data_4CWM # _entry.id 4CWM # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4CWM PDBE EBI-60229 WWPDB D_1290060229 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CWM _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2014-04-03 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Yu, T.-F.' 1 'Maestre-Reyna, M.' 2 'Ko, C.-Y.' 3 'Ko, T.-P.' 4 'Sun, Y.-J.' 5 'Lin, T.-Y.' 6 'Shaw, J.-F.' 7 'Wang, A.H.-J.' 8 # _citation.id primary _citation.title 'Structural Insights of the Ssdna Binding Site in the Multifunctional Endonuclease Atbfn2 from Arabidopsis Thaliana.' _citation.journal_abbrev 'Plos One' _citation.journal_volume 9 _citation.page_first 05821 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1932-6203 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 25157844 _citation.pdbx_database_id_DOI 10.1371/JOURNAL.PONE.0105821 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Yu, T.' 1 primary 'Maestre-Reyna, M.' 2 primary 'Ko, C.' 3 primary 'Ko, T.' 4 primary 'Sun, Y.' 5 primary 'Lin, T.' 6 primary 'Shaw, J.' 7 primary 'Wang, A.H.' 8 # _cell.entry_id 4CWM _cell.length_a 45.375 _cell.length_b 52.706 _cell.length_c 61.105 _cell.angle_alpha 71.34 _cell.angle_beta 78.57 _cell.angle_gamma 76.74 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4CWM _symmetry.space_group_name_H-M 'P 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 1 # 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 'ENDONUCLEASE 2' 30606.156 2 3.1.30.1 ? 'RESIDUES 28-290' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 12 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 4 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 4 ? ? ? ? 5 non-polymer syn 'ZINC ION' 65.409 6 ? ? ? ? 6 water nat water 18.015 457 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'ATENDO2, DEOXYRIBONUCLEASE ENDO2, SINGLE-STRANDED-NUCLEATE ENDONUCLEASE ENDO2, BIFUNCTIONAL ENDONUCLEASE ATBFN2' # _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 ;WGKEGHEIICKIAQTRLDETAAKAVKELLPESAEGDLSSLCLWADRVKFRYHWSSPLHYINTPDACSYQYNRDCKDESGE KGRCVAGAIYNYTTQLLSYKTAASSQSQYNLTEALLFVSHFMGDIHQPLHVSYASDKGGNTIEVHWYTRKANLHHIWDSN IIETAEADLYNSALEGMVDALKKNITTEWADQVKRWETCTKKTACPDIYASEGIQAACDWAYKGVTEGDTLEDEYFYSRL PIVYQRLAQGGVRLAATLNRIFGHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;WGKEGHEIICKIAQTRLDETAAKAVKELLPESAEGDLSSLCLWADRVKFRYHWSSPLHYINTPDACSYQYNRDCKDESGE KGRCVAGAIYNYTTQLLSYKTAASSQSQYNLTEALLFVSHFMGDIHQPLHVSYASDKGGNTIEVHWYTRKANLHHIWDSN IIETAEADLYNSALEGMVDALKKNITTEWADQVKRWETCTKKTACPDIYASEGIQAACDWAYKGVTEGDTLEDEYFYSRL PIVYQRLAQGGVRLAATLNRIFGHHHHHH ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 TRP n 1 2 GLY n 1 3 LYS n 1 4 GLU n 1 5 GLY n 1 6 HIS n 1 7 GLU n 1 8 ILE n 1 9 ILE n 1 10 CYS n 1 11 LYS n 1 12 ILE n 1 13 ALA n 1 14 GLN n 1 15 THR n 1 16 ARG n 1 17 LEU n 1 18 ASP n 1 19 GLU n 1 20 THR n 1 21 ALA n 1 22 ALA n 1 23 LYS n 1 24 ALA n 1 25 VAL n 1 26 LYS n 1 27 GLU n 1 28 LEU n 1 29 LEU n 1 30 PRO n 1 31 GLU n 1 32 SER n 1 33 ALA n 1 34 GLU n 1 35 GLY n 1 36 ASP n 1 37 LEU n 1 38 SER n 1 39 SER n 1 40 LEU n 1 41 CYS n 1 42 LEU n 1 43 TRP n 1 44 ALA n 1 45 ASP n 1 46 ARG n 1 47 VAL n 1 48 LYS n 1 49 PHE n 1 50 ARG n 1 51 TYR n 1 52 HIS n 1 53 TRP n 1 54 SER n 1 55 SER n 1 56 PRO n 1 57 LEU n 1 58 HIS n 1 59 TYR n 1 60 ILE n 1 61 ASN n 1 62 THR n 1 63 PRO n 1 64 ASP n 1 65 ALA n 1 66 CYS n 1 67 SER n 1 68 TYR n 1 69 GLN n 1 70 TYR n 1 71 ASN n 1 72 ARG n 1 73 ASP n 1 74 CYS n 1 75 LYS n 1 76 ASP n 1 77 GLU n 1 78 SER n 1 79 GLY n 1 80 GLU n 1 81 LYS n 1 82 GLY n 1 83 ARG n 1 84 CYS n 1 85 VAL n 1 86 ALA n 1 87 GLY n 1 88 ALA n 1 89 ILE n 1 90 TYR n 1 91 ASN n 1 92 TYR n 1 93 THR n 1 94 THR n 1 95 GLN n 1 96 LEU n 1 97 LEU n 1 98 SER n 1 99 TYR n 1 100 LYS n 1 101 THR n 1 102 ALA n 1 103 ALA n 1 104 SER n 1 105 SER n 1 106 GLN n 1 107 SER n 1 108 GLN n 1 109 TYR n 1 110 ASN n 1 111 LEU n 1 112 THR n 1 113 GLU n 1 114 ALA n 1 115 LEU n 1 116 LEU n 1 117 PHE n 1 118 VAL n 1 119 SER n 1 120 HIS n 1 121 PHE n 1 122 MET n 1 123 GLY n 1 124 ASP n 1 125 ILE n 1 126 HIS n 1 127 GLN n 1 128 PRO n 1 129 LEU n 1 130 HIS n 1 131 VAL n 1 132 SER n 1 133 TYR n 1 134 ALA n 1 135 SER n 1 136 ASP n 1 137 LYS n 1 138 GLY n 1 139 GLY n 1 140 ASN n 1 141 THR n 1 142 ILE n 1 143 GLU n 1 144 VAL n 1 145 HIS n 1 146 TRP n 1 147 TYR n 1 148 THR n 1 149 ARG n 1 150 LYS n 1 151 ALA n 1 152 ASN n 1 153 LEU n 1 154 HIS n 1 155 HIS n 1 156 ILE n 1 157 TRP n 1 158 ASP n 1 159 SER n 1 160 ASN n 1 161 ILE n 1 162 ILE n 1 163 GLU n 1 164 THR n 1 165 ALA n 1 166 GLU n 1 167 ALA n 1 168 ASP n 1 169 LEU n 1 170 TYR n 1 171 ASN n 1 172 SER n 1 173 ALA n 1 174 LEU n 1 175 GLU n 1 176 GLY n 1 177 MET n 1 178 VAL n 1 179 ASP n 1 180 ALA n 1 181 LEU n 1 182 LYS n 1 183 LYS n 1 184 ASN n 1 185 ILE n 1 186 THR n 1 187 THR n 1 188 GLU n 1 189 TRP n 1 190 ALA n 1 191 ASP n 1 192 GLN n 1 193 VAL n 1 194 LYS n 1 195 ARG n 1 196 TRP n 1 197 GLU n 1 198 THR n 1 199 CYS n 1 200 THR n 1 201 LYS n 1 202 LYS n 1 203 THR n 1 204 ALA n 1 205 CYS n 1 206 PRO n 1 207 ASP n 1 208 ILE n 1 209 TYR n 1 210 ALA n 1 211 SER n 1 212 GLU n 1 213 GLY n 1 214 ILE n 1 215 GLN n 1 216 ALA n 1 217 ALA n 1 218 CYS n 1 219 ASP n 1 220 TRP n 1 221 ALA n 1 222 TYR n 1 223 LYS n 1 224 GLY n 1 225 VAL n 1 226 THR n 1 227 GLU n 1 228 GLY n 1 229 ASP n 1 230 THR n 1 231 LEU n 1 232 GLU n 1 233 ASP n 1 234 GLU n 1 235 TYR n 1 236 PHE n 1 237 TYR n 1 238 SER n 1 239 ARG n 1 240 LEU n 1 241 PRO n 1 242 ILE n 1 243 VAL n 1 244 TYR n 1 245 GLN n 1 246 ARG n 1 247 LEU n 1 248 ALA n 1 249 GLN n 1 250 GLY n 1 251 GLY n 1 252 VAL n 1 253 ARG n 1 254 LEU n 1 255 ALA n 1 256 ALA n 1 257 THR n 1 258 LEU n 1 259 ASN n 1 260 ARG n 1 261 ILE n 1 262 PHE n 1 263 GLY n 1 264 HIS n 1 265 HIS n 1 266 HIS n 1 267 HIS n 1 268 HIS n 1 269 HIS 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 'THALE CRESS' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _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 'ARABIDOPSIS THALIANA' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 3702 _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 'THALE CRESS' _entity_src_gen.pdbx_host_org_scientific_name 'ARABIDOPSIS THALIANA' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 3702 _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 ENDO2_ARATH _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q9C9G4 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4CWM A 1 ? 263 ? Q9C9G4 28 ? 290 ? 1 263 2 1 4CWM B 1 ? 263 ? Q9C9G4 28 ? 290 ? 1 263 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4CWM HIS A 264 ? UNP Q9C9G4 ? ? 'expression tag' 264 1 1 4CWM HIS A 265 ? UNP Q9C9G4 ? ? 'expression tag' 265 2 1 4CWM HIS A 266 ? UNP Q9C9G4 ? ? 'expression tag' 266 3 1 4CWM HIS A 267 ? UNP Q9C9G4 ? ? 'expression tag' 267 4 1 4CWM HIS A 268 ? UNP Q9C9G4 ? ? 'expression tag' 268 5 1 4CWM HIS A 269 ? UNP Q9C9G4 ? ? 'expression tag' 269 6 2 4CWM HIS B 264 ? UNP Q9C9G4 ? ? 'expression tag' 264 7 2 4CWM HIS B 265 ? UNP Q9C9G4 ? ? 'expression tag' 265 8 2 4CWM HIS B 266 ? UNP Q9C9G4 ? ? 'expression tag' 266 9 2 4CWM HIS B 267 ? UNP Q9C9G4 ? ? 'expression tag' 267 10 2 4CWM HIS B 268 ? UNP Q9C9G4 ? ? 'expression tag' 268 11 2 4CWM HIS B 269 ? UNP Q9C9G4 ? ? 'expression tag' 269 12 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4CWM _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.19 _exptl_crystal.density_percent_sol 43.81 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M TRIS PH 8.5 0.2 M SODIUM ACETATE 30% W/V PEG4000' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM' _diffrn_detector.pdbx_collection_date 2012-10-10 _diffrn_detector.details MIRRORS # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'FIXED-EXIT DOUBLE CRYSTAL MONOCHROMATOR' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'NSRRC BEAMLINE BL13B1' _diffrn_source.pdbx_synchrotron_site NSRRC _diffrn_source.pdbx_synchrotron_beamline BL13B1 _diffrn_source.pdbx_wavelength 1 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CWM _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 23.28 _reflns.d_resolution_high 2.09 _reflns.number_obs 28226 _reflns.number_all ? _reflns.percent_possible_obs 97.3 _reflns.pdbx_Rmerge_I_obs 0.01 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 14.70 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.9 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.09 _reflns_shell.d_res_low 2.15 _reflns_shell.percent_possible_all 88.0 _reflns_shell.Rmerge_I_obs 0.45 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.70 _reflns_shell.pdbx_redundancy 3.9 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CWM _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 28226 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 23.28 _refine.ls_d_res_high 2.09 _refine.ls_percent_reflns_obs 97.33 _refine.ls_R_factor_obs 0.20108 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19749 _refine.ls_R_factor_R_free 0.26802 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1506 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.943 _refine.correlation_coeff_Fo_to_Fc_free 0.897 _refine.B_iso_mean 27.392 _refine.aniso_B[1][1] -0.22 _refine.aniso_B[2][2] 1.00 _refine.aniso_B[3][3] -0.57 _refine.aniso_B[1][2] -1.04 _refine.aniso_B[1][3] -0.08 _refine.aniso_B[2][3] 1.50 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY' _refine.pdbx_starting_model 'PDB ENTRY 3W52' _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 0.311 _refine.pdbx_overall_ESU_R_Free 0.238 _refine.overall_SU_ML 0.167 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 6.187 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4098 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 262 _refine_hist.number_atoms_solvent 457 _refine_hist.number_atoms_total 4817 _refine_hist.d_res_high 2.09 _refine_hist.d_res_low 23.28 # 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_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.011 0.019 ? 4480 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 4022 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.564 2.000 ? 6112 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.842 3.003 ? 9178 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.186 5.000 ? 506 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 38.078 24.175 ? 206 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.901 15.000 ? 690 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 10.519 15.000 ? 22 'X-RAY DIFFRACTION' ? r_chiral_restr 0.087 0.200 ? 704 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 4852 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 1010 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.092 _refine_ls_shell.d_res_low 2.147 _refine_ls_shell.number_reflns_R_work 1882 _refine_ls_shell.R_factor_R_work 0.208 _refine_ls_shell.percent_reflns_obs 87.90 _refine_ls_shell.R_factor_R_free 0.312 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 94 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CWM _struct.title 'High-glycosylation crystal structure of the bifunctional endonuclease (AtBFN2) from Arabidopsis thaliana' _struct.pdbx_descriptor 'ENDONUCLEASE 2 (E.C.3.1.30.1)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CWM _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, SSDNA BINDING' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 4 ? G N N 4 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 2 ? P N N 2 ? Q N N 3 ? R N N 4 ? S N N 4 ? T N N 2 ? U N N 2 ? V N N 3 ? W N N 2 ? X N N 2 ? Y N N 3 ? Z N N 5 ? AA N N 5 ? BA N N 5 ? CA N N 6 ? DA N N 6 ? # _struct_biol.id 1 # 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 GLY A 2 ? THR A 15 ? GLY A 2 THR A 15 1 ? 14 HELX_P HELX_P2 2 ASP A 18 ? LEU A 29 ? ASP A 18 LEU A 29 1 ? 12 HELX_P HELX_P3 3 PRO A 30 ? GLU A 34 ? PRO A 30 GLU A 34 5 ? 5 HELX_P HELX_P4 4 ASP A 36 ? CYS A 41 ? ASP A 36 CYS A 41 5 ? 6 HELX_P HELX_P5 5 LEU A 42 ? VAL A 47 ? LEU A 42 VAL A 47 5 ? 6 HELX_P HELX_P6 6 TYR A 51 ? TYR A 59 ? TYR A 51 TYR A 59 5 ? 9 HELX_P HELX_P7 7 GLN A 69 ? CYS A 74 ? GLN A 69 CYS A 74 1 ? 6 HELX_P HELX_P8 8 CYS A 84 ? LEU A 97 ? CYS A 84 LEU A 97 1 ? 14 HELX_P HELX_P9 9 ASN A 110 ? ILE A 125 ? ASN A 110 ILE A 125 1 ? 16 HELX_P HELX_P10 10 HIS A 126 ? LEU A 129 ? HIS A 126 LEU A 129 5 ? 4 HELX_P HELX_P11 11 SER A 135 ? ASN A 140 ? SER A 135 ASN A 140 5 ? 6 HELX_P HELX_P12 12 LEU A 153 ? SER A 159 ? LEU A 153 SER A 159 1 ? 7 HELX_P HELX_P13 13 SER A 159 ? TYR A 170 ? SER A 159 TYR A 170 1 ? 12 HELX_P HELX_P14 14 ALA A 173 ? GLU A 188 ? ALA A 173 GLU A 188 1 ? 16 HELX_P HELX_P15 15 TRP A 189 ? THR A 198 ? TRP A 189 THR A 198 1 ? 10 HELX_P HELX_P16 16 CYS A 205 ? TRP A 220 ? CYS A 205 TRP A 220 1 ? 16 HELX_P HELX_P17 17 GLU A 232 ? GLY A 263 ? GLU A 232 GLY A 263 1 ? 32 HELX_P HELX_P18 18 GLY B 2 ? THR B 15 ? GLY B 2 THR B 15 1 ? 14 HELX_P HELX_P19 19 ASP B 18 ? LEU B 29 ? ASP B 18 LEU B 29 1 ? 12 HELX_P HELX_P20 20 PRO B 30 ? GLU B 34 ? PRO B 30 GLU B 34 5 ? 5 HELX_P HELX_P21 21 ASP B 36 ? CYS B 41 ? ASP B 36 CYS B 41 5 ? 6 HELX_P HELX_P22 22 LEU B 42 ? VAL B 47 ? LEU B 42 VAL B 47 5 ? 6 HELX_P HELX_P23 23 TYR B 51 ? TYR B 59 ? TYR B 51 TYR B 59 5 ? 9 HELX_P HELX_P24 24 GLN B 69 ? CYS B 74 ? GLN B 69 CYS B 74 1 ? 6 HELX_P HELX_P25 25 CYS B 84 ? LEU B 97 ? CYS B 84 LEU B 97 1 ? 14 HELX_P HELX_P26 26 ASN B 110 ? ILE B 125 ? ASN B 110 ILE B 125 1 ? 16 HELX_P HELX_P27 27 HIS B 126 ? LEU B 129 ? HIS B 126 LEU B 129 5 ? 4 HELX_P HELX_P28 28 SER B 135 ? ASN B 140 ? SER B 135 ASN B 140 5 ? 6 HELX_P HELX_P29 29 LEU B 153 ? SER B 159 ? LEU B 153 SER B 159 1 ? 7 HELX_P HELX_P30 30 SER B 159 ? LEU B 169 ? SER B 159 LEU B 169 1 ? 11 HELX_P HELX_P31 31 ALA B 173 ? GLU B 188 ? ALA B 173 GLU B 188 1 ? 16 HELX_P HELX_P32 32 TRP B 189 ? THR B 198 ? TRP B 189 THR B 198 1 ? 10 HELX_P HELX_P33 33 CYS B 205 ? TRP B 220 ? CYS B 205 TRP B 220 1 ? 16 HELX_P HELX_P34 34 GLU B 232 ? GLY B 263 ? GLU B 232 GLY B 263 1 ? 32 # _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 10 SG ? ? ? 1_555 A CYS 41 SG ? ? A CYS 10 A CYS 41 1_555 ? ? ? ? ? ? ? 2.021 ? disulf2 disulf ? ? A CYS 66 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 66 A CYS 218 1_555 ? ? ? ? ? ? ? 2.056 ? disulf3 disulf ? ? A CYS 74 SG ? ? ? 1_555 A CYS 84 SG ? ? A CYS 74 A CYS 84 1_555 ? ? ? ? ? ? ? 2.127 ? disulf4 disulf ? ? A CYS 199 SG ? ? ? 1_555 A CYS 205 SG ? ? A CYS 199 A CYS 205 1_555 ? ? ? ? ? ? ? 2.051 ? disulf5 disulf ? ? B CYS 10 SG ? ? ? 1_555 B CYS 41 SG ? ? B CYS 10 B CYS 41 1_555 ? ? ? ? ? ? ? 2.019 ? disulf6 disulf ? ? B CYS 66 SG ? ? ? 1_555 B CYS 218 SG ? ? B CYS 66 B CYS 218 1_555 ? ? ? ? ? ? ? 2.059 ? disulf7 disulf ? ? B CYS 74 SG ? ? ? 1_555 B CYS 84 SG ? ? B CYS 74 B CYS 84 1_555 ? ? ? ? ? ? ? 2.097 ? disulf8 disulf ? ? B CYS 199 SG ? ? ? 1_555 B CYS 205 SG ? ? B CYS 199 B CYS 205 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale ? ? A ASN 91 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 91 A NAG 301 1_555 ? ? ? ? ? ? ? 1.452 ? covale2 covale ? ? A ASN 110 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 110 A NAG 331 1_555 ? ? ? ? ? ? ? 1.440 ? covale3 covale ? ? A ASN 184 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 184 A NAG 361 1_555 ? ? ? ? ? ? ? 1.428 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 301 A NAG 302 1_555 ? ? ? ? ? ? ? 1.418 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 302 A BMA 303 1_555 ? ? ? ? ? ? ? 1.452 ? covale6 covale ? ? E BMA . O6 ? ? ? 1_555 G MAN . C1 ? ? A BMA 303 A MAN 305 1_555 ? ? ? ? ? ? ? 1.426 ? covale7 covale ? ? E BMA . O3 ? ? ? 1_555 F MAN . C1 ? ? A BMA 303 A MAN 304 1_555 ? ? ? ? ? ? ? 1.435 ? covale8 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 331 A NAG 332 1_555 ? ? ? ? ? ? ? 1.436 ? covale9 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 361 A NAG 362 1_555 ? ? ? ? ? ? ? 1.454 ? metalc1 metalc ? ? L ZN . ZN ? ? ? 1_555 CA HOH . O ? ? A ZN 431 A HOH 2002 1_555 ? ? ? ? ? ? ? 2.136 ? metalc2 metalc ? ? L ZN . ZN ? ? ? 1_555 CA HOH . O ? ? A ZN 431 A HOH 2058 1_555 ? ? ? ? ? ? ? 2.395 ? metalc3 metalc ? ? L ZN . ZN ? ? ? 1_555 A ASP 45 OD1 ? ? A ZN 431 A ASP 45 1_555 ? ? ? ? ? ? ? 2.385 ? metalc4 metalc ? ? L ZN . ZN ? ? ? 1_555 A HIS 58 ND1 ? ? A ZN 431 A HIS 58 1_555 ? ? ? ? ? ? ? 2.276 ? metalc5 metalc ? ? L ZN . ZN ? ? ? 1_555 A HIS 120 NE2 ? ? A ZN 431 A HIS 120 1_555 ? ? ? ? ? ? ? 2.374 ? metalc6 metalc ? ? L ZN . ZN ? ? ? 1_555 A ASP 124 OD2 ? ? A ZN 431 A ASP 124 1_555 ? ? ? ? ? ? ? 2.267 ? metalc7 metalc ? ? M ZN . ZN ? ? ? 1_555 A HIS 154 NE2 ? ? A ZN 432 A HIS 154 1_555 ? ? ? ? ? ? ? 2.104 ? metalc8 metalc ? ? M ZN . ZN ? ? ? 1_555 A ASP 158 OD2 ? ? A ZN 432 A ASP 158 1_555 ? ? ? ? ? ? ? 2.151 ? metalc9 metalc ? ? M ZN . ZN ? ? ? 1_555 A HIS 130 NE2 ? ? A ZN 432 A HIS 130 1_555 ? ? ? ? ? ? ? 2.156 ? metalc10 metalc ? ? M ZN . ZN ? ? ? 1_555 CA HOH . O ? ? A ZN 432 A HOH 2001 1_555 ? ? ? ? ? ? ? 2.125 ? metalc11 metalc ? ? M ZN . ZN ? ? ? 1_555 CA HOH . O ? ? A ZN 432 A HOH 2132 1_555 ? ? ? ? ? ? ? 1.994 ? metalc12 metalc ? ? M ZN . ZN ? ? ? 1_555 A ASP 158 OD1 ? ? A ZN 432 A ASP 158 1_555 ? ? ? ? ? ? ? 2.630 ? metalc13 metalc ? ? N ZN . ZN ? ? ? 1_555 A TRP 1 O ? ? A ZN 433 A TRP 1 1_555 ? ? ? ? ? ? ? 2.294 ? metalc14 metalc ? ? N ZN . ZN ? ? ? 1_555 A ASP 124 OD1 ? ? A ZN 433 A ASP 124 1_555 ? ? ? ? ? ? ? 2.134 ? metalc15 metalc ? ? N ZN . ZN ? ? ? 1_555 A HIS 6 NE2 ? ? A ZN 433 A HIS 6 1_555 ? ? ? ? ? ? ? 2.090 ? metalc16 metalc ? ? N ZN . ZN ? ? ? 1_555 CA HOH . O ? ? A ZN 433 A HOH 2002 1_555 ? ? ? ? ? ? ? 2.008 ? covale10 covale ? ? B ASN 91 ND2 ? ? ? 1_555 O NAG . C1 ? ? B ASN 91 B NAG 301 1_555 ? ? ? ? ? ? ? 1.452 ? covale11 covale ? ? B ASN 110 ND2 ? ? ? 1_555 T NAG . C1 ? ? B ASN 110 B NAG 331 1_555 ? ? ? ? ? ? ? 1.441 ? covale12 covale ? ? B ASN 184 ND2 ? ? ? 1_555 W NAG . C1 ? ? B ASN 184 B NAG 361 1_555 ? ? ? ? ? ? ? 1.438 ? covale13 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? B NAG 301 B NAG 302 1_555 ? ? ? ? ? ? ? 1.433 ? covale14 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? B NAG 302 B BMA 303 1_555 ? ? ? ? ? ? ? 1.434 ? covale15 covale ? ? Q BMA . O6 ? ? ? 1_555 S MAN . C1 ? ? B BMA 303 B MAN 305 1_555 ? ? ? ? ? ? ? 1.431 ? covale16 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? B BMA 303 B MAN 304 1_555 ? ? ? ? ? ? ? 1.445 ? covale17 covale ? ? T NAG . O4 ? ? ? 1_555 U NAG . C1 ? ? B NAG 331 B NAG 332 1_555 ? ? ? ? ? ? ? 1.439 ? covale18 covale ? ? U NAG . O4 ? ? ? 1_555 V BMA . C1 ? ? B NAG 332 B BMA 333 1_555 ? ? ? ? ? ? ? 1.463 ? covale19 covale ? ? W NAG . O4 ? ? ? 1_555 X NAG . C1 ? ? B NAG 361 B NAG 362 1_555 ? ? ? ? ? ? ? 1.442 ? covale20 covale ? ? X NAG . O4 ? ? ? 1_555 Y BMA . C1 ? ? B NAG 362 B BMA 363 1_555 ? ? ? ? ? ? ? 1.435 ? metalc17 metalc ? ? Z ZN . ZN ? ? ? 1_555 DA HOH . O ? ? B ZN 431 B HOH 2043 1_555 ? ? ? ? ? ? ? 2.165 ? metalc18 metalc ? ? Z ZN . ZN ? ? ? 1_555 B ASP 124 OD2 ? ? B ZN 431 B ASP 124 1_555 ? ? ? ? ? ? ? 2.231 ? metalc19 metalc ? ? Z ZN . ZN ? ? ? 1_555 B HIS 120 NE2 ? ? B ZN 431 B HIS 120 1_555 ? ? ? ? ? ? ? 2.359 ? metalc20 metalc ? ? Z ZN . ZN ? ? ? 1_555 B HIS 58 ND1 ? ? B ZN 431 B HIS 58 1_555 ? ? ? ? ? ? ? 2.351 ? metalc21 metalc ? ? Z ZN . ZN ? ? ? 1_555 B ASP 45 OD1 ? ? B ZN 431 B ASP 45 1_555 ? ? ? ? ? ? ? 2.300 ? metalc22 metalc ? ? AA ZN . ZN ? ? ? 1_555 B HIS 154 NE2 ? ? B ZN 432 B HIS 154 1_555 ? ? ? ? ? ? ? 2.189 ? metalc23 metalc ? ? AA ZN . ZN ? ? ? 1_555 B HIS 130 NE2 ? ? B ZN 432 B HIS 130 1_555 ? ? ? ? ? ? ? 2.163 ? metalc24 metalc ? ? AA ZN . ZN ? ? ? 1_555 DA HOH . O ? ? B ZN 432 B HOH 2118 1_555 ? ? ? ? ? ? ? 2.000 ? metalc25 metalc ? ? AA ZN . ZN ? ? ? 1_555 DA HOH . O ? ? B ZN 432 B HOH 2001 1_555 ? ? ? ? ? ? ? 2.071 ? metalc26 metalc ? ? AA ZN . ZN ? ? ? 1_555 B ASP 158 OD2 ? ? B ZN 432 B ASP 158 1_555 ? ? ? ? ? ? ? 2.083 ? metalc27 metalc ? ? AA ZN . ZN ? ? ? 1_555 B ASP 158 OD1 ? ? B ZN 432 B ASP 158 1_555 ? ? ? ? ? ? ? 2.630 ? metalc28 metalc ? ? BA ZN . ZN ? ? ? 1_555 B TRP 1 O ? ? B ZN 433 B TRP 1 1_555 ? ? ? ? ? ? ? 2.329 ? metalc29 metalc ? ? BA ZN . ZN ? ? ? 1_555 B HIS 6 NE2 ? ? B ZN 433 B HIS 6 1_555 ? ? ? ? ? ? ? 2.058 ? metalc30 metalc ? ? BA ZN . ZN ? ? ? 1_555 B ASP 124 OD1 ? ? B ZN 433 B ASP 124 1_555 ? ? ? ? ? ? ? 2.156 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 2 ? AB ? 3 ? BA ? 2 ? BB ? 3 ? # 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 AA 1 2 ? parallel AB 1 2 ? anti-parallel AB 2 3 ? parallel BA 1 2 ? parallel BB 1 2 ? anti-parallel BB 2 3 ? 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 AA 1 ILE A 60 ? THR A 62 ? ILE A 60 THR A 62 AA 2 VAL A 131 ? TYR A 133 ? VAL A 131 TYR A 133 AB 1 ARG A 149 ? ASN A 152 ? ARG A 149 ASN A 152 AB 2 GLU A 143 ? TRP A 146 ? GLU A 143 TRP A 146 AB 3 THR A 230 ? LEU A 231 ? THR A 230 LEU A 231 BA 1 ILE B 60 ? THR B 62 ? ILE B 60 THR B 62 BA 2 VAL B 131 ? TYR B 133 ? VAL B 131 TYR B 133 BB 1 ARG B 149 ? ASN B 152 ? ARG B 149 ASN B 152 BB 2 GLU B 143 ? TRP B 146 ? GLU B 143 TRP B 146 BB 3 THR B 230 ? LEU B 231 ? THR B 230 LEU B 231 # 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 AA 1 2 N THR A 62 ? N THR A 62 O SER A 132 ? O SER A 132 AB 1 2 N ALA A 151 ? N ALA A 151 O VAL A 144 ? O VAL A 144 AB 2 3 O HIS A 145 ? O HIS A 145 N LEU A 231 ? N LEU A 231 BA 1 2 N THR B 62 ? N THR B 62 O SER B 132 ? O SER B 132 BB 1 2 N ALA B 151 ? N ALA B 151 O VAL B 144 ? O VAL B 144 BB 2 3 O HIS B 145 ? O HIS B 145 N LEU B 231 ? N LEU B 231 # 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 ? ? ? ? 7 'BINDING SITE FOR RESIDUE ZN A 431' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 432' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 433' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN B 431' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN B 432' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 433' AC7 Software ? ? ? ? 20 'Binding site for Poly-Saccharide residues NAG A 301 through MAN A 305 bound to ASN A 91' AC8 Software ? ? ? ? 8 'Binding site for Poly-Saccharide residues NAG A 331 through NAG A 332 bound to ASN A 110' AC9 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues NAG A 361 through NAG A 362 bound to ASN A 184' BC1 Software ? ? ? ? 18 'Binding site for Poly-Saccharide residues NAG B 301 through MAN B 305 bound to ASN B 91' BC2 Software ? ? ? ? 9 'Binding site for Poly-Saccharide residues NAG B 331 through BMA B 333 bound to ASN B 110' BC3 Software ? ? ? ? 15 'Binding site for Poly-Saccharide residues NAG B 361 through BMA B 363 bound to ASN B 184' # 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 7 ASP A 45 ? ASP A 45 . ? 1_555 ? 2 AC1 7 HIS A 58 ? HIS A 58 . ? 1_555 ? 3 AC1 7 HIS A 120 ? HIS A 120 . ? 1_555 ? 4 AC1 7 ASP A 124 ? ASP A 124 . ? 1_555 ? 5 AC1 7 ZN N . ? ZN A 433 . ? 1_555 ? 6 AC1 7 HOH CA . ? HOH A 2002 . ? 1_555 ? 7 AC1 7 HOH CA . ? HOH A 2058 . ? 1_555 ? 8 AC2 5 HIS A 130 ? HIS A 130 . ? 1_555 ? 9 AC2 5 HIS A 154 ? HIS A 154 . ? 1_555 ? 10 AC2 5 ASP A 158 ? ASP A 158 . ? 1_555 ? 11 AC2 5 HOH CA . ? HOH A 2001 . ? 1_555 ? 12 AC2 5 HOH CA . ? HOH A 2132 . ? 1_555 ? 13 AC3 5 TRP A 1 ? TRP A 1 . ? 1_555 ? 14 AC3 5 HIS A 6 ? HIS A 6 . ? 1_555 ? 15 AC3 5 ASP A 124 ? ASP A 124 . ? 1_555 ? 16 AC3 5 ZN L . ? ZN A 431 . ? 1_555 ? 17 AC3 5 HOH CA . ? HOH A 2002 . ? 1_555 ? 18 AC4 6 ASP B 45 ? ASP B 45 . ? 1_555 ? 19 AC4 6 HIS B 58 ? HIS B 58 . ? 1_555 ? 20 AC4 6 HIS B 120 ? HIS B 120 . ? 1_555 ? 21 AC4 6 ASP B 124 ? ASP B 124 . ? 1_555 ? 22 AC4 6 ZN BA . ? ZN B 433 . ? 1_555 ? 23 AC4 6 HOH DA . ? HOH B 2043 . ? 1_555 ? 24 AC5 5 HIS B 130 ? HIS B 130 . ? 1_555 ? 25 AC5 5 HIS B 154 ? HIS B 154 . ? 1_555 ? 26 AC5 5 ASP B 158 ? ASP B 158 . ? 1_555 ? 27 AC5 5 HOH DA . ? HOH B 2001 . ? 1_555 ? 28 AC5 5 HOH DA . ? HOH B 2118 . ? 1_555 ? 29 AC6 4 TRP B 1 ? TRP B 1 . ? 1_555 ? 30 AC6 4 HIS B 6 ? HIS B 6 . ? 1_555 ? 31 AC6 4 ASP B 124 ? ASP B 124 . ? 1_555 ? 32 AC6 4 ZN Z . ? ZN B 431 . ? 1_555 ? 33 AC7 20 HIS A 52 ? HIS A 52 . ? 1_555 ? 34 AC7 20 TRP A 53 ? TRP A 53 . ? 1_555 ? 35 AC7 20 LEU A 57 ? LEU A 57 . ? 1_555 ? 36 AC7 20 GLY A 82 ? GLY A 82 . ? 1_555 ? 37 AC7 20 ARG A 83 ? ARG A 83 . ? 1_555 ? 38 AC7 20 ALA A 88 ? ALA A 88 . ? 1_555 ? 39 AC7 20 ASN A 91 ? ASN A 91 . ? 1_555 ? 40 AC7 20 TYR A 92 ? TYR A 92 . ? 1_555 ? 41 AC7 20 GLN A 95 ? GLN A 95 . ? 1_555 ? 42 AC7 20 GLN A 108 ? GLN A 108 . ? 1_555 ? 43 AC7 20 TYR A 109 ? TYR A 109 . ? 1_555 ? 44 AC7 20 HOH CA . ? HOH A 2123 . ? 1_555 ? 45 AC7 20 HOH CA . ? HOH A 2214 . ? 1_555 ? 46 AC7 20 HOH CA . ? HOH A 2217 . ? 1_555 ? 47 AC7 20 HOH CA . ? HOH A 2218 . ? 1_555 ? 48 AC7 20 HOH CA . ? HOH A 2219 . ? 1_555 ? 49 AC7 20 HOH CA . ? HOH A 2220 . ? 1_555 ? 50 AC7 20 THR B 148 ? THR B 148 . ? 1_456 ? 51 AC7 20 ARG B 149 ? ARG B 149 . ? 1_456 ? 52 AC7 20 LYS B 150 ? LYS B 150 . ? 1_456 ? 53 AC8 8 PRO A 30 ? PRO A 30 . ? 1_555 ? 54 AC8 8 TRP A 43 ? TRP A 43 . ? 1_555 ? 55 AC8 8 ASN A 110 ? ASN A 110 . ? 1_555 ? 56 AC8 8 GLU A 113 ? GLU A 113 . ? 1_555 ? 57 AC8 8 HOH CA . ? HOH A 2047 . ? 1_555 ? 58 AC8 8 HOH CA . ? HOH A 2222 . ? 1_555 ? 59 AC8 8 HOH CA . ? HOH A 2223 . ? 1_555 ? 60 AC8 8 HOH CA . ? HOH A 2225 . ? 1_555 ? 61 AC9 11 TYR A 170 ? TYR A 170 . ? 1_555 ? 62 AC9 11 LEU A 181 ? LEU A 181 . ? 1_555 ? 63 AC9 11 ASN A 184 ? ASN A 184 . ? 1_555 ? 64 AC9 11 GLU A 188 ? GLU A 188 . ? 1_555 ? 65 AC9 11 TRP A 189 ? TRP A 189 . ? 1_555 ? 66 AC9 11 TYR A 244 ? TYR A 244 . ? 1_555 ? 67 AC9 11 HOH CA . ? HOH A 2168 . ? 1_555 ? 68 AC9 11 HOH CA . ? HOH A 2204 . ? 1_555 ? 69 AC9 11 HOH CA . ? HOH A 2229 . ? 1_555 ? 70 AC9 11 HOH CA . ? HOH A 2230 . ? 1_555 ? 71 AC9 11 HOH CA . ? HOH A 2232 . ? 1_555 ? 72 BC1 18 THR A 148 ? THR A 148 . ? 1_554 ? 73 BC1 18 LYS A 150 ? LYS A 150 . ? 1_554 ? 74 BC1 18 HIS B 52 ? HIS B 52 . ? 1_555 ? 75 BC1 18 TRP B 53 ? TRP B 53 . ? 1_555 ? 76 BC1 18 ARG B 83 ? ARG B 83 . ? 1_555 ? 77 BC1 18 ALA B 88 ? ALA B 88 . ? 1_555 ? 78 BC1 18 ASN B 91 ? ASN B 91 . ? 1_555 ? 79 BC1 18 TYR B 92 ? TYR B 92 . ? 1_555 ? 80 BC1 18 GLN B 95 ? GLN B 95 . ? 1_555 ? 81 BC1 18 GLN B 108 ? GLN B 108 . ? 1_555 ? 82 BC1 18 TYR B 109 ? TYR B 109 . ? 1_555 ? 83 BC1 18 HOH DA . ? HOH B 2112 . ? 1_555 ? 84 BC1 18 HOH DA . ? HOH B 2192 . ? 1_555 ? 85 BC1 18 HOH DA . ? HOH B 2195 . ? 1_555 ? 86 BC1 18 HOH DA . ? HOH B 2197 . ? 1_555 ? 87 BC1 18 HOH DA . ? HOH B 2198 . ? 1_555 ? 88 BC1 18 HOH DA . ? HOH B 2199 . ? 1_555 ? 89 BC1 18 HOH DA . ? HOH B 2200 . ? 1_555 ? 90 BC2 9 PRO B 30 ? PRO B 30 . ? 1_555 ? 91 BC2 9 ARG B 50 ? ARG B 50 . ? 1_555 ? 92 BC2 9 ASN B 110 ? ASN B 110 . ? 1_555 ? 93 BC2 9 GLU B 113 ? GLU B 113 . ? 1_555 ? 94 BC2 9 GLU B 234 ? GLU B 234 . ? 1_545 ? 95 BC2 9 HOH DA . ? HOH B 2110 . ? 1_555 ? 96 BC2 9 HOH DA . ? HOH B 2180 . ? 1_545 ? 97 BC2 9 HOH DA . ? HOH B 2203 . ? 1_555 ? 98 BC2 9 HOH DA . ? HOH B 2204 . ? 1_555 ? 99 BC3 15 GLU B 31 ? GLU B 31 . ? 1_565 ? 100 BC3 15 TYR B 170 ? TYR B 170 . ? 1_555 ? 101 BC3 15 ALA B 180 ? ALA B 180 . ? 1_555 ? 102 BC3 15 LEU B 181 ? LEU B 181 . ? 1_555 ? 103 BC3 15 ASN B 184 ? ASN B 184 . ? 1_555 ? 104 BC3 15 GLU B 188 ? GLU B 188 . ? 1_555 ? 105 BC3 15 TRP B 189 ? TRP B 189 . ? 1_555 ? 106 BC3 15 TYR B 244 ? TYR B 244 . ? 1_555 ? 107 BC3 15 HOH DA . ? HOH B 2143 . ? 1_555 ? 108 BC3 15 HOH DA . ? HOH B 2156 . ? 1_555 ? 109 BC3 15 HOH DA . ? HOH B 2205 . ? 1_555 ? 110 BC3 15 HOH DA . ? HOH B 2206 . ? 1_555 ? 111 BC3 15 HOH DA . ? HOH B 2207 . ? 1_555 ? 112 BC3 15 HOH DA . ? HOH B 2209 . ? 1_555 ? 113 BC3 15 HOH DA . ? HOH B 2210 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CWM _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 4CWM _atom_sites.fract_transf_matrix[1][1] 0.022039 _atom_sites.fract_transf_matrix[1][2] -0.005193 _atom_sites.fract_transf_matrix[1][3] -0.003092 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.019493 _atom_sites.fract_transf_matrix[2][3] -0.005856 _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] 0.017434 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S ZN # 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 . TRP A 1 1 ? -6.181 8.453 18.995 1.00 14.80 ? 1 TRP A N 1 ATOM 2 C CA . TRP A 1 1 ? -5.067 8.172 19.952 1.00 15.08 ? 1 TRP A CA 1 ATOM 3 C C . TRP A 1 1 ? -5.133 9.041 21.183 1.00 15.49 ? 1 TRP A C 1 ATOM 4 O O . TRP A 1 1 ? -5.771 10.086 21.200 1.00 14.58 ? 1 TRP A O 1 ATOM 5 C CB . TRP A 1 1 ? -3.703 8.440 19.323 1.00 14.73 ? 1 TRP A CB 1 ATOM 6 C CG . TRP A 1 1 ? -3.499 7.857 17.973 1.00 14.82 ? 1 TRP A CG 1 ATOM 7 C CD1 . TRP A 1 1 ? -3.767 8.458 16.778 1.00 15.14 ? 1 TRP A CD1 1 ATOM 8 C CD2 . TRP A 1 1 ? -2.946 6.578 17.668 1.00 14.34 ? 1 TRP A CD2 1 ATOM 9 N NE1 . TRP A 1 1 ? -3.415 7.629 15.753 1.00 15.58 ? 1 TRP A NE1 1 ATOM 10 C CE2 . TRP A 1 1 ? -2.913 6.464 16.277 1.00 14.86 ? 1 TRP A CE2 1 ATOM 11 C CE3 . TRP A 1 1 ? -2.478 5.518 18.445 1.00 15.35 ? 1 TRP A CE3 1 ATOM 12 C CZ2 . TRP A 1 1 ? -2.429 5.330 15.633 1.00 15.06 ? 1 TRP A CZ2 1 ATOM 13 C CZ3 . TRP A 1 1 ? -1.993 4.383 17.807 1.00 15.21 ? 1 TRP A CZ3 1 ATOM 14 C CH2 . TRP A 1 1 ? -1.984 4.301 16.416 1.00 15.43 ? 1 TRP A CH2 1 ATOM 15 N N . GLY A 1 2 ? -4.420 8.618 22.204 1.00 16.65 ? 2 GLY A N 1 ATOM 16 C CA . GLY A 1 2 ? -4.246 9.438 23.360 1.00 19.16 ? 2 GLY A CA 1 ATOM 17 C C . GLY A 1 2 ? -3.169 10.439 23.020 1.00 20.40 ? 2 GLY A C 1 ATOM 18 O O . GLY A 1 2 ? -2.769 10.590 21.857 1.00 19.71 ? 2 GLY A O 1 ATOM 19 N N . LYS A 1 3 ? -2.666 11.080 24.054 1.00 20.88 ? 3 LYS A N 1 ATOM 20 C CA . LYS A 1 3 ? -1.785 12.220 23.905 1.00 23.00 ? 3 LYS A CA 1 ATOM 21 C C . LYS A 1 3 ? -0.466 11.917 23.207 1.00 19.85 ? 3 LYS A C 1 ATOM 22 O O . LYS A 1 3 ? -0.070 12.673 22.322 1.00 17.27 ? 3 LYS A O 1 ATOM 23 C CB . LYS A 1 3 ? -1.518 12.830 25.275 1.00 25.70 ? 3 LYS A CB 1 ATOM 24 C CG . LYS A 1 3 ? -0.568 14.006 25.242 1.00 29.66 ? 3 LYS A CG 1 ATOM 25 C CD . LYS A 1 3 ? 0.788 13.650 25.829 1.00 32.23 ? 3 LYS A CD 1 ATOM 26 C CE . LYS A 1 3 ? 1.043 14.367 27.141 1.00 35.33 ? 3 LYS A CE 1 ATOM 27 N NZ . LYS A 1 3 ? 1.485 15.767 26.878 1.00 35.70 ? 3 LYS A NZ 1 ATOM 28 N N . GLU A 1 4 ? 0.189 10.838 23.611 1.00 20.10 ? 4 GLU A N 1 ATOM 29 C CA . GLU A 1 4 ? 1.476 10.424 23.027 1.00 21.85 ? 4 GLU A CA 1 ATOM 30 C C . GLU A 1 4 ? 1.362 10.231 21.526 1.00 20.57 ? 4 GLU A C 1 ATOM 31 O O . GLU A 1 4 ? 2.185 10.719 20.763 1.00 20.97 ? 4 GLU A O 1 ATOM 32 C CB . GLU A 1 4 ? 1.963 9.088 23.611 1.00 23.30 ? 4 GLU A CB 1 ATOM 33 C CG . GLU A 1 4 ? 2.255 9.102 25.110 1.00 25.03 ? 4 GLU A CG 1 ATOM 34 C CD . GLU A 1 4 ? 1.015 8.963 25.995 1.00 25.48 ? 4 GLU A CD 1 ATOM 35 O OE1 . GLU A 1 4 ? -0.122 8.677 25.512 1.00 23.43 ? 4 GLU A OE1 1 ATOM 36 O OE2 . GLU A 1 4 ? 1.193 9.149 27.212 1.00 29.22 ? 4 GLU A OE2 1 ATOM 37 N N . GLY A 1 5 ? 0.342 9.489 21.107 1.00 20.59 ? 5 GLY A N 1 ATOM 38 C CA . GLY A 1 5 ? 0.182 9.166 19.693 1.00 19.78 ? 5 GLY A CA 1 ATOM 39 C C . GLY A 1 5 ? 0.033 10.431 18.868 1.00 19.47 ? 5 GLY A C 1 ATOM 40 O O . GLY A 1 5 ? 0.688 10.593 17.844 1.00 18.36 ? 5 GLY A O 1 ATOM 41 N N . HIS A 1 6 ? -0.812 11.347 19.325 1.00 19.07 ? 6 HIS A N 1 ATOM 42 C CA . HIS A 1 6 ? -1.015 12.611 18.591 1.00 19.05 ? 6 HIS A CA 1 ATOM 43 C C . HIS A 1 6 ? 0.243 13.503 18.569 1.00 19.36 ? 6 HIS A C 1 ATOM 44 O O . HIS A 1 6 ? 0.510 14.201 17.583 1.00 20.12 ? 6 HIS A O 1 ATOM 45 C CB . HIS A 1 6 ? -2.209 13.379 19.178 1.00 18.15 ? 6 HIS A CB 1 ATOM 46 C CG . HIS A 1 6 ? -3.537 12.801 18.789 1.00 18.94 ? 6 HIS A CG 1 ATOM 47 N ND1 . HIS A 1 6 ? -4.012 12.832 17.499 1.00 19.25 ? 6 HIS A ND1 1 ATOM 48 C CD2 . HIS A 1 6 ? -4.479 12.162 19.517 1.00 18.46 ? 6 HIS A CD2 1 ATOM 49 C CE1 . HIS A 1 6 ? -5.198 12.254 17.453 1.00 19.60 ? 6 HIS A CE1 1 ATOM 50 N NE2 . HIS A 1 6 ? -5.505 11.842 18.665 1.00 19.38 ? 6 HIS A NE2 1 ATOM 51 N N . GLU A 1 7 ? 0.999 13.523 19.658 1.00 19.61 ? 7 GLU A N 1 ATOM 52 C CA . GLU A 1 7 ? 2.279 14.224 19.669 1.00 21.30 ? 7 GLU A CA 1 ATOM 53 C C . GLU A 1 7 ? 3.210 13.718 18.602 1.00 20.68 ? 7 GLU A C 1 ATOM 54 O O . GLU A 1 7 ? 3.818 14.478 17.830 1.00 20.36 ? 7 GLU A O 1 ATOM 55 C CB . GLU A 1 7 ? 2.971 14.012 20.995 1.00 24.90 ? 7 GLU A CB 1 ATOM 56 C CG . GLU A 1 7 ? 2.630 15.040 22.047 1.00 28.90 ? 7 GLU A CG 1 ATOM 57 C CD . GLU A 1 7 ? 3.671 15.002 23.151 1.00 33.39 ? 7 GLU A CD 1 ATOM 58 O OE1 . GLU A 1 7 ? 4.832 15.421 22.908 1.00 36.09 ? 7 GLU A OE1 1 ATOM 59 O OE2 . GLU A 1 7 ? 3.330 14.485 24.229 1.00 38.00 ? 7 GLU A OE2 1 ATOM 60 N N . ILE A 1 8 ? 3.338 12.398 18.582 1.00 21.23 ? 8 ILE A N 1 ATOM 61 C CA . ILE A 1 8 ? 4.267 11.729 17.690 1.00 19.73 ? 8 ILE A CA 1 ATOM 62 C C . ILE A 1 8 ? 3.881 12.079 16.290 1.00 18.91 ? 8 ILE A C 1 ATOM 63 O O . ILE A 1 8 ? 4.721 12.470 15.497 1.00 19.88 ? 8 ILE A O 1 ATOM 64 C CB . ILE A 1 8 ? 4.254 10.214 17.935 1.00 20.14 ? 8 ILE A CB 1 ATOM 65 C CG1 . ILE A 1 8 ? 4.901 9.917 19.288 1.00 20.87 ? 8 ILE A CG1 1 ATOM 66 C CG2 . ILE A 1 8 ? 4.985 9.474 16.838 1.00 20.32 ? 8 ILE A CG2 1 ATOM 67 C CD1 . ILE A 1 8 ? 4.517 8.571 19.854 1.00 21.44 ? 8 ILE A CD1 1 ATOM 68 N N . ILE A 1 9 ? 2.593 11.989 15.991 1.00 17.49 ? 9 ILE A N 1 ATOM 69 C CA . ILE A 1 9 ? 2.108 12.292 14.655 1.00 17.24 ? 9 ILE A CA 1 ATOM 70 C C . ILE A 1 9 ? 2.375 13.751 14.248 1.00 18.24 ? 9 ILE A C 1 ATOM 71 O O . ILE A 1 9 ? 2.891 14.040 13.180 1.00 21.31 ? 9 ILE A O 1 ATOM 72 C CB . ILE A 1 9 ? 0.610 11.900 14.532 1.00 16.21 ? 9 ILE A CB 1 ATOM 73 C CG1 . ILE A 1 9 ? 0.514 10.381 14.377 1.00 16.38 ? 9 ILE A CG1 1 ATOM 74 C CG2 . ILE A 1 9 ? -0.059 12.550 13.314 1.00 15.63 ? 9 ILE A CG2 1 ATOM 75 C CD1 . ILE A 1 9 ? -0.866 9.784 14.587 1.00 16.52 ? 9 ILE A CD1 1 ATOM 76 N N . CYS A 1 10 ? 2.015 14.681 15.102 1.00 19.75 ? 10 CYS A N 1 ATOM 77 C CA . CYS A 1 10 ? 2.188 16.081 14.786 1.00 21.13 ? 10 CYS A CA 1 ATOM 78 C C . CYS A 1 10 ? 3.649 16.529 14.765 1.00 20.62 ? 10 CYS A C 1 ATOM 79 O O . CYS A 1 10 ? 4.000 17.354 13.949 1.00 20.12 ? 10 CYS A O 1 ATOM 80 C CB . CYS A 1 10 ? 1.384 16.909 15.752 1.00 22.19 ? 10 CYS A CB 1 ATOM 81 S SG . CYS A 1 10 ? -0.318 16.850 15.290 1.00 21.67 ? 10 CYS A SG 1 ATOM 82 N N . LYS A 1 11 ? 4.486 15.963 15.622 1.00 20.93 ? 11 LYS A N 1 ATOM 83 C CA . LYS A 1 11 ? 5.930 16.257 15.577 1.00 23.02 ? 11 LYS A CA 1 ATOM 84 C C . LYS A 1 11 ? 6.553 15.855 14.255 1.00 23.15 ? 11 LYS A C 1 ATOM 85 O O . LYS A 1 11 ? 7.355 16.590 13.669 1.00 22.18 ? 11 LYS A O 1 ATOM 86 C CB . LYS A 1 11 ? 6.686 15.525 16.700 1.00 24.92 ? 11 LYS A CB 1 ATOM 87 C CG . LYS A 1 11 ? 6.621 16.249 18.022 1.00 29.12 ? 11 LYS A CG 1 ATOM 88 C CD . LYS A 1 11 ? 7.075 15.352 19.162 1.00 31.52 ? 11 LYS A CD 1 ATOM 89 C CE . LYS A 1 11 ? 6.895 16.053 20.506 1.00 33.47 ? 11 LYS A CE 1 ATOM 90 N NZ . LYS A 1 11 ? 7.997 16.992 20.839 1.00 32.74 ? 11 LYS A NZ 1 ATOM 91 N N . ILE A 1 12 ? 6.196 14.662 13.806 1.00 20.70 ? 12 ILE A N 1 ATOM 92 C CA . ILE A 1 12 ? 6.726 14.144 12.566 1.00 21.62 ? 12 ILE A CA 1 ATOM 93 C C . ILE A 1 12 ? 6.237 15.033 11.452 1.00 20.35 ? 12 ILE A C 1 ATOM 94 O O . ILE A 1 12 ? 7.024 15.556 10.684 1.00 20.48 ? 12 ILE A O 1 ATOM 95 C CB . ILE A 1 12 ? 6.274 12.666 12.370 1.00 21.10 ? 12 ILE A CB 1 ATOM 96 C CG1 . ILE A 1 12 ? 6.994 11.790 13.369 1.00 20.08 ? 12 ILE A CG1 1 ATOM 97 C CG2 . ILE A 1 12 ? 6.458 12.168 10.920 1.00 23.27 ? 12 ILE A CG2 1 ATOM 98 C CD1 . ILE A 1 12 ? 6.497 10.355 13.426 1.00 19.75 ? 12 ILE A CD1 1 ATOM 99 N N . ALA A 1 13 ? 4.921 15.211 11.377 1.00 20.38 ? 13 ALA A N 1 ATOM 100 C CA . ALA A 1 13 ? 4.318 16.069 10.379 1.00 19.67 ? 13 ALA A CA 1 ATOM 101 C C . ALA A 1 13 ? 5.025 17.410 10.270 1.00 19.81 ? 13 ALA A C 1 ATOM 102 O O . ALA A 1 13 ? 5.308 17.889 9.166 1.00 17.22 ? 13 ALA A O 1 ATOM 103 C CB . ALA A 1 13 ? 2.848 16.305 10.709 1.00 20.74 ? 13 ALA A CB 1 ATOM 104 N N . GLN A 1 14 ? 5.317 18.026 11.411 1.00 21.49 ? 14 GLN A N 1 ATOM 105 C CA . GLN A 1 14 ? 5.764 19.413 11.365 1.00 23.07 ? 14 GLN A CA 1 ATOM 106 C C . GLN A 1 14 ? 7.178 19.558 10.809 1.00 23.56 ? 14 GLN A C 1 ATOM 107 O O . GLN A 1 14 ? 7.527 20.600 10.305 1.00 25.49 ? 14 GLN A O 1 ATOM 108 C CB . GLN A 1 14 ? 5.625 20.117 12.717 1.00 24.80 ? 14 GLN A CB 1 ATOM 109 C CG . GLN A 1 14 ? 5.868 21.617 12.590 1.00 25.92 ? 14 GLN A CG 1 ATOM 110 C CD . GLN A 1 14 ? 5.280 22.476 13.693 1.00 28.58 ? 14 GLN A CD 1 ATOM 111 O OE1 . GLN A 1 14 ? 5.034 22.020 14.822 1.00 28.59 ? 14 GLN A OE1 1 ATOM 112 N NE2 . GLN A 1 14 ? 5.062 23.753 13.368 1.00 27.78 ? 14 GLN A NE2 1 ATOM 113 N N . THR A 1 15 ? 7.965 18.493 10.865 1.00 24.79 ? 15 THR A N 1 ATOM 114 C CA . THR A 1 15 ? 9.340 18.535 10.399 1.00 26.70 ? 15 THR A CA 1 ATOM 115 C C . THR A 1 15 ? 9.412 18.115 8.933 1.00 24.78 ? 15 THR A C 1 ATOM 116 O O . THR A 1 15 ? 10.487 18.097 8.337 1.00 23.22 ? 15 THR A O 1 ATOM 117 C CB . THR A 1 15 ? 10.231 17.625 11.277 1.00 27.39 ? 15 THR A CB 1 ATOM 118 O OG1 . THR A 1 15 ? 9.683 16.311 11.319 1.00 28.29 ? 15 THR A OG1 1 ATOM 119 C CG2 . THR A 1 15 ? 10.282 18.162 12.685 1.00 28.36 ? 15 THR A CG2 1 ATOM 120 N N . ARG A 1 16 ? 8.255 17.772 8.375 1.00 23.47 ? 16 ARG A N 1 ATOM 121 C CA . ARG A 1 16 ? 8.125 17.405 6.988 1.00 22.85 ? 16 ARG A CA 1 ATOM 122 C C . ARG A 1 16 ? 7.345 18.445 6.184 1.00 22.38 ? 16 ARG A C 1 ATOM 123 O O . ARG A 1 16 ? 7.049 18.217 5.033 1.00 18.19 ? 16 ARG A O 1 ATOM 124 C CB . ARG A 1 16 ? 7.441 16.048 6.880 1.00 23.40 ? 16 ARG A CB 1 ATOM 125 C CG . ARG A 1 16 ? 8.239 14.913 7.524 1.00 23.62 ? 16 ARG A CG 1 ATOM 126 C CD . ARG A 1 16 ? 7.555 13.576 7.266 1.00 23.89 ? 16 ARG A CD 1 ATOM 127 N NE . ARG A 1 16 ? 7.493 13.259 5.838 1.00 23.59 ? 16 ARG A NE 1 ATOM 128 C CZ . ARG A 1 16 ? 8.515 12.775 5.138 1.00 25.87 ? 16 ARG A CZ 1 ATOM 129 N NH1 . ARG A 1 16 ? 9.688 12.500 5.726 1.00 26.90 ? 16 ARG A NH1 1 ATOM 130 N NH2 . ARG A 1 16 ? 8.376 12.561 3.839 1.00 25.89 ? 16 ARG A NH2 1 ATOM 131 N N . LEU A 1 17 ? 7.035 19.585 6.794 1.00 23.86 ? 17 LEU A N 1 ATOM 132 C CA . LEU A 1 17 ? 6.325 20.658 6.098 1.00 25.95 ? 17 LEU A CA 1 ATOM 133 C C . LEU A 1 17 ? 7.314 21.397 5.192 1.00 25.19 ? 17 LEU A C 1 ATOM 134 O O . LEU A 1 17 ? 8.428 21.657 5.610 1.00 23.30 ? 17 LEU A O 1 ATOM 135 C CB . LEU A 1 17 ? 5.708 21.638 7.103 1.00 26.48 ? 17 LEU A CB 1 ATOM 136 C CG . LEU A 1 17 ? 4.656 21.088 8.084 1.00 27.25 ? 17 LEU A CG 1 ATOM 137 C CD1 . LEU A 1 17 ? 4.353 22.062 9.221 1.00 27.99 ? 17 LEU A CD1 1 ATOM 138 C CD2 . LEU A 1 17 ? 3.376 20.757 7.339 1.00 28.94 ? 17 LEU A CD2 1 ATOM 139 N N . ASP A 1 18 ? 6.912 21.704 3.955 1.00 28.42 ? 18 ASP A N 1 ATOM 140 C CA . ASP A 1 18 ? 7.706 22.612 3.095 1.00 30.94 ? 18 ASP A CA 1 ATOM 141 C C . ASP A 1 18 ? 7.568 24.044 3.616 1.00 30.14 ? 18 ASP A C 1 ATOM 142 O O . ASP A 1 18 ? 6.807 24.288 4.549 1.00 28.38 ? 18 ASP A O 1 ATOM 143 C CB . ASP A 1 18 ? 7.357 22.498 1.596 1.00 32.07 ? 18 ASP A CB 1 ATOM 144 C CG . ASP A 1 18 ? 5.905 22.895 1.259 1.00 33.94 ? 18 ASP A CG 1 ATOM 145 O OD1 . ASP A 1 18 ? 5.341 23.843 1.861 1.00 33.97 ? 18 ASP A OD1 1 ATOM 146 O OD2 . ASP A 1 18 ? 5.333 22.240 0.350 1.00 36.46 ? 18 ASP A OD2 1 ATOM 147 N N . GLU A 1 19 ? 8.295 24.980 3.015 1.00 29.60 ? 19 GLU A N 1 ATOM 148 C CA . GLU A 1 19 ? 8.393 26.334 3.555 1.00 30.91 ? 19 GLU A CA 1 ATOM 149 C C . GLU A 1 19 ? 7.064 27.079 3.623 1.00 28.50 ? 19 GLU A C 1 ATOM 150 O O . GLU A 1 19 ? 6.805 27.784 4.599 1.00 26.21 ? 19 GLU A O 1 ATOM 151 C CB . GLU A 1 19 ? 9.389 27.162 2.730 1.00 35.85 ? 19 GLU A CB 1 ATOM 152 C CG . GLU A 1 19 ? 9.901 28.414 3.422 1.00 39.05 ? 19 GLU A CG 1 ATOM 153 C CD . GLU A 1 19 ? 10.886 28.100 4.530 1.00 43.30 ? 19 GLU A CD 1 ATOM 154 O OE1 . GLU A 1 19 ? 11.286 26.920 4.657 1.00 44.06 ? 19 GLU A OE1 1 ATOM 155 O OE2 . GLU A 1 19 ? 11.265 29.040 5.266 1.00 45.88 ? 19 GLU A OE2 1 ATOM 156 N N . THR A 1 20 ? 6.245 26.971 2.585 1.00 28.24 ? 20 THR A N 1 ATOM 157 C CA . THR A 1 20 ? 4.957 27.685 2.593 1.00 30.69 ? 20 THR A CA 1 ATOM 158 C C . THR A 1 20 ? 3.983 27.101 3.656 1.00 29.53 ? 20 THR A C 1 ATOM 159 O O . THR A 1 20 ? 3.319 27.862 4.379 1.00 27.26 ? 20 THR A O 1 ATOM 160 C CB . THR A 1 20 ? 4.311 27.840 1.177 1.00 32.97 ? 20 THR A CB 1 ATOM 161 O OG1 . THR A 1 20 ? 2.944 28.280 1.294 1.00 37.29 ? 20 THR A OG1 1 ATOM 162 C CG2 . THR A 1 20 ? 4.328 26.554 0.357 1.00 34.87 ? 20 THR A CG2 1 ATOM 163 N N . ALA A 1 21 ? 3.946 25.777 3.799 1.00 25.99 ? 21 ALA A N 1 ATOM 164 C CA . ALA A 1 21 ? 3.072 25.163 4.804 1.00 25.25 ? 21 ALA A CA 1 ATOM 165 C C . ALA A 1 21 ? 3.555 25.491 6.233 1.00 25.33 ? 21 ALA A C 1 ATOM 166 O O . ALA A 1 21 ? 2.746 25.764 7.131 1.00 23.25 ? 21 ALA A O 1 ATOM 167 C CB . ALA A 1 21 ? 2.994 23.678 4.587 1.00 25.21 ? 21 ALA A CB 1 ATOM 168 N N . ALA A 1 22 ? 4.879 25.516 6.406 1.00 24.19 ? 22 ALA A N 1 ATOM 169 C CA . ALA A 1 22 ? 5.507 25.795 7.668 1.00 24.12 ? 22 ALA A CA 1 ATOM 170 C C . ALA A 1 22 ? 5.168 27.187 8.104 1.00 24.46 ? 22 ALA A C 1 ATOM 171 O O . ALA A 1 22 ? 4.858 27.405 9.274 1.00 23.73 ? 22 ALA A O 1 ATOM 172 C CB . ALA A 1 22 ? 7.021 25.613 7.572 1.00 25.37 ? 22 ALA A CB 1 ATOM 173 N N . LYS A 1 23 ? 5.208 28.117 7.151 1.00 26.22 ? 23 LYS A N 1 ATOM 174 C CA . LYS A 1 23 ? 4.781 29.496 7.360 1.00 29.40 ? 23 LYS A CA 1 ATOM 175 C C . LYS A 1 23 ? 3.306 29.580 7.764 1.00 26.91 ? 23 LYS A C 1 ATOM 176 O O . LYS A 1 23 ? 2.972 30.167 8.796 1.00 23.90 ? 23 LYS A O 1 ATOM 177 C CB . LYS A 1 23 ? 5.019 30.308 6.080 1.00 34.07 ? 23 LYS A CB 1 ATOM 178 C CG . LYS A 1 23 ? 5.004 31.807 6.295 1.00 39.36 ? 23 LYS A CG 1 ATOM 179 C CD . LYS A 1 23 ? 5.336 32.547 5.008 1.00 42.28 ? 23 LYS A CD 1 ATOM 180 C CE . LYS A 1 23 ? 5.014 34.032 5.121 1.00 44.73 ? 23 LYS A CE 1 ATOM 181 N NZ . LYS A 1 23 ? 3.569 34.287 5.400 1.00 45.65 ? 23 LYS A NZ 1 ATOM 182 N N . ALA A 1 24 ? 2.431 28.982 6.952 1.00 25.36 ? 24 ALA A N 1 ATOM 183 C CA . ALA A 1 24 ? 0.989 29.007 7.223 1.00 25.09 ? 24 ALA A CA 1 ATOM 184 C C . ALA A 1 24 ? 0.687 28.520 8.644 1.00 25.94 ? 24 ALA A C 1 ATOM 185 O O . ALA A 1 24 ? -0.068 29.171 9.376 1.00 23.31 ? 24 ALA A O 1 ATOM 186 C CB . ALA A 1 24 ? 0.232 28.163 6.211 1.00 25.72 ? 24 ALA A CB 1 ATOM 187 N N . VAL A 1 25 ? 1.295 27.391 9.028 1.00 24.71 ? 25 VAL A N 1 ATOM 188 C CA . VAL A 1 25 ? 1.003 26.761 10.314 1.00 26.65 ? 25 VAL A CA 1 ATOM 189 C C . VAL A 1 25 ? 1.396 27.644 11.482 1.00 29.17 ? 25 VAL A C 1 ATOM 190 O O . VAL A 1 25 ? 0.628 27.808 12.412 1.00 29.31 ? 25 VAL A O 1 ATOM 191 C CB . VAL A 1 25 ? 1.644 25.365 10.426 1.00 27.13 ? 25 VAL A CB 1 ATOM 192 C CG1 . VAL A 1 25 ? 1.509 24.814 11.842 1.00 29.42 ? 25 VAL A CG1 1 ATOM 193 C CG2 . VAL A 1 25 ? 0.988 24.434 9.421 1.00 26.09 ? 25 VAL A CG2 1 ATOM 194 N N . LYS A 1 26 ? 2.566 28.260 11.411 1.00 31.18 ? 26 LYS A N 1 ATOM 195 C CA . LYS A 1 26 ? 2.952 29.218 12.437 1.00 35.71 ? 26 LYS A CA 1 ATOM 196 C C . LYS A 1 26 ? 1.953 30.378 12.543 1.00 36.38 ? 26 LYS A C 1 ATOM 197 O O . LYS A 1 26 ? 1.605 30.797 13.654 1.00 38.75 ? 26 LYS A O 1 ATOM 198 C CB . LYS A 1 26 ? 4.388 29.704 12.209 1.00 37.80 ? 26 LYS A CB 1 ATOM 199 C CG . LYS A 1 26 ? 5.407 28.604 12.503 1.00 38.22 ? 26 LYS A CG 1 ATOM 200 C CD . LYS A 1 26 ? 6.758 28.859 11.860 1.00 41.92 ? 26 LYS A CD 1 ATOM 201 C CE . LYS A 1 26 ? 7.853 28.054 12.554 1.00 45.71 ? 26 LYS A CE 1 ATOM 202 N NZ . LYS A 1 26 ? 9.142 28.031 11.798 1.00 47.74 ? 26 LYS A NZ 1 ATOM 203 N N . GLU A 1 27 ? 1.463 30.867 11.406 1.00 37.61 ? 27 GLU A N 1 ATOM 204 C CA . GLU A 1 27 ? 0.555 32.016 11.412 1.00 39.53 ? 27 GLU A CA 1 ATOM 205 C C . GLU A 1 27 ? -0.813 31.669 12.042 1.00 36.51 ? 27 GLU A C 1 ATOM 206 O O . GLU A 1 27 ? -1.394 32.457 12.804 1.00 34.04 ? 27 GLU A O 1 ATOM 207 C CB . GLU A 1 27 ? 0.392 32.606 10.003 1.00 43.18 ? 27 GLU A CB 1 ATOM 208 C CG . GLU A 1 27 ? 0.249 34.130 10.026 1.00 50.26 ? 27 GLU A CG 1 ATOM 209 C CD . GLU A 1 27 ? 0.247 34.772 8.643 1.00 58.09 ? 27 GLU A CD 1 ATOM 210 O OE1 . GLU A 1 27 ? -0.798 34.706 7.946 1.00 59.24 ? 27 GLU A OE1 1 ATOM 211 O OE2 . GLU A 1 27 ? 1.286 35.373 8.261 1.00 63.32 ? 27 GLU A OE2 1 ATOM 212 N N . LEU A 1 28 ? -1.307 30.474 11.738 1.00 33.30 ? 28 LEU A N 1 ATOM 213 C CA . LEU A 1 28 ? -2.564 29.974 12.305 1.00 29.08 ? 28 LEU A CA 1 ATOM 214 C C . LEU A 1 28 ? -2.476 29.525 13.767 1.00 26.63 ? 28 LEU A C 1 ATOM 215 O O . LEU A 1 28 ? -3.472 29.520 14.481 1.00 26.36 ? 28 LEU A O 1 ATOM 216 C CB . LEU A 1 28 ? -3.070 28.817 11.434 1.00 28.27 ? 28 LEU A CB 1 ATOM 217 C CG . LEU A 1 28 ? -3.496 29.231 10.036 1.00 27.84 ? 28 LEU A CG 1 ATOM 218 C CD1 . LEU A 1 28 ? -3.720 28.012 9.176 1.00 27.69 ? 28 LEU A CD1 1 ATOM 219 C CD2 . LEU A 1 28 ? -4.754 30.096 10.067 1.00 28.09 ? 28 LEU A CD2 1 ATOM 220 N N . LEU A 1 29 ? -1.302 29.122 14.224 1.00 26.51 ? 29 LEU A N 1 ATOM 221 C CA . LEU A 1 29 ? -1.180 28.612 15.584 1.00 25.87 ? 29 LEU A CA 1 ATOM 222 C C . LEU A 1 29 ? -1.192 29.798 16.562 1.00 29.39 ? 29 LEU A C 1 ATOM 223 O O . LEU A 1 29 ? -0.617 30.843 16.260 1.00 30.29 ? 29 LEU A O 1 ATOM 224 C CB . LEU A 1 29 ? 0.106 27.803 15.739 1.00 26.28 ? 29 LEU A CB 1 ATOM 225 C CG . LEU A 1 29 ? 0.190 26.374 15.152 1.00 24.62 ? 29 LEU A CG 1 ATOM 226 C CD1 . LEU A 1 29 ? 1.589 25.798 15.343 1.00 23.30 ? 29 LEU A CD1 1 ATOM 227 C CD2 . LEU A 1 29 ? -0.880 25.460 15.779 1.00 24.27 ? 29 LEU A CD2 1 ATOM 228 N N . PRO A 1 30 ? -1.854 29.652 17.721 1.00 29.88 ? 30 PRO A N 1 ATOM 229 C CA . PRO A 1 30 ? -1.759 30.726 18.700 1.00 34.10 ? 30 PRO A CA 1 ATOM 230 C C . PRO A 1 30 ? -0.326 30.927 19.209 1.00 36.12 ? 30 PRO A C 1 ATOM 231 O O . PRO A 1 30 ? 0.510 30.030 19.096 1.00 37.89 ? 30 PRO A O 1 ATOM 232 C CB . PRO A 1 30 ? -2.680 30.259 19.830 1.00 33.20 ? 30 PRO A CB 1 ATOM 233 C CG . PRO A 1 30 ? -2.708 28.782 19.697 1.00 33.04 ? 30 PRO A CG 1 ATOM 234 C CD . PRO A 1 30 ? -2.662 28.532 18.220 1.00 31.14 ? 30 PRO A CD 1 ATOM 235 N N . GLU A 1 31 ? -0.053 32.117 19.735 1.00 39.14 ? 31 GLU A N 1 ATOM 236 C CA . GLU A 1 31 ? 1.263 32.457 20.277 1.00 40.15 ? 31 GLU A CA 1 ATOM 237 C C . GLU A 1 31 ? 1.618 31.545 21.444 1.00 40.46 ? 31 GLU A C 1 ATOM 238 O O . GLU A 1 31 ? 2.787 31.267 21.694 1.00 38.73 ? 31 GLU A O 1 ATOM 239 C CB . GLU A 1 31 ? 1.269 33.921 20.746 1.00 42.18 ? 31 GLU A CB 1 ATOM 240 C CG . GLU A 1 31 ? 1.368 34.926 19.615 1.00 41.93 ? 31 GLU A CG 1 ATOM 241 C CD . GLU A 1 31 ? 2.686 34.811 18.881 1.00 41.79 ? 31 GLU A CD 1 ATOM 242 O OE1 . GLU A 1 31 ? 3.735 34.683 19.561 1.00 38.37 ? 31 GLU A OE1 1 ATOM 243 O OE2 . GLU A 1 31 ? 2.667 34.839 17.629 1.00 46.24 ? 31 GLU A OE2 1 ATOM 244 N N . SER A 1 32 ? 0.589 31.087 22.153 1.00 42.28 ? 32 SER A N 1 ATOM 245 C CA . SER A 1 32 ? 0.745 30.190 23.299 1.00 42.94 ? 32 SER A CA 1 ATOM 246 C C . SER A 1 32 ? 1.380 28.850 22.901 1.00 44.21 ? 32 SER A C 1 ATOM 247 O O . SER A 1 32 ? 2.066 28.195 23.707 1.00 43.35 ? 32 SER A O 1 ATOM 248 C CB . SER A 1 32 ? -0.624 29.942 23.920 1.00 44.84 ? 32 SER A CB 1 ATOM 249 O OG . SER A 1 32 ? -1.634 30.661 23.221 1.00 49.58 ? 32 SER A OG 1 ATOM 250 N N . ALA A 1 33 ? 1.129 28.438 21.659 1.00 41.85 ? 33 ALA A N 1 ATOM 251 C CA . ALA A 1 33 ? 1.759 27.248 21.094 1.00 39.62 ? 33 ALA A CA 1 ATOM 252 C C . ALA A 1 33 ? 3.283 27.405 21.017 1.00 41.29 ? 33 ALA A C 1 ATOM 253 O O . ALA A 1 33 ? 4.013 26.461 21.310 1.00 41.96 ? 33 ALA A O 1 ATOM 254 C CB . ALA A 1 33 ? 1.173 26.946 19.718 1.00 35.17 ? 33 ALA A CB 1 ATOM 255 N N . GLU A 1 34 ? 3.749 28.607 20.667 1.00 45.88 ? 34 GLU A N 1 ATOM 256 C CA . GLU A 1 34 ? 5.169 28.872 20.346 1.00 45.60 ? 34 GLU A CA 1 ATOM 257 C C . GLU A 1 34 ? 5.622 28.104 19.103 1.00 40.82 ? 34 GLU A C 1 ATOM 258 O O . GLU A 1 34 ? 6.702 27.510 19.089 1.00 35.45 ? 34 GLU A O 1 ATOM 259 C CB . GLU A 1 34 ? 6.094 28.551 21.519 1.00 49.90 ? 34 GLU A CB 1 ATOM 260 C CG . GLU A 1 34 ? 5.806 29.345 22.782 1.00 57.18 ? 34 GLU A CG 1 ATOM 261 C CD . GLU A 1 34 ? 6.667 28.884 23.940 1.00 61.75 ? 34 GLU A CD 1 ATOM 262 O OE1 . GLU A 1 34 ? 6.496 27.718 24.358 1.00 64.09 ? 34 GLU A OE1 1 ATOM 263 O OE2 . GLU A 1 34 ? 7.521 29.672 24.414 1.00 64.28 ? 34 GLU A OE2 1 ATOM 264 N N . GLY A 1 35 ? 4.771 28.103 18.080 1.00 37.81 ? 35 GLY A N 1 ATOM 265 C CA . GLY A 1 35 ? 5.090 27.504 16.782 1.00 34.14 ? 35 GLY A CA 1 ATOM 266 C C . GLY A 1 35 ? 4.997 25.982 16.695 1.00 32.89 ? 35 GLY A C 1 ATOM 267 O O . GLY A 1 35 ? 5.121 25.424 15.605 1.00 31.79 ? 35 GLY A O 1 ATOM 268 N N . ASP A 1 36 ? 4.754 25.325 17.832 1.00 31.42 ? 36 ASP A N 1 ATOM 269 C CA . ASP A 1 36 ? 4.757 23.855 17.954 1.00 30.34 ? 36 ASP A CA 1 ATOM 270 C C . ASP A 1 36 ? 3.333 23.272 17.722 1.00 28.08 ? 36 ASP A C 1 ATOM 271 O O . ASP A 1 36 ? 2.468 23.400 18.595 1.00 28.20 ? 36 ASP A O 1 ATOM 272 C CB . ASP A 1 36 ? 5.273 23.512 19.362 1.00 29.52 ? 36 ASP A CB 1 ATOM 273 C CG . ASP A 1 36 ? 5.490 22.017 19.591 1.00 32.38 ? 36 ASP A CG 1 ATOM 274 O OD1 . ASP A 1 36 ? 5.395 21.210 18.644 1.00 33.23 ? 36 ASP A OD1 1 ATOM 275 O OD2 . ASP A 1 36 ? 5.762 21.653 20.754 1.00 35.62 ? 36 ASP A OD2 1 ATOM 276 N N . LEU A 1 37 ? 3.104 22.655 16.561 1.00 24.50 ? 37 LEU A N 1 ATOM 277 C CA . LEU A 1 37 ? 1.820 22.007 16.219 1.00 25.90 ? 37 LEU A CA 1 ATOM 278 C C . LEU A 1 37 ? 1.423 20.965 17.258 1.00 23.46 ? 37 LEU A C 1 ATOM 279 O O . LEU A 1 37 ? 0.251 20.890 17.655 1.00 23.00 ? 37 LEU A O 1 ATOM 280 C CB . LEU A 1 37 ? 1.886 21.347 14.818 1.00 26.37 ? 37 LEU A CB 1 ATOM 281 C CG . LEU A 1 37 ? 0.597 20.875 14.120 1.00 27.26 ? 37 LEU A CG 1 ATOM 282 C CD1 . LEU A 1 37 ? -0.469 21.947 14.010 1.00 27.98 ? 37 LEU A CD1 1 ATOM 283 C CD2 . LEU A 1 37 ? 0.902 20.320 12.735 1.00 27.09 ? 37 LEU A CD2 1 ATOM 284 N N . SER A 1 38 ? 2.406 20.209 17.742 1.00 22.24 ? 38 SER A N 1 ATOM 285 C CA . SER A 1 38 ? 2.149 19.144 18.715 1.00 21.09 ? 38 SER A CA 1 ATOM 286 C C . SER A 1 38 ? 1.635 19.642 20.046 1.00 21.68 ? 38 SER A C 1 ATOM 287 O O . SER A 1 38 ? 1.064 18.873 20.770 1.00 21.02 ? 38 SER A O 1 ATOM 288 C CB . SER A 1 38 ? 3.359 18.221 18.945 1.00 21.60 ? 38 SER A CB 1 ATOM 289 O OG . SER A 1 38 ? 4.442 18.874 19.596 1.00 21.00 ? 38 SER A OG 1 ATOM 290 N N . SER A 1 39 ? 1.797 20.927 20.374 1.00 22.93 ? 39 SER A N 1 ATOM 291 C CA . SER A 1 39 ? 1.267 21.410 21.643 1.00 22.92 ? 39 SER A CA 1 ATOM 292 C C . SER A 1 39 ? -0.279 21.428 21.655 1.00 23.11 ? 39 SER A C 1 ATOM 293 O O . SER A 1 39 ? -0.900 21.392 22.714 1.00 24.57 ? 39 SER A O 1 ATOM 294 C CB . SER A 1 39 ? 1.833 22.801 21.984 1.00 23.91 ? 39 SER A CB 1 ATOM 295 O OG . SER A 1 39 ? 1.442 23.790 21.036 1.00 22.61 ? 39 SER A OG 1 ATOM 296 N N . LEU A 1 40 ? -0.903 21.480 20.484 1.00 22.01 ? 40 LEU A N 1 ATOM 297 C CA . LEU A 1 40 ? -2.343 21.585 20.400 1.00 21.18 ? 40 LEU A CA 1 ATOM 298 C C . LEU A 1 40 ? -3.017 20.437 19.628 1.00 22.02 ? 40 LEU A C 1 ATOM 299 O O . LEU A 1 40 ? -4.175 20.550 19.216 1.00 22.95 ? 40 LEU A O 1 ATOM 300 C CB . LEU A 1 40 ? -2.687 22.916 19.768 1.00 20.83 ? 40 LEU A CB 1 ATOM 301 C CG . LEU A 1 40 ? -2.494 24.090 20.726 1.00 22.15 ? 40 LEU A CG 1 ATOM 302 C CD1 . LEU A 1 40 ? -2.579 25.419 19.970 1.00 22.74 ? 40 LEU A CD1 1 ATOM 303 C CD2 . LEU A 1 40 ? -3.514 24.034 21.843 1.00 22.59 ? 40 LEU A CD2 1 ATOM 304 N N . CYS A 1 41 ? -2.317 19.340 19.419 1.00 23.45 ? 41 CYS A N 1 ATOM 305 C CA . CYS A 1 41 ? -2.884 18.267 18.596 1.00 24.69 ? 41 CYS A CA 1 ATOM 306 C C . CYS A 1 41 ? -3.841 17.368 19.379 1.00 22.34 ? 41 CYS A C 1 ATOM 307 O O . CYS A 1 41 ? -4.433 16.459 18.802 1.00 23.14 ? 41 CYS A O 1 ATOM 308 C CB . CYS A 1 41 ? -1.796 17.472 17.865 1.00 26.43 ? 41 CYS A CB 1 ATOM 309 S SG . CYS A 1 41 ? -1.093 18.329 16.429 1.00 33.13 ? 41 CYS A SG 1 ATOM 310 N N . LEU A 1 42 ? -4.023 17.625 20.669 1.00 21.40 ? 42 LEU A N 1 ATOM 311 C CA . LEU A 1 42 ? -5.084 16.947 21.446 1.00 22.13 ? 42 LEU A CA 1 ATOM 312 C C . LEU A 1 42 ? -6.257 17.859 21.682 1.00 21.24 ? 42 LEU A C 1 ATOM 313 O O . LEU A 1 42 ? -7.249 17.425 22.237 1.00 21.90 ? 42 LEU A O 1 ATOM 314 C CB . LEU A 1 42 ? -4.556 16.424 22.790 1.00 23.15 ? 42 LEU A CB 1 ATOM 315 C CG . LEU A 1 42 ? -5.182 15.129 23.321 1.00 22.51 ? 42 LEU A CG 1 ATOM 316 C CD1 . LEU A 1 42 ? -4.887 13.903 22.442 1.00 21.67 ? 42 LEU A CD1 1 ATOM 317 C CD2 . LEU A 1 42 ? -4.659 14.902 24.721 1.00 23.33 ? 42 LEU A CD2 1 ATOM 318 N N . TRP A 1 43 ? -6.157 19.120 21.238 1.00 21.52 ? 43 TRP A N 1 ATOM 319 C CA . TRP A 1 43 ? -7.217 20.109 21.450 1.00 21.79 ? 43 TRP A CA 1 ATOM 320 C C . TRP A 1 43 ? -8.621 19.598 21.061 1.00 20.62 ? 43 TRP A C 1 ATOM 321 O O . TRP A 1 43 ? -9.596 19.800 21.789 1.00 19.66 ? 43 TRP A O 1 ATOM 322 C CB . TRP A 1 43 ? -6.889 21.383 20.660 1.00 22.37 ? 43 TRP A CB 1 ATOM 323 C CG . TRP A 1 43 ? -7.983 22.408 20.628 1.00 21.53 ? 43 TRP A CG 1 ATOM 324 C CD1 . TRP A 1 43 ? -8.184 23.406 21.525 1.00 22.62 ? 43 TRP A CD1 1 ATOM 325 C CD2 . TRP A 1 43 ? -9.011 22.547 19.636 1.00 21.34 ? 43 TRP A CD2 1 ATOM 326 N NE1 . TRP A 1 43 ? -9.297 24.133 21.179 1.00 21.96 ? 43 TRP A NE1 1 ATOM 327 C CE2 . TRP A 1 43 ? -9.813 23.632 20.017 1.00 21.48 ? 43 TRP A CE2 1 ATOM 328 C CE3 . TRP A 1 43 ? -9.329 21.856 18.457 1.00 21.41 ? 43 TRP A CE3 1 ATOM 329 C CZ2 . TRP A 1 43 ? -10.901 24.066 19.252 1.00 21.52 ? 43 TRP A CZ2 1 ATOM 330 C CZ3 . TRP A 1 43 ? -10.405 22.269 17.716 1.00 20.78 ? 43 TRP A CZ3 1 ATOM 331 C CH2 . TRP A 1 43 ? -11.191 23.365 18.121 1.00 22.07 ? 43 TRP A CH2 1 ATOM 332 N N . ALA A 1 44 ? -8.725 18.935 19.917 1.00 19.52 ? 44 ALA A N 1 ATOM 333 C CA . ALA A 1 44 ? -10.007 18.409 19.495 1.00 19.07 ? 44 ALA A CA 1 ATOM 334 C C . ALA A 1 44 ? -10.646 17.463 20.553 1.00 18.89 ? 44 ALA A C 1 ATOM 335 O O . ALA A 1 44 ? -11.870 17.376 20.661 1.00 18.92 ? 44 ALA A O 1 ATOM 336 C CB . ALA A 1 44 ? -9.857 17.697 18.171 1.00 19.01 ? 44 ALA A CB 1 ATOM 337 N N . ASP A 1 45 ? -9.843 16.764 21.343 1.00 18.60 ? 45 ASP A N 1 ATOM 338 C CA . ASP A 1 45 ? -10.425 15.823 22.317 1.00 19.27 ? 45 ASP A CA 1 ATOM 339 C C . ASP A 1 45 ? -11.060 16.582 23.504 1.00 21.14 ? 45 ASP A C 1 ATOM 340 O O . ASP A 1 45 ? -11.845 16.014 24.258 1.00 21.10 ? 45 ASP A O 1 ATOM 341 C CB . ASP A 1 45 ? -9.389 14.813 22.828 1.00 18.05 ? 45 ASP A CB 1 ATOM 342 C CG . ASP A 1 45 ? -9.238 13.566 21.923 1.00 17.33 ? 45 ASP A CG 1 ATOM 343 O OD1 . ASP A 1 45 ? -10.174 13.204 21.156 1.00 16.67 ? 45 ASP A OD1 1 ATOM 344 O OD2 . ASP A 1 45 ? -8.161 12.950 22.004 1.00 14.67 ? 45 ASP A OD2 1 ATOM 345 N N . ARG A 1 46 ? -10.713 17.856 23.648 1.00 22.59 ? 46 ARG A N 1 ATOM 346 C CA . ARG A 1 46 ? -11.187 18.698 24.750 1.00 25.34 ? 46 ARG A CA 1 ATOM 347 C C . ARG A 1 46 ? -12.460 19.436 24.392 1.00 24.38 ? 46 ARG A C 1 ATOM 348 O O . ARG A 1 46 ? -13.055 20.044 25.265 1.00 24.04 ? 46 ARG A O 1 ATOM 349 C CB . ARG A 1 46 ? -10.126 19.751 25.137 1.00 28.09 ? 46 ARG A CB 1 ATOM 350 C CG . ARG A 1 46 ? -8.811 19.155 25.588 1.00 31.97 ? 46 ARG A CG 1 ATOM 351 C CD . ARG A 1 46 ? -7.808 20.216 26.031 1.00 37.09 ? 46 ARG A CD 1 ATOM 352 N NE . ARG A 1 46 ? -6.934 20.725 24.959 1.00 40.81 ? 46 ARG A NE 1 ATOM 353 C CZ . ARG A 1 46 ? -5.688 20.305 24.718 1.00 44.33 ? 46 ARG A CZ 1 ATOM 354 N NH1 . ARG A 1 46 ? -5.132 19.338 25.456 1.00 43.04 ? 46 ARG A NH1 1 ATOM 355 N NH2 . ARG A 1 46 ? -4.985 20.860 23.733 1.00 46.45 ? 46 ARG A NH2 1 ATOM 356 N N . VAL A 1 47 ? -12.887 19.380 23.126 1.00 24.08 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? -14.095 20.103 22.719 1.00 23.44 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? -15.242 19.198 22.250 1.00 22.41 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? -16.097 19.642 21.515 1.00 23.05 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? -13.772 21.215 21.682 1.00 24.13 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? -12.707 22.137 22.236 1.00 24.43 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? -13.337 20.644 20.345 1.00 24.65 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? -15.271 17.936 22.670 1.00 22.45 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? -16.371 17.035 22.287 1.00 24.16 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? -17.755 17.426 22.845 1.00 25.22 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? -18.765 17.075 22.259 1.00 27.71 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? -16.082 15.589 22.697 1.00 25.60 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? -14.834 15.002 22.055 1.00 27.54 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? -14.723 13.524 22.351 1.00 28.35 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? -13.516 12.907 21.703 1.00 28.74 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? -13.315 11.542 22.263 1.00 30.88 ? 48 LYS A NZ 1 ATOM 372 N N . PHE A 1 49 ? -17.786 18.128 23.971 1.00 25.21 ? 49 PHE A N 1 ATOM 373 C CA . PHE A 1 49 ? -19.023 18.588 24.603 1.00 25.99 ? 49 PHE A CA 1 ATOM 374 C C . PHE A 1 49 ? -19.220 20.093 24.459 1.00 26.09 ? 49 PHE A C 1 ATOM 375 O O . PHE A 1 49 ? -20.350 20.553 24.303 1.00 22.93 ? 49 PHE A O 1 ATOM 376 C CB . PHE A 1 49 ? -19.070 18.128 26.066 1.00 25.94 ? 49 PHE A CB 1 ATOM 377 C CG . PHE A 1 49 ? -19.216 16.638 26.190 1.00 26.96 ? 49 PHE A CG 1 ATOM 378 C CD1 . PHE A 1 49 ? -18.113 15.816 26.131 1.00 26.76 ? 49 PHE A CD1 1 ATOM 379 C CD2 . PHE A 1 49 ? -20.466 16.059 26.251 1.00 27.92 ? 49 PHE A CD2 1 ATOM 380 C CE1 . PHE A 1 49 ? -18.253 14.435 26.186 1.00 27.97 ? 49 PHE A CE1 1 ATOM 381 C CE2 . PHE A 1 49 ? -20.610 14.687 26.305 1.00 28.36 ? 49 PHE A CE2 1 ATOM 382 C CZ . PHE A 1 49 ? -19.501 13.872 26.271 1.00 27.61 ? 49 PHE A CZ 1 ATOM 383 N N . ARG A 1 50 ? -18.123 20.845 24.452 1.00 25.22 ? 50 ARG A N 1 ATOM 384 C CA . ARG A 1 50 ? -18.171 22.236 24.046 1.00 28.62 ? 50 ARG A CA 1 ATOM 385 C C . ARG A 1 50 ? -18.796 22.430 22.639 1.00 26.71 ? 