data_5HNS # _entry.id 5HNS # _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 5HNS WWPDB D_1000217397 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5HNS _pdbx_database_status.recvd_initial_deposition_date 2016-01-18 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Zhao, Y.' 1 'Ren, J.' 2 'Harlos, K.' 3 'Stuart, D.I.' 4 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country NE _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Febs Lett.' _citation.journal_id_ASTM FEBLAL _citation.journal_id_CSD 0165 _citation.journal_id_ISSN 0014-5793 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 590 _citation.language ? _citation.page_first 605 _citation.page_last 612 _citation.title 'Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.' _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1002/1873-3468.12089 _citation.pdbx_database_id_PubMed 26846330 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zhao, Y.' 1 primary 'Ren, J.' 2 primary 'Harlos, K.' 3 primary 'Stuart, D.I.' 4 # _cell.entry_id 5HNS _cell.length_a 87.890 _cell.length_b 115.910 _cell.length_c 147.400 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5HNS _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 # 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 'Niemann-Pick C1 protein' 27952.037 2 ? ? 'domain C, UNP residues 387-618' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 17 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 3 ? ? ? ? 5 non-polymer man 'THIOCYANATE ION' 58.082 4 ? ? ? ? 6 water nat water 18.015 44 ? ? ? ? # _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 ;ETGQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVT LQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFP WLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDTGTLE VLFQ ; _entity_poly.pdbx_seq_one_letter_code_can ;ETGQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVT LQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFP WLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDTGTLE VLFQ ; _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 GLU n 1 2 THR n 1 3 GLY n 1 4 GLN n 1 5 ALA n 1 6 ARG n 1 7 LEU n 1 8 GLU n 1 9 LYS n 1 10 GLU n 1 11 TYR n 1 12 PHE n 1 13 ASP n 1 14 GLN n 1 15 HIS n 1 16 PHE n 1 17 GLY n 1 18 PRO n 1 19 PHE n 1 20 PHE n 1 21 ARG n 1 22 THR n 1 23 GLU n 1 24 GLN n 1 25 LEU n 1 26 ILE n 1 27 ILE n 1 28 ARG n 1 29 ALA n 1 30 PRO n 1 31 LEU n 1 32 THR n 1 33 ASP n 1 34 LYS n 1 35 HIS n 1 36 ILE n 1 37 TYR n 1 38 GLN n 1 39 PRO n 1 40 TYR n 1 41 PRO n 1 42 SER n 1 43 GLY n 1 44 ALA n 1 45 ASP n 1 46 VAL n 1 47 PRO n 1 48 PHE n 1 49 GLY n 1 50 PRO n 1 51 PRO n 1 52 LEU n 1 53 ASP n 1 54 ILE n 1 55 GLN n 1 56 ILE n 1 57 LEU n 1 58 HIS n 1 59 GLN n 1 60 VAL n 1 61 LEU n 1 62 ASP n 1 63 LEU n 1 64 GLN n 1 65 ILE n 1 66 ALA n 1 67 ILE n 1 68 GLU n 1 69 ASN n 1 70 ILE n 1 71 THR n 1 72 ALA n 1 73 SER n 1 74 TYR n 1 75 ASP n 1 76 ASN n 1 77 GLU n 1 78 THR n 1 79 VAL n 1 80 THR n 1 81 LEU n 1 82 GLN n 1 83 ASP n 1 84 ILE n 1 85 CYS n 1 86 LEU n 1 87 ALA n 1 88 PRO n 1 89 LEU n 1 90 SER n 1 91 PRO n 1 92 TYR n 1 93 ASN n 1 94 THR n 1 95 ASN n 1 96 CYS n 1 97 THR n 1 98 ILE n 1 99 LEU n 1 100 SER n 1 101 VAL n 1 102 LEU n 1 103 ASN n 1 104 TYR n 1 105 PHE n 1 106 GLN n 1 107 ASN n 1 108 SER n 1 109 HIS n 1 110 SER n 1 111 VAL n 1 112 LEU n 1 113 ASP n 1 114 HIS n 1 115 LYS n 1 116 LYS n 1 117 GLY n 1 118 ASP n 1 119 ASP n 1 120 PHE n 1 121 PHE n 1 122 VAL n 1 123 TYR n 1 124 ALA n 1 125 ASP n 1 126 TYR n 1 127 HIS n 1 128 THR n 1 129 HIS n 1 130 PHE n 1 131 LEU n 1 132 TYR n 1 133 CYS n 1 134 VAL n 1 135 ARG n 1 136 ALA n 1 137 PRO n 1 138 ALA n 1 139 SER n 1 140 LEU n 1 141 ASN n 1 142 ASP n 1 143 THR n 1 144 SER n 1 145 LEU n 1 146 LEU n 1 147 HIS n 1 148 ASP n 1 149 PRO n 1 150 CYS n 1 151 LEU n 1 152 GLY n 1 153 THR n 1 154 PHE n 1 155 GLY n 1 156 GLY n 1 157 PRO n 1 158 VAL n 1 159 PHE n 1 160 PRO n 1 161 TRP n 1 162 LEU n 1 163 VAL n 1 164 LEU n 1 165 GLY n 1 166 GLY n 1 167 TYR n 1 168 ASP n 1 169 ASP n 1 170 GLN n 1 171 ASN n 1 172 TYR n 1 173 ASN n 1 174 ASN n 1 175 ALA n 1 176 THR n 1 177 ALA n 1 178 LEU n 1 179 VAL n 1 180 ILE n 1 181 THR n 1 182 PHE n 1 183 PRO n 1 184 VAL n 1 185 ASN n 1 186 ASN n 1 187 TYR n 1 188 TYR n 1 189 ASN n 1 190 ASP n 1 191 THR n 1 192 GLU n 1 193 LYS n 1 194 LEU n 1 195 GLN n 1 196 ARG n 1 197 ALA n 1 198 GLN n 1 199 ALA n 1 200 TRP n 1 201 GLU n 1 202 LYS n 1 203 GLU n 1 204 PHE n 1 205 ILE n 1 206 ASN n 1 207 PHE n 1 208 VAL n 1 209 LYS n 1 210 ASN n 1 211 TYR n 1 212 LYS n 1 213 ASN n 1 214 PRO n 1 215 ASN n 1 216 LEU n 1 217 THR n 1 218 ILE n 1 219 SER n 1 220 PHE n 1 221 THR n 1 222 ALA n 1 223 GLU n 1 224 ARG n 1 225 SER n 1 226 ILE n 1 227 GLU n 1 228 ASP n 1 229 GLU n 1 230 LEU n 1 231 ASN n 1 232 ARG n 1 233 GLU n 1 234 SER n 1 235 ASP n 1 236 THR n 1 237 GLY n 1 238 THR n 1 239 LEU n 1 240 GLU n 1 241 VAL n 1 242 LEU n 1 243 PHE n 1 244 GLN n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _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 _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 _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _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 1 1 sample 'Biological sequence' 1 244 Human ? NPC1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? Kidney ? ? ? ? ? HEK293S ? ? ? ? ? ? ? ? ? ? ? ? 2 2 sample ? ? ? ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? kidney ? ? ? ? ? HEK293S ? ? ? ? ? ? ? ? ? ? ? ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code NPC1_HUMAN _struct_ref.pdbx_db_accession O15118 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;QARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVTLQD ICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFPWLV LGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESD ; _struct_ref.pdbx_align_begin 387 # 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 5HNS A 4 ? 235 ? O15118 387 ? 618 ? 387 618 2 1 5HNS B 4 ? 235 ? O15118 387 ? 618 ? 387 618 # 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 5HNS GLU A 1 ? UNP O15118 ? ? 'expression tag' 384 1 1 5HNS THR A 2 ? UNP O15118 ? ? 'expression tag' 385 2 1 5HNS GLY A 3 ? UNP O15118 ? ? 'expression tag' 386 3 1 5HNS THR A 236 ? UNP O15118 ? ? 'expression tag' 619 4 1 5HNS GLY A 237 ? UNP O15118 ? ? 'expression tag' 620 5 1 5HNS THR A 238 ? UNP O15118 ? ? 'expression tag' 621 6 1 5HNS LEU A 239 ? UNP O15118 ? ? 'expression tag' 622 7 1 5HNS GLU A 240 ? UNP O15118 ? ? 'expression tag' 623 8 1 5HNS VAL A 241 ? UNP O15118 ? ? 'expression tag' 624 9 1 5HNS LEU A 242 ? UNP O15118 ? ? 'expression tag' 625 10 1 5HNS PHE A 243 ? UNP O15118 ? ? 'expression tag' 626 11 1 5HNS GLN A 244 ? UNP O15118 ? ? 'expression tag' 627 12 2 5HNS GLU B 1 ? UNP O15118 ? ? 'expression tag' 384 13 2 5HNS THR B 2 ? UNP O15118 ? ? 'expression tag' 385 14 2 5HNS GLY B 3 ? UNP O15118 ? ? 'expression tag' 386 15 2 5HNS THR B 236 ? UNP O15118 ? ? 'expression tag' 619 16 2 5HNS GLY B 237 ? UNP O15118 ? ? 'expression tag' 620 17 2 5HNS THR B 238 ? UNP O15118 ? ? 'expression tag' 621 18 2 5HNS LEU B 239 ? UNP O15118 ? ? 'expression tag' 622 19 2 5HNS GLU B 240 ? UNP O15118 ? ? 'expression tag' 623 20 2 5HNS VAL B 241 ? UNP O15118 ? ? 'expression tag' 624 21 2 5HNS LEU B 242 ? UNP O15118 ? ? 'expression tag' 625 22 2 5HNS PHE B 243 ? UNP O15118 ? ? 'expression tag' 626 23 2 5HNS GLN B 244 ? UNP O15118 ? ? 'expression tag' 627 24 # 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 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 SCN non-polymer . 'THIOCYANATE ION' ? 'C N S -1' 58.082 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5HNS _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.36 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 63.37 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 7.4 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '30% polyethylene glycol mono-ethyl Ether 2000 and 0.1 M potassium thiocyanate' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2015-07-18 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0675 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'DIAMOND BEAMLINE I04' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.0675 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline I04 _diffrn_source.pdbx_synchrotron_site Diamond # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5HNS _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.45 _reflns.d_resolution_low 70 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 28062 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 100 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 26.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 13.3 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high . _reflns_shell.d_res_low ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5HNS _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 26647 _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 70.03 _refine.ls_d_res_high 2.45 _refine.ls_percent_reflns_obs 99.96 _refine.ls_R_factor_obs 0.22474 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.22406 _refine.ls_R_factor_R_free 0.23816 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_free 1385 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.946 _refine.correlation_coeff_Fo_to_Fc_free 0.941 _refine.B_iso_mean 73.014 _refine.aniso_B[1][1] 1.07 _refine.aniso_B[2][2] -2.19 _refine.aniso_B[3][3] 1.12 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] -0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SAD _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 0.336 _refine.pdbx_overall_ESU_R_Free 0.228 _refine.overall_SU_ML 0.219 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 21.463 _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 3499 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 316 _refine_hist.number_atoms_solvent 44 _refine_hist.number_atoms_total 3859 _refine_hist.d_res_high 2.45 _refine_hist.d_res_low 70.03 # 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 0.008 0.020 ? 4040 'X-RAY DIFFRACTION' ? r_bond_other_d 0.003 0.020 ? 3536 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.519 2.028 ? 5559 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.100 3.000 ? 8202 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.220 5.000 ? 441 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 38.245 25.127 ? 197 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.615 15.000 ? 538 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.237 15.000 ? 8 'X-RAY DIFFRACTION' ? r_chiral_restr 0.083 0.200 ? 655 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 4462 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.003 0.020 ? 936 '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 2.201 5.732 ? 1768 'X-RAY DIFFRACTION' ? r_mcbond_other 2.192 5.720 ? 1763 'X-RAY DIFFRACTION' ? r_mcangle_it 3.965 8.571 ? 2205 'X-RAY DIFFRACTION' ? r_mcangle_other 3.964 8.574 ? 2206 'X-RAY DIFFRACTION' ? r_scbond_it 2.390 6.798 ? 2272 'X-RAY DIFFRACTION' ? r_scbond_other 2.387 6.792 ? 2268 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other 4.170 10.057 ? 3351 'X-RAY DIFFRACTION' ? r_long_range_B_refined 7.350 49.759 ? 4159 'X-RAY DIFFRACTION' ? r_long_range_B_other 7.339 49.723 ? 4148 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_restr_ncs.pdbx_refine_id _refine_ls_restr_ncs.dom_id _refine_ls_restr_ncs.pdbx_ens_id _refine_ls_restr_ncs.pdbx_ordinal _refine_ls_restr_ncs.ncs_model_details _refine_ls_restr_ncs.rms_dev_position _refine_ls_restr_ncs.weight_position _refine_ls_restr_ncs.rms_dev_B_iso _refine_ls_restr_ncs.weight_B_iso _refine_ls_restr_ncs.pdbx_auth_asym_id _refine_ls_restr_ncs.pdbx_number _refine_ls_restr_ncs.pdbx_type 'X-RAY DIFFRACTION' 1 1 1 ? 0.09 0.05 ? ? A 24186 'interatomic distance' 'X-RAY DIFFRACTION' 2 1 2 ? 0.09 0.05 ? ? B 24186 'interatomic distance' # _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 2.450 _refine_ls_shell.d_res_low 2.514 _refine_ls_shell.number_reflns_R_work 1921 _refine_ls_shell.R_factor_R_work 0.359 _refine_ls_shell.percent_reflns_obs 99.95 _refine_ls_shell.R_factor_R_free 0.356 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 115 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.number_reflns_obs ? # loop_ _struct_ncs_dom.id _struct_ncs_dom.details _struct_ncs_dom.pdbx_ens_id 1 A 1 2 B 1 # loop_ _struct_ncs_dom_lim.dom_id _struct_ncs_dom_lim.beg_auth_asym_id _struct_ncs_dom_lim.beg_auth_seq_id _struct_ncs_dom_lim.end_auth_asym_id _struct_ncs_dom_lim.end_auth_seq_id _struct_ncs_dom_lim.pdbx_component_id _struct_ncs_dom_lim.pdbx_refine_code _struct_ncs_dom_lim.beg_label_asym_id _struct_ncs_dom_lim.beg_label_comp_id _struct_ncs_dom_lim.beg_label_seq_id _struct_ncs_dom_lim.beg_label_alt_id _struct_ncs_dom_lim.end_label_asym_id _struct_ncs_dom_lim.end_label_comp_id _struct_ncs_dom_lim.end_label_seq_id _struct_ncs_dom_lim.end_label_alt_id _struct_ncs_dom_lim.pdbx_ens_id _struct_ncs_dom_lim.selection_details 1 A 392 A 605 0 0 ? ? ? ? ? ? ? ? 1 ? 2 B 392 B 605 0 0 ? ? ? ? ? ? ? ? 1 ? # _struct_ncs_ens.id 1 _struct_ncs_ens.details ? # _struct.entry_id 5HNS _struct.title 'Structure of glycosylated NPC1 luminal domain C' _struct.pdbx_descriptor 'Niemann-Pick C1 protein' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5HNS _struct_keywords.text 'Niemann-Pick disease type C, NPC1, NPC2, cholesterol transport, Ebola virus receptor, Ebola virus susceptibility, protein binding' _struct_keywords.pdbx_keywords 'PROTEIN 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 2 ? F N N 2 ? G N N 3 ? H N N 4 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 2 ? N N N 5 ? O N N 5 ? P N N 2 ? Q N N 2 ? R N N 2 ? S N N 2 ? T N N 2 ? U N N 2 ? V N N 3 ? W N N 4 ? X N N 4 ? Y N N 2 ? Z N N 2 ? AA N N 3 ? BA N N 5 ? CA N N 5 ? DA N N 6 ? EA N N 6 ? # 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 AA1 GLY A 49 ? LEU A 52 ? GLY A 432 LEU A 435 5 ? 4 HELX_P HELX_P2 AA2 ASP A 53 ? ASN A 69 ? ASP A 436 ASN A 452 1 ? 17 HELX_P HELX_P3 AA3 LEU A 81 ? CYS A 85 ? LEU A 464 CYS A 468 1 ? 5 HELX_P HELX_P4 AA4 SER A 100 ? GLN A 106 ? SER A 483 GLN A 489 5 ? 7 HELX_P HELX_P5 AA5 SER A 108 ? HIS A 114 ? SER A 491 HIS A 497 1 ? 7 HELX_P HELX_P6 AA6 ASP A 125 ? VAL A 134 ? ASP A 508 VAL A 517 1 ? 10 HELX_P HELX_P7 AA7 PHE A 159 ? VAL A 163 ? PHE A 542 VAL A 546 1 ? 5 HELX_P HELX_P8 AA8 ASN A 171 ? ALA A 175 ? ASN A 554 ALA A 558 5 ? 5 HELX_P HELX_P9 AA9 ASP A 190 ? TYR A 211 ? ASP A 573 TYR A 594 1 ? 22 HELX_P HELX_P10 AB1 TYR B 11 ? PHE B 16 ? TYR B 394 PHE B 399 1 ? 6 HELX_P HELX_P11 AB2 GLY B 49 ? LEU B 52 ? GLY B 432 LEU B 435 5 ? 4 HELX_P HELX_P12 AB3 ASP B 53 ? ASN B 69 ? ASP B 436 ASN B 452 1 ? 17 HELX_P HELX_P13 AB4 LEU B 81 ? CYS B 85 ? LEU B 464 CYS B 468 1 ? 5 HELX_P HELX_P14 AB5 SER B 100 ? GLN B 106 ? SER B 483 GLN B 489 5 ? 7 HELX_P HELX_P15 AB6 SER B 108 ? HIS B 114 ? SER B 491 HIS B 497 1 ? 7 HELX_P HELX_P16 AB7 ASP B 125 ? VAL B 134 ? ASP B 508 VAL B 517 1 ? 10 HELX_P HELX_P17 AB8 PHE B 159 ? VAL B 163 ? PHE B 542 VAL B 546 1 ? 5 HELX_P HELX_P18 AB9 ASN B 171 ? ALA B 175 ? ASN B 554 ALA B 558 5 ? 5 HELX_P HELX_P19 AC1 ASP B 190 ? TYR B 211 ? ASP B 573 TYR B 594 1 ? 22 # _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 85 SG ? ? ? 1_555 A CYS 96 SG ? ? A CYS 468 A CYS 479 1_555 ? ? ? ? ? ? ? 2.065 ? disulf2 disulf ? ? A CYS 133 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 516 A CYS 533 1_555 ? ? ? ? ? ? ? 2.070 ? disulf3 disulf ? ? B CYS 85 SG ? ? ? 1_555 B CYS 96 SG ? ? B CYS 468 B CYS 479 1_555 ? ? ? ? ? ? ? 2.087 ? disulf4 disulf ? ? B CYS 133 SG ? ? ? 1_555 B CYS 150 SG ? ? B CYS 516 B CYS 533 1_555 ? ? ? ? ? ? ? 2.067 ? covale1 covale one ? A ASN 95 ND2 A ? ? 1_555 L NAG . C1 ? ? A ASN 478 A NAG 710 1_555 ? ? ? ? ? ? ? 1.446 ? covale2 covale one ? A ASN 95 ND2 B ? ? 1_555 L NAG . C1 ? ? A ASN 478 A NAG 710 1_555 ? ? ? ? ? ? ? 1.440 ? covale3 covale one ? A ASN 141 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 524 A NAG 701 1_555 ? ? ? ? ? ? ? 1.442 ? covale4 covale one ? A ASN 174 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 557 A NAG 703 1_555 ? ? ? ? ? ? ? 1.425 ? covale5 covale one ? A ASN 189 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 572 A NAG 707 1_555 ? ? ? ? ? ? ? 1.456 ? covale6 covale one ? A ASN 215 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 598 A NAG 708 1_555 ? ? ? ? ? ? ? 1.447 ? covale7 covale one ? B ASN 95 ND2 A ? ? 1_555 P NAG . C1 ? ? B ASN 478 B NAG 701 1_555 ? ? ? ? ? ? ? 1.436 ? covale8 covale one ? B ASN 95 ND2 B ? ? 1_555 P NAG . C1 ? ? B ASN 478 B NAG 701 1_555 ? ? ? ? ? ? ? 1.444 ? covale9 covale one ? B ASN 141 ND2 ? ? ? 1_555 R NAG . C1 ? ? B ASN 524 B NAG 703 1_555 ? ? ? ? ? ? ? 1.449 ? covale10 covale one ? B ASN 174 ND2 ? ? ? 1_555 T NAG . C1 ? ? B ASN 557 B NAG 705 1_555 ? ? ? ? ? ? ? 1.431 ? covale11 covale one ? B ASN 215 ND2 ? ? ? 1_555 Y NAG . C1 ? ? B ASN 598 B NAG 710 1_555 ? ? ? ? ? ? ? 1.421 ? covale12 covale both ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 701 A NAG 702 1_555 ? ? ? ? ? ? ? 1.455 ? covale13 covale both ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 703 A NAG 704 1_555 ? ? ? ? ? ? ? 1.449 ? covale14 covale both ? F NAG . O4 ? ? ? 1_555 G BMA . C1 ? ? A NAG 704 A BMA 705 1_555 ? ? ? ? ? ? ? 1.464 ? covale15 covale one ? G BMA . O6 ? ? ? 1_555 H MAN . C1 ? ? A BMA 705 A MAN 706 1_555 ? ? ? ? ? ? ? 1.452 ? covale16 covale both ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 708 A NAG 709 1_555 ? ? ? ? ? ? ? 1.457 ? covale17 covale both ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 710 A NAG 711 1_555 ? ? ? ? ? ? ? 1.446 ? covale18 covale both ? P NAG . O4 ? ? ? 1_555 Q NAG . C1 ? ? B NAG 701 B NAG 702 1_555 ? ? ? ? ? ? ? 1.448 ? covale19 covale both ? R NAG . O4 ? ? ? 1_555 S NAG . C1 ? ? B NAG 703 B NAG 704 1_555 ? ? ? ? ? ? ? 1.460 ? covale20 covale both ? T NAG . O4 ? ? ? 1_555 U NAG . C1 ? ? B NAG 705 B NAG 706 1_555 ? ? ? ? ? ? ? 1.434 ? covale21 covale both ? U NAG . O4 ? ? ? 1_555 V BMA . C1 ? ? B NAG 706 B BMA 707 1_555 ? ? ? ? ? ? ? 1.435 ? covale22 covale one ? V BMA . O3 ? ? ? 1_555 W MAN . C1 ? ? B BMA 707 B MAN 708 1_555 ? ? ? ? ? ? ? 1.441 ? covale23 covale one ? V BMA . O6 ? ? ? 1_555 X MAN . C1 ? ? B BMA 707 B MAN 709 1_555 ? ? ? ? ? ? ? 1.446 ? covale24 covale both ? Y NAG . O4 ? ? ? 1_555 Z NAG . C1 ? ? B NAG 710 B NAG 711 1_555 ? ? ? ? ? ? ? 1.432 ? covale25 covale both ? Z NAG . O4 ? ? ? 1_555 AA BMA . C1 ? ? B NAG 711 B BMA 712 1_555 ? ? ? ? ? ? ? 1.455 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 TYR 40 A . ? TYR 423 A PRO 41 A ? PRO 424 A 1 -2.89 2 TYR 40 B . ? TYR 423 B PRO 41 B ? PRO 424 B 1 -2.42 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 4 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 2 ? AA5 ? 4 ? AA6 ? 2 ? AA7 ? 2 ? AA8 ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? anti-parallel AA5 2 3 ? anti-parallel AA5 3 4 ? anti-parallel AA6 1 2 ? anti-parallel AA7 1 2 ? anti-parallel AA8 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 LEU A 164 ? GLY A 165 ? LEU A 547 GLY A 548 AA1 2 ALA A 177 ? ASN A 185 ? ALA A 560 ASN A 568 AA1 3 PHE A 20 ? ARG A 28 ? PHE A 403 ARG A 411 AA1 4 THR A 217 ? PHE A 220 ? THR A 600 PHE A 603 AA2 1 HIS A 35 ? TYR A 37 ? HIS A 418 TYR A 420 AA2 2 VAL A 46 ? PHE A 48 ? VAL A 429 PHE A 431 AA3 1 THR A 71 ? TYR A 74 ? THR A 454 TYR A 457 AA3 2 GLU A 77 ? THR A 80 ? GLU A 460 THR A 463 AA4 1 LYS A 116 ? GLY A 117 ? LYS A 499 GLY A 500 AA4 2 VAL A 122 ? ALA A 124 ? VAL A 505 ALA A 507 AA5 1 LEU B 164 ? GLY B 165 ? LEU B 547 GLY B 548 AA5 2 ALA B 177 ? ASN B 185 ? ALA B 560 ASN B 568 AA5 3 PHE B 20 ? ARG B 28 ? PHE B 403 ARG B 411 AA5 4 THR B 217 ? PHE B 220 ? THR B 600 PHE B 603 AA6 1 HIS B 35 ? TYR B 37 ? HIS B 418 TYR B 420 AA6 2 VAL B 46 ? PHE B 48 ? VAL B 429 PHE B 431 AA7 1 THR B 71 ? TYR B 74 ? THR B 454 TYR B 457 AA7 2 GLU B 77 ? THR B 80 ? GLU B 460 THR B 463 AA8 1 LYS B 116 ? GLY B 117 ? LYS B 499 GLY B 500 AA8 2 VAL B 122 ? ALA B 124 ? VAL B 505 ALA B 507 # 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 AA1 1 2 N GLY A 165 ? N GLY A 548 O ALA A 177 ? O ALA A 560 AA1 2 3 O VAL A 184 ? O VAL A 567 N ARG A 21 ? N ARG A 404 AA1 3 4 N ILE A 26 ? N ILE A 409 O SER A 219 ? O SER A 602 AA2 1 2 N HIS A 35 ? N HIS A 418 O PHE A 48 ? O PHE A 431 AA3 1 2 N ALA A 72 ? N ALA A 455 O VAL A 79 ? O VAL A 462 AA4 1 2 N LYS A 116 ? N LYS A 499 O TYR A 123 ? O TYR A 506 AA5 1 2 N GLY B 165 ? N GLY B 548 O ALA B 177 ? O ALA B 560 AA5 2 3 O VAL B 184 ? O VAL B 567 N ARG B 21 ? N ARG B 404 AA5 3 4 N ILE B 26 ? N ILE B 409 O SER B 219 ? O SER B 602 AA6 1 2 N HIS B 35 ? N HIS B 418 O PHE B 48 ? O PHE B 431 AA7 1 2 N ALA B 72 ? N ALA B 455 O VAL B 79 ? O VAL B 462 AA8 1 2 N LYS B 116 ? N LYS B 499 O TYR B 123 ? O TYR B 506 # 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 A SCN 712 ? 4 'binding site for residue SCN A 712' AC2 Software A SCN 713 ? 1 'binding site for residue SCN A 713' AC3 Software B SCN 713 ? 2 'binding site for residue SCN B 713' AC4 Software B SCN 714 ? 5 'binding site for residue SCN B 714' AC5 Software A ASN 478 ? 4 'binding site for Poly-Saccharide residues NAG A 710 through NAG A 711 bound to ASN A 478' AC6 Software A NAG 710 ? 5 'binding site for Mono-Saccharide NAG A 710 bound to ASN A 478' AC7 Software A ASN 524 ? 2 'binding site for Poly-Saccharide residues NAG A 701 through NAG A 702 bound to ASN A 524' AC8 Software A ASN 557 ? 6 'binding site for Poly-Saccharide residues NAG A 703 through MAN A 706 bound to ASN A 557' AC9 Software A NAG 707 ? 5 'binding site for Mono-Saccharide NAG A 707 bound to ASN A 572' AD1 Software A ASN 598 ? 5 'binding site for Poly-Saccharide residues NAG A 708 through NAG A 709 bound to ASN A 598' AD2 Software B ASN 478 ? 5 'binding site for Poly-Saccharide residues NAG B 701 through NAG B 702 bound to ASN B 478' AD3 Software B NAG 701 ? 6 'binding site for Mono-Saccharide NAG B 701 bound to ASN B 478' AD4 Software B ASN 524 ? 1 'binding site for Poly-Saccharide residues NAG B 703 through NAG B 704 bound to ASN B 524' AD5 Software B ASN 557 ? 7 'binding site for Poly-Saccharide residues NAG B 705 through MAN B 709 bound to ASN B 557' AD6 Software B ASN 598 ? 4 'binding site for Poly-Saccharide residues NAG B 710 through BMA B 712 bound to ASN B 598' # 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 4 CYS A 85 ? CYS A 468 . ? 1_555 ? 2 AC1 4 ALA A 87 ? ALA A 470 . ? 1_555 ? 3 AC1 4 SER A 90 ? SER A 473 . ? 1_555 ? 4 AC1 4 PRO A 91 ? PRO A 474 . ? 1_555 ? 5 AC2 1 TYR A 167 ? TYR A 550 . ? 1_555 ? 6 AC3 2 GLU B 8 ? GLU B 391 . ? 1_555 ? 7 AC3 2 GLY B 166 ? GLY B 549 . ? 1_555 ? 8 AC4 5 GLN B 82 ? GLN B 465 . ? 1_555 ? 9 AC4 5 ASP B 83 ? ASP B 466 . ? 1_555 ? 10 AC4 5 CYS B 85 ? CYS B 468 . ? 1_555 ? 11 AC4 5 TYR B 92 ? TYR B 475 . ? 1_555 ? 12 AC4 5 ASN B 185 ? ASN B 568 . ? 1_555 ? 13 AC5 4 LEU A 89 ? LEU A 472 . ? 1_555 ? 14 AC5 4 ASN A 93 ? ASN A 476 . ? 1_555 ? 15 AC5 4 ASN A 95 ? ASN A 478 . ? 1_555 ? 16 AC5 4 THR A 153 ? THR A 536 . ? 1_555 ? 17 AC6 5 LEU A 89 ? LEU A 472 . ? 1_555 ? 18 AC6 5 ASN A 93 ? ASN A 476 . ? 1_555 ? 19 AC6 5 ASN A 95 ? ASN A 478 . ? 1_555 ? 20 AC6 5 THR A 153 ? THR A 536 . ? 1_555 ? 21 AC6 5 NAG M . ? NAG A 711 . ? 1_555 ? 22 AC7 2 ASN A 141 ? ASN A 524 . ? 1_555 ? 23 AC7 2 HIS A 147 ? HIS A 530 . ? 1_555 ? 24 AC8 6 ALA A 44 ? ALA A 427 . ? 1_555 ? 25 AC8 6 ASP A 45 ? ASP A 428 . ? 1_555 ? 26 AC8 6 ASP A 168 ? ASP A 551 . ? 1_555 ? 27 AC8 6 ASN A 171 ? ASN A 554 . ? 1_555 ? 28 AC8 6 ASN A 173 ? ASN A 556 . ? 1_555 ? 29 AC8 6 ASN A 174 ? ASN A 557 . ? 1_555 ? 30 AC9 5 TYR A 188 ? TYR A 571 . ? 1_555 ? 31 AC9 5 ASN A 189 ? ASN A 572 . ? 1_555 ? 32 AC9 5 ASP A 190 ? ASP A 573 . ? 1_555 ? 33 AC9 5 ASP B 169 ? ASP B 552 . ? 1_555 ? 34 AC9 5 GLN B 170 ? GLN B 553 . ? 1_555 ? 35 AD1 5 GLN A 55 ? GLN A 438 . ? 1_555 ? 36 AD1 5 GLN A 59 ? GLN A 442 . ? 1_555 ? 37 AD1 5 ASN A 213 ? ASN A 596 . ? 1_555 ? 38 AD1 5 ASN A 215 ? ASN A 598 . ? 1_555 ? 39 AD1 5 BMA AA . ? BMA B 712 . ? 5_545 ? 40 AD2 5 LEU B 89 ? LEU B 472 . ? 1_555 ? 41 AD2 5 ASN B 93 ? ASN B 476 . ? 1_555 ? 42 AD2 5 ASN B 95 ? ASN B 478 . ? 1_555 ? 43 AD2 5 THR B 153 ? THR B 536 . ? 1_555 ? 44 AD2 5 HOH EA . ? HOH B 807 . ? 1_555 ? 45 AD3 6 LEU B 89 ? LEU B 472 . ? 1_555 ? 46 AD3 6 ASN B 93 ? ASN B 476 . ? 1_555 ? 47 AD3 6 ASN B 95 ? ASN B 478 . ? 1_555 ? 48 AD3 6 THR B 153 ? THR B 536 . ? 1_555 ? 49 AD3 6 NAG Q . ? NAG B 702 . ? 1_555 ? 50 AD3 6 HOH EA . ? HOH B 807 . ? 1_555 ? 51 AD4 1 ASN B 141 ? ASN B 524 . ? 1_555 ? 52 AD5 7 ALA B 44 ? ALA B 427 . ? 1_555 ? 53 AD5 7 ASP B 45 ? ASP B 428 . ? 1_555 ? 54 AD5 7 PRO B 47 ? PRO B 430 . ? 1_555 ? 55 AD5 7 ASN B 171 ? ASN B 554 . ? 1_555 ? 56 AD5 7 ASN B 173 ? ASN B 556 . ? 1_555 ? 57 AD5 7 ASN B 174 ? ASN B 557 . ? 1_555 ? 58 AD5 7 HOH EA . ? HOH B 802 . ? 1_555 ? 59 AD6 4 NAG K . ? NAG A 709 . ? 5_455 ? 60 AD6 4 GLN B 55 ? GLN B 438 . ? 1_555 ? 61 AD6 4 GLN B 59 ? GLN B 442 . ? 1_555 ? 62 AD6 4 ASN B 215 ? ASN B 598 . ? 1_555 ? # _atom_sites.entry_id 5HNS _atom_sites.fract_transf_matrix[1][1] 0.011378 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.008627 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] -0.000000 _atom_sites.fract_transf_matrix[3][3] 0.006784 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CL N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LYS A 1 9 ? 73.394 24.401 72.751 1.00 167.69 ? 392 LYS A N 1 ATOM 2 C CA . LYS A 1 9 ? 72.675 24.416 74.067 1.00 167.41 ? 392 LYS A CA 1 ATOM 3 C C . LYS A 1 9 ? 72.629 25.823 74.650 1.00 170.63 ? 392 LYS A C 1 ATOM 4 O O . LYS A 1 9 ? 71.538 26.374 74.827 1.00 170.62 ? 392 LYS A O 1 ATOM 5 C CB . LYS A 1 9 ? 73.302 23.436 75.066 1.00 163.34 ? 392 LYS A CB 1 ATOM 6 C CG . LYS A 1 9 ? 72.935 21.983 74.797 1.00 163.42 ? 392 LYS A CG 1 ATOM 7 C CD . LYS A 1 9 ? 73.960 21.006 75.345 1.00 161.69 ? 392 LYS A CD 1 ATOM 8 C CE . LYS A 1 9 ? 73.778 19.620 74.743 1.00 161.29 ? 392 LYS A CE 1 ATOM 9 N NZ . LYS A 1 9 ? 74.995 18.784 74.918 1.00 160.55 ? 392 LYS A NZ 1 ATOM 10 N N . GLU A 1 10 ? 73.802 26.406 74.918 1.00 172.56 ? 393 GLU A N 1 ATOM 11 C CA . GLU A 1 10 ? 73.889 27.782 75.460 1.00 173.98 ? 393 GLU A CA 1 ATOM 12 C C . GLU A 1 10 ? 73.945 28.860 74.342 1.00 178.64 ? 393 GLU A C 1 ATOM 13 O O . GLU A 1 10 ? 73.783 30.044 74.637 1.00 178.02 ? 393 GLU A O 1 ATOM 14 C CB . GLU A 1 10 ? 75.000 27.952 76.543 1.00 171.18 ? 393 GLU A CB 1 ATOM 15 C CG . GLU A 1 10 ? 74.503 27.807 78.032 1.00 168.72 ? 393 GLU A CG 1 ATOM 16 C CD . GLU A 1 10 ? 73.492 28.851 78.506 1.00 167.57 ? 393 GLU A CD 1 ATOM 17 O OE1 . GLU A 1 10 ? 73.482 29.965 77.951 1.00 173.13 ? 393 GLU A OE1 1 ATOM 18 O OE2 . GLU A 1 10 ? 72.695 28.552 79.443 1.00 154.16 ? 393 GLU A OE2 1 ATOM 19 N N . TYR A 1 11 ? 74.113 28.464 73.071 1.00 183.54 ? 394 TYR A N 1 ATOM 20 C CA . TYR A 1 11 ? 73.990 29.397 71.928 1.00 185.73 ? 394 TYR A CA 1 ATOM 21 C C . TYR A 1 11 ? 72.656 30.162 71.911 1.00 189.26 ? 394 TYR A C 1 ATOM 22 O O . TYR A 1 11 ? 72.623 31.365 71.629 1.00 185.92 ? 394 TYR A O 1 ATOM 23 C CB . TYR A 1 11 ? 74.167 28.665 70.586 1.00 185.21 ? 394 TYR A CB 1 ATOM 24 C CG . TYR A 1 11 ? 74.098 29.621 69.409 1.00 184.00 ? 394 TYR A CG 1 ATOM 25 C CD1 . TYR A 1 11 ? 75.239 30.265 68.955 1.00 183.17 ? 394 TYR A CD1 1 ATOM 26 C CD2 . TYR A 1 11 ? 72.880 29.918 68.781 1.00 182.86 ? 394 TYR A CD2 1 ATOM 27 C CE1 . TYR A 1 11 ? 75.184 31.155 67.896 1.00 183.91 ? 394 TYR A CE1 1 ATOM 28 C CE2 . TYR A 1 11 ? 72.814 30.812 67.722 1.00 182.30 ? 394 TYR A CE2 1 ATOM 29 C CZ . TYR A 1 11 ? 73.971 31.425 67.282 1.00 183.91 ? 394 TYR A CZ 1 ATOM 30 O OH . TYR A 1 11 ? 73.919 32.308 66.231 1.00 186.63 ? 394 TYR A OH 1 ATOM 31 N N . PHE A 1 12 ? 71.573 29.449 72.215 1.00 192.17 ? 395 PHE A N 1 ATOM 32 C CA . PHE A 1 12 ? 70.207 29.981 72.124 1.00 189.40 ? 395 PHE A CA 1 ATOM 33 C C . PHE A 1 12 ? 69.908 31.032 73.203 1.00 185.14 ? 395 PHE A C 1 ATOM 34 O O . PHE A 1 12 ? 69.123 31.953 72.973 1.00 183.59 ? 395 PHE A O 1 ATOM 35 C CB . PHE A 1 12 ? 69.180 28.845 72.222 1.00 189.58 ? 395 PHE A CB 1 ATOM 36 C CG . PHE A 1 12 ? 69.361 27.756 71.194 1.00 191.23 ? 395 PHE A CG 1 ATOM 37 C CD1 . PHE A 1 12 ? 68.902 27.924 69.891 1.00 192.52 ? 395 PHE A CD1 1 ATOM 38 C CD2 . PHE A 1 12 ? 69.982 26.552 71.533 1.00 189.25 ? 395 PHE A CD2 1 ATOM 39 C CE1 . PHE A 1 12 ? 69.066 26.919 68.944 1.00 191.01 ? 395 PHE A CE1 1 ATOM 40 C CE2 . PHE A 1 12 ? 70.149 25.548 70.590 1.00 187.71 ? 395 PHE A CE2 1 ATOM 41 C CZ . PHE A 1 12 ? 69.690 25.730 69.295 1.00 188.76 ? 395 PHE A CZ 1 ATOM 42 N N . ASP A 1 13 ? 70.553 30.902 74.364 1.00 179.19 ? 396 ASP A N 1 ATOM 43 C CA . ASP A 1 13 ? 70.384 31.853 75.477 1.00 172.29 ? 396 ASP A CA 1 ATOM 44 C C . ASP A 1 13 ? 70.985 33.264 75.256 1.00 165.72 ? 396 ASP A C 1 ATOM 45 O O . ASP A 1 13 ? 70.783 34.125 76.100 1.00 165.59 ? 396 ASP A O 1 ATOM 46 C CB . ASP A 1 13 ? 70.962 31.258 76.776 1.00 170.23 ? 396 ASP A CB 1 ATOM 47 C CG . ASP A 1 13 ? 70.204 30.035 77.255 1.00 170.33 ? 396 ASP A CG 1 ATOM 48 O OD1 . ASP A 1 13 ? 69.059 30.198 77.715 1.00 168.56 ? 396 ASP A OD1 1 ATOM 49 O OD2 . ASP A 1 13 ? 70.754 28.911 77.184 1.00 170.00 ? 396 ASP A OD2 1 ATOM 50 N N . GLN A 1 14 ? 71.693 33.516 74.144 1.00 156.98 ? 397 GLN A N 1 ATOM 51 C CA . GLN A 1 14 ? 72.517 34.731 73.969 1.00 150.16 ? 397 GLN A CA 1 ATOM 52 C C . GLN A 1 14 ? 73.771 34.592 74.870 1.00 144.07 ? 397 GLN A C 1 ATOM 53 O O . GLN A 1 14 ? 74.400 35.572 75.292 1.00 145.61 ? 397 GLN A O 1 ATOM 54 C CB . GLN A 1 14 ? 71.699 35.997 74.253 1.00 147.19 ? 397 GLN A CB 1 ATOM 55 C CG . GLN A 1 14 ? 72.220 37.270 73.623 1.00 143.74 ? 397 GLN A CG 1 ATOM 56 C CD . GLN A 1 14 ? 71.377 38.478 73.991 1.00 141.87 ? 397 GLN A CD 1 ATOM 57 O OE1 . GLN A 1 14 ? 70.499 38.410 74.857 1.00 139.87 ? 397 GLN A OE1 1 ATOM 58 N NE2 . GLN A 1 14 ? 71.640 39.594 73.329 1.00 141.25 ? 397 GLN A NE2 1 ATOM 59 N N . HIS A 1 15 ? 74.122 33.328 75.116 1.00 133.19 ? 398 HIS A N 1 ATOM 60 C CA . HIS A 1 15 ? 75.121 32.884 76.094 1.00 119.60 ? 398 HIS A CA 1 ATOM 61 C C . HIS A 1 15 ? 74.740 33.193 77.554 1.00 106.87 ? 398 HIS A C 1 ATOM 62 O O . HIS A 1 15 ? 74.435 32.270 78.293 1.00 110.36 ? 398 HIS A O 1 ATOM 63 C CB . HIS A 1 15 ? 76.554 33.302 75.712 1.00 118.34 ? 398 HIS A CB 1 ATOM 64 C CG . HIS A 1 15 ? 77.361 32.203 75.073 1.00 119.15 ? 398 HIS A CG 1 ATOM 65 N ND1 . HIS A 1 15 ? 78.710 32.333 74.834 1.00 121.39 ? 398 HIS A ND1 1 ATOM 66 C CD2 . HIS A 1 15 ? 77.024 30.959 74.643 1.00 119.25 ? 398 HIS A CD2 1 ATOM 67 C CE1 . HIS A 1 15 ? 79.170 31.228 74.273 1.00 121.73 ? 398 HIS A CE1 1 ATOM 68 N NE2 . HIS A 1 15 ? 78.167 30.376 74.150 1.00 120.21 ? 398 HIS A NE2 1 ATOM 69 N N . PHE A 1 16 ? 74.726 34.455 77.975 1.00 91.15 ? 399 PHE A N 1 ATOM 70 C CA . PHE A 1 16 ? 74.077 34.808 79.273 1.00 80.17 ? 399 PHE A CA 1 ATOM 71 C C . PHE A 1 16 ? 73.847 36.311 79.212 1.00 73.90 ? 399 PHE A C 1 ATOM 72 O O . PHE A 1 16 ? 74.466 37.104 79.919 1.00 74.06 ? 399 PHE A O 1 ATOM 73 C CB . PHE A 1 16 ? 74.941 34.399 80.494 1.00 76.05 ? 399 PHE A CB 1 ATOM 74 C CG . PHE A 1 16 ? 74.234 33.626 81.587 1.00 72.37 ? 399 PHE A CG 1 ATOM 75 C CD1 . PHE A 1 16 ? 74.063 32.258 81.455 1.00 71.86 ? 399 PHE A CD1 1 ATOM 76 C CD2 . PHE A 1 16 ? 73.890 34.216 82.823 1.00 70.94 ? 399 PHE A CD2 1 ATOM 77 C CE1 . PHE A 1 16 ? 73.497 31.497 82.468 1.00 71.42 ? 399 PHE A CE1 1 ATOM 78 C CE2 . PHE A 1 16 ? 73.318 33.456 83.842 1.00 69.84 ? 399 PHE A CE2 1 ATOM 79 C CZ . PHE A 1 16 ? 73.125 32.094 83.664 1.00 70.84 ? 399 PHE A CZ 1 ATOM 80 N N . GLY A 1 17 ? 72.998 36.686 78.268 1.00 68.58 ? 400 GLY A N 1 ATOM 81 C CA . GLY A 1 17 ? 72.683 38.076 77.996 1.00 66.61 ? 400 GLY A CA 1 ATOM 82 C C . GLY A 1 17 ? 73.870 38.704 77.314 1.00 64.39 ? 400 GLY A C 1 ATOM 83 O O . GLY A 1 17 ? 74.849 38.019 77.030 1.00 63.46 ? 400 GLY A O 1 ATOM 84 N N . PRO A 1 18 ? 73.807 40.016 77.070 1.00 62.96 ? 401 PRO A N 1 ATOM 85 C CA . PRO A 1 18 ? 74.856 40.674 76.306 1.00 61.77 ? 401 PRO A CA 1 ATOM 86 C C . PRO A 1 18 ? 76.206 40.832 77.004 1.00 60.21 ? 401 PRO A C 1 ATOM 87 O O . PRO A 1 18 ? 77.180 41.060 76.306 1.00 62.48 ? 401 PRO A O 1 ATOM 88 C CB . PRO A 1 18 ? 74.253 42.042 75.994 1.00 63.29 ? 401 PRO A CB 1 ATOM 89 C CG . PRO A 1 18 ? 73.309 42.297 77.104 1.00 63.39 ? 401 PRO A CG 1 ATOM 90 C CD . PRO A 1 18 ? 72.771 40.962 77.516 1.00 63.49 ? 401 PRO A CD 1 ATOM 91 N N . PHE A 1 19 ? 76.289 40.701 78.330 1.00 58.07 ? 402 PHE A N 1 ATOM 92 C CA . PHE A 1 19 ? 77.539 41.017 79.060 1.00 58.39 ? 402 PHE A CA 1 ATOM 93 C C . PHE A 1 19 ? 78.323 39.822 79.612 1.00 56.69 ? 402 PHE A C 1 ATOM 94 O O . PHE A 1 19 ? 79.405 39.997 80.168 1.00 55.59 ? 402 PHE A O 1 ATOM 95 C CB . PHE A 1 19 ? 77.236 41.994 80.204 1.00 59.48 ? 402 PHE A CB 1 ATOM 96 C CG . PHE A 1 19 ? 76.383 43.162 79.787 1.00 60.20 ? 402 PHE A CG 1 ATOM 97 C CD1 . PHE A 1 19 ? 76.857 44.076 78.856 1.00 62.01 ? 402 PHE A CD1 1 ATOM 98 C CD2 . PHE A 1 19 ? 75.108 43.340 80.307 1.00 60.14 ? 402 PHE A CD2 1 ATOM 99 C CE1 . PHE A 1 19 ? 76.077 45.146 78.450 1.00 62.30 ? 402 PHE A CE1 1 ATOM 100 C CE2 . PHE A 1 19 ? 74.323 44.408 79.906 1.00 60.89 ? 402 PHE A CE2 1 ATOM 101 C CZ . PHE A 1 19 ? 74.804 45.305 78.970 1.00 62.02 ? 402 PHE A CZ 1 ATOM 102 N N . PHE A 1 20 ? 77.782 38.616 79.464 1.00 57.52 ? 403 PHE A N 1 ATOM 103 C CA . PHE A 1 20 ? 78.414 37.400 79.980 1.00 56.75 ? 403 PHE A CA 1 ATOM 104 C C . PHE A 1 20 ? 78.387 36.346 78.897 1.00 58.03 ? 403 PHE A C 1 ATOM 105 O O . PHE A 1 20 ? 77.440 36.278 78.122 1.00 57.04 ? 403 PHE A O 1 ATOM 106 C CB . PHE A 1 20 ? 77.684 36.896 81.237 1.00 55.61 ? 403 PHE A CB 1 ATOM 107 C CG . PHE A 1 20 ? 77.941 37.729 82.466 1.00 55.18 ? 403 PHE A CG 1 ATOM 108 C CD1 . PHE A 1 20 ? 77.173 38.853 82.737 1.00 54.51 ? 403 PHE A CD1 1 ATOM 109 C CD2 . PHE A 1 20 ? 78.967 37.404 83.340 1.00 54.90 ? 403 PHE A CD2 1 ATOM 110 C CE1 . PHE A 1 20 ? 77.420 39.635 83.858 1.00 54.17 ? 403 PHE A CE1 1 ATOM 111 C CE2 . PHE A 1 20 ? 79.214 38.181 84.467 1.00 54.78 ? 403 PHE A CE2 1 ATOM 112 C CZ . PHE A 1 20 ? 78.441 39.297 84.724 1.00 53.94 ? 403 PHE A CZ 1 ATOM 113 N N . ARG A 1 21 ? 79.454 35.556 78.828 1.00 62.93 ? 404 ARG A N 1 ATOM 114 C CA . ARG A 1 21 ? 79.488 34.332 78.023 1.00 65.69 ? 404 ARG A CA 1 ATOM 115 C C . ARG A 1 21 ? 79.532 33.135 78.971 1.00 62.87 ? 404 ARG A C 1 ATOM 116 O O . ARG A 1 21 ? 79.709 33.302 80.169 1.00 59.45 ? 404 ARG A O 1 ATOM 117 C CB . ARG A 1 21 ? 80.677 34.325 77.052 1.00 70.45 ? 404 ARG A CB 1 ATOM 118 C CG . ARG A 1 21 ? 82.064 34.238 77.686 1.00 76.36 ? 404 ARG A CG 1 ATOM 119 C CD . ARG A 1 21 ? 83.141 33.862 76.669 1.00 80.82 ? 404 ARG A CD 1 ATOM 120 N NE . ARG A 1 21 ? 84.424 33.518 77.297 1.00 86.96 ? 404 ARG A NE 1 ATOM 121 C CZ . ARG A 1 21 ? 85.273 34.390 77.875 1.00 93.37 ? 404 ARG A CZ 1 ATOM 122 N NH1 . ARG A 1 21 ? 85.005 35.706 77.941 1.00 93.29 ? 404 ARG A NH1 1 ATOM 123 N NH2 . ARG A 1 21 ? 86.422 33.941 78.399 1.00 92.91 ? 404 ARG A NH2 1 ATOM 124 N N . THR A 1 22 ? 79.358 31.935 78.434 1.00 63.56 ? 405 THR A N 1 ATOM 125 C CA . THR A 1 22 ? 79.375 30.721 79.251 1.00 62.90 ? 405 THR A CA 1 ATOM 126 C C . THR A 1 22 ? 80.469 29.765 78.813 1.00 63.83 ? 405 THR A C 1 ATOM 127 O O . THR A 1 22 ? 80.603 29.496 77.624 1.00 67.45 ? 405 THR A O 1 ATOM 128 C CB . THR A 1 22 ? 78.028 29.976 79.188 1.00 60.73 ? 405 THR A CB 1 ATOM 129 O OG1 . THR A 1 22 ? 77.760 29.560 77.848 1.00 59.75 ? 405 THR A OG1 1 ATOM 130 C CG2 . THR A 1 22 ? 76.901 30.863 79.678 1.00 60.63 ? 405 THR A CG2 1 ATOM 131 N N . GLU A 1 23 ? 81.236 29.259 79.775 1.00 63.44 ? 406 GLU A N 1 ATOM 132 C CA . GLU A 1 23 ? 82.006 28.032 79.592 1.00 64.49 ? 406 GLU A CA 1 ATOM 133 C C . GLU A 1 23 ? 81.110 26.892 80.019 1.00 61.59 ? 406 GLU A C 1 ATOM 134 O O . GLU A 1 23 ? 80.551 26.930 81.106 1.00 60.67 ? 406 GLU A O 1 ATOM 135 C CB . GLU A 1 23 ? 83.259 28.016 80.458 1.00 67.50 ? 406 GLU A CB 1 ATOM 136 C CG . GLU A 1 23 ? 84.241 29.145 80.185 1.00 70.90 ? 406 GLU A CG 1 ATOM 137 C CD . GLU A 1 23 ? 84.712 29.220 78.739 1.00 74.53 ? 406 GLU A CD 1 ATOM 138 O OE1 . GLU A 1 23 ? 84.854 28.162 78.076 1.00 73.65 ? 406 GLU A OE1 1 ATOM 139 O OE2 . GLU A 1 23 ? 84.938 30.364 78.268 1.00 81.47 ? 406 GLU A OE2 1 ATOM 140 N N . GLN A 1 24 ? 80.981 25.881 79.168 1.00 60.97 ? 407 GLN A N 1 ATOM 141 C CA . GLN A 1 24 ? 80.031 24.808 79.388 1.00 59.44 ? 407 GLN A CA 1 ATOM 142 C C . GLN A 1 24 ? 80.606 23.417 79.073 1.00 57.58 ? 407 GLN A C 1 ATOM 143 O O . GLN A 1 24 ? 81.204 23.194 78.018 1.00 56.05 ? 407 GLN A O 1 ATOM 144 C CB . GLN A 1 24 ? 78.788 25.078 78.557 1.00 62.17 ? 407 GLN A CB 1 ATOM 145 C CG . GLN A 1 24 ? 77.708 24.025 78.708 1.00 66.46 ? 407 GLN A CG 1 ATOM 146 C CD . GLN A 1 24 ? 76.419 24.425 78.035 1.00 68.56 ? 407 GLN A CD 1 ATOM 147 O OE1 . GLN A 1 24 ? 76.147 24.049 76.893 1.00 72.67 ? 407 GLN A OE1 1 ATOM 148 N NE2 . GLN A 1 24 ? 75.611 25.179 78.747 1.00 68.68 ? 407 GLN A NE2 1 ATOM 149 N N . LEU A 1 25 ? 80.371 22.479 79.986 1.00 55.40 ? 408 LEU A N 1 ATOM 150 C CA . LEU A 1 25 ? 80.812 21.099 79.840 1.00 54.73 ? 408 LEU A CA 1 ATOM 151 C C . LEU A 1 25 ? 79.622 20.152 79.830 1.00 54.91 ? 408 LEU A C 1 ATOM 152 O O . LEU A 1 25 ? 78.684 20.339 80.602 1.00 54.69 ? 408 LEU A O 1 ATOM 153 C CB . LEU A 1 25 ? 81.723 20.724 81.003 1.00 54.02 ? 408 LEU A CB 1 ATOM 154 C CG . LEU A 1 25 ? 82.932 21.624 81.223 1.00 53.80 ? 408 LEU A CG 1 ATOM 155 C CD1 . LEU A 1 25 ? 83.657 21.192 82.483 1.00 54.33 ? 408 LEU A CD1 1 ATOM 156 C CD2 . LEU A 1 25 ? 83.861 21.583 80.023 1.00 54.72 ? 408 LEU A CD2 1 ATOM 157 N N . ILE A 1 26 ? 79.658 19.137 78.963 1.00 56.44 ? 409 ILE A N 1 ATOM 158 C CA . ILE A 1 26 ? 78.701 18.027 79.044 1.00 56.45 ? 409 ILE A CA 1 ATOM 159 C C . ILE A 1 26 ? 79.445 16.775 79.552 1.00 56.61 ? 409 ILE A C 1 ATOM 160 O O . ILE A 1 26 ? 80.542 16.449 79.080 1.00 56.67 ? 409 ILE A O 1 ATOM 161 C CB . ILE A 1 26 ? 77.888 17.801 77.750 1.00 57.64 ? 409 ILE A CB 1 ATOM 162 C CG1 . ILE A 1 26 ? 77.085 16.495 77.865 1.00 60.59 ? 409 ILE A CG1 1 ATOM 163 C CG2 . ILE A 1 26 ? 78.777 17.752 76.539 1.00 58.34 ? 409 ILE A CG2 1 ATOM 164 C CD1 . ILE A 1 26 ? 75.962 16.343 76.857 1.00 62.36 ? 409 ILE A CD1 1 ATOM 165 N N . ILE A 1 27 ? 78.854 16.110 80.544 1.00 56.06 ? 410 ILE A N 1 ATOM 166 C CA . ILE A 1 27 ? 79.501 15.033 81.275 1.00 57.47 ? 410 ILE A CA 1 ATOM 167 C C . ILE A 1 27 ? 78.630 13.789 81.228 1.00 58.75 ? 410 ILE A C 1 ATOM 168 O O . ILE A 1 27 ? 77.462 13.840 81.599 1.00 58.58 ? 410 ILE A O 1 ATOM 169 C CB . ILE A 1 27 ? 79.779 15.448 82.732 1.00 57.56 ? 410 ILE A CB 1 ATOM 170 C CG1 . ILE A 1 27 ? 80.793 16.597 82.749 1.00 58.13 ? 410 ILE A CG1 1 ATOM 171 C CG2 . ILE A 1 27 ? 80.355 14.287 83.541 1.00 58.95 ? 410 ILE A CG2 1 ATOM 172 C CD1 . ILE A 1 27 ? 80.962 17.256 84.097 1.00 58.75 ? 410 ILE A CD1 1 ATOM 173 N N . ARG A 1 28 ? 79.214 12.670 80.793 1.00 60.98 ? 411 ARG A N 1 ATOM 174 C CA . ARG A 1 28 ? 78.539 11.367 80.809 1.00 62.46 ? 411 ARG A CA 1 ATOM 175 C C . ARG A 1 28 ? 79.350 10.365 81.614 1.00 62.97 ? 411 ARG A C 1 ATOM 176 O O . ARG A 1 28 ? 80.536 10.573 81.830 1.00 63.03 ? 411 ARG A O 1 ATOM 177 C CB . ARG A 1 28 ? 78.323 10.863 79.387 1.00 63.29 ? 411 ARG A CB 1 ATOM 178 C CG . ARG A 1 28 ? 77.412 11.761 78.572 1.00 64.02 ? 411 ARG A CG 1 ATOM 179 C CD . ARG A 1 28 ? 77.058 11.147 77.236 1.00 66.06 ? 411 ARG A CD 1 ATOM 180 N NE . ARG A 1 28 ? 76.300 12.057 76.380 1.00 67.40 ? 411 ARG A NE 1 ATOM 181 C CZ . ARG A 1 28 ? 76.818 13.079 75.685 1.00 68.65 ? 411 ARG A CZ 1 ATOM 182 N NH1 . ARG A 1 28 ? 78.118 13.375 75.739 1.00 67.25 ? 411 ARG A NH1 1 ATOM 183 N NH2 . ARG A 1 28 ? 76.015 13.829 74.925 1.00 69.59 ? 411 ARG A NH2 1 ATOM 184 N N . ALA A 1 29 ? 78.693 9.296 82.068 1.00 64.25 ? 412 ALA A N 1 ATOM 185 C CA . ALA A 1 29 ? 79.337 8.233 82.843 1.00 65.82 ? 412 ALA A CA 1 ATOM 186 C C . ALA A 1 29 ? 79.254 6.874 82.103 1.00 67.44 ? 412 ALA A C 1 ATOM 187 O O . ALA A 1 29 ? 78.399 6.043 82.415 1.00 68.04 ? 412 ALA A O 1 ATOM 188 C CB . ALA A 1 29 ? 78.713 8.141 84.231 1.00 65.38 ? 412 ALA A CB 1 ATOM 189 N N . PRO A 1 30 ? 80.154 6.641 81.128 1.00 69.88 ? 413 PRO A N 1 ATOM 190 C CA . PRO A 1 30 ? 80.037 5.473 80.234 1.00 71.97 ? 413 PRO A CA 1 ATOM 191 C C . PRO A 1 30 ? 80.219 4.084 80.890 1.00 72.88 ? 413 PRO A C 1 ATOM 192 O O . PRO A 1 30 ? 79.722 3.100 80.357 1.00 71.15 ? 413 PRO A O 1 ATOM 193 C CB . PRO A 1 30 ? 81.141 5.723 79.198 1.00 72.20 ? 413 PRO A CB 1 ATOM 194 C CG . PRO A 1 30 ? 82.178 6.486 79.948 1.00 72.26 ? 413 PRO A CG 1 ATOM 195 C CD . PRO A 1 30 ? 81.420 7.372 80.898 1.00 71.12 ? 413 PRO A CD 1 ATOM 196 N N . LEU A 1 31 ? 80.923 4.013 82.020 1.00 74.47 ? 414 LEU A N 1 ATOM 197 C CA . LEU A 1 31 ? 81.159 2.746 82.724 1.00 77.09 ? 414 LEU A CA 1 ATOM 198 C C . LEU A 1 31 ? 80.214 2.524 83.904 1.00 76.09 ? 414 LEU A C 1 ATOM 199 O O . LEU A 1 31 ? 80.487 1.676 84.748 1.00 77.15 ? 414 LEU A O 1 ATOM 200 C CB . LEU A 1 31 ? 82.609 2.694 83.231 1.00 79.75 ? 414 LEU A CB 1 ATOM 201 C CG . LEU A 1 31 ? 83.692 2.956 82.179 1.00 81.60 ? 414 LEU A CG 1 ATOM 202 C CD1 . LEU A 1 31 ? 85.056 3.105 82.841 1.00 83.21 ? 414 LEU A CD1 1 ATOM 203 C CD2 . LEU A 1 31 ? 83.695 1.854 81.131 1.00 82.16 ? 414 LEU A CD2 1 ATOM 204 N N . THR A 1 32 ? 79.109 3.269 83.964 1.00 73.91 ? 415 THR A N 1 ATOM 205 C CA . THR A 1 32 ? 78.179 3.206 85.090 1.00 71.57 ? 415 THR A CA 1 ATOM 206 C C . THR A 1 32 ? 76.802 2.801 84.578 1.00 72.00 ? 415 THR A C 1 ATOM 207 O O . THR A 1 32 ? 76.380 3.239 83.507 1.00 70.59 ? 415 THR A O 1 ATOM 208 C CB . THR A 1 32 ? 78.085 4.561 85.810 1.00 68.96 ? 415 THR A CB 1 ATOM 209 O OG1 . THR A 1 32 ? 79.399 5.079 86.039 1.00 68.37 ? 415 THR A OG1 1 ATOM 210 C CG2 . THR A 1 32 ? 77.363 4.423 87.144 1.00 68.65 ? 415 THR A CG2 1 ATOM 211 N N . ASP A 1 33 ? 76.118 1.954 85.342 1.00 73.23 ? 416 ASP A N 1 ATOM 212 C CA . ASP A 1 33 ? 74.785 1.502 84.986 1.00 76.11 ? 416 ASP A CA 1 ATOM 213 C C . ASP A 1 33 ? 73.763 2.391 85.658 1.00 75.05 ? 416 ASP A C 1 ATOM 214 O O . ASP A 1 33 ? 74.075 3.086 86.624 1.00 73.84 ? 416 ASP A O 1 ATOM 215 C CB . ASP A 1 33 ? 74.550 0.051 85.429 1.00 79.80 ? 416 ASP A CB 1 ATOM 216 C CG . ASP A 1 33 ? 75.443 -0.947 84.702 1.00 82.68 ? 416 ASP A CG 1 ATOM 217 O OD1 . ASP A 1 33 ? 75.759 -0.732 83.504 1.00 84.48 ? 416 ASP A OD1 1 ATOM 218 O OD2 . ASP A 1 33 ? 75.816 -1.958 85.334 1.00 83.06 ? 416 ASP A OD2 1 ATOM 219 N N . LYS A 1 34 ? 72.536 2.352 85.147 1.00 74.58 ? 417 LYS A N 1 ATOM 220 C CA . LYS A 1 34 ? 71.411 2.964 85.836 1.00 74.62 ? 417 LYS A CA 1 ATOM 221 C C . LYS A 1 34 ? 71.159 2.215 87.146 1.00 73.82 ? 417 LYS A C 1 ATOM 222 O O . LYS A 1 34 ? 71.788 1.200 87.416 1.00 75.27 ? 417 LYS A O 1 ATOM 223 C CB . LYS A 1 34 ? 70.157 3.000 84.948 1.00 75.13 ? 417 LYS A CB 1 ATOM 224 C CG . LYS A 1 34 ? 69.532 1.651 84.623 1.00 78.26 ? 417 LYS A CG 1 ATOM 225 C CD . LYS A 1 34 ? 68.216 1.804 83.872 1.00 80.60 ? 417 LYS A CD 1 ATOM 226 C CE . LYS A 1 34 ? 68.398 2.524 82.542 1.00 81.09 ? 417 LYS A CE 1 ATOM 227 N NZ . LYS A 1 34 ? 67.251 2.294 81.622 1.00 82.86 ? 417 LYS A NZ 1 ATOM 228 N N . HIS A 1 35 ? 70.270 2.740 87.971 1.00 73.19 ? 418 HIS A N 1 ATOM 229 C CA . HIS A 1 35 ? 69.893 2.062 89.201 1.00 73.98 ? 418 HIS A CA 1 ATOM 230 C C . HIS A 1 35 ? 68.533 2.502 89.681 1.00 73.85 ? 418 HIS A C 1 ATOM 231 O O . HIS A 1 35 ? 68.027 3.545 89.277 1.00 73.17 ? 418 HIS A O 1 ATOM 232 C CB . HIS A 1 35 ? 70.949 2.250 90.291 1.00 74.08 ? 418 HIS A CB 1 ATOM 233 C CG . HIS A 1 35 ? 71.038 3.640 90.836 1.00 74.72 ? 418 HIS A CG 1 ATOM 234 N ND1 . HIS A 1 35 ? 71.383 4.729 90.063 1.00 74.50 ? 418 HIS A ND1 1 ATOM 235 C CD2 . HIS A 1 35 ? 70.872 4.109 92.095 1.00 74.90 ? 418 HIS A CD2 1 ATOM 236 C CE1 . HIS A 1 35 ? 71.406 5.812 90.819 1.00 73.16 ? 418 HIS A CE1 1 ATOM 237 N NE2 . HIS A 1 35 ? 71.099 5.462 92.054 1.00 73.31 ? 418 HIS A NE2 1 ATOM 238 N N . ILE A 1 36 ? 67.957 1.686 90.550 1.00 75.57 ? 419 ILE A N 1 ATOM 239 C CA . ILE A 1 36 ? 66.598 1.876 91.026 1.00 76.85 ? 419 ILE A CA 1 ATOM 240 C C . ILE A 1 36 ? 66.636 2.530 92.405 1.00 77.25 ? 419 ILE A C 1 ATOM 241 O O . ILE A 1 36 ? 67.493 2.208 93.235 1.00 80.41 ? 419 ILE A O 1 ATOM 242 C CB . ILE A 1 36 ? 65.845 0.523 91.091 1.00 78.42 ? 419 ILE A CB 1 ATOM 243 C CG1 . ILE A 1 36 ? 65.886 -0.194 89.729 1.00 78.69 ? 419 ILE A CG1 1 ATOM 244 C CG2 . ILE A 1 36 ? 64.405 0.715 91.551 1.00 78.33 ? 419 ILE A CG2 1 ATOM 245 C CD1 . ILE A 1 36 ? 65.283 0.584 88.576 1.00 78.13 ? 419 ILE A CD1 1 ATOM 246 N N . TYR A 1 37 ? 65.720 3.469 92.621 1.00 75.25 ? 420 TYR A N 1 ATOM 247 C CA . TYR A 1 37 ? 65.458 4.048 93.928 1.00 75.05 ? 420 TYR A CA 1 ATOM 248 C C . TYR A 1 37 ? 64.014 3.713 94.256 1.00 78.05 ? 420 TYR A C 1 ATOM 249 O O . TYR A 1 37 ? 63.117 3.961 93.440 1.00 76.88 ? 420 TYR A O 1 ATOM 250 C CB . TYR A 1 37 ? 65.684 5.558 93.903 1.00 73.08 ? 420 TYR A CB 1 ATOM 251 C CG . TYR A 1 37 ? 64.899 6.335 94.936 1.00 72.55 ? 420 TYR A CG 1 ATOM 252 C CD1 . TYR A 1 37 ? 65.275 6.332 96.285 1.00 72.59 ? 420 TYR A CD1 1 ATOM 253 C CD2 . TYR A 1 37 ? 63.782 7.086 94.563 1.00 72.74 ? 420 TYR A CD2 1 ATOM 254 C CE1 . TYR A 1 37 ? 64.556 7.055 97.236 1.00 72.74 ? 420 TYR A CE1 1 ATOM 255 C CE2 . TYR A 1 37 ? 63.053 7.806 95.501 1.00 72.89 ? 420 TYR A CE2 1 ATOM 256 C CZ . TYR A 1 37 ? 63.442 7.792 96.835 1.00 73.37 ? 420 TYR A CZ 1 ATOM 257 O OH . TYR A 1 37 ? 62.715 8.523 97.751 1.00 74.01 ? 420 TYR A OH 1 ATOM 258 N N . GLN A 1 38 ? 63.800 3.154 95.447 1.00 82.35 ? 421 GLN A N 1 ATOM 259 C CA . GLN A 1 38 ? 62.479 2.731 95.902 1.00 84.97 ? 421 GLN A CA 1 ATOM 260 C C . GLN A 1 38 ? 62.020 3.676 97.007 1.00 85.13 ? 421 GLN A C 1 ATOM 261 O O . GLN A 1 38 ? 62.602 3.681 98.089 1.00 85.12 ? 421 GLN A O 1 ATOM 262 C CB . GLN A 1 38 ? 62.542 1.297 96.404 1.00 88.00 ? 421 GLN A CB 1 ATOM 263 C CG . GLN A 1 38 ? 62.969 0.327 95.318 1.00 89.91 ? 421 GLN A CG 1 ATOM 264 C CD . GLN A 1 38 ? 63.041 -1.106 95.803 1.00 92.11 ? 421 GLN A CD 1 ATOM 265 O OE1 . GLN A 1 38 ? 63.685 -1.399 96.815 1.00 92.68 ? 421 GLN A OE1 1 ATOM 266 N NE2 . GLN A 1 38 ? 62.396 -2.013 95.073 1.00 93.51 ? 421 GLN A NE2 1 ATOM 267 N N . PRO A 1 39 ? 60.994 4.501 96.731 1.00 86.07 ? 422 PRO A N 1 ATOM 268 C CA . PRO A 1 39 ? 60.582 5.467 97.750 1.00 87.71 ? 422 PRO A CA 1 ATOM 269 C C . PRO A 1 39 ? 59.881 4.819 98.948 1.00 93.28 ? 422 PRO A C 1 ATOM 270 O O . PRO A 1 39 ? 59.194 3.806 98.799 1.00 94.20 ? 422 PRO A O 1 ATOM 271 C CB . PRO A 1 39 ? 59.645 6.416 96.999 1.00 86.31 ? 422 PRO A CB 1 ATOM 272 C CG . PRO A 1 39 ? 59.244 5.715 95.750 1.00 85.84 ? 422 PRO A CG 1 ATOM 273 C CD . PRO A 1 39 ? 60.187 4.586 95.499 1.00 85.05 ? 422 PRO A CD 1 ATOM 274 N N . TYR A 1 40 ? 60.086 5.420 100.119 1.00 97.93 ? 423 TYR A N 1 ATOM 275 C CA . TYR A 1 40 ? 59.518 4.970 101.385 1.00 102.39 ? 423 TYR A CA 1 ATOM 276 C C . TYR A 1 40 ? 58.296 5.851 101.700 1.00 103.29 ? 423 TYR A C 1 ATOM 277 O O . TYR A 1 40 ? 58.335 7.053 101.431 1.00 100.38 ? 423 TYR A O 1 ATOM 278 C CB . TYR A 1 40 ? 60.576 5.107 102.487 1.00 104.52 ? 423 TYR A CB 1 ATOM 279 C CG . TYR A 1 40 ? 60.136 4.667 103.871 1.00 108.53 ? 423 TYR A CG 1 ATOM 280 C CD1 . TYR A 1 40 ? 60.444 3.389 104.353 1.00 110.80 ? 423 TYR A CD1 1 ATOM 281 C CD2 . TYR A 1 40 ? 59.421 5.536 104.708 1.00 109.36 ? 423 TYR A CD2 1 ATOM 282 C CE1 . TYR A 1 40 ? 60.047 2.988 105.623 1.00 113.33 ? 423 TYR A CE1 1 ATOM 283 C CE2 . TYR A 1 40 ? 59.018 5.146 105.977 1.00 111.49 ? 423 TYR A CE2 1 ATOM 284 C CZ . TYR A 1 40 ? 59.330 3.874 106.429 1.00 114.04 ? 423 TYR A CZ 1 ATOM 285 O OH . TYR A 1 40 ? 58.929 3.494 107.685 1.00 117.44 ? 423 TYR A OH 1 ATOM 286 N N . PRO A 1 41 ? 57.214 5.293 102.258 1.00 106.97 ? 424 PRO A N 1 ATOM 287 C CA . PRO A 1 41 ? 57.040 3.857 102.562 1.00 108.49 ? 424 PRO A CA 1 ATOM 288 C C . PRO A 1 41 ? 56.617 3.010 101.353 1.00 108.69 ? 424 PRO A C 1 ATOM 289 O O . PRO A 1 41 ? 56.977 1.833 101.268 1.00 106.97 ? 424 PRO A O 1 ATOM 290 C CB . PRO A 1 41 ? 55.929 3.868 103.614 1.00 110.87 ? 424 PRO A CB 1 ATOM 291 C CG . PRO A 1 41 ? 55.121 5.087 103.295 1.00 110.44 ? 424 PRO A CG 1 ATOM 292 C CD . PRO A 1 41 ? 56.066 6.103 102.710 1.00 107.85 ? 424 PRO A CD 1 ATOM 293 N N . SER A 1 42 ? 55.851 3.612 100.443 1.00 108.86 ? 425 SER A N 1 ATOM 294 C CA . SER A 1 42 ? 55.387 2.966 99.223 1.00 109.42 ? 425 SER A CA 1 ATOM 295 C C . SER A 1 42 ? 55.523 3.952 98.071 1.00 107.16 ? 425 SER A C 1 ATOM 296 O O . SER A 1 42 ? 55.757 5.142 98.283 1.00 108.13 ? 425 SER A O 1 ATOM 297 C CB . SER A 1 42 ? 53.925 2.547 99.387 1.00 111.94 ? 425 SER A CB 1 ATOM 298 O OG . SER A 1 42 ? 53.352 2.132 98.157 1.00 113.19 ? 425 SER A OG 1 ATOM 299 N N . GLY A 1 43 ? 55.363 3.444 96.854 1.00 105.47 ? 426 GLY A N 1 ATOM 300 C CA . GLY A 1 43 ? 55.424 4.262 95.640 1.00 101.74 ? 426 GLY A CA 1 ATOM 301 C C . GLY A 1 43 ? 56.131 3.527 94.520 1.00 99.67 ? 426 GLY A C 1 ATOM 302 O O . GLY A 1 43 ? 56.917 2.608 94.768 1.00 99.71 ? 426 GLY A O 1 ATOM 303 N N . ALA A 1 44 ? 55.845 3.938 93.285 1.00 96.21 ? 427 ALA A N 1 ATOM 304 C CA . ALA A 1 44 ? 56.447 3.333 92.097 1.00 93.38 ? 427 ALA A CA 1 ATOM 305 C C . ALA A 1 44 ? 57.960 3.544 92.085 1.00 91.87 ? 427 ALA A C 1 ATOM 306 O O . ALA A 1 44 ? 58.456 4.566 92.580 1.00 92.22 ? 427 ALA A O 1 ATOM 307 C CB . ALA A 1 44 ? 55.826 3.917 90.835 1.00 92.12 ? 427 ALA A CB 1 ATOM 308 N N . ASP A 1 45 ? 58.683 2.570 91.531 1.00 89.27 ? 428 ASP A N 1 ATOM 309 C CA . ASP A 1 45 ? 60.137 2.665 91.394 1.00 85.49 ? 428 ASP A CA 1 ATOM 310 C C . ASP A 1 45 ? 60.538 3.828 90.489 1.00 81.12 ? 428 ASP A C 1 ATOM 311 O O . ASP A 1 45 ? 59.838 4.148 89.517 1.00 80.80 ? 428 ASP A O 1 ATOM 312 C CB . ASP A 1 45 ? 60.722 1.370 90.821 1.00 87.97 ? 428 ASP A CB 1 ATOM 313 C CG . ASP A 1 45 ? 60.613 0.189 91.777 1.00 92.25 ? 428 ASP A CG 1 ATOM 314 O OD1 . ASP A 1 45 ? 60.282 0.392 92.970 1.00 94.85 ? 428 ASP A OD1 1 ATOM 315 O OD2 . ASP A 1 45 ? 60.877 -0.951 91.328 1.00 92.79 ? 428 ASP A OD2 1 ATOM 316 N N . VAL A 1 46 ? 61.664 4.459 90.822 1.00 75.34 ? 429 VAL A N 1 ATOM 317 C CA . VAL A 1 46 ? 62.219 5.546 90.023 1.00 69.97 ? 429 VAL A CA 1 ATOM 318 C C . VAL A 1 46 ? 63.630 5.145 89.598 1.00 67.59 ? 429 VAL A C 1 ATOM 319 O O . VAL A 1 46 ? 64.522 5.067 90.442 1.00 67.18 ? 429 VAL A O 1 ATOM 320 C CB . VAL A 1 46 ? 62.256 6.874 90.803 1.00 67.07 ? 429 VAL A CB 1 ATOM 321 C CG1 . VAL A 1 46 ? 62.681 8.020 89.884 1.00 66.24 ? 429 VAL A CG1 1 ATOM 322 C CG2 . VAL A 1 46 ? 60.899 7.161 91.422 1.00 66.69 ? 429 VAL A CG2 1 ATOM 323 N N . PRO A 1 47 ? 63.833 4.869 88.298 1.00 64.81 ? 430 PRO A N 1 ATOM 324 C CA . PRO A 1 47 ? 65.181 4.610 87.822 1.00 64.40 ? 430 PRO A CA 1 ATOM 325 C C . PRO A 1 47 ? 65.983 5.906 87.683 1.00 62.98 ? 430 PRO A C 1 ATOM 326 O O . PRO A 1 47 ? 65.442 6.937 87.278 1.00 62.18 ? 430 PRO A O 1 ATOM 327 C CB . PRO A 1 47 ? 64.960 3.947 86.458 1.00 64.93 ? 430 PRO A CB 1 ATOM 328 C CG . PRO A 1 47 ? 63.634 4.410 86.003 1.00 64.73 ? 430 PRO A CG 1 ATOM 329 C CD . PRO A 1 47 ? 62.851 4.859 87.204 1.00 65.02 ? 430 PRO A CD 1 ATOM 330 N N . PHE A 1 48 ? 67.261 5.836 88.033 1.00 62.23 ? 431 PHE A N 1 ATOM 331 C CA . PHE A 1 48 ? 68.174 6.956 87.916 1.00 61.02 ? 431 PHE A CA 1 ATOM 332 C C . PHE A 1 48 ? 69.267 6.600 86.929 1.00 61.45 ? 431 PHE A C 1 ATOM 333 O O . PHE A 1 48 ? 69.859 5.526 87.024 1.00 63.50 ? 431 PHE A O 1 ATOM 334 C CB . PHE A 1 48 ? 68.764 7.302 89.277 1.00 60.88 ? 431 PHE A CB 1 ATOM 335 C CG . PHE A 1 48 ? 67.903 8.224 90.071 1.00 60.73 ? 431 PHE A CG 1 ATOM 336 C CD1 . PHE A 1 48 ? 66.710 7.780 90.599 1.00 62.09 ? 431 PHE A CD1 1 ATOM 337 C CD2 . PHE A 1 48 ? 68.264 9.549 90.261 1.00 61.53 ? 431 PHE A CD2 1 ATOM 338 C CE1 . PHE A 1 48 ? 65.888 8.634 91.324 1.00 63.15 ? 431 PHE A CE1 1 ATOM 339 C CE2 . PHE A 1 48 ? 67.452 10.414 90.987 1.00 61.62 ? 431 PHE A CE2 1 ATOM 340 C CZ . PHE A 1 48 ? 66.259 9.956 91.517 1.00 62.51 ? 431 PHE A CZ 1 ATOM 341 N N . GLY A 1 49 ? 69.534 7.497 85.985 1.00 59.78 ? 432 GLY A N 1 ATOM 342 C CA . GLY A 1 49 ? 70.502 7.237 84.926 1.00 60.38 ? 432 GLY A CA 1 ATOM 343 C C . GLY A 1 49 ? 71.941 7.208 85.419 1.00 60.32 ? 432 GLY A C 1 ATOM 344 O O . GLY A 1 49 ? 72.215 7.625 86.547 1.00 60.44 ? 432 GLY A O 1 ATOM 345 N N . PRO A 1 50 ? 72.874 6.740 84.564 1.00 59.94 ? 433 PRO A N 1 ATOM 346 C CA . PRO A 1 50 ? 74.281 6.594 84.949 1.00 60.18 ? 433 PRO A CA 1 ATOM 347 C C . PRO A 1 50 ? 74.920 7.799 85.651 1.00 59.84 ? 433 PRO A C 1 ATOM 348 O O . PRO A 1 50 ? 75.563 7.611 86.689 1.00 60.69 ? 433 PRO A O 1 ATOM 349 C CB . PRO A 1 50 ? 74.984 6.311 83.617 1.00 60.27 ? 433 PRO A CB 1 ATOM 350 C CG . PRO A 1 50 ? 73.938 5.672 82.781 1.00 60.72 ? 433 PRO A CG 1 ATOM 351 C CD . PRO A 1 50 ? 72.646 6.313 83.169 1.00 59.93 ? 433 PRO A CD 1 ATOM 352 N N . PRO A 1 51 ? 74.742 9.027 85.118 1.00 59.05 ? 434 PRO A N 1 ATOM 353 C CA . PRO A 1 51 ? 75.429 10.150 85.770 1.00 58.78 ? 434 PRO A CA 1 ATOM 354 C C . PRO A 1 51 ? 74.857 10.596 87.128 1.00 58.85 ? 434 PRO A C 1 ATOM 355 O O . PRO A 1 51 ? 75.466 11.441 87.788 1.00 56.69 ? 434 PRO A O 1 ATOM 356 C CB . PRO A 1 51 ? 75.308 11.285 84.763 1.00 59.62 ? 434 PRO A CB 1 ATOM 357 C CG . PRO A 1 51 ? 74.254 10.888 83.791 1.00 60.11 ? 434 PRO A CG 1 ATOM 358 C CD . PRO A 1 51 ? 73.836 9.479 84.050 1.00 59.65 ? 434 PRO A CD 1 ATOM 359 N N . LEU A 1 52 ? 73.719 10.031 87.546 1.00 59.27 ? 435 LEU A N 1 ATOM 360 C CA . LEU A 1 52 ? 73.141 10.324 88.859 1.00 59.14 ? 435 LEU A CA 1 ATOM 361 C C . LEU A 1 52 ? 73.427 9.246 89.904 1.00 60.61 ? 435 LEU A C 1 ATOM 362 O O . LEU A 1 52 ? 72.825 9.252 90.974 1.00 61.14 ? 435 LEU A O 1 ATOM 363 C CB . LEU A 1 52 ? 71.641 10.578 88.717 1.00 57.95 ? 435 LEU A CB 1 ATOM 364 C CG . LEU A 1 52 ? 71.281 11.678 87.718 1.00 57.18 ? 435 LEU A CG 1 ATOM 365 C CD1 . LEU A 1 52 ? 69.785 11.675 87.468 1.00 57.41 ? 435 LEU A CD1 1 ATOM 366 C CD2 . LEU A 1 52 ? 71.733 13.048 88.199 1.00 57.13 ? 435 LEU A CD2 1 ATOM 367 N N . ASP A 1 53 ? 74.344 8.331 89.597 1.00 62.23 ? 436 ASP A N 1 ATOM 368 C CA . ASP A 1 53 ? 74.933 7.454 90.603 1.00 64.30 ? 436 ASP A CA 1 ATOM 369 C C . ASP A 1 53 ? 75.638 8.332 91.642 1.00 65.00 ? 436 ASP A C 1 ATOM 370 O O . ASP A 1 53 ? 76.326 9.286 91.289 1.00 64.59 ? 436 ASP A O 1 ATOM 371 C CB . ASP A 1 53 ? 75.920 6.484 89.935 1.00 66.11 ? 436 ASP A CB 1 ATOM 372 C CG . ASP A 1 53 ? 76.776 5.722 90.935 1.00 67.90 ? 436 ASP A CG 1 ATOM 373 O OD1 . ASP A 1 53 ? 76.280 4.741 91.532 1.00 69.55 ? 436 ASP A OD1 1 ATOM 374 O OD2 . ASP A 1 53 ? 77.949 6.109 91.122 1.00 68.28 ? 436 ASP A OD2 1 ATOM 375 N N . ILE A 1 54 ? 75.441 8.012 92.917 1.00 67.62 ? 437 ILE A N 1 ATOM 376 C CA . ILE A 1 54 ? 75.973 8.816 94.028 1.00 68.97 ? 437 ILE A CA 1 ATOM 377 C C . ILE A 1 54 ? 77.478 9.074 93.907 1.00 69.13 ? 437 ILE A C 1 ATOM 378 O O . ILE A 1 54 ? 77.931 10.183 94.177 1.00 70.15 ? 437 ILE A O 1 ATOM 379 C CB . ILE A 1 54 ? 75.627 8.180 95.417 1.00 70.79 ? 437 ILE A CB 1 ATOM 380 C CG1 . ILE A 1 54 ? 75.991 9.101 96.589 1.00 70.90 ? 437 ILE A CG1 1 ATOM 381 C CG2 . ILE A 1 54 ? 76.336 6.847 95.628 1.00 71.89 ? 437 ILE A CG2 1 ATOM 382 C CD1 . ILE A 1 54 ? 75.218 10.395 96.639 1.00 70.34 ? 437 ILE A CD1 1 ATOM 383 N N . GLN A 1 55 ? 78.240 8.059 93.503 1.00 69.83 ? 438 GLN A N 1 ATOM 384 C CA . GLN A 1 55 ? 79.702 8.175 93.431 1.00 70.30 ? 438 GLN A CA 1 ATOM 385 C C . GLN A 1 55 ? 80.162 9.020 92.257 1.00 66.29 ? 438 GLN A C 1 ATOM 386 O O . GLN A 1 55 ? 81.128 9.783 92.385 1.00 64.18 ? 438 GLN A O 1 ATOM 387 C CB . GLN A 1 55 ? 80.373 6.786 93.392 1.00 74.35 ? 438 GLN A CB 1 ATOM 388 C CG . GLN A 1 55 ? 80.308 6.034 94.716 1.00 78.25 ? 438 GLN A CG 1 ATOM 389 C CD . GLN A 1 55 ? 80.904 6.835 95.871 1.00 81.96 ? 438 GLN A CD 1 ATOM 390 O OE1 . GLN A 1 55 ? 81.960 7.469 95.727 1.00 83.48 ? 438 GLN A OE1 1 ATOM 391 N NE2 . GLN A 1 55 ? 80.216 6.835 97.014 1.00 84.77 ? 438 GLN A NE2 1 ATOM 392 N N . ILE A 1 56 ? 79.474 8.896 91.120 1.00 64.63 ? 439 ILE A N 1 ATOM 393 C CA . ILE A 1 56 ? 79.806 9.742 89.965 1.00 63.42 ? 439 ILE A CA 1 ATOM 394 C C . ILE A 1 56 ? 79.464 11.217 90.287 1.00 59.83 ? 439 ILE A C 1 ATOM 395 O O . ILE A 1 56 ? 80.229 12.096 89.941 1.00 57.04 ? 439 ILE A O 1 ATOM 396 C CB . ILE A 1 56 ? 79.373 9.213 88.552 1.00 64.34 ? 439 ILE A CB 1 ATOM 397 C CG1 . ILE A 1 56 ? 78.157 9.932 87.999 1.00 64.08 ? 439 ILE A CG1 1 ATOM 398 C CG2 . ILE A 1 56 ? 79.307 7.690 88.427 1.00 65.47 ? 439 ILE A CG2 1 ATOM 399 C CD1 . ILE A 1 56 ? 78.577 11.132 87.183 1.00 64.36 ? 439 ILE A CD1 1 ATOM 400 N N . LEU A 1 57 ? 78.383 11.475 91.022 1.00 59.40 ? 440 LEU A N 1 ATOM 401 C CA . LEU A 1 57 ? 78.093 12.839 91.484 1.00 59.26 ? 440 LEU A CA 1 ATOM 402 C C . LEU A 1 57 ? 79.190 13.416 92.378 1.00 60.55 ? 440 LEU A C 1 ATOM 403 O O . LEU A 1 57 ? 79.553 14.589 92.223 1.00 61.04 ? 440 LEU A O 1 ATOM 404 C CB . LEU A 1 57 ? 76.733 12.931 92.194 1.00 58.61 ? 440 LEU A CB 1 ATOM 405 C CG . LEU A 1 57 ? 75.499 12.772 91.297 1.00 57.84 ? 440 LEU A CG 1 ATOM 406 C CD1 . LEU A 1 57 ? 74.245 12.695 92.144 1.00 57.53 ? 440 LEU A CD1 1 ATOM 407 C CD2 . LEU A 1 57 ? 75.375 13.902 90.287 1.00 57.24 ? 440 LEU A CD2 1 ATOM 408 N N . HIS A 1 58 ? 79.709 12.602 93.301 1.00 61.21 ? 441 HIS A N 1 ATOM 409 C CA . HIS A 1 58 ? 80.855 13.001 94.136 1.00 61.31 ? 441 HIS A CA 1 ATOM 410 C C . HIS A 1 58 ? 82.073 13.330 93.267 1.00 60.79 ? 441 HIS A C 1 ATOM 411 O O . HIS A 1 58 ? 82.770 14.313 93.507 1.00 59.83 ? 441 HIS A O 1 ATOM 412 C CB . HIS A 1 58 ? 81.239 11.902 95.140 1.00 62.12 ? 441 HIS A CB 1 ATOM 413 C CG . HIS A 1 58 ? 80.317 11.779 96.316 1.00 61.25 ? 441 HIS A CG 1 ATOM 414 N ND1 . HIS A 1 58 ? 80.187 12.760 97.273 1.00 60.81 ? 441 HIS A ND1 1 ATOM 415 C CD2 . HIS A 1 58 ? 79.523 10.761 96.722 1.00 61.86 ? 441 HIS A CD2 1 ATOM 416 C CE1 . HIS A 1 58 ? 79.333 12.367 98.199 1.00 60.96 ? 441 HIS A CE1 1 ATOM 417 N NE2 . HIS A 1 58 ? 78.914 11.156 97.889 1.00 61.22 ? 441 HIS A NE2 1 ATOM 418 N N . GLN A 1 59 ? 82.317 12.496 92.262 1.00 61.39 ? 442 GLN A N 1 ATOM 419 C CA . GLN A 1 59 ? 83.429 12.705 91.330 1.00 62.05 ? 442 GLN A CA 1 ATOM 420 C C . GLN A 1 59 ? 83.247 13.948 90.459 1.00 60.80 ? 442 GLN A C 1 ATOM 421 O O . GLN A 1 59 ? 84.208 14.688 90.210 1.00 61.64 ? 442 GLN A O 1 ATOM 422 C CB . GLN A 1 59 ? 83.618 11.474 90.450 1.00 62.75 ? 442 GLN A CB 1 ATOM 423 C CG . GLN A 1 59 ? 84.173 10.290 91.221 1.00 64.36 ? 442 GLN A CG 1 ATOM 424 C CD . GLN A 1 59 ? 84.058 8.988 90.457 1.00 64.27 ? 442 GLN A CD 1 ATOM 425 O OE1 . GLN A 1 59 ? 84.395 8.919 89.273 1.00 63.76 ? 442 GLN A OE1 1 ATOM 426 N NE2 . GLN A 1 59 ? 83.602 7.939 91.135 1.00 64.89 ? 442 GLN A NE2 1 ATOM 427 N N . VAL A 1 60 ? 82.015 14.181 90.012 1.00 59.48 ? 443 VAL A N 1 ATOM 428 C CA . VAL A 1 60 ? 81.686 15.389 89.257 1.00 57.72 ? 443 VAL A CA 1 ATOM 429 C C . VAL A 1 60 ? 81.817 16.634 90.155 1.00 57.87 ? 443 VAL A C 1 ATOM 430 O O . VAL A 1 60 ? 82.262 17.687 89.692 1.00 56.98 ? 443 VAL A O 1 ATOM 431 C CB . VAL A 1 60 ? 80.305 15.276 88.582 1.00 55.68 ? 443 VAL A CB 1 ATOM 432 C CG1 . VAL A 1 60 ? 79.887 16.586 87.943 1.00 54.63 ? 443 VAL A CG1 1 ATOM 433 C CG2 . VAL A 1 60 ? 80.346 14.202 87.506 1.00 55.38 ? 443 VAL A CG2 1 ATOM 434 N N . LEU A 1 61 ? 81.476 16.510 91.437 1.00 57.79 ? 444 LEU A N 1 ATOM 435 C CA . LEU A 1 61 ? 81.669 17.626 92.363 1.00 57.97 ? 444 LEU A CA 1 ATOM 436 C C . LEU A 1 61 ? 83.144 17.987 92.528 1.00 59.43 ? 444 LEU A C 1 ATOM 437 O O . LEU A 1 61 ? 83.473 19.167 92.661 1.00 61.82 ? 444 LEU A O 1 ATOM 438 C CB . LEU A 1 61 ? 81.031 17.348 93.728 1.00 57.60 ? 444 LEU A CB 1 ATOM 439 C CG . LEU A 1 61 ? 81.172 18.456 94.780 1.00 57.89 ? 444 LEU A CG 1 ATOM 440 C CD1 . LEU A 1 61 ? 80.646 19.798 94.289 1.00 56.89 ? 444 LEU A CD1 1 ATOM 441 C CD2 . LEU A 1 61 ? 80.447 18.057 96.050 1.00 58.90 ? 444 LEU A CD2 1 ATOM 442 N N . ASP A 1 62 ? 84.020 16.982 92.541 1.00 61.97 ? 445 ASP A N 1 ATOM 443 C CA . ASP A 1 62 ? 85.472 17.216 92.671 1.00 62.45 ? 445 ASP A CA 1 ATOM 444 C C . ASP A 1 62 ? 86.024 17.935 91.447 1.00 61.29 ? 445 ASP A C 1 ATOM 445 O O . ASP A 1 62 ? 86.826 18.859 91.585 1.00 60.39 ? 445 ASP A O 1 ATOM 446 C CB . ASP A 1 62 ? 86.238 15.908 92.914 1.00 62.77 ? 445 ASP A CB 1 ATOM 447 C CG . ASP A 1 62 ? 