data_4Q7Z # _entry.id 4Q7Z # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4Q7Z RCSB RCSB085718 WWPDB D_1000085718 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4Q7X . unspecified PDB 4Q7Y . unspecified PDB 4Q80 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4Q7Z _pdbx_database_status.recvd_initial_deposition_date 2014-04-25 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Eigenbrot, C.' 1 'Lin, S.J.' 2 'Dong, K.C.' 3 # _citation.id primary _citation.title 'Structures of neutrophil serine protease 4 reveal an unusual mechanism of substrate recognition by a trypsin-fold protease.' _citation.journal_abbrev Structure _citation.journal_volume 22 _citation.page_first 1333 _citation.page_last 1340 _citation.year 2014 _citation.journal_id_ASTM STRUE6 _citation.country UK _citation.journal_id_ISSN 0969-2126 _citation.journal_id_CSD 2005 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 25156428 _citation.pdbx_database_id_DOI 10.1016/j.str.2014.07.008 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lin, S.J.' 1 primary 'Dong, K.C.' 2 primary 'Eigenbrot, C.' 3 primary 'van Lookeren Campagne, M.' 4 primary 'Kirchhofer, D.' 5 # _cell.entry_id 4Q7Z _cell.length_a 54.986 _cell.length_b 64.466 _cell.length_c 68.383 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4Q7Z _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _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 man 'Serine protease 57' 27002.900 1 3.4.21.- ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 4 non-polymer syn 'L-phenylalanyl-N-[(2S,3S)-6-carbamimidamido-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide' 503.037 1 ? ? ? ? 5 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 6 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 7 water nat water 18.015 246 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Serine protease 1-like protein 1' # _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 ;IIGGHEVTPHSRPYMASVRFGGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHPD YHPMTHANDICLLRLNGSAVLGPAVGLLRLPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSWK GHLTLTMLCTRSGDSHRRGFCSADSGGPLVCRNRAHGLVSFSGLWCGDPKTPDVYTQVSAFVAWIWDVVRRSSPQPGPLP GTTRPPGEAA ; _entity_poly.pdbx_seq_one_letter_code_can ;IIGGHEVTPHSRPYMASVRFGGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHPD YHPMTHANDICLLRLNGSAVLGPAVGLLRLPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSWK GHLTLTMLCTRSGDSHRRGFCSADSGGPLVCRNRAHGLVSFSGLWCGDPKTPDVYTQVSAFVAWIWDVVRRSSPQPGPLP GTTRPPGEAA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ILE n 1 2 ILE n 1 3 GLY n 1 4 GLY n 1 5 HIS n 1 6 GLU n 1 7 VAL n 1 8 THR n 1 9 PRO n 1 10 HIS n 1 11 SER n 1 12 ARG n 1 13 PRO n 1 14 TYR n 1 15 MET n 1 16 ALA n 1 17 SER n 1 18 VAL n 1 19 ARG n 1 20 PHE n 1 21 GLY n 1 22 GLY n 1 23 GLN n 1 24 HIS n 1 25 HIS n 1 26 CYS n 1 27 GLY n 1 28 GLY n 1 29 PHE n 1 30 LEU n 1 31 LEU n 1 32 ARG n 1 33 ALA n 1 34 ARG n 1 35 TRP n 1 36 VAL n 1 37 VAL n 1 38 SER n 1 39 ALA n 1 40 ALA n 1 41 HIS n 1 42 CYS n 1 43 PHE n 1 44 SER n 1 45 HIS n 1 46 ARG n 1 47 ASP n 1 48 LEU n 1 49 ARG n 1 50 THR n 1 51 GLY n 1 52 LEU n 1 53 VAL n 1 54 VAL n 1 55 LEU n 1 56 GLY n 1 57 ALA n 1 58 HIS n 1 59 VAL n 1 60 LEU n 1 61 SER n 1 62 THR n 1 63 ALA n 1 64 GLU n 1 65 PRO n 1 66 THR n 1 67 GLN n 1 68 GLN n 1 69 VAL n 1 70 PHE n 1 71 GLY n 1 72 ILE n 1 73 ASP n 1 74 ALA n 1 75 LEU n 1 76 THR n 1 77 THR n 1 78 HIS n 1 79 PRO n 1 80 ASP n 1 81 TYR n 1 82 HIS n 1 83 PRO n 1 84 MET n 1 85 THR n 1 86 HIS n 1 87 ALA n 1 88 ASN n 1 89 ASP n 1 90 ILE n 1 91 CYS n 1 92 LEU n 1 93 LEU n 1 94 ARG n 1 95 LEU n 1 96 ASN n 1 97 GLY n 1 98 SER n 1 99 ALA n 1 100 VAL n 1 101 LEU n 1 102 GLY n 1 103 PRO n 1 104 ALA n 1 105 VAL n 1 106 GLY n 1 107 LEU n 1 108 LEU n 1 109 ARG n 1 110 LEU n 1 111 PRO n 1 112 GLY n 1 113 ARG n 1 114 ARG n 1 115 ALA n 1 116 ARG n 1 117 PRO n 1 118 PRO n 1 119 THR n 1 120 ALA n 1 121 GLY n 1 122 THR n 1 123 ARG n 1 124 CYS n 1 125 ARG n 1 126 VAL n 1 127 ALA n 1 128 GLY n 1 129 TRP n 1 130 GLY n 1 131 PHE n 1 132 VAL n 1 133 SER n 1 134 ASP n 1 135 PHE n 1 136 GLU n 1 137 GLU n 1 138 LEU n 1 139 PRO n 1 140 PRO n 1 141 GLY n 1 142 LEU n 1 143 MET n 1 144 GLU n 1 145 ALA n 1 146 LYS n 1 147 VAL n 1 148 ARG n 1 149 VAL n 1 150 LEU n 1 151 ASP n 1 152 PRO n 1 153 ASP n 1 154 VAL n 1 155 CYS n 1 156 ASN n 1 157 SER n 1 158 SER n 1 159 TRP n 1 160 LYS n 1 161 GLY n 1 162 HIS n 1 163 LEU n 1 164 THR n 1 165 LEU n 1 166 THR n 1 167 MET n 1 168 LEU n 1 169 CYS n 1 170 THR n 1 171 ARG n 1 172 SER n 1 173 GLY n 1 174 ASP n 1 175 SER n 1 176 HIS n 1 177 ARG n 1 178 ARG n 1 179 GLY n 1 180 PHE n 1 181 CYS n 1 182 SER n 1 183 ALA n 1 184 ASP n 1 185 SER n 1 186 GLY n 1 187 GLY n 1 188 PRO n 1 189 LEU n 1 190 VAL n 1 191 CYS n 1 192 ARG n 1 193 ASN n 1 194 ARG n 1 195 ALA n 1 196 HIS n 1 197 GLY n 1 198 LEU n 1 199 VAL n 1 200 SER n 1 201 PHE n 1 202 SER n 1 203 GLY n 1 204 LEU n 1 205 TRP n 1 206 CYS n 1 207 GLY n 1 208 ASP n 1 209 PRO n 1 210 LYS n 1 211 THR n 1 212 PRO n 1 213 ASP n 1 214 VAL n 1 215 TYR n 1 216 THR n 1 217 GLN n 1 218 VAL n 1 219 SER n 1 220 ALA n 1 221 PHE n 1 222 VAL n 1 223 ALA n 1 224 TRP n 1 225 ILE n 1 226 TRP n 1 227 ASP n 1 228 VAL n 1 229 VAL n 1 230 ARG n 1 231 ARG n 1 232 SER n 1 233 SER n 1 234 PRO n 1 235 GLN n 1 236 PRO n 1 237 GLY n 1 238 PRO n 1 239 LEU n 1 240 PRO n 1 241 GLY n 1 242 THR n 1 243 THR n 1 244 ARG n 1 245 PRO n 1 246 PRO n 1 247 GLY n 1 248 GLU n 1 249 ALA n 1 250 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'PRSS57, PRSSL1, UNQ782/PRO1599' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PRS57_HUMAN _struct_ref.pdbx_db_accession Q6UWY2 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;IIGGHEVTPHSRPYMASVRFGGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHPD YHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSWK GHLTLTMLCTRSGDSHRRGFCSADSGGPLVCRNRAHGLVSFSGLWCGDPKTPDVYTQVSAFVAWIWDVVRRSSPQPGPLP GTTRPPGEAA ; _struct_ref.pdbx_align_begin 34 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4Q7Z _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 250 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q6UWY2 _struct_ref_seq.db_align_beg 34 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 283 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 16 _struct_ref_seq.pdbx_auth_seq_align_end 263 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 4Q7Z _struct_ref_seq_dif.mon_id LEU _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 110 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q6UWY2 _struct_ref_seq_dif.db_mon_id PRO _struct_ref_seq_dif.pdbx_seq_db_seq_num 143 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 123 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 2YT peptide-like . 'L-phenylalanyl-N-[(2S,3S)-6-carbamimidamido-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide' PHE-PHE-ARG-chloromethylketone 'C25 H35 Cl N6 O3' 503.037 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 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4Q7Z _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.24 _exptl_crystal.density_percent_sol 45.19 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 292 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.5 _exptl_crystal_grow.pdbx_details '20% PEG-MME 2000, 0.1 M Tris 8.5, 0.2 M trimethylamine N-oxide, VAPOR DIFFUSION, SITTING DROP, temperature 292K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 110 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.pdbx_collection_date 2012-07-05 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.127092 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRL BEAMLINE BL7-1' _diffrn_source.pdbx_synchrotron_site SSRL _diffrn_source.pdbx_synchrotron_beamline BL7-1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.127092 # _reflns.entry_id 4Q7Z _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 46.92 _reflns.d_resolution_high 1.4 _reflns.number_obs 45530 _reflns.number_all 45664 _reflns.percent_possible_obs 93.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.048 _reflns.pdbx_netI_over_sigmaI 34.3 _reflns.B_iso_Wilson_estimate 18 _reflns.pdbx_redundancy 7.0 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.entry_id 4Q7Z _refine.ls_number_reflns_obs 43254 _refine.ls_number_reflns_all 45530 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 46.91 _refine.ls_d_res_high 1.40 _refine.ls_percent_reflns_obs 93.72 _refine.ls_R_factor_obs 0.19352 _refine.ls_R_factor_all 0.21 _refine.ls_R_factor_R_work 0.19244 _refine.ls_R_factor_R_free 0.21472 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 2276 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.963 _refine.correlation_coeff_Fo_to_Fc_free 0.957 _refine.B_iso_mean 19.684 _refine.aniso_B[1][1] 0.38 _refine.aniso_B[2][2] -0.08 _refine.aniso_B[3][3] -0.30 _refine.aniso_B[1][2] -0.00 _refine.aniso_B[1][3] -0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 1HNE _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.069 _refine.pdbx_overall_ESU_R_Free 0.069 _refine.overall_SU_ML 0.043 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.081 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 4Q7Z _refine_analyze.Luzzati_coordinate_error_obs 0.069 _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_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 1781 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 79 _refine_hist.number_atoms_solvent 246 _refine_hist.number_atoms_total 2106 _refine_hist.d_res_high 1.40 _refine_hist.d_res_low 46.91 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.008 0.019 ? 1954 ? 'X-RAY DIFFRACTION' r_bond_other_d 0.001 0.020 ? 1330 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.304 1.975 ? 2664 ? 'X-RAY DIFFRACTION' r_angle_other_deg 0.868 3.005 ? 3170 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.800 5.000 ? 240 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 25.056 20.370 ? 81 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 12.696 15.000 ? 280 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 16.136 15.000 ? 23 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.074 0.200 ? 294 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.006 0.021 ? 2169 ? 'X-RAY DIFFRACTION' r_gen_planes_other 0.001 0.020 ? 437 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_total_number_of_bins_used 10 _refine_ls_shell.d_res_high 1.400 _refine_ls_shell.d_res_low 1.476 _refine_ls_shell.number_reflns_R_work 6072 _refine_ls_shell.R_factor_R_work 0.323 _refine_ls_shell.percent_reflns_obs 97.53 _refine_ls_shell.R_factor_R_free 0.365 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 334 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 4Q7Z _struct.title 'Neutrophil serine protease 4 (PRSS57) with phe-phe-arg-chloromethylketone (FFR-cmk)' _struct.pdbx_descriptor 'Serine protease 57 (E.C.3.4.21.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4Q7Z _struct_keywords.pdbx_keywords 'HYDROLASE/HYDROLASE INHIBITOR' _struct_keywords.text 'trypsin homology, peptidase, HYDROLASE-HYDROLASE INHIBITOR complex' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 6 ? H N N 7 ? # _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 ALA A 39 ? SER A 44 ? ALA A 55 SER A 60 5 ? 6 HELX_P HELX_P2 2 ASP A 47 A ARG A 49 C ASP A 62 ARG A 62 5 ? 3 HELX_P HELX_P3 3 ASP A 151 ? TRP A 159 ? ASP A 164 TRP A 172 1 ? 9 HELX_P HELX_P4 4 PHE A 221 ? SER A 232 ? PHE A 234 SER A 245 1 ? 12 # _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 26 SG ? ? ? 1_555 A CYS 42 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? A CYS 124 SG ? ? ? 1_555 A CYS 191 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.029 ? disulf3 disulf ? ? A CYS 155 SG ? ? ? 1_555 A CYS 169 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.005 ? disulf4 disulf ? ? A CYS 181 SG ? ? ? 1_555 A CYS 206 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.070 ? covale1 covale ? ? A ASN 156 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 169 A NAG 302 1_555 ? ? ? ? ? ? ? 1.427 ? covale2 covale ? ? C NAG . O6 ? ? ? 1_555 D FUC . C1 ? ? A NAG 302 A FUC 303 1_555 ? ? ? ? ? ? ? 1.444 ? covale3 covale ? ? A ASN 96 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 109 A NAG 301 1_555 ? ? ? ? ? ? ? 1.448 ? covale4 covale ? ? A SER 185 OG ? ? ? 1_555 E 2YT . C30 ? ? A SER 195 A 2YT 304 1_555 ? ? ? ? ? ? ? 1.410 ? covale5 covale ? ? A HIS 41 NE2 ? ? ? 1_555 E 2YT . C32 ? ? A HIS 57 A 2YT 304 1_555 ? ? ? ? ? ? ? 1.514 ? # 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 ? 8 ? B ? 7 ? # 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 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? 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 HIS A 5 ? GLU A 6 ? HIS A 20 GLU A 21 A 2 MET A 143 ? LEU A 150 ? MET A 156 LEU A 163 A 3 MET A 167 ? ARG A 171 ? MET A 180 ARG A 184 A 4 VAL A 214 ? GLN A 217 ? VAL A 227 GLN A 230 A 5 ARG A 194 ? PHE A 201 ? ARG A 208 PHE A 215 A 6 PRO A 188 ? CYS A 191 ? PRO A 198 CYS A 201 A 7 ARG A 123 ? GLY A 128 ? ARG A 135 GLY A 140 A 8 MET A 143 ? LEU A 150 ? MET A 156 LEU A 163 B 1 GLN A 68 ? PHE A 70 ? GLN A 81 PHE A 83 B 2 GLY A 51 ? LEU A 55 ? GLY A 64 LEU A 68 B 3 MET A 15 ? PHE A 20 ? MET A 30 PHE A 35 B 4 GLN A 23 ? ARG A 32 ? GLN A 39 ARG A 48 B 5 TRP A 35 ? SER A 38 ? TRP A 51 SER A 54 B 6 CYS A 91 ? LEU A 95 ? CYS A 104 LEU A 108 B 7 ILE A 72 ? THR A 77 ? ILE A 85 THR A 90 # 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 HIS A 5 ? N HIS A 20 O GLU A 144 ? O GLU A 157 A 2 3 N ARG A 148 ? N ARG A 161 O ARG A 171 ? O ARG A 184 A 3 4 N LEU A 168 ? N LEU A 181 O TYR A 215 ? O TYR A 228 A 4 5 O VAL A 214 ? O VAL A 227 N PHE A 201 ? N PHE A 215 A 5 6 O GLY A 197 ? O GLY A 211 N LEU A 189 ? N LEU A 199 A 6 7 O VAL A 190 ? O VAL A 200 N ARG A 125 ? N ARG A 137 A 7 8 N CYS A 124 ? N CYS A 136 O VAL A 147 ? O VAL A 160 B 1 2 O GLN A 68 ? O GLN A 81 N LEU A 55 ? N LEU A 68 B 2 3 O VAL A 54 ? O VAL A 67 N SER A 17 ? N SER A 32 B 3 4 N VAL A 18 ? N VAL A 33 O CYS A 26 ? O CYS A 42 B 4 5 N LEU A 31 ? N LEU A 47 O TRP A 35 ? O TRP A 51 B 5 6 N VAL A 36 ? N VAL A 52 O LEU A 93 ? O LEU A 106 B 6 7 O ARG A 94 ? O ARG A 107 N ALA A 74 ? N ALA A 87 # 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 302' AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE FUC A 303' AC4 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE 2YT A 304' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 305' AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CL A 306' # 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 3 GLY A 71 ? GLY A 84 . ? 1_555 ? 2 AC1 3 ASN A 96 ? ASN A 109 . ? 1_555 ? 3 AC1 3 HOH H . ? HOH A 628 . ? 1_555 ? 4 AC2 7 ASN A 156 ? ASN A 169 . ? 1_555 ? 5 AC2 7 GLY A 161 ? GLY A 174 . ? 1_555 ? 6 AC2 7 LEU A 163 ? LEU A 176 . ? 1_555 ? 7 AC2 7 THR A 164 ? THR A 177 . ? 1_555 ? 8 AC2 7 FUC D . ? FUC A 303 . ? 1_555 ? 9 AC2 7 HOH H . ? HOH A 603 . ? 1_555 ? 10 AC2 7 HOH H . ? HOH A 642 . ? 1_555 ? 11 AC3 10 PHE A 43 ? PHE A 59 . ? 4_445 ? 12 AC3 10 SER A 44 ? SER A 60 . ? 4_445 ? 13 AC3 10 HIS A 45 ? HIS A 61 . ? 4_445 ? 14 AC3 10 ARG A 46 ? ARG A 62 . ? 4_445 ? 15 AC3 10 LYS A 160 ? LYS A 173 . ? 1_555 ? 16 AC3 10 NAG C . ? NAG A 302 . ? 1_555 ? 17 AC3 10 HOH H . ? HOH A 464 . ? 4_445 ? 18 AC3 10 HOH H . ? HOH A 511 . ? 1_555 ? 19 AC3 10 HOH H . ? HOH A 565 . ? 4_445 ? 20 AC3 10 HOH H . ? HOH A 642 . ? 1_555 ? 21 AC4 18 HIS A 41 ? HIS A 57 . ? 1_555 ? 22 AC4 18 TYR A 81 ? TYR A 94 . ? 1_555 ? 23 AC4 18 HIS A 86 ? HIS A 99 . ? 1_555 ? 24 AC4 18 ASP A 89 ? ASP A 102 . ? 1_555 ? 25 AC4 18 PHE A 180 ? PHE A 190 . ? 1_555 ? 26 AC4 18 CYS A 181 ? CYS A 191 . ? 1_555 ? 27 AC4 18 SER A 182 ? SER A 192 . ? 1_555 ? 28 AC4 18 ALA A 183 ? ALA A 193 . ? 1_555 ? 29 AC4 18 SER A 185 ? SER A 195 . ? 1_555 ? 30 AC4 18 SER A 200 ? SER A 214 . ? 1_555 ? 31 AC4 18 PHE A 201 ? PHE A 215 . ? 1_555 ? 32 AC4 18 SER A 202 ? SER A 216 . ? 1_555 ? 33 AC4 18 GLY A 203 ? GLY A 217 . ? 1_555 ? 34 AC4 18 CYS A 206 ? CYS A 220 . ? 1_555 ? 35 AC4 18 HOH H . ? HOH A 580 . ? 1_555 ? 36 AC4 18 HOH H . ? HOH A 582 . ? 1_555 ? 37 AC4 18 HOH H . ? HOH A 591 . ? 1_555 ? 38 AC4 18 HOH H . ? HOH A 635 . ? 1_555 ? 39 AC5 6 HIS A 78 ? HIS A 91 . ? 1_555 ? 40 AC5 6 ASP A 80 ? ASP A 93 . ? 1_555 ? 41 AC5 6 ASN A 88 ? ASN A 101 . ? 1_555 ? 42 AC5 6 ALA A 220 ? ALA A 233 . ? 1_555 ? 43 AC5 6 PHE A 221 ? PHE A 234 . ? 1_555 ? 44 AC5 6 HOH H . ? HOH A 450 . ? 1_555 ? 45 AC6 7 ARG A 32 ? ARG A 48 . ? 1_555 ? 46 AC6 7 ALA A 33 ? ALA A 49 . ? 1_555 ? 47 AC6 7 ARG A 34 ? ARG A 50 . ? 1_555 ? 48 AC6 7 TRP A 205 ? TRP A 219 . ? 2_455 ? 49 AC6 7 HOH H . ? HOH A 500 . ? 1_555 ? 50 AC6 7 HOH H . ? HOH A 530 . ? 1_555 ? 51 AC6 7 HOH H . ? HOH A 585 . ? 1_555 ? # _database_PDB_matrix.entry_id 4Q7Z _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4Q7Z _atom_sites.fract_transf_matrix[1][1] 0.018186 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.015512 _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] 0.014624 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CL 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 . ILE A 1 1 ? -22.150 4.730 3.921 1.00 11.94 ? 16 ILE A N 1 ATOM 2 C CA . ILE A 1 1 ? -23.248 4.263 4.807 1.00 12.09 ? 16 ILE A CA 1 ATOM 3 C C . ILE A 1 1 ? -24.580 4.484 4.111 1.00 13.23 ? 16 ILE A C 1 ATOM 4 O O . ILE A 1 1 ? -24.813 5.557 3.563 1.00 14.01 ? 16 ILE A O 1 ATOM 5 C CB . ILE A 1 1 ? -23.217 5.040 6.138 1.00 12.70 ? 16 ILE A CB 1 ATOM 6 C CG1 . ILE A 1 1 ? -21.908 4.780 6.901 1.00 13.15 ? 16 ILE A CG1 1 ATOM 7 C CG2 . ILE A 1 1 ? -24.445 4.713 6.985 1.00 14.66 ? 16 ILE A CG2 1 ATOM 8 C CD1 . ILE A 1 1 ? -21.736 3.398 7.475 1.00 12.77 ? 16 ILE A CD1 1 ATOM 9 N N . ILE A 1 2 ? -25.450 3.475 4.174 1.00 14.78 ? 17 ILE A N 1 ATOM 10 C CA . ILE A 1 2 ? -26.792 3.512 3.578 1.00 15.18 ? 17 ILE A CA 1 ATOM 11 C C . ILE A 1 2 ? -27.820 3.696 4.690 1.00 14.80 ? 17 ILE A C 1 ATOM 12 O O . ILE A 1 2 ? -27.754 3.038 5.725 1.00 15.73 ? 17 ILE A O 1 ATOM 13 C CB . ILE A 1 2 ? -27.114 2.186 2.831 1.00 15.94 ? 17 ILE A CB 1 ATOM 14 C CG1 . ILE A 1 2 ? -26.049 1.854 1.789 1.00 19.54 ? 17 ILE A CG1 1 ATOM 15 C CG2 . ILE A 1 2 ? -28.514 2.235 2.206 1.00 19.19 ? 17 ILE A CG2 1 ATOM 16 C CD1 . ILE A 1 2 ? -25.804 2.935 0.759 1.00 19.58 ? 17 ILE A CD1 1 ATOM 17 N N . GLY A 1 3 ? -28.775 4.599 4.463 1.00 16.58 ? 18 GLY A N 1 ATOM 18 C CA . GLY A 1 3 ? -29.865 4.806 5.423 1.00 17.29 ? 18 GLY A CA 1 ATOM 19 C C . GLY A 1 3 ? -29.384 5.301 6.775 1.00 16.80 ? 18 GLY A C 1 ATOM 20 O O . GLY A 1 3 ? -29.962 4.949 7.813 1.00 18.16 ? 18 GLY A O 1 ATOM 21 N N . GLY A 1 4 ? -28.342 6.128 6.745 1.00 15.44 ? 19 GLY A N 1 ATOM 22 C CA . GLY A 1 4 ? -27.795 6.715 7.950 1.00 16.00 ? 19 GLY A CA 1 ATOM 23 C C . GLY A 1 4 ? -27.995 8.212 7.969 1.00 16.70 ? 19 GLY A C 1 ATOM 24 O O . GLY A 1 4 ? -28.696 8.788 7.126 1.00 16.97 ? 19 GLY A O 1 ATOM 25 N N . HIS A 1 5 ? -27.373 8.845 8.952 1.00 18.25 ? 20 HIS A N 1 ATOM 26 C CA . HIS A 1 5 ? -27.459 10.284 9.120 1.00 17.44 ? 20 HIS A CA 1 ATOM 27 C C . HIS A 1 5 ? -26.126 10.823 9.505 1.00 15.55 ? 20 HIS A C 1 ATOM 28 O O . HIS A 1 5 ? -25.318 10.128 10.131 1.00 16.84 ? 20 HIS A O 1 ATOM 29 C CB . HIS A 1 5 ? -28.509 10.632 10.169 1.00 20.54 ? 20 HIS A CB 1 ATOM 30 C CG . HIS A 1 5 ? -29.892 10.191 9.776 1.00 23.13 ? 20 HIS A CG 1 ATOM 31 N ND1 . HIS A 1 5 ? -30.421 9.023 10.184 1.00 27.06 ? 20 HIS A ND1 1 ATOM 32 C CD2 . HIS A 1 5 ? -30.824 10.772 8.916 1.00 28.02 ? 20 HIS A CD2 1 ATOM 33 C CE1 . HIS A 1 5 ? -31.651 8.884 9.648 1.00 27.56 ? 20 HIS A CE1 1 ATOM 34 N NE2 . HIS A 1 5 ? -31.890 9.954 8.870 1.00 31.71 ? 20 HIS A NE2 1 ATOM 35 N N . GLU A 1 6 ? -25.868 12.057 9.118 1.00 16.23 ? 21 GLU A N 1 ATOM 36 C CA . GLU A 1 6 ? -24.633 12.723 9.436 1.00 15.40 ? 21 GLU A CA 1 ATOM 37 C C . GLU A 1 6 ? -24.505 12.893 10.945 1.00 15.90 ? 21 GLU A C 1 ATOM 38 O O . GLU A 1 6 ? -25.398 13.451 11.595 1.00 18.15 ? 21 GLU A O 1 ATOM 39 C CB . GLU A 1 6 ? -24.569 14.068 8.729 1.00 17.18 ? 21 GLU A CB 1 ATOM 40 C CG . GLU A 1 6 ? -23.209 14.735 8.801 1.00 18.29 ? 21 GLU A CG 1 ATOM 41 C CD . GLU A 1 6 ? -23.128 16.014 8.002 1.00 19.61 ? 21 GLU A CD 1 ATOM 42 O OE1 . GLU A 1 6 ? -24.116 16.380 7.327 1.00 21.17 ? 21 GLU A OE1 1 ATOM 43 O OE2 . GLU A 1 6 ? -22.073 16.658 8.045 1.00 20.76 ? 21 GLU A OE2 1 ATOM 44 N N . VAL A 1 7 ? -23.393 12.451 11.524 1.00 15.57 ? 22 VAL A N 1 ATOM 45 C CA . VAL A 1 7 ? -23.189 12.618 12.948 1.00 15.34 ? 22 VAL A CA 1 ATOM 46 C C . VAL A 1 7 ? -22.843 14.075 13.262 1.00 16.63 ? 22 VAL A C 1 ATOM 47 O O . VAL A 1 7 ? -22.461 14.859 12.385 1.00 16.23 ? 22 VAL A O 1 ATOM 48 C CB . VAL A 1 7 ? -22.115 11.665 13.506 1.00 14.70 ? 22 VAL A CB 1 ATOM 49 C CG1 . VAL A 1 7 ? -22.505 10.223 13.192 1.00 16.20 ? 22 VAL A CG1 1 ATOM 50 C CG2 . VAL A 1 7 ? -20.740 12.003 12.963 1.00 14.49 ? 22 VAL A CG2 1 ATOM 51 N N . THR A 1 8 ? -23.001 14.446 14.521 1.00 14.86 ? 23 THR A N 1 ATOM 52 C CA . THR A 1 8 ? -22.453 15.710 14.988 1.00 15.80 ? 23 THR A CA 1 ATOM 53 C C . THR A 1 8 ? -20.938 15.649 14.817 1.00 14.49 ? 23 THR A C 1 ATOM 54 O O . THR A 1 8 ? -20.310 14.659 15.227 1.00 13.22 ? 23 THR A O 1 ATOM 55 C CB . THR A 1 8 ? -22.787 15.946 16.466 1.00 16.62 ? 23 THR A CB 1 ATOM 56 O OG1 . THR A 1 8 ? -24.204 16.130 16.610 1.00 17.83 ? 23 THR A OG1 1 ATOM 57 C CG2 . THR A 1 8 ? -22.067 17.178 16.999 1.00 17.76 ? 23 THR A CG2 1 ATOM 58 N N . PRO A 1 9 ? -20.334 16.688 14.217 1.00 15.68 ? 24 PRO A N 1 ATOM 59 C CA . PRO A 1 9 ? -18.898 16.598 13.983 1.00 14.43 ? 24 PRO A CA 1 ATOM 60 C C . PRO A 1 9 ? -18.097 16.245 15.238 1.00 15.80 ? 24 PRO A C 1 ATOM 61 O O . PRO A 1 9 ? -18.310 16.816 16.304 1.00 17.01 ? 24 PRO A O 1 ATOM 62 C CB . PRO A 1 9 ? -18.548 17.992 13.460 1.00 15.73 ? 24 PRO A CB 1 ATOM 63 C CG . PRO A 1 9 ? -19.787 18.431 12.736 1.00 16.37 ? 24 PRO A CG 1 ATOM 64 C CD . PRO A 1 9 ? -20.920 17.876 13.565 1.00 18.71 ? 24 PRO A CD 1 ATOM 65 N N . HIS A 1 10 ? -17.210 15.261 15.113 1.00 12.98 ? 25 HIS A N 1 ATOM 66 C CA . HIS A 1 10 ? -16.260 14.870 16.171 1.00 13.00 ? 25 HIS A CA 1 ATOM 67 C C . HIS A 1 10 ? -16.901 14.155 17.328 1.00 12.59 ? 25 HIS A C 1 ATOM 68 O O . HIS A 1 10 ? -16.257 13.949 18.348 1.00 15.31 ? 25 HIS A O 1 ATOM 69 C CB . HIS A 1 10 ? -15.394 16.070 16.579 1.00 15.23 ? 25 HIS A CB 1 ATOM 70 C CG . HIS A 1 10 ? -14.942 16.863 15.385 1.00 16.26 ? 25 HIS A CG 1 ATOM 71 N ND1 . HIS A 1 10 ? -14.117 16.346 14.444 1.00 16.14 ? 25 HIS A ND1 1 ATOM 72 C CD2 . HIS A 1 10 ? -15.332 18.122 14.917 1.00 15.91 ? 25 HIS A CD2 1 ATOM 73 C CE1 . HIS A 1 10 ? -13.963 17.247 13.454 1.00 15.34 ? 25 HIS A CE1 1 ATOM 74 N NE2 . HIS A 1 10 ? -14.706 18.332 13.752 1.00 17.54 ? 25 HIS A NE2 1 ATOM 75 N N . SER A 1 11 ? -18.139 13.687 17.138 1.00 13.20 ? 26 SER A N 1 ATOM 76 C CA . SER A 1 11 ? -18.880 12.924 18.145 1.00 13.50 ? 26 SER A CA 1 ATOM 77 C C . SER A 1 11 ? -18.580 11.423 18.141 1.00 13.17 ? 26 SER A C 1 ATOM 78 O O . SER A 1 11 ? -19.026 10.707 19.036 1.00 14.48 ? 26 SER A O 1 ATOM 79 C CB . SER A 1 11 ? -20.389 13.173 18.017 1.00 13.69 ? 26 SER A CB 1 ATOM 80 O OG . SER A 1 11 ? -20.938 12.612 16.841 1.00 14.61 ? 26 SER A OG 1 ATOM 81 N N . ARG A 1 12 ? -17.797 10.969 17.157 1.00 12.53 ? 27 ARG A N 1 ATOM 82 C CA . ARG A 1 12 ? -17.284 9.591 17.086 1.00 13.07 ? 27 ARG A CA 1 ATOM 83 C C . ARG A 1 12 ? -15.765 9.638 16.956 1.00 12.26 ? 27 ARG A C 1 ATOM 84 O O . ARG A 1 12 ? -15.206 9.296 15.909 1.00 11.83 ? 27 ARG A O 1 ATOM 85 C CB . ARG A 1 12 ? -17.906 8.849 15.895 1.00 11.73 ? 27 ARG A CB 1 ATOM 86 C CG . ARG A 1 12 ? -19.426 8.834 15.896 1.00 14.44 ? 27 ARG A CG 1 ATOM 87 C CD . ARG A 1 12 ? -20.003 8.072 17.054 1.00 14.79 ? 27 ARG A CD 1 ATOM 88 N NE . ARG A 1 12 ? -21.457 8.060 17.002 1.00 15.45 ? 27 ARG A NE 1 ATOM 89 C CZ . ARG A 1 12 ? -22.270 8.834 17.711 1.00 16.85 ? 27 ARG A CZ 1 ATOM 90 N NH1 . ARG A 1 12 ? -21.808 9.734 18.571 1.00 17.37 ? 27 ARG A NH1 1 ATOM 91 N NH2 . ARG A 1 12 ? -23.573 8.686 17.556 1.00 17.83 ? 27 ARG A NH2 1 ATOM 92 N N . PRO A 1 13 ? -15.077 10.051 18.028 1.00 11.92 ? 28 PRO A N 1 ATOM 93 C CA . PRO A 1 13 ? -13.702 10.504 17.890 1.00 12.84 ? 28 PRO A CA 1 ATOM 94 C C . PRO A 1 13 ? -12.692 9.378 17.657 1.00 12.62 ? 28 PRO A C 1 ATOM 95 O O . PRO A 1 13 ? -11.524 9.652 17.428 1.00 12.45 ? 28 PRO A O 1 ATOM 96 C CB . PRO A 1 13 ? -13.450 11.218 19.230 1.00 13.32 ? 28 PRO A CB 1 ATOM 97 C CG . PRO A 1 13 ? -14.408 10.575 20.165 1.00 14.04 ? 28 PRO A CG 1 ATOM 98 C CD . PRO A 1 13 ? -15.631 10.361 19.353 1.00 13.73 ? 28 PRO A CD 1 ATOM 99 N N . TYR A 1 14 ? -13.147 8.129 17.727 1.00 11.44 ? 29 TYR A N 1 ATOM 100 C CA . TYR A 1 14 ? -12.325 6.963 17.387 1.00 10.86 ? 29 TYR A CA 1 ATOM 101 C C . TYR A 1 14 ? -12.266 6.665 15.892 1.00 10.16 ? 29 TYR A C 1 ATOM 102 O O . TYR A 1 14 ? -11.472 5.818 15.458 1.00 11.50 ? 29 TYR A O 1 ATOM 103 C CB . TYR A 1 14 ? -12.849 5.719 18.112 1.00 10.89 ? 29 TYR A CB 1 ATOM 104 C CG . TYR A 1 14 ? -14.328 5.524 17.975 1.00 11.69 ? 29 TYR A CG 1 ATOM 105 C CD1 . TYR A 1 14 ? -14.882 4.948 16.825 1.00 11.44 ? 29 TYR A CD1 1 ATOM 106 C CD2 . TYR A 1 14 ? -15.208 5.965 18.965 1.00 11.51 ? 29 TYR A CD2 1 ATOM 107 C CE1 . TYR A 1 14 ? -16.259 4.785 16.707 1.00 11.27 ? 29 TYR A CE1 1 ATOM 108 C CE2 . TYR A 1 14 ? -16.572 5.802 18.843 1.00 12.84 ? 29 TYR A CE2 1 ATOM 109 C CZ . TYR A 1 14 ? -17.104 5.212 17.706 1.00 13.13 ? 29 TYR A CZ 1 ATOM 110 O OH . TYR A 1 14 ? -18.477 5.052 17.586 1.00 14.02 ? 29 TYR A OH 1 ATOM 111 N N . MET A 1 15 ? -13.093 7.313 15.083 1.00 9.59 ? 30 MET A N 1 ATOM 112 C CA . MET A 1 15 ? -13.167 6.952 13.661 1.00 9.16 ? 30 MET A CA 1 ATOM 113 C C . MET A 1 15 ? -11.944 7.457 12.904 1.00 10.99 ? 30 MET A C 1 ATOM 114 O O . MET A 1 15 ? -11.519 8.606 13.069 1.00 12.67 ? 30 MET A O 1 ATOM 115 C CB . MET A 1 15 ? -14.442 7.507 13.037 1.00 10.35 ? 30 MET A CB 1 ATOM 116 C CG . MET A 1 15 ? -15.689 6.750 13.439 1.00 11.40 ? 30 MET A CG 1 ATOM 117 S SD . MET A 1 15 ? -15.643 5.008 12.986 1.00 11.24 ? 30 MET A SD 1 ATOM 118 C CE . MET A 1 15 ? -15.393 5.047 11.194 1.00 12.34 ? 30 MET A CE 1 ATOM 119 N N . ALA A 1 16 ? -11.414 6.599 12.042 1.00 11.10 ? 31 ALA A N 1 ATOM 120 C CA . ALA A 1 16 ? -10.262 6.888 11.221 1.00 10.93 ? 31 ALA A CA 1 ATOM 121 C C . ALA A 1 16 ? -10.606 6.738 9.741 1.00 10.09 ? 31 ALA A C 1 ATOM 122 O O . ALA A 1 16 ? -11.375 5.838 9.369 1.00 10.57 ? 31 ALA A O 1 ATOM 123 C CB . ALA A 1 16 ? -9.149 5.937 11.583 1.00 11.88 ? 31 ALA A CB 1 ATOM 124 N N . SER A 1 17 ? -10.062 7.619 8.909 1.00 10.03 ? 32 SER A N 1 ATOM 125 C CA . SER A 1 17 ? -10.100 7.473 7.460 1.00 11.24 ? 32 SER A CA 1 ATOM 126 C C . SER A 1 17 ? -8.743 7.028 6.952 1.00 11.48 ? 32 SER A C 1 ATOM 127 O O . SER A 1 17 ? -7.742 7.651 7.266 1.00 12.58 ? 32 SER A O 1 ATOM 128 C CB . SER A 1 17 ? -10.469 8.797 6.820 1.00 12.40 ? 32 SER A CB 1 ATOM 129 O OG . SER A 1 17 ? -10.273 8.752 5.417 1.00 14.29 ? 32 SER A OG 1 ATOM 130 N N . VAL A 1 18 ? -8.717 5.945 6.185 1.00 12.66 ? 33 VAL A N 1 ATOM 131 C CA . VAL A 1 18 ? -7.512 5.498 5.504 1.00 12.08 ? 33 VAL A CA 1 ATOM 132 C C . VAL A 1 18 ? -7.596 6.007 4.071 1.00 12.39 ? 33 VAL A C 1 ATOM 133 O O . VAL A 1 18 ? -8.563 5.701 3.352 1.00 13.53 ? 33 VAL A O 1 ATOM 134 C CB . VAL A 1 18 ? -7.405 3.958 5.492 1.00 14.00 ? 33 VAL A CB 1 ATOM 135 C CG1 . VAL A 1 18 ? -6.188 3.503 4.669 1.00 15.52 ? 33 VAL A CG1 1 ATOM 136 C CG2 . VAL A 1 18 ? -7.387 3.395 6.915 1.00 15.05 ? 33 VAL A CG2 1 ATOM 137 N N . ARG A 1 19 ? -6.617 6.808 3.680 1.00 13.73 ? 34 ARG A N 1 ATOM 138 C CA . ARG A 1 19 ? -6.617 7.408 2.359 1.00 14.89 ? 34 ARG A CA 1 ATOM 139 C C . ARG A 1 19 ? -5.411 6.951 1.570 1.00 16.33 ? 34 ARG A C 1 ATOM 140 O O . ARG A 1 19 ? -4.334 6.776 2.128 1.00 18.09 ? 34 ARG A O 1 ATOM 141 C CB . ARG A 1 19 ? -6.704 8.937 2.428 1.00 20.21 ? 34 ARG A CB 1 ATOM 142 C CG . ARG A 1 19 ? -5.634 9.634 3.229 1.00 24.47 ? 34 ARG A CG 1 ATOM 143 C CD . ARG A 1 19 ? -5.607 11.138 2.945 1.00 24.16 ? 34 ARG A CD 1 ATOM 144 N NE . ARG A 1 19 ? -6.850 11.818 3.329 1.00 22.97 ? 34 ARG A NE 1 ATOM 145 C CZ . ARG A 1 19 ? -6.957 13.124 3.587 1.00 26.24 ? 34 ARG A CZ 1 ATOM 146 N NH1 . ARG A 1 19 ? -5.899 13.937 3.516 1.00 27.19 ? 34 ARG A NH1 1 ATOM 147 N NH2 . ARG A 1 19 ? -8.133 13.620 3.945 1.00 25.96 ? 34 ARG A NH2 1 ATOM 148 N N . PHE A 1 20 ? -5.624 6.723 0.275 1.00 17.86 ? 35 PHE A N 1 ATOM 149 C CA . PHE A 1 20 ? -4.535 6.407 -0.649 1.00 20.71 ? 35 PHE A CA 1 ATOM 150 C C . PHE A 1 20 ? -4.541 7.432 -1.765 1.00 24.37 ? 35 PHE A C 1 ATOM 151 O O . PHE A 1 20 ? -5.585 7.708 -2.351 1.00 23.58 ? 35 PHE A O 1 ATOM 152 C CB . PHE A 1 20 ? -4.703 5.004 -1.234 1.00 19.17 ? 35 PHE A CB 1 ATOM 153 C CG . PHE A 1 20 ? -4.395 3.907 -0.266 1.00 20.87 ? 35 PHE A CG 1 ATOM 154 C CD1 . PHE A 1 20 ? -3.079 3.603 0.037 1.00 22.89 ? 35 PHE A CD1 1 ATOM 155 C CD2 . PHE A 1 20 ? -5.403 3.172 0.334 1.00 21.76 ? 35 PHE A CD2 1 ATOM 156 C CE1 . PHE A 1 20 ? -2.766 2.604 0.925 1.00 24.75 ? 35 PHE A CE1 1 ATOM 157 C CE2 . PHE A 1 20 ? -5.096 2.159 1.222 1.00 22.40 ? 35 PHE A CE2 1 ATOM 158 C CZ . PHE A 1 20 ? -3.775 1.881 1.517 1.00 23.66 ? 35 PHE A CZ 1 ATOM 159 N N . GLY A 1 21 ? -3.370 7.990 -2.046 1.00 27.99 ? 36 GLY A N 1 ATOM 160 C CA . GLY A 1 21 ? -3.237 9.045 -3.051 1.00 29.04 ? 36 GLY A CA 1 ATOM 161 C C . GLY A 1 21 ? -4.133 10.236 -2.763 1.00 33.49 ? 36 GLY A C 1 ATOM 162 O O . GLY A 1 21 ? -4.668 10.850 -3.689 1.00 35.70 ? 36 GLY A O 1 ATOM 163 N N . GLY A 1 22 ? -4.313 10.549 -1.479 1.00 25.65 ? 38 GLY A N 1 ATOM 164 C CA . GLY A 1 22 ? -5.156 11.664 -1.049 1.00 26.53 ? 38 GLY A CA 1 ATOM 165 C C . GLY A 1 22 ? -6.662 11.411 -1.044 1.00 28.59 ? 38 GLY A C 1 ATOM 166 O O . GLY A 1 22 ? -7.442 12.320 -0.741 1.00 31.12 ? 38 GLY A O 1 ATOM 167 N N . GLN A 1 23 ? -7.077 10.189 -1.378 1.00 24.03 ? 39 GLN A N 1 ATOM 168 C CA . GLN A 1 23 ? -8.492 9.855 -1.523 1.00 22.79 ? 39 GLN A CA 1 ATOM 169 C C . GLN A 1 23 ? -8.940 8.849 -0.455 1.00 18.29 ? 39 GLN A C 1 ATOM 170 O O . GLN A 1 23 ? -8.289 7.840 -0.244 1.00 18.17 ? 39 GLN A O 1 ATOM 171 C CB . GLN A 1 23 ? -8.734 9.288 -2.930 1.00 30.44 ? 39 GLN A CB 1 ATOM 172 C CG . GLN A 1 23 ? -10.162 8.848 -3.225 1.00 37.30 ? 39 GLN A CG 1 ATOM 173 C CD . GLN A 1 23 ? -10.448 8.672 -4.716 1.00 49.96 ? 39 GLN A CD 1 ATOM 174 O OE1 . GLN A 1 23 ? -9.561 8.814 -5.561 1.00 51.22 ? 39 GLN A OE1 1 ATOM 175 N NE2 . GLN A 1 23 ? -11.699 8.361 -5.040 1.00 56.30 ? 39 GLN A NE2 1 ATOM 176 N N . HIS A 1 24 ? -10.051 9.141 0.212 1.00 16.47 ? 40 HIS A N 1 ATOM 177 C CA . HIS A 1 24 ? -10.610 8.209 1.186 1.00 14.92 ? 40 HIS A CA 1 ATOM 178 C C . HIS A 1 24 ? -10.897 6.879 0.542 1.00 15.58 ? 40 HIS A C 1 ATOM 179 O O . HIS A 1 24 ? -11.549 6.816 -0.493 1.00 17.07 ? 40 HIS A O 1 ATOM 180 C CB . HIS A 1 24 ? -11.900 8.737 1.782 1.00 13.39 ? 40 HIS A CB 1 ATOM 181 C CG . HIS A 1 24 ? -12.607 7.730 2.663 1.00 12.45 ? 40 HIS A CG 1 ATOM 182 N ND1 . HIS A 1 24 ? -12.256 7.508 3.955 1.00 12.11 ? 40 HIS A ND1 1 ATOM 183 C CD2 . HIS A 1 24 ? -13.637 6.847 2.375 1.00 13.98 ? 40 HIS A CD2 1 ATOM 184 C CE1 . HIS A 1 24 ? -13.037 6.534 4.456 1.00 11.76 ? 40 HIS A CE1 1 ATOM 185 N NE2 . HIS A 1 24 ? -13.888 6.135 3.489 1.00 12.56 ? 40 HIS A NE2 1 ATOM 186 N N . HIS A 1 25 ? -10.461 5.808 1.191 1.00 14.08 ? 41 HIS A N 1 ATOM 187 C CA . HIS A 1 25 ? -10.598 4.442 0.682 1.00 14.54 ? 41 HIS A CA 1 ATOM 188 C C . HIS A 1 25 ? -11.248 3.498 1.657 1.00 13.10 ? 41 HIS A C 1 ATOM 189 O O . HIS A 1 25 ? -12.020 2.631 1.259 1.00 14.02 ? 41 HIS A O 1 ATOM 190 C CB . HIS A 1 25 ? -9.218 3.918 0.348 1.00 16.28 ? 41 HIS A CB 1 ATOM 191 C CG . HIS A 1 25 ? -9.215 2.539 -0.257 1.00 19.73 ? 41 HIS A CG 1 ATOM 192 N ND1 . HIS A 1 25 ? -9.857 2.247 -1.405 1.00 22.57 ? 41 HIS A ND1 1 ATOM 193 C CD2 . HIS A 1 25 ? -8.590 1.354 0.160 1.00 22.49 ? 41 HIS A CD2 1 ATOM 194 C CE1 . HIS A 1 25 ? -9.660 0.934 -1.704 1.00 26.09 ? 41 HIS A CE1 1 ATOM 195 N NE2 . HIS A 1 25 ? -8.887 0.396 -0.751 1.00 23.71 ? 41 HIS A NE2 1 ATOM 196 N N . CYS A 1 26 ? -10.951 3.636 2.949 1.00 12.59 ? 42 CYS A N 1 ATOM 197 C CA . CYS A 1 26 ? -11.528 2.754 3.955 1.00 12.31 ? 42 CYS A CA 1 ATOM 198 C C . CYS A 1 26 ? -11.645 3.467 5.298 1.00 10.14 ? 42 CYS A C 1 ATOM 199 O O . CYS A 1 26 ? -10.998 4.504 5.522 1.00 11.30 ? 42 CYS A O 1 ATOM 200 C CB . CYS A 1 26 ? -10.676 1.510 4.100 1.00 12.18 ? 42 CYS A CB 1 ATOM 201 S SG . CYS A 1 26 ? -11.073 0.214 2.916 1.00 15.56 ? 42 CYS A SG 1 ATOM 202 N N . GLY A 1 27 ? -12.455 2.891 6.179 1.00 10.01 ? 43 GLY A N 1 ATOM 203 C CA . GLY A 1 27 ? -12.494 3.296 7.571 1.00 11.01 ? 43 GLY A CA 1 ATOM 204 C C . GLY A 1 27 ? -11.580 2.479 8.456 1.00 10.96 ? 43 GLY A C 1 ATOM 205 O O . GLY A 1 27 ? -10.790 1.628 7.990 1.00 10.73 ? 43 GLY A O 1 ATOM 206 N N . GLY A 1 28 ? -11.649 2.766 9.746 1.00 11.03 ? 44 GLY A N 1 ATOM 207 C CA . GLY A 1 28 ? -10.842 2.113 10.769 1.00 9.71 ? 44 GLY A CA 1 ATOM 208 C C . GLY A 1 28 ? -11.177 2.775 12.084 1.00 8.72 ? 44 GLY A C 1 ATOM 209 O O . GLY A 1 28 ? -11.988 3.732 12.114 1.00 10.26 ? 44 GLY A O 1 ATOM 210 N N . PHE A 1 29 ? -10.629 2.242 13.174 1.00 9.80 ? 45 PHE A N 1 ATOM 211 C CA . PHE A 1 29 ? -10.739 2.929 14.445 1.00 9.38 ? 45 PHE A CA 1 ATOM 212 C C . PHE A 1 29 ? -9.467 2.935 15.261 1.00 9.83 ? 45 PHE A C 1 ATOM 213 O O . PHE A 1 29 ? -8.615 2.053 15.132 1.00 10.83 ? 45 PHE A O 1 ATOM 214 C CB . PHE A 1 29 ? -11.922 2.409 15.253 1.00 10.98 ? 45 PHE A CB 1 ATOM 215 C CG . PHE A 1 29 ? -11.722 1.047 15.869 1.00 12.02 ? 45 PHE A CG 1 ATOM 216 C CD1 . PHE A 1 29 ? -11.117 0.909 17.120 1.00 11.46 ? 45 PHE A CD1 1 ATOM 217 C CD2 . PHE A 1 29 ? -12.167 -0.115 15.220 1.00 12.25 ? 45 PHE A CD2 1 ATOM 218 C CE1 . PHE A 1 29 ? -10.964 -0.330 17.720 1.00 13.11 ? 45 PHE A CE1 1 ATOM 219 C CE2 . PHE A 1 29 ? -12.001 -1.365 15.823 1.00 11.21 ? 45 PHE A CE2 1 ATOM 220 C CZ . PHE A 1 29 ? -11.400 -1.466 17.064 1.00 12.78 ? 45 PHE A CZ 1 ATOM 221 N N . LEU A 1 30 ? -9.355 3.962 16.106 1.00 10.78 ? 46 LEU A N 1 ATOM 222 C CA . LEU A 1 30 ? -8.207 4.162 16.967 1.00 10.84 ? 46 LEU A CA 1 ATOM 223 C C . LEU A 1 30 ? -8.348 3.248 18.185 1.00 10.17 ? 46 LEU A C 1 ATOM 224 O O . LEU A 1 30 ? -9.250 3.412 19.004 1.00 11.49 ? 46 LEU A O 1 ATOM 225 C CB . LEU A 1 30 ? -8.102 5.644 17.361 1.00 11.81 ? 46 LEU A CB 1 ATOM 226 C CG . LEU A 1 30 ? -6.737 6.104 17.906 1.00 11.50 ? 46 LEU A CG 1 ATOM 227 C CD1 . LEU A 1 30 ? -5.615 5.928 16.891 1.00 12.99 ? 46 LEU A CD1 1 ATOM 228 C CD2 . LEU A 1 30 ? -6.801 7.557 18.369 1.00 12.76 ? 46 LEU A CD2 1 ATOM 229 N N . LEU A 1 31 ? -7.435 2.295 18.301 1.00 11.29 ? 47 LEU A N 1 ATOM 230 C CA . LEU A 1 31 ? -7.384 1.342 19.386 1.00 12.06 ? 47 LEU A CA 1 ATOM 231 C C . LEU A 1 31 ? -6.490 1.847 20.537 1.00 12.39 ? 47 LEU A C 1 ATOM 232 O O . LEU A 1 31 ? -6.845 1.712 21.714 1.00 13.29 ? 47 LEU A O 1 ATOM 233 C CB . LEU A 1 31 ? -6.849 0.010 18.840 1.00 11.89 ? 47 LEU A CB 1 ATOM 234 C CG . LEU A 1 31 ? -6.722 -1.132 19.841 1.00 13.09 ? 47 LEU A CG 1 ATOM 235 C CD1 . LEU A 1 31 ? -8.075 -1.666 20.279 1.00 14.29 ? 47 LEU A CD1 1 ATOM 236 C CD2 . LEU A 1 31 ? -5.817 -2.230 19.285 1.00 14.53 ? 47 LEU A CD2 1 ATOM 237 N N . ARG A 1 32 ? -5.317 2.344 20.153 1.00 12.01 ? 48 ARG A N 1 ATOM 238 C CA A ARG A 1 32 ? -4.356 2.961 21.065 0.50 13.25 ? 48 ARG A CA 1 ATOM 239 C CA B ARG A 1 32 ? -4.364 2.971 21.072 0.50 12.68 ? 48 ARG A CA 1 ATOM 240 C C . ARG A 1 32 ? -3.803 4.185 20.342 1.00 12.90 ? 48 ARG A C 1 ATOM 241 O O . ARG A 1 32 ? -4.090 4.384 19.167 1.00 13.09 ? 48 ARG A O 1 ATOM 242 C CB A ARG A 1 32 ? -3.232 1.981 21.417 0.50 14.61 ? 48 ARG A CB 1 ATOM 243 C CB B ARG A 1 32 ? -3.234 2.009 21.454 0.50 13.17 ? 48 ARG A CB 1 ATOM 244 C CG A ARG A 1 32 ? -3.675 0.823 22.297 0.50 16.49 ? 48 ARG A CG 1 ATOM 245 C CG B ARG A 1 32 ? -3.684 0.761 22.199 0.50 13.99 ? 48 ARG A CG 1 ATOM 246 C CD A ARG A 1 32 ? -3.964 1.304 23.710 0.50 19.83 ? 48 ARG A CD 1 ATOM 247 C CD B ARG A 1 32 ? -4.247 1.068 23.580 0.50 14.95 ? 48 ARG A CD 1 ATOM 248 N NE A ARG A 1 32 ? -4.750 0.375 24.519 0.50 24.16 ? 48 ARG A NE 1 ATOM 249 N NE B ARG A 1 32 ? -3.218 1.463 24.535 0.50 14.92 ? 48 ARG A NE 1 ATOM 250 C CZ A ARG A 1 32 ? -4.271 -0.239 25.587 0.50 27.26 ? 48 ARG A CZ 1 ATOM 251 C CZ B ARG A 1 32 ? -3.471 2.115 25.666 0.50 17.36 ? 48 ARG A CZ 1 ATOM 252 N NH1 A ARG A 1 32 ? -3.021 -0.026 25.950 0.50 33.60 ? 48 ARG A NH1 1 ATOM 253 N NH1 B ARG A 1 32 ? -4.713 2.449 25.987 0.50 18.00 ? 48 ARG A NH1 1 ATOM 254 N NH2 A ARG A 1 32 ? -5.030 -1.047 26.304 0.50 16.64 ? 48 ARG A NH2 1 ATOM 255 N NH2 B ARG A 1 32 ? -2.479 2.439 26.475 0.50 18.03 ? 48 ARG A NH2 1 ATOM 256 N N . ALA A 1 33 ? -3.025 5.022 21.017 1.00 14.96 ? 49 ALA A N 1 ATOM 257 C CA . ALA A 1 33 ? -2.583 6.268 20.361 1.00 14.92 ? 49 ALA A CA 1 ATOM 258 C C . ALA A 1 33 ? -1.806 6.050 19.061 1.00 15.70 ? 49 ALA A C 1 ATOM 259 O O . ALA A 1 33 ? -1.871 6.888 18.157 1.00 15.41 ? 49 ALA A O 1 ATOM 260 C CB . ALA A 1 33 ? -1.788 7.159 21.308 1.00 15.34 ? 49 ALA A CB 1 ATOM 261 N N . ARG A 1 34 ? -1.107 4.927 18.954 1.00 14.81 ? 50 ARG A N 1 ATOM 262 C CA . ARG A 1 34 ? -0.314 4.608 17.775 1.00 17.15 ? 50 ARG A CA 1 ATOM 263 C C . ARG A 1 34 ? -0.889 3.447 16.936 1.00 15.11 ? 50 ARG A C 1 ATOM 264 O O . ARG A 1 34 ? -0.209 2.945 16.048 1.00 14.57 ? 50 ARG A O 1 ATOM 265 C CB . ARG A 1 34 ? 1.120 4.266 18.212 1.00 23.55 ? 50 ARG A CB 1 ATOM 266 C CG . ARG A 1 34 ? 2.183 4.699 17.226 1.00 34.85 ? 50 ARG A CG 1 ATOM 267 C CD . ARG A 1 34 ? 3.552 4.149 17.586 1.00 40.13 ? 50 ARG A CD 1 ATOM 268 N NE . ARG A 1 34 ? 4.528 4.445 16.532 1.00 46.95 ? 50 ARG A NE 1 ATOM 269 C CZ . ARG A 1 34 ? 5.445 5.415 16.568 1.00 49.40 ? 50 ARG A CZ 1 ATOM 270 N NH1 . ARG A 1 34 ? 5.566 6.221 17.622 1.00 60.41 ? 50 ARG A NH1 1 ATOM 271 N NH2 . ARG A 1 34 ? 6.265 5.575 15.533 1.00 58.83 ? 50 ARG A NH2 1 ATOM 272 N N . TRP A 1 35 ? -2.117 3.011 17.217 1.00 12.67 ? 51 TRP A N 1 ATOM 273 C CA . TRP A 1 35 ? -2.654 1.794 16.603 1.00 11.98 ? 51 TRP A CA 1 ATOM 274 C C . TRP A 1 35 ? -4.059 1.968 16.096 1.00 11.64 ? 51 TRP A C 1 ATOM 275 O O . TRP A 1 35 ? -4.948 2.353 16.841 1.00 12.40 ? 51 TRP A O 1 ATOM 276 C CB . TRP A 1 35 ? -2.651 0.663 17.621 1.00 13.40 ? 51 TRP A CB 1 ATOM 277 C CG . TRP A 1 35 ? -1.266 0.205 17.979 1.00 14.43 ? 51 TRP A CG 1 ATOM 278 C CD1 . TRP A 1 35 ? -0.483 0.612 19.057 1.00 13.91 ? 51 TRP A CD1 1 ATOM 279 C CD2 . TRP A 1 35 ? -0.467 -0.769 17.265 1.00 13.45 ? 51 TRP A CD2 1 ATOM 280 N NE1 . TRP A 1 35 ? 0.717 -0.034 19.054 1.00 15.45 ? 51 TRP A NE1 1 ATOM 281 C CE2 . TRP A 1 35 ? 0.787 -0.894 18.007 1.00 15.00 ? 51 TRP A CE2 1 ATOM 282 C CE3 . TRP A 1 35 ? -0.662 -1.553 16.136 1.00 15.80 ? 51 TRP A CE3 1 ATOM 283 C CZ2 . TRP A 1 35 ? 1.795 -1.758 17.599 1.00 15.97 ? 51 TRP A CZ2 1 ATOM 284 C CZ3 . TRP A 1 35 ? 0.357 -2.416 15.740 1.00 15.36 ? 51 TRP A CZ3 1 ATOM 285 C CH2 . TRP A 1 35 ? 1.556 -2.510 16.453 1.00 16.51 ? 51 TRP A CH2 1 ATOM 286 N N . VAL A 1 36 ? -4.270 1.634 14.818 1.00 12.17 ? 52 VAL A N 1 ATOM 287 C CA . VAL A 1 36 ? -5.573 1.629 14.188 1.00 11.86 ? 52 VAL A CA 1 ATOM 288 C C . VAL A 1 36 ? -5.924 0.225 13.688 1.00 11.23 ? 52 VAL A C 1 ATOM 289 O O . VAL A 1 36 ? -5.078 -0.463 13.106 1.00 12.29 ? 52 VAL A O 1 ATOM 290 C CB . VAL A 1 36 ? -5.589 2.655 13.037 1.00 12.19 ? 52 VAL A CB 1 ATOM 291 C CG1 . VAL A 1 36 ? -6.807 2.504 12.142 1.00 13.13 ? 52 VAL A CG1 1 ATOM 292 C CG2 . VAL A 1 36 ? -5.515 4.061 13.621 1.00 12.46 ? 52 VAL A CG2 1 ATOM 293 N N . VAL A 1 37 ? -7.149 -0.203 13.949 1.00 10.09 ? 53 VAL A N 1 ATOM 294 C CA . VAL A 1 37 ? -7.703 -1.449 13.410 1.00 10.26 ? 53 VAL A CA 1 ATOM 295 C C . VAL A 1 37 ? -8.454 -1.115 12.113 1.00 10.63 ? 53 VAL A C 1 ATOM 296 O O . VAL A 1 37 ? -9.208 -0.161 12.061 1.00 10.90 ? 53 VAL A O 1 ATOM 297 C CB . VAL A 1 37 ? -8.673 -2.095 14.423 1.00 11.29 ? 53 VAL A CB 1 ATOM 298 C CG1 . VAL A 1 37 ? -9.354 -3.333 13.833 1.00 12.22 ? 53 VAL A CG1 1 ATOM 299 C CG2 . VAL A 1 37 ? -7.945 -2.442 15.714 1.00 12.74 ? 53 VAL A CG2 1 ATOM 300 N N . SER A 1 38 ? -8.260 -1.908 11.071 1.00 10.76 ? 54 SER A N 1 ATOM 301 C CA . SER A 1 38 ? -8.981 -1.753 9.815 1.00 11.03 ? 54 SER A CA 1 ATOM 302 C C . SER A 1 38 ? -9.187 -3.130 9.171 1.00 10.94 ? 54 SER A C 1 ATOM 303 O O . SER A 1 38 ? -8.967 -4.151 9.815 1.00 11.89 ? 54 SER A O 1 ATOM 304 C CB . SER A 1 38 ? -8.237 -0.786 8.886 1.00 11.99 ? 54 SER A CB 1 ATOM 305 O OG . SER A 1 38 ? -9.005 -0.434 7.727 1.00 11.46 ? 54 SER A OG 1 ATOM 306 N N . ALA A 1 39 ? -9.669 -3.149 7.930 1.00 10.31 ? 55 ALA A N 1 ATOM 307 C CA . ALA A 1 39 ? -9.951 -4.390 7.193 1.00 10.77 ? 55 ALA A CA 1 ATOM 308 C C . ALA A 1 39 ? -8.805 -4.720 6.270 1.00 12.74 ? 55 ALA A C 1 ATOM 309 O O . ALA A 1 39 ? -8.348 -3.870 5.519 1.00 14.13 ? 55 ALA A O 1 ATOM 310 C CB . ALA A 1 39 ? -11.238 -4.260 6.397 1.00 12.35 ? 55 ALA A CB 1 ATOM 311 N N . ALA A 1 40 ? -8.364 -5.976 6.285 1.00 11.52 ? 56 ALA A N 1 ATOM 312 C CA . ALA A 1 40 ? -7.253 -6.434 5.455 1.00 11.25 ? 56 ALA A CA 1 ATOM 313 C C . ALA A 1 40 ? -7.473 -6.172 3.965 1.00 12.88 ? 56 ALA A C 1 ATOM 314 O O . ALA A 1 40 ? -6.547 -5.778 3.261 1.00 13.18 ? 56 ALA A O 1 ATOM 315 C CB . ALA A 1 40 ? -7.017 -7.918 5.675 1.00 14.54 ? 56 ALA A CB 1 ATOM 316 N N . HIS A 1 41 ? -8.700 -6.340 3.490 1.00 11.89 ? 57 HIS A N 1 ATOM 317 C CA . HIS A 1 41 ? -8.952 -6.181 2.062 1.00 12.98 ? 57 HIS A CA 1 ATOM 318 C C . HIS A 1 41 ? -8.670 -4.777 1.561 1.00 13.84 ? 57 HIS A C 1 ATOM 319 O O . HIS A 1 41 ? -8.457 -4.568 0.372 1.00 16.02 ? 57 HIS A O 1 ATOM 320 C CB . HIS A 1 41 ? -10.358 -6.668 1.683 1.00 13.14 ? 57 HIS A CB 1 ATOM 321 C CG . HIS A 1 41 ? -11.471 -5.650 1.913 1.00 13.53 ? 57 HIS A CG 1 ATOM 322 N ND1 . HIS A 1 41 ? -12.400 -5.793 2.887 1.00 11.94 ? 57 HIS A ND1 1 ATOM 323 C CD2 . HIS A 1 41 ? -11.787 -4.483 1.235 1.00 12.55 ? 57 HIS A CD2 1 ATOM 324 C CE1 . HIS A 1 41 ? -13.275 -4.783 2.819 1.00 11.71 ? 57 HIS A CE1 1 ATOM 325 N NE2 . HIS A 1 41 ? -12.896 -3.961 1.816 1.00 12.37 ? 57 HIS A NE2 1 ATOM 326 N N . CYS A 1 42 ? -8.658 -3.800 2.473 1.00 12.72 ? 58 CYS A N 1 ATOM 327 C CA . CYS A 1 42 ? -8.376 -2.413 2.093 1.00 13.92 ? 58 CYS A CA 1 ATOM 328 C C . CYS A 1 42 ? -6.968 -2.144 1.582 1.00 12.54 ? 58 CYS A C 1 ATOM 329 O O . CYS A 1 42 ? -6.726 -1.102 0.954 1.00 14.36 ? 58 CYS A O 1 ATOM 330 C CB . CYS A 1 42 ? -8.627 -1.508 3.297 1.00 12.93 ? 58 CYS A CB 1 ATOM 331 S SG . CYS A 1 42 ? -10.360 -1.462 3.815 1.00 14.91 ? 58 CYS A SG 1 ATOM 332 N N . PHE A 1 43 ? -6.040 -3.052 1.889 1.00 14.35 ? 59 PHE A N 1 ATOM 333 C CA . PHE A 1 43 ? -4.610 -2.841 1.642 1.00 14.11 ? 59 PHE A CA 1 ATOM 334 C C . PHE A 1 43 ? -4.053 -3.727 0.549 1.00 16.65 ? 59 PHE A C 1 ATOM 335 O O . PHE A 1 43 ? -2.899 -3.581 0.170 1.00 17.00 ? 59 PHE A O 1 ATOM 336 C CB . PHE A 1 43 ? -3.860 -3.022 2.957 1.00 15.22 ? 59 PHE A CB 1 ATOM 337 C CG . PHE A 1 43 ? -4.259 -2.005 3.968 1.00 15.90 ? 59 PHE A CG 1 ATOM 338 C CD1 . PHE A 1 43 ? -3.643 -0.769 3.970 1.00 16.51 ? 59 PHE A CD1 1 ATOM 339 C CD2 . PHE A 1 43 ? -5.310 -2.223 4.825 1.00 14.86 ? 59 PHE A CD2 1 ATOM 340 C CE1 . PHE A 1 43 ? -4.042 0.214 4.856 1.00 19.15 ? 59 PHE A CE1 1 ATOM 341 C CE2 . PHE A 1 43 ? -5.713 -1.240 5.718 1.00 18.49 ? 59 PHE A CE2 1 ATOM 342 C CZ . PHE A 1 43 ? -5.075 -0.024 5.725 1.00 20.30 ? 59 PHE A CZ 1 ATOM 343 N N . SER A 1 44 ? -4.895 -4.610 0.023 1.00 16.62 ? 60 SER A N 1 ATOM 344 C CA . SER A 1 44 ? -4.476 -5.526 -1.034 1.00 20.69 ? 60 SER A CA 1 ATOM 345 C C . SER A 1 44 ? -3.948 -4.774 -2.241 1.00 19.52 ? 60 SER A C 1 ATOM 346 O O . SER A 1 44 ? -4.622 -3.907 -2.780 1.00 20.84 ? 60 SER A O 1 ATOM 347 C CB . SER A 1 44 ? -5.656 -6.385 -1.452 1.00 25.62 ? 60 SER A CB 1 ATOM 348 O OG . SER A 1 44 ? -6.083 -7.168 -0.360 1.00 32.42 ? 60 SER A OG 1 ATOM 349 N N . HIS A 1 45 ? -2.724 -5.116 -2.662 1.00 19.59 ? 61 HIS A N 1 ATOM 350 C CA . HIS A 1 45 ? -2.063 -4.492 -3.825 1.00 23.74 ? 