50 ARG A C 1 ATOM 386 O O . ARG A 1 50 ? -19.604 23.336 22.417 1.00 27.14 ? 50 ARG A O 1 ATOM 387 C CB . ARG A 1 50 ? -16.754 22.808 24.077 1.00 33.30 ? 50 ARG A CB 1 ATOM 388 C CG . ARG A 1 50 ? -16.687 24.326 24.151 1.00 37.19 ? 50 ARG A CG 1 ATOM 389 C CD . ARG A 1 50 ? -15.235 24.799 24.171 1.00 40.23 ? 50 ARG A CD 1 ATOM 390 N NE . ARG A 1 50 ? -15.084 25.997 24.985 1.00 46.97 ? 50 ARG A NE 1 ATOM 391 C CZ . ARG A 1 50 ? -14.932 26.018 26.315 1.00 51.00 ? 50 ARG A CZ 1 ATOM 392 N NH1 . ARG A 1 50 ? -14.899 24.890 27.042 1.00 51.97 ? 50 ARG A NH1 1 ATOM 393 N NH2 . ARG A 1 50 ? -14.809 27.190 26.925 1.00 53.76 ? 50 ARG A NH2 1 ATOM 394 N N . TYR A 1 51 ? -18.388 21.578 21.707 1.00 24.44 ? 51 TYR A N 1 ATOM 395 C CA . TYR A 1 51 ? -18.912 21.506 20.356 1.00 23.63 ? 51 TYR A CA 1 ATOM 396 C C . TYR A 1 51 ? -19.418 20.079 20.208 1.00 24.90 ? 51 TYR A C 1 ATOM 397 O O . TYR A 1 51 ? -18.740 19.219 19.642 1.00 24.11 ? 51 TYR A O 1 ATOM 398 C CB . TYR A 1 51 ? -17.783 21.717 19.356 1.00 24.37 ? 51 TYR A CB 1 ATOM 399 C CG . TYR A 1 51 ? -17.107 23.077 19.339 1.00 27.04 ? 51 TYR A CG 1 ATOM 400 C CD1 . TYR A 1 51 ? -17.818 24.245 19.573 1.00 28.52 ? 51 TYR A CD1 1 ATOM 401 C CD2 . TYR A 1 51 ? -15.748 23.193 19.029 1.00 28.45 ? 51 TYR A CD2 1 ATOM 402 C CE1 . TYR A 1 51 ? -17.196 25.502 19.557 1.00 29.55 ? 51 TYR A CE1 1 ATOM 403 C CE2 . TYR A 1 51 ? -15.120 24.429 18.996 1.00 29.36 ? 51 TYR A CE2 1 ATOM 404 C CZ . TYR A 1 51 ? -15.846 25.597 19.248 1.00 29.99 ? 51 TYR A CZ 1 ATOM 405 O OH . TYR A 1 51 ? -15.221 26.842 19.207 1.00 26.53 ? 51 TYR A OH 1 ATOM 406 N N . HIS A 1 52 ? -20.601 19.806 20.748 1.00 24.43 ? 52 HIS A N 1 ATOM 407 C CA . HIS A 1 52 ? -21.094 18.454 20.804 1.00 22.89 ? 52 HIS A CA 1 ATOM 408 C C . HIS A 1 52 ? -21.167 17.854 19.404 1.00 22.41 ? 52 HIS A C 1 ATOM 409 O O . HIS A 1 52 ? -21.060 16.638 19.241 1.00 21.01 ? 52 HIS A O 1 ATOM 410 C CB . HIS A 1 52 ? -22.484 18.402 21.424 1.00 23.31 ? 52 HIS A CB 1 ATOM 411 C CG . HIS A 1 52 ? -23.567 18.543 20.417 1.00 23.43 ? 52 HIS A CG 1 ATOM 412 N ND1 . HIS A 1 52 ? -23.918 19.759 19.882 1.00 24.39 ? 52 HIS A ND1 1 ATOM 413 C CD2 . HIS A 1 52 ? -24.321 17.615 19.783 1.00 23.57 ? 52 HIS A CD2 1 ATOM 414 C CE1 . HIS A 1 52 ? -24.871 19.582 18.983 1.00 24.21 ? 52 HIS A CE1 1 ATOM 415 N NE2 . HIS A 1 52 ? -25.116 18.285 18.891 1.00 24.83 ? 52 HIS A NE2 1 ATOM 416 N N . TRP A 1 53 ? -21.383 18.704 18.409 1.00 21.48 ? 53 TRP A N 1 ATOM 417 C CA . TRP A 1 53 ? -21.451 18.278 17.007 1.00 22.84 ? 53 TRP A CA 1 ATOM 418 C C . TRP A 1 53 ? -20.141 17.649 16.478 1.00 22.49 ? 53 TRP A C 1 ATOM 419 O O . TRP A 1 53 ? -20.140 16.964 15.419 1.00 20.07 ? 53 TRP A O 1 ATOM 420 C CB . TRP A 1 53 ? -21.868 19.467 16.108 1.00 22.30 ? 53 TRP A CB 1 ATOM 421 C CG . TRP A 1 53 ? -21.121 20.780 16.380 1.00 22.17 ? 53 TRP A CG 1 ATOM 422 C CD1 . TRP A 1 53 ? -21.584 21.857 17.078 1.00 23.28 ? 53 TRP A CD1 1 ATOM 423 C CD2 . TRP A 1 53 ? -19.807 21.132 15.929 1.00 22.68 ? 53 TRP A CD2 1 ATOM 424 N NE1 . TRP A 1 53 ? -20.642 22.860 17.094 1.00 21.90 ? 53 TRP A NE1 1 ATOM 425 C CE2 . TRP A 1 53 ? -19.528 22.425 16.417 1.00 22.75 ? 53 TRP A CE2 1 ATOM 426 C CE3 . TRP A 1 53 ? -18.840 20.478 15.162 1.00 23.68 ? 53 TRP A CE3 1 ATOM 427 C CZ2 . TRP A 1 53 ? -18.321 23.083 16.152 1.00 23.20 ? 53 TRP A CZ2 1 ATOM 428 C CZ3 . TRP A 1 53 ? -17.629 21.135 14.898 1.00 24.99 ? 53 TRP A CZ3 1 ATOM 429 C CH2 . TRP A 1 53 ? -17.389 22.425 15.387 1.00 24.45 ? 53 TRP A CH2 1 ATOM 430 N N . SER A 1 54 ? -19.037 17.915 17.191 1.00 22.24 ? 54 SER A N 1 ATOM 431 C CA . SER A 1 54 ? -17.712 17.373 16.811 1.00 22.08 ? 54 SER A CA 1 ATOM 432 C C . SER A 1 54 ? -17.416 15.918 17.218 1.00 22.37 ? 54 SER A C 1 ATOM 433 O O . SER A 1 54 ? -16.454 15.363 16.726 1.00 24.46 ? 54 SER A O 1 ATOM 434 C CB . SER A 1 54 ? -16.567 18.281 17.317 1.00 21.54 ? 54 SER A CB 1 ATOM 435 O OG . SER A 1 54 ? -16.371 18.224 18.728 1.00 20.49 ? 54 SER A OG 1 ATOM 436 N N . SER A 1 55 ? -18.205 15.295 18.103 1.00 22.28 ? 55 SER A N 1 ATOM 437 C CA . SER A 1 55 ? -17.760 14.060 18.723 1.00 19.66 ? 55 SER A CA 1 ATOM 438 C C . SER A 1 55 ? -17.805 12.833 17.806 1.00 20.32 ? 55 SER A C 1 ATOM 439 O O . SER A 1 55 ? -16.906 11.971 17.899 1.00 18.86 ? 55 SER A O 1 ATOM 440 C CB . SER A 1 55 ? -18.413 13.801 20.113 1.00 20.96 ? 55 SER A CB 1 ATOM 441 O OG . SER A 1 55 ? -19.803 13.580 20.059 1.00 23.01 ? 55 SER A OG 1 ATOM 442 N N . PRO A 1 56 ? -18.818 12.738 16.908 1.00 19.93 ? 56 PRO A N 1 ATOM 443 C CA . PRO A 1 56 ? -18.785 11.719 15.853 1.00 18.52 ? 56 PRO A CA 1 ATOM 444 C C . PRO A 1 56 ? -17.617 11.785 14.862 1.00 17.84 ? 56 PRO A C 1 ATOM 445 O O . PRO A 1 56 ? -17.391 10.848 14.058 1.00 16.23 ? 56 PRO A O 1 ATOM 446 C CB . PRO A 1 56 ? -20.091 11.958 15.087 1.00 20.46 ? 56 PRO A CB 1 ATOM 447 C CG . PRO A 1 56 ? -20.974 12.658 16.020 1.00 21.59 ? 56 PRO A CG 1 ATOM 448 C CD . PRO A 1 56 ? -20.071 13.513 16.877 1.00 21.55 ? 56 PRO A CD 1 ATOM 449 N N . LEU A 1 57 ? -16.907 12.894 14.880 1.00 17.45 ? 57 LEU A N 1 ATOM 450 C CA . LEU A 1 57 ? -15.936 13.217 13.855 1.00 16.48 ? 57 LEU A CA 1 ATOM 451 C C . LEU A 1 57 ? -14.604 12.598 14.170 1.00 16.01 ? 57 LEU A C 1 ATOM 452 O O . LEU A 1 57 ? -13.685 12.704 13.368 1.00 16.57 ? 57 LEU A O 1 ATOM 453 C CB . LEU A 1 57 ? -15.757 14.744 13.732 1.00 15.71 ? 57 LEU A CB 1 ATOM 454 C CG . LEU A 1 57 ? -17.033 15.546 13.438 1.00 15.88 ? 57 LEU A CG 1 ATOM 455 C CD1 . LEU A 1 57 ? -16.788 17.041 13.362 1.00 15.47 ? 57 LEU A CD1 1 ATOM 456 C CD2 . LEU A 1 57 ? -17.698 15.065 12.153 1.00 16.53 ? 57 LEU A CD2 1 ATOM 457 N N . HIS A 1 58 ? -14.497 11.981 15.337 1.00 15.42 ? 58 HIS A N 1 ATOM 458 C CA . HIS A 1 58 ? -13.251 11.369 15.761 1.00 16.40 ? 58 HIS A CA 1 ATOM 459 C C . HIS A 1 58 ? -13.073 9.925 15.252 1.00 16.07 ? 58 HIS A C 1 ATOM 460 O O . HIS A 1 58 ? -11.996 9.385 15.376 1.00 17.44 ? 58 HIS A O 1 ATOM 461 C CB . HIS A 1 58 ? -13.146 11.388 17.262 1.00 16.57 ? 58 HIS A CB 1 ATOM 462 C CG . HIS A 1 58 ? -12.965 12.760 17.834 1.00 17.27 ? 58 HIS A CG 1 ATOM 463 N ND1 . HIS A 1 58 ? -11.776 13.183 18.368 1.00 17.76 ? 58 HIS A ND1 1 ATOM 464 C CD2 . HIS A 1 58 ? -13.810 13.810 17.928 1.00 17.42 ? 58 HIS A CD2 1 ATOM 465 C CE1 . HIS A 1 58 ? -11.892 14.435 18.776 1.00 17.41 ? 58 HIS A CE1 1 ATOM 466 N NE2 . HIS A 1 58 ? -13.119 14.837 18.523 1.00 17.16 ? 58 HIS A NE2 1 ATOM 467 N N . TYR A 1 59 ? -14.107 9.318 14.682 1.00 16.68 ? 59 TYR A N 1 ATOM 468 C CA . TYR A 1 59 ? -14.066 7.867 14.371 1.00 18.28 ? 59 TYR A CA 1 ATOM 469 C C . TYR A 1 59 ? -14.997 7.490 13.234 1.00 18.82 ? 59 TYR A C 1 ATOM 470 O O . TYR A 1 59 ? -15.702 8.333 12.706 1.00 21.04 ? 59 TYR A O 1 ATOM 471 C CB . TYR A 1 59 ? -14.445 7.043 15.622 1.00 18.30 ? 59 TYR A CB 1 ATOM 472 C CG . TYR A 1 59 ? -15.799 7.415 16.158 1.00 20.49 ? 59 TYR A CG 1 ATOM 473 C CD1 . TYR A 1 59 ? -16.977 6.838 15.650 1.00 21.37 ? 59 TYR A CD1 1 ATOM 474 C CD2 . TYR A 1 59 ? -15.922 8.420 17.129 1.00 22.23 ? 59 TYR A CD2 1 ATOM 475 C CE1 . TYR A 1 59 ? -18.230 7.200 16.146 1.00 22.44 ? 59 TYR A CE1 1 ATOM 476 C CE2 . TYR A 1 59 ? -17.163 8.792 17.627 1.00 23.41 ? 59 TYR A CE2 1 ATOM 477 C CZ . TYR A 1 59 ? -18.312 8.193 17.126 1.00 24.33 ? 59 TYR A CZ 1 ATOM 478 O OH . TYR A 1 59 ? -19.507 8.620 17.638 1.00 26.94 ? 59 TYR A OH 1 ATOM 479 N N . ILE A 1 60 ? -14.932 6.222 12.836 1.00 21.06 ? 60 ILE A N 1 ATOM 480 C CA . ILE A 1 60 ? -15.902 5.591 11.941 1.00 23.45 ? 60 ILE A CA 1 ATOM 481 C C . ILE A 1 60 ? -16.366 4.244 12.527 1.00 22.35 ? 60 ILE A C 1 ATOM 482 O O . ILE A 1 60 ? -15.586 3.434 13.023 1.00 22.56 ? 60 ILE A O 1 ATOM 483 C CB . ILE A 1 60 ? -15.327 5.329 10.519 1.00 23.09 ? 60 ILE A CB 1 ATOM 484 C CG1 . ILE A 1 60 ? -14.919 6.628 9.840 1.00 21.77 ? 60 ILE A CG1 1 ATOM 485 C CG2 . ILE A 1 60 ? -16.336 4.590 9.653 1.00 23.13 ? 60 ILE A CG2 1 ATOM 486 C CD1 . ILE A 1 60 ? -13.936 6.475 8.701 1.00 20.27 ? 60 ILE A CD1 1 ATOM 487 N N . ASN A 1 61 ? -17.663 4.033 12.462 1.00 24.97 ? 61 ASN A N 1 ATOM 488 C CA . ASN A 1 61 ? -18.278 2.787 12.870 1.00 27.38 ? 61 ASN A CA 1 ATOM 489 C C . ASN A 1 61 ? -18.606 1.974 11.634 1.00 29.38 ? 61 ASN A C 1 ATOM 490 O O . ASN A 1 61 ? -19.237 2.476 10.710 1.00 32.87 ? 61 ASN A O 1 ATOM 491 C CB . ASN A 1 61 ? -19.578 3.056 13.632 1.00 28.35 ? 61 ASN A CB 1 ATOM 492 C CG . ASN A 1 61 ? -19.360 3.264 15.117 1.00 31.09 ? 61 ASN A CG 1 ATOM 493 O OD1 . ASN A 1 61 ? -20.060 4.069 15.740 1.00 35.51 ? 61 ASN A OD1 1 ATOM 494 N ND2 . ASN A 1 61 ? -18.387 2.555 15.698 1.00 31.71 ? 61 ASN A ND2 1 ATOM 495 N N . THR A 1 62 ? -18.189 0.720 11.621 1.00 29.95 ? 62 THR A N 1 ATOM 496 C CA . THR A 1 62 ? -18.580 -0.188 10.563 1.00 31.33 ? 62 THR A CA 1 ATOM 497 C C . THR A 1 62 ? -19.416 -1.341 11.137 1.00 32.05 ? 62 THR A C 1 ATOM 498 O O . THR A 1 62 ? -19.494 -1.519 12.377 1.00 28.70 ? 62 THR A O 1 ATOM 499 C CB . THR A 1 62 ? -17.352 -0.710 9.788 1.00 32.72 ? 62 THR A CB 1 ATOM 500 O OG1 . THR A 1 62 ? -16.674 -1.703 10.562 1.00 33.68 ? 62 THR A OG1 1 ATOM 501 C CG2 . THR A 1 62 ? -16.390 0.439 9.465 1.00 33.85 ? 62 THR A CG2 1 ATOM 502 N N . PRO A 1 63 ? -20.099 -2.090 10.243 1.00 33.10 ? 63 PRO A N 1 ATOM 503 C CA . PRO A 1 63 ? -20.778 -3.313 10.656 1.00 35.90 ? 63 PRO A CA 1 ATOM 504 C C . PRO A 1 63 ? -19.739 -4.348 11.045 1.00 37.32 ? 63 PRO A C 1 ATOM 505 O O . PRO A 1 63 ? -18.540 -4.081 10.910 1.00 38.61 ? 63 PRO A O 1 ATOM 506 C CB . PRO A 1 63 ? -21.541 -3.749 9.385 1.00 36.79 ? 63 PRO A CB 1 ATOM 507 C CG . PRO A 1 63 ? -21.661 -2.511 8.571 1.00 35.11 ? 63 PRO A CG 1 ATOM 508 C CD . PRO A 1 63 ? -20.376 -1.780 8.829 1.00 35.02 ? 63 PRO A CD 1 ATOM 509 N N . ASP A 1 64 ? -20.171 -5.514 11.515 1.00 39.22 ? 64 ASP A N 1 ATOM 510 C CA . ASP A 1 64 ? -19.219 -6.541 11.908 1.00 41.72 ? 64 ASP A CA 1 ATOM 511 C C . ASP A 1 64 ? -18.630 -7.126 10.656 1.00 42.15 ? 64 ASP A C 1 ATOM 512 O O . ASP A 1 64 ? -19.083 -8.166 10.184 1.00 43.93 ? 64 ASP A O 1 ATOM 513 C CB . ASP A 1 64 ? -19.883 -7.637 12.741 1.00 45.66 ? 64 ASP A CB 1 ATOM 514 C CG . ASP A 1 64 ? -20.280 -7.163 14.118 1.00 48.31 ? 64 ASP A CG 1 ATOM 515 O OD1 . ASP A 1 64 ? -20.052 -5.967 14.434 1.00 50.14 ? 64 ASP A OD1 1 ATOM 516 O OD2 . ASP A 1 64 ? -20.817 -7.996 14.887 1.00 53.61 ? 64 ASP A OD2 1 ATOM 517 N N . ALA A 1 65 ? -17.638 -6.437 10.098 1.00 41.28 ? 65 ALA A N 1 ATOM 518 C CA . ALA A 1 65 ? -16.976 -6.892 8.869 1.00 40.62 ? 65 ALA A CA 1 ATOM 519 C C . ALA A 1 65 ? -15.754 -6.029 8.597 1.00 38.92 ? 65 ALA A C 1 ATOM 520 O O . ALA A 1 65 ? -15.646 -4.913 9.116 1.00 40.21 ? 65 ALA A O 1 ATOM 521 C CB . ALA A 1 65 ? -17.946 -6.836 7.693 1.00 41.19 ? 65 ALA A CB 1 ATOM 522 N N . CYS A 1 66 ? -14.842 -6.544 7.784 1.00 36.56 ? 66 CYS A N 1 ATOM 523 C CA . CYS A 1 66 ? -13.558 -5.897 7.554 1.00 36.84 ? 66 CYS A CA 1 ATOM 524 C C . CYS A 1 66 ? -13.562 -5.075 6.271 1.00 35.25 ? 66 CYS A C 1 ATOM 525 O O . CYS A 1 66 ? -12.785 -5.322 5.348 1.00 35.23 ? 66 CYS A O 1 ATOM 526 C CB . CYS A 1 66 ? -12.448 -6.942 7.517 1.00 37.57 ? 66 CYS A CB 1 ATOM 527 S SG . CYS A 1 66 ? -12.400 -7.975 8.997 1.00 45.33 ? 66 CYS A SG 1 ATOM 528 N N . SER A 1 67 ? -14.442 -4.085 6.227 1.00 33.37 ? 67 SER A N 1 ATOM 529 C CA . SER A 1 67 ? -14.509 -3.195 5.088 1.00 31.49 ? 67 SER A CA 1 ATOM 530 C C . SER A 1 67 ? -14.983 -1.839 5.541 1.00 27.54 ? 67 SER A C 1 ATOM 531 O O . SER A 1 67 ? -15.709 -1.713 6.526 1.00 26.29 ? 67 SER A O 1 ATOM 532 C CB . SER A 1 67 ? -15.494 -3.719 4.041 1.00 32.92 ? 67 SER A CB 1 ATOM 533 O OG . SER A 1 67 ? -16.821 -3.721 4.551 1.00 32.76 ? 67 SER A OG 1 ATOM 534 N N . TYR A 1 68 ? -14.608 -0.837 4.766 1.00 24.32 ? 68 TYR A N 1 ATOM 535 C CA . TYR A 1 68 ? -15.138 0.474 4.927 1.00 23.47 ? 68 TYR A CA 1 ATOM 536 C C . TYR A 1 68 ? -15.617 0.984 3.583 1.00 24.20 ? 68 TYR A C 1 ATOM 537 O O . TYR A 1 68 ? -14.910 0.867 2.594 1.00 24.14 ? 68 TYR A O 1 ATOM 538 C CB . TYR A 1 68 ? -14.063 1.380 5.487 1.00 21.94 ? 68 TYR A CB 1 ATOM 539 C CG . TYR A 1 68 ? -14.362 2.829 5.262 1.00 21.79 ? 68 TYR A CG 1 ATOM 540 C CD1 . TYR A 1 68 ? -15.220 3.521 6.109 1.00 20.19 ? 68 TYR A CD1 1 ATOM 541 C CD2 . TYR A 1 68 ? -13.800 3.502 4.194 1.00 20.90 ? 68 TYR A CD2 1 ATOM 542 C CE1 . TYR A 1 68 ? -15.500 4.852 5.910 1.00 21.12 ? 68 TYR A CE1 1 ATOM 543 C CE2 . TYR A 1 68 ? -14.081 4.828 3.976 1.00 22.06 ? 68 TYR A CE2 1 ATOM 544 C CZ . TYR A 1 68 ? -14.923 5.510 4.836 1.00 21.45 ? 68 TYR A CZ 1 ATOM 545 O OH . TYR A 1 68 ? -15.183 6.846 4.604 1.00 21.50 ? 68 TYR A OH 1 ATOM 546 N N . GLN A 1 69 ? -16.818 1.554 3.565 1.00 26.33 ? 69 GLN A N 1 ATOM 547 C CA . GLN A 1 69 ? -17.310 2.335 2.422 1.00 27.06 ? 69 GLN A CA 1 ATOM 548 C C . GLN A 1 69 ? -17.832 3.651 2.934 1.00 25.19 ? 69 GLN A C 1 ATOM 549 O O . GLN A 1 69 ? -18.584 3.666 3.907 1.00 23.78 ? 69 GLN A O 1 ATOM 550 C CB . GLN A 1 69 ? -18.446 1.620 1.704 1.00 29.51 ? 69 GLN A CB 1 ATOM 551 C CG . GLN A 1 69 ? -18.261 0.119 1.616 1.00 33.06 ? 69 GLN A CG 1 ATOM 552 C CD . GLN A 1 69 ? -18.471 -0.396 0.225 1.00 36.78 ? 69 GLN A CD 1 ATOM 553 O OE1 . GLN A 1 69 ? -17.595 -0.273 -0.622 1.00 42.29 ? 69 GLN A OE1 1 ATOM 554 N NE2 . GLN A 1 69 ? -19.624 -1.000 -0.017 1.00 40.38 ? 69 GLN A NE2 1 ATOM 555 N N . TYR A 1 70 ? -17.494 4.736 2.246 1.00 24.85 ? 70 TYR A N 1 ATOM 556 C CA . TYR A 1 70 ? -17.896 6.075 2.673 1.00 25.23 ? 70 TYR A CA 1 ATOM 557 C C . TYR A 1 70 ? -19.394 6.275 2.787 1.00 26.89 ? 70 TYR A C 1 ATOM 558 O O . TYR A 1 70 ? -19.895 6.811 3.787 1.00 26.62 ? 70 TYR A O 1 ATOM 559 C CB . TYR A 1 70 ? -17.362 7.104 1.703 1.00 26.51 ? 70 TYR A CB 1 ATOM 560 C CG . TYR A 1 70 ? -17.691 8.533 2.071 1.00 28.07 ? 70 TYR A CG 1 ATOM 561 C CD1 . TYR A 1 70 ? -16.868 9.244 2.935 1.00 27.81 ? 70 TYR A CD1 1 ATOM 562 C CD2 . TYR A 1 70 ? -18.830 9.177 1.551 1.00 27.73 ? 70 TYR A CD2 1 ATOM 563 C CE1 . TYR A 1 70 ? -17.147 10.564 3.280 1.00 27.27 ? 70 TYR A CE1 1 ATOM 564 C CE2 . TYR A 1 70 ? -19.117 10.492 1.887 1.00 29.27 ? 70 TYR A CE2 1 ATOM 565 C CZ . TYR A 1 70 ? -18.271 11.179 2.765 1.00 28.19 ? 70 TYR A CZ 1 ATOM 566 O OH . TYR A 1 70 ? -18.506 12.496 3.117 1.00 32.12 ? 70 TYR A OH 1 ATOM 567 N N . ASN A 1 71 ? -20.117 5.882 1.751 1.00 28.24 ? 71 ASN A N 1 ATOM 568 C CA . ASN A 1 71 ? -21.531 6.193 1.688 1.00 29.33 ? 71 ASN A CA 1 ATOM 569 C C . ASN A 1 71 ? -22.276 5.330 2.714 1.00 27.38 ? 71 ASN A C 1 ATOM 570 O O . ASN A 1 71 ? -23.185 5.791 3.378 1.00 26.03 ? 71 ASN A O 1 ATOM 571 C CB . ASN A 1 71 ? -22.062 6.061 0.239 1.00 30.96 ? 71 ASN A CB 1 ATOM 572 C CG . ASN A 1 71 ? -21.264 6.922 -0.766 1.00 34.87 ? 71 ASN A CG 1 ATOM 573 O OD1 . ASN A 1 71 ? -20.308 6.458 -1.397 1.00 35.81 ? 71 ASN A OD1 1 ATOM 574 N ND2 . ASN A 1 71 ? -21.623 8.195 -0.879 1.00 36.24 ? 71 ASN A ND2 1 ATOM 575 N N . ARG A 1 72 ? -21.814 4.104 2.893 1.00 26.48 ? 72 ARG A N 1 ATOM 576 C CA . ARG A 1 72 ? -22.337 3.220 3.909 1.00 27.83 ? 72 ARG A CA 1 ATOM 577 C C . ARG A 1 72 ? -21.985 3.623 5.355 1.00 27.04 ? 72 ARG A C 1 ATOM 578 O O . ARG A 1 72 ? -22.861 3.685 6.245 1.00 27.84 ? 72 ARG A O 1 ATOM 579 C CB . ARG A 1 72 ? -21.813 1.812 3.648 1.00 29.73 ? 72 ARG A CB 1 ATOM 580 C CG . ARG A 1 72 ? -22.514 0.744 4.474 1.00 32.61 ? 72 ARG A CG 1 ATOM 581 C CD . ARG A 1 72 ? -21.793 -0.589 4.365 1.00 34.40 ? 72 ARG A CD 1 ATOM 582 N NE . ARG A 1 72 ? -20.413 -0.500 4.831 1.00 33.61 ? 72 ARG A NE 1 ATOM 583 C CZ . ARG A 1 72 ? -19.580 -1.531 4.868 1.00 36.77 ? 72 ARG A CZ 1 ATOM 584 N NH1 . ARG A 1 72 ? -20.004 -2.732 4.460 1.00 38.84 ? 72 ARG A NH1 1 ATOM 585 N NH2 . ARG A 1 72 ? -18.324 -1.374 5.293 1.00 34.18 ? 72 ARG A NH2 1 ATOM 586 N N . ASP A 1 73 ? -20.707 3.888 5.598 1.00 25.71 ? 73 ASP A N 1 ATOM 587 C CA . ASP A 1 73 ? -20.232 4.112 6.959 1.00 25.14 ? 73 ASP A CA 1 ATOM 588 C C . ASP A 1 73 ? -20.052 5.563 7.390 1.00 24.02 ? 73 ASP A C 1 ATOM 589 O O . ASP A 1 73 ? -20.054 5.833 8.589 1.00 27.63 ? 73 ASP A O 1 ATOM 590 C CB . ASP A 1 73 ? -18.934 3.347 7.190 1.00 23.83 ? 73 ASP A CB 1 ATOM 591 C CG . ASP A 1 73 ? -19.051 1.895 6.798 1.00 24.71 ? 73 ASP A CG 1 ATOM 592 O OD1 . ASP A 1 73 ? -20.143 1.292 7.009 1.00 23.31 ? 73 ASP A OD1 1 ATOM 593 O OD2 . ASP A 1 73 ? -18.059 1.359 6.266 1.00 22.33 ? 73 ASP A OD2 1 ATOM 594 N N . CYS A 1 74 ? -19.910 6.519 6.482 1.00 24.01 ? 74 CYS A N 1 ATOM 595 C CA . CYS A 1 74 ? -19.617 7.871 6.974 1.00 22.95 ? 74 CYS A CA 1 ATOM 596 C C . CYS A 1 74 ? -20.856 8.641 7.382 1.00 23.50 ? 74 CYS A C 1 ATOM 597 O O . CYS A 1 74 ? -21.475 9.357 6.571 1.00 22.72 ? 74 CYS A O 1 ATOM 598 C CB . CYS A 1 74 ? -18.774 8.688 6.000 1.00 23.06 ? 74 CYS A CB 1 ATOM 599 S SG . CYS A 1 74 ? -18.118 10.148 6.816 1.00 21.83 ? 74 CYS A SG 1 ATOM 600 N N . LYS A 1 75 ? -21.208 8.514 8.655 1.00 23.28 ? 75 LYS A N 1 ATOM 601 C CA . LYS A 1 75 ? -22.432 9.154 9.165 1.00 23.65 ? 75 LYS A CA 1 ATOM 602 C C . LYS A 1 75 ? -22.539 9.030 10.676 1.00 23.23 ? 75 LYS A C 1 ATOM 603 O O . LYS A 1 75 ? -22.010 8.112 11.286 1.00 24.77 ? 75 LYS A O 1 ATOM 604 C CB . LYS A 1 75 ? -23.713 8.604 8.484 1.00 21.87 ? 75 LYS A CB 1 ATOM 605 C CG . LYS A 1 75 ? -24.269 7.304 9.052 1.00 22.75 ? 75 LYS A CG 1 ATOM 606 C CD . LYS A 1 75 ? -23.611 6.030 8.513 1.00 22.88 ? 75 LYS A CD 1 ATOM 607 C CE . LYS A 1 75 ? -24.275 4.778 9.122 1.00 23.51 ? 75 LYS A CE 1 ATOM 608 N NZ . LYS A 1 75 ? -24.086 3.519 8.335 1.00 23.40 ? 75 LYS A NZ 1 ATOM 609 N N . ASP A 1 76 ? -23.244 9.962 11.284 1.00 25.06 ? 76 ASP A N 1 ATOM 610 C CA . ASP A 1 76 ? -23.364 9.944 12.740 1.00 24.65 ? 76 ASP A CA 1 ATOM 611 C C . ASP A 1 76 ? -24.596 9.162 13.182 1.00 26.12 ? 76 ASP A C 1 ATOM 612 O O . ASP A 1 76 ? -25.186 8.455 12.379 1.00 20.78 ? 76 ASP A O 1 ATOM 613 C CB . ASP A 1 76 ? -23.400 11.370 13.242 1.00 23.94 ? 76 ASP A CB 1 ATOM 614 C CG . ASP A 1 76 ? -24.676 12.073 12.915 1.00 23.58 ? 76 ASP A CG 1 ATOM 615 O OD1 . ASP A 1 76 ? -25.612 11.488 12.290 1.00 22.14 ? 76 ASP A OD1 1 ATOM 616 O OD2 . ASP A 1 76 ? -24.708 13.247 13.280 1.00 22.21 ? 76 ASP A OD2 1 ATOM 617 N N . GLU A 1 77 ? -25.014 9.341 14.436 1.00 27.94 ? 77 GLU A N 1 ATOM 618 C CA . GLU A 1 77 ? -26.113 8.553 14.989 1.00 30.31 ? 77 GLU A CA 1 ATOM 619 C C . GLU A 1 77 ? -27.468 9.045 14.499 1.00 28.78 ? 77 GLU A C 1 ATOM 620 O O . GLU A 1 77 ? -28.456 8.314 14.563 1.00 28.02 ? 77 GLU A O 1 ATOM 621 C CB . GLU A 1 77 ? -26.070 8.569 16.522 1.00 34.08 ? 77 GLU A CB 1 ATOM 622 C CG . GLU A 1 77 ? -24.735 8.176 17.120 1.00 36.63 ? 77 GLU A CG 1 ATOM 623 C CD . GLU A 1 77 ? -24.409 6.714 16.998 1.00 39.08 ? 77 GLU A CD 1 ATOM 624 O OE1 . GLU A 1 77 ? -23.995 6.278 15.901 1.00 43.50 ? 77 GLU A OE1 1 ATOM 625 O OE2 . GLU A 1 77 ? -24.542 6.004 18.018 1.00 46.91 ? 77 GLU A OE2 1 ATOM 626 N N . SER A 1 78 ? -27.504 10.286 14.028 1.00 26.85 ? 78 SER A N 1 ATOM 627 C CA . SER A 1 78 ? -28.652 10.813 13.275 1.00 30.56 ? 78 SER A CA 1 ATOM 628 C C . SER A 1 78 ? -28.659 10.371 11.808 1.00 29.51 ? 78 SER A C 1 ATOM 629 O O . SER A 1 78 ? -29.513 10.773 11.044 1.00 26.09 ? 78 SER A O 1 ATOM 630 C CB . SER A 1 78 ? -28.619 12.334 13.296 1.00 33.30 ? 78 SER A CB 1 ATOM 631 O OG . SER A 1 78 ? -28.136 12.800 14.559 1.00 38.89 ? 78 SER A OG 1 ATOM 632 N N . GLY A 1 79 ? -27.681 9.573 11.399 1.00 29.90 ? 79 GLY A N 1 ATOM 633 C CA . GLY A 1 79 ? -27.596 9.178 9.993 1.00 31.39 ? 79 GLY A CA 1 ATOM 634 C C . GLY A 1 79 ? -27.092 10.275 9.070 1.00 30.92 ? 79 GLY A C 1 ATOM 635 O O . GLY A 1 79 ? -27.021 10.060 7.867 1.00 31.99 ? 79 GLY A O 1 ATOM 636 N N . GLU A 1 80 ? -26.712 11.432 9.618 1.00 27.86 ? 80 GLU A N 1 ATOM 637 C CA . GLU A 1 80 ? -26.231 12.551 8.802 1.00 27.87 ? 80 GLU A CA 1 ATOM 638 C C . GLU A 1 80 ? -24.921 12.243 8.094 1.00 26.46 ? 80 GLU A C 1 ATOM 639 O O . GLU A 1 80 ? -23.898 11.912 8.737 1.00 20.64 ? 80 GLU A O 1 ATOM 640 C CB . GLU A 1 80 ? -26.057 13.812 9.655 1.00 29.78 ? 80 GLU A CB 1 ATOM 641 C CG . GLU A 1 80 ? -25.825 15.048 8.786 1.00 34.17 ? 80 GLU A CG 1 ATOM 642 C CD . GLU A 1 80 ? -26.267 16.350 9.426 1.00 35.69 ? 80 GLU A CD 1 ATOM 643 O OE1 . GLU A 1 80 ? -26.700 16.337 10.603 1.00 36.59 ? 80 GLU A OE1 1 ATOM 644 O OE2 . GLU A 1 80 ? -26.196 17.390 8.728 1.00 36.78 ? 80 GLU A OE2 1 ATOM 645 N N . LYS A 1 81 ? -24.949 12.383 6.770 1.00 27.07 ? 81 LYS A N 1 ATOM 646 C CA . LYS A 1 81 ? -23.871 11.915 5.899 1.00 27.74 ? 81 LYS A CA 1 ATOM 647 C C . LYS A 1 81 ? -22.583 12.748 6.001 1.00 26.64 ? 81 LYS A C 1 ATOM 648 O O . LYS A 1 81 ? -22.614 13.976 6.106 1.00 23.85 ? 81 LYS A O 1 ATOM 649 C CB . LYS A 1 81 ? -24.353 11.916 4.458 1.00 31.11 ? 81 LYS A CB 1 ATOM 650 C CG . LYS A 1 81 ? -23.425 11.225 3.479 1.00 34.22 ? 81 LYS A CG 1 ATOM 651 C CD . LYS A 1 81 ? -23.854 11.519 2.045 1.00 37.31 ? 81 LYS A CD 1 ATOM 652 C CE . LYS A 1 81 ? -22.982 10.812 1.028 1.00 37.56 ? 81 LYS A CE 1 ATOM 653 N NZ . LYS A 1 81 ? -23.112 9.339 1.157 1.00 39.82 ? 81 LYS A NZ 1 ATOM 654 N N . GLY A 1 82 ? -21.446 12.074 5.962 1.00 23.91 ? 82 GLY A N 1 ATOM 655 C CA . GLY A 1 82 ? -20.182 12.774 6.129 1.00 25.24 ? 82 GLY A CA 1 ATOM 656 C C . GLY A 1 82 ? -19.816 13.129 7.564 1.00 24.16 ? 82 GLY A C 1 ATOM 657 O O . GLY A 1 82 ? -18.728 13.678 7.814 1.00 24.21 ? 82 GLY A O 1 ATOM 658 N N . ARG A 1 83 ? -20.692 12.833 8.523 1.00 21.85 ? 83 ARG A N 1 ATOM 659 C CA . ARG A 1 83 ? -20.353 13.080 9.916 1.00 22.26 ? 83 ARG A CA 1 ATOM 660 C C . ARG A 1 83 ? -19.503 11.925 10.529 1.00 21.37 ? 83 ARG A C 1 ATOM 661 O O . ARG A 1 83 ? -19.975 11.094 11.323 1.00 20.43 ? 83 ARG A O 1 ATOM 662 C CB . ARG A 1 83 ? -21.626 13.475 10.706 1.00 22.83 ? 83 ARG A CB 1 ATOM 663 C CG . ARG A 1 83 ? -22.249 14.760 10.098 1.00 22.70 ? 83 ARG A CG 1 ATOM 664 C CD . ARG A 1 83 ? -22.973 15.657 11.082 1.00 23.36 ? 83 ARG A CD 1 ATOM 665 N NE . ARG A 1 83 ? -22.103 16.273 12.065 1.00 22.74 ? 83 ARG A NE 1 ATOM 666 C CZ . ARG A 1 83 ? -21.393 17.378 11.885 1.00 23.00 ? 83 ARG A CZ 1 ATOM 667 N NH1 . ARG A 1 83 ? -21.389 17.986 10.715 1.00 25.58 ? 83 ARG A NH1 1 ATOM 668 N NH2 . ARG A 1 83 ? -20.615 17.831 12.861 1.00 22.56 ? 83 ARG A NH2 1 ATOM 669 N N . CYS A 1 84 ? -18.246 11.890 10.108 1.00 18.34 ? 84 CYS A N 1 ATOM 670 C CA . CYS A 1 84 ? -17.277 10.921 10.598 1.00 18.25 ? 84 CYS A CA 1 ATOM 671 C C . CYS A 1 84 ? -15.842 11.417 10.363 1.00 15.58 ? 84 CYS A C 1 ATOM 672 O O . CYS A 1 84 ? -15.620 12.452 9.775 1.00 15.44 ? 84 CYS A O 1 ATOM 673 C CB . CYS A 1 84 ? -17.532 9.562 9.929 1.00 19.96 ? 84 CYS A CB 1 ATOM 674 S SG . CYS A 1 84 ? -16.814 9.363 8.302 1.00 20.89 ? 84 CYS A SG 1 ATOM 675 N N . VAL A 1 85 ? -14.854 10.716 10.872 1.00 15.83 ? 85 VAL A N 1 ATOM 676 C CA . VAL A 1 85 ? -13.483 11.219 10.765 1.00 15.55 ? 85 VAL A CA 1 ATOM 677 C C . VAL A 1 85 ? -13.046 11.471 9.310 1.00 16.57 ? 85 VAL A C 1 ATOM 678 O O . VAL A 1 85 ? -12.381 12.444 9.038 1.00 17.29 ? 85 VAL A O 1 ATOM 679 C CB . VAL A 1 85 ? -12.459 10.356 11.548 1.00 14.65 ? 85 VAL A CB 1 ATOM 680 C CG1 . VAL A 1 85 ? -12.224 9.012 10.865 1.00 14.74 ? 85 VAL A CG1 1 ATOM 681 C CG2 . VAL A 1 85 ? -11.167 11.109 11.685 1.00 14.55 ? 85 VAL A CG2 1 ATOM 682 N N . ALA A 1 86 ? -13.456 10.618 8.379 1.00 18.05 ? 86 ALA A N 1 ATOM 683 C CA . ALA A 1 86 ? -13.234 10.852 6.948 1.00 18.27 ? 86 ALA A CA 1 ATOM 684 C C . ALA A 1 86 ? -13.885 12.136 6.393 1.00 18.12 ? 86 ALA A C 1 ATOM 685 O O . ALA A 1 86 ? -13.204 12.978 5.807 1.00 17.58 ? 86 ALA A O 1 ATOM 686 C CB . ALA A 1 86 ? -13.718 9.647 6.171 1.00 17.99 ? 86 ALA A CB 1 ATOM 687 N N . GLY A 1 87 ? -15.199 12.269 6.570 1.00 19.34 ? 87 GLY A N 1 ATOM 688 C CA . GLY A 1 87 ? -15.927 13.494 6.229 1.00 17.89 ? 87 GLY A CA 1 ATOM 689 C C . GLY A 1 87 ? -15.357 14.747 6.902 1.00 18.70 ? 87 GLY A C 1 ATOM 690 O O . GLY A 1 87 ? -15.363 15.846 6.308 1.00 19.01 ? 87 GLY A O 1 ATOM 691 N N . ALA A 1 88 ? -14.886 14.625 8.144 1.00 17.49 ? 88 ALA A N 1 ATOM 692 C CA . ALA A 1 88 ? -14.277 15.781 8.835 1.00 16.97 ? 88 ALA A CA 1 ATOM 693 C C . ALA A 1 88 ? -12.953 16.246 8.195 1.00 17.33 ? 88 ALA A C 1 ATOM 694 O O . ALA A 1 88 ? -12.663 17.453 8.130 1.00 15.71 ? 88 ALA A O 1 ATOM 695 C CB . ALA A 1 88 ? -14.066 15.513 10.321 1.00 16.66 ? 88 ALA A CB 1 ATOM 696 N N . ILE A 1 89 ? -12.146 15.289 7.753 1.00 16.83 ? 89 ILE A N 1 ATOM 697 C CA . ILE A 1 89 ? -10.880 15.616 7.095 1.00 16.84 ? 89 ILE A CA 1 ATOM 698 C C . ILE A 1 89 ? -11.181 16.353 5.776 1.00 16.96 ? 89 ILE A C 1 ATOM 699 O O . ILE A 1 89 ? -10.494 17.311 5.419 1.00 18.57 ? 89 ILE A O 1 ATOM 700 C CB . ILE A 1 89 ? -10.027 14.320 6.899 1.00 17.32 ? 89 ILE A CB 1 ATOM 701 C CG1 . ILE A 1 89 ? -9.435 13.856 8.253 1.00 17.27 ? 89 ILE A CG1 1 ATOM 702 C CG2 . ILE A 1 89 ? -8.912 14.525 5.872 1.00 16.92 ? 89 ILE A CG2 1 ATOM 703 C CD1 . ILE A 1 89 ? -8.911 12.425 8.285 1.00 16.93 ? 89 ILE A CD1 1 ATOM 704 N N . TYR A 1 90 ? -12.224 15.931 5.056 1.00 18.27 ? 90 TYR A N 1 ATOM 705 C CA . TYR A 1 90 ? -12.609 16.574 3.791 1.00 18.35 ? 90 TYR A CA 1 ATOM 706 C C . TYR A 1 90 ? -13.063 18.008 4.064 1.00 18.80 ? 90 TYR A C 1 ATOM 707 O O . TYR A 1 90 ? -12.666 18.941 3.382 1.00 16.88 ? 90 TYR A O 1 ATOM 708 C CB . TYR A 1 90 ? -13.755 15.826 3.102 1.00 20.38 ? 90 TYR A CB 1 ATOM 709 C CG . TYR A 1 90 ? -13.411 14.583 2.296 1.00 21.39 ? 90 TYR A CG 1 ATOM 710 C CD1 . TYR A 1 90 ? -12.365 14.584 1.365 1.00 23.76 ? 90 TYR A CD1 1 ATOM 711 C CD2 . TYR A 1 90 ? -14.197 13.429 2.393 1.00 22.68 ? 90 TYR A CD2 1 ATOM 712 C CE1 . TYR A 1 90 ? -12.081 13.455 0.595 1.00 22.83 ? 90 TYR A CE1 1 ATOM 713 C CE2 . TYR A 1 90 ? -13.914 12.290 1.634 1.00 22.96 ? 90 TYR A CE2 1 ATOM 714 C CZ . TYR A 1 90 ? -12.853 12.313 0.745 1.00 23.76 ? 90 TYR A CZ 1 ATOM 715 O OH . TYR A 1 90 ? -12.563 11.206 -0.025 1.00 25.64 ? 90 TYR A OH 1 ATOM 716 N N . ASN A 1 91 ? -13.931 18.155 5.064 1.00 18.30 ? 91 ASN A N 1 ATOM 717 C CA . ASN A 1 91 ? -14.403 19.469 5.500 1.00 19.47 ? 91 ASN A CA 1 ATOM 718 C C . ASN A 1 91 ? -13.305 20.447 5.900 1.00 18.13 ? 91 ASN A C 1 ATOM 719 O O . ASN A 1 91 ? -13.202 21.546 5.367 1.00 16.60 ? 91 ASN A O 1 ATOM 720 C CB . ASN A 1 91 ? -15.312 19.280 6.701 1.00 20.07 ? 91 ASN A CB 1 ATOM 721 C CG . ASN A 1 91 ? -15.994 20.536 7.115 1.00 20.80 ? 91 ASN A CG 1 ATOM 722 O OD1 . ASN A 1 91 ? -16.050 21.514 6.387 1.00 21.41 ? 91 ASN A OD1 1 ATOM 723 N ND2 . ASN A 1 91 ? -16.495 20.510 8.325 1.00 22.36 ? 91 ASN A ND2 1 ATOM 724 N N . TYR A 1 92 ? -12.499 20.059 6.867 1.00 18.11 ? 92 TYR A N 1 ATOM 725 C CA . TYR A 1 92 ? -11.489 20.980 7.368 1.00 18.83 ? 92 TYR A CA 1 ATOM 726 C C . TYR A 1 92 ? -10.289 21.255 6.410 1.00 18.18 ? 92 TYR A C 1 ATOM 727 O O . TYR A 1 92 ? -9.708 22.342 6.429 1.00 16.85 ? 92 TYR A O 1 ATOM 728 C CB . TYR A 1 92 ? -11.064 20.556 8.755 1.00 19.15 ? 92 TYR A CB 1 ATOM 729 C CG . TYR A 1 92 ? -12.225 20.637 9.739 1.00 19.99 ? 92 TYR A CG 1 ATOM 730 C CD1 . TYR A 1 92 ? -12.748 21.862 10.117 1.00 19.32 ? 92 TYR A CD1 1 ATOM 731 C CD2 . TYR A 1 92 ? -12.810 19.481 10.263 1.00 20.42 ? 92 TYR A CD2 1 ATOM 732 C CE1 . TYR A 1 92 ? -13.820 21.936 10.975 1.00 19.45 ? 92 TYR A CE1 1 ATOM 733 C CE2 . TYR A 1 92 ? -13.871 19.544 11.141 1.00 19.26 ? 92 TYR A CE2 1 ATOM 734 C CZ . TYR A 1 92 ? -14.369 20.780 11.491 1.00 19.66 ? 92 TYR A CZ 1 ATOM 735 O OH . TYR A 1 92 ? -15.419 20.862 12.368 1.00 19.05 ? 92 TYR A OH 1 ATOM 736 N N . THR A 1 93 ? -9.943 20.309 5.556 1.00 18.47 ? 93 THR A N 1 ATOM 737 C CA . THR A 1 93 ? -8.885 20.578 4.551 1.00 19.81 ? 93 THR A CA 1 ATOM 738 C C . THR A 1 93 ? -9.402 21.576 3.509 1.00 20.48 ? 93 THR A C 1 ATOM 739 O O . THR A 1 93 ? -8.688 22.487 3.105 1.00 22.76 ? 93 THR A O 1 ATOM 740 C CB . THR A 1 93 ? -8.455 19.287 3.817 1.00 19.00 ? 93 THR A CB 1 ATOM 741 O OG1 . THR A 1 93 ? -9.608 18.684 3.249 1.00 18.29 ? 93 THR A OG1 1 ATOM 742 C CG2 . THR A 1 93 ? -7.808 18.303 4.757 1.00 19.16 ? 93 THR A CG2 1 ATOM 743 N N . THR A 1 94 ? -10.651 21.383 3.086 1.00 21.95 ? 94 THR A N 1 ATOM 744 C CA . THR A 1 94 ? -11.357 22.298 2.184 1.00 21.72 ? 94 THR A CA 1 ATOM 745 C C . THR A 1 94 ? -11.374 23.729 2.724 1.00 23.32 ? 94 THR A C 1 ATOM 746 O O . THR A 1 94 ? -11.041 24.669 2.005 1.00 23.64 ? 94 THR A O 1 ATOM 747 C CB . THR A 1 94 ? -12.803 21.811 1.949 1.00 21.04 ? 94 THR A CB 1 ATOM 748 O OG1 . THR A 1 94 ? -12.773 20.562 1.236 1.00 21.02 ? 94 THR A OG1 1 ATOM 749 C CG2 . THR A 1 94 ? -13.634 22.819 1.139 1.00 21.55 ? 94 THR A CG2 1 ATOM 750 N N . GLN A 1 95 ? -11.740 23.895 3.988 1.00 23.24 ? 95 GLN A N 1 ATOM 751 C CA . GLN A 1 95 ? -11.661 25.208 4.629 1.00 25.07 ? 95 GLN A CA 1 ATOM 752 C C . GLN A 1 95 ? -10.242 25.792 4.539 1.00 26.12 ? 95 GLN A C 1 ATOM 753 O O . GLN A 1 95 ? -10.088 26.966 4.203 1.00 24.66 ? 95 GLN A O 1 ATOM 754 C CB . GLN A 1 95 ? -12.081 25.135 6.108 1.00 23.68 ? 95 GLN A CB 1 ATOM 755 C CG . GLN A 1 95 ? -13.560 24.841 6.303 1.00 25.05 ? 95 GLN A CG 1 ATOM 756 C CD . GLN A 1 95 ? -13.938 24.569 7.741 1.00 25.18 ? 95 GLN A CD 1 ATOM 757 O OE1 . GLN A 1 95 ? -13.365 25.132 8.667 1.00 27.50 ? 95 GLN A OE1 1 ATOM 758 N NE2 . GLN A 1 95 ? -14.917 23.689 7.935 1.00 27.81 ? 95 GLN A NE2 1 ATOM 759 N N . LEU A 1 96 ? -9.215 24.989 4.842 1.00 25.27 ? 96 LEU A N 1 ATOM 760 C CA . LEU A 1 96 ? -7.853 25.536 4.862 1.00 27.01 ? 96 LEU A CA 1 ATOM 761 C C . LEU A 1 96 ? -7.399 25.963 3.460 1.00 28.05 ? 96 LEU A C 1 ATOM 762 O O . LEU A 1 96 ? -6.506 26.770 3.351 1.00 27.03 ? 96 LEU A O 1 ATOM 763 C CB . LEU A 1 96 ? -6.837 24.582 5.496 1.00 26.98 ? 96 LEU A CB 1 ATOM 764 C CG . LEU A 1 96 ? -6.946 24.265 6.990 1.00 26.55 ? 96 LEU A CG 1 ATOM 765 C CD1 . LEU A 1 96 ? -6.145 23.025 7.312 1.00 25.85 ? 96 LEU A CD1 1 ATOM 766 C CD2 . LEU A 1 96 ? -6.476 25.412 7.863 1.00 26.64 ? 96 LEU A CD2 1 ATOM 767 N N . LEU A 1 97 ? -8.039 25.446 2.405 1.00 30.16 ? 97 LEU A N 1 ATOM 768 C CA . LEU A 1 97 ? -7.840 25.979 1.041 1.00 30.89 ? 97 LEU A CA 1 ATOM 769 C C . LEU A 1 97 ? -8.158 27.472 0.916 1.00 33.54 ? 97 LEU A C 1 ATOM 770 O O . LEU A 1 97 ? -7.651 28.124 0.019 1.00 33.31 ? 97 LEU A O 1 ATOM 771 C CB . LEU A 1 97 ? -8.665 25.213 0.006 1.00 29.09 ? 97 LEU A CB 1 ATOM 772 C CG . LEU A 1 97 ? -8.239 23.772 -0.232 1.00 29.35 ? 97 LEU A CG 1 ATOM 773 C CD1 . LEU A 1 97 ? -9.231 23.086 -1.157 1.00 30.11 ? 97 LEU A CD1 1 ATOM 774 C CD2 . LEU A 1 97 ? -6.811 23.708 -0.787 1.00 29.71 ? 97 LEU A CD2 1 ATOM 775 N N . SER A 1 98 ? -8.974 28.008 1.816 1.00 35.41 ? 98 SER A N 1 ATOM 776 C CA . SER A 1 98 ? -9.278 29.436 1.829 1.00 39.46 ? 98 SER A CA 1 ATOM 777 C C . SER A 1 98 ? -8.190 30.353 2.410 1.00 39.56 ? 98 SER A C 1 ATOM 778 O O . SER A 1 98 ? -8.265 31.569 2.228 1.00 40.76 ? 98 SER A O 1 ATOM 779 C CB . SER A 1 98 ? -10.570 29.692 2.614 1.00 39.56 ? 98 SER A CB 1 ATOM 780 O OG . SER A 1 98 ? -11.642 28.992 2.035 1.00 43.75 ? 98 SER A OG 1 ATOM 781 N N . TYR A 1 99 ? -7.212 29.805 3.127 1.00 39.14 ? 99 TYR A N 1 ATOM 782 C CA . TYR A 1 99 ? -6.196 30.635 3.796 1.00 40.39 ? 99 TYR A CA 1 ATOM 783 C C . TYR A 1 99 ? -5.507 31.581 2.806 1.00 42.17 ? 99 TYR A C 1 ATOM 784 O O . TYR A 1 99 ? -5.227 31.190 1.692 1.00 40.43 ? 99 TYR A O 1 ATOM 785 C CB . TYR A 1 99 ? -5.170 29.729 4.467 1.00 38.61 ? 99 TYR A CB 1 ATOM 786 C CG . TYR A 1 99 ? -3.972 30.418 5.044 1.00 37.66 ? 99 TYR A CG 1 ATOM 787 C CD1 . TYR A 1 99 ? -4.060 31.134 6.228 1.00 38.00 ? 99 TYR A CD1 1 ATOM 788 C CD2 . TYR A 1 99 ? -2.722 30.319 4.426 1.00 40.16 ? 99 TYR A CD2 1 ATOM 789 C CE1 . TYR A 1 99 ? -2.948 31.762 6.779 1.00 36.04 ? 99 TYR A CE1 1 ATOM 790 C CE2 . TYR A 1 99 ? -1.599 30.929 4.977 1.00 39.09 ? 99 TYR A CE2 1 ATOM 791 C CZ . TYR A 1 99 ? -1.718 31.654 6.154 1.00 38.04 ? 99 TYR A CZ 1 ATOM 792 O OH . TYR A 1 99 ? -0.600 32.275 6.699 1.00 37.91 ? 99 TYR A OH 1 ATOM 793 N N . LYS A 1 100 ? -5.266 32.827 3.207 1.00 47.59 ? 100 LYS A N 1 ATOM 794 C CA . LYS A 1 100 ? -4.592 33.803 2.337 1.00 50.21 ? 100 LYS A CA 1 ATOM 795 C C . LYS A 1 100 ? -3.415 34.437 3.074 1.00 51.05 ? 100 LYS A C 1 ATOM 796 O O . LYS A 1 100 ? -2.274 33.985 2.952 1.00 48.91 ? 100 LYS A O 1 ATOM 797 C CB . LYS A 1 100 ? -5.563 34.897 1.893 1.00 53.01 ? 100 LYS A CB 1 ATOM 798 C CG . LYS A 1 100 ? -6.957 34.423 1.498 1.00 54.21 ? 100 LYS A CG 1 ATOM 799 C CD . LYS A 1 100 ? -6.981 33.654 0.185 1.00 52.21 ? 100 LYS A CD 1 ATOM 800 C CE . LYS A 1 100 ? -8.410 33.491 -0.323 1.00 50.43 ? 100 LYS A CE 1 ATOM 801 N NZ . LYS A 1 100 ? -9.060 34.803 -0.593 1.00 49.40 ? 100 LYS A NZ 1 ATOM 802 N N . SER A 1 107 ? -13.383 33.240 5.614 1.00 56.48 ? 107 SER A N 1 ATOM 803 C CA . SER A 1 107 ? -14.770 33.686 5.538 1.00 56.97 ? 107 SER A CA 1 ATOM 804 C C . SER A 1 107 ? -15.516 33.389 6.847 1.00 54.13 ? 107 SER A C 1 ATOM 805 O O . SER A 1 107 ? -15.225 34.004 7.875 1.00 55.93 ? 107 SER A O 1 ATOM 806 C CB . SER A 1 107 ? -15.480 33.065 4.320 1.00 58.57 ? 107 SER A CB 1 ATOM 807 O OG . SER A 1 107 ? -15.836 31.712 4.551 1.00 59.12 ? 107 SER A OG 1 ATOM 808 N N . GLN A 1 108 ? -16.463 32.454 6.829 1.00 50.29 ? 108 GLN A N 1 ATOM 809 C CA . GLN A 1 108 ? -17.246 32.163 8.040 1.00 52.01 ? 108 GLN A CA 1 ATOM 810 C C . GLN A 1 108 ? -16.439 31.326 9.046 1.00 48.45 ? 108 GLN A C 1 ATOM 811 O O . GLN A 1 108 ? -16.849 31.202 10.208 1.00 48.78 ? 108 GLN A O 1 ATOM 812 C CB . GLN A 1 108 ? -18.570 31.437 7.687 1.00 53.73 ? 108 GLN A CB 1 ATOM 813 C CG . GLN A 1 108 ? -19.791 31.843 8.537 1.00 55.90 ? 108 GLN A CG 1 ATOM 814 C CD . GLN A 1 108 ? -20.286 30.765 9.497 1.00 56.08 ? 108 GLN A CD 1 ATOM 815 O OE1 . GLN A 1 108 ? -20.911 29.780 9.081 1.00 54.35 ? 108 GLN A OE1 1 ATOM 816 N NE2 . GLN A 1 108 ? -20.036 30.962 10.793 1.00 55.61 ? 108 GLN A NE2 1 ATOM 817 N N . TYR A 1 109 ? -15.303 30.765 8.601 1.00 41.67 ? 109 TYR A N 1 ATOM 818 C CA . TYR A 1 109 ? -14.617 29.697 9.340 1.00 38.67 ? 109 TYR A CA 1 ATOM 819 C C . TYR A 1 109 ? -13.333 30.125 10.062 1.00 35.61 ? 109 TYR A C 1 ATOM 820 O O . TYR A 1 109 ? -12.533 30.906 9.551 1.00 36.09 ? 109 TYR A O 1 ATOM 821 C CB . TYR A 1 109 ? -14.320 28.513 8.409 1.00 38.25 ? 109 TYR A CB 1 ATOM 822 C CG . TYR A 1 109 ? -15.550 27.766 7.928 1.00 36.17 ? 109 TYR A CG 1 ATOM 823 C CD1 . TYR A 1 109 ? -16.448 27.192 8.836 1.00 37.51 ? 109 TYR A CD1 1 ATOM 824 C CD2 . TYR A 1 109 ? -15.809 27.613 6.571 1.00 37.07 ? 109 TYR A CD2 1 ATOM 825 C CE1 . TYR A 1 109 ? -17.576 26.494 8.397 1.00 37.69 ? 109 TYR A CE1 1 ATOM 826 C CE2 . TYR A 1 109 ? -16.932 26.911 6.119 1.00 37.32 ? 109 TYR A CE2 1 ATOM 827 C CZ . TYR A 1 109 ? -17.811 26.358 7.034 1.00 37.24 ? 109 TYR A CZ 1 ATOM 828 O OH . TYR A 1 109 ? -18.925 25.687 6.590 1.00 34.12 ? 109 TYR A OH 1 ATOM 829 N N . ASN A 1 110 ? -13.156 29.594 11.262 1.00 32.75 ? 110 ASN A N 1 ATOM 830 C CA . ASN A 1 110 ? -11.956 29.808 12.044 1.00 30.96 ? 110 ASN A CA 1 ATOM 831 C C . ASN A 1 110 ? -10.900 28.829 11.553 1.00 30.79 ? 110 ASN A C 1 ATOM 832 O O . ASN A 1 110 ? -11.025 27.610 11.770 1.00 32.15 ? 110 ASN A O 1 ATOM 833 C CB . ASN A 1 110 ? -12.280 29.590 13.519 1.00 29.80 ? 110 ASN A CB 1 ATOM 834 C CG . ASN A 1 110 ? -11.113 29.867 14.438 1.00 30.79 ? 110 ASN A CG 1 ATOM 835 O OD1 . ASN A 1 110 ? -9.942 29.728 14.066 1.00 28.46 ? 110 ASN A OD1 1 ATOM 836 N ND2 . ASN A 1 110 ? -11.444 30.278 15.678 1.00 31.81 ? 110 ASN A ND2 1 ATOM 837 N N . LEU A 1 111 ? -9.879 29.360 10.878 1.00 27.15 ? 111 LEU A N 1 ATOM 838 C CA . LEU A 1 111 ? -8.878 28.528 10.239 1.00 26.75 ? 111 LEU A CA 1 ATOM 839 C C . LEU A 1 111 ? -7.856 28.018 11.260 1.00 25.15 ? 111 LEU A C 1 ATOM 840 O O . LEU A 1 111 ? -7.163 27.035 10.983 1.00 22.63 ? 111 LEU A O 1 ATOM 841 C CB . LEU A 1 111 ? -8.190 29.255 9.065 1.00 27.47 ? 111 LEU A CB 1 ATOM 842 C CG . LEU A 1 111 ? -9.048 29.653 7.840 1.00 28.36 ? 111 LEU A CG 1 ATOM 843 C CD1 . LEU A 1 111 ? -8.181 29.789 6.605 1.00 28.49 ? 111 LEU A CD1 1 ATOM 844 C CD2 . LEU A 1 111 ? -10.175 28.674 7.529 1.00 29.59 ? 111 LEU A CD2 1 ATOM 845 N N . THR A 1 112 ? -7.765 28.644 12.438 1.00 22.90 ? 112 THR A N 1 ATOM 846 C CA . THR A 1 112 ? -7.002 28.001 13.533 1.00 22.95 ? 112 THR A CA 1 ATOM 847 C C . THR A 1 112 ? -7.667 26.685 13.978 1.00 22.32 ? 112 THR A C 1 ATOM 848 O O . THR A 1 112 ? -6.984 25.701 14.226 1.00 23.44 ? 112 THR A O 1 ATOM 849 C CB . THR A 1 112 ? -6.740 28.925 14.754 1.00 21.85 ? 112 THR A CB 1 ATOM 850 O OG1 . THR A 1 112 ? -5.829 29.946 14.375 1.00 21.09 ? 112 THR A OG1 1 ATOM 851 C CG2 . THR A 1 112 ? -6.091 28.146 15.869 1.00 21.74 ? 112 THR A CG2 1 ATOM 852 N N . GLU A 1 113 ? -8.996 26.653 14.006 1.00 22.73 ? 113 GLU A N 1 ATOM 853 C CA . GLU A 1 113 ? -9.751 25.434 14.387 1.00 20.51 ? 113 GLU A CA 1 ATOM 854 C C . GLU A 1 113 ? -9.623 24.374 13.328 1.00 19.98 ? 113 GLU A C 1 ATOM 855 O O . GLU A 1 113 ? -9.433 23.184 13.658 1.00 19.21 ? 113 GLU A O 1 ATOM 856 C CB . GLU A 1 113 ? -11.223 25.759 14.699 1.00 20.20 ? 113 GLU A CB 1 ATOM 857 C CG . GLU A 1 113 ? -11.379 26.435 16.068 1.00 21.14 ? 113 GLU A CG 1 ATOM 858 C CD . GLU A 1 113 ? -12.818 26.577 16.573 1.00 22.39 ? 113 GLU A CD 1 ATOM 859 O OE1 . GLU A 1 113 ? -13.770 26.375 15.802 1.00 22.14 ? 113 GLU A OE1 1 ATOM 860 O OE2 . GLU A 1 113 ? -12.986 26.913 17.772 1.00 25.09 ? 113 GLU A OE2 1 ATOM 861 N N . ALA A 1 114 ? -9.698 24.789 12.068 1.00 19.03 ? 114 ALA A N 1 ATOM 862 C CA . ALA A 1 114 ? -9.618 23.841 10.967 1.00 20.55 ? 114 ALA A CA 1 ATOM 863 C C . ALA A 1 114 ? -8.258 23.142 10.983 1.00 20.03 ? 114 ALA A C 1 ATOM 864 O O . ALA A 1 114 ? -8.180 21.923 10.792 1.00 20.89 ? 114 ALA A O 1 ATOM 865 C CB . ALA A 1 114 ? -9.874 24.519 9.627 1.00 20.35 ? 114 ALA A CB 1 ATOM 866 N N . LEU A 1 115 ? -7.200 23.911 11.212 1.00 19.47 ? 115 LEU A N 1 ATOM 867 C CA . LEU A 1 115 ? -5.868 23.346 11.385 1.00 19.97 ? 115 LEU A CA 1 ATOM 868 C C . LEU A 1 115 ? -5.820 22.328 12.543 1.00 20.75 ? 115 LEU A C 1 ATOM 869 O O . LEU A 1 115 ? -5.296 21.212 12.383 1.00 19.96 ? 115 LEU A O 1 ATOM 870 C CB . LEU A 1 115 ? -4.847 24.454 11.624 1.00 20.46 ? 115 LEU A CB 1 ATOM 871 C CG . LEU A 1 115 ? -3.430 23.961 11.901 1.00 20.75 ? 115 LEU A CG 1 ATOM 872 C CD1 . LEU A 1 115 ? -2.923 23.126 10.740 1.00 21.02 ? 115 LEU A CD1 1 ATOM 873 C CD2 . LEU A 1 115 ? -2.489 25.113 12.174 1.00 20.56 ? 115 LEU A CD2 1 ATOM 874 N N . LEU A 1 116 ? -6.365 22.713 13.696 1.00 20.28 ? 116 LEU A N 1 ATOM 875 C CA . LEU A 1 116 ? -6.321 21.862 14.879 1.00 21.14 ? 116 LEU A CA 1 ATOM 876 C C . LEU A 1 116 ? -7.181 20.605 14.702 1.00 20.25 ? 116 LEU A C 1 ATOM 877 O O . LEU A 1 116 ? -6.797 19.526 15.178 1.00 21.12 ? 116 LEU A O 1 ATOM 878 C CB . LEU A 1 116 ? -6.703 22.646 16.149 1.00 21.64 ? 116 LEU A CB 1 ATOM 879 C CG . LEU A 1 116 ? -5.821 23.875 16.449 1.00 22.65 ? 116 LEU A CG 1 ATOM 880 C CD1 . LEU A 1 116 ? -6.275 24.525 17.729 1.00 23.23 ? 116 LEU A CD1 1 ATOM 881 C CD2 . LEU A 1 116 ? -4.343 23.525 16.571 1.00 23.36 ? 116 LEU A CD2 1 ATOM 882 N N . PHE A 1 117 ? -8.314 20.732 14.003 1.00 19.00 ? 117 PHE A N 1 ATOM 883 C CA . PHE A 1 117 ? -9.196 19.592 13.742 1.00 17.71 ? 117 PHE A CA 1 ATOM 884 C C . PHE A 1 117 ? -8.517 18.664 12.735 1.00 17.67 ? 117 PHE A C 1 ATOM 885 O O . PHE A 1 117 ? -8.449 17.466 12.941 1.00 17.02 ? 117 PHE A O 1 ATOM 886 C CB . PHE A 1 117 ? -10.579 20.031 13.196 1.00 16.83 ? 117 PHE A CB 1 ATOM 887 C CG . PHE A 1 117 ? -11.569 20.458 14.254 1.00 16.37 ? 117 PHE A CG 1 ATOM 888 C CD1 . PHE A 1 117 ? -11.943 19.588 15.266 1.00 16.57 ? 117 PHE A CD1 1 ATOM 889 C CD2 . PHE A 1 117 ? -12.160 21.719 14.212 1.00 15.91 ? 117 PHE A CD2 1 ATOM 890 C CE1 . PHE A 1 117 ? -12.852 19.975 16.247 1.00 16.20 ? 117 PHE A CE1 1 ATOM 891 C CE2 . PHE A 1 117 ? -13.084 22.101 15.177 1.00 15.85 ? 117 PHE A CE2 1 ATOM 892 C CZ . PHE A 1 117 ? -13.421 21.236 16.192 1.00 16.35 ? 117 PHE A CZ 1 ATOM 893 N N . VAL A 1 118 ? -8.005 19.226 11.640 1.00 18.48 ? 118 VAL A N 1 ATOM 894 C CA . VAL A 1 118 ? -7.423 18.396 10.613 1.00 18.97 ? 118 VAL A CA 1 ATOM 895 C C . VAL A 1 118 ? -6.211 17.655 11.188 1.00 19.49 ? 118 VAL A C 1 ATOM 896 O O . VAL A 1 118 ? -6.016 16.447 10.917 1.00 17.10 ? 118 VAL A O 1 ATOM 897 C CB . VAL A 1 118 ? -7.117 19.170 9.318 1.00 20.96 ? 118 VAL A CB 1 ATOM 898 C CG1 . VAL A 1 118 ? -5.695 19.691 9.276 1.00 21.95 ? 118 VAL A CG1 1 ATOM 899 C CG2 . VAL A 1 118 ? -7.319 18.260 8.135 1.00 23.64 ? 118 VAL A CG2 1 ATOM 900 N N . SER A 1 119 ? -5.432 18.345 12.017 1.00 17.85 ? 119 SER A N 1 ATOM 901 C CA . SER A 1 119 ? -4.233 17.704 12.591 1.00 18.84 ? 119 SER A CA 1 ATOM 902 C C . SER A 1 119 ? -4.645 16.511 13.465 1.00 16.99 ? 119 SER A C 1 ATOM 903 O O . SER A 1 119 ? -4.117 15.411 13.353 1.00 15.98 ? 119 SER A O 1 ATOM 904 C CB . SER A 1 119 ? -3.390 18.726 13.365 1.00 18.57 ? 119 SER A CB 1 ATOM 905 O OG . SER A 1 119 ? -2.832 19.713 12.476 1.00 20.13 ? 119 SER A OG 1 ATOM 906 N N . HIS A 1 120 ? -5.654 16.722 14.285 1.00 17.45 ? 120 HIS A N 1 ATOM 907 C CA . HIS A 1 120 ? -6.136 15.681 15.183 1.00 17.32 ? 120 HIS A CA 1 ATOM 908 C C . HIS A 1 120 ? -6.784 14.522 14.446 1.00 17.10 ? 120 HIS A C 1 ATOM 909 O O . HIS A 1 120 ? -6.511 13.373 14.745 1.00 16.73 ? 120 HIS A O 1 ATOM 910 C CB . HIS A 1 120 ? -7.137 16.276 16.121 1.00 17.55 ? 120 HIS A CB 1 ATOM 911 C CG . HIS A 1 120 ? -7.594 15.323 17.161 1.00 16.84 ? 120 HIS A CG 1 ATOM 912 N ND1 . HIS A 1 120 ? -6.870 15.074 18.302 1.00 17.43 ? 120 HIS A ND1 1 ATOM 913 C CD2 . HIS A 1 120 ? -8.685 14.535 17.222 1.00 16.14 ? 120 HIS A CD2 1 ATOM 914 C CE1 . HIS A 1 120 ? -7.508 14.178 19.028 1.00 16.59 ? 120 HIS A CE1 1 ATOM 915 N NE2 . HIS A 1 120 ? -8.595 13.817 18.380 1.00 15.97 ? 120 HIS A NE2 1 ATOM 916 N N . PHE A 1 121 ? -7.638 14.839 13.473 1.00 17.26 ? 121 PHE A N 1 ATOM 917 C CA . PHE A 1 121 ? -8.373 13.825 12.770 1.00 16.70 ? 121 PHE A CA 1 ATOM 918 C C . PHE A 1 121 ? -7.482 12.969 11.850 1.00 16.52 ? 121 PHE A C 1 ATOM 919 O O . PHE A 1 121 ? -7.719 11.756 11.721 1.00 17.60 ? 121 PHE A O 1 ATOM 920 C CB . PHE A 1 121 ? -9.552 14.444 12.032 1.00 16.93 ? 121 PHE A CB 1 ATOM 921 C CG . PHE A 1 121 ? -10.577 15.083 12.952 1.00 17.56 ? 121 PHE A CG 1 ATOM 922 C CD1 . PHE A 1 121 ? -10.826 14.564 14.227 1.00 17.30 ? 121 PHE A CD1 1 ATOM 923 C CD2 . PHE A 1 121 ? -11.299 16.198 12.536 1.00 16.80 ? 121 PHE A CD2 1 ATOM 924 C CE1 . PHE A 1 121 ? -11.752 15.160 15.062 1.00 18.14 ? 121 PHE A CE1 1 ATOM 925 C CE2 . PHE A 1 121 ? -12.242 16.779 13.364 1.00 17.76 ? 121 PHE A CE2 1 ATOM 926 C CZ . PHE A 1 121 ? -12.467 16.265 14.631 1.00 18.10 ? 121 PHE A CZ 1 ATOM 927 N N . MET A 1 122 ? -6.471 13.585 11.230 1.00 16.22 ? 122 MET A N 1 ATOM 928 C CA . MET A 1 122 ? -5.502 12.825 10.466 1.00 17.43 ? 122 MET A CA 1 ATOM 929 C C . MET A 1 122 ? -4.864 11.774 11.374 1.00 14.97 ? 122 MET A C 1 ATOM 930 O O . MET A 1 122 ? -4.693 10.672 10.949 1.00 15.06 ? 122 MET A O 1 ATOM 931 C CB . MET A 1 122 ? -4.425 13.708 9.817 1.00 19.55 ? 122 MET A CB 1 ATOM 932 C CG . MET A 1 122 ? -3.553 12.920 8.818 1.00 22.08 ? 122 MET A CG 1 ATOM 933 S SD . MET A 1 122 ? -4.485 12.448 7.321 1.00 26.21 ? 122 MET A SD 1 ATOM 934 C CE . MET A 1 122 ? -5.157 13.988 6.735 1.00 24.03 ? 122 MET A CE 1 ATOM 935 N N . GLY A 1 123 ? -4.551 12.116 12.616 1.00 13.63 ? 123 GLY A N 1 ATOM 936 C CA . GLY A 1 123 ? -4.062 11.159 13.583 1.00 14.50 ? 123 GLY A CA 1 ATOM 937 C C . GLY A 1 123 ? -5.075 10.071 13.917 1.00 14.94 ? 123 GLY A C 1 ATOM 938 O O . GLY A 1 123 ? -4.735 8.887 13.895 1.00 15.46 ? 123 GLY A O 1 ATOM 939 N N . ASP A 1 124 ? -6.305 10.480 14.219 1.00 15.22 ? 124 ASP A N 1 ATOM 940 C CA . ASP A 1 124 ? -7.366 9.535 14.618 1.00 15.49 ? 124 ASP A CA 1 ATOM 941 C C . ASP A 1 124 ? -7.738 8.586 13.531 1.00 15.93 ? 124 ASP A C 1 ATOM 942 O O . ASP A 1 124 ? -7.946 7.447 13.848 1.00 15.84 ? 124 ASP A O 1 ATOM 943 C CB . ASP A 1 124 ? -8.636 10.229 15.097 1.00 15.09 ? 124 ASP A CB 1 ATOM 944 C CG . ASP A 1 124 ? -8.629 10.509 16.575 1.00 14.35 ? 124 ASP A CG 1 ATOM 945 O OD1 . ASP A 1 124 ? -7.637 10.240 17.234 1.00 14.25 ? 124 ASP A OD1 1 ATOM 946 O OD2 . ASP A 1 124 ? -9.614 11.044 17.081 1.00 15.10 ? 124 ASP A OD2 1 ATOM 947 N N . ILE A 1 125 ? -7.814 9.034 12.260 1.00 17.01 ? 125 ILE A N 1 ATOM 948 C CA . ILE A 1 125 ? -8.155 8.119 11.149 1.00 17.15 ? 125 ILE A CA 1 ATOM 949 C C . ILE A 1 125 ? -7.129 6.997 10.965 1.00 16.43 ? 125 ILE A C 1 ATOM 950 O O . ILE A 1 125 ? -7.384 5.989 10.279 1.00 16.60 ? 125 ILE A O 1 ATOM 951 C CB . ILE A 1 125 ? -8.410 8.866 9.807 1.00 17.49 ? 125 ILE A CB 1 ATOM 952 C CG1 . ILE A 1 125 ? -9.323 8.034 8.906 1.00 18.78 ? 125 ILE A CG1 1 ATOM 953 C CG2 . ILE A 1 125 ? -7.097 9.200 9.087 1.00 16.76 ? 125 ILE A CG2 1 ATOM 954 C CD1 . ILE A 1 125 ? -9.981 8.781 7.742 1.00 19.42 ? 125 ILE A CD1 1 ATOM 955 N N . HIS A 1 126 ? -5.976 7.155 11.585 1.00 15.77 ? 126 HIS A N 1 ATOM 956 C CA . HIS A 1 126 ? -4.920 6.145 11.522 1.00 15.65 ? 126 HIS A CA 1 ATOM 957 C C . HIS A 1 126 ? -4.890 5.193 12.718 1.00 16.35 ? 126 HIS A C 1 ATOM 958 O O . HIS A 1 126 ? -4.182 4.187 12.690 1.00 15.59 ? 126 HIS A O 1 ATOM 959 C CB . HIS A 1 126 ? -3.577 6.822 11.333 1.00 16.45 ? 126 HIS A CB 1 ATOM 960 C CG . HIS A 1 126 ? -3.350 7.287 9.938 1.00 16.58 ? 126 HIS A CG 1 ATOM 961 N ND1 . HIS A 1 126 ? -3.663 8.559 9.520 1.00 17.13 ? 126 HIS A ND1 1 ATOM 962 C CD2 . HIS A 1 126 ? -2.893 6.631 8.846 1.00 17.52 ? 126 HIS A CD2 1 ATOM 963 C CE1 . HIS A 1 126 ? -3.364 8.685 8.240 1.00 17.57 ? 126 HIS A CE1 1 ATOM 964 N NE2 . HIS A 1 126 ? -2.913 7.525 7.805 1.00 17.50 ? 126 HIS A NE2 1 ATOM 965 N N . GLN A 1 127 ? -5.664 5.505 13.754 1.00 16.37 ? 127 GLN A N 1 ATOM 966 C CA . GLN A 1 127 ? -5.911 4.552 14.842 1.00 17.49 ? 127 GLN A CA 1 ATOM 967 C C . GLN A 1 127 ? -6.845 3.443 14.317 1.00 16.90 ? 127 GLN A C 1 ATOM 968 O O . GLN A 1 127 ? -7.979 3.719 13.926 1.00 15.71 ? 127 GLN A O 1 ATOM 969 C CB . GLN A 1 127 ? -6.528 5.252 16.073 1.00 18.11 ? 127 GLN A CB 1 ATOM 970 C CG . GLN A 1 127 ? -6.009 4.743 17.438 1.00 18.48 ? 127 GLN A CG 1 ATOM 971 C CD . GLN A 1 127 ? -6.613 3.419 17.871 1.00 17.86 ? 127 GLN A CD 1 ATOM 972 O OE1 . GLN A 1 127 ? -6.536 2.414 17.171 1.00 17.09 ? 127 GLN A OE1 1 ATOM 973 N NE2 . GLN A 1 127 ? -7.184 3.409 19.060 1.00 18.38 ? 127 GLN A NE2 1 ATOM 974 N N . PRO A 1 128 ? -6.350 2.186 14.256 1.00 17.56 ? 128 PRO A N 1 ATOM 975 C CA . PRO A 1 128 ? -7.184 1.141 13.686 1.00 17.09 ? 128 PRO A CA 1 ATOM 976 C C . PRO A 1 128 ? -8.575 1.053 14.341 1.00 18.42 ? 128 PRO A C 1 ATOM 977 O O . PRO A 1 128 ? -9.584 0.964 13.638 1.00 16.90 ? 128 PRO A O 1 ATOM 978 C CB . PRO A 1 128 ? -6.354 -0.120 13.912 1.00 18.24 ? 128 PRO A CB 1 ATOM 979 C CG . PRO A 1 128 ? -4.932 0.374 13.829 1.00 17.81 ? 128 PRO A CG 1 ATOM 980 C CD . PRO A 1 128 ? -4.962 1.738 14.471 1.00 16.87 ? 128 PRO A CD 1 ATOM 981 N N . LEU A 1 129 ? -8.628 1.148 15.668 1.00 19.04 ? 129 LEU A N 1 ATOM 982 C CA . LEU A 1 129 ? -9.887 1.083 16.378 1.00 20.60 ? 129 LEU A CA 1 ATOM 983 C C . LEU A 1 129 ? -10.723 2.362 16.359 1.00 20.44 ? 129 LEU A C 1 ATOM 984 O O . LEU A 1 129 ? -11.806 2.377 16.922 1.00 19.58 ? 129 LEU A O 1 ATOM 985 C CB . LEU A 1 129 ? -9.675 0.577 17.810 1.00 22.02 ? 129 LEU A CB 1 ATOM 986 C CG . LEU A 1 129 ? -9.189 -0.870 17.840 1.00 22.69 ? 129 LEU A CG 1 ATOM 987 C CD1 . LEU A 1 129 ? -8.946 -1.344 19.270 1.00 24.24 ? 129 LEU A CD1 1 ATOM 988 C CD2 . LEU A 1 129 ? -10.196 -1.789 17.137 1.00 23.63 ? 129 LEU A CD2 1 ATOM 989 N N . HIS A 1 130 ? -10.265 3.412 15.679 1.00 19.62 ? 130 HIS A N 1 ATOM 990 C CA . HIS A 1 130 ? -11.137 4.581 15.398 1.00 19.36 ? 130 HIS A CA 1 ATOM 991 C C . HIS A 1 130 ? -11.885 4.392 14.081 1.00 19.75 ? 130 HIS A C 1 ATOM 992 O O . HIS A 1 130 ? -12.628 5.302 13.645 1.00 18.97 ? 130 HIS A O 1 ATOM 993 C CB . HIS A 1 130 ? -10.347 5.885 15.335 1.00 18.59 ? 130 HIS A CB 1 ATOM 994 C CG . HIS A 1 130 ? -10.172 6.519 16.664 1.00 19.02 ? 130 HIS A CG 1 ATOM 995 N ND1 . HIS A 1 130 ? -10.790 7.689 17.005 1.00 18.28 ? 130 HIS A ND1 1 ATOM 996 C CD2 . HIS A 1 130 ? -9.507 6.108 17.772 1.00 19.84 ? 130 HIS A CD2 1 ATOM 997 C CE1 . HIS A 1 130 ? -10.519 7.979 18.266 1.00 18.53 ? 130 HIS A CE1 1 ATOM 998 N NE2 . HIS A 1 130 ? -9.725 7.049 18.748 1.00 18.03 ? 130 HIS A NE2 1 ATOM 999 N N . VAL A 1 131 ? -11.633 3.250 13.457 1.00 18.98 ? 131 VAL A N 1 ATOM 1000 C CA . VAL A 1 131 ? -12.314 2.804 12.252 1.00 22.16 ? 131 VAL A CA 1 ATOM 1001 C C . VAL A 1 131 ? -12.619 1.307 12.389 1.00 22.87 ? 131 VAL A C 1 ATOM 1002 O O . VAL A 1 131 ? -11.962 0.461 11.794 1.00 24.33 ? 131 VAL A O 1 ATOM 1003 C CB . VAL A 1 131 ? -11.443 3.042 10.998 1.00 21.97 ? 131 VAL A CB 1 ATOM 1004 C CG1 . VAL A 1 131 ? -12.245 2.695 9.749 1.00 22.74 ? 131 VAL A CG1 1 ATOM 1005 C CG2 . VAL A 1 131 ? -10.958 4.482 10.943 1.00 20.65 ? 131 VAL A CG2 1 ATOM 1006 N N . SER A 1 132 ? -13.597 0.978 13.214 1.00 24.85 ? 132 SER A N 1 ATOM 1007 C CA . SER A 1 132 ? -13.846 -0.419 13.533 1.00 27.25 ? 132 SER A CA 1 ATOM 1008 C C . SER A 1 132 ? -15.319 -0.633 13.942 1.00 27.41 ? 132 SER A C 1 ATOM 1009 O O . SER A 1 132 ? -16.177 0.215 13.689 1.00 24.92 ? 132 SER A O 1 ATOM 1010 C CB . SER A 1 132 ? -12.860 -0.863 14.618 1.00 27.04 ? 132 SER A CB 1 ATOM 1011 O OG . SER A 1 132 ? -12.963 0.013 15.732 1.00 30.14 ? 132 SER A OG 1 ATOM 1012 N N . TYR A 1 133 ? -15.600 -1.775 14.555 1.00 27.36 ? 133 TYR A N 1 ATOM 1013 C CA . TYR A 1 133 ? -16.975 -2.232 14.733 1.00 28.43 ? 133 TYR A CA 1 ATOM 1014 C C . TYR A 1 133 ? -17.783 -1.303 15.653 1.00 28.14 ? 133 TYR A C 1 ATOM 1015 O O . TYR A 1 133 ? -17.382 -1.022 16.780 1.00 24.73 ? 133 TYR A O 1 ATOM 1016 C CB . TYR A 1 133 ? -16.972 -3.655 15.319 1.00 29.61 ? 133 TYR A CB 1 ATOM 1017 C CG . TYR A 1 133 ? -16.305 -4.752 14.462 1.00 31.41 ? 133 TYR A CG 1 ATOM 1018 C CD1 . TYR A 1 133 ? -15.721 -4.473 13.218 1.00 32.68 ? 133 TYR A CD1 1 ATOM 1019 C CD2 . TYR A 1 133 ? -16.240 -6.069 14.921 1.00 32.19 ? 133 TYR A CD2 1 ATOM 1020 C CE1 . TYR A 1 133 ? -15.113 -5.472 12.453 1.00 32.85 ? 133 TYR A CE1 1 ATOM 1021 C CE2 . TYR A 1 133 ? -15.648 -7.074 14.158 1.00 34.74 ? 133 TYR A CE2 1 ATOM 1022 C CZ . TYR A 1 133 ? -15.075 -6.767 12.926 1.00 35.08 ? 133 TYR A CZ 1 ATOM 1023 O OH . TYR A 1 133 ? -14.456 -7.757 12.172 1.00 38.60 ? 133 TYR A OH 1 ATOM 1024 N N . ALA A 1 134 ? -18.935 -0.850 15.162 1.00 27.16 ? 134 ALA A N 1 ATOM 1025 C CA . ALA A 1 134 ? -19.939 -0.250 16.023 1.00 26.31 ? 134 ALA A CA 1 ATOM 1026 C C . ALA A 1 134 ? -20.470 -1.190 17.095 1.00 26.09 ? 134 ALA A C 1 ATOM 1027 O O . ALA A 1 134 ? -20.920 -0.710 18.133 1.00 24.84 ? 134 ALA A O 1 ATOM 1028 C CB . ALA A 1 134 ? -21.092 0.312 15.206 1.00 29.22 ? 134 ALA A CB 1 ATOM 1029 N N . SER A 1 135 ? -20.409 -2.507 16.879 1.00 25.78 ? 135 SER A N 1 ATOM 1030 C CA . SER A 1 135 ? -21.014 -3.459 17.835 1.00 27.33 ? 135 SER A CA 1 ATOM 1031 C C . SER A 1 135 ? -20.285 -3.492 19.168 1.00 28.88 ? 135 SER A C 1 ATOM 1032 O O . SER A 1 135 ? -20.888 -3.785 20.204 1.00 28.47 ? 135 SER A O 1 ATOM 1033 C CB . SER A 1 135 ? -21.021 -4.881 17.278 1.00 27.35 ? 135 SER A CB 1 ATOM 1034 O OG . SER A 1 135 ? -19.694 -5.302 16.982 1.00 27.23 ? 135 SER A OG 1 ATOM 1035 N N . ASP A 1 136 ? -18.982 -3.229 19.134 1.00 28.22 ? 136 ASP A N 1 ATOM 1036 C CA . ASP A 1 136 ? -18.176 -3.169 20.350 1.00 28.29 ? 136 ASP A CA 1 ATOM 1037 C C . ASP A 1 136 ? -17.603 -1.764 20.504 1.00 27.78 ? 136 ASP A C 1 ATOM 1038 O O . ASP A 1 136 ? -16.593 -1.571 21.162 1.00 30.01 ? 136 ASP A O 1 ATOM 1039 C CB . ASP A 1 136 ? -17.053 -4.215 20.303 1.00 28.48 ? 136 ASP A CB 1 ATOM 1040 C CG . ASP A 1 136 ? -16.216 -4.126 19.035 1.00 30.07 ? 136 ASP A CG 1 ATOM 1041 O OD1 . ASP A 1 136 ? -15.848 -2.985 18.662 1.00 28.91 ? 136 ASP A OD1 1 ATOM 1042 O OD2 . ASP A 1 136 ? -15.950 -5.196 18.399 1.00 29.90 ? 136 ASP A OD2 1 ATOM 1043 N N . LYS A 1 137 ? -18.245 -0.801 19.862 1.00 27.41 ? 137 LYS A N 1 ATOM 1044 C CA . LYS A 1 137 ? -17.844 0.600 19.913 1.00 28.24 ? 137 LYS A CA 1 ATOM 1045 C C . LYS A 1 137 ? -16.350 0.808 19.707 1.00 26.00 ? 137 LYS A C 1 ATOM 1046 O O . LYS A 1 137 ? -15.697 1.473 20.505 1.00 27.93 ? 137 LYS A O 1 ATOM 1047 C CB . LYS A 1 137 ? -18.278 1.232 21.234 1.00 31.00 ? 137 LYS A CB 1 ATOM 1048 C CG . LYS A 1 137 ? -19.771 1.511 21.337 1.00 35.47 ? 137 LYS A CG 1 ATOM 1049 C CD . LYS A 1 137 ? -20.063 2.523 22.455 1.00 36.43 ? 137 LYS A CD 1 ATOM 1050 C CE . LYS A 1 137 ? -21.336 3.313 22.182 1.00 38.41 ? 137 LYS A CE 1 ATOM 1051 N NZ . LYS A 1 137 ? -22.549 2.629 22.691 1.00 34.70 ? 137 LYS A NZ 1 ATOM 1052 N N . GLY A 1 138 ? -15.801 0.218 18.664 1.00 23.40 ? 138 GLY A N 1 ATOM 1053 C CA . GLY A 1 138 ? -14.390 0.412 18.348 1.00 25.74 ? 138 GLY A CA 1 ATOM 1054 C C . GLY A 1 138 ? -13.483 -0.219 19.378 1.00 24.95 ? 138 GLY A C 1 ATOM 1055 O O . GLY A 1 138 ? -12.342 0.208 19.570 1.00 24.51 ? 138 GLY A O 1 ATOM 1056 N N . GLY A 1 139 ? -14.005 -1.237 20.051 1.00 23.19 ? 139 GLY A N 1 ATOM 1057 C CA . GLY A 1 139 ? -13.246 -1.982 21.036 1.00 22.78 ? 139 GLY A CA 1 ATOM 1058 C C . GLY A 1 139 ? -13.328 -1.497 22.469 1.00 22.03 ? 139 GLY A C 1 ATOM 1059 O O . GLY A 1 139 ? -12.775 -2.142 23.345 1.00 20.57 ? 139 GLY A O 1 ATOM 1060 N N . ASN A 1 140 ? -14.012 -0.383 22.706 1.00 23.41 ? 140 ASN A N 1 ATOM 1061 C CA . ASN A 1 140 ? -14.217 0.121 24.065 1.00 26.31 ? 140 ASN A CA 1 ATOM 1062 C C . ASN A 1 140 ? -14.960 -0.821 25.007 1.00 27.17 ? 140 ASN A C 1 ATOM 1063 O O . ASN A 1 140 ? -14.831 -0.689 26.228 1.00 29.64 ? 140 ASN A O 1 ATOM 1064 C CB . ASN A 1 140 ? -15.013 1.417 24.051 1.00 25.90 ? 140 ASN A CB 1 ATOM 1065 C CG . ASN A 1 140 ? -14.159 2.612 23.727 1.00 27.22 ? 140 ASN A CG 1 ATOM 1066 O OD1 . ASN A 1 140 ? -13.505 3.167 24.610 1.00 27.77 ? 140 ASN A OD1 1 ATOM 1067 N ND2 . ASN A 1 140 ? -14.170 3.031 22.468 1.00 25.91 ? 140 ASN A ND2 1 ATOM 1068 N N . THR A 1 141 ? -15.784 -1.698 24.453 1.00 24.95 ? 141 THR A N 1 ATOM 1069 C CA . THR A 1 141 ? -16.544 -2.633 25.273 1.00 27.05 ? 141 THR A CA 1 ATOM 1070 C C . THR A 1 141 ? -15.847 -3.962 25.469 1.00 27.29 ? 141 THR A C 1 ATOM 1071 O O . THR A 1 141 ? -16.408 -4.843 26.109 1.00 30.69 ? 141 THR A O 1 ATOM 1072 C CB . THR A 1 141 ? -17.926 -2.963 24.661 1.00 25.13 ? 141 THR A CB 1 ATOM 1073 O OG1 . THR A 1 141 ? -17.765 -3.760 23.492 1.00 23.24 ? 141 THR A OG1 1 ATOM 1074 C CG2 . THR A 1 141 ? -18.680 -1.743 24.333 1.00 24.44 ? 141 THR A CG2 1 ATOM 1075 N N . ILE A 1 142 ? -14.660 -4.133 24.888 1.00 26.03 ? 142 ILE A N 1 ATOM 1076 C CA . ILE A 1 142 ? -13.909 -5.352 25.075 1.00 27.89 ? 142 ILE A CA 1 ATOM 1077 C C . ILE A 1 142 ? -12.963 -5.143 26.249 1.00 27.36 ? 142 ILE A C 1 ATOM 1078 O O . ILE A 1 142 ? -11.902 -4.554 26.086 1.00 25.08 ? 142 ILE A O 1 ATOM 1079 C CB . ILE A 1 142 ? -13.112 -5.760 23.813 1.00 28.57 ? 142 ILE A CB 1 ATOM 1080 C CG1 . ILE A 1 142 ? -14.071 -6.148 22.688 1.00 29.49 ? 142 ILE A CG1 1 ATOM 1081 C CG2 . ILE A 1 142 ? -12.181 -6.924 24.108 1.00 29.37 ? 142 ILE A CG2 1 ATOM 1082 C CD1 . ILE A 1 142 ? -13.409 -6.312 21.340 1.00 27.39 ? 142 ILE A CD1 1 ATOM 1083 N N . GLU A 1 143 ? -13.355 -5.628 27.421 1.00 27.57 ? 143 GLU A N 1 ATOM 1084 C CA . GLU A 1 143 ? -12.502 -5.542 28.588 1.00 31.66 ? 143 GLU A CA 1 ATOM 1085 C C . GLU A 1 143 ? -11.490 -6.688 28.601 1.00 29.00 ? 143 GLU A C 1 ATOM 1086 O O . GLU A 1 143 ? -11.859 -7.855 28.541 1.00 27.54 ? 143 GLU A O 1 ATOM 1087 C CB . GLU A 1 143 ? -13.327 -5.544 29.863 1.00 36.60 ? 143 GLU A CB 1 ATOM 1088 C CG . GLU A 1 143 ? -14.393 -4.445 29.901 1.00 44.62 ? 143 GLU A CG 1 ATOM 1089 C CD . GLU A 1 143 ? -13.823 -3.037 29.861 1.00 49.70 ? 143 GLU A CD 1 ATOM 1090 O OE1 . GLU A 1 143 ? -12.886 -2.754 30.650 1.00 54.03 ? 143 GLU A OE1 1 ATOM 1091 O OE2 . GLU A 1 143 ? -14.318 -2.213 29.043 1.00 55.33 ? 143 GLU A OE2 1 ATOM 1092 N N . VAL A 1 144 ? -10.215 -6.324 28.629 1.00 25.99 ? 144 VAL A N 1 ATOM 1093 C CA . VAL A 1 144 ? -9.106 -7.256 28.795 1.00 25.38 ? 144 VAL A CA 1 ATOM 1094 C C . VAL A 1 144 ? -8.194 -6.725 29.916 1.00 25.31 ? 144 VAL A C 1 ATOM 1095 O O . VAL A 1 144 ? -8.518 -5.743 30.563 1.00 26.90 ? 144 VAL A O 1 ATOM 1096 C CB . VAL A 1 144 ? -8.301 -7.401 27.487 1.00 26.02 ? 144 VAL A CB 1 ATOM 1097 C CG1 . VAL A 1 144 ? -9.084 -8.198 26.462 1.00 26.75 ? 144 VAL A CG1 1 ATOM 1098 C CG2 . VAL A 1 144 ? -7.902 -6.056 26.896 1.00 24.84 ? 144 VAL A CG2 1 ATOM 1099 N N . HIS A 1 145 ? -7.061 -7.368 30.160 1.00 24.06 ? 145 HIS A N 1 ATOM 1100 C CA . HIS A 1 145 ? -6.039 -6.757 31.008 1.00 24.36 ? 145 HIS A CA 1 ATOM 1101 C C . HIS A 1 145 ? -4.858 -6.409 30.142 1.00 21.13 ? 145 HIS A C 1 ATOM 1102 O O . HIS A 1 145 ? -4.504 -7.181 29.224 1.00 19.24 ? 145 HIS A O 1 ATOM 1103 C CB . HIS A 1 145 ? -5.613 -7.712 32.123 1.00 26.15 ? 145 HIS A CB 1 ATOM 1104 C CG . HIS A 1 145 ? -6.682 -7.955 33.132 1.00 27.99 ? 145 HIS A CG 1 ATOM 1105 N ND1 . HIS A 1 145 ? -7.740 -8.800 32.898 1.00 30.50 ? 145 HIS A ND1 1 ATOM 1106 C CD2 . HIS A 1 145 ? -6.863 -7.457 34.374 1.00 32.87 ? 145 HIS A CD2 1 ATOM 1107 C CE1 . HIS A 1 145 ? -8.524 -8.824 33.957 1.00 32.96 ? 145 HIS A CE1 1 ATOM 1108 N NE2 . HIS A 1 145 ? -8.015 -8.016 34.868 1.00 34.90 ? 145 HIS A NE2 1 ATOM 1109 N N . TRP A 1 146 ? -4.287 -5.235 30.384 1.00 18.99 ? 146 TRP A N 1 ATOM 1110 C CA . TRP A 1 146 ? -2.968 -4.897 29.851 1.00 18.97 ? 146 TRP A CA 1 ATOM 1111 C C . TRP A 1 146 ? -1.912 -5.240 30.927 1.00 19.03 ? 146 TRP A C 1 ATOM 1112 O O . TRP A 1 146 ? -1.758 -4.524 31.928 1.00 18.15 ? 146 TRP A O 1 ATOM 1113 C CB . TRP A 1 146 ? -2.902 -3.423 29.441 1.00 19.02 ? 146 TRP A CB 1 ATOM 1114 C CG . TRP A 1 146 ? -1.622 -3.101 28.756 1.00 19.47 ? 146 TRP A CG 1 ATOM 1115 C CD1 . TRP A 1 146 ? -0.603 -2.333 29.228 1.00 20.00 ? 146 TRP A CD1 1 ATOM 1116 C CD2 . TRP A 1 146 ? -1.203 -3.578 27.472 1.00 19.36 ? 