46.900 1.00 16.13 ? 52 VAL A CG2 1 ATOM 406 N N . LEU A 1 53 ? 13.508 -11.191 49.522 1.00 16.15 ? 53 LEU A N 1 ATOM 407 C CA . LEU A 1 53 ? 14.753 -11.482 50.224 1.00 17.11 ? 53 LEU A CA 1 ATOM 408 C C . LEU A 1 53 ? 15.959 -11.095 49.374 1.00 16.66 ? 53 LEU A C 1 ATOM 409 O O . LEU A 1 53 ? 16.072 -11.493 48.213 1.00 18.15 ? 53 LEU A O 1 ATOM 410 C CB . LEU A 1 53 ? 14.857 -12.968 50.574 1.00 18.09 ? 53 LEU A CB 1 ATOM 411 C CG . LEU A 1 53 ? 13.921 -13.514 51.649 1.00 22.18 ? 53 LEU A CG 1 ATOM 412 C CD1 . LEU A 1 53 ? 14.292 -14.965 51.933 1.00 22.86 ? 53 LEU A CD1 1 ATOM 413 C CD2 . LEU A 1 53 ? 14.037 -12.678 52.916 1.00 21.41 ? 53 LEU A CD2 1 ATOM 414 N N . VAL A 1 54 ? 16.854 -10.308 49.953 1.00 14.65 ? 54 VAL A N 1 ATOM 415 C CA . VAL A 1 54 ? 18.058 -9.890 49.247 1.00 14.32 ? 54 VAL A CA 1 ATOM 416 C C . VAL A 1 54 ? 19.220 -10.635 49.883 1.00 12.61 ? 54 VAL A C 1 ATOM 417 O O . VAL A 1 54 ? 19.523 -10.426 51.056 1.00 11.92 ? 54 VAL A O 1 ATOM 418 C CB . VAL A 1 54 ? 18.307 -8.354 49.378 1.00 14.75 ? 54 VAL A CB 1 ATOM 419 C CG1 . VAL A 1 54 ? 19.607 -7.978 48.679 1.00 13.49 ? 54 VAL A CG1 1 ATOM 420 C CG2 . VAL A 1 54 ? 17.147 -7.575 48.773 1.00 12.92 ? 54 VAL A CG2 1 ATOM 421 N N . ALA A 1 55 ? 19.862 -11.504 49.110 1.00 12.49 ? 55 ALA A N 1 ATOM 422 C CA . ALA A 1 55 ? 20.992 -12.290 49.604 1.00 13.45 ? 55 ALA A CA 1 ATOM 423 C C . ALA A 1 55 ? 22.317 -11.577 49.329 1.00 13.24 ? 55 ALA A C 1 ATOM 424 O O . ALA A 1 55 ? 22.782 -11.520 48.193 1.00 13.50 ? 55 ALA A O 1 ATOM 425 C CB . ALA A 1 55 ? 20.986 -13.685 48.948 1.00 13.19 ? 55 ALA A CB 1 ATOM 426 N N . LEU A 1 56 ? 22.906 -11.022 50.383 1.00 13.59 ? 56 LEU A N 1 ATOM 427 C CA . LEU A 1 56 ? 24.168 -10.295 50.290 1.00 13.78 ? 56 LEU A CA 1 ATOM 428 C C . LEU A 1 56 ? 25.313 -11.169 50.795 1.00 14.45 ? 56 LEU A C 1 ATOM 429 O O . LEU A 1 56 ? 25.293 -11.619 51.940 1.00 14.56 ? 56 LEU A O 1 ATOM 430 C CB . LEU A 1 56 ? 24.108 -9.023 51.151 1.00 13.77 ? 56 LEU A CB 1 ATOM 431 C CG . LEU A 1 56 ? 22.915 -8.081 50.971 1.00 11.84 ? 56 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 56 ? 23.000 -6.939 51.985 1.00 11.14 ? 56 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 56 ? 22.903 -7.550 49.550 1.00 14.63 ? 56 LEU A CD2 1 ATOM 434 N N . SER A 1 57 ? 26.312 -11.403 49.951 1.00 14.91 ? 57 SER A N 1 ATOM 435 C CA . SER A 1 57 ? 27.453 -12.220 50.357 1.00 15.87 ? 57 SER A CA 1 ATOM 436 C C . SER A 1 57 ? 28.758 -11.538 49.966 1.00 16.78 ? 57 SER A C 1 ATOM 437 O O . SER A 1 57 ? 28.852 -10.924 48.910 1.00 15.66 ? 57 SER A O 1 ATOM 438 C CB . SER A 1 57 ? 27.362 -13.620 49.727 1.00 15.68 ? 57 SER A CB 1 ATOM 439 O OG . SER A 1 57 ? 27.343 -13.561 48.314 1.00 18.43 ? 57 SER A OG 1 ATOM 440 N N . ASN A 1 58 ? 29.771 -11.634 50.818 1.00 18.10 ? 58 ASN A N 1 ATOM 441 C CA . ASN A 1 58 ? 31.032 -10.986 50.498 1.00 19.91 ? 58 ASN A CA 1 ATOM 442 C C . ASN A 1 58 ? 32.074 -11.945 49.921 1.00 22.21 ? 58 ASN A C 1 ATOM 443 O O . ASN A 1 58 ? 31.781 -13.099 49.609 1.00 22.61 ? 58 ASN A O 1 ATOM 444 C CB . ASN A 1 58 ? 31.592 -10.248 51.728 1.00 18.47 ? 58 ASN A CB 1 ATOM 445 C CG . ASN A 1 58 ? 31.791 -11.157 52.930 1.00 19.92 ? 58 ASN A CG 1 ATOM 446 O OD1 . ASN A 1 58 ? 32.046 -12.352 52.788 1.00 20.27 ? 58 ASN A OD1 1 ATOM 447 N ND2 . ASN A 1 58 ? 31.700 -10.582 54.122 1.00 19.86 ? 58 ASN A ND2 1 ATOM 448 N N . ASP A 1 59 ? 33.294 -11.452 49.771 1.00 23.12 ? 59 ASP A N 1 ATOM 449 C CA . ASP A 1 59 ? 34.371 -12.250 49.217 1.00 25.37 ? 59 ASP A CA 1 ATOM 450 C C . ASP A 1 59 ? 34.670 -13.507 50.039 1.00 26.91 ? 59 ASP A C 1 ATOM 451 O O . ASP A 1 59 ? 35.076 -14.527 49.485 1.00 28.05 ? 59 ASP A O 1 ATOM 452 C CB . ASP A 1 59 ? 35.622 -11.380 49.091 1.00 25.72 ? 59 ASP A CB 1 ATOM 453 C CG . ASP A 1 59 ? 35.450 -10.246 48.081 1.00 28.71 ? 59 ASP A CG 1 ATOM 454 O OD1 . ASP A 1 59 ? 34.370 -9.607 48.057 1.00 27.84 ? 59 ASP A OD1 1 ATOM 455 O OD2 . ASP A 1 59 ? 36.405 -9.987 47.315 1.00 28.13 ? 59 ASP A OD2 1 ATOM 456 N N . ASN A 1 60 ? 34.459 -13.443 51.351 1.00 27.37 ? 60 ASN A N 1 ATOM 457 C CA . ASN A 1 60 ? 34.730 -14.587 52.217 1.00 28.94 ? 60 ASN A CA 1 ATOM 458 C C . ASN A 1 60 ? 33.615 -15.611 52.288 1.00 29.53 ? 60 ASN A C 1 ATOM 459 O O . ASN A 1 60 ? 33.741 -16.621 52.978 1.00 30.53 ? 60 ASN A O 1 ATOM 460 C CB . ASN A 1 60 ? 35.049 -14.123 53.634 1.00 31.85 ? 60 ASN A CB 1 ATOM 461 C CG . ASN A 1 60 ? 36.351 -13.361 53.713 1.00 36.15 ? 60 ASN A CG 1 ATOM 462 O OD1 . ASN A 1 60 ? 37.328 -13.712 53.047 1.00 37.75 ? 60 ASN A OD1 1 ATOM 463 N ND2 . ASN A 1 60 ? 36.380 -12.319 54.541 1.00 39.09 ? 60 ASN A ND2 1 ATOM 464 N N . GLY A 1 61 ? 32.518 -15.352 51.586 1.00 29.31 ? 61 GLY A N 1 ATOM 465 C CA . GLY A 1 61 ? 31.414 -16.291 51.609 1.00 28.69 ? 61 GLY A CA 1 ATOM 466 C C . GLY A 1 61 ? 30.387 -16.026 52.697 1.00 28.66 ? 61 GLY A C 1 ATOM 467 O O . GLY A 1 61 ? 29.375 -16.723 52.770 1.00 30.11 ? 61 GLY A O 1 ATOM 468 N N . GLN A 1 62 ? 30.640 -15.040 53.553 1.00 26.35 ? 62 GLN A N 1 ATOM 469 C CA . GLN A 1 62 ? 29.688 -14.704 54.605 1.00 22.44 ? 62 GLN A CA 1 ATOM 470 C C . GLN A 1 62 ? 28.416 -14.201 53.921 1.00 20.79 ? 62 GLN A C 1 ATOM 471 O O . GLN A 1 62 ? 28.484 -13.451 52.947 1.00 19.59 ? 62 GLN A O 1 ATOM 472 C CB . GLN A 1 62 ? 30.289 -13.649 55.523 1.00 22.05 ? 62 GLN A CB 1 ATOM 473 C CG . GLN A 1 62 ? 31.452 -14.197 56.327 1.00 22.18 ? 62 GLN A CG 1 ATOM 474 C CD . GLN A 1 62 ? 32.253 -13.115 57.002 1.00 21.90 ? 62 GLN A CD 1 ATOM 475 O OE1 . GLN A 1 62 ? 32.919 -12.319 56.342 1.00 21.37 ? 62 GLN A OE1 1 ATOM 476 N NE2 . GLN A 1 62 ? 32.192 -13.074 58.328 1.00 22.77 ? 62 GLN A NE2 1 ATOM 477 N N . LEU A 1 63 ? 27.265 -14.623 54.439 1.00 18.67 ? 63 LEU A N 1 ATOM 478 C CA . LEU A 1 63 ? 25.967 -14.290 53.856 1.00 17.80 ? 63 LEU A CA 1 ATOM 479 C C . LEU A 1 63 ? 24.955 -13.659 54.818 1.00 17.22 ? 63 LEU A C 1 ATOM 480 O O . LEU A 1 63 ? 24.824 -14.073 55.974 1.00 18.81 ? 63 LEU A O 1 ATOM 481 C CB . LEU A 1 63 ? 25.362 -15.566 53.264 1.00 17.82 ? 63 LEU A CB 1 ATOM 482 C CG . LEU A 1 63 ? 23.919 -15.585 52.748 1.00 19.76 ? 63 LEU A CG 1 ATOM 483 C CD1 . LEU A 1 63 ? 23.846 -14.922 51.375 1.00 20.34 ? 63 LEU A CD1 1 ATOM 484 C CD2 . LEU A 1 63 ? 23.436 -17.033 52.659 1.00 18.06 ? 63 LEU A CD2 1 ATOM 485 N N . ALA A 1 64 ? 24.235 -12.659 54.324 1.00 14.66 ? 64 ALA A N 1 ATOM 486 C CA . ALA A 1 64 ? 23.216 -11.981 55.108 1.00 14.64 ? 64 ALA A CA 1 ATOM 487 C C . ALA A 1 64 ? 22.006 -11.827 54.200 1.00 15.65 ? 64 ALA A C 1 ATOM 488 O O . ALA A 1 64 ? 22.108 -11.256 53.110 1.00 15.28 ? 64 ALA A O 1 ATOM 489 C CB . ALA A 1 64 ? 23.712 -10.619 55.563 1.00 12.59 ? 64 ALA A CB 1 ATOM 490 N N . GLU A 1 65 ? 20.867 -12.349 54.642 1.00 15.92 ? 65 GLU A N 1 ATOM 491 C CA . GLU A 1 65 ? 19.644 -12.268 53.851 1.00 16.33 ? 65 GLU A CA 1 ATOM 492 C C . GLU A 1 65 ? 18.681 -11.261 54.464 1.00 15.31 ? 65 GLU A C 1 ATOM 493 O O . GLU A 1 65 ? 18.128 -11.476 55.543 1.00 15.74 ? 65 GLU A O 1 ATOM 494 C CB . GLU A 1 65 ? 19.024 -13.664 53.735 1.00 18.94 ? 65 GLU A CB 1 ATOM 495 C CG . GLU A 1 65 ? 20.052 -14.669 53.198 1.00 22.41 ? 65 GLU A CG 1 ATOM 496 C CD . GLU A 1 65 ? 19.535 -16.090 53.092 1.00 25.32 ? 65 GLU A CD 1 ATOM 497 O OE1 . GLU A 1 65 ? 19.168 -16.514 51.972 1.00 26.44 ? 65 GLU A OE1 1 ATOM 498 O OE2 . GLU A 1 65 ? 19.501 -16.785 54.128 1.00 24.92 ? 65 GLU A OE2 1 ATOM 499 N N . ILE A 1 66 ? 18.500 -10.155 53.746 1.00 14.29 ? 66 ILE A N 1 ATOM 500 C CA . ILE A 1 66 ? 17.656 -9.039 54.162 1.00 11.99 ? 66 ILE A CA 1 ATOM 501 C C . ILE A 1 66 ? 16.210 -9.137 53.671 1.00 12.74 ? 66 ILE A C 1 ATOM 502 O O . ILE A 1 66 ? 15.958 -9.370 52.484 1.00 11.55 ? 66 ILE A O 1 ATOM 503 C CB . ILE A 1 66 ? 18.234 -7.701 53.627 1.00 11.76 ? 66 ILE A CB 1 ATOM 504 C CG1 . ILE A 1 66 ? 19.769 -7.723 53.682 1.00 10.73 ? 66 ILE A CG1 1 ATOM 505 C CG2 . ILE A 1 66 ? 17.649 -6.530 54.408 1.00 12.43 ? 66 ILE A CG2 1 ATOM 506 C CD1 . ILE A 1 66 ? 20.365 -7.964 55.044 1.00 10.92 ? 66 ILE A CD1 1 ATOM 507 N N . ALA A 1 67 ? 15.262 -8.947 54.589 1.00 12.86 ? 67 ALA A N 1 ATOM 508 C CA . ALA A 1 67 ? 13.838 -8.984 54.251 1.00 11.53 ? 67 ALA A CA 1 ATOM 509 C C . ALA A 1 67 ? 13.373 -7.541 54.012 1.00 12.83 ? 67 ALA A C 1 ATOM 510 O O . ALA A 1 67 ? 13.472 -6.686 54.902 1.00 12.48 ? 67 ALA A O 1 ATOM 511 C CB . ALA A 1 67 ? 13.043 -9.616 55.386 1.00 11.62 ? 67 ALA A CB 1 ATOM 512 N N . ILE A 1 68 ? 12.863 -7.278 52.812 1.00 13.78 ? 68 ILE A N 1 ATOM 513 C CA . ILE A 1 68 ? 12.412 -5.942 52.432 1.00 13.96 ? 68 ILE A CA 1 ATOM 514 C C . ILE A 1 68 ? 10.925 -5.914 52.060 1.00 15.55 ? 68 ILE A C 1 ATOM 515 O O . ILE A 1 68 ? 10.457 -6.704 51.239 1.00 16.71 ? 68 ILE A O 1 ATOM 516 C CB . ILE A 1 68 ? 13.272 -5.412 51.249 1.00 13.63 ? 68 ILE A CB 1 ATOM 517 C CG1 . ILE A 1 68 ? 14.742 -5.381 51.678 1.00 12.14 ? 68 ILE A CG1 1 ATOM 518 C CG2 . ILE A 1 68 ? 12.806 -4.006 50.810 1.00 11.65 ? 68 ILE A CG2 1 ATOM 519 C CD1 . ILE A 1 68 ? 15.681 -4.921 50.620 1.00 11.20 ? 68 ILE A CD1 1 ATOM 520 N N . ASP A 1 69 ? 10.198 -4.994 52.688 1.00 16.08 ? 69 ASP A N 1 ATOM 521 C CA . ASP A 1 69 ? 8.764 -4.790 52.476 1.00 16.17 ? 69 ASP A CA 1 ATOM 522 C C . ASP A 1 69 ? 8.519 -4.326 51.030 1.00 14.66 ? 69 ASP A C 1 ATOM 523 O O . ASP A 1 69 ? 9.172 -3.401 50.566 1.00 13.46 ? 69 ASP A O 1 ATOM 524 C CB . ASP A 1 69 ? 8.291 -3.723 53.466 1.00 20.94 ? 69 ASP A CB 1 ATOM 525 C CG . ASP A 1 69 ? 6.794 -3.515 53.446 1.00 27.11 ? 69 ASP A CG 1 ATOM 526 O OD1 . ASP A 1 69 ? 6.249 -3.165 52.380 1.00 31.57 ? 69 ASP A OD1 1 ATOM 527 O OD2 . ASP A 1 69 ? 6.158 -3.691 54.506 1.00 31.49 ? 69 ASP A OD2 1 ATOM 528 N N . VAL A 1 70 ? 7.576 -4.948 50.323 1.00 14.03 ? 70 VAL A N 1 ATOM 529 C CA . VAL A 1 70 ? 7.310 -4.561 48.929 1.00 13.50 ? 70 VAL A CA 1 ATOM 530 C C . VAL A 1 70 ? 6.475 -3.293 48.741 1.00 13.99 ? 70 VAL A C 1 ATOM 531 O O . VAL A 1 70 ? 6.347 -2.793 47.619 1.00 13.68 ? 70 VAL A O 1 ATOM 532 C CB . VAL A 1 70 ? 6.610 -5.688 48.127 1.00 13.45 ? 70 VAL A CB 1 ATOM 533 C CG1 . VAL A 1 70 ? 7.455 -6.954 48.146 1.00 11.07 ? 70 VAL A CG1 1 ATOM 534 C CG2 . VAL A 1 70 ? 5.214 -5.940 48.690 1.00 12.24 ? 70 VAL A CG2 1 ATOM 535 N N . THR A 1 71 ? 5.899 -2.770 49.819 1.00 13.96 ? 71 THR A N 1 ATOM 536 C CA . THR A 1 71 ? 5.092 -1.562 49.693 1.00 14.98 ? 71 THR A CA 1 ATOM 537 C C . THR A 1 71 ? 5.912 -0.312 49.994 1.00 15.72 ? 71 THR A C 1 ATOM 538 O O . THR A 1 71 ? 5.628 0.765 49.477 1.00 17.17 ? 71 THR A O 1 ATOM 539 C CB . THR A 1 71 ? 3.855 -1.584 50.638 1.00 14.86 ? 71 THR A CB 1 ATOM 540 O OG1 . THR A 1 71 ? 4.284 -1.563 52.006 1.00 15.23 ? 71 THR A OG1 1 ATOM 541 C CG2 . THR A 1 71 ? 3.005 -2.829 50.386 1.00 15.00 ? 71 THR A CG2 1 ATOM 542 N N . SER A 1 72 ? 6.958 -0.467 50.797 1.00 16.34 ? 72 SER A N 1 ATOM 543 C CA . SER A 1 72 ? 7.783 0.664 51.193 1.00 15.90 ? 72 SER A CA 1 ATOM 544 C C . SER A 1 72 ? 9.268 0.488 50.922 1.00 15.91 ? 72 SER A C 1 ATOM 545 O O . SER A 1 72 ? 10.021 1.453 51.016 1.00 17.84 ? 72 SER A O 1 ATOM 546 C CB . SER A 1 72 ? 7.610 0.897 52.684 1.00 16.39 ? 72 SER A CB 1 ATOM 547 O OG . SER A 1 72 ? 8.006 -0.280 53.381 1.00 18.59 ? 72 SER A OG 1 ATOM 548 N N . VAL A 1 73 ? 9.683 -0.733 50.598 1.00 14.30 ? 73 VAL A N 1 ATOM 549 C CA . VAL A 1 73 ? 11.094 -1.061 50.365 1.00 14.08 ? 73 VAL A CA 1 ATOM 550 C C . VAL A 1 73 ? 11.823 -0.910 51.713 1.00 13.79 ? 73 VAL A C 1 ATOM 551 O O . VAL A 1 73 ? 13.024 -0.622 51.775 1.00 13.78 ? 73 VAL A O 1 ATOM 552 C CB . VAL A 1 73 ? 11.781 -0.131 49.304 1.00 14.87 ? 73 VAL A CB 1 ATOM 553 C CG1 . VAL A 1 73 ? 13.065 -0.788 48.802 1.00 12.74 ? 73 VAL A CG1 1 ATOM 554 C CG2 . VAL A 1 73 ? 10.856 0.136 48.127 1.00 13.30 ? 73 VAL A CG2 1 ATOM 555 N N . TYR A 1 74 ? 11.075 -1.122 52.791 1.00 12.51 ? 74 TYR A N 1 ATOM 556 C CA . TYR A 1 74 ? 11.609 -1.015 54.140 1.00 13.64 ? 74 TYR A CA 1 ATOM 557 C C . TYR A 1 74 ? 12.258 -2.314 54.606 1.00 11.73 ? 74 TYR A C 1 ATOM 558 O O . TYR A 1 74 ? 11.691 -3.393 54.448 1.00 10.96 ? 74 TYR A O 1 ATOM 559 C CB . TYR A 1 74 ? 10.486 -0.651 55.112 1.00 17.09 ? 74 TYR A CB 1 ATOM 560 C CG . TYR A 1 74 ? 10.954 -0.116 56.452 1.00 20.41 ? 74 TYR A CG 1 ATOM 561 C CD1 . TYR A 1 74 ? 11.453 1.185 56.570 1.00 21.71 ? 74 TYR A CD1 1 ATOM 562 C CD2 . TYR A 1 74 ? 10.874 -0.899 57.606 1.00 23.15 ? 74 TYR A CD2 1 ATOM 563 C CE1 . TYR A 1 74 ? 11.855 1.696 57.806 1.00 24.26 ? 74 TYR A CE1 1 ATOM 564 C CE2 . TYR A 1 74 ? 11.275 -0.399 58.854 1.00 24.71 ? 74 TYR A CE2 1 ATOM 565 C CZ . TYR A 1 74 ? 11.763 0.901 58.945 1.00 26.68 ? 74 TYR A CZ 1 ATOM 566 O OH . TYR A 1 74 ? 12.143 1.411 60.171 1.00 27.14 ? 74 TYR A OH 1 ATOM 567 N N . VAL A 1 75 ? 13.454 -2.201 55.176 1.00 11.14 ? 75 VAL A N 1 ATOM 568 C CA . VAL A 1 75 ? 14.167 -3.361 55.710 1.00 11.37 ? 75 VAL A CA 1 ATOM 569 C C . VAL A 1 75 ? 13.587 -3.615 57.111 1.00 11.67 ? 75 VAL A C 1 ATOM 570 O O . VAL A 1 75 ? 13.646 -2.731 57.971 1.00 10.02 ? 75 VAL A O 1 ATOM 571 C CB . VAL A 1 75 ? 15.696 -3.080 55.829 1.00 10.74 ? 75 VAL A CB 1 ATOM 572 C CG1 . VAL A 1 75 ? 16.390 -4.247 56.513 1.00 10.30 ? 75 VAL A CG1 1 ATOM 573 C CG2 . VAL A 1 75 ? 16.298 -2.846 54.444 1.00 9.85 ? 75 VAL A CG2 1 ATOM 574 N N . VAL A 1 76 ? 13.007 -4.797 57.333 1.00 10.88 ? 76 VAL A N 1 ATOM 575 C CA . VAL A 1 76 ? 12.420 -5.114 58.641 1.00 12.47 ? 76 VAL A CA 1 ATOM 576 C C . VAL A 1 76 ? 13.249 -6.077 59.491 1.00 13.11 ? 76 VAL A C 1 ATOM 577 O O . VAL A 1 76 ? 13.083 -6.134 60.711 1.00 12.54 ? 76 VAL A O 1 ATOM 578 C CB . VAL A 1 76 ? 10.991 -5.713 58.502 1.00 11.30 ? 76 VAL A CB 1 ATOM 579 C CG1 . VAL A 1 76 ? 10.089 -4.734 57.778 1.00 11.41 ? 76 VAL A CG1 1 ATOM 580 C CG2 . VAL A 1 76 ? 11.043 -7.041 57.753 1.00 11.90 ? 76 VAL A CG2 1 ATOM 581 N N . GLY A 1 77 ? 14.135 -6.830 58.845 1.00 13.40 ? 77 GLY A N 1 ATOM 582 C CA . GLY A 1 77 ? 14.964 -7.793 59.555 1.00 12.39 ? 77 GLY A CA 1 ATOM 583 C C . GLY A 1 77 ? 15.855 -8.565 58.592 1.00 12.86 ? 77 GLY A C 1 ATOM 584 O O . GLY A 1 77 ? 15.807 -8.340 57.378 1.00 12.22 ? 77 GLY A O 1 ATOM 585 N N . TYR A 1 78 ? 16.657 -9.483 59.124 1.00 12.06 ? 78 TYR A N 1 ATOM 586 C CA . TYR A 1 78 ? 17.576 -10.261 58.301 1.00 11.07 ? 78 TYR A CA 1 ATOM 587 C C . TYR A 1 78 ? 17.986 -11.573 58.978 1.00 11.86 ? 78 TYR A C 1 ATOM 588 O O . TYR A 1 78 ? 17.818 -11.748 60.189 1.00 11.56 ? 78 TYR A O 1 ATOM 589 C CB . TYR A 1 78 ? 18.842 -9.443 58.022 1.00 10.25 ? 78 TYR A CB 1 ATOM 590 C CG . TYR A 1 78 ? 19.659 -9.158 59.274 1.00 10.30 ? 78 TYR A CG 1 ATOM 591 C CD1 . TYR A 1 78 ? 19.288 -8.144 60.161 1.00 10.11 ? 78 TYR A CD1 1 ATOM 592 C CD2 . TYR A 1 78 ? 20.768 -9.941 59.598 1.00 10.16 ? 78 TYR A CD2 1 ATOM 593 C CE1 . TYR A 1 78 ? 20.002 -7.918 61.341 1.00 9.81 ? 78 TYR A CE1 1 ATOM 594 C CE2 . TYR A 1 78 ? 21.486 -9.728 60.773 1.00 10.52 ? 78 TYR A CE2 1 ATOM 595 C CZ . TYR A 1 78 ? 21.100 -8.715 61.639 1.00 11.45 ? 78 TYR A CZ 1 ATOM 596 O OH . TYR A 1 78 ? 21.823 -8.487 62.792 1.00 10.00 ? 78 TYR A OH 1 ATOM 597 N N . GLN A 1 79 ? 18.532 -12.489 58.185 1.00 11.94 ? 79 GLN A N 1 ATOM 598 C CA . GLN A 1 79 ? 18.999 -13.767 58.704 1.00 12.68 ? 79 GLN A CA 1 ATOM 599 C C . GLN A 1 79 ? 20.465 -13.995 58.370 1.00 13.70 ? 79 GLN A C 1 ATOM 600 O O . GLN A 1 79 ? 20.908 -13.733 57.251 1.00 13.96 ? 79 GLN A O 1 ATOM 601 C CB . GLN A 1 79 ? 18.200 -14.936 58.122 1.00 14.25 ? 79 GLN A CB 1 ATOM 602 C CG . GLN A 1 79 ? 18.685 -16.284 58.645 1.00 15.07 ? 79 GLN A CG 1 ATOM 603 C CD . GLN A 1 79 ? 17.992 -17.461 57.994 1.00 17.36 ? 79 GLN A CD 1 ATOM 604 O OE1 . GLN A 1 79 ? 16.851 -17.359 57.545 1.00 16.03 ? 79 GLN A OE1 1 ATOM 605 N NE2 . GLN A 1 79 ? 18.676 -18.601 57.961 1.00 17.33 ? 79 GLN A NE2 1 ATOM 606 N N . VAL A 1 80 ? 21.210 -14.478 59.358 1.00 13.93 ? 80 VAL A N 1 ATOM 607 C CA . VAL A 1 80 ? 22.622 -14.802 59.198 1.00 14.55 ? 80 VAL A CA 1 ATOM 608 C C . VAL A 1 80 ? 22.773 -16.164 59.851 1.00 15.32 ? 80 VAL A C 1 ATOM 609 O O . VAL A 1 80 ? 22.328 -16.362 60.982 1.00 16.08 ? 80 VAL A O 1 ATOM 610 C CB . VAL A 1 80 ? 23.543 -13.779 59.895 1.00 13.12 ? 80 VAL A CB 1 ATOM 611 C CG1 . VAL A 1 80 ? 23.720 -12.548 59.001 1.00 12.07 ? 80 VAL A CG1 1 ATOM 612 C CG2 . VAL A 1 80 ? 22.966 -13.386 61.259 1.00 14.27 ? 80 VAL A CG2 1 ATOM 613 N N . ARG A 1 81 ? 23.370 -17.109 59.131 1.00 16.70 ? 81 ARG A N 1 ATOM 614 C CA . ARG A 1 81 ? 23.532 -18.466 59.652 1.00 18.37 ? 81 ARG A CA 1 ATOM 615 C C . ARG A 1 81 ? 22.143 -18.999 60.026 1.00 17.40 ? 81 ARG A C 1 ATOM 616 O O . ARG A 1 81 ? 21.228 -18.962 59.197 1.00 16.99 ? 81 ARG A O 1 ATOM 617 C CB . ARG A 1 81 ? 24.476 -18.455 60.861 1.00 21.54 ? 81 ARG A CB 1 ATOM 618 C CG . ARG A 1 81 ? 25.900 -18.017 60.498 1.00 26.23 ? 81 ARG A CG 1 ATOM 619 C CD . ARG A 1 81 ? 26.770 -17.789 61.724 1.00 30.61 ? 81 ARG A CD 1 ATOM 620 N NE . ARG A 1 81 ? 28.061 -17.200 61.371 1.00 36.01 ? 81 ARG A NE 1 ATOM 621 C CZ . ARG A 1 81 ? 28.963 -16.771 62.253 1.00 39.67 ? 81 ARG A CZ 1 ATOM 622 N NH1 . ARG A 1 81 ? 28.726 -16.863 63.557 1.00 41.09 ? 81 ARG A NH1 1 ATOM 623 N NH2 . ARG A 1 81 ? 30.102 -16.230 61.832 1.00 41.32 ? 81 ARG A NH2 1 ATOM 624 N N . ASN A 1 82 ? 21.964 -19.476 61.257 1.00 16.84 ? 82 ASN A N 1 ATOM 625 C CA . ASN A 1 82 ? 20.659 -20.002 61.664 1.00 16.88 ? 82 ASN A CA 1 ATOM 626 C C . ASN A 1 82 ? 19.922 -19.065 62.620 1.00 16.36 ? 82 ASN A C 1 ATOM 627 O O . ASN A 1 82 ? 19.080 -19.498 63.410 1.00 16.29 ? 82 ASN A O 1 ATOM 628 C CB . ASN A 1 82 ? 20.821 -21.388 62.305 1.00 18.31 ? 82 ASN A CB 1 ATOM 629 C CG . ASN A 1 82 ? 21.588 -21.342 63.612 1.00 20.16 ? 82 ASN A CG 1 ATOM 630 O OD1 . ASN A 1 82 ? 22.386 -20.431 63.857 1.00 20.83 ? 82 ASN A OD1 1 ATOM 631 N ND2 . ASN A 1 82 ? 21.359 -22.338 64.457 1.00 22.22 ? 82 ASN A ND2 1 ATOM 632 N N . ARG A 1 83 ? 20.230 -17.776 62.523 1.00 16.52 ? 83 ARG A N 1 ATOM 633 C CA . ARG A 1 83 ? 19.610 -16.762 63.371 1.00 16.91 ? 83 ARG A CA 1 ATOM 634 C C . ARG A 1 83 ? 18.951 -15.650 62.566 1.00 15.61 ? 83 ARG A C 1 ATOM 635 O O . ARG A 1 83 ? 19.325 -15.395 61.425 1.00 14.78 ? 83 ARG A O 1 ATOM 636 C CB . ARG A 1 83 ? 20.660 -16.147 64.289 1.00 17.29 ? 83 ARG A CB 1 ATOM 637 C CG . ARG A 1 83 ? 21.195 -17.110 65.319 1.00 21.41 ? 83 ARG A CG 1 ATOM 638 C CD . ARG A 1 83 ? 22.402 -16.521 65.986 1.00 25.76 ? 83 ARG A CD 1 ATOM 639 N NE . ARG A 1 83 ? 22.779 -17.262 67.181 1.00 31.82 ? 83 ARG A NE 1 ATOM 640 C CZ . ARG A 1 83 ? 22.269 -17.042 68.388 1.00 33.74 ? 83 ARG A CZ 1 ATOM 641 N NH1 . ARG A 1 83 ? 21.352 -16.096 68.569 1.00 33.95 ? 83 ARG A NH1 1 ATOM 642 N NH2 . ARG A 1 83 ? 22.689 -17.762 69.417 1.00 36.17 ? 83 ARG A NH2 1 ATOM 643 N N . SER A 1 84 ? 17.961 -14.997 63.165 1.00 13.61 ? 84 SER A N 1 ATOM 644 C CA . SER A 1 84 ? 17.288 -13.894 62.504 1.00 13.36 ? 84 SER A CA 1 ATOM 645 C C . SER A 1 84 ? 17.101 -12.761 63.509 1.00 13.33 ? 84 SER A C 1 ATOM 646 O O . SER A 1 84 ? 16.909 -13.005 64.706 1.00 11.62 ? 84 SER A O 1 ATOM 647 C CB . SER A 1 84 ? 15.945 -14.349 61.921 1.00 12.09 ? 84 SER A CB 1 ATOM 648 O OG . SER A 1 84 ? 15.058 -14.809 62.921 1.00 13.62 ? 84 SER A OG 1 ATOM 649 N N . TYR A 1 85 ? 17.198 -11.525 63.021 1.00 13.20 ? 85 TYR A N 1 ATOM 650 C CA . TYR A 1 85 ? 17.052 -10.338 63.861 1.00 12.67 ? 85 TYR A CA 1 ATOM 651 C C . TYR A 1 85 ? 16.062 -9.396 63.203 1.00 13.96 ? 85 TYR A C 1 ATOM 652 O O . TYR A 1 85 ? 16.072 -9.241 61.983 1.00 14.99 ? 85 TYR A O 1 ATOM 653 C CB . TYR A 1 85 ? 18.396 -9.624 64.034 1.00 12.02 ? 85 TYR A CB 1 ATOM 654 C CG . TYR A 1 85 ? 19.461 -10.509 64.628 1.00 14.03 ? 85 TYR A CG 1 ATOM 655 C CD1 . TYR A 1 85 ? 20.135 -11.452 63.840 1.00 14.96 ? 85 TYR A CD1 1 ATOM 656 C CD2 . TYR A 1 85 ? 19.755 -10.455 65.988 1.00 12.63 ? 85 TYR A CD2 1 ATOM 657 C CE1 . TYR A 1 85 ? 21.071 -12.321 64.398 1.00 15.49 ? 85 TYR A CE1 1 ATOM 658 C CE2 . TYR A 1 85 ? 20.691 -11.323 66.557 1.00 14.62 ? 85 TYR A CE2 1 ATOM 659 C CZ . TYR A 1 85 ? 21.340 -12.252 65.759 1.00 15.70 ? 85 TYR A CZ 1 ATOM 660 O OH . TYR A 1 85 ? 22.244 -13.124 66.322 1.00 16.92 ? 85 TYR A OH 1 ATOM 661 N N . PHE A 1 86 ? 15.217 -8.774 64.019 1.00 12.25 ? 86 PHE A N 1 ATOM 662 C CA . PHE A 1 86 ? 14.198 -7.852 63.538 1.00 11.96 ? 86 PHE A CA 1 ATOM 663 C C . PHE A 1 86 ? 14.262 -6.521 64.279 1.00 11.29 ? 86 PHE A C 1 ATOM 664 O O . PHE A 1 86 ? 14.549 -6.487 65.466 1.00 11.07 ? 86 PHE A O 1 ATOM 665 C CB . PHE A 1 86 ? 12.805 -8.456 63.751 1.00 10.70 ? 86 PHE A CB 1 ATOM 666 C CG . PHE A 1 86 ? 12.524 -9.670 62.905 1.00 11.73 ? 86 PHE A CG 1 ATOM 667 C CD1 . PHE A 1 86 ? 11.813 -9.554 61.710 1.00 11.56 ? 86 PHE A CD1 1 ATOM 668 C CD2 . PHE A 1 86 ? 12.954 -10.931 63.309 1.00 11.10 ? 86 PHE A CD2 1 ATOM 669 C CE1 . PHE A 1 86 ? 11.530 -10.677 60.929 1.00 11.02 ? 86 PHE A CE1 1 ATOM 670 C CE2 . PHE A 1 86 ? 12.677 -12.067 62.533 1.00 10.87 ? 86 PHE A CE2 1 ATOM 671 C CZ . PHE A 1 86 ? 11.965 -11.937 61.344 1.00 10.64 ? 86 PHE A CZ 1 ATOM 672 N N . PHE A 1 87 ? 13.987 -5.427 63.574 1.00 12.04 ? 87 PHE A N 1 ATOM 673 C CA . PHE A 1 87 ? 13.966 -4.109 64.198 1.00 11.66 ? 87 PHE A CA 1 ATOM 674 C C . PHE A 1 87 ? 12.840 -4.110 65.237 1.00 12.98 ? 87 PHE A C 1 ATOM 675 O O . PHE A 1 87 ? 11.835 -4.809 65.082 1.00 13.32 ? 87 PHE A O 1 ATOM 676 C CB . PHE A 1 87 ? 13.714 -3.027 63.146 1.00 12.55 ? 87 PHE A CB 1 ATOM 677 C CG . PHE A 1 87 ? 14.948 -2.632 62.366 1.00 12.47 ? 87 PHE A CG 1 ATOM 678 C CD1 . PHE A 1 87 ? 14.955 -2.681 60.968 1.00 12.09 ? 87 PHE A CD1 1 ATOM 679 C CD2 . PHE A 1 87 ? 16.080 -2.161 63.024 1.00 10.91 ? 87 PHE A CD2 1 ATOM 680 C CE1 . PHE A 1 87 ? 16.064 -2.263 60.242 1.00 10.11 ? 87 PHE A CE1 1 ATOM 681 C CE2 . PHE A 1 87 ? 17.196 -1.739 62.308 1.00 10.61 ? 87 PHE A CE2 1 ATOM 682 C CZ . PHE A 1 87 ? 17.189 -1.789 60.911 1.00 10.50 ? 87 PHE A CZ 1 ATOM 683 N N . LYS A 1 88 ? 13.014 -3.335 66.299 1.00 12.18 ? 88 LYS A N 1 ATOM 684 C CA . LYS A 1 88 ? 12.029 -3.285 67.361 1.00 14.22 ? 88 LYS A CA 1 ATOM 685 C C . LYS A 1 88 ? 10.644 -2.948 66.830 1.00 15.78 ? 88 LYS A C 1 ATOM 686 O O . LYS A 1 88 ? 9.640 -3.454 67.329 1.00 14.68 ? 88 LYS A O 1 ATOM 687 C CB . LYS A 1 88 ? 12.444 -2.251 68.408 1.00 14.07 ? 88 LYS A CB 1 ATOM 688 C CG . LYS A 1 88 ? 11.568 -2.249 69.641 1.00 15.67 ? 88 LYS A CG 1 ATOM 689 C CD . LYS A 1 88 ? 11.960 -1.156 70.607 1.00 14.41 ? 88 LYS A CD 1 ATOM 690 C CE . LYS A 1 88 ? 11.110 -1.223 71.856 1.00 16.47 ? 88 LYS A CE 1 ATOM 691 N NZ . LYS A 1 88 ? 11.404 -2.450 72.643 1.00 15.97 ? 88 LYS A NZ 1 ATOM 692 N N . ASP A 1 89 ? 10.597 -2.105 65.802 1.00 17.36 ? 89 ASP A N 1 ATOM 693 C CA . ASP A 1 89 ? 9.331 -1.675 65.212 1.00 19.14 ? 89 ASP A CA 1 ATOM 694 C C . ASP A 1 89 ? 8.752 -2.583 64.113 1.00 19.66 ? 89 ASP A C 1 ATOM 695 O O . ASP A 1 89 ? 7.762 -2.224 63.473 1.00 18.91 ? 89 ASP A O 1 ATOM 696 C CB . ASP A 1 89 ? 9.474 -0.233 64.692 1.00 21.75 ? 89 ASP A CB 1 ATOM 697 C CG . ASP A 1 89 ? 10.613 -0.072 63.690 1.00 24.12 ? 89 ASP A CG 1 ATOM 698 O OD1 . ASP A 1 89 ? 11.744 -0.519 63.970 1.00 24.38 ? 89 ASP A OD1 1 ATOM 699 O OD2 . ASP A 1 89 ? 10.381 0.517 62.616 1.00 30.01 ? 89 ASP A OD2 1 ATOM 700 N N . ALA A 1 90 ? 9.351 -3.754 63.899 1.00 18.25 ? 90 ALA A N 1 ATOM 701 C CA . ALA A 1 90 ? 8.847 -4.683 62.885 1.00 17.98 ? 90 ALA A CA 1 ATOM 702 C C . ALA A 1 90 ? 7.473 -5.180 63.340 1.00 18.27 ? 90 ALA A C 1 ATOM 703 O O . ALA A 1 90 ? 7.311 -5.568 64.496 1.00 20.19 ? 90 ALA A O 1 ATOM 704 C CB . ALA A 1 90 ? 9.804 -5.864 62.728 1.00 17.26 ? 90 ALA A CB 1 ATOM 705 N N . PRO A 1 91 ? 6.466 -5.173 62.446 1.00 17.25 ? 91 PRO A N 1 ATOM 706 C CA . PRO A 1 91 ? 5.124 -5.635 62.821 1.00 16.95 ? 91 PRO A CA 1 ATOM 707 C C . PRO A 1 91 ? 5.095 -7.107 63.219 1.00 16.68 ? 91 PRO A C 1 ATOM 708 O O . PRO A 1 91 ? 5.917 -7.895 62.748 1.00 14.88 ? 91 PRO A O 1 ATOM 709 C CB . PRO A 1 91 ? 4.295 -5.341 61.576 1.00 17.73 ? 91 PRO A CB 1 ATOM 710 C CG . PRO A 1 91 ? 5.280 -5.475 60.479 1.00 19.92 ? 91 PRO A CG 1 ATOM 711 C CD . PRO A 1 91 ? 6.502 -4.784 61.027 1.00 18.52 ? 91 PRO A CD 1 ATOM 712 N N . ASP A 1 92 ? 4.144 -7.468 64.082 1.00 17.54 ? 92 ASP A N 1 ATOM 713 C CA . ASP A 1 92 ? 4.023 -8.837 64.574 1.00 18.92 ? 92 ASP A CA 1 ATOM 714 C C . ASP A 1 92 ? 3.862 -9.879 63.474 1.00 19.40 ? 92 ASP A C 1 ATOM 715 O O . ASP A 1 92 ? 4.417 -10.971 63.566 1.00 19.05 ? 92 ASP A O 1 ATOM 716 C CB . ASP A 1 92 ? 2.861 -8.953 65.569 1.00 18.74 ? 92 ASP A CB 1 ATOM 717 C CG . ASP A 1 92 ? 3.146 -8.240 66.887 1.00 21.48 ? 92 ASP A CG 1 ATOM 718 O OD1 . ASP A 1 92 ? 4.334 -8.015 67.202 1.00 21.05 ? 92 ASP A OD1 1 ATOM 719 O OD2 . ASP A 1 92 ? 2.186 -7.918 67.618 1.00 21.53 ? 92 ASP A OD2 1 ATOM 720 N N . ALA A 1 93 ? 3.105 -9.545 62.435 1.00 20.17 ? 93 ALA A N 1 ATOM 721 C CA . ALA A 1 93 ? 2.892 -10.468 61.324 1.00 19.50 ? 93 ALA A CA 1 ATOM 722 C C . ALA A 1 93 ? 4.214 -10.885 60.683 1.00 19.55 ? 93 ALA A C 1 ATOM 723 O O . ALA A 1 93 ? 4.432 -12.059 60.390 1.00 20.58 ? 93 ALA A O 1 ATOM 724 C CB . ALA A 1 93 ? 1.999 -9.820 60.286 1.00 21.28 ? 93 ALA A CB 1 ATOM 725 N N . ALA A 1 94 ? 5.097 -9.916 60.467 1.00 18.25 ? 94 ALA A N 1 ATOM 726 C CA . ALA A 1 94 ? 6.392 -10.182 59.851 1.00 16.66 ? 94 ALA A CA 1 ATOM 727 C C . ALA A 1 94 ? 7.327 -10.932 60.784 1.00 15.59 ? 94 ALA A C 1 ATOM 728 O O . ALA A 1 94 ? 8.008 -11.866 60.365 1.00 16.45 ? 94 ALA A O 1 ATOM 729 C CB . ALA A 1 94 ? 7.041 -8.877 59.417 1.00 16.81 ? 94 ALA A CB 1 ATOM 730 N N . TYR A 1 95 ? 7.366 -10.518 62.046 1.00 14.90 ? 95 TYR A N 1 ATOM 731 C CA . TYR A 1 95 ? 8.239 -11.158 63.023 1.00 15.11 ? 95 TYR A CA 1 ATOM 732 C C . TYR A 1 95 ? 7.942 -12.651 63.123 1.00 16.44 ? 95 TYR A C 1 ATOM 733 O O . TYR A 1 95 ? 8.856 -13.481 63.191 1.00 16.98 ? 95 TYR A O 1 ATOM 734 C CB . TYR A 1 95 ? 8.056 -10.519 64.405 1.00 14.88 ? 95 TYR A CB 1 ATOM 735 C CG . TYR A 1 95 ? 9.019 -11.052 65.448 1.00 14.83 ? 95 TYR A CG 1 ATOM 736 C CD1 . TYR A 1 95 ? 10.348 -10.626 65.482 1.00 14.16 ? 95 TYR A CD1 1 ATOM 737 C CD2 . TYR A 1 95 ? 8.609 -12.002 66.382 1.00 14.40 ? 95 TYR A CD2 1 ATOM 738 C CE1 . TYR A 1 95 ? 11.244 -11.132 66.417 1.00 13.59 ? 95 TYR A CE1 1 ATOM 739 C CE2 . TYR A 1 95 ? 9.500 -12.515 67.324 1.00 14.26 ? 95 TYR A CE2 1 ATOM 740 C CZ . TYR A 1 95 ? 10.814 -12.075 67.334 1.00 14.37 ? 95 TYR A CZ 1 ATOM 741 O OH . TYR A 1 95 ? 11.694 -12.584 68.259 1.00 11.49 ? 95 TYR A OH 1 ATOM 742 N N . GLU A 1 96 ? 6.654 -12.982 63.132 1.00 16.60 ? 96 GLU A N 1 ATOM 743 C CA . GLU A 1 96 ? 6.219 -14.365 63.245 1.00 16.64 ? 96 GLU A CA 1 ATOM 744 C C . GLU A 1 96 ? 6.297 -15.085 61.910 1.00 16.41 ? 96 GLU A C 1 ATOM 745 O O . GLU A 1 96 ? 6.681 -16.250 61.851 1.00 16.80 ? 96 GLU A O 1 ATOM 746 C CB . GLU A 1 96 ? 4.779 -14.417 63.778 1.00 18.42 ? 96 GLU A CB 1 ATOM 747 C CG . GLU A 1 96 ? 4.566 -13.628 65.079 1.00 19.75 ? 96 GLU A CG 1 ATOM 748 C CD . GLU A 1 96 ? 3.103 -13.539 65.492 1.00 20.77 ? 96 GLU A CD 1 ATOM 749 O OE1 . GLU A 1 96 ? 2.222 -13.876 64.668 1.00 22.34 ? 96 GLU A OE1 1 ATOM 750 O OE2 . GLU A 1 96 ? 2.834 -13.119 66.639 1.00 20.42 ? 96 GLU A OE2 1 ATOM 751 N N . GLY A 1 97 ? 5.964 -14.374 60.836 1.00 15.82 ? 97 GLY A N 1 ATOM 752 C CA . GLY A 1 97 ? 5.953 -14.984 59.520 1.00 14.80 ? 97 GLY A CA 1 ATOM 753 C C . GLY A 1 97 ? 7.240 -15.168 58.746 1.00 14.98 ? 97 GLY A C 1 ATOM 754 O O . GLY A 1 97 ? 7.321 -16.081 57.925 1.00 16.20 ? 97 GLY A O 1 ATOM 755 N N . LEU A 1 98 ? 8.244 -14.332 58.993 1.00 14.51 ? 98 LEU A N 1 ATOM 756 C CA . LEU A 1 98 ? 9.502 -14.425 58.255 1.00 13.67 ? 98 LEU A CA 1 ATOM 757 C C . LEU A 1 98 ? 10.588 -15.240 58.921 1.00 14.38 ? 98 LEU A C 1 ATOM 758 O O . LEU A 1 98 ? 10.619 -15.392 60.138 1.00 15.12 ? 98 LEU A O 1 ATOM 759 C CB . LEU A 1 98 ? 10.068 -13.029 57.993 1.00 14.17 ? 98 LEU A CB 1 ATOM 760 C CG . LEU A 1 98 ? 9.234 -12.021 57.202 1.00 14.88 ? 98 LEU A CG 1 ATOM 761 C CD1 . LEU A 1 98 ? 9.877 -10.644 57.295 1.00 13.70 ? 98 LEU A CD1 1 ATOM 762 C CD2 . LEU A 1 98 ? 9.122 -12.471 55.763 1.00 15.39 ? 98 LEU A CD2 1 ATOM 763 N N . PHE A 1 99 ? 11.494 -15.749 58.098 1.00 15.44 ? 99 PHE A N 1 ATOM 764 C CA . PHE A 1 99 ? 12.637 -16.517 58.568 1.00 15.85 ? 99 PHE A CA 1 ATOM 765 C C . PHE A 1 99 ? 12.285 -17.612 59.557 1.00 16.93 ? 99 PHE A C 1 ATOM 766 O O . PHE A 1 99 ? 12.840 -17.668 60.654 1.00 16.41 ? 99 PHE A O 1 ATOM 767 C CB . PHE A 1 99 ? 13.684 -15.584 59.204 1.00 16.22 ? 99 PHE A CB 1 ATOM 768 C CG . PHE A 1 99 ? 14.147 -14.472 58.295 1.00 15.91 ? 99 PHE A CG 1 ATOM 769 C CD1 . PHE A 1 99 ? 14.052 -13.139 58.697 1.00 16.41 ? 99 PHE A CD1 1 ATOM 770 C CD2 . PHE A 1 99 ? 14.676 -14.752 57.037 1.00 15.12 ? 99 PHE A CD2 1 ATOM 771 C CE1 . PHE A 1 99 ? 14.475 -12.099 57.857 1.00 15.43 ? 99 PHE A CE1 1 ATOM 772 C CE2 . PHE A 1 99 ? 15.100 -13.723 56.196 1.00 14.72 ? 99 PHE A CE2 1 ATOM 773 C CZ . PHE A 1 99 ? 14.999 -12.396 56.607 1.00 15.09 ? 99 PHE A CZ 1 ATOM 774 N N . LYS A 1 100 ? 11.366 -18.489 59.175 1.00 17.26 ? 100 LYS A N 1 ATOM 775 C CA . LYS A 1 100 ? 11.019 -19.586 60.053 1.00 19.82 ? 100 LYS A CA 1 ATOM 776 C C . LYS A 1 100 ? 12.184 -20.581 60.121 1.00 19.42 ? 100 LYS A C 1 ATOM 777 O O . LYS A 1 100 ? 13.031 -20.636 59.225 1.00 21.49 ? 100 LYS A O 1 ATOM 778 C CB . LYS A 1 100 ? 9.709 -20.233 59.597 1.00 21.24 ? 100 LYS A CB 1 ATOM 779 C CG . LYS A 1 100 ? 8.530 -19.333 59.946 1.00 21.50 ? 100 LYS A CG 1 ATOM 780 C CD . LYS A 1 100 ? 7.195 -19.971 59.690 1.00 23.37 ? 100 LYS A CD 1 ATOM 781 C CE . LYS A 1 100 ? 6.075 -19.112 60.264 1.00 22.74 ? 100 LYS A CE 1 ATOM 782 N NZ . LYS A 1 100 ? 6.198 -18.930 61.744 1.00 22.35 ? 100 LYS A NZ 1 ATOM 783 N N . ASN A 1 101 ? 12.231 -21.335 61.213 1.00 18.40 ? 101 ASN A N 1 ATOM 784 C CA . ASN A 1 101 ? 13.299 -22.291 61.488 1.00 18.50 ? 101 ASN A CA 1 ATOM 785 C C . ASN A 1 101 ? 14.654 -21.602 61.693 1.00 17.64 ? 101 ASN A C 1 ATOM 786 O O . ASN A 1 101 ? 15.680 -22.002 61.135 1.00 17.17 ? 101 ASN A O 1 ATOM 787 C CB . ASN A 1 101 ? 13.413 -23.366 60.401 1.00 19.26 ? 101 ASN A CB 1 ATOM 788 C CG . ASN A 1 101 ? 14.403 -24.465 60.781 1.00 20.65 ? 101 ASN A CG 1 ATOM 789 O OD1 . ASN A 1 101 ? 14.537 -24.816 61.958 1.00 19.65 ? 101 ASN A OD1 1 ATOM 790 N ND2 . ASN A 1 101 ? 15.091 -25.015 59.790 1.00 20.21 ? 101 ASN A ND2 1 ATOM 791 N N . THR A 1 102 ? 14.632 -20.540 62.492 1.00 16.40 ? 102 THR A N 1 ATOM 792 C CA . THR A 1 102 ? 15.835 -19.809 62.854 1.00 15.60 ? 102 THR A CA 1 ATOM 793 C C . THR A 1 102 ? 15.636 -19.465 64.320 1.00 15.54 ? 102 THR A C 1 ATOM 794 O O . THR A 1 102 ? 14.512 -19.514 64.831 1.00 15.38 ? 102 THR A O 1 ATOM 795 C CB . THR A 1 102 ? 16.010 -18.465 62.062 1.00 16.45 ? 102 THR A CB 1 ATOM 796 O OG1 . THR A 1 102 ? 14.946 -17.560 62.390 1.00 15.04 ? 102 THR A OG1 1 ATOM 797 C CG2 . THR A 1 102 ? 16.028 -18.714 60.567 1.00 15.82 ? 102 THR A CG2 1 ATOM 798 N N . ILE A 1 103 ? 16.721 -19.149 65.009 1.00 14.74 ? 103 ILE A N 1 ATOM 799 C CA . ILE A 1 103 ? 16.614 -18.730 66.395 1.00 15.56 ? 103 ILE A CA 1 ATOM 800 C C . ILE A 1 103 ? 16.294 -17.233 66.244 1.00 15.68 ? 103 ILE A C 1 ATOM 801 O O . ILE A 1 103 ? 17.135 -16.469 65.779 1.00 16.05 ? 103 ILE A O 1 ATOM 802 C CB . ILE A 1 103 ? 17.955 -18.955 67.131 1.00 15.72 ? 103 ILE A CB 1 ATOM 803 C CG1 . ILE A 1 103 ? 18.241 -20.457 67.208 1.00 15.93 ? 103 ILE A CG1 1 ATOM 804 C CG2 . ILE A 1 103 ? 17.903 -18.354 68.528 1.00 13.97 ? 103 ILE A CG2 1 ATOM 805 C CD1 . ILE A 1 103 ? 19.688 -20.793 67.490 1.00 18.83 ? 103 ILE A CD1 1 ATOM 806 N N . LYS A 1 104 ? 15.070 -16.835 66.601 1.00 15.67 ? 104 LYS A N 1 ATOM 807 C CA . LYS A 1 104 ? 14.620 -15.444 66.460 1.00 15.73 ? 104 LYS A CA 1 ATOM 808 C C . LYS A 1 104 ? 14.876 -14.478 67.607 1.00 17.09 ? 104 LYS A C 1 ATOM 809 O O . LYS A 1 104 ? 14.736 -14.820 68.790 1.00 16.02 ? 104 LYS A O 1 ATOM 810 C CB . LYS A 1 104 ? 13.120 -15.393 66.137 1.00 15.96 ? 104 LYS A CB 1 ATOM 811 C CG . LYS A 1 104 ? 12.780 -15.697 64.695 1.00 17.82 ? 104 LYS A CG 1 ATOM 812 C CD . LYS A 1 104 ? 11.304 -15.477 64.397 1.00 15.93 ? 104 LYS A CD 1 ATOM 813 C CE . LYS A 1 104 ? 11.001 -15.929 62.981 1.00 15.90 ? 104 LYS A CE 1 ATOM 814 N NZ . LYS A 1 104 ? 9.545 -15.993 62.671 1.00 15.50 ? 104 LYS A NZ 1 ATOM 815 N N . THR A 1 105 ? 15.218 -13.246 67.231 1.00 17.22 ? 105 THR A N 1 ATOM 816 C CA . THR A 1 105 ? 15.489 -12.173 68.183 1.00 17.57 ? 105 THR A CA 1 ATOM 817 C C . THR A 1 105 ? 14.921 -10.849 67.689 1.00 16.15 ? 105 THR A C 1 ATOM 818 O O . THR A 1 105 ? 14.888 -10.588 66.485 1.00 13.72 ? 105 THR A O 1 ATOM 819 C CB . THR A 1 105 ? 16.990 -11.957 68.373 1.00 18.42 ? 105 THR A CB 1 ATOM 820 O OG1 . THR A 1 105 ? 17.597 -13.184 68.787 1.00 24.22 ? 105 THR A OG1 1 ATOM 821 C CG2 . THR A 1 105 ? 17.243 -10.878 69.415 1.00 21.45 ? 105 THR A CG2 1 ATOM 822 N N . ARG A 1 106 ? 14.477 -10.014 68.623 1.00 15.31 ? 106 ARG A N 1 ATOM 823 C CA . ARG A 1 106 ? 13.965 -8.704 68.266 1.00 15.66 ? 106 ARG A CA 1 ATOM 824 C C . ARG A 1 106 ? 14.953 -7.673 68.814 1.00 15.94 ? 106 ARG A C 1 ATOM 825 O O . ARG A 1 106 ? 15.188 -7.605 70.022 1.00 14.85 ? 106 ARG A O 1 ATOM 826 C CB . ARG A 1 106 ? 12.565 -8.477 68.852 1.00 15.42 ? 106 ARG A CB 1 ATOM 827 C CG . ARG A 1 106 ? 11.890 -7.194 68.356 1.00 17.87 ? 106 ARG A CG 1 ATOM 828 C CD . ARG A 1 106 ? 10.505 -6.998 68.963 1.00 20.68 ? 106 ARG A CD 1 ATOM 829 N NE . ARG A 1 106 ? 9.441 -7.727 68.265 1.00 23.64 ? 106 ARG A NE 1 ATOM 830 C CZ . ARG A 1 106 ? 8.909 -7.363 67.094 1.00 27.17 ? 106 ARG A CZ 1 ATOM 831 N NH1 . ARG A 1 106 ? 9.332 -6.272 66.455 1.00 26.87 ? 106 ARG A NH1 1 ATOM 832 N NH2 . ARG A 1 106 ? 7.932 -8.084 66.563 1.00 26.57 ? 106 ARG A NH2 1 ATOM 833 N N . LEU A 1 107 ? 15.548 -6.892 67.913 1.00 15.10 ? 107 LEU A N 1 ATOM 834 C CA . LEU A 1 107 ? 16.505 -5.866 68.301 1.00 16.36 ? 107 LEU A CA 1 ATOM 835 C C . LEU A 1 107 ? 15.835 -4.859 69.238 1.00 16.83 ? 107 LEU A C 1 ATOM 836 O O . LEU A 1 107 ? 14.607 -4.703 69.238 1.00 16.32 ? 107 LEU A O 1 ATOM 837 C CB . LEU A 1 107 ? 17.055 -5.156 67.052 1.00 16.22 ? 107 LEU A CB 1 ATOM 838 C CG . LEU A 1 107 ? 17.861 -6.032 66.071 1.00 16.20 ? 107 LEU A CG 1 ATOM 839 C CD1 . LEU A 1 107 ? 18.182 -5.264 64.781 1.00 14.43 ? 107 LEU A CD1 1 ATOM 840 C CD2 . LEU A 1 107 ? 19.137 -6.489 66.745 1.00 14.01 ? 107 LEU A CD2 1 ATOM 841 N N . HIS A 1 108 ? 16.644 -4.173 70.036 1.00 16.35 ? 108 HIS A N 1 ATOM 842 C CA . HIS A 1 108 ? 16.117 -3.198 70.978 1.00 16.95 ? 108 HIS A CA 1 ATOM 843 C C . HIS A 1 108 ? 16.143 -1.770 70.474 1.00 16.11 ? 108 HIS A C 1 ATOM 844 O O . HIS A 1 108 ? 16.178 -0.824 71.261 1.00 18.82 ? 108 HIS A O 1 ATOM 845 C CB . HIS A 1 108 ? 16.866 -3.318 72.300 1.00 19.00 ? 108 HIS A CB 1 ATOM 846 C CG . HIS A 1 108 ? 16.580 -4.598 73.019 1.00 23.80 ? 108 HIS A CG 1 ATOM 847 N ND1 . HIS A 1 108 ? 17.347 -5.056 74.067 1.00 26.87 ? 108 HIS A ND1 1 ATOM 848 C CD2 . HIS A 1 108 ? 15.603 -5.518 72.836 1.00 25.86 ? 108 HIS A CD2 1 ATOM 849 C CE1 . HIS A 1 108 ? 16.855 -6.205 74.497 1.00 27.17 ? 108 HIS A CE1 1 ATOM 850 N NE2 . HIS A 1 108 ? 15.798 -6.507 73.767 1.00 25.21 ? 108 HIS A NE2 1 ATOM 851 N N . PHE A 1 109 ? 16.126 -1.618 69.156 1.00 13.38 ? 109 PHE A N 1 ATOM 852 C CA . PHE A 1 109 ? 16.113 -0.301 68.541 1.00 13.00 ? 109 PHE A CA 1 ATOM 853 C C . PHE A 1 109 ? 15.345 -0.389 67.232 1.00 12.78 ? 109 PHE A C 1 ATOM 854 O O . PHE A 1 109 ? 15.281 -1.450 66.608 1.00 12.58 ? 109 PHE A O 1 ATOM 855 C CB . PHE A 1 109 ? 17.544 0.233 68.317 1.00 12.54 ? 109 PHE A CB 1 ATOM 856 C CG . PHE A 1 109 ? 18.432 -0.676 67.503 1.00 12.21 ? 109 PHE A CG 1 ATOM 857 C CD1 . PHE A 1 109 ? 18.476 -0.576 66.112 1.00 13.24 ? 109 PHE A CD1 1 ATOM 858 C CD2 . PHE A 1 109 ? 19.237 -1.625 68.131 1.00 12.15 ? 109 PHE A CD2 1 ATOM 859 C CE1 . PHE A 1 109 ? 19.308 -1.406 65.360 1.00 12.19 ? 109 PHE A CE1 1 ATOM 860 C CE2 . PHE A 1 109 ? 20.073 -2.462 67.391 1.00 11.83 ? 109 PHE A CE2 1 ATOM 861 C CZ . PHE A 1 109 ? 20.109 -2.352 66.002 1.00 13.87 ? 109 PHE A CZ 1 ATOM 862 N N . GLY A 1 110 ? 14.737 0.721 66.839 1.00 12.72 ? 110 GLY A N 1 ATOM 863 C CA . GLY A 1 110 ? 13.970 0.749 65.612 1.00 13.28 ? 110 GLY A CA 1 ATOM 864 C C . GLY A 1 110 ? 14.828 0.844 64.370 1.00 13.33 ? 110 GLY A C 1 ATOM 865 O O . GLY A 1 110 ? 16.049 1.015 64.444 1.00 12.58 ? 110 GLY A O 1 ATOM 866 N N . GLY A 1 111 ? 14.171 0.736 63.219 1.00 14.28 ? 111 GLY A N 1 ATOM 867 C CA . GLY A 1 111 ? 14.870 0.797 61.950 1.00 14.65 ? 111 GLY A CA 1 ATOM 868 C C . GLY A 1 111 ? 14.906 2.161 61.280 1.00 14.26 ? 111 GLY A C 1 ATOM 869 O O . GLY A 1 111 ? 15.489 2.292 60.207 1.00 12.56 ? 111 GLY A O 1 ATOM 870 N N . SER A 1 112 ? 14.298 3.176 61.895 1.00 13.38 ? 112 SER A N 1 ATOM 871 C CA . SER A 1 112 ? 14.302 4.512 61.300 1.00 12.73 ? 112 SER A CA 1 ATOM 872 C C . SER A 1 112 ? 15.693 5.117 61.457 1.00 11.54 ? 112 SER A C 1 ATOM 873 O O . SER A 1 112 ? 16.485 4.657 62.280 1.00 10.53 ? 112 SER A O 1 ATOM 874 C CB . SER A 1 112 ? 13.264 5.416 61.978 1.00 11.76 ? 112 SER A CB 1 ATOM 875 O OG . SER A 1 112 ? 13.657 5.765 63.297 1.00 11.62 ? 112 SER A OG 1 ATOM 876 N N . TYR A 1 113 ? 15.997 6.141 60.667 1.00 10.85 ? 113 TYR A N 1 ATOM 877 C CA . TYR A 1 113 ? 17.309 6.775 60.769 1.00 12.46 ? 113 TYR A CA 1 ATOM 878 C C . TYR A 1 113 ? 17.572 7.332 62.171 1.00 13.37 ? 113 TYR A C 1 ATOM 879 O O . TYR A 1 113 ? 18.661 7.151 62.709 1.00 12.54 ? 113 TYR A O 1 ATOM 880 C CB . TYR A 1 113 ? 17.476 7.865 59.700 1.00 11.37 ? 113 TYR A CB 1 ATOM 881 C CG . TYR A 1 113 ? 17.653 7.300 58.302 1.00 11.18 ? 113 TYR A CG 1 ATOM 882 C CD1 . TYR A 1 113 ? 18.578 6.271 58.059 1.00 10.70 ? 113 TYR A CD1 1 ATOM 883 C CD2 . TYR A 1 113 ? 16.903 7.786 57.225 1.00 9.49 ? 113 TYR A CD2 1 ATOM 884 C CE1 . TYR A 1 113 ? 18.753 5.739 56.779 1.00 11.68 ? 113 TYR A CE1 1 ATOM 885 C CE2 . TYR A 1 113 ? 17.071 7.267 55.935 1.00 9.55 ? 113 TYR A CE2 1 ATOM 886 C CZ . TYR A 1 113 ? 17.998 6.245 55.721 1.00 10.97 ? 113 TYR A CZ 1 ATOM 887 O OH . TYR A 1 113 ? 18.192 5.744 54.455 1.00 11.87 ? 113 TYR A OH 1 ATOM 888 N N . PRO A 1 114 ? 16.585 8.025 62.780 1.00 14.26 ? 114 PRO A N 1 ATOM 889 C CA . PRO A 1 114 ? 16.852 8.542 64.129 1.00 13.92 ? 114 PRO A CA 1 ATOM 890 C C . PRO A 1 114 ? 17.009 7.414 65.165 1.00 13.10 ? 114 PRO A C 1 ATOM 891 O O . PRO A 1 114 ? 17.723 7.574 66.159 1.00 13.20 ? 114 PRO A O 1 ATOM 892 C CB . PRO A 1 114 ? 15.656 9.465 64.401 1.00 14.22 ? 114 PRO A CB 1 ATOM 893 C CG . PRO A 1 114 ? 14.593 8.956 63.495 1.00 16.14 ? 114 PRO A CG 1 ATOM 894 C CD . PRO A 1 114 ? 15.342 8.598 62.241 1.00 13.90 ? 114 PRO A CD 1 ATOM 895 N N . SER A 1 115 ? 16.351 6.277 64.936 1.00 11.87 ? 