86.086 15.389 94.337 1.00 63.81 ? 445 ASP A CG 1 ATOM 448 O OD1 . ASP A 1 62 ? 85.934 16.202 95.273 1.00 61.99 ? 445 ASP A OD1 1 ATOM 449 O OD2 . ASP A 1 62 ? 86.129 14.151 94.518 1.00 66.35 ? 445 ASP A OD2 1 ATOM 450 N N . LEU A 1 63 ? 85.576 17.507 90.266 1.00 60.50 ? 446 LEU A N 1 ATOM 451 C CA . LEU A 1 63 ? 85.838 18.225 89.013 1.00 59.95 ? 446 LEU A CA 1 ATOM 452 C C . LEU A 1 63 ? 85.423 19.692 89.116 1.00 58.34 ? 446 LEU A C 1 ATOM 453 O O . LEU A 1 63 ? 86.195 20.593 88.791 1.00 56.17 ? 446 LEU A O 1 ATOM 454 C CB . LEU A 1 63 ? 85.096 17.557 87.851 1.00 59.43 ? 446 LEU A CB 1 ATOM 455 C CG . LEU A 1 63 ? 85.110 18.249 86.484 1.00 59.41 ? 446 LEU A CG 1 ATOM 456 C CD1 . LEU A 1 63 ? 86.528 18.381 85.957 1.00 60.30 ? 446 LEU A CD1 1 ATOM 457 C CD2 . LEU A 1 63 ? 84.251 17.475 85.495 1.00 59.46 ? 446 LEU A CD2 1 ATOM 458 N N . GLN A 1 64 ? 84.205 19.906 89.599 1.00 57.49 ? 447 GLN A N 1 ATOM 459 C CA . GLN A 1 64 ? 83.627 21.251 89.726 1.00 57.97 ? 447 GLN A CA 1 ATOM 460 C C . GLN A 1 64 ? 84.422 22.139 90.681 1.00 58.37 ? 447 GLN A C 1 ATOM 461 O O . GLN A 1 64 ? 84.735 23.288 90.355 1.00 57.32 ? 447 GLN A O 1 ATOM 462 C CB . GLN A 1 64 ? 82.180 21.142 90.202 1.00 57.83 ? 447 GLN A CB 1 ATOM 463 C CG . GLN A 1 64 ? 81.329 22.370 89.992 1.00 58.21 ? 447 GLN A CG 1 ATOM 464 C CD . GLN A 1 64 ? 79.881 22.078 90.326 1.00 58.68 ? 447 GLN A CD 1 ATOM 465 O OE1 . GLN A 1 64 ? 79.172 21.455 89.538 1.00 60.75 ? 447 GLN A OE1 1 ATOM 466 N NE2 . GLN A 1 64 ? 79.430 22.530 91.492 1.00 59.43 ? 447 GLN A NE2 1 ATOM 467 N N . ILE A 1 65 ? 84.752 21.591 91.849 1.00 59.44 ? 448 ILE A N 1 ATOM 468 C CA . ILE A 1 65 ? 85.559 22.297 92.849 1.00 59.81 ? 448 ILE A CA 1 ATOM 469 C C . ILE A 1 65 ? 86.941 22.623 92.295 1.00 59.93 ? 448 ILE A C 1 ATOM 470 O O . ILE A 1 65 ? 87.472 23.696 92.567 1.00 60.55 ? 448 ILE A O 1 ATOM 471 C CB . ILE A 1 65 ? 85.668 21.490 94.171 1.00 61.14 ? 448 ILE A CB 1 ATOM 472 C CG1 . ILE A 1 65 ? 84.311 21.494 94.890 1.00 61.14 ? 448 ILE A CG1 1 ATOM 473 C CG2 . ILE A 1 65 ? 86.743 22.059 95.099 1.00 61.47 ? 448 ILE A CG2 1 ATOM 474 C CD1 . ILE A 1 65 ? 84.157 20.429 95.955 1.00 62.05 ? 448 ILE A CD1 1 ATOM 475 N N . ALA A 1 66 ? 87.513 21.701 91.524 1.00 60.70 ? 449 ALA A N 1 ATOM 476 C CA . ALA A 1 66 ? 88.838 21.906 90.943 1.00 60.92 ? 449 ALA A CA 1 ATOM 477 C C . ALA A 1 66 ? 88.822 23.039 89.912 1.00 62.34 ? 449 ALA A C 1 ATOM 478 O O . ALA A 1 66 ? 89.742 23.862 89.883 1.00 63.67 ? 449 ALA A O 1 ATOM 479 C CB . ALA A 1 66 ? 89.353 20.622 90.328 1.00 59.97 ? 449 ALA A CB 1 ATOM 480 N N . ILE A 1 67 ? 87.766 23.083 89.097 1.00 62.74 ? 450 ILE A N 1 ATOM 481 C CA . ILE A 1 67 ? 87.533 24.181 88.146 1.00 63.19 ? 450 ILE A CA 1 ATOM 482 C C . ILE A 1 67 ? 87.454 25.545 88.852 1.00 65.13 ? 450 ILE A C 1 ATOM 483 O O . ILE A 1 67 ? 88.083 26.504 88.401 1.00 64.25 ? 450 ILE A O 1 ATOM 484 C CB . ILE A 1 67 ? 86.273 23.924 87.273 1.00 61.72 ? 450 ILE A CB 1 ATOM 485 C CG1 . ILE A 1 67 ? 86.544 22.789 86.271 1.00 61.78 ? 450 ILE A CG1 1 ATOM 486 C CG2 . ILE A 1 67 ? 85.851 25.178 86.513 1.00 61.53 ? 450 ILE A CG2 1 ATOM 487 C CD1 . ILE A 1 67 ? 85.296 22.144 85.699 1.00 61.28 ? 450 ILE A CD1 1 ATOM 488 N N . GLU A 1 68 ? 86.694 25.626 89.947 1.00 67.43 ? 451 GLU A N 1 ATOM 489 C CA . GLU A 1 68 ? 86.616 26.856 90.759 1.00 70.22 ? 451 GLU A CA 1 ATOM 490 C C . GLU A 1 68 ? 87.976 27.337 91.254 1.00 71.68 ? 451 GLU A C 1 ATOM 491 O O . GLU A 1 68 ? 88.186 28.545 91.410 1.00 73.03 ? 451 GLU A O 1 ATOM 492 C CB . GLU A 1 68 ? 85.730 26.659 91.988 1.00 72.17 ? 451 GLU A CB 1 ATOM 493 C CG . GLU A 1 68 ? 84.250 26.551 91.707 1.00 72.86 ? 451 GLU A CG 1 ATOM 494 C CD . GLU A 1 68 ? 83.440 26.494 92.989 1.00 75.99 ? 451 GLU A CD 1 ATOM 495 O OE1 . GLU A 1 68 ? 83.354 27.532 93.682 1.00 76.69 ? 451 GLU A OE1 1 ATOM 496 O OE2 . GLU A 1 68 ? 82.885 25.415 93.301 1.00 80.30 ? 451 GLU A OE2 1 ATOM 497 N N . ASN A 1 69 ? 88.870 26.388 91.521 1.00 72.14 ? 452 ASN A N 1 ATOM 498 C CA . ASN A 1 69 ? 90.204 26.671 92.044 1.00 73.76 ? 452 ASN A CA 1 ATOM 499 C C . ASN A 1 69 ? 91.271 26.945 90.970 1.00 71.49 ? 452 ASN A C 1 ATOM 500 O O . ASN A 1 69 ? 92.397 27.284 91.322 1.00 72.73 ? 452 ASN A O 1 ATOM 501 C CB . ASN A 1 69 ? 90.663 25.504 92.939 1.00 76.54 ? 452 ASN A CB 1 ATOM 502 C CG . ASN A 1 69 ? 91.626 25.945 94.027 1.00 79.66 ? 452 ASN A CG 1 ATOM 503 O OD1 . ASN A 1 69 ? 91.348 26.904 94.746 1.00 83.37 ? 452 ASN A OD1 1 ATOM 504 N ND2 . ASN A 1 69 ? 92.754 25.245 94.165 1.00 81.02 ? 452 ASN A ND2 1 ATOM 505 N N . ILE A 1 70 ? 90.940 26.799 89.684 1.00 68.67 ? 453 ILE A N 1 ATOM 506 C CA . ILE A 1 70 ? 91.898 27.076 88.606 1.00 68.14 ? 453 ILE A CA 1 ATOM 507 C C . ILE A 1 70 ? 92.312 28.539 88.641 1.00 70.21 ? 453 ILE A C 1 ATOM 508 O O . ILE A 1 70 ? 91.472 29.427 88.815 1.00 70.90 ? 453 ILE A O 1 ATOM 509 C CB . ILE A 1 70 ? 91.334 26.782 87.200 1.00 65.62 ? 453 ILE A CB 1 ATOM 510 C CG1 . ILE A 1 70 ? 91.144 25.277 86.999 1.00 64.56 ? 453 ILE A CG1 1 ATOM 511 C CG2 . ILE A 1 70 ? 92.264 27.323 86.114 1.00 66.21 ? 453 ILE A CG2 1 ATOM 512 C CD1 . ILE A 1 70 ? 90.277 24.925 85.811 1.00 63.31 ? 453 ILE A CD1 1 ATOM 513 N N . THR A 1 71 ? 93.614 28.765 88.479 1.00 72.67 ? 454 THR A N 1 ATOM 514 C CA . THR A 1 71 ? 94.178 30.101 88.370 1.00 73.06 ? 454 THR A CA 1 ATOM 515 C C . THR A 1 71 ? 95.052 30.181 87.121 1.00 72.98 ? 454 THR A C 1 ATOM 516 O O . THR A 1 71 ? 95.637 29.189 86.691 1.00 72.89 ? 454 THR A O 1 ATOM 517 C CB . THR A 1 71 ? 95.003 30.479 89.616 1.00 75.03 ? 454 THR A CB 1 ATOM 518 O OG1 . THR A 1 71 ? 96.096 29.568 89.771 1.00 76.85 ? 454 THR A OG1 1 ATOM 519 C CG2 . THR A 1 71 ? 94.145 30.429 90.870 1.00 75.50 ? 454 THR A CG2 1 ATOM 520 N N . ALA A 1 72 ? 95.097 31.373 86.538 1.00 73.16 ? 455 ALA A N 1 ATOM 521 C CA . ALA A 1 72 ? 95.983 31.703 85.428 1.00 73.27 ? 455 ALA A CA 1 ATOM 522 C C . ALA A 1 72 ? 96.771 32.951 85.821 1.00 74.71 ? 455 ALA A C 1 ATOM 523 O O . ALA A 1 72 ? 96.352 33.692 86.714 1.00 74.27 ? 455 ALA A O 1 ATOM 524 C CB . ALA A 1 72 ? 95.163 31.963 84.175 1.00 71.64 ? 455 ALA A CB 1 ATOM 525 N N . SER A 1 73 ? 97.910 33.181 85.176 1.00 77.00 ? 456 SER A N 1 ATOM 526 C CA . SER A 1 73 ? 98.677 34.415 85.392 1.00 80.74 ? 456 SER A CA 1 ATOM 527 C C . SER A 1 73 ? 98.697 35.271 84.131 1.00 82.67 ? 456 SER A C 1 ATOM 528 O O . SER A 1 73 ? 98.792 34.758 83.022 1.00 80.77 ? 456 SER A O 1 ATOM 529 C CB . SER A 1 73 ? 100.096 34.116 85.887 1.00 82.01 ? 456 SER A CB 1 ATOM 530 O OG . SER A 1 73 ? 100.697 33.080 85.147 1.00 83.57 ? 456 SER A OG 1 ATOM 531 N N . TYR A 1 74 ? 98.560 36.579 84.316 1.00 88.57 ? 457 TYR A N 1 ATOM 532 C CA . TYR A 1 74 ? 98.622 37.531 83.216 1.00 95.35 ? 457 TYR A CA 1 ATOM 533 C C . TYR A 1 74 ? 99.389 38.754 83.703 1.00 102.15 ? 457 TYR A C 1 ATOM 534 O O . TYR A 1 74 ? 99.002 39.373 84.699 1.00 102.61 ? 457 TYR A O 1 ATOM 535 C CB . TYR A 1 74 ? 97.221 37.912 82.742 1.00 95.77 ? 457 TYR A CB 1 ATOM 536 C CG . TYR A 1 74 ? 97.241 38.769 81.504 1.00 98.04 ? 457 TYR A CG 1 ATOM 537 C CD1 . TYR A 1 74 ? 97.144 40.162 81.595 1.00 99.92 ? 457 TYR A CD1 1 ATOM 538 C CD2 . TYR A 1 74 ? 97.386 38.194 80.238 1.00 98.88 ? 457 TYR A CD2 1 ATOM 539 C CE1 . TYR A 1 74 ? 97.180 40.956 80.457 1.00 101.96 ? 457 TYR A CE1 1 ATOM 540 C CE2 . TYR A 1 74 ? 97.423 38.977 79.091 1.00 101.37 ? 457 TYR A CE2 1 ATOM 541 C CZ . TYR A 1 74 ? 97.321 40.359 79.205 1.00 103.06 ? 457 TYR A CZ 1 ATOM 542 O OH . TYR A 1 74 ? 97.363 41.143 78.075 1.00 105.27 ? 457 TYR A OH 1 ATOM 543 N N . ASP A 1 75 ? 100.460 39.098 82.981 1.00 110.53 ? 458 ASP A N 1 ATOM 544 C CA . ASP A 1 75 ? 101.562 39.914 83.515 1.00 115.92 ? 458 ASP A CA 1 ATOM 545 C C . ASP A 1 75 ? 102.059 39.231 84.807 1.00 118.07 ? 458 ASP A C 1 ATOM 546 O O . ASP A 1 75 ? 102.332 38.026 84.779 1.00 118.44 ? 458 ASP A O 1 ATOM 547 C CB . ASP A 1 75 ? 101.151 41.390 83.694 1.00 117.43 ? 458 ASP A CB 1 ATOM 548 C CG . ASP A 1 75 ? 100.719 42.049 82.390 1.00 118.61 ? 458 ASP A CG 1 ATOM 549 O OD1 . ASP A 1 75 ? 100.759 41.394 81.323 1.00 119.65 ? 458 ASP A OD1 1 ATOM 550 O OD2 . ASP A 1 75 ? 100.345 43.240 82.433 1.00 119.96 ? 458 ASP A OD2 1 ATOM 551 N N . ASN A 1 76 ? 102.151 39.955 85.924 1.00 119.73 ? 459 ASN A N 1 ATOM 552 C CA . ASN A 1 76 ? 102.545 39.355 87.202 1.00 121.13 ? 459 ASN A CA 1 ATOM 553 C C . ASN A 1 76 ? 101.317 39.021 88.071 1.00 118.97 ? 459 ASN A C 1 ATOM 554 O O . ASN A 1 76 ? 101.456 38.363 89.105 1.00 119.33 ? 459 ASN A O 1 ATOM 555 C CB . ASN A 1 76 ? 103.519 40.299 87.947 1.00 123.71 ? 459 ASN A CB 1 ATOM 556 C CG . ASN A 1 76 ? 104.702 39.568 88.586 1.00 123.81 ? 459 ASN A CG 1 ATOM 557 O OD1 . ASN A 1 76 ? 105.026 38.426 88.242 1.00 122.80 ? 459 ASN A OD1 1 ATOM 558 N ND2 . ASN A 1 76 ? 105.368 40.246 89.511 1.00 124.68 ? 459 ASN A ND2 1 ATOM 559 N N . GLU A 1 77 ? 100.125 39.447 87.637 1.00 116.76 ? 460 GLU A N 1 ATOM 560 C CA . GLU A 1 77 ? 98.877 39.212 88.378 1.00 113.37 ? 460 GLU A CA 1 ATOM 561 C C . GLU A 1 77 ? 98.434 37.741 88.303 1.00 106.53 ? 460 GLU A C 1 ATOM 562 O O . GLU A 1 77 ? 98.883 36.985 87.431 1.00 104.08 ? 460 GLU A O 1 ATOM 563 C CB . GLU A 1 77 ? 97.738 40.089 87.827 1.00 116.05 ? 460 GLU A CB 1 ATOM 564 C CG . GLU A 1 77 ? 97.966 41.601 87.852 1.00 118.85 ? 460 GLU A CG 1 ATOM 565 C CD . GLU A 1 77 ? 96.801 42.389 87.246 1.00 120.45 ? 460 GLU A CD 1 ATOM 566 O OE1 . GLU A 1 77 ? 96.127 41.883 86.315 1.00 119.90 ? 460 GLU A OE1 1 ATOM 567 O OE2 . GLU A 1 77 ? 96.557 43.530 87.696 1.00 121.22 ? 460 GLU A OE2 1 ATOM 568 N N . THR A 1 78 ? 97.543 37.361 89.221 1.00 99.82 ? 461 THR A N 1 ATOM 569 C CA . THR A 1 78 ? 96.857 36.059 89.193 1.00 95.10 ? 461 THR A CA 1 ATOM 570 C C . THR A 1 78 ? 95.372 36.270 88.891 1.00 88.46 ? 461 THR A C 1 ATOM 571 O O . THR A 1 78 ? 94.739 37.174 89.440 1.00 85.56 ? 461 THR A O 1 ATOM 572 C CB . THR A 1 78 ? 97.007 35.262 90.506 1.00 95.87 ? 461 THR A CB 1 ATOM 573 O OG1 . THR A 1 78 ? 96.583 36.057 91.615 1.00 96.90 ? 461 THR A OG1 1 ATOM 574 C CG2 . THR A 1 78 ? 98.457 34.819 90.719 1.00 97.75 ? 461 THR A CG2 1 ATOM 575 N N . VAL A 1 79 ? 94.829 35.429 88.013 1.00 83.61 ? 462 VAL A N 1 ATOM 576 C CA . VAL A 1 79 ? 93.425 35.493 87.615 1.00 80.54 ? 462 VAL A CA 1 ATOM 577 C C . VAL A 1 79 ? 92.684 34.258 88.125 1.00 76.95 ? 462 VAL A C 1 ATOM 578 O O . VAL A 1 79 ? 93.027 33.125 87.764 1.00 73.32 ? 462 VAL A O 1 ATOM 579 C CB . VAL A 1 79 ? 93.266 35.581 86.083 1.00 80.34 ? 462 VAL A CB 1 ATOM 580 C CG1 . VAL A 1 79 ? 91.808 35.837 85.720 1.00 79.39 ? 462 VAL A CG1 1 ATOM 581 C CG2 . VAL A 1 79 ? 94.150 36.683 85.511 1.00 81.47 ? 462 VAL A CG2 1 ATOM 582 N N . THR A 1 80 ? 91.669 34.494 88.956 1.00 73.90 ? 463 THR A N 1 ATOM 583 C CA . THR A 1 80 ? 90.777 33.439 89.441 1.00 73.30 ? 463 THR A CA 1 ATOM 584 C C . THR A 1 80 ? 89.442 33.519 88.717 1.00 70.06 ? 463 THR A C 1 ATOM 585 O O . THR A 1 80 ? 89.128 34.534 88.090 1.00 69.39 ? 463 THR A O 1 ATOM 586 C CB . THR A 1 80 ? 90.483 33.603 90.940 1.00 75.33 ? 463 THR A CB 1 ATOM 587 O OG1 . THR A 1 80 ? 89.891 34.888 91.177 1.00 76.09 ? 463 THR A OG1 1 ATOM 588 C CG2 . THR A 1 80 ? 91.751 33.470 91.771 1.00 76.33 ? 463 THR A CG2 1 ATOM 589 N N . LEU A 1 81 ? 88.651 32.453 88.820 1.00 67.56 ? 464 LEU A N 1 ATOM 590 C CA . LEU A 1 81 ? 87.265 32.472 88.347 1.00 65.43 ? 464 LEU A CA 1 ATOM 591 C C . LEU A 1 81 ? 86.430 33.536 89.083 1.00 66.11 ? 464 LEU A C 1 ATOM 592 O O . LEU A 1 81 ? 85.538 34.140 88.494 1.00 64.75 ? 464 LEU A O 1 ATOM 593 C CB . LEU A 1 81 ? 86.624 31.092 88.503 1.00 64.24 ? 464 LEU A CB 1 ATOM 594 C CG . LEU A 1 81 ? 85.179 30.930 88.038 1.00 63.37 ? 464 LEU A CG 1 ATOM 595 C CD1 . LEU A 1 81 ? 85.015 31.300 86.572 1.00 62.95 ? 464 LEU A CD1 1 ATOM 596 C CD2 . LEU A 1 81 ? 84.734 29.499 88.285 1.00 63.76 ? 464 LEU A CD2 1 ATOM 597 N N . GLN A 1 82 ? 86.754 33.787 90.349 1.00 67.20 ? 465 GLN A N 1 ATOM 598 C CA . GLN A 1 82 ? 86.016 34.748 91.169 1.00 66.96 ? 465 GLN A CA 1 ATOM 599 C C . GLN A 1 82 ? 86.188 36.191 90.674 1.00 66.90 ? 465 GLN A C 1 ATOM 600 O O . GLN A 1 82 ? 85.305 37.025 90.877 1.00 66.77 ? 465 GLN A O 1 ATOM 601 C CB . GLN A 1 82 ? 86.405 34.616 92.647 1.00 68.72 ? 465 GLN A CB 1 ATOM 602 C CG . GLN A 1 82 ? 85.984 33.295 93.301 1.00 69.50 ? 465 GLN A CG 1 ATOM 603 C CD . GLN A 1 82 ? 86.885 32.102 92.958 1.00 70.88 ? 465 GLN A CD 1 ATOM 604 O OE1 . GLN A 1 82 ? 86.412 31.060 92.504 1.00 71.60 ? 465 GLN A OE1 1 ATOM 605 N NE2 . GLN A 1 82 ? 88.188 32.249 93.185 1.00 72.95 ? 465 GLN A NE2 1 ATOM 606 N N . ASP A 1 83 ? 87.307 36.470 90.009 1.00 67.76 ? 466 ASP A N 1 ATOM 607 C CA . ASP A 1 83 ? 87.535 37.773 89.377 1.00 68.61 ? 466 ASP A CA 1 ATOM 608 C C . ASP A 1 83 ? 86.669 38.035 88.144 1.00 67.63 ? 466 ASP A C 1 ATOM 609 O O . ASP A 1 83 ? 86.374 39.189 87.841 1.00 68.50 ? 466 ASP A O 1 ATOM 610 C CB . ASP A 1 83 ? 89.004 37.926 88.967 1.00 70.47 ? 466 ASP A CB 1 ATOM 611 C CG . ASP A 1 83 ? 89.953 37.913 90.152 1.00 73.05 ? 466 ASP A CG 1 ATOM 612 O OD1 . ASP A 1 83 ? 89.609 38.477 91.220 1.00 72.48 ? 466 ASP A OD1 1 ATOM 613 O OD2 . ASP A 1 83 ? 91.058 37.343 89.999 1.00 75.84 ? 466 ASP A OD2 1 ATOM 614 N N . ILE A 1 84 ? 86.282 36.981 87.429 1.00 66.39 ? 467 ILE A N 1 ATOM 615 C CA . ILE A 1 84 ? 85.608 37.133 86.140 1.00 65.07 ? 467 ILE A CA 1 ATOM 616 C C . ILE A 1 84 ? 84.164 36.643 86.093 1.00 63.15 ? 467 ILE A C 1 ATOM 617 O O . ILE A 1 84 ? 83.487 36.875 85.095 1.00 63.02 ? 467 ILE A O 1 ATOM 618 C CB . ILE A 1 84 ? 86.424 36.465 85.005 1.00 66.66 ? 467 ILE A CB 1 ATOM 619 C CG1 . ILE A 1 84 ? 86.524 34.941 85.177 1.00 65.89 ? 467 ILE A CG1 1 ATOM 620 C CG2 . ILE A 1 84 ? 87.823 37.074 84.941 1.00 68.11 ? 467 ILE A CG2 1 ATOM 621 C CD1 . ILE A 1 84 ? 87.189 34.253 84.010 1.00 65.99 ? 467 ILE A CD1 1 ATOM 622 N N . CYS A 1 85 ? 83.690 35.980 87.150 1.00 62.67 ? 468 CYS A N 1 ATOM 623 C CA . CYS A 1 85 ? 82.399 35.290 87.113 1.00 60.90 ? 468 CYS A CA 1 ATOM 624 C C . CYS A 1 85 ? 81.215 36.201 87.428 1.00 59.90 ? 468 CYS A C 1 ATOM 625 O O . CYS A 1 85 ? 81.373 37.330 87.910 1.00 60.08 ? 468 CYS A O 1 ATOM 626 C CB . CYS A 1 85 ? 82.381 34.108 88.084 1.00 61.46 ? 468 CYS A CB 1 ATOM 627 S SG . CYS A 1 85 ? 82.354 34.559 89.839 1.00 66.21 ? 468 CYS A SG 1 ATOM 628 N N . LEU A 1 86 ? 80.029 35.678 87.125 1.00 57.50 ? 469 LEU A N 1 ATOM 629 C CA . LEU A 1 86 ? 78.772 36.254 87.546 1.00 56.82 ? 469 LEU A CA 1 ATOM 630 C C . LEU A 1 86 ? 78.514 35.794 88.987 1.00 57.31 ? 469 LEU A C 1 ATOM 631 O O . LEU A 1 86 ? 78.380 34.599 89.243 1.00 54.88 ? 469 LEU A O 1 ATOM 632 C CB . LEU A 1 86 ? 77.645 35.794 86.614 1.00 55.62 ? 469 LEU A CB 1 ATOM 633 C CG . LEU A 1 86 ? 76.209 36.233 86.910 1.00 55.11 ? 469 LEU A CG 1 ATOM 634 C CD1 . LEU A 1 86 ? 76.052 37.743 86.963 1.00 55.16 ? 469 LEU A CD1 1 ATOM 635 C CD2 . LEU A 1 86 ? 75.287 35.641 85.864 1.00 54.73 ? 469 LEU A CD2 1 ATOM 636 N N . ALA A 1 87 ? 78.438 36.752 89.912 1.00 57.89 ? 470 ALA A N 1 ATOM 637 C CA . ALA A 1 87 ? 78.267 36.464 91.328 1.00 56.97 ? 470 ALA A CA 1 ATOM 638 C C . ALA A 1 87 ? 77.212 37.393 91.936 1.00 55.50 ? 470 ALA A C 1 ATOM 639 O O . ALA A 1 87 ? 77.551 38.394 92.527 1.00 57.26 ? 470 ALA A O 1 ATOM 640 C CB . ALA A 1 87 ? 79.600 36.604 92.030 1.00 58.16 ? 470 ALA A CB 1 ATOM 641 N N . PRO A 1 88 ? 75.920 37.050 91.793 1.00 54.47 ? 471 PRO A N 1 ATOM 642 C CA . PRO A 1 88 ? 74.841 37.997 92.076 1.00 55.39 ? 471 PRO A CA 1 ATOM 643 C C . PRO A 1 88 ? 74.426 38.190 93.540 1.00 57.19 ? 471 PRO A C 1 ATOM 644 O O . PRO A 1 88 ? 73.457 38.911 93.784 1.00 55.97 ? 471 PRO A O 1 ATOM 645 C CB . PRO A 1 88 ? 73.669 37.419 91.274 1.00 54.31 ? 471 PRO A CB 1 ATOM 646 C CG . PRO A 1 88 ? 73.907 35.959 91.294 1.00 53.61 ? 471 PRO A CG 1 ATOM 647 C CD . PRO A 1 88 ? 75.397 35.792 91.229 1.00 54.30 ? 471 PRO A CD 1 ATOM 648 N N . LEU A 1 89 ? 75.121 37.569 94.495 1.00 60.12 ? 472 LEU A N 1 ATOM 649 C CA . LEU A 1 89 ? 74.807 37.773 95.916 1.00 62.70 ? 472 LEU A CA 1 ATOM 650 C C . LEU A 1 89 ? 75.312 39.106 96.452 1.00 66.69 ? 472 LEU A C 1 ATOM 651 O O . LEU A 1 89 ? 74.681 39.687 97.341 1.00 67.62 ? 472 LEU A O 1 ATOM 652 C CB . LEU A 1 89 ? 75.319 36.622 96.791 1.00 62.54 ? 472 LEU A CB 1 ATOM 653 C CG . LEU A 1 89 ? 74.356 35.434 96.888 1.00 62.08 ? 472 LEU A CG 1 ATOM 654 C CD1 . LEU A 1 89 ? 75.079 34.209 97.400 1.00 62.81 ? 472 LEU A CD1 1 ATOM 655 C CD2 . LEU A 1 89 ? 73.160 35.743 97.772 1.00 62.67 ? 472 LEU A CD2 1 ATOM 656 N N . SER A 1 90 ? 76.422 39.596 95.907 1.00 70.68 ? 473 SER A N 1 ATOM 657 C CA . SER A 1 90 ? 76.986 40.872 96.338 1.00 76.76 ? 473 SER A CA 1 ATOM 658 C C . SER A 1 90 ? 77.773 41.526 95.182 1.00 79.55 ? 473 SER A C 1 ATOM 659 O O . SER A 1 90 ? 78.224 40.815 94.285 1.00 80.38 ? 473 SER A O 1 ATOM 660 C CB . SER A 1 90 ? 77.849 40.665 97.595 1.00 78.85 ? 473 SER A CB 1 ATOM 661 O OG . SER A 1 90 ? 79.088 41.356 97.539 1.00 83.75 ? 473 SER A OG 1 ATOM 662 N N A PRO A 1 91 ? 77.909 42.875 95.188 0.50 82.09 ? 474 PRO A N 1 ATOM 663 N N B PRO A 1 91 ? 77.969 42.862 95.223 0.50 82.35 ? 474 PRO A N 1 ATOM 664 C CA A PRO A 1 91 ? 78.654 43.596 94.131 0.50 83.15 ? 474 PRO A CA 1 ATOM 665 C CA B PRO A 1 91 ? 78.780 43.562 94.204 0.50 83.47 ? 474 PRO A CA 1 ATOM 666 C C A PRO A 1 91 ? 80.129 43.210 93.989 0.50 84.07 ? 474 PRO A C 1 ATOM 667 C C B PRO A 1 91 ? 80.218 43.044 93.994 0.50 84.32 ? 474 PRO A C 1 ATOM 668 O O A PRO A 1 91 ? 80.717 43.441 92.936 0.50 84.37 ? 474 PRO A O 1 ATOM 669 O O B PRO A 1 91 ? 80.817 43.342 92.961 0.50 84.73 ? 474 PRO A O 1 ATOM 670 C CB A PRO A 1 91 ? 78.558 45.064 94.559 0.50 84.37 ? 474 PRO A CB 1 ATOM 671 C CB B PRO A 1 91 ? 78.800 45.006 94.710 0.50 84.79 ? 474 PRO A CB 1 ATOM 672 C CG A PRO A 1 91 ? 77.370 45.143 95.446 0.50 83.95 ? 474 PRO A CG 1 ATOM 673 C CG B PRO A 1 91 ? 77.520 45.148 95.463 0.50 84.40 ? 474 PRO A CG 1 ATOM 674 C CD A PRO A 1 91 ? 77.250 43.811 96.124 0.50 83.00 ? 474 PRO A CD 1 ATOM 675 C CD B PRO A 1 91 ? 77.297 43.817 96.128 0.50 83.33 ? 474 PRO A CD 1 ATOM 676 N N A TYR A 1 92 ? 80.720 42.635 95.033 0.50 85.70 ? 475 TYR A N 1 ATOM 677 N N B TYR A 1 92 ? 80.773 42.299 94.950 0.50 85.83 ? 475 TYR A N 1 ATOM 678 C CA A TYR A 1 92 ? 82.134 42.291 95.009 0.50 87.96 ? 475 TYR A CA 1 ATOM 679 C CA B TYR A 1 92 ? 82.032 41.583 94.703 0.50 87.41 ? 475 TYR A CA 1 ATOM 680 C C A TYR A 1 92 ? 82.345 40.773 95.006 0.50 86.67 ? 475 TYR A C 1 ATOM 681 C C B TYR A 1 92 ? 82.071 40.189 95.345 0.50 85.80 ? 475 TYR A C 1 ATOM 682 O O A TYR A 1 92 ? 81.606 40.037 95.661 0.50 88.18 ? 475 TYR A O 1 ATOM 683 O O B TYR A 1 92 ? 83.117 39.748 95.822 0.50 85.07 ? 475 TYR A O 1 ATOM 684 C CB A TYR A 1 92 ? 82.839 42.928 96.212 0.50 90.26 ? 475 TYR A CB 1 ATOM 685 C CB B TYR A 1 92 ? 83.231 42.408 95.197 0.50 90.94 ? 475 TYR A CB 1 ATOM 686 C CG A TYR A 1 92 ? 82.933 44.440 96.139 0.50 92.01 ? 475 TYR A CG 1 ATOM 687 C CG B TYR A 1 92 ? 83.885 43.282 94.138 0.50 92.08 ? 475 TYR A CG 1 ATOM 688 C CD1 A TYR A 1 92 ? 83.955 45.059 95.425 0.50 93.41 ? 475 TYR A CD1 1 ATOM 689 C CD1 B TYR A 1 92 ? 84.664 42.721 93.131 0.50 91.43 ? 475 TYR A CD1 1 ATOM 690 C CD2 A TYR A 1 92 ? 82.004 45.248 96.785 0.50 92.83 ? 475 TYR A CD2 1 ATOM 691 C CD2 B TYR A 1 92 ? 83.737 44.666 94.158 0.50 93.15 ? 475 TYR A CD2 1 ATOM 692 C CE1 A TYR A 1 92 ? 84.046 46.436 95.355 0.50 94.92 ? 475 TYR A CE1 1 ATOM 693 C CE1 B TYR A 1 92 ? 85.264 43.510 92.170 0.50 91.50 ? 475 TYR A CE1 1 ATOM 694 C CE2 A TYR A 1 92 ? 82.086 46.627 96.720 0.50 94.17 ? 475 TYR A CE2 1 ATOM 695 C CE2 B TYR A 1 92 ? 84.335 45.462 93.199 0.50 93.28 ? 475 TYR A CE2 1 ATOM 696 C CZ A TYR A 1 92 ? 83.109 47.215 96.005 0.50 95.83 ? 475 TYR A CZ 1 ATOM 697 C CZ B TYR A 1 92 ? 85.096 44.876 92.210 0.50 92.90 ? 475 TYR A CZ 1 ATOM 698 O OH A TYR A 1 92 ? 83.197 48.587 95.940 0.50 98.41 ? 475 TYR A OH 1 ATOM 699 O OH B TYR A 1 92 ? 85.696 45.656 91.252 0.50 94.69 ? 475 TYR A OH 1 ATOM 700 N N A ASN A 1 93 ? 83.355 40.310 94.272 0.50 84.91 ? 476 ASN A N 1 ATOM 701 N N B ASN A 1 93 ? 80.940 39.490 95.328 0.50 84.26 ? 476 ASN A N 1 ATOM 702 C CA A ASN A 1 93 ? 83.650 38.881 94.195 0.50 83.73 ? 476 ASN A CA 1 ATOM 703 C CA B ASN A 1 93 ? 80.814 38.210 96.033 0.50 81.83 ? 476 ASN A CA 1 ATOM 704 C C A ASN A 1 93 ? 82.837 38.101 95.218 0.50 84.04 ? 476 ASN A C 1 ATOM 705 C C B ASN A 1 93 ? 81.785 37.164 95.509 0.50 80.84 ? 476 ASN A C 1 ATOM 706 O O A ASN A 1 93 ? 82.578 38.590 96.320 0.50 83.11 ? 476 ASN A O 1 ATOM 707 O O B ASN A 1 93 ? 82.340 37.300 94.416 0.50 80.59 ? 476 ASN A O 1 ATOM 708 C CB A ASN A 1 93 ? 85.137 38.622 94.442 0.50 83.28 ? 476 ASN A CB 1 ATOM 709 C CB B ASN A 1 93 ? 79.392 37.662 95.929 0.50 79.49 ? 476 ASN A CB 1 ATOM 710 C CG A ASN A 1 93 ? 86.021 39.263 93.397 0.50 82.25 ? 476 ASN A CG 1 ATOM 711 C CG B ASN A 1 93 ? 79.200 36.386 96.726 0.50 78.20 ? 476 ASN A CG 1 ATOM 712 O OD1 A ASN A 1 93 ? 85.548 40.011 92.540 0.50 81.10 ? 476 ASN A OD1 1 ATOM 713 O OD1 B ASN A 1 93 ? 79.631 35.311 96.310 0.50 77.93 ? 476 ASN A OD1 1 ATOM 714 N ND2 A ASN A 1 93 ? 87.314 38.973 93.461 0.50 81.84 ? 476 ASN A ND2 1 ATOM 715 N ND2 B ASN A 1 93 ? 78.543 36.497 97.873 0.50 77.64 ? 476 ASN A ND2 1 ATOM 716 N N A THR A 1 94 ? 82.446 36.881 94.857 0.50 83.55 ? 477 THR A N 1 ATOM 717 N N B THR A 1 94 ? 81.966 36.107 96.296 0.50 79.46 ? 477 THR A N 1 ATOM 718 C CA A THR A 1 94 ? 81.725 36.020 95.786 0.50 83.39 ? 477 THR A CA 1 ATOM 719 C CA B THR A 1 94 ? 82.926 35.065 95.964 0.50 77.78 ? 477 THR A CA 1 ATOM 720 C C A THR A 1 94 ? 81.585 34.587 95.282 0.50 81.33 ? 477 THR A C 1 ATOM 721 C C B THR A 1 94 ? 82.247 33.722 95.665 0.50 76.93 ? 477 THR A C 1 ATOM 722 O O A THR A 1 94 ? 82.468 34.029 94.628 0.50 82.52 ? 477 THR A O 1 ATOM 723 O O B THR A 1 94 ? 82.933 32.720 95.440 0.50 74.55 ? 477 THR A O 1 ATOM 724 C CB A THR A 1 94 ? 80.306 36.562 96.063 0.50 83.48 ? 477 THR A CB 1 ATOM 725 C CB B THR A 1 94 ? 83.954 34.879 97.096 0.50 77.13 ? 477 THR A CB 1 ATOM 726 O OG1 A THR A 1 94 ? 80.369 37.962 96.355 0.50 85.62 ? 477 THR A OG1 1 ATOM 727 O OG1 B THR A 1 94 ? 85.170 34.358 96.553 0.50 76.17 ? 477 THR A OG1 1 ATOM 728 C CG2 A THR A 1 94 ? 79.663 35.829 97.235 0.50 83.68 ? 477 THR A CG2 1 ATOM 729 C CG2 B THR A 1 94 ? 83.419 33.938 98.167 0.50 76.78 ? 477 THR A CG2 1 ATOM 730 N N A ASN A 1 95 ? 80.448 33.999 95.612 0.50 78.96 ? 478 ASN A N 1 ATOM 731 N N B ASN A 1 95 ? 80.911 33.698 95.678 0.50 76.13 ? 478 ASN A N 1 ATOM 732 C CA A ASN A 1 95 ? 80.125 32.645 95.231 0.50 77.67 ? 478 ASN A CA 1 ATOM 733 C CA B ASN A 1 95 ? 80.170 32.518 95.228 0.50 75.88 ? 478 ASN A CA 1 ATOM 734 C C A ASN A 1 95 ? 79.713 32.689 93.773 0.50 72.96 ? 478 ASN A C 1 ATOM 735 C C B ASN A 1 95 ? 79.722 32.669 93.779 0.50 71.96 ? 478 ASN A C 1 ATOM 736 O O A ASN A 1 95 ? 78.691 33.286 93.464 0.50 72.01 ? 478 ASN A O 1 ATOM 737 O O B ASN A 1 95 ? 78.697 33.287 93.481 0.50 71.10 ? 478 ASN A O 1 ATOM 738 C CB A ASN A 1 95 ? 78.957 32.191 96.096 0.50 81.02 ? 478 ASN A CB 1 ATOM 739 C CB B ASN A 1 95 ? 78.973 32.209 96.121 0.50 79.46 ? 478 ASN A CB 1 ATOM 740 C CG A ASN A 1 95 ? 79.388 31.443 97.340 0.50 86.50 ? 478 ASN A CG 1 ATOM 741 C CG B ASN A 1 95 ? 79.374 31.459 97.372 0.50 85.24 ? 478 ASN A CG 1 ATOM 742 O OD1 A ASN A 1 95 ? 80.497 30.913 97.413 0.50 87.80 ? 478 ASN A OD1 1 ATOM 743 O OD1 B ASN A 1 95 ? 80.484 30.932 97.457 0.50 86.52 ? 478 ASN A OD1 1 ATOM 744 N ND2 A ASN A 1 95 ? 78.493 31.396 98.333 0.50 93.06 ? 478 ASN A ND2 1 ATOM 745 N ND2 B ASN A 1 95 ? 78.474 31.404 98.348 0.50 92.19 ? 478 ASN A ND2 1 ATOM 746 N N . CYS A 1 96 ? 80.515 32.094 92.885 1.00 69.77 ? 479 CYS A N 1 ATOM 747 C CA . CYS A 1 96 ? 80.266 32.153 91.446 1.00 66.79 ? 479 CYS A CA 1 ATOM 748 C C . CYS A 1 96 ? 79.066 31.326 91.029 1.00 62.30 ? 479 CYS A C 1 ATOM 749 O O . CYS A 1 96 ? 78.777 30.296 91.627 1.00 61.75 ? 479 CYS A O 1 ATOM 750 C CB . CYS A 1 96 ? 81.497 31.690 90.659 1.00 68.78 ? 479 CYS A CB 1 ATOM 751 S SG . CYS A 1 96 ? 82.915 32.815 90.791 1.00 75.70 ? 479 CYS A SG 1 ATOM 752 N N . THR A 1 97 ? 78.375 31.802 89.997 1.00 58.55 ? 480 THR A N 1 ATOM 753 C CA . THR A 1 97 ? 77.229 31.114 89.440 1.00 56.10 ? 480 THR A CA 1 ATOM 754 C C . THR A 1 97 ? 77.726 29.872 88.710 1.00 55.60 ? 480 THR A C 1 ATOM 755 O O . THR A 1 97 ? 78.534 29.976 87.792 1.00 55.48 ? 480 THR A O 1 ATOM 756 C CB . THR A 1 97 ? 76.441 32.031 88.477 1.00 54.63 ? 480 THR A CB 1 ATOM 757 O OG1 . THR A 1 97 ? 76.021 33.201 89.180 1.00 55.05 ? 480 THR A OG1 1 ATOM 758 C CG2 . THR A 1 97 ? 75.199 31.319 87.907 1.00 54.30 ? 480 THR A CG2 1 ATOM 759 N N . ILE A 1 98 ? 77.275 28.706 89.168 1.00 54.74 ? 481 ILE A N 1 ATOM 760 C CA . ILE A 1 98 ? 77.559 27.435 88.521 1.00 54.33 ? 481 ILE A CA 1 ATOM 761 C C . ILE A 1 98 ? 76.235 26.717 88.370 1.00 52.49 ? 481 ILE A C 1 ATOM 762 O O . ILE A 1 98 ? 75.638 26.313 89.361 1.00 54.06 ? 481 ILE A O 1 ATOM 763 C CB . ILE A 1 98 ? 78.522 26.555 89.345 1.00 55.69 ? 481 ILE A CB 1 ATOM 764 C CG1 . ILE A 1 98 ? 79.778 27.336 89.744 1.00 57.41 ? 481 ILE A CG1 1 ATOM 765 C CG2 . ILE A 1 98 ? 78.925 25.328 88.536 1.00 56.08 ? 481 ILE A CG2 1 ATOM 766 C CD1 . ILE A 1 98 ? 80.621 26.648 90.802 1.00 59.91 ? 481 ILE A CD1 1 ATOM 767 N N . LEU A 1 99 ? 75.757 26.586 87.141 1.00 51.18 ? 482 LEU A N 1 ATOM 768 C CA . LEU A 1 99 ? 74.534 25.837 86.897 1.00 51.30 ? 482 LEU A CA 1 ATOM 769 C C . LEU A 1 99 ? 74.913 24.373 86.816 1.00 51.31 ? 482 LEU A C 1 ATOM 770 O O . LEU A 1 99 ? 75.584 23.954 85.890 1.00 52.53 ? 482 LEU A O 1 ATOM 771 C CB . LEU A 1 99 ? 73.819 26.313 85.636 1.00 50.44 ? 482 LEU A CB 1 ATOM 772 C CG . LEU A 1 99 ? 73.521 27.817 85.607 1.00 51.06 ? 482 LEU A CG 1 ATOM 773 C CD1 . LEU A 1 99 ? 72.729 28.151 84.354 1.00 51.53 ? 482 LEU A CD1 1 ATOM 774 C CD2 . LEU A 1 99 ? 72.778 28.278 86.852 1.00 49.84 ? 482 LEU A CD2 1 ATOM 775 N N . SER A 1 100 ? 74.500 23.616 87.822 1.00 51.55 ? 483 SER A N 1 ATOM 776 C CA . SER A 1 100 ? 74.869 22.220 87.957 1.00 52.48 ? 483 SER A CA 1 ATOM 777 C C . SER A 1 100 ? 73.881 21.531 88.895 1.00 52.34 ? 483 SER A C 1 ATOM 778 O O . SER A 1 100 ? 73.372 22.166 89.823 1.00 51.11 ? 483 SER A O 1 ATOM 779 C CB . SER A 1 100 ? 76.283 22.162 88.528 1.00 53.16 ? 483 SER A CB 1 ATOM 780 O OG . SER A 1 100 ? 76.594 20.896 89.050 1.00 54.27 ? 483 SER A OG 1 ATOM 781 N N . VAL A 1 101 ? 73.618 20.241 88.667 1.00 51.95 ? 484 VAL A N 1 ATOM 782 C CA . VAL A 1 101 ? 72.819 19.451 89.639 1.00 51.64 ? 484 VAL A CA 1 ATOM 783 C C . VAL A 1 101 ? 73.451 19.393 91.016 1.00 49.37 ? 484 VAL A C 1 ATOM 784 O O . VAL A 1 101 ? 72.734 19.211 91.986 1.00 49.27 ? 484 VAL A O 1 ATOM 785 C CB . VAL A 1 101 ? 72.459 17.996 89.232 1.00 53.04 ? 484 VAL A CB 1 ATOM 786 C CG1 . VAL A 1 101 ? 71.402 18.018 88.152 1.00 55.22 ? 484 VAL A CG1 1 ATOM 787 C CG2 . VAL A 1 101 ? 73.687 17.207 88.808 1.00 54.15 ? 484 VAL A CG2 1 ATOM 788 N N . LEU A 1 102 ? 74.763 19.581 91.112 1.00 47.85 ? 485 LEU A N 1 ATOM 789 C CA . LEU A 1 102 ? 75.408 19.605 92.416 1.00 49.47 ? 485 LEU A CA 1 ATOM 790 C C . LEU A 1 102 ? 75.022 20.814 93.268 1.00 50.33 ? 485 LEU A C 1 ATOM 791 O O . LEU A 1 102 ? 75.153 20.765 94.501 1.00 52.17 ? 485 LEU A O 1 ATOM 792 C CB . LEU A 1 102 ? 76.924 19.519 92.292 1.00 49.82 ? 485 LEU A CB 1 ATOM 793 C CG . LEU A 1 102 ? 77.578 18.180 91.948 1.00 51.54 ? 485 LEU A CG 1 ATOM 794 C CD1 . LEU A 1 102 ? 77.197 17.037 92.876 1.00 52.29 ? 485 LEU A CD1 1 ATOM 795 C CD2 . LEU A 1 102 ? 77.383 17.841 90.471 1.00 50.93 ? 485 LEU A CD2 1 ATOM 796 N N . ASN A 1 103 ? 74.539 21.886 92.639 1.00 49.27 ? 486 ASN A N 1 ATOM 797 C CA . ASN A 1 103 ? 74.081 23.039 93.387 1.00 49.66 ? 486 ASN A CA 1 ATOM 798 C C . ASN A 1 103 ? 72.764 22.811 94.115 1.00 50.33 ? 486 ASN A C 1 ATOM 799 O O . ASN A 1 103 ? 72.454 23.564 95.040 1.00 51.53 ? 486 ASN A O 1 ATOM 800 C CB . ASN A 1 103 ? 74.027 24.313 92.531 1.00 49.38 ? 486 ASN A CB 1 ATOM 801 C CG . ASN A 1 103 ? 75.029 25.363 92.994 1.00 50.33 ? 486 ASN A CG 1 ATOM 802 O OD1 . ASN A 1 103 ? 75.295 25.492 94.191 1.00 51.39 ? 486 ASN A OD1 1 ATOM 803 N ND2 . ASN A 1 103 ? 75.584 26.122 92.054 1.00 50.48 ? 486 ASN A ND2 1 ATOM 804 N N . TYR A 1 104 ? 72.008 21.778 93.733 1.00 50.37 ? 487 TYR A N 1 ATOM 805 C CA . TYR A 1 104 ? 70.877 21.317 94.551 1.00 50.27 ? 487 TYR A CA 1 ATOM 806 C C . TYR A 1 104 ? 71.343 20.812 95.922 1.00 51.73 ? 487 TYR A C 1 ATOM 807 O O . TYR A 1 104 ? 70.560 20.801 96.864 1.00 55.09 ? 487 TYR A O 1 ATOM 808 C CB . TYR A 1 104 ? 70.075 20.211 93.856 1.00 49.48 ? 487 TYR A CB 1 ATOM 809 C CG . TYR A 1 104 ? 69.387 20.585 92.553 1.00 48.26 ? 487 TYR A CG 1 ATOM 810 C CD1 . TYR A 1 104 ? 68.773 21.824 92.378 1.00 47.62 ? 487 TYR A CD1 1 ATOM 811 C CD2 . TYR A 1 104 ? 69.294 19.663 91.512 1.00 48.07 ? 487 TYR A CD2 1 ATOM 812 C CE1 . TYR A 1 104 ? 68.134 22.149 91.192 1.00 46.86 ? 487 TYR A CE1 1 ATOM 813 C CE2 . TYR A 1 104 ? 68.650 19.978 90.327 1.00 47.55 ? 487 TYR A CE2 1 ATOM 814 C CZ . TYR A 1 104 ? 68.068 21.223 90.173 1.00 47.06 ? 487 TYR A CZ 1 ATOM 815 O OH . TYR A 1 104 ? 67.436 21.531 88.987 1.00 47.95 ? 487 TYR A OH 1 ATOM 816 N N . PHE A 1 105 ? 72.608 20.401 96.023 1.00 52.28 ? 488 PHE A N 1 ATOM 817 C CA . PHE A 1 105 ? 73.243 20.019 97.285 1.00 53.64 ? 488 PHE A CA 1 ATOM 818 C C . PHE A 1 105 ? 74.266 21.056 97.768 1.00 54.76 ? 488 PHE A C 1 ATOM 819 O O . PHE A 1 105 ? 75.145 20.746 98.576 1.00 56.97 ? 488 PHE A O 1 ATOM 820 C CB . PHE A 1 105 ? 73.889 18.648 97.101 1.00 52.99 ? 488 PHE A CB 1 ATOM 821 C CG . PHE A 1 105 ? 72.945 17.634 96.536 1.00 52.98 ? 488 PHE A CG 1 ATOM 822 C CD1 . PHE A 1 105 ? 72.823 17.463 95.163 1.00 52.16 ? 488 PHE A CD1 1 ATOM 823 C CD2 . PHE A 1 105 ? 72.116 16.896 97.377 1.00 53.54 ? 488 PHE A CD2 1 ATOM 824 C CE1 . PHE A 1 105 ? 71.919 16.549 94.641 1.00 52.10 ? 488 PHE A CE1 1 ATOM 825 C CE2 . PHE A 1 105 ? 71.214 15.977 96.859 1.00 53.14 ? 488 PHE A CE2 1 ATOM 826 C CZ . PHE A 1 105 ? 71.116 15.802 95.489 1.00 52.39 ? 488 PHE A CZ 1 ATOM 827 N N . GLN A 1 106 ? 74.134 22.286 97.280 1.00 53.83 ? 489 GLN A N 1 ATOM 828 C CA . GLN A 1 106 ? 75.022 23.397 97.612 1.00 55.00 ? 489 GLN A CA 1 ATOM 829 C C . GLN A 1 106 ? 76.497 23.075 97.411 1.00 54.80 ? 489 GLN A C 1 ATOM 830 O O . GLN A 1 106 ? 77.350 23.529 98.170 1.00 56.91 ? 489 GLN A O 1 ATOM 831 C CB . GLN A 1 106 ? 74.736 23.926 99.023 1.00 56.68 ? 489 GLN A CB 1 ATOM 832 C CG . GLN A 1 106 ? 73.354 24.557 99.159 1.00 57.91 ? 489 GLN A CG 1 ATOM 833 C CD . GLN A 1 106 ? 72.235 23.525 99.072 1.00 60.41 ? 489 GLN A CD 1 ATOM 834 O OE1 . GLN A 1 106 ? 72.186 22.592 99.878 1.00 64.26 ? 489 GLN A OE1 1 ATOM 835 N NE2 . GLN A 1 106 ? 71.348 23.667 98.082 1.00 59.41 ? 489 GLN A NE2 1 ATOM 836 N N . ASN A 1 107 ? 76.784 22.307 96.358 1.00 53.74 ? 490 ASN A N 1 ATOM 837 C CA . ASN A 1 107 ? 78.146 21.896 96.013 1.00 54.02 ? 490 ASN A CA 1 ATOM 838 C C . ASN A 1 107 ? 78.936 21.305 97.198 1.00 54.66 ? 490 ASN A C 1 ATOM 839 O O . ASN A 1 107 ? 80.125 21.557 97.341 1.00 54.10 ? 490 ASN A O 1 ATOM 840 C CB . ASN A 1 107 ? 78.895 23.083 95.391 1.00 54.14 ? 490 ASN A CB 1 ATOM 841 C CG . ASN A 1 107 ? 78.150 23.701 94.208 1.00 53.75 ? 490 ASN A CG 1 ATOM 842 O OD1 . ASN A 1 107 ? 77.368 23.037 93.526 1.00 52.45 ? 490 ASN A OD1 1 ATOM 843 N ND2 . ASN A 1 107 ? 78.405 24.976 93.955 1.00 54.65 ? 490 ASN A ND2 1 ATOM 844 N N . SER A 1 108 ? 78.257 20.510 98.024 1.00 56.01 ? 491 SER A N 1 ATOM 845 C CA . SER A 1 108 ? 78.832 19.942 99.245 1.00 58.61 ? 491 SER A CA 1 ATOM 846 C C . SER A 1 108 ? 78.766 18.423 99.212 1.00 58.97 ? 491 SER A C 1 ATOM 847 O O . SER A 1 108 ? 77.687 17.859 99.021 1.00 58.41 ? 491 SER A O 1 ATOM 848 C CB . SER A 1 108 ? 78.073 20.445 100.474 1.00 60.25 ? 491 SER A CB 1 ATOM 849 O OG . SER A 1 108 ? 78.384 19.684 101.637 1.00 61.73 ? 491 SER A OG 1 ATOM 850 N N . HIS A 1 109 ? 79.909 17.773 99.441 1.00 59.90 ? 492 HIS A N 1 ATOM 851 C CA . HIS A 1 109 ? 79.962 16.307 99.533 1.00 60.47 ? 492 HIS A CA 1 ATOM 852 C C . HIS A 1 109 ? 79.090 15.772 100.672 1.00 61.54 ? 492 HIS A C 1 ATOM 853 O O . HIS A 1 109 ? 78.381 14.778 100.500 1.00 60.26 ? 492 HIS A O 1 ATOM 854 C CB . HIS A 1 109 ? 81.392 15.815 99.734 1.00 61.68 ? 492 HIS A CB 1 ATOM 855 C CG . HIS A 1 109 ? 82.308 16.089 98.582 1.00 60.58 ? 492 HIS A CG 1 ATOM 856 N ND1 . HIS A 1 109 ? 82.329 15.314 97.446 1.00 59.89 ? 492 HIS A ND1 1 ATOM 857 C CD2 . HIS A 1 109 ? 83.257 17.038 98.404 1.00 61.45 ? 492 HIS A CD2 1 ATOM 858 C CE1 . HIS A 1 109 ? 83.239 15.776 96.610 1.00 60.64 ? 492 HIS A CE1 1 ATOM 859 N NE2 . HIS A 1 109 ? 83.821 16.822 97.169 1.00 61.71 ? 492 HIS A NE2 1 ATOM 860 N N . SER A 1 110 ? 79.119 16.443 101.825 1.00 64.14 ? 493 SER A N 1 ATOM 861 C CA . SER A 1 110 ? 78.306 16.011 102.973 1.00 65.76 ? 493 SER A CA 1 ATOM 862 C C . SER A 1 110 ? 76.794 16.182 102.745 1.00 64.18 ? 493 SER A C 1 ATOM 863 O O . SER A 1 110 ? 76.026 15.307 103.126 1.00 66.31 ? 493 SER A O 1 ATOM 864 C CB . SER A 1 110 ? 78.743 16.701 104.272 1.00 66.91 ? 493 SER A CB 1 ATOM 865 O OG . SER A 1 110 ? 78.657 18.101 104.162 1.00 67.11 ? 493 SER A OG 1 ATOM 866 N N . VAL A 1 111 ? 76.369 17.271 102.105 1.00 62.56 ? 494 VAL A N 1 ATOM 867 C CA . VAL A 1 111 ? 74.930 17.485 101.814 1.00 60.36 ? 494 VAL A CA 1 ATOM 868 C C . VAL A 1 111 ? 74.428 16.422 100.826 1.00 59.37 ? 494 VAL A C 1 ATOM 869 O O . VAL A 1 111 ? 73.338 15.883 100.984 1.00 58.98 ? 494 VAL A O 1 ATOM 870 C CB . VAL A 1 111 ? 74.633 18.920 101.294 1.00 57.95 ? 494 VAL A CB 1 ATOM 871 C CG1 . VAL A 1 111 ? 73.167 19.074 100.900 1.00 57.14 ? 494 VAL A CG1 1 ATOM 872 C CG2 . VAL A 1 111 ? 74.989 19.962 102.343 1.00 57.27 ? 494 VAL A CG2 1 ATOM 873 N N . LEU A 1 112 ? 75.244 16.104 99.832 1.00 60.07 ? 495 LEU A N 1 ATOM 874 C CA . LEU A 1 112 ? 74.946 15.011 98.905 1.00 61.13 ? 495 LEU A CA 1 ATOM 875 C C . LEU A 1 112 ? 74.798 13.659 99.621 1.00 63.86 ? 495 LEU A C 1 ATOM 876 O O . LEU A 1 112 ? 73.998 12.821 99.207 1.00 63.46 ? 495 LEU A O 1 ATOM 877 C CB . LEU A 1 112 ? 76.035 14.938 97.832 1.00 61.49 ? 495 LEU A CB 1 ATOM 878 C CG . LEU A 1 112 ? 75.806 14.039 96.622 1.00 62.46 ? 495 LEU A CG 1 ATOM 879 C CD1 . LEU A 1 112 ? 74.603 14.484 95.805 1.00 61.87 ? 495 LEU A CD1 1 ATOM 880 C CD2 . LEU A 1 112 ? 77.056 14.039 95.751 1.00 63.54 ? 495 LEU A CD2 1 ATOM 881 N N . ASP A 1 113 ? 75.560 13.458 100.696 1.00 67.27 ? 496 ASP A N 1 ATOM 882 C CA . ASP A 1 113 ? 75.462 12.243 101.521 1.00 70.92 ? 496 ASP A CA 1 ATOM 883 C C . ASP A 1 113 ? 74.363 12.246 102.596 1.00 75.24 ? 496 ASP A C 1 ATOM 884 O O . ASP A 1 113 ? 74.103 11.193 103.180 1.00 80.45 ? 496 ASP A O 1 ATOM 885 C CB . ASP A 1 113 ? 76.817 11.936 102.184 1.00 70.69 ? 496 ASP A CB 1 ATOM 886 C CG . ASP A 1 113 ? 77.828 11.339 101.220 1.00 70.56 ? 496 ASP A CG 1 ATOM 887 O OD1 . ASP A 1 113 ? 77.423 10.747 100.194 1.00 68.59 ? 496 ASP A OD1 1 ATOM 888 O OD2 . ASP A 1 113 ? 79.042 11.456 101.503 1.00 71.52 ? 496 ASP A OD2 1 ATOM 889 N N . HIS A 1 114 ? 73.740 13.396 102.876 1.00 77.55 ? 497 HIS A N 1 ATOM 890 C CA . HIS A 1 114 ? 72.622 13.478 103.829 1.00 80.66 ? 497 HIS A CA 1 ATOM 891 C C . HIS A 1 114 ? 71.648 12.335 103.606 1.00 80.86 ? 497 HIS A C 1 ATOM 892 O O . HIS A 1 114 ? 71.239 12.080 102.472 1.00 78.68 ? 497 HIS A O 1 ATOM 893 C CB . HIS A 1 114 ? 71.817 14.767 103.651 1.00 84.08 ? 497 HIS A CB 1 ATOM 894 C CG . HIS A 1 114 ? 72.211 15.897 104.541 1.00 89.33 ? 497 HIS A CG 1 ATOM 895 N ND1 . HIS A 1 114 ? 71.272 16.709 105.141 1.00 93.50 ? 497 HIS A ND1 1 ATOM 896 C CD2 . HIS A 1 114 ? 73.420 16.369 104.925 1.00 92.48 ? 497 HIS A CD2 1 ATOM 897 C CE1 . HIS A 1 114 ? 71.885 17.632 105.859 1.00 95.45 ? 497 HIS A CE1 1 ATOM 898 N NE2 . HIS A 1 114 ? 73.190 17.451 105.741 1.00 95.50 ? 497 HIS A NE2 1 ATOM 899 N N . LYS A 1 115 ? 71.277 11.662 104.689 1.00 84.01 ? 498 LYS A N 1 ATOM 900 C CA . LYS A 1 115 ? 70.253 10.629 104.639 1.00 85.50 ? 498 LYS A CA 1 ATOM 901 C C . LYS A 1 115 ? 69.581 10.463 105.990 1.00 86.18 ? 498 LYS A C 1 ATOM 902 O O . LYS A 1 115 ? 70.214 10.645 107.027 1.00 85.88 ? 498 LYS A O 1 ATOM 903 C CB . LYS A 1 115 ? 70.843 9.297 104.146 1.00 87.31 ? 498 LYS A CB 1 ATOM 904 C CG . LYS A 1 115 ? 72.023 8.763 104.950 1.00 90.11 ? 498 LYS A CG 1 ATOM 905 C CD . LYS A 1 115 ? 72.258 7.261 104.807 1.00 92.79 ? 498 LYS A CD 1 ATOM 906 C CE . LYS A 1 115 ? 72.441 6.856 103.344 1.00 92.50 ? 498 LYS A CE 1 ATOM 907 N NZ . LYS A 1 115 ? 72.382 5.390 103.049 1.00 93.69 ? 498 LYS A NZ 1 ATOM 908 N N . LYS A 1 116 ? 68.293 10.137 105.956 1.00 89.49 ? 499 LYS A N 1 ATOM 909 C CA . LYS A 1 116 ? 67.525 9.801 107.147 1.00 94.18 ? 499 LYS A CA 1 ATOM 910 C C . LYS A 1 116 ? 66.948 8.414 106.962 1.00 95.45 ? 499 LYS A C 1 ATOM 911 O O . LYS A 1 116 ? 66.274 8.135 105.969 1.00 93.20 ? 499 LYS A O 1 ATOM 912 C CB . LYS A 1 116 ? 66.392 10.799 107.378 1.00 96.24 ? 499 LYS A CB 1 ATOM 913 C CG . LYS A 1 116 ? 66.847 12.232 107.611 1.00 98.28 ? 499 LYS A CG 1 ATOM 914 C CD . LYS A 1 116 ? 67.710 12.417 108.859 1.00 101.50 ? 499 LYS A CD 1 ATOM 915 C CE . LYS A 1 116 ? 67.965 13.924 109.121 1.00 103.62 ? 499 LYS A CE 1 ATOM 916 N NZ . LYS A 1 116 ? 66.850 14.573 109.876 1.00 105.23 ? 499 LYS A NZ 1 ATOM 917 N N . GLY A 1 117 ? 67.238 7.541 107.916 1.00 100.92 ? 500 GLY A N 1 ATOM 918 C CA . GLY A 1 117 ? 66.745 6.180 107.880 1.00 106.04 ? 500 GLY A CA 1 ATOM 919 C C . GLY A 1 117 ? 66.928 5.482 109.207 1.00 111.53 ? 500 GLY A C 1 ATOM 920 O O . GLY A 1 117 ? 67.681 5.941 110.067 1.00 114.35 ? 500 GLY A O 1 ATOM 921 N N . ASP A 1 118 ? 66.213 4.377 109.372 1.00 116.34 ? 501 ASP A N 1 ATOM 922 C CA . ASP A 1 118 ? 66.383 3.500 110.534 1.00 123.15 ? 501 ASP A CA 1 ATOM 923 C C . ASP A 1 118 ? 67.479 2.475 110.272 1.00 127.68 ? 501 ASP A C 1 ATOM 924 O O . ASP A 1 118 ? 68.175 2.535 109.247 1.00 129.47 ? 501 ASP A O 1 ATOM 925 C CB . ASP A 1 118 ? 65.051 2.838 110.921 1.00 123.56 ? 501 ASP A CB 1 ATOM 926 C CG . ASP A 1 118 ? 64.438 2.009 109.794 1.00 122.11 ? 501 ASP A CG 1 ATOM 927 O OD1 . ASP A 1 118 ? 65.043 1.033 109.264 1.00 120.91 ? 501 ASP A OD1 1 ATOM 928 O OD2 . ASP A 1 118 ? 63.309 2.369 109.443 1.00 118.18 ? 501 ASP A OD2 1 ATOM 929 N N . ASP A 1 119 ? 67.616 1.521 111.191 1.00 132.89 ? 502 ASP A N 1 ATOM 930 C CA . ASP A 1 119 ? 68.627 0.478 111.092 1.00 137.13 ? 502 ASP A CA 1 ATOM 931 C C . ASP A 1 119 ? 68.696 -0.227 109.711 1.00 140.96 ? 502 ASP A C 1 ATOM 932 O O . ASP A 1 119 ? 69.758 -0.744 109.376 1.00 142.53 ? 502 ASP A O 1 ATOM 933 C CB . ASP A 1 119 ? 68.486 -0.515 112.264 1.00 137.89 ? 502 ASP A CB 1 ATOM 934 C CG . ASP A 1 119 ? 69.164 -0.017 113.534 1.00 138.26 ? 502 ASP A CG 1 ATOM 935 O OD1 . ASP A 1 119 ? 69.864 -0.819 114.195 1.00 139.42 ? 502 ASP A OD1 1 ATOM 936 O OD2 . ASP A 1 119 ? 69.004 1.180 113.859 1.00 134.41 ? 502 ASP A OD2 1 ATOM 937 N N . PHE A 1 120 ? 67.616 -0.195 108.905 1.00 142.24 ? 503 PHE A N 1 ATOM 938 C CA . PHE A 1 120 ? 67.603 -0.851 107.566 1.00 142.49 ? 503 PHE A CA 1 ATOM 939 C C . PHE A 1 120 ? 66.963 -0.108 106.351 1.00 133.99 ? 503 PHE A C 1 ATOM 940 O O . PHE A 1 120 ? 67.461 -0.287 105.235 1.00 131.75 ? 503 PHE A O 1 ATOM 941 C CB . PHE A 1 120 ? 67.061 -2.285 107.721 1.00 149.51 ? 503 PHE A CB 1 ATOM 942 C CG . PHE A 1 120 ? 67.102 -3.120 106.461 1.00 153.60 ? 503 PHE A CG 1 ATOM 943 C CD1 . PHE A 1 120 ? 68.289 -3.285 105.742 1.00 155.10 ? 503 PHE A CD1 1 ATOM 944 C CD2 . PHE A 1 120 ? 65.955 -3.779 106.014 1.00 155.59 ? 503 PHE A CD2 1 ATOM 945 C CE1 . PHE A 1 120 ? 68.321 -4.065 104.591 1.00 155.97 ? 503 PHE A CE1 1 ATOM 946 C CE2 . PHE A 1 120 ? 65.984 -4.562 104.866 1.00 156.21 ? 503 PHE A CE2 1 ATOM 947 C CZ . PHE A 1 120 ? 67.168 -4.705 104.154 1.00 156.14 ? 503 PHE A CZ 1 ATOM 948 N N . PHE A 1 121 ? 65.902 0.695 106.535 1.00 126.38 ? 504 PHE A N 1 ATOM 949 C CA . PHE A 1 121 ? 65.269 1.469 105.429 1.00 119.54 ? 504 PHE A CA 1 ATOM 950 C C . PHE A 1 121 ? 65.749 2.921 105.351 1.00 108.37 ? 504 PHE A C 1 ATOM 951 O O . PHE A 1 121 ? 66.113 3.516 106.368 1.00 105.23 ? 504 PHE A O 1 ATOM 952 C CB . PHE A 1 121 ? 63.736 1.470 105.552 1.00 121.08 ? 504 PHE A CB 1 ATOM 953 C CG . PHE A 1 121 ? 63.116 0.124 105.335 1.00 124.75 ? 504 PHE A CG 1 ATOM 954 C CD1 . PHE A 1 121 ? 63.132 -0.464 104.073 1.00 125.71 ? 504 PHE A CD1 1 ATOM 955 C CD2 . PHE A 1 121 ? 62.525 -0.569 106.389 1.00 127.59 ? 504 PHE A CD2 1 ATOM 956 C CE1 . PHE A 1 121 ? 62.569 -1.715 103.866 1.00 128.92 ? 504 PHE A CE1 1 ATOM 957 C CE2 . PHE A 1 121 ? 61.958 -1.819 106.188 1.00 129.95 ? 504 PHE A CE2 1 ATOM 958 C CZ . PHE A 1 121 ? 61.981 -2.394 104.925 1.00 130.95 ? 504 PHE A CZ 1 ATOM 959 N N . VAL A 1 122 ? 65.727 3.466 104.130 1.00 99.33 ? 505 VAL A N 1 ATOM 960 C CA . VAL A 1 122 ? 66.056 4.867 103.837 1.00 92.49 ? 505 VAL A CA 1 ATOM 961 C C . VAL A 1 122 ? 64.750 5.631 103.653 1.00 87.11 ? 505 VAL A C 1 ATOM 962 O O . VAL A 1 122 ? 63.961 5.303 102.772 1.00 82.51 ? 505 VAL A O 1 ATOM 963 C CB . VAL A 1 122 ? 66.899 4.992 102.541 1.00 90.98 ? 505 VAL A CB 1 ATOM 964 C CG1 . VAL A 1 122 ? 67.211 6.453 102.215 1.00 89.75 ? 505 VAL A CG1 1 ATOM 965 C CG2 . VAL A 1 122 ? 68.189 4.187 102.659 1.00 90.50 ? 505 VAL A CG2 1 ATOM 966 N N . TYR A 1 123 ? 64.514 6.626 104.502 1.00 86.14 ? 506 TYR A N 1 ATOM 967 C CA . TYR A 1 123 ? 63.311 7.460 104.404 1.00 86.21 ? 506 TYR A CA 1 ATOM 968 C C . TYR A 1 123 ? 63.511 8.531 103.361 1.00 81.98 ? 506 TYR A C 1 ATOM 969 O O . TYR A 1 123 ? 62.640 8.765 102.527 1.00 81.51 ? 506 TYR A O 1 ATOM 970 C CB . TYR A 1 123 ? 62.991 8.151 105.731 1.00 90.25 ? 506 TYR A CB 1 ATOM 971 C CG . TYR A 1 123 ? 62.884 7.247 106.944 1.00 95.91 ? 506 TYR A CG 1 ATOM 972 C CD1 . TYR A 1 123 ? 62.272 5.990 106.870 1.00 98.06 ? 506 TYR A CD1 1 ATOM 973 C CD2 . TYR A 1 123 ? 63.363 7.672 108.185 1.00 99.22 ? 506 TYR A CD2 1 ATOM 974 C CE1 . TYR A 1 123 ? 62.164 5.181 107.991 1.00 100.63 ? 506 TYR A CE1 1 ATOM 975 C CE2 . TYR A 1 123 ? 63.257 6.874 109.310 1.00 101.77 ? 506 TYR A CE2 1 ATOM 976 C CZ . TYR A 1 123 ? 62.657 5.632 109.207 1.00 103.25 ? 506 TYR A CZ 1 ATOM 977 O OH . TYR A 1 123 ? 62.555 4.847 110.325 1.00 107.74 ? 506 TYR A OH 1 ATOM 978 N N . ALA A 1 124 ? 64.665 9.188 103.441 1.00 78.07 ? 507 ALA A N 1 ATOM 979 C CA . ALA A 1 124 ? 65.024 10.277 102.552 1.00 74.50 ? 507 ALA A CA 1 ATOM 980 C C . ALA A 1 124 ? 66.523 10.268 102.302 1.00 72.48 ? 507 ALA A C 1 ATOM 981 O O . ALA A 1 124 ? 67.300 9.922 103.192 1.00 74.30 ? 507 ALA A O 1 ATOM 982 C CB . ALA A 1 124 ? 64.599 11.602 103.165 1.00 73.87 ? 507 ALA A CB 1 ATOM 983 N N . ASP A 1 125 ? 66.918 10.608 101.077 1.00 70.21 ? 508 ASP A N 1 ATOM 984 C CA . ASP A 1 125 ? 68.329 10.752 100.698 1.00 69.51 ? 508 ASP A CA 1 ATOM 985 C C . ASP A 1 125 ? 68.438 11.667 99.455 1.00 68.05 ? 508 ASP A C 1 ATOM 986 O O . ASP A 1 125 ? 67.481 12.367 99.132 1.00 66.64 ? 508 ASP A O 1 ATOM 987 C CB . ASP A 1 125 ? 68.967 9.366 100.481 1.00 69.84 ? 508 ASP A CB 1 ATOM 988 C CG . ASP A 1 125 ? 68.359 8.602 99.314 1.00 69.98 ? 508 ASP A CG 1 ATOM 989 O OD1 . ASP A 1 125 ? 67.349 9.049 98.728 1.00 68.84 ? 508 ASP A OD1 1 ATOM 990 O OD2 . ASP A 1 125 ? 68.894 7.525 98.979 1.00 73.08 ? 508 ASP A OD2 1 ATOM 991 N N . TYR A 1 126 ? 69.574 11.641 98.754 1.00 67.84 ? 509 TYR A N 1 ATOM 992 C CA . TYR A 1 126 ? 69.799 12.522 97.603 1.00 66.06 ? 509 TYR A CA 1 ATOM 993 C C . TYR A 1 126 ? 68.783 12.354 96.467 1.00 64.48 ? 509 TYR A C 1 ATOM 994 O O . TYR A 1 126 ? 68.450 13.344 95.792 1.00 63.78 ? 509 TYR A O 1 ATOM 995 C CB . TYR A 1 126 ? 71.238 12.404 97.076 1.00 65.62 ? 509 TYR A CB 1 ATOM 996 C CG . TYR A 1 126 ? 71.491 11.279 96.096 1.00 66.69 ? 509 TYR A CG 1 ATOM 997 C CD1 . TYR A 1 126 ? 71.633 9.958 96.531 1.00 67.86 ? 509 TYR A CD1 1 ATOM 998 C CD2 . TYR A 1 126 ? 71.613 11.538 94.728 1.00 65.98 ? 509 TYR A CD2 1 ATOM 999 C CE1 . TYR A 1 126 ? 71.887 8.933 95.628 1.00 67.44 ? 509 TYR A CE1 1 ATOM 1000 C CE2 . TYR A 1 126 ? 71.859 10.521 93.822 1.00 66.10 ? 509 TYR A CE2 1 ATOM 1001 C CZ . TYR A 1 126 ? 71.997 9.220 94.274 1.00 67.22 ? 509 TYR A CZ 1 ATOM 1002 O OH . TYR A 1 126 ? 72.244 8.209 93.375 1.00 68.58 ? 509 TYR A OH 1 ATOM 1003 N N . HIS A 1 127 ? 68.284 11.129 96.284 1.00 62.70 ? 510 HIS A N 1 ATOM 1004 C CA . HIS A 1 127 ? 67.198 10.863 95.323 1.00 62.34 ? 510 HIS A CA 1 ATOM 1005 C C . HIS A 1 127 ? 65.967 11.692 95.657 1.00 60.41 ? 510 HIS A C 1 ATOM 1006 O O . HIS A 1 127 ? 65.384 12.339 94.795 1.00 57.89 ? 510 HIS A O 1 ATOM 1007 C CB . HIS A 1 127 ? 66.757 9.390 95.340 1.00 62.98 ? 510 HIS A CB 1 ATOM 1008 C CG . HIS A 1 127 ? 67.859 8.416 95.092 1.00 63.27 ? 510 HIS A CG 1 ATOM 1009 N ND1 . HIS A 1 127 ? 68.353 7.591 96.080 1.00 64.21 ? 510 HIS A ND1 1 ATOM 1010 C CD2 . HIS A 1 127 ? 68.560 8.128 93.973 1.00 62.92 ? 510 HIS A CD2 1 ATOM 1011 C CE1 . HIS A 1 127 ? 69.311 6.835 95.579 1.00 64.12 ? 510 HIS A CE1 1 ATOM 1012 N NE2 . HIS A 1 127 ? 69.455 7.142 94.303 1.00 63.19 ? 510 HIS A NE2 1 ATOM 1013 N N . THR A 1 128 ? 65.577 11.634 96.926 1.00 61.43 ? 511 THR A N 1 ATOM 1014 C CA . THR A 1 128 ? 64.412 12.356 97.425 1.00 61.19 ? 511 THR A CA 1 ATOM 1015 C C . THR A 1 128 ? 64.585 13.846 97.227 1.00 58.38 ? 511 THR A C 1 ATOM 1016 O O . THR A 1 128 ? 63.669 14.515 96.761 1.00 57.76 ? 511 THR A O 1 ATOM 1017 C CB . THR A 1 128 ? 64.166 12.071 98.919 1.00 62.25 ? 511 THR A CB 1 ATOM 1018 O OG1 . THR A 1 128 ? 64.333 10.671 99.155 1.00 63.92 ? 511 THR A OG1 1 ATOM 1019 C CG2 . THR A 1 128 ? 62.755 12.483 99.332 1.00 62.39 ? 511 THR A CG2 1 ATOM 1020 N N . HIS A 1 129 ? 65.765 14.346 97.578 1.00 57.21 ? 512 HIS A N 1 ATOM 1021 C CA . HIS A 1 129 ? 66.084 15.759 97.418 1.00 56.14 ? 512 HIS A CA 1 ATOM 1022 C C . HIS A 1 129 ? 66.043 16.178 95.943 1.00 54.09 ? 512 HIS A C 1 ATOM 1023 O O . HIS A 1 129 ? 65.383 17.153 95.601 1.00 52.67 ? 512 HIS A O 1 ATOM 1024 C CB . HIS A 1 129 ? 67.446 16.082 98.030 1.00 56.25 ? 512 HIS A CB 1 ATOM 1025 C CG . HIS A 1 129 ? 67.692 17.546 98.174 1.00 56.18 ? 512 HIS A CG 1 ATOM 1026 N ND1 . HIS A 1 129 ? 66.875 18.360 98.929 1.00 56.54 ? 512 HIS A ND1 1 ATOM 1027 C CD2 . HIS A 1 129 ? 68.648 18.348 97.656 1.00 56.13 ? 512 HIS A CD2 1 ATOM 1028 C CE1 . HIS A 1 129 ? 67.320 19.601 98.875 1.00 56.07 ? 512 HIS A CE1 1 ATOM 1029 N NE2 . HIS A 1 129 ? 68.397 19.622 98.111 1.00 56.99 ? 512 HIS A NE2 1 ATOM 1030 N N . PHE A 1 130 ? 66.725 15.408 95.090 1.00 53.35 ? 513 PHE A N 1 ATOM 1031 C CA . PHE A 1 130 ? 66.709 15.601 93.632 1.00 51.34 ? 513 PHE A CA 1 ATOM 1032 C C . PHE A 1 130 ? 65.295 15.725 93.068 1.00 51.91 ? 513 PHE A C 1 ATOM 1033 O O . PHE A 1 130 ? 64.984 16.704 92.401 1.00 52.86 ? 513 PHE A O 1 ATOM 1034 C CB . PHE A 1 130 ? 67.439 14.451 92.929 1.00 50.67 ? 513 PHE A CB 1 ATOM 1035 C CG . PHE A 1 130 ? 67.456 14.558 91.423 1.00 49.70 ? 513 PHE A CG 1 ATOM 1036 C CD1 . PHE A 1 130 ? 68.438 15.299 90.776 1.00 49.18 ? 513 PHE A CD1 1 ATOM 1037 C CD2 . PHE A 1 130 ? 66.512 13.898 90.653 1.00 49.69 ? 513 PHE A CD2 1 ATOM 1038 C CE1 . PHE A 1 130 ? 68.468 15.387 89.396 1.00 48.63 ? 513 PHE A CE1 1 ATOM 1039 C CE2 . PHE A 1 130 ? 66.535 13.982 89.270 1.00 49.15 ? 513 PHE A CE2 1 ATOM 1040 C CZ . PHE A 1 130 ? 67.512 14.729 88.641 1.00 49.34 ? 513 PHE A CZ 1 ATOM 1041 N N . LEU A 1 131 ? 64.441 14.744 93.358 1.00 53.04 ? 514 LEU A N 1 ATOM 1042 C CA . LEU A 1 131 ? 63.069 14.718 92.822 1.00 52.77 ? 514 LEU A CA 1 ATOM 1043 C C . LEU A 1 131 ? 62.212 15.879 93.309 1.00 52.58 ? 514 LEU A C 1 ATOM 1044 O O . LEU A 1 131 ? 61.311 16.310 92.595 1.00 54.17 ? 514 LEU A O 1 ATOM 1045 C CB . LEU A 1 131 ? 62.374 13.388 93.135 1.00 53.57 ? 514 LEU A CB 1 ATOM 1046 C CG . LEU A 1 131 ? 62.974 12.188 92.406 1.00 54.44 ? 514 LEU A CG 1 ATOM 1047 C CD1 . LEU A 1 131 ? 62.495 10.883 93.034 1.00 55.63 ? 514 LEU A CD1 1 ATOM 1048 C CD2 . LEU A 1 131 ? 62.656 12.231 90.918 1.00 53.64 ? 514 LEU A CD2 1 ATOM 1049 N N . TYR A 1 132 ? 62.487 16.382 94.511 1.00 52.27 ? 515 TYR A N 1 ATOM 1050 C CA . TYR A 1 132 ? 61.848 17.608 94.983 1.00 52.44 ? 515 TYR A CA 1 ATOM 1051 C C . TYR A 1 132 ? 62.454 18.839 94.271 1.00 51.51 ? 515 TYR A C 1 ATOM 1052 O O . TYR A 1 132 ? 61.724 19.658 93.729 1.00 51.26 ? 515 TYR A O 1 ATOM 1053 C CB . TYR A 1 132 ? 61.946 17.739 96.509 1.00 52.30 ? 515 TYR A CB 1 ATOM 1054 C CG . TYR A 1 132 ? 61.433 19.060 97.030 1.00 52.16 ? 515 TYR A CG 1 ATOM 1055 C CD1 . TYR A 1 132 ? 62.291 20.143 97.169 1.00 52.67 ? 515 TYR A CD1 1 ATOM 1056 C CD2 . TYR A 1 132 ? 60.097 19.242 97.360 1.00 52.11 ? 515 TYR A CD2 1 ATOM 1057 C CE1 . TYR A 1 132 ? 61.841 21.368 97.634 1.00 52.53 ? 515 TYR A CE1 1 ATOM 1058 C CE2 . TYR A 1 132 ? 59.635 20.463 97.839 1.00 52.29 ? 515 TYR A CE2 1 ATOM 1059 C CZ . TYR A 1 132 ? 60.513 21.524 97.977 1.00 52.09 ? 515 TYR A CZ 1 ATOM 1060 O OH . TYR A 1 132 ? 60.072 22.739 98.439 1.00 51.89 ? 515 TYR A OH 1 ATOM 1061 N N . CYS A 1 133 ? 63.778 18.952 94.274 1.00 51.18 ? 516 CYS A N 1 ATOM 1062 C CA . CYS A 1 133 ? 64.454 20.142 93.750 1.00 51.73 ? 516 CYS A CA 1 ATOM 1063 C C . CYS A 1 133 ? 64.213 20.436 92.258 1.00 51.30 ? 516 CYS A C 1 ATOM 1064 O O . CYS A 1 133 ? 64.132 21.601 91.862 1.00 50.21 ? 516 CYS A O 1 ATOM 1065 C CB . CYS A 1 133 ? 65.963 20.084 94.037 1.00 51.38 ? 516 CYS A CB 1 ATOM 1066 S SG . CYS A 1 133 ? 66.411 20.291 95.777 1.00 54.26 ? 516 CYS A SG 1 ATOM 1067 N N . VAL A 1 134 ? 64.078 19.395 91.439 1.00 52.15 ? 517 VAL A N 1 ATOM 1068 C CA . VAL A 1 134 ? 63.709 19.587 90.022 1.00 51.97 ? 517 VAL A CA 1 ATOM 1069 C C . VAL A 1 134 ? 62.311 20.199 89.832 1.00 52.52 ? 517 VAL A C 1 ATOM 1070 O O . VAL A 1 134 ? 62.044 20.812 88.808 1.00 52.79 ? 517 VAL A O 1 ATOM 1071 C CB . VAL A 1 134 ? 63.850 18.303 89.178 1.00 51.87 ? 517 VAL A CB 1 ATOM 1072 C CG1 . VAL A 1 134 ? 65.297 17.834 89.173 1.00 51.04 ? 517 VAL A CG1 1 ATOM 1073 C CG2 . VAL A 1 134 ? 62.888 17.207 89.637 1.00 53.22 ? 517 VAL A CG2 1 ATOM 1074 N N . ARG A 1 135 ? 61.440 20.040 90.824 1.00 54.73 ? 518 ARG A N 1 ATOM 1075 C CA . ARG A 1 135 ? 60.129 20.690 90.840 1.00 57.73 ? 518 ARG A CA 1 ATOM 1076 C C . ARG A 1 135 ? 60.109 22.057 91.547 1.00 55.39 ? 518 ARG A C 1 ATOM 1077 O O . ARG A 1 135 ? 59.241 22.884 91.249 1.00 58.50 ? 518 ARG A O 1 ATOM 1078 C CB . ARG A 1 135 ? 59.096 19.772 91.496 1.00 62.16 ? 518 ARG A CB 1 ATOM 1079 C CG . ARG A 1 135 ? 58.872 18.450 90.772 1.00 67.14 ? 518 ARG A CG 1 ATOM 1080 C CD . ARG A 1 135 ? 58.212 17.452 91.714 1.00 74.93 ? 518 ARG A CD 1 ATOM 1081 N NE . ARG A 1 135 ? 57.711 16.254 91.035 1.00 82.83 ? 518 ARG A NE 1 ATOM 1082 C CZ . ARG A 1 135 ? 56.512 16.126 90.448 1.00 88.04 ? 518 ARG A CZ 1 ATOM 1083 N NH1 . ARG A 1 135 ? 55.629 17.133 90.416 1.00 89.49 ? 518 ARG A NH1 1 ATOM 1084 N NH2 . ARG A 1 135 ? 56.191 14.965 89.873 1.00 91.24 ? 518 ARG A NH2 1 ATOM 1085 N N . ALA A 1 136 ? 61.034 22.288 92.479 1.00 51.47 ? 519 ALA A N 1 ATOM 1086 C CA . ALA A 1 136 ? 61.073 23.527 93.259 1.00 49.62 ? 519 ALA A CA 1 ATOM 1087 C C . ALA A 1 136 ? 62.513 24.012 93.510 1.00 47.82 ? 519 ALA A C 1 ATOM 1088 O O . ALA A 1 136 ? 62.965 24.076 94.662 1.00 46.15 ? 519 ALA A O 1 ATOM 1089 C CB . ALA A 1 136 ? 60.351 23.311 94.572 1.00 50.84 ? 519 ALA A CB 1 ATOM 1090 N N . PRO A 1 137 ? 63.230 24.386 92.433 1.00 45.09 ? 520 PRO A N 1 ATOM 1091 C CA . PRO A 1 137 ? 64.651 24.697 92.580 1.00 45.04 ? 520 PRO A CA 1 ATOM 1092 C C . PRO A 1 137 ? 64.996 25.979 93.348 1.00 45.47 ? 520 PRO A C 1 ATOM 1093 O O . PRO A 1 137 ? 66.158 26.161 93.698 1.00 47.22 ? 520 PRO A O 1 ATOM 1094 C CB . PRO A 1 137 ? 65.149 24.775 91.136 1.00 44.83 ? 520 PRO A CB 1 ATOM 1095 C CG . PRO A 1 137 ? 63.926 25.097 90.330 1.00 44.83 ? 520 PRO A CG 1 ATOM 1096 C CD . PRO A 1 137 ? 62.788 24.430 91.030 1.00 44.24 ? 520 PRO A CD 1 ATOM 1097 N N . ALA A 1 138 ? 64.023 26.846 93.608 1.00 45.98 ? 521 ALA A N 1 ATOM 1098 C CA . ALA A 1 138 ? 64.234 28.034 94.445 1.00 47.82 ? 521 ALA A CA 1 ATOM 1099 C C . ALA A 1 138 ? 63.996 27.788 95.934 1.00 49.30 ? 521 ALA A C 1 ATOM 1100 O O . ALA A 1 138 ? 64.298 28.654 96.750 1.00 49.79 ? 521 ALA A O 1 ATOM 1101 C CB . ALA A 1 138 ? 63.350 29.184 93.969 1.00 48.73 ? 521 ALA A CB 1 ATOM 1102 N N . SER A 1 139 ? 63.442 26.624 96.285 1.00 51.21 ? 522 SER A N 1 ATOM 1103 C CA . SER A 1 139 ? 63.094 26.298 97.670 1.00 51.77 ? 522 SER A CA 1 ATOM 1104 C C . SER A 1 139 ? 64.286 26.403 98.592 1.00 52.52 ? 522 SER A C 1 ATOM 1105 O O . SER A 1 139 ? 65.376 25.962 98.235 1.00 51.76 ? 522 SER A O 1 ATOM 1106 C CB . SER A 1 139 ? 62.543 24.880 97.756 1.00 52.31 ? 522 SER A CB 1 ATOM 1107 O OG . SER A 1 139 ? 62.258 24.527 99.091 1.00 51.54 ? 522 SER A OG 1 ATOM 1108 N N . LEU A 1 140 ? 64.073 27.006 99.763 1.00 54.80 ? 523 LEU A N 1 ATOM 1109 C CA . LEU A 1 140 ? 65.087 27.043 100.824 1.00 58.27 ? 523 LEU A CA 1 ATOM 1110 C C . LEU A 1 140 ? 64.992 25.828 101.755 1.00 61.68 ? 523 LEU A C 1 ATOM 1111 O O . LEU A 1 140 ? 65.826 25.668 102.642 1.00 61.43 ? 523 LEU A O 1 ATOM 1112 C CB . LEU A 1 140 ? 64.959 28.327 101.649 1.00 58.51 ? 523 LEU A CB 1 ATOM 1113 C CG . LEU A 1 140 ? 65.061 29.643 100.869 1.00 59.39 ? 523 LEU A CG 1 ATOM 1114 C CD1 . LEU A 1 140 ? 64.858 30.841 101.786 1.00 60.02 ? 523 LEU A CD1 1 ATOM 1115 C CD2 . LEU A 1 140 ? 66.392 29.755 100.141 1.00 59.05 ? 523 LEU A CD2 1 ATOM 1116 N N . ASN A 1 141 ? 63.992 24.970 101.541 1.00 65.53 ? 524 ASN A N 1 ATOM 1117 C CA . ASN A 1 141 ? 63.651 23.935 102.496 1.00 70.85 ? 524 ASN A CA 1 ATOM 1118 C C . ASN A 1 141 ? 62.886 22.805 101.813 1.00 69.24 ? 524 ASN A C 1 ATOM 1119 O O . ASN A 1 141 ? 61.735 22.954 101.442 1.00 65.33 ? 524 ASN A O 1 ATOM 1120 C CB . ASN A 1 141 ? 62.824 24.553 103.629 1.00 77.64 ? 524 ASN A CB 1 ATOM 1121 C CG . ASN A 1 141 ? 62.646 23.627 104.814 1.00 85.94 ? 524 ASN A CG 1 ATOM 1122 O OD1 . ASN A 1 141 ? 63.014 22.455 104.778 1.00 86.38 ? 524 ASN A OD1 1 ATOM 1123 N ND2 . ASN A 1 141 ? 62.072 24.171 105.887 1.00 97.56 ? 524 ASN A ND2 1 ATOM 1124 N N . ASP A 1 142 ? 63.575 21.690 101.623 1.00 73.20 ? 525 ASP A N 1 ATOM 1125 C CA . ASP A 1 142 ? 62.978 20.416 101.223 1.00 79.03 ? 525 ASP A CA 1 ATOM 1126 C C . ASP A 1 142 ? 61.807 20.082 102.165 1.00 82.54 ? 525 ASP A C 1 ATOM 1127 O O . ASP A 1 142 ? 61.900 20.292 103.375 1.00 82.96 ? 525 ASP A O 1 ATOM 1128 C CB . ASP A 1 142 ? 64.065 19.325 101.312 1.00 81.96 ? 525 ASP A CB 1 ATOM 1129 C CG . ASP A 1 142 ? 63.707 18.045 100.591 1.00 85.09 ? 525 ASP A CG 1 ATOM 1130 O OD1 . ASP A 1 142 ? 62.515 17.792 100.289 1.00 88.96 ? 525 ASP A OD1 1 ATOM 1131 O OD2 . ASP A 1 142 ? 64.662 17.273 100.335 1.00 85.14 ? 525 ASP A OD2 1 ATOM 1132 N N . THR A 1 143 ? 60.709 19.577 101.615 1.00 85.33 ? 526 THR A N 1 ATOM 1133 C CA . THR A 1 143 ? 59.543 19.222 102.437 1.00 88.92 ? 526 THR A CA 1 ATOM 1134 C C . THR A 1 143 ? 59.745 17.865 103.118 1.00 90.59 ? 526 THR A C 1 ATOM 1135 O O . THR A 1 143 ? 59.084 17.571 104.109 1.00 89.96 ? 526 THR A O 1 ATOM 1136 C CB . THR A 1 143 ? 58.254 19.274 101.621 1.00 90.20 ? 526 THR A CB 1 ATOM 1137 O OG1 . THR A 1 143 ? 58.074 20.613 101.153 1.00 92.74 ? 526 THR A OG1 1 ATOM 1138 C CG2 . THR A 1 143 ? 57.009 18.862 102.423 1.00 93.62 ? 526 THR A CG2 1 ATOM 1139 N N . SER A 1 144 ? 60.677 17.059 102.603 1.00 92.97 ? 527 SER A N 1 ATOM 1140 C CA . SER A 1 144 ? 61.043 15.778 103.221 1.00 94.59 ? 527 SER A CA 1 ATOM 1141 C C . SER A 1 144 ? 61.730 15.973 104.587 1.00 96.23 ? 527 SER A C 1 ATOM 1142 O O . SER A 1 144 ? 61.870 17.094 105.075 1.00 96.14 ? 527 SER A O 1 ATOM 1143 C CB . SER A 1 144 ? 61.956 14.964 102.281 1.00 93.54 ? 527 SER A CB 1 ATOM 1144 O OG . SER A 1 144 ? 63.325 15.305 102.457 1.00 91.45 ? 527 SER A OG 1 ATOM 1145 N N . LEU A 1 145 ? 62.191 14.872 105.171 1.00 96.47 ? 528 LEU A N 1 ATOM 1146 C CA . LEU A 1 145 ? 62.827 14.890 106.488 1.00 97.18 ? 528 LEU A CA 1 ATOM 1147 C C . LEU A 1 145 ? 64.236 15.504 106.487 1.00 95.52 ? 528 LEU A C 1 ATOM 1148 O O . LEU A 1 145 ? 64.774 15.820 107.552 1.00 95.80 ? 528 LEU A O 1 ATOM 1149 C CB . LEU A 1 145 ? 62.896 13.471 107.057 1.00 100.30 ? 528 LEU A CB 1 ATOM 1150 C CG . LEU A 1 145 ? 61.550 12.768 107.306 1.00 102.86 ? 528 LEU A CG 1 ATOM 1151 C CD1 . LEU A 1 145 ? 61.132 11.834 106.167 1.00 103.12 ? 528 LEU A CD1 1 ATOM 1152 C CD2 . LEU A 1 145 ? 61.615 11.997 108.617 1.00 105.00 ? 528 LEU A CD2 1 ATOM 1153 N N . LEU A 1 146 ? 64.827 15.666 105.300 1.00 92.69 ? 529 LEU A N 1 ATOM 1154 C CA . LEU A 1 146 ? 66.154 16.260 105.158 1.00 88.99 ? 529 LEU A CA 1 ATOM 1155 C C . LEU A 1 146 ? 66.133 17.753 105.489 1.00 87.21 ? 529 LEU A C 1 ATOM 1156 O O . LEU A 1 146 ? 67.031 18.251 106.162 1.00 85.64 ? 529 LEU A O 1 ATOM 1157 C CB . LEU A 1 146 ? 66.687 16.049 103.736 1.00 87.99 ? 529 LEU A CB 1 ATOM 1158 C CG . LEU A 1 146 ? 66.809 14.603 103.229 1.00 88.58 ? 529 LEU A CG 1 ATOM 1159 C CD1 . LEU A 1 146 ? 67.132 14.571 101.741 1.00 87.38 ? 529 LEU A CD1 1 ATOM 1160 C CD2 . LEU A 1 146 ? 67.845 13.825 104.025 1.00 89.44 ? 529 LEU A CD2 1 ATOM 1161 N N . HIS A 1 147 ? 65.099 18.450 105.011 1.00 86.74 ? 530 HIS A N 1 ATOM 1162 C CA . HIS A 1 147 ? 64.955 19.904 105.166 1.00 84.89 ? 530 HIS A CA 1 ATOM 1163 C C . HIS A 1 147 ? 66.171 20.680 104.653 1.00 78.90 ? 530 HIS A C 1 ATOM 1164 O O . HIS A 1 147 ? 66.578 21.679 105.251 1.00 78.12 ? 530 HIS A O 1 ATOM 1165 C CB . HIS A 1 147 ? 64.647 20.283 106.626 1.00 90.41 ? 530 HIS A CB 1 ATOM 1166 C CG . HIS A 1 147 ? 63.407 19.641 107.168 1.00 95.17 ? 530 HIS A CG 1 ATOM 1167 N ND1 . HIS A 1 147 ? 63.408 18.856 108.301 1.00 98.50 ? 530 HIS A ND1 1 ATOM 1168 C CD2 . HIS A 1 147 ? 62.127 19.669 106.728 1.00 95.95 ? 530 HIS A CD2 1 ATOM 1169 C CE1 . HIS A 1 147 ? 62.179 18.429 108.536 1.00 99.47 ? 530 HIS A CE1 1 ATOM 1170 N NE2 . HIS A 1 147 ? 61.384 18.907 107.595 1.00 97.74 ? 530 HIS A NE2 1 ATOM 1171 N N . ASP A 1 148 ? 66.744 20.205 103.544 1.00 74.11 ? 531 ASP A N 1 ATOM 1172 C CA . ASP A 1 148 ? 67.878 20.864 102.901 1.00 70.85 ? 531 ASP A CA 1 ATOM 1173 C C . ASP A 1 148 ? 67.349 21.859 101.872 1.00 66.09 ? 531 ASP A C 1 ATOM 1174 O O . ASP A 1 148 ? 66.265 21.658 101.318 1.00 62.97 ? 531 ASP A O 1 ATOM 1175 C CB . ASP A 1 148 ? 68.794 19.852 102.191 1.00 72.44 ? 531 ASP A CB 1 ATOM 1176 C CG . ASP A 1 148 ? 69.722 19.106 103.139 1.00 75.67 ? 531 ASP A CG 1 ATOM 1177 O OD1 . ASP A 1 148 ? 70.223 19.709 104.122 1.00 78.27 ? 531 ASP A OD1 1 ATOM 1178 O OD2 . ASP A 1 148 ? 69.985 17.913 102.869 1.00 78.09 ? 531 ASP A OD2 1 ATOM 1179 N N . PRO A 1 149 ? 68.114 22.930 101.597 1.00 62.41 ? 532 PRO A N 1 ATOM 1180 C CA . PRO A 1 149 ? 67.684 23.840 100.547 1.00 59.61 ? 532 PRO A CA 1 ATOM 1181 C C . PRO A 1 149 ? 67.958 23.277 99.150 1.00 56.10 ? 532 PRO A C 1 ATOM 1182 O O . PRO A 1 149 ? 68.841 22.432 98.988 1.00 55.25 ? 532 PRO A O 1 ATOM 1183 C CB . PRO A 1 149 ? 68.530 25.094 100.807 1.00 60.50 ? 532 PRO A CB 1 ATOM 1184 C CG . PRO A 1 149 ? 69.716 24.642 101.581 1.00 60.50 ? 532 PRO A CG 1 ATOM 1185 C CD . PRO A 1 149 ? 69.464 23.255 102.089 1.00 61.95 ? 532 PRO A CD 1 ATOM 1186 N N . CYS A 1 150 ? 67.195 23.749 98.164 1.00 52.98 ? 533 CYS A N 1 ATOM 1187 C CA . CYS A 1 150 ? 67.473 23.480 96.746 1.00 51.20 ? 533 CYS A CA 1 ATOM 1188 C C . CYS A 1 150 ? 68.318 24.573 96.072 1.00 49.72 ? 533 CYS A C 1 ATOM 1189 O O . CYS A 1 150 ? 69.044 24.311 95.109 1.00 48.64 ? 533 CYS A O 1 ATOM 1190 C CB . CYS A 1 150 ? 66.165 23.306 95.992 1.00 51.65 ? 533 CYS A CB 1 ATOM 1191 S SG . CYS A 1 150 ? 65.245 21.841 96.499 1.00 52.77 ? 533 CYS A SG 1 ATOM 1192 N N . LEU A 1 151 ? 68.234 25.790 96.603 1.00 50.06 ? 534 LEU A N 1 ATOM 1193 C CA . LEU A 1 151 ? 68.866 26.968 96.006 1.00 48.80 ? 534 LEU A CA 1 ATOM 1194 C C . LEU A 1 151 ? 70.377 26.791 95.906 1.00 47.89 ? 534 LEU A C 1 ATOM 1195 O O . LEU A 1 151 ? 70.998 26.332 96.857 1.00 49.20 ? 534 LEU A O 1 ATOM 1196 C CB . LEU A 1 151 ? 68.558 28.212 96.848 1.00 49.35 ? 534 LEU A CB 1 ATOM 1197 C CG . LEU A 1 151 ? 68.699 29.564 96.153 1.00 49.03 ? 534 LEU A CG 1 ATOM 1198 C CD1 . LEU A 1 151 ? 67.460 29.822 95.309 1.00 49.06 ? 534 LEU A CD1 1 ATOM 1199 C CD2 . LEU A 1 151 ? 68.893 30.682 97.160 1.00 49.04 ? 534 LEU A CD2 1 ATOM 1200 N N . GLY A 1 152 ? 70.954 27.147 94.759 1.00 46.42 ? 535 GLY A N 1 ATOM 1201 C CA . GLY A 1 152 ? 72.390 27.047 94.547 1.00 46.66 ? 535 GLY A CA 1 ATOM 1202 C C . GLY A 1 152 ? 73.128 28.047 95.404 1.00 47.71 ? 535 GLY A C 1 ATOM 1203 O O . GLY A 1 152 ? 72.538 29.015 95.881 1.00 49.01 ? 535 GLY A O 1 ATOM 1204 N N . THR A 1 153 ? 74.422 27.834 95.588 1.00 48.42 ? 536 THR A N 1 ATOM 1205 C CA . THR A 1 153 ? 75.207 28.669 96.496 1.00 50.63 ? 