146 TRP A CD2 1 ATOM 1117 N NE1 . TRP A 1 146 ? 0.433 -2.294 28.309 1.00 19.36 ? 146 TRP A NE1 1 ATOM 1118 C CE2 . TRP A 1 146 ? 0.072 -3.032 27.214 1.00 19.52 ? 146 TRP A CE2 1 ATOM 1119 C CE3 . TRP A 1 146 ? -1.788 -4.398 26.513 1.00 19.13 ? 146 TRP A CE3 1 ATOM 1120 C CZ2 . TRP A 1 146 ? 0.775 -3.303 26.046 1.00 18.80 ? 146 TRP A CZ2 1 ATOM 1121 C CZ3 . TRP A 1 146 ? -1.101 -4.649 25.350 1.00 18.78 ? 146 TRP A CZ3 1 ATOM 1122 C CH2 . TRP A 1 146 ? 0.175 -4.103 25.128 1.00 18.48 ? 146 TRP A CH2 1 ATOM 1123 N N . TYR A 1 147 ? -1.207 -6.349 30.724 1.00 20.26 ? 147 TYR A N 1 ATOM 1124 C CA . TYR A 1 147 ? -0.433 -6.975 31.778 1.00 22.24 ? 147 TYR A CA 1 ATOM 1125 C C . TYR A 1 147 ? -1.330 -7.027 33.010 1.00 23.96 ? 147 TYR A C 1 ATOM 1126 O O . TYR A 1 147 ? -2.407 -7.633 32.943 1.00 24.13 ? 147 TYR A O 1 ATOM 1127 C CB . TYR A 1 147 ? 0.868 -6.201 32.028 1.00 22.99 ? 147 TYR A CB 1 ATOM 1128 C CG . TYR A 1 147 ? 1.815 -6.246 30.846 1.00 23.52 ? 147 TYR A CG 1 ATOM 1129 C CD1 . TYR A 1 147 ? 1.674 -5.362 29.770 1.00 23.59 ? 147 TYR A CD1 1 ATOM 1130 C CD2 . TYR A 1 147 ? 2.825 -7.191 30.793 1.00 23.55 ? 147 TYR A CD2 1 ATOM 1131 C CE1 . TYR A 1 147 ? 2.533 -5.417 28.679 1.00 23.67 ? 147 TYR A CE1 1 ATOM 1132 C CE2 . TYR A 1 147 ? 3.688 -7.262 29.721 1.00 25.29 ? 147 TYR A CE2 1 ATOM 1133 C CZ . TYR A 1 147 ? 3.546 -6.375 28.664 1.00 25.75 ? 147 TYR A CZ 1 ATOM 1134 O OH . TYR A 1 147 ? 4.431 -6.472 27.617 1.00 23.92 ? 147 TYR A OH 1 ATOM 1135 N N . THR A 1 148 ? -0.953 -6.321 34.082 1.00 23.27 ? 148 THR A N 1 ATOM 1136 C CA . THR A 1 148 ? -1.652 -6.385 35.387 1.00 24.42 ? 148 THR A CA 1 ATOM 1137 C C . THR A 1 148 ? -2.829 -5.407 35.554 1.00 26.06 ? 148 THR A C 1 ATOM 1138 O O . THR A 1 148 ? -3.533 -5.439 36.571 1.00 26.69 ? 148 THR A O 1 ATOM 1139 C CB . THR A 1 148 ? -0.649 -6.072 36.512 1.00 24.71 ? 148 THR A CB 1 ATOM 1140 O OG1 . THR A 1 148 ? 0.018 -4.825 36.227 1.00 24.02 ? 148 THR A OG1 1 ATOM 1141 C CG2 . THR A 1 148 ? 0.397 -7.163 36.584 1.00 25.56 ? 148 THR A CG2 1 ATOM 1142 N N . ARG A 1 149 ? -3.045 -4.529 34.584 1.00 26.98 ? 149 ARG A N 1 ATOM 1143 C CA . ARG A 1 149 ? -4.125 -3.556 34.691 1.00 29.26 ? 149 ARG A CA 1 ATOM 1144 C C . ARG A 1 149 ? -5.293 -3.879 33.781 1.00 28.99 ? 149 ARG A C 1 ATOM 1145 O O . ARG A 1 149 ? -5.084 -4.112 32.591 1.00 26.32 ? 149 ARG A O 1 ATOM 1146 C CB . ARG A 1 149 ? -3.644 -2.162 34.330 1.00 30.30 ? 149 ARG A CB 1 ATOM 1147 C CG . ARG A 1 149 ? -4.561 -1.101 34.919 1.00 34.67 ? 149 ARG A CG 1 ATOM 1148 C CD . ARG A 1 149 ? -4.569 0.165 34.085 1.00 37.76 ? 149 ARG A CD 1 ATOM 1149 N NE . ARG A 1 149 ? -3.390 0.967 34.345 1.00 38.48 ? 149 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 149 ? -3.269 1.796 35.373 1.00 41.10 ? 149 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 149 ? -4.260 1.935 36.242 1.00 40.34 ? 149 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 149 ? -2.146 2.480 35.541 1.00 41.69 ? 149 ARG A NH2 1 ATOM 1153 N N . LYS A 1 150 ? -6.510 -3.839 34.332 1.00 29.04 ? 150 LYS A N 1 ATOM 1154 C CA . LYS A 1 150 ? -7.733 -3.853 33.503 1.00 31.32 ? 150 LYS A CA 1 ATOM 1155 C C . LYS A 1 150 ? -7.708 -2.694 32.516 1.00 30.26 ? 150 LYS A C 1 ATOM 1156 O O . LYS A 1 150 ? -7.404 -1.570 32.892 1.00 30.76 ? 150 LYS A O 1 ATOM 1157 C CB . LYS A 1 150 ? -9.016 -3.723 34.346 1.00 33.12 ? 150 LYS A CB 1 ATOM 1158 C CG . LYS A 1 150 ? -9.801 -5.007 34.512 1.00 37.06 ? 150 LYS A CG 1 ATOM 1159 C CD . LYS A 1 150 ? -11.234 -4.757 34.952 1.00 40.48 ? 150 LYS A CD 1 ATOM 1160 C CE . LYS A 1 150 ? -12.087 -6.006 34.746 1.00 44.46 ? 150 LYS A CE 1 ATOM 1161 N NZ . LYS A 1 150 ? -11.558 -7.202 35.470 1.00 46.90 ? 150 LYS A NZ 1 ATOM 1162 N N . ALA A 1 151 ? -8.042 -2.974 31.265 1.00 29.96 ? 151 ALA A N 1 ATOM 1163 C CA . ALA A 1 151 ? -8.141 -1.934 30.237 1.00 29.45 ? 151 ALA A CA 1 ATOM 1164 C C . ALA A 1 151 ? -9.119 -2.397 29.186 1.00 27.59 ? 151 ALA A C 1 ATOM 1165 O O . ALA A 1 151 ? -9.371 -3.589 29.068 1.00 31.03 ? 151 ALA A O 1 ATOM 1166 C CB . ALA A 1 151 ? -6.784 -1.705 29.607 1.00 30.62 ? 151 ALA A CB 1 ATOM 1167 N N . ASN A 1 152 ? -9.666 -1.489 28.400 1.00 24.56 ? 152 ASN A N 1 ATOM 1168 C CA . ASN A 1 152 ? -10.396 -1.953 27.221 1.00 22.34 ? 152 ASN A CA 1 ATOM 1169 C C . ASN A 1 152 ? -9.498 -1.969 25.999 1.00 20.88 ? 152 ASN A C 1 ATOM 1170 O O . ASN A 1 152 ? -8.466 -1.288 25.966 1.00 19.61 ? 152 ASN A O 1 ATOM 1171 C CB . ASN A 1 152 ? -11.673 -1.163 26.986 1.00 22.06 ? 152 ASN A CB 1 ATOM 1172 C CG . ASN A 1 152 ? -11.409 0.243 26.578 1.00 20.73 ? 152 ASN A CG 1 ATOM 1173 O OD1 . ASN A 1 152 ? -11.047 0.507 25.435 1.00 20.91 ? 152 ASN A OD1 1 ATOM 1174 N ND2 . ASN A 1 152 ? -11.581 1.164 27.512 1.00 21.31 ? 152 ASN A ND2 1 ATOM 1175 N N . LEU A 1 153 ? -9.892 -2.748 24.995 1.00 19.73 ? 153 LEU A N 1 ATOM 1176 C CA . LEU A 1 153 ? -9.075 -2.925 23.805 1.00 20.10 ? 153 LEU A CA 1 ATOM 1177 C C . LEU A 1 153 ? -8.821 -1.608 23.092 1.00 20.41 ? 153 LEU A C 1 ATOM 1178 O O . LEU A 1 153 ? -7.757 -1.405 22.492 1.00 18.12 ? 153 LEU A O 1 ATOM 1179 C CB . LEU A 1 153 ? -9.727 -3.911 22.829 1.00 20.98 ? 153 LEU A CB 1 ATOM 1180 C CG . LEU A 1 153 ? -8.867 -4.377 21.659 1.00 23.18 ? 153 LEU A CG 1 ATOM 1181 C CD1 . LEU A 1 153 ? -7.526 -4.878 22.172 1.00 23.40 ? 153 LEU A CD1 1 ATOM 1182 C CD2 . LEU A 1 153 ? -9.593 -5.477 20.861 1.00 24.08 ? 153 LEU A CD2 1 ATOM 1183 N N . HIS A 1 154 ? -9.796 -0.713 23.144 1.00 19.69 ? 154 HIS A N 1 ATOM 1184 C CA . HIS A 1 154 ? -9.654 0.543 22.431 1.00 19.40 ? 154 HIS A CA 1 ATOM 1185 C C . HIS A 1 154 ? -8.517 1.322 23.073 1.00 19.10 ? 154 HIS A C 1 ATOM 1186 O O . HIS A 1 154 ? -7.646 1.841 22.375 1.00 14.95 ? 154 HIS A O 1 ATOM 1187 C CB . HIS A 1 154 ? -10.945 1.370 22.503 1.00 19.35 ? 154 HIS A CB 1 ATOM 1188 C CG . HIS A 1 154 ? -10.868 2.637 21.737 1.00 19.24 ? 154 HIS A CG 1 ATOM 1189 N ND1 . HIS A 1 154 ? -11.192 2.711 20.400 1.00 20.94 ? 154 HIS A ND1 1 ATOM 1190 C CD2 . HIS A 1 154 ? -10.468 3.872 22.099 1.00 19.75 ? 154 HIS A CD2 1 ATOM 1191 C CE1 . HIS A 1 154 ? -10.972 3.936 19.966 1.00 20.91 ? 154 HIS A CE1 1 ATOM 1192 N NE2 . HIS A 1 154 ? -10.525 4.659 20.975 1.00 20.52 ? 154 HIS A NE2 1 ATOM 1193 N N . HIS A 1 155 ? -8.573 1.420 24.411 1.00 19.41 ? 155 HIS A N 1 ATOM 1194 C CA . HIS A 1 155 ? -7.596 2.177 25.168 1.00 19.63 ? 155 HIS A CA 1 ATOM 1195 C C . HIS A 1 155 ? -6.168 1.632 24.976 1.00 19.30 ? 155 HIS A C 1 ATOM 1196 O O . HIS A 1 155 ? -5.198 2.389 24.900 1.00 15.89 ? 155 HIS A O 1 ATOM 1197 C CB . HIS A 1 155 ? -7.943 2.183 26.648 1.00 21.49 ? 155 HIS A CB 1 ATOM 1198 C CG . HIS A 1 155 ? -7.185 3.202 27.440 1.00 23.34 ? 155 HIS A CG 1 ATOM 1199 N ND1 . HIS A 1 155 ? -6.109 2.876 28.246 1.00 24.79 ? 155 HIS A ND1 1 ATOM 1200 C CD2 . HIS A 1 155 ? -7.334 4.545 27.535 1.00 24.25 ? 155 HIS A CD2 1 ATOM 1201 C CE1 . HIS A 1 155 ? -5.644 3.972 28.821 1.00 24.67 ? 155 HIS A CE1 1 ATOM 1202 N NE2 . HIS A 1 155 ? -6.379 4.996 28.418 1.00 25.94 ? 155 HIS A NE2 1 ATOM 1203 N N . ILE A 1 156 ? -6.056 0.309 24.878 1.00 19.98 ? 156 ILE A N 1 ATOM 1204 C CA . ILE A 1 156 ? -4.772 -0.334 24.630 1.00 19.64 ? 156 ILE A CA 1 ATOM 1205 C C . ILE A 1 156 ? -4.135 0.176 23.337 1.00 20.50 ? 156 ILE A C 1 ATOM 1206 O O . ILE A 1 156 ? -2.892 0.340 23.258 1.00 19.66 ? 156 ILE A O 1 ATOM 1207 C CB . ILE A 1 156 ? -4.935 -1.866 24.610 1.00 20.01 ? 156 ILE A CB 1 ATOM 1208 C CG1 . ILE A 1 156 ? -5.021 -2.364 26.060 1.00 20.69 ? 156 ILE A CG1 1 ATOM 1209 C CG2 . ILE A 1 156 ? -3.796 -2.535 23.863 1.00 19.12 ? 156 ILE A CG2 1 ATOM 1210 C CD1 . ILE A 1 156 ? -5.591 -3.757 26.223 1.00 21.49 ? 156 ILE A CD1 1 ATOM 1211 N N . TRP A 1 157 ? -4.971 0.402 22.315 1.00 18.57 ? 157 TRP A N 1 ATOM 1212 C CA . TRP A 1 157 ? -4.480 0.948 21.047 1.00 17.92 ? 157 TRP A CA 1 ATOM 1213 C C . TRP A 1 157 ? -4.285 2.472 21.064 1.00 19.14 ? 157 TRP A C 1 ATOM 1214 O O . TRP A 1 157 ? -3.359 2.982 20.421 1.00 19.86 ? 157 TRP A O 1 ATOM 1215 C CB . TRP A 1 157 ? -5.365 0.517 19.884 1.00 17.60 ? 157 TRP A CB 1 ATOM 1216 C CG . TRP A 1 157 ? -5.032 -0.886 19.494 1.00 18.01 ? 157 TRP A CG 1 ATOM 1217 C CD1 . TRP A 1 157 ? -5.383 -2.032 20.155 1.00 17.40 ? 157 TRP A CD1 1 ATOM 1218 C CD2 . TRP A 1 157 ? -4.187 -1.284 18.419 1.00 18.08 ? 157 TRP A CD2 1 ATOM 1219 N NE1 . TRP A 1 157 ? -4.848 -3.120 19.510 1.00 18.39 ? 157 TRP A NE1 1 ATOM 1220 C CE2 . TRP A 1 157 ? -4.101 -2.686 18.451 1.00 17.51 ? 157 TRP A CE2 1 ATOM 1221 C CE3 . TRP A 1 157 ? -3.498 -0.587 17.423 1.00 18.08 ? 157 TRP A CE3 1 ATOM 1222 C CZ2 . TRP A 1 157 ? -3.364 -3.402 17.528 1.00 18.46 ? 157 TRP A CZ2 1 ATOM 1223 C CZ3 . TRP A 1 157 ? -2.767 -1.310 16.499 1.00 18.62 ? 157 TRP A CZ3 1 ATOM 1224 C CH2 . TRP A 1 157 ? -2.705 -2.697 16.557 1.00 18.11 ? 157 TRP A CH2 1 ATOM 1225 N N . ASP A 1 158 ? -5.133 3.195 21.787 1.00 18.08 ? 158 ASP A N 1 ATOM 1226 C CA . ASP A 1 158 ? -4.942 4.656 21.958 1.00 19.03 ? 158 ASP A CA 1 ATOM 1227 C C . ASP A 1 158 ? -3.639 5.007 22.657 1.00 19.40 ? 158 ASP A C 1 ATOM 1228 O O . ASP A 1 158 ? -2.931 5.912 22.220 1.00 20.41 ? 158 ASP A O 1 ATOM 1229 C CB . ASP A 1 158 ? -6.084 5.271 22.774 1.00 18.61 ? 158 ASP A CB 1 ATOM 1230 C CG . ASP A 1 158 ? -7.268 5.645 21.932 1.00 19.37 ? 158 ASP A CG 1 ATOM 1231 O OD1 . ASP A 1 158 ? -7.135 5.630 20.701 1.00 19.32 ? 158 ASP A OD1 1 ATOM 1232 O OD2 . ASP A 1 158 ? -8.342 5.985 22.496 1.00 18.63 ? 158 ASP A OD2 1 ATOM 1233 N N . SER A 1 159 ? -3.355 4.283 23.748 1.00 20.01 ? 159 SER A N 1 ATOM 1234 C CA . SER A 1 159 ? -2.341 4.636 24.716 1.00 20.29 ? 159 SER A CA 1 ATOM 1235 C C . SER A 1 159 ? -1.377 3.543 25.186 1.00 21.33 ? 159 SER A C 1 ATOM 1236 O O . SER A 1 159 ? -0.151 3.754 25.153 1.00 20.89 ? 159 SER A O 1 ATOM 1237 C CB . SER A 1 159 ? -3.027 5.170 25.959 1.00 20.90 ? 159 SER A CB 1 ATOM 1238 O OG . SER A 1 159 ? -3.833 6.260 25.598 1.00 20.93 ? 159 SER A OG 1 ATOM 1239 N N . ASN A 1 160 ? -1.910 2.431 25.694 1.00 20.69 ? 160 ASN A N 1 ATOM 1240 C CA . ASN A 1 160 ? -1.075 1.496 26.439 1.00 21.91 ? 160 ASN A CA 1 ATOM 1241 C C . ASN A 1 160 ? 0.106 0.999 25.637 1.00 19.93 ? 160 ASN A C 1 ATOM 1242 O O . ASN A 1 160 ? 1.214 0.978 26.157 1.00 18.87 ? 160 ASN A O 1 ATOM 1243 C CB . ASN A 1 160 ? -1.865 0.291 26.965 1.00 24.83 ? 160 ASN A CB 1 ATOM 1244 C CG . ASN A 1 160 ? -2.950 0.667 27.959 1.00 26.81 ? 160 ASN A CG 1 ATOM 1245 O OD1 . ASN A 1 160 ? -4.036 0.110 27.926 1.00 32.78 ? 160 ASN A OD1 1 ATOM 1246 N ND2 . ASN A 1 160 ? -2.656 1.589 28.857 1.00 27.59 ? 160 ASN A ND2 1 ATOM 1247 N N . ILE A 1 161 ? -0.117 0.607 24.382 1.00 18.00 ? 161 ILE A N 1 ATOM 1248 C CA . ILE A 1 161 ? 0.970 0.069 23.572 1.00 19.28 ? 161 ILE A CA 1 ATOM 1249 C C . ILE A 1 161 ? 2.117 1.083 23.415 1.00 18.57 ? 161 ILE A C 1 ATOM 1250 O O . ILE A 1 161 ? 3.272 0.760 23.688 1.00 18.09 ? 161 ILE A O 1 ATOM 1251 C CB . ILE A 1 161 ? 0.496 -0.421 22.181 1.00 19.40 ? 161 ILE A CB 1 ATOM 1252 C CG1 . ILE A 1 161 ? -0.437 -1.625 22.348 1.00 18.91 ? 161 ILE A CG1 1 ATOM 1253 C CG2 . ILE A 1 161 ? 1.691 -0.796 21.312 1.00 19.49 ? 161 ILE A CG2 1 ATOM 1254 C CD1 . ILE A 1 161 ? -1.400 -1.800 21.203 1.00 18.60 ? 161 ILE A CD1 1 ATOM 1255 N N . ILE A 1 162 ? 1.774 2.301 23.009 1.00 18.70 ? 162 ILE A N 1 ATOM 1256 C CA . ILE A 1 162 ? 2.745 3.413 22.889 1.00 19.21 ? 162 ILE A CA 1 ATOM 1257 C C . ILE A 1 162 ? 3.445 3.671 24.236 1.00 19.85 ? 162 ILE A C 1 ATOM 1258 O O . ILE A 1 162 ? 4.674 3.762 24.308 1.00 18.97 ? 162 ILE A O 1 ATOM 1259 C CB . ILE A 1 162 ? 2.026 4.697 22.435 1.00 18.33 ? 162 ILE A CB 1 ATOM 1260 C CG1 . ILE A 1 162 ? 1.545 4.532 20.987 1.00 18.21 ? 162 ILE A CG1 1 ATOM 1261 C CG2 . ILE A 1 162 ? 2.926 5.925 22.558 1.00 18.68 ? 162 ILE A CG2 1 ATOM 1262 C CD1 . ILE A 1 162 ? 0.569 5.593 20.549 1.00 17.30 ? 162 ILE A CD1 1 ATOM 1263 N N . GLU A 1 163 ? 2.656 3.779 25.292 1.00 21.45 ? 163 GLU A N 1 ATOM 1264 C CA . GLU A 1 163 ? 3.193 4.069 26.626 1.00 24.53 ? 163 GLU A CA 1 ATOM 1265 C C . GLU A 1 163 ? 4.193 2.995 27.081 1.00 24.14 ? 163 GLU A C 1 ATOM 1266 O O . GLU A 1 163 ? 5.211 3.304 27.699 1.00 24.08 ? 163 GLU A O 1 ATOM 1267 C CB . GLU A 1 163 ? 2.065 4.121 27.644 1.00 27.10 ? 163 GLU A CB 1 ATOM 1268 C CG . GLU A 1 163 ? 1.158 5.338 27.583 1.00 29.49 ? 163 GLU A CG 1 ATOM 1269 C CD . GLU A 1 163 ? 0.055 5.299 28.645 1.00 30.74 ? 163 GLU A CD 1 ATOM 1270 O OE1 . GLU A 1 163 ? -0.650 4.275 28.767 1.00 33.13 ? 163 GLU A OE1 1 ATOM 1271 O OE2 . GLU A 1 163 ? -0.118 6.298 29.376 1.00 35.58 ? 163 GLU A OE2 1 ATOM 1272 N N . THR A 1 164 ? 3.876 1.736 26.776 1.00 22.61 ? 164 THR A N 1 ATOM 1273 C CA . THR A 1 164 ? 4.684 0.612 27.195 1.00 22.20 ? 164 THR A CA 1 ATOM 1274 C C . THR A 1 164 ? 6.010 0.597 26.430 1.00 23.55 ? 164 THR A C 1 ATOM 1275 O O . THR A 1 164 ? 7.073 0.362 27.029 1.00 20.37 ? 164 THR A O 1 ATOM 1276 C CB . THR A 1 164 ? 3.920 -0.701 27.012 1.00 22.73 ? 164 THR A CB 1 ATOM 1277 O OG1 . THR A 1 164 ? 2.768 -0.679 27.846 1.00 20.78 ? 164 THR A OG1 1 ATOM 1278 C CG2 . THR A 1 164 ? 4.773 -1.891 27.403 1.00 23.65 ? 164 THR A CG2 1 ATOM 1279 N N . ALA A 1 165 ? 5.941 0.873 25.121 1.00 22.91 ? 165 ALA A N 1 ATOM 1280 C CA . ALA A 1 165 ? 7.132 0.989 24.300 1.00 23.21 ? 165 ALA A CA 1 ATOM 1281 C C . ALA A 1 165 ? 7.952 2.172 24.789 1.00 22.83 ? 165 ALA A C 1 ATOM 1282 O O . ALA A 1 165 ? 9.152 2.067 24.913 1.00 24.99 ? 165 ALA A O 1 ATOM 1283 C CB . ALA A 1 165 ? 6.767 1.188 22.845 1.00 23.43 ? 165 ALA A CB 1 ATOM 1284 N N . GLU A 1 166 ? 7.295 3.297 25.033 1.00 22.89 ? 166 GLU A N 1 ATOM 1285 C CA . GLU A 1 166 ? 7.959 4.470 25.553 1.00 25.91 ? 166 GLU A CA 1 ATOM 1286 C C . GLU A 1 166 ? 8.848 4.139 26.768 1.00 26.82 ? 166 GLU A C 1 ATOM 1287 O O . GLU A 1 166 ? 10.010 4.559 26.829 1.00 26.50 ? 166 GLU A O 1 ATOM 1288 C CB . GLU A 1 166 ? 6.926 5.531 25.931 1.00 28.26 ? 166 GLU A CB 1 ATOM 1289 C CG . GLU A 1 166 ? 7.479 6.932 26.144 1.00 31.65 ? 166 GLU A CG 1 ATOM 1290 C CD . GLU A 1 166 ? 6.558 7.846 26.941 1.00 35.77 ? 166 GLU A CD 1 ATOM 1291 O OE1 . GLU A 1 166 ? 5.335 7.560 27.065 1.00 39.90 ? 166 GLU A OE1 1 ATOM 1292 O OE2 . GLU A 1 166 ? 7.060 8.877 27.446 1.00 42.27 ? 166 GLU A OE2 1 ATOM 1293 N N . ALA A 1 167 ? 8.304 3.410 27.741 1.00 27.70 ? 167 ALA A N 1 ATOM 1294 C CA . ALA A 1 167 ? 9.054 3.134 28.977 1.00 30.47 ? 167 ALA A CA 1 ATOM 1295 C C . ALA A 1 167 ? 10.020 1.952 28.809 1.00 32.81 ? 167 ALA A C 1 ATOM 1296 O O . ALA A 1 167 ? 11.101 1.950 29.396 1.00 32.76 ? 167 ALA A O 1 ATOM 1297 C CB . ALA A 1 167 ? 8.098 2.901 30.144 1.00 31.51 ? 167 ALA A CB 1 ATOM 1298 N N . ASP A 1 168 ? 9.655 0.976 27.976 1.00 32.85 ? 168 ASP A N 1 ATOM 1299 C CA . ASP A 1 168 ? 10.420 -0.271 27.882 1.00 39.38 ? 168 ASP A CA 1 ATOM 1300 C C . ASP A 1 168 ? 11.500 -0.278 26.768 1.00 39.30 ? 168 ASP A C 1 ATOM 1301 O O . ASP A 1 168 ? 12.522 -0.932 26.915 1.00 43.98 ? 168 ASP A O 1 ATOM 1302 C CB . ASP A 1 168 ? 9.464 -1.472 27.759 1.00 41.88 ? 168 ASP A CB 1 ATOM 1303 C CG . ASP A 1 168 ? 8.351 -1.476 28.853 1.00 46.85 ? 168 ASP A CG 1 ATOM 1304 O OD1 . ASP A 1 168 ? 8.241 -0.510 29.653 1.00 48.00 ? 168 ASP A OD1 1 ATOM 1305 O OD2 . ASP A 1 168 ? 7.555 -2.449 28.893 1.00 52.28 ? 168 ASP A OD2 1 ATOM 1306 N N . LEU A 1 169 ? 11.293 0.453 25.678 1.00 36.02 ? 169 LEU A N 1 ATOM 1307 C CA . LEU A 1 169 ? 12.255 0.453 24.570 1.00 35.18 ? 169 LEU A CA 1 ATOM 1308 C C . LEU A 1 169 ? 12.801 1.821 24.214 1.00 34.33 ? 169 LEU A C 1 ATOM 1309 O O . LEU A 1 169 ? 13.459 1.960 23.180 1.00 35.45 ? 169 LEU A O 1 ATOM 1310 C CB . LEU A 1 169 ? 11.610 -0.143 23.297 1.00 35.21 ? 169 LEU A CB 1 ATOM 1311 C CG . LEU A 1 169 ? 10.649 -1.311 23.511 1.00 35.47 ? 169 LEU A CG 1 ATOM 1312 C CD1 . LEU A 1 169 ? 9.951 -1.651 22.212 1.00 37.14 ? 169 LEU A CD1 1 ATOM 1313 C CD2 . LEU A 1 169 ? 11.337 -2.532 24.122 1.00 34.83 ? 169 LEU A CD2 1 ATOM 1314 N N . TYR A 1 170 ? 12.483 2.835 25.015 1.00 35.11 ? 170 TYR A N 1 ATOM 1315 C CA . TYR A 1 170 ? 12.962 4.210 24.766 1.00 34.37 ? 170 TYR A CA 1 ATOM 1316 C C . TYR A 1 170 ? 13.167 4.988 26.069 1.00 36.13 ? 170 TYR A C 1 ATOM 1317 O O . TYR A 1 170 ? 13.065 6.236 26.099 1.00 36.22 ? 170 TYR A O 1 ATOM 1318 C CB . TYR A 1 170 ? 12.024 4.956 23.793 1.00 32.67 ? 170 TYR A CB 1 ATOM 1319 C CG . TYR A 1 170 ? 11.801 4.222 22.482 1.00 32.33 ? 170 TYR A CG 1 ATOM 1320 C CD1 . TYR A 1 170 ? 12.822 4.130 21.530 1.00 32.86 ? 170 TYR A CD1 1 ATOM 1321 C CD2 . TYR A 1 170 ? 10.596 3.572 22.217 1.00 30.24 ? 170 TYR A CD2 1 ATOM 1322 C CE1 . TYR A 1 170 ? 12.635 3.459 20.338 1.00 30.74 ? 170 TYR A CE1 1 ATOM 1323 C CE2 . TYR A 1 170 ? 10.402 2.894 21.038 1.00 30.90 ? 170 TYR A CE2 1 ATOM 1324 C CZ . TYR A 1 170 ? 11.425 2.839 20.099 1.00 32.84 ? 170 TYR A CZ 1 ATOM 1325 O OH . TYR A 1 170 ? 11.240 2.156 18.911 1.00 36.74 ? 170 TYR A OH 1 ATOM 1326 N N . ASN A 1 171 ? 13.478 4.239 27.132 1.00 40.98 ? 171 ASN A N 1 ATOM 1327 C CA . ASN A 1 171 ? 13.867 4.790 28.437 1.00 46.56 ? 171 ASN A CA 1 ATOM 1328 C C . ASN A 1 171 ? 13.135 6.080 28.795 1.00 48.36 ? 171 ASN A C 1 ATOM 1329 O O . ASN A 1 171 ? 13.767 7.085 29.138 1.00 50.91 ? 171 ASN A O 1 ATOM 1330 C CB . ASN A 1 171 ? 15.394 5.007 28.494 1.00 49.54 ? 171 ASN A CB 1 ATOM 1331 C CG . ASN A 1 171 ? 16.184 3.700 28.414 1.00 53.54 ? 171 ASN A CG 1 ATOM 1332 O OD1 . ASN A 1 171 ? 16.784 3.267 29.395 1.00 54.91 ? 171 ASN A OD1 1 ATOM 1333 N ND2 . ASN A 1 171 ? 16.191 3.075 27.241 1.00 53.69 ? 171 ASN A ND2 1 ATOM 1334 N N . SER A 1 172 ? 11.802 6.040 28.673 1.00 50.63 ? 172 SER A N 1 ATOM 1335 C CA . SER A 1 172 ? 10.892 7.135 29.064 1.00 49.40 ? 172 SER A CA 1 ATOM 1336 C C . SER A 1 172 ? 11.057 8.451 28.269 1.00 50.66 ? 172 SER A C 1 ATOM 1337 O O . SER A 1 172 ? 10.559 9.503 28.695 1.00 49.51 ? 172 SER A O 1 ATOM 1338 C CB . SER A 1 172 ? 10.971 7.389 30.584 1.00 51.13 ? 172 SER A CB 1 ATOM 1339 O OG . SER A 1 172 ? 10.033 6.598 31.295 1.00 49.93 ? 172 SER A OG 1 ATOM 1340 N N . ALA A 1 173 ? 11.721 8.381 27.109 1.00 50.96 ? 173 ALA A N 1 ATOM 1341 C CA . ALA A 1 173 ? 11.861 9.533 26.202 1.00 49.43 ? 173 ALA A CA 1 ATOM 1342 C C . ALA A 1 173 ? 11.079 9.305 24.887 1.00 47.20 ? 173 ALA A C 1 ATOM 1343 O O . ALA A 1 173 ? 11.505 8.529 24.008 1.00 41.74 ? 173 ALA A O 1 ATOM 1344 C CB . ALA A 1 173 ? 13.334 9.818 25.916 1.00 49.59 ? 173 ALA A CB 1 ATOM 1345 N N . LEU A 1 174 ? 9.936 9.991 24.778 1.00 44.30 ? 174 LEU A N 1 ATOM 1346 C CA . LEU A 1 174 ? 9.091 9.988 23.566 1.00 42.45 ? 174 LEU A CA 1 ATOM 1347 C C . LEU A 1 174 ? 9.846 10.439 22.295 1.00 38.32 ? 174 LEU A C 1 ATOM 1348 O O . LEU A 1 174 ? 9.664 9.853 21.217 1.00 34.05 ? 174 LEU A O 1 ATOM 1349 C CB . LEU A 1 174 ? 7.842 10.857 23.802 1.00 41.36 ? 174 LEU A CB 1 ATOM 1350 C CG . LEU A 1 174 ? 6.809 11.035 22.679 1.00 41.39 ? 174 LEU A CG 1 ATOM 1351 C CD1 . LEU A 1 174 ? 5.383 10.898 23.197 1.00 40.30 ? 174 LEU A CD1 1 ATOM 1352 C CD2 . LEU A 1 174 ? 6.984 12.380 21.979 1.00 40.67 ? 174 LEU A CD2 1 ATOM 1353 N N . GLU A 1 175 ? 10.703 11.458 22.421 1.00 34.20 ? 175 GLU A N 1 ATOM 1354 C CA . GLU A 1 175 ? 11.548 11.868 21.286 1.00 35.05 ? 175 GLU A CA 1 ATOM 1355 C C . GLU A 1 175 ? 12.467 10.709 20.865 1.00 26.22 ? 175 GLU A C 1 ATOM 1356 O O . GLU A 1 175 ? 12.994 10.692 19.801 1.00 23.85 ? 175 GLU A O 1 ATOM 1357 C CB . GLU A 1 175 ? 12.362 13.147 21.593 1.00 36.74 ? 175 GLU A CB 1 ATOM 1358 C CG . GLU A 1 175 ? 13.099 13.765 20.384 1.00 41.33 ? 175 GLU A CG 1 ATOM 1359 C CD . GLU A 1 175 ? 12.196 14.326 19.263 1.00 44.45 ? 175 GLU A CD 1 ATOM 1360 O OE1 . GLU A 1 175 ? 11.054 14.757 19.541 1.00 43.15 ? 175 GLU A OE1 1 ATOM 1361 O OE2 . GLU A 1 175 ? 12.630 14.346 18.079 1.00 45.06 ? 175 GLU A OE2 1 ATOM 1362 N N . GLY A 1 176 ? 12.697 9.771 21.754 1.00 27.16 ? 176 GLY A N 1 ATOM 1363 C CA . GLY A 1 176 ? 13.385 8.553 21.392 1.00 26.76 ? 176 GLY A CA 1 ATOM 1364 C C . GLY A 1 176 ? 12.654 7.811 20.290 1.00 26.86 ? 176 GLY A C 1 ATOM 1365 O O . GLY A 1 176 ? 13.205 7.572 19.206 1.00 26.38 ? 176 GLY A O 1 ATOM 1366 N N . MET A 1 177 ? 11.432 7.391 20.602 1.00 25.42 ? 177 MET A N 1 ATOM 1367 C CA . MET A 1 177 ? 10.522 6.839 19.617 1.00 25.91 ? 177 MET A CA 1 ATOM 1368 C C . MET A 1 177 ? 10.236 7.746 18.392 1.00 23.16 ? 177 MET A C 1 ATOM 1369 O O . MET A 1 177 ? 10.124 7.246 17.295 1.00 22.02 ? 177 MET A O 1 ATOM 1370 C CB . MET A 1 177 ? 9.199 6.510 20.321 1.00 26.75 ? 177 MET A CB 1 ATOM 1371 C CG . MET A 1 177 ? 8.216 5.733 19.484 1.00 26.62 ? 177 MET A CG 1 ATOM 1372 S SD . MET A 1 177 ? 6.762 5.475 20.494 1.00 28.95 ? 177 MET A SD 1 ATOM 1373 C CE . MET A 1 177 ? 5.488 5.507 19.254 1.00 33.74 ? 177 MET A CE 1 ATOM 1374 N N . VAL A 1 178 ? 10.097 9.066 18.553 1.00 25.00 ? 178 VAL A N 1 ATOM 1375 C CA . VAL A 1 178 ? 9.877 9.963 17.367 1.00 25.17 ? 178 VAL A CA 1 ATOM 1376 C C . VAL A 1 178 ? 11.101 9.910 16.425 1.00 25.38 ? 178 VAL A C 1 ATOM 1377 O O . VAL A 1 178 ? 10.973 9.688 15.187 1.00 21.03 ? 178 VAL A O 1 ATOM 1378 C CB . VAL A 1 178 ? 9.588 11.460 17.744 1.00 27.57 ? 178 VAL A CB 1 ATOM 1379 C CG1 . VAL A 1 178 ? 9.738 12.363 16.539 1.00 26.25 ? 178 VAL A CG1 1 ATOM 1380 C CG2 . VAL A 1 178 ? 8.169 11.649 18.297 1.00 27.63 ? 178 VAL A CG2 1 ATOM 1381 N N . ASP A 1 179 ? 12.283 10.068 17.015 1.00 22.81 ? 179 ASP A N 1 ATOM 1382 C CA . ASP A 1 179 ? 13.504 9.927 16.243 1.00 24.64 ? 179 ASP A CA 1 ATOM 1383 C C . ASP A 1 179 ? 13.602 8.559 15.545 1.00 22.77 ? 179 ASP A C 1 ATOM 1384 O O . ASP A 1 179 ? 13.891 8.526 14.370 1.00 21.47 ? 179 ASP A O 1 ATOM 1385 C CB . ASP A 1 179 ? 14.735 10.253 17.094 1.00 26.94 ? 179 ASP A CB 1 ATOM 1386 C CG . ASP A 1 179 ? 14.803 11.725 17.431 1.00 27.72 ? 179 ASP A CG 1 ATOM 1387 O OD1 . ASP A 1 179 ? 14.137 12.477 16.705 1.00 27.78 ? 179 ASP A OD1 1 ATOM 1388 O OD2 . ASP A 1 179 ? 15.465 12.133 18.406 1.00 30.55 ? 179 ASP A OD2 1 ATOM 1389 N N . ALA A 1 180 ? 13.294 7.457 16.229 1.00 21.89 ? 180 ALA A N 1 ATOM 1390 C CA . ALA A 1 180 ? 13.271 6.119 15.538 1.00 21.59 ? 180 ALA A CA 1 ATOM 1391 C C . ALA A 1 180 ? 12.224 5.979 14.415 1.00 22.22 ? 180 ALA A C 1 ATOM 1392 O O . ALA A 1 180 ? 12.496 5.296 13.432 1.00 23.20 ? 180 ALA A O 1 ATOM 1393 C CB . ALA A 1 180 ? 13.077 4.986 16.523 1.00 21.66 ? 180 ALA A CB 1 ATOM 1394 N N . LEU A 1 181 ? 11.026 6.549 14.561 1.00 21.23 ? 181 LEU A N 1 ATOM 1395 C CA . LEU A 1 181 ? 10.064 6.522 13.428 1.00 21.81 ? 181 LEU A CA 1 ATOM 1396 C C . LEU A 1 181 ? 10.609 7.339 12.254 1.00 20.91 ? 181 LEU A C 1 ATOM 1397 O O . LEU A 1 181 ? 10.646 6.859 11.132 1.00 20.83 ? 181 LEU A O 1 ATOM 1398 C CB . LEU A 1 181 ? 8.702 7.059 13.829 1.00 20.33 ? 181 LEU A CB 1 ATOM 1399 C CG . LEU A 1 181 ? 8.019 6.201 14.884 1.00 19.45 ? 181 LEU A CG 1 ATOM 1400 C CD1 . LEU A 1 181 ? 6.794 6.898 15.443 1.00 18.82 ? 181 LEU A CD1 1 ATOM 1401 C CD2 . LEU A 1 181 ? 7.694 4.856 14.272 1.00 20.96 ? 181 LEU A CD2 1 ATOM 1402 N N . LYS A 1 182 ? 11.077 8.544 12.550 1.00 21.03 ? 182 LYS A N 1 ATOM 1403 C CA . LYS A 1 182 ? 11.756 9.381 11.572 1.00 22.21 ? 182 LYS A CA 1 ATOM 1404 C C . LYS A 1 182 ? 12.891 8.658 10.889 1.00 22.73 ? 182 LYS A C 1 ATOM 1405 O O . LYS A 1 182 ? 13.008 8.743 9.672 1.00 22.21 ? 182 LYS A O 1 ATOM 1406 C CB . LYS A 1 182 ? 12.287 10.651 12.213 1.00 23.71 ? 182 LYS A CB 1 ATOM 1407 C CG . LYS A 1 182 ? 11.245 11.741 12.411 1.00 25.91 ? 182 LYS A CG 1 ATOM 1408 C CD . LYS A 1 182 ? 11.848 12.872 13.234 1.00 26.72 ? 182 LYS A CD 1 ATOM 1409 C CE . LYS A 1 182 ? 11.002 14.128 13.209 1.00 28.76 ? 182 LYS A CE 1 ATOM 1410 N NZ . LYS A 1 182 ? 11.413 15.115 14.262 1.00 29.35 ? 182 LYS A NZ 1 ATOM 1411 N N . LYS A 1 183 ? 13.749 7.983 11.654 1.00 23.64 ? 183 LYS A N 1 ATOM 1412 C CA . LYS A 1 183 ? 14.832 7.193 11.046 1.00 25.47 ? 183 LYS A CA 1 ATOM 1413 C C . LYS A 1 183 ? 14.295 6.186 10.038 1.00 25.81 ? 183 LYS A C 1 ATOM 1414 O O . LYS A 1 183 ? 14.828 6.059 8.937 1.00 25.67 ? 183 LYS A O 1 ATOM 1415 C CB . LYS A 1 183 ? 15.639 6.450 12.092 1.00 27.18 ? 183 LYS A CB 1 ATOM 1416 C CG . LYS A 1 183 ? 16.776 5.621 11.512 1.00 30.84 ? 183 LYS A CG 1 ATOM 1417 C CD . LYS A 1 183 ? 17.104 4.409 12.386 1.00 32.56 ? 183 LYS A CD 1 ATOM 1418 C CE . LYS A 1 183 ? 18.162 4.737 13.433 1.00 35.70 ? 183 LYS A CE 1 ATOM 1419 N NZ . LYS A 1 183 ? 19.537 4.731 12.849 1.00 37.41 ? 183 LYS A NZ 1 ATOM 1420 N N . ASN A 1 184 ? 13.260 5.447 10.406 1.00 25.68 ? 184 ASN A N 1 ATOM 1421 C CA . ASN A 1 184 ? 12.727 4.421 9.494 1.00 25.03 ? 184 ASN A CA 1 ATOM 1422 C C . ASN A 1 184 ? 11.959 4.964 8.292 1.00 25.62 ? 184 ASN A C 1 ATOM 1423 O O . ASN A 1 184 ? 11.851 4.289 7.242 1.00 26.96 ? 184 ASN A O 1 ATOM 1424 C CB . ASN A 1 184 ? 11.865 3.440 10.259 1.00 25.10 ? 184 ASN A CB 1 ATOM 1425 C CG . ASN A 1 184 ? 12.678 2.471 11.046 1.00 25.78 ? 184 ASN A CG 1 ATOM 1426 O OD1 . ASN A 1 184 ? 13.901 2.546 11.082 1.00 26.65 ? 184 ASN A OD1 1 ATOM 1427 N ND2 . ASN A 1 184 ? 12.000 1.549 11.699 1.00 27.86 ? 184 ASN A ND2 1 ATOM 1428 N N . ILE A 1 185 ? 11.435 6.175 8.438 1.00 24.09 ? 185 ILE A N 1 ATOM 1429 C CA . ILE A 1 185 ? 10.796 6.861 7.329 1.00 24.70 ? 185 ILE A CA 1 ATOM 1430 C C . ILE A 1 185 ? 11.809 7.123 6.203 1.00 26.50 ? 185 ILE A C 1 ATOM 1431 O O . ILE A 1 185 ? 11.496 6.903 5.022 1.00 23.22 ? 185 ILE A O 1 ATOM 1432 C CB . ILE A 1 185 ? 10.111 8.155 7.809 1.00 23.80 ? 185 ILE A CB 1 ATOM 1433 C CG1 . ILE A 1 185 ? 8.787 7.773 8.473 1.00 23.66 ? 185 ILE A CG1 1 ATOM 1434 C CG2 . ILE A 1 185 ? 9.899 9.150 6.670 1.00 23.45 ? 185 ILE A CG2 1 ATOM 1435 C CD1 . ILE A 1 185 ? 8.138 8.885 9.285 1.00 23.33 ? 185 ILE A CD1 1 ATOM 1436 N N . THR A 1 186 ? 13.022 7.556 6.557 1.00 26.44 ? 186 THR A N 1 ATOM 1437 C CA . THR A 1 186 ? 13.997 7.908 5.522 1.00 28.03 ? 186 THR A CA 1 ATOM 1438 C C . THR A 1 186 ? 14.837 6.760 5.035 1.00 28.53 ? 186 THR A C 1 ATOM 1439 O O . THR A 1 186 ? 15.339 6.873 3.938 1.00 35.20 ? 186 THR A O 1 ATOM 1440 C CB . THR A 1 186 ? 14.917 9.071 5.939 1.00 30.43 ? 186 THR A CB 1 ATOM 1441 O OG1 . THR A 1 186 ? 14.164 10.002 6.723 1.00 32.18 ? 186 THR A OG1 1 ATOM 1442 C CG2 . THR A 1 186 ? 15.487 9.796 4.717 1.00 29.92 ? 186 THR A CG2 1 ATOM 1443 N N . THR A 1 187 ? 14.986 5.662 5.785 1.00 27.34 ? 187 THR A N 1 ATOM 1444 C CA . THR A 1 187 ? 15.922 4.578 5.371 1.00 30.21 ? 187 THR A CA 1 ATOM 1445 C C . THR A 1 187 ? 15.434 3.097 5.348 1.00 30.77 ? 187 THR A C 1 ATOM 1446 O O . THR A 1 187 ? 16.217 2.175 5.021 1.00 33.76 ? 187 THR A O 1 ATOM 1447 C CB . THR A 1 187 ? 17.152 4.548 6.280 1.00 29.76 ? 187 THR A CB 1 ATOM 1448 O OG1 . THR A 1 187 ? 16.825 3.823 7.470 1.00 28.45 ? 187 THR A OG1 1 ATOM 1449 C CG2 . THR A 1 187 ? 17.658 5.998 6.588 1.00 32.01 ? 187 THR A CG2 1 ATOM 1450 N N . GLU A 1 188 ? 14.205 2.868 5.776 1.00 29.21 ? 188 GLU A N 1 ATOM 1451 C CA . GLU A 1 188 ? 13.566 1.552 5.724 1.00 29.26 ? 188 GLU A CA 1 ATOM 1452 C C . GLU A 1 188 ? 12.277 1.614 4.908 1.00 29.42 ? 188 GLU A C 1 ATOM 1453 O O . GLU A 1 188 ? 12.001 0.725 4.085 1.00 27.36 ? 188 GLU A O 1 ATOM 1454 C CB . GLU A 1 188 ? 13.255 1.070 7.149 1.00 30.48 ? 188 GLU A CB 1 ATOM 1455 C CG . GLU A 1 188 ? 14.427 0.412 7.851 1.00 31.33 ? 188 GLU A CG 1 ATOM 1456 C CD . GLU A 1 188 ? 14.792 -0.926 7.214 1.00 32.18 ? 188 GLU A CD 1 ATOM 1457 O OE1 . GLU A 1 188 ? 15.194 -0.953 6.038 1.00 31.70 ? 188 GLU A OE1 1 ATOM 1458 O OE2 . GLU A 1 188 ? 14.629 -1.966 7.866 1.00 37.73 ? 188 GLU A OE2 1 ATOM 1459 N N . TRP A 1 189 ? 11.513 2.686 5.111 1.00 25.76 ? 189 TRP A N 1 ATOM 1460 C CA . TRP A 1 189 ? 10.212 2.850 4.495 1.00 26.75 ? 189 TRP A CA 1 ATOM 1461 C C . TRP A 1 189 ? 10.162 3.870 3.344 1.00 25.30 ? 189 TRP A C 1 ATOM 1462 O O . TRP A 1 189 ? 9.067 4.309 2.937 1.00 24.67 ? 189 TRP A O 1 ATOM 1463 C CB . TRP A 1 189 ? 9.218 3.256 5.585 1.00 28.25 ? 189 TRP A CB 1 ATOM 1464 C CG . TRP A 1 189 ? 9.208 2.307 6.765 1.00 29.35 ? 189 TRP A CG 1 ATOM 1465 C CD1 . TRP A 1 189 ? 9.475 0.963 6.748 1.00 30.21 ? 189 TRP A CD1 1 ATOM 1466 C CD2 . TRP A 1 189 ? 8.890 2.633 8.126 1.00 30.22 ? 189 TRP A CD2 1 ATOM 1467 N NE1 . TRP A 1 189 ? 9.356 0.443 8.010 1.00 30.25 ? 189 TRP A NE1 1 ATOM 1468 C CE2 . TRP A 1 189 ? 9.004 1.449 8.875 1.00 29.06 ? 189 TRP A CE2 1 ATOM 1469 C CE3 . TRP A 1 189 ? 8.546 3.824 8.790 1.00 29.23 ? 189 TRP A CE3 1 ATOM 1470 C CZ2 . TRP A 1 189 ? 8.757 1.412 10.239 1.00 30.11 ? 189 TRP A CZ2 1 ATOM 1471 C CZ3 . TRP A 1 189 ? 8.321 3.784 10.144 1.00 28.38 ? 189 TRP A CZ3 1 ATOM 1472 C CH2 . TRP A 1 189 ? 8.421 2.595 10.859 1.00 29.84 ? 189 TRP A CH2 1 ATOM 1473 N N . ALA A 1 190 ? 11.313 4.237 2.796 1.00 25.76 ? 190 ALA A N 1 ATOM 1474 C CA . ALA A 1 190 ? 11.359 5.361 1.849 1.00 29.84 ? 190 ALA A CA 1 ATOM 1475 C C . ALA A 1 190 ? 10.362 5.187 0.683 1.00 33.36 ? 190 ALA A C 1 ATOM 1476 O O . ALA A 1 190 ? 9.609 6.119 0.348 1.00 32.59 ? 190 ALA A O 1 ATOM 1477 C CB . ALA A 1 190 ? 12.768 5.582 1.333 1.00 31.61 ? 190 ALA A CB 1 ATOM 1478 N N . ASP A 1 191 ? 10.319 3.979 0.119 1.00 34.06 ? 191 ASP A N 1 ATOM 1479 C CA . ASP A 1 191 ? 9.401 3.675 -0.972 1.00 37.69 ? 191 ASP A CA 1 ATOM 1480 C C . ASP A 1 191 ? 7.934 3.726 -0.535 1.00 35.03 ? 191 ASP A C 1 ATOM 1481 O O . ASP A 1 191 ? 7.107 4.315 -1.239 1.00 39.26 ? 191 ASP A O 1 ATOM 1482 C CB . ASP A 1 191 ? 9.734 2.307 -1.611 1.00 39.94 ? 191 ASP A CB 1 ATOM 1483 C CG . ASP A 1 191 ? 11.009 2.356 -2.469 1.00 43.72 ? 191 ASP A CG 1 ATOM 1484 O OD1 . ASP A 1 191 ? 12.113 2.529 -1.910 1.00 45.74 ? 191 ASP A OD1 1 ATOM 1485 O OD2 . ASP A 1 191 ? 10.911 2.229 -3.711 1.00 50.69 ? 191 ASP A OD2 1 ATOM 1486 N N . GLN A 1 192 ? 7.615 3.102 0.598 1.00 30.80 ? 192 GLN A N 1 ATOM 1487 C CA . GLN A 1 192 ? 6.262 3.149 1.166 1.00 30.47 ? 192 GLN A CA 1 ATOM 1488 C C . GLN A 1 192 ? 5.801 4.586 1.424 1.00 29.30 ? 192 GLN A C 1 ATOM 1489 O O . GLN A 1 192 ? 4.654 4.926 1.158 1.00 26.01 ? 192 GLN A O 1 ATOM 1490 C CB . GLN A 1 192 ? 6.203 2.368 2.484 1.00 32.80 ? 192 GLN A CB 1 ATOM 1491 C CG . GLN A 1 192 ? 6.273 0.860 2.285 1.00 31.65 ? 192 GLN A CG 1 ATOM 1492 C CD . GLN A 1 192 ? 6.453 0.102 3.570 1.00 34.14 ? 192 GLN A CD 1 ATOM 1493 O OE1 . GLN A 1 192 ? 5.498 -0.119 4.322 1.00 36.19 ? 192 GLN A OE1 1 ATOM 1494 N NE2 . GLN A 1 192 ? 7.684 -0.320 3.829 1.00 35.19 ? 192 GLN A NE2 1 ATOM 1495 N N . VAL A 1 193 ? 6.713 5.420 1.921 1.00 28.34 ? 193 VAL A N 1 ATOM 1496 C CA . VAL A 1 193 ? 6.405 6.797 2.280 1.00 28.18 ? 193 VAL A CA 1 ATOM 1497 C C . VAL A 1 193 ? 5.921 7.589 1.072 1.00 30.58 ? 193 VAL A C 1 ATOM 1498 O O . VAL A 1 193 ? 4.920 8.307 1.177 1.00 30.04 ? 193 VAL A O 1 ATOM 1499 C CB . VAL A 1 193 ? 7.608 7.515 2.913 1.00 27.93 ? 193 VAL A CB 1 ATOM 1500 C CG1 . VAL A 1 193 ? 7.351 8.999 3.026 1.00 28.65 ? 193 VAL A CG1 1 ATOM 1501 C CG2 . VAL A 1 193 ? 7.943 6.923 4.285 1.00 27.67 ? 193 VAL A CG2 1 ATOM 1502 N N . LYS A 1 194 ? 6.614 7.462 -0.065 1.00 31.00 ? 194 LYS A N 1 ATOM 1503 C CA . LYS A 1 194 ? 6.166 8.106 -1.301 1.00 31.33 ? 194 LYS A CA 1 ATOM 1504 C C . LYS A 1 194 ? 4.690 7.766 -1.622 1.00 27.67 ? 194 LYS A C 1 ATOM 1505 O O . LYS A 1 194 ? 3.901 8.649 -1.986 1.00 27.35 ? 194 LYS A O 1 ATOM 1506 C CB . LYS A 1 194 ? 7.067 7.729 -2.482 1.00 36.23 ? 194 LYS A CB 1 ATOM 1507 C CG . LYS A 1 194 ? 8.549 8.055 -2.301 1.00 42.14 ? 194 LYS A CG 1 ATOM 1508 C CD . LYS A 1 194 ? 9.230 8.388 -3.637 1.00 47.34 ? 194 LYS A CD 1 ATOM 1509 C CE . LYS A 1 194 ? 10.752 8.249 -3.590 1.00 50.42 ? 194 LYS A CE 1 ATOM 1510 N NZ . LYS A 1 194 ? 11.199 6.821 -3.632 1.00 52.67 ? 194 LYS A NZ 1 ATOM 1511 N N . ARG A 1 195 ? 4.324 6.503 -1.467 1.00 24.91 ? 195 ARG A N 1 ATOM 1512 C CA . ARG A 1 195 ? 2.945 6.051 -1.671 1.00 25.65 ? 195 ARG A CA 1 ATOM 1513 C C . ARG A 1 195 ? 1.981 6.584 -0.608 1.00 24.13 ? 195 ARG A C 1 ATOM 1514 O O . ARG A 1 195 ? 0.810 6.934 -0.893 1.00 22.26 ? 195 ARG A O 1 ATOM 1515 C CB . ARG A 1 195 ? 2.879 4.531 -1.668 1.00 26.08 ? 195 ARG A CB 1 ATOM 1516 C CG . ARG A 1 195 ? 3.737 3.878 -2.747 1.00 28.78 ? 195 ARG A CG 1 ATOM 1517 C CD . ARG A 1 195 ? 3.258 2.476 -3.095 1.00 28.49 ? 195 ARG A CD 1 ATOM 1518 N NE . ARG A 1 195 ? 3.452 1.526 -2.005 1.00 29.83 ? 195 ARG A NE 1 ATOM 1519 C CZ . ARG A 1 195 ? 4.609 0.935 -1.703 1.00 33.39 ? 195 ARG A CZ 1 ATOM 1520 N NH1 . ARG A 1 195 ? 5.717 1.206 -2.395 1.00 34.86 ? 195 ARG A NH1 1 ATOM 1521 N NH2 . ARG A 1 195 ? 4.669 0.073 -0.687 1.00 34.97 ? 195 ARG A NH2 1 ATOM 1522 N N . TRP A 1 196 ? 2.458 6.626 0.622 1.00 22.35 ? 196 TRP A N 1 ATOM 1523 C CA . TRP A 1 196 ? 1.624 7.123 1.697 1.00 23.47 ? 196 TRP A CA 1 ATOM 1524 C C . TRP A 1 196 ? 1.243 8.572 1.384 1.00 22.88 ? 196 TRP A C 1 ATOM 1525 O O . TRP A 1 196 ? 0.094 8.969 1.575 1.00 23.34 ? 196 TRP A O 1 ATOM 1526 C CB . TRP A 1 196 ? 2.336 7.051 3.041 1.00 22.32 ? 196 TRP A CB 1 ATOM 1527 C CG . TRP A 1 196 ? 2.686 5.692 3.490 1.00 20.29 ? 196 TRP A CG 1 ATOM 1528 C CD1 . TRP A 1 196 ? 2.206 4.504 3.011 1.00 19.79 ? 196 TRP A CD1 1 ATOM 1529 C CD2 . TRP A 1 196 ? 3.564 5.360 4.578 1.00 19.71 ? 196 TRP A CD2 1 ATOM 1530 N NE1 . TRP A 1 196 ? 2.739 3.459 3.717 1.00 18.72 ? 196 TRP A NE1 1 ATOM 1531 C CE2 . TRP A 1 196 ? 3.580 3.953 4.685 1.00 19.12 ? 196 TRP A CE2 1 ATOM 1532 C CE3 . TRP A 1 196 ? 4.340 6.116 5.465 1.00 19.63 ? 196 TRP A CE3 1 ATOM 1533 C CZ2 . TRP A 1 196 ? 4.357 3.279 5.636 1.00 19.60 ? 196 TRP A CZ2 1 ATOM 1534 C CZ3 . TRP A 1 196 ? 5.127 5.430 6.414 1.00 20.38 ? 196 TRP A CZ3 1 ATOM 1535 C CH2 . TRP A 1 196 ? 5.117 4.021 6.484 1.00 19.21 ? 196 TRP A CH2 1 ATOM 1536 N N . GLU A 1 197 ? 2.188 9.322 0.836 1.00 23.26 ? 197 GLU A N 1 ATOM 1537 C CA . GLU A 1 197 ? 1.977 10.741 0.550 1.00 26.48 ? 197 GLU A CA 1 ATOM 1538 C C . GLU A 1 197 ? 1.140 10.989 -0.700 1.00 27.89 ? 197 GLU A C 1 ATOM 1539 O O . GLU A 1 197 ? 0.708 12.102 -0.912 1.00 29.57 ? 197 GLU A O 1 ATOM 1540 C CB . GLU A 1 197 ? 3.319 11.437 0.317 1.00 26.76 ? 197 GLU A CB 1 ATOM 1541 C CG . GLU A 1 197 ? 4.244 11.482 1.517 1.00 27.76 ? 197 GLU A CG 1 ATOM 1542 C CD . GLU A 1 197 ? 5.613 12.004 1.154 1.00 27.60 ? 197 GLU A CD 1 ATOM 1543 O OE1 . GLU A 1 197 ? 6.008 11.840 -0.013 1.00 31.77 ? 197 GLU A OE1 1 ATOM 1544 O OE2 . GLU A 1 197 ? 6.300 12.574 2.017 1.00 28.01 ? 197 GLU A OE2 1 ATOM 1545 N N . THR A 1 198 ? 0.945 9.985 -1.556 1.00 27.11 ? 198 THR A N 1 ATOM 1546 C CA . THR A 1 198 ? 0.256 10.222 -2.818 1.00 29.13 ? 198 THR A CA 1 ATOM 1547 C C . THR A 1 198 ? -1.259 10.355 -2.652 1.00 28.63 ? 198 THR A C 1 ATOM 1548 O O . THR A 1 198 ? -1.878 9.536 -1.975 1.00 26.54 ? 198 THR A O 1 ATOM 1549 C CB . THR A 1 198 ? 0.504 9.102 -3.830 1.00 30.49 ? 198 THR A CB 1 ATOM 1550 O OG1 . THR A 1 198 ? 1.908 8.881 -3.967 1.00 33.96 ? 198 THR A OG1 1 ATOM 1551 C CG2 . THR A 1 198 ? -0.074 9.499 -5.181 1.00 33.36 ? 198 THR A CG2 1 ATOM 1552 N N . CYS A 1 199 ? -1.828 11.386 -3.281 1.00 28.72 ? 199 CYS A N 1 ATOM 1553 C CA . CYS A 1 199 ? -3.265 11.636 -3.290 1.00 30.83 ? 199 CYS A CA 1 ATOM 1554 C C . CYS A 1 199 ? -3.624 12.531 -4.473 1.00 33.49 ? 199 CYS A C 1 ATOM 1555 O O . CYS A 1 199 ? -3.048 13.594 -4.641 1.00 32.41 ? 199 CYS A O 1 ATOM 1556 C CB . CYS A 1 199 ? -3.716 12.305 -1.985 1.00 30.90 ? 199 CYS A CB 1 ATOM 1557 S SG . CYS A 1 199 ? -5.497 12.654 -1.868 1.00 30.92 ? 199 CYS A SG 1 ATOM 1558 N N . THR A 1 200 ? -4.599 12.077 -5.260 1.00 37.88 ? 200 THR A N 1 ATOM 1559 C CA . THR A 1 200 ? -5.043 12.717 -6.496 1.00 40.81 ? 200 THR A CA 1 ATOM 1560 C C . THR A 1 200 ? -6.255 13.649 -6.351 1.00 43.83 ? 200 THR A C 1 ATOM 1561 O O . THR A 1 200 ? -6.677 14.248 -7.339 1.00 47.46 ? 200 THR A O 1 ATOM 1562 C CB . THR A 1 200 ? -5.475 11.638 -7.500 1.00 40.66 ? 200 THR A CB 1 ATOM 1563 O OG1 . THR A 1 200 ? -6.497 10.828 -6.905 1.00 41.91 ? 200 THR A OG1 1 ATOM 1564 C CG2 . THR A 1 200 ? -4.299 10.764 -7.895 1.00 39.96 ? 200 THR A CG2 1 ATOM 1565 N N . LYS A 1 201 ? -6.845 13.739 -5.155 1.00 45.73 ? 201 LYS A N 1 ATOM 1566 C CA . LYS A 1 201 ? -7.870 14.766 -4.884 1.00 44.20 ? 201 LYS A CA 1 ATOM 1567 C C . LYS A 1 201 ? -7.199 16.110 -4.707 1.00 42.47 ? 201 LYS A C 1 ATOM 1568 O O . LYS A 1 201 ? -6.118 16.173 -4.131 1.00 42.72 ? 201 LYS A O 1 ATOM 1569 C CB . LYS A 1 201 ? -8.707 14.442 -3.645 1.00 43.31 ? 201 LYS A CB 1 ATOM 1570 C CG . LYS A 1 201 ? -9.918 13.595 -3.944 1.00 44.32 ? 201 LYS A CG 1 ATOM 1571 C CD . LYS A 1 201 ? -9.567 12.128 -4.054 1.00 45.46 ? 201 LYS A CD 1 ATOM 1572 C CE . LYS A 1 201 ? -10.168 11.340 -2.900 1.00 44.29 ? 201 LYS A CE 1 ATOM 1573 N NZ . LYS A 1 201 ? -11.638 11.198 -3.057 1.00 43.06 ? 201 LYS A NZ 1 ATOM 1574 N N . THR A 1 203 ? -7.134 16.547 -2.215 1.00 39.37 ? 203 THR A N 1 ATOM 1575 C CA . THR A 1 203 ? -6.271 17.299 -1.328 1.00 36.20 ? 203 THR A CA 1 ATOM 1576 C C . THR A 1 203 ? -5.991 16.439 -0.103 1.00 32.63 ? 203 THR A C 1 ATOM 1577 O O . THR A 1 203 ? -4.872 16.419 0.399 1.00 33.60 ? 203 THR A O 1 ATOM 1578 C CB . THR A 1 203 ? -6.909 18.650 -0.993 1.00 39.77 ? 203 THR A CB 1 ATOM 1579 O OG1 . THR A 1 203 ? -6.676 19.553 -2.089 1.00 36.32 ? 203 THR A OG1 1 ATOM 1580 C CG2 . THR A 1 203 ? -6.323 19.231 0.289 1.00 42.09 ? 203 THR A CG2 1 ATOM 1581 N N . ALA A 1 204 ? -6.993 15.681 0.334 1.00 28.43 ? 204 ALA A N 1 ATOM 1582 C CA . ALA A 1 204 ? -6.761 14.576 1.248 1.00 27.71 ? 204 ALA A CA 1 ATOM 1583 C C . ALA A 1 204 ? -7.437 13.319 0.746 1.00 25.41 ? 204 ALA A C 1 ATOM 1584 O O . ALA A 1 204 ? -8.431 13.373 0.013 1.00 23.34 ? 204 ALA A O 1 ATOM 1585 C CB . ALA A 1 204 ? -7.247 14.924 2.643 1.00 28.80 ? 204 ALA A CB 1 ATOM 1586 N N . CYS A 1 205 ? -6.907 12.185 1.181 1.00 25.67 ? 205 CYS A N 1 ATOM 1587 C CA . CYS A 1 205 ? -7.377 10.871 0.722 1.00 25.68 ? 205 CYS A CA 1 ATOM 1588 C C . CYS A 1 205 ? -7.828 9.965 1.891 1.00 23.57 ? 205 CYS A C 1 ATOM 1589 O O . CYS A 1 205 ? -7.344 8.847 2.059 1.00 23.00 ? 205 CYS A O 1 ATOM 1590 C CB . CYS A 1 205 ? -6.286 10.239 -0.152 1.00 27.64 ? 205 CYS A CB 1 ATOM 1591 S SG . CYS A 1 205 ? -6.367 10.797 -1.882 1.00 31.31 ? 205 CYS A SG 1 ATOM 1592 N N . PRO A 1 206 ? -8.798 10.452 2.697 1.00 21.90 ? 206 PRO A N 1 ATOM 1593 C CA . PRO A 1 206 ? -9.180 9.767 3.939 1.00 21.68 ? 206 PRO A CA 1 ATOM 1594 C C . PRO A 1 206 ? -9.720 8.354 3.780 1.00 20.24 ? 206 PRO A C 1 ATOM 1595 O O . PRO A 1 206 ? -9.443 7.509 4.646 1.00 18.33 ? 206 PRO A O 1 ATOM 1596 C CB . PRO A 1 206 ? -10.225 10.704 4.565 1.00 21.71 ? 206 PRO A CB 1 ATOM 1597 C CG . PRO A 1 206 ? -10.719 11.557 3.450 1.00 21.51 ? 206 PRO A CG 1 ATOM 1598 C CD . PRO A 1 206 ? -9.609 11.663 2.456 1.00 21.65 ? 206 PRO A CD 1 ATOM 1599 N N . ASP A 1 207 ? -10.455 8.067 2.706 1.00 20.11 ? 207 ASP A N 1 ATOM 1600 C CA . ASP A 1 207 ? -11.052 6.710 2.576 1.00 21.86 ? 207 ASP A CA 1 ATOM 1601 C C . ASP A 1 207 ? -9.984 5.625 2.422 1.00 21.02 ? 207 ASP A C 1 ATOM 1602 O O . ASP A 1 207 ? -10.206 4.453 2.802 1.00 21.46 ? 207 ASP A O 1 ATOM 1603 C CB . ASP A 1 207 ? -12.059 6.600 1.404 1.00 23.16 ? 207 ASP A CB 1 ATOM 1604 C CG . ASP A 1 207 ? -13.259 7.553 1.537 1.00 25.38 ? 207 ASP A CG 1 ATOM 1605 O OD1 . ASP A 1 207 ? -13.506 8.046 2.662 1.00 23.34 ? 207 ASP A OD1 1 ATOM 1606 O OD2 . ASP A 1 207 ? -13.957 7.787 0.492 1.00 28.00 ? 207 ASP A OD2 1 ATOM 1607 N N . ILE A 1 208 ? -8.840 6.009 1.856 1.00 22.08 ? 208 ILE A N 1 ATOM 1608 C CA . ILE A 1 208 ? -7.673 5.120 1.781 1.00 23.57 ? 208 ILE A CA 1 ATOM 1609 C C . ILE A 1 208 ? -7.190 4.752 3.185 1.00 21.09 ? 208 ILE A C 1 ATOM 1610 O O . ILE A 1 208 ? -6.882 3.594 3.502 1.00 20.54 ? 208 ILE A O 1 ATOM 1611 C CB . ILE A 1 208 ? -6.472 5.792 1.078 1.00 25.64 ? 208 ILE A CB 1 ATOM 1612 C CG1 . ILE A 1 208 ? -6.808 6.240 -0.362 1.00 27.62 ? 208 ILE A CG1 1 ATOM 1613 C CG2 . ILE A 1 208 ? -5.260 4.866 1.111 1.00 27.29 ? 208 ILE A CG2 1 ATOM 1614 C CD1 . ILE A 1 208 ? -7.442 5.168 -1.217 1.00 28.41 ? 208 ILE A CD1 1 ATOM 1615 N N . TYR A 1 209 ? -7.111 5.767 4.029 1.00 19.90 ? 209 TYR A N 1 ATOM 1616 C CA . TYR A 1 209 ? -6.585 5.595 5.369 1.00 17.87 ? 209 TYR A CA 1 ATOM 1617 C C . TYR A 1 209 ? -7.588 4.810 6.194 1.00 17.47 ? 209 TYR A C 1 ATOM 1618 O O . TYR A 1 209 ? -7.180 3.933 6.958 1.00 17.18 ? 209 TYR A O 1 ATOM 1619 C CB . TYR A 1 209 ? -6.278 6.940 5.994 1.00 18.52 ? 209 TYR A CB 1 ATOM 1620 C CG . TYR A 1 209 ? -5.576 7.914 5.066 1.00 18.83 ? 209 TYR A CG 1 ATOM 1621 C CD1 . TYR A 1 209 ? -4.746 7.471 4.031 1.00 18.65 ? 209 TYR A CD1 1 ATOM 1622 C CD2 . TYR A 1 209 ? -5.723 9.273 5.248 1.00 18.02 ? 209 TYR A CD2 1 ATOM 1623 C CE1 . TYR A 1 209 ? -4.136 8.372 3.179 1.00 19.54 ? 209 TYR A CE1 1 ATOM 1624 C CE2 . TYR A 1 209 ? -5.099 10.178 4.428 1.00 18.40 ? 209 TYR A CE2 1 ATOM 1625 C CZ . TYR A 1 209 ? -4.303 9.739 3.410 1.00 19.74 ? 209 TYR A CZ 1 ATOM 1626 O OH . TYR A 1 209 ? -3.693 10.665 2.604 1.00 21.69 ? 209 TYR A OH 1 ATOM 1627 N N . ALA A 1 210 ? -8.890 5.074 6.006 1.00 17.00 ? 210 ALA A N 1 ATOM 1628 C CA . ALA A 1 210 ? -9.940 4.309 6.721 1.00 18.48 ? 210 ALA A CA 1 ATOM 1629 C C . ALA A 1 210 ? -9.937 2.837 6.314 1.00 18.99 ? 210 ALA A C 1 ATOM 1630 O O . ALA A 1 210 ? -10.119 1.941 7.148 1.00 22.08 ? 210 ALA A O 1 ATOM 1631 C CB . ALA A 1 210 ? -11.325 4.876 6.427 1.00 19.06 ? 210 ALA A CB 1 ATOM 1632 N N . SER A 1 211 ? -9.787 2.576 5.033 1.00 18.80 ? 211 SER A N 1 ATOM 1633 C CA . SER A 1 211 ? -9.818 1.174 4.575 1.00 20.51 ? 211 SER A CA 1 ATOM 1634 C C . SER A 1 211 ? -8.661 0.410 5.150 1.00 20.04 ? 211 SER A C 1 ATOM 1635 O O . SER A 1 211 ? -8.802 -0.747 5.546 1.00 21.78 ? 211 SER A O 1 ATOM 1636 C CB . SER A 1 211 ? -9.814 1.095 3.045 1.00 20.26 ? 211 SER A CB 1 ATOM 1637 O OG . SER A 1 211 ? -11.042 1.616 2.574 1.00 20.79 ? 211 SER A OG 1 ATOM 1638 N N . GLU A 1 212 ? -7.522 1.078 5.236 1.00 21.26 ? 212 GLU A N 1 ATOM 1639 C CA . GLU A 1 212 ? -6.327 0.498 5.823 1.00 20.97 ? 212 GLU A CA 1 ATOM 1640 C C . GLU A 1 212 ? -6.600 0.179 7.279 1.00 20.70 ? 212 GLU A C 1 ATOM 1641 O O . GLU A 1 212 ? -6.234 -0.872 7.780 1.00 19.31 ? 212 GLU A O 1 ATOM 1642 C CB . GLU A 1 212 ? -5.167 1.493 5.727 1.00 22.72 ? 212 GLU A CB 1 ATOM 1643 C CG . GLU A 1 212 ? -4.493 1.591 4.362 1.00 23.91 ? 212 GLU A CG 1 ATOM 1644 C CD . GLU A 1 212 ? -3.575 2.807 4.241 1.00 23.96 ? 212 GLU A CD 1 ATOM 1645 O OE1 . GLU A 1 212 ? -3.353 3.495 5.227 1.00 22.20 ? 212 GLU A OE1 1 ATOM 1646 O OE2 . GLU A 1 212 ? -3.099 3.120 3.142 1.00 26.30 ? 212 GLU A OE2 1 ATOM 1647 N N . GLY A 1 213 ? -7.253 1.108 7.960 1.00 21.21 ? 213 GLY A N 1 ATOM 1648 C CA . GLY A 1 213 ? -7.472 0.982 9.393 1.00 21.62 ? 213 GLY A CA 1 ATOM 1649 C C . GLY A 1 213 ? -8.378 -0.164 9.779 1.00 20.86 ? 213 GLY A C 1 ATOM 1650 O O . GLY A 1 213 ? -8.092 -0.888 10.750 1.00 19.89 ? 213 GLY A O 1 ATOM 1651 N N . ILE A 1 214 ? -9.468 -0.338 9.029 1.00 21.63 ? 214 ILE A N 1 ATOM 1652 C CA . ILE A 1 214 ? -10.404 -1.442 9.297 1.00 23.17 ? 214 ILE A CA 1 ATOM 1653 C C . ILE A 1 214 ? -9.703 -2.771 9.082 1.00 22.80 ? 214 ILE A C 1 ATOM 1654 O O . ILE A 1 214 ? -9.874 -3.678 9.874 1.00 22.02 ? 214 ILE A O 1 ATOM 1655 C CB . ILE A 1 214 ? -11.727 -1.339 8.484 1.00 23.98 ? 214 ILE A CB 1 ATOM 1656 C CG1 . ILE A 1 214 ? -12.736 -2.405 8.922 1.00 25.53 ? 214 ILE A CG1 1 ATOM 1657 C CG2 . ILE A 1 214 ? -11.507 -1.464 6.983 1.00 24.38 ? 214 ILE A CG2 1 ATOM 1658 C CD1 . ILE A 1 214 ? -13.531 -2.011 10.129 1.00 25.76 ? 214 ILE A CD1 1 ATOM 1659 N N . GLN A 1 215 ? -8.892 -2.850 8.032 1.00 25.39 ? 215 GLN A N 1 ATOM 1660 C CA . GLN A 1 215 ? -8.067 -4.027 7.736 1.00 28.62 ? 215 GLN A CA 1 ATOM 1661 C C . GLN A 1 215 ? -7.149 -4.339 8.918 1.00 28.53 ? 215 GLN A C 1 ATOM 1662 O O . GLN A 1 215 ? -6.981 -5.504 9.288 1.00 25.24 ? 215 GLN A O 1 ATOM 1663 C CB . GLN A 1 215 ? -7.201 -3.766 6.483 1.00 33.55 ? 215 GLN A CB 1 ATOM 1664 C CG . GLN A 1 215 ? -6.495 -4.980 5.876 1.00 38.78 ? 215 GLN A CG 1 ATOM 1665 C CD . GLN A 1 215 ? -5.337 -4.618 4.925 1.00 45.09 ? 215 GLN A CD 1 ATOM 1666 O OE1 . GLN A 1 215 ? -4.948 -3.446 4.780 1.00 48.11 ? 215 GLN A OE1 1 ATOM 1667 N NE2 . GLN A 1 215 ? -4.767 -5.641 4.280 1.00 48.39 ? 215 GLN A NE2 1 ATOM 1668 N N . ALA A 1 216 ? -6.554 -3.291 9.508 1.00 26.92 ? 216 ALA A N 1 ATOM 1669 C CA . ALA A 1 216 ? -5.615 -3.497 10.601 1.00 27.68 ? 216 ALA A CA 1 ATOM 1670 C C . ALA A 1 216 ? -6.351 -3.776 11.921 1.00 27.33 ? 216 ALA A C 1 ATOM 1671 O O . ALA A 1 216 ? -5.880 -4.561 12.734 1.00 27.32 ? 216 ALA A O 1 ATOM 1672 C CB . ALA A 1 216 ? -4.644 -2.324 10.736 1.00 27.21 ? 216 ALA A CB 1 ATOM 1673 N N . ALA A 1 217 ? -7.512 -3.156 12.132 1.00 27.37 ? 217 ALA A N 1 ATOM 1674 C CA . ALA A 1 217 ? -8.347 -3.509 13.293 1.00 26.38 ? 217 ALA A CA 1 ATOM 1675 C C . ALA A 1 217 ? -8.588 -5.022 13.332 1.00 26.40 ? 217 ALA A C 1 ATOM 1676 O O . ALA A 1 217 ? -8.345 -5.652 14.354 1.00 24.69 ? 217 ALA A O 1 ATOM 1677 C CB . ALA A 1 217 ? -9.685 -2.778 13.254 1.00 26.83 ? 217 ALA A CB 1 ATOM 1678 N N . CYS A 1 218 ? -9.069 -5.572 12.210 1.00 28.87 ? 218 CYS A N 1 ATOM 1679 C CA . CYS A 1 218 ? -9.346 -7.020 12.050 1.00 29.75 ? 218 CYS A CA 1 ATOM 1680 C C . CYS A 1 218 ? -8.101 -7.895 12.056 1.00 28.55 ? 218 CYS A C 1 ATOM 1681 O O . CYS A 1 218 ? -8.069 -8.915 12.733 1.00 29.67 ? 218 CYS A O 1 ATOM 1682 C CB . CYS A 1 218 ? -10.088 -7.316 10.731 1.00 31.91 ? 218 CYS A CB 1 ATOM 1683 S SG . CYS A 1 218 ? -11.786 -6.718 10.504 1.00 30.75 ? 218 CYS A SG 1 ATOM 1684 N N . ASP A 1 219 ? -7.091 -7.538 11.272 1.00 27.80 ? 219 ASP A N 1 ATOM 1685 C CA . ASP A 1 219 ? -5.889 -8.372 11.205 1.00 27.37 ? 219 ASP A CA 1 ATOM 1686 C C . ASP A 1 219 ? -5.054 -8.377 12.481 1.00 26.34 ? 219 ASP A C 1 ATOM 1687 O O . ASP A 1 219 ? -4.351 -9.361 12.745 1.00 24.02 ? 219 ASP A O 1 ATOM 1688 C CB . ASP A 1 219 ? -4.969 -7.946 10.063 1.00 29.20 ? 219 ASP A CB 1 ATOM 1689 C CG . ASP A 1 219 ? -5.539 -8.244 8.696 1.00 28.74 ? 219 ASP A CG 1 ATOM 1690 O OD1 . ASP A 1 219 ? -6.495 -9.045 8.579 1.00 25.54 ? 219 ASP A OD1 1 ATOM 1691 O OD2 . ASP A 1 219 ? -4.994 -7.653 7.738 1.00 30.20 ? 219 ASP A OD2 1 ATOM 1692 N N . TRP A 1 220 ? -5.114 -7.297 13.261 1.00 23.59 ? 220 TRP A N 1 ATOM 1693 C CA . TRP A 1 220 ? -4.140 -7.107 14.347 1.00 23.23 ? 220 TRP A CA 1 ATOM 1694 C C . TRP A 1 220 ? -4.765 -6.720 15.692 1.00 21.88 ? 220 TRP A C 1 ATOM 1695 O O . TRP A 1 220 ? -4.366 -7.232 16.723 1.00 20.95 ? 220 TRP A O 1 ATOM 1696 C CB . TRP A 1 220 ? -3.086 -6.057 13.938 1.00 23.86 ? 220 TRP A CB 1 ATOM 1697 C CG . TRP A 1 220 ? -2.168 -6.516 12.819 1.00 24.09 ? 220 TRP A CG 1 ATOM 1698 C CD1 . TRP A 1 220 ? -2.180 -6.094 11.519 1.00 26.63 ? 220 TRP A CD1 1 ATOM 1699 C CD2 . TRP A 1 220 ? -1.121 -7.475 12.916 1.00 25.36 ? 220 TRP A CD2 1 ATOM 1700 N NE1 . TRP A 1 220 ? -1.218 -6.742 10.797 1.00 25.50 ? 220 TRP A NE1 1 ATOM 1701 C CE2 . TRP A 1 220 ? -0.548 -7.598 11.630 1.00 26.84 ? 220 TRP A CE2 1 ATOM 1702 C CE3 . TRP A 1 220 ? -0.610 -8.253 13.967 1.00 26.18 ? 220 TRP A CE3 1 ATOM 1703 C CZ2 . TRP A 1 220 ? 0.518 -8.458 11.365 1.00 27.11 ? 220 TRP A CZ2 1 ATOM 1704 C CZ3 . TRP A 1 220 ? 0.459 -9.114 13.707 1.00 27.22 ? 220 TRP A CZ3 1 ATOM 1705 C CH2 . TRP A 1 220 ? 1.001 -9.216 12.412 1.00 27.57 ? 220 TRP A CH2 1 ATOM 1706 N N . ALA A 1 221 ? -5.750 -5.837 15.703 1.00 21.32 ? 221 ALA A N 1 ATOM 1707 C CA . ALA A 1 221 ? -6.257 -5.351 16.990 1.00 21.53 ? 221 ALA A CA 1 ATOM 1708 C C . ALA A 1 221 ? -7.195 -6.365 17.632 1.00 22.19 ? 221 ALA A C 1 ATOM 1709 O O . ALA A 1 221 ? -6.953 -6.827 18.771 1.00 21.42 ? 221 ALA A O 1 ATOM 1710 C CB . ALA A 1 221 ? -6.938 -3.998 16.837 1.00 21.82 ? 221 ALA A CB 1 ATOM 1711 N N . TYR A 1 222 ? -8.240 -6.712 16.883 1.00 23.06 ? 222 TYR A N 1 ATOM 1712 C CA . TYR A 1 222 ? -9.246 -7.686 17.315 1.00 24.75 ? 222 TYR A CA 1 ATOM 1713 C C . TYR A 1 222 ? -8.720 -9.095 17.340 1.00 24.77 ? 222 TYR A C 1 ATOM 1714 O O . TYR A 1 222 ? -9.192 -9.903 18.125 1.00 26.45 ? 222 TYR A O 1 ATOM 1715 C CB . TYR A 1 222 ? -10.435 -7.687 16.364 1.00 24.30 ? 222 TYR A CB 1 ATOM 1716 C CG . TYR A 1 222 ? -11.334 -6.501 16.452 1.00 23.36 ? 222 TYR A CG 1 ATOM 1717 C CD1 . TYR A 1 222 ? -11.841 -6.099 17.666 1.00 23.91 ? 222 TYR A CD1 1 ATOM 1718 C CD2 . TYR A 1 222 ? -11.732 -5.819 15.305 1.00 23.33 ? 222 TYR A CD2 1 ATOM 1719 C CE1 . TYR A 1 222 ? -12.697 -5.023 17.765 1.00 23.05 ? 222 TYR A CE1 1 ATOM 1720 C CE2 . TYR A 1 222 ? -12.580 -4.732 15.386 1.00 24.09 ? 222 TYR A CE2 1 ATOM 1721 C CZ . TYR A 1 222 ? -13.083 -4.349 16.619 1.00 24.17 ? 222 TYR A CZ 1 ATOM 1722 O OH . TYR A 1 222 ? -13.939 -3.261 16.726 1.00 22.72 ? 222 TYR A OH 1 ATOM 1723 N N . LYS A 1 223 ? -7.760 -9.372 16.464 1.00 27.63 ? 223 LYS A N 1 ATOM 1724 C CA . LYS A 1 223 ? -7.270 -10.727 16.170 1.00 29.29 ? 223 LYS A CA 1 ATOM 1725 C C . LYS A 1 223 ? -6.782 -11.411 17.436 1.00 29.50 ? 223 LYS A C 1 ATOM 1726 O O . LYS A 1 223 ? -6.041 -10.815 18.223 1.00 29.06 ? 223 LYS A O 1 ATOM 1727 C CB . LYS A 1 223 ? -6.154 -10.664 15.100 1.00 32.21 ? 223 LYS A CB 1 ATOM 1728 C CG . LYS A 1 223 ? -5.515 -11.994 14.684 1.00 34.87 ? 223 LYS A CG 1 ATOM 1729 C CD . LYS A 1 223 ? -6.410 -12.807 13.756 1.00 38.38 ? 223 LYS A CD 1 ATOM 1730 C CE . LYS A 1 223 ? -5.992 -12.690 12.294 1.00 41.39 ? 223 LYS A CE 1 ATOM 1731 N NZ . LYS A 1 223 ? -7.154 -12.381 11.419 1.00 45.40 ? 223 LYS A NZ 1 ATOM 1732 N N . GLY A 1 224 ? -7.239 -12.650 17.646 1.00 31.16 ? 224 GLY A N 1 ATOM 1733 C CA . GLY A 1 224 ? -6.837 -13.467 18.804 1.00 31.06 ? 224 GLY A CA 1 ATOM 1734 C C . GLY A 1 224 ? -7.457 -13.098 20.147 1.00 32.37 ? 224 GLY A C 1 ATOM 1735 O O . GLY A 1 224 ? -7.449 -13.910 21.061 1.00 34.29 ? 224 GLY A O 1 ATOM 1736 N N . VAL A 1 225 ? -8.043 -11.901 20.244 1.00 29.67 ? 225 VAL A N 1 ATOM 1737 C CA . VAL A 1 225 ? -8.464 -11.321 21.503 1.00 27.89 ? 225 VAL A CA 1 ATOM 1738 C C . VAL A 1 225 ? -9.908 -11.702 21.888 1.00 28.44 ? 225 VAL A C 1 ATOM 1739 O O . VAL A 1 225 ? -10.840 -11.533 21.102 1.00 23.96 ? 225 VAL A O 1 ATOM 1740 C CB . VAL A 1 225 ? -8.414 -9.782 21.424 1.00 27.69 ? 225 VAL A CB 1 ATOM 1741 C CG1 . VAL A 1 225 ? -8.841 -9.175 22.747 1.00 28.23 ? 225 VAL A CG1 1 ATOM 1742 C CG2 . VAL A 1 225 ? -7.028 -9.291 21.021 1.00 28.17 ? 225 VAL A CG2 1 ATOM 1743 N N . THR A 1 226 ? -10.068 -12.180 23.121 1.00 28.77 ? 226 THR A N 1 ATOM 1744 C CA . THR A 1 226 ? -11.368 -12.519 23.698 1.00 30.21 ? 226 THR A CA 1 ATOM 1745 C C . THR A 1 226 ? -11.544 -11.716 24.985 1.00 30.63 ? 226 THR A C 1 ATOM 1746 O O . THR A 1 226 ? -10.572 -11.523 25.734 1.00 30.89 ? 226 THR A O 1 ATOM 1747 C CB . THR A 1 226 ? -11.453 -14.026 24.072 1.00 30.41 ? 226 THR A CB 1 ATOM 1748 O OG1 . THR A 1 226 ? -11.264 -14.853 22.914 1.00 29.10 ? 226 THR A OG1 1 ATOM 1749 C CG2 . THR A 1 226 ? -12.818 -14.368 24.721 1.00 32.23 ? 226 THR A CG2 1 ATOM 1750 N N . GLU A 1 227 ? -12.769 -11.275 25.254 1.00 29.80 ? 227 GLU A N 1 ATOM 1751 C CA . GLU A 1 227 ? -13.109 -10.641 26.534 1.00 34.45 ? 227 GLU A CA 1 ATOM 1752 C C . GLU A 1 227 ? -12.495 -11.423 27.701 1.00 32.54 ? 227 GLU A C 1 ATOM 1753 O O . GLU A 1 227 ? -12.668 -12.638 27.792 1.00 33.64 ? 227 GLU A O 1 ATOM 1754 C CB . GLU A 1 227 ? -14.636 -10.554 26.702 1.00 37.32 ? 227 GLU A CB 1 ATOM 1755 C CG . GLU A 1 227 ? -15.106 -10.248 28.124 1.00 40.13 ? 227 GLU A CG 1 ATOM 1756 C CD . GLU A 1 227 ? -15.280 -8.760 28.415 1.00 44.29 ? 227 GLU A CD 1 ATOM 1757 O OE1 . GLU A 1 227 ? -15.383 -7.964 27.456 1.00 44.49 ? 227 GLU A OE1 1 ATOM 1758 O OE2 . GLU A 1 227 ? -15.328 -8.389 29.620 1.00 46.98 ? 227 GLU A OE2 1 ATOM 1759 N N . GLY A 1 228 ? -11.762 -10.723 28.566 1.00 31.25 ? 228 GLY A N 1 ATOM 1760 C CA . GLY A 1 228 ? -11.139 -11.336 29.730 1.00 29.90 ? 228 GLY A CA 1 ATOM 1761 C C . GLY A 1 228 ? -9.680 -11.733 29.558 1.00 29.02 ? 228 GLY A C 1 ATOM 1762 O O . GLY A 1 228 ? -9.026 -12.092 30.537 1.00 30.35 ? 228 GLY A O 1 ATOM 1763 N N . ASP A 1 229 ? -9.143 -11.649 28.349 1.00 26.40 ? 229 ASP A N 1 ATOM 1764 C CA . ASP A 1 229 ? -7.750 -12.054 28.118 1.00 26.66 ? 229 ASP A CA 1 ATOM 1765 C C . ASP A 1 229 ? -6.789 -11.120 28.817 1.00 27.41 ? 229 ASP A C 1 ATOM 1766 O O . ASP A 1 229 ? -7.119 -9.973 29.110 1.00 30.03 ? 229 ASP A O 1 ATOM 1767 C CB . ASP A 1 229 ? -7.414 -12.026 26.638 1.00 27.39 ? 229 ASP A CB 1 ATOM 1768 C CG . ASP A 1 229 ? -7.988 -13.201 25.887 1.00 28.01 ? 229 ASP A CG 1 ATOM 1769 O OD1 . ASP A 1 229 ? -8.512 -14.108 26.548 1.00 27.83 ? 229 ASP A OD1 1 ATOM 1770 O OD2 . ASP A 1 229 ? -7.902 -13.203 24.637 1.00 29.96 ? 229 ASP A OD2 1 ATOM 1771 N N . THR A 1 230 ? -5.607 -11.622 29.101 1.00 27.94 ? 230 THR A N 1 ATOM 1772 C CA . THR A 1 230 ? -4.521 -10.791 29.574 1.00 27.77 ? 230 THR A CA 1 ATOM 1773 C C . THR A 1 230 ? -3.657 -10.617 28.356 1.00 27.94 ? 230 THR A C 1 ATOM 1774 O O . THR A 1 230 ? -3.235 -11.599 27.766 1.00 26.73 ? 230 THR A O 1 ATOM 1775 C CB . THR A 1 230 ? -3.751 -11.441 30.746 1.00 28.56 ? 230 THR A CB 1 ATOM 1776 O OG1 . THR A 1 230 ? -4.611 -11.510 31.883 1.00 29.31 ? 230 THR A OG1 1 ATOM 1777 C CG2 . THR A 1 230 ? -2.555 -10.600 31.152 1.00 29.36 ? 230 THR A CG2 1 ATOM 1778 N N . LEU A 1 231 ? -3.454 -9.373 27.929 1.00 25.96 ? 231 LEU A N 1 ATOM 1779 C CA . LEU A 1 231 ? -2.569 -9.121 26.814 1.00 25.92 ? 231 LEU A CA 1 ATOM 1780 C C . LEU A 1 231 ? -1.254 -8.705 27.431 1.00 25.32 ? 231 LEU A C 1 ATOM 1781 O O . LEU A 1 231 ? -1.216 -7.822 28.304 1.00 26.75 ? 231 LEU A O 1 ATOM 1782 C CB . LEU A 1 231 ? -3.136 -8.037 25.902 1.00 26.10 ? 231 LEU A CB 1 ATOM 1783 C CG . LEU A 1 231 ? -4.540 -8.327 25.363 1.00 25.65 ? 231 LEU A CG 1 ATOM 1784 C CD1 . LEU A 1 231 ? -4.952 -7.229 24.409 1.00 25.73 ? 231 LEU A CD1 1 ATOM 1785 C CD2 . LEU A 1 231 ? -4.596 -9.688 24.676 1.00 26.76 ? 231 LEU A CD2 1 ATOM 1786 N N . GLU A 1 232 ? -0.180 -9.348 27.000 1.00 24.46 ? 232 GLU A N 1 ATOM 1787 C CA . GLU A 1 232 ? 1.122 -9.128 27.599 1.00 25.80 ? 232 GLU A CA 1 ATOM 1788 C C . GLU A 1 232 ? 2.159 -9.055 26.518 1.00 23.83 ? 232 GLU A C 1 ATOM 1789 O O . GLU A 1 232 ? 1.868 -8.587 25.408 1.00 21.07 ? 232 GLU A O 1 ATOM 1790 C CB . GLU A 1 232 ? 1.467 -10.268 28.558 1.00 28.57 ? 232 GLU A CB 1 ATOM 1791 C CG . GLU A 1 232 ? 0.391 -10.668 29.520 1.00 30.53 ? 232 GLU A CG 1 ATOM 1792 C CD . GLU A 1 232 ? 0.898 -11.768 30.415 1.00 32.48 ? 232 GLU A CD 1 ATOM 1793 O OE1 . GLU A 1 232 ? 1.590 -11.441 31.388 1.00 29.58 ? 232 GLU A OE1 1 ATOM 1794 O OE2 . GLU A 1 232 ? 0.651 -12.951 30.096 1.00 33.08 ? 232 GLU A OE2 1 ATOM 1795 N N . ASP A 1 233 ? 3.381 -9.507 26.824 1.00 23.58 ? 233 ASP A N 1 ATOM 1796 C CA . ASP A 1 233 ? 4.486 -9.408 25.860 1.00 26.07 ? 233 ASP A CA 1 ATOM 1797 C C . ASP A 1 233 ? 4.126 -9.860 24.437 1.00 25.47 ? 233 ASP A C 1 ATOM 1798 O O . ASP A 1 233 ? 4.410 -9.152 23.487 1.00 24.92 ? 233 ASP A O 1 ATOM 1799 C CB . ASP A 1 233 ? 5.701 -10.200 26.334 1.00 26.58 ? 233 ASP A CB 1 ATOM 1800 C CG . ASP A 1 233 ? 6.514 -9.469 27.343 1.00 27.10 ? 233 ASP A CG 1 ATOM 1801 O OD1 . ASP A 1 233 ? 6.154 -8.336 27.721 1.00 29.48 ? 233 ASP A OD1 1 ATOM 1802 O OD2 . ASP A 1 233 ? 7.530 -10.039 27.769 1.00 29.24 ? 233 ASP A OD2 1 ATOM 1803 N N . GLU A 1 234 ? 3.523 -11.034 24.289 1.00 25.80 ? 234 GLU A N 1 ATOM 1804 C CA . GLU A 1 234 ? 3.297 -11.601 22.926 1.00 27.96 ? 234 GLU A CA 1 ATOM 1805 C C . GLU A 1 234 ? 2.463 -10.657 22.051 1.00 25.16 ? 234 GLU A C 1 ATOM 1806 O O . GLU A 1 234 ? 2.752 -10.423 20.862 1.00 26.18 ? 234 GLU A O 1 ATOM 1807 C CB . GLU A 1 234 ? 2.596 -12.965 22.978 1.00 30.32 ? 234 GLU A CB 1 ATOM 1808 C CG . GLU A 1 234 ? 2.390 -13.603 21.599 1.00 35.72 ? 234 GLU A CG 1 ATOM 1809 C CD . GLU A 1 234 ? 1.789 -15.021 21.622 1.00 40.15 ? 234 GLU A CD 1 ATOM 1810 O OE1 . GLU A 1 234 ? 1.206 -15.454 22.651 1.00 43.47 ? 234 GLU A OE1 1 ATOM 1811 O OE2 . GLU A 1 234 ? 1.893 -15.705 20.579 1.00 42.96 ? 234 GLU A OE2 1 ATOM 1812 N N . TYR A 1 235 ? 1.393 -10.167 22.632 1.00 23.69 ? 235 TYR A N 1 ATOM 1813 C CA . TYR A 1 235 ? 0.533 -9.241 21.931 1.00 22.97 ? 235 TYR A CA 1 ATOM 1814 C C . TYR A 1 235 ? 1.278 -7.918 21.723 1.00 21.69 ? 235 TYR A C 1 ATOM 1815 O O . TYR A 1 235 ? 1.342 -7.411 20.643 1.00 23.09 ? 235 TYR A O 1 ATOM 1816 C CB . TYR A 1 235 ? -0.730 -9.004 22.728 1.00 22.01 ? 235 TYR A CB 1 ATOM 1817 C CG . TYR A 1 235 ? -1.765 -8.273 21.936 1.00 21.11 ? 235 TYR A CG 1 ATOM 1818 C CD1 . TYR A 1 235 ? -1.802 -6.887 21.940 1.00 20.58 ? 235 TYR A CD1 1 ATOM 1819 C CD2 . TYR A 1 235 ? -2.702 -8.954 21.179 1.00 20.66 ? 235 TYR A CD2 1 ATOM 1820 C CE1 . TYR A 1 235 ? -2.748 -6.195 21.229 1.00 20.09 ? 235 TYR A CE1 1 ATOM 1821 C CE2 . TYR A 1 235 ? -3.658 -8.264 20.453 1.00 20.96 ? 235 TYR A CE2 1 ATOM 1822 C CZ . TYR A 1 235 ? -3.674 -6.871 20.504 1.00 21.09 ? 235 TYR A CZ 1 ATOM 1823 O OH . TYR A 1 235 ? -4.610 -6.138 19.810 1.00 22.71 ? 235 TYR A OH 1 ATOM 1824 N N . PHE A 1 236 ? 1.869 -7.399 22.775 1.00 22.19 ? 236 PHE A N 1 ATOM 1825 C CA . PHE A 1 236 ? 2.640 -6.167 22.689 1.00 22.59 ? 236 PHE A CA 1 ATOM 1826 C C . PHE A 1 236 ? 3.649 -6.185 21.522 1.00 22.67 ? 236 PHE A C 1 ATOM 1827 O O . PHE A 1 236 ? 3.663 -5.265 20.687 1.00 19.75 ? 236 PHE A O 1 ATOM 1828 C CB . PHE A 1 236 ? 3.333 -5.893 24.037 1.00 22.32 ? 236 PHE A CB 1 ATOM 1829 C CG . PHE A 1 236 ? 4.259 -4.726 24.004 1.00 22.29 ? 236 PHE A CG 1 ATOM 1830 C CD1 . PHE A 1 236 ? 3.783 -3.462 23.669 1.00 21.08 ? 236 PHE A CD1 1 ATOM 1831 C CD2 . PHE A 1 236 ? 5.621 -4.889 24.297 1.00 21.88 ? 236 PHE A CD2 1 ATOM 1832 C CE1 . PHE A 1 236 ? 4.660 -2.390 23.617 1.00 21.81 ? 236 PHE A CE1 1 ATOM 1833 C CE2 . PHE A 1 236 ? 6.483 -3.823 24.245 1.00 21.10 ? 236 PHE A CE2 1 ATOM 1834 C CZ . PHE A 1 236 ? 6.001 -2.569 23.911 1.00 20.82 ? 236 PHE A CZ 1 ATOM 1835 N N . TYR A 1 237 ? 4.474 -7.228 21.470 1.00 21.70 ? 237 TYR A N 1 ATOM 1836 C CA . TYR A 1 237 ? 5.547 -7.283 20.484 1.00 23.89 ? 237 TYR A CA 1 ATOM 1837 C C . TYR A 1 237 ? 