61 HIS A CA 1 ATOM 351 C C . HIS A 1 45 ? -1.841 -3.009 -3.696 1.00 25.47 ? 61 HIS A C 1 ATOM 352 O O . HIS A 1 45 ? -1.691 -2.310 -4.702 1.00 29.59 ? 61 HIS A O 1 ATOM 353 C CB . HIS A 1 45 ? -2.811 -4.816 -5.121 1.00 27.91 ? 61 HIS A CB 1 ATOM 354 C CG . HIS A 1 45 ? -2.860 -6.289 -5.430 1.00 29.36 ? 61 HIS A CG 1 ATOM 355 N ND1 . HIS A 1 45 ? -3.812 -7.102 -4.937 1.00 33.78 ? 61 HIS A ND1 1 ATOM 356 C CD2 . HIS A 1 45 ? -2.015 -7.086 -6.194 1.00 34.56 ? 61 HIS A CD2 1 ATOM 357 C CE1 . HIS A 1 45 ? -3.586 -8.359 -5.363 1.00 37.58 ? 61 HIS A CE1 1 ATOM 358 N NE2 . HIS A 1 45 ? -2.485 -8.346 -6.128 1.00 33.32 ? 61 HIS A NE2 1 ATOM 359 N N . ARG A 1 46 ? -1.780 -2.520 -2.456 1.00 24.05 ? 62 ARG A N 1 ATOM 360 C CA . ARG A 1 46 ? -1.569 -1.101 -2.198 1.00 25.13 ? 62 ARG A CA 1 ATOM 361 C C . ARG A 1 46 ? -0.148 -0.805 -1.776 1.00 25.00 ? 62 ARG A C 1 ATOM 362 O O . ARG A 1 46 ? 0.401 -1.468 -0.914 1.00 21.69 ? 62 ARG A O 1 ATOM 363 C CB . ARG A 1 46 ? -2.512 -0.624 -1.099 1.00 22.81 ? 62 ARG A CB 1 ATOM 364 C CG . ARG A 1 46 ? -3.960 -0.606 -1.520 1.00 27.52 ? 62 ARG A CG 1 ATOM 365 C CD . ARG A 1 46 ? -4.275 0.666 -2.269 1.00 32.54 ? 62 ARG A CD 1 ATOM 366 N NE . ARG A 1 46 ? -5.592 0.607 -2.882 1.00 35.19 ? 62 ARG A NE 1 ATOM 367 C CZ . ARG A 1 46 ? -6.127 1.584 -3.608 1.00 40.02 ? 62 ARG A CZ 1 ATOM 368 N NH1 . ARG A 1 46 ? -5.460 2.720 -3.816 1.00 43.16 ? 62 ARG A NH1 1 ATOM 369 N NH2 . ARG A 1 46 ? -7.336 1.422 -4.128 1.00 39.69 ? 62 ARG A NH2 1 ATOM 370 N N . ASP A 1 47 A 0.432 0.222 -2.386 1.00 26.33 ? 62 ASP A N 1 ATOM 371 C CA . ASP A 1 47 A 1.694 0.771 -1.918 1.00 27.53 ? 62 ASP A CA 1 ATOM 372 C C . ASP A 1 47 A 1.423 1.530 -0.608 1.00 26.27 ? 62 ASP A C 1 ATOM 373 O O . ASP A 1 47 A 0.824 2.606 -0.618 1.00 27.14 ? 62 ASP A O 1 ATOM 374 C CB . ASP A 1 47 A 2.283 1.698 -2.983 1.00 30.48 ? 62 ASP A CB 1 ATOM 375 C CG . ASP A 1 47 A 3.700 2.143 -2.666 1.00 34.42 ? 62 ASP A CG 1 ATOM 376 O OD1 . ASP A 1 47 A 4.131 2.079 -1.489 1.00 31.01 ? 62 ASP A OD1 1 ATOM 377 O OD2 . ASP A 1 47 A 4.390 2.574 -3.615 1.00 42.23 ? 62 ASP A OD2 1 ATOM 378 N N . LEU A 1 48 B 1.860 0.953 0.512 1.00 24.46 ? 62 LEU A N 1 ATOM 379 C CA . LEU A 1 48 B 1.645 1.562 1.840 1.00 29.02 ? 62 LEU A CA 1 ATOM 380 C C . LEU A 1 48 B 2.151 2.998 1.945 1.00 26.98 ? 62 LEU A C 1 ATOM 381 O O . LEU A 1 48 B 1.592 3.804 2.685 1.00 26.21 ? 62 LEU A O 1 ATOM 382 C CB . LEU A 1 48 B 2.313 0.736 2.949 1.00 31.46 ? 62 LEU A CB 1 ATOM 383 C CG . LEU A 1 48 B 1.530 -0.370 3.651 1.00 36.61 ? 62 LEU A CG 1 ATOM 384 C CD1 . LEU A 1 48 B 2.375 -0.904 4.797 1.00 32.22 ? 62 LEU A CD1 1 ATOM 385 C CD2 . LEU A 1 48 B 0.184 0.134 4.161 1.00 29.68 ? 62 LEU A CD2 1 ATOM 386 N N . ARG A 1 49 C 3.212 3.318 1.206 1.00 30.49 ? 62 ARG A N 1 ATOM 387 C CA . ARG A 1 49 C 3.799 4.661 1.253 1.00 30.93 ? 62 ARG A CA 1 ATOM 388 C C . ARG A 1 49 C 2.859 5.726 0.678 1.00 26.23 ? 62 ARG A C 1 ATOM 389 O O . ARG A 1 49 C 3.075 6.921 0.911 1.00 29.10 ? 62 ARG A O 1 ATOM 390 C CB . ARG A 1 49 C 5.130 4.709 0.492 1.00 38.49 ? 62 ARG A CB 1 ATOM 391 C CG . ARG A 1 49 C 6.157 3.649 0.889 1.00 46.85 ? 62 ARG A CG 1 ATOM 392 C CD . ARG A 1 49 C 7.312 3.577 -0.107 1.00 55.85 ? 62 ARG A CD 1 ATOM 393 N NE . ARG A 1 49 C 6.848 3.584 -1.497 1.00 63.87 ? 62 ARG A NE 1 ATOM 394 C CZ . ARG A 1 49 C 7.639 3.505 -2.566 1.00 73.16 ? 62 ARG A CZ 1 ATOM 395 N NH1 . ARG A 1 49 C 8.958 3.381 -2.435 1.00 71.43 ? 62 ARG A NH1 1 ATOM 396 N NH2 . ARG A 1 49 C 7.100 3.533 -3.781 1.00 77.06 ? 62 ARG A NH2 1 ATOM 397 N N . THR A 1 50 ? 1.836 5.306 -0.077 1.00 22.23 ? 63 THR A N 1 ATOM 398 C CA . THR A 1 50 ? 0.827 6.233 -0.588 1.00 21.66 ? 63 THR A CA 1 ATOM 399 C C . THR A 1 50 ? -0.351 6.386 0.388 1.00 20.79 ? 63 THR A C 1 ATOM 400 O O . THR A 1 50 ? -1.294 7.135 0.111 1.00 21.85 ? 63 THR A O 1 ATOM 401 C CB . THR A 1 50 ? 0.292 5.815 -1.987 1.00 25.01 ? 63 THR A CB 1 ATOM 402 O OG1 . THR A 1 50 ? -0.438 4.580 -1.904 1.00 25.58 ? 63 THR A OG1 1 ATOM 403 C CG2 . THR A 1 50 ? 1.444 5.669 -2.998 1.00 26.53 ? 63 THR A CG2 1 ATOM 404 N N . GLY A 1 51 ? -0.278 5.685 1.520 1.00 19.03 ? 64 GLY A N 1 ATOM 405 C CA . GLY A 1 51 ? -1.345 5.665 2.519 1.00 17.30 ? 64 GLY A CA 1 ATOM 406 C C . GLY A 1 51 ? -1.155 6.678 3.621 1.00 16.90 ? 64 GLY A C 1 ATOM 407 O O . GLY A 1 51 ? -0.044 6.927 4.082 1.00 18.25 ? 64 GLY A O 1 ATOM 408 N N . LEU A 1 52 ? -2.269 7.244 4.064 1.00 15.55 ? 65 LEU A N 1 ATOM 409 C CA . LEU A 1 52 ? -2.301 8.096 5.244 1.00 16.18 ? 65 LEU A CA 1 ATOM 410 C C . LEU A 1 52 ? -3.505 7.699 6.082 1.00 15.30 ? 65 LEU A C 1 ATOM 411 O O . LEU A 1 52 ? -4.516 7.232 5.555 1.00 15.60 ? 65 LEU A O 1 ATOM 412 C CB . LEU A 1 52 ? -2.375 9.572 4.856 1.00 17.89 ? 65 LEU A CB 1 ATOM 413 C CG . LEU A 1 52 ? -1.152 10.160 4.143 1.00 19.27 ? 65 LEU A CG 1 ATOM 414 C CD1 . LEU A 1 52 ? -1.508 11.548 3.625 1.00 22.25 ? 65 LEU A CD1 1 ATOM 415 C CD2 . LEU A 1 52 ? 0.054 10.217 5.063 1.00 18.89 ? 65 LEU A CD2 1 ATOM 416 N N . VAL A 1 53 ? -3.384 7.874 7.389 1.00 13.19 ? 66 VAL A N 1 ATOM 417 C CA . VAL A 1 53 ? -4.491 7.682 8.300 1.00 12.64 ? 66 VAL A CA 1 ATOM 418 C C . VAL A 1 53 ? -4.874 9.048 8.872 1.00 13.92 ? 66 VAL A C 1 ATOM 419 O O . VAL A 1 53 ? -4.016 9.753 9.442 1.00 13.84 ? 66 VAL A O 1 ATOM 420 C CB . VAL A 1 53 ? -4.115 6.720 9.449 1.00 13.40 ? 66 VAL A CB 1 ATOM 421 C CG1 . VAL A 1 53 ? -5.270 6.595 10.435 1.00 17.79 ? 66 VAL A CG1 1 ATOM 422 C CG2 . VAL A 1 53 ? -3.696 5.366 8.896 1.00 15.13 ? 66 VAL A CG2 1 ATOM 423 N N . VAL A 1 54 ? -6.133 9.442 8.712 1.00 12.01 ? 67 VAL A N 1 ATOM 424 C CA . VAL A 1 54 ? -6.631 10.730 9.195 1.00 12.05 ? 67 VAL A CA 1 ATOM 425 C C . VAL A 1 54 ? -7.554 10.526 10.396 1.00 12.40 ? 67 VAL A C 1 ATOM 426 O O . VAL A 1 54 ? -8.579 9.843 10.295 1.00 11.87 ? 67 VAL A O 1 ATOM 427 C CB . VAL A 1 54 ? -7.389 11.473 8.084 1.00 14.61 ? 67 VAL A CB 1 ATOM 428 C CG1 . VAL A 1 54 ? -7.892 12.823 8.582 1.00 16.15 ? 67 VAL A CG1 1 ATOM 429 C CG2 . VAL A 1 54 ? -6.483 11.633 6.873 1.00 16.77 ? 67 VAL A CG2 1 ATOM 430 N N . LEU A 1 55 ? -7.163 11.108 11.531 1.00 12.18 ? 68 LEU A N 1 ATOM 431 C CA . LEU A 1 55 ? -7.931 11.097 12.769 1.00 13.14 ? 68 LEU A CA 1 ATOM 432 C C . LEU A 1 55 ? -8.527 12.486 12.986 1.00 13.35 ? 68 LEU A C 1 ATOM 433 O O . LEU A 1 55 ? -8.048 13.460 12.419 1.00 14.21 ? 68 LEU A O 1 ATOM 434 C CB . LEU A 1 55 ? -7.009 10.749 13.950 1.00 13.71 ? 68 LEU A CB 1 ATOM 435 C CG . LEU A 1 55 ? -6.204 9.450 13.821 1.00 15.05 ? 68 LEU A CG 1 ATOM 436 C CD1 . LEU A 1 55 ? -5.246 9.323 14.999 1.00 17.39 ? 68 LEU A CD1 1 ATOM 437 C CD2 . LEU A 1 55 ? -7.086 8.217 13.691 1.00 15.64 ? 68 LEU A CD2 1 ATOM 438 N N . GLY A 1 56 ? -9.554 12.572 13.811 1.00 12.82 ? 69 GLY A N 1 ATOM 439 C CA . GLY A 1 56 ? -10.157 13.860 14.155 1.00 12.53 ? 69 GLY A CA 1 ATOM 440 C C . GLY A 1 56 ? -10.957 14.524 13.051 1.00 14.86 ? 69 GLY A C 1 ATOM 441 O O . GLY A 1 56 ? -11.232 15.721 13.118 1.00 14.86 ? 69 GLY A O 1 ATOM 442 N N . ALA A 1 57 ? -11.400 13.751 12.063 1.00 12.79 ? 70 ALA A N 1 ATOM 443 C CA . ALA A 1 57 ? -12.088 14.309 10.903 1.00 12.46 ? 70 ALA A CA 1 ATOM 444 C C . ALA A 1 57 ? -13.609 14.245 10.961 1.00 12.80 ? 70 ALA A C 1 ATOM 445 O O . ALA A 1 57 ? -14.205 13.359 11.571 1.00 12.52 ? 70 ALA A O 1 ATOM 446 C CB . ALA A 1 57 ? -11.622 13.595 9.646 1.00 12.84 ? 70 ALA A CB 1 ATOM 447 N N . HIS A 1 58 ? -14.243 15.206 10.295 1.00 13.61 ? 71 HIS A N 1 ATOM 448 C CA . HIS A 1 58 ? -15.647 15.112 9.935 1.00 12.73 ? 71 HIS A CA 1 ATOM 449 C C . HIS A 1 58 ? -15.823 15.232 8.436 1.00 14.49 ? 71 HIS A C 1 ATOM 450 O O . HIS A 1 58 ? -16.313 14.304 7.789 1.00 14.50 ? 71 HIS A O 1 ATOM 451 C CB . HIS A 1 58 ? -16.508 16.142 10.655 1.00 13.84 ? 71 HIS A CB 1 ATOM 452 C CG . HIS A 1 58 ? -17.960 15.898 10.434 1.00 14.40 ? 71 HIS A CG 1 ATOM 453 N ND1 . HIS A 1 58 ? -18.585 14.786 10.871 1.00 14.16 ? 71 HIS A ND1 1 ATOM 454 C CD2 . HIS A 1 58 ? -18.895 16.617 9.712 1.00 15.66 ? 71 HIS A CD2 1 ATOM 455 C CE1 . HIS A 1 58 ? -19.868 14.811 10.467 1.00 15.03 ? 71 HIS A CE1 1 ATOM 456 N NE2 . HIS A 1 58 ? -20.055 15.940 9.763 1.00 16.25 ? 71 HIS A NE2 1 ATOM 457 N N . VAL A 1 59 ? -15.433 16.377 7.877 1.00 14.56 ? 72 VAL A N 1 ATOM 458 C CA . VAL A 1 59 ? -15.399 16.613 6.432 1.00 17.57 ? 72 VAL A CA 1 ATOM 459 C C . VAL A 1 59 ? -13.972 16.380 5.948 1.00 17.25 ? 72 VAL A C 1 ATOM 460 O O . VAL A 1 59 ? -13.050 17.152 6.241 1.00 17.21 ? 72 VAL A O 1 ATOM 461 C CB . VAL A 1 59 ? -15.859 18.042 6.068 1.00 18.52 ? 72 VAL A CB 1 ATOM 462 C CG1 . VAL A 1 59 ? -15.968 18.179 4.546 1.00 19.45 ? 72 VAL A CG1 1 ATOM 463 C CG2 . VAL A 1 59 ? -17.187 18.361 6.738 1.00 19.27 ? 72 VAL A CG2 1 ATOM 464 N N . LEU A 1 60 ? -13.780 15.289 5.216 1.00 16.92 ? 73 LEU A N 1 ATOM 465 C CA . LEU A 1 60 ? -12.436 14.845 4.848 1.00 19.24 ? 73 LEU A CA 1 ATOM 466 C C . LEU A 1 60 ? -11.763 15.728 3.815 1.00 19.92 ? 73 LEU A C 1 ATOM 467 O O . LEU A 1 60 ? -10.539 15.741 3.743 1.00 21.87 ? 73 LEU A O 1 ATOM 468 C CB . LEU A 1 60 ? -12.465 13.399 4.334 1.00 18.92 ? 73 LEU A CB 1 ATOM 469 C CG . LEU A 1 60 ? -12.832 12.313 5.356 1.00 19.86 ? 73 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 60 ? -13.089 11.001 4.616 1.00 18.51 ? 73 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 60 ? -11.741 12.148 6.399 1.00 21.74 ? 73 LEU A CD2 1 ATOM 472 N N . SER A 1 61 ? -12.556 16.461 3.037 1.00 21.49 ? 74 SER A N 1 ATOM 473 C CA . SER A 1 61 ? -12.014 17.311 1.977 1.00 23.56 ? 74 SER A CA 1 ATOM 474 C C . SER A 1 61 ? -11.555 18.675 2.500 1.00 23.92 ? 74 SER A C 1 ATOM 475 O O . SER A 1 61 ? -11.007 19.476 1.743 1.00 29.11 ? 74 SER A O 1 ATOM 476 C CB . SER A 1 61 ? -13.044 17.498 0.852 1.00 24.42 ? 74 SER A CB 1 ATOM 477 O OG . SER A 1 61 ? -14.277 17.971 1.354 1.00 26.51 ? 74 SER A OG 1 ATOM 478 N N . THR A 1 62 ? -11.785 18.936 3.784 1.00 23.61 ? 75 THR A N 1 ATOM 479 C CA . THR A 1 62 ? -11.383 20.186 4.417 1.00 26.00 ? 75 THR A CA 1 ATOM 480 C C . THR A 1 62 ? -10.263 19.916 5.401 1.00 26.65 ? 75 THR A C 1 ATOM 481 O O . THR A 1 62 ? -10.299 18.920 6.121 1.00 21.84 ? 75 THR A O 1 ATOM 482 C CB . THR A 1 62 ? -12.559 20.812 5.187 1.00 26.54 ? 75 THR A CB 1 ATOM 483 O OG1 . THR A 1 62 ? -13.660 21.018 4.296 1.00 29.47 ? 75 THR A OG1 1 ATOM 484 C CG2 . THR A 1 62 ? -12.152 22.148 5.834 1.00 30.61 ? 75 THR A CG2 1 ATOM 485 N N . ALA A 1 63 ? -9.277 20.807 5.438 1.00 27.66 ? 76 ALA A N 1 ATOM 486 C CA . ALA A 1 63 ? -8.189 20.724 6.402 1.00 30.14 ? 76 ALA A CA 1 ATOM 487 C C . ALA A 1 63 ? -8.675 21.236 7.750 1.00 30.31 ? 76 ALA A C 1 ATOM 488 O O . ALA A 1 63 ? -8.354 22.352 8.149 1.00 31.28 ? 76 ALA A O 1 ATOM 489 C CB . ALA A 1 63 ? -6.998 21.544 5.923 1.00 31.73 ? 76 ALA A CB 1 ATOM 490 N N . GLU A 1 64 ? -9.444 20.408 8.452 1.00 22.03 ? 77 GLU A N 1 ATOM 491 C CA . GLU A 1 64 ? -10.092 20.807 9.702 1.00 20.65 ? 77 GLU A CA 1 ATOM 492 C C . GLU A 1 64 ? -9.082 20.913 10.843 1.00 20.95 ? 77 GLU A C 1 ATOM 493 O O . GLU A 1 64 ? -8.160 20.125 10.919 1.00 20.58 ? 77 GLU A O 1 ATOM 494 C CB . GLU A 1 64 ? -11.174 19.790 10.092 1.00 19.57 ? 77 GLU A CB 1 ATOM 495 C CG . GLU A 1 64 ? -12.291 19.630 9.075 1.00 19.84 ? 77 GLU A CG 1 ATOM 496 C CD . GLU A 1 64 ? -13.192 18.456 9.394 1.00 17.03 ? 77 GLU A CD 1 ATOM 497 O OE1 . GLU A 1 64 ? -12.653 17.400 9.773 1.00 17.64 ? 77 GLU A OE1 1 ATOM 498 O OE2 . GLU A 1 64 ? -14.423 18.584 9.271 1.00 17.66 ? 77 GLU A OE2 1 ATOM 499 N N . PRO A 1 65 ? -9.273 21.869 11.759 1.00 19.20 ? 78 PRO A N 1 ATOM 500 C CA . PRO A 1 65 ? -8.283 22.071 12.829 1.00 21.83 ? 78 PRO A CA 1 ATOM 501 C C . PRO A 1 65 ? -8.041 20.871 13.747 1.00 20.06 ? 78 PRO A C 1 ATOM 502 O O . PRO A 1 65 ? -6.954 20.747 14.311 1.00 19.47 ? 78 PRO A O 1 ATOM 503 C CB . PRO A 1 65 ? -8.843 23.265 13.626 1.00 22.56 ? 78 PRO A CB 1 ATOM 504 C CG . PRO A 1 65 ? -10.231 23.483 13.132 1.00 25.15 ? 78 PRO A CG 1 ATOM 505 C CD . PRO A 1 65 ? -10.314 22.911 11.754 1.00 20.81 ? 78 PRO A CD 1 ATOM 506 N N . THR A 1 66 ? -9.039 19.996 13.888 1.00 19.24 ? 79 THR A N 1 ATOM 507 C CA . THR A 1 66 ? -8.914 18.812 14.744 1.00 18.48 ? 79 THR A CA 1 ATOM 508 C C . THR A 1 66 ? -8.270 17.606 14.052 1.00 17.68 ? 79 THR A C 1 ATOM 509 O O . THR A 1 66 ? -8.019 16.599 14.701 1.00 17.34 ? 79 THR A O 1 ATOM 510 C CB . THR A 1 66 ? -10.287 18.369 15.279 1.00 19.08 ? 79 THR A CB 1 ATOM 511 O OG1 . THR A 1 66 ? -11.176 18.164 14.183 1.00 18.91 ? 79 THR A OG1 1 ATOM 512 C CG2 . THR A 1 66 ? -10.869 19.419 16.221 1.00 20.13 ? 79 THR A CG2 1 ATOM 513 N N . GLN A 1 67 ? -7.982 17.705 12.760 1.00 16.15 ? 80 GLN A N 1 ATOM 514 C CA . GLN A 1 67 ? -7.418 16.569 12.049 1.00 15.74 ? 80 GLN A CA 1 ATOM 515 C C . GLN A 1 67 ? -5.971 16.343 12.450 1.00 17.79 ? 80 GLN A C 1 ATOM 516 O O . GLN A 1 67 ? -5.197 17.285 12.599 1.00 19.62 ? 80 GLN A O 1 ATOM 517 C CB . GLN A 1 67 ? -7.547 16.708 10.530 1.00 17.44 ? 80 GLN A CB 1 ATOM 518 C CG . GLN A 1 67 ? -8.929 16.336 10.019 1.00 16.48 ? 80 GLN A CG 1 ATOM 519 C CD . GLN A 1 67 ? -9.127 16.591 8.539 1.00 17.45 ? 80 GLN A CD 1 ATOM 520 O OE1 . GLN A 1 67 ? -8.180 16.541 7.759 1.00 21.14 ? 80 GLN A OE1 1 ATOM 521 N NE2 . GLN A 1 67 ? -10.367 16.844 8.143 1.00 16.12 ? 80 GLN A NE2 1 ATOM 522 N N . GLN A 1 68 ? -5.631 15.076 12.653 1.00 15.24 ? 81 GLN A N 1 ATOM 523 C CA . GLN A 1 68 ? -4.261 14.605 12.876 1.00 14.99 ? 81 GLN A CA 1 ATOM 524 C C . GLN A 1 68 ? -4.010 13.513 11.838 1.00 15.64 ? 81 GLN A C 1 ATOM 525 O O . GLN A 1 68 ? -4.752 12.528 11.755 1.00 15.82 ? 81 GLN A O 1 ATOM 526 C CB . GLN A 1 68 ? -4.050 14.078 14.299 1.00 14.38 ? 81 GLN A CB 1 ATOM 527 C CG . GLN A 1 68 ? -4.400 15.076 15.396 1.00 15.91 ? 81 GLN A CG 1 ATOM 528 C CD . GLN A 1 68 ? -4.141 14.545 16.793 1.00 15.94 ? 81 GLN A CD 1 ATOM 529 O OE1 . GLN A 1 68 ? -3.149 13.848 17.035 1.00 17.19 ? 81 GLN A OE1 1 ATOM 530 N NE2 . GLN A 1 68 ? -5.028 14.883 17.731 1.00 16.53 ? 81 GLN A NE2 1 ATOM 531 N N . VAL A 1 69 ? -2.981 13.705 11.023 1.00 15.71 ? 82 VAL A N 1 ATOM 532 C CA . VAL A 1 69 ? -2.668 12.828 9.908 1.00 16.76 ? 82 VAL A CA 1 ATOM 533 C C . VAL A 1 69 ? -1.355 12.118 10.169 1.00 18.15 ? 82 VAL A C 1 ATOM 534 O O . VAL A 1 69 ? -0.378 12.745 10.585 1.00 20.00 ? 82 VAL A O 1 ATOM 535 C CB . VAL A 1 69 ? -2.573 13.622 8.597 1.00 19.54 ? 82 VAL A CB 1 ATOM 536 C CG1 . VAL A 1 69 ? -2.224 12.703 7.433 1.00 21.06 ? 82 VAL A CG1 1 ATOM 537 C CG2 . VAL A 1 69 ? -3.879 14.369 8.342 1.00 20.54 ? 82 VAL A CG2 1 ATOM 538 N N . PHE A 1 70 ? -1.332 10.813 9.894 1.00 17.00 ? 83 PHE A N 1 ATOM 539 C CA . PHE A 1 70 ? -0.190 9.953 10.158 1.00 15.39 ? 83 PHE A CA 1 ATOM 540 C C . PHE A 1 70 ? 0.101 9.045 8.983 1.00 15.76 ? 83 PHE A C 1 ATOM 541 O O . PHE A 1 70 ? -0.810 8.640 8.242 1.00 16.09 ? 83 PHE A O 1 ATOM 542 C CB . PHE A 1 70 ? -0.484 9.066 11.361 1.00 16.85 ? 83 PHE A CB 1 ATOM 543 C CG . PHE A 1 70 ? -0.549 9.826 12.641 1.00 16.07 ? 83 PHE A CG 1 ATOM 544 C CD1 . PHE A 1 70 ? 0.614 10.170 13.307 1.00 16.93 ? 83 PHE A CD1 1 ATOM 545 C CD2 . PHE A 1 70 ? -1.768 10.231 13.156 1.00 16.75 ? 83 PHE A CD2 1 ATOM 546 C CE1 . PHE A 1 70 ? 0.571 10.892 14.487 1.00 17.98 ? 83 PHE A CE1 1 ATOM 547 C CE2 . PHE A 1 70 ? -1.811 10.984 14.324 1.00 16.25 ? 83 PHE A CE2 1 ATOM 548 C CZ . PHE A 1 70 ? -0.643 11.298 14.996 1.00 19.08 ? 83 PHE A CZ 1 ATOM 549 N N . GLY A 1 71 ? 1.379 8.721 8.818 1.00 15.98 ? 84 GLY A N 1 ATOM 550 C CA . GLY A 1 71 ? 1.769 7.634 7.938 1.00 17.50 ? 84 GLY A CA 1 ATOM 551 C C . GLY A 1 71 ? 1.654 6.292 8.634 1.00 16.66 ? 84 GLY A C 1 ATOM 552 O O . GLY A 1 71 ? 1.455 6.208 9.860 1.00 16.55 ? 84 GLY A O 1 ATOM 553 N N . ILE A 1 72 ? 1.774 5.229 7.843 1.00 18.07 ? 85 ILE A N 1 ATOM 554 C CA . ILE A 1 72 ? 1.701 3.874 8.365 1.00 18.44 ? 85 ILE A CA 1 ATOM 555 C C . ILE A 1 72 ? 3.112 3.291 8.477 1.00 19.38 ? 85 ILE A C 1 ATOM 556 O O . ILE A 1 72 ? 3.751 2.995 7.463 1.00 20.89 ? 85 ILE A O 1 ATOM 557 C CB . ILE A 1 72 ? 0.818 2.994 7.467 1.00 19.45 ? 85 ILE A CB 1 ATOM 558 C CG1 . ILE A 1 72 ? -0.590 3.596 7.367 1.00 19.46 ? 85 ILE A CG1 1 ATOM 559 C CG2 . ILE A 1 72 ? 0.746 1.579 8.037 1.00 20.91 ? 85 ILE A CG2 1 ATOM 560 C CD1 . ILE A 1 72 ? -1.392 3.107 6.187 1.00 20.91 ? 85 ILE A CD1 1 ATOM 561 N N . ASP A 1 73 ? 3.608 3.167 9.704 1.00 18.09 ? 86 ASP A N 1 ATOM 562 C CA . ASP A 1 73 ? 4.905 2.535 9.967 1.00 20.13 ? 86 ASP A CA 1 ATOM 563 C C . ASP A 1 73 ? 4.896 1.045 9.608 1.00 22.18 ? 86 ASP A C 1 ATOM 564 O O . ASP A 1 73 ? 5.856 0.531 9.027 1.00 21.80 ? 86 ASP A O 1 ATOM 565 C CB . ASP A 1 73 ? 5.268 2.696 11.454 1.00 25.82 ? 86 ASP A CB 1 ATOM 566 C CG . ASP A 1 73 ? 6.633 3.309 11.666 1.00 35.63 ? 86 ASP A CG 1 ATOM 567 O OD1 . ASP A 1 73 ? 7.394 2.768 12.494 1.00 55.78 ? 86 ASP A OD1 1 ATOM 568 O OD2 . ASP A 1 73 ? 6.933 4.333 11.015 1.00 35.59 ? 86 ASP A OD2 1 ATOM 569 N N . ALA A 1 74 ? 3.817 0.346 9.959 1.00 17.44 ? 87 ALA A N 1 ATOM 570 C CA . ALA A 1 74 ? 3.723 -1.095 9.727 1.00 16.24 ? 87 ALA A CA 1 ATOM 571 C C . ALA A 1 74 ? 2.283 -1.547 9.620 1.00 15.92 ? 87 ALA A C 1 ATOM 572 O O . ALA A 1 74 ? 1.449 -1.217 10.467 1.00 17.05 ? 87 ALA A O 1 ATOM 573 C CB . ALA A 1 74 ? 4.401 -1.865 10.846 1.00 17.66 ? 87 ALA A CB 1 ATOM 574 N N . LEU A 1 75 ? 2.006 -2.315 8.572 1.00 16.95 ? 88 LEU A N 1 ATOM 575 C CA . LEU A 1 75 ? 0.746 -3.018 8.383 1.00 15.85 ? 88 LEU A CA 1 ATOM 576 C C . LEU A 1 75 ? 0.933 -4.466 8.786 1.00 15.80 ? 88 LEU A C 1 ATOM 577 O O . LEU A 1 75 ? 1.868 -5.121 8.300 1.00 17.35 ? 88 LEU A O 1 ATOM 578 C CB . LEU A 1 75 ? 0.343 -2.994 6.913 1.00 15.74 ? 88 LEU A CB 1 ATOM 579 C CG . LEU A 1 75 ? -0.746 -3.951 6.452 1.00 15.38 ? 88 LEU A CG 1 ATOM 580 C CD1 . LEU A 1 75 ? -2.094 -3.602 7.066 1.00 17.36 ? 88 LEU A CD1 1 ATOM 581 C CD2 . LEU A 1 75 ? -0.824 -3.888 4.934 1.00 15.85 ? 88 LEU A CD2 1 ATOM 582 N N . THR A 1 76 ? 0.043 -4.986 9.630 1.00 16.28 ? 89 THR A N 1 ATOM 583 C CA . THR A 1 76 ? 0.021 -6.409 9.968 1.00 15.67 ? 89 THR A CA 1 ATOM 584 C C . THR A 1 76 ? -1.342 -6.949 9.598 1.00 15.20 ? 89 THR A C 1 ATOM 585 O O . THR A 1 76 ? -2.338 -6.633 10.234 1.00 14.73 ? 89 THR A O 1 ATOM 586 C CB . THR A 1 76 ? 0.281 -6.680 11.464 1.00 16.57 ? 89 THR A CB 1 ATOM 587 O OG1 . THR A 1 76 ? 1.512 -6.061 11.852 1.00 16.68 ? 89 THR A OG1 1 ATOM 588 C CG2 . THR A 1 76 ? 0.350 -8.186 11.761 1.00 15.93 ? 89 THR A CG2 1 ATOM 589 N N . THR A 1 77 ? -1.385 -7.740 8.539 1.00 18.30 ? 90 THR A N 1 ATOM 590 C CA . THR A 1 77 ? -2.591 -8.398 8.094 1.00 18.31 ? 90 THR A CA 1 ATOM 591 C C . THR A 1 77 ? -2.733 -9.696 8.869 1.00 17.90 ? 90 THR A C 1 ATOM 592 O O . THR A 1 77 ? -1.731 -10.344 9.182 1.00 19.70 ? 90 THR A O 1 ATOM 593 C CB . THR A 1 77 ? -2.515 -8.646 6.574 1.00 19.68 ? 90 THR A CB 1 ATOM 594 O OG1 . THR A 1 77 ? -2.465 -7.382 5.892 1.00 20.45 ? 90 THR A OG1 1 ATOM 595 C CG2 . THR A 1 77 ? -3.704 -9.440 6.083 1.00 18.17 ? 90 THR A CG2 1 ATOM 596 N N . HIS A 1 78 ? -3.970 -10.079 9.192 1.00 16.29 ? 91 HIS A N 1 ATOM 597 C CA . HIS A 1 78 ? -4.190 -11.325 9.896 1.00 17.53 ? 91 HIS A CA 1 ATOM 598 C C . HIS A 1 78 ? -3.490 -12.440 9.153 1.00 18.20 ? 91 HIS A C 1 ATOM 599 O O . HIS A 1 78 ? -3.595 -12.500 7.915 1.00 18.50 ? 91 HIS A O 1 ATOM 600 C CB . HIS A 1 78 ? -5.661 -11.656 10.029 1.00 17.08 ? 91 HIS A CB 1 ATOM 601 C CG . HIS A 1 78 ? -5.914 -12.744 11.036 1.00 15.95 ? 91 HIS A CG 1 ATOM 602 N ND1 . HIS A 1 78 ? -5.840 -14.059 10.724 1.00 16.26 ? 91 HIS A ND1 1 ATOM 603 C CD2 . HIS A 1 78 ? -6.140 -12.676 12.401 1.00 19.21 ? 91 HIS A CD2 1 ATOM 604 C CE1 . HIS A 1 78 ? -6.046 -14.785 11.836 1.00 16.97 ? 91 HIS A CE1 1 ATOM 605 N NE2 . HIS A 1 78 ? -6.227 -13.936 12.860 1.00 18.73 ? 91 HIS A NE2 1 ATOM 606 N N . PRO A 1 79 ? -2.776 -13.324 9.891 1.00 17.34 ? 92 PRO A N 1 ATOM 607 C CA . PRO A 1 79 ? -2.008 -14.369 9.204 1.00 20.46 ? 92 PRO A CA 1 ATOM 608 C C . PRO A 1 79 ? -2.874 -15.333 8.384 1.00 19.66 ? 92 PRO A C 1 ATOM 609 O O . PRO A 1 79 ? -2.356 -15.959 7.449 1.00 20.32 ? 92 PRO A O 1 ATOM 610 C CB . PRO A 1 79 ? -1.279 -15.099 10.341 1.00 23.46 ? 92 PRO A CB 1 ATOM 611 C CG . PRO A 1 79 ? -1.945 -14.692 11.606 1.00 22.25 ? 92 PRO A CG 1 ATOM 612 C CD . PRO A 1 79 ? -2.557 -13.350 11.350 1.00 18.58 ? 92 PRO A CD 1 ATOM 613 N N . ASP A 1 80 ? -4.162 -15.445 8.704 1.00 18.60 ? 93 ASP A N 1 ATOM 614 C CA . ASP A 1 80 ? -5.058 -16.350 7.975 1.00 19.62 ? 93 ASP A CA 1 ATOM 615 C C . ASP A 1 80 ? -5.900 -15.656 6.902 1.00 21.00 ? 93 ASP A C 1 ATOM 616 O O . ASP A 1 80 ? -6.765 -16.283 6.284 1.00 19.68 ? 93 ASP A O 1 ATOM 617 C CB . ASP A 1 80 ? -5.964 -17.105 8.958 1.00 25.27 ? 93 ASP A CB 1 ATOM 618 C CG . ASP A 1 80 ? -5.177 -17.962 9.954 1.00 26.45 ? 93 ASP A CG 1 ATOM 619 O OD1 . ASP A 1 80 ? -4.118 -18.524 9.593 1.00 29.76 ? 93 ASP A OD1 1 ATOM 620 O OD2 . ASP A 1 80 ? -5.631 -18.085 11.109 1.00 26.54 ? 93 ASP A OD2 1 ATOM 621 N N . TYR A 1 81 ? -5.673 -14.362 6.677 1.00 17.39 ? 94 TYR A N 1 ATOM 622 C CA . TYR A 1 81 ? -6.322 -13.683 5.572 1.00 17.47 ? 94 TYR A CA 1 ATOM 623 C C . TYR A 1 81 ? -5.693 -14.186 4.277 1.00 18.07 ? 94 TYR A C 1 ATOM 624 O O . TYR A 1 81 ? -4.467 -14.261 4.170 1.00 19.21 ? 94 TYR A O 1 ATOM 625 C CB . TYR A 1 81 ? -6.192 -12.152 5.674 1.00 16.20 ? 94 TYR A CB 1 ATOM 626 C CG . TYR A 1 81 ? -6.904 -11.420 4.570 1.00 14.20 ? 94 TYR A CG 1 ATOM 627 C CD1 . TYR A 1 81 ? -8.289 -11.397 4.518 1.00 16.98 ? 94 TYR A CD1 1 ATOM 628 C CD2 . TYR A 1 81 ? -6.201 -10.781 3.541 1.00 18.47 ? 94 TYR A CD2 1 ATOM 629 C CE1 . TYR A 1 81 ? -8.966 -10.739 3.510 1.00 18.24 ? 94 TYR A CE1 1 ATOM 630 C CE2 . TYR A 1 81 ? -6.874 -10.129 2.515 1.00 18.23 ? 94 TYR A CE2 1 ATOM 631 C CZ . TYR A 1 81 ? -8.253 -10.110 2.510 1.00 20.79 ? 94 TYR A CZ 1 ATOM 632 O OH . TYR A 1 81 ? -8.937 -9.466 1.505 1.00 23.87 ? 94 TYR A OH 1 ATOM 633 N N . HIS A 1 82 ? -6.538 -14.508 3.306 1.00 16.89 ? 95 HIS A N 1 ATOM 634 C CA . HIS A 1 82 ? -6.084 -15.156 2.071 1.00 19.93 ? 95 HIS A CA 1 ATOM 635 C C . HIS A 1 82 ? -7.045 -14.882 0.938 1.00 28.04 ? 95 HIS A C 1 ATOM 636 O O . HIS A 1 82 ? -8.229 -14.677 1.174 1.00 28.75 ? 95 HIS A O 1 ATOM 637 C CB . HIS A 1 82 ? -5.981 -16.663 2.319 1.00 20.25 ? 95 HIS A CB 1 ATOM 638 C CG . HIS A 1 82 ? -5.291 -17.426 1.209 1.00 21.92 ? 95 HIS A CG 1 ATOM 639 N ND1 . HIS A 1 82 ? -5.896 -17.699 0.037 1.00 28.71 ? 95 HIS A ND1 1 ATOM 640 C CD2 . HIS A 1 82 ? -4.013 -17.974 1.130 1.00 20.55 ? 95 HIS A CD2 1 ATOM 641 C CE1 . HIS A 1 82 ? -5.044 -18.384 -0.760 1.00 29.67 ? 95 HIS A CE1 1 ATOM 642 N NE2 . HIS A 1 82 ? -3.893 -18.549 -0.091 1.00 24.98 ? 95 HIS A NE2 1 ATOM 643 N N . PRO A 1 83 ? -6.557 -14.867 -0.319 1.00 36.47 ? 96 PRO A N 1 ATOM 644 C CA . PRO A 1 83 ? -7.500 -14.930 -1.449 1.00 31.71 ? 96 PRO A CA 1 ATOM 645 C C . PRO A 1 83 ? -8.327 -16.219 -1.432 1.00 44.03 ? 96 PRO A C 1 ATOM 646 O O . PRO A 1 83 ? -8.130 -17.066 -0.560 1.00 55.58 ? 96 PRO A O 1 ATOM 647 C CB . PRO A 1 83 ? -6.583 -14.894 -2.675 1.00 37.93 ? 96 PRO A CB 1 ATOM 648 C CG . PRO A 1 83 ? -5.356 -14.190 -2.205 1.00 39.65 ? 96 PRO A CG 1 ATOM 649 C CD . PRO A 1 83 ? -5.181 -14.576 -0.762 1.00 36.28 ? 96 PRO A CD 1 ATOM 650 N N . MET A 1 84 ? -9.262 -16.352 -2.366 1.00 54.30 ? 97 MET A N 1 ATOM 651 C CA . MET A 1 84 ? -10.172 -17.509 -2.418 1.00 64.39 ? 97 MET A CA 1 ATOM 652 C C . MET A 1 84 ? -10.945 -17.773 -1.105 1.00 63.04 ? 97 MET A C 1 ATOM 653 O O . MET A 1 84 ? -11.630 -18.792 -0.983 1.00 79.84 ? 97 MET A O 1 ATOM 654 C CB . MET A 1 84 ? -9.438 -18.781 -2.923 1.00 83.80 ? 97 MET A CB 1 ATOM 655 C CG . MET A 1 84 ? -8.654 -19.602 -1.896 1.00 77.22 ? 97 MET A CG 1 ATOM 656 S SD . MET A 1 84 ? -7.898 -21.091 -2.590 1.00 83.46 ? 97 MET A SD 1 ATOM 657 C CE . MET A 1 84 ? -6.605 -20.388 -3.615 1.00 65.65 ? 97 MET A CE 1 ATOM 658 N N . THR A 1 85 ? -10.845 -16.855 -0.142 1.00 49.32 ? 98 THR A N 1 ATOM 659 C CA . THR A 1 85 ? -11.663 -16.896 1.070 1.00 41.70 ? 98 THR A CA 1 ATOM 660 C C . THR A 1 85 ? -11.894 -15.477 1.600 1.00 28.73 ? 98 THR A C 1 ATOM 661 O O . THR A 1 85 ? -11.091 -14.568 1.373 1.00 26.31 ? 98 THR A O 1 ATOM 662 C CB . THR A 1 85 ? -11.054 -17.786 2.170 1.00 45.02 ? 98 THR A CB 1 ATOM 663 O OG1 . THR A 1 85 ? -11.906 -17.769 3.326 1.00 49.60 ? 98 THR A OG1 1 ATOM 664 C CG2 . THR A 1 85 ? -9.666 -17.303 2.556 1.00 42.16 ? 98 THR A CG2 1 ATOM 665 N N . HIS A 1 86 ? -12.992 -15.310 2.323 1.00 26.38 ? 99 HIS A N 1 ATOM 666 C CA A HIS A 1 86 ? -13.456 -13.989 2.746 0.50 24.09 ? 99 HIS A CA 1 ATOM 667 C CA B HIS A 1 86 ? -13.435 -13.981 2.744 0.50 26.66 ? 99 HIS A CA 1 ATOM 668 C C . HIS A 1 86 ? -13.226 -13.736 4.214 1.00 21.37 ? 99 HIS A C 1 ATOM 669 O O . HIS A 1 86 ? -13.333 -12.608 4.669 1.00 21.17 ? 99 HIS A O 1 ATOM 670 C CB A HIS A 1 86 ? -14.933 -13.783 2.360 0.50 28.44 ? 99 HIS A CB 1 ATOM 671 C CB B HIS A 1 86 ? -14.900 -13.766 2.368 0.50 35.91 ? 99 HIS A CB 1 ATOM 672 C CG A HIS A 1 86 ? -15.799 -15.028 2.492 0.50 27.53 ? 99 HIS A CG 1 ATOM 673 C CG B HIS A 1 86 ? -15.181 -13.921 0.886 0.50 39.30 ? 99 HIS A CG 1 ATOM 674 N ND1 A HIS A 1 86 ? -15.566 -16.157 1.792 0.50 29.87 ? 99 HIS A ND1 1 ATOM 675 N ND1 B HIS A 1 86 ? -14.773 -13.020 -0.026 0.50 45.94 ? 99 HIS A ND1 1 ATOM 676 C CD2 A HIS A 1 86 ? -16.939 -15.272 3.257 0.50 30.33 ? 99 HIS A CD2 1 ATOM 677 C CD2 B HIS A 1 86 ? -15.861 -14.915 0.180 0.50 46.25 ? 99 HIS A CD2 1 ATOM 678 C CE1 A HIS A 1 86 ? -16.492 -17.082 2.111 0.50 31.12 ? 99 HIS A CE1 1 ATOM 679 C CE1 B HIS A 1 86 ? -15.164 -13.417 -1.254 0.50 47.04 ? 99 HIS A CE1 1 ATOM 680 N NE2 A HIS A 1 86 ? -17.334 -16.537 3.005 0.50 29.29 ? 99 HIS A NE2 1 ATOM 681 N NE2 B HIS A 1 86 ? -15.829 -14.575 -1.125 0.50 48.98 ? 99 HIS A NE2 1 ATOM 682 N N . ALA A 1 87 ? -12.882 -14.773 4.968 1.00 17.95 ? 100 ALA A N 1 ATOM 683 C CA . ALA A 1 87 ? -12.687 -14.671 6.416 1.00 18.93 ? 100 ALA A CA 1 ATOM 684 C C . ALA A 1 87 ? -11.411 -13.926 6.818 1.00 16.63 ? 100 ALA A C 1 ATOM 685 O O . ALA A 1 87 ? -10.512 -13.666 5.999 1.00 17.28 ? 100 ALA A O 1 ATOM 686 C CB . ALA A 1 87 ? -12.690 -16.069 7.038 1.00 21.36 ? 100 ALA A CB 1 ATOM 687 N N . ASN A 1 88 ? -11.360 -13.566 8.092 1.00 16.32 ? 101 ASN A N 1 ATOM 688 C CA . ASN A 1 88 ? -10.174 -12.966 8.691 1.00 15.75 ? 101 ASN A CA 1 ATOM 689 C C . ASN A 1 88 ? -9.804 -11.626 8.075 1.00 13.57 ? 101 ASN A C 1 ATOM 690 O O . ASN A 1 88 ? -8.629 -11.307 7.962 1.00 15.48 ? 101 ASN A O 1 ATOM 691 C CB . ASN A 1 88 ? -8.995 -13.931 8.631 1.00 17.50 ? 101 ASN A CB 1 ATOM 692 C CG . ASN A 1 88 ? -9.368 -15.320 9.111 1.00 17.39 ? 101 ASN A CG 1 ATOM 693 O OD1 . ASN A 1 88 ? -9.797 -15.496 10.248 1.00 18.16 ? 101 ASN A OD1 1 ATOM 694 N ND2 . ASN A 1 88 ? -9.214 -16.317 8.237 1.00 18.99 ? 101 ASN A ND2 1 ATOM 695 N N . ASP A 1 89 ? -10.835 -10.858 7.713 1.00 13.13 ? 102 ASP A N 1 ATOM 696 C CA . ASP A 1 89 ? -10.665 -9.588 7.014 1.00 14.50 ? 102 ASP A CA 1 ATOM 697 C C . ASP A 1 89 ? -10.325 -8.438 7.979 1.00 13.23 ? 102 ASP A C 1 ATOM 698 O O . ASP A 1 89 ? -11.095 -7.504 8.141 1.00 17.06 ? 102 ASP A O 1 ATOM 699 C CB . ASP A 1 89 ? -11.925 -9.272 6.212 1.00 13.66 ? 102 ASP A CB 1 ATOM 700 C CG . ASP A 1 89 ? -11.742 -8.093 5.288 1.00 12.83 ? 102 ASP A CG 1 ATOM 701 O OD1 . ASP A 1 89 ? -10.580 -7.656 5.102 1.00 14.49 ? 102 ASP A OD1 1 ATOM 702 O OD2 . ASP A 1 89 ? -12.737 -7.562 4.776 1.00 12.28 ? 102 ASP A OD2 1 ATOM 703 N N . ILE A 1 90 ? -9.159 -8.521 8.598 1.00 12.01 ? 103 ILE A N 1 ATOM 704 C CA . ILE A 1 90 ? -8.785 -7.611 9.685 1.00 12.72 ? 103 ILE A CA 1 ATOM 705 C C . ILE A 1 90 ? -7.276 -7.403 9.660 1.00 12.02 ? 103 ILE A C 1 ATOM 706 O O . ILE A 1 90 ? -6.487 -8.316 9.311 1.00 13.86 ? 103 ILE A O 1 ATOM 707 C CB . ILE A 1 90 ? -9.284 -8.136 11.060 1.00 13.47 ? 103 ILE A CB 1 ATOM 708 C CG1 . ILE A 1 90 ? -8.999 -7.120 12.171 1.00 13.23 ? 103 ILE A CG1 1 ATOM 709 C CG2 . ILE A 1 90 ? -8.698 -9.521 11.381 1.00 13.53 ? 103 ILE A CG2 1 ATOM 710 C CD1 . ILE A 1 90 ? -9.792 -7.388 13.436 1.00 18.54 ? 103 ILE A CD1 1 ATOM 711 N N . CYS A 1 91 ? -6.853 -6.199 10.010 1.00 12.72 ? 104 CYS A N 1 ATOM 712 C CA . CYS A 1 91 ? -5.451 -5.848 10.059 1.00 13.55 ? 104 CYS A CA 1 ATOM 713 C C . CYS A 1 91 ? -5.226 -4.758 11.092 1.00 13.04 ? 104 CYS A C 1 ATOM 714 O O . CYS A 1 91 ? -6.187 -4.124 11.554 1.00 12.63 ? 104 CYS A O 1 ATOM 715 C CB . CYS A 1 91 ? -4.966 -5.378 8.687 1.00 14.87 ? 104 CYS A CB 1 ATOM 716 S SG . CYS A 1 91 ? -5.728 -3.853 8.103 1.00 14.07 ? 104 CYS A SG 1 ATOM 717 N N . LEU A 1 92 ? -3.966 -4.553 11.453 1.00 12.32 ? 105 LEU A N 1 ATOM 718 C CA . LEU A 1 92 ? -3.539 -3.499 12.360 1.00 13.49 ? 105 LEU A CA 1 ATOM 719 C C . LEU A 1 92 ? -2.602 -2.581 11.603 1.00 13.98 ? 105 LEU A C 1 ATOM 720 O O . LEU A 1 92 ? -1.754 -3.037 10.813 1.00 14.19 ? 105 LEU A O 1 ATOM 721 C CB . LEU A 1 92 ? -2.799 -4.090 13.565 1.00 13.43 ? 105 LEU A CB 1 ATOM 722 C CG . LEU A 1 92 ? -3.670 -4.590 14.718 1.00 16.70 ? 105 LEU A CG 1 ATOM 723 C CD1 . LEU A 1 92 ? -2.919 -5.540 15.636 1.00 21.23 ? 105 LEU A CD1 1 ATOM 724 C CD2 . LEU A 1 92 ? -4.229 -3.427 15.531 1.00 18.12 ? 105 LEU A CD2 1 ATOM 725 N N . LEU A 1 93 ? -2.730 -1.290 11.873 1.00 13.24 ? 106 LEU A N 1 ATOM 726 C CA . LEU A 1 93 ? -1.849 -0.268 11.365 1.00 13.77 ? 106 LEU A CA 1 ATOM 727 C C . LEU A 1 93 ? -1.117 0.349 12.547 1.00 15.35 ? 106 LEU A C 1 ATOM 728 O O . LEU A 1 93 ? -1.751 0.920 13.444 1.00 14.38 ? 106 LEU A O 1 ATOM 729 C CB . LEU A 1 93 ? -2.660 0.815 10.641 1.00 13.50 ? 106 LEU A CB 1 ATOM 730 C CG . LEU A 1 93 ? -3.644 0.365 9.571 1.00 14.78 ? 106 LEU A CG 1 ATOM 731 C CD1 . LEU A 1 93 ? -4.417 1.571 9.044 1.00 14.55 ? 106 LEU A CD1 1 ATOM 732 C CD2 . LEU A 1 93 ? -2.934 -0.394 8.459 1.00 16.36 ? 106 LEU A CD2 1 ATOM 733 N N . ARG A 1 94 ? 0.213 0.235 12.551 1.00 13.88 ? 107 ARG A N 1 ATOM 734 C CA A ARG A 1 94 ? 1.046 0.937 13.516 0.50 14.60 ? 107 ARG A CA 1 ATOM 735 C CA B ARG A 1 94 ? 1.043 0.941 13.514 0.50 14.78 ? 107 ARG A CA 1 ATOM 736 C C . ARG A 1 94 ? 1.397 2.270 12.870 1.00 15.48 ? 107 ARG A C 1 ATOM 737 O O . ARG A 1 94 ? 2.024 2.298 11.821 1.00 16.90 ? 107 ARG A O 1 ATOM 738 C CB A ARG A 1 94 ? 2.322 0.143 13.847 0.50 18.30 ? 107 ARG A CB 1 ATOM 739 C CB B ARG A 1 94 ? 2.322 0.162 13.850 0.50 18.93 ? 107 ARG A CB 1 ATOM 740 C CG A ARG A 1 94 ? 3.130 0.755 14.981 0.50 19.39 ? 107 ARG A CG 1 ATOM 741 C CG B ARG A 1 94 ? 3.221 0.913 14.817 0.50 20.94 ? 107 ARG A CG 1 ATOM 742 C CD A ARG A 1 94 ? 4.376 -0.052 15.333 0.50 21.49 ? 107 ARG A CD 1 ATOM 743 C CD B ARG A 1 94 ? 4.288 0.033 15.446 0.50 22.50 ? 107 ARG A CD 1 ATOM 744 N NE A ARG A 1 94 ? 5.494 0.172 14.419 0.50 24.41 ? 107 ARG A NE 1 ATOM 745 N NE B ARG A 1 94 ? 4.579 0.480 16.803 0.50 25.22 ? 107 ARG A NE 1 ATOM 746 C CZ A ARG A 1 94 ? 6.248 -0.794 13.894 0.50 26.95 ? 107 ARG A CZ 1 ATOM 747 C CZ B ARG A 1 94 ? 5.582 1.286 17.131 0.50 28.69 ? 107 ARG A CZ 1 ATOM 748 N NH1 A ARG A 1 94 ? 6.011 -2.065 14.191 0.50 28.20 ? 107 ARG A NH1 1 ATOM 749 N NH1 B ARG A 1 94 ? 6.414 1.726 16.199 0.50 34.57 ? 107 ARG A NH1 1 ATOM 750 N NH2 A ARG A 1 94 ? 7.247 -0.490 13.080 0.50 26.96 ? 107 ARG A NH2 1 ATOM 751 N NH2 B ARG A 1 94 ? 5.752 1.648 18.393 0.50 28.67 ? 107 ARG A NH2 1 ATOM 752 N N . LEU A 1 95 ? 0.976 3.360 13.493 1.00 14.87 ? 108 LEU A N 1 ATOM 753 C CA . LEU A 1 95 ? 1.178 4.683 12.919 1.00 14.19 ? 108 LEU A CA 1 ATOM 754 C C . LEU A 1 95 ? 2.613 5.144 13.150 1.00 16.04 ? 108 LEU A C 1 ATOM 755 O O . LEU A 1 95 ? 3.280 4.679 14.082 1.00 16.95 ? 108 LEU A O 1 ATOM 756 C CB . LEU A 1 95 ? 0.201 5.676 13.550 1.00 13.36 ? 108 LEU A CB 1 ATOM 757 C CG . LEU A 1 95 ? -1.291 5.319 13.533 1.00 14.04 ? 108 LEU A CG 1 ATOM 758 C CD1 . LEU A 1 95 ? -2.172 6.416 14.131 1.00 16.56 ? 108 LEU A CD1 1 ATOM 759 C CD2 . LEU A 1 95 ? -1.738 4.976 12.118 1.00 15.51 ? 108 LEU A CD2 1 ATOM 760 N N . ASN A 1 96 ? 3.076 6.080 12.324 1.00 17.02 ? 109 ASN A N 1 ATOM 761 C CA . ASN A 1 96 ? 4.447 6.631 12.474 1.00 17.88 ? 109 ASN A CA 1 ATOM 762 C C . ASN A 1 96 ? 4.545 7.775 13.493 1.00 19.38 ? 109 ASN A C 1 ATOM 763 O O . ASN A 1 96 ? 5.494 8.555 13.489 1.00 21.77 ? 109 ASN A O 1 ATOM 764 C CB . ASN A 1 96 ? 5.057 7.033 11.124 1.00 20.54 ? 109 ASN A CB 1 ATOM 765 C CG . ASN A 1 96 ? 4.426 8.265 10.522 1.00 21.43 ? 109 ASN A CG 1 ATOM 766 O OD1 . ASN A 1 96 ? 3.334 8.693 10.915 1.00 21.98 ? 109 ASN A OD1 1 ATOM 767 N ND2 . ASN A 1 96 ? 5.134 8.851 9.537 1.00 26.01 ? 109 ASN A ND2 1 ATOM 768 N N . GLY A 1 97 ? 3.569 7.836 14.385 1.00 19.43 ? 110 GLY A N 1 ATOM 769 C CA . GLY A 1 97 ? 3.526 8.815 15.441 1.00 19.52 ? 110 GLY A CA 1 ATOM 770 C C . GLY A 1 97 ? 2.357 8.444 16.321 1.00 17.99 ? 110 GLY A C 1 ATOM 771 O O . GLY A 1 97 ? 1.606 7.522 16.000 1.00 19.81 ? 110 GLY A O 1 ATOM 772 N N . SER A 1 98 ? 2.211 9.135 17.437 1.00 17.37 ? 111 SER A N 1 ATOM 773 C CA . SER A 1 98 ? 1.151 8.876 18.400 1.00 18.44 ? 111 SER A CA 1 ATOM 774 C C . SER A 1 98 ? 0.134 10.012 18.364 1.00 19.54 ? 111 SER A C 1 ATOM 775 O O . SER A 1 98 ? 0.487 11.182 18.467 1.00 18.76 ? 111 SER A O 1 ATOM 776 C CB . SER A 1 98 ? 1.738 8.726 19.811 1.00 18.99 ? 111 SER A CB 1 ATOM 777 O OG . SER A 1 98 ? 2.466 7.517 19.920 1.00 23.09 ? 111 SER A OG 1 ATOM 778 N N . ALA A 1 99 ? -1.139 9.669 18.224 1.00 17.43 ? 112 ALA A N 1 ATOM 779 C CA . ALA A 1 99 ? -2.202 10.652 18.297 1.00 16.43 ? 112 ALA A CA 1 ATOM 780 C C . ALA A 1 99 ? -2.189 11.348 19.655 1.00 17.85 ? 112 ALA A C 1 ATOM 781 O O . ALA A 1 99 ? -1.919 10.713 20.678 1.00 18.73 ? 112 ALA A O 1 ATOM 782 C CB . ALA A 1 99 ? -3.539 9.973 18.089 1.00 17.16 ? 112 ALA A CB 1 ATOM 783 N N . VAL A 1 100 ? -2.476 12.647 19.659 1.00 18.10 ? 113 VAL A N 1 ATOM 784 C CA . VAL A 1 100 ? -2.712 13.384 20.890 1.00 17.78 ? 113 VAL A CA 1 ATOM 785 C C . VAL A 1 100 ? -4.215 13.286 21.148 1.00 15.74 ? 113 VAL A C 1 ATOM 786 O O . VAL A 1 100 ? -5.009 13.819 20.382 1.00 16.76 ? 113 VAL A O 1 ATOM 787 C CB . VAL A 1 100 ? -2.288 14.858 20.769 1.00 17.43 ? 113 VAL A CB 1 ATOM 788 C CG1 . VAL A 1 100 ? -2.610 15.602 22.061 1.00 20.21 ? 113 VAL A CG1 1 ATOM 789 C CG2 . VAL A 1 100 ? -0.809 14.977 20.445 1.00 19.65 ? 113 VAL A CG2 1 ATOM 790 N N . LEU A 1 101 ? -4.588 12.584 22.211 1.00 16.59 ? 114 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? -5.983 12.342 22.499 1.00 18.46 ? 114 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? -6.647 13.597 23.049 1.00 18.04 ? 114 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? -6.035 14.366 23.813 1.00 18.52 ? 114 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? -6.137 11.171 23.462 1.00 17.19 ? 114 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? -5.465 9.877 23.003 1.00 17.65 ? 114 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? -5.764 8.782 24.022 1.00 19.90 ? 114 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? -5.909 9.453 21.603 1.00 16.89 ? 114 LEU A CD2 1 ATOM 798 N N . GLY A 1 102 ? -7.891 13.813 22.648 1.00 17.57 ? 115 GLY A N 1 ATOM 799 C CA . GLY A 1 102 ? -8.635 15.011 23.014 1.00 18.61 ? 115 GLY A CA 1 ATOM 800 C C . GLY A 1 102 ? -10.085 14.887 22.599 1.00 19.06 ? 115 GLY A C 1 ATOM 801 O O . GLY A 1 102 ? -10.537 13.793 22.240 1.00 17.64 ? 115 GLY A O 1 ATOM 802 N N . PRO A 1 103 ? -10.819 16.010 22.591 1.00 19.46 ? 116 PRO A N 1 ATOM 803 C CA . PRO A 1 103 ? -12.258 15.973 22.311 1.00 21.19 ? 116 PRO A CA 1 ATOM 804 C C . PRO A 1 103 ? -12.625 15.323 20.972 1.00 20.50 ? 116 PRO A C 1 ATOM 805 O O . PRO A 1 103 ? -13.684 14.711 20.854 1.00 21.14 ? 116 PRO A O 1 ATOM 806 C CB . PRO A 1 103 ? -12.649 17.454 22.309 1.00 23.08 ? 116 PRO A CB 1 ATOM 807 C CG . PRO A 1 103 ? -11.642 18.115 23.189 1.00 26.41 ? 116 PRO A CG 1 ATOM 808 C CD . PRO A 1 103 ? -10.365 17.356 23.001 1.00 20.70 ? 116 PRO A CD 1 ATOM 809 N N . ALA A 1 104 ? -11.748 15.452 19.983 1.00 16.45 ? 117 ALA A N 1 ATOM 810 C CA . ALA A 1 104 ? -12.020 14.936 18.644 1.00 15.19 ? 117 ALA A CA 1 ATOM 811 C C . ALA A 1 104 ? -11.275 13.644 18.301 1.00 13.33 ? 117 ALA A C 1 ATOM 812 O O . ALA A 1 104 ? -11.488 13.106 17.204 1.00 14.79 ? 117 ALA A O 1 ATOM 813 C CB . ALA A 1 104 ? -11.685 16.000 17.616 1.00 14.29 ? 117 ALA A CB 1 ATOM 814 N N . VAL A 1 105 ? -10.397 13.161 19.183 1.00 13.08 ? 118 VAL A N 1 ATOM 815 C CA . VAL A 1 105 ? -9.563 11.998 18.900 1.00 13.28 ? 118 VAL A CA 1 ATOM 816 C C . VAL A 1 105 ? -9.506 11.159 20.163 1.00 15.05 ? 118 VAL A C 1 ATOM 817 O O . VAL A 1 105 ? -8.978 11.597 21.185 1.00 14.64 ? 118 VAL A O 1 ATOM 818 C CB . VAL A 1 105 ? -8.149 12.417 18.430 1.00 14.76 ? 118 VAL A CB 1 ATOM 819 C CG1 . VAL A 1 105 ? -7.283 11.185 18.143 1.00 16.63 ? 118 VAL A CG1 1 ATOM 820 C CG2 . VAL A 1 105 ? -8.248 13.306 17.198 1.00 15.55 ? 118 VAL A CG2 1 ATOM 821 N N . GLY A 1 106 ? -10.059 9.957 20.101 1.00 12.70 ? 119 GLY A N 1 ATOM 822 C CA . GLY A 1 106 ? -10.139 9.085 21.245 1.00 11.99 ? 119 GLY A CA 1 ATOM 823 C C . GLY A 1 106 ? -10.182 7.651 20.831 1.00 12.31 ? 119 GLY A C 1 ATOM 824 O O . GLY A 1 106 ? -10.231 7.343 19.636 1.00 12.59 ? 119 GLY A O 1 ATOM 825 N N . LEU A 1 107 ? -10.130 6.787 21.829 1.00 11.43 ? 120 LEU A N 1 ATOM 826 C CA . LEU A 1 107 ? -10.051 5.341 21.661 1.00 12.39 ? 120 LEU A CA 1 ATOM 827 C C . LEU A 1 107 ? -11.423 4.672 21.713 1.00 12.31 ? 120 LEU A C 1 ATOM 828 O O . LEU A 1 107 ? -12.339 5.168 22.370 1.00 13.81 ? 120 LEU A O 1 ATOM 829 C CB . LEU A 1 107 ? -9.154 4.735 22.748 1.00 13.14 ? 120 LEU A CB 1 ATOM 830 C CG . LEU A 1 107 ? -7.793 5.403 22.899 1.00 13.35 ? 120 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 107 ? -6.952 4.680 23.944 1.00 15.10 ? 120 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 107 ? -7.035 5.465 21.569 1.00 14.14 ? 120 LEU A CD2 1 ATOM 833 N N . LEU A 1 108 ? -11.545 3.531 21.020 1.00 11.55 ? 121 LEU A N 1 ATOM 834 C CA . LEU A 1 108 ? -12.704 2.650 21.096 1.00 11.46 ? 121 LEU A CA 1 ATOM 835 C C . LEU A 1 108 ? -12.234 1.337 21.696 1.00 11.25 ? 121 LEU A C 1 ATOM 836 O O . LEU A 1 108 ? -11.190 0.808 21.286 1.00 12.19 ? 121 LEU A O 1 ATOM 837 C CB . LEU A 1 108 ? -13.293 2.409 19.697 1.00 12.21 ? 121 LEU A CB 1 ATOM 838 C CG . LEU A 1 108 ? -14.505 1.474 19.601 1.00 12.10 ? 121 LEU A CG 1 ATOM 839 C CD1 . LEU A 1 108 ? -15.698 1.965 20.410 1.00 12.80 ? 121 LEU A CD1 1 ATOM 840 C CD2 . LEU A 1 108 ? -14.878 1.308 18.134 1.00 13.45 ? 121 LEU A CD2 1 ATOM 841 N N . ARG A 1 109 ? -12.977 0.838 22.681 1.00 12.60 ? 122 ARG A N 1 ATOM 842 C CA . ARG A 1 109 ? -12.647 -0.411 23.351 1.00 13.42 ? 122 ARG A CA 1 ATOM 843 C C . ARG A 1 109 ? -13.087 -1.642 22.533 1.00 12.41 ? 122 ARG A C 1 ATOM 844 O O . ARG A 1 109 ? -14.180 -1.687 21.978 1.00 12.63 ? 122 ARG A O 1 ATOM 845 C CB . ARG A 1 109 ? -13.254 -0.458 24.766 1.00 15.25 ? 122 ARG A CB 1 ATOM 846 C CG . ARG A 1 109 ? -12.630 0.537 25.745 1.00 17.91 ? 122 ARG A CG 1 ATOM 847 C CD . ARG A 1 109 ? -11.380 0.022 26.446 1.00 22.64 ? 122 ARG A CD 1 ATOM 848 N NE . ARG A 1 109 ? -11.641 -1.228 27.164 1.00 23.02 ? 122 ARG A NE 1 ATOM 849 C CZ . ARG A 1 109 ? -12.142 -1.344 28.401 1.00 24.11 ? 122 ARG A CZ 1 ATOM 850 N NH1 . ARG A 1 109 ? -12.431 -0.272 29.146 1.00 23.13 ? 122 ARG A NH1 1 ATOM 851 N NH2 . ARG A 1 109 ? -12.360 -2.558 28.902 1.00 22.39 ? 122 ARG A NH2 1 ATOM 852 N N . LEU A 1 110 ? -12.239 -2.664 22.563 1.00 12.04 ? 123 LEU A N 1 ATOM 853 C CA . LEU A 1 110 ? -12.594 -3.988 22.070 1.00 13.37 ? 123 LEU A CA 1 ATOM 854 C C . LEU A 1 110 ? -13.509 -4.730 23.026 1.00 14.01 ? 123 LEU A C 1 ATOM 855 O O . LEU A 1 110 ? -13.566 -4.409 24.220 1.00 14.31 ? 123 LEU A O 1 ATOM 856 C CB . LEU A 1 110 ? -11.332 -4.835 21.891 1.00 13.89 ? 123 LEU A CB 1 ATOM 857 C CG . LEU A 1 110 ? -10.320 -4.351 20.869 1.00 13.10 ? 123 LEU A CG 1 ATOM 858 C CD1 . LEU A 1 110 ? -9.018 -5.131 20.948 1.00 13.73 ? 123 LEU A CD1 1 ATOM 859 C CD2 . LEU A 1 110 ? -10.891 -4.431 19.459 1.00 15.15 ? 123 LEU A CD2 1 ATOM 860 N N . PRO A 1 111 ? -14.207 -5.756 22.525 1.00 13.79 ? 124 PRO A N 1 ATOM 861 C CA . PRO A 1 111 ? -14.846 -6.672 23.450 1.00 15.66 ? 124 PRO A CA 1 ATOM 862 C C . PRO A 1 111 ? -13.804 -7.350 24.341 1.00 18.81 ? 124 PRO A C 1 ATOM 863 O O . PRO A 1 111 ? -12.640 -7.462 23.970 1.00 17.68 ? 124 PRO A O 1 ATOM 864 C CB . PRO A 1 111 ? -15.515 -7.704 22.528 1.00 17.77 ? 124 PRO A CB 1 ATOM 865 C CG . PRO A 1 111 ? -15.536 -7.092 21.171 1.00 17.24 ? 124 PRO A CG 1 ATOM 866 C CD . PRO A 1 111 ? -14.312 -6.231 21.133 1.00 15.28 ? 124 PRO A CD 1 ATOM 867 N N . GLY A 1 112 A -14.229 -7.788 25.515 1.00 25.19 ? 124 GLY A N 1 ATOM 868 C CA . GLY A 1 112 A -13.335 -8.488 26.435 1.00 28.37 ? 124 GLY A CA 1 ATOM 869 C C . GLY A 1 112 A -12.783 -9.780 25.854 1.00 28.99 ? 124 GLY A C 1 ATOM 870 O O . GLY A 1 112 A -13.341 -10.353 24.920 1.00 25.18 ? 124 GLY A O 1 ATOM 871 N N . ARG A 1 113 ? -11.670 -10.245 26.409 1.00 29.27 ? 125 ARG A N 1 ATOM 872 C CA . ARG A 1 113 ? -11.073 -11.508 25.960 1.00 31.17 ? 125 ARG A CA 1 ATOM 873 C C . ARG A 1 113 ? -11.992 -12.723 26.176 1.00 34.65 ? 125 ARG A C 1 ATOM 874 O O . ARG A 1 113 ? -11.818 -13.749 25.511 1.00 32.06 ? 125 ARG A O 1 ATOM 875 C CB . ARG A 1 113 ? -9.732 -11.735 26.648 1.00 30.29 ? 125 ARG A CB 1 ATOM 876 C CG . ARG A 1 113 ? -8.601 -10.875 26.104 1.00 29.70 ? 125 ARG A CG 1 ATOM 877 C CD . ARG A 1 113 ? -7.402 -11.001 27.015 1.00 29.21 ? 125 ARG A CD 1 ATOM 878 N NE . ARG A 1 113 ? -6.244 -10.221 26.593 1.00 27.65 ? 125 ARG A NE 1 ATOM 879 C CZ . ARG A 1 113 ? -5.338 -10.627 25.713 1.00 26.82 ? 125 ARG A CZ 1 ATOM 880 N NH1 . ARG A 1 113 ? -5.455 -11.810 25.105 1.00 27.41 ? 125 ARG A NH1 1 ATOM 881 N NH2 . ARG A 1 113 ? -4.298 -9.850 25.445 1.00 25.78 ? 125 ARG A NH2 1 ATOM 882 N N . ARG A 1 114 ? -12.959 -12.605 27.089 1.00 38.29 ? 126 ARG A N 1 ATOM 883 C CA . ARG A 1 114 ? -13.924 -13.681 27.354 1.00 47.33 ? 126 ARG A CA 1 ATOM 884 C C . ARG A 1 114 ? -15.335 -13.400 26.812 1.00 44.98 ? 126 ARG A C 1 ATOM 885 O O . ARG A 1 114 ? -16.229 -14.229 26.978 1.00 42.55 ? 126 ARG A O 1 ATOM 886 C CB . ARG A 1 114 ? -14.000 -13.962 28.863 1.00 54.46 ? 126 ARG A CB 1 ATOM 887 C CG . ARG A 1 114 ? -12.695 -14.453 29.469 1.00 59.85 ? 126 ARG A CG 1 ATOM 888 C CD . ARG A 1 114 ? -12.822 -14.687 30.966 1.00 76.26 ? 126 ARG A CD 1 ATOM 889 N NE . ARG A 1 114 ? -11.544 -15.075 31.565 1.00 90.01 ? 126 ARG A NE 1 ATOM 890 C CZ . ARG A 1 114 ? -11.330 -15.235 32.871 1.00 103.61 ? 126 ARG A CZ 1 ATOM 891 N NH1 . ARG A 1 114 ? -12.309 -15.046 33.752 1.00 114.60 ? 126 ARG A NH1 1 ATOM 892 N NH2 . ARG A 1 114 ? -10.122 -15.588 33.302 1.00 99.55 ? 126 ARG A NH2 1 ATOM 893 N N . ALA A 1 115 ? -15.532 -12.255 26.156 1.00 38.56 ? 127 ALA A N 1 ATOM 894 C CA . ALA A 1 115 ? -16.865 -11.852 25.673 1.00 37.82 ? 127 ALA A CA 1 ATOM 895 C C . ALA A 1 115 ? -17.375 -12.690 24.489 1.00 37.50 ? 127 ALA A C 1 ATOM 896 O O . ALA A 1 115 ? -16.589 -13.175 23.667 1.00 32.34 ? 127 ALA A O 1 ATOM 897 C CB . ALA A 1 115 ? -16.876 -10.372 25.312 1.00 41.49 ? 127 ALA A CB 1 ATOM 898 N N . ARG A 1 116 ? -18.701 -12.854 24.436 1.00 44.49 ? 128 ARG A N 1 ATOM 899 C CA . ARG A 1 116 ? -19.402 -13.507 23.324 1.00 43.14 ? 128 ARG A CA 1 ATOM 900 C C . ARG A 1 116 ? -19.798 -12.447 22.295 1.00 40.63 ? 128 ARG A C 1 ATOM 901 O O . ARG A 1 116 ? -19.808 -11.256 22.608 1.00 39.37 ? 128 ARG A O 1 ATOM 902 C CB . ARG A 1 116 ? -20.689 -14.194 23.820 1.00 55.58 ? 128 ARG A CB 1 ATOM 903 C CG . ARG A 1 116 ? -20.506 -15.281 24.875 1.00 69.53 ? 128 ARG A CG 1 ATOM 904 C CD . ARG A 1 116 ? -20.472 -16.688 24.288 1.00 78.16 ? 128 ARG A CD 1 ATOM 905 N NE . ARG A 1 116 ? -21.805 -17.299 24.183 1.00 85.37 ? 128 ARG A NE 1 ATOM 906 C CZ . ARG A 1 116 ? -22.386 -17.725 23.056 1.00 94.31 ? 128 ARG A CZ 1 ATOM 907 N NH1 . ARG A 1 116 ? -21.775 -17.626 21.876 1.00 107.30 ? 128 ARG A NH1 1 ATOM 908 N NH2 . ARG A 1 116 ? -23.600 -18.266 23.110 1.00 82.72 ? 128 ARG A NH2 1 ATOM 909 N N . PRO A 1 117 ? -20.142 -12.871 21.065 1.00 48.98 ? 129 PRO A N 1 ATOM 910 C CA . PRO A 1 117 ? -20.746 -11.924 20.122 1.00 42.94 ? 129 PRO A CA 1 ATOM 911 C C . PRO A 1 117 ? -22.136 -11.489 20.595 1.00 37.50 ? 129 PRO A C 1 ATOM 912 O O . PRO A 1 117 ? -22.776 -12.219 21.343 1.00 30.72 ? 