536 THR A CA 1 ATOM 1206 C C . THR A 1 153 ? 75.382 30.096 95.986 1.00 51.40 ? 536 THR A C 1 ATOM 1207 O O . THR A 1 153 ? 75.768 30.982 96.752 1.00 54.36 ? 536 THR A O 1 ATOM 1208 C CB . THR A 1 153 ? 76.599 28.089 96.759 1.00 51.11 ? 536 THR A CB 1 ATOM 1209 O OG1 . THR A 1 153 ? 77.360 28.121 95.553 1.00 53.51 ? 536 THR A OG1 1 ATOM 1210 C CG2 . THR A 1 153 ? 76.514 26.655 97.273 1.00 51.32 ? 536 THR A CG2 1 ATOM 1211 N N . PHE A 1 154 ? 75.124 30.302 94.695 1.00 50.86 ? 537 PHE A N 1 ATOM 1212 C CA . PHE A 1 154 ? 75.143 31.635 94.081 1.00 50.48 ? 537 PHE A CA 1 ATOM 1213 C C . PHE A 1 154 ? 73.885 32.478 94.340 1.00 50.34 ? 537 PHE A C 1 ATOM 1214 O O . PHE A 1 154 ? 73.836 33.633 93.917 1.00 51.43 ? 537 PHE A O 1 ATOM 1215 C CB . PHE A 1 154 ? 75.416 31.539 92.574 1.00 49.60 ? 537 PHE A CB 1 ATOM 1216 C CG . PHE A 1 154 ? 74.294 30.912 91.783 1.00 48.87 ? 537 PHE A CG 1 ATOM 1217 C CD1 . PHE A 1 154 ? 74.267 29.544 91.552 1.00 48.48 ? 537 PHE A CD1 1 ATOM 1218 C CD2 . PHE A 1 154 ? 73.282 31.696 91.245 1.00 48.08 ? 537 PHE A CD2 1 ATOM 1219 C CE1 . PHE A 1 154 ? 73.241 28.969 90.829 1.00 47.95 ? 537 PHE A CE1 1 ATOM 1220 C CE2 . PHE A 1 154 ? 72.254 31.127 90.516 1.00 46.89 ? 537 PHE A CE2 1 ATOM 1221 C CZ . PHE A 1 154 ? 72.230 29.766 90.312 1.00 47.27 ? 537 PHE A CZ 1 ATOM 1222 N N . GLY A 1 155 ? 72.878 31.911 95.006 1.00 49.07 ? 538 GLY A N 1 ATOM 1223 C CA . GLY A 1 155 ? 71.718 32.668 95.463 1.00 48.55 ? 538 GLY A CA 1 ATOM 1224 C C . GLY A 1 155 ? 70.497 32.606 94.565 1.00 48.00 ? 538 GLY A C 1 ATOM 1225 O O . GLY A 1 155 ? 69.527 33.354 94.775 1.00 48.41 ? 538 GLY A O 1 ATOM 1226 N N . GLY A 1 156 ? 70.526 31.732 93.566 1.00 46.57 ? 539 GLY A N 1 ATOM 1227 C CA . GLY A 1 156 ? 69.392 31.569 92.657 1.00 46.10 ? 539 GLY A CA 1 ATOM 1228 C C . GLY A 1 156 ? 69.102 30.121 92.339 1.00 45.53 ? 539 GLY A C 1 ATOM 1229 O O . GLY A 1 156 ? 69.939 29.249 92.568 1.00 46.27 ? 539 GLY A O 1 ATOM 1230 N N . PRO A 1 157 ? 67.916 29.853 91.780 1.00 45.69 ? 540 PRO A N 1 ATOM 1231 C CA . PRO A 1 157 ? 67.551 28.484 91.439 1.00 45.95 ? 540 PRO A CA 1 ATOM 1232 C C . PRO A 1 157 ? 68.309 27.984 90.219 1.00 46.21 ? 540 PRO A C 1 ATOM 1233 O O . PRO A 1 157 ? 68.699 28.776 89.373 1.00 48.00 ? 540 PRO A O 1 ATOM 1234 C CB . PRO A 1 157 ? 66.073 28.591 91.134 1.00 45.30 ? 540 PRO A CB 1 ATOM 1235 C CG . PRO A 1 157 ? 65.934 29.969 90.578 1.00 45.76 ? 540 PRO A CG 1 ATOM 1236 C CD . PRO A 1 157 ? 66.907 30.819 91.325 1.00 45.32 ? 540 PRO A CD 1 ATOM 1237 N N . VAL A 1 158 ? 68.532 26.677 90.169 1.00 46.93 ? 541 VAL A N 1 ATOM 1238 C CA . VAL A 1 158 ? 69.124 25.998 89.030 1.00 46.69 ? 541 VAL A CA 1 ATOM 1239 C C . VAL A 1 158 ? 68.010 25.198 88.363 1.00 46.67 ? 541 VAL A C 1 ATOM 1240 O O . VAL A 1 158 ? 67.492 24.239 88.940 1.00 49.62 ? 541 VAL A O 1 ATOM 1241 C CB . VAL A 1 158 ? 70.252 25.060 89.497 1.00 47.70 ? 541 VAL A CB 1 ATOM 1242 C CG1 . VAL A 1 158 ? 70.830 24.286 88.322 1.00 48.00 ? 541 VAL A CG1 1 ATOM 1243 C CG2 . VAL A 1 158 ? 71.345 25.861 90.194 1.00 48.03 ? 541 VAL A CG2 1 ATOM 1244 N N . PHE A 1 159 ? 67.607 25.603 87.169 1.00 46.45 ? 542 PHE A N 1 ATOM 1245 C CA . PHE A 1 159 ? 66.499 24.935 86.501 1.00 46.71 ? 542 PHE A CA 1 ATOM 1246 C C . PHE A 1 159 ? 66.948 23.605 85.900 1.00 46.09 ? 542 PHE A C 1 ATOM 1247 O O . PHE A 1 159 ? 67.960 23.561 85.213 1.00 46.38 ? 542 PHE A O 1 ATOM 1248 C CB . PHE A 1 159 ? 65.883 25.850 85.444 1.00 47.43 ? 542 PHE A CB 1 ATOM 1249 C CG . PHE A 1 159 ? 65.239 27.066 86.025 1.00 47.40 ? 542 PHE A CG 1 ATOM 1250 C CD1 . PHE A 1 159 ? 64.143 26.941 86.851 1.00 48.04 ? 542 PHE A CD1 1 ATOM 1251 C CD2 . PHE A 1 159 ? 65.738 28.333 85.768 1.00 49.03 ? 542 PHE A CD2 1 ATOM 1252 C CE1 . PHE A 1 159 ? 63.544 28.054 87.411 1.00 48.44 ? 542 PHE A CE1 1 ATOM 1253 C CE2 . PHE A 1 159 ? 65.145 29.453 86.321 1.00 48.67 ? 542 PHE A CE2 1 ATOM 1254 C CZ . PHE A 1 159 ? 64.047 29.311 87.147 1.00 48.89 ? 542 PHE A CZ 1 ATOM 1255 N N . PRO A 1 160 ? 66.193 22.520 86.144 1.00 46.05 ? 543 PRO A N 1 ATOM 1256 C CA . PRO A 1 160 ? 66.654 21.158 85.796 1.00 46.53 ? 543 PRO A CA 1 ATOM 1257 C C . PRO A 1 160 ? 66.989 20.925 84.306 1.00 46.05 ? 543 PRO A C 1 ATOM 1258 O O . PRO A 1 160 ? 67.970 20.251 84.002 1.00 45.42 ? 543 PRO A O 1 ATOM 1259 C CB . PRO A 1 160 ? 65.485 20.272 86.233 1.00 47.11 ? 543 PRO A CB 1 ATOM 1260 C CG . PRO A 1 160 ? 64.294 21.161 86.144 1.00 47.28 ? 543 PRO A CG 1 ATOM 1261 C CD . PRO A 1 160 ? 64.795 22.509 86.600 1.00 46.76 ? 543 PRO A CD 1 ATOM 1262 N N . TRP A 1 161 ? 66.205 21.511 83.406 1.00 45.64 ? 544 TRP A N 1 ATOM 1263 C CA . TRP A 1 161 ? 66.455 21.433 81.956 1.00 45.69 ? 544 TRP A CA 1 ATOM 1264 C C . TRP A 1 161 ? 67.780 22.078 81.492 1.00 46.03 ? 544 TRP A C 1 ATOM 1265 O O . TRP A 1 161 ? 68.248 21.784 80.396 1.00 46.25 ? 544 TRP A O 1 ATOM 1266 C CB . TRP A 1 161 ? 65.272 22.011 81.157 1.00 45.91 ? 544 TRP A CB 1 ATOM 1267 C CG . TRP A 1 161 ? 65.005 23.447 81.426 1.00 45.92 ? 544 TRP A CG 1 ATOM 1268 C CD1 . TRP A 1 161 ? 65.644 24.502 80.873 1.00 46.79 ? 544 TRP A CD1 1 ATOM 1269 C CD2 . TRP A 1 161 ? 64.031 23.995 82.326 1.00 46.38 ? 544 TRP A CD2 1 ATOM 1270 N NE1 . TRP A 1 161 ? 65.140 25.673 81.364 1.00 47.25 ? 544 TRP A NE1 1 ATOM 1271 C CE2 . TRP A 1 161 ? 64.148 25.394 82.259 1.00 46.12 ? 544 TRP A CE2 1 ATOM 1272 C CE3 . TRP A 1 161 ? 63.067 23.436 83.179 1.00 46.76 ? 544 TRP A CE3 1 ATOM 1273 C CZ2 . TRP A 1 161 ? 63.352 26.254 83.013 1.00 46.69 ? 544 TRP A CZ2 1 ATOM 1274 C CZ3 . TRP A 1 161 ? 62.265 24.288 83.930 1.00 47.19 ? 544 TRP A CZ3 1 ATOM 1275 C CH2 . TRP A 1 161 ? 62.417 25.687 83.843 1.00 47.49 ? 544 TRP A CH2 1 ATOM 1276 N N . LEU A 1 162 ? 68.383 22.941 82.313 1.00 44.89 ? 545 LEU A N 1 ATOM 1277 C CA . LEU A 1 162 ? 69.699 23.516 82.015 1.00 44.73 ? 545 LEU A CA 1 ATOM 1278 C C . LEU A 1 162 ? 70.884 22.642 82.426 1.00 45.74 ? 545 LEU A C 1 ATOM 1279 O O . LEU A 1 162 ? 71.981 22.840 81.929 1.00 46.51 ? 545 LEU A O 1 ATOM 1280 C CB . LEU A 1 162 ? 69.843 24.879 82.700 1.00 43.83 ? 545 LEU A CB 1 ATOM 1281 C CG . LEU A 1 162 ? 68.789 25.925 82.327 1.00 43.42 ? 545 LEU A CG 1 ATOM 1282 C CD1 . LEU A 1 162 ? 69.054 27.197 83.109 1.00 42.32 ? 545 LEU A CD1 1 ATOM 1283 C CD2 . LEU A 1 162 ? 68.760 26.206 80.834 1.00 42.92 ? 545 LEU A CD2 1 ATOM 1284 N N . VAL A 1 163 ? 70.674 21.700 83.342 1.00 46.65 ? 546 VAL A N 1 ATOM 1285 C CA . VAL A 1 163 ? 71.774 20.948 83.945 1.00 46.16 ? 546 VAL A CA 1 ATOM 1286 C C . VAL A 1 163 ? 71.733 19.427 83.684 1.00 47.24 ? 546 VAL A C 1 ATOM 1287 O O . VAL A 1 163 ? 72.570 18.684 84.205 1.00 46.55 ? 546 VAL A O 1 ATOM 1288 C CB . VAL A 1 163 ? 71.869 21.245 85.456 1.00 46.02 ? 546 VAL A CB 1 ATOM 1289 C CG1 . VAL A 1 163 ? 72.227 22.695 85.678 1.00 44.76 ? 546 VAL A CG1 1 ATOM 1290 C CG2 . VAL A 1 163 ? 70.579 20.910 86.190 1.00 46.66 ? 546 VAL A CG2 1 ATOM 1291 N N . LEU A 1 164 ? 70.800 18.973 82.853 1.00 48.01 ? 547 LEU A N 1 ATOM 1292 C CA . LEU A 1 164 ? 70.651 17.555 82.547 1.00 50.22 ? 547 LEU A CA 1 ATOM 1293 C C . LEU A 1 164 ? 70.352 17.381 81.072 1.00 51.80 ? 547 LEU A C 1 ATOM 1294 O O . LEU A 1 164 ? 69.721 18.240 80.472 1.00 53.77 ? 547 LEU A O 1 ATOM 1295 C CB . LEU A 1 164 ? 69.515 16.955 83.369 1.00 50.60 ? 547 LEU A CB 1 ATOM 1296 C CG . LEU A 1 164 ? 69.735 17.008 84.879 1.00 51.03 ? 547 LEU A CG 1 ATOM 1297 C CD1 . LEU A 1 164 ? 68.439 16.736 85.614 1.00 52.14 ? 547 LEU A CD1 1 ATOM 1298 C CD2 . LEU A 1 164 ? 70.808 16.009 85.285 1.00 52.24 ? 547 LEU A CD2 1 ATOM 1299 N N . GLY A 1 165 ? 70.807 16.268 80.502 1.00 53.27 ? 548 GLY A N 1 ATOM 1300 C CA . GLY A 1 165 ? 70.539 15.927 79.106 1.00 54.07 ? 548 GLY A CA 1 ATOM 1301 C C . GLY A 1 165 ? 70.151 14.470 78.933 1.00 54.81 ? 548 GLY A C 1 ATOM 1302 O O . GLY A 1 165 ? 70.458 13.633 79.782 1.00 54.87 ? 548 GLY A O 1 ATOM 1303 N N . GLY A 1 166 ? 69.446 14.190 77.836 1.00 55.96 ? 549 GLY A N 1 ATOM 1304 C CA . GLY A 1 166 ? 69.122 12.832 77.415 1.00 57.14 ? 549 GLY A CA 1 ATOM 1305 C C . GLY A 1 166 ? 68.050 12.123 78.218 1.00 58.64 ? 549 GLY A C 1 ATOM 1306 O O . GLY A 1 166 ? 68.081 10.904 78.368 1.00 62.23 ? 549 GLY A O 1 ATOM 1307 N N . TYR A 1 167 ? 67.087 12.883 78.711 1.00 58.15 ? 550 TYR A N 1 ATOM 1308 C CA . TYR A 1 167 ? 65.971 12.344 79.481 1.00 58.16 ? 550 TYR A CA 1 ATOM 1309 C C . TYR A 1 167 ? 64.727 12.518 78.632 1.00 59.48 ? 550 TYR A C 1 ATOM 1310 O O . TYR A 1 167 ? 64.703 13.332 77.709 1.00 60.08 ? 550 TYR A O 1 ATOM 1311 C CB . TYR A 1 167 ? 65.810 13.076 80.828 1.00 58.11 ? 550 TYR A CB 1 ATOM 1312 C CG . TYR A 1 167 ? 65.641 14.578 80.691 1.00 56.72 ? 550 TYR A CG 1 ATOM 1313 C CD1 . TYR A 1 167 ? 66.750 15.418 80.666 1.00 55.86 ? 550 TYR A CD1 1 ATOM 1314 C CD2 . TYR A 1 167 ? 64.378 15.147 80.548 1.00 56.96 ? 550 TYR A CD2 1 ATOM 1315 C CE1 . TYR A 1 167 ? 66.611 16.783 80.511 1.00 55.86 ? 550 TYR A CE1 1 ATOM 1316 C CE2 . TYR A 1 167 ? 64.230 16.518 80.398 1.00 57.48 ? 550 TYR A CE2 1 ATOM 1317 C CZ . TYR A 1 167 ? 65.351 17.328 80.380 1.00 55.82 ? 550 TYR A CZ 1 ATOM 1318 O OH . TYR A 1 167 ? 65.214 18.678 80.221 1.00 55.51 ? 550 TYR A OH 1 ATOM 1319 N N . ASP A 1 168 ? 63.689 11.772 78.980 1.00 61.59 ? 551 ASP A N 1 ATOM 1320 C CA . ASP A 1 168 ? 62.410 11.789 78.264 1.00 63.37 ? 551 ASP A CA 1 ATOM 1321 C C . ASP A 1 168 ? 61.392 12.628 79.034 1.00 64.51 ? 551 ASP A C 1 ATOM 1322 O O . ASP A 1 168 ? 61.381 12.606 80.267 1.00 64.55 ? 551 ASP A O 1 ATOM 1323 C CB . ASP A 1 168 ? 61.882 10.367 78.098 1.00 63.68 ? 551 ASP A CB 1 ATOM 1324 C CG . ASP A 1 168 ? 61.652 9.680 79.426 1.00 64.11 ? 551 ASP A CG 1 ATOM 1325 O OD1 . ASP A 1 168 ? 62.648 9.468 80.158 1.00 64.08 ? 551 ASP A OD1 1 ATOM 1326 O OD2 . ASP A 1 168 ? 60.486 9.388 79.753 1.00 64.23 ? 551 ASP A OD2 1 ATOM 1327 N N . ASP A 1 169 ? 60.540 13.347 78.299 1.00 66.40 ? 552 ASP A N 1 ATOM 1328 C CA . ASP A 1 169 ? 59.557 14.272 78.872 1.00 67.30 ? 552 ASP A CA 1 ATOM 1329 C C . ASP A 1 169 ? 60.188 15.141 79.980 1.00 64.74 ? 552 ASP A C 1 ATOM 1330 O O . ASP A 1 169 ? 61.190 15.802 79.711 1.00 61.55 ? 552 ASP A O 1 ATOM 1331 C CB . ASP A 1 169 ? 58.308 13.505 79.332 1.00 71.29 ? 552 ASP A CB 1 ATOM 1332 C CG . ASP A 1 169 ? 57.482 12.971 78.170 1.00 76.34 ? 552 ASP A CG 1 ATOM 1333 O OD1 . ASP A 1 169 ? 57.251 13.724 77.193 1.00 78.99 ? 552 ASP A OD1 1 ATOM 1334 O OD2 . ASP A 1 169 ? 57.021 11.806 78.253 1.00 80.83 ? 552 ASP A OD2 1 ATOM 1335 N N . GLN A 1 170 ? 59.645 15.122 81.204 1.00 64.84 ? 553 GLN A N 1 ATOM 1336 C CA . GLN A 1 170 ? 60.252 15.809 82.348 1.00 64.41 ? 553 GLN A CA 1 ATOM 1337 C C . GLN A 1 170 ? 60.691 14.805 83.424 1.00 61.10 ? 553 GLN A C 1 ATOM 1338 O O . GLN A 1 170 ? 60.684 15.112 84.613 1.00 61.01 ? 553 GLN A O 1 ATOM 1339 C CB . GLN A 1 170 ? 59.286 16.859 82.915 1.00 66.42 ? 553 GLN A CB 1 ATOM 1340 C CG . GLN A 1 170 ? 58.918 17.946 81.908 1.00 69.62 ? 553 GLN A CG 1 ATOM 1341 C CD . GLN A 1 170 ? 57.995 19.008 82.488 1.00 72.21 ? 553 GLN A CD 1 ATOM 1342 O OE1 . GLN A 1 170 ? 58.450 19.953 83.144 1.00 75.07 ? 553 GLN A OE1 1 ATOM 1343 N NE2 . GLN A 1 170 ? 56.699 18.874 82.229 1.00 72.48 ? 553 GLN A NE2 1 ATOM 1344 N N . ASN A 1 171 ? 61.095 13.617 82.990 1.00 58.77 ? 554 ASN A N 1 ATOM 1345 C CA . ASN A 1 171 ? 61.588 12.588 83.884 1.00 58.43 ? 554 ASN A CA 1 ATOM 1346 C C . ASN A 1 171 ? 63.084 12.774 84.051 1.00 57.24 ? 554 ASN A C 1 ATOM 1347 O O . ASN A 1 171 ? 63.887 12.007 83.512 1.00 59.69 ? 554 ASN A O 1 ATOM 1348 C CB . ASN A 1 171 ? 61.260 11.193 83.337 1.00 58.99 ? 554 ASN A CB 1 ATOM 1349 C CG . ASN A 1 171 ? 59.770 10.901 83.338 1.00 58.13 ? 554 ASN A CG 1 ATOM 1350 O OD1 . ASN A 1 171 ? 59.088 11.128 84.331 1.00 57.95 ? 554 ASN A OD1 1 ATOM 1351 N ND2 . ASN A 1 171 ? 59.268 10.379 82.234 1.00 57.72 ? 554 ASN A ND2 1 ATOM 1352 N N . TYR A 1 172 ? 63.448 13.788 84.832 1.00 54.80 ? 555 TYR A N 1 ATOM 1353 C CA . TYR A 1 172 ? 64.841 14.236 84.957 1.00 53.22 ? 555 TYR A CA 1 ATOM 1354 C C . TYR A 1 172 ? 65.740 13.146 85.535 1.00 54.46 ? 555 TYR A C 1 ATOM 1355 O O . TYR A 1 172 ? 66.933 13.092 85.243 1.00 53.70 ? 555 TYR A O 1 ATOM 1356 C CB . TYR A 1 172 ? 64.924 15.508 85.815 1.00 51.42 ? 555 TYR A CB 1 ATOM 1357 C CG . TYR A 1 172 ? 64.222 16.693 85.188 1.00 51.29 ? 555 TYR A CG 1 ATOM 1358 C CD1 . TYR A 1 172 ? 64.729 17.299 84.039 1.00 50.84 ? 555 TYR A CD1 1 ATOM 1359 C CD2 . TYR A 1 172 ? 63.033 17.190 85.723 1.00 50.24 ? 555 TYR A CD2 1 ATOM 1360 C CE1 . TYR A 1 172 ? 64.075 18.373 83.451 1.00 51.19 ? 555 TYR A CE1 1 ATOM 1361 C CE2 . TYR A 1 172 ? 62.379 18.260 85.141 1.00 49.95 ? 555 TYR A CE2 1 ATOM 1362 C CZ . TYR A 1 172 ? 62.903 18.853 84.012 1.00 50.46 ? 555 TYR A CZ 1 ATOM 1363 O OH . TYR A 1 172 ? 62.261 19.923 83.437 1.00 51.06 ? 555 TYR A OH 1 ATOM 1364 N N . ASN A 1 173 ? 65.148 12.303 86.378 1.00 55.34 ? 556 ASN A N 1 ATOM 1365 C CA . ASN A 1 173 ? 65.783 11.097 86.892 1.00 56.03 ? 556 ASN A CA 1 ATOM 1366 C C . ASN A 1 173 ? 66.404 10.188 85.820 1.00 55.89 ? 556 ASN A C 1 ATOM 1367 O O . ASN A 1 173 ? 67.399 9.530 86.093 1.00 54.66 ? 556 ASN A O 1 ATOM 1368 C CB . ASN A 1 173 ? 64.769 10.301 87.717 1.00 58.21 ? 556 ASN A CB 1 ATOM 1369 C CG . ASN A 1 173 ? 63.524 9.934 86.919 1.00 59.28 ? 556 ASN A CG 1 ATOM 1370 O OD1 . ASN A 1 173 ? 62.696 10.790 86.609 1.00 58.81 ? 556 ASN A OD1 1 ATOM 1371 N ND2 . ASN A 1 173 ? 63.396 8.660 86.575 1.00 61.25 ? 556 ASN A ND2 1 ATOM 1372 N N . ASN A 1 174 ? 65.841 10.166 84.609 1.00 56.52 ? 557 ASN A N 1 ATOM 1373 C CA . ASN A 1 174 ? 66.368 9.329 83.512 1.00 57.65 ? 557 ASN A CA 1 ATOM 1374 C C . ASN A 1 174 ? 67.448 9.988 82.665 1.00 56.17 ? 557 ASN A C 1 ATOM 1375 O O . ASN A 1 174 ? 67.738 9.517 81.573 1.00 56.95 ? 557 ASN A O 1 ATOM 1376 C CB . ASN A 1 174 ? 65.186 8.752 82.686 1.00 61.08 ? 557 ASN A CB 1 ATOM 1377 C CG . ASN A 1 174 ? 64.384 7.753 83.551 1.00 66.02 ? 557 ASN A CG 1 ATOM 1378 O OD1 . ASN A 1 174 ? 64.972 7.257 84.485 1.00 66.81 ? 557 ASN A OD1 1 ATOM 1379 N ND2 . ASN A 1 174 ? 63.125 7.441 83.334 1.00 72.91 ? 557 ASN A ND2 1 ATOM 1380 N N . ALA A 1 175 ? 68.090 11.034 83.195 1.00 54.68 ? 558 ALA A N 1 ATOM 1381 C CA . ALA A 1 175 ? 69.122 11.756 82.469 1.00 53.86 ? 558 ALA A CA 1 ATOM 1382 C C . ALA A 1 175 ? 70.326 10.865 82.191 1.00 54.80 ? 558 ALA A C 1 ATOM 1383 O O . ALA A 1 175 ? 70.748 10.104 83.057 1.00 53.47 ? 558 ALA A O 1 ATOM 1384 C CB . ALA A 1 175 ? 69.560 12.988 83.250 1.00 53.23 ? 558 ALA A CB 1 ATOM 1385 N N . THR A 1 176 ? 70.869 10.972 80.979 1.00 55.49 ? 559 THR A N 1 ATOM 1386 C CA . THR A 1 176 ? 72.110 10.286 80.601 1.00 57.30 ? 559 THR A CA 1 ATOM 1387 C C . THR A 1 176 ? 73.304 11.244 80.482 1.00 56.84 ? 559 THR A C 1 ATOM 1388 O O . THR A 1 176 ? 74.396 10.821 80.108 1.00 58.94 ? 559 THR A O 1 ATOM 1389 C CB . THR A 1 176 ? 71.933 9.520 79.275 1.00 57.61 ? 559 THR A CB 1 ATOM 1390 O OG1 . THR A 1 176 ? 71.465 10.421 78.272 1.00 57.02 ? 559 THR A OG1 1 ATOM 1391 C CG2 . THR A 1 176 ? 70.919 8.387 79.443 1.00 57.80 ? 559 THR A CG2 1 ATOM 1392 N N . ALA A 1 177 ? 73.109 12.516 80.824 1.00 55.36 ? 560 ALA A N 1 ATOM 1393 C CA . ALA A 1 177 ? 74.194 13.501 80.782 1.00 53.62 ? 560 ALA A CA 1 ATOM 1394 C C . ALA A 1 177 ? 73.958 14.631 81.767 1.00 52.18 ? 560 ALA A C 1 ATOM 1395 O O . ALA A 1 177 ? 72.816 15.026 82.009 1.00 53.04 ? 560 ALA A O 1 ATOM 1396 C CB . ALA A 1 177 ? 74.339 14.064 79.380 1.00 53.53 ? 560 ALA A CB 1 ATOM 1397 N N . LEU A 1 178 ? 75.043 15.127 82.342 1.00 51.27 ? 561 LEU A N 1 ATOM 1398 C CA . LEU A 1 178 ? 75.020 16.324 83.156 1.00 51.42 ? 561 LEU A CA 1 ATOM 1399 C C . LEU A 1 178 ? 75.609 17.455 82.337 1.00 51.23 ? 561 LEU A C 1 ATOM 1400 O O . LEU A 1 178 ? 76.515 17.239 81.536 1.00 52.35 ? 561 LEU A O 1 ATOM 1401 C CB . LEU A 1 178 ? 75.850 16.140 84.419 1.00 52.04 ? 561 LEU A CB 1 ATOM 1402 C CG . LEU A 1 178 ? 75.597 14.891 85.249 1.00 53.19 ? 561 LEU A CG 1 ATOM 1403 C CD1 . LEU A 1 178 ? 76.547 14.891 86.433 1.00 54.53 ? 561 LEU A CD1 1 ATOM 1404 C CD2 . LEU A 1 178 ? 74.158 14.815 85.723 1.00 53.94 ? 561 LEU A CD2 1 ATOM 1405 N N . VAL A 1 179 ? 75.090 18.659 82.546 1.00 50.66 ? 562 VAL A N 1 ATOM 1406 C CA . VAL A 1 179 ? 75.588 19.855 81.898 1.00 49.69 ? 562 VAL A CA 1 ATOM 1407 C C . VAL A 1 179 ? 76.008 20.813 83.010 1.00 49.84 ? 562 VAL A C 1 ATOM 1408 O O . VAL A 1 179 ? 75.246 21.039 83.949 1.00 48.91 ? 562 VAL A O 1 ATOM 1409 C CB . VAL A 1 179 ? 74.515 20.486 80.993 1.00 49.59 ? 562 VAL A CB 1 ATOM 1410 C CG1 . VAL A 1 179 ? 75.059 21.718 80.287 1.00 50.40 ? 562 VAL A CG1 1 ATOM 1411 C CG2 . VAL A 1 179 ? 74.045 19.492 79.953 1.00 50.08 ? 562 VAL A CG2 1 ATOM 1412 N N . ILE A 1 180 ? 77.229 21.334 82.918 1.00 50.76 ? 563 ILE A N 1 ATOM 1413 C CA . ILE A 1 180 ? 77.783 22.262 83.905 1.00 52.69 ? 563 ILE A CA 1 ATOM 1414 C C . ILE A 1 180 ? 78.104 23.579 83.192 1.00 52.58 ? 563 ILE A C 1 ATOM 1415 O O . ILE A 1 180 ? 78.787 23.559 82.178 1.00 52.85 ? 563 ILE A O 1 ATOM 1416 C CB . ILE A 1 180 ? 79.058 21.685 84.541 1.00 55.36 ? 563 ILE A CB 1 ATOM 1417 C CG1 . ILE A 1 180 ? 78.711 20.438 85.351 1.00 56.53 ? 563 ILE A CG1 1 ATOM 1418 C CG2 . ILE A 1 180 ? 79.747 22.712 85.445 1.00 57.07 ? 563 ILE A CG2 1 ATOM 1419 C CD1 . ILE A 1 180 ? 79.912 19.810 86.029 1.00 58.97 ? 563 ILE A CD1 1 ATOM 1420 N N . THR A 1 181 ? 77.613 24.703 83.719 1.00 51.62 ? 564 THR A N 1 ATOM 1421 C CA . THR A 1 181 ? 77.735 25.992 83.048 1.00 52.63 ? 564 THR A CA 1 ATOM 1422 C C . THR A 1 181 ? 78.220 27.092 83.992 1.00 54.08 ? 564 THR A C 1 ATOM 1423 O O . THR A 1 181 ? 77.618 27.313 85.028 1.00 56.77 ? 564 THR A O 1 ATOM 1424 C CB . THR A 1 181 ? 76.396 26.389 82.407 1.00 52.33 ? 564 THR A CB 1 ATOM 1425 O OG1 . THR A 1 181 ? 75.932 25.315 81.584 1.00 52.39 ? 564 THR A OG1 1 ATOM 1426 C CG2 . THR A 1 181 ? 76.560 27.609 81.527 1.00 54.32 ? 564 THR A CG2 1 ATOM 1427 N N . PHE A 1 182 ? 79.301 27.770 83.607 1.00 55.38 ? 565 PHE A N 1 ATOM 1428 C CA . PHE A 1 182 ? 79.887 28.890 84.352 1.00 56.72 ? 565 PHE A CA 1 ATOM 1429 C C . PHE A 1 182 ? 79.731 30.144 83.494 1.00 56.92 ? 565 PHE A C 1 ATOM 1430 O O . PHE A 1 182 ? 80.368 30.241 82.445 1.00 57.28 ? 565 PHE A O 1 ATOM 1431 C CB . PHE A 1 182 ? 81.401 28.695 84.576 1.00 58.53 ? 565 PHE A CB 1 ATOM 1432 C CG . PHE A 1 182 ? 81.778 27.401 85.240 1.00 60.39 ? 565 PHE A CG 1 ATOM 1433 C CD1 . PHE A 1 182 ? 81.991 26.249 84.484 1.00 60.87 ? 565 PHE A CD1 1 ATOM 1434 C CD2 . PHE A 1 182 ? 81.966 27.337 86.624 1.00 62.06 ? 565 PHE A CD2 1 ATOM 1435 C CE1 . PHE A 1 182 ? 82.348 25.048 85.097 1.00 62.09 ? 565 PHE A CE1 1 ATOM 1436 C CE2 . PHE A 1 182 ? 82.328 26.144 87.243 1.00 62.79 ? 565 PHE A CE2 1 ATOM 1437 C CZ . PHE A 1 182 ? 82.516 24.995 86.478 1.00 63.08 ? 565 PHE A CZ 1 ATOM 1438 N N . PRO A 1 183 ? 78.880 31.098 83.903 1.00 57.80 ? 566 PRO A N 1 ATOM 1439 C CA . PRO A 1 183 ? 78.914 32.391 83.216 1.00 57.51 ? 566 PRO A CA 1 ATOM 1440 C C . PRO A 1 183 ? 80.149 33.193 83.605 1.00 58.26 ? 566 PRO A C 1 ATOM 1441 O O . PRO A 1 183 ? 80.481 33.261 84.788 1.00 58.31 ? 566 PRO A O 1 ATOM 1442 C CB . PRO A 1 183 ? 77.646 33.091 83.711 1.00 58.86 ? 566 PRO A CB 1 ATOM 1443 C CG . PRO A 1 183 ? 76.764 31.999 84.218 1.00 58.51 ? 566 PRO A CG 1 ATOM 1444 C CD . PRO A 1 183 ? 77.702 30.976 84.777 1.00 58.21 ? 566 PRO A CD 1 ATOM 1445 N N . VAL A 1 184 ? 80.836 33.759 82.612 1.00 60.40 ? 567 VAL A N 1 ATOM 1446 C CA . VAL A 1 184 ? 81.974 34.669 82.835 1.00 61.51 ? 567 VAL A CA 1 ATOM 1447 C C . VAL A 1 184 ? 81.804 35.940 82.006 1.00 62.20 ? 567 VAL A C 1 ATOM 1448 O O . VAL A 1 184 ? 81.195 35.908 80.933 1.00 60.53 ? 567 VAL A O 1 ATOM 1449 C CB . VAL A 1 184 ? 83.333 34.010 82.513 1.00 62.46 ? 567 VAL A CB 1 ATOM 1450 C CG1 . VAL A 1 184 ? 83.475 32.686 83.259 1.00 63.58 ? 567 VAL A CG1 1 ATOM 1451 C CG2 . VAL A 1 184 ? 83.523 33.798 81.019 1.00 62.40 ? 567 VAL A CG2 1 ATOM 1452 N N . ASN A 1 185 ? 82.348 37.047 82.514 1.00 64.16 ? 568 ASN A N 1 ATOM 1453 C CA . ASN A 1 185 ? 82.246 38.363 81.857 1.00 64.66 ? 568 ASN A CA 1 ATOM 1454 C C . ASN A 1 185 ? 82.819 38.307 80.461 1.00 64.23 ? 568 ASN A C 1 ATOM 1455 O O . ASN A 1 185 ? 83.927 37.797 80.273 1.00 64.41 ? 568 ASN A O 1 ATOM 1456 C CB . ASN A 1 185 ? 83.004 39.443 82.644 1.00 66.57 ? 568 ASN A CB 1 ATOM 1457 C CG . ASN A 1 185 ? 82.115 40.190 83.614 1.00 68.33 ? 568 ASN A CG 1 ATOM 1458 O OD1 . ASN A 1 185 ? 81.353 41.066 83.213 1.00 68.77 ? 568 ASN A OD1 1 ATOM 1459 N ND2 . ASN A 1 185 ? 82.217 39.858 84.902 1.00 70.11 ? 568 ASN A ND2 1 ATOM 1460 N N . ASN A 1 186 ? 82.069 38.805 79.480 1.00 65.77 ? 569 ASN A N 1 ATOM 1461 C CA . ASN A 1 186 ? 82.645 38.975 78.142 1.00 69.81 ? 569 ASN A CA 1 ATOM 1462 C C . ASN A 1 186 ? 83.550 40.207 78.045 1.00 71.85 ? 569 ASN A C 1 ATOM 1463 O O . ASN A 1 186 ? 84.430 40.228 77.196 1.00 75.12 ? 569 ASN A O 1 ATOM 1464 C CB . ASN A 1 186 ? 81.643 38.850 76.992 1.00 70.77 ? 569 ASN A CB 1 ATOM 1465 C CG . ASN A 1 186 ? 80.627 39.946 76.962 1.00 72.87 ? 569 ASN A CG 1 ATOM 1466 O OD1 . ASN A 1 186 ? 80.954 41.077 77.273 1.00 74.94 ? 569 ASN A OD1 1 ATOM 1467 N ND2 . ASN A 1 186 ? 79.395 39.634 76.536 1.00 72.69 ? 569 ASN A ND2 1 ATOM 1468 N N . TYR A 1 187 ? 83.361 41.199 78.926 1.00 73.66 ? 570 TYR A N 1 ATOM 1469 C CA . TYR A 1 187 ? 84.219 42.403 78.979 1.00 76.73 ? 570 TYR A CA 1 ATOM 1470 C C . TYR A 1 187 ? 84.376 43.111 77.613 1.00 81.22 ? 570 TYR A C 1 ATOM 1471 O O . TYR A 1 187 ? 85.449 43.604 77.275 1.00 83.16 ? 570 TYR A O 1 ATOM 1472 C CB . TYR A 1 187 ? 85.610 42.072 79.560 1.00 75.90 ? 570 TYR A CB 1 ATOM 1473 C CG . TYR A 1 187 ? 85.659 41.716 81.034 1.00 75.68 ? 570 TYR A CG 1 ATOM 1474 C CD1 . TYR A 1 187 ? 86.199 40.495 81.462 1.00 74.99 ? 570 TYR A CD1 1 ATOM 1475 C CD2 . TYR A 1 187 ? 85.206 42.611 82.010 1.00 76.97 ? 570 TYR A CD2 1 ATOM 1476 C CE1 . TYR A 1 187 ? 86.265 40.166 82.814 1.00 75.77 ? 570 TYR A CE1 1 ATOM 1477 C CE2 . TYR A 1 187 ? 85.261 42.289 83.367 1.00 77.31 ? 570 TYR A CE2 1 ATOM 1478 C CZ . TYR A 1 187 ? 85.787 41.067 83.769 1.00 76.97 ? 570 TYR A CZ 1 ATOM 1479 O OH . TYR A 1 187 ? 85.842 40.744 85.112 1.00 75.84 ? 570 TYR A OH 1 ATOM 1480 N N . TYR A 1 188 ? 83.301 43.161 76.833 1.00 85.63 ? 571 TYR A N 1 ATOM 1481 C CA . TYR A 1 188 ? 83.295 43.821 75.519 1.00 90.61 ? 571 TYR A CA 1 ATOM 1482 C C . TYR A 1 188 ? 83.875 45.246 75.470 1.00 93.80 ? 571 TYR A C 1 ATOM 1483 O O . TYR A 1 188 ? 84.401 45.664 74.434 1.00 93.50 ? 571 TYR A O 1 ATOM 1484 C CB . TYR A 1 188 ? 81.844 43.901 75.009 1.00 92.12 ? 571 TYR A CB 1 ATOM 1485 C CG . TYR A 1 188 ? 80.981 44.896 75.790 1.00 94.84 ? 571 TYR A CG 1 ATOM 1486 C CD1 . TYR A 1 188 ? 80.595 44.653 77.121 1.00 95.41 ? 571 TYR A CD1 1 ATOM 1487 C CD2 . TYR A 1 188 ? 80.596 46.106 75.214 1.00 97.32 ? 571 TYR A CD2 1 ATOM 1488 C CE1 . TYR A 1 188 ? 79.847 45.576 77.835 1.00 97.29 ? 571 TYR A CE1 1 ATOM 1489 C CE2 . TYR A 1 188 ? 79.838 47.032 75.920 1.00 98.49 ? 571 TYR A CE2 1 ATOM 1490 C CZ . TYR A 1 188 ? 79.466 46.762 77.229 1.00 98.84 ? 571 TYR A CZ 1 ATOM 1491 O OH . TYR A 1 188 ? 78.724 47.669 77.943 1.00 99.24 ? 571 TYR A OH 1 ATOM 1492 N N . ASN A 1 189 ? 83.728 45.986 76.570 1.00 95.65 ? 572 ASN A N 1 ATOM 1493 C CA . ASN A 1 189 ? 84.219 47.354 76.677 1.00 100.09 ? 572 ASN A CA 1 ATOM 1494 C C . ASN A 1 189 ? 85.532 47.492 77.441 1.00 99.54 ? 572 ASN A C 1 ATOM 1495 O O . ASN A 1 189 ? 86.095 48.582 77.464 1.00 100.10 ? 572 ASN A O 1 ATOM 1496 C CB . ASN A 1 189 ? 83.155 48.237 77.364 1.00 103.17 ? 572 ASN A CB 1 ATOM 1497 C CG . ASN A 1 189 ? 83.378 48.385 78.873 1.00 106.57 ? 572 ASN A CG 1 ATOM 1498 O OD1 . ASN A 1 189 ? 83.141 47.454 79.640 1.00 100.13 ? 572 ASN A OD1 1 ATOM 1499 N ND2 . ASN A 1 189 ? 83.845 49.571 79.293 1.00 116.97 ? 572 ASN A ND2 1 ATOM 1500 N N . ASP A 1 190 ? 85.978 46.437 78.120 1.00 97.71 ? 573 ASP A N 1 ATOM 1501 C CA . ASP A 1 190 ? 87.225 46.487 78.885 1.00 98.75 ? 573 ASP A CA 1 ATOM 1502 C C . ASP A 1 190 ? 88.239 45.497 78.320 1.00 99.76 ? 573 ASP A C 1 ATOM 1503 O O . ASP A 1 190 ? 88.133 44.289 78.514 1.00 97.75 ? 573 ASP A O 1 ATOM 1504 C CB . ASP A 1 190 ? 86.975 46.238 80.378 1.00 97.79 ? 573 ASP A CB 1 ATOM 1505 C CG . ASP A 1 190 ? 88.084 46.817 81.260 1.00 97.15 ? 573 ASP A CG 1 ATOM 1506 O OD1 . ASP A 1 190 ? 89.278 46.662 80.925 1.00 92.35 ? 573 ASP A OD1 1 ATOM 1507 O OD2 . ASP A 1 190 ? 87.753 47.430 82.295 1.00 98.74 ? 573 ASP A OD2 1 ATOM 1508 N N . THR A 1 191 ? 89.235 46.042 77.637 1.00 102.41 ? 574 THR A N 1 ATOM 1509 C CA . THR A 1 191 ? 90.255 45.255 76.961 1.00 103.87 ? 574 THR A CA 1 ATOM 1510 C C . THR A 1 191 ? 91.213 44.561 77.933 1.00 104.34 ? 574 THR A C 1 ATOM 1511 O O . THR A 1 191 ? 91.548 43.402 77.739 1.00 100.57 ? 574 THR A O 1 ATOM 1512 C CB . THR A 1 191 ? 91.032 46.153 75.980 1.00 106.37 ? 574 THR A CB 1 ATOM 1513 O OG1 . THR A 1 191 ? 90.174 46.479 74.882 1.00 106.41 ? 574 THR A OG1 1 ATOM 1514 C CG2 . THR A 1 191 ? 92.276 45.482 75.451 1.00 106.79 ? 574 THR A CG2 1 ATOM 1515 N N . GLU A 1 192 ? 91.644 45.268 78.974 1.00 108.06 ? 575 GLU A N 1 ATOM 1516 C CA . GLU A 1 192 ? 92.616 44.712 79.931 1.00 110.01 ? 575 GLU A CA 1 ATOM 1517 C C . GLU A 1 192 ? 92.021 43.597 80.799 1.00 106.14 ? 575 GLU A C 1 ATOM 1518 O O . GLU A 1 192 ? 92.720 42.644 81.143 1.00 106.10 ? 575 GLU A O 1 ATOM 1519 C CB . GLU A 1 192 ? 93.222 45.814 80.801 1.00 114.79 ? 575 GLU A CB 1 ATOM 1520 C CG . GLU A 1 192 ? 94.134 46.738 79.979 1.00 119.38 ? 575 GLU A CG 1 ATOM 1521 C CD . GLU A 1 192 ? 94.561 48.015 80.684 1.00 123.62 ? 575 GLU A CD 1 ATOM 1522 O OE1 . GLU A 1 192 ? 93.966 48.385 81.722 1.00 127.27 ? 575 GLU A OE1 1 ATOM 1523 O OE2 . GLU A 1 192 ? 95.509 48.657 80.182 1.00 125.22 ? 575 GLU A OE2 1 ATOM 1524 N N . LYS A 1 193 ? 90.738 43.720 81.146 1.00 100.83 ? 576 LYS A N 1 ATOM 1525 C CA . LYS A 1 193 ? 90.039 42.692 81.925 1.00 94.97 ? 576 LYS A CA 1 ATOM 1526 C C . LYS A 1 193 ? 89.637 41.492 81.067 1.00 88.50 ? 576 LYS A C 1 ATOM 1527 O O . LYS A 1 193 ? 89.564 40.376 81.577 1.00 84.70 ? 576 LYS A O 1 ATOM 1528 C CB . LYS A 1 193 ? 88.813 43.281 82.630 1.00 97.21 ? 576 LYS A CB 1 ATOM 1529 C CG . LYS A 1 193 ? 89.160 44.335 83.676 1.00 100.62 ? 576 LYS A CG 1 ATOM 1530 C CD . LYS A 1 193 ? 87.923 45.019 84.257 1.00 102.68 ? 576 LYS A CD 1 ATOM 1531 C CE . LYS A 1 193 ? 87.454 44.387 85.562 1.00 103.85 ? 576 LYS A CE 1 ATOM 1532 N NZ . LYS A 1 193 ? 88.246 44.905 86.710 1.00 104.92 ? 576 LYS A NZ 1 ATOM 1533 N N . LEU A 1 194 ? 89.373 41.719 79.779 1.00 84.50 ? 577 LEU A N 1 ATOM 1534 C CA . LEU A 1 194 ? 89.031 40.631 78.858 1.00 82.16 ? 577 LEU A CA 1 ATOM 1535 C C . LEU A 1 194 ? 90.216 39.710 78.629 1.00 81.54 ? 577 LEU A C 1 ATOM 1536 O O . LEU A 1 194 ? 90.070 38.494 78.618 1.00 80.50 ? 577 LEU A O 1 ATOM 1537 C CB . LEU A 1 194 ? 88.551 41.186 77.519 1.00 82.88 ? 577 LEU A CB 1 ATOM 1538 C CG . LEU A 1 194 ? 88.044 40.220 76.438 1.00 84.22 ? 577 LEU A CG 1 ATOM 1539 C CD1 . LEU A 1 194 ? 87.319 38.992 76.988 1.00 84.15 ? 577 LEU A CD1 1 ATOM 1540 C CD2 . LEU A 1 194 ? 87.122 40.978 75.484 1.00 85.72 ? 577 LEU A CD2 1 ATOM 1541 N N . GLN A 1 195 ? 91.391 40.302 78.455 1.00 82.28 ? 578 GLN A N 1 ATOM 1542 C CA . GLN A 1 195 ? 92.635 39.546 78.319 1.00 82.17 ? 578 GLN A CA 1 ATOM 1543 C C . GLN A 1 195 ? 92.881 38.632 79.521 1.00 81.07 ? 578 GLN A C 1 ATOM 1544 O O . GLN A 1 195 ? 93.307 37.491 79.345 1.00 79.91 ? 578 GLN A O 1 ATOM 1545 C CB . GLN A 1 195 ? 93.831 40.487 78.112 1.00 84.61 ? 578 GLN A CB 1 ATOM 1546 C CG . GLN A 1 195 ? 94.083 40.868 76.657 1.00 84.93 ? 578 GLN A CG 1 ATOM 1547 C CD . GLN A 1 195 ? 94.872 42.152 76.492 1.00 86.02 ? 578 GLN A CD 1 ATOM 1548 O OE1 . GLN A 1 195 ? 95.350 42.740 77.465 1.00 85.34 ? 578 GLN A OE1 1 ATOM 1549 N NE2 . GLN A 1 195 ? 95.037 42.579 75.246 1.00 86.97 ? 578 GLN A NE2 1 ATOM 1550 N N . ARG A 1 196 ? 92.615 39.135 80.728 1.00 80.37 ? 579 ARG A N 1 ATOM 1551 C CA . ARG A 1 196 ? 92.710 38.323 81.949 1.00 80.96 ? 579 ARG A CA 1 ATOM 1552 C C . ARG A 1 196 ? 91.718 37.152 81.919 1.00 76.48 ? 579 ARG A C 1 ATOM 1553 O O . ARG A 1 196 ? 92.078 36.024 82.249 1.00 74.44 ? 579 ARG A O 1 ATOM 1554 C CB . ARG A 1 196 ? 92.500 39.178 83.209 1.00 83.69 ? 579 ARG A CB 1 ATOM 1555 C CG . ARG A 1 196 ? 93.629 40.171 83.479 1.00 88.21 ? 579 ARG A CG 1 ATOM 1556 C CD . ARG A 1 196 ? 93.309 41.162 84.603 1.00 91.25 ? 579 ARG A CD 1 ATOM 1557 N NE . ARG A 1 196 ? 93.216 40.516 85.927 1.00 93.75 ? 579 ARG A NE 1 ATOM 1558 C CZ . ARG A 1 196 ? 92.093 40.254 86.620 1.00 94.08 ? 579 ARG A CZ 1 ATOM 1559 N NH1 . ARG A 1 196 ? 90.869 40.579 86.168 1.00 93.51 ? 579 ARG A NH1 1 ATOM 1560 N NH2 . ARG A 1 196 ? 92.195 39.652 87.807 1.00 93.59 ? 579 ARG A NH2 1 ATOM 1561 N N . ALA A 1 197 ? 90.483 37.418 81.502 1.00 72.76 ? 580 ALA A N 1 ATOM 1562 C CA . ALA A 1 197 ? 89.463 36.366 81.397 1.00 70.92 ? 580 ALA A CA 1 ATOM 1563 C C . ALA A 1 197 ? 89.840 35.303 80.369 1.00 69.88 ? 580 ALA A C 1 ATOM 1564 O O . ALA A 1 197 ? 89.613 34.117 80.592 1.00 69.11 ? 580 ALA A O 1 ATOM 1565 C CB . ALA A 1 197 ? 88.107 36.964 81.059 1.00 69.74 ? 580 ALA A CB 1 ATOM 1566 N N . GLN A 1 198 ? 90.405 35.744 79.249 1.00 70.43 ? 581 GLN A N 1 ATOM 1567 C CA . GLN A 1 198 ? 90.881 34.843 78.199 1.00 70.75 ? 581 GLN A CA 1 ATOM 1568 C C . GLN A 1 198 ? 92.078 34.010 78.644 1.00 69.59 ? 581 GLN A C 1 ATOM 1569 O O . GLN A 1 198 ? 92.231 32.875 78.209 1.00 67.40 ? 581 GLN A O 1 ATOM 1570 C CB . GLN A 1 198 ? 91.211 35.618 76.921 1.00 72.49 ? 581 GLN A CB 1 ATOM 1571 C CG . GLN A 1 198 ? 89.968 36.115 76.201 1.00 74.92 ? 581 GLN A CG 1 ATOM 1572 C CD . GLN A 1 198 ? 90.267 36.845 74.903 1.00 78.42 ? 581 GLN A CD 1 ATOM 1573 O OE1 . GLN A 1 198 ? 91.371 37.351 74.682 1.00 81.38 ? 581 GLN A OE1 1 ATOM 1574 N NE2 . GLN A 1 198 ? 89.269 36.909 74.033 1.00 78.73 ? 581 GLN A NE2 1 ATOM 1575 N N . ALA A 1 199 ? 92.921 34.577 79.503 1.00 70.08 ? 582 ALA A N 1 ATOM 1576 C CA . ALA A 1 199 ? 94.021 33.826 80.110 1.00 69.29 ? 582 ALA A CA 1 ATOM 1577 C C . ALA A 1 199 ? 93.467 32.704 80.985 1.00 68.99 ? 582 ALA A C 1 ATOM 1578 O O . ALA A 1 199 ? 93.962 31.579 80.927 1.00 69.71 ? 582 ALA A O 1 ATOM 1579 C CB . ALA A 1 199 ? 94.925 34.743 80.919 1.00 69.42 ? 582 ALA A CB 1 ATOM 1580 N N . TRP A 1 200 ? 92.434 33.016 81.778 1.00 68.00 ? 583 TRP A N 1 ATOM 1581 C CA . TRP A 1 200 ? 91.757 32.014 82.600 1.00 66.55 ? 583 TRP A CA 1 ATOM 1582 C C . TRP A 1 200 ? 91.132 30.924 81.738 1.00 66.59 ? 583 TRP A C 1 ATOM 1583 O O . TRP A 1 200 ? 91.277 29.744 82.042 1.00 65.69 ? 583 TRP A O 1 ATOM 1584 C CB . TRP A 1 200 ? 90.685 32.643 83.510 1.00 65.46 ? 583 TRP A CB 1 ATOM 1585 C CG . TRP A 1 200 ? 90.133 31.642 84.499 1.00 64.91 ? 583 TRP A CG 1 ATOM 1586 C CD1 . TRP A 1 200 ? 90.615 31.369 85.750 1.00 64.68 ? 583 TRP A CD1 1 ATOM 1587 C CD2 . TRP A 1 200 ? 89.030 30.745 84.292 1.00 62.86 ? 583 TRP A CD2 1 ATOM 1588 N NE1 . TRP A 1 200 ? 89.878 30.363 86.334 1.00 63.88 ? 583 TRP A NE1 1 ATOM 1589 C CE2 . TRP A 1 200 ? 88.899 29.963 85.462 1.00 62.24 ? 583 TRP A CE2 1 ATOM 1590 C CE3 . TRP A 1 200 ? 88.138 30.533 83.234 1.00 61.73 ? 583 TRP A CE3 1 ATOM 1591 C CZ2 . TRP A 1 200 ? 87.905 28.997 85.610 1.00 61.56 ? 583 TRP A CZ2 1 ATOM 1592 C CZ3 . TRP A 1 200 ? 87.156 29.564 83.377 1.00 61.49 ? 583 TRP A CZ3 1 ATOM 1593 C CH2 . TRP A 1 200 ? 87.047 28.808 84.558 1.00 61.76 ? 583 TRP A CH2 1 ATOM 1594 N N . GLU A 1 201 ? 90.456 31.320 80.660 1.00 68.74 ? 584 GLU A N 1 ATOM 1595 C CA . GLU A 1 201 ? 89.809 30.366 79.757 1.00 72.40 ? 584 GLU A CA 1 ATOM 1596 C C . GLU A 1 201 ? 90.811 29.382 79.156 1.00 71.38 ? 584 GLU A C 1 ATOM 1597 O O . GLU A 1 201 ? 90.490 28.214 78.968 1.00 71.68 ? 584 GLU A O 1 ATOM 1598 C CB . GLU A 1 201 ? 89.038 31.080 78.634 1.00 77.45 ? 584 GLU A CB 1 ATOM 1599 C CG . GLU A 1 201 ? 88.133 30.152 77.814 1.00 83.51 ? 584 GLU A CG 1 ATOM 1600 C CD . GLU A 1 201 ? 87.433 30.826 76.632 1.00 88.87 ? 584 GLU A CD 1 ATOM 1601 O OE1 . GLU A 1 201 ? 87.298 32.075 76.626 1.00 95.29 ? 584 GLU A OE1 1 ATOM 1602 O OE2 . GLU A 1 201 ? 86.997 30.095 75.708 1.00 88.58 ? 584 GLU A OE2 1 ATOM 1603 N N . LYS A 1 202 ? 92.008 29.860 78.834 1.00 71.99 ? 585 LYS A N 1 ATOM 1604 C CA . LYS A 1 202 ? 93.055 28.990 78.303 1.00 72.38 ? 585 LYS A CA 1 ATOM 1605 C C . LYS A 1 202 ? 93.462 27.938 79.319 1.00 69.46 ? 585 LYS A C 1 ATOM 1606 O O . LYS A 1 202 ? 93.624 26.788 78.958 1.00 68.89 ? 585 LYS A O 1 ATOM 1607 C CB . LYS A 1 202 ? 94.274 29.795 77.857 1.00 75.62 ? 585 LYS A CB 1 ATOM 1608 C CG . LYS A 1 202 ? 95.249 29.103 76.907 1.00 79.65 ? 585 LYS A CG 1 ATOM 1609 C CD . LYS A 1 202 ? 96.494 29.924 76.663 1.00 83.96 ? 585 LYS A CD 1 ATOM 1610 C CE . LYS A 1 202 ? 97.609 29.139 75.986 1.00 87.81 ? 585 LYS A CE 1 ATOM 1611 N NZ . LYS A 1 202 ? 98.787 30.019 75.749 1.00 89.66 ? 585 LYS A NZ 1 ATOM 1612 N N . GLU A 1 203 ? 93.606 28.329 80.582 1.00 67.97 ? 586 GLU A N 1 ATOM 1613 C CA . GLU A 1 203 ? 93.867 27.362 81.653 1.00 68.78 ? 586 GLU A CA 1 ATOM 1614 C C . GLU A 1 203 ? 92.711 26.378 81.859 1.00 66.17 ? 586 GLU A C 1 ATOM 1615 O O . GLU A 1 203 ? 92.948 25.189 82.089 1.00 65.76 ? 586 GLU A O 1 ATOM 1616 C CB . GLU A 1 203 ? 94.193 28.065 82.979 1.00 70.09 ? 586 GLU A CB 1 ATOM 1617 C CG . GLU A 1 203 ? 95.579 28.687 83.021 1.00 74.09 ? 586 GLU A CG 1 ATOM 1618 C CD . GLU A 1 203 ? 96.685 27.676 82.780 1.00 77.53 ? 586 GLU A CD 1 ATOM 1619 O OE1 . GLU A 1 203 ? 96.705 26.630 83.471 1.00 80.40 ? 586 GLU A OE1 1 ATOM 1620 O OE2 . GLU A 1 203 ? 97.524 27.919 81.883 1.00 80.21 ? 586 GLU A OE2 1 ATOM 1621 N N . PHE A 1 204 ? 91.477 26.880 81.778 1.00 62.05 ? 587 PHE A N 1 ATOM 1622 C CA . PHE A 1 204 ? 90.274 26.045 81.874 1.00 58.88 ? 587 PHE A CA 1 ATOM 1623 C C . PHE A 1 204 ? 90.244 24.970 80.787 1.00 57.25 ? 587 PHE A C 1 ATOM 1624 O O . PHE A 1 204 ? 89.980 23.814 81.069 1.00 55.78 ? 587 PHE A O 1 ATOM 1625 C CB . PHE A 1 204 ? 89.009 26.912 81.814 1.00 56.93 ? 587 PHE A CB 1 ATOM 1626 C CG . PHE A 1 204 ? 87.742 26.129 81.666 1.00 55.55 ? 587 PHE A CG 1 ATOM 1627 C CD1 . PHE A 1 204 ? 87.245 25.389 82.725 1.00 55.60 ? 587 PHE A CD1 1 ATOM 1628 C CD2 . PHE A 1 204 ? 87.042 26.130 80.465 1.00 55.50 ? 587 PHE A CD2 1 ATOM 1629 C CE1 . PHE A 1 204 ? 86.069 24.663 82.594 1.00 55.48 ? 587 PHE A CE1 1 ATOM 1630 C CE2 . PHE A 1 204 ? 85.874 25.399 80.320 1.00 54.73 ? 587 PHE A CE2 1 ATOM 1631 C CZ . PHE A 1 204 ? 85.384 24.669 81.389 1.00 55.56 ? 587 PHE A CZ 1 ATOM 1632 N N . ILE A 1 205 ? 90.540 25.361 79.558 1.00 57.40 ? 588 ILE A N 1 ATOM 1633 C CA . ILE A 1 205 ? 90.575 24.424 78.447 1.00 59.51 ? 588 ILE A CA 1 ATOM 1634 C C . ILE A 1 205 ? 91.644 23.347 78.681 1.00 61.57 ? 588 ILE A C 1 ATOM 1635 O O . ILE A 1 205 ? 91.398 22.160 78.452 1.00 59.76 ? 588 ILE A O 1 ATOM 1636 C CB . ILE A 1 205 ? 90.787 25.155 77.099 1.00 60.45 ? 588 ILE A CB 1 ATOM 1637 C CG1 . ILE A 1 205 ? 89.551 26.005 76.769 1.00 60.20 ? 588 ILE A CG1 1 ATOM 1638 C CG2 . ILE A 1 205 ? 91.030 24.156 75.968 1.00 61.09 ? 588 ILE A CG2 1 ATOM 1639 C CD1 . ILE A 1 205 ? 89.803 27.112 75.772 1.00 60.31 ? 588 ILE A CD1 1 ATOM 1640 N N . ASN A 1 206 ? 92.815 23.777 79.145 1.00 65.42 ? 589 ASN A N 1 ATOM 1641 C CA . ASN A 1 206 ? 93.911 22.861 79.486 1.00 68.55 ? 589 ASN A CA 1 ATOM 1642 C C . ASN A 1 206 ? 93.566 21.899 80.589 1.00 67.03 ? 589 ASN A C 1 ATOM 1643 O O . ASN A 1 206 ? 93.874 20.709 80.492 1.00 68.32 ? 589 ASN A O 1 ATOM 1644 C CB . ASN A 1 206 ? 95.179 23.622 79.877 1.00 71.40 ? 589 ASN A CB 1 ATOM 1645 C CG . ASN A 1 206 ? 96.036 23.909 78.666 1.00 74.44 ? 589 ASN A CG 1 ATOM 1646 O OD1 . ASN A 1 206 ? 97.032 23.222 78.432 1.00 77.48 ? 589 ASN A OD1 1 ATOM 1647 N ND2 . ASN A 1 206 ? 95.584 24.830 77.820 1.00 75.60 ? 589 ASN A ND2 1 ATOM 1648 N N . PHE A 1 207 ? 92.952 22.425 81.639 1.00 64.67 ? 590 PHE A N 1 ATOM 1649 C CA . PHE A 1 207 ? 92.540 21.607 82.758 1.00 64.58 ? 590 PHE A CA 1 ATOM 1650 C C . PHE A 1 207 ? 91.589 20.496 82.302 1.00 64.29 ? 590 PHE A C 1 ATOM 1651 O O . PHE A 1 207 ? 91.791 19.328 82.639 1.00 67.31 ? 590 PHE A O 1 ATOM 1652 C CB . PHE A 1 207 ? 91.890 22.462 83.847 1.00 63.76 ? 590 PHE A CB 1 ATOM 1653 C CG . PHE A 1 207 ? 91.541 21.684 85.066 1.00 63.91 ? 590 PHE A CG 1 ATOM 1654 C CD1 . PHE A 1 207 ? 92.482 21.491 86.066 1.00 65.25 ? 590 PHE A CD1 1 ATOM 1655 C CD2 . PHE A 1 207 ? 90.296 21.092 85.190 1.00 63.58 ? 590 PHE A CD2 1 ATOM 1656 C CE1 . PHE A 1 207 ? 92.179 20.741 87.186 1.00 66.25 ? 590 PHE A CE1 1 ATOM 1657 C CE2 . PHE A 1 207 ? 89.984 20.341 86.307 1.00 65.07 ? 590 PHE A CE2 1 ATOM 1658 C CZ . PHE A 1 207 ? 90.927 20.166 87.310 1.00 66.02 ? 590 PHE A CZ 1 ATOM 1659 N N . VAL A 1 208 ? 90.582 20.858 81.515 1.00 62.64 ? 591 VAL A N 1 ATOM 1660 C CA . VAL A 1 208 ? 89.585 19.897 81.046 1.00 62.11 ? 591 VAL A CA 1 ATOM 1661 C C . VAL A 1 208 ? 90.208 18.872 80.111 1.00 62.37 ? 591 VAL A C 1 ATOM 1662 O O . VAL A 1 208 ? 89.945 17.687 80.231 1.00 63.63 ? 591 VAL A O 1 ATOM 1663 C CB . VAL A 1 208 ? 88.393 20.606 80.363 1.00 61.20 ? 591 VAL A CB 1 ATOM 1664 C CG1 . VAL A 1 208 ? 87.462 19.613 79.677 1.00 60.64 ? 591 VAL A CG1 1 ATOM 1665 C CG2 . VAL A 1 208 ? 87.616 21.420 81.390 1.00 61.08 ? 591 VAL A CG2 1 ATOM 1666 N N . LYS A 1 209 ? 91.043 19.330 79.194 1.00 63.74 ? 592 LYS A N 1 ATOM 1667 C CA . LYS A 1 209 ? 91.727 18.443 78.250 1.00 65.23 ? 592 LYS A CA 1 ATOM 1668 C C . LYS A 1 209 ? 92.588 17.378 78.906 1.00 65.78 ? 592 LYS A C 1 ATOM 1669 O O . LYS A 1 209 ? 92.630 16.251 78.434 1.00 66.60 ? 592 LYS A O 1 ATOM 1670 C CB . LYS A 1 209 ? 92.607 19.294 77.329 1.00 66.52 ? 592 LYS A CB 1 ATOM 1671 C CG . LYS A 1 209 ? 93.366 18.575 76.220 1.00 69.40 ? 592 LYS A CG 1 ATOM 1672 C CD . LYS A 1 209 ? 93.994 19.541 75.248 1.00 70.30 ? 592 LYS A CD 1 ATOM 1673 C CE . LYS A 1 209 ? 95.418 19.917 75.586 1.00 71.68 ? 592 LYS A CE 1 ATOM 1674 N NZ . LYS A 1 209 ? 95.785 21.176 74.875 1.00 72.20 ? 592 LYS A NZ 1 ATOM 1675 N N . ASN A 1 210 ? 93.276 17.752 79.978 1.00 65.93 ? 593 ASN A N 1 ATOM 1676 C CA . ASN A 1 210 ? 94.158 16.845 80.702 1.00 67.79 ? 593 ASN A CA 1 ATOM 1677 C C . ASN A 1 210 ? 93.520 16.145 81.909 1.00 67.27 ? 593 ASN A C 1 ATOM 1678 O O . ASN A 1 210 ? 94.201 15.384 82.585 1.00 69.55 ? 593 ASN A O 1 ATOM 1679 C CB . ASN A 1 210 ? 95.408 17.613 81.164 1.00 70.25 ? 593 ASN A CB 1 ATOM 1680 C CG . ASN A 1 210 ? 96.202 18.193 80.001 1.00 70.85 ? 593 ASN A CG 1 ATOM 1681 O OD1 . ASN A 1 210 ? 96.553 17.478 79.057 1.00 70.05 ? 593 ASN A OD1 1 ATOM 1682 N ND2 . ASN A 1 210 ? 96.485 19.496 80.061 1.00 71.42 ? 593 ASN A ND2 1 ATOM 1683 N N . TYR A 1 211 ? 92.239 16.380 82.191 1.00 66.07 ? 594 TYR A N 1 ATOM 1684 C CA . TYR A 1 211 ? 91.603 15.776 83.369 1.00 65.58 ? 594 TYR A CA 1 ATOM 1685 C C . TYR A 1 211 ? 91.441 14.283 83.150 1.00 67.04 ? 594 TYR A C 1 ATOM 1686 O O . TYR A 1 211 ? 90.904 13.866 82.123 1.00 66.60 ? 594 TYR A O 1 ATOM 1687 C CB . TYR A 1 211 ? 90.240 16.410 83.654 1.00 63.97 ? 594 TYR A CB 1 ATOM 1688 C CG . TYR A 1 211 ? 89.689 16.115 85.035 1.00 61.65 ? 594 TYR A CG 1 ATOM 1689 C CD1 . TYR A 1 211 ? 88.738 15.117 85.232 1.00 61.72 ? 594 TYR A CD1 1 ATOM 1690 C CD2 . TYR A 1 211 ? 90.108 16.847 86.138 1.00 61.32 ? 594 TYR A CD2 1 ATOM 1691 C CE1 . TYR A 1 211 ? 88.219 14.854 86.492 1.00 62.11 ? 594 TYR A CE1 1 ATOM 1692 C CE2 . TYR A 1 211 ? 89.597 16.597 87.404 1.00 62.25 ? 594 TYR A CE2 1 ATOM 1693 C CZ . TYR A 1 211 ? 88.652 15.600 87.580 1.00 62.62 ? 594 TYR A CZ 1 ATOM 1694 O OH . TYR A 1 211 ? 88.145 15.343 88.841 1.00 62.96 ? 594 TYR A OH 1 ATOM 1695 N N . LYS A 1 212 ? 91.937 13.493 84.102 1.00 70.87 ? 595 LYS A N 1 ATOM 1696 C CA . LYS A 1 212 ? 91.939 12.030 84.005 1.00 74.13 ? 595 LYS A CA 1 ATOM 1697 C C . LYS A 1 212 ? 90.891 11.462 84.945 1.00 71.68 ? 595 LYS A C 1 ATOM 1698 O O . LYS A 1 212 ? 90.998 11.604 86.168 1.00 70.72 ? 595 LYS A O 1 ATOM 1699 C CB . LYS A 1 212 ? 93.300 11.431 84.400 1.00 79.25 ? 595 LYS A CB 1 ATOM 1700 C CG . LYS A 1 212 ? 94.528 11.980 83.686 1.00 82.62 ? 595 LYS A CG 1 ATOM 1701 C CD . LYS A 1 212 ? 95.137 10.975 82.706 1.00 87.56 ? 595 LYS A CD 1 ATOM 1702 C CE . LYS A 1 212 ? 95.828 9.840 83.483 1.00 90.21 ? 595 LYS A CE 1 ATOM 1703 N NZ . LYS A 1 212 ? 96.651 8.936 82.634 1.00 91.31 ? 595 LYS A NZ 1 ATOM 1704 N N . ASN A 1 213 ? 89.874 10.840 84.366 1.00 70.28 ? 596 ASN A N 1 ATOM 1705 C CA . ASN A 1 213 ? 88.952 10.010 85.117 1.00 71.08 ? 596 ASN A CA 1 ATOM 1706 C C . ASN A 1 213 ? 88.291 9.048 84.139 1.00 73.92 ? 596 ASN A C 1 ATOM 1707 O O . ASN A 1 213 ? 87.508 9.476 83.301 1.00 74.12 ? 596 ASN A O 1 ATOM 1708 C CB . ASN A 1 213 ? 87.902 10.845 85.855 1.00 68.62 ? 596 ASN A CB 1 ATOM 1709 C CG . ASN A 1 213 ? 87.050 10.010 86.799 1.00 68.09 ? 596 ASN A CG 1 ATOM 1710 O OD1 . ASN A 1 213 ? 86.882 8.808 86.598 1.00 70.52 ? 596 ASN A OD1 1 ATOM 1711 N ND2 . ASN A 1 213 ? 86.510 10.639 87.832 1.00 65.91 ? 596 ASN A ND2 1 ATOM 1712 N N . PRO A 1 214 ? 88.608 7.742 84.241 1.00 78.74 ? 597 PRO A N 1 ATOM 1713 C CA . PRO A 1 214 ? 87.959 6.761 83.364 1.00 80.43 ? 597 PRO A CA 1 ATOM 1714 C C . PRO A 1 214 ? 86.430 6.711 83.492 1.00 80.27 ? 597 PRO A C 1 ATOM 1715 O O . PRO A 1 214 ? 85.758 6.343 82.529 1.00 81.37 ? 597 PRO A O 1 ATOM 1716 C CB . PRO A 1 214 ? 88.558 5.416 83.796 1.00 82.08 ? 597 PRO A CB 1 ATOM 1717 C CG . PRO A 1 214 ? 89.653 5.710 84.750 1.00 82.46 ? 597 PRO A CG 1 ATOM 1718 C CD . PRO A 1 214 ? 89.537 7.122 85.205 1.00 80.38 ? 597 PRO A CD 1 ATOM 1719 N N . ASN A 1 215 ? 85.899 7.086 84.658 1.00 79.45 ? 598 ASN A N 1 ATOM 1720 C CA . ASN A 1 215 ? 84.453 7.066 84.904 1.00 78.77 ? 598 ASN A CA 1 ATOM 1721 C C . ASN A 1 215 ? 83.648 8.173 84.207 1.00 75.50 ? 598 ASN A C 1 ATOM 1722 O O . ASN A 1 215 ? 82.428 8.086 84.159 1.00 73.77 ? 598 ASN A O 1 ATOM 1723 C CB . ASN A 1 215 ? 84.171 7.177 86.402 1.00 81.24 ? 598 ASN A CB 1 ATOM 1724 C CG . ASN A 1 215 ? 84.773 6.042 87.212 1.00 85.42 ? 598 ASN A CG 1 ATOM 1725 O OD1 . ASN A 1 215 ? 84.735 4.879 86.800 1.00 86.79 ? 598 ASN A OD1 1 ATOM 1726 N ND2 . ASN A 1 215 ? 85.328 6.383 88.378 1.00 89.80 ? 598 ASN A ND2 1 ATOM 1727 N N . LEU A 1 216 ? 84.309 9.223 83.719 1.00 73.54 ? 599 LEU A N 1 ATOM 1728 C CA . LEU A 1 216 ? 83.624 10.369 83.118 1.00 71.61 ? 599 LEU A CA 1 ATOM 1729 C C . LEU A 1 216 ? 84.151 10.641 81.728 1.00 70.94 ? 599 LEU A C 1 ATOM 1730 O O . LEU A 1 216 ? 85.362 10.617 81.526 1.00 75.88 ? 599 LEU A O 1 ATOM 1731 C CB . LEU A 1 216 ? 83.846 11.631 83.960 1.00 69.85 ? 599 LEU A CB 1 ATOM 1732 C CG . LEU A 1 216 ? 83.573 11.567 85.462 1.00 69.46 ? 599 LEU A CG 1 ATOM 1733 C CD1 . LEU A 1 216 ? 84.045 12.845 86.141 1.00 69.05 ? 599 LEU A CD1 1 ATOM 1734 C CD2 . LEU A 1 216 ? 82.105 11.332 85.738 1.00 69.52 ? 599 LEU A CD2 1 ATOM 1735 N N . THR A 1 217 ? 83.261 10.909 80.776 1.00 68.29 ? 600 THR A N 1 ATOM 1736 C CA . THR A 1 217 ? 83.669 11.560 79.532 1.00 68.75 ? 600 THR A CA 1 ATOM 1737 C C . THR A 1 217 ? 83.202 13.019 79.609 1.00 67.14 ? 600 THR A C 1 ATOM 1738 O O . THR A 1 217 ? 82.009 13.294 79.726 1.00 66.50 ? 600 THR A O 1 ATOM 1739 C CB . THR A 1 217 ? 83.148 10.841 78.272 1.00 69.38 ? 600 THR A CB 1 ATOM 1740 O OG1 . THR A 1 217 ? 81.740 10.639 78.368 1.00 70.87 ? 600 THR A OG1 1 ATOM 1741 C CG2 . THR A 1 217 ? 83.822 9.481 78.110 1.00 71.55 ? 600 THR A CG2 1 ATOM 1742 N N . ILE A 1 218 ? 84.166 13.936 79.561 1.00 65.54 ? 601 ILE A N 1 ATOM 1743 C CA . ILE A 1 218 ? 83.937 15.369 79.671 1.00 63.67 ? 601 ILE A CA 1 ATOM 1744 C C . ILE A 1 218 ? 84.139 16.014 78.301 1.00 63.79 ? 601 ILE A C 1 ATOM 1745 O O . ILE A 1 218 ? 85.179 15.826 77.689 1.00 67.11 ? 601 ILE A O 1 ATOM 1746 C CB . ILE A 1 218 ? 84.940 15.999 80.655 1.00 63.16 ? 601 ILE A CB 1 ATOM 1747 C CG1 . ILE A 1 218 ? 84.840 15.322 82.028 1.00 62.02 ? 601 ILE A CG1 1 ATOM 1748 C CG2 . ILE A 1 218 ? 84.694 17.504 80.778 1.00 63.26 ? 601 ILE A CG2 1 ATOM 1749 C CD1 . ILE A 1 218 ? 85.982 15.646 82.962 1.00 62.03 ? 601 ILE A CD1 1 ATOM 1750 N N . SER A 1 219 ? 83.147 16.767 77.825 1.00 63.12 ? 602 SER A N 1 ATOM 1751 C CA . SER A 1 219 ? 83.230 17.461 76.535 1.00 62.14 ? 602 SER A CA 1 ATOM 1752 C C . SER A 1 219 ? 82.835 18.919 76.662 1.00 61.64 ? 602 SER A C 1 ATOM 1753 O O . SER A 1 219 ? 82.025 19.268 77.500 1.00 61.44 ? 602 SER A O 1 ATOM 1754 C CB . SER A 1 219 ? 82.292 16.809 75.528 1.00 62.05 ? 602 SER A CB 1 ATOM 1755 O OG . SER A 1 219 ? 82.475 15.418 75.513 1.00 64.73 ? 602 SER A OG 1 ATOM 1756 N N . PHE A 1 220 ? 83.390 19.753 75.796 1.00 61.90 ? 603 PHE A N 1 ATOM 1757 C CA . PHE A 1 220 ? 82.890 21.106 75.588 1.00 62.84 ? 603 PHE A CA 1 ATOM 1758 C C . PHE A 1 220 ? 81.650 21.031 74.713 1.00 63.04 ? 603 PHE A C 1 ATOM 1759 O O . PHE A 1 220 ? 81.559 20.178 73.846 1.00 63.49 ? 603 PHE A O 1 ATOM 1760 C CB . PHE A 1 220 ? 83.954 21.977 74.906 1.00 63.92 ? 603 PHE A CB 1 ATOM 1761 C CG . PHE A 1 220 ? 85.247 22.034 75.657 1.00 63.12 ? 603 PHE A CG 1 ATOM 1762 C CD1 . PHE A 1 220 ? 86.341 21.282 75.245 1.00 64.01 ? 603 PHE A CD1 1 ATOM 1763 C CD2 . PHE A 1 220 ? 85.354 22.792 76.804 1.00 62.70 ? 603 PHE A CD2 1 ATOM 1764 C CE1 . PHE A 1 220 ? 87.529 21.310 75.951 1.00 65.10 ? 603 PHE A CE1 1 ATOM 1765 C CE2 . PHE A 1 220 ? 86.543 22.832 77.517 1.00 64.30 ? 603 PHE A CE2 1 ATOM 1766 C CZ . PHE A 1 220 ? 87.632 22.088 77.091 1.00 65.10 ? 603 PHE A CZ 1 ATOM 1767 N N . THR A 1 221 ? 80.699 21.925 74.935 1.00 65.50 ? 604 THR A N 1 ATOM 1768 C CA . THR A 1 221 ? 79.486 21.966 74.122 1.00 69.35 ? 604 THR A CA 1 ATOM 1769 C C . THR A 1 221 ? 79.684 22.816 72.884 1.00 73.48 ? 604 THR A C 1 ATOM 1770 O O . THR A 1 221 ? 80.486 23.757 72.899 1.00 70.07 ? 604 THR A O 1 ATOM 1771 C CB . THR A 1 221 ? 78.304 22.532 74.913 1.00 69.29 ? 604 THR A CB 1 ATOM 1772 O OG1 . THR A 1 221 ? 78.656 23.822 75.427 1.00 69.15 ? 604 THR A OG1 1 ATOM 1773 C CG2 . THR A 1 221 ? 77.973 21.605 76.049 1.00 68.66 ? 604 THR A CG2 1 ATOM 1774 N N . ALA A 1 222 ? 78.954 22.448 71.823 1.00 82.06 ? 605 ALA A N 1 ATOM 1775 C CA . ALA A 1 222 ? 78.969 23.142 70.532 1.00 89.54 ? 605 ALA A CA 1 ATOM 1776 C C . ALA A 1 222 ? 78.097 24.406 70.561 1.00 94.04 ? 605 ALA A C 1 ATOM 1777 O O . ALA A 1 222 ? 76.872 24.336 70.695 1.00 95.68 ? 605 ALA A O 1 ATOM 1778 C CB . ALA A 1 222 ? 78.516 22.194 69.415 1.00 90.49 ? 605 ALA A CB 1 ATOM 1779 N N . GLU A 1 223 ? 78.749 25.558 70.419 1.00 98.83 ? 606 GLU A N 1 ATOM 1780 C CA . GLU A 1 223 ? 78.086 26.864 70.403 1.00 102.22 ? 606 GLU A CA 1 ATOM 1781 C C . GLU A 1 223 ? 77.432 27.143 69.044 1.00 102.66 ? 606 GLU A C 1 ATOM 1782 O O . GLU A 1 223 ? 76.968 26.230 68.350 1.00 102.03 ? 606 GLU A O 1 ATOM 1783 C CB . GLU A 1 223 ? 79.115 27.953 70.751 1.00 104.85 ? 606 GLU A CB 1 ATOM 1784 C CG . GLU A 1 223 ? 78.566 29.364 70.906 1.00 107.91 ? 606 GLU A CG 1 ATOM 1785 C CD . GLU A 1 223 ? 78.898 30.278 69.737 1.00 110.51 ? 606 GLU A CD 1 ATOM 1786 O OE1 . GLU A 1 223 ? 79.544 31.321 69.979 1.00 111.65 ? 606 GLU A OE1 1 ATOM 1787 O OE2 . GLU A 1 223 ? 78.524 29.965 68.585 1.00 112.21 ? 606 GLU A OE2 1 ATOM 1788 N N . GLU B 1 8 ? 68.350 39.264 76.308 1.00 137.08 ? 391 GLU B N 1 ATOM 1789 C CA . GLU B 1 8 ? 67.396 40.394 76.068 1.00 139.97 ? 391 GLU B CA 1 ATOM 1790 C C . GLU B 1 8 ? 66.185 40.040 75.184 1.00 143.40 ? 391 GLU B C 1 ATOM 1791 O O . GLU B 1 8 ? 65.128 40.663 75.328 1.00 145.67 ? 391 GLU B O 1 ATOM 1792 C CB . GLU B 1 8 ? 68.125 41.606 75.466 1.00 140.01 ? 391 GLU B CB 1 ATOM 1793 C CG . GLU B 1 8 ? 69.158 42.247 76.388 1.00 139.06 ? 391 GLU B CG 1 ATOM 1794 C CD . GLU B 1 8 ? 69.168 43.772 76.312 1.00 138.23 ? 391 GLU B CD 1 ATOM 1795 O OE1 . GLU B 1 8 ? 69.308 44.305 75.190 1.00 140.44 ? 391 GLU B OE1 1 ATOM 1796 O OE2 . GLU B 1 8 ? 69.038 44.437 77.368 1.00 127.95 ? 391 GLU B OE2 1 ATOM 1797 N N . LYS B 1 9 ? 66.348 39.090 74.257 1.00 144.91 ? 392 LYS B N 1 ATOM 1798 C CA . LYS B 1 9 ? 65.259 38.619 73.379 1.00 144.19 ? 392 LYS B CA 1 ATOM 1799 C C . LYS B 1 9 ? 65.183 37.088 73.274 1.00 142.37 ? 392 LYS B C 1 ATOM 1800 O O . LYS B 1 9 ? 64.147 36.488 73.565 1.00 141.55 ? 392 LYS B O 1 ATOM 1801 C CB . LYS B 1 9 ? 65.428 39.237 71.985 1.00 143.91 ? 392 LYS B CB 1 ATOM 1802 C CG . LYS B 1 9 ? 65.018 40.700 71.928 1.00 142.28 ? 392 LYS B CG 1 ATOM 1803 C CD . LYS B 1 9 ? 65.713 41.459 70.811 1.00 141.47 ? 392 LYS B CD 1 ATOM 1804 C CE . LYS B 1 9 ? 65.571 42.962 70.999 1.00 140.28 ? 392 LYS B CE 1 ATOM 1805 N NZ . LYS B 1 9 ? 66.569 43.707 70.188 1.00 140.38 ? 392 LYS B NZ 1 ATOM 1806 N N . GLU B 1 10 ? 66.275 36.469 72.835 1.00 142.95 ? 393 GLU B N 1 ATOM 1807 C CA . GLU B 1 10 ? 66.345 35.018 72.680 1.00 140.65 ? 393 GLU B CA 1 ATOM 1808 C C . GLU B 1 10 ? 66.776 34.262 73.927 1.00 141.50 ? 393 GLU B C 1 ATOM 1809 O O . GLU B 1 10 ? 66.677 33.032 73.943 1.00 144.55 ? 393 GLU B O 1 ATOM 1810 C CB . GLU B 1 10 ? 67.365 34.682 71.602 1.00 141.79 ? 393 GLU B CB 1 ATOM 1811 C CG . GLU B 1 10 ? 67.157 35.349 70.270 1.00 141.82 ? 393 GLU B CG 1 ATOM 1812 C CD . GLU B 1 10 ? 68.064 36.534 70.003 1.00 140.22 ? 393 GLU B CD 1 ATOM 1813 O OE1 . GLU B 1 10 ? 68.466 37.239 70.948 1.00 137.79 ? 393 GLU B OE1 1 ATOM 1814 O OE2 . GLU B 1 10 ? 68.376 36.748 68.824 1.00 138.44 ? 393 GLU B OE2 1 ATOM 1815 N N . TYR B 1 11 ? 67.305 34.978 74.926 1.00 140.63 ? 394 TYR B N 1 ATOM 1816 C CA . TYR B 1 11 ? 67.643 34.393 76.245 1.00 136.20 ? 394 TYR B CA 1 ATOM 1817 C C . TYR B 1 11 ? 66.456 33.643 76.851 1.00 136.12 ? 394 TYR B C 1 ATOM 1818 O O . TYR B 1 11 ? 66.618 32.544 77.381 1.00 134.59 ? 394 TYR B O 1 ATOM 1819 C CB . TYR B 1 11 ? 68.149 35.485 77.214 1.00 131.99 ? 394 TYR B CB 1 ATOM 1820 C CG . TYR B 1 11 ? 68.577 35.031 78.616 1.00 129.14 ? 394 TYR B CG 1 ATOM 1821 C CD1 . TYR B 1 11 ? 69.928 34.845 78.947 1.00 126.38 ? 394 TYR B CD1 1 ATOM 1822 C CD2 . TYR B 1 11 ? 67.631 34.829 79.625 1.00 127.55 ? 394 TYR B CD2 1 ATOM 1823 C CE1 . TYR B 1 11 ? 70.315 34.447 80.222 1.00 121.16 ? 394 TYR B CE1 1 ATOM 1824 C CE2 . TYR B 1 11 ? 68.013 34.432 80.903 1.00 123.19 ? 394 TYR B CE2 1 ATOM 1825 C CZ . TYR B 1 11 ? 69.355 34.243 81.193 1.00 120.09 ? 394 TYR B CZ 1 ATOM 1826 O OH . TYR B 1 11 ? 69.729 33.850 82.453 1.00 115.58 ? 394 TYR B OH 1 ATOM 1827 N N . PHE B 1 12 ? 65.267 34.230 76.718 1.00 136.14 ? 395 PHE B N 1 ATOM 1828 C CA . PHE B 1 12 ? 64.052 33.716 77.352 1.00 134.51 ? 395 PHE B CA 1 ATOM 1829 C C . PHE B 1 12 ? 63.547 32.413 76.721 1.00 135.91 ? 395 PHE B C 1 ATOM 1830 O O . PHE B 1 12 ? 62.955 31.576 77.414 1.00 135.17 ? 395 PHE B O 1 ATOM 1831 C CB . PHE B 1 12 ? 62.937 34.765 77.296 1.00 131.27 ? 395 PHE B CB 1 ATOM 1832 C CG . PHE B 1 12 ? 63.309 36.088 77.900 1.00 126.76 ? 395 PHE B CG 1 ATOM 1833 C CD1 . PHE B 1 12 ? 63.290 36.270 79.276 1.00 122.94 ? 395 PHE B CD1 1 ATOM 1834 C CD2 . PHE B 1 12 ? 63.667 37.164 77.085 1.00 127.09 ? 395 PHE B CD2 1 ATOM 1835 C CE1 . PHE B 1 12 ? 63.623 37.497 79.830 1.00 123.52 ? 395 PHE B CE1 1 ATOM 1836 C CE2 . PHE B 1 12 ? 64.010 38.388 77.636 1.00 126.32 ? 395 PHE B CE2 1 ATOM 1837 C CZ . PHE B 1 12 ? 63.978 38.559 79.009 1.00 124.40 ? 395 PHE B CZ 1 ATOM 1838 N N . ASP B 1 13 ? 63.778 32.254 75.415 1.00 136.76 ? 396 ASP B N 1 ATOM 1839 C CA . ASP B 1 13 ? 63.349 31.061 74.672 1.00 137.49 ? 396 ASP B CA 1 ATOM 1840 C C . ASP B 1 13 ? 64.152 29.791 74.979 1.00 136.88 ? 396 ASP B C 1 ATOM 1841 O O . ASP B 1 13 ? 63.727 28.698 74.597 1.00 137.46 ? 396 ASP B O 1 ATOM 1842 C CB . ASP B 1 13 ? 63.427 31.303 73.164 1.00 137.83 ? 396 ASP B CB 1 ATOM 1843 C CG . ASP B 1 13 ? 62.462 32.364 72.691 1.00 137.87 ? 396 ASP B CG 1 ATOM 1844 O OD1 . ASP B 1 13 ? 61.243 32.104 72.709 1.00 136.01 ? 396 ASP B OD1 1 ATOM 1845 O OD2 . ASP B 1 13 ? 62.926 33.449 72.287 1.00 138.80 ? 396 ASP B OD2 1 ATOM 1846 N N . GLN B 1 14 ? 65.326 29.940 75.599 1.00 135.46 ? 397 GLN B N 1 ATOM 1847 C CA . GLN B 1 14 ? 66.146 28.786 76.034 1.00 137.68 ? 397 GLN B CA 1 ATOM 1848 C C . GLN B 1 14 ? 66.433 28.759 77.530 1.00 129.22 ? 397 GLN B C 1 ATOM 1849 O O . GLN B 1 14 ? 66.684 27.674 78.062 1.00 129.48 ? 397 GLN B O 1 ATOM 1850 C CB . GLN B 1 14 ? 67.475 28.700 75.255 1.00 146.83 ? 397 GLN B CB 1 ATOM 1851 C CG . GLN B 1 14 ? 68.456 27.583 75.682 1.00 152.78 ? 397 GLN B CG 1 ATOM 1852 C CD . GLN B 1 14 ? 67.946 26.153 75.494 1.00 157.60 ? 397 GLN B CD 1 ATOM 1853 O OE1 . GLN B 1 14 ? 66.915 25.914 74.867 1.00 162.03 ? 397 GLN B OE1 1 ATOM 1854 N NE2 . GLN B 1 14 ? 68.689 25.188 76.039 1.00 159.52 ? 397 GLN B NE2 1 ATOM 1855 N N . HIS B 1 15 ? 66.462 29.914 78.204 1.00 118.38 ? 398 HIS B N 1 ATOM 1856 C CA . HIS B 1 15 ? 66.447 29.891 79.664 1.00 109.06 ? 398 HIS B CA 1 ATOM 1857 C C . HIS B 1 15 ? 65.173 29.198 80.158 1.00 96.62 ? 398 HIS B C 1 ATOM 1858 O O . HIS B 1 15 ? 65.283 28.316 81.011 1.00 90.24 ? 398 HIS B O 1 ATOM 1859 C CB . HIS B 1 15 ? 66.615 31.274 80.308 1.00 111.98 ? 398 HIS B CB 1 ATOM 1860 C CG . HIS B 1 15 ? 67.245 31.215 81.666 1.00 116.99 ? 398 HIS B CG 1 ATOM 1861 N ND1 . HIS B 1 15 ? 68.560 30.846 81.874 1.00 120.76 ? 398 HIS B ND1 1 ATOM 1862 C CD2 . HIS B 1 15 ? 66.726 31.453 82.892 1.00 119.20 ? 398 HIS B CD2 1 ATOM 1863 C CE1 . HIS B 1 15 ? 68.823 30.874 83.169 1.00 121.73 ? 398 HIS B CE1 1 ATOM 1864 N NE2 . HIS B 1 15 ? 67.727 31.241 83.808 1.00 122.10 ? 398 HIS B NE2 1 ATOM 1865 N N . PHE B 1 16 ? 64.000 29.565 79.609 1.00 84.64 ? 399 PHE B N 1 ATOM 1866 C CA . PHE B 1 16 ? 62.724 28.881 79.931 1.00 75.27 ? 399 PHE B CA 1 ATOM 1867 C C . PHE B 1 16 ? 62.495 27.611 79.190 1.00 70.18 ? 399 PHE B C 1 ATOM 1868 O O . PHE B 1 16 ? 61.653 26.830 79.596 1.00 71.29 ? 399 PHE B O 1 ATOM 1869 C CB . PHE B 1 16 ? 61.525 29.840 80.039 1.00 72.80 ? 399 PHE B CB 1 ATOM 1870 C CG . PHE B 1 16 ? 61.796 30.870 81.059 1.00 69.76 ? 399 PHE B CG 1 ATOM 1871 C CD1 . PHE B 1 16 ? 62.034 32.203 80.739 1.00 70.33 ? 399 PHE B CD1 1 ATOM 1872 C CD2 . PHE B 1 16 ? 62.057 30.427 82.345 1.00 67.53 ? 399 PHE B CD2 1 ATOM 1873 C CE1 . PHE B 1 16 ? 62.422 33.089 81.736 1.00 70.15 ? 399 PHE B CE1 1 ATOM 1874 C CE2 . PHE B 1 16 ? 62.447 31.293 83.335 1.00 67.66 ? 399 PHE B CE2 1 ATOM 1875 C CZ . PHE B 1 16 ? 62.630 32.629 83.033 1.00 68.89 ? 399 PHE B CZ 1 ATOM 1876 N N . GLY B 1 17 ? 63.313 27.355 78.177 1.00 66.61 ? 400 GLY B N 1 ATOM 1877 C CA . GLY B 1 17 ? 63.642 25.983 77.834 1.00 63.27 ? 400 GLY B CA 1 ATOM 1878 C C . GLY B 1 17 ? 62.506 25.339 77.089 1.00 60.85 ? 400 GLY B C 1 ATOM 1879 O O . GLY B 1 17 ? 61.587 26.020 76.666 1.00 61.72 ? 400 GLY B O 1 ATOM 1880 N N . PRO B 1 18 ? 62.547 24.019 76.949 1.00 59.55 ? 401 PRO B N 1 ATOM 1881 C CA . PRO B 1 18 ? 61.537 23.346 76.155 1.00 59.77 ? 401 PRO B CA 1 ATOM 1882 C C . PRO B 1 18 ? 60.142 23.285 76.768 1.00 58.63 ? 401 PRO B C 1 ATOM 1883 O O . PRO B 1 18 ? 59.196 23.024 76.026 1.00 63.82 ? 401 PRO B O 1 ATOM 1884 C CB . PRO B 1 18 ? 62.109 21.934 75.988 1.00 60.61 ? 401 PRO B CB 1 ATOM 1885 C CG . PRO B 1 18 ? 62.975 21.735 77.173 1.00 60.03 ? 401 PRO B CG 1 ATOM 1886 C CD . PRO B 1 18 ? 63.533 23.082 77.512 1.00 59.95 ? 401 PRO B CD 1 ATOM 1887 N N . PHE B 1 19 ? 59.992 23.498 78.077 1.00 54.84 ? 402 PHE B N 1 ATOM 1888 C CA . PHE B 1 19 ? 58.700 23.243 78.728 1.00 53.83 ? 402 PHE B CA 1 ATOM 1889 C C . PHE B 1 19 ? 57.911 24.488 79.094 1.00 52.36 ? 402 PHE B C 1 ATOM 1890 O O . PHE B 1 19 ? 56.789 24.372 79.563 1.00 52.39 ? 402 PHE B O 1 ATOM 1891 C CB . PHE B 1 19 ? 58.881 22.364 79.970 1.00 54.11 ? 402 PHE B CB 1 ATOM 1892 C CG . PHE B 1 19 ? 59.718 21.151 79.718 1.00 54.65 ? 402 PHE B CG 1 ATOM 1893 C CD1 . PHE B 1 19 ? 59.285 20.176 78.822 1.00 54.97 ? 402 PHE B CD1 1 ATOM 1894 C CD2 . PHE B 1 19 ? 60.953 20.993 80.334 1.00 53.36 ? 402 PHE B CD2 1 ATOM 1895 C CE1 . PHE B 1 19 ? 60.061 19.061 78.558 1.00 54.46 ? 402 PHE B CE1 1 ATOM 1896 C CE2 . PHE B 1 19 ? 61.729 19.876 80.073 1.00 54.30 ? 402 PHE B CE2 1 ATOM 1897 C CZ . PHE B 1 19 ? 61.286 18.914 79.180 1.00 54.43 ? 402 PHE B CZ 1 ATOM 1898 N N . PHE B 1 20 ? 58.490 25.667 78.908 1.00 51.31 ? 403 PHE B N 1 ATOM 1899 C CA . PHE B 1 20 ? 57.820 26.920 79.244 1.00 51.41 ? 403 PHE B CA 1 ATOM 1900 C C . PHE B 1 20 ? 57.973 27.891 78.090 1.00 52.67 ? 403 PHE B C 1 ATOM 1901 O O . PHE B 1 20 ? 59.014 27.917 77.435 1.00 50.37 ? 403 PHE B O 1 ATOM 1902 C CB . PHE B 1 20 ? 58.407 27.528 80.525 1.00 50.14 ? 403 PHE B CB 1 ATOM 1903 C CG . PHE B 1 20 ? 58.016 26.796 81.777 1.00 48.86 ? 403 PHE B CG 1 ATOM 1904 C CD1 . PHE B 1 20 ? 58.758 25.706 82.222 1.00 49.41 ? 403 PHE B CD1 1 ATOM 1905 C CD2 . PHE B 1 20 ? 56.910 27.192 82.514 1.00 48.36 ? 403 PHE B CD2 1 ATOM 1906 C CE1 . PHE B 1 20 ? 58.394 25.023 83.380 1.00 49.47 ? 403 PHE B CE1 1 ATOM 1907 C CE2 . PHE B 1 20 ? 56.543 26.513 83.671 1.00 49.38 ? 403 PHE B CE2 1 ATOM 1908 C CZ . PHE B 1 20 ? 57.287 25.429 84.107 1.00 48.65 ? 403 PHE B CZ 1 ATOM 1909 N N . ARG B 1 21 ? 56.915 28.650 77.825 1.00 55.92 ? 404 ARG B N 1 ATOM 1910 C CA . ARG B 1 21 ? 56.979 29.788 76.914 1.00 59.24 ? 404 ARG B CA 1 ATOM 1911 C C . ARG B 1 21 ? 56.846 31.061 77.743 1.00 57.85 ? 404 ARG B C 1 ATOM 1912 O O . ARG B 1 21 ? 56.519 30.991 78.924 1.00 57.03 ? 404 ARG B O 1 ATOM 1913 C CB . ARG B 1 21 ? 55.896 29.690 75.834 1.00 63.57 ? 404 ARG B CB 1 ATOM 1914 C CG . ARG B 1 21 ? 54.451 29.795 76.313 1.00 70.13 ? 404 ARG B CG 1 ATOM 1915 C CD . ARG B 1 21 ? 53.486 30.057 75.163 1.00 76.98 ? 404 ARG B CD 1 ATOM 1916 N NE . ARG B 1 21 ? 52.141 30.431 75.624 1.00 85.35 ? 404 ARG B NE 1 ATOM 1917 C CZ . ARG B 1 21 ? 51.236 29.595 76.169 1.00 93.00 ? 404 ARG B CZ 1 ATOM 1918 N NH1 . ARG B 1 21 ? 51.501 28.290 76.378 1.00 91.97 ? 404 ARG B NH1 1 ATOM 1919 N NH2 . ARG B 1 21 ? 50.036 30.076 76.528 1.00 95.92 ? 404 ARG B NH2 1 ATOM 1920 N N . THR B 1 22 ? 57.073 32.213 77.122 1.00 58.17 ? 405 THR B N 1 ATOM 1921 C CA . THR B 1 22 ? 56.967 33.497 77.818 1.00 58.86 ? 405 THR B CA 1 ATOM 1922 C C . THR B 1 22 ? 55.949 34.434 77.176 1.00 59.82 ? 405 THR B C 1 ATOM 1923 O O . THR B 1 22 ? 55.943 34.588 75.964 1.00 57.89 ? 405 THR B O 1 ATOM 1924 C CB . THR B 1 22 ? 58.308 34.237 77.842 1.00 58.85 ? 405 THR B CB 1 ATOM 1925 O OG1 . THR B 1 22 ? 58.730 34.535 76.509 1.00 58.51 ? 405 THR B OG1 1 ATOM 1926 C CG2 . THR B 1 22 ? 59.366 33.399 78.532 1.00 58.85 ? 405 THR B CG2 1 ATOM 1927 N N . GLU B 1 23 ? 55.059 35.001 77.997 1.00 61.13 ? 406 GLU B N 1 ATOM 1928 C CA . GLU B 1 23 ? 54.279 36.168 77.614 1.00 62.79 ? 406 GLU B CA 1 ATOM 1929 C C . GLU B 1 23 ? 55.115 37.345 78.031 1.00 60.36 ? 406 GLU B C 1 ATOM 1930 O O . GLU B 1 23 ? 55.550 37.406 79.180 1.00 60.16 ? 406 GLU B O 1 ATOM 1931 C CB . GLU B 1 23 ? 52.936 36.231 78.344 1.00 67.21 ? 406 GLU B CB 1 ATOM 1932 C CG . GLU B 1 23 ? 51.990 35.068 78.078 1.00 72.88 ? 406 GLU B CG 1 ATOM 1933 C CD . GLU B 1 23 ? 51.674 34.851 76.604 1.00 77.97 ? 406 GLU B CD 1 ATOM 1934 O OE1 . GLU B 1 23 ? 51.593 35.855 75.841 1.00 79.41 ? 406 GLU B OE1 1 ATOM 1935 O OE2 . GLU B 1 23 ? 51.507 33.659 76.227 1.00 83.40 ? 406 GLU B OE2 1 ATOM 1936 N N . GLN B 1 24 ? 55.317 38.286 77.118 1.00 58.89 ? 407 GLN B N 1 ATOM 1937 C CA . GLN B 1 24 ? 56.234 39.390 77.341 1.00 57.30 ? 407 GLN B CA 1 ATOM 1938 C C . GLN B 1 24 ? 55.701 40.747 76.846 1.00 55.10 ? 407 GLN B C 1 ATOM 1939 O O . GLN B 1 24 ? 55.196 40.863 75.725 1.00 54.86 ? 407 GLN B O 1 ATOM 1940 C CB . GLN B 1 24 ? 57.560 39.059 76.676 1.00 59.26 ? 407 GLN B CB 1 ATOM 1941 C CG . GLN B 1 24 ? 58.607 40.144 76.841 1.00 62.73 ? 407 GLN B CG 1 ATOM 1942 C CD . GLN B 1 24 ? 59.965 39.708 76.354 1.00 65.74 ? 407 GLN B CD 1 ATOM 1943 O OE1 . GLN B 1 24 ? 60.349 39.977 75.220 1.00 67.34 ? 407 GLN B OE1 1 ATOM 1944 N NE2 . GLN B 1 24 ? 60.699 39.020 77.216 1.00 66.88 ? 407 GLN B NE2 1 ATOM 1945 N N . LEU B 1 25 ? 55.836 41.766 77.694 1.00 51.97 ? 408 LEU B N 1 ATOM 1946 C CA . LEU B 1 25 ? 55.399 43.121 77.389 1.00 51.80 ? 408 LEU B CA 1 ATOM 1947 C C . LEU B 1 25 ? 56.566 44.085 77.426 1.00 51.08 ? 408 LEU B C 1 ATOM 1948 O O . LEU B 1 25 ? 57.423 43.957 78.300 1.00 50.69 ? 408 LEU B O 1 ATOM 1949 C CB . LEU B 1 25 ? 54.362 43.580 78.416 1.00 51.66 ? 408 LEU B CB 1 ATOM 1950 C CG . LEU B 1 25 ? 53.134 42.693 78.583 1.00 53.06 ? 408 LEU B CG 1 ATOM 1951 C CD1 . LEU B 1 25 ? 52.271 43.219 79.714 1.00 53.05 ? 408 LEU B CD1 1 ATOM 1952 C CD2 . LEU B 1 25 ? 52.335 42.620 77.287 1.00 54.69 ? 408 LEU B CD2 1 ATOM 1953 N N . ILE B 1 26 ? 56.609 45.034 76.488 1.00 51.40 ? 409 ILE B N 1 ATOM 1954 C CA . ILE B 1 26 ? 57.533 46.174 76.590 1.00 52.92 ? 409 ILE B CA 1 ATOM 1955 C C . ILE B 1 26 ? 56.737 47.407 76.929 1.00 52.36 ? 409 ILE B C 1 ATOM 1956 O O . ILE B 1 26 ? 55.733 47.687 76.282 1.00 52.32 ? 