5.059 -7.511 19.083 1.00 23.71 ? 237 TYR A C 1 ATOM 1838 O O . TYR A 1 237 ? 5.629 -6.962 18.147 1.00 23.57 ? 237 TYR A O 1 ATOM 1839 C CB . TYR A 1 237 ? 6.632 -8.322 20.856 1.00 24.46 ? 237 TYR A CB 1 ATOM 1840 C CG . TYR A 1 237 ? 7.506 -7.844 21.996 1.00 25.75 ? 237 TYR A CG 1 ATOM 1841 C CD1 . TYR A 1 237 ? 8.247 -6.670 21.878 1.00 26.12 ? 237 TYR A CD1 1 ATOM 1842 C CD2 . TYR A 1 237 ? 7.589 -8.562 23.191 1.00 27.50 ? 237 TYR A CD2 1 ATOM 1843 C CE1 . TYR A 1 237 ? 9.050 -6.220 22.920 1.00 28.26 ? 237 TYR A CE1 1 ATOM 1844 C CE2 . TYR A 1 237 ? 8.382 -8.116 24.247 1.00 28.81 ? 237 TYR A CE2 1 ATOM 1845 C CZ . TYR A 1 237 ? 9.104 -6.948 24.109 1.00 29.61 ? 237 TYR A CZ 1 ATOM 1846 O OH . TYR A 1 237 ? 9.893 -6.522 25.146 1.00 32.75 ? 237 TYR A OH 1 ATOM 1847 N N . SER A 1 238 ? 3.999 -8.299 18.922 1.00 23.48 ? 238 SER A N 1 ATOM 1848 C CA . SER A 1 238 ? 3.516 -8.570 17.594 1.00 23.45 ? 238 SER A CA 1 ATOM 1849 C C . SER A 1 238 ? 2.693 -7.394 17.056 1.00 22.96 ? 238 SER A C 1 ATOM 1850 O O . SER A 1 238 ? 2.604 -7.227 15.857 1.00 23.72 ? 238 SER A O 1 ATOM 1851 C CB . SER A 1 238 ? 2.731 -9.892 17.556 1.00 23.97 ? 238 SER A CB 1 ATOM 1852 O OG . SER A 1 238 ? 1.824 -9.993 18.630 1.00 24.75 ? 238 SER A OG 1 ATOM 1853 N N . ARG A 1 239 ? 2.135 -6.548 17.916 1.00 21.50 ? 239 ARG A N 1 ATOM 1854 C CA . ARG A 1 239 ? 1.295 -5.447 17.430 1.00 21.31 ? 239 ARG A CA 1 ATOM 1855 C C . ARG A 1 239 ? 2.013 -4.092 17.360 1.00 22.07 ? 239 ARG A C 1 ATOM 1856 O O . ARG A 1 239 ? 1.484 -3.141 16.798 1.00 21.19 ? 239 ARG A O 1 ATOM 1857 C CB . ARG A 1 239 ? 0.059 -5.295 18.302 1.00 20.89 ? 239 ARG A CB 1 ATOM 1858 C CG . ARG A 1 239 ? -1.141 -6.097 17.848 1.00 21.39 ? 239 ARG A CG 1 ATOM 1859 C CD . ARG A 1 239 ? -0.854 -7.584 17.753 1.00 22.11 ? 239 ARG A CD 1 ATOM 1860 N NE . ARG A 1 239 ? -2.103 -8.324 17.593 1.00 23.72 ? 239 ARG A NE 1 ATOM 1861 C CZ . ARG A 1 239 ? -2.193 -9.656 17.590 1.00 25.30 ? 239 ARG A CZ 1 ATOM 1862 N NH1 . ARG A 1 239 ? -1.108 -10.403 17.747 1.00 25.38 ? 239 ARG A NH1 1 ATOM 1863 N NH2 . ARG A 1 239 ? -3.377 -10.238 17.461 1.00 25.99 ? 239 ARG A NH2 1 ATOM 1864 N N . LEU A 1 240 ? 3.188 -4.003 17.971 1.00 23.00 ? 240 LEU A N 1 ATOM 1865 C CA . LEU A 1 240 ? 3.947 -2.747 18.034 1.00 20.98 ? 240 LEU A CA 1 ATOM 1866 C C . LEU A 1 240 ? 4.348 -2.256 16.636 1.00 20.37 ? 240 LEU A C 1 ATOM 1867 O O . LEU A 1 240 ? 4.267 -1.039 16.362 1.00 18.22 ? 240 LEU A O 1 ATOM 1868 C CB . LEU A 1 240 ? 5.158 -2.890 18.971 1.00 20.74 ? 240 LEU A CB 1 ATOM 1869 C CG . LEU A 1 240 ? 5.984 -1.615 19.234 1.00 22.14 ? 240 LEU A CG 1 ATOM 1870 C CD1 . LEU A 1 240 ? 5.090 -0.418 19.536 1.00 21.71 ? 240 LEU A CD1 1 ATOM 1871 C CD2 . LEU A 1 240 ? 7.005 -1.822 20.333 1.00 21.68 ? 240 LEU A CD2 1 ATOM 1872 N N . PRO A 1 241 ? 4.757 -3.184 15.731 1.00 19.92 ? 241 PRO A N 1 ATOM 1873 C CA . PRO A 1 241 ? 5.076 -2.768 14.367 1.00 20.20 ? 241 PRO A CA 1 ATOM 1874 C C . PRO A 1 241 ? 3.940 -2.084 13.601 1.00 19.61 ? 241 PRO A C 1 ATOM 1875 O O . PRO A 1 241 ? 4.209 -1.204 12.782 1.00 18.95 ? 241 PRO A O 1 ATOM 1876 C CB . PRO A 1 241 ? 5.421 -4.104 13.663 1.00 21.35 ? 241 PRO A CB 1 ATOM 1877 C CG . PRO A 1 241 ? 5.909 -4.989 14.758 1.00 20.25 ? 241 PRO A CG 1 ATOM 1878 C CD . PRO A 1 241 ? 5.101 -4.606 15.956 1.00 20.73 ? 241 PRO A CD 1 ATOM 1879 N N . ILE A 1 242 ? 2.696 -2.508 13.812 1.00 19.23 ? 242 ILE A N 1 ATOM 1880 C CA . ILE A 1 242 ? 1.550 -1.850 13.140 1.00 19.47 ? 242 ILE A CA 1 ATOM 1881 C C . ILE A 1 242 ? 1.232 -0.509 13.802 1.00 19.72 ? 242 ILE A C 1 ATOM 1882 O O . ILE A 1 242 ? 0.873 0.467 13.141 1.00 18.36 ? 242 ILE A O 1 ATOM 1883 C CB . ILE A 1 242 ? 0.317 -2.770 13.098 1.00 21.19 ? 242 ILE A CB 1 ATOM 1884 C CG1 . ILE A 1 242 ? -0.858 -2.113 12.364 1.00 22.54 ? 242 ILE A CG1 1 ATOM 1885 C CG2 . ILE A 1 242 ? -0.057 -3.244 14.458 1.00 21.20 ? 242 ILE A CG2 1 ATOM 1886 C CD1 . ILE A 1 242 ? -2.211 -2.422 12.960 1.00 24.05 ? 242 ILE A CD1 1 ATOM 1887 N N . VAL A 1 243 ? 1.392 -0.433 15.116 1.00 19.43 ? 243 VAL A N 1 ATOM 1888 C CA . VAL A 1 243 ? 1.245 0.857 15.769 1.00 19.51 ? 243 VAL A CA 1 ATOM 1889 C C . VAL A 1 243 ? 2.239 1.872 15.148 1.00 19.86 ? 243 VAL A C 1 ATOM 1890 O O . VAL A 1 243 ? 1.835 2.937 14.658 1.00 19.89 ? 243 VAL A O 1 ATOM 1891 C CB . VAL A 1 243 ? 1.386 0.713 17.290 1.00 19.28 ? 243 VAL A CB 1 ATOM 1892 C CG1 . VAL A 1 243 ? 1.487 2.084 17.975 1.00 18.54 ? 243 VAL A CG1 1 ATOM 1893 C CG2 . VAL A 1 243 ? 0.197 -0.087 17.824 1.00 19.34 ? 243 VAL A CG2 1 ATOM 1894 N N . TYR A 1 244 ? 3.521 1.524 15.128 1.00 20.86 ? 244 TYR A N 1 ATOM 1895 C CA . TYR A 1 244 ? 4.548 2.364 14.496 1.00 22.17 ? 244 TYR A CA 1 ATOM 1896 C C . TYR A 1 244 ? 4.181 2.684 13.060 1.00 21.55 ? 244 TYR A C 1 ATOM 1897 O O . TYR A 1 244 ? 4.278 3.814 12.620 1.00 19.39 ? 244 TYR A O 1 ATOM 1898 C CB . TYR A 1 244 ? 5.897 1.654 14.425 1.00 23.29 ? 244 TYR A CB 1 ATOM 1899 C CG . TYR A 1 244 ? 6.626 1.413 15.713 1.00 24.39 ? 244 TYR A CG 1 ATOM 1900 C CD1 . TYR A 1 244 ? 6.527 2.301 16.764 1.00 26.67 ? 244 TYR A CD1 1 ATOM 1901 C CD2 . TYR A 1 244 ? 7.482 0.307 15.843 1.00 26.05 ? 244 TYR A CD2 1 ATOM 1902 C CE1 . TYR A 1 244 ? 7.237 2.105 17.930 1.00 28.75 ? 244 TYR A CE1 1 ATOM 1903 C CE2 . TYR A 1 244 ? 8.192 0.103 17.007 1.00 28.67 ? 244 TYR A CE2 1 ATOM 1904 C CZ . TYR A 1 244 ? 8.054 1.012 18.045 1.00 26.95 ? 244 TYR A CZ 1 ATOM 1905 O OH . TYR A 1 244 ? 8.718 0.848 19.191 1.00 28.11 ? 244 TYR A OH 1 ATOM 1906 N N . GLN A 1 245 ? 3.807 1.661 12.310 1.00 22.12 ? 245 GLN A N 1 ATOM 1907 C CA . GLN A 1 245 ? 3.363 1.895 10.962 1.00 23.35 ? 245 GLN A CA 1 ATOM 1908 C C . GLN A 1 245 ? 2.335 3.016 10.904 1.00 20.77 ? 245 GLN A C 1 ATOM 1909 O O . GLN A 1 245 ? 2.505 3.961 10.157 1.00 17.71 ? 245 GLN A O 1 ATOM 1910 C CB . GLN A 1 245 ? 2.753 0.661 10.325 1.00 24.92 ? 245 GLN A CB 1 ATOM 1911 C CG . GLN A 1 245 ? 2.235 1.007 8.941 1.00 29.93 ? 245 GLN A CG 1 ATOM 1912 C CD . GLN A 1 245 ? 1.696 -0.176 8.175 1.00 34.09 ? 245 GLN A CD 1 ATOM 1913 O OE1 . GLN A 1 245 ? 2.436 -1.090 7.826 1.00 38.63 ? 245 GLN A OE1 1 ATOM 1914 N NE2 . GLN A 1 245 ? 0.404 -0.154 7.897 1.00 35.96 ? 245 GLN A NE2 1 ATOM 1915 N N . ARG A 1 246 ? 1.290 2.909 11.722 1.00 19.46 ? 246 ARG A N 1 ATOM 1916 C CA . ARG A 1 246 ? 0.165 3.844 11.665 1.00 18.34 ? 246 ARG A CA 1 ATOM 1917 C C . ARG A 1 246 ? 0.515 5.250 12.176 1.00 18.06 ? 246 ARG A C 1 ATOM 1918 O O . ARG A 1 246 ? -0.015 6.239 11.697 1.00 16.14 ? 246 ARG A O 1 ATOM 1919 C CB . ARG A 1 246 ? -1.034 3.256 12.420 1.00 18.01 ? 246 ARG A CB 1 ATOM 1920 C CG . ARG A 1 246 ? -1.490 1.908 11.869 1.00 17.95 ? 246 ARG A CG 1 ATOM 1921 C CD . ARG A 1 246 ? -1.954 2.013 10.421 1.00 18.44 ? 246 ARG A CD 1 ATOM 1922 N NE . ARG A 1 246 ? -3.277 2.622 10.315 1.00 17.94 ? 246 ARG A NE 1 ATOM 1923 C CZ . ARG A 1 246 ? -3.867 3.005 9.183 1.00 17.13 ? 246 ARG A CZ 1 ATOM 1924 N NH1 . ARG A 1 246 ? -3.241 2.944 8.012 1.00 17.14 ? 246 ARG A NH1 1 ATOM 1925 N NH2 . ARG A 1 246 ? -5.087 3.533 9.250 1.00 16.73 ? 246 ARG A NH2 1 ATOM 1926 N N . LEU A 1 247 ? 1.461 5.343 13.097 1.00 17.57 ? 247 LEU A N 1 ATOM 1927 C CA . LEU A 1 247 ? 1.904 6.652 13.559 1.00 16.20 ? 247 LEU A CA 1 ATOM 1928 C C . LEU A 1 247 ? 2.685 7.331 12.433 1.00 16.19 ? 247 LEU A C 1 ATOM 1929 O O . LEU A 1 247 ? 2.443 8.511 12.146 1.00 14.90 ? 247 LEU A O 1 ATOM 1930 C CB . LEU A 1 247 ? 2.718 6.550 14.863 1.00 16.86 ? 247 LEU A CB 1 ATOM 1931 C CG . LEU A 1 247 ? 1.944 6.036 16.081 1.00 16.71 ? 247 LEU A CG 1 ATOM 1932 C CD1 . LEU A 1 247 ? 2.889 5.720 17.232 1.00 17.29 ? 247 LEU A CD1 1 ATOM 1933 C CD2 . LEU A 1 247 ? 0.834 6.979 16.528 1.00 17.27 ? 247 LEU A CD2 1 ATOM 1934 N N . ALA A 1 248 ? 3.570 6.589 11.744 1.00 15.61 ? 248 ALA A N 1 ATOM 1935 C CA . ALA A 1 248 ? 4.416 7.200 10.701 1.00 15.27 ? 248 ALA A CA 1 ATOM 1936 C C . ALA A 1 248 ? 3.588 7.680 9.499 1.00 16.62 ? 248 ALA A C 1 ATOM 1937 O O . ALA A 1 248 ? 3.835 8.764 8.889 1.00 14.51 ? 248 ALA A O 1 ATOM 1938 C CB . ALA A 1 248 ? 5.474 6.203 10.249 1.00 15.74 ? 248 ALA A CB 1 ATOM 1939 N N . GLN A 1 249 ? 2.669 6.795 9.114 1.00 16.49 ? 249 GLN A N 1 ATOM 1940 C CA . GLN A 1 249 ? 1.635 7.115 8.151 1.00 17.17 ? 249 GLN A CA 1 ATOM 1941 C C . GLN A 1 249 ? 0.812 8.360 8.468 1.00 16.27 ? 249 GLN A C 1 ATOM 1942 O O . GLN A 1 249 ? 0.610 9.165 7.617 1.00 18.18 ? 249 GLN A O 1 ATOM 1943 C CB . GLN A 1 249 ? 0.707 5.940 8.017 1.00 16.99 ? 249 GLN A CB 1 ATOM 1944 C CG . GLN A 1 249 ? 1.259 4.926 7.034 1.00 17.14 ? 249 GLN A CG 1 ATOM 1945 C CD . GLN A 1 249 ? 0.372 3.751 6.944 1.00 17.18 ? 249 GLN A CD 1 ATOM 1946 O OE1 . GLN A 1 249 ? -0.249 3.373 7.938 1.00 15.58 ? 249 GLN A OE1 1 ATOM 1947 N NE2 . GLN A 1 249 ? 0.252 3.185 5.740 1.00 17.39 ? 249 GLN A NE2 1 ATOM 1948 N N . GLY A 1 250 ? 0.307 8.481 9.670 1.00 15.90 ? 250 GLY A N 1 ATOM 1949 C CA . GLY A 1 250 ? -0.398 9.704 10.094 1.00 15.80 ? 250 GLY A CA 1 ATOM 1950 C C . GLY A 1 250 ? 0.453 10.940 9.939 1.00 14.84 ? 250 GLY A C 1 ATOM 1951 O O . GLY A 1 250 ? 0.059 11.929 9.293 1.00 13.61 ? 250 GLY A O 1 ATOM 1952 N N . GLY A 1 251 ? 1.654 10.834 10.501 1.00 14.93 ? 251 GLY A N 1 ATOM 1953 C CA . GLY A 1 251 ? 2.706 11.830 10.365 1.00 15.33 ? 251 GLY A CA 1 ATOM 1954 C C . GLY A 1 251 ? 3.070 12.266 8.975 1.00 15.74 ? 251 GLY A C 1 ATOM 1955 O O . GLY A 1 251 ? 3.194 13.457 8.679 1.00 16.28 ? 251 GLY A O 1 ATOM 1956 N N . VAL A 1 252 ? 3.267 11.301 8.111 1.00 16.70 ? 252 VAL A N 1 ATOM 1957 C CA . VAL A 1 252 ? 3.606 11.589 6.730 1.00 17.54 ? 252 VAL A CA 1 ATOM 1958 C C . VAL A 1 252 ? 2.425 12.173 5.973 1.00 17.24 ? 252 VAL A C 1 ATOM 1959 O O . VAL A 1 252 ? 2.583 13.105 5.173 1.00 18.86 ? 252 VAL A O 1 ATOM 1960 C CB . VAL A 1 252 ? 4.160 10.306 6.082 1.00 18.33 ? 252 VAL A CB 1 ATOM 1961 C CG1 . VAL A 1 252 ? 4.118 10.374 4.583 1.00 19.91 ? 252 VAL A CG1 1 ATOM 1962 C CG2 . VAL A 1 252 ? 5.592 10.090 6.560 1.00 17.98 ? 252 VAL A CG2 1 ATOM 1963 N N . ARG A 1 253 ? 1.231 11.669 6.234 1.00 17.18 ? 253 ARG A N 1 ATOM 1964 C CA . ARG A 1 253 ? 0.056 12.111 5.476 1.00 16.87 ? 253 ARG A CA 1 ATOM 1965 C C . ARG A 1 253 ? -0.455 13.441 5.979 1.00 16.25 ? 253 ARG A C 1 ATOM 1966 O O . ARG A 1 253 ? -1.015 14.240 5.227 1.00 15.92 ? 253 ARG A O 1 ATOM 1967 C CB . ARG A 1 253 ? -1.023 11.049 5.530 1.00 17.94 ? 253 ARG A CB 1 ATOM 1968 C CG . ARG A 1 253 ? -0.822 9.981 4.449 1.00 18.49 ? 253 ARG A CG 1 ATOM 1969 C CD . ARG A 1 253 ? -1.241 8.614 4.918 1.00 17.00 ? 253 ARG A CD 1 ATOM 1970 N NE . ARG A 1 253 ? -1.169 7.620 3.856 1.00 16.37 ? 253 ARG A NE 1 ATOM 1971 C CZ . ARG A 1 253 ? -1.619 6.383 4.011 1.00 16.18 ? 253 ARG A CZ 1 ATOM 1972 N NH1 . ARG A 1 253 ? -2.149 6.044 5.190 1.00 16.24 ? 253 ARG A NH1 1 ATOM 1973 N NH2 . ARG A 1 253 ? -1.567 5.483 3.015 1.00 15.21 ? 253 ARG A NH2 1 ATOM 1974 N N . LEU A 1 254 ? -0.250 13.706 7.254 1.00 16.93 ? 254 LEU A N 1 ATOM 1975 C CA . LEU A 1 254 ? -0.613 15.044 7.775 1.00 16.23 ? 254 LEU A CA 1 ATOM 1976 C C . LEU A 1 254 ? 0.221 16.077 7.057 1.00 16.13 ? 254 LEU A C 1 ATOM 1977 O O . LEU A 1 254 ? -0.350 16.928 6.410 1.00 16.89 ? 254 LEU A O 1 ATOM 1978 C CB . LEU A 1 254 ? -0.489 15.135 9.297 1.00 15.15 ? 254 LEU A CB 1 ATOM 1979 C CG . LEU A 1 254 ? -0.794 16.515 9.930 1.00 14.18 ? 254 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 254 ? -2.094 17.115 9.436 1.00 13.15 ? 254 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 254 ? -0.768 16.389 11.422 1.00 14.20 ? 254 LEU A CD2 1 ATOM 1982 N N . ALA A 1 255 ? 1.558 15.973 7.113 1.00 17.74 ? 255 ALA A N 1 ATOM 1983 C CA . ALA A 1 255 ? 2.466 16.883 6.354 1.00 17.71 ? 255 ALA A CA 1 ATOM 1984 C C . ALA A 1 255 ? 2.163 16.992 4.858 1.00 17.73 ? 255 ALA A C 1 ATOM 1985 O O . ALA A 1 255 ? 2.031 18.085 4.318 1.00 18.24 ? 255 ALA A O 1 ATOM 1986 C CB . ALA A 1 255 ? 3.929 16.482 6.555 1.00 17.78 ? 255 ALA A CB 1 ATOM 1987 N N . ALA A 1 256 ? 2.040 15.859 4.183 1.00 19.65 ? 256 ALA A N 1 ATOM 1988 C CA . ALA A 1 256 ? 1.684 15.823 2.761 1.00 20.73 ? 256 ALA A CA 1 ATOM 1989 C C . ALA A 1 256 ? 0.401 16.611 2.478 1.00 22.25 ? 256 ALA A C 1 ATOM 1990 O O . ALA A 1 256 ? 0.260 17.283 1.433 1.00 22.60 ? 256 ALA A O 1 ATOM 1991 C CB . ALA A 1 256 ? 1.522 14.372 2.307 1.00 22.56 ? 256 ALA A CB 1 ATOM 1992 N N . THR A 1 257 ? -0.541 16.549 3.413 1.00 21.43 ? 257 THR A N 1 ATOM 1993 C CA . THR A 1 257 ? -1.824 17.215 3.222 1.00 20.69 ? 257 THR A CA 1 ATOM 1994 C C . THR A 1 257 ? -1.717 18.729 3.420 1.00 20.60 ? 257 THR A C 1 ATOM 1995 O O . THR A 1 257 ? -2.271 19.519 2.638 1.00 20.46 ? 257 THR A O 1 ATOM 1996 C CB . THR A 1 257 ? -2.882 16.598 4.144 1.00 20.73 ? 257 THR A CB 1 ATOM 1997 O OG1 . THR A 1 257 ? -3.108 15.248 3.725 1.00 20.27 ? 257 THR A OG1 1 ATOM 1998 C CG2 . THR A 1 257 ? -4.178 17.359 4.091 1.00 20.43 ? 257 THR A CG2 1 ATOM 1999 N N . LEU A 1 258 ? -1.001 19.151 4.441 1.00 20.26 ? 258 LEU A N 1 ATOM 2000 C CA . LEU A 1 258 ? -0.842 20.584 4.650 1.00 21.11 ? 258 LEU A CA 1 ATOM 2001 C C . LEU A 1 258 ? 0.025 21.239 3.575 1.00 22.19 ? 258 LEU A C 1 ATOM 2002 O O . LEU A 1 258 ? -0.203 22.404 3.210 1.00 22.38 ? 258 LEU A O 1 ATOM 2003 C CB . LEU A 1 258 ? -0.274 20.861 6.043 1.00 21.26 ? 258 LEU A CB 1 ATOM 2004 C CG . LEU A 1 258 ? -1.171 20.389 7.180 1.00 20.61 ? 258 LEU A CG 1 ATOM 2005 C CD1 . LEU A 1 258 ? -0.455 20.507 8.498 1.00 21.83 ? 258 LEU A CD1 1 ATOM 2006 C CD2 . LEU A 1 258 ? -2.470 21.167 7.200 1.00 22.01 ? 258 LEU A CD2 1 ATOM 2007 N N . ASN A 1 259 ? 1.029 20.515 3.089 1.00 24.02 ? 259 ASN A N 1 ATOM 2008 C CA . ASN A 1 259 ? 1.836 20.977 1.948 1.00 24.96 ? 259 ASN A CA 1 ATOM 2009 C C . ASN A 1 259 ? 0.978 21.174 0.702 1.00 25.48 ? 259 ASN A C 1 ATOM 2010 O O . ASN A 1 259 ? 1.136 22.172 -0.005 1.00 24.76 ? 259 ASN A O 1 ATOM 2011 C CB . ASN A 1 259 ? 2.966 19.997 1.610 1.00 25.20 ? 259 ASN A CB 1 ATOM 2012 C CG . ASN A 1 259 ? 4.075 19.998 2.630 1.00 24.60 ? 259 ASN A CG 1 ATOM 2013 O OD1 . ASN A 1 259 ? 4.208 20.927 3.388 1.00 23.56 ? 259 ASN A OD1 1 ATOM 2014 N ND2 . ASN A 1 259 ? 4.880 18.930 2.651 1.00 25.66 ? 259 ASN A ND2 1 ATOM 2015 N N . ARG A 1 260 ? 0.086 20.223 0.429 1.00 26.91 ? 260 ARG A N 1 ATOM 2016 C CA . ARG A 1 260 ? -0.837 20.325 -0.715 1.00 29.05 ? 260 ARG A CA 1 ATOM 2017 C C . ARG A 1 260 ? -1.764 21.506 -0.534 1.00 28.45 ? 260 ARG A C 1 ATOM 2018 O O . ARG A 1 260 ? -1.901 22.315 -1.420 1.00 27.68 ? 260 ARG A O 1 ATOM 2019 C CB . ARG A 1 260 ? -1.706 19.074 -0.894 1.00 30.07 ? 260 ARG A CB 1 ATOM 2020 C CG . ARG A 1 260 ? -1.076 18.002 -1.757 1.00 34.06 ? 260 ARG A CG 1 ATOM 2021 C CD . ARG A 1 260 ? -2.095 16.960 -2.210 1.00 36.45 ? 260 ARG A CD 1 ATOM 2022 N NE . ARG A 1 260 ? -2.621 16.211 -1.083 1.00 38.17 ? 260 ARG A NE 1 ATOM 2023 C CZ . ARG A 1 260 ? -1.974 15.248 -0.423 1.00 39.80 ? 260 ARG A CZ 1 ATOM 2024 N NH1 . ARG A 1 260 ? -0.740 14.870 -0.765 1.00 40.80 ? 260 ARG A NH1 1 ATOM 2025 N NH2 . ARG A 1 260 ? -2.580 14.651 0.598 1.00 39.50 ? 260 ARG A NH2 1 ATOM 2026 N N . ILE A 1 261 ? -2.412 21.572 0.622 1.00 30.04 ? 261 ILE A N 1 ATOM 2027 C CA . ILE A 1 261 ? -3.356 22.646 0.923 1.00 30.45 ? 261 ILE A CA 1 ATOM 2028 C C . ILE A 1 261 ? -2.730 24.019 0.774 1.00 30.41 ? 261 ILE A C 1 ATOM 2029 O O . ILE A 1 261 ? -3.273 24.891 0.118 1.00 32.75 ? 261 ILE A O 1 ATOM 2030 C CB . ILE A 1 261 ? -3.890 22.540 2.361 1.00 30.58 ? 261 ILE A CB 1 ATOM 2031 C CG1 . ILE A 1 261 ? -4.849 21.352 2.474 1.00 31.67 ? 261 ILE A CG1 1 ATOM 2032 C CG2 . ILE A 1 261 ? -4.605 23.825 2.757 1.00 31.24 ? 261 ILE A CG2 1 ATOM 2033 C CD1 . ILE A 1 261 ? -5.121 20.961 3.908 1.00 31.87 ? 261 ILE A CD1 1 ATOM 2034 N N . PHE A 1 262 ? -1.587 24.218 1.395 1.00 30.06 ? 262 PHE A N 1 ATOM 2035 C CA . PHE A 1 262 ? -1.034 25.555 1.459 1.00 30.18 ? 262 PHE A CA 1 ATOM 2036 C C . PHE A 1 262 ? -0.140 25.870 0.271 1.00 31.90 ? 262 PHE A C 1 ATOM 2037 O O . PHE A 1 262 ? 0.401 26.946 0.206 1.00 33.38 ? 262 PHE A O 1 ATOM 2038 C CB . PHE A 1 262 ? -0.254 25.734 2.754 1.00 29.30 ? 262 PHE A CB 1 ATOM 2039 C CG . PHE A 1 262 ? -1.108 25.681 3.991 1.00 27.70 ? 262 PHE A CG 1 ATOM 2040 C CD1 . PHE A 1 262 ? -2.223 26.493 4.117 1.00 27.48 ? 262 PHE A CD1 1 ATOM 2041 C CD2 . PHE A 1 262 ? -0.764 24.861 5.043 1.00 25.47 ? 262 PHE A CD2 1 ATOM 2042 C CE1 . PHE A 1 262 ? -2.988 26.464 5.274 1.00 28.81 ? 262 PHE A CE1 1 ATOM 2043 C CE2 . PHE A 1 262 ? -1.512 24.831 6.200 1.00 26.47 ? 262 PHE A CE2 1 ATOM 2044 C CZ . PHE A 1 262 ? -2.621 25.636 6.325 1.00 26.85 ? 262 PHE A CZ 1 ATOM 2045 N N . GLY A 1 263 ? 0.029 24.921 -0.645 1.00 33.19 ? 263 GLY A N 1 ATOM 2046 C CA . GLY A 1 263 ? 0.852 25.113 -1.829 1.00 34.11 ? 263 GLY A CA 1 ATOM 2047 C C . GLY A 1 263 ? 0.011 25.485 -3.043 1.00 36.96 ? 263 GLY A C 1 ATOM 2048 O O . GLY A 1 263 ? -1.236 25.424 -3.052 1.00 37.55 ? 263 GLY A O 1 ATOM 2049 N N . HIS A 1 264 ? 0.588 25.850 -4.071 1.00 39.45 ? 264 HIS A N 1 ATOM 2050 N N . TRP B 1 1 ? 4.369 -8.270 -19.053 1.00 15.75 ? 1 TRP B N 1 ATOM 2051 C CA . TRP B 1 1 ? 5.563 -8.157 -19.921 1.00 14.98 ? 1 TRP B CA 1 ATOM 2052 C C . TRP B 1 1 ? 5.435 -8.964 -21.184 1.00 15.76 ? 1 TRP B C 1 ATOM 2053 O O . TRP B 1 1 ? 4.720 -9.983 -21.229 1.00 16.11 ? 1 TRP B O 1 ATOM 2054 C CB . TRP B 1 1 ? 6.798 -8.685 -19.209 1.00 14.66 ? 1 TRP B CB 1 ATOM 2055 C CG . TRP B 1 1 ? 7.033 -8.051 -17.876 1.00 14.90 ? 1 TRP B CG 1 ATOM 2056 C CD1 . TRP B 1 1 ? 6.790 -8.606 -16.666 1.00 14.33 ? 1 TRP B CD1 1 ATOM 2057 C CD2 . TRP B 1 1 ? 7.537 -6.735 -17.631 1.00 13.97 ? 1 TRP B CD2 1 ATOM 2058 N NE1 . TRP B 1 1 ? 7.104 -7.715 -15.676 1.00 14.78 ? 1 TRP B NE1 1 ATOM 2059 C CE2 . TRP B 1 1 ? 7.592 -6.565 -16.247 1.00 14.54 ? 1 TRP B CE2 1 ATOM 2060 C CE3 . TRP B 1 1 ? 7.977 -5.704 -18.450 1.00 15.13 ? 1 TRP B CE3 1 ATOM 2061 C CZ2 . TRP B 1 1 ? 8.049 -5.378 -15.650 1.00 14.33 ? 1 TRP B CZ2 1 ATOM 2062 C CZ3 . TRP B 1 1 ? 8.436 -4.511 -17.861 1.00 15.10 ? 1 TRP B CZ3 1 ATOM 2063 C CH2 . TRP B 1 1 ? 8.463 -4.368 -16.474 1.00 14.90 ? 1 TRP B CH2 1 ATOM 2064 N N . GLY B 1 2 ? 6.177 -8.545 -22.206 1.00 15.28 ? 2 GLY B N 1 ATOM 2065 C CA . GLY B 1 2 ? 6.386 -9.388 -23.363 1.00 16.57 ? 2 GLY B CA 1 ATOM 2066 C C . GLY B 1 2 ? 7.406 -10.446 -23.042 1.00 16.88 ? 2 GLY B C 1 ATOM 2067 O O . GLY B 1 2 ? 7.829 -10.586 -21.898 1.00 16.64 ? 2 GLY B O 1 ATOM 2068 N N . LYS B 1 3 ? 7.818 -11.173 -24.067 1.00 18.80 ? 3 LYS B N 1 ATOM 2069 C CA . LYS B 1 3 ? 8.762 -12.275 -23.949 1.00 21.99 ? 3 LYS B CA 1 ATOM 2070 C C . LYS B 1 3 ? 10.069 -11.963 -23.233 1.00 20.92 ? 3 LYS B C 1 ATOM 2071 O O . LYS B 1 3 ? 10.506 -12.744 -22.390 1.00 18.50 ? 3 LYS B O 1 ATOM 2072 C CB . LYS B 1 3 ? 9.135 -12.786 -25.345 1.00 26.06 ? 3 LYS B CB 1 ATOM 2073 C CG . LYS B 1 3 ? 10.127 -13.945 -25.356 1.00 31.90 ? 3 LYS B CG 1 ATOM 2074 C CD . LYS B 1 3 ? 10.988 -13.926 -26.621 1.00 36.02 ? 3 LYS B CD 1 ATOM 2075 C CE . LYS B 1 3 ? 11.973 -15.087 -26.641 1.00 37.93 ? 3 LYS B CE 1 ATOM 2076 N NZ . LYS B 1 3 ? 11.269 -16.380 -26.817 1.00 38.77 ? 3 LYS B NZ 1 ATOM 2077 N N . GLU B 1 4 ? 10.733 -10.880 -23.611 1.00 20.61 ? 4 GLU B N 1 ATOM 2078 C CA . GLU B 1 4 ? 12.035 -10.624 -23.027 1.00 23.49 ? 4 GLU B CA 1 ATOM 2079 C C . GLU B 1 4 ? 11.872 -10.315 -21.529 1.00 22.31 ? 4 GLU B C 1 ATOM 2080 O O . GLU B 1 4 ? 12.622 -10.812 -20.703 1.00 21.21 ? 4 GLU B O 1 ATOM 2081 C CB . GLU B 1 4 ? 12.868 -9.576 -23.802 1.00 26.44 ? 4 GLU B CB 1 ATOM 2082 C CG . GLU B 1 4 ? 12.141 -8.432 -24.494 1.00 29.39 ? 4 GLU B CG 1 ATOM 2083 C CD . GLU B 1 4 ? 11.291 -8.861 -25.695 1.00 28.70 ? 4 GLU B CD 1 ATOM 2084 O OE1 . GLU B 1 4 ? 11.856 -9.269 -26.727 1.00 32.61 ? 4 GLU B OE1 1 ATOM 2085 O OE2 . GLU B 1 4 ? 10.047 -8.794 -25.597 1.00 27.22 ? 4 GLU B OE2 1 ATOM 2086 N N . GLY B 1 5 ? 10.823 -9.588 -21.172 1.00 21.96 ? 5 GLY B N 1 ATOM 2087 C CA . GLY B 1 5 ? 10.547 -9.311 -19.774 1.00 21.40 ? 5 GLY B CA 1 ATOM 2088 C C . GLY B 1 5 ? 10.431 -10.534 -18.880 1.00 20.27 ? 5 GLY B C 1 ATOM 2089 O O . GLY B 1 5 ? 11.106 -10.620 -17.845 1.00 19.22 ? 5 GLY B O 1 ATOM 2090 N N . HIS B 1 6 ? 9.582 -11.493 -19.248 1.00 19.60 ? 6 HIS B N 1 ATOM 2091 C CA . HIS B 1 6 ? 9.476 -12.706 -18.431 1.00 19.70 ? 6 HIS B CA 1 ATOM 2092 C C . HIS B 1 6 ? 10.769 -13.528 -18.424 1.00 19.84 ? 6 HIS B C 1 ATOM 2093 O O . HIS B 1 6 ? 11.124 -14.146 -17.418 1.00 17.44 ? 6 HIS B O 1 ATOM 2094 C CB . HIS B 1 6 ? 8.310 -13.572 -18.894 1.00 20.79 ? 6 HIS B CB 1 ATOM 2095 C CG . HIS B 1 6 ? 6.980 -12.934 -18.671 1.00 21.68 ? 6 HIS B CG 1 ATOM 2096 N ND1 . HIS B 1 6 ? 6.372 -12.914 -17.440 1.00 22.02 ? 6 HIS B ND1 1 ATOM 2097 C CD2 . HIS B 1 6 ? 6.158 -12.267 -19.512 1.00 22.83 ? 6 HIS B CD2 1 ATOM 2098 C CE1 . HIS B 1 6 ? 5.218 -12.278 -17.537 1.00 24.03 ? 6 HIS B CE1 1 ATOM 2099 N NE2 . HIS B 1 6 ? 5.068 -11.869 -18.783 1.00 23.64 ? 6 HIS B NE2 1 ATOM 2100 N N . GLU B 1 7 ? 11.456 -13.558 -19.562 1.00 20.24 ? 7 GLU B N 1 ATOM 2101 C CA . GLU B 1 7 ? 12.767 -14.231 -19.636 1.00 21.16 ? 7 GLU B CA 1 ATOM 2102 C C . GLU B 1 7 ? 13.725 -13.712 -18.571 1.00 19.93 ? 7 GLU B C 1 ATOM 2103 O O . GLU B 1 7 ? 14.274 -14.449 -17.749 1.00 19.04 ? 7 GLU B O 1 ATOM 2104 C CB . GLU B 1 7 ? 13.382 -13.978 -20.980 1.00 23.42 ? 7 GLU B CB 1 ATOM 2105 C CG . GLU B 1 7 ? 13.412 -15.142 -21.895 1.00 27.96 ? 7 GLU B CG 1 ATOM 2106 C CD . GLU B 1 7 ? 14.550 -14.986 -22.894 1.00 31.88 ? 7 GLU B CD 1 ATOM 2107 O OE1 . GLU B 1 7 ? 15.738 -15.083 -22.490 1.00 33.20 ? 7 GLU B OE1 1 ATOM 2108 O OE2 . GLU B 1 7 ? 14.253 -14.712 -24.070 1.00 35.00 ? 7 GLU B OE2 1 ATOM 2109 N N . ILE B 1 8 ? 13.896 -12.398 -18.585 1.00 18.97 ? 8 ILE B N 1 ATOM 2110 C CA . ILE B 1 8 ? 14.764 -11.730 -17.642 1.00 17.37 ? 8 ILE B CA 1 ATOM 2111 C C . ILE B 1 8 ? 14.389 -12.087 -16.209 1.00 17.51 ? 8 ILE B C 1 ATOM 2112 O O . ILE B 1 8 ? 15.277 -12.382 -15.389 1.00 16.90 ? 8 ILE B O 1 ATOM 2113 C CB . ILE B 1 8 ? 14.723 -10.199 -17.858 1.00 17.03 ? 8 ILE B CB 1 ATOM 2114 C CG1 . ILE B 1 8 ? 15.290 -9.842 -19.222 1.00 17.57 ? 8 ILE B CG1 1 ATOM 2115 C CG2 . ILE B 1 8 ? 15.492 -9.484 -16.769 1.00 17.17 ? 8 ILE B CG2 1 ATOM 2116 C CD1 . ILE B 1 8 ? 15.114 -8.380 -19.572 1.00 18.94 ? 8 ILE B CD1 1 ATOM 2117 N N . ILE B 1 9 ? 13.090 -12.074 -15.899 1.00 17.30 ? 9 ILE B N 1 ATOM 2118 C CA . ILE B 1 9 ? 12.638 -12.283 -14.505 1.00 18.05 ? 9 ILE B CA 1 ATOM 2119 C C . ILE B 1 9 ? 12.892 -13.724 -14.076 1.00 19.27 ? 9 ILE B C 1 ATOM 2120 O O . ILE B 1 9 ? 13.398 -13.998 -12.973 1.00 20.73 ? 9 ILE B O 1 ATOM 2121 C CB . ILE B 1 9 ? 11.151 -11.859 -14.329 1.00 18.47 ? 9 ILE B CB 1 ATOM 2122 C CG1 . ILE B 1 9 ? 11.047 -10.327 -14.318 1.00 17.56 ? 9 ILE B CG1 1 ATOM 2123 C CG2 . ILE B 1 9 ? 10.516 -12.390 -13.031 1.00 16.92 ? 9 ILE B CG2 1 ATOM 2124 C CD1 . ILE B 1 9 ? 9.679 -9.774 -14.644 1.00 16.81 ? 9 ILE B CD1 1 ATOM 2125 N N . CYS B 1 10 ? 12.579 -14.653 -14.961 1.00 19.39 ? 10 CYS B N 1 ATOM 2126 C CA . CYS B 1 10 ? 12.755 -16.046 -14.642 1.00 21.29 ? 10 CYS B CA 1 ATOM 2127 C C . CYS B 1 10 ? 14.230 -16.426 -14.595 1.00 20.57 ? 10 CYS B C 1 ATOM 2128 O O . CYS B 1 10 ? 14.628 -17.144 -13.702 1.00 19.62 ? 10 CYS B O 1 ATOM 2129 C CB . CYS B 1 10 ? 11.976 -16.905 -15.606 1.00 23.58 ? 10 CYS B CB 1 ATOM 2130 S SG . CYS B 1 10 ? 10.256 -16.805 -15.192 1.00 25.53 ? 10 CYS B SG 1 ATOM 2131 N N . LYS B 1 11 ? 15.036 -15.891 -15.498 1.00 21.12 ? 11 LYS B N 1 ATOM 2132 C CA . LYS B 1 11 ? 16.485 -16.077 -15.428 1.00 23.27 ? 11 LYS B CA 1 ATOM 2133 C C . LYS B 1 11 ? 17.089 -15.598 -14.128 1.00 22.30 ? 11 LYS B C 1 ATOM 2134 O O . LYS B 1 11 ? 17.947 -16.249 -13.554 1.00 22.81 ? 11 LYS B O 1 ATOM 2135 C CB . LYS B 1 11 ? 17.188 -15.338 -16.566 1.00 25.35 ? 11 LYS B CB 1 ATOM 2136 C CG . LYS B 1 11 ? 17.035 -16.045 -17.881 1.00 27.58 ? 11 LYS B CG 1 ATOM 2137 C CD . LYS B 1 11 ? 17.494 -15.163 -19.022 1.00 29.77 ? 11 LYS B CD 1 ATOM 2138 C CE . LYS B 1 11 ? 17.421 -15.935 -20.337 1.00 32.04 ? 11 LYS B CE 1 ATOM 2139 N NZ . LYS B 1 11 ? 18.236 -17.176 -20.303 1.00 31.89 ? 11 LYS B NZ 1 ATOM 2140 N N . ILE B 1 12 ? 16.683 -14.423 -13.690 1.00 21.64 ? 12 ILE B N 1 ATOM 2141 C CA . ILE B 1 12 ? 17.223 -13.885 -12.454 1.00 20.98 ? 12 ILE B CA 1 ATOM 2142 C C . ILE B 1 12 ? 16.777 -14.814 -11.344 1.00 20.84 ? 12 ILE B C 1 ATOM 2143 O O . ILE B 1 12 ? 17.584 -15.229 -10.521 1.00 20.07 ? 12 ILE B O 1 ATOM 2144 C CB . ILE B 1 12 ? 16.773 -12.412 -12.267 1.00 20.62 ? 12 ILE B CB 1 ATOM 2145 C CG1 . ILE B 1 12 ? 17.561 -11.561 -13.260 1.00 19.65 ? 12 ILE B CG1 1 ATOM 2146 C CG2 . ILE B 1 12 ? 16.928 -11.898 -10.814 1.00 20.76 ? 12 ILE B CG2 1 ATOM 2147 C CD1 . ILE B 1 12 ? 17.001 -10.194 -13.495 1.00 19.01 ? 12 ILE B CD1 1 ATOM 2148 N N . ALA B 1 13 ? 15.491 -15.184 -11.356 1.00 20.97 ? 13 ALA B N 1 ATOM 2149 C CA . ALA B 1 13 ? 14.914 -15.945 -10.265 1.00 20.45 ? 13 ALA B CA 1 ATOM 2150 C C . ALA B 1 13 ? 15.575 -17.319 -10.151 1.00 21.79 ? 13 ALA B C 1 ATOM 2151 O O . ALA B 1 13 ? 16.014 -17.741 -9.073 1.00 20.20 ? 13 ALA B O 1 ATOM 2152 C CB . ALA B 1 13 ? 13.397 -16.086 -10.453 1.00 21.68 ? 13 ALA B CB 1 ATOM 2153 N N . GLN B 1 14 ? 15.711 -18.007 -11.267 1.00 23.48 ? 14 GLN B N 1 ATOM 2154 C CA . GLN B 1 14 ? 16.249 -19.361 -11.192 1.00 25.97 ? 14 GLN B CA 1 ATOM 2155 C C . GLN B 1 14 ? 17.651 -19.411 -10.594 1.00 26.27 ? 14 GLN B C 1 ATOM 2156 O O . GLN B 1 14 ? 17.973 -20.322 -9.849 1.00 28.94 ? 14 GLN B O 1 ATOM 2157 C CB . GLN B 1 14 ? 16.206 -20.071 -12.536 1.00 25.84 ? 14 GLN B CB 1 ATOM 2158 C CG . GLN B 1 14 ? 16.560 -21.551 -12.389 1.00 28.07 ? 14 GLN B CG 1 ATOM 2159 C CD . GLN B 1 14 ? 16.009 -22.413 -13.506 1.00 30.80 ? 14 GLN B CD 1 ATOM 2160 O OE1 . GLN B 1 14 ? 15.801 -21.934 -14.633 1.00 30.37 ? 14 GLN B OE1 1 ATOM 2161 N NE2 . GLN B 1 14 ? 15.770 -23.706 -13.205 1.00 31.27 ? 14 GLN B NE2 1 ATOM 2162 N N . THR B 1 15 ? 18.472 -18.415 -10.889 1.00 28.09 ? 15 THR B N 1 ATOM 2163 C CA . THR B 1 15 ? 19.833 -18.374 -10.355 1.00 29.74 ? 15 THR B CA 1 ATOM 2164 C C . THR B 1 15 ? 19.884 -18.015 -8.871 1.00 26.65 ? 15 THR B C 1 ATOM 2165 O O . THR B 1 15 ? 20.943 -18.069 -8.262 1.00 26.01 ? 15 THR B O 1 ATOM 2166 C CB . THR B 1 15 ? 20.720 -17.374 -11.133 1.00 32.26 ? 15 THR B CB 1 ATOM 2167 O OG1 . THR B 1 15 ? 20.254 -16.025 -10.940 1.00 35.16 ? 15 THR B OG1 1 ATOM 2168 C CG2 . THR B 1 15 ? 20.732 -17.709 -12.598 1.00 32.38 ? 15 THR B CG2 1 ATOM 2169 N N . ARG B 1 16 ? 18.744 -17.642 -8.304 1.00 24.16 ? 16 ARG B N 1 ATOM 2170 C CA . ARG B 1 16 ? 18.664 -17.246 -6.910 1.00 23.10 ? 16 ARG B CA 1 ATOM 2171 C C . ARG B 1 16 ? 17.878 -18.226 -6.052 1.00 21.85 ? 16 ARG B C 1 ATOM 2172 O O . ARG B 1 16 ? 17.669 -17.976 -4.891 1.00 18.40 ? 16 ARG B O 1 ATOM 2173 C CB . ARG B 1 16 ? 18.058 -15.845 -6.800 1.00 22.55 ? 16 ARG B CB 1 ATOM 2174 C CG . ARG B 1 16 ? 18.921 -14.770 -7.455 1.00 21.94 ? 16 ARG B CG 1 ATOM 2175 C CD . ARG B 1 16 ? 18.236 -13.409 -7.338 1.00 22.53 ? 16 ARG B CD 1 ATOM 2176 N NE . ARG B 1 16 ? 18.112 -13.005 -5.948 1.00 20.76 ? 16 ARG B NE 1 ATOM 2177 C CZ . ARG B 1 16 ? 19.131 -12.568 -5.216 1.00 23.00 ? 16 ARG B CZ 1 ATOM 2178 N NH1 . ARG B 1 16 ? 20.359 -12.424 -5.752 1.00 23.53 ? 16 ARG B NH1 1 ATOM 2179 N NH2 . ARG B 1 16 ? 18.926 -12.256 -3.940 1.00 23.68 ? 16 ARG B NH2 1 ATOM 2180 N N . LEU B 1 17 ? 17.467 -19.346 -6.632 1.00 24.07 ? 17 LEU B N 1 ATOM 2181 C CA . LEU B 1 17 ? 16.810 -20.402 -5.880 1.00 27.08 ? 17 LEU B CA 1 ATOM 2182 C C . LEU B 1 17 ? 17.847 -21.144 -5.047 1.00 27.74 ? 17 LEU B C 1 ATOM 2183 O O . LEU B 1 17 ? 18.923 -21.449 -5.545 1.00 27.30 ? 17 LEU B O 1 ATOM 2184 C CB . LEU B 1 17 ? 16.130 -21.408 -6.823 1.00 27.56 ? 17 LEU B CB 1 ATOM 2185 C CG . LEU B 1 17 ? 15.073 -20.912 -7.808 1.00 26.51 ? 17 LEU B CG 1 ATOM 2186 C CD1 . LEU B 1 17 ? 14.661 -22.034 -8.763 1.00 27.31 ? 17 LEU B CD1 1 ATOM 2187 C CD2 . LEU B 1 17 ? 13.849 -20.388 -7.079 1.00 27.57 ? 17 LEU B CD2 1 ATOM 2188 N N . ASP B 1 18 ? 17.509 -21.416 -3.786 1.00 30.40 ? 18 ASP B N 1 ATOM 2189 C CA . ASP B 1 18 ? 18.268 -22.353 -2.949 1.00 31.18 ? 18 ASP B CA 1 ATOM 2190 C C . ASP B 1 18 ? 18.147 -23.763 -3.525 1.00 32.01 ? 18 ASP B C 1 ATOM 2191 O O . ASP B 1 18 ? 17.494 -23.967 -4.550 1.00 30.23 ? 18 ASP B O 1 ATOM 2192 C CB . ASP B 1 18 ? 17.846 -22.286 -1.466 1.00 32.46 ? 18 ASP B CB 1 ATOM 2193 C CG . ASP B 1 18 ? 16.354 -22.655 -1.220 1.00 35.89 ? 18 ASP B CG 1 ATOM 2194 O OD1 . ASP B 1 18 ? 15.844 -23.665 -1.772 1.00 36.08 ? 18 ASP B OD1 1 ATOM 2195 O OD2 . ASP B 1 18 ? 15.693 -21.925 -0.437 1.00 37.17 ? 18 ASP B OD2 1 ATOM 2196 N N . GLU B 1 19 ? 18.800 -24.722 -2.874 1.00 33.13 ? 19 GLU B N 1 ATOM 2197 C CA . GLU B 1 19 ? 18.978 -26.055 -3.420 1.00 32.05 ? 19 GLU B CA 1 ATOM 2198 C C . GLU B 1 19 ? 17.672 -26.840 -3.423 1.00 31.09 ? 19 GLU B C 1 ATOM 2199 O O . GLU B 1 19 ? 17.418 -27.627 -4.342 1.00 30.66 ? 19 GLU B O 1 ATOM 2200 C CB . GLU B 1 19 ? 20.042 -26.812 -2.622 1.00 34.15 ? 19 GLU B CB 1 ATOM 2201 C CG . GLU B 1 19 ? 20.540 -28.082 -3.299 1.00 36.82 ? 19 GLU B CG 1 ATOM 2202 C CD . GLU B 1 19 ? 21.565 -27.820 -4.394 1.00 37.64 ? 19 GLU B CD 1 ATOM 2203 O OE1 . GLU B 1 19 ? 22.081 -26.688 -4.482 1.00 36.78 ? 19 GLU B OE1 1 ATOM 2204 O OE2 . GLU B 1 19 ? 21.871 -28.772 -5.153 1.00 40.85 ? 19 GLU B OE2 1 ATOM 2205 N N . THR B 1 20 ? 16.853 -26.641 -2.403 1.00 29.79 ? 20 THR B N 1 ATOM 2206 C CA . THR B 1 20 ? 15.559 -27.325 -2.336 1.00 33.09 ? 20 THR B CA 1 ATOM 2207 C C . THR B 1 20 ? 14.611 -26.812 -3.422 1.00 32.34 ? 20 THR B C 1 ATOM 2208 O O . THR B 1 20 ? 13.971 -27.596 -4.129 1.00 31.37 ? 20 THR B O 1 ATOM 2209 C CB . THR B 1 20 ? 14.864 -27.133 -0.982 1.00 33.80 ? 20 THR B CB 1 ATOM 2210 O OG1 . THR B 1 20 ? 15.825 -27.178 0.075 1.00 35.95 ? 20 THR B OG1 1 ATOM 2211 C CG2 . THR B 1 20 ? 13.792 -28.211 -0.780 1.00 36.30 ? 20 THR B CG2 1 ATOM 2212 N N . ALA B 1 21 ? 14.521 -25.490 -3.556 1.00 30.55 ? 21 ALA B N 1 ATOM 2213 C CA . ALA B 1 21 ? 13.613 -24.916 -4.546 1.00 27.46 ? 21 ALA B CA 1 ATOM 2214 C C . ALA B 1 21 ? 14.076 -25.292 -5.966 1.00 27.60 ? 21 ALA B C 1 ATOM 2215 O O . ALA B 1 21 ? 13.246 -25.532 -6.856 1.00 25.75 ? 21 ALA B O 1 ATOM 2216 C CB . ALA B 1 21 ? 13.521 -23.416 -4.358 1.00 27.57 ? 21 ALA B CB 1 ATOM 2217 N N . ALA B 1 22 ? 15.396 -25.394 -6.156 1.00 27.03 ? 22 ALA B N 1 ATOM 2218 C CA . ALA B 1 22 ? 15.976 -25.720 -7.455 1.00 28.03 ? 22 ALA B CA 1 ATOM 2219 C C . ALA B 1 22 ? 15.653 -27.130 -7.939 1.00 27.86 ? 22 ALA B C 1 ATOM 2220 O O . ALA B 1 22 ? 15.286 -27.314 -9.103 1.00 26.41 ? 22 ALA B O 1 ATOM 2221 C CB . ALA B 1 22 ? 17.491 -25.468 -7.461 1.00 28.01 ? 22 ALA B CB 1 ATOM 2222 N N . LYS B 1 23 ? 15.760 -28.119 -7.058 1.00 28.66 ? 23 LYS B N 1 ATOM 2223 C CA . LYS B 1 23 ? 15.298 -29.465 -7.404 1.00 31.24 ? 23 LYS B CA 1 ATOM 2224 C C . LYS B 1 23 ? 13.791 -29.479 -7.663 1.00 28.04 ? 23 LYS B C 1 ATOM 2225 O O . LYS B 1 23 ? 13.327 -30.086 -8.627 1.00 25.48 ? 23 LYS B O 1 ATOM 2226 C CB . LYS B 1 23 ? 15.662 -30.505 -6.311 1.00 35.07 ? 23 LYS B CB 1 ATOM 2227 C CG . LYS B 1 23 ? 14.867 -31.804 -6.432 1.00 38.77 ? 23 LYS B CG 1 ATOM 2228 C CD . LYS B 1 23 ? 15.687 -33.077 -6.285 1.00 42.45 ? 23 LYS B CD 1 ATOM 2229 C CE . LYS B 1 23 ? 15.640 -33.634 -4.866 1.00 45.33 ? 23 LYS B CE 1 ATOM 2230 N NZ . LYS B 1 23 ? 14.305 -34.140 -4.436 1.00 47.08 ? 23 LYS B NZ 1 ATOM 2231 N N . ALA B 1 24 ? 13.019 -28.800 -6.823 1.00 26.29 ? 24 ALA B N 1 ATOM 2232 C CA . ALA B 1 24 ? 11.581 -28.837 -7.020 1.00 27.01 ? 24 ALA B CA 1 ATOM 2233 C C . ALA B 1 24 ? 11.234 -28.324 -8.428 1.00 26.77 ? 24 ALA B C 1 ATOM 2234 O O . ALA B 1 24 ? 10.462 -28.962 -9.139 1.00 26.56 ? 24 ALA B O 1 ATOM 2235 C CB . ALA B 1 24 ? 10.862 -28.035 -5.946 1.00 28.37 ? 24 ALA B CB 1 ATOM 2236 N N . VAL B 1 25 ? 11.847 -27.211 -8.836 1.00 25.42 ? 25 VAL B N 1 ATOM 2237 C CA . VAL B 1 25 ? 11.600 -26.634 -10.151 1.00 26.49 ? 25 VAL B CA 1 ATOM 2238 C C . VAL B 1 25 ? 12.013 -27.573 -11.294 1.00 29.90 ? 25 VAL B C 1 ATOM 2239 O O . VAL B 1 25 ? 11.291 -27.689 -12.276 1.00 29.08 ? 25 VAL B O 1 ATOM 2240 C CB . VAL B 1 25 ? 12.277 -25.254 -10.287 1.00 27.29 ? 25 VAL B CB 1 ATOM 2241 C CG1 . VAL B 1 25 ? 12.168 -24.720 -11.721 1.00 28.17 ? 25 VAL B CG1 1 ATOM 2242 C CG2 . VAL B 1 25 ? 11.661 -24.291 -9.276 1.00 25.60 ? 25 VAL B CG2 1 ATOM 2243 N N . LYS B 1 26 ? 13.152 -28.254 -11.165 1.00 32.35 ? 26 LYS B N 1 ATOM 2244 C CA . LYS B 1 26 ? 13.551 -29.266 -12.158 1.00 37.36 ? 26 LYS B CA 1 ATOM 2245 C C . LYS B 1 26 ? 12.484 -30.341 -12.321 1.00 35.24 ? 26 LYS B C 1 ATOM 2246 O O . LYS B 1 26 ? 12.125 -30.697 -13.441 1.00 35.88 ? 26 LYS B O 1 ATOM 2247 C CB . LYS B 1 26 ? 14.875 -29.944 -11.764 1.00 40.50 ? 26 LYS B CB 1 ATOM 2248 C CG . LYS B 1 26 ? 15.276 -31.113 -12.661 1.00 41.85 ? 26 LYS B CG 1 ATOM 2249 C CD . LYS B 1 26 ? 14.847 -32.466 -12.068 1.00 44.07 ? 26 LYS B CD 1 ATOM 2250 C CE . LYS B 1 26 ? 15.349 -33.638 -12.893 1.00 42.61 ? 26 LYS B CE 1 ATOM 2251 N NZ . LYS B 1 26 ? 14.447 -33.924 -14.042 1.00 44.33 ? 26 LYS B NZ 1 ATOM 2252 N N . GLU B 1 27 ? 11.991 -30.863 -11.200 1.00 38.07 ? 27 GLU B N 1 ATOM 2253 C CA . GLU B 1 27 ? 11.002 -31.947 -11.238 1.00 39.90 ? 27 GLU B CA 1 ATOM 2254 C C . GLU B 1 27 ? 9.686 -31.507 -11.885 1.00 36.19 ? 27 GLU B C 1 ATOM 2255 O O . GLU B 1 27 ? 9.168 -32.178 -12.756 1.00 34.92 ? 27 GLU B O 1 ATOM 2256 C CB . GLU B 1 27 ? 10.766 -32.504 -9.843 1.00 45.64 ? 27 GLU B CB 1 ATOM 2257 C CG . GLU B 1 27 ? 11.992 -33.200 -9.271 1.00 54.06 ? 27 GLU B CG 1 ATOM 2258 C CD . GLU B 1 27 ? 11.750 -33.800 -7.892 1.00 63.75 ? 27 GLU B CD 1 ATOM 2259 O OE1 . GLU B 1 27 ? 11.279 -34.965 -7.830 1.00 66.34 ? 27 GLU B OE1 1 ATOM 2260 O OE2 . GLU B 1 27 ? 12.023 -33.102 -6.872 1.00 67.66 ? 27 GLU B OE2 1 ATOM 2261 N N . LEU B 1 28 ? 9.178 -30.354 -11.472 1.00 33.46 ? 28 LEU B N 1 ATOM 2262 C CA . LEU B 1 28 ? 7.924 -29.812 -12.017 1.00 30.12 ? 28 LEU B CA 1 ATOM 2263 C C . LEU B 1 28 ? 8.003 -29.385 -13.474 1.00 27.32 ? 28 LEU B C 1 ATOM 2264 O O . LEU B 1 28 ? 7.006 -29.399 -14.187 1.00 28.72 ? 28 LEU B O 1 ATOM 2265 C CB . LEU B 1 28 ? 7.475 -28.632 -11.164 1.00 29.44 ? 28 LEU B CB 1 ATOM 2266 C CG . LEU B 1 28 ? 7.076 -29.013 -9.747 1.00 29.67 ? 28 LEU B CG 1 ATOM 2267 C CD1 . LEU B 1 28 ? 6.827 -27.758 -8.936 1.00 31.05 ? 28 LEU B CD1 1 ATOM 2268 C CD2 . LEU B 1 28 ? 5.842 -29.915 -9.749 1.00 29.45 ? 28 LEU B CD2 1 ATOM 2269 N N . LEU B 1 29 ? 9.174 -28.994 -13.937 1.00 27.52 ? 29 LEU B N 1 ATOM 2270 C CA . LEU B 1 29 ? 9.288 -28.560 -15.314 1.00 28.90 ? 29 LEU B CA 1 ATOM 2271 C C . LEU B 1 29 ? 9.223 -29.780 -16.218 1.00 31.06 ? 29 LEU B C 1 ATOM 2272 O O . LEU B 1 29 ? 9.770 -30.818 -15.868 1.00 30.99 ? 29 LEU B O 1 ATOM 2273 C CB . LEU B 1 29 ? 10.602 -27.818 -15.537 1.00 29.66 ? 29 LEU B CB 1 ATOM 2274 C CG . LEU B 1 29 ? 10.661 -26.368 -15.015 1.00 30.31 ? 29 LEU B CG 1 ATOM 2275 C CD1 . LEU B 1 29 ? 12.064 -25.805 -15.194 1.00 28.29 ? 29 LEU B CD1 1 ATOM 2276 C CD2 . LEU B 1 29 ? 9.607 -25.501 -15.709 1.00 29.83 ? 29 LEU B CD2 1 ATOM 2277 N N . PRO B 1 30 ? 8.572 -29.660 -17.386 1.00 30.74 ? 30 PRO B N 1 ATOM 2278 C CA . PRO B 1 30 ? 8.619 -30.793 -18.299 1.00 31.83 ? 30 PRO B CA 1 ATOM 2279 C C . PRO B 1 30 ? 10.051 -31.032 -18.780 1.00 33.59 ? 30 PRO B C 1 ATOM 2280 O O . PRO B 1 30 ? 10.839 -30.084 -18.822 1.00 28.23 ? 30 PRO B O 1 ATOM 2281 C CB . PRO B 1 30 ? 7.713 -30.345 -19.455 1.00 31.30 ? 30 PRO B CB 1 ATOM 2282 C CG . PRO B 1 30 ? 7.743 -28.858 -19.402 1.00 31.02 ? 30 PRO B CG 1 ATOM 2283 C CD . PRO B 1 30 ? 7.783 -28.545 -17.939 1.00 30.90 ? 30 PRO B CD 1 ATOM 2284 N N . GLU B 1 31 ? 10.380 -32.280 -19.141 1.00 35.89 ? 31 GLU B N 1 ATOM 2285 C CA . GLU B 1 31 ? 11.736 -32.612 -19.610 1.00 38.65 ? 31 GLU B CA 1 ATOM 2286 C C . GLU B 1 31 ? 12.134 -31.755 -20.828 1.00 38.45 ? 31 GLU B C 1 ATOM 2287 O O . GLU B 1 31 ? 13.311 -31.430 -21.012 1.00 32.85 ? 31 GLU B O 1 ATOM 2288 C CB . GLU B 1 31 ? 11.885 -34.115 -19.929 1.00 40.97 ? 31 GLU B CB 1 ATOM 2289 C CG . GLU B 1 31 ? 10.970 -34.633 -21.035 1.00 44.94 ? 31 GLU B CG 1 ATOM 2290 C CD . GLU B 1 31 ? 11.480 -35.903 -21.722 1.00 48.05 ? 31 GLU B CD 1 ATOM 2291 O OE1 . GLU B 1 31 ? 11.982 -36.799 -21.017 1.00 50.07 ? 31 GLU B OE1 1 ATOM 2292 O OE2 . GLU B 1 31 ? 11.370 -36.002 -22.971 1.00 47.53 ? 31 GLU B OE2 1 ATOM 2293 N N . SER B 1 32 ? 11.143 -31.389 -21.642 1.00 39.64 ? 32 SER B N 1 ATOM 2294 C CA . SER B 1 32 ? 11.360 -30.534 -22.813 1.00 42.02 ? 32 SER B CA 1 ATOM 2295 C C . SER B 1 32 ? 11.956 -29.151 -22.491 1.00 43.97 ? 32 SER B C 1 ATOM 2296 O O . SER B 1 32 ? 12.577 -28.525 -23.356 1.00 43.05 ? 32 SER B O 1 ATOM 2297 C CB . SER B 1 32 ? 10.030 -30.345 -23.553 1.00 44.22 ? 32 SER B CB 1 ATOM 2298 O OG . SER B 1 32 ? 9.006 -30.015 -22.633 1.00 44.82 ? 32 SER B OG 1 ATOM 2299 N N . ALA B 1 33 ? 11.762 -28.669 -21.261 1.00 42.71 ? 33 ALA B N 1 ATOM 2300 C CA . ALA B 1 33 ? 12.331 -27.374 -20.841 1.00 41.63 ? 33 ALA B CA 1 ATOM 2301 C C . ALA B 1 33 ? 13.830 -27.446 -20.507 1.00 40.88 ? 33 ALA B C 1 ATOM 2302 O O . ALA B 1 33 ? 14.436 -26.423 -20.187 1.00 34.79 ? 33 ALA B O 1 ATOM 2303 C CB . ALA B 1 33 ? 11.553 -26.797 -19.660 1.00 37.22 ? 33 ALA B CB 1 ATOM 2304 N N . GLU B 1 34 ? 14.439 -28.631 -20.572 1.00 42.97 ? 34 GLU B N 1 ATOM 2305 C CA . GLU B 1 34 ? 15.877 -28.750 -20.282 1.00 43.91 ? 34 GLU B CA 1 ATOM 2306 C C . GLU B 1 34 ? 16.253 -28.093 -18.932 1.00 39.60 ? 34 GLU B C 1 ATOM 2307 O O . GLU B 1 34 ? 17.328 -27.530 -18.805 1.00 37.92 ? 34 GLU B O 1 ATOM 2308 C CB . GLU B 1 34 ? 16.718 -28.087 -21.396 1.00 45.62 ? 34 GLU B CB 1 ATOM 2309 C CG . GLU B 1 34 ? 16.356 -28.448 -22.836 1.00 49.76 ? 34 GLU B CG 1 ATOM 2310 C CD . GLU B 1 34 ? 17.231 -29.542 -23.450 1.00 55.45 ? 34 GLU B CD 1 ATOM 2311 O OE1 . GLU B 1 34 ? 18.407 -29.700 -23.041 1.00 55.32 ? 34 GLU B OE1 1 ATOM 2312 O OE2 . GLU B 1 34 ? 16.738 -30.245 -24.365 1.00 57.40 ? 34 GLU B OE2 1 ATOM 2313 N N . GLY B 1 35 ? 15.356 -28.145 -17.945 1.00 37.09 ? 35 GLY B N 1 ATOM 2314 C CA . GLY B 1 35 ? 15.590 -27.532 -16.617 1.00 32.32 ? 35 GLY B CA 1 ATOM 2315 C C . GLY B 1 35 ? 15.507 -25.997 -16.552 1.00 29.90 ? 35 GLY B C 1 ATOM 2316 O O . GLY B 1 35 ? 15.671 -25.419 -15.478 1.00 28.72 ? 35 GLY B O 1 ATOM 2317 N N . ASP B 1 36 ? 15.220 -25.344 -17.677 1.00 27.94 ? 36 ASP B N 1 ATOM 2318 C CA . ASP B 1 36 ? 15.261 -23.860 -17.784 1.00 29.87 ? 36 ASP B CA 1 ATOM 2319 C C . ASP B 1 36 ? 13.871 -23.223 -17.517 1.00 26.63 ? 36 ASP B C 1 ATOM 2320 O O . ASP B 1 36 ? 12.974 -23.316 -18.348 1.00 28.12 ? 36 ASP B O 1 ATOM 2321 C CB . ASP B 1 36 ? 15.793 -23.470 -19.177 1.00 28.87 ? 36 ASP B CB 1 ATOM 2322 C CG . ASP B 1 36 ? 15.992 -21.960 -19.349 1.00 33.18 ? 36 ASP B CG 1 ATOM 2323 O OD1 . ASP B 1 36 ? 15.831 -21.181 -18.371 1.00 34.78 ? 36 ASP B OD1 1 ATOM 2324 O OD2 . ASP B 1 36 ? 16.311 -21.550 -20.485 1.00 33.33 ? 36 ASP B OD2 1 ATOM 2325 N N . LEU B 1 37 ? 13.690 -22.595 -16.365 1.00 23.24 ? 37 LEU B N 1 ATOM 2326 C CA . LEU B 1 37 ? 12.416 -21.970 -16.060 1.00 23.53 ? 37 LEU B CA 1 ATOM 2327 C C . LEU B 1 37 ? 12.045 -20.957 -17.138 1.00 22.28 ? 37 LEU B C 1 ATOM 2328 O O . LEU B 1 37 ? 10.893 -20.922 -17.591 1.00 21.64 ? 37 LEU B O 1 ATOM 2329 C CB . LEU B 1 37 ? 12.447 -21.325 -14.670 1.00 24.25 ? 37 LEU B CB 1 ATOM 2330 C CG . LEU B 1 37 ? 11.185 -20.697 -14.082 1.00 25.26 ? 37 LEU B CG 1 ATOM 2331 C CD1 . LEU B 1 37 ? 9.970 -21.609 -14.204 1.00 27.30 ? 37 LEU B CD1 1 ATOM 2332 C CD2 . LEU B 1 37 ? 11.414 -20.311 -12.631 1.00 24.78 ? 37 LEU B CD2 1 ATOM 2333 N N . SER B 1 38 ? 13.015 -20.152 -17.571 1.00 22.58 ? 38 SER B N 1 ATOM 2334 C CA . SER B 1 38 ? 12.784 -19.100 -18.589 1.00 21.58 ? 38 SER B CA 1 ATOM 2335 C C . SER B 1 38 ? 12.232 -19.586 -19.932 1.00 23.10 ? 38 SER B C 1 ATOM 2336 O O . SER B 1 38 ? 11.591 -18.823 -20.617 1.00 22.65 ? 38 SER B O 1 ATOM 2337 C CB . SER B 1 38 ? 14.031 -18.244 -18.833 1.00 22.08 ? 38 SER B CB 1 ATOM 2338 O OG . SER B 1 38 ? 15.094 -18.959 -19.428 1.00 19.98 ? 38 SER B OG 1 ATOM 2339 N N . SER B 1 39 ? 12.425 -20.856 -20.288 1.00 25.25 ? 39 SER B N 1 ATOM 2340 C CA . SER B 1 39 ? 11.891 -21.356 -21.536 1.00 27.14 ? 39 SER B CA 1 ATOM 2341 C C . SER B 1 39 ? 10.344 -21.410 -21.552 1.00 26.59 ? 39 SER B C 1 ATOM 2342 O O . SER B 1 39 ? 9.741 -21.481 -22.613 1.00 26.74 ? 39 SER B O 1 ATOM 2343 C CB . SER B 1 39 ? 12.444 -22.755 -21.832 1.00 29.52 ? 39 SER B CB 1 ATOM 2344 O OG . SER B 1 39 ? 11.846 -23.704 -20.958 1.00 31.50 ? 39 SER B OG 1 ATOM 2345 N N . LEU B 1 40 ? 9.706 -21.395 -20.388 1.00 25.08 ? 40 LEU B N 1 ATOM 2346 C CA . LEU B 1 40 ? 8.258 -21.511 -20.321 1.00 25.21 ? 40 LEU B CA 1 ATOM 2347 C C . LEU B 1 40 ? 7.554 -20.391 -19.544 1.00 24.93 ? 40 LEU B C 1 ATOM 2348 O O . LEU B 1 40 ? 6.372 -20.493 -19.238 1.00 25.66 ? 40 LEU B O 1 ATOM 2349 C CB . LEU B 1 40 ? 7.896 -22.842 -19.704 1.00 24.69 ? 40 LEU B CB 1 ATOM 2350 C CG . LEU B 1 40 ? 8.149 -24.029 -20.606 1.00 26.43 ? 40 LEU B CG 1 ATOM 2351 C CD1 . LEU B 1 40 ? 8.052 -25.293 -19.748 1.00 27.14 ? 40 LEU B CD1 1 ATOM 2352 C CD2 . LEU B 1 40 ? 7.165 -24.041 -21.775 1.00 26.23 ? 40 LEU B CD2 1 ATOM 2353 N N . CYS B 1 41 ? 8.251 -19.316 -19.224 1.00 27.38 ? 41 CYS B N 1 ATOM 2354 C CA . CYS B 1 41 ? 7.605 -18.240 -18.458 1.00 27.58 ? 41 CYS B CA 1 ATOM 2355 C C . CYS B 1 41 ? 6.640 -17.421 -19.327 1.00 23.51 ? 41 CYS B C 1 ATOM 2356 O O . CYS B 1 41 ? 5.912 -16.587 -18.798 1.00 25.08 ? 41 CYS B O 1 ATOM 2357 C CB . CYS B 1 41 ? 8.630 -17.352 -17.711 1.00 29.98 ? 41 CYS B CB 1 ATOM 2358 S SG . CYS B 1 41 ? 9.393 -18.238 -16.323 1.00 36.75 ? 41 CYS B SG 1 ATOM 2359 N N . LEU B 1 42 ? 6.591 -17.667 -20.634 1.00 22.27 ? 42 LEU B N 1 ATOM 2360 C CA . LEU B 1 42 ? 5.516 -17.077 -21.467 1.00 22.55 ? 42 LEU B CA 1 ATOM 2361 C C . LEU B 1 42 ? 4.283 -17.941 -21.633 1.00 22.21 ? 42 LEU B C 1 ATOM 2362 O O . LEU B 1 42 ? 3.296 -17.486 -22.199 1.00 22.75 ? 42 LEU B O 1 ATOM 2363 C CB . LEU B 1 42 ? 6.024 -16.668 -22.849 1.00 22.46 ? 42 LEU B CB 1 ATOM 2364 C CG . LEU B 1 42 ? 5.377 -15.392 -23.394 1.00 22.89 ? 42 LEU B CG 1 ATOM 2365 C CD1 . LEU B 1 42 ? 5.649 -14.194 -22.474 1.00 22.78 ? 42 LEU B CD1 1 ATOM 2366 C CD2 . LEU B 1 42 ? 5.858 -15.107 -24.807 1.00 22.61 ? 42 LEU B CD2 1 ATOM 2367 N N . TRP B 1 43 ? 4.345 -19.188 -21.162 1.00 22.52 ? 43 TRP B N 1 ATOM 2368 C CA . TRP B 1 43 ? 3.281 -20.175 -21.388 1.00 22.54 ? 43 TRP B CA 1 ATOM 2369 C C . TRP B 1 43 ? 1.861 -19.674 -21.031 1.00 21.51 ? 43 TRP B C 1 ATOM 2370 O O . TRP B 1 43 ? 0.903 -19.908 -21.771 1.00 22.06 ? 43 TRP B O 1 ATOM 2371 C CB . TRP B 1 43 ? 3.605 -21.443 -20.584 1.00 23.63 ? 43 TRP B CB 1 ATOM 2372 C CG . TRP B 1 43 ? 2.487 -22.418 -20.531 1.00 24.26 ? 43 TRP B CG 1 ATOM 2373 C CD1 . TRP B 1 43 ? 2.201 -23.387 -21.444 1.00 26.11 ? 43 TRP B CD1 1 ATOM 2374 C CD2 . TRP B 1 43 ? 1.503 -22.516 -19.509 1.00 24.49 ? 43 TRP B CD2 1 ATOM 2375 N NE1 . TRP B 1 43 ? 1.070 -24.070 -21.063 1.00 26.42 ? 43 TRP B NE1 1 ATOM 2376 C CE2 . TRP B 1 43 ? 0.637 -23.560 -19.863 1.00 25.75 ? 43 TRP B CE2 1 ATOM 2377 C CE3 . TRP B 1 43 ? 1.262 -21.808 -18.318 1.00 25.50 ? 43 TRP B CE3 1 ATOM 2378 C CZ2 . TRP B 1 43 ? -0.444 -23.930 -19.065 1.00 25.11 ? 43 TRP B CZ2 1 ATOM 2379 C CZ3 . TRP B 1 43 ? 0.192 -22.175 -17.534 1.00 24.74 ? 43 TRP B CZ3 1 ATOM 2380 C CH2 . TRP B 1 43 ? -0.648 -23.228 -17.913 1.00 25.24 ? 43 TRP B CH2 1 ATOM 2381 N N . ALA B 1 44 ? 1.719 -18.990 -19.900 1.00 20.41 ? 44 ALA B N 1 ATOM 2382 C CA . ALA B 1 44 ? 0.410 -18.472 -19.493 1.00 19.37 ? 44 ALA B CA 1 ATOM 2383 C C . ALA B 1 44 ? -0.223 -17.466 -20.488 1.00 19.42 ? 44 ALA B C 1 ATOM 2384 O O . ALA B 1 44 ? -1.475 -17.401 -20.601 1.00 18.77 ? 44 ALA B O 1 ATOM 2385 C CB . ALA B 1 44 ? 0.481 -17.871 -18.114 1.00 19.42 ? 44 ALA B CB 1 ATOM 2386 N N . ASP B 1 45 ? 0.589 -16.671 -21.187 1.00 19.03 ? 45 ASP B N 1 ATOM 2387 C CA . ASP B 1 45 ? 0.029 -15.766 -22.231 1.00 20.32 ? 45 ASP B CA 1 ATOM 2388 C C . ASP B 1 45 ? -0.534 -16.575 -23.436 1.00 22.21 ? 45 ASP B C 1 ATOM 2389 O O . ASP B 1 45 ? -1.320 -16.055 -24.231 1.00 22.87 ? 45 ASP B O 1 ATOM 2390 C CB . ASP B 1 45 ? 1.054 -14.780 -22.766 1.00 19.22 ? 45 ASP B CB 1 ATOM 2391 C CG . ASP B 1 45 ? 1.256 -13.562 -21.879 1.00 18.86 ? 45 ASP B CG 1 ATOM 2392 O OD1 . ASP B 1 45 ? 0.403 -13.237 -21.013 1.00 17.13 ? 45 ASP B OD1 1 ATOM 2393 O OD2 . ASP B 1 45 ? 2.306 -12.927 -22.089 1.00 17.33 ? 45 ASP B OD2 1 ATOM 2394 N N . ARG B 1 46 ? -0.122 -17.831 -23.550 1.00 25.07 ? 46 ARG B N 1 ATOM 2395 C CA . ARG B 1 46 ? -0.575 -18.715 -24.627 1.00 30.68 ? 46 ARG B CA 1 ATOM 2396 C C . ARG B 1 46 ? -1.899 -19.442 -24.308 1.00 29.84 ? 46 ARG B C 1 ATOM 2397 O O . ARG B 1 46 ? -2.493 -20.031 -25.206 1.00 30.76 ? 46 ARG B O 1 ATOM 2398 C CB . ARG B 1 46 ? 0.510 -19.758 -24.973 1.00 35.22 ? 46 ARG B CB 1 ATOM 2399 C CG . ARG B 1 46 ? 1.472 -19.370 -26.093 1.00 40.55 ? 46 ARG B CG 1 ATOM 2400 C CD . ARG B 1 46 ? 2.555 -20.434 -26.358 1.00 47.78 ? 46 ARG B CD 1 ATOM 2401 N NE . ARG B 1 46 ? 2.114 -21.834 -26.173 1.00 54.47 ? 46 ARG B NE 1 ATOM 2402 C CZ . ARG B 1 46 ? 2.853 -22.921 -26.433 1.00 58.06 ? 46 ARG B CZ 1 ATOM 2403 N NH1 . ARG B 1 46 ? 4.087 -22.831 -26.936 1.00 58.02 ? 46 ARG B NH1 1 ATOM 2404 N NH2 . ARG B 1 46 ? 2.333 -24.122 -26.205 1.00 60.36 ? 46 ARG B NH2 1 ATOM 2405 N N . VAL B 1 47 ? -2.360 -19.406 -23.056 1.00 27.33 ? 47 VAL B N 1 ATOM 2406 C CA . VAL B 1 47 ? -3.567 -20.159 -22.676 1.00 26.80 ? 47 VAL B CA 1 ATOM 2407 C C . VAL B 1 47 ? -4.718 -19.274 -22.204 1.00 26.29 ? 47 VAL B C 1 ATOM 2408 O O . VAL B 1 47 ? -5.575 -19.720 -21.466 1.00 28.70 ? 47 VAL B O 1 ATOM 2409 C CB . VAL B 1 47 ? -3.260 -21.260 -21.624 1.00 26.55 ? 47 VAL B CB 1 ATOM 2410 C CG1 . VAL B 1 47 ? -2.252 -22.255 -22.183 1.00 26.57 ? 47 VAL B CG1 1 ATOM 2411 C CG2 . VAL B 1 47 ? -2.777 -20.678 -20.310 1.00 26.70 ? 47 VAL B CG2 1 ATOM 2412 N N . LYS B 1 48 ? -4.756 -18.025 -22.654 1.00 28.49 ? 48 LYS B N 1 ATOM 2413 C CA . LYS B 1 48 ? -5.826 -17.092 -22.259 1.00 28.76 ? 48 LYS B CA 1 ATOM 2414 C C . LYS B 1 48 ? -7.205 -17.416 -22.866 1.00 26.99 ? 48 LYS B C 1 ATOM 2415 O O . LYS B 1 48 ? -8.199 -16.933 -22.357 1.00 26.42 ? 48 LYS B O 1 ATOM 2416 C CB . LYS B 1 48 ? -5.450 -15.640 -22.593 1.00 30.19 ? 48 LYS B CB 1 ATOM 2417 C CG . LYS B 1 48 ? -4.327 -15.046 -21.759 1.00 31.00 ? 48 LYS B CG 1 ATOM 2418 C CD . LYS B 1 48 ? -4.193 -13.578 -22.132 1.00 32.52 ? 48 LYS B CD 1 ATOM 2419 C CE . LYS B 1 48 ? -2.894 -12.948 -21.691 1.00 31.66 ? 48 LYS B CE 1 ATOM 2420 N NZ . LYS B 1 48 ? -2.748 -11.641 -22.397 1.00 32.34 ? 48 LYS B NZ 1 ATOM 2421 N N . PHE B 1 49 ? -7.234 -18.202 -23.946 1.00 25.62 ? 49 PHE B N 1 ATOM 2422 C CA . PHE B 1 49 ? -8.459 -18.718 -24.556 1.00 27.53 ? 49 PHE B CA 1 ATOM 2423 C C . PHE B 1 49 ? -8.624 -20.238 -24.408 1.00 26.98 ? 49 PHE B C 1 ATOM 2424 O O . PHE B 1 49 ? -9.745 -20.745 -24.287 1.00 24.27 ? 49 PHE B O 1 ATOM 2425 C CB . PHE B 1 49 ? -8.530 -18.290 -26.024 1.00 28.05 ? 49 PHE B CB 1 ATOM 2426 C CG . PHE B 1 49 ? -8.709 -16.805 -26.184 1.00 29.11 ? 49 PHE B CG 1 ATOM 2427 C CD1 . PHE B 1 49 ? -9.969 -16.240 -26.161 1.00 30.12 ? 49 PHE B CD1 1 ATOM 2428 C CD2 . PHE B 1 49 ? -7.613 -15.975 -26.302 1.00 29.35 ? 49 PHE B CD2 1 ATOM 2429 C CE1 . PHE B 1 49 ? -10.135 -14.862 -26.268 1.00 29.84 ? 49 PHE B CE1 1 ATOM 2430 C CE2 . PHE B 1 49 ? -7.770 -14.601 -26.427 1.00 30.77 ? 49 PHE B CE2 1 ATOM 2431 C CZ . PHE B 1 49 ? -9.033 -14.043 -26.392 1.00 29.81 ? 49 PHE B CZ 1 ATOM 2432 N N . ARG B 1 50 ? -7.511 -20.956 -24.382 1.00 26.66 ? 50 ARG B N 1 ATOM 2433 C CA . ARG B 1 50 ? -7.526 -22.351 -23.952 1.00 28.88 ? 50 ARG B CA 1 ATOM 2434 C C . ARG B 1 50 ? -8.214 -22.451 -22.584 1.00 26.93 ? 50 ARG B C 1 ATOM 2435 O O . ARG B 1 50 ? -9.118 -23.258 -22.376 1.00 27.09 ? 50 ARG B O 1 ATOM 2436 C CB . ARG B 1 50 ? -6.092 -22.867 -23.856 1.00 31.02 ? 50 ARG B CB 1 ATOM 2437 C CG . ARG B 1 50 ? -5.943 -24.374 -23.773 1.00 33.96 ? 50 ARG B CG 1 ATOM 2438 C CD . ARG B 1 50 ? -4.549 -24.799 -24.253 1.00 37.10 ? 50 ARG B CD 1 ATOM 2439 N NE . ARG B 1 50 ? -4.645 -25.918 -25.192 1.00 41.44 ? 50 ARG B NE 1 ATOM 2440 C CZ . ARG B 1 50 ? -3.762 -26.202 -26.149 1.00 44.32 ? 50 ARG B CZ 1 ATOM 2441 N NH1 . ARG B 1 50 ? -2.678 -25.448 -26.333 1.00 47.78 ? 50 ARG B NH1 1 ATOM 2442 N NH2 . ARG B 1 50 ? -3.967 -27.259 -26.932 1.00 45.80 ? 50 ARG B NH2 1 ATOM 2443 N N . TYR B 1 51 ? -7.779 -21.597 -21.669 1.00 25.25 ? 51 TYR B N 1 ATOM 2444 C CA . TYR B 1 51 ? -8.321 -21.501 -20.340 1.00 23.76 ? 51 TYR B CA 1 ATOM 2445 C C . TYR B 1 51 ? -8.848 -20.068 -20.150 1.00 24.62 ? 51 TYR B C 1 ATOM 2446 O O . TYR B 1 51 ? -8.214 -19.236 -19.522 1.00 23.82 ? 51 TYR B O 1 ATOM 2447 C CB . TYR B 1 51 ? -7.197 -21.757 -19.337 1.00 25.72 ? 51 TYR B CB 1 ATOM 2448 C CG . TYR B 1 51 ? -6.519 -23.127 -19.331 1.00 27.41 ? 51 TYR B CG 1 ATOM 2449 C CD1 . TYR B 1 51 ? -7.227 -24.298 -19.583 1.00 28.42 ? 51 TYR B CD1 1 ATOM 2450 C CD2 . TYR B 1 51 ? -5.164 -23.248 -18.976 1.00 28.82 ? 51 TYR B CD2 1 ATOM 2451 C CE1 . TYR B 1 51 ? -6.605 -25.551 -19.526 1.00 29.34 ? 51 TYR B CE1 1 ATOM 2452 C CE2 . TYR B 1 51 ? -4.533 -24.487 -18.915 1.00 29.34 ? 51 TYR B CE2 1 ATOM 2453 C CZ . TYR B 1 51 ? -5.259 -25.647 -19.192 1.00 30.68 ? 51 TYR B CZ 1 ATOM 2454 O OH . TYR B 1 51 ? -4.649 -26.902 -19.137 1.00 28.74 ? 51 TYR B OH 1 ATOM 2455 N N . HIS B 1 52 ? -10.023 -19.784 -20.688 1.00 24.37 ? 52 HIS B N 1 ATOM 2456 C CA . HIS B 1 52 ? -10.531 -18.431 -20.747 1.00 23.44 ? 52 HIS B CA 1 ATOM 2457 C C . HIS B 1 52 ? -10.656 -17.837 -19.371 1.00 23.44 ? 52 HIS B C 1 ATOM 2458 O O . HIS B 1 52 ? -10.657 -16.624 -19.230 1.00 21.16 ? 52 HIS B O 1 ATOM 2459 C CB . HIS B 1 52 ? -11.919 -18.399 -21.411 1.00 23.41 ? 52 HIS B CB 1 ATOM 2460 C CG . HIS B 1 52 ? -13.000 -18.820 -20.486 1.00 24.28 ? 52 HIS B CG 1 ATOM 2461 N ND1 . HIS B 1 52 ? -13.206 -20.136 -20.152 1.00 25.75 ? 52 HIS B ND1 1 ATOM 2462 C CD2 . HIS B 1 52 ? -13.866 -18.095 -19.736 1.00 26.37 ? 52 HIS B CD2 1 ATOM 2463 C CE1 . HIS B 1 52 ? -14.190 -20.216 -19.273 1.00 27.67 ? 52 HIS B CE1 1 ATOM 2464 N NE2 . HIS B 1 52 ? -14.600 -18.991 -18.996 1.00 27.12 ? 52 HIS B NE2 1 ATOM 2465 N N . TRP B 1 53 ? -10.852 -18.695 -18.376 1.00 22.00 ? 53 TRP B N 1 ATOM 2466 C CA . TRP B 1 53 ? -10.929 -18.291 -16.983 1.00 22.55 ? 53 TRP B CA 1 ATOM 2467 C C . TRP B 1 53 ? -9.620 -17.632 -16.477 1.00 21.63 ? 53 TRP B C 1 ATOM 2468 O O . TRP B 1 53 ? -9.633 -16.872 -15.467 1.00 20.41 ? 53 TRP B O 1 ATOM 2469 C CB . TRP B 1 53 ? -11.326 -19.498 -16.100 1.00 23.04 ? 53 TRP B CB 1 ATOM 2470 C CG . TRP B 1 53 ? -10.561 -20.808 -16.360 1.00 22.44 ? 53 TRP B CG 1 ATOM 2471 C CD1 . TRP B 1 53 ? -11.009 -21.885 -17.034 1.00 23.24 ? 53 TRP B CD1 1 ATOM 2472 C CD2 . TRP B 1 53 ? -9.249 -21.146 -15.897 1.00 23.52 ? 53 TRP B CD2 1 ATOM 2473 N NE1 . TRP B 1 53 ? -10.064 -22.875 -17.053 1.00 22.40 ? 53 TRP B NE1 1 ATOM 2474 C CE2 . TRP B 1 53 ? -8.964 -22.440 -16.360 1.00 24.27 ? 53 TRP B CE2 1 ATOM 2475 C CE3 . TRP B 1 53 ? -8.291 -20.483 -15.135 1.00 23.35 ? 53 TRP B CE3 1 ATOM 2476 C CZ2 . TRP B 1 53 ? -7.747 -23.074 -16.101 1.00 22.57 ? 53 TRP B CZ2 1 ATOM 2477 C CZ3 . TRP B 1 53 ? -7.094 -21.117 -14.873 1.00 23.43 ? 53 TRP B CZ3 1 ATOM 2478 C CH2 . TRP B 1 53 ? -6.836 -22.399 -15.347 1.00 24.09 ? 53 TRP B CH2 1 ATOM 2479 N N . SER B 1 54 ? -8.515 -17.929 -17.173 1.00 20.69 ? 54 SER B N 1 ATOM 2480 C CA . SER B 1 54 ? -7.157 -17.437 -16.817 1.00 20.65 ? 54 SER B CA 1 ATOM 2481 C C . SER B 1 54 ? -6.828 -15.986 -17.208 1.00 20.76 ? 54 SER B C 1 ATOM 2482 O O . SER B 1 54 ? -5.910 -15.385 -16.648 1.00 21.43 ? 54 SER B O 1 ATOM 2483 C CB . SER B 1 54 ? -6.074 -18.377 -17.418 1.00 20.18 ? 54 SER B CB 1 ATOM 2484 O OG . SER B 1 54 ? -5.903 -18.224 -18.828 1.00 18.89 ? 54 SER B OG 1 ATOM 2485 N N . SER B 1 55 ? -7.561 -15.442 -18.182 1.00 21.52 ? 55 SER B N 1 ATOM 2486 C CA . SER B 1 55 ? -7.259 -14.148 -18.778 1.00 20.58 ? 55 SER B CA 1 ATOM 2487 C C . SER B 1 55 ? -7.227 -13.006 -17.809 1.00 19.16 ? 55 SER B C 1 ATOM 2488 O O . SER B 1 55 ? -6.343 -12.141 -17.909 1.00 20.65 ? 55 SER B O 1 ATOM 2489 C CB . SER B 1 55 ? -8.278 -13.801 -19.900 1.00 22.85 ? 55 SER B CB 1 ATOM 2490 O OG . SER B 1 55 ? -7.878 -14.366 -21.123 1.00 27.66 ? 55 SER B OG 1 ATOM 2491 N N . PRO B 1 56 ? -8.226 -12.926 -16.914 1.00 19.35 ? 56 PRO B N 1 ATOM 2492 C CA . PRO B 1 56 ? -8.231 -11.863 -15.899 1.00 17.24 ? 56 PRO B CA 1 ATOM 2493 C C . PRO B 1 56 ? -7.099 -11.910 -14.857 1.00 16.89 ? 56 PRO B C 1 ATOM 2494 O O . PRO B 1 56 ? -6.933 -10.988 -14.008 1.00 16.81 ? 56 PRO B O 1 ATOM 2495 C CB . PRO B 1 56 ? -9.564 -12.058 -15.187 1.00 18.63 ? 56 PRO B CB 1 ATOM 2496 C CG . PRO B 1 56 ? -10.426 -12.827 -16.116 1.00 20.39 ? 56 PRO B CG 1 ATOM 2497 C CD . PRO B 1 56 ? -9.516 -13.667 -16.967 1.00 19.84 ? 56 PRO B CD 1 ATOM 2498 N N . LEU B 1 57 ? -6.346 -12.987 -14.869 1.00 17.06 ? 57 LEU B N 1 ATOM 2499 C CA . LEU B 1 57 ? -5.394 -13.257 -13.803 1.00 16.56 ? 57 LEU B CA 1 ATOM 2500 C C . LEU B 1 57 ? -4.076 -12.553 -14.077 1.00 17.06 ? 57 LEU B C 1 ATOM 2501 O O . LEU B 1 57 ? -3.207 -12.510 -13.211 1.00 18.45 ? 57 LEU B O 1 ATOM 2502 C CB . LEU B 1 57 ? -5.202 -14.764 -13.685 1.00 15.82 ? 57 LEU B CB 1 ATOM 2503 C CG . LEU B 1 57 ? -6.527 -15.492 -13.387 1.00 15.05 ? 57 LEU B CG 1 ATOM 2504 C CD1 . LEU B 1 57 ? -6.354 -16.989 -13.383 1.00 14.30 ? 57 LEU B CD1 1 ATOM 2505 C CD2 . LEU B 1 57 ? -7.111 -15.057 -12.049 1.00 15.64 ? 57 LEU B CD2 1 ATOM 2506 N N . HIS B 1 58 ? -3.953 -11.963 -15.262 1.00 15.64 ? 58 HIS B N 1 ATOM 2507 C CA . HIS B 1 58 ? -2.721 -11.317 -15.666 1.00 16.27 ? 58 HIS B CA 1 ATOM 2508 C C . HIS B 1 58 ? -2.604 -9.865 -15.220 1.00 15.67 ? 58 HIS B C 1 ATOM 2509 O O . HIS B 1 58 ? -1.524 -9.310 -15.340 1.00 15.75 ? 58 HIS B O 1 ATOM 2510 C CB . HIS B 1 58 ? -2.565 -11.361 -17.165 1.00 16.56 ? 58 HIS B CB 1 ATOM 2511 C CG . HIS B 1 58 ? -2.461 -12.746 -17.702 1.00 16.84 ? 58 HIS B CG 1 ATOM 2512 N ND1 . HIS B 1 58 ? -1.329 -13.214 -18.302 1.00 17.38 ? 58 HIS B ND1 1 ATOM 2513 C CD2 . HIS B 1 58 ? -3.332 -13.783 -17.677 1.00 17.54 ? 58 HIS B CD2 1 ATOM 2514 C CE1 . HIS B 1 58 ? -1.503 -14.478 -18.653 1.00 17.16 ? 58 HIS B CE1 1 ATOM 2515 N NE2 . HIS B 1 58 ? -2.718 -14.843 -18.288 1.00 17.26 ? 58 HIS B NE2 1 ATOM 2516 N N . TYR B 1 59 ? -3.665 -9.286 -14.659 1.00 15.65 ? 59 TYR B N 1 ATOM 2517 C CA . TYR B 1 59 ? -3.668 -7.837 -14.365 1.00 16.16 ? 59 TYR B CA 1 ATOM 2518 C C . TYR B 1 59 ? -4.612 -7.439 -13.244 1.00 16.05 ? 59 TYR B C 1 ATOM 2519 O O . TYR B 1 59 ? -5.308 -8.263 -12.678 1.00 16.03 ? 59 TYR B O 1 ATOM 2520 C CB . TYR B 1 59 ? -3.982 -7.052 -15.634 1.00 16.25 ? 59 TYR B CB 1 ATOM 2521 C CG . TYR B 1 59 ? -5.289 -7.444 -16.221 1.00 17.86 ? 59 TYR B CG 1 ATOM 2522 C CD1 . TYR B 1 59 ? -6.478 -6.937 -15.706 1.00 17.83 ? 59 TYR B CD1 1 ATOM 2523 C CD2 . TYR B 1 59 ? -5.360 -8.401 -17.242 1.00 19.16 ? 59 TYR B CD2 1 ATOM 2524 C CE1 . TYR B 1 59 ? -7.693 -7.317 -16.227 1.00 19.28 ? 59 TYR B CE1 1 ATOM 2525 C CE2 . TYR B 1 59 ? -6.579 -8.801 -17.763 1.00 20.34 ? 59 TYR B CE2 1 ATOM 2526 C CZ . TYR B 1 59 ? -7.743 -8.256 -17.240 1.00 20.10 ? 59 TYR B CZ 1 ATOM 2527 O OH . TYR B 1 59 ? -8.962 -8.636 -17.730 1.00 25.29 ? 59 TYR B OH 1 ATOM 2528 N N . ILE B 1 60 ? -4.544 -6.171 -12.878 1.00 17.51 ? 60 ILE B N 1 ATOM 2529 C CA . ILE B 1 60 ? -5.445 -5.562 -11.926 1.00 18.41 ? 60 ILE B CA 1 ATOM 2530 C C . ILE B 1 60 ? -5.857 -4.228 -12.556 1.00 18.31 ? 60 ILE B C 1 ATOM 2531 O O . ILE B 1 60 ? -5.035 -3.471 -13.072 1.00 18.91 ? 60 ILE B O 1 ATOM 2532 C CB . ILE B 1 60 ? -4.751 -5.288 -10.550 1.00 17.70 ? 60 ILE B CB 1 ATOM 2533 C CG1 . ILE B 1 60 ? -4.548 -6.554 -9.771 1.00 16.66 ? 60 ILE B CG1 1 ATOM 2534 C CG2 . ILE B 1 60 ? -5.575 -4.351 -9.690 1.00 17.84 ? 60 ILE B CG2 1 ATOM 2535 C CD1 . ILE B 1 60 ? -3.455 -6.478 -8.727 1.00 16.63 ? 60 ILE B CD1 1 ATOM 2536 N N . ASN B 1 61 ? -7.146 -3.982 -12.498 1.00 21.15 ? 61 ASN B N 1 ATOM 2537 C CA . ASN B 1 61 ? -7.781 -2.761 -12.912 1.00 24.67 ? 61 ASN B CA 1 ATOM 2538 C C . ASN B 1 61 ? -8.147 -1.964 -11.677 1.00 24.73 ? 61 ASN B C 1 ATOM 2539 O O . ASN B 1 61 ? -8.766 -2.491 -10.744 1.00 24.48 ? 61 ASN B O 1 ATOM 2540 C CB . ASN B 1 61 ? -9.088 -3.080 -13.629 1.00 26.58 ? 61 ASN B CB 1 ATOM 2541 C CG . ASN B 1 61 ? -8.897 -3.334 -15.088 1.00 29.34 ? 61 ASN B CG 1 ATOM 2542 O OD1 . ASN B 1 61 ? -9.589 -4.166 -15.670 1.00 35.24 ? 61 ASN B OD1 1 ATOM 2543 N ND2 . ASN B 1 61 ? -7.955 -2.636 -15.698 1.00 31.74 ? 61 ASN B ND2 1 ATOM 2544 N N . THR B 1 62 ? -7.746 -0.711 -11.667 1.00 25.89 ? 62 THR B N 1 ATOM 2545 C CA . THR B 1 62 ? -8.112 0.213 -10.601 1.00 25.38 ? 62 THR B CA 1 ATOM 2546 C C . THR B 1 62 ? -8.965 1.359 -11.167 1.00 26.54 ? 62 THR B C 1 ATOM 2547 O O . THR B 1 62 ? -9.080 1.517 -12.409 1.00 22.95 ? 62 THR B O 1 ATOM 2548 C CB . THR B 1 62 ? -6.852 0.788 -9.961 1.00 27.48 ? 62 THR B CB 1 ATOM 2549 O OG1 . THR B 1 62 ? -6.204 1.663 -10.895 1.00 29.11 ? 62 THR B OG1 1 ATOM 2550 C CG2 . THR B 1 62 ? -5.889 -0.345 -9.598 1.00 28.66 ? 62 THR B CG2 1 ATOM 2551 N N . PRO B 1 63 ? -9.596 2.155 -10.260 1.00 28.70 ? 63 PRO B N 1 ATOM 2552 C CA . PRO B 1 63 ? -10.205 3.433 -10.662 1.00 30.30 ? 63 PRO B CA 1 ATOM 2553 C C . PRO B 1 63 ? -9.123 4.395 -11.141 1.00 30.11 ? 63 PRO B C 1 ATOM 2554 O O . PRO B 1 63 ? -7.942 4.067 -11.039 1.00 27.42 ? 63 PRO B O 1 ATOM 2555 C CB . PRO B 1 63 ? -10.802 3.981 -9.344 1.00 31.17 ? 63 PRO B CB 1 ATOM 2556 C CG . PRO B 1 63 ? -10.966 2.795 -8.463 1.00 31.16 ? 63 PRO B CG 1 ATOM 2557 C CD . PRO B 1 63 ? -9.876 1.828 -8.849 1.00 28.94 ? 63 PRO B CD 1 ATOM 2558 N N . ASP B 1 64 ? -9.504 5.591 -11.585 1.00 32.54 ? 64 ASP B N 1 ATOM 2559 C CA . ASP B 1 64 ? -8.525 6.590 -11.993 1.00 34.53 ? 