129 PRO A O 1 ATOM 913 C CB . PRO A 1 117 ? -20.839 -12.729 18.820 1.00 47.85 ? 129 PRO A CB 1 ATOM 914 C CG . PRO A 1 117 ? -20.811 -14.156 19.244 1.00 46.97 ? 129 PRO A CG 1 ATOM 915 C CD . PRO A 1 117 ? -19.920 -14.191 20.449 1.00 49.73 ? 129 PRO A CD 1 ATOM 916 N N . PRO A 1 118 ? -22.599 -10.302 20.172 1.00 23.83 ? 130 PRO A N 1 ATOM 917 C CA . PRO A 1 118 ? -23.892 -9.811 20.654 1.00 26.89 ? 130 PRO A CA 1 ATOM 918 C C . PRO A 1 118 ? -25.084 -10.639 20.157 1.00 30.62 ? 130 PRO A C 1 ATOM 919 O O . PRO A 1 118 ? -25.052 -11.174 19.047 1.00 29.82 ? 130 PRO A O 1 ATOM 920 C CB . PRO A 1 118 ? -23.952 -8.373 20.123 1.00 28.98 ? 130 PRO A CB 1 ATOM 921 C CG . PRO A 1 118 ? -22.963 -8.312 19.013 1.00 28.92 ? 130 PRO A CG 1 ATOM 922 C CD . PRO A 1 118 ? -21.908 -9.326 19.306 1.00 26.80 ? 130 PRO A CD 1 ATOM 923 N N . THR A 1 119 ? -26.126 -10.727 20.975 1.00 27.40 ? 131 THR A N 1 ATOM 924 C CA . THR A 1 119 ? -27.293 -11.540 20.632 1.00 31.92 ? 131 THR A CA 1 ATOM 925 C C . THR A 1 119 ? -28.082 -10.899 19.481 1.00 30.30 ? 131 THR A C 1 ATOM 926 O O . THR A 1 119 ? -28.019 -9.688 19.277 1.00 25.77 ? 131 THR A O 1 ATOM 927 C CB . THR A 1 119 ? -28.213 -11.755 21.857 1.00 37.26 ? 131 THR A CB 1 ATOM 928 O OG1 . THR A 1 119 ? -28.764 -10.503 22.283 1.00 40.21 ? 131 THR A OG1 1 ATOM 929 C CG2 . THR A 1 119 ? -27.441 -12.382 23.012 1.00 42.39 ? 131 THR A CG2 1 ATOM 930 N N . ALA A 1 120 ? -28.818 -11.715 18.728 1.00 25.64 ? 132 ALA A N 1 ATOM 931 C CA . ALA A 1 120 ? -29.689 -11.203 17.684 1.00 22.25 ? 132 ALA A CA 1 ATOM 932 C C . ALA A 1 120 ? -30.639 -10.153 18.238 1.00 24.65 ? 132 ALA A C 1 ATOM 933 O O . ALA A 1 120 ? -31.208 -10.324 19.330 1.00 27.28 ? 132 ALA A O 1 ATOM 934 C CB . ALA A 1 120 ? -30.462 -12.339 17.035 1.00 22.42 ? 132 ALA A CB 1 ATOM 935 N N . GLY A 1 121 ? -30.792 -9.059 17.500 1.00 24.27 ? 133 GLY A N 1 ATOM 936 C CA . GLY A 1 121 ? -31.653 -7.945 17.893 1.00 25.28 ? 133 GLY A CA 1 ATOM 937 C C . GLY A 1 121 ? -30.926 -6.814 18.608 1.00 21.93 ? 133 GLY A C 1 ATOM 938 O O . GLY A 1 121 ? -31.464 -5.709 18.730 1.00 24.71 ? 133 GLY A O 1 ATOM 939 N N . THR A 1 122 ? -29.698 -7.070 19.060 1.00 23.61 ? 134 THR A N 1 ATOM 940 C CA . THR A 1 122 ? -28.909 -6.052 19.747 1.00 21.10 ? 134 THR A CA 1 ATOM 941 C C . THR A 1 122 ? -28.746 -4.826 18.863 1.00 22.99 ? 134 THR A C 1 ATOM 942 O O . THR A 1 122 ? -28.374 -4.945 17.692 1.00 19.58 ? 134 THR A O 1 ATOM 943 C CB . THR A 1 122 ? -27.525 -6.590 20.154 1.00 21.90 ? 134 THR A CB 1 ATOM 944 O OG1 . THR A 1 122 ? -27.698 -7.659 21.091 1.00 26.01 ? 134 THR A OG1 1 ATOM 945 C CG2 . THR A 1 122 ? -26.670 -5.490 20.796 1.00 21.61 ? 134 THR A CG2 1 ATOM 946 N N . ARG A 1 123 ? -29.054 -3.662 19.416 1.00 22.65 ? 135 ARG A N 1 ATOM 947 C CA . ARG A 1 123 ? -28.938 -2.388 18.716 1.00 22.02 ? 135 ARG A CA 1 ATOM 948 C C . ARG A 1 123 ? -27.484 -1.933 18.671 1.00 19.47 ? 135 ARG A C 1 ATOM 949 O O . ARG A 1 123 ? -26.809 -1.852 19.697 1.00 19.15 ? 135 ARG A O 1 ATOM 950 C CB . ARG A 1 123 ? -29.786 -1.312 19.403 1.00 26.89 ? 135 ARG A CB 1 ATOM 951 C CG . ARG A 1 123 ? -31.281 -1.493 19.212 1.00 32.73 ? 135 ARG A CG 1 ATOM 952 C CD . ARG A 1 123 ? -32.030 -0.251 19.675 1.00 47.08 ? 135 ARG A CD 1 ATOM 953 N NE . ARG A 1 123 ? -33.390 -0.547 20.122 1.00 56.91 ? 135 ARG A NE 1 ATOM 954 C CZ . ARG A 1 123 ? -33.698 -1.157 21.269 1.00 62.24 ? 135 ARG A CZ 1 ATOM 955 N NH1 . ARG A 1 123 ? -32.747 -1.558 22.112 1.00 63.68 ? 135 ARG A NH1 1 ATOM 956 N NH2 . ARG A 1 123 ? -34.972 -1.375 21.575 1.00 66.07 ? 135 ARG A NH2 1 ATOM 957 N N . CYS A 1 124 ? -27.007 -1.661 17.459 1.00 16.88 ? 136 CYS A N 1 ATOM 958 C CA . CYS A 1 124 ? -25.639 -1.219 17.231 1.00 15.79 ? 136 CYS A CA 1 ATOM 959 C C . CYS A 1 124 ? -25.642 -0.059 16.247 1.00 16.47 ? 136 CYS A C 1 ATOM 960 O O . CYS A 1 124 ? -26.661 0.291 15.670 1.00 17.28 ? 136 CYS A O 1 ATOM 961 C CB . CYS A 1 124 ? -24.821 -2.372 16.632 1.00 16.59 ? 136 CYS A CB 1 ATOM 962 S SG . CYS A 1 124 ? -24.879 -3.937 17.548 1.00 19.44 ? 136 CYS A SG 1 ATOM 963 N N . ARG A 1 125 ? -24.463 0.513 16.039 1.00 14.57 ? 137 ARG A N 1 ATOM 964 C CA . ARG A 1 125 ? -24.299 1.597 15.067 1.00 16.11 ? 137 ARG A CA 1 ATOM 965 C C . ARG A 1 125 ? -23.044 1.368 14.240 1.00 12.94 ? 137 ARG A C 1 ATOM 966 O O . ARG A 1 125 ? -22.061 0.814 14.728 1.00 12.76 ? 137 ARG A O 1 ATOM 967 C CB . ARG A 1 125 ? -24.246 2.951 15.773 1.00 17.58 ? 137 ARG A CB 1 ATOM 968 C CG . ARG A 1 125 ? -23.122 3.070 16.779 1.00 21.35 ? 137 ARG A CG 1 ATOM 969 C CD . ARG A 1 125 ? -23.247 4.262 17.725 1.00 26.77 ? 137 ARG A CD 1 ATOM 970 N NE . ARG A 1 125 ? -21.930 4.631 18.247 1.00 27.20 ? 137 ARG A NE 1 ATOM 971 C CZ . ARG A 1 125 ? -21.697 5.422 19.294 1.00 27.25 ? 137 ARG A CZ 1 ATOM 972 N NH1 . ARG A 1 125 ? -22.700 5.973 19.982 1.00 28.95 ? 137 ARG A NH1 1 ATOM 973 N NH2 . ARG A 1 125 ? -20.433 5.658 19.651 1.00 22.91 ? 137 ARG A NH2 1 ATOM 974 N N . VAL A 1 126 ? -23.103 1.766 12.980 1.00 12.90 ? 138 VAL A N 1 ATOM 975 C CA . VAL A 1 126 ? -21.938 1.703 12.094 1.00 11.56 ? 138 VAL A CA 1 ATOM 976 C C . VAL A 1 126 ? -21.761 3.033 11.407 1.00 12.24 ? 138 VAL A C 1 ATOM 977 O O . VAL A 1 126 ? -22.699 3.576 10.849 1.00 13.23 ? 138 VAL A O 1 ATOM 978 C CB . VAL A 1 126 ? -22.044 0.527 11.084 1.00 12.40 ? 138 VAL A CB 1 ATOM 979 C CG1 . VAL A 1 126 ? -23.309 0.603 10.240 1.00 12.89 ? 138 VAL A CG1 1 ATOM 980 C CG2 . VAL A 1 126 ? -20.790 0.445 10.222 1.00 12.54 ? 138 VAL A CG2 1 ATOM 981 N N . ALA A 1 127 ? -20.531 3.540 11.430 1.00 12.17 ? 139 ALA A N 1 ATOM 982 C CA . ALA A 1 127 ? -20.211 4.850 10.875 1.00 11.79 ? 139 ALA A CA 1 ATOM 983 C C . ALA A 1 127 ? -19.160 4.754 9.791 1.00 10.91 ? 139 ALA A C 1 ATOM 984 O O . ALA A 1 127 ? -18.339 3.834 9.786 1.00 11.94 ? 139 ALA A O 1 ATOM 985 C CB . ALA A 1 127 ? -19.762 5.828 11.973 1.00 13.21 ? 139 ALA A CB 1 ATOM 986 N N . GLY A 1 128 ? -19.162 5.719 8.892 1.00 11.34 ? 140 GLY A N 1 ATOM 987 C CA . GLY A 1 128 ? -18.154 5.772 7.848 1.00 11.36 ? 140 GLY A CA 1 ATOM 988 C C . GLY A 1 128 ? -18.378 6.865 6.832 1.00 10.87 ? 140 GLY A C 1 ATOM 989 O O . GLY A 1 128 ? -19.397 7.569 6.834 1.00 12.48 ? 140 GLY A O 1 ATOM 990 N N . TRP A 1 129 ? -17.393 7.006 5.954 1.00 11.27 ? 141 TRP A N 1 ATOM 991 C CA . TRP A 1 129 ? -17.402 7.967 4.850 1.00 11.20 ? 141 TRP A CA 1 ATOM 992 C C . TRP A 1 129 ? -17.603 7.293 3.496 1.00 13.13 ? 141 TRP A C 1 ATOM 993 O O . TRP A 1 129 ? -17.320 7.877 2.469 1.00 13.87 ? 141 TRP A O 1 ATOM 994 C CB . TRP A 1 129 ? -16.117 8.763 4.829 1.00 11.71 ? 141 TRP A CB 1 ATOM 995 C CG . TRP A 1 129 ? -15.876 9.670 6.021 1.00 12.18 ? 141 TRP A CG 1 ATOM 996 C CD1 . TRP A 1 129 ? -16.245 11.009 6.169 1.00 12.37 ? 141 TRP A CD1 1 ATOM 997 C CD2 . TRP A 1 129 ? -15.126 9.353 7.226 1.00 12.04 ? 141 TRP A CD2 1 ATOM 998 N NE1 . TRP A 1 129 ? -15.809 11.509 7.373 1.00 11.70 ? 141 TRP A NE1 1 ATOM 999 C CE2 . TRP A 1 129 ? -15.120 10.571 8.051 1.00 12.30 ? 141 TRP A CE2 1 ATOM 1000 C CE3 . TRP A 1 129 ? -14.499 8.218 7.713 1.00 11.43 ? 141 TRP A CE3 1 ATOM 1001 C CZ2 . TRP A 1 129 ? -14.493 10.612 9.292 1.00 13.25 ? 141 TRP A CZ2 1 ATOM 1002 C CZ3 . TRP A 1 129 ? -13.880 8.276 8.958 1.00 11.61 ? 141 TRP A CZ3 1 ATOM 1003 C CH2 . TRP A 1 129 ? -13.856 9.445 9.719 1.00 11.53 ? 141 TRP A CH2 1 ATOM 1004 N N . GLY A 1 130 ? -18.108 6.064 3.506 1.00 12.21 ? 142 GLY A N 1 ATOM 1005 C CA . GLY A 1 130 ? -18.372 5.344 2.264 1.00 11.28 ? 142 GLY A CA 1 ATOM 1006 C C . GLY A 1 130 ? -19.591 5.876 1.542 1.00 12.39 ? 142 GLY A C 1 ATOM 1007 O O . GLY A 1 130 ? -20.249 6.800 2.002 1.00 14.32 ? 142 GLY A O 1 ATOM 1008 N N . PHE A 1 131 ? -19.907 5.275 0.401 1.00 11.54 ? 143 PHE A N 1 ATOM 1009 C CA . PHE A 1 131 ? -20.977 5.794 -0.422 1.00 12.91 ? 143 PHE A CA 1 ATOM 1010 C C . PHE A 1 131 ? -22.320 5.700 0.291 1.00 13.08 ? 143 PHE A C 1 ATOM 1011 O O . PHE A 1 131 ? -22.547 4.788 1.106 1.00 13.66 ? 143 PHE A O 1 ATOM 1012 C CB . PHE A 1 131 ? -21.071 5.021 -1.730 1.00 14.78 ? 143 PHE A CB 1 ATOM 1013 C CG . PHE A 1 131 ? -19.843 5.111 -2.579 1.00 15.76 ? 143 PHE A CG 1 ATOM 1014 C CD1 . PHE A 1 131 ? -19.245 6.327 -2.854 1.00 17.27 ? 143 PHE A CD1 1 ATOM 1015 C CD2 . PHE A 1 131 ? -19.341 3.971 -3.161 1.00 15.47 ? 143 PHE A CD2 1 ATOM 1016 C CE1 . PHE A 1 131 ? -18.125 6.395 -3.658 1.00 19.71 ? 143 PHE A CE1 1 ATOM 1017 C CE2 . PHE A 1 131 ? -18.221 4.023 -3.977 1.00 17.32 ? 143 PHE A CE2 1 ATOM 1018 C CZ . PHE A 1 131 ? -17.610 5.238 -4.220 1.00 18.69 ? 143 PHE A CZ 1 ATOM 1019 N N . VAL A 1 132 ? -23.225 6.616 -0.067 1.00 14.29 ? 144 VAL A N 1 ATOM 1020 C CA . VAL A 1 132 ? -24.542 6.689 0.557 1.00 15.29 ? 144 VAL A CA 1 ATOM 1021 C C . VAL A 1 132 ? -25.651 6.160 -0.355 1.00 16.39 ? 144 VAL A C 1 ATOM 1022 O O . VAL A 1 132 ? -26.828 6.229 -0.017 1.00 18.33 ? 144 VAL A O 1 ATOM 1023 C CB . VAL A 1 132 ? -24.862 8.121 1.046 1.00 15.13 ? 144 VAL A CB 1 ATOM 1024 C CG1 . VAL A 1 132 ? -23.816 8.553 2.067 1.00 15.28 ? 144 VAL A CG1 1 ATOM 1025 C CG2 . VAL A 1 132 ? -24.934 9.107 -0.118 1.00 16.23 ? 144 VAL A CG2 1 ATOM 1026 N N . SER A 1 133 ? -25.267 5.588 -1.497 1.00 15.50 ? 145 SER A N 1 ATOM 1027 C CA . SER A 1 133 ? -26.217 5.018 -2.446 1.00 17.13 ? 145 SER A CA 1 ATOM 1028 C C . SER A 1 133 ? -25.471 3.992 -3.288 1.00 16.77 ? 145 SER A C 1 ATOM 1029 O O . SER A 1 133 ? -24.266 3.793 -3.118 1.00 16.22 ? 145 SER A O 1 ATOM 1030 C CB . SER A 1 133 ? -26.791 6.105 -3.343 1.00 16.68 ? 145 SER A CB 1 ATOM 1031 O OG . SER A 1 133 ? -25.807 6.558 -4.254 1.00 16.79 ? 145 SER A OG 1 ATOM 1032 N N . ASP A 1 134 ? -26.195 3.321 -4.170 1.00 17.73 ? 147 ASP A N 1 ATOM 1033 C CA . ASP A 1 134 ? -25.564 2.470 -5.162 1.00 16.85 ? 147 ASP A CA 1 ATOM 1034 C C . ASP A 1 134 ? -25.132 3.235 -6.406 1.00 17.17 ? 147 ASP A C 1 ATOM 1035 O O . ASP A 1 134 ? -24.847 2.610 -7.418 1.00 17.77 ? 147 ASP A O 1 ATOM 1036 C CB . ASP A 1 134 ? -26.496 1.334 -5.554 1.00 20.06 ? 147 ASP A CB 1 ATOM 1037 C CG . ASP A 1 134 ? -26.710 0.361 -4.438 1.00 19.07 ? 147 ASP A CG 1 ATOM 1038 O OD1 . ASP A 1 134 ? -25.711 -0.117 -3.839 1.00 19.49 ? 147 ASP A OD1 1 ATOM 1039 O OD2 . ASP A 1 134 ? -27.888 0.071 -4.172 1.00 19.95 ? 147 ASP A OD2 1 ATOM 1040 N N . PHE A 1 135 ? -25.060 4.563 -6.336 1.00 16.76 ? 148 PHE A N 1 ATOM 1041 C CA . PHE A 1 135 ? -24.577 5.376 -7.454 1.00 18.22 ? 148 PHE A CA 1 ATOM 1042 C C . PHE A 1 135 ? -23.336 6.162 -7.077 1.00 18.01 ? 148 PHE A C 1 ATOM 1043 O O . PHE A 1 135 ? -23.060 7.233 -7.592 1.00 18.01 ? 148 PHE A O 1 ATOM 1044 C CB . PHE A 1 135 ? -25.701 6.262 -7.969 1.00 18.83 ? 148 PHE A CB 1 ATOM 1045 C CG . PHE A 1 135 ? -26.983 5.516 -8.129 1.00 20.04 ? 148 PHE A CG 1 ATOM 1046 C CD1 . PHE A 1 135 ? -28.007 5.666 -7.209 1.00 22.00 ? 148 PHE A CD1 1 ATOM 1047 C CD2 . PHE A 1 135 ? -27.137 4.591 -9.152 1.00 22.04 ? 148 PHE A CD2 1 ATOM 1048 C CE1 . PHE A 1 135 ? -29.181 4.944 -7.332 1.00 25.86 ? 148 PHE A CE1 1 ATOM 1049 C CE2 . PHE A 1 135 ? -28.311 3.868 -9.279 1.00 24.12 ? 148 PHE A CE2 1 ATOM 1050 C CZ . PHE A 1 135 ? -29.333 4.046 -8.367 1.00 25.30 ? 148 PHE A CZ 1 ATOM 1051 N N . GLU A 1 136 ? -22.579 5.588 -6.163 1.00 15.41 ? 149 GLU A N 1 ATOM 1052 C CA . GLU A 1 136 ? -21.299 6.113 -5.748 1.00 16.19 ? 149 GLU A CA 1 ATOM 1053 C C . GLU A 1 136 ? -21.364 7.564 -5.277 1.00 16.89 ? 149 GLU A C 1 ATOM 1054 O O . GLU A 1 136 ? -20.450 8.342 -5.516 1.00 18.90 ? 149 GLU A O 1 ATOM 1055 C CB . GLU A 1 136 ? -20.254 5.894 -6.856 1.00 17.93 ? 149 GLU A CB 1 ATOM 1056 C CG . GLU A 1 136 ? -20.096 4.408 -7.196 1.00 16.69 ? 149 GLU A CG 1 ATOM 1057 C CD . GLU A 1 136 ? -18.843 4.088 -7.984 1.00 20.26 ? 149 GLU A CD 1 ATOM 1058 O OE1 . GLU A 1 136 ? -18.258 5.012 -8.588 1.00 23.18 ? 149 GLU A OE1 1 ATOM 1059 O OE2 . GLU A 1 136 ? -18.471 2.900 -7.997 1.00 19.81 ? 149 GLU A OE2 1 ATOM 1060 N N . GLU A 1 137 ? -22.455 7.904 -4.584 1.00 18.41 ? 150 GLU A N 1 ATOM 1061 C CA A GLU A 1 137 ? -22.602 9.244 -4.018 0.50 17.17 ? 150 GLU A CA 1 ATOM 1062 C CA B GLU A 1 137 ? -22.629 9.241 -4.000 0.50 17.58 ? 150 GLU A CA 1 ATOM 1063 C C . GLU A 1 137 ? -21.828 9.354 -2.708 1.00 15.93 ? 150 GLU A C 1 ATOM 1064 O O . GLU A 1 137 ? -21.927 8.488 -1.838 1.00 16.48 ? 150 GLU A O 1 ATOM 1065 C CB A GLU A 1 137 ? -24.075 9.583 -3.791 0.50 18.10 ? 150 GLU A CB 1 ATOM 1066 C CB B GLU A 1 137 ? -24.111 9.516 -3.707 0.50 18.92 ? 150 GLU A CB 1 ATOM 1067 C CG A GLU A 1 137 ? -24.876 9.744 -5.077 0.50 20.95 ? 150 GLU A CG 1 ATOM 1068 C CG B GLU A 1 137 ? -24.396 10.861 -3.042 0.50 21.49 ? 150 GLU A CG 1 ATOM 1069 C CD A GLU A 1 137 ? -26.372 9.708 -4.830 0.50 20.53 ? 150 GLU A CD 1 ATOM 1070 C CD B GLU A 1 137 ? -25.863 11.053 -2.688 0.50 23.92 ? 150 GLU A CD 1 ATOM 1071 O OE1 A GLU A 1 137 ? -26.896 10.689 -4.249 0.50 27.16 ? 150 GLU A OE1 1 ATOM 1072 O OE1 B GLU A 1 137 ? -26.682 10.138 -2.919 0.50 25.13 ? 150 GLU A OE1 1 ATOM 1073 O OE2 A GLU A 1 137 ? -27.025 8.710 -5.207 0.50 17.33 ? 150 GLU A OE2 1 ATOM 1074 O OE2 B GLU A 1 137 ? -26.206 12.128 -2.165 0.50 21.00 ? 150 GLU A OE2 1 ATOM 1075 N N . LEU A 1 138 ? -21.060 10.427 -2.574 1.00 16.94 ? 151 LEU A N 1 ATOM 1076 C CA . LEU A 1 138 ? -20.271 10.679 -1.381 1.00 18.54 ? 151 LEU A CA 1 ATOM 1077 C C . LEU A 1 138 ? -21.110 11.389 -0.320 1.00 17.23 ? 151 LEU A C 1 ATOM 1078 O O . LEU A 1 138 ? -22.004 12.182 -0.645 1.00 18.67 ? 151 LEU A O 1 ATOM 1079 C CB . LEU A 1 138 ? -19.039 11.527 -1.729 1.00 20.03 ? 151 LEU A CB 1 ATOM 1080 C CG . LEU A 1 138 ? -17.994 10.825 -2.601 1.00 27.84 ? 151 LEU A CG 1 ATOM 1081 C CD1 . LEU A 1 138 ? -16.930 11.805 -3.071 1.00 34.88 ? 151 LEU A CD1 1 ATOM 1082 C CD2 . LEU A 1 138 ? -17.365 9.689 -1.821 1.00 31.07 ? 151 LEU A CD2 1 ATOM 1083 N N . PRO A 1 139 ? -20.803 11.119 0.953 1.00 16.66 ? 152 PRO A N 1 ATOM 1084 C CA . PRO A 1 139 ? -21.487 11.817 2.036 1.00 16.27 ? 152 PRO A CA 1 ATOM 1085 C C . PRO A 1 139 ? -20.904 13.210 2.235 1.00 15.98 ? 152 PRO A C 1 ATOM 1086 O O . PRO A 1 139 ? -19.773 13.470 1.818 1.00 16.80 ? 152 PRO A O 1 ATOM 1087 C CB . PRO A 1 139 ? -21.174 10.939 3.246 1.00 17.48 ? 152 PRO A CB 1 ATOM 1088 C CG . PRO A 1 139 ? -19.824 10.411 2.948 1.00 16.89 ? 152 PRO A CG 1 ATOM 1089 C CD . PRO A 1 139 ? -19.768 10.200 1.464 1.00 17.43 ? 152 PRO A CD 1 ATOM 1090 N N . PRO A 1 140 ? -21.662 14.105 2.897 1.00 17.91 ? 153 PRO A N 1 ATOM 1091 C CA . PRO A 1 140 ? -21.118 15.434 3.204 1.00 19.34 ? 153 PRO A CA 1 ATOM 1092 C C . PRO A 1 140 ? -20.123 15.448 4.367 1.00 19.09 ? 153 PRO A C 1 ATOM 1093 O O . PRO A 1 140 ? -19.417 16.439 4.558 1.00 21.76 ? 153 PRO A O 1 ATOM 1094 C CB . PRO A 1 140 ? -22.354 16.240 3.581 1.00 20.02 ? 153 PRO A CB 1 ATOM 1095 C CG . PRO A 1 140 ? -23.333 15.233 4.073 1.00 18.90 ? 153 PRO A CG 1 ATOM 1096 C CD . PRO A 1 140 ? -23.040 13.933 3.383 1.00 19.42 ? 153 PRO A CD 1 ATOM 1097 N N . GLY A 1 141 ? -20.107 14.367 5.148 1.00 17.03 ? 154 GLY A N 1 ATOM 1098 C CA . GLY A 1 141 ? -19.189 14.180 6.274 1.00 15.03 ? 154 GLY A CA 1 ATOM 1099 C C . GLY A 1 141 ? -19.451 12.814 6.873 1.00 14.97 ? 154 GLY A C 1 ATOM 1100 O O . GLY A 1 141 ? -20.150 12.005 6.256 1.00 15.34 ? 154 GLY A O 1 ATOM 1101 N N . LEU A 1 142 ? -18.891 12.536 8.042 1.00 13.04 ? 155 LEU A N 1 ATOM 1102 C CA . LEU A 1 142 ? -19.079 11.225 8.665 1.00 14.02 ? 155 LEU A CA 1 ATOM 1103 C C . LEU A 1 142 ? -20.549 10.910 8.907 1.00 14.75 ? 155 LEU A C 1 ATOM 1104 O O . LEU A 1 142 ? -21.286 11.726 9.503 1.00 14.30 ? 155 LEU A O 1 ATOM 1105 C CB . LEU A 1 142 ? -18.302 11.150 9.975 1.00 13.10 ? 155 LEU A CB 1 ATOM 1106 C CG . LEU A 1 142 ? -18.310 9.829 10.743 1.00 12.02 ? 155 LEU A CG 1 ATOM 1107 C CD1 . LEU A 1 142 ? -17.700 8.711 9.905 1.00 11.91 ? 155 LEU A CD1 1 ATOM 1108 C CD2 . LEU A 1 142 ? -17.530 10.022 12.029 1.00 13.53 ? 155 LEU A CD2 1 ATOM 1109 N N . MET A 1 143 ? -20.984 9.754 8.411 1.00 12.73 ? 156 MET A N 1 ATOM 1110 C CA . MET A 1 143 ? -22.345 9.266 8.549 1.00 13.74 ? 156 MET A CA 1 ATOM 1111 C C . MET A 1 143 ? -22.407 8.071 9.485 1.00 13.08 ? 156 MET A C 1 ATOM 1112 O O . MET A 1 143 ? -21.444 7.324 9.633 1.00 12.49 ? 156 MET A O 1 ATOM 1113 C CB . MET A 1 143 ? -22.873 8.821 7.190 1.00 14.07 ? 156 MET A CB 1 ATOM 1114 C CG . MET A 1 143 ? -22.692 9.824 6.073 1.00 13.80 ? 156 MET A CG 1 ATOM 1115 S SD . MET A 1 143 ? -23.674 11.324 6.296 1.00 16.49 ? 156 MET A SD 1 ATOM 1116 C CE . MET A 1 143 ? -25.275 10.731 5.774 1.00 18.27 ? 156 MET A CE 1 ATOM 1117 N N . GLU A 1 144 ? -23.588 7.836 10.059 1.00 14.82 ? 157 GLU A N 1 ATOM 1118 C CA . GLU A 1 144 ? -23.800 6.661 10.886 1.00 15.73 ? 157 GLU A CA 1 ATOM 1119 C C . GLU A 1 144 ? -25.214 6.117 10.716 1.00 16.59 ? 157 GLU A C 1 ATOM 1120 O O . GLU A 1 144 ? -26.177 6.881 10.643 1.00 16.38 ? 157 GLU A O 1 ATOM 1121 C CB . GLU A 1 144 ? -23.540 7.027 12.345 1.00 16.12 ? 157 GLU A CB 1 ATOM 1122 C CG . GLU A 1 144 ? -23.639 5.876 13.320 1.00 15.17 ? 157 GLU A CG 1 ATOM 1123 C CD . GLU A 1 144 ? -23.234 6.311 14.715 1.00 17.30 ? 157 GLU A CD 1 ATOM 1124 O OE1 . GLU A 1 144 ? -24.116 6.801 15.453 1.00 20.17 ? 157 GLU A OE1 1 ATOM 1125 O OE2 . GLU A 1 144 ? -22.041 6.179 15.061 1.00 16.96 ? 157 GLU A OE2 1 ATOM 1126 N N . ALA A 1 145 ? -25.316 4.798 10.660 1.00 14.52 ? 158 ALA A N 1 ATOM 1127 C CA . ALA A 1 145 ? -26.600 4.110 10.550 1.00 16.23 ? 158 ALA A CA 1 ATOM 1128 C C . ALA A 1 145 ? -26.851 3.281 11.798 1.00 16.24 ? 158 ALA A C 1 ATOM 1129 O O . ALA A 1 145 ? -25.932 2.750 12.417 1.00 16.26 ? 158 ALA A O 1 ATOM 1130 C CB . ALA A 1 145 ? -26.650 3.222 9.302 1.00 14.23 ? 158 ALA A CB 1 ATOM 1131 N N . LYS A 1 146 ? -28.133 3.180 12.159 1.00 18.21 ? 159 LYS A N 1 ATOM 1132 C CA . LYS A 1 146 ? -28.581 2.318 13.244 1.00 17.84 ? 159 LYS A CA 1 ATOM 1133 C C . LYS A 1 146 ? -29.007 0.986 12.641 1.00 14.29 ? 159 LYS A C 1 ATOM 1134 O O . LYS A 1 146 ? -29.806 0.952 11.700 1.00 18.69 ? 159 LYS A O 1 ATOM 1135 C CB . LYS A 1 146 ? -29.760 2.956 13.974 1.00 20.43 ? 159 LYS A CB 1 ATOM 1136 C CG . LYS A 1 146 ? -29.480 4.321 14.582 1.00 22.55 ? 159 LYS A CG 1 ATOM 1137 C CD . LYS A 1 146 ? -30.718 4.832 15.321 1.00 24.70 ? 159 LYS A CD 1 ATOM 1138 C CE . LYS A 1 146 ? -30.655 6.337 15.523 1.00 38.78 ? 159 LYS A CE 1 ATOM 1139 N NZ . LYS A 1 146 ? -29.440 6.747 16.274 1.00 46.32 ? 159 LYS A NZ 1 ATOM 1140 N N . VAL A 1 147 ? -28.428 -0.100 13.154 1.00 16.23 ? 160 VAL A N 1 ATOM 1141 C CA . VAL A 1 147 ? -28.730 -1.460 12.696 1.00 16.11 ? 160 VAL A CA 1 ATOM 1142 C C . VAL A 1 147 ? -28.855 -2.409 13.886 1.00 19.13 ? 160 VAL A C 1 ATOM 1143 O O . VAL A 1 147 ? -28.540 -2.046 15.025 1.00 19.60 ? 160 VAL A O 1 ATOM 1144 C CB . VAL A 1 147 ? -27.662 -1.969 11.696 1.00 17.70 ? 160 VAL A CB 1 ATOM 1145 C CG1 . VAL A 1 147 ? -27.634 -1.087 10.451 1.00 16.95 ? 160 VAL A CG1 1 ATOM 1146 C CG2 . VAL A 1 147 ? -26.288 -2.005 12.333 1.00 15.97 ? 160 VAL A CG2 1 ATOM 1147 N N . ARG A 1 148 ? -29.334 -3.617 13.629 1.00 20.45 ? 161 ARG A N 1 ATOM 1148 C CA . ARG A 1 148 ? -29.493 -4.623 14.673 1.00 20.32 ? 161 ARG A CA 1 ATOM 1149 C C . ARG A 1 148 ? -28.806 -5.899 14.258 1.00 20.18 ? 161 ARG A C 1 ATOM 1150 O O . ARG A 1 148 ? -28.785 -6.222 13.078 1.00 18.50 ? 161 ARG A O 1 ATOM 1151 C CB . ARG A 1 148 ? -30.986 -4.884 14.925 1.00 26.55 ? 161 ARG A CB 1 ATOM 1152 C CG . ARG A 1 148 ? -31.698 -3.716 15.590 1.00 36.64 ? 161 ARG A CG 1 ATOM 1153 C CD . ARG A 1 148 ? -33.209 -3.839 15.488 1.00 44.74 ? 161 ARG A CD 1 ATOM 1154 N NE . ARG A 1 148 ? -33.908 -2.837 16.297 1.00 55.54 ? 161 ARG A NE 1 ATOM 1155 C CZ . ARG A 1 148 ? -34.361 -3.029 17.537 1.00 61.58 ? 161 ARG A CZ 1 ATOM 1156 N NH1 . ARG A 1 148 ? -34.198 -4.196 18.160 1.00 61.84 ? 161 ARG A NH1 1 ATOM 1157 N NH2 . ARG A 1 148 ? -34.987 -2.038 18.164 1.00 65.07 ? 161 ARG A NH2 1 ATOM 1158 N N . VAL A 1 149 ? -28.207 -6.606 15.203 1.00 16.55 ? 162 VAL A N 1 ATOM 1159 C CA . VAL A 1 149 ? -27.556 -7.880 14.916 1.00 17.21 ? 162 VAL A CA 1 ATOM 1160 C C . VAL A 1 149 ? -28.596 -8.872 14.376 1.00 18.72 ? 162 VAL A C 1 ATOM 1161 O O . VAL A 1 149 ? -29.693 -8.969 14.917 1.00 19.15 ? 162 VAL A O 1 ATOM 1162 C CB . VAL A 1 149 ? -26.845 -8.449 16.160 1.00 19.75 ? 162 VAL A CB 1 ATOM 1163 C CG1 . VAL A 1 149 ? -26.310 -9.853 15.900 1.00 20.03 ? 162 VAL A CG1 1 ATOM 1164 C CG2 . VAL A 1 149 ? -25.713 -7.509 16.577 1.00 17.79 ? 162 VAL A CG2 1 ATOM 1165 N N . LEU A 1 150 ? -28.248 -9.592 13.314 1.00 18.17 ? 163 LEU A N 1 ATOM 1166 C CA . LEU A 1 150 ? -29.143 -10.537 12.654 1.00 17.87 ? 163 LEU A CA 1 ATOM 1167 C C . LEU A 1 150 ? -28.747 -11.932 13.104 1.00 17.50 ? 163 LEU A C 1 ATOM 1168 O O . LEU A 1 150 ? -27.563 -12.241 13.185 1.00 17.65 ? 163 LEU A O 1 ATOM 1169 C CB . LEU A 1 150 ? -28.961 -10.418 11.139 1.00 18.67 ? 163 LEU A CB 1 ATOM 1170 C CG . LEU A 1 150 ? -29.806 -11.320 10.244 1.00 19.48 ? 163 LEU A CG 1 ATOM 1171 C CD1 . LEU A 1 150 ? -31.306 -11.098 10.414 1.00 21.32 ? 163 LEU A CD1 1 ATOM 1172 C CD2 . LEU A 1 150 ? -29.400 -11.054 8.799 1.00 18.90 ? 163 LEU A CD2 1 ATOM 1173 N N . ASP A 1 151 ? -29.743 -12.782 13.381 1.00 18.73 ? 164 ASP A N 1 ATOM 1174 C CA . ASP A 1 151 ? -29.515 -14.198 13.697 1.00 20.98 ? 164 ASP A CA 1 ATOM 1175 C C . ASP A 1 151 ? -28.478 -14.803 12.717 1.00 19.86 ? 164 ASP A C 1 ATOM 1176 O O . ASP A 1 151 ? -28.663 -14.732 11.494 1.00 17.05 ? 164 ASP A O 1 ATOM 1177 C CB . ASP A 1 151 ? -30.876 -14.929 13.653 1.00 22.48 ? 164 ASP A CB 1 ATOM 1178 C CG . ASP A 1 151 ? -30.794 -16.420 13.956 1.00 27.83 ? 164 ASP A CG 1 ATOM 1179 O OD1 . ASP A 1 151 ? -29.839 -17.102 13.556 1.00 25.54 ? 164 ASP A OD1 1 ATOM 1180 O OD2 . ASP A 1 151 ? -31.766 -16.946 14.558 1.00 36.30 ? 164 ASP A OD2 1 ATOM 1181 N N . PRO A 1 152 ? -27.379 -15.377 13.244 1.00 18.45 ? 165 PRO A N 1 ATOM 1182 C CA . PRO A 1 152 ? -26.351 -15.884 12.319 1.00 19.60 ? 165 PRO A CA 1 ATOM 1183 C C . PRO A 1 152 ? -26.817 -17.025 11.405 1.00 19.77 ? 165 PRO A C 1 ATOM 1184 O O . PRO A 1 152 ? -26.243 -17.215 10.328 1.00 20.06 ? 165 PRO A O 1 ATOM 1185 C CB . PRO A 1 152 ? -25.238 -16.367 13.247 1.00 21.32 ? 165 PRO A CB 1 ATOM 1186 C CG . PRO A 1 152 ? -25.895 -16.607 14.565 1.00 21.06 ? 165 PRO A CG 1 ATOM 1187 C CD . PRO A 1 152 ? -26.994 -15.587 14.656 1.00 17.34 ? 165 PRO A CD 1 ATOM 1188 N N . ASP A 1 153 ? -27.825 -17.790 11.823 1.00 18.47 ? 166 ASP A N 1 ATOM 1189 C CA . ASP A 1 153 ? -28.361 -18.853 10.967 1.00 18.22 ? 166 ASP A CA 1 ATOM 1190 C C . ASP A 1 153 ? -29.195 -18.290 9.828 1.00 19.39 ? 166 ASP A C 1 ATOM 1191 O O . ASP A 1 153 ? -29.092 -18.769 8.694 1.00 20.58 ? 166 ASP A O 1 ATOM 1192 C CB . ASP A 1 153 ? -29.190 -19.848 11.781 1.00 21.06 ? 166 ASP A CB 1 ATOM 1193 C CG . ASP A 1 153 ? -28.357 -20.609 12.779 1.00 30.35 ? 166 ASP A CG 1 ATOM 1194 O OD1 . ASP A 1 153 ? -27.251 -21.059 12.410 1.00 30.97 ? 166 ASP A OD1 1 ATOM 1195 O OD2 . ASP A 1 153 ? -28.815 -20.761 13.937 1.00 31.18 ? 166 ASP A OD2 1 ATOM 1196 N N . VAL A 1 154 ? -30.002 -17.279 10.124 1.00 18.46 ? 167 VAL A N 1 ATOM 1197 C CA . VAL A 1 154 ? -30.765 -16.563 9.103 1.00 17.54 ? 167 VAL A CA 1 ATOM 1198 C C . VAL A 1 154 ? -29.796 -15.902 8.115 1.00 18.80 ? 167 VAL A C 1 ATOM 1199 O O . VAL A 1 154 ? -29.951 -16.017 6.910 1.00 22.82 ? 167 VAL A O 1 ATOM 1200 C CB . VAL A 1 154 ? -31.687 -15.504 9.729 1.00 21.58 ? 167 VAL A CB 1 ATOM 1201 C CG1 . VAL A 1 154 ? -32.398 -14.691 8.654 1.00 26.63 ? 167 VAL A CG1 1 ATOM 1202 C CG2 . VAL A 1 154 ? -32.708 -16.164 10.658 1.00 22.49 ? 167 VAL A CG2 1 ATOM 1203 N N . CYS A 1 155 ? -28.772 -15.229 8.628 1.00 17.89 ? 168 CYS A N 1 ATOM 1204 C CA . CYS A 1 155 ? -27.781 -14.615 7.755 1.00 17.31 ? 168 CYS A CA 1 ATOM 1205 C C . CYS A 1 155 ? -27.092 -15.638 6.873 1.00 18.94 ? 168 CYS A C 1 ATOM 1206 O O . CYS A 1 155 ? -26.910 -15.417 5.673 1.00 18.67 ? 168 CYS A O 1 ATOM 1207 C CB . CYS A 1 155 ? -26.739 -13.871 8.586 1.00 15.68 ? 168 CYS A CB 1 ATOM 1208 S SG . CYS A 1 155 ? -25.631 -12.930 7.539 1.00 17.39 ? 168 CYS A SG 1 ATOM 1209 N N . ASN A 1 156 ? -26.662 -16.737 7.470 1.00 19.02 ? 169 ASN A N 1 ATOM 1210 C CA . ASN A 1 156 ? -25.985 -17.773 6.714 1.00 19.42 ? 169 ASN A CA 1 ATOM 1211 C C . ASN A 1 156 ? -26.865 -18.357 5.591 1.00 22.75 ? 169 ASN A C 1 ATOM 1212 O O . ASN A 1 156 ? -26.380 -18.596 4.473 1.00 21.79 ? 169 ASN A O 1 ATOM 1213 C CB . ASN A 1 156 ? -25.479 -18.862 7.651 1.00 21.37 ? 169 ASN A CB 1 ATOM 1214 C CG . ASN A 1 156 ? -24.574 -19.838 6.960 1.00 23.61 ? 169 ASN A CG 1 ATOM 1215 O OD1 . ASN A 1 156 ? -23.893 -19.508 5.978 1.00 21.74 ? 169 ASN A OD1 1 ATOM 1216 N ND2 . ASN A 1 156 ? -24.555 -21.056 7.472 1.00 26.25 ? 169 ASN A ND2 1 ATOM 1217 N N . SER A 1 157 ? -28.151 -18.569 5.862 1.00 20.74 ? 170 SER A N 1 ATOM 1218 C CA . SER A 1 157 ? -29.044 -19.060 4.798 1.00 23.27 ? 170 SER A CA 1 ATOM 1219 C C . SER A 1 157 ? -29.194 -18.024 3.666 1.00 26.86 ? 170 SER A C 1 ATOM 1220 O O . SER A 1 157 ? -29.128 -18.380 2.479 1.00 24.02 ? 170 SER A O 1 ATOM 1221 C CB . SER A 1 157 ? -30.402 -19.493 5.348 1.00 33.22 ? 170 SER A CB 1 ATOM 1222 O OG . SER A 1 157 ? -30.995 -18.495 6.151 1.00 37.79 ? 170 SER A OG 1 ATOM 1223 N N . SER A 1 158 ? -29.345 -16.743 4.012 1.00 22.36 ? 171 SER A N 1 ATOM 1224 C CA . SER A 1 158 ? -29.410 -15.680 2.991 1.00 25.57 ? 171 SER A CA 1 ATOM 1225 C C . SER A 1 158 ? -28.140 -15.621 2.141 1.00 26.31 ? 171 SER A C 1 ATOM 1226 O O . SER A 1 158 ? -28.200 -15.306 0.956 1.00 26.57 ? 171 SER A O 1 ATOM 1227 C CB . SER A 1 158 ? -29.662 -14.319 3.628 1.00 25.49 ? 171 SER A CB 1 ATOM 1228 O OG . SER A 1 158 ? -30.932 -14.267 4.246 1.00 29.54 ? 171 SER A OG 1 ATOM 1229 N N . TRP A 1 159 ? -27.002 -15.951 2.745 1.00 21.45 ? 172 TRP A N 1 ATOM 1230 C CA . TRP A 1 159 ? -25.726 -16.052 2.040 1.00 23.10 ? 172 TRP A CA 1 ATOM 1231 C C . TRP A 1 159 ? -25.470 -17.418 1.465 1.00 22.36 ? 172 TRP A C 1 ATOM 1232 O O . TRP A 1 159 ? -24.322 -17.776 1.190 1.00 23.37 ? 172 TRP A O 1 ATOM 1233 C CB . TRP A 1 159 ? -24.579 -15.626 2.966 1.00 19.01 ? 172 TRP A CB 1 ATOM 1234 C CG . TRP A 1 159 ? -24.421 -14.145 2.970 1.00 17.08 ? 172 TRP A CG 1 ATOM 1235 C CD1 . TRP A 1 159 ? -24.855 -13.239 3.924 1.00 15.41 ? 172 TRP A CD1 1 ATOM 1236 C CD2 . TRP A 1 159 ? -23.827 -13.343 1.916 1.00 16.92 ? 172 TRP A CD2 1 ATOM 1237 N NE1 . TRP A 1 159 ? -24.574 -11.970 3.539 1.00 14.73 ? 172 TRP A NE1 1 ATOM 1238 C CE2 . TRP A 1 159 ? -23.955 -11.964 2.334 1.00 16.24 ? 172 TRP A CE2 1 ATOM 1239 C CE3 . TRP A 1 159 ? -23.228 -13.629 0.691 1.00 17.37 ? 172 TRP A CE3 1 ATOM 1240 C CZ2 . TRP A 1 159 ? -23.476 -10.921 1.561 1.00 16.63 ? 172 TRP A CZ2 1 ATOM 1241 C CZ3 . TRP A 1 159 ? -22.750 -12.578 -0.076 1.00 19.49 ? 172 TRP A CZ3 1 ATOM 1242 C CH2 . TRP A 1 159 ? -22.872 -11.256 0.345 1.00 19.33 ? 172 TRP A CH2 1 ATOM 1243 N N . LYS A 1 160 ? -26.537 -18.210 1.318 1.00 24.64 ? 173 LYS A N 1 ATOM 1244 C CA . LYS A 1 160 ? -26.480 -19.522 0.651 1.00 25.22 ? 173 LYS A CA 1 ATOM 1245 C C . LYS A 1 160 ? -25.411 -20.440 1.259 1.00 23.67 ? 173 LYS A C 1 ATOM 1246 O O . LYS A 1 160 ? -24.773 -21.220 0.556 1.00 30.83 ? 173 LYS A O 1 ATOM 1247 C CB . LYS A 1 160 ? -26.228 -19.370 -0.862 1.00 26.53 ? 173 LYS A CB 1 ATOM 1248 C CG . LYS A 1 160 ? -26.987 -18.254 -1.564 1.00 37.61 ? 173 LYS A CG 1 ATOM 1249 C CD . LYS A 1 160 ? -28.489 -18.336 -1.367 1.00 41.62 ? 173 LYS A CD 1 ATOM 1250 C CE . LYS A 1 160 ? -29.244 -17.889 -2.615 1.00 46.07 ? 173 LYS A CE 1 ATOM 1251 N NZ . LYS A 1 160 ? -28.813 -16.575 -3.165 1.00 44.61 ? 173 LYS A NZ 1 ATOM 1252 N N . GLY A 1 161 ? -25.205 -20.312 2.572 1.00 23.81 ? 174 GLY A N 1 ATOM 1253 C CA . GLY A 1 161 ? -24.336 -21.218 3.320 1.00 25.40 ? 174 GLY A CA 1 ATOM 1254 C C . GLY A 1 161 ? -22.860 -20.894 3.398 1.00 28.03 ? 174 GLY A C 1 ATOM 1255 O O . GLY A 1 161 ? -22.081 -21.700 3.918 1.00 28.38 ? 174 GLY A O 1 ATOM 1256 N N . HIS A 1 162 ? -22.481 -19.697 2.954 1.00 30.77 ? 175 HIS A N 1 ATOM 1257 C CA . HIS A 1 162 ? -21.066 -19.326 2.807 1.00 34.16 ? 175 HIS A CA 1 ATOM 1258 C C . HIS A 1 162 ? -20.439 -18.609 3.982 1.00 34.09 ? 175 HIS A C 1 ATOM 1259 O O . HIS A 1 162 ? -19.267 -18.233 3.913 1.00 39.87 ? 175 HIS A O 1 ATOM 1260 C CB . HIS A 1 162 ? -20.878 -18.492 1.533 1.00 43.39 ? 175 HIS A CB 1 ATOM 1261 C CG . HIS A 1 162 ? -20.835 -19.318 0.270 1.00 50.74 ? 175 HIS A CG 1 ATOM 1262 N ND1 . HIS A 1 162 ? -21.906 -19.479 -0.529 1.00 52.07 ? 175 HIS A ND1 1 ATOM 1263 C CD2 . HIS A 1 162 ? -19.797 -20.049 -0.309 1.00 65.03 ? 175 HIS A CD2 1 ATOM 1264 C CE1 . HIS A 1 162 ? -21.573 -20.268 -1.571 1.00 61.23 ? 175 HIS A CE1 1 ATOM 1265 N NE2 . HIS A 1 162 ? -20.282 -20.616 -1.434 1.00 65.92 ? 175 HIS A NE2 1 ATOM 1266 N N . LEU A 1 163 ? -21.180 -18.422 5.075 1.00 27.40 ? 176 LEU A N 1 ATOM 1267 C CA . LEU A 1 163 ? -20.649 -17.692 6.245 1.00 24.47 ? 176 LEU A CA 1 ATOM 1268 C C . LEU A 1 163 ? -19.851 -18.604 7.160 1.00 27.66 ? 176 LEU A C 1 ATOM 1269 O O . LEU A 1 163 ? -20.139 -19.803 7.264 1.00 25.73 ? 176 LEU A O 1 ATOM 1270 C CB . LEU A 1 163 ? -21.782 -17.052 7.053 1.00 26.67 ? 176 LEU A CB 1 ATOM 1271 C CG . LEU A 1 163 ? -22.187 -15.619 6.725 1.00 38.85 ? 176 LEU A CG 1 ATOM 1272 C CD1 . LEU A 1 163 ? -22.317 -15.396 5.230 1.00 41.33 ? 176 LEU A CD1 1 ATOM 1273 C CD2 . LEU A 1 163 ? -23.476 -15.283 7.446 1.00 35.39 ? 176 LEU A CD2 1 ATOM 1274 N N . THR A 1 164 ? -18.867 -18.028 7.843 1.00 22.64 ? 177 THR A N 1 ATOM 1275 C CA . THR A 1 164 ? -18.065 -18.763 8.817 1.00 22.47 ? 177 THR A CA 1 ATOM 1276 C C . THR A 1 164 ? -18.425 -18.326 10.237 1.00 21.88 ? 177 THR A C 1 ATOM 1277 O O . THR A 1 164 ? -19.188 -17.378 10.428 1.00 22.63 ? 177 THR A O 1 ATOM 1278 C CB . THR A 1 164 ? -16.557 -18.555 8.595 1.00 23.33 ? 177 THR A CB 1 ATOM 1279 O OG1 . THR A 1 164 ? -16.160 -17.281 9.129 1.00 21.79 ? 177 THR A OG1 1 ATOM 1280 C CG2 . THR A 1 164 ? -16.208 -18.618 7.116 1.00 25.29 ? 177 THR A CG2 1 ATOM 1281 N N . LEU A 1 165 ? -17.853 -19.002 11.228 1.00 22.01 ? 178 LEU A N 1 ATOM 1282 C CA . LEU A 1 165 ? -18.150 -18.729 12.633 1.00 22.57 ? 178 LEU A CA 1 ATOM 1283 C C . LEU A 1 165 ? -17.650 -17.378 13.117 1.00 21.66 ? 178 LEU A C 1 ATOM 1284 O O . LEU A 1 165 ? -18.138 -16.883 14.113 1.00 24.23 ? 178 LEU A O 1 ATOM 1285 C CB . LEU A 1 165 ? -17.577 -19.827 13.530 1.00 27.82 ? 178 LEU A CB 1 ATOM 1286 C CG . LEU A 1 165 ? -18.389 -21.127 13.536 1.00 31.53 ? 178 LEU A CG 1 ATOM 1287 C CD1 . LEU A 1 165 ? -17.591 -22.243 14.194 1.00 37.71 ? 178 LEU A CD1 1 ATOM 1288 C CD2 . LEU A 1 165 ? -19.723 -20.915 14.240 1.00 35.27 ? 178 LEU A CD2 1 ATOM 1289 N N . THR A 1 166 ? -16.699 -16.778 12.408 1.00 19.53 ? 179 THR A N 1 ATOM 1290 C CA . THR A 1 166 ? -16.103 -15.504 12.849 1.00 18.36 ? 179 THR A CA 1 ATOM 1291 C C . THR A 1 166 ? -16.652 -14.316 12.041 1.00 16.50 ? 179 THR A C 1 ATOM 1292 O O . THR A 1 166 ? -15.996 -13.268 11.899 1.00 16.21 ? 179 THR A O 1 ATOM 1293 C CB . THR A 1 166 ? -14.571 -15.568 12.784 1.00 18.38 ? 179 THR A CB 1 ATOM 1294 O OG1 . THR A 1 166 ? -14.176 -15.807 11.434 1.00 18.95 ? 179 THR A OG1 1 ATOM 1295 C CG2 . THR A 1 166 ? -14.027 -16.675 13.690 1.00 19.12 ? 179 THR A CG2 1 ATOM 1296 N N . MET A 1 167 ? -17.872 -14.476 11.548 1.00 18.05 ? 180 MET A N 1 ATOM 1297 C CA . MET A 1 167 ? -18.601 -13.449 10.834 1.00 16.58 ? 180 MET A CA 1 ATOM 1298 C C . MET A 1 167 ? -19.873 -13.148 11.585 1.00 19.82 ? 180 MET A C 1 ATOM 1299 O O . MET A 1 167 ? -20.494 -14.051 12.154 1.00 22.66 ? 180 MET A O 1 ATOM 1300 C CB . MET A 1 167 ? -18.931 -13.900 9.420 1.00 18.96 ? 180 MET A CB 1 ATOM 1301 C CG . MET A 1 167 ? -17.703 -14.026 8.552 1.00 19.05 ? 180 MET A CG 1 ATOM 1302 S SD . MET A 1 167 ? -18.063 -14.781 6.972 1.00 18.90 ? 180 MET A SD 1 ATOM 1303 C CE . MET A 1 167 ? -16.387 -14.940 6.355 1.00 21.83 ? 180 MET A CE 1 ATOM 1304 N N . LEU A 1 168 ? -20.254 -11.886 11.620 1.00 17.45 ? 181 LEU A N 1 ATOM 1305 C CA . LEU A 1 168 ? -21.563 -11.542 12.147 1.00 17.82 ? 181 LEU A CA 1 ATOM 1306 C C . LEU A 1 168 ? -22.272 -10.542 11.263 1.00 16.95 ? 181 LEU A C 1 ATOM 1307 O O . LEU A 1 168 ? -21.651 -9.776 10.520 1.00 18.39 ? 181 LEU A O 1 ATOM 1308 C CB . LEU A 1 168 ? -21.512 -11.102 13.615 1.00 28.91 ? 181 LEU A CB 1 ATOM 1309 C CG . LEU A 1 168 ? -21.025 -9.710 13.956 1.00 25.91 ? 181 LEU A CG 1 ATOM 1310 C CD1 . LEU A 1 168 ? -22.090 -8.676 13.648 1.00 25.82 ? 181 LEU A CD1 1 ATOM 1311 C CD2 . LEU A 1 168 ? -20.616 -9.606 15.416 1.00 25.79 ? 181 LEU A CD2 1 ATOM 1312 N N . CYS A 1 169 ? -23.590 -10.577 11.321 1.00 14.64 ? 182 CYS A N 1 ATOM 1313 C CA . CYS A 1 169 ? -24.411 -9.868 10.383 1.00 15.91 ? 182 CYS A CA 1 ATOM 1314 C C . CYS A 1 169 ? -25.357 -8.906 11.033 1.00 15.38 ? 182 CYS A C 1 ATOM 1315 O O . CYS A 1 169 ? -25.674 -9.040 12.235 1.00 16.71 ? 182 CYS A O 1 ATOM 1316 C CB . CYS A 1 169 ? -25.255 -10.876 9.626 1.00 16.67 ? 182 CYS A CB 1 ATOM 1317 S SG . CYS A 1 169 ? -24.287 -12.137 8.798 1.00 18.08 ? 182 CYS A SG 1 ATOM 1318 N N . THR A 1 170 ? -25.844 -7.964 10.241 1.00 13.46 ? 183 THR A N 1 ATOM 1319 C CA . THR A 1 170 ? -26.857 -7.044 10.690 1.00 14.63 ? 183 THR A CA 1 ATOM 1320 C C . THR A 1 170 ? -28.039 -6.942 9.748 1.00 16.99 ? 183 THR A C 1 ATOM 1321 O O . THR A 1 170 ? -28.007 -7.425 8.610 1.00 16.40 ? 183 THR A O 1 ATOM 1322 C CB . THR A 1 170 ? -26.286 -5.623 10.929 1.00 14.89 ? 183 THR A CB 1 ATOM 1323 O OG1 . THR A 1 170 ? -25.893 -5.048 9.675 1.00 14.04 ? 183 THR A OG1 1 ATOM 1324 C CG2 . THR A 1 170 ? -25.094 -5.646 11.907 1.00 15.43 ? 183 THR A CG2 1 ATOM 1325 N N . ARG A 1 171 ? -29.107 -6.348 10.269 1.00 18.55 ? 184 ARG A N 1 ATOM 1326 C CA . ARG A 1 171 ? -30.247 -5.926 9.465 1.00 20.26 ? 184 ARG A CA 1 ATOM 1327 C C . ARG A 1 171 ? -30.729 -4.563 9.958 1.00 17.96 ? 184 ARG A C 1 ATOM 1328 O O . ARG A 1 171 ? -30.383 -4.125 11.068 1.00 17.60 ? 184 ARG A O 1 ATOM 1329 C CB . ARG A 1 171 ? -31.398 -6.938 9.547 1.00 22.13 ? 184 ARG A CB 1 ATOM 1330 C CG . ARG A 1 171 ? -31.911 -7.144 10.966 1.00 26.30 ? 184 ARG A CG 1 ATOM 1331 C CD . ARG A 1 171 ? -33.271 -7.821 11.003 1.00 34.73 ? 184 ARG A CD 1 ATOM 1332 N NE . ARG A 1 171 ? -33.858 -7.721 12.341 1.00 42.99 ? 184 ARG A NE 1 ATOM 1333 C CZ . ARG A 1 171 ? -34.728 -6.791 12.744 1.00 50.36 ? 184 ARG A CZ 1 ATOM 1334 N NH1 . ARG A 1 171 ? -35.179 -5.849 11.917 1.00 56.58 ? 184 ARG A NH1 1 ATOM 1335 N NH2 . ARG A 1 171 ? -35.169 -6.813 13.998 1.00 55.57 ? 184 ARG A NH2 1 ATOM 1336 N N . SER A 1 172 ? -31.512 -3.887 9.132 1.00 19.72 ? 185 SER A N 1 ATOM 1337 C CA . SER A 1 172 ? -32.207 -2.673 9.540 1.00 21.41 ? 185 SER A CA 1 ATOM 1338 C C . SER A 1 172 ? -33.249 -2.957 10.613 1.00 24.47 ? 185 SER A C 1 ATOM 1339 O O . SER A 1 172 ? -33.829 -4.037 10.646 1.00 25.93 ? 185 SER A O 1 ATOM 1340 C CB . SER A 1 172 ? -32.906 -2.045 8.344 1.00 22.18 ? 185 SER A CB 1 ATOM 1341 O OG . SER A 1 172 ? -33.606 -0.873 8.718 1.00 22.51 ? 185 SER A OG 1 ATOM 1342 N N . GLY A 1 173 ? -33.492 -1.965 11.464 1.00 26.63 ? 186 GLY A N 1 ATOM 1343 C CA . GLY A 1 173 ? -34.558 -2.055 12.461 1.00 30.29 ? 186 GLY A CA 1 ATOM 1344 C C . GLY A 1 173 ? -35.946 -1.877 11.871 1.00 33.53 ? 186 GLY A C 1 ATOM 1345 O O . GLY A 1 173 ? -36.940 -2.163 12.539 1.00 35.40 ? 186 GLY A O 1 ATOM 1346 N N . ASP A 1 174 A -36.022 -1.395 10.630 1.00 28.58 ? 186 ASP A N 1 ATOM 1347 C CA . ASP A 1 174 A -37.302 -1.152 9.964 1.00 30.68 ? 186 ASP A CA 1 ATOM 1348 C C . ASP A 1 174 A -37.273 -1.567 8.480 1.00 30.33 ? 186 ASP A C 1 ATOM 1349 O O . ASP A 1 174 A -36.432 -2.376 8.080 1.00 29.83 ? 186 ASP A O 1 ATOM 1350 C CB . ASP A 1 174 A -37.723 0.313 10.165 1.00 31.54 ? 186 ASP A CB 1 ATOM 1351 C CG . ASP A 1 174 A -36.745 1.308 9.561 1.00 33.90 ? 186 ASP A CG 1 ATOM 1352 O OD1 . ASP A 1 174 A -35.916 0.932 8.698 1.00 28.51 ? 186 ASP A OD1 1 ATOM 1353 O OD2 . ASP A 1 174 A -36.811 2.488 9.961 1.00 36.50 ? 186 ASP A OD2 1 ATOM 1354 N N . SER A 1 175 B -38.190 -1.029 7.674 1.00 30.46 ? 186 SER A N 1 ATOM 1355 C CA . SER A 1 175 B -38.336 -1.435 6.279 1.00 31.72 ? 186 SER A CA 1 ATOM 1356 C C . SER A 1 175 B -37.340 -0.770 5.328 1.00 31.63 ? 186 SER A C 1 ATOM 1357 O O . SER A 1 175 B -37.271 -1.144 4.154 1.00 30.75 ? 186 SER A O 1 ATOM 1358 C CB . SER A 1 175 B -39.752 -1.124 5.796 1.00 30.81 ? 186 SER A CB 1 ATOM 1359 O OG . SER A 1 175 B -40.002 0.269 5.876 1.00 36.11 ? 186 SER A OG 1 ATOM 1360 N N . HIS A 1 176 ? -36.592 0.220 5.817 1.00 33.32 ? 187 HIS A N 1 ATOM 1361 C CA . HIS A 1 176 ? -35.586 0.907 4.997 1.00 30.21 ? 187 HIS A CA 1 ATOM 1362 C C . HIS A 1 176 ? -34.284 0.157 4.981 1.00 24.93 ? 187 HIS A C 1 ATOM 1363 O O . HIS A 1 176 ? -33.930 -0.501 5.956 1.00 22.07 ? 187 HIS A O 1 ATOM 1364 C CB . HIS A 1 176 ? -35.356 2.319 5.519 1.00 36.11 ? 187 HIS A CB 1 ATOM 1365 C CG . HIS A 1 176 ? -36.569 3.204 5.417 1.00 43.41 ? 187 HIS A CG 1 ATOM 1366 N ND1 . HIS A 1 176 ? -37.586 3.141 6.299 1.00 50.25 ? 187 HIS A ND1 1 ATOM 1367 C CD2 . HIS A 1 176 ? -36.910 4.185 4.490 1.00 53.78 ? 187 HIS A CD2 1 ATOM 1368 C CE1 . HIS A 1 176 ? -38.529 4.038 5.957 1.00 53.42 ? 187 HIS A CE1 1 ATOM 1369 N NE2 . HIS A 1 176 ? -38.115 4.677 4.850 1.00 64.64 ? 187 HIS A NE2 1 ATOM 1370 N N . ARG A 1 177 ? -33.565 0.235 3.863 1.00 24.31 ? 188 ARG A N 1 ATOM 1371 C CA . ARG A 1 177 ? -32.200 -0.291 3.794 1.00 19.77 ? 188 ARG A CA 1 ATOM 1372 C C . ARG A 1 177 ? -31.270 0.554 4.648 1.00 19.23 ? 188 ARG A C 1 ATOM 1373 O O . ARG A 1 177 ? -31.198 1.779 4.508 1.00 18.33 ? 188 ARG A O 1 ATOM 1374 C CB . ARG A 1 177 ? -31.680 -0.353 2.350 1.00 22.40 ? 188 ARG A CB 1 ATOM 1375 C CG . ARG A 1 177 ? -32.427 -1.365 1.492 1.00 22.08 ? 188 ARG A CG 1 ATOM 1376 C CD . ARG A 1 177 ? -31.806 -1.502 0.111 1.00 22.08 ? 188 ARG A CD 1 ATOM 1377 N NE . ARG A 1 177 ? -32.531 -2.486 -0.688 1.00 28.39 ? 188 ARG A NE 1 ATOM 1378 C CZ . ARG A 1 177 ? -32.225 -2.827 -1.933 1.00 30.02 ? 188 ARG A CZ 1 ATOM 1379 N NH1 . ARG A 1 177 ? -31.191 -2.270 -2.547 1.00 30.53 ? 188 ARG A NH1 1 ATOM 1380 N NH2 . ARG A 1 177 ? -32.962 -3.731 -2.567 1.00 34.01 ? 188 ARG A NH2 1 ATOM 1381 N N . ARG A 1 178 A -30.573 -0.122 5.552 1.00 17.22 ? 188 ARG A N 1 ATOM 1382 C CA . ARG A 1 178 A -29.655 0.532 6.472 1.00 17.72 ? 188 ARG A CA 1 ATOM 1383 C C . ARG A 1 178 A -28.437 -0.358 6.648 1.00 15.80 ? 188 ARG A C 1 ATOM 1384 O O . ARG A 1 178 A -28.557 -1.558 6.902 1.00 16.11 ? 188 ARG A O 1 ATOM 1385 C CB . ARG A 1 178 A -30.347 0.804 7.817 1.00 19.61 ? 188 ARG A CB 1 ATOM 1386 C CG . ARG A 1 178 A -31.595 1.670 7.699 1.00 21.64 ? 188 ARG A CG 1 ATOM 1387 C CD . ARG A 1 178 A -32.105 2.104 9.060 1.00 21.71 ? 188 ARG A CD 1 ATOM 1388 N NE . ARG A 1 178 A -33.434 2.714 8.989 1.00 22.55 ? 188 ARG A NE 1 ATOM 1389 C CZ . ARG A 1 178 A -33.687 3.975 8.638 1.00 25.67 ? 188 ARG A CZ 1 ATOM 1390 N NH1 . ARG A 1 178 A -32.716 4.819 8.308 1.00 26.97 ? 188 ARG A NH1 1 ATOM 1391 N NH2 . ARG A 1 178 A -34.941 4.412 8.625 1.00 31.01 ? 188 ARG A NH2 1 ATOM 1392 N N . GLY A 1 179 ? -27.248 0.224 6.498 1.00 14.35 ? 189 GLY A N 1 ATOM 1393 C CA . GLY A 1 179 ? -26.036 -0.564 6.583 1.00 14.37 ? 189 GLY A CA 1 ATOM 1394 C C . GLY A 1 179 ? -24.868 0.167 5.982 1.00 13.99 ? 189 GLY A C 1 ATOM 1395 O O . GLY A 1 179 ? -24.853 1.397 5.962 1.00 14.33 ? 189 GLY A O 1 ATOM 1396 N N . PHE A 1 180 ? -23.865 -0.592 5.530 1.00 13.24 ? 190 PHE A N 1 ATOM 1397 C CA . PHE A 1 180 ? -22.649 0.007 5.005 1.00 12.28 ? 190 PHE A CA 1 ATOM 1398 C C . PHE A 1 180 ? -22.563 -0.095 3.484 1.00 11.00 ? 190 PHE A C 1 ATOM 1399 O O . PHE A 1 180 ? -23.414 -0.702 2.841 1.00 13.30 ? 190 PHE A O 1 ATOM 1400 C CB . PHE A 1 180 ? -21.416 -0.571 5.697 1.00 12.39 ? 190 PHE A CB 1 ATOM 1401 C CG . PHE A 1 180 ? -21.260 -2.067 5.598 1.00 11.52 ? 190 PHE A CG 1 ATOM 1402 C CD1 . PHE A 1 180 ? -20.962 -2.695 4.385 1.00 13.12 ? 190 PHE A CD1 1 ATOM 1403 C CD2 . PHE A 1 180 ? -21.298 -2.848 6.743 1.00 12.12 ? 190 PHE A CD2 1 ATOM 1404 C CE1 . PHE A 1 180 ? -20.760 -4.063 4.313 1.00 12.17 ? 190 PHE A CE1 1 ATOM 1405 C CE2 . PHE A 1 180 ? -21.098 -4.207 6.673 1.00 11.78 ? 190 PHE A CE2 1 ATOM 1406 C CZ . PHE A 1 180 ? -20.803 -4.814 5.458 1.00 12.60 ? 190 PHE A CZ 1 ATOM 1407 N N . CYS A 1 181 ? -21.555 0.551 2.910 1.00 11.10 ? 191 CYS A N 1 ATOM 1408 C CA . CYS A 1 181 ? -21.333 0.475 1.461 1.00 11.54 ? 191 CYS A CA 1 ATOM 1409 C C . CYS A 1 181 ? -19.834 0.600 1.188 1.00 11.76 ? 191 CYS A C 1 ATOM 1410 O O . CYS A 1 181 ? -19.011 0.545 2.111 1.00 11.43 ? 191 CYS A O 1 ATOM 1411 C CB . CYS A 1 181 ? -22.170 1.523 0.720 1.00 11.85 ? 191 CYS A CB 1 ATOM 1412 S SG . CYS A 1 181 ? -22.505 1.183 -1.032 1.00 15.89 ? 191 CYS A SG 1 ATOM 1413 N N . SER A 1 182 ? -19.447 0.683 -0.082 1.00 12.66 ? 192 SER A N 1 ATOM 1414 C CA . SER A 1 182 ? -18.020 0.744 -0.415 1.00 12.55 ? 192 SER A CA 1 ATOM 1415 C C . SER A 1 182 ? -17.321 1.893 0.294 1.00 10.90 ? 192 SER A C 1 ATOM 1416 O O . SER A 1 182 ? -17.862 3.007 0.356 1.00 11.55 ? 192 SER A O 1 ATOM 1417 C CB . SER A 1 182 ? -17.824 0.910 -1.921 1.00 14.92 ? 192 SER A CB 1 ATOM 1418 O OG . SER A 1 182 ? -18.589 -0.031 -2.660 1.00 20.41 ? 192 SER A OG 1 ATOM 1419 N N . ALA A 1 183 ? -16.129 1.608 0.808 1.00 10.77 ? 193 ALA A N 1 ATOM 1420 C CA . ALA A 1 183 ? -15.269 2.528 1.526 1.00 10.83 ? 193 ALA A CA 1 ATOM 1421 C C . ALA A 1 183 ? -15.704 2.757 2.967 1.00 12.08 ? 193 ALA A C 1 ATOM 1422 O O . ALA A 1 183 ? -15.113 3.584 3.635 1.00 12.21 ? 193 ALA A O 1 ATOM 1423 C CB . ALA A 1 183 ? -15.053 3.840 0.780 1.00 11.54 ? 193 ALA A CB 1 ATOM 1424 N N . ASP A 1 184 ? -16.664 1.975 3.434 1.00 11.91 ? 194 ASP A N 1 ATOM 1425 C CA . ASP A 1 184 ? -16.938 1.873 4.876 1.00 10.84 ? 194 ASP A CA 1 ATOM 1426 C C . ASP A 1 184 ? -16.136 0.740 5.526 1.00 10.62 ? 194 ASP A C 1 ATOM 1427 O O . ASP A 1 184 ? -16.101 0.611 6.746 1.00 10.97 ? 194 ASP A O 1 ATOM 1428 C CB . ASP A 1 184 ? -18.430 1.641 5.114 1.00 11.75 ? 194 ASP A CB 1 ATOM 1429 C CG . ASP A 1 184 ? -19.259 2.867 4.841 1.00 12.45 ? 194 ASP A CG 1 ATOM 1430 O OD1 . ASP A 1 184 ? -18.795 3.995 5.173 1.00 12.35 ? 194 ASP A OD1 1 ATOM 1431 O OD2 . ASP A 1 184 ? -20.390 2.720 4.317 1.00 11.51 ? 194 ASP A OD2 1 ATOM 1432 N N . SER A 1 185 ? -15.478 -0.096 4.721 1.00 10.26 ? 195 SER A N 1 ATOM 1433 C CA . SER A 1 185 ? -14.717 -1.216 5.260 1.00 11.44 ? 195 SER A CA 1 ATOM 1434 C C . SER A 1 185 ? -13.713 -0.820 6.296 1.00 11.54 ? 195 SER A C 1 ATOM 1435 O O . SER A 1 185 ? -13.085 0.228 6.188 1.00 12.30 ? 195 SER A O 1 ATOM 1436 C CB . SER A 1 185 ? -13.976 -1.938 4.153 1.00 12.23 ? 195 SER A CB 1 ATOM 1437 O OG . SER A 1 185 ? -14.912 -2.560 3.315 1.00 12.39 ? 195 SER A OG 1 ATOM 1438 N N . GLY A 1 186 ? -13.576 -1.674 7.301 1.00 11.44 ? 196 GLY A N 1 ATOM 1439 C CA . GLY A 1 186 ? -12.684 -1.440 8.408 1.00 11.54 ? 196 GLY A CA 1 ATOM 1440 C C . GLY A 1 186 ? -13.245 -0.605 9.538 1.00 12.70 ? 196 GLY A C 1 ATOM 1441 O O . GLY A 1 186 ? -12.636 -0.558 10.603 1.00 12.85 ? 196 GLY A O 1 ATOM 1442 N N . GLY A 1 187 ? -14.397 0.030 9.343 1.00 10.69 ? 197 GLY A N 1 ATOM 1443 C CA . GLY A 1 187 ? -15.042 0.749 10.436 1.00 11.14 ? 197 GLY A CA 1 ATOM 1444 C C . GLY A 1 187 ? -15.697 -0.222 11.393 1.00 10.65 ? 197 GLY A C 1 ATOM 1445 O O . GLY A 1 187 ? -16.144 -1.299 11.003 1.00 11.74 ? 197 GLY A O 1 ATOM 1446 N N . PRO A 1 188 ? -15.825 0.169 12.666 1.00 9.74 ? 198 PRO A N 1 ATOM 1447 C CA . PRO A 1 188 ? -16.414 -0.698 13.658 1.00 11.27 ? 198 PRO A CA 1 ATOM 1448 C C . PRO A 1 188 ? -17.936 -0.665 13.670 1.00 10.77 ? 198 PRO A C 1 ATOM 1449 O O . PRO A 1 188 ? -18.556 0.355 13.393 1.00 12.80 ? 198 PRO A O 1 ATOM 1450 C CB . PRO A 1 188 ? -15.865 -0.149 14.969 1.00 12.19 ? 198 PRO A CB 1 ATOM 1451 C CG . PRO A 1 188 ? -15.694 1.305 14.709 1.00 12.19 ? 198 PRO A CG 1 ATOM 1452 C CD . PRO A 1 188 ? -15.264 1.390 13.265 1.00 11.53 ? 198 PRO A CD 1 ATOM 1453 N N . LEU A 1 189 ? -18.511 -1.834 13.946 1.00 10.95 ? 199 LEU A N 1 ATOM 1454 C CA . LEU A 1 189 ? -19.870 -1.966 14.436 1.00 12.11 ? 199 LEU A CA 1 ATOM 1455 C C . LEU A 1 189 ? -19.769 -1.827 15.947 1.00 11.38 ? 