115 SER A N 1 ATOM 896 C CA . SER A 1 115 ? 16.487 5.145 65.849 1.00 11.66 ? 115 SER A CA 1 ATOM 897 C C . SER A 1 115 ? 17.897 4.552 65.690 1.00 12.91 ? 115 SER A C 1 ATOM 898 O O . SER A 1 115 ? 18.514 4.112 66.669 1.00 13.72 ? 115 SER A O 1 ATOM 899 C CB . SER A 1 115 ? 15.432 4.069 65.552 1.00 13.29 ? 115 SER A CB 1 ATOM 900 O OG . SER A 1 115 ? 14.128 4.503 65.917 1.00 16.39 ? 115 SER A OG 1 ATOM 901 N N . LEU A 1 116 ? 18.402 4.539 64.455 1.00 12.85 ? 116 LEU A N 1 ATOM 902 C CA . LEU A 1 116 ? 19.742 4.017 64.190 1.00 12.70 ? 116 LEU A CA 1 ATOM 903 C C . LEU A 1 116 ? 20.797 4.964 64.771 1.00 13.74 ? 116 LEU A C 1 ATOM 904 O O . LEU A 1 116 ? 21.874 4.522 65.195 1.00 14.71 ? 116 LEU A O 1 ATOM 905 C CB . LEU A 1 116 ? 19.964 3.821 62.681 1.00 12.58 ? 116 LEU A CB 1 ATOM 906 C CG . LEU A 1 116 ? 19.224 2.638 62.036 1.00 12.53 ? 116 LEU A CG 1 ATOM 907 C CD1 . LEU A 1 116 ? 19.295 2.739 60.529 1.00 13.55 ? 116 LEU A CD1 1 ATOM 908 C CD2 . LEU A 1 116 ? 19.822 1.318 62.508 1.00 14.70 ? 116 LEU A CD2 1 ATOM 909 N N . GLU A 1 117 ? 20.495 6.263 64.807 1.00 13.54 ? 117 GLU A N 1 ATOM 910 C CA . GLU A 1 117 ? 21.438 7.236 65.374 1.00 14.71 ? 117 GLU A CA 1 ATOM 911 C C . GLU A 1 117 ? 21.545 6.995 66.871 1.00 14.74 ? 117 GLU A C 1 ATOM 912 O O . GLU A 1 117 ? 22.552 7.325 67.494 1.00 15.73 ? 117 GLU A O 1 ATOM 913 C CB . GLU A 1 117 ? 20.970 8.672 65.120 1.00 15.79 ? 117 GLU A CB 1 ATOM 914 C CG . GLU A 1 117 ? 20.911 9.030 63.651 1.00 16.58 ? 117 GLU A CG 1 ATOM 915 C CD . GLU A 1 117 ? 20.405 10.429 63.408 1.00 18.09 ? 117 GLU A CD 1 ATOM 916 O OE1 . GLU A 1 117 ? 19.670 10.959 64.269 1.00 18.74 ? 117 GLU A OE1 1 ATOM 917 O OE2 . GLU A 1 117 ? 20.732 10.993 62.342 1.00 21.42 ? 117 GLU A OE2 1 ATOM 918 N N . GLY A 1 118 ? 20.488 6.430 67.444 1.00 15.29 ? 118 GLY A N 1 ATOM 919 C CA . GLY A 1 118 ? 20.496 6.122 68.862 1.00 14.69 ? 118 GLY A CA 1 ATOM 920 C C . GLY A 1 118 ? 21.548 5.060 69.137 1.00 15.82 ? 118 GLY A C 1 ATOM 921 O O . GLY A 1 118 ? 22.021 4.925 70.269 1.00 15.04 ? 118 GLY A O 1 ATOM 922 N N . GLU A 1 119 ? 21.908 4.303 68.098 1.00 15.05 ? 119 GLU A N 1 ATOM 923 C CA . GLU A 1 119 ? 22.922 3.259 68.208 1.00 16.44 ? 119 GLU A CA 1 ATOM 924 C C . GLU A 1 119 ? 24.233 3.715 67.581 1.00 15.92 ? 119 GLU A C 1 ATOM 925 O O . GLU A 1 119 ? 25.040 2.897 67.137 1.00 17.03 ? 119 GLU A O 1 ATOM 926 C CB . GLU A 1 119 ? 22.453 1.972 67.528 1.00 18.51 ? 119 GLU A CB 1 ATOM 927 C CG . GLU A 1 119 ? 21.294 1.289 68.226 1.00 22.27 ? 119 GLU A CG 1 ATOM 928 C CD . GLU A 1 119 ? 21.536 1.109 69.721 1.00 28.10 ? 119 GLU A CD 1 ATOM 929 O OE1 . GLU A 1 119 ? 22.599 0.558 70.101 1.00 27.78 ? 119 GLU A OE1 1 ATOM 930 O OE2 . GLU A 1 119 ? 20.653 1.524 70.514 1.00 30.67 ? 119 GLU A OE2 1 ATOM 931 N N . LYS A 1 120 ? 24.420 5.030 67.537 1.00 16.08 ? 120 LYS A N 1 ATOM 932 C CA . LYS A 1 120 ? 25.625 5.664 67.000 1.00 14.96 ? 120 LYS A CA 1 ATOM 933 C C . LYS A 1 120 ? 25.846 5.606 65.489 1.00 13.85 ? 120 LYS A C 1 ATOM 934 O O . LYS A 1 120 ? 26.921 5.966 65.016 1.00 13.71 ? 120 LYS A O 1 ATOM 935 C CB . LYS A 1 120 ? 26.872 5.116 67.708 1.00 16.47 ? 120 LYS A CB 1 ATOM 936 C CG . LYS A 1 120 ? 26.819 5.190 69.231 1.00 19.70 ? 120 LYS A CG 1 ATOM 937 C CD . LYS A 1 120 ? 28.140 4.728 69.842 1.00 24.75 ? 120 LYS A CD 1 ATOM 938 C CE . LYS A 1 120 ? 28.016 4.458 71.346 1.00 29.43 ? 120 LYS A CE 1 ATOM 939 N NZ . LYS A 1 120 ? 27.502 5.623 72.133 1.00 32.65 ? 120 LYS A NZ 1 ATOM 940 N N . ALA A 1 121 ? 24.848 5.171 64.725 1.00 13.64 ? 121 ALA A N 1 ATOM 941 C CA . ALA A 1 121 ? 24.999 5.106 63.270 1.00 11.99 ? 121 ALA A CA 1 ATOM 942 C C . ALA A 1 121 ? 24.358 6.330 62.597 1.00 12.13 ? 121 ALA A C 1 ATOM 943 O O . ALA A 1 121 ? 23.131 6.405 62.462 1.00 9.52 ? 121 ALA A O 1 ATOM 944 C CB . ALA A 1 121 ? 24.374 3.818 62.733 1.00 11.90 ? 121 ALA A CB 1 ATOM 945 N N . TYR A 1 122 ? 25.200 7.274 62.173 1.00 10.74 ? 122 TYR A N 1 ATOM 946 C CA . TYR A 1 122 ? 24.748 8.506 61.523 1.00 12.76 ? 122 TYR A CA 1 ATOM 947 C C . TYR A 1 122 ? 25.067 8.510 60.033 1.00 12.90 ? 122 TYR A C 1 ATOM 948 O O . TYR A 1 122 ? 26.199 8.223 59.635 1.00 12.80 ? 122 TYR A O 1 ATOM 949 C CB . TYR A 1 122 ? 25.428 9.724 62.165 1.00 12.04 ? 122 TYR A CB 1 ATOM 950 C CG . TYR A 1 122 ? 25.067 9.959 63.612 1.00 13.56 ? 122 TYR A CG 1 ATOM 951 C CD1 . TYR A 1 122 ? 24.032 10.826 63.961 1.00 14.85 ? 122 TYR A CD1 1 ATOM 952 C CD2 . TYR A 1 122 ? 25.752 9.303 64.637 1.00 15.42 ? 122 TYR A CD2 1 ATOM 953 C CE1 . TYR A 1 122 ? 23.683 11.042 65.307 1.00 16.17 ? 122 TYR A CE1 1 ATOM 954 C CE2 . TYR A 1 122 ? 25.411 9.507 65.986 1.00 16.49 ? 122 TYR A CE2 1 ATOM 955 C CZ . TYR A 1 122 ? 24.378 10.378 66.310 1.00 15.98 ? 122 TYR A CZ 1 ATOM 956 O OH . TYR A 1 122 ? 24.045 10.588 67.629 1.00 19.28 ? 122 TYR A OH 1 ATOM 957 N N . ARG A 1 123 ? 24.082 8.860 59.212 1.00 12.99 ? 123 ARG A N 1 ATOM 958 C CA . ARG A 1 123 ? 24.294 8.907 57.766 1.00 14.99 ? 123 ARG A CA 1 ATOM 959 C C . ARG A 1 123 ? 25.484 9.787 57.387 1.00 15.51 ? 123 ARG A C 1 ATOM 960 O O . ARG A 1 123 ? 26.287 9.431 56.529 1.00 14.56 ? 123 ARG A O 1 ATOM 961 C CB . ARG A 1 123 ? 23.042 9.429 57.052 1.00 13.94 ? 123 ARG A CB 1 ATOM 962 C CG . ARG A 1 123 ? 21.948 8.391 56.864 1.00 13.27 ? 123 ARG A CG 1 ATOM 963 C CD . ARG A 1 123 ? 20.702 9.001 56.227 1.00 12.47 ? 123 ARG A CD 1 ATOM 964 N NE . ARG A 1 123 ? 19.940 9.812 57.176 1.00 12.23 ? 123 ARG A NE 1 ATOM 965 C CZ . ARG A 1 123 ? 18.837 10.492 56.867 1.00 12.31 ? 123 ARG A CZ 1 ATOM 966 N NH1 . ARG A 1 123 ? 18.367 10.466 55.628 1.00 8.92 ? 123 ARG A NH1 1 ATOM 967 N NH2 . ARG A 1 123 ? 18.194 11.190 57.801 1.00 11.92 ? 123 ARG A NH2 1 ATOM 968 N N . GLU A 1 124 ? 25.603 10.938 58.036 1.00 18.05 ? 124 GLU A N 1 ATOM 969 C CA . GLU A 1 124 ? 26.689 11.852 57.721 1.00 20.74 ? 124 GLU A CA 1 ATOM 970 C C . GLU A 1 124 ? 28.092 11.301 57.993 1.00 20.04 ? 124 GLU A C 1 ATOM 971 O O . GLU A 1 124 ? 29.058 11.779 57.404 1.00 20.32 ? 124 GLU A O 1 ATOM 972 C CB . GLU A 1 124 ? 26.489 13.182 58.458 1.00 23.35 ? 124 GLU A CB 1 ATOM 973 C CG . GLU A 1 124 ? 26.130 13.025 59.915 1.00 32.08 ? 124 GLU A CG 1 ATOM 974 C CD . GLU A 1 124 ? 24.624 13.032 60.165 1.00 36.32 ? 124 GLU A CD 1 ATOM 975 O OE1 . GLU A 1 124 ? 23.877 12.336 59.443 1.00 37.50 ? 124 GLU A OE1 1 ATOM 976 O OE2 . GLU A 1 124 ? 24.188 13.735 61.105 1.00 40.01 ? 124 GLU A OE2 1 ATOM 977 N N . THR A 1 125 ? 28.222 10.294 58.855 1.00 18.67 ? 125 THR A N 1 ATOM 978 C CA . THR A 1 125 ? 29.552 9.756 59.143 1.00 17.89 ? 125 THR A CA 1 ATOM 979 C C . THR A 1 125 ? 29.739 8.276 58.832 1.00 18.42 ? 125 THR A C 1 ATOM 980 O O . THR A 1 125 ? 30.657 7.638 59.341 1.00 19.11 ? 125 THR A O 1 ATOM 981 C CB . THR A 1 125 ? 29.934 9.981 60.607 1.00 17.46 ? 125 THR A CB 1 ATOM 982 O OG1 . THR A 1 125 ? 29.020 9.272 61.449 1.00 18.63 ? 125 THR A OG1 1 ATOM 983 C CG2 . THR A 1 125 ? 29.878 11.460 60.945 1.00 16.22 ? 125 THR A CG2 1 ATOM 984 N N . THR A 1 126 ? 28.873 7.727 57.993 1.00 18.56 ? 126 THR A N 1 ATOM 985 C CA . THR A 1 126 ? 28.975 6.321 57.632 1.00 16.78 ? 126 THR A CA 1 ATOM 986 C C . THR A 1 126 ? 29.363 6.204 56.160 1.00 16.68 ? 126 THR A C 1 ATOM 987 O O . THR A 1 126 ? 28.639 6.656 55.276 1.00 14.48 ? 126 THR A O 1 ATOM 988 C CB . THR A 1 126 ? 27.634 5.586 57.897 1.00 17.86 ? 126 THR A CB 1 ATOM 989 O OG1 . THR A 1 126 ? 27.342 5.619 59.301 1.00 17.74 ? 126 THR A OG1 1 ATOM 990 C CG2 . THR A 1 126 ? 27.704 4.130 57.433 1.00 16.32 ? 126 THR A CG2 1 ATOM 991 N N . ASP A 1 127 ? 30.531 5.618 55.915 1.00 17.23 ? 127 ASP A N 1 ATOM 992 C CA . ASP A 1 127 ? 31.047 5.411 54.565 1.00 17.25 ? 127 ASP A CA 1 ATOM 993 C C . ASP A 1 127 ? 30.173 4.448 53.769 1.00 16.95 ? 127 ASP A C 1 ATOM 994 O O . ASP A 1 127 ? 29.646 3.477 54.315 1.00 17.60 ? 127 ASP A O 1 ATOM 995 C CB . ASP A 1 127 ? 32.459 4.823 54.627 1.00 18.36 ? 127 ASP A CB 1 ATOM 996 C CG . ASP A 1 127 ? 33.508 5.845 55.001 1.00 20.54 ? 127 ASP A CG 1 ATOM 997 O OD1 . ASP A 1 127 ? 34.672 5.438 55.197 1.00 21.00 ? 127 ASP A OD1 1 ATOM 998 O OD2 . ASP A 1 127 ? 33.178 7.047 55.088 1.00 21.37 ? 127 ASP A OD2 1 ATOM 999 N N . LEU A 1 128 ? 30.030 4.719 52.477 1.00 15.76 ? 128 LEU A N 1 ATOM 1000 C CA . LEU A 1 128 ? 29.261 3.858 51.586 1.00 14.65 ? 128 LEU A CA 1 ATOM 1001 C C . LEU A 1 128 ? 30.177 3.497 50.410 1.00 14.38 ? 128 LEU A C 1 ATOM 1002 O O . LEU A 1 128 ? 31.026 4.295 50.002 1.00 14.79 ? 128 LEU A O 1 ATOM 1003 C CB . LEU A 1 128 ? 28.003 4.581 51.076 1.00 14.68 ? 128 LEU A CB 1 ATOM 1004 C CG . LEU A 1 128 ? 26.982 5.124 52.091 1.00 14.40 ? 128 LEU A CG 1 ATOM 1005 C CD1 . LEU A 1 128 ? 25.854 5.811 51.332 1.00 10.80 ? 128 LEU A CD1 1 ATOM 1006 C CD2 . LEU A 1 128 ? 26.433 4.005 52.964 1.00 10.89 ? 128 LEU A CD2 1 ATOM 1007 N N . GLY A 1 129 ? 30.008 2.291 49.877 1.00 14.43 ? 129 GLY A N 1 ATOM 1008 C CA . GLY A 1 129 ? 30.831 1.839 48.768 1.00 12.68 ? 129 GLY A CA 1 ATOM 1009 C C . GLY A 1 129 ? 30.953 0.335 48.852 1.00 13.73 ? 129 GLY A C 1 ATOM 1010 O O . GLY A 1 129 ? 30.401 -0.263 49.771 1.00 14.58 ? 129 GLY A O 1 ATOM 1011 N N . ILE A 1 130 ? 31.669 -0.289 47.921 1.00 13.38 ? 130 ILE A N 1 ATOM 1012 C CA . ILE A 1 130 ? 31.799 -1.743 47.955 1.00 15.15 ? 130 ILE A CA 1 ATOM 1013 C C . ILE A 1 130 ? 32.571 -2.274 49.178 1.00 15.51 ? 130 ILE A C 1 ATOM 1014 O O . ILE A 1 130 ? 32.200 -3.307 49.729 1.00 16.24 ? 130 ILE A O 1 ATOM 1015 C CB . ILE A 1 130 ? 32.434 -2.287 46.646 1.00 14.04 ? 130 ILE A CB 1 ATOM 1016 C CG1 . ILE A 1 130 ? 32.313 -3.812 46.610 1.00 12.92 ? 130 ILE A CG1 1 ATOM 1017 C CG2 . ILE A 1 130 ? 33.877 -1.843 46.536 1.00 16.60 ? 130 ILE A CG2 1 ATOM 1018 C CD1 . ILE A 1 130 ? 30.868 -4.304 46.627 1.00 13.17 ? 130 ILE A CD1 1 ATOM 1019 N N . GLU A 1 131 ? 33.631 -1.591 49.608 1.00 16.34 ? 131 GLU A N 1 ATOM 1020 C CA . GLU A 1 131 ? 34.361 -2.055 50.793 1.00 17.29 ? 131 GLU A CA 1 ATOM 1021 C C . GLU A 1 131 ? 33.476 -1.922 52.033 1.00 17.15 ? 131 GLU A C 1 ATOM 1022 O O . GLU A 1 131 ? 33.405 -2.841 52.848 1.00 16.92 ? 131 GLU A O 1 ATOM 1023 C CB . GLU A 1 131 ? 35.662 -1.279 50.996 1.00 20.32 ? 131 GLU A CB 1 ATOM 1024 C CG . GLU A 1 131 ? 36.887 -2.020 50.489 1.00 26.68 ? 131 GLU A CG 1 ATOM 1025 C CD . GLU A 1 131 ? 37.030 -3.417 51.099 1.00 28.27 ? 131 GLU A CD 1 ATOM 1026 O OE1 . GLU A 1 131 ? 37.175 -3.522 52.335 1.00 30.97 ? 131 GLU A OE1 1 ATOM 1027 O OE2 . GLU A 1 131 ? 36.997 -4.410 50.339 1.00 28.87 ? 131 GLU A OE2 1 ATOM 1028 N N . PRO A 1 132 ? 32.815 -0.758 52.211 1.00 17.22 ? 132 PRO A N 1 ATOM 1029 C CA . PRO A 1 132 ? 31.940 -0.593 53.377 1.00 14.96 ? 132 PRO A CA 1 ATOM 1030 C C . PRO A 1 132 ? 30.845 -1.664 53.385 1.00 14.32 ? 132 PRO A C 1 ATOM 1031 O O . PRO A 1 132 ? 30.364 -2.065 54.443 1.00 14.37 ? 132 PRO A O 1 ATOM 1032 C CB . PRO A 1 132 ? 31.379 0.807 53.179 1.00 15.87 ? 132 PRO A CB 1 ATOM 1033 C CG . PRO A 1 132 ? 32.567 1.533 52.599 1.00 15.29 ? 132 PRO A CG 1 ATOM 1034 C CD . PRO A 1 132 ? 33.067 0.546 51.562 1.00 15.54 ? 132 PRO A CD 1 ATOM 1035 N N . LEU A 1 133 ? 30.454 -2.126 52.199 1.00 13.07 ? 133 LEU A N 1 ATOM 1036 C CA . LEU A 1 133 ? 29.426 -3.157 52.092 1.00 12.56 ? 133 LEU A CA 1 ATOM 1037 C C . LEU A 1 133 ? 29.995 -4.522 52.489 1.00 13.11 ? 133 LEU A C 1 ATOM 1038 O O . LEU A 1 133 ? 29.349 -5.283 53.201 1.00 13.14 ? 133 LEU A O 1 ATOM 1039 C CB . LEU A 1 133 ? 28.863 -3.217 50.668 1.00 12.65 ? 133 LEU A CB 1 ATOM 1040 C CG . LEU A 1 133 ? 27.770 -4.274 50.444 1.00 12.10 ? 133 LEU A CG 1 ATOM 1041 C CD1 . LEU A 1 133 ? 26.558 -3.977 51.320 1.00 12.32 ? 133 LEU A CD1 1 ATOM 1042 C CD2 . LEU A 1 133 ? 27.372 -4.295 48.979 1.00 13.93 ? 133 LEU A CD2 1 ATOM 1043 N N . ARG A 1 134 ? 31.198 -4.838 52.015 1.00 13.62 ? 134 ARG A N 1 ATOM 1044 C CA . ARG A 1 134 ? 31.842 -6.105 52.364 1.00 14.52 ? 134 ARG A CA 1 ATOM 1045 C C . ARG A 1 134 ? 31.984 -6.205 53.881 1.00 13.83 ? 134 ARG A C 1 ATOM 1046 O O . ARG A 1 134 ? 31.716 -7.247 54.475 1.00 12.63 ? 134 ARG A O 1 ATOM 1047 C CB . ARG A 1 134 ? 33.235 -6.191 51.730 1.00 15.62 ? 134 ARG A CB 1 ATOM 1048 C CG . ARG A 1 134 ? 33.221 -6.397 50.233 1.00 16.15 ? 134 ARG A CG 1 ATOM 1049 C CD . ARG A 1 134 ? 34.619 -6.329 49.663 1.00 18.85 ? 134 ARG A CD 1 ATOM 1050 N NE . ARG A 1 134 ? 34.650 -6.733 48.261 1.00 20.34 ? 134 ARG A NE 1 ATOM 1051 C CZ . ARG A 1 134 ? 35.185 -6.004 47.289 1.00 20.56 ? 134 ARG A CZ 1 ATOM 1052 N NH1 . ARG A 1 134 ? 35.734 -4.830 47.566 1.00 18.59 ? 134 ARG A NH1 1 ATOM 1053 N NH2 . ARG A 1 134 ? 35.171 -6.451 46.040 1.00 22.94 ? 134 ARG A NH2 1 ATOM 1054 N N . ILE A 1 135 ? 32.416 -5.108 54.495 1.00 12.92 ? 135 ILE A N 1 ATOM 1055 C CA . ILE A 1 135 ? 32.610 -5.049 55.935 1.00 14.18 ? 135 ILE A CA 1 ATOM 1056 C C . ILE A 1 135 ? 31.284 -5.167 56.687 1.00 14.48 ? 135 ILE A C 1 ATOM 1057 O O . ILE A 1 135 ? 31.219 -5.795 57.748 1.00 14.10 ? 135 ILE A O 1 ATOM 1058 C CB . ILE A 1 135 ? 33.333 -3.734 56.319 1.00 16.84 ? 135 ILE A CB 1 ATOM 1059 C CG1 . ILE A 1 135 ? 34.757 -3.763 55.755 1.00 17.85 ? 135 ILE A CG1 1 ATOM 1060 C CG2 . ILE A 1 135 ? 33.350 -3.547 57.829 1.00 16.66 ? 135 ILE A CG2 1 ATOM 1061 C CD1 . ILE A 1 135 ? 35.515 -2.473 55.930 1.00 20.21 ? 135 ILE A CD1 1 ATOM 1062 N N . GLY A 1 136 ? 30.231 -4.566 56.134 1.00 14.46 ? 136 GLY A N 1 ATOM 1063 C CA . GLY A 1 136 ? 28.922 -4.633 56.765 1.00 12.88 ? 136 GLY A CA 1 ATOM 1064 C C . GLY A 1 136 ? 28.407 -6.061 56.818 1.00 13.55 ? 136 GLY A C 1 ATOM 1065 O O . GLY A 1 136 ? 27.874 -6.505 57.837 1.00 15.38 ? 136 GLY A O 1 ATOM 1066 N N . ILE A 1 137 ? 28.557 -6.785 55.715 1.00 12.64 ? 137 ILE A N 1 ATOM 1067 C CA . ILE A 1 137 ? 28.125 -8.174 55.656 1.00 13.84 ? 137 ILE A CA 1 ATOM 1068 C C . ILE A 1 137 ? 28.938 -8.974 56.666 1.00 15.91 ? 137 ILE A C 1 ATOM 1069 O O . ILE A 1 137 ? 28.395 -9.790 57.410 1.00 17.00 ? 137 ILE A O 1 ATOM 1070 C CB . ILE A 1 137 ? 28.357 -8.783 54.256 1.00 13.02 ? 137 ILE A CB 1 ATOM 1071 C CG1 . ILE A 1 137 ? 27.484 -8.063 53.227 1.00 12.81 ? 137 ILE A CG1 1 ATOM 1072 C CG2 . ILE A 1 137 ? 28.058 -10.278 54.285 1.00 12.96 ? 137 ILE A CG2 1 ATOM 1073 C CD1 . ILE A 1 137 ? 27.863 -8.346 51.785 1.00 15.93 ? 137 ILE A CD1 1 ATOM 1074 N N . LYS A 1 138 ? 30.244 -8.722 56.687 1.00 16.04 ? 138 LYS A N 1 ATOM 1075 C CA . LYS A 1 138 ? 31.152 -9.411 57.591 1.00 14.70 ? 138 LYS A CA 1 ATOM 1076 C C . LYS A 1 138 ? 30.731 -9.207 59.033 1.00 15.01 ? 138 LYS A C 1 ATOM 1077 O O . LYS A 1 138 ? 30.718 -10.155 59.817 1.00 15.94 ? 138 LYS A O 1 ATOM 1078 C CB . LYS A 1 138 ? 32.579 -8.894 57.384 1.00 17.12 ? 138 LYS A CB 1 ATOM 1079 C CG . LYS A 1 138 ? 33.598 -9.405 58.392 1.00 18.16 ? 138 LYS A CG 1 ATOM 1080 C CD . LYS A 1 138 ? 34.932 -8.730 58.178 1.00 21.88 ? 138 LYS A CD 1 ATOM 1081 C CE . LYS A 1 138 ? 35.885 -9.033 59.306 1.00 26.40 ? 138 LYS A CE 1 ATOM 1082 N NZ . LYS A 1 138 ? 36.055 -10.507 59.455 1.00 34.13 ? 138 LYS A NZ 1 ATOM 1083 N N . LYS A 1 139 ? 30.385 -7.973 59.386 1.00 14.11 ? 139 LYS A N 1 ATOM 1084 C CA . LYS A 1 139 ? 29.970 -7.671 60.752 1.00 14.59 ? 139 LYS A CA 1 ATOM 1085 C C . LYS A 1 139 ? 28.632 -8.313 61.129 1.00 15.52 ? 139 LYS A C 1 ATOM 1086 O O . LYS A 1 139 ? 28.450 -8.762 62.265 1.00 12.88 ? 139 LYS A O 1 ATOM 1087 C CB . LYS A 1 139 ? 29.888 -6.160 60.965 1.00 16.01 ? 139 LYS A CB 1 ATOM 1088 C CG . LYS A 1 139 ? 31.228 -5.456 60.986 1.00 21.05 ? 139 LYS A CG 1 ATOM 1089 C CD . LYS A 1 139 ? 31.011 -3.991 61.299 1.00 28.47 ? 139 LYS A CD 1 ATOM 1090 C CE . LYS A 1 139 ? 32.303 -3.198 61.292 1.00 32.48 ? 139 LYS A CE 1 ATOM 1091 N NZ . LYS A 1 139 ? 32.017 -1.747 61.529 1.00 35.79 ? 139 LYS A NZ 1 ATOM 1092 N N . LEU A 1 140 ? 27.692 -8.355 60.188 1.00 15.02 ? 140 LEU A N 1 ATOM 1093 C CA . LEU A 1 140 ? 26.393 -8.954 60.473 1.00 15.61 ? 140 LEU A CA 1 ATOM 1094 C C . LEU A 1 140 ? 26.562 -10.439 60.779 1.00 16.71 ? 140 LEU A C 1 ATOM 1095 O O . LEU A 1 140 ? 25.899 -10.983 61.669 1.00 16.01 ? 140 LEU A O 1 ATOM 1096 C CB . LEU A 1 140 ? 25.440 -8.761 59.292 1.00 12.93 ? 140 LEU A CB 1 ATOM 1097 C CG . LEU A 1 140 ? 24.917 -7.337 59.086 1.00 13.68 ? 140 LEU A CG 1 ATOM 1098 C CD1 . LEU A 1 140 ? 23.983 -7.339 57.894 1.00 13.12 ? 140 LEU A CD1 1 ATOM 1099 C CD2 . LEU A 1 140 ? 24.178 -6.839 60.335 1.00 11.01 ? 140 LEU A CD2 1 ATOM 1100 N N . ASP A 1 141 ? 27.457 -11.090 60.042 1.00 18.00 ? 141 ASP A N 1 ATOM 1101 C CA . ASP A 1 141 ? 27.708 -12.509 60.248 1.00 19.56 ? 141 ASP A CA 1 ATOM 1102 C C . ASP A 1 141 ? 28.457 -12.720 61.563 1.00 19.97 ? 141 ASP A C 1 ATOM 1103 O O . ASP A 1 141 ? 28.131 -13.622 62.333 1.00 20.20 ? 141 ASP A O 1 ATOM 1104 C CB . ASP A 1 141 ? 28.516 -13.082 59.082 1.00 20.25 ? 141 ASP A CB 1 ATOM 1105 C CG . ASP A 1 141 ? 28.811 -14.562 59.251 1.00 21.68 ? 141 ASP A CG 1 ATOM 1106 O OD1 . ASP A 1 141 ? 29.984 -14.914 59.502 1.00 22.86 ? 141 ASP A OD1 1 ATOM 1107 O OD2 . ASP A 1 141 ? 27.866 -15.372 59.139 1.00 21.55 ? 141 ASP A OD2 1 ATOM 1108 N N . GLU A 1 142 ? 29.457 -11.883 61.821 1.00 19.85 ? 142 GLU A N 1 ATOM 1109 C CA . GLU A 1 142 ? 30.232 -11.985 63.055 1.00 21.39 ? 142 GLU A CA 1 ATOM 1110 C C . GLU A 1 142 ? 29.338 -11.820 64.277 1.00 21.43 ? 142 GLU A C 1 ATOM 1111 O O . GLU A 1 142 ? 29.633 -12.336 65.349 1.00 22.19 ? 142 GLU A O 1 ATOM 1112 C CB . GLU A 1 142 ? 31.332 -10.917 63.092 1.00 22.28 ? 142 GLU A CB 1 ATOM 1113 C CG . GLU A 1 142 ? 32.534 -11.232 62.233 1.00 25.66 ? 142 GLU A CG 1 ATOM 1114 C CD . GLU A 1 142 ? 33.569 -10.120 62.242 1.00 29.38 ? 142 GLU A CD 1 ATOM 1115 O OE1 . GLU A 1 142 ? 34.657 -10.312 61.653 1.00 29.87 ? 142 GLU A OE1 1 ATOM 1116 O OE2 . GLU A 1 142 ? 33.293 -9.052 62.831 1.00 30.88 ? 142 GLU A OE2 1 ATOM 1117 N N . ASN A 1 143 ? 28.242 -11.093 64.115 1.00 20.63 ? 143 ASN A N 1 ATOM 1118 C CA . ASN A 1 143 ? 27.325 -10.869 65.219 1.00 19.90 ? 143 ASN A CA 1 ATOM 1119 C C . ASN A 1 143 ? 26.142 -11.830 65.233 1.00 18.90 ? 143 ASN A C 1 ATOM 1120 O O . ASN A 1 143 ? 25.102 -11.536 65.826 1.00 19.16 ? 143 ASN A O 1 ATOM 1121 C CB . ASN A 1 143 ? 26.843 -9.419 65.198 1.00 20.38 ? 143 ASN A CB 1 ATOM 1122 C CG . ASN A 1 143 ? 27.886 -8.464 65.733 1.00 20.91 ? 143 ASN A CG 1 ATOM 1123 O OD1 . ASN A 1 143 ? 28.064 -8.337 66.948 1.00 21.11 ? 143 ASN A OD1 1 ATOM 1124 N ND2 . ASN A 1 143 ? 28.599 -7.801 64.831 1.00 19.79 ? 143 ASN A ND2 1 ATOM 1125 N N . ALA A 1 144 ? 26.299 -12.975 64.572 1.00 19.17 ? 144 ALA A N 1 ATOM 1126 C CA . ALA A 1 144 ? 25.247 -13.989 64.549 1.00 19.15 ? 144 ALA A CA 1 ATOM 1127 C C . ALA A 1 144 ? 25.434 -14.791 65.833 1.00 20.38 ? 144 ALA A C 1 ATOM 1128 O O . ALA A 1 144 ? 25.683 -15.997 65.795 1.00 19.82 ? 144 ALA A O 1 ATOM 1129 C CB . ALA A 1 144 ? 25.398 -14.896 63.328 1.00 18.79 ? 144 ALA A CB 1 ATOM 1130 N N . ILE A 1 145 ? 25.325 -14.092 66.964 1.00 21.14 ? 145 ILE A N 1 ATOM 1131 C CA . ILE A 1 145 ? 25.495 -14.675 68.293 1.00 22.30 ? 145 ILE A CA 1 ATOM 1132 C C . ILE A 1 145 ? 24.511 -14.059 69.289 1.00 23.19 ? 145 ILE A C 1 ATOM 1133 O O . ILE A 1 145 ? 23.818 -13.099 68.974 1.00 23.36 ? 145 ILE A O 1 ATOM 1134 C CB . ILE A 1 145 ? 26.925 -14.429 68.812 1.00 20.38 ? 145 ILE A CB 1 ATOM 1135 C CG1 . ILE A 1 145 ? 27.213 -12.923 68.826 1.00 20.69 ? 145 ILE A CG1 1 ATOM 1136 C CG2 . ILE A 1 145 ? 27.922 -15.169 67.939 1.00 18.56 ? 145 ILE A CG2 1 ATOM 1137 C CD1 . ILE A 1 145 ? 28.606 -12.551 69.260 1.00 18.39 ? 145 ILE A CD1 1 ATOM 1138 N N . ASP A 1 146 ? 24.457 -14.615 70.493 1.00 26.13 ? 146 ASP A N 1 ATOM 1139 C CA . ASP A 1 146 ? 23.561 -14.108 71.531 1.00 28.93 ? 146 ASP A CA 1 ATOM 1140 C C . ASP A 1 146 ? 24.033 -12.743 72.029 1.00 28.60 ? 146 ASP A C 1 ATOM 1141 O O . ASP A 1 146 ? 23.242 -11.813 72.183 1.00 29.13 ? 146 ASP A O 1 ATOM 1142 C CB . ASP A 1 146 ? 23.512 -15.072 72.729 1.00 33.90 ? 146 ASP A CB 1 ATOM 1143 C CG . ASP A 1 146 ? 22.876 -16.415 72.391 1.00 39.62 ? 146 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 146 ? 21.641 -16.464 72.182 1.00 41.48 ? 146 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 146 ? 23.617 -17.426 72.338 1.00 44.01 ? 146 ASP A OD2 1 ATOM 1146 N N . ASN A 1 147 ? 25.329 -12.631 72.289 1.00 27.31 ? 147 ASN A N 1 ATOM 1147 C CA . ASN A 1 147 ? 25.890 -11.393 72.796 1.00 26.45 ? 147 ASN A CA 1 ATOM 1148 C C . ASN A 1 147 ? 26.418 -10.517 71.666 1.00 24.25 ? 147 ASN A C 1 ATOM 1149 O O . ASN A 1 147 ? 27.606 -10.205 71.593 1.00 23.39 ? 147 ASN A O 1 ATOM 1150 C CB . ASN A 1 147 ? 26.997 -11.715 73.796 1.00 29.37 ? 147 ASN A CB 1 ATOM 1151 C CG . ASN A 1 147 ? 27.541 -10.476 74.473 1.00 35.12 ? 147 ASN A CG 1 ATOM 1152 O OD1 . ASN A 1 147 ? 26.777 -9.639 74.974 1.00 35.76 ? 147 ASN A OD1 1 ATOM 1153 N ND2 . ASN A 1 147 ? 28.872 -10.350 74.499 1.00 36.69 ? 147 ASN A ND2 1 ATOM 1154 N N . TYR A 1 148 ? 25.511 -10.108 70.791 1.00 22.33 ? 148 TYR A N 1 ATOM 1155 C CA . TYR A 1 148 ? 25.868 -9.287 69.649 1.00 21.09 ? 148 TYR A CA 1 ATOM 1156 C C . TYR A 1 148 ? 26.065 -7.821 70.025 1.00 20.48 ? 148 TYR A C 1 ATOM 1157 O O . TYR A 1 148 ? 25.521 -7.343 71.023 1.00 20.14 ? 148 TYR A O 1 ATOM 1158 C CB . TYR A 1 148 ? 24.782 -9.413 68.582 1.00 19.80 ? 148 TYR A CB 1 ATOM 1159 C CG . TYR A 1 148 ? 23.421 -8.948 69.050 1.00 20.40 ? 148 TYR A CG 1 ATOM 1160 C CD1 . TYR A 1 148 ? 23.112 -7.587 69.126 1.00 20.53 ? 148 TYR A CD1 1 ATOM 1161 C CD2 . TYR A 1 148 ? 22.442 -9.868 69.424 1.00 21.20 ? 148 TYR A CD2 1 ATOM 1162 C CE1 . TYR A 1 148 ? 21.855 -7.155 69.564 1.00 21.53 ? 148 TYR A CE1 1 ATOM 1163 C CE2 . TYR A 1 148 ? 21.181 -9.450 69.863 1.00 21.02 ? 148 TYR A CE2 1 ATOM 1164 C CZ . TYR A 1 148 ? 20.893 -8.094 69.930 1.00 22.25 ? 148 TYR A CZ 1 ATOM 1165 O OH . TYR A 1 148 ? 19.651 -7.686 70.365 1.00 22.67 ? 148 TYR A OH 1 ATOM 1166 N N . LYS A 1 149 ? 26.850 -7.118 69.210 1.00 19.72 ? 149 LYS A N 1 ATOM 1167 C CA . LYS A 1 149 ? 27.125 -5.705 69.417 1.00 18.81 ? 149 LYS A CA 1 ATOM 1168 C C . LYS A 1 149 ? 26.153 -4.866 68.593 1.00 18.53 ? 149 LYS A C 1 ATOM 1169 O O . LYS A 1 149 ? 26.279 -4.781 67.373 1.00 18.31 ? 149 LYS A O 1 ATOM 1170 C CB . LYS A 1 149 ? 28.564 -5.396 69.002 1.00 19.94 ? 149 LYS A CB 1 ATOM 1171 C CG . LYS A 1 149 ? 29.601 -6.115 69.850 1.00 23.99 ? 149 LYS A CG 1 ATOM 1172 C CD . LYS A 1 149 ? 31.024 -5.673 69.523 1.00 29.48 ? 149 LYS A CD 1 ATOM 1173 C CE . LYS A 1 149 ? 31.164 -4.142 69.538 1.00 34.02 ? 149 LYS A CE 1 ATOM 1174 N NZ . LYS A 1 149 ? 30.637 -3.485 70.779 1.00 36.59 ? 149 LYS A NZ 1 ATOM 1175 N N . PRO A 1 150 ? 25.165 -4.234 69.248 1.00 18.51 ? 150 PRO A N 1 ATOM 1176 C CA . PRO A 1 150 ? 24.182 -3.406 68.533 1.00 17.70 ? 150 PRO A CA 1 ATOM 1177 C C . PRO A 1 150 ? 24.739 -2.261 67.676 1.00 16.93 ? 150 PRO A C 1 ATOM 1178 O O . PRO A 1 150 ? 24.143 -1.906 66.660 1.00 16.21 ? 150 PRO A O 1 ATOM 1179 C CB . PRO A 1 150 ? 23.258 -2.915 69.655 1.00 18.02 ? 150 PRO A CB 1 ATOM 1180 C CG . PRO A 1 150 ? 24.132 -2.961 70.868 1.00 19.69 ? 150 PRO A CG 1 ATOM 1181 C CD . PRO A 1 150 ? 24.879 -4.252 70.691 1.00 17.62 ? 150 PRO A CD 1 ATOM 1182 N N . THR A 1 151 ? 25.869 -1.682 68.070 1.00 16.04 ? 151 THR A N 1 ATOM 1183 C CA . THR A 1 151 ? 26.445 -0.592 67.294 1.00 16.55 ? 151 THR A CA 1 ATOM 1184 C C . THR A 1 151 ? 26.956 -1.084 65.943 1.00 16.02 ? 151 THR A C 1 ATOM 1185 O O . THR A 1 151 ? 26.884 -0.367 64.950 1.00 17.59 ? 151 THR A O 1 ATOM 1186 C CB . THR A 1 151 ? 27.605 0.098 68.041 1.00 16.15 ? 151 THR A CB 1 ATOM 1187 O OG1 . THR A 1 151 ? 28.555 -0.884 68.464 1.00 21.23 ? 151 THR A OG1 1 ATOM 1188 C CG2 . THR A 1 151 ? 27.090 0.847 69.248 1.00 16.68 ? 151 THR A CG2 1 ATOM 1189 N N . GLU A 1 152 ? 27.469 -2.308 65.900 1.00 16.30 ? 152 GLU A N 1 ATOM 1190 C CA . GLU A 1 152 ? 27.979 -2.863 64.650 1.00 16.46 ? 152 GLU A CA 1 ATOM 1191 C C . GLU A 1 152 ? 26.825 -3.242 63.728 1.00 15.88 ? 152 GLU A C 1 ATOM 1192 O O . GLU A 1 152 ? 26.896 -3.048 62.512 1.00 16.15 ? 152 GLU A O 1 ATOM 1193 C CB . GLU A 1 152 ? 28.862 -4.079 64.933 1.00 18.04 ? 152 GLU A CB 1 ATOM 1194 C CG . GLU A 1 152 ? 30.136 -3.721 65.680 1.00 21.96 ? 152 GLU A CG 1 ATOM 1195 C CD . GLU A 1 152 ? 31.077 -4.895 65.853 1.00 25.41 ? 152 GLU A CD 1 ATOM 1196 O OE1 . GLU A 1 152 ? 32.259 -4.654 66.185 1.00 28.86 ? 152 GLU A OE1 1 ATOM 1197 O OE2 . GLU A 1 152 ? 30.644 -6.052 65.666 1.00 25.76 ? 152 GLU A OE2 1 ATOM 1198 N N . ILE A 1 153 ? 25.760 -3.782 64.314 1.00 15.38 ? 153 ILE A N 1 ATOM 1199 C CA . ILE A 1 153 ? 24.585 -4.159 63.538 1.00 13.85 ? 153 ILE A CA 1 ATOM 1200 C C . ILE A 1 153 ? 23.949 -2.883 62.964 1.00 13.67 ? 153 ILE A C 1 ATOM 1201 O O . ILE A 1 153 ? 23.575 -2.839 61.790 1.00 13.23 ? 153 ILE A O 1 ATOM 1202 C CB . ILE A 1 153 ? 23.560 -4.932 64.417 1.00 12.71 ? 153 ILE A CB 1 ATOM 1203 C CG1 . ILE A 1 153 ? 24.137 -6.300 64.797 1.00 11.04 ? 153 ILE A CG1 1 ATOM 1204 C CG2 . ILE A 1 153 ? 22.246 -5.106 63.669 1.00 12.33 ? 153 ILE A CG2 1 ATOM 1205 C CD1 . ILE A 1 153 ? 23.232 -7.139 65.706 1.00 10.16 ? 153 ILE A CD1 1 ATOM 1206 N N . ALA A 1 154 ? 23.855 -1.843 63.792 1.00 12.42 ? 154 ALA A N 1 ATOM 1207 C CA . ALA A 1 154 ? 23.280 -0.567 63.370 1.00 10.91 ? 154 ALA A CA 1 ATOM 1208 C C . ALA A 1 154 ? 24.058 0.078 62.213 1.00 11.01 ? 154 ALA A C 1 ATOM 1209 O O . ALA A 1 154 ? 23.462 0.481 61.217 1.00 10.81 ? 154 ALA A O 1 ATOM 1210 C CB . ALA A 1 154 ? 23.205 0.394 64.558 1.00 8.59 ? 154 ALA A CB 1 ATOM 1211 N N . SER A 1 155 ? 25.380 0.176 62.327 1.00 10.94 ? 155 SER A N 1 ATOM 1212 C CA . SER A 1 155 ? 26.153 0.792 61.252 1.00 13.40 ? 155 SER A CA 1 ATOM 1213 C C . SER A 1 155 ? 26.106 -0.053 59.983 1.00 12.97 ? 155 SER A C 1 ATOM 1214 O O . SER A 1 155 ? 26.023 0.488 58.876 1.00 12.71 ? 155 SER A O 1 ATOM 1215 C CB . SER A 1 155 ? 27.610 1.012 61.668 1.00 15.13 ? 155 SER A CB 1 ATOM 1216 O OG . SER A 1 155 ? 28.319 -0.210 61.696 1.00 24.68 ? 155 SER A OG 1 ATOM 1217 N N . SER A 1 156 ? 26.157 -1.377 60.136 1.00 11.80 ? 156 SER A N 1 ATOM 1218 C CA . SER A 1 156 ? 26.101 -2.264 58.976 1.00 11.70 ? 156 SER A CA 1 ATOM 1219 C C . SER A 1 156 ? 24.746 -2.163 58.264 1.00 11.26 ? 156 SER A C 1 ATOM 1220 O O . SER A 1 156 ? 24.683 -2.085 57.036 1.00 10.68 ? 156 SER A O 1 ATOM 1221 C CB . SER A 1 156 ? 26.367 -3.711 59.399 1.00 13.65 ? 156 SER A CB 1 ATOM 1222 O OG . SER A 1 156 ? 27.667 -3.852 59.945 1.00 14.95 ? 156 SER A OG 1 ATOM 1223 N N . LEU A 1 157 ? 23.659 -2.154 59.027 1.00 10.73 ? 157 LEU A N 1 ATOM 1224 C CA . LEU A 1 157 ? 22.343 -2.046 58.413 1.00 10.80 ? 157 LEU A CA 1 ATOM 1225 C C . LEU A 1 157 ? 22.161 -0.669 57.774 1.00 10.40 ? 157 LEU A C 1 ATOM 1226 O O . LEU A 1 157 ? 21.458 -0.536 56.776 1.00 8.82 ? 157 LEU A O 1 ATOM 1227 C CB . LEU A 1 157 ? 21.239 -2.322 59.444 1.00 12.52 ? 157 LEU A CB 1 ATOM 1228 C CG . LEU A 1 157 ? 21.176 -3.783 59.926 1.00 13.63 ? 157 LEU A CG 1 ATOM 1229 C CD1 . LEU A 1 157 ? 20.064 -3.952 60.944 1.00 12.78 ? 157 LEU A CD1 1 ATOM 1230 C CD2 . LEU A 1 157 ? 20.968 -4.710 58.729 1.00 12.34 ? 157 LEU A CD2 1 ATOM 1231 N N . LEU A 1 158 ? 22.799 0.353 58.340 1.00 11.12 ? 158 LEU A N 1 ATOM 1232 C CA . LEU A 1 158 ? 22.708 1.699 57.770 1.00 11.82 ? 158 LEU A CA 1 ATOM 1233 C C . LEU A 1 158 ? 23.332 1.703 56.374 1.00 11.96 ? 158 LEU A C 1 ATOM 1234 O O . LEU A 1 158 ? 22.835 2.371 55.468 1.00 10.44 ? 158 LEU A O 1 ATOM 1235 C CB . LEU A 1 158 ? 23.425 2.733 58.652 1.00 12.08 ? 158 LEU A CB 1 ATOM 1236 C CG . LEU A 1 158 ? 23.377 4.170 58.105 1.00 12.21 ? 158 LEU A CG 1 ATOM 1237 C CD1 . LEU A 1 158 ? 21.930 4.584 57.822 1.00 10.78 ? 158 LEU A CD1 1 ATOM 1238 C CD2 . LEU A 1 158 ? 24.010 5.118 59.102 1.00 11.00 ? 158 LEU A CD2 1 ATOM 1239 N N . VAL A 1 159 ? 24.430 0.964 56.208 1.00 12.44 ? 159 VAL A N 1 ATOM 1240 C CA . VAL A 1 159 ? 25.089 0.866 54.904 1.00 12.41 ? 159 VAL A CA 1 ATOM 1241 C C . VAL A 1 159 ? 24.152 0.102 53.948 1.00 12.81 ? 159 VAL A C 1 ATOM 1242 O O . VAL A 1 159 ? 23.886 0.548 52.835 1.00 12.07 ? 159 VAL A O 1 ATOM 1243 C CB . VAL A 1 159 ? 26.459 0.112 55.010 1.00 12.72 ? 159 VAL A CB 1 ATOM 1244 C CG1 . VAL A 1 159 ? 27.037 -0.132 53.616 1.00 11.03 ? 159 VAL A CG1 1 ATOM 1245 C CG2 . VAL A 1 159 ? 27.436 0.917 55.856 1.00 9.41 ? 159 VAL A CG2 1 ATOM 1246 N N . VAL A 1 160 ? 23.647 -1.045 54.402 1.00 11.62 ? 160 VAL A N 1 ATOM 1247 C CA . VAL A 1 160 ? 22.733 -1.866 53.611 1.00 11.16 ? 160 VAL A CA 1 ATOM 1248 C C . VAL A 1 160 ? 21.456 -1.096 53.226 1.00 11.85 ? 160 VAL A C 1 ATOM 1249 O O . VAL A 1 160 ? 21.027 -1.129 52.071 1.00 11.85 ? 160 VAL A O 1 ATOM 1250 C CB . VAL A 1 160 ? 22.335 -3.149 54.396 1.00 12.84 ? 160 VAL A CB 1 ATOM 1251 C CG1 . VAL A 1 160 ? 21.207 -3.881 53.687 1.00 11.46 ? 160 VAL A CG1 1 ATOM 1252 C CG2 . VAL A 1 160 ? 23.538 -4.063 54.530 1.00 12.25 ? 160 VAL A CG2 1 ATOM 1253 N N . ILE A 1 161 ? 20.850 -0.412 54.196 1.00 10.39 ? 161 ILE A N 1 ATOM 1254 C CA . ILE A 1 161 ? 19.633 0.361 53.950 1.00 11.48 ? 161 ILE A CA 1 ATOM 1255 C C . ILE A 1 161 ? 19.811 1.380 52.818 1.00 10.62 ? 161 ILE A C 1 ATOM 1256 O O . ILE A 1 161 ? 18.951 1.499 51.946 1.00 10.97 ? 161 ILE A O 1 ATOM 1257 C CB . ILE A 1 161 ? 19.167 1.093 55.241 1.00 10.81 ? 161 ILE A CB 1 ATOM 1258 C CG1 . ILE A 1 161 ? 18.532 0.082 56.197 1.00 11.69 ? 161 ILE A CG1 1 ATOM 1259 C CG2 . ILE A 1 161 ? 18.185 2.210 54.902 1.00 11.25 ? 161 ILE A CG2 1 ATOM 1260 C CD1 . ILE A 1 161 ? 18.258 0.631 57.589 1.00 13.01 ? 161 ILE A CD1 1 ATOM 1261 N N . GLN A 1 162 ? 20.928 2.100 52.812 1.00 9.55 ? 162 GLN A N 1 ATOM 1262 C CA . GLN A 1 162 ? 21.143 3.088 51.759 1.00 9.99 ? 162 GLN A CA 1 ATOM 1263 C C . GLN A 1 162 ? 21.619 2.506 50.431 1.00 9.26 ? 162 GLN A C 1 ATOM 1264 O O . GLN A 1 162 ? 21.177 2.958 49.374 1.00 10.92 ? 162 GLN A O 1 ATOM 1265 C CB . GLN A 1 162 ? 22.114 4.170 52.235 1.00 9.38 ? 162 GLN A CB 1 ATOM 1266 C CG . GLN A 1 162 ? 21.633 4.895 53.486 1.00 12.67 ? 162 GLN A CG 1 ATOM 1267 C CD . GLN A 1 162 ? 22.542 6.037 53.888 1.00 13.48 ? 162 GLN A CD 1 ATOM 1268 O OE1 . GLN A 1 162 ? 22.382 7.167 53.424 1.00 15.51 ? 162 GLN A OE1 1 ATOM 1269 N NE2 . GLN A 1 162 ? 23.516 5.744 54.745 1.00 12.21 ? 162 GLN A NE2 1 ATOM 1270 N N . MET A 1 163 ? 22.501 1.506 50.465 1.00 9.77 ? 163 MET A N 1 ATOM 1271 C CA . MET A 1 163 ? 23.002 0.924 49.216 1.00 10.60 ? 163 MET A CA 1 ATOM 1272 C C . MET A 1 163 ? 21.991 0.017 48.533 1.00 11.04 ? 163 MET A C 1 ATOM 1273 O O . MET A 1 163 ? 22.121 -0.272 47.342 1.00 11.35 ? 163 MET A O 1 ATOM 1274 C CB . MET A 1 163 ? 24.322 0.155 49.438 1.00 12.50 ? 163 MET A CB 1 ATOM 1275 C CG . MET A 1 163 ? 25.506 1.043 49.847 1.00 13.85 ? 163 MET A CG 1 ATOM 1276 S SD . MET A 1 163 ? 27.123 0.232 49.889 1.00 13.05 ? 163 MET A SD 1 ATOM 1277 C CE . MET A 1 163 ? 27.601 0.276 48.133 1.00 14.35 ? 163 MET A CE 1 ATOM 1278 N N . VAL A 1 164 ? 20.987 -0.437 49.277 1.00 11.96 ? 164 VAL A N 1 ATOM 1279 C CA . VAL A 1 164 ? 19.967 -1.304 48.695 1.00 11.74 ? 164 VAL A CA 1 ATOM 1280 C C . VAL A 1 164 ? 18.620 -0.586 48.595 1.00 10.75 ? 164 VAL A C 1 ATOM 1281 O O . VAL A 1 164 ? 18.177 -0.286 47.491 1.00 11.88 ? 164 VAL A O 1 ATOM 1282 C CB . VAL A 1 164 ? 19.790 -2.633 49.505 1.00 12.53 ? 164 VAL A CB 1 ATOM 1283 C CG1 . VAL A 1 164 ? 18.768 -3.534 48.818 1.00 10.05 ? 164 VAL A CG1 1 ATOM 1284 C CG2 . VAL A 1 164 ? 21.124 -3.379 49.604 1.00 9.86 ? 164 VAL A CG2 1 ATOM 1285 N N . SER A 1 165 ? 17.988 -0.286 49.733 1.00 10.16 ? 165 SER A N 1 ATOM 1286 C CA . SER A 1 165 ? 16.677 0.384 49.728 1.00 9.81 ? 165 SER A CA 1 ATOM 1287 C C . SER A 1 165 ? 16.627 1.781 49.121 1.00 10.19 ? 165 SER A C 1 ATOM 1288 O O . SER A 1 165 ? 15.819 2.031 48.236 1.00 11.21 ? 165 SER A O 1 ATOM 1289 C CB . SER A 1 165 ? 16.081 0.456 51.138 1.00 9.06 ? 165 SER A CB 1 ATOM 1290 O OG . SER A 1 165 ? 15.632 -0.814 51.568 1.00 10.55 ? 165 SER A OG 1 ATOM 1291 N N . GLU A 1 166 ? 17.464 2.696 49.607 1.00 10.16 ? 166 GLU A N 1 ATOM 1292 C CA . GLU A 1 166 ? 17.470 4.066 49.087 1.00 10.48 ? 166 GLU A CA 1 ATOM 1293 C C . GLU A 1 166 ? 17.866 4.098 47.609 1.00 11.16 ? 166 GLU A C 1 ATOM 1294 O O . GLU A 1 166 ? 17.232 4.788 46.805 1.00 10.15 ? 166 GLU A O 1 ATOM 1295 C CB . GLU A 1 166 ? 18.416 4.953 49.915 1.00 11.42 ? 166 GLU A CB 1 ATOM 1296 C CG . GLU A 1 166 ? 18.023 5.077 51.390 1.00 10.12 ? 166 GLU A CG 1 ATOM 1297 C CD . GLU A 1 166 ? 16.710 5.828 51.607 1.00 11.29 ? 166 GLU A CD 1 ATOM 1298 O OE1 . GLU A 1 166 ? 15.926 5.984 50.649 1.00 9.76 ? 166 GLU A OE1 1 ATOM 1299 O OE2 . GLU A 1 166 ? 16.457 6.256 52.750 1.00 10.65 ? 166 GLU A OE2 1 ATOM 1300 N N . ALA A 1 167 ? 18.910 3.351 47.252 1.00 11.63 ? 167 ALA A N 1 ATOM 1301 C CA . ALA A 1 167 ? 19.351 3.289 45.861 1.00 11.80 ? 167 ALA A CA 1 ATOM 1302 C C . ALA A 1 167 ? 18.251 2.695 44.965 1.00 11.02 ? 167 ALA A C 1 ATOM 1303 O O . ALA A 1 167 ? 18.103 3.096 43.815 1.00 10.77 ? 167 ALA A O 1 ATOM 1304 C CB . ALA A 1 167 ? 20.638 2.463 45.746 1.00 11.48 ? 167 ALA A CB 1 ATOM 1305 N N . ALA A 1 168 ? 17.481 1.743 45.485 1.00 10.12 ? 168 ALA A N 1 ATOM 1306 C CA . ALA A 1 168 ? 16.404 1.146 44.697 1.00 9.89 ? 168 ALA A CA 1 ATOM 1307 C C . ALA A 1 168 ? 15.297 2.188 44.450 1.00 10.01 ? 168 ALA A C 1 ATOM 1308 O O . ALA A 1 168 ? 14.712 2.240 43.370 1.00 10.83 ? 168 ALA A O 1 ATOM 1309 C CB . ALA A 1 168 ? 15.832 -0.081 45.424 1.00 9.00 ? 168 ALA A CB 1 ATOM 1310 N N . ARG A 1 169 ? 15.029 3.019 45.454 1.00 10.71 ? 169 ARG A N 1 ATOM 1311 C CA . ARG A 1 169 ? 14.007 4.067 45.367 1.00 10.64 ? 169 ARG A CA 1 ATOM 1312 C C . ARG A 1 169 ? 14.406 5.251 44.470 1.00 11.44 ? 169 ARG A C 1 ATOM 1313 O O . ARG A 1 169 ? 13.576 5.783 43.733 1.00 10.27 ? 169 ARG A O 1 ATOM 1314 C CB . ARG A 1 169 ? 13.719 4.644 46.762 1.00 10.99 ? 169 ARG A CB 1 ATOM 1315 C CG . ARG A 1 169 ? 12.951 3.755 47.737 1.00 11.08 ? 169 ARG A CG 1 ATOM 1316 C CD . ARG A 1 169 ? 13.175 4.298 49.145 1.00 10.59 ? 169 ARG A CD 1 ATOM 1317 N NE . ARG A 1 169 ? 12.451 3.576 50.188 1.00 11.72 ? 169 ARG A NE 1 ATOM 1318 C CZ . ARG A 1 169 ? 12.905 3.425 51.430 1.00 13.96 ? 169 ARG A CZ 1 ATOM 1319 N NH1 . ARG A 1 169 ? 14.081 3.936 51.777 1.00 12.84 ? 169 ARG A NH1 1 ATOM 1320 N NH2 . ARG A 1 169 ? 12.186 2.770 52.332 1.00 11.50 ? 169 ARG A NH2 1 ATOM 1321 N N . PHE A 1 170 ? 15.671 5.668 44.567 1.00 11.01 ? 170 PHE A N 1 ATOM 1322 C CA . PHE A 1 170 ? 16.191 6.826 43.839 1.00 10.06 ? 170 PHE A CA 1 ATOM 1323 C C . PHE A 1 170 ? 17.331 6.541 42.869 1.00 10.82 ? 170 PHE A C 1 ATOM 1324 O O . PHE A 1 170 ? 18.382 6.029 43.256 1.00 8.86 ? 170 PHE A O 1 ATOM 1325 C CB . PHE A 1 170 ? 16.702 7.881 44.835 1.00 12.60 ? 170 PHE A CB 1 ATOM 1326 C CG . PHE A 1 170 ? 15.630 8.505 45.694 1.00 11.65 ? 170 PHE A CG 1 ATOM 1327 C CD1 . PHE A 1 170 ? 14.853 9.555 45.210 1.00 12.15 ? 170 PHE A CD1 1 ATOM 1328 C CD2 . PHE A 1 170 ? 15.414 8.058 46.988 1.00 10.57 ? 170 PHE A CD2 1 ATOM 1329 C CE1 . PHE A 1 170 ? 13.878 10.153 46.005 1.00 12.51 ? 170 PHE A CE1 1 ATOM 1330 C CE2 . PHE A 1 170 ? 14.440 8.648 47.795 1.00 10.42 ? 170 PHE A CE2 1 ATOM 1331 C CZ . PHE A 1 170 ? 13.671 9.698 47.302 1.00 11.09 ? 170 PHE A CZ 1 ATOM 1332 N N . THR A 1 171 ? 17.135 6.907 41.609 1.00 10.68 ? 171 THR A N 1 ATOM 1333 C CA . THR A 1 171 ? 18.176 6.724 40.612 1.00 12.37 ? 171 THR A CA 1 ATOM 1334 C C . THR A 1 171 ? 19.354 7.646 40.982 1.00 12.13 ? 171 THR A C 1 ATOM 1335 O O . THR A 1 171 ? 20.511 7.329 40.711 1.00 12.89 ? 171 THR A O 1 ATOM 1336 C CB . THR A 1 171 ? 17.658 7.089 39.193 1.00 14.18 ? 171 THR A CB 1 ATOM 1337 O OG1 . THR A 1 171 ? 17.128 8.423 39.210 1.00 14.02 ? 171 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 171 ? 16.557 6.106 38.737 1.00 13.99 ? 171 THR A CG2 1 ATOM 1339 N N . PHE A 1 172 ? 19.048 8.783 41.609 1.00 12.36 ? 172 PHE A N 1 ATOM 1340 C CA . PHE A 1 172 ? 20.071 9.748 42.025 1.00 11.77 ? 172 PHE A CA 1 ATOM 1341 C C . PHE A 1 172 ? 21.079 9.113 42.984 1.00 11.35 ? 172 PHE A C 1 ATOM 1342 O O . PHE A 1 172 ? 22.290 9.264 42.817 1.00 11.72 ? 172 PHE A O 1 ATOM 1343 C CB . PHE A 1 172 ? 19.414 10.958 42.708 1.00 12.11 ? 172 PHE A CB 1 ATOM 1344 C CG . PHE A 1 172 ? 20.395 12.026 43.140 1.00 14.62 ? 172 PHE A CG 1 ATOM 1345 C CD1 . PHE A 1 172 ? 20.841 12.987 42.242 1.00 14.94 ? 172 PHE A CD1 1 ATOM 1346 C CD2 . PHE A 1 172 ? 20.882 12.059 44.447 1.00 14.92 ? 172 PHE A CD2 1 ATOM 1347 C CE1 . PHE A 1 172 ? 21.757 13.963 42.638 1.00 16.39 ? 172 PHE A CE1 1 ATOM 1348 C CE2 . PHE A 1 172 ? 21.796 13.030 44.851 1.00 15.19 ? 172 PHE A CE2 1 ATOM 1349 C CZ . PHE A 1 172 ? 22.234 13.983 43.942 1.00 14.96 ? 172 PHE A CZ 1 ATOM 1350 N N . ILE A 1 173 ? 20.572 8.408 43.990 1.00 11.74 ? 173 ILE A N 1 ATOM 1351 C CA . ILE A 1 173 ? 21.421 7.748 44.981 1.00 12.28 ? 173 ILE A CA 1 ATOM 1352 C C . ILE A 1 173 ? 22.166 6.564 44.346 1.00 13.61 ? 173 ILE A C 1 ATOM 1353 O O . ILE A 1 173 ? 23.348 6.326 44.628 1.00 11.65 ? 173 ILE A O 1 ATOM 1354 C CB . ILE A 1 173 ? 20.563 7.293 46.187 1.00 12.29 ? 173 ILE A CB 1 ATOM 1355 C CG1 . ILE A 1 173 ? 20.019 8.534 46.907 1.00 12.59 ? 173 ILE A CG1 1 ATOM 1356 C CG2 . ILE A 1 173 ? 21.383 6.436 47.136 1.00 12.43 ? 173 ILE A CG2 1 ATOM 1357 C CD1 . ILE A 1 173 ? 19.087 8.242 48.076 1.00 13.04 ? 173 ILE A CD1 1 ATOM 1358 N N . GLU A 1 174 ? 21.463 5.836 43.481 1.00 13.06 ? 174 GLU A N 1 ATOM 1359 C CA . GLU A 1 174 ? 22.031 4.704 42.748 1.00 13.79 ? 174 GLU A CA 1 ATOM 1360 C C . GLU A 1 174 ? 23.316 5.120 42.031 1.00 15.08 ? 174 GLU A C 1 ATOM 1361 O O . GLU A 1 174 ? 24.320 4.394 42.044 1.00 14.64 ? 174 GLU A O 1 ATOM 1362 C CB . GLU A 1 174 ? 21.037 4.219 41.687 1.00 14.63 ? 174 GLU A CB 1 ATOM 1363 C CG . GLU A 1 174 ? 21.645 3.282 40.645 1.00 15.19 ? 174 GLU A CG 1 ATOM 1364 C CD . GLU A 1 174 ? 20.752 3.078 39.428 1.00 17.29 ? 174 GLU A CD 1 ATOM 1365 O OE1 . GLU A 1 174 ? 19.595 3.556 39.426 1.00 17.08 ? 174 GLU A OE1 1 ATOM 1366 O OE2 . GLU A 1 174 ? 21.210 2.433 38.466 1.00 18.84 ? 174 GLU A OE2 1 ATOM 1367 N N . ASN A 1 175 ? 23.274 6.287 41.389 1.00 14.46 ? 175 ASN A N 1 ATOM 1368 C CA . ASN A 1 175 ? 24.427 6.778 40.650 1.00 15.40 ? 175 ASN A CA 1 ATOM 1369 C C . ASN A 1 175 ? 25.507 7.443 41.492 1.00 15.38 ? 175 ASN A C 1 ATOM 1370 O O . ASN A 1 175 ? 26.664 7.523 41.071 1.00 15.54 ? 175 ASN A O 1 ATOM 1371 C CB . ASN A 1 175 ? 23.951 7.694 39.537 1.00 15.72 ? 175 ASN A CB 1 ATOM 1372 C CG . ASN A 1 175 ? 23.151 6.942 38.508 1.00 17.27 ? 175 ASN A CG 1 ATOM 1373 O OD1 . ASN A 1 175 ? 23.562 5.870 38.065 1.00 16.83 ? 175 ASN A OD1 1 ATOM 1374 N ND2 . ASN A 1 175 ? 22.000 7.485 38.125 1.00 17.01 ? 175 ASN A ND2 1 ATOM 1375 N N . GLN A 1 176 ? 25.139 7.921 42.677 1.00 16.69 ? 