64 ASP B CA 1 ATOM 2560 C C . ASP B 1 64 ? -7.848 7.222 -10.787 1.00 37.90 ? 64 ASP B C 1 ATOM 2561 O O . ASP B 1 64 ? -7.963 8.426 -10.555 1.00 40.11 ? 64 ASP B O 1 ATOM 2562 C CB . ASP B 1 64 ? -9.174 7.686 -12.827 1.00 36.97 ? 64 ASP B CB 1 ATOM 2563 C CG . ASP B 1 64 ? -9.619 7.209 -14.183 1.00 38.68 ? 64 ASP B CG 1 ATOM 2564 O OD1 . ASP B 1 64 ? -9.228 6.096 -14.601 1.00 40.02 ? 64 ASP B OD1 1 ATOM 2565 O OD2 . ASP B 1 64 ? -10.374 7.964 -14.834 1.00 42.79 ? 64 ASP B OD2 1 ATOM 2566 N N . ALA B 1 65 ? -7.127 6.416 -10.025 1.00 38.38 ? 65 ALA B N 1 ATOM 2567 C CA . ALA B 1 65 ? -6.388 6.915 -8.875 1.00 39.03 ? 65 ALA B CA 1 ATOM 2568 C C . ALA B 1 65 ? -5.162 6.047 -8.647 1.00 36.75 ? 65 ALA B C 1 ATOM 2569 O O . ALA B 1 65 ? -5.115 4.897 -9.073 1.00 40.24 ? 65 ALA B O 1 ATOM 2570 C CB . ALA B 1 65 ? -7.280 6.921 -7.636 1.00 40.42 ? 65 ALA B CB 1 ATOM 2571 N N . CYS B 1 66 ? -4.194 6.598 -7.936 1.00 34.29 ? 66 CYS B N 1 ATOM 2572 C CA . CYS B 1 66 ? -2.901 5.968 -7.746 1.00 33.69 ? 66 CYS B CA 1 ATOM 2573 C C . CYS B 1 66 ? -2.868 5.190 -6.443 1.00 34.29 ? 66 CYS B C 1 ATOM 2574 O O . CYS B 1 66 ? -2.076 5.477 -5.554 1.00 35.84 ? 66 CYS B O 1 ATOM 2575 C CB . CYS B 1 66 ? -1.817 7.040 -7.761 1.00 34.76 ? 66 CYS B CB 1 ATOM 2576 S SG . CYS B 1 66 ? -1.916 8.036 -9.262 1.00 38.92 ? 66 CYS B SG 1 ATOM 2577 N N . SER B 1 67 ? -3.745 4.204 -6.338 1.00 30.48 ? 67 SER B N 1 ATOM 2578 C CA . SER B 1 67 ? -3.806 3.361 -5.166 1.00 29.55 ? 67 SER B CA 1 ATOM 2579 C C . SER B 1 67 ? -4.468 2.060 -5.560 1.00 25.38 ? 67 SER B C 1 ATOM 2580 O O . SER B 1 67 ? -5.305 2.030 -6.441 1.00 26.64 ? 67 SER B O 1 ATOM 2581 C CB . SER B 1 67 ? -4.616 4.029 -4.054 1.00 30.74 ? 67 SER B CB 1 ATOM 2582 O OG . SER B 1 67 ? -6.011 3.828 -4.231 1.00 30.79 ? 67 SER B OG 1 ATOM 2583 N N . TYR B 1 68 ? -4.115 0.993 -4.877 1.00 24.43 ? 68 TYR B N 1 ATOM 2584 C CA . TYR B 1 68 ? -4.721 -0.286 -5.120 1.00 23.70 ? 68 TYR B CA 1 ATOM 2585 C C . TYR B 1 68 ? -5.170 -0.852 -3.803 1.00 23.82 ? 68 TYR B C 1 ATOM 2586 O O . TYR B 1 68 ? -4.419 -0.797 -2.837 1.00 23.90 ? 68 TYR B O 1 ATOM 2587 C CB . TYR B 1 68 ? -3.707 -1.221 -5.778 1.00 23.86 ? 68 TYR B CB 1 ATOM 2588 C CG . TYR B 1 68 ? -3.961 -2.669 -5.485 1.00 23.60 ? 68 TYR B CG 1 ATOM 2589 C CD1 . TYR B 1 68 ? -4.863 -3.378 -6.235 1.00 22.98 ? 68 TYR B CD1 1 ATOM 2590 C CD2 . TYR B 1 68 ? -3.325 -3.314 -4.421 1.00 24.05 ? 68 TYR B CD2 1 ATOM 2591 C CE1 . TYR B 1 68 ? -5.113 -4.702 -5.992 1.00 23.78 ? 68 TYR B CE1 1 ATOM 2592 C CE2 . TYR B 1 68 ? -3.584 -4.640 -4.144 1.00 24.55 ? 68 TYR B CE2 1 ATOM 2593 C CZ . TYR B 1 68 ? -4.475 -5.338 -4.947 1.00 24.70 ? 68 TYR B CZ 1 ATOM 2594 O OH . TYR B 1 68 ? -4.774 -6.657 -4.718 1.00 22.14 ? 68 TYR B OH 1 ATOM 2595 N N . GLN B 1 69 ? -6.383 -1.413 -3.778 1.00 25.79 ? 69 GLN B N 1 ATOM 2596 C CA . GLN B 1 69 ? -6.894 -2.179 -2.622 1.00 27.22 ? 69 GLN B CA 1 ATOM 2597 C C . GLN B 1 69 ? -7.384 -3.537 -3.091 1.00 26.22 ? 69 GLN B C 1 ATOM 2598 O O . GLN B 1 69 ? -8.158 -3.611 -4.022 1.00 26.15 ? 69 GLN B O 1 ATOM 2599 C CB . GLN B 1 69 ? -8.044 -1.456 -1.929 1.00 27.10 ? 69 GLN B CB 1 ATOM 2600 C CG . GLN B 1 69 ? -7.818 0.035 -1.717 1.00 31.59 ? 69 GLN B CG 1 ATOM 2601 C CD . GLN B 1 69 ? -8.790 0.665 -0.696 1.00 35.24 ? 69 GLN B CD 1 ATOM 2602 O OE1 . GLN B 1 69 ? -9.218 0.012 0.255 1.00 42.50 ? 69 GLN B OE1 1 ATOM 2603 N NE2 . GLN B 1 69 ? -9.118 1.933 -0.887 1.00 37.89 ? 69 GLN B NE2 1 ATOM 2604 N N . TYR B 1 70 ? -6.948 -4.605 -2.431 1.00 26.43 ? 70 TYR B N 1 ATOM 2605 C CA . TYR B 1 70 ? -7.390 -5.946 -2.773 1.00 25.65 ? 70 TYR B CA 1 ATOM 2606 C C . TYR B 1 70 ? -8.916 -6.118 -2.795 1.00 28.48 ? 70 TYR B C 1 ATOM 2607 O O . TYR B 1 70 ? -9.477 -6.558 -3.801 1.00 28.62 ? 70 TYR B O 1 ATOM 2608 C CB . TYR B 1 70 ? -6.788 -6.930 -1.799 1.00 26.28 ? 70 TYR B CB 1 ATOM 2609 C CG . TYR B 1 70 ? -7.129 -8.347 -2.122 1.00 26.84 ? 70 TYR B CG 1 ATOM 2610 C CD1 . TYR B 1 70 ? -6.387 -9.045 -3.051 1.00 25.99 ? 70 TYR B CD1 1 ATOM 2611 C CD2 . TYR B 1 70 ? -8.239 -8.987 -1.529 1.00 27.86 ? 70 TYR B CD2 1 ATOM 2612 C CE1 . TYR B 1 70 ? -6.693 -10.351 -3.376 1.00 26.22 ? 70 TYR B CE1 1 ATOM 2613 C CE2 . TYR B 1 70 ? -8.545 -10.306 -1.846 1.00 27.85 ? 70 TYR B CE2 1 ATOM 2614 C CZ . TYR B 1 70 ? -7.766 -10.976 -2.770 1.00 27.00 ? 70 TYR B CZ 1 ATOM 2615 O OH . TYR B 1 70 ? -8.029 -12.282 -3.115 1.00 30.35 ? 70 TYR B OH 1 ATOM 2616 N N . ASN B 1 71 ? -9.577 -5.794 -1.686 1.00 30.90 ? 71 ASN B N 1 ATOM 2617 C CA . ASN B 1 71 ? -11.055 -5.827 -1.590 1.00 32.04 ? 71 ASN B CA 1 ATOM 2618 C C . ASN B 1 71 ? -11.751 -5.134 -2.769 1.00 29.42 ? 71 ASN B C 1 ATOM 2619 O O . ASN B 1 71 ? -12.669 -5.647 -3.350 1.00 31.76 ? 71 ASN B O 1 ATOM 2620 C CB . ASN B 1 71 ? -11.532 -5.088 -0.324 1.00 33.15 ? 71 ASN B CB 1 ATOM 2621 C CG . ASN B 1 71 ? -11.206 -5.799 0.967 1.00 36.70 ? 71 ASN B CG 1 ATOM 2622 O OD1 . ASN B 1 71 ? -11.497 -5.261 2.046 1.00 43.92 ? 71 ASN B OD1 1 ATOM 2623 N ND2 . ASN B 1 71 ? -10.619 -6.989 0.892 1.00 35.25 ? 71 ASN B ND2 1 ATOM 2624 N N . ARG B 1 72 ? -11.304 -3.941 -3.089 1.00 28.57 ? 72 ARG B N 1 ATOM 2625 C CA . ARG B 1 72 ? -11.917 -3.144 -4.117 1.00 30.02 ? 72 ARG B CA 1 ATOM 2626 C C . ARG B 1 72 ? -11.485 -3.524 -5.544 1.00 28.97 ? 72 ARG B C 1 ATOM 2627 O O . ARG B 1 72 ? -12.323 -3.555 -6.460 1.00 29.39 ? 72 ARG B O 1 ATOM 2628 C CB . ARG B 1 72 ? -11.606 -1.681 -3.848 1.00 31.17 ? 72 ARG B CB 1 ATOM 2629 C CG . ARG B 1 72 ? -12.306 -0.702 -4.785 1.00 32.20 ? 72 ARG B CG 1 ATOM 2630 C CD . ARG B 1 72 ? -11.589 0.630 -4.782 1.00 32.28 ? 72 ARG B CD 1 ATOM 2631 N NE . ARG B 1 72 ? -10.181 0.473 -5.142 1.00 32.63 ? 72 ARG B NE 1 ATOM 2632 C CZ . ARG B 1 72 ? -9.282 1.444 -5.064 1.00 33.71 ? 72 ARG B CZ 1 ATOM 2633 N NH1 . ARG B 1 72 ? -9.647 2.647 -4.632 1.00 35.60 ? 72 ARG B NH1 1 ATOM 2634 N NH2 . ARG B 1 72 ? -8.014 1.222 -5.405 1.00 32.44 ? 72 ARG B NH2 1 ATOM 2635 N N . ASP B 1 73 ? -10.198 -3.810 -5.746 1.00 25.41 ? 73 ASP B N 1 ATOM 2636 C CA . ASP B 1 73 ? -9.681 -4.025 -7.101 1.00 24.08 ? 73 ASP B CA 1 ATOM 2637 C C . ASP B 1 73 ? -9.508 -5.477 -7.533 1.00 22.66 ? 73 ASP B C 1 ATOM 2638 O O . ASP B 1 73 ? -9.699 -5.781 -8.704 1.00 24.13 ? 73 ASP B O 1 ATOM 2639 C CB . ASP B 1 73 ? -8.382 -3.267 -7.256 1.00 23.88 ? 73 ASP B CB 1 ATOM 2640 C CG . ASP B 1 73 ? -8.566 -1.803 -6.972 1.00 24.50 ? 73 ASP B CG 1 ATOM 2641 O OD1 . ASP B 1 73 ? -9.662 -1.302 -7.327 1.00 25.57 ? 73 ASP B OD1 1 ATOM 2642 O OD2 . ASP B 1 73 ? -7.660 -1.165 -6.385 1.00 22.56 ? 73 ASP B OD2 1 ATOM 2643 N N . CYS B 1 74 ? -9.188 -6.391 -6.627 1.00 21.98 ? 74 CYS B N 1 ATOM 2644 C CA . CYS B 1 74 ? -9.006 -7.793 -7.067 1.00 21.93 ? 74 CYS B CA 1 ATOM 2645 C C . CYS B 1 74 ? -10.282 -8.507 -7.445 1.00 21.12 ? 74 CYS B C 1 ATOM 2646 O O . CYS B 1 74 ? -10.854 -9.241 -6.657 1.00 21.03 ? 74 CYS B O 1 ATOM 2647 C CB . CYS B 1 74 ? -8.223 -8.645 -6.070 1.00 22.25 ? 74 CYS B CB 1 ATOM 2648 S SG . CYS B 1 74 ? -7.567 -10.092 -6.917 1.00 22.93 ? 74 CYS B SG 1 ATOM 2649 N N . LYS B 1 75 ? -10.750 -8.280 -8.659 1.00 22.08 ? 75 LYS B N 1 ATOM 2650 C CA . LYS B 1 75 ? -11.900 -9.038 -9.149 1.00 23.42 ? 75 LYS B CA 1 ATOM 2651 C C . LYS B 1 75 ? -12.003 -8.977 -10.668 1.00 23.52 ? 75 LYS B C 1 ATOM 2652 O O . LYS B 1 75 ? -11.430 -8.089 -11.287 1.00 26.76 ? 75 LYS B O 1 ATOM 2653 C CB . LYS B 1 75 ? -13.209 -8.585 -8.455 1.00 23.39 ? 75 LYS B CB 1 ATOM 2654 C CG . LYS B 1 75 ? -13.916 -7.375 -9.037 1.00 25.10 ? 75 LYS B CG 1 ATOM 2655 C CD . LYS B 1 75 ? -13.261 -6.053 -8.658 1.00 25.46 ? 75 LYS B CD 1 ATOM 2656 C CE . LYS B 1 75 ? -14.026 -4.888 -9.262 1.00 26.21 ? 75 LYS B CE 1 ATOM 2657 N NZ . LYS B 1 75 ? -13.599 -3.553 -8.763 1.00 26.90 ? 75 LYS B NZ 1 ATOM 2658 N N . ASP B 1 76 ? -12.730 -9.905 -11.278 1.00 23.36 ? 76 ASP B N 1 ATOM 2659 C CA . ASP B 1 76 ? -12.865 -9.874 -12.739 1.00 23.31 ? 76 ASP B CA 1 ATOM 2660 C C . ASP B 1 76 ? -14.106 -9.122 -13.169 1.00 25.97 ? 76 ASP B C 1 ATOM 2661 O O . ASP B 1 76 ? -14.781 -8.500 -12.334 1.00 23.60 ? 76 ASP B O 1 ATOM 2662 C CB . ASP B 1 76 ? -12.826 -11.287 -13.341 1.00 22.58 ? 76 ASP B CB 1 ATOM 2663 C CG . ASP B 1 76 ? -14.034 -12.146 -12.972 1.00 21.56 ? 76 ASP B CG 1 ATOM 2664 O OD1 . ASP B 1 76 ? -15.051 -11.642 -12.434 1.00 20.28 ? 76 ASP B OD1 1 ATOM 2665 O OD2 . ASP B 1 76 ? -13.922 -13.362 -13.201 1.00 20.67 ? 76 ASP B OD2 1 ATOM 2666 N N . GLU B 1 77 ? -14.425 -9.209 -14.460 1.00 26.30 ? 77 GLU B N 1 ATOM 2667 C CA . GLU B 1 77 ? -15.520 -8.441 -15.026 1.00 30.67 ? 77 GLU B CA 1 ATOM 2668 C C . GLU B 1 77 ? -16.889 -8.912 -14.522 1.00 27.91 ? 77 GLU B C 1 ATOM 2669 O O . GLU B 1 77 ? -17.883 -8.233 -14.723 1.00 23.78 ? 77 GLU B O 1 ATOM 2670 C CB . GLU B 1 77 ? -15.492 -8.499 -16.564 1.00 35.01 ? 77 GLU B CB 1 ATOM 2671 C CG . GLU B 1 77 ? -14.174 -8.107 -17.225 1.00 40.68 ? 77 GLU B CG 1 ATOM 2672 C CD . GLU B 1 77 ? -13.611 -6.772 -16.791 1.00 43.49 ? 77 GLU B CD 1 ATOM 2673 O OE1 . GLU B 1 77 ? -13.400 -6.552 -15.580 1.00 49.55 ? 77 GLU B OE1 1 ATOM 2674 O OE2 . GLU B 1 77 ? -13.330 -5.950 -17.685 1.00 52.66 ? 77 GLU B OE2 1 ATOM 2675 N N . SER B 1 78 ? -16.930 -10.083 -13.891 1.00 26.33 ? 78 SER B N 1 ATOM 2676 C CA . SER B 1 78 ? -18.147 -10.561 -13.217 1.00 28.12 ? 78 SER B CA 1 ATOM 2677 C C . SER B 1 78 ? -18.188 -10.202 -11.728 1.00 25.95 ? 78 SER B C 1 ATOM 2678 O O . SER B 1 78 ? -19.054 -10.680 -11.007 1.00 23.54 ? 78 SER B O 1 ATOM 2679 C CB . SER B 1 78 ? -18.240 -12.080 -13.307 1.00 28.26 ? 78 SER B CB 1 ATOM 2680 O OG . SER B 1 78 ? -17.969 -12.502 -14.634 1.00 33.73 ? 78 SER B OG 1 ATOM 2681 N N . GLY B 1 79 ? -17.235 -9.413 -11.255 1.00 24.62 ? 79 GLY B N 1 ATOM 2682 C CA . GLY B 1 79 ? -17.171 -9.089 -9.833 1.00 24.38 ? 79 GLY B CA 1 ATOM 2683 C C . GLY B 1 79 ? -16.636 -10.201 -8.951 1.00 25.42 ? 79 GLY B C 1 ATOM 2684 O O . GLY B 1 79 ? -16.602 -10.034 -7.747 1.00 25.43 ? 79 GLY B O 1 ATOM 2685 N N . GLU B 1 80 ? -16.172 -11.314 -9.532 1.00 25.38 ? 80 GLU B N 1 ATOM 2686 C CA . GLU B 1 80 ? -15.715 -12.467 -8.732 1.00 26.59 ? 80 GLU B CA 1 ATOM 2687 C C . GLU B 1 80 ? -14.392 -12.204 -8.003 1.00 26.00 ? 80 GLU B C 1 ATOM 2688 O O . GLU B 1 80 ? -13.347 -11.967 -8.639 1.00 22.01 ? 80 GLU B O 1 ATOM 2689 C CB . GLU B 1 80 ? -15.599 -13.724 -9.606 1.00 28.28 ? 80 GLU B CB 1 ATOM 2690 C CG . GLU B 1 80 ? -15.822 -14.996 -8.788 1.00 32.65 ? 80 GLU B CG 1 ATOM 2691 C CD . GLU B 1 80 ? -16.030 -16.228 -9.643 1.00 33.94 ? 80 GLU B CD 1 ATOM 2692 O OE1 . GLU B 1 80 ? -16.918 -16.223 -10.516 1.00 34.84 ? 80 GLU B OE1 1 ATOM 2693 O OE2 . GLU B 1 80 ? -15.309 -17.208 -9.430 1.00 39.92 ? 80 GLU B OE2 1 ATOM 2694 N N . LYS B 1 81 ? -14.444 -12.245 -6.671 1.00 25.99 ? 81 LYS B N 1 ATOM 2695 C CA . LYS B 1 81 ? -13.330 -11.781 -5.815 1.00 28.47 ? 81 LYS B CA 1 ATOM 2696 C C . LYS B 1 81 ? -12.064 -12.641 -5.914 1.00 26.57 ? 81 LYS B C 1 ATOM 2697 O O . LYS B 1 81 ? -12.141 -13.852 -5.906 1.00 24.93 ? 81 LYS B O 1 ATOM 2698 C CB . LYS B 1 81 ? -13.787 -11.751 -4.354 1.00 32.74 ? 81 LYS B CB 1 ATOM 2699 C CG . LYS B 1 81 ? -12.861 -11.003 -3.401 1.00 35.46 ? 81 LYS B CG 1 ATOM 2700 C CD . LYS B 1 81 ? -12.988 -11.569 -1.997 1.00 37.48 ? 81 LYS B CD 1 ATOM 2701 C CE . LYS B 1 81 ? -12.110 -10.810 -1.030 1.00 38.57 ? 81 LYS B CE 1 ATOM 2702 N NZ . LYS B 1 81 ? -12.636 -9.450 -0.746 1.00 38.80 ? 81 LYS B NZ 1 ATOM 2703 N N . GLY B 1 82 ? -10.893 -12.016 -5.988 1.00 23.50 ? 82 GLY B N 1 ATOM 2704 C CA . GLY B 1 82 ? -9.672 -12.796 -6.118 1.00 23.66 ? 82 GLY B CA 1 ATOM 2705 C C . GLY B 1 82 ? -9.241 -13.036 -7.559 1.00 22.89 ? 82 GLY B C 1 ATOM 2706 O O . GLY B 1 82 ? -8.096 -13.426 -7.819 1.00 21.92 ? 82 GLY B O 1 ATOM 2707 N N . ARG B 1 83 ? -10.126 -12.762 -8.515 1.00 21.45 ? 83 ARG B N 1 ATOM 2708 C CA . ARG B 1 83 ? -9.797 -13.016 -9.896 1.00 22.22 ? 83 ARG B CA 1 ATOM 2709 C C . ARG B 1 83 ? -8.984 -11.848 -10.499 1.00 22.07 ? 83 ARG B C 1 ATOM 2710 O O . ARG B 1 83 ? -9.479 -11.044 -11.269 1.00 20.33 ? 83 ARG B O 1 ATOM 2711 C CB . ARG B 1 83 ? -11.061 -13.406 -10.665 1.00 22.87 ? 83 ARG B CB 1 ATOM 2712 C CG . ARG B 1 83 ? -11.673 -14.675 -10.043 1.00 23.55 ? 83 ARG B CG 1 ATOM 2713 C CD . ARG B 1 83 ? -12.414 -15.567 -11.038 1.00 25.44 ? 83 ARG B CD 1 ATOM 2714 N NE . ARG B 1 83 ? -11.585 -16.230 -12.053 1.00 23.12 ? 83 ARG B NE 1 ATOM 2715 C CZ . ARG B 1 83 ? -10.854 -17.305 -11.843 1.00 23.88 ? 83 ARG B CZ 1 ATOM 2716 N NH1 . ARG B 1 83 ? -10.775 -17.814 -10.624 1.00 25.93 ? 83 ARG B NH1 1 ATOM 2717 N NH2 . ARG B 1 83 ? -10.131 -17.833 -12.833 1.00 23.39 ? 83 ARG B NH2 1 ATOM 2718 N N . CYS B 1 84 ? -7.715 -11.790 -10.096 1.00 20.53 ? 84 CYS B N 1 ATOM 2719 C CA . CYS B 1 84 ? -6.767 -10.826 -10.600 1.00 19.05 ? 84 CYS B CA 1 ATOM 2720 C C . CYS B 1 84 ? -5.358 -11.357 -10.329 1.00 17.62 ? 84 CYS B C 1 ATOM 2721 O O . CYS B 1 84 ? -5.162 -12.447 -9.769 1.00 17.48 ? 84 CYS B O 1 ATOM 2722 C CB . CYS B 1 84 ? -7.002 -9.449 -9.962 1.00 21.39 ? 84 CYS B CB 1 ATOM 2723 S SG . CYS B 1 84 ? -6.284 -9.201 -8.316 1.00 20.86 ? 84 CYS B SG 1 ATOM 2724 N N . VAL B 1 85 ? -4.360 -10.626 -10.773 1.00 17.14 ? 85 VAL B N 1 ATOM 2725 C CA . VAL B 1 85 ? -3.004 -11.137 -10.698 1.00 16.37 ? 85 VAL B CA 1 ATOM 2726 C C . VAL B 1 85 ? -2.550 -11.428 -9.267 1.00 16.79 ? 85 VAL B C 1 ATOM 2727 O O . VAL B 1 85 ? -1.930 -12.456 -9.011 1.00 16.54 ? 85 VAL B O 1 ATOM 2728 C CB . VAL B 1 85 ? -2.010 -10.251 -11.489 1.00 16.18 ? 85 VAL B CB 1 ATOM 2729 C CG1 . VAL B 1 85 ? -1.821 -8.903 -10.843 1.00 16.27 ? 85 VAL B CG1 1 ATOM 2730 C CG2 . VAL B 1 85 ? -0.710 -10.978 -11.705 1.00 16.45 ? 85 VAL B CG2 1 ATOM 2731 N N . ALA B 1 86 ? -2.851 -10.522 -8.341 1.00 17.72 ? 86 ALA B N 1 ATOM 2732 C CA . ALA B 1 86 ? -2.667 -10.767 -6.922 1.00 17.28 ? 86 ALA B CA 1 ATOM 2733 C C . ALA B 1 86 ? -3.381 -12.036 -6.416 1.00 17.45 ? 86 ALA B C 1 ATOM 2734 O O . ALA B 1 86 ? -2.767 -12.891 -5.791 1.00 17.29 ? 86 ALA B O 1 ATOM 2735 C CB . ALA B 1 86 ? -3.131 -9.553 -6.142 1.00 17.39 ? 86 ALA B CB 1 ATOM 2736 N N . GLY B 1 87 ? -4.678 -12.146 -6.663 1.00 17.65 ? 87 GLY B N 1 ATOM 2737 C CA . GLY B 1 87 ? -5.430 -13.349 -6.288 1.00 17.28 ? 87 GLY B CA 1 ATOM 2738 C C . GLY B 1 87 ? -4.827 -14.606 -6.922 1.00 18.08 ? 87 GLY B C 1 ATOM 2739 O O . GLY B 1 87 ? -4.701 -15.646 -6.278 1.00 18.65 ? 87 GLY B O 1 ATOM 2740 N N . ALA B 1 88 ? -4.428 -14.529 -8.185 1.00 17.50 ? 88 ALA B N 1 ATOM 2741 C CA . ALA B 1 88 ? -3.772 -15.673 -8.812 1.00 16.83 ? 88 ALA B CA 1 ATOM 2742 C C . ALA B 1 88 ? -2.489 -16.143 -8.080 1.00 18.36 ? 88 ALA B C 1 ATOM 2743 O O . ALA B 1 88 ? -2.216 -17.354 -8.030 1.00 16.44 ? 88 ALA B O 1 ATOM 2744 C CB . ALA B 1 88 ? -3.457 -15.408 -10.279 1.00 16.41 ? 88 ALA B CB 1 ATOM 2745 N N . ILE B 1 89 ? -1.692 -15.194 -7.606 1.00 17.50 ? 89 ILE B N 1 ATOM 2746 C CA . ILE B 1 89 ? -0.424 -15.530 -6.986 1.00 20.24 ? 89 ILE B CA 1 ATOM 2747 C C . ILE B 1 89 ? -0.729 -16.263 -5.663 1.00 20.89 ? 89 ILE B C 1 ATOM 2748 O O . ILE B 1 89 ? -0.126 -17.305 -5.360 1.00 21.76 ? 89 ILE B O 1 ATOM 2749 C CB . ILE B 1 89 ? 0.484 -14.269 -6.841 1.00 20.49 ? 89 ILE B CB 1 ATOM 2750 C CG1 . ILE B 1 89 ? 1.161 -13.964 -8.195 1.00 20.29 ? 89 ILE B CG1 1 ATOM 2751 C CG2 . ILE B 1 89 ? 1.566 -14.454 -5.781 1.00 20.27 ? 89 ILE B CG2 1 ATOM 2752 C CD1 . ILE B 1 89 ? 1.631 -12.527 -8.369 1.00 19.09 ? 89 ILE B CD1 1 ATOM 2753 N N . TYR B 1 90 ? -1.724 -15.767 -4.919 1.00 21.72 ? 90 TYR B N 1 ATOM 2754 C CA . TYR B 1 90 ? -2.142 -16.420 -3.685 1.00 20.88 ? 90 TYR B CA 1 ATOM 2755 C C . TYR B 1 90 ? -2.540 -17.851 -3.951 1.00 21.03 ? 90 TYR B C 1 ATOM 2756 O O . TYR B 1 90 ? -2.087 -18.763 -3.249 1.00 21.17 ? 90 TYR B O 1 ATOM 2757 C CB . TYR B 1 90 ? -3.293 -15.686 -3.014 1.00 22.21 ? 90 TYR B CB 1 ATOM 2758 C CG . TYR B 1 90 ? -2.925 -14.421 -2.253 1.00 23.85 ? 90 TYR B CG 1 ATOM 2759 C CD1 . TYR B 1 90 ? -1.851 -14.389 -1.346 1.00 25.08 ? 90 TYR B CD1 1 ATOM 2760 C CD2 . TYR B 1 90 ? -3.702 -13.283 -2.374 1.00 23.90 ? 90 TYR B CD2 1 ATOM 2761 C CE1 . TYR B 1 90 ? -1.566 -13.239 -0.618 1.00 24.65 ? 90 TYR B CE1 1 ATOM 2762 C CE2 . TYR B 1 90 ? -3.421 -12.142 -1.671 1.00 24.13 ? 90 TYR B CE2 1 ATOM 2763 C CZ . TYR B 1 90 ? -2.353 -12.120 -0.798 1.00 24.08 ? 90 TYR B CZ 1 ATOM 2764 O OH . TYR B 1 90 ? -2.100 -10.970 -0.112 1.00 23.40 ? 90 TYR B OH 1 ATOM 2765 N N . ASN B 1 91 ? -3.385 -18.045 -4.962 1.00 20.54 ? 91 ASN B N 1 ATOM 2766 C CA . ASN B 1 91 ? -3.853 -19.369 -5.385 1.00 21.41 ? 91 ASN B CA 1 ATOM 2767 C C . ASN B 1 91 ? -2.745 -20.344 -5.738 1.00 21.55 ? 91 ASN B C 1 ATOM 2768 O O . ASN B 1 91 ? -2.675 -21.469 -5.227 1.00 19.10 ? 91 ASN B O 1 ATOM 2769 C CB . ASN B 1 91 ? -4.694 -19.209 -6.650 1.00 22.80 ? 91 ASN B CB 1 ATOM 2770 C CG . ASN B 1 91 ? -5.442 -20.459 -7.041 1.00 23.02 ? 91 ASN B CG 1 ATOM 2771 O OD1 . ASN B 1 91 ? -5.655 -21.360 -6.243 1.00 23.49 ? 91 ASN B OD1 1 ATOM 2772 N ND2 . ASN B 1 91 ? -5.850 -20.499 -8.312 1.00 22.87 ? 91 ASN B ND2 1 ATOM 2773 N N . TYR B 1 92 ? -1.908 -19.931 -6.677 1.00 20.65 ? 92 TYR B N 1 ATOM 2774 C CA . TYR B 1 92 ? -0.959 -20.861 -7.225 1.00 20.73 ? 92 TYR B CA 1 ATOM 2775 C C . TYR B 1 92 ? 0.238 -21.121 -6.291 1.00 19.81 ? 92 TYR B C 1 ATOM 2776 O O . TYR B 1 92 ? 0.796 -22.209 -6.299 1.00 19.67 ? 92 TYR B O 1 ATOM 2777 C CB . TYR B 1 92 ? -0.554 -20.429 -8.622 1.00 20.44 ? 92 TYR B CB 1 ATOM 2778 C CG . TYR B 1 92 ? -1.681 -20.594 -9.622 1.00 20.75 ? 92 TYR B CG 1 ATOM 2779 C CD1 . TYR B 1 92 ? -2.139 -21.864 -9.986 1.00 20.87 ? 92 TYR B CD1 1 ATOM 2780 C CD2 . TYR B 1 92 ? -2.303 -19.480 -10.189 1.00 20.54 ? 92 TYR B CD2 1 ATOM 2781 C CE1 . TYR B 1 92 ? -3.192 -22.002 -10.892 1.00 20.99 ? 92 TYR B CE1 1 ATOM 2782 C CE2 . TYR B 1 92 ? -3.331 -19.604 -11.097 1.00 19.79 ? 92 TYR B CE2 1 ATOM 2783 C CZ . TYR B 1 92 ? -3.770 -20.868 -11.455 1.00 20.23 ? 92 TYR B CZ 1 ATOM 2784 O OH . TYR B 1 92 ? -4.801 -20.975 -12.356 1.00 17.81 ? 92 TYR B OH 1 ATOM 2785 N N . THR B 1 93 ? 0.610 -20.140 -5.489 1.00 20.06 ? 93 THR B N 1 ATOM 2786 C CA . THR B 1 93 ? 1.607 -20.382 -4.447 1.00 21.09 ? 93 THR B CA 1 ATOM 2787 C C . THR B 1 93 ? 1.034 -21.332 -3.391 1.00 21.12 ? 93 THR B C 1 ATOM 2788 O O . THR B 1 93 ? 1.740 -22.206 -2.917 1.00 21.48 ? 93 THR B O 1 ATOM 2789 C CB . THR B 1 93 ? 2.087 -19.083 -3.762 1.00 20.62 ? 93 THR B CB 1 ATOM 2790 O OG1 . THR B 1 93 ? 0.978 -18.361 -3.243 1.00 19.71 ? 93 THR B OG1 1 ATOM 2791 C CG2 . THR B 1 93 ? 2.836 -18.192 -4.728 1.00 21.40 ? 93 THR B CG2 1 ATOM 2792 N N . THR B 1 94 ? -0.243 -21.149 -3.038 1.00 22.25 ? 94 THR B N 1 ATOM 2793 C CA . THR B 1 94 ? -0.937 -22.029 -2.087 1.00 22.41 ? 94 THR B CA 1 ATOM 2794 C C . THR B 1 94 ? -0.939 -23.476 -2.608 1.00 24.62 ? 94 THR B C 1 ATOM 2795 O O . THR B 1 94 ? -0.593 -24.414 -1.885 1.00 25.66 ? 94 THR B O 1 ATOM 2796 C CB . THR B 1 94 ? -2.375 -21.527 -1.772 1.00 21.19 ? 94 THR B CB 1 ATOM 2797 O OG1 . THR B 1 94 ? -2.311 -20.293 -1.016 1.00 21.09 ? 94 THR B OG1 1 ATOM 2798 C CG2 . THR B 1 94 ? -3.177 -22.541 -0.963 1.00 20.84 ? 94 THR B CG2 1 ATOM 2799 N N . GLN B 1 95 ? -1.285 -23.659 -3.868 1.00 26.20 ? 95 GLN B N 1 ATOM 2800 C CA . GLN B 1 95 ? -1.204 -24.991 -4.490 1.00 26.59 ? 95 GLN B CA 1 ATOM 2801 C C . GLN B 1 95 ? 0.207 -25.596 -4.373 1.00 28.50 ? 95 GLN B C 1 ATOM 2802 O O . GLN B 1 95 ? 0.320 -26.766 -4.037 1.00 27.86 ? 95 GLN B O 1 ATOM 2803 C CB . GLN B 1 95 ? -1.630 -24.935 -5.960 1.00 25.82 ? 95 GLN B CB 1 ATOM 2804 C CG . GLN B 1 95 ? -3.120 -24.673 -6.156 1.00 26.10 ? 95 GLN B CG 1 ATOM 2805 C CD . GLN B 1 95 ? -3.522 -24.352 -7.584 1.00 24.32 ? 95 GLN B CD 1 ATOM 2806 O OE1 . GLN B 1 95 ? -3.044 -24.972 -8.556 1.00 25.50 ? 95 GLN B OE1 1 ATOM 2807 N NE2 . GLN B 1 95 ? -4.429 -23.383 -7.725 1.00 22.74 ? 95 GLN B NE2 1 ATOM 2808 N N . LEU B 1 96 ? 1.266 -24.806 -4.631 1.00 27.40 ? 96 LEU B N 1 ATOM 2809 C CA . LEU B 1 96 ? 2.663 -25.339 -4.624 1.00 26.78 ? 96 LEU B CA 1 ATOM 2810 C C . LEU B 1 96 ? 3.169 -25.766 -3.244 1.00 27.40 ? 96 LEU B C 1 ATOM 2811 O O . LEU B 1 96 ? 4.084 -26.595 -3.152 1.00 24.61 ? 96 LEU B O 1 ATOM 2812 C CB . LEU B 1 96 ? 3.669 -24.360 -5.253 1.00 25.58 ? 96 LEU B CB 1 ATOM 2813 C CG . LEU B 1 96 ? 3.521 -24.102 -6.750 1.00 25.14 ? 96 LEU B CG 1 ATOM 2814 C CD1 . LEU B 1 96 ? 4.290 -22.857 -7.164 1.00 27.00 ? 96 LEU B CD1 1 ATOM 2815 C CD2 . LEU B 1 96 ? 3.950 -25.301 -7.586 1.00 25.36 ? 96 LEU B CD2 1 ATOM 2816 N N . LEU B 1 97 ? 2.583 -25.195 -2.191 1.00 26.93 ? 97 LEU B N 1 ATOM 2817 C CA . LEU B 1 97 ? 2.768 -25.691 -0.822 1.00 27.68 ? 97 LEU B CA 1 ATOM 2818 C C . LEU B 1 97 ? 2.380 -27.171 -0.657 1.00 29.48 ? 97 LEU B C 1 ATOM 2819 O O . LEU B 1 97 ? 2.804 -27.794 0.302 1.00 31.05 ? 97 LEU B O 1 ATOM 2820 C CB . LEU B 1 97 ? 1.963 -24.844 0.176 1.00 26.39 ? 97 LEU B CB 1 ATOM 2821 C CG . LEU B 1 97 ? 2.438 -23.398 0.353 1.00 26.67 ? 97 LEU B CG 1 ATOM 2822 C CD1 . LEU B 1 97 ? 1.477 -22.624 1.270 1.00 26.70 ? 97 LEU B CD1 1 ATOM 2823 C CD2 . LEU B 1 97 ? 3.867 -23.364 0.897 1.00 25.65 ? 97 LEU B CD2 1 ATOM 2824 N N . SER B 1 98 ? 1.590 -27.712 -1.581 1.00 30.29 ? 98 SER B N 1 ATOM 2825 C CA . SER B 1 98 ? 1.224 -29.146 -1.605 1.00 33.89 ? 98 SER B CA 1 ATOM 2826 C C . SER B 1 98 ? 2.305 -30.070 -2.132 1.00 34.53 ? 98 SER B C 1 ATOM 2827 O O . SER B 1 98 ? 2.192 -31.290 -2.007 1.00 36.54 ? 98 SER B O 1 ATOM 2828 C CB . SER B 1 98 ? -0.006 -29.393 -2.490 1.00 32.97 ? 98 SER B CB 1 ATOM 2829 O OG . SER B 1 98 ? -1.087 -28.571 -2.121 1.00 35.96 ? 98 SER B OG 1 ATOM 2830 N N . TYR B 1 99 ? 3.326 -29.510 -2.761 1.00 35.32 ? 99 TYR B N 1 ATOM 2831 C CA . TYR B 1 99 ? 4.393 -30.310 -3.348 1.00 36.98 ? 99 TYR B CA 1 ATOM 2832 C C . TYR B 1 99 ? 5.039 -31.224 -2.289 1.00 38.37 ? 99 TYR B C 1 ATOM 2833 O O . TYR B 1 99 ? 5.396 -30.761 -1.217 1.00 38.19 ? 99 TYR B O 1 ATOM 2834 C CB . TYR B 1 99 ? 5.432 -29.375 -3.959 1.00 35.72 ? 99 TYR B CB 1 ATOM 2835 C CG . TYR B 1 99 ? 6.561 -30.083 -4.638 1.00 36.23 ? 99 TYR B CG 1 ATOM 2836 C CD1 . TYR B 1 99 ? 6.375 -30.689 -5.867 1.00 37.53 ? 99 TYR B CD1 1 ATOM 2837 C CD2 . TYR B 1 99 ? 7.827 -30.144 -4.060 1.00 36.19 ? 99 TYR B CD2 1 ATOM 2838 C CE1 . TYR B 1 99 ? 7.403 -31.342 -6.506 1.00 35.70 ? 99 TYR B CE1 1 ATOM 2839 C CE2 . TYR B 1 99 ? 8.870 -30.795 -4.703 1.00 36.84 ? 99 TYR B CE2 1 ATOM 2840 C CZ . TYR B 1 99 ? 8.644 -31.388 -5.927 1.00 36.92 ? 99 TYR B CZ 1 ATOM 2841 O OH . TYR B 1 99 ? 9.664 -32.042 -6.591 1.00 41.21 ? 99 TYR B OH 1 ATOM 2842 N N . LYS B 1 100 ? 5.169 -32.511 -2.602 1.00 44.56 ? 100 LYS B N 1 ATOM 2843 C CA . LYS B 1 100 ? 5.758 -33.501 -1.683 1.00 48.67 ? 100 LYS B CA 1 ATOM 2844 C C . LYS B 1 100 ? 7.079 -34.010 -2.256 1.00 49.64 ? 100 LYS B C 1 ATOM 2845 O O . LYS B 1 100 ? 8.153 -33.546 -1.879 1.00 53.26 ? 100 LYS B O 1 ATOM 2846 C CB . LYS B 1 100 ? 4.817 -34.696 -1.474 1.00 50.80 ? 100 LYS B CB 1 ATOM 2847 C CG . LYS B 1 100 ? 3.351 -34.363 -1.212 1.00 51.48 ? 100 LYS B CG 1 ATOM 2848 C CD . LYS B 1 100 ? 3.140 -33.734 0.161 1.00 50.74 ? 100 LYS B CD 1 ATOM 2849 C CE . LYS B 1 100 ? 1.687 -33.823 0.591 1.00 49.83 ? 100 LYS B CE 1 ATOM 2850 N NZ . LYS B 1 100 ? 1.187 -35.229 0.636 1.00 46.96 ? 100 LYS B NZ 1 ATOM 2851 N N . SER B 1 107 ? -2.511 -33.363 -5.580 1.00 57.71 ? 107 SER B N 1 ATOM 2852 C CA . SER B 1 107 ? -3.912 -33.692 -5.353 1.00 60.13 ? 107 SER B CA 1 ATOM 2853 C C . SER B 1 107 ? -4.781 -33.225 -6.536 1.00 56.71 ? 107 SER B C 1 ATOM 2854 O O . SER B 1 107 ? -4.591 -33.667 -7.670 1.00 57.98 ? 107 SER B O 1 ATOM 2855 C CB . SER B 1 107 ? -4.392 -33.074 -4.031 1.00 61.68 ? 107 SER B CB 1 ATOM 2856 O OG . SER B 1 107 ? -4.575 -31.671 -4.166 1.00 59.90 ? 107 SER B OG 1 ATOM 2857 N N . GLN B 1 108 ? -5.725 -32.325 -6.283 1.00 53.48 ? 108 GLN B N 1 ATOM 2858 C CA . GLN B 1 108 ? -6.593 -31.841 -7.340 1.00 54.83 ? 108 GLN B CA 1 ATOM 2859 C C . GLN B 1 108 ? -5.784 -31.182 -8.487 1.00 53.53 ? 108 GLN B C 1 ATOM 2860 O O . GLN B 1 108 ? -6.155 -31.307 -9.656 1.00 55.40 ? 108 GLN B O 1 ATOM 2861 C CB . GLN B 1 108 ? -7.618 -30.851 -6.764 1.00 56.80 ? 108 GLN B CB 1 ATOM 2862 C CG . GLN B 1 108 ? -8.792 -30.559 -7.689 1.00 59.82 ? 108 GLN B CG 1 ATOM 2863 C CD . GLN B 1 108 ? -9.225 -29.112 -7.634 1.00 62.58 ? 108 GLN B CD 1 ATOM 2864 O OE1 . GLN B 1 108 ? -9.438 -28.562 -6.552 1.00 67.41 ? 108 GLN B OE1 1 ATOM 2865 N NE2 . GLN B 1 108 ? -9.355 -28.481 -8.802 1.00 62.12 ? 108 GLN B NE2 1 ATOM 2866 N N . TYR B 1 109 ? -4.663 -30.532 -8.150 1.00 44.34 ? 109 TYR B N 1 ATOM 2867 C CA . TYR B 1 109 ? -4.040 -29.536 -9.029 1.00 40.91 ? 109 TYR B CA 1 ATOM 2868 C C . TYR B 1 109 ? -2.721 -29.942 -9.700 1.00 37.92 ? 109 TYR B C 1 ATOM 2869 O O . TYR B 1 109 ? -1.839 -30.515 -9.080 1.00 42.29 ? 109 TYR B O 1 ATOM 2870 C CB . TYR B 1 109 ? -3.798 -28.259 -8.234 1.00 39.22 ? 109 TYR B CB 1 ATOM 2871 C CG . TYR B 1 109 ? -5.050 -27.566 -7.767 1.00 37.11 ? 109 TYR B CG 1 ATOM 2872 C CD1 . TYR B 1 109 ? -5.990 -27.089 -8.682 1.00 38.97 ? 109 TYR B CD1 1 ATOM 2873 C CD2 . TYR B 1 109 ? -5.282 -27.351 -6.421 1.00 36.20 ? 109 TYR B CD2 1 ATOM 2874 C CE1 . TYR B 1 109 ? -7.142 -26.434 -8.258 1.00 39.16 ? 109 TYR B CE1 1 ATOM 2875 C CE2 . TYR B 1 109 ? -6.420 -26.691 -5.982 1.00 37.33 ? 109 TYR B CE2 1 ATOM 2876 C CZ . TYR B 1 109 ? -7.350 -26.233 -6.901 1.00 36.50 ? 109 TYR B CZ 1 ATOM 2877 O OH . TYR B 1 109 ? -8.480 -25.578 -6.473 1.00 31.91 ? 109 TYR B OH 1 ATOM 2878 N N . ASN B 1 110 ? -2.612 -29.610 -10.977 1.00 35.17 ? 110 ASN B N 1 ATOM 2879 C CA . ASN B 1 110 ? -1.411 -29.783 -11.764 1.00 33.69 ? 110 ASN B CA 1 ATOM 2880 C C . ASN B 1 110 ? -0.387 -28.745 -11.302 1.00 33.07 ? 110 ASN B C 1 ATOM 2881 O O . ASN B 1 110 ? -0.532 -27.549 -11.589 1.00 35.46 ? 110 ASN B O 1 ATOM 2882 C CB . ASN B 1 110 ? -1.792 -29.585 -13.240 1.00 34.48 ? 110 ASN B CB 1 ATOM 2883 C CG . ASN B 1 110 ? -0.637 -29.781 -14.202 1.00 35.74 ? 110 ASN B CG 1 ATOM 2884 O OD1 . ASN B 1 110 ? 0.532 -29.584 -13.861 1.00 34.54 ? 110 ASN B OD1 1 ATOM 2885 N ND2 . ASN B 1 110 ? -0.979 -30.178 -15.446 1.00 35.26 ? 110 ASN B ND2 1 ATOM 2886 N N . LEU B 1 111 ? 0.636 -29.208 -10.588 1.00 28.13 ? 111 LEU B N 1 ATOM 2887 C CA . LEU B 1 111 ? 1.628 -28.344 -9.973 1.00 27.75 ? 111 LEU B CA 1 ATOM 2888 C C . LEU B 1 111 ? 2.658 -27.798 -10.955 1.00 27.01 ? 111 LEU B C 1 ATOM 2889 O O . LEU B 1 111 ? 3.331 -26.792 -10.650 1.00 25.55 ? 111 LEU B O 1 ATOM 2890 C CB . LEU B 1 111 ? 2.325 -29.065 -8.812 1.00 27.56 ? 111 LEU B CB 1 ATOM 2891 C CG . LEU B 1 111 ? 1.362 -29.440 -7.684 1.00 28.47 ? 111 LEU B CG 1 ATOM 2892 C CD1 . LEU B 1 111 ? 2.128 -29.924 -6.472 1.00 28.85 ? 111 LEU B CD1 1 ATOM 2893 C CD2 . LEU B 1 111 ? 0.503 -28.247 -7.290 1.00 29.22 ? 111 LEU B CD2 1 ATOM 2894 N N . THR B 1 112 ? 2.771 -28.440 -12.117 1.00 24.36 ? 112 THR B N 1 ATOM 2895 C CA . THR B 1 112 ? 3.523 -27.876 -13.239 1.00 25.96 ? 112 THR B CA 1 ATOM 2896 C C . THR B 1 112 ? 2.873 -26.558 -13.687 1.00 26.29 ? 112 THR B C 1 ATOM 2897 O O . THR B 1 112 ? 3.546 -25.527 -13.788 1.00 26.36 ? 112 THR B O 1 ATOM 2898 C CB . THR B 1 112 ? 3.642 -28.873 -14.426 1.00 25.49 ? 112 THR B CB 1 ATOM 2899 O OG1 . THR B 1 112 ? 4.415 -29.994 -14.014 1.00 26.06 ? 112 THR B OG1 1 ATOM 2900 C CG2 . THR B 1 112 ? 4.364 -28.258 -15.601 1.00 26.50 ? 112 THR B CG2 1 ATOM 2901 N N . GLU B 1 113 ? 1.560 -26.591 -13.904 1.00 24.72 ? 113 GLU B N 1 ATOM 2902 C CA . GLU B 1 113 ? 0.818 -25.401 -14.297 1.00 23.62 ? 113 GLU B CA 1 ATOM 2903 C C . GLU B 1 113 ? 0.951 -24.329 -13.230 1.00 22.43 ? 113 GLU B C 1 ATOM 2904 O O . GLU B 1 113 ? 1.135 -23.168 -13.554 1.00 22.82 ? 113 GLU B O 1 ATOM 2905 C CB . GLU B 1 113 ? -0.649 -25.720 -14.552 1.00 23.56 ? 113 GLU B CB 1 ATOM 2906 C CG . GLU B 1 113 ? -0.887 -26.473 -15.838 1.00 24.47 ? 113 GLU B CG 1 ATOM 2907 C CD . GLU B 1 113 ? -2.344 -26.497 -16.284 1.00 24.88 ? 113 GLU B CD 1 ATOM 2908 O OE1 . GLU B 1 113 ? -3.259 -26.361 -15.454 1.00 27.52 ? 113 GLU B OE1 1 ATOM 2909 O OE2 . GLU B 1 113 ? -2.575 -26.634 -17.488 1.00 24.51 ? 113 GLU B OE2 1 ATOM 2910 N N . ALA B 1 114 ? 0.913 -24.740 -11.970 1.00 21.16 ? 114 ALA B N 1 ATOM 2911 C CA . ALA B 1 114 ? 0.954 -23.821 -10.859 1.00 21.56 ? 114 ALA B CA 1 ATOM 2912 C C . ALA B 1 114 ? 2.269 -23.033 -10.825 1.00 21.77 ? 114 ALA B C 1 ATOM 2913 O O . ALA B 1 114 ? 2.281 -21.833 -10.540 1.00 22.74 ? 114 ALA B O 1 ATOM 2914 C CB . ALA B 1 114 ? 0.759 -24.567 -9.557 1.00 20.58 ? 114 ALA B CB 1 ATOM 2915 N N . LEU B 1 115 ? 3.356 -23.727 -11.095 1.00 20.65 ? 115 LEU B N 1 ATOM 2916 C CA . LEU B 1 115 ? 4.667 -23.117 -11.190 1.00 21.35 ? 115 LEU B CA 1 ATOM 2917 C C . LEU B 1 115 ? 4.733 -22.168 -12.401 1.00 21.17 ? 115 LEU B C 1 ATOM 2918 O O . LEU B 1 115 ? 5.238 -21.042 -12.297 1.00 20.72 ? 115 LEU B O 1 ATOM 2919 C CB . LEU B 1 115 ? 5.733 -24.201 -11.301 1.00 22.45 ? 115 LEU B CB 1 ATOM 2920 C CG . LEU B 1 115 ? 7.166 -23.713 -11.574 1.00 22.90 ? 115 LEU B CG 1 ATOM 2921 C CD1 . LEU B 1 115 ? 7.739 -22.987 -10.384 1.00 23.37 ? 115 LEU B CD1 1 ATOM 2922 C CD2 . LEU B 1 115 ? 8.047 -24.880 -11.945 1.00 22.96 ? 115 LEU B CD2 1 ATOM 2923 N N . LEU B 1 116 ? 4.205 -22.600 -13.535 1.00 19.86 ? 116 LEU B N 1 ATOM 2924 C CA . LEU B 1 116 ? 4.248 -21.756 -14.724 1.00 20.26 ? 116 LEU B CA 1 ATOM 2925 C C . LEU B 1 116 ? 3.393 -20.511 -14.551 1.00 20.21 ? 116 LEU B C 1 ATOM 2926 O O . LEU B 1 116 ? 3.784 -19.434 -14.981 1.00 20.41 ? 116 LEU B O 1 ATOM 2927 C CB . LEU B 1 116 ? 3.838 -22.525 -15.980 1.00 20.25 ? 116 LEU B CB 1 ATOM 2928 C CG . LEU B 1 116 ? 4.704 -23.749 -16.285 1.00 20.00 ? 116 LEU B CG 1 ATOM 2929 C CD1 . LEU B 1 116 ? 4.209 -24.442 -17.534 1.00 20.81 ? 116 LEU B CD1 1 ATOM 2930 C CD2 . LEU B 1 116 ? 6.162 -23.410 -16.463 1.00 20.48 ? 116 LEU B CD2 1 ATOM 2931 N N . PHE B 1 117 ? 2.223 -20.654 -13.926 1.00 19.90 ? 117 PHE B N 1 ATOM 2932 C CA . PHE B 1 117 ? 1.363 -19.508 -13.663 1.00 19.08 ? 117 PHE B CA 1 ATOM 2933 C C . PHE B 1 117 ? 2.032 -18.573 -12.658 1.00 18.57 ? 117 PHE B C 1 ATOM 2934 O O . PHE B 1 117 ? 2.047 -17.353 -12.815 1.00 19.65 ? 117 PHE B O 1 ATOM 2935 C CB . PHE B 1 117 ? 0.000 -19.973 -13.100 1.00 18.64 ? 117 PHE B CB 1 ATOM 2936 C CG . PHE B 1 117 ? -0.995 -20.404 -14.147 1.00 18.44 ? 117 PHE B CG 1 ATOM 2937 C CD1 . PHE B 1 117 ? -1.360 -19.552 -15.167 1.00 19.20 ? 117 PHE B CD1 1 ATOM 2938 C CD2 . PHE B 1 117 ? -1.585 -21.663 -14.094 1.00 19.23 ? 117 PHE B CD2 1 ATOM 2939 C CE1 . PHE B 1 117 ? -2.279 -19.949 -16.139 1.00 19.67 ? 117 PHE B CE1 1 ATOM 2940 C CE2 . PHE B 1 117 ? -2.509 -22.053 -15.030 1.00 18.82 ? 117 PHE B CE2 1 ATOM 2941 C CZ . PHE B 1 117 ? -2.864 -21.191 -16.048 1.00 20.22 ? 117 PHE B CZ 1 ATOM 2942 N N . VAL B 1 118 ? 2.570 -19.136 -11.591 1.00 18.32 ? 118 VAL B N 1 ATOM 2943 C CA . VAL B 1 118 ? 3.129 -18.289 -10.558 1.00 18.13 ? 118 VAL B CA 1 ATOM 2944 C C . VAL B 1 118 ? 4.359 -17.569 -11.108 1.00 17.44 ? 118 VAL B C 1 ATOM 2945 O O . VAL B 1 118 ? 4.562 -16.393 -10.805 1.00 15.59 ? 118 VAL B O 1 ATOM 2946 C CB . VAL B 1 118 ? 3.430 -19.053 -9.263 1.00 20.08 ? 118 VAL B CB 1 ATOM 2947 C CG1 . VAL B 1 118 ? 4.908 -19.388 -9.139 1.00 21.05 ? 118 VAL B CG1 1 ATOM 2948 C CG2 . VAL B 1 118 ? 3.033 -18.190 -8.078 1.00 22.13 ? 118 VAL B CG2 1 ATOM 2949 N N . SER B 1 119 ? 5.145 -18.260 -11.935 1.00 16.16 ? 119 SER B N 1 ATOM 2950 C CA . SER B 1 119 ? 6.343 -17.660 -12.503 1.00 17.81 ? 119 SER B CA 1 ATOM 2951 C C . SER B 1 119 ? 5.933 -16.481 -13.413 1.00 17.44 ? 119 SER B C 1 ATOM 2952 O O . SER B 1 119 ? 6.502 -15.410 -13.338 1.00 17.51 ? 119 SER B O 1 ATOM 2953 C CB . SER B 1 119 ? 7.189 -18.696 -13.246 1.00 17.82 ? 119 SER B CB 1 ATOM 2954 O OG . SER B 1 119 ? 7.657 -19.698 -12.341 1.00 19.83 ? 119 SER B OG 1 ATOM 2955 N N . HIS B 1 120 ? 4.883 -16.671 -14.205 1.00 16.80 ? 120 HIS B N 1 ATOM 2956 C CA . HIS B 1 120 ? 4.428 -15.635 -15.088 1.00 16.60 ? 120 HIS B CA 1 ATOM 2957 C C . HIS B 1 120 ? 3.713 -14.475 -14.387 1.00 15.90 ? 120 HIS B C 1 ATOM 2958 O O . HIS B 1 120 ? 3.935 -13.323 -14.724 1.00 14.31 ? 120 HIS B O 1 ATOM 2959 C CB . HIS B 1 120 ? 3.503 -16.241 -16.111 1.00 17.47 ? 120 HIS B CB 1 ATOM 2960 C CG . HIS B 1 120 ? 2.999 -15.254 -17.114 1.00 18.47 ? 120 HIS B CG 1 ATOM 2961 N ND1 . HIS B 1 120 ? 3.664 -14.987 -18.291 1.00 18.86 ? 120 HIS B ND1 1 ATOM 2962 C CD2 . HIS B 1 120 ? 1.895 -14.474 -17.116 1.00 17.60 ? 120 HIS B CD2 1 ATOM 2963 C CE1 . HIS B 1 120 ? 2.974 -14.102 -18.987 1.00 18.41 ? 120 HIS B CE1 1 ATOM 2964 N NE2 . HIS B 1 120 ? 1.897 -13.779 -18.297 1.00 18.00 ? 120 HIS B NE2 1 ATOM 2965 N N . PHE B 1 121 ? 2.836 -14.788 -13.435 1.00 15.94 ? 121 PHE B N 1 ATOM 2966 C CA . PHE B 1 121 ? 2.127 -13.755 -12.728 1.00 15.77 ? 121 PHE B CA 1 ATOM 2967 C C . PHE B 1 121 ? 3.017 -12.906 -11.824 1.00 16.38 ? 121 PHE B C 1 ATOM 2968 O O . PHE B 1 121 ? 2.748 -11.706 -11.647 1.00 16.62 ? 121 PHE B O 1 ATOM 2969 C CB . PHE B 1 121 ? 0.952 -14.339 -11.968 1.00 15.24 ? 121 PHE B CB 1 ATOM 2970 C CG . PHE B 1 121 ? -0.085 -14.947 -12.868 1.00 15.93 ? 121 PHE B CG 1 ATOM 2971 C CD1 . PHE B 1 121 ? -0.335 -14.413 -14.147 1.00 15.20 ? 121 PHE B CD1 1 ATOM 2972 C CD2 . PHE B 1 121 ? -0.805 -16.074 -12.464 1.00 16.09 ? 121 PHE B CD2 1 ATOM 2973 C CE1 . PHE B 1 121 ? -1.266 -14.991 -14.982 1.00 15.22 ? 121 PHE B CE1 1 ATOM 2974 C CE2 . PHE B 1 121 ? -1.748 -16.626 -13.311 1.00 15.99 ? 121 PHE B CE2 1 ATOM 2975 C CZ . PHE B 1 121 ? -1.986 -16.071 -14.556 1.00 15.35 ? 121 PHE B CZ 1 ATOM 2976 N N . MET B 1 122 ? 4.036 -13.525 -11.224 1.00 16.29 ? 122 MET B N 1 ATOM 2977 C CA . MET B 1 122 ? 4.983 -12.774 -10.420 1.00 18.19 ? 122 MET B CA 1 ATOM 2978 C C . MET B 1 122 ? 5.686 -11.723 -11.303 1.00 16.05 ? 122 MET B C 1 ATOM 2979 O O . MET B 1 122 ? 5.884 -10.601 -10.889 1.00 16.38 ? 122 MET B O 1 ATOM 2980 C CB . MET B 1 122 ? 5.984 -13.713 -9.755 1.00 20.69 ? 122 MET B CB 1 ATOM 2981 C CG . MET B 1 122 ? 6.964 -13.003 -8.826 1.00 24.69 ? 122 MET B CG 1 ATOM 2982 S SD . MET B 1 122 ? 6.188 -12.151 -7.426 1.00 29.74 ? 122 MET B SD 1 ATOM 2983 C CE . MET B 1 122 ? 5.614 -13.547 -6.459 1.00 28.23 ? 122 MET B CE 1 ATOM 2984 N N . GLY B 1 123 ? 6.005 -12.092 -12.525 1.00 15.38 ? 123 GLY B N 1 ATOM 2985 C CA . GLY B 1 123 ? 6.429 -11.159 -13.549 1.00 16.20 ? 123 GLY B CA 1 ATOM 2986 C C . GLY B 1 123 ? 5.404 -10.084 -13.858 1.00 15.63 ? 123 GLY B C 1 ATOM 2987 O O . GLY B 1 123 ? 5.745 -8.913 -13.887 1.00 16.15 ? 123 GLY B O 1 ATOM 2988 N N . ASP B 1 124 ? 4.165 -10.478 -14.152 1.00 15.62 ? 124 ASP B N 1 ATOM 2989 C CA . ASP B 1 124 ? 3.131 -9.484 -14.544 1.00 14.80 ? 124 ASP B CA 1 ATOM 2990 C C . ASP B 1 124 ? 2.766 -8.558 -13.434 1.00 14.93 ? 124 ASP B C 1 ATOM 2991 O O . ASP B 1 124 ? 2.500 -7.408 -13.713 1.00 14.78 ? 124 ASP B O 1 ATOM 2992 C CB . ASP B 1 124 ? 1.829 -10.112 -15.098 1.00 14.62 ? 124 ASP B CB 1 ATOM 2993 C CG . ASP B 1 124 ? 1.893 -10.377 -16.604 1.00 13.81 ? 124 ASP B CG 1 ATOM 2994 O OD1 . ASP B 1 124 ? 2.931 -10.080 -17.207 1.00 13.11 ? 124 ASP B OD1 1 ATOM 2995 O OD2 . ASP B 1 124 ? 0.931 -10.923 -17.163 1.00 13.71 ? 124 ASP B OD2 1 ATOM 2996 N N . ILE B 1 125 ? 2.779 -9.010 -12.162 1.00 15.76 ? 125 ILE B N 1 ATOM 2997 C CA . ILE B 1 125 ? 2.418 -8.080 -11.075 1.00 14.58 ? 125 ILE B CA 1 ATOM 2998 C C . ILE B 1 125 ? 3.404 -6.923 -10.945 1.00 14.55 ? 125 ILE B C 1 ATOM 2999 O O . ILE B 1 125 ? 3.112 -5.887 -10.301 1.00 15.78 ? 125 ILE B O 1 ATOM 3000 C CB . ILE B 1 125 ? 2.172 -8.816 -9.729 1.00 14.82 ? 125 ILE B CB 1 ATOM 3001 C CG1 . ILE B 1 125 ? 1.190 -8.001 -8.856 1.00 15.68 ? 125 ILE B CG1 1 ATOM 3002 C CG2 . ILE B 1 125 ? 3.488 -9.105 -8.991 1.00 14.15 ? 125 ILE B CG2 1 ATOM 3003 C CD1 . ILE B 1 125 ? 0.499 -8.812 -7.739 1.00 16.00 ? 125 ILE B CD1 1 ATOM 3004 N N . HIS B 1 126 ? 4.569 -7.086 -11.551 1.00 13.91 ? 126 HIS B N 1 ATOM 3005 C CA . HIS B 1 126 ? 5.628 -6.058 -11.539 1.00 13.84 ? 126 HIS B CA 1 ATOM 3006 C C . HIS B 1 126 ? 5.661 -5.126 -12.740 1.00 14.09 ? 126 HIS B C 1 ATOM 3007 O O . HIS B 1 126 ? 6.352 -4.106 -12.711 1.00 13.95 ? 126 HIS B O 1 ATOM 3008 C CB . HIS B 1 126 ? 6.978 -6.738 -11.389 1.00 13.46 ? 126 HIS B CB 1 ATOM 3009 C CG . HIS B 1 126 ? 7.225 -7.194 -10.008 1.00 13.31 ? 126 HIS B CG 1 ATOM 3010 N ND1 . HIS B 1 126 ? 6.843 -8.437 -9.562 1.00 13.56 ? 126 HIS B ND1 1 ATOM 3011 C CD2 . HIS B 1 126 ? 7.780 -6.555 -8.947 1.00 13.60 ? 126 HIS B CD2 1 ATOM 3012 C CE1 . HIS B 1 126 ? 7.161 -8.555 -8.286 1.00 13.77 ? 126 HIS B CE1 1 ATOM 3013 N NE2 . HIS B 1 126 ? 7.742 -7.434 -7.897 1.00 14.24 ? 126 HIS B NE2 1 ATOM 3014 N N . GLN B 1 127 ? 4.895 -5.454 -13.784 1.00 14.25 ? 127 GLN B N 1 ATOM 3015 C CA . GLN B 1 127 ? 4.713 -4.544 -14.887 1.00 15.28 ? 127 GLN B CA 1 ATOM 3016 C C . GLN B 1 127 ? 3.753 -3.416 -14.400 1.00 15.11 ? 127 GLN B C 1 ATOM 3017 O O . GLN B 1 127 ? 2.606 -3.657 -14.047 1.00 16.21 ? 127 GLN B O 1 ATOM 3018 C CB . GLN B 1 127 ? 4.129 -5.269 -16.118 1.00 15.60 ? 127 GLN B CB 1 ATOM 3019 C CG . GLN B 1 127 ? 4.565 -4.745 -17.496 1.00 15.43 ? 127 GLN B CG 1 ATOM 3020 C CD . GLN B 1 127 ? 3.918 -3.420 -17.913 1.00 15.97 ? 127 GLN B CD 1 ATOM 3021 O OE1 . GLN B 1 127 ? 3.955 -2.417 -17.192 1.00 17.06 ? 127 GLN B OE1 1 ATOM 3022 N NE2 . GLN B 1 127 ? 3.326 -3.413 -19.104 1.00 15.88 ? 127 GLN B NE2 1 ATOM 3023 N N . PRO B 1 128 ? 4.214 -2.175 -14.401 1.00 16.53 ? 128 PRO B N 1 ATOM 3024 C CA . PRO B 1 128 ? 3.353 -1.129 -13.834 1.00 16.28 ? 128 PRO B CA 1 ATOM 3025 C C . PRO B 1 128 ? 1.942 -0.990 -14.488 1.00 17.04 ? 128 PRO B C 1 ATOM 3026 O O . PRO B 1 128 ? 0.920 -0.829 -13.801 1.00 16.92 ? 128 PRO B O 1 ATOM 3027 C CB . PRO B 1 128 ? 4.200 0.098 -14.020 1.00 16.11 ? 128 PRO B CB 1 ATOM 3028 C CG . PRO B 1 128 ? 5.588 -0.393 -13.897 1.00 15.87 ? 128 PRO B CG 1 ATOM 3029 C CD . PRO B 1 128 ? 5.543 -1.638 -14.741 1.00 16.57 ? 128 PRO B CD 1 ATOM 3030 N N . LEU B 1 129 ? 1.884 -1.104 -15.800 1.00 17.84 ? 129 LEU B N 1 ATOM 3031 C CA . LEU B 1 129 ? 0.616 -1.015 -16.475 1.00 18.43 ? 129 LEU B CA 1 ATOM 3032 C C . LEU B 1 129 ? -0.180 -2.325 -16.475 1.00 18.88 ? 129 LEU B C 1 ATOM 3033 O O . LEU B 1 129 ? -1.177 -2.402 -17.147 1.00 19.08 ? 129 LEU B O 1 ATOM 3034 C CB . LEU B 1 129 ? 0.805 -0.487 -17.882 1.00 19.29 ? 129 LEU B CB 1 ATOM 3035 C CG . LEU B 1 129 ? 1.315 0.955 -17.880 1.00 20.07 ? 129 LEU B CG 1 ATOM 3036 C CD1 . LEU B 1 129 ? 1.546 1.372 -19.319 1.00 21.39 ? 129 LEU B CD1 1 ATOM 3037 C CD2 . LEU B 1 129 ? 0.353 1.905 -17.155 1.00 21.02 ? 129 LEU B CD2 1 ATOM 3038 N N . HIS B 1 130 ? 0.231 -3.327 -15.691 1.00 17.02 ? 130 HIS B N 1 ATOM 3039 C CA . HIS B 1 130 ? -0.640 -4.463 -15.400 1.00 16.57 ? 130 HIS B CA 1 ATOM 3040 C C . HIS B 1 130 ? -1.393 -4.272 -14.086 1.00 17.06 ? 130 HIS B C 1 ATOM 3041 O O . HIS B 1 130 ? -2.146 -5.157 -13.671 1.00 18.30 ? 130 HIS B O 1 ATOM 3042 C CB . HIS B 1 130 ? 0.150 -5.768 -15.362 1.00 15.59 ? 130 HIS B CB 1 ATOM 3043 C CG . HIS B 1 130 ? 0.264 -6.429 -16.686 1.00 14.61 ? 130 HIS B CG 1 ATOM 3044 N ND1 . HIS B 1 130 ? -0.334 -7.624 -16.952 1.00 13.72 ? 130 HIS B ND1 1 ATOM 3045 C CD2 . HIS B 1 130 ? 0.883 -6.059 -17.834 1.00 15.44 ? 130 HIS B CD2 1 ATOM 3046 C CE1 . HIS B 1 130 ? -0.103 -7.971 -18.206 1.00 13.93 ? 130 HIS B CE1 1 ATOM 3047 N NE2 . HIS B 1 130 ? 0.632 -7.039 -18.766 1.00 13.93 ? 130 HIS B NE2 1 ATOM 3048 N N . VAL B 1 131 ? -1.151 -3.128 -13.450 1.00 18.10 ? 131 VAL B N 1 ATOM 3049 C CA . VAL B 1 131 ? -1.825 -2.676 -12.253 1.00 19.35 ? 131 VAL B CA 1 ATOM 3050 C C . VAL B 1 131 ? -2.089 -1.209 -12.512 1.00 21.31 ? 131 VAL B C 1 ATOM 3051 O O . VAL B 1 131 ? -1.349 -0.320 -12.070 1.00 22.83 ? 131 VAL B O 1 ATOM 3052 C CB . VAL B 1 131 ? -0.974 -2.855 -10.996 1.00 19.42 ? 131 VAL B CB 1 ATOM 3053 C CG1 . VAL B 1 131 ? -1.799 -2.497 -9.767 1.00 20.07 ? 131 VAL B CG1 1 ATOM 3054 C CG2 . VAL B 1 131 ? -0.484 -4.300 -10.894 1.00 19.12 ? 131 VAL B CG2 1 ATOM 3055 N N . SER B 1 132 ? -3.121 -0.960 -13.293 1.00 23.62 ? 132 SER B N 1 ATOM 3056 C CA . SER B 1 132 ? -3.368 0.379 -13.773 1.00 24.35 ? 132 SER B CA 1 ATOM 3057 C C . SER B 1 132 ? -4.844 0.565 -14.125 1.00 24.84 ? 132 SER B C 1 ATOM 3058 O O . SER B 1 132 ? -5.701 -0.202 -13.697 1.00 26.56 ? 132 SER B O 1 ATOM 3059 C CB . SER B 1 132 ? -2.403 0.713 -14.915 1.00 23.71 ? 132 SER B CB 1 ATOM 3060 O OG . SER B 1 132 ? -2.619 -0.120 -16.055 1.00 24.84 ? 132 SER B OG 1 ATOM 3061 N N . TYR B 1 133 ? -5.147 1.620 -14.854 1.00 25.69 ? 133 TYR B N 1 ATOM 3062 C CA . TYR B 1 133 ? -6.511 2.099 -14.949 1.00 25.76 ? 133 TYR B CA 1 ATOM 3063 C C . TYR B 1 133 ? -7.420 1.240 -15.810 1.00 25.45 ? 133 TYR B C 1 ATOM 3064 O O . TYR B 1 133 ? -7.080 0.942 -16.943 1.00 23.57 ? 133 TYR B O 1 ATOM 3065 C CB . TYR B 1 133 ? -6.496 3.508 -15.510 1.00 26.04 ? 133 TYR B CB 1 ATOM 3066 C CG . TYR B 1 133 ? -5.841 4.540 -14.621 1.00 27.10 ? 133 TYR B CG 1 ATOM 3067 C CD1 . TYR B 1 133 ? -5.466 4.254 -13.313 1.00 27.16 ? 133 TYR B CD1 1 ATOM 3068 C CD2 . TYR B 1 133 ? -5.629 5.825 -15.087 1.00 29.18 ? 133 TYR B CD2 1 ATOM 3069 C CE1 . TYR B 1 133 ? -4.876 5.211 -12.510 1.00 27.80 ? 133 TYR B CE1 1 ATOM 3070 C CE2 . TYR B 1 133 ? -5.063 6.797 -14.273 1.00 30.96 ? 133 TYR B CE2 1 ATOM 3071 C CZ . TYR B 1 133 ? -4.680 6.475 -12.992 1.00 29.49 ? 133 TYR B CZ 1 ATOM 3072 O OH . TYR B 1 133 ? -4.117 7.440 -12.195 1.00 33.15 ? 133 TYR B OH 1 ATOM 3073 N N . ALA B 1 134 ? -8.590 0.876 -15.274 1.00 24.40 ? 134 ALA B N 1 ATOM 3074 C CA . ALA B 1 134 ? -9.653 0.293 -16.098 1.00 25.92 ? 134 ALA B CA 1 ATOM 3075 C C . ALA B 1 134 ? -10.039 1.196 -17.278 1.00 25.17 ? 134 ALA B C 1 ATOM 3076 O O . ALA B 1 134 ? -10.389 0.688 -18.347 1.00 25.08 ? 134 ALA B O 1 ATOM 3077 C CB . ALA B 1 134 ? -10.899 0.012 -15.253 1.00 28.19 ? 134 ALA B CB 1 ATOM 3078 N N . SER B 1 135 ? -9.993 2.517 -17.088 1.00 23.68 ? 135 SER B N 1 ATOM 3079 C CA . SER B 1 135 ? -10.572 3.434 -18.067 1.00 24.59 ? 135 SER B CA 1 ATOM 3080 C C . SER B 1 135 ? -9.788 3.449 -19.388 1.00 26.34 ? 135 SER B C 1 ATOM 3081 O O . SER B 1 135 ? -10.363 3.690 -20.439 1.00 26.70 ? 135 SER B O 1 ATOM 3082 C CB . SER B 1 135 ? -10.661 4.865 -17.513 1.00 24.22 ? 135 SER B CB 1 ATOM 3083 O OG . SER B 1 135 ? -9.378 5.433 -17.343 1.00 23.49 ? 135 SER B OG 1 ATOM 3084 N N . ASP B 1 136 ? -8.483 3.197 -19.328 1.00 26.02 ? 136 ASP B N 1 ATOM 3085 C CA . ASP B 1 136 ? -7.668 3.107 -20.543 1.00 25.58 ? 136 ASP B CA 1 ATOM 3086 C C . ASP B 1 136 ? -7.139 1.690 -20.741 1.00 25.63 ? 136 ASP B C 1 ATOM 3087 O O . ASP B 1 136 ? -6.161 1.489 -21.438 1.00 24.17 ? 136 ASP B O 1 ATOM 3088 C CB . ASP B 1 136 ? -6.528 4.162 -20.538 1.00 25.21 ? 136 ASP B CB 1 ATOM 3089 C CG . ASP B 1 136 ? -5.724 4.176 -19.228 1.00 26.61 ? 136 ASP B CG 1 ATOM 3090 O OD1 . ASP B 1 136 ? -5.278 3.082 -18.827 1.00 27.60 ? 136 ASP B OD1 1 ATOM 3091 O OD2 . ASP B 1 136 ? -5.525 5.271 -18.604 1.00 26.73 ? 136 ASP B OD2 1 ATOM 3092 N N . LYS B 1 137 ? -7.811 0.708 -20.148 1.00 27.06 ? 137 LYS B N 1 ATOM 3093 C CA . LYS B 1 137 ? -7.388 -0.690 -20.239 1.00 28.50 ? 137 LYS B CA 1 ATOM 3094 C C . LYS B 1 137 ? -5.859 -0.837 -20.030 1.00 27.85 ? 137 LYS B C 1 ATOM 3095 O O . LYS B 1 137 ? -5.134 -1.441 -20.831 1.00 26.02 ? 137 LYS B O 1 ATOM 3096 C CB . LYS B 1 137 ? -7.827 -1.289 -21.581 1.00 33.59 ? 137 LYS B CB 1 ATOM 3097 C CG . LYS B 1 137 ? -9.136 -0.709 -22.117 1.00 38.47 ? 137 LYS B CG 1 ATOM 3098 C CD . LYS B 1 137 ? -9.769 -1.624 -23.151 1.00 40.12 ? 137 LYS B CD 1 ATOM 3099 C CE . LYS B 1 137 ? -10.534 -2.755 -22.474 1.00 42.47 ? 137 LYS B CE 1 ATOM 3100 N NZ . LYS B 1 137 ? -11.991 -2.458 -22.427 1.00 40.92 ? 137 LYS B NZ 1 ATOM 3101 N N . GLY B 1 138 ? -5.375 -0.241 -18.964 1.00 24.83 ? 138 GLY B N 1 ATOM 3102 C CA . GLY B 1 138 ? -3.995 -0.377 -18.585 1.00 28.14 ? 138 GLY B CA 1 ATOM 3103 C C . GLY B 1 138 ? -3.024 0.281 -19.544 1.00 27.07 ? 138 GLY B C 1 ATOM 3104 O O . GLY B 1 138 ? -1.870 -0.151 -19.641 1.00 26.57 ? 138 GLY B O 1 ATOM 3105 N N . GLY B 1 139 ? -3.500 1.314 -20.244 1.00 24.06 ? 139 GLY B N 1 ATOM 3106 C CA . GLY B 1 139 ? -2.703 2.021 -21.233 1.00 23.07 ? 139 GLY B CA 1 ATOM 3107 C C . GLY B 1 139 ? -2.847 1.526 -22.666 1.00 22.91 ? 139 GLY B C 1 ATOM 3108 O O . GLY B 1 139 ? -2.353 2.187 -23.582 1.00 19.57 ? 139 GLY B O 1 ATOM 3109 N N . ASN B 1 140 ? -3.510 0.380 -22.853 1.00 21.97 ? 140 ASN B N 1 ATOM 3110 C CA . ASN B 1 140 ? -3.788 -0.151 -24.182 1.00 23.53 ? 140 ASN B CA 1 ATOM 3111 C C . ASN B 1 140 ? -4.570 0.765 -25.104 1.00 24.77 ? 140 ASN B C 1 ATOM 3112 O O . ASN B 1 140 ? -4.483 0.594 -26.322 1.00 25.24 ? 140 ASN B O 1 ATOM 3113 C CB . ASN B 1 140 ? -4.558 -1.458 -24.131 1.00 23.28 ? 140 ASN B CB 1 ATOM 3114 C CG . ASN B 1 140 ? -3.669 -2.636 -23.892 1.00 24.00 ? 140 ASN B CG 1 ATOM 3115 O OD1 . ASN B 1 140 ? -3.076 -3.183 -24.838 1.00 24.04 ? 140 ASN B OD1 1 ATOM 3116 N ND2 . ASN B 1 140 ? -3.579 -3.062 -22.633 1.00 22.45 ? 140 ASN B ND2 1 ATOM 3117 N N . THR B 1 141 ? -5.343 1.694 -24.551 1.00 23.00 ? 141 THR B N 1 ATOM 3118 C CA . THR B 1 141 ? -6.074 2.626 -25.400 1.00 26.52 ? 141 THR B CA 1 ATOM 3119 C C . THR B 1 141 ? -5.341 3.944 -25.610 1.00 25.85 ? 141 THR B C 1 ATOM 3120 O O . THR B 1 141 ? -5.829 4.767 -26.348 1.00 28.83 ? 141 THR B O 1 ATOM 3121 C CB . THR B 1 141 ? -7.470 2.964 -24.832 1.00 25.27 ? 141 THR B CB 1 ATOM 3122 O OG1 . THR B 1 141 ? -7.316 3.601 -23.566 1.00 23.15 ? 141 THR B OG1 1 ATOM 3123 C CG2 . THR B 1 141 ? -8.306 1.713 -24.706 1.00 24.90 ? 141 THR B CG2 1 ATOM 3124 N N . ILE B 1 142 ? -4.194 4.148 -24.965 1.00 24.73 ? 142 ILE B N 1 ATOM 3125 C CA . ILE B 1 142 ? -3.427 5.350 -25.178 1.00 24.90 ? 142 ILE B CA 1 ATOM 3126 C C . ILE B 1 142 ? -2.432 5.082 -26.308 1.00 26.18 ? 142 ILE B C 1 ATOM 3127 O O . ILE B 1 142 ? -1.391 4.470 -26.076 1.00 23.07 ? 142 ILE B O 1 ATOM 3128 C CB . ILE B 1 142 ? -2.655 5.788 -23.916 1.00 24.87 ? 142 ILE B CB 1 ATOM 3129 C CG1 . ILE B 1 142 ? -3.623 6.202 -22.805 1.00 26.02 ? 142 ILE B CG1 1 ATOM 3130 C CG2 . ILE B 1 142 ? -1.704 6.925 -24.245 1.00 23.74 ? 142 ILE B CG2 1 ATOM 3131 C CD1 . ILE B 1 142 ? -2.963 6.393 -21.448 1.00 24.58 ? 142 ILE B CD1 1 ATOM 3132 N N . GLU B 1 143 ? -2.771 5.538 -27.518 1.00 28.90 ? 143 GLU B N 1 ATOM 3133 C CA . GLU B 1 143 ? -1.904 5.394 -28.686 1.00 32.47 ? 143 GLU B CA 1 ATOM 3134 C C . GLU B 1 143 ? -0.941 6.574 -28.781 1.00 29.78 ? 143 GLU B C 1 ATOM 3135 O O . GLU B 1 143 ? -1.334 7.732 -28.713 1.00 31.36 ? 143 GLU B O 1 ATOM 3136 C CB . GLU B 1 143 ? -2.711 5.244 -29.976 1.00 35.70 ? 143 GLU B CB 1 ATOM 3137 C CG . GLU B 1 143 ? -3.446 3.907 -30.099 1.00 41.62 ? 143 GLU B CG 1 ATOM 3138 C CD . GLU B 1 143 ? -2.643 2.748 -30.729 1.00 46.64 ? 143 GLU B CD 1 ATOM 3139 O OE1 . GLU B 1 143 ? -1.501 2.928 -31.241 1.00 48.16 ? 143 GLU B OE1 1 ATOM 3140 O OE2 . GLU B 1 143 ? -3.186 1.615 -30.726 1.00 50.40 ? 143 GLU B OE2 1 ATOM 3141 N N . VAL B 1 144 ? 0.329 6.230 -28.885 1.00 26.23 ? 144 VAL B N 1 ATOM 3142 C CA . VAL B 1 144 ? 1.423 7.162 -28.969 1.00 26.34 ? 144 VAL B CA 1 ATOM 3143 C C . VAL B 1 144 ? 2.348 6.618 -30.039 1.00 25.43 ? 144 VAL B C 1 ATOM 3144 O O . VAL B 1 144 ? 1.997 5.661 -30.734 1.00 24.60 ? 144 VAL B O 1 ATOM 3145 C CB . VAL B 1 144 ? 2.162 7.272 -27.623 1.00 28.43 ? 144 VAL B CB 1 ATOM 3146 C CG1 . VAL B 1 144 ? 1.305 8.004 -26.611 1.00 29.89 ? 144 VAL B CG1 1 ATOM 3147 C CG2 . VAL B 1 144 ? 2.552 5.908 -27.084 1.00 28.87 ? 144 VAL B CG2 1 ATOM 3148 N N . HIS B 1 145 ? 3.506 7.239 -30.200 1.00 24.93 ? 145 HIS B N 1 ATOM 3149 C CA . HIS B 1 145 ? 4.560 6.674 -31.021 1.00 24.00 ? 145 HIS B CA 1 ATOM 3150 C C . HIS B 1 145 ? 5.743 6.396 -30.126 1.00 21.20 ? 145 HIS B C 1 ATOM 3151 O O . HIS B 1 145 ? 6.062 7.171 -29.219 1.00 20.28 ? 145 HIS B O 1 ATOM 3152 C CB . HIS B 1 145 ? 4.981 7.641 -32.120 1.00 26.18 ? 145 HIS B CB 1 ATOM 3153 C CG . HIS B 1 145 ? 3.883 8.002 -33.057 1.00 28.16 ? 145 HIS B CG 1 ATOM 3154 N ND1 . HIS B 1 145 ? 2.922 8.941 -32.746 1.00 28.67 ? 145 HIS B ND1 1 ATOM 3155 C CD2 . HIS B 1 145 ? 3.597 7.562 -34.302 1.00 29.41 ? 145 HIS B CD2 1 ATOM 3156 C CE1 . HIS B 1 145 ? 2.091 9.062 -33.765 1.00 30.92 ? 145 HIS B CE1 1 ATOM 3157 N NE2 . HIS B 1 145 ? 2.484 8.239 -34.722 1.00 31.33 ? 145 HIS B NE2 1 ATOM 3158 N N . TRP B 1 146 ? 6.366 5.263 -30.383 1.00 19.75 ? 146 TRP B N 1 ATOM 3159 C CA . TRP B 1 146 ? 7.650 4.904 -29.838 1.00 18.57 ? 146 TRP B CA 1 ATOM 3160 C C . TRP B 1 146 ? 8.639 5.204 -30.951 1.00 19.44 ? 146 TRP B C 1 ATOM 3161 O O . TRP B 1 146 ? 8.758 4.435 -31.937 1.00 19.67 ? 146 TRP B O 1 ATOM 3162 C CB . TRP B 1 146 ? 7.707 3.417 -29.464 1.00 18.95 ? 146 TRP B CB 1 ATOM 3163 C CG . TRP B 1 146 ? 8.960 3.116 -28.726 1.00 19.28 ? 146 TRP B CG 1 ATOM 3164 C CD1 . TRP B 1 146 ? 10.010 2.349 -29.146 1.00 20.08 ? 146 TRP B CD1 1 ATOM 3165 C CD2 . TRP B 1 146 ? 9.337 3.658 -27.464 1.00 18.92 ? 146 TRP B CD2 1 ATOM 3166 N NE1 . TRP B 1 146 ? 11.009 2.350 -28.201 1.00 20.07 ? 146 TRP B NE1 1 ATOM 3167 C CE2 . TRP B 1 146 ? 10.612 3.141 -27.151 1.00 20.11 ? 146 TRP B CE2 1 ATOM 3168 C CE3 . TRP B 1 146 ? 8.712 4.516 -26.553 1.00 18.84 ? 146 TRP B CE3 1 ATOM 3169 C CZ2 . TRP B 1 146 ? 11.262 3.456 -25.974 1.00 18.61 ? 146 TRP B CZ2 1 ATOM 3170 C CZ3 . TRP B 1 146 ? 9.369 4.818 -25.369 1.00 17.75 ? 146 TRP B CZ3 1 ATOM 3171 C CH2 . TRP B 1 146 ? 10.631 4.304 -25.105 1.00 18.08 ? 146 TRP B CH2 1 ATOM 3172 N N . TYR B 1 147 ? 9.345 6.312 -30.788 1.00 19.04 ? 147 TYR B N 1 ATOM 3173 C CA . TYR B 1 147 ? 10.106 6.910 -31.852 1.00 21.45 ? 147 TYR B CA 1 ATOM 3174 C C . TYR B 1 147 ? 9.228 6.991 -33.120 1.00 22.57 ? 147 TYR B C 1 ATOM 3175 O O . TYR B 1 147 ? 8.234 7.752 -33.141 1.00 23.27 ? 147 TYR B O 1 ATOM 3176 C CB . TYR B 1 147 ? 11.417 6.143 -32.065 1.00 21.69 ? 147 TYR B CB 1 ATOM 3177 C CG . TYR B 1 147 ? 12.345 6.226 -30.890 1.00 21.81 ? 147 TYR B CG 1 ATOM 3178 C CD1 . TYR B 1 147 ? 12.201 5.367 -29.811 1.00 22.49 ? 147 TYR B CD1 1 ATOM 3179 C CD2 . TYR B 1 147 ? 13.377 7.159 -30.857 1.00 22.04 ? 147 TYR B CD2 1 ATOM 3180 C CE1 . TYR B 1 147 ? 13.066 5.424 -28.727 1.00 24.39 ? 147 TYR B CE1 1 ATOM 3181 C CE2 . TYR B 1 147 ? 14.257 7.220 -29.781 1.00 23.53 ? 147 TYR B CE2 1 ATOM 3182 C CZ . TYR B 1 147 ? 14.093 6.356 -28.715 1.00 24.16 ? 147 TYR B CZ 1 ATOM 3183 O OH . TYR B 1 147 ? 14.947 6.402 -27.639 1.00 26.06 ? 147 TYR B OH 1 ATOM 3184 N N . THR B 1 148 ? 9.555 6.193 -34.142 1.00 22.62 ? 148 THR B N 1 ATOM 3185 C CA . THR B 1 148 ? 8.895 6.268 -35.467 1.00 23.21 ? 148 THR B CA 1 ATOM 3186 C C . THR B 1 148 ? 7.777 5.231 -35.687 1.00 24.82 ? 148 THR B C 1 ATOM 3187 O O . THR B 1 148 ? 7.175 5.200 -36.772 1.00 26.83 ? 148 THR B O 1 ATOM 3188 C CB . THR B 1 148 ? 9.918 5.975 -36.586 1.00 22.56 ? 148 THR B CB 1 ATOM 3189 O OG1 . THR B 1 148 ? 10.445 4.654 -36.397 1.00 20.46 ? 148 THR B OG1 1 ATOM 3190 C CG2 . THR B 1 148 ? 11.016 6.946 -36.557 1.00 21.59 ? 148 THR B CG2 1 ATOM 3191 N N . ARG B 1 149 ? 7.516 4.365 -34.712 1.00 24.98 ? 149 ARG B N 1 ATOM 3192 C CA . ARG B 1 149 ? 6.408 3.419 -34.836 1.00 26.95 ? 149 ARG B CA 1 ATOM 3193 C C . ARG B 1 149 ? 5.281 3.692 -33.865 1.00 27.37 ? 149 ARG B C 1 ATOM 3194 O O . ARG B 1 149 ? 5.516 3.877 -32.651 1.00 24.92 ? 149 ARG B O 1 ATOM 3195 C CB . ARG B 1 149 ? 6.839 1.975 -34.650 1.00 30.21 ? 149 ARG B CB 1 ATOM 3196 C CG . ARG B 1 149 ? 6.042 1.065 -35.579 1.00 33.89 ? 149 ARG B CG 1 ATOM 3197 C CD . ARG B 1 149 ? 5.570 -0.226 -34.959 1.00 37.46 ? 149 ARG B CD 1 ATOM 3198 N NE . ARG B 1 149 ? 6.411 -1.339 -35.372 1.00 41.01 ? 149 ARG B NE 1 ATOM 3199 C CZ . ARG B 1 149 ? 7.382 -1.856 -34.633 1.00 44.90 ? 149 ARG B CZ 1 ATOM 3200 N NH1 . ARG B 1 149 ? 7.631 -1.373 -33.423 1.00 46.01 ? 149 ARG B NH1 1 ATOM 3201 N NH2 . ARG B 1 149 ? 8.105 -2.867 -35.108 1.00 45.32 ? 149 ARG B NH2 1 ATOM 3202 N N . LYS B 1 150 ? 4.064 3.695 -34.419 1.00 28.04 ? 150 LYS B N 1 ATOM 3203 C CA . LYS B 1 150 ? 2.823 3.749 -33.636 1.00 29.07 ? 150 LYS B CA 1 ATOM 3204 C C . LYS B 1 150 ? 2.788 2.595 -32.657 1.00 27.08 ? 150 LYS B C 1 ATOM 3205 O O . LYS B 1 150 ? 3.135 1.449 -32.985 1.00 25.85 ? 150 LYS B O 1 ATOM 3206 C CB . LYS B 1 150 ? 1.573 3.647 -34.540 1.00 31.71 ? 150 LYS B CB 1 ATOM 3207 C CG . LYS B 1 150 ? 0.818 4.956 -34.702 1.00 36.15 ? 150 LYS B CG 1 ATOM 3208 C CD . LYS B 1 150 ? -0.700 4.775 -34.652 1.00 40.25 ? 150 LYS B CD 1 ATOM 3209 C CE . LYS B 1 150 ? -1.232 3.965 -35.830 1.00 43.17 ? 150 LYS B CE 1 ATOM 3210 N NZ . LYS B 1 150 ? -0.889 4.595 -37.141 1.00 45.58 ? 150 LYS B NZ 1 ATOM 3211 N N . ALA B 1 151 ? 2.331 2.880 -31.463 1.00 25.24 ? 151 ALA B N 1 ATOM 3212 C CA . ALA B 1 151 ? 2.318 1.862 -30.416 1.00 25.75 ? 151 ALA B CA 1 ATOM 3213 C C . ALA B 1 151 ? 1.463 2.375 -29.279 1.00 24.63 ? 151 ALA B C 1 ATOM 3214 O O . ALA B 1 151 ? 1.366 3.587 -29.085 1.00 30.23 ? 151 ALA B O 1 ATOM 3215 C CB . ALA B 1 151 ? 3.735 1.587 -29.940 1.00 24.51 ? 151 ALA B CB 1 ATOM 3216 N N . ASN B 1 152 ? 0.831 1.496 -28.523 1.00 23.04 ? 152 ASN B N 1 ATOM 3217 C CA . ASN B 1 152 ? 0.129 1.993 -27.335 1.00 21.25 ? 152 ASN B CA 1 ATOM 3218 C C . ASN B 1 152 ? 1.033 1.975 -26.134 1.00 19.44 ? 152 ASN B C 1 ATOM 3219 O O . ASN B 1 152 ? 2.108 1.359 -26.159 1.00 17.97 ? 152 ASN B O 1 ATOM 3220 C CB . ASN B 1 152 ? -1.176 1.265 -27.071 1.00 22.24 ? 152 ASN B CB 1 ATOM 3221 C CG . ASN B 1 152 ? -0.974 -0.190 -26.762 1.00 21.42 ? 152 ASN B CG 1 ATOM 3222 O OD1 . ASN B 1 152 ? -0.508 -0.553 -25.683 1.00 20.51 ? 152 ASN B OD1 1 ATOM 3223 N ND2 . ASN B 1 152 ? -1.331 -1.029 -27.702 1.00 20.98 ? 152 ASN B ND2 1 ATOM 3224 N N . LEU B 1 153 ? 0.598 2.662 -25.076 1.00 19.18 ? 153 LEU B N 1 ATOM 3225 C CA . LEU B 1 153 ? 1.438 2.854 -23.923 1.00 18.72 ? 153 LEU B CA 1 ATOM 3226 C C . LEU B 1 153 ? 1.706 1.534 -23.254 1.00 18.94 ? 153 LEU B C 1 ATOM 3227 O O . LEU B 1 153 ? 2.815 1.282 -22.772 1.00 20.39 ? 153 LEU B O 1 ATOM 3228 C CB . LEU B 1 153 ? 0.833 3.869 -22.939 1.00 18.78 ? 153 LEU B CB 1 ATOM 3229 C CG . LEU B 1 153 ? 1.781 4.418 -21.869 1.00 18.65 ? 153 LEU B CG 1 ATOM 3230 C CD1 . LEU B 1 153 ? 3.070 4.915 -22.487 1.00 18.78 ? 153 LEU B CD1 1 ATOM 3231 C CD2 . LEU B 1 153 ? 1.123 5.542 -21.085 1.00 19.74 ? 153 LEU B CD2 1 ATOM 3232 N N . HIS B 1 154 ? 0.716 0.666 -23.230 1.00 18.05 ? 154 HIS B N 1 ATOM 3233 C CA . HIS B 1 154 ? 0.908 -0.593 -22.525 1.00 18.09 ? 154 HIS B CA 1 ATOM 3234 C C . HIS B 1 154 ? 2.035 -1.383 -23.130 1.00 17.32 ? 154 HIS B C 1 ATOM 3235 O O . HIS B 1 154 ? 2.861 -1.944 -22.402 1.00 15.73 ? 154 HIS B O 1 ATOM 3236 C CB . HIS B 1 154 ? -0.361 -1.436 -22.564 1.00 17.42 ? 154 HIS B CB 1 ATOM 3237 C CG . HIS B 1 154 ? -0.291 -2.664 -21.731 1.00 17.54 ? 154 HIS B CG 1 ATOM 3238 N ND1 . HIS B 1 154 ? -0.748 -2.715 -20.430 1.00 19.06 ? 154 HIS B ND1 1 ATOM 3239 C CD2 . HIS B 1 154 ? 0.155 -3.902 -22.017 1.00 17.84 ? 154 HIS B CD2 1 ATOM 3240 C CE1 . HIS B 1 154 ? -0.588 -3.932 -19.955 1.00 18.82 ? 154 HIS B CE1 1 ATOM 3241 N NE2 . HIS B 1 154 ? -0.027 -4.670 -20.894 1.00 18.47 ? 154 HIS B NE2 1 ATOM 3242 N N . HIS B 1 155 ? 2.022 -1.467 -24.460 1.00 18.17 ? 155 HIS B N 1 ATOM 3243 C CA . HIS B 1 155 ? 2.995 -2.259 -25.211 1.00 19.06 ? 155 HIS B CA 1 ATOM 3244 C C . HIS B 1 155 ? 4.371 -1.638 -25.052 1.00 18.32 ? 155 HIS B C 1 ATOM 3245 O O . HIS B 1 155 ? 5.375 -2.334 -25.015 1.00 16.69 ? 155 HIS B O 1 ATOM 3246 C CB . HIS B 1 155 ? 2.598 -2.344 -26.689 1.00 22.27 ? 155 HIS B CB 1 ATOM 3247 C CG . HIS B 1 155 ? 3.376 -3.352 -27.489 1.00 24.94 ? 155 HIS B CG 1 ATOM 3248 N ND1 . HIS B 1 155 ? 4.454 -3.009 -28.284 1.00 28.08 ? 155 HIS B ND1 1 ATOM 3249 C CD2 . HIS B 1 155 ? 3.220 -4.690 -27.633 1.00 28.75 ? 155 HIS B CD2 1 ATOM 3250 C CE1 . HIS B 1 155 ? 4.928 -4.092 -28.881 1.00 28.00 ? 155 HIS B CE1 1 ATOM 3251 N NE2 . HIS B 1 155 ? 4.197 -5.127 -28.502 1.00 29.37 ? 155 HIS B NE2 1 ATOM 3252 N N . ILE B 1 156 ? 4.429 -0.318 -24.891 1.00 18.17 ? 156 ILE B N 1 ATOM 3253 C CA . ILE B 1 156 ? 5.721 0.319 -24.651 1.00 17.04 ? 156 ILE B CA 1 ATOM 3254 C C . ILE B 1 156 ? 6.341 -0.268 -23.399 1.00 16.55 ? 156 ILE B C 1 ATOM 3255 O O . ILE B 1 156 ? 7.560 -0.532 -23.360 1.00 15.81 ? 156 ILE B O 1 ATOM 3256 C CB . ILE B 1 156 ? 5.591 1.844 -24.592 1.00 16.14 ? 156 ILE B CB 1 ATOM 3257 C CG1 . ILE B 1 156 ? 5.506 2.359 -26.047 1.00 16.18 ? 156 ILE B CG1 1 ATOM 3258 C CG2 . ILE B 1 156 ? 6.751 2.467 -23.851 1.00 15.40 ? 156 ILE B CG2 1 ATOM 3259 C CD1 . ILE B 1 156 ? 4.966 3.772 -26.187 1.00 16.36 ? 156 ILE B CD1 1 ATOM 3260 N N . TRP B 1 157 ? 5.501 -0.493 -22.390 1.00 15.57 ? 157 TRP B N 1 ATOM 3261 C CA . TRP B 1 157 ? 5.996 -1.016 -21.125 1.00 16.65 ? 157 TRP B CA 1 ATOM 3262 C C . TRP B 1 157 ? 6.128 -2.577 -21.146 1.00 17.29 ? 157 TRP B C 1 ATOM 3263 O O . TRP B 1 157 ? 6.944 -3.142 -20.424 1.00 18.91 ? 157 TRP B O 1 ATOM 3264 C CB . TRP B 1 157 ? 5.126 -0.520 -19.963 1.00 17.23 ? 157 TRP B CB 1 ATOM 3265 C CG . TRP B 1 157 ? 5.461 0.885 -19.622 1.00 16.97 ? 157 TRP B CG 1 ATOM 3266 C CD1 . TRP B 1 157 ? 5.123 1.986 -20.323 1.00 16.75 ? 157 TRP B CD1 1 ATOM 3267 C CD2 . TRP B 1 157 ? 6.276 1.326 -18.529 1.00 17.61 ? 157 TRP B CD2 1 ATOM 3268 N NE1 . TRP B 1 157 ? 5.666 3.104 -19.734 1.00 17.69 ? 157 TRP B NE1 1 ATOM 3269 C CE2 . TRP B 1 157 ? 6.376 2.723 -18.626 1.00 16.83 ? 157 TRP B CE2 1 ATOM 3270 C CE3 . TRP B 1 157 ? 6.922 0.671 -17.468 1.00 17.74 ? 157 TRP B CE3 1 ATOM 3271 C CZ2 . TRP B 1 157 ? 7.083 3.488 -17.701 1.00 18.17 ? 157 TRP B CZ2 1 ATOM 3272 C CZ3 . TRP B 1 157 ? 7.661 1.444 -16.550 1.00 17.92 ? 157 TRP B CZ3 1 ATOM 3273 C CH2 . TRP B 1 157 ? 7.720 2.830 -16.672 1.00 17.88 ? 157 TRP B CH2 1 ATOM 3274 N N . ASP B 1 158 ? 5.351 -3.260 -21.966 1.00 16.02 ? 158 ASP B N 1 ATOM 3275 C CA . ASP B 1 158 ? 5.518 -4.733 -22.074 1.00 16.10 ? 