409 ILE B O 1 ATOM 1957 C CB . ILE B 1 26 ? 58.339 46.457 75.302 1.00 55.69 ? 409 ILE B CB 1 ATOM 1958 C CG1 . ILE B 1 26 ? 59.319 45.311 75.066 1.00 59.18 ? 409 ILE B CG1 1 ATOM 1959 C CG2 . ILE B 1 26 ? 59.123 47.769 75.400 1.00 56.43 ? 409 ILE B CG2 1 ATOM 1960 C CD1 . ILE B 1 26 ? 59.917 45.251 73.676 1.00 62.28 ? 409 ILE B CD1 1 ATOM 1961 N N . ILE B 1 27 ? 57.228 48.163 77.904 1.00 51.75 ? 410 ILE B N 1 ATOM 1962 C CA . ILE B 1 27 ? 56.511 49.296 78.461 1.00 53.33 ? 410 ILE B CA 1 ATOM 1963 C C . ILE B 1 27 ? 57.380 50.554 78.413 1.00 54.00 ? 410 ILE B C 1 ATOM 1964 O O . ILE B 1 27 ? 58.509 50.538 78.893 1.00 53.85 ? 410 ILE B O 1 ATOM 1965 C CB . ILE B 1 27 ? 56.076 48.995 79.906 1.00 53.76 ? 410 ILE B CB 1 ATOM 1966 C CG1 . ILE B 1 27 ? 55.074 47.840 79.900 1.00 54.65 ? 410 ILE B CG1 1 ATOM 1967 C CG2 . ILE B 1 27 ? 55.414 50.211 80.542 1.00 55.06 ? 410 ILE B CG2 1 ATOM 1968 C CD1 . ILE B 1 27 ? 54.759 47.296 81.270 1.00 55.89 ? 410 ILE B CD1 1 ATOM 1969 N N . ARG B 1 28 ? 56.848 51.625 77.822 1.00 54.19 ? 411 ARG B N 1 ATOM 1970 C CA . ARG B 1 28 ? 57.517 52.928 77.786 1.00 54.74 ? 411 ARG B CA 1 ATOM 1971 C C . ARG B 1 28 ? 56.619 53.976 78.404 1.00 54.21 ? 411 ARG B C 1 ATOM 1972 O O . ARG B 1 28 ? 55.410 53.770 78.500 1.00 54.40 ? 411 ARG B O 1 ATOM 1973 C CB . ARG B 1 28 ? 57.889 53.318 76.358 1.00 56.10 ? 411 ARG B CB 1 ATOM 1974 C CG . ARG B 1 28 ? 58.890 52.367 75.727 1.00 58.01 ? 411 ARG B CG 1 ATOM 1975 C CD . ARG B 1 28 ? 59.385 52.869 74.391 1.00 60.40 ? 411 ARG B CD 1 ATOM 1976 N NE . ARG B 1 28 ? 60.237 51.891 73.710 1.00 62.85 ? 411 ARG B NE 1 ATOM 1977 C CZ . ARG B 1 28 ? 59.807 50.804 73.059 1.00 64.76 ? 411 ARG B CZ 1 ATOM 1978 N NH1 . ARG B 1 28 ? 58.508 50.500 72.991 1.00 67.55 ? 411 ARG B NH1 1 ATOM 1979 N NH2 . ARG B 1 28 ? 60.687 49.994 72.473 1.00 64.61 ? 411 ARG B NH2 1 ATOM 1980 N N . ALA B 1 29 ? 57.218 55.087 78.834 1.00 53.00 ? 412 ALA B N 1 ATOM 1981 C CA . ALA B 1 29 ? 56.478 56.205 79.437 1.00 52.91 ? 412 ALA B CA 1 ATOM 1982 C C . ALA B 1 29 ? 56.618 57.503 78.600 1.00 53.35 ? 412 ALA B C 1 ATOM 1983 O O . ALA B 1 29 ? 57.440 58.364 78.923 1.00 53.48 ? 412 ALA B O 1 ATOM 1984 C CB . ALA B 1 29 ? 56.947 56.425 80.869 1.00 52.09 ? 412 ALA B CB 1 ATOM 1985 N N . PRO B 1 30 ? 55.808 57.653 77.530 1.00 53.78 ? 413 PRO B N 1 ATOM 1986 C CA . PRO B 1 30 ? 56.016 58.739 76.555 1.00 55.51 ? 413 PRO B CA 1 ATOM 1987 C C . PRO B 1 30 ? 55.753 60.168 77.058 1.00 56.88 ? 413 PRO B C 1 ATOM 1988 O O . PRO B 1 30 ? 56.309 61.115 76.503 1.00 59.82 ? 413 PRO B O 1 ATOM 1989 C CB . PRO B 1 30 ? 55.031 58.386 75.437 1.00 55.66 ? 413 PRO B CB 1 ATOM 1990 C CG . PRO B 1 30 ? 53.932 57.670 76.133 1.00 54.56 ? 413 PRO B CG 1 ATOM 1991 C CD . PRO B 1 30 ? 54.595 56.875 77.219 1.00 53.47 ? 413 PRO B CD 1 ATOM 1992 N N . LEU B 1 31 ? 54.942 60.321 78.100 1.00 57.53 ? 414 LEU B N 1 ATOM 1993 C CA . LEU B 1 31 ? 54.631 61.638 78.674 1.00 58.38 ? 414 LEU B CA 1 ATOM 1994 C C . LEU B 1 31 ? 55.456 61.969 79.921 1.00 58.40 ? 414 LEU B C 1 ATOM 1995 O O . LEU B 1 31 ? 55.086 62.874 80.664 1.00 59.79 ? 414 LEU B O 1 ATOM 1996 C CB . LEU B 1 31 ? 53.138 61.716 79.022 1.00 58.04 ? 414 LEU B CB 1 ATOM 1997 C CG . LEU B 1 31 ? 52.186 61.350 77.888 1.00 59.81 ? 414 LEU B CG 1 ATOM 1998 C CD1 . LEU B 1 31 ? 50.758 61.235 78.400 1.00 60.56 ? 414 LEU B CD1 1 ATOM 1999 C CD2 . LEU B 1 31 ? 52.291 62.363 76.759 1.00 61.79 ? 414 LEU B CD2 1 ATOM 2000 N N . THR B 1 32 ? 56.562 61.257 80.148 1.00 57.94 ? 415 THR B N 1 ATOM 2001 C CA . THR B 1 32 ? 57.370 61.426 81.355 1.00 58.79 ? 415 THR B CA 1 ATOM 2002 C C . THR B 1 32 ? 58.792 61.791 80.954 1.00 61.25 ? 415 THR B C 1 ATOM 2003 O O . THR B 1 32 ? 59.328 61.263 79.971 1.00 62.03 ? 415 THR B O 1 ATOM 2004 C CB . THR B 1 32 ? 57.394 60.135 82.197 1.00 57.84 ? 415 THR B CB 1 ATOM 2005 O OG1 . THR B 1 32 ? 56.063 59.615 82.335 1.00 57.74 ? 415 THR B OG1 1 ATOM 2006 C CG2 . THR B 1 32 ? 57.976 60.392 83.571 1.00 57.89 ? 415 THR B CG2 1 ATOM 2007 N N . ASP B 1 33 ? 59.395 62.704 81.706 1.00 64.54 ? 416 ASP B N 1 ATOM 2008 C CA . ASP B 1 33 ? 60.762 63.133 81.442 1.00 68.40 ? 416 ASP B CA 1 ATOM 2009 C C . ASP B 1 33 ? 61.705 62.325 82.294 1.00 68.03 ? 416 ASP B C 1 ATOM 2010 O O . ASP B 1 33 ? 61.295 61.713 83.280 1.00 68.08 ? 416 ASP B O 1 ATOM 2011 C CB . ASP B 1 33 ? 60.943 64.621 81.764 1.00 71.70 ? 416 ASP B CB 1 ATOM 2012 C CG . ASP B 1 33 ? 60.125 65.533 80.854 1.00 74.58 ? 416 ASP B CG 1 ATOM 2013 O OD1 . ASP B 1 33 ? 59.937 65.212 79.659 1.00 75.45 ? 416 ASP B OD1 1 ATOM 2014 O OD2 . ASP B 1 33 ? 59.679 66.593 81.341 1.00 77.85 ? 416 ASP B OD2 1 ATOM 2015 N N . LYS B 1 34 ? 62.979 62.339 81.920 1.00 69.92 ? 417 LYS B N 1 ATOM 2016 C CA . LYS B 1 34 ? 64.025 61.797 82.780 1.00 70.87 ? 417 LYS B CA 1 ATOM 2017 C C . LYS B 1 34 ? 64.127 62.658 84.038 1.00 69.85 ? 417 LYS B C 1 ATOM 2018 O O . LYS B 1 34 ? 63.470 63.685 84.148 1.00 69.38 ? 417 LYS B O 1 ATOM 2019 C CB . LYS B 1 34 ? 65.373 61.699 82.043 1.00 73.17 ? 417 LYS B CB 1 ATOM 2020 C CG . LYS B 1 34 ? 66.027 63.026 81.681 1.00 78.29 ? 417 LYS B CG 1 ATOM 2021 C CD . LYS B 1 34 ? 67.420 62.833 81.097 1.00 81.76 ? 417 LYS B CD 1 ATOM 2022 C CE . LYS B 1 34 ? 67.389 62.016 79.812 1.00 83.12 ? 417 LYS B CE 1 ATOM 2023 N NZ . LYS B 1 34 ? 68.632 62.194 79.014 1.00 84.48 ? 417 LYS B NZ 1 ATOM 2024 N N . HIS B 1 35 ? 64.925 62.217 84.998 1.00 69.61 ? 418 HIS B N 1 ATOM 2025 C CA . HIS B 1 35 ? 65.166 63.000 86.196 1.00 69.86 ? 418 HIS B CA 1 ATOM 2026 C C . HIS B 1 35 ? 66.465 62.614 86.862 1.00 69.00 ? 418 HIS B C 1 ATOM 2027 O O . HIS B 1 35 ? 67.019 61.551 86.599 1.00 69.14 ? 418 HIS B O 1 ATOM 2028 C CB . HIS B 1 35 ? 63.996 62.897 87.176 1.00 69.90 ? 418 HIS B CB 1 ATOM 2029 C CG . HIS B 1 35 ? 63.853 61.561 87.830 1.00 71.17 ? 418 HIS B CG 1 ATOM 2030 N ND1 . HIS B 1 35 ? 63.608 60.401 87.122 1.00 71.78 ? 418 HIS B ND1 1 ATOM 2031 C CD2 . HIS B 1 35 ? 63.882 61.206 89.135 1.00 70.51 ? 418 HIS B CD2 1 ATOM 2032 C CE1 . HIS B 1 35 ? 63.497 59.391 87.963 1.00 69.41 ? 418 HIS B CE1 1 ATOM 2033 N NE2 . HIS B 1 35 ? 63.665 59.853 89.187 1.00 69.64 ? 418 HIS B NE2 1 ATOM 2034 N N . ILE B 1 36 ? 66.942 63.507 87.718 1.00 70.08 ? 419 ILE B N 1 ATOM 2035 C CA . ILE B 1 36 ? 68.243 63.380 88.348 1.00 69.91 ? 419 ILE B CA 1 ATOM 2036 C C . ILE B 1 36 ? 68.056 62.849 89.759 1.00 68.29 ? 419 ILE B C 1 ATOM 2037 O O . ILE B 1 36 ? 67.119 63.231 90.459 1.00 68.06 ? 419 ILE B O 1 ATOM 2038 C CB . ILE B 1 36 ? 68.979 64.745 88.374 1.00 71.68 ? 419 ILE B CB 1 ATOM 2039 C CG1 . ILE B 1 36 ? 69.083 65.339 86.959 1.00 72.46 ? 419 ILE B CG1 1 ATOM 2040 C CG2 . ILE B 1 36 ? 70.366 64.607 88.990 1.00 73.09 ? 419 ILE B CG2 1 ATOM 2041 C CD1 . ILE B 1 36 ? 69.812 64.467 85.944 1.00 72.52 ? 419 ILE B CD1 1 ATOM 2042 N N . TYR B 1 37 ? 68.946 61.941 90.145 1.00 68.15 ? 420 TYR B N 1 ATOM 2043 C CA . TYR B 1 37 ? 69.072 61.477 91.517 1.00 68.63 ? 420 TYR B CA 1 ATOM 2044 C C . TYR B 1 37 ? 70.477 61.844 91.970 1.00 71.26 ? 420 TYR B C 1 ATOM 2045 O O . TYR B 1 37 ? 71.453 61.546 91.276 1.00 69.11 ? 420 TYR B O 1 ATOM 2046 C CB . TYR B 1 37 ? 68.845 59.970 91.596 1.00 66.58 ? 420 TYR B CB 1 ATOM 2047 C CG . TYR B 1 37 ? 69.512 59.295 92.769 1.00 66.52 ? 420 TYR B CG 1 ATOM 2048 C CD1 . TYR B 1 37 ? 68.991 59.412 94.061 1.00 66.48 ? 420 TYR B CD1 1 ATOM 2049 C CD2 . TYR B 1 37 ? 70.669 58.529 92.589 1.00 66.10 ? 420 TYR B CD2 1 ATOM 2050 C CE1 . TYR B 1 37 ? 69.604 58.782 95.139 1.00 66.34 ? 420 TYR B CE1 1 ATOM 2051 C CE2 . TYR B 1 37 ? 71.287 57.900 93.657 1.00 66.62 ? 420 TYR B CE2 1 ATOM 2052 C CZ . TYR B 1 37 ? 70.750 58.025 94.928 1.00 67.30 ? 420 TYR B CZ 1 ATOM 2053 O OH . TYR B 1 37 ? 71.373 57.392 95.978 1.00 71.24 ? 420 TYR B OH 1 ATOM 2054 N N . GLN B 1 38 ? 70.562 62.498 93.126 1.00 76.05 ? 421 GLN B N 1 ATOM 2055 C CA . GLN B 1 38 ? 71.823 62.978 93.677 1.00 79.47 ? 421 GLN B CA 1 ATOM 2056 C C . GLN B 1 38 ? 72.159 62.137 94.898 1.00 80.07 ? 421 GLN B C 1 ATOM 2057 O O . GLN B 1 38 ? 71.465 62.229 95.912 1.00 81.37 ? 421 GLN B O 1 ATOM 2058 C CB . GLN B 1 38 ? 71.701 64.455 94.044 1.00 81.99 ? 421 GLN B CB 1 ATOM 2059 C CG . GLN B 1 38 ? 71.399 65.328 92.840 1.00 83.98 ? 421 GLN B CG 1 ATOM 2060 C CD . GLN B 1 38 ? 71.283 66.798 93.187 1.00 88.30 ? 421 GLN B CD 1 ATOM 2061 O OE1 . GLN B 1 38 ? 70.539 67.177 94.097 1.00 89.80 ? 421 GLN B OE1 1 ATOM 2062 N NE2 . GLN B 1 38 ? 72.004 67.641 92.451 1.00 90.58 ? 421 GLN B NE2 1 ATOM 2063 N N . PRO B 1 39 ? 73.207 61.300 94.803 1.00 81.39 ? 422 PRO B N 1 ATOM 2064 C CA . PRO B 1 39 ? 73.511 60.436 95.939 1.00 83.88 ? 422 PRO B CA 1 ATOM 2065 C C . PRO B 1 39 ? 74.081 61.200 97.131 1.00 89.80 ? 422 PRO B C 1 ATOM 2066 O O . PRO B 1 39 ? 74.786 62.203 96.962 1.00 90.93 ? 422 PRO B O 1 ATOM 2067 C CB . PRO B 1 39 ? 74.526 59.427 95.382 1.00 81.73 ? 422 PRO B CB 1 ATOM 2068 C CG . PRO B 1 39 ? 75.060 60.018 94.128 1.00 81.33 ? 422 PRO B CG 1 ATOM 2069 C CD . PRO B 1 39 ? 74.147 61.118 93.681 1.00 81.58 ? 422 PRO B CD 1 ATOM 2070 N N . TYR B 1 40 ? 73.749 60.707 98.320 1.00 95.66 ? 423 TYR B N 1 ATOM 2071 C CA . TYR B 1 40 ? 74.168 61.285 99.583 1.00 102.09 ? 423 TYR B CA 1 ATOM 2072 C C . TYR B 1 40 ? 75.341 60.451 100.120 1.00 103.24 ? 423 TYR B C 1 ATOM 2073 O O . TYR B 1 40 ? 75.327 59.226 99.980 1.00 99.52 ? 423 TYR B O 1 ATOM 2074 C CB . TYR B 1 40 ? 72.986 61.253 100.559 1.00 105.58 ? 423 TYR B CB 1 ATOM 2075 C CG . TYR B 1 40 ? 73.257 61.840 101.928 1.00 111.78 ? 423 TYR B CG 1 ATOM 2076 C CD1 . TYR B 1 40 ? 72.903 63.162 102.228 1.00 113.50 ? 423 TYR B CD1 1 ATOM 2077 C CD2 . TYR B 1 40 ? 73.857 61.070 102.933 1.00 113.42 ? 423 TYR B CD2 1 ATOM 2078 C CE1 . TYR B 1 40 ? 73.144 63.698 103.484 1.00 116.71 ? 423 TYR B CE1 1 ATOM 2079 C CE2 . TYR B 1 40 ? 74.104 61.598 104.189 1.00 117.24 ? 423 TYR B CE2 1 ATOM 2080 C CZ . TYR B 1 40 ? 73.746 62.909 104.461 1.00 119.17 ? 423 TYR B CZ 1 ATOM 2081 O OH . TYR B 1 40 ? 73.989 63.424 105.711 1.00 124.30 ? 423 TYR B OH 1 ATOM 2082 N N . PRO B 1 41 ? 76.351 61.073 100.736 1.00 109.71 ? 424 PRO B N 1 ATOM 2083 C CA . PRO B 1 41 ? 76.487 62.532 100.919 1.00 111.55 ? 424 PRO B CA 1 ATOM 2084 C C . PRO B 1 41 ? 77.052 63.258 99.690 1.00 111.17 ? 424 PRO B C 1 ATOM 2085 O O . PRO B 1 41 ? 76.714 64.419 99.451 1.00 113.45 ? 424 PRO B O 1 ATOM 2086 C CB . PRO B 1 41 ? 77.463 62.636 102.094 1.00 114.74 ? 424 PRO B CB 1 ATOM 2087 C CG . PRO B 1 41 ? 78.301 61.398 101.997 1.00 114.53 ? 424 PRO B CG 1 ATOM 2088 C CD . PRO B 1 41 ? 77.430 60.323 101.410 1.00 112.13 ? 424 PRO B CD 1 ATOM 2089 N N . SER B 1 42 ? 77.918 62.575 98.943 1.00 108.98 ? 425 SER B N 1 ATOM 2090 C CA . SER B 1 42 ? 78.526 63.106 97.733 1.00 108.00 ? 425 SER B CA 1 ATOM 2091 C C . SER B 1 42 ? 78.516 62.017 96.670 1.00 103.82 ? 425 SER B C 1 ATOM 2092 O O . SER B 1 42 ? 78.254 60.848 96.965 1.00 104.29 ? 425 SER B O 1 ATOM 2093 C CB . SER B 1 42 ? 79.965 63.544 98.026 1.00 110.26 ? 425 SER B CB 1 ATOM 2094 O OG . SER B 1 42 ? 80.681 63.836 96.837 1.00 110.95 ? 425 SER B OG 1 ATOM 2095 N N . GLY B 1 43 ? 78.815 62.415 95.439 1.00 99.17 ? 426 GLY B N 1 ATOM 2096 C CA . GLY B 1 43 ? 78.878 61.496 94.307 1.00 94.45 ? 426 GLY B CA 1 ATOM 2097 C C . GLY B 1 43 ? 78.298 62.135 93.063 1.00 91.15 ? 426 GLY B C 1 ATOM 2098 O O . GLY B 1 43 ? 77.483 63.061 93.149 1.00 90.35 ? 426 GLY B O 1 ATOM 2099 N N . ALA B 1 44 ? 78.714 61.627 91.907 1.00 87.71 ? 427 ALA B N 1 ATOM 2100 C CA . ALA B 1 44 ? 78.237 62.122 90.617 1.00 86.16 ? 427 ALA B CA 1 ATOM 2101 C C . ALA B 1 44 ? 76.731 61.900 90.465 1.00 83.94 ? 427 ALA B C 1 ATOM 2102 O O . ALA B 1 44 ? 76.186 60.917 90.982 1.00 83.30 ? 427 ALA B O 1 ATOM 2103 C CB . ALA B 1 44 ? 78.992 61.436 89.481 1.00 85.52 ? 427 ALA B CB 1 ATOM 2104 N N . ASP B 1 45 ? 76.072 62.813 89.753 1.00 82.42 ? 428 ASP B N 1 ATOM 2105 C CA . ASP B 1 45 ? 74.640 62.689 89.467 1.00 80.74 ? 428 ASP B CA 1 ATOM 2106 C C . ASP B 1 45 ? 74.342 61.444 88.629 1.00 78.07 ? 428 ASP B C 1 ATOM 2107 O O . ASP B 1 45 ? 75.144 61.054 87.770 1.00 77.55 ? 428 ASP B O 1 ATOM 2108 C CB . ASP B 1 45 ? 74.112 63.922 88.721 1.00 83.01 ? 428 ASP B CB 1 ATOM 2109 C CG . ASP B 1 45 ? 74.112 65.181 89.574 1.00 86.87 ? 428 ASP B CG 1 ATOM 2110 O OD1 . ASP B 1 45 ? 74.321 65.086 90.807 1.00 89.51 ? 428 ASP B OD1 1 ATOM 2111 O OD2 . ASP B 1 45 ? 73.903 66.274 88.997 1.00 88.53 ? 428 ASP B OD2 1 ATOM 2112 N N . VAL B 1 46 ? 73.184 60.833 88.890 1.00 73.54 ? 429 VAL B N 1 ATOM 2113 C CA . VAL B 1 46 ? 72.719 59.675 88.132 1.00 69.42 ? 429 VAL B CA 1 ATOM 2114 C C . VAL B 1 46 ? 71.365 60.024 87.529 1.00 66.51 ? 429 VAL B C 1 ATOM 2115 O O . VAL B 1 46 ? 70.383 60.174 88.258 1.00 66.37 ? 429 VAL B O 1 ATOM 2116 C CB . VAL B 1 46 ? 72.597 58.418 89.013 1.00 67.65 ? 429 VAL B CB 1 ATOM 2117 C CG1 . VAL B 1 46 ? 72.272 57.195 88.162 1.00 65.54 ? 429 VAL B CG1 1 ATOM 2118 C CG2 . VAL B 1 46 ? 73.883 58.201 89.799 1.00 67.97 ? 429 VAL B CG2 1 ATOM 2119 N N . PRO B 1 47 ? 71.310 60.184 86.199 1.00 63.61 ? 430 PRO B N 1 ATOM 2120 C CA . PRO B 1 47 ? 70.019 60.397 85.560 1.00 63.43 ? 430 PRO B CA 1 ATOM 2121 C C . PRO B 1 47 ? 69.232 59.086 85.443 1.00 63.56 ? 430 PRO B C 1 ATOM 2122 O O . PRO B 1 47 ? 69.820 58.024 85.185 1.00 62.67 ? 430 PRO B O 1 ATOM 2123 C CB . PRO B 1 47 ? 70.389 60.939 84.179 1.00 63.22 ? 430 PRO B CB 1 ATOM 2124 C CG . PRO B 1 47 ? 71.768 60.463 83.922 1.00 62.90 ? 430 PRO B CG 1 ATOM 2125 C CD . PRO B 1 47 ? 72.409 60.114 85.228 1.00 62.71 ? 430 PRO B CD 1 ATOM 2126 N N . PHE B 1 48 ? 67.921 59.175 85.641 1.00 61.81 ? 431 PHE B N 1 ATOM 2127 C CA . PHE B 1 48 ? 67.029 58.039 85.522 1.00 59.85 ? 431 PHE B CA 1 ATOM 2128 C C . PHE B 1 48 ? 66.053 58.302 84.396 1.00 59.56 ? 431 PHE B C 1 ATOM 2129 O O . PHE B 1 48 ? 65.449 59.367 84.343 1.00 59.64 ? 431 PHE B O 1 ATOM 2130 C CB . PHE B 1 48 ? 66.295 57.799 86.838 1.00 58.94 ? 431 PHE B CB 1 ATOM 2131 C CG . PHE B 1 48 ? 67.070 56.956 87.797 1.00 58.41 ? 431 PHE B CG 1 ATOM 2132 C CD1 . PHE B 1 48 ? 68.198 57.462 88.418 1.00 58.96 ? 431 PHE B CD1 1 ATOM 2133 C CD2 . PHE B 1 48 ? 66.694 55.648 88.060 1.00 57.92 ? 431 PHE B CD2 1 ATOM 2134 C CE1 . PHE B 1 48 ? 68.932 56.684 89.301 1.00 59.06 ? 431 PHE B CE1 1 ATOM 2135 C CE2 . PHE B 1 48 ? 67.424 54.860 88.944 1.00 57.51 ? 431 PHE B CE2 1 ATOM 2136 C CZ . PHE B 1 48 ? 68.547 55.380 89.564 1.00 57.94 ? 431 PHE B CZ 1 ATOM 2137 N N . GLY B 1 49 ? 65.886 57.317 83.512 1.00 58.68 ? 432 GLY B N 1 ATOM 2138 C CA . GLY B 1 49 ? 65.037 57.469 82.335 1.00 56.97 ? 432 GLY B CA 1 ATOM 2139 C C . GLY B 1 49 ? 63.558 57.523 82.673 1.00 56.05 ? 432 GLY B C 1 ATOM 2140 O O . GLY B 1 49 ? 63.166 57.206 83.801 1.00 55.38 ? 432 GLY B O 1 ATOM 2141 N N . PRO B 1 50 ? 62.718 57.911 81.695 1.00 56.44 ? 433 PRO B N 1 ATOM 2142 C CA . PRO B 1 50 ? 61.272 58.075 81.913 1.00 56.28 ? 433 PRO B CA 1 ATOM 2143 C C . PRO B 1 50 ? 60.555 56.928 82.643 1.00 55.23 ? 433 PRO B C 1 ATOM 2144 O O . PRO B 1 50 ? 59.813 57.195 83.588 1.00 55.09 ? 433 PRO B O 1 ATOM 2145 C CB . PRO B 1 50 ? 60.719 58.238 80.495 1.00 57.06 ? 433 PRO B CB 1 ATOM 2146 C CG . PRO B 1 50 ? 61.845 58.814 79.721 1.00 57.23 ? 433 PRO B CG 1 ATOM 2147 C CD . PRO B 1 50 ? 63.092 58.217 80.300 1.00 57.25 ? 433 PRO B CD 1 ATOM 2148 N N . PRO B 1 51 ? 60.796 55.660 82.244 1.00 54.69 ? 434 PRO B N 1 ATOM 2149 C CA . PRO B 1 51 ? 60.049 54.590 82.918 1.00 53.44 ? 434 PRO B CA 1 ATOM 2150 C C . PRO B 1 51 ? 60.471 54.279 84.365 1.00 53.32 ? 434 PRO B C 1 ATOM 2151 O O . PRO B 1 51 ? 59.803 53.476 85.021 1.00 53.19 ? 434 PRO B O 1 ATOM 2152 C CB . PRO B 1 51 ? 60.284 53.369 82.033 1.00 53.30 ? 434 PRO B CB 1 ATOM 2153 C CG . PRO B 1 51 ? 61.437 53.689 81.158 1.00 54.40 ? 434 PRO B CG 1 ATOM 2154 C CD . PRO B 1 51 ? 61.820 55.125 81.329 1.00 54.75 ? 434 PRO B CD 1 ATOM 2155 N N . LEU B 1 52 ? 61.554 54.891 84.851 1.00 53.35 ? 435 LEU B N 1 ATOM 2156 C CA . LEU B 1 52 ? 61.991 54.712 86.231 1.00 53.92 ? 435 LEU B CA 1 ATOM 2157 C C . LEU B 1 52 ? 61.597 55.867 87.139 1.00 55.82 ? 435 LEU B C 1 ATOM 2158 O O . LEU B 1 52 ? 62.076 55.960 88.268 1.00 56.04 ? 435 LEU B O 1 ATOM 2159 C CB . LEU B 1 52 ? 63.498 54.461 86.274 1.00 53.53 ? 435 LEU B CB 1 ATOM 2160 C CG . LEU B 1 52 ? 63.969 53.283 85.423 1.00 52.84 ? 435 LEU B CG 1 ATOM 2161 C CD1 . LEU B 1 52 ? 65.486 53.282 85.333 1.00 53.31 ? 435 LEU B CD1 1 ATOM 2162 C CD2 . LEU B 1 52 ? 63.469 51.954 85.971 1.00 52.85 ? 435 LEU B CD2 1 ATOM 2163 N N . ASP B 1 53 ? 60.712 56.740 86.657 1.00 58.69 ? 436 ASP B N 1 ATOM 2164 C CA . ASP B 1 53 ? 60.012 57.696 87.517 1.00 60.37 ? 436 ASP B CA 1 ATOM 2165 C C . ASP B 1 53 ? 59.199 56.904 88.546 1.00 60.06 ? 436 ASP B C 1 ATOM 2166 O O . ASP B 1 53 ? 58.555 55.915 88.202 1.00 60.42 ? 436 ASP B O 1 ATOM 2167 C CB . ASP B 1 53 ? 59.107 58.595 86.670 1.00 63.19 ? 436 ASP B CB 1 ATOM 2168 C CG . ASP B 1 53 ? 58.144 59.424 87.504 1.00 66.37 ? 436 ASP B CG 1 ATOM 2169 O OD1 . ASP B 1 53 ? 58.567 60.461 88.062 1.00 70.38 ? 436 ASP B OD1 1 ATOM 2170 O OD2 . ASP B 1 53 ? 56.953 59.045 87.587 1.00 68.15 ? 436 ASP B OD2 1 ATOM 2171 N N . ILE B 1 54 ? 59.255 57.330 89.805 1.00 61.88 ? 437 ILE B N 1 ATOM 2172 C CA . ILE B 1 54 ? 58.601 56.625 90.922 1.00 62.42 ? 437 ILE B CA 1 ATOM 2173 C C . ILE B 1 54 ? 57.113 56.345 90.667 1.00 63.12 ? 437 ILE B C 1 ATOM 2174 O O . ILE B 1 54 ? 56.638 55.256 90.973 1.00 61.78 ? 437 ILE B O 1 ATOM 2175 C CB . ILE B 1 54 ? 58.789 57.384 92.275 1.00 63.35 ? 437 ILE B CB 1 ATOM 2176 C CG1 . ILE B 1 54 ? 58.295 56.569 93.476 1.00 63.16 ? 437 ILE B CG1 1 ATOM 2177 C CG2 . ILE B 1 54 ? 58.056 58.721 92.283 1.00 63.79 ? 437 ILE B CG2 1 ATOM 2178 C CD1 . ILE B 1 54 ? 59.056 55.295 93.723 1.00 63.51 ? 437 ILE B CD1 1 ATOM 2179 N N . GLN B 1 55 ? 56.400 57.309 90.086 1.00 65.23 ? 438 GLN B N 1 ATOM 2180 C CA . GLN B 1 55 ? 54.956 57.169 89.862 1.00 67.01 ? 438 GLN B CA 1 ATOM 2181 C C . GLN B 1 55 ? 54.631 56.210 88.730 1.00 62.66 ? 438 GLN B C 1 ATOM 2182 O O . GLN B 1 55 ? 53.665 55.452 88.803 1.00 62.64 ? 438 GLN B O 1 ATOM 2183 C CB . GLN B 1 55 ? 54.288 58.538 89.626 1.00 70.88 ? 438 GLN B CB 1 ATOM 2184 C CG . GLN B 1 55 ? 54.203 59.400 90.879 1.00 74.50 ? 438 GLN B CG 1 ATOM 2185 C CD . GLN B 1 55 ? 53.489 58.692 92.023 1.00 78.71 ? 438 GLN B CD 1 ATOM 2186 O OE1 . GLN B 1 55 ? 52.456 58.036 91.820 1.00 81.52 ? 438 GLN B OE1 1 ATOM 2187 N NE2 . GLN B 1 55 ? 54.047 58.797 93.229 1.00 80.66 ? 438 GLN B NE2 1 ATOM 2188 N N . ILE B 1 56 ? 55.442 56.233 87.689 1.00 59.18 ? 439 ILE B N 1 ATOM 2189 C CA . ILE B 1 56 ? 55.283 55.282 86.605 1.00 57.05 ? 439 ILE B CA 1 ATOM 2190 C C . ILE B 1 56 ? 55.540 53.860 87.091 1.00 54.44 ? 439 ILE B C 1 ATOM 2191 O O . ILE B 1 56 ? 54.835 52.948 86.692 1.00 52.85 ? 439 ILE B O 1 ATOM 2192 C CB . ILE B 1 56 ? 56.258 55.631 85.470 1.00 56.11 ? 439 ILE B CB 1 ATOM 2193 C CG1 . ILE B 1 56 ? 55.879 56.992 84.844 1.00 57.05 ? 439 ILE B CG1 1 ATOM 2194 C CG2 . ILE B 1 56 ? 56.340 54.534 84.430 1.00 55.34 ? 439 ILE B CG2 1 ATOM 2195 C CD1 . ILE B 1 56 ? 54.688 57.005 83.896 1.00 57.49 ? 439 ILE B CD1 1 ATOM 2196 N N . LEU B 1 57 ? 56.546 53.673 87.936 1.00 53.53 ? 440 LEU B N 1 ATOM 2197 C CA . LEU B 1 57 ? 56.800 52.351 88.525 1.00 53.87 ? 440 LEU B CA 1 ATOM 2198 C C . LEU B 1 57 ? 55.617 51.848 89.345 1.00 54.33 ? 440 LEU B C 1 ATOM 2199 O O . LEU B 1 57 ? 55.267 50.669 89.242 1.00 54.19 ? 440 LEU B O 1 ATOM 2200 C CB . LEU B 1 57 ? 58.070 52.350 89.375 1.00 54.02 ? 440 LEU B CB 1 ATOM 2201 C CG . LEU B 1 57 ? 59.385 52.457 88.605 1.00 54.71 ? 440 LEU B CG 1 ATOM 2202 C CD1 . LEU B 1 57 ? 60.539 52.624 89.574 1.00 55.47 ? 440 LEU B CD1 1 ATOM 2203 C CD2 . LEU B 1 57 ? 59.623 51.245 87.719 1.00 54.61 ? 440 LEU B CD2 1 ATOM 2204 N N . HIS B 1 58 ? 54.991 52.738 90.126 1.00 54.16 ? 441 HIS B N 1 ATOM 2205 C CA . HIS B 1 58 ? 53.757 52.399 90.852 1.00 53.93 ? 441 HIS B CA 1 ATOM 2206 C C . HIS B 1 58 ? 52.653 51.973 89.877 1.00 53.08 ? 441 HIS B C 1 ATOM 2207 O O . HIS B 1 58 ? 51.930 51.014 90.128 1.00 54.45 ? 441 HIS B O 1 ATOM 2208 C CB . HIS B 1 58 ? 53.249 53.577 91.702 1.00 54.90 ? 441 HIS B CB 1 ATOM 2209 C CG . HIS B 1 58 ? 54.030 53.819 92.959 1.00 54.66 ? 441 HIS B CG 1 ATOM 2210 N ND1 . HIS B 1 58 ? 54.055 52.929 94.006 1.00 54.78 ? 441 HIS B ND1 1 ATOM 2211 C CD2 . HIS B 1 58 ? 54.772 54.878 93.356 1.00 55.44 ? 441 HIS B CD2 1 ATOM 2212 C CE1 . HIS B 1 58 ? 54.803 53.409 94.980 1.00 55.53 ? 441 HIS B CE1 1 ATOM 2213 N NE2 . HIS B 1 58 ? 55.250 54.594 94.611 1.00 55.67 ? 441 HIS B NE2 1 ATOM 2214 N N . GLN B 1 59 ? 52.521 52.707 88.780 1.00 52.51 ? 442 GLN B N 1 ATOM 2215 C CA . GLN B 1 59 ? 51.512 52.412 87.763 1.00 52.07 ? 442 GLN B CA 1 ATOM 2216 C C . GLN B 1 59 ? 51.787 51.098 87.032 1.00 51.94 ? 442 GLN B C 1 ATOM 2217 O O . GLN B 1 59 ? 50.859 50.336 86.740 1.00 51.05 ? 442 GLN B O 1 ATOM 2218 C CB . GLN B 1 59 ? 51.410 53.566 86.766 1.00 52.43 ? 442 GLN B CB 1 ATOM 2219 C CG . GLN B 1 59 ? 50.762 54.797 87.368 1.00 53.02 ? 442 GLN B CG 1 ATOM 2220 C CD . GLN B 1 59 ? 50.947 56.027 86.514 1.00 53.89 ? 442 GLN B CD 1 ATOM 2221 O OE1 . GLN B 1 59 ? 50.748 55.989 85.299 1.00 53.13 ? 442 GLN B OE1 1 ATOM 2222 N NE2 . GLN B 1 59 ? 51.331 57.133 87.139 1.00 56.02 ? 442 GLN B NE2 1 ATOM 2223 N N . VAL B 1 60 ? 53.062 50.842 86.749 1.00 51.03 ? 443 VAL B N 1 ATOM 2224 C CA . VAL B 1 60 ? 53.473 49.583 86.147 1.00 50.20 ? 443 VAL B CA 1 ATOM 2225 C C . VAL B 1 60 ? 53.248 48.419 87.127 1.00 50.06 ? 443 VAL B C 1 ATOM 2226 O O . VAL B 1 60 ? 52.863 47.327 86.708 1.00 50.84 ? 443 VAL B O 1 ATOM 2227 C CB . VAL B 1 60 ? 54.925 49.659 85.626 1.00 49.52 ? 443 VAL B CB 1 ATOM 2228 C CG1 . VAL B 1 60 ? 55.418 48.301 85.153 1.00 48.82 ? 443 VAL B CG1 1 ATOM 2229 C CG2 . VAL B 1 60 ? 55.000 50.639 84.463 1.00 49.57 ? 443 VAL B CG2 1 ATOM 2230 N N . LEU B 1 61 ? 53.443 48.654 88.421 1.00 49.74 ? 444 LEU B N 1 ATOM 2231 C CA . LEU B 1 61 ? 53.155 47.625 89.412 1.00 50.23 ? 444 LEU B CA 1 ATOM 2232 C C . LEU B 1 61 ? 51.675 47.263 89.454 1.00 51.96 ? 444 LEU B C 1 ATOM 2233 O O . LEU B 1 61 ? 51.338 46.096 89.645 1.00 52.43 ? 444 LEU B O 1 ATOM 2234 C CB . LEU B 1 61 ? 53.635 48.034 90.807 1.00 51.03 ? 444 LEU B CB 1 ATOM 2235 C CG . LEU B 1 61 ? 53.386 47.026 91.935 1.00 51.74 ? 444 LEU B CG 1 ATOM 2236 C CD1 . LEU B 1 61 ? 53.971 45.647 91.621 1.00 51.92 ? 444 LEU B CD1 1 ATOM 2237 C CD2 . LEU B 1 61 ? 53.971 47.543 93.230 1.00 52.13 ? 444 LEU B CD2 1 ATOM 2238 N N . ASP B 1 62 ? 50.799 48.256 89.282 1.00 53.64 ? 445 ASP B N 1 ATOM 2239 C CA . ASP B 1 62 ? 49.351 48.015 89.268 1.00 53.87 ? 445 ASP B CA 1 ATOM 2240 C C . ASP B 1 62 ? 48.940 47.183 88.068 1.00 52.14 ? 445 ASP B C 1 ATOM 2241 O O . ASP B 1 62 ? 48.125 46.269 88.197 1.00 51.31 ? 445 ASP B O 1 ATOM 2242 C CB . ASP B 1 62 ? 48.559 49.334 89.302 1.00 56.13 ? 445 ASP B CB 1 ATOM 2243 C CG . ASP B 1 62 ? 48.556 49.988 90.682 1.00 58.32 ? 445 ASP B CG 1 ATOM 2244 O OD1 . ASP B 1 62 ? 48.596 49.257 91.703 1.00 59.63 ? 445 ASP B OD1 1 ATOM 2245 O OD2 . ASP B 1 62 ? 48.489 51.235 90.741 1.00 58.93 ? 445 ASP B OD2 1 ATOM 2246 N N . LEU B 1 63 ? 49.503 47.515 86.909 1.00 52.10 ? 446 LEU B N 1 ATOM 2247 C CA . LEU B 1 63 ? 49.374 46.695 85.700 1.00 53.07 ? 446 LEU B CA 1 ATOM 2248 C C . LEU B 1 63 ? 49.785 45.242 85.975 1.00 51.42 ? 446 LEU B C 1 ATOM 2249 O O . LEU B 1 63 ? 49.056 44.310 85.647 1.00 50.06 ? 446 LEU B O 1 ATOM 2250 C CB . LEU B 1 63 ? 50.234 47.273 84.565 1.00 53.71 ? 446 LEU B CB 1 ATOM 2251 C CG . LEU B 1 63 ? 50.369 46.468 83.264 1.00 54.50 ? 446 LEU B CG 1 ATOM 2252 C CD1 . LEU B 1 63 ? 49.019 46.268 82.603 1.00 55.46 ? 446 LEU B CD1 1 ATOM 2253 C CD2 . LEU B 1 63 ? 51.330 47.159 82.310 1.00 55.06 ? 446 LEU B CD2 1 ATOM 2254 N N . GLN B 1 64 ? 50.947 45.080 86.594 1.00 50.95 ? 447 GLN B N 1 ATOM 2255 C CA . GLN B 1 64 ? 51.509 43.759 86.899 1.00 50.65 ? 447 GLN B CA 1 ATOM 2256 C C . GLN B 1 64 ? 50.614 42.950 87.833 1.00 50.88 ? 447 GLN B C 1 ATOM 2257 O O . GLN B 1 64 ? 50.345 41.779 87.580 1.00 49.67 ? 447 GLN B O 1 ATOM 2258 C CB . GLN B 1 64 ? 52.894 43.926 87.519 1.00 51.41 ? 447 GLN B CB 1 ATOM 2259 C CG . GLN B 1 64 ? 53.765 42.688 87.509 1.00 52.41 ? 447 GLN B CG 1 ATOM 2260 C CD . GLN B 1 64 ? 55.176 43.001 87.964 1.00 53.62 ? 447 GLN B CD 1 ATOM 2261 O OE1 . GLN B 1 64 ? 55.958 43.594 87.213 1.00 56.53 ? 447 GLN B OE1 1 ATOM 2262 N NE2 . GLN B 1 64 ? 55.497 42.660 89.207 1.00 53.83 ? 447 GLN B NE2 1 ATOM 2263 N N . ILE B 1 65 ? 50.159 43.589 88.912 1.00 52.61 ? 448 ILE B N 1 ATOM 2264 C CA . ILE B 1 65 ? 49.255 42.965 89.884 1.00 52.40 ? 448 ILE B CA 1 ATOM 2265 C C . ILE B 1 65 ? 47.943 42.584 89.207 1.00 54.03 ? 448 ILE B C 1 ATOM 2266 O O . ILE B 1 65 ? 47.384 41.532 89.512 1.00 55.54 ? 448 ILE B O 1 ATOM 2267 C CB . ILE B 1 65 ? 48.997 43.883 91.107 1.00 52.93 ? 448 ILE B CB 1 ATOM 2268 C CG1 . ILE B 1 65 ? 50.266 43.955 91.967 1.00 53.79 ? 448 ILE B CG1 1 ATOM 2269 C CG2 . ILE B 1 65 ? 47.826 43.386 91.955 1.00 52.85 ? 448 ILE B CG2 1 ATOM 2270 C CD1 . ILE B 1 65 ? 50.297 45.113 92.946 1.00 54.55 ? 448 ILE B CD1 1 ATOM 2271 N N . ALA B 1 66 ? 47.459 43.429 88.297 1.00 53.44 ? 449 ALA B N 1 ATOM 2272 C CA . ALA B 1 66 ? 46.201 43.156 87.598 1.00 54.74 ? 449 ALA B CA 1 ATOM 2273 C C . ALA B 1 66 ? 46.330 41.943 86.671 1.00 56.24 ? 449 ALA B C 1 ATOM 2274 O O . ALA B 1 66 ? 45.420 41.108 86.623 1.00 57.46 ? 449 ALA B O 1 ATOM 2275 C CB . ALA B 1 66 ? 45.738 44.375 86.823 1.00 53.95 ? 449 ALA B CB 1 ATOM 2276 N N . ILE B 1 67 ? 47.467 41.846 85.971 1.00 55.15 ? 450 ILE B N 1 ATOM 2277 C CA . ILE B 1 67 ? 47.808 40.673 85.155 1.00 54.82 ? 450 ILE B CA 1 ATOM 2278 C C . ILE B 1 67 ? 47.821 39.377 85.985 1.00 57.34 ? 450 ILE B C 1 ATOM 2279 O O . ILE B 1 67 ? 47.242 38.375 85.559 1.00 58.90 ? 450 ILE B O 1 ATOM 2280 C CB . ILE B 1 67 ? 49.159 40.869 84.415 1.00 53.43 ? 450 ILE B CB 1 ATOM 2281 C CG1 . ILE B 1 67 ? 48.998 41.908 83.299 1.00 53.47 ? 450 ILE B CG1 1 ATOM 2282 C CG2 . ILE B 1 67 ? 49.669 39.559 83.818 1.00 53.54 ? 450 ILE B CG2 1 ATOM 2283 C CD1 . ILE B 1 67 ? 50.298 42.514 82.806 1.00 52.34 ? 450 ILE B CD1 1 ATOM 2284 N N . GLU B 1 68 ? 48.458 39.399 87.161 1.00 59.21 ? 451 GLU B N 1 ATOM 2285 C CA . GLU B 1 68 ? 48.443 38.244 88.083 1.00 61.92 ? 451 GLU B CA 1 ATOM 2286 C C . GLU B 1 68 ? 47.039 37.789 88.470 1.00 63.33 ? 451 GLU B C 1 ATOM 2287 O O . GLU B 1 68 ? 46.821 36.610 88.709 1.00 63.82 ? 451 GLU B O 1 ATOM 2288 C CB . GLU B 1 68 ? 49.188 38.557 89.381 1.00 64.17 ? 451 GLU B CB 1 ATOM 2289 C CG . GLU B 1 68 ? 50.691 38.653 89.256 1.00 66.53 ? 451 GLU B CG 1 ATOM 2290 C CD . GLU B 1 68 ? 51.360 38.825 90.608 1.00 70.55 ? 451 GLU B CD 1 ATOM 2291 O OE1 . GLU B 1 68 ? 51.369 37.846 91.389 1.00 73.08 ? 451 GLU B OE1 1 ATOM 2292 O OE2 . GLU B 1 68 ? 51.872 39.939 90.888 1.00 73.55 ? 451 GLU B OE2 1 ATOM 2293 N N . ASN B 1 69 ? 46.112 38.744 88.560 1.00 66.41 ? 452 ASN B N 1 ATOM 2294 C CA . ASN B 1 69 ? 44.724 38.497 88.959 1.00 68.61 ? 452 ASN B CA 1 ATOM 2295 C C . ASN B 1 69 ? 43.776 38.132 87.797 1.00 67.33 ? 452 ASN B C 1 ATOM 2296 O O . ASN B 1 69 ? 42.614 37.820 88.047 1.00 68.54 ? 452 ASN B O 1 ATOM 2297 C CB . ASN B 1 69 ? 44.173 39.736 89.695 1.00 71.46 ? 452 ASN B CB 1 ATOM 2298 C CG . ASN B 1 69 ? 43.091 39.389 90.705 1.00 77.18 ? 452 ASN B CG 1 ATOM 2299 O OD1 . ASN B 1 69 ? 43.276 38.491 91.526 1.00 81.02 ? 452 ASN B OD1 1 ATOM 2300 N ND2 . ASN B 1 69 ? 41.958 40.099 90.656 1.00 80.56 ? 452 ASN B ND2 1 ATOM 2301 N N . ILE B 1 70 ? 44.247 38.170 86.548 1.00 63.78 ? 453 ILE B N 1 ATOM 2302 C CA . ILE B 1 70 ? 43.411 37.785 85.407 1.00 64.62 ? 453 ILE B CA 1 ATOM 2303 C C . ILE B 1 70 ? 43.002 36.323 85.536 1.00 67.21 ? 453 ILE B C 1 ATOM 2304 O O . ILE B 1 70 ? 43.834 35.463 85.870 1.00 67.87 ? 453 ILE B O 1 ATOM 2305 C CB . ILE B 1 70 ? 44.128 37.956 84.044 1.00 63.40 ? 453 ILE B CB 1 ATOM 2306 C CG1 . ILE B 1 70 ? 44.342 39.435 83.730 1.00 61.76 ? 453 ILE B CG1 1 ATOM 2307 C CG2 . ILE B 1 70 ? 43.324 37.305 82.916 1.00 63.42 ? 453 ILE B CG2 1 ATOM 2308 C CD1 . ILE B 1 70 ? 45.335 39.685 82.622 1.00 60.89 ? 453 ILE B CD1 1 ATOM 2309 N N . THR B 1 71 ? 41.727 36.062 85.259 1.00 68.50 ? 454 THR B N 1 ATOM 2310 C CA . THR B 1 71 ? 41.192 34.708 85.206 1.00 71.22 ? 454 THR B CA 1 ATOM 2311 C C . THR B 1 71 ? 40.459 34.488 83.881 1.00 72.05 ? 454 THR B C 1 ATOM 2312 O O . THR B 1 71 ? 39.919 35.427 83.291 1.00 76.39 ? 454 THR B O 1 ATOM 2313 C CB . THR B 1 71 ? 40.243 34.425 86.385 1.00 72.69 ? 454 THR B CB 1 ATOM 2314 O OG1 . THR B 1 71 ? 39.128 35.315 86.331 1.00 75.28 ? 454 THR B OG1 1 ATOM 2315 C CG2 . THR B 1 71 ? 40.961 34.616 87.708 1.00 71.95 ? 454 THR B CG2 1 ATOM 2316 N N . ALA B 1 72 ? 40.497 33.250 83.405 1.00 72.10 ? 455 ALA B N 1 ATOM 2317 C CA . ALA B 1 72 ? 39.745 32.805 82.238 1.00 73.21 ? 455 ALA B CA 1 ATOM 2318 C C . ALA B 1 72 ? 38.929 31.583 82.653 1.00 74.82 ? 455 ALA B C 1 ATOM 2319 O O . ALA B 1 72 ? 39.245 30.940 83.651 1.00 73.29 ? 455 ALA B O 1 ATOM 2320 C CB . ALA B 1 72 ? 40.701 32.448 81.110 1.00 72.29 ? 455 ALA B CB 1 ATOM 2321 N N . SER B 1 73 ? 37.871 31.276 81.908 1.00 80.57 ? 456 SER B N 1 ATOM 2322 C CA . SER B 1 73 ? 37.091 30.057 82.150 1.00 84.58 ? 456 SER B CA 1 ATOM 2323 C C . SER B 1 73 ? 37.221 29.087 80.981 1.00 87.06 ? 456 SER B C 1 ATOM 2324 O O . SER B 1 73 ? 37.245 29.491 79.821 1.00 85.40 ? 456 SER B O 1 ATOM 2325 C CB . SER B 1 73 ? 35.625 30.382 82.444 1.00 86.98 ? 456 SER B CB 1 ATOM 2326 O OG . SER B 1 73 ? 35.106 31.333 81.532 1.00 89.15 ? 456 SER B OG 1 ATOM 2327 N N . TYR B 1 74 ? 37.345 27.806 81.305 1.00 92.23 ? 457 TYR B N 1 ATOM 2328 C CA . TYR B 1 74 ? 37.407 26.752 80.304 1.00 97.86 ? 457 TYR B CA 1 ATOM 2329 C C . TYR B 1 74 ? 36.589 25.569 80.813 1.00 101.69 ? 457 TYR B C 1 ATOM 2330 O O . TYR B 1 74 ? 36.862 25.050 81.897 1.00 101.99 ? 457 TYR B O 1 ATOM 2331 C CB . TYR B 1 74 ? 38.852 26.345 80.032 1.00 98.56 ? 457 TYR B CB 1 ATOM 2332 C CG . TYR B 1 74 ? 38.968 25.366 78.897 1.00 102.34 ? 457 TYR B CG 1 ATOM 2333 C CD1 . TYR B 1 74 ? 39.053 23.991 79.141 1.00 104.01 ? 457 TYR B CD1 1 ATOM 2334 C CD2 . TYR B 1 74 ? 38.957 25.806 77.570 1.00 104.07 ? 457 TYR B CD2 1 ATOM 2335 C CE1 . TYR B 1 74 ? 39.145 23.080 78.100 1.00 107.20 ? 457 TYR B CE1 1 ATOM 2336 C CE2 . TYR B 1 74 ? 39.045 24.902 76.518 1.00 107.10 ? 457 TYR B CE2 1 ATOM 2337 C CZ . TYR B 1 74 ? 39.139 23.541 76.787 1.00 109.35 ? 457 TYR B CZ 1 ATOM 2338 O OH . TYR B 1 74 ? 39.236 22.637 75.752 1.00 114.63 ? 457 TYR B OH 1 ATOM 2339 N N . ASP B 1 75 ? 35.607 25.146 80.011 1.00 105.52 ? 458 ASP B N 1 ATOM 2340 C CA . ASP B 1 75 ? 34.453 24.370 80.487 1.00 106.63 ? 458 ASP B CA 1 ATOM 2341 C C . ASP B 1 75 ? 33.814 25.156 81.652 1.00 106.73 ? 458 ASP B C 1 ATOM 2342 O O . ASP B 1 75 ? 33.542 26.351 81.489 1.00 106.08 ? 458 ASP B O 1 ATOM 2343 C CB . ASP B 1 75 ? 34.840 22.920 80.839 1.00 106.14 ? 458 ASP B CB 1 ATOM 2344 C CG . ASP B 1 75 ? 35.398 22.150 79.647 1.00 107.12 ? 458 ASP B CG 1 ATOM 2345 O OD1 . ASP B 1 75 ? 35.502 22.719 78.538 1.00 105.84 ? 458 ASP B OD1 1 ATOM 2346 O OD2 . ASP B 1 75 ? 35.731 20.957 79.824 1.00 108.17 ? 458 ASP B OD2 1 ATOM 2347 N N . ASN B 1 76 ? 33.599 24.531 82.809 1.00 106.79 ? 459 ASN B N 1 ATOM 2348 C CA . ASN B 1 76 ? 33.060 25.234 83.974 1.00 107.63 ? 459 ASN B CA 1 ATOM 2349 C C . ASN B 1 76 ? 34.185 25.678 84.929 1.00 104.53 ? 459 ASN B C 1 ATOM 2350 O O . ASN B 1 76 ? 33.928 26.428 85.872 1.00 103.02 ? 459 ASN B O 1 ATOM 2351 C CB . ASN B 1 76 ? 32.023 24.337 84.698 1.00 110.35 ? 459 ASN B CB 1 ATOM 2352 C CG . ASN B 1 76 ? 30.766 25.091 85.138 1.00 111.40 ? 459 ASN B CG 1 ATOM 2353 O OD1 . ASN B 1 76 ? 30.467 26.194 84.667 1.00 108.38 ? 459 ASN B OD1 1 ATOM 2354 N ND2 . ASN B 1 76 ? 30.010 24.476 86.042 1.00 112.99 ? 459 ASN B ND2 1 ATOM 2355 N N . GLU B 1 77 ? 35.421 25.235 84.671 1.00 103.41 ? 460 GLU B N 1 ATOM 2356 C CA . GLU B 1 77 ? 36.582 25.554 85.522 1.00 100.47 ? 460 GLU B CA 1 ATOM 2357 C C . GLU B 1 77 ? 37.042 27.012 85.355 1.00 95.46 ? 460 GLU B C 1 ATOM 2358 O O . GLU B 1 77 ? 36.674 27.685 84.386 1.00 95.76 ? 460 GLU B O 1 ATOM 2359 C CB . GLU B 1 77 ? 37.771 24.638 85.193 1.00 102.34 ? 460 GLU B CB 1 ATOM 2360 C CG . GLU B 1 77 ? 37.537 23.133 85.334 1.00 105.40 ? 460 GLU B CG 1 ATOM 2361 C CD . GLU B 1 77 ? 38.758 22.304 84.931 1.00 107.21 ? 460 GLU B CD 1 ATOM 2362 O OE1 . GLU B 1 77 ? 39.543 22.738 84.054 1.00 105.76 ? 460 GLU B OE1 1 ATOM 2363 O OE2 . GLU B 1 77 ? 38.942 21.204 85.498 1.00 110.86 ? 460 GLU B OE2 1 ATOM 2364 N N . THR B 1 78 ? 37.834 27.481 86.324 1.00 88.99 ? 461 THR B N 1 ATOM 2365 C CA . THR B 1 78 ? 38.493 28.794 86.286 1.00 82.63 ? 461 THR B CA 1 ATOM 2366 C C . THR B 1 78 ? 39.995 28.587 86.158 1.00 77.87 ? 461 THR B C 1 ATOM 2367 O O . THR B 1 78 ? 40.562 27.754 86.859 1.00 78.00 ? 461 THR B O 1 ATOM 2368 C CB . THR B 1 78 ? 38.190 29.600 87.575 1.00 81.45 ? 461 THR B CB 1 ATOM 2369 O OG1 . THR B 1 78 ? 36.838 30.063 87.529 1.00 83.54 ? 461 THR B OG1 1 ATOM 2370 C CG2 . THR B 1 78 ? 39.121 30.814 87.748 1.00 80.25 ? 461 THR B CG2 1 ATOM 2371 N N . VAL B 1 79 ? 40.626 29.360 85.272 1.00 73.27 ? 462 VAL B N 1 ATOM 2372 C CA . VAL B 1 79 ? 42.066 29.289 85.034 1.00 69.33 ? 462 VAL B CA 1 ATOM 2373 C C . VAL B 1 79 ? 42.745 30.576 85.491 1.00 66.60 ? 462 VAL B C 1 ATOM 2374 O O . VAL B 1 79 ? 42.432 31.664 84.999 1.00 64.57 ? 462 VAL B O 1 ATOM 2375 C CB . VAL B 1 79 ? 42.391 29.060 83.546 1.00 69.38 ? 462 VAL B CB 1 ATOM 2376 C CG1 . VAL B 1 79 ? 43.882 28.796 83.370 1.00 68.66 ? 462 VAL B CG1 1 ATOM 2377 C CG2 . VAL B 1 79 ? 41.583 27.890 82.991 1.00 71.30 ? 462 VAL B CG2 1 ATOM 2378 N N . THR B 1 80 ? 43.665 30.437 86.443 1.00 64.41 ? 463 THR B N 1 ATOM 2379 C CA . THR B 1 80 ? 44.487 31.546 86.923 1.00 61.66 ? 463 THR B CA 1 ATOM 2380 C C . THR B 1 80 ? 45.886 31.420 86.348 1.00 59.58 ? 463 THR B C 1 ATOM 2381 O O . THR B 1 80 ? 46.273 30.350 85.872 1.00 60.16 ? 463 THR B O 1 ATOM 2382 C CB . THR B 1 80 ? 44.614 31.522 88.458 1.00 61.27 ? 463 THR B CB 1 ATOM 2383 O OG1 . THR B 1 80 ? 45.174 30.275 88.879 1.00 59.99 ? 463 THR B OG1 1 ATOM 2384 C CG2 . THR B 1 80 ? 43.263 31.712 89.133 1.00 63.48 ? 463 THR B CG2 1 ATOM 2385 N N . LEU B 1 81 ? 46.657 32.499 86.432 1.00 57.14 ? 464 LEU B N 1 ATOM 2386 C CA . LEU B 1 81 ? 48.087 32.448 86.128 1.00 55.33 ? 464 LEU B CA 1 ATOM 2387 C C . LEU B 1 81 ? 48.845 31.473 87.057 1.00 56.85 ? 464 LEU B C 1 ATOM 2388 O O . LEU B 1 81 ? 49.797 30.824 86.626 1.00 56.47 ? 464 LEU B O 1 ATOM 2389 C CB . LEU B 1 81 ? 48.706 33.843 86.226 1.00 53.30 ? 464 LEU B CB 1 ATOM 2390 C CG . LEU B 1 81 ? 50.195 33.980 85.911 1.00 51.11 ? 464 LEU B CG 1 ATOM 2391 C CD1 . LEU B 1 81 ? 50.523 33.484 84.513 1.00 50.45 ? 464 LEU B CD1 1 ATOM 2392 C CD2 . LEU B 1 81 ? 50.603 35.429 86.077 1.00 50.75 ? 464 LEU B CD2 1 ATOM 2393 N N . GLN B 1 82 ? 48.387 31.339 88.302 1.00 58.81 ? 465 GLN B N 1 ATOM 2394 C CA . GLN B 1 82 ? 49.026 30.463 89.285 1.00 60.69 ? 465 GLN B CA 1 ATOM 2395 C C . GLN B 1 82 ? 48.919 28.979 88.912 1.00 61.13 ? 465 GLN B C 1 ATOM 2396 O O . GLN B 1 82 ? 49.781 28.176 89.292 1.00 64.10 ? 465 GLN B O 1 ATOM 2397 C CB . GLN B 1 82 ? 48.466 30.714 90.691 1.00 62.63 ? 465 GLN B CB 1 ATOM 2398 C CG . GLN B 1 82 ? 48.807 32.086 91.272 1.00 64.57 ? 465 GLN B CG 1 ATOM 2399 C CD . GLN B 1 82 ? 47.951 33.236 90.724 1.00 65.36 ? 465 GLN B CD 1 ATOM 2400 O OE1 . GLN B 1 82 ? 48.473 34.238 90.227 1.00 62.20 ? 465 GLN B OE1 1 ATOM 2401 N NE2 . GLN B 1 82 ? 46.634 33.094 90.817 1.00 68.93 ? 465 GLN B NE2 1 ATOM 2402 N N . ASP B 1 83 ? 47.885 28.625 88.153 1.00 60.30 ? 466 ASP B N 1 ATOM 2403 C CA . ASP B 1 83 ? 47.727 27.266 87.633 1.00 60.96 ? 466 ASP B CA 1 ATOM 2404 C C . ASP B 1 83 ? 48.720 26.902 86.529 1.00 59.04 ? 466 ASP B C 1 ATOM 2405 O O . ASP B 1 83 ? 49.053 25.733 86.376 1.00 59.29 ? 466 ASP B O 1 ATOM 2406 C CB . ASP B 1 83 ? 46.311 27.057 87.084 1.00 63.01 ? 466 ASP B CB 1 ATOM 2407 C CG . ASP B 1 83 ? 45.239 27.167 88.151 1.00 65.09 ? 466 ASP B CG 1 ATOM 2408 O OD1 . ASP B 1 83 ? 45.466 26.720 89.299 1.00 67.31 ? 466 ASP B OD1 1 ATOM 2409 O OD2 . ASP B 1 83 ? 44.160 27.707 87.830 1.00 67.81 ? 466 ASP B OD2 1 ATOM 2410 N N . ILE B 1 84 ? 49.183 27.888 85.764 1.00 57.44 ? 467 ILE B N 1 ATOM 2411 C CA . ILE B 1 84 ? 49.994 27.627 84.570 1.00 56.27 ? 467 ILE B CA 1 ATOM 2412 C C . ILE B 1 84 ? 51.430 28.131 84.627 1.00 55.85 ? 467 ILE B C 1 ATOM 2413 O O . ILE B 1 84 ? 52.213 27.822 83.729 1.00 57.24 ? 467 ILE B O 1 ATOM 2414 C CB . ILE B 1 84 ? 49.305 28.176 83.299 1.00 56.64 ? 467 ILE B CB 1 ATOM 2415 C CG1 . ILE B 1 84 ? 49.183 29.709 83.315 1.00 55.62 ? 467 ILE B CG1 1 ATOM 2416 C CG2 . ILE B 1 84 ? 47.927 27.545 83.145 1.00 57.26 ? 467 ILE B CG2 1 ATOM 2417 C CD1 . ILE B 1 84 ? 48.648 30.278 82.016 1.00 55.46 ? 467 ILE B CD1 1 ATOM 2418 N N . CYS B 1 85 ? 51.788 28.883 85.668 1.00 55.71 ? 468 CYS B N 1 ATOM 2419 C CA . CYS B 1 85 ? 53.080 29.577 85.700 1.00 54.34 ? 468 CYS B CA 1 ATOM 2420 C C . CYS B 1 85 ? 54.227 28.706 86.211 1.00 52.93 ? 468 CYS B C 1 ATOM 2421 O O . CYS B 1 85 ? 54.020 27.639 86.783 1.00 52.99 ? 468 CYS B O 1 ATOM 2422 C CB . CYS B 1 85 ? 52.988 30.842 86.555 1.00 55.55 ? 468 CYS B CB 1 ATOM 2423 S SG . CYS B 1 85 ? 52.818 30.548 88.334 1.00 57.70 ? 468 CYS B SG 1 ATOM 2424 N N . LEU B 1 86 ? 55.435 29.205 85.988 1.00 50.63 ? 469 LEU B N 1 ATOM 2425 C CA . LEU B 1 86 ? 56.639 28.689 86.609 1.00 49.57 ? 469 LEU B CA 1 ATOM 2426 C C . LEU B 1 86 ? 56.738 29.273 88.017 1.00 48.89 ? 469 LEU B C 1 ATOM 2427 O O . LEU B 1 86 ? 56.824 30.490 88.183 1.00 49.70 ? 469 LEU B O 1 ATOM 2428 C CB . LEU B 1 86 ? 57.860 29.092 85.772 1.00 50.00 ? 469 LEU B CB 1 ATOM 2429 C CG . LEU B 1 86 ? 59.254 28.693 86.263 1.00 49.71 ? 469 LEU B CG 1 ATOM 2430 C CD1 . LEU B 1 86 ? 59.407 27.205 86.459 1.00 48.36 ? 469 LEU B CD1 1 ATOM 2431 C CD2 . LEU B 1 86 ? 60.283 29.209 85.272 1.00 50.16 ? 469 LEU B CD2 1 ATOM 2432 N N . ALA B 1 87 ? 56.712 28.406 89.025 1.00 48.77 ? 470 ALA B N 1 ATOM 2433 C CA . ALA B 1 87 ? 56.703 28.823 90.427 1.00 48.07 ? 470 ALA B CA 1 ATOM 2434 C C . ALA B 1 87 ? 57.679 27.962 91.236 1.00 46.92 ? 470 ALA B C 1 ATOM 2435 O O . ALA B 1 87 ? 57.271 27.004 91.874 1.00 46.25 ? 470 ALA B O 1 ATOM 2436 C CB . ALA B 1 87 ? 55.293 28.727 90.984 1.00 48.46 ? 470 ALA B CB 1 ATOM 2437 N N . PRO B 1 88 ? 58.980 28.312 91.213 1.00 46.65 ? 471 PRO B N 1 ATOM 2438 C CA . PRO B 1 88 ? 60.026 27.404 91.695 1.00 47.11 ? 471 PRO B CA 1 ATOM 2439 C C . PRO B 1 88 ? 60.260 27.341 93.200 1.00 49.89 ? 471 PRO B C 1 ATOM 2440 O O . PRO B 1 88 ? 61.192 26.654 93.616 1.00 50.20 ? 471 PRO B O 1 ATOM 2441 C CB . PRO B 1 88 ? 61.278 27.924 90.980 1.00 45.20 ? 471 PRO B CB 1 ATOM 2442 C CG . PRO B 1 88 ? 61.031 29.367 90.843 1.00 44.59 ? 471 PRO B CG 1 ATOM 2443 C CD . PRO B 1 88 ? 59.560 29.515 90.593 1.00 45.18 ? 471 PRO B CD 1 ATOM 2444 N N . LEU B 1 89 ? 59.455 28.032 94.012 1.00 53.28 ? 472 LEU B N 1 ATOM 2445 C CA . LEU B 1 89 ? 59.603 27.954 95.469 1.00 56.27 ? 472 LEU B CA 1 ATOM 2446 C C . LEU B 1 89 ? 59.048 26.668 96.061 1.00 61.01 ? 472 LEU B C 1 ATOM 2447 O O . LEU B 1 89 ? 59.579 26.178 97.067 1.00 62.87 ? 472 LEU B O 1 ATOM 2448 C CB . LEU B 1 89 ? 59.003 29.175 96.182 1.00 55.30 ? 472 LEU B CB 1 ATOM 2449 C CG . LEU B 1 89 ? 59.953 30.373 96.283 1.00 54.45 ? 472 LEU B CG 1 ATOM 2450 C CD1 . LEU B 1 89 ? 59.181 31.634 96.606 1.00 54.61 ? 472 LEU B CD1 1 ATOM 2451 C CD2 . LEU B 1 89 ? 61.050 30.153 97.313 1.00 54.77 ? 472 LEU B CD2 1 ATOM 2452 N N . SER B 1 90 ? 58.006 26.115 95.446 1.00 65.37 ? 473 SER B N 1 ATOM 2453 C CA . SER B 1 90 ? 57.388 24.880 95.938 1.00 72.06 ? 473 SER B CA 1 ATOM 2454 C C . SER B 1 90 ? 56.718 24.105 94.783 1.00 74.86 ? 473 SER B C 1 ATOM 2455 O O . SER B 1 90 ? 56.381 24.725 93.770 1.00 72.86 ? 473 SER B O 1 ATOM 2456 C CB . SER B 1 90 ? 56.399 25.203 97.075 1.00 74.14 ? 473 SER B CB 1 ATOM 2457 O OG . SER B 1 90 ? 55.168 24.509 96.952 1.00 79.69 ? 473 SER B OG 1 ATOM 2458 N N A PRO B 1 91 ? 56.518 22.774 94.935 0.50 77.63 ? 474 PRO B N 1 ATOM 2459 N N B PRO B 1 91 ? 56.539 22.765 94.942 0.50 78.53 ? 474 PRO B N 1 ATOM 2460 C CA A PRO B 1 91 ? 55.832 21.962 93.911 0.50 79.35 ? 474 PRO B CA 1 ATOM 2461 C CA B PRO B 1 91 ? 55.949 21.862 93.929 0.50 80.79 ? 474 PRO B CA 1 ATOM 2462 C C A PRO B 1 91 ? 54.427 22.443 93.502 0.50 81.36 ? 474 PRO B C 1 ATOM 2463 C C B PRO B 1 91 ? 54.555 22.226 93.401 0.50 83.69 ? 474 PRO B C 1 ATOM 2464 O O A PRO B 1 91 ? 53.932 22.058 92.437 0.50 81.82 ? 474 PRO B O 1 ATOM 2465 O O B PRO B 1 91 ? 54.212 21.836 92.280 0.50 84.24 ? 474 PRO B O 1 ATOM 2466 C CB A PRO B 1 91 ? 55.750 20.578 94.563 0.50 79.39 ? 474 PRO B CB 1 ATOM 2467 C CB B PRO B 1 91 ? 55.868 20.518 94.660 0.50 80.68 ? 474 PRO B CB 1 ATOM 2468 C CG A PRO B 1 91 ? 56.930 20.526 95.466 0.50 78.86 ? 474 PRO B CG 1 ATOM 2469 C CG B PRO B 1 91 ? 56.953 20.567 95.665 0.50 80.11 ? 474 PRO B CG 1 ATOM 2470 C CD A PRO B 1 91 ? 57.089 21.923 96.000 0.50 78.14 ? 474 PRO B CD 1 ATOM 2471 C CD B PRO B 1 91 ? 57.036 21.998 96.107 0.50 79.19 ? 474 PRO B CD 1 ATOM 2472 N N A TYR B 1 92 ? 53.790 23.255 94.342 0.50 82.26 ? 475 TYR B N 1 ATOM 2473 N N B TYR B 1 92 ? 53.749 22.931 94.190 0.50 85.70 ? 475 TYR B N 1 ATOM 2474 C CA A TYR B 1 92 ? 52.566 23.947 93.953 0.50 83.36 ? 475 TYR B CA 1 ATOM 2475 C CA B TYR B 1 92 ? 52.436 23.359 93.708 0.50 87.54 ? 475 TYR B CA 1 ATOM 2476 C C A TYR B 1 92 ? 52.497 25.353 94.562 0.50 80.97 ? 475 TYR B C 1 ATOM 2477 C C B TYR B 1 92 ? 52.380 24.857 93.424 0.50 84.58 ? 475 TYR B C 1 ATOM 2478 O O A TYR B 1 92 ? 51.470 25.746 95.112 0.50 82.52 ? 475 TYR B O 1 ATOM 2479 O O B TYR B 1 92 ? 53.383 25.474 93.066 0.50 84.52 ? 475 TYR B O 1 ATOM 2480 C CB A TYR B 1 92 ? 51.340 23.112 94.347 0.50 87.23 ? 475 TYR B CB 1 ATOM 2481 C CB B TYR B 1 92 ? 51.322 22.954 94.687 0.50 91.29 ? 475 TYR B CB 1 ATOM 2482 C CG A TYR B 1 92 ? 51.182 21.844 93.516 0.50 89.28 ? 475 TYR B CG 1 ATOM 2483 C CG B TYR B 1 92 ? 50.411 21.856 94.158 0.50 93.69 ? 475 TYR B CG 1 ATOM 2484 C CD1 A TYR B 1 92 ? 50.470 21.858 92.315 0.50 88.44 ? 475 TYR B CD1 1 ATOM 2485 C CD1 B TYR B 1 92 ? 49.317 22.161 93.346 0.50 93.52 ? 475 TYR B CD1 1 ATOM 2486 C CD2 A TYR B 1 92 ? 51.753 20.637 93.927 0.50 90.08 ? 475 TYR B CD2 1 ATOM 2487 C CD2 B TYR B 1 92 ? 50.645 20.515 94.465 0.50 94.69 ? 475 TYR B CD2 1 ATOM 2488 C CE1 A TYR B 1 92 ? 50.329 20.711 91.553 0.50 88.15 ? 475 TYR B CE1 1 ATOM 2489 C CE1 B TYR B 1 92 ? 48.487 21.167 92.858 0.50 94.10 ? 475 TYR B CE1 1 ATOM 2490 C CE2 A TYR B 1 92 ? 51.616 19.485 93.167 0.50 89.36 ? 475 TYR B CE2 1 ATOM 2491 C CE2 B TYR B 1 92 ? 49.819 19.516 93.979 0.50 95.34 ? 475 TYR B CE2 1 ATOM 2492 C CZ A TYR B 1 92 ? 50.903 19.529 91.984 0.50 88.33 ? 475 TYR B CZ 1 ATOM 2493 C CZ B TYR B 1 92 ? 48.743 19.847 93.178 0.50 95.30 ? 475 TYR B CZ 1 ATOM 2494 O OH A TYR B 1 92 ? 50.764 18.391 91.225 0.50 86.06 ? 475 TYR B OH 1 ATOM 2495 O OH B TYR B 1 92 ? 47.921 18.855 92.698 0.50 95.35 ? 475 TYR B OH 1 ATOM 2496 N N A ASN B 1 93 ? 53.586 26.112 94.450 0.50 77.41 ? 476 ASN B N 1 ATOM 2497 N N B ASN B 1 93 ? 51.192 25.430 93.563 0.50 82.56 ? 476 ASN B N 1 ATOM 2498 C CA A ASN B 1 93 ? 53.628 27.465 95.002 0.50 73.97 ? 476 ASN B CA 1 ATOM 2499 C CA B ASN B 1 93 ? 51.003 26.846 93.314 0.50 79.33 ? 476 ASN B CA 1 ATOM 2500 C C A ASN B 1 93 ? 52.717 28.438 94.274 0.50 71.04 ? 476 ASN B C 1 ATOM 2501 C C B ASN B 1 93 ? 51.761 27.659 94.354 0.50 77.42 ? 476 ASN B C 1 ATOM 2502 O O A ASN B 1 93 ? 52.318 28.207 93.128 0.50 70.15 ? 476 ASN B O 1 ATOM 2503 O O B ASN B 1 93 ? 51.972 27.213 95.477 0.50 77.15 ? 476 ASN B O 1 ATOM 2504 C CB A ASN B 1 93 ? 55.050 28.020 94.973 0.50 73.66 ? 476 ASN B CB 1 ATOM 2505 C CB B ASN B 1 93 ? 49.512 27.200 93.347 0.50 79.03 ? 476 ASN B CB 1 ATOM 2506 C CG A ASN B 1 93 ? 55.157 29.370 95.659 0.50 74.03 ? 476 ASN B CG 1 ATOM 2507 C CG B ASN B 1 93 ? 48.715 26.471 92.281 0.50 77.94 ? 476 ASN B CG 1 ATOM 2508 O OD1 A ASN B 1 93 ? 54.781 30.400 95.096 0.50 75.55 ? 476 ASN B OD1 1 ATOM 2509 O OD1 B ASN B 1 93 ? 49.186 25.502 91.687 0.50 77.11 ? 476 ASN B OD1 1 ATOM 2510 N ND2 A ASN B 1 93 ? 55.678 29.372 96.878 0.50 73.57 ? 476 ASN B ND2 1 ATOM 2511 N ND2 B ASN B 1 93 ? 47.500 26.937 92.034 0.50 77.20 ? 476 ASN B ND2 1 ATOM 2512 N N A THR B 1 94 ? 52.423 29.547 94.948 0.50 69.07 ? 477 THR B N 1 ATOM 2513 N N B THR B 1 94 ? 52.181 28.851 93.962 0.50 75.69 ? 477 THR B N 1 ATOM 2514 C CA A THR B 1 94 ? 51.537 30.575 94.412 0.50 67.37 ? 477 THR B CA 1 ATOM 2515 C CA B THR B 1 94 ? 52.813 29.786 94.878 0.50 74.94 ? 477 THR B CA 1 ATOM 2516 C C A THR B 1 94 ? 52.260 31.884 94.058 0.50 66.48 ? 477 THR B C 1 ATOM 2517 C C B THR B 1 94 ? 53.156 31.033 94.055 0.50 72.84 ? 477 THR B C 1 ATOM 2518 O O A THR B 1 94 ? 51.614 32.858 93.663 0.50 64.72 ? 477 THR B O 1 ATOM 2519 O O B THR B 1 94 ? 52.497 31.297 93.050 0.50 74.37 ? 477 THR B O 1 ATOM 2520 C CB A THR B 1 94 ? 50.401 30.896 95.399 0.50 66.49 ? 477 THR B CB 1 ATOM 2521 C CB B THR B 1 94 ? 54.037 29.154 95.590 0.50 74.87 ? 477 THR B CB 1 ATOM 2522 O OG1 A THR B 1 94 ? 49.244 31.307 94.670 0.50 66.25 ? 477 THR B OG1 1 ATOM 2523 O OG1 B THR B 1 94 ? 54.466 29.988 96.676 0.50 74.39 ? 477 THR B OG1 1 ATOM 2524 C CG2 A THR B 1 94 ? 50.812 31.997 96.363 0.50 65.69 ? 477 THR B CG2 1 ATOM 2525 C CG2 B THR B 1 94 ? 55.188 28.942 94.628 0.50 74.32 ? 477 THR B CG2 1 ATOM 2526 N N A ASN B 1 95 ? 53.586 31.918 94.207 0.50 65.95 ? 478 ASN B N 1 ATOM 2527 N N B ASN B 1 95 ? 54.156 31.804 94.465 0.50 70.36 ? 478 ASN B N 1 ATOM 2528 C CA A ASN B 1 95 ? 54.366 33.061 93.725 0.50 66.51 ? 478 ASN B CA 1 ATOM 2529 C CA B ASN B 1 95 ? 54.490 33.039 93.758 0.50 69.18 ? 478 ASN B CA 1 ATOM 2530 C C A ASN B 1 95 ? 54.970 32.796 92.349 0.50 63.49 ? 478 ASN B C 1 ATOM 2531 C C B ASN B 1 95 ? 54.988 32.766 92.336 0.50 65.01 ? 478 ASN B C 1 ATOM 2532 O O A ASN B 1 95 ? 56.022 32.175 92.218 0.50 63.98 ? 478 ASN B O 1 ATOM 2533 O O B ASN B 1 95 ? 55.998 32.090 92.160 0.50 65.35 ? 478 ASN B O 1 ATOM 2534 C CB A ASN B 1 95 ? 55.455 33.473 94.710 0.50 69.41 ? 478 ASN B CB 1 ATOM 2535 C CB B ASN B 1 95 ? 55.549 33.813 94.540 0.50 71.61 ? 478 ASN B CB 1 ATOM 2536 C CG A ASN B 1 95 ? 54.910 34.308 95.841 0.50 74.27 ? 478 ASN B CG 1 ATOM 2537 C CG B ASN B 1 95 ? 54.972 34.530 95.741 0.50 76.29 ? 478 ASN B CG 1 ATOM 2538 O OD1 A ASN B 1 95 ? 53.796 34.815 95.760 0.50 75.19 ? 478 ASN B OD1 1 ATOM 2539 O OD1 B ASN B 1 95 ? 53.861 35.053 95.681 0.50 77.41 ? 478 ASN B OD1 1 ATOM 2540 N ND2 A ASN B 1 95 ? 55.692 34.457 96.898 0.50 80.63 ? 478 ASN B ND2 1 ATOM 2541 N ND2 B ASN B 1 95 ? 55.726 34.558 96.840 0.50 81.92 ? 478 ASN B ND2 1 ATOM 2542 N N . CYS B 1 96 ? 54.283 33.284 91.327 1.00 62.20 ? 479 CYS B N 1 ATOM 2543 C CA . CYS B 1 96 ? 54.692 33.102 89.936 1.00 60.31 ? 479 CYS B CA 1 ATOM 2544 C C . CYS B 1 96 ? 55.934 33.906 89.584 1.00 56.35 ? 479 CYS B C 1 ATOM 2545 O O . CYS B 1 96 ? 56.145 34.996 90.108 1.00 56.12 ? 479 CYS B O 1 ATOM 2546 C CB . CYS B 1 96 ? 53.561 33.492 88.977 1.00 61.54 ? 479 CYS B CB 1 ATOM 2547 S SG . CYS B 1 96 ? 52.134 32.385 89.051 1.00 68.19 ? 479 CYS B SG 1 ATOM 2548 N N . THR B 1 97 ? 56.742 33.348 88.688 1.00 52.70 ? 480 THR B N 1 ATOM 2549 C CA . THR B 1 97 ? 57.935 34.005 88.194 1.00 51.54 ? 480 THR B CA 1 ATOM 2550 C C . THR B 1 97 ? 57.519 35.170 87.306 1.00 51.59 ? 480 THR B C 1 ATOM 2551 O O . THR B 1 97 ? 56.822 34.980 86.310 1.00 53.93 ? 480 THR B O 1 ATOM 2552 C CB . THR B 1 97 ? 58.827 33.021 87.412 1.00 50.89 ? 480 THR B CB 1 ATOM 2553 O OG1 . THR B 1 97 ? 59.170 31.917 88.262 1.00 49.70 ? 480 THR B OG1 1 ATOM 2554 C CG2 . THR B 1 97 ? 60.111 33.702 86.917 1.00 50.03 ? 480 THR B CG2 1 ATOM 2555 N N . ILE B 1 98 ? 57.901 36.377 87.710 1.00 51.49 ? 481 ILE B N 1 ATOM 2556 C CA . ILE B 1 98 ? 57.692 37.580 86.916 1.00 51.47 ? 481 ILE B CA 1 ATOM 2557 C C . ILE B 1 98 ? 59.024 38.295 86.851 1.00 50.09 ? 481 ILE B C 1 ATOM 2558 O O . ILE B 1 98 ? 59.502 38.804 87.866 1.00 52.12 ? 481 ILE B O 1 ATOM 2559 C CB . ILE B 1 98 ? 56.642 38.519 87.544 1.00 54.27 ? 481 ILE B CB 1 ATOM 2560 C CG1 . ILE B 1 98 ? 55.344 37.761 87.867 1.00 56.01 ? 481 ILE B CG1 1 ATOM 2561 C CG2 . ILE B 1 98 ? 56.328 39.669 86.588 1.00 55.38 ? 481 ILE B CG2 1 ATOM 2562 C CD1 . ILE B 1 98 ? 54.391 38.527 88.767 1.00 56.69 ? 481 ILE B CD1 1 ATOM 2563 N N . LEU B 1 99 ? 59.638 38.321 85.676 1.00 47.70 ? 482 LEU B N 1 ATOM 2564 C CA . LEU B 1 99 ? 60.873 39.066 85.505 1.00 47.16 ? 482 LEU B CA 1 ATOM 2565 C C . LEU B 1 99 ? 60.501 40.515 85.251 1.00 47.64 ? 482 LEU B C 1 ATOM 2566 O O . LEU B 1 99 ? 59.935 40.850 84.217 1.00 49.26 ? 482 LEU B O 1 ATOM 2567 C CB . LEU B 1 99 ? 61.719 38.499 84.380 1.00 46.71 ? 482 LEU B CB 1 ATOM 2568 C CG . LEU B 1 99 ? 62.024 37.011 84.513 1.00 47.54 ? 482 LEU B CG 1 ATOM 2569 C CD1 . LEU B 1 99 ? 62.945 36.577 83.391 1.00 49.13 ? 482 LEU B CD1 1 ATOM 2570 C CD2 . LEU B 1 99 ? 62.631 36.674 85.860 1.00 47.27 ? 482 LEU B CD2 1 ATOM 2571 N N . SER B 1 100 ? 60.799 41.362 86.226 1.00 47.63 ? 483 SER B N 1 ATOM 2572 C CA . SER B 1 100 ? 60.410 42.756 86.196 1.00 47.76 ? 483 SER B CA 1 ATOM 2573 C C . SER B 1 100 ? 61.270 43.529 87.180 1.00 46.77 ? 483 SER B C 1 ATOM 2574 O O . SER B 1 100 ? 61.687 42.992 88.202 1.00 48.27 ? 483 SER B O 1 ATOM 2575 C CB . SER B 1 100 ? 58.940 42.856 86.594 1.00 48.62 ? 483 SER B CB 1 ATOM 2576 O OG . SER B 1 100 ? 58.570 44.170 86.961 1.00 49.88 ? 483 SER B OG 1 ATOM 2577 N N . VAL B 1 101 ? 61.538 44.789 86.875 1.00 47.07 ? 484 VAL B N 1 ATOM 2578 C CA . VAL B 1 101 ? 62.240 45.682 87.808 1.00 46.57 ? 484 VAL B CA 1 ATOM 2579 C C . VAL B 1 101 ? 61.493 45.855 89.119 1.00 45.54 ? 484 VAL B C 1 ATOM 2580 O O . VAL B 1 101 ? 62.095 46.125 90.150 1.00 45.74 ? 484 VAL B O 1 ATOM 2581 C CB . VAL B 1 101 ? 62.535 47.049 87.125 1.00 47.90 ? 484 VAL B CB 1 ATOM 2582 C CG1 . VAL B 1 101 ? 61.275 47.884 86.887 1.00 48.68 ? 484 VAL B CG1 1 ATOM 2583 C CG2 . VAL B 1 101 ? 63.586 47.844 87.879 1.00 49.34 ? 484 VAL B CG2 1 ATOM 2584 N N . LEU B 1 102 ? 60.180 45.661 89.095 1.00 46.22 ? 485 LEU B N 1 ATOM 2585 C CA . LEU B 1 102 ? 59.389 45.735 90.324 1.00 46.79 ? 485 LEU B CA 1 ATOM 2586 C C . LEU B 1 102 ? 59.680 44.623 91.314 1.00 46.48 ? 485 LEU B C 1 ATOM 2587 O O . LEU B 1 102 ? 59.399 44.780 92.512 1.00 47.77 ? 485 LEU B O 1 ATOM 2588 C CB . LEU B 1 102 ? 57.896 45.795 90.001 1.00 48.40 ? 485 LEU B CB 1 ATOM 2589 C CG . LEU B 1 102 ? 57.621 47.152 89.322 1.00 50.31 ? 485 LEU B CG 1 ATOM 2590 C CD1 . LEU B 1 102 ? 56.463 47.186 88.363 1.00 52.77 ? 485 LEU B CD1 1 ATOM 2591 C CD2 . LEU B 1 102 ? 57.555 48.312 90.333 1.00 52.25 ? 485 LEU B CD2 1 ATOM 2592 N N . ASN B 1 103 ? 60.239 43.510 90.840 1.00 44.40 ? 486 ASN B N 1 ATOM 2593 C CA . ASN B 1 103 ? 60.602 42.429 91.736 1.00 44.84 ? 486 ASN B CA 1 ATOM 2594 C C . ASN B 1 103 ? 61.823 42.734 92.579 1.00 46.05 ? 486 ASN B C 1 ATOM 2595 O O . ASN B 1 103 ? 62.035 42.069 93.592 1.00 46.94 ? 486 ASN B O 1 ATOM 2596 C CB . ASN B 1 103 ? 60.753 41.086 91.007 1.00 44.33 ? 486 ASN B CB 1 ATOM 2597 C CG . ASN B 1 103 ? 59.705 40.076 91.440 1.00 44.92 ? 486 ASN B CG 1 ATOM 2598 O OD1 . ASN B 1 103 ? 59.309 40.039 92.613 1.00 44.88 ? 486 ASN B OD1 1 ATOM 2599 N ND2 . ASN B 1 103 ? 59.256 39.236 90.505 1.00 44.92 ? 486 ASN B ND2 1 ATOM 2600 N N . TYR B 1 104 ? 62.609 43.741 92.193 1.00 46.59 ? 487 TYR B N 1 ATOM 2601 C CA . TYR B 1 104 ? 63.643 44.278 93.086 1.00 47.63 ? 487 TYR B CA 1 ATOM 2602 C C . TYR B 1 104 ? 63.021 44.901 94.354 1.00 48.85 ? 487 TYR B C 1 ATOM 2603 O O . TYR B 1 104 ? 63.694 45.009 95.373 1.00 51.40 ? 487 TYR B O 1 ATOM 2604 C CB . TYR B 1 104 ? 64.527 45.326 92.390 1.00 47.09 ? 487 TYR B CB 1 ATOM 2605 C CG . TYR B 1 104 ? 65.355 44.847 91.214 1.00 46.25 ? 487 TYR B CG 1 ATOM 2606 C CD1 . TYR B 1 104 ? 65.988 43.601 91.220 1.00 45.87 ? 487 TYR B CD1 1 ATOM 2607 C CD2 . TYR B 1 104 ? 65.554 45.673 90.106 1.00 45.77 ? 487 TYR B CD2 1 ATOM 2608 C CE1 . TYR B 1 104 ? 66.748 43.181 90.145 1.00 44.87 ? 487 TYR B CE1 1 ATOM 2609 C CE2 . TYR B 1 104 ? 66.332 45.264 89.038 1.00 45.30 ? 487 TYR B CE2 1 ATOM 2610 C CZ . TYR B 1 104 ? 66.921 44.017 89.060 1.00 45.50 ? 487 TYR B CZ 1 ATOM 2611 O OH . TYR B 1 104 ? 67.680 43.615 87.983 1.00 47.96 ? 487 TYR B OH 1 ATOM 2612 N N . PHE B 1 105 ? 61.757 45.309 94.274 1.00 48.57 ? 488 PHE B N 1 ATOM 2613 C CA . PHE B 1 105 ? 60.986 45.790 95.424 1.00 50.33 ? 488 PHE B CA 1 ATOM 2614 C C . PHE B 1 105 ? 59.911 44.789 95.875 1.00 50.73 ? 488 PHE B C 1 ATOM 2615 O O . PHE B 1 105 ? 58.957 45.152 96.553 1.00 51.35 ? 488 PHE B O 1 ATOM 2616 C CB . PHE B 1 105 ? 60.364 47.134 95.049 1.00 49.87 ? 488 PHE B CB 1 ATOM 2617 C CG . PHE B 1 105 ? 61.366 48.104 94.497 1.00 49.97 ? 488 PHE B CG 1 ATOM 2618 C CD1 . PHE B 1 105 ? 61.635 48.153 93.137 1.00 49.32 ? 488 PHE B CD1 1 ATOM 2619 C CD2 . PHE B 1 105 ? 62.088 48.925 95.349 1.00 50.40 ? 488 PHE B CD2 1 ATOM 2620 C CE1 . PHE B 1 105 ? 62.576 49.032 92.636 1.00 49.22 ? 488 PHE B CE1 1 ATOM 2621 C CE2 . PHE B 1 105 ? 63.038 49.794 94.853 1.00 49.85 ? 488 PHE B CE2 1 ATOM 2622 C CZ . PHE B 1 105 ? 63.279 49.854 93.498 1.00 49.50 ? 488 PHE B CZ 1 ATOM 2623 N N . GLN B 1 106 ? 60.088 43.526 95.498 1.00 50.89 ? 489 GLN B N 1 ATOM 2624 C CA . GLN B 1 106 ? 59.179 42.428 95.833 1.00 50.89 ? 489 GLN B CA 1 ATOM 2625 C C . GLN B 1 106 ? 57.742 42.711 95.450 1.00 50.89 ? 489 GLN B C 1 ATOM 2626 O O . GLN B 1 106 ? 56.814 42.316 96.148 1.00 52.14 ? 489 GLN B O 1 ATOM 2627 C CB . GLN B 1 106 ? 59.318 42.027 97.313 1.00 51.96 ? 489 GLN B CB 1 ATOM 2628 C CG . GLN B 1 106 ? 60.679 41.425 97.657 1.00 51.96 ? 489 GLN B CG 1 ATOM 2629 C CD . GLN B 1 106 ? 61.790 42.464 97.600 1.00 53.48 ? 489 GLN B CD 1 ATOM 2630 O OE1 . GLN B 1 106 ? 61.747 43.462 98.329 1.00 58.64 ? 489 GLN B OE1 1 ATOM 2631 N NE2 . GLN B 1 106 ? 62.774 42.257 96.729 1.00 51.28 ? 489 GLN B NE2 1 ATOM 2632 N N . ASN B 1 107 ? 57.579 43.384 94.315 1.00 51.31 ? 490 ASN B N 1 ATOM 2633 C CA . ASN B 1 107 ? 56.268 43.746 93.786 1.00 51.70 ? 490 ASN B CA 1 ATOM 2634 C C . ASN B 1 107 ? 55.350 44.436 94.820 1.00 51.00 ? 490 ASN B C 1 ATOM 2635 O O . ASN B 1 107 ? 54.155 44.180 94.852 1.00 50.98 ? 490 ASN B O 1 ATOM 2636 C CB . ASN B 1 107 ? 55.597 42.495 93.193 1.00 51.23 ? 490 ASN B CB 1 ATOM 2637 C CG . ASN B 1 107 ? 56.468 41.789 92.158 1.00 51.04 ? 490 ASN B CG 1 ATOM 2638 O OD1 . ASN B 1 107 ? 57.316 42.403 91.501 1.00 49.55 ? 490 ASN B OD1 1 ATOM 2639 N ND2 . ASN B 1 107 ? 56.244 40.492 91.992 1.00 51.34 ? 490 ASN B ND2 1 ATOM 2640 N N . SER B 1 108 ? 55.931 45.302 95.647 1.00 50.55 ? 491 SER B N 1 ATOM 2641 C CA . SER B 1 108 ? 55.227 45.962 96.748 1.00 51.59 ? 491 SER B CA 1 ATOM 2642 C C . SER B 1 108 ? 55.290 47.472 96.594 1.00 52.39 ? 491 SER B C 1 ATOM 2643 O O . SER B 1 108 ? 56.376 48.033 96.467 1.00 52.27 ? 491 SER B O 1 ATOM 2644 C CB . SER B 1 108 ? 55.850 45.582 98.091 1.00 51.58 ? 491 SER B CB 1 ATOM 2645 O OG . SER B 1 108 ? 55.404 46.438 99.136 1.00 51.66 ? 491 SER B OG 1 ATOM 2646 N N . HIS B 1 109 ? 54.126 48.122 96.630 1.00 53.80 ? 492 HIS B N 1 ATOM 2647 C CA . HIS B 1 109 ? 54.057 49.585 96.584 1.00 55.00 ? 492 HIS B CA 1 ATOM 2648 C C . HIS B 1 109 ? 54.807 50.225 97.763 1.00 55.03 ? 492 HIS B C 1 ATOM 2649 O O . HIS B 1 109 ? 55.510 51.219 97.582 1.00 54.03 ? 492 HIS B O 1 ATOM 2650 C CB . HIS B 1 109 ? 52.610 50.074 96.583 1.00 55.49 ? 492 HIS B CB 1 ATOM 2651 C CG . HIS B 1 109 ? 51.834 49.685 95.367 1.00 54.77 ? 492 HIS B CG 1 ATOM 2652 N ND1 . HIS B 1 109 ? 51.942 50.354 94.168 1.00 54.16 ? 492 HIS B ND1 1 ATOM 2653 C CD2 . HIS B 1 109 ? 50.907 48.717 95.175 1.00 55.04 ? 492 HIS B CD2 1 ATOM 2654 C CE1 . HIS B 1 109 ? 51.129 49.809 93.284 1.00 54.70 ? 492 HIS B CE1 1 ATOM 2655 N NE2 . HIS B 1 109 ? 50.489 48.811 93.868 1.00 55.50 ? 492 HIS B NE2 1 ATOM 2656 N N . SER B 1 110 ? 54.657 49.657 98.955 1.00 56.46 ? 493 SER B N 1 ATOM 2657 C CA . SER B 1 110 ? 55.322 50.205 100.147 1.00 58.75 ? 493 SER B CA 1 ATOM 2658 C C . SER B 1 110 ? 56.845 50.036 100.112 1.00 58.70 ? 493 SER B C 1 ATOM 2659 O O . SER B 1 110 ? 57.558 50.954 100.490 1.00 62.68 ? 493 SER B O 1 ATOM 2660 C CB . SER B 1 110 ? 54.732 49.627 101.439 1.00 59.28 ? 493 SER B CB 1 ATOM 2661 O OG . SER B 1 110 ? 54.829 48.224 101.465 1.00 60.43 ? 493 SER B OG 1 ATOM 2662 N N . VAL B 1 111 ? 57.344 48.904 99.622 1.00 58.05 ? 494 VAL B N 1 ATOM 2663 C CA . VAL B 1 111 ? 58.803 48.693 99.509 1.00 57.01 ? 494 VAL B CA 1 ATOM 2664 C C . VAL B 1 111 ? 59.403 49.672 98.496 1.00 57.31 ? 494 VAL B C 1 ATOM 2665 O O . VAL B 1 111 ? 60.472 50.237 98.717 1.00 57.90 ? 494 VAL B O 1 ATOM 2666 C CB . VAL B 1 111 ? 59.164 47.225 99.149 1.00 55.17 ? 494 VAL B CB 1 ATOM 2667 C CG1 . VAL B 1 111 ? 60.661 47.056 98.931 1.00 55.04 ? 494 VAL B CG1 1 ATOM 2668 C CG2 . VAL B 1 111 ? 58.700 46.270 100.239 1.00 54.60 ? 494 VAL B CG2 1 ATOM 2669 N N . LEU B 1 112 ? 58.701 49.884 97.390 1.00 58.66 ? 495 LEU B N 1 ATOM 2670 C CA . LEU B 1 112 ? 59.096 50.893 96.402 1.00 59.60 ? 495 LEU B CA 1 ATOM 2671 C C . LEU B 1 112 ? 59.159 52.314 97.010 1.00 61.23 ? 495 LEU B C 1 ATOM 2672 O O . LEU B 1 112 ? 59.995 53.122 96.610 1.00 59.72 ? 495 LEU B O 1 ATOM 2673 C CB . LEU B 1 112 ? 58.131 50.857 95.211 1.00 58.96 ? 495 LEU B CB 1 ATOM 2674 C CG . LEU B 1 112 ? 58.488 51.653 93.955 1.00 59.08 ? 495 LEU B CG 1 ATOM 2675 C CD1 . LEU B 1 112 ? 59.775 51.154 93.322 1.00 58.43 ? 495 LEU B CD1 1 ATOM 2676 C CD2 . LEU B 1 112 ? 57.346 51.562 92.956 1.00 59.35 ? 495 LEU B CD2 1 ATOM 2677 N N . ASP B 1 113 ? 58.279 52.597 97.973 1.00 63.31 ? 496 ASP B N 1 ATOM 2678 C CA . ASP B 1 113 ? 58.269 53.884 98.684 1.00 64.85 ? 496 ASP B CA 1 ATOM 2679 C C . ASP B 1 113 ? 59.245 54.008 99.855 1.00 67.26 ? 496 ASP B C 1 ATOM 2680 O O . ASP B 1 113 ? 59.432 55.116 100.353 1.00 69.50 ? 496 ASP B O 1 ATOM 2681 C CB . ASP B 1 113 ? 56.848 54.219 99.166 1.00 64.40 ? 496 ASP B CB 1 ATOM 2682 C CG . ASP B 1 113 ? 55.945 54.707 98.047 1.00 63.67 ? 496 ASP B CG 1 ATOM 2683 O OD1 . ASP B 1 113 ? 56.459 55.215 97.023 1.00 62.60 ? 496 ASP B OD1 1 ATOM 2684 O OD2 . ASP B 1 113 ? 54.709 54.599 98.204 1.00 64.55 ? 496 ASP B OD2 1 ATOM 2685 N N . HIS B 1 114 ? 59.845 52.903 100.304 1.00 69.03 ? 497 HIS B N 1 ATOM 2686 C CA . HIS B 1 114 ? 60.847 52.941 101.373 1.00 72.36 ? 497 HIS B CA 1 ATOM 2687 C C . HIS B 1 114 ? 61.840 54.059 101.146 1.00 73.66 ? 497 HIS B C 1 ATOM 2688 O O . HIS B 1 114 ? 62.364 54.201 100.044 1.00 72.00 ? 497 HIS B O 1 ATOM 2689 C CB . HIS B 1 114 ? 61.628 51.630 101.455 1.00 75.20 ? 497 HIS B CB 1 ATOM 2690 C CG . HIS B 1 114 ? 60.973 50.594 102.315 1.00 78.85 ? 497 HIS B CG 1 ATOM 2691 N ND1 . HIS B 1 114 ? 61.661 49.528 102.854 1.00 81.76 ? 497 HIS B ND1 1 ATOM 2692 C CD2 . HIS B 1 114 ? 59.691 50.463 102.736 1.00 81.27 ? 497 HIS B CD2 1 ATOM 2693 C CE1 . HIS B 1 114 ? 60.829 48.778 103.557 1.00 82.74 ? 497 HIS B CE1 1 ATOM 2694 N NE2 . HIS B 1 114 ? 59.627 49.327 103.506 1.00 83.06 ? 497 HIS B NE2 1 ATOM 2695 N N . LYS B 1 115 ? 62.083 54.847 102.188 1.00 76.77 ? 498 LYS B N 1 ATOM 2696 C CA . LYS B 1 115 ? 63.097 55.885 102.143 1.00 79.16 ? 498 LYS B CA 1 ATOM 2697 C C . LYS B 1 115 ? 63.607 56.210 103.535 1.00 80.44 ? 498 LYS B C 1 ATOM 2698 O O . LYS B 1 115 ? 62.865 56.118 104.512 1.00 81.13 ? 498 LYS B O 1 ATOM 2699 C CB . LYS B 1 115 ? 62.564 57.145 101.455 1.00 82.01 ? 498 LYS B CB 1 ATOM 2700 C CG . LYS B 1 115 ? 61.310 57.748 102.065 1.00 86.13 ? 498 LYS B CG 1 ATOM 2701 C CD . LYS B 1 115 ? 61.210 59.232 101.697 1.00 89.45 ? 498 LYS B CD 1 ATOM 2702 C CE . LYS B 1 115 ? 59.968 59.945 102.235 1.00 92.28 ? 498 LYS B CE 1 ATOM 2703 N NZ . LYS B 1 115 ? 58.757 59.623 101.438 1.00 91.81 ? 498 LYS B NZ 1 ATOM 2704 N N . LYS B 1 116 ? 64.890 56.546 103.611 1.00 82.08 ? 499 LYS B N 1 ATOM 2705 C CA . LYS B 1 116 ? 65.518 57.004 104.839 1.00 84.34 ? 499 LYS B CA 1 ATOM 2706 C C . LYS B 1 116 ? 66.098 58.380 104.562 1.00 85.74 ? 499 LYS B C 1 ATOM 2707 O O . LYS B 1 116 ? 66.892 58.556 103.642 1.00 83.02 ? 499 LYS B O 1 ATOM 2708 C CB . LYS B 1 116 ? 66.619 56.043 105.291 1.00 85.62 ? 499 LYS B CB 1 ATOM 2709 C CG . LYS B 1 116 ? 66.146 54.631 105.607 1.00 86.92 ? 499 LYS B CG 1 ATOM 2710 C CD . LYS B 1 116 ? 65.147 54.592 106.752 1.00 89.32 ? 499 LYS B CD 1 ATOM 2711 C CE . LYS B 1 116 ? 64.786 53.183 107.121 1.00 90.55 ? 499 LYS B CE 1 ATOM 2712 N NZ . LYS B 1 116 ? 63.530 53.098 107.906 1.00 91.96 ? 499 LYS B NZ 1 ATOM 2713 N N . GLY B 1 117 ? 