176 GLN A N 1 ATOM 1376 C CA . GLN A 1 176 ? 26.127 8.511 43.578 1.00 19.24 ? 176 GLN A CA 1 ATOM 1377 C C . GLN A 1 176 ? 27.035 7.332 43.940 1.00 18.42 ? 176 GLN A C 1 ATOM 1378 O O . GLN A 1 176 ? 28.252 7.469 44.054 1.00 20.88 ? 176 GLN A O 1 ATOM 1379 C CB . GLN A 1 176 ? 25.458 9.054 44.850 1.00 22.43 ? 176 GLN A CB 1 ATOM 1380 C CG . GLN A 1 176 ? 24.536 10.249 44.635 1.00 27.14 ? 176 GLN A CG 1 ATOM 1381 C CD . GLN A 1 176 ? 25.287 11.562 44.570 1.00 30.14 ? 176 GLN A CD 1 ATOM 1382 O OE1 . GLN A 1 176 ? 26.318 11.664 43.910 1.00 32.87 ? 176 GLN A OE1 1 ATOM 1383 N NE2 . GLN A 1 176 ? 24.769 12.580 45.253 1.00 32.90 ? 176 GLN A NE2 1 ATOM 1384 N N . ILE A 1 177 ? 26.420 6.165 44.095 1.00 16.07 ? 177 ILE A N 1 ATOM 1385 C CA . ILE A 1 177 ? 27.144 4.950 44.435 1.00 15.63 ? 177 ILE A CA 1 ATOM 1386 C C . ILE A 1 177 ? 27.857 4.332 43.231 1.00 16.39 ? 177 ILE A C 1 ATOM 1387 O O . ILE A 1 177 ? 29.031 3.965 43.326 1.00 16.88 ? 177 ILE A O 1 ATOM 1388 C CB . ILE A 1 177 ? 26.187 3.927 45.073 1.00 16.25 ? 177 ILE A CB 1 ATOM 1389 C CG1 . ILE A 1 177 ? 25.703 4.476 46.417 1.00 16.47 ? 177 ILE A CG1 1 ATOM 1390 C CG2 . ILE A 1 177 ? 26.883 2.592 45.274 1.00 15.19 ? 177 ILE A CG2 1 ATOM 1391 C CD1 . ILE A 1 177 ? 24.670 3.626 47.081 1.00 20.25 ? 177 ILE A CD1 1 ATOM 1392 N N . ARG A 1 178 ? 27.155 4.236 42.103 1.00 14.82 ? 178 ARG A N 1 ATOM 1393 C CA . ARG A 1 178 ? 27.716 3.667 40.879 1.00 14.27 ? 178 ARG A CA 1 ATOM 1394 C C . ARG A 1 178 ? 29.044 4.302 40.449 1.00 14.32 ? 178 ARG A C 1 ATOM 1395 O O . ARG A 1 178 ? 29.999 3.592 40.113 1.00 13.06 ? 178 ARG A O 1 ATOM 1396 C CB . ARG A 1 178 ? 26.702 3.792 39.732 1.00 16.66 ? 178 ARG A CB 1 ATOM 1397 C CG . ARG A 1 178 ? 27.291 3.515 38.338 1.00 19.19 ? 178 ARG A CG 1 ATOM 1398 C CD . ARG A 1 178 ? 26.242 3.630 37.237 1.00 21.69 ? 178 ARG A CD 1 ATOM 1399 N NE . ARG A 1 178 ? 26.805 3.435 35.901 1.00 22.27 ? 178 ARG A NE 1 ATOM 1400 C CZ . ARG A 1 178 ? 26.176 2.819 34.898 1.00 27.08 ? 178 ARG A CZ 1 ATOM 1401 N NH1 . ARG A 1 178 ? 24.947 2.322 35.063 1.00 25.05 ? 178 ARG A NH1 1 ATOM 1402 N NH2 . ARG A 1 178 ? 26.774 2.699 33.719 1.00 26.78 ? 178 ARG A NH2 1 ATOM 1403 N N . ASN A 1 179 ? 29.103 5.635 40.458 1.00 12.76 ? 179 ASN A N 1 ATOM 1404 C CA . ASN A 1 179 ? 30.311 6.339 40.042 1.00 13.09 ? 179 ASN A CA 1 ATOM 1405 C C . ASN A 1 179 ? 31.301 6.620 41.171 1.00 13.79 ? 179 ASN A C 1 ATOM 1406 O O . ASN A 1 179 ? 32.205 7.443 41.025 1.00 15.02 ? 179 ASN A O 1 ATOM 1407 C CB . ASN A 1 179 ? 29.943 7.647 39.328 1.00 12.68 ? 179 ASN A CB 1 ATOM 1408 C CG . ASN A 1 179 ? 29.311 7.409 37.961 1.00 13.95 ? 179 ASN A CG 1 ATOM 1409 O OD1 . ASN A 1 179 ? 29.607 6.417 37.298 1.00 13.67 ? 179 ASN A OD1 1 ATOM 1410 N ND2 . ASN A 1 179 ? 28.454 8.334 37.526 1.00 12.29 ? 179 ASN A ND2 1 ATOM 1411 N N . ASN A 1 180 ? 31.116 5.936 42.296 1.00 14.49 ? 180 ASN A N 1 ATOM 1412 C CA . ASN A 1 180 ? 31.995 6.047 43.466 1.00 14.54 ? 180 ASN A CA 1 ATOM 1413 C C . ASN A 1 180 ? 32.104 4.641 44.041 1.00 15.74 ? 180 ASN A C 1 ATOM 1414 O O . ASN A 1 180 ? 32.536 4.446 45.176 1.00 15.17 ? 180 ASN A O 1 ATOM 1415 C CB . ASN A 1 180 ? 31.378 6.954 44.534 1.00 14.56 ? 180 ASN A CB 1 ATOM 1416 C CG . ASN A 1 180 ? 31.497 8.421 44.202 1.00 13.60 ? 180 ASN A CG 1 ATOM 1417 O OD1 . ASN A 1 180 ? 32.596 8.946 44.047 1.00 13.26 ? 180 ASN A OD1 1 ATOM 1418 N ND2 . ASN A 1 180 ? 30.362 9.096 44.099 1.00 13.13 ? 180 ASN A ND2 1 ATOM 1419 N N . PHE A 1 181 ? 31.704 3.666 43.233 1.00 17.03 ? 181 PHE A N 1 ATOM 1420 C CA . PHE A 1 181 ? 31.673 2.270 43.636 1.00 18.83 ? 181 PHE A CA 1 ATOM 1421 C C . PHE A 1 181 ? 32.906 1.716 44.347 1.00 19.56 ? 181 PHE A C 1 ATOM 1422 O O . PHE A 1 181 ? 32.797 1.101 45.414 1.00 19.97 ? 181 PHE A O 1 ATOM 1423 C CB . PHE A 1 181 ? 31.346 1.395 42.425 1.00 17.70 ? 181 PHE A CB 1 ATOM 1424 C CG . PHE A 1 181 ? 30.914 0.013 42.792 1.00 18.88 ? 181 PHE A CG 1 ATOM 1425 C CD1 . PHE A 1 181 ? 29.737 -0.189 43.503 1.00 18.38 ? 181 PHE A CD1 1 ATOM 1426 C CD2 . PHE A 1 181 ? 31.690 -1.088 42.451 1.00 18.52 ? 181 PHE A CD2 1 ATOM 1427 C CE1 . PHE A 1 181 ? 29.338 -1.471 43.870 1.00 19.60 ? 181 PHE A CE1 1 ATOM 1428 C CE2 . PHE A 1 181 ? 31.301 -2.370 42.813 1.00 18.78 ? 181 PHE A CE2 1 ATOM 1429 C CZ . PHE A 1 181 ? 30.122 -2.563 43.524 1.00 18.58 ? 181 PHE A CZ 1 ATOM 1430 N N . GLN A 1 182 ? 34.075 1.923 43.758 1.00 18.86 ? 182 GLN A N 1 ATOM 1431 C CA . GLN A 1 182 ? 35.299 1.418 44.351 1.00 19.96 ? 182 GLN A CA 1 ATOM 1432 C C . GLN A 1 182 ? 35.913 2.400 45.349 1.00 21.35 ? 182 GLN A C 1 ATOM 1433 O O . GLN A 1 182 ? 37.088 2.302 45.674 1.00 22.88 ? 182 GLN A O 1 ATOM 1434 C CB . GLN A 1 182 ? 36.305 1.080 43.249 1.00 20.18 ? 182 GLN A CB 1 ATOM 1435 C CG . GLN A 1 182 ? 35.848 -0.014 42.279 1.00 22.03 ? 182 GLN A CG 1 ATOM 1436 C CD . GLN A 1 182 ? 35.681 -1.369 42.951 1.00 25.63 ? 182 GLN A CD 1 ATOM 1437 O OE1 . GLN A 1 182 ? 36.247 -1.614 44.020 1.00 27.30 ? 182 GLN A OE1 1 ATOM 1438 N NE2 . GLN A 1 182 ? 34.917 -2.263 42.319 1.00 25.57 ? 182 GLN A NE2 1 ATOM 1439 N N . GLN A 1 183 ? 35.118 3.346 45.836 1.00 21.35 ? 183 GLN A N 1 ATOM 1440 C CA . GLN A 1 183 ? 35.603 4.320 46.808 1.00 21.47 ? 183 GLN A CA 1 ATOM 1441 C C . GLN A 1 183 ? 34.706 4.338 48.044 1.00 20.42 ? 183 GLN A C 1 ATOM 1442 O O . GLN A 1 183 ? 33.729 3.604 48.131 1.00 21.88 ? 183 GLN A O 1 ATOM 1443 C CB . GLN A 1 183 ? 35.617 5.720 46.201 1.00 24.17 ? 183 GLN A CB 1 ATOM 1444 C CG . GLN A 1 183 ? 36.393 5.851 44.918 1.00 28.80 ? 183 GLN A CG 1 ATOM 1445 C CD . GLN A 1 183 ? 35.990 7.094 44.147 1.00 34.15 ? 183 GLN A CD 1 ATOM 1446 O OE1 . GLN A 1 183 ? 36.156 8.220 44.629 1.00 35.65 ? 183 GLN A OE1 1 ATOM 1447 N NE2 . GLN A 1 183 ? 35.442 6.898 42.944 1.00 34.86 ? 183 GLN A NE2 1 ATOM 1448 N N . ARG A 1 184 ? 35.061 5.178 49.005 1.00 19.70 ? 184 ARG A N 1 ATOM 1449 C CA . ARG A 1 184 ? 34.290 5.336 50.227 1.00 20.31 ? 184 ARG A CA 1 ATOM 1450 C C . ARG A 1 184 ? 33.783 6.769 50.211 1.00 21.00 ? 184 ARG A C 1 ATOM 1451 O O . ARG A 1 184 ? 34.570 7.716 50.141 1.00 22.09 ? 184 ARG A O 1 ATOM 1452 C CB . ARG A 1 184 ? 35.171 5.103 51.452 1.00 20.70 ? 184 ARG A CB 1 ATOM 1453 C CG . ARG A 1 184 ? 35.489 3.643 51.721 1.00 21.90 ? 184 ARG A CG 1 ATOM 1454 C CD . ARG A 1 184 ? 36.626 3.511 52.713 1.00 24.59 ? 184 ARG A CD 1 ATOM 1455 N NE . ARG A 1 184 ? 36.695 2.172 53.287 1.00 29.23 ? 184 ARG A NE 1 ATOM 1456 C CZ . ARG A 1 184 ? 35.934 1.749 54.296 1.00 32.89 ? 184 ARG A CZ 1 ATOM 1457 N NH1 . ARG A 1 184 ? 35.042 2.560 54.857 1.00 32.81 ? 184 ARG A NH1 1 ATOM 1458 N NH2 . ARG A 1 184 ? 36.055 0.504 54.742 1.00 34.32 ? 184 ARG A NH2 1 ATOM 1459 N N . ILE A 1 185 ? 32.469 6.929 50.259 1.00 20.03 ? 185 ILE A N 1 ATOM 1460 C CA . ILE A 1 185 ? 31.872 8.257 50.234 1.00 19.87 ? 185 ILE A CA 1 ATOM 1461 C C . ILE A 1 185 ? 30.776 8.345 51.274 1.00 18.44 ? 185 ILE A C 1 ATOM 1462 O O . ILE A 1 185 ? 30.148 7.346 51.616 1.00 20.92 ? 185 ILE A O 1 ATOM 1463 C CB . ILE A 1 185 ? 31.226 8.564 48.863 1.00 21.10 ? 185 ILE A CB 1 ATOM 1464 C CG1 . ILE A 1 185 ? 30.074 7.578 48.613 1.00 22.19 ? 185 ILE A CG1 1 ATOM 1465 C CG2 . ILE A 1 185 ? 32.273 8.477 47.757 1.00 20.91 ? 185 ILE A CG2 1 ATOM 1466 C CD1 . ILE A 1 185 ? 29.179 7.922 47.436 1.00 22.32 ? 185 ILE A CD1 1 ATOM 1467 N N . ARG A 1 186 ? 30.543 9.546 51.772 1.00 17.69 ? 186 ARG A N 1 ATOM 1468 C CA . ARG A 1 186 ? 29.492 9.758 52.746 1.00 18.36 ? 186 ARG A CA 1 ATOM 1469 C C . ARG A 1 186 ? 28.439 10.628 52.087 1.00 19.91 ? 186 ARG A C 1 ATOM 1470 O O . ARG A 1 186 ? 28.769 11.582 51.379 1.00 20.27 ? 186 ARG A O 1 ATOM 1471 C CB . ARG A 1 186 ? 30.059 10.442 53.981 1.00 17.91 ? 186 ARG A CB 1 ATOM 1472 C CG . ARG A 1 186 ? 30.986 9.531 54.736 1.00 20.31 ? 186 ARG A CG 1 ATOM 1473 C CD . ARG A 1 186 ? 31.715 10.247 55.836 1.00 21.58 ? 186 ARG A CD 1 ATOM 1474 N NE . ARG A 1 186 ? 32.526 9.305 56.592 1.00 22.98 ? 186 ARG A NE 1 ATOM 1475 C CZ . ARG A 1 186 ? 33.195 9.609 57.695 1.00 24.62 ? 186 ARG A CZ 1 ATOM 1476 N NH1 . ARG A 1 186 ? 33.157 10.843 58.174 1.00 23.13 ? 186 ARG A NH1 1 ATOM 1477 N NH2 . ARG A 1 186 ? 33.881 8.667 58.330 1.00 25.95 ? 186 ARG A NH2 1 ATOM 1478 N N . PRO A 1 187 ? 27.154 10.305 52.294 1.00 19.89 ? 187 PRO A N 1 ATOM 1479 C CA . PRO A 1 187 ? 26.099 11.113 51.676 1.00 19.30 ? 187 PRO A CA 1 ATOM 1480 C C . PRO A 1 187 ? 26.182 12.570 52.102 1.00 18.86 ? 187 PRO A C 1 ATOM 1481 O O . PRO A 1 187 ? 26.568 12.868 53.231 1.00 18.26 ? 187 PRO A O 1 ATOM 1482 C CB . PRO A 1 187 ? 24.817 10.434 52.151 1.00 18.85 ? 187 PRO A CB 1 ATOM 1483 C CG . PRO A 1 187 ? 25.202 9.863 53.476 1.00 20.60 ? 187 PRO A CG 1 ATOM 1484 C CD . PRO A 1 187 ? 26.579 9.279 53.179 1.00 20.69 ? 187 PRO A CD 1 ATOM 1485 N N . ALA A 1 188 ? 25.837 13.469 51.181 1.00 18.50 ? 188 ALA A N 1 ATOM 1486 C CA . ALA A 1 188 ? 25.849 14.904 51.445 1.00 17.63 ? 188 ALA A CA 1 ATOM 1487 C C . ALA A 1 188 ? 24.421 15.344 51.733 1.00 18.39 ? 188 ALA A C 1 ATOM 1488 O O . ALA A 1 188 ? 23.522 14.507 51.844 1.00 17.29 ? 188 ALA A O 1 ATOM 1489 C CB . ALA A 1 188 ? 26.402 15.652 50.240 1.00 18.31 ? 188 ALA A CB 1 ATOM 1490 N N . ASN A 1 189 ? 24.209 16.651 51.852 1.00 19.74 ? 189 ASN A N 1 ATOM 1491 C CA . ASN A 1 189 ? 22.875 17.195 52.127 1.00 20.96 ? 189 ASN A CA 1 ATOM 1492 C C . ASN A 1 189 ? 21.856 16.872 51.025 1.00 18.80 ? 189 ASN A C 1 ATOM 1493 O O . ASN A 1 189 ? 20.657 16.757 51.285 1.00 16.91 ? 189 ASN A O 1 ATOM 1494 C CB . ASN A 1 189 ? 22.964 18.715 52.327 1.00 25.25 ? 189 ASN A CB 1 ATOM 1495 C CG . ASN A 1 189 ? 23.819 19.095 53.529 1.00 32.05 ? 189 ASN A CG 1 ATOM 1496 O OD1 . ASN A 1 189 ? 23.419 18.875 54.673 1.00 29.93 ? 189 ASN A OD1 1 ATOM 1497 N ND2 . ASN A 1 189 ? 25.000 19.654 53.262 1.00 40.58 ? 189 ASN A ND2 1 ATOM 1498 N N . ASN A 1 190 ? 22.326 16.733 49.791 1.00 18.34 ? 190 ASN A N 1 ATOM 1499 C CA . ASN A 1 190 ? 21.418 16.424 48.700 1.00 18.73 ? 190 ASN A CA 1 ATOM 1500 C C . ASN A 1 190 ? 20.850 15.007 48.840 1.00 18.55 ? 190 ASN A C 1 ATOM 1501 O O . ASN A 1 190 ? 19.634 14.811 48.815 1.00 17.19 ? 190 ASN A O 1 ATOM 1502 C CB . ASN A 1 190 ? 22.103 16.631 47.331 1.00 19.37 ? 190 ASN A CB 1 ATOM 1503 C CG . ASN A 1 190 ? 23.538 16.103 47.273 1.00 22.03 ? 190 ASN A CG 1 ATOM 1504 O OD1 . ASN A 1 190 ? 24.231 16.304 46.273 1.00 23.96 ? 190 ASN A OD1 1 ATOM 1505 N ND2 . ASN A 1 190 ? 23.986 15.431 48.327 1.00 21.00 ? 190 ASN A ND2 1 ATOM 1506 N N . THR A 1 191 ? 21.729 14.028 49.021 1.00 17.46 ? 191 THR A N 1 ATOM 1507 C CA . THR A 1 191 ? 21.305 12.641 49.178 1.00 15.96 ? 191 THR A CA 1 ATOM 1508 C C . THR A 1 191 ? 20.407 12.466 50.399 1.00 14.92 ? 191 THR A C 1 ATOM 1509 O O . THR A 1 191 ? 19.365 11.815 50.332 1.00 14.64 ? 191 THR A O 1 ATOM 1510 C CB . THR A 1 191 ? 22.532 11.724 49.313 1.00 17.53 ? 191 THR A CB 1 ATOM 1511 O OG1 . THR A 1 191 ? 23.283 11.770 48.094 1.00 18.50 ? 191 THR A OG1 1 ATOM 1512 C CG2 . THR A 1 191 ? 22.111 10.282 49.606 1.00 15.91 ? 191 THR A CG2 1 ATOM 1513 N N . ILE A 1 192 ? 20.806 13.061 51.516 1.00 14.24 ? 192 ILE A N 1 ATOM 1514 C CA . ILE A 1 192 ? 20.034 12.948 52.748 1.00 13.77 ? 192 ILE A CA 1 ATOM 1515 C C . ILE A 1 192 ? 18.626 13.563 52.671 1.00 13.53 ? 192 ILE A C 1 ATOM 1516 O O . ILE A 1 192 ? 17.674 12.981 53.194 1.00 12.05 ? 192 ILE A O 1 ATOM 1517 C CB . ILE A 1 192 ? 20.840 13.540 53.939 1.00 12.70 ? 192 ILE A CB 1 ATOM 1518 C CG1 . ILE A 1 192 ? 22.065 12.646 54.206 1.00 12.73 ? 192 ILE A CG1 1 ATOM 1519 C CG2 . ILE A 1 192 ? 19.958 13.678 55.161 1.00 10.86 ? 192 ILE A CG2 1 ATOM 1520 C CD1 . ILE A 1 192 ? 22.988 13.115 55.338 1.00 14.66 ? 192 ILE A CD1 1 ATOM 1521 N N . SER A 1 193 ? 18.478 14.717 52.017 1.00 13.35 ? 193 SER A N 1 ATOM 1522 C CA . SER A 1 193 ? 17.149 15.330 51.912 1.00 14.69 ? 193 SER A CA 1 ATOM 1523 C C . SER A 1 193 ? 16.231 14.503 51.014 1.00 13.50 ? 193 SER A C 1 ATOM 1524 O O . SER A 1 193 ? 15.026 14.433 51.250 1.00 13.47 ? 193 SER A O 1 ATOM 1525 C CB . SER A 1 193 ? 17.225 16.781 51.392 1.00 16.02 ? 193 SER A CB 1 ATOM 1526 O OG . SER A 1 193 ? 17.657 16.853 50.045 1.00 17.27 ? 193 SER A OG 1 ATOM 1527 N N . LEU A 1 194 ? 16.791 13.879 49.984 1.00 12.20 ? 194 LEU A N 1 ATOM 1528 C CA . LEU A 1 194 ? 15.979 13.046 49.110 1.00 13.09 ? 194 LEU A CA 1 ATOM 1529 C C . LEU A 1 194 ? 15.440 11.883 49.930 1.00 12.74 ? 194 LEU A C 1 ATOM 1530 O O . LEU A 1 194 ? 14.239 11.614 49.934 1.00 12.15 ? 194 LEU A O 1 ATOM 1531 C CB . LEU A 1 194 ? 16.806 12.491 47.947 1.00 14.47 ? 194 LEU A CB 1 ATOM 1532 C CG . LEU A 1 194 ? 16.787 13.265 46.632 1.00 17.35 ? 194 LEU A CG 1 ATOM 1533 C CD1 . LEU A 1 194 ? 17.664 12.540 45.630 1.00 18.23 ? 194 LEU A CD1 1 ATOM 1534 C CD2 . LEU A 1 194 ? 15.364 13.380 46.112 1.00 14.32 ? 194 LEU A CD2 1 ATOM 1535 N N . GLU A 1 195 ? 16.344 11.193 50.617 1.00 11.42 ? 195 GLU A N 1 ATOM 1536 C CA . GLU A 1 195 ? 15.968 10.062 51.448 1.00 11.78 ? 195 GLU A CA 1 ATOM 1537 C C . GLU A 1 195 ? 14.841 10.473 52.390 1.00 13.63 ? 195 GLU A C 1 ATOM 1538 O O . GLU A 1 195 ? 13.861 9.744 52.551 1.00 14.70 ? 195 GLU A O 1 ATOM 1539 C CB . GLU A 1 195 ? 17.172 9.577 52.273 1.00 11.48 ? 195 GLU A CB 1 ATOM 1540 C CG . GLU A 1 195 ? 18.371 9.104 51.441 1.00 11.73 ? 195 GLU A CG 1 ATOM 1541 C CD . GLU A 1 195 ? 19.549 8.652 52.288 1.00 13.44 ? 195 GLU A CD 1 ATOM 1542 O OE1 . GLU A 1 195 ? 19.748 9.202 53.394 1.00 13.78 ? 195 GLU A OE1 1 ATOM 1543 O OE2 . GLU A 1 195 ? 20.297 7.756 51.838 1.00 12.89 ? 195 GLU A OE2 1 ATOM 1544 N N . ASN A 1 196 ? 14.979 11.647 53.002 1.00 12.62 ? 196 ASN A N 1 ATOM 1545 C CA . ASN A 1 196 ? 13.981 12.127 53.950 1.00 14.31 ? 196 ASN A CA 1 ATOM 1546 C C . ASN A 1 196 ? 12.631 12.469 53.328 1.00 14.83 ? 196 ASN A C 1 ATOM 1547 O O . ASN A 1 196 ? 11.590 12.296 53.960 1.00 15.12 ? 196 ASN A O 1 ATOM 1548 C CB . ASN A 1 196 ? 14.484 13.382 54.690 1.00 14.56 ? 196 ASN A CB 1 ATOM 1549 C CG . ASN A 1 196 ? 15.688 13.110 55.595 1.00 15.38 ? 196 ASN A CG 1 ATOM 1550 O OD1 . ASN A 1 196 ? 15.920 11.984 56.025 1.00 13.03 ? 196 ASN A OD1 1 ATOM 1551 N ND2 . ASN A 1 196 ? 16.442 14.161 55.904 1.00 15.00 ? 196 ASN A ND2 1 ATOM 1552 N N . LYS A 1 197 ? 12.652 12.941 52.088 1.00 14.08 ? 197 LYS A N 1 ATOM 1553 C CA . LYS A 1 197 ? 11.437 13.391 51.422 1.00 15.04 ? 197 LYS A CA 1 ATOM 1554 C C . LYS A 1 197 ? 10.742 12.447 50.447 1.00 14.84 ? 197 LYS A C 1 ATOM 1555 O O . LYS A 1 197 ? 9.861 12.875 49.706 1.00 14.93 ? 197 LYS A O 1 ATOM 1556 C CB . LYS A 1 197 ? 11.736 14.718 50.711 1.00 15.68 ? 197 LYS A CB 1 ATOM 1557 C CG . LYS A 1 197 ? 12.034 15.892 51.653 1.00 16.06 ? 197 LYS A CG 1 ATOM 1558 C CD . LYS A 1 197 ? 10.854 16.140 52.585 1.00 16.89 ? 197 LYS A CD 1 ATOM 1559 C CE . LYS A 1 197 ? 10.842 17.558 53.146 1.00 19.79 ? 197 LYS A CE 1 ATOM 1560 N NZ . LYS A 1 197 ? 11.985 17.872 54.030 1.00 20.80 ? 197 LYS A NZ 1 ATOM 1561 N N . TRP A 1 198 ? 11.116 11.172 50.446 1.00 13.71 ? 198 TRP A N 1 ATOM 1562 C CA . TRP A 1 198 ? 10.507 10.222 49.523 1.00 13.52 ? 198 TRP A CA 1 ATOM 1563 C C . TRP A 1 198 ? 8.982 10.155 49.662 1.00 13.52 ? 198 TRP A C 1 ATOM 1564 O O . TRP A 1 198 ? 8.267 10.098 48.664 1.00 13.05 ? 198 TRP A O 1 ATOM 1565 C CB . TRP A 1 198 ? 11.121 8.825 49.717 1.00 12.32 ? 198 TRP A CB 1 ATOM 1566 C CG . TRP A 1 198 ? 10.645 7.796 48.715 1.00 11.82 ? 198 TRP A CG 1 ATOM 1567 C CD1 . TRP A 1 198 ? 10.693 7.892 47.350 1.00 11.80 ? 198 TRP A CD1 1 ATOM 1568 C CD2 . TRP A 1 198 ? 10.074 6.512 49.005 1.00 11.87 ? 198 TRP A CD2 1 ATOM 1569 N NE1 . TRP A 1 198 ? 10.191 6.749 46.774 1.00 11.93 ? 198 TRP A NE1 1 ATOM 1570 C CE2 . TRP A 1 198 ? 9.804 5.885 47.765 1.00 11.31 ? 198 TRP A CE2 1 ATOM 1571 C CE3 . TRP A 1 198 ? 9.767 5.829 50.191 1.00 11.23 ? 198 TRP A CE3 1 ATOM 1572 C CZ2 . TRP A 1 198 ? 9.237 4.603 47.676 1.00 11.90 ? 198 TRP A CZ2 1 ATOM 1573 C CZ3 . TRP A 1 198 ? 9.203 4.550 50.104 1.00 13.16 ? 198 TRP A CZ3 1 ATOM 1574 C CH2 . TRP A 1 198 ? 8.945 3.953 48.850 1.00 12.64 ? 198 TRP A CH2 1 ATOM 1575 N N . GLY A 1 199 ? 8.488 10.166 50.896 1.00 15.46 ? 199 GLY A N 1 ATOM 1576 C CA . GLY A 1 199 ? 7.055 10.099 51.119 1.00 15.44 ? 199 GLY A CA 1 ATOM 1577 C C . GLY A 1 199 ? 6.308 11.324 50.620 1.00 16.59 ? 199 GLY A C 1 ATOM 1578 O O . GLY A 1 199 ? 5.274 11.194 49.959 1.00 17.24 ? 199 GLY A O 1 ATOM 1579 N N . LYS A 1 200 ? 6.821 12.509 50.942 1.00 16.95 ? 200 LYS A N 1 ATOM 1580 C CA . LYS A 1 200 ? 6.201 13.765 50.518 1.00 17.99 ? 200 LYS A CA 1 ATOM 1581 C C . LYS A 1 200 ? 6.224 13.887 48.998 1.00 17.88 ? 200 LYS A C 1 ATOM 1582 O O . LYS A 1 200 ? 5.223 14.273 48.378 1.00 16.72 ? 200 LYS A O 1 ATOM 1583 C CB . LYS A 1 200 ? 6.926 14.955 51.150 1.00 20.42 ? 200 LYS A CB 1 ATOM 1584 C CG . LYS A 1 200 ? 6.622 15.136 52.635 1.00 25.92 ? 200 LYS A CG 1 ATOM 1585 C CD . LYS A 1 200 ? 7.461 16.247 53.257 1.00 29.44 ? 200 LYS A CD 1 ATOM 1586 C CE . LYS A 1 200 ? 7.011 16.566 54.689 1.00 32.36 ? 200 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 200 ? 7.088 15.390 55.612 1.00 35.35 ? 200 LYS A NZ 1 ATOM 1588 N N . LEU A 1 201 ? 7.368 13.561 48.397 1.00 15.49 ? 201 LEU A N 1 ATOM 1589 C CA . LEU A 1 201 ? 7.485 13.612 46.948 1.00 14.15 ? 201 LEU A CA 1 ATOM 1590 C C . LEU A 1 201 ? 6.474 12.644 46.339 1.00 14.29 ? 201 LEU A C 1 ATOM 1591 O O . LEU A 1 201 ? 5.780 12.988 45.386 1.00 14.70 ? 201 LEU A O 1 ATOM 1592 C CB . LEU A 1 201 ? 8.907 13.233 46.494 1.00 13.04 ? 201 LEU A CB 1 ATOM 1593 C CG . LEU A 1 201 ? 10.051 14.227 46.755 1.00 13.61 ? 201 LEU A CG 1 ATOM 1594 C CD1 . LEU A 1 201 ? 11.390 13.563 46.436 1.00 11.46 ? 201 LEU A CD1 1 ATOM 1595 C CD2 . LEU A 1 201 ? 9.865 15.501 45.911 1.00 12.13 ? 201 LEU A CD2 1 ATOM 1596 N N . SER A 1 202 ? 6.381 11.439 46.899 1.00 13.01 ? 202 SER A N 1 ATOM 1597 C CA . SER A 1 202 ? 5.459 10.429 46.385 1.00 13.95 ? 202 SER A CA 1 ATOM 1598 C C . SER A 1 202 ? 3.994 10.866 46.425 1.00 14.63 ? 202 SER A C 1 ATOM 1599 O O . SER A 1 202 ? 3.230 10.590 45.492 1.00 14.31 ? 202 SER A O 1 ATOM 1600 C CB . SER A 1 202 ? 5.623 9.113 47.157 1.00 13.94 ? 202 SER A CB 1 ATOM 1601 O OG . SER A 1 202 ? 6.860 8.487 46.840 1.00 13.18 ? 202 SER A OG 1 ATOM 1602 N N . PHE A 1 203 ? 3.605 11.546 47.499 1.00 14.98 ? 203 PHE A N 1 ATOM 1603 C CA . PHE A 1 203 ? 2.229 12.007 47.636 1.00 14.90 ? 203 PHE A CA 1 ATOM 1604 C C . PHE A 1 203 ? 1.906 13.160 46.683 1.00 15.06 ? 203 PHE A C 1 ATOM 1605 O O . PHE A 1 203 ? 0.883 13.133 46.000 1.00 15.71 ? 203 PHE A O 1 ATOM 1606 C CB . PHE A 1 203 ? 1.949 12.422 49.084 1.00 15.58 ? 203 PHE A CB 1 ATOM 1607 C CG . PHE A 1 203 ? 0.566 12.991 49.292 1.00 18.06 ? 203 PHE A CG 1 ATOM 1608 C CD1 . PHE A 1 203 ? 0.374 14.368 49.415 1.00 19.67 ? 203 PHE A CD1 1 ATOM 1609 C CD2 . PHE A 1 203 ? -0.549 12.155 49.300 1.00 17.61 ? 203 PHE A CD2 1 ATOM 1610 C CE1 . PHE A 1 203 ? -0.913 14.904 49.537 1.00 20.73 ? 203 PHE A CE1 1 ATOM 1611 C CE2 . PHE A 1 203 ? -1.834 12.679 49.420 1.00 19.51 ? 203 PHE A CE2 1 ATOM 1612 C CZ . PHE A 1 203 ? -2.016 14.054 49.537 1.00 19.23 ? 203 PHE A CZ 1 ATOM 1613 N N . GLN A 1 204 ? 2.776 14.165 46.627 1.00 16.02 ? 204 GLN A N 1 ATOM 1614 C CA . GLN A 1 204 ? 2.558 15.313 45.742 1.00 16.38 ? 204 GLN A CA 1 ATOM 1615 C C . GLN A 1 204 ? 2.538 14.920 44.262 1.00 16.72 ? 204 GLN A C 1 ATOM 1616 O O . GLN A 1 204 ? 1.808 15.507 43.466 1.00 18.99 ? 204 GLN A O 1 ATOM 1617 C CB . GLN A 1 204 ? 3.645 16.371 45.955 1.00 16.77 ? 204 GLN A CB 1 ATOM 1618 C CG . GLN A 1 204 ? 3.589 17.093 47.291 1.00 16.87 ? 204 GLN A CG 1 ATOM 1619 C CD . GLN A 1 204 ? 2.266 17.796 47.518 1.00 18.84 ? 204 GLN A CD 1 ATOM 1620 O OE1 . GLN A 1 204 ? 1.730 18.449 46.618 1.00 20.25 ? 204 GLN A OE1 1 ATOM 1621 N NE2 . GLN A 1 204 ? 1.738 17.677 48.729 1.00 18.69 ? 204 GLN A NE2 1 ATOM 1622 N N . ILE A 1 205 ? 3.351 13.938 43.893 1.00 15.07 ? 205 ILE A N 1 ATOM 1623 C CA . ILE A 1 205 ? 3.421 13.488 42.507 1.00 14.85 ? 205 ILE A CA 1 ATOM 1624 C C . ILE A 1 205 ? 2.154 12.736 42.136 1.00 16.45 ? 205 ILE A C 1 ATOM 1625 O O . ILE A 1 205 ? 1.519 13.036 41.129 1.00 16.92 ? 205 ILE A O 1 ATOM 1626 C CB . ILE A 1 205 ? 4.652 12.553 42.276 1.00 13.99 ? 205 ILE A CB 1 ATOM 1627 C CG1 . ILE A 1 205 ? 5.949 13.363 42.355 1.00 12.31 ? 205 ILE A CG1 1 ATOM 1628 C CG2 . ILE A 1 205 ? 4.550 11.859 40.925 1.00 11.39 ? 205 ILE A CG2 1 ATOM 1629 C CD1 . ILE A 1 205 ? 7.211 12.515 42.378 1.00 12.99 ? 205 ILE A CD1 1 ATOM 1630 N N . ARG A 1 206 ? 1.783 11.763 42.962 1.00 17.85 ? 206 ARG A N 1 ATOM 1631 C CA . ARG A 1 206 ? 0.596 10.956 42.699 1.00 18.27 ? 206 ARG A CA 1 ATOM 1632 C C . ARG A 1 206 ? -0.700 11.771 42.649 1.00 18.77 ? 206 ARG A C 1 ATOM 1633 O O . ARG A 1 206 ? -1.568 11.510 41.810 1.00 19.52 ? 206 ARG A O 1 ATOM 1634 C CB . ARG A 1 206 ? 0.468 9.852 43.755 1.00 19.26 ? 206 ARG A CB 1 ATOM 1635 C CG . ARG A 1 206 ? -0.562 8.770 43.405 1.00 18.44 ? 206 ARG A CG 1 ATOM 1636 C CD . ARG A 1 206 ? -0.677 7.727 44.503 1.00 20.20 ? 206 ARG A CD 1 ATOM 1637 N NE . ARG A 1 206 ? -1.149 8.326 45.747 1.00 20.38 ? 206 ARG A NE 1 ATOM 1638 C CZ . ARG A 1 206 ? -2.415 8.644 45.991 1.00 20.23 ? 206 ARG A CZ 1 ATOM 1639 N NH1 . ARG A 1 206 ? -3.348 8.412 45.077 1.00 19.70 ? 206 ARG A NH1 1 ATOM 1640 N NH2 . ARG A 1 206 ? -2.742 9.213 47.139 1.00 19.00 ? 206 ARG A NH2 1 ATOM 1641 N N . THR A 1 207 ? -0.826 12.761 43.532 1.00 18.08 ? 207 THR A N 1 ATOM 1642 C CA . THR A 1 207 ? -2.036 13.588 43.585 1.00 18.51 ? 207 THR A CA 1 ATOM 1643 C C . THR A 1 207 ? -2.046 14.814 42.658 1.00 19.19 ? 207 THR A C 1 ATOM 1644 O O . THR A 1 207 ? -3.012 15.587 42.643 1.00 18.19 ? 207 THR A O 1 ATOM 1645 C CB . THR A 1 207 ? -2.318 14.062 45.034 1.00 17.46 ? 207 THR A CB 1 ATOM 1646 O OG1 . THR A 1 207 ? -1.246 14.897 45.494 1.00 18.61 ? 207 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 207 ? -2.458 12.866 45.960 1.00 16.05 ? 207 THR A CG2 1 ATOM 1648 N N . SER A 1 208 ? -0.983 14.993 41.880 1.00 18.30 ? 208 SER A N 1 ATOM 1649 C CA . SER A 1 208 ? -0.914 16.128 40.967 1.00 18.21 ? 208 SER A CA 1 ATOM 1650 C C . SER A 1 208 ? -1.730 15.869 39.699 1.00 17.99 ? 208 SER A C 1 ATOM 1651 O O . SER A 1 208 ? -2.039 14.718 39.362 1.00 16.39 ? 208 SER A O 1 ATOM 1652 C CB . SER A 1 208 ? 0.545 16.433 40.596 1.00 17.68 ? 208 SER A CB 1 ATOM 1653 O OG . SER A 1 208 ? 1.126 15.374 39.855 1.00 19.81 ? 208 SER A OG 1 ATOM 1654 N N . GLY A 1 209 ? -2.088 16.949 39.011 1.00 17.72 ? 209 GLY A N 1 ATOM 1655 C CA . GLY A 1 209 ? -2.854 16.820 37.788 1.00 19.72 ? 209 GLY A CA 1 ATOM 1656 C C . GLY A 1 209 ? -1.948 16.555 36.604 1.00 21.39 ? 209 GLY A C 1 ATOM 1657 O O . GLY A 1 209 ? -0.748 16.332 36.775 1.00 21.42 ? 209 GLY A O 1 ATOM 1658 N N . ALA A 1 210 ? -2.508 16.586 35.399 1.00 22.23 ? 210 ALA A N 1 ATOM 1659 C CA . ALA A 1 210 ? -1.721 16.339 34.199 1.00 22.94 ? 210 ALA A CA 1 ATOM 1660 C C . ALA A 1 210 ? -0.550 17.316 34.065 1.00 23.68 ? 210 ALA A C 1 ATOM 1661 O O . ALA A 1 210 ? 0.498 16.957 33.528 1.00 24.72 ? 210 ALA A O 1 ATOM 1662 C CB . ALA A 1 210 ? -2.612 16.408 32.964 1.00 23.21 ? 210 ALA A CB 1 ATOM 1663 N N . ASN A 1 211 ? -0.709 18.543 34.554 1.00 23.18 ? 211 ASN A N 1 ATOM 1664 C CA . ASN A 1 211 ? 0.379 19.505 34.447 1.00 24.53 ? 211 ASN A CA 1 ATOM 1665 C C . ASN A 1 211 ? 1.527 19.216 35.417 1.00 25.03 ? 211 ASN A C 1 ATOM 1666 O O . ASN A 1 211 ? 2.559 19.887 35.376 1.00 26.63 ? 211 ASN A O 1 ATOM 1667 C CB . ASN A 1 211 ? -0.127 20.937 34.660 1.00 25.06 ? 211 ASN A CB 1 ATOM 1668 C CG . ASN A 1 211 ? -0.745 21.147 36.028 1.00 26.41 ? 211 ASN A CG 1 ATOM 1669 O OD1 . ASN A 1 211 ? -0.527 20.368 36.954 1.00 27.71 ? 211 ASN A OD1 1 ATOM 1670 N ND2 . ASN A 1 211 ? -1.514 22.218 36.163 1.00 26.58 ? 211 ASN A ND2 1 ATOM 1671 N N . GLY A 1 212 ? 1.344 18.232 36.294 1.00 24.31 ? 212 GLY A N 1 ATOM 1672 C CA . GLY A 1 212 ? 2.386 17.872 37.246 1.00 22.62 ? 212 GLY A CA 1 ATOM 1673 C C . GLY A 1 212 ? 2.692 18.847 38.375 1.00 22.35 ? 212 GLY A C 1 ATOM 1674 O O . GLY A 1 212 ? 3.667 18.660 39.110 1.00 20.45 ? 212 GLY A O 1 ATOM 1675 N N . MET A 1 213 ? 1.869 19.881 38.532 1.00 22.06 ? 213 MET A N 1 ATOM 1676 C CA . MET A 1 213 ? 2.088 20.871 39.583 1.00 22.75 ? 213 MET A CA 1 ATOM 1677 C C . MET A 1 213 ? 1.706 20.365 40.970 1.00 22.48 ? 213 MET A C 1 ATOM 1678 O O . MET A 1 213 ? 0.588 19.892 41.182 1.00 22.79 ? 213 MET A O 1 ATOM 1679 C CB . MET A 1 213 ? 1.300 22.151 39.285 1.00 24.17 ? 213 MET A CB 1 ATOM 1680 C CG . MET A 1 213 ? 1.710 22.853 38.002 1.00 28.71 ? 213 MET A CG 1 ATOM 1681 S SD . MET A 1 213 ? 3.479 23.235 37.935 1.00 34.27 ? 213 MET A SD 1 ATOM 1682 C CE . MET A 1 213 ? 3.613 24.476 39.258 1.00 30.47 ? 213 MET A CE 1 ATOM 1683 N N . PHE A 1 214 ? 2.644 20.470 41.909 1.00 22.33 ? 214 PHE A N 1 ATOM 1684 C CA . PHE A 1 214 ? 2.416 20.046 43.289 1.00 22.46 ? 214 PHE A CA 1 ATOM 1685 C C . PHE A 1 214 ? 1.448 21.014 43.955 1.00 24.39 ? 214 PHE A C 1 ATOM 1686 O O . PHE A 1 214 ? 1.520 22.220 43.721 1.00 24.57 ? 214 PHE A O 1 ATOM 1687 C CB . PHE A 1 214 ? 3.724 20.076 44.086 1.00 20.52 ? 214 PHE A CB 1 ATOM 1688 C CG . PHE A 1 214 ? 4.679 18.960 43.757 1.00 19.15 ? 214 PHE A CG 1 ATOM 1689 C CD1 . PHE A 1 214 ? 4.458 18.116 42.675 1.00 18.13 ? 214 PHE A CD1 1 ATOM 1690 C CD2 . PHE A 1 214 ? 5.823 18.773 44.527 1.00 18.03 ? 214 PHE A CD2 1 ATOM 1691 C CE1 . PHE A 1 214 ? 5.365 17.105 42.363 1.00 18.30 ? 214 PHE A CE1 1 ATOM 1692 C CE2 . PHE A 1 214 ? 6.732 17.766 44.223 1.00 17.51 ? 214 PHE A CE2 1 ATOM 1693 C CZ . PHE A 1 214 ? 6.502 16.932 43.138 1.00 17.83 ? 214 PHE A CZ 1 ATOM 1694 N N . SER A 1 215 ? 0.549 20.497 44.787 1.00 26.46 ? 215 SER A N 1 ATOM 1695 C CA . SER A 1 215 ? -0.384 21.365 45.497 1.00 28.35 ? 215 SER A CA 1 ATOM 1696 C C . SER A 1 215 ? 0.448 22.091 46.551 1.00 28.38 ? 215 SER A C 1 ATOM 1697 O O . SER A 1 215 ? 0.199 23.254 46.871 1.00 28.70 ? 215 SER A O 1 ATOM 1698 C CB . SER A 1 215 ? -1.495 20.541 46.147 1.00 28.61 ? 215 SER A CB 1 ATOM 1699 O OG . SER A 1 215 ? -0.954 19.461 46.875 1.00 33.62 ? 215 SER A OG 1 ATOM 1700 N N . GLU A 1 216 ? 1.451 21.386 47.072 1.00 28.24 ? 216 GLU A N 1 ATOM 1701 C CA . GLU A 1 216 ? 2.382 21.933 48.056 1.00 28.29 ? 216 GLU A CA 1 ATOM 1702 C C . GLU A 1 216 ? 3.803 21.573 47.614 1.00 26.52 ? 216 GLU A C 1 ATOM 1703 O O . GLU A 1 216 ? 4.092 20.418 47.317 1.00 25.60 ? 216 GLU A O 1 ATOM 1704 C CB . GLU A 1 216 ? 2.114 21.353 49.451 1.00 31.32 ? 216 GLU A CB 1 ATOM 1705 C CG . GLU A 1 216 ? 1.165 22.174 50.330 1.00 37.81 ? 216 GLU A CG 1 ATOM 1706 C CD . GLU A 1 216 ? -0.271 22.190 49.823 1.00 41.56 ? 216 GLU A CD 1 ATOM 1707 O OE1 . GLU A 1 216 ? -0.865 21.095 49.680 1.00 43.49 ? 216 GLU A OE1 1 ATOM 1708 O OE2 . GLU A 1 216 ? -0.807 23.297 49.574 1.00 42.16 ? 216 GLU A OE2 1 ATOM 1709 N N . ALA A 1 217 ? 4.681 22.566 47.554 1.00 25.38 ? 217 ALA A N 1 ATOM 1710 C CA . ALA A 1 217 ? 6.063 22.332 47.147 1.00 24.91 ? 217 ALA A CA 1 ATOM 1711 C C . ALA A 1 217 ? 6.777 21.479 48.187 1.00 24.20 ? 217 ALA A C 1 ATOM 1712 O O . ALA A 1 217 ? 6.369 21.432 49.352 1.00 24.93 ? 217 ALA A O 1 ATOM 1713 C CB . ALA A 1 217 ? 6.794 23.655 46.982 1.00 24.09 ? 217 ALA A CB 1 ATOM 1714 N N . VAL A 1 218 ? 7.839 20.803 47.758 1.00 21.79 ? 218 VAL A N 1 ATOM 1715 C CA . VAL A 1 218 ? 8.631 19.959 48.644 1.00 19.01 ? 218 VAL A CA 1 ATOM 1716 C C . VAL A 1 218 ? 10.057 20.503 48.717 1.00 18.77 ? 218 VAL A C 1 ATOM 1717 O O . VAL A 1 218 ? 10.728 20.687 47.696 1.00 18.41 ? 218 VAL A O 1 ATOM 1718 C CB . VAL A 1 218 ? 8.670 18.500 48.143 1.00 18.18 ? 218 VAL A CB 1 ATOM 1719 C CG1 . VAL A 1 218 ? 9.502 17.641 49.100 1.00 15.23 ? 218 VAL A CG1 1 ATOM 1720 C CG2 . VAL A 1 218 ? 7.258 17.956 48.035 1.00 15.89 ? 218 VAL A CG2 1 ATOM 1721 N N . GLU A 1 219 ? 10.523 20.764 49.930 1.00 18.64 ? 219 GLU A N 1 ATOM 1722 C CA . GLU A 1 219 ? 11.860 21.309 50.100 1.00 19.75 ? 219 GLU A CA 1 ATOM 1723 C C . GLU A 1 219 ? 12.957 20.250 50.075 1.00 18.90 ? 219 GLU A C 1 ATOM 1724 O O . GLU A 1 219 ? 12.881 19.241 50.778 1.00 17.81 ? 219 GLU A O 1 ATOM 1725 C CB . GLU A 1 219 ? 11.937 22.090 51.409 1.00 20.35 ? 219 GLU A CB 1 ATOM 1726 C CG . GLU A 1 219 ? 13.283 22.728 51.677 1.00 23.28 ? 219 GLU A CG 1 ATOM 1727 C CD . GLU A 1 219 ? 13.294 23.462 53.002 1.00 28.39 ? 219 GLU A CD 1 ATOM 1728 O OE1 . GLU A 1 219 ? 12.670 24.544 53.099 1.00 29.36 ? 219 GLU A OE1 1 ATOM 1729 O OE2 . GLU A 1 219 ? 13.916 22.948 53.956 1.00 29.99 ? 219 GLU A OE2 1 ATOM 1730 N N . LEU A 1 220 ? 13.970 20.490 49.247 1.00 18.03 ? 220 LEU A N 1 ATOM 1731 C CA . LEU A 1 220 ? 15.117 19.599 49.134 1.00 16.60 ? 220 LEU A CA 1 ATOM 1732 C C . LEU A 1 220 ? 16.348 20.466 49.379 1.00 18.00 ? 220 LEU A C 1 ATOM 1733 O O . LEU A 1 220 ? 16.219 21.679 49.582 1.00 17.52 ? 220 LEU A O 1 ATOM 1734 C CB . LEU A 1 220 ? 15.178 18.949 47.745 1.00 14.76 ? 220 LEU A CB 1 ATOM 1735 C CG . LEU A 1 220 ? 14.128 17.865 47.449 1.00 16.59 ? 220 LEU A CG 1 ATOM 1736 C CD1 . LEU A 1 220 ? 14.345 17.318 46.052 1.00 15.27 ? 220 LEU A CD1 1 ATOM 1737 C CD2 . LEU A 1 220 ? 14.225 16.731 48.477 1.00 16.93 ? 220 LEU A CD2 1 ATOM 1738 N N . GLU A 1 221 ? 17.532 19.861 49.380 1.00 17.52 ? 221 GLU A N 1 ATOM 1739 C CA . GLU A 1 221 ? 18.750 20.623 49.620 1.00 18.02 ? 221 GLU A CA 1 ATOM 1740 C C . GLU A 1 221 ? 19.832 20.219 48.656 1.00 19.36 ? 221 GLU A C 1 ATOM 1741 O O . GLU A 1 221 ? 19.841 19.093 48.162 1.00 19.13 ? 221 GLU A O 1 ATOM 1742 C CB . GLU A 1 221 ? 19.282 20.398 51.042 1.00 19.63 ? 221 GLU A CB 1 ATOM 1743 C CG . GLU A 1 221 ? 18.263 20.584 52.168 1.00 21.94 ? 221 GLU A CG 1 ATOM 1744 C CD . GLU A 1 221 ? 18.910 20.614 53.545 1.00 22.21 ? 221 GLU A CD 1 ATOM 1745 O OE1 . GLU A 1 221 ? 19.967 19.971 53.728 1.00 24.14 ? 221 GLU A OE1 1 ATOM 1746 O OE2 . GLU A 1 221 ? 18.356 21.272 54.451 1.00 22.83 ? 221 GLU A OE2 1 ATOM 1747 N N . ARG A 1 222 ? 20.739 21.154 48.391 1.00 18.88 ? 222 ARG A N 1 ATOM 1748 C CA . ARG A 1 222 ? 21.872 20.905 47.520 1.00 19.57 ? 222 ARG A CA 1 ATOM 1749 C C . ARG A 1 222 ? 22.913 20.266 48.435 1.00 20.59 ? 222 ARG A C 1 ATOM 1750 O O . ARG A 1 222 ? 22.668 20.107 49.635 1.00 20.39 ? 222 ARG A O 1 ATOM 1751 C CB . ARG A 1 222 ? 22.403 22.221 46.933 1.00 19.87 ? 222 ARG A CB 1 ATOM 1752 C CG . ARG A 1 222 ? 21.453 22.901 45.950 1.00 19.23 ? 222 ARG A CG 1 ATOM 1753 C CD . ARG A 1 222 ? 21.172 22.020 44.732 1.00 20.88 ? 222 ARG A CD 1 ATOM 1754 N NE . ARG A 1 222 ? 20.153 22.603 43.859 1.00 21.76 ? 222 ARG A NE 1 ATOM 1755 C CZ . ARG A 1 222 ? 19.563 21.960 42.851 1.00 23.36 ? 222 ARG A CZ 1 ATOM 1756 N NH1 . ARG A 1 222 ? 19.883 20.698 42.571 1.00 20.58 ? 222 ARG A NH1 1 ATOM 1757 N NH2 . ARG A 1 222 ? 18.636 22.575 42.127 1.00 22.47 ? 222 ARG A NH2 1 ATOM 1758 N N . ALA A 1 223 ? 24.065 19.902 47.874 1.00 22.14 ? 223 ALA A N 1 ATOM 1759 C CA . ALA A 1 223 ? 25.132 19.264 48.638 1.00 23.24 ? 223 ALA A CA 1 ATOM 1760 C C . ALA A 1 223 ? 25.544 20.082 49.858 1.00 25.38 ? 223 ALA A C 1 ATOM 1761 O O . ALA A 1 223 ? 25.813 19.531 50.923 1.00 25.30 ? 223 ALA A O 1 ATOM 1762 C CB . ALA A 1 223 ? 26.342 19.020 47.736 1.00 21.89 ? 223 ALA A CB 1 ATOM 1763 N N . ASN A 1 224 ? 25.563 21.401 49.699 1.00 27.57 ? 224 ASN A N 1 ATOM 1764 C CA . ASN A 1 224 ? 25.958 22.311 50.765 1.00 29.13 ? 224 ASN A CA 1 ATOM 1765 C C . ASN A 1 224 ? 24.842 22.736 51.718 1.00 28.98 ? 224 ASN A C 1 ATOM 1766 O O . ASN A 1 224 ? 25.048 23.596 52.572 1.00 29.66 ? 224 ASN A O 1 ATOM 1767 C CB . ASN A 1 224 ? 26.602 23.546 50.142 1.00 32.48 ? 224 ASN A CB 1 ATOM 1768 C CG . ASN A 1 224 ? 25.691 24.230 49.150 1.00 35.09 ? 224 ASN A CG 1 ATOM 1769 O OD1 . ASN A 1 224 ? 24.844 25.030 49.529 1.00 37.53 ? 224 ASN A OD1 1 ATOM 1770 N ND2 . ASN A 1 224 ? 25.846 23.900 47.871 1.00 37.50 ? 224 ASN A ND2 1 ATOM 1771 N N . GLY A 1 225 ? 23.660 22.144 51.580 1.00 27.74 ? 225 GLY A N 1 ATOM 1772 C CA . GLY A 1 225 ? 22.570 22.498 52.472 1.00 26.36 ? 225 GLY A CA 1 ATOM 1773 C C . GLY A 1 225 ? 21.613 23.557 51.951 1.00 26.93 ? 225 GLY A C 1 ATOM 1774 O O . GLY A 1 225 ? 20.510 23.705 52.483 1.00 26.51 ? 225 GLY A O 1 ATOM 1775 N N . LYS A 1 226 ? 22.027 24.304 50.928 1.00 26.27 ? 226 LYS A N 1 ATOM 1776 C CA . LYS A 1 226 ? 21.169 25.335 50.341 1.00 25.31 ? 226 LYS A CA 1 ATOM 1777 C C . LYS A 1 226 ? 19.844 24.697 49.929 1.00 24.57 ? 226 LYS A C 1 ATOM 1778 O O . LYS A 1 226 ? 19.820 23.719 49.180 1.00 24.06 ? 226 LYS A O 1 ATOM 1779 C CB . LYS A 1 226 ? 21.832 25.951 49.104 1.00 26.93 ? 226 LYS A CB 1 ATOM 1780 C CG . LYS A 1 226 ? 20.922 26.892 48.324 1.00 28.64 ? 226 LYS A CG 1 ATOM 1781 C CD . LYS A 1 226 ? 21.366 27.033 46.876 1.00 31.46 ? 226 LYS A CD 1 ATOM 1782 C CE . LYS A 1 226 ? 22.531 27.990 46.730 1.00 34.62 ? 226 LYS A CE 1 ATOM 1783 N NZ . LYS A 1 226 ? 23.715 27.602 47.537 1.00 38.87 ? 226 LYS A NZ 1 ATOM 1784 N N . LYS A 1 227 ? 18.744 25.258 50.409 1.00 22.89 ? 227 LYS A N 1 ATOM 1785 C CA . LYS A 1 227 ? 17.424 24.725 50.100 1.00 23.44 ? 227 LYS A CA 1 ATOM 1786 C C . LYS A 1 227 ? 16.902 25.149 48.745 1.00 21.96 ? 227 LYS A C 1 ATOM 1787 O O . LYS A 1 227 ? 17.302 26.172 48.204 1.00 21.77 ? 227 LYS A O 1 ATOM 1788 C CB . LYS A 1 227 ? 16.414 25.186 51.154 1.00 25.67 ? 227 LYS A CB 1 ATOM 1789 C CG . LYS A 1 227 ? 16.916 25.028 52.570 1.00 31.46 ? 227 LYS A CG 1 ATOM 1790 C CD . LYS A 1 227 ? 15.964 25.613 53.588 1.00 33.73 ? 227 LYS A CD 1 ATOM 1791 C CE . LYS A 1 227 ? 16.568 25.489 54.977 1.00 36.18 ? 227 LYS A CE 1 ATOM 1792 N NZ . LYS A 1 227 ? 17.017 24.088 55.259 1.00 36.03 ? 227 LYS A NZ 1 ATOM 1793 N N . TYR A 1 228 ? 16.014 24.329 48.199 1.00 21.08 ? 228 TYR A N 1 ATOM 1794 C CA . TYR A 1 228 ? 15.334 24.626 46.953 1.00 21.19 ? 228 TYR A CA 1 ATOM 1795 C C . TYR A 1 228 ? 14.006 23.889 47.041 1.00 22.83 ? 228 TYR A C 1 ATOM 1796 O O . TYR A 1 228 ? 13.865 22.936 47.809 1.00 22.87 ? 228 TYR A O 1 ATOM 1797 C CB . TYR A 1 228 ? 16.139 24.222 45.709 1.00 21.20 ? 228 TYR A CB 1 ATOM 1798 C CG . TYR A 1 228 ? 16.373 22.748 45.459 1.00 22.20 ? 228 TYR A CG 1 ATOM 1799 C CD1 . TYR A 1 228 ? 17.445 22.081 46.053 1.00 21.29 ? 228 TYR A CD1 1 ATOM 1800 C CD2 . TYR A 1 228 ? 15.584 22.045 44.542 1.00 22.62 ? 228 TYR A CD2 1 ATOM 1801 C CE1 . TYR A 1 228 ? 17.738 20.760 45.737 1.00 20.14 ? 228 TYR A CE1 1 ATOM 1802 C CE2 . TYR A 1 228 ? 15.869 20.716 44.218 1.00 22.61 ? 228 TYR A CE2 1 ATOM 1803 C CZ . TYR A 1 228 ? 16.952 20.083 44.820 1.00 21.96 ? 228 TYR A CZ 1 ATOM 1804 O OH . TYR A 1 228 ? 17.259 18.781 44.493 1.00 22.40 ? 228 TYR A OH 1 ATOM 1805 N N . TYR A 1 229 ? 13.015 24.350 46.290 1.00 23.70 ? 229 TYR A N 1 ATOM 1806 C CA . TYR A 1 229 ? 11.706 23.734 46.354 1.00 22.15 ? 229 TYR A CA 1 ATOM 1807 C C . TYR A 1 229 ? 11.296 23.068 45.069 1.00 21.77 ? 229 TYR A C 1 ATOM 1808 O O . TYR A 1 229 ? 11.460 23.629 43.985 1.00 22.26 ? 229 TYR A O 1 ATOM 1809 C CB . TYR A 1 229 ? 10.666 24.782 46.756 1.00 22.83 ? 229 TYR A CB 1 ATOM 1810 C CG . TYR A 1 229 ? 10.948 25.354 48.114 1.00 23.13 ? 229 TYR A CG 1 ATOM 1811 C CD1 . TYR A 1 229 ? 12.006 26.241 48.311 1.00 26.15 ? 229 TYR A CD1 1 ATOM 1812 C CD2 . TYR A 1 229 ? 10.223 24.942 49.225 1.00 25.32 ? 229 TYR A CD2 1 ATOM 1813 C CE1 . TYR A 1 229 ? 12.341 26.697 49.582 1.00 26.04 ? 229 TYR A CE1 1 ATOM 1814 C CE2 . TYR A 1 229 ? 10.548 25.393 50.502 1.00 26.76 ? 229 TYR A CE2 1 ATOM 1815 C CZ . TYR A 1 229 ? 11.610 26.267 50.668 1.00 26.83 ? 229 TYR A CZ 1 ATOM 1816 O OH . TYR A 1 229 ? 11.948 26.692 51.926 1.00 30.95 ? 229 TYR A OH 1 ATOM 1817 N N . VAL A 1 230 ? 10.792 21.846 45.194 1.00 20.25 ? 230 VAL A N 1 ATOM 1818 C CA . VAL A 1 230 ? 10.315 21.116 44.034 1.00 19.88 ? 230 VAL A CA 1 ATOM 1819 C C . VAL A 1 230 ? 8.821 21.437 43.971 1.00 19.80 ? 230 VAL A C 1 ATOM 1820 O O . VAL A 1 230 ? 8.089 21.224 44.940 1.00 19.23 ? 230 VAL A O 1 ATOM 1821 C CB . VAL A 1 230 ? 10.532 19.592 44.184 1.00 18.18 ? 230 VAL A CB 1 ATOM 1822 C CG1 . VAL A 1 230 ? 9.950 18.859 42.973 1.00 16.41 ? 230 VAL A CG1 1 ATOM 1823 C CG2 . VAL A 1 230 ? 12.016 19.297 44.306 1.00 17.78 ? 230 VAL A CG2 1 ATOM 1824 N N . THR A 1 231 ? 8.387 21.983 42.841 1.00 20.19 ? 231 THR A N 1 ATOM 1825 C CA . THR A 1 231 ? 6.988 22.349 42.659 1.00 21.90 ? 231 THR A CA 1 ATOM 1826 C C . THR A 1 231 ? 6.330 21.607 41.499 1.00 21.98 ? 231 THR A C 1 ATOM 1827 O O . THR A 1 231 ? 5.146 21.792 41.229 1.00 22.21 ? 231 THR A O 1 ATOM 1828 C CB . THR A 1 231 ? 6.842 23.865 42.414 1.00 21.36 ? 231 THR A CB 1 ATOM 1829 O OG1 . THR A 1 231 ? 7.653 24.250 41.294 1.00 21.27 ? 231 THR A OG1 1 ATOM 1830 C CG2 . THR A 1 231 ? 7.270 24.647 43.650 1.00 21.00 ? 231 THR A CG2 1 ATOM 1831 N N . ALA A 1 232 ? 7.099 20.767 40.816 1.00 21.31 ? 232 ALA A N 1 ATOM 1832 C CA . ALA A 1 232 ? 6.563 20.013 39.690 1.00 21.67 ? 232 ALA A CA 1 ATOM 1833 C C . ALA A 1 232 ? 7.224 18.645 39.558 1.00 20.71 ? 232 ALA A C 1 ATOM 1834 O O . ALA A 1 232 ? 8.401 18.479 39.880 1.00 20.99 ? 232 ALA A O 1 ATOM 1835 C CB . ALA A 1 232 ? 6.744 20.808 38.391 1.00 21.16 ? 232 ALA A CB 1 ATOM 1836 N N . VAL A 1 233 ? 6.454 17.678 39.071 1.00 19.54 ? 233 VAL A N 1 ATOM 1837 C CA . VAL A 1 233 ? 6.931 16.313 38.876 1.00 19.52 ? 233 VAL A CA 1 ATOM 1838 C C . VAL A 1 233 ? 8.240 16.257 38.090 1.00 21.69 ? 233 VAL A C 1 ATOM 1839 O O . VAL A 1 233 ? 9.240 15.706 38.551 1.00 21.40 ? 233 VAL A O 1 ATOM 1840 C CB . VAL A 1 233 ? 5.875 15.471 38.116 1.00 17.96 ? 233 VAL A CB 1 ATOM 1841 C CG1 . VAL A 1 233 ? 6.445 14.112 37.749 1.00 16.37 ? 233 VAL A CG1 1 ATOM 1842 C CG2 . VAL A 1 233 ? 4.615 15.320 38.966 1.00 16.72 ? 233 VAL A CG2 1 ATOM 1843 N N . ASP A 1 234 ? 8.231 16.838 36.899 1.00 23.35 ? 234 ASP A N 1 ATOM 1844 C CA . ASP A 1 234 ? 9.404 16.813 36.041 1.00 25.28 ? 234 ASP A CA 1 ATOM 1845 C C . ASP A 1 234 ? 10.680 17.371 36.647 1.00 23.87 ? 234 ASP A C 1 ATOM 1846 O O . ASP A 1 234 ? 11.767 17.086 36.157 1.00 25.82 ? 234 ASP A O 1 ATOM 1847 C CB . ASP A 1 234 ? 9.093 17.523 34.727 1.00 30.59 ? 234 ASP A CB 1 ATOM 1848 C CG . ASP A 1 234 ? 7.976 16.844 33.961 1.00 35.55 ? 234 ASP A CG 1 ATOM 1849 O OD1 . ASP A 1 234 ? 8.041 15.602 33.790 1.00 37.14 ? 234 ASP A OD1 1 ATOM 1850 O OD2 . ASP A 1 234 ? 7.032 17.546 33.534 1.00 40.59 ? 234 ASP A OD2 1 ATOM 1851 N N . GLN A 1 235 ? 10.562 18.159 37.706 1.00 21.47 ? 235 GLN A N 1 ATOM 1852 C CA . GLN A 1 235 ? 11.743 18.719 38.352 1.00 20.76 ? 235 GLN A CA 1 ATOM 1853 C C . GLN A 1 235 ? 12.538 17.641 39.082 1.00 20.41 ? 235 GLN A C 1 ATOM 1854 O O . GLN A 1 235 ? 13.751 17.759 39.256 1.00 21.01 ? 