158 ASP B CA 1 ATOM 3276 C C . ASP B 1 158 ? 6.824 -5.072 -22.729 1.00 16.23 ? 158 ASP B C 1 ATOM 3277 O O . ASP B 1 158 ? 7.566 -5.930 -22.223 1.00 15.96 ? 158 ASP B O 1 ATOM 3278 C CB . ASP B 1 158 ? 4.389 -5.387 -22.847 1.00 15.40 ? 158 ASP B CB 1 ATOM 3279 C CG . ASP B 1 158 ? 3.251 -5.790 -21.965 1.00 15.85 ? 158 ASP B CG 1 ATOM 3280 O OD1 . ASP B 1 158 ? 3.472 -5.824 -20.732 1.00 15.31 ? 158 ASP B OD1 1 ATOM 3281 O OD2 . ASP B 1 158 ? 2.138 -6.073 -22.496 1.00 13.89 ? 158 ASP B OD2 1 ATOM 3282 N N . SER B 1 159 ? 7.118 -4.338 -23.809 1.00 16.26 ? 159 SER B N 1 ATOM 3283 C CA . SER B 1 159 ? 8.133 -4.716 -24.756 1.00 16.42 ? 159 SER B CA 1 ATOM 3284 C C . SER B 1 159 ? 9.072 -3.650 -25.261 1.00 16.75 ? 159 SER B C 1 ATOM 3285 O O . SER B 1 159 ? 10.268 -3.900 -25.310 1.00 16.36 ? 159 SER B O 1 ATOM 3286 C CB . SER B 1 159 ? 7.454 -5.353 -25.967 1.00 16.54 ? 159 SER B CB 1 ATOM 3287 O OG . SER B 1 159 ? 6.673 -6.432 -25.534 1.00 17.52 ? 159 SER B OG 1 ATOM 3288 N N . ASN B 1 160 ? 8.562 -2.489 -25.662 1.00 17.84 ? 160 ASN B N 1 ATOM 3289 C CA . ASN B 1 160 ? 9.398 -1.545 -26.430 1.00 19.54 ? 160 ASN B CA 1 ATOM 3290 C C . ASN B 1 160 ? 10.586 -1.003 -25.651 1.00 18.48 ? 160 ASN B C 1 ATOM 3291 O O . ASN B 1 160 ? 11.687 -0.965 -26.202 1.00 18.27 ? 160 ASN B O 1 ATOM 3292 C CB . ASN B 1 160 ? 8.590 -0.401 -27.057 1.00 21.20 ? 160 ASN B CB 1 ATOM 3293 C CG . ASN B 1 160 ? 7.477 -0.888 -27.992 1.00 23.20 ? 160 ASN B CG 1 ATOM 3294 O OD1 . ASN B 1 160 ? 6.301 -0.680 -27.723 1.00 27.92 ? 160 ASN B OD1 1 ATOM 3295 N ND2 . ASN B 1 160 ? 7.845 -1.532 -29.082 1.00 22.47 ? 160 ASN B ND2 1 ATOM 3296 N N . ILE B 1 161 ? 10.390 -0.592 -24.388 1.00 18.54 ? 161 ILE B N 1 ATOM 3297 C CA . ILE B 1 161 ? 11.510 -0.069 -23.584 1.00 17.64 ? 161 ILE B CA 1 ATOM 3298 C C . ILE B 1 161 ? 12.651 -1.105 -23.429 1.00 16.90 ? 161 ILE B C 1 ATOM 3299 O O . ILE B 1 161 ? 13.824 -0.832 -23.727 1.00 15.47 ? 161 ILE B O 1 ATOM 3300 C CB . ILE B 1 161 ? 11.085 0.443 -22.193 1.00 18.95 ? 161 ILE B CB 1 ATOM 3301 C CG1 . ILE B 1 161 ? 10.159 1.665 -22.318 1.00 19.12 ? 161 ILE B CG1 1 ATOM 3302 C CG2 . ILE B 1 161 ? 12.327 0.871 -21.381 1.00 19.04 ? 161 ILE B CG2 1 ATOM 3303 C CD1 . ILE B 1 161 ? 9.280 1.891 -21.120 1.00 19.45 ? 161 ILE B CD1 1 ATOM 3304 N N . ILE B 1 162 ? 12.299 -2.300 -22.992 1.00 16.66 ? 162 ILE B N 1 ATOM 3305 C CA . ILE B 1 162 ? 13.284 -3.388 -22.867 1.00 17.32 ? 162 ILE B CA 1 ATOM 3306 C C . ILE B 1 162 ? 13.966 -3.691 -24.228 1.00 17.63 ? 162 ILE B C 1 ATOM 3307 O O . ILE B 1 162 ? 15.198 -3.759 -24.328 1.00 17.56 ? 162 ILE B O 1 ATOM 3308 C CB . ILE B 1 162 ? 12.628 -4.670 -22.337 1.00 17.14 ? 162 ILE B CB 1 ATOM 3309 C CG1 . ILE B 1 162 ? 12.072 -4.435 -20.944 1.00 16.86 ? 162 ILE B CG1 1 ATOM 3310 C CG2 . ILE B 1 162 ? 13.624 -5.816 -22.325 1.00 16.81 ? 162 ILE B CG2 1 ATOM 3311 C CD1 . ILE B 1 162 ? 11.032 -5.433 -20.538 1.00 16.56 ? 162 ILE B CD1 1 ATOM 3312 N N . GLU B 1 163 ? 13.172 -3.812 -25.272 1.00 18.60 ? 163 GLU B N 1 ATOM 3313 C CA . GLU B 1 163 ? 13.704 -4.168 -26.589 1.00 21.99 ? 163 GLU B CA 1 ATOM 3314 C C . GLU B 1 163 ? 14.702 -3.131 -27.090 1.00 22.08 ? 163 GLU B C 1 ATOM 3315 O O . GLU B 1 163 ? 15.699 -3.460 -27.725 1.00 21.67 ? 163 GLU B O 1 ATOM 3316 C CB . GLU B 1 163 ? 12.554 -4.252 -27.590 1.00 26.47 ? 163 GLU B CB 1 ATOM 3317 C CG . GLU B 1 163 ? 11.792 -5.552 -27.565 1.00 29.35 ? 163 GLU B CG 1 ATOM 3318 C CD . GLU B 1 163 ? 10.695 -5.614 -28.625 1.00 33.35 ? 163 GLU B CD 1 ATOM 3319 O OE1 . GLU B 1 163 ? 10.029 -4.589 -28.902 1.00 34.79 ? 163 GLU B OE1 1 ATOM 3320 O OE2 . GLU B 1 163 ? 10.492 -6.714 -29.176 1.00 39.05 ? 163 GLU B OE2 1 ATOM 3321 N N . THR B 1 164 ? 14.390 -1.856 -26.840 1.00 21.76 ? 164 THR B N 1 ATOM 3322 C CA . THR B 1 164 ? 15.231 -0.768 -27.263 1.00 20.19 ? 164 THR B CA 1 ATOM 3323 C C . THR B 1 164 ? 16.540 -0.775 -26.510 1.00 20.79 ? 164 THR B C 1 ATOM 3324 O O . THR B 1 164 ? 17.586 -0.522 -27.102 1.00 20.68 ? 164 THR B O 1 ATOM 3325 C CB . THR B 1 164 ? 14.510 0.586 -27.078 1.00 19.93 ? 164 THR B CB 1 ATOM 3326 O OG1 . THR B 1 164 ? 13.348 0.632 -27.910 1.00 18.46 ? 164 THR B OG1 1 ATOM 3327 C CG2 . THR B 1 164 ? 15.418 1.746 -27.478 1.00 20.05 ? 164 THR B CG2 1 ATOM 3328 N N . ALA B 1 165 ? 16.489 -1.031 -25.200 1.00 21.01 ? 165 ALA B N 1 ATOM 3329 C CA . ALA B 1 165 ? 17.692 -1.059 -24.398 1.00 20.95 ? 165 ALA B CA 1 ATOM 3330 C C . ALA B 1 165 ? 18.547 -2.248 -24.834 1.00 22.38 ? 165 ALA B C 1 ATOM 3331 O O . ALA B 1 165 ? 19.760 -2.104 -24.987 1.00 22.93 ? 165 ALA B O 1 ATOM 3332 C CB . ALA B 1 165 ? 17.346 -1.157 -22.935 1.00 22.12 ? 165 ALA B CB 1 ATOM 3333 N N . GLU B 1 166 ? 17.899 -3.396 -25.058 1.00 22.83 ? 166 GLU B N 1 ATOM 3334 C CA . GLU B 1 166 ? 18.561 -4.597 -25.580 1.00 27.09 ? 166 GLU B CA 1 ATOM 3335 C C . GLU B 1 166 ? 19.434 -4.281 -26.803 1.00 27.71 ? 166 GLU B C 1 ATOM 3336 O O . GLU B 1 166 ? 20.611 -4.634 -26.838 1.00 25.50 ? 166 GLU B O 1 ATOM 3337 C CB . GLU B 1 166 ? 17.532 -5.676 -25.948 1.00 28.64 ? 166 GLU B CB 1 ATOM 3338 C CG . GLU B 1 166 ? 18.131 -7.039 -26.292 1.00 33.02 ? 166 GLU B CG 1 ATOM 3339 C CD . GLU B 1 166 ? 17.159 -8.017 -26.974 1.00 37.29 ? 166 GLU B CD 1 ATOM 3340 O OE1 . GLU B 1 166 ? 15.954 -7.686 -27.180 1.00 39.92 ? 166 GLU B OE1 1 ATOM 3341 O OE2 . GLU B 1 166 ? 17.607 -9.151 -27.290 1.00 40.66 ? 166 GLU B OE2 1 ATOM 3342 N N . ALA B 1 167 ? 18.845 -3.615 -27.798 1.00 29.12 ? 167 ALA B N 1 ATOM 3343 C CA . ALA B 1 167 ? 19.541 -3.361 -29.058 1.00 30.77 ? 167 ALA B CA 1 ATOM 3344 C C . ALA B 1 167 ? 20.512 -2.192 -28.928 1.00 33.56 ? 167 ALA B C 1 ATOM 3345 O O . ALA B 1 167 ? 21.568 -2.217 -29.531 1.00 30.65 ? 167 ALA B O 1 ATOM 3346 C CB . ALA B 1 167 ? 18.555 -3.091 -30.179 1.00 30.37 ? 167 ALA B CB 1 ATOM 3347 N N . ASP B 1 168 ? 20.153 -1.179 -28.133 1.00 37.06 ? 168 ASP B N 1 ATOM 3348 C CA . ASP B 1 168 ? 20.853 0.096 -28.182 1.00 42.15 ? 168 ASP B CA 1 ATOM 3349 C C . ASP B 1 168 ? 21.989 0.225 -27.139 1.00 43.26 ? 168 ASP B C 1 ATOM 3350 O O . ASP B 1 168 ? 22.920 1.008 -27.329 1.00 45.37 ? 168 ASP B O 1 ATOM 3351 C CB . ASP B 1 168 ? 19.857 1.264 -28.056 1.00 43.55 ? 168 ASP B CB 1 ATOM 3352 C CG . ASP B 1 168 ? 18.741 1.250 -29.147 1.00 45.84 ? 168 ASP B CG 1 ATOM 3353 O OD1 . ASP B 1 168 ? 18.462 0.220 -29.815 1.00 41.94 ? 168 ASP B OD1 1 ATOM 3354 O OD2 . ASP B 1 168 ? 18.099 2.304 -29.309 1.00 49.64 ? 168 ASP B OD2 1 ATOM 3355 N N . LEU B 1 169 ? 21.904 -0.517 -26.041 1.00 40.82 ? 169 LEU B N 1 ATOM 3356 C CA . LEU B 1 169 ? 22.959 -0.509 -25.021 1.00 37.00 ? 169 LEU B CA 1 ATOM 3357 C C . LEU B 1 169 ? 23.659 -1.852 -24.908 1.00 37.26 ? 169 LEU B C 1 ATOM 3358 O O . LEU B 1 169 ? 24.834 -1.889 -24.585 1.00 43.17 ? 169 LEU B O 1 ATOM 3359 C CB . LEU B 1 169 ? 22.385 -0.130 -23.645 1.00 37.23 ? 169 LEU B CB 1 ATOM 3360 C CG . LEU B 1 169 ? 21.431 1.082 -23.577 1.00 35.82 ? 169 LEU B CG 1 ATOM 3361 C CD1 . LEU B 1 169 ? 20.607 1.006 -22.311 1.00 35.34 ? 169 LEU B CD1 1 ATOM 3362 C CD2 . LEU B 1 169 ? 22.133 2.434 -23.692 1.00 32.42 ? 169 LEU B CD2 1 ATOM 3363 N N . TYR B 1 170 ? 22.950 -2.952 -25.172 1.00 37.57 ? 170 TYR B N 1 ATOM 3364 C CA . TYR B 1 170 ? 23.506 -4.311 -24.981 1.00 35.38 ? 170 TYR B CA 1 ATOM 3365 C C . TYR B 1 170 ? 23.737 -5.067 -26.265 1.00 37.63 ? 170 TYR B C 1 ATOM 3366 O O . TYR B 1 170 ? 23.783 -6.308 -26.265 1.00 39.91 ? 170 TYR B O 1 ATOM 3367 C CB . TYR B 1 170 ? 22.618 -5.126 -24.029 1.00 32.67 ? 170 TYR B CB 1 ATOM 3368 C CG . TYR B 1 170 ? 22.506 -4.460 -22.685 1.00 31.61 ? 170 TYR B CG 1 ATOM 3369 C CD1 . TYR B 1 170 ? 23.614 -4.373 -21.827 1.00 32.96 ? 170 TYR B CD1 1 ATOM 3370 C CD2 . TYR B 1 170 ? 21.329 -3.841 -22.297 1.00 31.11 ? 170 TYR B CD2 1 ATOM 3371 C CE1 . TYR B 1 170 ? 23.519 -3.731 -20.597 1.00 28.70 ? 170 TYR B CE1 1 ATOM 3372 C CE2 . TYR B 1 170 ? 21.229 -3.204 -21.088 1.00 29.07 ? 170 TYR B CE2 1 ATOM 3373 C CZ . TYR B 1 170 ? 22.323 -3.154 -20.247 1.00 29.27 ? 170 TYR B CZ 1 ATOM 3374 O OH . TYR B 1 170 ? 22.169 -2.505 -19.050 1.00 29.82 ? 170 TYR B OH 1 ATOM 3375 N N . ASN B 1 171 ? 23.908 -4.320 -27.356 1.00 43.69 ? 171 ASN B N 1 ATOM 3376 C CA . ASN B 1 171 ? 24.349 -4.886 -28.626 1.00 45.00 ? 171 ASN B CA 1 ATOM 3377 C C . ASN B 1 171 ? 23.640 -6.194 -28.922 1.00 47.91 ? 171 ASN B C 1 ATOM 3378 O O . ASN B 1 171 ? 24.279 -7.216 -29.199 1.00 47.56 ? 171 ASN B O 1 ATOM 3379 C CB . ASN B 1 171 ? 25.876 -5.056 -28.605 1.00 47.41 ? 171 ASN B CB 1 ATOM 3380 C CG . ASN B 1 171 ? 26.604 -3.719 -28.661 1.00 48.77 ? 171 ASN B CG 1 ATOM 3381 O OD1 . ASN B 1 171 ? 26.356 -2.918 -29.559 1.00 51.14 ? 171 ASN B OD1 1 ATOM 3382 N ND2 . ASN B 1 171 ? 27.496 -3.470 -27.707 1.00 48.05 ? 171 ASN B ND2 1 ATOM 3383 N N . SER B 1 172 ? 22.308 -6.148 -28.796 1.00 48.47 ? 172 SER B N 1 ATOM 3384 C CA . SER B 1 172 ? 21.397 -7.244 -29.157 1.00 47.01 ? 172 SER B CA 1 ATOM 3385 C C . SER B 1 172 ? 21.586 -8.550 -28.356 1.00 50.01 ? 172 SER B C 1 ATOM 3386 O O . SER B 1 172 ? 21.052 -9.604 -28.735 1.00 51.02 ? 172 SER B O 1 ATOM 3387 C CB . SER B 1 172 ? 21.452 -7.500 -30.680 1.00 46.72 ? 172 SER B CB 1 ATOM 3388 O OG . SER B 1 172 ? 20.518 -6.683 -31.379 1.00 44.26 ? 172 SER B OG 1 ATOM 3389 N N . ALA B 1 173 ? 22.313 -8.474 -27.239 1.00 51.42 ? 173 ALA B N 1 ATOM 3390 C CA . ALA B 1 173 ? 22.544 -9.631 -26.376 1.00 48.76 ? 173 ALA B CA 1 ATOM 3391 C C . ALA B 1 173 ? 21.763 -9.449 -25.068 1.00 44.63 ? 173 ALA B C 1 ATOM 3392 O O . ALA B 1 173 ? 22.163 -8.670 -24.188 1.00 44.09 ? 173 ALA B O 1 ATOM 3393 C CB . ALA B 1 173 ? 24.031 -9.802 -26.100 1.00 48.05 ? 173 ALA B CB 1 ATOM 3394 N N . LEU B 1 174 ? 20.647 -10.171 -24.959 1.00 42.38 ? 174 LEU B N 1 ATOM 3395 C CA . LEU B 1 174 ? 19.792 -10.148 -23.759 1.00 39.98 ? 174 LEU B CA 1 ATOM 3396 C C . LEU B 1 174 ? 20.553 -10.575 -22.482 1.00 39.21 ? 174 LEU B C 1 ATOM 3397 O O . LEU B 1 174 ? 20.428 -9.910 -21.435 1.00 36.18 ? 174 LEU B O 1 ATOM 3398 C CB . LEU B 1 174 ? 18.539 -11.023 -23.968 1.00 39.09 ? 174 LEU B CB 1 ATOM 3399 C CG . LEU B 1 174 ? 17.468 -11.059 -22.853 1.00 39.20 ? 174 LEU B CG 1 ATOM 3400 C CD1 . LEU B 1 174 ? 16.052 -10.925 -23.409 1.00 37.47 ? 174 LEU B CD1 1 ATOM 3401 C CD2 . LEU B 1 174 ? 17.575 -12.319 -21.992 1.00 39.29 ? 174 LEU B CD2 1 ATOM 3402 N N . GLU B 1 175 ? 21.351 -11.650 -22.554 1.00 36.16 ? 175 GLU B N 1 ATOM 3403 C CA . GLU B 1 175 ? 22.137 -12.043 -21.380 1.00 37.43 ? 175 GLU B CA 1 ATOM 3404 C C . GLU B 1 175 ? 22.935 -10.834 -20.829 1.00 32.04 ? 175 GLU B C 1 ATOM 3405 O O . GLU B 1 175 ? 23.311 -10.848 -19.688 1.00 28.79 ? 175 GLU B O 1 ATOM 3406 C CB . GLU B 1 175 ? 23.110 -13.213 -21.637 1.00 40.50 ? 175 GLU B CB 1 ATOM 3407 C CG . GLU B 1 175 ? 22.528 -14.631 -21.618 1.00 44.15 ? 175 GLU B CG 1 ATOM 3408 C CD . GLU B 1 175 ? 21.457 -14.873 -20.567 1.00 46.95 ? 175 GLU B CD 1 ATOM 3409 O OE1 . GLU B 1 175 ? 21.749 -14.780 -19.344 1.00 51.29 ? 175 GLU B OE1 1 ATOM 3410 O OE2 . GLU B 1 175 ? 20.316 -15.179 -20.973 1.00 44.80 ? 175 GLU B OE2 1 ATOM 3411 N N . GLY B 1 176 ? 23.205 -9.830 -21.658 1.00 28.70 ? 176 GLY B N 1 ATOM 3412 C CA . GLY B 1 176 ? 23.944 -8.645 -21.243 1.00 25.98 ? 176 GLY B CA 1 ATOM 3413 C C . GLY B 1 176 ? 23.214 -7.787 -20.228 1.00 26.02 ? 176 GLY B C 1 ATOM 3414 O O . GLY B 1 176 ? 23.787 -7.340 -19.216 1.00 21.77 ? 176 GLY B O 1 ATOM 3415 N N . MET B 1 177 ? 21.955 -7.518 -20.539 1.00 24.10 ? 177 MET B N 1 ATOM 3416 C CA . MET B 1 177 ? 21.059 -6.894 -19.614 1.00 24.55 ? 177 MET B CA 1 ATOM 3417 C C . MET B 1 177 ? 20.840 -7.727 -18.343 1.00 22.36 ? 177 MET B C 1 ATOM 3418 O O . MET B 1 177 ? 20.826 -7.179 -17.253 1.00 22.23 ? 177 MET B O 1 ATOM 3419 C CB . MET B 1 177 ? 19.707 -6.682 -20.305 1.00 25.44 ? 177 MET B CB 1 ATOM 3420 C CG . MET B 1 177 ? 18.857 -5.635 -19.624 1.00 26.02 ? 177 MET B CG 1 ATOM 3421 S SD . MET B 1 177 ? 17.198 -5.630 -20.309 1.00 28.44 ? 177 MET B SD 1 ATOM 3422 C CE . MET B 1 177 ? 17.494 -4.809 -21.861 1.00 27.52 ? 177 MET B CE 1 ATOM 3423 N N . VAL B 1 178 ? 20.658 -9.043 -18.485 1.00 22.06 ? 178 VAL B N 1 ATOM 3424 C CA . VAL B 1 178 ? 20.465 -9.918 -17.327 1.00 22.08 ? 178 VAL B CA 1 ATOM 3425 C C . VAL B 1 178 ? 21.706 -9.883 -16.414 1.00 22.18 ? 178 VAL B C 1 ATOM 3426 O O . VAL B 1 178 ? 21.569 -9.652 -15.197 1.00 21.21 ? 178 VAL B O 1 ATOM 3427 C CB . VAL B 1 178 ? 20.024 -11.369 -17.701 1.00 23.58 ? 178 VAL B CB 1 ATOM 3428 C CG1 . VAL B 1 178 ? 19.973 -12.268 -16.461 1.00 23.45 ? 178 VAL B CG1 1 ATOM 3429 C CG2 . VAL B 1 178 ? 18.632 -11.377 -18.322 1.00 22.76 ? 178 VAL B CG2 1 ATOM 3430 N N . ASP B 1 179 ? 22.898 -9.976 -17.002 1.00 21.36 ? 179 ASP B N 1 ATOM 3431 C CA . ASP B 1 179 ? 24.127 -9.877 -16.221 1.00 23.28 ? 179 ASP B CA 1 ATOM 3432 C C . ASP B 1 179 ? 24.175 -8.530 -15.476 1.00 20.87 ? 179 ASP B C 1 ATOM 3433 O O . ASP B 1 179 ? 24.345 -8.527 -14.286 1.00 19.17 ? 179 ASP B O 1 ATOM 3434 C CB . ASP B 1 179 ? 25.370 -10.068 -17.077 1.00 25.97 ? 179 ASP B CB 1 ATOM 3435 C CG . ASP B 1 179 ? 25.311 -11.324 -17.903 1.00 30.97 ? 179 ASP B CG 1 ATOM 3436 O OD1 . ASP B 1 179 ? 25.296 -12.401 -17.287 1.00 35.24 ? 179 ASP B OD1 1 ATOM 3437 O OD2 . ASP B 1 179 ? 25.262 -11.220 -19.159 1.00 31.16 ? 179 ASP B OD2 1 ATOM 3438 N N . ALA B 1 180 ? 23.930 -7.411 -16.158 1.00 19.53 ? 180 ALA B N 1 ATOM 3439 C CA . ALA B 1 180 ? 23.903 -6.096 -15.468 1.00 20.39 ? 180 ALA B CA 1 ATOM 3440 C C . ALA B 1 180 ? 22.832 -5.965 -14.366 1.00 20.00 ? 180 ALA B C 1 ATOM 3441 O O . ALA B 1 180 ? 23.079 -5.312 -13.380 1.00 21.83 ? 180 ALA B O 1 ATOM 3442 C CB . ALA B 1 180 ? 23.706 -4.982 -16.474 1.00 22.12 ? 180 ALA B CB 1 ATOM 3443 N N . LEU B 1 181 ? 21.628 -6.517 -14.542 1.00 20.82 ? 181 LEU B N 1 ATOM 3444 C CA . LEU B 1 181 ? 20.642 -6.526 -13.426 1.00 20.20 ? 181 LEU B CA 1 ATOM 3445 C C . LEU B 1 181 ? 21.181 -7.339 -12.234 1.00 20.68 ? 181 LEU B C 1 ATOM 3446 O O . LEU B 1 181 ? 21.152 -6.866 -11.099 1.00 19.16 ? 181 LEU B O 1 ATOM 3447 C CB . LEU B 1 181 ? 19.305 -7.109 -13.842 1.00 19.43 ? 181 LEU B CB 1 ATOM 3448 C CG . LEU B 1 181 ? 18.598 -6.355 -14.958 1.00 18.82 ? 181 LEU B CG 1 ATOM 3449 C CD1 . LEU B 1 181 ? 17.451 -7.123 -15.551 1.00 18.63 ? 181 LEU B CD1 1 ATOM 3450 C CD2 . LEU B 1 181 ? 18.101 -5.013 -14.497 1.00 18.91 ? 181 LEU B CD2 1 ATOM 3451 N N . LYS B 1 182 ? 21.669 -8.550 -12.500 1.00 21.27 ? 182 LYS B N 1 ATOM 3452 C CA . LYS B 1 182 ? 22.259 -9.360 -11.450 1.00 22.49 ? 182 LYS B CA 1 ATOM 3453 C C . LYS B 1 182 ? 23.374 -8.585 -10.776 1.00 22.52 ? 182 LYS B C 1 ATOM 3454 O O . LYS B 1 182 ? 23.490 -8.622 -9.560 1.00 22.71 ? 182 LYS B O 1 ATOM 3455 C CB . LYS B 1 182 ? 22.783 -10.690 -11.973 1.00 23.98 ? 182 LYS B CB 1 ATOM 3456 C CG . LYS B 1 182 ? 21.741 -11.744 -12.362 1.00 26.12 ? 182 LYS B CG 1 ATOM 3457 C CD . LYS B 1 182 ? 22.500 -12.879 -13.058 1.00 29.34 ? 182 LYS B CD 1 ATOM 3458 C CE . LYS B 1 182 ? 21.695 -14.134 -13.337 1.00 32.25 ? 182 LYS B CE 1 ATOM 3459 N NZ . LYS B 1 182 ? 22.413 -14.979 -14.350 1.00 32.36 ? 182 LYS B NZ 1 ATOM 3460 N N . LYS B 1 183 ? 24.190 -7.863 -11.551 1.00 24.44 ? 183 LYS B N 1 ATOM 3461 C CA . LYS B 1 183 ? 25.294 -7.106 -10.967 1.00 24.42 ? 183 LYS B CA 1 ATOM 3462 C C . LYS B 1 183 ? 24.763 -6.033 -10.015 1.00 24.36 ? 183 LYS B C 1 ATOM 3463 O O . LYS B 1 183 ? 25.273 -5.876 -8.912 1.00 23.47 ? 183 LYS B O 1 ATOM 3464 C CB . LYS B 1 183 ? 26.171 -6.466 -12.031 1.00 28.70 ? 183 LYS B CB 1 ATOM 3465 C CG . LYS B 1 183 ? 27.388 -5.735 -11.450 1.00 30.97 ? 183 LYS B CG 1 ATOM 3466 C CD . LYS B 1 183 ? 27.914 -4.625 -12.374 1.00 34.22 ? 183 LYS B CD 1 ATOM 3467 C CE . LYS B 1 183 ? 29.109 -5.073 -13.214 1.00 34.73 ? 183 LYS B CE 1 ATOM 3468 N NZ . LYS B 1 183 ? 30.244 -4.123 -13.026 1.00 36.31 ? 183 LYS B NZ 1 ATOM 3469 N N . ASN B 1 184 ? 23.771 -5.274 -10.442 1.00 23.97 ? 184 ASN B N 1 ATOM 3470 C CA . ASN B 1 184 ? 23.165 -4.262 -9.547 1.00 24.57 ? 184 ASN B CA 1 ATOM 3471 C C . ASN B 1 184 ? 22.407 -4.817 -8.336 1.00 26.03 ? 184 ASN B C 1 ATOM 3472 O O . ASN B 1 184 ? 22.411 -4.207 -7.252 1.00 28.18 ? 184 ASN B O 1 ATOM 3473 C CB . ASN B 1 184 ? 22.302 -3.313 -10.350 1.00 24.57 ? 184 ASN B CB 1 ATOM 3474 C CG . ASN B 1 184 ? 23.143 -2.384 -11.166 1.00 25.24 ? 184 ASN B CG 1 ATOM 3475 O OD1 . ASN B 1 184 ? 24.357 -2.411 -11.056 1.00 26.43 ? 184 ASN B OD1 1 ATOM 3476 N ND2 . ASN B 1 184 ? 22.523 -1.581 -11.988 1.00 26.26 ? 184 ASN B ND2 1 ATOM 3477 N N . ILE B 1 185 ? 21.781 -5.975 -8.506 1.00 25.36 ? 185 ILE B N 1 ATOM 3478 C CA . ILE B 1 185 ? 21.175 -6.667 -7.368 1.00 26.62 ? 185 ILE B CA 1 ATOM 3479 C C . ILE B 1 185 ? 22.244 -6.955 -6.280 1.00 28.93 ? 185 ILE B C 1 ATOM 3480 O O . ILE B 1 185 ? 21.973 -6.777 -5.082 1.00 24.62 ? 185 ILE B O 1 ATOM 3481 C CB . ILE B 1 185 ? 20.489 -7.964 -7.816 1.00 26.04 ? 185 ILE B CB 1 ATOM 3482 C CG1 . ILE B 1 185 ? 19.181 -7.627 -8.544 1.00 25.88 ? 185 ILE B CG1 1 ATOM 3483 C CG2 . ILE B 1 185 ? 20.244 -8.893 -6.637 1.00 27.52 ? 185 ILE B CG2 1 ATOM 3484 C CD1 . ILE B 1 185 ? 18.529 -8.798 -9.247 1.00 24.80 ? 185 ILE B CD1 1 ATOM 3485 N N . THR B 1 186 ? 23.431 -7.417 -6.704 1.00 29.19 ? 186 THR B N 1 ATOM 3486 C CA . THR B 1 186 ? 24.508 -7.720 -5.765 1.00 33.27 ? 186 THR B CA 1 ATOM 3487 C C . THR B 1 186 ? 25.156 -6.499 -5.136 1.00 31.00 ? 186 THR B C 1 ATOM 3488 O O . THR B 1 186 ? 25.386 -6.510 -3.943 1.00 35.85 ? 186 THR B O 1 ATOM 3489 C CB . THR B 1 186 ? 25.636 -8.571 -6.387 1.00 37.66 ? 186 THR B CB 1 ATOM 3490 O OG1 . THR B 1 186 ? 25.077 -9.607 -7.198 1.00 39.42 ? 186 THR B OG1 1 ATOM 3491 C CG2 . THR B 1 186 ? 26.467 -9.207 -5.287 1.00 38.76 ? 186 THR B CG2 1 ATOM 3492 N N . THR B 1 187 ? 25.442 -5.459 -5.915 1.00 31.12 ? 187 THR B N 1 ATOM 3493 C CA . THR B 1 187 ? 26.365 -4.413 -5.476 1.00 36.15 ? 187 THR B CA 1 ATOM 3494 C C . THR B 1 187 ? 25.835 -2.987 -5.417 1.00 37.75 ? 187 THR B C 1 ATOM 3495 O O . THR B 1 187 ? 26.507 -2.102 -4.887 1.00 44.59 ? 187 THR B O 1 ATOM 3496 C CB . THR B 1 187 ? 27.588 -4.368 -6.387 1.00 36.88 ? 187 THR B CB 1 ATOM 3497 O OG1 . THR B 1 187 ? 27.174 -3.979 -7.699 1.00 39.47 ? 187 THR B OG1 1 ATOM 3498 C CG2 . THR B 1 187 ? 28.271 -5.757 -6.424 1.00 38.42 ? 187 THR B CG2 1 ATOM 3499 N N . GLU B 1 188 ? 24.681 -2.745 -6.009 1.00 37.88 ? 188 GLU B N 1 ATOM 3500 C CA . GLU B 1 188 ? 24.079 -1.428 -5.977 1.00 38.14 ? 188 GLU B CA 1 ATOM 3501 C C . GLU B 1 188 ? 22.813 -1.436 -5.140 1.00 34.87 ? 188 GLU B C 1 ATOM 3502 O O . GLU B 1 188 ? 22.556 -0.482 -4.420 1.00 34.43 ? 188 GLU B O 1 ATOM 3503 C CB . GLU B 1 188 ? 23.759 -0.951 -7.397 1.00 39.66 ? 188 GLU B CB 1 ATOM 3504 C CG . GLU B 1 188 ? 24.944 -0.372 -8.149 1.00 43.13 ? 188 GLU B CG 1 ATOM 3505 C CD . GLU B 1 188 ? 25.332 1.023 -7.667 1.00 45.69 ? 188 GLU B CD 1 ATOM 3506 O OE1 . GLU B 1 188 ? 25.748 1.172 -6.491 1.00 49.52 ? 188 GLU B OE1 1 ATOM 3507 O OE2 . GLU B 1 188 ? 25.197 1.990 -8.453 1.00 51.83 ? 188 GLU B OE2 1 ATOM 3508 N N . TRP B 1 189 ? 22.020 -2.501 -5.253 1.00 31.25 ? 189 TRP B N 1 ATOM 3509 C CA . TRP B 1 189 ? 20.704 -2.555 -4.621 1.00 30.06 ? 189 TRP B CA 1 ATOM 3510 C C . TRP B 1 189 ? 20.613 -3.531 -3.472 1.00 29.39 ? 189 TRP B C 1 ATOM 3511 O O . TRP B 1 189 ? 19.507 -3.832 -3.015 1.00 27.74 ? 189 TRP B O 1 ATOM 3512 C CB . TRP B 1 189 ? 19.651 -2.938 -5.653 1.00 30.61 ? 189 TRP B CB 1 ATOM 3513 C CG . TRP B 1 189 ? 19.644 -2.074 -6.850 1.00 30.96 ? 189 TRP B CG 1 ATOM 3514 C CD1 . TRP B 1 189 ? 19.912 -0.747 -6.900 1.00 30.27 ? 189 TRP B CD1 1 ATOM 3515 C CD2 . TRP B 1 189 ? 19.327 -2.476 -8.191 1.00 30.56 ? 189 TRP B CD2 1 ATOM 3516 N NE1 . TRP B 1 189 ? 19.803 -0.293 -8.188 1.00 31.46 ? 189 TRP B NE1 1 ATOM 3517 C CE2 . TRP B 1 189 ? 19.426 -1.331 -8.999 1.00 30.86 ? 189 TRP B CE2 1 ATOM 3518 C CE3 . TRP B 1 189 ? 18.968 -3.690 -8.782 1.00 28.86 ? 189 TRP B CE3 1 ATOM 3519 C CZ2 . TRP B 1 189 ? 19.181 -1.366 -10.376 1.00 30.08 ? 189 TRP B CZ2 1 ATOM 3520 C CZ3 . TRP B 1 189 ? 18.718 -3.719 -10.138 1.00 28.34 ? 189 TRP B CZ3 1 ATOM 3521 C CH2 . TRP B 1 189 ? 18.822 -2.565 -10.919 1.00 28.81 ? 189 TRP B CH2 1 ATOM 3522 N N . ALA B 1 190 ? 21.759 -4.015 -2.986 1.00 30.77 ? 190 ALA B N 1 ATOM 3523 C CA . ALA B 1 190 ? 21.782 -5.041 -1.941 1.00 32.27 ? 190 ALA B CA 1 ATOM 3524 C C . ALA B 1 190 ? 20.866 -4.711 -0.750 1.00 33.90 ? 190 ALA B C 1 ATOM 3525 O O . ALA B 1 190 ? 20.048 -5.529 -0.317 1.00 32.54 ? 190 ALA B O 1 ATOM 3526 C CB . ALA B 1 190 ? 23.205 -5.279 -1.464 1.00 33.49 ? 190 ALA B CB 1 ATOM 3527 N N . ASP B 1 191 ? 21.003 -3.507 -0.222 1.00 32.77 ? 191 ASP B N 1 ATOM 3528 C CA . ASP B 1 191 ? 20.122 -3.066 0.851 1.00 38.42 ? 191 ASP B CA 1 ATOM 3529 C C . ASP B 1 191 ? 18.623 -3.150 0.482 1.00 34.70 ? 191 ASP B C 1 ATOM 3530 O O . ASP B 1 191 ? 17.831 -3.711 1.242 1.00 39.21 ? 191 ASP B O 1 ATOM 3531 C CB . ASP B 1 191 ? 20.514 -1.648 1.293 1.00 41.43 ? 191 ASP B CB 1 ATOM 3532 C CG . ASP B 1 191 ? 19.471 -1.007 2.144 1.00 46.12 ? 191 ASP B CG 1 ATOM 3533 O OD1 . ASP B 1 191 ? 18.291 -1.080 1.752 1.00 51.58 ? 191 ASP B OD1 1 ATOM 3534 O OD2 . ASP B 1 191 ? 19.819 -0.410 3.187 1.00 49.37 ? 191 ASP B OD2 1 ATOM 3535 N N . GLN B 1 192 ? 18.241 -2.601 -0.671 1.00 30.80 ? 192 GLN B N 1 ATOM 3536 C CA . GLN B 1 192 ? 16.853 -2.693 -1.163 1.00 29.27 ? 192 GLN B CA 1 ATOM 3537 C C . GLN B 1 192 ? 16.390 -4.139 -1.389 1.00 29.34 ? 192 GLN B C 1 ATOM 3538 O O . GLN B 1 192 ? 15.266 -4.510 -1.051 1.00 29.20 ? 192 GLN B O 1 ATOM 3539 C CB . GLN B 1 192 ? 16.723 -1.980 -2.495 1.00 28.59 ? 192 GLN B CB 1 ATOM 3540 C CG . GLN B 1 192 ? 16.872 -0.494 -2.445 1.00 28.70 ? 192 GLN B CG 1 ATOM 3541 C CD . GLN B 1 192 ? 17.042 0.081 -3.828 1.00 29.30 ? 192 GLN B CD 1 ATOM 3542 O OE1 . GLN B 1 192 ? 16.081 0.177 -4.601 1.00 28.78 ? 192 GLN B OE1 1 ATOM 3543 N NE2 . GLN B 1 192 ? 18.265 0.476 -4.152 1.00 28.99 ? 192 GLN B NE2 1 ATOM 3544 N N . VAL B 1 193 ? 17.257 -4.939 -1.996 1.00 28.10 ? 193 VAL B N 1 ATOM 3545 C CA . VAL B 1 193 ? 16.953 -6.345 -2.276 1.00 27.47 ? 193 VAL B CA 1 ATOM 3546 C C . VAL B 1 193 ? 16.430 -7.077 -1.050 1.00 29.07 ? 193 VAL B C 1 ATOM 3547 O O . VAL B 1 193 ? 15.497 -7.873 -1.164 1.00 29.57 ? 193 VAL B O 1 ATOM 3548 C CB . VAL B 1 193 ? 18.181 -7.081 -2.848 1.00 25.95 ? 193 VAL B CB 1 ATOM 3549 C CG1 . VAL B 1 193 ? 17.982 -8.576 -2.855 1.00 24.53 ? 193 VAL B CG1 1 ATOM 3550 C CG2 . VAL B 1 193 ? 18.481 -6.586 -4.268 1.00 27.58 ? 193 VAL B CG2 1 ATOM 3551 N N . LYS B 1 194 ? 17.016 -6.802 0.116 1.00 32.78 ? 194 LYS B N 1 ATOM 3552 C CA . LYS B 1 194 ? 16.624 -7.478 1.355 1.00 33.08 ? 194 LYS B CA 1 ATOM 3553 C C . LYS B 1 194 ? 15.169 -7.126 1.761 1.00 30.74 ? 194 LYS B C 1 ATOM 3554 O O . LYS B 1 194 ? 14.417 -7.967 2.248 1.00 31.33 ? 194 LYS B O 1 ATOM 3555 C CB . LYS B 1 194 ? 17.686 -7.238 2.461 1.00 37.00 ? 194 LYS B CB 1 ATOM 3556 C CG . LYS B 1 194 ? 17.490 -6.040 3.386 1.00 44.44 ? 194 LYS B CG 1 ATOM 3557 C CD . LYS B 1 194 ? 18.808 -5.335 3.764 1.00 49.60 ? 194 LYS B CD 1 ATOM 3558 C CE . LYS B 1 194 ? 19.773 -6.177 4.606 1.00 50.26 ? 194 LYS B CE 1 ATOM 3559 N NZ . LYS B 1 194 ? 20.459 -7.287 3.868 1.00 50.07 ? 194 LYS B NZ 1 ATOM 3560 N N . ARG B 1 195 ? 14.751 -5.903 1.503 1.00 31.78 ? 195 ARG B N 1 ATOM 3561 C CA . ARG B 1 195 ? 13.362 -5.515 1.763 1.00 31.51 ? 195 ARG B CA 1 ATOM 3562 C C . ARG B 1 195 ? 12.417 -6.109 0.740 1.00 29.97 ? 195 ARG B C 1 ATOM 3563 O O . ARG B 1 195 ? 11.302 -6.534 1.103 1.00 29.17 ? 195 ARG B O 1 ATOM 3564 C CB . ARG B 1 195 ? 13.208 -4.002 1.803 1.00 30.83 ? 195 ARG B CB 1 ATOM 3565 C CG . ARG B 1 195 ? 14.022 -3.371 2.929 1.00 34.10 ? 195 ARG B CG 1 ATOM 3566 C CD . ARG B 1 195 ? 13.697 -1.901 3.129 1.00 34.16 ? 195 ARG B CD 1 ATOM 3567 N NE . ARG B 1 195 ? 14.123 -1.112 1.973 1.00 39.31 ? 195 ARG B NE 1 ATOM 3568 C CZ . ARG B 1 195 ? 15.275 -0.439 1.861 1.00 41.48 ? 195 ARG B CZ 1 ATOM 3569 N NH1 . ARG B 1 195 ? 16.175 -0.432 2.847 1.00 42.14 ? 195 ARG B NH1 1 ATOM 3570 N NH2 . ARG B 1 195 ? 15.535 0.242 0.736 1.00 43.27 ? 195 ARG B NH2 1 ATOM 3571 N N . TRP B 1 196 ? 12.855 -6.141 -0.520 1.00 27.90 ? 196 TRP B N 1 ATOM 3572 C CA . TRP B 1 196 ? 12.067 -6.736 -1.613 1.00 27.07 ? 196 TRP B CA 1 ATOM 3573 C C . TRP B 1 196 ? 11.712 -8.204 -1.307 1.00 28.41 ? 196 TRP B C 1 ATOM 3574 O O . TRP B 1 196 ? 10.607 -8.661 -1.629 1.00 27.04 ? 196 TRP B O 1 ATOM 3575 C CB . TRP B 1 196 ? 12.805 -6.694 -2.960 1.00 24.72 ? 196 TRP B CB 1 ATOM 3576 C CG . TRP B 1 196 ? 13.187 -5.364 -3.472 1.00 22.40 ? 196 TRP B CG 1 ATOM 3577 C CD1 . TRP B 1 196 ? 12.747 -4.152 -3.035 1.00 20.19 ? 196 TRP B CD1 1 ATOM 3578 C CD2 . TRP B 1 196 ? 14.071 -5.091 -4.595 1.00 21.78 ? 196 TRP B CD2 1 ATOM 3579 N NE1 . TRP B 1 196 ? 13.303 -3.153 -3.785 1.00 20.54 ? 196 TRP B NE1 1 ATOM 3580 C CE2 . TRP B 1 196 ? 14.130 -3.695 -4.738 1.00 20.10 ? 196 TRP B CE2 1 ATOM 3581 C CE3 . TRP B 1 196 ? 14.828 -5.895 -5.469 1.00 21.37 ? 196 TRP B CE3 1 ATOM 3582 C CZ2 . TRP B 1 196 ? 14.909 -3.073 -5.722 1.00 21.88 ? 196 TRP B CZ2 1 ATOM 3583 C CZ3 . TRP B 1 196 ? 15.617 -5.264 -6.456 1.00 20.98 ? 196 TRP B CZ3 1 ATOM 3584 C CH2 . TRP B 1 196 ? 15.653 -3.873 -6.564 1.00 21.84 ? 196 TRP B CH2 1 ATOM 3585 N N . GLU B 1 197 ? 12.634 -8.922 -0.662 1.00 28.64 ? 197 GLU B N 1 ATOM 3586 C CA . GLU B 1 197 ? 12.410 -10.335 -0.307 1.00 31.35 ? 197 GLU B CA 1 ATOM 3587 C C . GLU B 1 197 ? 11.630 -10.557 0.996 1.00 32.26 ? 197 GLU B C 1 ATOM 3588 O O . GLU B 1 197 ? 11.114 -11.644 1.196 1.00 36.10 ? 197 GLU B O 1 ATOM 3589 C CB . GLU B 1 197 ? 13.745 -11.073 -0.141 1.00 30.62 ? 197 GLU B CB 1 ATOM 3590 C CG . GLU B 1 197 ? 14.709 -10.955 -1.292 1.00 29.85 ? 197 GLU B CG 1 ATOM 3591 C CD . GLU B 1 197 ? 16.084 -11.465 -0.919 1.00 29.32 ? 197 GLU B CD 1 ATOM 3592 O OE1 . GLU B 1 197 ? 16.577 -11.077 0.137 1.00 27.27 ? 197 GLU B OE1 1 ATOM 3593 O OE2 . GLU B 1 197 ? 16.670 -12.259 -1.680 1.00 32.15 ? 197 GLU B OE2 1 ATOM 3594 N N . THR B 1 198 ? 11.592 -9.564 1.886 1.00 32.37 ? 198 THR B N 1 ATOM 3595 C CA . THR B 1 198 ? 10.841 -9.642 3.158 1.00 35.93 ? 198 THR B CA 1 ATOM 3596 C C . THR B 1 198 ? 9.323 -9.756 2.954 1.00 36.07 ? 198 THR B C 1 ATOM 3597 O O . THR B 1 198 ? 8.705 -8.853 2.385 1.00 37.41 ? 198 THR B O 1 ATOM 3598 C CB . THR B 1 198 ? 11.077 -8.380 4.028 1.00 36.78 ? 198 THR B CB 1 ATOM 3599 O OG1 . THR B 1 198 ? 12.476 -8.165 4.213 1.00 37.74 ? 198 THR B OG1 1 ATOM 3600 C CG2 . THR B 1 198 ? 10.409 -8.507 5.393 1.00 38.59 ? 198 THR B CG2 1 ATOM 3601 N N . CYS B 1 199 ? 8.732 -10.846 3.437 1.00 37.77 ? 199 CYS B N 1 ATOM 3602 C CA . CYS B 1 199 ? 7.281 -11.066 3.365 1.00 39.31 ? 199 CYS B CA 1 ATOM 3603 C C . CYS B 1 199 ? 6.843 -11.918 4.539 1.00 39.88 ? 199 CYS B C 1 ATOM 3604 O O . CYS B 1 199 ? 7.290 -13.054 4.670 1.00 38.36 ? 199 CYS B O 1 ATOM 3605 C CB . CYS B 1 199 ? 6.889 -11.773 2.057 1.00 40.61 ? 199 CYS B CB 1 ATOM 3606 S SG . CYS B 1 199 ? 5.113 -12.127 1.858 1.00 42.49 ? 199 CYS B SG 1 ATOM 3607 N N . THR B 1 200 ? 5.940 -11.372 5.353 1.00 41.69 ? 200 THR B N 1 ATOM 3608 C CA . THR B 1 200 ? 5.444 -12.014 6.582 1.00 43.83 ? 200 THR B CA 1 ATOM 3609 C C . THR B 1 200 ? 4.205 -12.919 6.410 1.00 45.92 ? 200 THR B C 1 ATOM 3610 O O . THR B 1 200 ? 3.458 -13.127 7.374 1.00 48.52 ? 200 THR B O 1 ATOM 3611 C CB . THR B 1 200 ? 5.006 -10.934 7.586 1.00 42.26 ? 200 THR B CB 1 ATOM 3612 O OG1 . THR B 1 200 ? 3.799 -10.343 7.108 1.00 42.95 ? 200 THR B OG1 1 ATOM 3613 C CG2 . THR B 1 200 ? 6.055 -9.843 7.732 1.00 42.72 ? 200 THR B CG2 1 ATOM 3614 N N . LYS B 1 201 ? 3.952 -13.423 5.201 1.00 46.52 ? 201 LYS B N 1 ATOM 3615 C CA . LYS B 1 201 ? 2.840 -14.360 4.973 1.00 44.69 ? 201 LYS B CA 1 ATOM 3616 C C . LYS B 1 201 ? 3.360 -15.768 4.723 1.00 43.27 ? 201 LYS B C 1 ATOM 3617 O O . LYS B 1 201 ? 4.537 -15.955 4.401 1.00 45.05 ? 201 LYS B O 1 ATOM 3618 C CB . LYS B 1 201 ? 1.979 -13.887 3.797 1.00 45.19 ? 201 LYS B CB 1 ATOM 3619 C CG . LYS B 1 201 ? 1.420 -12.496 3.992 1.00 44.87 ? 201 LYS B CG 1 ATOM 3620 C CD . LYS B 1 201 ? 0.384 -12.155 2.932 1.00 45.78 ? 201 LYS B CD 1 ATOM 3621 C CE . LYS B 1 201 ? -0.357 -10.874 3.286 1.00 43.72 ? 201 LYS B CE 1 ATOM 3622 N NZ . LYS B 1 201 ? -1.743 -10.871 2.751 1.00 44.60 ? 201 LYS B NZ 1 ATOM 3623 N N . THR B 1 203 ? 2.898 -16.179 2.250 1.00 42.90 ? 203 THR B N 1 ATOM 3624 C CA . THR B 1 203 ? 3.892 -16.938 1.507 1.00 41.85 ? 203 THR B CA 1 ATOM 3625 C C . THR B 1 203 ? 4.354 -16.196 0.234 1.00 39.42 ? 203 THR B C 1 ATOM 3626 O O . THR B 1 203 ? 5.455 -16.429 -0.256 1.00 41.01 ? 203 THR B O 1 ATOM 3627 C CB . THR B 1 203 ? 3.353 -18.345 1.214 1.00 46.90 ? 203 THR B CB 1 ATOM 3628 O OG1 . THR B 1 203 ? 4.289 -19.316 1.700 1.00 43.97 ? 203 THR B OG1 1 ATOM 3629 C CG2 . THR B 1 203 ? 3.026 -18.536 -0.291 1.00 47.15 ? 203 THR B CG2 1 ATOM 3630 N N . ALA B 1 204 ? 3.505 -15.311 -0.289 1.00 35.45 ? 204 ALA B N 1 ATOM 3631 C CA . ALA B 1 204 ? 3.948 -14.179 -1.117 1.00 31.79 ? 204 ALA B CA 1 ATOM 3632 C C . ALA B 1 204 ? 3.216 -12.929 -0.656 1.00 30.21 ? 204 ALA B C 1 ATOM 3633 O O . ALA B 1 204 ? 2.189 -13.027 0.016 1.00 26.94 ? 204 ALA B O 1 ATOM 3634 C CB . ALA B 1 204 ? 3.663 -14.428 -2.584 1.00 32.25 ? 204 ALA B CB 1 ATOM 3635 N N . CYS B 1 205 ? 3.695 -11.764 -1.094 1.00 29.42 ? 205 CYS B N 1 ATOM 3636 C CA . CYS B 1 205 ? 3.141 -10.474 -0.676 1.00 29.13 ? 205 CYS B CA 1 ATOM 3637 C C . CYS B 1 205 ? 2.660 -9.611 -1.851 1.00 26.77 ? 205 CYS B C 1 ATOM 3638 O O . CYS B 1 205 ? 3.067 -8.457 -1.968 1.00 25.14 ? 205 CYS B O 1 ATOM 3639 C CB . CYS B 1 205 ? 4.201 -9.730 0.150 1.00 31.47 ? 205 CYS B CB 1 ATOM 3640 S SG . CYS B 1 205 ? 4.267 -10.260 1.883 1.00 35.88 ? 205 CYS B SG 1 ATOM 3641 N N . PRO B 1 206 ? 1.760 -10.149 -2.705 1.00 24.10 ? 206 PRO B N 1 ATOM 3642 C CA . PRO B 1 206 ? 1.385 -9.482 -3.981 1.00 23.86 ? 206 PRO B CA 1 ATOM 3643 C C . PRO B 1 206 ? 0.784 -8.071 -3.851 1.00 22.77 ? 206 PRO B C 1 ATOM 3644 O O . PRO B 1 206 ? 1.003 -7.191 -4.730 1.00 22.02 ? 206 PRO B O 1 ATOM 3645 C CB . PRO B 1 206 ? 0.354 -10.444 -4.596 1.00 24.45 ? 206 PRO B CB 1 ATOM 3646 C CG . PRO B 1 206 ? -0.080 -11.356 -3.478 1.00 24.06 ? 206 PRO B CG 1 ATOM 3647 C CD . PRO B 1 206 ? 1.096 -11.455 -2.561 1.00 24.38 ? 206 PRO B CD 1 ATOM 3648 N N . ASP B 1 207 ? 0.044 -7.834 -2.775 1.00 21.46 ? 207 ASP B N 1 ATOM 3649 C CA . ASP B 1 207 ? -0.635 -6.528 -2.623 1.00 22.96 ? 207 ASP B CA 1 ATOM 3650 C C . ASP B 1 207 ? 0.373 -5.391 -2.525 1.00 22.42 ? 207 ASP B C 1 ATOM 3651 O O . ASP B 1 207 ? 0.139 -4.265 -3.015 1.00 23.66 ? 207 ASP B O 1 ATOM 3652 C CB . ASP B 1 207 ? -1.577 -6.546 -1.412 1.00 24.48 ? 207 ASP B CB 1 ATOM 3653 C CG . ASP B 1 207 ? -2.752 -7.524 -1.596 1.00 25.26 ? 207 ASP B CG 1 ATOM 3654 O OD1 . ASP B 1 207 ? -3.041 -7.918 -2.749 1.00 24.50 ? 207 ASP B OD1 1 ATOM 3655 O OD2 . ASP B 1 207 ? -3.375 -7.903 -0.575 1.00 28.20 ? 207 ASP B OD2 1 ATOM 3656 N N . ILE B 1 208 ? 1.516 -5.713 -1.938 1.00 21.44 ? 208 ILE B N 1 ATOM 3657 C CA . ILE B 1 208 ? 2.663 -4.813 -1.900 1.00 23.15 ? 208 ILE B CA 1 ATOM 3658 C C . ILE B 1 208 ? 3.229 -4.516 -3.296 1.00 20.28 ? 208 ILE B C 1 ATOM 3659 O O . ILE B 1 208 ? 3.473 -3.357 -3.660 1.00 19.23 ? 208 ILE B O 1 ATOM 3660 C CB . ILE B 1 208 ? 3.762 -5.427 -1.002 1.00 24.70 ? 208 ILE B CB 1 ATOM 3661 C CG1 . ILE B 1 208 ? 3.275 -5.482 0.478 1.00 27.84 ? 208 ILE B CG1 1 ATOM 3662 C CG2 . ILE B 1 208 ? 5.076 -4.688 -1.147 1.00 25.61 ? 208 ILE B CG2 1 ATOM 3663 C CD1 . ILE B 1 208 ? 3.377 -4.168 1.240 1.00 29.01 ? 208 ILE B CD1 1 ATOM 3664 N N . TYR B 1 209 ? 3.480 -5.574 -4.062 1.00 19.26 ? 209 TYR B N 1 ATOM 3665 C CA . TYR B 1 209 ? 4.068 -5.443 -5.402 1.00 18.49 ? 209 TYR B CA 1 ATOM 3666 C C . TYR B 1 209 ? 3.086 -4.746 -6.315 1.00 17.06 ? 209 TYR B C 1 ATOM 3667 O O . TYR B 1 209 ? 3.509 -4.013 -7.197 1.00 18.56 ? 209 TYR B O 1 ATOM 3668 C CB . TYR B 1 209 ? 4.401 -6.812 -6.018 1.00 20.12 ? 209 TYR B CB 1 ATOM 3669 C CG . TYR B 1 209 ? 4.963 -7.826 -5.070 1.00 21.24 ? 209 TYR B CG 1 ATOM 3670 C CD1 . TYR B 1 209 ? 5.729 -7.440 -3.965 1.00 23.37 ? 209 TYR B CD1 1 ATOM 3671 C CD2 . TYR B 1 209 ? 4.768 -9.186 -5.287 1.00 21.52 ? 209 TYR B CD2 1 ATOM 3672 C CE1 . TYR B 1 209 ? 6.244 -8.388 -3.078 1.00 24.10 ? 209 TYR B CE1 1 ATOM 3673 C CE2 . TYR B 1 209 ? 5.279 -10.129 -4.410 1.00 22.38 ? 209 TYR B CE2 1 ATOM 3674 C CZ . TYR B 1 209 ? 6.008 -9.728 -3.308 1.00 24.98 ? 209 TYR B CZ 1 ATOM 3675 O OH . TYR B 1 209 ? 6.515 -10.669 -2.421 1.00 27.32 ? 209 TYR B OH 1 ATOM 3676 N N . ALA B 1 210 ? 1.781 -4.964 -6.103 1.00 15.80 ? 210 ALA B N 1 ATOM 3677 C CA . ALA B 1 210 ? 0.731 -4.263 -6.861 1.00 15.36 ? 210 ALA B CA 1 ATOM 3678 C C . ALA B 1 210 ? 0.667 -2.785 -6.476 1.00 16.28 ? 210 ALA B C 1 ATOM 3679 O O . ALA B 1 210 ? 0.556 -1.906 -7.351 1.00 17.47 ? 210 ALA B O 1 ATOM 3680 C CB . ALA B 1 210 ? -0.638 -4.880 -6.590 1.00 15.61 ? 210 ALA B CB 1 ATOM 3681 N N . SER B 1 211 ? 0.694 -2.495 -5.174 1.00 15.80 ? 211 SER B N 1 ATOM 3682 C CA . SER B 1 211 ? 0.688 -1.082 -4.750 1.00 16.62 ? 211 SER B CA 1 ATOM 3683 C C . SER B 1 211 ? 1.846 -0.294 -5.338 1.00 17.27 ? 211 SER B C 1 ATOM 3684 O O . SER B 1 211 ? 1.657 0.833 -5.791 1.00 17.91 ? 211 SER B O 1 ATOM 3685 C CB . SER B 1 211 ? 0.649 -0.966 -3.216 1.00 16.94 ? 211 SER B CB 1 ATOM 3686 O OG . SER B 1 211 ? -0.605 -1.421 -2.723 1.00 15.50 ? 211 SER B OG 1 ATOM 3687 N N . GLU B 1 212 ? 3.046 -0.892 -5.350 1.00 18.37 ? 212 GLU B N 1 ATOM 3688 C CA . GLU B 1 212 ? 4.213 -0.315 -6.027 1.00 17.46 ? 212 GLU B CA 1 ATOM 3689 C C . GLU B 1 212 ? 3.914 -0.039 -7.493 1.00 17.55 ? 212 GLU B C 1 ATOM 3690 O O . GLU B 1 212 ? 4.289 1.006 -8.042 1.00 15.82 ? 212 GLU B O 1 ATOM 3691 C CB . GLU B 1 212 ? 5.395 -1.286 -5.950 1.00 18.76 ? 212 GLU B CB 1 ATOM 3692 C CG . GLU B 1 212 ? 6.014 -1.440 -4.552 1.00 18.96 ? 212 GLU B CG 1 ATOM 3693 C CD . GLU B 1 212 ? 6.935 -2.640 -4.403 1.00 19.40 ? 212 GLU B CD 1 ATOM 3694 O OE1 . GLU B 1 212 ? 7.024 -3.471 -5.334 1.00 18.65 ? 212 GLU B OE1 1 ATOM 3695 O OE2 . GLU B 1 212 ? 7.590 -2.764 -3.338 1.00 19.88 ? 212 GLU B OE2 1 ATOM 3696 N N . GLY B 1 213 ? 3.251 -1.005 -8.126 1.00 18.30 ? 213 GLY B N 1 ATOM 3697 C CA . GLY B 1 213 ? 3.011 -0.982 -9.549 1.00 18.98 ? 213 GLY B CA 1 ATOM 3698 C C . GLY B 1 213 ? 2.180 0.203 -9.977 1.00 19.58 ? 213 GLY B C 1 ATOM 3699 O O . GLY B 1 213 ? 2.542 0.921 -10.913 1.00 19.02 ? 213 GLY B O 1 ATOM 3700 N N . ILE B 1 214 ? 1.076 0.423 -9.271 1.00 21.77 ? 214 ILE B N 1 ATOM 3701 C CA . ILE B 1 214 ? 0.208 1.561 -9.543 1.00 22.04 ? 214 ILE B CA 1 ATOM 3702 C C . ILE B 1 214 ? 0.932 2.877 -9.265 1.00 21.94 ? 214 ILE B C 1 ATOM 3703 O O . ILE B 1 214 ? 0.829 3.795 -10.041 1.00 21.86 ? 214 ILE B O 1 ATOM 3704 C CB . ILE B 1 214 ? -1.177 1.435 -8.832 1.00 22.99 ? 214 ILE B CB 1 ATOM 3705 C CG1 . ILE B 1 214 ? -2.160 2.500 -9.334 1.00 23.97 ? 214 ILE B CG1 1 ATOM 3706 C CG2 . ILE B 1 214 ? -1.072 1.515 -7.335 1.00 22.34 ? 214 ILE B CG2 1 ATOM 3707 C CD1 . ILE B 1 214 ? -2.454 2.442 -10.802 1.00 25.34 ? 214 ILE B CD1 1 ATOM 3708 N N . GLN B 1 215 ? 1.723 2.946 -8.199 1.00 22.84 ? 215 GLN B N 1 ATOM 3709 C CA . GLN B 1 215 ? 2.564 4.123 -7.963 1.00 22.59 ? 215 GLN B CA 1 ATOM 3710 C C . GLN B 1 215 ? 3.470 4.430 -9.151 1.00 21.12 ? 215 GLN B C 1 ATOM 3711 O O . GLN B 1 215 ? 3.571 5.578 -9.579 1.00 19.36 ? 215 GLN B O 1 ATOM 3712 C CB . GLN B 1 215 ? 3.448 3.936 -6.725 1.00 24.05 ? 215 GLN B CB 1 ATOM 3713 C CG . GLN B 1 215 ? 4.116 5.215 -6.216 1.00 24.87 ? 215 GLN B CG 1 ATOM 3714 C CD . GLN B 1 215 ? 3.130 6.246 -5.722 1.00 26.46 ? 215 GLN B CD 1 ATOM 3715 O OE1 . GLN B 1 215 ? 2.064 5.908 -5.207 1.00 27.66 ? 215 GLN B OE1 1 ATOM 3716 N NE2 . GLN B 1 215 ? 3.493 7.530 -5.852 1.00 27.85 ? 215 GLN B NE2 1 ATOM 3717 N N . ALA B 1 216 ? 4.150 3.406 -9.651 1.00 20.64 ? 216 ALA B N 1 ATOM 3718 C CA . ALA B 1 216 ? 5.035 3.557 -10.801 1.00 20.89 ? 216 ALA B CA 1 ATOM 3719 C C . ALA B 1 216 ? 4.222 3.874 -12.056 1.00 20.95 ? 216 ALA B C 1 ATOM 3720 O O . ALA B 1 216 ? 4.681 4.599 -12.950 1.00 20.34 ? 216 ALA B O 1 ATOM 3721 C CB . ALA B 1 216 ? 5.847 2.283 -11.002 1.00 22.23 ? 216 ALA B CB 1 ATOM 3722 N N . ALA B 1 217 ? 3.010 3.332 -12.139 1.00 21.47 ? 217 ALA B N 1 ATOM 3723 C CA . ALA B 1 217 ? 2.137 3.625 -13.282 1.00 22.51 ? 217 ALA B CA 1 ATOM 3724 C C . ALA B 1 217 ? 1.958 5.126 -13.400 1.00 23.13 ? 217 ALA B C 1 ATOM 3725 O O . ALA B 1 217 ? 2.208 5.708 -14.461 1.00 22.65 ? 217 ALA B O 1 ATOM 3726 C CB . ALA B 1 217 ? 0.783 2.956 -13.132 1.00 22.92 ? 217 ALA B CB 1 ATOM 3727 N N . CYS B 1 218 ? 1.553 5.720 -12.280 1.00 24.28 ? 218 CYS B N 1 ATOM 3728 C CA . CYS B 1 218 ? 1.281 7.160 -12.146 1.00 25.32 ? 218 CYS B CA 1 ATOM 3729 C C . CYS B 1 218 ? 2.512 8.029 -12.207 1.00 23.06 ? 218 CYS B C 1 ATOM 3730 O O . CYS B 1 218 ? 2.515 9.020 -12.910 1.00 22.84 ? 218 CYS B O 1 ATOM 3731 C CB . CYS B 1 218 ? 0.558 7.448 -10.836 1.00 26.91 ? 218 CYS B CB 1 ATOM 3732 S SG . CYS B 1 218 ? -1.126 6.790 -10.698 1.00 30.58 ? 218 CYS B SG 1 ATOM 3733 N N . ASP B 1 219 ? 3.561 7.670 -11.484 1.00 23.44 ? 219 ASP B N 1 ATOM 3734 C CA . ASP B 1 219 ? 4.773 8.505 -11.454 1.00 22.33 ? 219 ASP B CA 1 ATOM 3735 C C . ASP B 1 219 ? 5.598 8.442 -12.730 1.00 22.03 ? 219 ASP B C 1 ATOM 3736 O O . ASP B 1 219 ? 6.317 9.383 -13.049 1.00 18.93 ? 219 ASP B O 1 ATOM 3737 C CB . ASP B 1 219 ? 5.674 8.135 -10.267 1.00 22.91 ? 219 ASP B CB 1 ATOM 3738 C CG . ASP B 1 219 ? 5.085 8.548 -8.922 1.00 24.94 ? 219 ASP B CG 1 ATOM 3739 O OD1 . ASP B 1 219 ? 4.162 9.387 -8.900 1.00 28.54 ? 219 ASP B OD1 1 ATOM 3740 O OD2 . ASP B 1 219 ? 5.530 8.024 -7.878 1.00 23.27 ? 219 ASP B OD2 1 ATOM 3741 N N . TRP B 1 220 ? 5.508 7.339 -13.468 1.00 22.26 ? 220 TRP B N 1 ATOM 3742 C CA . TRP B 1 220 ? 6.450 7.117 -14.568 1.00 22.51 ? 220 TRP B CA 1 ATOM 3743 C C . TRP B 1 220 ? 5.823 6.686 -15.913 1.00 21.77 ? 220 TRP B C 1 ATOM 3744 O O . TRP B 1 220 ? 6.243 7.156 -16.967 1.00 21.84 ? 220 TRP B O 1 ATOM 3745 C CB . TRP B 1 220 ? 7.507 6.100 -14.112 1.00 24.75 ? 220 TRP B CB 1 ATOM 3746 C CG . TRP B 1 220 ? 8.390 6.610 -13.023 1.00 26.33 ? 220 TRP B CG 1 ATOM 3747 C CD1 . TRP B 1 220 ? 8.373 6.244 -11.714 1.00 26.54 ? 220 TRP B CD1 1 ATOM 3748 C CD2 . TRP B 1 220 ? 9.414 7.613 -13.142 1.00 28.41 ? 220 TRP B CD2 1 ATOM 3749 N NE1 . TRP B 1 220 ? 9.334 6.921 -11.019 1.00 25.30 ? 220 TRP B NE1 1 ATOM 3750 C CE2 . TRP B 1 220 ? 9.986 7.773 -11.868 1.00 27.73 ? 220 TRP B CE2 1 ATOM 3751 C CE3 . TRP B 1 220 ? 9.913 8.374 -14.208 1.00 29.65 ? 220 TRP B CE3 1 ATOM 3752 C CZ2 . TRP B 1 220 ? 11.028 8.681 -11.619 1.00 29.66 ? 220 TRP B CZ2 1 ATOM 3753 C CZ3 . TRP B 1 220 ? 10.956 9.259 -13.967 1.00 29.35 ? 220 TRP B CZ3 1 ATOM 3754 C CH2 . TRP B 1 220 ? 11.499 9.408 -12.679 1.00 29.13 ? 220 TRP B CH2 1 ATOM 3755 N N . ALA B 1 221 ? 4.844 5.784 -15.901 1.00 20.32 ? 221 ALA B N 1 ATOM 3756 C CA . ALA B 1 221 ? 4.238 5.329 -17.155 1.00 20.96 ? 221 ALA B CA 1 ATOM 3757 C C . ALA B 1 221 ? 3.314 6.399 -17.769 1.00 21.83 ? 221 ALA B C 1 ATOM 3758 O O . ALA B 1 221 ? 3.558 6.882 -18.884 1.00 21.62 ? 221 ALA B O 1 ATOM 3759 C CB . ALA B 1 221 ? 3.493 3.994 -16.967 1.00 20.02 ? 221 ALA B CB 1 ATOM 3760 N N . TYR B 1 222 ? 2.256 6.741 -17.039 1.00 22.68 ? 222 TYR B N 1 ATOM 3761 C CA . TYR B 1 222 ? 1.260 7.708 -17.496 1.00 24.10 ? 222 TYR B CA 1 ATOM 3762 C C . TYR B 1 222 ? 1.815 9.122 -17.467 1.00 24.53 ? 222 TYR B C 1 ATOM 3763 O O . TYR B 1 222 ? 1.315 10.025 -18.148 1.00 24.58 ? 222 TYR B O 1 ATOM 3764 C CB . TYR B 1 222 ? 0.043 7.680 -16.573 1.00 23.48 ? 222 TYR B CB 1 ATOM 3765 C CG . TYR B 1 222 ? -0.842 6.457 -16.649 1.00 22.80 ? 222 TYR B CG 1 ATOM 3766 C CD1 . TYR B 1 222 ? -1.376 6.046 -17.854 1.00 22.03 ? 222 TYR B CD1 1 ATOM 3767 C CD2 . TYR B 1 222 ? -1.218 5.770 -15.494 1.00 22.73 ? 222 TYR B CD2 1 ATOM 3768 C CE1 . TYR B 1 222 ? -2.221 4.968 -17.937 1.00 21.87 ? 222 TYR B CE1 1 ATOM 3769 C CE2 . TYR B 1 222 ? -2.071 4.674 -15.558 1.00 23.28 ? 222 TYR B CE2 1 ATOM 3770 C CZ . TYR B 1 222 ? -2.581 4.278 -16.786 1.00 23.06 ? 222 TYR B CZ 1 ATOM 3771 O OH . TYR B 1 222 ? -3.433 3.192 -16.893 1.00 22.58 ? 222 TYR B OH 1 ATOM 3772 N N . LYS B 1 223 ? 2.846 9.314 -16.661 1.00 25.59 ? 223 LYS B N 1 ATOM 3773 C CA . LYS B 1 223 ? 3.277 10.644 -16.294 1.00 28.38 ? 223 LYS B CA 1 ATOM 3774 C C . LYS B 1 223 ? 3.690 11.404 -17.561 1.00 29.55 ? 223 LYS B C 1 ATOM 3775 O O . LYS B 1 223 ? 4.522 10.925 -18.331 1.00 29.27 ? 223 LYS B O 1 ATOM 3776 C CB . LYS B 1 223 ? 4.412 10.548 -15.264 1.00 28.48 ? 223 LYS B CB 1 ATOM 3777 C CG . LYS B 1 223 ? 4.989 11.867 -14.768 1.00 30.50 ? 223 LYS B CG 1 ATOM 3778 C CD . LYS B 1 223 ? 3.989 12.663 -13.948 1.00 31.54 ? 223 LYS B CD 1 ATOM 3779 C CE . LYS B 1 223 ? 4.610 13.225 -12.665 1.00 34.76 ? 223 LYS B CE 1 ATOM 3780 N NZ . LYS B 1 223 ? 4.035 14.559 -12.276 1.00 34.65 ? 223 LYS B NZ 1 ATOM 3781 N N . GLY B 1 224 ? 3.036 12.545 -17.804 1.00 30.32 ? 224 GLY B N 1 ATOM 3782 C CA . GLY B 1 224 ? 3.377 13.426 -18.912 1.00 31.71 ? 224 GLY B CA 1 ATOM 3783 C C . GLY B 1 224 ? 2.895 13.008 -20.291 1.00 31.99 ? 224 GLY B C 1 ATOM 3784 O O . GLY B 1 224 ? 2.836 13.835 -21.202 1.00 37.32 ? 224 GLY B O 1 ATOM 3785 N N . VAL B 1 225 ? 2.539 11.739 -20.449 1.00 29.33 ? 225 VAL B N 1 ATOM 3786 C CA . VAL B 1 225 ? 2.112 11.209 -21.725 1.00 27.05 ? 225 VAL B CA 1 ATOM 3787 C C . VAL B 1 225 ? 0.670 11.648 -22.031 1.00 28.14 ? 225 VAL B C 1 ATOM 3788 O O . VAL B 1 225 ? -0.224 11.578 -21.172 1.00 25.58 ? 225 VAL B O 1 ATOM 3789 C CB . VAL B 1 225 ? 2.174 9.665 -21.717 1.00 26.81 ? 225 VAL B CB 1 ATOM 3790 C CG1 . VAL B 1 225 ? 1.512 9.080 -22.965 1.00 26.38 ? 225 VAL B CG1 1 ATOM 3791 C CG2 . VAL B 1 225 ? 3.616 9.198 -21.561 1.00 25.24 ? 225 VAL B CG2 1 ATOM 3792 N N . THR B 1 226 ? 0.482 12.104 -23.268 1.00 27.94 ? 226 THR B N 1 ATOM 3793 C CA . THR B 1 226 ? -0.811 12.458 -23.823 1.00 29.12 ? 226 THR B CA 1 ATOM 3794 C C . THR B 1 226 ? -0.994 11.682 -25.122 1.00 29.49 ? 226 THR B C 1 ATOM 3795 O O . THR B 1 226 ? -0.033 11.460 -25.856 1.00 26.12 ? 226 THR B O 1 ATOM 3796 C CB . THR B 1 226 ? -0.850 13.967 -24.172 1.00 29.99 ? 226 THR B CB 1 ATOM 3797 O OG1 . THR B 1 226 ? -0.711 14.755 -22.977 1.00 30.93 ? 226 THR B OG1 1 ATOM 3798 C CG2 . THR B 1 226 ? -2.159 14.339 -24.876 1.00 30.73 ? 226 THR B CG2 1 ATOM 3799 N N . GLU B 1 227 ? -2.233 11.318 -25.415 1.00 31.21 ? 227 GLU B N 1 ATOM 3800 C CA . GLU B 1 227 ? -2.610 10.687 -26.674 1.00 34.69 ? 227 GLU B CA 1 ATOM 3801 C C . GLU B 1 227 ? -1.991 11.385 -27.889 1.00 34.19 ? 227 GLU B C 1 ATOM 3802 O O . GLU B 1 227 ? -2.150 12.590 -28.075 1.00 33.82 ? 227 GLU B O 1 ATOM 3803 C CB . GLU B 1 227 ? -4.129 10.715 -26.816 1.00 37.80 ? 227 GLU B CB 1 ATOM 3804 C CG . GLU B 1 227 ? -4.644 9.837 -27.936 1.00 40.94 ? 227 GLU B CG 1 ATOM 3805 C CD . GLU B 1 227 ? -5.012 8.458 -27.443 1.00 44.83 ? 227 GLU B CD 1 ATOM 3806 O OE1 . GLU B 1 227 ? -5.970 8.351 -26.643 1.00 49.15 ? 227 GLU B OE1 1 ATOM 3807 O OE2 . GLU B 1 227 ? -4.356 7.484 -27.868 1.00 46.77 ? 227 GLU B OE2 1 ATOM 3808 N N . GLY B 1 228 ? -1.288 10.621 -28.715 1.00 32.17 ? 228 GLY B N 1 ATOM 3809 C CA . GLY B 1 228 ? -0.659 11.183 -29.888 1.00 31.51 ? 228 GLY B CA 1 ATOM 3810 C C . GLY B 1 228 ? 0.789 11.610 -29.714 1.00 28.97 ? 228 GLY B C 1 ATOM 3811 O O . GLY B 1 228 ? 1.433 11.924 -30.686 1.00 30.07 ? 228 GLY B O 1 ATOM 3812 N N . ASP B 1 229 ? 1.323 11.595 -28.499 1.00 26.01 ? 229 ASP B N 1 ATOM 3813 C CA . ASP B 1 229 ? 2.718 11.992 -28.302 1.00 25.74 ? 229 ASP B CA 1 ATOM 3814 C C . ASP B 1 229 ? 3.700 11.110 -29.042 1.00 24.88 ? 229 ASP B C 1 ATOM 3815 O O . ASP B 1 229 ? 3.411 9.961 -29.346 1.00 24.54 ? 229 ASP B O 1 ATOM 3816 C CB . ASP B 1 229 ? 3.078 12.011 -26.811 1.00 25.09 ? 229 ASP B CB 1 ATOM 3817 C CG . ASP B 1 229 ? 2.472 13.202 -26.095 1.00 27.21 ? 229 ASP B CG 1 ATOM 3818 O OD1 . ASP B 1 229 ? 1.786 13.964 -26.799 1.00 28.00 ? 229 ASP B OD1 1 ATOM 3819 O OD2 . ASP B 1 229 ? 2.651 13.364 -24.862 1.00 26.64 ? 229 ASP B OD2 1 ATOM 3820 N N . THR B 1 230 ? 4.874 11.651 -29.319 1.00 26.13 ? 230 THR B N 1 ATOM 3821 C CA . THR B 1 230 ? 6.016 10.819 -29.713 1.00 27.19 ? 230 THR B CA 1 ATOM 3822 C C . THR B 1 230 ? 6.901 10.714 -28.490 1.00 25.88 ? 230 THR B C 1 ATOM 3823 O O . THR B 1 230 ? 7.359 11.749 -27.972 1.00 23.41 ? 230 THR B O 1 ATOM 3824 C CB . THR B 1 230 ? 6.797 11.390 -30.908 1.00 29.02 ? 230 THR B CB 1 ATOM 3825 O OG1 . THR B 1 230 ? 5.932 11.492 -32.033 1.00 31.53 ? 230 THR B OG1 1 ATOM 3826 C CG2 . THR B 1 230 ? 7.936 10.478 -31.292 1.00 30.53 ? 230 THR B CG2 1 ATOM 3827 N N . LEU B 1 231 ? 7.093 9.479 -28.004 1.00 23.73 ? 231 LEU B N 1 ATOM 3828 C CA . LEU B 1 231 ? 8.043 9.188 -26.915 1.00 24.42 ? 231 LEU B CA 1 ATOM 3829 C C . LEU B 1 231 ? 9.325 8.689 -27.531 1.00 24.85 ? 231 LEU B C 1 ATOM 3830 O O . LEU B 1 231 ? 9.304 7.725 -28.313 1.00 26.45 ? 231 LEU B O 1 ATOM 3831 C CB . LEU B 1 231 ? 7.486 8.128 -25.963 1.00 25.30 ? 231 LEU B CB 1 ATOM 3832 C CG . LEU B 1 231 ? 6.038 8.365 -25.510 1.00 24.92 ? 231 LEU B CG 1 ATOM 3833 C CD1 . LEU B 1 231 ? 5.504 7.210 -24.696 1.00 25.56 ? 231 LEU B CD1 1 ATOM 3834 C CD2 . LEU B 1 231 ? 5.989 9.662 -24.735 1.00 26.48 ? 231 LEU B CD2 1 ATOM 3835 N N . GLU B 1 232 ? 10.431 9.345 -27.210 1.00 23.51 ? 232 GLU B N 1 ATOM 3836 C CA . GLU B 1 232 ? 11.719 8.968 -27.776 1.00 24.70 ? 232 GLU B CA 1 ATOM 3837 C C . GLU B 1 232 ? 12.722 9.020 -26.658 1.00 22.37 ? 232 GLU B C 1 ATOM 3838 O O . GLU B 1 232 ? 12.364 8.594 -25.574 1.00 21.18 ? 232 GLU B O 1 ATOM 3839 C CB . GLU B 1 232 ? 12.091 9.816 -29.006 1.00 26.04 ? 232 GLU B CB 1 ATOM 3840 C CG . GLU B 1 232 ? 11.762 11.292 -28.927 1.00 27.53 ? 232 GLU B CG 1 ATOM 3841 C CD . GLU B 1 232 ? 11.696 11.920 -30.318 1.00 28.83 ? 232 GLU B CD 1 ATOM 3842 O OE1 . GLU B 1 232 ? 12.613 11.717 -31.120 1.00 32.37 ? 232 GLU B OE1 1 ATOM 3843 O OE2 . GLU B 1 232 ? 10.723 12.605 -30.623 1.00 31.83 ? 232 GLU B OE2 1 ATOM 3844 N N . ASP B 1 233 ? 13.943 9.515 -26.890 1.00 24.23 ? 233 ASP B N 1 ATOM 3845 C CA . ASP B 1 233 ? 15.048 9.409 -25.904 1.00 25.91 ? 233 ASP B CA 1 ATOM 3846 C C . ASP B 1 233 ? 14.693 9.971 -24.514 1.00 26.38 ? 233 ASP B C 1 ATOM 3847 O O . ASP B 1 233 ? 15.007 9.344 -23.519 1.00 24.48 ? 233 ASP B O 1 ATOM 3848 C CB . ASP B 1 233 ? 16.347 10.074 -26.422 1.00 27.71 ? 233 ASP B CB 1 ATOM 3849 C CG . ASP B 1 233 ? 17.139 9.189 -27.402 1.00 29.16 ? 233 ASP B CG 1 ATOM 3850 O OD1 . ASP B 1 233 ? 16.752 8.033 -27.648 1.00 29.83 ? 233 ASP B OD1 1 ATOM 3851 O OD2 . ASP B 1 233 ? 18.177 9.655 -27.933 1.00 31.52 ? 233 ASP B OD2 1 ATOM 3852 N N . GLU B 1 234 ? 14.060 11.144 -24.422 1.00 26.11 ? 234 GLU B N 1 ATOM 3853 C CA . GLU B 1 234 ? 13.748 11.694 -23.074 1.00 28.86 ? 234 GLU B CA 1 ATOM 3854 C C . GLU B 1 234 ? 13.022 10.661 -22.194 1.00 25.03 ? 234 GLU B C 1 ATOM 3855 O O . GLU B 1 234 ? 13.482 10.278 -21.121 1.00 26.89 ? 234 GLU B O 1 ATOM 3856 C CB . GLU B 1 234 ? 12.886 12.967 -23.134 1.00 32.32 ? 234 GLU B CB 1 ATOM 3857 C CG . GLU B 1 234 ? 12.565 13.519 -21.736 1.00 38.61 ? 234 GLU B CG 1 ATOM 3858 C CD . GLU B 1 234 ? 11.941 14.928 -21.711 1.00 44.61 ? 234 GLU B CD 1 ATOM 3859 O OE1 . GLU B 1 234 ? 10.791 15.114 -22.206 1.00 43.35 ? 234 GLU B OE1 1 ATOM 3860 O OE2 . GLU B 1 234 ? 12.602 15.843 -21.151 1.00 48.53 ? 234 GLU B OE2 1 ATOM 3861 N N . TYR B 1 235 ? 11.869 10.235 -22.668 1.00 23.51 ? 235 TYR B N 1 ATOM 3862 C CA . TYR B 1 235 ? 11.060 9.245 -21.977 1.00 21.87 ? 235 TYR B CA 1 ATOM 3863 C C . TYR B 1 235 ? 11.814 7.935 -21.835 1.00 19.76 ? 235 TYR B C 1 ATOM 3864 O O . TYR B 1 235 ? 11.841 7.354 -20.791 1.00 21.28 ? 235 TYR B O 1 ATOM 3865 C CB . TYR B 1 235 ? 9.798 8.993 -22.779 1.00 21.45 ? 235 TYR B CB 1 ATOM 3866 C CG . TYR B 1 235 ? 8.755 8.203 -22.042 1.00 21.15 ? 235 TYR B CG 1 ATOM 3867 C CD1 . TYR B 1 235 ? 8.759 6.818 -22.057 1.00 20.24 ? 235 TYR B CD1 1 ATOM 3868 C CD2 . TYR B 1 235 ? 7.765 8.849 -21.319 1.00 20.39 ? 235 TYR B CD2 1 ATOM 3869 C CE1 . TYR B 1 235 ? 7.765 6.093 -21.407 1.00 20.02 ? 235 TYR B CE1 1 ATOM 3870 C CE2 . TYR B 1 235 ? 6.784 8.141 -20.655 1.00 20.18 ? 235 TYR B CE2 1 ATOM 3871 C CZ . TYR B 1 235 ? 6.794 6.756 -20.700 1.00 19.89 ? 235 TYR B CZ 1 ATOM 3872 O OH . TYR B 1 235 ? 5.805 6.057 -20.046 1.00 19.01 ? 235 TYR B OH 1 ATOM 3873 N N . PHE B 1 236 ? 12.445 7.496 -22.896 1.00 21.20 ? 236 PHE B N 1 ATOM 3874 C CA . PHE B 1 236 ? 13.172 6.246 -22.870 1.00 20.95 ? 236 PHE B CA 1 ATOM 3875 C C . PHE B 1 236 ? 14.183 6.218 -21.730 1.00 20.65 ? 236 PHE B C 1 ATOM 3876 O O . PHE B 1 236 ? 14.184 5.280 -20.933 1.00 18.10 ? 236 PHE B O 1 ATOM 3877 C CB . PHE B 1 236 ? 13.850 5.946 -24.204 1.00 21.10 ? 236 PHE B CB 1 ATOM 3878 C CG . PHE B 1 236 ? 14.778 4.745 -24.144 1.00 21.88 ? 236 PHE B CG 1 ATOM 3879 C CD1 . PHE B 1 236 ? 14.288 3.498 -23.802 1.00 20.37 ? 236 PHE B CD1 1 ATOM 3880 C CD2 . PHE B 1 236 ? 16.170 4.886 -24.368 1.00 21.66 ? 236 PHE B CD2 1 ATOM 3881 C CE1 . PHE B 1 236 ? 15.139 2.401 -23.718 1.00 21.20 ? 236 PHE B CE1 1 ATOM 3882 C CE2 . PHE B 1 236 ? 17.022 3.796 -24.285 1.00 20.11 ? 236 PHE B CE2 1 ATOM 3883 C CZ . PHE B 1 236 ? 16.506 2.551 -23.969 1.00 21.68 ? 236 PHE B CZ 1 ATOM 3884 N N . TYR B 1 237 ? 15.045 7.229 -21.637 1.00 20.94 ? 237 TYR B N 1 ATOM 3885 C CA . TYR B 1 237 ? 16.129 7.152 -20.663 1.00 22.83 ? 237 TYR B CA 1 ATOM 3886 C C . TYR B 1 237 ? 15.687 7.437 -19.233 1.00 22.57 ? 237 TYR B C 1 ATOM 3887 O O . TYR B 1 237 ? 16.297 6.925 -18.290 1.00 22.24 ? 237 TYR B O 1 ATOM 3888 C CB . TYR B 1 237 ? 17.300 8.074 -21.039 1.00 25.12 ? 237 TYR B CB 1 ATOM 3889 C CG . TYR B 1 237 ? 18.145 7.575 -22.182 1.00 25.76 ? 237 TYR B CG 1 ATOM 3890 C CD1 . TYR B 1 237 ? 19.020 6.524 -22.008 1.00 26.08 ? 237 TYR B CD1 1 ATOM 3891 C CD2 . TYR B 1 237 ? 18.076 8.172 -23.439 1.00 26.54 ? 237 TYR B CD2 1 ATOM 3892 C CE1 . TYR B 1 237 ? 19.810 6.074 -23.058 1.00 28.78 ? 237 TYR B CE1 1 ATOM 3893 C CE2 . TYR B 1 237 ? 18.857 7.724 -24.497 1.00 27.57 ? 237 TYR B CE2 1 ATOM 3894 C CZ . TYR B 1 237 ? 19.724 6.672 -24.296 1.00 29.77 ? 237 TYR B CZ 1 ATOM 3895 O OH . TYR B 1 237 ? 20.517 6.220 -25.333 1.00 36.43 ? 237 TYR B OH 1 ATOM 3896 N N . SER B 1 238 ? 14.640 8.237 -19.059 1.00 22.77 ? 238 SER B N 1 ATOM 3897 C CA . SER B 1 238 ? 14.158 8.531 -17.709 1.00 23.39 ? 238 SER B CA 1 ATOM 3898 C C . SER B 1 238 ? 13.292 7.383 -17.167 1.00 22.49 ? 238 SER B C 1 ATOM 3899 O O . SER B 1 238 ? 13.131 7.276 -15.958 1.00 23.44 ? 238 SER B O 1 ATOM 3900 C CB . SER B 1 238 ? 13.380 9.865 -17.651 1.00 23.80 ? 238 SER B CB 1 ATOM 3901 O OG . SER B 1 238 ? 12.368 9.939 -18.648 1.00 23.55 ? 238 SER B OG 1 ATOM 3902 N N . ARG B 1 239 ? 12.737 6.538 -18.039 1.00 20.32 ? 239 ARG B N 1 ATOM 3903 C CA . ARG B 1 239 ? 11.858 5.438 -17.576 1.00 19.27 ? 239 ARG B CA 1 ATOM 3904 C C . ARG B 1 239 ? 12.586 4.071 -17.476 1.00 19.12 ? 239 ARG B C 1 ATOM 3905 O O . ARG B 1 239 ? 12.111 3.159 -16.822 1.00 17.80 ? 239 ARG B O 1 ATOM 3906 C CB . ARG B 1 239 ? 10.654 5.288 -18.486 1.00 19.84 ? 239 ARG B CB 1 ATOM 3907 C CG . ARG B 1 239 ? 9.439 6.157 -18.153 1.00 20.17 ? 239 ARG B CG 1 ATOM 3908 C CD . ARG B 1 239 ? 9.710 7.645 -18.084 1.00 21.37 ? 239 ARG B CD 1 ATOM 3909 N NE . ARG B 1 239 ? 8.511 8.354 -17.652 1.00 22.01 ? 239 ARG B NE 1 ATOM 3910 C CZ . ARG B 1 239 ? 8.416 9.677 -17.581 1.00 25.61 ? 239 ARG B CZ 1 ATOM 3911 N NH1 . ARG B 1 239 ? 9.449 10.443 -17.922 1.00 25.22 ? 239 ARG B NH1 1 ATOM 3912 N NH2 . ARG B 1 239 ? 7.279 10.241 -17.181 1.00 26.26 ? 239 ARG B NH2 1 ATOM 3913 N N . LEU B 1 240 ? 13.722 3.956 -18.134 1.00 19.82 ? 240 LEU B N 1 ATOM 3914 C CA . LEU B 1 240 ? 14.461 2.712 -18.192 1.00 20.51 ? 240 LEU B CA 1 ATOM 3915 C C . LEU B 1 240 ? 14.852 2.272 -16.789 1.00 21.22 ? 240 LEU B C 1 ATOM 3916 O O . LEU B 1 240 ? 14.693 1.089 -16.469 1.00 22.24 ? 240 LEU B O 1 ATOM 3917 C CB . LEU B 1 240 ? 15.650 2.831 -19.161 1.00 19.80 ? 240 LEU B CB 1 ATOM 3918 C CG . LEU B 1 240 ? 16.505 1.596 -19.505 1.00 19.64 ? 240 LEU B CG 1 ATOM 3919 C CD1 . LEU B 1 240 ? 15.674 0.415 -19.941 1.00 20.27 ? 240 LEU B CD1 1 ATOM 3920 C CD2 . LEU B 1 240 ? 17.600 1.899 -20.521 1.00 19.34 ? 240 LEU B CD2 1 ATOM 3921 N N . PRO B 1 241 ? 15.301 3.210 -15.922 1.00 21.32 ? 241 PRO B N 1 ATOM 3922 C CA . PRO B 1 241 ? 15.654 2.776 -14.564 1.00 22.31 ? 241 PRO B CA 1 ATOM 3923 C C . PRO B 1 241 ? 14.498 2.127 -13.777 1.00 21.56 ? 241 PRO B C 1 ATOM 3924 O O . PRO B 1 241 ? 14.732 1.303 -12.883 1.00 19.95 ? 241 PRO B O 1 ATOM 3925 C CB . PRO B 1 241 ? 16.072 4.074 -13.873 1.00 23.50 ? 241 PRO B CB 1 ATOM 3926 C CG . PRO B 1 241 ? 16.462 5.023 -14.975 1.00 22.77 ? 241 PRO B CG 1 ATOM 3927 C CD . PRO B 1 241 ? 15.743 4.583 -16.208 1.00 22.55 ? 241 PRO B CD 1 ATOM 3928 N N . ILE B 1 242 ? 13.274 2.534 -14.081 1.00 20.71 ? 242 ILE B N 1 ATOM 3929 C CA . ILE B 1 242 ? 12.095 1.984 -13.418 1.00 20.83 ? 242 ILE B CA 1 ATOM 3930 C C . ILE B 1 242 ? 11.852 0.601 -13.994 1.00 19.68 ? 242 ILE B C 1 ATOM 3931 O O . ILE B 1 242 ? 11.468 -0.340 -13.275 1.00 19.93 ? 242 ILE B O 1 ATOM 3932 C CB . ILE B 1 242 ? 10.837 2.843 -13.685 1.00 21.62 ? 242 ILE B CB 1 ATOM 3933 C CG1 . ILE B 1 242 ? 11.125 4.328 -13.415 1.00 23.46 ? 242 ILE B CG1 1 ATOM 3934 C CG2 . ILE B 1 242 ? 9.687 2.385 -12.806 1.00 22.33 ? 242 ILE B CG2 1 ATOM 3935 C CD1 . ILE B 1 242 ? 11.640 4.620 -12.020 1.00 24.81 ? 242 ILE B CD1 1 ATOM 3936 N N . VAL B 1 243 ? 12.054 0.476 -15.297 1.00 17.33 ? 243 VAL B N 1 ATOM 3937 C CA . VAL B 1 243 ? 11.841 -0.808 -15.908 1.00 18.12 ? 243 VAL B CA 1 ATOM 3938 C C . VAL B 1 243 ? 12.838 -1.794 -15.260 1.00 17.83 ? 243 VAL B C 1 ATOM 3939 O O . VAL B 1 243 ? 12.424 -2.762 -14.663 1.00 17.33 ? 243 VAL B O 1 ATOM 3940 C CB . VAL B 1 243 ? 11.901 -0.741 -17.444 1.00 17.72 ? 243 VAL B CB 1 ATOM 3941 C CG1 . VAL B 1 243 ? 12.089 -2.118 -18.027 1.00 17.71 ? 243 VAL B CG1 1 ATOM 3942 C CG2 . VAL B 1 243 ? 10.612 -0.112 -17.985 1.00 17.56 ? 243 VAL B CG2 1 ATOM 3943 N N . TYR B 1 244 ? 14.127 -1.474 -15.290 1.00 17.72 ? 244 TYR B N 1 ATOM 3944 C CA . TYR B 1 244 ? 15.149 -2.304 -14.654 1.00 19.02 ? 244 TYR B CA 1 ATOM 3945 C C . TYR B 1 244 ? 14.786 -2.655 -13.210 1.00 19.25 ? 244 TYR B C 1 ATOM 3946 O O . TYR B 1 244 ? 14.973 -3.787 -12.772 1.00 17.84 ? 244 TYR B O 1 ATOM 3947 C CB . TYR B 1 244 ? 16.479 -1.572 -14.598 1.00 19.59 ? 244 TYR B CB 1 ATOM 3948 C CG . TYR B 1 244 ? 17.225 -1.294 -15.886 1.00 20.78 ? 244 TYR B CG 1 ATOM 3949 C CD1 . TYR B 1 244 ? 17.214 -2.177 -16.954 1.00 22.73 ? 244 TYR B CD1 1 ATOM 3950 C CD2 . TYR B 1 244 ? 18.026 -0.154 -15.985 1.00 22.05 ? 244 TYR B CD2 1 ATOM 3951 C CE1 . TYR B 1 244 ? 17.973 -1.930 -18.100 1.00 24.48 ? 244 TYR B CE1 1 ATOM 3952 C CE2 . TYR B 1 244 ? 18.760 0.112 -17.125 1.00 24.35 ? 244 TYR B CE2 1 ATOM 3953 C CZ . TYR B 1 244 ? 18.739 -0.775 -18.177 1.00 24.06 ? 244 TYR B CZ 1 ATOM 3954 O OH . TYR B 1 244 ? 19.456 -0.473 -19.293 1.00 28.86 ? 244 TYR B OH 1 ATOM 3955 N N . GLN B 1 245 ? 14.302 -1.652 -12.471 1.00 19.32 ? 245 GLN B N 1 ATOM 3956 C CA . GLN B 1 245 ? 13.886 -1.843 -11.089 1.00 19.85 ? 245 GLN B CA 1 ATOM 3957 C C . GLN B 1 245 ? 12.803 -2.905 -10.930 1.00 18.40 ? 245 GLN B C 1 ATOM 3958 O O . GLN B 1 245 ? 12.930 -3.802 -10.116 1.00 16.78 ? 245 GLN B O 1 ATOM 3959 C CB . GLN B 1 245 ? 13.398 -0.541 -10.439 1.00 20.51 ? 245 GLN B CB 1 ATOM 3960 C CG . GLN B 1 245 ? 12.887 -0.819 -9.030 1.00 23.56 ? 245 GLN B CG 1 ATOM 3961 C CD . GLN B 1 245 ? 12.644 0.445 -8.230 1.00 26.20 ? 245 GLN B CD 1 ATOM 3962 O OE1 . GLN B 1 245 ? 13.566 1.224 -7.992 1.00 28.92 ? 245 GLN B OE1 1 ATOM 3963 N NE2 . GLN B 1 245 ? 11.400 0.661 -7.830 1.00 25.87 ? 245 GLN B NE2 1 ATOM 3964 N N . ARG B 1 246 ? 11.752 -2.818 -11.724 1.00 18.27 ? 246 ARG B N 1 ATOM 3965 C CA . ARG B 1 246 ? 10.666 -3.812 -11.666 1.00 17.89 ? 246 ARG B CA 1 ATOM 3966 C C . ARG B 1 246 ? 11.033 -5.224 -12.125 1.00 17.48 ? 246 ARG B C 1 ATOM 3967 O O . ARG B 1 246 ? 10.473 -6.219 -11.650 1.00 16.63 ? 246 ARG B O 1 ATOM 3968 C CB . ARG B 1 246 ? 9.487 -3.301 -12.517 1.00 17.99 ? 246 ARG B CB 1 ATOM 3969 C CG . ARG B 1 246 ? 8.969 -1.962 -12.029 1.00 18.36 ? 246 ARG B CG 1 ATOM 3970 C CD . ARG B 1 246 ? 8.498 -2.012 -10.569 1.00 18.52 ? 246 ARG B CD 1 ATOM 3971 N NE . ARG B 1 246 ? 7.167 -2.597 -10.438 1.00 18.39 ? 246 ARG B NE 1 ATOM 3972 C CZ . ARG B 1 246 ? 6.575 -2.961 -9.299 1.00 16.76 ? 246 ARG B CZ 1 ATOM 3973 N NH1 . ARG B 1 246 ? 7.208 -2.884 -8.127 1.00 16.65 ? 246 ARG B NH1 1 ATOM 3974 N NH2 . ARG B 1 246 ? 5.351 -3.502 -9.359 1.00 16.01 ? 246 ARG B NH2 1 ATOM 3975 N N . LEU B 1 247 ? 11.950 -5.324 -13.061 1.00 17.72 ? 247 LEU B N 1 ATOM 3976 C CA . LEU B 1 247 ? 12.404 -6.657 -13.529 1.00 17.19 ? 247 LEU B CA 1 ATOM 3977 C C . LEU B 1 247 ? 13.203 -7.347 -12.418 1.00 17.57 ? 247 LEU B C 1 ATOM 3978 O O . LEU B 1 247 ? 12.950 -8.509 -12.108 1.00 17.80 ? 247 LEU B O 1 ATOM 3979 C CB . LEU B 1 247 ? 13.217 -6.536 -14.817 1.00 17.73 ? 247 LEU B CB 1 ATOM 3980 C CG . LEU B 1 247 ? 12.489 -6.052 -16.074 1.00 17.57 ? 247 LEU B CG 1 ATOM 3981 C CD1 . LEU B 1 247 ? 13.479 -5.845 -17.214 1.00 17.74 ? 247 LEU B CD1 1 ATOM 3982 C CD2 . LEU B 1 247 ? 11.369 -6.979 -16.508 1.00 18.13 ? 247 LEU B CD2 1 ATOM 3983 N N . ALA B 1 248 ? 14.135 -6.622 -11.789 1.00 17.12 ? 248 ALA B N 1 ATOM 3984 C CA . ALA B 1 248 ? 14.960 -7.160 -10.698 1.00 16.50 ? 248 ALA B CA 1 ATOM 3985 C C . ALA B 1 248 ? 14.086 -7.603 -9.510 1.00 18.08 ? 248 ALA B C 1 ATOM 3986 O O . ALA B 1 248 ? 14.330 -8.643 -8.835 1.00 15.15 ? 248 ALA B O 1 ATOM 3987 C CB . ALA B 1 248 ? 15.932 -6.087 -10.241 1.00 16.87 ? 248 ALA B CB 1 ATOM 3988 N N . GLN B 1 249 ? 13.096 -6.754 -9.237 1.00 18.55 ? 249 GLN B N 1 ATOM 3989 C CA . GLN B 1 249 ? 