65.682 59.355 105.359 1.00 91.06 ? 500 GLY B N 1 ATOM 2714 C CA . GLY B 1 117 ? 66.171 60.717 105.221 1.00 94.53 ? 500 GLY B CA 1 ATOM 2715 C C . GLY B 1 117 ? 65.783 61.588 106.391 1.00 98.16 ? 500 GLY B C 1 ATOM 2716 O O . GLY B 1 117 ? 64.903 61.237 107.178 1.00 97.55 ? 500 GLY B O 1 ATOM 2717 N N . ASP B 1 118 ? 66.477 62.713 106.512 1.00 105.42 ? 501 ASP B N 1 ATOM 2718 C CA . ASP B 1 118 ? 66.152 63.752 107.501 1.00 110.43 ? 501 ASP B CA 1 ATOM 2719 C C . ASP B 1 118 ? 65.175 64.773 106.898 1.00 115.46 ? 501 ASP B C 1 ATOM 2720 O O . ASP B 1 118 ? 64.574 64.516 105.859 1.00 112.34 ? 501 ASP B O 1 ATOM 2721 C CB . ASP B 1 118 ? 67.446 64.413 108.019 1.00 110.25 ? 501 ASP B CB 1 ATOM 2722 C CG . ASP B 1 118 ? 68.261 65.103 106.919 1.00 109.41 ? 501 ASP B CG 1 ATOM 2723 O OD1 . ASP B 1 118 ? 69.487 64.953 106.990 1.00 110.31 ? 501 ASP B OD1 1 ATOM 2724 O OD2 . ASP B 1 118 ? 67.726 65.765 105.988 1.00 107.17 ? 501 ASP B OD2 1 ATOM 2725 N N . ASP B 1 119 ? 65.011 65.903 107.584 1.00 125.93 ? 502 ASP B N 1 ATOM 2726 C CA . ASP B 1 119 ? 64.219 67.061 107.115 1.00 131.95 ? 502 ASP B CA 1 ATOM 2727 C C . ASP B 1 119 ? 64.478 67.520 105.665 1.00 133.53 ? 502 ASP B C 1 ATOM 2728 O O . ASP B 1 119 ? 63.545 67.864 104.929 1.00 134.12 ? 502 ASP B O 1 ATOM 2729 C CB . ASP B 1 119 ? 64.502 68.277 108.036 1.00 135.19 ? 502 ASP B CB 1 ATOM 2730 C CG . ASP B 1 119 ? 63.291 69.174 108.236 1.00 138.44 ? 502 ASP B CG 1 ATOM 2731 O OD1 . ASP B 1 119 ? 63.407 70.389 107.970 1.00 142.34 ? 502 ASP B OD1 1 ATOM 2732 O OD2 . ASP B 1 119 ? 62.233 68.683 108.686 1.00 139.16 ? 502 ASP B OD2 1 ATOM 2733 N N . PHE B 1 120 ? 65.751 67.573 105.287 1.00 135.95 ? 503 PHE B N 1 ATOM 2734 C CA . PHE B 1 120 ? 66.167 68.095 103.983 1.00 136.59 ? 503 PHE B CA 1 ATOM 2735 C C . PHE B 1 120 ? 66.435 66.959 102.998 1.00 132.17 ? 503 PHE B C 1 ATOM 2736 O O . PHE B 1 120 ? 65.817 66.876 101.927 1.00 128.66 ? 503 PHE B O 1 ATOM 2737 C CB . PHE B 1 120 ? 67.452 68.952 104.139 1.00 140.76 ? 503 PHE B CB 1 ATOM 2738 C CG . PHE B 1 120 ? 67.224 70.319 104.759 1.00 147.14 ? 503 PHE B CG 1 ATOM 2739 C CD1 . PHE B 1 120 ? 66.265 71.200 104.248 1.00 148.69 ? 503 PHE B CD1 1 ATOM 2740 C CD2 . PHE B 1 120 ? 67.998 70.745 105.846 1.00 150.41 ? 503 PHE B CD2 1 ATOM 2741 C CE1 . PHE B 1 120 ? 66.068 72.455 104.820 1.00 150.07 ? 503 PHE B CE1 1 ATOM 2742 C CE2 . PHE B 1 120 ? 67.805 72.000 106.417 1.00 151.40 ? 503 PHE B CE2 1 ATOM 2743 C CZ . PHE B 1 120 ? 66.840 72.856 105.903 1.00 151.39 ? 503 PHE B CZ 1 ATOM 2744 N N . PHE B 1 121 ? 67.343 66.073 103.396 1.00 127.28 ? 504 PHE B N 1 ATOM 2745 C CA . PHE B 1 121 ? 68.014 65.156 102.476 1.00 120.81 ? 504 PHE B CA 1 ATOM 2746 C C . PHE B 1 121 ? 67.526 63.703 102.510 1.00 110.96 ? 504 PHE B C 1 ATOM 2747 O O . PHE B 1 121 ? 67.051 63.212 103.536 1.00 109.11 ? 504 PHE B O 1 ATOM 2748 C CB . PHE B 1 121 ? 69.511 65.179 102.773 1.00 124.67 ? 504 PHE B CB 1 ATOM 2749 C CG . PHE B 1 121 ? 70.169 66.496 102.477 1.00 130.30 ? 504 PHE B CG 1 ATOM 2750 C CD1 . PHE B 1 121 ? 70.319 66.930 101.161 1.00 131.56 ? 504 PHE B CD1 1 ATOM 2751 C CD2 . PHE B 1 121 ? 70.650 67.302 103.507 1.00 133.98 ? 504 PHE B CD2 1 ATOM 2752 C CE1 . PHE B 1 121 ? 70.929 68.144 100.876 1.00 134.01 ? 504 PHE B CE1 1 ATOM 2753 C CE2 . PHE B 1 121 ? 71.262 68.517 103.226 1.00 136.21 ? 504 PHE B CE2 1 ATOM 2754 C CZ . PHE B 1 121 ? 71.402 68.938 101.910 1.00 135.80 ? 504 PHE B CZ 1 ATOM 2755 N N . VAL B 1 122 ? 67.680 63.029 101.367 1.00 100.67 ? 505 VAL B N 1 ATOM 2756 C CA . VAL B 1 122 ? 67.379 61.604 101.209 1.00 91.17 ? 505 VAL B CA 1 ATOM 2757 C C . VAL B 1 122 ? 68.700 60.846 101.283 1.00 84.07 ? 505 VAL B C 1 ATOM 2758 O O . VAL B 1 122 ? 69.581 61.066 100.460 1.00 80.10 ? 505 VAL B O 1 ATOM 2759 C CB . VAL B 1 122 ? 66.686 61.324 99.848 1.00 89.33 ? 505 VAL B CB 1 ATOM 2760 C CG1 . VAL B 1 122 ? 66.400 59.834 99.663 1.00 87.36 ? 505 VAL B CG1 1 ATOM 2761 C CG2 . VAL B 1 122 ? 65.395 62.129 99.728 1.00 89.67 ? 505 VAL B CG2 1 ATOM 2762 N N . TYR B 1 123 ? 68.826 59.950 102.257 1.00 81.15 ? 506 TYR B N 1 ATOM 2763 C CA . TYR B 1 123 ? 70.023 59.106 102.381 1.00 81.10 ? 506 TYR B CA 1 ATOM 2764 C C . TYR B 1 123 ? 69.942 57.928 101.428 1.00 76.36 ? 506 TYR B C 1 ATOM 2765 O O . TYR B 1 123 ? 70.905 57.613 100.733 1.00 74.28 ? 506 TYR B O 1 ATOM 2766 C CB . TYR B 1 123 ? 70.185 58.553 103.802 1.00 83.87 ? 506 TYR B CB 1 ATOM 2767 C CG . TYR B 1 123 ? 70.137 59.584 104.910 1.00 87.65 ? 506 TYR B CG 1 ATOM 2768 C CD1 . TYR B 1 123 ? 70.746 60.838 104.769 1.00 89.64 ? 506 TYR B CD1 1 ATOM 2769 C CD2 . TYR B 1 123 ? 69.498 59.294 106.117 1.00 89.92 ? 506 TYR B CD2 1 ATOM 2770 C CE1 . TYR B 1 123 ? 70.700 61.776 105.792 1.00 93.15 ? 506 TYR B CE1 1 ATOM 2771 C CE2 . TYR B 1 123 ? 69.455 60.224 107.148 1.00 93.03 ? 506 TYR B CE2 1 ATOM 2772 C CZ . TYR B 1 123 ? 70.055 61.461 106.982 1.00 94.31 ? 506 TYR B CZ 1 ATOM 2773 O OH . TYR B 1 123 ? 70.003 62.377 108.005 1.00 97.56 ? 506 TYR B OH 1 ATOM 2774 N N . ALA B 1 124 ? 68.786 57.269 101.441 1.00 72.94 ? 507 ALA B N 1 ATOM 2775 C CA . ALA B 1 124 ? 68.531 56.095 100.631 1.00 70.15 ? 507 ALA B CA 1 ATOM 2776 C C . ALA B 1 124 ? 67.059 56.073 100.210 1.00 68.67 ? 507 ALA B C 1 ATOM 2777 O O . ALA B 1 124 ? 66.189 56.481 100.977 1.00 68.10 ? 507 ALA B O 1 ATOM 2778 C CB . ALA B 1 124 ? 68.881 54.839 101.412 1.00 69.42 ? 507 ALA B CB 1 ATOM 2779 N N . ASP B 1 125 ? 66.803 55.610 98.985 1.00 65.29 ? 508 ASP B N 1 ATOM 2780 C CA . ASP B 1 125 ? 65.444 55.406 98.475 1.00 62.99 ? 508 ASP B CA 1 ATOM 2781 C C . ASP B 1 125 ? 65.485 54.382 97.323 1.00 60.95 ? 508 ASP B C 1 ATOM 2782 O O . ASP B 1 125 ? 66.472 53.654 97.186 1.00 61.10 ? 508 ASP B O 1 ATOM 2783 C CB . ASP B 1 125 ? 64.837 56.752 98.058 1.00 62.90 ? 508 ASP B CB 1 ATOM 2784 C CG . ASP B 1 125 ? 65.575 57.406 96.908 1.00 62.92 ? 508 ASP B CG 1 ATOM 2785 O OD1 . ASP B 1 125 ? 66.648 56.913 96.485 1.00 61.95 ? 508 ASP B OD1 1 ATOM 2786 O OD2 . ASP B 1 125 ? 65.075 58.439 96.419 1.00 64.53 ? 508 ASP B OD2 1 ATOM 2787 N N . TYR B 1 126 ? 64.436 54.324 96.504 1.00 58.93 ? 509 TYR B N 1 ATOM 2788 C CA . TYR B 1 126 ? 64.345 53.323 95.437 1.00 57.43 ? 509 TYR B CA 1 ATOM 2789 C C . TYR B 1 126 ? 65.483 53.394 94.410 1.00 57.62 ? 509 TYR B C 1 ATOM 2790 O O . TYR B 1 126 ? 65.887 52.356 93.868 1.00 56.13 ? 509 TYR B O 1 ATOM 2791 C CB . TYR B 1 126 ? 62.974 53.372 94.753 1.00 56.97 ? 509 TYR B CB 1 ATOM 2792 C CG . TYR B 1 126 ? 62.821 54.403 93.652 1.00 58.34 ? 509 TYR B CG 1 ATOM 2793 C CD1 . TYR B 1 126 ? 62.636 55.760 93.948 1.00 58.99 ? 509 TYR B CD1 1 ATOM 2794 C CD2 . TYR B 1 126 ? 62.847 54.024 92.311 1.00 56.65 ? 509 TYR B CD2 1 ATOM 2795 C CE1 . TYR B 1 126 ? 62.488 56.702 92.938 1.00 58.76 ? 509 TYR B CE1 1 ATOM 2796 C CE2 . TYR B 1 126 ? 62.711 54.961 91.298 1.00 57.17 ? 509 TYR B CE2 1 ATOM 2797 C CZ . TYR B 1 126 ? 62.528 56.298 91.614 1.00 58.42 ? 509 TYR B CZ 1 ATOM 2798 O OH . TYR B 1 126 ? 62.375 57.228 90.611 1.00 58.50 ? 509 TYR B OH 1 ATOM 2799 N N . HIS B 1 127 ? 65.999 54.605 94.164 1.00 58.25 ? 510 HIS B N 1 ATOM 2800 C CA . HIS B 1 127 ? 67.179 54.800 93.305 1.00 58.39 ? 510 HIS B CA 1 ATOM 2801 C C . HIS B 1 127 ? 68.360 54.016 93.855 1.00 59.01 ? 510 HIS B C 1 ATOM 2802 O O . HIS B 1 127 ? 69.046 53.303 93.122 1.00 57.35 ? 510 HIS B O 1 ATOM 2803 C CB . HIS B 1 127 ? 67.620 56.273 93.233 1.00 59.76 ? 510 HIS B CB 1 ATOM 2804 C CG . HIS B 1 127 ? 66.553 57.214 92.784 1.00 60.54 ? 510 HIS B CG 1 ATOM 2805 N ND1 . HIS B 1 127 ? 65.951 58.116 93.637 1.00 61.16 ? 510 HIS B ND1 1 ATOM 2806 C CD2 . HIS B 1 127 ? 65.979 57.399 91.575 1.00 60.18 ? 510 HIS B CD2 1 ATOM 2807 C CE1 . HIS B 1 127 ? 65.051 58.815 92.974 1.00 60.34 ? 510 HIS B CE1 1 ATOM 2808 N NE2 . HIS B 1 127 ? 65.048 58.397 91.723 1.00 60.76 ? 510 HIS B NE2 1 ATOM 2809 N N . THR B 1 128 ? 68.609 54.197 95.153 1.00 60.38 ? 511 THR B N 1 ATOM 2810 C CA . THR B 1 128 ? 69.718 53.540 95.840 1.00 60.51 ? 511 THR B CA 1 ATOM 2811 C C . THR B 1 128 ? 69.572 52.036 95.767 1.00 57.94 ? 511 THR B C 1 ATOM 2812 O O . THR B 1 128 ? 70.531 51.339 95.462 1.00 57.38 ? 511 THR B O 1 ATOM 2813 C CB . THR B 1 128 ? 69.793 53.964 97.312 1.00 61.88 ? 511 THR B CB 1 ATOM 2814 O OG1 . THR B 1 128 ? 69.597 55.374 97.390 1.00 64.07 ? 511 THR B OG1 1 ATOM 2815 C CG2 . THR B 1 128 ? 71.153 53.615 97.914 1.00 63.45 ? 511 THR B CG2 1 ATOM 2816 N N . HIS B 1 129 ? 68.359 51.556 96.028 1.00 56.82 ? 512 HIS B N 1 ATOM 2817 C CA . HIS B 1 129 ? 68.059 50.135 95.965 1.00 56.03 ? 512 HIS B CA 1 ATOM 2818 C C . HIS B 1 129 ? 68.264 49.593 94.548 1.00 54.75 ? 512 HIS B C 1 ATOM 2819 O O . HIS B 1 129 ? 68.959 48.585 94.369 1.00 54.82 ? 512 HIS B O 1 ATOM 2820 C CB . HIS B 1 129 ? 66.639 49.853 96.445 1.00 55.63 ? 512 HIS B CB 1 ATOM 2821 C CG . HIS B 1 129 ? 66.382 48.405 96.690 1.00 55.21 ? 512 HIS B CG 1 ATOM 2822 N ND1 . HIS B 1 129 ? 67.103 47.675 97.606 1.00 55.72 ? 512 HIS B ND1 1 ATOM 2823 C CD2 . HIS B 1 129 ? 65.498 47.544 96.136 1.00 55.16 ? 512 HIS B CD2 1 ATOM 2824 C CE1 . HIS B 1 129 ? 66.670 46.428 97.616 1.00 55.05 ? 512 HIS B CE1 1 ATOM 2825 N NE2 . HIS B 1 129 ? 65.701 46.320 96.727 1.00 55.14 ? 512 HIS B NE2 1 ATOM 2826 N N . PHE B 1 130 ? 67.692 50.286 93.559 1.00 52.94 ? 513 PHE B N 1 ATOM 2827 C CA . PHE B 1 130 ? 67.868 49.954 92.140 1.00 52.19 ? 513 PHE B CA 1 ATOM 2828 C C . PHE B 1 130 ? 69.339 49.790 91.758 1.00 53.03 ? 513 PHE B C 1 ATOM 2829 O O . PHE B 1 130 ? 69.721 48.755 91.210 1.00 54.08 ? 513 PHE B O 1 ATOM 2830 C CB . PHE B 1 130 ? 67.208 51.023 91.252 1.00 51.28 ? 513 PHE B CB 1 ATOM 2831 C CG . PHE B 1 130 ? 67.353 50.778 89.763 1.00 49.67 ? 513 PHE B CG 1 ATOM 2832 C CD1 . PHE B 1 130 ? 66.447 49.972 89.081 1.00 48.00 ? 513 PHE B CD1 1 ATOM 2833 C CD2 . PHE B 1 130 ? 68.380 51.379 89.044 1.00 49.39 ? 513 PHE B CD2 1 ATOM 2834 C CE1 . PHE B 1 130 ? 66.575 49.756 87.718 1.00 48.19 ? 513 PHE B CE1 1 ATOM 2835 C CE2 . PHE B 1 130 ? 68.510 51.174 87.682 1.00 49.71 ? 513 PHE B CE2 1 ATOM 2836 C CZ . PHE B 1 130 ? 67.605 50.358 87.015 1.00 49.17 ? 513 PHE B CZ 1 ATOM 2837 N N . LEU B 1 131 ? 70.155 50.804 92.051 1.00 53.74 ? 514 LEU B N 1 ATOM 2838 C CA . LEU B 1 131 ? 71.574 50.798 91.668 1.00 53.09 ? 514 LEU B CA 1 ATOM 2839 C C . LEU B 1 131 ? 72.378 49.697 92.346 1.00 52.62 ? 514 LEU B C 1 ATOM 2840 O O . LEU B 1 131 ? 73.351 49.211 91.774 1.00 52.57 ? 514 LEU B O 1 ATOM 2841 C CB . LEU B 1 131 ? 72.223 52.155 91.924 1.00 54.31 ? 514 LEU B CB 1 ATOM 2842 C CG . LEU B 1 131 ? 71.703 53.270 91.015 1.00 55.43 ? 514 LEU B CG 1 ATOM 2843 C CD1 . LEU B 1 131 ? 72.110 54.635 91.560 1.00 57.15 ? 514 LEU B CD1 1 ATOM 2844 C CD2 . LEU B 1 131 ? 72.186 53.093 89.580 1.00 55.27 ? 514 LEU B CD2 1 ATOM 2845 N N . TYR B 1 132 ? 71.971 49.298 93.546 1.00 53.00 ? 515 TYR B N 1 ATOM 2846 C CA . TYR B 1 132 ? 72.558 48.133 94.197 1.00 53.93 ? 515 TYR B CA 1 ATOM 2847 C C . TYR B 1 132 ? 72.042 46.834 93.537 1.00 53.67 ? 515 TYR B C 1 ATOM 2848 O O . TYR B 1 132 ? 72.838 45.975 93.153 1.00 52.09 ? 515 TYR B O 1 ATOM 2849 C CB . TYR B 1 132 ? 72.275 48.140 95.712 1.00 54.45 ? 515 TYR B CB 1 ATOM 2850 C CG . TYR B 1 132 ? 72.727 46.877 96.414 1.00 55.28 ? 515 TYR B CG 1 ATOM 2851 C CD1 . TYR B 1 132 ? 71.868 45.795 96.541 1.00 54.92 ? 515 TYR B CD1 1 ATOM 2852 C CD2 . TYR B 1 132 ? 74.018 46.746 96.911 1.00 55.98 ? 515 TYR B CD2 1 ATOM 2853 C CE1 . TYR B 1 132 ? 72.270 44.622 97.153 1.00 54.84 ? 515 TYR B CE1 1 ATOM 2854 C CE2 . TYR B 1 132 ? 74.428 45.578 97.534 1.00 56.39 ? 515 TYR B CE2 1 ATOM 2855 C CZ . TYR B 1 132 ? 73.548 44.517 97.651 1.00 55.58 ? 515 TYR B CZ 1 ATOM 2856 O OH . TYR B 1 132 ? 73.949 43.350 98.265 1.00 56.02 ? 515 TYR B OH 1 ATOM 2857 N N . CYS B 1 133 ? 70.722 46.700 93.403 1.00 52.62 ? 516 CYS B N 1 ATOM 2858 C CA . CYS B 1 133 ? 70.116 45.451 92.914 1.00 51.91 ? 516 CYS B CA 1 ATOM 2859 C C . CYS B 1 133 ? 70.528 45.033 91.490 1.00 52.82 ? 516 CYS B C 1 ATOM 2860 O O . CYS B 1 133 ? 70.658 43.841 91.210 1.00 52.71 ? 516 CYS B O 1 ATOM 2861 C CB . CYS B 1 133 ? 68.587 45.512 93.024 1.00 51.20 ? 516 CYS B CB 1 ATOM 2862 S SG . CYS B 1 133 ? 67.936 45.462 94.718 1.00 51.90 ? 516 CYS B SG 1 ATOM 2863 N N . VAL B 1 134 ? 70.750 45.998 90.601 1.00 53.44 ? 517 VAL B N 1 ATOM 2864 C CA . VAL B 1 134 ? 71.265 45.685 89.263 1.00 53.54 ? 517 VAL B CA 1 ATOM 2865 C C . VAL B 1 134 ? 72.676 45.070 89.288 1.00 55.20 ? 517 VAL B C 1 ATOM 2866 O O . VAL B 1 134 ? 73.063 44.380 88.341 1.00 55.90 ? 517 VAL B O 1 ATOM 2867 C CB . VAL B 1 134 ? 71.216 46.891 88.292 1.00 53.50 ? 517 VAL B CB 1 ATOM 2868 C CG1 . VAL B 1 134 ? 69.771 47.345 88.079 1.00 53.18 ? 517 VAL B CG1 1 ATOM 2869 C CG2 . VAL B 1 134 ? 72.115 48.038 88.751 1.00 53.49 ? 517 VAL B CG2 1 ATOM 2870 N N . ARG B 1 135 ? 73.436 45.330 90.350 1.00 56.97 ? 518 ARG B N 1 ATOM 2871 C CA . ARG B 1 135 ? 74.747 44.707 90.557 1.00 59.01 ? 518 ARG B CA 1 ATOM 2872 C C . ARG B 1 135 ? 74.696 43.413 91.377 1.00 56.33 ? 518 ARG B C 1 ATOM 2873 O O . ARG B 1 135 ? 75.588 42.579 91.253 1.00 56.65 ? 518 ARG B O 1 ATOM 2874 C CB . ARG B 1 135 ? 75.693 45.696 91.233 1.00 64.69 ? 518 ARG B CB 1 ATOM 2875 C CG . ARG B 1 135 ? 75.985 46.953 90.419 1.00 70.59 ? 518 ARG B CG 1 ATOM 2876 C CD . ARG B 1 135 ? 76.532 48.052 91.328 1.00 77.95 ? 518 ARG B CD 1 ATOM 2877 N NE . ARG B 1 135 ? 77.087 49.197 90.596 1.00 84.15 ? 518 ARG B NE 1 ATOM 2878 C CZ . ARG B 1 135 ? 78.337 49.294 90.121 1.00 90.67 ? 518 ARG B CZ 1 ATOM 2879 N NH1 . ARG B 1 135 ? 79.230 48.303 90.264 1.00 93.29 ? 518 ARG B NH1 1 ATOM 2880 N NH2 . ARG B 1 135 ? 78.704 50.405 89.481 1.00 93.89 ? 518 ARG B NH2 1 ATOM 2881 N N . ALA B 1 136 ? 73.671 43.251 92.213 1.00 53.97 ? 519 ALA B N 1 ATOM 2882 C CA . ALA B 1 136 ? 73.547 42.089 93.095 1.00 52.29 ? 519 ALA B CA 1 ATOM 2883 C C . ALA B 1 136 ? 72.092 41.613 93.228 1.00 51.05 ? 519 ALA B C 1 ATOM 2884 O O . ALA B 1 136 ? 71.510 41.644 94.325 1.00 52.93 ? 519 ALA B O 1 ATOM 2885 C CB . ALA B 1 136 ? 74.119 42.431 94.457 1.00 53.11 ? 519 ALA B CB 1 ATOM 2886 N N . PRO B 1 137 ? 71.507 41.124 92.121 1.00 48.57 ? 520 PRO B N 1 ATOM 2887 C CA . PRO B 1 137 ? 70.069 40.813 92.136 1.00 47.00 ? 520 PRO B CA 1 ATOM 2888 C C . PRO B 1 137 ? 69.640 39.611 92.979 1.00 46.29 ? 520 PRO B C 1 ATOM 2889 O O . PRO B 1 137 ? 68.444 39.439 93.196 1.00 46.67 ? 520 PRO B O 1 ATOM 2890 C CB . PRO B 1 137 ? 69.735 40.598 90.652 1.00 46.80 ? 520 PRO B CB 1 ATOM 2891 C CG . PRO B 1 137 ? 71.040 40.224 90.017 1.00 47.30 ? 520 PRO B CG 1 ATOM 2892 C CD . PRO B 1 137 ? 72.099 40.962 90.781 1.00 47.64 ? 520 PRO B CD 1 ATOM 2893 N N . ALA B 1 138 ? 70.586 38.796 93.439 1.00 47.07 ? 521 ALA B N 1 ATOM 2894 C CA . ALA B 1 138 ? 70.289 37.668 94.329 1.00 47.82 ? 521 ALA B CA 1 ATOM 2895 C C . ALA B 1 138 ? 70.365 38.040 95.798 1.00 49.14 ? 521 ALA B C 1 ATOM 2896 O O . ALA B 1 138 ? 69.965 37.246 96.651 1.00 51.13 ? 521 ALA B O 1 ATOM 2897 C CB . ALA B 1 138 ? 71.224 36.492 94.045 1.00 46.90 ? 521 ALA B CB 1 ATOM 2898 N N . SER B 1 139 ? 70.872 39.232 96.099 1.00 50.40 ? 522 SER B N 1 ATOM 2899 C CA . SER B 1 139 ? 71.055 39.678 97.485 1.00 52.15 ? 522 SER B CA 1 ATOM 2900 C C . SER B 1 139 ? 69.758 39.636 98.273 1.00 52.56 ? 522 SER B C 1 ATOM 2901 O O . SER B 1 139 ? 68.715 40.039 97.762 1.00 50.35 ? 522 SER B O 1 ATOM 2902 C CB . SER B 1 139 ? 71.590 41.113 97.507 1.00 52.26 ? 522 SER B CB 1 ATOM 2903 O OG . SER B 1 139 ? 71.719 41.591 98.826 1.00 51.80 ? 522 SER B OG 1 ATOM 2904 N N . LEU B 1 140 ? 69.838 39.153 99.515 1.00 57.00 ? 523 LEU B N 1 ATOM 2905 C CA . LEU B 1 140 ? 68.711 39.200 100.459 1.00 59.16 ? 523 LEU B CA 1 ATOM 2906 C C . LEU B 1 140 ? 68.700 40.491 101.283 1.00 62.81 ? 523 LEU B C 1 ATOM 2907 O O . LEU B 1 140 ? 67.764 40.721 102.047 1.00 64.60 ? 523 LEU B O 1 ATOM 2908 C CB . LEU B 1 140 ? 68.746 37.996 101.398 1.00 59.21 ? 523 LEU B CB 1 ATOM 2909 C CG . LEU B 1 140 ? 68.740 36.614 100.729 1.00 61.04 ? 523 LEU B CG 1 ATOM 2910 C CD1 . LEU B 1 140 ? 68.842 35.502 101.766 1.00 61.31 ? 523 LEU B CD1 1 ATOM 2911 C CD2 . LEU B 1 140 ? 67.501 36.418 99.866 1.00 60.46 ? 523 LEU B CD2 1 ATOM 2912 N N . ASN B 1 141 ? 69.707 41.344 101.106 1.00 66.62 ? 524 ASN B N 1 ATOM 2913 C CA . ASN B 1 141 ? 69.921 42.472 101.991 1.00 73.37 ? 524 ASN B CA 1 ATOM 2914 C C . ASN B 1 141 ? 70.750 43.545 101.289 1.00 72.47 ? 524 ASN B C 1 ATOM 2915 O O . ASN B 1 141 ? 71.936 43.380 101.066 1.00 69.15 ? 524 ASN B O 1 ATOM 2916 C CB . ASN B 1 141 ? 70.621 41.984 103.268 1.00 81.34 ? 524 ASN B CB 1 ATOM 2917 C CG . ASN B 1 141 ? 70.603 43.008 104.390 1.00 90.16 ? 524 ASN B CG 1 ATOM 2918 O OD1 . ASN B 1 141 ? 70.284 44.176 104.179 1.00 90.42 ? 524 ASN B OD1 1 ATOM 2919 N ND2 . ASN B 1 141 ? 70.949 42.561 105.600 1.00 100.75 ? 524 ASN B ND2 1 ATOM 2920 N N . ASP B 1 142 ? 70.081 44.632 100.926 1.00 75.89 ? 525 ASP B N 1 ATOM 2921 C CA . ASP B 1 142 ? 70.709 45.877 100.484 1.00 79.17 ? 525 ASP B CA 1 ATOM 2922 C C . ASP B 1 142 ? 71.765 46.311 101.512 1.00 80.97 ? 525 ASP B C 1 ATOM 2923 O O . ASP B 1 142 ? 71.552 46.211 102.718 1.00 79.87 ? 525 ASP B O 1 ATOM 2924 C CB . ASP B 1 142 ? 69.620 46.963 100.356 1.00 80.71 ? 525 ASP B CB 1 ATOM 2925 C CG . ASP B 1 142 ? 70.055 48.177 99.567 1.00 82.70 ? 525 ASP B CG 1 ATOM 2926 O OD1 . ASP B 1 142 ? 71.270 48.421 99.379 1.00 87.74 ? 525 ASP B OD1 1 ATOM 2927 O OD2 . ASP B 1 142 ? 69.138 48.910 99.137 1.00 82.16 ? 525 ASP B OD2 1 ATOM 2928 N N . THR B 1 143 ? 72.903 46.784 101.022 1.00 82.93 ? 526 THR B N 1 ATOM 2929 C CA . THR B 1 143 ? 73.995 47.227 101.877 1.00 86.02 ? 526 THR B CA 1 ATOM 2930 C C . THR B 1 143 ? 73.707 48.634 102.448 1.00 89.01 ? 526 THR B C 1 ATOM 2931 O O . THR B 1 143 ? 74.270 49.021 103.475 1.00 92.27 ? 526 THR B O 1 ATOM 2932 C CB . THR B 1 143 ? 75.338 47.193 101.087 1.00 86.03 ? 526 THR B CB 1 ATOM 2933 O OG1 . THR B 1 143 ? 76.411 47.052 102.009 1.00 89.51 ? 526 THR B OG1 1 ATOM 2934 C CG2 . THR B 1 143 ? 75.562 48.465 100.237 1.00 86.62 ? 526 THR B CG2 1 ATOM 2935 N N . SER B 1 144 ? 72.835 49.390 101.777 1.00 88.35 ? 527 SER B N 1 ATOM 2936 C CA . SER B 1 144 ? 72.410 50.718 102.242 1.00 88.42 ? 527 SER B CA 1 ATOM 2937 C C . SER B 1 144 ? 71.576 50.643 103.526 1.00 86.38 ? 527 SER B C 1 ATOM 2938 O O . SER B 1 144 ? 71.389 49.569 104.103 1.00 84.53 ? 527 SER B O 1 ATOM 2939 C CB . SER B 1 144 ? 71.607 51.435 101.143 1.00 89.54 ? 527 SER B CB 1 ATOM 2940 O OG . SER B 1 144 ? 70.228 51.093 101.198 1.00 89.12 ? 527 SER B OG 1 ATOM 2941 N N . LEU B 1 145 ? 71.054 51.792 103.949 1.00 87.12 ? 528 LEU B N 1 ATOM 2942 C CA . LEU B 1 145 ? 70.279 51.894 105.188 1.00 89.10 ? 528 LEU B CA 1 ATOM 2943 C C . LEU B 1 145 ? 68.886 51.255 105.096 1.00 87.00 ? 528 LEU B C 1 ATOM 2944 O O . LEU B 1 145 ? 68.233 51.043 106.123 1.00 85.88 ? 528 LEU B O 1 ATOM 2945 C CB . LEU B 1 145 ? 70.137 53.363 105.613 1.00 92.76 ? 528 LEU B CB 1 ATOM 2946 C CG . LEU B 1 145 ? 71.438 54.112 105.949 1.00 96.82 ? 528 LEU B CG 1 ATOM 2947 C CD1 . LEU B 1 145 ? 71.978 54.942 104.782 1.00 97.18 ? 528 LEU B CD1 1 ATOM 2948 C CD2 . LEU B 1 145 ? 71.219 55.004 107.167 1.00 100.24 ? 528 LEU B CD2 1 ATOM 2949 N N . LEU B 1 146 ? 68.430 50.971 103.874 1.00 83.96 ? 529 LEU B N 1 ATOM 2950 C CA . LEU B 1 146 ? 67.123 50.350 103.650 1.00 81.42 ? 529 LEU B CA 1 ATOM 2951 C C . LEU B 1 146 ? 67.108 48.896 104.114 1.00 78.01 ? 529 LEU B C 1 ATOM 2952 O O . LEU B 1 146 ? 66.147 48.452 104.731 1.00 74.06 ? 529 LEU B O 1 ATOM 2953 C CB . LEU B 1 146 ? 66.746 50.423 102.164 1.00 81.40 ? 529 LEU B CB 1 ATOM 2954 C CG . LEU B 1 146 ? 66.679 51.817 101.516 1.00 82.65 ? 529 LEU B CG 1 ATOM 2955 C CD1 . LEU B 1 146 ? 66.520 51.706 100.004 1.00 80.88 ? 529 LEU B CD1 1 ATOM 2956 C CD2 . LEU B 1 146 ? 65.563 52.658 102.120 1.00 83.10 ? 529 LEU B CD2 1 ATOM 2957 N N . HIS B 1 147 ? 68.185 48.173 103.814 1.00 79.73 ? 530 HIS B N 1 ATOM 2958 C CA . HIS B 1 147 ? 68.316 46.739 104.118 1.00 81.58 ? 530 HIS B CA 1 ATOM 2959 C C . HIS B 1 147 ? 67.172 45.894 103.545 1.00 78.01 ? 530 HIS B C 1 ATOM 2960 O O . HIS B 1 147 ? 66.704 44.950 104.193 1.00 83.22 ? 530 HIS B O 1 ATOM 2961 C CB . HIS B 1 147 ? 68.471 46.503 105.632 1.00 84.50 ? 530 HIS B CB 1 ATOM 2962 C CG . HIS B 1 147 ? 69.648 47.208 106.231 1.00 89.21 ? 530 HIS B CG 1 ATOM 2963 N ND1 . HIS B 1 147 ? 69.527 48.105 107.272 1.00 93.97 ? 530 HIS B ND1 1 ATOM 2964 C CD2 . HIS B 1 147 ? 70.969 47.152 105.934 1.00 90.51 ? 530 HIS B CD2 1 ATOM 2965 C CE1 . HIS B 1 147 ? 70.723 48.565 107.595 1.00 96.01 ? 530 HIS B CE1 1 ATOM 2966 N NE2 . HIS B 1 147 ? 71.615 48.006 106.796 1.00 94.79 ? 530 HIS B NE2 1 ATOM 2967 N N . ASP B 1 148 ? 66.725 46.252 102.341 1.00 70.36 ? 531 ASP B N 1 ATOM 2968 C CA . ASP B 1 148 ? 65.675 45.514 101.646 1.00 65.50 ? 531 ASP B CA 1 ATOM 2969 C C . ASP B 1 148 ? 66.317 44.441 100.772 1.00 60.56 ? 531 ASP B C 1 ATOM 2970 O O . ASP B 1 148 ? 67.453 44.608 100.329 1.00 58.15 ? 531 ASP B O 1 ATOM 2971 C CB . ASP B 1 148 ? 64.838 46.446 100.764 1.00 66.34 ? 531 ASP B CB 1 ATOM 2972 C CG . ASP B 1 148 ? 63.807 47.259 101.550 1.00 67.97 ? 531 ASP B CG 1 ATOM 2973 O OD1 . ASP B 1 148 ? 63.208 46.727 102.511 1.00 68.04 ? 531 ASP B OD1 1 ATOM 2974 O OD2 . ASP B 1 148 ? 63.568 48.432 101.167 1.00 70.18 ? 531 ASP B OD2 1 ATOM 2975 N N . PRO B 1 149 ? 65.597 43.334 100.516 1.00 56.25 ? 532 PRO B N 1 ATOM 2976 C CA . PRO B 1 149 ? 66.147 42.336 99.607 1.00 54.20 ? 532 PRO B CA 1 ATOM 2977 C C . PRO B 1 149 ? 66.025 42.764 98.143 1.00 52.54 ? 532 PRO B C 1 ATOM 2978 O O . PRO B 1 149 ? 65.166 43.587 97.807 1.00 52.57 ? 532 PRO B O 1 ATOM 2979 C CB . PRO B 1 149 ? 65.285 41.102 99.880 1.00 54.34 ? 532 PRO B CB 1 ATOM 2980 C CG . PRO B 1 149 ? 64.021 41.609 100.480 1.00 54.48 ? 532 PRO B CG 1 ATOM 2981 C CD . PRO B 1 149 ? 64.206 43.034 100.888 1.00 55.01 ? 532 PRO B CD 1 ATOM 2982 N N . CYS B 1 150 ? 66.897 42.224 97.296 1.00 50.14 ? 533 CYS B N 1 ATOM 2983 C CA . CYS B 1 150 ? 66.782 42.365 95.841 1.00 48.67 ? 533 CYS B CA 1 ATOM 2984 C C . CYS B 1 150 ? 66.018 41.210 95.181 1.00 47.95 ? 533 CYS B C 1 ATOM 2985 O O . CYS B 1 150 ? 65.413 41.378 94.118 1.00 48.51 ? 533 CYS B O 1 ATOM 2986 C CB . CYS B 1 150 ? 68.171 42.480 95.229 1.00 49.15 ? 533 CYS B CB 1 ATOM 2987 S SG . CYS B 1 150 ? 69.018 44.001 95.701 1.00 52.57 ? 533 CYS B SG 1 ATOM 2988 N N . LEU B 1 151 ? 66.048 40.043 95.816 1.00 48.46 ? 534 LEU B N 1 ATOM 2989 C CA . LEU B 1 151 ? 65.497 38.810 95.254 1.00 48.49 ? 534 LEU B CA 1 ATOM 2990 C C . LEU B 1 151 ? 64.015 38.960 94.969 1.00 48.16 ? 534 LEU B C 1 ATOM 2991 O O . LEU B 1 151 ? 63.286 39.489 95.797 1.00 49.80 ? 534 LEU B O 1 ATOM 2992 C CB . LEU B 1 151 ? 65.708 37.642 96.234 1.00 49.24 ? 534 LEU B CB 1 ATOM 2993 C CG . LEU B 1 151 ? 65.651 36.232 95.640 1.00 48.96 ? 534 LEU B CG 1 ATOM 2994 C CD1 . LEU B 1 151 ? 66.975 35.918 94.962 1.00 48.45 ? 534 LEU B CD1 1 ATOM 2995 C CD2 . LEU B 1 151 ? 65.350 35.201 96.713 1.00 48.70 ? 534 LEU B CD2 1 ATOM 2996 N N . GLY B 1 152 ? 63.573 38.490 93.804 1.00 47.87 ? 535 GLY B N 1 ATOM 2997 C CA . GLY B 1 152 ? 62.159 38.557 93.427 1.00 49.03 ? 535 GLY B CA 1 ATOM 2998 C C . GLY B 1 152 ? 61.329 37.628 94.294 1.00 49.39 ? 535 GLY B C 1 ATOM 2999 O O . GLY B 1 152 ? 61.865 36.705 94.905 1.00 49.91 ? 535 GLY B O 1 ATOM 3000 N N . THR B 1 153 ? 60.020 37.841 94.315 1.00 49.27 ? 536 THR B N 1 ATOM 3001 C CA . THR B 1 153 ? 59.136 37.074 95.193 1.00 50.46 ? 536 THR B CA 1 ATOM 3002 C C . THR B 1 153 ? 59.020 35.602 94.794 1.00 50.39 ? 536 THR B C 1 ATOM 3003 O O . THR B 1 153 ? 58.556 34.783 95.588 1.00 51.09 ? 536 THR B O 1 ATOM 3004 C CB . THR B 1 153 ? 57.718 37.658 95.237 1.00 51.28 ? 536 THR B CB 1 ATOM 3005 O OG1 . THR B 1 153 ? 57.103 37.509 93.960 1.00 51.40 ? 536 THR B OG1 1 ATOM 3006 C CG2 . THR B 1 153 ? 57.744 39.129 95.625 1.00 51.89 ? 536 THR B CG2 1 ATOM 3007 N N . PHE B 1 154 ? 59.422 35.287 93.562 1.00 49.23 ? 537 PHE B N 1 ATOM 3008 C CA . PHE B 1 154 ? 59.474 33.908 93.066 1.00 48.91 ? 537 PHE B CA 1 ATOM 3009 C C . PHE B 1 154 ? 60.692 33.101 93.542 1.00 49.17 ? 537 PHE B C 1 ATOM 3010 O O . PHE B 1 154 ? 60.788 31.917 93.229 1.00 49.19 ? 537 PHE B O 1 ATOM 3011 C CB . PHE B 1 154 ? 59.374 33.871 91.536 1.00 47.65 ? 537 PHE B CB 1 ATOM 3012 C CG . PHE B 1 154 ? 60.569 34.441 90.817 1.00 47.46 ? 537 PHE B CG 1 ATOM 3013 C CD1 . PHE B 1 154 ? 60.621 35.792 90.474 1.00 46.47 ? 537 PHE B CD1 1 ATOM 3014 C CD2 . PHE B 1 154 ? 61.630 33.623 90.457 1.00 47.58 ? 537 PHE B CD2 1 ATOM 3015 C CE1 . PHE B 1 154 ? 61.716 36.310 89.815 1.00 46.97 ? 537 PHE B CE1 1 ATOM 3016 C CE2 . PHE B 1 154 ? 62.736 34.139 89.796 1.00 47.28 ? 537 PHE B CE2 1 ATOM 3017 C CZ . PHE B 1 154 ? 62.776 35.481 89.467 1.00 46.65 ? 537 PHE B CZ 1 ATOM 3018 N N . GLY B 1 155 ? 61.623 33.734 94.260 1.00 48.19 ? 538 GLY B N 1 ATOM 3019 C CA . GLY B 1 155 ? 62.733 33.026 94.903 1.00 48.14 ? 538 GLY B CA 1 ATOM 3020 C C . GLY B 1 155 ? 64.040 33.017 94.131 1.00 47.51 ? 538 GLY B C 1 ATOM 3021 O O . GLY B 1 155 ? 64.982 32.322 94.514 1.00 47.33 ? 538 GLY B O 1 ATOM 3022 N N . GLY B 1 156 ? 64.117 33.800 93.057 1.00 47.24 ? 539 GLY B N 1 ATOM 3023 C CA . GLY B 1 156 ? 65.350 33.914 92.271 1.00 46.37 ? 539 GLY B CA 1 ATOM 3024 C C . GLY B 1 156 ? 65.672 35.338 91.856 1.00 45.77 ? 539 GLY B C 1 ATOM 3025 O O . GLY B 1 156 ? 64.821 36.219 91.923 1.00 44.86 ? 539 GLY B O 1 ATOM 3026 N N . PRO B 1 157 ? 66.911 35.570 91.411 1.00 46.68 ? 540 PRO B N 1 ATOM 3027 C CA . PRO B 1 157 ? 67.312 36.915 91.010 1.00 45.97 ? 540 PRO B CA 1 ATOM 3028 C C . PRO B 1 157 ? 66.704 37.296 89.681 1.00 44.78 ? 540 PRO B C 1 ATOM 3029 O O . PRO B 1 157 ? 66.409 36.422 88.867 1.00 47.04 ? 540 PRO B O 1 ATOM 3030 C CB . PRO B 1 157 ? 68.825 36.796 90.887 1.00 47.46 ? 540 PRO B CB 1 ATOM 3031 C CG . PRO B 1 157 ? 69.038 35.366 90.469 1.00 47.95 ? 540 PRO B CG 1 ATOM 3032 C CD . PRO B 1 157 ? 67.980 34.577 91.176 1.00 46.63 ? 540 PRO B CD 1 ATOM 3033 N N . VAL B 1 158 ? 66.499 38.591 89.487 1.00 44.23 ? 541 VAL B N 1 ATOM 3034 C CA . VAL B 1 158 ? 66.024 39.152 88.238 1.00 43.64 ? 541 VAL B CA 1 ATOM 3035 C C . VAL B 1 158 ? 67.208 39.898 87.637 1.00 44.67 ? 541 VAL B C 1 ATOM 3036 O O . VAL B 1 158 ? 67.644 40.919 88.178 1.00 46.31 ? 541 VAL B O 1 ATOM 3037 C CB . VAL B 1 158 ? 64.843 40.110 88.485 1.00 44.25 ? 541 VAL B CB 1 ATOM 3038 C CG1 . VAL B 1 158 ? 64.389 40.778 87.192 1.00 44.74 ? 541 VAL B CG1 1 ATOM 3039 C CG2 . VAL B 1 158 ? 63.680 39.360 89.117 1.00 44.24 ? 541 VAL B CG2 1 ATOM 3040 N N . PHE B 1 159 ? 67.737 39.397 86.526 1.00 44.24 ? 542 PHE B N 1 ATOM 3041 C CA . PHE B 1 159 ? 68.906 40.015 85.922 1.00 45.77 ? 542 PHE B CA 1 ATOM 3042 C C . PHE B 1 159 ? 68.519 41.283 85.163 1.00 46.44 ? 542 PHE B C 1 ATOM 3043 O O . PHE B 1 159 ? 67.585 41.262 84.372 1.00 48.27 ? 542 PHE B O 1 ATOM 3044 C CB . PHE B 1 159 ? 69.634 39.023 85.019 1.00 46.76 ? 542 PHE B CB 1 ATOM 3045 C CG . PHE B 1 159 ? 70.228 37.873 85.769 1.00 46.82 ? 542 PHE B CG 1 ATOM 3046 C CD1 . PHE B 1 159 ? 71.242 38.088 86.687 1.00 47.63 ? 542 PHE B CD1 1 ATOM 3047 C CD2 . PHE B 1 159 ? 69.762 36.589 85.579 1.00 47.24 ? 542 PHE B CD2 1 ATOM 3048 C CE1 . PHE B 1 159 ? 71.780 37.045 87.409 1.00 47.93 ? 542 PHE B CE1 1 ATOM 3049 C CE2 . PHE B 1 159 ? 70.298 35.536 86.286 1.00 47.08 ? 542 PHE B CE2 1 ATOM 3050 C CZ . PHE B 1 159 ? 71.305 35.766 87.209 1.00 48.78 ? 542 PHE B CZ 1 ATOM 3051 N N . PRO B 1 160 ? 69.232 42.396 85.401 1.00 46.86 ? 543 PRO B N 1 ATOM 3052 C CA . PRO B 1 160 ? 68.803 43.709 84.882 1.00 46.83 ? 543 PRO B CA 1 ATOM 3053 C C . PRO B 1 160 ? 68.622 43.802 83.354 1.00 45.71 ? 543 PRO B C 1 ATOM 3054 O O . PRO B 1 160 ? 67.691 44.450 82.883 1.00 45.37 ? 543 PRO B O 1 ATOM 3055 C CB . PRO B 1 160 ? 69.916 44.650 85.367 1.00 47.89 ? 543 PRO B CB 1 ATOM 3056 C CG . PRO B 1 160 ? 71.110 43.769 85.493 1.00 48.55 ? 543 PRO B CG 1 ATOM 3057 C CD . PRO B 1 160 ? 70.570 42.468 86.008 1.00 47.15 ? 543 PRO B CD 1 ATOM 3058 N N . TRP B 1 161 ? 69.500 43.149 82.600 1.00 46.37 ? 544 TRP B N 1 ATOM 3059 C CA . TRP B 1 161 ? 69.417 43.111 81.132 1.00 46.17 ? 544 TRP B CA 1 ATOM 3060 C C . TRP B 1 161 ? 68.143 42.424 80.587 1.00 45.62 ? 544 TRP B C 1 ATOM 3061 O O . TRP B 1 161 ? 67.807 42.607 79.425 1.00 48.28 ? 544 TRP B O 1 ATOM 3062 C CB . TRP B 1 161 ? 70.685 42.476 80.520 1.00 46.06 ? 544 TRP B CB 1 ATOM 3063 C CG . TRP B 1 161 ? 70.918 41.061 80.937 1.00 47.28 ? 544 TRP B CG 1 ATOM 3064 C CD1 . TRP B 1 161 ? 70.335 39.944 80.408 1.00 46.83 ? 544 TRP B CD1 1 ATOM 3065 C CD2 . TRP B 1 161 ? 71.786 40.602 81.977 1.00 47.45 ? 544 TRP B CD2 1 ATOM 3066 N NE1 . TRP B 1 161 ? 70.792 38.819 81.044 1.00 46.30 ? 544 TRP B NE1 1 ATOM 3067 C CE2 . TRP B 1 161 ? 71.682 39.189 82.014 1.00 46.98 ? 544 TRP B CE2 1 ATOM 3068 C CE3 . TRP B 1 161 ? 72.655 41.243 82.868 1.00 47.98 ? 544 TRP B CE3 1 ATOM 3069 C CZ2 . TRP B 1 161 ? 72.400 38.406 82.916 1.00 47.36 ? 544 TRP B CZ2 1 ATOM 3070 C CZ3 . TRP B 1 161 ? 73.375 40.465 83.772 1.00 48.44 ? 544 TRP B CZ3 1 ATOM 3071 C CH2 . TRP B 1 161 ? 73.240 39.059 83.788 1.00 48.83 ? 544 TRP B CH2 1 ATOM 3072 N N . LEU B 1 162 ? 67.463 41.627 81.404 1.00 44.00 ? 545 LEU B N 1 ATOM 3073 C CA . LEU B 1 162 ? 66.198 41.013 81.015 1.00 43.91 ? 545 LEU B CA 1 ATOM 3074 C C . LEU B 1 162 ? 64.970 41.899 81.217 1.00 44.62 ? 545 LEU B C 1 ATOM 3075 O O . LEU B 1 162 ? 63.928 41.651 80.609 1.00 46.09 ? 545 LEU B O 1 ATOM 3076 C CB . LEU B 1 162 ? 65.994 39.716 81.799 1.00 43.57 ? 545 LEU B CB 1 ATOM 3077 C CG . LEU B 1 162 ? 67.082 38.653 81.639 1.00 43.32 ? 545 LEU B CG 1 ATOM 3078 C CD1 . LEU B 1 162 ? 66.739 37.456 82.498 1.00 42.19 ? 545 LEU B CD1 1 ATOM 3079 C CD2 . LEU B 1 162 ? 67.274 38.234 80.183 1.00 43.30 ? 545 LEU B CD2 1 ATOM 3080 N N . VAL B 1 163 ? 65.084 42.925 82.055 1.00 45.41 ? 546 VAL B N 1 ATOM 3081 C CA . VAL B 1 163 ? 63.925 43.724 82.460 1.00 46.28 ? 546 VAL B CA 1 ATOM 3082 C C . VAL B 1 163 ? 63.980 45.210 82.065 1.00 46.36 ? 546 VAL B C 1 ATOM 3083 O O . VAL B 1 163 ? 63.095 45.979 82.417 1.00 45.59 ? 546 VAL B O 1 ATOM 3084 C CB . VAL B 1 163 ? 63.661 43.562 83.971 1.00 46.21 ? 546 VAL B CB 1 ATOM 3085 C CG1 . VAL B 1 163 ? 63.287 42.128 84.275 1.00 46.52 ? 546 VAL B CG1 1 ATOM 3086 C CG2 . VAL B 1 163 ? 64.860 43.963 84.810 1.00 46.78 ? 546 VAL B CG2 1 ATOM 3087 N N . LEU B 1 164 ? 64.995 45.596 81.303 1.00 48.11 ? 547 LEU B N 1 ATOM 3088 C CA . LEU B 1 164 ? 65.180 46.982 80.892 1.00 49.41 ? 547 LEU B CA 1 ATOM 3089 C C . LEU B 1 164 ? 65.637 47.020 79.459 1.00 49.48 ? 547 LEU B C 1 ATOM 3090 O O . LEU B 1 164 ? 66.323 46.117 79.009 1.00 50.59 ? 547 LEU B O 1 ATOM 3091 C CB . LEU B 1 164 ? 66.219 47.664 81.776 1.00 49.21 ? 547 LEU B CB 1 ATOM 3092 C CG . LEU B 1 164 ? 65.834 47.743 83.249 1.00 48.83 ? 547 LEU B CG 1 ATOM 3093 C CD1 . LEU B 1 164 ? 67.038 48.089 84.099 1.00 49.72 ? 547 LEU B CD1 1 ATOM 3094 C CD2 . LEU B 1 164 ? 64.722 48.758 83.444 1.00 49.92 ? 547 LEU B CD2 1 ATOM 3095 N N . GLY B 1 165 ? 65.250 48.074 78.752 1.00 50.81 ? 548 GLY B N 1 ATOM 3096 C CA . GLY B 1 165 ? 65.667 48.293 77.370 1.00 52.36 ? 548 GLY B CA 1 ATOM 3097 C C . GLY B 1 165 ? 66.075 49.732 77.115 1.00 53.32 ? 548 GLY B C 1 ATOM 3098 O O . GLY B 1 165 ? 65.661 50.642 77.837 1.00 51.99 ? 548 GLY B O 1 ATOM 3099 N N . GLY B 1 166 ? 66.889 49.917 76.079 1.00 55.27 ? 549 GLY B N 1 ATOM 3100 C CA . GLY B 1 166 ? 67.236 51.237 75.566 1.00 57.92 ? 549 GLY B CA 1 ATOM 3101 C C . GLY B 1 166 ? 68.214 52.024 76.413 1.00 59.78 ? 549 GLY B C 1 ATOM 3102 O O . GLY B 1 166 ? 68.160 53.254 76.447 1.00 63.90 ? 549 GLY B O 1 ATOM 3103 N N . TYR B 1 167 ? 69.119 51.311 77.074 1.00 59.38 ? 550 TYR B N 1 ATOM 3104 C CA . TYR B 1 167 ? 70.150 51.915 77.907 1.00 59.08 ? 550 TYR B CA 1 ATOM 3105 C C . TYR B 1 167 ? 71.480 51.674 77.214 1.00 60.45 ? 550 TYR B C 1 ATOM 3106 O O . TYR B 1 167 ? 71.601 50.784 76.374 1.00 61.28 ? 550 TYR B O 1 ATOM 3107 C CB . TYR B 1 167 ? 70.162 51.318 79.324 1.00 57.52 ? 550 TYR B CB 1 ATOM 3108 C CG . TYR B 1 167 ? 70.346 49.829 79.340 1.00 56.30 ? 550 TYR B CG 1 ATOM 3109 C CD1 . TYR B 1 167 ? 69.246 48.979 79.277 1.00 55.46 ? 550 TYR B CD1 1 ATOM 3110 C CD2 . TYR B 1 167 ? 71.619 49.259 79.384 1.00 56.70 ? 550 TYR B CD2 1 ATOM 3111 C CE1 . TYR B 1 167 ? 69.407 47.607 79.263 1.00 54.93 ? 550 TYR B CE1 1 ATOM 3112 C CE2 . TYR B 1 167 ? 71.787 47.882 79.374 1.00 55.85 ? 550 TYR B CE2 1 ATOM 3113 C CZ . TYR B 1 167 ? 70.680 47.064 79.308 1.00 55.41 ? 550 TYR B CZ 1 ATOM 3114 O OH . TYR B 1 167 ? 70.832 45.701 79.292 1.00 56.23 ? 550 TYR B OH 1 ATOM 3115 N N . ASP B 1 168 ? 72.474 52.461 77.600 1.00 61.76 ? 551 ASP B N 1 ATOM 3116 C CA . ASP B 1 168 ? 73.820 52.392 77.034 1.00 63.10 ? 551 ASP B CA 1 ATOM 3117 C C . ASP B 1 168 ? 74.743 51.638 77.986 1.00 63.48 ? 551 ASP B C 1 ATOM 3118 O O . ASP B 1 168 ? 74.626 51.782 79.204 1.00 62.08 ? 551 ASP B O 1 ATOM 3119 C CB . ASP B 1 168 ? 74.363 53.800 76.796 1.00 63.70 ? 551 ASP B CB 1 ATOM 3120 C CG . ASP B 1 168 ? 74.442 54.614 78.070 1.00 63.00 ? 551 ASP B CG 1 ATOM 3121 O OD1 . ASP B 1 168 ? 73.377 54.886 78.665 1.00 61.59 ? 551 ASP B OD1 1 ATOM 3122 O OD2 . ASP B 1 168 ? 75.566 54.944 78.490 1.00 64.15 ? 551 ASP B OD2 1 ATOM 3123 N N . ASP B 1 169 ? 75.669 50.863 77.419 1.00 66.44 ? 552 ASP B N 1 ATOM 3124 C CA . ASP B 1 169 ? 76.589 50.009 78.185 1.00 68.67 ? 552 ASP B CA 1 ATOM 3125 C C . ASP B 1 169 ? 75.838 49.239 79.296 1.00 65.27 ? 552 ASP B C 1 ATOM 3126 O O . ASP B 1 169 ? 74.874 48.552 78.977 1.00 61.59 ? 552 ASP B O 1 ATOM 3127 C CB . ASP B 1 169 ? 77.788 50.826 78.710 1.00 72.96 ? 552 ASP B CB 1 ATOM 3128 C CG . ASP B 1 169 ? 78.758 51.238 77.609 1.00 77.28 ? 552 ASP B CG 1 ATOM 3129 O OD1 . ASP B 1 169 ? 79.086 50.392 76.746 1.00 80.80 ? 552 ASP B OD1 1 ATOM 3130 O OD2 . ASP B 1 169 ? 79.216 52.403 77.628 1.00 79.50 ? 552 ASP B OD2 1 ATOM 3131 N N . GLN B 1 170 ? 76.245 49.371 80.566 1.00 64.63 ? 553 GLN B N 1 ATOM 3132 C CA . GLN B 1 170 ? 75.521 48.788 81.693 1.00 64.06 ? 553 GLN B CA 1 ATOM 3133 C C . GLN B 1 170 ? 74.981 49.888 82.617 1.00 61.75 ? 553 GLN B C 1 ATOM 3134 O O . GLN B 1 170 ? 74.859 49.693 83.825 1.00 61.13 ? 553 GLN B O 1 ATOM 3135 C CB . GLN B 1 170 ? 76.415 47.799 82.452 1.00 66.67 ? 553 GLN B CB 1 ATOM 3136 C CG . GLN B 1 170 ? 76.878 46.621 81.590 1.00 70.31 ? 553 GLN B CG 1 ATOM 3137 C CD . GLN B 1 170 ? 77.736 45.611 82.343 1.00 72.04 ? 553 GLN B CD 1 ATOM 3138 O OE1 . GLN B 1 170 ? 77.218 44.741 83.042 1.00 72.47 ? 553 GLN B OE1 1 ATOM 3139 N NE2 . GLN B 1 170 ? 79.053 45.718 82.194 1.00 74.58 ? 553 GLN B NE2 1 ATOM 3140 N N . ASN B 1 171 ? 74.623 51.030 82.032 1.00 60.16 ? 554 ASN B N 1 ATOM 3141 C CA . ASN B 1 171 ? 74.033 52.136 82.767 1.00 60.31 ? 554 ASN B CA 1 ATOM 3142 C C . ASN B 1 171 ? 72.518 51.952 82.791 1.00 59.41 ? 554 ASN B C 1 ATOM 3143 O O . ASN B 1 171 ? 71.778 52.653 82.090 1.00 59.11 ? 554 ASN B O 1 ATOM 3144 C CB . ASN B 1 171 ? 74.415 53.471 82.128 1.00 61.87 ? 554 ASN B CB 1 ATOM 3145 C CG . ASN B 1 171 ? 75.896 53.784 82.266 1.00 62.55 ? 554 ASN B CG 1 ATOM 3146 O OD1 . ASN B 1 171 ? 76.468 53.653 83.339 1.00 62.69 ? 554 ASN B OD1 1 ATOM 3147 N ND2 . ASN B 1 171 ? 76.514 54.212 81.182 1.00 63.10 ? 554 ASN B ND2 1 ATOM 3148 N N . TYR B 1 172 ? 72.075 51.005 83.615 1.00 56.63 ? 555 TYR B N 1 ATOM 3149 C CA . TYR B 1 172 ? 70.676 50.556 83.630 1.00 55.20 ? 555 TYR B CA 1 ATOM 3150 C C . TYR B 1 172 ? 69.716 51.679 84.010 1.00 55.26 ? 555 TYR B C 1 ATOM 3151 O O . TYR B 1 172 ? 68.568 51.699 83.576 1.00 54.80 ? 555 TYR B O 1 ATOM 3152 C CB . TYR B 1 172 ? 70.507 49.369 84.581 1.00 53.51 ? 555 TYR B CB 1 ATOM 3153 C CG . TYR B 1 172 ? 71.282 48.143 84.139 1.00 53.04 ? 555 TYR B CG 1 ATOM 3154 C CD1 . TYR B 1 172 ? 70.897 47.423 83.009 1.00 53.02 ? 555 TYR B CD1 1 ATOM 3155 C CD2 . TYR B 1 172 ? 72.397 47.707 84.846 1.00 51.62 ? 555 TYR B CD2 1 ATOM 3156 C CE1 . TYR B 1 172 ? 71.606 46.306 82.596 1.00 53.59 ? 555 TYR B CE1 1 ATOM 3157 C CE2 . TYR B 1 172 ? 73.102 46.598 84.447 1.00 52.65 ? 555 TYR B CE2 1 ATOM 3158 C CZ . TYR B 1 172 ? 72.704 45.894 83.323 1.00 54.21 ? 555 TYR B CZ 1 ATOM 3159 O OH . TYR B 1 172 ? 73.416 44.779 82.927 1.00 56.21 ? 555 TYR B OH 1 ATOM 3160 N N . ASN B 1 173 ? 70.214 52.602 84.824 1.00 56.08 ? 556 ASN B N 1 ATOM 3161 C CA . ASN B 1 173 ? 69.531 53.845 85.148 1.00 56.40 ? 556 ASN B CA 1 ATOM 3162 C C . ASN B 1 173 ? 69.029 54.647 83.934 1.00 56.94 ? 556 ASN B C 1 ATOM 3163 O O . ASN B 1 173 ? 68.004 55.320 84.034 1.00 56.66 ? 556 ASN B O 1 ATOM 3164 C CB . ASN B 1 173 ? 70.447 54.723 86.001 1.00 58.08 ? 556 ASN B CB 1 ATOM 3165 C CG . ASN B 1 173 ? 71.770 55.030 85.310 1.00 59.81 ? 556 ASN B CG 1 ATOM 3166 O OD1 . ASN B 1 173 ? 72.625 54.155 85.168 1.00 60.23 ? 556 ASN B OD1 1 ATOM 3167 N ND2 . ASN B 1 173 ? 71.935 56.268 84.862 1.00 60.43 ? 556 ASN B ND2 1 ATOM 3168 N N . ASN B 1 174 ? 69.719 54.568 82.795 1.00 57.32 ? 557 ASN B N 1 ATOM 3169 C CA . ASN B 1 174 ? 69.296 55.305 81.594 1.00 59.71 ? 557 ASN B CA 1 ATOM 3170 C C . ASN B 1 174 ? 68.301 54.565 80.704 1.00 59.94 ? 557 ASN B C 1 ATOM 3171 O O . ASN B 1 174 ? 68.145 54.915 79.530 1.00 62.96 ? 557 ASN B O 1 ATOM 3172 C CB . ASN B 1 174 ? 70.513 55.713 80.755 1.00 62.25 ? 557 ASN B CB 1 ATOM 3173 C CG . ASN B 1 174 ? 71.443 56.627 81.463 1.00 65.99 ? 557 ASN B CG 1 ATOM 3174 O OD1 . ASN B 1 174 ? 71.044 57.414 82.341 1.00 65.50 ? 557 ASN B OD1 1 ATOM 3175 N ND2 . ASN B 1 174 ? 72.727 56.524 81.067 1.00 69.54 ? 557 ASN B ND2 1 ATOM 3176 N N . ALA B 1 175 ? 67.620 53.558 81.247 1.00 58.29 ? 558 ALA B N 1 ATOM 3177 C CA . ALA B 1 175 ? 66.680 52.754 80.470 1.00 56.50 ? 558 ALA B CA 1 ATOM 3178 C C . ALA B 1 175 ? 65.505 53.603 79.986 1.00 55.03 ? 558 ALA B C 1 ATOM 3179 O O . ALA B 1 175 ? 65.002 54.442 80.729 1.00 53.78 ? 558 ALA B O 1 ATOM 3180 C CB . ALA B 1 175 ? 66.173 51.591 81.309 1.00 55.81 ? 558 ALA B CB 1 ATOM 3181 N N . THR B 1 176 ? 65.101 53.392 78.735 1.00 54.42 ? 559 THR B N 1 ATOM 3182 C CA . THR B 1 176 ? 63.914 54.036 78.171 1.00 54.37 ? 559 THR B CA 1 ATOM 3183 C C . THR B 1 176 ? 62.747 53.066 78.021 1.00 54.12 ? 559 THR B C 1 ATOM 3184 O O . THR B 1 176 ? 61.702 53.444 77.494 1.00 56.07 ? 559 THR B O 1 ATOM 3185 C CB . THR B 1 176 ? 64.230 54.671 76.808 1.00 55.50 ? 559 THR B CB 1 ATOM 3186 O OG1 . THR B 1 176 ? 64.806 53.687 75.949 1.00 55.76 ? 559 THR B OG1 1 ATOM 3187 C CG2 . THR B 1 176 ? 65.215 55.827 76.974 1.00 57.05 ? 559 THR B CG2 1 ATOM 3188 N N . ALA B 1 177 ? 62.908 51.828 78.491 1.00 52.34 ? 560 ALA B N 1 ATOM 3189 C CA . ALA B 1 177 ? 61.845 50.837 78.410 1.00 51.89 ? 560 ALA B CA 1 ATOM 3190 C C . ALA B 1 177 ? 61.975 49.793 79.505 1.00 51.23 ? 560 ALA B C 1 ATOM 3191 O O . ALA B 1 177 ? 63.079 49.428 79.906 1.00 51.27 ? 560 ALA B O 1 ATOM 3192 C CB . ALA B 1 177 ? 61.858 50.159 77.050 1.00 52.31 ? 560 ALA B CB 1 ATOM 3193 N N . LEU B 1 178 ? 60.833 49.336 79.998 1.00 50.12 ? 561 LEU B N 1 ATOM 3194 C CA . LEU B 1 178 ? 60.774 48.208 80.910 1.00 48.44 ? 561 LEU B CA 1 ATOM 3195 C C . LEU B 1 178 ? 60.276 47.008 80.127 1.00 46.71 ? 561 LEU B C 1 ATOM 3196 O O . LEU B 1 178 ? 59.463 47.149 79.212 1.00 46.27 ? 561 LEU B O 1 ATOM 3197 C CB . LEU B 1 178 ? 59.809 48.492 82.052 1.00 48.66 ? 561 LEU B CB 1 ATOM 3198 C CG . LEU B 1 178 ? 59.968 49.806 82.795 1.00 49.51 ? 561 LEU B CG 1 ATOM 3199 C CD1 . LEU B 1 178 ? 58.887 49.897 83.864 1.00 50.30 ? 561 LEU B CD1 1 ATOM 3200 C CD2 . LEU B 1 178 ? 61.345 49.945 83.417 1.00 49.99 ? 561 LEU B CD2 1 ATOM 3201 N N . VAL B 1 179 ? 60.770 45.837 80.495 1.00 46.41 ? 562 VAL B N 1 ATOM 3202 C CA . VAL B 1 179 ? 60.350 44.586 79.901 1.00 45.16 ? 562 VAL B CA 1 ATOM 3203 C C . VAL B 1 179 ? 59.813 43.733 81.042 1.00 45.10 ? 562 VAL B C 1 ATOM 3204 O O . VAL B 1 179 ? 60.472 43.589 82.068 1.00 45.53 ? 562 VAL B O 1 ATOM 3205 C CB . VAL B 1 179 ? 61.513 43.895 79.170 1.00 45.38 ? 562 VAL B CB 1 ATOM 3206 C CG1 . VAL B 1 179 ? 61.048 42.606 78.499 1.00 46.77 ? 562 VAL B CG1 1 ATOM 3207 C CG2 . VAL B 1 179 ? 62.100 44.804 78.109 1.00 45.37 ? 562 VAL B CG2 1 ATOM 3208 N N . ILE B 1 180 ? 58.612 43.188 80.862 1.00 46.48 ? 563 ILE B N 1 ATOM 3209 C CA . ILE B 1 180 ? 57.966 42.336 81.853 1.00 47.16 ? 563 ILE B CA 1 ATOM 3210 C C . ILE B 1 180 ? 57.750 40.970 81.213 1.00 48.44 ? 563 ILE B C 1 ATOM 3211 O O . ILE B 1 180 ? 57.165 40.890 80.139 1.00 48.23 ? 563 ILE B O 1 ATOM 3212 C CB . ILE B 1 180 ? 56.622 42.943 82.291 1.00 49.10 ? 563 ILE B CB 1 ATOM 3213 C CG1 . ILE B 1 180 ? 56.869 44.260 83.031 1.00 50.67 ? 563 ILE B CG1 1 ATOM 3214 C CG2 . ILE B 1 180 ? 55.844 41.993 83.200 1.00 50.04 ? 563 ILE B CG2 1 ATOM 3215 C CD1 . ILE B 1 180 ? 55.603 44.928 83.516 1.00 51.61 ? 563 ILE B CD1 1 ATOM 3216 N N . THR B 1 181 ? 58.183 39.901 81.886 1.00 49.55 ? 564 THR B N 1 ATOM 3217 C CA . THR B 1 181 ? 58.134 38.547 81.320 1.00 50.47 ? 564 THR B CA 1 ATOM 3218 C C . THR B 1 181 ? 57.565 37.514 82.300 1.00 52.12 ? 564 THR B C 1 ATOM 3219 O O . THR B 1 181 ? 58.030 37.402 83.423 1.00 53.21 ? 564 THR B O 1 ATOM 3220 C CB . THR B 1 181 ? 59.527 38.122 80.866 1.00 50.96 ? 564 THR B CB 1 ATOM 3221 O OG1 . THR B 1 181 ? 60.065 39.132 80.013 1.00 49.00 ? 564 THR B OG1 1 ATOM 3222 C CG2 . THR B 1 181 ? 59.467 36.831 80.085 1.00 53.25 ? 564 THR B CG2 1 ATOM 3223 N N . PHE B 1 182 ? 56.525 36.799 81.869 1.00 55.95 ? 565 PHE B N 1 ATOM 3224 C CA . PHE B 1 182 ? 55.857 35.748 82.652 1.00 56.88 ? 565 PHE B CA 1 ATOM 3225 C C . PHE B 1 182 ? 56.118 34.426 81.927 1.00 55.39 ? 565 PHE B C 1 ATOM 3226 O O . PHE B 1 182 ? 55.602 34.230 80.826 1.00 55.63 ? 565 PHE B O 1 ATOM 3227 C CB . PHE B 1 182 ? 54.326 35.940 82.688 1.00 60.75 ? 565 PHE B CB 1 ATOM 3228 C CG . PHE B 1 182 ? 53.871 37.279 83.189 1.00 65.98 ? 565 PHE B CG 1 ATOM 3229 C CD1 . PHE B 1 182 ? 53.738 38.359 82.315 1.00 67.70 ? 565 PHE B CD1 1 ATOM 3230 C CD2 . PHE B 1 182 ? 53.527 37.462 84.535 1.00 69.53 ? 565 PHE B CD2 1 ATOM 3231 C CE1 . PHE B 1 182 ? 53.301 39.601 82.781 1.00 69.69 ? 565 PHE B CE1 1 ATOM 3232 C CE2 . PHE B 1 182 ? 53.089 38.703 85.006 1.00 69.90 ? 565 PHE B CE2 1 ATOM 3233 C CZ . PHE B 1 182 ? 52.980 39.775 84.128 1.00 69.33 ? 565 PHE B CZ 1 ATOM 3234 N N . PRO B 1 183 ? 56.921 33.523 82.512 1.00 52.24 ? 566 PRO B N 1 ATOM 3235 C CA . PRO B 1 183 ? 56.957 32.172 81.955 1.00 52.14 ? 566 PRO B CA 1 ATOM 3236 C C . PRO B 1 183 ? 55.674 31.400 82.271 1.00 52.74 ? 566 PRO B C 1 ATOM 3237 O O . PRO B 1 183 ? 55.224 31.423 83.415 1.00 55.77 ? 566 PRO B O 1 ATOM 3238 C CB . PRO B 1 183 ? 58.164 31.531 82.649 1.00 50.94 ? 566 PRO B CB 1 ATOM 3239 C CG . PRO B 1 183 ? 58.972 32.673 83.146 1.00 50.75 ? 566 PRO B CG 1 ATOM 3240 C CD . PRO B 1 183 ? 57.984 33.729 83.502 1.00 51.15 ? 566 PRO B CD 1 ATOM 3241 N N . VAL B 1 184 ? 55.104 30.739 81.267 1.00 53.36 ? 567 VAL B N 1 ATOM 3242 C CA . VAL B 1 184 ? 53.955 29.838 81.450 1.00 55.52 ? 567 VAL B CA 1 ATOM 3243 C C . VAL B 1 184 ? 54.214 28.505 80.754 1.00 56.78 ? 567 VAL B C 1 ATOM 3244 O O . VAL B 1 184 ? 54.955 28.449 79.765 1.00 54.36 ? 567 VAL B O 1 ATOM 3245 C CB . VAL B 1 184 ? 52.638 30.442 80.927 1.00 56.52 ? 567 VAL B CB 1 ATOM 3246 C CG1 . VAL B 1 184 ? 52.419 31.828 81.526 1.00 57.51 ? 567 VAL B CG1 1 ATOM 3247 C CG2 . VAL B 1 184 ? 52.619 30.510 79.412 1.00 56.93 ? 567 VAL B CG2 1 ATOM 3248 N N . ASN B 1 185 ? 53.617 27.442 81.297 1.00 59.22 ? 568 ASN B N 1 ATOM 3249 C CA . ASN B 1 185 ? 53.799 26.076 80.787 1.00 61.46 ? 568 ASN B CA 1 ATOM 3250 C C . ASN B 1 185 ? 53.378 25.980 79.341 1.00 62.01 ? 568 ASN B C 1 ATOM 3251 O O . ASN B 1 185 ? 52.313 26.452 78.987 1.00 61.10 ? 568 ASN B O 1 ATOM 3252 C CB . ASN B 1 185 ? 52.969 25.060 81.599 1.00 64.01 ? 568 ASN B CB 1 ATOM 3253 C CG . ASN B 1 185 ? 53.757 24.411 82.726 1.00 66.04 ? 568 ASN B CG 1 ATOM 3254 O OD1 . ASN B 1 185 ? 54.571 23.513 82.487 1.00 67.42 ? 568 ASN B OD1 1 ATOM 3255 N ND2 . ASN B 1 185 ? 53.515 24.852 83.963 1.00 66.86 ? 568 ASN B ND2 1 ATOM 3256 N N . ASN B 1 186 ? 54.230 25.390 78.511 1.00 65.32 ? 569 ASN B N 1 ATOM 3257 C CA . ASN B 1 186 ? 53.859 25.024 77.151 1.00 70.14 ? 569 ASN B CA 1 ATOM 3258 C C . ASN B 1 186 ? 52.928 23.828 77.111 1.00 73.07 ? 569 ASN B C 1 ATOM 3259 O O . ASN B 1 186 ? 52.164 23.693 76.156 1.00 75.22 ? 569 ASN B O 1 ATOM 3260 C CB . ASN B 1 186 ? 55.091 24.610 76.321 1.00 71.33 ? 569 ASN B CB 1 ATOM 3261 C CG . ASN B 1 186 ? 55.617 25.726 75.437 1.00 73.18 ? 569 ASN B CG 1 ATOM 3262 O OD1 . ASN B 1 186 ? 56.809 26.092 75.448 1.00 77.15 ? 569 ASN B OD1 1 ATOM 3263 N ND2 . ASN B 1 186 ? 54.725 26.235 74.610 1.00 74.65 ? 569 ASN B ND2 1 ATOM 3264 N N . TYR B 1 187 ? 53.044 22.931 78.091 1.00 76.38 ? 570 TYR B N 1 ATOM 3265 C CA . TYR B 1 187 ? 52.213 21.717 78.175 1.00 79.37 ? 570 TYR B CA 1 ATOM 3266 C C . TYR B 1 187 ? 52.207 20.861 76.870 1.00 81.49 ? 570 TYR B C 1 ATOM 3267 O O . TYR B 1 187 ? 51.165 20.321 76.492 1.00 81.89 ? 570 TYR B O 1 ATOM 3268 C CB . TYR B 1 187 ? 50.766 22.085 78.579 1.00 79.35 ? 570 TYR B CB 1 ATOM 3269 C CG . TYR B 1 187 ? 50.555 22.598 79.997 1.00 78.86 ? 570 TYR B CG 1 ATOM 3270 C CD1 . TYR B 1 187 ? 49.953 23.842 80.230 1.00 77.29 ? 570 TYR B CD1 1 ATOM 3271 C CD2 . TYR B 1 187 ? 50.913 21.821 81.110 1.00 79.40 ? 570 TYR B CD2 1 ATOM 3272 C CE1 . TYR B 1 187 ? 49.734 24.303 81.521 1.00 76.96 ? 570 TYR B CE1 1 ATOM 3273 C CE2 . TYR B 1 187 ? 50.707 22.278 82.411 1.00 78.08 ? 570 TYR B CE2 1 ATOM 3274 C CZ . TYR B 1 187 ? 50.116 23.521 82.609 1.00 78.38 ? 570 TYR B CZ 1 ATOM 3275 O OH . TYR B 1 187 ? 49.910 23.978 83.887 1.00 76.62 ? 570 TYR B OH 1 ATOM 3276 N N . TYR B 1 188 ? 53.356 20.748 76.192 1.00 85.94 ? 571 TYR B N 1 ATOM 3277 C CA . TYR B 1 188 ? 53.468 19.977 74.919 1.00 92.68 ? 571 TYR B CA 1 ATOM 3278 C C . TYR B 1 188 ? 52.943 18.527 74.976 1.00 94.06 ? 571 TYR B C 1 ATOM 3279 O O . TYR B 1 188 ? 52.473 18.016 73.961 1.00 93.00 ? 571 TYR B O 1 ATOM 3280 C CB . TYR B 1 188 ? 54.882 20.041 74.278 1.00 97.29 ? 571 TYR B CB 1 ATOM 3281 C CG . TYR B 1 188 ? 55.167 21.348 73.538 1.00 102.71 ? 571 TYR B CG 1 ATOM 3282 C CD1 . TYR B 1 188 ? 54.348 21.767 72.479 1.00 105.36 ? 571 TYR B CD1 1 ATOM 3283 C CD2 . TYR B 1 188 ? 56.264 22.160 73.880 1.00 104.05 ? 571 TYR B CD2 1 ATOM 3284 C CE1 . TYR B 1 188 ? 54.596 22.950 71.799 1.00 106.72 ? 571 TYR B CE1 1 ATOM 3285 C CE2 . TYR B 1 188 ? 56.520 23.346 73.194 1.00 104.89 ? 571 TYR B CE2 1 ATOM 3286 C CZ . TYR B 1 188 ? 55.684 23.735 72.157 1.00 106.12 ? 571 TYR B CZ 1 ATOM 3287 O OH . TYR B 1 188 ? 55.925 24.904 71.472 1.00 106.15 ? 571 TYR B OH 1 ATOM 3288 N N . ASN B 1 189 ? 52.981 17.892 76.153 1.00 94.46 ? 572 ASN B N 1 ATOM 3289 C CA . ASN B 1 189 ? 52.451 16.529 76.323 1.00 96.46 ? 572 ASN B CA 1 ATOM 3290 C C . ASN B 1 189 ? 51.149 16.442 77.141 1.00 95.21 ? 572 ASN B C 1 ATOM 3291 O O . ASN B 1 189 ? 50.602 15.344 77.282 1.00 97.45 ? 572 ASN B O 1 ATOM 3292 C CB . ASN B 1 189 ? 53.534 15.571 76.861 1.00 99.25 ? 572 ASN B CB 1 ATOM 3293 C CG . ASN B 1 189 ? 54.103 14.656 75.767 1.00 101.97 ? 572 ASN B CG 1 ATOM 3294 O OD1 . ASN B 1 189 ? 54.464 15.113 74.677 1.00 101.60 ? 572 ASN B OD1 1 ATOM 3295 N ND2 . ASN B 1 189 ? 54.169 13.357 76.053 1.00 103.24 ? 572 ASN B ND2 1 ATOM 3296 N N . ASP B 1 190 ? 50.629 17.571 77.638 1.00 92.07 ? 573 ASP B N 1 ATOM 3297 C CA . ASP B 1 190 ? 49.307 17.595 78.278 1.00 91.61 ? 573 ASP B CA 1 ATOM 3298 C C . ASP B 1 190 ? 48.338 18.491 77.500 1.00 92.65 ? 573 ASP B C 1 ATOM 3299 O O . ASP B 1 190 ? 48.397 19.720 77.551 1.00 93.22 ? 573 ASP B O 1 ATOM 3300 C CB . ASP B 1 190 ? 49.391 18.026 79.744 1.00 89.82 ? 573 ASP B CB 1 ATOM 3301 C CG . ASP B 1 190 ? 48.209 17.525 80.566 1.00 91.60 ? 573 ASP B CG 1 ATOM 3302 O OD1 . ASP B 1 190 ? 47.048 17.597 80.092 1.00 94.79 ? 573 ASP B OD1 1 ATOM 3303 O OD2 . ASP B 1 190 ? 48.439 17.033 81.688 1.00 93.49 ? 573 ASP B OD2 1 ATOM 3304 N N . THR B 1 191 ? 47.428 17.842 76.793 1.00 92.08 ? 574 THR B N 1 ATOM 3305 C CA . THR B 1 191 ? 46.486 18.516 75.932 1.00 91.16 ? 574 THR B CA 1 ATOM 3306 C C . THR B 1 191 ? 45.423 19.303 76.707 1.00 93.24 ? 574 THR B C 1 ATOM 3307 O O . THR B 1 191 ? 45.074 20.426 76.324 1.00 95.14 ? 574 THR B O 1 ATOM 3308 C CB . THR B 1 191 ? 45.838 17.475 75.010 1.00 92.53 ? 574 THR B CB 1 ATOM 3309 O OG1 . THR B 1 191 ? 46.814 17.046 74.057 1.00 89.68 ? 574 THR B OG1 1 ATOM 3310 C CG2 . THR B 1 191 ? 44.645 18.030 74.275 1.00 96.77 ? 574 THR B CG2 1 ATOM 3311 N N . GLU B 1 192 ? 44.892 18.708 77.770 1.00 94.81 ? 575 GLU B N 1 ATOM 3312 C CA . GLU B 1 192 ? 43.802 19.327 78.530 1.00 96.59 ? 575 GLU B CA 1 ATOM 3313 C C . GLU B 1 192 ? 44.279 20.558 79.318 1.00 92.73 ? 575 GLU B C 1 ATOM 3314 O O . GLU B 1 192 ? 43.534 21.534 79.462 1.00 90.37 ? 575 GLU B O 1 ATOM 3315 C CB . GLU B 1 192 ? 43.151 18.307 79.481 1.00 99.94 ? 575 GLU B CB 1 ATOM 3316 C CG . GLU B 1 192 ? 42.718 16.970 78.872 1.00 102.92 ? 575 GLU B CG 1 ATOM 3317 C CD . GLU B 1 192 ? 43.601 15.795 79.328 1.00 104.77 ? 575 GLU B CD 1 ATOM 3318 O OE1 . GLU B 1 192 ? 43.051 14.814 79.885 1.00 105.92 ? 575 GLU B OE1 1 ATOM 3319 O OE2 . GLU B 1 192 ? 44.849 15.853 79.147 1.00 100.64 ? 575 GLU B OE2 1 ATOM 3320 N N . LYS B 1 193 ? 45.517 20.507 79.809 1.00 89.88 ? 576 LYS B N 1 ATOM 3321 C CA . LYS B 1 193 ? 46.117 21.631 80.531 1.00 88.51 ? 576 LYS B CA 1 ATOM 3322 C C . LYS B 1 193 ? 46.596 22.742 79.592 1.00 84.64 ? 576 LYS B C 1 ATOM 3323 O O . LYS B 1 193 ? 46.597 23.910 79.979 1.00 84.41 ? 576 LYS B O 1 ATOM 3324 C CB . LYS B 1 193 ? 47.269 21.153 81.428 1.00 90.13 ? 576 LYS B CB 1 ATOM 3325 C CG . LYS B 1 193 ? 46.829 20.215 82.549 1.00 94.14 ? 576 LYS B CG 1 ATOM 3326 C CD . LYS B 1 193 ? 48.003 19.626 83.331 1.00 95.99 ? 576 LYS B CD 1 ATOM 3327 C CE . LYS B 1 193 ? 48.317 20.397 84.602 1.00 96.77 ? 576 LYS B CE 1 ATOM 3328 N NZ . LYS B 1 193 ? 47.408 19.993 85.707 1.00 98.44 ? 576 LYS B NZ 1 ATOM 3329 N N . LEU B 1 194 ? 47.001 22.388 78.373 1.00 81.00 ? 577 LEU B N 1 ATOM 3330 C CA . LEU B 1 194 ? 47.423 23.386 77.383 1.00 79.51 ? 577 LEU B CA 1 ATOM 3331 C C . LEU B 1 194 ? 46.260 24.260 76.935 1.00 78.68 ? 577 LEU B C 1 ATOM 3332 O O . LEU B 1 194 ? 46.397 25.474 76.804 1.00 74.53 ? 577 LEU B O 1 ATOM 3333 C CB . LEU B 1 194 ? 48.045 22.705 76.167 1.00 81.43 ? 577 LEU B CB 1 ATOM 3334 C CG . LEU B 1 194 ? 48.649 23.571 75.044 1.00 83.56 ? 577 LEU B CG 1 ATOM 3335 C CD1 . LEU B 1 194 ? 49.307 24.859 75.539 1.00 84.01 ? 577 LEU B CD1 1 ATOM 3336 C CD2 . LEU B 1 194 ? 49.657 22.736 74.265 1.00 85.04 ? 577 LEU B CD2 1 ATOM 3337 N N . GLN B 1 195 ? 45.119 23.624 76.697 1.00 80.36 ? 578 GLN B N 1 ATOM 3338 C CA . GLN B 1 195 ? 43.888 24.333 76.346 1.00 80.90 ? 578 GLN B CA 1 ATOM 3339 C C . GLN B 1 195 ? 43.500 25.370 77.410 1.00 77.95 ? 578 GLN B C 1 ATOM 3340 O O . GLN B 1 195 ? 43.092 26.483 77.069 1.00 77.22 ? 578 GLN B O 1 ATOM 3341 C CB . GLN B 1 195 ? 42.741 23.332 76.120 1.00 82.88 ? 578 GLN B CB 1 ATOM 3342 C CG . GLN B 1 195 ? 42.862 22.502 74.845 1.00 85.31 ? 578 GLN B CG 1 ATOM 3343 C CD . GLN B 1 195 ? 42.632 23.236 73.531 1.00 88.13 ? 578 GLN B CD 1 ATOM 3344 O OE1 . GLN B 1 195 ? 42.475 24.458 73.482 1.00 90.87 ? 578 GLN B OE1 1 ATOM 3345 N NE2 . GLN B 1 195 ? 42.641 22.474 72.437 1.00 90.40 ? 578 GLN B NE2 1 ATOM 3346 N N . ARG B 1 196 ? 43.647 25.004 78.684 1.00 76.58 ? 579 ARG B N 1 ATOM 3347 C CA . ARG B 1 196 ? 43.419 25.936 79.797 1.00 76.79 ? 579 ARG B CA 1 ATOM 3348 C C . ARG B 1 196 ? 44.406 27.116 79.763 1.00 71.34 ? 579 ARG B C 1 ATOM 3349 O O . ARG B 1 196 ? 44.003 28.263 79.929 1.00 69.80 ? 579 ARG B O 1 ATOM 3350 C CB . ARG B 1 196 ? 43.491 25.211 81.150 1.00 80.85 ? 579 ARG B CB 1 ATOM 3351 C CG . ARG B 1 196 ? 42.344 24.227 81.394 1.00 87.28 ? 579 ARG B CG 1 ATOM 3352 C CD . ARG B 1 196 ? 42.544 23.353 82.637 1.00 90.55 ? 579 ARG B CD 1 ATOM 3353 N NE . ARG B 1 196 ? 42.482 24.123 83.890 1.00 94.14 ? 579 ARG B NE 1 ATOM 3354 C CZ . ARG B 1 196 ? 43.520 24.469 84.672 1.00 94.68 ? 579 ARG B CZ 1 ATOM 3355 N NH1 . ARG B 1 196 ? 44.785 24.119 84.395 1.00 92.55 ? 579 ARG B NH1 1 ATOM 3356 N NH2 . ARG B 1 196 ? 43.282 25.185 85.771 1.00 94.54 ? 579 ARG B NH2 1 ATOM 3357 N N . ALA B 1 197 ? 45.679 26.834 79.506 1.00 66.66 ? 580 ALA B N 1 ATOM 3358 C CA . ALA B 1 197 ? 46.695 27.887 79.403 1.00 65.22 ? 580 ALA B CA 1 ATOM 3359 C C . ALA B 1 197 ? 46.436 28.839 78.243 1.00 65.02 ? 580 ALA B C 1 ATOM 3360 O O . ALA B 1 197 ? 46.621 30.053 78.371 1.00 64.08 ? 580 ALA B O 1 ATOM 3361 C CB . ALA B 1 197 ? 48.082 27.281 79.272 1.00 64.76 ? 580 ALA B CB 1 ATOM 3362 N N . GLN B 1 198 ? 46.002 28.279 77.115 1.00 66.86 ? 581 GLN B N 1 ATOM 3363 C CA . GLN B 1 198 ? 45.636 29.072 75.937 1.00 66.19 ? 581 GLN B CA 1 ATOM 3364 C C . GLN B 1 198 ? 44.387 29.924 76.167 1.00 64.90 ? 581 GLN B C 1 ATOM 3365 O O . GLN B 1 198 ? 44.274 31.025 75.613 1.00 65.87 ? 581 GLN B O 1 ATOM 3366 C CB . GLN B 1 198 ? 45.456 28.170 74.718 1.00 68.65 ? 581 GLN B CB 1 ATOM 3367 C CG . GLN B 1 198 ? 46.774 27.622 74.191 1.00 69.96 ? 581 GLN B CG 1 ATOM 3368 C CD . GLN B 1 198 ? 46.619 26.758 72.949 1.00 74.59 ? 581 GLN B CD 1 ATOM 3369 O OE1 . GLN B 1 198 ? 45.538 26.224 72.664 1.00 80.73 ? 581 GLN B OE1 1 ATOM 3370 N NE2 . GLN B 1 198 ? 47.702 26.609 72.204 1.00 73.95 ? 581 GLN B NE2 1 ATOM 3371 N N . ALA B 1 199 ? 43.458 29.421 76.977 1.00 62.75 ? 582 ALA B N 1 ATOM 3372 C CA . ALA B 1 199 ? 42.305 30.215 77.389 1.00 63.00 ? 582 ALA B CA 1 ATOM 3373 C C . ALA B 1 199 ? 42.744 31.437 78.210 1.00 61.90 ? 582 ALA B C 1 ATOM 3374 O O . ALA B 1 199 ? 42.252 32.547 77.989 1.00 61.01 ? 582 ALA B O 1 ATOM 3375 C CB . ALA B 1 199 ? 41.321 29.368 78.176 1.00 63.44 ? 582 ALA B CB 1 ATOM 3376 N N . TRP B 1 200 ? 43.677 31.222 79.136 1.00 60.61 ? 583 TRP B N 1 ATOM 3377 C CA . TRP B 1 200 ? 44.252 32.308 79.916 1.00 60.69 ? 583 TRP B CA 1 ATOM 3378 C C . TRP B 1 200 ? 44.959 33.332 79.022 1.00 60.56 ? 583 TRP B C 1 ATOM 3379 O O . TRP B 1 200 ? 44.782 34.529 79.206 1.00 58.31 ? 583 TRP B O 1 ATOM 3380 C CB . TRP B 1 200 ? 45.229 31.787 80.994 1.00 59.59 ? 583 TRP B CB 1 ATOM 3381 C CG . TRP B 1 200 ? 45.661 32.892 81.938 1.00 57.45 ? 583 TRP B CG 1 ATOM 3382 C CD1 . TRP B 1 200 ? 45.035 33.278 83.094 1.00 57.90 ? 583 TRP B CD1 1 ATOM 3383 C CD2 . TRP B 1 200 ? 46.774 33.775 81.772 1.00 55.72 ? 583 TRP B CD2 1 ATOM 3384 N NE1 . TRP B 1 200 ? 45.698 34.342 83.663 1.00 57.46 ? 583 TRP B NE1 1 ATOM 3385 C CE2 . TRP B 1 200 ? 46.766 34.671 82.870 1.00 55.89 ? 583 TRP B CE2 1 ATOM 3386 C CE3 . TRP B 1 200 ? 47.780 33.899 80.804 1.00 54.48 ? 583 TRP B CE3 1 ATOM 3387 C CZ2 . TRP B 1 200 ? 47.732 35.669 83.030 1.00 54.05 ? 583 TRP B CZ2 1 ATOM 3388 C CZ3 . TRP B 1 200 ? 48.740 34.901 80.960 1.00 53.75 ? 583 TRP B CZ3 1 ATOM 3389 C CH2 . TRP B 1 200 ? 48.705 35.771 82.066 1.00 53.38 ? 583 TRP B CH2 1 ATOM 3390 N N . GLU B 1 201 ? 45.761 32.850 78.074 1.00 62.86 ? 584 GLU B N 1 ATOM 3391 C CA . GLU B 1 201 ? 46.508 33.732 77.171 1.00 64.94 ? 584 GLU B CA 1 ATOM 3392 C C . GLU B 1 201 ? 45.581 34.638 76.369 1.00 63.89 ? 584 GLU B C 1 ATOM 3393 O O . GLU B 1 201 ? 45.904 35.790 76.118 1.00 63.22 ? 584 GLU B O 1 ATOM 3394 C CB . GLU B 1 201 ? 47.399 32.923 76.212 1.00 69.07 ? 584 GLU B CB 1 ATOM 3395 C CG . GLU B 1 201 ? 48.380 33.789 75.418 1.00 73.60 ? 584 GLU B CG 1 ATOM 3396 C CD . GLU B 1 201 ? 49.206 33.015 74.389 1.00 79.93 ? 584 GLU B CD 1 ATOM 3397 O OE1 . GLU B 1 201 ? 49.337 31.765 74.507 1.00 83.81 ? 584 GLU B OE1 1 ATOM 3398 O OE2 . GLU B 1 201 ? 49.738 33.674 73.455 1.00 83.16 ? 584 GLU B OE2 1 ATOM 3399 N N . LYS B 1 202 ? 44.437 34.103 75.960 1.00 64.15 ? 585 LYS B N 1 ATOM 3400 C CA . LYS B 1 202 ? 43.450 34.883 75.240 1.00 64.56 ? 585 LYS B CA 1 ATOM 3401 C C . LYS B 1 202 ? 42.892 36.037 76.111 1.00 63.32 ? 585 LYS B C 1 ATOM 3402 O O . LYS B 1 202 ? 42.788 37.175 75.646 1.00 62.74 ? 585 LYS B O 1 ATOM 3403 C CB . LYS B 1 202 ? 42.389 33.950 74.613 1.00 66.29 ? 585 LYS B CB 1 ATOM 3404 C CG . LYS B 1 202 ? 42.927 33.329 73.334 1.00 67.31 ? 585 LYS B CG 1 ATOM 3405 C CD . LYS B 1 202 ? 41.835 32.538 72.595 1.00 69.01 ? 585 LYS B CD 1 ATOM 3406 C CE . LYS B 1 202 ? 41.753 31.118 73.102 1.00 69.23 ? 585 LYS B CE 1 ATOM 3407 N NZ . LYS B 1 202 ? 40.616 30.396 72.472 1.00 71.35 ? 585 LYS B NZ 1 ATOM 3408 N N . GLU B 1 203 ? 42.621 35.765 77.384 1.00 63.24 ? 586 GLU B N 1 ATOM 3409 C CA . GLU B 1 203 ? 42.244 36.829 78.334 1.00 65.15 ? 586 GLU B CA 1 ATOM 3410 C C . GLU B 1 203 ? 43.364 37.848 78.582 1.00 61.77 ? 586 GLU B C 1 ATOM 3411 O O . GLU B 1 203 ? 43.098 39.047 78.679 1.00 62.55 ? 586 GLU B O 1 ATOM 3412 C CB . GLU B 1 203 ? 41.772 36.240 79.676 1.00 67.08 ? 586 GLU B CB 1 ATOM 3413 C CG . GLU B 1 203 ? 40.389 35.606 79.615 1.00 70.46 ? 586 GLU B CG 1 ATOM 3414 C CD . GLU B 1 203 ? 39.310 36.584 79.163 1.00 72.74 ? 586 GLU B CD 1 ATOM 3415 O OE1 . GLU B 1 203 ? 39.201 37.668 79.768 1.00 74.15 ? 586 GLU B OE1 1 ATOM 3416 O OE2 . GLU B 1 203 ? 38.583 36.273 78.198 1.00 74.66 ? 586 GLU B OE2 1 ATOM 3417 N N . PHE B 1 204 ? 44.598 37.361 78.681 1.00 57.74 ? 587 PHE B N 1 ATOM 3418 C CA . PHE B 1 204 ? 45.771 38.220 78.835 1.00 55.77 ? 587 PHE B CA 1 ATOM 3419 C C . PHE B 1 204 ? 45.913 39.195 77.673 1.00 55.48 ? 587 PHE B C 1 ATOM 3420 O O . PHE B 1 204 ? 46.154 40.379 77.876 1.00 54.24 ? 587 PHE B O 1 ATOM 3421 C CB . PHE B 1 204 ? 47.047 37.369 78.986 1.00 54.71 ? 587 PHE B CB 1 ATOM 3422 C CG . PHE B 1 204 ? 48.325 38.157 78.905 1.00 52.65 ? 587 PHE B CG 1 ATOM 3423 C CD1 . PHE B 1 204 ? 48.709 38.988 79.951 1.00 51.30 ? 587 PHE B CD1 1 ATOM 3424 C CD2 . PHE B 1 204 ? 49.143 38.072 77.782 1.00 52.03 ? 587 PHE B CD2 1 ATOM 3425 C CE1 . PHE B 1 204 ? 49.884 39.722 79.877 1.00 50.64 ? 587 PHE B CE1 1 ATOM 3426 C CE2 . PHE B 1 204 ? 50.322 38.804 77.704 1.00 51.89 ? 587 PHE B CE2 1 ATOM 3427 C CZ . PHE B 1 204 ? 50.696 39.628 78.754 1.00 50.20 ? 587 PHE B CZ 1 ATOM 3428 N N . ILE B 1 205 ? 45.763 38.688 76.458 1.00 56.77 ? 588 ILE B N 1 ATOM 3429 C CA . ILE B 1 205 ? 45.860 39.532 75.269 1.00 58.71 ? 588 ILE B CA 1 ATOM 3430 C C . ILE B 1 205 ? 44.761 40.611 75.291 1.00 59.44 ? 588 ILE B C 1 ATOM 3431 O O . ILE B 1 205 ? 45.026 41.779 74.988 1.00 57.51 ? 588 ILE B O 1 ATOM 3432 C CB . ILE B 1 205 ? 45.809 38.688 73.975 1.00 59.84 ? 588 ILE B CB 1 ATOM 3433 C CG1 . ILE B 1 205 ? 47.077 37.834 73.865 1.00 59.66 ? 588 ILE B CG1 1 ATOM 3434 C CG2 . ILE B 1 205 ? 45.691 39.582 72.741 1.00 60.92 ? 588 ILE B CG2 1 ATOM 3435 C CD1 . ILE B 1 205 ? 46.944 36.638 72.942 1.00 60.96 ? 588 ILE B CD1 1 ATOM 3436 N N . ASN B 1 206 ? 43.542 40.199 75.651 1.00 60.18 ? 589 ASN B N 1 ATOM 3437 C CA . ASN B 1 206 ? 42.401 41.110 75.773 1.00 60.88 ? 589 ASN B CA 1 ATOM 3438 C C . ASN B 1 206 ? 42.625 42.182 76.826 1.00 60.02 ? 589 ASN B C 1 ATOM 3439 O O . ASN B 1 206 ? 42.332 43.356 76.602 1.00 60.40 ? 589 ASN B O 1 ATOM 3440 C CB . ASN B 1 206 ? 41.123 40.344 76.149 1.00 61.73 ? 589 ASN B CB 1 ATOM 3441 C CG . ASN B 1 206 ? 40.527 39.548 75.013 1.00 61.83 ? 589 ASN B CG 1 ATOM 3442 O OD1 . ASN B 1 206 ? 39.727 38.642 75.258 1.00 60.57 ? 589 ASN B OD1 1 ATOM 3443 N ND2 . ASN B 1 206 ? 40.922 39.848 73.785 1.00 61.97 ? 589 ASN B ND2 1 ATOM 3444 N N . PHE B 1 207 ? 43.124 41.764 77.980 1.00 60.29 ? 590 PHE B N 1 ATOM 3445 C CA . PHE B 1 207 ? 43.402 42.686 79.065 1.00 61.22 ? 590 PHE B CA 1 ATOM 3446 C C . PHE B 1 207 ? 44.397 43.776 78.630 1.00 61.84 ? 590 PHE B C 1 ATOM 3447 O O . PHE B 1 207 ? 44.157 44.963 78.843 1.00 61.78 ? 590 PHE B O 1 ATOM 3448 C CB . PHE B 1 207 ? 43.924 41.939 80.292 1.00 60.92 ? 590 PHE B CB 1 ATOM 3449 C CG . PHE B 1 207 ? 44.133 42.829 81.470 1.00 62.10 ? 590 PHE B CG 1 ATOM 3450 C CD1 . PHE B 1 207 ? 43.086 43.105 82.335 1.00 62.69 ? 590 PHE B CD1 1 ATOM 3451 C CD2 . PHE B 1 207 ? 45.366 43.437 81.684 1.00 62.53 ? 590 PHE B CD2 1 ATOM 3452 C CE1 . PHE B 1 207 ? 43.263 43.956 83.412 1.00 63.25 ? 590 PHE B CE1 1 ATOM 3453 C CE2 . PHE B 1 207 ? 45.552 44.291 82.756 1.00 63.25 ? 590 PHE B CE2 1 ATOM 3454 C CZ . PHE B 1 207 ? 44.498 44.549 83.622 1.00 63.55 ? 590 PHE B CZ 1 ATOM 3455 N N . VAL B 1 208 ? 45.491 43.363 77.997 1.00 62.19 ? 591 VAL B N 1 ATOM 3456 C CA . VAL B 1 208 ? 46.528 44.293 77.561 1.00 62.54 ? 591 VAL B CA 1 ATOM 3457 C C . VAL B 1 208 ? 45.999 45.225 76.474 1.00 63.73 ? 591 VAL B C 1 ATOM 3458 O O . VAL B 1 208 ? 46.246 46.417 76.524 1.00 64.09 ? 591 VAL B O 1 ATOM 3459 C CB . VAL B 1 208 ? 47.792 43.546 77.075 1.00 62.09 ? 591 VAL B CB 1 ATOM 3460 C CG1 . VAL B 1 208 ? 