235 GLN A O 1 ATOM 1855 C CB . GLN A 1 235 ? 11.336 19.790 39.362 1.00 20.47 ? 235 GLN A CB 1 ATOM 1856 C CG . GLN A 1 235 ? 10.885 21.094 38.752 1.00 22.18 ? 235 GLN A CG 1 ATOM 1857 C CD . GLN A 1 235 ? 10.288 22.029 39.785 1.00 25.02 ? 235 GLN A CD 1 ATOM 1858 O OE1 . GLN A 1 235 ? 10.704 22.046 40.942 1.00 25.28 ? 235 GLN A OE1 1 ATOM 1859 N NE2 . GLN A 1 235 ? 9.314 22.824 39.366 1.00 29.34 ? 235 GLN A NE2 1 ATOM 1860 N N . VAL A 1 236 ? 11.849 16.588 39.504 1.00 18.51 ? 236 VAL A N 1 ATOM 1861 C CA . VAL A 1 236 ? 12.487 15.526 40.259 1.00 16.79 ? 236 VAL A CA 1 ATOM 1862 C C . VAL A 1 236 ? 12.360 14.134 39.629 1.00 16.35 ? 236 VAL A C 1 ATOM 1863 O O . VAL A 1 236 ? 13.067 13.209 40.020 1.00 15.42 ? 236 VAL A O 1 ATOM 1864 C CB . VAL A 1 236 ? 11.913 15.517 41.703 1.00 17.70 ? 236 VAL A CB 1 ATOM 1865 C CG1 . VAL A 1 236 ? 10.504 14.930 41.706 1.00 16.99 ? 236 VAL A CG1 1 ATOM 1866 C CG2 . VAL A 1 236 ? 12.840 14.781 42.635 1.00 19.79 ? 236 VAL A CG2 1 ATOM 1867 N N . LYS A 1 237 ? 11.484 13.994 38.638 1.00 15.70 ? 237 LYS A N 1 ATOM 1868 C CA . LYS A 1 237 ? 11.269 12.706 37.982 1.00 15.94 ? 237 LYS A CA 1 ATOM 1869 C C . LYS A 1 237 ? 12.528 11.918 37.596 1.00 16.19 ? 237 LYS A C 1 ATOM 1870 O O . LYS A 1 237 ? 12.590 10.710 37.805 1.00 16.23 ? 237 LYS A O 1 ATOM 1871 C CB . LYS A 1 237 ? 10.390 12.877 36.737 1.00 17.06 ? 237 LYS A CB 1 ATOM 1872 C CG . LYS A 1 237 ? 10.110 11.562 36.018 1.00 19.49 ? 237 LYS A CG 1 ATOM 1873 C CD . LYS A 1 237 ? 9.312 11.727 34.723 1.00 18.30 ? 237 LYS A CD 1 ATOM 1874 C CE . LYS A 1 237 ? 7.833 11.908 34.995 1.00 17.60 ? 237 LYS A CE 1 ATOM 1875 N NZ . LYS A 1 237 ? 7.034 11.883 33.734 1.00 12.06 ? 237 LYS A NZ 1 ATOM 1876 N N . PRO A 1 238 ? 13.544 12.581 37.018 1.00 16.46 ? 238 PRO A N 1 ATOM 1877 C CA . PRO A 1 238 ? 14.743 11.819 36.646 1.00 16.31 ? 238 PRO A CA 1 ATOM 1878 C C . PRO A 1 238 ? 15.548 11.233 37.804 1.00 14.61 ? 238 PRO A C 1 ATOM 1879 O O . PRO A 1 238 ? 16.416 10.390 37.591 1.00 15.16 ? 238 PRO A O 1 ATOM 1880 C CB . PRO A 1 238 ? 15.548 12.819 35.811 1.00 16.10 ? 238 PRO A CB 1 ATOM 1881 C CG . PRO A 1 238 ? 15.127 14.132 36.349 1.00 18.13 ? 238 PRO A CG 1 ATOM 1882 C CD . PRO A 1 238 ? 13.646 13.977 36.558 1.00 17.50 ? 238 PRO A CD 1 ATOM 1883 N N . LYS A 1 239 ? 15.246 11.666 39.024 1.00 13.70 ? 239 LYS A N 1 ATOM 1884 C CA . LYS A 1 239 ? 15.946 11.187 40.216 1.00 13.04 ? 239 LYS A CA 1 ATOM 1885 C C . LYS A 1 239 ? 15.256 10.033 40.944 1.00 12.72 ? 239 LYS A C 1 ATOM 1886 O O . LYS A 1 239 ? 15.849 9.418 41.832 1.00 11.38 ? 239 LYS A O 1 ATOM 1887 C CB . LYS A 1 239 ? 16.113 12.339 41.209 1.00 13.41 ? 239 LYS A CB 1 ATOM 1888 C CG . LYS A 1 239 ? 16.876 13.514 40.648 1.00 15.15 ? 239 LYS A CG 1 ATOM 1889 C CD . LYS A 1 239 ? 17.053 14.613 41.679 1.00 17.78 ? 239 LYS A CD 1 ATOM 1890 C CE . LYS A 1 239 ? 17.818 15.779 41.077 1.00 19.47 ? 239 LYS A CE 1 ATOM 1891 N NZ . LYS A 1 239 ? 18.077 16.812 42.100 1.00 24.59 ? 239 LYS A NZ 1 ATOM 1892 N N . ILE A 1 240 ? 14.012 9.744 40.567 1.00 12.58 ? 240 ILE A N 1 ATOM 1893 C CA . ILE A 1 240 ? 13.208 8.707 41.214 1.00 12.91 ? 240 ILE A CA 1 ATOM 1894 C C . ILE A 1 240 ? 12.964 7.452 40.372 1.00 12.63 ? 240 ILE A C 1 ATOM 1895 O O . ILE A 1 240 ? 12.611 7.545 39.197 1.00 11.32 ? 240 ILE A O 1 ATOM 1896 C CB . ILE A 1 240 ? 11.822 9.288 41.622 1.00 13.66 ? 240 ILE A CB 1 ATOM 1897 C CG1 . ILE A 1 240 ? 12.016 10.591 42.405 1.00 13.69 ? 240 ILE A CG1 1 ATOM 1898 C CG2 . ILE A 1 240 ? 11.048 8.271 42.464 1.00 13.73 ? 240 ILE A CG2 1 ATOM 1899 C CD1 . ILE A 1 240 ? 10.724 11.334 42.701 1.00 14.55 ? 240 ILE A CD1 1 ATOM 1900 N N . ALA A 1 241 ? 13.135 6.281 40.987 1.00 12.21 ? 241 ALA A N 1 ATOM 1901 C CA . ALA A 1 241 ? 12.915 5.004 40.303 1.00 11.82 ? 241 ALA A CA 1 ATOM 1902 C C . ALA A 1 241 ? 11.588 4.360 40.714 1.00 12.22 ? 241 ALA A C 1 ATOM 1903 O O . ALA A 1 241 ? 10.949 3.680 39.914 1.00 12.60 ? 241 ALA A O 1 ATOM 1904 C CB . ALA A 1 241 ? 14.063 4.042 40.600 1.00 11.82 ? 241 ALA A CB 1 ATOM 1905 N N . LEU A 1 242 ? 11.185 4.582 41.965 1.00 12.88 ? 242 LEU A N 1 ATOM 1906 C CA . LEU A 1 242 ? 9.953 4.014 42.514 1.00 12.86 ? 242 LEU A CA 1 ATOM 1907 C C . LEU A 1 242 ? 9.201 5.023 43.375 1.00 13.64 ? 242 LEU A C 1 ATOM 1908 O O . LEU A 1 242 ? 9.819 5.813 44.096 1.00 13.15 ? 242 LEU A O 1 ATOM 1909 C CB . LEU A 1 242 ? 10.278 2.807 43.402 1.00 12.93 ? 242 LEU A CB 1 ATOM 1910 C CG . LEU A 1 242 ? 10.975 1.572 42.837 1.00 12.60 ? 242 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 242 ? 11.453 0.681 43.985 1.00 11.02 ? 242 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 242 ? 10.013 0.832 41.928 1.00 12.76 ? 242 LEU A CD2 1 ATOM 1913 N N . LEU A 1 243 ? 7.870 4.969 43.315 1.00 13.36 ? 243 LEU A N 1 ATOM 1914 C CA . LEU A 1 243 ? 7.013 5.844 44.112 1.00 14.23 ? 243 LEU A CA 1 ATOM 1915 C C . LEU A 1 243 ? 6.284 5.048 45.184 1.00 13.85 ? 243 LEU A C 1 ATOM 1916 O O . LEU A 1 243 ? 5.846 3.925 44.949 1.00 12.61 ? 243 LEU A O 1 ATOM 1917 C CB . LEU A 1 243 ? 5.953 6.534 43.250 1.00 14.86 ? 243 LEU A CB 1 ATOM 1918 C CG . LEU A 1 243 ? 6.332 7.671 42.305 1.00 15.18 ? 243 LEU A CG 1 ATOM 1919 C CD1 . LEU A 1 243 ? 5.075 8.090 41.556 1.00 16.78 ? 243 LEU A CD1 1 ATOM 1920 C CD2 . LEU A 1 243 ? 6.928 8.842 43.075 1.00 12.51 ? 243 LEU A CD2 1 ATOM 1921 N N . LYS A 1 244 ? 6.161 5.641 46.363 1.00 14.26 ? 244 LYS A N 1 ATOM 1922 C CA . LYS A 1 244 ? 5.445 5.005 47.452 1.00 15.73 ? 244 LYS A CA 1 ATOM 1923 C C . LYS A 1 244 ? 3.986 5.414 47.294 1.00 16.36 ? 244 LYS A C 1 ATOM 1924 O O . LYS A 1 244 ? 3.699 6.530 46.865 1.00 15.88 ? 244 LYS A O 1 ATOM 1925 C CB . LYS A 1 244 ? 5.960 5.510 48.796 1.00 16.80 ? 244 LYS A CB 1 ATOM 1926 C CG . LYS A 1 244 ? 5.332 4.815 49.988 1.00 17.40 ? 244 LYS A CG 1 ATOM 1927 C CD . LYS A 1 244 ? 5.886 5.352 51.280 1.00 17.48 ? 244 LYS A CD 1 ATOM 1928 C CE . LYS A 1 244 ? 5.389 4.534 52.451 1.00 21.39 ? 244 LYS A CE 1 ATOM 1929 N NZ . LYS A 1 244 ? 6.049 4.963 53.718 1.00 24.38 ? 244 LYS A NZ 1 ATOM 1930 N N . PHE A 1 245 ? 3.063 4.517 47.612 1.00 16.76 ? 245 PHE A N 1 ATOM 1931 C CA . PHE A 1 245 ? 1.659 4.868 47.511 1.00 19.73 ? 245 PHE A CA 1 ATOM 1932 C C . PHE A 1 245 ? 1.253 5.521 48.829 1.00 20.99 ? 245 PHE A C 1 ATOM 1933 O O . PHE A 1 245 ? 1.069 4.836 49.826 1.00 21.60 ? 245 PHE A O 1 ATOM 1934 C CB . PHE A 1 245 ? 0.801 3.626 47.261 1.00 20.69 ? 245 PHE A CB 1 ATOM 1935 C CG . PHE A 1 245 ? -0.576 3.946 46.744 1.00 23.49 ? 245 PHE A CG 1 ATOM 1936 C CD1 . PHE A 1 245 ? -1.449 4.736 47.491 1.00 24.32 ? 245 PHE A CD1 1 ATOM 1937 C CD2 . PHE A 1 245 ? -0.978 3.511 45.487 1.00 22.72 ? 245 PHE A CD2 1 ATOM 1938 C CE1 . PHE A 1 245 ? -2.699 5.094 46.989 1.00 23.91 ? 245 PHE A CE1 1 ATOM 1939 C CE2 . PHE A 1 245 ? -2.222 3.862 44.977 1.00 24.27 ? 245 PHE A CE2 1 ATOM 1940 C CZ . PHE A 1 245 ? -3.085 4.657 45.729 1.00 23.92 ? 245 PHE A CZ 1 ATOM 1941 N N . VAL A 1 246 ? 1.125 6.845 48.834 1.00 23.27 ? 246 VAL A N 1 ATOM 1942 C CA . VAL A 1 246 ? 0.749 7.572 50.047 1.00 25.45 ? 246 VAL A CA 1 ATOM 1943 C C . VAL A 1 246 ? -0.698 8.080 49.993 1.00 29.03 ? 246 VAL A C 1 ATOM 1944 O O . VAL A 1 246 ? -1.069 8.854 49.110 1.00 27.90 ? 246 VAL A O 1 ATOM 1945 C CB . VAL A 1 246 ? 1.695 8.768 50.288 1.00 23.65 ? 246 VAL A CB 1 ATOM 1946 C CG1 . VAL A 1 246 ? 1.345 9.458 51.603 1.00 22.54 ? 246 VAL A CG1 1 ATOM 1947 C CG2 . VAL A 1 246 ? 3.136 8.288 50.309 1.00 23.36 ? 246 VAL A CG2 1 ATOM 1948 N N . ASP A 1 247 ? -1.501 7.645 50.961 1.00 34.08 ? 247 ASP A N 1 ATOM 1949 C CA . ASP A 1 247 ? -2.912 8.013 51.046 1.00 38.86 ? 247 ASP A CA 1 ATOM 1950 C C . ASP A 1 247 ? -3.198 9.442 51.474 1.00 41.38 ? 247 ASP A C 1 ATOM 1951 O O . ASP A 1 247 ? -3.670 10.258 50.685 1.00 41.97 ? 247 ASP A O 1 ATOM 1952 C CB . ASP A 1 247 ? -3.635 7.079 52.008 1.00 40.87 ? 247 ASP A CB 1 ATOM 1953 C CG . ASP A 1 247 ? -4.670 6.238 51.318 1.00 43.40 ? 247 ASP A CG 1 ATOM 1954 O OD1 . ASP A 1 247 ? -5.395 6.790 50.467 1.00 46.03 ? 247 ASP A OD1 1 ATOM 1955 O OD2 . ASP A 1 247 ? -4.768 5.032 51.629 1.00 46.51 ? 247 ASP A OD2 1 ATOM 1956 N N . LYS A 1 248 ? -2.946 9.728 52.744 1.00 45.04 ? 248 LYS A N 1 ATOM 1957 C CA . LYS A 1 248 ? -3.185 11.058 53.279 1.00 48.51 ? 248 LYS A CA 1 ATOM 1958 C C . LYS A 1 248 ? -1.927 11.891 53.117 1.00 50.23 ? 248 LYS A C 1 ATOM 1959 O O . LYS A 1 248 ? -0.835 11.357 52.914 1.00 49.61 ? 248 LYS A O 1 ATOM 1960 C CB . LYS A 1 248 ? -3.548 10.988 54.767 1.00 50.02 ? 248 LYS A CB 1 ATOM 1961 C CG . LYS A 1 248 ? -4.771 10.153 55.106 1.00 52.48 ? 248 LYS A CG 1 ATOM 1962 C CD . LYS A 1 248 ? -5.027 10.177 56.614 1.00 54.25 ? 248 LYS A CD 1 ATOM 1963 C CE . LYS A 1 248 ? -6.277 9.385 56.993 1.00 56.40 ? 248 LYS A CE 1 ATOM 1964 N NZ . LYS A 1 248 ? -6.606 9.465 58.452 1.00 55.27 ? 248 LYS A NZ 1 ATOM 1965 N N . ASP A 1 249 ? -2.086 13.204 53.211 1.00 52.91 ? 249 ASP A N 1 ATOM 1966 C CA . ASP A 1 249 ? -0.958 14.104 53.090 1.00 56.18 ? 249 ASP A CA 1 ATOM 1967 C C . ASP A 1 249 ? 0.013 13.778 54.224 1.00 58.37 ? 249 ASP A C 1 ATOM 1968 O O . ASP A 1 249 ? -0.334 13.902 55.400 1.00 58.07 ? 249 ASP A O 1 ATOM 1969 C CB . ASP A 1 249 ? -1.435 15.549 53.212 1.00 57.28 ? 249 ASP A CB 1 ATOM 1970 C CG . ASP A 1 249 ? -0.444 16.536 52.642 1.00 58.86 ? 249 ASP A CG 1 ATOM 1971 O OD1 . ASP A 1 249 ? 0.769 16.390 52.915 1.00 58.82 ? 249 ASP A OD1 1 ATOM 1972 O OD2 . ASP A 1 249 ? -0.884 17.461 51.925 1.00 60.27 ? 249 ASP A OD2 1 ATOM 1973 N N . PRO A 1 250 ? 1.240 13.343 53.887 1.00 60.96 ? 250 PRO A N 1 ATOM 1974 C CA . PRO A 1 250 ? 2.253 13.000 54.891 1.00 63.53 ? 250 PRO A CA 1 ATOM 1975 C C . PRO A 1 250 ? 2.957 14.231 55.459 1.00 66.27 ? 250 PRO A C 1 ATOM 1976 O O . PRO A 1 250 ? 3.078 15.256 54.784 1.00 66.95 ? 250 PRO A O 1 ATOM 1977 C CB . PRO A 1 250 ? 3.209 12.109 54.110 1.00 62.78 ? 250 PRO A CB 1 ATOM 1978 C CG . PRO A 1 250 ? 3.221 12.779 52.774 1.00 62.14 ? 250 PRO A CG 1 ATOM 1979 C CD . PRO A 1 250 ? 1.742 13.063 52.529 1.00 61.69 ? 250 PRO A CD 1 ATOM 1980 N N . LYS A 1 251 ? 3.417 14.122 56.703 1.00 69.13 ? 251 LYS A N 1 ATOM 1981 C CA . LYS A 1 251 ? 4.126 15.213 57.371 1.00 71.14 ? 251 LYS A CA 1 ATOM 1982 C C . LYS A 1 251 ? 4.435 14.844 58.820 1.00 71.71 ? 251 LYS A C 1 ATOM 1983 O O . LYS A 1 251 ? 3.552 14.216 59.447 1.00 72.37 ? 251 LYS A O 1 ATOM 1984 C CB . LYS A 1 251 ? 3.295 16.502 57.339 1.00 71.37 ? 251 LYS A CB 1 ATOM 1985 C CG . LYS A 1 251 ? 4.056 17.727 57.816 1.00 72.17 ? 251 LYS A CG 1 ATOM 1986 C CD . LYS A 1 251 ? 3.167 18.955 57.850 1.00 73.13 ? 251 LYS A CD 1 ATOM 1987 C CE . LYS A 1 251 ? 3.939 20.174 58.340 1.00 74.11 ? 251 LYS A CE 1 ATOM 1988 N NZ . LYS A 1 251 ? 3.075 21.385 58.465 1.00 74.34 ? 251 LYS A NZ 1 ATOM 1989 N N . GLY B 1 1 ? 34.358 -11.326 15.675 1.00 48.18 ? 1 GLY B N 1 ATOM 1990 C CA . GLY B 1 1 ? 34.301 -9.980 15.036 1.00 46.59 ? 1 GLY B CA 1 ATOM 1991 C C . GLY B 1 1 ? 33.870 -8.885 15.996 1.00 45.42 ? 1 GLY B C 1 ATOM 1992 O O . GLY B 1 1 ? 34.470 -8.699 17.060 1.00 46.16 ? 1 GLY B O 1 ATOM 1993 N N . LEU B 1 2 ? 32.826 -8.156 15.615 1.00 42.54 ? 2 LEU B N 1 ATOM 1994 C CA . LEU B 1 2 ? 32.304 -7.071 16.436 1.00 39.86 ? 2 LEU B CA 1 ATOM 1995 C C . LEU B 1 2 ? 31.222 -7.598 17.374 1.00 38.43 ? 2 LEU B C 1 ATOM 1996 O O . LEU B 1 2 ? 30.512 -8.548 17.037 1.00 37.99 ? 2 LEU B O 1 ATOM 1997 C CB . LEU B 1 2 ? 31.689 -5.991 15.543 1.00 40.04 ? 2 LEU B CB 1 ATOM 1998 C CG . LEU B 1 2 ? 32.545 -5.338 14.458 1.00 40.32 ? 2 LEU B CG 1 ATOM 1999 C CD1 . LEU B 1 2 ? 31.670 -4.384 13.659 1.00 39.39 ? 2 LEU B CD1 1 ATOM 2000 C CD2 . LEU B 1 2 ? 33.724 -4.600 15.084 1.00 39.00 ? 2 LEU B CD2 1 ATOM 2001 N N . ASP B 1 3 ? 31.087 -6.983 18.547 1.00 35.83 ? 3 ASP B N 1 ATOM 2002 C CA . ASP B 1 3 ? 30.050 -7.397 19.487 1.00 34.10 ? 3 ASP B CA 1 ATOM 2003 C C . ASP B 1 3 ? 28.709 -6.837 19.020 1.00 31.36 ? 3 ASP B C 1 ATOM 2004 O O . ASP B 1 3 ? 28.649 -5.804 18.348 1.00 30.03 ? 3 ASP B O 1 ATOM 2005 C CB . ASP B 1 3 ? 30.353 -6.892 20.904 1.00 36.77 ? 3 ASP B CB 1 ATOM 2006 C CG . ASP B 1 3 ? 31.566 -7.574 21.523 1.00 39.71 ? 3 ASP B CG 1 ATOM 2007 O OD1 . ASP B 1 3 ? 31.592 -8.825 21.560 1.00 40.13 ? 3 ASP B OD1 1 ATOM 2008 O OD2 . ASP B 1 3 ? 32.490 -6.861 21.974 1.00 40.90 ? 3 ASP B OD2 1 ATOM 2009 N N . THR B 1 4 ? 27.632 -7.530 19.360 1.00 28.34 ? 4 THR B N 1 ATOM 2010 C CA . THR B 1 4 ? 26.312 -7.074 18.976 1.00 26.93 ? 4 THR B CA 1 ATOM 2011 C C . THR B 1 4 ? 25.373 -7.068 20.171 1.00 24.43 ? 4 THR B C 1 ATOM 2012 O O . THR B 1 4 ? 25.275 -8.048 20.901 1.00 24.02 ? 4 THR B O 1 ATOM 2013 C CB . THR B 1 4 ? 25.708 -7.961 17.866 1.00 28.20 ? 4 THR B CB 1 ATOM 2014 O OG1 . THR B 1 4 ? 26.579 -7.960 16.729 1.00 29.88 ? 4 THR B OG1 1 ATOM 2015 C CG2 . THR B 1 4 ? 24.340 -7.429 17.440 1.00 27.49 ? 4 THR B CG2 1 ATOM 2016 N N . VAL B 1 5 ? 24.698 -5.943 20.368 1.00 22.27 ? 5 VAL B N 1 ATOM 2017 C CA . VAL B 1 5 ? 23.741 -5.795 21.452 1.00 20.99 ? 5 VAL B CA 1 ATOM 2018 C C . VAL B 1 5 ? 22.393 -5.612 20.775 1.00 20.33 ? 5 VAL B C 1 ATOM 2019 O O . VAL B 1 5 ? 22.254 -4.797 19.864 1.00 20.53 ? 5 VAL B O 1 ATOM 2020 C CB . VAL B 1 5 ? 24.076 -4.567 22.336 1.00 21.52 ? 5 VAL B CB 1 ATOM 2021 C CG1 . VAL B 1 5 ? 23.050 -4.425 23.451 1.00 21.22 ? 5 VAL B CG1 1 ATOM 2022 C CG2 . VAL B 1 5 ? 25.467 -4.727 22.937 1.00 21.41 ? 5 VAL B CG2 1 ATOM 2023 N N . SER B 1 6 ? 21.403 -6.381 21.209 1.00 20.18 ? 6 SER B N 1 ATOM 2024 C CA . SER B 1 6 ? 20.073 -6.314 20.614 1.00 20.76 ? 6 SER B CA 1 ATOM 2025 C C . SER B 1 6 ? 19.030 -5.702 21.529 1.00 19.52 ? 6 SER B C 1 ATOM 2026 O O . SER B 1 6 ? 19.175 -5.718 22.751 1.00 19.22 ? 6 SER B O 1 ATOM 2027 C CB . SER B 1 6 ? 19.599 -7.719 20.231 1.00 21.66 ? 6 SER B CB 1 ATOM 2028 O OG . SER B 1 6 ? 20.516 -8.356 19.363 1.00 26.72 ? 6 SER B OG 1 ATOM 2029 N N . PHE B 1 7 ? 17.976 -5.172 20.917 1.00 18.54 ? 7 PHE B N 1 ATOM 2030 C CA . PHE B 1 7 ? 16.851 -4.592 21.643 1.00 19.24 ? 7 PHE B CA 1 ATOM 2031 C C . PHE B 1 7 ? 15.583 -4.701 20.792 1.00 19.67 ? 7 PHE B C 1 ATOM 2032 O O . PHE B 1 7 ? 15.572 -4.306 19.623 1.00 20.58 ? 7 PHE B O 1 ATOM 2033 C CB . PHE B 1 7 ? 17.097 -3.117 21.993 1.00 17.93 ? 7 PHE B CB 1 ATOM 2034 C CG . PHE B 1 7 ? 15.944 -2.477 22.726 1.00 17.55 ? 7 PHE B CG 1 ATOM 2035 C CD1 . PHE B 1 7 ? 15.601 -2.895 24.013 1.00 18.30 ? 7 PHE B CD1 1 ATOM 2036 C CD2 . PHE B 1 7 ? 15.170 -1.491 22.118 1.00 16.58 ? 7 PHE B CD2 1 ATOM 2037 C CE1 . PHE B 1 7 ? 14.498 -2.341 24.684 1.00 16.98 ? 7 PHE B CE1 1 ATOM 2038 C CE2 . PHE B 1 7 ? 14.064 -0.933 22.782 1.00 16.42 ? 7 PHE B CE2 1 ATOM 2039 C CZ . PHE B 1 7 ? 13.731 -1.361 24.066 1.00 15.44 ? 7 PHE B CZ 1 ATOM 2040 N N . SER B 1 8 ? 14.522 -5.248 21.375 1.00 20.14 ? 8 SER B N 1 ATOM 2041 C CA . SER B 1 8 ? 13.253 -5.382 20.668 1.00 21.48 ? 8 SER B CA 1 ATOM 2042 C C . SER B 1 8 ? 12.222 -4.466 21.298 1.00 21.34 ? 8 SER B C 1 ATOM 2043 O O . SER B 1 8 ? 12.180 -4.313 22.518 1.00 20.74 ? 8 SER B O 1 ATOM 2044 C CB . SER B 1 8 ? 12.731 -6.817 20.727 1.00 22.14 ? 8 SER B CB 1 ATOM 2045 O OG . SER B 1 8 ? 11.415 -6.866 20.193 1.00 23.42 ? 8 SER B OG 1 ATOM 2046 N N . THR B 1 9 ? 11.388 -3.858 20.464 1.00 21.63 ? 9 THR B N 1 ATOM 2047 C CA . THR B 1 9 ? 10.367 -2.958 20.967 1.00 22.53 ? 9 THR B CA 1 ATOM 2048 C C . THR B 1 9 ? 9.103 -3.732 21.321 1.00 23.19 ? 9 THR B C 1 ATOM 2049 O O . THR B 1 9 ? 8.234 -3.220 22.027 1.00 23.94 ? 9 THR B O 1 ATOM 2050 C CB . THR B 1 9 ? 10.020 -1.872 19.930 1.00 22.21 ? 9 THR B CB 1 ATOM 2051 O OG1 . THR B 1 9 ? 9.494 -2.488 18.751 1.00 23.53 ? 9 THR B OG1 1 ATOM 2052 C CG2 . THR B 1 9 ? 11.260 -1.072 19.559 1.00 23.46 ? 9 THR B CG2 1 ATOM 2053 N N . LYS B 1 10 ? 9.007 -4.970 20.842 1.00 24.74 ? 10 LYS B N 1 ATOM 2054 C CA . LYS B 1 10 ? 7.834 -5.804 21.106 1.00 24.76 ? 10 LYS B CA 1 ATOM 2055 C C . LYS B 1 10 ? 7.789 -6.216 22.571 1.00 23.54 ? 10 LYS B C 1 ATOM 2056 O O . LYS B 1 10 ? 8.624 -6.993 23.033 1.00 23.05 ? 10 LYS B O 1 ATOM 2057 C CB . LYS B 1 10 ? 7.860 -7.048 20.218 1.00 27.02 ? 10 LYS B CB 1 ATOM 2058 C CG . LYS B 1 10 ? 6.493 -7.683 19.993 1.00 31.87 ? 10 LYS B CG 1 ATOM 2059 C CD . LYS B 1 10 ? 6.538 -8.599 18.771 1.00 37.68 ? 10 LYS B CD 1 ATOM 2060 C CE . LYS B 1 10 ? 5.152 -8.832 18.167 1.00 41.42 ? 10 LYS B CE 1 ATOM 2061 N NZ . LYS B 1 10 ? 5.215 -9.512 16.826 1.00 43.69 ? 10 LYS B NZ 1 ATOM 2062 N N . GLY B 1 11 ? 6.815 -5.683 23.299 1.00 23.10 ? 11 GLY B N 1 ATOM 2063 C CA . GLY B 1 11 ? 6.692 -6.001 24.709 1.00 22.45 ? 11 GLY B CA 1 ATOM 2064 C C . GLY B 1 11 ? 7.769 -5.323 25.536 1.00 21.99 ? 11 GLY B C 1 ATOM 2065 O O . GLY B 1 11 ? 8.085 -5.755 26.645 1.00 22.36 ? 11 GLY B O 1 ATOM 2066 N N . ALA B 1 12 ? 8.342 -4.254 24.997 1.00 20.53 ? 12 ALA B N 1 ATOM 2067 C CA . ALA B 1 12 ? 9.389 -3.538 25.706 1.00 19.48 ? 12 ALA B CA 1 ATOM 2068 C C . ALA B 1 12 ? 8.820 -2.783 26.900 1.00 19.07 ? 12 ALA B C 1 ATOM 2069 O O . ALA B 1 12 ? 7.682 -2.299 26.870 1.00 18.19 ? 12 ALA B O 1 ATOM 2070 C CB . ALA B 1 12 ? 10.099 -2.569 24.758 1.00 18.01 ? 12 ALA B CB 1 ATOM 2071 N N . THR B 1 13 ? 9.618 -2.702 27.959 1.00 18.40 ? 13 THR B N 1 ATOM 2072 C CA . THR B 1 13 ? 9.230 -1.985 29.169 1.00 17.59 ? 13 THR B CA 1 ATOM 2073 C C . THR B 1 13 ? 10.395 -1.095 29.558 1.00 17.38 ? 13 THR B C 1 ATOM 2074 O O . THR B 1 13 ? 11.496 -1.228 29.014 1.00 16.17 ? 13 THR B O 1 ATOM 2075 C CB . THR B 1 13 ? 8.954 -2.932 30.348 1.00 17.44 ? 13 THR B CB 1 ATOM 2076 O OG1 . THR B 1 13 ? 10.186 -3.518 30.791 1.00 17.10 ? 13 THR B OG1 1 ATOM 2077 C CG2 . THR B 1 13 ? 7.981 -4.022 29.933 1.00 14.87 ? 13 THR B CG2 1 ATOM 2078 N N . TYR B 1 14 ? 10.155 -0.197 30.504 1.00 16.59 ? 14 TYR B N 1 ATOM 2079 C CA . TYR B 1 14 ? 11.198 0.702 30.952 1.00 17.23 ? 14 TYR B CA 1 ATOM 2080 C C . TYR B 1 14 ? 12.398 -0.109 31.456 1.00 16.76 ? 14 TYR B C 1 ATOM 2081 O O . TYR B 1 14 ? 13.537 0.356 31.409 1.00 17.04 ? 14 TYR B O 1 ATOM 2082 C CB . TYR B 1 14 ? 10.652 1.608 32.051 1.00 16.70 ? 14 TYR B CB 1 ATOM 2083 C CG . TYR B 1 14 ? 10.250 0.868 33.302 1.00 17.15 ? 14 TYR B CG 1 ATOM 2084 C CD1 . TYR B 1 14 ? 11.055 0.895 34.440 1.00 17.21 ? 14 TYR B CD1 1 ATOM 2085 C CD2 . TYR B 1 14 ? 9.071 0.133 33.347 1.00 17.08 ? 14 TYR B CD2 1 ATOM 2086 C CE1 . TYR B 1 14 ? 10.687 0.208 35.593 1.00 18.43 ? 14 TYR B CE1 1 ATOM 2087 C CE2 . TYR B 1 14 ? 8.697 -0.558 34.489 1.00 17.00 ? 14 TYR B CE2 1 ATOM 2088 C CZ . TYR B 1 14 ? 9.505 -0.516 35.608 1.00 18.08 ? 14 TYR B CZ 1 ATOM 2089 O OH . TYR B 1 14 ? 9.129 -1.197 36.742 1.00 16.90 ? 14 TYR B OH 1 ATOM 2090 N N . ILE B 1 15 ? 12.137 -1.327 31.922 1.00 16.52 ? 15 ILE B N 1 ATOM 2091 C CA . ILE B 1 15 ? 13.192 -2.202 32.428 1.00 16.24 ? 15 ILE B CA 1 ATOM 2092 C C . ILE B 1 15 ? 14.038 -2.874 31.335 1.00 15.27 ? 15 ILE B C 1 ATOM 2093 O O . ILE B 1 15 ? 15.268 -2.911 31.441 1.00 15.58 ? 15 ILE B O 1 ATOM 2094 C CB . ILE B 1 15 ? 12.599 -3.273 33.381 1.00 17.38 ? 15 ILE B CB 1 ATOM 2095 C CG1 . ILE B 1 15 ? 12.366 -2.651 34.756 1.00 18.66 ? 15 ILE B CG1 1 ATOM 2096 C CG2 . ILE B 1 15 ? 13.523 -4.471 33.488 1.00 19.47 ? 15 ILE B CG2 1 ATOM 2097 C CD1 . ILE B 1 15 ? 13.625 -2.067 35.394 1.00 20.46 ? 15 ILE B CD1 1 ATOM 2098 N N . THR B 1 16 ? 13.410 -3.401 30.285 1.00 15.91 ? 16 THR B N 1 ATOM 2099 C CA . THR B 1 16 ? 14.196 -4.033 29.219 1.00 15.21 ? 16 THR B CA 1 ATOM 2100 C C . THR B 1 16 ? 15.049 -2.972 28.518 1.00 15.25 ? 16 THR B C 1 ATOM 2101 O O . THR B 1 16 ? 16.148 -3.262 28.037 1.00 15.29 ? 16 THR B O 1 ATOM 2102 C CB . THR B 1 16 ? 13.310 -4.754 28.161 1.00 16.33 ? 16 THR B CB 1 ATOM 2103 O OG1 . THR B 1 16 ? 12.501 -3.800 27.462 1.00 17.49 ? 16 THR B OG1 1 ATOM 2104 C CG2 . THR B 1 16 ? 12.416 -5.786 28.827 1.00 13.68 ? 16 THR B CG2 1 ATOM 2105 N N . TYR B 1 17 ? 14.546 -1.739 28.478 1.00 14.71 ? 17 TYR B N 1 ATOM 2106 C CA . TYR B 1 17 ? 15.270 -0.627 27.859 1.00 13.72 ? 17 TYR B CA 1 ATOM 2107 C C . TYR B 1 17 ? 16.549 -0.314 28.656 1.00 13.73 ? 17 TYR B C 1 ATOM 2108 O O . TYR B 1 17 ? 17.641 -0.211 28.091 1.00 14.11 ? 17 TYR B O 1 ATOM 2109 C CB . TYR B 1 17 ? 14.373 0.618 27.802 1.00 13.35 ? 17 TYR B CB 1 ATOM 2110 C CG . TYR B 1 17 ? 15.088 1.878 27.363 1.00 12.53 ? 17 TYR B CG 1 ATOM 2111 C CD1 . TYR B 1 17 ? 15.578 2.011 26.062 1.00 12.79 ? 17 TYR B CD1 1 ATOM 2112 C CD2 . TYR B 1 17 ? 15.306 2.927 28.262 1.00 13.72 ? 17 TYR B CD2 1 ATOM 2113 C CE1 . TYR B 1 17 ? 16.272 3.157 25.664 1.00 12.34 ? 17 TYR B CE1 1 ATOM 2114 C CE2 . TYR B 1 17 ? 16.001 4.076 27.875 1.00 13.77 ? 17 TYR B CE2 1 ATOM 2115 C CZ . TYR B 1 17 ? 16.480 4.179 26.576 1.00 12.10 ? 17 TYR B CZ 1 ATOM 2116 O OH . TYR B 1 17 ? 17.184 5.293 26.195 1.00 14.24 ? 17 TYR B OH 1 ATOM 2117 N N . VAL B 1 18 ? 16.403 -0.169 29.968 1.00 13.75 ? 18 VAL B N 1 ATOM 2118 C CA . VAL B 1 18 ? 17.529 0.128 30.846 1.00 14.76 ? 18 VAL B CA 1 ATOM 2119 C C . VAL B 1 18 ? 18.548 -1.014 30.898 1.00 15.33 ? 18 VAL B C 1 ATOM 2120 O O . VAL B 1 18 ? 19.754 -0.770 30.954 1.00 15.77 ? 18 VAL B O 1 ATOM 2121 C CB . VAL B 1 18 ? 17.033 0.467 32.279 1.00 15.86 ? 18 VAL B CB 1 ATOM 2122 C CG1 . VAL B 1 18 ? 18.199 0.482 33.252 1.00 17.60 ? 18 VAL B CG1 1 ATOM 2123 C CG2 . VAL B 1 18 ? 16.352 1.833 32.275 1.00 13.85 ? 18 VAL B CG2 1 ATOM 2124 N N . ASN B 1 19 ? 18.078 -2.257 30.884 1.00 15.23 ? 19 ASN B N 1 ATOM 2125 C CA . ASN B 1 19 ? 19.006 -3.388 30.903 1.00 16.57 ? 19 ASN B CA 1 ATOM 2126 C C . ASN B 1 19 ? 19.787 -3.397 29.578 1.00 17.13 ? 19 ASN B C 1 ATOM 2127 O O . ASN B 1 19 ? 20.968 -3.759 29.533 1.00 16.33 ? 19 ASN B O 1 ATOM 2128 C CB . ASN B 1 19 ? 18.241 -4.701 31.099 1.00 17.60 ? 19 ASN B CB 1 ATOM 2129 C CG . ASN B 1 19 ? 17.734 -4.878 32.529 1.00 19.79 ? 19 ASN B CG 1 ATOM 2130 O OD1 . ASN B 1 19 ? 16.788 -5.633 32.779 1.00 22.56 ? 19 ASN B OD1 1 ATOM 2131 N ND2 . ASN B 1 19 ? 18.371 -4.193 33.474 1.00 19.36 ? 19 ASN B ND2 1 ATOM 2132 N N . PHE B 1 20 ? 19.120 -2.980 28.505 1.00 17.08 ? 20 PHE B N 1 ATOM 2133 C CA . PHE B 1 20 ? 19.751 -2.897 27.189 1.00 17.02 ? 20 PHE B CA 1 ATOM 2134 C C . PHE B 1 20 ? 20.909 -1.888 27.213 1.00 15.94 ? 20 PHE B C 1 ATOM 2135 O O . PHE B 1 20 ? 22.014 -2.194 26.757 1.00 14.78 ? 20 PHE B O 1 ATOM 2136 C CB . PHE B 1 20 ? 18.716 -2.467 26.141 1.00 18.14 ? 20 PHE B CB 1 ATOM 2137 C CG . PHE B 1 20 ? 19.310 -1.745 24.955 1.00 21.74 ? 20 PHE B CG 1 ATOM 2138 C CD1 . PHE B 1 20 ? 20.172 -2.401 24.075 1.00 22.98 ? 20 PHE B CD1 1 ATOM 2139 C CD2 . PHE B 1 20 ? 19.024 -0.400 24.729 1.00 21.95 ? 20 PHE B CD2 1 ATOM 2140 C CE1 . PHE B 1 20 ? 20.744 -1.722 22.984 1.00 23.81 ? 20 PHE B CE1 1 ATOM 2141 C CE2 . PHE B 1 20 ? 19.588 0.286 23.645 1.00 22.33 ? 20 PHE B CE2 1 ATOM 2142 C CZ . PHE B 1 20 ? 20.450 -0.379 22.772 1.00 22.41 ? 20 PHE B CZ 1 ATOM 2143 N N . LEU B 1 21 ? 20.647 -0.690 27.742 1.00 15.12 ? 21 LEU B N 1 ATOM 2144 C CA . LEU B 1 21 ? 21.661 0.365 27.820 1.00 14.19 ? 21 LEU B CA 1 ATOM 2145 C C . LEU B 1 21 ? 22.889 -0.047 28.622 1.00 14.47 ? 21 LEU B C 1 ATOM 2146 O O . LEU B 1 21 ? 24.008 0.327 28.284 1.00 14.92 ? 21 LEU B O 1 ATOM 2147 C CB . LEU B 1 21 ? 21.077 1.633 28.441 1.00 13.61 ? 21 LEU B CB 1 ATOM 2148 C CG . LEU B 1 21 ? 20.036 2.431 27.657 1.00 13.91 ? 21 LEU B CG 1 ATOM 2149 C CD1 . LEU B 1 21 ? 19.610 3.637 28.492 1.00 14.28 ? 21 LEU B CD1 1 ATOM 2150 C CD2 . LEU B 1 21 ? 20.621 2.887 26.332 1.00 11.82 ? 21 LEU B CD2 1 ATOM 2151 N N . ASN B 1 22 ? 22.688 -0.808 29.692 1.00 14.23 ? 22 ASN B N 1 ATOM 2152 C CA . ASN B 1 22 ? 23.820 -1.239 30.492 1.00 15.66 ? 22 ASN B CA 1 ATOM 2153 C C . ASN B 1 22 ? 24.589 -2.344 29.799 1.00 16.21 ? 22 ASN B C 1 ATOM 2154 O O . ASN B 1 22 ? 25.778 -2.540 30.047 1.00 17.74 ? 22 ASN B O 1 ATOM 2155 C CB . ASN B 1 22 ? 23.361 -1.672 31.876 1.00 14.43 ? 22 ASN B CB 1 ATOM 2156 C CG . ASN B 1 22 ? 23.042 -0.492 32.751 1.00 14.22 ? 22 ASN B CG 1 ATOM 2157 O OD1 . ASN B 1 22 ? 23.850 0.436 32.860 1.00 13.96 ? 22 ASN B OD1 1 ATOM 2158 N ND2 . ASN B 1 22 ? 21.865 -0.506 33.378 1.00 15.70 ? 22 ASN B ND2 1 ATOM 2159 N N . GLU B 1 23 ? 23.913 -3.055 28.910 1.00 16.65 ? 23 GLU B N 1 ATOM 2160 C CA . GLU B 1 23 ? 24.563 -4.113 28.154 1.00 18.33 ? 23 GLU B CA 1 ATOM 2161 C C . GLU B 1 23 ? 25.504 -3.429 27.150 1.00 16.88 ? 23 GLU B C 1 ATOM 2162 O O . GLU B 1 23 ? 26.636 -3.865 26.928 1.00 16.03 ? 23 GLU B O 1 ATOM 2163 C CB . GLU B 1 23 ? 23.509 -4.925 27.418 1.00 22.93 ? 23 GLU B CB 1 ATOM 2164 C CG . GLU B 1 23 ? 23.952 -6.309 27.040 1.00 31.53 ? 23 GLU B CG 1 ATOM 2165 C CD . GLU B 1 23 ? 22.960 -6.989 26.123 1.00 35.75 ? 23 GLU B CD 1 ATOM 2166 O OE1 . GLU B 1 23 ? 21.742 -6.965 26.436 1.00 35.83 ? 23 GLU B OE1 1 ATOM 2167 O OE2 . GLU B 1 23 ? 23.410 -7.546 25.094 1.00 38.55 ? 23 GLU B OE2 1 ATOM 2168 N N . LEU B 1 24 ? 25.017 -2.340 26.563 1.00 14.66 ? 24 LEU B N 1 ATOM 2169 C CA . LEU B 1 24 ? 25.773 -1.559 25.592 1.00 14.46 ? 24 LEU B CA 1 ATOM 2170 C C . LEU B 1 24 ? 26.982 -0.881 26.234 1.00 13.77 ? 24 LEU B C 1 ATOM 2171 O O . LEU B 1 24 ? 28.071 -0.870 25.661 1.00 15.77 ? 24 LEU B O 1 ATOM 2172 C CB . LEU B 1 24 ? 24.863 -0.497 24.950 1.00 12.77 ? 24 LEU B CB 1 ATOM 2173 C CG . LEU B 1 24 ? 25.532 0.522 24.022 1.00 12.14 ? 24 LEU B CG 1 ATOM 2174 C CD1 . LEU B 1 24 ? 26.176 -0.200 22.841 1.00 12.79 ? 24 LEU B CD1 1 ATOM 2175 C CD2 . LEU B 1 24 ? 24.503 1.535 23.545 1.00 10.79 ? 24 LEU B CD2 1 ATOM 2176 N N . ARG B 1 25 ? 26.789 -0.313 27.420 1.00 13.06 ? 25 ARG B N 1 ATOM 2177 C CA . ARG B 1 25 ? 27.868 0.362 28.132 1.00 14.34 ? 25 ARG B CA 1 ATOM 2178 C C . ARG B 1 25 ? 29.032 -0.585 28.400 1.00 15.79 ? 25 ARG B C 1 ATOM 2179 O O . ARG B 1 25 ? 30.197 -0.178 28.388 1.00 17.06 ? 25 ARG B O 1 ATOM 2180 C CB . ARG B 1 25 ? 27.341 0.941 29.453 1.00 14.25 ? 25 ARG B CB 1 ATOM 2181 C CG . ARG B 1 25 ? 26.516 2.214 29.273 1.00 13.67 ? 25 ARG B CG 1 ATOM 2182 C CD . ARG B 1 25 ? 25.633 2.523 30.476 1.00 13.20 ? 25 ARG B CD 1 ATOM 2183 N NE . ARG B 1 25 ? 24.884 3.763 30.273 1.00 14.32 ? 25 ARG B NE 1 ATOM 2184 C CZ . ARG B 1 25 ? 23.810 4.120 30.975 1.00 15.62 ? 25 ARG B CZ 1 ATOM 2185 N NH1 . ARG B 1 25 ? 23.341 3.331 31.934 1.00 14.97 ? 25 ARG B NH1 1 ATOM 2186 N NH2 . ARG B 1 25 ? 23.206 5.273 30.723 1.00 13.37 ? 25 ARG B NH2 1 ATOM 2187 N N . VAL B 1 26 ? 28.709 -1.852 28.638 1.00 17.46 ? 26 VAL B N 1 ATOM 2188 C CA . VAL B 1 26 ? 29.720 -2.875 28.898 1.00 18.97 ? 26 VAL B CA 1 ATOM 2189 C C . VAL B 1 26 ? 30.504 -3.200 27.633 1.00 19.68 ? 26 VAL B C 1 ATOM 2190 O O . VAL B 1 26 ? 31.741 -3.187 27.635 1.00 18.20 ? 26 VAL B O 1 ATOM 2191 C CB . VAL B 1 26 ? 29.080 -4.191 29.422 1.00 19.33 ? 26 VAL B CB 1 ATOM 2192 C CG1 . VAL B 1 26 ? 30.102 -5.328 29.397 1.00 18.66 ? 26 VAL B CG1 1 ATOM 2193 C CG2 . VAL B 1 26 ? 28.571 -3.990 30.834 1.00 19.44 ? 26 VAL B CG2 1 ATOM 2194 N N . LYS B 1 27 ? 29.779 -3.483 26.553 1.00 20.33 ? 27 LYS B N 1 ATOM 2195 C CA . LYS B 1 27 ? 30.417 -3.833 25.293 1.00 21.37 ? 27 LYS B CA 1 ATOM 2196 C C . LYS B 1 27 ? 31.179 -2.711 24.596 1.00 21.63 ? 27 LYS B C 1 ATOM 2197 O O . LYS B 1 27 ? 31.936 -2.966 23.666 1.00 21.38 ? 27 LYS B O 1 ATOM 2198 C CB . LYS B 1 27 ? 29.399 -4.475 24.356 1.00 22.49 ? 27 LYS B CB 1 ATOM 2199 C CG . LYS B 1 27 ? 29.010 -5.870 24.833 1.00 24.10 ? 27 LYS B CG 1 ATOM 2200 C CD . LYS B 1 27 ? 28.215 -6.619 23.789 1.00 30.48 ? 27 LYS B CD 1 ATOM 2201 C CE . LYS B 1 27 ? 27.935 -8.052 24.220 1.00 30.14 ? 27 LYS B CE 1 ATOM 2202 N NZ . LYS B 1 27 ? 27.131 -8.758 23.181 1.00 31.14 ? 27 LYS B NZ 1 ATOM 2203 N N . LEU B 1 28 ? 30.990 -1.473 25.038 1.00 21.00 ? 28 LEU B N 1 ATOM 2204 C CA . LEU B 1 28 ? 31.744 -0.363 24.461 1.00 21.46 ? 28 LEU B CA 1 ATOM 2205 C C . LEU B 1 28 ? 33.169 -0.504 25.019 1.00 22.49 ? 28 LEU B C 1 ATOM 2206 O O . LEU B 1 28 ? 34.127 0.089 24.511 1.00 22.32 ? 28 LEU B O 1 ATOM 2207 C CB . LEU B 1 28 ? 31.140 0.976 24.892 1.00 19.82 ? 28 LEU B CB 1 ATOM 2208 C CG . LEU B 1 28 ? 29.827 1.396 24.231 1.00 19.20 ? 28 LEU B CG 1 ATOM 2209 C CD1 . LEU B 1 28 ? 29.306 2.633 24.924 1.00 17.30 ? 28 LEU B CD1 1 ATOM 2210 C CD2 . LEU B 1 28 ? 30.044 1.669 22.749 1.00 16.08 ? 28 LEU B CD2 1 ATOM 2211 N N . LYS B 1 29 ? 33.276 -1.295 26.085 1.00 22.25 ? 29 LYS B N 1 ATOM 2212 C CA . LYS B 1 29 ? 34.535 -1.581 26.762 1.00 22.30 ? 29 LYS B CA 1 ATOM 2213 C C . LYS B 1 29 ? 35.425 -0.389 27.110 1.00 21.76 ? 29 LYS B C 1 ATOM 2214 O O . LYS B 1 29 ? 36.514 -0.226 26.548 1.00 22.59 ? 29 LYS B O 1 ATOM 2215 C CB . LYS B 1 29 ? 35.332 -2.602 25.945 1.00 22.42 ? 29 LYS B CB 1 ATOM 2216 C CG . LYS B 1 29 ? 34.620 -3.932 25.820 1.00 24.64 ? 29 LYS B CG 1 ATOM 2217 C CD . LYS B 1 29 ? 35.403 -4.947 25.010 1.00 27.77 ? 29 LYS B CD 1 ATOM 2218 C CE . LYS B 1 29 ? 34.575 -6.206 24.815 1.00 29.88 ? 29 LYS B CE 1 ATOM 2219 N NZ . LYS B 1 29 ? 35.299 -7.259 24.058 1.00 33.05 ? 29 LYS B NZ 1 ATOM 2220 N N . PRO B 1 30 ? 34.975 0.468 28.043 1.00 20.69 ? 30 PRO B N 1 ATOM 2221 C CA . PRO B 1 30 ? 35.801 1.620 28.419 1.00 21.22 ? 30 PRO B CA 1 ATOM 2222 C C . PRO B 1 30 ? 37.069 1.099 29.095 1.00 22.44 ? 30 PRO B C 1 ATOM 2223 O O . PRO B 1 30 ? 37.087 -0.029 29.584 1.00 22.69 ? 30 PRO B O 1 ATOM 2224 C CB . PRO B 1 30 ? 34.900 2.394 29.388 1.00 19.14 ? 30 PRO B CB 1 ATOM 2225 C CG . PRO B 1 30 ? 34.057 1.327 29.997 1.00 18.41 ? 30 PRO B CG 1 ATOM 2226 C CD . PRO B 1 30 ? 33.718 0.448 28.810 1.00 19.03 ? 30 PRO B CD 1 ATOM 2227 N N . GLU B 1 31 ? 38.134 1.889 29.109 1.00 23.36 ? 31 GLU B N 1 ATOM 2228 C CA . GLU B 1 31 ? 39.353 1.430 29.762 1.00 26.05 ? 31 GLU B CA 1 ATOM 2229 C C . GLU B 1 31 ? 39.689 2.335 30.924 1.00 24.97 ? 31 GLU B C 1 ATOM 2230 O O . GLU B 1 31 ? 40.063 3.493 30.741 1.00 26.12 ? 31 GLU B O 1 ATOM 2231 C CB . GLU B 1 31 ? 40.529 1.389 28.785 1.00 29.31 ? 31 GLU B CB 1 ATOM 2232 C CG . GLU B 1 31 ? 40.314 0.459 27.606 1.00 34.47 ? 31 GLU B CG 1 ATOM 2233 C CD . GLU B 1 31 ? 41.585 0.225 26.815 1.00 37.66 ? 31 GLU B CD 1 ATOM 2234 O OE1 . GLU B 1 31 ? 42.406 1.166 26.709 1.00 40.06 ? 31 GLU B OE1 1 ATOM 2235 O OE2 . GLU B 1 31 ? 41.754 -0.896 26.289 1.00 39.08 ? 31 GLU B OE2 1 ATOM 2236 N N . GLY B 1 32 ? 39.549 1.801 32.127 1.00 24.39 ? 32 GLY B N 1 ATOM 2237 C CA . GLY B 1 32 ? 39.838 2.598 33.298 1.00 24.32 ? 32 GLY B CA 1 ATOM 2238 C C . GLY B 1 32 ? 38.708 3.562 33.592 1.00 24.11 ? 32 GLY B C 1 ATOM 2239 O O . GLY B 1 32 ? 37.570 3.386 33.137 1.00 23.25 ? 32 GLY B O 1 ATOM 2240 N N . ASN B 1 33 ? 39.024 4.606 34.340 1.00 23.54 ? 33 ASN B N 1 ATOM 2241 C CA . ASN B 1 33 ? 38.007 5.568 34.707 1.00 22.89 ? 33 ASN B CA 1 ATOM 2242 C C . ASN B 1 33 ? 38.661 6.865 35.118 1.00 22.14 ? 33 ASN B C 1 ATOM 2243 O O . ASN B 1 33 ? 39.882 6.954 35.205 1.00 24.10 ? 33 ASN B O 1 ATOM 2244 C CB . ASN B 1 33 ? 37.217 5.021 35.888 1.00 23.32 ? 33 ASN B CB 1 ATOM 2245 C CG . ASN B 1 33 ? 38.039 4.999 37.173 1.00 24.55 ? 33 ASN B CG 1 ATOM 2246 O OD1 . ASN B 1 33 ? 38.141 6.006 37.878 1.00 25.81 ? 33 ASN B OD1 1 ATOM 2247 N ND2 . ASN B 1 33 ? 38.648 3.857 37.467 1.00 23.74 ? 33 ASN B ND2 1 ATOM 2248 N N . SER B 1 34 ? 37.834 7.870 35.362 1.00 20.64 ? 34 SER B N 1 ATOM 2249 C CA . SER B 1 34 ? 38.299 9.161 35.828 1.00 20.37 ? 34 SER B CA 1 ATOM 2250 C C . SER B 1 34 ? 37.308 9.559 36.911 1.00 20.46 ? 34 SER B C 1 ATOM 2251 O O . SER B 1 34 ? 36.117 9.761 36.643 1.00 20.65 ? 34 SER B O 1 ATOM 2252 C CB . SER B 1 34 ? 38.300 10.194 34.701 1.00 22.30 ? 34 SER B CB 1 ATOM 2253 O OG . SER B 1 34 ? 38.766 11.451 35.169 1.00 24.06 ? 34 SER B OG 1 ATOM 2254 N N . HIS B 1 35 ? 37.793 9.642 38.142 1.00 20.00 ? 35 HIS B N 1 ATOM 2255 C CA . HIS B 1 35 ? 36.939 10.004 39.260 1.00 20.19 ? 35 HIS B CA 1 ATOM 2256 C C . HIS B 1 35 ? 35.795 9.008 39.417 1.00 20.39 ? 35 HIS B C 1 ATOM 2257 O O . HIS B 1 35 ? 34.684 9.379 39.807 1.00 22.14 ? 35 HIS B O 1 ATOM 2258 C CB . HIS B 1 35 ? 36.385 11.406 39.047 1.00 21.77 ? 35 HIS B CB 1 ATOM 2259 C CG . HIS B 1 35 ? 37.437 12.467 39.043 1.00 24.80 ? 35 HIS B CG 1 ATOM 2260 N ND1 . HIS B 1 35 ? 37.882 13.078 40.196 1.00 26.71 ? 35 HIS B ND1 1 ATOM 2261 C CD2 . HIS B 1 35 ? 38.162 12.999 38.030 1.00 26.08 ? 35 HIS B CD2 1 ATOM 2262 C CE1 . HIS B 1 35 ? 38.835 13.941 39.893 1.00 28.69 ? 35 HIS B CE1 1 ATOM 2263 N NE2 . HIS B 1 35 ? 39.024 13.913 38.585 1.00 28.86 ? 35 HIS B NE2 1 ATOM 2264 N N . GLY B 1 36 ? 36.067 7.745 39.100 1.00 18.55 ? 36 GLY B N 1 ATOM 2265 C CA . GLY B 1 36 ? 35.050 6.716 39.239 1.00 18.15 ? 36 GLY B CA 1 ATOM 2266 C C . GLY B 1 36 ? 34.124 6.538 38.055 1.00 16.83 ? 36 GLY B C 1 ATOM 2267 O O . GLY B 1 36 ? 33.374 5.566 38.005 1.00 16.90 ? 36 GLY B O 1 ATOM 2268 N N . ILE B 1 37 ? 34.164 7.475 37.112 1.00 17.27 ? 37 ILE B N 1 ATOM 2269 C CA . ILE B 1 37 ? 33.325 7.401 35.917 1.00 18.29 ? 37 ILE B CA 1 ATOM 2270 C C . ILE B 1 37 ? 34.087 6.655 34.818 1.00 19.18 ? 37 ILE B C 1 ATOM 2271 O O . ILE B 1 37 ? 35.202 7.045 34.449 1.00 20.22 ? 37 ILE B O 1 ATOM 2272 C CB . ILE B 1 37 ? 32.950 8.817 35.399 1.00 17.89 ? 37 ILE B CB 1 ATOM 2273 C CG1 . ILE B 1 37 ? 32.336 9.641 36.537 1.00 17.71 ? 37 ILE B CG1 1 ATOM 2274 C CG2 . ILE B 1 37 ? 31.953 8.706 34.255 1.00 14.36 ? 37 ILE B CG2 1 ATOM 2275 C CD1 . ILE B 1 37 ? 32.154 11.111 36.217 1.00 18.17 ? 37 ILE B CD1 1 ATOM 2276 N N . PRO B 1 38 ? 33.506 5.561 34.292 1.00 19.60 ? 38 PRO B N 1 ATOM 2277 C CA . PRO B 1 38 ? 34.187 4.807 33.235 1.00 20.03 ? 38 PRO B CA 1 ATOM 2278 C C . PRO B 1 38 ? 34.622 5.690 32.057 1.00 21.01 ? 38 PRO B C 1 ATOM 2279 O O . PRO B 1 38 ? 33.844 6.504 31.548 1.00 19.62 ? 38 PRO B O 1 ATOM 2280 C CB . PRO B 1 38 ? 33.165 3.722 32.856 1.00 19.82 ? 38 PRO B CB 1 ATOM 2281 C CG . PRO B 1 38 ? 31.865 4.219 33.404 1.00 20.07 ? 38 PRO B CG 1 ATOM 2282 C CD . PRO B 1 38 ? 32.235 4.919 34.667 1.00 17.65 ? 38 PRO B CD 1 ATOM 2283 N N . LEU B 1 39 ? 35.884 5.528 31.653 1.00 21.33 ? 39 LEU B N 1 ATOM 2284 C CA . LEU B 1 39 ? 36.478 6.308 30.568 1.00 20.92 ? 39 LEU B CA 1 ATOM 2285 C C . LEU B 1 39 ? 36.645 5.514 29.270 1.00 20.98 ? 39 LEU B C 1 ATOM 2286 O O . LEU B 1 39 ? 37.353 4.499 29.231 1.00 18.67 ? 39 LEU B O 1 ATOM 2287 C CB . LEU B 1 39 ? 37.842 6.840 31.020 1.00 22.10 ? 39 LEU B CB 1 ATOM 2288 C CG . LEU B 1 39 ? 38.585 7.812 30.100 1.00 21.13 ? 39 LEU B CG 1 ATOM 2289 C CD1 . LEU B 1 39 ? 37.766 9.082 29.907 1.00 20.56 ? 39 LEU B CD1 1 ATOM 2290 C CD2 . LEU B 1 39 ? 39.938 8.143 30.720 1.00 21.98 ? 39 LEU B CD2 1 ATOM 2291 N N . LEU B 1 40 ? 36.001 5.985 28.205 1.00 19.44 ? 40 LEU B N 1 ATOM 2292 C CA . LEU B 1 40 ? 36.084 5.309 26.911 1.00 20.11 ? 40 LEU B CA 1 ATOM 2293 C C . LEU B 1 40 ? 37.512 5.322 26.357 1.00 20.80 ? 40 LEU B C 1 ATOM 2294 O O . LEU B 1 40 ? 38.313 6.195 26.687 1.00 19.81 ? 40 LEU B O 1 ATOM 2295 C CB . LEU B 1 40 ? 35.135 5.972 25.902 1.00 17.11 ? 40 LEU B CB 1 ATOM 2296 C CG . LEU B 1 40 ? 33.630 5.897 26.187 1.00 16.29 ? 40 LEU B CG 1 ATOM 2297 C CD1 . LEU B 1 40 ? 32.888 6.846 25.253 1.00 11.14 ? 40 LEU B CD1 1 ATOM 2298 C CD2 . LEU B 1 40 ? 33.137 4.455 26.020 1.00 12.90 ? 40 LEU B CD2 1 ATOM 2299 N N . ARG B 1 41 ? 37.821 4.344 25.512 1.00 24.12 ? 41 ARG B N 1 ATOM 2300 C CA . ARG B 1 41 ? 39.144 4.242 24.906 1.00 26.77 ? 41 ARG B CA 1 ATOM 2301 C C . ARG B 1 41 ? 39.491 5.471 24.077 1.00 29.76 ? 41 ARG B C 1 ATOM 2302 O O . ARG B 1 41 ? 38.626 6.057 23.420 1.00 29.15 ? 41 ARG B O 1 ATOM 2303 C CB . ARG B 1 41 ? 39.220 2.992 24.031 1.00 25.88 ? 41 ARG B CB 1 ATOM 2304 C CG . ARG B 1 41 ? 39.414 1.722 24.827 1.00 25.14 ? 41 ARG B CG 1 ATOM 2305 C CD . ARG B 1 41 ? 39.355 0.500 23.949 1.00 26.37 ? 41 ARG B CD 1 ATOM 2306 N NE . ARG B 1 41 ? 37.977 0.121 23.675 1.00 26.00 ? 41 ARG B NE 1 ATOM 2307 C CZ . ARG B 1 41 ? 37.626 -0.864 22.860 1.00 26.90 ? 41 ARG B CZ 1 ATOM 2308 N NH1 . ARG B 1 41 ? 36.342 -1.147 22.676 1.00 28.52 ? 41 ARG B NH1 1 ATOM 2309 N NH2 . ARG B 1 41 ? 38.558 -1.563 22.224 1.00 26.83 ? 41 ARG B NH2 1 ATOM 2310 N N . LYS B 1 42 ? 40.767 5.851 24.107 1.00 33.30 ? 42 LYS B N 1 ATOM 2311 C CA . LYS B 1 42 ? 41.238 7.018 23.370 1.00 36.76 ? 42 LYS B CA 1 ATOM 2312 C C . LYS B 1 42 ? 41.348 6.738 21.881 1.00 37.65 ? 42 LYS B C 1 ATOM 2313 O O . LYS B 1 42 ? 40.737 7.425 21.069 1.00 37.15 ? 42 LYS B O 1 ATOM 2314 C CB . LYS B 1 42 ? 42.605 7.468 23.890 1.00 38.34 ? 42 LYS B CB 1 ATOM 2315 C CG . LYS B 1 42 ? 43.048 8.826 23.340 1.00 41.33 ? 42 LYS B CG 1 ATOM 2316 C CD . LYS B 1 42 ? 44.537 9.078 23.563 1.00 44.85 ? 42 LYS B CD 1 ATOM 2317 C CE . LYS B 1 42 ? 44.929 8.918 25.026 1.00 47.04 ? 42 LYS B CE 1 ATOM 2318 N NZ . LYS B 1 42 ? 46.399 9.080 25.253 1.00 50.05 ? 42 LYS B NZ 1 ATOM 2319 N N . LYS B 1 43 ? 42.139 5.733 21.528 1.00 40.76 ? 43 LYS B N 1 ATOM 2320 C CA . LYS B 1 43 ? 42.329 5.378 20.129 1.00 44.50 ? 43 LYS B CA 1 ATOM 2321 C C . LYS B 1 43 ? 41.820 3.979 19.844 1.00 45.58 ? 43 LYS B C 1 ATOM 2322 O O . LYS B 1 43 ? 41.787 3.115 20.723 1.00 45.05 ? 43 LYS B O 1 ATOM 2323 C CB . LYS B 1 43 ? 43.812 5.487 19.730 1.00 47.07 ? 43 LYS B CB 1 ATOM 2324 C CG . LYS B 1 43 ? 44.764 4.596 20.533 1.00 51.94 ? 43 LYS B CG 1 ATOM 2325 C CD . LYS B 1 43 ? 46.225 4.812 20.121 1.00 55.31 ? 43 LYS B CD 1 ATOM 2326 C CE . LYS B 1 43 ? 47.195 3.987 20.979 1.00 56.84 ? 43 LYS B CE 1 ATOM 2327 N NZ . LYS B 1 43 ? 48.635 4.209 20.612 1.00 56.56 ? 43 LYS B NZ 1 ATOM 2328 N N . CYS B 1 44 ? 41.426 3.775 18.593 1.00 48.33 ? 44 CYS B N 1 ATOM 2329 C CA . CYS B 1 44 ? 40.893 2.505 18.120 1.00 50.52 ? 44 CYS B CA 1 ATOM 2330 C C . CYS B 1 44 ? 40.494 2.792 16.676 1.00 52.26 ? 44 CYS B C 1 ATOM 2331 O O . CYS B 1 44 ? 39.355 3.180 16.399 1.00 52.55 ? 44 CYS B O 1 ATOM 2332 C CB . CYS B 1 44 ? 39.657 2.120 18.942 1.00 50.27 ? 44 CYS B CB 1 ATOM 2333 S SG . CYS B 1 44 ? 39.180 0.359 18.911 1.00 48.73 ? 44 CYS B SG 1 ATOM 2334 N N . ASP B 1 45 ? 41.440 2.618 15.760 1.00 53.75 ? 45 ASP B N 1 ATOM 2335 C CA . ASP B 1 45 ? 41.186 2.888 14.349 1.00 55.30 ? 45 ASP B CA 1 ATOM 2336 C C . ASP B 1 45 ? 40.892 1.637 13.529 1.00 55.10 ? 45 ASP B C 1 ATOM 2337 O O . ASP B 1 45 ? 40.687 1.720 12.317 1.00 56.11 ? 45 ASP B O 1 ATOM 2338 C CB . ASP B 1 45 ? 42.385 3.619 13.741 1.00 57.22 ? 45 ASP B CB 1 ATOM 2339 C CG . ASP B 1 45 ? 42.759 4.869 14.516 1.00 58.78 ? 45 ASP B CG 1 ATOM 2340 O OD1 . ASP B 1 45 ? 41.894 5.761 14.652 1.00 58.63 ? 45 ASP B OD1 1 ATOM 2341 O OD2 . ASP B 1 45 ? 43.916 4.958 14.987 1.00 59.22 ? 45 ASP B OD2 1 ATOM 2342 N N . ASP B 1 46 ? 40.869 0.484 14.184 1.00 53.55 ? 46 ASP B N 1 ATOM 2343 C CA . ASP B 1 46 ? 40.608 -0.766 13.490 1.00 52.79 ? 46 ASP B CA 1 ATOM 2344 C C . ASP B 1 46 ? 39.110 -1.082 13.431 1.00 52.18 ? 46 ASP B C 1 ATOM 2345 O O . ASP B 1 46 ? 38.499 -1.443 14.440 1.00 51.69 ? 