12.120 -6.986 -8.168 1.00 19.18 ? 249 GLN B CA 1 ATOM 3990 C C . GLN B 1 249 ? 11.330 -8.266 -8.415 1.00 19.59 ? 249 GLN B C 1 ATOM 3991 O O . GLN B 1 249 ? 11.242 -9.127 -7.556 1.00 20.03 ? 249 GLN B O 1 ATOM 3992 C CB . GLN B 1 249 ? 11.195 -5.780 -8.046 1.00 17.98 ? 249 GLN B CB 1 ATOM 3993 C CG . GLN B 1 249 ? 11.708 -4.708 -7.082 1.00 18.36 ? 249 GLN B CG 1 ATOM 3994 C CD . GLN B 1 249 ? 10.777 -3.507 -7.019 1.00 18.35 ? 249 GLN B CD 1 ATOM 3995 O OE1 . GLN B 1 249 ? 10.221 -3.093 -8.033 1.00 17.15 ? 249 GLN B OE1 1 ATOM 3996 N NE2 . GLN B 1 249 ? 10.602 -2.946 -5.831 1.00 17.84 ? 249 GLN B NE2 1 ATOM 3997 N N . GLY B 1 250 ? 10.772 -8.395 -9.604 1.00 20.20 ? 250 GLY B N 1 ATOM 3998 C CA . GLY B 1 250 ? 10.103 -9.633 -10.006 1.00 20.63 ? 250 GLY B CA 1 ATOM 3999 C C . GLY B 1 250 ? 10.951 -10.879 -9.857 1.00 19.21 ? 250 GLY B C 1 ATOM 4000 O O . GLY B 1 250 ? 10.522 -11.850 -9.246 1.00 19.45 ? 250 GLY B O 1 ATOM 4001 N N . GLY B 1 251 ? 12.159 -10.821 -10.415 1.00 19.96 ? 251 GLY B N 1 ATOM 4002 C CA . GLY B 1 251 ? 13.174 -11.875 -10.317 1.00 19.62 ? 251 GLY B CA 1 ATOM 4003 C C . GLY B 1 251 ? 13.552 -12.266 -8.905 1.00 20.41 ? 251 GLY B C 1 ATOM 4004 O O . GLY B 1 251 ? 13.595 -13.457 -8.545 1.00 21.06 ? 251 GLY B O 1 ATOM 4005 N N . VAL B 1 252 ? 13.832 -11.256 -8.103 1.00 21.06 ? 252 VAL B N 1 ATOM 4006 C CA . VAL B 1 252 ? 14.182 -11.452 -6.705 1.00 22.23 ? 252 VAL B CA 1 ATOM 4007 C C . VAL B 1 252 ? 13.007 -12.029 -5.942 1.00 22.21 ? 252 VAL B C 1 ATOM 4008 O O . VAL B 1 252 ? 13.168 -12.957 -5.167 1.00 24.11 ? 252 VAL B O 1 ATOM 4009 C CB . VAL B 1 252 ? 14.662 -10.118 -6.100 1.00 22.91 ? 252 VAL B CB 1 ATOM 4010 C CG1 . VAL B 1 252 ? 14.683 -10.161 -4.580 1.00 24.16 ? 252 VAL B CG1 1 ATOM 4011 C CG2 . VAL B 1 252 ? 16.063 -9.803 -6.622 1.00 21.89 ? 252 VAL B CG2 1 ATOM 4012 N N . ARG B 1 253 ? 11.811 -11.501 -6.197 1.00 20.79 ? 253 ARG B N 1 ATOM 4013 C CA . ARG B 1 253 ? 10.623 -11.930 -5.488 1.00 18.71 ? 253 ARG B CA 1 ATOM 4014 C C . ARG B 1 253 ? 10.125 -13.260 -5.956 1.00 18.16 ? 253 ARG B C 1 ATOM 4015 O O . ARG B 1 253 ? 9.691 -14.072 -5.158 1.00 18.06 ? 253 ARG B O 1 ATOM 4016 C CB . ARG B 1 253 ? 9.564 -10.876 -5.604 1.00 18.64 ? 253 ARG B CB 1 ATOM 4017 C CG . ARG B 1 253 ? 9.780 -9.794 -4.545 1.00 18.36 ? 253 ARG B CG 1 ATOM 4018 C CD . ARG B 1 253 ? 9.176 -8.491 -4.982 1.00 18.25 ? 253 ARG B CD 1 ATOM 4019 N NE . ARG B 1 253 ? 9.222 -7.474 -3.934 1.00 18.15 ? 253 ARG B NE 1 ATOM 4020 C CZ . ARG B 1 253 ? 8.786 -6.237 -4.111 1.00 18.40 ? 253 ARG B CZ 1 ATOM 4021 N NH1 . ARG B 1 253 ? 8.275 -5.882 -5.295 1.00 17.55 ? 253 ARG B NH1 1 ATOM 4022 N NH2 . ARG B 1 253 ? 8.832 -5.359 -3.104 1.00 18.24 ? 253 ARG B NH2 1 ATOM 4023 N N . LEU B 1 254 ? 10.205 -13.518 -7.245 1.00 18.18 ? 254 LEU B N 1 ATOM 4024 C CA . LEU B 1 254 ? 9.895 -14.872 -7.702 1.00 17.83 ? 254 LEU B CA 1 ATOM 4025 C C . LEU B 1 254 ? 10.778 -15.871 -6.954 1.00 17.03 ? 254 LEU B C 1 ATOM 4026 O O . LEU B 1 254 ? 10.267 -16.754 -6.323 1.00 16.59 ? 254 LEU B O 1 ATOM 4027 C CB . LEU B 1 254 ? 10.036 -15.004 -9.207 1.00 17.58 ? 254 LEU B CB 1 ATOM 4028 C CG . LEU B 1 254 ? 9.753 -16.384 -9.798 1.00 17.15 ? 254 LEU B CG 1 ATOM 4029 C CD1 . LEU B 1 254 ? 8.466 -16.978 -9.253 1.00 16.98 ? 254 LEU B CD1 1 ATOM 4030 C CD2 . LEU B 1 254 ? 9.710 -16.268 -11.294 1.00 18.15 ? 254 LEU B CD2 1 ATOM 4031 N N . ALA B 1 255 ? 12.089 -15.670 -6.959 1.00 18.54 ? 255 ALA B N 1 ATOM 4032 C CA . ALA B 1 255 ? 13.020 -16.567 -6.230 1.00 18.50 ? 255 ALA B CA 1 ATOM 4033 C C . ALA B 1 255 ? 12.712 -16.796 -4.756 1.00 20.02 ? 255 ALA B C 1 ATOM 4034 O O . ALA B 1 255 ? 12.645 -17.932 -4.304 1.00 21.38 ? 255 ALA B O 1 ATOM 4035 C CB . ALA B 1 255 ? 14.416 -16.076 -6.380 1.00 17.93 ? 255 ALA B CB 1 ATOM 4036 N N . ALA B 1 256 ? 12.528 -15.721 -4.012 1.00 21.63 ? 256 ALA B N 1 ATOM 4037 C CA . ALA B 1 256 ? 12.213 -15.788 -2.595 1.00 22.15 ? 256 ALA B CA 1 ATOM 4038 C C . ALA B 1 256 ? 10.885 -16.494 -2.302 1.00 23.13 ? 256 ALA B C 1 ATOM 4039 O O . ALA B 1 256 ? 10.681 -17.038 -1.186 1.00 21.73 ? 256 ALA B O 1 ATOM 4040 C CB . ALA B 1 256 ? 12.158 -14.376 -2.029 1.00 22.40 ? 256 ALA B CB 1 ATOM 4041 N N . THR B 1 257 ? 9.960 -16.434 -3.263 1.00 21.77 ? 257 THR B N 1 ATOM 4042 C CA . THR B 1 257 ? 8.646 -17.027 -3.066 1.00 21.71 ? 257 THR B CA 1 ATOM 4043 C C . THR B 1 257 ? 8.775 -18.546 -3.214 1.00 21.25 ? 257 THR B C 1 ATOM 4044 O O . THR B 1 257 ? 8.179 -19.317 -2.439 1.00 19.96 ? 257 THR B O 1 ATOM 4045 C CB . THR B 1 257 ? 7.609 -16.458 -4.051 1.00 23.41 ? 257 THR B CB 1 ATOM 4046 O OG1 . THR B 1 257 ? 7.358 -15.086 -3.723 1.00 23.89 ? 257 THR B OG1 1 ATOM 4047 C CG2 . THR B 1 257 ? 6.288 -17.240 -3.966 1.00 24.58 ? 257 THR B CG2 1 ATOM 4048 N N . LEU B 1 258 ? 9.576 -18.983 -4.172 1.00 20.60 ? 258 LEU B N 1 ATOM 4049 C CA . LEU B 1 258 ? 9.728 -20.410 -4.380 1.00 22.05 ? 258 LEU B CA 1 ATOM 4050 C C . LEU B 1 258 ? 10.582 -21.016 -3.304 1.00 24.25 ? 258 LEU B C 1 ATOM 4051 O O . LEU B 1 258 ? 10.329 -22.143 -2.893 1.00 26.42 ? 258 LEU B O 1 ATOM 4052 C CB . LEU B 1 258 ? 10.294 -20.730 -5.739 1.00 21.63 ? 258 LEU B CB 1 ATOM 4053 C CG . LEU B 1 258 ? 9.434 -20.241 -6.913 1.00 22.04 ? 258 LEU B CG 1 ATOM 4054 C CD1 . LEU B 1 258 ? 10.199 -20.365 -8.201 1.00 21.90 ? 258 LEU B CD1 1 ATOM 4055 C CD2 . LEU B 1 258 ? 8.121 -21.010 -6.975 1.00 23.31 ? 258 LEU B CD2 1 ATOM 4056 N N . ASN B 1 259 ? 11.580 -20.275 -2.842 1.00 25.44 ? 259 ASN B N 1 ATOM 4057 C CA . ASN B 1 259 ? 12.391 -20.714 -1.732 1.00 26.16 ? 259 ASN B CA 1 ATOM 4058 C C . ASN B 1 259 ? 11.533 -20.935 -0.491 1.00 27.91 ? 259 ASN B C 1 ATOM 4059 O O . ASN B 1 259 ? 11.662 -21.965 0.176 1.00 30.35 ? 259 ASN B O 1 ATOM 4060 C CB . ASN B 1 259 ? 13.507 -19.698 -1.450 1.00 25.62 ? 259 ASN B CB 1 ATOM 4061 C CG . ASN B 1 259 ? 14.598 -19.724 -2.503 1.00 24.61 ? 259 ASN B CG 1 ATOM 4062 O OD1 . ASN B 1 259 ? 14.790 -20.722 -3.183 1.00 23.09 ? 259 ASN B OD1 1 ATOM 4063 N ND2 . ASN B 1 259 ? 15.300 -18.612 -2.661 1.00 24.81 ? 259 ASN B ND2 1 ATOM 4064 N N . ARG B 1 260 ? 10.674 -19.976 -0.163 1.00 29.24 ? 260 ARG B N 1 ATOM 4065 C CA . ARG B 1 260 ? 9.750 -20.141 0.970 1.00 31.55 ? 260 ARG B CA 1 ATOM 4066 C C . ARG B 1 260 ? 8.799 -21.306 0.728 1.00 30.89 ? 260 ARG B C 1 ATOM 4067 O O . ARG B 1 260 ? 8.608 -22.152 1.596 1.00 29.64 ? 260 ARG B O 1 ATOM 4068 C CB . ARG B 1 260 ? 8.931 -18.879 1.245 1.00 35.45 ? 260 ARG B CB 1 ATOM 4069 C CG . ARG B 1 260 ? 9.482 -17.996 2.363 1.00 39.68 ? 260 ARG B CG 1 ATOM 4070 C CD . ARG B 1 260 ? 8.438 -16.979 2.821 1.00 42.14 ? 260 ARG B CD 1 ATOM 4071 N NE . ARG B 1 260 ? 7.959 -16.230 1.675 1.00 45.72 ? 260 ARG B NE 1 ATOM 4072 C CZ . ARG B 1 260 ? 8.627 -15.238 1.087 1.00 49.24 ? 260 ARG B CZ 1 ATOM 4073 N NH1 . ARG B 1 260 ? 9.803 -14.835 1.559 1.00 50.44 ? 260 ARG B NH1 1 ATOM 4074 N NH2 . ARG B 1 260 ? 8.108 -14.633 0.019 1.00 50.24 ? 260 ARG B NH2 1 ATOM 4075 N N . ILE B 1 261 ? 8.208 -21.358 -0.460 1.00 30.77 ? 261 ILE B N 1 ATOM 4076 C CA . ILE B 1 261 ? 7.219 -22.392 -0.764 1.00 31.37 ? 261 ILE B CA 1 ATOM 4077 C C . ILE B 1 261 ? 7.802 -23.798 -0.630 1.00 32.05 ? 261 ILE B C 1 ATOM 4078 O O . ILE B 1 261 ? 7.172 -24.678 -0.079 1.00 34.84 ? 261 ILE B O 1 ATOM 4079 C CB . ILE B 1 261 ? 6.611 -22.191 -2.164 1.00 31.00 ? 261 ILE B CB 1 ATOM 4080 C CG1 . ILE B 1 261 ? 5.558 -21.083 -2.108 1.00 31.98 ? 261 ILE B CG1 1 ATOM 4081 C CG2 . ILE B 1 261 ? 6.005 -23.477 -2.683 1.00 32.92 ? 261 ILE B CG2 1 ATOM 4082 C CD1 . ILE B 1 261 ? 5.119 -20.605 -3.477 1.00 33.17 ? 261 ILE B CD1 1 ATOM 4083 N N . PHE B 1 262 ? 9.010 -24.005 -1.118 1.00 34.16 ? 262 PHE B N 1 ATOM 4084 C CA . PHE B 1 262 ? 9.572 -25.345 -1.160 1.00 34.71 ? 262 PHE B CA 1 ATOM 4085 C C . PHE B 1 262 ? 10.385 -25.736 0.088 1.00 35.98 ? 262 PHE B C 1 ATOM 4086 O O . PHE B 1 262 ? 10.727 -26.900 0.255 1.00 40.91 ? 262 PHE B O 1 ATOM 4087 C CB . PHE B 1 262 ? 10.387 -25.511 -2.447 1.00 32.18 ? 262 PHE B CB 1 ATOM 4088 C CG . PHE B 1 262 ? 9.550 -25.511 -3.694 1.00 33.14 ? 262 PHE B CG 1 ATOM 4089 C CD1 . PHE B 1 262 ? 8.469 -26.387 -3.828 1.00 33.18 ? 262 PHE B CD1 1 ATOM 4090 C CD2 . PHE B 1 262 ? 9.839 -24.654 -4.746 1.00 31.78 ? 262 PHE B CD2 1 ATOM 4091 C CE1 . PHE B 1 262 ? 7.697 -26.386 -4.981 1.00 34.71 ? 262 PHE B CE1 1 ATOM 4092 C CE2 . PHE B 1 262 ? 9.075 -24.652 -5.900 1.00 31.47 ? 262 PHE B CE2 1 ATOM 4093 C CZ . PHE B 1 262 ? 7.999 -25.512 -6.021 1.00 33.70 ? 262 PHE B CZ 1 ATOM 4094 N N . GLY B 1 263 ? 10.662 -24.788 0.977 1.00 38.65 ? 263 GLY B N 1 ATOM 4095 C CA . GLY B 1 263 ? 11.476 -25.057 2.171 1.00 41.27 ? 263 GLY B CA 1 ATOM 4096 C C . GLY B 1 263 ? 10.717 -25.252 3.484 1.00 42.76 ? 263 GLY B C 1 ATOM 4097 O O . GLY B 1 263 ? 9.665 -24.659 3.728 1.00 43.23 ? 263 GLY B O 1 ATOM 4098 N N . HIS B 1 264 ? 11.150 -25.992 4.377 1.00 40.02 ? 264 HIS B N 1 HETATM 4099 C C1 . NAG C 2 . ? -17.333 21.422 9.082 1.00 21.86 ? 301 NAG A C1 1 HETATM 4100 C C2 . NAG C 2 . ? -18.136 20.504 10.010 1.00 21.74 ? 301 NAG A C2 1 HETATM 4101 C C3 . NAG C 2 . ? -19.293 21.333 10.596 1.00 22.80 ? 301 NAG A C3 1 HETATM 4102 C C4 . NAG C 2 . ? -18.694 22.523 11.356 1.00 22.72 ? 301 NAG A C4 1 HETATM 4103 C C5 . NAG C 2 . ? -17.609 23.226 10.532 1.00 21.91 ? 301 NAG A C5 1 HETATM 4104 C C6 . NAG C 2 . ? -16.734 24.204 11.333 1.00 21.67 ? 301 NAG A C6 1 HETATM 4105 C C7 . NAG C 2 . ? -17.977 18.102 9.288 1.00 19.93 ? 301 NAG A C7 1 HETATM 4106 C C8 . NAG C 2 . ? -16.628 17.897 9.903 1.00 19.46 ? 301 NAG A C8 1 HETATM 4107 N N2 . NAG C 2 . ? -18.606 19.278 9.366 1.00 20.53 ? 301 NAG A N2 1 HETATM 4108 O O3 . NAG C 2 . ? -20.047 20.493 11.458 1.00 24.08 ? 301 NAG A O3 1 HETATM 4109 O O4 . NAG C 2 . ? -19.652 23.539 11.531 1.00 24.94 ? 301 NAG A O4 1 HETATM 4110 O O5 . NAG C 2 . ? -16.734 22.339 9.902 1.00 20.92 ? 301 NAG A O5 1 HETATM 4111 O O6 . NAG C 2 . ? -16.163 23.561 12.456 1.00 22.07 ? 301 NAG A O6 1 HETATM 4112 O O7 . NAG C 2 . ? -18.499 17.144 8.720 1.00 23.78 ? 301 NAG A O7 1 HETATM 4113 C C1 . NAG D 2 . ? -20.506 23.419 12.657 1.00 26.68 ? 302 NAG A C1 1 HETATM 4114 C C2 . NAG D 2 . ? -21.113 24.805 12.919 1.00 27.50 ? 302 NAG A C2 1 HETATM 4115 C C3 . NAG D 2 . ? -21.914 24.681 14.220 1.00 28.16 ? 302 NAG A C3 1 HETATM 4116 C C4 . NAG D 2 . ? -23.005 23.658 14.003 1.00 27.21 ? 302 NAG A C4 1 HETATM 4117 C C5 . NAG D 2 . ? -22.379 22.320 13.592 1.00 27.07 ? 302 NAG A C5 1 HETATM 4118 C C6 . NAG D 2 . ? -23.468 21.265 13.437 1.00 26.95 ? 302 NAG A C6 1 HETATM 4119 C C7 . NAG D 2 . ? -19.815 26.736 11.984 1.00 29.98 ? 302 NAG A C7 1 HETATM 4120 C C8 . NAG D 2 . ? -18.845 27.842 12.286 1.00 29.23 ? 302 NAG A C8 1 HETATM 4121 N N2 . NAG D 2 . ? -20.169 25.912 13.001 1.00 31.25 ? 302 NAG A N2 1 HETATM 4122 O O3 . NAG D 2 . ? -22.496 25.887 14.658 1.00 25.08 ? 302 NAG A O3 1 HETATM 4123 O O4 . NAG D 2 . ? -23.719 23.483 15.197 1.00 30.02 ? 302 NAG A O4 1 HETATM 4124 O O5 . NAG D 2 . ? -21.549 22.467 12.451 1.00 25.34 ? 302 NAG A O5 1 HETATM 4125 O O6 . NAG D 2 . ? -23.031 20.095 12.789 1.00 28.53 ? 302 NAG A O6 1 HETATM 4126 O O7 . NAG D 2 . ? -20.186 26.616 10.825 1.00 31.81 ? 302 NAG A O7 1 HETATM 4127 C C1 . BMA E 3 . ? -25.127 23.831 15.139 1.00 33.61 ? 303 BMA A C1 1 HETATM 4128 C C2 . BMA E 3 . ? -25.863 23.063 16.231 1.00 32.98 ? 303 BMA A C2 1 HETATM 4129 C C3 . BMA E 3 . ? -27.355 23.412 16.327 1.00 36.82 ? 303 BMA A C3 1 HETATM 4130 C C4 . BMA E 3 . ? -27.533 24.911 16.410 1.00 40.00 ? 303 BMA A C4 1 HETATM 4131 C C5 . BMA E 3 . ? -26.731 25.567 15.286 1.00 41.83 ? 303 BMA A C5 1 HETATM 4132 C C6 . BMA E 3 . ? -26.847 27.080 15.326 1.00 45.25 ? 303 BMA A C6 1 HETATM 4133 O O2 . BMA E 3 . ? -25.213 23.341 17.438 1.00 29.36 ? 303 BMA A O2 1 HETATM 4134 O O3 . BMA E 3 . ? -27.919 22.849 17.491 1.00 37.61 ? 303 BMA A O3 1 HETATM 4135 O O4 . BMA E 3 . ? -28.908 25.151 16.260 1.00 41.16 ? 303 BMA A O4 1 HETATM 4136 O O5 . BMA E 3 . ? -25.355 25.197 15.384 1.00 38.12 ? 303 BMA A O5 1 HETATM 4137 O O6 . BMA E 3 . ? -25.561 27.615 15.081 1.00 51.61 ? 303 BMA A O6 1 HETATM 4138 C C1 . MAN F 4 . ? -29.177 22.191 17.280 1.00 39.75 ? 304 MAN A C1 1 HETATM 4139 C C2 . MAN F 4 . ? -29.725 21.718 18.635 1.00 38.03 ? 304 MAN A C2 1 HETATM 4140 C C3 . MAN F 4 . ? -29.022 20.449 19.175 1.00 37.86 ? 304 MAN A C3 1 HETATM 4141 C C4 . MAN F 4 . ? -28.791 19.409 18.084 1.00 41.09 ? 304 MAN A C4 1 HETATM 4142 C C5 . MAN F 4 . ? -28.214 20.081 16.845 1.00 41.84 ? 304 MAN A C5 1 HETATM 4143 C C6 . MAN F 4 . ? -28.008 19.125 15.682 1.00 42.30 ? 304 MAN A C6 1 HETATM 4144 O O2 . MAN F 4 . ? -31.113 21.523 18.477 1.00 40.26 ? 304 MAN A O2 1 HETATM 4145 O O3 . MAN F 4 . ? -29.724 19.831 20.242 1.00 31.73 ? 304 MAN A O3 1 HETATM 4146 O O4 . MAN F 4 . ? -27.935 18.401 18.568 1.00 41.49 ? 304 MAN A O4 1 HETATM 4147 O O5 . MAN F 4 . ? -29.101 21.094 16.396 1.00 42.05 ? 304 MAN A O5 1 HETATM 4148 O O6 . MAN F 4 . ? -26.863 19.577 14.988 1.00 44.26 ? 304 MAN A O6 1 HETATM 4149 C C1 . MAN G 4 . ? -25.565 29.037 15.189 1.00 53.16 ? 305 MAN A C1 1 HETATM 4150 C C2 . MAN G 4 . ? -25.556 29.581 13.776 1.00 57.10 ? 305 MAN A C2 1 HETATM 4151 C C3 . MAN G 4 . ? -24.464 30.639 13.585 1.00 58.78 ? 305 MAN A C3 1 HETATM 4152 C C4 . MAN G 4 . ? -23.085 30.185 14.073 1.00 57.03 ? 305 MAN A C4 1 HETATM 4153 C C5 . MAN G 4 . ? -23.205 29.328 15.335 1.00 55.82 ? 305 MAN A C5 1 HETATM 4154 C C6 . MAN G 4 . ? -22.150 29.694 16.376 1.00 53.64 ? 305 MAN A C6 1 HETATM 4155 O O2 . MAN G 4 . ? -26.861 30.084 13.538 1.00 56.88 ? 305 MAN A O2 1 HETATM 4156 O O3 . MAN G 4 . ? -24.809 31.790 14.326 1.00 61.49 ? 305 MAN A O3 1 HETATM 4157 O O4 . MAN G 4 . ? -22.407 29.469 13.069 1.00 57.12 ? 305 MAN A O4 1 HETATM 4158 O O5 . MAN G 4 . ? -24.475 29.515 15.940 1.00 55.57 ? 305 MAN A O5 1 HETATM 4159 O O6 . MAN G 4 . ? -22.800 30.054 17.578 1.00 43.99 ? 305 MAN A O6 1 HETATM 4160 C C1 . NAG H 2 . ? -10.525 30.569 16.748 1.00 33.64 ? 331 NAG A C1 1 HETATM 4161 C C2 . NAG H 2 . ? -10.760 31.801 17.620 1.00 36.24 ? 331 NAG A C2 1 HETATM 4162 C C3 . NAG H 2 . ? -9.713 31.865 18.724 1.00 36.40 ? 331 NAG A C3 1 HETATM 4163 C C4 . NAG H 2 . ? -9.792 30.578 19.530 1.00 35.92 ? 331 NAG A C4 1 HETATM 4164 C C5 . NAG H 2 . ? -9.620 29.389 18.597 1.00 32.87 ? 331 NAG A C5 1 HETATM 4165 C C6 . NAG H 2 . ? -9.760 28.061 19.334 1.00 31.31 ? 331 NAG A C6 1 HETATM 4166 C C7 . NAG H 2 . ? -11.867 33.809 16.667 1.00 42.38 ? 331 NAG A C7 1 HETATM 4167 C C8 . NAG H 2 . ? -13.086 33.581 17.510 1.00 41.56 ? 331 NAG A C8 1 HETATM 4168 N N2 . NAG H 2 . ? -10.812 32.984 16.766 1.00 38.74 ? 331 NAG A N2 1 HETATM 4169 O O3 . NAG H 2 . ? -9.947 32.957 19.590 1.00 38.85 ? 331 NAG A O3 1 HETATM 4170 O O4 . NAG H 2 . ? -8.790 30.577 20.529 1.00 39.74 ? 331 NAG A O4 1 HETATM 4171 O O5 . NAG H 2 . ? -10.595 29.442 17.586 1.00 30.93 ? 331 NAG A O5 1 HETATM 4172 O O6 . NAG H 2 . ? -11.129 27.719 19.487 1.00 32.00 ? 331 NAG A O6 1 HETATM 4173 O O7 . NAG H 2 . ? -11.854 34.780 15.910 1.00 49.13 ? 331 NAG A O7 1 HETATM 4174 C C1 . NAG I 2 . ? -9.359 30.417 21.838 1.00 46.34 ? 332 NAG A C1 1 HETATM 4175 C C2 . NAG I 2 . ? -8.240 30.072 22.816 1.00 47.89 ? 332 NAG A C2 1 HETATM 4176 C C3 . NAG I 2 . ? -8.763 29.991 24.251 1.00 48.70 ? 332 NAG A C3 1 HETATM 4177 C C4 . NAG I 2 . ? -9.705 31.151 24.587 1.00 50.63 ? 332 NAG A C4 1 HETATM 4178 C C5 . NAG I 2 . ? -10.768 31.255 23.495 1.00 51.58 ? 332 NAG A C5 1 HETATM 4179 C C6 . NAG I 2 . ? -11.855 32.291 23.777 1.00 53.57 ? 332 NAG A C6 1 HETATM 4180 C C7 . NAG I 2 . ? -6.655 28.694 21.539 1.00 49.52 ? 332 NAG A C7 1 HETATM 4181 C C8 . NAG I 2 . ? -6.192 27.310 21.197 1.00 51.06 ? 332 NAG A C8 1 HETATM 4182 N N2 . NAG I 2 . ? -7.671 28.796 22.404 1.00 46.18 ? 332 NAG A N2 1 HETATM 4183 O O3 . NAG I 2 . ? -7.675 29.983 25.145 1.00 51.04 ? 332 NAG A O3 1 HETATM 4184 O O4 . NAG I 2 . ? -10.303 30.973 25.856 1.00 52.41 ? 332 NAG A O4 1 HETATM 4185 O O5 . NAG I 2 . ? -10.083 31.556 22.291 1.00 48.96 ? 332 NAG A O5 1 HETATM 4186 O O6 . NAG I 2 . ? -11.274 33.562 23.959 1.00 57.10 ? 332 NAG A O6 1 HETATM 4187 O O7 . NAG I 2 . ? -6.091 29.649 21.010 1.00 50.07 ? 332 NAG A O7 1 HETATM 4188 C C1 . NAG J 2 . ? 12.642 0.514 12.445 1.00 28.35 ? 361 NAG A C1 1 HETATM 4189 C C2 . NAG J 2 . ? 11.805 -0.034 13.576 1.00 28.54 ? 361 NAG A C2 1 HETATM 4190 C C3 . NAG J 2 . ? 12.555 -1.201 14.202 1.00 31.44 ? 361 NAG A C3 1 HETATM 4191 C C4 . NAG J 2 . ? 12.956 -2.269 13.170 1.00 33.98 ? 361 NAG A C4 1 HETATM 4192 C C5 . NAG J 2 . ? 13.719 -1.550 12.060 1.00 33.86 ? 361 NAG A C5 1 HETATM 4193 C C6 . NAG J 2 . ? 14.290 -2.467 10.977 1.00 36.27 ? 361 NAG A C6 1 HETATM 4194 C C7 . NAG J 2 . ? 10.426 1.732 14.539 1.00 25.53 ? 361 NAG A C7 1 HETATM 4195 C C8 . NAG J 2 . ? 10.255 2.738 15.646 1.00 24.72 ? 361 NAG A C8 1 HETATM 4196 N N2 . NAG J 2 . ? 11.523 0.973 14.575 1.00 26.63 ? 361 NAG A N2 1 HETATM 4197 O O3 . NAG J 2 . ? 11.790 -1.716 15.265 1.00 30.31 ? 361 NAG A O3 1 HETATM 4198 O O4 . NAG J 2 . ? 13.864 -3.119 13.820 1.00 36.61 ? 361 NAG A O4 1 HETATM 4199 O O5 . NAG J 2 . ? 12.922 -0.531 11.501 1.00 29.99 ? 361 NAG A O5 1 HETATM 4200 O O6 . NAG J 2 . ? 13.324 -2.819 10.029 1.00 38.24 ? 361 NAG A O6 1 HETATM 4201 O O7 . NAG J 2 . ? 9.592 1.674 13.632 1.00 27.09 ? 361 NAG A O7 1 HETATM 4202 C C1 . NAG K 2 . ? 13.631 -4.547 13.680 1.00 43.72 ? 362 NAG A C1 1 HETATM 4203 C C2 . NAG K 2 . ? 14.964 -5.153 14.154 1.00 45.11 ? 362 NAG A C2 1 HETATM 4204 C C3 . NAG K 2 . ? 14.865 -6.463 14.939 1.00 49.94 ? 362 NAG A C3 1 HETATM 4205 C C4 . NAG K 2 . ? 13.806 -6.254 16.012 1.00 50.09 ? 362 NAG A C4 1 HETATM 4206 C C5 . NAG K 2 . ? 12.484 -6.088 15.270 1.00 47.89 ? 362 NAG A C5 1 HETATM 4207 C C6 . NAG K 2 . ? 11.302 -5.944 16.227 1.00 49.29 ? 362 NAG A C6 1 HETATM 4208 C C7 . NAG K 2 . ? 16.949 -4.306 13.054 1.00 49.62 ? 362 NAG A C7 1 HETATM 4209 C C8 . NAG K 2 . ? 17.927 -4.408 11.922 1.00 51.48 ? 362 NAG A C8 1 HETATM 4210 N N2 . NAG K 2 . ? 15.937 -5.186 13.086 1.00 43.55 ? 362 NAG A N2 1 HETATM 4211 O O3 . NAG K 2 . ? 16.085 -6.747 15.590 1.00 51.38 ? 362 NAG A O3 1 HETATM 4212 O O4 . NAG K 2 . ? 13.809 -7.334 16.932 1.00 52.47 ? 362 NAG A O4 1 HETATM 4213 O O5 . NAG K 2 . ? 12.474 -4.964 14.397 1.00 43.11 ? 362 NAG A O5 1 HETATM 4214 O O6 . NAG K 2 . ? 10.108 -6.080 15.474 1.00 46.31 ? 362 NAG A O6 1 HETATM 4215 O O7 . NAG K 2 . ? 17.119 -3.417 13.893 1.00 51.18 ? 362 NAG A O7 1 HETATM 4216 ZN ZN . ZN L 5 . ? -9.964 12.016 19.099 1.00 22.93 ? 431 ZN A ZN 1 HETATM 4217 ZN ZN . ZN M 5 . ? -9.597 6.543 20.840 1.00 18.91 ? 432 ZN A ZN 1 HETATM 4218 ZN ZN . ZN N 5 . ? -6.908 10.401 19.233 1.00 15.96 ? 433 ZN A ZN 1 HETATM 4219 C C1 . NAG O 2 . ? -6.694 -21.434 -9.034 1.00 22.87 ? 301 NAG B C1 1 HETATM 4220 C C2 . NAG O 2 . ? -7.528 -20.526 -9.971 1.00 22.23 ? 301 NAG B C2 1 HETATM 4221 C C3 . NAG O 2 . ? -8.694 -21.339 -10.536 1.00 22.16 ? 301 NAG B C3 1 HETATM 4222 C C4 . NAG O 2 . ? -8.100 -22.562 -11.251 1.00 22.84 ? 301 NAG B C4 1 HETATM 4223 C C5 . NAG O 2 . ? -7.001 -23.284 -10.443 1.00 23.18 ? 301 NAG B C5 1 HETATM 4224 C C6 . NAG O 2 . ? -6.149 -24.242 -11.286 1.00 23.34 ? 301 NAG B C6 1 HETATM 4225 C C7 . NAG O 2 . ? -7.442 -18.135 -9.187 1.00 20.50 ? 301 NAG B C7 1 HETATM 4226 C C8 . NAG O 2 . ? -6.099 -17.840 -9.789 1.00 18.67 ? 301 NAG B C8 1 HETATM 4227 N N2 . NAG O 2 . ? -8.035 -19.335 -9.299 1.00 20.62 ? 301 NAG B N2 1 HETATM 4228 O O3 . NAG O 2 . ? -9.534 -20.526 -11.375 1.00 20.92 ? 301 NAG B O3 1 HETATM 4229 O O4 . NAG O 2 . ? -9.071 -23.570 -11.440 1.00 23.00 ? 301 NAG B O4 1 HETATM 4230 O O5 . NAG O 2 . ? -6.090 -22.422 -9.821 1.00 23.26 ? 301 NAG B O5 1 HETATM 4231 O O6 . NAG O 2 . ? -5.688 -23.579 -12.452 1.00 24.26 ? 301 NAG B O6 1 HETATM 4232 O O7 . NAG O 2 . ? -7.988 -17.226 -8.559 1.00 24.22 ? 301 NAG B O7 1 HETATM 4233 C C1 . NAG P 2 . ? -9.949 -23.352 -12.551 1.00 26.49 ? 302 NAG B C1 1 HETATM 4234 C C2 . NAG P 2 . ? -10.521 -24.724 -12.880 1.00 27.54 ? 302 NAG B C2 1 HETATM 4235 C C3 . NAG P 2 . ? -11.386 -24.624 -14.118 1.00 30.35 ? 302 NAG B C3 1 HETATM 4236 C C4 . NAG P 2 . ? -12.490 -23.636 -13.871 1.00 31.29 ? 302 NAG B C4 1 HETATM 4237 C C5 . NAG P 2 . ? -11.939 -22.292 -13.377 1.00 28.11 ? 302 NAG B C5 1 HETATM 4238 C C6 . NAG P 2 . ? -13.100 -21.395 -12.957 1.00 27.81 ? 302 NAG B C6 1 HETATM 4239 C C7 . NAG P 2 . ? -9.150 -26.561 -12.081 1.00 27.67 ? 302 NAG B C7 1 HETATM 4240 C C8 . NAG P 2 . ? -8.137 -27.638 -12.393 1.00 26.96 ? 302 NAG B C8 1 HETATM 4241 N N2 . NAG P 2 . ? -9.530 -25.762 -13.082 1.00 28.46 ? 302 NAG B N2 1 HETATM 4242 O O3 . NAG P 2 . ? -11.968 -25.860 -14.437 1.00 32.29 ? 302 NAG B O3 1 HETATM 4243 O O4 . NAG P 2 . ? -13.146 -23.465 -15.108 1.00 37.76 ? 302 NAG B O4 1 HETATM 4244 O O5 . NAG P 2 . ? -11.007 -22.424 -12.308 1.00 25.24 ? 302 NAG B O5 1 HETATM 4245 O O6 . NAG P 2 . ? -12.629 -20.094 -12.681 1.00 26.05 ? 302 NAG B O6 1 HETATM 4246 O O7 . NAG P 2 . ? -9.583 -26.412 -10.939 1.00 24.44 ? 302 NAG B O7 1 HETATM 4247 C C1 . BMA Q 3 . ? -14.511 -23.904 -15.098 1.00 42.62 ? 303 BMA B C1 1 HETATM 4248 C C2 . BMA Q 3 . ? -15.282 -23.037 -16.068 1.00 43.39 ? 303 BMA B C2 1 HETATM 4249 C C3 . BMA Q 3 . ? -16.755 -23.402 -16.029 1.00 48.19 ? 303 BMA B C3 1 HETATM 4250 C C4 . BMA Q 3 . ? -16.967 -24.890 -16.215 1.00 52.19 ? 303 BMA B C4 1 HETATM 4251 C C5 . BMA Q 3 . ? -15.974 -25.709 -15.394 1.00 55.06 ? 303 BMA B C5 1 HETATM 4252 C C6 . BMA Q 3 . ? -16.034 -27.165 -15.826 1.00 57.53 ? 303 BMA B C6 1 HETATM 4253 O O2 . BMA Q 3 . ? -14.748 -23.277 -17.342 1.00 38.80 ? 303 BMA B O2 1 HETATM 4254 O O3 . BMA Q 3 . ? -17.473 -22.752 -17.055 1.00 49.39 ? 303 BMA B O3 1 HETATM 4255 O O4 . BMA Q 3 . ? -18.282 -25.172 -15.798 1.00 55.59 ? 303 BMA B O4 1 HETATM 4256 O O5 . BMA Q 3 . ? -14.640 -25.235 -15.531 1.00 47.78 ? 303 BMA B O5 1 HETATM 4257 O O6 . BMA Q 3 . ? -15.194 -27.881 -14.955 1.00 63.83 ? 303 BMA B O6 1 HETATM 4258 C C1 . MAN R 4 . ? -18.624 -22.036 -16.553 1.00 53.97 ? 304 MAN B C1 1 HETATM 4259 C C2 . MAN R 4 . ? -19.914 -22.554 -17.220 1.00 55.77 ? 304 MAN B C2 1 HETATM 4260 C C3 . MAN R 4 . ? -20.230 -21.921 -18.584 1.00 54.67 ? 304 MAN B C3 1 HETATM 4261 C C4 . MAN R 4 . ? -19.501 -20.598 -18.915 1.00 57.43 ? 304 MAN B C4 1 HETATM 4262 C C5 . MAN R 4 . ? -18.232 -20.350 -18.121 1.00 58.74 ? 304 MAN B C5 1 HETATM 4263 C C6 . MAN R 4 . ? -17.849 -18.888 -18.246 1.00 57.80 ? 304 MAN B C6 1 HETATM 4264 O O2 . MAN R 4 . ? -21.057 -22.464 -16.369 1.00 51.53 ? 304 MAN B O2 1 HETATM 4265 O O3 . MAN R 4 . ? -21.638 -21.773 -18.631 1.00 53.42 ? 304 MAN B O3 1 HETATM 4266 O O4 . MAN R 4 . ? -19.079 -20.534 -20.265 1.00 56.56 ? 304 MAN B O4 1 HETATM 4267 O O5 . MAN R 4 . ? -18.450 -20.660 -16.761 1.00 58.65 ? 304 MAN B O5 1 HETATM 4268 O O6 . MAN R 4 . ? -16.707 -18.676 -17.461 1.00 61.71 ? 304 MAN B O6 1 HETATM 4269 C C1 . MAN S 4 . ? -15.186 -29.266 -15.316 1.00 63.94 ? 305 MAN B C1 1 HETATM 4270 C C2 . MAN S 4 . ? -15.207 -30.098 -14.038 1.00 66.22 ? 305 MAN B C2 1 HETATM 4271 C C3 . MAN S 4 . ? -13.877 -30.836 -13.819 1.00 66.98 ? 305 MAN B C3 1 HETATM 4272 C C4 . MAN S 4 . ? -12.694 -29.916 -14.096 1.00 65.58 ? 305 MAN B C4 1 HETATM 4273 C C5 . MAN S 4 . ? -12.827 -29.208 -15.450 1.00 65.52 ? 305 MAN B C5 1 HETATM 4274 C C6 . MAN S 4 . ? -11.678 -29.565 -16.394 1.00 64.64 ? 305 MAN B C6 1 HETATM 4275 O O2 . MAN S 4 . ? -16.316 -30.981 -14.063 1.00 65.66 ? 305 MAN B O2 1 HETATM 4276 O O3 . MAN S 4 . ? -13.768 -31.998 -14.621 1.00 65.50 ? 305 MAN B O3 1 HETATM 4277 O O4 . MAN S 4 . ? -12.628 -28.980 -13.044 1.00 66.13 ? 305 MAN B O4 1 HETATM 4278 O O5 . MAN S 4 . ? -14.047 -29.558 -16.082 1.00 66.47 ? 305 MAN B O5 1 HETATM 4279 O O6 . MAN S 4 . ? -12.121 -29.582 -17.736 1.00 58.89 ? 305 MAN B O6 1 HETATM 4280 C C1 . NAG T 2 . ? -0.037 -30.390 -16.516 1.00 35.67 ? 331 NAG B C1 1 HETATM 4281 C C2 . NAG T 2 . ? -0.319 -31.627 -17.346 1.00 36.21 ? 331 NAG B C2 1 HETATM 4282 C C3 . NAG T 2 . ? 0.690 -31.786 -18.473 1.00 35.40 ? 331 NAG B C3 1 HETATM 4283 C C4 . NAG T 2 . ? 0.718 -30.497 -19.301 1.00 35.02 ? 331 NAG B C4 1 HETATM 4284 C C5 . NAG T 2 . ? 0.940 -29.297 -18.392 1.00 33.60 ? 331 NAG B C5 1 HETATM 4285 C C6 . NAG T 2 . ? 0.875 -27.975 -19.156 1.00 31.07 ? 331 NAG B C6 1 HETATM 4286 C C7 . NAG T 2 . ? -1.492 -33.538 -16.282 1.00 38.87 ? 331 NAG B C7 1 HETATM 4287 C C8 . NAG T 2 . ? -2.688 -33.376 -17.175 1.00 38.55 ? 331 NAG B C8 1 HETATM 4288 N N2 . NAG T 2 . ? -0.418 -32.736 -16.407 1.00 38.36 ? 331 NAG B N2 1 HETATM 4289 O O3 . NAG T 2 . ? 0.314 -32.864 -19.309 1.00 36.94 ? 331 NAG B O3 1 HETATM 4290 O O4 . NAG T 2 . ? 1.735 -30.524 -20.285 1.00 34.90 ? 331 NAG B O4 1 HETATM 4291 O O5 . NAG T 2 . ? -0.052 -29.286 -17.387 1.00 35.36 ? 331 NAG B O5 1 HETATM 4292 O O6 . NAG T 2 . ? -0.471 -27.628 -19.380 1.00 30.22 ? 331 NAG B O6 1 HETATM 4293 O O7 . NAG T 2 . ? -1.510 -34.443 -15.455 1.00 44.13 ? 331 NAG B O7 1 HETATM 4294 C C1 . NAG U 2 . ? 1.212 -30.302 -21.607 1.00 41.39 ? 332 NAG B C1 1 HETATM 4295 C C2 . NAG U 2 . ? 2.316 -29.907 -22.571 1.00 42.80 ? 332 NAG B C2 1 HETATM 4296 C C3 . NAG U 2 . ? 1.777 -29.740 -23.990 1.00 46.16 ? 332 NAG B C3 1 HETATM 4297 C C4 . NAG U 2 . ? 0.736 -30.772 -24.442 1.00 49.59 ? 332 NAG B C4 1 HETATM 4298 C C5 . NAG U 2 . ? -0.197 -31.152 -23.285 1.00 47.69 ? 332 NAG B C5 1 HETATM 4299 C C6 . NAG U 2 . ? -1.012 -32.405 -23.559 1.00 47.41 ? 332 NAG B C6 1 HETATM 4300 C C7 . NAG U 2 . ? 3.945 -28.501 -21.372 1.00 44.67 ? 332 NAG B C7 1 HETATM 4301 C C8 . NAG U 2 . ? 4.312 -27.085 -21.043 1.00 47.52 ? 332 NAG B C8 1 HETATM 4302 N N2 . NAG U 2 . ? 2.865 -28.639 -22.141 1.00 43.66 ? 332 NAG B N2 1 HETATM 4303 O O3 . NAG U 2 . ? 2.865 -29.705 -24.881 1.00 46.77 ? 332 NAG B O3 1 HETATM 4304 O O4 . NAG U 2 . ? -0.005 -30.202 -25.521 1.00 58.75 ? 332 NAG B O4 1 HETATM 4305 O O5 . NAG U 2 . ? 0.565 -31.444 -22.125 1.00 44.54 ? 332 NAG B O5 1 HETATM 4306 O O6 . NAG U 2 . ? -0.111 -33.477 -23.431 1.00 45.40 ? 332 NAG B O6 1 HETATM 4307 O O7 . NAG U 2 . ? 4.621 -29.427 -20.935 1.00 44.28 ? 332 NAG B O7 1 HETATM 4308 C C1 . BMA V 3 . ? -0.217 -31.059 -26.687 1.00 66.42 ? 333 BMA B C1 1 HETATM 4309 C C2 . BMA V 3 . ? -0.804 -30.253 -27.868 1.00 66.36 ? 333 BMA B C2 1 HETATM 4310 C C3 . BMA V 3 . ? 0.251 -29.613 -28.776 1.00 68.86 ? 333 BMA B C3 1 HETATM 4311 C C4 . BMA V 3 . ? 1.624 -29.720 -28.126 1.00 69.74 ? 333 BMA B C4 1 HETATM 4312 C C5 . BMA V 3 . ? 1.881 -31.217 -27.951 1.00 70.03 ? 333 BMA B C5 1 HETATM 4313 C C6 . BMA V 3 . ? 3.294 -31.530 -27.458 1.00 68.18 ? 333 BMA B C6 1 HETATM 4314 O O2 . BMA V 3 . ? -1.699 -29.265 -27.401 1.00 65.57 ? 333 BMA B O2 1 HETATM 4315 O O3 . BMA V 3 . ? -0.068 -28.267 -29.044 1.00 70.12 ? 333 BMA B O3 1 HETATM 4316 O O4 . BMA V 3 . ? 2.616 -29.122 -28.930 1.00 67.88 ? 333 BMA B O4 1 HETATM 4317 O O5 . BMA V 3 . ? 0.931 -31.813 -27.078 1.00 68.90 ? 333 BMA B O5 1 HETATM 4318 O O6 . BMA V 3 . ? 4.030 -32.092 -28.519 1.00 64.07 ? 333 BMA B O6 1 HETATM 4319 C C1 . NAG W 2 . ? 23.240 -0.625 -12.787 1.00 30.13 ? 361 NAG B C1 1 HETATM 4320 C C2 . NAG W 2 . ? 22.343 -0.068 -13.896 1.00 30.38 ? 361 NAG B C2 1 HETATM 4321 C C3 . NAG W 2 . ? 23.048 1.070 -14.623 1.00 32.81 ? 361 NAG B C3 1 HETATM 4322 C C4 . NAG W 2 . ? 23.584 2.086 -13.613 1.00 35.31 ? 361 NAG B C4 1 HETATM 4323 C C5 . NAG W 2 . ? 24.308 1.402 -12.458 1.00 35.16 ? 361 NAG B C5 1 HETATM 4324 C C6 . NAG W 2 . ? 24.666 2.438 -11.409 1.00 35.56 ? 361 NAG B C6 1 HETATM 4325 C C7 . NAG W 2 . ? 20.920 -1.900 -14.686 1.00 26.35 ? 361 NAG B C7 1 HETATM 4326 C C8 . NAG W 2 . ? 20.768 -2.998 -15.709 1.00 23.74 ? 361 NAG B C8 1 HETATM 4327 N N2 . NAG W 2 . ? 22.006 -1.132 -14.802 1.00 28.44 ? 361 NAG B N2 1 HETATM 4328 O O3 . NAG W 2 . ? 22.139 1.634 -15.547 1.00 31.64 ? 361 NAG B O3 1 HETATM 4329 O O4 . NAG W 2 . ? 24.556 2.908 -14.210 1.00 38.32 ? 361 NAG B O4 1 HETATM 4330 O O5 . NAG W 2 . ? 23.499 0.417 -11.857 1.00 30.45 ? 361 NAG B O5 1 HETATM 4331 O O6 . NAG W 2 . ? 23.471 3.020 -10.957 1.00 35.15 ? 361 NAG B O6 1 HETATM 4332 O O7 . NAG W 2 . ? 20.097 -1.768 -13.780 1.00 25.37 ? 361 NAG B O7 1 HETATM 4333 C C1 . NAG X 2 . ? 24.239 4.313 -14.151 1.00 44.26 ? 362 NAG B C1 1 HETATM 4334 C C2 . NAG X 2 . ? 25.525 5.054 -14.527 1.00 45.25 ? 362 NAG B C2 1 HETATM 4335 C C3 . NAG X 2 . ? 25.344 6.527 -14.817 1.00 50.21 ? 362 NAG B C3 1 HETATM 4336 C C4 . NAG X 2 . ? 24.168 6.769 -15.749 1.00 50.35 ? 362 NAG B C4 1 HETATM 4337 C C5 . NAG X 2 . ? 22.938 5.965 -15.322 1.00 48.62 ? 362 NAG B C5 1 HETATM 4338 C C6 . NAG X 2 . ? 21.871 6.033 -16.416 1.00 49.84 ? 362 NAG B C6 1 HETATM 4339 C C7 . NAG X 2 . ? 27.673 4.267 -13.773 1.00 42.40 ? 362 NAG B C7 1 HETATM 4340 C C8 . NAG X 2 . ? 28.704 4.201 -12.678 1.00 40.88 ? 362 NAG B C8 1 HETATM 4341 N N2 . NAG X 2 . ? 26.555 4.938 -13.515 1.00 42.75 ? 362 NAG B N2 1 HETATM 4342 O O3 . NAG X 2 . ? 26.533 6.995 -15.424 1.00 51.70 ? 362 NAG B O3 1 HETATM 4343 O O4 . NAG X 2 . ? 23.843 8.135 -15.604 1.00 52.98 ? 362 NAG B O4 1 HETATM 4344 O O5 . NAG X 2 . ? 23.203 4.603 -15.056 1.00 45.44 ? 362 NAG B O5 1 HETATM 4345 O O6 . NAG X 2 . ? 22.463 5.836 -17.679 1.00 42.62 ? 362 NAG B O6 1 HETATM 4346 O O7 . NAG X 2 . ? 27.857 3.711 -14.860 1.00 43.80 ? 362 NAG B O7 1 HETATM 4347 C C1 . BMA Y 3 . ? 23.941 8.904 -16.811 1.00 51.97 ? 363 BMA B C1 1 HETATM 4348 C C2 . BMA Y 3 . ? 22.934 10.015 -16.606 1.00 52.26 ? 363 BMA B C2 1 HETATM 4349 C C3 . BMA Y 3 . ? 22.927 11.004 -17.761 1.00 53.23 ? 363 BMA B C3 1 HETATM 4350 C C4 . BMA Y 3 . ? 24.347 11.416 -18.120 1.00 51.33 ? 363 BMA B C4 1 HETATM 4351 C C5 . BMA Y 3 . ? 25.357 10.253 -18.146 1.00 49.67 ? 363 BMA B C5 1 HETATM 4352 C C6 . BMA Y 3 . ? 26.804 10.755 -18.253 1.00 52.20 ? 363 BMA B C6 1 HETATM 4353 O O2 . BMA Y 3 . ? 23.306 10.654 -15.419 1.00 51.41 ? 363 BMA B O2 1 HETATM 4354 O O3 . BMA Y 3 . ? 22.151 12.151 -17.435 1.00 56.52 ? 363 BMA B O3 1 HETATM 4355 O O4 . BMA Y 3 . ? 24.242 12.025 -19.386 1.00 48.33 ? 363 BMA B O4 1 HETATM 4356 O O5 . BMA Y 3 . ? 25.236 9.432 -17.007 1.00 52.09 ? 363 BMA B O5 1 HETATM 4357 O O6 . BMA Y 3 . ? 27.627 10.543 -17.117 1.00 49.26 ? 363 BMA B O6 1 HETATM 4358 ZN ZN . ZN Z 5 . ? 0.540 -12.012 -19.071 1.00 22.52 ? 431 ZN B ZN 1 HETATM 4359 ZN ZN . ZN AA 5 . ? 0.968 -6.619 -20.861 1.00 20.02 ? 432 ZN B ZN 1 HETATM 4360 ZN ZN . ZN BA 5 . ? 3.657 -10.432 -19.206 1.00 17.63 ? 433 ZN B ZN 1 HETATM 4361 O O . HOH CA 6 . ? -8.893 8.525 21.142 1.00 14.71 ? 2001 HOH A O 1 HETATM 4362 O O . HOH CA 6 . ? -8.559 10.902 20.260 1.00 8.77 ? 2002 HOH A O 1 HETATM 4363 O O . HOH CA 6 . ? -7.878 8.835 23.813 1.00 23.44 ? 2003 HOH A O 1 HETATM 4364 O O . HOH CA 6 . ? -1.147 7.843 22.950 1.00 11.93 ? 2004 HOH A O 1 HETATM 4365 O O . HOH CA 6 . ? -3.955 10.913 26.765 1.00 35.16 ? 2005 HOH A O 1 HETATM 4366 O O . HOH CA 6 . ? -1.069 15.589 22.301 1.00 39.58 ? 2006 HOH A O 1 HETATM 4367 O O . HOH CA 6 . ? 3.662 20.660 24.270 1.00 39.12 ? 2007 HOH A O 1 HETATM 4368 O O . HOH CA 6 . ? -2.492 8.461 26.956 1.00 37.97 ? 2008 HOH A O 1 HETATM 4369 O O . HOH CA 6 . ? -2.675 14.010 15.299 1.00 13.17 ? 2009 HOH A O 1 HETATM 4370 O O . HOH CA 6 . ? -0.382 16.871 20.025 1.00 29.15 ? 2010 HOH A O 1 HETATM 4371 O O . HOH CA 6 . ? 4.799 18.945 22.249 1.00 47.70 ? 2011 HOH A O 1 HETATM 4372 O O . HOH CA 6 . ? 2.349 17.854 23.545 1.00 51.55 ? 2012 HOH A O 1 HETATM 4373 O O . HOH CA 6 . ? 5.116 15.767 26.395 1.00 44.03 ? 2013 HOH A O 1 HETATM 4374 O O . HOH CA 6 . ? 10.864 21.100 1.625 1.00 28.98 ? 2014 HOH A O 1 HETATM 4375 O O . HOH CA 6 . ? -0.843 30.724 -0.283 1.00 42.30 ? 2015 HOH A O 1 HETATM 4376 O O . HOH CA 6 . ? 11.869 24.473 11.883 1.00 36.69 ? 2016 HOH A O 1 HETATM 4377 O O . HOH CA 6 . ? 4.770 19.867 16.241 1.00 31.67 ? 2017 HOH A O 1 HETATM 4378 O O . HOH CA 6 . ? 8.288 19.179 22.609 1.00 31.23 ? 2018 HOH A O 1 HETATM 4379 O O . HOH CA 6 . ? 2.220 23.595 25.378 1.00 37.98 ? 2019 HOH A O 1 HETATM 4380 O O . HOH CA 6 . ? 5.318 24.983 10.941 1.00 30.30 ? 2020 HOH A O 1 HETATM 4381 O O . HOH CA 6 . ? 9.214 21.268 13.889 1.00 41.69 ? 2021 HOH A O 1 HETATM 4382 O O . HOH CA 6 . ? 11.690 22.141 10.059 1.00 38.62 ? 2022 HOH A O 1 HETATM 4383 O O . HOH CA 6 . ? 10.807 16.625 5.229 1.00 30.74 ? 2023 HOH A O 1 HETATM 4384 O O . HOH CA 6 . ? 13.567 18.901 10.611 1.00 34.38 ? 2024 HOH A O 1 HETATM 4385 O O . HOH CA 6 . ? 5.101 13.936 4.302 1.00 20.19 ? 2025 HOH A O 1 HETATM 4386 O O . HOH CA 6 . ? 11.173 11.307 3.368 1.00 30.90 ? 2026 HOH A O 1 HETATM 4387 O O . HOH CA 6 . ? -13.314 8.644 19.594 1.00 31.28 ? 2027 HOH A O 1 HETATM 4388 O O . HOH CA 6 . ? 11.231 21.051 5.874 1.00 30.48 ? 2028 HOH A O 1 HETATM 4389 O O . HOH CA 6 . ? -20.344 26.802 20.010 1.00 30.79 ? 2029 HOH A O 1 HETATM 4390 O O . HOH CA 6 . ? 7.162 25.751 0.163 1.00 30.23 ? 2030 HOH A O 1 HETATM 4391 O O . HOH CA 6 . ? 10.760 23.673 1.840 1.00 25.97 ? 2031 HOH A O 1 HETATM 4392 O O . HOH CA 6 . ? 12.389 24.525 3.668 1.00 28.74 ? 2032 HOH A O 1 HETATM 4393 O O . HOH CA 6 . ? -24.912 12.591 18.120 1.00 40.55 ? 2033 HOH A O 1 HETATM 4394 O O . HOH CA 6 . ? 8.883 32.959 4.314 1.00 41.18 ? 2034 HOH A O 1 HETATM 4395 O O . HOH CA 6 . ? 2.306 30.598 3.872 1.00 30.37 ? 2035 HOH A O 1 HETATM 4396 O O . HOH CA 6 . ? -0.085 29.200 1.761 1.00 35.20 ? 2036 HOH A O 1 HETATM 4397 O O . HOH CA 6 . ? -23.766 -2.899 13.505 1.00 28.75 ? 2037 HOH A O 1 HETATM 4398 O O . HOH CA 6 . ? 1.496 32.463 5.482 1.00 37.34 ? 2038 HOH A O 1 HETATM 4399 O O . HOH CA 6 . ? 0.266 32.930 15.105 1.00 41.31 ? 2039 HOH A O 1 HETATM 4400 O O . HOH CA 6 . ? 2.875 30.129 16.418 1.00 35.71 ? 2040 HOH A O 1 HETATM 4401 O O . HOH CA 6 . ? 8.079 24.733 11.295 1.00 25.91 ? 2041 HOH A O 1 HETATM 4402 O O . HOH CA 6 . ? 13.438 28.503 11.085 1.00 39.61 ? 2042 HOH A O 1 HETATM 4403 O O . HOH CA 6 . ? -19.398 17.197 5.094 1.00 40.04 ? 2043 HOH A O 1 HETATM 4404 O O . HOH CA 6 . ? -2.155 34.362 19.339 1.00 39.85 ? 2044 HOH A O 1 HETATM 4405 O O . HOH CA 6 . ? -1.223 26.995 23.085 1.00 40.63 ? 2045 HOH A O 1 HETATM 4406 O O . HOH CA 6 . ? 3.088 29.098 26.574 1.00 30.71 ? 2046 HOH A O 1 HETATM 4407 O O . HOH CA 6 . ? -4.066 30.961 22.796 1.00 39.02 ? 2047 HOH A O 1 HETATM 4408 O O . HOH CA 6 . ? -19.513 20.640 1.691 1.00 46.58 ? 2048 HOH A O 1 HETATM 4409 O O . HOH CA 6 . ? 10.625 30.986 24.316 1.00 35.00 ? 2049 HOH A O 1 HETATM 4410 O O . HOH CA 6 . ? 7.369 20.078 17.336 1.00 29.36 ? 2050 HOH A O 1 HETATM 4411 O O . HOH CA 6 . ? 5.558 22.030 23.745 1.00 52.68 ? 2051 HOH A O 1 HETATM 4412 O O . HOH CA 6 . ? -2.650 19.716 22.941 1.00 23.03 ? 2052 HOH A O 1 HETATM 4413 O O . HOH CA 6 . ? -1.081 20.105 25.094 1.00 40.72 ? 2053 HOH A O 1 HETATM 4414 O O . HOH CA 6 . ? -2.918 23.353 25.638 1.00 48.38 ? 2054 HOH A O 1 HETATM 4415 O O . HOH CA 6 . ? -6.623 19.290 17.889 1.00 17.97 ? 2055 HOH A O 1 HETATM 4416 O O . HOH CA 6 . ? -10.258 26.491 22.971 1.00 34.15 ? 2056 HOH A O 1 HETATM 4417 O O . HOH CA 6 . ? -13.759 17.521 18.743 1.00 15.17 ? 2057 HOH A O 1 HETATM 4418 O O . HOH CA 6 . ? -11.548 10.553 20.141 1.00 11.77 ? 2058 HOH A O 1 HETATM 4419 O O . HOH CA 6 . ? -19.498 -7.273 21.090 1.00 25.81 ? 2059 HOH A O 1 HETATM 4420 O O . HOH CA 6 . ? -20.685 14.849 22.634 1.00 36.64 ? 2060 HOH A O 1 HETATM 4421 O O . HOH CA 6 . ? -15.485 10.594 20.081 1.00 30.26 ? 2061 HOH A O 1 HETATM 4422 O O . HOH CA 6 . ? -15.818 10.399 23.080 1.00 41.12 ? 2062 HOH A O 1 HETATM 4423 O O . HOH CA 6 . ? -20.306 0.927 26.627 1.00 25.50 ? 2063 HOH A O 1 HETATM 4424 O O . HOH CA 6 . ? -22.665 19.726 24.881 1.00 20.66 ? 2064 HOH A O 1 HETATM 4425 O O . HOH CA 6 . ? -19.704 26.057 22.623 1.00 26.33 ? 2065 HOH A O 1 HETATM 4426 O O . HOH CA 6 . ? -13.733 29.616 26.039 1.00 35.92 ? 2066 HOH A O 1 HETATM 4427 O O . HOH CA 6 . ? -21.742 -6.560 30.043 1.00 39.29 ? 2067 HOH A O 1 HETATM 4428 O O . HOH CA 6 . ? -21.923 -3.375 26.575 1.00 42.17 ? 2068 HOH A O 1 HETATM 4429 O O . HOH CA 6 . ? -22.208 -9.153 26.688 1.00 36.38 ? 2069 HOH A O 1 HETATM 4430 O O . HOH CA 6 . ? -16.567 26.769 16.405 1.00 42.61 ? 2070 HOH A O 1 HETATM 4431 O O . HOH CA 6 . ? -14.132 29.246 18.283 1.00 69.27 ? 2071 HOH A O 1 HETATM 4432 O O . HOH CA 6 . ? -15.972 28.869 20.498 1.00 38.45 ? 2072 HOH A O 1 HETATM 4433 O O . HOH CA 6 . ? -12.671 -8.887 41.210 1.00 40.45 ? 2073 HOH A O 1 HETATM 4434 O O . HOH CA 6 . ? -24.081 16.812 15.298 1.00 23.07 ? 2074 HOH A O 1 HETATM 4435 O O . HOH CA 6 . ? -20.820 25.551 17.778 1.00 18.98 ? 2075 HOH A O 1 HETATM 4436 O O . HOH CA 6 . ? -16.197 5.601 19.532 1.00 39.48 ? 2076 HOH A O 1 HETATM 4437 O O . HOH CA 6 . ? -22.879 13.195 19.503 1.00 37.55 ? 2077 HOH A O 1 HETATM 4438 O O . HOH CA 6 . ? -20.309 10.761 18.591 1.00 31.69 ? 2078 HOH A O 1 HETATM 4439 O O . HOH CA 6 . ? -19.073 8.682 12.734 1.00 17.97 ? 2079 HOH A O 1 HETATM 4440 O O . HOH CA 6 . ? 16.230 5.516 22.540 1.00 33.11 ? 2080 HOH A O 1 HETATM 4441 O O . HOH CA 6 . ? -21.387 8.241 14.815 1.00 29.17 ? 2081 HOH A O 1 HETATM 4442 O O . HOH CA 6 . ? -14.863 2.674 15.739 1.00 33.17 ? 2082 HOH A O 1 HETATM 4443 O O . HOH CA 6 . ? -19.318 6.340 11.715 1.00 26.07 ? 2083 HOH A O 1 HETATM 4444 O O . HOH CA 6 . ? -21.947 0.894 11.644 1.00 33.08 ? 2084 HOH A O 1 HETATM 4445 O O . HOH CA 6 . ? -21.559 4.163 10.541 1.00 28.82 ? 2085 HOH A O 1 HETATM 4446 O O . HOH CA 6 . ? 17.460 8.537 19.554 1.00 20.99 ? 2086 HOH A O 1 HETATM 4447 O O . HOH CA 6 . ? -20.976 -3.303 14.055 1.00 28.20 ? 2087 HOH A O 1 HETATM 4448 O O . HOH CA 6 . ? -24.686 -5.998 14.015 1.00 43.51 ? 2088 HOH A O 1 HETATM 4449 O O . HOH CA 6 . ? -9.652 -4.976 4.906 1.00 40.28 ? 2089 HOH A O 1 HETATM 4450 O O . HOH CA 6 . ? 0.726 -0.908 4.138 1.00 45.26 ? 2090 HOH A O 1 HETATM 4451 O O . HOH CA 6 . ? -13.900 3.427 0.350 1.00 27.46 ? 2091 HOH A O 1 HETATM 4452 O O . HOH CA 6 . ? -15.449 4.908 0.608 1.00 32.86 ? 2092 HOH A O 1 HETATM 4453 O O . HOH CA 6 . ? -16.473 11.795 -0.487 1.00 38.37 ? 2093 HOH A O 1 HETATM 4454 O O . HOH CA 6 . ? -2.127 19.646 -5.886 1.00 38.96 ? 2094 HOH A O 1 HETATM 4455 O O . HOH CA 6 . ? -22.212 1.151 8.734 1.00 35.54 ? 2095 HOH A O 1 HETATM 4456 O O . HOH CA 6 . ? -22.921 -3.762 2.828 1.00 30.22 ? 2096 HOH A O 1 HETATM 4457 O O . HOH CA 6 . ? -3.081 2.799 -1.312 1.00 34.11 ? 2097 HOH A O 1 HETATM 4458 O O . HOH CA 6 . ? -6.936 -13.021 34.687 1.00 48.72 ? 2098 HOH A O 1 HETATM 4459 O O . HOH CA 6 . ? -23.394 10.441 17.016 1.00 30.77 ? 2099 HOH A O 1 HETATM 4460 O O . HOH CA 6 . ? -28.401 5.685 16.276 1.00 34.53 ? 2100 HOH A O 1 HETATM 4461 O O . HOH CA 6 . ? 6.430 -3.376 9.863 1.00 37.72 ? 2101 HOH A O 1 HETATM 4462 O O . HOH CA 6 . ? -3.126 -17.437 16.552 1.00 54.61 ? 2102 HOH A O 1 HETATM 4463 O O . HOH CA 6 . ? -21.496 16.331 6.482 1.00 36.58 ? 2103 HOH A O 1 HETATM 4464 O O . HOH CA 6 . ? -23.519 16.617 3.259 1.00 41.55 ? 2104 HOH A O 1 HETATM 4465 O O . HOH CA 6 . ? 1.578 16.420 -4.234 1.00 44.22 ? 2105 HOH A O 1 HETATM 4466 O O . HOH CA 6 . ? -13.099 13.489 -2.511 1.00 42.62 ? 2106 HOH A O 1 HETATM 4467 O O . HOH CA 6 . ? -10.237 9.310 -0.127 1.00 40.33 ? 2107 HOH A O 1 HETATM 4468 O O . HOH CA 6 . ? -16.883 20.971 3.259 1.00 32.99 ? 2108 HOH A O 1 HETATM 4469 O O . HOH CA 6 . ? -13.406 26.158 1.163 1.00 59.98 ? 2109 HOH A O 1 HETATM 4470 O O . HOH CA 6 . ? -13.038 25.413 11.485 1.00 28.24 ? 2110 HOH A O 1 HETATM 4471 O O . HOH CA 6 . ? -14.696 27.473 2.938 1.00 38.59 ? 2111 HOH A O 1 HETATM 4472 O O . HOH CA 6 . ? -3.806 31.442 -2.187 1.00 35.66 ? 2112 HOH A O 1 HETATM 4473 O O . HOH CA 6 . ? -11.498 34.711 -3.709 1.00 33.58 ? 2113 HOH A O 1 HETATM 4474 O O . HOH CA 6 . ? -23.187 27.223 8.889 1.00 30.71 ? 2114 HOH A O 1 HETATM 4475 O O . HOH CA 6 . ? -19.678 28.805 6.471 1.00 49.14 ? 2115 HOH A O 1 HETATM 4476 O O . HOH CA 6 . ? -34.419 20.450 16.190 1.00 38.91 ? 2116 HOH A O 1 HETATM 4477 O O . HOH CA 6 . ? -33.454 22.380 14.212 1.00 40.59 ? 2117 HOH A O 1 HETATM 4478 O O . HOH CA 6 . ? -20.636 33.371 16.972 1.00 54.76 ? 2118 HOH A O 1 HETATM 4479 O O . HOH CA 6 . ? -12.856 33.011 12.760 1.00 40.69 ? 2119 HOH A O 1 HETATM 4480 O O . HOH CA 6 . ? -30.033 31.282 20.483 1.00 46.69 ? 2120 HOH A O 1 HETATM 4481 O O . HOH CA 6 . ? -15.213 28.129 12.445 1.00 23.62 ? 2121 HOH A O 1 HETATM 4482 O O . HOH CA 6 . ? -14.303 30.984 16.154 1.00 34.15 ? 2122 HOH A O 1 HETATM 4483 O O . HOH CA 6 . ? -14.634 25.506 13.315 1.00 27.62 ? 2123 HOH A O 1 HETATM 4484 O O . HOH CA 6 . ? -5.105 28.307 28.382 1.00 43.64 ? 2124 HOH A O 1 HETATM 4485 O O . HOH CA 6 . ? -7.375 24.615 28.562 1.00 36.16 ? 2125 HOH A O 1 HETATM 4486 O O . HOH CA 6 . ? -7.234 3.443 11.326 1.00 16.42 ? 2126 HOH A O 1 HETATM 4487 O O . HOH CA 6 . ? 16.239 -2.841 19.524 1.00 40.84 ? 2127 HOH A O 1 HETATM 4488 O O . HOH CA 6 . ? 17.838 -10.357 15.596 1.00 35.46 ? 2128 HOH A O 1 HETATM 4489 O O . HOH CA 6 . ? 11.488 -12.890 15.719 1.00 41.47 ? 2129 HOH A O 1 HETATM 4490 O O . HOH CA 6 . ? 11.031 -10.470 13.738 1.00 37.75 ? 2130 HOH A O 1 HETATM 4491 O O . HOH CA 6 . ? 13.400 -11.651 20.795 1.00 38.64 ? 2131 HOH A O 1 HETATM 4492 O O . HOH CA 6 . ? -11.193 7.551 21.482 1.00 17.76 ? 2132 HOH A O 1 HETATM 4493 O O . HOH CA 6 . ? -23.745 -2.072 16.906 1.00 38.74 ? 2133 HOH A O 1 HETATM 4494 O O . HOH CA 6 . ? -18.597 -6.868 18.551 1.00 23.11 ? 2134 HOH A O 1 HETATM 4495 O O . HOH CA 6 . ? -22.590 -7.471 21.440 1.00 39.42 ? 2135 HOH A O 1 HETATM 4496 O O . HOH CA 6 . ? -22.293 3.862 25.013 1.00 36.62 ? 2136 HOH A O 1 HETATM 4497 O O . HOH CA 6 . ? -25.817 0.774 23.010 1.00 50.13 ? 2137 HOH A O 1 HETATM 4498 O O . HOH CA 6 . ? -17.048 3.752 24.870 1.00 37.51 ? 2138 HOH A O 1 HETATM 4499 O O . HOH CA 6 . ? -11.165 4.545 26.544 1.00 28.03 ? 2139 HOH A O 1 HETATM 4500 O O . HOH CA 6 . ? -17.780 -5.924 23.841 1.00 35.76 ? 2140 HOH A O 1 HETATM 4501 O O . HOH CA 6 . ? -16.754 -6.089 28.444 1.00 42.77 ? 2141 HOH A O 1 HETATM 4502 O O . HOH CA 6 . ? -19.449 -5.993 27.393 1.00 42.99 ? 2142 HOH A O 1 HETATM 4503 O O . HOH CA 6 . ? -20.898 -4.060 23.958 1.00 48.33 ? 2143 HOH A O 1 HETATM 4504 O O . HOH CA 6 . ? -13.990 -4.037 33.168 1.00 50.41 ? 2144 HOH A O 1 HETATM 4505 O O . HOH CA 6 . ? -2.911 -9.670 34.364 1.00 32.78 ? 2145 HOH A O 1 HETATM 4506 O O . HOH CA 6 . ? -1.568 6.601 33.811 1.00 31.84 ? 2146 HOH A O 1 HETATM 4507 O O . HOH CA 6 . ? -12.905 -6.663 38.593 1.00 37.71 ? 2147 HOH A O 1 HETATM 4508 O O . HOH CA 6 . ? -9.575 1.289 29.697 1.00 30.22 ? 2148 HOH A O 1 HETATM 4509 O O . HOH CA 6 . ? -13.544 6.115 20.073 1.00 39.75 ? 2149 HOH A O 1 HETATM 4510 O O . HOH CA 6 . ? -1.218 2.621 22.202 1.00 16.17 ? 2150 HOH A O 1 HETATM 4511 O O . HOH CA 6 . ? -6.441 7.235 25.511 1.00 24.46 ? 2151 HOH A O 1 HETATM 4512 O O . HOH CA 6 . ? 5.144 5.765 29.417 1.00 33.78 ? 2152 HOH A O 1 HETATM 4513 O O . HOH CA 6 . ? 5.221 11.362 27.436 1.00 38.56 ? 2153 HOH A O 1 HETATM 4514 O O . HOH CA 6 . ? 6.875 -2.356 31.624 1.00 27.51 ? 2154 HOH A O 1 HETATM 4515 O O . HOH CA 6 . ? 16.352 2.622 22.428 1.00 28.57 ? 2155 HOH A O 1 HETATM 4516 O O . HOH CA 6 . ? 15.522 2.129 24.973 1.00 38.94 ? 2156 HOH A O 1 HETATM 4517 O O . HOH CA 6 . ? 10.599 -0.290 19.205 1.00 45.77 ? 2157 HOH A O 1 HETATM 4518 O O . HOH CA 6 . ? 19.418 2.807 25.259 1.00 37.92 ? 2158 HOH A O 1 HETATM 4519 O O . HOH CA 6 . ? 15.692 6.361 18.666 1.00 29.82 ? 2159 HOH A O 1 HETATM 4520 O O . HOH CA 6 . ? 14.535 6.389 21.054 1.00 18.02 ? 2160 HOH A O 1 HETATM 4521 O O . HOH CA 6 . ? 17.052 10.569 19.459 1.00 13.80 ? 2161 HOH A O 1 HETATM 4522 O O . HOH CA 6 . ? 12.785 11.199 8.658 1.00 33.47 ? 2162 HOH A O 1 HETATM 4523 O O . HOH CA 6 . ? 22.069 5.603 12.568 1.00 23.23 ? 2163 HOH A O 1 HETATM 4524 O O . HOH CA 6 . ? 17.315 1.517 13.974 1.00 38.65 ? 2164 HOH A O 1 HETATM 4525 O O . HOH CA 6 . ? 11.481 8.692 2.812 1.00 30.03 ? 2165 HOH A O 1 HETATM 4526 O O . HOH CA 6 . ? 14.176 3.624 3.150 1.00 29.43 ? 2166 HOH A O 1 HETATM 4527 O O . HOH CA 6 . ? 5.926 0.585 9.017 1.00 31.41 ? 2167 HOH A O 1 HETATM 4528 O O . HOH CA 6 . ? 10.939 -2.253 9.139 1.00 30.18 ? 2168 HOH A O 1 HETATM 4529 O O . HOH CA 6 . ? 10.339 8.524 0.421 1.00 40.45 ? 2169 HOH A O 1 HETATM 4530 O O . HOH CA 6 . ? 6.350 2.785 -4.230 1.00 27.03 ? 2170 HOH A O 1 HETATM 4531 O O . HOH CA 6 . ? 7.981 5.183 -4.124 1.00 62.36 ? 2171 HOH A O 1 HETATM 4532 O O . HOH CA 6 . ? 12.988 -0.205 -3.626 1.00 37.53 ? 2172 HOH A O 1 HETATM 4533 O O . HOH CA 6 . ? 14.195 1.693 -5.099 1.00 47.92 ? 2173 HOH A O 1 HETATM 4534 O O . HOH CA 6 . ? 2.864 1.262 2.778 1.00 42.18 ? 2174 HOH A O 1 HETATM 4535 O O . HOH CA 6 . ? 6.411 -2.140 5.916 1.00 48.89 ? 2175 HOH A O 1 HETATM 4536 O O . HOH CA 6 . ? -1.515 6.390 0.368 1.00 28.95 ? 2176 HOH A O 1 HETATM 4537 O O . HOH CA 6 . ? 7.068 -1.397 -1.102 1.00 21.42 ? 2177 HOH A O 1 HETATM 4538 O O . HOH CA 6 . ? -2.383 9.928 0.823 1.00 36.65 ? 2178 HOH A O 1 HETATM 4539 O O . HOH CA 6 . ? 5.926 11.823 -2.500 1.00 32.29 ? 2179 HOH A O 1 HETATM 4540 O O . HOH CA 6 . ? 8.402 11.643 -0.172 1.00 29.05 ? 2180 HOH A O 1 HETATM 4541 O O . HOH CA 6 . ? 1.783 12.689 -4.714 1.00 46.81 ? 2181 HOH A O 1 HETATM 4542 O O . HOH CA 6 . ? -4.957 8.370 -4.531 1.00 39.16 ? 2182 HOH A O 1 HETATM 4543 O O . HOH CA 6 . ? -5.063 21.619 -3.669 1.00 45.10 ? 2183 HOH A O 1 HETATM 4544 O O . HOH CA 6 . ? -11.211 3.743 0.148 1.00 33.42 ? 2184 HOH A O 1 HETATM 4545 O O . HOH CA 6 . ? -10.654 -2.370 4.009 1.00 24.64 ? 2185 HOH A O 1 HETATM 4546 O O . HOH CA 6 . ? -3.835 -2.226 7.146 1.00 28.32 ? 2186 HOH A O 1 HETATM 4547 O O . HOH CA 6 . ? -3.666 1.740 1.052 1.00 17.87 ? 2187 HOH A O 1 HETATM 4548 O O . HOH CA 6 . ? -6.313 -7.931 4.992 1.00 36.15 ? 2188 HOH A O 1 HETATM 4549 O O . HOH CA 6 . ? -6.980 -7.228 1.969 1.00 35.71 ? 2189 HOH A O 1 HETATM 4550 O O . HOH CA 6 . ? -3.181 -4.326 8.716 1.00 28.89 ? 2190 HOH A O 1 HETATM 4551 O O . HOH CA 6 . ? -10.128 -10.264 13.505 1.00 24.68 ? 2191 HOH A O 1 HETATM 4552 O O . HOH CA 6 . ? -4.315 -11.855 20.353 1.00 33.66 ? 2192 HOH A O 1 HETATM 4553 O O . HOH CA 6 . ? -5.526 -12.984 23.412 1.00 32.77 ? 2193 HOH A O 1 HETATM 4554 O O . HOH CA 6 . ? -8.647 -15.093 23.179 1.00 29.06 ? 2194 HOH A O 1 HETATM 4555 O O . HOH CA 6 . ? -13.174 -14.577 20.777 1.00 38.75 ? 2195 HOH A O 1 HETATM 4556 O O . HOH CA 6 . ? -10.830 -14.396 28.690 1.00 33.24 ? 2196 HOH A O 1 HETATM 4557 O O . HOH CA 6 . ? -17.724 -9.581 27.065 1.00 32.72 ? 2197 HOH A O 1 HETATM 4558 O O . HOH CA 6 . ? -10.137 -12.960 33.001 1.00 36.19 ? 2198 HOH A O 1 HETATM 4559 O O . HOH CA 6 . ? -6.839 -12.715 31.876 1.00 42.07 ? 2199 HOH A O 1 HETATM 4560 O O . HOH CA 6 . ? -5.153 -14.378 28.537 1.00 33.29 ? 2200 HOH A O 1 HETATM 4561 O O . HOH CA 6 . ? 0.051 -11.319 25.169 1.00 10.87 ? 2201 HOH A O 1 HETATM 4562 O O . HOH CA 6 . ? 0.984 -9.756 33.311 1.00 20.96 ? 2202 HOH A O 1 HETATM 4563 O O . HOH CA 6 . ? 6.771 -12.513 22.841 1.00 47.61 ? 2203 HOH A O 1 HETATM 4564 O O . HOH CA 6 . ? 8.449 -5.843 17.717 1.00 26.86 ? 2204 HOH A O 1 HETATM 4565 O O . HOH CA 6 . ? 4.246 -8.033 13.921 1.00 29.86 ? 2205 HOH A O 1 HETATM 4566 O O . HOH CA 6 . ? -3.006 -13.177 17.137 1.00 28.99 ? 2206 HOH A O 1 HETATM 4567 O O . HOH CA 6 . ? 6.235 -1.059 11.043 1.00 29.16 ? 2207 HOH A O 1 HETATM 4568 O O . HOH CA 6 . ? 2.528 -3.978 5.671 1.00 36.21 ? 2208 HOH A O 1 HETATM 4569 O O . HOH CA 6 . ? 2.054 16.936 -0.578 1.00 27.78 ? 2209 HOH A O 1 HETATM 4570 O O . HOH CA 6 . ? -4.360 24.581 -2.973 1.00 47.04 ? 2210 HOH A O 1 HETATM 4571 O O . HOH CA 6 . ? 0.685 29.441 -2.572 1.00 48.43 ? 2211 HOH A O 1 HETATM 4572 O O . HOH CA 6 . ? -2.226 29.366 -2.622 1.00 39.41 ? 2212 HOH A O 1 HETATM 4573 O O . HOH CA 6 . ? -21.692 20.260 7.858 1.00 22.60 ? 2213 HOH A O 1 HETATM 4574 O O . HOH CA 6 . ? -19.329 26.400 15.623 1.00 32.52 ? 2214 HOH A O 1 HETATM 4575 O O . HOH CA 6 . ? -22.940 22.279 9.105 1.00 41.07 ? 2215 HOH A O 1 HETATM 4576 O O . HOH CA 6 . ? -32.027 26.395 14.603 1.00 36.03 ? 2216 HOH A O 1 HETATM 4577 O O . HOH CA 6 . ? -32.306 22.633 17.277 1.00 34.95 ? 2217 HOH A O 1 HETATM 4578 O O . HOH CA 6 . ? -24.020 28.830 10.827 1.00 46.91 ? 2218 HOH A O 1 HETATM 4579 O O . HOH CA 6 . ? -24.884 30.949 19.403 1.00 51.34 ? 2219 HOH A O 1 HETATM 4580 O O . HOH CA 6 . ? -21.231 30.681 18.866 1.00 34.75 ? 2220 HOH A O 1 HETATM 4581 O O . HOH CA 6 . ? -26.961 30.204 17.926 1.00 46.57 ? 2221 HOH A O 1 HETATM 4582 O O . HOH CA 6 . ? -7.770 33.691 20.266 1.00 37.46 ? 2222 HOH A O 1 HETATM 4583 O O . HOH CA 6 . ? -7.700 29.466 27.956 1.00 39.84 ? 2223 HOH A O 1 HETATM 4584 O O . HOH CA 6 . ? -12.420 31.621 28.700 1.00 54.65 ? 2224 HOH A O 1 HETATM 4585 O O . HOH CA 6 . ? -9.567 31.661 28.770 1.00 33.45 ? 2225 HOH A O 1 HETATM 4586 O O . HOH CA 6 . ? -10.159 28.905 28.563 1.00 42.79 ? 2226 HOH A O 1 HETATM 4587 O O . HOH CA 6 . ? -6.149 25.491 24.180 1.00 40.61 ? 2227 HOH A O 1 HETATM 4588 O O . HOH CA 6 . ? 14.210 1.585 16.688 1.00 36.65 ? 2228 HOH A O 1 HETATM 4589 O O . HOH CA 6 . ? 8.336 -0.549 12.740 1.00 33.57 ? 2229 HOH A O 1 HETATM 4590 O O . HOH CA 6 . ? 9.277 -2.784 14.367 1.00 31.54 ? 2230 HOH A O 1 HETATM 4591 O O . HOH CA 6 . ? 13.566 -3.112 17.427 1.00 48.70 ? 2231 HOH A O 1 HETATM 4592 O O . HOH CA 6 . ? 15.423 -9.898 17.038 1.00 52.25 ? 2232 HOH A O 1 HETATM 4593 O O . HOH CA 6 . ? 12.673 -10.320 16.740 1.00 48.81 ? 2233 HOH A O 1 HETATM 4594 O O . HOH DA 6 . ? 1.838 -8.461 -21.232 1.00 12.41 ? 2001 HOH B O 1 HETATM 4595 O O . HOH DA 6 . ? 2.742 -9.240 -23.868 1.00 20.45 ? 2002 HOH B O 1 HETATM 4596 O O . HOH DA 6 . ? 9.306 -8.030 -23.035 1.00 17.32 ? 2003 HOH B O 1 HETATM 4597 O O . HOH DA 6 . ? 6.728 -10.633 -26.694 1.00 24.69 ? 2004 HOH B O 1 HETATM 4598 O O . HOH DA 6 . ? 9.470 -15.335 -22.027 1.00 42.11 ? 2005 HOH B O 1 HETATM 4599 O O . HOH DA 6 . ? 9.657 -19.765 -28.541 1.00 31.38 ? 2006 HOH B O 1 HETATM 4600 O O . HOH DA 6 . ? 7.850 -14.079 -15.466 1.00 20.71 ? 2007 HOH B O 1 HETATM 4601 O O . HOH DA 6 . ? 10.152 -16.890 -19.946 1.00 29.86 ? 2008 HOH B O 1 HETATM 4602 O O . HOH DA 6 . ? 13.537 -17.421 -23.558 1.00 36.35 ? 2009 HOH B O 1 HETATM 4603 O O . HOH DA 6 . ? 7.979 -35.712 -14.835 1.00 39.98 ? 2010 HOH B O 1 HETATM 4604 O O . HOH DA 6 . ? 18.747 -19.053 -22.948 1.00 44.49 ? 2011 HOH B O 1 HETATM 4605 O O . HOH DA 6 . ? 18.666 -22.196 -15.700 1.00 35.96 ? 2012 HOH B O 1 HETATM 4606 O O . HOH DA 6 . ? 16.053 -25.090 -10.721 1.00 31.64 ? 2013 HOH B O 1 HETATM 4607 O O . HOH DA 6 . ? 22.612 -15.040 -7.294 1.00 33.17 ? 2014 HOH B O 1 HETATM 4608 O O . HOH DA 6 . ? 17.865 -16.209 -2.990 1.00 35.18 ? 2015 HOH B O 1 HETATM 4609 O O . HOH DA 6 . ? 15.489 -13.525 -4.165 1.00 20.97 ? 2016 HOH B O 1 HETATM 4610 O O . HOH DA 6 . ? 21.705 -11.138 -3.063 1.00 35.09 ? 2017 HOH B O 1 HETATM 4611 O O . HOH DA 6 . ? 20.522 -23.563 -7.394 1.00 37.08 ? 2018 HOH B O 1 HETATM 4612 O O . HOH DA 6 . ? 21.951 -21.400 -5.680 1.00 34.90 ? 2019 HOH B O 1 HETATM 4613 O O . HOH DA 6 . ? -9.630 -26.846 -20.022 1.00 28.67 ? 2020 HOH B O 1 HETATM 4614 O O . HOH DA 6 . ? 24.425 -25.172 -4.449 1.00 45.03 ? 2021 HOH B O 1 HETATM 4615 O O . HOH DA 6 . ? -12.101 -10.830 -20.979 1.00 53.00 ? 2022 HOH B O 1 HETATM 4616 O O . HOH DA 6 . ? 12.521 -29.857 -3.116 1.00 36.13 ? 2023 HOH B O 1 HETATM 4617 O O . HOH DA 6 . ? 17.722 -26.154 2.872 1.00 30.27 ? 2024 HOH B O 1 HETATM 4618 O O . HOH DA 6 . ? 17.626 -34.644 -3.037 1.00 39.95 ? 2025 HOH B O 1 HETATM 4619 O O . HOH DA 6 . ? -13.699 0.599 -7.934 1.00 27.37 ? 2026 HOH B O 1 HETATM 4620 O O . HOH DA 6 . ? 16.349 -27.728 -12.714 1.00 36.62 ? 2027 HOH B O 1 HETATM 4621 O O . HOH DA 6 . ? 11.085 -32.803 -15.120 1.00 36.24 ? 2028 HOH B O 1 HETATM 4622 O O . HOH DA 6 . ? 6.999 -32.426 -14.892 1.00 45.67 ? 2029 HOH B O 1 HETATM 4623 O O . HOH DA 6 . ? -14.316 -13.105 -18.083 1.00 45.17 ? 2030 HOH B O 1 HETATM 4624 O O . HOH DA 6 . ? -11.968 -11.934 3.657 1.00 68.48 ? 2031 HOH B O 1 HETATM 4625 O O . HOH DA 6 . ? -10.388 -9.390 3.799 1.00 47.28 ? 2032 HOH B O 1 HETATM 4626 O O . HOH DA 6 . ? 13.097 -29.807 -17.693 1.00 35.45 ? 2033 HOH B O 1 HETATM 4627 O O . HOH DA 6 . ? 14.417 -38.098 -24.967 1.00 36.07 ? 2034 HOH B O 1 HETATM 4628 O O . HOH DA 6 . ? 9.020 -27.440 -23.093 1.00 46.45 ? 2035 HOH B O 1 HETATM 4629 O O . HOH DA 6 . ? 15.055 -25.340 -23.134 1.00 49.11 ? 2036 HOH B O 1 HETATM 4630 O O . HOH DA 6 . ? 14.513 -21.291 -24.107 1.00 36.54 ? 2037 HOH B O 1 HETATM 4631 O O . HOH DA 6 . ? 8.045 -19.069 -22.702 1.00 35.68 ? 2038 HOH B O 1 HETATM 4632 O O . HOH DA 6 . ? 3.986 -19.103 -17.793 1.00 17.86 ? 2039 HOH B O 1 HETATM 4633 O O . HOH DA 6 . ? 0.606 -26.407 -22.968 1.00 32.14 ? 2040 HOH B O 1 HETATM 4634 O O . HOH DA 6 . ? -3.163 -17.578 -18.845 1.00 17.22 ? 2041 HOH B O 1 HETATM 4635 O O . HOH DA 6 . ? -3.690 -16.915 -25.080 1.00 23.39 ? 2042 HOH B O 1 HETATM 4636 O O . HOH DA 6 . ? -0.932 -10.758 -20.045 1.00 11.27 ? 2043 HOH B O 1 HETATM 4637 O O . HOH DA 6 . ? 3.282 -11.847 -24.302 1.00 40.65 ? 2044 HOH B O 1 HETATM 4638 O O . HOH DA 6 . ? 7.005 -23.502 -27.106 1.00 46.78 ? 2045 HOH B O 1 HETATM 4639 O O . HOH DA 6 . ? 4.086 -25.804 -24.681 1.00 39.58 ? 2046 HOH B O 1 HETATM 4640 O O . HOH DA 6 . ? -4.451 -6.087 -19.692 1.00 32.99 ? 2047 HOH B O 1 HETATM 4641 O O . HOH DA 6 . ? -15.282 -0.045 -16.160 1.00 41.28 ? 2048 HOH B O 1 HETATM 4642 O O . HOH DA 6 . ? -14.579 3.096 -18.765 1.00 38.03 ? 2049 HOH B O 1 HETATM 4643 O O . HOH DA 6 . ? -9.228 7.149 -21.585 1.00 31.94 ? 2050 HOH B O 1 HETATM 4644 O O . HOH DA 6 . ? -7.950 9.631 -17.191 1.00 48.75 ? 2051 HOH B O 1 HETATM 4645 O O . HOH DA 6 . ? -4.356 -10.179 -23.892 1.00 50.54 ? 2052 HOH B O 1 HETATM 4646 O O . HOH DA 6 . ? -5.000 -11.136 -20.059 1.00 35.91 ? 2053 HOH B O 1 HETATM 4647 O O . HOH DA 6 . ? -3.167 -9.612 -20.040 1.00 37.14 ? 2054 HOH B O 1 HETATM 4648 O O . HOH DA 6 . ? -10.187 -1.029 -26.156 1.00 38.23 ? 2055 HOH B O 1 HETATM 4649 O O . HOH DA 6 . ? -9.305 -3.778 -27.012 1.00 44.78 ? 2056 HOH B O 1 HETATM 4650 O O . HOH DA 6 . ? -16.207 -0.399 -22.640 1.00 36.97 ? 2057 HOH B O 1 HETATM 4651 O O . HOH DA 6 . ? -14.407 -0.802 -27.143 1.00 35.50 ? 2058 HOH B O 1 HETATM 4652 O O . HOH DA 6 . ? -12.197 -19.559 -24.789 1.00 25.32 ? 2059 HOH B O 1 HETATM 4653 O O . HOH DA 6 . ? -9.222 -25.983 -22.526 1.00 22.83 ? 2060 HOH B O 1 HETATM 4654 O O . HOH DA 6 . ? -4.245 -23.753 -27.997 1.00 38.09 ? 2061 HOH B O 1 HETATM 4655 O O . HOH DA 6 . ? -9.313 6.297 -27.198 1.00 44.16 ? 2062 HOH B O 1 HETATM 4656 O O . HOH DA 6 . ? -5.863 -27.525 -15.972 1.00 35.00 ? 2063 HOH B O 1 HETATM 4657 O O . HOH DA 6 . ? -1.592 9.397 -41.012 1.00 38.87 ? 2064 HOH B O 1 HETATM 4658 O O . HOH DA 6 . ? -9.979 -25.580 -17.843 1.00 24.56 ? 2065 HOH B O 1 HETATM 4659 O O . HOH DA 6 . ? -13.680 -17.187 -15.254 1.00 35.50 ? 2066 HOH B O 1 HETATM 4660 O O . HOH DA 6 . ? -9.634 -10.495 -18.647 1.00 26.53 ? 2067 HOH B O 1 HETATM 4661 O O . HOH DA 6 . ? -8.795 -8.793 -12.816 1.00 19.55 ? 2068 HOH B O 1 HETATM 4662 O O . HOH DA 6 . ? 26.665 1.273 -26.006 1.00 46.57 ? 2069 HOH B O 1 HETATM 4663 O O . HOH DA 6 . ? -10.766 -8.089 -14.766 1.00 29.53 ? 2070 HOH B O 1 HETATM 4664 O O . HOH DA 6 . ? 26.054 -0.755 -14.561 1.00 35.88 ? 2071 HOH B O 1 HETATM 4665 O O . HOH DA 6 . ? -6.909 -5.579 -20.288 1.00 34.06 ? 2072 HOH B O 1 HETATM 4666 O O . HOH DA 6 . ? -8.850 -6.531 -11.817 1.00 20.19 ? 2073 HOH B O 1 HETATM 4667 O O . HOH DA 6 . ? -10.883 -4.208 -10.647 1.00 22.66 ? 2074 HOH B O 1 HETATM 4668 O O . HOH DA 6 . ? -11.570 -0.616 -11.659 1.00 32.78 ? 2075 HOH B O 1 HETATM 4669 O O . HOH DA 6 . ? 28.478 -5.751 -22.338 1.00 30.51 ? 2076 HOH B O 1 HETATM 4670 O O . HOH DA 6 . ? -10.484 3.315 -14.082 1.00 28.40 ? 2077 HOH B O 1 HETATM 4671 O O . HOH DA 6 . ? -12.067 6.379 -11.703 1.00 35.49 ? 2078 HOH B O 1 HETATM 4672 O O . HOH DA 6 . ? -0.193 5.120 -4.033 1.00 30.34 ? 2079 HOH B O 1 HETATM 4673 O O . HOH DA 6 . ? -3.142 -2.616 -0.530 1.00 33.07 ? 2080 HOH B O 1 HETATM 4674 O O . HOH DA 6 . ? -6.609 -1.217 2.245 1.00 31.47 ? 2081 HOH B O 1 HETATM 4675 O O . HOH DA 6 . ? -4.879 -4.771 -0.707 1.00 31.26 ? 2082 HOH B O 1 HETATM 4676 O O . HOH DA 6 . ? -8.048 -4.571 1.053 1.00 33.11 ? 2083 HOH B O 1 HETATM 4677 O O . HOH DA 6 . ? -11.818 -1.320 -8.889 1.00 27.66 ? 2084 HOH B O 1 HETATM 4678 O O . HOH DA 6 . ? -11.297 8.595 -27.201 1.00 42.40 ? 2085 HOH B O 1 HETATM 4679 O O . HOH DA 6 . ? -10.896 9.993 -22.000 1.00 38.82 ? 2086 HOH B O 1 HETATM 4680 O O . HOH DA 6 . ? -13.263 -10.835 -16.976 1.00 39.40 ? 2087 HOH B O 1 HETATM 4681 O O . HOH DA 6 . ? 7.929 15.904 -29.769 1.00 40.23 ? 2088 HOH B O 1 HETATM 4682 O O . HOH DA 6 . ? -10.627 -16.409 -6.310 1.00 27.03 ? 2089 HOH B O 1 HETATM 4683 O O . HOH DA 6 . ? -12.401 -10.096 1.866 1.00 48.73 ? 2090 HOH B O 1 HETATM 4684 O O . HOH DA 6 . ? -13.574 -16.382 -3.460 1.00 36.97 ? 2091 HOH B O 1 HETATM 4685 O O . HOH DA 6 . ? -7.218 -16.363 -4.888 1.00 36.15 ? 2092 HOH B O 1 HETATM 4686 O O . HOH DA 6 . ? -0.862 -17.531 -0.523 1.00 40.37 ? 2093 HOH B O 1 HETATM 4687 O O . HOH DA 6 . ? -5.502 -10.952 0.092 1.00 46.40 ? 2094 HOH B O 1 HETATM 4688 O O . HOH DA 6 . ? 0.138 -9.362 -0.106 1.00 26.60 ? 2095 HOH B O 1 HETATM 4689 O O . HOH DA 6 . ? -6.465 -21.054 -2.936 1.00 37.39 ? 2096 HOH B O 1 HETATM 4690 O O . HOH DA 6 . ? -2.465 -28.620 -4.751 1.00 45.71 ? 2097 HOH B O 1 HETATM 4691 O O . HOH DA 6 . ? -2.294 -25.358 -11.150 1.00 29.42 ? 2098 HOH B O 1 HETATM 4692 O O . HOH DA 6 . ? 5.946 -27.002 -0.938 1.00 23.33 ? 2099 HOH B O 1 HETATM 4693 O O . HOH DA 6 . ? -3.970 -27.328 -3.230 1.00 31.61 ? 2100 HOH B O 1 HETATM 4694 O O . HOH DA 6 . ? -12.545 -27.488 -9.180 1.00 36.34 ? 2101 HOH B O 1 HETATM 4695 O O . HOH DA 6 . ? -23.055 -24.811 -12.088 1.00 35.97 ? 