48.788 44.491 76.405 1.00 62.26 ? 591 VAL B CG1 1 ATOM 3461 C CG2 . VAL B 1 208 ? 48.458 42.832 78.239 1.00 60.77 ? 591 VAL B CG2 1 ATOM 3462 N N . LYS B 1 209 ? 45.277 44.676 75.501 1.00 67.67 ? 592 LYS B N 1 ATOM 3463 C CA . LYS B 1 209 ? 44.719 45.481 74.394 1.00 70.57 ? 592 LYS B CA 1 ATOM 3464 C C . LYS B 1 209 ? 43.728 46.574 74.863 1.00 71.36 ? 592 LYS B C 1 ATOM 3465 O O . LYS B 1 209 ? 43.753 47.695 74.349 1.00 70.88 ? 592 LYS B O 1 ATOM 3466 C CB . LYS B 1 209 ? 44.188 44.587 73.249 1.00 72.73 ? 592 LYS B CB 1 ATOM 3467 C CG . LYS B 1 209 ? 45.360 44.088 72.394 1.00 74.40 ? 592 LYS B CG 1 ATOM 3468 C CD . LYS B 1 209 ? 44.947 43.465 71.037 1.00 77.26 ? 592 LYS B CD 1 ATOM 3469 C CE . LYS B 1 209 ? 43.906 42.362 71.180 1.00 77.83 ? 592 LYS B CE 1 ATOM 3470 N NZ . LYS B 1 209 ? 43.946 41.442 70.003 1.00 78.28 ? 592 LYS B NZ 1 ATOM 3471 N N . ASN B 1 210 ? 42.946 46.273 75.898 1.00 71.87 ? 593 ASN B N 1 ATOM 3472 C CA . ASN B 1 210 ? 41.991 47.222 76.474 1.00 74.21 ? 593 ASN B CA 1 ATOM 3473 C C . ASN B 1 210 ? 42.495 48.032 77.683 1.00 71.34 ? 593 ASN B C 1 ATOM 3474 O O . ASN B 1 210 ? 41.739 48.835 78.224 1.00 71.73 ? 593 ASN B O 1 ATOM 3475 C CB . ASN B 1 210 ? 40.708 46.473 76.861 1.00 78.57 ? 593 ASN B CB 1 ATOM 3476 C CG . ASN B 1 210 ? 40.049 45.793 75.665 1.00 83.75 ? 593 ASN B CG 1 ATOM 3477 O OD1 . ASN B 1 210 ? 39.786 46.438 74.641 1.00 86.58 ? 593 ASN B OD1 1 ATOM 3478 N ND2 . ASN B 1 210 ? 39.781 44.488 75.783 1.00 84.27 ? 593 ASN B ND2 1 ATOM 3479 N N . TYR B 1 211 ? 43.745 47.848 78.106 1.00 68.59 ? 594 TYR B N 1 ATOM 3480 C CA . TYR B 1 211 ? 44.259 48.567 79.274 1.00 66.71 ? 594 TYR B CA 1 ATOM 3481 C C . TYR B 1 211 ? 44.422 50.041 78.926 1.00 68.01 ? 594 TYR B C 1 ATOM 3482 O O . TYR B 1 211 ? 45.059 50.367 77.933 1.00 67.01 ? 594 TYR B O 1 ATOM 3483 C CB . TYR B 1 211 ? 45.589 47.983 79.748 1.00 63.71 ? 594 TYR B CB 1 ATOM 3484 C CG . TYR B 1 211 ? 45.989 48.400 81.152 1.00 61.20 ? 594 TYR B CG 1 ATOM 3485 C CD1 . TYR B 1 211 ? 46.909 49.426 81.364 1.00 59.70 ? 594 TYR B CD1 1 ATOM 3486 C CD2 . TYR B 1 211 ? 45.453 47.760 82.266 1.00 60.65 ? 594 TYR B CD2 1 ATOM 3487 C CE1 . TYR B 1 211 ? 47.279 49.806 82.643 1.00 58.28 ? 594 TYR B CE1 1 ATOM 3488 C CE2 . TYR B 1 211 ? 45.811 48.136 83.552 1.00 60.09 ? 594 TYR B CE2 1 ATOM 3489 C CZ . TYR B 1 211 ? 46.728 49.159 83.736 1.00 59.51 ? 594 TYR B CZ 1 ATOM 3490 O OH . TYR B 1 211 ? 47.092 49.524 85.021 1.00 60.46 ? 594 TYR B OH 1 ATOM 3491 N N . LYS B 1 212 ? 43.831 50.910 79.740 1.00 70.64 ? 595 LYS B N 1 ATOM 3492 C CA . LYS B 1 212 ? 43.840 52.350 79.491 1.00 76.31 ? 595 LYS B CA 1 ATOM 3493 C C . LYS B 1 212 ? 44.757 53.040 80.489 1.00 74.51 ? 595 LYS B C 1 ATOM 3494 O O . LYS B 1 212 ? 44.492 53.042 81.695 1.00 76.95 ? 595 LYS B O 1 ATOM 3495 C CB . LYS B 1 212 ? 42.435 52.949 79.636 1.00 81.18 ? 595 LYS B CB 1 ATOM 3496 C CG . LYS B 1 212 ? 41.337 52.299 78.809 1.00 85.51 ? 595 LYS B CG 1 ATOM 3497 C CD . LYS B 1 212 ? 41.508 52.503 77.310 1.00 88.09 ? 595 LYS B CD 1 ATOM 3498 C CE . LYS B 1 212 ? 40.388 51.795 76.547 1.00 91.13 ? 595 LYS B CE 1 ATOM 3499 N NZ . LYS B 1 212 ? 40.560 51.827 75.069 1.00 93.70 ? 595 LYS B NZ 1 ATOM 3500 N N . ASN B 1 213 ? 45.847 53.599 79.988 1.00 71.27 ? 596 ASN B N 1 ATOM 3501 C CA . ASN B 1 213 ? 46.675 54.496 80.778 1.00 69.58 ? 596 ASN B CA 1 ATOM 3502 C C . ASN B 1 213 ? 47.439 55.375 79.806 1.00 68.83 ? 596 ASN B C 1 ATOM 3503 O O . ASN B 1 213 ? 48.308 54.887 79.095 1.00 69.51 ? 596 ASN B O 1 ATOM 3504 C CB . ASN B 1 213 ? 47.634 53.739 81.701 1.00 67.82 ? 596 ASN B CB 1 ATOM 3505 C CG . ASN B 1 213 ? 48.378 54.663 82.655 1.00 66.60 ? 596 ASN B CG 1 ATOM 3506 O OD1 . ASN B 1 213 ? 48.562 55.840 82.374 1.00 65.91 ? 596 ASN B OD1 1 ATOM 3507 N ND2 . ASN B 1 213 ? 48.811 54.127 83.786 1.00 66.50 ? 596 ASN B ND2 1 ATOM 3508 N N . PRO B 1 214 ? 47.115 56.675 79.772 1.00 69.48 ? 597 PRO B N 1 ATOM 3509 C CA . PRO B 1 214 ? 47.843 57.580 78.884 1.00 69.03 ? 597 PRO B CA 1 ATOM 3510 C C . PRO B 1 214 ? 49.343 57.652 79.171 1.00 68.12 ? 597 PRO B C 1 ATOM 3511 O O . PRO B 1 214 ? 50.112 57.968 78.267 1.00 70.14 ? 597 PRO B O 1 ATOM 3512 C CB . PRO B 1 214 ? 47.190 58.950 79.132 1.00 69.69 ? 597 PRO B CB 1 ATOM 3513 C CG . PRO B 1 214 ? 45.998 58.722 79.984 1.00 69.45 ? 597 PRO B CG 1 ATOM 3514 C CD . PRO B 1 214 ? 46.072 57.359 80.567 1.00 69.32 ? 597 PRO B CD 1 ATOM 3515 N N . ASN B 1 215 ? 49.745 57.384 80.413 1.00 66.51 ? 598 ASN B N 1 ATOM 3516 C CA . ASN B 1 215 ? 51.151 57.452 80.811 1.00 65.97 ? 598 ASN B CA 1 ATOM 3517 C C . ASN B 1 215 ? 52.038 56.299 80.324 1.00 63.24 ? 598 ASN B C 1 ATOM 3518 O O . ASN B 1 215 ? 53.257 56.407 80.396 1.00 63.35 ? 598 ASN B O 1 ATOM 3519 C CB . ASN B 1 215 ? 51.265 57.473 82.324 1.00 68.02 ? 598 ASN B CB 1 ATOM 3520 C CG . ASN B 1 215 ? 50.580 58.666 82.964 1.00 70.32 ? 598 ASN B CG 1 ATOM 3521 O OD1 . ASN B 1 215 ? 50.657 59.792 82.477 1.00 71.06 ? 598 ASN B OD1 1 ATOM 3522 N ND2 . ASN B 1 215 ? 49.913 58.415 84.080 1.00 72.54 ? 598 ASN B ND2 1 ATOM 3523 N N . LEU B 1 216 ? 51.444 55.205 79.855 1.00 60.84 ? 599 LEU B N 1 ATOM 3524 C CA . LEU B 1 216 ? 52.200 54.026 79.425 1.00 58.85 ? 599 LEU B CA 1 ATOM 3525 C C . LEU B 1 216 ? 51.829 53.631 78.011 1.00 59.81 ? 599 LEU B C 1 ATOM 3526 O O . LEU B 1 216 ? 50.647 53.631 77.669 1.00 62.42 ? 599 LEU B O 1 ATOM 3527 C CB . LEU B 1 216 ? 51.888 52.838 80.337 1.00 56.40 ? 599 LEU B CB 1 ATOM 3528 C CG . LEU B 1 216 ? 51.993 53.034 81.849 1.00 54.87 ? 599 LEU B CG 1 ATOM 3529 C CD1 . LEU B 1 216 ? 51.452 51.815 82.575 1.00 54.06 ? 599 LEU B CD1 1 ATOM 3530 C CD2 . LEU B 1 216 ? 53.423 53.311 82.267 1.00 54.24 ? 599 LEU B CD2 1 ATOM 3531 N N . THR B 1 217 ? 52.823 53.299 77.190 1.00 59.27 ? 600 THR B N 1 ATOM 3532 C CA . THR B 1 217 ? 52.562 52.550 75.965 1.00 61.45 ? 600 THR B CA 1 ATOM 3533 C C . THR B 1 217 ? 53.026 51.110 76.204 1.00 59.58 ? 600 THR B C 1 ATOM 3534 O O . THR B 1 217 ? 54.194 50.866 76.487 1.00 59.69 ? 600 THR B O 1 ATOM 3535 C CB . THR B 1 217 ? 53.219 53.174 74.712 1.00 63.50 ? 600 THR B CB 1 ATOM 3536 O OG1 . THR B 1 217 ? 54.602 53.407 74.948 1.00 66.50 ? 600 THR B OG1 1 ATOM 3537 C CG2 . THR B 1 217 ? 52.557 54.500 74.363 1.00 65.94 ? 600 THR B CG2 1 ATOM 3538 N N . ILE B 1 218 ? 52.081 50.179 76.121 1.00 58.29 ? 601 ILE B N 1 ATOM 3539 C CA . ILE B 1 218 ? 52.308 48.770 76.382 1.00 58.36 ? 601 ILE B CA 1 ATOM 3540 C C . ILE B 1 218 ? 52.288 48.039 75.048 1.00 58.68 ? 601 ILE B C 1 ATOM 3541 O O . ILE B 1 218 ? 51.323 48.162 74.313 1.00 58.01 ? 601 ILE B O 1 ATOM 3542 C CB . ILE B 1 218 ? 51.195 48.205 77.295 1.00 58.71 ? 601 ILE B CB 1 ATOM 3543 C CG1 . ILE B 1 218 ? 51.134 48.989 78.617 1.00 59.35 ? 601 ILE B CG1 1 ATOM 3544 C CG2 . ILE B 1 218 ? 51.423 46.723 77.572 1.00 58.23 ? 601 ILE B CG2 1 ATOM 3545 C CD1 . ILE B 1 218 ? 49.892 48.734 79.449 1.00 59.98 ? 601 ILE B CD1 1 ATOM 3546 N N . SER B 1 219 ? 53.331 47.260 74.756 1.00 58.54 ? 602 SER B N 1 ATOM 3547 C CA . SER B 1 219 ? 53.399 46.460 73.528 1.00 59.83 ? 602 SER B CA 1 ATOM 3548 C C . SER B 1 219 ? 53.753 45.017 73.811 1.00 59.56 ? 602 SER B C 1 ATOM 3549 O O . SER B 1 219 ? 54.445 44.729 74.777 1.00 59.49 ? 602 SER B O 1 ATOM 3550 C CB . SER B 1 219 ? 54.454 47.021 72.590 1.00 60.68 ? 602 SER B CB 1 ATOM 3551 O OG . SER B 1 219 ? 54.296 48.413 72.460 1.00 64.02 ? 602 SER B OG 1 ATOM 3552 N N . PHE B 1 220 ? 53.277 44.116 72.960 1.00 62.28 ? 603 PHE B N 1 ATOM 3553 C CA . PHE B 1 220 ? 53.764 42.743 72.937 1.00 64.57 ? 603 PHE B CA 1 ATOM 3554 C C . PHE B 1 220 ? 55.081 42.723 72.188 1.00 68.62 ? 603 PHE B C 1 ATOM 3555 O O . PHE B 1 220 ? 55.278 43.500 71.268 1.00 70.05 ? 603 PHE B O 1 ATOM 3556 C CB . PHE B 1 220 ? 52.775 41.827 72.238 1.00 64.70 ? 603 PHE B CB 1 ATOM 3557 C CG . PHE B 1 220 ? 51.420 41.821 72.864 1.00 65.29 ? 603 PHE B CG 1 ATOM 3558 C CD1 . PHE B 1 220 ? 50.366 42.511 72.275 1.00 65.84 ? 603 PHE B CD1 1 ATOM 3559 C CD2 . PHE B 1 220 ? 51.200 41.131 74.057 1.00 64.67 ? 603 PHE B CD2 1 ATOM 3560 C CE1 . PHE B 1 220 ? 49.114 42.510 72.853 1.00 66.93 ? 603 PHE B CE1 1 ATOM 3561 C CE2 . PHE B 1 220 ? 49.951 41.129 74.645 1.00 65.62 ? 603 PHE B CE2 1 ATOM 3562 C CZ . PHE B 1 220 ? 48.905 41.821 74.039 1.00 67.65 ? 603 PHE B CZ 1 ATOM 3563 N N . THR B 1 221 ? 55.992 41.852 72.598 1.00 76.07 ? 604 THR B N 1 ATOM 3564 C CA . THR B 1 221 ? 57.268 41.721 71.916 1.00 85.07 ? 604 THR B CA 1 ATOM 3565 C C . THR B 1 221 ? 57.115 40.768 70.752 1.00 95.28 ? 604 THR B C 1 ATOM 3566 O O . THR B 1 221 ? 56.350 39.803 70.815 1.00 97.04 ? 604 THR B O 1 ATOM 3567 C CB . THR B 1 221 ? 58.372 41.234 72.863 1.00 85.16 ? 604 THR B CB 1 ATOM 3568 O OG1 . THR B 1 221 ? 57.980 40.003 73.472 1.00 83.90 ? 604 THR B OG1 1 ATOM 3569 C CG2 . THR B 1 221 ? 58.602 42.273 73.933 1.00 85.37 ? 604 THR B CG2 1 ATOM 3570 N N . ALA B 1 222 ? 57.863 41.038 69.688 1.00 104.79 ? 605 ALA B N 1 ATOM 3571 C CA . ALA B 1 222 ? 57.730 40.267 68.455 1.00 111.33 ? 605 ALA B CA 1 ATOM 3572 C C . ALA B 1 222 ? 58.242 38.834 68.653 1.00 111.48 ? 605 ALA B C 1 ATOM 3573 O O . ALA B 1 222 ? 59.389 38.654 69.069 1.00 112.45 ? 605 ALA B O 1 ATOM 3574 C CB . ALA B 1 222 ? 58.500 40.946 67.338 1.00 114.12 ? 605 ALA B CB 1 ATOM 3575 N N . GLU B 1 223 ? 57.385 37.841 68.391 1.00 112.44 ? 606 GLU B N 1 ATOM 3576 C CA . GLU B 1 223 ? 57.778 36.422 68.368 1.00 114.38 ? 606 GLU B CA 1 ATOM 3577 C C . GLU B 1 223 ? 57.664 35.896 66.938 1.00 115.66 ? 606 GLU B C 1 ATOM 3578 O O . GLU B 1 223 ? 58.430 35.027 66.522 1.00 114.83 ? 606 GLU B O 1 ATOM 3579 C CB . GLU B 1 223 ? 56.897 35.585 69.303 1.00 114.18 ? 606 GLU B CB 1 ATOM 3580 C CG . GLU B 1 223 ? 57.444 34.186 69.587 1.00 114.53 ? 606 GLU B CG 1 ATOM 3581 C CD . GLU B 1 223 ? 56.402 33.245 70.176 1.00 114.33 ? 606 GLU B CD 1 ATOM 3582 O OE1 . GLU B 1 223 ? 56.240 32.126 69.642 1.00 113.08 ? 606 GLU B OE1 1 ATOM 3583 O OE2 . GLU B 1 223 ? 55.742 33.625 71.168 1.00 113.12 ? 606 GLU B OE2 1 HETATM 3584 C C1 . NAG C 2 . ? 61.752 23.538 107.143 1.00 97.44 ? 701 NAG A C1 1 HETATM 3585 C C2 . NAG C 2 . ? 62.140 23.809 108.595 1.00 102.91 ? 701 NAG A C2 1 HETATM 3586 C C3 . NAG C 2 . ? 61.508 22.747 109.511 1.00 105.80 ? 701 NAG A C3 1 HETATM 3587 C C4 . NAG C 2 . ? 60.016 22.464 109.246 1.00 110.08 ? 701 NAG A C4 1 HETATM 3588 C C5 . NAG C 2 . ? 59.670 22.499 107.752 1.00 106.99 ? 701 NAG A C5 1 HETATM 3589 C C6 . NAG C 2 . ? 58.184 22.668 107.444 1.00 107.58 ? 701 NAG A C6 1 HETATM 3590 C C7 . NAG C 2 . ? 64.375 24.779 108.223 1.00 101.91 ? 701 NAG A C7 1 HETATM 3591 C C8 . NAG C 2 . ? 65.848 24.634 108.485 1.00 100.80 ? 701 NAG A C8 1 HETATM 3592 N N2 . NAG C 2 . ? 63.590 23.830 108.749 1.00 102.32 ? 701 NAG A N2 1 HETATM 3593 O O3 . NAG C 2 . ? 61.669 23.156 110.874 1.00 104.31 ? 701 NAG A O3 1 HETATM 3594 O O4 . NAG C 2 . ? 59.712 21.144 109.743 1.00 122.63 ? 701 NAG A O4 1 HETATM 3595 O O5 . NAG C 2 . ? 60.327 23.598 107.135 1.00 102.90 ? 701 NAG A O5 1 HETATM 3596 O O6 . NAG C 2 . ? 57.514 21.405 107.510 1.00 107.69 ? 701 NAG A O6 1 HETATM 3597 O O7 . NAG C 2 . ? 63.941 25.713 107.566 1.00 101.57 ? 701 NAG A O7 1 HETATM 3598 C C1 . NAG D 2 . ? 58.535 20.980 110.582 1.00 129.00 ? 702 NAG A C1 1 HETATM 3599 C C2 . NAG D 2 . ? 58.946 21.148 112.049 1.00 130.43 ? 702 NAG A C2 1 HETATM 3600 C C3 . NAG D 2 . ? 57.752 21.133 113.012 1.00 131.34 ? 702 NAG A C3 1 HETATM 3601 C C4 . NAG D 2 . ? 56.540 21.904 112.484 1.00 131.85 ? 702 NAG A C4 1 HETATM 3602 C C5 . NAG D 2 . ? 56.246 21.529 111.032 1.00 131.33 ? 702 NAG A C5 1 HETATM 3603 C C6 . NAG D 2 . ? 55.025 22.226 110.421 1.00 130.37 ? 702 NAG A C6 1 HETATM 3604 C C7 . NAG D 2 . ? 61.105 20.251 112.893 1.00 128.73 ? 702 NAG A C7 1 HETATM 3605 C C8 . NAG D 2 . ? 61.875 18.989 113.159 1.00 127.47 ? 702 NAG A C8 1 HETATM 3606 N N2 . NAG D 2 . ? 59.874 20.072 112.390 1.00 128.99 ? 702 NAG A N2 1 HETATM 3607 O O3 . NAG D 2 . ? 58.155 21.710 114.260 1.00 129.22 ? 702 NAG A O3 1 HETATM 3608 O O4 . NAG D 2 . ? 55.389 21.628 113.292 1.00 131.82 ? 702 NAG A O4 1 HETATM 3609 O O5 . NAG D 2 . ? 57.415 21.821 110.262 1.00 131.96 ? 702 NAG A O5 1 HETATM 3610 O O6 . NAG D 2 . ? 54.639 23.404 111.141 1.00 127.36 ? 702 NAG A O6 1 HETATM 3611 O O7 . NAG D 2 . ? 61.598 21.345 113.131 1.00 126.71 ? 702 NAG A O7 1 HETATM 3612 C C1 . NAG E 2 . ? 61.935 7.567 82.561 1.00 65.08 ? 703 NAG A C1 1 HETATM 3613 C C2 . NAG E 2 . ? 61.943 6.030 82.299 1.00 69.54 ? 703 NAG A C2 1 HETATM 3614 C C3 . NAG E 2 . ? 60.706 5.282 82.792 1.00 71.03 ? 703 NAG A C3 1 HETATM 3615 C C4 . NAG E 2 . ? 60.314 5.664 84.213 1.00 72.37 ? 703 NAG A C4 1 HETATM 3616 C C5 . NAG E 2 . ? 60.110 7.182 84.332 1.00 69.83 ? 703 NAG A C5 1 HETATM 3617 C C6 . NAG E 2 . ? 60.384 7.679 85.752 1.00 67.54 ? 703 NAG A C6 1 HETATM 3618 C C7 . NAG E 2 . ? 63.302 5.321 80.382 1.00 73.44 ? 703 NAG A C7 1 HETATM 3619 C C8 . NAG E 2 . ? 63.335 5.177 78.888 1.00 74.10 ? 703 NAG A C8 1 HETATM 3620 N N2 . NAG E 2 . ? 62.158 5.812 80.877 1.00 71.94 ? 703 NAG A N2 1 HETATM 3621 O O3 . NAG E 2 . ? 60.996 3.880 82.786 1.00 69.52 ? 703 NAG A O3 1 HETATM 3622 O O4 . NAG E 2 . ? 59.081 4.981 84.545 1.00 77.87 ? 703 NAG A O4 1 HETATM 3623 O O5 . NAG E 2 . ? 60.867 8.014 83.419 1.00 66.92 ? 703 NAG A O5 1 HETATM 3624 O O6 . NAG E 2 . ? 59.240 7.490 86.584 1.00 69.17 ? 703 NAG A O6 1 HETATM 3625 O O7 . NAG E 2 . ? 64.261 5.002 81.076 1.00 71.11 ? 703 NAG A O7 1 HETATM 3626 C C1 . NAG F 2 . ? 59.120 4.065 85.667 1.00 83.07 ? 704 NAG A C1 1 HETATM 3627 C C2 . NAG F 2 . ? 57.681 3.783 86.092 1.00 86.20 ? 704 NAG A C2 1 HETATM 3628 C C3 . NAG F 2 . ? 57.586 2.753 87.216 1.00 91.29 ? 704 NAG A C3 1 HETATM 3629 C C4 . NAG F 2 . ? 58.355 1.473 86.904 1.00 93.49 ? 704 NAG A C4 1 HETATM 3630 C C5 . NAG F 2 . ? 59.762 1.844 86.426 1.00 92.40 ? 704 NAG A C5 1 HETATM 3631 C C6 . NAG F 2 . ? 60.512 0.604 85.949 1.00 93.30 ? 704 NAG A C6 1 HETATM 3632 C C7 . NAG F 2 . ? 55.948 5.541 85.981 1.00 82.24 ? 704 NAG A C7 1 HETATM 3633 C C8 . NAG F 2 . ? 55.443 6.799 86.621 1.00 81.90 ? 704 NAG A C8 1 HETATM 3634 N N2 . NAG F 2 . ? 57.035 5.006 86.550 1.00 83.88 ? 704 NAG A N2 1 HETATM 3635 O O3 . NAG F 2 . ? 56.203 2.482 87.466 1.00 92.47 ? 704 NAG A O3 1 HETATM 3636 O O4 . NAG F 2 . ? 58.465 0.681 88.109 1.00 102.63 ? 704 NAG A O4 1 HETATM 3637 O O5 . NAG F 2 . ? 59.739 2.812 85.359 1.00 87.79 ? 704 NAG A O5 1 HETATM 3638 O O6 . NAG F 2 . ? 61.845 0.964 85.573 1.00 95.83 ? 704 NAG A O6 1 HETATM 3639 O O7 . NAG F 2 . ? 55.388 5.071 85.003 1.00 81.58 ? 704 NAG A O7 1 HETATM 3640 C C1 . BMA G 3 . ? 57.717 -0.554 88.349 1.00 111.97 ? 705 BMA A C1 1 HETATM 3641 C C2 . BMA G 3 . ? 56.379 -0.753 87.625 1.00 115.23 ? 705 BMA A C2 1 HETATM 3642 C C3 . BMA G 3 . ? 55.640 -1.916 88.280 1.00 115.80 ? 705 BMA A C3 1 HETATM 3643 C C4 . BMA G 3 . ? 56.495 -3.185 88.242 1.00 118.39 ? 705 BMA A C4 1 HETATM 3644 C C5 . BMA G 3 . ? 57.933 -2.931 88.714 1.00 121.71 ? 705 BMA A C5 1 HETATM 3645 C C6 . BMA G 3 . ? 58.833 -4.127 88.400 1.00 123.93 ? 705 BMA A C6 1 HETATM 3646 O O2 . BMA G 3 . ? 56.565 -1.069 86.239 1.00 117.48 ? 705 BMA A O2 1 HETATM 3647 O O3 . BMA G 3 . ? 54.386 -2.134 87.622 1.00 111.00 ? 705 BMA A O3 1 HETATM 3648 O O4 . BMA G 3 . ? 55.883 -4.172 89.080 1.00 120.80 ? 705 BMA A O4 1 HETATM 3649 O O5 . BMA G 3 . ? 58.489 -1.743 88.114 1.00 117.34 ? 705 BMA A O5 1 HETATM 3650 O O6 . BMA G 3 . ? 59.975 -4.088 89.274 1.00 128.21 ? 705 BMA A O6 1 HETATM 3651 C C1 . MAN H 4 . ? 60.949 -5.147 89.078 1.00 133.23 ? 706 MAN A C1 1 HETATM 3652 C C2 . MAN H 4 . ? 61.704 -4.945 87.747 1.00 135.20 ? 706 MAN A C2 1 HETATM 3653 C C3 . MAN H 4 . ? 61.329 -5.933 86.642 1.00 136.98 ? 706 MAN A C3 1 HETATM 3654 C C4 . MAN H 4 . ? 61.297 -7.345 87.200 1.00 138.18 ? 706 MAN A C4 1 HETATM 3655 C C5 . MAN H 4 . ? 60.204 -7.421 88.259 1.00 139.17 ? 706 MAN A C5 1 HETATM 3656 C C6 . MAN H 4 . ? 60.146 -8.824 88.864 1.00 139.57 ? 706 MAN A C6 1 HETATM 3657 O O2 . MAN H 4 . ? 63.111 -5.045 88.005 1.00 137.83 ? 706 MAN A O2 1 HETATM 3658 O O3 . MAN H 4 . ? 62.261 -5.861 85.555 1.00 134.08 ? 706 MAN A O3 1 HETATM 3659 O O4 . MAN H 4 . ? 61.058 -8.281 86.140 1.00 135.96 ? 706 MAN A O4 1 HETATM 3660 O O5 . MAN H 4 . ? 60.410 -6.468 89.319 1.00 136.48 ? 706 MAN A O5 1 HETATM 3661 O O6 . MAN H 4 . ? 59.077 -8.910 89.812 1.00 142.05 ? 706 MAN A O6 1 HETATM 3662 C C1 . NAG I 2 . ? 84.126 49.936 80.674 1.00 112.49 ? 707 NAG A C1 1 HETATM 3663 C C2 . NAG I 2 . ? 83.259 49.687 81.896 1.00 116.15 ? 707 NAG A C2 1 HETATM 3664 C C3 . NAG I 2 . ? 83.469 50.763 82.947 1.00 116.39 ? 707 NAG A C3 1 HETATM 3665 C C4 . NAG I 2 . ? 84.947 50.802 83.311 1.00 119.28 ? 707 NAG A C4 1 HETATM 3666 C C5 . NAG I 2 . ? 85.823 50.925 82.055 1.00 122.05 ? 707 NAG A C5 1 HETATM 3667 C C6 . NAG I 2 . ? 87.301 50.838 82.434 1.00 125.75 ? 707 NAG A C6 1 HETATM 3668 C C7 . NAG I 2 . ? 81.003 48.792 81.861 1.00 117.55 ? 707 NAG A C7 1 HETATM 3669 C C8 . NAG I 2 . ? 79.667 48.986 81.243 1.00 117.11 ? 707 NAG A C8 1 HETATM 3670 N N2 . NAG I 2 . ? 81.891 49.682 81.450 1.00 116.36 ? 707 NAG A N2 1 HETATM 3671 O O3 . NAG I 2 . ? 82.661 50.492 84.099 1.00 113.06 ? 707 NAG A O3 1 HETATM 3672 O O4 . NAG I 2 . ? 85.176 51.907 84.192 1.00 118.16 ? 707 NAG A O4 1 HETATM 3673 O O5 . NAG I 2 . ? 85.501 49.915 81.077 1.00 117.74 ? 707 NAG A O5 1 HETATM 3674 O O6 . NAG I 2 . ? 88.116 50.715 81.261 1.00 128.16 ? 707 NAG A O6 1 HETATM 3675 O O7 . NAG I 2 . ? 81.226 47.894 82.658 1.00 120.18 ? 707 NAG A O7 1 HETATM 3676 C C1 . NAG J 2 . ? 85.946 5.468 89.313 1.00 78.86 ? 708 NAG A C1 1 HETATM 3677 C C2 . NAG J 2 . ? 86.744 6.297 90.318 1.00 81.01 ? 708 NAG A C2 1 HETATM 3678 C C3 . NAG J 2 . ? 87.293 5.424 91.433 1.00 83.45 ? 708 NAG A C3 1 HETATM 3679 C C4 . NAG J 2 . ? 86.238 4.554 92.108 1.00 87.75 ? 708 NAG A C4 1 HETATM 3680 C C5 . NAG J 2 . ? 85.361 3.862 91.052 1.00 86.47 ? 708 NAG A C5 1 HETATM 3681 C C6 . NAG J 2 . ? 84.077 3.236 91.596 1.00 88.35 ? 708 NAG A C6 1 HETATM 3682 C C7 . NAG J 2 . ? 88.182 8.256 89.868 1.00 83.97 ? 708 NAG A C7 1 HETATM 3683 C C8 . NAG J 2 . ? 89.376 8.745 89.103 1.00 85.42 ? 708 NAG A C8 1 HETATM 3684 N N2 . NAG J 2 . ? 87.856 6.973 89.668 1.00 81.82 ? 708 NAG A N2 1 HETATM 3685 O O3 . NAG J 2 . ? 87.900 6.267 92.415 1.00 82.80 ? 708 NAG A O3 1 HETATM 3686 O O4 . NAG J 2 . ? 87.032 3.632 92.879 1.00 100.06 ? 708 NAG A O4 1 HETATM 3687 O O5 . NAG J 2 . ? 84.925 4.779 90.040 1.00 83.84 ? 708 NAG A O5 1 HETATM 3688 O O6 . NAG J 2 . ? 83.278 4.198 92.297 1.00 88.21 ? 708 NAG A O6 1 HETATM 3689 O O7 . NAG J 2 . ? 87.572 9.008 90.612 1.00 85.54 ? 708 NAG A O7 1 HETATM 3690 C C1 . NAG K 2 . ? 86.618 3.060 94.153 1.00 112.49 ? 709 NAG A C1 1 HETATM 3691 C C2 . NAG K 2 . ? 85.809 3.951 95.125 1.00 115.98 ? 709 NAG A C2 1 HETATM 3692 C C3 . NAG K 2 . ? 85.229 3.155 96.310 1.00 120.30 ? 709 NAG A C3 1 HETATM 3693 C C4 . NAG K 2 . ? 84.797 1.724 95.983 1.00 120.91 ? 709 NAG A C4 1 HETATM 3694 C C5 . NAG K 2 . ? 85.830 1.022 95.108 1.00 121.76 ? 709 NAG A C5 1 HETATM 3695 C C6 . NAG K 2 . ? 85.452 -0.412 94.740 1.00 123.41 ? 709 NAG A C6 1 HETATM 3696 C C7 . NAG K 2 . ? 86.213 6.077 96.344 1.00 116.06 ? 709 NAG A C7 1 HETATM 3697 C C8 . NAG K 2 . ? 87.251 7.064 96.798 1.00 114.60 ? 709 NAG A C8 1 HETATM 3698 N N2 . NAG K 2 . ? 86.662 5.023 95.644 1.00 116.74 ? 709 NAG A N2 1 HETATM 3699 O O3 . NAG K 2 . ? 84.070 3.825 96.828 1.00 121.51 ? 709 NAG A O3 1 HETATM 3700 O O4 . NAG K 2 . ? 84.606 0.996 97.203 1.00 122.33 ? 709 NAG A O4 1 HETATM 3701 O O5 . NAG K 2 . ? 85.968 1.805 93.924 1.00 117.72 ? 709 NAG A O5 1 HETATM 3702 O O6 . NAG K 2 . ? 84.145 -0.456 94.147 1.00 124.01 ? 709 NAG A O6 1 HETATM 3703 O O7 . NAG K 2 . ? 85.037 6.254 96.614 1.00 116.73 ? 709 NAG A O7 1 HETATM 3704 C C1 . NAG L 2 . ? 78.723 30.722 99.591 1.00 90.76 ? 710 NAG A C1 1 HETATM 3705 C C2 . NAG L 2 . ? 77.918 31.283 100.755 1.00 102.62 ? 710 NAG A C2 1 HETATM 3706 C C3 . NAG L 2 . ? 78.262 30.520 102.038 1.00 106.75 ? 710 NAG A C3 1 HETATM 3707 C C4 . NAG L 2 . ? 78.065 29.015 101.858 1.00 110.80 ? 710 NAG A C4 1 HETATM 3708 C C5 . NAG L 2 . ? 78.809 28.552 100.605 1.00 107.60 ? 710 NAG A C5 1 HETATM 3709 C C6 . NAG L 2 . ? 78.558 27.087 100.271 1.00 110.07 ? 710 NAG A C6 1 HETATM 3710 C C7 . NAG L 2 . ? 77.320 33.682 100.709 1.00 105.33 ? 710 NAG A C7 1 HETATM 3711 C C8 . NAG L 2 . ? 77.851 35.078 100.870 1.00 104.88 ? 710 NAG A C8 1 HETATM 3712 N N2 . NAG L 2 . ? 78.220 32.704 100.873 1.00 104.78 ? 710 NAG A N2 1 HETATM 3713 O O3 . NAG L 2 . ? 77.455 30.980 103.126 1.00 107.92 ? 710 NAG A O3 1 HETATM 3714 O O4 . NAG L 2 . ? 78.586 28.315 103.007 1.00 121.92 ? 710 NAG A O4 1 HETATM 3715 O O5 . NAG L 2 . ? 78.408 29.337 99.480 1.00 96.88 ? 710 NAG A O5 1 HETATM 3716 O O6 . NAG L 2 . ? 79.494 26.667 99.268 1.00 113.12 ? 710 NAG A O6 1 HETATM 3717 O O7 . NAG L 2 . ? 76.141 33.481 100.460 1.00 102.78 ? 710 NAG A O7 1 HETATM 3718 C C1 . NAG M 2 . ? 77.600 27.603 103.790 1.00 128.36 ? 711 NAG A C1 1 HETATM 3719 C C2 . NAG M 2 . ? 78.290 26.469 104.544 1.00 132.12 ? 711 NAG A C2 1 HETATM 3720 C C3 . NAG M 2 . ? 77.311 25.744 105.463 1.00 133.06 ? 711 NAG A C3 1 HETATM 3721 C C4 . NAG M 2 . ? 76.570 26.724 106.366 1.00 134.81 ? 711 NAG A C4 1 HETATM 3722 C C5 . NAG M 2 . ? 75.959 27.877 105.561 1.00 133.69 ? 711 NAG A C5 1 HETATM 3723 C C6 . NAG M 2 . ? 75.403 28.979 106.464 1.00 133.70 ? 711 NAG A C6 1 HETATM 3724 C C7 . NAG M 2 . ? 80.162 25.352 103.358 1.00 143.75 ? 711 NAG A C7 1 HETATM 3725 C C8 . NAG M 2 . ? 80.503 24.282 102.356 1.00 142.01 ? 711 NAG A C8 1 HETATM 3726 N N2 . NAG M 2 . ? 78.854 25.499 103.614 1.00 139.11 ? 711 NAG A N2 1 HETATM 3727 O O3 . NAG M 2 . ? 78.015 24.788 106.269 1.00 129.32 ? 711 NAG A O3 1 HETATM 3728 O O4 . NAG M 2 . ? 75.551 26.008 107.075 1.00 135.10 ? 711 NAG A O4 1 HETATM 3729 O O5 . NAG M 2 . ? 76.941 28.481 104.707 1.00 130.95 ? 711 NAG A O5 1 HETATM 3730 O O6 . NAG M 2 . ? 74.610 28.441 107.530 1.00 133.78 ? 711 NAG A O6 1 HETATM 3731 O O7 . NAG M 2 . ? 81.039 26.026 103.879 1.00 146.20 ? 711 NAG A O7 1 HETATM 3732 S S . SCN N 5 . ? 79.590 40.460 91.307 1.00 99.94 ? 712 SCN A S 1 HETATM 3733 C C . SCN N 5 . ? 79.584 40.351 89.616 1.00 101.83 ? 712 SCN A C 1 HETATM 3734 N N . SCN N 5 . ? 79.587 40.282 88.455 1.00 94.78 ? 712 SCN A N 1 HETATM 3735 S S . SCN O 5 . ? 66.299 15.697 76.010 1.00 96.27 ? 713 SCN A S 1 HETATM 3736 C C . SCN O 5 . ? 65.345 17.093 75.936 1.00 94.13 ? 713 SCN A C 1 HETATM 3737 N N . SCN O 5 . ? 64.689 18.051 75.893 1.00 88.74 ? 713 SCN A N 1 HETATM 3738 C C1 . NAG P 2 . ? 55.322 35.211 98.063 1.00 82.16 ? 701 NAG B C1 1 HETATM 3739 C C2 . NAG P 2 . ? 56.084 34.687 99.278 1.00 94.24 ? 701 NAG B C2 1 HETATM 3740 C C3 . NAG P 2 . ? 55.664 35.466 100.525 1.00 97.61 ? 701 NAG B C3 1 HETATM 3741 C C4 . NAG P 2 . ? 55.837 36.972 100.300 1.00 98.09 ? 701 NAG B C4 1 HETATM 3742 C C5 . NAG P 2 . ? 55.068 37.365 99.039 1.00 95.94 ? 701 NAG B C5 1 HETATM 3743 C C6 . NAG P 2 . ? 55.156 38.852 98.708 1.00 98.11 ? 701 NAG B C6 1 HETATM 3744 C C7 . NAG P 2 . ? 56.813 32.346 99.664 1.00 99.03 ? 701 NAG B C7 1 HETATM 3745 C C8 . NAG P 2 . ? 56.359 30.923 99.830 1.00 100.01 ? 701 NAG B C8 1 HETATM 3746 N N2 . NAG P 2 . ? 55.845 33.256 99.456 1.00 96.12 ? 701 NAG B N2 1 HETATM 3747 O O3 . NAG P 2 . ? 56.429 34.997 101.643 1.00 101.39 ? 701 NAG B O3 1 HETATM 3748 O O4 . NAG P 2 . ? 55.338 37.741 101.413 1.00 108.14 ? 701 NAG B O4 1 HETATM 3749 O O5 . NAG P 2 . ? 55.577 36.608 97.939 1.00 85.21 ? 701 NAG B O5 1 HETATM 3750 O O6 . NAG P 2 . ? 54.527 39.103 97.442 1.00 99.22 ? 701 NAG B O6 1 HETATM 3751 O O7 . NAG P 2 . ? 58.003 32.622 99.727 1.00 98.70 ? 701 NAG B O7 1 HETATM 3752 C C1 . NAG Q 2 . ? 56.290 37.909 102.491 1.00 117.28 ? 702 NAG B C1 1 HETATM 3753 C C2 . NAG Q 2 . ? 56.120 39.296 103.108 1.00 119.75 ? 702 NAG B C2 1 HETATM 3754 C C3 . NAG Q 2 . ? 56.945 39.476 104.386 1.00 123.80 ? 702 NAG B C3 1 HETATM 3755 C C4 . NAG Q 2 . ? 56.852 38.270 105.323 1.00 124.71 ? 702 NAG B C4 1 HETATM 3756 C C5 . NAG Q 2 . ? 57.090 36.975 104.547 1.00 122.81 ? 702 NAG B C5 1 HETATM 3757 C C6 . NAG Q 2 . ? 56.972 35.733 105.426 1.00 121.22 ? 702 NAG B C6 1 HETATM 3758 C C7 . NAG Q 2 . ? 55.671 41.103 101.482 1.00 120.00 ? 702 NAG B C7 1 HETATM 3759 C C8 . NAG Q 2 . ? 56.309 42.072 100.527 1.00 118.22 ? 702 NAG B C8 1 HETATM 3760 N N2 . NAG Q 2 . ? 56.521 40.307 102.138 1.00 118.76 ? 702 NAG B N2 1 HETATM 3761 O O3 . NAG Q 2 . ? 56.495 40.652 105.074 1.00 125.24 ? 702 NAG B O3 1 HETATM 3762 O O4 . NAG Q 2 . ? 57.810 38.410 106.383 1.00 125.35 ? 702 NAG B O4 1 HETATM 3763 O O5 . NAG Q 2 . ? 56.132 36.895 103.487 1.00 120.65 ? 702 NAG B O5 1 HETATM 3764 O O6 . NAG Q 2 . ? 57.218 34.565 104.633 1.00 119.38 ? 702 NAG B O6 1 HETATM 3765 O O7 . NAG Q 2 . ? 54.458 41.063 101.624 1.00 120.04 ? 702 NAG B O7 1 HETATM 3766 C C1 . NAG R 2 . ? 70.972 43.401 106.780 1.00 101.06 ? 703 NAG B C1 1 HETATM 3767 C C2 . NAG R 2 . ? 70.131 42.615 107.787 1.00 108.25 ? 703 NAG B C2 1 HETATM 3768 C C3 . NAG R 2 . ? 70.111 43.335 109.128 1.00 113.20 ? 703 NAG B C3 1 HETATM 3769 C C4 . NAG R 2 . ? 71.503 43.698 109.635 1.00 115.39 ? 703 NAG B C4 1 HETATM 3770 C C5 . NAG R 2 . ? 72.360 44.321 108.518 1.00 111.33 ? 703 NAG B C5 1 HETATM 3771 C C6 . NAG R 2 . ? 73.844 44.401 108.870 1.00 110.41 ? 703 NAG B C6 1 HETATM 3772 C C7 . NAG R 2 . ? 68.203 41.315 106.938 1.00 107.33 ? 703 NAG B C7 1 HETATM 3773 C C8 . NAG R 2 . ? 66.760 41.407 106.529 1.00 108.59 ? 703 NAG B C8 1 HETATM 3774 N N2 . NAG R 2 . ? 68.753 42.464 107.341 1.00 107.43 ? 703 NAG B N2 1 HETATM 3775 O O3 . NAG R 2 . ? 69.459 42.508 110.101 1.00 116.60 ? 703 NAG B O3 1 HETATM 3776 O O4 . NAG R 2 . ? 71.243 44.603 110.733 1.00 124.09 ? 703 NAG B O4 1 HETATM 3777 O O5 . NAG R 2 . ? 72.284 43.546 107.314 1.00 107.56 ? 703 NAG B O5 1 HETATM 3778 O O6 . NAG R 2 . ? 74.577 44.961 107.771 1.00 106.59 ? 703 NAG B O6 1 HETATM 3779 O O7 . NAG R 2 . ? 68.807 40.254 106.894 1.00 104.63 ? 703 NAG B O7 1 HETATM 3780 C C1 . NAG S 2 . ? 72.034 44.613 111.960 1.00 132.02 ? 704 NAG B C1 1 HETATM 3781 C C2 . NAG S 2 . ? 72.649 43.274 112.414 1.00 134.53 ? 704 NAG B C2 1 HETATM 3782 C C3 . NAG S 2 . ? 73.572 43.438 113.622 1.00 136.74 ? 704 NAG B C3 1 HETATM 3783 C C4 . NAG S 2 . ? 74.511 44.636 113.488 1.00 137.28 ? 704 NAG B C4 1 HETATM 3784 C C5 . NAG S 2 . ? 73.732 45.890 113.092 1.00 136.75 ? 704 NAG B C5 1 HETATM 3785 C C6 . NAG S 2 . ? 74.630 47.107 112.889 1.00 136.62 ? 704 NAG B C6 1 HETATM 3786 C C7 . NAG S 2 . ? 71.638 41.012 112.512 1.00 133.17 ? 704 NAG B C7 1 HETATM 3787 C C8 . NAG S 2 . ? 70.440 40.229 112.972 1.00 132.89 ? 704 NAG B C8 1 HETATM 3788 N N2 . NAG S 2 . ? 71.596 42.328 112.766 1.00 132.81 ? 704 NAG B N2 1 HETATM 3789 O O3 . NAG S 2 . ? 74.351 42.245 113.780 1.00 136.40 ? 704 NAG B O3 1 HETATM 3790 O O4 . NAG S 2 . ? 75.187 44.846 114.734 1.00 137.23 ? 704 NAG B O4 1 HETATM 3791 O O5 . NAG S 2 . ? 73.034 45.633 111.874 1.00 134.27 ? 704 NAG B O5 1 HETATM 3792 O O6 . NAG S 2 . ? 75.485 46.900 111.758 1.00 136.98 ? 704 NAG B O6 1 HETATM 3793 O O7 . NAG S 2 . ? 72.568 40.453 111.947 1.00 131.42 ? 704 NAG B O7 1 HETATM 3794 C C1 . NAG T 2 . ? 73.903 57.221 81.491 1.00 65.01 ? 705 NAG B C1 1 HETATM 3795 C C2 . NAG T 2 . ? 73.870 58.677 81.039 1.00 68.68 ? 705 NAG B C2 1 HETATM 3796 C C3 . NAG T 2 . ? 75.083 59.460 81.520 1.00 68.94 ? 705 NAG B C3 1 HETATM 3797 C C4 . NAG T 2 . ? 75.464 59.093 82.945 1.00 70.00 ? 705 NAG B C4 1 HETATM 3798 C C5 . NAG T 2 . ? 75.524 57.581 83.150 1.00 68.11 ? 705 NAG B C5 1 HETATM 3799 C C6 . NAG T 2 . ? 75.921 57.174 84.563 1.00 67.02 ? 705 NAG B C6 1 HETATM 3800 C C7 . NAG T 2 . ? 72.685 58.981 78.902 1.00 70.12 ? 705 NAG B C7 1 HETATM 3801 C C8 . NAG T 2 . ? 72.822 58.957 77.407 1.00 70.31 ? 705 NAG B C8 1 HETATM 3802 N N2 . NAG T 2 . ? 73.801 58.709 79.584 1.00 69.47 ? 705 NAG B N2 1 HETATM 3803 O O3 . NAG T 2 . ? 74.755 60.850 81.476 1.00 70.54 ? 705 NAG B O3 1 HETATM 3804 O O4 . NAG T 2 . ? 76.742 59.671 83.224 1.00 76.46 ? 705 NAG B O4 1 HETATM 3805 O O5 . NAG T 2 . ? 74.233 57.051 82.867 1.00 65.83 ? 705 NAG B O5 1 HETATM 3806 O O6 . NAG T 2 . ? 74.943 57.649 85.492 1.00 67.26 ? 705 NAG B O6 1 HETATM 3807 O O7 . NAG T 2 . ? 71.617 59.242 79.434 1.00 71.56 ? 705 NAG B O7 1 HETATM 3808 C C1 . NAG U 2 . ? 76.624 60.731 84.182 1.00 82.78 ? 706 NAG B C1 1 HETATM 3809 C C2 . NAG U 2 . ? 78.002 61.061 84.723 1.00 85.85 ? 706 NAG B C2 1 HETATM 3810 C C3 . NAG U 2 . ? 77.908 62.189 85.738 1.00 91.87 ? 706 NAG B C3 1 HETATM 3811 C C4 . NAG U 2 . ? 77.117 63.366 85.182 1.00 95.83 ? 706 NAG B C4 1 HETATM 3812 C C5 . NAG U 2 . ? 75.792 62.922 84.572 1.00 92.99 ? 706 NAG B C5 1 HETATM 3813 C C6 . NAG U 2 . ? 75.059 64.077 83.900 1.00 92.88 ? 706 NAG B C6 1 HETATM 3814 C C7 . NAG U 2 . ? 79.653 59.238 84.927 1.00 82.01 ? 706 NAG B C7 1 HETATM 3815 C C8 . NAG U 2 . ? 80.057 58.045 85.747 1.00 81.46 ? 706 NAG B C8 1 HETATM 3816 N N2 . NAG U 2 . ? 78.566 59.883 85.361 1.00 84.17 ? 706 NAG B N2 1 HETATM 3817 O O3 . NAG U 2 . ? 79.224 62.621 86.105 1.00 92.67 ? 706 NAG B O3 1 HETATM 3818 O O4 . NAG U 2 . ? 76.850 64.256 86.268 1.00 108.09 ? 706 NAG B O4 1 HETATM 3819 O O5 . NAG U 2 . ? 76.033 61.895 83.609 1.00 86.95 ? 706 NAG B O5 1 HETATM 3820 O O6 . NAG U 2 . ? 73.788 63.618 83.431 1.00 93.19 ? 706 NAG B O6 1 HETATM 3821 O O7 . NAG U 2 . ? 80.287 59.574 83.940 1.00 78.22 ? 706 NAG B O7 1 HETATM 3822 C C1 . BMA V 3 . ? 77.337 65.580 86.003 1.00 119.24 ? 707 BMA B C1 1 HETATM 3823 C C2 . BMA V 3 . ? 76.694 66.509 87.010 1.00 124.90 ? 707 BMA B C2 1 HETATM 3824 C C3 . BMA V 3 . ? 77.104 67.962 86.764 1.00 129.89 ? 707 BMA B C3 1 HETATM 3825 C C4 . BMA V 3 . ? 78.571 68.150 86.338 1.00 128.38 ? 707 BMA B C4 1 HETATM 3826 C C5 . BMA V 3 . ? 79.244 66.952 85.647 1.00 126.54 ? 707 BMA B C5 1 HETATM 3827 C C6 . BMA V 3 . ? 80.762 66.997 85.831 1.00 128.74 ? 707 BMA B C6 1 HETATM 3828 O O2 . BMA V 3 . ? 77.062 66.069 88.328 1.00 123.58 ? 707 BMA B O2 1 HETATM 3829 O O3 . BMA V 3 . ? 76.842 68.657 87.996 1.00 139.54 ? 707 BMA B O3 1 HETATM 3830 O O4 . BMA V 3 . ? 78.636 69.251 85.424 1.00 127.08 ? 707 BMA B O4 1 HETATM 3831 O O5 . BMA V 3 . ? 78.753 65.698 86.126 1.00 121.79 ? 707 BMA B O5 1 HETATM 3832 O O6 . BMA V 3 . ? 81.117 66.720 87.198 1.00 134.56 ? 707 BMA B O6 1 HETATM 3833 C C1 . MAN W 4 . ? 76.672 70.084 87.884 1.00 145.86 ? 708 MAN B C1 1 HETATM 3834 C C2 . MAN W 4 . ? 76.463 70.603 89.306 1.00 147.56 ? 708 MAN B C2 1 HETATM 3835 C C3 . MAN W 4 . ? 75.077 70.216 89.824 1.00 146.80 ? 708 MAN B C3 1 HETATM 3836 C C4 . MAN W 4 . ? 73.988 70.647 88.844 1.00 143.96 ? 708 MAN B C4 1 HETATM 3837 C C5 . MAN W 4 . ? 74.281 70.122 87.438 1.00 141.45 ? 708 MAN B C5 1 HETATM 3838 C C6 . MAN W 4 . ? 73.258 70.659 86.439 1.00 137.15 ? 708 MAN B C6 1 HETATM 3839 O O2 . MAN W 4 . ? 76.638 72.026 89.336 1.00 149.03 ? 708 MAN B O2 1 HETATM 3840 O O3 . MAN W 4 . ? 74.848 70.813 91.106 1.00 150.85 ? 708 MAN B O3 1 HETATM 3841 O O4 . MAN W 4 . ? 72.717 70.162 89.293 1.00 140.48 ? 708 MAN B O4 1 HETATM 3842 O O5 . MAN W 4 . ? 75.599 70.506 87.027 1.00 145.78 ? 708 MAN B O5 1 HETATM 3843 O O6 . MAN W 4 . ? 73.671 70.372 85.097 1.00 132.47 ? 708 MAN B O6 1 HETATM 3844 C C1 . MAN X 4 . ? 82.454 67.182 87.498 1.00 137.57 ? 709 MAN B C1 1 HETATM 3845 C C2 . MAN X 4 . ? 83.014 66.385 88.676 1.00 137.29 ? 709 MAN B C2 1 HETATM 3846 C C3 . MAN X 4 . ? 82.363 66.791 90.001 1.00 137.59 ? 709 MAN B C3 1 HETATM 3847 C C4 . MAN X 4 . ? 82.370 68.306 90.195 1.00 136.74 ? 709 MAN B C4 1 HETATM 3848 C C5 . MAN X 4 . ? 81.841 69.032 88.956 1.00 137.46 ? 709 MAN B C5 1 HETATM 3849 C C6 . MAN X 4 . ? 82.011 70.546 89.087 1.00 136.21 ? 709 MAN B C6 1 HETATM 3850 O O2 . MAN X 4 . ? 84.432 66.584 88.733 1.00 134.17 ? 709 MAN B O2 1 HETATM 3851 O O3 . MAN X 4 . ? 83.033 66.165 91.105 1.00 135.99 ? 709 MAN B O3 1 HETATM 3852 O O4 . MAN X 4 . ? 81.566 68.624 91.338 1.00 133.30 ? 709 MAN B O4 1 HETATM 3853 O O5 . MAN X 4 . ? 82.527 68.589 87.773 1.00 139.93 ? 709 MAN B O5 1 HETATM 3854 O O6 . MAN X 4 . ? 81.352 71.214 88.004 1.00 133.08 ? 709 MAN B O6 1 HETATM 3855 C C1 . NAG Y 2 . ? 49.266 59.454 84.801 1.00 64.78 ? 710 NAG B C1 1 HETATM 3856 C C2 . NAG Y 2 . ? 48.335 58.859 85.849 1.00 67.92 ? 710 NAG B C2 1 HETATM 3857 C C3 . NAG Y 2 . ? 47.906 59.936 86.833 1.00 69.51 ? 710 NAG B C3 1 HETATM 3858 C C4 . NAG Y 2 . ? 49.134 60.628 87.410 1.00 73.25 ? 710 NAG B C4 1 HETATM 3859 C C5 . NAG Y 2 . ? 50.084 61.117 86.322 1.00 71.64 ? 710 NAG B C5 1 HETATM 3860 C C6 . NAG Y 2 . ? 51.401 61.681 86.857 1.00 70.99 ? 710 NAG B C6 1 HETATM 3861 C C7 . NAG Y 2 . ? 46.676 57.066 85.518 1.00 72.81 ? 710 NAG B C7 1 HETATM 3862 C C8 . NAG Y 2 . ? 45.514 56.627 84.675 1.00 72.16 ? 710 NAG B C8 1 HETATM 3863 N N2 . NAG Y 2 . ? 47.202 58.247 85.174 1.00 69.84 ? 710 NAG B N2 1 HETATM 3864 O O3 . NAG Y 2 . ? 47.157 59.330 87.885 1.00 68.66 ? 710 NAG B O3 1 HETATM 3865 O O4 . NAG Y 2 . ? 48.755 61.787 88.159 1.00 84.03 ? 710 NAG B O4 1 HETATM 3866 O O5 . NAG Y 2 . ? 50.389 60.034 85.467 1.00 65.19 ? 710 NAG B O5 1 HETATM 3867 O O6 . NAG Y 2 . ? 52.041 60.749 87.738 1.00 73.10 ? 710 NAG B O6 1 HETATM 3868 O O7 . NAG Y 2 . ? 47.086 56.375 86.444 1.00 75.51 ? 710 NAG B O7 1 HETATM 3869 C C1 . NAG Z 2 . ? 49.178 61.666 89.522 1.00 91.70 ? 711 NAG B C1 1 HETATM 3870 C C2 . NAG Z 2 . ? 49.299 63.017 90.215 1.00 94.93 ? 711 NAG B C2 1 HETATM 3871 C C3 . NAG Z 2 . ? 49.860 62.757 91.609 1.00 100.40 ? 711 NAG B C3 1 HETATM 3872 C C4 . NAG Z 2 . ? 48.971 61.763 92.362 1.00 106.84 ? 711 NAG B C4 1 HETATM 3873 C C5 . NAG Z 2 . ? 48.677 60.509 91.527 1.00 103.46 ? 711 NAG B C5 1 HETATM 3874 C C6 . NAG Z 2 . ? 47.575 59.631 92.108 1.00 103.18 ? 711 NAG B C6 1 HETATM 3875 C C7 . NAG Z 2 . ? 49.700 64.777 88.519 1.00 90.60 ? 711 NAG B C7 1 HETATM 3876 C C8 . NAG Z 2 . ? 50.753 65.623 87.864 1.00 87.53 ? 711 NAG B C8 1 HETATM 3877 N N2 . NAG Z 2 . ? 50.150 63.932 89.462 1.00 93.72 ? 711 NAG B N2 1 HETATM 3878 O O3 . NAG Z 2 . ? 49.954 63.988 92.332 1.00 101.17 ? 711 NAG B O3 1 HETATM 3879 O O4 . NAG Z 2 . ? 49.626 61.343 93.576 1.00 120.73 ? 711 NAG B O4 1 HETATM 3880 O O5 . NAG Z 2 . ? 48.240 60.863 90.221 1.00 95.40 ? 711 NAG B O5 1 HETATM 3881 O O6 . NAG Z 2 . ? 48.092 58.857 93.194 1.00 105.78 ? 711 NAG B O6 1 HETATM 3882 O O7 . NAG Z 2 . ? 48.524 64.868 88.189 1.00 88.38 ? 711 NAG B O7 1 HETATM 3883 C C1 . BMA AA 3 . ? 49.374 62.047 94.824 1.00 130.08 ? 712 BMA B C1 1 HETATM 3884 C C2 . BMA AA 3 . ? 47.891 62.359 95.094 1.00 133.68 ? 712 BMA B C2 1 HETATM 3885 C C3 . BMA AA 3 . ? 47.647 62.821 96.525 1.00 136.13 ? 712 BMA B C3 1 HETATM 3886 C C4 . BMA AA 3 . ? 48.233 61.830 97.521 1.00 137.55 ? 712 BMA B C4 1 HETATM 3887 C C5 . BMA AA 3 . ? 49.713 61.576 97.236 1.00 137.85 ? 712 BMA B C5 1 HETATM 3888 C C6 . BMA AA 3 . ? 50.226 60.429 98.108 1.00 137.07 ? 712 BMA B C6 1 HETATM 3889 O O2 . BMA AA 3 . ? 47.067 61.213 94.836 1.00 135.35 ? 712 BMA B O2 1 HETATM 3890 O O3 . BMA AA 3 . ? 46.238 62.972 96.748 1.00 134.38 ? 712 BMA B O3 1 HETATM 3891 O O4 . BMA AA 3 . ? 48.077 62.355 98.845 1.00 137.62 ? 712 BMA B O4 1 HETATM 3892 O O5 . BMA AA 3 . ? 49.940 61.231 95.862 1.00 133.72 ? 712 BMA B O5 1 HETATM 3893 O O6 . BMA AA 3 . ? 51.639 60.272 97.939 1.00 137.72 ? 712 BMA B O6 1 HETATM 3894 S S . SCN BA 5 . ? 68.999 48.064 74.699 1.00 99.90 ? 713 SCN B S 1 HETATM 3895 C C . SCN BA 5 . ? 70.436 47.199 74.909 1.00 100.11 ? 713 SCN B C 1 HETATM 3896 N N . SCN BA 5 . ? 71.412 46.580 75.023 1.00 98.77 ? 713 SCN B N 1 HETATM 3897 S S . SCN CA 5 . ? 52.425 25.908 89.707 1.00 112.62 ? 714 SCN B S 1 HETATM 3898 C C . SCN CA 5 . ? 52.422 25.127 88.208 1.00 105.60 ? 714 SCN B C 1 HETATM 3899 N N . SCN CA 5 . ? 52.453 24.612 87.170 1.00 102.27 ? 714 SCN B N 1 HETATM 3900 O O . HOH DA 6 . ? 67.199 19.589 78.783 1.00 49.45 ? 801 HOH A O 1 HETATM 3901 O O . HOH DA 6 . ? 57.650 13.794 82.392 1.00 69.63 ? 802 HOH A O 1 HETATM 3902 O O . HOH DA 6 . ? 65.926 18.156 108.978 1.00 76.13 ? 803 HOH A O 1 HETATM 3903 O O . HOH DA 6 . ? 72.114 10.941 100.184 1.00 57.53 ? 804 HOH A O 1 HETATM 3904 O O . HOH DA 6 . ? 93.453 14.588 86.104 1.00 76.26 ? 805 HOH A O 1 HETATM 3905 O O . HOH DA 6 . ? 68.532 25.334 92.571 1.00 40.60 ? 806 HOH A O 1 HETATM 3906 O O . HOH DA 6 . ? 69.427 34.503 97.288 1.00 44.04 ? 807 HOH A O 1 HETATM 3907 O O . HOH DA 6 . ? 74.663 19.270 86.087 1.00 46.57 ? 808 HOH A O 1 HETATM 3908 O O . HOH DA 6 . ? 69.163 31.645 88.804 1.00 50.71 ? 809 HOH A O 1 HETATM 3909 O O . HOH DA 6 . ? 59.525 25.598 104.839 1.00 75.62 ? 810 HOH A O 1 HETATM 3910 O O . HOH DA 6 . ? 60.795 23.302 87.397 1.00 58.03 ? 811 HOH A O 1 HETATM 3911 O O . HOH DA 6 . ? 92.078 13.647 88.489 1.00 66.71 ? 812 HOH A O 1 HETATM 3912 O O . HOH DA 6 . ? 62.176 28.387 104.125 1.00 69.27 ? 813 HOH A O 1 HETATM 3913 O O . HOH EA 6 . ? 54.279 10.729 76.428 1.00 76.54 ? 801 HOH B O 1 HETATM 3914 O O . HOH EA 6 . ? 76.705 58.848 87.151 1.00 59.44 ? 802 HOH B O 1 HETATM 3915 O O . HOH EA 6 . ? 61.455 24.264 80.417 1.00 50.22 ? 803 HOH B O 1 HETATM 3916 O O . HOH EA 6 . ? 64.624 31.486 97.078 1.00 44.67 ? 804 HOH B O 1 HETATM 3917 O O . HOH EA 6 . ? 59.284 26.874 99.686 1.00 56.72 ? 805 HOH B O 1 HETATM 3918 O O . HOH EA 6 . ? 50.648 57.131 89.794 1.00 74.01 ? 806 HOH B O 1 HETATM 3919 O O . HOH EA 6 . ? 53.286 32.518 98.796 1.00 63.01 ? 807 HOH B O 1 HETATM 3920 O O . HOH EA 6 . ? 61.723 55.197 97.558 1.00 50.62 ? 808 HOH B O 1 HETATM 3921 O O . HOH EA 6 . ? 62.917 51.256 104.654 1.00 79.16 ? 809 HOH B O 1 HETATM 3922 O O . HOH EA 6 . ? 55.885 49.825 74.279 1.00 58.63 ? 810 HOH B O 1 HETATM 3923 O O . HOH EA 6 . ? 66.088 33.614 88.795 1.00 42.02 ? 811 HOH B O 1 HETATM 3924 O O . HOH EA 6 . ? 42.134 45.969 80.581 1.00 59.66 ? 812 HOH B O 1 HETATM 3925 O O . HOH EA 6 . ? 47.148 49.107 75.906 1.00 62.33 ? 813 HOH B O 1 HETATM 3926 O O . HOH EA 6 . ? 49.355 51.092 75.685 1.00 64.01 ? 814 HOH B O 1 HETATM 3927 O O . HOH EA 6 . ? 55.449 24.661 90.972 1.00 57.54 ? 815 HOH B O 1 HETATM 3928 O O . HOH EA 6 . ? 63.887 44.333 104.833 1.00 75.90 ? 816 HOH B O 1 HETATM 3929 O O . HOH EA 6 . ? 47.852 51.403 93.650 1.00 61.01 ? 817 HOH B O 1 HETATM 3930 O O . HOH EA 6 . ? 61.106 59.974 90.717 1.00 69.41 ? 818 HOH B O 1 HETATM 3931 O O . HOH EA 6 . ? 56.559 25.472 88.416 1.00 51.16 ? 819 HOH B O 1 HETATM 3932 O O . HOH EA 6 . ? 48.116 52.063 78.096 1.00 57.91 ? 820 HOH B O 1 HETATM 3933 O O . HOH EA 6 . ? 53.544 25.936 99.219 1.00 66.99 ? 821 HOH B O 1 HETATM 3934 O O . HOH EA 6 . ? 66.309 34.011 84.468 1.00 51.10 ? 822 HOH B O 1 HETATM 3935 O O . HOH EA 6 . ? 74.812 40.539 88.777 1.00 66.93 ? 823 HOH B O 1 HETATM 3936 O O . HOH EA 6 . ? 49.882 52.834 95.094 1.00 77.10 ? 824 HOH B O 1 HETATM 3937 O O . HOH EA 6 . ? 47.726 56.712 89.912 1.00 77.93 ? 825 HOH B O 1 HETATM 3938 O O . HOH EA 6 . ? 70.267 31.565 86.034 1.00 71.50 ? 826 HOH B O 1 HETATM 3939 O O . HOH EA 6 . ? 61.629 58.340 97.153 1.00 67.42 ? 827 HOH B O 1 HETATM 3940 O O . HOH EA 6 . ? 75.401 42.024 86.355 1.00 75.76 ? 828 HOH B O 1 HETATM 3941 O O . HOH EA 6 . ? 50.672 53.558 97.645 1.00 69.77 ? 829 HOH B O 1 HETATM 3942 O O . HOH EA 6 . ? 70.889 33.527 99.477 1.00 50.35 ? 830 HOH B O 1 HETATM 3943 O O . HOH EA 6 . ? 62.997 32.903 98.833 1.00 60.10 ? 831 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LYS A 9 ? 2.1380 2.1334 2.1000 -0.1331 0.0255 -0.0105 392 LYS A N 2 C CA . LYS A 9 ? 2.1257 2.1314 2.1037 -0.1220 0.0195 -0.0032 392 LYS A CA 3 C C . LYS A 9 ? 2.1593 2.1735 2.1504 -0.1143 0.0201 0.0016 392 LYS A C 4 O O . LYS A 9 ? 2.1558 2.1765 2.1503 -0.1135 0.0142 0.0148 392 LYS A O 5 C CB . LYS A 9 ? 2.0708 2.0766 2.0587 -0.1127 0.0218 -0.0124 392 LYS A CB 6 C CG . LYS A 9 ? 2.0771 2.0756 2.0565 -0.1183 0.0197 -0.0132 392 LYS A CG 7 C CD . LYS A 9 ? 2.0545 2.0487 2.0401 -0.1114 0.0256 -0.0252 392 LYS A CD 8 C CE . LYS A 9 ? 2.0567 2.0396 2.0320 -0.1198 0.0264 -0.0283 392 LYS A CE 9 N NZ . LYS A 9 ? 2.0482 2.0243 2.0277 -0.1152 0.0346 -0.0415 392 LYS A NZ 10 N N . GLU A 10 ? 2.1808 2.1951 2.1806 -0.1092 0.0277 -0.0092 393 GLU A N 11 C CA . GLU A 10 ? 2.1918 2.2130 2.2054 -0.1025 0.0299 -0.0071 393 GLU A CA 12 C C . GLU A 10 ? 2.2548 2.2710 2.2615 -0.1109 0.0342 -0.0027 393 GLU A C 13 O O . GLU A 10 ? 2.2421 2.2624 2.2594 -0.1069 0.0360 0.0019 393 GLU A O 14 C CB . GLU A 10 ? 2.1489 2.1757 2.1791 -0.0915 0.0346 -0.0207 393 GLU A CB 15 C CG . GLU A 10 ? 2.1101 2.1476 2.1526 -0.0787 0.0292 -0.0180 393 GLU A CG 16 C CD . GLU A 10 ? 2.0909 2.1350 2.1409 -0.0749 0.0260 -0.0064 393 GLU A CD 17 O OE1 . GLU A 10 ? 2.1614 2.2035 2.2132 -0.0790 0.0296 -0.0035 393 GLU A OE1 18 O OE2 . GLU A 10 ? 1.9174 1.9681 1.9719 -0.0675 0.0208 0.0002 393 GLU A OE2 19 N N . TYR A 11 ? 2.3261 2.3330 2.3144 -0.1223 0.0363 -0.0033 394 TYR A N 20 C CA . TYR A 11 ? 2.3589 2.3611 2.3368 -0.1306 0.0395 0.0041 394 TYR A CA 21 C C . TYR A 11 ? 2.4011 2.4095 2.3804 -0.1303 0.0322 0.0224 394 TYR A C 22 O O . TYR A 11 ? 2.3574 2.3657 2.3410 -0.1300 0.0361 0.0290 394 TYR A O 23 C CB . TYR A 11 ? 2.3636 2.3557 2.3175 -0.1432 0.0410 0.0018 394 TYR A CB 24 C CG . TYR A 11 ? 2.3542 2.3416 2.2954 -0.1511 0.0448 0.0100 394 TYR A CG 25 C CD1 . TYR A 11 ? 2.3456 2.3262 2.2877 -0.1525 0.0569 0.0019 394 TYR A CD1 26 C CD2 . TYR A 11 ? 2.3426 2.3330 2.2721 -0.1564 0.0364 0.0268 394 TYR A CD2 27 C CE1 . TYR A 11 ? 2.3607 2.3362 2.2908 -0.1590 0.0615 0.0106 394 TYR A CE1 28 C CE2 . TYR A 11 ? 2.3409 2.3274 2.2582 -0.1625 0.0398 0.0359 394 TYR A CE2 29 C CZ . TYR A 11 ? 2.3641 2.3425 2.2810 -0.1637 0.0528 0.0281 394 TYR A CZ 30 O OH . TYR A 11 ? 2.4044 2.3780 2.3085 -0.1693 0.0573 0.0381 394 TYR A OH 31 N N . PHE A 12 ? 2.4368 2.4506 2.4142 -0.1301 0.0222 0.0306 395 PHE A N 32 C CA . PHE A 12 ? 2.3988 2.4197 2.3776 -0.1306 0.0141 0.0486 395 PHE A CA 33 C C . PHE A 12 ? 2.3351 2.3636 2.3357 -0.1191 0.0154 0.0538 395 PHE A C 34 O O . PHE A 12 ? 2.3128 2.3451 2.3174 -0.1189 0.0134 0.0678 395 PHE A O 35 C CB . PHE A 12 ? 2.4015 2.4266 2.3751 -0.1337 0.0038 0.0544 395 PHE A CB 36 C CG . PHE A 12 ? 2.4320 2.4494 2.3844 -0.1456 0.0021 0.0486 395 PHE A CG 37 C CD1 . PHE A 12 ? 2.4553 2.4707 2.3889 -0.1569 -0.0016 0.0565 395 PHE A CD1 38 C CD2 . PHE A 12 ? 2.4093 2.4213 2.3602 -0.1452 0.0045 0.0352 395 PHE A CD2 39 C CE1 . PHE A 12 ? 2.4455 2.4537 2.3582 -0.1684 -0.0028 0.0497 395 PHE A CE1 40 C CE2 . PHE A 12 ? 2.3987 2.4024 2.3308 -0.1564 0.0041 0.0288 395 PHE A CE2 41 C CZ . PHE A 12 ? 2.4193 2.4209 2.3317 -0.1683 0.0004 0.0353 395 PHE A CZ 42 N N . ASP A 13 ? 2.2542 2.2852 2.2688 -0.1096 0.0191 0.0424 396 ASP A N 43 C CA . ASP A 13 ? 2.1578 2.1958 2.1924 -0.0986 0.0211 0.0441 396 ASP A CA 44 C C . ASP A 13 ? 2.0729 2.1077 2.1161 -0.0976 0.0301 0.0423 396 ASP A C 45 O O . ASP A 13 ? 2.0640 2.1037 2.1236 -0.0894 0.0323 0.0437 396 ASP A O 46 C CB . ASP A 13 ? 2.1269 2.1692 2.1716 -0.0887 0.0219 0.0314 396 ASP A CB 47 C CG . ASP A 13 ? 2.1282 2.1742 2.1693 -0.0870 0.0142 0.0358 396 ASP A CG 48 O OD1 . ASP A 13 ? 2.1015 2.1540 2.1487 -0.0835 0.0092 0.0481 396 ASP A OD1 49 O OD2 . ASP A 13 ? 2.1278 2.1700 2.1614 -0.0890 0.0140 0.0270 396 ASP A OD2 50 N N . GLN A 14 ? 1.9685 1.9948 2.0011 -0.1059 0.0360 0.0393 397 GLN A N 51 C CA . GLN A 14 ? 1.8804 1.9021 1.9226 -0.1052 0.0468 0.0343 397 GLN A CA 52 C C . GLN A 14 ? 1.7984 1.8217 1.8537 -0.0991 0.0526 0.0143 397 GLN A C 53 O O . GLN A 14 ? 1.8125 1.8361 1.8837 -0.0950 0.0603 0.0071 397 GLN A O 54 C CB . GLN A 14 ? 1.8372 1.8621 1.8931 -0.1003 0.0477 0.0474 397 GLN A CB 55 C CG . GLN A 14 ? 1.7942 1.8117 1.8554 -0.1029 0.0584 0.0490 397 GLN A CG 56 C CD . GLN A 14 ? 1.7644 1.7845 1.8413 -0.0971 0.0599 0.0620 397 GLN A CD 57 O OE1 . GLN A 14 ? 1.7335 1.7616 1.8192 -0.0902 0.0537 0.0676 397 GLN A OE1 58 N NE2 . GLN A 14 ? 1.7577 1.7704 1.8386 -0.0996 0.0692 0.0673 397 GLN A NE2 59 N N . HIS A 15 ? 1.6625 1.6870 1.7111 -0.0988 0.0488 0.0055 398 HIS A N 60 C CA . HIS A 15 ? 1.4851 1.5142 1.5448 -0.0915 0.0508 -0.0114 398 HIS A CA 61 C C . HIS A 15 ? 1.3150 1.3547 1.3907 -0.0797 0.0472 -0.0122 398 HIS A C 62 O O . HIS A 15 ? 1.3578 1.4029 1.4321 -0.0742 0.0409 -0.0127 398 HIS A O 63 C CB . HIS A 15 ? 1.4687 1.4933 1.5343 -0.0943 0.0613 -0.0260 398 HIS A CB 64 C CG . HIS A 15 ? 1.4849 1.5037 1.5386 -0.0999 0.0635 -0.0352 398 HIS A CG 65 N ND1 . HIS A 15 ? 1.5119 1.5279 1.5725 -0.1015 0.0727 -0.0498 398 HIS A ND1 66 C CD2 . HIS A 15 ? 1.4927 1.5078 1.5301 -0.1042 0.0584 -0.0325 398 HIS A CD2 67 C CE1 . HIS A 15 ? 1.5220 1.5327 1.5705 -0.1062 0.0736 -0.0553 398 HIS A CE1 68 N NE2 . HIS A 15 ? 1.5080 1.5175 1.5419 -0.1079 0.0651 -0.0454 398 HIS A NE2 69 N N . PHE A 16 ? 1.1102 1.1524 1.2006 -0.0757 0.0517 -0.0123 399 PHE A N 70 C CA . PHE A 16 ? 0.9640 1.0154 1.0667 -0.0652 0.0481 -0.0102 399 PHE A CA 71 C C . PHE A 16 ? 0.8811 0.9304 0.9963 -0.0649 0.0546 -0.0058 399 PHE A C 72 O O . PHE A 16 ? 0.8768 0.9293 1.0077 -0.0600 0.0600 -0.0173 399 PHE A O 73 C CB . PHE A 16 ? 0.9058 0.9659 1.0176 -0.0561 0.0474 -0.0268 399 PHE A CB 74 C CG . PHE A 16 ? 0.8570 0.9254 0.9673 -0.0471 0.0396 -0.0230 399 PHE A CG 75 C CD1 . PHE A 16 ? 0.8549 0.9224 0.9529 -0.0481 0.0341 -0.0200 399 PHE A CD1 76 C CD2 . PHE A 16 ? 0.8322 0.9092 0.9537 -0.0372 0.0390 -0.0246 399 PHE A CD2 77 C CE1 . PHE A 16 ? 0.8473 0.9218 0.9443 -0.0396 0.0282 -0.0165 399 PHE A CE1 78 C CE2 . PHE A 16 ? 0.8168 0.9012 0.9356 -0.0285 0.0329 -0.0213 399 PHE A CE2 79 C CZ . PHE A 16 ? 0.8339 0.9170 0.9407 -0.0296 0.0277 -0.0167 399 PHE A CZ 80 N N . GLY A 17 ? 0.8179 0.8616 0.9261 -0.0710 0.0542 0.0105 400 GLY A N 81 C CA . GLY A 17 ? 0.7907 0.8305 0.9095 -0.0714 0.0609 0.0183 400 GLY A CA 82 C C . GLY A 17 ? 0.7641 0.7959 0.8865 -0.0771 0.0713 0.0083 400 GLY A C 83 O O . GLY A 17 ? 0.7550 0.7852 0.8709 -0.0808 0.0726 -0.0035 400 GLY A O 84 N N . PRO A 18 ? 0.7438 0.7704 0.8780 -0.0775 0.0798 0.0132 401 PRO A N 85 C CA . PRO A 18 ? 0.7304 0.7480 0.8683 -0.0838 0.0911 0.0061 401 PRO A CA 86 C C . PRO A 18 ? 0.7045 0.7249 0.8580 -0.0815 0.0975 -0.0170 401 PRO A C 87 O O . PRO A 18 ? 0.7352 0.7490 0.8898 -0.0877 0.1062 -0.0243 401 PRO A O 88 C CB . PRO A 18 ? 0.7481 0.7596 0.8967 -0.0834 0.0983 0.0196 401 PRO A CB 89 C CG . PRO A 18 ? 0.7430 0.7623 0.9031 -0.0743 0.0934 0.0238 401 PRO A CG 90 C CD . PRO A 18 ? 0.7459 0.7740 0.8923 -0.0720 0.0805 0.0254 401 PRO A CD 91 N N . PHE A 19 ? 0.6702 0.7009 0.8353 -0.0730 0.0935 -0.0284 402 PHE A N 92 C CA . PHE A 19 ? 0.6667 0.7023 0.8493 -0.0705 0.0989 -0.0507 402 PHE A CA 93 C C . PHE A 19 ? 0.6435 0.6885 0.8219 -0.0676 0.0923 -0.0653 402 PHE A C 94 O O . PHE A 19 ? 0.6228 0.6738 0.8155 -0.0657 0.0956 -0.0839 402 PHE A O 95 C CB . PHE A 19 ? 0.6724 0.7133 0.8742 -0.0630 0.1011 -0.0559 402 PHE A CB 96 C CG . PHE A 19 ? 0.6823 0.7141 0.8907 -0.0641 0.1078 -0.0407 402 PHE A CG 97 C CD1 . PHE A 19 ? 0.7067 0.7271 0.9222 -0.0711 0.1197 -0.0387 402 PHE A CD1 98 C CD2 . PHE A 19 ? 0.6808 0.7153 0.8889 -0.0580 0.1030 -0.0275 402 PHE A CD2 99 C CE1 . PHE A 19 ? 0.7111 0.7228 0.9333 -0.0714 0.1264 -0.0232 402 PHE A CE1 100 C CE2 . PHE A 19 ? 0.6903 0.7169 0.9061 -0.0584 0.1095 -0.0125 402 PHE A CE2 101 C CZ . PHE A 19 ? 0.7063 0.7213 0.9288 -0.0649 0.1210 -0.0099 402 PHE A CZ 102 N N . PHE A 20 ? 0.6595 0.7061 0.8196 -0.0672 0.0831 -0.0570 403 PHE A N 103 C CA . PHE A 20 ? 0.6486 0.7031 0.8042 -0.0635 0.0768 -0.0682 403 PHE A CA 104 C C . PHE A 20 ? 0.6739 0.7211 0.8098 -0.0708 0.0748 -0.0613 403 PHE A C 105 O O . PHE A 20 ? 0.6683 0.7085 0.7904 -0.0758 0.0728 -0.0450 403 PHE A O 106 C CB . PHE A 20 ? 0.6310 0.6961 0.7856 -0.0532 0.0673 -0.0662 403 PHE A CB 107 C CG . PHE A 20 ? 0.6165 0.6909 0.7890 -0.0452 0.0687 -0.0780 403 PHE A CG 108 C CD1 . PHE A 20 ? 0.6058 0.6782 0.7870 -0.0434 0.0722 -0.0714 403 PHE A CD1 109 C CD2 . PHE A 20 ? 0.6064 0.6920 0.7875 -0.0394 0.0666 -0.0961 403 PHE A CD2 110 C CE1 . PHE A 20 ? 0.5936 0.6739 0.7907 -0.0367 0.0742 -0.0839 403 PHE A CE1 111 C CE2 . PHE A 20 ? 0.5966 0.6918 0.7929 -0.0326 0.0673 -0.1083 403 PHE A CE2 112 C CZ . PHE A 20 ? 0.5845 0.6765 0.7883 -0.0316 0.0714 -0.1028 403 PHE A CZ 113 N N . ARG A 21 ? 0.7356 0.7845 0.8710 -0.0716 0.0758 -0.0742 404 ARG A N 114 C CA . ARG A 21 ? 0.7785 0.8215 0.8956 -0.0769 0.0733 -0.0707 404 ARG A CA 115 C C . ARG A 21 ? 0.7404 0.7923 0.8560 -0.0687 0.0649 -0.0755 404 ARG A C 116 O O . ARG A 21 ? 0.6892 0.7523 0.8173 -0.0592 0.0617 -0.0829 404 ARG A O 117 C CB . ARG A 21 ? 0.8412 0.8770 0.9585 -0.0848 0.0830 -0.0804 404 ARG A CB 118 C CG . ARG A 21 ? 0.9071 0.9514 1.0426 -0.0803 0.0866 -0.1003 404 ARG A CG 119 C CD . ARG A 21 ? 0.9670 1.0038 1.0997 -0.0880 0.0956 -0.1084 404 ARG A CD 120 N NE . ARG A 21 ? 1.0356 1.0825 1.1859 -0.0828 0.0972 -0.1266 404 ARG A NE 121 C CZ . ARG A 21 ? 1.1060 1.1616 1.2799 -0.0800 0.1016 -0.1400 404 ARG A CZ 122 N NH1 . ARG A 21 ? 1.1021 1.1562 1.2860 -0.0818 0.1060 -0.1380 404 ARG A NH1 123 N NH2 . ARG A 21 ? 1.0915 1.1578 1.2807 -0.0754 0.1016 -0.1559 404 ARG A NH2 124 N N . THR A 22 ? 0.7561 0.8028 0.8560 -0.0722 0.0617 -0.0713 405 THR A N 125 C CA . THR A 22 ? 0.7461 0.7993 0.8442 -0.0645 0.0549 -0.0742 405 THR A CA 126 C C . THR A 22 ? 0.7597 0.8096 0.8558 -0.0668 0.0586 -0.0851 405 THR A C 127 O O . THR A 22 ? 0.8132 0.8519 0.8976 -0.0767 0.0634 -0.0835 405 THR A O 128 C CB . THR A 22 ? 0.7247 0.7748 0.8079 -0.0653 0.0473 -0.0585 405 THR A CB 129 O OG1 . THR A 22 ? 0.7217 0.7599 0.7883 -0.0770 0.0491 -0.0521 405 THR A OG1 130 C CG2 . THR A 22 ? 0.7208 0.7750 0.8077 -0.0621 0.0437 -0.0470 405 THR A CG2 131 N N . GLU A 23 ? 0.7476 0.8078 0.8550 -0.0572 0.0565 -0.0960 406 GLU A N 132 C CA . GLU A 23 ? 0.7623 0.8204 0.8675 -0.0564 0.0578 -0.1030 406 GLU A CA 133 C C . GLU A 23 ? 0.7296 0.7867 0.8236 -0.0520 0.0503 -0.0929 406 GLU A C 134 O O . GLU A 23 ? 0.7136 0.7799 0.8113 -0.0427 0.0437 -0.0884 406 GLU A O 135 C CB . GLU A 23 ? 0.7897 0.8609 0.9139 -0.0473 0.0584 -0.1183 406 GLU A CB 136 C CG . GLU A 23 ? 0.8265 0.9008 0.9664 -0.0510 0.0660 -0.1304 406 GLU A CG 137 C CD . GLU A 23 ? 0.8791 0.9396 1.0129 -0.0634 0.0763 -0.1321 406 GLU A CD 138 O OE1 . GLU A 23 ? 0.8746 0.9263 0.9971 -0.0672 0.0785 -0.1311 406 GLU A OE1 139 O OE2 . GLU A 23 ? 0.9658 1.0236 1.1060 -0.0694 0.0831 -0.1344 406 GLU A OE2 140 N N . GLN A 24 ? 0.7300 0.7756 0.8107 -0.0589 0.0521 -0.0898 407 GLN A N 141 C CA . GLN A 24 ? 0.7154 0.7575 0.7853 -0.0573 0.0462 -0.0795 407 GLN A CA 142 C C . GLN A 24 ? 0.6957 0.7305 0.7617 -0.0579 0.0492 -0.0847 407 GLN A C 143 O O . GLN A 24 ? 0.6813 0.7063 0.7418 -0.0668 0.0562 -0.0909 407 GLN A O 144 C CB . GLN A 24 ? 0.7578 0.7915 0.8128 -0.0677 0.0439 -0.0662 407 GLN A CB 145 C CG . GLN A 24 ? 0.8165 0.8466 0.8618 -0.0678 0.0379 -0.0554 407 GLN A CG 146 C CD . GLN A 24 ? 0.8482 0.8742 0.8822 -0.0769 0.0339 -0.0419 407 GLN A CD 147 O OE1 . GLN A 24 ? 0.9084 0.9243 0.9282 -0.0885 0.0349 -0.0395 407 GLN A OE1 148 N NE2 . GLN A 24 ? 0.8449 0.8793 0.8851 -0.0714 0.0292 -0.0331 407 GLN A NE2 149 N N . LEU A 25 ? 0.6659 0.7047 0.7343 -0.0482 0.0446 -0.0814 408 LEU A N 150 C CA . LEU A 25 ? 0.6603 0.6920 0.7270 -0.0470 0.0476 -0.0847 408 LEU A CA 151 C C . LEU A 25 ? 0.6690 0.6928 0.7243 -0.0493 0.0436 -0.0727 408 LEU A C 152 O O . LEU A 25 ? 0.6640 0.6942 0.7195 -0.0440 0.0372 -0.0626 408 LEU A O 153 C CB . LEU A 25 ? 0.6421 0.6860 0.7243 -0.0319 0.0465 -0.0914 408 LEU A CB 154 C CG . LEU A 25 ? 0.6305 0.6857 0.7279 -0.0281 0.0491 -0.1044 408 LEU A CG 155 C CD1 . LEU A 25 ? 0.6275 0.6975 0.7392 -0.0123 0.0454 -0.1091 408 LEU A CD1 156 C CD2 . LEU A 25 ? 0.6452 0.6909 0.7430 -0.0380 0.0587 -0.1145 408 LEU A CD2 157 N N . ILE A 26 ? 0.6961 0.7059 0.7424 -0.0575 0.0481 -0.0744 409 ILE A N 158 C CA . ILE A 26 ? 0.7011 0.7033 0.7403 -0.0589 0.0455 -0.0653 409 ILE A CA 159 C C . ILE A 26 ? 0.7015 0.7006 0.7487 -0.0498 0.0496 -0.0701 409 ILE A C 160 O O . ILE A 26 ? 0.7026 0.6970 0.7535 -0.0508 0.0568 -0.0812 409 ILE A O 161 C CB . ILE A 26 ? 0.7263 0.7151 0.7484 -0.0757 0.0459 -0.0617 409 ILE A CB 162 C CG1 . ILE A 26 ? 0.7679 0.7482 0.7861 -0.0771 0.0445 -0.0552 409 ILE A CG1 163 C CG2 . ILE A 26 ? 0.7410 0.7195 0.7558 -0.0858 0.0541 -0.0732 409 ILE A CG2 164 C CD1 . ILE A 26 ? 0.7981 0.7699 0.8011 -0.0926 0.0413 -0.0491 409 ILE A CD1 165 N N . ILE A 27 ? 0.6921 0.6944 0.7432 -0.0402 0.0457 -0.0611 410 ILE A N 166 C CA . ILE A 27 ? 0.7068 0.7090 0.7676 -0.0282 0.0488 -0.0627 410 ILE A CA 167 C C . ILE A 27 ? 0.7289 0.7185 0.7846 -0.0310 0.0500 -0.0542 410 ILE A C 168 O O . ILE A 27 ? 0.7275 0.7187 0.7794 -0.0316 0.0447 -0.0428 410 ILE A O 169 C CB . ILE A 27 ? 0.6982 0.7185 0.7702 -0.0108 0.0435 -0.0599 410 ILE A CB 170 C CG1 . ILE A 27 ? 0.6988 0.7312 0.7786 -0.0087 0.0433 -0.0711 410 ILE A CG1 171 C CG2 . ILE A 27 ? 0.7126 0.7336 0.7936 0.0029 0.0459 -0.0589 410 ILE A CG2 172 C CD1 . ILE A 27 ? 0.6972 0.7488 0.7859 0.0058 0.0368 -0.0699 410 ILE A CD1 173 N N . ARG A 28 ? 0.7608 0.7378 0.8183 -0.0325 0.0576 -0.0600 411 ARG A N 174 C CA . ARG A 28 ? 0.7845 0.7482 0.8404 -0.0341 0.0605 -0.0534 411 ARG A CA 175 C C . ARG A 28 ? 0.7868 0.7499 0.8557 -0.0191 0.0656 -0.0537 411 ARG A C 176 O O . ARG A 28 ? 0.7822 0.7527 0.8600 -0.0108 0.0679 -0.0618 411 ARG A O 177 C CB . ARG A 28 ? 0.8049 0.7505 0.8492 -0.0523 0.0659 -0.0600 411 ARG A CB 178 C CG . ARG A 28 ? 0.8184 0.7649 0.8488 -0.0670 0.0600 -0.0576 411 ARG A CG 179 C CD . ARG A 28 ? 0.8545 0.7840 0.8715 -0.0849 0.0640 -0.0631 411 ARG A CD 180 N NE . ARG A 28 ? 0.8754 0.8072 0.8781 -0.0985 0.0580 -0.0609 411 ARG A NE 181 C CZ . ARG A 28 ? 0.8925 0.8278 0.8879 -0.1039 0.0584 -0.0669 411 ARG A CZ 182 N NH1 . ARG A 28 ? 0.8718 0.8094 0.8740 -0.0975 0.0647 -0.0767 411 ARG A NH1 183 N NH2 . ARG A 28 ? 0.9081 0.8453 0.8905 -0.1158 0.0526 -0.0626 411 ARG A NH2 184 N N . ALA A 29 ? 0.8051 0.7599 0.8760 -0.0155 0.0675 -0.0443 412 ALA A N 185 C CA . ALA A 29 ? 0.8217 0.7741 0.9048 -0.0006 0.0730 -0.0418 412 ALA A CA 186 C C . ALA A 29 ? 0.8498 0.7795 0.9332 -0.0089 0.0831 -0.0444 412 ALA A C 187 O O . ALA A 29 ? 0.8601 0.7808 0.9443 -0.0087 0.0847 -0.0347 412 ALA A O 188 C CB . ALA A 29 ? 0.8113 0.7743 0.8985 0.0141 0.0677 -0.0269 412 ALA A CB 189 N N . PRO A 30 ? 0.8839 0.8037 0.9673 -0.0162 0.0908 -0.0581 413 PRO A N 190 C CA . PRO A 30 ? 0.9188 0.8156 0.9999 -0.0273 0.1009 -0.0635 413 PRO A CA 191 C C . PRO A 30 ? 0.9293 0.8156 1.0239 -0.0156 0.1091 -0.0575 413 PRO A C 192 O O . PRO A 30 ? 0.9145 0.7815 1.0074 -0.0250 0.1162 -0.0583 413 PRO A O 193 C CB . PRO A 30 ? 0.9240 0.8162 1.0030 -0.0347 0.1075 -0.0798 413 PRO A CB 194 C CG . PRO A 30 ? 0.9145 0.8263 1.0047 -0.0196 0.1041 -0.0813 413 PRO A CG 195 C CD . PRO A 30 ? 0.8949 0.8245 0.9829 -0.0130 0.0918 -0.0698 413 PRO A CD 196 N N . LEU A 31 ? 0.9408 0.8396 1.0487 0.0044 0.1082 -0.0515 414 LEU A N 197 C CA . LEU A 31 ? 0.9725 0.8627 1.0939 0.0179 0.1159 -0.0437 414 LEU A CA 198 C C . LEU A 31 ? 0.9573 0.8534 1.0801 0.0285 0.1109 -0.0257 414 LEU A C 199 O O . LEU A 31 ? 0.9676 0.8618 1.1018 0.0441 0.1155 -0.0165 414 LEU A O 200 C CB . LEU A 31 ? 0.9976 0.8987 1.1339 0.0349 0.1185 -0.0476 414 LEU A CB 201 C CG . LEU A 31 ? 1.0215 0.9192 1.1595 0.0268 0.1245 -0.0652 414 LEU A CG 202 C CD1 . LEU A 31 ? 1.0307 0.9451 1.1856 0.0448 0.1243 -0.0677 414 LEU A CD1 203 C CD2 . LEU A 31 ? 1.0377 0.9085 1.1752 0.0146 0.1382 -0.0731 414 LEU A CD2 204 N N . THR A 32 ? 0.9312 0.8340 1.0430 0.0207 0.1021 -0.0201 415 THR A N 205 C CA . THR A 32 ? 0.8991 0.8089 1.0113 0.0305 0.0974 -0.0031 415 THR A CA 206 C C . THR A 32 ? 0.9111 0.8068 1.0175 0.0147 0.0986 0.0015 415 THR A C 207 O O . THR A 32 ? 0.8981 0.7891 0.9948 -0.0035 0.0962 -0.0070 415 THR A O 208 C CB . THR A 32 ? 0.8597 0.7937 0.9665 0.0376 0.0853 0.0002 415 THR A CB 209 O OG1 . THR A 32 ? 0.8459 0.7937 0.9581 0.0480 0.0833 -0.0082 415 THR A OG1 210 C CG2 . THR A 32 ? 0.8525 0.7950 0.9607 0.0518 0.0821 0.0175 415 THR A CG2 211 N N . ASP A 33 ? 0.9266 0.8160 1.0394 0.0220 0.1025 0.0155 416 ASP A N 212 C CA . ASP A 33 ? 0.9679 0.8451 1.0786 0.0081 0.1040 0.0210 416 ASP A CA 213 C C . ASP A 33 ? 0.9509 0.8443 1.0563 0.0100 0.0941 0.0324 416 ASP A C 214 O O . ASP A 33 ? 0.9299 0.8410 1.0345 0.0252 0.0884 0.0384 416 ASP A O 215 C CB . ASP A 33 ? 1.0164 0.8762 1.1392 0.0141 0.1155 0.0303 416 ASP A CB 216 C CG . ASP A 33 ? 1.0570 0.8975 1.1867 0.0109 0.1272 0.0190 416 ASP A CG 217 O OD1 . ASP A 33 ? 1.0842 0.9182 1.2071 -0.0045 0.1277 0.0030 416 ASP A OD1 218 O OD2 . ASP A 33 ? 1.0608 0.8922 1.2028 0.0243 0.1367 0.0267 416 ASP A OD2 219 N N . LYS A 34 ? 0.9478 0.8353 1.0503 -0.0055 0.0922 0.0351 417 LYS A N 220 C CA . LYS A 34 ? 0.9447 0.8447 1.0457 -0.0035 0.0852 0.0481 417 LYS A CA 221 C C . LYS A 34 ? 0.9318 0.8310 1.0420 0.0137 0.0911 0.0645 417 LYS A C 222 O O . LYS A 34 ? 0.9513 0.8391 1.0692 0.0226 0.1003 0.0659 417 LYS A O 223 C CB . LYS A 34 ? 0.9539 0.8482 1.0523 -0.0244 0.0821 0.0474 417 LYS A CB 224 C CG . LYS A 34 ? 0.9972 0.8715 1.1046 -0.0337 0.0911 0.0493 417 LYS A CG 225 C CD . LYS A 34 ? 1.0277 0.9011 1.1336 -0.0535 0.0858 0.0495 417 LYS A CD 226 C CE . LYS A 34 ? 1.0376 0.9130 1.1303 -0.0705 0.0786 0.0346 417 LYS A CE 227 N NZ . LYS A 34 ? 1.0619 0.9322 1.1539 -0.0916 0.0751 0.0323 417 LYS A NZ 228 N N . HIS A 35 ? 0.9200 0.8313 1.0293 0.0194 0.0863 0.0773 418 HIS A N 229 C CA . HIS A 35 ? 0.9280 0.8385 1.0443 0.0349 0.0924 0.0942 418 HIS A CA 230 C C . HIS A 35 ? 0.9236 0.8420 1.0402 0.0325 0.0889 0.1066 418 HIS A C 231 O O . HIS A 35 ? 0.9134 0.8427 1.0240 0.0230 0.0800 0.1029 418 HIS A O 232 C CB . HIS A 35 ? 0.9259 0.8485 1.0401 0.0578 0.0918 0.0981 418 HIS A CB 233 C CG . HIS A 35 ? 0.9296 0.8749 1.0344 0.0648 0.0811 0.0975 418 HIS A CG 234 N ND1 . HIS A 35 ? 0.9261 0.8801 1.0242 0.0548 0.0728 0.0836 418 HIS A ND1 235 C CD2 . HIS A 35 ? 0.9282 0.8888 1.0290 0.0811 0.0781 0.1086 418 HIS A CD2 236 C CE1 . HIS A 35 ? 0.9049 0.8779 0.9969 0.0643 0.0654 0.0860 418 HIS A CE1 237 N NE2 . HIS A 35 ? 0.9049 0.8826 0.9978 0.0801 0.0682 0.1004 418 HIS A NE2 238 N N . ILE A 36 ? 0.9448 0.8573 1.0691 0.0415 0.0968 0.1220 419 ILE A N 239 C CA . ILE A 36 ? 0.9582 0.8755 1.0860 0.0391 0.0964 0.1351 419 ILE A CA 240 C C . ILE A 36 ? 0.9597 0.8943 1.0811 0.0594 0.0940 0.1468 419 ILE A C 241 O O . ILE A 36 ? 0.9999 0.9365 1.1186 0.0776 0.0973 0.1511 419 ILE A O 242 C CB . ILE A 36 ? 0.9797 0.8782 1.1214 0.0350 0.1082 0.1449 419 ILE A CB 243 C CG1 . ILE A 36 ? 0.9872 0.8677 1.1347 0.0148 0.1112 0.1312 419 ILE A CG1 244 C CG2 . ILE A 36 ? 0.9748 0.8789 1.1225 0.0316 0.1084 0.1585 419 ILE A CG2 245 C CD1 . ILE A 36 ? 0.9798 0.8658 1.1228 -0.0064 0.1010 0.1201 419 ILE A CD1 246 N N . TYR A 37 ? 0.9309 0.8784 1.0496 0.0562 0.0879 0.1515 420 TYR A N 247 C CA . TYR A 37 ? 0.9253 0.8877 1.0384 0.0732 0.0871 0.1636 420 TYR A CA 248 C C . TYR A 37 ? 0.9613 0.9202 1.0838 0.0688 0.0927 0.1783 420 TYR A C 249 O O . TYR A 37 ? 0.9447 0.9025 1.0738 0.0513 0.0894 0.1756 420 TYR A O 250 C CB . TYR A 37 ? 0.8976 0.8787 1.0004 0.0735 0.0759 0.1551 420 TYR A CB 251 C CG . TYR A 37 ? 0.8872 0.8828 0.9863 0.0830 0.0746 0.1663 420 TYR A CG 252 C CD1 . TYR A 37 ? 0.8875 0.8916 0.9789 0.1042 0.0773 0.1750 420 TYR A CD1 253 C CD2 . TYR A 37 ? 0.8865 0.8878 0.9896 0.0711 0.0706 0.1682 420 TYR A CD2 254 C CE1 . TYR A 37 ? 0.8868 0.9035 0.9733 0.1128 0.0771 0.1844 420 TYR A CE1 255 C CE2 . TYR A 37 ? 0.8850 0.8988 0.9857 0.0798 0.0706 0.1781 420 TYR A CE2 256 C CZ . TYR A 37 ? 0.8915 0.9126 0.9834 0.1004 0.0743 0.1856 420 TYR A CZ 257 O OH . TYR A 37 ? 0.8970 0.9299 0.9852 0.1088 0.0750 0.1944 420 TYR A OH 258 N N . GLN A 38 ? 1.0157 0.9738 1.1391 0.0850 0.1012 0.1941 421 GLN A N 259 C CA . GLN A 38 ? 1.0469 1.0010 1.1806 0.0832 0.1090 0.2097 421 GLN A CA 260 C C . GLN A 38 ? 1.0459 1.0176 1.1710 0.0963 0.1070 0.2193 421 GLN A C 261 O O . GLN A 38 ? 1.0472 1.0251 1.1616 0.1159 0.1094 0.2258 421 GLN A O 262 C CB . GLN A 38 ? 1.0882 1.0254 1.2300 0.0915 0.1227 0.2216 421 GLN A CB 263 C CG . GLN A 38 ? 1.1155 1.0336 1.2668 0.0782 0.1262 0.2114 421 GLN A CG 264 C CD . GLN A 38 ? 1.1462 1.0459 1.3074 0.0866 0.1410 0.2233 421 GLN A CD 265 O OE1 . GLN A 38 ? 1.1551 1.0565 1.3097 0.1073 0.1458 0.2331 421 GLN A OE1 266 N NE2 . GLN A 38 ? 1.1644 1.0465 1.3420 0.0704 0.1482 0.2224 421 GLN A NE2 267 N N . PRO A 39 ? 1.0533 1.0338 1.1829 0.0856 0.1024 0.2198 422 PRO A N 268 C CA . PRO A 39 ? 1.0714 1.0682 1.1928 0.0978 0.1011 0.2274 422 PRO A CA 269 C C . PRO A 39 ? 1.1420 1.1361 1.2662 0.1110 0.1135 0.2471 422 PRO A C 270 O O . PRO A 39 ? 