46 ASP B O 1 ATOM 2346 C CB . ASP B 1 46 ? 41.373 -1.903 14.178 1.00 53.86 ? 46 ASP B CB 1 ATOM 2347 C CG . ASP B 1 46 ? 41.315 -3.204 13.400 1.00 54.54 ? 46 ASP B CG 1 ATOM 2348 O OD1 . ASP B 1 46 ? 41.573 -3.178 12.180 1.00 54.87 ? 46 ASP B OD1 1 ATOM 2349 O OD2 . ASP B 1 46 ? 41.023 -4.255 14.009 1.00 55.75 ? 46 ASP B OD2 1 ATOM 2350 N N . PRO B 1 47 ? 38.497 -0.943 12.240 1.00 51.34 ? 47 PRO B N 1 ATOM 2351 C CA . PRO B 1 47 ? 37.068 -1.219 12.062 1.00 50.74 ? 47 PRO B CA 1 ATOM 2352 C C . PRO B 1 47 ? 36.751 -2.651 12.463 1.00 50.64 ? 47 PRO B C 1 ATOM 2353 O O . PRO B 1 47 ? 35.595 -3.004 12.705 1.00 50.79 ? 47 PRO B O 1 ATOM 2354 C CB . PRO B 1 47 ? 36.852 -0.991 10.566 1.00 50.45 ? 47 PRO B CB 1 ATOM 2355 C CG . PRO B 1 47 ? 37.896 0.012 10.215 1.00 50.98 ? 47 PRO B CG 1 ATOM 2356 C CD . PRO B 1 47 ? 39.098 -0.491 10.973 1.00 51.27 ? 47 PRO B CD 1 ATOM 2357 N N . GLY B 1 48 ? 37.799 -3.469 12.527 1.00 50.73 ? 48 GLY B N 1 ATOM 2358 C CA . GLY B 1 48 ? 37.650 -4.867 12.882 1.00 51.06 ? 48 GLY B CA 1 ATOM 2359 C C . GLY B 1 48 ? 37.171 -5.115 14.300 1.00 51.47 ? 48 GLY B C 1 ATOM 2360 O O . GLY B 1 48 ? 36.671 -6.201 14.611 1.00 52.87 ? 48 GLY B O 1 ATOM 2361 N N . LYS B 1 49 ? 37.318 -4.122 15.171 1.00 49.93 ? 49 LYS B N 1 ATOM 2362 C CA . LYS B 1 49 ? 36.879 -4.288 16.548 1.00 48.79 ? 49 LYS B CA 1 ATOM 2363 C C . LYS B 1 49 ? 36.710 -2.967 17.295 1.00 45.89 ? 49 LYS B C 1 ATOM 2364 O O . LYS B 1 49 ? 36.803 -2.926 18.525 1.00 46.09 ? 49 LYS B O 1 ATOM 2365 C CB . LYS B 1 49 ? 37.856 -5.208 17.293 1.00 51.22 ? 49 LYS B CB 1 ATOM 2366 C CG . LYS B 1 49 ? 39.329 -4.808 17.185 1.00 53.61 ? 49 LYS B CG 1 ATOM 2367 C CD . LYS B 1 49 ? 40.254 -5.921 17.695 1.00 55.92 ? 49 LYS B CD 1 ATOM 2368 C CE . LYS B 1 49 ? 39.980 -6.271 19.159 1.00 58.02 ? 49 LYS B CE 1 ATOM 2369 N NZ . LYS B 1 49 ? 40.803 -7.421 19.645 1.00 59.47 ? 49 LYS B NZ 1 ATOM 2370 N N . CYS B 1 50 ? 36.440 -1.897 16.551 1.00 41.07 ? 50 CYS B N 1 ATOM 2371 C CA . CYS B 1 50 ? 36.262 -0.581 17.155 1.00 37.59 ? 50 CYS B CA 1 ATOM 2372 C C . CYS B 1 50 ? 34.845 -0.029 17.032 1.00 32.53 ? 50 CYS B C 1 ATOM 2373 O O . CYS B 1 50 ? 34.608 1.171 17.187 1.00 28.77 ? 50 CYS B O 1 ATOM 2374 C CB . CYS B 1 50 ? 37.270 0.394 16.556 1.00 41.49 ? 50 CYS B CB 1 ATOM 2375 S SG . CYS B 1 50 ? 38.994 -0.072 16.935 1.00 47.95 ? 50 CYS B SG 1 ATOM 2376 N N . PHE B 1 51 ? 33.907 -0.930 16.764 1.00 28.65 ? 51 PHE B N 1 ATOM 2377 C CA . PHE B 1 51 ? 32.500 -0.588 16.632 1.00 25.53 ? 51 PHE B CA 1 ATOM 2378 C C . PHE B 1 51 ? 31.675 -1.667 17.322 1.00 24.70 ? 51 PHE B C 1 ATOM 2379 O O . PHE B 1 51 ? 32.098 -2.827 17.415 1.00 23.67 ? 51 PHE B O 1 ATOM 2380 C CB . PHE B 1 51 ? 32.097 -0.530 15.153 1.00 23.47 ? 51 PHE B CB 1 ATOM 2381 C CG . PHE B 1 51 ? 32.788 0.549 14.379 1.00 23.53 ? 51 PHE B CG 1 ATOM 2382 C CD1 . PHE B 1 51 ? 32.327 1.861 14.426 1.00 22.38 ? 51 PHE B CD1 1 ATOM 2383 C CD2 . PHE B 1 51 ? 33.937 0.265 13.640 1.00 22.97 ? 51 PHE B CD2 1 ATOM 2384 C CE1 . PHE B 1 51 ? 33.001 2.876 13.753 1.00 19.43 ? 51 PHE B CE1 1 ATOM 2385 C CE2 . PHE B 1 51 ? 34.618 1.274 12.965 1.00 22.10 ? 51 PHE B CE2 1 ATOM 2386 C CZ . PHE B 1 51 ? 34.149 2.580 13.023 1.00 21.74 ? 51 PHE B CZ 1 ATOM 2387 N N . VAL B 1 52 ? 30.506 -1.275 17.820 1.00 22.25 ? 52 VAL B N 1 ATOM 2388 C CA . VAL B 1 52 ? 29.586 -2.208 18.453 1.00 21.07 ? 52 VAL B CA 1 ATOM 2389 C C . VAL B 1 52 ? 28.322 -2.111 17.603 1.00 20.77 ? 52 VAL B C 1 ATOM 2390 O O . VAL B 1 52 ? 27.909 -1.011 17.231 1.00 19.66 ? 52 VAL B O 1 ATOM 2391 C CB . VAL B 1 52 ? 29.285 -1.811 19.924 1.00 20.92 ? 52 VAL B CB 1 ATOM 2392 C CG1 . VAL B 1 52 ? 28.226 -2.733 20.523 1.00 20.25 ? 52 VAL B CG1 1 ATOM 2393 C CG2 . VAL B 1 52 ? 30.557 -1.912 20.745 1.00 22.93 ? 52 VAL B CG2 1 ATOM 2394 N N . LEU B 1 53 ? 27.730 -3.249 17.257 1.00 19.52 ? 53 LEU B N 1 ATOM 2395 C CA . LEU B 1 53 ? 26.517 -3.219 16.448 1.00 20.85 ? 53 LEU B CA 1 ATOM 2396 C C . LEU B 1 53 ? 25.304 -3.349 17.349 1.00 19.66 ? 53 LEU B C 1 ATOM 2397 O O . LEU B 1 53 ? 25.244 -4.241 18.194 1.00 20.88 ? 53 LEU B O 1 ATOM 2398 C CB . LEU B 1 53 ? 26.509 -4.354 15.423 1.00 21.76 ? 53 LEU B CB 1 ATOM 2399 C CG . LEU B 1 53 ? 27.657 -4.421 14.412 1.00 22.67 ? 53 LEU B CG 1 ATOM 2400 C CD1 . LEU B 1 53 ? 27.381 -5.570 13.459 1.00 21.74 ? 53 LEU B CD1 1 ATOM 2401 C CD2 . LEU B 1 53 ? 27.784 -3.111 13.640 1.00 21.55 ? 53 LEU B CD2 1 ATOM 2402 N N . VAL B 1 54 ? 24.350 -2.443 17.177 1.00 18.42 ? 54 VAL B N 1 ATOM 2403 C CA . VAL B 1 54 ? 23.129 -2.464 17.970 1.00 17.59 ? 54 VAL B CA 1 ATOM 2404 C C . VAL B 1 54 ? 21.984 -2.830 17.037 1.00 16.22 ? 54 VAL B C 1 ATOM 2405 O O . VAL B 1 54 ? 21.675 -2.102 16.097 1.00 15.39 ? 54 VAL B O 1 ATOM 2406 C CB . VAL B 1 54 ? 22.873 -1.085 18.633 1.00 18.26 ? 54 VAL B CB 1 ATOM 2407 C CG1 . VAL B 1 54 ? 21.536 -1.086 19.371 1.00 17.58 ? 54 VAL B CG1 1 ATOM 2408 C CG2 . VAL B 1 54 ? 24.012 -0.769 19.601 1.00 16.95 ? 54 VAL B CG2 1 ATOM 2409 N N . ALA B 1 55 ? 21.377 -3.981 17.297 1.00 17.69 ? 55 ALA B N 1 ATOM 2410 C CA . ALA B 1 55 ? 20.277 -4.486 16.484 1.00 18.18 ? 55 ALA B CA 1 ATOM 2411 C C . ALA B 1 55 ? 18.916 -4.070 17.038 1.00 18.64 ? 55 ALA B C 1 ATOM 2412 O O . ALA B 1 55 ? 18.423 -4.628 18.022 1.00 19.12 ? 55 ALA B O 1 ATOM 2413 C CB . ALA B 1 55 ? 20.369 -6.009 16.389 1.00 18.35 ? 55 ALA B CB 1 ATOM 2414 N N . LEU B 1 56 ? 18.314 -3.082 16.392 1.00 18.27 ? 56 LEU B N 1 ATOM 2415 C CA . LEU B 1 56 ? 17.017 -2.571 16.799 1.00 18.43 ? 56 LEU B CA 1 ATOM 2416 C C . LEU B 1 56 ? 15.910 -3.216 15.973 1.00 20.60 ? 56 LEU B C 1 ATOM 2417 O O . LEU B 1 56 ? 15.905 -3.103 14.751 1.00 22.07 ? 56 LEU B O 1 ATOM 2418 C CB . LEU B 1 56 ? 16.976 -1.058 16.590 1.00 17.26 ? 56 LEU B CB 1 ATOM 2419 C CG . LEU B 1 56 ? 18.033 -0.223 17.304 1.00 16.55 ? 56 LEU B CG 1 ATOM 2420 C CD1 . LEU B 1 56 ? 17.866 1.239 16.920 1.00 16.51 ? 56 LEU B CD1 1 ATOM 2421 C CD2 . LEU B 1 56 ? 17.888 -0.402 18.806 1.00 17.23 ? 56 LEU B CD2 1 ATOM 2422 N N . SER B 1 57 ? 14.970 -3.888 16.630 1.00 21.29 ? 57 SER B N 1 ATOM 2423 C CA . SER B 1 57 ? 13.867 -4.513 15.912 1.00 23.43 ? 57 SER B CA 1 ATOM 2424 C C . SER B 1 57 ? 12.527 -4.094 16.509 1.00 24.55 ? 57 SER B C 1 ATOM 2425 O O . SER B 1 57 ? 12.379 -4.031 17.732 1.00 24.80 ? 57 SER B O 1 ATOM 2426 C CB . SER B 1 57 ? 14.010 -6.042 15.937 1.00 23.57 ? 57 SER B CB 1 ATOM 2427 O OG . SER B 1 57 ? 14.134 -6.538 17.259 1.00 27.23 ? 57 SER B OG 1 ATOM 2428 N N . ASN B 1 58 ? 11.550 -3.793 15.655 1.00 25.10 ? 58 ASN B N 1 ATOM 2429 C CA . ASN B 1 58 ? 10.247 -3.388 16.171 1.00 27.13 ? 58 ASN B CA 1 ATOM 2430 C C . ASN B 1 58 ? 9.223 -4.522 16.239 1.00 27.55 ? 58 ASN B C 1 ATOM 2431 O O . ASN B 1 58 ? 9.557 -5.698 16.071 1.00 25.87 ? 58 ASN B O 1 ATOM 2432 C CB . ASN B 1 58 ? 9.675 -2.198 15.381 1.00 26.30 ? 58 ASN B CB 1 ATOM 2433 C CG . ASN B 1 58 ? 9.420 -2.519 13.917 1.00 28.98 ? 58 ASN B CG 1 ATOM 2434 O OD1 . ASN B 1 58 ? 9.298 -3.683 13.527 1.00 29.05 ? 58 ASN B OD1 1 ATOM 2435 N ND2 . ASN B 1 58 ? 9.316 -1.474 13.098 1.00 28.44 ? 58 ASN B ND2 1 ATOM 2436 N N . ASP B 1 59 ? 7.974 -4.149 16.498 1.00 29.88 ? 59 ASP B N 1 ATOM 2437 C CA . ASP B 1 59 ? 6.880 -5.098 16.634 1.00 32.58 ? 59 ASP B CA 1 ATOM 2438 C C . ASP B 1 59 ? 6.567 -5.929 15.396 1.00 34.20 ? 59 ASP B C 1 ATOM 2439 O O . ASP B 1 59 ? 6.054 -7.043 15.511 1.00 34.20 ? 59 ASP B O 1 ATOM 2440 C CB . ASP B 1 59 ? 5.628 -4.351 17.087 1.00 34.01 ? 59 ASP B CB 1 ATOM 2441 C CG . ASP B 1 59 ? 5.760 -3.799 18.502 1.00 36.99 ? 59 ASP B CG 1 ATOM 2442 O OD1 . ASP B 1 59 ? 6.805 -3.177 18.807 1.00 35.90 ? 59 ASP B OD1 1 ATOM 2443 O OD2 . ASP B 1 59 ? 4.817 -3.985 19.306 1.00 36.93 ? 59 ASP B OD2 1 ATOM 2444 N N . ASN B 1 60 ? 6.877 -5.397 14.217 1.00 35.91 ? 60 ASN B N 1 ATOM 2445 C CA . ASN B 1 60 ? 6.609 -6.112 12.973 1.00 36.73 ? 60 ASN B CA 1 ATOM 2446 C C . ASN B 1 60 ? 7.811 -6.852 12.400 1.00 36.57 ? 60 ASN B C 1 ATOM 2447 O O . ASN B 1 60 ? 7.801 -7.251 11.239 1.00 36.89 ? 60 ASN B O 1 ATOM 2448 C CB . ASN B 1 60 ? 6.056 -5.150 11.916 1.00 38.84 ? 60 ASN B CB 1 ATOM 2449 C CG . ASN B 1 60 ? 4.641 -4.690 12.231 1.00 42.13 ? 60 ASN B CG 1 ATOM 2450 O OD1 . ASN B 1 60 ? 3.774 -5.500 12.571 1.00 43.61 ? 60 ASN B OD1 1 ATOM 2451 N ND2 . ASN B 1 60 ? 4.396 -3.387 12.109 1.00 43.47 ? 60 ASN B ND2 1 ATOM 2452 N N . GLY B 1 61 ? 8.848 -7.036 13.207 1.00 36.41 ? 61 GLY B N 1 ATOM 2453 C CA . GLY B 1 61 ? 10.022 -7.744 12.729 1.00 35.99 ? 61 GLY B CA 1 ATOM 2454 C C . GLY B 1 61 ? 11.017 -6.927 11.917 1.00 35.09 ? 61 GLY B C 1 ATOM 2455 O O . GLY B 1 61 ? 12.042 -7.459 11.478 1.00 36.12 ? 61 GLY B O 1 ATOM 2456 N N . GLN B 1 62 ? 10.726 -5.645 11.699 1.00 32.63 ? 62 GLN B N 1 ATOM 2457 C CA . GLN B 1 62 ? 11.634 -4.780 10.947 1.00 29.04 ? 62 GLN B CA 1 ATOM 2458 C C . GLN B 1 62 ? 12.901 -4.563 11.766 1.00 27.55 ? 62 GLN B C 1 ATOM 2459 O O . GLN B 1 62 ? 12.827 -4.318 12.966 1.00 27.66 ? 62 GLN B O 1 ATOM 2460 C CB . GLN B 1 62 ? 10.960 -3.450 10.656 1.00 26.68 ? 62 GLN B CB 1 ATOM 2461 C CG . GLN B 1 62 ? 9.777 -3.595 9.753 1.00 28.24 ? 62 GLN B CG 1 ATOM 2462 C CD . GLN B 1 62 ? 9.052 -2.299 9.569 1.00 30.56 ? 62 GLN B CD 1 ATOM 2463 O OE1 . GLN B 1 62 ? 8.523 -1.731 10.528 1.00 31.87 ? 62 GLN B OE1 1 ATOM 2464 N NE2 . GLN B 1 62 ? 9.023 -1.806 8.334 1.00 30.46 ? 62 GLN B NE2 1 ATOM 2465 N N . LEU B 1 63 ? 14.054 -4.654 11.113 1.00 26.07 ? 63 LEU B N 1 ATOM 2466 C CA . LEU B 1 63 ? 15.340 -4.503 11.784 1.00 25.61 ? 63 LEU B CA 1 ATOM 2467 C C . LEU B 1 63 ? 16.271 -3.449 11.181 1.00 25.53 ? 63 LEU B C 1 ATOM 2468 O O . LEU B 1 63 ? 16.319 -3.253 9.963 1.00 26.10 ? 63 LEU B O 1 ATOM 2469 C CB . LEU B 1 63 ? 16.070 -5.851 11.800 1.00 26.52 ? 63 LEU B CB 1 ATOM 2470 C CG . LEU B 1 63 ? 17.537 -5.873 12.260 1.00 29.44 ? 63 LEU B CG 1 ATOM 2471 C CD1 . LEU B 1 63 ? 17.648 -5.571 13.755 1.00 27.70 ? 63 LEU B CD1 1 ATOM 2472 C CD2 . LEU B 1 63 ? 18.132 -7.241 11.959 1.00 29.79 ? 63 LEU B CD2 1 ATOM 2473 N N . ALA B 1 64 ? 17.007 -2.775 12.061 1.00 23.65 ? 64 ALA B N 1 ATOM 2474 C CA . ALA B 1 64 ? 17.984 -1.762 11.676 1.00 21.56 ? 64 ALA B CA 1 ATOM 2475 C C . ALA B 1 64 ? 19.166 -2.020 12.595 1.00 21.14 ? 64 ALA B C 1 ATOM 2476 O O . ALA B 1 64 ? 19.021 -1.980 13.818 1.00 20.97 ? 64 ALA B O 1 ATOM 2477 C CB . ALA B 1 64 ? 17.428 -0.355 11.905 1.00 19.56 ? 64 ALA B CB 1 ATOM 2478 N N . GLU B 1 65 ? 20.323 -2.312 12.013 1.00 20.69 ? 65 GLU B N 1 ATOM 2479 C CA . GLU B 1 65 ? 21.516 -2.583 12.804 1.00 22.13 ? 65 GLU B CA 1 ATOM 2480 C C . GLU B 1 65 ? 22.372 -1.320 12.800 1.00 21.04 ? 65 GLU B C 1 ATOM 2481 O O . GLU B 1 65 ? 22.830 -0.885 11.748 1.00 21.32 ? 65 GLU B O 1 ATOM 2482 C CB . GLU B 1 65 ? 22.280 -3.758 12.196 1.00 25.37 ? 65 GLU B CB 1 ATOM 2483 C CG . GLU B 1 65 ? 23.008 -4.614 13.214 1.00 34.40 ? 65 GLU B CG 1 ATOM 2484 C CD . GLU B 1 65 ? 23.753 -5.791 12.589 1.00 39.18 ? 65 GLU B CD 1 ATOM 2485 O OE1 . GLU B 1 65 ? 24.245 -6.652 13.356 1.00 43.26 ? 65 GLU B OE1 1 ATOM 2486 O OE2 . GLU B 1 65 ? 23.855 -5.857 11.341 1.00 42.29 ? 65 GLU B OE2 1 ATOM 2487 N N . ILE B 1 66 ? 22.580 -0.737 13.979 1.00 19.52 ? 66 ILE B N 1 ATOM 2488 C CA . ILE B 1 66 ? 23.346 0.506 14.113 1.00 17.43 ? 66 ILE B CA 1 ATOM 2489 C C . ILE B 1 66 ? 24.816 0.295 14.487 1.00 17.58 ? 66 ILE B C 1 ATOM 2490 O O . ILE B 1 66 ? 25.122 -0.465 15.407 1.00 16.95 ? 66 ILE B O 1 ATOM 2491 C CB . ILE B 1 66 ? 22.711 1.419 15.195 1.00 16.58 ? 66 ILE B CB 1 ATOM 2492 C CG1 . ILE B 1 66 ? 21.187 1.483 15.003 1.00 16.36 ? 66 ILE B CG1 1 ATOM 2493 C CG2 . ILE B 1 66 ? 23.332 2.804 15.141 1.00 13.94 ? 66 ILE B CG2 1 ATOM 2494 C CD1 . ILE B 1 66 ? 20.728 2.139 13.702 1.00 17.46 ? 66 ILE B CD1 1 ATOM 2495 N N . ALA B 1 67 ? 25.716 0.973 13.774 1.00 15.50 ? 67 ALA B N 1 ATOM 2496 C CA . ALA B 1 67 ? 27.151 0.884 14.050 1.00 17.00 ? 67 ALA B CA 1 ATOM 2497 C C . ALA B 1 67 ? 27.555 2.049 14.973 1.00 17.62 ? 67 ALA B C 1 ATOM 2498 O O . ALA B 1 67 ? 27.431 3.226 14.602 1.00 18.04 ? 67 ALA B O 1 ATOM 2499 C CB . ALA B 1 67 ? 27.952 0.939 12.738 1.00 15.92 ? 67 ALA B CB 1 ATOM 2500 N N . ILE B 1 68 ? 28.031 1.712 16.170 1.00 17.05 ? 68 ILE B N 1 ATOM 2501 C CA . ILE B 1 68 ? 28.435 2.708 17.166 1.00 17.71 ? 68 ILE B CA 1 ATOM 2502 C C . ILE B 1 68 ? 29.949 2.664 17.427 1.00 18.96 ? 68 ILE B C 1 ATOM 2503 O O . ILE B 1 68 ? 30.501 1.615 17.767 1.00 18.20 ? 68 ILE B O 1 ATOM 2504 C CB . ILE B 1 68 ? 27.707 2.465 18.535 1.00 18.48 ? 68 ILE B CB 1 ATOM 2505 C CG1 . ILE B 1 68 ? 26.186 2.389 18.339 1.00 17.72 ? 68 ILE B CG1 1 ATOM 2506 C CG2 . ILE B 1 68 ? 28.068 3.568 19.531 1.00 15.20 ? 68 ILE B CG2 1 ATOM 2507 C CD1 . ILE B 1 68 ? 25.515 3.706 18.076 1.00 20.96 ? 68 ILE B CD1 1 ATOM 2508 N N . ASP B 1 69 ? 30.609 3.809 17.272 1.00 20.59 ? 69 ASP B N 1 ATOM 2509 C CA . ASP B 1 69 ? 32.052 3.941 17.510 1.00 21.30 ? 69 ASP B CA 1 ATOM 2510 C C . ASP B 1 69 ? 32.301 3.756 19.010 1.00 20.12 ? 69 ASP B C 1 ATOM 2511 O O . ASP B 1 69 ? 31.626 4.384 19.824 1.00 19.48 ? 69 ASP B O 1 ATOM 2512 C CB . ASP B 1 69 ? 32.508 5.339 17.082 1.00 24.80 ? 69 ASP B CB 1 ATOM 2513 C CG . ASP B 1 69 ? 34.004 5.543 17.222 1.00 29.17 ? 69 ASP B CG 1 ATOM 2514 O OD1 . ASP B 1 69 ? 34.540 5.408 18.339 1.00 33.01 ? 69 ASP B OD1 1 ATOM 2515 O OD2 . ASP B 1 69 ? 34.652 5.851 16.205 1.00 32.51 ? 69 ASP B OD2 1 ATOM 2516 N N . VAL B 1 70 ? 33.268 2.916 19.382 1.00 19.06 ? 70 VAL B N 1 ATOM 2517 C CA . VAL B 1 70 ? 33.537 2.673 20.803 1.00 18.27 ? 70 VAL B CA 1 ATOM 2518 C C . VAL B 1 70 ? 34.307 3.765 21.536 1.00 18.30 ? 70 VAL B C 1 ATOM 2519 O O . VAL B 1 70 ? 34.427 3.715 22.757 1.00 18.86 ? 70 VAL B O 1 ATOM 2520 C CB . VAL B 1 70 ? 34.294 1.344 21.033 1.00 19.25 ? 70 VAL B CB 1 ATOM 2521 C CG1 . VAL B 1 70 ? 33.488 0.176 20.475 1.00 18.19 ? 70 VAL B CG1 1 ATOM 2522 C CG2 . VAL B 1 70 ? 35.684 1.421 20.411 1.00 19.55 ? 70 VAL B CG2 1 ATOM 2523 N N . THR B 1 71 ? 34.837 4.748 20.816 1.00 17.65 ? 71 THR B N 1 ATOM 2524 C CA . THR B 1 71 ? 35.576 5.821 21.481 1.00 19.10 ? 71 THR B CA 1 ATOM 2525 C C . THR B 1 71 ? 34.714 7.055 21.770 1.00 19.11 ? 71 THR B C 1 ATOM 2526 O O . THR B 1 71 ? 35.076 7.883 22.604 1.00 20.44 ? 71 THR B O 1 ATOM 2527 C CB . THR B 1 71 ? 36.797 6.275 20.653 1.00 19.36 ? 71 THR B CB 1 ATOM 2528 O OG1 . THR B 1 71 ? 36.350 6.875 19.430 1.00 19.00 ? 71 THR B OG1 1 ATOM 2529 C CG2 . THR B 1 71 ? 37.700 5.088 20.349 1.00 19.10 ? 71 THR B CG2 1 ATOM 2530 N N . SER B 1 72 ? 33.570 7.172 21.099 1.00 19.58 ? 72 SER B N 1 ATOM 2531 C CA . SER B 1 72 ? 32.691 8.325 21.297 1.00 18.54 ? 72 SER B CA 1 ATOM 2532 C C . SER B 1 72 ? 31.209 7.969 21.344 1.00 17.72 ? 72 SER B C 1 ATOM 2533 O O . SER B 1 72 ? 30.372 8.841 21.581 1.00 16.31 ? 72 SER B O 1 ATOM 2534 C CB . SER B 1 72 ? 32.912 9.332 20.170 1.00 19.57 ? 72 SER B CB 1 ATOM 2535 O OG . SER B 1 72 ? 32.607 8.734 18.918 1.00 21.65 ? 72 SER B OG 1 ATOM 2536 N N . VAL B 1 73 ? 30.895 6.694 21.118 1.00 16.96 ? 73 VAL B N 1 ATOM 2537 C CA . VAL B 1 73 ? 29.513 6.207 21.091 1.00 17.57 ? 73 VAL B CA 1 ATOM 2538 C C . VAL B 1 73 ? 28.766 6.902 19.947 1.00 17.62 ? 73 VAL B C 1 ATOM 2539 O O . VAL B 1 73 ? 27.537 7.032 19.963 1.00 15.60 ? 73 VAL B O 1 ATOM 2540 C CB . VAL B 1 73 ? 28.760 6.486 22.420 1.00 18.32 ? 73 VAL B CB 1 ATOM 2541 C CG1 . VAL B 1 73 ? 27.507 5.606 22.492 1.00 17.34 ? 73 VAL B CG1 1 ATOM 2542 C CG2 . VAL B 1 73 ? 29.678 6.228 23.617 1.00 15.88 ? 73 VAL B CG2 1 ATOM 2543 N N . TYR B 1 74 ? 29.533 7.333 18.950 1.00 17.12 ? 74 TYR B N 1 ATOM 2544 C CA . TYR B 1 74 ? 28.995 8.030 17.786 1.00 18.25 ? 74 TYR B CA 1 ATOM 2545 C C . TYR B 1 74 ? 28.374 7.050 16.783 1.00 16.42 ? 74 TYR B C 1 ATOM 2546 O O . TYR B 1 74 ? 28.976 6.034 16.439 1.00 14.99 ? 74 TYR B O 1 ATOM 2547 C CB . TYR B 1 74 ? 30.131 8.815 17.104 1.00 22.09 ? 74 TYR B CB 1 ATOM 2548 C CG . TYR B 1 74 ? 29.707 9.852 16.076 1.00 27.82 ? 74 TYR B CG 1 ATOM 2549 C CD1 . TYR B 1 74 ? 29.156 11.080 16.472 1.00 29.61 ? 74 TYR B CD1 1 ATOM 2550 C CD2 . TYR B 1 74 ? 29.886 9.622 14.705 1.00 29.83 ? 74 TYR B CD2 1 ATOM 2551 C CE1 . TYR B 1 74 ? 28.798 12.058 15.526 1.00 31.27 ? 74 TYR B CE1 1 ATOM 2552 C CE2 . TYR B 1 74 ? 29.529 10.590 13.748 1.00 32.17 ? 74 TYR B CE2 1 ATOM 2553 C CZ . TYR B 1 74 ? 28.989 11.806 14.168 1.00 33.54 ? 74 TYR B CZ 1 ATOM 2554 O OH . TYR B 1 74 ? 28.662 12.770 13.234 1.00 33.79 ? 74 TYR B OH 1 ATOM 2555 N N . VAL B 1 75 ? 27.157 7.348 16.335 1.00 15.45 ? 75 VAL B N 1 ATOM 2556 C CA . VAL B 1 75 ? 26.492 6.521 15.330 1.00 13.63 ? 75 VAL B CA 1 ATOM 2557 C C . VAL B 1 75 ? 27.126 6.907 13.986 1.00 14.23 ? 75 VAL B C 1 ATOM 2558 O O . VAL B 1 75 ? 27.020 8.067 13.574 1.00 13.78 ? 75 VAL B O 1 ATOM 2559 C CB . VAL B 1 75 ? 24.984 6.840 15.262 1.00 13.51 ? 75 VAL B CB 1 ATOM 2560 C CG1 . VAL B 1 75 ? 24.350 6.115 14.085 1.00 12.06 ? 75 VAL B CG1 1 ATOM 2561 C CG2 . VAL B 1 75 ? 24.306 6.448 16.569 1.00 13.86 ? 75 VAL B CG2 1 ATOM 2562 N N . VAL B 1 76 ? 27.785 5.964 13.310 1.00 13.69 ? 76 VAL B N 1 ATOM 2563 C CA . VAL B 1 76 ? 28.417 6.267 12.020 1.00 14.49 ? 76 VAL B CA 1 ATOM 2564 C C . VAL B 1 76 ? 27.599 5.820 10.800 1.00 14.03 ? 76 VAL B C 1 ATOM 2565 O O . VAL B 1 76 ? 27.749 6.368 9.708 1.00 13.19 ? 76 VAL B O 1 ATOM 2566 C CB . VAL B 1 76 ? 29.839 5.640 11.909 1.00 14.22 ? 76 VAL B CB 1 ATOM 2567 C CG1 . VAL B 1 76 ? 30.738 6.200 12.990 1.00 15.53 ? 76 VAL B CG1 1 ATOM 2568 C CG2 . VAL B 1 76 ? 29.760 4.121 12.012 1.00 14.40 ? 76 VAL B CG2 1 ATOM 2569 N N . GLY B 1 77 ? 26.741 4.824 10.989 1.00 13.87 ? 77 GLY B N 1 ATOM 2570 C CA . GLY B 1 77 ? 25.922 4.324 9.899 1.00 13.51 ? 77 GLY B CA 1 ATOM 2571 C C . GLY B 1 77 ? 25.085 3.153 10.376 1.00 15.07 ? 77 GLY B C 1 ATOM 2572 O O . GLY B 1 77 ? 25.128 2.793 11.555 1.00 15.71 ? 77 GLY B O 1 ATOM 2573 N N . TYR B 1 78 ? 24.326 2.548 9.471 1.00 14.41 ? 78 TYR B N 1 ATOM 2574 C CA . TYR B 1 78 ? 23.478 1.417 9.831 1.00 15.88 ? 78 TYR B CA 1 ATOM 2575 C C . TYR B 1 78 ? 23.147 0.538 8.631 1.00 17.85 ? 78 TYR B C 1 ATOM 2576 O O . TYR B 1 78 ? 23.308 0.945 7.472 1.00 17.33 ? 78 TYR B O 1 ATOM 2577 C CB . TYR B 1 78 ? 22.161 1.907 10.429 1.00 14.83 ? 78 TYR B CB 1 ATOM 2578 C CG . TYR B 1 78 ? 21.340 2.709 9.451 1.00 14.89 ? 78 TYR B CG 1 ATOM 2579 C CD1 . TYR B 1 78 ? 21.651 4.043 9.180 1.00 14.06 ? 78 TYR B CD1 1 ATOM 2580 C CD2 . TYR B 1 78 ? 20.288 2.121 8.750 1.00 16.45 ? 78 TYR B CD2 1 ATOM 2581 C CE1 . TYR B 1 78 ? 20.939 4.765 8.234 1.00 15.36 ? 78 TYR B CE1 1 ATOM 2582 C CE2 . TYR B 1 78 ? 19.568 2.839 7.796 1.00 14.83 ? 78 TYR B CE2 1 ATOM 2583 C CZ . TYR B 1 78 ? 19.903 4.156 7.544 1.00 14.80 ? 78 TYR B CZ 1 ATOM 2584 O OH . TYR B 1 78 ? 19.224 4.859 6.585 1.00 14.03 ? 78 TYR B OH 1 ATOM 2585 N N . GLN B 1 79 ? 22.665 -0.667 8.920 1.00 19.02 ? 79 GLN B N 1 ATOM 2586 C CA . GLN B 1 79 ? 22.273 -1.596 7.875 1.00 18.99 ? 79 GLN B CA 1 ATOM 2587 C C . GLN B 1 79 ? 20.801 -1.964 8.027 1.00 20.02 ? 79 GLN B C 1 ATOM 2588 O O . GLN B 1 79 ? 20.310 -2.175 9.143 1.00 19.06 ? 79 GLN B O 1 ATOM 2589 C CB . GLN B 1 79 ? 23.106 -2.874 7.935 1.00 20.87 ? 79 GLN B CB 1 ATOM 2590 C CG . GLN B 1 79 ? 22.862 -3.775 6.729 1.00 24.66 ? 79 GLN B CG 1 ATOM 2591 C CD . GLN B 1 79 ? 23.353 -5.197 6.922 1.00 26.37 ? 79 GLN B CD 1 ATOM 2592 O OE1 . GLN B 1 79 ? 24.391 -5.437 7.542 1.00 26.59 ? 79 GLN B OE1 1 ATOM 2593 N NE2 . GLN B 1 79 ? 22.614 -6.152 6.366 1.00 27.81 ? 79 GLN B NE2 1 ATOM 2594 N N . VAL B 1 80 ? 20.104 -2.017 6.896 1.00 19.26 ? 80 VAL B N 1 ATOM 2595 C CA . VAL B 1 80 ? 18.698 -2.400 6.840 1.00 21.40 ? 80 VAL B CA 1 ATOM 2596 C C . VAL B 1 80 ? 18.576 -3.286 5.603 1.00 23.69 ? 80 VAL B C 1 ATOM 2597 O O . VAL B 1 80 ? 18.940 -2.870 4.499 1.00 23.44 ? 80 VAL B O 1 ATOM 2598 C CB . VAL B 1 80 ? 17.757 -1.175 6.705 1.00 20.59 ? 80 VAL B CB 1 ATOM 2599 C CG1 . VAL B 1 80 ? 17.530 -0.546 8.069 1.00 20.30 ? 80 VAL B CG1 1 ATOM 2600 C CG2 . VAL B 1 80 ? 18.354 -0.147 5.750 1.00 20.15 ? 80 VAL B CG2 1 ATOM 2601 N N . ARG B 1 81 ? 18.084 -4.510 5.789 1.00 25.34 ? 81 ARG B N 1 ATOM 2602 C CA . ARG B 1 81 ? 17.956 -5.461 4.685 1.00 25.68 ? 81 ARG B CA 1 ATOM 2603 C C . ARG B 1 81 ? 19.346 -5.729 4.090 1.00 25.77 ? 81 ARG B C 1 ATOM 2604 O O . ARG B 1 81 ? 20.292 -6.029 4.824 1.00 24.64 ? 81 ARG B O 1 ATOM 2605 C CB . ARG B 1 81 ? 17.000 -4.908 3.626 1.00 26.75 ? 81 ARG B CB 1 ATOM 2606 C CG . ARG B 1 81 ? 15.565 -4.827 4.124 1.00 31.60 ? 81 ARG B CG 1 ATOM 2607 C CD . ARG B 1 81 ? 14.703 -3.941 3.251 1.00 35.06 ? 81 ARG B CD 1 ATOM 2608 N NE . ARG B 1 81 ? 13.295 -4.028 3.628 1.00 39.14 ? 81 ARG B NE 1 ATOM 2609 C CZ . ARG B 1 81 ? 12.312 -3.362 3.027 1.00 42.17 ? 81 ARG B CZ 1 ATOM 2610 N NH1 . ARG B 1 81 ? 12.576 -2.548 2.011 1.00 43.10 ? 81 ARG B NH1 1 ATOM 2611 N NH2 . ARG B 1 81 ? 11.058 -3.510 3.443 1.00 43.54 ? 81 ARG B NH2 1 ATOM 2612 N N . ASN B 1 82 ? 19.481 -5.609 2.773 1.00 25.00 ? 82 ASN B N 1 ATOM 2613 C CA . ASN B 1 82 ? 20.771 -5.854 2.126 1.00 24.86 ? 82 ASN B CA 1 ATOM 2614 C C . ASN B 1 82 ? 21.512 -4.549 1.819 1.00 23.77 ? 82 ASN B C 1 ATOM 2615 O O . ASN B 1 82 ? 22.376 -4.506 0.936 1.00 23.47 ? 82 ASN B O 1 ATOM 2616 C CB . ASN B 1 82 ? 20.565 -6.637 0.822 1.00 24.97 ? 82 ASN B CB 1 ATOM 2617 C CG . ASN B 1 82 ? 19.725 -5.873 -0.188 1.00 26.68 ? 82 ASN B CG 1 ATOM 2618 O OD1 . ASN B 1 82 ? 19.932 -5.985 -1.397 1.00 27.35 ? 82 ASN B OD1 1 ATOM 2619 N ND2 . ASN B 1 82 ? 18.764 -5.092 0.306 1.00 26.47 ? 82 ASN B ND2 1 ATOM 2620 N N . ARG B 1 83 ? 21.185 -3.493 2.556 1.00 22.53 ? 83 ARG B N 1 ATOM 2621 C CA . ARG B 1 83 ? 21.806 -2.195 2.330 1.00 22.95 ? 83 ARG B CA 1 ATOM 2622 C C . ARG B 1 83 ? 22.370 -1.558 3.589 1.00 22.07 ? 83 ARG B C 1 ATOM 2623 O O . ARG B 1 83 ? 21.971 -1.904 4.698 1.00 22.93 ? 83 ARG B O 1 ATOM 2624 C CB . ARG B 1 83 ? 20.781 -1.242 1.725 1.00 23.06 ? 83 ARG B CB 1 ATOM 2625 C CG . ARG B 1 83 ? 20.296 -1.643 0.348 1.00 27.97 ? 83 ARG B CG 1 ATOM 2626 C CD . ARG B 1 83 ? 19.041 -0.883 0.013 1.00 29.82 ? 83 ARG B CD 1 ATOM 2627 N NE . ARG B 1 83 ? 18.696 -0.942 -1.403 1.00 35.30 ? 83 ARG B NE 1 ATOM 2628 C CZ . ARG B 1 83 ? 19.319 -0.253 -2.353 1.00 37.31 ? 83 ARG B CZ 1 ATOM 2629 N NH1 . ARG B 1 83 ? 20.334 0.553 -2.044 1.00 37.55 ? 83 ARG B NH1 1 ATOM 2630 N NH2 . ARG B 1 83 ? 18.908 -0.353 -3.610 1.00 37.89 ? 83 ARG B NH2 1 ATOM 2631 N N . SER B 1 84 ? 23.305 -0.631 3.406 1.00 19.93 ? 84 SER B N 1 ATOM 2632 C CA . SER B 1 84 ? 23.893 0.101 4.520 1.00 20.05 ? 84 SER B CA 1 ATOM 2633 C C . SER B 1 84 ? 24.065 1.563 4.110 1.00 20.40 ? 84 SER B C 1 ATOM 2634 O O . SER B 1 84 ? 24.253 1.875 2.933 1.00 20.02 ? 84 SER B O 1 ATOM 2635 C CB . SER B 1 84 ? 25.236 -0.516 4.959 1.00 19.70 ? 84 SER B CB 1 ATOM 2636 O OG . SER B 1 84 ? 26.193 -0.552 3.919 1.00 19.21 ? 84 SER B OG 1 ATOM 2637 N N . TYR B 1 85 ? 23.965 2.457 5.088 1.00 20.22 ? 85 TYR B N 1 ATOM 2638 C CA . TYR B 1 85 ? 24.092 3.891 4.856 1.00 19.19 ? 85 TYR B CA 1 ATOM 2639 C C . TYR B 1 85 ? 25.043 4.488 5.887 1.00 18.32 ? 85 TYR B C 1 ATOM 2640 O O . TYR B 1 85 ? 24.950 4.189 7.076 1.00 17.23 ? 85 TYR B O 1 ATOM 2641 C CB . TYR B 1 85 ? 22.720 4.566 4.961 1.00 19.07 ? 85 TYR B CB 1 ATOM 2642 C CG . TYR B 1 85 ? 21.700 3.996 4.009 1.00 19.21 ? 85 TYR B CG 1 ATOM 2643 C CD1 . TYR B 1 85 ? 21.109 2.754 4.250 1.00 19.73 ? 85 TYR B CD1 1 ATOM 2644 C CD2 . TYR B 1 85 ? 21.349 4.682 2.846 1.00 18.86 ? 85 TYR B CD2 1 ATOM 2645 C CE1 . TYR B 1 85 ? 20.191 2.209 3.352 1.00 21.07 ? 85 TYR B CE1 1 ATOM 2646 C CE2 . TYR B 1 85 ? 20.435 4.147 1.938 1.00 19.94 ? 85 TYR B CE2 1 ATOM 2647 C CZ . TYR B 1 85 ? 19.860 2.913 2.198 1.00 21.45 ? 85 TYR B CZ 1 ATOM 2648 O OH . TYR B 1 85 ? 18.949 2.387 1.313 1.00 22.26 ? 85 TYR B OH 1 ATOM 2649 N N . PHE B 1 86 ? 25.953 5.335 5.423 1.00 16.70 ? 86 PHE B N 1 ATOM 2650 C CA . PHE B 1 86 ? 26.933 5.955 6.297 1.00 16.42 ? 86 PHE B CA 1 ATOM 2651 C C . PHE B 1 86 ? 26.848 7.469 6.252 1.00 17.06 ? 86 PHE B C 1 ATOM 2652 O O . PHE B 1 86 ? 26.571 8.055 5.208 1.00 18.72 ? 86 PHE B O 1 ATOM 2653 C CB . PHE B 1 86 ? 28.341 5.519 5.882 1.00 15.41 ? 86 PHE B CB 1 ATOM 2654 C CG . PHE B 1 86 ? 28.614 4.061 6.109 1.00 16.62 ? 86 PHE B CG 1 ATOM 2655 C CD1 . PHE B 1 86 ? 29.253 3.632 7.271 1.00 16.26 ? 86 PHE B CD1 1 ATOM 2656 C CD2 . PHE B 1 86 ? 28.211 3.112 5.175 1.00 16.41 ? 86 PHE B CD2 1 ATOM 2657 C CE1 . PHE B 1 86 ? 29.489 2.276 7.502 1.00 16.41 ? 86 PHE B CE1 1 ATOM 2658 C CE2 . PHE B 1 86 ? 28.440 1.755 5.395 1.00 18.10 ? 86 PHE B CE2 1 ATOM 2659 C CZ . PHE B 1 86 ? 29.083 1.336 6.566 1.00 17.59 ? 86 PHE B CZ 1 ATOM 2660 N N . PHE B 1 87 ? 27.079 8.102 7.395 1.00 17.29 ? 87 PHE B N 1 ATOM 2661 C CA . PHE B 1 87 ? 27.061 9.554 7.461 1.00 18.28 ? 87 PHE B CA 1 ATOM 2662 C C . PHE B 1 87 ? 28.216 10.065 6.605 1.00 19.57 ? 87 PHE B C 1 ATOM 2663 O O . PHE B 1 87 ? 29.238 9.389 6.453 1.00 17.23 ? 87 PHE B O 1 ATOM 2664 C CB . PHE B 1 87 ? 27.218 10.029 8.913 1.00 16.05 ? 87 PHE B CB 1 ATOM 2665 C CG . PHE B 1 87 ? 25.929 10.034 9.688 1.00 17.55 ? 87 PHE B CG 1 ATOM 2666 C CD1 . PHE B 1 87 ? 25.855 9.446 10.948 1.00 19.55 ? 87 PHE B CD1 1 ATOM 2667 C CD2 . PHE B 1 87 ? 24.790 10.640 9.162 1.00 17.48 ? 87 PHE B CD2 1 ATOM 2668 C CE1 . PHE B 1 87 ? 24.659 9.461 11.679 1.00 21.11 ? 87 PHE B CE1 1 ATOM 2669 C CE2 . PHE B 1 87 ? 23.586 10.666 9.877 1.00 19.37 ? 87 PHE B CE2 1 ATOM 2670 C CZ . PHE B 1 87 ? 23.519 10.074 11.140 1.00 21.59 ? 87 PHE B CZ 1 ATOM 2671 N N . LYS B 1 88 ? 28.036 11.253 6.043 1.00 20.35 ? 88 LYS B N 1 ATOM 2672 C CA . LYS B 1 88 ? 29.041 11.866 5.192 1.00 24.73 ? 88 LYS B CA 1 ATOM 2673 C C . LYS B 1 88 ? 30.409 11.914 5.865 1.00 25.93 ? 88 LYS B C 1 ATOM 2674 O O . LYS B 1 88 ? 31.441 11.730 5.215 1.00 26.96 ? 88 LYS B O 1 ATOM 2675 C CB . LYS B 1 88 ? 28.603 13.288 4.815 1.00 26.72 ? 88 LYS B CB 1 ATOM 2676 C CG . LYS B 1 88 ? 29.539 14.004 3.845 1.00 30.83 ? 88 LYS B CG 1 ATOM 2677 C CD . LYS B 1 88 ? 29.672 13.231 2.529 1.00 33.74 ? 88 LYS B CD 1 ATOM 2678 C CE . LYS B 1 88 ? 30.647 13.914 1.578 1.00 35.22 ? 88 LYS B CE 1 ATOM 2679 N NZ . LYS B 1 88 ? 31.971 14.139 2.224 1.00 35.40 ? 88 LYS B NZ 1 ATOM 2680 N N . ASP B 1 89 ? 30.411 12.148 7.171 1.00 26.73 ? 89 ASP B N 1 ATOM 2681 C CA . ASP B 1 89 ? 31.649 12.255 7.930 1.00 27.87 ? 89 ASP B CA 1 ATOM 2682 C C . ASP B 1 89 ? 32.216 10.941 8.474 1.00 28.70 ? 89 ASP B C 1 ATOM 2683 O O . ASP B 1 89 ? 33.230 10.949 9.163 1.00 30.34 ? 89 ASP B O 1 ATOM 2684 C CB . ASP B 1 89 ? 31.450 13.257 9.073 1.00 28.92 ? 89 ASP B CB 1 ATOM 2685 C CG . ASP B 1 89 ? 30.266 12.909 9.956 1.00 30.42 ? 89 ASP B CG 1 ATOM 2686 O OD1 . ASP B 1 89 ? 29.235 12.459 9.422 1.00 31.09 ? 89 ASP B OD1 1 ATOM 2687 O OD2 . ASP B 1 89 ? 30.353 13.095 11.187 1.00 33.78 ? 89 ASP B OD2 1 ATOM 2688 N N . ALA B 1 90 ? 31.579 9.813 8.172 1.00 28.19 ? 90 ALA B N 1 ATOM 2689 C CA . ALA B 1 90 ? 32.084 8.524 8.649 1.00 28.90 ? 90 ALA B CA 1 ATOM 2690 C C . ALA B 1 90 ? 33.506 8.291 8.114 1.00 28.88 ? 90 ALA B C 1 ATOM 2691 O O . ALA B 1 90 ? 33.769 8.498 6.933 1.00 29.13 ? 90 ALA B O 1 ATOM 2692 C CB . ALA B 1 90 ? 31.154 7.387 8.190 1.00 26.30 ? 90 ALA B CB 1 ATOM 2693 N N . PRO B 1 91 ? 34.446 7.872 8.982 1.00 30.05 ? 91 PRO B N 1 ATOM 2694 C CA . PRO B 1 91 ? 35.823 7.624 8.537 1.00 31.03 ? 91 PRO B CA 1 ATOM 2695 C C . PRO B 1 91 ? 35.895 6.560 7.437 1.00 32.49 ? 91 PRO B C 1 ATOM 2696 O O . PRO B 1 91 ? 35.210 5.538 7.504 1.00 32.54 ? 91 PRO B O 1 ATOM 2697 C CB . PRO B 1 91 ? 36.528 7.195 9.823 1.00 30.00 ? 91 PRO B CB 1 ATOM 2698 C CG . PRO B 1 91 ? 35.428 6.629 10.653 1.00 30.00 ? 91 PRO B CG 1 ATOM 2699 C CD . PRO B 1 91 ? 34.314 7.604 10.422 1.00 29.09 ? 91 PRO B CD 1 ATOM 2700 N N . ASP B 1 92 ? 36.725 6.806 6.428 1.00 33.85 ? 92 ASP B N 1 ATOM 2701 C CA . ASP B 1 92 ? 36.857 5.882 5.309 1.00 35.24 ? 92 ASP B CA 1 ATOM 2702 C C . ASP B 1 92 ? 37.127 4.447 5.720 1.00 35.53 ? 92 ASP B C 1 ATOM 2703 O O . ASP B 1 92 ? 36.673 3.514 5.056 1.00 36.66 ? 92 ASP B O 1 ATOM 2704 C CB . ASP B 1 92 ? 37.947 6.354 4.345 1.00 38.21 ? 92 ASP B CB 1 ATOM 2705 C CG . ASP B 1 92 ? 37.590 7.666 3.664 1.00 41.13 ? 92 ASP B CG 1 ATOM 2706 O OD1 . ASP B 1 92 ? 36.398 8.041 3.692 1.00 41.65 ? 92 ASP B OD1 1 ATOM 2707 O OD2 . ASP B 1 92 ? 38.497 8.317 3.095 1.00 43.14 ? 92 ASP B OD2 1 ATOM 2708 N N . ALA B 1 93 ? 37.864 4.256 6.808 1.00 34.79 ? 93 ALA B N 1 ATOM 2709 C CA . ALA B 1 93 ? 38.149 2.902 7.268 1.00 33.56 ? 93 ALA B CA 1 ATOM 2710 C C . ALA B 1 93 ? 36.855 2.226 7.741 1.00 32.23 ? 93 ALA B C 1 ATOM 2711 O O . ALA B 1 93 ? 36.690 1.018 7.593 1.00 33.17 ? 93 ALA B O 1 ATOM 2712 C CB . ALA B 1 93 ? 39.175 2.931 8.396 1.00 32.51 ? 93 ALA B CB 1 ATOM 2713 N N . ALA B 1 94 ? 35.935 3.012 8.297 1.00 29.97 ? 94 ALA B N 1 ATOM 2714 C CA . ALA B 1 94 ? 34.663 2.480 8.782 1.00 28.09 ? 94 ALA B CA 1 ATOM 2715 C C . ALA B 1 94 ? 33.732 2.177 7.611 1.00 27.37 ? 94 ALA B C 1 ATOM 2716 O O . ALA B 1 94 ? 33.080 1.135 7.571 1.00 25.81 ? 94 ALA B O 1 ATOM 2717 C CB . ALA B 1 94 ? 34.004 3.478 9.732 1.00 27.18 ? 94 ALA B CB 1 ATOM 2718 N N . TYR B 1 95 ? 33.672 3.101 6.661 1.00 26.72 ? 95 TYR B N 1 ATOM 2719 C CA . TYR B 1 95 ? 32.835 2.939 5.482 1.00 27.25 ? 95 TYR B CA 1 ATOM 2720 C C . TYR B 1 95 ? 33.186 1.638 4.757 1.00 28.64 ? 95 TYR B C 1 ATOM 2721 O O . TYR B 1 95 ? 32.313 0.951 4.228 1.00 28.50 ? 95 TYR B O 1 ATOM 2722 C CB . TYR B 1 95 ? 33.050 4.119 4.535 1.00 26.44 ? 95 TYR B CB 1 ATOM 2723 C CG . TYR B 1 95 ? 32.211 4.062 3.286 1.00 26.93 ? 95 TYR B CG 1 ATOM 2724 C CD1 . TYR B 1 95 ? 30.839 4.292 3.335 1.00 26.84 ? 95 TYR B CD1 1 ATOM 2725 C CD2 . TYR B 1 95 ? 32.785 3.772 2.051 1.00 27.73 ? 95 TYR B CD2 1 ATOM 2726 C CE1 . TYR B 1 95 ? 30.057 4.237 2.188 1.00 27.60 ? 95 TYR B CE1 1 ATOM 2727 C CE2 . TYR B 1 95 ? 32.012 3.712 0.896 1.00 27.83 ? 95 TYR B CE2 1 ATOM 2728 C CZ . TYR B 1 95 ? 30.649 3.948 0.973 1.00 28.69 ? 95 TYR B CZ 1 ATOM 2729 O OH . TYR B 1 95 ? 29.879 3.911 -0.169 1.00 31.54 ? 95 TYR B OH 1 ATOM 2730 N N . GLU B 1 96 ? 34.473 1.303 4.750 1.00 30.34 ? 96 GLU B N 1 ATOM 2731 C CA . GLU B 1 96 ? 34.954 0.103 4.075 1.00 32.34 ? 96 GLU B CA 1 ATOM 2732 C C . GLU B 1 96 ? 34.877 -1.184 4.898 1.00 30.78 ? 96 GLU B C 1 ATOM 2733 O O . GLU B 1 96 ? 34.553 -2.242 4.363 1.00 30.76 ? 96 GLU B O 1 ATOM 2734 C CB . GLU B 1 96 ? 36.406 0.303 3.615 1.00 35.08 ? 96 GLU B CB 1 ATOM 2735 C CG . GLU B 1 96 ? 36.637 1.466 2.647 1.00 41.75 ? 96 GLU B CG 1 ATOM 2736 C CD . GLU B 1 96 ? 35.783 1.382 1.384 1.00 46.13 ? 96 GLU B CD 1 ATOM 2737 O OE1 . GLU B 1 96 ? 35.623 0.267 0.836 1.00 49.18 ? 96 GLU B OE1 1 ATOM 2738 O OE2 . GLU B 1 96 ? 35.284 2.435 0.928 1.00 48.91 ? 96 GLU B OE2 1 ATOM 2739 N N . GLY B 1 97 ? 35.171 -1.095 6.192 1.00 30.38 ? 97 GLY B N 1 ATOM 2740 C CA . GLY B 1 97 ? 35.167 -2.278 7.039 1.00 28.75 ? 97 GLY B CA 1 ATOM 2741 C C . GLY B 1 97 ? 33.863 -2.772 7.648 1.00 28.56 ? 97 GLY B C 1 ATOM 2742 O O . GLY B 1 97 ? 33.812 -3.897 8.148 1.00 29.50 ? 97 GLY B O 1 ATOM 2743 N N . LEU B 1 98 ? 32.812 -1.957 7.618 1.00 26.42 ? 98 LEU B N 1 ATOM 2744 C CA . LEU B 1 98 ? 31.527 -2.350 8.199 1.00 25.11 ? 98 LEU B CA 1 ATOM 2745 C C . LEU B 1 98 ? 30.505 -2.775 7.144 1.00 24.87 ? 98 LEU B C 1 ATOM 2746 O O . LEU B 1 98 ? 30.548 -2.303 6.011 1.00 25.18 ? 98 LEU B O 1 ATOM 2747 C CB . LEU B 1 98 ? 30.953 -1.186 9.017 1.00 23.49 ? 98 LEU B CB 1 ATOM 2748 C CG . LEU B 1 98 ? 31.668 -0.831 10.320 1.00 22.13 ? 98 LEU B CG 1 ATOM 2749 C CD1 . LEU B 1 98 ? 31.296 0.572 10.780 1.00 20.43 ? 98 LEU B CD1 1 ATOM 2750 C CD2 . LEU B 1 98 ? 31.295 -1.867 11.361 1.00 23.28 ? 98 LEU B CD2 1 ATOM 2751 N N . PHE B 1 99 ? 29.592 -3.666 7.525 1.00 23.77 ? 99 PHE B N 1 ATOM 2752 C CA . PHE B 1 99 ? 28.537 -4.131 6.631 1.00 25.29 ? 99 PHE B CA 1 ATOM 2753 C C . PHE B 1 99 ? 29.061 -4.392 5.213 1.00 27.20 ? 99 PHE B C 1 ATOM 2754 O O . PHE B 1 99 ? 28.557 -3.820 4.241 1.00 26.86 ? 99 PHE B O 1 ATOM 2755 C CB . PHE B 1 99 ? 27.425 -3.076 6.577 1.00 24.49 ? 99 PHE B CB 1 ATOM 2756 C CG . PHE B 1 99 ? 26.996 -2.565 7.933 1.00 24.21 ? 99 PHE B CG 1 ATOM 2757 C CD1 . PHE B 1 99 ? 26.895 -1.193 8.172 1.00 22.72 ? 99 PHE B CD1 1 ATOM 2758 C CD2 . PHE B 1 99 ? 26.676 -3.449 8.962 1.00 22.39 ? 99 PHE B CD2 1 ATOM 2759 C CE1 . PHE B 1 99 ? 26.480 -0.708 9.412 1.00 21.72 ? 99 PHE B CE1 1 ATOM 2760 C CE2 . PHE B 1 99 ? 26.261 -2.973 10.204 1.00 22.89 ? 99 PHE B CE2 1 ATOM 2761 C CZ . PHE B 1 99 ? 26.162 -1.598 10.427 1.00 21.75 ? 99 PHE B CZ 1 ATOM 2762 N N . LYS B 1 100 ? 30.062 -5.263 5.102 1.00 29.68 ? 100 LYS B N 1 ATOM 2763 C CA . LYS B 1 100 ? 30.685 -5.587 3.817 1.00 30.38 ? 100 LYS B CA 1 ATOM 2764 C C . LYS B 1 100 ? 29.772 -6.167 2.737 1.00 29.14 ? 100 LYS B C 1 ATOM 2765 O O . LYS B 1 100 ? 29.871 -5.777 1.574 1.00 30.22 ? 100 LYS B O 1 ATOM 2766 C CB . LYS B 1 100 ? 31.878 -6.521 4.041 1.00 33.06 ? 100 LYS B CB 1 ATOM 2767 C CG . LYS B 1 100 ? 33.052 -5.844 4.735 1.00 36.55 ? 100 LYS B CG 1 ATOM 2768 C CD . LYS B 1 100 ? 34.050 -6.865 5.238 1.00 40.62 ? 100 LYS B CD 1 ATOM 2769 C CE . LYS B 1 100 ? 35.231 -6.196 5.919 1.00 43.27 ? 100 LYS B CE 1 ATOM 2770 N NZ . LYS B 1 100 ? 35.983 -5.322 4.970 1.00 45.44 ? 100 LYS B NZ 1 ATOM 2771 N N . ASN B 1 101 ? 28.893 -7.095 3.095 1.00 26.75 ? 101 ASN B N 1 ATOM 2772 C CA . ASN B 1 101 ? 28.004 -7.653 2.089 1.00 24.65 ? 101 ASN B CA 1 ATOM 2773 C C . ASN B 1 101 ? 26.668 -6.928 2.051 1.00 23.35 ? 101 ASN B C 1 ATOM 2774 O O . ASN B 1 101 ? 25.626 -7.480 2.401 1.00 21.95 ? 101 ASN B O 1 ATOM 2775 C CB . ASN B 1 101 ? 27.790 -9.154 2.311 1.00 26.75 ? 101 ASN B CB 1 ATOM 2776 C CG . ASN B 1 101 ? 29.058 -9.962 2.088 1.00 27.94 ? 101 ASN B CG 1 ATOM 2777 O OD1 . ASN B 1 101 ? 30.009 -9.491 1.467 1.00 27.52 ? 101 ASN B OD1 1 ATOM 2778 N ND2 . ASN B 1 101 ? 29.070 -11.192 2.586 1.00 31.14 ? 101 ASN B ND2 1 ATOM 2779 N N . THR B 1 102 ? 26.718 -5.674 1.620 1.00 21.85 ? 102 THR B N 1 ATOM 2780 C CA . THR B 1 102 ? 25.535 -4.838 1.496 1.00 20.81 ? 102 THR B CA 1 ATOM 2781 C C . THR B 1 102 ? 25.823 -3.830 0.395 1.00 22.41 ? 102 THR B C 1 ATOM 2782 O O . THR B 1 102 ? 26.985 -3.613 0.040 1.00 21.75 ? 102 THR B O 1 ATOM 2783 C CB . THR B 1 102 ? 25.253 -4.020 2.775 1.00 19.56 ? 102 THR B CB 1 ATOM 2784 O OG1 . THR B 1 102 ? 26.331 -3.099 2.992 1.00 19.72 ? 102 THR B OG1 1 ATOM 2785 C CG2 . THR B 1 102 ? 25.103 -4.922 3.985 1.00 17.36 ? 102 THR B CG2 1 ATOM 2786 N N . ILE B 1 103 ? 24.764 -3.235 -0.148 1.00 23.09 ? 103 ILE B N 1 ATOM 2787 C CA . ILE B 1 103 ? 24.890 -2.192 -1.162 1.00 23.56 ? 103 ILE B CA 1 ATOM 2788 C C . ILE B 1 103 ? 25.122 -0.922 -0.322 1.00 23.81 ? 103 ILE B C 1 ATOM 2789 O O . ILE B 1 103 ? 24.188 -0.409 0.301 1.00 25.03 ? 103 ILE B O 1 ATOM 2790 C CB . ILE B 1 103 ? 23.579 -2.044 -1.969 1.00 23.59 ? 103 ILE B CB 1 ATOM 2791 C CG1 . ILE B 1 103 ? 23.274 -3.345 -2.715 1.00 23.83 ? 103 ILE B CG1 1 ATOM 2792 C CG2 . ILE B 1 103 ? 23.685 -0.877 -2.939 1.00 22.13 ? 103 ILE B CG2 1 ATOM 2793 C CD1 . ILE B 1 103 ? 21.924 -3.342 -3.398 1.00 23.48 ? 103 ILE B CD1 1 ATOM 2794 N N . LYS B 1 104 ? 26.363 -0.436 -0.290 1.00 22.95 ? 104 LYS B N 1 ATOM 2795 C CA . LYS B 1 104 ? 26.715 0.739 0.507 1.00 22.43 ? 104 LYS B CA 1 ATOM 2796 C C . LYS B 1 104 ? 26.408 2.095 -0.110 1.00 23.41 ? 104 LYS B C 1 ATOM 2797 O O . LYS B 1 104 ? 26.569 2.309 -1.315 1.00 22.84 ? 104 LYS B O 1 ATOM 2798 C CB . LYS B 1 104 ? 28.198 0.698 0.895 1.00 22.01 ? 104 LYS B CB 1 ATOM 2799 C CG . LYS B 1 104 ? 28.575 -0.486 1.772 1.00 22.85 ? 104 LYS B CG 1 ATOM 2800 C CD . LYS B 1 104 ? 29.995 -0.370 2.302 1.00 23.07 ? 104 LYS B CD 1 ATOM 2801 C CE . LYS B 1 104 ? 30.316 -1.538 3.207 1.00 20.86 ? 104 LYS B CE 1 ATOM 2802 N NZ . LYS B 1 104 ? 31.676 -1.431 3.765 1.00 24.15 ? 104 LYS B NZ 1 ATOM 2803 N N . THR B 1 105 ? 25.984 3.015 0.750 1.00 22.31 ? 105 THR B N 1 ATOM 2804 C CA . THR B 1 105 ? 25.640 4.367 0.342 1.00 22.14 ? 105 THR B CA 1 ATOM 2805 C C . THR B 1 105 ? 26.155 5.374 1.353 1.00 23.07 ? 105 THR B C 1 ATOM 2806 O O . THR B 1 105 ? 25.860 5.263 2.544 1.00 21.95 ? 105 THR B O 1 ATOM 2807 C CB . THR B 1 105 ? 24.106 4.555 0.242 1.00 21.63 ? 105 THR B CB 1 ATOM 2808 O OG1 . THR B 1 105 ? 23.612 3.866 -0.911 1.00 22.29 ? 105 THR B OG1 1 ATOM 2809 C CG2 . THR B 1 105 ? 23.747 6.030 0.150 1.00 20.30 ? 105 THR B CG2 1 ATOM 2810 N N . ARG B 1 106 ? 26.940 6.344 0.889 1.00 22.65 ? 106 ARG B N 1 ATOM 2811 C CA . ARG B 1 106 ? 27.405 7.378 1.794 1.00 22.71 ? 106 ARG B CA 1 ATOM 2812 C C . ARG B 1 106 ? 26.409 8.528 1.664 1.00 22.38 ? 106 ARG B C 1 ATOM 2813 O O . ARG B 1 106 ? 26.246 9.100 0.580 1.00 22.85 ? 106 ARG B O 1 ATOM 2814 C CB . ARG B 1 106 ? 28.810 7.865 1.444 1.00 22.39 ? 106 ARG B CB 1 ATOM 2815 C CG . ARG B 1 106 ? 29.381 8.748 2.557 1.00 23.75 ? 106 ARG B CG 1 ATOM 2816 C CD . ARG B 1 106 ? 30.759 9.260 2.246 1.00 26.02 ? 106 ARG B CD 1 ATOM 2817 N NE . ARG B 1 106 ? 31.813 8.291 2.526 1.00 27.49 ? 106 ARG B NE 1 ATOM 2818 C CZ . ARG B 1 106 ? 32.306 8.046 3.735 1.00 28.32 ? 106 ARG B CZ 1 ATOM 2819 N NH1 . ARG B 1 106 ? 33.270 7.148 3.889 1.00 28.77 ? 106 ARG B NH1 1 ATOM 2820 N NH2 . ARG B 1 106 ? 31.837 8.697 4.789 1.00 28.52 ? 106 ARG B NH2 1 ATOM 2821 N N . LEU B 1 107 ? 25.727 8.846 2.762 1.00 21.25 ? 107 LEU B N 1 ATOM 2822 C CA . LEU B 1 107 ? 24.745 9.923 2.773 1.00 20.33 ? 107 LEU B CA 1 ATOM 2823 C C . LEU B 1 107 ? 25.400 11.276 2.477 1.00 20.87 ? 107 LEU B C 1 ATOM 2824 O O . LEU B 1 107 ? 26.598 11.473 2.727 1.00 19.40 ? 107 LEU B O 1 ATOM 2825 C CB . LEU B 1 107 ? 24.026 9.956 4.128 1.00 19.78 ? 107 LEU B CB 1 ATOM 2826 C CG . LEU B 1 107 ? 23.197 8.703 4.468 1.00 21.96 ? 107 LEU B CG 1 ATOM 2827 C CD1 . LEU B 1 107 ? 22.655 8.805 5.896 1.00 19.93 ? 107 LEU B CD1 1 ATOM 2828 C CD2 . LEU B 1 107 ? 22.040 8.549 3.471 1.00 20.46 ? 107 LEU B CD2 1 ATOM 2829 N N . HIS B 1 108 ? 24.616 12.207 1.938 1.00 20.83 ? 108 HIS B N 1 ATOM 2830 C CA . HIS B 1 108 ? 25.142 13.525 1.607 1.00 19.31 ? 108 HIS B CA 1 ATOM 2831 C C . HIS B 1 108 ? 25.269 14.416 2.834 1.00 18.93 ? 108 HIS B C 1 ATOM 2832 O O . HIS B 1 108 ? 25.894 15.471 2.780 1.00 20.13 ? 108 HIS B O 1 ATOM 2833 C CB . HIS B 1 108 ? 24.269 14.203 0.542 1.00 17.90 ? 108 HIS B CB 1 ATOM 2834 C CG . HIS B 1 108 ? 22.877 14.511 0.995 1.00 16.57 ? 108 HIS B CG 1 ATOM 2835 N ND1 . HIS B 1 108 ? 22.559 15.652 1.701 1.00 19.81 ? 108 HIS B ND1 1 ATOM 2836 C CD2 . HIS B 1 108 ? 21.714 13.838 0.825 1.00 15.31 ? 108 HIS B CD2 1 ATOM 2837 C CE1 . HIS B 1 108 ? 21.259 15.671 1.943 1.00 15.74 ? 108 HIS B CE1 1 ATOM 2838 N NE2 . HIS B 1 108 ? 20.723 14.581 1.422 1.00 16.70 ? 108 HIS B NE2 1 ATOM 2839 N N . PHE B 1 109 ? 