199 LEU A C 1 ATOM 1456 O O . LEU A 1 189 ? -19.118 -2.637 16.607 1.00 12.66 ? 199 LEU A O 1 ATOM 1457 C CB . LEU A 1 189 ? -20.454 -3.323 14.083 1.00 12.84 ? 199 LEU A CB 1 ATOM 1458 C CG . LEU A 1 189 ? -21.920 -3.519 14.450 1.00 12.80 ? 199 LEU A CG 1 ATOM 1459 C CD1 . LEU A 1 189 ? -22.833 -2.650 13.605 1.00 12.70 ? 199 LEU A CD1 1 ATOM 1460 C CD2 . LEU A 1 189 ? -22.294 -4.998 14.329 1.00 15.82 ? 199 LEU A CD2 1 ATOM 1461 N N . VAL A 1 190 ? -20.386 -0.768 16.469 1.00 12.43 ? 200 VAL A N 1 ATOM 1462 C CA . VAL A 1 190 ? -20.294 -0.423 17.887 1.00 13.71 ? 200 VAL A CA 1 ATOM 1463 C C . VAL A 1 190 ? -21.617 -0.821 18.539 1.00 13.80 ? 200 VAL A C 1 ATOM 1464 O O . VAL A 1 190 ? -22.679 -0.362 18.127 1.00 14.98 ? 200 VAL A O 1 ATOM 1465 C CB . VAL A 1 190 ? -20.002 1.081 18.085 1.00 13.47 ? 200 VAL A CB 1 ATOM 1466 C CG1 . VAL A 1 190 ? -19.983 1.437 19.578 1.00 14.15 ? 200 VAL A CG1 1 ATOM 1467 C CG2 . VAL A 1 190 ? -18.679 1.485 17.419 1.00 12.82 ? 200 VAL A CG2 1 ATOM 1468 N N . CYS A 1 191 ? -21.519 -1.721 19.515 1.00 14.99 ? 201 CYS A N 1 ATOM 1469 C CA . CYS A 1 191 ? -22.669 -2.162 20.322 1.00 18.16 ? 201 CYS A CA 1 ATOM 1470 C C . CYS A 1 191 ? -22.250 -2.037 21.781 1.00 17.00 ? 201 CYS A C 1 ATOM 1471 O O . CYS A 1 191 ? -21.216 -2.560 22.182 1.00 16.75 ? 201 CYS A O 1 ATOM 1472 C CB . CYS A 1 191 ? -23.068 -3.613 20.008 1.00 19.39 ? 201 CYS A CB 1 ATOM 1473 S SG . CYS A 1 191 ? -22.988 -4.116 18.262 1.00 19.33 ? 201 CYS A SG 1 ATOM 1474 N N . ARG A 1 192 ? -23.060 -1.321 22.564 1.00 22.99 ? 202 ARG A N 1 ATOM 1475 C CA . ARG A 1 192 ? -22.746 -1.085 23.979 1.00 24.78 ? 202 ARG A CA 1 ATOM 1476 C C . ARG A 1 192 ? -21.320 -0.546 24.151 1.00 19.69 ? 202 ARG A C 1 ATOM 1477 O O . ARG A 1 192 ? -20.581 -0.998 25.014 1.00 20.76 ? 202 ARG A O 1 ATOM 1478 C CB . ARG A 1 192 ? -22.951 -2.372 24.801 1.00 33.57 ? 202 ARG A CB 1 ATOM 1479 C CG . ARG A 1 192 ? -24.154 -2.361 25.732 1.00 50.42 ? 202 ARG A CG 1 ATOM 1480 C CD . ARG A 1 192 ? -25.478 -2.357 24.984 1.00 64.71 ? 202 ARG A CD 1 ATOM 1481 N NE . ARG A 1 192 ? -26.615 -2.232 25.901 1.00 82.10 ? 202 ARG A NE 1 ATOM 1482 C CZ . ARG A 1 192 ? -27.196 -3.239 26.560 1.00 84.80 ? 202 ARG A CZ 1 ATOM 1483 N NH1 . ARG A 1 192 ? -26.768 -4.491 26.425 1.00 87.72 ? 202 ARG A NH1 1 ATOM 1484 N NH2 . ARG A 1 192 ? -28.222 -2.987 27.368 1.00 82.18 ? 202 ARG A NH2 1 ATOM 1485 N N . ASN A 1 193 ? -20.944 0.420 23.309 1.00 18.51 ? 207 ASN A N 1 ATOM 1486 C CA . ASN A 1 193 ? -19.635 1.085 23.390 1.00 19.57 ? 207 ASN A CA 1 ATOM 1487 C C . ASN A 1 193 ? -18.431 0.149 23.261 1.00 16.98 ? 207 ASN A C 1 ATOM 1488 O O . ASN A 1 193 ? -17.349 0.418 23.786 1.00 18.68 ? 207 ASN A O 1 ATOM 1489 C CB . ASN A 1 193 ? -19.526 1.926 24.680 1.00 24.17 ? 207 ASN A CB 1 ATOM 1490 C CG . ASN A 1 193 ? -20.155 3.293 24.532 1.00 39.41 ? 207 ASN A CG 1 ATOM 1491 O OD1 . ASN A 1 193 ? -19.701 4.111 23.729 1.00 53.90 ? 207 ASN A OD1 1 ATOM 1492 N ND2 . ASN A 1 193 ? -21.198 3.555 25.311 1.00 45.25 ? 207 ASN A ND2 1 ATOM 1493 N N . ARG A 1 194 ? -18.620 -0.936 22.511 1.00 15.43 ? 208 ARG A N 1 ATOM 1494 C CA . ARG A 1 194 ? -17.539 -1.858 22.185 1.00 15.63 ? 208 ARG A CA 1 ATOM 1495 C C . ARG A 1 194 ? -17.554 -2.163 20.680 1.00 12.58 ? 208 ARG A C 1 ATOM 1496 O O . ARG A 1 194 ? -18.620 -2.227 20.058 1.00 14.97 ? 208 ARG A O 1 ATOM 1497 C CB . ARG A 1 194 ? -17.656 -3.173 22.975 1.00 16.55 ? 208 ARG A CB 1 ATOM 1498 C CG . ARG A 1 194 ? -17.590 -2.998 24.489 1.00 17.93 ? 208 ARG A CG 1 ATOM 1499 C CD . ARG A 1 194 ? -16.197 -2.634 24.979 1.00 18.32 ? 208 ARG A CD 1 ATOM 1500 N NE . ARG A 1 194 ? -16.143 -2.580 26.454 1.00 21.10 ? 208 ARG A NE 1 ATOM 1501 C CZ . ARG A 1 194 ? -16.350 -1.496 27.199 1.00 21.82 ? 208 ARG A CZ 1 ATOM 1502 N NH1 . ARG A 1 194 ? -16.622 -0.314 26.658 1.00 20.76 ? 208 ARG A NH1 1 ATOM 1503 N NH2 . ARG A 1 194 ? -16.271 -1.599 28.523 1.00 26.22 ? 208 ARG A NH2 1 ATOM 1504 N N . ALA A 1 195 ? -16.357 -2.354 20.124 1.00 13.53 ? 209 ALA A N 1 ATOM 1505 C CA . ALA A 1 195 ? -16.196 -2.709 18.695 1.00 12.09 ? 209 ALA A CA 1 ATOM 1506 C C . ALA A 1 195 ? -16.466 -4.203 18.465 1.00 11.12 ? 209 ALA A C 1 ATOM 1507 O O . ALA A 1 195 ? -15.535 -4.995 18.502 1.00 13.36 ? 209 ALA A O 1 ATOM 1508 C CB . ALA A 1 195 ? -14.785 -2.354 18.237 1.00 14.63 ? 209 ALA A CB 1 ATOM 1509 N N . HIS A 1 196 ? -17.731 -4.570 18.300 1.00 12.19 ? 210 HIS A N 1 ATOM 1510 C CA . HIS A 1 196 ? -18.094 -5.982 18.139 1.00 13.98 ? 210 HIS A CA 1 ATOM 1511 C C . HIS A 1 196 ? -17.944 -6.485 16.729 1.00 14.17 ? 210 HIS A C 1 ATOM 1512 O O . HIS A 1 196 ? -17.813 -7.684 16.521 1.00 14.51 ? 210 HIS A O 1 ATOM 1513 C CB . HIS A 1 196 ? -19.510 -6.244 18.654 1.00 14.99 ? 210 HIS A CB 1 ATOM 1514 C CG . HIS A 1 196 ? -19.567 -6.431 20.141 1.00 17.58 ? 210 HIS A CG 1 ATOM 1515 N ND1 . HIS A 1 196 ? -19.192 -7.578 20.735 1.00 29.02 ? 210 HIS A ND1 1 ATOM 1516 C CD2 . HIS A 1 196 ? -19.953 -5.562 21.157 1.00 22.37 ? 210 HIS A CD2 1 ATOM 1517 C CE1 . HIS A 1 196 ? -19.338 -7.450 22.073 1.00 29.19 ? 210 HIS A CE1 1 ATOM 1518 N NE2 . HIS A 1 196 ? -19.817 -6.227 22.326 1.00 26.48 ? 210 HIS A NE2 1 ATOM 1519 N N . GLY A 1 197 ? -17.974 -5.585 15.752 1.00 12.28 ? 211 GLY A N 1 ATOM 1520 C CA . GLY A 1 197 ? -17.810 -5.961 14.357 1.00 12.82 ? 211 GLY A CA 1 ATOM 1521 C C . GLY A 1 197 ? -16.875 -5.024 13.622 1.00 12.70 ? 211 GLY A C 1 ATOM 1522 O O . GLY A 1 197 ? -16.610 -3.898 14.073 1.00 12.12 ? 211 GLY A O 1 ATOM 1523 N N . LEU A 1 198 ? -16.375 -5.495 12.478 1.00 12.34 ? 212 LEU A N 1 ATOM 1524 C CA . LEU A 1 198 ? -15.626 -4.647 11.565 1.00 11.40 ? 212 LEU A CA 1 ATOM 1525 C C . LEU A 1 198 ? -16.224 -4.826 10.183 1.00 11.24 ? 212 LEU A C 1 ATOM 1526 O O . LEU A 1 198 ? -16.401 -5.960 9.718 1.00 11.47 ? 212 LEU A O 1 ATOM 1527 C CB . LEU A 1 198 ? -14.140 -5.003 11.554 1.00 14.55 ? 212 LEU A CB 1 ATOM 1528 C CG . LEU A 1 198 ? -13.208 -3.815 11.384 1.00 16.09 ? 212 LEU A CG 1 ATOM 1529 C CD1 . LEU A 1 198 ? -13.099 -3.037 12.698 1.00 14.43 ? 212 LEU A CD1 1 ATOM 1530 C CD2 . LEU A 1 198 ? -11.835 -4.273 10.943 1.00 18.48 ? 212 LEU A CD2 1 ATOM 1531 N N . VAL A 1 199 ? -16.546 -3.729 9.509 1.00 10.32 ? 213 VAL A N 1 ATOM 1532 C CA . VAL A 1 199 ? -17.184 -3.795 8.202 1.00 11.57 ? 213 VAL A CA 1 ATOM 1533 C C . VAL A 1 199 ? -16.307 -4.623 7.251 1.00 10.52 ? 213 VAL A C 1 ATOM 1534 O O . VAL A 1 199 ? -15.119 -4.324 7.083 1.00 11.58 ? 213 VAL A O 1 ATOM 1535 C CB . VAL A 1 199 ? -17.381 -2.399 7.589 1.00 11.00 ? 213 VAL A CB 1 ATOM 1536 C CG1 . VAL A 1 199 ? -17.841 -2.521 6.144 1.00 10.85 ? 213 VAL A CG1 1 ATOM 1537 C CG2 . VAL A 1 199 ? -18.369 -1.565 8.401 1.00 10.56 ? 213 VAL A CG2 1 ATOM 1538 N N . SER A 1 200 ? -16.896 -5.650 6.627 1.00 10.82 ? 214 SER A N 1 ATOM 1539 C CA . SER A 1 200 ? -16.135 -6.508 5.693 1.00 11.39 ? 214 SER A CA 1 ATOM 1540 C C . SER A 1 200 ? -16.741 -6.577 4.293 1.00 11.25 ? 214 SER A C 1 ATOM 1541 O O . SER A 1 200 ? -16.122 -6.098 3.350 1.00 12.52 ? 214 SER A O 1 ATOM 1542 C CB . SER A 1 200 ? -15.956 -7.905 6.278 1.00 11.74 ? 214 SER A CB 1 ATOM 1543 O OG . SER A 1 200 ? -15.173 -8.708 5.378 1.00 13.63 ? 214 SER A OG 1 ATOM 1544 N N . PHE A 1 201 ? -17.902 -7.191 4.132 1.00 12.23 ? 215 PHE A N 1 ATOM 1545 C CA . PHE A 1 201 ? -18.467 -7.342 2.791 1.00 12.57 ? 215 PHE A CA 1 ATOM 1546 C C . PHE A 1 201 ? -19.978 -7.383 2.770 1.00 12.15 ? 215 PHE A C 1 ATOM 1547 O O . PHE A 1 201 ? -20.616 -7.651 3.788 1.00 13.19 ? 215 PHE A O 1 ATOM 1548 C CB . PHE A 1 201 ? -17.896 -8.592 2.069 1.00 14.37 ? 215 PHE A CB 1 ATOM 1549 C CG . PHE A 1 201 ? -18.336 -9.909 2.650 1.00 13.97 ? 215 PHE A CG 1 ATOM 1550 C CD1 . PHE A 1 201 ? -19.500 -10.522 2.215 1.00 14.18 ? 215 PHE A CD1 1 ATOM 1551 C CD2 . PHE A 1 201 ? -17.568 -10.571 3.609 1.00 14.41 ? 215 PHE A CD2 1 ATOM 1552 C CE1 . PHE A 1 201 ? -19.901 -11.745 2.729 1.00 14.77 ? 215 PHE A CE1 1 ATOM 1553 C CE2 . PHE A 1 201 ? -17.966 -11.792 4.127 1.00 15.65 ? 215 PHE A CE2 1 ATOM 1554 C CZ . PHE A 1 201 ? -19.133 -12.376 3.684 1.00 15.41 ? 215 PHE A CZ 1 ATOM 1555 N N . SER A 1 202 ? -20.559 -7.157 1.594 1.00 13.85 ? 216 SER A N 1 ATOM 1556 C CA . SER A 1 202 ? -21.980 -7.356 1.408 1.00 13.59 ? 216 SER A CA 1 ATOM 1557 C C . SER A 1 202 ? -22.256 -7.762 -0.044 1.00 15.16 ? 216 SER A C 1 ATOM 1558 O O . SER A 1 202 ? -21.346 -8.236 -0.717 1.00 14.84 ? 216 SER A O 1 ATOM 1559 C CB . SER A 1 202 ? -22.734 -6.103 1.868 1.00 14.92 ? 216 SER A CB 1 ATOM 1560 O OG . SER A 1 202 ? -22.410 -4.963 1.098 1.00 14.12 ? 216 SER A OG 1 ATOM 1561 N N . GLY A 1 203 ? -23.500 -7.618 -0.488 1.00 15.98 ? 217 GLY A N 1 ATOM 1562 C CA . GLY A 1 203 ? -23.915 -8.101 -1.811 1.00 15.30 ? 217 GLY A CA 1 ATOM 1563 C C . GLY A 1 203 ? -23.947 -7.024 -2.866 1.00 16.18 ? 217 GLY A C 1 ATOM 1564 O O . GLY A 1 203 ? -23.429 -5.932 -2.670 1.00 17.94 ? 217 GLY A O 1 ATOM 1565 N N . LEU A 1 204 ? -24.583 -7.330 -3.996 1.00 17.35 ? 218 LEU A N 1 ATOM 1566 C CA . LEU A 1 204 ? -24.548 -6.460 -5.164 1.00 18.99 ? 218 LEU A CA 1 ATOM 1567 C C . LEU A 1 204 ? -25.104 -5.058 -4.882 1.00 17.09 ? 218 LEU A C 1 ATOM 1568 O O . LEU A 1 204 ? -24.603 -4.061 -5.412 1.00 20.05 ? 218 LEU A O 1 ATOM 1569 C CB . LEU A 1 204 ? -25.308 -7.123 -6.325 1.00 22.25 ? 218 LEU A CB 1 ATOM 1570 C CG . LEU A 1 204 ? -25.354 -6.344 -7.651 1.00 23.86 ? 218 LEU A CG 1 ATOM 1571 C CD1 . LEU A 1 204 ? -23.957 -6.165 -8.232 1.00 24.92 ? 218 LEU A CD1 1 ATOM 1572 C CD2 . LEU A 1 204 ? -26.281 -7.036 -8.646 1.00 32.00 ? 218 LEU A CD2 1 ATOM 1573 N N . TRP A 1 205 ? -26.128 -4.981 -4.036 1.00 16.90 ? 219 TRP A N 1 ATOM 1574 C CA . TRP A 1 205 ? -26.762 -3.713 -3.698 1.00 17.58 ? 219 TRP A CA 1 ATOM 1575 C C . TRP A 1 205 ? -26.535 -3.401 -2.247 1.00 15.90 ? 219 TRP A C 1 ATOM 1576 O O . TRP A 1 205 ? -26.868 -4.210 -1.399 1.00 17.27 ? 219 TRP A O 1 ATOM 1577 C CB . TRP A 1 205 ? -28.259 -3.791 -3.983 1.00 20.66 ? 219 TRP A CB 1 ATOM 1578 C CG . TRP A 1 205 ? -28.551 -4.252 -5.384 1.00 23.69 ? 219 TRP A CG 1 ATOM 1579 C CD1 . TRP A 1 205 ? -28.968 -5.513 -5.803 1.00 24.43 ? 219 TRP A CD1 1 ATOM 1580 C CD2 . TRP A 1 205 ? -28.422 -3.467 -6.598 1.00 30.02 ? 219 TRP A CD2 1 ATOM 1581 N NE1 . TRP A 1 205 ? -29.104 -5.550 -7.167 1.00 27.26 ? 219 TRP A NE1 1 ATOM 1582 C CE2 . TRP A 1 205 ? -28.798 -4.348 -7.702 1.00 26.46 ? 219 TRP A CE2 1 ATOM 1583 C CE3 . TRP A 1 205 ? -28.064 -2.163 -6.873 1.00 28.39 ? 219 TRP A CE3 1 ATOM 1584 C CZ2 . TRP A 1 205 ? -28.788 -3.918 -9.018 1.00 31.06 ? 219 TRP A CZ2 1 ATOM 1585 C CZ3 . TRP A 1 205 ? -28.064 -1.734 -8.203 1.00 33.80 ? 219 TRP A CZ3 1 ATOM 1586 C CH2 . TRP A 1 205 ? -28.413 -2.595 -9.248 1.00 33.65 ? 219 TRP A CH2 1 ATOM 1587 N N . CYS A 1 206 ? -25.977 -2.229 -1.942 1.00 15.59 ? 220 CYS A N 1 ATOM 1588 C CA . CYS A 1 206 ? -25.631 -1.909 -0.552 1.00 15.35 ? 220 CYS A CA 1 ATOM 1589 C C . CYS A 1 206 ? -26.858 -1.879 0.369 1.00 15.46 ? 220 CYS A C 1 ATOM 1590 O O . CYS A 1 206 ? -27.858 -1.241 0.075 1.00 17.30 ? 220 CYS A O 1 ATOM 1591 C CB . CYS A 1 206 ? -24.869 -0.597 -0.469 1.00 14.77 ? 220 CYS A CB 1 ATOM 1592 S SG . CYS A 1 206 ? -23.190 -0.769 -1.106 1.00 15.63 ? 220 CYS A SG 1 ATOM 1593 N N . GLY A 1 207 ? -26.768 -2.588 1.491 1.00 15.82 ? 221 GLY A N 1 ATOM 1594 C CA . GLY A 1 207 ? -27.857 -2.615 2.466 1.00 16.73 ? 221 GLY A CA 1 ATOM 1595 C C . GLY A 1 207 ? -29.025 -3.517 2.109 1.00 20.29 ? 221 GLY A C 1 ATOM 1596 O O . GLY A 1 207 ? -30.015 -3.541 2.825 1.00 20.56 ? 221 GLY A O 1 ATOM 1597 N N . ASP A 1 208 ? -28.918 -4.263 1.012 1.00 18.05 ? 222 ASP A N 1 ATOM 1598 C CA . ASP A 1 208 ? -29.984 -5.151 0.565 1.00 20.39 ? 222 ASP A CA 1 ATOM 1599 C C . ASP A 1 208 ? -30.196 -6.235 1.616 1.00 16.68 ? 222 ASP A C 1 ATOM 1600 O O . ASP A 1 208 ? -29.268 -6.969 1.930 1.00 16.63 ? 222 ASP A O 1 ATOM 1601 C CB . ASP A 1 208 ? -29.558 -5.788 -0.759 1.00 18.88 ? 222 ASP A CB 1 ATOM 1602 C CG . ASP A 1 208 ? -30.660 -6.592 -1.438 1.00 20.46 ? 222 ASP A CG 1 ATOM 1603 O OD1 . ASP A 1 208 ? -31.700 -6.881 -0.813 1.00 22.48 ? 222 ASP A OD1 1 ATOM 1604 O OD2 . ASP A 1 208 ? -30.464 -6.956 -2.622 1.00 22.03 ? 222 ASP A OD2 1 ATOM 1605 N N . PRO A 1 209 A -31.438 -6.358 2.140 1.00 20.10 ? 222 PRO A N 1 ATOM 1606 C CA . PRO A 1 209 A -31.698 -7.422 3.104 1.00 20.79 ? 222 PRO A CA 1 ATOM 1607 C C . PRO A 1 209 A -31.546 -8.834 2.546 1.00 18.78 ? 222 PRO A C 1 ATOM 1608 O O . PRO A 1 209 A -31.398 -9.772 3.317 1.00 21.40 ? 222 PRO A O 1 ATOM 1609 C CB . PRO A 1 209 A -33.149 -7.165 3.548 1.00 23.57 ? 222 PRO A CB 1 ATOM 1610 C CG . PRO A 1 209 A -33.737 -6.283 2.507 1.00 27.71 ? 222 PRO A CG 1 ATOM 1611 C CD . PRO A 1 209 A -32.595 -5.465 1.977 1.00 21.83 ? 222 PRO A CD 1 ATOM 1612 N N . LYS A 1 210 ? -31.550 -8.992 1.221 1.00 19.73 ? 223 LYS A N 1 ATOM 1613 C CA . LYS A 1 210 ? -31.289 -10.307 0.629 1.00 22.37 ? 223 LYS A CA 1 ATOM 1614 C C . LYS A 1 210 ? -29.842 -10.757 0.819 1.00 18.80 ? 223 LYS A C 1 ATOM 1615 O O . LYS A 1 210 ? -29.532 -11.946 0.821 1.00 20.84 ? 223 LYS A O 1 ATOM 1616 C CB . LYS A 1 210 ? -31.625 -10.317 -0.872 1.00 28.15 ? 223 LYS A CB 1 ATOM 1617 C CG . LYS A 1 210 ? -33.113 -10.230 -1.186 1.00 33.19 ? 223 LYS A CG 1 ATOM 1618 C CD . LYS A 1 210 ? -33.375 -10.420 -2.677 1.00 40.58 ? 223 LYS A CD 1 ATOM 1619 C CE . LYS A 1 210 ? -34.825 -10.120 -3.039 1.00 51.85 ? 223 LYS A CE 1 ATOM 1620 N NZ . LYS A 1 210 ? -35.789 -11.033 -2.358 1.00 52.11 ? 223 LYS A NZ 1 ATOM 1621 N N . THR A 1 211 ? -28.949 -9.781 0.983 1.00 17.97 ? 224 THR A N 1 ATOM 1622 C CA . THR A 1 211 ? -27.523 -10.046 1.180 1.00 20.85 ? 224 THR A CA 1 ATOM 1623 C C . THR A 1 211 ? -27.045 -9.264 2.409 1.00 19.12 ? 224 THR A C 1 ATOM 1624 O O . THR A 1 211 ? -26.395 -8.229 2.282 1.00 16.54 ? 224 THR A O 1 ATOM 1625 C CB . THR A 1 211 ? -26.688 -9.688 -0.077 1.00 17.92 ? 224 THR A CB 1 ATOM 1626 O OG1 . THR A 1 211 ? -27.022 -8.381 -0.547 1.00 16.99 ? 224 THR A OG1 1 ATOM 1627 C CG2 . THR A 1 211 ? -26.955 -10.711 -1.193 1.00 18.59 ? 224 THR A CG2 1 ATOM 1628 N N . PRO A 1 212 ? -27.370 -9.766 3.618 1.00 17.23 ? 225 PRO A N 1 ATOM 1629 C CA . PRO A 1 212 ? -27.104 -8.996 4.838 1.00 16.87 ? 225 PRO A CA 1 ATOM 1630 C C . PRO A 1 212 ? -25.651 -8.589 4.982 1.00 14.35 ? 225 PRO A C 1 ATOM 1631 O O . PRO A 1 212 ? -24.746 -9.353 4.635 1.00 14.89 ? 225 PRO A O 1 ATOM 1632 C CB . PRO A 1 212 ? -27.483 -9.964 5.960 1.00 17.83 ? 225 PRO A CB 1 ATOM 1633 C CG . PRO A 1 212 ? -28.440 -10.930 5.341 1.00 20.55 ? 225 PRO A CG 1 ATOM 1634 C CD . PRO A 1 212 ? -28.017 -11.061 3.910 1.00 20.91 ? 225 PRO A CD 1 ATOM 1635 N N . ASP A 1 213 ? -25.448 -7.380 5.498 1.00 14.63 ? 226 ASP A N 1 ATOM 1636 C CA . ASP A 1 213 ? -24.113 -6.878 5.799 1.00 14.44 ? 226 ASP A CA 1 ATOM 1637 C C . ASP A 1 213 ? -23.343 -7.845 6.679 1.00 13.61 ? 226 ASP A C 1 ATOM 1638 O O . ASP A 1 213 ? -23.845 -8.264 7.727 1.00 13.99 ? 226 ASP A O 1 ATOM 1639 C CB . ASP A 1 213 ? -24.202 -5.531 6.526 1.00 13.73 ? 226 ASP A CB 1 ATOM 1640 C CG . ASP A 1 213 ? -24.480 -4.372 5.589 1.00 13.96 ? 226 ASP A CG 1 ATOM 1641 O OD1 . ASP A 1 213 ? -24.591 -4.609 4.352 1.00 14.79 ? 226 ASP A OD1 1 ATOM 1642 O OD2 . ASP A 1 213 ? -24.581 -3.222 6.065 1.00 14.21 ? 226 ASP A OD2 1 ATOM 1643 N N . VAL A 1 214 ? -22.119 -8.167 6.275 1.00 12.30 ? 227 VAL A N 1 ATOM 1644 C CA . VAL A 1 214 ? -21.270 -9.058 7.007 1.00 13.78 ? 227 VAL A CA 1 ATOM 1645 C C . VAL A 1 214 ? -20.073 -8.306 7.587 1.00 12.96 ? 227 VAL A C 1 ATOM 1646 O O . VAL A 1 214 ? -19.358 -7.586 6.877 1.00 11.52 ? 227 VAL A O 1 ATOM 1647 C CB . VAL A 1 214 ? -20.802 -10.261 6.145 1.00 13.08 ? 227 VAL A CB 1 ATOM 1648 C CG1 . VAL A 1 214 ? -19.960 -11.226 6.967 1.00 15.52 ? 227 VAL A CG1 1 ATOM 1649 C CG2 . VAL A 1 214 ? -21.999 -10.979 5.530 1.00 15.55 ? 227 VAL A CG2 1 ATOM 1650 N N . TYR A 1 215 ? -19.862 -8.524 8.887 1.00 13.85 ? 228 TYR A N 1 ATOM 1651 C CA . TYR A 1 215 ? -18.768 -7.971 9.646 1.00 12.50 ? 228 TYR A CA 1 ATOM 1652 C C . TYR A 1 215 ? -17.844 -9.070 10.142 1.00 13.24 ? 228 TYR A C 1 ATOM 1653 O O . TYR A 1 215 ? -18.280 -10.185 10.443 1.00 13.03 ? 228 TYR A O 1 ATOM 1654 C CB . TYR A 1 215 ? -19.328 -7.273 10.892 1.00 12.38 ? 228 TYR A CB 1 ATOM 1655 C CG . TYR A 1 215 ? -20.151 -6.048 10.618 1.00 12.80 ? 228 TYR A CG 1 ATOM 1656 C CD1 . TYR A 1 215 ? -19.605 -4.784 10.776 1.00 11.66 ? 228 TYR A CD1 1 ATOM 1657 C CD2 . TYR A 1 215 ? -21.479 -6.133 10.238 1.00 12.73 ? 228 TYR A CD2 1 ATOM 1658 C CE1 . TYR A 1 215 ? -20.329 -3.649 10.523 1.00 11.86 ? 228 TYR A CE1 1 ATOM 1659 C CE2 . TYR A 1 215 ? -22.228 -4.987 9.985 1.00 13.21 ? 228 TYR A CE2 1 ATOM 1660 C CZ . TYR A 1 215 ? -21.643 -3.745 10.144 1.00 11.33 ? 228 TYR A CZ 1 ATOM 1661 O OH . TYR A 1 215 ? -22.346 -2.584 9.907 1.00 12.90 ? 228 TYR A OH 1 ATOM 1662 N N . THR A 1 216 ? -16.574 -8.747 10.277 1.00 12.28 ? 229 THR A N 1 ATOM 1663 C CA . THR A 1 216 ? -15.658 -9.547 11.057 1.00 13.09 ? 229 THR A CA 1 ATOM 1664 C C . THR A 1 216 ? -16.116 -9.528 12.514 1.00 13.33 ? 229 THR A C 1 ATOM 1665 O O . THR A 1 216 ? -16.367 -8.459 13.082 1.00 14.11 ? 229 THR A O 1 ATOM 1666 C CB . THR A 1 216 ? -14.254 -8.944 10.973 1.00 13.21 ? 229 THR A CB 1 ATOM 1667 O OG1 . THR A 1 216 ? -13.865 -8.868 9.598 1.00 14.81 ? 229 THR A OG1 1 ATOM 1668 C CG2 . THR A 1 216 ? -13.229 -9.769 11.758 1.00 14.72 ? 229 THR A CG2 1 ATOM 1669 N N . GLN A 1 217 ? -16.296 -10.706 13.100 1.00 12.80 ? 230 GLN A N 1 ATOM 1670 C CA . GLN A 1 217 ? -16.662 -10.831 14.497 1.00 14.89 ? 230 GLN A CA 1 ATOM 1671 C C . GLN A 1 217 ? -15.424 -10.562 15.333 1.00 13.04 ? 230 GLN A C 1 ATOM 1672 O O . GLN A 1 217 ? -14.595 -11.438 15.534 1.00 14.99 ? 230 GLN A O 1 ATOM 1673 C CB . GLN A 1 217 ? -17.185 -12.232 14.786 1.00 14.31 ? 230 GLN A CB 1 ATOM 1674 C CG . GLN A 1 217 ? -17.714 -12.384 16.211 1.00 17.23 ? 230 GLN A CG 1 ATOM 1675 C CD . GLN A 1 217 ? -17.506 -13.769 16.768 1.00 25.66 ? 230 GLN A CD 1 ATOM 1676 O OE1 . GLN A 1 217 ? -18.063 -14.742 16.269 1.00 28.69 ? 230 GLN A OE1 1 ATOM 1677 N NE2 . GLN A 1 217 ? -16.715 -13.863 17.820 1.00 28.38 ? 230 GLN A NE2 1 ATOM 1678 N N . VAL A 1 218 ? -15.310 -9.342 15.863 1.00 12.42 ? 231 VAL A N 1 ATOM 1679 C CA . VAL A 1 218 ? -14.075 -8.873 16.478 1.00 13.78 ? 231 VAL A CA 1 ATOM 1680 C C . VAL A 1 218 ? -13.643 -9.667 17.725 1.00 14.25 ? 231 VAL A C 1 ATOM 1681 O O . VAL A 1 218 ? -12.439 -9.879 17.948 1.00 14.02 ? 231 VAL A O 1 ATOM 1682 C CB . VAL A 1 218 ? -14.173 -7.369 16.798 1.00 13.29 ? 231 VAL A CB 1 ATOM 1683 C CG1 . VAL A 1 218 ? -12.989 -6.907 17.644 1.00 15.94 ? 231 VAL A CG1 1 ATOM 1684 C CG2 . VAL A 1 218 ? -14.262 -6.557 15.504 1.00 13.50 ? 231 VAL A CG2 1 ATOM 1685 N N . SER A 1 219 ? -14.605 -10.151 18.509 1.00 14.26 ? 232 SER A N 1 ATOM 1686 C CA . SER A 1 219 ? -14.221 -10.877 19.727 1.00 16.94 ? 232 SER A CA 1 ATOM 1687 C C . SER A 1 219 ? -13.314 -12.085 19.432 1.00 16.39 ? 232 SER A C 1 ATOM 1688 O O . SER A 1 219 ? -12.454 -12.424 20.244 1.00 17.82 ? 232 SER A O 1 ATOM 1689 C CB . SER A 1 219 ? -15.439 -11.287 20.550 1.00 21.51 ? 232 SER A CB 1 ATOM 1690 O OG . SER A 1 219 ? -16.258 -12.177 19.843 1.00 23.78 ? 232 SER A OG 1 ATOM 1691 N N . ALA A 1 220 ? -13.476 -12.710 18.267 1.00 16.90 ? 233 ALA A N 1 ATOM 1692 C CA . ALA A 1 220 ? -12.646 -13.859 17.885 1.00 16.02 ? 233 ALA A CA 1 ATOM 1693 C C . ALA A 1 220 ? -11.193 -13.483 17.628 1.00 16.92 ? 233 ALA A C 1 ATOM 1694 O O . ALA A 1 220 ? -10.309 -14.341 17.641 1.00 20.09 ? 233 ALA A O 1 ATOM 1695 C CB . ALA A 1 220 ? -13.237 -14.563 16.657 1.00 18.06 ? 233 ALA A CB 1 ATOM 1696 N N . PHE A 1 221 ? -10.949 -12.195 17.399 1.00 13.84 ? 234 PHE A N 1 ATOM 1697 C CA . PHE A 1 221 ? -9.631 -11.685 17.032 1.00 14.65 ? 234 PHE A CA 1 ATOM 1698 C C . PHE A 1 221 ? -8.924 -10.866 18.118 1.00 13.04 ? 234 PHE A C 1 ATOM 1699 O O . PHE A 1 221 ? -7.803 -10.423 17.921 1.00 13.88 ? 234 PHE A O 1 ATOM 1700 C CB . PHE A 1 221 ? -9.753 -10.878 15.745 1.00 14.60 ? 234 PHE A CB 1 ATOM 1701 C CG . PHE A 1 221 ? -10.246 -11.690 14.593 1.00 14.46 ? 234 PHE A CG 1 ATOM 1702 C CD1 . PHE A 1 221 ? -9.352 -12.427 13.834 1.00 17.03 ? 234 PHE A CD1 1 ATOM 1703 C CD2 . PHE A 1 221 ? -11.602 -11.789 14.314 1.00 15.33 ? 234 PHE A CD2 1 ATOM 1704 C CE1 . PHE A 1 221 ? -9.806 -13.210 12.783 1.00 18.28 ? 234 PHE A CE1 1 ATOM 1705 C CE2 . PHE A 1 221 ? -12.064 -12.568 13.267 1.00 16.15 ? 234 PHE A CE2 1 ATOM 1706 C CZ . PHE A 1 221 ? -11.157 -13.287 12.497 1.00 17.55 ? 234 PHE A CZ 1 ATOM 1707 N N . VAL A 1 222 ? -9.585 -10.674 19.261 1.00 15.26 ? 235 VAL A N 1 ATOM 1708 C CA . VAL A 1 222 ? -9.028 -9.855 20.340 1.00 14.10 ? 235 VAL A CA 1 ATOM 1709 C C . VAL A 1 222 ? -7.653 -10.337 20.794 1.00 13.95 ? 235 VAL A C 1 ATOM 1710 O O . VAL A 1 222 ? -6.731 -9.546 20.941 1.00 14.82 ? 235 VAL A O 1 ATOM 1711 C CB . VAL A 1 222 ? -9.998 -9.747 21.535 1.00 16.33 ? 235 VAL A CB 1 ATOM 1712 C CG1 . VAL A 1 222 ? -9.287 -9.124 22.727 1.00 17.23 ? 235 VAL A CG1 1 ATOM 1713 C CG2 . VAL A 1 222 ? -11.221 -8.926 21.145 1.00 16.10 ? 235 VAL A CG2 1 ATOM 1714 N N . ALA A 1 223 ? -7.508 -11.646 21.020 1.00 16.89 ? 236 ALA A N 1 ATOM 1715 C CA . ALA A 1 223 ? -6.219 -12.181 21.452 1.00 17.66 ? 236 ALA A CA 1 ATOM 1716 C C . ALA A 1 223 ? -5.104 -11.864 20.452 1.00 16.13 ? 236 ALA A C 1 ATOM 1717 O O . ALA A 1 223 ? -4.037 -11.397 20.817 1.00 18.63 ? 236 ALA A O 1 ATOM 1718 C CB . ALA A 1 223 ? -6.322 -13.682 21.687 1.00 16.66 ? 236 ALA A CB 1 ATOM 1719 N N . TRP A 1 224 ? -5.380 -12.085 19.175 1.00 16.74 ? 237 TRP A N 1 ATOM 1720 C CA . TRP A 1 224 ? -4.422 -11.774 18.137 1.00 16.34 ? 237 TRP A CA 1 ATOM 1721 C C . TRP A 1 224 ? -4.104 -10.283 18.081 1.00 18.30 ? 237 TRP A C 1 ATOM 1722 O O . TRP A 1 224 ? -2.941 -9.898 17.990 1.00 15.57 ? 237 TRP A O 1 ATOM 1723 C CB . TRP A 1 224 ? -4.938 -12.282 16.790 1.00 15.59 ? 237 TRP A CB 1 ATOM 1724 C CG . TRP A 1 224 ? -4.086 -11.796 15.651 1.00 15.84 ? 237 TRP A CG 1 ATOM 1725 C CD1 . TRP A 1 224 ? -2.856 -12.290 15.224 1.00 16.44 ? 237 TRP A CD1 1 ATOM 1726 C CD2 . TRP A 1 224 ? -4.377 -10.683 14.769 1.00 15.24 ? 237 TRP A CD2 1 ATOM 1727 N NE1 . TRP A 1 224 ? -2.385 -11.564 14.172 1.00 19.02 ? 237 TRP A NE1 1 ATOM 1728 C CE2 . TRP A 1 224 ? -3.262 -10.591 13.838 1.00 17.39 ? 237 TRP A CE2 1 ATOM 1729 C CE3 . TRP A 1 224 ? -5.421 -9.780 14.659 1.00 16.38 ? 237 TRP A CE3 1 ATOM 1730 C CZ2 . TRP A 1 224 ? -3.206 -9.622 12.866 1.00 18.80 ? 237 TRP A CZ2 1 ATOM 1731 C CZ3 . TRP A 1 224 ? -5.364 -8.819 13.658 1.00 17.39 ? 237 TRP A CZ3 1 ATOM 1732 C CH2 . TRP A 1 224 ? -4.280 -8.741 12.788 1.00 16.54 ? 237 TRP A CH2 1 ATOM 1733 N N . ILE A 1 225 ? -5.121 -9.418 18.135 1.00 15.59 ? 238 ILE A N 1 ATOM 1734 C CA . ILE A 1 225 ? -4.876 -7.972 18.121 1.00 15.46 ? 238 ILE A CA 1 ATOM 1735 C C . ILE A 1 225 ? -3.867 -7.569 19.204 1.00 15.64 ? 238 ILE A C 1 ATOM 1736 O O . ILE A 1 225 ? -2.870 -6.890 18.933 1.00 14.67 ? 238 ILE A O 1 ATOM 1737 C CB . ILE A 1 225 ? -6.188 -7.174 18.291 1.00 13.73 ? 238 ILE A CB 1 ATOM 1738 C CG1 . ILE A 1 225 ? -7.065 -7.293 17.037 1.00 15.09 ? 238 ILE A CG1 1 ATOM 1739 C CG2 . ILE A 1 225 ? -5.872 -5.713 18.547 1.00 15.31 ? 238 ILE A CG2 1 ATOM 1740 C CD1 . ILE A 1 225 ? -8.494 -6.846 17.241 1.00 15.53 ? 238 ILE A CD1 1 ATOM 1741 N N . TRP A 1 226 ? -4.103 -8.027 20.435 1.00 14.49 ? 239 TRP A N 1 ATOM 1742 C CA . TRP A 1 226 ? -3.206 -7.658 21.527 1.00 15.40 ? 239 TRP A CA 1 ATOM 1743 C C . TRP A 1 226 ? -1.845 -8.277 21.408 1.00 16.85 ? 239 TRP A C 1 ATOM 1744 O O . TRP A 1 226 ? -0.861 -7.659 21.808 1.00 17.67 ? 239 TRP A O 1 ATOM 1745 C CB . TRP A 1 226 ? -3.821 -7.963 22.892 1.00 14.84 ? 239 TRP A CB 1 ATOM 1746 C CG . TRP A 1 226 ? -4.967 -7.058 23.210 1.00 15.48 ? 239 TRP A CG 1 ATOM 1747 C CD1 . TRP A 1 226 ? -6.265 -7.422 23.508 1.00 14.55 ? 239 TRP A CD1 1 ATOM 1748 C CD2 . TRP A 1 226 ? -4.960 -5.601 23.207 1.00 16.79 ? 239 TRP A CD2 1 ATOM 1749 N NE1 . TRP A 1 226 ? -7.043 -6.312 23.709 1.00 16.03 ? 239 TRP A NE1 1 ATOM 1750 C CE2 . TRP A 1 226 ? -6.317 -5.186 23.531 1.00 16.06 ? 239 TRP A CE2 1 ATOM 1751 C CE3 . TRP A 1 226 ? -3.992 -4.631 22.973 1.00 16.88 ? 239 TRP A CE3 1 ATOM 1752 C CZ2 . TRP A 1 226 ? -6.668 -3.843 23.622 1.00 16.59 ? 239 TRP A CZ2 1 ATOM 1753 C CZ3 . TRP A 1 226 ? -4.359 -3.290 23.061 1.00 18.59 ? 239 TRP A CZ3 1 ATOM 1754 C CH2 . TRP A 1 226 ? -5.671 -2.914 23.383 1.00 15.69 ? 239 TRP A CH2 1 ATOM 1755 N N . ASP A 1 227 ? -1.770 -9.480 20.852 1.00 18.36 ? 240 ASP A N 1 ATOM 1756 C CA . ASP A 1 227 ? -0.456 -10.082 20.581 1.00 23.01 ? 240 ASP A CA 1 ATOM 1757 C C . ASP A 1 227 ? 0.367 -9.200 19.650 1.00 21.91 ? 240 ASP A C 1 ATOM 1758 O O . ASP A 1 227 ? 1.549 -8.967 19.914 1.00 20.68 ? 240 ASP A O 1 ATOM 1759 C CB . ASP A 1 227 ? -0.587 -11.488 19.981 1.00 21.58 ? 240 ASP A CB 1 ATOM 1760 C CG . ASP A 1 227 ? -0.971 -12.554 21.022 1.00 24.25 ? 240 ASP A CG 1 ATOM 1761 O OD1 . ASP A 1 227 ? -1.448 -13.624 20.596 1.00 29.84 ? 240 ASP A OD1 1 ATOM 1762 O OD2 . ASP A 1 227 ? -0.812 -12.324 22.242 1.00 25.97 ? 240 ASP A OD2 1 ATOM 1763 N N . VAL A 1 228 ? -0.256 -8.683 18.587 1.00 19.42 ? 241 VAL A N 1 ATOM 1764 C CA . VAL A 1 228 ? 0.454 -7.857 17.621 1.00 18.59 ? 241 VAL A CA 1 ATOM 1765 C C . VAL A 1 228 ? 0.898 -6.545 18.264 1.00 18.44 ? 241 VAL A C 1 ATOM 1766 O O . VAL A 1 228 ? 2.030 -6.106 18.088 1.00 18.40 ? 241 VAL A O 1 ATOM 1767 C CB . VAL A 1 228 ? -0.408 -7.560 16.370 1.00 16.67 ? 241 VAL A CB 1 ATOM 1768 C CG1 . VAL A 1 228 ? 0.243 -6.516 15.469 1.00 18.42 ? 241 VAL A CG1 1 ATOM 1769 C CG2 . VAL A 1 228 ? -0.670 -8.840 15.590 1.00 18.06 ? 241 VAL A CG2 1 ATOM 1770 N N . VAL A 1 229 ? -0.003 -5.921 19.015 1.00 18.49 ? 242 VAL A N 1 ATOM 1771 C CA . VAL A 1 229 ? 0.308 -4.656 19.675 1.00 18.32 ? 242 VAL A CA 1 ATOM 1772 C C . VAL A 1 229 ? 1.455 -4.833 20.674 1.00 19.49 ? 242 VAL A C 1 ATOM 1773 O O . VAL A 1 229 ? 2.439 -4.100 20.625 1.00 18.87 ? 242 VAL A O 1 ATOM 1774 C CB . VAL A 1 229 ? -0.922 -4.052 20.381 1.00 14.88 ? 242 VAL A CB 1 ATOM 1775 C CG1 . VAL A 1 229 ? -0.525 -2.792 21.158 1.00 17.31 ? 242 VAL A CG1 1 ATOM 1776 C CG2 . VAL A 1 229 ? -2.037 -3.734 19.374 1.00 16.73 ? 242 VAL A CG2 1 ATOM 1777 N N . ARG A 1 230 ? 1.332 -5.825 21.560 1.00 19.84 ? 243 ARG A N 1 ATOM 1778 C CA . ARG A 1 230 ? 2.366 -6.088 22.580 1.00 23.52 ? 243 ARG A CA 1 ATOM 1779 C C . ARG A 1 230 ? 3.738 -6.358 21.954 1.00 25.26 ? 243 ARG A C 1 ATOM 1780 O O . ARG A 1 230 ? 4.766 -5.871 22.433 1.00 24.22 ? 243 ARG A O 1 ATOM 1781 C CB . ARG A 1 230 ? 1.955 -7.280 23.445 1.00 28.26 ? 243 ARG A CB 1 ATOM 1782 C CG . ARG A 1 230 ? 2.949 -7.630 24.553 1.00 28.82 ? 243 ARG A CG 1 ATOM 1783 C CD . ARG A 1 230 ? 2.421 -8.729 25.469 1.00 35.61 ? 243 ARG A CD 1 ATOM 1784 N NE . ARG A 1 230 ? 1.807 -9.827 24.722 1.00 37.10 ? 243 ARG A NE 1 ATOM 1785 C CZ . ARG A 1 230 ? 2.475 -10.766 24.046 1.00 43.41 ? 243 ARG A CZ 1 ATOM 1786 N NH1 . ARG A 1 230 ? 1.797 -11.713 23.400 1.00 39.13 ? 243 ARG A NH1 1 ATOM 1787 N NH2 . ARG A 1 230 ? 3.808 -10.774 24.002 1.00 41.97 ? 243 ARG A NH2 1 ATOM 1788 N N . ARG A 1 231 ? 3.720 -7.159 20.891 1.00 24.63 ? 244 ARG A N 1 ATOM 1789 C CA . ARG A 1 231 ? 4.879 -7.505 20.055 1.00 30.93 ? 244 ARG A CA 1 ATOM 1790 C C . ARG A 1 231 ? 5.738 -6.315 19.623 1.00 25.93 ? 244 ARG A C 1 ATOM 1791 O O . ARG A 1 231 ? 6.969 -6.389 19.592 1.00 26.27 ? 244 ARG A O 1 ATOM 1792 C CB . ARG A 1 231 ? 4.340 -8.173 18.786 1.00 33.40 ? 244 ARG A CB 1 ATOM 1793 C CG . ARG A 1 231 ? 5.257 -9.132 18.075 1.00 43.55 ? 244 ARG A CG 1 ATOM 1794 C CD . ARG A 1 231 ? 4.420 -10.221 17.420 1.00 38.18 ? 244 ARG A CD 1 ATOM 1795 N NE . ARG A 1 231 ? 3.912 -9.870 16.087 1.00 36.72 ? 244 ARG A NE 1 ATOM 1796 C CZ . ARG A 1 231 ? 2.878 -10.469 15.486 1.00 32.02 ? 244 ARG A CZ 1 ATOM 1797 N NH1 . ARG A 1 231 ? 2.188 -11.426 16.106 1.00 33.33 ? 244 ARG A NH1 1 ATOM 1798 N NH2 . ARG A 1 231 ? 2.516 -10.094 14.260 1.00 24.87 ? 244 ARG A NH2 1 ATOM 1799 N N . SER A 1 232 ? 5.085 -5.227 19.235 1.00 22.07 ? 245 SER A N 1 ATOM 1800 C CA . SER A 1 232 ? 5.807 -4.030 18.787 1.00 25.92 ? 245 SER A CA 1 ATOM 1801 C C . SER A 1 232 ? 5.679 -2.862 19.768 1.00 29.94 ? 245 SER A C 1 ATOM 1802 O O . SER A 1 232 ? 5.621 -1.702 19.351 1.00 37.79 ? 245 SER A O 1 ATOM 1803 C CB . SER A 1 232 ? 5.332 -3.623 17.385 1.00 33.16 ? 245 SER A CB 1 ATOM 1804 O OG . SER A 1 232 ? 5.791 -4.566 16.426 1.00 31.65 ? 245 SER A OG 1 ATOM 1805 N N . SER A 1 233 ? 5.647 -3.172 21.067 1.00 25.77 ? 246 SER A N 1 ATOM 1806 C CA . SER A 1 233 ? 5.576 -2.154 22.124 1.00 35.25 ? 246 SER A CA 1 ATOM 1807 C C . SER A 1 233 ? 6.727 -2.318 23.122 1.00 50.63 ? 246 SER A C 1 ATOM 1808 O O . SER A 1 233 ? 7.748 -2.933 22.809 1.00 56.40 ? 246 SER A O 1 ATOM 1809 C CB . SER A 1 233 ? 4.221 -2.218 22.833 1.00 37.11 ? 246 SER A CB 1 ATOM 1810 O OG . SER A 1 233 ? 3.167 -1.865 21.948 1.00 29.75 ? 246 SER A OG 1 HETATM 1811 C C1 . NAG B 2 . ? 4.769 10.007 8.745 1.00 24.77 ? 301 NAG A C1 1 HETATM 1812 C C2 . NAG B 2 . ? 5.816 11.121 8.754 1.00 35.80 ? 301 NAG A C2 1 HETATM 1813 C C3 . NAG B 2 . ? 5.316 12.253 7.859 1.00 39.07 ? 301 NAG A C3 1 HETATM 1814 C C4 . NAG B 2 . ? 5.051 11.725 6.447 1.00 40.13 ? 301 NAG A C4 1 HETATM 1815 C C5 . NAG B 2 . ? 4.110 10.512 6.464 1.00 36.20 ? 301 NAG A C5 1 HETATM 1816 C C6 . NAG B 2 . ? 3.976 9.909 5.055 1.00 38.88 ? 301 NAG A C6 1 HETATM 1817 C C7 . NAG B 2 . ? 7.243 11.506 10.735 1.00 38.78 ? 301 NAG A C7 1 HETATM 1818 C C8 . NAG B 2 . ? 7.313 12.049 12.136 1.00 43.97 ? 301 NAG A C8 1 HETATM 1819 N N2 . NAG B 2 . ? 6.060 11.596 10.111 1.00 33.77 ? 301 NAG A N2 1 HETATM 1820 O O3 . NAG B 2 . ? 6.240 13.326 7.847 1.00 49.29 ? 301 NAG A O3 1 HETATM 1821 O O4 . NAG B 2 . ? 4.503 12.752 5.646 1.00 40.57 ? 301 NAG A O4 1 HETATM 1822 O O5 . NAG B 2 . ? 4.578 9.555 7.408 1.00 29.93 ? 301 NAG A O5 1 HETATM 1823 O O6 . NAG B 2 . ? 4.515 8.608 4.921 1.00 42.93 ? 301 NAG A O6 1 HETATM 1824 O O7 . NAG B 2 . ? 8.254 11.015 10.227 1.00 39.95 ? 301 NAG A O7 1 HETATM 1825 C C1 . NAG C 2 . ? -23.787 -22.115 6.902 1.00 36.52 ? 302 NAG A C1 1 HETATM 1826 C C2 . NAG C 2 . ? -22.967 -22.881 7.927 1.00 37.40 ? 302 NAG A C2 1 HETATM 1827 C C3 . NAG C 2 . ? -22.270 -24.030 7.208 1.00 48.21 ? 302 NAG A C3 1 HETATM 1828 C C4 . NAG C 2 . ? -23.277 -24.870 6.411 1.00 49.43 ? 302 NAG A C4 1 HETATM 1829 C C5 . NAG C 2 . ? -24.125 -23.999 5.473 1.00 46.16 ? 302 NAG A C5 1 HETATM 1830 C C6 . NAG C 2 . ? -25.207 -24.781 4.704 1.00 30.35 ? 302 NAG A C6 1 HETATM 1831 C C7 . NAG C 2 . ? -22.194 -21.507 9.832 1.00 33.77 ? 302 NAG A C7 1 HETATM 1832 C C8 . NAG C 2 . ? -21.110 -20.624 10.385 1.00 31.57 ? 302 NAG A C8 1 HETATM 1833 N N2 . NAG C 2 . ? -22.009 -22.009 8.603 1.00 38.57 ? 302 NAG A N2 1 HETATM 1834 O O3 . NAG C 2 . ? -21.574 -24.809 8.155 1.00 49.74 ? 302 NAG A O3 1 HETATM 1835 O O4 . NAG C 2 . ? -22.573 -25.830 5.661 1.00 54.90 ? 302 NAG A O4 1 HETATM 1836 O O5 . NAG C 2 . ? -24.721 -22.969 6.245 1.00 35.89 ? 302 NAG A O5 1 HETATM 1837 O O6 . NAG C 2 . ? -26.019 -23.915 3.909 1.00 33.82 ? 302 NAG A O6 1 HETATM 1838 O O7 . NAG C 2 . ? -23.195 -21.725 10.522 1.00 38.12 ? 302 NAG A O7 1 HETATM 1839 C C1 . FUC D 3 . ? -27.270 -24.537 3.543 1.00 36.76 ? 303 FUC A C1 1 HETATM 1840 C C2 . FUC D 3 . ? -28.138 -23.626 2.656 1.00 33.46 ? 303 FUC A C2 1 HETATM 1841 C C3 . FUC D 3 . ? -27.556 -23.535 1.242 1.00 31.24 ? 303 FUC A C3 1 HETATM 1842 C C4 . FUC D 3 . ? -27.381 -24.937 0.668 1.00 37.48 ? 303 FUC A C4 1 HETATM 1843 C C5 . FUC D 3 . ? -26.521 -25.779 1.610 1.00 36.66 ? 303 FUC A C5 1 HETATM 1844 C C6 . FUC D 3 . ? -26.400 -27.219 1.117 1.00 38.10 ? 303 FUC A C6 1 HETATM 1845 O O2 . FUC D 3 . ? -28.303 -22.324 3.188 1.00 33.31 ? 303 FUC A O2 1 HETATM 1846 O O3 . FUC D 3 . ? -28.397 -22.762 0.401 1.00 35.13 ? 303 FUC A O3 1 HETATM 1847 O O4 . FUC D 3 . ? -28.656 -25.526 0.488 1.00 34.85 ? 303 FUC A O4 1 HETATM 1848 O O5 . FUC D 3 . ? -27.073 -25.797 2.918 1.00 44.03 ? 303 FUC A O5 1 HETATM 1849 N N1 . 2YT E 4 . ? -19.499 -6.714 -2.820 1.00 24.49 ? 304 2YT A N1 1 HETATM 1850 C C2 . 2YT E 4 . ? -18.463 -7.645 -2.375 1.00 19.85 ? 304 2YT A C2 1 HETATM 1851 C C10 . 2YT E 4 . ? -17.741 -6.989 -1.228 1.00 15.38 ? 304 2YT A C10 1 HETATM 1852 O O34 . 2YT E 4 . ? -18.418 -6.370 -0.386 1.00 14.86 ? 304 2YT A O34 1 HETATM 1853 C C3 . 2YT E 4 . ? -17.631 -7.917 -3.640 1.00 25.37 ? 304 2YT A C3 1 HETATM 1854 C C4 . 2YT E 4 . ? -16.164 -8.301 -3.603 1.00 54.25 ? 304 2YT A C4 1 HETATM 1855 C C5 . 2YT E 4 . ? -15.205 -7.372 -4.009 1.00 48.65 ? 304 2YT A C5 1 HETATM 1856 C C9 . 2YT E 4 . ? -15.766 -9.580 -3.225 1.00 76.42 ? 304 2YT A C9 1 HETATM 1857 C C6 . 2YT E 4 . ? -13.857 -7.699 -4.005 1.00 63.46 ? 304 2YT A C6 1 HETATM 1858 C C8 . 2YT E 4 . ? -14.416 -9.911 -3.225 1.00 84.34 ? 304 2YT A C8 1 HETATM 1859 C C7 . 2YT E 4 . ? -13.465 -8.973 -3.615 1.00 84.71 ? 304 2YT A C7 1 HETATM 1860 N N11 . 2YT E 4 . ? -16.414 -7.088 -1.144 1.00 13.87 ? 304 2YT A N11 1 HETATM 1861 C C12 . 2YT E 4 . ? -15.649 -6.452 -0.063 1.00 13.17 ? 304 2YT A C12 1 HETATM 1862 C C20 . 2YT E 4 . ? -15.806 -4.954 -0.107 1.00 14.59 ? 304 2YT A C20 1 HETATM 1863 O O33 . 2YT E 4 . ? -15.812 -4.317 -1.146 1.00 15.48 ? 304 2YT A O33 1 HETATM 1864 C C13 . 2YT E 4 . ? -14.169 -6.724 -0.267 1.00 13.74 ? 304 2YT A C13 1 HETATM 1865 C C14 . 2YT E 4 . ? -13.676 -8.017 0.357 1.00 16.49 ? 304 2YT A C14 1 HETATM 1866 C C19 . 2YT E 4 . ? -14.080 -8.476 1.613 1.00 18.58 ? 304 2YT A C19 1 HETATM 1867 C C15 . 2YT E 4 . ? -12.733 -8.779 -0.338 1.00 23.52 ? 304 2YT A C15 1 HETATM 1868 C C18 . 2YT E 4 . ? -13.582 -9.654 2.148 1.00 20.83 ? 304 2YT A C18 1 HETATM 1869 C C16 . 2YT E 4 . ? -12.220 -9.956 0.194 1.00 24.00 ? 304 2YT A C16 1 HETATM 1870 C C17 . 2YT E 4 . ? -12.650 -10.401 1.437 1.00 23.04 ? 304 2YT A C17 1 HETATM 1871 N N21 . 2YT E 4 . ? -15.933 -4.313 1.087 1.00 13.62 ? 304 2YT A N21 1 HETATM 1872 C C22 . 2YT E 4 . ? -16.085 -2.854 1.195 1.00 13.20 ? 304 2YT A C22 1 HETATM 1873 C C23 . 2YT E 4 . ? -17.383 -2.507 1.974 1.00 13.75 ? 304 2YT A C23 1 HETATM 1874 C C24 . 2YT E 4 . ? -18.628 -3.230 1.450 1.00 13.63 ? 304 2YT A C24 1 HETATM 1875 C C25 . 2YT E 4 . ? -18.924 -2.922 -0.022 1.00 14.83 ? 304 2YT A C25 1 HETATM 1876 N N26 . 2YT E 4 . ? -20.241 -3.499 -0.332 1.00 13.53 ? 304 2YT A N26 1 HETATM 1877 C C27 . 2YT E 4 . ? -20.826 -3.349 -1.562 1.00 14.50 ? 304 2YT A C27 1 HETATM 1878 N N28 . 2YT E 4 . ? -20.223 -2.554 -2.494 1.00 17.91 ? 304 2YT A N28 1 HETATM 1879 N N29 . 2YT E 4 . ? -21.960 -3.950 -1.856 1.00 18.16 ? 304 2YT A N29 1 HETATM 1880 C C30 . 2YT E 4 . ? -14.880 -2.243 1.941 1.00 14.02 ? 304 2YT A C30 1 HETATM 1881 O O31 . 2YT E 4 . ? -14.923 -0.855 1.707 1.00 12.39 ? 304 2YT A O31 1 HETATM 1882 C C32 . 2YT E 4 . ? -13.602 -2.754 1.236 1.00 13.71 ? 304 2YT A C32 1 HETATM 1883 C C1 . GOL F 5 . ? -10.126 -17.087 14.586 1.00 43.49 ? 305 GOL A C1 1 HETATM 1884 O O1 . GOL F 5 . ? -10.488 -18.147 13.686 1.00 48.09 ? 305 GOL A O1 1 HETATM 1885 C C2 . GOL F 5 . ? -8.634 -16.772 14.483 1.00 39.09 ? 305 GOL A C2 1 HETATM 1886 O O2 . GOL F 5 . ? -8.336 -16.556 13.095 1.00 48.17 ? 305 GOL A O2 1 HETATM 1887 C C3 . GOL F 5 . ? -8.330 -15.556 15.377 1.00 38.43 ? 305 GOL A C3 1 HETATM 1888 O O3 . GOL F 5 . ? -6.975 -15.044 15.350 1.00 26.41 ? 305 GOL A O3 1 HETATM 1889 CL CL . CL G 6 . ? 0.057 3.570 21.706 1.00 24.15 ? 306 CL A CL 1 HETATM 1890 O O . HOH H 7 . ? -17.466 -9.626 18.415 1.00 16.03 ? 401 HOH A O 1 HETATM 1891 O O . HOH H 7 . ? -21.131 7.286 4.460 1.00 12.18 ? 402 HOH A O 1 HETATM 1892 O O . HOH H 7 . ? -24.629 -2.761 8.754 1.00 14.43 ? 403 HOH A O 1 HETATM 1893 O O . HOH H 7 . ? -16.137 3.064 8.215 1.00 10.96 ? 404 HOH A O 1 HETATM 1894 O O . HOH H 7 . ? -11.002 10.890 11.390 1.00 11.59 ? 405 HOH A O 1 HETATM 1895 O O . HOH H 7 . ? -13.697 -11.318 8.442 1.00 14.92 ? 406 HOH A O 1 HETATM 1896 O O . HOH H 7 . ? -13.341 13.672 15.250 1.00 13.11 ? 407 HOH A O 1 HETATM 1897 O O . HOH H 7 . ? -8.878 16.570 19.728 1.00 13.38 ? 408 HOH A O 1 HETATM 1898 O O . HOH H 7 . ? -15.328 4.900 6.232 1.00 10.75 ? 409 HOH A O 1 HETATM 1899 O O . HOH H 7 . ? -13.801 11.440 13.629 1.00 13.06 ? 410 HOH A O 1 HETATM 1900 O O . HOH H 7 . ? -19.855 4.536 15.509 1.00 16.87 ? 411 HOH A O 1 HETATM 1901 O O . HOH H 7 . ? -16.482 11.866 14.797 1.00 12.10 ? 412 HOH A O 1 HETATM 1902 O O . HOH H 7 . ? -24.074 -3.225 2.202 1.00 14.08 ? 413 HOH A O 1 HETATM 1903 O O . HOH H 7 . ? -15.209 2.245 23.896 1.00 14.99 ? 414 HOH A O 1 HETATM 1904 O O . HOH H 7 . ? -8.943 0.610 22.970 1.00 13.35 ? 415 HOH A O 1 HETATM 1905 O O . HOH H 7 . ? -24.761 -12.588 13.043 1.00 18.89 ? 416 HOH A O 1 HETATM 1906 O O . HOH H 7 . ? 1.388 -3.450 12.498 1.00 18.35 ? 417 HOH A O 1 HETATM 1907 O O . HOH H 7 . ? -32.451 0.519 12.329 1.00 22.53 ? 418 HOH A O 1 HETATM 1908 O O . HOH H 7 . ? -29.377 -0.184 -1.959 1.00 20.17 ? 419 HOH A O 1 HETATM 1909 O O . HOH H 7 . ? -27.748 -7.476 -3.045 1.00 19.47 ? 420 HOH A O 1 HETATM 1910 O O . HOH H 7 . ? -31.663 -9.371 6.056 1.00 21.30 ? 421 HOH A O 1 HETATM 1911 O O . HOH H 7 . ? -7.195 16.727 17.243 1.00 17.35 ? 422 HOH A O 1 HETATM 1912 O O . HOH H 7 . ? -18.519 3.064 13.486 1.00 15.77 ? 423 HOH A O 1 HETATM 1913 O O . HOH H 7 . ? -15.167 -11.336 6.171 1.00 15.61 ? 424 HOH A O 1 HETATM 1914 O O . HOH H 7 . ? -26.588 7.355 4.879 1.00 19.48 ? 425 HOH A O 1 HETATM 1915 O O . HOH H 7 . ? -25.716 -6.048 0.303 1.00 17.05 ? 426 HOH A O 1 HETATM 1916 O O . HOH H 7 . ? -13.571 7.652 22.009 1.00 20.84 ? 427 HOH A O 1 HETATM 1917 O O . HOH H 7 . ? -29.869 -7.350 6.514 1.00 17.88 ? 428 HOH A O 1 HETATM 1918 O O . HOH H 7 . ? -21.404 12.573 -4.661 1.00 26.29 ? 429 HOH A O 1 HETATM 1919 O O . HOH H 7 . ? -9.348 -14.565 3.793 1.00 24.89 ? 430 HOH A O 1 HETATM 1920 O O . HOH H 7 . ? -27.957 -9.867 -4.743 1.00 26.87 ? 431 HOH A O 1 HETATM 1921 O O . HOH H 7 . ? -31.730 -5.243 6.544 1.00 18.86 ? 432 HOH A O 1 HETATM 1922 O O . HOH H 7 . ? -27.815 -4.054 7.926 1.00 16.85 ? 433 HOH A O 1 HETATM 1923 O O . HOH H 7 . ? 3.761 -3.525 13.851 1.00 21.92 ? 434 HOH A O 1 HETATM 1924 O O . HOH H 7 . ? -22.271 3.062 -4.844 1.00 18.11 ? 435 HOH A O 1 HETATM 1925 O O . HOH H 7 . ? -13.545 -6.497 8.492 1.00 16.67 ? 436 HOH A O 1 HETATM 1926 O O . HOH H 7 . ? -3.913 -6.713 3.288 1.00 25.98 ? 437 HOH A O 1 HETATM 1927 O O . HOH H 7 . ? -7.557 -14.019 18.277 1.00 21.10 ? 438 HOH A O 1 HETATM 1928 O O . HOH H 7 . ? -17.541 7.231 -8.935 1.00 27.51 ? 439 HOH A O 1 HETATM 1929 O O . HOH H 7 . ? -26.689 -5.512 2.948 1.00 16.47 ? 440 HOH A O 1 HETATM 1930 O O . HOH H 7 . ? -19.848 0.861 -7.121 1.00 21.44 ? 441 HOH A O 1 HETATM 1931 O O . HOH H 7 . ? -11.248 10.600 14.829 1.00 17.58 ? 442 HOH A O 1 HETATM 1932 O O . HOH H 7 . ? -29.938 4.856 10.623 1.00 19.21 ? 443 HOH A O 1 HETATM 1933 O O . HOH H 7 . ? -23.151 -0.570 -4.756 1.00 22.42 ? 444 HOH A O 1 HETATM 1934 O O . HOH H 7 . ? -20.654 0.785 -4.451 1.00 22.12 ? 445 HOH A O 1 HETATM 1935 O O . HOH H 7 . ? -9.844 -13.515 20.939 1.00 22.61 ? 446 HOH A O 1 HETATM 1936 O O . HOH H 7 . ? 4.229 -2.846 6.751 1.00 26.43 ? 447 HOH A O 1 HETATM 1937 O O . HOH H 7 . ? -30.499 -3.014 5.439 1.00 17.98 ? 448 HOH A O 1 HETATM 1938 O O . HOH H 7 . ? 1.479 8.772 2.391 1.00 26.24 ? 449 HOH A O 1 HETATM 1939 O O . HOH H 7 . ? -11.713 -16.961 11.291 1.00 23.22 ? 450 HOH A O 1 HETATM 1940 O O . HOH H 7 . ? -3.418 -11.652 23.512 1.00 29.26 ? 451 HOH A O 1 HETATM 1941 O O . HOH H 7 . ? -9.983 8.173 24.432 1.00 22.65 ? 452 HOH A O 1 HETATM 1942 O O . HOH H 7 . ? -12.150 20.637 13.471 1.00 23.38 ? 453 HOH A O 1 HETATM 1943 O O . HOH H 7 . ? -3.010 9.451 0.764 1.00 23.40 ? 454 HOH A O 1 HETATM 1944 O O . HOH H 7 . ? -27.888 -5.565 5.514 1.00 17.51 ? 455 HOH A O 1 HETATM 1945 O O . HOH H 7 . ? -32.475 -11.861 13.814 1.00 21.84 ? 456 HOH A O 1 HETATM 1946 O O . HOH H 7 . ? -6.244 16.280 20.769 1.00 21.64 ? 457 HOH A O 1 HETATM 1947 O O . HOH H 7 . ? -13.631 -18.231 9.428 1.00 26.08 ? 458 HOH A O 1 HETATM 1948 O O . HOH H 7 . ? -16.192 7.783 22.042 1.00 29.65 ? 459 HOH A O 1 HETATM 1949 O O . HOH H 7 . ? -13.814 -3.928 31.364 1.00 29.73 ? 460 HOH A O 1 HETATM 1950 O O . HOH H 7 . ? -14.147 18.840 18.934 1.00 29.45 ? 461 HOH A O 1 HETATM 1951 O O . HOH H 7 . ? -23.709 12.384 16.483 1.00 19.14 ? 462 HOH A O 1 HETATM 1952 O O . HOH H 7 . ? -25.782 11.800 2.405 1.00 24.70 ? 463 HOH A O 1 HETATM 1953 O O . HOH H 7 . ? -1.452 -5.812 1.947 1.00 27.14 ? 464 HOH A O 1 HETATM 1954 O O . HOH H 7 . ? -10.660 12.039 1.581 1.00 27.10 ? 465 HOH A O 1 HETATM 1955 O O . HOH H 7 . ? -13.150 10.684 -1.889 1.00 35.37 ? 466 HOH A O 1 HETATM 1956 O O . HOH H 7 . ? -12.829 9.740 23.723 1.00 31.91 ? 467 HOH A O 1 HETATM 1957 O O . HOH H 7 . ? -9.600 -12.304 0.334 1.00 31.32 ? 468 HOH A O 1 HETATM 1958 O O . HOH H 7 . ? -25.148 0.088 21.086 1.00 30.97 ? 469 HOH A O 1 HETATM 1959 O O . HOH H 7 . ? -27.638 -14.155 -1.476 1.00 31.75 ? 470 HOH A O 1 HETATM 1960 O O . HOH H 7 . ? 2.140 5.627 5.087 1.00 21.65 ? 471 HOH A O 1 HETATM 1961 O O . HOH H 7 . ? -11.819 -3.748 26.237 1.00 25.85 ? 472 HOH A O 1 HETATM 1962 O O . HOH H 7 . ? -9.427 10.890 3.867 1.00 20.33 ? 473 HOH A O 1 HETATM 1963 O O . HOH H 7 . ? 3.407 -4.278 4.339 1.00 33.58 ? 474 HOH A O 1 HETATM 1964 O O . HOH H 7 . ? -27.523 9.595 3.336 1.00 24.88 ? 475 HOH A O 1 HETATM 1965 O O . HOH H 7 . ? -26.314 9.659 12.821 1.00 29.64 ? 476 HOH A O 1 HETATM 1966 O O . HOH H 7 . ? -17.581 8.402 -6.212 1.00 23.82 ? 477 HOH A O 1 HETATM 1967 O O . HOH H 7 . ? -1.363 -1.295 24.520 1.00 24.13 ? 478 HOH A O 1 HETATM 1968 O O . HOH H 7 . ? 3.417 -7.531 13.405 1.00 23.50 ? 479 HOH A O 1 HETATM 1969 O O . HOH H 7 . ? -24.619 12.827 0.012 1.00 25.15 ? 480 HOH A O 1 HETATM 1970 O O . HOH H 7 . ? -2.428 -19.461 7.311 1.00 44.29 ? 481 HOH A O 1 HETATM 1971 O O . HOH H 7 . ? 3.754 -1.323 0.462 1.00 33.03 ? 482 HOH A O 1 HETATM 1972 O O . HOH H 7 . ? -26.706 6.614 15.274 1.00 29.30 ? 483 HOH A O 1 HETATM 1973 O O . HOH H 7 . ? -13.745 -13.819 9.554 1.00 21.08 ? 484 HOH A O 1 HETATM 1974 O O . HOH H 7 . ? -26.141 -23.771 13.518 1.00 39.25 ? 485 HOH A O 1 HETATM 1975 O O . HOH H 7 . ? -13.395 -1.331 31.959 1.00 27.52 ? 486 HOH A O 1 HETATM 1976 O O . HOH H 7 . ? -26.448 15.600 6.071 1.00 27.12 ? 487 HOH A O 1 HETATM 1977 O O . HOH H 7 . ? -15.787 16.777 20.116 1.00 25.31 ? 488 HOH A O 1 HETATM 1978 O O . HOH H 7 . ? 0.493 -11.834 13.197 1.00 23.90 ? 489 HOH A O 1 HETATM 1979 O O . HOH H 7 . ? -29.423 -18.532 16.007 1.00 30.84 ? 490 HOH A O 1 HETATM 1980 O O . HOH H 7 . ? -7.790 16.381 5.000 1.00 31.48 ? 491 HOH A O 1 HETATM 1981 O O . HOH H 7 . ? -13.106 -5.615 28.154 1.00 25.91 ? 492 HOH A O 1 HETATM 1982 O O . HOH H 7 . ? -34.184 -8.927 7.057 1.00 37.41 ? 493 HOH A O 1 HETATM 1983 O O . HOH H 7 . ? -32.279 3.829 2.644 1.00 26.52 ? 494 HOH A O 1 HETATM 1984 O O . HOH H 7 . ? -6.175 17.380 23.688 1.00 32.33 ? 495 HOH A O 1 HETATM 1985 O O . HOH H 7 . ? -23.955 -13.430 15.581 1.00 32.85 ? 496 HOH A O 1 HETATM 1986 O O . HOH H 7 . ? -13.756 -10.566 29.134 1.00 22.28 ? 497 HOH A O 1 HETATM 1987 O O . HOH H 7 . ? -0.971 1.372 -4.706 1.00 33.93 ? 498 HOH A O 1 HETATM 1988 O O . HOH H 7 . ? -8.136 -8.609 -0.697 1.00 31.54 ? 499 HOH A O 1 HETATM 1989 O O . HOH H 7 . ? 1.783 1.464 21.594 1.00 27.37 ? 500 HOH A O 1 HETATM 1990 O O . HOH H 7 . ? -14.873 13.049 23.042 1.00 37.44 ? 501 HOH A O 1 HETATM 1991 O O . HOH H 7 . ? -11.586 6.478 26.244 1.00 43.45 ? 502 HOH A O 1 HETATM 1992 O O . HOH H 7 . ? -18.312 16.579 18.964 1.00 24.92 ? 503 HOH A O 1 HETATM 1993 O O . HOH H 7 . ? -27.853 13.375 7.302 1.00 27.55 ? 504 HOH A O 1 HETATM 1994 O O . HOH H 7 . ? -12.430 -7.965 29.596 1.00 29.50 ? 505 HOH A O 1 HETATM 1995 O O . HOH H 7 . ? -7.556 1.381 25.557 1.00 24.37 ? 506 HOH A O 1 HETATM 1996 O O . HOH H 7 . ? -30.849 8.216 5.497 1.00 33.63 ? 507 HOH A O 1 HETATM 1997 O O . HOH H 7 . ? -0.697 14.761 15.944 1.00 27.64 ? 508 HOH A O 1 HETATM 1998 O O . HOH H 7 . ? 1.118 -14.931 17.451 1.00 39.68 ? 509 HOH A O 1 HETATM 1999 O O . HOH H 7 . ? 2.338 -3.705 1.890 1.00 36.81 ? 