1.1533 1.1339 1.2920 0.1046 0.1226 0.2563 422 PRO A O 271 C CB . PRO A 39 ? 1.0484 1.0534 1.1773 0.0816 0.0938 0.2231 422 PRO A CB 272 C CG . PRO A 39 ? 1.0421 1.0343 1.1850 0.0612 0.0933 0.2182 422 PRO A CG 273 C CD . PRO A 39 ? 1.0376 1.0142 1.1796 0.0628 0.0981 0.2136 422 PRO A CD 274 N N . TYR A 40 ? 1.2014 1.2082 1.3113 0.1291 0.1139 0.2528 423 TYR A N 275 C CA . TYR A 40 ? 1.2587 1.2652 1.3662 0.1444 0.1256 0.2716 423 TYR A CA 276 C C . TYR A 40 ? 1.2651 1.2824 1.3768 0.1413 0.1264 0.2778 423 TYR A C 277 O O . TYR A 40 ? 1.2257 1.2557 1.3325 0.1372 0.1168 0.2673 423 TYR A O 278 C CB . TYR A 40 ? 1.2898 1.3050 1.3763 0.1669 0.1248 0.2730 423 TYR A CB 279 C CG . TYR A 40 ? 1.3428 1.3587 1.4219 0.1852 0.1366 0.2925 423 TYR A CG 280 C CD1 . TYR A 40 ? 1.3757 1.3788 1.4553 0.1959 0.1470 0.3053 423 TYR A CD1 281 C CD2 . TYR A 40 ? 1.3517 1.3806 1.4227 0.1922 0.1383 0.2986 423 TYR A CD2 282 C CE1 . TYR A 40 ? 1.4103 1.4138 1.4817 0.2133 0.1585 0.3244 423 TYR A CE1 283 C CE2 . TYR A 40 ? 1.3815 1.4109 1.4437 0.2091 0.1499 0.3165 423 TYR A CE2 284 C CZ . TYR A 40 ? 1.4180 1.4349 1.4799 0.2196 0.1598 0.3298 423 TYR A CZ 285 O OH . TYR A 40 ? 1.4643 1.4816 1.5162 0.2368 0.1719 0.3487 423 TYR A OH 286 N N . PRO A 41 ? 1.3100 1.3222 1.4320 0.1432 0.1385 0.2947 424 PRO A N 287 C CA . PRO A 41 ? 1.3319 1.3274 1.4627 0.1469 0.1518 0.3086 424 PRO A CA 288 C C . PRO A 41 ? 1.3319 1.3122 1.4853 0.1261 0.1532 0.3049 424 PRO A C 289 O O . PRO A 41 ? 1.3137 1.2779 1.4726 0.1272 0.1608 0.3087 424 PRO A O 290 C CB . PRO A 41 ? 1.3600 1.3589 1.4936 0.1557 0.1639 0.3270 424 PRO A CB 291 C CG . PRO A 41 ? 1.3481 1.3610 1.4872 0.1459 0.1569 0.3216 424 PRO A CG 292 C CD . PRO A 41 ? 1.3161 1.3391 1.4425 0.1429 0.1412 0.3022 424 PRO A CD 293 N N . SER A 42 ? 1.3281 1.3136 1.4943 0.1077 0.1460 0.2976 425 SER A N 294 C CA . SER A 42 ? 1.3323 1.3064 1.5186 0.0860 0.1449 0.2919 425 SER A CA 295 C C . SER A 42 ? 1.3010 1.2845 1.4860 0.0706 0.1292 0.2747 425 SER A C 296 O O . SER A 42 ? 1.3124 1.3108 1.4850 0.0763 0.1212 0.2697 425 SER A O 297 C CB . SER A 42 ? 1.3576 1.3293 1.5661 0.0785 0.1546 0.3059 425 SER A CB 298 O OG . SER A 42 ? 1.3690 1.3341 1.5975 0.0556 0.1510 0.2986 425 SER A OG 299 N N . GLY A 43 ? 1.2784 1.2528 1.4761 0.0511 0.1256 0.2658 426 GLY A N 300 C CA . GLY A 43 ? 1.2290 1.2108 1.4259 0.0347 0.1113 0.2504 426 GLY A CA 301 C C . GLY A 43 ? 1.2073 1.1750 1.4045 0.0218 0.1083 0.2366 426 GLY A C 302 O O . GLY A 43 ? 1.2136 1.1677 1.4072 0.0294 0.1156 0.2364 426 GLY A O 303 N N . ALA A 44 ? 1.1609 1.1320 1.3624 0.0027 0.0978 0.2252 427 ALA A N 304 C CA . ALA A 44 ? 1.1296 1.0881 1.3301 -0.0117 0.0943 0.2104 427 ALA A CA 305 C C . ALA A 44 ? 1.1177 1.0738 1.2990 -0.0017 0.0915 0.1994 427 ALA A C 306 O O . ALA A 44 ? 1.1222 1.0912 1.2903 0.0100 0.0863 0.1984 427 ALA A O 307 C CB . ALA A 44 ? 1.1095 1.0756 1.3149 -0.0328 0.0822 0.2012 427 ALA A CB 308 N N . ASP A 45 ? 1.0904 1.0298 1.2716 -0.0065 0.0956 0.1908 428 ASP A N 309 C CA . ASP A 45 ? 1.0486 0.9849 1.2146 0.0012 0.0935 0.1794 428 ASP A CA 310 C C . ASP A 45 ? 0.9934 0.9407 1.1480 -0.0077 0.0803 0.1651 428 ASP A C 311 O O . ASP A 45 ? 0.9870 0.9372 1.1458 -0.0256 0.0734 0.1600 428 ASP A O 312 C CB . ASP A 45 ? 1.0854 1.0006 1.2563 -0.0046 0.1013 0.1722 428 ASP A CB 313 C CG . ASP A 45 ? 1.1406 1.0429 1.3215 0.0075 0.1158 0.1862 428 ASP A CG 314 O OD1 . ASP A 45 ? 1.1710 1.0814 1.3513 0.0233 0.1198 0.2014 428 ASP A OD1 315 O OD2 . ASP A 45 ? 1.1511 1.0343 1.3400 0.0014 0.1240 0.1821 428 ASP A OD2 316 N N . VAL A 46 ? 0.9226 0.8766 1.0633 0.0048 0.0770 0.1592 429 VAL A N 317 C CA . VAL A 46 ? 0.8552 0.8183 0.9850 -0.0019 0.0662 0.1456 429 VAL A CA 318 C C . VAL A 46 ? 0.8307 0.7846 0.9527 0.0003 0.0677 0.1325 429 VAL A C 319 O O . VAL A 46 ? 0.8264 0.7823 0.9435 0.0176 0.0709 0.1341 429 VAL A O 320 C CB . VAL A 46 ? 0.8147 0.7967 0.9368 0.0103 0.0605 0.1492 429 VAL A CB 321 C CG1 . VAL A 46 ? 0.8044 0.7945 0.9177 0.0011 0.0501 0.1361 429 VAL A CG1 322 C CG2 . VAL A 46 ? 0.8042 0.7944 0.9352 0.0113 0.0616 0.1639 429 VAL A CG2 323 N N . PRO A 47 ? 0.7991 0.7433 0.9201 -0.0168 0.0656 0.1196 430 PRO A N 324 C CA . PRO A 47 ? 0.7989 0.7352 0.9127 -0.0153 0.0672 0.1062 430 PRO A CA 325 C C . PRO A 47 ? 0.7801 0.7306 0.8823 -0.0114 0.0588 0.0973 430 PRO A C 326 O O . PRO A 47 ? 0.7676 0.7288 0.8660 -0.0194 0.0506 0.0963 430 PRO A O 327 C CB . PRO A 47 ? 0.8099 0.7316 0.9256 -0.0365 0.0680 0.0956 430 PRO A CB 328 C CG . PRO A 47 ? 0.8037 0.7325 0.9230 -0.0507 0.0612 0.1000 430 PRO A CG 329 C CD . PRO A 47 ? 0.8010 0.7427 0.9265 -0.0382 0.0609 0.1164 430 PRO A CD 330 N N . PHE A 48 ? 0.7719 0.7224 0.8699 0.0009 0.0612 0.0913 431 PHE A N 331 C CA . PHE A 48 ? 0.7555 0.7181 0.8446 0.0048 0.0546 0.0814 431 PHE A CA 332 C C . PHE A 48 ? 0.7655 0.7177 0.8516 -0.0022 0.0569 0.0661 431 PHE A C 333 O O . PHE A 48 ? 0.7939 0.7340 0.8847 0.0026 0.0648 0.0648 431 PHE A O 334 C CB . PHE A 48 ? 0.7500 0.7253 0.8377 0.0266 0.0546 0.0872 431 PHE A CB 335 C CG . PHE A 48 ? 0.7437 0.7337 0.8299 0.0322 0.0499 0.0971 431 PHE A CG 336 C CD1 . PHE A 48 ? 0.7596 0.7475 0.8518 0.0329 0.0535 0.1116 431 PHE A CD1 337 C CD2 . PHE A 48 ? 0.7507 0.7563 0.8307 0.0362 0.0429 0.0915 431 PHE A CD2 338 C CE1 . PHE A 48 ? 0.7689 0.7701 0.8604 0.0381 0.0503 0.1207 431 PHE A CE1 339 C CE2 . PHE A 48 ? 0.7480 0.7662 0.8271 0.0413 0.0396 0.1000 431 PHE A CE2 340 C CZ . PHE A 48 ? 0.7581 0.7742 0.8427 0.0424 0.0434 0.1148 431 PHE A CZ 341 N N . GLY A 49 ? 0.7454 0.7018 0.8239 -0.0133 0.0510 0.0550 432 GLY A N 342 C CA . GLY A 49 ? 0.7578 0.7041 0.8321 -0.0220 0.0537 0.0398 432 GLY A CA 343 C C . GLY A 49 ? 0.7553 0.7050 0.8313 -0.0072 0.0569 0.0334 432 GLY A C 344 O O . GLY A 49 ? 0.7517 0.7147 0.8298 0.0091 0.0546 0.0394 432 GLY A O 345 N N . PRO A 50 ? 0.7545 0.6932 0.8297 -0.0131 0.0620 0.0205 433 PRO A N 346 C CA . PRO A 50 ? 0.7551 0.6966 0.8348 0.0002 0.0657 0.0139 433 PRO A CA 347 C C . PRO A 50 ? 0.7442 0.7064 0.8229 0.0122 0.0587 0.0122 433 PRO A C 348 O O . PRO A 50 ? 0.7503 0.7207 0.8349 0.0298 0.0594 0.0159 433 PRO A O 349 C CB . PRO A 50 ? 0.7617 0.6900 0.8380 -0.0132 0.0707 -0.0014 433 PRO A CB 350 C CG . PRO A 50 ? 0.7738 0.6868 0.8462 -0.0304 0.0729 -0.0005 433 PRO A CG 351 C CD . PRO A 50 ? 0.7612 0.6845 0.8311 -0.0330 0.0647 0.0111 433 PRO A CD 352 N N . PRO A 51 ? 0.7338 0.7045 0.8053 0.0031 0.0521 0.0069 434 PRO A N 353 C CA . PRO A 51 ? 0.7239 0.7130 0.7962 0.0139 0.0467 0.0035 434 PRO A CA 354 C C . PRO A 51 ? 0.7195 0.7234 0.7930 0.0279 0.0416 0.0154 434 PRO A C 355 O O . PRO A 51 ? 0.6866 0.7061 0.7612 0.0380 0.0373 0.0118 434 PRO A O 356 C CB . PRO A 51 ? 0.7361 0.7277 0.8012 -0.0005 0.0426 -0.0044 434 PRO A CB 357 C CG . PRO A 51 ? 0.7489 0.7272 0.8075 -0.0175 0.0432 -0.0012 434 PRO A CG 358 C CD . PRO A 51 ? 0.7459 0.7115 0.8090 -0.0157 0.0489 0.0056 434 PRO A CD 359 N N . LEU A 52 ? 0.7265 0.7255 0.8000 0.0282 0.0426 0.0288 435 LEU A N 360 C CA . LEU A 52 ? 0.7206 0.7318 0.7943 0.0419 0.0397 0.0409 435 LEU A CA 361 C C . LEU A 52 ? 0.7382 0.7478 0.8166 0.0585 0.0446 0.0498 435 LEU A C 362 O O . LEU A 52 ? 0.7430 0.7597 0.8203 0.0695 0.0440 0.0619 435 LEU A O 363 C CB . LEU A 52 ? 0.7068 0.7163 0.7785 0.0324 0.0376 0.0511 435 LEU A CB 364 C CG . LEU A 52 ? 0.6977 0.7099 0.7649 0.0172 0.0322 0.0447 435 LEU A CG 365 C CD1 . LEU A 52 ? 0.7015 0.7107 0.7691 0.0070 0.0306 0.0555 435 LEU A CD1 366 C CD2 . LEU A 52 ? 0.6922 0.7210 0.7574 0.0243 0.0268 0.0398 435 LEU A CD2 367 N N . ASP A 53 ? 0.7603 0.7604 0.8436 0.0608 0.0502 0.0443 436 ASP A N 368 C CA . ASP A 53 ? 0.7843 0.7858 0.8728 0.0791 0.0543 0.0514 436 ASP A CA 369 C C . ASP A 53 ? 0.7865 0.8103 0.8727 0.0951 0.0472 0.0496 436 ASP A C 370 O O . ASP A 53 ? 0.7782 0.8120 0.8638 0.0918 0.0421 0.0368 436 ASP A O 371 C CB . ASP A 53 ? 0.8092 0.7974 0.9050 0.0776 0.0614 0.0433 436 ASP A CB 372 C CG . ASP A 53 ? 0.8282 0.8208 0.9308 0.0982 0.0646 0.0493 436 ASP A CG 373 O OD1 . ASP A 53 ? 0.8510 0.8351 0.9565 0.1059 0.0706 0.0631 436 ASP A OD1 374 O OD2 . ASP A 53 ? 0.8277 0.8329 0.9335 0.1067 0.0612 0.0405 436 ASP A OD2 375 N N . ILE A 54 ? 0.8176 0.8490 0.9023 0.1120 0.0473 0.0623 437 ILE A N 376 C CA . ILE A 54 ? 0.8287 0.8824 0.9093 0.1277 0.0400 0.0614 437 ILE A CA 377 C C . ILE A 54 ? 0.8253 0.8895 0.9116 0.1332 0.0365 0.0472 437 ILE A C 378 O O . ILE A 54 ? 0.8333 0.9146 0.9174 0.1355 0.0291 0.0379 437 ILE A O 379 C CB . ILE A 54 ? 0.8514 0.9099 0.9282 0.1466 0.0420 0.0784 437 ILE A CB 380 C CG1 . ILE A 54 ? 0.8474 0.9298 0.9166 0.1615 0.0338 0.0773 437 ILE A CG1 381 C CG2 . ILE A 54 ? 0.8657 0.9160 0.9498 0.1576 0.0485 0.0842 437 ILE A CG2 382 C CD1 . ILE A 54 ? 0.8398 0.9307 0.9019 0.1540 0.0286 0.0740 437 ILE A CD1 383 N N . GLN A 55 ? 0.8346 0.8887 0.9296 0.1351 0.0424 0.0452 438 GLN A N 384 C CA . GLN A 55 ? 0.8344 0.8989 0.9377 0.1417 0.0400 0.0329 438 GLN A CA 385 C C . GLN A 55 ? 0.7830 0.8466 0.8889 0.1254 0.0386 0.0155 438 GLN A C 386 O O . GLN A 55 ? 0.7495 0.8293 0.8598 0.1294 0.0331 0.0039 438 GLN A O 387 C CB . GLN A 55 ? 0.8859 0.9394 0.9995 0.1500 0.0480 0.0373 438 GLN A CB 388 C CG . GLN A 55 ? 0.9336 0.9931 1.0462 0.1709 0.0485 0.0540 438 GLN A CG 389 C CD . GLN A 55 ? 0.9727 1.0601 1.0812 0.1871 0.0379 0.0527 438 GLN A CD 390 O OE1 . GLN A 55 ? 0.9849 1.0870 1.0996 0.1883 0.0320 0.0385 438 GLN A OE1 391 N NE2 . GLN A 55 ? 1.0092 1.1043 1.1071 0.1991 0.0355 0.0667 438 GLN A NE2 392 N N . ILE A 56 ? 0.7690 0.8143 0.8721 0.1071 0.0434 0.0136 439 ILE A N 393 C CA . ILE A 56 ? 0.7543 0.7979 0.8572 0.0911 0.0425 -0.0014 439 ILE A CA 394 C C . ILE A 56 ? 0.7055 0.7651 0.8023 0.0893 0.0340 -0.0046 439 ILE A C 395 O O . ILE A 56 ? 0.6661 0.7347 0.7663 0.0858 0.0312 -0.0175 439 ILE A O 396 C CB . ILE A 56 ? 0.7743 0.7950 0.8750 0.0719 0.0498 -0.0049 439 ILE A CB 397 C CG1 . ILE A 56 ? 0.7758 0.7925 0.8663 0.0567 0.0466 -0.0024 439 ILE A CG1 398 C CG2 . ILE A 56 ? 0.7931 0.7957 0.8986 0.0737 0.0589 0.0015 439 ILE A CG2 399 C CD1 . ILE A 56 ? 0.7783 0.8005 0.8663 0.0458 0.0434 -0.0155 439 ILE A CD1 400 N N . LEU A 57 ? 0.7013 0.7649 0.7907 0.0928 0.0308 0.0070 440 LEU A N 401 C CA . LEU A 57 ? 0.6959 0.7749 0.7806 0.0935 0.0237 0.0043 440 LEU A CA 402 C C . LEU A 57 ? 0.7038 0.8039 0.7929 0.1076 0.0179 -0.0039 440 LEU A C 403 O O . LEU A 57 ? 0.7059 0.8165 0.7966 0.1034 0.0137 -0.0151 440 LEU A O 404 C CB . LEU A 57 ? 0.6901 0.7697 0.7671 0.0962 0.0225 0.0189 440 LEU A CB 405 C CG . LEU A 57 ? 0.6868 0.7503 0.7605 0.0799 0.0257 0.0255 440 LEU A CG 406 C CD1 . LEU A 57 ? 0.6838 0.7489 0.7530 0.0852 0.0256 0.0409 440 LEU A CD1 407 C CD2 . LEU A 57 ? 0.6797 0.7431 0.7518 0.0644 0.0229 0.0160 440 LEU A CD2 408 N N . HIS A 58 ? 0.7091 0.8158 0.8008 0.1243 0.0177 0.0017 441 HIS A N 409 C CA . HIS A 58 ? 0.7013 0.8297 0.7983 0.1383 0.0113 -0.0064 441 HIS A CA 410 C C . HIS A 58 ? 0.6900 0.8207 0.7989 0.1313 0.0118 -0.0234 441 HIS A C 411 O O . HIS A 58 ? 0.6706 0.8182 0.7843 0.1331 0.0060 -0.0355 441 HIS A O 412 C CB . HIS A 58 ? 0.7094 0.8430 0.8076 0.1574 0.0116 0.0041 441 HIS A CB 413 C CG . HIS A 58 ? 0.7008 0.8393 0.7870 0.1689 0.0098 0.0193 441 HIS A CG 414 N ND1 . HIS A 58 ? 0.6915 0.8490 0.7699 0.1764 0.0023 0.0171 441 HIS A ND1 415 C CD2 . HIS A 58 ? 0.7140 0.8410 0.7951 0.1747 0.0154 0.0367 441 HIS A CD2 416 C CE1 . HIS A 58 ? 0.6970 0.8543 0.7647 0.1863 0.0035 0.0328 441 HIS A CE1 417 N NE2 . HIS A 58 ? 0.7057 0.8447 0.7753 0.1856 0.0115 0.0453 441 HIS A NE2 418 N N . GLN A 59 ? 0.7015 0.8148 0.8159 0.1231 0.0194 -0.0247 442 GLN A N 419 C CA . GLN A 59 ? 0.7064 0.8191 0.8319 0.1155 0.0221 -0.0401 442 GLN A CA 420 C C . GLN A 59 ? 0.6919 0.8032 0.8148 0.0991 0.0214 -0.0508 442 GLN A C 421 O O . GLN A 59 ? 0.6960 0.8178 0.8282 0.0971 0.0199 -0.0647 442 GLN A O 422 C CB . GLN A 59 ? 0.7207 0.8128 0.8506 0.1101 0.0318 -0.0385 442 GLN A CB 423 C CG . GLN A 59 ? 0.7376 0.8324 0.8753 0.1275 0.0336 -0.0306 442 GLN A CG 424 C CD . GLN A 59 ? 0.7435 0.8144 0.8841 0.1222 0.0446 -0.0262 442 GLN A CD 425 O OE1 . GLN A 59 ? 0.7401 0.7981 0.8840 0.1087 0.0510 -0.0364 442 GLN A OE1 426 N NE2 . GLN A 59 ? 0.7539 0.8183 0.8932 0.1330 0.0475 -0.0112 442 GLN A NE2 427 N N . VAL A 60 ? 0.6831 0.7821 0.7947 0.0877 0.0226 -0.0436 443 VAL A N 428 C CA . VAL A 60 ? 0.6623 0.7601 0.7703 0.0733 0.0217 -0.0507 443 VAL A CA 429 C C . VAL A 60 ? 0.6570 0.7751 0.7665 0.0802 0.0143 -0.0555 443 VAL A C 430 O O . VAL A 60 ? 0.6425 0.7656 0.7567 0.0728 0.0137 -0.0670 443 VAL A O 431 C CB . VAL A 60 ? 0.6459 0.7271 0.7424 0.0603 0.0241 -0.0407 443 VAL A CB 432 C CG1 . VAL A 60 ? 0.6336 0.7156 0.7262 0.0477 0.0223 -0.0453 443 VAL A CG1 433 C CG2 . VAL A 60 ? 0.6491 0.7104 0.7446 0.0504 0.0317 -0.0407 443 VAL A CG2 434 N N . LEU A 61 ? 0.6534 0.7830 0.7593 0.0945 0.0093 -0.0473 444 LEU A N 435 C CA . LEU A 61 ? 0.6487 0.7981 0.7555 0.1019 0.0024 -0.0535 444 LEU A CA 436 C C . LEU A 61 ? 0.6573 0.8229 0.7776 0.1073 -0.0005 -0.0693 444 LEU A C 437 O O . LEU A 61 ? 0.6822 0.8595 0.8071 0.1048 -0.0039 -0.0805 444 LEU A O 438 C CB . LEU A 61 ? 0.6439 0.8024 0.7419 0.1169 -0.0017 -0.0416 444 LEU A CB 439 C CG . LEU A 61 ? 0.6413 0.8204 0.7379 0.1251 -0.0088 -0.0483 444 LEU A CG 440 C CD1 . LEU A 61 ? 0.6294 0.8065 0.7256 0.1125 -0.0083 -0.0546 444 LEU A CD1 441 C CD2 . LEU A 61 ? 0.6558 0.8412 0.7408 0.1394 -0.0114 -0.0349 444 LEU A CD2 442 N N . ASP A 62 ? 0.6866 0.8530 0.8148 0.1146 0.0009 -0.0700 445 ASP A N 443 C CA . ASP A 62 ? 0.6819 0.8648 0.8259 0.1201 -0.0018 -0.0847 445 ASP A CA 444 C C . ASP A 62 ? 0.6663 0.8430 0.8195 0.1043 0.0031 -0.0985 445 ASP A C 445 O O . ASP A 62 ? 0.6460 0.8379 0.8104 0.1041 0.0000 -0.1124 445 ASP A O 446 C CB . ASP A 62 ? 0.6829 0.8673 0.8348 0.1320 -0.0004 -0.0806 445 ASP A CB 447 C CG . ASP A 62 ? 0.6934 0.8916 0.8393 0.1512 -0.0071 -0.0698 445 ASP A CG 448 O OD1 . ASP A 62 ? 0.6664 0.8818 0.8071 0.1577 -0.0150 -0.0721 445 ASP A OD1 449 O OD2 . ASP A 62 ? 0.7278 0.9191 0.8739 0.1600 -0.0039 -0.0588 445 ASP A OD2 450 N N . LEU A 63 ? 0.6653 0.8198 0.8135 0.0912 0.0113 -0.0947 446 LEU A N 451 C CA . LEU A 63 ? 0.6602 0.8054 0.8120 0.0747 0.0171 -0.1050 446 LEU A CA 452 C C . LEU A 63 ? 0.6383 0.7904 0.7878 0.0686 0.0137 -0.1096 446 LEU A C 453 O O . LEU A 63 ? 0.6047 0.7640 0.7654 0.0635 0.0147 -0.1230 446 LEU A O 454 C CB . LEU A 63 ? 0.6656 0.7859 0.8065 0.0617 0.0248 -0.0974 446 LEU A CB 455 C CG . LEU A 63 ? 0.6701 0.7782 0.8089 0.0438 0.0311 -0.1047 446 LEU A CG 456 C CD1 . LEU A 63 ? 0.6747 0.7872 0.8289 0.0420 0.0361 -0.1197 446 LEU A CD1 457 C CD2 . LEU A 63 ? 0.6827 0.7682 0.8080 0.0323 0.0368 -0.0961 446 LEU A CD2 458 N N . GLN A 64 ? 0.6326 0.7824 0.7693 0.0696 0.0104 -0.0984 447 GLN A N 459 C CA . GLN A 64 ? 0.6382 0.7923 0.7721 0.0644 0.0080 -0.1006 447 GLN A CA 460 C C . GLN A 64 ? 0.6322 0.8085 0.7770 0.0731 0.0022 -0.1131 447 GLN A C 461 O O . GLN A 64 ? 0.6152 0.7950 0.7676 0.0656 0.0035 -0.1239 447 GLN A O 462 C CB . GLN A 64 ? 0.6430 0.7916 0.7625 0.0663 0.0058 -0.0850 447 GLN A CB 463 C CG . GLN A 64 ? 0.6498 0.7962 0.7654 0.0578 0.0059 -0.0838 447 GLN A CG 464 C CD . GLN A 64 ? 0.6622 0.8018 0.7654 0.0589 0.0048 -0.0672 447 GLN A CD 465 O OE1 . GLN A 64 ? 0.6958 0.8200 0.7923 0.0505 0.0080 -0.0577 447 GLN A OE1 466 N NE2 . GLN A 64 ? 0.6688 0.8201 0.7692 0.0690 0.0006 -0.0643 447 GLN A NE2 467 N N . ILE A 65 ? 0.6405 0.8318 0.7861 0.0887 -0.0040 -0.1117 448 ILE A N 468 C CA . ILE A 65 ? 0.6341 0.8490 0.7893 0.0982 -0.0110 -0.1243 448 ILE A CA 469 C C . ILE A 65 ? 0.6266 0.8490 0.8012 0.0938 -0.0092 -0.1411 448 ILE A C 470 O O . ILE A 65 ? 0.6264 0.8624 0.8116 0.0923 -0.0118 -0.1549 448 ILE A O 471 C CB . ILE A 65 ? 0.6477 0.8774 0.7979 0.1168 -0.0184 -0.1178 448 ILE A CB 472 C CG1 . ILE A 65 ? 0.6550 0.8807 0.7871 0.1213 -0.0200 -0.1035 448 ILE A CG1 473 C CG2 . ILE A 65 ? 0.6391 0.8955 0.8009 0.1265 -0.0267 -0.1328 448 ILE A CG2 474 C CD1 . ILE A 65 ? 0.6672 0.8998 0.7904 0.1381 -0.0242 -0.0914 448 ILE A CD1 475 N N . ALA A 66 ? 0.6374 0.8508 0.8178 0.0914 -0.0039 -0.1403 449 ALA A N 476 C CA . ALA A 66 ? 0.6317 0.8512 0.8317 0.0873 -0.0007 -0.1555 449 ALA A CA 477 C C . ALA A 66 ? 0.6514 0.8614 0.8557 0.0706 0.0061 -0.1640 449 ALA A C 478 O O . ALA A 66 ? 0.6585 0.8807 0.8798 0.0680 0.0062 -0.1792 449 ALA A O 479 C CB . ALA A 66 ? 0.6215 0.8312 0.8256 0.0885 0.0048 -0.1517 449 ALA A CB 480 N N . ILE A 67 ? 0.6685 0.8574 0.8578 0.0597 0.0116 -0.1538 450 ILE A N 481 C CA . ILE A 67 ? 0.6776 0.8561 0.8672 0.0446 0.0180 -0.1581 450 ILE A CA 482 C C . ILE A 67 ? 0.6956 0.8875 0.8913 0.0456 0.0138 -0.1660 450 ILE A C 483 O O . ILE A 67 ? 0.6793 0.8735 0.8882 0.0378 0.0181 -0.1782 450 ILE A O 484 C CB . ILE A 67 ? 0.6728 0.8286 0.8433 0.0344 0.0225 -0.1435 450 ILE A CB 485 C CG1 . ILE A 67 ? 0.6799 0.8204 0.8469 0.0290 0.0292 -0.1406 450 ILE A CG1 486 C CG2 . ILE A 67 ? 0.6737 0.8213 0.8427 0.0213 0.0272 -0.1451 450 ILE A CG2 487 C CD1 . ILE A 67 ? 0.6863 0.8078 0.8340 0.0225 0.0310 -0.1254 450 ILE A CD1 488 N N . GLU A 68 ? 0.7252 0.9251 0.9117 0.0549 0.0064 -0.1595 451 GLU A N 489 C CA . GLU A 68 ? 0.7543 0.9676 0.9459 0.0572 0.0023 -0.1680 451 GLU A CA 490 C C . GLU A 68 ? 0.7590 0.9933 0.9712 0.0613 -0.0009 -0.1872 451 GLU A C 491 O O . GLU A 68 ? 0.7704 1.0114 0.9928 0.0570 -0.0003 -0.1989 451 GLU A O 492 C CB . GLU A 68 ? 0.7811 1.0019 0.9590 0.0691 -0.0050 -0.1587 451 GLU A CB 493 C CG . GLU A 68 ? 0.8013 1.0050 0.9618 0.0648 -0.0023 -0.1413 451 GLU A CG 494 C CD . GLU A 68 ? 0.8418 1.0543 0.9908 0.0767 -0.0085 -0.1337 451 GLU A CD 495 O OE1 . GLU A 68 ? 0.8464 1.0692 0.9982 0.0789 -0.0107 -0.1416 451 GLU A OE1 496 O OE2 . GLU A 68 ? 0.9017 1.1102 1.0390 0.0837 -0.0102 -0.1200 451 GLU A OE2 497 N N . ASN A 69 ? 0.7588 1.0037 0.9783 0.0700 -0.0045 -0.1902 452 ASN A N 498 C CA . ASN A 69 ? 0.7647 1.0325 1.0053 0.0753 -0.0092 -0.2076 452 ASN A CA 499 C C . ASN A 69 ? 0.7302 0.9947 0.9911 0.0646 -0.0009 -0.2198 452 ASN A C 500 O O . ASN A 69 ? 0.7325 1.0164 1.0144 0.0674 -0.0041 -0.2354 452 ASN A O 501 C CB . ASN A 69 ? 0.7950 1.0781 1.0349 0.0917 -0.0178 -0.2038 452 ASN A CB 502 C CG . ASN A 69 ? 0.8195 1.1324 1.0744 0.1014 -0.0279 -0.2193 452 ASN A CG 503 O OD1 . ASN A 69 ? 0.8638 1.1869 1.1167 0.1021 -0.0326 -0.2265 452 ASN A OD1 504 N ND2 . ASN A 69 ? 0.8267 1.1544 1.0972 0.1090 -0.0314 -0.2248 452 ASN A ND2 505 N N . ILE A 70 ? 0.7042 0.9456 0.9593 0.0525 0.0095 -0.2130 453 ILE A N 506 C CA . ILE A 70 ? 0.6934 0.9298 0.9656 0.0419 0.0192 -0.2235 453 ILE A CA 507 C C . ILE A 70 ? 0.7115 0.9559 1.0001 0.0347 0.0214 -0.2384 453 ILE A C 508 O O . ILE A 70 ? 0.7246 0.9640 1.0050 0.0308 0.0213 -0.2357 453 ILE A O 509 C CB . ILE A 70 ? 0.6752 0.8842 0.9339 0.0292 0.0303 -0.2131 453 ILE A CB 510 C CG1 . ILE A 70 ? 0.6688 0.8685 0.9157 0.0344 0.0304 -0.2016 453 ILE A CG1 511 C CG2 . ILE A 70 ? 0.6790 0.8826 0.9540 0.0174 0.0415 -0.2246 453 ILE A CG2 512 C CD1 . ILE A 70 ? 0.6681 0.8415 0.8959 0.0229 0.0386 -0.1896 453 ILE A CD1 513 N N . THR A 71 ? 0.7301 0.9871 1.0437 0.0330 0.0239 -0.2541 454 THR A N 514 C CA . THR A 71 ? 0.7261 0.9898 1.0599 0.0247 0.0282 -0.2699 454 THR A CA 515 C C . THR A 71 ? 0.7231 0.9773 1.0725 0.0136 0.0413 -0.2764 454 THR A C 516 O O . THR A 71 ? 0.7213 0.9740 1.0740 0.0159 0.0440 -0.2748 454 THR A O 517 C CB . THR A 71 ? 0.7343 1.0283 1.0878 0.0340 0.0172 -0.2863 454 THR A CB 518 O OG1 . THR A 71 ? 0.7471 1.0567 1.1159 0.0418 0.0136 -0.2918 454 THR A OG1 519 C CG2 . THR A 71 ? 0.7430 1.0464 1.0790 0.0452 0.0050 -0.2803 454 THR A CG2 520 N N . ALA A 72 ? 0.7250 0.9713 1.0832 0.0016 0.0503 -0.2829 455 ALA A N 521 C CA . ALA A 72 ? 0.7231 0.9620 1.0988 -0.0094 0.0640 -0.2909 455 ALA A CA 522 C C . ALA A 72 ? 0.7265 0.9812 1.1309 -0.0133 0.0653 -0.3099 455 ALA A C 523 O O . ALA A 72 ? 0.7177 0.9817 1.1225 -0.0104 0.0579 -0.3142 455 ALA A O 524 C CB . ALA A 72 ? 0.7185 0.9286 1.0746 -0.0216 0.0759 -0.2779 455 ALA A CB 525 N N . SER A 73 ? 0.7463 1.0038 1.1754 -0.0201 0.0751 -0.3219 456 SER A N 526 C CA . SER A 73 ? 0.7795 1.0496 1.2386 -0.0262 0.0788 -0.3404 456 SER A CA 527 C C . SER A 73 ? 0.8098 1.0579 1.2730 -0.0414 0.0970 -0.3392 456 SER A C 528 O O . SER A 73 ? 0.7943 1.0253 1.2489 -0.0470 0.1078 -0.3311 456 SER A O 529 C CB . SER A 73 ? 0.7758 1.0731 1.2669 -0.0208 0.0741 -0.3579 456 SER A CB 530 O OG . SER A 73 ? 0.7964 1.0891 1.2898 -0.0200 0.0802 -0.3540 456 SER A OG 531 N N . TYR A 74 ? 0.8810 1.1287 1.3556 -0.0478 0.1007 -0.3468 457 TYR A N 532 C CA . TYR A 74 ? 0.9711 1.1991 1.4525 -0.0617 0.1185 -0.3462 457 TYR A CA 533 C C . TYR A 74 ? 1.0408 1.2834 1.5569 -0.0664 0.1215 -0.3666 457 TYR A C 534 O O . TYR A 74 ? 1.0423 1.2952 1.5610 -0.0627 0.1125 -0.3730 457 TYR A O 535 C CB . TYR A 74 ? 0.9945 1.1980 1.4461 -0.0657 0.1221 -0.3273 457 TYR A CB 536 C CG . TYR A 74 ? 1.0295 1.2113 1.4841 -0.0790 0.1407 -0.3231 457 TYR A CG 537 C CD1 . TYR A 74 ? 1.0494 1.2275 1.5195 -0.0855 0.1480 -0.3291 457 TYR A CD1 538 C CD2 . TYR A 74 ? 1.0500 1.2146 1.4922 -0.0851 0.1519 -0.3133 457 TYR A CD2 539 C CE1 . TYR A 74 ? 1.0810 1.2387 1.5543 -0.0971 0.1659 -0.3239 457 TYR A CE1 540 C CE2 . TYR A 74 ? 1.0879 1.2327 1.5310 -0.0968 0.1693 -0.3086 457 TYR A CE2 541 C CZ . TYR A 74 ? 1.1051 1.2465 1.5640 -0.1026 0.1763 -0.3132 457 TYR A CZ 542 O OH . TYR A 74 ? 1.1394 1.2608 1.5994 -0.1136 0.1943 -0.3072 457 TYR A OH 543 N N . ASP A 75 ? 1.1382 1.3806 1.6807 -0.0751 0.1349 -0.3771 458 ASP A N 544 C CA . ASP A 75 ? 1.1860 1.4494 1.7690 -0.0783 0.1360 -0.4006 458 ASP A CA 545 C C . ASP A 75 ? 1.1992 1.4947 1.7922 -0.0656 0.1163 -0.4125 458 ASP A C 546 O O . ASP A 75 ? 1.2042 1.5062 1.7896 -0.0578 0.1103 -0.4071 458 ASP A O 547 C CB . ASP A 75 ? 1.2044 1.4603 1.7969 -0.0861 0.1424 -0.4063 458 ASP A CB 548 C CG . ASP A 75 ? 1.2326 1.4575 1.8163 -0.0978 0.1622 -0.3931 458 ASP A CG 549 O OD1 . ASP A 75 ? 1.2557 1.4653 1.8250 -0.1007 0.1711 -0.3807 458 ASP A OD1 550 O OD2 . ASP A 75 ? 1.2502 1.4661 1.8415 -0.1040 0.1693 -0.3953 458 ASP A OD2 551 N N . ASN A 76 ? 1.2086 1.5236 1.8168 -0.0631 0.1063 -0.4277 459 ASN A N 552 C CA . ASN A 76 ? 1.2139 1.5602 1.8280 -0.0504 0.0865 -0.4381 459 ASN A CA 553 C C . ASN A 76 ? 1.1985 1.5436 1.7782 -0.0399 0.0723 -0.4259 459 ASN A C 554 O O . ASN A 76 ? 1.1965 1.5646 1.7728 -0.0276 0.0555 -0.4295 459 ASN A O 555 C CB . ASN A 76 ? 1.2249 1.5973 1.8782 -0.0540 0.0831 -0.4649 459 ASN A CB 556 C CG . ASN A 76 ? 1.2068 1.6131 1.8842 -0.0456 0.0704 -0.4788 459 ASN A CG 557 O OD1 . ASN A 76 ? 1.1951 1.6032 1.8672 -0.0391 0.0689 -0.4697 459 ASN A OD1 558 N ND2 . ASN A 76 ? 1.1994 1.6329 1.9047 -0.0459 0.0616 -0.5015 459 ASN A ND2 559 N N . GLU A 77 ? 1.1876 1.5064 1.7423 -0.0443 0.0794 -0.4106 460 GLU A N 560 C CA . GLU A 77 ? 1.1564 1.4716 1.6794 -0.0354 0.0683 -0.3981 460 GLU A CA 561 C C . GLU A 77 ? 1.0801 1.3918 1.5755 -0.0253 0.0607 -0.3798 460 GLU A C 562 O O . GLU A 77 ? 1.0513 1.3556 1.5474 -0.0273 0.0672 -0.3737 460 GLU A O 563 C CB . GLU A 77 ? 1.2049 1.4925 1.7118 -0.0435 0.0792 -0.3859 460 GLU A CB 564 C CG . GLU A 77 ? 1.2329 1.5184 1.7644 -0.0536 0.0889 -0.4008 460 GLU A CG 565 C CD . GLU A 77 ? 1.2681 1.5251 1.7831 -0.0603 0.1002 -0.3856 460 GLU A CD 566 O OE1 . GLU A 77 ? 1.2760 1.5119 1.7676 -0.0619 0.1060 -0.3647 460 GLU A OE1 567 O OE2 . GLU A 77 ? 1.2745 1.5305 1.8006 -0.0639 0.1035 -0.3948 460 GLU A OE2 568 N N . THR A 78 ? 1.0015 1.3177 1.4731 -0.0149 0.0480 -0.3715 461 THR A N 569 C CA . THR A 78 ? 0.9539 1.2629 1.3964 -0.0057 0.0419 -0.3519 461 THR A CA 570 C C . THR A 78 ? 0.8876 1.1723 1.3010 -0.0082 0.0456 -0.3332 461 THR A C 571 O O . THR A 78 ? 0.8521 1.1361 1.2626 -0.0090 0.0444 -0.3357 461 THR A O 572 C CB . THR A 78 ? 0.9569 1.2913 1.3943 0.0099 0.0241 -0.3546 461 THR A CB 573 O OG1 . THR A 78 ? 0.9667 1.3130 1.4020 0.0136 0.0159 -0.3630 461 THR A OG1 574 C CG2 . THR A 78 ? 0.9632 1.3224 1.4284 0.0139 0.0193 -0.3697 461 THR A CG2 575 N N . VAL A 79 ? 0.8396 1.1048 1.2324 -0.0096 0.0503 -0.3149 462 VAL A N 576 C CA . VAL A 79 ? 0.8172 1.0600 1.1829 -0.0122 0.0534 -0.2957 462 VAL A CA 577 C C . VAL A 79 ? 0.7798 1.0235 1.1204 -0.0009 0.0429 -0.2808 462 VAL A C 578 O O . VAL A 79 ? 0.7357 0.9782 1.0717 0.0021 0.0421 -0.2755 462 VAL A O 579 C CB . VAL A 79 ? 0.8248 1.0425 1.1849 -0.0246 0.0680 -0.2856 462 VAL A CB 580 C CG1 . VAL A 79 ? 0.8279 1.0253 1.1630 -0.0277 0.0703 -0.2669 462 VAL A CG1 581 C CG2 . VAL A 79 ? 0.8307 1.0474 1.2174 -0.0355 0.0801 -0.2998 462 VAL A CG2 582 N N . THR A 80 ? 0.7458 0.9907 1.0714 0.0049 0.0360 -0.2743 463 THR A N 583 C CA . THR A 80 ? 0.7470 0.9901 1.0480 0.0148 0.0276 -0.2583 463 THR A CA 584 C C . THR A 80 ? 0.7210 0.9402 1.0008 0.0086 0.0333 -0.2393 463 THR A C 585 O O . THR A 80 ? 0.7153 0.9222 0.9988 -0.0012 0.0420 -0.2389 463 THR A O 586 C CB . THR A 80 ? 0.7677 1.0295 1.0648 0.0266 0.0158 -0.2630 463 THR A CB 587 O OG1 . THR A 80 ? 0.7780 1.0358 1.0771 0.0218 0.0193 -0.2669 463 THR A OG1 588 C CG2 . THR A 80 ? 0.7650 1.0538 1.0812 0.0341 0.0075 -0.2813 463 THR A CG2 589 N N . LEU A 81 ? 0.6983 0.9116 0.9570 0.0147 0.0284 -0.2234 464 LEU A N 590 C CA . LEU A 81 ? 0.6843 0.8788 0.9228 0.0105 0.0312 -0.2050 464 LEU A CA 591 C C . LEU A 81 ? 0.6926 0.8893 0.9296 0.0123 0.0297 -0.2046 464 LEU A C 592 O O . LEU A 81 ? 0.6826 0.8643 0.9131 0.0052 0.0355 -0.1945 464 LEU A O 593 C CB . LEU A 81 ? 0.6770 0.8677 0.8961 0.0176 0.0256 -0.1898 464 LEU A CB 594 C CG . LEU A 81 ? 0.6784 0.8516 0.8776 0.0136 0.0271 -0.1704 464 LEU A CG 595 C CD1 . LEU A 81 ? 0.6800 0.8345 0.8771 -0.0005 0.0368 -0.1653 464 LEU A CD1 596 C CD2 . LEU A 81 ? 0.6890 0.8604 0.8730 0.0210 0.0218 -0.1582 464 LEU A CD2 597 N N . GLN A 82 ? 0.6979 0.9138 0.9415 0.0217 0.0223 -0.2161 465 GLN A N 598 C CA . GLN A 82 ? 0.6943 0.9134 0.9362 0.0245 0.0210 -0.2177 465 GLN A CA 599 C C . GLN A 82 ? 0.6904 0.9027 0.9488 0.0138 0.0306 -0.2271 465 GLN A C 600 O O . GLN A 82 ? 0.6920 0.8976 0.9475 0.0126 0.0338 -0.2227 465 GLN A O 601 C CB . GLN A 82 ? 0.7084 0.9507 0.9516 0.0372 0.0105 -0.2291 465 GLN A CB 602 C CG . GLN A 82 ? 0.7229 0.9706 0.9472 0.0495 0.0018 -0.2166 465 GLN A CG 603 C CD . GLN A 82 ? 0.7378 0.9902 0.9650 0.0524 -0.0011 -0.2164 465 GLN A CD 604 O OE1 . GLN A 82 ? 0.7551 0.9962 0.9689 0.0535 -0.0006 -0.2009 465 GLN A OE1 605 N NE2 . GLN A 82 ? 0.7522 1.0214 0.9981 0.0537 -0.0039 -0.2342 465 GLN A NE2 606 N N . ASP A 83 ? 0.6948 0.9082 0.9716 0.0063 0.0362 -0.2394 466 ASP A N 607 C CA . ASP A 83 ? 0.7028 0.9072 0.9965 -0.0047 0.0473 -0.2470 466 ASP A CA 608 C C . ASP A 83 ? 0.7019 0.8821 0.9854 -0.0141 0.0570 -0.2292 466 ASP A C 609 O O . ASP A 83 ? 0.7132 0.8841 1.0053 -0.0206 0.0654 -0.2297 466 ASP A O 610 C CB . ASP A 83 ? 0.7160 0.9282 1.0330 -0.0103 0.0515 -0.2643 466 ASP A CB 611 C CG . ASP A 83 ? 0.7351 0.9735 1.0670 -0.0024 0.0421 -0.2845 466 ASP A CG 612 O OD1 . ASP A 83 ? 0.7244 0.9730 1.0562 0.0030 0.0367 -0.2915 466 ASP A OD1 613 O OD2 . ASP A 83 ? 0.7627 1.0120 1.1068 -0.0018 0.0401 -0.2935 466 ASP A OD2 614 N N . ILE A 84 ? 0.6953 0.8657 0.9613 -0.0149 0.0559 -0.2137 467 ILE A N 615 C CA . ILE A 84 ? 0.6891 0.8383 0.9450 -0.0246 0.0642 -0.1978 467 ILE A CA 616 C C . ILE A 84 ? 0.6753 0.8153 0.9086 -0.0219 0.0599 -0.1769 467 ILE A C 617 O O . ILE A 84 ? 0.6819 0.8059 0.9067 -0.0296 0.0656 -0.1632 467 ILE A O 618 C CB . ILE A 84 ? 0.7115 0.8537 0.9674 -0.0316 0.0695 -0.1983 467 ILE A CB 619 C CG1 . ILE A 84 ? 0.7045 0.8516 0.9473 -0.0250 0.0614 -0.1939 467 ILE A CG1 620 C CG2 . ILE A 84 ? 0.7186 0.8690 1.0000 -0.0356 0.0757 -0.2183 467 ILE A CG2 621 C CD1 . ILE A 84 ? 0.7095 0.8474 0.9502 -0.0322 0.0677 -0.1933 467 ILE A CD1 622 N N . CYS A 85 ? 0.6690 0.8192 0.8930 -0.0112 0.0501 -0.1740 468 CYS A N 623 C CA . CYS A 85 ? 0.6558 0.7984 0.8594 -0.0084 0.0458 -0.1544 468 CYS A CA 624 C C . CYS A 85 ? 0.6453 0.7833 0.8470 -0.0077 0.0474 -0.1453 468 CYS A C 625 O O . CYS A 85 ? 0.6419 0.7837 0.8570 -0.0073 0.0510 -0.1553 468 CYS A O 626 C CB . CYS A 85 ? 0.6621 0.8165 0.8564 0.0030 0.0359 -0.1535 468 CYS A CB 627 S SG . CYS A 85 ? 0.7142 0.8879 0.9133 0.0160 0.0290 -0.1641 468 CYS A SG 628 N N . LEU A 86 ? 0.6232 0.7526 0.8090 -0.0079 0.0451 -0.1264 469 LEU A N 629 C CA . LEU A 86 ? 0.6165 0.7433 0.7990 -0.0049 0.0450 -0.1150 469 LEU A CA 630 C C . LEU A 86 ? 0.6197 0.7601 0.7976 0.0077 0.0376 -0.1178 469 LEU A C 631 O O . LEU A 86 ? 0.5917 0.7354 0.7579 0.0128 0.0313 -0.1118 469 LEU A O 632 C CB . LEU A 86 ? 0.6101 0.7243 0.7786 -0.0105 0.0447 -0.0939 469 LEU A CB 633 C CG . LEU A 86 ? 0.6058 0.7171 0.7710 -0.0078 0.0443 -0.0786 469 LEU A CG 634 C CD1 . LEU A 86 ? 0.6026 0.7109 0.7821 -0.0095 0.0519 -0.0818 469 LEU A CD1 635 C CD2 . LEU A 86 ? 0.6086 0.7096 0.7612 -0.0146 0.0427 -0.0595 469 LEU A CD2 636 N N . ALA A 87 ? 0.6217 0.7692 0.8085 0.0127 0.0390 -0.1266 470 ALA A N 637 C CA . ALA A 87 ? 0.6072 0.7683 0.7889 0.0249 0.0328 -0.1311 470 ALA A CA 638 C C . ALA A 87 ? 0.5887 0.7480 0.7720 0.0282 0.0364 -0.1263 470 ALA A C 639 O O . ALA A 87 ? 0.6055 0.7700 0.7999 0.0296 0.0396 -0.1404 470 ALA A O 640 C CB . ALA A 87 ? 0.6139 0.7901 0.8056 0.0289 0.0299 -0.1532 470 ALA A CB 641 N N . PRO A 88 ? 0.5814 0.7335 0.7545 0.0293 0.0361 -0.1066 471 PRO A N 642 C CA . PRO A 88 ? 0.5933 0.7407 0.7704 0.0306 0.0415 -0.0992 471 PRO A CA 643 C C . PRO A 88 ? 0.6137 0.7715 0.7875 0.0421 0.0402 -0.1041 471 PRO A C 644 O O . PRO A 88 ? 0.5986 0.7520 0.7758 0.0437 0.0454 -0.0970 471 PRO A O 645 C CB . PRO A 88 ? 0.5859 0.7232 0.7543 0.0269 0.0408 -0.0758 471 PRO A CB 646 C CG . PRO A 88 ? 0.5802 0.7213 0.7353 0.0295 0.0333 -0.0721 471 PRO A CG 647 C CD . PRO A 88 ? 0.5856 0.7324 0.7450 0.0281 0.0317 -0.0901 471 PRO A CD 648 N N . LEU A 89 ? 0.6486 0.8201 0.8156 0.0504 0.0337 -0.1156 472 LEU A N 649 C CA . LEU A 89 ? 0.6795 0.8617 0.8409 0.0616 0.0325 -0.1216 472 LEU A CA 650 C C . LEU A 89 ? 0.7241 0.9108 0.8988 0.0610 0.0374 -0.1416 472 LEU A C 651 O O . LEU A 89 ? 0.7357 0.9248 0.9088 0.0671 0.0407 -0.1436 472 LEU A O 652 C CB . LEU A 89 ? 0.6774 0.8736 0.8251 0.0717 0.0234 -0.1252 472 LEU A CB 653 C CG . LEU A 89 ? 0.6777 0.8707 0.8100 0.0771 0.0205 -0.1042 472 LEU A CG 654 C CD1 . LEU A 89 ? 0.6871 0.8909 0.8085 0.0850 0.0123 -0.1066 472 LEU A CD1 655 C CD2 . LEU A 89 ? 0.6872 0.8806 0.8132 0.0846 0.0241 -0.0957 472 LEU A CD2 656 N N . SER A 90 ? 0.7699 0.9570 0.9584 0.0535 0.0387 -0.1565 473 SER A N 657 C CA . SER A 90 ? 0.8407 1.0313 1.0445 0.0514 0.0440 -0.1772 473 SER A CA 658 C C . SER A 90 ? 0.8727 1.0546 1.0950 0.0390 0.0500 -0.1839 473 SER A C 659 O O . SER A 90 ? 0.8849 1.0635 1.1055 0.0340 0.0474 -0.1780 473 SER A O 660 C CB . SER A 90 ? 0.8618 1.0726 1.0613 0.0599 0.0361 -0.1972 473 SER A CB 661 O OG . SER A 90 ? 0.9158 1.1335 1.1327 0.0542 0.0369 -0.2199 473 SER A OG 662 N N A PRO A 91 ? 0.9007 1.0776 1.1405 0.0341 0.0591 -0.1958 474 PRO A N 663 N N B PRO A 91 ? 0.9037 1.0814 1.1436 0.0342 0.0587 -0.1968 474 PRO A N 664 C CA A PRO A 91 ? 0.9109 1.0786 1.1696 0.0224 0.0667 -0.2022 474 PRO A CA 665 C CA B PRO A 91 ? 0.9143 1.0838 1.1732 0.0227 0.0659 -0.2045 474 PRO A CA 666 C C A PRO A 91 ? 0.9164 1.0952 1.1825 0.0192 0.0617 -0.2193 474 PRO A C 667 C C B PRO A 91 ? 0.9196 1.0999 1.1842 0.0197 0.0603 -0.2194 474 PRO A C 668 O O A PRO A 91 ? 0.9192 1.0897 1.1967 0.0098 0.0672 -0.2198 474 PRO A O 669 O O B PRO A 91 ? 0.9233 1.0954 1.2004 0.0100 0.0662 -0.2208 474 PRO A O 670 C CB A PRO A 91 ? 0.9220 1.0856 1.1980 0.0204 0.0767 -0.2153 474 PRO A CB 671 C CB B PRO A 91 ? 0.9259 1.0932 1.2024 0.0209 0.0752 -0.2199 474 PRO A CB 672 C CG A PRO A 91 ? 0.9202 1.0841 1.1852 0.0293 0.0769 -0.2071 474 PRO A CG 673 C CG B PRO A 91 ? 0.9252 1.0903 1.1911 0.0290 0.0765 -0.2095 474 PRO A CG 674 C CD A PRO A 91 ? 0.9111 1.0883 1.1541 0.0389 0.0646 -0.2017 474 PRO A CD 675 C CD B PRO A 91 ? 0.9151 1.0926 1.1584 0.0387 0.0645 -0.2025 474 PRO A CD 676 N N A TYR A 92 ? 0.9329 1.1307 1.1926 0.0273 0.0518 -0.2325 475 TYR A N 677 N N B TYR A 92 ? 0.9353 1.1341 1.1916 0.0280 0.0497 -0.2299 475 TYR A N 678 C CA A TYR A 92 ? 0.9539 1.1650 1.2230 0.0254 0.0464 -0.2495 475 TYR A CA 679 C CA B TYR A 92 ? 0.9503 1.1600 1.2108 0.0266 0.0433 -0.2398 475 TYR A CA 680 C C A TYR A 92 ? 0.9403 1.1595 1.1930 0.0317 0.0358 -0.2401 475 TYR A C 681 C C B TYR A 92 ? 0.9318 1.1548 1.1733 0.0373 0.0310 -0.2342 475 TYR A C 682 O O A TYR A 92 ? 0.9645 1.1876 1.1983 0.0412 0.0296 -0.2290 475 TYR A O 683 O O B TYR A 92 ? 0.9157 1.1556 1.1608 0.0412 0.0233 -0.2483 475 TYR A O 684 C CB A TYR A 92 ? 0.9738 1.2030 1.2526 0.0293 0.0429 -0.2753 475 TYR A CB 685 C CB B TYR A 92 ? 0.9836 1.2065 1.2650 0.0237 0.0438 -0.2675 475 TYR A CB 686 C CG A TYR A 92 ? 0.9913 1.2128 1.2916 0.0213 0.0544 -0.2892 475 TYR A CG 687 C CG B TYR A 92 ? 0.9941 1.2059 1.2985 0.0108 0.0547 -0.2746 475 TYR A CG 688 C CD1 A TYR A 92 ? 1.0019 1.2210 1.3259 0.0107 0.0608 -0.3025 475 TYR A CD1 689 C CD1 B TYR A 92 ? 0.9850 1.1942 1.2947 0.0046 0.0554 -0.2722 475 TYR A CD1 690 C CD2 A TYR A 92 ? 1.0044 1.2203 1.3025 0.0243 0.0600 -0.2891 475 TYR A CD2 691 C CD2 B TYR A 92 ? 1.0047 1.2082 1.3260 0.0049 0.0655 -0.2837 475 TYR A CD2 692 C CE1 A TYR A 92 ? 1.0168 1.2276 1.3620 0.0032 0.0724 -0.3150 475 TYR A CE1 693 C CE1 B TYR A 92 ? 0.9826 1.1814 1.3125 -0.0068 0.0664 -0.2779 475 TYR A CE1 694 C CE2 A TYR A 92 ? 1.0172 1.2246 1.3362 0.0171 0.0716 -0.3019 475 TYR A CE2 695 C CE2 B TYR A 92 ? 1.0029 1.1955 1.3456 -0.0066 0.0766 -0.2892 475 TYR A CE2 696 C CZ A TYR A 92 ? 1.0312 1.2359 1.3739 0.0065 0.0777 -0.3147 475 TYR A CZ 697 C CZ B TYR A 92 ? 0.9976 1.1881 1.3439 -0.0124 0.0770 -0.2860 475 TYR A CZ 698 O OH A TYR A 92 ? 1.0596 1.2547 1.4246 -0.0007 0.0904 -0.3273 475 TYR A OH 699 O OH B TYR A 92 ? 1.0171 1.1965 1.3840 -0.0237 0.0890 -0.2907 475 TYR A OH 700 N N A ASN A 93 ? 0.9146 1.1358 1.1755 0.0265 0.0347 -0.2446 476 ASN A N 701 N N B ASN A 93 ? 0.9211 1.1363 1.1439 0.0421 0.0294 -0.2130 476 ASN A N 702 C CA A ASN A 93 ? 0.9019 1.1294 1.1500 0.0320 0.0261 -0.2366 476 ASN A CA 703 C CA B ASN A 93 ? 0.8929 1.1190 1.0973 0.0533 0.0193 -0.2058 476 ASN A CA 704 C C A ASN A 93 ? 0.9105 1.1452 1.1372 0.0447 0.0178 -0.2263 476 ASN A C 705 C C B ASN A 93 ? 0.8784 1.1094 1.0835 0.0525 0.0139 -0.2066 476 ASN A C 706 O O A ASN A 93 ? 0.8964 1.1409 1.1203 0.0514 0.0154 -0.2345 476 ASN A O 707 O O B ASN A 93 ? 0.8743 1.0968 1.0908 0.0425 0.0188 -0.2082 476 ASN A O 708 C CB A ASN A 93 ? 0.8855 1.1312 1.1474 0.0330 0.0204 -0.2560 476 ASN A CB 709 C CB B ASN A 93 ? 0.8728 1.0872 1.0601 0.0565 0.0204 -0.1817 476 ASN A CB 710 C CG A ASN A 93 ? 0.8674 1.1063 1.1513 0.0206 0.0292 -0.2656 476 ASN A CG 711 C CG B ASN A 93 ? 0.8592 1.0835 1.0282 0.0684 0.0115 -0.1736 476 ASN A CG 712 O OD1 A ASN A 93 ? 0.8573 1.0781 1.1460 0.0113 0.0399 -0.2588 476 ASN A OD1 713 O OD1 B ASN A 93 ? 0.8571 1.0821 1.0216 0.0689 0.0071 -0.1680 476 ASN A OD1 714 N ND2 A ASN A 93 ? 0.8525 1.1065 1.1505 0.0206 0.0251 -0.2810 476 ASN A ND2 715 N ND2 B ASN A 93 ? 0.8534 1.0847 1.0117 0.0781 0.0099 -0.1726 476 ASN A ND2 716 N N A THR A 94 ? 0.9110 1.1407 1.1226 0.0478 0.0142 -0.2089 477 THR A N 717 N N B THR A 94 ? 0.8608 1.1048 1.0533 0.0635 0.0045 -0.2047 477 THR A N 718 C CA A THR A 94 ? 0.9135 1.1494 1.1054 0.0599 0.0072 -0.1979 477 THR A CA 719 C CA B THR A 94 ? 0.8369 1.0874 1.0309 0.0650 -0.0007 -0.2061 477 THR A CA 720 C C A THR A 94 ? 0.8932 1.1238 1.0729 0.0621 0.0037 -0.1817 477 THR A C 721 C C B THR A 94 ? 0.8348 1.0766 1.0115 0.0690 -0.0029 -0.1847 477 THR A C 722 O O A THR A 94 ? 0.9061 1.1371 1.0921 0.0585 0.0028 -0.1851 477 THR A O 723 O O B THR A 94 ? 0.8034 1.0492 0.9798 0.0715 -0.0069 -0.1837 477 THR A O 724 C CB A THR A 94 ? 0.9210 1.1468 1.1040 0.0611 0.0120 -0.1856 477 THR A CB 725 C CB B THR A 94 ? 0.8192 1.0946 1.0165 0.0749 -0.0104 -0.2233 477 THR A CB 726 O OG1 A THR A 94 ? 0.9434 1.1699 1.1396 0.0575 0.0177 -0.1999 477 THR A OG1 727 O OG1 B THR A 94 ? 0.8007 1.0824 1.0106 0.0724 -0.0128 -0.2310 477 THR A OG1 728 C CG2 A THR A 94 ? 0.9268 1.1616 1.0910 0.0746 0.0057 -0.1778 477 THR A CG2 729 C CG2 B THR A 94 ? 0.8188 1.1032 0.9951 0.0895 -0.0183 -0.2129 477 THR A CG2 730 N N A ASN A 95 ? 0.8706 1.0959 1.0336 0.0679 0.0025 -0.1643 478 ASN A N 731 N N B ASN A 95 ? 0.8328 1.0629 0.9969 0.0696 0.0000 -0.1679 478 ASN A N 732 C CA A ASN A 95 ? 0.8604 1.0794 1.0113 0.0702 0.0000 -0.1479 478 ASN A CA 733 C CA B ASN A 95 ? 0.8378 1.0571 0.9881 0.0707 -0.0004 -0.1474 478 ASN A CA 734 C C A ASN A 95 ? 0.8063 1.0059 0.9598 0.0571 0.0067 -0.1373 478 ASN A C 735 C C B ASN A 95 ? 0.7936 0.9934 0.9470 0.0572 0.0066 -0.1373 478 ASN A C 736 O O A ASN A 95 ? 0.7984 0.9874 0.9501 0.0524 0.0115 -0.1276 478 ASN A O 737 O O B ASN A 95 ? 0.7868 0.9761 0.9385 0.0526 0.0114 -0.1277 478 ASN A O 738 C CB A ASN A 95 ? 0.9082 1.1274 1.0426 0.0798 -0.0019 -0.1334 478 ASN A CB 739 C CB B ASN A 95 ? 0.8883 1.1079 1.0228 0.0800 -0.0020 -0.1338 478 ASN A CB 740 C CG A ASN A 95 ? 0.9750 1.2114 1.1001 0.0943 -0.0098 -0.1369 478 ASN A CG 741 C CG B ASN A 95 ? 0.9590 1.1956 1.0839 0.0945 -0.0099 -0.1370 478 ASN A CG 742 O OD1 A ASN A 95 ? 0.9865 1.2332 1.1161 0.0976 -0.0149 -0.1459 478 ASN A OD1 743 O OD1 B ASN A 95 ? 0.9702 1.2173 1.0995 0.0979 -0.0150 -0.1460 478 ASN A OD1 744 N ND2 A ASN A 95 ? 1.0613 1.3011 1.1733 0.1036 -0.0106 -0.1291 478 ASN A ND2 745 N ND2 B ASN A 95 ? 1.0503 1.2901 1.1621 0.1037 -0.0105 -0.1290 478 ASN A ND2 746 N N . CYS A 96 ? 0.7658 0.9615 0.9236 0.0514 0.0072 -0.1395 479 CYS A N 747 C CA . CYS A 96 ? 0.7334 0.9116 0.8924 0.0384 0.0136 -0.1314 479 CYS A CA 748 C C . CYS A 96 ? 0.6857 0.8517 0.8297 0.0371 0.0133 -0.1107 479 CYS A C 749 O O . CYS A 96 ? 0.6808 0.8505 0.8148 0.0455 0.0086 -0.1032 479 CYS A O 750 C CB . CYS A 96 ? 0.7562 0.9340 0.9230 0.0331 0.0149 -0.1404 479 CYS A CB 751 S SG . CYS A 96 ? 0.8324 1.0221 1.0218 0.0303 0.0174 -0.1649 479 CYS A SG 752 N N . THR A 97 ? 0.6431 0.7950 0.7865 0.0264 0.0185 -0.1013 480 THR A N 753 C CA . THR A 97 ? 0.6198 0.7604 0.7511 0.0228 0.0181 -0.0825 480 THR A CA 754 C C . THR A 97 ? 0.6175 0.7522 0.7428 0.0193 0.0171 -0.0806 480 THR A C 755 O O . THR A 97 ? 0.6161 0.7458 0.7461 0.0111 0.0208 -0.0879 480 THR A O 756 C CB . THR A 97 ? 0.6045 0.7334 0.7376 0.0123 0.0233 -0.0737 480 THR A CB 757 O OG1 . THR A 97 ? 0.6058 0.7393 0.7465 0.0161 0.0255 -0.0761 480 THR A OG1 758 C CG2 . THR A 97 ? 0.6074 0.7268 0.7289 0.0082 0.0216 -0.0542 480 THR A CG2 759 N N . ILE A 98 ? 0.6095 0.7450 0.7252 0.0258 0.0130 -0.0714 481 ILE A N 760 C CA . ILE A 98 ? 0.6088 0.7368 0.7184 0.0227 0.0127 -0.0679 481 ILE A CA 761 C C . ILE A 98 ? 0.5920 0.7116 0.6908 0.0210 0.0114 -0.0502 481 ILE A C 762 O O . ILE A 98 ? 0.6113 0.7364 0.7063 0.0307 0.0085 -0.0431 481 ILE A O 763 C CB . ILE A 98 ? 0.6221 0.7604 0.7336 0.0339 0.0094 -0.0757 481 ILE A CB 764 C CG1 . ILE A 98 ? 0.6352 0.7863 0.7597 0.0373 0.0092 -0.0940 481 ILE A CG1 765 C CG2 . ILE A 98 ? 0.6314 0.7601 0.7392 0.0296 0.0111 -0.0737 481 ILE A CG2 766 C CD1 . ILE A 98 ? 0.6610 0.8270 0.7881 0.0508 0.0040 -0.1010 481 ILE A CD1 767 N N . LEU A 99 ? 0.5812 0.6880 0.6751 0.0087 0.0136 -0.0431 482 LEU A N 768 C CA . LEU A 99 ? 0.5881 0.6875 0.6733 0.0055 0.0118 -0.0272 482 LEU A CA 769 C C . LEU A 99 ? 0.5914 0.6861 0.6716 0.0071 0.0114 -0.0270 482 LEU A C 770 O O . LEU A 99 ? 0.6101 0.6971 0.6886 -0.0004 0.0139 -0.0329 482 LEU A O 771 C CB . LEU A 99 ? 0.5818 0.6711 0.6634 -0.0082 0.0132 -0.0196 482 LEU A CB 772 C CG . LEU A 99 ? 0.5864 0.6789 0.6748 -0.0100 0.0149 -0.0195 482 LEU A CG 773 C CD1 . LEU A 99 ? 0.5971 0.6803 0.6806 -0.0227 0.0154 -0.0091 482 LEU A CD1 774 C CD2 . LEU A 99 ? 0.5664 0.6680 0.6592 0.0005 0.0133 -0.0143 482 LEU A CD2 775 N N . SER A 100 ? 0.5937 0.6928 0.6719 0.0176 0.0091 -0.0202 483 SER A N 776 C CA . SER A 100 ? 0.6078 0.7029 0.6831 0.0217 0.0094 -0.0192 483 SER A CA 777 C C . SER A 100 ? 0.6066 0.7034 0.6783 0.0304 0.0079 -0.0058 483 SER A C 778 O O . SER A 100 ? 0.5877 0.6937 0.6603 0.0382 0.0063 -0.0020 483 SER A O 779 C CB . SER A 100 ? 0.6112 0.7158 0.6926 0.0312 0.0093 -0.0328 483 SER A CB 780 O OG . SER A 100 ? 0.6258 0.7302 0.7060 0.0400 0.0092 -0.0301 483 SER A OG 781 N N . VAL A 101 ? 0.6060 0.6936 0.6743 0.0289 0.0093 0.0010 484 VAL A N 782 C CA . VAL A 101 ? 0.6024 0.6911 0.6685 0.0385 0.0091 0.0137 484 VAL A CA 783 C C . VAL A 101 ? 0.5691 0.6707 0.6360 0.0560 0.0079 0.0110 484 VAL A C 784 O O . VAL A 101 ? 0.5673 0.6733 0.6315 0.0652 0.0078 0.0210 484 VAL A O 785 C CB . VAL A 101 ? 0.6252 0.7009 0.6892 0.0346 0.0120 0.0215 484 VAL A CB 786 C CG1 . VAL A 101 ? 0.6567 0.7225 0.7188 0.0187 0.0118 0.0281 484 VAL A CG1 787 C CG2 . VAL A 101 ? 0.6406 0.7107 0.7060 0.0348 0.0146 0.0115 484 VAL A CG2 788 N N . LEU A 102 ? 0.5463 0.6547 0.6168 0.0605 0.0069 -0.0024 485 LEU A N 789 C CA . LEU A 102 ? 0.5618 0.6850 0.6327 0.0770 0.0042 -0.0060 485 LEU A CA 790 C C . LEU A 102 ? 0.5688 0.7046 0.6385 0.0826 0.0016 -0.0076 485 LEU A C 791 O O . LEU A 102 ? 0.5894 0.7370 0.6556 0.0968 -0.0006 -0.0066 485 LEU A O 792 C CB . LEU A 102 ? 0.5620 0.6913 0.6394 0.0802 0.0032 -0.0205 485 LEU A CB 793 C CG . LEU A 102 ? 0.5857 0.7071 0.6653 0.0820 0.0060 -0.0198 485 LEU A CG 794 C CD1 . LEU A 102 ? 0.5969 0.7178 0.6721 0.0948 0.0067 -0.0067 485 LEU A CD1 795 C CD2 . LEU A 102 ? 0.5839 0.6874 0.6637 0.0652 0.0107 -0.0203 485 LEU A CD2 796 N N . ASN A 103 ? 0.5556 0.6887 0.6277 0.0719 0.0022 -0.0096 486 ASN A N 797 C CA . ASN A 103 ? 0.5572 0.7000 0.6294 0.0763 0.0011 -0.0108 486 ASN A CA 798 C C . ASN A 103 ? 0.5679 0.7101 0.6342 0.0819 0.0024 0.0046 486 ASN A C 799 O O . ASN A 103 ? 0.5805 0.7322 0.6451 0.0895 0.0020 0.0038 486 ASN A O 800 C CB . ASN A 103 ? 0.5526 0.6926 0.6309 0.0643 0.0023 -0.0176 486 ASN A CB 801 C CG . ASN A 103 ? 0.5584 0.7107 0.6431 0.0684 0.0009 -0.0344 486 ASN A CG 802 O OD1 . ASN A 103 ? 0.5682 0.7333 0.6508 0.0808 -0.0015 -0.0388 486 ASN A OD1 803 N ND2 . ASN A 103 ? 0.5591 0.7077 0.6512 0.0579 0.0027 -0.0441 486 ASN A ND2 804 N N . TYR A 104 ? 0.5729 0.7042 0.6367 0.0781 0.0044 0.0180 487 TYR A N 805 C CA . TYR A 104 ? 0.5731 0.7044 0.6325 0.0853 0.0064 0.0333 487 TYR A CA 806 C C . TYR A 104 ? 0.5902 0.7318 0.6431 0.1028 0.0058 0.0337 487 TYR A C 807 O O . TYR A 104 ? 0.6331 0.7788 0.6810 0.1115 0.0077 0.0433 487 TYR A O 808 C CB . TYR A 104 ? 0.5674 0.6851 0.6274 0.0772 0.0089 0.0462 487 TYR A CB 809 C CG . TYR A 104 ? 0.5535 0.6620 0.6180 0.0602 0.0088 0.0488 487 TYR A CG 810 C CD1 . TYR A 104 ? 0.5429 0.6552 0.6110 0.0555 0.0082 0.0493 487 TYR A CD1 811 C CD2 . TYR A 104 ? 0.5550 0.6511 0.6200 0.0492 0.0095 0.0515 487 TYR A CD2 812 C CE1 . TYR A 104 ? 0.5345 0.6397 0.6062 0.0408 0.0074 0.0532 487 TYR A CE1 813 C CE2 . TYR A 104 ? 0.5501 0.6393 0.6173 0.0338 0.0084 0.0541 487 TYR A CE2 814 C CZ . TYR A 104 ? 0.5410 0.6353 0.6114 0.0300 0.0070 0.0556 487 TYR A CZ 815 O OH . TYR A 104 ? 0.5536 0.6422 0.6259 0.0155 0.0052 0.0594 487 TYR A OH 816 N N . PHE A 105 ? 0.5958 0.7419 0.6486 0.1082 0.0032 0.0238 488 PHE A N 817 C CA . PHE A 105 ? 0.6108 0.7695 0.6574 0.1254 0.0010 0.0226 488 PHE A CA 818 C C . PHE A 105 ? 0.6192 0.7940 0.6671 0.1305 -0.0039 0.0052 488 PHE A C 819 O O . PHE A 105 ? 0.6442 0.8312 0.6890 0.1429 -0.0077 0.0000 488 PHE A O 820 C CB . PHE A 105 ? 0.6044 0.7572 0.6518 0.1291 0.0018 0.0260 488 PHE A CB 821 C CG . PHE A 105 ? 0.6096 0.7455 0.6576 0.1223 0.0072 0.0409 488 PHE A CG 822 C CD1 . PHE A 105 ? 0.6018 0.7239 0.6559 0.1060 0.0089 0.0388 488 PHE A CD1 823 C CD2 . PHE A 105 ? 0.6193 0.7533 0.6615 0.1316 0.0108 0.0567 488 PHE A CD2 824 C CE1 . PHE A 105 ? 0.6057 0.7131 0.6607 0.0987 0.0133 0.0512 488 PHE A CE1 825 C CE2 . PHE A 105 ? 0.6185 0.7371 0.6634 0.1244 0.0161 0.0697 488 PHE A CE2 826 C CZ . PHE A 105 ? 0.6110 0.7167 0.6627 0.1076 0.0169 0.0664 488 PHE A CZ 827 N N . GLN A 106 ? 0.6056 0.7808 0.6590 0.1208 -0.0039 -0.0034 489 GLN A N 828 C CA . GLN A 106 ? 0.6144 0.8032 0.6719 0.1228 -0.0076 -0.0212 489 GLN A CA 829 C C . GLN A 106 ? 0.6075 0.8032 0.6712 0.1247 -0.0116 -0.0343 489 GLN A C 830 O O . GLN A 106 ? 0.6285 0.8404 0.6932 0.1330 -0.0163 -0.0468 489 GLN A O 831 C CB . GLN A 106 ? 0.6341 0.8366 0.6828 0.1357 -0.0091 -0.0221 489 GLN A CB 832 C CG . GLN A 106 ? 0.6524 0.8491 0.6985 0.1326 -0.0042 -0.0124 489 GLN A CG 833 C CD . GLN A 106 ? 0.6896 0.8747 0.7309 0.1328 0.0000 0.0080 489 GLN A CD 834 O OE1 . GLN A 106 ? 0.7403 0.9285 0.7727 0.1445 0.0000 0.0167 489 GLN A OE1 835 N NE2 . GLN A 106 ? 0.6790 0.8513 0.7267 0.1199 0.0034 0.0160 489 GLN A NE2 836 N N . ASN A 107 ? 0.5966 0.7802 0.6652 0.1165 -0.0094 -0.0319 490 ASN A N 837 C CA . ASN A 107 ? 0.5960 0.7839 0.6726 0.1173 -0.0116 -0.0431 490 ASN A CA 838 C C . ASN A 107 ? 0.5995 0.8038 0.6733 0.1347 -0.0168 -0.0450 490 ASN A C 839 O O . ASN A 107 ? 0.5855 0.8027 0.6673 0.1381 -0.0211 -0.0591 490 ASN A O 840 C CB . ASN A 107 ? 0.5925 0.7845 0.6802 0.1077 -0.0120 -0.0604 490 ASN A CB 841 C CG . ASN A 107 ? 0.5919 0.7684 0.6816 0.0914 -0.0070 -0.0575 490 ASN A CG 842 O OD1 . ASN A 107 ? 0.5820 0.7437 0.6671 0.0847 -0.0037 -0.0450 490 ASN A OD1 843 N ND2 . ASN A 107 ? 0.5997 0.7799 0.6967 0.0849 -0.0064 -0.0690 490 ASN A ND2 844 N N . SER A 108 ? 0.6205 0.8243 0.6832 0.1456 -0.0164 -0.0301 491 SER A N 845 C CA . SER A 108 ? 0.6502 0.8696 0.7070 0.1636 -0.0213 -0.0285 491 SER A CA 846 C C . SER A 108 ? 0.6588 0.8684 0.7133 0.1699 -0.0180 -0.0137 491 SER A C 847 O O . SER A 108 ? 0.6585 0.8530 0.7077 0.1666 -0.0122 0.0013 491 SER A O 848 C CB . SER A 108 ? 0.6722 0.9014 0.7156 0.1735 -0.0228 -0.0236 491 SER A CB 849 O OG . SER A 108 ? 0.6902 0.9315 0.7238 0.1915 -0.0264 -0.0169 491 SER A OG 850 N N . HIS A 109 ? 0.6657 0.8844 0.7256 0.1792 -0.0215 -0.0178 492 HIS A N 851 C CA . HIS A 109 ? 0.6760 0.8864 0.7351 0.1875 -0.0180 -0.0038 492 HIS A CA 852 C C . HIS A 109 ? 0.6942 0.9058 0.7383 0.2010 -0.0167 0.0137 492 HIS A C 853 O O . HIS A 109 ? 0.6841 0.8796 0.7259 0.2009 -0.0097 0.0294 492 HIS A O 854 C CB . HIS A 109 ? 0.6837 0.9073 0.7522 0.1976 -0.0227 -0.0113 492 HIS A CB 855 C CG . HIS A 109 ? 0.6655 0.8859 0.7503 0.1853 -0.0219 -0.0266 492 HIS A CG 856 N ND1 . HIS A 109 ? 0.6609 0.8613 0.7531 0.1754 -0.0144 -0.0237 492 HIS A ND1 857 C CD2 . HIS A 109 ? 0.6683 0.9030 0.7635 0.1816 -0.0271 -0.0452 492 HIS A CD2 858 C CE1 . HIS A 109 ? 0.6655 0.8678 0.7707 0.1662 -0.0145 -0.0392 492 HIS A CE1 859 N NE2 . HIS A 109 ? 0.6711 0.8941 0.7794 0.1698 -0.0220 -0.0523 492 HIS A NE2 860 N N . SER A 110 ? 0.7241 0.9545 0.7580 0.2121 -0.0226 0.0106 493 SER A N 861 C CA . SER A 110 ? 0.7494 0.9821 0.7671 0.2257 -0.0208 0.0270 493 SER A CA 862 C C . SER A 110 ? 0.7366 0.9531 0.7487 0.2166 -0.0130 0.0384 493 SER A C 863 O O . SER A 110 ? 0.7689 0.9761 0.7743 0.2226 -0.0070 0.0563 493 SER A O 864 C CB . SER A 110 ? 0.7594 1.0170 0.7656 0.2398 -0.0291 0.0197 493 SER A CB 865 O OG . SER A 110 ? 0.7592 1.0237 0.7667 0.2306 -0.0321 0.0038 493 SER A OG 866 N N . VAL A 111 ? 0.7157 0.9287 0.7323 0.2022 -0.0127 0.0289 494 VAL A N 867 C CA . VAL A 111 ? 0.6934 0.8924 0.7075 0.1930 -0.0058 0.0396 494 VAL A CA 868 C C . VAL A 111 ? 0.6854 0.8632 0.7069 0.1834 0.0007 0.0512 494 VAL A C 869 O O . VAL A 111 ? 0.6852 0.8526 0.7030 0.1834 0.0069 0.0669 494 VAL A O 870 C CB . VAL A 111 ? 0.6608 0.8610 0.6797 0.1800 -0.0070 0.0271 494 VAL A CB 871 C CG1 . VAL A 111 ? 0.6552 0.8415 0.6742 0.1704 -0.0004 0.0392 494 VAL A CG1 872 C CG2 . VAL A 111 ? 0.6482 0.8679 0.6596 0.1892 -0.0123 0.0156 494 VAL A CG2 873 N N . LEU A 112 ? 0.6928 0.8644 0.7249 0.1752 0.0000 0.0428 495 LEU A N 874 C CA . LEU A 112 ? 0.7106 0.8626 0.7493 0.1666 0.0060 0.0514 495 LEU A CA 875 C C . LEU A 112 ? 0.7481 0.8953 0.7827 0.1799 0.0106 0.0677 495 LEU A C 876 O O . LEU A 112 ? 0.7478 0.8782 0.7849 0.1741 0.0176 0.0798 495 LEU A O 877 C CB . LEU A 112 ? 0.7127 0.8611 0.7624 0.1576 0.0045 0.0376 495 LEU A CB 878 C CG . LEU A 112 ? 0.7297 0.8571 0.7863 0.1446 0.0108 0.0413 495 LEU A CG 879 C CD1 . LEU A 112 ? 0.7263 0.8418 0.7825 0.1282 0.0134 0.0449 495 LEU A CD1 880 C CD2 . LEU A 112 ? 0.7404 0.8673 0.8064 0.1388 0.0096 0.0263 495 LEU A CD2 881 N N . ASP A 113 ? 0.7882 0.9506 0.8168 0.1977 0.0067 0.0681 496 ASP A N 882 C CA . ASP A 113 ? 0.8371 0.9969 0.8605 0.2130 0.0110 0.0850 496 ASP A CA 883 C C . ASP A 113 ? 0.8956 1.0575 0.9056 0.2223 0.0147 0.1004 496 ASP A C 884 O O . ASP A 113 ? 0.9648 1.1209 0.9708 0.2333 0.0204 0.1167 496 ASP A O 885 C CB . ASP A 113 ? 0.8289 1.0050 0.8519 0.2292 0.0048 0.0802 496 ASP A CB 886 C CG . ASP A 113 ? 0.8245 0.9936 0.8626 0.2238 0.0053 0.0723 496 ASP A CG 887 O OD1 . ASP A 113 ? 0.8038 0.9521 0.8501 0.2108 0.0126 0.0753 496 ASP A OD1 888 O OD2 . ASP A 113 ? 0.8299 1.0151 0.8721 0.2326 -0.0014 0.0626 496 ASP A OD2 889 N N . HIS A 114 ? 0.9245 1.0940 0.9279 0.2186 0.0124 0.0957 497 HIS A N 890 C CA . HIS A 114 ? 0.9674 1.1381 0.9590 0.2261 0.0173 0.1096 497 HIS A CA 891 C C . HIS A 114 ? 0.9751 1.1264 0.9708 0.2234 0.0276 0.1286 497 HIS A C 892 O O . HIS A 114 ? 0.9486 1.0843 0.9565 0.2074 0.0310 0.1283 497 HIS A O 893 C CB . HIS A 114 ? 1.0102 1.1833 1.0011 0.2155 0.0167 0.1028 497 HIS A CB 894 C CG . HIS A 114 ? 1.0735 1.2666 1.0538 0.2240 0.0102 0.0912 497 HIS A CG 895 N ND1 . HIS A 114 ? 1.1277 1.3247 1.1000 0.2250 0.0131 0.0937 497 HIS A ND1 896 C CD2 . HIS A 114 ? 1.1087 1.3191 1.0859 0.2311 0.0014 0.0762 497 HIS A CD2 897 C CE1 . HIS A 114 ? 1.1493 1.3643 1.1130 0.2322 0.0065 0.0801 497 HIS A CE1 898 N NE2 . HIS A 114 ? 1.1459 1.3698 1.1127 0.2358 -0.0010 0.0691 497 HIS A NE2 899 N N . LYS A 115 ? 1.0180 1.1705 1.0032 0.2387 0.0328 0.1450 498 LYS A N 900 C CA . LYS A 115 ? 1.0414 1.1762 1.0307 0.2371 0.0440 0.1641 498 LYS A CA 901 C C . LYS A 115 ? 1.0532 1.1936 1.0275 0.2531 0.0498 0.1802 498 LYS A C 902 O O . LYS A 115 ? 1.0490 1.2055 1.0085 0.2697 0.0453 0.1795 498 LYS A O 903 C CB . LYS A 115 ? 1.0655 1.1870 1.0647 0.2380 0.0478 0.1695 498 LYS A CB 904 C CG . LYS A 115 ? 1.0996 1.2323 1.0916 0.2574 0.0442 0.1712 498 LYS A CG 905 C CD . LYS A 115 ? 1.1361 1.2531 1.1365 0.2628 0.0523 0.1844 498 LYS A CD 906 C CE . LYS A 115 ? 1.1321 1.2317 1.1506 0.2444 0.0544 0.1755 498 LYS A CE 907 N NZ . LYS A 115 ? 1.1503 1.2296 1.1796 0.2454 0.0650 0.1881 498 LYS A NZ 908 N N . LYS A 116 ? 1.0979 1.2257 1.0764 0.2475 0.0596 0.1943 499 LYS A N 909 C CA . LYS A 116 ? 1.1610 1.2901 1.1273 0.2615 0.0682 0.2124 499 LYS A CA 910 C C . LYS A 116 ? 1.1802 1.2896 1.1567 0.2606 0.0799 0.2308 499 LYS A C 911 O O . LYS A 116 ? 1.1510 1.2455 1.1444 0.2437 0.0841 0.2316 499 LYS A O 912 C CB . LYS A 116 ? 1.1867 1.3196 1.1503 0.2558 0.0709 0.2127 499 LYS A CB 913 C CG . LYS A 116 ? 1.2096 1.3605 1.1639 0.2563 0.0611 0.1946 499 LYS A CG 914 C CD . LYS A 116 ? 1.2514 1.4206 1.1844 0.2764 0.0560 0.1919 499 LYS A CD 915 C CE . LYS A 116 ? 1.2753 1.4613 1.2004 0.2751 0.0478 0.1732 499 LYS A CE 916 N NZ . LYS A 116 ? 1.2979 1.4867 1.2135 0.2782 0.0550 0.1794 499 LYS A NZ 917 N N . GLY A 117 ? 1.2526 1.3625 1.2191 0.2788 0.0852 0.2454 500 GLY A N 918 C CA . GLY A 117 ? 1.3207 1.4116 1.2967 0.2803 0.0978 0.2641 500 GLY A CA 919 C C . GLY A 117 ? 1.3943 1.4892 1.3541 0.3036 0.1041 0.2823 500 GLY A C 920 O O . GLY A 117 ? 1.4299 1.5434 1.3712 0.3190 0.0964 0.2785 500 GLY A O 921 N N . ASP A 118 ? 1.4584 1.5361 1.4256 0.3058 0.1182 0.3021 501 ASP A N 922 C CA . ASP A 118 ? 1.5491 1.6267 1.5032 0.3278 0.1263 0.3225 501 ASP A CA 923 C C . ASP A 118 ? 1.6064 1.6771 1.5676 0.3349 0.1255 0.3246 501 ASP A C 924 O O . ASP A 118 ? 1.6256 1.6937 1.6000 0.3234 0.1179 0.3085 501 ASP A O 925 C CB . ASP A 118 ? 1.5578 1.6200 1.5169 0.3278 0.1436 0.3441 501 ASP A CB 926 C CG . ASP A 118 ? 1.5381 1.5765 1.5250 0.3090 0.1523 0.3466 501 ASP A CG 927 O OD1 . ASP A 118 ? 1.5232 1.5483 1.5224 0.3080 0.1548 0.3479 501 ASP A OD1 928 O OD2 . ASP A 118 ? 1.4865 1.5201 1.4833 0.2949 0.1568 0.3467 501 ASP A OD2 929 N N . ASP A 119 ? 1.6763 1.7435 1.6293 0.3542 0.1344 0.3453 502 ASP A N 930 C CA . ASP A 119 ? 1.7298 1.7906 1.6897 0.3642 0.1353 0.3507 502 ASP A CA 931 C C . ASP A 119 ? 1.7764 1.8151 1.7642 0.3456 0.1395 0.3436 502 ASP A C 932 O O . ASP A 119 ? 1.7944 1.8315 1.7893 0.3502 0.1359 0.3392 502 ASP A O 933 C CB . ASP A 119 ? 1.7446 1.8009 1.6934 0.3866 0.1476 0.3781 502 ASP A CB 934 C CG . ASP A 119 ? 1.7503 1.8326 1.6701 0.4096 0.1384 0.3814 502 ASP A CG 935 O OD1 . ASP A 119 ? 1.7665 1.8512 1.6795 0.4296 0.1403 0.3959 502 ASP A OD1 936 O OD2 . ASP A 119 ? 1.7007 1.8012 1.6050 0.4076 0.1291 0.3690 502 ASP A OD2 937 N N . PHE A 120 ? 1.7927 1.8159 1.7957 0.3248 0.1461 0.3410 503 PHE A N 938 C CA . PHE A 120 ? 1.7945 1.7966 1.8225 0.3057 0.1500 0.3330 503 PHE A CA 939 C C . PHE A 120 ? 1.6841 1.6826 1.7242 0.2792 0.1448 0.3149 503 PHE A C 940 O O . PHE A 120 ? 1.6541 1.6441 1.7075 0.2656 0.1413 0.3007 503 PHE A O 941 C CB . PHE A 120 ? 1.8871 1.8651 1.9282 0.3092 0.1684 0.3541 503 PHE A CB 942 C CG . PHE A 120 ? 1.9383 1.8933 2.0042 0.2917 0.1742 0.3469 503 PHE A CG 943 C CD1 . PHE A 120 ? 1.9555 1.9097 2.0278 0.2898 0.1672 0.3325 503 PHE A CD1 944 C CD2 . PHE A 120 ? 1.9647 1.8986 2.0483 0.2772 0.1874 0.3546 503 PHE A CD2 945 C CE1 . PHE A 120 ? 1.9667 1.8989 2.0603 0.2736 0.1735 0.3251 503 PHE A CE1 946 C CE2 . PHE A 120 ? 1.9724 1.8851 2.0778 0.2606 0.1929 0.3468 503 PHE A CE2 947 C CZ . PHE A 120 ? 1.9706 1.8818 2.0800 0.2589 0.1862 0.3319 503 PHE A CZ 948 N N . PHE A 121 ? 1.5870 1.5918 1.6228 0.2721 0.1447 0.3156 504 PHE A N 949 C CA . PHE A 121 ? 1.4972 1.5009 1.5438 0.2482 0.1389 0.3001 504 PHE A CA 950 C C . PHE A 121 ? 1.3527 1.3778 1.3869 0.2463 0.1235 0.2818 504 PHE A C 951 O O . PHE A 121 ? 1.3133 1.3558 1.3289 0.2624 0.1188 0.2834 504 PHE A O 952 C CB . PHE A 121 ? 1.5164 1.5133 1.5707 0.2397 0.1485 0.3118 504 PHE A CB 953 C CG . PHE A 121 ? 1.5645 1.5385 1.6368 0.2349 0.1636 0.3260 504 PHE A CG 954 C CD1 . PHE A 121 ? 1.5757 1.5331 1.6675 0.2163 0.1645 0.3166 504 PHE A CD1 955 C CD2 . PHE A 121 ? 1.6032 1.5714 1.6729 0.2489 0.1777 0.3486 504 PHE A CD2 956 C CE1 . PHE A 121 ? 1.6176 1.5531 1.7273 0.2111 0.1789 0.3283 504 PHE A CE1 957 C CE2 . PHE A 121 ? 1.6344 1.5803 1.7228 0.2441 0.1927 0.3617 504 PHE A CE2 958 C CZ . PHE A 121 ? 1.6456 1.5751 1.7548 0.2249 0.1932 0.3510 504 PHE A CZ 959 N N . VAL A 122 ? 1.2355 1.2584 1.2800 0.2263 0.1162 0.2647 505 VAL A N 960 C CA . VAL A 122 ? 1.1457 1.1857 1.1827 0.2205 0.1029 0.2467 505 VAL A CA 961 C C . VAL A 122 ? 1.0756 1.1173 1.1166 0.2081 0.1039 0.2480 505 VAL A C 962 O O . VAL A 122 ? 1.0165 1.0453 1.0732 0.1912 0.1078 0.2488 505 VAL A O 963 C CB . VAL A 122 ? 1.1249 1.1609 1.1709 0.2062 0.0949 0.2276 505 VAL A CB 964 C CG1 . VAL A 122 ? 1.1059 1.1583 1.1456 0.1997 0.0825 0.2098 505 VAL A CG1 965 C CG2 . VAL A 122 ? 1.1198 1.1535 1.1652 0.2180 0.0948 0.2264 505 VAL A CG2 966 N N . TYR A 123 ? 1.0624 1.1204 1.0898 0.2169 0.1007 0.2482 506 TYR A N 967 C CA . TYR A 123 ? 1.0608 1.1223 1.0923 0.2070 0.1018 0.2494 506 TYR A CA 968 C C . TYR A 123 ? 1.0037 1.0710 1.0401 0.1912 0.0906 0.2304 506 TYR A C 969 O O . TYR A 123 ? 0.9952 1.0569 1.0449 0.1745 0.0909 0.2293 506 TYR A O 970 C CB . TYR A 123 ? 1.1128 1.1889 1.1273 0.2228 0.1038 0.2561 506 TYR A CB 971 C CG . TYR A 123 ? 1.1888 1.2624 1.1930 0.2417 0.1145 0.2753 506 TYR A CG 972 C CD1 . TYR A 123 ? 1.2177 1.2737 1.2343 0.2401 0.1268 0.2919 506 TYR A CD1 973 C CD2 . TYR A 123 ? 1.2331 1.3221 1.2146 0.2612 0.1126 0.2771 506 TYR A CD2 974 C CE1 . TYR A 123 ? 1.2545 1.3075 1.2614 0.2580 0.1376 0.3108 506 TYR A CE1 975 C CE2 . TYR A 123 ? 1.2698 1.3571 1.2396 0.2793 0.1224 0.2958 506 TYR A CE2 976 C CZ . TYR A 123 ? 1.2904 1.3593 1.2731 0.2779 0.1353 0.3133 506 TYR A CZ 977 O OH . TYR A 123 ? 1.3520 1.4186 1.3230 0.2964 0.1460 0.3330 506 TYR A OH 978 N N . ALA A 124 ? 0.9537 1.0328 0.9795 0.1970 0.0809 0.2160 507 ALA A N 979 C CA . ALA A 124 ? 0.9053 0.9910 0.9341 0.1842 0.0707 0.1976 507 ALA A CA 980 C C . ALA A 124 ? 0.8796 0.9699 0.9041 0.1882 0.0629 0.1835 507 ALA A C 981 O O . ALA A 124 ? 0.9039 1.0013 0.9178 0.2051 0.0625 0.1860 507 ALA A O 982 C CB . ALA A 124 ? 0.8952 0.9957 0.9156 0.1878 0.0678 0.1940 507 ALA A CB 983 N N . ASP A 125 ? 0.8493 0.9358 0.8824 0.1726 0.0570 0.1693 508 ASP A N 984 C CA . ASP A 125 ? 0.8393 0.9308 0.8708 0.1740 0.0496 0.1539 508 ASP A CA 985 C C . ASP A 125 ? 0.8187 0.9098 0.8571 0.1558 0.0432 0.1381 508 ASP A C 986 O O . ASP A 125 ? 0.7998 0.8909 0.8413 0.1458 0.0430 0.1393 508 ASP A O 987 C CB . ASP A 125 ? 0.8458 0.9250 0.8826 0.1776 0.0542 0.1584 508 ASP A CB 988 C CG . ASP A 125 ? 0.8497 0.9091 0.9001 0.1602 0.0596 0.1608 508 ASP A CG 989 O OD1 . ASP A 125 ? 0.8347 0.8905 0.8903 0.1459 0.0597 0.1613 508 ASP A OD1 990 O OD2 . ASP A 125 ? 0.8910 0.9385 0.9472 0.1607 0.0638 0.1620 508 ASP A OD2 991 N N . TYR A 126 ? 0.8151 0.9057 0.8565 0.1518 0.0386 0.1245 509 TYR A N 992 C CA . TYR A 126 ? 0.7911 0.8815 0.8374 0.1358 0.0331 0.1097 509 TYR A CA 993 C C . TYR A 126 ? 0.7730 0.8493 0.8275 0.1169 0.0357 0.1131 509 TYR A C 994 O O . TYR A 126 ? 0.7626 0.8415 0.8189 0.1051 0.0317 0.1064 509 TYR A O 995 C CB . TYR A 126 ? 0.7843 0.8758 0.8329 0.1356 0.0293 0.0952 509 TYR A CB 996 C CG . TYR A 126 ? 0.8011 0.8753 0.8575 0.1266 0.0339 0.0949 509 TYR A CG 997 C CD1 . TYR A 126 ? 0.8180 0.8838 0.8764 0.1361 0.0402 0.1054 509 TYR A CD1 998 C CD2 . TYR A 126 ? 0.7931 0.8589 0.8547 0.1087 0.0325 0.0841 509 TYR A CD2 999 C CE1 . TYR A 126 ? 0.8158 0.8645 0.8821 0.1276 0.0453 0.1039 509 TYR A CE1 1000 C CE2 . TYR A 126 ? 0.7981 0.8477 0.8655 0.1000 0.0372 0.0823 509 TYR A CE2 1001 C CZ . TYR A 126 ? 0.8142 0.8550 0.8847 0.1093 0.0437 0.0916 509 TYR A CZ 1002 O OH . TYR A 126 ? 0.8350 0.8585 0.9121 0.1004 0.0494 0.0889 509 TYR A OH 1003 N N . HIS A 127 ? 0.7535 0.8155 0.8133 0.1142 0.0424 0.1238 510 HIS A N 1004 C CA . HIS A 127 ? 0.7502 0.8001 0.8183 0.0967 0.0448 0.1282 510 HIS A CA 1005 C C . HIS A 127 ? 0.7229 0.7803 0.7919 0.0944 0.0441 0.1362 510 HIS A C 1006 O O . HIS A 127 ? 0.6896 0.7468 0.7630 0.0801 0.0404 0.1328 510 HIS A O 1007 C CB . HIS A 127 ? 0.7611 0.7956 0.8359 0.0963 0.0534 0.1398 510 HIS A CB 1008 C CG . HIS A 127 ? 0.7675 0.7926 0.8436 0.0998 0.0563 0.1345 510 HIS A CG 1009 N ND1 . HIS A 127 ? 0.7803 0.8048 0.8545 0.1173 0.0615 0.1429 510 HIS A ND1 1010 C CD2 . HIS A 127 ? 0.7651 0.7810 0.8444 0.0887 0.0552 0.1221 510 HIS A CD2 1011 C CE1 . HIS A 127 ? 0.7810 0.7963 0.8588 0.1169 0.0636 0.1361 510 HIS A CE1 1012 N NE2 . HIS A 127 ? 0.7701 0.7798 0.8510 0.0995 0.0602 0.1230 510 HIS A NE2 1013 N N . THR A 128 ? 0.7352 0.7991 0.7998 0.1093 0.0481 0.1475 511 THR A N 1014 C CA . THR A 128 ? 0.7292 0.8004 0.7950 0.1098 0.0494 0.1562 511 THR A CA 1015 C C . THR A 128 ? 0.6908 0.7739 0.7535 0.1066 0.0423 0.1450 511 THR A C 1016 O O . THR A 128 ? 0.6802 0.7648 0.7495 0.0965 0.0410 0.1473 511 THR A O 1017 C CB . THR A 128 ? 0.7433 0.8201 0.8016 0.1286 0.0557 0.1688 511 THR A CB 1018 O OG1 . THR A 128 ? 0.7676 0.8332 0.8277 0.1341 0.0625 0.1780 511 THR A OG1 1019 C CG2 . THR A 128 ? 0.7424 0.8223 0.8055 0.1273 0.0602 0.1809 511 THR A CG2 1020 N N . HIS A 129 ? 0.6759 0.7677 0.7299 0.1153 0.0378 0.1332 512 HIS A N 1021 C CA . HIS A 129 ? 0.6594 0.7620 0.7114 0.1128 0.0318 0.1209 512 HIS A CA 1022 C C . HIS A 129 ? 0.6331 0.7293 0.6926 0.0940 0.0277 0.1129 512 HIS A C 1023 O O . HIS A 129 ? 0.6126 0.7124 0.6761 0.0867 0.0258 0.1127 512 HIS A O 1024 C CB . HIS A 129 ? 0.6603 0.7733 0.7035 0.1248 0.0277 0.1086 512 HIS A CB 1025 C CG . HIS A 129 ? 0.6561 0.7812 0.6973 0.1249 0.0232 0.0970 512 HIS A CG 1026 N ND1 . HIS A 129 ? 0.6589 0.7916 0.6975 0.1299 0.0252 0.1016 512 HIS A ND1 1027 C CD2 . HIS A 129 ? 0.6534 0.7834 0.6959 0.1203 0.0177 0.0807 512 HIS A CD2 1028 C CE1 . HIS A 129 ? 0.6502 0.7914 0.6887 0.1284 0.0211 0.0884 512 HIS A CE1 1029 N NE2 . HIS A 129 ? 0.6614 0.8014 0.7025 0.1224 0.0166 0.0757 512 HIS A NE2 1030 N N . PHE A 130 ? 0.6264 0.7129 0.6877 0.0868 0.0269 0.1071 513 PHE A N 1031 C CA . PHE A 130 ? 0.6019 0.6807 0.6681 0.0687 0.0238 0.1002 513 PHE A CA 1032 C C . PHE A 130 ? 0.6079 0.6831 0.6813 0.0565 0.0241 0.1102 513 PHE A C 1033 O O . PHE A 130 ? 0.6181 0.6966 0.6937 0.0472 0.0202 0.1068 513 PHE A O 1034 C CB . PHE A 130 ? 0.5972 0.6638 0.6641 0.0638 0.0255 0.0955 513 PHE A CB 1035 C CG . PHE A 130 ? 0.5870 0.6450 0.6563 0.0452 0.0229 0.0879 513 PHE A CG 1036 C CD1 . PHE A 130 ? 0.5804 0.6411 0.6468 0.0408 0.0192 0.0736 513 PHE A CD1 1037 C CD2 . PHE A 130 ? 