24.689 13.987 3.947 1.00 18.07 ? 109 PHE B N 1 ATOM 2840 C CA . PHE B 1 109 ? 24.768 14.772 5.171 1.00 17.33 ? 109 PHE B CA 1 ATOM 2841 C C . PHE B 1 109 ? 25.530 14.047 6.271 1.00 17.36 ? 109 PHE B C 1 ATOM 2842 O O . PHE B 1 109 ? 25.628 12.815 6.275 1.00 18.20 ? 109 PHE B O 1 ATOM 2843 C CB . PHE B 1 109 ? 23.355 15.165 5.656 1.00 16.59 ? 109 PHE B CB 1 ATOM 2844 C CG . PHE B 1 109 ? 22.418 14.004 5.846 1.00 17.17 ? 109 PHE B CG 1 ATOM 2845 C CD1 . PHE B 1 109 ? 22.168 13.494 7.119 1.00 17.64 ? 109 PHE B CD1 1 ATOM 2846 C CD2 . PHE B 1 109 ? 21.771 13.429 4.755 1.00 18.11 ? 109 PHE B CD2 1 ATOM 2847 C CE1 . PHE B 1 109 ? 21.286 12.431 7.304 1.00 18.74 ? 109 PHE B CE1 1 ATOM 2848 C CE2 . PHE B 1 109 ? 20.887 12.364 4.925 1.00 19.22 ? 109 PHE B CE2 1 ATOM 2849 C CZ . PHE B 1 109 ? 20.643 11.864 6.205 1.00 19.56 ? 109 PHE B CZ 1 ATOM 2850 N N . GLY B 1 110 ? 26.081 14.826 7.195 1.00 16.59 ? 110 GLY B N 1 ATOM 2851 C CA . GLY B 1 110 ? 26.827 14.259 8.300 1.00 16.24 ? 110 GLY B CA 1 ATOM 2852 C C . GLY B 1 110 ? 25.933 13.869 9.455 1.00 14.85 ? 110 GLY B C 1 ATOM 2853 O O . GLY B 1 110 ? 24.719 14.037 9.391 1.00 14.51 ? 110 GLY B O 1 ATOM 2854 N N . GLY B 1 111 ? 26.541 13.352 10.519 1.00 17.46 ? 111 GLY B N 1 ATOM 2855 C CA . GLY B 1 111 ? 25.782 12.924 11.680 1.00 15.68 ? 111 GLY B CA 1 ATOM 2856 C C . GLY B 1 111 ? 25.686 13.910 12.833 1.00 16.31 ? 111 GLY B C 1 ATOM 2857 O O . GLY B 1 111 ? 25.094 13.590 13.866 1.00 17.83 ? 111 GLY B O 1 ATOM 2858 N N . SER B 1 112 ? 26.258 15.101 12.680 1.00 14.73 ? 112 SER B N 1 ATOM 2859 C CA . SER B 1 112 ? 26.192 16.101 13.741 1.00 14.65 ? 112 SER B CA 1 ATOM 2860 C C . SER B 1 112 ? 24.753 16.594 13.860 1.00 15.61 ? 112 SER B C 1 ATOM 2861 O O . SER B 1 112 ? 23.946 16.395 12.951 1.00 16.94 ? 112 SER B O 1 ATOM 2862 C CB . SER B 1 112 ? 27.104 17.288 13.417 1.00 14.66 ? 112 SER B CB 1 ATOM 2863 O OG . SER B 1 112 ? 26.600 18.034 12.316 1.00 16.39 ? 112 SER B OG 1 ATOM 2864 N N . TYR B 1 113 ? 24.421 17.241 14.971 1.00 15.03 ? 113 TYR B N 1 ATOM 2865 C CA . TYR B 1 113 ? 23.070 17.746 15.122 1.00 15.32 ? 113 TYR B CA 1 ATOM 2866 C C . TYR B 1 113 ? 22.793 18.842 14.090 1.00 15.68 ? 113 TYR B C 1 ATOM 2867 O O . TYR B 1 113 ? 21.735 18.859 13.462 1.00 15.74 ? 113 TYR B O 1 ATOM 2868 C CB . TYR B 1 113 ? 22.843 18.233 16.554 1.00 15.12 ? 113 TYR B CB 1 ATOM 2869 C CG . TYR B 1 113 ? 22.690 17.082 17.541 1.00 16.64 ? 113 TYR B CG 1 ATOM 2870 C CD1 . TYR B 1 113 ? 21.775 16.047 17.297 1.00 15.28 ? 113 TYR B CD1 1 ATOM 2871 C CD2 . TYR B 1 113 ? 23.437 17.036 18.725 1.00 14.91 ? 113 TYR B CD2 1 ATOM 2872 C CE1 . TYR B 1 113 ? 21.603 14.996 18.204 1.00 15.51 ? 113 TYR B CE1 1 ATOM 2873 C CE2 . TYR B 1 113 ? 23.267 15.986 19.645 1.00 17.28 ? 113 TYR B CE2 1 ATOM 2874 C CZ . TYR B 1 113 ? 22.347 14.973 19.375 1.00 16.16 ? 113 TYR B CZ 1 ATOM 2875 O OH . TYR B 1 113 ? 22.155 13.954 20.280 1.00 15.67 ? 113 TYR B OH 1 ATOM 2876 N N . PRO B 1 114 ? 23.737 19.776 13.898 1.00 17.36 ? 114 PRO B N 1 ATOM 2877 C CA . PRO B 1 114 ? 23.455 20.808 12.894 1.00 17.79 ? 114 PRO B CA 1 ATOM 2878 C C . PRO B 1 114 ? 23.260 20.214 11.498 1.00 18.39 ? 114 PRO B C 1 ATOM 2879 O O . PRO B 1 114 ? 22.442 20.703 10.713 1.00 18.53 ? 114 PRO B O 1 ATOM 2880 C CB . PRO B 1 114 ? 24.666 21.742 12.990 1.00 17.54 ? 114 PRO B CB 1 ATOM 2881 C CG . PRO B 1 114 ? 25.704 20.948 13.723 1.00 19.96 ? 114 PRO B CG 1 ATOM 2882 C CD . PRO B 1 114 ? 24.917 20.138 14.700 1.00 17.92 ? 114 PRO B CD 1 ATOM 2883 N N . SER B 1 115 ? 24.006 19.153 11.193 1.00 18.78 ? 115 SER B N 1 ATOM 2884 C CA . SER B 1 115 ? 23.878 18.501 9.895 1.00 18.55 ? 115 SER B CA 1 ATOM 2885 C C . SER B 1 115 ? 22.503 17.859 9.786 1.00 18.57 ? 115 SER B C 1 ATOM 2886 O O . SER B 1 115 ? 21.914 17.823 8.707 1.00 19.60 ? 115 SER B O 1 ATOM 2887 C CB . SER B 1 115 ? 24.949 17.427 9.716 1.00 19.31 ? 115 SER B CB 1 ATOM 2888 O OG . SER B 1 115 ? 26.242 17.999 9.695 1.00 22.12 ? 115 SER B OG 1 ATOM 2889 N N . LEU B 1 116 ? 21.988 17.353 10.906 1.00 17.07 ? 116 LEU B N 1 ATOM 2890 C CA . LEU B 1 116 ? 20.676 16.719 10.902 1.00 16.67 ? 116 LEU B CA 1 ATOM 2891 C C . LEU B 1 116 ? 19.561 17.762 10.763 1.00 17.55 ? 116 LEU B C 1 ATOM 2892 O O . LEU B 1 116 ? 18.520 17.481 10.161 1.00 16.70 ? 116 LEU B O 1 ATOM 2893 C CB . LEU B 1 116 ? 20.483 15.866 12.166 1.00 14.29 ? 116 LEU B CB 1 ATOM 2894 C CG . LEU B 1 116 ? 21.384 14.622 12.238 1.00 12.99 ? 116 LEU B CG 1 ATOM 2895 C CD1 . LEU B 1 116 ? 21.245 13.948 13.596 1.00 13.42 ? 116 LEU B CD1 1 ATOM 2896 C CD2 . LEU B 1 116 ? 21.021 13.650 11.117 1.00 11.60 ? 116 LEU B CD2 1 ATOM 2897 N N . GLU B 1 117 ? 19.777 18.964 11.302 1.00 17.29 ? 117 GLU B N 1 ATOM 2898 C CA . GLU B 1 117 ? 18.774 20.023 11.180 1.00 18.93 ? 117 GLU B CA 1 ATOM 2899 C C . GLU B 1 117 ? 18.716 20.456 9.708 1.00 20.27 ? 117 GLU B C 1 ATOM 2900 O O . GLU B 1 117 ? 17.695 20.958 9.229 1.00 19.39 ? 117 GLU B O 1 ATOM 2901 C CB . GLU B 1 117 ? 19.134 21.216 12.066 1.00 18.26 ? 117 GLU B CB 1 ATOM 2902 C CG . GLU B 1 117 ? 19.213 20.871 13.539 1.00 20.02 ? 117 GLU B CG 1 ATOM 2903 C CD . GLU B 1 117 ? 19.570 22.064 14.409 1.00 20.94 ? 117 GLU B CD 1 ATOM 2904 O OE1 . GLU B 1 117 ? 20.269 22.980 13.916 1.00 22.21 ? 117 GLU B OE1 1 ATOM 2905 O OE2 . GLU B 1 117 ? 19.166 22.074 15.593 1.00 21.00 ? 117 GLU B OE2 1 ATOM 2906 N N . GLY B 1 118 ? 19.827 20.254 9.003 1.00 20.02 ? 118 GLY B N 1 ATOM 2907 C CA . GLY B 1 118 ? 19.888 20.593 7.596 1.00 20.29 ? 118 GLY B CA 1 ATOM 2908 C C . GLY B 1 118 ? 18.913 19.713 6.844 1.00 22.25 ? 118 GLY B C 1 ATOM 2909 O O . GLY B 1 118 ? 18.528 20.014 5.716 1.00 23.44 ? 118 GLY B O 1 ATOM 2910 N N . GLU B 1 119 ? 18.520 18.607 7.468 1.00 21.69 ? 119 GLU B N 1 ATOM 2911 C CA . GLU B 1 119 ? 17.557 17.691 6.870 1.00 21.66 ? 119 GLU B CA 1 ATOM 2912 C C . GLU B 1 119 ? 16.236 17.780 7.623 1.00 20.59 ? 119 GLU B C 1 ATOM 2913 O O . GLU B 1 119 ? 15.457 16.829 7.646 1.00 21.01 ? 119 GLU B O 1 ATOM 2914 C CB . GLU B 1 119 ? 18.080 16.257 6.899 1.00 23.96 ? 119 GLU B CB 1 ATOM 2915 C CG . GLU B 1 119 ? 19.170 15.986 5.888 1.00 27.07 ? 119 GLU B CG 1 ATOM 2916 C CD . GLU B 1 119 ? 18.723 16.289 4.468 1.00 30.61 ? 119 GLU B CD 1 ATOM 2917 O OE1 . GLU B 1 119 ? 17.594 15.897 4.106 1.00 33.31 ? 119 GLU B OE1 1 ATOM 2918 O OE2 . GLU B 1 119 ? 19.497 16.912 3.708 1.00 32.10 ? 119 GLU B OE2 1 ATOM 2919 N N . LYS B 1 120 ? 16.016 18.928 8.256 1.00 19.25 ? 120 LYS B N 1 ATOM 2920 C CA . LYS B 1 120 ? 14.792 19.223 8.996 1.00 20.50 ? 120 LYS B CA 1 ATOM 2921 C C . LYS B 1 120 ? 14.514 18.418 10.262 1.00 19.64 ? 120 LYS B C 1 ATOM 2922 O O . LYS B 1 120 ? 13.374 18.367 10.730 1.00 19.29 ? 120 LYS B O 1 ATOM 2923 C CB . LYS B 1 120 ? 13.589 19.132 8.054 1.00 21.36 ? 120 LYS B CB 1 ATOM 2924 C CG . LYS B 1 120 ? 13.720 20.035 6.836 1.00 24.67 ? 120 LYS B CG 1 ATOM 2925 C CD . LYS B 1 120 ? 12.423 20.127 6.046 1.00 29.98 ? 120 LYS B CD 1 ATOM 2926 C CE . LYS B 1 120 ? 11.959 18.763 5.554 1.00 33.60 ? 120 LYS B CE 1 ATOM 2927 N NZ . LYS B 1 120 ? 10.799 18.873 4.611 1.00 37.58 ? 120 LYS B NZ 1 ATOM 2928 N N . ALA B 1 121 ? 15.552 17.800 10.818 1.00 17.65 ? 121 ALA B N 1 ATOM 2929 C CA . ALA B 1 121 ? 15.411 17.028 12.045 1.00 17.57 ? 121 ALA B CA 1 ATOM 2930 C C . ALA B 1 121 ? 15.969 17.860 13.207 1.00 18.60 ? 121 ALA B C 1 ATOM 2931 O O . ALA B 1 121 ? 17.186 18.014 13.352 1.00 20.10 ? 121 ALA B O 1 ATOM 2932 C CB . ALA B 1 121 ? 16.167 15.717 11.923 1.00 16.92 ? 121 ALA B CB 1 ATOM 2933 N N . TYR B 1 122 ? 15.073 18.395 14.029 1.00 17.40 ? 122 TYR B N 1 ATOM 2934 C CA . TYR B 1 122 ? 15.458 19.221 15.167 1.00 17.80 ? 122 TYR B CA 1 ATOM 2935 C C . TYR B 1 122 ? 15.129 18.516 16.469 1.00 17.44 ? 122 TYR B C 1 ATOM 2936 O O . TYR B 1 122 ? 14.067 17.903 16.605 1.00 16.80 ? 122 TYR B O 1 ATOM 2937 C CB . TYR B 1 122 ? 14.708 20.559 15.136 1.00 19.24 ? 122 TYR B CB 1 ATOM 2938 C CG . TYR B 1 122 ? 14.985 21.407 13.910 1.00 22.64 ? 122 TYR B CG 1 ATOM 2939 C CD1 . TYR B 1 122 ? 15.921 22.444 13.947 1.00 23.88 ? 122 TYR B CD1 1 ATOM 2940 C CD2 . TYR B 1 122 ? 14.314 21.170 12.709 1.00 23.29 ? 122 TYR B CD2 1 ATOM 2941 C CE1 . TYR B 1 122 ? 16.178 23.221 12.820 1.00 24.00 ? 122 TYR B CE1 1 ATOM 2942 C CE2 . TYR B 1 122 ? 14.564 21.938 11.580 1.00 24.13 ? 122 TYR B CE2 1 ATOM 2943 C CZ . TYR B 1 122 ? 15.494 22.960 11.643 1.00 25.40 ? 122 TYR B CZ 1 ATOM 2944 O OH . TYR B 1 122 ? 15.737 23.721 10.521 1.00 29.30 ? 122 TYR B OH 1 ATOM 2945 N N . ARG B 1 123 ? 16.040 18.619 17.431 1.00 17.98 ? 123 ARG B N 1 ATOM 2946 C CA . ARG B 1 123 ? 15.839 18.005 18.736 1.00 17.18 ? 123 ARG B CA 1 ATOM 2947 C C . ARG B 1 123 ? 14.604 18.565 19.433 1.00 18.38 ? 123 ARG B C 1 ATOM 2948 O O . ARG B 1 123 ? 13.828 17.819 20.028 1.00 18.92 ? 123 ARG B O 1 ATOM 2949 C CB . ARG B 1 123 ? 17.082 18.215 19.606 1.00 15.36 ? 123 ARG B CB 1 ATOM 2950 C CG . ARG B 1 123 ? 18.238 17.273 19.246 1.00 15.73 ? 123 ARG B CG 1 ATOM 2951 C CD . ARG B 1 123 ? 19.462 17.533 20.096 1.00 14.75 ? 123 ARG B CD 1 ATOM 2952 N NE . ARG B 1 123 ? 20.173 18.741 19.682 1.00 13.74 ? 123 ARG B NE 1 ATOM 2953 C CZ . ARG B 1 123 ? 21.185 19.268 20.360 1.00 13.46 ? 123 ARG B CZ 1 ATOM 2954 N NH1 . ARG B 1 123 ? 21.586 18.693 21.482 1.00 14.29 ? 123 ARG B NH1 1 ATOM 2955 N NH2 . ARG B 1 123 ? 21.803 20.356 19.914 1.00 12.73 ? 123 ARG B NH2 1 ATOM 2956 N N . GLU B 1 124 ? 14.418 19.880 19.337 1.00 20.76 ? 124 GLU B N 1 ATOM 2957 C CA . GLU B 1 124 ? 13.283 20.558 19.964 1.00 22.95 ? 124 GLU B CA 1 ATOM 2958 C C . GLU B 1 124 ? 11.936 19.998 19.520 1.00 21.77 ? 124 GLU B C 1 ATOM 2959 O O . GLU B 1 124 ? 11.003 19.918 20.314 1.00 22.79 ? 124 GLU B O 1 ATOM 2960 C CB . GLU B 1 124 ? 13.283 22.062 19.638 1.00 26.06 ? 124 GLU B CB 1 ATOM 2961 C CG . GLU B 1 124 ? 14.569 22.827 19.923 1.00 31.94 ? 124 GLU B CG 1 ATOM 2962 C CD . GLU B 1 124 ? 15.741 22.375 19.057 1.00 35.81 ? 124 GLU B CD 1 ATOM 2963 O OE1 . GLU B 1 124 ? 15.539 22.104 17.851 1.00 36.09 ? 124 GLU B OE1 1 ATOM 2964 O OE2 . GLU B 1 124 ? 16.875 22.304 19.585 1.00 41.33 ? 124 GLU B OE2 1 ATOM 2965 N N . THR B 1 125 ? 11.843 19.608 18.253 1.00 20.90 ? 125 THR B N 1 ATOM 2966 C CA . THR B 1 125 ? 10.585 19.117 17.700 1.00 21.41 ? 125 THR B CA 1 ATOM 2967 C C . THR B 1 125 ? 10.485 17.622 17.393 1.00 20.90 ? 125 THR B C 1 ATOM 2968 O O . THR B 1 125 ? 9.593 17.200 16.666 1.00 22.27 ? 125 THR B O 1 ATOM 2969 C CB . THR B 1 125 ? 10.238 19.908 16.414 1.00 20.62 ? 125 THR B CB 1 ATOM 2970 O OG1 . THR B 1 125 ? 11.294 19.764 15.456 1.00 22.62 ? 125 THR B OG1 1 ATOM 2971 C CG2 . THR B 1 125 ? 10.084 21.381 16.731 1.00 22.20 ? 125 THR B CG2 1 ATOM 2972 N N . THR B 1 126 ? 11.378 16.816 17.951 1.00 20.69 ? 126 THR B N 1 ATOM 2973 C CA . THR B 1 126 ? 11.340 15.380 17.689 1.00 19.24 ? 126 THR B CA 1 ATOM 2974 C C . THR B 1 126 ? 11.002 14.577 18.940 1.00 18.98 ? 126 THR B C 1 ATOM 2975 O O . THR B 1 126 ? 11.743 14.591 19.923 1.00 17.84 ? 126 THR B O 1 ATOM 2976 C CB . THR B 1 126 ? 12.687 14.895 17.108 1.00 19.79 ? 126 THR B CB 1 ATOM 2977 O OG1 . THR B 1 126 ? 12.876 15.473 15.808 1.00 18.29 ? 126 THR B OG1 1 ATOM 2978 C CG2 . THR B 1 126 ? 12.718 13.368 17.009 1.00 18.08 ? 126 THR B CG2 1 ATOM 2979 N N . ASP B 1 127 ? 9.869 13.886 18.895 1.00 19.29 ? 127 ASP B N 1 ATOM 2980 C CA . ASP B 1 127 ? 9.409 13.067 20.014 1.00 20.44 ? 127 ASP B CA 1 ATOM 2981 C C . ASP B 1 127 ? 10.344 11.888 20.274 1.00 18.91 ? 127 ASP B C 1 ATOM 2982 O O . ASP B 1 127 ? 10.946 11.338 19.349 1.00 18.02 ? 127 ASP B O 1 ATOM 2983 C CB . ASP B 1 127 ? 8.010 12.504 19.730 1.00 22.37 ? 127 ASP B CB 1 ATOM 2984 C CG . ASP B 1 127 ? 6.917 13.563 19.775 1.00 28.08 ? 127 ASP B CG 1 ATOM 2985 O OD1 . ASP B 1 127 ? 5.785 13.252 19.341 1.00 29.56 ? 127 ASP B OD1 1 ATOM 2986 O OD2 . ASP B 1 127 ? 7.172 14.693 20.249 1.00 28.99 ? 127 ASP B OD2 1 ATOM 2987 N N . LEU B 1 128 ? 10.456 11.507 21.541 1.00 17.26 ? 128 LEU B N 1 ATOM 2988 C CA . LEU B 1 128 ? 11.268 10.364 21.929 1.00 16.83 ? 128 LEU B CA 1 ATOM 2989 C C . LEU B 1 128 ? 10.354 9.499 22.786 1.00 16.48 ? 128 LEU B C 1 ATOM 2990 O O . LEU B 1 128 ? 9.436 10.007 23.424 1.00 16.09 ? 128 LEU B O 1 ATOM 2991 C CB . LEU B 1 128 ? 12.492 10.806 22.737 1.00 15.81 ? 128 LEU B CB 1 ATOM 2992 C CG . LEU B 1 128 ? 13.462 11.773 22.060 1.00 15.72 ? 128 LEU B CG 1 ATOM 2993 C CD1 . LEU B 1 128 ? 14.575 12.099 23.034 1.00 13.38 ? 128 LEU B CD1 1 ATOM 2994 C CD2 . LEU B 1 128 ? 14.026 11.164 20.781 1.00 13.03 ? 128 LEU B CD2 1 ATOM 2995 N N . GLY B 1 129 ? 10.603 8.196 22.797 1.00 16.27 ? 129 GLY B N 1 ATOM 2996 C CA . GLY B 1 129 ? 9.770 7.288 23.562 1.00 15.80 ? 129 GLY B CA 1 ATOM 2997 C C . GLY B 1 129 ? 9.735 5.984 22.794 1.00 17.34 ? 129 GLY B C 1 ATOM 2998 O O . GLY B 1 129 ? 10.265 5.914 21.678 1.00 17.02 ? 129 GLY B O 1 ATOM 2999 N N . ILE B 1 130 ? 9.112 4.955 23.360 1.00 16.18 ? 130 ILE B N 1 ATOM 3000 C CA . ILE B 1 130 ? 9.063 3.659 22.691 1.00 16.60 ? 130 ILE B CA 1 ATOM 3001 C C . ILE B 1 130 ? 8.319 3.672 21.350 1.00 17.81 ? 130 ILE B C 1 ATOM 3002 O O . ILE B 1 130 ? 8.736 3.007 20.400 1.00 17.48 ? 130 ILE B O 1 ATOM 3003 C CB . ILE B 1 130 ? 8.453 2.575 23.622 1.00 16.14 ? 130 ILE B CB 1 ATOM 3004 C CG1 . ILE B 1 130 ? 8.616 1.195 22.978 1.00 16.50 ? 130 ILE B CG1 1 ATOM 3005 C CG2 . ILE B 1 130 ? 6.980 2.884 23.912 1.00 16.15 ? 130 ILE B CG2 1 ATOM 3006 C CD1 . ILE B 1 130 ? 10.071 0.838 22.631 1.00 14.57 ? 130 ILE B CD1 1 ATOM 3007 N N . GLU B 1 131 ? 7.230 4.432 21.264 1.00 18.17 ? 131 GLU B N 1 ATOM 3008 C CA . GLU B 1 131 ? 6.468 4.500 20.024 1.00 19.88 ? 131 GLU B CA 1 ATOM 3009 C C . GLU B 1 131 ? 7.299 5.222 18.935 1.00 20.52 ? 131 GLU B C 1 ATOM 3010 O O . GLU B 1 131 ? 7.367 4.761 17.791 1.00 20.11 ? 131 GLU B O 1 ATOM 3011 C CB . GLU B 1 131 ? 5.122 5.187 20.284 1.00 22.59 ? 131 GLU B CB 1 ATOM 3012 C CG . GLU B 1 131 ? 4.049 4.947 19.216 1.00 27.05 ? 131 GLU B CG 1 ATOM 3013 C CD . GLU B 1 131 ? 3.823 3.471 18.889 1.00 29.61 ? 131 GLU B CD 1 ATOM 3014 O OE1 . GLU B 1 131 ? 3.770 2.631 19.821 1.00 29.05 ? 131 GLU B OE1 1 ATOM 3015 O OE2 . GLU B 1 131 ? 3.685 3.155 17.686 1.00 31.10 ? 131 GLU B OE2 1 ATOM 3016 N N . PRO B 1 132 ? 7.928 6.368 19.267 1.00 20.46 ? 132 PRO B N 1 ATOM 3017 C CA . PRO B 1 132 ? 8.728 7.025 18.223 1.00 20.20 ? 132 PRO B CA 1 ATOM 3018 C C . PRO B 1 132 ? 9.933 6.181 17.795 1.00 18.88 ? 132 PRO B C 1 ATOM 3019 O O . PRO B 1 132 ? 10.449 6.347 16.692 1.00 18.61 ? 132 PRO B O 1 ATOM 3020 C CB . PRO B 1 132 ? 9.130 8.364 18.857 1.00 22.09 ? 132 PRO B CB 1 ATOM 3021 C CG . PRO B 1 132 ? 8.846 8.193 20.319 1.00 23.13 ? 132 PRO B CG 1 ATOM 3022 C CD . PRO B 1 132 ? 7.646 7.304 20.366 1.00 20.08 ? 132 PRO B CD 1 ATOM 3023 N N . LEU B 1 133 ? 10.378 5.274 18.663 1.00 17.17 ? 133 LEU B N 1 ATOM 3024 C CA . LEU B 1 133 ? 11.490 4.387 18.317 1.00 15.80 ? 133 LEU B CA 1 ATOM 3025 C C . LEU B 1 133 ? 10.983 3.329 17.333 1.00 16.27 ? 133 LEU B C 1 ATOM 3026 O O . LEU B 1 133 ? 11.672 2.972 16.378 1.00 15.91 ? 133 LEU B O 1 ATOM 3027 C CB . LEU B 1 133 ? 12.046 3.695 19.561 1.00 14.43 ? 133 LEU B CB 1 ATOM 3028 C CG . LEU B 1 133 ? 13.178 2.701 19.274 1.00 13.44 ? 133 LEU B CG 1 ATOM 3029 C CD1 . LEU B 1 133 ? 14.290 3.383 18.477 1.00 11.98 ? 133 LEU B CD1 1 ATOM 3030 C CD2 . LEU B 1 133 ? 13.718 2.156 20.585 1.00 13.82 ? 133 LEU B CD2 1 ATOM 3031 N N . ARG B 1 134 ? 9.774 2.827 17.580 1.00 17.88 ? 134 ARG B N 1 ATOM 3032 C CA . ARG B 1 134 ? 9.159 1.826 16.709 1.00 18.57 ? 134 ARG B CA 1 ATOM 3033 C C . ARG B 1 134 ? 8.992 2.411 15.310 1.00 18.00 ? 134 ARG B C 1 ATOM 3034 O O . ARG B 1 134 ? 9.292 1.758 14.306 1.00 18.19 ? 134 ARG B O 1 ATOM 3035 C CB . ARG B 1 134 ? 7.784 1.403 17.249 1.00 16.93 ? 134 ARG B CB 1 ATOM 3036 C CG . ARG B 1 134 ? 7.833 0.508 18.468 1.00 18.92 ? 134 ARG B CG 1 ATOM 3037 C CD . ARG B 1 134 ? 6.431 0.104 18.911 1.00 20.39 ? 134 ARG B CD 1 ATOM 3038 N NE . ARG B 1 134 ? 6.449 -0.781 20.073 1.00 20.18 ? 134 ARG B NE 1 ATOM 3039 C CZ . ARG B 1 134 ? 5.788 -0.545 21.205 1.00 22.12 ? 134 ARG B CZ 1 ATOM 3040 N NH1 . ARG B 1 134 ? 5.049 0.552 21.331 1.00 21.12 ? 134 ARG B NH1 1 ATOM 3041 N NH2 . ARG B 1 134 ? 5.870 -1.403 22.216 1.00 21.24 ? 134 ARG B NH2 1 ATOM 3042 N N . ILE B 1 135 ? 8.513 3.648 15.258 1.00 17.69 ? 135 ILE B N 1 ATOM 3043 C CA . ILE B 1 135 ? 8.299 4.350 13.995 1.00 17.73 ? 135 ILE B CA 1 ATOM 3044 C C . ILE B 1 135 ? 9.625 4.652 13.300 1.00 17.36 ? 135 ILE B C 1 ATOM 3045 O O . ILE B 1 135 ? 9.734 4.544 12.075 1.00 18.50 ? 135 ILE B O 1 ATOM 3046 C CB . ILE B 1 135 ? 7.539 5.663 14.241 1.00 19.01 ? 135 ILE B CB 1 ATOM 3047 C CG1 . ILE B 1 135 ? 6.145 5.343 14.793 1.00 18.23 ? 135 ILE B CG1 1 ATOM 3048 C CG2 . ILE B 1 135 ? 7.464 6.482 12.957 1.00 19.02 ? 135 ILE B CG2 1 ATOM 3049 C CD1 . ILE B 1 135 ? 5.403 6.559 15.300 1.00 19.42 ? 135 ILE B CD1 1 ATOM 3050 N N . GLY B 1 136 ? 10.628 5.035 14.083 1.00 16.24 ? 136 GLY B N 1 ATOM 3051 C CA . GLY B 1 136 ? 11.936 5.319 13.517 1.00 17.29 ? 136 GLY B CA 1 ATOM 3052 C C . GLY B 1 136 ? 12.548 4.081 12.882 1.00 17.26 ? 136 GLY B C 1 ATOM 3053 O O . GLY B 1 136 ? 13.159 4.158 11.815 1.00 18.59 ? 136 GLY B O 1 ATOM 3054 N N . ILE B 1 137 ? 12.396 2.935 13.540 1.00 16.90 ? 137 ILE B N 1 ATOM 3055 C CA . ILE B 1 137 ? 12.920 1.678 13.008 1.00 17.68 ? 137 ILE B CA 1 ATOM 3056 C C . ILE B 1 137 ? 12.145 1.343 11.731 1.00 19.04 ? 137 ILE B C 1 ATOM 3057 O O . ILE B 1 137 ? 12.722 0.906 10.737 1.00 18.88 ? 137 ILE B O 1 ATOM 3058 C CB . ILE B 1 137 ? 12.744 0.517 14.022 1.00 18.37 ? 137 ILE B CB 1 ATOM 3059 C CG1 . ILE B 1 137 ? 13.619 0.768 15.263 1.00 16.07 ? 137 ILE B CG1 1 ATOM 3060 C CG2 . ILE B 1 137 ? 13.060 -0.818 13.340 1.00 15.61 ? 137 ILE B CG2 1 ATOM 3061 C CD1 . ILE B 1 137 ? 13.274 -0.112 16.466 1.00 14.63 ? 137 ILE B CD1 1 ATOM 3062 N N . LYS B 1 138 ? 10.833 1.560 11.775 1.00 19.50 ? 138 LYS B N 1 ATOM 3063 C CA . LYS B 1 138 ? 9.961 1.305 10.636 1.00 20.16 ? 138 LYS B CA 1 ATOM 3064 C C . LYS B 1 138 ? 10.378 2.128 9.416 1.00 19.57 ? 138 LYS B C 1 ATOM 3065 O O . LYS B 1 138 ? 10.467 1.607 8.307 1.00 19.34 ? 138 LYS B O 1 ATOM 3066 C CB . LYS B 1 138 ? 8.508 1.642 10.996 1.00 20.57 ? 138 LYS B CB 1 ATOM 3067 C CG . LYS B 1 138 ? 7.506 1.268 9.904 1.00 24.08 ? 138 LYS B CG 1 ATOM 3068 C CD . LYS B 1 138 ? 6.093 1.733 10.221 1.00 27.82 ? 138 LYS B CD 1 ATOM 3069 C CE . LYS B 1 138 ? 5.958 3.244 10.065 1.00 31.52 ? 138 LYS B CE 1 ATOM 3070 N NZ . LYS B 1 138 ? 4.584 3.734 10.382 1.00 34.08 ? 138 LYS B NZ 1 ATOM 3071 N N . LYS B 1 139 ? 10.629 3.415 9.623 1.00 19.53 ? 139 LYS B N 1 ATOM 3072 C CA . LYS B 1 139 ? 11.024 4.290 8.529 1.00 20.36 ? 139 LYS B CA 1 ATOM 3073 C C . LYS B 1 139 ? 12.418 4.002 7.963 1.00 19.77 ? 139 LYS B C 1 ATOM 3074 O O . LYS B 1 139 ? 12.650 4.166 6.765 1.00 19.83 ? 139 LYS B O 1 ATOM 3075 C CB . LYS B 1 139 ? 10.923 5.749 8.972 1.00 21.33 ? 139 LYS B CB 1 ATOM 3076 C CG . LYS B 1 139 ? 9.506 6.202 9.168 1.00 22.58 ? 139 LYS B CG 1 ATOM 3077 C CD . LYS B 1 139 ? 9.457 7.630 9.638 1.00 26.91 ? 139 LYS B CD 1 ATOM 3078 C CE . LYS B 1 139 ? 8.028 8.040 9.964 1.00 30.72 ? 139 LYS B CE 1 ATOM 3079 N NZ . LYS B 1 139 ? 7.962 9.394 10.598 1.00 33.53 ? 139 LYS B NZ 1 ATOM 3080 N N . LEU B 1 140 ? 13.349 3.582 8.809 1.00 17.97 ? 140 LEU B N 1 ATOM 3081 C CA . LEU B 1 140 ? 14.680 3.269 8.316 1.00 18.20 ? 140 LEU B CA 1 ATOM 3082 C C . LEU B 1 140 ? 14.569 2.046 7.425 1.00 19.07 ? 140 LEU B C 1 ATOM 3083 O O . LEU B 1 140 ? 15.245 1.941 6.405 1.00 19.59 ? 140 LEU B O 1 ATOM 3084 C CB . LEU B 1 140 ? 15.642 2.976 9.470 1.00 16.37 ? 140 LEU B CB 1 ATOM 3085 C CG . LEU B 1 140 ? 16.137 4.172 10.291 1.00 14.51 ? 140 LEU B CG 1 ATOM 3086 C CD1 . LEU B 1 140 ? 17.056 3.672 11.409 1.00 14.79 ? 140 LEU B CD1 1 ATOM 3087 C CD2 . LEU B 1 140 ? 16.879 5.163 9.387 1.00 12.08 ? 140 LEU B CD2 1 ATOM 3088 N N . ASP B 1 141 ? 13.703 1.120 7.814 1.00 20.15 ? 141 ASP B N 1 ATOM 3089 C CA . ASP B 1 141 ? 13.519 -0.098 7.038 1.00 22.27 ? 141 ASP B CA 1 ATOM 3090 C C . ASP B 1 141 ? 12.805 0.184 5.721 1.00 22.50 ? 141 ASP B C 1 ATOM 3091 O O . ASP B 1 141 ? 13.171 -0.357 4.683 1.00 22.57 ? 141 ASP B O 1 ATOM 3092 C CB . ASP B 1 141 ? 12.742 -1.142 7.848 1.00 23.04 ? 141 ASP B CB 1 ATOM 3093 C CG . ASP B 1 141 ? 12.455 -2.406 7.045 1.00 26.12 ? 141 ASP B CG 1 ATOM 3094 O OD1 . ASP B 1 141 ? 11.342 -2.517 6.485 1.00 26.59 ? 141 ASP B OD1 1 ATOM 3095 O OD2 . ASP B 1 141 ? 13.348 -3.277 6.956 1.00 26.00 ? 141 ASP B OD2 1 ATOM 3096 N N . GLU B 1 142 ? 11.791 1.038 5.764 1.00 23.23 ? 142 GLU B N 1 ATOM 3097 C CA . GLU B 1 142 ? 11.049 1.383 4.564 1.00 24.99 ? 142 GLU B CA 1 ATOM 3098 C C . GLU B 1 142 ? 11.920 2.151 3.571 1.00 25.77 ? 142 GLU B C 1 ATOM 3099 O O . GLU B 1 142 ? 11.664 2.123 2.365 1.00 26.13 ? 142 GLU B O 1 ATOM 3100 C CB . GLU B 1 142 ? 9.819 2.216 4.932 1.00 27.74 ? 142 GLU B CB 1 ATOM 3101 C CG . GLU B 1 142 ? 8.739 1.422 5.657 1.00 30.55 ? 142 GLU B CG 1 ATOM 3102 C CD . GLU B 1 142 ? 7.579 2.290 6.115 1.00 33.82 ? 142 GLU B CD 1 ATOM 3103 O OE1 . GLU B 1 142 ? 6.601 1.725 6.654 1.00 35.31 ? 142 GLU B OE1 1 ATOM 3104 O OE2 . GLU B 1 142 ? 7.648 3.532 5.941 1.00 35.10 ? 142 GLU B OE2 1 ATOM 3105 N N . ASN B 1 143 ? 12.951 2.828 4.075 1.00 25.20 ? 143 ASN B N 1 ATOM 3106 C CA . ASN B 1 143 ? 13.844 3.601 3.216 1.00 23.84 ? 143 ASN B CA 1 ATOM 3107 C C . ASN B 1 143 ? 15.115 2.847 2.823 1.00 24.07 ? 143 ASN B C 1 ATOM 3108 O O . ASN B 1 143 ? 16.115 3.450 2.432 1.00 24.86 ? 143 ASN B O 1 ATOM 3109 C CB . ASN B 1 143 ? 14.194 4.933 3.886 1.00 21.92 ? 143 ASN B CB 1 ATOM 3110 C CG . ASN B 1 143 ? 13.076 5.962 3.754 1.00 22.11 ? 143 ASN B CG 1 ATOM 3111 O OD1 . ASN B 1 143 ? 12.923 6.604 2.708 1.00 20.54 ? 143 ASN B OD1 1 ATOM 3112 N ND2 . ASN B 1 143 ? 12.284 6.115 4.809 1.00 19.19 ? 143 ASN B ND2 1 ATOM 3113 N N . ALA B 1 144 ? 15.072 1.523 2.943 1.00 24.67 ? 144 ALA B N 1 ATOM 3114 C CA . ALA B 1 144 ? 16.199 0.685 2.552 1.00 26.38 ? 144 ALA B CA 1 ATOM 3115 C C . ALA B 1 144 ? 15.936 0.491 1.071 1.00 28.29 ? 144 ALA B C 1 ATOM 3116 O O . ALA B 1 144 ? 15.631 -0.613 0.614 1.00 28.62 ? 144 ALA B O 1 ATOM 3117 C CB . ALA B 1 144 ? 16.158 -0.656 3.279 1.00 25.82 ? 144 ALA B CB 1 ATOM 3118 N N . ILE B 1 145 ? 16.025 1.594 0.335 1.00 29.40 ? 145 ILE B N 1 ATOM 3119 C CA . ILE B 1 145 ? 15.772 1.599 -1.095 1.00 30.47 ? 145 ILE B CA 1 ATOM 3120 C C . ILE B 1 145 ? 16.707 2.587 -1.782 1.00 32.14 ? 145 ILE B C 1 ATOM 3121 O O . ILE B 1 145 ? 17.446 3.314 -1.123 1.00 32.32 ? 145 ILE B O 1 ATOM 3122 C CB . ILE B 1 145 ? 14.312 2.014 -1.372 1.00 29.51 ? 145 ILE B CB 1 ATOM 3123 C CG1 . ILE B 1 145 ? 14.062 3.418 -0.819 1.00 28.36 ? 145 ILE B CG1 1 ATOM 3124 C CG2 . ILE B 1 145 ? 13.355 1.020 -0.725 1.00 28.50 ? 145 ILE B CG2 1 ATOM 3125 C CD1 . ILE B 1 145 ? 12.622 3.869 -0.910 1.00 28.54 ? 145 ILE B CD1 1 ATOM 3126 N N . ASP B 1 146 ? 16.670 2.610 -3.109 1.00 33.94 ? 146 ASP B N 1 ATOM 3127 C CA . ASP B 1 146 ? 17.509 3.518 -3.870 1.00 35.60 ? 146 ASP B CA 1 ATOM 3128 C C . ASP B 1 146 ? 17.021 4.952 -3.718 1.00 35.02 ? 146 ASP B C 1 ATOM 3129 O O . ASP B 1 146 ? 17.812 5.870 -3.488 1.00 34.34 ? 146 ASP B O 1 ATOM 3130 C CB . ASP B 1 146 ? 17.493 3.129 -5.349 1.00 41.90 ? 146 ASP B CB 1 ATOM 3131 C CG . ASP B 1 146 ? 18.192 1.809 -5.613 1.00 47.19 ? 146 ASP B CG 1 ATOM 3132 O OD1 . ASP B 1 146 ? 19.442 1.766 -5.504 1.00 50.15 ? 146 ASP B OD1 1 ATOM 3133 O OD2 . ASP B 1 146 ? 17.491 0.815 -5.922 1.00 50.72 ? 146 ASP B OD2 1 ATOM 3134 N N . ASN B 1 147 ? 15.714 5.148 -3.851 1.00 34.39 ? 147 ASN B N 1 ATOM 3135 C CA . ASN B 1 147 ? 15.156 6.488 -3.733 1.00 34.71 ? 147 ASN B CA 1 ATOM 3136 C C . ASN B 1 147 ? 14.673 6.764 -2.310 1.00 33.57 ? 147 ASN B C 1 ATOM 3137 O O . ASN B 1 147 ? 13.497 7.057 -2.086 1.00 32.93 ? 147 ASN B O 1 ATOM 3138 C CB . ASN B 1 147 ? 14.000 6.670 -4.718 1.00 36.94 ? 147 ASN B CB 1 ATOM 3139 C CG . ASN B 1 147 ? 13.620 8.131 -4.905 1.00 40.41 ? 147 ASN B CG 1 ATOM 3140 O OD1 . ASN B 1 147 ? 12.638 8.448 -5.583 1.00 43.98 ? 147 ASN B OD1 1 ATOM 3141 N ND2 . ASN B 1 147 ? 14.402 9.030 -4.309 1.00 41.09 ? 147 ASN B ND2 1 ATOM 3142 N N . TYR B 1 148 ? 15.593 6.669 -1.354 1.00 31.24 ? 148 TYR B N 1 ATOM 3143 C CA . TYR B 1 148 ? 15.283 6.906 0.048 1.00 28.65 ? 148 TYR B CA 1 ATOM 3144 C C . TYR B 1 148 ? 14.988 8.383 0.312 1.00 27.32 ? 148 TYR B C 1 ATOM 3145 O O . TYR B 1 148 ? 15.462 9.257 -0.416 1.00 24.29 ? 148 TYR B O 1 ATOM 3146 C CB . TYR B 1 148 ? 16.460 6.446 0.919 1.00 28.49 ? 148 TYR B CB 1 ATOM 3147 C CG . TYR B 1 148 ? 17.784 7.091 0.555 1.00 27.70 ? 148 TYR B CG 1 ATOM 3148 C CD1 . TYR B 1 148 ? 18.119 8.373 1.011 1.00 25.64 ? 148 TYR B CD1 1 ATOM 3149 C CD2 . TYR B 1 148 ? 18.690 6.433 -0.283 1.00 26.61 ? 148 TYR B CD2 1 ATOM 3150 C CE1 . TYR B 1 148 ? 19.328 8.981 0.636 1.00 25.50 ? 148 TYR B CE1 1 ATOM 3151 C CE2 . TYR B 1 148 ? 19.894 7.029 -0.665 1.00 25.09 ? 148 TYR B CE2 1 ATOM 3152 C CZ . TYR B 1 148 ? 20.207 8.300 -0.207 1.00 25.82 ? 148 TYR B CZ 1 ATOM 3153 O OH . TYR B 1 148 ? 21.385 8.886 -0.619 1.00 26.32 ? 148 TYR B OH 1 ATOM 3154 N N . LYS B 1 149 ? 14.190 8.644 1.348 1.00 26.19 ? 149 LYS B N 1 ATOM 3155 C CA . LYS B 1 149 ? 13.849 10.004 1.746 1.00 25.52 ? 149 LYS B CA 1 ATOM 3156 C C . LYS B 1 149 ? 14.830 10.388 2.851 1.00 25.17 ? 149 LYS B C 1 ATOM 3157 O O . LYS B 1 149 ? 14.755 9.868 3.963 1.00 24.00 ? 149 LYS B O 1 ATOM 3158 C CB . LYS B 1 149 ? 12.430 10.073 2.310 1.00 27.45 ? 149 LYS B CB 1 ATOM 3159 C CG . LYS B 1 149 ? 11.327 9.625 1.371 1.00 31.79 ? 149 LYS B CG 1 ATOM 3160 C CD . LYS B 1 149 ? 9.963 9.800 2.034 1.00 34.58 ? 149 LYS B CD 1 ATOM 3161 C CE . LYS B 1 149 ? 8.836 9.238 1.185 1.00 37.23 ? 149 LYS B CE 1 ATOM 3162 N NZ . LYS B 1 149 ? 7.517 9.348 1.887 1.00 39.61 ? 149 LYS B NZ 1 ATOM 3163 N N . PRO B 1 150 ? 15.770 11.297 2.559 1.00 25.01 ? 150 PRO B N 1 ATOM 3164 C CA . PRO B 1 150 ? 16.735 11.700 3.581 1.00 24.08 ? 150 PRO B CA 1 ATOM 3165 C C . PRO B 1 150 ? 16.126 12.350 4.823 1.00 22.62 ? 150 PRO B C 1 ATOM 3166 O O . PRO B 1 150 ? 16.684 12.240 5.904 1.00 21.86 ? 150 PRO B O 1 ATOM 3167 C CB . PRO B 1 150 ? 17.676 12.637 2.816 1.00 25.47 ? 150 PRO B CB 1 ATOM 3168 C CG . PRO B 1 150 ? 16.804 13.196 1.738 1.00 24.38 ? 150 PRO B CG 1 ATOM 3169 C CD . PRO B 1 150 ? 16.045 11.980 1.283 1.00 25.37 ? 150 PRO B CD 1 ATOM 3170 N N . THR B 1 151 ? 14.988 13.021 4.683 1.00 21.89 ? 151 THR B N 1 ATOM 3171 C CA . THR B 1 151 ? 14.375 13.660 5.842 1.00 21.17 ? 151 THR B CA 1 ATOM 3172 C C . THR B 1 151 ? 13.802 12.623 6.810 1.00 20.51 ? 151 THR B C 1 ATOM 3173 O O . THR B 1 151 ? 13.772 12.844 8.025 1.00 19.79 ? 151 THR B O 1 ATOM 3174 C CB . THR B 1 151 ? 13.251 14.662 5.437 1.00 22.02 ? 151 THR B CB 1 ATOM 3175 O OG1 . THR B 1 151 ? 12.215 13.976 4.728 1.00 25.04 ? 151 THR B OG1 1 ATOM 3176 C CG2 . THR B 1 151 ? 13.813 15.770 4.569 1.00 19.58 ? 151 THR B CG2 1 ATOM 3177 N N . GLU B 1 152 ? 13.349 11.494 6.271 1.00 19.24 ? 152 GLU B N 1 ATOM 3178 C CA . GLU B 1 152 ? 12.793 10.433 7.103 1.00 18.81 ? 152 GLU B CA 1 ATOM 3179 C C . GLU B 1 152 ? 13.915 9.667 7.785 1.00 16.97 ? 152 GLU B C 1 ATOM 3180 O O . GLU B 1 152 ? 13.754 9.185 8.902 1.00 17.09 ? 152 GLU B O 1 ATOM 3181 C CB . GLU B 1 152 ? 11.939 9.479 6.266 1.00 20.14 ? 152 GLU B CB 1 ATOM 3182 C CG . GLU B 1 152 ? 10.604 10.065 5.841 1.00 23.69 ? 152 GLU B CG 1 ATOM 3183 C CD . GLU B 1 152 ? 9.681 9.037 5.204 1.00 26.58 ? 152 GLU B CD 1 ATOM 3184 O OE1 . GLU B 1 152 ? 8.527 9.393 4.882 1.00 28.43 ? 152 GLU B OE1 1 ATOM 3185 O OE2 . GLU B 1 152 ? 10.106 7.874 5.027 1.00 27.86 ? 152 GLU B OE2 1 ATOM 3186 N N . ILE B 1 153 ? 15.051 9.556 7.106 1.00 16.18 ? 153 ILE B N 1 ATOM 3187 C CA . ILE B 1 153 ? 16.209 8.871 7.664 1.00 15.35 ? 153 ILE B CA 1 ATOM 3188 C C . ILE B 1 153 ? 16.794 9.738 8.775 1.00 14.75 ? 153 ILE B C 1 ATOM 3189 O O . ILE B 1 153 ? 17.039 9.260 9.884 1.00 15.78 ? 153 ILE B O 1 ATOM 3190 C CB . ILE B 1 153 ? 17.286 8.622 6.583 1.00 16.30 ? 153 ILE B CB 1 ATOM 3191 C CG1 . ILE B 1 153 ? 16.797 7.543 5.610 1.00 16.20 ? 153 ILE B CG1 1 ATOM 3192 C CG2 . ILE B 1 153 ? 18.610 8.222 7.237 1.00 15.13 ? 153 ILE B CG2 1 ATOM 3193 C CD1 . ILE B 1 153 ? 17.788 7.207 4.499 1.00 15.41 ? 153 ILE B CD1 1 ATOM 3194 N N . ALA B 1 154 ? 16.996 11.018 8.472 1.00 13.16 ? 154 ALA B N 1 ATOM 3195 C CA . ALA B 1 154 ? 17.540 11.971 9.434 1.00 12.54 ? 154 ALA B CA 1 ATOM 3196 C C . ALA B 1 154 ? 16.699 12.008 10.709 1.00 14.48 ? 154 ALA B C 1 ATOM 3197 O O . ALA B 1 154 ? 17.228 11.966 11.827 1.00 13.58 ? 154 ALA B O 1 ATOM 3198 C CB . ALA B 1 154 ? 17.599 13.355 8.810 1.00 12.36 ? 154 ALA B CB 1 ATOM 3199 N N . SER B 1 155 ? 15.386 12.091 10.525 1.00 14.99 ? 155 SER B N 1 ATOM 3200 C CA . SER B 1 155 ? 14.439 12.131 11.626 1.00 16.90 ? 155 SER B CA 1 ATOM 3201 C C . SER B 1 155 ? 14.534 10.848 12.466 1.00 17.13 ? 155 SER B C 1 ATOM 3202 O O . SER B 1 155 ? 14.615 10.904 13.699 1.00 17.58 ? 155 SER B O 1 ATOM 3203 C CB . SER B 1 155 ? 13.021 12.303 11.062 1.00 17.72 ? 155 SER B CB 1 ATOM 3204 O OG . SER B 1 155 ? 12.061 12.361 12.099 1.00 24.07 ? 155 SER B OG 1 ATOM 3205 N N . SER B 1 156 ? 14.527 9.696 11.800 1.00 17.02 ? 156 SER B N 1 ATOM 3206 C CA . SER B 1 156 ? 14.616 8.414 12.495 1.00 17.70 ? 156 SER B CA 1 ATOM 3207 C C . SER B 1 156 ? 15.943 8.247 13.246 1.00 18.03 ? 156 SER B C 1 ATOM 3208 O O . SER B 1 156 ? 15.967 7.768 14.386 1.00 18.85 ? 156 SER B O 1 ATOM 3209 C CB . SER B 1 156 ? 14.434 7.267 11.501 1.00 17.05 ? 156 SER B CB 1 ATOM 3210 O OG . SER B 1 156 ? 13.132 7.299 10.955 1.00 17.16 ? 156 SER B OG 1 ATOM 3211 N N . LEU B 1 157 ? 17.044 8.641 12.613 1.00 17.23 ? 157 LEU B N 1 ATOM 3212 C CA . LEU B 1 157 ? 18.343 8.524 13.255 1.00 15.41 ? 157 LEU B CA 1 ATOM 3213 C C . LEU B 1 157 ? 18.448 9.461 14.457 1.00 15.23 ? 157 LEU B C 1 ATOM 3214 O O . LEU B 1 157 ? 19.117 9.134 15.441 1.00 15.66 ? 157 LEU B O 1 ATOM 3215 C CB . LEU B 1 157 ? 19.468 8.804 12.247 1.00 14.23 ? 157 LEU B CB 1 ATOM 3216 C CG . LEU B 1 157 ? 19.673 7.703 11.197 1.00 14.22 ? 157 LEU B CG 1 ATOM 3217 C CD1 . LEU B 1 157 ? 20.794 8.109 10.250 1.00 13.45 ? 157 LEU B CD1 1 ATOM 3218 C CD2 . LEU B 1 157 ? 19.997 6.362 11.878 1.00 12.62 ? 157 LEU B CD2 1 ATOM 3219 N N . LEU B 1 158 ? 17.790 10.619 14.389 1.00 13.28 ? 158 LEU B N 1 ATOM 3220 C CA . LEU B 1 158 ? 17.836 11.558 15.509 1.00 13.50 ? 158 LEU B CA 1 ATOM 3221 C C . LEU B 1 158 ? 17.231 10.890 16.749 1.00 13.57 ? 158 LEU B C 1 ATOM 3222 O O . LEU B 1 158 ? 17.701 11.097 17.866 1.00 11.72 ? 158 LEU B O 1 ATOM 3223 C CB . LEU B 1 158 ? 17.077 12.855 15.177 1.00 12.44 ? 158 LEU B CB 1 ATOM 3224 C CG . LEU B 1 158 ? 17.074 13.929 16.279 1.00 13.56 ? 158 LEU B CG 1 ATOM 3225 C CD1 . LEU B 1 158 ? 18.498 14.151 16.806 1.00 11.73 ? 158 LEU B CD1 1 ATOM 3226 C CD2 . LEU B 1 158 ? 16.492 15.228 15.733 1.00 13.04 ? 158 LEU B CD2 1 ATOM 3227 N N . VAL B 1 159 ? 16.188 10.088 16.541 1.00 14.11 ? 159 VAL B N 1 ATOM 3228 C CA . VAL B 1 159 ? 15.541 9.377 17.638 1.00 14.01 ? 159 VAL B CA 1 ATOM 3229 C C . VAL B 1 159 ? 16.513 8.327 18.182 1.00 15.36 ? 159 VAL B C 1 ATOM 3230 O O . VAL B 1 159 ? 16.718 8.226 19.389 1.00 15.18 ? 159 VAL B O 1 ATOM 3231 C CB . VAL B 1 159 ? 14.235 8.664 17.169 1.00 13.68 ? 159 VAL B CB 1 ATOM 3232 C CG1 . VAL B 1 159 ? 13.691 7.774 18.285 1.00 12.70 ? 159 VAL B CG1 1 ATOM 3233 C CG2 . VAL B 1 159 ? 13.189 9.697 16.759 1.00 11.78 ? 159 VAL B CG2 1 ATOM 3234 N N . VAL B 1 160 ? 17.109 7.551 17.277 1.00 14.54 ? 160 VAL B N 1 ATOM 3235 C CA . VAL B 1 160 ? 18.058 6.505 17.645 1.00 14.23 ? 160 VAL B CA 1 ATOM 3236 C C . VAL B 1 160 ? 19.261 7.089 18.402 1.00 13.97 ? 160 VAL B C 1 ATOM 3237 O O . VAL B 1 160 ? 19.637 6.600 19.474 1.00 11.42 ? 160 VAL B O 1 ATOM 3238 C CB . VAL B 1 160 ? 18.545 5.749 16.374 1.00 14.93 ? 160 VAL B CB 1 ATOM 3239 C CG1 . VAL B 1 160 ? 19.723 4.849 16.703 1.00 15.29 ? 160 VAL B CG1 1 ATOM 3240 C CG2 . VAL B 1 160 ? 17.405 4.922 15.802 1.00 15.15 ? 160 VAL B CG2 1 ATOM 3241 N N . ILE B 1 161 ? 19.847 8.141 17.839 1.00 13.42 ? 161 ILE B N 1 ATOM 3242 C CA . ILE B 1 161 ? 21.001 8.806 18.434 1.00 13.26 ? 161 ILE B CA 1 ATOM 3243 C C . ILE B 1 161 ? 20.763 9.224 19.883 1.00 14.19 ? 161 ILE B C 1 ATOM 3244 O O . ILE B 1 161 ? 21.623 9.040 20.741 1.00 13.12 ? 161 ILE B O 1 ATOM 3245 C CB . ILE B 1 161 ? 21.396 10.052 17.610 1.00 14.08 ? 161 ILE B CB 1 ATOM 3246 C CG1 . ILE B 1 161 ? 22.171 9.609 16.363 1.00 13.52 ? 161 ILE B CG1 1 ATOM 3247 C CG2 . ILE B 1 161 ? 22.194 11.034 18.477 1.00 11.76 ? 161 ILE B CG2 1 ATOM 3248 C CD1 . ILE B 1 161 ? 22.292 10.689 15.288 1.00 15.02 ? 161 ILE B CD1 1 ATOM 3249 N N . GLN B 1 162 ? 19.593 9.778 20.167 1.00 13.80 ? 162 GLN B N 1 ATOM 3250 C CA . GLN B 1 162 ? 19.318 10.205 21.529 1.00 14.18 ? 162 GLN B CA 1 ATOM 3251 C C . GLN B 1 162 ? 18.891 9.092 22.485 1.00 12.91 ? 162 GLN B C 1 ATOM 3252 O O . GLN B 1 162 ? 19.295 9.087 23.647 1.00 14.02 ? 162 GLN B O 1 ATOM 3253 C CB . GLN B 1 162 ? 18.281 11.314 21.509 1.00 14.45 ? 162 GLN B CB 1 ATOM 3254 C CG . GLN B 1 162 ? 18.814 12.573 20.878 1.00 17.31 ? 162 GLN B CG 1 ATOM 3255 C CD . GLN B 1 162 ? 17.805 13.677 20.897 1.00 20.25 ? 162 GLN B CD 1 ATOM 3256 O OE1 . GLN B 1 162 ? 16.883 13.704 20.080 1.00 23.45 ? 162 GLN B OE1 1 ATOM 3257 N NE2 . GLN B 1 162 ? 17.954 14.594 21.842 1.00 18.69 ? 162 GLN B NE2 1 ATOM 3258 N N . MET B 1 163 ? 18.092 8.147 22.002 1.00 11.65 ? 163 MET B N 1 ATOM 3259 C CA . MET B 1 163 ? 17.623 7.057 22.851 1.00 11.89 ? 163 MET B CA 1 ATOM 3260 C C . MET B 1 163 ? 18.672 5.972 23.052 1.00 12.85 ? 163 MET B C 1 ATOM 3261 O O . MET B 1 163 ? 18.557 5.151 23.974 1.00 12.35 ? 163 MET B O 1 ATOM 3262 C CB . MET B 1 163 ? 16.337 6.443 22.279 1.00 13.97 ? 163 MET B CB 1 ATOM 3263 C CG . MET B 1 163 ? 15.114 7.356 22.376 1.00 15.43 ? 163 MET B CG 1 ATOM 3264 S SD . MET B 1 163 ? 13.581 6.568 21.858 1.00 16.37 ? 163 MET B SD 1 ATOM 3265 C CE . MET B 1 163 ? 13.297 5.438 23.234 1.00 15.58 ? 163 MET B CE 1 ATOM 3266 N N . VAL B 1 164 ? 19.692 5.964 22.198 1.00 12.44 ? 164 VAL B N 1 ATOM 3267 C CA . VAL B 1 164 ? 20.760 4.977 22.324 1.00 13.37 ? 164 VAL B CA 1 ATOM 3268 C C . VAL B 1 164 ? 22.072 5.616 22.773 1.00 13.52 ? 164 VAL B C 1 ATOM 3269 O O . VAL B 1 164 ? 22.528 5.360 23.886 1.00 15.22 ? 164 VAL B O 1 ATOM 3270 C CB . VAL B 1 164 ? 20.990 4.213 21.006 1.00 13.62 ? 164 VAL B CB 1 ATOM 3271 C CG1 . VAL B 1 164 ? 22.188 3.261 21.152 1.00 12.88 ? 164 VAL B CG1 1 ATOM 3272 C CG2 . VAL B 1 164 ? 19.725 3.434 20.637 1.00 11.74 ? 164 VAL B CG2 1 ATOM 3273 N N . SER B 1 165 ? 22.659 6.459 21.922 1.00 13.54 ? 165 SER B N 1 ATOM 3274 C CA . SER B 1 165 ? 23.931 7.133 22.226 1.00 13.38 ? 165 SER B CA 1 ATOM 3275 C C . SER B 1 165 ? 23.909 8.125 23.402 1.00 12.96 ? 165 SER B C 1 ATOM 3276 O O . SER B 1 165 ? 24.697 8.000 24.340 1.00 12.87 ? 165 SER B O 1 ATOM 3277 C CB . SER B 1 165 ? 24.449 7.859 20.977 1.00 13.73 ? 165 SER B CB 1 ATOM 3278 O OG . SER B 1 165 ? 24.726 6.943 19.935 1.00 16.13 ? 165 SER B OG 1 ATOM 3279 N N . GLU B 1 166 ? 23.025 9.118 23.353 1.00 11.69 ? 166 GLU B N 1 ATOM 3280 C CA . GLU B 1 166 ? 22.968 10.098 24.434 1.00 13.26 ? 166 GLU B CA 1 ATOM 3281 C C . GLU B 1 166 ? 22.528 9.431 25.737 1.00 12.20 ? 166 GLU B C 1 ATOM 3282 O O . GLU B 1 166 ? 23.044 9.755 26.807 1.00 11.73 ? 166 GLU B O 1 ATOM 3283 C CB . GLU B 1 166 ? 22.032 11.263 24.066 1.00 12.24 ? 166 GLU B CB 1 ATOM 3284 C CG . GLU B 1 166 ? 22.460 12.030 22.799 1.00 13.94 ? 166 GLU B CG 1 ATOM 3285 C CD . GLU B 1 166 ? 23.759 12.832 22.962 1.00 15.72 ? 166 GLU B CD 1 ATOM 3286 O OE1 . GLU B 1 166 ? 24.541 12.561 23.902 1.00 15.23 ? 166 GLU B OE1 1 ATOM 3287 O OE2 . GLU B 1 166 ? 24.007 13.735 22.131 1.00 15.89 ? 166 GLU B OE2 1 ATOM 3288 N N . ALA B 1 167 ? 21.579 8.500 25.644 1.00 11.55 ? 167 ALA B N 1 ATOM 3289 C CA . ALA B 1 167 ? 21.113 7.771 26.822 1.00 12.72 ? 167 ALA B CA 1 ATOM 3290 C C . ALA B 1 167 ? 22.274 6.944 27.410 1.00 13.72 ? 167 ALA B C 1 ATOM 3291 O O . ALA B 1 167 ? 22.456 6.881 28.630 1.00 12.54 ? 167 ALA B O 1 ATOM 3292 C CB . ALA B 1 167 ? 19.965 6.861 26.448 1.00 10.20 ? 167 ALA B CB 1 ATOM 3293 N N . ALA B 1 168 ? 23.061 6.318 26.535 1.00 14.59 ? 168 ALA B N 1 ATOM 3294 C CA . ALA B 1 168 ? 24.207 5.512 26.967 1.00 14.19 ? 168 ALA B CA 1 ATOM 3295 C C . ALA B 1 168 ? 25.239 6.379 27.702 1.00 13.95 ? 168 ALA B C 1 ATOM 3296 O O . ALA B 1 168 ? 25.852 5.942 28.680 1.00 12.79 ? 168 ALA B O 1 ATOM 3297 C CB . ALA B 1 168 ? 24.859 4.838 25.755 1.00 12.98 ? 168 ALA B CB 1 ATOM 3298 N N . ARG B 1 169 ? 25.414 7.608 27.221 1.00 12.55 ? 169 ARG B N 1 ATOM 3299 C CA . ARG B 1 169 ? 26.360 8.559 27.796 1.00 12.23 ? 169 ARG B CA 1 ATOM 3300 C C . ARG B 1 169 ? 25.930 9.181 29.122 1.00 12.56 ? 169 ARG B C 1 ATOM 3301 O O . ARG B 1 169 ? 26.752 9.343 30.027 1.00 13.29 ? 169 ARG B O 1 ATOM 3302 C CB . ARG B 1 169 ? 26.611 9.706 26.821 1.00 11.79 ? 169 ARG B CB 1 ATOM 3303 C CG . ARG B 1 169 ? 27.393 9.361 25.572 1.00 13.20 ? 169 ARG B CG 1 ATOM 3304 C CD . ARG B 1 169 ? 27.206 10.481 24.581 1.00 12.71 ? 169 ARG B CD 1 ATOM 3305 N NE . ARG B 1 169 ? 27.975 10.307 23.362 1.00 13.47 ? 169 ARG B NE 1 ATOM 3306 C CZ . ARG B 1 169 ? 27.588 10.770 22.180 1.00 15.60 ? 169 ARG B CZ 1 ATOM 3307 N NH1 . ARG B 1 169 ? 26.438 11.422 22.066 1.00 16.81 ? 169 ARG B NH1 1 ATOM 3308 N NH2 . ARG B 1 169 ? 28.359 10.603 21.116 1.00 15.04 ? 169 ARG B NH2 1 ATOM 3309 N N . PHE B 1 170 ? 24.648 9.531 29.228 1.00 11.83 ? 170 PHE B N 1 ATOM 3310 C CA . PHE B 1 170 ? 24.112 10.202 30.412 1.00 11.68 ? 170 PHE B CA 1 ATOM 3311 C C . PHE B 1 170 ? 23.003 9.440 31.112 1.00 12.10 ? 170 PHE B C 1 ATOM 3312 O O . PHE B 1 170 ? 21.975 9.142 30.504 1.00 11.22 ? 170 PHE B O 1 ATOM 3313 C CB . PHE B 1 170 ? 23.551 11.584 30.023 1.00 10.89 ? 170 PHE B CB 1 ATOM 3314 C CG . PHE B 1 170 ? 24.590 12.562 29.537 1.00 11.79 ? 170 PHE B CG 1 ATOM 3315 C CD1 . PHE B 1 170 ? 25.340 13.310 30.443 1.00 10.14 ? 170 PHE B CD1 1 ATOM 3316 C CD2 . PHE B 1 170 ? 24.817 12.735 28.172 1.00 10.53 ? 170 PHE B CD2 1 ATOM 3317 C CE1 . PHE B 1 170 ? 26.303 14.220 29.996 1.00 12.94 ? 170 PHE B CE1 1 ATOM 3318 C CE2 . PHE B 1 170 ? 25.777 13.641 27.711 1.00 11.68 ? 170 PHE B CE2 1 ATOM 3319 C CZ . PHE B 1 170 ? 26.521 14.386 28.624 1.00 11.30 ? 170 PHE B CZ 1 ATOM 3320 N N . THR B 1 171 ? 23.203 9.144 32.393 1.00 12.76 ? 171 THR B N 1 ATOM 3321 C CA . THR B 1 171 ? 22.188 8.456 33.188 1.00 13.11 ? 