510 HOH A O 1 HETATM 2000 O O . HOH H 7 . ? -30.331 -20.596 2.024 1.00 37.09 ? 511 HOH A O 1 HETATM 2001 O O . HOH H 7 . ? -11.427 11.682 -0.824 1.00 34.55 ? 512 HOH A O 1 HETATM 2002 O O . HOH H 7 . ? -15.481 -5.030 27.065 1.00 37.28 ? 513 HOH A O 1 HETATM 2003 O O . HOH H 7 . ? -2.029 -12.673 5.737 1.00 27.35 ? 514 HOH A O 1 HETATM 2004 O O . HOH H 7 . ? -28.577 2.353 18.139 1.00 33.77 ? 515 HOH A O 1 HETATM 2005 O O . HOH H 7 . ? 7.013 -7.396 23.531 1.00 39.43 ? 516 HOH A O 1 HETATM 2006 O O . HOH H 7 . ? -16.154 10.147 1.234 1.00 28.05 ? 517 HOH A O 1 HETATM 2007 O O . HOH H 7 . ? -26.882 12.879 13.933 1.00 38.10 ? 518 HOH A O 1 HETATM 2008 O O . HOH H 7 . ? -22.119 14.344 -2.527 1.00 37.39 ? 519 HOH A O 1 HETATM 2009 O O . HOH H 7 . ? -28.994 11.188 5.587 1.00 30.18 ? 520 HOH A O 1 HETATM 2010 O O . HOH H 7 . ? -35.085 -3.230 0.548 1.00 29.58 ? 521 HOH A O 1 HETATM 2011 O O . HOH H 7 . ? -28.666 6.245 2.011 1.00 28.19 ? 522 HOH A O 1 HETATM 2012 O O . HOH H 7 . ? -1.659 16.263 11.106 1.00 28.23 ? 523 HOH A O 1 HETATM 2013 O O . HOH H 7 . ? 2.942 -12.933 18.509 1.00 36.52 ? 524 HOH A O 1 HETATM 2014 O O . HOH H 7 . ? -21.966 -9.161 23.726 1.00 55.56 ? 525 HOH A O 1 HETATM 2015 O O . HOH H 7 . ? -14.774 -10.960 23.393 1.00 42.86 ? 526 HOH A O 1 HETATM 2016 O O . HOH H 7 . ? -9.205 -16.185 20.839 1.00 37.95 ? 527 HOH A O 1 HETATM 2017 O O . HOH H 7 . ? 5.023 7.802 19.571 1.00 40.64 ? 528 HOH A O 1 HETATM 2018 O O . HOH H 7 . ? 6.238 -4.455 8.309 1.00 42.13 ? 529 HOH A O 1 HETATM 2019 O O . HOH H 7 . ? 1.870 6.044 22.142 1.00 21.66 ? 530 HOH A O 1 HETATM 2020 O O . HOH H 7 . ? -2.610 11.778 24.377 1.00 25.12 ? 531 HOH A O 1 HETATM 2021 O O . HOH H 7 . ? -19.410 14.158 21.926 1.00 40.50 ? 532 HOH A O 1 HETATM 2022 O O . HOH H 7 . ? -24.704 -15.493 -1.718 1.00 46.71 ? 533 HOH A O 1 HETATM 2023 O O . HOH H 7 . ? 0.050 -7.184 4.519 1.00 36.52 ? 534 HOH A O 1 HETATM 2024 O O . HOH H 7 . ? -9.814 11.133 23.949 1.00 25.95 ? 535 HOH A O 1 HETATM 2025 O O . HOH H 7 . ? 1.123 -0.643 23.619 1.00 26.94 ? 536 HOH A O 1 HETATM 2026 O O . HOH H 7 . ? -19.300 -6.964 25.196 1.00 35.96 ? 537 HOH A O 1 HETATM 2027 O O . HOH H 7 . ? 3.651 -5.665 15.811 1.00 27.68 ? 538 HOH A O 1 HETATM 2028 O O . HOH H 7 . ? -16.802 13.289 21.047 1.00 28.43 ? 539 HOH A O 1 HETATM 2029 O O . HOH H 7 . ? -3.347 -18.570 13.155 1.00 48.00 ? 540 HOH A O 1 HETATM 2030 O O . HOH H 7 . ? -13.960 22.136 11.859 1.00 35.65 ? 541 HOH A O 1 HETATM 2031 O O . HOH H 7 . ? 4.167 1.592 23.782 1.00 42.28 ? 542 HOH A O 1 HETATM 2032 O O . HOH H 7 . ? -6.788 -2.364 -3.161 1.00 38.86 ? 543 HOH A O 1 HETATM 2033 O O . HOH H 7 . ? 1.222 -8.811 7.702 1.00 25.85 ? 544 HOH A O 1 HETATM 2034 O O . HOH H 7 . ? -17.033 -7.200 26.100 1.00 35.55 ? 545 HOH A O 1 HETATM 2035 O O . HOH H 7 . ? -9.584 -19.037 8.625 1.00 33.82 ? 546 HOH A O 1 HETATM 2036 O O . HOH H 7 . ? -32.440 -6.884 -4.440 1.00 37.80 ? 547 HOH A O 1 HETATM 2037 O O . HOH H 7 . ? -19.057 18.800 3.045 1.00 38.32 ? 548 HOH A O 1 HETATM 2038 O O . HOH H 7 . ? -25.676 10.864 15.386 1.00 34.44 ? 549 HOH A O 1 HETATM 2039 O O . HOH H 7 . ? -3.249 -17.984 4.813 1.00 31.92 ? 550 HOH A O 1 HETATM 2040 O O . HOH H 7 . ? -0.351 -3.074 1.498 1.00 30.06 ? 551 HOH A O 1 HETATM 2041 O O . HOH H 7 . ? -14.717 3.324 26.400 1.00 29.21 ? 552 HOH A O 1 HETATM 2042 O O . HOH H 7 . ? -2.246 -11.253 3.171 1.00 36.30 ? 553 HOH A O 1 HETATM 2043 O O . HOH H 7 . ? -25.953 -5.619 24.385 1.00 42.31 ? 554 HOH A O 1 HETATM 2044 O O . HOH H 7 . ? -28.257 7.411 12.509 1.00 46.79 ? 555 HOH A O 1 HETATM 2045 O O . HOH H 7 . ? -35.290 -2.996 3.381 1.00 38.06 ? 556 HOH A O 1 HETATM 2046 O O . HOH H 7 . ? 2.666 -14.057 21.025 1.00 41.49 ? 557 HOH A O 1 HETATM 2047 O O . HOH H 7 . ? -24.208 18.810 5.856 1.00 33.77 ? 558 HOH A O 1 HETATM 2048 O O . HOH H 7 . ? -16.040 20.511 17.536 1.00 40.46 ? 559 HOH A O 1 HETATM 2049 O O . HOH H 7 . ? -18.537 8.322 20.665 1.00 42.83 ? 560 HOH A O 1 HETATM 2050 O O . HOH H 7 . ? -8.931 -2.458 -1.341 1.00 29.44 ? 561 HOH A O 1 HETATM 2051 O O . HOH H 7 . ? -20.026 19.934 9.080 1.00 40.63 ? 562 HOH A O 1 HETATM 2052 O O . HOH H 7 . ? -25.874 -13.189 17.423 1.00 36.48 ? 563 HOH A O 1 HETATM 2053 O O . HOH H 7 . ? -0.113 14.466 13.060 1.00 33.59 ? 564 HOH A O 1 HETATM 2054 O O . HOH H 7 . ? -3.782 -8.706 0.394 1.00 35.73 ? 565 HOH A O 1 HETATM 2055 O O . HOH H 7 . ? -20.873 18.603 6.549 1.00 35.10 ? 566 HOH A O 1 HETATM 2056 O O . HOH H 7 . ? -13.667 23.076 9.341 1.00 35.50 ? 567 HOH A O 1 HETATM 2057 O O . HOH H 7 . ? -0.911 10.038 23.131 1.00 38.97 ? 568 HOH A O 1 HETATM 2058 O O . HOH H 7 . ? 0.702 -11.261 9.639 1.00 38.40 ? 569 HOH A O 1 HETATM 2059 O O . HOH H 7 . ? -22.824 18.909 10.650 1.00 49.20 ? 570 HOH A O 1 HETATM 2060 O O . HOH H 7 . ? -20.552 -14.053 14.974 1.00 29.19 ? 571 HOH A O 1 HETATM 2061 O O . HOH H 7 . ? -23.241 -6.422 23.134 1.00 44.26 ? 572 HOH A O 1 HETATM 2062 O O . HOH H 7 . ? -24.548 17.004 11.801 1.00 37.03 ? 573 HOH A O 1 HETATM 2063 O O . HOH H 7 . ? -6.663 -18.804 5.174 1.00 34.26 ? 574 HOH A O 1 HETATM 2064 O O . HOH H 7 . ? -15.637 21.798 5.779 1.00 30.61 ? 575 HOH A O 1 HETATM 2065 O O . HOH H 7 . ? 5.951 -12.313 25.202 1.00 39.16 ? 576 HOH A O 1 HETATM 2066 O O . HOH H 7 . ? -17.791 2.067 -10.448 1.00 14.44 ? 577 HOH A O 1 HETATM 2067 O O . HOH H 7 . ? -22.951 2.021 21.778 1.00 22.20 ? 578 HOH A O 1 HETATM 2068 O O . HOH H 7 . ? -12.452 -12.370 23.035 1.00 30.21 ? 579 HOH A O 1 HETATM 2069 O O . HOH H 7 . ? -15.716 -1.837 -2.382 1.00 23.39 ? 580 HOH A O 1 HETATM 2070 O O . HOH H 7 . ? 4.303 11.026 18.062 1.00 31.36 ? 581 HOH A O 1 HETATM 2071 O O . HOH H 7 . ? -22.172 -3.029 -4.753 1.00 26.19 ? 582 HOH A O 1 HETATM 2072 O O . HOH H 7 . ? -18.824 19.533 16.917 1.00 32.32 ? 583 HOH A O 1 HETATM 2073 O O . HOH H 7 . ? -29.989 9.804 16.205 1.00 44.78 ? 584 HOH A O 1 HETATM 2074 O O . HOH H 7 . ? -2.112 4.543 23.613 1.00 24.95 ? 585 HOH A O 1 HETATM 2075 O O . HOH H 7 . ? -29.109 3.611 -3.896 1.00 23.16 ? 586 HOH A O 1 HETATM 2076 O O . HOH H 7 . ? -31.578 -2.096 -5.651 1.00 46.10 ? 587 HOH A O 1 HETATM 2077 O O . HOH H 7 . ? -33.909 2.849 12.345 1.00 37.87 ? 588 HOH A O 1 HETATM 2078 O O . HOH H 7 . ? 2.319 12.595 10.138 1.00 33.49 ? 589 HOH A O 1 HETATM 2079 O O . HOH H 7 . ? -9.388 19.422 19.808 1.00 26.46 ? 590 HOH A O 1 HETATM 2080 O O . HOH H 7 . ? -20.603 -7.025 -4.891 1.00 46.90 ? 591 HOH A O 1 HETATM 2081 O O . HOH H 7 . ? -20.549 16.084 20.480 1.00 29.44 ? 592 HOH A O 1 HETATM 2082 O O . HOH H 7 . ? -12.802 -6.627 32.274 1.00 40.43 ? 593 HOH A O 1 HETATM 2083 O O . HOH H 7 . ? -1.702 -19.909 3.410 1.00 31.60 ? 594 HOH A O 1 HETATM 2084 O O . HOH H 7 . ? 0.191 -9.738 3.009 1.00 36.45 ? 595 HOH A O 1 HETATM 2085 O O . HOH H 7 . ? -16.901 1.167 29.868 1.00 32.88 ? 596 HOH A O 1 HETATM 2086 O O . HOH H 7 . ? -29.833 -3.518 22.393 1.00 31.23 ? 597 HOH A O 1 HETATM 2087 O O . HOH H 7 . ? -27.326 9.032 16.726 1.00 37.12 ? 598 HOH A O 1 HETATM 2088 O O . HOH H 7 . ? -16.423 -3.811 30.990 1.00 34.27 ? 599 HOH A O 1 HETATM 2089 O O . HOH H 7 . ? 1.476 13.565 17.208 1.00 31.81 ? 600 HOH A O 1 HETATM 2090 O O . HOH H 7 . ? -12.955 22.368 15.579 1.00 32.96 ? 601 HOH A O 1 HETATM 2091 O O . HOH H 7 . ? -4.393 18.287 19.951 1.00 34.60 ? 602 HOH A O 1 HETATM 2092 O O . HOH H 7 . ? -24.884 -19.608 11.870 1.00 35.34 ? 603 HOH A O 1 HETATM 2093 O O . HOH H 7 . ? -15.842 4.991 22.974 1.00 44.72 ? 604 HOH A O 1 HETATM 2094 O O . HOH H 7 . ? -20.649 21.030 15.338 1.00 45.58 ? 605 HOH A O 1 HETATM 2095 O O . HOH H 7 . ? 4.033 3.385 4.727 1.00 29.48 ? 606 HOH A O 1 HETATM 2096 O O . HOH H 7 . ? -5.682 19.002 17.418 1.00 30.04 ? 607 HOH A O 1 HETATM 2097 O O . HOH H 7 . ? 3.979 -14.164 24.606 1.00 43.59 ? 608 HOH A O 1 HETATM 2098 O O . HOH H 7 . ? -29.887 0.728 -5.672 1.00 32.02 ? 609 HOH A O 1 HETATM 2099 O O . HOH H 7 . ? -15.436 20.011 11.760 1.00 28.74 ? 610 HOH A O 1 HETATM 2100 O O . HOH H 7 . ? -16.315 13.906 3.875 1.00 25.58 ? 611 HOH A O 1 HETATM 2101 O O . HOH H 7 . ? -8.870 22.818 17.388 1.00 41.56 ? 612 HOH A O 1 HETATM 2102 O O . HOH H 7 . ? 3.711 12.509 15.126 1.00 40.72 ? 613 HOH A O 1 HETATM 2103 O O . HOH H 7 . ? -25.518 17.686 14.606 1.00 32.02 ? 614 HOH A O 1 HETATM 2104 O O . HOH H 7 . ? -2.386 3.768 -3.802 1.00 36.97 ? 615 HOH A O 1 HETATM 2105 O O . HOH H 7 . ? -12.888 -16.277 20.678 1.00 45.82 ? 616 HOH A O 1 HETATM 2106 O O . HOH H 7 . ? -34.305 -6.565 -1.766 1.00 38.63 ? 617 HOH A O 1 HETATM 2107 O O . HOH H 7 . ? -3.681 10.521 26.718 1.00 29.61 ? 618 HOH A O 1 HETATM 2108 O O . HOH H 7 . ? 3.137 -0.383 25.800 1.00 37.67 ? 619 HOH A O 1 HETATM 2109 O O . HOH H 7 . ? -16.540 -21.492 10.652 1.00 40.09 ? 620 HOH A O 1 HETATM 2110 O O . HOH H 7 . ? -34.455 -5.828 6.908 1.00 32.43 ? 621 HOH A O 1 HETATM 2111 O O . HOH H 7 . ? -13.547 12.171 0.987 1.00 48.89 ? 622 HOH A O 1 HETATM 2112 O O . HOH H 7 . ? -27.150 4.838 17.499 1.00 26.78 ? 623 HOH A O 1 HETATM 2113 O O . HOH H 7 . ? -17.213 -3.260 -5.372 1.00 33.32 ? 624 HOH A O 1 HETATM 2114 O O . HOH H 7 . ? 1.461 -13.943 14.791 1.00 34.04 ? 625 HOH A O 1 HETATM 2115 O O . HOH H 7 . ? -32.573 -9.117 14.180 1.00 27.91 ? 626 HOH A O 1 HETATM 2116 O O . HOH H 7 . ? -12.838 2.463 28.730 1.00 35.35 ? 627 HOH A O 1 HETATM 2117 O O . HOH H 7 . ? 2.157 13.902 7.241 1.00 46.62 ? 628 HOH A O 1 HETATM 2118 O O . HOH H 7 . ? -11.757 22.437 17.997 1.00 36.75 ? 629 HOH A O 1 HETATM 2119 O O . HOH H 7 . ? -25.461 5.932 19.485 1.00 35.88 ? 630 HOH A O 1 HETATM 2120 O O . HOH H 7 . ? 5.721 1.170 3.997 1.00 37.43 ? 631 HOH A O 1 HETATM 2121 O O . HOH H 7 . ? -15.553 -15.427 19.348 1.00 40.36 ? 632 HOH A O 1 HETATM 2122 O O . HOH H 7 . ? 1.278 8.524 23.582 1.00 32.49 ? 633 HOH A O 1 HETATM 2123 O O . HOH H 7 . ? -16.855 13.587 12.719 1.00 13.01 ? 634 HOH A O 1 HETATM 2124 O O . HOH H 7 . ? -13.094 0.306 0.098 1.00 16.18 ? 635 HOH A O 1 HETATM 2125 O O . HOH H 7 . ? -25.012 -10.151 -4.574 1.00 27.02 ? 636 HOH A O 1 HETATM 2126 O O . HOH H 7 . ? -28.614 -21.495 8.136 1.00 27.03 ? 637 HOH A O 1 HETATM 2127 O O . HOH H 7 . ? -32.043 -0.054 15.165 1.00 29.97 ? 638 HOH A O 1 HETATM 2128 O O . HOH H 7 . ? -29.610 0.333 16.427 1.00 27.74 ? 639 HOH A O 1 HETATM 2129 O O . HOH H 7 . ? -15.566 20.959 8.521 1.00 27.59 ? 640 HOH A O 1 HETATM 2130 O O . HOH H 7 . ? -19.947 -10.145 25.627 1.00 44.59 ? 641 HOH A O 1 HETATM 2131 O O . HOH H 7 . ? -27.302 -21.755 5.682 1.00 30.14 ? 642 HOH A O 1 HETATM 2132 O O . HOH H 7 . ? -20.650 -4.661 24.487 1.00 40.56 ? 643 HOH A O 1 HETATM 2133 O O . HOH H 7 . ? -26.523 14.352 3.339 1.00 32.19 ? 644 HOH A O 1 HETATM 2134 O O . HOH H 7 . ? -20.499 -10.663 -2.311 1.00 37.89 ? 645 HOH A O 1 HETATM 2135 O O . HOH H 7 . ? -21.597 -16.715 11.806 1.00 30.24 ? 646 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ILE A 1 ? 0.1490 0.1629 0.1417 0.0052 0.0061 -0.0191 16 ILE A N 2 C CA . ILE A 1 ? 0.1492 0.1674 0.1426 0.0042 0.0061 -0.0211 16 ILE A CA 3 C C . ILE A 1 ? 0.1620 0.1857 0.1549 0.0053 0.0053 -0.0228 16 ILE A C 4 O O . ILE A 1 ? 0.1720 0.1960 0.1643 0.0079 0.0040 -0.0225 16 ILE A O 5 C CB . ILE A 1 ? 0.1569 0.1745 0.1512 0.0051 0.0053 -0.0211 16 ILE A CB 6 C CG1 . ILE A 1 ? 0.1639 0.1767 0.1589 0.0039 0.0059 -0.0195 16 ILE A CG1 7 C CG2 . ILE A 1 ? 0.1798 0.2026 0.1747 0.0044 0.0053 -0.0233 16 ILE A CG2 8 C CD1 . ILE A 1 ? 0.1591 0.1717 0.1543 0.0011 0.0072 -0.0197 16 ILE A CD1 9 N N . ILE A 2 ? 0.1802 0.2082 0.1733 0.0032 0.0059 -0.0246 17 ILE A N 10 C CA . ILE A 2 ? 0.1831 0.2174 0.1761 0.0037 0.0052 -0.0265 17 ILE A CA 11 C C . ILE A 2 ? 0.1761 0.2156 0.1707 0.0038 0.0048 -0.0282 17 ILE A C 12 O O . ILE A 2 ? 0.1878 0.2270 0.1830 0.0015 0.0058 -0.0286 17 ILE A O 13 C CB . ILE A 2 ? 0.1925 0.2287 0.1846 0.0007 0.0062 -0.0276 17 ILE A CB 14 C CG1 . ILE A 2 ? 0.2403 0.2713 0.2307 0.0005 0.0069 -0.0261 17 ILE A CG1 15 C CG2 . ILE A 2 ? 0.2312 0.2747 0.2234 0.0011 0.0052 -0.0296 17 ILE A CG2 16 C CD1 . ILE A 2 ? 0.2416 0.2716 0.2309 0.0034 0.0058 -0.0249 17 ILE A CD1 17 N N . GLY A 3 ? 0.1969 0.2412 0.1920 0.0065 0.0034 -0.0292 18 GLY A N 18 C CA . GLY A 3 ? 0.2032 0.2536 0.2000 0.0069 0.0031 -0.0311 18 GLY A CA 19 C C . GLY A 3 ? 0.1980 0.2453 0.1952 0.0075 0.0033 -0.0307 18 GLY A C 20 O O . GLY A 3 ? 0.2136 0.2645 0.2118 0.0061 0.0040 -0.0320 18 GLY A O 21 N N . GLY A 4 ? 0.1831 0.2239 0.1795 0.0094 0.0027 -0.0288 19 GLY A N 22 C CA . GLY A 4 ? 0.1915 0.2287 0.1879 0.0101 0.0026 -0.0283 19 GLY A CA 23 C C . GLY A 4 ? 0.2007 0.2371 0.1968 0.0142 0.0010 -0.0283 19 GLY A C 24 O O . GLY A 4 ? 0.2032 0.2423 0.1991 0.0168 0.0000 -0.0288 19 GLY A O 25 N N . HIS A 5 ? 0.2218 0.2539 0.2176 0.0148 0.0008 -0.0278 20 HIS A N 26 C CA . HIS A 5 ? 0.2126 0.2424 0.2075 0.0185 -0.0006 -0.0278 20 HIS A CA 27 C C . HIS A 5 ? 0.1916 0.2136 0.1855 0.0182 -0.0008 -0.0259 20 HIS A C 28 O O . HIS A 5 ? 0.2086 0.2284 0.2028 0.0154 0.0000 -0.0251 20 HIS A O 29 C CB . HIS A 5 ? 0.2500 0.2848 0.2457 0.0200 -0.0007 -0.0302 20 HIS A CB 30 C CG . HIS A 5 ? 0.2793 0.3229 0.2765 0.0205 -0.0006 -0.0322 20 HIS A CG 31 N ND1 . HIS A 5 ? 0.3269 0.3759 0.3253 0.0173 0.0008 -0.0334 20 HIS A ND1 32 C CD2 . HIS A 5 ? 0.3398 0.3877 0.3373 0.0237 -0.0018 -0.0331 20 HIS A CD2 33 C CE1 . HIS A 5 ? 0.3302 0.3871 0.3300 0.0182 0.0005 -0.0351 20 HIS A CE1 34 N NE2 . HIS A 5 ? 0.3830 0.4394 0.3823 0.0223 -0.0011 -0.0349 20 HIS A NE2 35 N N . GLU A 6 ? 0.2021 0.2199 0.1946 0.0211 -0.0022 -0.0251 21 GLU A N 36 C CA . GLU A 6 ? 0.1945 0.2048 0.1858 0.0208 -0.0026 -0.0233 21 GLU A CA 37 C C . GLU A 6 ? 0.2011 0.2105 0.1926 0.0202 -0.0026 -0.0244 21 GLU A C 38 O O . GLU A 6 ? 0.2289 0.2408 0.2200 0.0224 -0.0031 -0.0264 21 GLU A O 39 C CB . GLU A 6 ? 0.2191 0.2250 0.2085 0.0240 -0.0042 -0.0224 21 GLU A CB 40 C CG . GLU A 6 ? 0.2363 0.2343 0.2244 0.0231 -0.0046 -0.0203 21 GLU A CG 41 C CD . GLU A 6 ? 0.2555 0.2484 0.2411 0.0258 -0.0061 -0.0191 21 GLU A CD 42 O OE1 . GLU A 6 ? 0.2746 0.2701 0.2595 0.0288 -0.0069 -0.0198 21 GLU A OE1 43 O OE2 . GLU A 6 ? 0.2726 0.2591 0.2570 0.0250 -0.0065 -0.0174 21 GLU A OE2 44 N N . VAL A 7 ? 0.1979 0.2039 0.1896 0.0174 -0.0020 -0.0231 22 VAL A N 45 C CA . VAL A 7 ? 0.1955 0.2004 0.1869 0.0167 -0.0021 -0.0239 22 VAL A CA 46 C C . VAL A 7 ? 0.2143 0.2136 0.2039 0.0189 -0.0036 -0.0239 22 VAL A C 47 O O . VAL A 7 ? 0.2110 0.2061 0.1996 0.0202 -0.0045 -0.0225 22 VAL A O 48 C CB . VAL A 7 ? 0.1876 0.1909 0.1799 0.0131 -0.0012 -0.0225 22 VAL A CB 49 C CG1 . VAL A 7 ? 0.2046 0.2126 0.1982 0.0110 0.0002 -0.0227 22 VAL A CG1 50 C CG2 . VAL A 7 ? 0.1870 0.1845 0.1792 0.0123 -0.0017 -0.0201 22 VAL A CG2 51 N N . THR A 8 ? 0.1923 0.1912 0.1811 0.0192 -0.0039 -0.0253 23 THR A N 52 C CA . THR A 8 ? 0.2071 0.1996 0.1938 0.0204 -0.0053 -0.0253 23 THR A CA 53 C C . THR A 8 ? 0.1922 0.1794 0.1790 0.0177 -0.0055 -0.0227 23 THR A C 54 O O . THR A 8 ? 0.1751 0.1637 0.1634 0.0148 -0.0046 -0.0218 23 THR A O 55 C CB . THR A 8 ? 0.2175 0.2107 0.2032 0.0206 -0.0053 -0.0274 23 THR A CB 56 O OG1 . THR A 8 ? 0.2311 0.2295 0.2167 0.0235 -0.0051 -0.0299 23 THR A OG1 57 C CG2 . THR A 8 ? 0.2353 0.2211 0.2185 0.0213 -0.0068 -0.0273 23 THR A CG2 58 N N . PRO A 9 ? 0.2097 0.1910 0.1952 0.0186 -0.0066 -0.0213 24 PRO A N 59 C CA . PRO A 9 ? 0.1949 0.1722 0.1810 0.0158 -0.0066 -0.0188 24 PRO A CA 60 C C . PRO A 9 ? 0.2124 0.1890 0.1990 0.0131 -0.0067 -0.0188 24 PRO A C 61 O O . PRO A 9 ? 0.2287 0.2039 0.2137 0.0137 -0.0075 -0.0204 24 PRO A O 62 C CB . PRO A 9 ? 0.2145 0.1851 0.1982 0.0173 -0.0080 -0.0179 24 PRO A CB 63 C CG . PRO A 9 ? 0.2225 0.1946 0.2050 0.0209 -0.0083 -0.0191 24 PRO A CG 64 C CD . PRO A 9 ? 0.2498 0.2281 0.2331 0.0221 -0.0077 -0.0217 24 PRO A CD 65 N N . HIS A 10 ? 0.1754 0.1534 0.1642 0.0104 -0.0058 -0.0171 25 HIS A N 66 C CA . HIS A 10 ? 0.1757 0.1531 0.1652 0.0078 -0.0061 -0.0165 25 HIS A CA 67 C C . HIS A 10 ? 0.1693 0.1505 0.1587 0.0074 -0.0056 -0.0183 25 HIS A C 68 O O . HIS A 10 ? 0.2040 0.1845 0.1933 0.0056 -0.0060 -0.0180 25 HIS A O 69 C CB . HIS A 10 ? 0.2064 0.1779 0.1944 0.0072 -0.0076 -0.0160 25 HIS A CB 70 C CG . HIS A 10 ? 0.2208 0.1885 0.2085 0.0077 -0.0080 -0.0144 25 HIS A CG 71 N ND1 . HIS A 10 ? 0.2184 0.1867 0.2082 0.0062 -0.0072 -0.0121 25 HIS A ND1 72 C CD2 . HIS A 10 ? 0.2188 0.1819 0.2038 0.0098 -0.0090 -0.0147 25 HIS A CD2 73 C CE1 . HIS A 10 ? 0.2100 0.1745 0.1984 0.0070 -0.0076 -0.0110 25 HIS A CE1 74 N NE2 . HIS A 10 ? 0.2400 0.2010 0.2255 0.0092 -0.0087 -0.0125 25 HIS A NE2 75 N N . SER A 11 ? 0.1756 0.1611 0.1649 0.0089 -0.0046 -0.0198 26 SER A N 76 C CA . SER A 11 ? 0.1779 0.1678 0.1671 0.0083 -0.0039 -0.0214 26 SER A CA 77 C C . SER A 11 ? 0.1722 0.1650 0.1631 0.0058 -0.0026 -0.0203 26 SER A C 78 O O . SER A 11 ? 0.1880 0.1837 0.1785 0.0047 -0.0019 -0.0212 26 SER A O 79 C CB . SER A 11 ? 0.1793 0.1731 0.1678 0.0108 -0.0035 -0.0238 26 SER A CB 80 O OG . SER A 11 ? 0.1894 0.1864 0.1793 0.0114 -0.0026 -0.0235 26 SER A OG 81 N N . ARG A 12 ? 0.1640 0.1557 0.1565 0.0049 -0.0022 -0.0182 27 ARG A N 82 C CA . ARG A 12 ? 0.1697 0.1630 0.1638 0.0028 -0.0011 -0.0168 27 ARG A CA 83 C C . ARG A 12 ? 0.1602 0.1501 0.1556 0.0016 -0.0017 -0.0145 27 ARG A C 84 O O . ARG A 12 ? 0.1543 0.1438 0.1512 0.0014 -0.0010 -0.0130 27 ARG A O 85 C CB . ARG A 12 ? 0.1516 0.1476 0.1466 0.0031 0.0001 -0.0169 27 ARG A CB 86 C CG . ARG A 12 ? 0.1848 0.1849 0.1789 0.0043 0.0006 -0.0192 27 ARG A CG 87 C CD . ARG A 12 ? 0.1885 0.1915 0.1819 0.0029 0.0012 -0.0204 27 ARG A CD 88 N NE . ARG A 12 ? 0.1953 0.2033 0.1884 0.0039 0.0018 -0.0226 27 ARG A NE 89 C CZ . ARG A 12 ? 0.2127 0.2226 0.2048 0.0054 0.0014 -0.0246 27 ARG A CZ 90 N NH1 . ARG A 12 ? 0.2208 0.2275 0.2117 0.0062 0.0003 -0.0248 27 ARG A NH1 91 N NH2 . ARG A 12 ? 0.2233 0.2386 0.2156 0.0063 0.0020 -0.0265 27 ARG A NH2 92 N N . PRO A 13 ? 0.1567 0.1446 0.1515 0.0007 -0.0028 -0.0142 28 PRO A N 93 C CA . PRO A 13 ? 0.1689 0.1539 0.1650 -0.0002 -0.0037 -0.0123 28 PRO A CA 94 C C . PRO A 13 ? 0.1650 0.1509 0.1635 -0.0016 -0.0030 -0.0103 28 PRO A C 95 O O . PRO A 13 ? 0.1628 0.1472 0.1629 -0.0024 -0.0036 -0.0086 28 PRO A O 96 C CB . PRO A 13 ? 0.1761 0.1593 0.1706 -0.0008 -0.0053 -0.0131 28 PRO A CB 97 C CG . PRO A 13 ? 0.1849 0.1708 0.1779 -0.0008 -0.0047 -0.0147 28 PRO A CG 98 C CD . PRO A 13 ? 0.1802 0.1685 0.1730 0.0007 -0.0035 -0.0160 28 PRO A CD 99 N N . TYR A 14 ? 0.1492 0.1375 0.1479 -0.0020 -0.0018 -0.0104 29 TYR A N 100 C CA . TYR A 14 ? 0.1410 0.1299 0.1416 -0.0029 -0.0009 -0.0087 29 TYR A CA 101 C C . TYR A 14 ? 0.1317 0.1209 0.1336 -0.0022 0.0003 -0.0080 29 TYR A C 102 O O . TYR A 14 ? 0.1479 0.1373 0.1516 -0.0027 0.0011 -0.0066 29 TYR A O 103 C CB . TYR A 14 ? 0.1412 0.1316 0.1408 -0.0037 -0.0002 -0.0091 29 TYR A CB 104 C CG . TYR A 14 ? 0.1512 0.1437 0.1491 -0.0033 0.0007 -0.0111 29 TYR A CG 105 C CD1 . TYR A 14 ? 0.1476 0.1412 0.1459 -0.0029 0.0021 -0.0114 29 TYR A CD1 106 C CD2 . TYR A 14 ? 0.1493 0.1428 0.1451 -0.0033 0.0002 -0.0129 29 TYR A CD2 107 C CE1 . TYR A 14 ? 0.1450 0.1413 0.1419 -0.0027 0.0028 -0.0134 29 TYR A CE1 108 C CE2 . TYR A 14 ? 0.1657 0.1620 0.1603 -0.0029 0.0011 -0.0148 29 TYR A CE2 109 C CZ . TYR A 14 ? 0.1686 0.1664 0.1639 -0.0027 0.0024 -0.0150 29 TYR A CZ 110 O OH . TYR A 14 ? 0.1789 0.1803 0.1734 -0.0025 0.0032 -0.0169 29 TYR A OH 111 N N . MET A 15 ? 0.1247 0.1141 0.1257 -0.0010 0.0005 -0.0091 30 MET A N 112 C CA . MET A 15 ? 0.1189 0.1088 0.1205 -0.0004 0.0018 -0.0087 30 MET A CA 113 C C . MET A 15 ? 0.1420 0.1303 0.1453 -0.0005 0.0017 -0.0068 30 MET A C 114 O O . MET A 15 ? 0.1639 0.1503 0.1671 -0.0005 0.0005 -0.0063 30 MET A O 115 C CB . MET A 15 ? 0.1341 0.1251 0.1340 0.0009 0.0019 -0.0103 30 MET A CB 116 C CG . MET A 15 ? 0.1468 0.1407 0.1456 0.0008 0.0025 -0.0122 30 MET A CG 117 S SD . MET A 15 ? 0.1441 0.1394 0.1436 -0.0005 0.0043 -0.0118 30 MET A SD 118 C CE . MET A 15 ? 0.1579 0.1529 0.1580 0.0003 0.0052 -0.0110 30 MET A CE 119 N N . ALA A 16 ? 0.1427 0.1317 0.1474 -0.0007 0.0031 -0.0057 31 ALA A N 120 C CA . ALA A 16 ? 0.1402 0.1285 0.1467 -0.0009 0.0034 -0.0040 31 ALA A CA 121 C C . ALA A 16 ? 0.1296 0.1183 0.1355 -0.0001 0.0048 -0.0040 31 ALA A C 122 O O . ALA A 16 ? 0.1355 0.1255 0.1405 0.0002 0.0058 -0.0051 31 ALA A O 123 C CB . ALA A 16 ? 0.1511 0.1401 0.1600 -0.0016 0.0039 -0.0026 31 ALA A CB 124 N N . SER A 17 ? 0.1292 0.1168 0.1352 0.0000 0.0048 -0.0029 32 SER A N 125 C CA . SER A 17 ? 0.1445 0.1325 0.1500 0.0006 0.0062 -0.0025 32 SER A CA 126 C C . SER A 17 ? 0.1465 0.1351 0.1544 0.0000 0.0074 -0.0007 32 SER A C 127 O O . SER A 17 ? 0.1600 0.1482 0.1697 -0.0009 0.0068 0.0006 32 SER A O 128 C CB . SER A 17 ? 0.1605 0.1466 0.1640 0.0012 0.0054 -0.0022 32 SER A CB 129 O OG . SER A 17 ? 0.1846 0.1710 0.1875 0.0015 0.0066 -0.0014 32 SER A OG 130 N N . VAL A 18 ? 0.1610 0.1509 0.1691 0.0003 0.0091 -0.0009 33 VAL A N 131 C CA . VAL A 18 ? 0.1525 0.1435 0.1628 0.0001 0.0106 0.0004 33 VAL A CA 132 C C . VAL A 18 ? 0.1571 0.1479 0.1658 0.0004 0.0116 0.0009 33 VAL A C 133 O O . VAL A 18 ? 0.1724 0.1632 0.1786 0.0012 0.0122 -0.0003 33 VAL A O 134 C CB . VAL A 18 ? 0.1764 0.1683 0.1874 0.0005 0.0121 -0.0001 33 VAL A CB 135 C CG1 . VAL A 18 ? 0.1943 0.1876 0.2076 0.0008 0.0138 0.0011 33 VAL A CG1 136 C CG2 . VAL A 18 ? 0.1893 0.1811 0.2014 0.0002 0.0110 -0.0004 33 VAL A CG2 137 N N . ARG A 19 ? 0.1737 0.1645 0.1836 -0.0002 0.0118 0.0026 34 ARG A N 138 C CA . ARG A 19 ? 0.1891 0.1794 0.1972 -0.0001 0.0127 0.0034 34 ARG A CA 139 C C . ARG A 19 ? 0.2060 0.1983 0.2161 -0.0004 0.0148 0.0047 34 ARG A C 140 O O . ARG A 19 ? 0.2266 0.2205 0.2402 -0.0011 0.0149 0.0057 34 ARG A O 141 C CB . ARG A 19 ? 0.2579 0.2455 0.2644 -0.0007 0.0111 0.0043 34 ARG A CB 142 C CG . ARG A 19 ? 0.3112 0.2984 0.3202 -0.0023 0.0102 0.0057 34 ARG A CG 143 C CD . ARG A 19 ? 0.3091 0.2930 0.3160 -0.0031 0.0091 0.0069 34 ARG A CD 144 N NE . ARG A 19 ? 0.2961 0.2770 0.2998 -0.0019 0.0073 0.0056 34 ARG A NE 145 C CZ . ARG A 19 ? 0.3393 0.3165 0.3412 -0.0024 0.0057 0.0061 34 ARG A CZ 146 N NH1 . ARG A 19 ? 0.3516 0.3272 0.3542 -0.0044 0.0056 0.0080 34 ARG A NH1 147 N NH2 . ARG A 19 ? 0.3375 0.3123 0.3365 -0.0008 0.0042 0.0047 34 ARG A NH2 148 N N . PHE A 20 ? 0.2260 0.2186 0.2340 0.0000 0.0163 0.0046 35 PHE A N 149 C CA . PHE A 20 ? 0.2609 0.2556 0.2704 -0.0001 0.0186 0.0057 35 PHE A CA 150 C C . PHE A 20 ? 0.3085 0.3022 0.3153 -0.0007 0.0190 0.0070 35 PHE A C 151 O O . PHE A 20 ? 0.3003 0.2923 0.3033 0.0000 0.0185 0.0063 35 PHE A O 152 C CB . PHE A 20 ? 0.2411 0.2371 0.2501 0.0011 0.0205 0.0043 35 PHE A CB 153 C CG . PHE A 20 ? 0.2615 0.2583 0.2733 0.0016 0.0205 0.0036 35 PHE A CG 154 C CD1 . PHE A 20 ? 0.2849 0.2840 0.3007 0.0015 0.0213 0.0048 35 PHE A CD1 155 C CD2 . PHE A 20 ? 0.2737 0.2691 0.2840 0.0021 0.0197 0.0018 35 PHE A CD2 156 C CE1 . PHE A 20 ? 0.3075 0.3071 0.3257 0.0023 0.0212 0.0043 35 PHE A CE1 157 C CE2 . PHE A 20 ? 0.2810 0.2766 0.2935 0.0026 0.0197 0.0013 35 PHE A CE2 158 C CZ . PHE A 20 ? 0.2950 0.2925 0.3113 0.0028 0.0204 0.0026 35 PHE A CZ 159 N N . GLY A 21 ? 0.3533 0.3482 0.3621 -0.0020 0.0198 0.0090 36 GLY A N 160 C CA . GLY A 21 ? 0.3680 0.3615 0.3740 -0.0030 0.0203 0.0106 36 GLY A CA 161 C C . GLY A 21 ? 0.4268 0.4161 0.4296 -0.0031 0.0179 0.0107 36 GLY A C 162 O O . GLY A 21 ? 0.4568 0.4440 0.4556 -0.0028 0.0178 0.0113 36 GLY A O 163 N N . GLY A 22 ? 0.3274 0.3154 0.3317 -0.0033 0.0158 0.0102 38 GLY A N 164 C CA . GLY A 22 ? 0.3409 0.3248 0.3423 -0.0032 0.0135 0.0101 38 GLY A CA 165 C C . GLY A 22 ? 0.3683 0.3512 0.3668 -0.0010 0.0124 0.0081 38 GLY A C 166 O O . GLY A 22 ? 0.4022 0.3820 0.3983 -0.0004 0.0105 0.0078 38 GLY A O 167 N N . GLN A 23 ? 0.3096 0.2951 0.3083 0.0000 0.0136 0.0066 39 GLN A N 168 C CA . GLN A 23 ? 0.2948 0.2802 0.2908 0.0016 0.0129 0.0047 39 GLN A CA 169 C C . GLN A 23 ? 0.2366 0.2238 0.2347 0.0020 0.0125 0.0027 39 GLN A C 170 O O . GLN A 23 ? 0.2335 0.2226 0.2341 0.0016 0.0138 0.0025 39 GLN A O 171 C CB . GLN A 23 ? 0.3920 0.3789 0.3857 0.0022 0.0146 0.0045 39 GLN A CB 172 C CG . GLN A 23 ? 0.4795 0.4671 0.4706 0.0037 0.0139 0.0024 39 GLN A CG 173 C CD . GLN A 23 ? 0.6407 0.6290 0.6284 0.0042 0.0150 0.0025 39 GLN A CD 174 O OE1 . GLN A 23 ? 0.6569 0.6451 0.6441 0.0035 0.0166 0.0041 39 GLN A OE1 175 N NE2 . GLN A 23 ? 0.7215 0.7108 0.7068 0.0054 0.0143 0.0007 39 GLN A NE2 176 N N . HIS A 24 ? 0.2142 0.2006 0.2110 0.0029 0.0108 0.0013 40 HIS A N 177 C CA . HIS A 24 ? 0.1935 0.1815 0.1918 0.0031 0.0105 -0.0005 40 HIS A CA 178 C C . HIS A 24 ? 0.2014 0.1915 0.1992 0.0032 0.0121 -0.0016 40 HIS A C 179 O O . HIS A 24 ? 0.2208 0.2115 0.2162 0.0039 0.0125 -0.0022 40 HIS A O 180 C CB . HIS A 24 ? 0.1749 0.1625 0.1714 0.0041 0.0087 -0.0019 40 HIS A CB 181 C CG . HIS A 24 ? 0.1620 0.1516 0.1594 0.0040 0.0086 -0.0039 40 HIS A CG 182 N ND1 . HIS A 24 ? 0.1570 0.1465 0.1565 0.0033 0.0081 -0.0041 40 HIS A ND1 183 C CD2 . HIS A 24 ? 0.1810 0.1729 0.1773 0.0044 0.0091 -0.0057 40 HIS A CD2 184 C CE1 . HIS A 24 ? 0.1520 0.1433 0.1514 0.0032 0.0083 -0.0058 40 HIS A CE1 185 N NE2 . HIS A 24 ? 0.1622 0.1551 0.1599 0.0037 0.0089 -0.0068 40 HIS A NE2 186 N N . HIS A 25 ? 0.1813 0.1724 0.1814 0.0027 0.0129 -0.0021 41 HIS A N 187 C CA . HIS A 25 ? 0.1868 0.1791 0.1866 0.0027 0.0146 -0.0033 41 HIS A CA 188 C C . HIS A 25 ? 0.1684 0.1610 0.1685 0.0024 0.0142 -0.0049 41 HIS A C 189 O O . HIS A 25 ? 0.1803 0.1736 0.1788 0.0023 0.0149 -0.0065 41 HIS A O 190 C CB . HIS A 25 ? 0.2081 0.2006 0.2100 0.0024 0.0163 -0.0020 41 HIS A CB 191 C CG . HIS A 25 ? 0.2518 0.2448 0.2532 0.0027 0.0182 -0.0031 41 HIS A CG 192 N ND1 . HIS A 25 ? 0.2886 0.2819 0.2870 0.0030 0.0191 -0.0042 41 HIS A ND1 193 C CD2 . HIS A 25 ? 0.2862 0.2790 0.2893 0.0028 0.0193 -0.0034 41 HIS A CD2 194 C CE1 . HIS A 25 ? 0.3334 0.3264 0.3316 0.0031 0.0207 -0.0053 41 HIS A CE1 195 N NE2 . HIS A 25 ? 0.3024 0.2950 0.3034 0.0031 0.0209 -0.0047 41 HIS A NE2 196 N N . CYS A 26 ? 0.1613 0.1535 0.1634 0.0020 0.0132 -0.0045 42 CYS A N 197 C CA . CYS A 26 ? 0.1577 0.1500 0.1599 0.0015 0.0129 -0.0058 42 CYS A CA 198 C C . CYS A 26 ? 0.1300 0.1221 0.1331 0.0012 0.0111 -0.0056 42 CYS A C 199 O O . CYS A 26 ? 0.1447 0.1360 0.1488 0.0013 0.0102 -0.0043 42 CYS A O 200 C CB . CYS A 26 ? 0.1557 0.1475 0.1594 0.0012 0.0143 -0.0054 42 CYS A CB 201 S SG . CYS A 26 ? 0.1994 0.1909 0.2009 0.0013 0.0163 -0.0068 42 CYS A SG 202 N N . GLY A 27 ? 0.1285 0.1210 0.1310 0.0007 0.0107 -0.0070 43 GLY A N 203 C CA . GLY A 27 ? 0.1410 0.1333 0.1441 0.0003 0.0093 -0.0069 43 GLY A CA 204 C C . GLY A 27 ? 0.1400 0.1315 0.1448 -0.0003 0.0095 -0.0060 43 GLY A C 205 O O . GLY A 27 ? 0.1370 0.1279 0.1428 -0.0002 0.0108 -0.0052 43 GLY A O 206 N N . GLY A 28 ? 0.1409 0.1322 0.1459 -0.0008 0.0082 -0.0060 44 GLY A N 207 C CA . GLY A 28 ? 0.1241 0.1146 0.1304 -0.0014 0.0079 -0.0050 44 GLY A CA 208 C C . GLY A 28 ? 0.1117 0.1023 0.1174 -0.0019 0.0063 -0.0054 44 GLY A C 209 O O . GLY A 28 ? 0.1314 0.1225 0.1359 -0.0016 0.0055 -0.0065 44 GLY A O 210 N N . PHE A 29 ? 0.1253 0.1154 0.1316 -0.0025 0.0057 -0.0046 45 PHE A N 211 C CA . PHE A 29 ? 0.1202 0.1102 0.1259 -0.0030 0.0041 -0.0049 45 PHE A CA 212 C C . PHE A 29 ? 0.1255 0.1150 0.1330 -0.0034 0.0030 -0.0032 45 PHE A C 213 O O . PHE A 29 ? 0.1377 0.1271 0.1468 -0.0032 0.0036 -0.0018 45 PHE A O 214 C CB . PHE A 29 ? 0.1411 0.1316 0.1443 -0.0037 0.0042 -0.0064 45 PHE A CB 215 C CG . PHE A 29 ? 0.1548 0.1444 0.1574 -0.0045 0.0047 -0.0057 45 PHE A CG 216 C CD1 . PHE A 29 ? 0.1480 0.1369 0.1505 -0.0051 0.0036 -0.0047 45 PHE A CD1 217 C CD2 . PHE A 29 ? 0.1581 0.1473 0.1599 -0.0048 0.0063 -0.0061 45 PHE A CD2 218 C CE1 . PHE A 29 ? 0.1696 0.1573 0.1712 -0.0057 0.0039 -0.0039 45 PHE A CE1 219 C CE2 . PHE A 29 ? 0.1459 0.1334 0.1466 -0.0056 0.0068 -0.0054 45 PHE A CE2 220 C CZ . PHE A 29 ? 0.1661 0.1527 0.1666 -0.0060 0.0055 -0.0042 45 PHE A CZ 221 N N . LEU A 30 ? 0.1377 0.1270 0.1448 -0.0038 0.0014 -0.0033 46 LEU A N 222 C CA . LEU A 30 ? 0.1379 0.1272 0.1467 -0.0044 0.0000 -0.0019 46 LEU A CA 223 C C . LEU A 30 ? 0.1300 0.1192 0.1374 -0.0050 -0.0005 -0.0018 46 LEU A C 224 O O . LEU A 30 ? 0.1476 0.1366 0.1523 -0.0055 -0.0009 -0.0031 46 LEU A O 225 C CB . LEU A 30 ? 0.1505 0.1392 0.1589 -0.0049 -0.0016 -0.0023 46 LEU A CB 226 C CG . LEU A 30 ? 0.1458 0.1348 0.1564 -0.0058 -0.0031 -0.0008 46 LEU A CG 227 C CD1 . LEU A 30 ? 0.1631 0.1533 0.1772 -0.0056 -0.0023 0.0009 46 LEU A CD1 228 C CD2 . LEU A 30 ? 0.1626 0.1501 0.1720 -0.0065 -0.0048 -0.0016 46 LEU A CD2 229 N N . LEU A 31 ? 0.1436 0.1329 0.1526 -0.0048 -0.0003 -0.0002 47 LEU A N 230 C CA . LEU A 31 ? 0.1540 0.1427 0.1617 -0.0052 -0.0008 0.0003 47 LEU A CA 231 C C . LEU A 31 ? 0.1576 0.1470 0.1660 -0.0058 -0.0030 0.0014 47 LEU A C 232 O O . LEU A 31 ? 0.1701 0.1589 0.1759 -0.0066 -0.0040 0.0011 47 LEU A O 233 C CB . LEU A 31 ? 0.1517 0.1397 0.1605 -0.0043 0.0003 0.0016 47 LEU A CB 234 C CG . LEU A 31 ? 0.1678 0.1544 0.1750 -0.0044 0.0000 0.0026 47 LEU A CG 235 C CD1 . LEU A 31 ? 0.1850 0.1700 0.1881 -0.0056 0.0007 0.0013 47 LEU A CD1 236 C CD2 . LEU A 31 ? 0.1857 0.1714 0.1948 -0.0030 0.0008 0.0042 47 LEU A CD2 237 N N . ARG A 32 ? 0.1514 0.1420 0.1631 -0.0056 -0.0037 0.0026 48 ARG A N 238 C CA A ARG A 32 ? 0.1661 0.1580 0.1792 -0.0063 -0.0059 0.0036 48 ARG A CA 239 C CA B ARG A 32 ? 0.1590 0.1508 0.1720 -0.0064 -0.0059 0.0036 48 ARG A CA 240 C C . ARG A 32 ? 0.1606 0.1533 0.1761 -0.0068 -0.0062 0.0036 48 ARG A C 241 O O . ARG A 32 ? 0.1629 0.1554 0.1790 -0.0062 -0.0047 0.0032 48 ARG A O 242 C CB A ARG A 32 ? 0.1822 0.1753 0.1975 -0.0056 -0.0065 0.0057 48 ARG A CB 243 C CB B ARG A 32 ? 0.1640 0.1571 0.1793 -0.0057 -0.0066 0.0057 48 ARG A CB 244 C CG A ARG A 32 ? 0.2075 0.1990 0.2199 -0.0054 -0.0066 0.0060 48 ARG A CG 245 C CG B ARG A 32 ? 0.1758 0.1673 0.1884 -0.0053 -0.0064 0.0060 48 ARG A CG 246 C CD A ARG A 32 ? 0.2510 0.2421 0.2605 -0.0068 -0.0086 0.0055 48 ARG A CD 247 C CD B ARG A 32 ? 0.1895 0.1802 0.1984 -0.0066 -0.0080 0.0053 48 ARG A CD 248 N NE A ARG A 32 ? 0.3077 0.2969 0.3132 -0.0070 -0.0083 0.0054 48 ARG A NE 249 N NE B ARG A 32 ? 0.1882 0.1804 0.1982 -0.0072 -0.0105 0.0065 48 ARG A NE 250 C CZ A ARG A 32 ? 0.3475 0.3365 0.3518 -0.0071 -0.0098 0.0068 48 ARG A CZ 251 C CZ B ARG A 32 ? 0.2201 0.2121 0.2275 -0.0085 -0.0122 0.0057 48 ARG A CZ 252 N NH1 A ARG A 32 ? 0.4262 0.4172 0.4333 -0.0068 -0.0117 0.0084 48 ARG A NH1 253 N NH1 B ARG A 32 ? 0.2300 0.2205 0.2336 -0.0093 -0.0116 0.0038 48 ARG A NH1 254 N NH2 A ARG A 32 ? 0.2150 0.2019 0.2153 -0.0076 -0.0094 0.0068 48 ARG A NH2 255 N NH2 B ARG A 32 ? 0.2276 0.2214 0.2362 -0.0091 -0.0145 0.0068 48 ARG A NH2 256 N N . ALA A 33 ? 0.1861 0.1797 0.2026 -0.0080 -0.0083 0.0041 49 ALA A N 257 C CA . ALA A 33 ? 0.1850 0.1787 0.2032 -0.0089 -0.0086 0.0040 49 ALA A CA 258 C C . ALA A 33 ? 0.1929 0.1886 0.2149 -0.0082 -0.0070 0.0053 49 ALA A C 259 O O . ALA A 33 ? 0.1894 0.1844 0.2117 -0.0086 -0.0063 0.0051 49 ALA A O 260 C CB . ALA A 33 ? 0.1899 0.1843 0.2086 -0.0106 -0.0110 0.0043 49 ALA A CB 261 N N . ARG A 34 ? 0.1801 0.1780 0.2046 -0.0071 -0.0064 0.0067 50 ARG A N 262 C CA . ARG A 34 ? 0.2077 0.2079 0.2359 -0.0063 -0.0048 0.0079 50 ARG A CA 263 C C . ARG A 34 ? 0.1826 0.1817 0.2099 -0.0044 -0.0024 0.0076 50 ARG A C 264 O O . ARG A 34 ? 0.1742 0.1752 0.2043 -0.0033 -0.0010 0.0085 50 ARG A O 265 C CB . ARG A 34 ? 0.2861 0.2903 0.3185 -0.0063 -0.0059 0.0098 50 ARG A CB 266 C CG . ARG A 34 ? 0.4267 0.4342 0.4634 -0.0066 -0.0051 0.0109 50 ARG A CG 267 C CD . ARG A 34 ? 0.4903 0.5027 0.5317 -0.0060 -0.0059 0.0127 50 ARG A CD 268 N NE . ARG A 34 ? 0.5739 0.5902 0.6197 -0.0063 -0.0046 0.0137 50 ARG A NE 269 C CZ . ARG A 34 ? 0.6029 0.6225 0.6517 -0.0085 -0.0057 0.0145 50 ARG A CZ 270 N NH1 . ARG A 34 ? 0.7427 0.7620 0.7907 -0.0107 -0.0083 0.0143 50 ARG A NH1 271 N NH2 . ARG A 34 ? 0.7198 0.7431 0.7724 -0.0086 -0.0041 0.0154 50 ARG A NH2 272 N N . TRP A 35 ? 0.1538 0.1502 0.1773 -0.0041 -0.0020 0.0062 51 TRP A N 273 C CA . TRP A 35 ? 0.1458 0.1410 0.1682 -0.0027 0.0000 0.0059 51 TRP A CA 274 C C . TRP A 35 ? 0.1434 0.1364 0.1624 -0.0028 0.0010 0.0040 51 TRP A C 275 O O . TRP A 35 ? 0.1544 0.1461 0.1706 -0.0036 0.0001 0.0029 51 TRP A O 276 C CB . TRP A 35 ? 0.1646 0.1587 0.1858 -0.0021 -0.0007 0.0064 51 TRP A CB 277 C CG . TRP A 35 ? 0.1756 0.1722 0.2004 -0.0012 -0.0015 0.0084 51 TRP A CG 278 C CD1 . TRP A 35 ? 0.1680 0.1664 0.1941 -0.0020 -0.0039 0.0094 51 TRP A CD1 279 C CD2 . TRP A 35 ? 0.1620 0.1596 0.1895 0.0006 -0.0002 0.0095 51 TRP A CD2 280 N NE1 . TRP A 35 ? 0.1855 0.1865 0.2152 -0.0006 -0.0042 0.0112 51 TRP A NE1 281 C CE2 . TRP A 35 ? 0.1796 0.1802 0.2103 0.0012 -0.0019 0.0113 51 TRP A CE2 282 C CE3 . TRP A 35 ? 0.1922 0.1886 0.2195 0.0020 0.0021 0.0091 51 TRP A CE3 283 C CZ2 . TRP A 35 ? 0.1900 0.1926 0.2241 0.0034 -0.0012 0.0126 51 TRP A CZ2 284 C CZ3 . TRP A 35 ? 0.1852 0.1831 0.2155 0.0041 0.0029 0.0103 51 TRP A CZ3 285 C CH2 . TRP A 35 ? 0.1975 0.1985 0.2312 0.0049 0.0013 0.0120 51 TRP A CH2 286 N N . VAL A 36 ? 0.1501 0.1429 0.1694 -0.0020 0.0030 0.0037 52 VAL A N 287 C CA . VAL A 36 ? 0.1477 0.1390 0.1639 -0.0020 0.0041 0.0020 52 VAL A CA 288 C C . VAL A 36 ? 0.1404 0.1305 0.1556 -0.0011 0.0059 0.0016 52 VAL A C 289 O O . VAL A 36 ? 0.1531 0.1436 0.1703 -0.0001 0.0069 0.0026 52 VAL A O 290 C CB . VAL A 36 ? 0.1514 0.1433 0.1683 -0.0020 0.0047 0.0018 52 VAL A CB 291 C CG1 . VAL A 36 ? 0.1646 0.1555 0.1788 -0.0016 0.0060 0.0002 52 VAL A CG1 292 C CG2 . VAL A 36 ? 0.1550 0.1468 0.1718 -0.0030 0.0029 0.0017 52 VAL A CG2 293 N N . VAL A 37 ? 0.1275 0.1163 0.1396 -0.0017 0.0062 0.0002 53 VAL A N 294 C CA . VAL A 37 ? 0.1308 0.1179 0.1411 -0.0014 0.0079 -0.0005 53 VAL A CA 295 C C . VAL A 37 ? 0.1357 0.1233 0.1450 -0.0013 0.0091 -0.0018 53 VAL A C 296 O O . VAL A 37 ? 0.1391 0.1276 0.1474 -0.0017 0.0085 -0.0028 53 VAL A O 297 C CB . VAL A 37 ? 0.1454 0.1311 0.1526 -0.0025 0.0075 -0.0013 53 VAL A CB 298 C CG1 . VAL A 37 ? 0.1586 0.1422 0.1636 -0.0027 0.0092 -0.0022 53 VAL A CG1 299 C CG2 . VAL A 37 ? 0.1638 0.1487 0.1714 -0.0026 0.0061 0.0001 53 VAL A CG2 300 N N . SER A 38 ? 0.1375 0.1244 0.1469 -0.0005 0.0108 -0.0020 54 SER A N 301 C CA . SER A 38 ? 0.1413 0.1286 0.1493 -0.0004 0.0120 -0.0033 54 SER A CA 302 C C . SER A 38 ? 0.1413 0.1266 0.1478 -0.0002 0.0138 -0.0040 54 SER A C 303 O O . SER A 38 ? 0.1542 0.1374 0.1602 -0.0003 0.0139 -0.0036 54 SER A O 304 C CB . SER A 38 ? 0.1522 0.1411 0.1623 0.0002 0.0123 -0.0024 54 SER A CB 305 O OG . SER A 38 ? 0.1459 0.1353 0.1543 0.0003 0.0131 -0.0036 54 SER A OG 306 N N . ALA A 39 ? 0.1337 0.1193 0.1389 -0.0001 0.0150 -0.0052 55 ALA A N 307 C CA . ALA A 39 ? 0.1409 0.1244 0.1441 -0.0001 0.0166 -0.0063 55 ALA A CA 308 C C . ALA A 39 ? 0.1653 0.1485 0.1701 0.0014 0.0181 -0.0055 55 ALA A C 309 O O . ALA A 39 ? 0.1817 0.1671 0.1880 0.0020 0.0183 -0.0049 55 ALA A O 310 C CB . ALA A 39 ? 0.1613 0.1458 0.1620 -0.0011 0.0170 -0.0082 55 ALA A CB 311 N N . ALA A 40 ? 0.1510 0.1313 0.1553 0.0021 0.0192 -0.0054 56 ALA A N 312 C CA . ALA A 40 ? 0.1471 0.1272 0.1530 0.0040 0.0207 -0.0049 56 ALA A CA 313 C C . ALA A 40 ? 0.1678 0.1490 0.1725 0.0042 0.0222 -0.0060 56 ALA A C 314 O O . ALA A 40 ? 0.1703 0.1534 0.1770 0.0054 0.0231 -0.0051 56 ALA A O 315 C CB . ALA A 40 ? 0.1907 0.1666 0.1951 0.0047 0.0217 -0.0051 56 ALA A CB 316 N N . HIS A 41 ? 0.1567 0.1371 0.1580 0.0028 0.0224 -0.0078 57 HIS A N 317 C CA . HIS A 41 ? 0.1707 0.1521 0.1704 0.0030 0.0237 -0.0090 57 HIS A CA 318 C C . HIS A 41 ? 0.1799 0.1648 0.1812 0.0033 0.0232 -0.0079 57 HIS A C 319 O O . HIS A 41 ? 0.2074 0.1933 0.2080 0.0039 0.0244 -0.0081 57 HIS A O 320 C CB . HIS A 41 ? 0.1744 0.1546 0.1702 0.0013 0.0237 -0.0112 57 HIS A CB 321 C CG . HIS A 41 ? 0.1785 0.1616 0.1738 0.0000 0.0221 -0.0117 57 HIS A CG 322 N ND1 . HIS A 41 ? 0.1587 0.1417 0.1532 -0.0014 0.0209 -0.0123 57 HIS A ND1 323 C CD2 . HIS A 41 ? 0.1652 0.1512 0.1604 0.0002 0.0215 -0.0115 57 HIS A CD2 324 C CE1 . HIS A 41 ? 0.1549 0.1410 0.1491 -0.0020 0.0197 -0.0128 57 HIS A CE1 325 N NE2 . HIS A 41 ? 0.1626 0.1503 0.1572 -0.0008 0.0199 -0.0122 57 HIS A NE2 326 N N . CYS A 42 ? 0.1646 0.1510 0.1678 0.0029 0.0214 -0.0067 58 CYS A N 327 C CA . CYS A 42 ? 0.1785 0.1675 0.1830 0.0030 0.0208 -0.0056 58 CYS A CA 328 C C . CYS A 42 ? 0.1597 0.1500 0.1669 0.0040 0.0219 -0.0039 58 CYS A C 329 O O . CYS A 42 ? 0.1820 0.1741 0.1897 0.0039 0.0219 -0.0031 58 CYS A O 330 C CB . CYS A 42 ? 0.1652 0.1549 0.1710 0.0023 0.0186 -0.0049 58 CYS A CB 331 S SG . CYS A 42 ? 0.1914 0.1809 0.1943 0.0010 0.0173 -0.0068 58 CYS A SG 332 N N . PHE A 43 ? 0.1821 0.1718 0.1913 0.0051 0.0228 -0.0034 59 PHE A N 333 C CA . PHE A 43 ? 0.1772 0.1691 0.1899 0.0061 0.0237 -0.0018 59 PHE A CA 334 C C . PHE A 43 ? 0.2095 0.2013 0.2218 0.0076 0.0263 -0.0024 59 PHE A C 335 O O . PHE A 43 ? 0.2122 0.2065 0.2274 0.0086 0.0274 -0.0012 59 PHE A O 336 C CB . PHE A 43 ? 0.1900 0.1824 0.2060 0.0065 0.0225 -0.0005 59 PHE A CB 337 C CG . PHE A 43 ? 0.1983 0.1911 0.2147 0.0051 0.0201 0.0001 59 PHE A CG 338 C CD1 . PHE A 43 ? 0.2044 0.1997 0.2231 0.0044 0.0194 0.0015 59 PHE A CD1 339 C CD2 . PHE A 43 ? 0.1865 0.1772 0.2008 0.0042 0.0188 -0.0008 59 PHE A CD2 340 C CE1 . PHE A 43 ? 0.2380 0.2331 0.2566 0.0031 0.0172 0.0018 59 PHE A CE1 341 C CE2 . PHE A 43 ? 0.2323 0.2235 0.2467 0.0030 0.0167 -0.0005 59 PHE A CE2 342 C CZ . PHE A 43 ? 0.2539 0.2470 0.2703 0.0026 0.0159 0.0007 59 PHE A CZ 343 N N . SER A 44 ? 0.2113 0.2003 0.2199 0.0076 0.0272 -0.0044 60 SER A N 344 C CA . SER A 44 ? 0.2635 0.2516 0.2709 0.0090 0.0296 -0.0054 60 SER A CA 345 C C . SER A 44 ? 0.2476 0.2388 0.2553 0.0093 0.0310 -0.0048 60 SER A C 346 O O . SER A 44 ? 0.2647 0.2567 0.2704 0.0080 0.0305 -0.0049 60 SER A O 347 C CB . SER A 44 ? 0.3286 0.3133 0.3314 0.0083 0.0300 -0.0078 60 SER A CB 348 O OG . SER A 44 ? 0.4160 0.3976 0.4182 0.0079 0.0289 -0.0082 60 SER A OG 349 N N . HIS A 45 ? 0.2471 0.2401 0.2573 0.0110 0.0329 -0.0042 61 HIS A N 350 C CA . HIS A 45 ? 0.2984 0.2947 0.3091 0.0112 0.0347 -0.0035 61 HIS A CA 351 C C . HIS A 45 ? 0.3186 0.3179 0.3312 0.0097 0.0335 -0.0015 61 HIS A C 352 O O . HIS A 45 ? 0.3706 0.3717 0.3820 0.0091 0.0345 -0.0009 61 HIS A O 353 C CB . HIS A 45 ? 0.3534 0.3481 0.3591 0.0110 0.0362 -0.0054 61 HIS A CB 354 C CG . HIS A 45 ? 0.3736 0.3650 0.3771 0.0125 0.0378 -0.0075 61 HIS A CG 355 N ND1 . HIS A 45 ? 0.4318 0.4191 0.4327 0.0120 0.0369 -0.0091 61 HIS A ND1 356 C CD2 . HIS A 45 ? 0.4393 0.4309 0.4429 0.0146 0.0405 -0.0083 61 HIS A CD2 357 C CE1 . HIS A 45 ? 0.4815 0.4657 0.4806 0.0135 0.0387 -0.0108 61 HIS A CE1 358 N NE2 . HIS A 45 ? 0.4261 0.4130 0.4269 0.0153 0.0410 -0.0104 61 HIS A NE2 359 N N . ARG A 46 ? 0.2997 0.2992 0.3148 0.0089 0.0312 -0.0003 62 ARG A N 360 C CA . ARG A 46 ? 0.3121 0.3137 0.3289 0.0073 0.0298 0.0014 62 ARG A CA 361 C C . ARG A 46 ? 0.3075 0.3129 0.3295 0.0075 0.0301 0.0034 62 ARG A C 362 O O . ARG A 46 ? 0.2644 0.2704 0.2893 0.0086 0.0297 0.0036 62 ARG A O 363 C CB . ARG A 46 ? 0.2837 0.2832 0.2996 0.0061 0.0271 0.0013 62 ARG A CB 364 C CG . ARG A 46 ? 0.3458 0.3428 0.3570 0.0056 0.0265 -0.0003 62 ARG A CG 365 C CD . ARG A 46 ? 0.4098 0.4073 0.4191 0.0046 0.0261 0.0004 62 ARG A CD 366 N NE . ARG A 46 ? 0.4453 0.4413 0.4503 0.0044 0.0258 -0.0011 62 ARG A NE 367 C CZ . ARG A 46 ? 0.5074 0.5033 0.5098 0.0039 0.0253 -0.0008 62 ARG A CZ 368 N NH1 . ARG A 46 ? 0.5465 0.5433 0.5499 0.0033 0.0251 0.0011 62 ARG A NH1 369 N NH2 . ARG A 46 ? 0.5048 0.4997 0.5034 0.0039 0.0249 -0.0024 62 ARG A NH2 370 N N . ASP A 47 A 0.3231 0.3313 0.3461 0.0064 0.0307 0.0048 62 ASP A N 371 C CA . ASP A 47 A 0.3353 0.3475 0.3633 0.0058 0.0305 0.0068 62 ASP A CA 372 C C . ASP A 47 A 0.3194 0.3304 0.3485 0.0043 0.0274 0.0076 62 ASP A C 373 O O . ASP A 47 A 0.3317 0.3410 0.3586 0.0025 0.0261 0.0080 62 ASP A O 374 C CB . ASP A 47 A 0.3717 0.3867 0.3998 0.0044 0.0321 0.0082 62 ASP A CB 375 C CG . ASP A 47 A 0.4180 0.4381 0.4516 0.0037 0.0324 0.0101 62 ASP A CG 376 O OD1 . ASP A 47 A 0.3733 0.3946 0.4105 0.0036 0.0306 0.0107 62 ASP A OD1 377 O OD2 . ASP A 47 A 0.5157 0.5390 0.5500 0.0029 0.0344 0.0111 62 ASP A OD2 378 N N . LEU A 48 B 0.2951 0.3069 0.3273 0.0051 0.0263 0.0077 62 LEU A N 379 C CA . LEU A 48 B 0.3529 0.3637 0.3860 0.0038 0.0234 0.0083 62 LEU A CA 380 C C . LEU A 48 B 0.3259 0.3385 0.3606 0.0014 0.0223 0.0100 62 LEU A C 381 O O . LEU A 48 B 0.3175 0.3277 0.3508 0.0000 0.0201 0.0100 62 LEU A O 382 C CB . LEU A 48 B 0.3822 0.3944 0.4188 0.0050 0.0225 0.0086 62 LEU A CB 383 C CG . LEU A 48 B 0.4494 0.4579 0.4838 0.0064 0.0218 0.0073 62 LEU A CG 384 C CD1 . LEU A 48 B 0.3919 0.4023 0.4301 0.0074 0.0206 0.0082 62 LEU A CD1 385 C CD2 . LEU A 48 B 0.3642 0.3689 0.3947 0.0050 0.0200 0.0063 62 LEU A CD2 386 N N . ARG A 49 C 0.3682 0.3848 0.4056 0.0008 0.0240 0.0112 62 ARG A N 387 C CA . ARG A 49 C 0.3727 0.3909 0.4116 -0.0018 0.0232 0.0130 62 ARG A CA 388 C C . ARG A 49 C 0.3162 0.3302 0.3502 -0.0033 0.0227 0.0129 62 ARG A C 389 O O . ARG A 49 C 0.3527 0.3662 0.3869 -0.0057 0.0214 0.0142 62 ARG A O 390 C CB . ARG A 49 C 0.4653 0.4892 0.5081 -0.0022 0.0255 0.0143 62 ARG A CB 391 C CG . ARG A 49 C 0.5678 0.5967 0.6157 -0.0001 0.0263 0.0144 62 ARG A CG 392 C CD . ARG A 49 C 0.6786 0.7134 0.7299 0.0000 0.0292 0.0154 62 ARG A CD 393 N NE . ARG A 49 C 0.7822 0.8153 0.8294 0.0001 0.0316 0.0148 62 ARG A NE 394 C CZ . ARG A 49 C 0.8978 0.9353 0.9465 0.0003 0.0346 0.0154 62 ARG A CZ 395 N NH1 . ARG A 49 C 0.8717 0.9161 0.9263 0.0004 0.0356 0.0164 62 ARG A NH1 396 N NH2 . ARG A 49 C 0.9494 0.9848 0.9936 0.0004 0.0366 0.0148 62 ARG A NH2 397 N N . THR A 50 ? 0.2679 0.2790 0.2976 -0.0020 0.0236 0.0116 63 THR A N 398 C CA . THR A 50 ? 0.2636 0.2708 0.2886 -0.0029 0.0229 0.0114 63 THR A CA 399 C C . THR A 50 ? 0.2546 0.2579 0.2773 -0.0026 0.0203 0.0102 63 THR A C 400 O O . THR A 50 ? 0.2705 0.2705 0.2893 -0.0030 0.0194 0.0098 63 THR A O 401 C CB . THR A 50 ? 0.3075 0.3140 0.3288 -0.0018 0.0250 0.0106 63 THR A CB 402 O OG1 . THR A 50 ? 0.3155 0.3209 0.3355 0.0001 0.0254 0.0086 63 THR A OG1 403 C CG2 . THR A 50 ? 0.3247 0.3353 0.3480 -0.0020 0.0278 0.0118 63 THR A CG2 404 N N . GLY A 51 ? 0.2314 0.2353 0.2564 -0.0020 0.0193 0.0095 64 GLY A N 405 C CA . GLY A 51 ? 0.2112 0.2121 0.2342 -0.0017 0.0171 0.0082 64 GLY A CA 406 C C . GLY A 51 ? 0.2060 0.2060 0.2300 -0.0033 0.0147 0.0089 64 GLY A C 407 O O . GLY A 51 ? 0.2212 0.2236 0.2488 -0.0044 0.0144 0.0102 64 GLY A O 408 N N . LEU A 52 ? 0.1912 0.1878 0.2120 -0.0033 0.0131 0.0079 65 LEU A N 409 C CA . LEU A 52 ? 0.1996 0.1946 0.2206 -0.0045 0.0107 0.0080 65 LEU A CA 410 C C . LEU A 52 ? 0.1898 0.1829 0.2085 -0.0035 0.0094 0.0062 65 LEU A C 411 O O . LEU A 52 ? 0.1948 0.1870 0.2109 -0.0023 0.0101 0.0049 65 LEU A O 412 C CB . LEU A 52 ? 0.2228 0.2152 0.2418 -0.0059 0.0098 0.0089 65 LEU A CB 413 C CG . LEU A 52 ? 0.2391 0.2331 0.2600 -0.0077 0.0109 0.0109 65 LEU A CG 414 C CD1 . LEU A 52 ? 0.2793 0.2694 0.2968 -0.0088 0.0101 0.0116 65 LEU A CD1 415 C CD2 . LEU A 52 ? 0.2318 0.2287 0.2571 -0.0093 0.0100 0.0119 65 LEU A CD2 416 N N . VAL A 53 ? 0.1629 0.1557 0.1826 -0.0042 0.0076 0.0060 66 VAL A N 417 C CA . VAL A 53 ? 0.1572 0.1483 0.1746 -0.0035 0.0064 0.0043 66 VAL A CA 418 C C . VAL A 53 ? 0.1750 0.1633 0.1905 -0.0044 0.0044 0.0040 66 VAL A C 419 O O . VAL A 53 ? 0.1736 0.1617 0.1907 -0.0059 0.0032 0.0050 66 VAL A O 420 C CB . VAL A 53 ? 0.1656 0.1583 0.1851 -0.0035 0.0058 0.0042 66 VAL A CB 421 C CG1 . VAL A 53 ? 0.2227 0.2137 0.2396 -0.0031 0.0046 0.0026 66 VAL A CG1 422 C CG2 . VAL A 53 ? 0.1863 0.1810 0.2074 -0.0024 0.0077 0.0045 66 VAL A CG2 423 N N . VAL A 54 ? 0.1526 0.1388 0.1648 -0.0034 0.0040 0.0026 67 VAL A N 424 C CA . VAL A 54 ? 0.1550 0.1380 0.1649 -0.0036 0.0022 0.0020 67 VAL A CA 425 C C . VAL A 54 ? 0.1600 0.1428 0.1685 -0.0030 0.0011 0.0002 67 VAL A C 426 O O . VAL A 54 ? 0.1533 0.1371 0.1605 -0.0018 0.0017 -0.0011 67 VAL A O 427 C CB . VAL A 54 ? 0.1891 0.1700 0.1960 -0.0026 0.0025 0.0019 67 VAL A CB 428 C CG1 . VAL A 54 ? 0.2108 0.1878 0.2151 -0.0024 0.0007 0.0013 67 VAL A CG1 429 C CG2 . VAL A 54 ? 