2102 HOH B O 1 HETATM 4696 O O . HOH DA 6 . ? -13.933 -20.968 -5.291 1.00 37.70 ? 2103 HOH B O 1 HETATM 4697 O O . HOH DA 6 . ? -16.911 -23.946 -11.114 1.00 39.86 ? 2104 HOH B O 1 HETATM 4698 O O . HOH DA 6 . ? -16.174 -29.291 -10.507 1.00 40.78 ? 2105 HOH B O 1 HETATM 4699 O O . HOH DA 6 . ? -12.964 -32.169 -9.903 1.00 28.24 ? 2106 HOH B O 1 HETATM 4700 O O . HOH DA 6 . ? -7.685 -32.041 -17.616 1.00 41.86 ? 2107 HOH B O 1 HETATM 4701 O O . HOH DA 6 . ? -0.509 -33.262 -11.904 1.00 31.02 ? 2108 HOH B O 1 HETATM 4702 O O . HOH DA 6 . ? -4.567 -28.391 -12.582 1.00 28.67 ? 2109 HOH B O 1 HETATM 4703 O O . HOH DA 6 . ? -3.903 -30.941 -16.067 1.00 31.13 ? 2110 HOH B O 1 HETATM 4704 O O . HOH DA 6 . ? 5.205 -32.853 -11.309 1.00 44.48 ? 2111 HOH B O 1 HETATM 4705 O O . HOH DA 6 . ? -4.259 -25.338 -13.291 1.00 23.84 ? 2112 HOH B O 1 HETATM 4706 O O . HOH DA 6 . ? 3.795 -25.593 -31.060 1.00 40.75 ? 2113 HOH B O 1 HETATM 4707 O O . HOH DA 6 . ? 8.461 -26.453 -30.387 1.00 41.92 ? 2114 HOH B O 1 HETATM 4708 O O . HOH DA 6 . ? 3.259 -3.531 -11.390 1.00 15.78 ? 2115 HOH B O 1 HETATM 4709 O O . HOH DA 6 . ? 30.008 8.817 -12.747 1.00 38.05 ? 2116 HOH B O 1 HETATM 4710 O O . HOH DA 6 . ? -2.415 -6.901 -19.733 1.00 41.09 ? 2117 HOH B O 1 HETATM 4711 O O . HOH DA 6 . ? -0.750 -7.384 -21.541 1.00 21.04 ? 2118 HOH B O 1 HETATM 4712 O O . HOH DA 6 . ? -13.534 2.376 -16.580 1.00 36.49 ? 2119 HOH B O 1 HETATM 4713 O O . HOH DA 6 . ? -8.119 6.799 -18.552 1.00 31.84 ? 2120 HOH B O 1 HETATM 4714 O O . HOH DA 6 . ? -12.018 6.996 -21.852 1.00 36.51 ? 2121 HOH B O 1 HETATM 4715 O O . HOH DA 6 . ? -6.545 7.346 -20.996 1.00 42.06 ? 2122 HOH B O 1 HETATM 4716 O O . HOH DA 6 . ? -11.168 -3.765 -25.094 1.00 25.95 ? 2123 HOH B O 1 HETATM 4717 O O . HOH DA 6 . ? -13.602 -0.298 -23.454 1.00 35.98 ? 2124 HOH B O 1 HETATM 4718 O O . HOH DA 6 . ? -0.686 -4.771 -26.242 1.00 26.95 ? 2125 HOH B O 1 HETATM 4719 O O . HOH DA 6 . ? -7.187 -3.589 -25.032 1.00 39.02 ? 2126 HOH B O 1 HETATM 4720 O O . HOH DA 6 . ? -6.217 6.202 -28.609 1.00 36.72 ? 2127 HOH B O 1 HETATM 4721 O O . HOH DA 6 . ? -7.651 6.036 -23.363 1.00 31.42 ? 2128 HOH B O 1 HETATM 4722 O O . HOH DA 6 . ? -10.777 3.963 -25.518 1.00 34.56 ? 2129 HOH B O 1 HETATM 4723 O O . HOH DA 6 . ? 3.739 -3.585 -35.221 1.00 32.93 ? 2130 HOH B O 1 HETATM 4724 O O . HOH DA 6 . ? 9.673 -0.346 -31.950 1.00 33.86 ? 2131 HOH B O 1 HETATM 4725 O O . HOH DA 6 . ? 9.075 -6.390 -34.075 1.00 30.50 ? 2132 HOH B O 1 HETATM 4726 O O . HOH DA 6 . ? 2.472 -0.257 -35.393 1.00 25.76 ? 2133 HOH B O 1 HETATM 4727 O O . HOH DA 6 . ? -2.671 6.860 -38.634 1.00 42.79 ? 2134 HOH B O 1 HETATM 4728 O O . HOH DA 6 . ? 4.075 -6.937 -25.550 1.00 33.06 ? 2135 HOH B O 1 HETATM 4729 O O . HOH DA 6 . ? 9.411 -2.577 -22.151 1.00 12.87 ? 2136 HOH B O 1 HETATM 4730 O O . HOH DA 6 . ? 1.406 -5.479 -25.076 1.00 28.58 ? 2137 HOH B O 1 HETATM 4731 O O . HOH DA 6 . ? 16.087 -5.676 -29.177 1.00 21.07 ? 2138 HOH B O 1 HETATM 4732 O O . HOH DA 6 . ? 19.006 -0.413 -32.180 1.00 23.78 ? 2139 HOH B O 1 HETATM 4733 O O . HOH DA 6 . ? 17.472 2.338 -31.624 1.00 22.64 ? 2140 HOH B O 1 HETATM 4734 O O . HOH DA 6 . ? 18.522 5.149 -27.958 1.00 49.32 ? 2141 HOH B O 1 HETATM 4735 O O . HOH DA 6 . ? 26.945 -2.209 -25.503 1.00 40.04 ? 2142 HOH B O 1 HETATM 4736 O O . HOH DA 6 . ? 23.912 -1.465 -16.583 1.00 45.64 ? 2143 HOH B O 1 HETATM 4737 O O . HOH DA 6 . ? 22.166 -12.586 -24.982 1.00 36.90 ? 2144 HOH B O 1 HETATM 4738 O O . HOH DA 6 . ? 23.018 -14.110 -17.008 1.00 28.52 ? 2145 HOH B O 1 HETATM 4739 O O . HOH DA 6 . ? 25.124 -6.388 -20.697 1.00 17.37 ? 2146 HOH B O 1 HETATM 4740 O O . HOH DA 6 . ? 26.101 -6.879 -18.609 1.00 24.82 ? 2147 HOH B O 1 HETATM 4741 O O . HOH DA 6 . ? 26.985 -9.498 -23.365 1.00 39.95 ? 2148 HOH B O 1 HETATM 4742 O O . HOH DA 6 . ? 27.703 -10.374 -19.273 1.00 15.71 ? 2149 HOH B O 1 HETATM 4743 O O . HOH DA 6 . ? 32.518 -5.438 -12.607 1.00 33.22 ? 2150 HOH B O 1 HETATM 4744 O O . HOH DA 6 . ? 32.663 -2.220 -12.675 1.00 26.32 ? 2151 HOH B O 1 HETATM 4745 O O . HOH DA 6 . ? 21.692 -8.284 -2.876 1.00 27.29 ? 2152 HOH B O 1 HETATM 4746 O O . HOH DA 6 . ? 27.862 -0.970 -8.072 1.00 47.66 ? 2153 HOH B O 1 HETATM 4747 O O . HOH DA 6 . ? 20.126 -0.708 -2.295 1.00 33.38 ? 2154 HOH B O 1 HETATM 4748 O O . HOH DA 6 . ? 27.420 5.054 -9.095 1.00 35.98 ? 2155 HOH B O 1 HETATM 4749 O O . HOH DA 6 . ? 21.397 2.109 -9.641 1.00 28.76 ? 2156 HOH B O 1 HETATM 4750 O O . HOH DA 6 . ? 20.949 -8.138 -0.506 1.00 30.13 ? 2157 HOH B O 1 HETATM 4751 O O . HOH DA 6 . ? 16.827 2.002 -5.954 1.00 36.41 ? 2158 HOH B O 1 HETATM 4752 O O . HOH DA 6 . ? 9.243 -5.834 -0.283 1.00 21.67 ? 2159 HOH B O 1 HETATM 4753 O O . HOH DA 6 . ? 10.899 -1.602 -0.555 1.00 20.78 ? 2160 HOH B O 1 HETATM 4754 O O . HOH DA 6 . ? 8.440 -10.138 -0.797 1.00 33.27 ? 2161 HOH B O 1 HETATM 4755 O O . HOH DA 6 . ? 19.180 -11.054 0.069 1.00 34.81 ? 2162 HOH B O 1 HETATM 4756 O O . HOH DA 6 . ? 0.018 2.576 -4.216 1.00 21.53 ? 2163 HOH B O 1 HETATM 4757 O O . HOH DA 6 . ? 7.514 4.253 -8.905 1.00 28.77 ? 2164 HOH B O 1 HETATM 4758 O O . HOH DA 6 . ? 0.347 10.126 -13.714 1.00 29.94 ? 2165 HOH B O 1 HETATM 4759 O O . HOH DA 6 . ? 7.146 9.836 -5.591 1.00 52.41 ? 2166 HOH B O 1 HETATM 4760 O O . HOH DA 6 . ? 6.595 11.582 -19.968 1.00 28.71 ? 2167 HOH B O 1 HETATM 4761 O O . HOH DA 6 . ? 0.848 13.163 -16.286 1.00 35.28 ? 2168 HOH B O 1 HETATM 4762 O O . HOH DA 6 . ? 3.171 15.774 -16.515 1.00 37.95 ? 2169 HOH B O 1 HETATM 4763 O O . HOH DA 6 . ? 1.867 15.332 -23.088 1.00 28.92 ? 2170 HOH B O 1 HETATM 4764 O O . HOH DA 6 . ? -0.079 14.558 -28.439 1.00 27.69 ? 2171 HOH B O 1 HETATM 4765 O O . HOH DA 6 . ? -8.693 8.741 -25.829 1.00 40.16 ? 2172 HOH B O 1 HETATM 4766 O O . HOH DA 6 . ? -7.063 10.708 -24.304 1.00 37.93 ? 2173 HOH B O 1 HETATM 4767 O O . HOH DA 6 . ? 3.466 12.944 -32.518 1.00 40.42 ? 2174 HOH B O 1 HETATM 4768 O O . HOH DA 6 . ? 5.275 14.356 -28.598 1.00 29.86 ? 2175 HOH B O 1 HETATM 4769 O O . HOH DA 6 . ? 10.716 11.297 -25.253 1.00 18.23 ? 2176 HOH B O 1 HETATM 4770 O O . HOH DA 6 . ? 15.063 11.330 -29.307 1.00 48.69 ? 2177 HOH B O 1 HETATM 4771 O O . HOH DA 6 . ? 19.636 11.337 -26.194 1.00 40.11 ? 2178 HOH B O 1 HETATM 4772 O O . HOH DA 6 . ? 8.596 12.450 -21.379 1.00 37.81 ? 2179 HOH B O 1 HETATM 4773 O O . HOH DA 6 . ? 14.771 17.739 -19.547 1.00 33.67 ? 2180 HOH B O 1 HETATM 4774 O O . HOH DA 6 . ? 18.866 5.745 -18.003 1.00 22.42 ? 2181 HOH B O 1 HETATM 4775 O O . HOH DA 6 . ? 14.842 8.392 -14.243 1.00 34.89 ? 2182 HOH B O 1 HETATM 4776 O O . HOH DA 6 . ? 16.765 1.070 -11.353 1.00 26.87 ? 2183 HOH B O 1 HETATM 4777 O O . HOH DA 6 . ? 21.175 1.788 -19.288 1.00 34.64 ? 2184 HOH B O 1 HETATM 4778 O O . HOH DA 6 . ? 14.291 4.230 -6.532 1.00 48.89 ? 2185 HOH B O 1 HETATM 4779 O O . HOH DA 6 . ? 9.208 -0.578 -5.865 1.00 39.23 ? 2186 HOH B O 1 HETATM 4780 O O . HOH DA 6 . ? 12.762 -16.762 0.762 1.00 34.25 ? 2187 HOH B O 1 HETATM 4781 O O . HOH DA 6 . ? 10.163 -29.336 -0.950 1.00 32.44 ? 2188 HOH B O 1 HETATM 4782 O O . HOH DA 6 . ? 11.546 -28.554 3.243 1.00 41.39 ? 2189 HOH B O 1 HETATM 4783 O O . HOH DA 6 . ? 7.753 -26.324 3.395 1.00 40.64 ? 2190 HOH B O 1 HETATM 4784 O O . HOH DA 6 . ? -10.843 -19.828 -7.397 1.00 27.33 ? 2191 HOH B O 1 HETATM 4785 O O . HOH DA 6 . ? -8.408 -26.322 -15.911 1.00 38.21 ? 2192 HOH B O 1 HETATM 4786 O O . HOH DA 6 . ? -12.253 -23.560 -9.178 1.00 39.62 ? 2193 HOH B O 1 HETATM 4787 O O . HOH DA 6 . ? -16.264 -20.596 -12.164 1.00 31.46 ? 2194 HOH B O 1 HETATM 4788 O O . HOH DA 6 . ? -22.814 -23.077 -14.043 1.00 45.18 ? 2195 HOH B O 1 HETATM 4789 O O . HOH DA 6 . ? -23.668 -20.298 -16.226 1.00 36.36 ? 2196 HOH B O 1 HETATM 4790 O O . HOH DA 6 . ? -19.964 -22.844 -13.518 1.00 29.57 ? 2197 HOH B O 1 HETATM 4791 O O . HOH DA 6 . ? -15.927 -31.932 -11.679 1.00 58.04 ? 2198 HOH B O 1 HETATM 4792 O O . HOH DA 6 . ? -11.484 -30.811 -11.633 1.00 50.24 ? 2199 HOH B O 1 HETATM 4793 O O . HOH DA 6 . ? -10.383 -30.669 -18.845 1.00 50.14 ? 2200 HOH B O 1 HETATM 4794 O O . HOH DA 6 . ? -16.623 -30.200 -19.763 1.00 36.09 ? 2201 HOH B O 1 HETATM 4795 O O . HOH DA 6 . ? -3.210 -30.370 -18.563 1.00 33.02 ? 2202 HOH B O 1 HETATM 4796 O O . HOH DA 6 . ? 5.393 -28.110 -29.269 1.00 49.79 ? 2203 HOH B O 1 HETATM 4797 O O . HOH DA 6 . ? 4.394 -30.562 -30.615 1.00 48.51 ? 2204 HOH B O 1 HETATM 4798 O O . HOH DA 6 . ? 19.078 0.676 -13.096 1.00 32.39 ? 2205 HOH B O 1 HETATM 4799 O O . HOH DA 6 . ? 19.933 3.009 -14.332 1.00 32.58 ? 2206 HOH B O 1 HETATM 4800 O O . HOH DA 6 . ? 27.327 6.528 -18.164 1.00 36.97 ? 2207 HOH B O 1 HETATM 4801 O O . HOH DA 6 . ? 29.958 7.386 -15.966 1.00 40.73 ? 2208 HOH B O 1 HETATM 4802 O O . HOH DA 6 . ? 23.730 11.479 -21.547 1.00 38.50 ? 2209 HOH B O 1 HETATM 4803 O O . HOH DA 6 . ? 28.054 12.126 -20.376 1.00 49.99 ? 2210 HOH B O 1 HETATM 4804 O O . HOH DA 6 . ? 18.476 10.581 -18.408 1.00 37.30 ? 2211 HOH B O 1 HETATM 4805 O O . HOH DA 6 . ? 21.730 -29.689 -10.454 1.00 36.42 ? 2212 HOH B O 1 HETATM 4806 O O . HOH DA 6 . ? -20.006 -32.069 -18.539 1.00 37.14 ? 2213 HOH B O 1 HETATM 4807 O O . HOH DA 6 . ? -3.138 24.616 28.098 1.00 31.27 ? 2214 HOH B O 1 HETATM 4808 O O . HOH DA 6 . ? 12.971 11.806 -2.678 1.00 34.75 ? 2215 HOH B O 1 HETATM 4809 O O . HOH DA 6 . ? -23.573 36.770 19.318 1.00 47.21 ? 2216 HOH B O 1 HETATM 4810 O O . HOH DA 6 . ? 8.751 -7.048 8.303 1.00 38.37 ? 2217 HOH B O 1 HETATM 4811 O O . HOH DA 6 . ? 26.531 6.802 -26.454 1.00 38.39 ? 2218 HOH B O 1 HETATM 4812 O O . HOH DA 6 . ? -1.610 26.524 29.676 1.00 37.96 ? 2219 HOH B O 1 HETATM 4813 O O . HOH DA 6 . ? -10.888 37.640 4.305 1.00 49.05 ? 2220 HOH B O 1 HETATM 4814 O O . HOH DA 6 . ? -13.337 9.301 -21.896 1.00 42.54 ? 2221 HOH B O 1 HETATM 4815 O O . HOH DA 6 . ? 19.780 -33.898 -16.215 1.00 43.26 ? 2222 HOH B O 1 HETATM 4816 O O . HOH DA 6 . ? -16.303 -12.673 17.218 1.00 52.50 ? 2223 HOH B O 1 HETATM 4817 O O . HOH DA 6 . ? -26.253 -7.121 21.411 1.00 45.79 ? 2224 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 TRP 1 1 1 TRP TRP A . n A 1 2 GLY 2 2 2 GLY GLY A . n A 1 3 LYS 3 3 3 LYS LYS A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 GLY 5 5 5 GLY GLY A . n A 1 6 HIS 6 6 6 HIS HIS A . n A 1 7 GLU 7 7 7 GLU GLU A . n A 1 8 ILE 8 8 8 ILE ILE A . n A 1 9 ILE 9 9 9 ILE ILE A . n A 1 10 CYS 10 10 10 CYS CYS A . n A 1 11 LYS 11 11 11 LYS LYS A . n A 1 12 ILE 12 12 12 ILE ILE A . n A 1 13 ALA 13 13 13 ALA ALA A . n A 1 14 GLN 14 14 14 GLN GLN A . n A 1 15 THR 15 15 15 THR THR A . n A 1 16 ARG 16 16 16 ARG ARG A . n A 1 17 LEU 17 17 17 LEU LEU A . n A 1 18 ASP 18 18 18 ASP ASP A . n A 1 19 GLU 19 19 19 GLU GLU A . n A 1 20 THR 20 20 20 THR THR A . n A 1 21 ALA 21 21 21 ALA ALA A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 LYS 23 23 23 LYS LYS A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 VAL 25 25 25 VAL VAL A . n A 1 26 LYS 26 26 26 LYS LYS A . n A 1 27 GLU 27 27 27 GLU GLU A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 LEU 29 29 29 LEU LEU A . n A 1 30 PRO 30 30 30 PRO PRO A . n A 1 31 GLU 31 31 31 GLU GLU A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 ALA 33 33 33 ALA ALA A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 GLY 35 35 35 GLY GLY A . n A 1 36 ASP 36 36 36 ASP ASP A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 SER 38 38 38 SER SER A . n A 1 39 SER 39 39 39 SER SER A . n A 1 40 LEU 40 40 40 LEU LEU A . n A 1 41 CYS 41 41 41 CYS CYS A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 TRP 43 43 43 TRP TRP A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 TYR 51 51 51 TYR TYR A . n A 1 52 HIS 52 52 52 HIS HIS A . n A 1 53 TRP 53 53 53 TRP TRP A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 PRO 56 56 56 PRO PRO A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 HIS 58 58 58 HIS HIS A . n A 1 59 TYR 59 59 59 TYR TYR A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 ASN 61 61 61 ASN ASN A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 PRO 63 63 63 PRO PRO A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 CYS 66 66 66 CYS CYS A . n A 1 67 SER 67 67 67 SER SER A . n A 1 68 TYR 68 68 68 TYR TYR A . n A 1 69 GLN 69 69 69 GLN GLN A . n A 1 70 TYR 70 70 70 TYR TYR A . n A 1 71 ASN 71 71 71 ASN ASN A . n A 1 72 ARG 72 72 72 ARG ARG A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 CYS 74 74 74 CYS CYS A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ASP 76 76 76 ASP ASP A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 GLU 80 80 80 GLU GLU A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 GLY 82 82 82 GLY GLY A . n A 1 83 ARG 83 83 83 ARG ARG A . n A 1 84 CYS 84 84 84 CYS CYS A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 GLY 87 87 87 GLY GLY A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 ILE 89 89 89 ILE ILE A . n A 1 90 TYR 90 90 90 TYR TYR A . n A 1 91 ASN 91 91 91 ASN ASN A . n A 1 92 TYR 92 92 92 TYR TYR A . n A 1 93 THR 93 93 93 THR THR A . n A 1 94 THR 94 94 94 THR THR A . n A 1 95 GLN 95 95 95 GLN GLN A . n A 1 96 LEU 96 96 96 LEU LEU A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 SER 98 98 98 SER SER A . n A 1 99 TYR 99 99 99 TYR TYR A . n A 1 100 LYS 100 100 100 LYS LYS A . n A 1 101 THR 101 101 ? ? ? A . n A 1 102 ALA 102 102 ? ? ? A . n A 1 103 ALA 103 103 ? ? ? A . n A 1 104 SER 104 104 ? ? ? A . n A 1 105 SER 105 105 ? ? ? A . n A 1 106 GLN 106 106 ? ? ? A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 GLN 108 108 108 GLN GLN A . n A 1 109 TYR 109 109 109 TYR TYR A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 ALA 114 114 114 ALA ALA A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 LEU 116 116 116 LEU LEU A . n A 1 117 PHE 117 117 117 PHE PHE A . n A 1 118 VAL 118 118 118 VAL VAL A . n A 1 119 SER 119 119 119 SER SER A . n A 1 120 HIS 120 120 120 HIS HIS A . n A 1 121 PHE 121 121 121 PHE PHE A . n A 1 122 MET 122 122 122 MET MET A . n A 1 123 GLY 123 123 123 GLY GLY A . n A 1 124 ASP 124 124 124 ASP ASP A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 HIS 126 126 126 HIS HIS A . n A 1 127 GLN 127 127 127 GLN GLN A . n A 1 128 PRO 128 128 128 PRO PRO A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 HIS 130 130 130 HIS HIS A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 TYR 133 133 133 TYR TYR A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 ASP 136 136 136 ASP ASP A . n A 1 137 LYS 137 137 137 LYS LYS A . n A 1 138 GLY 138 138 138 GLY GLY A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 ASN 140 140 140 ASN ASN A . n A 1 141 THR 141 141 141 THR THR A . n A 1 142 ILE 142 142 142 ILE ILE A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 VAL 144 144 144 VAL VAL A . n A 1 145 HIS 145 145 145 HIS HIS A . n A 1 146 TRP 146 146 146 TRP TRP A . n A 1 147 TYR 147 147 147 TYR TYR A . n A 1 148 THR 148 148 148 THR THR A . n A 1 149 ARG 149 149 149 ARG ARG A . n A 1 150 LYS 150 150 150 LYS LYS A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 LEU 153 153 153 LEU LEU A . n A 1 154 HIS 154 154 154 HIS HIS A . n A 1 155 HIS 155 155 155 HIS HIS A . n A 1 156 ILE 156 156 156 ILE ILE A . n A 1 157 TRP 157 157 157 TRP TRP A . n A 1 158 ASP 158 158 158 ASP ASP A . n A 1 159 SER 159 159 159 SER SER A . n A 1 160 ASN 160 160 160 ASN ASN A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 ILE 162 162 162 ILE ILE A . n A 1 163 GLU 163 163 163 GLU GLU A . n A 1 164 THR 164 164 164 THR THR A . n A 1 165 ALA 165 165 165 ALA ALA A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 ALA 167 167 167 ALA ALA A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 TYR 170 170 170 TYR TYR A . n A 1 171 ASN 171 171 171 ASN ASN A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 ALA 173 173 173 ALA ALA A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 GLU 175 175 175 GLU GLU A . n A 1 176 GLY 176 176 176 GLY GLY A . n A 1 177 MET 177 177 177 MET MET A . n A 1 178 VAL 178 178 178 VAL VAL A . n A 1 179 ASP 179 179 179 ASP ASP A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 LEU 181 181 181 LEU LEU A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 LYS 183 183 183 LYS LYS A . n A 1 184 ASN 184 184 184 ASN ASN A . n A 1 185 ILE 185 185 185 ILE ILE A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 GLU 188 188 188 GLU GLU A . n A 1 189 TRP 189 189 189 TRP TRP A . n A 1 190 ALA 190 190 190 ALA ALA A . n A 1 191 ASP 191 191 191 ASP ASP A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 VAL 193 193 193 VAL VAL A . n A 1 194 LYS 194 194 194 LYS LYS A . n A 1 195 ARG 195 195 195 ARG ARG A . n A 1 196 TRP 196 196 196 TRP TRP A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 THR 198 198 198 THR THR A . n A 1 199 CYS 199 199 199 CYS CYS A . n A 1 200 THR 200 200 200 THR THR A . n A 1 201 LYS 201 201 201 LYS LYS A . n A 1 202 LYS 202 202 ? ? ? A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 ALA 204 204 204 ALA ALA A . n A 1 205 CYS 205 205 205 CYS CYS A . n A 1 206 PRO 206 206 206 PRO PRO A . n A 1 207 ASP 207 207 207 ASP ASP A . n A 1 208 ILE 208 208 208 ILE ILE A . n A 1 209 TYR 209 209 209 TYR TYR A . n A 1 210 ALA 210 210 210 ALA ALA A . n A 1 211 SER 211 211 211 SER SER A . n A 1 212 GLU 212 212 212 GLU GLU A . n A 1 213 GLY 213 213 213 GLY GLY A . n A 1 214 ILE 214 214 214 ILE ILE A . n A 1 215 GLN 215 215 215 GLN GLN A . n A 1 216 ALA 216 216 216 ALA ALA A . n A 1 217 ALA 217 217 217 ALA ALA A . n A 1 218 CYS 218 218 218 CYS CYS A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 TRP 220 220 220 TRP TRP A . n A 1 221 ALA 221 221 221 ALA ALA A . n A 1 222 TYR 222 222 222 TYR TYR A . n A 1 223 LYS 223 223 223 LYS LYS A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 THR 226 226 226 THR THR A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 GLY 228 228 228 GLY GLY A . n A 1 229 ASP 229 229 229 ASP ASP A . n A 1 230 THR 230 230 230 THR THR A . n A 1 231 LEU 231 231 231 LEU LEU A . n A 1 232 GLU 232 232 232 GLU GLU A . n A 1 233 ASP 233 233 233 ASP ASP A . n A 1 234 GLU 234 234 234 GLU GLU A . n A 1 235 TYR 235 235 235 TYR TYR A . n A 1 236 PHE 236 236 236 PHE PHE A . n A 1 237 TYR 237 237 237 TYR TYR A . n A 1 238 SER 238 238 238 SER SER A . n A 1 239 ARG 239 239 239 ARG ARG A . n A 1 240 LEU 240 240 240 LEU LEU A . n A 1 241 PRO 241 241 241 PRO PRO A . n A 1 242 ILE 242 242 242 ILE ILE A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 GLN 245 245 245 GLN GLN A . n A 1 246 ARG 246 246 246 ARG ARG A . n A 1 247 LEU 247 247 247 LEU LEU A . n A 1 248 ALA 248 248 248 ALA ALA A . n A 1 249 GLN 249 249 249 GLN GLN A . n A 1 250 GLY 250 250 250 GLY GLY A . n A 1 251 GLY 251 251 251 GLY GLY A . n A 1 252 VAL 252 252 252 VAL VAL A . n A 1 253 ARG 253 253 253 ARG ARG A . n A 1 254 LEU 254 254 254 LEU LEU A . n A 1 255 ALA 255 255 255 ALA ALA A . n A 1 256 ALA 256 256 256 ALA ALA A . n A 1 257 THR 257 257 257 THR THR A . n A 1 258 LEU 258 258 258 LEU LEU A . n A 1 259 ASN 259 259 259 ASN ASN A . n A 1 260 ARG 260 260 260 ARG ARG A . n A 1 261 ILE 261 261 261 ILE ILE A . n A 1 262 PHE 262 262 262 PHE PHE A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 HIS 264 264 264 HIS HIS A . n A 1 265 HIS 265 265 ? ? ? A . n A 1 266 HIS 266 266 ? ? ? A . n A 1 267 HIS 267 267 ? ? ? A . n A 1 268 HIS 268 268 ? ? ? A . n A 1 269 HIS 269 269 ? ? ? A . n B 1 1 TRP 1 1 1 TRP TRP B . n B 1 2 GLY 2 2 2 GLY GLY B . n B 1 3 LYS 3 3 3 LYS LYS B . n B 1 4 GLU 4 4 4 GLU GLU B . n B 1 5 GLY 5 5 5 GLY GLY B . n B 1 6 HIS 6 6 6 HIS HIS B . n B 1 7 GLU 7 7 7 GLU GLU B . n B 1 8 ILE 8 8 8 ILE ILE B . n B 1 9 ILE 9 9 9 ILE ILE B . n B 1 10 CYS 10 10 10 CYS CYS B . n B 1 11 LYS 11 11 11 LYS LYS B . n B 1 12 ILE 12 12 12 ILE ILE B . n B 1 13 ALA 13 13 13 ALA ALA B . n B 1 14 GLN 14 14 14 GLN GLN B . n B 1 15 THR 15 15 15 THR THR B . n B 1 16 ARG 16 16 16 ARG ARG B . n B 1 17 LEU 17 17 17 LEU LEU B . n B 1 18 ASP 18 18 18 ASP ASP B . n B 1 19 GLU 19 19 19 GLU GLU B . n B 1 20 THR 20 20 20 THR THR B . n B 1 21 ALA 21 21 21 ALA ALA B . n B 1 22 ALA 22 22 22 ALA ALA B . n B 1 23 LYS 23 23 23 LYS LYS B . n B 1 24 ALA 24 24 24 ALA ALA B . n B 1 25 VAL 25 25 25 VAL VAL B . n B 1 26 LYS 26 26 26 LYS LYS B . n B 1 27 GLU 27 27 27 GLU GLU B . n B 1 28 LEU 28 28 28 LEU LEU B . n B 1 29 LEU 29 29 29 LEU LEU B . n B 1 30 PRO 30 30 30 PRO PRO B . n B 1 31 GLU 31 31 31 GLU GLU B . n B 1 32 SER 32 32 32 SER SER B . n B 1 33 ALA 33 33 33 ALA ALA B . n B 1 34 GLU 34 34 34 GLU GLU B . n B 1 35 GLY 35 35 35 GLY GLY B . n B 1 36 ASP 36 36 36 ASP ASP B . n B 1 37 LEU 37 37 37 LEU LEU B . n B 1 38 SER 38 38 38 SER SER B . n B 1 39 SER 39 39 39 SER SER B . n B 1 40 LEU 40 40 40 LEU LEU B . n B 1 41 CYS 41 41 41 CYS CYS B . n B 1 42 LEU 42 42 42 LEU LEU B . n B 1 43 TRP 43 43 43 TRP TRP B . n B 1 44 ALA 44 44 44 ALA ALA B . n B 1 45 ASP 45 45 45 ASP ASP B . n B 1 46 ARG 46 46 46 ARG ARG B . n B 1 47 VAL 47 47 47 VAL VAL B . n B 1 48 LYS 48 48 48 LYS LYS B . n B 1 49 PHE 49 49 49 PHE PHE B . n B 1 50 ARG 50 50 50 ARG ARG B . n B 1 51 TYR 51 51 51 TYR TYR B . n B 1 52 HIS 52 52 52 HIS HIS B . n B 1 53 TRP 53 53 53 TRP TRP B . n B 1 54 SER 54 54 54 SER SER B . n B 1 55 SER 55 55 55 SER SER B . n B 1 56 PRO 56 56 56 PRO PRO B . n B 1 57 LEU 57 57 57 LEU LEU B . n B 1 58 HIS 58 58 58 HIS HIS B . n B 1 59 TYR 59 59 59 TYR TYR B . n B 1 60 ILE 60 60 60 ILE ILE B . n B 1 61 ASN 61 61 61 ASN ASN B . n B 1 62 THR 62 62 62 THR THR B . n B 1 63 PRO 63 63 63 PRO PRO B . n B 1 64 ASP 64 64 64 ASP ASP B . n B 1 65 ALA 65 65 65 ALA ALA B . n B 1 66 CYS 66 66 66 CYS CYS B . n B 1 67 SER 67 67 67 SER SER B . n B 1 68 TYR 68 68 68 TYR TYR B . n B 1 69 GLN 69 69 69 GLN GLN B . n B 1 70 TYR 70 70 70 TYR TYR B . n B 1 71 ASN 71 71 71 ASN ASN B . n B 1 72 ARG 72 72 72 ARG ARG B . n B 1 73 ASP 73 73 73 ASP ASP B . n B 1 74 CYS 74 74 74 CYS CYS B . n B 1 75 LYS 75 75 75 LYS LYS B . n B 1 76 ASP 76 76 76 ASP ASP B . n B 1 77 GLU 77 77 77 GLU GLU B . n B 1 78 SER 78 78 78 SER SER B . n B 1 79 GLY 79 79 79 GLY GLY B . n B 1 80 GLU 80 80 80 GLU GLU B . n B 1 81 LYS 81 81 81 LYS LYS B . n B 1 82 GLY 82 82 82 GLY GLY B . n B 1 83 ARG 83 83 83 ARG ARG B . n B 1 84 CYS 84 84 84 CYS CYS B . n B 1 85 VAL 85 85 85 VAL VAL B . n B 1 86 ALA 86 86 86 ALA ALA B . n B 1 87 GLY 87 87 87 GLY GLY B . n B 1 88 ALA 88 88 88 ALA ALA B . n B 1 89 ILE 89 89 89 ILE ILE B . n B 1 90 TYR 90 90 90 TYR TYR B . n B 1 91 ASN 91 91 91 ASN ASN B . n B 1 92 TYR 92 92 92 TYR TYR B . n B 1 93 THR 93 93 93 THR THR B . n B 1 94 THR 94 94 94 THR THR B . n B 1 95 GLN 95 95 95 GLN GLN B . n B 1 96 LEU 96 96 96 LEU LEU B . n B 1 97 LEU 97 97 97 LEU LEU B . n B 1 98 SER 98 98 98 SER SER B . n B 1 99 TYR 99 99 99 TYR TYR B . n B 1 100 LYS 100 100 100 LYS LYS B . n B 1 101 THR 101 101 ? ? ? B . n B 1 102 ALA 102 102 ? ? ? B . n B 1 103 ALA 103 103 ? ? ? B . n B 1 104 SER 104 104 ? ? ? B . n B 1 105 SER 105 105 ? ? ? B . n B 1 106 GLN 106 106 ? ? ? B . n B 1 107 SER 107 107 107 SER SER B . n B 1 108 GLN 108 108 108 GLN GLN B . n B 1 109 TYR 109 109 109 TYR TYR B . n B 1 110 ASN 110 110 110 ASN ASN B . n B 1 111 LEU 111 111 111 LEU LEU B . n B 1 112 THR 112 112 112 THR THR B . n B 1 113 GLU 113 113 113 GLU GLU B . n B 1 114 ALA 114 114 114 ALA ALA B . n B 1 115 LEU 115 115 115 LEU LEU B . n B 1 116 LEU 116 116 116 LEU LEU B . n B 1 117 PHE 117 117 117 PHE PHE B . n B 1 118 VAL 118 118 118 VAL VAL B . n B 1 119 SER 119 119 119 SER SER B . n B 1 120 HIS 120 120 120 HIS HIS B . n B 1 121 PHE 121 121 121 PHE PHE B . n B 1 122 MET 122 122 122 MET MET B . n B 1 123 GLY 123 123 123 GLY GLY B . n B 1 124 ASP 124 124 124 ASP ASP B . n B 1 125 ILE 125 125 125 ILE ILE B . n B 1 126 HIS 126 126 126 HIS HIS B . n B 1 127 GLN 127 127 127 GLN GLN B . n B 1 128 PRO 128 128 128 PRO PRO B . n B 1 129 LEU 129 129 129 LEU LEU B . n B 1 130 HIS 130 130 130 HIS HIS B . n B 1 131 VAL 131 131 131 VAL VAL B . n B 1 132 SER 132 132 132 SER SER B . n B 1 133 TYR 133 133 133 TYR TYR B . n B 1 134 ALA 134 134 134 ALA ALA B . n B 1 135 SER 135 135 135 SER SER B . n B 1 136 ASP 136 136 136 ASP ASP B . n B 1 137 LYS 137 137 137 LYS LYS B . n B 1 138 GLY 138 138 138 GLY GLY B . n B 1 139 GLY 139 139 139 GLY GLY B . n B 1 140 ASN 140 140 140 ASN ASN B . n B 1 141 THR 141 141 141 THR THR B . n B 1 142 ILE 142 142 142 ILE ILE B . n B 1 143 GLU 143 143 143 GLU GLU B . n B 1 144 VAL 144 144 144 VAL VAL B . n B 1 145 HIS 145 145 145 HIS HIS B . n B 1 146 TRP 146 146 146 TRP TRP B . n B 1 147 TYR 147 147 147 TYR TYR B . n B 1 148 THR 148 148 148 THR THR B . n B 1 149 ARG 149 149 149 ARG ARG B . n B 1 150 LYS 150 150 150 LYS LYS B . n B 1 151 ALA 151 151 151 ALA ALA B . n B 1 152 ASN 152 152 152 ASN ASN B . n B 1 153 LEU 153 153 153 LEU LEU B . n B 1 154 HIS 154 154 154 HIS HIS B . n B 1 155 HIS 155 155 155 HIS HIS B . n B 1 156 ILE 156 156 156 ILE ILE B . n B 1 157 TRP 157 157 157 TRP TRP B . n B 1 158 ASP 158 158 158 ASP ASP B . n B 1 159 SER 159 159 159 SER SER B . n B 1 160 ASN 160 160 160 ASN ASN B . n B 1 161 ILE 161 161 161 ILE ILE B . n B 1 162 ILE 162 162 162 ILE ILE B . n B 1 163 GLU 163 163 163 GLU GLU B . n B 1 164 THR 164 164 164 THR THR B . n B 1 165 ALA 165 165 165 ALA ALA B . n B 1 166 GLU 166 166 166 GLU GLU B . n B 1 167 ALA 167 167 167 ALA ALA B . n B 1 168 ASP 168 168 168 ASP ASP B . n B 1 169 LEU 169 169 169 LEU LEU B . n B 1 170 TYR 170 170 170 TYR TYR B . n B 1 171 ASN 171 171 171 ASN ASN B . n B 1 172 SER 172 172 172 SER SER B . n B 1 173 ALA 173 173 173 ALA ALA B . n B 1 174 LEU 174 174 174 LEU LEU B . n B 1 175 GLU 175 175 175 GLU GLU B . n B 1 176 GLY 176 176 176 GLY GLY B . n B 1 177 MET 177 177 177 MET MET B . n B 1 178 VAL 178 178 178 VAL VAL B . n B 1 179 ASP 179 179 179 ASP ASP B . n B 1 180 ALA 180 180 180 ALA ALA B . n B 1 181 LEU 181 181 181 LEU LEU B . n B 1 182 LYS 182 182 182 LYS LYS B . n B 1 183 LYS 183 183 183 LYS LYS B . n B 1 184 ASN 184 184 184 ASN ASN B . n B 1 185 ILE 185 185 185 ILE ILE B . n B 1 186 THR 186 186 186 THR THR B . n B 1 187 THR 187 187 187 THR THR B . n B 1 188 GLU 188 188 188 GLU GLU B . n B 1 189 TRP 189 189 189 TRP TRP B . n B 1 190 ALA 190 190 190 ALA ALA B . n B 1 191 ASP 191 191 191 ASP ASP B . n B 1 192 GLN 192 192 192 GLN GLN B . n B 1 193 VAL 193 193 193 VAL VAL B . n B 1 194 LYS 194 194 194 LYS LYS B . n B 1 195 ARG 195 195 195 ARG ARG B . n B 1 196 TRP 196 196 196 TRP TRP B . n B 1 197 GLU 197 197 197 GLU GLU B . n B 1 198 THR 198 198 198 THR THR B . n B 1 199 CYS 199 199 199 CYS CYS B . n B 1 200 THR 200 200 200 THR THR B . n B 1 201 LYS 201 201 201 LYS LYS B . n B 1 202 LYS 202 202 ? ? ? B . n B 1 203 THR 203 203 203 THR THR B . n B 1 204 ALA 204 204 204 ALA ALA B . n B 1 205 CYS 205 205 205 CYS CYS B . n B 1 206 PRO 206 206 206 PRO PRO B . n B 1 207 ASP 207 207 207 ASP ASP B . n B 1 208 ILE 208 208 208 ILE ILE B . n B 1 209 TYR 209 209 209 TYR TYR B . n B 1 210 ALA 210 210 210 ALA ALA B . n B 1 211 SER 211 211 211 SER SER B . n B 1 212 GLU 212 212 212 GLU GLU B . n B 1 213 GLY 213 213 213 GLY GLY B . n B 1 214 ILE 214 214 214 ILE ILE B . n B 1 215 GLN 215 215 215 GLN GLN B . n B 1 216 ALA 216 216 216 ALA ALA B . n B 1 217 ALA 217 217 217 ALA ALA B . n B 1 218 CYS 218 218 218 CYS CYS B . n B 1 219 ASP 219 219 219 ASP ASP B . n B 1 220 TRP 220 220 220 TRP TRP B . n B 1 221 ALA 221 221 221 ALA ALA B . n B 1 222 TYR 222 222 222 TYR TYR B . n B 1 223 LYS 223 223 223 LYS LYS B . n B 1 224 GLY 224 224 224 GLY GLY B . n B 1 225 VAL 225 225 225 VAL VAL B . n B 1 226 THR 226 226 226 THR THR B . n B 1 227 GLU 227 227 227 GLU GLU B . n B 1 228 GLY 228 228 228 GLY GLY B . n B 1 229 ASP 229 229 229 ASP ASP B . n B 1 230 THR 230 230 230 THR THR B . n B 1 231 LEU 231 231 231 LEU LEU B . n B 1 232 GLU 232 232 232 GLU GLU B . n B 1 233 ASP 233 233 233 ASP ASP B . n B 1 234 GLU 234 234 234 GLU GLU B . n B 1 235 TYR 235 235 235 TYR TYR B . n B 1 236 PHE 236 236 236 PHE PHE B . n B 1 237 TYR 237 237 237 TYR TYR B . n B 1 238 SER 238 238 238 SER SER B . n B 1 239 ARG 239 239 239 ARG ARG B . n B 1 240 LEU 240 240 240 LEU LEU B . n B 1 241 PRO 241 241 241 PRO PRO B . n B 1 242 ILE 242 242 242 ILE ILE B . n B 1 243 VAL 243 243 243 VAL VAL B . n B 1 244 TYR 244 244 244 TYR TYR B . n B 1 245 GLN 245 245 245 GLN GLN B . n B 1 246 ARG 246 246 246 ARG ARG B . n B 1 247 LEU 247 247 247 LEU LEU B . n B 1 248 ALA 248 248 248 ALA ALA B . n B 1 249 GLN 249 249 249 GLN GLN B . n B 1 250 GLY 250 250 250 GLY GLY B . n B 1 251 GLY 251 251 251 GLY GLY B . n B 1 252 VAL 252 252 252 VAL VAL B . n B 1 253 ARG 253 253 253 ARG ARG B . n B 1 254 LEU 254 254 254 LEU LEU B . n B 1 255 ALA 255 255 255 ALA ALA B . n B 1 256 ALA 256 256 256 ALA ALA B . n B 1 257 THR 257 257 257 THR THR B . n B 1 258 LEU 258 258 258 LEU LEU B . n B 1 259 ASN 259 259 259 ASN ASN B . n B 1 260 ARG 260 260 260 ARG ARG B . n B 1 261 ILE 261 261 261 ILE ILE B . n B 1 262 PHE 262 262 262 PHE PHE B . n B 1 263 GLY 263 263 263 GLY GLY B . n B 1 264 HIS 264 264 264 HIS HIS B . n B 1 265 HIS 265 265 ? ? ? B . n B 1 266 HIS 266 266 ? ? ? B . n B 1 267 HIS 267 267 ? ? ? B . n B 1 268 HIS 268 268 ? ? ? B . n B 1 269 HIS 269 269 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 301 301 NAG NAG A . D 2 NAG 2 302 302 NAG NAG A . E 3 BMA 3 303 303 BMA BMA A . F 4 MAN 4 304 304 MAN MAN A . G 4 MAN 5 305 305 MAN MAN A . H 2 NAG 1 331 331 NAG NAG A . I 2 NAG 2 332 332 NAG NAG A . J 2 NAG 1 361 361 NAG NAG A . K 2 NAG 2 362 362 NAG NAG A . L 5 ZN 1 431 431 ZN ZN A . M 5 ZN 1 432 432 ZN ZN A . N 5 ZN 1 433 433 ZN ZN A . O 2 NAG 1 301 301 NAG NAG B . P 2 NAG 2 302 302 NAG NAG B . Q 3 BMA 3 303 303 BMA BMA B . R 4 MAN 4 304 304 MAN MAN B . S 4 MAN 5 305 305 MAN MAN B . T 2 NAG 1 331 331 NAG NAG B . U 2 NAG 2 332 332 NAG NAG B . V 3 BMA 3 333 333 BMA BMA B . W 2 NAG 1 361 361 NAG NAG B . X 2 NAG 2 362 362 NAG NAG B . Y 3 BMA 3 363 363 BMA BMA B . Z 5 ZN 1 431 431 ZN ZN B . AA 5 ZN 1 432 432 ZN ZN B . BA 5 ZN 1 433 433 ZN ZN B . CA 6 HOH 1 2001 2001 HOH HOH A . CA 6 HOH 2 2002 2002 HOH HOH A . CA 6 HOH 3 2003 2003 HOH HOH A . CA 6 HOH 4 2004 2004 HOH HOH A . CA 6 HOH 5 2005 2005 HOH HOH A . CA 6 HOH 6 2006 2006 HOH HOH A . CA 6 HOH 7 2007 2007 HOH HOH A . CA 6 HOH 8 2008 2008 HOH HOH A . CA 6 HOH 9 2009 2009 HOH HOH A . CA 6 HOH 10 2010 2010 HOH HOH A . CA 6 HOH 11 2011 2011 HOH HOH A . CA 6 HOH 12 2012 2012 HOH HOH A . CA 6 HOH 13 2013 2013 HOH HOH A . CA 6 HOH 14 2014 2014 HOH HOH A . CA 6 HOH 15 2015 2015 HOH HOH A . CA 6 HOH 16 2016 2016 HOH HOH A . CA 6 HOH 17 2017 2017 HOH HOH A . CA 6 HOH 18 2018 2018 HOH HOH A . CA 6 HOH 19 2019 2019 HOH HOH A . CA 6 HOH 20 2020 2020 HOH HOH A . CA 6 HOH 21 2021 2021 HOH HOH A . CA 6 HOH 22 2022 2022 HOH HOH A . CA 6 HOH 23 2023 2023 HOH HOH A . CA 6 HOH 24 2024 2024 HOH HOH A . CA 6 HOH 25 2025 2025 HOH HOH A . CA 6 HOH 26 2026 2026 HOH HOH A . CA 6 HOH 27 2027 2027 HOH HOH A . CA 6 HOH 28 2028 2028 HOH HOH A . CA 6 HOH 29 2029 2029 HOH HOH A . CA 6 HOH 30 2030 2030 HOH HOH A . CA 6 HOH 31 2031 2031 HOH HOH A . CA 6 HOH 32 2032 2032 HOH HOH A . CA 6 HOH 33 2033 2033 HOH HOH A . CA 6 HOH 34 2034 2034 HOH HOH A . CA 6 HOH 35 2035 2035 HOH HOH A . CA 6 HOH 36 2036 2036 HOH HOH A . CA 6 HOH 37 2037 2037 HOH HOH A . CA 6 HOH 38 2038 2038 HOH HOH A . CA 6 HOH 39 2039 2039 HOH HOH A . CA 6 HOH 40 2040 2040 HOH HOH A . CA 6 HOH 41 2041 2041 HOH HOH A . CA 6 HOH 42 2042 2042 HOH HOH A . CA 6 HOH 43 2043 2043 HOH HOH A . CA 6 HOH 44 2044 2044 HOH HOH A . CA 6 HOH 45 2045 2045 HOH HOH A . CA 6 HOH 46 2046 2046 HOH HOH A . CA 6 HOH 47 2047 2047 HOH HOH A . CA 6 HOH 48 2048 2048 HOH HOH A . CA 6 HOH 49 2049 2049 HOH HOH A . CA 6 HOH 50 2050 2050 HOH HOH A . CA 6 HOH 51 2051 2051 HOH HOH A . CA 6 HOH 52 2052 2052 HOH HOH A . CA 6 HOH 53 2053 2053 HOH HOH A . CA 6 HOH 54 2054 2054 HOH HOH A . CA 6 HOH 55 2055 2055 HOH HOH A . CA 6 HOH 56 2056 2056 HOH HOH A . CA 6 HOH 57 2057 2057 HOH HOH A . CA 6 HOH 58 2058 2058 HOH HOH A . CA 6 HOH 59 2059 2059 HOH HOH A . CA 6 HOH 60 2060 2060 HOH HOH A . CA 6 HOH 61 2061 2061 HOH HOH A . CA 6 HOH 62 2062 2062 HOH HOH A . CA 6 HOH 63 2063 2063 HOH HOH A . CA 6 HOH 64 2064 2064 HOH HOH A . CA 6 HOH 65 2065 2065 HOH HOH A . CA 6 HOH 66 2066 2066 HOH HOH A . CA 6 HOH 67 2067 2067 HOH HOH A . CA 6 HOH 68 2068 2068 HOH HOH A . CA 6 HOH 69 2069 2069 HOH HOH A . CA 6 HOH 70 2070 2070 HOH HOH A . CA 6 HOH 71 2071 2071 HOH HOH A . CA 6 HOH 72 2072 2072 HOH HOH A . CA 6 HOH 73 2073 2073 HOH HOH A . CA 6 HOH 74 2074 2074 HOH HOH A . CA 6 HOH 75 2075 2075 HOH HOH A . CA 6 HOH 76 2076 2076 HOH HOH A . CA 6 HOH 77 2077 2077 HOH HOH A . CA 6 HOH 78 2078 2078 HOH HOH A . CA 6 HOH 79 2079 2079 HOH HOH A . CA 6 HOH 80 2080 2080 HOH HOH A . CA 6 HOH 81 2081 2081 HOH HOH A . CA 6 HOH 82 2082 2082 HOH HOH A . CA 6 HOH 83 2083 2083 HOH HOH A . CA 6 HOH 84 2084 2084 HOH HOH A . CA 6 HOH 85 2085 2085 HOH HOH A . CA 6 HOH 86 2086 2086 HOH HOH A . CA 6 HOH 87 2087 2087 HOH HOH A . CA 6 HOH 88 2088 2088 HOH HOH A . CA 6 HOH 89 2089 2089 HOH HOH A . CA 6 HOH 90 2090 2090 HOH HOH A . CA 6 HOH 91 2091 2091 HOH HOH A . CA 6 HOH 92 2092 2092 HOH HOH A . CA 6 HOH 93 2093 2093 HOH HOH A . CA 6 HOH 94 2094 2094 HOH HOH A . CA 6 HOH 95 2095 2095 HOH HOH A . CA 6 HOH 96 2096 2096 HOH HOH A . CA 6 HOH 97 2097 2097 HOH HOH A . CA 6 HOH 98 2098 2098 HOH HOH A . CA 6 HOH 99 2099 2099 HOH HOH A . CA 6 HOH 100 2100 2100 HOH HOH A . CA 6 HOH 101 2101 2101 HOH HOH A . CA 6 HOH 102 2102 2102 HOH HOH A . CA 6 HOH 103 2103 2103 HOH HOH A . CA 6 HOH 104 2104 2104 HOH HOH A . CA 6 HOH 105 2105 2105 HOH HOH A . CA 6 HOH 106 2106 2106 HOH HOH A . CA 6 HOH 107 2107 2107 HOH HOH A . CA 6 HOH 108 2108 2108 HOH HOH A . CA 6 HOH 109 2109 2109 HOH HOH A . CA 6 HOH 110 2110 2110 HOH HOH A . CA 6 HOH 111 2111 2111 HOH HOH A . CA 6 HOH 112 2112 2112 HOH HOH A . CA 6 HOH 113 2113 2113 HOH HOH A . CA 6 HOH 114 2114 2114 HOH HOH A . CA 6 HOH 115 2115 2115 HOH HOH A . CA 6 HOH 116 2116 2116 HOH HOH A . CA 6 HOH 117 2117 2117 HOH HOH A . CA 6 HOH 118 2118 2118 HOH HOH A . CA 6 HOH 119 2119 2119 HOH HOH A . CA 6 HOH 120 2120 2120 HOH HOH A . CA 6 HOH 121 2121 2121 HOH HOH A . CA 6 HOH 122 2122 2122 HOH HOH A . CA 6 HOH 123 2123 2123 HOH HOH A . CA 6 HOH 124 2124 2124 HOH HOH A . CA 6 HOH 125 2125 2125 HOH HOH A . CA 6 HOH 126 2126 2126 HOH HOH A . CA 6 HOH 127 2127 2127 HOH HOH A . CA 6 HOH 128 2128 2128 HOH HOH A . CA 6 HOH 129 2129 2129 HOH HOH A . CA 6 HOH 130 2130 2130 HOH HOH A . CA 6 HOH 131 2131 2131 HOH HOH A . CA 6 HOH 132 2132 2132 HOH HOH A . CA 6 HOH 133 2133 2133 HOH HOH A . CA 6 HOH 134 2134 2134 HOH HOH A . CA 6 HOH 135 2135 2135 HOH HOH A . CA 6 HOH 136 2136 2136 HOH HOH A . CA 6 HOH 137 2137 2137 HOH HOH A . CA 6 HOH 138 2138 2138 HOH HOH A . CA 6 HOH 139 2139 2139 HOH HOH A . CA 6 HOH 140 2140 2140 HOH HOH A . CA 6 HOH 141 2141 2141 HOH HOH A . CA 6 HOH 142 2142 2142 HOH HOH A . CA 6 HOH 143 2143 2143 HOH HOH A . CA 6 HOH 144 2144 2144 HOH HOH A . CA 6 HOH 145 2145 2145 HOH HOH A . CA 6 HOH 146 2146 2146 HOH HOH A . CA 6 HOH 147 2147 2147 HOH HOH A . CA 6 HOH 148 2148 2148 HOH HOH A . CA 6 HOH 149 2149 2149 HOH HOH A . CA 6 HOH 150 2150 2150 HOH HOH A . CA 6 HOH 151 2151 2151 HOH HOH A . CA 6 HOH 152 2152 2152 HOH HOH A . CA 6 HOH 153 2153 2153 HOH HOH A . CA 6 HOH 154 2154 2154 HOH HOH A . CA 6 HOH 155 2155 2155 HOH HOH A . CA 6 HOH 156 2156 2156 HOH HOH A . CA 6 HOH 157 2157 2157 HOH HOH A . CA 6 HOH 158 2158 2158 HOH HOH A . CA 6 HOH 159 2159 2159 HOH HOH A . CA 6 HOH 160 2160 2160 HOH HOH A . CA 6 HOH 161 2161 2161 HOH HOH A . CA 6 HOH 162 2162 2162 HOH HOH A . CA 6 HOH 163 2163 2163 HOH HOH A . CA 6 HOH 164 2164 2164 HOH HOH A . CA 6 HOH 165 2165 2165 HOH HOH A . CA 6 HOH 166 2166 2166 HOH HOH A . CA 6 HOH 167 2167 2167 HOH HOH A . CA 6 HOH 168 2168 2168 HOH HOH A . CA 6 HOH 169 2169 2169 HOH HOH A . CA 6 HOH 170 2170 2170 HOH HOH A . CA 6 HOH 171 2171 2171 HOH HOH A . CA 6 HOH 172 2172 2172 HOH HOH A . CA 6 HOH 173 2173 2173 HOH HOH A . CA 6 HOH 174 2174 2174 HOH HOH A . CA 6 HOH 175 2175 2175 HOH HOH A . CA 6 HOH 176 2176 2176 HOH HOH A . CA 6 HOH 177 2177 2177 HOH HOH A . CA 6 HOH 178 2178 2178 HOH HOH A . CA 6 HOH 179 2179 2179 HOH HOH A . CA 6 HOH 180 2180 2180 HOH HOH A . CA 6 HOH 181 2181 2181 HOH HOH A . CA 6 HOH 182 2182 2182 HOH HOH A . CA 6 HOH 183 2183 2183 HOH HOH A . CA 6 HOH 184 2184 2184 HOH HOH A . CA 6 HOH 185 2185 2185 HOH HOH A . CA 6 HOH 186 2186 2186 HOH HOH A . CA 6 HOH 187 2187 2187 HOH HOH A . CA 6 HOH 188 2188 2188 HOH HOH A . CA 6 HOH 189 2189 2189 HOH HOH A . CA 6 HOH 190 2190 2190 HOH HOH A . CA 6 HOH 191 2191 2191 HOH HOH A . CA 6 HOH 192 2192 2192 HOH HOH A . CA 6 HOH 193 2193 2193 HOH HOH A . CA 6 HOH 194 2194 2194 HOH HOH A . CA 6 HOH 195 2195 2195 HOH HOH A . CA 6 HOH 196 2196 2196 HOH HOH A . CA 6 HOH 197 2197 2197 HOH HOH A . CA 6 HOH 198 2198 2198 HOH HOH A . CA 6 HOH 199 2199 2199 HOH HOH A . CA 6 HOH 200 2200 2200 HOH HOH A . CA 6 HOH 201 2201 2201 HOH HOH A . CA 6 HOH 202 2202 2202 HOH HOH A . CA 6 HOH 203 2203 2203 HOH HOH A . CA 6 HOH 204 2204 2204 HOH HOH A . CA 6 HOH 205 2205 2205 HOH HOH A . CA 6 HOH 206 2206 2206 HOH HOH A . CA 6 HOH 207 2207 2207 HOH HOH A . CA 6 HOH 208 2208 2208 HOH HOH A . CA 6 HOH 209 2209 2209 HOH HOH A . CA 6 HOH 210 2210 2210 HOH HOH A . CA 6 HOH 211 2211 2211 HOH HOH A . CA 6 HOH 212 2212 2212 HOH HOH A . CA 6 HOH 213 2213 2213 HOH HOH A . CA 6 HOH 214 2214 2214 HOH HOH A . CA 6 HOH 215 2215 2215 HOH HOH A . CA 6 HOH 216 2216 2216 HOH HOH A . CA 6 HOH 217 2217 2217 HOH HOH A . CA 6 HOH 218 2218 2218 HOH HOH A . CA 6 HOH 219 2219 2219 HOH HOH A . CA 6 HOH 220 2220 2220 HOH HOH A . CA 6 HOH 221 2221 2221 HOH HOH A . CA 6 HOH 222 2222 2222 HOH HOH A . CA 6 HOH 223 2223 2223 HOH HOH A . CA 6 HOH 224 2224 2224 HOH HOH A . CA 6 HOH 225 2225 2225 HOH HOH A . CA 6 HOH 226 2226 2226 HOH HOH A . CA 6 HOH 227 2227 2227 HOH HOH A . CA 6 HOH 228 2228 2228 HOH HOH A . CA 6 HOH 229 2229 2229 HOH HOH A . CA 6 HOH 230 2230 2230 HOH HOH A . CA 6 HOH 231 2231 2231 HOH HOH A . CA 6 HOH 232 2232 2232 HOH HOH A . CA 6 HOH 233 2233 2233 HOH HOH A . DA 6 HOH 1 2001 2001 HOH HOH B . DA 6 HOH 2 2002 2002 HOH HOH B . DA 6 HOH 3 2003 2003 HOH HOH B . DA 6 HOH 4 2004 2004 HOH HOH B . DA 6 HOH 5 2005 2005 HOH HOH B . DA 6 HOH 6 2006 2006 HOH HOH B . DA 6 HOH 7 2007 2007 HOH HOH B . DA 6 HOH 8 2008 2008 HOH HOH B . DA 6 HOH 9 2009 2009 HOH HOH B . DA 6 HOH 10 2010 2010 HOH HOH B . DA 6 HOH 11 2011 2011 HOH HOH B . DA 6 HOH 12 2012 2012 HOH HOH B . DA 6 HOH 13 2013 2013 HOH HOH B . DA 6 HOH 14 2014 2014 HOH HOH B . DA 6 HOH 15 2015 2015 HOH HOH B . DA 6 HOH 16 2016 2016 HOH HOH B . DA 6 HOH 17 2017 2017 HOH HOH B . DA 6 HOH 18 2018 2018 HOH HOH B . DA 6 HOH 19 2019 2019 HOH HOH B . DA 6 HOH 20 2020 2020 HOH HOH B . DA 6 HOH 21 2021 2021 HOH HOH B . DA 6 HOH 22 2022 2022 HOH HOH B . DA 6 HOH 23 2023 2023 HOH HOH B . DA 6 HOH 24 2024 2024 HOH HOH B . DA 6 HOH 25 2025 2025 HOH HOH B . DA 6 HOH 26 2026 2026 HOH HOH B . DA 6 HOH 27 2027 2027 HOH HOH B . DA 6 HOH 28 2028 2028 HOH HOH B . DA 6 HOH 29 2029 2029 HOH HOH B . DA 6 HOH 30 2030 2030 HOH HOH B . DA 6 HOH 31 2031 2031 HOH HOH B . DA 6 HOH 32 2032 2032 HOH HOH B . DA 6 HOH 33 2033 2033 HOH HOH B . DA 6 HOH 34 2034 2034 HOH HOH B . DA 6 HOH 35 2035 2035 HOH HOH B . DA 6 HOH 36 2036 2036 HOH HOH B . DA 6 HOH 37 2037 2037 HOH HOH B . DA 6 HOH 38 2038 2038 HOH HOH B . DA 6 HOH 39 2039 2039 HOH HOH B . DA 6 HOH 40 2040 2040 HOH HOH B . DA 6 HOH 41 2041 2041 HOH HOH B . DA 6 HOH 42 2042 2042 HOH HOH B . DA 6 HOH 43 2043 2043 HOH HOH B . DA 6 HOH 44 2044 2044 HOH HOH B . DA 6 HOH 45 2045 2045 HOH HOH B . DA 6 HOH 46 2046 2046 HOH HOH B . DA 6 HOH 47 2047 2047 HOH HOH B . DA 6 HOH 48 2048 2048 HOH HOH B . DA 6 HOH 49 2049 2049 HOH HOH B . DA 6 HOH 50 2050 2050 HOH HOH B . DA 6 HOH 51 2051 2051 HOH HOH B . DA 6 HOH 52 2052 2052 HOH HOH B . DA 6 HOH 53 2053 2053 HOH HOH B . DA 6 HOH 54 2054 2054 HOH HOH B . DA 6 HOH 55 2055 2055 HOH HOH B . DA 6 HOH 56 2056 2056 HOH HOH B . DA 6 HOH 57 2057 2057 HOH HOH B . DA 6 HOH 58 2058 2058 HOH HOH B . DA 6 HOH 59 2059 2059 HOH HOH B . DA 6 HOH 60 2060 2060 HOH HOH B . DA 6 HOH 61 2061 2061 HOH HOH B . DA 6 HOH 62 2062 2062 HOH HOH B . DA 6 HOH 63 2063 2063 HOH HOH B . DA 6 HOH 64 2064 2064 HOH HOH B . DA 6 HOH 65 2065 2065 HOH HOH B . DA 6 HOH 66 2066 2066 HOH HOH B . DA 6 HOH 67 2067 2067 HOH HOH B . DA 6 HOH 68 2068 2068 HOH HOH B . DA 6 HOH 69 2069 2069 HOH HOH B . DA 6 HOH 70 2070 2070 HOH HOH B . DA 6 HOH 71 2071 2071 HOH HOH B . DA 6 HOH 72 2072 2072 HOH HOH B . DA 6 HOH 73 2073 2073 HOH HOH B . DA 6 HOH 74 2074 2074 HOH HOH B . DA 6 HOH 75 2075 2075 HOH HOH B . DA 6 HOH 76 2076 2076 HOH HOH B . DA 6 HOH 77 2077 2077 HOH HOH B . DA 6 HOH 78 2078 2078 HOH HOH B . DA 6 HOH 79 2079 2079 HOH HOH B . DA 6 HOH 80 2080 2080 HOH HOH B . DA 6 HOH 81 2081 2081 HOH HOH B . DA 6 HOH 82 2082 2082 HOH HOH B . DA 6 HOH 83 2083 2083 HOH HOH B . DA 6 HOH 84 2084 2084 HOH HOH B . DA 6 HOH 85 2085 2085 HOH HOH B . DA 6 HOH 86 2086 2086 HOH HOH B . DA 6 HOH 87 2087 2087 HOH HOH B . DA 6 HOH 88 2088 2088 HOH HOH B . DA 6 HOH 89 2089 2089 HOH HOH B . DA 6 HOH 90 2090 2090 HOH HOH B . DA 6 HOH 91 2091 2091 HOH HOH B . DA 6 HOH 92 2092 2092 HOH HOH B . DA 6 HOH 93 2093 2093 HOH HOH B . DA 6 HOH 94 2094 2094 HOH HOH B . DA 6 HOH 95 2095 2095 HOH HOH B . DA 6 HOH 96 2096 2096 HOH HOH B . DA 6 HOH 97 2097 2097 HOH HOH B . DA 6 HOH 98 2098 2098 HOH HOH B . DA 6 HOH 99 2099 2099 HOH HOH B . DA 6 HOH 100 2100 2100 HOH HOH B . DA 6 HOH 101 2101 2101 HOH HOH B . DA 6 HOH 102 2102 2102 HOH HOH B . DA 6 HOH 103 2103 2103 HOH HOH B . DA 6 HOH 104 2104 2104 HOH HOH B . DA 6 HOH 105 2105 2105 HOH HOH B . DA 6 HOH 106 2106 2106 HOH HOH B . DA 6 HOH 107 2107 2107 HOH HOH B . DA 6 HOH 108 2108 2108 HOH HOH B . DA 6 HOH 109 2109 2109 HOH HOH B . DA 6 HOH 110 2110 2110 HOH HOH B . DA 6 HOH 111 2111 2111 HOH HOH B . DA 6 HOH 112 2112 2112 HOH HOH B . DA 6 HOH 113 2113 2113 HOH HOH B . DA 6 HOH 114 2114 2114 HOH HOH B . DA 6 HOH 115 2115 2115 HOH HOH B . DA 6 HOH 116 2116 2116 HOH HOH B . DA 6 HOH 117 2117 2117 HOH HOH B . DA 6 HOH 118 2118 2118 HOH HOH B . DA 6 HOH 119 2119 2119 HOH HOH B . DA 6 HOH 120 2120 2120 HOH HOH B . DA 6 HOH 121 2121 2121 HOH HOH B . DA 6 HOH 122 2122 2122 HOH HOH B . DA 6 HOH 123 2123 2123 HOH HOH B . DA 6 HOH 124 2124 2124 HOH HOH B . DA 6 HOH 125 2125 2125 HOH HOH B . DA 6 HOH 126 2126 2126 HOH HOH B . DA 6 HOH 127 2127 2127 HOH HOH B . DA 6 HOH 128 2128 2128 HOH HOH B . DA 6 HOH 129 2129 2129 HOH HOH B . DA 6 HOH 130 2130 2130 HOH HOH B . DA 6 HOH 131 2131 2131 HOH HOH B . DA 6 HOH 132 2132 2132 HOH HOH B . DA 6 HOH 133 2133 2133 HOH HOH B . DA 6 HOH 134 2134 2134 HOH HOH B . DA 6 HOH 135 2135 2135 HOH HOH B . DA 6 HOH 136 2136 2136 HOH HOH B . DA 6 HOH 137 2137 2137 HOH HOH B . DA 6 HOH 138 2138 2138 HOH HOH B . DA 6 HOH 139 2139 2139 HOH HOH B . DA 6 HOH 140 2140 2140 HOH HOH B . DA 6 HOH 141 2141 2141 HOH HOH B . DA 6 HOH 142 2142 2142 HOH HOH B . DA 6 HOH 143 2143 2143 HOH HOH B . DA 6 HOH 144 2144 2144 HOH HOH B . DA 6 HOH 145 2145 2145 HOH HOH B . DA 6 HOH 146 2146 2146 HOH HOH B . DA 6 HOH 147 2147 2147 HOH HOH B . DA 6 HOH 148 2148 2148 HOH HOH B . DA 6 HOH 149 2149 2149 HOH HOH B . DA 6 HOH 150 2150 2150 HOH HOH B . DA 6 HOH 151 2151 2151 HOH HOH B . DA 6 HOH 152 2152 2152 HOH HOH B . DA 6 HOH 153 2153 2153 HOH HOH B . DA 6 HOH 154 2154 2154 HOH HOH B . DA 6 HOH 155 2155 2155 HOH HOH B . DA 6 HOH 156 2156 2156 HOH HOH B . DA 6 HOH 157 2157 2157 HOH HOH B . DA 6 HOH 158 2158 2158 HOH HOH B . DA 6 HOH 159 2159 2159 HOH HOH B . DA 6 HOH 160 2160 2160 HOH HOH B . DA 6 HOH 161 2161 2161 HOH HOH B . DA 6 HOH 162 2162 2162 HOH HOH B . DA 6 HOH 163 2163 2163 HOH HOH B . DA 6 HOH 164 2164 2164 HOH HOH B . DA 6 HOH 165 2165 2165 HOH HOH B . DA 6 HOH 166 2166 2166 HOH HOH B . DA 6 HOH 167 2167 2167 HOH HOH B . DA 6 HOH 168 2168 2168 HOH HOH B . DA 6 HOH 169 2169 2169 HOH HOH B . DA 6 HOH 170 2170 2170 HOH HOH B . DA 6 HOH 171 2171 2171 HOH HOH B . DA 6 HOH 172 2172 2172 HOH HOH B . DA 6 HOH 173 2173 2173 HOH HOH B . DA 6 HOH 174 2174 2174 HOH HOH B . DA 6 HOH 175 2175 2175 HOH HOH B . DA 6 HOH 176 2176 2176 HOH HOH B . DA 6 HOH 177 2177 2177 HOH HOH B . DA 6 HOH 178 2178 2178 HOH HOH B . DA 6 HOH 179 2179 2179 HOH HOH B . DA 6 HOH 180 2180 2180 HOH HOH B . DA 6 HOH 181 2181 2181 HOH HOH B . DA 6 HOH 182 2182 2182 HOH HOH B . DA 6 HOH 183 2183 2183 HOH HOH B . DA 6 HOH 184 2184 2184 HOH HOH B . DA 6 HOH 185 2185 2185 HOH HOH B . DA 6 HOH 186 2186 2186 HOH HOH B . DA 6 HOH 187 2187 2187 HOH HOH B . DA 6 HOH 188 2188 2188 HOH HOH B . DA 6 HOH 189 2189 2189 HOH HOH B . DA 6 HOH 190 2190 2190 HOH HOH B . DA 6 HOH 191 2191 2191 HOH HOH B . DA 6 HOH 192 2192 2192 HOH HOH B . DA 6 HOH 193 2193 2193 HOH HOH B . DA 6 HOH 194 2194 2194 HOH HOH B . DA 6 HOH 195 2195 2195 HOH HOH B . DA 6 HOH 196 2196 2196 HOH HOH B . DA 6 HOH 197 2197 2197 HOH HOH B . DA 6 HOH 198 2198 2198 HOH HOH B . DA 6 HOH 199 2199 2199 HOH HOH B . DA 6 HOH 200 2200 2200 HOH HOH B . DA 6 HOH 201 2201 2201 HOH HOH B . DA 6 HOH 202 2202 2202 HOH HOH B . DA 6 HOH 203 2203 2203 HOH HOH B . DA 6 HOH 204 2204 2204 HOH HOH B . DA 6 HOH 205 2205 2205 HOH HOH B . DA 6 HOH 206 2206 2206 HOH HOH B . DA 6 HOH 207 2207 2207 HOH HOH B . DA 6 HOH 208 2208 2208 HOH HOH B . DA 6 HOH 209 2209 2209 HOH HOH B . DA 6 HOH 210 2210 2210 HOH HOH B . DA 6 HOH 211 2211 2211 HOH HOH B . DA 6 HOH 212 2212 2212 HOH HOH B . DA 6 HOH 213 2213 2213 HOH HOH B . DA 6 HOH 214 2214 2214 HOH HOH B . DA 6 HOH 215 2215 2215 HOH HOH B . DA 6 HOH 216 2216 2216 HOH HOH B . DA 6 HOH 217 2217 2217 HOH HOH B . DA 6 HOH 218 2218 2218 HOH HOH B . DA 6 HOH 219 2219 2219 HOH HOH B . DA 6 HOH 220 2220 2220 HOH HOH B . DA 6 HOH 221 2221 2221 HOH HOH B . DA 6 HOH 222 2222 2222 HOH HOH B . DA 6 HOH 223 2223 2223 HOH HOH B . DA 6 HOH 224 2224 2224 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 91 A ASN 91 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 110 A ASN 110 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 184 A ASN 184 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 91 B ASN 91 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 110 B ASN 110 ? ASN 'GLYCOSYLATION SITE' 6 B ASN 184 B ASN 184 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA monomeric 1 2 author_and_software_defined_assembly PISA monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,CA 2 1 B,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,DA # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? CA HOH . ? A HOH 2002 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 O ? CA HOH . ? A HOH 2058 ? 1_555 83.1 ? 2 O ? CA HOH . ? A HOH 2002 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD1 ? A ASP 45 ? A ASP 45 ? 1_555 81.3 ? 3 O ? CA HOH . ? A HOH 2058 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD1 ? A ASP 45 ? A ASP 45 ? 1_555 82.6 ? 4 O ? CA HOH . ? A HOH 2002 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 ND1 ? A HIS 58 ? A HIS 58 ? 1_555 164.9 ? 5 O ? CA HOH . ? A HOH 2058 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 ND1 ? A HIS 58 ? A HIS 58 ? 1_555 85.8 ? 6 OD1 ? A ASP 45 ? A ASP 45 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 ND1 ? A HIS 58 ? A HIS 58 ? 1_555 87.2 ? 7 O ? CA HOH . ? A HOH 2002 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 100.4 ? 8 O ? CA HOH . ? A HOH 2058 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 167.6 ? 9 OD1 ? A ASP 45 ? A ASP 45 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 86.2 ? 10 ND1 ? A HIS 58 ? A HIS 58 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 88.4 ? 11 O ? CA HOH . ? A HOH 2002 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD2 ? A ASP 124 ? A ASP 124 ? 1_555 99.1 ? 12 O ? CA HOH . ? A HOH 2058 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD2 ? A ASP 124 ? A ASP 124 ? 1_555 103.1 ? 13 OD1 ? A ASP 45 ? A ASP 45 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD2 ? A ASP 124 ? A ASP 124 ? 1_555 174.3 ? 14 ND1 ? A HIS 58 ? A HIS 58 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD2 ? A ASP 124 ? A ASP 124 ? 1_555 93.3 ? 15 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? L ZN . ? A ZN 431 ? 1_555 OD2 ? A ASP 124 ? A ASP 124 ? 1_555 88.1 ? 16 NE2 ? A HIS 154 ? A HIS 154 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD2 ? A ASP 158 ? A ASP 158 ? 1_555 88.6 ? 17 NE2 ? A HIS 154 ? A HIS 154 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 NE2 ? A HIS 130 ? A HIS 130 ? 1_555 104.3 ? 18 OD2 ? A ASP 158 ? A ASP 158 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 NE2 ? A HIS 130 ? A HIS 130 ? 1_555 147.4 ? 19 NE2 ? A HIS 154 ? A HIS 154 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2001 ? 1_555 166.4 ? 20 OD2 ? A ASP 158 ? A ASP 158 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2001 ? 1_555 86.5 ? 21 NE2 ? A HIS 130 ? A HIS 130 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2001 ? 1_555 86.5 ? 22 NE2 ? A HIS 154 ? A HIS 154 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2132 ? 1_555 94.5 ? 23 OD2 ? A ASP 158 ? A ASP 158 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2132 ? 1_555 110.5 ? 24 NE2 ? A HIS 130 ? A HIS 130 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2132 ? 1_555 98.4 ? 25 O ? CA HOH . ? A HOH 2001 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 O ? CA HOH . ? A HOH 2132 ? 1_555 75.4 ? 26 NE2 ? A HIS 154 ? A HIS 154 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD1 ? A ASP 158 ? A ASP 158 ? 1_555 96.1 ? 27 OD2 ? A ASP 158 ? A ASP 158 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD1 ? A ASP 158 ? A ASP 158 ? 1_555 53.4 ? 28 NE2 ? A HIS 130 ? A HIS 130 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD1 ? A ASP 158 ? A ASP 158 ? 1_555 94.9 ? 29 O ? CA HOH . ? A HOH 2001 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD1 ? A ASP 158 ? A ASP 158 ? 1_555 91.2 ? 30 O ? CA HOH . ? A HOH 2132 ? 1_555 ZN ? M ZN . ? A ZN 432 ? 1_555 OD1 ? A ASP 158 ? A ASP 158 ? 1_555 160.4 ? 31 O ? A TRP 1 ? A TRP 1 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 OD1 ? A ASP 124 ? A ASP 124 ? 1_555 164.2 ? 32 O ? A TRP 1 ? A TRP 1 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 89.7 ? 33 OD1 ? A ASP 124 ? A ASP 124 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 91.5 ? 34 O ? A TRP 1 ? A TRP 1 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 O ? CA HOH . ? A HOH 2002 ? 1_555 90.2 ? 35 OD1 ? A ASP 124 ? A ASP 124 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 O ? CA HOH . ? A HOH 2002 ? 1_555 102.5 ? 36 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 ZN ? N ZN . ? A ZN 433 ? 1_555 O ? CA HOH . ? A HOH 2002 ? 1_555 121.3 ? 37 O ? DA HOH . ? B HOH 2043 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 OD2 ? B ASP 124 ? B ASP 124 ? 1_555 102.8 ? 38 O ? DA HOH . ? B HOH 2043 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 166.6 ? 39 OD2 ? B ASP 124 ? B ASP 124 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 89.1 ? 40 O ? DA HOH . ? B HOH 2043 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 ND1 ? B HIS 58 ? B HIS 58 ? 1_555 84.4 ? 41 OD2 ? B ASP 124 ? B ASP 124 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 ND1 ? B HIS 58 ? B HIS 58 ? 1_555 96.3 ? 42 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 ND1 ? B HIS 58 ? B HIS 58 ? 1_555 88.1 ? 43 O ? DA HOH . ? B HOH 2043 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 OD1 ? B ASP 45 ? B ASP 45 ? 1_555 83.6 ? 44 OD2 ? B ASP 124 ? B ASP 124 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 OD1 ? B ASP 45 ? B ASP 45 ? 1_555 172.9 ? 45 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 OD1 ? B ASP 45 ? B ASP 45 ? 1_555 85.0 ? 46 ND1 ? B HIS 58 ? B HIS 58 ? 1_555 ZN ? Z ZN . ? B ZN 431 ? 1_555 OD1 ? B ASP 45 ? B ASP 45 ? 1_555 87.5 ? 47 NE2 ? B HIS 154 ? B HIS 154 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 NE2 ? B HIS 130 ? B HIS 130 ? 1_555 96.7 ? 48 NE2 ? B HIS 154 ? B HIS 154 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 O ? DA HOH . ? B HOH 2118 ? 1_555 86.8 ? 49 NE2 ? B HIS 130 ? B HIS 130 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 O ? DA HOH . ? B HOH 2118 ? 1_555 97.0 ? 50 NE2 ? B HIS 154 ? B HIS 154 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 O ? DA HOH . ? B HOH 2001 ? 1_555 168.7 ? 51 NE2 ? B HIS 130 ? B HIS 130 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 O ? DA HOH . ? B HOH 2001 ? 1_555 93.8 ? 52 O ? DA HOH . ? B HOH 2118 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 O ? DA HOH . ? B HOH 2001 ? 1_555 87.7 ? 53 NE2 ? B HIS 154 ? B HIS 154 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 90.6 ? 54 NE2 ? B HIS 130 ? B HIS 130 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 153.9 ? 55 O ? DA HOH . ? B HOH 2118 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 108.4 ? 56 O ? DA HOH . ? B HOH 2001 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 81.8 ? 57 NE2 ? B HIS 154 ? B HIS 154 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD1 ? B ASP 158 ? B ASP 158 ? 1_555 99.5 ? 58 NE2 ? B HIS 130 ? B HIS 130 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD1 ? B ASP 158 ? B ASP 158 ? 1_555 99.2 ? 59 O ? DA HOH . ? B HOH 2118 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD1 ? B ASP 158 ? B ASP 158 ? 1_555 161.8 ? 60 O ? DA HOH . ? B HOH 2001 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD1 ? B ASP 158 ? B ASP 158 ? 1_555 83.0 ? 61 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 ZN ? AA ZN . ? B ZN 432 ? 1_555 OD1 ? B ASP 158 ? B ASP 158 ? 1_555 54.9 ? 62 O ? B TRP 1 ? B TRP 1 ? 1_555 ZN ? BA ZN . ? B ZN 433 ? 1_555 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 90.0 ? 63 O ? B TRP 1 ? B TRP 1 ? 1_555 ZN ? BA ZN . ? B ZN 433 ? 1_555 OD1 ? B ASP 124 ? B ASP 124 ? 1_555 158.1 ? 64 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 ZN ? BA ZN . ? B ZN 433 ? 1_555 OD1 ? B ASP 124 ? B ASP 124 ? 1_555 98.9 ? # 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 2014-07-23 2 'Structure model' 1 1 2015-01-28 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0029 ? 1 HKL-2000 'data reduction' . ? 2 HKL-2000 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CWM _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ;ALPHA-D-MANNOSE (MAN): PART OF N-GLYCANS ZINC ION (ZN2): PART OF THE TRINUCLEAR ACTIVE SITE N-ACETYL-D-GLUCOSAMINE (NAG): PART OF N-GLYCANS ; _pdbx_entry_details.sequence_details ? # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O2 A MAN 304 ? ? O A HOH 2217 ? ? 2.02 2 1 O B GLU 175 ? ? OD2 B ASP 179 ? ? 2.06 3 1 O A HOH 2086 ? ? O A HOH 2161 ? ? 2.07 4 1 O6 A MAN 305 ? ? O A HOH 2220 ? ? 2.12 5 1 O A HOH 2091 ? ? O A HOH 2092 ? ? 2.16 6 1 OH B TYR 59 ? ? O B HOH 2067 ? ? 2.18 7 1 OG1 A THR 141 ? ? O A HOH 2140 ? ? 2.19 8 1 O B HOH 2047 ? ? O B HOH 2117 ? ? 2.19 # 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 TYR A 147 ? ? 46.30 -115.97 2 1 SER A 159 ? ? -133.68 -55.19 3 1 TYR A 170 ? ? -148.33 28.66 4 1 ASN A 171 ? ? 35.34 50.41 5 1 TRP A 220 ? ? -132.20 -41.71 6 1 GLU A 232 ? ? -138.11 -147.95 7 1 TYR B 147 ? ? 47.51 -110.67 8 1 SER B 159 ? ? -136.62 -46.83 9 1 TRP B 220 ? ? -132.25 -42.19 10 1 GLU B 232 ? ? -137.44 -139.71 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2048 ? 5.90 . 2 1 O ? A HOH 2067 ? 6.68 . 3 1 O ? A HOH 2069 ? 6.97 . 4 1 O ? A HOH 2073 ? 6.08 . 5 1 O ? A HOH 2102 ? 6.41 . 6 1 O ? A HOH 2120 ? . 7.39 7 1 O ? A HOH 2129 ? . 6.14 8 1 O ? A HOH 2131 ? . 5.81 9 1 O ? B HOH 2064 ? 6.21 . 10 1 O ? B HOH 2086 ? 6.52 . 11 1 O ? B HOH 2114 ? . 6.59 12 1 O ? B HOH 2213 ? . 5.90 13 1 O ? B HOH 2214 ? 6.05 . 14 1 O ? B HOH 2216 ? . 6.98 15 1 O ? B HOH 2218 ? 6.15 . 16 1 O ? B HOH 2219 ? 7.21 . 17 1 O ? B HOH 2221 ? 6.52 . 18 1 O ? B HOH 2223 ? 6.80 . 19 1 O ? B HOH 2224 ? 6.43 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A HIS 264 ? CA ? A HIS 264 CA 2 1 Y 1 A HIS 264 ? C ? A HIS 264 C 3 1 Y 1 A HIS 264 ? O ? A HIS 264 O 4 1 Y 1 A HIS 264 ? CB ? A HIS 264 CB 5 1 Y 1 A HIS 264 ? CG ? A HIS 264 CG 6 1 Y 1 A HIS 264 ? ND1 ? A HIS 264 ND1 7 1 Y 1 A HIS 264 ? CD2 ? A HIS 264 CD2 8 1 Y 1 A HIS 264 ? CE1 ? A HIS 264 CE1 9 1 Y 1 A HIS 264 ? NE2 ? A HIS 264 NE2 10 1 Y 1 B HIS 264 ? CA ? B HIS 264 CA 11 1 Y 1 B HIS 264 ? C ? B HIS 264 C 12 1 Y 1 B HIS 264 ? O ? B HIS 264 O 13 1 Y 1 B HIS 264 ? CB ? B HIS 264 CB 14 1 Y 1 B HIS 264 ? CG ? B HIS 264 CG 15 1 Y 1 B HIS 264 ? ND1 ? B HIS 264 ND1 16 1 Y 1 B HIS 264 ? CD2 ? B HIS 264 CD2 17 1 Y 1 B HIS 264 ? CE1 ? B HIS 264 CE1 18 1 Y 1 B HIS 264 ? NE2 ? B HIS 264 NE2 # 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 THR 101 ? A THR 101 2 1 Y 1 A ALA 102 ? A ALA 102 3 1 Y 1 A ALA 103 ? A ALA 103 4 1 Y 1 A SER 104 ? A SER 104 5 1 Y 1 A SER 105 ? A SER 105 6 1 Y 1 A GLN 106 ? A GLN 106 7 1 Y 1 A LYS 202 ? A LYS 202 8 1 Y 1 A HIS 265 ? A HIS 265 9 1 Y 1 A HIS 266 ? A HIS 266 10 1 Y 1 A HIS 267 ? A HIS 267 11 1 Y 1 A HIS 268 ? A HIS 268 12 1 Y 1 A HIS 269 ? A HIS 269 13 1 Y 1 B THR 101 ? B THR 101 14 1 Y 1 B ALA 102 ? B ALA 102 15 1 Y 1 B ALA 103 ? B ALA 103 16 1 Y 1 B SER 104 ? B SER 104 17 1 Y 1 B SER 105 ? B SER 105 18 1 Y 1 B GLN 106 ? B GLN 106 19 1 Y 1 B LYS 202 ? B LYS 202 20 1 Y 1 B HIS 265 ? B HIS 265 21 1 Y 1 B HIS 266 ? B HIS 266 22 1 Y 1 B HIS 267 ? B HIS 267 23 1 Y 1 B HIS 268 ? B HIS 268 24 1 Y 1 B HIS 269 ? B HIS 269 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'ZINC ION' ZN 6 water HOH #