171 THR B CA 1 ATOM 3322 C C . THR B 1 171 ? 20.987 9.390 33.275 1.00 13.45 ? 171 THR B C 1 ATOM 3323 O O . THR B 1 171 ? 19.853 8.939 33.386 1.00 14.21 ? 171 THR B O 1 ATOM 3324 C CB . THR B 1 171 ? 22.672 8.180 34.624 1.00 13.75 ? 171 THR B CB 1 ATOM 3325 O OG1 . THR B 1 171 ? 23.139 9.405 35.201 1.00 15.75 ? 171 THR B OG1 1 ATOM 3326 C CG2 . THR B 1 171 ? 23.806 7.165 34.638 1.00 14.56 ? 171 THR B CG2 1 ATOM 3327 N N . PHE B 1 172 ? 21.246 10.696 33.223 1.00 13.66 ? 172 PHE B N 1 ATOM 3328 C CA . PHE B 1 172 ? 20.186 11.697 33.290 1.00 14.46 ? 172 PHE B CA 1 ATOM 3329 C C . PHE B 1 172 ? 19.220 11.567 32.108 1.00 14.65 ? 172 PHE B C 1 ATOM 3330 O O . PHE B 1 172 ? 17.997 11.593 32.279 1.00 15.01 ? 172 PHE B O 1 ATOM 3331 C CB . PHE B 1 172 ? 20.781 13.105 33.299 1.00 16.08 ? 172 PHE B CB 1 ATOM 3332 C CG . PHE B 1 172 ? 19.749 14.193 33.425 1.00 19.92 ? 172 PHE B CG 1 ATOM 3333 C CD1 . PHE B 1 172 ? 19.260 14.567 34.674 1.00 21.03 ? 172 PHE B CD1 1 ATOM 3334 C CD2 . PHE B 1 172 ? 19.232 14.815 32.290 1.00 21.79 ? 172 PHE B CD2 1 ATOM 3335 C CE1 . PHE B 1 172 ? 18.267 15.546 34.793 1.00 21.47 ? 172 PHE B CE1 1 ATOM 3336 C CE2 . PHE B 1 172 ? 18.238 15.795 32.396 1.00 22.19 ? 172 PHE B CE2 1 ATOM 3337 C CZ . PHE B 1 172 ? 17.756 16.159 33.652 1.00 21.17 ? 172 PHE B CZ 1 ATOM 3338 N N . ILE B 1 173 ? 19.770 11.426 30.908 1.00 14.51 ? 173 ILE B N 1 ATOM 3339 C CA . ILE B 1 173 ? 18.946 11.298 29.711 1.00 14.44 ? 173 ILE B CA 1 ATOM 3340 C C . ILE B 1 173 ? 18.265 9.932 29.681 1.00 14.80 ? 173 ILE B C 1 ATOM 3341 O O . ILE B 1 173 ? 17.109 9.822 29.287 1.00 14.40 ? 173 ILE B O 1 ATOM 3342 C CB . ILE B 1 173 ? 19.800 11.553 28.434 1.00 13.24 ? 173 ILE B CB 1 ATOM 3343 C CG1 . ILE B 1 173 ? 20.272 13.020 28.447 1.00 12.73 ? 173 ILE B CG1 1 ATOM 3344 C CG2 . ILE B 1 173 ? 18.991 11.248 27.171 1.00 10.86 ? 173 ILE B CG2 1 ATOM 3345 C CD1 . ILE B 1 173 ? 21.145 13.437 27.273 1.00 10.21 ? 173 ILE B CD1 1 ATOM 3346 N N . GLU B 1 174 ? 18.979 8.899 30.122 1.00 15.18 ? 174 GLU B N 1 ATOM 3347 C CA . GLU B 1 174 ? 18.432 7.542 30.195 1.00 14.51 ? 174 GLU B CA 1 ATOM 3348 C C . GLU B 1 174 ? 17.171 7.538 31.070 1.00 13.74 ? 174 GLU B C 1 ATOM 3349 O O . GLU B 1 174 ? 16.169 6.922 30.734 1.00 13.19 ? 174 GLU B O 1 ATOM 3350 C CB . GLU B 1 174 ? 19.466 6.588 30.816 1.00 15.95 ? 174 GLU B CB 1 ATOM 3351 C CG . GLU B 1 174 ? 18.859 5.350 31.486 1.00 17.28 ? 174 GLU B CG 1 ATOM 3352 C CD . GLU B 1 174 ? 19.846 4.604 32.395 1.00 20.21 ? 174 GLU B CD 1 ATOM 3353 O OE1 . GLU B 1 174 ? 20.991 5.077 32.593 1.00 19.15 ? 174 GLU B OE1 1 ATOM 3354 O OE2 . GLU B 1 174 ? 19.464 3.536 32.921 1.00 21.38 ? 174 GLU B OE2 1 ATOM 3355 N N . ASN B 1 175 ? 17.226 8.238 32.195 1.00 13.03 ? 175 ASN B N 1 ATOM 3356 C CA . ASN B 1 175 ? 16.090 8.271 33.101 1.00 14.43 ? 175 ASN B CA 1 ATOM 3357 C C . ASN B 1 175 ? 14.922 9.148 32.673 1.00 15.31 ? 175 ASN B C 1 ATOM 3358 O O . ASN B 1 175 ? 13.796 8.937 33.116 1.00 15.47 ? 175 ASN B O 1 ATOM 3359 C CB . ASN B 1 175 ? 16.563 8.631 34.508 1.00 14.27 ? 175 ASN B CB 1 ATOM 3360 C CG . ASN B 1 175 ? 17.314 7.485 35.161 1.00 14.66 ? 175 ASN B CG 1 ATOM 3361 O OD1 . ASN B 1 175 ? 16.878 6.335 35.086 1.00 14.96 ? 175 ASN B OD1 1 ATOM 3362 N ND2 . ASN B 1 175 ? 18.438 7.786 35.800 1.00 15.03 ? 175 ASN B ND2 1 ATOM 3363 N N . GLN B 1 176 ? 15.171 10.126 31.812 1.00 17.03 ? 176 GLN B N 1 ATOM 3364 C CA . GLN B 1 176 ? 14.075 10.961 31.342 1.00 18.58 ? 176 GLN B CA 1 ATOM 3365 C C . GLN B 1 176 ? 13.225 10.132 30.389 1.00 18.24 ? 176 GLN B C 1 ATOM 3366 O O . GLN B 1 176 ? 12.035 10.388 30.205 1.00 19.58 ? 176 GLN B O 1 ATOM 3367 C CB . GLN B 1 176 ? 14.606 12.199 30.633 1.00 21.07 ? 176 GLN B CB 1 ATOM 3368 C CG . GLN B 1 176 ? 15.402 13.094 31.548 1.00 25.01 ? 176 GLN B CG 1 ATOM 3369 C CD . GLN B 1 176 ? 15.634 14.447 30.944 1.00 30.54 ? 176 GLN B CD 1 ATOM 3370 O OE1 . GLN B 1 176 ? 14.935 15.413 31.263 1.00 33.35 ? 176 GLN B OE1 1 ATOM 3371 N NE2 . GLN B 1 176 ? 16.611 14.530 30.047 1.00 31.63 ? 176 GLN B NE2 1 ATOM 3372 N N . ILE B 1 177 ? 13.850 9.126 29.792 1.00 17.11 ? 177 ILE B N 1 ATOM 3373 C CA . ILE B 1 177 ? 13.157 8.236 28.872 1.00 16.34 ? 177 ILE B CA 1 ATOM 3374 C C . ILE B 1 177 ? 12.536 7.094 29.678 1.00 16.57 ? 177 ILE B C 1 ATOM 3375 O O . ILE B 1 177 ? 11.389 6.703 29.436 1.00 14.58 ? 177 ILE B O 1 ATOM 3376 C CB . ILE B 1 177 ? 14.140 7.683 27.807 1.00 15.46 ? 177 ILE B CB 1 ATOM 3377 C CG1 . ILE B 1 177 ? 14.512 8.808 26.837 1.00 16.37 ? 177 ILE B CG1 1 ATOM 3378 C CG2 . ILE B 1 177 ? 13.516 6.529 27.038 1.00 16.90 ? 177 ILE B CG2 1 ATOM 3379 C CD1 . ILE B 1 177 ? 15.806 8.580 26.093 1.00 17.39 ? 177 ILE B CD1 1 ATOM 3380 N N . ARG B 1 178 ? 13.291 6.581 30.651 1.00 15.89 ? 178 ARG B N 1 ATOM 3381 C CA . ARG B 1 178 ? 12.814 5.487 31.498 1.00 15.42 ? 178 ARG B CA 1 ATOM 3382 C C . ARG B 1 178 ? 11.463 5.827 32.129 1.00 14.52 ? 178 ARG B C 1 ATOM 3383 O O . ARG B 1 178 ? 10.531 5.033 32.057 1.00 15.94 ? 178 ARG B O 1 ATOM 3384 C CB . ARG B 1 178 ? 13.840 5.180 32.600 1.00 15.47 ? 178 ARG B CB 1 ATOM 3385 C CG . ARG B 1 178 ? 13.357 4.191 33.669 1.00 16.36 ? 178 ARG B CG 1 ATOM 3386 C CD . ARG B 1 178 ? 14.333 4.104 34.865 1.00 16.09 ? 178 ARG B CD 1 ATOM 3387 N NE . ARG B 1 178 ? 13.893 3.117 35.851 1.00 16.17 ? 178 ARG B NE 1 ATOM 3388 C CZ . ARG B 1 178 ? 14.642 2.118 36.325 1.00 17.88 ? 178 ARG B CZ 1 ATOM 3389 N NH1 . ARG B 1 178 ? 15.897 1.948 35.921 1.00 14.72 ? 178 ARG B NH1 1 ATOM 3390 N NH2 . ARG B 1 178 ? 14.118 1.261 37.193 1.00 18.79 ? 178 ARG B NH2 1 ATOM 3391 N N . ASN B 1 179 ? 11.352 7.008 32.730 1.00 13.48 ? 179 ASN B N 1 ATOM 3392 C CA . ASN B 1 179 ? 10.104 7.409 33.377 1.00 13.93 ? 179 ASN B CA 1 ATOM 3393 C C . ASN B 1 179 ? 9.092 8.112 32.478 1.00 13.28 ? 179 ASN B C 1 ATOM 3394 O O . ASN B 1 179 ? 8.141 8.724 32.967 1.00 12.41 ? 179 ASN B O 1 ATOM 3395 C CB . ASN B 1 179 ? 10.388 8.279 34.609 1.00 15.10 ? 179 ASN B CB 1 ATOM 3396 C CG . ASN B 1 179 ? 10.979 7.479 35.770 1.00 16.15 ? 179 ASN B CG 1 ATOM 3397 O OD1 . ASN B 1 179 ? 10.630 6.317 35.979 1.00 15.61 ? 179 ASN B OD1 1 ATOM 3398 N ND2 . ASN B 1 179 ? 11.860 8.110 36.539 1.00 15.55 ? 179 ASN B ND2 1 ATOM 3399 N N . ASN B 1 180 ? 9.307 8.025 31.169 1.00 13.49 ? 180 ASN B N 1 ATOM 3400 C CA . ASN B 1 180 ? 8.405 8.605 30.169 1.00 16.36 ? 180 ASN B CA 1 ATOM 3401 C C . ASN B 1 180 ? 8.344 7.604 29.019 1.00 16.93 ? 180 ASN B C 1 ATOM 3402 O O . ASN B 1 180 ? 7.953 7.944 27.899 1.00 16.83 ? 180 ASN B O 1 ATOM 3403 C CB . ASN B 1 180 ? 8.951 9.934 29.622 1.00 16.46 ? 180 ASN B CB 1 ATOM 3404 C CG . ASN B 1 180 ? 8.737 11.100 30.569 1.00 17.45 ? 180 ASN B CG 1 ATOM 3405 O OD1 . ASN B 1 180 ? 7.611 11.371 30.991 1.00 15.55 ? 180 ASN B OD1 1 ATOM 3406 N ND2 . ASN B 1 180 ? 9.819 11.810 30.895 1.00 15.14 ? 180 ASN B ND2 1 ATOM 3407 N N . PHE B 1 181 ? 8.727 6.365 29.310 1.00 17.69 ? 181 PHE B N 1 ATOM 3408 C CA . PHE B 1 181 ? 8.787 5.312 28.298 1.00 18.63 ? 181 PHE B CA 1 ATOM 3409 C C . PHE B 1 181 ? 7.575 5.117 27.384 1.00 19.44 ? 181 PHE B C 1 ATOM 3410 O O . PHE B 1 181 ? 7.731 5.048 26.158 1.00 19.78 ? 181 PHE B O 1 ATOM 3411 C CB . PHE B 1 181 ? 9.142 3.976 28.957 1.00 18.87 ? 181 PHE B CB 1 ATOM 3412 C CG . PHE B 1 181 ? 9.677 2.955 27.995 1.00 19.08 ? 181 PHE B CG 1 ATOM 3413 C CD1 . PHE B 1 181 ? 10.882 3.177 27.327 1.00 19.56 ? 181 PHE B CD1 1 ATOM 3414 C CD2 . PHE B 1 181 ? 8.977 1.780 27.743 1.00 18.49 ? 181 PHE B CD2 1 ATOM 3415 C CE1 . PHE B 1 181 ? 11.384 2.239 26.420 1.00 18.59 ? 181 PHE B CE1 1 ATOM 3416 C CE2 . PHE B 1 181 ? 9.466 0.839 26.842 1.00 18.26 ? 181 PHE B CE2 1 ATOM 3417 C CZ . PHE B 1 181 ? 10.674 1.068 26.178 1.00 18.91 ? 181 PHE B CZ 1 ATOM 3418 N N . GLN B 1 182 ? 6.383 5.019 27.966 1.00 19.17 ? 182 GLN B N 1 ATOM 3419 C CA . GLN B 1 182 ? 5.166 4.808 27.187 1.00 20.50 ? 182 GLN B CA 1 ATOM 3420 C C . GLN B 1 182 ? 4.538 6.109 26.689 1.00 23.14 ? 182 GLN B C 1 ATOM 3421 O O . GLN B 1 182 ? 3.396 6.120 26.224 1.00 24.33 ? 182 GLN B O 1 ATOM 3422 C CB . GLN B 1 182 ? 4.135 4.041 28.018 1.00 19.92 ? 182 GLN B CB 1 ATOM 3423 C CG . GLN B 1 182 ? 4.553 2.650 28.466 1.00 20.37 ? 182 GLN B CG 1 ATOM 3424 C CD . GLN B 1 182 ? 4.765 1.695 27.311 1.00 25.12 ? 182 GLN B CD 1 ATOM 3425 O OE1 . GLN B 1 182 ? 4.148 1.837 26.250 1.00 26.20 ? 182 GLN B OE1 1 ATOM 3426 N NE2 . GLN B 1 182 ? 5.630 0.700 27.514 1.00 24.78 ? 182 GLN B NE2 1 ATOM 3427 N N . GLN B 1 183 ? 5.280 7.205 26.781 1.00 24.68 ? 183 GLN B N 1 ATOM 3428 C CA . GLN B 1 183 ? 4.774 8.499 26.339 1.00 24.83 ? 183 GLN B CA 1 ATOM 3429 C C . GLN B 1 183 ? 5.636 9.069 25.215 1.00 25.33 ? 183 GLN B C 1 ATOM 3430 O O . GLN B 1 183 ? 6.609 8.448 24.783 1.00 24.71 ? 183 GLN B O 1 ATOM 3431 C CB . GLN B 1 183 ? 4.761 9.468 27.516 1.00 25.73 ? 183 GLN B CB 1 ATOM 3432 C CG . GLN B 1 183 ? 4.063 8.907 28.740 1.00 29.58 ? 183 GLN B CG 1 ATOM 3433 C CD . GLN B 1 183 ? 4.497 9.592 30.025 1.00 33.29 ? 183 GLN B CD 1 ATOM 3434 O OE1 . GLN B 1 183 ? 4.386 10.812 30.157 1.00 35.62 ? 183 GLN B OE1 1 ATOM 3435 N NE2 . GLN B 1 183 ? 4.994 8.808 30.981 1.00 31.98 ? 183 GLN B NE2 1 ATOM 3436 N N . ARG B 1 184 ? 5.258 10.250 24.741 1.00 25.17 ? 184 ARG B N 1 ATOM 3437 C CA . ARG B 1 184 ? 5.978 10.944 23.682 1.00 24.75 ? 184 ARG B CA 1 ATOM 3438 C C . ARG B 1 184 ? 6.484 12.265 24.256 1.00 25.70 ? 184 ARG B C 1 ATOM 3439 O O . ARG B 1 184 ? 5.699 13.178 24.516 1.00 28.26 ? 184 ARG B O 1 ATOM 3440 C CB . ARG B 1 184 ? 5.041 11.202 22.506 1.00 24.45 ? 184 ARG B CB 1 ATOM 3441 C CG . ARG B 1 184 ? 4.780 9.967 21.673 1.00 25.95 ? 184 ARG B CG 1 ATOM 3442 C CD . ARG B 1 184 ? 3.573 10.136 20.778 1.00 28.57 ? 184 ARG B CD 1 ATOM 3443 N NE . ARG B 1 184 ? 3.630 9.240 19.629 1.00 31.13 ? 184 ARG B NE 1 ATOM 3444 C CZ . ARG B 1 184 ? 4.396 9.453 18.559 1.00 33.57 ? 184 ARG B CZ 1 ATOM 3445 N NH1 . ARG B 1 184 ? 5.167 10.537 18.487 1.00 32.70 ? 184 ARG B NH1 1 ATOM 3446 N NH2 . ARG B 1 184 ? 4.401 8.578 17.562 1.00 33.50 ? 184 ARG B NH2 1 ATOM 3447 N N . ILE B 1 185 ? 7.792 12.366 24.460 1.00 24.05 ? 185 ILE B N 1 ATOM 3448 C CA . ILE B 1 185 ? 8.370 13.575 25.034 1.00 23.37 ? 185 ILE B CA 1 ATOM 3449 C C . ILE B 1 185 ? 9.445 14.164 24.143 1.00 22.77 ? 185 ILE B C 1 ATOM 3450 O O . ILE B 1 185 ? 10.078 13.456 23.365 1.00 24.71 ? 185 ILE B O 1 ATOM 3451 C CB . ILE B 1 185 ? 9.025 13.281 26.397 1.00 23.90 ? 185 ILE B CB 1 ATOM 3452 C CG1 . ILE B 1 185 ? 10.182 12.293 26.186 1.00 24.37 ? 185 ILE B CG1 1 ATOM 3453 C CG2 . ILE B 1 185 ? 7.984 12.733 27.378 1.00 21.47 ? 185 ILE B CG2 1 ATOM 3454 C CD1 . ILE B 1 185 ? 11.051 12.052 27.392 1.00 23.79 ? 185 ILE B CD1 1 ATOM 3455 N N . ARG B 1 186 ? 9.647 15.468 24.265 1.00 21.96 ? 186 ARG B N 1 ATOM 3456 C CA . ARG B 1 186 ? 10.675 16.155 23.502 1.00 22.82 ? 186 ARG B CA 1 ATOM 3457 C C . ARG B 1 186 ? 11.695 16.670 24.496 1.00 22.82 ? 186 ARG B C 1 ATOM 3458 O O . ARG B 1 186 ? 11.331 17.139 25.569 1.00 24.02 ? 186 ARG B O 1 ATOM 3459 C CB . ARG B 1 186 ? 10.064 17.305 22.718 1.00 21.63 ? 186 ARG B CB 1 ATOM 3460 C CG . ARG B 1 186 ? 9.106 16.795 21.692 1.00 23.58 ? 186 ARG B CG 1 ATOM 3461 C CD . ARG B 1 186 ? 8.503 17.888 20.884 1.00 24.16 ? 186 ARG B CD 1 ATOM 3462 N NE . ARG B 1 186 ? 7.637 17.316 19.866 1.00 26.02 ? 186 ARG B NE 1 ATOM 3463 C CZ . ARG B 1 186 ? 7.012 18.029 18.943 1.00 28.51 ? 186 ARG B CZ 1 ATOM 3464 N NH1 . ARG B 1 186 ? 7.160 19.346 18.918 1.00 28.84 ? 186 ARG B NH1 1 ATOM 3465 N NH2 . ARG B 1 186 ? 6.246 17.426 18.046 1.00 29.48 ? 186 ARG B NH2 1 ATOM 3466 N N . PRO B 1 187 ? 12.990 16.583 24.160 1.00 23.10 ? 187 PRO B N 1 ATOM 3467 C CA . PRO B 1 187 ? 14.043 17.054 25.066 1.00 23.10 ? 187 PRO B CA 1 ATOM 3468 C C . PRO B 1 187 ? 13.943 18.530 25.469 1.00 23.74 ? 187 PRO B C 1 ATOM 3469 O O . PRO B 1 187 ? 13.715 19.405 24.629 1.00 24.13 ? 187 PRO B O 1 ATOM 3470 C CB . PRO B 1 187 ? 15.326 16.735 24.298 1.00 22.48 ? 187 PRO B CB 1 ATOM 3471 C CG . PRO B 1 187 ? 14.898 16.799 22.869 1.00 22.51 ? 187 PRO B CG 1 ATOM 3472 C CD . PRO B 1 187 ? 13.563 16.099 22.892 1.00 22.14 ? 187 PRO B CD 1 ATOM 3473 N N . ALA B 1 188 ? 14.109 18.790 26.764 1.00 24.13 ? 188 ALA B N 1 ATOM 3474 C CA . ALA B 1 188 ? 14.054 20.146 27.303 1.00 24.43 ? 188 ALA B CA 1 ATOM 3475 C C . ALA B 1 188 ? 15.440 20.776 27.253 1.00 25.10 ? 188 ALA B C 1 ATOM 3476 O O . ALA B 1 188 ? 16.399 20.149 26.800 1.00 24.81 ? 188 ALA B O 1 ATOM 3477 C CB . ALA B 1 188 ? 13.550 20.121 28.734 1.00 25.37 ? 188 ALA B CB 1 ATOM 3478 N N . ASN B 1 189 ? 15.551 22.009 27.730 1.00 25.44 ? 189 ASN B N 1 ATOM 3479 C CA . ASN B 1 189 ? 16.834 22.701 27.709 1.00 27.02 ? 189 ASN B CA 1 ATOM 3480 C C . ASN B 1 189 ? 17.927 21.975 28.489 1.00 24.23 ? 189 ASN B C 1 ATOM 3481 O O . ASN B 1 189 ? 19.102 22.059 28.131 1.00 22.22 ? 189 ASN B O 1 ATOM 3482 C CB . ASN B 1 189 ? 16.672 24.137 28.226 1.00 32.14 ? 189 ASN B CB 1 ATOM 3483 C CG . ASN B 1 189 ? 15.876 25.020 27.262 1.00 37.78 ? 189 ASN B CG 1 ATOM 3484 O OD1 . ASN B 1 189 ? 16.304 25.262 26.129 1.00 34.85 ? 189 ASN B OD1 1 ATOM 3485 N ND2 . ASN B 1 189 ? 14.715 25.487 27.719 1.00 43.47 ? 189 ASN B ND2 1 ATOM 3486 N N . ASN B 1 190 ? 17.548 21.262 29.547 1.00 22.70 ? 190 ASN B N 1 ATOM 3487 C CA . ASN B 1 190 ? 18.538 20.536 30.340 1.00 21.93 ? 190 ASN B CA 1 ATOM 3488 C C . ASN B 1 190 ? 19.151 19.378 29.546 1.00 20.98 ? 190 ASN B C 1 ATOM 3489 O O . ASN B 1 190 ? 20.373 19.230 29.488 1.00 18.74 ? 190 ASN B O 1 ATOM 3490 C CB . ASN B 1 190 ? 17.933 20.026 31.664 1.00 21.60 ? 190 ASN B CB 1 ATOM 3491 C CG . ASN B 1 190 ? 16.507 19.522 31.519 1.00 22.80 ? 190 ASN B CG 1 ATOM 3492 O OD1 . ASN B 1 190 ? 16.065 19.166 30.428 1.00 27.19 ? 190 ASN B OD1 1 ATOM 3493 N ND2 . ASN B 1 190 ? 15.786 19.471 32.634 1.00 21.27 ? 190 ASN B ND2 1 ATOM 3494 N N . THR B 1 191 ? 18.299 18.574 28.921 1.00 19.10 ? 191 THR B N 1 ATOM 3495 C CA . THR B 1 191 ? 18.765 17.448 28.124 1.00 18.40 ? 191 THR B CA 1 ATOM 3496 C C . THR B 1 191 ? 19.648 17.942 26.989 1.00 17.73 ? 191 THR B C 1 ATOM 3497 O O . THR B 1 191 ? 20.753 17.446 26.778 1.00 18.52 ? 191 THR B O 1 ATOM 3498 C CB . THR B 1 191 ? 17.585 16.690 27.518 1.00 17.68 ? 191 THR B CB 1 ATOM 3499 O OG1 . THR B 1 191 ? 16.693 16.308 28.567 1.00 18.79 ? 191 THR B OG1 1 ATOM 3500 C CG2 . THR B 1 191 ? 18.060 15.453 26.767 1.00 15.67 ? 191 THR B CG2 1 ATOM 3501 N N . ILE B 1 192 ? 19.155 18.937 26.266 1.00 17.70 ? 192 ILE B N 1 ATOM 3502 C CA . ILE B 1 192 ? 19.893 19.485 25.141 1.00 17.02 ? 192 ILE B CA 1 ATOM 3503 C C . ILE B 1 192 ? 21.261 20.049 25.525 1.00 16.29 ? 192 ILE B C 1 ATOM 3504 O O . ILE B 1 192 ? 22.235 19.809 24.817 1.00 16.37 ? 192 ILE B O 1 ATOM 3505 C CB . ILE B 1 192 ? 19.041 20.557 24.411 1.00 18.69 ? 192 ILE B CB 1 ATOM 3506 C CG1 . ILE B 1 192 ? 17.809 19.889 23.789 1.00 18.78 ? 192 ILE B CG1 1 ATOM 3507 C CG2 . ILE B 1 192 ? 19.865 21.253 23.333 1.00 18.40 ? 192 ILE B CG2 1 ATOM 3508 C CD1 . ILE B 1 192 ? 16.848 20.848 23.112 1.00 20.76 ? 192 ILE B CD1 1 ATOM 3509 N N . SER B 1 193 ? 21.353 20.776 26.640 1.00 16.00 ? 193 SER B N 1 ATOM 3510 C CA . SER B 1 193 ? 22.644 21.345 27.053 1.00 16.70 ? 193 SER B CA 1 ATOM 3511 C C . SER B 1 193 ? 23.637 20.247 27.451 1.00 16.06 ? 193 SER B C 1 ATOM 3512 O O . SER B 1 193 ? 24.841 20.356 27.198 1.00 16.90 ? 193 SER B O 1 ATOM 3513 C CB . SER B 1 193 ? 22.467 22.368 28.201 1.00 16.03 ? 193 SER B CB 1 ATOM 3514 O OG . SER B 1 193 ? 22.029 21.776 29.411 1.00 18.39 ? 193 SER B OG 1 ATOM 3515 N N . LEU B 1 194 ? 23.131 19.186 28.069 1.00 15.23 ? 194 LEU B N 1 ATOM 3516 C CA . LEU B 1 194 ? 23.976 18.065 28.454 1.00 14.45 ? 194 LEU B CA 1 ATOM 3517 C C . LEU B 1 194 ? 24.593 17.445 27.213 1.00 13.99 ? 194 LEU B C 1 ATOM 3518 O O . LEU B 1 194 ? 25.796 17.186 27.164 1.00 14.19 ? 194 LEU B O 1 ATOM 3519 C CB . LEU B 1 194 ? 23.155 16.999 29.176 1.00 14.10 ? 194 LEU B CB 1 ATOM 3520 C CG . LEU B 1 194 ? 22.977 17.213 30.670 1.00 16.95 ? 194 LEU B CG 1 ATOM 3521 C CD1 . LEU B 1 194 ? 22.032 16.164 31.209 1.00 19.13 ? 194 LEU B CD1 1 ATOM 3522 C CD2 . LEU B 1 194 ? 24.340 17.137 31.366 1.00 17.95 ? 194 LEU B CD2 1 ATOM 3523 N N . GLU B 1 195 ? 23.753 17.195 26.214 1.00 14.62 ? 195 GLU B N 1 ATOM 3524 C CA . GLU B 1 195 ? 24.206 16.596 24.965 1.00 14.62 ? 195 GLU B CA 1 ATOM 3525 C C . GLU B 1 195 ? 25.302 17.444 24.333 1.00 15.37 ? 195 GLU B C 1 ATOM 3526 O O . GLU B 1 195 ? 26.303 16.917 23.846 1.00 14.62 ? 195 GLU B O 1 ATOM 3527 C CB . GLU B 1 195 ? 23.036 16.457 23.990 1.00 14.08 ? 195 GLU B CB 1 ATOM 3528 C CG . GLU B 1 195 ? 21.869 15.634 24.519 1.00 16.18 ? 195 GLU B CG 1 ATOM 3529 C CD . GLU B 1 195 ? 20.718 15.556 23.532 1.00 17.16 ? 195 GLU B CD 1 ATOM 3530 O OE1 . GLU B 1 195 ? 20.469 16.559 22.830 1.00 16.82 ? 195 GLU B OE1 1 ATOM 3531 O OE2 . GLU B 1 195 ? 20.053 14.499 23.467 1.00 17.49 ? 195 GLU B OE2 1 ATOM 3532 N N . ASN B 1 196 ? 25.106 18.759 24.354 1.00 15.97 ? 196 ASN B N 1 ATOM 3533 C CA . ASN B 1 196 ? 26.065 19.693 23.783 1.00 17.11 ? 196 ASN B CA 1 ATOM 3534 C C . ASN B 1 196 ? 27.409 19.761 24.520 1.00 17.71 ? 196 ASN B C 1 ATOM 3535 O O . ASN B 1 196 ? 28.451 19.918 23.892 1.00 18.11 ? 196 ASN B O 1 ATOM 3536 C CB . ASN B 1 196 ? 25.479 21.113 23.746 1.00 17.61 ? 196 ASN B CB 1 ATOM 3537 C CG . ASN B 1 196 ? 24.291 21.251 22.806 1.00 17.25 ? 196 ASN B CG 1 ATOM 3538 O OD1 . ASN B 1 196 ? 24.107 20.463 21.881 1.00 16.45 ? 196 ASN B OD1 1 ATOM 3539 N ND2 . ASN B 1 196 ? 23.491 22.286 23.032 1.00 17.43 ? 196 ASN B ND2 1 ATOM 3540 N N . LYS B 1 197 ? 27.388 19.644 25.844 1.00 17.24 ? 197 LYS B N 1 ATOM 3541 C CA . LYS B 1 197 ? 28.612 19.757 26.635 1.00 17.16 ? 197 LYS B CA 1 ATOM 3542 C C . LYS B 1 197 ? 29.323 18.472 27.064 1.00 16.20 ? 197 LYS B C 1 ATOM 3543 O O . LYS B 1 197 ? 30.203 18.523 27.928 1.00 16.36 ? 197 LYS B O 1 ATOM 3544 C CB . LYS B 1 197 ? 28.322 20.593 27.889 1.00 18.27 ? 197 LYS B CB 1 ATOM 3545 C CG . LYS B 1 197 ? 27.713 21.961 27.613 1.00 19.46 ? 197 LYS B CG 1 ATOM 3546 C CD . LYS B 1 197 ? 28.654 22.840 26.796 1.00 20.22 ? 197 LYS B CD 1 ATOM 3547 C CE . LYS B 1 197 ? 28.130 24.265 26.702 1.00 21.78 ? 197 LYS B CE 1 ATOM 3548 N NZ . LYS B 1 197 ? 29.014 25.111 25.860 1.00 23.25 ? 197 LYS B NZ 1 ATOM 3549 N N . TRP B 1 198 ? 28.972 17.330 26.478 1.00 15.02 ? 198 TRP B N 1 ATOM 3550 C CA . TRP B 1 198 ? 29.614 16.070 26.866 1.00 14.73 ? 198 TRP B CA 1 ATOM 3551 C C . TRP B 1 198 ? 31.134 16.124 26.705 1.00 15.36 ? 198 TRP B C 1 ATOM 3552 O O . TRP B 1 198 ? 31.876 15.713 27.596 1.00 13.98 ? 198 TRP B O 1 ATOM 3553 C CB . TRP B 1 198 ? 29.059 14.894 26.048 1.00 12.64 ? 198 TRP B CB 1 ATOM 3554 C CG . TRP B 1 198 ? 29.588 13.534 26.487 1.00 12.03 ? 198 TRP B CG 1 ATOM 3555 C CD1 . TRP B 1 198 ? 29.559 13.010 27.752 1.00 10.06 ? 198 TRP B CD1 1 ATOM 3556 C CD2 . TRP B 1 198 ? 30.194 12.531 25.654 1.00 11.33 ? 198 TRP B CD2 1 ATOM 3557 N NE1 . TRP B 1 198 ? 30.108 11.744 27.758 1.00 11.09 ? 198 TRP B NE1 1 ATOM 3558 C CE2 . TRP B 1 198 ? 30.506 11.425 26.486 1.00 10.47 ? 198 TRP B CE2 1 ATOM 3559 C CE3 . TRP B 1 198 ? 30.505 12.459 24.284 1.00 10.72 ? 198 TRP B CE3 1 ATOM 3560 C CZ2 . TRP B 1 198 ? 31.113 10.258 25.994 1.00 10.72 ? 198 TRP B CZ2 1 ATOM 3561 C CZ3 . TRP B 1 198 ? 31.111 11.294 23.790 1.00 10.54 ? 198 TRP B CZ3 1 ATOM 3562 C CH2 . TRP B 1 198 ? 31.407 10.209 24.649 1.00 9.79 ? 198 TRP B CH2 1 ATOM 3563 N N . GLY B 1 199 ? 31.591 16.634 25.566 1.00 16.37 ? 199 GLY B N 1 ATOM 3564 C CA . GLY B 1 199 ? 33.019 16.725 25.319 1.00 17.68 ? 199 GLY B CA 1 ATOM 3565 C C . GLY B 1 199 ? 33.721 17.641 26.302 1.00 20.26 ? 199 GLY B C 1 ATOM 3566 O O . GLY B 1 199 ? 34.777 17.290 26.836 1.00 20.85 ? 199 GLY B O 1 ATOM 3567 N N . LYS B 1 200 ? 33.146 18.818 26.543 1.00 21.05 ? 200 LYS B N 1 ATOM 3568 C CA . LYS B 1 200 ? 33.737 19.771 27.478 1.00 21.60 ? 200 LYS B CA 1 ATOM 3569 C C . LYS B 1 200 ? 33.760 19.212 28.902 1.00 20.77 ? 200 LYS B C 1 ATOM 3570 O O . LYS B 1 200 ? 34.763 19.334 29.605 1.00 19.66 ? 200 LYS B O 1 ATOM 3571 C CB . LYS B 1 200 ? 32.969 21.099 27.461 1.00 24.78 ? 200 LYS B CB 1 ATOM 3572 C CG . LYS B 1 200 ? 33.143 21.912 26.180 1.00 27.15 ? 200 LYS B CG 1 ATOM 3573 C CD . LYS B 1 200 ? 32.620 23.339 26.367 1.00 30.35 ? 200 LYS B CD 1 ATOM 3574 C CE . LYS B 1 200 ? 32.768 24.189 25.101 1.00 31.87 ? 200 LYS B CE 1 ATOM 3575 N NZ . LYS B 1 200 ? 31.812 23.790 24.017 1.00 35.81 ? 200 LYS B NZ 1 ATOM 3576 N N . LEU B 1 201 ? 32.655 18.601 29.326 1.00 18.64 ? 201 LEU B N 1 ATOM 3577 C CA . LEU B 1 201 ? 32.579 18.021 30.666 1.00 17.39 ? 201 LEU B CA 1 ATOM 3578 C C . LEU B 1 201 ? 33.600 16.897 30.823 1.00 16.43 ? 201 LEU B C 1 ATOM 3579 O O . LEU B 1 201 ? 34.276 16.802 31.847 1.00 16.25 ? 201 LEU B O 1 ATOM 3580 C CB . LEU B 1 201 ? 31.172 17.473 30.933 1.00 15.53 ? 201 LEU B CB 1 ATOM 3581 C CG . LEU B 1 201 ? 30.044 18.493 31.084 1.00 15.90 ? 201 LEU B CG 1 ATOM 3582 C CD1 . LEU B 1 201 ? 28.686 17.790 30.986 1.00 16.62 ? 201 LEU B CD1 1 ATOM 3583 C CD2 . LEU B 1 201 ? 30.190 19.218 32.409 1.00 14.05 ? 201 LEU B CD2 1 ATOM 3584 N N . SER B 1 202 ? 33.703 16.049 29.803 1.00 16.13 ? 202 SER B N 1 ATOM 3585 C CA . SER B 1 202 ? 34.635 14.929 29.823 1.00 16.37 ? 202 SER B CA 1 ATOM 3586 C C . SER B 1 202 ? 36.076 15.427 29.953 1.00 18.47 ? 202 SER B C 1 ATOM 3587 O O . SER B 1 202 ? 36.894 14.823 30.658 1.00 18.69 ? 202 SER B O 1 ATOM 3588 C CB . SER B 1 202 ? 34.484 14.085 28.549 1.00 16.91 ? 202 SER B CB 1 ATOM 3589 O OG . SER B 1 202 ? 33.195 13.486 28.457 1.00 13.68 ? 202 SER B OG 1 ATOM 3590 N N . PHE B 1 203 ? 36.391 16.531 29.280 1.00 17.55 ? 203 PHE B N 1 ATOM 3591 C CA . PHE B 1 203 ? 37.742 17.080 29.347 1.00 16.89 ? 203 PHE B CA 1 ATOM 3592 C C . PHE B 1 203 ? 38.059 17.662 30.720 1.00 17.47 ? 203 PHE B C 1 ATOM 3593 O O . PHE B 1 203 ? 39.110 17.375 31.293 1.00 18.40 ? 203 PHE B O 1 ATOM 3594 C CB . PHE B 1 203 ? 37.943 18.157 28.274 1.00 16.94 ? 203 PHE B CB 1 ATOM 3595 C CG . PHE B 1 203 ? 39.268 18.859 28.369 1.00 15.24 ? 203 PHE B CG 1 ATOM 3596 C CD1 . PHE B 1 203 ? 39.360 20.120 28.947 1.00 15.47 ? 203 PHE B CD1 1 ATOM 3597 C CD2 . PHE B 1 203 ? 40.429 18.233 27.926 1.00 16.82 ? 203 PHE B CD2 1 ATOM 3598 C CE1 . PHE B 1 203 ? 40.596 20.755 29.089 1.00 17.47 ? 203 PHE B CE1 1 ATOM 3599 C CE2 . PHE B 1 203 ? 41.674 18.852 28.061 1.00 17.35 ? 203 PHE B CE2 1 ATOM 3600 C CZ . PHE B 1 203 ? 41.757 20.118 28.646 1.00 17.24 ? 203 PHE B CZ 1 ATOM 3601 N N . GLN B 1 204 ? 37.153 18.477 31.251 1.00 16.83 ? 204 GLN B N 1 ATOM 3602 C CA . GLN B 1 204 ? 37.364 19.092 32.552 1.00 17.82 ? 204 GLN B CA 1 ATOM 3603 C C . GLN B 1 204 ? 37.402 18.048 33.664 1.00 18.93 ? 204 GLN B C 1 ATOM 3604 O O . GLN B 1 204 ? 38.169 18.177 34.622 1.00 20.22 ? 204 GLN B O 1 ATOM 3605 C CB . GLN B 1 204 ? 36.267 20.129 32.841 1.00 18.02 ? 204 GLN B CB 1 ATOM 3606 C CG . GLN B 1 204 ? 36.289 21.338 31.900 1.00 18.25 ? 204 GLN B CG 1 ATOM 3607 C CD . GLN B 1 204 ? 37.562 22.173 32.036 1.00 20.34 ? 204 GLN B CD 1 ATOM 3608 O OE1 . GLN B 1 204 ? 37.962 22.877 31.107 1.00 20.99 ? 204 GLN B OE1 1 ATOM 3609 N NE2 . GLN B 1 204 ? 38.191 22.105 33.197 1.00 19.23 ? 204 GLN B NE2 1 ATOM 3610 N N . ILE B 1 205 ? 36.582 17.009 33.542 1.00 17.83 ? 205 ILE B N 1 ATOM 3611 C CA . ILE B 1 205 ? 36.560 15.972 34.565 1.00 17.50 ? 205 ILE B CA 1 ATOM 3612 C C . ILE B 1 205 ? 37.847 15.149 34.525 1.00 17.83 ? 205 ILE B C 1 ATOM 3613 O O . ILE B 1 205 ? 38.527 15.001 35.541 1.00 16.48 ? 205 ILE B O 1 ATOM 3614 C CB . ILE B 1 205 ? 35.332 15.037 34.397 1.00 17.08 ? 205 ILE B CB 1 ATOM 3615 C CG1 . ILE B 1 205 ? 34.042 15.837 34.624 1.00 15.57 ? 205 ILE B CG1 1 ATOM 3616 C CG2 . ILE B 1 205 ? 35.413 13.869 35.385 1.00 15.59 ? 205 ILE B CG2 1 ATOM 3617 C CD1 . ILE B 1 205 ? 32.760 15.051 34.409 1.00 13.47 ? 205 ILE B CD1 1 ATOM 3618 N N . ARG B 1 206 ? 38.199 14.643 33.348 1.00 18.24 ? 206 ARG B N 1 ATOM 3619 C CA . ARG B 1 206 ? 39.398 13.821 33.224 1.00 18.68 ? 206 ARG B CA 1 ATOM 3620 C C . ARG B 1 206 ? 40.680 14.517 33.648 1.00 19.05 ? 206 ARG B C 1 ATOM 3621 O O . ARG B 1 206 ? 41.520 13.913 34.311 1.00 19.51 ? 206 ARG B O 1 ATOM 3622 C CB . ARG B 1 206 ? 39.579 13.318 31.794 1.00 19.12 ? 206 ARG B CB 1 ATOM 3623 C CG . ARG B 1 206 ? 40.765 12.365 31.653 1.00 20.24 ? 206 ARG B CG 1 ATOM 3624 C CD . ARG B 1 206 ? 40.995 11.914 30.211 1.00 20.14 ? 206 ARG B CD 1 ATOM 3625 N NE . ARG B 1 206 ? 41.483 12.991 29.350 1.00 20.86 ? 206 ARG B NE 1 ATOM 3626 C CZ . ARG B 1 206 ? 42.720 13.485 29.375 1.00 20.88 ? 206 ARG B CZ 1 ATOM 3627 N NH1 . ARG B 1 206 ? 43.626 13.004 30.222 1.00 22.03 ? 206 ARG B NH1 1 ATOM 3628 N NH2 . ARG B 1 206 ? 43.051 14.466 28.550 1.00 18.90 ? 206 ARG B NH2 1 ATOM 3629 N N . THR B 1 207 ? 40.836 15.784 33.281 1.00 19.81 ? 207 THR B N 1 ATOM 3630 C CA . THR B 1 207 ? 42.063 16.504 33.612 1.00 19.90 ? 207 THR B CA 1 ATOM 3631 C C . THR B 1 207 ? 42.132 17.103 35.018 1.00 20.86 ? 207 THR B C 1 ATOM 3632 O O . THR B 1 207 ? 43.204 17.518 35.461 1.00 21.18 ? 207 THR B O 1 ATOM 3633 C CB . THR B 1 207 ? 42.366 17.615 32.552 1.00 18.59 ? 207 THR B CB 1 ATOM 3634 O OG1 . THR B 1 207 ? 41.311 18.584 32.534 1.00 17.94 ? 207 THR B OG1 1 ATOM 3635 C CG2 . THR B 1 207 ? 42.501 16.996 31.166 1.00 16.89 ? 207 THR B CG2 1 ATOM 3636 N N . SER B 1 208 ? 41.006 17.135 35.729 1.00 22.09 ? 208 SER B N 1 ATOM 3637 C CA . SER B 1 208 ? 40.981 17.697 37.084 1.00 21.15 ? 208 SER B CA 1 ATOM 3638 C C . SER B 1 208 ? 41.709 16.804 38.089 1.00 20.45 ? 208 SER B C 1 ATOM 3639 O O . SER B 1 208 ? 41.822 15.595 37.895 1.00 19.88 ? 208 SER B O 1 ATOM 3640 C CB . SER B 1 208 ? 39.534 17.921 37.549 1.00 20.46 ? 208 SER B CB 1 ATOM 3641 O OG . SER B 1 208 ? 38.865 16.689 37.741 1.00 24.35 ? 208 SER B OG 1 ATOM 3642 N N . GLY B 1 209 ? 42.208 17.412 39.160 1.00 20.38 ? 209 GLY B N 1 ATOM 3643 C CA . GLY B 1 209 ? 42.915 16.657 40.177 1.00 21.46 ? 209 GLY B CA 1 ATOM 3644 C C . GLY B 1 209 ? 41.944 15.927 41.077 1.00 22.95 ? 209 GLY B C 1 ATOM 3645 O O . GLY B 1 209 ? 40.756 15.855 40.773 1.00 23.25 ? 209 GLY B O 1 ATOM 3646 N N . ALA B 1 210 ? 42.437 15.396 42.192 1.00 24.01 ? 210 ALA B N 1 ATOM 3647 C CA . ALA B 1 210 ? 41.594 14.650 43.124 1.00 25.60 ? 210 ALA B CA 1 ATOM 3648 C C . ALA B 1 210 ? 40.414 15.449 43.678 1.00 26.47 ? 210 ALA B C 1 ATOM 3649 O O . ALA B 1 210 ? 39.346 14.883 43.939 1.00 27.01 ? 210 ALA B O 1 ATOM 3650 C CB . ALA B 1 210 ? 42.444 14.108 44.277 1.00 26.80 ? 210 ALA B CB 1 ATOM 3651 N N . ASN B 1 211 ? 40.600 16.754 43.862 1.00 26.87 ? 211 ASN B N 1 ATOM 3652 C CA . ASN B 1 211 ? 39.526 17.595 44.383 1.00 27.86 ? 211 ASN B CA 1 ATOM 3653 C C . ASN B 1 211 ? 38.403 17.785 43.360 1.00 27.56 ? 211 ASN B C 1 ATOM 3654 O O . ASN B 1 211 ? 37.390 18.417 43.653 1.00 28.33 ? 211 ASN B O 1 ATOM 3655 C CB . ASN B 1 211 ? 40.067 18.962 44.819 1.00 29.55 ? 211 ASN B CB 1 ATOM 3656 C CG . ASN B 1 211 ? 40.804 19.683 43.708 1.00 33.05 ? 211 ASN B CG 1 ATOM 3657 O OD1 . ASN B 1 211 ? 40.343 19.737 42.566 1.00 36.68 ? 211 ASN B OD1 1 ATOM 3658 N ND2 . ASN B 1 211 ? 41.953 20.253 44.040 1.00 34.10 ? 211 ASN B ND2 1 ATOM 3659 N N . GLY B 1 212 ? 38.591 17.238 42.163 1.00 25.77 ? 212 GLY B N 1 ATOM 3660 C CA . GLY B 1 212 ? 37.581 17.344 41.128 1.00 25.56 ? 212 GLY B CA 1 ATOM 3661 C C . GLY B 1 212 ? 37.254 18.745 40.634 1.00 26.36 ? 212 GLY B C 1 ATOM 3662 O O . GLY B 1 212 ? 36.243 18.937 39.949 1.00 25.70 ? 212 GLY B O 1 ATOM 3663 N N . MET B 1 213 ? 38.093 19.726 40.963 1.00 26.25 ? 213 MET B N 1 ATOM 3664 C CA . MET B 1 213 ? 37.852 21.101 40.528 1.00 27.13 ? 213 MET B CA 1 ATOM 3665 C C . MET B 1 213 ? 38.213 21.318 39.054 1.00 26.95 ? 213 MET B C 1 ATOM 3666 O O . MET B 1 213 ? 39.311 20.968 38.612 1.00 26.49 ? 213 MET B O 1 ATOM 3667 C CB . MET B 1 213 ? 38.643 22.080 41.400 1.00 29.62 ? 213 MET B CB 1 ATOM 3668 C CG . MET B 1 213 ? 38.230 22.078 42.869 1.00 35.09 ? 213 MET B CG 1 ATOM 3669 S SD . MET B 1 213 ? 36.439 22.337 43.115 1.00 41.03 ? 213 MET B SD 1 ATOM 3670 C CE . MET B 1 213 ? 35.997 20.872 44.103 1.00 38.44 ? 213 MET B CE 1 ATOM 3671 N N . PHE B 1 214 ? 37.278 21.898 38.304 1.00 25.53 ? 214 PHE B N 1 ATOM 3672 C CA . PHE B 1 214 ? 37.460 22.178 36.878 1.00 25.58 ? 214 PHE B CA 1 ATOM 3673 C C . PHE B 1 214 ? 38.397 23.358 36.680 1.00 27.29 ? 214 PHE B C 1 ATOM 3674 O O . PHE B 1 214 ? 38.291 24.358 37.395 1.00 28.52 ? 214 PHE B O 1 ATOM 3675 C CB . PHE B 1 214 ? 36.119 22.543 36.224 1.00 24.00 ? 214 PHE B CB 1 ATOM 3676 C CG . PHE B 1 214 ? 35.191 21.383 36.002 1.00 21.80 ? 214 PHE B CG 1 ATOM 3677 C CD1 . PHE B 1 214 ? 35.417 20.147 36.605 1.00 18.71 ? 214 PHE B CD1 1 ATOM 3678 C CD2 . PHE B 1 214 ? 34.066 21.540 35.190 1.00 21.18 ? 214 PHE B CD2 1 ATOM 3679 C CE1 . PHE B 1 214 ? 34.537 19.087 36.402 1.00 17.91 ? 214 PHE B CE1 1 ATOM 3680 C CE2 . PHE B 1 214 ? 33.178 20.487 34.982 1.00 19.86 ? 214 PHE B CE2 1 ATOM 3681 C CZ . PHE B 1 214 ? 33.414 19.257 35.589 1.00 19.27 ? 214 PHE B CZ 1 ATOM 3682 N N . SER B 1 215 ? 39.303 23.262 35.712 1.00 28.08 ? 215 SER B N 1 ATOM 3683 C CA . SER B 1 215 ? 40.199 24.378 35.436 1.00 29.54 ? 215 SER B CA 1 ATOM 3684 C C . SER B 1 215 ? 39.325 25.505 34.875 1.00 30.31 ? 215 SER B C 1 ATOM 3685 O O . SER B 1 215 ? 39.620 26.691 35.056 1.00 29.97 ? 215 SER B O 1 ATOM 3686 C CB . SER B 1 215 ? 41.268 23.971 34.424 1.00 30.52 ? 215 SER B CB 1 ATOM 3687 O OG . SER B 1 215 ? 40.680 23.424 33.260 1.00 35.56 ? 215 SER B OG 1 ATOM 3688 N N . GLU B 1 216 ? 38.240 25.115 34.202 1.00 30.44 ? 216 GLU B N 1 ATOM 3689 C CA . GLU B 1 216 ? 37.275 26.057 33.632 1.00 30.18 ? 216 GLU B CA 1 ATOM 3690 C C . GLU B 1 216 ? 35.851 25.521 33.759 1.00 28.55 ? 216 GLU B C 1 ATOM 3691 O O . GLU B 1 216 ? 35.585 24.352 33.482 1.00 27.40 ? 216 GLU B O 1 ATOM 3692 C CB . GLU B 1 216 ? 37.606 26.336 32.171 1.00 32.88 ? 216 GLU B CB 1 ATOM 3693 C CG . GLU B 1 216 ? 38.890 27.125 32.014 1.00 40.54 ? 216 GLU B CG 1 ATOM 3694 C CD . GLU B 1 216 ? 39.766 26.591 30.903 1.00 45.30 ? 216 GLU B CD 1 ATOM 3695 O OE1 . GLU B 1 216 ? 40.069 25.375 30.918 1.00 47.48 ? 216 GLU B OE1 1 ATOM 3696 O OE2 . GLU B 1 216 ? 40.158 27.386 30.019 1.00 48.80 ? 216 GLU B OE2 1 ATOM 3697 N N . ALA B 1 217 ? 34.943 26.388 34.194 1.00 26.62 ? 217 ALA B N 1 ATOM 3698 C CA . ALA B 1 217 ? 33.544 26.020 34.378 1.00 25.12 ? 217 ALA B CA 1 ATOM 3699 C C . ALA B 1 217 ? 32.846 25.700 33.065 1.00 24.54 ? 217 ALA B C 1 ATOM 3700 O O . ALA B 1 217 ? 33.177 26.254 32.014 1.00 22.67 ? 217 ALA B O 1 ATOM 3701 C CB . ALA B 1 217 ? 32.800 27.146 35.092 1.00 24.62 ? 217 ALA B CB 1 ATOM 3702 N N . VAL B 1 218 ? 31.878 24.792 33.138 1.00 24.18 ? 218 VAL B N 1 ATOM 3703 C CA . VAL B 1 218 ? 31.096 24.402 31.975 1.00 23.43 ? 218 VAL B CA 1 ATOM 3704 C C . VAL B 1 218 ? 29.673 24.873 32.235 1.00 23.39 ? 218 VAL B C 1 ATOM 3705 O O . VAL B 1 218 ? 29.105 24.611 33.295 1.00 23.29 ? 218 VAL B O 1 ATOM 3706 C CB . VAL B 1 218 ? 31.089 22.873 31.769 1.00 22.43 ? 218 VAL B CB 1 ATOM 3707 C CG1 . VAL B 1 218 ? 30.290 22.527 30.525 1.00 23.91 ? 218 VAL B CG1 1 ATOM 3708 C CG2 . VAL B 1 218 ? 32.512 22.353 31.636 1.00 23.27 ? 218 VAL B CG2 1 ATOM 3709 N N . GLU B 1 219 ? 29.099 25.576 31.268 1.00 24.46 ? 219 GLU B N 1 ATOM 3710 C CA . GLU B 1 219 ? 27.746 26.087 31.424 1.00 25.24 ? 219 GLU B CA 1 ATOM 3711 C C . GLU B 1 219 ? 26.664 25.135 30.931 1.00 23.24 ? 219 GLU B C 1 ATOM 3712 O O . GLU B 1 219 ? 26.714 24.646 29.803 1.00 22.16 ? 219 GLU B O 1 ATOM 3713 C CB . GLU B 1 219 ? 27.605 27.426 30.698 1.00 26.49 ? 219 GLU B CB 1 ATOM 3714 C CG . GLU B 1 219 ? 26.198 27.987 30.720 1.00 30.83 ? 219 GLU B CG 1 ATOM 3715 C CD . GLU B 1 219 ? 26.117 29.345 30.062 1.00 33.22 ? 219 GLU B CD 1 ATOM 3716 O OE1 . GLU B 1 219 ? 26.452 30.348 30.726 1.00 36.57 ? 219 GLU B OE1 1 ATOM 3717 O OE2 . GLU B 1 219 ? 25.733 29.407 28.876 1.00 34.69 ? 219 GLU B OE2 1 ATOM 3718 N N . LEU B 1 220 ? 25.693 24.879 31.799 1.00 21.80 ? 220 LEU B N 1 ATOM 3719 C CA . LEU B 1 220 ? 24.567 24.018 31.477 1.00 22.08 ? 220 LEU B CA 1 ATOM 3720 C C . LEU B 1 220 ? 23.283 24.824 31.688 1.00 23.53 ? 220 LEU B C 1 ATOM 3721 O O . LEU B 1 220 ? 23.331 25.988 32.088 1.00 24.49 ? 220 LEU B O 1 ATOM 3722 C CB . LEU B 1 220 ? 24.564 22.772 32.364 1.00 19.00 ? 220 LEU B CB 1 ATOM 3723 C CG . LEU B 1 220 ? 25.667 21.743 32.100 1.00 17.56 ? 220 LEU B CG 1 ATOM 3724 C CD1 . LEU B 1 220 ? 25.538 20.600 33.091 1.00 15.17 ? 220 LEU B CD1 1 ATOM 3725 C CD2 . LEU B 1 220 ? 25.565 21.227 30.671 1.00 16.71 ? 220 LEU B CD2 1 ATOM 3726 N N . GLU B 1 221 ? 22.140 24.208 31.414 1.00 24.22 ? 221 GLU B N 1 ATOM 3727 C CA . GLU B 1 221 ? 20.862 24.885 31.561 1.00 25.98 ? 221 GLU B CA 1 ATOM 3728 C C . GLU B 1 221 ? 19.799 24.009 32.191 1.00 26.87 ? 221 GLU B C 1 ATOM 3729 O O . GLU B 1 221 ? 19.775 22.797 31.977 1.00 26.35 ? 221 GLU B O 1 ATOM 3730 C CB . GLU B 1 221 ? 20.362 25.354 30.198 1.00 26.10 ? 221 GLU B CB 1 ATOM 3731 C CG . GLU B 1 221 ? 20.950 26.659 29.741 1.00 28.38 ? 221 GLU B CG 1 ATOM 3732 C CD . GLU B 1 221 ? 20.513 27.017 28.344 1.00 29.35 ? 221 GLU B CD 1 ATOM 3733 O OE1 . GLU B 1 221 ? 19.400 26.601 27.953 1.00 29.54 ? 221 GLU B OE1 1 ATOM 3734 O OE2 . GLU B 1 221 ? 21.272 27.721 27.642 1.00 30.63 ? 221 GLU B OE2 1 ATOM 3735 N N . ARG B 1 222 ? 18.924 24.633 32.975 1.00 28.02 ? 222 ARG B N 1 ATOM 3736 C CA . ARG B 1 222 ? 17.826 23.919 33.612 1.00 28.74 ? 222 ARG B CA 1 ATOM 3737 C C . ARG B 1 222 ? 16.761 23.759 32.529 1.00 29.20 ? 222 ARG B C 1 ATOM 3738 O O . ARG B 1 222 ? 16.898 24.310 31.433 1.00 29.12 ? 222 ARG B O 1 ATOM 3739 C CB . ARG B 1 222 ? 17.266 24.732 34.784 1.00 28.88 ? 222 ARG B CB 1 ATOM 3740 C CG . ARG B 1 222 ? 18.258 24.978 35.913 1.00 28.37 ? 222 ARG B CG 1 ATOM 3741 C CD . ARG B 1 222 ? 18.638 23.679 36.593 1.00 29.42 ? 222 ARG B CD 1 ATOM 3742 N NE . ARG B 1 222 ? 19.541 23.883 37.724 1.00 31.71 ? 222 ARG B NE 1 ATOM 3743 C CZ . ARG B 1 222 ? 20.137 22.898 38.397 1.00 31.47 ? 222 ARG B CZ 1 ATOM 3744 N NH1 . ARG B 1 222 ? 19.931 21.631 38.056 1.00 31.86 ? 222 ARG B NH1 1 ATOM 3745 N NH2 . ARG B 1 222 ? 20.939 23.177 39.412 1.00 30.10 ? 222 ARG B NH2 1 ATOM 3746 N N . ALA B 1 223 ? 15.707 23.011 32.826 1.00 30.21 ? 223 ALA B N 1 ATOM 3747 C CA . ALA B 1 223 ? 14.647 22.795 31.849 1.00 31.69 ? 223 ALA B CA 1 ATOM 3748 C C . ALA B 1 223 ? 14.147 24.109 31.244 1.00 33.05 ? 223 ALA B C 1 ATOM 3749 O O . ALA B 1 223 ? 14.021 24.231 30.025 1.00 32.13 ? 223 ALA B O 1 ATOM 3750 C CB . ALA B 1 223 ? 13.485 22.037 32.498 1.00 31.80 ? 223 ALA B CB 1 ATOM 3751 N N . ASN B 1 224 ? 13.886 25.093 32.103 1.00 35.53 ? 224 ASN B N 1 ATOM 3752 C CA . ASN B 1 224 ? 13.373 26.394 31.673 1.00 36.14 ? 224 ASN B CA 1 ATOM 3753 C C . ASN B 1 224 ? 14.384 27.258 30.930 1.00 35.58 ? 224 ASN B C 1 ATOM 3754 O O . ASN B 1 224 ? 14.071 28.374 30.522 1.00 35.78 ? 224 ASN B O 1 ATOM 3755 C CB . ASN B 1 224 ? 12.834 27.165 32.879 1.00 38.80 ? 224 ASN B CB 1 ATOM 3756 C CG . ASN B 1 224 ? 13.931 27.675 33.783 1.00 41.98 ? 224 ASN B CG 1 ATOM 3757 O OD1 . ASN B 1 224 ? 14.812 26.923 34.201 1.00 44.11 ? 224 ASN B OD1 1 ATOM 3758 N ND2 . ASN B 1 224 ? 13.882 28.962 34.098 1.00 45.58 ? 224 ASN B ND2 1 ATOM 3759 N N . GLY B 1 225 ? 15.597 26.750 30.757 1.00 34.92 ? 225 GLY B N 1 ATOM 3760 C CA . GLY B 1 225 ? 16.600 27.510 30.035 1.00 33.74 ? 225 GLY B CA 1 ATOM 3761 C C . GLY B 1 225 ? 17.530 28.329 30.905 1.00 33.41 ? 225 GLY B C 1 ATOM 3762 O O . GLY B 1 225 ? 18.480 28.928 30.399 1.00 32.77 ? 225 GLY B O 1 ATOM 3763 N N . LYS B 1 226 ? 17.273 28.368 32.209 1.00 33.69 ? 226 LYS B N 1 ATOM 3764 C CA . LYS B 1 226 ? 18.136 29.137 33.095 1.00 33.80 ? 226 LYS B CA 1 ATOM 3765 C C . LYS B 1 226 ? 19.538 28.532 33.123 1.00 33.63 ? 226 LYS B C 1 ATOM 3766 O O . LYS B 1 226 ? 19.712 27.333 33.364 1.00 33.42 ? 226 LYS B O 1 ATOM 3767 C CB . LYS B 1 226 ? 17.572 29.187 34.511 1.00 35.04 ? 226 LYS B CB 1 ATOM 3768 C CG . LYS B 1 226 ? 18.296 30.212 35.357 1.00 36.54 ? 226 LYS B CG 1 ATOM 3769 C CD . LYS B 1 226 ? 18.021 30.036 36.824 1.00 38.55 ? 226 LYS B CD 1 ATOM 3770 C CE . LYS B 1 226 ? 18.852 31.015 37.624 1.00 38.90 ? 226 LYS B CE 1 ATOM 3771 N NZ . LYS B 1 226 ? 18.668 30.801 39.078 1.00 42.30 ? 226 LYS B NZ 1 ATOM 3772 N N . LYS B 1 227 ? 20.536 29.372 32.876 1.00 32.77 ? 227 LYS B N 1 ATOM 3773 C CA . LYS B 1 227 ? 21.916 28.927 32.842 1.00 32.41 ? 227 LYS B CA 1 ATOM 3774 C C . LYS B 1 227 ? 22.545 28.828 34.219 1.00 32.56 ? 227 LYS B C 1 ATOM 3775 O O . LYS B 1 227 ? 22.242 29.615 35.116 1.00 33.05 ? 227 LYS B O 1 ATOM 3776 C CB . LYS B 1 227 ? 22.752 29.876 31.983 1.00 32.53 ? 227 LYS B CB 1 ATOM 3777 C CG . LYS B 1 227 ? 22.110 30.243 30.656 1.00 34.14 ? 227 LYS B CG 1 ATOM 3778 C CD . LYS B 1 227 ? 22.972 31.236 29.894 1.00 36.06 ? 227 LYS B CD 1 ATOM 3779 C CE . LYS B 1 227 ? 22.206 31.872 28.747 1.00 37.37 ? 227 LYS B CE 1 ATOM 3780 N NZ . LYS B 1 227 ? 21.664 30.852 27.807 1.00 41.01 ? 227 LYS B NZ 1 ATOM 3781 N N . TYR B 1 228 ? 23.413 27.834 34.377 1.00 31.89 ? 228 TYR B N 1 ATOM 3782 C CA . TYR B 1 228 ? 24.148 27.621 35.612 1.00 30.36 ? 228 TYR B CA 1 ATOM 3783 C C . TYR B 1 228 ? 25.485 27.024 35.213 1.00 31.21 ? 228 TYR B C 1 ATOM 3784 O O . TYR B 1 228 ? 25.628 26.499 34.106 1.00 31.83 ? 228 TYR B O 1 ATOM 3785 C CB . TYR B 1 228 ? 23.400 26.692 36.578 1.00 29.86 ? 228 TYR B CB 1 ATOM 3786 C CG . TYR B 1 228 ? 23.220 25.256 36.133 1.00 31.19 ? 228 TYR B CG 1 ATOM 3787 C CD1 . TYR B 1 228 ? 22.210 24.901 35.236 1.00 29.57 ? 228 TYR B CD1 1 ATOM 3788 C CD2 . TYR B 1 228 ? 24.033 24.240 36.649 1.00 30.64 ? 228 TYR B CD2 1 ATOM 3789 C CE1 . TYR B 1 228 ? 22.008 23.573 34.871 1.00 29.37 ? 228 TYR B CE1 1 ATOM 3790 C CE2 . TYR B 1 228 ? 23.841 22.914 36.290 1.00 29.28 ? 228 TYR B CE2 1 ATOM 3791 C CZ . TYR B 1 228 ? 22.825 22.586 35.402 1.00 30.78 ? 228 TYR B CZ 1 ATOM 3792 O OH . TYR B 1 228 ? 22.611 21.268 35.062 1.00 32.37 ? 228 TYR B OH 1 ATOM 3793 N N . TYR B 1 229 ? 26.470 27.111 36.100 1.00 31.38 ? 229 TYR B N 1 ATOM 3794 C CA . TYR B 1 229 ? 27.793 26.595 35.792 1.00 30.28 ? 229 TYR B CA 1 ATOM 3795 C C . TYR B 1 229 ? 28.208 25.413 36.633 1.00 28.14 ? 229 TYR B C 1 ATOM 3796 O O . TYR B 1 229 ? 27.898 25.335 37.820 1.00 27.34 ? 229 TYR B O 1 ATOM 3797 C CB . TYR B 1 229 ? 28.835 27.700 35.947 1.00 34.48 ? 229 TYR B CB 1 ATOM 3798 C CG . TYR B 1 229 ? 28.623 28.873 35.021 1.00 38.41 ? 229 TYR B CG 1 ATOM 3799 C CD1 . TYR B 1 229 ? 27.442 29.616 35.063 1.00 40.49 ? 229 TYR B CD1 1 ATOM 3800 C CD2 . TYR B 1 229 ? 