0.2160 0.1973 0.2239 -0.0034 0.0039 0.0038 67 VAL A CG2 430 N N . LEU A 55 ? 0.1576 0.1391 0.1662 -0.0041 -0.0005 0.0001 68 LEU A N 431 C CA . LEU A 55 ? 0.1703 0.1514 0.1774 -0.0037 -0.0017 -0.0015 68 LEU A CA 432 C C . LEU A 55 ? 0.1752 0.1526 0.1793 -0.0033 -0.0031 -0.0025 68 LEU A C 433 O O . LEU A 55 ? 0.1871 0.1619 0.1908 -0.0038 -0.0035 -0.0015 68 LEU A O 434 C CB . LEU A 55 ? 0.1765 0.1588 0.1855 -0.0052 -0.0027 -0.0009 68 LEU A CB 435 C CG . LEU A 55 ? 0.1914 0.1769 0.2036 -0.0054 -0.0016 0.0003 68 LEU A CG 436 C CD1 . LEU A 55 ? 0.2201 0.2067 0.2341 -0.0067 -0.0030 0.0011 68 LEU A CD1 437 C CD2 . LEU A 55 ? 0.1987 0.1855 0.2100 -0.0042 -0.0002 -0.0006 68 LEU A CD2 438 N N . GLY A 56 ? 0.1693 0.1464 0.1714 -0.0022 -0.0038 -0.0045 69 GLY A N 439 C CA . GLY A 56 ? 0.1678 0.1413 0.1670 -0.0014 -0.0052 -0.0057 69 GLY A CA 440 C C . GLY A 56 ? 0.1986 0.1703 0.1957 0.0004 -0.0049 -0.0060 69 GLY A C 441 O O . GLY A 56 ? 0.2007 0.1684 0.1954 0.0011 -0.0061 -0.0065 69 GLY A O 442 N N . ALA A 57 ? 0.1713 0.1456 0.1690 0.0013 -0.0034 -0.0058 70 ALA A N 443 C CA . ALA A 57 ? 0.1682 0.1412 0.1640 0.0031 -0.0032 -0.0058 70 ALA A CA 444 C C . ALA A 57 ? 0.1725 0.1473 0.1666 0.0055 -0.0032 -0.0080 70 ALA A C 445 O O . ALA A 57 ? 0.1675 0.1458 0.1623 0.0056 -0.0027 -0.0094 70 ALA A O 446 C CB . ALA A 57 ? 0.1718 0.1468 0.1691 0.0026 -0.0016 -0.0042 70 ALA A CB 447 N N . HIS A 58 ? 0.1844 0.1567 0.1761 0.0075 -0.0039 -0.0082 71 HIS A N 448 C CA . HIS A 58 ? 0.1728 0.1477 0.1633 0.0100 -0.0038 -0.0099 71 HIS A CA 449 C C . HIS A 58 ? 0.1954 0.1702 0.1849 0.0111 -0.0034 -0.0088 71 HIS A C 450 O O . HIS A 58 ? 0.1940 0.1728 0.1843 0.0113 -0.0023 -0.0091 71 HIS A O 451 C CB . HIS A 58 ? 0.1883 0.1611 0.1765 0.0123 -0.0053 -0.0118 71 HIS A CB 452 C CG . HIS A 58 ? 0.1941 0.1712 0.1818 0.0148 -0.0051 -0.0137 71 HIS A CG 453 N ND1 . HIS A 58 ? 0.1887 0.1714 0.1780 0.0143 -0.0041 -0.0151 71 HIS A ND1 454 C CD2 . HIS A 58 ? 0.2109 0.1875 0.1966 0.0179 -0.0058 -0.0143 71 HIS A CD2 455 C CE1 . HIS A 58 ? 0.1987 0.1850 0.1875 0.0167 -0.0042 -0.0167 71 HIS A CE1 456 N NE2 . HIS A 58 ? 0.2161 0.1987 0.2027 0.0191 -0.0053 -0.0162 71 HIS A NE2 457 N N . VAL A 59 ? 0.1987 0.1685 0.1862 0.0116 -0.0042 -0.0074 72 VAL A N 458 C CA . VAL A 59 ? 0.2376 0.2063 0.2237 0.0123 -0.0038 -0.0058 72 VAL A CA 459 C C . VAL A 59 ? 0.2336 0.2010 0.2210 0.0094 -0.0028 -0.0034 72 VAL A C 460 O O . VAL A 59 ? 0.2344 0.1978 0.2217 0.0079 -0.0034 -0.0021 72 VAL A O 461 C CB . VAL A 59 ? 0.2525 0.2160 0.2350 0.0146 -0.0054 -0.0055 72 VAL A CB 462 C CG1 . VAL A 59 ? 0.2652 0.2281 0.2458 0.0155 -0.0050 -0.0039 72 VAL A CG1 463 C CG2 . VAL A 59 ? 0.2620 0.2268 0.2435 0.0176 -0.0065 -0.0081 72 VAL A CG2 464 N N . LEU A 60 ? 0.2274 0.1988 0.2165 0.0086 -0.0012 -0.0029 73 LEU A N 465 C CA . LEU A 60 ? 0.2562 0.2277 0.2473 0.0061 0.0001 -0.0010 73 LEU A CA 466 C C . LEU A 60 ? 0.2665 0.2344 0.2558 0.0055 0.0002 0.0012 73 LEU A C 467 O O . LEU A 60 ? 0.2909 0.2582 0.2818 0.0032 0.0009 0.0029 73 LEU A O 468 C CB . LEU A 60 ? 0.2499 0.2262 0.2428 0.0057 0.0019 -0.0013 73 LEU A CB 469 C CG . LEU A 60 ? 0.2598 0.2397 0.2549 0.0055 0.0021 -0.0031 73 LEU A CG 470 C CD1 . LEU A 60 ? 0.2413 0.2249 0.2371 0.0054 0.0038 -0.0036 73 LEU A CD1 471 C CD2 . LEU A 60 ? 0.2831 0.2624 0.2806 0.0035 0.0020 -0.0024 73 LEU A CD2 472 N N . SER A 61 ? 0.2883 0.2540 0.2742 0.0076 -0.0005 0.0014 74 SER A N 473 C CA . SER A 61 ? 0.3166 0.2784 0.3000 0.0070 -0.0004 0.0037 74 SER A CA 474 C C . SER A 61 ? 0.3239 0.2793 0.3055 0.0063 -0.0019 0.0047 74 SER A C 475 O O . SER A 61 ? 0.3918 0.3431 0.3712 0.0054 -0.0018 0.0069 74 SER A O 476 C CB . SER A 61 ? 0.3287 0.2905 0.3088 0.0096 -0.0006 0.0037 74 SER A CB 477 O OG . SER A 61 ? 0.3559 0.3170 0.3344 0.0125 -0.0024 0.0018 74 SER A OG 478 N N . THR A 62 ? 0.3201 0.2744 0.3025 0.0066 -0.0031 0.0031 75 THR A N 479 C CA . THR A 62 ? 0.3531 0.3011 0.3336 0.0058 -0.0047 0.0036 75 THR A CA 480 C C . THR A 62 ? 0.3599 0.3089 0.3437 0.0027 -0.0045 0.0037 75 THR A C 481 O O . THR A 62 ? 0.2964 0.2502 0.2832 0.0024 -0.0040 0.0024 75 THR A O 482 C CB . THR A 62 ? 0.3615 0.3072 0.3397 0.0088 -0.0065 0.0013 75 THR A CB 483 O OG1 . THR A 62 ? 0.3995 0.3452 0.3751 0.0121 -0.0068 0.0010 75 THR A OG1 484 C CG2 . THR A 62 ? 0.4164 0.3545 0.3921 0.0081 -0.0081 0.0016 75 THR A CG2 485 N N . ALA A 63 ? 0.3745 0.3189 0.3575 0.0002 -0.0050 0.0054 76 ALA A N 486 C CA . ALA A 63 ? 0.4047 0.3498 0.3906 -0.0028 -0.0052 0.0056 76 ALA A CA 487 C C . ALA A 63 ? 0.4082 0.3506 0.3929 -0.0020 -0.0071 0.0035 76 ALA A C 488 O O . ALA A 63 ? 0.4232 0.3596 0.4057 -0.0032 -0.0085 0.0037 76 ALA A O 489 C CB . ALA A 63 ? 0.4263 0.3677 0.4117 -0.0061 -0.0051 0.0082 76 ALA A CB 490 N N . GLU A 64 ? 0.3015 0.2481 0.2876 -0.0002 -0.0070 0.0013 77 GLU A N 491 C CA . GLU A 64 ? 0.2851 0.2298 0.2698 0.0010 -0.0086 -0.0010 77 GLU A CA 492 C C . GLU A 64 ? 0.2885 0.2327 0.2749 -0.0020 -0.0094 -0.0010 77 GLU A C 493 O O . GLU A 64 ? 0.2812 0.2296 0.2712 -0.0042 -0.0085 0.0000 77 GLU A O 494 C CB . GLU A 64 ? 0.2691 0.2193 0.2550 0.0033 -0.0080 -0.0031 77 GLU A CB 495 C CG . GLU A 64 ? 0.2726 0.2243 0.2571 0.0064 -0.0074 -0.0035 77 GLU A CG 496 C CD . GLU A 64 ? 0.2343 0.1923 0.2205 0.0078 -0.0066 -0.0054 77 GLU A CD 497 O OE1 . GLU A 64 ? 0.2396 0.2017 0.2289 0.0059 -0.0056 -0.0052 77 GLU A OE1 498 O OE2 . GLU A 64 ? 0.2425 0.2014 0.2271 0.0107 -0.0069 -0.0070 77 GLU A OE2 499 N N . PRO A 65 ? 0.2688 0.2081 0.2526 -0.0018 -0.0111 -0.0024 78 PRO A N 500 C CA . PRO A 65 ? 0.3020 0.2404 0.2869 -0.0049 -0.0122 -0.0025 78 PRO A CA 501 C C . PRO A 65 ? 0.2762 0.2211 0.2647 -0.0057 -0.0118 -0.0033 78 PRO A C 502 O O . PRO A 65 ? 0.2677 0.2138 0.2583 -0.0087 -0.0123 -0.0024 78 PRO A O 503 C CB . PRO A 65 ? 0.3150 0.2467 0.2955 -0.0038 -0.0140 -0.0045 78 PRO A CB 504 C CG . PRO A 65 ? 0.3491 0.2795 0.3269 0.0004 -0.0138 -0.0058 78 PRO A CG 505 C CD . PRO A 65 ? 0.2926 0.2261 0.2718 0.0011 -0.0123 -0.0039 78 PRO A CD 506 N N . THR A 66 ? 0.2644 0.2134 0.2533 -0.0032 -0.0110 -0.0047 79 THR A N 507 C CA . THR A 66 ? 0.2520 0.2066 0.2437 -0.0038 -0.0105 -0.0054 79 THR A CA 508 C C . THR A 66 ? 0.2387 0.1987 0.2343 -0.0048 -0.0089 -0.0035 79 THR A C 509 O O . THR A 66 ? 0.2323 0.1964 0.2303 -0.0054 -0.0085 -0.0037 79 THR A O 510 C CB . THR A 66 ? 0.2592 0.2161 0.2496 -0.0011 -0.0103 -0.0078 79 THR A CB 511 O OG1 . THR A 66 ? 0.2568 0.2149 0.2467 0.0012 -0.0092 -0.0078 79 THR A OG1 512 C CG2 . THR A 66 ? 0.2752 0.2277 0.2620 0.0000 -0.0119 -0.0100 79 THR A CG2 513 N N . GLN A 67 ? 0.2193 0.1789 0.2154 -0.0049 -0.0078 -0.0018 80 GLN A N 514 C CA . GLN A 67 ? 0.2113 0.1758 0.2109 -0.0055 -0.0061 -0.0003 80 GLN A CA 515 C C . GLN A 67 ? 0.2356 0.2020 0.2385 -0.0083 -0.0062 0.0011 80 GLN A C 516 O O . GLN A 67 ? 0.2598 0.2233 0.2624 -0.0104 -0.0073 0.0020 80 GLN A O 517 C CB . GLN A 67 ? 0.2334 0.1972 0.2322 -0.0047 -0.0047 0.0009 80 GLN A CB 518 C CG . GLN A 67 ? 0.2215 0.1863 0.2184 -0.0017 -0.0041 -0.0005 80 GLN A CG 519 C CD . GLN A 67 ? 0.2346 0.1984 0.2301 -0.0008 -0.0031 0.0007 80 GLN A CD 520 O OE1 . GLN A 67 ? 0.2807 0.2450 0.2775 -0.0024 -0.0021 0.0026 80 GLN A OE1 521 N NE2 . GLN A 67 ? 0.2189 0.1818 0.2117 0.0017 -0.0034 -0.0005 80 GLN A NE2 522 N N . GLN A 68 ? 0.1922 0.1743 0.2127 -0.0154 -0.0162 0.0124 81 GLN A N 523 C CA . GLN A 68 ? 0.1865 0.1714 0.2116 -0.0171 -0.0164 0.0154 81 GLN A CA 524 C C . GLN A 68 ? 0.1923 0.1821 0.2200 -0.0162 -0.0126 0.0169 81 GLN A C 525 O O . GLN A 68 ? 0.1947 0.1859 0.2205 -0.0145 -0.0102 0.0149 81 GLN A O 526 C CB . GLN A 68 ? 0.1793 0.1636 0.2034 -0.0175 -0.0179 0.0143 81 GLN A CB 527 C CG . GLN A 68 ? 0.2016 0.1808 0.2222 -0.0179 -0.0216 0.0123 81 GLN A CG 528 C CD . GLN A 68 ? 0.2026 0.1813 0.2219 -0.0182 -0.0231 0.0114 81 GLN A CD 529 O OE1 . GLN A 68 ? 0.2163 0.1978 0.2390 -0.0191 -0.0230 0.0135 81 GLN A OE1 530 N NE2 . GLN A 68 ? 0.2129 0.1881 0.2271 -0.0171 -0.0245 0.0083 81 GLN A NE2 531 N N . VAL A 69 ? 0.1908 0.1832 0.2228 -0.0173 -0.0121 0.0203 82 VAL A N 532 C CA . VAL A 69 ? 0.2018 0.1988 0.2361 -0.0161 -0.0085 0.0219 82 VAL A CA 533 C C . VAL A 69 ? 0.2164 0.2176 0.2556 -0.0169 -0.0082 0.0245 82 VAL A C 534 O O . VAL A 69 ? 0.2387 0.2401 0.2812 -0.0191 -0.0105 0.0268 82 VAL A O 535 C CB . VAL A 69 ? 0.2366 0.2341 0.2718 -0.0162 -0.0076 0.0239 82 VAL A CB 536 C CG1 . VAL A 69 ? 0.2535 0.2558 0.2907 -0.0147 -0.0039 0.0254 82 VAL A CG1 537 C CG2 . VAL A 69 ? 0.2523 0.2456 0.2827 -0.0151 -0.0083 0.0212 82 VAL A CG2 538 N N . PHE A 70 ? 0.2008 0.2050 0.2403 -0.0152 -0.0054 0.0241 83 PHE A N 539 C CA . PHE A 70 ? 0.1777 0.1858 0.2212 -0.0153 -0.0049 0.0262 83 PHE A CA 540 C C . PHE A 70 ? 0.1804 0.1928 0.2255 -0.0132 -0.0013 0.0274 83 PHE A C 541 O O . PHE A 70 ? 0.1860 0.1976 0.2278 -0.0114 0.0008 0.0255 83 PHE A O 542 C CB . PHE A 70 ? 0.1974 0.2040 0.2388 -0.0148 -0.0056 0.0241 83 PHE A CB 543 C CG . PHE A 70 ? 0.1891 0.1922 0.2291 -0.0165 -0.0092 0.0231 83 PHE A CG 544 C CD1 . PHE A 70 ? 0.1985 0.2026 0.2422 -0.0183 -0.0118 0.0254 83 PHE A CD1 545 C CD2 . PHE A 70 ? 0.2009 0.1996 0.2358 -0.0162 -0.0101 0.0200 83 PHE A CD2 546 C CE1 . PHE A 70 ? 0.2136 0.2140 0.2556 -0.0198 -0.0154 0.0243 83 PHE A CE1 547 C CE2 . PHE A 70 ? 0.1964 0.1916 0.2295 -0.0175 -0.0135 0.0191 83 PHE A CE2 548 C CZ . PHE A 70 ? 0.2309 0.2266 0.2673 -0.0193 -0.0163 0.0212 83 PHE A CZ 549 N N . GLY A 71 ? 0.1800 0.1970 0.2301 -0.0134 -0.0007 0.0303 84 GLY A N 550 C CA . GLY A 71 ? 0.1974 0.2186 0.2489 -0.0110 0.0025 0.0312 84 GLY A CA 551 C C . GLY A 71 ? 0.1875 0.2081 0.2375 -0.0095 0.0029 0.0294 84 GLY A C 552 O O . GLY A 71 ? 0.1875 0.2052 0.2360 -0.0105 0.0007 0.0280 84 GLY A O 553 N N . ILE A 72 ? 0.2046 0.2275 0.2544 -0.0069 0.0057 0.0293 85 ILE A N 554 C CA . ILE A 72 ? 0.2101 0.2322 0.2584 -0.0052 0.0063 0.0278 85 ILE A CA 555 C C . ILE A 72 ? 0.2188 0.2456 0.2719 -0.0043 0.0065 0.0305 85 ILE A C 556 O O . ILE A 72 ? 0.2357 0.2668 0.2913 -0.0024 0.0088 0.0321 85 ILE A O 557 C CB . ILE A 72 ? 0.2246 0.2453 0.2690 -0.0027 0.0089 0.0256 85 ILE A CB 558 C CG1 . ILE A 72 ? 0.2276 0.2443 0.2676 -0.0036 0.0085 0.0229 85 ILE A CG1 559 C CG2 . ILE A 72 ? 0.2443 0.2633 0.2868 -0.0012 0.0092 0.0241 85 ILE A CG2 560 C CD1 . ILE A 72 ? 0.2471 0.2633 0.2840 -0.0015 0.0109 0.0212 85 ILE A CD1 561 N N . ASP A 73 ? 0.2022 0.2284 0.2567 -0.0054 0.0041 0.0309 86 ASP A N 562 C CA . ASP A 73 ? 0.2251 0.2557 0.2842 -0.0044 0.0039 0.0331 86 ASP A CA 563 C C . ASP A 73 ? 0.2516 0.2822 0.3089 -0.0010 0.0062 0.0321 86 ASP A C 564 O O . ASP A 73 ? 0.2440 0.2795 0.3048 0.0011 0.0077 0.0339 86 ASP A O 565 C CB . ASP A 73 ? 0.2974 0.3264 0.3573 -0.0063 0.0004 0.0333 86 ASP A CB 566 C CG . ASP A 73 ? 0.4176 0.4518 0.4842 -0.0077 -0.0012 0.0366 86 ASP A CG 567 O OD1 . ASP A 73 ? 0.6717 0.7072 0.7404 -0.0073 -0.0028 0.0373 86 ASP A OD1 568 O OD2 . ASP A 73 ? 0.4152 0.4520 0.4849 -0.0093 -0.0010 0.0384 86 ASP A OD2 569 N N . ALA A 74 ? 0.1952 0.2204 0.2469 -0.0004 0.0063 0.0291 87 ALA A N 570 C CA . ALA A 74 ? 0.1812 0.2051 0.2306 0.0024 0.0079 0.0279 87 ALA A CA 571 C C . ALA A 74 ? 0.1810 0.1995 0.2245 0.0024 0.0087 0.0247 87 ALA A C 572 O O . ALA A 74 ? 0.1975 0.2122 0.2381 0.0003 0.0072 0.0232 87 ALA A O 573 C CB . ALA A 74 ? 0.1991 0.2224 0.2494 0.0028 0.0062 0.0286 87 ALA A CB 574 N N . LEU A 75 ? 0.1947 0.2129 0.2363 0.0049 0.0111 0.0237 88 LEU A N 575 C CA . LEU A 75 ? 0.1842 0.1976 0.2206 0.0054 0.0119 0.0207 88 LEU A CA 576 C C . LEU A 75 ? 0.1850 0.1957 0.2196 0.0072 0.0119 0.0201 88 LEU A C 577 O O . LEU A 75 ? 0.2033 0.2163 0.2397 0.0100 0.0129 0.0213 88 LEU A O 578 C CB . LEU A 75 ? 0.1828 0.1972 0.2180 0.0071 0.0142 0.0198 88 LEU A CB 579 C CG . LEU A 75 ? 0.1814 0.1914 0.2117 0.0083 0.0151 0.0169 88 LEU A CG 580 C CD1 . LEU A 75 ? 0.2087 0.2150 0.2360 0.0056 0.0140 0.0147 88 LEU A CD1 581 C CD2 . LEU A 75 ? 0.1869 0.1989 0.2165 0.0106 0.0173 0.0165 88 LEU A CD2 582 N N . THR A 76 ? 0.1940 0.1997 0.2248 0.0058 0.0109 0.0183 89 THR A N 583 C CA . THR A 76 ? 0.1885 0.1903 0.2167 0.0073 0.0109 0.0175 89 THR A CA 584 C C . THR A 76 ? 0.1855 0.1829 0.2092 0.0068 0.0118 0.0147 89 THR A C 585 O O . THR A 76 ? 0.1810 0.1761 0.2026 0.0042 0.0111 0.0135 89 THR A O 586 C CB . THR A 76 ? 0.2008 0.2003 0.2285 0.0059 0.0088 0.0183 89 THR A CB 587 O OG1 . THR A 76 ? 0.1992 0.2031 0.2314 0.0060 0.0077 0.0208 89 THR A OG1 588 C CG2 . THR A 76 ? 0.1950 0.1902 0.2199 0.0076 0.0088 0.0179 89 THR A CG2 589 N N . THR A 77 ? 0.2256 0.2220 0.2478 0.0093 0.0132 0.0137 90 THR A N 590 C CA . THR A 77 ? 0.2285 0.2207 0.2466 0.0091 0.0138 0.0111 90 THR A CA 591 C C . THR A 77 ? 0.2259 0.2128 0.2413 0.0090 0.0129 0.0106 90 THR A C 592 O O . THR A 77 ? 0.2486 0.2352 0.2648 0.0110 0.0125 0.0120 90 THR A O 593 C CB . THR A 77 ? 0.2456 0.2389 0.2632 0.0120 0.0155 0.0101 90 THR A CB 594 O OG1 . THR A 77 ? 0.2530 0.2510 0.2729 0.0118 0.0163 0.0108 90 THR A OG1 595 C CG2 . THR A 77 ? 0.2295 0.2181 0.2429 0.0119 0.0157 0.0073 90 THR A CG2 596 N N . HIS A 78 ? 0.2081 0.1908 0.2202 0.0068 0.0126 0.0087 91 HIS A N 597 C CA . HIS A 78 ? 0.2266 0.2037 0.2356 0.0064 0.0118 0.0084 91 HIS A CA 598 C C . HIS A 78 ? 0.2362 0.2111 0.2443 0.0100 0.0122 0.0082 91 HIS A C 599 O O . HIS A 78 ? 0.2399 0.2156 0.2475 0.0120 0.0133 0.0069 91 HIS A O 600 C CB . HIS A 78 ? 0.2231 0.1966 0.2291 0.0037 0.0118 0.0063 91 HIS A CB 601 C CG . HIS A 78 ? 0.2117 0.1797 0.2148 0.0022 0.0109 0.0066 91 HIS A CG 602 N ND1 . HIS A 78 ? 0.2182 0.1810 0.2187 0.0037 0.0107 0.0060 91 HIS A ND1 603 C CD2 . HIS A 78 ? 0.2536 0.2204 0.2558 -0.0003 0.0101 0.0077 91 HIS A CD2 604 C CE1 . HIS A 78 ? 0.2293 0.1877 0.2276 0.0018 0.0097 0.0068 91 HIS A CE1 605 N NE2 . HIS A 78 ? 0.2504 0.2115 0.2497 -0.0005 0.0095 0.0079 91 HIS A NE2 606 N N . PRO A 79 ? 0.2265 0.1984 0.2338 0.0111 0.0112 0.0095 92 PRO A N 607 C CA . PRO A 79 ? 0.2671 0.2369 0.2734 0.0151 0.0114 0.0094 92 PRO A CA 608 C C . PRO A 79 ? 0.2601 0.2244 0.2624 0.0157 0.0117 0.0068 92 PRO A C 609 O O . PRO A 79 ? 0.2691 0.2325 0.2704 0.0195 0.0122 0.0061 92 PRO A O 610 C CB . PRO A 79 ? 0.3062 0.2731 0.3120 0.0156 0.0099 0.0111 92 PRO A CB 611 C CG . PRO A 79 ? 0.2916 0.2573 0.2966 0.0115 0.0090 0.0117 92 PRO A CG 612 C CD . PRO A 79 ? 0.2427 0.2133 0.2499 0.0091 0.0098 0.0112 92 PRO A CD 613 N N . ASP A 80 ? 0.2487 0.2096 0.2486 0.0122 0.0113 0.0054 93 ASP A N 614 C CA . ASP A 80 ? 0.2645 0.2200 0.2608 0.0122 0.0112 0.0029 93 ASP A CA 615 C C . ASP A 80 ? 0.2810 0.2394 0.2776 0.0116 0.0122 0.0008 93 ASP A C 616 O O . ASP A 80 ? 0.2664 0.2209 0.2604 0.0112 0.0119 -0.0014 93 ASP A O 617 C CB . ASP A 80 ? 0.3391 0.2886 0.3326 0.0085 0.0101 0.0027 93 ASP A CB 618 C CG . ASP A 80 ? 0.3558 0.3011 0.3479 0.0093 0.0089 0.0046 93 ASP A CG 619 O OD1 . ASP A 80 ? 0.3982 0.3425 0.3901 0.0134 0.0087 0.0051 93 ASP A OD1 620 O OD2 . ASP A 80 ? 0.3581 0.3011 0.3491 0.0061 0.0082 0.0057 93 ASP A OD2 621 N N . TYR A 81 ? 0.2320 0.1970 0.2319 0.0116 0.0132 0.0016 94 TYR A N 622 C CA . TYR A 81 ? 0.2320 0.1998 0.2321 0.0118 0.0141 0.0000 94 TYR A CA 623 C C . TYR A 81 ? 0.2401 0.2076 0.2389 0.0162 0.0148 -0.0009 94 TYR A C 624 O O . TYR A 81 ? 0.2533 0.2230 0.2536 0.0193 0.0154 0.0007 94 TYR A O 625 C CB . TYR A 81 ? 0.2125 0.1868 0.2161 0.0106 0.0147 0.0012 94 TYR A CB 626 C CG . TYR A 81 ? 0.1864 0.1633 0.1898 0.0108 0.0155 -0.0004 94 TYR A CG 627 C CD1 . TYR A 81 ? 0.2227 0.1980 0.2246 0.0082 0.0151 -0.0026 94 TYR A CD1 628 C CD2 . TYR A 81 ? 0.2386 0.2198 0.2435 0.0136 0.0167 0.0002 94 TYR A CD2 629 C CE1 . TYR A 81 ? 0.2380 0.2155 0.2396 0.0086 0.0155 -0.0042 94 TYR A CE1 630 C CE2 . TYR A 81 ? 0.2351 0.2182 0.2393 0.0139 0.0173 -0.0012 94 TYR A CE2 631 C CZ . TYR A 81 ? 0.2688 0.2499 0.2712 0.0115 0.0166 -0.0035 94 TYR A CZ 632 O OH . TYR A 81 ? 0.3074 0.2904 0.3092 0.0119 0.0170 -0.0050 94 TYR A OH 633 N N . HIS A 82 ? 0.2268 0.1920 0.2229 0.0166 0.0148 -0.0035 95 HIS A N 634 C CA . HIS A 82 ? 0.2666 0.2303 0.2603 0.0210 0.0153 -0.0048 95 HIS A CA 635 C C . HIS A 82 ? 0.3699 0.3338 0.3618 0.0210 0.0155 -0.0074 95 HIS A C 636 O O . HIS A 82 ? 0.3793 0.3422 0.3709 0.0175 0.0147 -0.0087 95 HIS A O 637 C CB . HIS A 82 ? 0.2743 0.2305 0.2647 0.0221 0.0140 -0.0057 95 HIS A CB 638 C CG . HIS A 82 ? 0.2971 0.2512 0.2847 0.0274 0.0144 -0.0069 95 HIS A CG 639 N ND1 . HIS A 82 ? 0.3848 0.3369 0.3693 0.0289 0.0143 -0.0097 95 HIS A ND1 640 C CD2 . HIS A 82 ? 0.2797 0.2339 0.2673 0.0317 0.0148 -0.0057 95 HIS A CD2 641 C CE1 . HIS A 82 ? 0.3983 0.3488 0.3804 0.0341 0.0147 -0.0103 95 HIS A CE1 642 N NE2 . HIS A 82 ? 0.3376 0.2897 0.3218 0.0358 0.0151 -0.0078 95 HIS A NE2 643 N N . PRO A 83 ? 0.4766 0.4421 0.4671 0.0252 0.0166 -0.0081 96 PRO A N 644 C CA . PRO A 83 ? 0.4178 0.3817 0.4052 0.0257 0.0163 -0.0110 96 PRO A CA 645 C C . PRO A 83 ? 0.5778 0.5338 0.5614 0.0247 0.0143 -0.0137 96 PRO A C 646 O O . PRO A 83 ? 0.7256 0.6772 0.7088 0.0237 0.0133 -0.0131 96 PRO A O 647 C CB . PRO A 83 ? 0.4962 0.4626 0.4823 0.0310 0.0178 -0.0109 96 PRO A CB 648 C CG . PRO A 83 ? 0.5147 0.4870 0.5049 0.0319 0.0194 -0.0075 96 PRO A CG 649 C CD . PRO A 83 ? 0.4721 0.4422 0.4643 0.0292 0.0182 -0.0060 96 PRO A CD 650 N N . MET A 84 ? 0.7094 0.6634 0.6902 0.0248 0.0136 -0.0166 97 MET A N 651 C CA . MET A 84 ? 0.8408 0.7875 0.8184 0.0232 0.0114 -0.0193 97 MET A CA 652 C C . MET A 84 ? 0.8239 0.7681 0.8031 0.0179 0.0102 -0.0187 97 MET A C 653 O O . MET A 84 ? 1.0396 0.9775 1.0165 0.0161 0.0083 -0.0203 97 MET A O 654 C CB . MET A 84 ? 1.0900 1.0305 1.0634 0.0275 0.0107 -0.0204 97 MET A CB 655 C CG . MET A 84 ? 1.0079 0.9446 0.9815 0.0277 0.0103 -0.0186 97 MET A CG 656 S SD . MET A 84 ? 1.0914 1.0202 1.0595 0.0332 0.0092 -0.0204 97 MET A SD 657 C CE . MET A 84 ? 0.8632 0.7994 0.8319 0.0395 0.0120 -0.0193 97 MET A CE 658 N N . THR A 85 ? 0.6472 0.5964 0.6304 0.0153 0.0112 -0.0162 98 THR A N 659 C CA . THR A 85 ? 0.5504 0.4987 0.5352 0.0103 0.0104 -0.0156 98 THR A CA 660 C C . THR A 85 ? 0.3825 0.3379 0.3711 0.0081 0.0115 -0.0141 98 THR A C 661 O O . THR A 85 ? 0.3496 0.3099 0.3401 0.0103 0.0128 -0.0126 98 THR A O 662 C CB . THR A 85 ? 0.5942 0.5379 0.5785 0.0096 0.0098 -0.0137 98 THR A CB 663 O OG1 . THR A 85 ? 0.6519 0.5952 0.6375 0.0047 0.0093 -0.0130 98 THR A OG1 664 C CG2 . THR A 85 ? 0.5561 0.5035 0.5424 0.0123 0.0111 -0.0110 98 THR A CG2 665 N N . HIS A 86 ? 0.3522 0.3080 0.3420 0.0038 0.0110 -0.0145 99 HIS A N 666 C CA A HIS A 86 ? 0.3202 0.2821 0.3131 0.0017 0.0117 -0.0138 99 HIS A CA 667 C CA B HIS A 86 ? 0.3527 0.3147 0.3456 0.0018 0.0117 -0.0137 99 HIS A CA 668 C C . HIS A 86 ? 0.2848 0.2478 0.2795 -0.0007 0.0120 -0.0114 99 HIS A C 669 O O . HIS A 86 ? 0.2799 0.2476 0.2769 -0.0017 0.0126 -0.0104 99 HIS A O 670 C CB A HIS A 86 ? 0.3748 0.3379 0.3679 -0.0007 0.0110 -0.0162 99 HIS A CB 671 C CB B HIS A 86 ? 0.4694 0.4326 0.4626 -0.0006 0.0110 -0.0162 99 HIS A CB 672 C CG A HIS A 86 ? 0.3657 0.3234 0.3571 -0.0032 0.0096 -0.0178 99 HIS A CG 673 C CG B HIS A 86 ? 0.5132 0.4756 0.5043 0.0018 0.0105 -0.0187 99 HIS A CG 674 N ND1 A HIS A 86 ? 0.3982 0.3501 0.3865 -0.0014 0.0085 -0.0192 99 HIS A ND1 675 N ND1 B HIS A 86 ? 0.5961 0.5622 0.5872 0.0048 0.0114 -0.0187 99 HIS A ND1 676 C CD2 A HIS A 86 ? 0.4007 0.3583 0.3933 -0.0077 0.0090 -0.0182 99 HIS A CD2 677 C CD2 B HIS A 86 ? 0.6037 0.5615 0.5922 0.0017 0.0090 -0.0213 99 HIS A CD2 678 C CE1 A HIS A 86 ? 0.4158 0.3635 0.4033 -0.0048 0.0071 -0.0203 99 HIS A CE1 679 C CE1 B HIS A 86 ? 0.6116 0.5758 0.6000 0.0068 0.0106 -0.0212 99 HIS A CE1 680 N NE2 A HIS A 86 ? 0.3903 0.3419 0.3806 -0.0087 0.0075 -0.0196 99 HIS A NE2 681 N NE2 B HIS A 86 ? 0.6384 0.5974 0.6253 0.0048 0.0090 -0.0229 99 HIS A NE2 682 N N . ALA A 87 ? 0.2434 0.2016 0.2369 -0.0014 0.0114 -0.0103 100 ALA A N 683 C CA . ALA A 87 ? 0.2555 0.2139 0.2499 -0.0038 0.0116 -0.0081 100 ALA A CA 684 C C . ALA A 87 ? 0.2247 0.1864 0.2209 -0.0016 0.0122 -0.0057 100 ALA A C 685 O O . ALA A 87 ? 0.2322 0.1956 0.2289 0.0017 0.0127 -0.0054 100 ALA A O 686 C CB . ALA A 87 ? 0.2894 0.2410 0.2813 -0.0051 0.0106 -0.0076 100 ALA A CB 687 N N . ASN A 88 ? 0.2199 0.1828 0.2172 -0.0039 0.0122 -0.0039 101 ASN A N 688 C CA . ASN A 88 ? 0.2113 0.1768 0.2103 -0.0025 0.0124 -0.0015 101 ASN A CA 689 C C . ASN A 88 ? 0.1810 0.1522 0.1825 -0.0009 0.0131 -0.0013 101 ASN A C 690 O O . ASN A 88 ? 0.2040 0.1772 0.2071 0.0013 0.0133 0.0002 101 ASN A O 691 C CB . ASN A 88 ? 0.2351 0.1970 0.2330 0.0003 0.0120 -0.0003 101 ASN A CB 692 C CG . ASN A 88 ? 0.2369 0.1920 0.2317 -0.0009 0.0111 -0.0006 101 ASN A CG 693 O OD1 . ASN A 88 ? 0.2475 0.2010 0.2416 -0.0039 0.0107 0.0003 101 ASN A OD1 694 N ND2 . ASN A 88 ? 0.2593 0.2101 0.2520 0.0012 0.0107 -0.0018 101 ASN A ND2 695 N N . ASP A 89 ? 0.1743 0.1482 0.1764 -0.0024 0.0134 -0.0029 102 ASP A N 696 C CA . ASP A 89 ? 0.1894 0.1681 0.1934 -0.0011 0.0139 -0.0029 102 ASP A CA 697 C C . ASP A 89 ? 0.1715 0.1536 0.1777 -0.0023 0.0137 -0.0012 102 ASP A C 698 O O . ASP A 89 ? 0.2190 0.2035 0.2257 -0.0038 0.0136 -0.0020 102 ASP A O 699 C CB . ASP A 89 ? 0.1786 0.1584 0.1820 -0.0019 0.0140 -0.0054 102 ASP A CB 700 C CG . ASP A 89 ? 0.1662 0.1501 0.1710 -0.0001 0.0145 -0.0055 102 ASP A CG 701 O OD1 . ASP A 89 ? 0.1863 0.1720 0.1924 0.0017 0.0149 -0.0036 102 ASP A OD1 702 O OD2 . ASP A 89 ? 0.1588 0.1442 0.1634 -0.0007 0.0144 -0.0073 102 ASP A OD2 703 N N . ILE A 90 ? 0.1557 0.1377 0.1629 -0.0015 0.0134 0.0009 103 ILE A N 704 C CA . ILE A 90 ? 0.1635 0.1476 0.1722 -0.0028 0.0127 0.0026 103 ILE A CA 705 C C . ILE A 90 ? 0.1533 0.1392 0.1643 -0.0008 0.0125 0.0049 103 ILE A C 706 O O . ILE A 90 ? 0.1771 0.1615 0.1879 0.0012 0.0128 0.0056 103 ILE A O 707 C CB . ILE A 90 ? 0.1745 0.1559 0.1814 -0.0053 0.0121 0.0028 103 ILE A CB 708 C CG1 . ILE A 90 ? 0.1704 0.1538 0.1783 -0.0066 0.0112 0.0040 103 ILE A CG1 709 C CG2 . ILE A 90 ? 0.1772 0.1543 0.1826 -0.0046 0.0118 0.0037 103 ILE A CG2 710 C CD1 . ILE A 90 ? 0.2390 0.2207 0.2447 -0.0091 0.0109 0.0038 103 ILE A CD1 711 N N . CYS A 91 ? 0.1603 0.1494 0.1735 -0.0013 0.0120 0.0062 104 CYS A N 712 C CA . CYS A 91 ? 0.1690 0.1606 0.1852 0.0000 0.0116 0.0086 104 CYS A CA 713 C C . CYS A 91 ? 0.1615 0.1547 0.1791 -0.0018 0.0102 0.0097 104 CYS A C 714 O O . CYS A 91 ? 0.1570 0.1498 0.1732 -0.0037 0.0098 0.0084 104 CYS A O 715 C CB . CYS A 91 ? 0.1840 0.1789 0.2021 0.0021 0.0128 0.0090 104 CYS A CB 716 S SG . CYS A 91 ? 0.1729 0.1703 0.1915 0.0009 0.0129 0.0081 104 CYS A SG 717 N N . LEU A 92 ? 0.1509 0.1460 0.1712 -0.0011 0.0093 0.0120 105 LEU A N 718 C CA . LEU A 92 ? 0.1647 0.1613 0.1867 -0.0027 0.0076 0.0133 105 LEU A CA 719 C C . LEU A 92 ? 0.1681 0.1690 0.1942 -0.0019 0.0077 0.0150 105 LEU A C 720 O O . LEU A 92 ? 0.1693 0.1723 0.1975 0.0001 0.0087 0.0163 105 LEU A O 721 C CB . LEU A 92 ? 0.1644 0.1597 0.1863 -0.0029 0.0062 0.0147 105 LEU A CB 722 C CG . LEU A 92 ? 0.2084 0.1997 0.2263 -0.0045 0.0055 0.0135 105 LEU A CG 723 C CD1 . LEU A 92 ? 0.2667 0.2560 0.2839 -0.0040 0.0045 0.0150 105 LEU A CD1 724 C CD2 . LEU A 92 ? 0.2266 0.2182 0.2436 -0.0066 0.0043 0.0129 105 LEU A CD2 725 N N . LEU A 93 ? 0.1581 0.1600 0.1851 -0.0036 0.0065 0.0152 106 LEU A N 726 C CA . LEU A 93 ? 0.1622 0.1678 0.1931 -0.0036 0.0061 0.0173 106 LEU A CA 727 C C . LEU A 93 ? 0.1815 0.1875 0.2143 -0.0052 0.0035 0.0188 106 LEU A C 728 O O . LEU A 93 ? 0.1708 0.1743 0.2013 -0.0069 0.0019 0.0176 106 LEU A O 729 C CB . LEU A 93 ? 0.1590 0.1648 0.1891 -0.0043 0.0065 0.0162 106 LEU A CB 730 C CG . LEU A 93 ? 0.1763 0.1812 0.2039 -0.0030 0.0085 0.0142 106 LEU A CG 731 C CD1 . LEU A 93 ? 0.1737 0.1787 0.2005 -0.0038 0.0083 0.0132 106 LEU A CD1 732 C CD2 . LEU A 93 ? 0.1951 0.2023 0.2241 -0.0006 0.0105 0.0152 106 LEU A CD2 733 N N . ARG A 94 ? 0.1605 0.1695 0.1973 -0.0046 0.0030 0.0213 107 ARG A N 734 C CA A ARG A 94 ? 0.1684 0.1785 0.2079 -0.0062 0.0003 0.0229 107 ARG A CA 735 C CA B ARG A 94 ? 0.1706 0.1807 0.2101 -0.0062 0.0003 0.0229 107 ARG A CA 736 C C . ARG A 94 ? 0.1775 0.1903 0.2202 -0.0074 -0.0001 0.0243 107 ARG A C 737 O O . ARG A 94 ? 0.1932 0.2098 0.2392 -0.0063 0.0014 0.0260 107 ARG A O 738 C CB A ARG A 94 ? 0.2133 0.2260 0.2561 -0.0049 -0.0002 0.0250 107 ARG A CB 739 C CB B ARG A 94 ? 0.2213 0.2339 0.2640 -0.0049 -0.0002 0.0250 107 ARG A CB 740 C CG A ARG A 94 ? 0.2262 0.2395 0.2712 -0.0066 -0.0034 0.0265 107 ARG A CG 741 C CG B ARG A 94 ? 0.2453 0.2593 0.2912 -0.0067 -0.0033 0.0268 107 ARG A CG 742 C CD A ARG A 94 ? 0.2507 0.2668 0.2991 -0.0051 -0.0041 0.0285 107 ARG A CD 743 C CD B ARG A 94 ? 0.2637 0.2794 0.3118 -0.0054 -0.0044 0.0283 107 ARG A CD 744 N NE A ARG A 94 ? 0.2836 0.3058 0.3381 -0.0043 -0.0032 0.0310 107 ARG A NE 745 N NE B ARG A 94 ? 0.2988 0.3129 0.3465 -0.0072 -0.0078 0.0286 107 ARG A NE 746 C CZ A ARG A 94 ? 0.3138 0.3393 0.3707 -0.0015 -0.0016 0.0322 107 ARG A CZ 747 C CZ B ARG A 94 ? 0.3401 0.3573 0.3925 -0.0086 -0.0103 0.0306 107 ARG A CZ 748 N NH1 A ARG A 94 ? 0.3319 0.3543 0.3853 0.0004 -0.0010 0.0310 107 ARG A NH1 749 N NH1 B ARG A 94 ? 0.4109 0.4335 0.4690 -0.0085 -0.0094 0.0328 107 ARG A NH1 750 N NH2 A ARG A 94 ? 0.3100 0.3418 0.3727 -0.0008 -0.0006 0.0346 107 ARG A NH2 751 N NH2 B ARG A 94 ? 0.3410 0.3560 0.3922 -0.0100 -0.0136 0.0304 107 ARG A NH2 752 N N . LEU A 95 ? 0.1710 0.1816 0.2125 -0.0095 -0.0022 0.0236 108 LEU A N 753 C CA . LEU A 95 ? 0.1611 0.1731 0.2051 -0.0108 -0.0030 0.0248 108 LEU A CA 754 C C . LEU A 95 ? 0.1813 0.1970 0.2310 -0.0120 -0.0048 0.0280 108 LEU A C 755 O O . LEU A 95 ? 0.1923 0.2084 0.2432 -0.0121 -0.0065 0.0286 108 LEU A O 756 C CB . LEU A 95 ? 0.1532 0.1610 0.1935 -0.0124 -0.0049 0.0228 108 LEU A CB 757 C CG . LEU A 95 ? 0.1646 0.1692 0.1996 -0.0116 -0.0035 0.0196 108 LEU A CG 758 C CD1 . LEU A 95 ? 0.1988 0.1998 0.2305 -0.0128 -0.0055 0.0176 108 LEU A CD1 759 C CD2 . LEU A 95 ? 0.1828 0.1889 0.2176 -0.0100 -0.0005 0.0192 108 LEU A CD2 760 N N . ASN A 96 ? 0.1917 0.2101 0.2448 -0.0130 -0.0046 0.0300 109 ASN A N 761 C CA . ASN A 96 ? 0.1992 0.2216 0.2584 -0.0146 -0.0065 0.0332 109 ASN A CA 762 C C . ASN A 96 ? 0.2192 0.2386 0.2785 -0.0175 -0.0106 0.0332 109 ASN A C 763 O O . ASN A 96 ? 0.2469 0.2690 0.3111 -0.0195 -0.0124 0.0358 109 ASN A O 764 C CB . ASN A 96 ? 0.2299 0.2572 0.2934 -0.0145 -0.0043 0.0360 109 ASN A CB 765 C CG . ASN A 96 ? 0.2425 0.2674 0.3045 -0.0160 -0.0045 0.0359 109 ASN A CG 766 O OD1 . ASN A 96 ? 0.2529 0.2724 0.3099 -0.0164 -0.0057 0.0332 109 ASN A OD1 767 N ND2 . ASN A 96 ? 0.2976 0.3267 0.3638 -0.0167 -0.0034 0.0390 109 ASN A ND2 768 N N . GLY A 97 ? 0.2235 0.2375 0.2774 -0.0176 -0.0120 0.0303 110 GLY A N 769 C CA . GLY A 97 ? 0.2263 0.2366 0.2789 -0.0197 -0.0159 0.0296 110 GLY A CA 770 C C . GLY A 97 ? 0.2107 0.2161 0.2566 -0.0188 -0.0162 0.0261 110 GLY A C 771 O O . GLY A 97 ? 0.2348 0.2399 0.2778 -0.0169 -0.0134 0.0246 110 GLY A O 772 N N . SER A 98 ? 0.2049 0.2065 0.2484 -0.0201 -0.0197 0.0249 111 SER A N 773 C CA . SER A 98 ? 0.2221 0.2194 0.2592 -0.0193 -0.0201 0.0218 111 SER A CA 774 C C . SER A 98 ? 0.2387 0.2319 0.2720 -0.0197 -0.0211 0.0197 111 SER A C 775 O O . SER A 98 ? 0.2290 0.2205 0.2634 -0.0213 -0.0239 0.0203 111 SER A O 776 C CB . SER A 98 ? 0.2298 0.2257 0.2661 -0.0199 -0.0233 0.0219 111 SER A CB 777 O OG . SER A 98 ? 0.2799 0.2790 0.3185 -0.0189 -0.0222 0.0234 111 SER A OG 778 N N . ALA A 99 ? 0.2139 0.2055 0.2427 -0.0182 -0.0188 0.0171 112 ALA A N 779 C CA . ALA A 99 ? 0.2039 0.1919 0.2286 -0.0181 -0.0197 0.0147 112 ALA A CA 780 C C . ALA A 99 ? 0.2242 0.2082 0.2457 -0.0188 -0.0235 0.0134 112 ALA A C 781 O O . ALA A 99 ? 0.2359 0.2197 0.2560 -0.0187 -0.0244 0.0132 112 ALA A O 782 C CB . ALA A 99 ? 0.2145 0.2022 0.2352 -0.0164 -0.0166 0.0122 112 ALA A CB 783 N N . VAL A 100 ? 0.2291 0.2097 0.2491 -0.0194 -0.0259 0.0124 113 VAL A N 784 C CA . VAL A 100 ? 0.2279 0.2040 0.2436 -0.0195 -0.0294 0.0104 113 VAL A CA 785 C C . VAL A 100 ? 0.2046 0.1790 0.2144 -0.0174 -0.0276 0.0070 113 VAL A C 786 O O . VAL A 100 ? 0.2181 0.1918 0.2269 -0.0166 -0.0265 0.0059 113 VAL A O 787 C CB . VAL A 100 ? 0.2243 0.1970 0.2410 -0.0210 -0.0331 0.0110 113 VAL A CB 788 C CG1 . VAL A 100 ? 0.2630 0.2304 0.2744 -0.0207 -0.0369 0.0084 113 VAL A CG1 789 C CG2 . VAL A 100 ? 0.2494 0.2246 0.2726 -0.0234 -0.0347 0.0146 113 VAL A CG2 790 N N . LEU A 101 ? 0.2167 0.1908 0.2228 -0.0165 -0.0273 0.0055 114 LEU A N 791 C CA . LEU A 101 ? 0.2422 0.2158 0.2433 -0.0147 -0.0252 0.0026 114 LEU A CA 792 C C . LEU A 101 ? 0.2399 0.2091 0.2364 -0.0138 -0.0278 0.0000 114 LEU A C 793 O O . LEU A 101 ? 0.2474 0.2133 0.2428 -0.0145 -0.0317 0.0000 114 LEU A O 794 C CB . LEU A 101 ? 0.2266 0.2012 0.2252 -0.0142 -0.0239 0.0023 114 LEU A CB 795 C CG . LEU A 101 ? 0.2300 0.2081 0.2325 -0.0148 -0.0216 0.0048 114 LEU A CG 796 C CD1 . LEU A 101 ? 0.2596 0.2378 0.2586 -0.0143 -0.0204 0.0043 114 LEU A CD1 797 C CD2 . LEU A 101 ? 0.2184 0.1994 0.2238 -0.0145 -0.0181 0.0051 114 LEU A CD2 798 N N . GLY A 102 ? 0.2347 0.2041 0.2287 -0.0122 -0.0259 -0.0022 115 GLY A N 799 C CA . GLY A 102 ? 0.2506 0.2162 0.2403 -0.0107 -0.0281 -0.0049 115 GLY A CA 800 C C . GLY A 102 ? 0.2565 0.2240 0.2438 -0.0087 -0.0251 -0.0073 115 GLY A C 801 O O . GLY A 102 ? 0.2367 0.2083 0.2253 -0.0086 -0.0215 -0.0070 115 GLY A O 802 N N . PRO A 103 ? 0.2635 0.2281 0.2477 -0.0070 -0.0267 -0.0097 116 PRO A N 803 C CA . PRO A 103 ? 0.2856 0.2523 0.2674 -0.0047 -0.0241 -0.0123 116 PRO A CA 804 C C . PRO A 103 ? 0.2741 0.2450 0.2599 -0.0050 -0.0207 -0.0113 116 PRO A C 805 O O . PRO A 103 ? 0.2813 0.2557 0.2662 -0.0039 -0.0178 -0.0129 116 PRO A O 806 C CB . PRO A 103 ? 0.3121 0.2741 0.2908 -0.0030 -0.0272 -0.0144 116 PRO A CB 807 C CG . PRO A 103 ? 0.3564 0.3134 0.3336 -0.0041 -0.0314 -0.0138 116 PRO A CG 808 C CD . PRO A 103 ? 0.2819 0.2407 0.2640 -0.0070 -0.0312 -0.0103 116 PRO A CD 809 N N . ALA A 104 ? 0.2215 0.1921 0.2115 -0.0066 -0.0211 -0.0087 117 ALA A N 810 C CA . ALA A 104 ? 0.2033 0.1774 0.1966 -0.0066 -0.0182 -0.0078 117 ALA A CA 811 C C . ALA A 104 ? 0.1772 0.1547 0.1744 -0.0082 -0.0159 -0.0052 117 ALA A C 812 O O . ALA A 104 ? 0.1940 0.1743 0.1936 -0.0081 -0.0134 -0.0046 117 ALA A O 813 C CB . ALA A 104 ? 0.1921 0.1637 0.1870 -0.0068 -0.0199 -0.0067 117 ALA A CB 814 N N . VAL A 105 ? 0.1741 0.1512 0.1717 -0.0095 -0.0169 -0.0039 118 VAL A N 815 C CA . VAL A 105 ? 0.1745 0.1544 0.1757 -0.0108 -0.0151 -0.0014 118 VAL A CA 816 C C . VAL A 105 ? 0.1976 0.1776 0.1965 -0.0110 -0.0150 -0.0017 118 VAL A C 817 O O . VAL A 105 ? 0.1939 0.1714 0.1911 -0.0114 -0.0177 -0.0016 118 VAL A O 818 C CB . VAL A 105 ? 0.1921 0.1714 0.1974 -0.0124 -0.0170 0.0016 118 VAL A CB 819 C CG1 . VAL A 105 ? 0.2134 0.1960 0.2225 -0.0132 -0.0151 0.0041 118 VAL A CG1 820 C CG2 . VAL A 105 ? 0.2017 0.1805 0.2087 -0.0122 -0.0171 0.0021 118 VAL A CG2 821 N N . GLY A 106 ? 0.1670 0.1498 0.1658 -0.0108 -0.0119 -0.0020 119 GLY A N 822 C CA . GLY A 106 ? 0.1588 0.1417 0.1550 -0.0110 -0.0114 -0.0022 119 GLY A CA 823 C C . GLY A 106 ? 0.1614 0.1469 0.1594 -0.0115 -0.0084 -0.0011 119 GLY A C 824 O O . GLY A 106 ? 0.1634 0.1506 0.1643 -0.0114 -0.0067 -0.0005 119 GLY A O 825 N N . LEU A 107 ? 0.1510 0.1362 0.1469 -0.0119 -0.0080 -0.0008 120 LEU A N 826 C CA . LEU A 107 ? 0.1625 0.1490 0.1594 -0.0124 -0.0056 0.0004 120 LEU A CA 827 C C . LEU A 107 ? 0.1617 0.1498 0.1564 -0.0123 -0.0029 -0.0012 120 LEU A C 828 O O . LEU A 107 ? 0.1817 0.1700 0.1732 -0.0118 -0.0029 -0.0032 120 LEU A O 829 C CB . LEU A 107 ? 0.1728 0.1578 0.1686 -0.0130 -0.0070 0.0021 120 LEU A CB 830 C CG . LEU A 107 ? 0.1751 0.1589 0.1731 -0.0133 -0.0101 0.0037 120 LEU A CG 831 C CD1 . LEU A 107 ? 0.1980 0.1806 0.1950 -0.0137 -0.0113 0.0053 120 LEU A CD1 832 C CD2 . LEU A 107 ? 0.1828 0.1684 0.1862 -0.0134 -0.0097 0.0054 120 LEU A CD2 833 N N . LEU A 108 ? 0.1510 0.1404 0.1475 -0.0128 -0.0006 -0.0005 121 LEU A N 834 C CA . LEU A 108 ? 0.1500 0.1407 0.1449 -0.0133 0.0018 -0.0016 121 LEU A CA 835 C C . LEU A 108 ? 0.1480 0.1374 0.1421 -0.0142 0.0025 0.0001 121 LEU A C 836 O O . LEU A 108 ? 0.1595 0.1479 0.1559 -0.0142 0.0020 0.0019 121 LEU A O 837 C CB . LEU A 108 ? 0.1579 0.1506 0.1555 -0.0130 0.0036 -0.0025 121 LEU A CB 838 C CG . LEU A 108 ? 0.1562 0.1506 0.1530 -0.0138 0.0060 -0.0036 121 LEU A CG 839 C CD1 . LEU A 108 ? 0.1653 0.1615 0.1594 -0.0138 0.0065 -0.0055 121 LEU A CD1 840 C CD2 . LEU A 108 ? 0.1719 0.1678 0.1715 -0.0134 0.0071 -0.0044 121 LEU A CD2 841 N N . ARG A 109 ? 0.1663 0.1556 0.1570 -0.0149 0.0035 -0.0002 122 ARG A N 842 C CA . ARG A 109 ? 0.1778 0.1653 0.1668 -0.0159 0.0041 0.0014 122 ARG A CA 843 C C . ARG A 109 ? 0.1644 0.1522 0.1550 -0.0168 0.0063 0.0017 122 ARG A C 844 O O . ARG A 109 ? 0.1662 0.1561 0.1574 -0.0173 0.0080 0.0002 122 ARG A O 845 C CB . ARG A 109 ? 0.2026 0.1898 0.1870 -0.0164 0.0044 0.0011 122 ARG A CB 846 C CG . ARG A 109 ? 0.2376 0.2234 0.2195 -0.0154 0.0018 0.0011 122 ARG A CG 847 C CD . ARG A 109 ? 0.2989 0.2817 0.2798 -0.0155 0.0000 0.0034 122 ARG A CD 848 N NE . ARG A 109 ? 0.3051 0.2866 0.2830 -0.0166 0.0015 0.0047 122 ARG A NE 849 C CZ . ARG A 109 ? 0.3207 0.3016 0.2937 -0.0169 0.0018 0.0047 122 ARG A CZ 850 N NH1 . ARG A 109 ? 0.3091 0.2906 0.2791 -0.0159 0.0007 0.0032 122 ARG A NH1 851 N NH2 . ARG A 109 ? 0.3001 0.2797 0.2708 -0.0181 0.0034 0.0063 122 ARG A NH2 852 N N . LEU A 110 ? 0.1604 0.1457 0.1514 -0.0171 0.0061 0.0037 123 LEU A N 853 C CA . LEU A 110 ? 0.1775 0.1617 0.1688 -0.0180 0.0079 0.0042 123 LEU A CA 854 C C . LEU A 110 ? 0.1869 0.1705 0.1748 -0.0198 0.0093 0.0044 123 LEU A C 855 O O . LEU A 110 ? 0.1919 0.1752 0.1765 -0.0200 0.0088 0.0048 123 LEU A O 856 C CB . LEU A 110 ? 0.1847 0.1660 0.1770 -0.0173 0.0070 0.0063 123 LEU A CB 857 C CG . LEU A 110 ? 0.1731 0.1554 0.1692 -0.0157 0.0060 0.0066 123 LEU A CG 858 C CD1 . LEU A 110 ? 0.1816 0.1617 0.1785 -0.0147 0.0049 0.0088 123 LEU A CD1 859 C CD2 . LEU A 110 ? 0.1977 0.1816 0.1962 -0.0154 0.0074 0.0052 123 LEU A CD2 860 N N . PRO A 111 ? 0.2020 0.1603 0.1617 -0.0312 0.0085 0.0063 124 PRO A N 861 C CA . PRO A 111 ? 0.2300 0.1836 0.1814 -0.0383 0.0078 0.0092 124 PRO A CA 862 C C . PRO A 111 ? 0.2752 0.2179 0.2216 -0.0372 0.0041 0.0139 124 PRO A C 863 O O . PRO A 111 ? 0.2616 0.1989 0.2112 -0.0306 0.0019 0.0143 124 PRO A O 864 C CB . PRO A 111 ? 0.2596 0.2070 0.2084 -0.0419 0.0085 0.0080 124 PRO A CB 865 C CG . PRO A 111 ? 0.2481 0.2022 0.2047 -0.0370 0.0103 0.0039 124 PRO A CG 866 C CD . PRO A 111 ? 0.2211 0.1764 0.1832 -0.0296 0.0091 0.0041 124 PRO A CD 867 N N . GLY A 112 A 0.3593 0.3001 0.2976 -0.0436 0.0032 0.0175 124 GLY A N 868 C CA . GLY A 112 A 0.4053 0.3354 0.3372 -0.0428 -0.0009 0.0231 124 GLY A CA 869 C C . GLY A 112 A 0.4204 0.3324 0.3488 -0.0400 -0.0041 0.0254 124 GLY A C 870 O O . GLY A 112 A 0.3740 0.2805 0.3023 -0.0420 -0.0026 0.0232 124 GLY A O 871 N N . ARG A 113 ? 0.4278 0.3309 0.3535 -0.0350 -0.0087 0.0295 125 ARG A N 872 C CA . ARG A 113 ? 0.4593 0.3436 0.3816 -0.0309 -0.0125 0.0315 125 ARG A CA 873 C C . ARG A 113 ? 0.5127 0.3809 0.4230 -0.0396 -0.0130 0.0354 125 ARG A C 874 O O . ARG A 113 ? 0.4860 0.3380 0.3941 -0.0377 -0.0148 0.0352 125 ARG A O 875 C CB . ARG A 113 ? 0.4500 0.3295 0.3715 -0.0231 -0.0181 0.0353 125 ARG A CB 876 C CG . ARG A 113 ? 0.4345 0.3261 0.3679 -0.0137 -0.0180 0.0303 125 ARG A CG 877 C CD . ARG A 113 ? 0.4289 0.3201 0.3609 -0.0074 -0.0233 0.0338 125 ARG A CD 878 N NE . ARG A 113 ? 0.4013 0.3054 0.3439 0.0006 -0.0233 0.0288 125 ARG A NE 879 C CZ . ARG A 113 ? 0.3896 0.2910 0.3384 0.0089 -0.0253 0.0249 125 ARG A CZ 880 N NH1 . ARG A 113 ? 0.4034 0.2884 0.3496 0.0111 -0.0275 0.0251 125 ARG A NH1 881 N NH2 . ARG A 113 ? 0.3688 0.2844 0.3264 0.0146 -0.0249 0.0201 125 ARG A NH2 882 N N . ARG A 114 ? 0.5598 0.4326 0.4623 -0.0498 -0.0113 0.0382 126 ARG A N 883 C CA . ARG A 114 ? 0.6831 0.5423 0.5729 -0.0605 -0.0110 0.0417 126 ARG A CA 884 C C . ARG A 114 ? 0.6490 0.5199 0.5402 -0.0696 -0.0051 0.0363 126 ARG A C 885 O O . ARG A 114 ? 0.6245 0.4869 0.5054 -0.0801 -0.0040 0.0380 126 ARG A O 886 C CB . ARG A 114 ? 0.7790 0.6341 0.6563 -0.0673 -0.0138 0.0493 126 ARG A CB 887 C CG . ARG A 114 ? 0.8530 0.6946 0.7264 -0.0589 -0.0206 0.0557 126 ARG A CG 888 C CD . ARG A 114 ? 1.0661 0.9052 0.9261 -0.0663 -0.0234 0.0639 126 ARG A CD 889 N NE . ARG A 114 ? 1.2448 1.0734 1.1016 -0.0572 -0.0304 0.0700 126 ARG A NE 890 C CZ . ARG A 114 ? 1.4212 1.2483 1.2672 -0.0607 -0.0343 0.0778 126 ARG A CZ 891 N NH1 . ARG A 114 ? 1.5606 1.3960 1.3976 -0.0741 -0.0315 0.0802 126 ARG A NH1 892 N NH2 . ARG A 114 ? 1.3732 1.1919 1.2174 -0.0508 -0.0412 0.0829 126 ARG A NH2 893 N N . ALA A 115 ? 0.5573 0.4473 0.4606 -0.0656 -0.0016 0.0299 127 ALA A N 894 C CA . ALA A 115 ? 0.5423 0.4467 0.4481 -0.0725 0.0034 0.0245 127 ALA A CA 895 C C . ALA A 115 ? 0.5410 0.4374 0.4463 -0.0752 0.0051 0.0212 127 ALA A C 896 O O . ALA A 115 ? 0.4786 0.3633 0.3870 -0.0683 0.0032 0.0206 127 ALA A O 897 C CB . ALA A 115 ? 0.5778 0.5028 0.4960 -0.0662 0.0059 0.0193 127 ALA A CB 898 N N . ARG A 116 ? 0.6282 0.5327 0.5295 -0.0855 0.0088 0.0184 128 ARG A N 899 C CA . ARG A 116 ? 0.6119 0.5141 0.5132 -0.0898 0.0114 0.0139 128 ARG A CA 900 C C . ARG A 116 ? 0.5689 0.4920 0.4828 -0.0844 0.0143 0.0070 128 ARG A C 901 O O . ARG A 116 ? 0.5455 0.4843 0.4660 -0.0799 0.0148 0.0059 128 ARG A O 902 C CB . ARG A 116 ? 0.7728 0.6759 0.6629 -0.1050 0.0141 0.0137 128 ARG A CB 903 C CG . ARG A 116 ? 0.9619 0.8435 0.8366 -0.1131 0.0114 0.0212 128 ARG A CG 904 C CD . ARG A 116 ? 1.0822 0.9392 0.9484 -0.1176 0.0107 0.0222 128 ARG A CD 905 N NE . ARG A 116 ? 1.1753 1.0354 1.0331 -0.1329 0.0150 0.0190 128 ARG A NE 906 C CZ . ARG A 116 ? 1.2872 1.1488 1.1475 -0.1363 0.0182 0.0126 128 ARG A CZ 907 N NH1 . ARG A 116 ? 1.4486 1.3089 1.3196 -0.1256 0.0177 0.0086 128 ARG A NH1 908 N NH2 . ARG A 116 ? 1.1417 1.0077 0.9934 -0.1515 0.0222 0.0097 128 ARG A NH2 909 N N . PRO A 117 ? 0.6738 0.5968 0.5905 -0.0850 0.0162 0.0025 129 PRO A N 910 C CA . PRO A 117 ? 0.5870 0.5310 0.5136 -0.0815 0.0188 -0.0034 129 PRO A CA 911 C C . PRO A 117 ? 0.5120 0.4755 0.4373 -0.0895 0.0218 -0.0065 129 PRO A C 912 O O . PRO A 117 ? 0.4306 0.3905 0.3462 -0.1005 0.0229 -0.0053 129 PRO A O 913 C CB . PRO A 117 ? 0.6507 0.5890 0.5782 -0.0826 0.0200 -0.0072 129 PRO A CB 914 C CG . PRO A 117 ? 0.6506 0.5673 0.5667 -0.0908 0.0193 -0.0045 129 PRO A CG 915 C CD . PRO A 117 ? 0.6916 0.5951 0.6029 -0.0878 0.0156 0.0024 129 PRO A CD 916 N N . PRO A 118 ? 0.3290 0.3129 0.2634 -0.0840 0.0231 -0.0106 130 PRO A N 917 C CA . PRO A 118 ? 0.3608 0.3654 0.2954 -0.0899 0.0255 -0.0146 130 PRO A CA 918 C C . PRO A 118 ? 0.4070 0.4191 0.3372 -0.1005 0.0285 -0.0193 130 PRO A C 919 O O . PRO A 118 ? 0.3979 0.4058 0.3293 -0.1003 0.0291 -0.0213 130 PRO A O 920 C CB . PRO A 118 ? 0.3780 0.3992 0.3240 -0.0791 0.0253 -0.0177 130 PRO A CB 921 C CG . PRO A 118 ? 0.3790 0.3901 0.3296 -0.0705 0.0237 -0.0163 130 PRO A CG 922 C CD . PRO A 118 ? 0.3618 0.3502 0.3064 -0.0721 0.0220 -0.0115 130 PRO A CD 923 N N . THR A 119 ? 0.3637 0.3884 0.2891 -0.1104 0.0307 -0.0218 131 THR A N 924 C CA . THR A 119 ? 0.4197 0.4531 0.3399 -0.1226 0.0340 -0.0268 131 THR A CA 925 C C . THR A 119 ? 0.3882 0.4447 0.3183 -0.1176 0.0354 -0.0340 131 THR A C 926 O O . THR A 119 ? 0.3234 0.3927 0.2632 -0.1064 0.0340 -0.0353 131 THR A O 927 C CB . THR A 119 ? 0.4866 0.5303 0.3987 -0.1355 0.0361 -0.0281 131 THR A CB 928 O OG1 . THR A 119 ? 0.5128 0.5816 0.4335 -0.1302 0.0364 -0.0325 131 THR A OG1 929 C CG2 . THR A 119 ? 0.5629 0.5838 0.4639 -0.1406 0.0342 -0.0200 131 THR A CG2 930 N N . ALA A 120 ? 0.3287 0.3897 0.2558 -0.1260 0.0379 -0.0385 132 ALA A N 931 C CA . ALA A 120 ? 0.2749 0.3604 0.2102 -0.1227 0.0392 -0.0455 132 ALA A CA 932 C C . ALA A 120 ? 0.2940 0.4072 0.2352 -0.1204 0.0396 -0.0503 132 ALA A C 933 O O . ALA A 120 ? 0.3270 0.4468 0.2627 -0.1297 0.0412 -0.0517 132 ALA A O 934 C CB . ALA A 120 ? 0.2780 0.3663 0.2075 -0.1352 0.0425 -0.0505 132 ALA A CB 935 N N . GLY A 121 ? 0.2805 0.4093 0.2324 -0.1079 0.0378 -0.0529 133 GLY A N 936 C CA . GLY A 121 ? 0.2822 0.4370 0.2414 -0.1025 0.0374 -0.0581 133 GLY A CA 937 C C . GLY A 121 ? 0.2402 0.3890 0.2041 -0.0914 0.0347 -0.0542 133 GLY A C 938 O O . GLY A 121 ? 0.2666 0.4338 0.2383 -0.0832 0.0335 -0.0584 133 GLY A O 939 N N . THR A 122 ? 0.2714 0.3948 0.2310 -0.0907 0.0335 -0.0468 134 THR A N 940 C CA . THR A 122 ? 0.2405 0.3572 0.2040 -0.0813 0.0312 -0.0433 134 THR A CA 941 C C . THR A 122 ? 0.2592 0.3819 0.2324 -0.0667 0.0288 -0.0440 134 THR A C 942 O O . THR A 122 ? 0.2175 0.3342 0.1922 -0.0625 0.0279 -0.0422 134 THR A O 943 C CB . THR A 122 ? 0.2618 0.3509 0.2195 -0.0820 0.0300 -0.0353 134 THR A CB 944 O OG1 . THR A 122 ? 0.3196 0.4017 0.2670 -0.0952 0.0316 -0.0337 134 THR A OG1 945 C CG2 . THR A 122 ? 0.2583 0.3422 0.2204 -0.0725 0.0279 -0.0322 134 THR A CG2 946 N N . ARG A 123 ? 0.2489 0.3836 0.2281 -0.0596 0.0278 -0.0468 135 ARG A N 947 C CA . ARG A 123 ? 0.2371 0.3754 0.2243 -0.0456 0.0252 -0.0470 135 ARG A CA 948 C C . ARG A 123 ? 0.2124 0.3280 0.1995 -0.0389 0.0234 -0.0400 135 ARG A C 949 O O . ARG A 123 ? 0.2123 0.3180 0.1972 -0.0406 0.0236 -0.0375 135 ARG A O 950 C CB . ARG A 123 ? 0.2902 0.4477 0.2838 -0.0401 0.0247 -0.0533 135 ARG A CB 951 C CG . ARG A 123 ? 0.3541 0.5391 0.3503 -0.0434 0.0258 -0.0617 135 ARG A CG 952 C CD . ARG A 123 ? 0.5268 0.7306 0.5313 -0.0341 0.0243 -0.0684 135 ARG A CD 953 N NE . ARG A 123 ? 0.6414 0.8734 0.6476 -0.0408 0.0264 -0.0778 135 ARG A NE 954 C CZ . ARG A 123 ? 0.7081 0.9469 0.7097 -0.0534 0.0296 -0.0808 135 ARG A CZ 955 N NH1 . ARG A 123 ? 0.7354 0.9540 0.7302 -0.0600 0.0307 -0.0747 135 ARG A NH1 956 N NH2 . ARG A 123 ? 0.7466 1.0137 0.7499 -0.0597 0.0316 -0.0902 135 ARG A NH2 957 N N . CYS A 124 ? 0.1811 0.2901 0.1701 -0.0321 0.0217 -0.0372 136 CYS A N 958 C CA . CYS A 124 ? 0.1738 0.2635 0.1627 -0.0263 0.0202 -0.0312 136 CYS A CA 959 C C . CYS A 124 ? 0.1801 0.2722 0.1736 -0.0153 0.0178 -0.0306 136 CYS A C 960 O O . CYS A 124 ? 0.1841 0.2918 0.1808 -0.0116 0.0169 -0.0342 136 CYS A O 961 C CB . CYS A 124 ? 0.1902 0.2656 0.1744 -0.0316 0.0208 -0.0275 136 CYS A CB 962 S SG . CYS A 124 ? 0.2310 0.2999 0.2076 -0.0449 0.0230 -0.0273 136 CYS A SG 963 N N . ARG A 125 ? 0.1613 0.2376 0.1546 -0.0104 0.0166 -0.0258 137 ARG A N 964 C CA . ARG A 125 ? 0.1808 0.2552 0.1762 -0.0011 0.0143 -0.0237 137 ARG A CA 965 C C . ARG A 125 ? 0.1465 0.2060 0.1391 -0.0015 0.0141 -0.0186 137 ARG A C 966 O O . ARG A 125 ? 0.1488 0.1969 0.1392 -0.0058 0.0152 -0.0166 137 ARG A O 967 C CB . ARG A 125 ? 0.1993 0.2712 0.1976 0.0061 0.0130 -0.0243 137 ARG A CB 968 C CG . ARG A 125 ? 0.2522 0.3102 0.2489 0.0036 0.0142 -0.0221 137 ARG A CG 969 C CD . ARG A 125 ? 0.3198 0.3779 0.3195 0.0088 0.0138 -0.0247 137 ARG A CD 970 N NE . ARG A 125 ? 0.3310 0.3737 0.3289 0.0081 0.0144 -0.0215 137 ARG A NE 971 C CZ . ARG A 125 ? 0.3319 0.3721 0.3314 0.0096 0.0150 -0.0236 137 ARG A CZ 972 N NH1 . ARG A 125 ? 0.3482 0.4000 0.3516 0.0125 0.0149 -0.0293 137 ARG A NH1 973 N NH2 . ARG A 125 ? 0.2819 0.3092 0.2793 0.0081 0.0157 -0.0207 137 ARG A NH2 974 N N . VAL A 126 ? 0.1454 0.2067 0.1380 0.0028 0.0125 -0.0168 138 VAL A N 975 C CA . VAL A 126 ? 0.1332 0.1829 0.1232 0.0025 0.0123 -0.0126 138 VAL A CA 976 C C . VAL A 126 ? 0.1434 0.1891 0.1326 0.0101 0.0099 -0.0093 138 VAL A C 977 O O . VAL A 126 ? 0.1525 0.2077 0.1426 0.0153 0.0078 -0.0098 138 VAL A O 978 C CB . VAL A 126 ? 0.1425 0.1974 0.1312 -0.0027 0.0133 -0.0137 138 VAL A CB 979 C CG1 . VAL A 126 ? 0.1427 0.2144 0.1326 -0.0007 0.0121 -0.0160 138 VAL A CG1 980 C CG2 . VAL A 126 ? 0.1484 0.1930 0.1350 -0.0032 0.0134 -0.0105 138 VAL A CG2 981 N N . ALA A 127 ? 0.1479 0.1794 0.1350 0.0105 0.0101 -0.0057 139 ALA A N 982 C CA . ALA A 127 ? 0.1466 0.1703 0.1312 0.0163 0.0080 -0.0019 139 ALA A CA 983 C C . ALA A 127 ? 0.1390 0.1561 0.1196 0.0135 0.0083 0.0017 139 ALA A C 984 O O . ALA A 127 ? 0.1526 0.1677 0.1334 0.0079 0.0103 0.0008 139 ALA A O 985 C CB . ALA A 127 ? 0.1679 0.1811 0.1529 0.0190 0.0082 -0.0017 139 ALA A CB 986 N N . GLY A 128 ? 0.1470 0.1604 0.1236 0.0175 0.0061 0.0057 140 GLY A N 987 C CA . GLY A 128 ? 0.1505 0.1585 0.1225 0.0140 0.0065 0.0093 140 GLY A CA 988 C C . GLY A 128 ? 0.1476 0.1520 0.1136 0.0182 0.0035 0.0145 140 GLY A C 989 O O . GLY A 128 ? 0.1673 0.1738 0.1332 0.0253 0.0005 0.0156 140 GLY A O 990 N N . TRP A 129 ? 0.1338 0.1373 0.1570 0.0074 -0.0179 -0.0128 141 TRP A N 991 C CA . TRP A 129 ? 0.1342 0.1352 0.1562 0.0089 -0.0192 -0.0123 141 TRP A CA 992 C C . TRP A 129 ? 0.1586 0.1604 0.1798 0.0067 -0.0177 -0.0118 141 TRP A C 993 O O . TRP A 129 ? 0.1694 0.1680 0.1896 0.0070 -0.0183 -0.0109 141 TRP A O 994 C CB . TRP A 129 ? 0.1430 0.1370 0.1651 0.0094 -0.0200 -0.0110 141 TRP A CB 995 C CG . TRP A 129 ? 0.1495 0.1416 0.1715 0.0116 -0.0218 -0.0116 141 TRP A CG 996 C CD1 . TRP A 129 ? 0.1533 0.1434 0.1732 0.0148 -0.0242 -0.0123 141 TRP A CD1 997 C CD2 . TRP A 129 ? 0.1476 0.1387 0.1712 0.0107 -0.0215 -0.0113 141 TRP A CD2 998 N NE1 . TRP A 129 ? 0.1456 0.1335 0.1655 0.0157 -0.0252 -0.0127 141 TRP A NE1 999 C CE2 . TRP A 129 ? 0.1522 0.1409 0.1744 0.0132 -0.0237 -0.0121 141 TRP A CE2 1000 C CE3 . TRP A 129 ? 0.1391 0.1308 0.1645 0.0083 -0.0197 -0.0106 141 TRP A CE3 1001 C CZ2 . TRP A 129 ? 0.1643 0.1519 0.1873 0.0128 -0.0240 -0.0121 141 TRP A CZ2 1002 C CZ3 . TRP A 129 ? 0.1413 0.1321 0.1677 0.0082 -0.0202 -0.0105 141 TRP A CZ3 1003 C CH2 . TRP A 129 ? 0.1413 0.1302 0.1666 0.0103 -0.0223 -0.0111 141 TRP A CH2 1004 N N . GLY A 130 ? 0.1458 0.1514 0.1669 0.0042 -0.0158 -0.0122 142 GLY A N 1005 C CA . GLY A 130 ? 0.1340 0.1405 0.1539 0.0016 -0.0142 -0.0119 142 GLY A CA 1006 C C . GLY A 130 ? 0.1469 0.1585 0.1654 0.0029 -0.0155 -0.0126 142 GLY A C 1007 O O . GLY A 130 ? 0.1703 0.1848 0.1889 0.0062 -0.0176 -0.0135 142 GLY A O 1008 N N . PHE A 131 ? 0.1363 0.1490 0.1532 0.0004 -0.0143 -0.0124 143 PHE A N 1009 C CA . PHE A 131 ? 0.1524 0.1700 0.1681 0.0015 -0.0156 -0.0128 143 PHE A CA 1010 C C . PHE A 131 ? 0.1515 0.1780 0.1674 0.0025 -0.0163 -0.0144 143 PHE A C 1011 O O . PHE A 131 ? 0.1578 0.1872 0.1741 0.0004 -0.0149 -0.0152 143 PHE A O 1012 C CB . PHE A 131 ? 0.1767 0.1944 0.1905 -0.0020 -0.0139 -0.0123 143 PHE A CB 1013 C CG . PHE A 131 ? 0.1919 0.2017 0.2053 -0.0030 -0.0131 -0.0108 143 PHE A CG 1014 C CD1 . PHE A 131 ? 0.2124 0.2178 0.2261 -0.0003 -0.0149 -0.0099 143 PHE A CD1 1015 C CD2 . PHE A 131 ? 0.1895 0.1966 0.2018 -0.0068 -0.0103 -0.0104 143 PHE A CD2 1016 C CE1 . PHE A 131 ? 0.2456 0.2446 0.2588 -0.0017 -0.0141 -0.0086 143 PHE A CE1 1017 C CE2 . PHE A 131 ? 0.2151 0.2158 0.2271 -0.0077 -0.0094 -0.0091 143 PHE A CE2 1018 C CZ . PHE A 131 ? 0.2334 0.2305 0.2461 -0.0053 -0.0112 -0.0082 143 PHE A CZ 1019 N N . VAL A 132 ? 0.1654 0.1966 0.1809 0.0056 -0.0184 -0.0148 144 VAL A N 1020 C CA . VAL A 132 ? 0.1747 0.2155 0.1906 0.0073 -0.0193 -0.0164 144 VAL A CA 1021 C C . VAL A 132 ? 0.1863 0.2353 0.2010 0.0051 -0.0189 -0.0167 144 VAL A C 1022 O O . VAL A 132 ? 0.2076 0.2661 0.2227 0.0063 -0.0197 -0.0180 144 VAL A O 1023 C CB . VAL A 132 ? 0.1724 0.2138 0.1888 0.0132 -0.0220 -0.0170 144 VAL A CB 1024 C CG1 . VAL A 132 ? 0.1764 0.2104 0.1937 0.0146 -0.0223 -0.0168 144 VAL A CG1 1025 C CG2 . VAL A 132 ? 0.1876 0.2266 0.2024 0.0158 -0.0238 -0.0160 144 VAL A CG2 1026 N N . SER A 133 ? 0.1768 0.2223 0.1899 0.0016 -0.0176 -0.0157 145 SER A N 1027 C CA . SER A 133 ? 0.1957 0.2482 0.2071 -0.0012 -0.0171 -0.0159 145 SER A CA 1028 C C . SER A 133 ? 0.1938 0.2402 0.2032 -0.0063 -0.0145 -0.0150 145 SER A C 1029 O O . SER A 133 ? 0.1896 0.2272 0.1993 -0.0069 -0.0134 -0.0142 145 SER A O 1030 C CB . SER A 133 ? 0.1891 0.2445 0.2000 0.0022 -0.0195 -0.0153 145 SER A CB 1031 O OG . SER A 133 ? 0.1940 0.2403 0.2038 0.0024 -0.0197 -0.0138 145 SER A OG 1032 N N . ASP A 134 ? 0.2050 0.2563 0.2122 -0.0100 -0.0137 -0.0151 147 ASP A N 1033 C CA . ASP A 134 ? 0.1968 0.2421 0.2014 -0.0144 -0.0114 -0.0143 147 ASP A CA 1034 C C . ASP A 134 ? 0.2025 0.2436 0.2063 -0.0132 -0.0124 -0.0130 147 ASP A C 1035 O O . ASP A 134 ? 0.2119 0.2499 0.2133 -0.0169 -0.0107 -0.0125 147 ASP A O 1036 C CB . ASP A 134 ? 0.2364 0.2878 0.2380 -0.0197 -0.0098 -0.0151 147 ASP A CB 1037 C CG . ASP A 134 ? 0.2234 0.2766 0.2246 -0.0223 -0.0082 -0.0162 147 ASP A CG 1038 O OD1 . ASP A 134 ? 0.2314 0.2766 0.2327 -0.0228 -0.0067 -0.0159 147 ASP A OD1 1039 O OD2 . ASP A 134 ? 0.2315 0.2943 0.2321 -0.0239 -0.0086 -0.0172 147 ASP A OD2 1040 N N . PHE A 135 ? 0.1969 0.2374 0.2024 -0.0081 -0.0150 -0.0125 148 PHE A N 1041 C CA . PHE A 135 ? 0.2175 0.2530 0.2219 -0.0068 -0.0162 -0.0111 148 PHE A CA 1042 C C . PHE A 135 ? 0.2174 0.2439 0.2231 -0.0041 -0.0168 -0.0103 148 PHE A C 1043 O O . PHE A 135 ? 0.2188 0.2417 0.2239 -0.0014 -0.0187 -0.0093 148 PHE A O 1044 C CB . PHE A 135 ? 0.2229 0.2657 0.2268 -0.0038 -0.0189 -0.0110 148 PHE A CB 1045 C CG . PHE A 135 ? 0.2350 0.2885 0.2381 -0.0064 -0.0185 -0.0120 148 PHE A CG 1046 C CD1 . PHE A 135 ? 0.2561 0.3188 0.2609 -0.0041 -0.0196 -0.0132 148 PHE A CD1 1047 C CD2 . PHE A 135 ? 0.2609 0.3153 0.2613 -0.0118 -0.0167 -0.0118 148 PHE A CD2 1048 C CE1 . PHE A 135 ? 0.3017 0.3751 0.3057 -0.0070 -0.0192 -0.0141 148 PHE A CE1 1049 C CE2 . PHE A 135 ? 0.2843 0.3487 0.2835 -0.0149 -0.0162 -0.0127 148 PHE A CE2 1050 C CZ . PHE A 135 ? 0.2952 0.3695 0.2964 -0.0126 -0.0175 -0.0138 148 PHE A CZ 1051 N N . GLU A 136 ? 0.1852 0.2079 0.1923 -0.0050 -0.0151 -0.0106 149 GLU A N 1052 C CA . GLU A 136 ? 0.1973 0.2119 0.2058 -0.0034 -0.0153 -0.0098 149 GLU A CA 1053 C C . GLU A 136 ? 0.2063 0.2199 0.2155 0.0015 -0.0183 -0.0097 149 GLU A C 1054 O O . GLU A 136 ? 0.2342 0.2409 0.2430 0.0027 -0.0191 -0.0086 149 GLU A O 1055 C CB . GLU A 136 ? 0.2221 0.2299 0.2292 -0.0060 -0.0137 -0.0086 149 GLU A CB 1056 C CG . GLU A 136 ? 0.2069 0.2145 0.2129 -0.0107 -0.0105 -0.0089 149 GLU A CG 1057 C CD . GLU A 136 ? 0.2547 0.2550 0.2600 -0.0128 -0.0085 -0.0078 149 GLU A CD 1058 O OE1 . GLU A 136 ? 0.2931 0.2896 0.2982 -0.0115 -0.0097 -0.0068 149 GLU A OE1 1059 O OE2 . GLU A 136 ? 0.2499 0.2483 0.2544 -0.0158 -0.0056 -0.0081 149 GLU A OE2 1060 N N . GLU A 137 ? 0.2230 0.2435 0.2329 0.0043 -0.0199 -0.0108 150 GLU A N 1061 C CA A GLU A 137 ? 0.2077 0.2269 0.2177 0.0095 -0.0226 -0.0110 150 GLU A CA 1062 C CA B GLU A 137 ? 0.2128 0.2322 0.2228 0.0095 -0.0226 -0.0110 150 GLU A CA 1063 C C . GLU A 137 ? 0.1927 0.2079 0.2045 0.0105 -0.0224 -0.0114 150 GLU A C 1064 O O . GLU A 137 ? 0.1982 0.2165 0.2116 0.0089 -0.0209 -0.0122 150 GLU A O 1065 C CB A GLU A 137 ? 0.2164 0.2450 0.2264 0.0126 -0.0243 -0.0121 150 GLU A CB 1066 C CB B GLU A 137 ? 0.2265 0.2556 0.2367 0.0125 -0.0242 -0.0122 150 GLU A CB 1067 C CG A GLU A 137 ? 0.2516 0.2846 0.2598 0.0125 -0.0252 -0.0115 150 GLU A CG 1068 C CG B GLU A 137 ? 0.2594 0.2876 0.2694 0.0184 -0.0269 -0.0127 150 GLU A CG 1069 C CD A GLU A 137 ? 0.2422 0.2869 0.2510 0.0145 -0.0262 -0.0128 150 GLU A CD 1070 C CD B GLU A 137 ? 0.2864 0.3254 0.2970 0.0217 -0.0282 -0.0140 150 GLU A CD 1071 O OE1 A GLU A 137 ? 0.3253 0.3722 0.3344 0.0198 -0.0284 -0.0134 150 GLU A OE1 1072 O OE1 B GLU A 137 ? 0.2986 0.3463 0.3099 0.0189 -0.0270 -0.0146 150 GLU A OE1 1073 O OE2 A GLU A 137 ? 0.1992 0.2511 0.2080 0.0107 -0.0248 -0.0132 150 GLU A OE2 1074 O OE2 B GLU A 137 ? 0.2497 0.2884 0.2598 0.0270 -0.0303 -0.0146 150 GLU A OE2 1075 N N . LEU A 138 ? 0.2081 0.2162 0.2192 0.0130 -0.0240 -0.0106 151 LEU A N 1076 C CA . LEU A 138 ? 0.2294 0.2332 0.2418 0.0139 -0.0241 -0.0109 151 LEU A CA 1077 C C . LEU A 138 ? 0.2115 0.2190 0.2241 0.0182 -0.0259 -0.0123 151 LEU A C 1078 O O . LEU A 138 ? 0.2295 0.2395 0.2404 0.0217 -0.0278 -0.0127 151 LEU A O 1079 C CB . LEU A 138 ? 0.2519 0.2463 0.2630 0.0140 -0.0249 -0.0094 151 LEU A CB 1080 C CG . LEU A 138 ? 0.3520 0.3426 0.3633 0.0098 -0.0228 -0.0081 151 LEU A CG 1081 C CD1 . LEU A 138 ? 0.4444 0.4269 0.4540 0.0099 -0.0239 -0.0067 151 LEU A CD1 1082 C CD2 . LEU A 138 ? 0.3917 0.3831 0.4058 0.0072 -0.0204 -0.0083 151 LEU A CD2 1083 N N . PRO A 139 ? 0.2037 0.2113 0.2180 0.0181 -0.0253 -0.0131 152 PRO A N 1084 C CA . PRO A 139 ? 0.1978 0.2082 0.2120 0.0222 -0.0269 -0.0146 152 PRO A CA 1085 C C . PRO A 139 ? 0.1977 0.1999 0.2096 0.0255 -0.0291 -0.0142 152 PRO A C 1086 O O . PRO A 139 ? 0.2109 0.2054 0.2220 0.0237 -0.0290 -0.0127 152 PRO A O 1087 C CB . PRO A 139 ? 0.2118 0.2240 0.2283 0.0200 -0.0253 -0.0153 152 PRO A CB 1088 C CG . PRO A 139 ? 0.2062 0.2120 0.2234 0.0164 -0.0238 -0.0137 152 PRO A CG 1089 C CD . PRO A 139 ? 0.2138 0.2185 0.2299 0.0146 -0.0232 -0.0126 152 PRO A CD 1090 N N . PRO A 140 ? 0.2220 0.2258 0.2327 0.0301 -0.0309 -0.0155 153 PRO A N 1091 C CA . PRO A 140 ? 0.2442 0.2390 0.2517 0.0332 -0.0329 -0.0153 153 PRO A CA 1092 C C . PRO A 140 ? 0.2424 0.2325 0.2506 0.0317 -0.0325 -0.0155 153 PRO A C 1093 O O . PRO A 140 ? 0.2799 0.2616 0.2853 0.0328 -0.0339 -0.0150 153 PRO A O 1094 C CB . PRO A 140 ? 0.2520 0.2509 0.2579 0.0389 -0.0347 -0.0169 153 PRO A CB 1095 C CG . PRO A 140 ? 0.2328 0.2433 0.2420 0.0382 -0.0333 -0.0183 153 PRO A CG 1096 C CD . PRO A 140 ? 0.2375 0.2511 0.2491 0.0328 -0.0311 -0.0173 153 PRO A CD 1097 N N . GLY A 141 ? 0.2133 0.2088 0.2248 0.0292 -0.0307 -0.0161 154 GLY A N 1098 C CA . GLY A 141 ? 0.1887 0.1810 0.2013 0.0274 -0.0301 -0.0161 154 GLY A CA 1099 C C . GLY A 141 ? 0.1844 0.1840 0.2003 0.0246 -0.0280 -0.0166 154 GLY A C 1100 O O . GLY A 141 ? 0.1868 0.1924 0.2038 0.0234 -0.0269 -0.0167 154 GLY A O 1101 N N . LEU A 142 ? 0.1599 0.1586 0.1770 0.0234 -0.0276 -0.0169 155 LEU A N 1102 C CA . LEU A 142 ? 0.1695 0.1741 0.1892 0.0207 -0.0257 -0.0173 155 LEU A CA 1103 C C . LEU A 142 ? 0.1757 0.1893 0.1956 0.0221 -0.0255 -0.0191 155 LEU A C 1104 O O . LEU A 142 ? 0.1695 0.1854 0.1883 0.0258 -0.0269 -0.0206 155 LEU A O 1105 C CB . LEU A 142 ? 0.1584 0.1606 0.1789 0.0197 -0.0256 -0.0173 155 LEU A CB 1106 C CG . LEU A 142 ? 0.1426 0.1491 0.1651 0.0168 -0.0238 -0.0174 155 LEU A CG 1107 C CD1 . LEU A 142 ? 0.1411 0.1466 0.1648 0.0132 -0.0218 -0.0157 155 LEU A CD1 1108 C CD2 . LEU A 142 ? 0.1625 0.1661 0.1853 0.0165 -0.0243 -0.0173 155 LEU A CD2 1109 N N . MET A 143 ? 0.1479 0.1668 0.1689 0.0192 -0.0237 -0.0189 156 MET A N 1110 C CA . MET A 143 ? 0.1574 0.1859 0.1787 0.0194 -0.0233 -0.0204 156 MET A CA 1111 C C . MET A 143 ? 0.1475 0.1797 0.1699 0.0160 -0.0215 -0.0209 156 MET A C 1112 O O . MET A 143 ? 0.1413 0.1689 0.1642 0.0129 -0.0203 -0.0196 156 MET A O 1113 C CB . MET A 143 ? 0.1607 0.1924 0.1816 0.0179 -0.0226 -0.0199 156 MET A CB 1114 C CG . MET A 143 ? 0.1592 0.1863 0.1787 0.0204 -0.0241 -0.0190 156 MET A CG 1115 S SD . MET A 143 ? 0.1929 0.2226 0.2109 0.0269 -0.0268 -0.0204 156 MET A SD 1116 C CE . MET A 143 ? 0.2110 0.2535 0.2297 0.0269 -0.0264 -0.0215 156 MET A CE 1117 N N . GLU A 144 ? 0.1666 0.2075 0.1890 0.0165 -0.0214 -0.0226 157 GLU A N 1118 C CA . GLU A 144 ? 0.1767 0.2217 0.1994 0.0128 -0.0198 -0.0231 157 GLU A CA 1119 C C . GLU A 144 ? 0.1841 0.2397 0.2064 0.0117 -0.0192 -0.0244 157 GLU A C 1120 O O . GLU A 144 ? 0.1793 0.2412 0.2017 0.0152 -0.0204 -0.0258 157 GLU A O 1121 C CB . GLU A 144 ? 0.1818 0.2258 0.2048 0.0142 -0.0204 -0.0239 157 GLU A CB 1122 C CG . GLU A 144 ? 0.1688 0.2158 0.1917 0.0105 -0.0189 -0.0242 157 GLU A CG 1123 C CD . GLU A 144 ? 0.1963 0.2415 0.2194 0.0118 -0.0197 -0.0248 157 GLU A CD 1124 O OE1 . GLU A 144 ? 0.2308 0.2820 0.2537 0.0140 -0.0204 -0.0268 157 GLU A OE1 1125 O OE2 . GLU A 144 ? 0.1943 0.2323 0.2178 0.0106 -0.0196 -0.0234 157 GLU A OE2 1126 N N . ALA A 145 ? 0.1575 0.2150 0.1791 0.0068 -0.0172 -0.0241 158 ALA A N 1127 C CA . ALA A 145 ? 0.1761 0.2437 0.1968 0.0044 -0.0164 -0.0253 158 ALA A CA 1128 C C . ALA A 145 ? 0.1753 0.2463 0.1954 0.0014 -0.0153 -0.0261 158 ALA A C 1129 O O . ALA A 145 ? 0.1780 0.2423 0.1976 -0.0005 -0.0145 -0.0252 158 ALA A O 1130 C CB . ALA A 145 ? 0.1515 0.2185 0.1708 0.0004 -0.0150 -0.0242 158 ALA A CB 1131 N N . LYS A 146 ? 0.1967 0.2787 0.2166 0.0011 -0.0153 -0.0279 159 LYS A N 1132 C CA . LYS A 146 ? 0.1908 0.2776 0.2094 -0.0024 -0.0142 -0.0288 159 LYS A CA 1133 C C . LYS A 146 ? 0.1460 0.2352 0.1619 -0.0085 -0.0123 -0.0284 159 LYS A C 1134 O O . LYS A 146 ? 0.1997 0.2952 0.2153 -0.0092 -0.0123 -0.0288 159 LYS A O 1135 C CB . LYS A 146 ? 0.2195 0.3177 0.2392 0.0003 -0.0151 -0.0311 159 LYS A CB 1136 C CG . LYS A 146 ? 0.2464 0.3424 0.2679 0.0065 -0.0169 -0.0319 159 LYS A CG 1137 C CD . LYS A 146 ? 0.2694 0.3773 0.2916 0.0093 -0.0174 -0.0344 159 LYS A CD 1138 C CE . LYS A 146 ? 0.4480 0.5541 0.4714 0.0164 -0.0193 -0.0352 159 LYS A CE 1139 N NZ . LYS A 146 ? 0.5473 0.6423 0.5704 0.0175 -0.0198 -0.0346 159 LYS A NZ 1140 N N . VAL A 147 ? 0.1731 0.2566 0.1868 -0.0129 -0.0108 -0.0275 160 VAL A N 1141 C CA . VAL A 147 ? 0.1728 0.2564 0.1828 -0.0192 -0.0089 -0.0271 160 VAL A CA 1142 C C . VAL A 147 ? 0.2119 0.2959 0.2192 -0.0233 -0.0078 -0.0274 160 VAL A C 1143 O O . VAL A 147 ? 0.2177 0.3009 0.2262 -0.0213 -0.0085 -0.0278 160 VAL A O 1144 C CB . VAL A 147 ? 0.1972 0.2696 0.2059 -0.0206 -0.0079 -0.0251 160 VAL A CB 1145 C CG1 . VAL A 147 ? 0.1869 0.2595 0.1978 -0.0172 -0.0089 -0.0248 160 VAL A CG1 1146 C CG2 . VAL A 147 ? 0.1785 0.2403 0.1879 -0.0192 -0.0078 -0.0237 160 VAL A CG2 1147 N N . ARG A 148 ? 0.2296 0.3148 0.2326 -0.0293 -0.0061 -0.0274 161 ARG A N 1148 C CA . ARG A 148 ? 0.2293 0.3142 0.2287 -0.0340 -0.0049 -0.0275 161 ARG A CA 1149 C C . ARG A 148 ? 0.2327 0.3068 0.2272 -0.0387 -0.0031 -0.0259 161 ARG A C 1150 O O . ARG A 148 ? 0.2127 0.2843 0.2058 -0.0402 -0.0023 -0.0253 161 ARG A O 1151 C CB . ARG A 148 ? 0.3043 0.4026 0.3020 -0.0375 -0.0047 -0.0294 161 ARG A CB 1152 C CG . ARG A 148 ? 0.4269 0.5362 0.4289 -0.0328 -0.0063 -0.0313 161 ARG A CG 1153 C CD . ARG A 148 ? 0.5248 0.6491 0.5261 -0.0354 -0.0061 -0.0331 161 ARG A CD 1154 N NE . ARG A 148 ? 0.6568 0.7919 0.6617 -0.0310 -0.0074 -0.0351 161 ARG A NE 1155 C CZ . ARG A 148 ? 0.7317 0.8725 0.7356 -0.0326 -0.0071 -0.0364 161 ARG A CZ 1156 N NH1 . ARG A 148 ? 0.7379 0.8746 0.7373 -0.0389 -0.0057 -0.0358 161 ARG A NH1 1157 N NH2 . ARG A 148 ? 0.7715 0.9219 0.7788 -0.0279 -0.0082 -0.0383 161 ARG A NH2 1158 N N . VAL A 149 ? 0.1899 0.2572 0.1819 -0.0406 -0.0024 -0.0250 162 VAL A N 1159 C CA . VAL A 149 ? 0.2036 0.2600 0.1903 -0.0447 -0.0006 -0.0234 162 VAL A CA 1160 C C . VAL A 149 ? 0.2232 0.2836 0.2043 -0.0513 0.0009 -0.0242 162 VAL A C 1161 O O . VAL A 149 ? 0.2259 0.2962 0.2056 -0.0542 0.0007 -0.0257 162 VAL A O 1162 C CB . VAL A 149 ? 0.2387 0.2882 0.2234 -0.0455 -0.0004 -0.0224 162 VAL A CB 1163 C CG1 . VAL A 149 ? 0.2482 0.2865 0.2264 -0.0498 0.0015 -0.0209 162 VAL A CG1 1164 C CG2 . VAL A 149 ? 0.2137 0.2587 0.2037 -0.0394 -0.0018 -0.0215 162 VAL A CG2 1165 N N . LEU A 150 ? 0.2200 0.2728 0.1975 -0.0537 0.0023 -0.0232 163 LEU A N 1166 C CA . LEU A 150 ? 0.2174 0.2726 0.1889 -0.0602 0.0039 -0.0238 163 LEU A CA 1167 C C . LEU A 150 ? 0.2189 0.2633 0.1828 -0.0653 0.0057 -0.0228 163 LEU A C 1168 O O . LEU A 150 ? 0.2249 0.2574 0.1882 -0.0631 0.0062 -0.0212 163 LEU A O 1169 C CB . LEU A 150 ? 0.2283 0.2808 0.2001 -0.0596 0.0044 -0.0234 163 LEU A CB 1170 C CG . LEU A 150 ? 0.2400 0.2944 0.2056 -0.0662 0.0059 -0.0240 163 LEU A CG 1171 C CD1 . LEU A 150 ? 0.2580 0.3281 0.2238 -0.0693 0.0052 -0.0258 163 LEU A CD1 1172 C CD2 . LEU A 150 ? 0.2336 0.2842 0.2004 -0.0645 0.0063 -0.0234 163 LEU A CD2 1173 N N . ASP A 151 ? 0.2351 0.2837 0.1929 -0.0720 0.0066 -0.0237 164 ASP A N 1174 C CA . ASP A 151 ? 0.2701 0.3079 0.2190 -0.0777 0.0085 -0.0228 164 ASP A CA 1175 C C . ASP A 151 ? 0.2619 0.2852 0.2076 -0.0770 0.0100 -0.0212 164 ASP A C 1176 O O . ASP A 151 ? 0.2260 0.2501 0.1716 -0.0777 0.0106 -0.0215 164 ASP A O 1177 C CB . ASP A 151 ? 0.2888 0.3342 0.2312 -0.0858 0.0094 -0.0242 164 ASP A CB 1178 C CG . ASP A 151 ? 0.3638 0.3980 0.2956 -0.0926 0.0114 -0.0234 164 ASP A CG 1179 O OD1 . ASP A 151 ? 0.3410 0.3606 0.2687 -0.0922 0.0126 -0.0219 164 ASP A OD1 1180 O OD2 . ASP A 151 ? 0.4706 0.5110 0.3975 -0.0988 0.0117 -0.0244 164 ASP A OD2 1181 N N . PRO A 152 ? 0.2490 0.2596 0.1923 -0.0755 0.0107 -0.0195 165 PRO A N 1182 C CA . PRO A 152 ? 0.2688 0.2663 0.2097 -0.0740 0.0122 -0.0181 165 PRO A CA 1183 C C . PRO A 152 ? 0.2760 0.2676 0.2077 -0.0806 0.0144 -0.0184 165 PRO A C 1184 O O . PRO A 152 ? 0.2823 0.2667 0.2130 -0.0794 0.0156 -0.0179 165 PRO A O 1185 C CB . PRO A 152 ? 0.2948 0.2812 0.2342 -0.0716 0.0123 -0.0163 165 PRO A CB 1186 C CG . PRO A 152 ? 0.2907 0.2817 0.2276 -0.0749 0.0116 -0.0168 165 PRO A CG 1187 C CD . PRO A 152 ? 0.2363 0.2437 0.1789 -0.0749 0.0100 -0.0188 165 PRO A CD 1188 N N . ASP A 153 ? 0.2609 0.2553 0.1856 -0.0876 0.0151 -0.0193 166 ASP A N 1189 C CA . ASP A 153 ? 0.2626 0.2518 0.1777 -0.0946 0.0172 -0.0198 166 ASP A CA 1190 C C . ASP A 153 ? 0.2730 0.2730 0.1909 -0.0960 0.0169 -0.0212 166 ASP A C 1191 O O . ASP A 153 ? 0.2915 0.2853 0.2051 -0.0982 0.0185 -0.0211 166 ASP A O 1192 C CB . ASP A 153 ? 0.3017 0.2905 0.2078 -0.1024 0.0179 -0.0202 166 ASP A CB 1193 C CG . ASP A 153 ? 0.4253 0.4011 0.3266 -0.1018 0.0184 -0.0186 166 ASP A CG 1194 O OD1 . ASP A 153 ? 0.4386 0.4004 0.3377 -0.0986 0.0196 -0.0172 166 ASP A OD1 1195 O OD2 . ASP A 153 ? 0.4352 0.4149 0.3347 -0.1043 0.0177 -0.0188 166 ASP A OD2 1196 N N . VAL A 154 ? 0.2535 0.2694 0.1785 -0.0945 0.0150 -0.0224 167 VAL A N 1197 C CA . VAL A 154 ? 0.2366 0.2642 0.1656 -0.0945 0.0143 -0.0235 167 VAL A CA 1198 C C . VAL A 154 ? 0.2526 0.2749 0.1870 -0.0882 0.0141 -0.0226 167 VAL A C 1199 O O . VAL A 154 ? 0.3043 0.3260 0.2369 -0.0900 0.0149 -0.0228 167 VAL A O 1200 C CB . VAL A 154 ? 0.2796 0.3247 0.2157 -0.0925 0.0121 -0.0248 167 VAL A CB 1201 C CG1 . VAL A 154 ? 0.3381 0.3950 0.2788 -0.0914 0.0112 -0.0258 167 VAL A CG1 1202 C CG2 . VAL A 154 ? 0.2908 0.3424 0.2215 -0.0993 0.0124 -0.0258 167 VAL A CG2 1203 N N . CYS A 155 ? 0.2402 0.2587 0.1809 -0.0812 0.0131 -0.0216 168 CYS A N 1204 C CA . CYS A 155 ? 0.2329 0.2462 0.1785 -0.0755 0.0129 -0.0207 168 CYS A CA 1205 C C . CYS A 155 ? 0.2604 0.2598 0.1993 -0.0778 0.0154 -0.0199 168 CYS A C 1206 O O . CYS A 155 ? 0.2572 0.2554 0.1969 -0.0770 0.0159 -0.0198 168 CYS A O 1207 C CB . CYS A 155 ? 0.2110 0.2216 0.1633 -0.0686 0.0115 -0.0197 168 CYS A CB 1208 S SG . CYS A 155 ? 0.2316 0.2385 0.1907 -0.0618 0.0110 -0.0187 168 CYS A SG 1209 N N . ASN A 156 ? 0.2674 0.2557 0.1994 -0.0804 0.0169 -0.0191 169 ASN A N 1210 C CA . ASN A 156 ? 0.2797 0.2537 0.2044 -0.0822 0.0194 -0.0183 169 ASN A CA 1211 C C . ASN A 156 ? 0.3239 0.2988 0.2418 -0.0888 0.0209 -0.0195 169 ASN A C 1212 O O . ASN A 156 ? 0.3148 0.2826 0.2306 -0.0885 0.0224 -0.0192 169 ASN A O 1213 C CB . ASN A 156 ? 0.3107 0.2727 0.2285 -0.0838 0.0206 -0.0173 169 ASN A CB 1214 C CG . ASN A 156 ? 0.3467 0.2928 0.2577 -0.0838 0.0232 -0.0163 169 ASN A CG 1215 O OD1 . ASN A 156 ? 0.3230 0.2660 0.2372 -0.0802 0.0238 -0.0160 169 ASN A OD1 1216 N ND2 . ASN A 156 ? 0.3868 0.3222 0.2882 -0.0878 0.0247 -0.0159 169 ASN A ND2 1217 N N . SER A 157 ? 0.2964 0.2806 0.2109 -0.0949 0.0205 -0.0207 170 SER A N 1218 C CA . SER A 157 ? 0.3297 0.3164 0.2381 -0.1016 0.0218 -0.0218 170 SER A CA 1219 C C . SER A 157 ? 0.3699 0.3654 0.2853 -0.0984 0.0207 -0.0222 170 SER A C 1220 O O . SER A 157 ? 0.3369 0.3276 0.2483 -0.1007 0.0222 -0.0223 170 SER A O 1221 C CB . SER A 157 ? 0.4543 0.4503 0.3577 -0.1091 0.0215 -0.0230 170 SER A CB 1222 O OG . SER A 157 ? 0.5044 0.5155 0.4159 -0.1063 0.0191 -0.0236 170 SER A OG 1223 N N . SER A 158 ? 0.3055 0.3130 0.2309 -0.0929 0.0182 -0.0224 171 SER A N 1224 C CA . SER A 158 ? 0.3415 0.3565 0.2736 -0.0892 0.0169 -0.0225 171 SER A CA 1225 C C . SER A 158 ? 0.3544 0.3577 0.2877 -0.0850 0.0180 -0.0214 171 SER A C 1226 O O . SER A 158 ? 0.3569 0.3617 0.2909 -0.0849 0.0181 -0.0215 171 SER A O 1227 C CB . SER A 158 ? 0.3329 0.3605 0.2750 -0.0833 0.0141 -0.0228 171 SER A CB 1228 O OG . SER A 158 ? 0.3800 0.4206 0.3218 -0.0869 0.0130 -0.0240 171 SER A OG 1229 N N . TRP A 159 ? 0.2966 0.2886 0.2297 -0.0816 0.0188 -0.0203 172 TRP A N 1230 C CA . TRP A 159 ? 0.3213 0.3017 0.2547 -0.0779 0.0202 -0.0192 172 TRP A CA 1231 C C . TRP A 159 ? 0.3197 0.2869 0.2429 -0.0826 0.0232 -0.0191 172 TRP A C 1232 O O . TRP A 159 ? 0.3367 0.2923 0.2588 -0.0795 0.0248 -0.0182 172 TRP A O 1233 C CB . TRP A 159 ? 0.2691 0.2450 0.2082 -0.0713 0.0193 -0.0179 172 TRP A CB 1234 C CG . TRP A 159 ? 0.2382 0.2234 0.1875 -0.0654 0.0168 -0.0178 172 TRP A CG 1235 C CD1 . TRP A 159 ? 0.2117 0.2069 0.1670 -0.0628 0.0143 -0.0181 172 TRP A CD1 1236 C CD2 . TRP A 159 ? 0.2345 0.2197 0.1886 -0.0615 0.0164 -0.0174 172 TRP A CD2 1237 N NE1 . TRP A 159 ? 0.1986 0.1993 0.1616 -0.0576 0.0125 -0.0179 172 TRP A NE1 1238 C CE2 . TRP A 159 ? 0.2198 0.2148 0.1824 -0.0567 0.0136 -0.0174 172 TRP A CE2 1239 C CE3 . TRP A 159 ? 0.2434 0.2214 0.1952 -0.0616 0.0182 -0.0170 172 TRP A CE3 1240 C CZ2 . TRP A 159 ? 0.2223 0.2192 0.1905 -0.0524 0.0125 -0.0170 172 TRP A CZ2 1241 C CZ3 . TRP A 159 ? 0.2673 0.2479 0.2252 -0.0573 0.0171 -0.0166 172 TRP A CZ3 1242 C CH2 . TRP A 159 ? 0.2597 0.2494 0.2255 -0.0530 0.0143 -0.0165 172 TRP A CH2 1243 N N . LYS A 160 ? 0.3507 0.3196 0.2660 -0.0902 0.0242 -0.0202 173 LYS A N 1244 C CA . LYS A 160 ? 0.3659 0.3224 0.2699 -0.0958 0.0272 -0.0204 173 LYS A CA 1245 C C . LYS A 160 ? 0.3532 0.2938 0.2522 -0.0940 0.0290 -0.0193 173 LYS A C 1246 O O . LYS A 160 ? 0.4503 0.3781 0.3430 -0.0946 0.0315 -0.0191 173 LYS A O 1247 C CB . LYS A 160 ? 0.3833 0.3376 0.2871 -0.0956 0.0283 -0.0207 173 LYS A CB 1248 C CG . LYS A 160 ? 0.5164 0.4856 0.4269 -0.0952 0.0262 -0.0213 173 LYS A CG 1249 C CD . LYS A 160 ? 0.5640 0.5454 0.4719 -0.1016 0.0252 -0.0225 173 LYS A CD 1250 C CE . LYS A 160 ? 0.6171 0.6076 0.5257 -0.1041 0.0246 -0.0232 173 LYS A CE 1251 N NZ . LYS A 160 ? 0.5933 0.5899 0.5118 -0.0972 0.0227 -0.0226 173 LYS A NZ 1252 N N . GLY A 161 ? 0.3537 0.2954 0.2557 -0.0914 0.0277 -0.0186 174 GLY A N 1253 C CA . GLY A 161 ? 0.3802 0.3079 0.2769 -0.0901 0.0291 -0.0175 174 GLY A CA 1254 C C . GLY A 161 ? 0.4140 0.3347 0.3165 -0.0820 0.0292 -0.0160 174 GLY A C 1255 O O . GLY A 161 ? 0.4240 0.3326 0.3218 -0.0805 0.0305 -0.0149 174 GLY A O 1256 N N . HIS A 162 ? 0.4426 0.3713 0.3552 -0.0767 0.0277 -0.0158 175 HIS A N 1257 C CA . HIS A 162 ? 0.4856 0.4086 0.4038 -0.0695 0.0279 -0.0145 175 HIS A CA 1258 C C . HIS A 162 ? 0.4807 0.4076 0.4069 -0.0638 0.0258 -0.0133 175 HIS A C 1259 O O . HIS A 162 ? 0.5533 0.4769 0.4847 -0.0579 0.0257 -0.0121 175 HIS A O 1260 C CB . HIS A 162 ? 0.5991 0.5268 0.5226 -0.0673 0.0278 -0.0149 175 HIS A CB 1261 C CG . HIS A 162 ? 0.6977 0.6167 0.6135 -0.0707 0.0307 -0.0155 175 HIS A CG 1262 N ND1 . HIS A 162 ? 0.7147 0.6379 0.6260 -0.0767 0.0311 -0.0168 175 HIS A ND1 1263 C CD2 . HIS A 162 ? 0.8844 0.7904 0.7959 -0.0687 0.0334 -0.0149 175 HIS A CD2 1264 C CE1 . HIS A 162 ? 0.8365 0.7494 0.7407 -0.0787 0.0339 -0.0171 175 HIS A CE1 1265 N NE2 . HIS A 162 ? 0.8994 0.8017 0.8037 -0.0736 0.0354 -0.0160 175 HIS A NE2 1266 N N . LEU A 163 ? 0.3933 0.3272 0.3204 -0.0656 0.0240 -0.0136 176 LEU A N 1267 C CA . LEU A 163 ? 0.3524 0.2905 0.2869 -0.0606 0.0218 -0.0126 176 LEU A CA 1268 C C . LEU A 163 ? 0.3979 0.3251 0.3281 -0.0593 0.0227 -0.0112 176 LEU A C 1269 O O . LEU A 163 ? 0.3796 0.2981 0.3000 -0.0638 0.0244 -0.0112 176 LEU A O 1270 C CB . LEU A 163 ? 0.3750 0.3259 0.3126 -0.0628 0.0195 -0.0137 176 LEU A CB 1271 C CG . LEU A 163 ? 0.5220 0.4858 0.4685 -0.0600 0.0173 -0.0145 176 LEU A CG 1272 C CD1 . LEU A 163 ? 0.5530 0.5177 0.4996 -0.0607 0.0181 -0.0151 176 LEU A CD1 1273 C CD2 . LEU A 163 ? 0.4741 0.4495 0.4211 -0.0632 0.0156 -0.0158 176 LEU A CD2 1274 N N . THR A 164 ? 0.3319 0.2595 0.2689 -0.0534 0.0213 -0.0098 177 THR A N 1275 C CA . THR A 164 ? 0.3337 0.2524 0.2677 -0.0514 0.0217 -0.0082 177 THR A CA 1276 C C . THR A 164 ? 0.3229 0.2485 0.2600 -0.0514 0.0193 -0.0080 177 THR A C 1277 O O . THR A 164 ? 0.3267 0.2640 0.2690 -0.0521 0.0174 -0.0092 177 THR A O 1278 C CB . THR A 164 ? 0.3447 0.2582 0.2836 -0.0447 0.0221 -0.0065 177 THR A CB 1279 O OG1 . THR A 164 ? 0.3187 0.2416 0.2678 -0.0403 0.0195 -0.0061 177 THR A OG1 1280 C CG2 . THR A 164 ? 0.3709 0.2808 0.3092 -0.0441 0.0241 -0.0069 177 THR A CG2 1281 N N . LEU A 165 ? 0.3280 0.2464 0.2619 -0.0503 0.0194 -0.0065 178 LEU A N 1282 C CA . LEU A 165 ? 0.3327 0.2564 0.2685 -0.0507 0.0173 -0.0062 178 LEU A CA 1283 C C . LEU A 165 ? 0.3145 0.2475 0.2611 -0.0454 0.0148 -0.0059 178 LEU A C 1284 O O . LEU A 165 ? 0.3438 0.2840 0.2929 -0.0461 0.0130 -0.0063 178 LEU A O 1285 C CB . LEU A 165 ? 0.4051 0.3177 0.3342 -0.0506 0.0180 -0.0044 178 LEU A CB 1286 C CG . LEU A 165 ? 0.4589 0.3634 0.3758 -0.0573 0.0198 -0.0049 178 LEU A CG 1287 C CD1 . LEU A 165 ? 0.5439 0.4349 0.4539 -0.0561 0.0207 -0.0028 178 LEU A CD1 1288 C CD2 . LEU A 165 ? 0.5034 0.4176 0.4191 -0.0629 0.0185 -0.0064 178 LEU A CD2 1289 N N . THR A 166 ? 0.2856 0.2182 0.2382 -0.0405 0.0148 -0.0052 179 THR A N 1290 C CA . THR A 166 ? 0.2650 0.2052 0.2273 -0.0356 0.0125 -0.0047 179 THR A CA 1291 C C . THR A 166 ? 0.2363 0.1861 0.2044 -0.0353 0.0115 -0.0063 179 THR A C 1292 O O . THR A 166 ? 0.2289 0.1827 0.2043 -0.0310 0.0102 -0.0059 179 THR A O 1293 C CB . THR A 166 ? 0.2663 0.2003 0.2316 -0.0302 0.0129 -0.0026 179 THR A CB 1294 O OG1 . THR A 166 ? 0.2754 0.2049 0.2398 -0.0294 0.0149 -0.0027 179 THR A OG1 1295 C CG2 . THR A 166 ? 0.2805 0.2056 0.2404 -0.0299 0.0135 -0.0009 179 THR A CG2 1296 N N . MET A 167 ? 0.2560 0.2095 0.2204 -0.0398 0.0121 -0.0081 180 MET A N 1297 C CA . MET A 167 ? 0.2327 0.1957 0.2016 -0.0400 0.0111 -0.0096 180 MET A CA 1298 C C . MET A 167 ? 0.2708 0.2431 0.2393 -0.0430 0.0097 -0.0111 180 MET A C 1299 O O . MET A 167 ? 0.3094 0.2799 0.2717 -0.0474 0.0105 -0.0114 180 MET A O 1300 C CB . MET A 167 ? 0.2651 0.2253 0.2301 -0.0426 0.0130 -0.0103 180 MET A CB 1301 C CG . MET A 167 ? 0.2684 0.2208 0.2345 -0.0392 0.0144 -0.0091 180 MET A CG 1302 S SD . MET A 167 ? 0.2703 0.2176 0.2301 -0.0429 0.0171 -0.0099 180 MET A SD 1303 C CE . MET A 167 ? 0.3099 0.2480 0.2717 -0.0377 0.0187 -0.0082 180 MET A CE 1304 N N . LEU A 168 ? 0.2353 0.2174 0.2103 -0.0407 0.0077 -0.0121 181 LEU A N 1305 C CA . LEU A 168 ? 0.2366 0.2288 0.2115 -0.0434 0.0066 -0.0138 181 LEU A CA 1306 C C . LEU A 168 ? 0.2213 0.2224 0.2002 -0.0424 0.0056 -0.0152 181 LEU A C 1307 O O . LEU A 168 ? 0.2383 0.2387 0.2216 -0.0386 0.0051 -0.0147 181 LEU A O 1308 C CB . LEU A 168 ? 0.3749 0.3709 0.3526 -0.0417 0.0048 -0.0138 181 LEU A CB 1309 C CG . LEU A 168 ? 0.3327 0.3334 0.3182 -0.0363 0.0026 -0.0137 181 LEU A CG 1310 C CD1 . LEU A 168 ? 0.3268 0.3385 0.3156 -0.0357 0.0013 -0.0157 181 LEU A CD1 1311 C CD2 . LEU A 168 ? 0.3310 0.3314 0.3176 -0.0349 0.0014 -0.0131 181 LEU A CD2 1312 N N . CYS A 169 ? 0.1899 0.1996 0.1668 -0.0460 0.0054 -0.0168 182 CYS A N 1313 C CA . CYS A 169 ? 0.2024 0.2205 0.1816 -0.0459 0.0048 -0.0181 182 CYS A CA 1314 C C . CYS A 169 ? 0.1903 0.2206 0.1735 -0.0445 0.0028 -0.0196 182 CYS A C 1315 O O . CYS A 169 ? 0.2063 0.2397 0.1889 -0.0455 0.0023 -0.0200 182 CYS A O 1316 C CB . CYS A 169 ? 0.2142 0.2324 0.1868 -0.0521 0.0066 -0.0187 182 CYS A CB 1317 S SG . CYS A 169 ? 0.2392 0.2423 0.2055 -0.0542 0.0093 -0.0173 182 CYS A SG 1318 N N . THR A 170 ? 0.1624 0.1998 0.1492 -0.0422 0.0017 -0.0204 183 THR A N 1319 C CA . THR A 170 ? 0.1719 0.2216 0.1622 -0.0405 0.0000 -0.0220 183 THR A CA 1320 C C . THR A 170 ? 0.1991 0.2580 0.1885 -0.0428 0.0000 -0.0231 183 THR A C 1321 O O . THR A 170 ? 0.1936 0.2493 0.1804 -0.0452 0.0011 -0.0227 183 THR A O 1322 C CB . THR A 170 ? 0.1727 0.2234 0.1695 -0.0338 -0.0021 -0.0218 183 THR A CB 1323 O OG1 . THR A 170 ? 0.1621 0.2103 0.1609 -0.0313 -0.0024 -0.0212 183 THR A OG1 1324 C CG2 . THR A 170 ? 0.1820 0.2244 0.1800 -0.0316 -0.0023 -0.0206 183 THR A CG2 1325 N N . ARG A 171 ? 0.2140 0.2851 0.2056 -0.0420 -0.0013 -0.0247 184 ARG A N 1326 C CA . ARG A 171 ? 0.2317 0.3140 0.2242 -0.0424 -0.0019 -0.0259 184 ARG A CA 1327 C C . ARG A 171 ? 0.1975 0.2893 0.1955 -0.0366 -0.0042 -0.0270 184 ARG A C 1328 O O . ARG A 171 ? 0.1925 0.2834 0.1928 -0.0336 -0.0050 -0.0273 184 ARG A O 1329 C CB . ARG A 171 ? 0.2545 0.3442 0.2420 -0.0494 -0.0007 -0.0269 184 ARG A CB 1330 C CG . ARG A 171 ? 0.3057 0.4011 0.2924 -0.0509 -0.0008 -0.0280 184 ARG A CG 1331 C CD . ARG A 171 ? 0.4100 0.5167 0.3929 -0.0572 0.0000 -0.0293 184 ARG A CD 1332 N NE . ARG A 171 ? 0.5118 0.6264 0.4954 -0.0576 -0.0005 -0.0306 184 ARG A NE 1333 C CZ . ARG A 171 ? 0.5990 0.7273 0.5870 -0.0541 -0.0019 -0.0322 184 ARG A CZ 1334 N NH1 . ARG A 171 ? 0.6738 0.8098 0.6660 -0.0499 -0.0033 -0.0327 184 ARG A NH1 1335 N NH2 . ARG A 171 ? 0.6629 0.7974 0.6510 -0.0549 -0.0021 -0.0334 184 ARG A NH2 1336 N N . SER A 172 ? 0.2163 0.3168 0.2163 -0.0347 -0.0052 -0.0277 185 SER A N 1337 C CA . SER A 172 ? 0.2326 0.3436 0.2371 -0.0293 -0.0073 -0.0290 185 SER A CA 1338 C C . SER A 172 ? 0.2680 0.3901 0.2718 -0.0316 -0.0071 -0.0307 185 SER A C 1339 O O . SER A 172 ? 0.2867 0.4123 0.2864 -0.0381 -0.0056 -0.0310 185 SER A O 1340 C CB . SER A 172 ? 0.2394 0.3578 0.2455 -0.0274 -0.0083 -0.0292 185 SER A CB 1341 O OG . SER A 172 ? 0.2390 0.3673 0.2490 -0.0217 -0.0103 -0.0304 185 SER A OG 1342 N N . GLY A 173 ? 0.2922 0.4199 0.2997 -0.0264 -0.0086 -0.0319 186 GLY A N 1343 C CA . GLY A 173 ? 0.3345 0.4745 0.3420 -0.0277 -0.0085 -0.0337 186 GLY A CA 1344 C C . GLY A 173 ? 0.3701 0.5256 0.3783 -0.0282 -0.0090 -0.0350 186 GLY A C 1345 O O . GLY A 173 ? 0.3900 0.5573 0.3976 -0.0307 -0.0086 -0.0366 186 GLY A O 1346 N N . ASP A 174 A 0.3067 0.4629 0.3162 -0.0259 -0.0098 -0.0343 186 ASP A N 1347 C CA . ASP A 174 A 0.3280 0.4991 0.3385 -0.0258 -0.0105 -0.0353 186 ASP A CA 1348 C C . ASP A 174 A 0.3251 0.4937 0.3335 -0.0289 -0.0101 -0.0340 186 ASP A C 1349 O O . ASP A 174 A 0.3239 0.4804 0.3290 -0.0331 -0.0088 -0.0326 186 ASP A O 1350 C CB . ASP A 174 A 0.3349 0.5134 0.3502 -0.0171 -0.0126 -0.0363 186 ASP A CB 1351 C CG . ASP A 174 A 0.3680 0.5350 0.3852 -0.0108 -0.0141 -0.0350 186 ASP A CG 1352 O OD1 . ASP A 174 A 0.3038 0.4600 0.3194 -0.0130 -0.0135 -0.0333 186 ASP A OD1 1353 O OD2 . ASP A 174 A 0.3992 0.5680 0.4195 -0.0037 -0.0157 -0.0358 186 ASP A OD2 1354 N N . SER A 175 B 0.3224 0.5024 0.3326 -0.0268 -0.0114 -0.0343 186 SER A N 1355 C CA . SER A 175 B 0.3391 0.5190 0.3471 -0.0303 -0.0111 -0.0332 186 SER A CA 1356 C C . SER A 175 B 0.3416 0.5094 0.3507 -0.0259 -0.0120 -0.0316 186 SER A C 1357 O O . SER A 175 B 0.3320 0.4973 0.3390 -0.0290 -0.0116 -0.0305 186 SER A O 1358 C CB . SER A 175 B 0.3210 0.5191 0.3305 -0.0298 -0.0122 -0.0342 186 SER A CB 1359 O OG . SER A 175 B 0.3848 0.5882 0.3991 -0.0208 -0.0144 -0.0346 186 SER A OG 1360 N N . HIS A 176 ? 0.3643 0.5250 0.3766 -0.0192 -0.0132 -0.0314 187 HIS A N 1361 C CA . HIS A 176 ? 0.3286 0.4775 0.3417 -0.0152 -0.0141 -0.0298 187 HIS A CA 1362 C C . HIS A 176 ? 0.2676 0.4011 0.2784 -0.0187 -0.0124 -0.0285 187 HIS A C 1363 O O . HIS A 176 ? 0.2331 0.3628 0.2426 -0.0214 -0.0111 -0.0289 187 HIS A O 1364 C CB . HIS A 176 ? 0.4025 0.5503 0.4194 -0.0067 -0.0162 -0.0302 187 HIS A CB 1365 C CG . HIS A 176 ? 0.4894 0.6513 0.5087 -0.0017 -0.0181 -0.0313 187 HIS A CG 1366 N ND1 . HIS A 176 ? 0.5713 0.7462 0.5916 -0.0016 -0.0180 -0.0331 187 HIS A ND1 1367 C CD2 . HIS A 176 ? 0.6193 0.7843 0.6399 0.0034 -0.0201 -0.0308 187 HIS A CD2 1368 C CE1 . HIS A 176 ? 0.6070 0.7932 0.6296 0.0037 -0.0198 -0.0338 187 HIS A CE1 1369 N NE2 . HIS A 176 ? 0.7512 0.9310 0.7738 0.0069 -0.0212 -0.0323 187 HIS A NE2 1370 N N . ARG A 177 ? 0.2630 0.3878 0.2729 -0.0186 -0.0124 -0.0270 188 ARG A N 1371 C CA . ARG A 177 ? 0.2110 0.3208 0.2192 -0.0205 -0.0109 -0.0257 188 ARG A CA 1372 C C . ARG A 177 ? 0.2057 0.3081 0.2169 -0.0151 -0.0119 -0.0255 188 ARG A C 1373 O O . ARG A 177 ? 0.1934 0.2960 0.2072 -0.0092 -0.0139 -0.0254 188 ARG A O 1374 C CB . ARG A 177 ? 0.2470 0.3502 0.2538 -0.0216 -0.0106 -0.0243 188 ARG A CB 1375 C CG . ARG A 177 ? 0.2425 0.3508 0.2455 -0.0281 -0.0092 -0.0244 188 ARG A CG 1376 C CD . ARG A 177 ? 0.2458 0.3463 0.2469 -0.0295 -0.0086 -0.0230 188 ARG A CD 1377 N NE . ARG A 177 ? 0.3256 0.4307 0.3224 -0.0361 -0.0072 -0.0232 188 ARG A NE 1378 C CZ . ARG A 177 ? 0.3488 0.4488 0.3429 -0.0389 -0.0063 -0.0223 188 ARG A CZ 1379 N NH1 . ARG A 177 ? 0.3581 0.4485 0.3534 -0.0356 -0.0066 -0.0211 188 ARG A NH1 1380 N NH2 . ARG A 177 ? 0.3993 0.5040 0.3890 -0.0452 -0.0051 -0.0227 188 ARG A NH2 1381 N N . ARG A 178 A 0.1829 0.2785 0.1930 -0.0174 -0.0106 -0.0253 188 ARG A N 1382 C CA . ARG A 178 A 0.1907 0.2794 0.2031 -0.0132 -0.0114 -0.0251 188 ARG A CA 1383 C C . ARG A 178 A 0.1709 0.2478 0.1815 -0.0163 -0.0096 -0.0238 188 ARG A C 1384 O O . ARG A 178 A 0.1761 0.2523 0.1836 -0.0215 -0.0078 -0.0239 188 ARG A O 1385 C CB . ARG A 178 A 0.2115 0.3082 0.2253 -0.0116 -0.0121 -0.0267 188 ARG A CB 1386 C CG . ARG A 178 A 0.2324 0.3417 0.2481 -0.0079 -0.0137 -0.0281 188 ARG A CG 1387 C CD . ARG A 178 A 0.2305 0.3464 0.2478 -0.0053 -0.0144 -0.0298 188 ARG A CD 1388 N NE . ARG A 178 A 0.2361 0.3659 0.2549 -0.0023 -0.0156 -0.0314 188 ARG A NE 1389 C CZ . ARG A 178 A 0.2741 0.4063 0.2951 0.0041 -0.0176 -0.0316 188 ARG A CZ 1390 N NH1 . ARG A 178 A 0.2939 0.4152 0.3155 0.0082 -0.0187 -0.0305 188 ARG A NH1 1391 N NH2 . ARG A 178 A 0.3367 0.4825 0.3590 0.0068 -0.0185 -0.0330 188 ARG A NH2 1392 N N . GLY A 179 ? 0.1551 0.2226 0.1674 -0.0132 -0.0101 -0.0226 189 GLY A N 1393 C CA . GLY A 179 ? 0.1594 0.2161 0.1704 -0.0155 -0.0085 -0.0212 189 GLY A CA 1394 C C . GLY A 179 ? 0.1567 0.2051 0.1696 -0.0123 -0.0091 -0.0198 189 GLY A C 1395 O O . GLY A 179 ? 0.1600 0.2094 0.1752 -0.0077 -0.0111 -0.0200 189 GLY A O 1396 N N . PHE A 180 ? 0.1506 0.1903 0.1620 -0.0146 -0.0074 -0.0185 190 PHE A N 1397 C CA . PHE A 180 ? 0.1405 0.1723 0.1536 -0.0120 -0.0078 -0.0171 190 PHE A CA 1398 C C . PHE A 180 ? 0.1255 0.1552 0.1373 -0.0133 -0.0071 -0.0164 190 PHE A C 1399 O O . PHE A 180 ? 0.1541 0.1880 0.1634 -0.0165 -0.0062 -0.0170 190 PHE A O 1400 C CB . PHE A 180 ? 0.1445 0.1685 0.1579 -0.0125 -0.0067 -0.0160 190 PHE A CB 1401 C CG . PHE A 180 ? 0.1358 0.1561 0.1457 -0.0169 -0.0041 -0.0156 190 PHE A CG 1402 C CD1 . PHE A 180 ? 0.1583 0.1743 0.1658 -0.0192 -0.0023 -0.0149 190 PHE A CD1 1403 C CD2 . PHE A 180 ? 0.1440 0.1639 0.1525 -0.0187 -0.0034 -0.0158 190 PHE A CD2 1404 C CE1 . PHE A 180 ? 0.1492 0.1604 0.1529 -0.0230 0.0000 -0.0146 190 PHE A CE1 1405 C CE2 . PHE A 180 ? 0.1426 0.1577 0.1472 -0.0225 -0.0010 -0.0153 190 PHE A CE2 1406 C CZ . PHE A 180 ? 0.1555 0.1658 0.1575 -0.0245 0.0007 -0.0147 190 PHE A CZ 1407 N N . CYS A 181 ? 0.1283 0.1520 0.1416 -0.0111 -0.0075 -0.0152 191 CYS A N 1408 C CA . CYS A 181 ? 0.1353 0.1561 0.1471 -0.0124 -0.0067 -0.0145 191 CYS A CA 1409 C C . CYS A 181 ? 0.1405 0.1527 0.1536 -0.0115 -0.0061 -0.0130 191 CYS A C 1410 O O . CYS A 181 ? 0.1370 0.1457 0.1517 -0.0104 -0.0060 -0.0125 191 CYS A O 1411 C CB . CYS A 181 ? 0.1372 0.1635 0.1495 -0.0103 -0.0088 -0.0149 191 CYS A CB 1412 S SG . CYS A 181 ? 0.1893 0.2158 0.1988 -0.0132 -0.0078 -0.0144 191 CYS A SG 1413 N N . SER A 182 ? 0.1533 0.1623 0.1654 -0.0122 -0.0054 -0.0122 192 SER A N 1414 C CA . SER A 182 ? 0.1540 0.1556 0.1672 -0.0116 -0.0046 -0.0108 192 SER A CA 1415 C C . SER A 182 ? 0.1325 0.1326 0.1489 -0.0080 -0.0066 -0.0103 192 SER A C 1416 O O . SER A 182 ? 0.1396 0.1426 0.1566 -0.0056 -0.0090 -0.0107 192 SER A O 1417 C CB . SER A 182 ? 0.1852 0.1847 0.1970 -0.0127 -0.0040 -0.0102 192 SER A CB 1418 O OG . SER A 182 ? 0.2552 0.2566 0.2637 -0.0162 -0.0023 -0.0109 192 SER A OG 1419 N N . ALA A 183 ? 0.1321 0.1274 0.1499 -0.0078 -0.0057 -0.0093 193 ALA A N 1420 C CA . ALA A 183 ? 0.1327 0.1258 0.1531 -0.0052 -0.0074 -0.0086 193 ALA A CA 1421 C C . ALA A 183 ? 0.1471 0.1433 0.1687 -0.0037 -0.0088 -0.0095 193 ALA A C 1422 O O . ALA A 183 ? 0.1486 0.1433 0.1719 -0.0017 -0.0103 -0.0091 193 ALA A O 1423 C CB . ALA A 183 ? 0.1419 0.1337 0.1627 -0.0035 -0.0092 -0.0082 193 ALA A CB 1424 N N . ASP A 184 ? 0.1440 0.1442 0.1642 -0.0051 -0.0081 -0.0105 194 ASP A N 1425 C CA . ASP A 184 ? 0.1294 0.1321 0.1504 -0.0044 -0.0087 -0.0112 194 ASP A CA 1426 C C . ASP A 184 ? 0.1278 0.1269 0.1487 -0.0061 -0.0069 -0.0104 194 ASP A C 1427 O O . ASP A 184 ? 0.1318 0.1317 0.1533 -0.0057 -0.0074 -0.0106 194 ASP A O 1428 C CB . ASP A 184 ? 0.1391 0.1487 0.1585 -0.0053 -0.0090 -0.0129 194 ASP A CB 1429 C CG . ASP A 184 ? 0.1464 0.1604 0.1663 -0.0025 -0.0113 -0.0138 194 ASP A CG 1430 O OD1 . ASP A 184 ? 0.1453 0.1572 0.1667 0.0004 -0.0131 -0.0135 194 ASP A OD1 1431 O OD2 . ASP A 184 ? 0.1331 0.1527 0.1516 -0.0034 -0.0113 -0.0147 194 ASP A OD2 1432 N N . SER A 185 ? 0.1251 0.1198 0.1448 -0.0078 -0.0048 -0.0094 195 SER A N 1433 C CA . SER A 185 ? 0.1415 0.1323 0.1607 -0.0089 -0.0029 -0.0085 195 SER A CA 1434 C C . SER A 185 ? 0.1423 0.1316 0.1644 -0.0068 -0.0040 -0.0075 195 SER A C 1435 O O . SER A 185 ? 0.1514 0.1402 0.1759 -0.0049 -0.0054 -0.0070 195 SER A O 1436 C CB . SER A 185 ? 0.1536 0.1396 0.1716 -0.0101 -0.0006 -0.0076 195 SER A CB 1437 O OG . SER A 185 ? 0.1565 0.1434 0.1710 -0.0127 0.0006 -0.0085 195 SER A OG 1438 N N . GLY A 186 ? 0.1417 0.1301 0.1630 -0.0075 -0.0033 -0.0073 196 GLY A N 1439 C CA . GLY A 186 ? 0.1424 0.1298 0.1662 -0.0059 -0.0043 -0.0063 196 GLY A CA 1440 C C . GLY A 186 ? 0.1554 0.1469 0.1802 -0.0048 -0.0066 -0.0072 196 GLY A C 1441 O O . GLY A 186 ? 0.1570 0.1480 0.1832 -0.0040 -0.0073 -0.0065 196 GLY A O 1442 N N . GLY A 187 ? 0.1287 0.1244 0.1529 -0.0047 -0.0077 -0.0088 197 GLY A N 1443 C CA . GLY A 187 ? 0.1329 0.1327 0.1576 -0.0035 -0.0096 -0.0100 197 GLY A CA 1444 C C . GLY A 187 ? 0.1266 0.1286 0.1493 -0.0054 -0.0088 -0.0107 197 GLY A C 1445 O O . GLY A 187 ? 0.1414 0.1432 0.1615 -0.0079 -0.0070 -0.0108 197 GLY A O 1446 N N . PRO A 188 ? 0.1141 0.1184 0.1375 -0.0045 -0.0102 -0.0112 198 PRO A N 1447 C CA . PRO A 188 ? 0.1334 0.1399 0.1548 -0.0065 -0.0096 -0.0118 198 PRO A CA 1448 C C . PRO A 188 ? 0.1255 0.1387 0.1451 -0.0076 -0.0097 -0.0139 198 PRO A C 1449 O O . PRO A 188 ? 0.1495 0.1666 0.1702 -0.0056 -0.0110 -0.0151 198 PRO A O 1450 C CB . PRO A 188 ? 0.1446 0.1510 0.1676 -0.0051 -0.0112 -0.0115 198 PRO A CB 1451 C CG . PRO A 188 ? 0.1437 0.1507 0.1689 -0.0022 -0.0130 -0.0120 198 PRO A CG 1452 C CD . PRO A 188 ? 0.1361 0.1401 0.1619 -0.0019 -0.0123 -0.0111 198 PRO A CD 1453 N N . LEU A 189 ? 0.1285 0.1427 0.1450 -0.0108 -0.0082 -0.0141 199 LEU A N 1454 C CA . LEU A 189 ? 0.1413 0.1628 0.1561 -0.0125 -0.0084 -0.0160 199 LEU A CA 1455 C C . LEU A 189 ? 0.1315 0.1543 0.1467 -0.0121 -0.0093 -0.0163 199 LEU A C 1456 O O . LEU A 189 ? 0.1496 0.1680 0.1634 -0.0136 -0.0087 -0.0150 199 LEU A O 1457 C CB . LEU A 189 ? 0.1520 0.1733 0.1626 -0.0169 -0.0063 -0.0161 199 LEU A CB 1458 C CG . LEU A 189 ? 0.1493 0.1791 0.1578 -0.0193 -0.0062 -0.0180 199 LEU A CG 1459 C CD1 . LEU A 189 ? 0.1452 0.1820 0.1553 -0.0177 -0.0071 -0.0194 199 LEU A CD1 1460 C CD2 . LEU A 189 ? 0.1900 0.2178 0.1933 -0.0245 -0.0042 -0.0178 199 LEU A CD2 1461 N N . VAL A 190 ? 0.1423 0.1707 0.1591 -0.0097 -0.0110 -0.0179 200 VAL A N 1462 C CA . VAL A 190 ? 0.1579 0.1877 0.1752 -0.0089 -0.0121 -0.0184 200 VAL A CA 1463 C C . VAL A 190 ? 0.1571 0.1948 0.1723 -0.0112 -0.0117 -0.0203 200 VAL A C 1464 O O . VAL A 190 ? 0.1697 0.2142 0.1851 -0.0104 -0.0119 -0.0220 200 VAL A O 1465 C CB . VAL A 190 ? 0.1539 0.1840 0.1740 -0.0047 -0.0141 -0.0190 200 VAL A CB 1466 C CG1 . VAL A 190 ? 0.1619 0.1937 0.1820 -0.0041 -0.0151 -0.0197 200 VAL A CG1 1467 C CG2 . VAL A 190 ? 0.1474 0.1702 0.1694 -0.0030 -0.0145 -0.0171 200 VAL A CG2 1468 N N . CYS A 191 ? 0.1733 0.2099 0.1862 -0.0141 -0.0110 -0.0198 201 CYS A N 1469 C CA . CYS A 191 ? 0.2120 0.2557 0.2224 -0.0168 -0.0106 -0.0214 201 CYS A CA 1470 C C . CYS A 191 ? 0.1975 0.2404 0.2079 -0.0166 -0.0114 -0.0213 201 CYS A C 1471 O O . CYS A 191 ? 0.1969 0.2328 0.2067 -0.0173 -0.0113 -0.0194 201 CYS A O 1472 C CB . CYS A 191 ? 0.2293 0.2720 0.2354 -0.0219 -0.0086 -0.0209 201 CYS A CB 1473 S SG . CYS A 191 ? 0.2301 0.2691 0.2353 -0.0230 -0.0072 -0.0200 201 CYS A SG 1474 N N . ARG A 192 ? 0.2708 0.3210 0.2819 -0.0153 -0.0123 -0.0234 202 ARG A N 1475 C CA . ARG A 192 ? 0.2935 0.3436 0.3044 -0.0151 -0.0132 -0.0236 202 ARG A CA 1476 C C . ARG A 192 ? 0.2310 0.2732 0.2441 -0.0125 -0.0144 -0.0218 202 ARG A C 1477 O O . ARG A 192 ? 0.2462 0.2844 0.2583 -0.0138 -0.0146 -0.0204 202 ARG A O 1478 C CB . ARG A 192 ? 0.4062 0.4561 0.4131 -0.0199 -0.0121 -0.0231 202 ARG A CB 1479 C CG . ARG A 192 ? 0.6171 0.6762 0.6224 -0.0217 -0.0120 -0.0254 202 ARG A CG 1480 C CD . ARG A 192 ? 0.7952 0.8632 0.8002 -0.0226 -0.0112 -0.0273 202 ARG A CD 1481 N NE . ARG A 192 ? 1.0126 1.0905 1.0165 -0.0239 -0.0111 -0.0297 202 ARG A NE 1482 C CZ . ARG A 192 ? 1.0470 1.1282 1.0470 -0.0290 -0.0101 -0.0300 202 ARG A CZ 1483 N NH1 . ARG A 192 ? 1.0875 1.1619 1.0837 -0.0334 -0.0090 -0.0280 202 ARG A NH1 1484 N NH2 . ARG A 192 ? 1.0106 1.1018 1.0101 -0.0297 -0.0100 -0.0323 202 ARG A NH2 1485 N N . ASN A 193 ? 0.2158 0.2560 0.2315 -0.0089 -0.0152 -0.0218 207 ASN A N 1486 C CA . ASN A 193 ? 0.2307 0.2643 0.2485 -0.0066 -0.0164 -0.0202 207 ASN A CA 1487 C C . ASN A 193 ? 0.2004 0.2269 0.2180 -0.0083 -0.0158 -0.0174 207 ASN A C 1488 O O . ASN A 193 ? 0.2228 0.2452 0.2416 -0.0075 -0.0167 -0.0160 207 ASN A O 1489 C CB . ASN A 193 ? 0.2885 0.3234 0.3065 -0.0051 -0.0179 -0.0213 207 ASN A CB 1490 C CG . ASN A 193 ? 0.4801 0.5183 0.4990 -0.0014 -0.0190 -0.0235 207 ASN A CG 1491 O OD1 . ASN A 193 ? 0.6643 0.6991 0.6847 0.0011 -0.0198 -0.0232 207 ASN A OD1 1492 N ND2 . ASN A 193 ? 0.5522 0.5971 0.5700 -0.0011 -0.0191 -0.0259 207 ASN A ND2 1493 N N . ARG A 194 ? 0.1817 0.2070 0.1977 -0.0107 -0.0141 -0.0166 208 ARG A N 1494 C CA . ARG A 194 ? 0.1867 0.2050 0.2022 -0.0118 -0.0132 -0.0140 208 ARG A CA 1495 C C . ARG A 194 ? 0.1487 0.1649 0.1643 -0.0118 -0.0119 -0.0136 208 ARG A C 1496 O O . ARG A 194 ? 0.1780 0.1984 0.1925 -0.0128 -0.0112 -0.0151 208 ARG A O 1497 C CB . ARG A 194 ? 0.2001 0.2170 0.2119 -0.0153 -0.0122 -0.0132 208 ARG A CB 1498 C CG . ARG A 194 ? 0.2171 0.2358 0.2284 -0.0157 -0.0134 -0.0134 208 ARG A CG 1499 C CD . ARG A 194 ? 0.2228 0.2369 0.2364 -0.0137 -0.0146 -0.0114 208 ARG A CD 1500 N NE . ARG A 194 ? 0.2579 0.2735 0.2704 -0.0146 -0.0157 -0.0114 208 ARG A NE 1501 C CZ . ARG A 194 ? 0.2652 0.2846 0.2791 -0.0132 -0.0172 -0.0130 208 ARG A CZ 1502 N NH1 . ARG A 194 ? 0.2503 0.2719 0.2664 -0.0106 -0.0179 -0.0146 208 ARG A NH1 1503 N NH2 . ARG A 194 ? 0.3211 0.3415 0.3335 -0.0145 -0.0180 -0.0129 208 ARG A NH2 1504 N N . ALA A 195 ? 0.1624 0.1724 0.1793 -0.0108 -0.0116 -0.0115 209 ALA A N 1505 C CA . ALA A 195 ? 0.1451 0.1522 0.1620 -0.0109 -0.0102 -0.0109 209 ALA A CA 1506 C C . ALA A 195 ? 0.1352 0.1395 0.1479 -0.0142 -0.0081 -0.0103 209 ALA A C 1507 O O . ALA A 195 ? 0.1658 0.1641 0.1776 -0.0144 -0.0073 -0.0083 209 ALA A O 1508 C CB . ALA A 195 ? 0.1779 0.1802 0.1978 -0.0086 -0.0105 -0.0089 209 ALA A CB 1509 N N . HIS A 196 ? 0.1482 0.1567 0.1581 -0.0167 -0.0074 -0.0119 210 HIS A N 1510 C CA . HIS A 196 ? 0.1737 0.1791 0.1785 -0.0206 -0.0054 -0.0115 210 HIS A CA 1511 C C . HIS A 196 ? 0.1778 0.1793 0.1814 -0.0212 -0.0037 -0.0110 210 HIS A C 1512 O O . HIS A 196 ? 0.1854 0.1813 0.1847 -0.0237 -0.0020 -0.0101 210 HIS A O 1513 C CB . HIS A 196 ? 0.1852 0.1974 0.1870 -0.0238 -0.0052 -0.0135 210 HIS A CB 1514 C CG . HIS A 196 ? 0.2180 0.2314 0.2186 -0.0249 -0.0060 -0.0135 210 HIS A CG 1515 N ND1 . HIS A 196 ? 0.3662 0.3738 0.3626 -0.0273 -0.0051 -0.0120 210 HIS A ND1 1516 C CD2 . HIS A 196 ? 0.2759 0.2954 0.2786 -0.0236 -0.0076 -0.0148 210 HIS A CD2 1517 C CE1 . HIS A 196 ? 0.3675 0.3779 0.3636 -0.0279 -0.0062 -0.0123 210 HIS A CE1 1518 N NE2 . HIS A 196 ? 0.3295 0.3473 0.3294 -0.0257 -0.0077 -0.0141 210 HIS A NE2 1519 N N . GLY A 197 ? 0.1520 0.1557 0.1588 -0.0191 -0.0042 -0.0116 211 GLY A N 1520 C CA . GLY A 197 ? 0.1604 0.1606 0.1661 -0.0197 -0.0027 -0.0112 211 GLY A CA 1521 C C . GLY A 197 ? 0.1580 0.1564 0.1681 -0.0161 -0.0034 -0.0104 211 GLY A C 1522 O O . GLY A 197 ? 