29.607 29.249 34.108 1.00 40.10 ? 229 TYR B CD2 1 ATOM 3801 C CE1 . TYR B 1 229 ? 27.244 30.703 34.221 1.00 43.65 ? 229 TYR B CE1 1 ATOM 3802 C CE2 . TYR B 1 229 ? 29.425 30.338 33.263 1.00 43.31 ? 229 TYR B CE2 1 ATOM 3803 C CZ . TYR B 1 229 ? 28.241 31.061 33.324 1.00 45.31 ? 229 TYR B CZ 1 ATOM 3804 O OH . TYR B 1 229 ? 28.056 32.147 32.493 1.00 49.43 ? 229 TYR B OH 1 ATOM 3805 N N . VAL B 1 230 ? 28.908 24.487 35.992 1.00 26.44 ? 230 VAL B N 1 ATOM 3806 C CA . VAL B 1 230 ? 29.425 23.304 36.664 1.00 25.15 ? 230 VAL B CA 1 ATOM 3807 C C . VAL B 1 230 ? 30.905 23.604 36.867 1.00 24.06 ? 230 VAL B C 1 ATOM 3808 O O . VAL B 1 230 ? 31.623 23.863 35.902 1.00 25.14 ? 230 VAL B O 1 ATOM 3809 C CB . VAL B 1 230 ? 29.285 22.039 35.783 1.00 25.19 ? 230 VAL B CB 1 ATOM 3810 C CG1 . VAL B 1 230 ? 30.009 20.868 36.429 1.00 23.30 ? 230 VAL B CG1 1 ATOM 3811 C CG2 . VAL B 1 230 ? 27.814 21.705 35.581 1.00 25.04 ? 230 VAL B CG2 1 ATOM 3812 N N . THR B 1 231 ? 31.360 23.592 38.114 1.00 23.25 ? 231 THR B N 1 ATOM 3813 C CA . THR B 1 231 ? 32.765 23.872 38.386 1.00 21.96 ? 231 THR B CA 1 ATOM 3814 C C . THR B 1 231 ? 33.493 22.708 39.053 1.00 21.99 ? 231 THR B C 1 ATOM 3815 O O . THR B 1 231 ? 34.715 22.750 39.197 1.00 23.70 ? 231 THR B O 1 ATOM 3816 C CB . THR B 1 231 ? 32.923 25.126 39.264 1.00 20.90 ? 231 THR B CB 1 ATOM 3817 O OG1 . THR B 1 231 ? 32.224 24.938 40.498 1.00 21.07 ? 231 THR B OG1 1 ATOM 3818 C CG2 . THR B 1 231 ? 32.368 26.343 38.551 1.00 20.27 ? 231 THR B CG2 1 ATOM 3819 N N . ALA B 1 232 ? 32.752 21.676 39.454 1.00 19.77 ? 232 ALA B N 1 ATOM 3820 C CA . ALA B 1 232 ? 33.355 20.506 40.088 1.00 20.57 ? 232 ALA B CA 1 ATOM 3821 C C . ALA B 1 232 ? 32.718 19.210 39.595 1.00 20.89 ? 232 ALA B C 1 ATOM 3822 O O . ALA B 1 232 ? 31.545 19.188 39.219 1.00 20.04 ? 232 ALA B O 1 ATOM 3823 C CB . ALA B 1 232 ? 33.234 20.602 41.603 1.00 20.01 ? 232 ALA B CB 1 ATOM 3824 N N . VAL B 1 233 ? 33.508 18.136 39.605 1.00 22.07 ? 233 VAL B N 1 ATOM 3825 C CA . VAL B 1 233 ? 33.063 16.808 39.161 1.00 21.54 ? 233 VAL B CA 1 ATOM 3826 C C . VAL B 1 233 ? 31.811 16.295 39.879 1.00 22.49 ? 233 VAL B C 1 ATOM 3827 O O . VAL B 1 233 ? 30.905 15.759 39.240 1.00 21.11 ? 233 VAL B O 1 ATOM 3828 C CB . VAL B 1 233 ? 34.196 15.746 39.342 1.00 21.00 ? 233 VAL B CB 1 ATOM 3829 C CG1 . VAL B 1 233 ? 33.670 14.340 39.019 1.00 18.62 ? 233 VAL B CG1 1 ATOM 3830 C CG2 . VAL B 1 233 ? 35.379 16.082 38.433 1.00 19.21 ? 233 VAL B CG2 1 ATOM 3831 N N . ASP B 1 234 ? 31.768 16.454 41.200 1.00 23.18 ? 234 ASP B N 1 ATOM 3832 C CA . ASP B 1 234 ? 30.637 15.985 41.995 1.00 23.08 ? 234 ASP B CA 1 ATOM 3833 C C . ASP B 1 234 ? 29.304 16.614 41.626 1.00 22.70 ? 234 ASP B C 1 ATOM 3834 O O . ASP B 1 234 ? 28.258 16.020 41.851 1.00 23.17 ? 234 ASP B O 1 ATOM 3835 C CB . ASP B 1 234 ? 30.909 16.210 43.478 1.00 26.88 ? 234 ASP B CB 1 ATOM 3836 C CG . ASP B 1 234 ? 31.716 15.088 44.094 1.00 31.60 ? 234 ASP B CG 1 ATOM 3837 O OD1 . ASP B 1 234 ? 32.123 14.165 43.345 1.00 33.14 ? 234 ASP B OD1 1 ATOM 3838 O OD2 . ASP B 1 234 ? 31.939 15.130 45.329 1.00 34.21 ? 234 ASP B OD2 1 ATOM 3839 N N . GLN B 1 235 ? 29.336 17.814 41.064 1.00 21.73 ? 235 GLN B N 1 ATOM 3840 C CA . GLN B 1 235 ? 28.109 18.496 40.669 1.00 21.91 ? 235 GLN B CA 1 ATOM 3841 C C . GLN B 1 235 ? 27.436 17.824 39.474 1.00 23.12 ? 235 GLN B C 1 ATOM 3842 O O . GLN B 1 235 ? 26.225 17.929 39.290 1.00 24.10 ? 235 GLN B O 1 ATOM 3843 C CB . GLN B 1 235 ? 28.413 19.942 40.291 1.00 22.48 ? 235 GLN B CB 1 ATOM 3844 C CG . GLN B 1 235 ? 28.785 20.839 41.443 1.00 23.58 ? 235 GLN B CG 1 ATOM 3845 C CD . GLN B 1 235 ? 29.590 22.040 40.994 1.00 25.12 ? 235 GLN B CD 1 ATOM 3846 O OE1 . GLN B 1 235 ? 29.348 22.609 39.928 1.00 22.65 ? 235 GLN B OE1 1 ATOM 3847 N NE2 . GLN B 1 235 ? 30.555 22.438 41.815 1.00 28.68 ? 235 GLN B NE2 1 ATOM 3848 N N . VAL B 1 236 ? 28.219 17.128 38.661 1.00 22.13 ? 236 VAL B N 1 ATOM 3849 C CA . VAL B 1 236 ? 27.678 16.503 37.466 1.00 21.18 ? 236 VAL B CA 1 ATOM 3850 C C . VAL B 1 236 ? 27.801 14.977 37.441 1.00 20.54 ? 236 VAL B C 1 ATOM 3851 O O . VAL B 1 236 ? 27.142 14.304 36.647 1.00 19.51 ? 236 VAL B O 1 ATOM 3852 C CB . VAL B 1 236 ? 28.367 17.128 36.203 1.00 21.42 ? 236 VAL B CB 1 ATOM 3853 C CG1 . VAL B 1 236 ? 29.842 16.774 36.182 1.00 20.78 ? 236 VAL B CG1 1 ATOM 3854 C CG2 . VAL B 1 236 ? 27.685 16.662 34.930 1.00 23.90 ? 236 VAL B CG2 1 ATOM 3855 N N . LYS B 1 237 ? 28.619 14.426 38.330 1.00 20.40 ? 237 LYS B N 1 ATOM 3856 C CA . LYS B 1 237 ? 28.841 12.986 38.355 1.00 18.72 ? 237 LYS B CA 1 ATOM 3857 C C . LYS B 1 237 ? 27.604 12.085 38.318 1.00 17.62 ? 237 LYS B C 1 ATOM 3858 O O . LYS B 1 237 ? 27.598 11.076 37.614 1.00 18.54 ? 237 LYS B O 1 ATOM 3859 C CB . LYS B 1 237 ? 29.714 12.596 39.554 1.00 19.03 ? 237 LYS B CB 1 ATOM 3860 C CG . LYS B 1 237 ? 29.982 11.099 39.616 1.00 20.43 ? 237 LYS B CG 1 ATOM 3861 C CD . LYS B 1 237 ? 30.829 10.698 40.813 1.00 23.08 ? 237 LYS B CD 1 ATOM 3862 C CE . LYS B 1 237 ? 32.283 11.063 40.609 1.00 23.16 ? 237 LYS B CE 1 ATOM 3863 N NZ . LYS B 1 237 ? 33.140 10.445 41.664 1.00 23.20 ? 237 LYS B NZ 1 ATOM 3864 N N . PRO B 1 238 ? 26.545 12.420 39.072 1.00 16.38 ? 238 PRO B N 1 ATOM 3865 C CA . PRO B 1 238 ? 25.375 11.533 39.019 1.00 15.89 ? 238 PRO B CA 1 ATOM 3866 C C . PRO B 1 238 ? 24.584 11.497 37.704 1.00 16.19 ? 238 PRO B C 1 ATOM 3867 O O . PRO B 1 238 ? 23.713 10.645 37.532 1.00 16.28 ? 238 PRO B O 1 ATOM 3868 C CB . PRO B 1 238 ? 24.532 11.995 40.210 1.00 15.11 ? 238 PRO B CB 1 ATOM 3869 C CG . PRO B 1 238 ? 24.897 13.430 40.353 1.00 17.69 ? 238 PRO B CG 1 ATOM 3870 C CD . PRO B 1 238 ? 26.390 13.440 40.121 1.00 15.85 ? 238 PRO B CD 1 ATOM 3871 N N . LYS B 1 239 ? 24.894 12.395 36.773 1.00 15.46 ? 239 LYS B N 1 ATOM 3872 C CA . LYS B 1 239 ? 24.194 12.450 35.482 1.00 16.32 ? 239 LYS B CA 1 ATOM 3873 C C . LYS B 1 239 ? 24.973 11.800 34.346 1.00 14.89 ? 239 LYS B C 1 ATOM 3874 O O . LYS B 1 239 ? 24.455 11.645 33.245 1.00 13.85 ? 239 LYS B O 1 ATOM 3875 C CB . LYS B 1 239 ? 23.935 13.906 35.079 1.00 17.71 ? 239 LYS B CB 1 ATOM 3876 C CG . LYS B 1 239 ? 23.122 14.705 36.066 1.00 20.20 ? 239 LYS B CG 1 ATOM 3877 C CD . LYS B 1 239 ? 22.937 16.140 35.613 1.00 22.70 ? 239 LYS B CD 1 ATOM 3878 C CE . LYS B 1 239 ? 22.216 16.936 36.695 1.00 25.31 ? 239 LYS B CE 1 ATOM 3879 N NZ . LYS B 1 239 ? 22.031 18.355 36.311 1.00 29.70 ? 239 LYS B NZ 1 ATOM 3880 N N . ILE B 1 240 ? 26.216 11.428 34.619 1.00 14.66 ? 240 ILE B N 1 ATOM 3881 C CA . ILE B 1 240 ? 27.094 10.857 33.606 1.00 15.09 ? 240 ILE B CA 1 ATOM 3882 C C . ILE B 1 240 ? 27.400 9.373 33.778 1.00 15.16 ? 240 ILE B C 1 ATOM 3883 O O . ILE B 1 240 ? 27.810 8.935 34.854 1.00 15.11 ? 240 ILE B O 1 ATOM 3884 C CB . ILE B 1 240 ? 28.431 11.639 33.583 1.00 15.67 ? 240 ILE B CB 1 ATOM 3885 C CG1 . ILE B 1 240 ? 28.147 13.119 33.311 1.00 15.61 ? 240 ILE B CG1 1 ATOM 3886 C CG2 . ILE B 1 240 ? 29.382 11.051 32.540 1.00 15.49 ? 240 ILE B CG2 1 ATOM 3887 C CD1 . ILE B 1 240 ? 29.381 13.992 33.284 1.00 15.39 ? 240 ILE B CD1 1 ATOM 3888 N N . ALA B 1 241 ? 27.219 8.609 32.699 1.00 14.21 ? 241 ALA B N 1 ATOM 3889 C CA . ALA B 1 241 ? 27.484 7.171 32.709 1.00 12.59 ? 241 ALA B CA 1 ATOM 3890 C C . ALA B 1 241 ? 28.840 6.823 32.071 1.00 13.32 ? 241 ALA B C 1 ATOM 3891 O O . ALA B 1 241 ? 29.488 5.851 32.477 1.00 11.67 ? 241 ALA B O 1 ATOM 3892 C CB . ALA B 1 241 ? 26.358 6.431 31.974 1.00 12.42 ? 241 ALA B CB 1 ATOM 3893 N N . LEU B 1 242 ? 29.249 7.622 31.079 1.00 13.36 ? 242 LEU B N 1 ATOM 3894 C CA . LEU B 1 242 ? 30.505 7.421 30.342 1.00 14.64 ? 242 LEU B CA 1 ATOM 3895 C C . LEU B 1 242 ? 31.228 8.729 30.037 1.00 15.00 ? 242 LEU B C 1 ATOM 3896 O O . LEU B 1 242 ? 30.599 9.733 29.710 1.00 17.55 ? 242 LEU B O 1 ATOM 3897 C CB . LEU B 1 242 ? 30.233 6.725 29.001 1.00 12.09 ? 242 LEU B CB 1 ATOM 3898 C CG . LEU B 1 242 ? 29.611 5.331 28.970 1.00 14.31 ? 242 LEU B CG 1 ATOM 3899 C CD1 . LEU B 1 242 ? 29.087 5.055 27.567 1.00 15.00 ? 242 LEU B CD1 1 ATOM 3900 C CD2 . LEU B 1 242 ? 30.637 4.280 29.382 1.00 14.30 ? 242 LEU B CD2 1 ATOM 3901 N N . LEU B 1 243 ? 32.553 8.710 30.129 1.00 16.37 ? 243 LEU B N 1 ATOM 3902 C CA . LEU B 1 243 ? 33.353 9.888 29.824 1.00 15.16 ? 243 LEU B CA 1 ATOM 3903 C C . LEU B 1 243 ? 34.117 9.668 28.538 1.00 16.50 ? 243 LEU B C 1 ATOM 3904 O O . LEU B 1 243 ? 34.651 8.588 28.291 1.00 16.89 ? 243 LEU B O 1 ATOM 3905 C CB . LEU B 1 243 ? 34.377 10.186 30.919 1.00 15.50 ? 243 LEU B CB 1 ATOM 3906 C CG . LEU B 1 243 ? 33.993 10.859 32.233 1.00 16.46 ? 243 LEU B CG 1 ATOM 3907 C CD1 . LEU B 1 243 ? 35.269 11.106 33.017 1.00 17.10 ? 243 LEU B CD1 1 ATOM 3908 C CD2 . LEU B 1 243 ? 33.266 12.164 31.990 1.00 14.86 ? 243 LEU B CD2 1 ATOM 3909 N N . LYS B 1 244 ? 34.169 10.704 27.717 1.00 18.70 ? 244 LYS B N 1 ATOM 3910 C CA . LYS B 1 244 ? 34.908 10.648 26.469 1.00 19.82 ? 244 LYS B CA 1 ATOM 3911 C C . LYS B 1 244 ? 36.365 10.955 26.840 1.00 20.79 ? 244 LYS B C 1 ATOM 3912 O O . LYS B 1 244 ? 36.624 11.664 27.813 1.00 19.38 ? 244 LYS B O 1 ATOM 3913 C CB . LYS B 1 244 ? 34.379 11.717 25.509 1.00 20.04 ? 244 LYS B CB 1 ATOM 3914 C CG . LYS B 1 244 ? 35.029 11.714 24.139 1.00 20.88 ? 244 LYS B CG 1 ATOM 3915 C CD . LYS B 1 244 ? 34.408 12.799 23.278 1.00 23.93 ? 244 LYS B CD 1 ATOM 3916 C CE . LYS B 1 244 ? 34.936 12.768 21.861 1.00 25.83 ? 244 LYS B CE 1 ATOM 3917 N NZ . LYS B 1 244 ? 34.258 13.794 21.014 1.00 28.52 ? 244 LYS B NZ 1 ATOM 3918 N N . PHE B 1 245 ? 37.316 10.409 26.092 1.00 22.45 ? 245 PHE B N 1 ATOM 3919 C CA . PHE B 1 245 ? 38.712 10.702 26.378 1.00 24.11 ? 245 PHE B CA 1 ATOM 3920 C C . PHE B 1 245 ? 39.105 11.827 25.432 1.00 25.74 ? 245 PHE B C 1 ATOM 3921 O O . PHE B 1 245 ? 39.372 11.586 24.260 1.00 26.43 ? 245 PHE B O 1 ATOM 3922 C CB . PHE B 1 245 ? 39.600 9.480 26.130 1.00 25.01 ? 245 PHE B CB 1 ATOM 3923 C CG . PHE B 1 245 ? 40.981 9.612 26.718 1.00 25.77 ? 245 PHE B CG 1 ATOM 3924 C CD1 . PHE B 1 245 ? 41.794 10.694 26.390 1.00 27.03 ? 245 PHE B CD1 1 ATOM 3925 C CD2 . PHE B 1 245 ? 41.457 8.677 27.626 1.00 26.18 ? 245 PHE B CD2 1 ATOM 3926 C CE1 . PHE B 1 245 ? 43.053 10.841 26.961 1.00 26.23 ? 245 PHE B CE1 1 ATOM 3927 C CE2 . PHE B 1 245 ? 42.714 8.819 28.200 1.00 25.33 ? 245 PHE B CE2 1 ATOM 3928 C CZ . PHE B 1 245 ? 43.510 9.901 27.867 1.00 25.48 ? 245 PHE B CZ 1 ATOM 3929 N N . VAL B 1 246 ? 39.122 13.053 25.944 1.00 27.75 ? 246 VAL B N 1 ATOM 3930 C CA . VAL B 1 246 ? 39.469 14.230 25.153 1.00 31.05 ? 246 VAL B CA 1 ATOM 3931 C C . VAL B 1 246 ? 40.874 14.728 25.526 1.00 34.34 ? 246 VAL B C 1 ATOM 3932 O O . VAL B 1 246 ? 41.171 14.930 26.701 1.00 34.35 ? 246 VAL B O 1 ATOM 3933 C CB . VAL B 1 246 ? 38.439 15.362 25.398 1.00 30.67 ? 246 VAL B CB 1 ATOM 3934 C CG1 . VAL B 1 246 ? 38.763 16.575 24.531 1.00 29.09 ? 246 VAL B CG1 1 ATOM 3935 C CG2 . VAL B 1 246 ? 37.027 14.849 25.116 1.00 29.83 ? 246 VAL B CG2 1 ATOM 3936 N N . ASP B 1 247 ? 41.731 14.930 24.526 1.00 38.46 ? 247 ASP B N 1 ATOM 3937 C CA . ASP B 1 247 ? 43.096 15.390 24.764 1.00 43.13 ? 247 ASP B CA 1 ATOM 3938 C C . ASP B 1 247 ? 43.269 16.873 25.059 1.00 45.78 ? 247 ASP B C 1 ATOM 3939 O O . ASP B 1 247 ? 43.810 17.244 26.103 1.00 46.64 ? 247 ASP B O 1 ATOM 3940 C CB . ASP B 1 247 ? 43.985 15.019 23.584 1.00 45.81 ? 247 ASP B CB 1 ATOM 3941 C CG . ASP B 1 247 ? 44.533 13.618 23.698 1.00 50.55 ? 247 ASP B CG 1 ATOM 3942 O OD1 . ASP B 1 247 ? 45.288 13.356 24.660 1.00 52.85 ? 247 ASP B OD1 1 ATOM 3943 O OD2 . ASP B 1 247 ? 44.211 12.775 22.833 1.00 54.40 ? 247 ASP B OD2 1 ATOM 3944 N N . LYS B 1 248 ? 42.824 17.721 24.142 1.00 48.48 ? 248 LYS B N 1 ATOM 3945 C CA . LYS B 1 248 ? 42.959 19.161 24.324 1.00 52.33 ? 248 LYS B CA 1 ATOM 3946 C C . LYS B 1 248 ? 41.607 19.803 24.610 1.00 53.99 ? 248 LYS B C 1 ATOM 3947 O O . LYS B 1 248 ? 40.565 19.245 24.268 1.00 54.24 ? 248 LYS B O 1 ATOM 3948 C CB . LYS B 1 248 ? 43.588 19.770 23.072 1.00 54.33 ? 248 LYS B CB 1 ATOM 3949 C CG . LYS B 1 248 ? 44.887 19.083 22.664 1.00 56.69 ? 248 LYS B CG 1 ATOM 3950 C CD . LYS B 1 248 ? 45.303 19.472 21.256 1.00 59.49 ? 248 LYS B CD 1 ATOM 3951 C CE . LYS B 1 248 ? 46.480 18.635 20.774 1.00 60.82 ? 248 LYS B CE 1 ATOM 3952 N NZ . LYS B 1 248 ? 46.836 18.958 19.357 1.00 62.59 ? 248 LYS B NZ 1 ATOM 3953 N N . ASP B 1 249 ? 41.624 20.972 25.244 1.00 56.22 ? 249 ASP B N 1 ATOM 3954 C CA . ASP B 1 249 ? 40.383 21.662 25.574 1.00 59.29 ? 249 ASP B CA 1 ATOM 3955 C C . ASP B 1 249 ? 39.516 21.797 24.329 1.00 61.13 ? 249 ASP B C 1 ATOM 3956 O O . ASP B 1 249 ? 39.908 22.431 23.350 1.00 61.77 ? 249 ASP B O 1 ATOM 3957 C CB . ASP B 1 249 ? 40.676 23.045 26.159 1.00 60.54 ? 249 ASP B CB 1 ATOM 3958 C CG . ASP B 1 249 ? 39.412 23.777 26.587 1.00 62.21 ? 249 ASP B CG 1 ATOM 3959 O OD1 . ASP B 1 249 ? 38.536 24.012 25.726 1.00 62.98 ? 249 ASP B OD1 1 ATOM 3960 O OD2 . ASP B 1 249 ? 39.294 24.119 27.784 1.00 62.97 ? 249 ASP B OD2 1 ATOM 3961 N N . PRO B 1 250 ? 38.322 21.190 24.350 1.00 63.30 ? 250 PRO B N 1 ATOM 3962 C CA . PRO B 1 250 ? 37.402 21.248 23.212 1.00 65.37 ? 250 PRO B CA 1 ATOM 3963 C C . PRO B 1 250 ? 36.638 22.568 23.095 1.00 67.58 ? 250 PRO B C 1 ATOM 3964 O O . PRO B 1 250 ? 36.348 23.226 24.097 1.00 67.50 ? 250 PRO B O 1 ATOM 3965 C CB . PRO B 1 250 ? 36.473 20.069 23.473 1.00 65.01 ? 250 PRO B CB 1 ATOM 3966 C CG . PRO B 1 250 ? 36.360 20.085 24.964 1.00 64.22 ? 250 PRO B CG 1 ATOM 3967 C CD . PRO B 1 250 ? 37.797 20.304 25.404 1.00 63.55 ? 250 PRO B CD 1 ATOM 3968 N N . LYS B 1 251 ? 36.323 22.944 21.859 1.00 70.05 ? 251 LYS B N 1 ATOM 3969 C CA . LYS B 1 251 ? 35.575 24.167 21.579 1.00 72.35 ? 251 LYS B CA 1 ATOM 3970 C C . LYS B 1 251 ? 35.347 24.340 20.082 1.00 72.55 ? 251 LYS B C 1 ATOM 3971 O O . LYS B 1 251 ? 36.237 23.907 19.321 1.00 73.33 ? 251 LYS B O 1 ATOM 3972 C CB . LYS B 1 251 ? 36.304 25.398 22.129 1.00 73.95 ? 251 LYS B CB 1 ATOM 3973 C CG . LYS B 1 251 ? 35.541 26.691 21.877 1.00 75.98 ? 251 LYS B CG 1 ATOM 3974 C CD . LYS B 1 251 ? 36.052 27.844 22.722 1.00 77.97 ? 251 LYS B CD 1 ATOM 3975 C CE . LYS B 1 251 ? 35.149 29.063 22.555 1.00 78.96 ? 251 LYS B CE 1 ATOM 3976 N NZ . LYS B 1 251 ? 35.486 30.173 23.493 1.00 79.66 ? 251 LYS B NZ 1 HETATM 3977 N N9 . ADE C 2 . ? 14.883 4.397 55.744 1.00 11.82 ? 800 ADE A N9 1 HETATM 3978 C C8 . ADE C 2 . ? 15.132 4.505 57.089 1.00 11.58 ? 800 ADE A C8 1 HETATM 3979 N N7 . ADE C 2 . ? 15.149 3.355 57.718 1.00 13.04 ? 800 ADE A N7 1 HETATM 3980 C C5 . ADE C 2 . ? 14.894 2.423 56.719 1.00 12.10 ? 800 ADE A C5 1 HETATM 3981 C C6 . ADE C 2 . ? 14.776 1.013 56.738 1.00 11.33 ? 800 ADE A C6 1 HETATM 3982 N N6 . ADE C 2 . ? 14.904 0.269 57.842 1.00 12.42 ? 800 ADE A N6 1 HETATM 3983 N N1 . ADE C 2 . ? 14.515 0.392 55.569 1.00 11.80 ? 800 ADE A N1 1 HETATM 3984 C C2 . ADE C 2 . ? 14.377 1.137 54.460 1.00 13.37 ? 800 ADE A C2 1 HETATM 3985 N N3 . ADE C 2 . ? 14.464 2.463 54.315 1.00 13.87 ? 800 ADE A N3 1 HETATM 3986 C C4 . ADE C 2 . ? 14.727 3.052 55.497 1.00 11.73 ? 800 ADE A C4 1 HETATM 3987 C C1 . NAG D 3 . ? 25.900 20.072 54.329 1.00 49.18 ? 410 NAG A C1 1 HETATM 3988 C C2 . NAG D 3 . ? 26.853 18.918 54.697 1.00 51.44 ? 410 NAG A C2 1 HETATM 3989 C C3 . NAG D 3 . ? 27.891 19.363 55.744 1.00 52.81 ? 410 NAG A C3 1 HETATM 3990 C C4 . NAG D 3 . ? 28.588 20.655 55.306 1.00 53.70 ? 410 NAG A C4 1 HETATM 3991 C C5 . NAG D 3 . ? 27.546 21.723 54.949 1.00 53.87 ? 410 NAG A C5 1 HETATM 3992 C C6 . NAG D 3 . ? 28.201 22.983 54.408 1.00 55.68 ? 410 NAG A C6 1 HETATM 3993 C C7 . NAG D 3 . ? 26.418 16.561 54.890 1.00 55.03 ? 410 NAG A C7 1 HETATM 3994 C C8 . NAG D 3 . ? 26.363 15.511 55.990 1.00 55.74 ? 410 NAG A C8 1 HETATM 3995 N N2 . NAG D 3 . ? 26.084 17.804 55.216 1.00 54.03 ? 410 NAG A N2 1 HETATM 3996 O O3 . NAG D 3 . ? 28.863 18.341 55.923 1.00 52.14 ? 410 NAG A O3 1 HETATM 3997 O O4 . NAG D 3 . ? 29.429 21.131 56.350 1.00 53.83 ? 410 NAG A O4 1 HETATM 3998 O O5 . NAG D 3 . ? 26.655 21.228 53.919 1.00 52.75 ? 410 NAG A O5 1 HETATM 3999 O O6 . NAG D 3 . ? 27.236 23.907 53.921 1.00 56.63 ? 410 NAG A O6 1 HETATM 4000 O O7 . NAG D 3 . ? 26.772 16.246 53.756 1.00 55.61 ? 410 NAG A O7 1 HETATM 4001 N N9 . ADE E 2 . ? 25.319 13.562 18.678 1.00 17.10 ? 801 ADE B N9 1 HETATM 4002 C C8 . ADE E 2 . ? 25.058 14.210 17.492 1.00 18.29 ? 801 ADE B C8 1 HETATM 4003 N N7 . ADE E 2 . ? 25.152 13.438 16.436 1.00 18.44 ? 801 ADE B N7 1 HETATM 4004 C C5 . ADE E 2 . ? 25.498 12.198 16.959 1.00 17.35 ? 801 ADE B C5 1 HETATM 4005 C C6 . ADE E 2 . ? 25.748 10.950 16.353 1.00 18.70 ? 801 ADE B C6 1 HETATM 4006 N N6 . ADE E 2 . ? 25.689 10.740 15.031 1.00 16.27 ? 801 ADE B N6 1 HETATM 4007 N N1 . ADE E 2 . ? 26.065 9.911 17.164 1.00 18.06 ? 801 ADE B N1 1 HETATM 4008 C C2 . ADE E 2 . ? 26.129 10.127 18.490 1.00 17.88 ? 801 ADE B C2 1 HETATM 4009 N N3 . ADE E 2 . ? 25.919 11.253 19.174 1.00 17.14 ? 801 ADE B N3 1 HETATM 4010 C C4 . ADE E 2 . ? 25.603 12.261 18.340 1.00 15.93 ? 801 ADE B C4 1 HETATM 4011 C C1 . NAG F 3 . ? 13.979 26.509 26.995 1.00 50.11 ? 411 NAG B C1 1 HETATM 4012 C C2 . NAG F 3 . ? 12.795 25.850 26.251 1.00 52.21 ? 411 NAG B C2 1 HETATM 4013 C C3 . NAG F 3 . ? 11.862 26.904 25.628 1.00 53.78 ? 411 NAG B C3 1 HETATM 4014 C C4 . NAG F 3 . ? 11.462 27.956 26.663 1.00 54.96 ? 411 NAG B C4 1 HETATM 4015 C C5 . NAG F 3 . ? 12.730 28.556 27.292 1.00 56.39 ? 411 NAG B C5 1 HETATM 4016 C C6 . NAG F 3 . ? 12.447 29.597 28.367 1.00 57.55 ? 411 NAG B C6 1 HETATM 4017 C C7 . NAG F 3 . ? 13.251 23.665 25.328 1.00 53.27 ? 411 NAG B C7 1 HETATM 4018 C C8 . NAG F 3 . ? 13.581 22.843 24.091 1.00 53.79 ? 411 NAG B C8 1 HETATM 4019 N N2 . NAG F 3 . ? 13.308 24.987 25.202 1.00 53.41 ? 411 NAG B N2 1 HETATM 4020 O O3 . NAG F 3 . ? 10.696 26.273 25.115 1.00 51.80 ? 411 NAG B O3 1 HETATM 4021 O O4 . NAG F 3 . ? 10.694 28.977 26.035 1.00 56.97 ? 411 NAG B O4 1 HETATM 4022 O O5 . NAG F 3 . ? 13.514 27.511 27.918 1.00 53.85 ? 411 NAG B O5 1 HETATM 4023 O O6 . NAG F 3 . ? 11.147 30.156 28.231 1.00 62.01 ? 411 NAG B O6 1 HETATM 4024 O O7 . NAG F 3 . ? 12.947 23.101 26.380 1.00 53.41 ? 411 NAG B O7 1 HETATM 4025 O O . HOH G 4 . ? 13.203 -19.172 67.185 1.00 10.78 ? 810 HOH A O 1 HETATM 4026 O O . HOH G 4 . ? 21.252 9.558 60.008 1.00 10.75 ? 812 HOH A O 1 HETATM 4027 O O . HOH G 4 . ? 4.977 -3.106 45.453 1.00 13.25 ? 813 HOH A O 1 HETATM 4028 O O . HOH G 4 . ? 17.687 3.696 69.154 1.00 16.86 ? 814 HOH A O 1 HETATM 4029 O O . HOH G 4 . ? 20.839 6.827 60.959 1.00 10.19 ? 816 HOH A O 1 HETATM 4030 O O . HOH G 4 . ? 28.763 3.266 32.056 1.00 14.65 ? 818 HOH A O 1 HETATM 4031 O O . HOH G 4 . ? 23.080 3.658 36.753 1.00 15.74 ? 819 HOH A O 1 HETATM 4032 O O . HOH G 4 . ? 23.935 -10.240 63.296 1.00 13.66 ? 820 HOH A O 1 HETATM 4033 O O . HOH G 4 . ? 26.707 2.485 65.012 1.00 12.82 ? 822 HOH A O 1 HETATM 4034 O O . HOH G 4 . ? 12.335 3.244 64.357 1.00 16.92 ? 823 HOH A O 1 HETATM 4035 O O . HOH G 4 . ? 25.794 7.040 55.234 1.00 14.72 ? 827 HOH A O 1 HETATM 4036 O O . HOH G 4 . ? 3.232 1.914 48.566 1.00 12.71 ? 828 HOH A O 1 HETATM 4037 O O . HOH G 4 . ? 33.618 -1.172 39.361 1.00 14.11 ? 829 HOH A O 1 HETATM 4038 O O . HOH G 4 . ? 7.723 4.898 32.354 1.00 13.40 ? 830 HOH A O 1 HETATM 4039 O O . HOH G 4 . ? 18.619 -14.369 66.612 1.00 11.92 ? 831 HOH A O 1 HETATM 4040 O O . HOH G 4 . ? 13.600 7.444 51.186 1.00 16.39 ? 832 HOH A O 1 HETATM 4041 O O . HOH G 4 . ? 30.565 2.295 56.551 1.00 18.64 ? 833 HOH A O 1 HETATM 4042 O O . HOH G 4 . ? 28.614 4.800 35.100 1.00 15.47 ? 835 HOH A O 1 HETATM 4043 O O . HOH G 4 . ? 28.676 -8.719 41.713 1.00 19.32 ? 837 HOH A O 1 HETATM 4044 O O . HOH G 4 . ? 13.913 7.407 59.028 1.00 13.89 ? 838 HOH A O 1 HETATM 4045 O O . HOH G 4 . ? 28.233 6.915 62.082 1.00 13.19 ? 840 HOH A O 1 HETATM 4046 O O . HOH G 4 . ? 30.869 -0.850 56.739 1.00 18.35 ? 844 HOH A O 1 HETATM 4047 O O . HOH G 4 . ? 1.643 8.259 46.519 1.00 13.30 ? 847 HOH A O 1 HETATM 4048 O O . HOH G 4 . ? 27.950 -2.270 70.794 1.00 23.84 ? 848 HOH A O 1 HETATM 4049 O O . HOH G 4 . ? 21.477 -15.806 55.823 1.00 13.82 ? 852 HOH A O 1 HETATM 4050 O O . HOH G 4 . ? 17.527 28.549 49.706 1.00 21.47 ? 853 HOH A O 1 HETATM 4051 O O . HOH G 4 . ? 14.117 6.658 54.177 1.00 20.03 ? 855 HOH A O 1 HETATM 4052 O O . HOH G 4 . ? 27.277 15.667 45.805 1.00 29.93 ? 856 HOH A O 1 HETATM 4053 O O . HOH G 4 . ? 18.903 -6.310 36.051 1.00 21.24 ? 859 HOH A O 1 HETATM 4054 O O . HOH G 4 . ? 30.496 1.257 30.915 1.00 22.60 ? 861 HOH A O 1 HETATM 4055 O O . HOH G 4 . ? 19.259 1.781 36.518 1.00 14.73 ? 862 HOH A O 1 HETATM 4056 O O . HOH G 4 . ? 34.884 0.964 48.497 1.00 16.17 ? 863 HOH A O 1 HETATM 4057 O O . HOH G 4 . ? 14.996 18.649 52.628 1.00 27.14 ? 865 HOH A O 1 HETATM 4058 O O . HOH G 4 . ? 15.673 17.005 54.694 1.00 21.68 ? 866 HOH A O 1 HETATM 4059 O O . HOH G 4 . ? 24.697 -13.574 46.995 1.00 16.87 ? 867 HOH A O 1 HETATM 4060 O O . HOH G 4 . ? 19.388 -4.636 70.322 1.00 13.18 ? 868 HOH A O 1 HETATM 4061 O O . HOH G 4 . ? 10.448 -18.799 56.213 1.00 18.54 ? 869 HOH A O 1 HETATM 4062 O O . HOH G 4 . ? 15.930 -6.059 35.835 1.00 19.39 ? 870 HOH A O 1 HETATM 4063 O O . HOH G 4 . ? 0.007 17.535 44.208 1.00 17.28 ? 872 HOH A O 1 HETATM 4064 O O . HOH G 4 . ? 7.719 -9.936 45.162 1.00 23.39 ? 873 HOH A O 1 HETATM 4065 O O . HOH G 4 . ? 14.698 -9.585 71.699 1.00 21.76 ? 877 HOH A O 1 HETATM 4066 O O . HOH G 4 . ? -0.758 9.602 35.841 1.00 23.13 ? 878 HOH A O 1 HETATM 4067 O O . HOH G 4 . ? 29.296 9.913 64.149 1.00 18.36 ? 880 HOH A O 1 HETATM 4068 O O . HOH G 4 . ? 30.592 -9.443 67.790 1.00 21.84 ? 881 HOH A O 1 HETATM 4069 O O . HOH G 4 . ? 9.637 8.978 53.352 1.00 28.84 ? 885 HOH A O 1 HETATM 4070 O O . HOH G 4 . ? 8.007 -9.825 68.962 1.00 23.87 ? 887 HOH A O 1 HETATM 4071 O O . HOH G 4 . ? 7.793 -5.967 38.313 1.00 23.59 ? 891 HOH A O 1 HETATM 4072 O O . HOH G 4 . ? 30.991 5.142 47.342 1.00 25.27 ? 892 HOH A O 1 HETATM 4073 O O . HOH G 4 . ? 8.322 12.077 53.142 1.00 23.39 ? 894 HOH A O 1 HETATM 4074 O O . HOH G 4 . ? 14.497 -19.197 57.222 1.00 25.18 ? 896 HOH A O 1 HETATM 4075 O O . HOH G 4 . ? 5.983 18.578 35.893 1.00 23.08 ? 897 HOH A O 1 HETATM 4076 O O . HOH G 4 . ? 21.935 13.117 61.891 1.00 25.06 ? 898 HOH A O 1 HETATM 4077 O O . HOH G 4 . ? 21.512 -9.627 40.965 1.00 26.37 ? 899 HOH A O 1 HETATM 4078 O O . HOH G 4 . ? 1.865 -5.314 64.871 1.00 25.28 ? 900 HOH A O 1 HETATM 4079 O O . HOH G 4 . ? 8.047 -11.664 47.279 1.00 22.97 ? 902 HOH A O 1 HETATM 4080 O O . HOH G 4 . ? 19.707 -12.589 42.038 1.00 31.15 ? 904 HOH A O 1 HETATM 4081 O O . HOH G 4 . ? 28.708 4.033 60.945 1.00 26.72 ? 905 HOH A O 1 HETATM 4082 O O . HOH G 4 . ? 28.731 7.932 65.748 1.00 19.03 ? 906 HOH A O 1 HETATM 4083 O O . HOH G 4 . ? -1.706 19.566 39.486 1.00 20.62 ? 908 HOH A O 1 HETATM 4084 O O . HOH G 4 . ? 32.534 5.182 58.089 1.00 24.55 ? 909 HOH A O 1 HETATM 4085 O O . HOH G 4 . ? 18.035 -14.148 48.079 1.00 28.46 ? 910 HOH A O 1 HETATM 4086 O O . HOH G 4 . ? 3.783 1.087 53.059 1.00 32.22 ? 914 HOH A O 1 HETATM 4087 O O . HOH G 4 . ? 13.054 -17.532 44.815 1.00 23.23 ? 917 HOH A O 1 HETATM 4088 O O . HOH G 4 . ? 25.985 -10.361 42.321 1.00 28.83 ? 918 HOH A O 1 HETATM 4089 O O . HOH G 4 . ? 30.826 -6.287 35.283 1.00 29.02 ? 920 HOH A O 1 HETATM 4090 O O . HOH G 4 . ? 0.198 0.654 43.058 1.00 27.51 ? 921 HOH A O 1 HETATM 4091 O O . HOH G 4 . ? 29.949 -1.570 59.306 1.00 29.82 ? 923 HOH A O 1 HETATM 4092 O O . HOH G 4 . ? 12.741 -5.140 71.294 1.00 23.65 ? 925 HOH A O 1 HETATM 4093 O O . HOH G 4 . ? -1.265 9.687 39.684 1.00 27.42 ? 926 HOH A O 1 HETATM 4094 O O . HOH G 4 . ? 20.556 -18.957 71.323 1.00 33.27 ? 929 HOH A O 1 HETATM 4095 O O . HOH G 4 . ? 11.463 -15.744 55.395 1.00 28.16 ? 931 HOH A O 1 HETATM 4096 O O . HOH G 4 . ? 25.656 13.086 48.224 1.00 29.92 ? 933 HOH A O 1 HETATM 4097 O O . HOH G 4 . ? -4.243 18.465 42.427 1.00 36.97 ? 934 HOH A O 1 HETATM 4098 O O . HOH G 4 . ? 18.687 -2.211 75.491 1.00 32.81 ? 936 HOH A O 1 HETATM 4099 O O . HOH G 4 . ? 17.557 -15.148 42.898 1.00 30.10 ? 938 HOH A O 1 HETATM 4100 O O . HOH G 4 . ? 18.908 11.817 60.464 1.00 32.19 ? 940 HOH A O 1 HETATM 4101 O O . HOH G 4 . ? 15.320 20.719 54.046 1.00 33.20 ? 942 HOH A O 1 HETATM 4102 O O . HOH G 4 . ? 2.532 -13.939 60.244 1.00 18.46 ? 943 HOH A O 1 HETATM 4103 O O . HOH G 4 . ? -1.760 -0.567 44.663 1.00 33.62 ? 944 HOH A O 1 HETATM 4104 O O . HOH G 4 . ? 18.333 14.563 58.014 1.00 27.82 ? 951 HOH A O 1 HETATM 4105 O O . HOH G 4 . ? 6.803 -0.620 56.250 1.00 31.19 ? 952 HOH A O 1 HETATM 4106 O O . HOH G 4 . ? 23.707 -8.273 73.284 1.00 26.93 ? 957 HOH A O 1 HETATM 4107 O O . HOH G 4 . ? -2.251 17.191 46.805 1.00 32.54 ? 958 HOH A O 1 HETATM 4108 O O . HOH G 4 . ? 11.757 7.064 64.601 1.00 30.36 ? 959 HOH A O 1 HETATM 4109 O O . HOH G 4 . ? 38.023 6.428 48.682 1.00 22.53 ? 960 HOH A O 1 HETATM 4110 O O . HOH G 4 . ? 4.972 -5.189 38.899 1.00 48.29 ? 961 HOH A O 1 HETATM 4111 O O . HOH G 4 . ? -1.281 2.918 36.533 1.00 30.04 ? 963 HOH A O 1 HETATM 4112 O O . HOH G 4 . ? 11.758 6.477 52.791 1.00 22.59 ? 964 HOH A O 1 HETATM 4113 O O . HOH G 4 . ? 13.368 8.293 56.249 1.00 28.52 ? 967 HOH A O 1 HETATM 4114 O O . HOH G 4 . ? 35.173 -5.076 43.383 1.00 29.45 ? 968 HOH A O 1 HETATM 4115 O O . HOH G 4 . ? 5.172 -9.912 45.970 1.00 28.22 ? 972 HOH A O 1 HETATM 4116 O O . HOH G 4 . ? 19.735 3.640 71.734 1.00 31.97 ? 974 HOH A O 1 HETATM 4117 O O . HOH G 4 . ? 17.741 -9.357 71.941 1.00 37.31 ? 975 HOH A O 1 HETATM 4118 O O . HOH G 4 . ? 25.100 -5.268 31.728 1.00 23.61 ? 976 HOH A O 1 HETATM 4119 O O . HOH G 4 . ? 36.516 -9.076 44.804 1.00 28.06 ? 977 HOH A O 1 HETATM 4120 O O . HOH G 4 . ? 24.175 -16.753 56.666 1.00 27.96 ? 978 HOH A O 1 HETATM 4121 O O . HOH G 4 . ? 30.021 -13.856 47.622 1.00 26.44 ? 979 HOH A O 1 HETATM 4122 O O . HOH G 4 . ? 15.752 18.050 41.522 1.00 33.87 ? 980 HOH A O 1 HETATM 4123 O O . HOH G 4 . ? 30.598 -0.496 63.672 1.00 30.55 ? 982 HOH A O 1 HETATM 4124 O O . HOH G 4 . ? 1.144 -7.264 62.876 1.00 28.08 ? 983 HOH A O 1 HETATM 4125 O O . HOH H 4 . ? 11.995 1.214 38.930 1.00 11.57 ? 811 HOH B O 1 HETATM 4126 O O . HOH H 4 . ? 7.022 0.304 30.469 1.00 10.55 ? 815 HOH B O 1 HETATM 4127 O O . HOH H 4 . ? 17.629 3.793 35.084 1.00 18.91 ? 817 HOH B O 1 HETATM 4128 O O . HOH H 4 . ? 20.374 -2.776 34.585 1.00 12.37 ? 821 HOH B O 1 HETATM 4129 O O . HOH H 4 . ? 19.422 17.631 15.040 1.00 12.00 ? 824 HOH B O 1 HETATM 4130 O O . HOH H 4 . ? 32.761 3.662 39.849 1.00 14.77 ? 825 HOH B O 1 HETATM 4131 O O . HOH H 4 . ? 11.707 4.038 37.103 1.00 16.36 ? 826 HOH B O 1 HETATM 4132 O O . HOH H 4 . ? 35.759 2.160 24.693 1.00 19.70 ? 834 HOH B O 1 HETATM 4133 O O . HOH H 4 . ? 10.291 -1.203 39.048 1.00 17.21 ? 836 HOH B O 1 HETATM 4134 O O . HOH H 4 . ? 26.680 17.603 17.006 1.00 18.87 ? 839 HOH B O 1 HETATM 4135 O O . HOH H 4 . ? 18.903 19.467 16.799 1.00 15.37 ? 841 HOH B O 1 HETATM 4136 O O . HOH H 4 . ? 21.231 2.273 34.464 1.00 13.83 ? 842 HOH B O 1 HETATM 4137 O O . HOH H 4 . ? 14.369 15.116 20.112 1.00 15.66 ? 843 HOH B O 1 HETATM 4138 O O . HOH H 4 . ? 34.122 17.259 42.769 1.00 17.62 ? 845 HOH B O 1 HETATM 4139 O O . HOH H 4 . ? 40.494 5.021 28.345 1.00 20.79 ? 846 HOH B O 1 HETATM 4140 O O . HOH H 4 . ? 23.250 18.724 6.453 1.00 21.35 ? 849 HOH B O 1 HETATM 4141 O O . HOH H 4 . ? 12.165 17.739 13.802 1.00 19.33 ? 850 HOH B O 1 HETATM 4142 O O . HOH H 4 . ? 9.632 11.048 16.743 1.00 16.75 ? 851 HOH B O 1 HETATM 4143 O O . HOH H 4 . ? 16.797 -6.997 17.766 1.00 20.05 ? 854 HOH B O 1 HETATM 4144 O O . HOH H 4 . ? 28.456 16.331 10.646 1.00 22.14 ? 857 HOH B O 1 HETATM 4145 O O . HOH H 4 . ? 17.074 3.541 5.263 1.00 13.75 ? 858 HOH B O 1 HETATM 4146 O O . HOH H 4 . ? 12.455 -5.204 25.033 1.00 18.90 ? 860 HOH B O 1 HETATM 4147 O O . HOH H 4 . ? 37.376 8.469 23.967 1.00 17.65 ? 864 HOH B O 1 HETATM 4148 O O . HOH H 4 . ? 21.767 23.808 21.284 1.00 22.84 ? 871 HOH B O 1 HETATM 4149 O O . HOH H 4 . ? 38.439 13.363 28.795 1.00 19.15 ? 874 HOH B O 1 HETATM 4150 O O . HOH H 4 . ? 45.147 19.550 35.377 1.00 22.54 ? 875 HOH B O 1 HETATM 4151 O O . HOH H 4 . ? 25.862 17.785 6.680 1.00 19.57 ? 876 HOH B O 1 HETATM 4152 O O . HOH H 4 . ? 9.455 9.478 26.195 1.00 25.03 ? 879 HOH B O 1 HETATM 4153 O O . HOH H 4 . ? 22.101 -5.201 31.646 1.00 20.71 ? 882 HOH B O 1 HETATM 4154 O O . HOH H 4 . ? 24.474 24.093 25.184 1.00 18.76 ? 883 HOH B O 1 HETATM 4155 O O . HOH H 4 . ? 33.063 -4.913 19.002 1.00 33.09 ? 884 HOH B O 1 HETATM 4156 O O . HOH H 4 . ? 11.551 14.985 13.620 1.00 21.65 ? 886 HOH B O 1 HETATM 4157 O O . HOH H 4 . ? 14.856 -6.468 23.883 1.00 21.63 ? 888 HOH B O 1 HETATM 4158 O O . HOH H 4 . ? 21.601 -8.209 23.298 1.00 29.91 ? 889 HOH B O 1 HETATM 4159 O O . HOH H 4 . ? 31.326 19.543 24.538 1.00 27.77 ? 890 HOH B O 1 HETATM 4160 O O . HOH H 4 . ? 33.393 -3.474 29.709 1.00 17.76 ? 893 HOH B O 1 HETATM 4161 O O . HOH H 4 . ? 3.547 0.727 23.958 1.00 24.10 ? 895 HOH B O 1 HETATM 4162 O O . HOH H 4 . ? 5.908 6.195 30.633 1.00 23.15 ? 901 HOH B O 1 HETATM 4163 O O . HOH H 4 . ? 25.036 24.787 27.718 1.00 24.43 ? 903 HOH B O 1 HETATM 4164 O O . HOH H 4 . ? 11.285 20.986 22.783 1.00 24.79 ? 907 HOH B O 1 HETATM 4165 O O . HOH H 4 . ? 26.119 14.929 21.114 1.00 26.53 ? 911 HOH B O 1 HETATM 4166 O O . HOH H 4 . ? 8.142 14.053 16.610 1.00 30.38 ? 912 HOH B O 1 HETATM 4167 O O . HOH H 4 . ? 33.288 -4.386 21.665 1.00 28.26 ? 913 HOH B O 1 HETATM 4168 O O . HOH H 4 . ? 29.807 -5.075 10.072 1.00 26.69 ? 915 HOH B O 1 HETATM 4169 O O . HOH H 4 . ? 32.878 -9.406 1.819 1.00 36.80 ? 916 HOH B O 1 HETATM 4170 O O . HOH H 4 . ? 5.823 6.245 23.244 1.00 24.97 ? 919 HOH B O 1 HETATM 4171 O O . HOH H 4 . ? 30.914 12.120 44.342 1.00 31.23 ? 922 HOH B O 1 HETATM 4172 O O . HOH H 4 . ? 26.732 14.208 24.032 1.00 23.09 ? 924 HOH B O 1 HETATM 4173 O O . HOH H 4 . ? 13.442 15.279 9.193 1.00 20.54 ? 927 HOH B O 1 HETATM 4174 O O . HOH H 4 . ? 22.277 11.121 0.325 1.00 23.04 ? 928 HOH B O 1 HETATM 4175 O O . HOH H 4 . ? 31.190 -6.884 7.582 1.00 22.71 ? 930 HOH B O 1 HETATM 4176 O O . HOH H 4 . ? 40.291 20.155 34.820 1.00 24.79 ? 932 HOH B O 1 HETATM 4177 O O . HOH H 4 . ? 41.587 19.872 39.948 1.00 23.36 ? 935 HOH B O 1 HETATM 4178 O O . HOH H 4 . ? 1.862 10.413 24.785 1.00 37.82 ? 937 HOH B O 1 HETATM 4179 O O . HOH H 4 . ? 22.585 1.662 0.464 1.00 19.81 ? 939 HOH B O 1 HETATM 4180 O O . HOH H 4 . ? 5.460 -1.880 24.919 1.00 33.88 ? 941 HOH B O 1 HETATM 4181 O O . HOH H 4 . ? 35.578 -3.499 21.332 1.00 30.00 ? 945 HOH B O 1 HETATM 4182 O O . HOH H 4 . ? 16.766 -5.661 26.841 1.00 27.85 ? 946 HOH B O 1 HETATM 4183 O O . HOH H 4 . ? 4.551 -4.483 22.233 1.00 29.01 ? 947 HOH B O 1 HETATM 4184 O O . HOH H 4 . ? 15.261 -6.960 30.891 1.00 27.00 ? 948 HOH B O 1 HETATM 4185 O O . HOH H 4 . ? 20.055 5.532 36.734 1.00 23.26 ? 949 HOH B O 1 HETATM 4186 O O . HOH H 4 . ? 5.288 15.775 22.125 1.00 37.46 ? 950 HOH B O 1 HETATM 4187 O O . HOH H 4 . ? 9.836 8.675 15.078 1.00 28.28 ? 953 HOH B O 1 HETATM 4188 O O . HOH H 4 . ? 43.791 10.759 31.930 1.00 27.59 ? 954 HOH B O 1 HETATM 4189 O O . HOH H 4 . ? 10.491 21.200 13.527 1.00 28.20 ? 955 HOH B O 1 HETATM 4190 O O . HOH H 4 . ? 41.670 21.306 37.056 1.00 37.64 ? 956 HOH B O 1 HETATM 4191 O O . HOH H 4 . ? 21.601 22.020 17.206 1.00 37.33 ? 962 HOH B O 1 HETATM 4192 O O . HOH H 4 . ? 34.369 1.542 39.356 1.00 36.40 ? 965 HOH B O 1 HETATM 4193 O O . HOH H 4 . ? 28.363 14.223 22.167 1.00 21.50 ? 966 HOH B O 1 HETATM 4194 O O . HOH H 4 . ? 26.959 17.336 20.076 1.00 29.04 ? 969 HOH B O 1 HETATM 4195 O O . HOH H 4 . ? 21.751 18.490 4.143 1.00 25.77 ? 970 HOH B O 1 HETATM 4196 O O . HOH H 4 . ? 24.362 21.284 6.764 1.00 28.03 ? 971 HOH B O 1 HETATM 4197 O O . HOH H 4 . ? 27.876 6.031 -2.119 1.00 33.12 ? 973 HOH B O 1 HETATM 4198 O O . HOH H 4 . ? 23.821 27.586 28.134 1.00 32.69 ? 981 HOH B O 1 HETATM 4199 O O . HOH H 4 . ? 2.742 7.358 22.913 1.00 33.98 ? 984 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 ADE 1 800 800 ADE ADE A . D 3 NAG 1 410 410 NAG NAG A . E 2 ADE 1 801 801 ADE ADE B . F 3 NAG 1 411 411 NAG NAG B . G 4 HOH 1 810 810 HOH TIP A . G 4 HOH 2 812 812 HOH TIP A . G 4 HOH 3 813 813 HOH TIP A . G 4 HOH 4 814 814 HOH TIP A . G 4 HOH 5 816 816 HOH TIP A . G 4 HOH 6 818 818 HOH TIP A . G 4 HOH 7 819 819 HOH TIP A . G 4 HOH 8 820 820 HOH TIP A . G 4 HOH 9 822 822 HOH TIP A . G 4 HOH 10 823 823 HOH TIP A . G 4 HOH 11 827 827 HOH TIP A . G 4 HOH 12 828 828 HOH TIP A . G 4 HOH 13 829 829 HOH TIP A . G 4 HOH 14 830 830 HOH TIP A . G 4 HOH 15 831 831 HOH TIP A . G 4 HOH 16 832 832 HOH TIP A . G 4 HOH 17 833 833 HOH TIP A . G 4 HOH 18 835 835 HOH TIP A . G 4 HOH 19 837 837 HOH TIP A . G 4 HOH 20 838 838 HOH TIP A . G 4 HOH 21 840 840 HOH TIP A . G 4 HOH 22 844 844 HOH TIP A . G 4 HOH 23 847 847 HOH TIP A . G 4 HOH 24 848 848 HOH TIP A . G 4 HOH 25 852 852 HOH TIP A . G 4 HOH 26 853 853 HOH TIP A . G 4 HOH 27 855 855 HOH TIP A . G 4 HOH 28 856 856 HOH TIP A . G 4 HOH 29 859 859 HOH TIP A . G 4 HOH 30 861 861 HOH TIP A . G 4 HOH 31 862 862 HOH TIP A . G 4 HOH 32 863 863 HOH TIP A . G 4 HOH 33 865 865 HOH TIP A . G 4 HOH 34 866 866 HOH TIP A . G 4 HOH 35 867 867 HOH TIP A . G 4 HOH 36 868 868 HOH TIP A . G 4 HOH 37 869 869 HOH TIP A . G 4 HOH 38 870 870 HOH TIP A . G 4 HOH 39 872 872 HOH TIP A . G 4 HOH 40 873 873 HOH TIP A . G 4 HOH 41 877 877 HOH TIP A . G 4 HOH 42 878 878 HOH TIP A . G 4 HOH 43 880 880 HOH TIP A . G 4 HOH 44 881 881 HOH TIP A . G 4 HOH 45 885 885 HOH TIP A . G 4 HOH 46 887 887 HOH TIP A . G 4 HOH 47 891 891 HOH TIP A . G 4 HOH 48 892 892 HOH TIP A . G 4 HOH 49 894 894 HOH TIP A . G 4 HOH 50 896 896 HOH TIP A . G 4 HOH 51 897 897 HOH TIP A . G 4 HOH 52 898 898 HOH TIP A . G 4 HOH 53 899 899 HOH TIP A . G 4 HOH 54 900 900 HOH TIP A . G 4 HOH 55 902 902 HOH TIP A . G 4 HOH 56 904 904 HOH TIP A . G 4 HOH 57 905 905 HOH TIP A . G 4 HOH 58 906 906 HOH TIP A . G 4 HOH 59 908 908 HOH TIP A . G 4 HOH 60 909 909 HOH TIP A . G 4 HOH 61 910 910 HOH TIP A . G 4 HOH 62 914 914 HOH TIP A . G 4 HOH 63 917 917 HOH TIP A . G 4 HOH 64 918 918 HOH TIP A . G 4 HOH 65 920 920 HOH TIP A . G 4 HOH 66 921 921 HOH TIP A . G 4 HOH 67 923 923 HOH TIP A . G 4 HOH 68 925 925 HOH TIP A . G 4 HOH 69 926 926 HOH TIP A . G 4 HOH 70 929 929 HOH TIP A . G 4 HOH 71 931 931 HOH TIP A . G 4 HOH 72 933 933 HOH TIP A . G 4 HOH 73 934 934 HOH TIP A . G 4 HOH 74 936 936 HOH TIP A . G 4 HOH 75 938 938 HOH TIP A . G 4 HOH 76 940 940 HOH TIP A . G 4 HOH 77 942 942 HOH TIP A . G 4 HOH 78 943 943 HOH TIP A . G 4 HOH 79 944 944 HOH TIP A . G 4 HOH 80 951 951 HOH TIP A . G 4 HOH 81 952 952 HOH TIP A . G 4 HOH 82 957 957 HOH TIP A . G 4 HOH 83 958 958 HOH TIP A . G 4 HOH 84 959 959 HOH TIP A . G 4 HOH 85 960 960 HOH TIP A . G 4 HOH 86 961 961 HOH TIP A . G 4 HOH 87 963 963 HOH TIP A . G 4 HOH 88 964 964 HOH TIP A . G 4 HOH 89 967 967 HOH TIP A . G 4 HOH 90 968 968 HOH TIP A . G 4 HOH 91 972 972 HOH TIP A . G 4 HOH 92 974 974 HOH TIP A . G 4 HOH 93 975 975 HOH TIP A . G 4 HOH 94 976 976 HOH TIP A . G 4 HOH 95 977 977 HOH TIP A . G 4 HOH 96 978 978 HOH TIP A . G 4 HOH 97 979 979 HOH TIP A . G 4 HOH 98 980 980 HOH TIP A . G 4 HOH 99 982 982 HOH TIP A . G 4 HOH 100 983 983 HOH TIP A . H 4 HOH 1 811 811 HOH TIP B . H 4 HOH 2 815 815 HOH TIP B . H 4 HOH 3 817 817 HOH TIP B . H 4 HOH 4 821 821 HOH TIP B . H 4 HOH 5 824 824 HOH TIP B . H 4 HOH 6 825 825 HOH TIP B . H 4 HOH 7 826 826 HOH TIP B . H 4 HOH 8 834 834 HOH TIP B . H 4 HOH 9 836 836 HOH TIP B . H 4 HOH 10 839 839 HOH TIP B . H 4 HOH 11 841 841 HOH TIP B . H 4 HOH 12 842 842 HOH TIP B . H 4 HOH 13 843 843 HOH TIP B . H 4 HOH 14 845 845 HOH TIP B . H 4 HOH 15 846 846 HOH TIP B . H 4 HOH 16 849 849 HOH TIP B . H 4 HOH 17 850 850 HOH TIP B . H 4 HOH 18 851 851 HOH TIP B . H 4 HOH 19 854 854 HOH TIP B . H 4 HOH 20 857 857 HOH TIP B . H 4 HOH 21 858 858 HOH TIP B . H 4 HOH 22 860 860 HOH TIP B . H 4 HOH 23 864 864 HOH TIP B . H 4 HOH 24 871 871 HOH TIP B . H 4 HOH 25 874 874 HOH TIP B . H 4 HOH 26 875 875 HOH TIP B . H 4 HOH 27 876 876 HOH TIP B . H 4 HOH 28 879 879 HOH TIP B . H 4 HOH 29 882 882 HOH TIP B . H 4 HOH 30 883 883 HOH TIP B . H 4 HOH 31 884 884 HOH TIP B . H 4 HOH 32 886 886 HOH TIP B . H 4 HOH 33 888 888 HOH TIP B . H 4 HOH 34 889 889 HOH TIP B . H 4 HOH 35 890 890 HOH TIP B . H 4 HOH 36 893 893 HOH TIP B . H 4 HOH 37 895 895 HOH TIP B . H 4 HOH 38 901 901 HOH TIP B . H 4 HOH 39 903 903 HOH TIP B . H 4 HOH 40 907 907 HOH TIP B . H 4 HOH 41 911 911 HOH TIP B . H 4 HOH 42 912 912 HOH TIP B . H 4 HOH 43 913 913 HOH TIP B . H 4 HOH 44 915 915 HOH TIP B . H 4 HOH 45 916 916 HOH TIP B . H 4 HOH 46 919 919 HOH TIP B . H 4 HOH 47 922 922 HOH TIP B . H 4 HOH 48 924 924 HOH TIP B . H 4 HOH 49 927 927 HOH TIP B . H 4 HOH 50 928 928 HOH TIP B . H 4 HOH 51 930 930 HOH TIP B . H 4 HOH 52 932 932 HOH TIP B . H 4 HOH 53 935 935 HOH TIP B . H 4 HOH 54 937 937 HOH TIP B . H 4 HOH 55 939 939 HOH TIP B . H 4 HOH 56 941 941 HOH TIP B . H 4 HOH 57 945 945 HOH TIP B . H 4 HOH 58 946 946 HOH TIP B . H 4 HOH 59 947 947 HOH TIP B . H 4 HOH 60 948 948 HOH TIP B . H 4 HOH 61 949 949 HOH TIP B . H 4 HOH 62 950 950 HOH TIP B . H 4 HOH 63 953 953 HOH TIP B . H 4 HOH 64 954 954 HOH TIP B . H 4 HOH 65 955 955 HOH TIP B . H 4 HOH 66 956 956 HOH TIP B . H 4 HOH 67 962 962 HOH TIP B . H 4 HOH 68 965 965 HOH TIP B . H 4 HOH 69 966 966 HOH TIP B . H 4 HOH 70 969 969 HOH TIP B . H 4 HOH 71 970 970 HOH TIP B . H 4 HOH 72 971 971 HOH TIP B . H 4 HOH 73 973 973 HOH TIP B . H 4 HOH 74 981 981 HOH TIP B . H 4 HOH 75 984 984 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 software_defined_assembly PISA monomeric 1 2 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,D,G 2 1 B,E,F,H # _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 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Version format compliance' # 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 HKL-2000 . ? ? ? ? 'data collection' ? ? ? 4 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 5 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? 6 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 ? ? -174.19 88.31 2 1 LYS A 49 ? ? -155.82 23.79 3 1 ARG A 81 ? ? 56.37 -126.66 4 1 ASN A 180 ? ? -142.16 15.58 5 1 ASP A 247 ? ? -72.67 -70.99 6 1 CYS B 44 ? ? 175.98 88.15 7 1 LYS B 49 ? ? -162.09 26.36 8 1 ARG B 81 ? ? 60.25 -129.16 9 1 ASN B 147 ? ? -94.37 59.01 10 1 ASN B 180 ? ? -141.12 19.16 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ADENINE ADE 3 N-ACETYL-D-GLUCOSAMINE NAG 4 water HOH #