0.1485 0.1495 0.1624 -0.0133 -0.0054 -0.0106 211 GLY A O 1523 N N . LEU A 198 ? 0.1554 0.1489 0.1645 -0.0164 -0.0019 -0.0095 212 LEU A N 1524 C CA . LEU A 198 ? 0.1427 0.1351 0.1554 -0.0137 -0.0023 -0.0089 212 LEU A CA 1525 C C . LEU A 198 ? 0.1412 0.1339 0.1520 -0.0153 -0.0011 -0.0096 212 LEU A C 1526 O O . LEU A 198 ? 0.1466 0.1358 0.1533 -0.0180 0.0009 -0.0095 212 LEU A O 1527 C CB . LEU A 198 ? 0.1842 0.1703 0.1983 -0.0120 -0.0016 -0.0068 212 LEU A CB 1528 C CG . LEU A 198 ? 0.2020 0.1886 0.2209 -0.0089 -0.0031 -0.0061 212 LEU A CG 1529 C CD1 . LEU A 198 ? 0.1791 0.1687 0.2003 -0.0074 -0.0053 -0.0062 212 LEU A CD1 1530 C CD2 . LEU A 198 ? 0.2336 0.2149 0.2536 -0.0076 -0.0018 -0.0041 212 LEU A CD2 1531 N N . VAL A 199 ? 0.1275 0.1240 0.1408 -0.0137 -0.0024 -0.0104 213 VAL A N 1532 C CA . VAL A 199 ? 0.1435 0.1412 0.1550 -0.0152 -0.0015 -0.0111 213 VAL A CA 1533 C C . VAL A 199 ? 0.1331 0.1237 0.1429 -0.0161 0.0007 -0.0098 213 VAL A C 1534 O O . VAL A 199 ? 0.1469 0.1337 0.1593 -0.0138 0.0007 -0.0085 213 VAL A O 1535 C CB . VAL A 199 ? 0.1339 0.1353 0.1486 -0.0126 -0.0034 -0.0116 213 VAL A CB 1536 C CG1 . VAL A 199 ? 0.1325 0.1342 0.1454 -0.0141 -0.0024 -0.0119 213 VAL A CG1 1537 C CG2 . VAL A 199 ? 0.1256 0.1341 0.1414 -0.0113 -0.0055 -0.0130 213 VAL A CG2 1538 N N . SER A 200 ? 0.1389 0.1281 0.1442 -0.0195 0.0027 -0.0103 214 SER A N 1539 C CA . SER A 200 ? 0.1494 0.1313 0.1522 -0.0204 0.0051 -0.0094 214 SER A CA 1540 C C . SER A 200 ? 0.1481 0.1309 0.1486 -0.0226 0.0061 -0.0102 214 SER A C 1541 O O . SER A 200 ? 0.1641 0.1451 0.1665 -0.0211 0.0063 -0.0096 214 SER A O 1542 C CB . SER A 200 ? 0.1573 0.1334 0.1555 -0.0225 0.0070 -0.0089 214 SER A CB 1543 O OG . SER A 200 ? 0.1845 0.1532 0.1802 -0.0228 0.0095 -0.0081 214 SER A OG 1544 N N . PHE A 201 ? 0.1611 0.1464 0.1573 -0.0263 0.0068 -0.0114 215 PHE A N 1545 C CA . PHE A 201 ? 0.1660 0.1520 0.1595 -0.0288 0.0078 -0.0120 215 PHE A CA 1546 C C . PHE A 201 ? 0.1589 0.1526 0.1501 -0.0321 0.0072 -0.0135 215 PHE A C 1547 O O . PHE A 201 ? 0.1713 0.1684 0.1614 -0.0334 0.0066 -0.0142 215 PHE A O 1548 C CB . PHE A 201 ? 0.1935 0.1706 0.1820 -0.0312 0.0109 -0.0115 215 PHE A CB 1549 C CG . PHE A 201 ? 0.1917 0.1651 0.1740 -0.0349 0.0126 -0.0119 215 PHE A CG 1550 C CD1 . PHE A 201 ? 0.1954 0.1710 0.1723 -0.0398 0.0134 -0.0131 215 PHE A CD1 1551 C CD2 . PHE A 201 ? 0.1996 0.1669 0.1809 -0.0337 0.0133 -0.0109 215 PHE A CD2 1552 C CE1 . PHE A 201 ? 0.2064 0.1779 0.1768 -0.0438 0.0150 -0.0134 215 PHE A CE1 1553 C CE2 . PHE A 201 ? 0.2189 0.1818 0.1938 -0.0373 0.0148 -0.0111 215 PHE A CE2 1554 C CZ . PHE A 201 ? 0.2172 0.1819 0.1864 -0.0425 0.0157 -0.0124 215 PHE A CZ 1555 N N . SER A 202 ? 0.1798 0.1764 0.1699 -0.0336 0.0072 -0.0141 216 SER A N 1556 C CA . SER A 202 ? 0.1750 0.1791 0.1622 -0.0373 0.0070 -0.0154 216 SER A CA 1557 C C . SER A 202 ? 0.1966 0.1993 0.1800 -0.0405 0.0084 -0.0156 216 SER A C 1558 O O . SER A 202 ? 0.1959 0.1902 0.1776 -0.0406 0.0103 -0.0149 216 SER A O 1559 C CB . SER A 202 ? 0.1869 0.2012 0.1789 -0.0344 0.0040 -0.0161 216 SER A CB 1560 O OG . SER A 202 ? 0.1752 0.1905 0.1709 -0.0308 0.0026 -0.0156 216 SER A OG 1561 N N . GLY A 203 ? 0.2047 0.2158 0.1868 -0.0431 0.0077 -0.0167 217 GLY A N 1562 C CA . GLY A 203 ? 0.1977 0.2083 0.1754 -0.0471 0.0091 -0.0170 217 GLY A CA 1563 C C . GLY A 203 ? 0.2064 0.2208 0.1875 -0.0446 0.0075 -0.0166 217 GLY A C 1564 O O . GLY A 203 ? 0.2268 0.2419 0.2131 -0.0396 0.0057 -0.0160 217 GLY A O 1565 N N . LEU A 204 ? 0.2218 0.2384 0.1992 -0.0483 0.0082 -0.0170 218 LEU A N 1566 C CA . LEU A 204 ? 0.2412 0.2599 0.2206 -0.0466 0.0071 -0.0166 218 LEU A CA 1567 C C . LEU A 204 ? 0.2121 0.2401 0.1970 -0.0421 0.0037 -0.0166 218 LEU A C 1568 O O . LEU A 204 ? 0.2489 0.2759 0.2371 -0.0383 0.0024 -0.0157 218 LEU A O 1569 C CB . LEU A 204 ? 0.2836 0.3042 0.2575 -0.0521 0.0084 -0.0171 218 LEU A CB 1570 C CG . LEU A 204 ? 0.3030 0.3258 0.2779 -0.0512 0.0074 -0.0166 218 LEU A CG 1571 C CD1 . LEU A 204 ? 0.3194 0.3321 0.2952 -0.0488 0.0085 -0.0155 218 LEU A CD1 1572 C CD2 . LEU A 204 ? 0.4068 0.4331 0.3760 -0.0572 0.0084 -0.0172 218 LEU A CD2 1573 N N . TRP A 205 ? 0.2065 0.2435 0.1922 -0.0424 0.0025 -0.0175 219 TRP A N 1574 C CA . TRP A 205 ? 0.2105 0.2566 0.2010 -0.0379 -0.0005 -0.0177 219 TRP A CA 1575 C C . TRP A 205 ? 0.1880 0.2345 0.1817 -0.0346 -0.0014 -0.0180 219 TRP A C 1576 O O . TRP A 205 ? 0.2056 0.2533 0.1974 -0.0374 -0.0003 -0.0187 219 TRP A O 1577 C CB . TRP A 205 ? 0.2459 0.3041 0.2349 -0.0406 -0.0014 -0.0187 219 TRP A CB 1578 C CG . TRP A 205 ? 0.2857 0.3438 0.2705 -0.0449 -0.0003 -0.0185 219 TRP A CG 1579 C CD1 . TRP A 205 ? 0.2974 0.3547 0.2763 -0.0517 0.0019 -0.0190 219 TRP A CD1 1580 C CD2 . TRP A 205 ? 0.3655 0.4236 0.3514 -0.0429 -0.0015 -0.0176 219 TRP A CD2 1581 N NE1 . TRP A 205 ? 0.3341 0.3913 0.3105 -0.0541 0.0022 -0.0186 219 TRP A NE1 1582 C CE2 . TRP A 205 ? 0.3224 0.3803 0.3028 -0.0490 0.0001 -0.0177 219 TRP A CE2 1583 C CE3 . TRP A 205 ? 0.3436 0.4016 0.3335 -0.0372 -0.0038 -0.0167 219 TRP A CE3 1584 C CZ2 . TRP A 205 ? 0.3809 0.4388 0.3606 -0.0491 -0.0003 -0.0170 219 TRP A CZ2 1585 C CZ3 . TRP A 205 ? 0.4125 0.4702 0.4014 -0.0374 -0.0044 -0.0159 219 TRP A CZ3 1586 C CH2 . TRP A 205 ? 0.4121 0.4701 0.3963 -0.0431 -0.0027 -0.0160 219 TRP A CH2 1587 N N . CYS A 206 ? 0.1830 0.2282 0.1811 -0.0290 -0.0033 -0.0174 220 CYS A N 1588 C CA . CYS A 206 ? 0.1792 0.2237 0.1803 -0.0259 -0.0041 -0.0177 220 CYS A CA 1589 C C . CYS A 206 ? 0.1769 0.2320 0.1785 -0.0261 -0.0051 -0.0191 220 CYS A C 1590 O O . CYS A 206 ? 0.1968 0.2612 0.1995 -0.0247 -0.0068 -0.0197 220 CYS A O 1591 C CB . CYS A 206 ? 0.1716 0.2128 0.1767 -0.0202 -0.0061 -0.0169 220 CYS A CB 1592 S SG . CYS A 206 ? 0.1867 0.2153 0.1917 -0.0201 -0.0046 -0.0153 220 CYS A SG 1593 N N . GLY A 207 ? 0.1822 0.2361 0.1829 -0.0279 -0.0041 -0.0195 221 GLY A N 1594 C CA . GLY A 207 ? 0.1903 0.2541 0.1914 -0.0284 -0.0048 -0.0209 221 GLY A CA 1595 C C . GLY A 207 ? 0.2341 0.3055 0.2312 -0.0341 -0.0038 -0.0219 221 GLY A C 1596 O O . GLY A 207 ? 0.2343 0.3153 0.2317 -0.0349 -0.0043 -0.0231 221 GLY A O 1597 N N . ASP A 208 ? 0.2084 0.2757 0.2017 -0.0382 -0.0021 -0.0213 222 ASP A N 1598 C CA . ASP A 208 ? 0.2374 0.3112 0.2262 -0.0444 -0.0010 -0.0221 222 ASP A CA 1599 C C . ASP A 208 ? 0.1919 0.2648 0.1771 -0.0488 0.0004 -0.0228 222 ASP A C 1600 O O . ASP A 208 ? 0.1957 0.2577 0.1785 -0.0502 0.0021 -0.0221 222 ASP A O 1601 C CB . ASP A 208 ? 0.2220 0.2884 0.2068 -0.0479 0.0006 -0.0213 222 ASP A CB 1602 C CG . ASP A 208 ? 0.2415 0.3146 0.2212 -0.0545 0.0016 -0.0221 222 ASP A CG 1603 O OD1 . ASP A 208 ? 0.2642 0.3470 0.2429 -0.0572 0.0013 -0.0232 222 ASP A OD1 1604 O OD2 . ASP A 208 ? 0.2640 0.3327 0.2405 -0.0571 0.0027 -0.0216 222 ASP A OD2 1605 N N . PRO A 209 A 0.2314 0.3164 0.2160 -0.0513 0.0000 -0.0241 222 PRO A N 1606 C CA . PRO A 209 A 0.2418 0.3261 0.2222 -0.0563 0.0014 -0.0247 222 PRO A CA 1607 C C . PRO A 209 A 0.2216 0.2976 0.1944 -0.0634 0.0040 -0.0244 222 PRO A C 1608 O O . PRO A 209 A 0.2580 0.3287 0.2265 -0.0671 0.0055 -0.0245 222 PRO A O 1609 C CB . PRO A 209 A 0.2711 0.3718 0.2526 -0.0576 0.0002 -0.0262 222 PRO A CB 1610 C CG . PRO A 209 A 0.3196 0.4289 0.3042 -0.0549 -0.0014 -0.0263 222 PRO A CG 1611 C CD . PRO A 209 A 0.2473 0.3470 0.2353 -0.0490 -0.0021 -0.0250 222 PRO A CD 1612 N N . LYS A 210 ? 0.2351 0.3091 0.2056 -0.0654 0.0047 -0.0240 223 LYS A N 1613 C CA . LYS A 210 ? 0.2744 0.3386 0.2371 -0.0718 0.0074 -0.0237 223 LYS A CA 1614 C C . LYS A 210 ? 0.2349 0.2831 0.1963 -0.0699 0.0090 -0.0226 223 LYS A C 1615 O O . LYS A 210 ? 0.2662 0.3048 0.2208 -0.0745 0.0113 -0.0224 223 LYS A O 1616 C CB . LYS A 210 ? 0.3477 0.4137 0.3082 -0.0742 0.0077 -0.0237 223 LYS A CB 1617 C CG . LYS A 210 ? 0.4066 0.4880 0.3663 -0.0781 0.0067 -0.0247 223 LYS A CG 1618 C CD . LYS A 210 ? 0.5012 0.5829 0.4576 -0.0815 0.0072 -0.0245 223 LYS A CD 1619 C CE . LYS A 210 ? 0.6381 0.7369 0.5951 -0.0841 0.0057 -0.0253 223 LYS A CE 1620 N NZ . LYS A 210 ? 0.6408 0.7463 0.5929 -0.0911 0.0066 -0.0265 223 LYS A NZ 1621 N N . THR A 211 ? 0.2232 0.2686 0.1910 -0.0629 0.0077 -0.0218 224 THR A N 1622 C CA . THR A 211 ? 0.2641 0.2960 0.2320 -0.0602 0.0089 -0.0206 224 THR A CA 1623 C C . THR A 211 ? 0.2399 0.2729 0.2137 -0.0547 0.0071 -0.0203 224 THR A C 1624 O O . THR A 211 ? 0.2055 0.2380 0.1849 -0.0491 0.0057 -0.0196 224 THR A O 1625 C CB . THR A 211 ? 0.2287 0.2543 0.1979 -0.0578 0.0093 -0.0197 224 THR A CB 1626 O OG1 . THR A 211 ? 0.2122 0.2463 0.1871 -0.0538 0.0069 -0.0197 224 THR A OG1 1627 C CG2 . THR A 211 ? 0.2411 0.2624 0.2030 -0.0638 0.0116 -0.0199 224 THR A CG2 1628 N N . PRO A 212 ? 0.2161 0.2506 0.1881 -0.0566 0.0073 -0.0207 225 PRO A N 1629 C CA . PRO A 212 ? 0.2088 0.2461 0.1862 -0.0519 0.0055 -0.0207 225 PRO A CA 1630 C C . PRO A 212 ? 0.1788 0.2066 0.1597 -0.0468 0.0054 -0.0193 225 PRO A C 1631 O O . PRO A 212 ? 0.1902 0.2073 0.1681 -0.0478 0.0072 -0.0183 225 PRO A O 1632 C CB . PRO A 212 ? 0.2226 0.2594 0.1954 -0.0561 0.0064 -0.0211 225 PRO A CB 1633 C CG . PRO A 212 ? 0.2585 0.2977 0.2246 -0.0632 0.0080 -0.0219 225 PRO A CG 1634 C CD . PRO A 212 ? 0.2655 0.2989 0.2300 -0.0636 0.0091 -0.0213 225 PRO A CD 1635 N N . ASP A 213 ? 0.1788 0.2109 0.1660 -0.0414 0.0032 -0.0193 226 ASP A N 1636 C CA . ASP A 213 ? 0.1777 0.2023 0.1685 -0.0367 0.0027 -0.0180 226 ASP A CA 1637 C C . ASP A 213 ? 0.1710 0.1872 0.1591 -0.0380 0.0041 -0.0171 226 ASP A C 1638 O O . ASP A 213 ? 0.1754 0.1943 0.1617 -0.0400 0.0040 -0.0177 226 ASP A O 1639 C CB . ASP A 213 ? 0.1647 0.1957 0.1614 -0.0317 0.0001 -0.0184 226 ASP A CB 1640 C CG . ASP A 213 ? 0.1649 0.2006 0.1649 -0.0286 -0.0014 -0.0187 226 ASP A CG 1641 O OD1 . ASP A 213 ? 0.1765 0.2110 0.1746 -0.0304 -0.0005 -0.0184 226 ASP A OD1 1642 O OD2 . ASP A 213 ? 0.1654 0.2053 0.1694 -0.0243 -0.0035 -0.0191 226 ASP A OD2 1643 N N . VAL A 214 ? 0.1577 0.1641 0.1456 -0.0366 0.0053 -0.0157 227 VAL A N 1644 C CA . VAL A 214 ? 0.1801 0.1780 0.1655 -0.0370 0.0065 -0.0146 227 VAL A CA 1645 C C . VAL A 214 ? 0.1688 0.1639 0.1597 -0.0318 0.0053 -0.0134 227 VAL A C 1646 O O . VAL A 214 ? 0.1498 0.1435 0.1444 -0.0287 0.0048 -0.0128 227 VAL A O 1647 C CB . VAL A 214 ? 0.1763 0.1646 0.1560 -0.0398 0.0093 -0.0140 227 VAL A CB 1648 C CG1 . VAL A 214 ? 0.2113 0.1905 0.1880 -0.0398 0.0106 -0.0128 227 VAL A CG1 1649 C CG2 . VAL A 214 ? 0.2087 0.1996 0.1824 -0.0455 0.0105 -0.0152 227 VAL A CG2 1650 N N . TYR A 215 ? 0.1803 0.1747 0.1713 -0.0313 0.0047 -0.0130 228 TYR A N 1651 C CA . TYR A 215 ? 0.1626 0.1545 0.1579 -0.0272 0.0036 -0.0118 228 TYR A CA 1652 C C . TYR A 215 ? 0.1759 0.1590 0.1682 -0.0276 0.0051 -0.0103 228 TYR A C 1653 O O . TYR A 215 ? 0.1762 0.1561 0.1628 -0.0312 0.0065 -0.0104 228 TYR A O 1654 C CB . TYR A 215 ? 0.1578 0.1568 0.1557 -0.0262 0.0015 -0.0127 228 TYR A CB 1655 C CG . TYR A 215 ? 0.1590 0.1668 0.1604 -0.0246 -0.0002 -0.0141 228 TYR A CG 1656 C CD1 . TYR A 215 ? 0.1424 0.1516 0.1489 -0.0202 -0.0022 -0.0139 228 TYR A CD1 1657 C CD2 . TYR A 215 ? 0.1566 0.1713 0.1559 -0.0273 -0.0001 -0.0157 228 TYR A CD2 1658 C CE1 . TYR A 215 ? 0.1418 0.1579 0.1509 -0.0182 -0.0038 -0.0152 228 TYR A CE1 1659 C CE2 . TYR A 215 ? 0.1589 0.1818 0.1614 -0.0251 -0.0019 -0.0170 228 TYR A CE2 1660 C CZ . TYR A 215 ? 0.1333 0.1565 0.1406 -0.0204 -0.0037 -0.0167 228 TYR A CZ 1661 O OH . TYR A 215 ? 0.1500 0.1801 0.1599 -0.0177 -0.0055 -0.0178 228 TYR A OH 1662 N N . THR A 216 ? 0.1638 0.1429 0.1597 -0.0239 0.0047 -0.0088 229 THR A N 1663 C CA . THR A 216 ? 0.1768 0.1493 0.1712 -0.0231 0.0054 -0.0072 229 THR A CA 1664 C C . THR A 216 ? 0.1788 0.1548 0.1729 -0.0239 0.0040 -0.0075 229 THR A C 1665 O O . THR A 216 ? 0.1851 0.1676 0.1834 -0.0223 0.0019 -0.0081 229 THR A O 1666 C CB . THR A 216 ? 0.1774 0.1477 0.1770 -0.0187 0.0048 -0.0056 229 THR A CB 1667 O OG1 . THR A 216 ? 0.1982 0.1662 0.1984 -0.0180 0.0061 -0.0055 229 THR A OG1 1668 C CG2 . THR A 216 ? 0.1989 0.1631 0.1974 -0.0173 0.0055 -0.0037 229 THR A CG2 1669 N N . GLN A 217 ? 0.1755 0.1468 0.1639 -0.0266 0.0052 -0.0070 230 GLN A N 1670 C CA . GLN A 217 ? 0.2016 0.1753 0.1889 -0.0278 0.0040 -0.0071 230 GLN A CA 1671 C C . GLN A 217 ? 0.1777 0.1489 0.1688 -0.0240 0.0029 -0.0053 230 GLN A C 1672 O O . GLN A 217 ? 0.2058 0.1695 0.1943 -0.0233 0.0039 -0.0035 230 GLN A O 1673 C CB . GLN A 217 ? 0.1988 0.1671 0.1780 -0.0322 0.0057 -0.0070 230 GLN A CB 1674 C CG . GLN A 217 ? 0.2352 0.2066 0.2127 -0.0342 0.0045 -0.0073 230 GLN A CG 1675 C CD . GLN A 217 ? 0.3474 0.3099 0.3175 -0.0367 0.0059 -0.0060 230 GLN A CD 1676 O OE1 . GLN A 217 ? 0.3896 0.3475 0.3528 -0.0408 0.0077 -0.0064 230 GLN A OE1 1677 N NE2 . GLN A 217 ? 0.3826 0.3422 0.3537 -0.0345 0.0049 -0.0044 230 GLN A NE2 1678 N N . VAL A 218 ? 0.1659 0.1434 0.1626 -0.0215 0.0007 -0.0056 231 VAL A N 1679 C CA . VAL A 218 ? 0.1822 0.1583 0.1832 -0.0178 -0.0005 -0.0040 231 VAL A CA 1680 C C . VAL A 218 ? 0.1903 0.1627 0.1886 -0.0182 -0.0007 -0.0025 231 VAL A C 1681 O O . VAL A 218 ? 0.1881 0.1564 0.1881 -0.0156 -0.0008 -0.0004 231 VAL A O 1682 C CB . VAL A 218 ? 0.1717 0.1550 0.1783 -0.0157 -0.0028 -0.0049 231 VAL A CB 1683 C CG1 . VAL A 218 ? 0.2042 0.1868 0.2146 -0.0128 -0.0043 -0.0033 231 VAL A CG1 1684 C CG2 . VAL A 218 ? 0.1728 0.1581 0.1822 -0.0144 -0.0028 -0.0058 231 VAL A CG2 1685 N N . SER A 219 ? 0.1913 0.1652 0.1855 -0.0216 -0.0008 -0.0034 232 SER A N 1686 C CA . SER A 219 ? 0.2274 0.1976 0.2186 -0.0221 -0.0011 -0.0019 232 SER A CA 1687 C C . SER A 219 ? 0.2249 0.1853 0.2124 -0.0213 0.0005 0.0002 232 SER A C 1688 O O . SER A 219 ? 0.2442 0.2012 0.2316 -0.0195 0.0000 0.0022 232 SER A O 1689 C CB . SER A 219 ? 0.2858 0.2590 0.2724 -0.0264 -0.0012 -0.0032 232 SER A CB 1690 O OG . SER A 219 ? 0.3175 0.2880 0.2982 -0.0302 0.0006 -0.0041 232 SER A OG 1691 N N . ALA A 220 ? 0.2341 0.1899 0.2183 -0.0224 0.0026 0.0000 233 ALA A N 1692 C CA . ALA A 220 ? 0.2275 0.1734 0.2076 -0.0213 0.0045 0.0018 233 ALA A CA 1693 C C . ALA A 220 ? 0.2375 0.1821 0.2231 -0.0161 0.0042 0.0036 233 ALA A C 1694 O O . ALA A 220 ? 0.2809 0.2183 0.2642 -0.0140 0.0053 0.0056 233 ALA A O 1695 C CB . ALA A 220 ? 0.2566 0.1980 0.2315 -0.0240 0.0070 0.0007 233 ALA A CB 1696 N N . PHE A 221 ? 0.1937 0.1455 0.1866 -0.0140 0.0027 0.0031 234 PHE A N 1697 C CA . PHE A 221 ? 0.2020 0.1540 0.2005 -0.0097 0.0024 0.0046 234 PHE A CA 1698 C C . PHE A 221 ? 0.1782 0.1351 0.1820 -0.0075 0.0000 0.0057 234 PHE A C 1699 O O . PHE A 221 ? 0.1869 0.1449 0.1955 -0.0043 -0.0004 0.0071 234 PHE A O 1700 C CB . PHE A 221 ? 0.1991 0.1544 0.2011 -0.0093 0.0029 0.0033 234 PHE A CB 1701 C CG . PHE A 221 ? 0.2007 0.1509 0.1977 -0.0113 0.0054 0.0024 234 PHE A CG 1702 C CD1 . PHE A 221 ? 0.2359 0.1795 0.2315 -0.0092 0.0075 0.0037 234 PHE A CD1 1703 C CD2 . PHE A 221 ? 0.2124 0.1644 0.2057 -0.0152 0.0058 0.0004 234 PHE A CD2 1704 C CE1 . PHE A 221 ? 0.2553 0.1937 0.2457 -0.0113 0.0099 0.0028 234 PHE A CE1 1705 C CE2 . PHE A 221 ? 0.2260 0.1733 0.2142 -0.0176 0.0081 -0.0003 234 PHE A CE2 1706 C CZ . PHE A 221 ? 0.2468 0.1868 0.2333 -0.0156 0.0103 0.0008 234 PHE A CZ 1707 N N . VAL A 222 ? 0.2056 0.1657 0.2084 -0.0094 -0.0016 0.0051 235 VAL A N 1708 C CA . VAL A 222 ? 0.1879 0.1527 0.1951 -0.0078 -0.0040 0.0059 235 VAL A CA 1709 C C . VAL A 222 ? 0.1867 0.1483 0.1951 -0.0048 -0.0042 0.0088 235 VAL A C 1710 O O . VAL A 222 ? 0.1947 0.1600 0.2085 -0.0023 -0.0056 0.0098 235 VAL A O 1711 C CB . VAL A 222 ? 0.2158 0.1839 0.2206 -0.0107 -0.0053 0.0047 235 VAL A CB 1712 C CG1 . VAL A 222 ? 0.2250 0.1963 0.2332 -0.0091 -0.0077 0.0059 235 VAL A CG1 1713 C CG2 . VAL A 222 ? 0.2108 0.1845 0.2163 -0.0126 -0.0056 0.0019 235 VAL A CG2 1714 N N . ALA A 223 ? 0.2280 0.1827 0.2311 -0.0049 -0.0029 0.0102 236 ALA A N 1715 C CA . ALA A 223 ? 0.2385 0.1901 0.2425 -0.0015 -0.0031 0.0131 236 ALA A CA 1716 C C . ALA A 223 ? 0.2172 0.1696 0.2262 0.0020 -0.0023 0.0140 236 ALA A C 1717 O O . ALA A 223 ? 0.2460 0.2020 0.2599 0.0048 -0.0037 0.0157 236 ALA A O 1718 C CB . ALA A 223 ? 0.2312 0.1740 0.2277 -0.0020 -0.0016 0.0143 236 ALA A CB 1719 N N . TRP A 224 ? 0.2263 0.1759 0.2339 0.0017 -0.0002 0.0129 237 TRP A N 1720 C CA . TRP A 224 ? 0.2195 0.1700 0.2315 0.0047 0.0007 0.0135 237 TRP A CA 1721 C C . TRP A 224 ? 0.2393 0.1980 0.2582 0.0052 -0.0012 0.0130 237 TRP A C 1722 O O . TRP A 224 ? 0.2020 0.1636 0.2258 0.0080 -0.0017 0.0145 237 TRP A O 1723 C CB . TRP A 224 ? 0.2127 0.1584 0.2211 0.0036 0.0033 0.0121 237 TRP A CB 1724 C CG . TRP A 224 ? 0.2137 0.1614 0.2268 0.0062 0.0043 0.0123 237 TRP A CG 1725 C CD1 . TRP A 224 ? 0.2215 0.1669 0.2361 0.0100 0.0057 0.0142 237 TRP A CD1 1726 C CD2 . TRP A 224 ? 0.2032 0.1558 0.2200 0.0051 0.0039 0.0106 237 TRP A CD2 1727 N NE1 . TRP A 224 ? 0.2516 0.2006 0.2706 0.0110 0.0062 0.0137 237 TRP A NE1 1728 C CE2 . TRP A 224 ? 0.2292 0.1821 0.2495 0.0080 0.0052 0.0116 237 TRP A CE2 1729 C CE3 . TRP A 224 ? 0.2160 0.1728 0.2335 0.0022 0.0027 0.0085 237 TRP A CE3 1730 C CZ2 . TRP A 224 ? 0.2446 0.2014 0.2685 0.0076 0.0051 0.0106 237 TRP A CZ2 1731 C CZ3 . TRP A 224 ? 0.2264 0.1867 0.2475 0.0023 0.0027 0.0076 237 TRP A CZ3 1732 C CH2 . TRP A 224 ? 0.2148 0.1748 0.2388 0.0047 0.0038 0.0086 237 TRP A CH2 1733 N N . ILE A 225 ? 0.2034 0.1660 0.2228 0.0024 -0.0023 0.0108 238 ILE A N 1734 C CA . ILE A 225 ? 0.1977 0.1669 0.2227 0.0027 -0.0043 0.0102 238 ILE A CA 1735 C C . ILE A 225 ? 0.1976 0.1703 0.2263 0.0044 -0.0064 0.0121 238 ILE A C 1736 O O . ILE A 225 ? 0.1827 0.1587 0.2160 0.0061 -0.0071 0.0131 238 ILE A O 1737 C CB . ILE A 225 ? 0.1750 0.1475 0.1992 0.0000 -0.0054 0.0076 238 ILE A CB 1738 C CG1 . ILE A 225 ? 0.1935 0.1643 0.2154 -0.0014 -0.0036 0.0058 238 ILE A CG1 1739 C CG2 . ILE A 225 ? 0.1916 0.1697 0.2206 0.0005 -0.0077 0.0072 238 ILE A CG2 1740 C CD1 . ILE A 225 ? 0.1988 0.1727 0.2187 -0.0041 -0.0044 0.0034 238 ILE A CD1 1741 N N . TRP A 226 ? 0.1842 0.1562 0.2103 0.0036 -0.0074 0.0127 239 TRP A N 1742 C CA . TRP A 226 ? 0.1935 0.1691 0.2227 0.0048 -0.0095 0.0146 239 TRP A CA 1743 C C . TRP A 226 ? 0.2115 0.1861 0.2427 0.0082 -0.0089 0.0174 239 TRP A C 1744 O O . TRP A 226 ? 0.2187 0.1981 0.2544 0.0095 -0.0105 0.0188 239 TRP A O 1745 C CB . TRP A 226 ? 0.1876 0.1629 0.2135 0.0030 -0.0108 0.0145 239 TRP A CB 1746 C CG . TRP A 226 ? 0.1947 0.1734 0.2202 0.0002 -0.0120 0.0119 239 TRP A CG 1747 C CD1 . TRP A 226 ? 0.1848 0.1623 0.2057 -0.0024 -0.0115 0.0100 239 TRP A CD1 1748 C CD2 . TRP A 226 ? 0.2082 0.1921 0.2375 0.0000 -0.0137 0.0106 239 TRP A CD2 1749 N NE1 . TRP A 226 ? 0.2016 0.1837 0.2237 -0.0038 -0.0128 0.0077 239 TRP A NE1 1750 C CE2 . TRP A 226 ? 0.1993 0.1847 0.2262 -0.0023 -0.0141 0.0079 239 TRP A CE2 1751 C CE3 . TRP A 226 ? 0.2067 0.1939 0.2408 0.0013 -0.0148 0.0113 239 TRP A CE3 1752 C CZ2 . TRP A 226 ? 0.2039 0.1934 0.2330 -0.0028 -0.0156 0.0061 239 TRP A CZ2 1753 C CZ3 . TRP A 226 ? 0.2267 0.2173 0.2624 0.0003 -0.0164 0.0095 239 TRP A CZ3 1754 C CH2 . TRP A 226 ? 0.1906 0.1820 0.2237 -0.0013 -0.0168 0.0070 239 TRP A CH2 1755 N N . ASP A 227 ? 0.2337 0.2023 0.2615 0.0095 -0.0066 0.0181 240 ASP A N 1756 C CA . ASP A 227 ? 0.2923 0.2600 0.3221 0.0134 -0.0057 0.0206 240 ASP A CA 1757 C C . ASP A 227 ? 0.2747 0.2474 0.3103 0.0148 -0.0056 0.0207 240 ASP A C 1758 O O . ASP A 227 ? 0.2562 0.2335 0.2962 0.0172 -0.0065 0.0227 240 ASP A O 1759 C CB . ASP A 227 ? 0.2788 0.2380 0.3031 0.0148 -0.0029 0.0210 240 ASP A CB 1760 C CG . ASP A 227 ? 0.3165 0.2701 0.3348 0.0143 -0.0031 0.0221 240 ASP A CG 1761 O OD1 . ASP A 227 ? 0.3921 0.3376 0.4042 0.0139 -0.0010 0.0217 240 ASP A OD1 1762 O OD2 . ASP A 227 ? 0.3369 0.2936 0.3561 0.0139 -0.0054 0.0232 240 ASP A OD2 1763 N N . VAL A 228 ? 0.2433 0.2157 0.2789 0.0132 -0.0045 0.0185 241 VAL A N 1764 C CA . VAL A 228 ? 0.2298 0.2064 0.2703 0.0140 -0.0043 0.0184 241 VAL A CA 1765 C C . VAL A 228 ? 0.2240 0.2076 0.2691 0.0131 -0.0071 0.0187 241 VAL A C 1766 O O . VAL A 228 ? 0.2205 0.2087 0.2701 0.0146 -0.0075 0.0201 241 VAL A O 1767 C CB . VAL A 228 ? 0.2067 0.1811 0.2456 0.0122 -0.0028 0.0160 241 VAL A CB 1768 C CG1 . VAL A 228 ? 0.2258 0.2047 0.2694 0.0124 -0.0029 0.0158 241 VAL A CG1 1769 C CG2 . VAL A 228 ? 0.2282 0.1956 0.2625 0.0130 0.0001 0.0158 241 VAL A CG2 1770 N N . VAL A 229 ? 0.2248 0.2093 0.2686 0.0105 -0.0089 0.0172 242 VAL A N 1771 C CA . VAL A 229 ? 0.2197 0.2097 0.2667 0.0093 -0.0115 0.0172 242 VAL A CA 1772 C C . VAL A 229 ? 0.2325 0.2261 0.2820 0.0108 -0.0130 0.0198 242 VAL A C 1773 O O . VAL A 229 ? 0.2215 0.2201 0.2752 0.0111 -0.0140 0.0209 242 VAL A O 1774 C CB . VAL A 229 ? 0.1770 0.1669 0.2214 0.0066 -0.0130 0.0150 242 VAL A CB 1775 C CG1 . VAL A 229 ? 0.2054 0.2000 0.2524 0.0055 -0.0157 0.0150 242 VAL A CG1 1776 C CG2 . VAL A 229 ? 0.2018 0.1895 0.2442 0.0052 -0.0119 0.0124 242 VAL A CG2 1777 N N . ARG A 230 ? 0.2386 0.2297 0.2854 0.0116 -0.0130 0.0210 243 ARG A N 1778 C CA . ARG A 230 ? 0.2834 0.2779 0.3322 0.0132 -0.0145 0.0237 243 ARG A CA 1779 C C . ARG A 230 ? 0.3031 0.3006 0.3559 0.0164 -0.0135 0.0260 243 ARG A C 1780 O O . ARG A 230 ? 0.2865 0.2903 0.3434 0.0170 -0.0152 0.0277 243 ARG A O 1781 C CB . ARG A 230 ? 0.3466 0.3363 0.3908 0.0137 -0.0142 0.0246 243 ARG A CB 1782 C CG . ARG A 230 ? 0.3522 0.3451 0.3979 0.0155 -0.0159 0.0276 243 ARG A CG 1783 C CD . ARG A 230 ? 0.4417 0.4292 0.4820 0.0156 -0.0159 0.0284 243 ARG A CD 1784 N NE . ARG A 230 ? 0.4649 0.4445 0.5004 0.0164 -0.0132 0.0277 243 ARG A NE 1785 C CZ . ARG A 230 ? 0.5461 0.5222 0.5811 0.0200 -0.0112 0.0293 243 ARG A CZ 1786 N NH1 . ARG A 230 ? 0.4964 0.4644 0.5260 0.0200 -0.0088 0.0283 243 ARG A NH1 1787 N NH2 . ARG A 230 ? 0.5249 0.5054 0.5644 0.0235 -0.0116 0.0317 243 ARG A NH2 1788 N N . ARG A 231 ? 0.2971 0.2903 0.3486 0.0184 -0.0108 0.0258 244 ARG A N 1789 C CA . ARG A 231 ? 0.3750 0.3704 0.4298 0.0218 -0.0092 0.0274 244 ARG A CA 1790 C C . ARG A 231 ? 0.3072 0.3103 0.3677 0.0210 -0.0102 0.0277 244 ARG A C 1791 O O . ARG A 231 ? 0.3084 0.3169 0.3729 0.0235 -0.0103 0.0298 244 ARG A O 1792 C CB . ARG A 231 ? 0.4095 0.3984 0.4613 0.0225 -0.0061 0.0260 244 ARG A CB 1793 C CG . ARG A 231 ? 0.5383 0.5258 0.5907 0.0267 -0.0037 0.0276 244 ARG A CG 1794 C CD . ARG A 231 ? 0.4755 0.4534 0.5217 0.0271 -0.0010 0.0263 244 ARG A CD 1795 N NE . ARG A 231 ? 0.4577 0.4340 0.5034 0.0254 0.0007 0.0241 244 ARG A NE 1796 C CZ . ARG A 231 ? 0.4026 0.3714 0.4428 0.0239 0.0026 0.0222 244 ARG A CZ 1797 N NH1 . ARG A 231 ? 0.4233 0.3854 0.4577 0.0235 0.0030 0.0223 244 ARG A NH1 1798 N NH2 . ARG A 231 ? 0.3122 0.2803 0.3524 0.0225 0.0041 0.0204 244 ARG A NH2 1799 N N . SER A 232 ? 0.2581 0.2616 0.3187 0.0177 -0.0109 0.0254 245 SER A N 1800 C CA . SER A 232 ? 0.3035 0.3132 0.3683 0.0164 -0.0119 0.0255 245 SER A CA 1801 C C . SER A 232 ? 0.3530 0.3661 0.4184 0.0132 -0.0150 0.0250 245 SER A C 1802 O O . SER A 232 ? 0.4516 0.4664 0.5179 0.0108 -0.0159 0.0238 245 SER A O 1803 C CB . SER A 232 ? 0.3963 0.4033 0.4604 0.0153 -0.0102 0.0234 245 SER A CB 1804 O OG . SER A 232 ? 0.3775 0.3829 0.4420 0.0182 -0.0074 0.0241 245 SER A OG 1805 N N . SER A 233 ? 0.3004 0.3141 0.3648 0.0133 -0.0166 0.0261 246 SER A N 1806 C CA . SER A 233 ? 0.4194 0.4362 0.4839 0.0104 -0.0195 0.0258 246 SER A CA 1807 C C . SER A 233 ? 0.6111 0.6341 0.6785 0.0113 -0.0212 0.0287 246 SER A C 1808 O O . SER A 233 ? 0.6821 0.7085 0.7525 0.0142 -0.0203 0.0309 246 SER A O 1809 C CB . SER A 233 ? 0.4461 0.4580 0.5061 0.0087 -0.0201 0.0238 246 SER A CB 1810 O OG . SER A 233 ? 0.3550 0.3627 0.4128 0.0076 -0.0189 0.0211 246 SER A OG # 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 ILE 1 16 16 ILE ILE A . n A 1 2 ILE 2 17 17 ILE ILE A . n A 1 3 GLY 3 18 18 GLY GLY A . n A 1 4 GLY 4 19 19 GLY GLY A . n A 1 5 HIS 5 20 20 HIS HIS A . n A 1 6 GLU 6 21 21 GLU GLU A . n A 1 7 VAL 7 22 22 VAL VAL A . n A 1 8 THR 8 23 23 THR THR A . n A 1 9 PRO 9 24 24 PRO PRO A . n A 1 10 HIS 10 25 25 HIS HIS A . n A 1 11 SER 11 26 26 SER SER A . n A 1 12 ARG 12 27 27 ARG ARG A . n A 1 13 PRO 13 28 28 PRO PRO A . n A 1 14 TYR 14 29 29 TYR TYR A . n A 1 15 MET 15 30 30 MET MET A . n A 1 16 ALA 16 31 31 ALA ALA A . n A 1 17 SER 17 32 32 SER SER A . n A 1 18 VAL 18 33 33 VAL VAL A . n A 1 19 ARG 19 34 34 ARG ARG A . n A 1 20 PHE 20 35 35 PHE PHE A . n A 1 21 GLY 21 36 36 GLY GLY A . n A 1 22 GLY 22 38 38 GLY GLY A . n A 1 23 GLN 23 39 39 GLN GLN A . n A 1 24 HIS 24 40 40 HIS HIS A . n A 1 25 HIS 25 41 41 HIS HIS A . n A 1 26 CYS 26 42 42 CYS CYS A . n A 1 27 GLY 27 43 43 GLY GLY A . n A 1 28 GLY 28 44 44 GLY GLY A . n A 1 29 PHE 29 45 45 PHE PHE A . n A 1 30 LEU 30 46 46 LEU LEU A . n A 1 31 LEU 31 47 47 LEU LEU A . n A 1 32 ARG 32 48 48 ARG ARG A . n A 1 33 ALA 33 49 49 ALA ALA A . n A 1 34 ARG 34 50 50 ARG ARG A . n A 1 35 TRP 35 51 51 TRP TRP A . n A 1 36 VAL 36 52 52 VAL VAL A . n A 1 37 VAL 37 53 53 VAL VAL A . n A 1 38 SER 38 54 54 SER SER A . n A 1 39 ALA 39 55 55 ALA ALA A . n A 1 40 ALA 40 56 56 ALA ALA A . n A 1 41 HIS 41 57 57 HIS HIS A . n A 1 42 CYS 42 58 58 CYS CYS A . n A 1 43 PHE 43 59 59 PHE PHE A . n A 1 44 SER 44 60 60 SER SER A . n A 1 45 HIS 45 61 61 HIS HIS A . n A 1 46 ARG 46 62 62 ARG ARG A . n A 1 47 ASP 47 62 62 ASP ASP A A n A 1 48 LEU 48 62 62 LEU LEU A B n A 1 49 ARG 49 62 62 ARG ARG A C n A 1 50 THR 50 63 63 THR THR A . n A 1 51 GLY 51 64 64 GLY GLY A . n A 1 52 LEU 52 65 65 LEU LEU A . n A 1 53 VAL 53 66 66 VAL VAL A . n A 1 54 VAL 54 67 67 VAL VAL A . n A 1 55 LEU 55 68 68 LEU LEU A . n A 1 56 GLY 56 69 69 GLY GLY A . n A 1 57 ALA 57 70 70 ALA ALA A . n A 1 58 HIS 58 71 71 HIS HIS A . n A 1 59 VAL 59 72 72 VAL VAL A . n A 1 60 LEU 60 73 73 LEU LEU A . n A 1 61 SER 61 74 74 SER SER A . n A 1 62 THR 62 75 75 THR THR A . n A 1 63 ALA 63 76 76 ALA ALA A . n A 1 64 GLU 64 77 77 GLU GLU A . n A 1 65 PRO 65 78 78 PRO PRO A . n A 1 66 THR 66 79 79 THR THR A . n A 1 67 GLN 67 80 80 GLN GLN A . n A 1 68 GLN 68 81 81 GLN GLN A . n A 1 69 VAL 69 82 82 VAL VAL A . n A 1 70 PHE 70 83 83 PHE PHE A . n A 1 71 GLY 71 84 84 GLY GLY A . n A 1 72 ILE 72 85 85 ILE ILE A . n A 1 73 ASP 73 86 86 ASP ASP A . n A 1 74 ALA 74 87 87 ALA ALA A . n A 1 75 LEU 75 88 88 LEU LEU A . n A 1 76 THR 76 89 89 THR THR A . n A 1 77 THR 77 90 90 THR THR A . n A 1 78 HIS 78 91 91 HIS HIS A . n A 1 79 PRO 79 92 92 PRO PRO A . n A 1 80 ASP 80 93 93 ASP ASP A . n A 1 81 TYR 81 94 94 TYR TYR A . n A 1 82 HIS 82 95 95 HIS HIS A . n A 1 83 PRO 83 96 96 PRO PRO A . n A 1 84 MET 84 97 97 MET MET A . n A 1 85 THR 85 98 98 THR THR A . n A 1 86 HIS 86 99 99 HIS HIS A . n A 1 87 ALA 87 100 100 ALA ALA A . n A 1 88 ASN 88 101 101 ASN ASN A . n A 1 89 ASP 89 102 102 ASP ASP A . n A 1 90 ILE 90 103 103 ILE ILE A . n A 1 91 CYS 91 104 104 CYS CYS A . n A 1 92 LEU 92 105 105 LEU LEU A . n A 1 93 LEU 93 106 106 LEU LEU A . n A 1 94 ARG 94 107 107 ARG ARG A . n A 1 95 LEU 95 108 108 LEU LEU A . n A 1 96 ASN 96 109 109 ASN ASN A . n A 1 97 GLY 97 110 110 GLY GLY A . n A 1 98 SER 98 111 111 SER SER A . n A 1 99 ALA 99 112 112 ALA ALA A . n A 1 100 VAL 100 113 113 VAL VAL A . n A 1 101 LEU 101 114 114 LEU LEU A . n A 1 102 GLY 102 115 115 GLY GLY A . n A 1 103 PRO 103 116 116 PRO PRO A . n A 1 104 ALA 104 117 117 ALA ALA A . n A 1 105 VAL 105 118 118 VAL VAL A . n A 1 106 GLY 106 119 119 GLY GLY A . n A 1 107 LEU 107 120 120 LEU LEU A . n A 1 108 LEU 108 121 121 LEU LEU A . n A 1 109 ARG 109 122 122 ARG ARG A . n A 1 110 LEU 110 123 123 LEU LEU A . n A 1 111 PRO 111 124 124 PRO PRO A . n A 1 112 GLY 112 124 124 GLY GLY A A n A 1 113 ARG 113 125 125 ARG ARG A . n A 1 114 ARG 114 126 126 ARG ARG A . n A 1 115 ALA 115 127 127 ALA ALA A . n A 1 116 ARG 116 128 128 ARG ARG A . n A 1 117 PRO 117 129 129 PRO PRO A . n A 1 118 PRO 118 130 130 PRO PRO A . n A 1 119 THR 119 131 131 THR THR A . n A 1 120 ALA 120 132 132 ALA ALA A . n A 1 121 GLY 121 133 133 GLY GLY A . n A 1 122 THR 122 134 134 THR THR A . n A 1 123 ARG 123 135 135 ARG ARG A . n A 1 124 CYS 124 136 136 CYS CYS A . n A 1 125 ARG 125 137 137 ARG ARG A . n A 1 126 VAL 126 138 138 VAL VAL A . n A 1 127 ALA 127 139 139 ALA ALA A . n A 1 128 GLY 128 140 140 GLY GLY A . n A 1 129 TRP 129 141 141 TRP TRP A . n A 1 130 GLY 130 142 142 GLY GLY A . n A 1 131 PHE 131 143 143 PHE PHE A . n A 1 132 VAL 132 144 144 VAL VAL A . n A 1 133 SER 133 145 145 SER SER A . n A 1 134 ASP 134 147 147 ASP ASP A . n A 1 135 PHE 135 148 148 PHE PHE A . n A 1 136 GLU 136 149 149 GLU GLU A . n A 1 137 GLU 137 150 150 GLU GLU A . n A 1 138 LEU 138 151 151 LEU LEU A . n A 1 139 PRO 139 152 152 PRO PRO A . n A 1 140 PRO 140 153 153 PRO PRO A . n A 1 141 GLY 141 154 154 GLY GLY A . n A 1 142 LEU 142 155 155 LEU LEU A . n A 1 143 MET 143 156 156 MET MET A . n A 1 144 GLU 144 157 157 GLU GLU A . n A 1 145 ALA 145 158 158 ALA ALA A . n A 1 146 LYS 146 159 159 LYS LYS A . n A 1 147 VAL 147 160 160 VAL VAL A . n A 1 148 ARG 148 161 161 ARG ARG A . n A 1 149 VAL 149 162 162 VAL VAL A . n A 1 150 LEU 150 163 163 LEU LEU A . n A 1 151 ASP 151 164 164 ASP ASP A . n A 1 152 PRO 152 165 165 PRO PRO A . n A 1 153 ASP 153 166 166 ASP ASP A . n A 1 154 VAL 154 167 167 VAL VAL A . n A 1 155 CYS 155 168 168 CYS CYS A . n A 1 156 ASN 156 169 169 ASN ASN A . n A 1 157 SER 157 170 170 SER SER A . n A 1 158 SER 158 171 171 SER SER A . n A 1 159 TRP 159 172 172 TRP TRP A . n A 1 160 LYS 160 173 173 LYS LYS A . n A 1 161 GLY 161 174 174 GLY GLY A . n A 1 162 HIS 162 175 175 HIS HIS A . n A 1 163 LEU 163 176 176 LEU LEU A . n A 1 164 THR 164 177 177 THR THR A . n A 1 165 LEU 165 178 178 LEU LEU A . n A 1 166 THR 166 179 179 THR THR A . n A 1 167 MET 167 180 180 MET MET A . n A 1 168 LEU 168 181 181 LEU LEU A . n A 1 169 CYS 169 182 182 CYS CYS A . n A 1 170 THR 170 183 183 THR THR A . n A 1 171 ARG 171 184 184 ARG ARG A . n A 1 172 SER 172 185 185 SER SER A . n A 1 173 GLY 173 186 186 GLY GLY A . n A 1 174 ASP 174 186 186 ASP ASP A A n A 1 175 SER 175 186 186 SER SER A B n A 1 176 HIS 176 187 187 HIS HIS A . n A 1 177 ARG 177 188 188 ARG ARG A . n A 1 178 ARG 178 188 188 ARG ARG A A n A 1 179 GLY 179 189 189 GLY GLY A . n A 1 180 PHE 180 190 190 PHE PHE A . n A 1 181 CYS 181 191 191 CYS CYS A . n A 1 182 SER 182 192 192 SER SER A . n A 1 183 ALA 183 193 193 ALA ALA A . n A 1 184 ASP 184 194 194 ASP ASP A . n A 1 185 SER 185 195 195 SER SER A . n A 1 186 GLY 186 196 196 GLY GLY A . n A 1 187 GLY 187 197 197 GLY GLY A . n A 1 188 PRO 188 198 198 PRO PRO A . n A 1 189 LEU 189 199 199 LEU LEU A . n A 1 190 VAL 190 200 200 VAL VAL A . n A 1 191 CYS 191 201 201 CYS CYS A . n A 1 192 ARG 192 202 202 ARG ARG A . n A 1 193 ASN 193 207 207 ASN ASN A . n A 1 194 ARG 194 208 208 ARG ARG A . n A 1 195 ALA 195 209 209 ALA ALA A . n A 1 196 HIS 196 210 210 HIS HIS A . n A 1 197 GLY 197 211 211 GLY GLY A . n A 1 198 LEU 198 212 212 LEU LEU A . n A 1 199 VAL 199 213 213 VAL VAL A . n A 1 200 SER 200 214 214 SER SER A . n A 1 201 PHE 201 215 215 PHE PHE A . n A 1 202 SER 202 216 216 SER SER A . n A 1 203 GLY 203 217 217 GLY GLY A . n A 1 204 LEU 204 218 218 LEU LEU A . n A 1 205 TRP 205 219 219 TRP TRP A . n A 1 206 CYS 206 220 220 CYS CYS A . n A 1 207 GLY 207 221 221 GLY GLY A . n A 1 208 ASP 208 222 222 ASP ASP A . n A 1 209 PRO 209 222 222 PRO PRO A A n A 1 210 LYS 210 223 223 LYS LYS A . n A 1 211 THR 211 224 224 THR THR A . n A 1 212 PRO 212 225 225 PRO PRO A . n A 1 213 ASP 213 226 226 ASP ASP A . n A 1 214 VAL 214 227 227 VAL VAL A . n A 1 215 TYR 215 228 228 TYR TYR A . n A 1 216 THR 216 229 229 THR THR A . n A 1 217 GLN 217 230 230 GLN GLN A . n A 1 218 VAL 218 231 231 VAL VAL A . n A 1 219 SER 219 232 232 SER SER A . n A 1 220 ALA 220 233 233 ALA ALA A . n A 1 221 PHE 221 234 234 PHE PHE A . n A 1 222 VAL 222 235 235 VAL VAL A . n A 1 223 ALA 223 236 236 ALA ALA A . n A 1 224 TRP 224 237 237 TRP TRP A . n A 1 225 ILE 225 238 238 ILE ILE A . n A 1 226 TRP 226 239 239 TRP TRP A . n A 1 227 ASP 227 240 240 ASP ASP A . n A 1 228 VAL 228 241 241 VAL VAL A . n A 1 229 VAL 229 242 242 VAL VAL A . n A 1 230 ARG 230 243 243 ARG ARG A . n A 1 231 ARG 231 244 244 ARG ARG A . n A 1 232 SER 232 245 245 SER SER A . n A 1 233 SER 233 246 246 SER SER A . n A 1 234 PRO 234 247 ? ? ? A . n A 1 235 GLN 235 248 ? ? ? A . n A 1 236 PRO 236 249 ? ? ? A . n A 1 237 GLY 237 250 ? ? ? A . n A 1 238 PRO 238 251 ? ? ? A . n A 1 239 LEU 239 252 ? ? ? A . n A 1 240 PRO 240 253 ? ? ? A . n A 1 241 GLY 241 254 ? ? ? A . n A 1 242 THR 242 255 ? ? ? A . n A 1 243 THR 243 256 ? ? ? A . n A 1 244 ARG 244 257 ? ? ? A . n A 1 245 PRO 245 258 ? ? ? A . n A 1 246 PRO 246 259 ? ? ? A . n A 1 247 GLY 247 260 ? ? ? A . n A 1 248 GLU 248 261 ? ? ? A . n A 1 249 ALA 249 262 ? ? ? A . n A 1 250 ALA 250 263 ? ? ? A . 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 B 2 NAG 1 301 896 NAG NAG A . C 2 NAG 1 302 956 NAG NAG A . D 3 FUC 2 303 957 FUC FUC A . E 4 2YT 1 304 1 2YT DRG A . F 5 GOL 1 305 401 GOL GOL A . G 6 CL 1 306 402 CL CL A . H 7 HOH 1 401 1 HOH HOH A . H 7 HOH 2 402 2 HOH HOH A . H 7 HOH 3 403 4 HOH HOH A . H 7 HOH 4 404 5 HOH HOH A . H 7 HOH 5 405 6 HOH HOH A . H 7 HOH 6 406 7 HOH HOH A . H 7 HOH 7 407 8 HOH HOH A . H 7 HOH 8 408 9 HOH HOH A . H 7 HOH 9 409 10 HOH HOH A . H 7 HOH 10 410 11 HOH HOH A . H 7 HOH 11 411 12 HOH HOH A . H 7 HOH 12 412 13 HOH HOH A . H 7 HOH 13 413 14 HOH HOH A . H 7 HOH 14 414 15 HOH HOH A . H 7 HOH 15 415 16 HOH HOH A . H 7 HOH 16 416 17 HOH HOH A . H 7 HOH 17 417 18 HOH HOH A . H 7 HOH 18 418 19 HOH HOH A . H 7 HOH 19 419 20 HOH HOH A . H 7 HOH 20 420 21 HOH HOH A . H 7 HOH 21 421 22 HOH HOH A . H 7 HOH 22 422 23 HOH HOH A . H 7 HOH 23 423 24 HOH HOH A . H 7 HOH 24 424 25 HOH HOH A . H 7 HOH 25 425 26 HOH HOH A . H 7 HOH 26 426 27 HOH HOH A . H 7 HOH 27 427 28 HOH HOH A . H 7 HOH 28 428 29 HOH HOH A . H 7 HOH 29 429 30 HOH HOH A . H 7 HOH 30 430 31 HOH HOH A . H 7 HOH 31 431 32 HOH HOH A . H 7 HOH 32 432 33 HOH HOH A . H 7 HOH 33 433 34 HOH HOH A . H 7 HOH 34 434 35 HOH HOH A . H 7 HOH 35 435 36 HOH HOH A . H 7 HOH 36 436 37 HOH HOH A . H 7 HOH 37 437 38 HOH HOH A . H 7 HOH 38 438 39 HOH HOH A . H 7 HOH 39 439 40 HOH HOH A . H 7 HOH 40 440 41 HOH HOH A . H 7 HOH 41 441 42 HOH HOH A . H 7 HOH 42 442 43 HOH HOH A . H 7 HOH 43 443 44 HOH HOH A . H 7 HOH 44 444 46 HOH HOH A . H 7 HOH 45 445 47 HOH HOH A . H 7 HOH 46 446 48 HOH HOH A . H 7 HOH 47 447 49 HOH HOH A . H 7 HOH 48 448 50 HOH HOH A . H 7 HOH 49 449 51 HOH HOH A . H 7 HOH 50 450 52 HOH HOH A . H 7 HOH 51 451 53 HOH HOH A . H 7 HOH 52 452 54 HOH HOH A . H 7 HOH 53 453 55 HOH HOH A . H 7 HOH 54 454 57 HOH HOH A . H 7 HOH 55 455 58 HOH HOH A . H 7 HOH 56 456 59 HOH HOH A . H 7 HOH 57 457 60 HOH HOH A . H 7 HOH 58 458 61 HOH HOH A . H 7 HOH 59 459 62 HOH HOH A . H 7 HOH 60 460 64 HOH HOH A . H 7 HOH 61 461 65 HOH HOH A . H 7 HOH 62 462 66 HOH HOH A . H 7 HOH 63 463 67 HOH HOH A . H 7 HOH 64 464 68 HOH HOH A . H 7 HOH 65 465 69 HOH HOH A . H 7 HOH 66 466 70 HOH HOH A . H 7 HOH 67 467 71 HOH HOH A . H 7 HOH 68 468 72 HOH HOH A . H 7 HOH 69 469 73 HOH HOH A . H 7 HOH 70 470 74 HOH HOH A . H 7 HOH 71 471 75 HOH HOH A . H 7 HOH 72 472 76 HOH HOH A . H 7 HOH 73 473 77 HOH HOH A . H 7 HOH 74 474 78 HOH HOH A . H 7 HOH 75 475 79 HOH HOH A . H 7 HOH 76 476 80 HOH HOH A . H 7 HOH 77 477 81 HOH HOH A . H 7 HOH 78 478 82 HOH HOH A . H 7 HOH 79 479 83 HOH HOH A . H 7 HOH 80 480 84 HOH HOH A . H 7 HOH 81 481 85 HOH HOH A . H 7 HOH 82 482 86 HOH HOH A . H 7 HOH 83 483 87 HOH HOH A . H 7 HOH 84 484 88 HOH HOH A . H 7 HOH 85 485 89 HOH HOH A . H 7 HOH 86 486 90 HOH HOH A . H 7 HOH 87 487 91 HOH HOH A . H 7 HOH 88 488 92 HOH HOH A . H 7 HOH 89 489 93 HOH HOH A . H 7 HOH 90 490 94 HOH HOH A . H 7 HOH 91 491 95 HOH HOH A . H 7 HOH 92 492 96 HOH HOH A . H 7 HOH 93 493 98 HOH HOH A . H 7 HOH 94 494 100 HOH HOH A . H 7 HOH 95 495 101 HOH HOH A . H 7 HOH 96 496 102 HOH HOH A . H 7 HOH 97 497 103 HOH HOH A . H 7 HOH 98 498 104 HOH HOH A . H 7 HOH 99 499 105 HOH HOH A . H 7 HOH 100 500 106 HOH HOH A . H 7 HOH 101 501 107 HOH HOH A . H 7 HOH 102 502 108 HOH HOH A . H 7 HOH 103 503 109 HOH HOH A . H 7 HOH 104 504 110 HOH HOH A . H 7 HOH 105 505 111 HOH HOH A . H 7 HOH 106 506 113 HOH HOH A . H 7 HOH 107 507 114 HOH HOH A . H 7 HOH 108 508 115 HOH HOH A . H 7 HOH 109 509 116 HOH HOH A . H 7 HOH 110 510 118 HOH HOH A . H 7 HOH 111 511 119 HOH HOH A . H 7 HOH 112 512 120 HOH HOH A . H 7 HOH 113 513 121 HOH HOH A . H 7 HOH 114 514 122 HOH HOH A . H 7 HOH 115 515 124 HOH HOH A . H 7 HOH 116 516 125 HOH HOH A . H 7 HOH 117 517 126 HOH HOH A . H 7 HOH 118 518 127 HOH HOH A . H 7 HOH 119 519 128 HOH HOH A . H 7 HOH 120 520 129 HOH HOH A . H 7 HOH 121 521 131 HOH HOH A . H 7 HOH 122 522 132 HOH HOH A . H 7 HOH 123 523 133 HOH HOH A . H 7 HOH 124 524 134 HOH HOH A . H 7 HOH 125 525 135 HOH HOH A . H 7 HOH 126 526 136 HOH HOH A . H 7 HOH 127 527 137 HOH HOH A . H 7 HOH 128 528 138 HOH HOH A . H 7 HOH 129 529 139 HOH HOH A . H 7 HOH 130 530 141 HOH HOH A . H 7 HOH 131 531 143 HOH HOH A . H 7 HOH 132 532 145 HOH HOH A . H 7 HOH 133 533 146 HOH HOH A . H 7 HOH 134 534 147 HOH HOH A . H 7 HOH 135 535 149 HOH HOH A . H 7 HOH 136 536 151 HOH HOH A . H 7 HOH 137 537 152 HOH HOH A . H 7 HOH 138 538 153 HOH HOH A . H 7 HOH 139 539 154 HOH HOH A . H 7 HOH 140 540 155 HOH HOH A . H 7 HOH 141 541 156 HOH HOH A . H 7 HOH 142 542 157 HOH HOH A . H 7 HOH 143 543 159 HOH HOH A . H 7 HOH 144 544 160 HOH HOH A . H 7 HOH 145 545 161 HOH HOH A . H 7 HOH 146 546 162 HOH HOH A . H 7 HOH 147 547 163 HOH HOH A . H 7 HOH 148 548 164 HOH HOH A . H 7 HOH 149 549 166 HOH HOH A . H 7 HOH 150 550 168 HOH HOH A . H 7 HOH 151 551 169 HOH HOH A . H 7 HOH 152 552 170 HOH HOH A . H 7 HOH 153 553 171 HOH HOH A . H 7 HOH 154 554 173 HOH HOH A . H 7 HOH 155 555 174 HOH HOH A . H 7 HOH 156 556 175 HOH HOH A . H 7 HOH 157 557 176 HOH HOH A . H 7 HOH 158 558 177 HOH HOH A . H 7 HOH 159 559 178 HOH HOH A . H 7 HOH 160 560 180 HOH HOH A . H 7 HOH 161 561 181 HOH HOH A . H 7 HOH 162 562 182 HOH HOH A . H 7 HOH 163 563 183 HOH HOH A . H 7 HOH 164 564 184 HOH HOH A . H 7 HOH 165 565 185 HOH HOH A . H 7 HOH 166 566 187 HOH HOH A . H 7 HOH 167 567 188 HOH HOH A . H 7 HOH 168 568 190 HOH HOH A . H 7 HOH 169 569 192 HOH HOH A . H 7 HOH 170 570 193 HOH HOH A . H 7 HOH 171 571 194 HOH HOH A . H 7 HOH 172 572 195 HOH HOH A . H 7 HOH 173 573 196 HOH HOH A . H 7 HOH 174 574 197 HOH HOH A . H 7 HOH 175 575 198 HOH HOH A . H 7 HOH 176 576 199 HOH HOH A . H 7 HOH 177 577 200 HOH HOH A . H 7 HOH 178 578 201 HOH HOH A . H 7 HOH 179 579 202 HOH HOH A . H 7 HOH 180 580 203 HOH HOH A . H 7 HOH 181 581 204 HOH HOH A . H 7 HOH 182 582 205 HOH HOH A . H 7 HOH 183 583 206 HOH HOH A . H 7 HOH 184 584 208 HOH HOH A . H 7 HOH 185 585 209 HOH HOH A . H 7 HOH 186 586 210 HOH HOH A . H 7 HOH 187 587 211 HOH HOH A . H 7 HOH 188 588 212 HOH HOH A . H 7 HOH 189 589 213 HOH HOH A . H 7 HOH 190 590 214 HOH HOH A . H 7 HOH 191 591 217 HOH HOH A . H 7 HOH 192 592 218 HOH HOH A . H 7 HOH 193 593 219 HOH HOH A . H 7 HOH 194 594 220 HOH HOH A . H 7 HOH 195 595 222 HOH HOH A . H 7 HOH 196 596 225 HOH HOH A . H 7 HOH 197 597 229 HOH HOH A . H 7 HOH 198 598 231 HOH HOH A . H 7 HOH 199 599 234 HOH HOH A . H 7 HOH 200 600 236 HOH HOH A . H 7 HOH 201 601 237 HOH HOH A . H 7 HOH 202 602 242 HOH HOH A . H 7 HOH 203 603 245 HOH HOH A . H 7 HOH 204 604 253 HOH HOH A . H 7 HOH 205 605 255 HOH HOH A . H 7 HOH 206 606 256 HOH HOH A . H 7 HOH 207 607 259 HOH HOH A . H 7 HOH 208 608 261 HOH HOH A . H 7 HOH 209 609 263 HOH HOH A . H 7 HOH 210 610 265 HOH HOH A . H 7 HOH 211 611 267 HOH HOH A . H 7 HOH 212 612 270 HOH HOH A . H 7 HOH 213 613 272 HOH HOH A . H 7 HOH 214 614 273 HOH HOH A . H 7 HOH 215 615 275 HOH HOH A . H 7 HOH 216 616 276 HOH HOH A . H 7 HOH 217 617 277 HOH HOH A . H 7 HOH 218 618 278 HOH HOH A . H 7 HOH 219 619 282 HOH HOH A . H 7 HOH 220 620 285 HOH HOH A . H 7 HOH 221 621 286 HOH HOH A . H 7 HOH 222 622 289 HOH HOH A . H 7 HOH 223 623 293 HOH HOH A . H 7 HOH 224 624 295 HOH HOH A . H 7 HOH 225 625 297 HOH HOH A . H 7 HOH 226 626 298 HOH HOH A . H 7 HOH 227 627 299 HOH HOH A . H 7 HOH 228 628 300 HOH HOH A . H 7 HOH 229 629 301 HOH HOH A . H 7 HOH 230 630 303 HOH HOH A . H 7 HOH 231 631 305 HOH HOH A . H 7 HOH 232 632 307 HOH HOH A . H 7 HOH 233 633 309 HOH HOH A . H 7 HOH 234 634 310 HOH HOH A . H 7 HOH 235 635 311 HOH HOH A . H 7 HOH 236 636 312 HOH HOH A . H 7 HOH 237 637 313 HOH HOH A . H 7 HOH 238 638 314 HOH HOH A . H 7 HOH 239 639 315 HOH HOH A . H 7 HOH 240 640 316 HOH HOH A . H 7 HOH 241 641 317 HOH HOH A . H 7 HOH 242 642 318 HOH HOH A . H 7 HOH 243 643 319 HOH HOH A . H 7 HOH 244 644 320 HOH HOH A . H 7 HOH 245 645 321 HOH HOH A . H 7 HOH 246 646 322 HOH HOH A . # _pdbx_molecule_features.prd_id PRD_001231 _pdbx_molecule_features.name PHE-PHE-ARG-chloromethylketone _pdbx_molecule_features.type Peptide-like _pdbx_molecule_features.class Inhibitor _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_001231 _pdbx_molecule.asym_id E # 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 A ASN 156 A ASN 169 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 96 A ASN 109 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,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 2014-09-03 2 'Structure model' 1 1 2014-09-17 3 'Structure model' 1 2 2017-11-22 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined -9.7268 6.8894 8.4884 0.0276 0.0161 0.0345 -0.0001 0.0059 -0.0025 0.2321 0.2202 0.4741 0.0290 0.0167 0.0254 -0.0096 -0.0325 0.0421 0.0145 0.0164 -0.0511 -0.0103 -0.0329 -0.0023 'X-RAY DIFFRACTION' 2 ? refined -5.0930 -1.3887 12.1689 0.0224 0.0201 0.0433 -0.0053 0.0072 0.0111 0.2458 0.2892 0.4099 -0.1062 0.1355 -0.0318 0.0065 -0.0539 0.0474 0.0113 -0.0073 -0.0642 0.0234 0.0342 0.0376 'X-RAY DIFFRACTION' 3 ? refined -20.8268 -7.0729 20.9746 0.0687 0.0647 0.0206 -0.0598 0.0194 -0.0076 1.0275 0.2780 1.4694 0.3494 0.0753 0.5080 0.0593 -0.1128 0.0535 -0.0786 -0.0961 -0.0167 0.0970 0.2515 -0.2934 'X-RAY DIFFRACTION' 4 ? refined -20.7200 -4.7757 9.0689 0.0324 0.0460 0.0369 -0.0225 -0.0014 -0.0151 0.1379 0.1291 0.6309 0.1060 -0.0046 -0.0127 -0.0370 -0.0154 0.0524 -0.0157 0.0072 -0.0332 -0.0134 0.0885 -0.1644 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 16 A 67 ? . . . . ? 'X-RAY DIFFRACTION' 2 2 A 68 A 110 ? . . . . ? 'X-RAY DIFFRACTION' 3 3 A 111 A 128 ? . . . . ? 'X-RAY DIFFRACTION' 4 4 A 129 A 233 ? . . . . ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal Blu-Ice 'data collection' Ice ? 1 REFMAC refinement 5.6.0117 ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 # _pdbx_entry_details.entry_id 4Q7Z _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'NATURAL VARIANT DESCRIBED IN THE UNIPROT ENTRY Q6UWY2' # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 O _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 GLY _pdbx_validate_close_contact.auth_seq_id_1 124 _pdbx_validate_close_contact.PDB_ins_code_1 A _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 526 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.18 # 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 HIS A 71 ? ? -122.06 -61.96 2 1 MET A 97 ? ? 54.06 8.19 3 1 ASP A 186 A ? -139.60 -159.39 4 1 SER A 214 ? ? -123.24 -68.21 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A PRO 247 ? A PRO 234 2 1 Y 1 A GLN 248 ? A GLN 235 3 1 Y 1 A PRO 249 ? A PRO 236 4 1 Y 1 A GLY 250 ? A GLY 237 5 1 Y 1 A PRO 251 ? A PRO 238 6 1 Y 1 A LEU 252 ? A LEU 239 7 1 Y 1 A PRO 253 ? A PRO 240 8 1 Y 1 A GLY 254 ? A GLY 241 9 1 Y 1 A THR 255 ? A THR 242 10 1 Y 1 A THR 256 ? A THR 243 11 1 Y 1 A ARG 257 ? A ARG 244 12 1 Y 1 A PRO 258 ? A PRO 245 13 1 Y 1 A PRO 259 ? A PRO 246 14 1 Y 1 A GLY 260 ? A GLY 247 15 1 Y 1 A GLU 261 ? A GLU 248 16 1 Y 1 A ALA 262 ? A ALA 249 17 1 Y 1 A ALA 263 ? A ALA 250 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-L-FUCOSE FUC 4 'L-phenylalanyl-N-[(2S,3S)-6-carbamimidamido-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide' 2YT 5 GLYCEROL GOL 6 'CHLORIDE ION' CL 7 water HOH #