0.5888 0.6363 0.6627 0.0320 0.0243 0.0947 513 PHE A CD2 1038 C CE1 . PHE A 130 ? 0.5762 0.6288 0.6424 0.0242 0.0175 0.0671 513 PHE A CE1 1039 C CE2 . PHE A 130 ? 0.5845 0.6249 0.6580 0.0150 0.0214 0.0874 513 PHE A CE2 1040 C CZ . PHE A 130 ? 0.5877 0.6304 0.6564 0.0114 0.0182 0.0740 513 PHE A CZ 1041 N N . LEU A 131 ? 0.6228 0.6916 0.7008 0.0570 0.0290 0.1232 514 LEU A N 1042 C CA . LEU A 131 ? 0.6171 0.6832 0.7045 0.0449 0.0292 0.1331 514 LEU A CA 1043 C C . LEU A 131 ? 0.6097 0.6874 0.7004 0.0480 0.0282 0.1391 514 LEU A C 1044 O O . LEU A 131 ? 0.6268 0.7057 0.7254 0.0363 0.0254 0.1432 514 LEU A O 1045 C CB . LEU A 131 ? 0.6282 0.6852 0.7220 0.0455 0.0358 0.1454 514 LEU A CB 1046 C CG . LEU A 131 ? 0.6439 0.6866 0.7380 0.0385 0.0376 0.1402 514 LEU A CG 1047 C CD1 . LEU A 131 ? 0.6599 0.6936 0.7600 0.0439 0.0462 0.1524 514 LEU A CD1 1048 C CD2 . LEU A 131 ? 0.6344 0.6712 0.7323 0.0180 0.0325 0.1340 514 LEU A CD2 1049 N N . TYR A 132 ? 0.6049 0.6915 0.6895 0.0637 0.0306 0.1395 515 TYR A N 1050 C CA . TYR A 132 ? 0.6028 0.7002 0.6896 0.0673 0.0303 0.1423 515 TYR A CA 1051 C C . TYR A 132 ? 0.5899 0.6917 0.6753 0.0610 0.0242 0.1291 515 TYR A C 1052 O O . TYR A 132 ? 0.5834 0.6881 0.6761 0.0528 0.0221 0.1318 515 TYR A O 1053 C CB . TYR A 132 ? 0.6008 0.7060 0.6800 0.0859 0.0354 0.1458 515 TYR A CB 1054 C CG . TYR A 132 ? 0.5952 0.7108 0.6755 0.0902 0.0360 0.1459 515 TYR A CG 1055 C CD1 . TYR A 132 ? 0.6013 0.7242 0.6755 0.0940 0.0323 0.1320 515 TYR A CD1 1056 C CD2 . TYR A 132 ? 0.5908 0.7087 0.6801 0.0902 0.0408 0.1592 515 TYR A CD2 1057 C CE1 . TYR A 132 ? 0.5961 0.7272 0.6723 0.0977 0.0339 0.1310 515 TYR A CE1 1058 C CE2 . TYR A 132 ? 0.5895 0.7162 0.6809 0.0945 0.0425 0.1589 515 TYR A CE2 1059 C CZ . TYR A 132 ? 0.5874 0.7201 0.6717 0.0983 0.0392 0.1446 515 TYR A CZ 1060 O OH . TYR A 132 ? 0.5815 0.7214 0.6687 0.1023 0.0418 0.1433 515 TYR A OH 1061 N N . CYS A 133 ? 0.5882 0.6908 0.6654 0.0650 0.0218 0.1156 516 CYS A N 1062 C CA . CYS A 133 ? 0.5940 0.7010 0.6702 0.0607 0.0174 0.1026 516 CYS A CA 1063 C C . CYS A 133 ? 0.5889 0.6898 0.6703 0.0432 0.0135 0.1008 516 CYS A C 1064 O O . CYS A 133 ? 0.5727 0.6777 0.6571 0.0388 0.0114 0.0971 516 CYS A O 1065 C CB . CYS A 133 ? 0.5914 0.7009 0.6599 0.0681 0.0158 0.0884 516 CYS A CB 1066 S SG . CYS A 133 ? 0.6264 0.7483 0.6867 0.0890 0.0179 0.0865 516 CYS A SG 1067 N N . VAL A 134 ? 0.6026 0.6938 0.6848 0.0333 0.0128 0.1036 517 VAL A N 1068 C CA . VAL A 134 ? 0.6010 0.6871 0.6863 0.0163 0.0087 0.1033 517 VAL A CA 1069 C C . VAL A 134 ? 0.6033 0.6943 0.6979 0.0107 0.0073 0.1155 517 VAL A C 1070 O O . VAL A 134 ? 0.6059 0.6970 0.7026 -0.0006 0.0030 0.1150 517 VAL A O 1071 C CB . VAL A 134 ? 0.6043 0.6786 0.6877 0.0061 0.0084 0.1023 517 VAL A CB 1072 C CG1 . VAL A 134 ? 0.5980 0.6673 0.6738 0.0105 0.0099 0.0894 517 VAL A CG1 1073 C CG2 . VAL A 134 ? 0.6207 0.6913 0.7101 0.0074 0.0119 0.1150 517 VAL A CG2 1074 N N . ARG A 135 ? 0.6278 0.7235 0.7282 0.0192 0.0111 0.1267 518 ARG A N 1075 C CA . ARG A 135 ? 0.6597 0.7621 0.7714 0.0166 0.0109 0.1386 518 ARG A CA 1076 C C . ARG A 135 ? 0.6266 0.7381 0.7399 0.0261 0.0129 0.1371 518 ARG A C 1077 O O . ARG A 135 ? 0.6610 0.7775 0.7840 0.0220 0.0118 0.1441 518 ARG A O 1078 C CB . ARG A 135 ? 0.7134 0.8155 0.8328 0.0199 0.0154 0.1523 518 ARG A CB 1079 C CG . ARG A 135 ? 0.7788 0.8716 0.9004 0.0090 0.0142 0.1550 518 ARG A CG 1080 C CD . ARG A 135 ? 0.8762 0.9671 1.0035 0.0163 0.0212 0.1663 518 ARG A CD 1081 N NE . ARG A 135 ? 0.9768 1.0594 1.1109 0.0044 0.0208 0.1706 518 ARG A NE 1082 C CZ . ARG A 135 ? 1.0373 1.1225 1.1852 -0.0072 0.0182 0.1795 518 ARG A CZ 1083 N NH1 . ARG A 135 ? 1.0486 1.1450 1.2063 -0.0084 0.0156 0.1867 518 ARG A NH1 1084 N NH2 . ARG A 135 ? 1.0788 1.1557 1.2322 -0.0180 0.0182 0.1809 518 ARG A NH2 1085 N N . ALA A 136 ? 0.5789 0.6929 0.6836 0.0386 0.0158 0.1281 519 ALA A N 1086 C CA . ALA A 136 ? 0.5525 0.6747 0.6580 0.0480 0.0185 0.1246 519 ALA A CA 1087 C C . ALA A 136 ? 0.5324 0.6561 0.6284 0.0537 0.0174 0.1076 519 ALA A C 1088 O O . ALA A 136 ? 0.5116 0.6408 0.6011 0.0668 0.0203 0.1029 519 ALA A O 1089 C CB . ALA A 136 ? 0.5660 0.6931 0.6725 0.0606 0.0248 0.1341 519 ALA A CB 1090 N N . PRO A 137 ? 0.4992 0.6191 0.5946 0.0437 0.0133 0.0982 520 PRO A N 1091 C CA . PRO A 137 ? 0.5004 0.6218 0.5890 0.0478 0.0124 0.0817 520 PRO A CA 1092 C C . PRO A 137 ? 0.5027 0.6322 0.5926 0.0561 0.0146 0.0728 520 PRO A C 1093 O O . PRO A 137 ? 0.5253 0.6582 0.6104 0.0612 0.0138 0.0588 520 PRO A O 1094 C CB . PRO A 137 ? 0.5000 0.6142 0.5888 0.0337 0.0088 0.0760 520 PRO A CB 1095 C CG . PRO A 137 ? 0.4982 0.6104 0.5945 0.0234 0.0075 0.0885 520 PRO A CG 1096 C CD . PRO A 137 ? 0.4887 0.6031 0.5890 0.0283 0.0095 0.1025 520 PRO A CD 1097 N N . ALA A 138 ? 0.5055 0.6383 0.6029 0.0573 0.0175 0.0801 521 ALA A N 1098 C CA . ALA A 138 ? 0.5260 0.6657 0.6250 0.0656 0.0210 0.0717 521 ALA A CA 1099 C C . ALA A 138 ? 0.5445 0.6913 0.6372 0.0803 0.0248 0.0734 521 ALA A C 1100 O O . ALA A 138 ? 0.5491 0.7022 0.6403 0.0881 0.0275 0.0641 521 ALA A O 1101 C CB . ALA A 138 ? 0.5338 0.6728 0.6450 0.0600 0.0235 0.0780 521 ALA A CB 1102 N N . SER A 139 ? 0.5705 0.7159 0.6592 0.0838 0.0256 0.0853 522 SER A N 1103 C CA . SER A 139 ? 0.5781 0.7292 0.6595 0.0979 0.0302 0.0900 522 SER A CA 1104 C C . SER A 139 ? 0.5892 0.7477 0.6586 0.1089 0.0289 0.0752 522 SER A C 1105 O O . SER A 139 ? 0.5812 0.7390 0.6463 0.1072 0.0240 0.0659 522 SER A O 1106 C CB . SER A 139 ? 0.5872 0.7339 0.6664 0.0988 0.0312 0.1042 522 SER A CB 1107 O OG . SER A 139 ? 0.5786 0.7303 0.6493 0.1129 0.0364 0.1095 522 SER A OG 1108 N N . LEU A 140 ? 0.6172 0.7834 0.6814 0.1201 0.0332 0.0726 523 LEU A N 1109 C CA . LEU A 140 ? 0.6624 0.8381 0.7133 0.1322 0.0315 0.0596 523 LEU A CA 1110 C C . LEU A 140 ? 0.7091 0.8873 0.7470 0.1441 0.0328 0.0693 523 LEU A C 1111 O O . LEU A 140 ? 0.7073 0.8942 0.7324 0.1551 0.0304 0.0608 523 LEU A O 1112 C CB . LEU A 140 ? 0.6634 0.8463 0.7133 0.1383 0.0356 0.0501 523 LEU A CB 1113 C CG . LEU A 140 ? 0.6709 0.8512 0.7345 0.1282 0.0360 0.0403 523 LEU A CG 1114 C CD1 . LEU A 140 ? 0.6770 0.8634 0.7401 0.1350 0.0416 0.0312 523 LEU A CD1 1115 C CD2 . LEU A 140 ? 0.6657 0.8462 0.7314 0.1215 0.0292 0.0251 523 LEU A CD2 1116 N N . ASN A 141 ? 0.7591 0.9299 0.8007 0.1418 0.0366 0.0873 524 ASN A N 1117 C CA . ASN A 141 ? 0.8296 1.0014 0.8606 0.1534 0.0406 0.0994 524 ASN A CA 1118 C C . ASN A 141 ? 0.8102 0.9712 0.8495 0.1460 0.0427 0.1160 524 ASN A C 1119 O O . ASN A 141 ? 0.7581 0.9149 0.8089 0.1393 0.0468 0.1270 524 ASN A O 1120 C CB . ASN A 141 ? 0.9154 1.0932 0.9412 0.1634 0.0483 0.1038 524 ASN A CB 1121 C CG . ASN A 141 ? 1.0246 1.2053 1.0353 0.1780 0.0531 0.1142 524 ASN A CG 1122 O OD1 . ASN A 141 ? 1.0328 1.2100 1.0389 0.1806 0.0514 0.1206 524 ASN A OD1 1123 N ND2 . ASN A 141 ? 1.1724 1.3591 1.1752 0.1879 0.0601 0.1162 524 ASN A ND2 1124 N N . ASP A 142 ? 0.8631 1.0202 0.8979 0.1470 0.0397 0.1169 525 ASP A N 1125 C CA . ASP A 142 ? 0.9386 1.0853 0.9788 0.1427 0.0427 0.1319 525 ASP A CA 1126 C C . ASP A 142 ? 0.9833 1.1304 1.0222 0.1511 0.0518 0.1485 525 ASP A C 1127 O O . ASP A 142 ? 0.9904 1.1453 1.0164 0.1654 0.0553 0.1485 525 ASP A O 1128 C CB . ASP A 142 ? 0.9792 1.1236 1.0113 0.1483 0.0398 0.1291 525 ASP A CB 1129 C CG . ASP A 142 ? 1.0205 1.1518 1.0604 0.1405 0.0419 0.1400 525 ASP A CG 1130 O OD1 . ASP A 142 ? 1.0683 1.1935 1.1183 0.1333 0.0465 0.1525 525 ASP A OD1 1131 O OD2 . ASP A 142 ? 1.0235 1.1510 1.0604 0.1416 0.0391 0.1354 525 ASP A OD2 1132 N N . THR A 143 ? 1.0169 1.1561 1.0690 0.1421 0.0557 0.1621 526 THR A N 1133 C CA . THR A 143 ? 1.0618 1.2008 1.1159 0.1489 0.0655 0.1786 526 THR A CA 1134 C C . THR A 143 ? 1.0874 1.2217 1.1327 0.1590 0.0704 0.1887 526 THR A C 1135 O O . THR A 143 ? 1.0804 1.2161 1.1212 0.1694 0.0793 0.2008 526 THR A O 1136 C CB . THR A 143 ? 1.0728 1.2073 1.1471 0.1354 0.0677 0.1892 526 THR A CB 1137 O OG1 . THR A 143 ? 1.1009 1.2408 1.1821 0.1290 0.0641 0.1813 526 THR A OG1 1138 C CG2 . THR A 143 ? 1.1143 1.2487 1.1940 0.1415 0.0787 0.2068 526 THR A CG2 1139 N N . SER A 144 ? 1.1203 1.2487 1.1632 0.1565 0.0654 0.1837 527 SER A N 1140 C CA . SER A 144 ? 1.1453 1.2687 1.1801 0.1670 0.0698 0.1925 527 SER A CA 1141 C C . SER A 144 ? 1.1693 1.3035 1.1834 0.1866 0.0707 0.1901 527 SER A C 1142 O O . SER A 144 ? 1.1671 1.3123 1.1735 0.1913 0.0684 0.1808 527 SER A O 1143 C CB . SER A 144 ? 1.1337 1.2483 1.1721 0.1595 0.0643 0.1860 527 SER A CB 1144 O OG . SER A 144 ? 1.1084 1.2307 1.1353 0.1664 0.0570 0.1714 527 SER A OG 1145 N N . LEU A 145 ? 1.1763 1.3074 1.1816 0.1978 0.0739 0.1980 528 LEU A N 1146 C CA . LEU A 145 ? 1.1887 1.3305 1.1730 0.2173 0.0743 0.1979 528 LEU A CA 1147 C C . LEU A 145 ? 1.1670 1.3204 1.1419 0.2210 0.0629 0.1786 528 LEU A C 1148 O O . LEU A 145 ? 1.1721 1.3382 1.1294 0.2359 0.0610 0.1747 528 LEU A O 1149 C CB . LEU A 145 ? 1.2323 1.3669 1.2114 0.2284 0.0813 0.2141 528 LEU A CB 1150 C CG . LEU A 145 ? 1.2656 1.3896 1.2528 0.2277 0.0944 0.2346 528 LEU A CG 1151 C CD1 . LEU A 145 ? 1.2673 1.3748 1.2757 0.2123 0.0970 0.2406 528 LEU A CD1 1152 C CD2 . LEU A 145 ? 1.2978 1.4233 1.2681 0.2475 0.1026 0.2495 528 LEU A CD2 1153 N N . LEU A 146 ? 1.1285 1.2780 1.1152 0.2076 0.0555 0.1664 529 LEU A N 1154 C CA . LEU A 146 ? 1.0798 1.2395 1.0617 0.2089 0.0453 0.1474 529 LEU A CA 1155 C C . LEU A 146 ? 1.0547 1.2268 1.0320 0.2088 0.0419 0.1342 529 LEU A C 1156 O O . LEU A 146 ? 1.0341 1.2199 0.9999 0.2185 0.0361 0.1223 529 LEU A O 1157 C CB . LEU A 146 ? 1.0653 1.2159 1.0617 0.1934 0.0402 0.1387 529 LEU A CB 1158 C CG . LEU A 146 ? 1.0753 1.2119 1.0784 0.1912 0.0436 0.1485 529 LEU A CG 1159 C CD1 . LEU A 146 ? 1.0587 1.1857 1.0754 0.1734 0.0397 0.1388 529 LEU A CD1 1160 C CD2 . LEU A 146 ? 1.0878 1.2300 1.0804 0.2078 0.0423 0.1500 529 LEU A CD2 1161 N N . HIS A 147 ? 1.0468 1.2142 1.0344 0.1978 0.0455 0.1362 530 HIS A N 1162 C CA . HIS A 147 ? 1.0206 1.1968 1.0079 0.1956 0.0438 0.1243 530 HIS A CA 1163 C C . HIS A 147 ? 0.9418 1.1248 0.9310 0.1907 0.0343 0.1033 530 HIS A C 1164 O O . HIS A 147 ? 0.9304 1.1249 0.9126 0.1959 0.0317 0.0904 530 HIS A O 1165 C CB . HIS A 147 ? 1.0927 1.2793 1.0632 0.2113 0.0487 0.1270 530 HIS A CB 1166 C CG . HIS A 147 ? 1.1554 1.3357 1.1248 0.2162 0.0596 0.1475 530 HIS A CG 1167 N ND1 . HIS A 147 ? 1.2021 1.3854 1.1551 0.2322 0.0646 0.1586 530 HIS A ND1 1168 C CD2 . HIS A 147 ? 1.1634 1.3351 1.1471 0.2073 0.0668 0.1594 530 HIS A CD2 1169 C CE1 . HIS A 147 ? 1.2154 1.3912 1.1728 0.2326 0.0753 0.1763 530 HIS A CE1 1170 N NE2 . HIS A 147 ? 1.1891 1.3584 1.1660 0.2175 0.0765 0.1768 530 HIS A NE2 1171 N N . ASP A 148 ? 0.8804 1.0558 0.8794 0.1804 0.0299 0.0996 531 ASP A N 1172 C CA . ASP A 148 ? 0.8360 1.0161 0.8396 0.1740 0.0220 0.0807 531 ASP A CA 1173 C C . ASP A 148 ? 0.7732 0.9476 0.7901 0.1583 0.0223 0.0760 531 ASP A C 1174 O O . ASP A 148 ? 0.7343 0.8989 0.7593 0.1499 0.0266 0.0884 531 ASP A O 1175 C CB . ASP A 148 ? 0.8568 1.0310 0.8643 0.1709 0.0182 0.0790 531 ASP A CB 1176 C CG . ASP A 148 ? 0.8985 1.0819 0.8945 0.1870 0.0155 0.0787 531 ASP A CG 1177 O OD1 . ASP A 148 ? 0.9298 1.1284 0.9154 0.1982 0.0120 0.0701 531 ASP A OD1 1178 O OD2 . ASP A 148 ? 0.9311 1.1066 0.9291 0.1883 0.0167 0.0866 531 ASP A OD2 1179 N N . PRO A 149 ? 0.7234 0.9042 0.7435 0.1542 0.0176 0.0586 532 PRO A N 1180 C CA . PRO A 149 ? 0.6858 0.8603 0.7187 0.1395 0.0181 0.0552 532 PRO A CA 1181 C C . PRO A 149 ? 0.6421 0.8054 0.6838 0.1259 0.0156 0.0558 532 PRO A C 1182 O O . PRO A 149 ? 0.6325 0.7949 0.6717 0.1277 0.0126 0.0525 532 PRO A O 1183 C CB . PRO A 149 ? 0.6935 0.8782 0.7267 0.1408 0.0149 0.0359 532 PRO A CB 1184 C CG . PRO A 149 ? 0.6932 0.8890 0.7165 0.1523 0.0099 0.0264 532 PRO A CG 1185 C CD . PRO A 149 ? 0.7153 0.9087 0.7296 0.1615 0.0114 0.0416 532 PRO A CD 1186 N N . CYS A 150 ? 0.6019 0.7573 0.6537 0.1127 0.0170 0.0602 533 CYS A N 1187 C CA . CYS A 150 ? 0.5802 0.7259 0.6391 0.0983 0.0143 0.0583 533 CYS A CA 1188 C C . CYS A 150 ? 0.5591 0.7068 0.6231 0.0910 0.0115 0.0424 533 CYS A C 1189 O O . CYS A 150 ? 0.5464 0.6886 0.6128 0.0824 0.0091 0.0360 533 CYS A O 1190 C CB . CYS A 150 ? 0.5864 0.7234 0.6527 0.0877 0.0166 0.0729 533 CYS A CB 1191 S SG . CYS A 150 ? 0.6031 0.7348 0.6669 0.0927 0.0206 0.0912 533 CYS A SG 1192 N N . LEU A 151 ? 0.5603 0.7153 0.6262 0.0945 0.0128 0.0358 534 LEU A N 1193 C CA . LEU A 151 ? 0.5417 0.6977 0.6148 0.0873 0.0119 0.0220 534 LEU A CA 1194 C C . LEU A 151 ? 0.5291 0.6893 0.6010 0.0884 0.0080 0.0061 534 LEU A C 1195 O O . LEU A 151 ? 0.5450 0.7142 0.6100 0.0999 0.0058 0.0012 534 LEU A O 1196 C CB . LEU A 151 ? 0.5453 0.7089 0.6206 0.0933 0.0151 0.0167 534 LEU A CB 1197 C CG . LEU A 151 ? 0.5385 0.6997 0.6247 0.0843 0.0169 0.0081 534 LEU A CG 1198 C CD1 . LEU A 151 ? 0.5393 0.6916 0.6331 0.0751 0.0197 0.0233 534 LEU A CD1 1199 C CD2 . LEU A 151 ? 0.5353 0.7054 0.6226 0.0921 0.0196 -0.0037 534 LEU A CD2 1200 N N . GLY A 152 ? 0.5101 0.6646 0.5888 0.0769 0.0073 -0.0011 535 GLY A N 1201 C CA . GLY A 152 ? 0.5113 0.6696 0.5918 0.0766 0.0046 -0.0165 535 GLY A CA 1202 C C . GLY A 152 ? 0.5194 0.6905 0.6029 0.0836 0.0037 -0.0324 535 GLY A C 1203 O O . GLY A 152 ? 0.5342 0.7081 0.6197 0.0854 0.0063 -0.0329 535 GLY A O 1204 N N . THR A 153 ? 0.5251 0.7043 0.6102 0.0873 0.0001 -0.0461 536 THR A N 1205 C CA . THR A 153 ? 0.5472 0.7410 0.6352 0.0945 -0.0019 -0.0628 536 THR A CA 1206 C C . THR A 153 ? 0.5536 0.7455 0.6537 0.0852 0.0015 -0.0741 536 THR A C 1207 O O . THR A 153 ? 0.5863 0.7889 0.6900 0.0897 0.0011 -0.0876 536 THR A O 1208 C CB . THR A 153 ? 0.5492 0.7539 0.6388 0.1002 -0.0073 -0.0749 536 THR A CB 1209 O OG1 . THR A 153 ? 0.5784 0.7762 0.6784 0.0889 -0.0059 -0.0817 536 THR A OG1 1210 C CG2 . THR A 153 ? 0.5549 0.7611 0.6337 0.1104 -0.0102 -0.0633 536 THR A CG2 1211 N N . PHE A 154 ? 0.5493 0.7277 0.6554 0.0723 0.0052 -0.0689 537 PHE A N 1212 C CA . PHE A 154 ? 0.5422 0.7159 0.6597 0.0630 0.0100 -0.0758 537 PHE A CA 1213 C C . PHE A 154 ? 0.5415 0.7112 0.6599 0.0631 0.0145 -0.0667 537 PHE A C 1214 O O . PHE A 154 ? 0.5533 0.7188 0.6820 0.0565 0.0193 -0.0714 537 PHE A O 1215 C CB . PHE A 154 ? 0.5337 0.6950 0.6559 0.0496 0.0125 -0.0734 537 PHE A CB 1216 C CG . PHE A 154 ? 0.5308 0.6798 0.6460 0.0435 0.0132 -0.0540 537 PHE A CG 1217 C CD1 . PHE A 154 ? 0.5300 0.6755 0.6365 0.0441 0.0102 -0.0462 537 PHE A CD1 1218 C CD2 . PHE A 154 ? 0.5225 0.6635 0.6409 0.0369 0.0170 -0.0440 537 PHE A CD2 1219 C CE1 . PHE A 154 ? 0.5286 0.6635 0.6296 0.0376 0.0105 -0.0299 537 PHE A CE1 1220 C CE2 . PHE A 154 ? 0.5123 0.6441 0.6251 0.0310 0.0165 -0.0267 537 PHE A CE2 1221 C CZ . PHE A 154 ? 0.5210 0.6499 0.6250 0.0309 0.0131 -0.0204 537 PHE A CZ 1222 N N . GLY A 155 ? 0.5283 0.6989 0.6372 0.0704 0.0137 -0.0532 538 GLY A N 1223 C CA . GLY A 155 ? 0.5217 0.6908 0.6321 0.0728 0.0183 -0.0454 538 GLY A CA 1224 C C . GLY A 155 ? 0.5179 0.6753 0.6305 0.0649 0.0210 -0.0265 538 GLY A C 1225 O O . GLY A 155 ? 0.5220 0.6775 0.6395 0.0657 0.0256 -0.0195 538 GLY A O 1226 N N . GLY A 156 ? 0.5032 0.6532 0.6130 0.0573 0.0183 -0.0186 539 GLY A N 1227 C CA . GLY A 156 ? 0.5000 0.6404 0.6111 0.0491 0.0193 -0.0010 539 GLY A CA 1228 C C . GLY A 156 ? 0.4969 0.6336 0.5995 0.0476 0.0155 0.0097 539 GLY A C 1229 O O . GLY A 156 ? 0.5074 0.6465 0.6039 0.0513 0.0126 0.0033 539 GLY A O 1230 N N . PRO A 157 ? 0.5004 0.6313 0.6040 0.0419 0.0155 0.0263 540 PRO A N 1231 C CA . PRO A 157 ? 0.5075 0.6339 0.6045 0.0392 0.0124 0.0364 540 PRO A CA 1232 C C . PRO A 157 ? 0.5144 0.6331 0.6083 0.0284 0.0101 0.0315 540 PRO A C 1233 O O . PRO A 157 ? 0.5370 0.6522 0.6346 0.0203 0.0110 0.0260 540 PRO A O 1234 C CB . PRO A 157 ? 0.4983 0.6223 0.6003 0.0349 0.0131 0.0537 540 PRO A CB 1235 C CG . PRO A 157 ? 0.5015 0.6246 0.6123 0.0295 0.0153 0.0522 540 PRO A CG 1236 C CD . PRO A 157 ? 0.4938 0.6219 0.6062 0.0368 0.0182 0.0359 540 PRO A CD 1237 N N . VAL A 158 ? 0.5268 0.6423 0.6140 0.0287 0.0080 0.0332 541 VAL A N 1238 C CA . VAL A 158 ? 0.5278 0.6348 0.6111 0.0185 0.0066 0.0297 541 VAL A CA 1239 C C . VAL A 158 ? 0.5307 0.6308 0.6118 0.0102 0.0049 0.0442 541 VAL A C 1240 O O . VAL A 158 ? 0.5686 0.6686 0.6479 0.0151 0.0047 0.0520 541 VAL A O 1241 C CB . VAL A 158 ? 0.5417 0.6500 0.6206 0.0254 0.0063 0.0200 541 VAL A CB 1242 C CG1 . VAL A 158 ? 0.5501 0.6483 0.6252 0.0150 0.0061 0.0163 541 VAL A CG1 1243 C CG2 . VAL A 158 ? 0.5415 0.6592 0.6240 0.0335 0.0068 0.0050 541 VAL A CG2 1244 N N . PHE A 159 ? 0.5295 0.6242 0.6110 -0.0023 0.0036 0.0482 542 PHE A N 1245 C CA . PHE A 159 ? 0.5348 0.6249 0.6151 -0.0111 0.0008 0.0613 542 PHE A CA 1246 C C . PHE A 159 ? 0.5323 0.6137 0.6050 -0.0174 0.0000 0.0578 542 PHE A C 1247 O O . PHE A 159 ? 0.5394 0.6156 0.6070 -0.0224 0.0008 0.0470 542 PHE A O 1248 C CB . PHE A 159 ? 0.5435 0.6325 0.6261 -0.0219 -0.0011 0.0675 542 PHE A CB 1249 C CG . PHE A 159 ? 0.5373 0.6337 0.6297 -0.0158 0.0004 0.0734 542 PHE A CG 1250 C CD1 . PHE A 159 ? 0.5413 0.6434 0.6404 -0.0093 0.0006 0.0849 542 PHE A CD1 1251 C CD2 . PHE A 159 ? 0.5566 0.6537 0.6525 -0.0163 0.0030 0.0673 542 PHE A CD2 1252 C CE1 . PHE A 159 ? 0.5412 0.6495 0.6498 -0.0033 0.0033 0.0900 542 PHE A CE1 1253 C CE2 . PHE A 159 ? 0.5468 0.6494 0.6528 -0.0106 0.0056 0.0722 542 PHE A CE2 1254 C CZ . PHE A 159 ? 0.5456 0.6540 0.6579 -0.0039 0.0058 0.0834 542 PHE A CZ 1255 N N . PRO A 160 ? 0.5325 0.6117 0.6054 -0.0173 -0.0007 0.0669 543 PRO A N 1256 C CA . PRO A 160 ? 0.5435 0.6136 0.6107 -0.0210 0.0000 0.0630 543 PRO A CA 1257 C C . PRO A 160 ? 0.5430 0.6037 0.6028 -0.0363 -0.0015 0.0573 543 PRO A C 1258 O O . PRO A 160 ? 0.5390 0.5927 0.5937 -0.0376 0.0009 0.0472 543 PRO A O 1259 C CB . PRO A 160 ? 0.5495 0.6191 0.6210 -0.0202 -0.0002 0.0762 543 PRO A CB 1260 C CG . PRO A 160 ? 0.5471 0.6238 0.6254 -0.0233 -0.0030 0.0872 543 PRO A CG 1261 C CD . PRO A 160 ? 0.5375 0.6214 0.6174 -0.0157 -0.0018 0.0818 543 PRO A CD 1262 N N . TRP A 161 ? 0.5378 0.5991 0.5970 -0.0472 -0.0053 0.0637 544 TRP A N 1263 C CA . TRP A 161 ? 0.5442 0.5979 0.5939 -0.0620 -0.0070 0.0590 544 TRP A CA 1264 C C . TRP A 161 ? 0.5513 0.6020 0.5955 -0.0626 -0.0036 0.0457 544 TRP A C 1265 O O . TRP A 161 ? 0.5601 0.6025 0.5947 -0.0732 -0.0030 0.0393 544 TRP A O 1266 C CB . TRP A 161 ? 0.5456 0.6030 0.5958 -0.0722 -0.0128 0.0704 544 TRP A CB 1267 C CG . TRP A 161 ? 0.5405 0.6065 0.5975 -0.0672 -0.0131 0.0756 544 TRP A CG 1268 C CD1 . TRP A 161 ? 0.5528 0.6182 0.6066 -0.0693 -0.0116 0.0703 544 TRP A CD1 1269 C CD2 . TRP A 161 ? 0.5392 0.6147 0.6083 -0.0590 -0.0139 0.0869 544 TRP A CD2 1270 N NE1 . TRP A 161 ? 0.5527 0.6261 0.6164 -0.0631 -0.0113 0.0774 544 TRP A NE1 1271 C CE2 . TRP A 161 ? 0.5331 0.6130 0.6062 -0.0566 -0.0127 0.0875 544 TRP A CE2 1272 C CE3 . TRP A 161 ? 0.5396 0.6198 0.6174 -0.0535 -0.0145 0.0969 544 TRP A CE3 1273 C CZ2 . TRP A 161 ? 0.5335 0.6219 0.6186 -0.0487 -0.0120 0.0967 544 TRP A CZ2 1274 C CZ3 . TRP A 161 ? 0.5380 0.6274 0.6273 -0.0456 -0.0138 0.1065 544 TRP A CZ3 1275 C CH2 . TRP A 161 ? 0.5394 0.6327 0.6322 -0.0432 -0.0126 0.1060 544 TRP A CH2 1276 N N . LEU A 162 ? 0.5325 0.5899 0.5831 -0.0517 -0.0009 0.0409 545 LEU A N 1277 C CA . LEU A 162 ? 0.5316 0.5873 0.5805 -0.0514 0.0029 0.0274 545 LEU A CA 1278 C C . LEU A 162 ? 0.5455 0.5982 0.5939 -0.0452 0.0066 0.0155 545 LEU A C 1279 O O . LEU A 162 ? 0.5570 0.6065 0.6036 -0.0477 0.0102 0.0039 545 LEU A O 1280 C CB . LEU A 162 ? 0.5143 0.5789 0.5721 -0.0432 0.0043 0.0262 545 LEU A CB 1281 C CG . LEU A 162 ? 0.5071 0.5748 0.5678 -0.0477 0.0020 0.0378 545 LEU A CG 1282 C CD1 . LEU A 162 ? 0.4873 0.5624 0.5581 -0.0387 0.0050 0.0343 545 LEU A CD1 1283 C CD2 . LEU A 162 ? 0.5059 0.5666 0.5580 -0.0617 0.0012 0.0393 545 LEU A CD2 1284 N N . VAL A 163 ? 0.5558 0.6099 0.6068 -0.0366 0.0063 0.0188 546 VAL A N 1285 C CA . VAL A 163 ? 0.5490 0.6028 0.6019 -0.0276 0.0094 0.0093 546 VAL A CA 1286 C C . VAL A 163 ? 0.5674 0.6109 0.6164 -0.0306 0.0111 0.0106 546 VAL A C 1287 O O . VAL A 163 ? 0.5581 0.6008 0.6095 -0.0222 0.0140 0.0048 546 VAL A O 1288 C CB . VAL A 163 ? 0.5408 0.6067 0.6008 -0.0112 0.0088 0.0103 546 VAL A CB 1289 C CG1 . VAL A 163 ? 0.5204 0.5950 0.5852 -0.0086 0.0086 0.0044 546 VAL A CG1 1290 C CG2 . VAL A 163 ? 0.5477 0.6162 0.6090 -0.0066 0.0067 0.0248 546 VAL A CG2 1291 N N . LEU A 164 ? 0.5816 0.6174 0.6252 -0.0426 0.0094 0.0177 547 LEU A N 1292 C CA . LEU A 164 ? 0.6141 0.6390 0.6549 -0.0472 0.0114 0.0186 547 LEU A CA 1293 C C . LEU A 164 ? 0.6406 0.6557 0.6718 -0.0649 0.0105 0.0165 547 LEU A C 1294 O O . LEU A 164 ? 0.6655 0.6842 0.6931 -0.0728 0.0063 0.0211 547 LEU A O 1295 C CB . LEU A 164 ? 0.6164 0.6434 0.6626 -0.0422 0.0098 0.0318 547 LEU A CB 1296 C CG . LEU A 164 ? 0.6164 0.6527 0.6695 -0.0241 0.0111 0.0350 547 LEU A CG 1297 C CD1 . LEU A 164 ? 0.6277 0.6675 0.6856 -0.0203 0.0098 0.0498 547 LEU A CD1 1298 C CD2 . LEU A 164 ? 0.6331 0.6645 0.6872 -0.0157 0.0159 0.0280 547 LEU A CD2 1299 N N . GLY A 165 ? 0.6648 0.6677 0.6915 -0.0707 0.0147 0.0096 548 GLY A N 1300 C CA . GLY A 165 ? 0.6821 0.6748 0.6975 -0.0879 0.0142 0.0061 548 GLY A CA 1301 C C . GLY A 165 ? 0.6955 0.6766 0.7105 -0.0933 0.0166 0.0065 548 GLY A C 1302 O O . GLY A 165 ? 0.6945 0.6727 0.7176 -0.0831 0.0210 0.0068 548 GLY A O 1303 N N . GLY A 166 ? 0.7151 0.6900 0.7210 -0.1095 0.0136 0.0067 549 GLY A N 1304 C CA . GLY A 166 ? 0.7349 0.6970 0.7391 -0.1183 0.0164 0.0040 549 GLY A CA 1305 C C . GLY A 166 ? 0.7494 0.7131 0.7653 -0.1149 0.0147 0.0155 549 GLY A C 1306 O O . GLY A 166 ? 0.7971 0.7497 0.8174 -0.1153 0.0202 0.0133 549 GLY A O 1307 N N . TYR A 167 ? 0.7369 0.7136 0.7587 -0.1118 0.0080 0.0279 550 TYR A N 1308 C CA . TYR A 167 ? 0.7319 0.7118 0.7658 -0.1088 0.0066 0.0401 550 TYR A CA 1309 C C . TYR A 167 ? 0.7479 0.7320 0.7798 -0.1243 -0.0015 0.0459 550 TYR A C 1310 O O . TYR A 167 ? 0.7575 0.7459 0.7791 -0.1332 -0.0070 0.0435 550 TYR A O 1311 C CB . TYR A 167 ? 0.7237 0.7165 0.7675 -0.0917 0.0061 0.0503 550 TYR A CB 1312 C CG . TYR A 167 ? 0.7026 0.7083 0.7438 -0.0911 0.0001 0.0535 550 TYR A CG 1313 C CD1 . TYR A 167 ? 0.6928 0.7009 0.7286 -0.0854 0.0017 0.0451 550 TYR A CD1 1314 C CD2 . TYR A 167 ? 0.7011 0.7163 0.7468 -0.0966 -0.0067 0.0649 550 TYR A CD2 1315 C CE1 . TYR A 167 ? 0.6899 0.7080 0.7244 -0.0852 -0.0025 0.0478 550 TYR A CE1 1316 C CE2 . TYR A 167 ? 0.7045 0.7303 0.7489 -0.0957 -0.0113 0.0684 550 TYR A CE2 1317 C CZ . TYR A 167 ? 0.6853 0.7117 0.7239 -0.0901 -0.0088 0.0598 550 TYR A CZ 1318 O OH . TYR A 167 ? 0.6784 0.7138 0.7169 -0.0894 -0.0121 0.0632 550 TYR A OH 1319 N N . ASP A 168 ? 0.7710 0.7551 0.8139 -0.1269 -0.0022 0.0543 551 ASP A N 1320 C CA . ASP A 168 ? 0.7910 0.7807 0.8357 -0.1416 -0.0106 0.0604 551 ASP A CA 1321 C C . ASP A 168 ? 0.7959 0.8019 0.8532 -0.1343 -0.0156 0.0760 551 ASP A C 1322 O O . ASP A 168 ? 0.7919 0.8007 0.8597 -0.1195 -0.0107 0.0831 551 ASP A O 1323 C CB . ASP A 168 ? 0.7965 0.7753 0.8478 -0.1509 -0.0075 0.0585 551 ASP A CB 1324 C CG . ASP A 168 ? 0.7972 0.7738 0.8649 -0.1377 -0.0001 0.0672 551 ASP A CG 1325 O OD1 . ASP A 168 ? 0.7989 0.7694 0.8661 -0.1238 0.0077 0.0641 551 ASP A OD1 1326 O OD2 . ASP A 168 ? 0.7924 0.7743 0.8737 -0.1406 -0.0022 0.0776 551 ASP A OD2 1327 N N . ASP A 169 ? 0.8167 0.8334 0.8727 -0.1444 -0.0252 0.0816 552 ASP A N 1328 C CA . ASP A 169 ? 0.8185 0.8514 0.8869 -0.1385 -0.0302 0.0964 552 ASP A CA 1329 C C . ASP A 169 ? 0.7838 0.8212 0.8547 -0.1198 -0.0251 0.0992 552 ASP A C 1330 O O . ASP A 169 ? 0.7478 0.7832 0.8074 -0.1169 -0.0239 0.0911 552 ASP A O 1331 C CB . ASP A 169 ? 0.8619 0.8984 0.9480 -0.1412 -0.0309 0.1067 552 ASP A CB 1332 C CG . ASP A 169 ? 0.9257 0.9632 1.0113 -0.1610 -0.0390 0.1051 552 ASP A CG 1333 O OD1 . ASP A 169 ? 0.9596 1.0051 1.0364 -0.1703 -0.0482 0.1052 552 ASP A OD1 1334 O OD2 . ASP A 169 ? 0.9818 1.0127 1.0764 -0.1672 -0.0363 0.1042 552 ASP A OD2 1335 N N . GLN A 170 ? 0.7784 0.8216 0.8635 -0.1078 -0.0217 0.1095 553 GLN A N 1336 C CA . GLN A 170 ? 0.7712 0.8183 0.8577 -0.0899 -0.0164 0.1107 553 GLN A CA 1337 C C . GLN A 170 ? 0.7306 0.7701 0.8207 -0.0783 -0.0077 0.1100 553 GLN A C 1338 O O . GLN A 170 ? 0.7257 0.7708 0.8212 -0.0634 -0.0037 0.1159 553 GLN A O 1339 C CB . GLN A 170 ? 0.7880 0.8497 0.8858 -0.0838 -0.0193 0.1239 553 GLN A CB 1340 C CG . GLN A 170 ? 0.8268 0.8965 0.9217 -0.0931 -0.0274 0.1260 553 GLN A CG 1341 C CD . GLN A 170 ? 0.8507 0.9342 0.9587 -0.0860 -0.0291 0.1391 553 GLN A CD 1342 O OE1 . GLN A 170 ? 0.8857 0.9729 0.9936 -0.0744 -0.0257 0.1384 553 GLN A OE1 1343 N NE2 . GLN A 170 ? 0.8473 0.9389 0.9676 -0.0934 -0.0343 0.1505 553 GLN A NE2 1344 N N . ASN A 171 ? 0.7067 0.7331 0.7931 -0.0849 -0.0045 0.1026 554 ASN A N 1345 C CA . ASN A 171 ? 0.7043 0.7218 0.7938 -0.0743 0.0041 0.1020 554 ASN A CA 1346 C C . ASN A 171 ? 0.6941 0.7074 0.7732 -0.0652 0.0077 0.0906 554 ASN A C 1347 O O . ASN A 171 ? 0.7311 0.7324 0.8044 -0.0696 0.0111 0.0802 554 ASN A O 1348 C CB . ASN A 171 ? 0.7145 0.7190 0.8076 -0.0860 0.0069 0.0998 554 ASN A CB 1349 C CG . ASN A 171 ? 0.6974 0.7069 0.8044 -0.0940 0.0042 0.1115 554 ASN A CG 1350 O OD1 . ASN A 171 ? 0.6888 0.7065 0.8066 -0.0842 0.0062 0.1238 554 ASN A OD1 1351 N ND2 . ASN A 171 ? 0.6936 0.6986 0.8007 -0.1120 -0.0001 0.1072 554 ASN A ND2 1352 N N . TYR A 172 ? 0.6600 0.6837 0.7383 -0.0522 0.0072 0.0921 555 TYR A N 1353 C CA . TYR A 172 ? 0.6427 0.6664 0.7130 -0.0442 0.0090 0.0806 555 TYR A CA 1354 C C . TYR A 172 ? 0.6613 0.6762 0.7315 -0.0347 0.0160 0.0762 555 TYR A C 1355 O O . TYR A 172 ? 0.6550 0.6657 0.7195 -0.0331 0.0179 0.0646 555 TYR A O 1356 C CB . TYR A 172 ? 0.6149 0.6523 0.6865 -0.0320 0.0073 0.0834 555 TYR A CB 1357 C CG . TYR A 172 ? 0.6103 0.6557 0.6825 -0.0403 0.0013 0.0869 555 TYR A CG 1358 C CD1 . TYR A 172 ? 0.6079 0.6513 0.6724 -0.0509 -0.0019 0.0781 555 TYR A CD1 1359 C CD2 . TYR A 172 ? 0.5910 0.6456 0.6720 -0.0376 -0.0004 0.0998 555 TYR A CD2 1360 C CE1 . TYR A 172 ? 0.6097 0.6601 0.6749 -0.0579 -0.0072 0.0829 555 TYR A CE1 1361 C CE2 . TYR A 172 ? 0.5842 0.6462 0.6674 -0.0445 -0.0057 0.1040 555 TYR A CE2 1362 C CZ . TYR A 172 ? 0.5940 0.6539 0.6691 -0.0544 -0.0093 0.0960 555 TYR A CZ 1363 O OH . TYR A 172 ? 0.5984 0.6656 0.6759 -0.0604 -0.0142 0.1017 555 TYR A OH 1364 N N . ASN A 173 ? 0.6708 0.6834 0.7484 -0.0278 0.0203 0.0865 556 ASN A N 1365 C CA . ASN A 173 ? 0.6822 0.6849 0.7615 -0.0194 0.0277 0.0856 556 ASN A CA 1366 C C . ASN A 173 ? 0.6866 0.6738 0.7628 -0.0308 0.0306 0.0746 556 ASN A C 1367 O O . ASN A 173 ? 0.6734 0.6539 0.7492 -0.0227 0.0362 0.0693 556 ASN A O 1368 C CB . ASN A 173 ? 0.7075 0.7080 0.7962 -0.0144 0.0323 0.1002 556 ASN A CB 1369 C CG . ASN A 173 ? 0.7202 0.7162 0.8157 -0.0314 0.0304 0.1051 556 ASN A CG 1370 O OD1 . ASN A 173 ? 0.7105 0.7161 0.8076 -0.0383 0.0241 0.1091 556 ASN A OD1 1371 N ND2 . ASN A 173 ? 0.7484 0.7300 0.8487 -0.0383 0.0358 0.1045 556 ASN A ND2 1372 N N . ASN A 174 ? 0.6971 0.6793 0.7710 -0.0492 0.0271 0.0709 557 ASN A N 1373 C CA . ASN A 174 ? 0.7180 0.6850 0.7873 -0.0616 0.0302 0.0591 557 ASN A CA 1374 C C . ASN A 174 ? 0.7031 0.6699 0.7613 -0.0661 0.0284 0.0451 557 ASN A C 1375 O O . ASN A 174 ? 0.7188 0.6744 0.7706 -0.0791 0.0300 0.0351 557 ASN A O 1376 C CB . ASN A 174 ? 0.7626 0.7233 0.8348 -0.0795 0.0280 0.0619 557 ASN A CB 1377 C CG . ASN A 174 ? 0.8221 0.7783 0.9080 -0.0743 0.0337 0.0738 557 ASN A CG 1378 O OD1 . ASN A 174 ? 0.8320 0.7847 0.9216 -0.0593 0.0407 0.0767 557 ASN A OD1 1379 N ND2 . ASN A 174 ? 0.9065 0.8631 1.0005 -0.0848 0.0314 0.0811 557 ASN A ND2 1380 N N . ALA A 175 ? 0.6808 0.6595 0.7370 -0.0550 0.0261 0.0438 558 ALA A N 1381 C CA . ALA A 175 ? 0.6731 0.6526 0.7208 -0.0584 0.0251 0.0312 558 ALA A CA 1382 C C . ALA A 175 ? 0.6893 0.6567 0.7360 -0.0568 0.0326 0.0197 558 ALA A C 1383 O O . ALA A 175 ? 0.6710 0.6358 0.7248 -0.0442 0.0379 0.0221 558 ALA A O 1384 C CB . ALA A 175 ? 0.6596 0.6543 0.7086 -0.0459 0.0220 0.0319 558 ALA A CB 1385 N N . THR A 176 ? 0.7035 0.6637 0.7412 -0.0692 0.0336 0.0079 559 THR A N 1386 C CA . THR A 176 ? 0.7303 0.6796 0.7672 -0.0682 0.0415 -0.0045 559 THR A CA 1387 C C . THR A 176 ? 0.7227 0.6795 0.7573 -0.0633 0.0417 -0.0142 559 THR A C 1388 O O . THR A 176 ? 0.7517 0.7011 0.7865 -0.0627 0.0483 -0.0252 559 THR A O 1389 C CB . THR A 176 ? 0.7425 0.6755 0.7709 -0.0863 0.0448 -0.0127 559 THR A CB 1390 O OG1 . THR A 176 ? 0.7377 0.6746 0.7540 -0.1003 0.0384 -0.0145 559 THR A OG1 1391 C CG2 . THR A 176 ? 0.7460 0.6699 0.7800 -0.0907 0.0464 -0.0053 559 THR A CG2 1392 N N . ALA A 177 ? 0.6992 0.6705 0.7334 -0.0597 0.0354 -0.0103 560 ALA A N 1393 C CA . ALA A 177 ? 0.6744 0.6537 0.7089 -0.0552 0.0358 -0.0193 560 ALA A CA 1394 C C . ALA A 177 ? 0.6489 0.6450 0.6886 -0.0445 0.0300 -0.0129 560 ALA A C 1395 O O . ALA A 177 ? 0.6584 0.6595 0.6973 -0.0462 0.0248 -0.0022 560 ALA A O 1396 C CB . ALA A 177 ? 0.6790 0.6527 0.7019 -0.0710 0.0361 -0.0272 560 ALA A CB 1397 N N . LEU A 178 ? 0.6323 0.6373 0.6782 -0.0335 0.0311 -0.0201 561 LEU A N 1398 C CA . LEU A 178 ? 0.6276 0.6482 0.6779 -0.0248 0.0264 -0.0179 561 LEU A CA 1399 C C . LEU A 178 ? 0.6252 0.6479 0.6732 -0.0326 0.0269 -0.0272 561 LEU A C 1400 O O . LEU A 178 ? 0.6424 0.6580 0.6887 -0.0383 0.0319 -0.0378 561 LEU A O 1401 C CB . LEU A 178 ? 0.6288 0.6598 0.6884 -0.0070 0.0268 -0.0203 561 LEU A CB 1402 C CG . LEU A 178 ? 0.6434 0.6713 0.7060 0.0029 0.0284 -0.0121 561 LEU A CG 1403 C CD1 . LEU A 178 ? 0.6536 0.6943 0.7239 0.0208 0.0277 -0.0153 561 LEU A CD1 1404 C CD2 . LEU A 178 ? 0.6536 0.6820 0.7137 0.0029 0.0253 0.0025 561 LEU A CD2 1405 N N . VAL A 179 ? 0.6148 0.6465 0.6633 -0.0326 0.0227 -0.0230 562 VAL A N 1406 C CA . VAL A 179 ? 0.6018 0.6361 0.6498 -0.0387 0.0237 -0.0303 562 VAL A CA 1407 C C . VAL A 179 ? 0.5953 0.6445 0.6536 -0.0262 0.0217 -0.0333 562 VAL A C 1408 O O . VAL A 179 ? 0.5802 0.6372 0.6409 -0.0185 0.0177 -0.0248 562 VAL A O 1409 C CB . VAL A 179 ? 0.6048 0.6351 0.6442 -0.0515 0.0208 -0.0220 562 VAL A CB 1410 C CG1 . VAL A 179 ? 0.6149 0.6464 0.6536 -0.0575 0.0232 -0.0283 562 VAL A CG1 1411 C CG2 . VAL A 179 ? 0.6191 0.6362 0.6474 -0.0641 0.0216 -0.0197 562 VAL A CG2 1412 N N . ILE A 180 ? 0.6035 0.6568 0.6682 -0.0245 0.0250 -0.0462 563 ILE A N 1413 C CA . ILE A 180 ? 0.6194 0.6874 0.6949 -0.0139 0.0232 -0.0523 563 ILE A CA 1414 C C . ILE A 180 ? 0.6171 0.6852 0.6952 -0.0222 0.0260 -0.0586 563 ILE A C 1415 O O . ILE A 180 ? 0.6237 0.6841 0.7002 -0.0309 0.0312 -0.0657 563 ILE A O 1416 C CB . ILE A 180 ? 0.6479 0.7229 0.7325 -0.0033 0.0245 -0.0630 563 ILE A CB 1417 C CG1 . ILE A 180 ? 0.6634 0.7385 0.7459 0.0065 0.0222 -0.0550 563 ILE A CG1 1418 C CG2 . ILE A 180 ? 0.6603 0.7516 0.7564 0.0057 0.0223 -0.0722 563 ILE A CG2 1419 C CD1 . ILE A 180 ? 0.6886 0.7717 0.7803 0.0185 0.0227 -0.0633 563 ILE A CD1 1420 N N . THR A 181 ? 0.6010 0.6769 0.6834 -0.0193 0.0237 -0.0557 564 THR A N 1421 C CA . THR A 181 ? 0.6133 0.6878 0.6986 -0.0272 0.0270 -0.0589 564 THR A CA 1422 C C . THR A 181 ? 0.6229 0.7102 0.7216 -0.0189 0.0268 -0.0674 564 THR A C 1423 O O . THR A 181 ? 0.6536 0.7491 0.7542 -0.0102 0.0227 -0.0629 564 THR A O 1424 C CB . THR A 181 ? 0.6146 0.6822 0.6911 -0.0356 0.0253 -0.0445 564 THR A CB 1425 O OG1 . THR A 181 ? 0.6231 0.6801 0.6873 -0.0436 0.0246 -0.0379 564 THR A OG1 1426 C CG2 . THR A 181 ? 0.6406 0.7044 0.7188 -0.0445 0.0298 -0.0463 564 THR A CG2 1427 N N . PHE A 182 ? 0.6359 0.7244 0.7436 -0.0223 0.0318 -0.0802 565 PHE A N 1428 C CA . PHE A 182 ? 0.6442 0.7442 0.7665 -0.0168 0.0326 -0.0910 565 PHE A CA 1429 C C . PHE A 182 ? 0.6481 0.7410 0.7734 -0.0269 0.0385 -0.0902 565 PHE A C 1430 O O . PHE A 182 ? 0.6554 0.7404 0.7807 -0.0359 0.0447 -0.0947 565 PHE A O 1431 C CB . PHE A 182 ? 0.6602 0.7685 0.7948 -0.0131 0.0345 -0.1080 565 PHE A CB 1432 C CG . PHE A 182 ? 0.6824 0.7967 0.8153 -0.0034 0.0299 -0.1092 565 PHE A CG 1433 C CD1 . PHE A 182 ? 0.6942 0.7985 0.8198 -0.0076 0.0323 -0.1066 565 PHE A CD1 1434 C CD2 . PHE A 182 ? 0.6964 0.8265 0.8350 0.0099 0.0238 -0.1132 565 PHE A CD2 1435 C CE1 . PHE A 182 ? 0.7081 0.8171 0.8339 0.0018 0.0291 -0.1069 565 PHE A CE1 1436 C CE2 . PHE A 182 ? 0.7042 0.8401 0.8414 0.0198 0.0198 -0.1128 565 PHE A CE2 1437 C CZ . PHE A 182 ? 0.7134 0.8383 0.8450 0.0159 0.0227 -0.1092 565 PHE A CZ 1438 N N . PRO A 183 ? 0.6578 0.7527 0.7856 -0.0252 0.0377 -0.0838 566 PRO A N 1439 C CA . PRO A 183 ? 0.6537 0.7429 0.7882 -0.0330 0.0444 -0.0846 566 PRO A CA 1440 C C . PRO A 183 ? 0.6547 0.7516 0.8071 -0.0311 0.0490 -0.1027 566 PRO A C 1441 O O . PRO A 183 ? 0.6481 0.7580 0.8090 -0.0215 0.0451 -0.1120 566 PRO A O 1442 C CB . PRO A 183 ? 0.6706 0.7609 0.8048 -0.0298 0.0422 -0.0727 566 PRO A CB 1443 C CG . PRO A 183 ? 0.6693 0.7617 0.7922 -0.0243 0.0347 -0.0619 566 PRO A CG 1444 C CD . PRO A 183 ? 0.6631 0.7624 0.7862 -0.0179 0.0319 -0.0726 566 PRO A CD 1445 N N . VAL A 184 ? 0.6826 0.7720 0.8403 -0.0403 0.0572 -0.1079 567 VAL A N 1446 C CA . VAL A 184 ? 0.6880 0.7834 0.8654 -0.0407 0.0632 -0.1250 567 VAL A CA 1447 C C . VAL A 184 ? 0.6985 0.7832 0.8815 -0.0495 0.0726 -0.1213 567 VAL A C 1448 O O . VAL A 184 ? 0.6859 0.7579 0.8558 -0.0572 0.0755 -0.1076 567 VAL A O 1449 C CB . VAL A 184 ? 0.6970 0.7954 0.8805 -0.0423 0.0659 -0.1384 567 VAL A CB 1450 C CG1 . VAL A 184 ? 0.7101 0.8176 0.8878 -0.0331 0.0572 -0.1398 567 VAL A CG1 1451 C CG2 . VAL A 184 ? 0.7044 0.7876 0.8786 -0.0538 0.0737 -0.1332 567 VAL A CG2 1452 N N . ASN A 185 ? 0.7150 0.8052 0.9174 -0.0483 0.0774 -0.1335 568 ASN A N 1453 C CA . ASN A 185 ? 0.7216 0.8018 0.9331 -0.0556 0.0877 -0.1309 568 ASN A CA 1454 C C . ASN A 185 ? 0.7217 0.7898 0.9290 -0.0662 0.0965 -0.1288 568 ASN A C 1455 O O . ASN A 185 ? 0.7210 0.7925 0.9335 -0.0678 0.0988 -0.1410 568 ASN A O 1456 C CB . ASN A 185 ? 0.7348 0.8234 0.9709 -0.0534 0.0924 -0.1487 568 ASN A CB 1457 C CG . ASN A 185 ? 0.7544 0.8468 0.9950 -0.0469 0.0898 -0.1461 568 ASN A CG 1458 O OD1 . ASN A 185 ? 0.7630 0.8451 1.0047 -0.0501 0.0957 -0.1350 568 ASN A OD1 1459 N ND2 . ASN A 185 ? 0.7710 0.8786 1.0143 -0.0373 0.0814 -0.1561 568 ASN A ND2 1460 N N . ASN A 186 ? 0.7489 0.8033 0.9464 -0.0729 0.1016 -0.1130 569 ASN A N 1461 C CA . ASN A 186 ? 0.8054 0.8477 0.9991 -0.0831 0.1119 -0.1113 569 ASN A CA 1462 C C . ASN A 186 ? 0.8243 0.8644 1.0411 -0.0868 0.1245 -0.1229 569 ASN A C 1463 O O . ASN A 186 ? 0.8670 0.9010 1.0862 -0.0939 0.1338 -0.1281 569 ASN A O 1464 C CB . ASN A 186 ? 0.8294 0.8587 1.0006 -0.0895 0.1121 -0.0902 569 ASN A CB 1465 C CG . ASN A 186 ? 0.8567 0.8811 1.0308 -0.0890 0.1140 -0.0763 569 ASN A CG 1466 O OD1 . ASN A 186 ? 0.8766 0.9003 1.0702 -0.0884 0.1219 -0.0825 569 ASN A OD1 1467 N ND2 . ASN A 186 ? 0.8618 0.8823 1.0176 -0.0898 0.1074 -0.0572 569 ASN A ND2 1468 N N . TYR A 187 ? 0.8396 0.8848 1.0743 -0.0823 0.1255 -0.1280 570 TYR A N 1469 C CA . TYR A 187 ? 0.8704 0.9143 1.1307 -0.0858 0.1375 -0.1413 570 TYR A CA 1470 C C . TYR A 187 ? 0.9333 0.9601 1.1924 -0.0957 0.1517 -0.1319 570 TYR A C 1471 O O . TYR A 187 ? 0.9530 0.9776 1.2289 -0.1010 0.1629 -0.1439 570 TYR A O 1472 C CB . TYR A 187 ? 0.8495 0.9067 1.1275 -0.0844 0.1372 -0.1647 570 TYR A CB 1473 C CG . TYR A 187 ? 0.8383 0.9139 1.1233 -0.0743 0.1253 -0.1771 570 TYR A CG 1474 C CD1 . TYR A 187 ? 0.8271 0.9151 1.1069 -0.0692 0.1159 -0.1848 570 TYR A CD1 1475 C CD2 . TYR A 187 ? 0.8489 0.9295 1.1460 -0.0694 0.1241 -0.1815 570 TYR A CD2 1476 C CE1 . TYR A 187 ? 0.8295 0.9349 1.1143 -0.0593 0.1049 -0.1952 570 TYR A CE1 1477 C CE2 . TYR A 187 ? 0.8461 0.9440 1.1472 -0.0600 0.1133 -0.1931 570 TYR A CE2 1478 C CZ . TYR A 187 ? 0.8399 0.9505 1.1341 -0.0547 0.1034 -0.1994 570 TYR A CZ 1479 O OH . TYR A 187 ? 0.8189 0.9471 1.1154 -0.0447 0.0926 -0.2096 570 TYR A OH 1480 N N . TYR A 188 ? 0.9994 1.0150 1.2391 -0.0980 0.1513 -0.1101 571 TYR A N 1481 C CA . TYR A 188 ? 1.0695 1.0690 1.3040 -0.1064 0.1638 -0.0978 571 TYR A CA 1482 C C . TYR A 188 ? 1.1035 1.0963 1.3640 -0.1096 0.1793 -0.1045 571 TYR A C 1483 O O . TYR A 188 ? 1.1035 1.0847 1.3643 -0.1171 0.1921 -0.1012 571 TYR A O 1484 C CB . TYR A 188 ? 1.0978 1.0899 1.3122 -0.1058 0.1589 -0.0729 571 TYR A CB 1485 C CG . TYR A 188 ? 1.1272 1.1204 1.3558 -0.0997 0.1585 -0.0672 571 TYR A CG 1486 C CD1 . TYR A 188 ? 1.1278 1.1338 1.3635 -0.0910 0.1483 -0.0747 571 TYR A CD1 1487 C CD2 . TYR A 188 ? 1.1601 1.1412 1.3961 -0.1023 0.1696 -0.0545 571 TYR A CD2 1488 C CE1 . TYR A 188 ? 1.1471 1.1534 1.3961 -0.0855 0.1494 -0.0708 571 TYR A CE1 1489 C CE2 . TYR A 188 ? 1.1700 1.1511 1.4209 -0.0965 0.1707 -0.0498 571 TYR A CE2 1490 C CZ . TYR A 188 ? 1.1682 1.1618 1.4254 -0.0883 0.1608 -0.0585 571 TYR A CZ 1491 O OH . TYR A 188 ? 1.1685 1.1617 1.4403 -0.0826 0.1628 -0.0548 571 TYR A OH 1492 N N . ASN A 189 ? 1.1177 1.1171 1.3993 -0.1041 0.1785 -0.1133 572 ASN A N 1493 C CA . ASN A 189 ? 1.1668 1.1601 1.4759 -0.1068 0.1929 -0.1214 572 ASN A CA 1494 C C . ASN A 189 ? 1.1472 1.1519 1.4826 -0.1073 0.1959 -0.1489 572 ASN A C 1495 O O . ASN A 189 ? 1.1478 1.1475 1.5081 -0.1112 0.2089 -0.1581 572 ASN A O 1496 C CB . ASN A 189 ? 1.2037 1.1952 1.5209 -0.1009 0.1920 -0.1135 572 ASN A CB 1497 C CG . ASN A 189 ? 1.2356 1.2419 1.5714 -0.0943 0.1859 -0.1340 572 ASN A CG 1498 O OD1 . ASN A 189 ? 1.1533 1.1729 1.4781 -0.0880 0.1717 -0.1381 572 ASN A OD1 1499 N ND2 . ASN A 189 ? 1.3589 1.3625 1.7227 -0.0959 0.1971 -0.1470 572 ASN A ND2 1500 N N . ASP A 190 ? 1.1201 1.1406 1.4516 -0.1031 0.1838 -0.1618 573 ASP A N 1501 C CA . ASP A 190 ? 1.1204 1.1549 1.4767 -0.1029 0.1844 -0.1879 573 ASP A CA 1502 C C . ASP A 190 ? 1.1333 1.1721 1.4850 -0.1065 0.1843 -0.1949 573 ASP A C 1503 O O . ASP A 190 ? 1.1108 1.1579 1.4453 -0.1019 0.1722 -0.1935 573 ASP A O 1504 C CB . ASP A 190 ? 1.1008 1.1530 1.4616 -0.0933 0.1704 -0.1996 573 ASP A CB 1505 C CG . ASP A 190 ? 1.0778 1.1436 1.4698 -0.0936 0.1730 -0.2264 573 ASP A CG 1506 O OD1 . ASP A 190 ? 1.0108 1.0811 1.4168 -0.0987 0.1782 -0.2396 573 ASP A OD1 1507 O OD2 . ASP A 190 ? 1.0921 1.1646 1.4949 -0.0889 0.1698 -0.2348 573 ASP A OD2 1508 N N . THR A 191 ? 1.1631 1.1958 1.5322 -0.1145 0.1989 -0.2028 574 THR A N 1509 C CA . THR A 191 ? 1.1816 1.2159 1.5491 -0.1190 0.2027 -0.2092 574 THR A CA 1510 C C . THR A 191 ? 1.1750 1.2313 1.5582 -0.1140 0.1931 -0.2312 574 THR A C 1511 O O . THR A 191 ? 1.1294 1.1910 1.5004 -0.1123 0.1871 -0.2318 574 THR A O 1512 C CB . THR A 191 ? 1.2121 1.2331 1.5961 -0.1290 0.2229 -0.2111 574 THR A CB 1513 O OG1 . THR A 191 ? 1.2267 1.2276 1.5886 -0.1330 0.2304 -0.1875 574 THR A OG1 1514 C CG2 . THR A 191 ? 1.2140 1.2391 1.6044 -0.1335 0.2287 -0.2225 574 THR A CG2 1515 N N . GLU A 192 ? 1.2087 1.2778 1.6191 -0.1117 0.1917 -0.2492 575 GLU A N 1516 C CA . GLU A 192 ? 1.2198 1.3122 1.6476 -0.1068 0.1822 -0.2709 575 GLU A CA 1517 C C . GLU A 192 ? 1.1733 1.2787 1.5806 -0.0958 0.1631 -0.2674 575 GLU A C 1518 O O . GLU A 192 ? 1.1672 1.2875 1.5767 -0.0915 0.1551 -0.2767 575 GLU A O 1519 C CB . GLU A 192 ? 1.2654 1.3688 1.7273 -0.1080 0.1855 -0.2920 575 GLU A CB 1520 C CG . GLU A 192 ? 1.3180 1.4118 1.8060 -0.1192 0.2050 -0.2995 575 GLU A CG 1521 C CD . GLU A 192 ? 1.3585 1.4578 1.8805 -0.1224 0.2112 -0.3182 575 GLU A CD 1522 O OE1 . GLU A 192 ? 1.4020 1.5087 1.9249 -0.1167 0.2023 -0.3230 575 GLU A OE1 1523 O OE2 . GLU A 192 ? 1.3710 1.4670 1.9196 -0.1312 0.2260 -0.3287 575 GLU A OE2 1524 N N . LYS A 193 ? 1.1141 1.2139 1.5030 -0.0911 0.1566 -0.2533 576 LYS A N 1525 C CA . LYS A 193 ? 1.0434 1.1532 1.4115 -0.0809 0.1400 -0.2473 576 LYS A CA 1526 C C . LYS A 193 ? 0.9739 1.0746 1.3141 -0.0812 0.1371 -0.2305 576 LYS A C 1527 O O . LYS A 193 ? 0.9263 1.0371 1.2547 -0.0739 0.1252 -0.2301 576 LYS A O 1528 C CB . LYS A 193 ? 1.0753 1.1826 1.4357 -0.0758 0.1352 -0.2389 576 LYS A CB 1529 C CG . LYS A 193 ? 1.1062 1.2245 1.4921 -0.0742 0.1361 -0.2577 576 LYS A CG 1530 C CD . LYS A 193 ? 1.1364 1.2492 1.5156 -0.0699 0.1345 -0.2488 576 LYS A CD 1531 C CE . LYS A 193 ? 1.1495 1.2786 1.5176 -0.0584 0.1189 -0.2521 576 LYS A CE 1532 N NZ . LYS A 193 ? 1.1496 1.2970 1.5399 -0.0556 0.1156 -0.2772 576 LYS A NZ 1533 N N . LEU A 194 ? 0.9332 1.0147 1.2626 -0.0897 0.1480 -0.2167 577 LEU A N 1534 C CA . LEU A 194 ? 0.9157 0.9876 1.2184 -0.0917 0.1463 -0.2022 577 LEU A CA 1535 C C . LEU A 194 ? 0.9035 0.9826 1.2119 -0.0924 0.1473 -0.2142 577 LEU A C 1536 O O . LEU A 194 ? 0.8951 0.9766 1.1868 -0.0885 0.1393 -0.2097 577 LEU A O 1537 C CB . LEU A 194 ? 0.9360 0.9869 1.2260 -0.1009 0.1583 -0.1859 577 LEU A CB 1538 C CG . LEU A 194 ? 0.9672 1.0062 1.2267 -0.1047 0.1572 -0.1698 577 LEU A CG 1539 C CD1 . LEU A 194 ? 0.9704 1.0163 1.2105 -0.0973 0.1417 -0.1636 577 LEU A CD1 1540 C CD2 . LEU A 194 ? 0.9967 1.0184 1.2418 -0.1107 0.1643 -0.1503 577 LEU A CD2 1541 N N . GLN A 195 ? 0.9031 0.9856 1.2372 -0.0973 0.1578 -0.2295 578 GLN A N 1542 C CA . GLN A 195 ? 0.8948 0.9865 1.2407 -0.0976 0.1598 -0.2429 578 GLN A CA 1543 C C . GLN A 195 ? 0.8725 0.9852 1.2224 -0.0863 0.1441 -0.2524 578 GLN A C 1544 O O . GLN A 195 ? 0.8588 0.9750 1.2023 -0.0836 0.1410 -0.2532 578 GLN A O 1545 C CB . GLN A 195 ? 0.9138 1.0085 1.2922 -0.1043 0.1733 -0.2592 578 GLN A CB 1546 C CG . GLN A 195 ? 0.9261 1.0007 1.3000 -0.1155 0.1913 -0.2516 578 GLN A CG 1547 C CD . GLN A 195 ? 0.9301 1.0032 1.3349 -0.1227 0.2061 -0.2631 578 GLN A CD 1548 O OE1 . GLN A 195 ? 0.9072 0.9956 1.3396 -0.1201 0.2029 -0.2795 578 GLN A OE1 1549 N NE2 . GLN A 195 ? 0.9498 1.0044 1.3501 -0.1320 0.2229 -0.2549 578 GLN A NE2 1550 N N . ARG A 196 ? 0.8557 0.9820 1.2158 -0.0797 0.1350 -0.2594 579 ARG A N 1551 C CA . ARG A 196 ? 0.8563 1.0029 1.2168 -0.0679 0.1193 -0.2663 579 ARG A CA 1552 C C . ARG A 196 ? 0.8120 0.9524 1.1414 -0.0621 0.1100 -0.2488 579 ARG A C 1553 O O . ARG A 196 ? 0.7841 0.9341 1.1100 -0.0553 0.1025 -0.2509 579 ARG A O 1554 C CB . ARG A 196 ? 0.8819 1.0423 1.2556 -0.0625 0.1121 -0.2763 579 ARG A CB 1555 C CG . ARG A 196 ? 0.9238 1.0956 1.3321 -0.0670 0.1186 -0.2979 579 ARG A CG 1556 C CD . ARG A 196 ? 0.9552 1.1370 1.3749 -0.0637 0.1137 -0.3078 579 ARG A CD 1557 N NE . ARG A 196 ? 0.9816 1.1845 1.3959 -0.0513 0.0967 -0.3137 579 ARG A NE 1558 C CZ . ARG A 196 ? 0.9932 1.1958 1.3854 -0.0432 0.0871 -0.3026 579 ARG A CZ 1559 N NH1 . ARG A 196 ? 0.9987 1.1818 1.3723 -0.0458 0.0915 -0.2846 579 ARG A NH1 1560 N NH2 . ARG A 196 ? 0.9812 1.2043 1.3703 -0.0319 0.0727 -0.3093 579 ARG A NH2 1561 N N . ALA A 197 ? 0.7770 0.9016 1.0856 -0.0649 0.1111 -0.2315 580 ALA A N 1562 C CA . ALA A 197 ? 0.7654 0.8833 1.0457 -0.0610 0.1031 -0.2145 580 ALA A CA 1563 C C . ALA A 197 ? 0.7595 0.8679 1.0277 -0.0654 0.1074 -0.2101 580 ALA A C 1564 O O . ALA A 197 ? 0.7533 0.8642 1.0082 -0.0596 0.0996 -0.2052 580 ALA A O 1565 C CB . ALA A 197 ? 0.7608 0.8644 1.0245 -0.0643 0.1041 -0.1973 580 ALA A CB 1566 N N . GLN A 198 ? 0.7686 0.8656 1.0415 -0.0756 0.1208 -0.2119 581 GLN A N 1567 C CA . GLN A 198 ? 0.7793 0.8666 1.0420 -0.0808 0.1274 -0.2100 581 GLN A CA 1568 C C . GLN A 198 ? 0.7543 0.8561 1.0336 -0.0751 0.1254 -0.2248 581 GLN A C 1569 O O . GLN A 198 ? 0.7319 0.8291 0.9996 -0.0745 0.1254 -0.2219 581 GLN A O 1570 C CB . GLN A 198 ? 0.8063 0.8780 1.0699 -0.0929 0.1435 -0.2083 581 GLN A CB 1571 C CG . GLN A 198 ? 0.8504 0.9053 1.0908 -0.0988 0.1454 -0.1895 581 GLN A CG 1572 C CD . GLN A 198 ? 0.9007 0.9397 1.1391 -0.1101 0.1614 -0.1858 581 GLN A CD 1573 O OE1 . GLN A 198 ? 0.9304 0.9712 1.1902 -0.1139 0.1726 -0.1983 581 GLN A OE1 1574 N NE2 . GLN A 198 ? 0.9184 0.9422 1.1308 -0.1154 0.1626 -0.1680 581 GLN A NE2 1575 N N . ALA A 199 ? 0.7452 0.8648 1.0525 -0.0708 0.1237 -0.2408 582 ALA A N 1576 C CA . ALA A 199 ? 0.7231 0.8608 1.0487 -0.0634 0.1192 -0.2546 582 ALA A CA 1577 C C . ALA A 199 ? 0.7213 0.8673 1.0326 -0.0516 0.1045 -0.2481 582 ALA A C 1578 O O . ALA A 199 ? 0.7296 0.8787 1.0403 -0.0471 0.1030 -0.2493 582 ALA A O 1579 C CB . ALA A 199 ? 0.7074 0.8645 1.0655 -0.0615 0.1184 -0.2730 582 ALA A CB 1580 N N . TRP A 200 ? 0.7115 0.8601 1.0119 -0.0465 0.0949 -0.2407 583 TRP A N 1581 C CA . TRP A 200 ? 0.6963 0.8508 0.9812 -0.0356 0.0821 -0.2322 583 TRP A CA 1582 C C . TRP A 200 ? 0.7110 0.8478 0.9711 -0.0386 0.0842 -0.2175 583 TRP A C 1583 O O . TRP A 200 ? 0.6998 0.8406 0.9553 -0.0312 0.0789 -0.2157 583 TRP A O 1584 C CB . TRP A 200 ? 0.6839 0.8423 0.9609 -0.0307 0.0737 -0.2261 583 TRP A CB 1585 C CG . TRP A 200 ? 0.6783 0.8454 0.9425 -0.0183 0.0610 -0.2191 583 TRP A CG 1586 C CD1 . TRP A 200 ? 0.6648 0.8534 0.9393 -0.0063 0.0510 -0.2280 583 TRP A CD1 1587 C CD2 . TRP A 200 ? 0.6648 0.8195 0.9038 -0.0169 0.0576 -0.2014 583 TRP A CD2 1588 N NE1 . TRP A 200 ? 0.6604 0.8497 0.9170 0.0029 0.0424 -0.2160 583 TRP A NE1 1589 C CE2 . TRP A 200 ? 0.6534 0.8219 0.8893 -0.0035 0.0465 -0.2000 583 TRP A CE2 1590 C CE3 . TRP A 200 ? 0.6640 0.7981 0.8832 -0.0256 0.0627 -0.1869 583 TRP A CE3 1591 C CZ2 . TRP A 200 ? 0.6541 0.8153 0.8694 0.0009 0.0415 -0.1845 583 TRP A CZ2 1592 C CZ3 . TRP A 200 ? 0.6696 0.7976 0.8688 -0.0217 0.0566 -0.1726 583 TRP A CZ3 1593 C CH2 . TRP A 200 ? 0.6691 0.8100 0.8673 -0.0086 0.0467 -0.1714 583 TRP A CH2 1594 N N . GLU A 201 ? 0.7499 0.8673 0.9945 -0.0494 0.0919 -0.2072 584 GLU A N 1595 C CA . GLU A 201 ? 0.8101 0.9104 1.0301 -0.0541 0.0939 -0.1941 584 GLU A CA 1596 C C . GLU A 201 ? 0.7968 0.8944 1.0207 -0.0553 0.1003 -0.2010 584 GLU A C 1597 O O . GLU A 201 ? 0.8078 0.8987 1.0168 -0.0534 0.0979 -0.1943 584 GLU A O 1598 C CB . GLU A 201 ? 0.8856 0.9675 1.0897 -0.0661 0.1013 -0.1831 584 GLU A CB 1599 C CG . GLU A 201 ? 0.9769 1.0429 1.1530 -0.0709 0.1005 -0.1687 584 GLU A CG 1600 C CD . GLU A 201 ? 1.0558 1.1053 1.2153 -0.0828 0.1072 -0.1576 584 GLU A CD 1601 O OE1 . GLU A 201 ? 1.1344 1.1841 1.3019 -0.0855 0.1107 -0.1568 584 GLU A OE1 1602 O OE2 . GLU A 201 ? 1.0637 1.1000 1.2017 -0.0893 0.1090 -0.1496 584 GLU A OE2 1603 N N . LYS A 202 ? 0.7961 0.8983 1.0409 -0.0589 0.1094 -0.2145 585 LYS A N 1604 C CA . LYS A 202 ? 0.7988 0.8998 1.0513 -0.0595 0.1167 -0.2224 585 LYS A CA 1605 C C . LYS A 202 ? 0.7535 0.8701 1.0152 -0.0461 0.1071 -0.2265 585 LYS A C 1606 O O . LYS A 202 ? 0.7510 0.8608 1.0054 -0.0447 0.1093 -0.2241 585 LYS A O 1607 C CB . LYS A 202 ? 0.8303 0.9354 1.1073 -0.0654 0.1286 -0.2365 585 LYS A CB 1608 C CG . LYS A 202 ? 0.8823 0.9800 1.1638 -0.0701 0.1411 -0.2428 585 LYS A CG 1609 C CD . LYS A 202 ? 0.9247 1.0300 1.2353 -0.0745 0.1521 -0.2576 585 LYS A CD 1610 C CE . LYS A 202 ? 0.9707 1.0737 1.2920 -0.0760 0.1634 -0.2660 585 LYS A CE 1611 N NZ . LYS A 202 ? 0.9814 1.0923 1.3331 -0.0810 0.1748 -0.2801 585 LYS A NZ 1612 N N . GLU A 203 ? 0.7229 0.8597 0.9998 -0.0363 0.0967 -0.2322 586 GLU A N 1613 C CA . GLU A 203 ? 0.7257 0.8785 1.0088 -0.0221 0.0859 -0.2335 586 GLU A CA 1614 C C . GLU A 203 ? 0.7046 0.8476 0.9618 -0.0174 0.0789 -0.2176 586 GLU A C 1615 O O . GLU A 203 ? 0.6990 0.8437 0.9555 -0.0098 0.0765 -0.2155 586 GLU A O 1616 C CB . GLU A 203 ? 0.7280 0.9053 1.0297 -0.0130 0.0755 -0.2430 586 GLU A CB 1617 C CG . GLU A 203 ? 0.7629 0.9558 1.0963 -0.0143 0.0800 -0.2613 586 GLU A CG 1618 C CD . GLU A 203 ? 0.7996 0.9983 1.1477 -0.0101 0.0838 -0.2675 586 GLU A CD 1619 O OE1 . GLU A 203 ? 0.8339 1.0413 1.1795 0.0019 0.0751 -0.2634 586 GLU A OE1 1620 O OE2 . GLU A 203 ? 0.8306 1.0242 1.1928 -0.0186 0.0963 -0.2758 586 GLU A OE2 1621 N N . PHE A 204 ? 0.6620 0.7951 0.9004 -0.0220 0.0763 -0.2064 587 PHE A N 1622 C CA . PHE A 204 ? 0.6332 0.7560 0.8477 -0.0196 0.0706 -0.1907 587 PHE A CA 1623 C C . PHE A 204 ? 0.6232 0.7276 0.8242 -0.0261 0.0782 -0.1858 587 PHE A C 1624 O O . PHE A 204 ? 0.6080 0.7099 0.8014 -0.0197 0.0745 -0.1797 587 PHE A O 1625 C CB . PHE A 204 ? 0.6160 0.7313 0.8156 -0.0250 0.0681 -0.1802 587 PHE A CB 1626 C CG . PHE A 204 ? 0.6105 0.7134 0.7866 -0.0256 0.0640 -0.1641 587 PHE A CG 1627 C CD1 . PHE A 204 ? 0.6099 0.7206 0.7819 -0.0139 0.0546 -0.1576 587 PHE A CD1 1628 C CD2 . PHE A 204 ? 0.6222 0.7061 0.7803 -0.0379 0.0697 -0.1553 587 PHE A CD2 1629 C CE1 . PHE A 204 ? 0.6187 0.7180 0.7712 -0.0150 0.0515 -0.1430 587 PHE A CE1 1630 C CE2 . PHE A 204 ? 0.6224 0.6962 0.7606 -0.0393 0.0655 -0.1414 587 PHE A CE2 1631 C CZ . PHE A 204 ? 0.6309 0.7123 0.7676 -0.0280 0.0567 -0.1354 587 PHE A CZ 1632 N N . ILE A 205 ? 0.6304 0.7217 0.8285 -0.0386 0.0894 -0.1889 588 ILE A N 1633 C CA . ILE A 205 ? 0.6677 0.7411 0.8520 -0.0461 0.0978 -0.1864 588 ILE A CA 1634 C C . ILE A 205 ? 0.6870 0.7663 0.8861 -0.0381 0.1004 -0.1947 588 ILE A C 1635 O O . ILE A 205 ? 0.6711 0.7402 0.8593 -0.0369 0.1013 -0.1897 588 ILE A O 1636 C CB . ILE A 205 ? 0.6862 0.7458 0.8645 -0.0607 0.1102 -0.1889 588 ILE A CB 1637 C CG1 . ILE A 205 ? 0.6920 0.7433 0.8519 -0.0681 0.1072 -0.1769 588 ILE A CG1 1638 C CG2 . ILE A 205 ? 0.7044 0.7468 0.8697 -0.0680 0.1200 -0.1895 588 ILE A CG2 1639 C CD1 . ILE A 205 ? 0.6962 0.7394 0.8556 -0.0796 0.1178 -0.1791 588 ILE A CD1 1640 N N . ASN A 206 ? 0.7214 0.8174 0.9468 -0.0327 0.1016 -0.2075 589 ASN A N 1641 C CA . ASN A 206 ? 0.7515 0.8571 0.9957 -0.0234 0.1031 -0.2156 589 ASN A CA 1642 C C . ASN A 206 ? 0.7298 0.8442 0.9725 -0.0091 0.0919 -0.2086 589 ASN A C 1643 O O . ASN A 206 ? 0.7475 0.8570 0.9911 -0.0043 0.0948 -0.2073 589 ASN A O 1644 C CB . ASN A 206 ? 0.7707 0.8963 1.0457 -0.0201 0.1046 -0.2307 589 ASN A CB 1645 C CG . ASN A 206 ? 0.8098 0.9256 1.0929 -0.0313 0.1204 -0.2398 589 ASN A CG 1646 O OD1 . ASN A 206 ? 0.8424 0.9607 1.1408 -0.0284 0.1273 -0.2473 589 ASN A OD1 1647 N ND2 . ASN A 206 ? 0.8330 0.9356 1.1037 -0.0442 0.1273 -0.2375 589 ASN A ND2 1648 N N . PHE A 207 ? 0.6962 0.8233 0.9373 -0.0022 0.0800 -0.2041 590 PHE A N 1649 C CA . PHE A 207 ? 0.6933 0.8292 0.9311 0.0117 0.0693 -0.1961 590 PHE A CA 1650 C C . PHE A 207 ? 0.7039 0.8193 0.9193 0.0092 0.0714 -0.1828 590 PHE A C 1651 O O . PHE A 207 ? 0.7415 0.8567 0.9592 0.0182 0.0707 -0.1794 590 PHE A O 1652 C CB . PHE A 207 ? 0.6790 0.8289 0.9145 0.0175 0.0578 -0.1931 590 PHE A CB 1653 C CG . PHE A 207 ? 0.6784 0.8391 0.9106 0.0328 0.0472 -0.1850 590 PHE A CG 1654 C CD1 . PHE A 207 ? 0.6815 0.8651 0.9326 0.0465 0.0405 -0.1923 590 PHE A CD1 1655 C CD2 . PHE A 207 ? 0.6856 0.8339 0.8963 0.0336 0.0443 -0.1698 590 PHE A CD2 1656 C CE1 . PHE A 207 ? 0.6924 0.8858 0.9389 0.0615 0.0312 -0.1836 590 PHE A CE1 1657 C CE2 . PHE A 207 ? 0.7025 0.8597 0.9100 0.0480 0.0359 -0.1614 590 PHE A CE2 1658 C CZ . PHE A 207 ? 0.7015 0.8810 0.9259 0.0623 0.0295 -0.1679 590 PHE A CZ 1659 N N . VAL A 208 ? 0.6955 0.7939 0.8905 -0.0031 0.0741 -0.1756 591 VAL A N 1660 C CA . VAL A 208 ? 0.7021 0.7818 0.8759 -0.0074 0.0753 -0.1638 591 VAL A CA 1661 C C . VAL A 208 ? 0.7102 0.7755 0.8840 -0.0120 0.0863 -0.1683 591 VAL A C 1662 O O . VAL A 208 ? 0.7305 0.7879 0.8991 -0.0075 0.0865 -0.1624 591 VAL A O 1663 C CB . VAL A 208 ? 0.7016 0.7687 0.8548 -0.0202 0.0751 -0.1556 591 VAL A CB 1664 C CG1 . VAL A 208 ? 0.7079 0.7555 0.8404 -0.0272 0.0772 -0.1457 591 VAL A CG1 1665 C CG2 . VAL A 208 ? 0.6962 0.7759 0.8486 -0.0140 0.0645 -0.1491 591 VAL A CG2 1666 N N . LYS A 209 ? 0.7266 0.7880 0.9070 -0.0207 0.0963 -0.1789 592 LYS A N 1667 C CA . LYS A 209 ? 0.7498 0.7974 0.9310 -0.0256 0.1085 -0.1849 592 LYS A CA 1668 C C . LYS A 209 ? 0.7479 0.8035 0.9477 -0.0119 0.1090 -0.1884 592 LYS A C 1669 O O . LYS A 209 ? 0.7648 0.8060 0.9597 -0.0128 0.1160 -0.1873 592 LYS A O 1670 C CB . LYS A 209 ? 0.7641 0.8102 0.9531 -0.0355 0.1193 -0.1965 592 LYS A CB 1671 C CG . LYS A 209 ? 0.8055 0.8366 0.9945 -0.0423 0.1342 -0.2043 592 LYS A CG 1672 C CD . LYS A 209 ? 0.8173 0.8448 1.0089 -0.0537 0.1452 -0.2131 592 LYS A CD 1673 C CE . LYS A 209 ? 0.8183 0.8629 1.0421 -0.0473 0.1498 -0.2260 592 LYS A CE 1674 N NZ . LYS A 209 ? 0.8242 0.8680 1.0509 -0.0581 0.1579 -0.2321 592 LYS A NZ 1675 N N . ASN A 210 ? 0.7348 0.8137 0.9564 0.0006 0.1017 -0.1927 593 ASN A N 1676 C CA . ASN A 210 ? 0.7477 0.8384 0.9896 0.0155 0.1006 -0.1952 593 ASN A CA 1677 C C . ASN A 210 ? 0.7400 0.8380 0.9779 0.0298 0.0892 -0.1832 593 ASN A C 1678 O O . ASN A 210 ? 0.7598 0.8686 1.0139 0.0436 0.0874 -0.1833 593 ASN A O 1679 C CB . ASN A 210 ? 0.7614 0.8760 1.0316 0.0215 0.0990 -0.2079 593 ASN A CB 1680 C CG . ASN A 210 ? 0.7686 0.8764 1.0468 0.0087 0.1123 -0.2201 593 ASN A CG 1681 O OD1 . ASN A 210 ? 0.7646 0.8560 1.0407 0.0030 0.1249 -0.2228 593 ASN A OD1 1682 N ND2 . ASN A 210 ? 0.7688 0.8884 1.0564 0.0041 0.1107 -0.2275 593 ASN A ND2 1683 N N . TYR A 211 ? 0.7333 0.8261 0.9509 0.0272 0.0820 -0.1723 594 TYR A N 1684 C CA . TYR A 211 ? 0.7262 0.8260 0.9396 0.0408 0.0720 -0.1603 594 TYR A CA 1685 C C . TYR A 211 ? 0.7515 0.8349 0.9607 0.0440 0.0782 -0.1531 594 TYR A C 1686 O O . TYR A 211 ? 0.7582 0.8192 0.9528 0.0314 0.0862 -0.1514 594 TYR A O 1687 C CB . TYR A 211 ? 0.7132 0.8103 0.9070 0.0364 0.0644 -0.1504 594 TYR A CB 1688 C CG . TYR A 211 ? 0.6804 0.7900 0.8720 0.0514 0.0536 -0.1397 594 TYR A CG 1689 C CD1 . TYR A 211 ? 0.6899 0.7867 0.8681 0.0541 0.0533 -0.1259 594 TYR A CD1 1690 C CD2 . TYR A 211 ? 0.6644 0.7984 0.8669 0.0623 0.0440 -0.1436 594 TYR A CD2 1691 C CE1 . TYR A 211 ? 0.6924 0.7999 0.8676 0.0680 0.0445 -0.1152 594 TYR A CE1 1692 C CE2 . TYR A 211 ? 0.6739 0.8193 0.8718 0.0762 0.0345 -0.1337 594 TYR A CE2 1693 C CZ . TYR A 211 ? 0.6877 0.8196 0.8717 0.0793 0.0351 -0.1189 594 TYR A CZ 1694 O OH . TYR A 211 ? 0.6902 0.8329 0.8691 0.0934 0.0268 -0.1083 594 TYR A OH 1695 N N . LYS A 212 ? 0.7918 0.8867 1.0143 0.0609 0.0745 -0.1494 595 LYS A N 1696 C CA . LYS A 212 ? 0.8376 0.9181 1.0609 0.0663 0.0813 -0.1427 595 LYS A CA 1697 C C . LYS A 212 ? 0.8109 0.8902 1.0224 0.0755 0.0740 -0.1267 595 LYS A C 1698 O O . LYS A 212 ? 0.7900 0.8894 1.0075 0.0905 0.0639 -0.1216 595 LYS A O 1699 C CB . LYS A 212 ? 0.8894 0.9829 1.1385 0.0804 0.0839 -0.1481 595 LYS A CB 1700 C CG . LYS A 212 ? 0.9240 1.0239 1.1910 0.0747 0.0909 -0.1644 595 LYS A CG 1701 C CD . LYS A 212 ? 0.9904 1.0715 1.2647 0.0706 0.1064 -0.1692 595 LYS A CD 1702 C CE . LYS A 212 ? 1.0147 1.1039 1.3087 0.0896 0.1065 -0.1640 595 LYS A CE 1703 N NZ . LYS A 212 ? 1.0291 1.1038 1.3364 0.0879 0.1221 -0.1706 595 LYS A NZ 1704 N N . ASN A 213 ? 0.8065 0.8629 1.0010 0.0661 0.0791 -0.1191 596 ASN A N 1705 C CA . ASN A 213 ? 0.8211 0.8721 1.0074 0.0743 0.0758 -0.1036 596 ASN A CA 1706 C C . ASN A 213 ? 0.8702 0.8929 1.0455 0.0622 0.0861 -0.1007 596 ASN A C 1707 O O . ASN A 213 ? 0.8820 0.8926 1.0415 0.0459 0.0873 -0.1021 596 ASN A O 1708 C CB . ASN A 213 ? 0.7911 0.8519 0.9641 0.0751 0.0646 -0.0952 596 ASN A CB 1709 C CG . ASN A 213 ? 0.7873 0.8456 0.9541 0.0861 0.0615 -0.0787 596 ASN A CG 1710 O OD1 . ASN A 213 ? 0.8233 0.8652 0.9907 0.0873 0.0690 -0.0726 596 ASN A OD1 1711 N ND2 . ASN A 213 ? 0.7564 0.8302 0.9175 0.0941 0.0513 -0.0716 596 ASN A ND2 1712 N N . PRO A 214 ? 0.9318 0.9440 1.1159 0.0702 0.0937 -0.0966 597 PRO A N 1713 C CA . PRO A 214 ? 0.9655 0.9501 1.1400 0.0585 0.1039 -0.0947 597 PRO A CA 1714 C C . PRO A 214 ? 0.9726 0.9480 1.1290 0.0515 0.0993 -0.0830 597 PRO A C 1715 O O . PRO A 214 ? 0.9972 0.9524 1.1418 0.0359 0.1052 -0.0848 597 PRO A O 1716 C CB . PRO A 214 ? 0.9832 0.9618 1.1735 0.0727 0.1115 -0.0899 597 PRO A CB 1717 C CG . PRO A 214 ? 0.9735 0.9773 1.1823 0.0911 0.1055 -0.0906 597 PRO A CG 1718 C CD . PRO A 214 ? 0.9415 0.9674 1.1450 0.0906 0.0928 -0.0931 597 PRO A CD 1719 N N . ASN A 215 ? 0.9578 0.9487 1.1123 0.0626 0.0888 -0.0717 598 ASN A N 1720 C CA . ASN A 215 ? 0.9560 0.9406 1.0961 0.0577 0.0845 -0.0596 598 ASN A CA 1721 C C . ASN A 215 ? 0.9199 0.9041 1.0447 0.0408 0.0795 -0.0630 598 ASN A C 1722 O O . ASN A 215 ? 0.9042 0.8808 1.0180 0.0337 0.0772 -0.0543 598 ASN A O 1723 C CB . ASN A 215 ? 0.9808 0.9829 1.1230 0.0756 0.0757 -0.0465 598 ASN A CB 1724 C CG . ASN A 215 ? 1.0290 1.0319 1.1844 0.0938 0.0797 -0.0390 598 ASN A CG 1725 O OD1 . ASN A 215 ? 1.0515 1.0349 1.2109 0.0920 0.0898 -0.0365 598 ASN A OD1 1726 N ND2 . ASN A 215 ? 1.0746 1.1003 1.2367 0.1117 0.0718 -0.0352 598 ASN A ND2 1727 N N . LEU A 216 ? 0.8916 0.8851 1.0172 0.0352 0.0777 -0.0748 599 LEU A N 1728 C CA . LEU A 216 ? 0.8712 0.8659 0.9837 0.0211 0.0729 -0.0770 599 LEU A CA 1729 C C . LEU A 216 ? 0.8675 0.8516 0.9760 0.0057 0.0802 -0.0902 599 LEU A C 1730 O O . LEU A 216 ? 0.9251 0.9126 1.0453 0.0093 0.0855 -0.1006 599 LEU A O 1731 C CB . LEU A 216 ? 0.8398 0.8576 0.9564 0.0294 0.0634 -0.0776 599 LEU A CB 1732 C CG . LEU A 216 ? 0.8285 0.8616 0.9491 0.0469 0.0557 -0.0668 599 LEU A CG 1733 C CD1 . LEU A 216 ? 0.8141 0.8697 0.9397 0.0535 0.0477 -0.0723 599 LEU A CD1 1734 C CD2 . LEU A 216 ? 0.8356 0.8614 0.9441 0.0440 0.0529 -0.0527 599 LEU A CD2 1735 N N . THR A 217 ? 0.8432 0.8156 0.9357 -0.0110 0.0804 -0.0897 600 THR A N 1736 C CA . THR A 217 ? 0.8534 0.8200 0.9387 -0.0254 0.0851 -0.1010 600 THR A CA 1737 C C . THR A 217 ? 0.8307 0.8099 0.9100 -0.0292 0.0768 -0.0986 600 THR A C 1738 O O . THR A 217 ? 0.8261 0.8051 0.8952 -0.0335 0.0702 -0.0887 600 THR A O 1739 C CB . THR A 217 ? 0.8738 0.8181 0.9440 -0.0421 0.0920 -0.1037 600 THR A CB 1740 O OG1 . THR A 217 ? 0.8979 0.8375 0.9570 -0.0477 0.0859 -0.0923 600 THR A OG1 1741 C CG2 . THR A 217 ? 0.9030 0.8338 0.9814 -0.0386 0.1027 -0.1090 600 THR A CG2 1742 N N . ILE A 218 ? 0.8040 0.7942 0.8918 -0.0273 0.0777 -0.1078 601 ILE A N 1743 C CA . ILE A 218 ? 0.7770 0.7791 0.8629 -0.0297 0.0716 -0.1073 601 ILE A CA 1744 C C . ILE A 218 ? 0.7849 0.7777 0.8609 -0.0456 0.0778 -0.1148 601 ILE A C 1745 O O . ILE A 218 ? 0.8267 0.8150 0.9081 -0.0481 0.0866 -0.1258 601 ILE A O 1746 C CB . ILE A 218 ? 0.7576 0.7799 0.8622 -0.0159 0.0686 -0.1133 601 ILE A CB 1747 C CG1 . ILE A 218 ? 0.7370 0.7694 0.8499 0.0009 0.0626 -0.1058 601 ILE A CG1 1748 C CG2 . ILE A 218 ? 0.7553 0.7887 0.8593 -0.0189 0.0633 -0.1138 601 ILE A CG2 1749 C CD1 . ILE A 218 ? 0.7242 0.7766 0.8558 0.0152 0.0598 -0.1130 601 ILE A CD1 1750 N N . SER A 219 ? 0.7819 0.7722 0.8438 -0.0557 0.0736 -0.1083 602 SER A N 1751 C CA . SER A 219 ? 0.7762 0.7583 0.8264 -0.0704 0.0788 -0.1130 602 SER A CA 1752 C C . SER A 219 ? 0.7667 0.7589 0.8165 -0.0719 0.0735 -0.1088 602 SER A C 1753 O O . SER A 219 ? 0.7605 0.7615 0.8121 -0.0660 0.0649 -0.0994 602 SER A O 1754 C CB . SER A 219 ? 0.7875 0.7531 0.8170 -0.0841 0.0796 -0.1083 602 SER A CB 1755 O OG . SER A 219 ? 0.8245 0.7798 0.8549 -0.0825 0.0843 -0.1111 602 SER A OG 1756 N N . PHE A 220 ? 0.7717 0.7613 0.8190 -0.0802 0.0796 -0.1153 603 PHE A N 1757 C CA . PHE A 220 ? 0.7833 0.7775 0.8267 -0.0850 0.0766 -0.1100 603 PHE A CA 1758 C C . PHE A 220 ? 0.7966 0.7803 0.8181 -0.0972 0.0733 -0.0994 603 PHE A C 1759 O O . PHE A 220 ? 0.8113 0.7820 0.8188 -0.1059 0.0772 -0.1013 603 PHE A O 1760 C CB . PHE A 220 ? 0.7953 0.7890 0.8442 -0.0900 0.0860 -0.1202 603 PHE A CB 1761 C CG . PHE A 220 ? 0.7737 0.7787 0.8459 -0.0794 0.0893 -0.1320 603 PHE A CG 1762 C CD1 . PHE A 220 ? 0.7846 0.7845 0.8628 -0.0796 0.0985 -0.1431 603 PHE A CD1 1763 C CD2 . PHE A 220 ? 0.7573 0.7788 0.8461 -0.0690 0.0831 -0.1324 603 PHE A CD2 1764 C CE1 . PHE A 220 ? 0.7864 0.7988 0.8881 -0.0694 0.1007 -0.1536 603 PHE A CE1 1765 C CE2 . PHE A 220 ? 0.7660 0.8002 0.8767 -0.0593 0.0848 -0.1439 603 PHE A CE2 1766 C CZ . PHE A 220 ? 0.7750 0.8054 0.8930 -0.0594 0.0933 -0.1541 603 PHE A CZ 1767 N N . THR A 221 ? 0.8268 0.8164 0.8456 -0.0977 0.0663 -0.0888 604 THR A N 1768 C CA . THR A 221 ? 0.8841 0.8667 0.8839 -0.1088 0.0618 -0.0777 604 THR A CA 1769 C C . THR A 221 ? 0.9426 0.9187 0.9304 -0.1202 0.0675 -0.0786 604 THR A C 1770 O O . THR A 221 ? 0.8949 0.8748 0.8924 -0.1181 0.0732 -0.0841 604 THR A O 1771 C CB . THR A 221 ? 0.8788 0.8712 0.8824 -0.1037 0.0519 -0.0644 604 THR A CB 1772 O OG1 . THR A 221 ? 0.8695 0.8717 0.8861 -0.0977 0.0526 -0.0654 604 THR A OG1 1773 C CG2 . THR A 221 ? 0.8664 0.8637 0.8784 -0.0934 0.0468 -0.0617 604 THR A CG2 1774 N N . ALA A 222 ? 1.0615 1.0280 1.0280 -0.1324 0.0660 -0.0732 605 ALA A N 1775 C CA . ALA A 222 ? 1.1642 1.1237 1.1139 -0.1442 0.0705 -0.0716 605 ALA A CA 1776 C C . ALA A 222 ? 1.2188 1.1857 1.1684 -0.1444 0.0644 -0.0580 605 ALA A C 1777 O O . ALA A 222 ? 1.2399 1.2106 1.1845 -0.1457 0.0545 -0.0459 605 ALA A O 1778 C CB . ALA A 222 ? 1.1883 1.1357 1.1140 -0.1570 0.0704 -0.0718 605 ALA A CB 1779 N N . GLU A 223 ? 1.2765 1.2450 1.2332 -0.1432 0.0711 -0.0600 606 GLU A N 1780 C CA . GLU A 223 ? 1.3170 1.2909 1.2759 -0.1430 0.0679 -0.0478 606 GLU A CA 1781 C C . GLU A 223 ? 1.3330 1.2998 1.2678 -0.1554 0.0672 -0.0378 606 GLU A C 1782 O O . GLU A 223 ? 1.3333 1.2942 1.2489 -0.1637 0.0635 -0.0367 606 GLU A O 1783 C CB . GLU A 223 ? 1.3430 1.3203 1.3203 -0.1375 0.0768 -0.0551 606 GLU A CB 1784 C CG . GLU A 223 ? 1.3776 1.3599 1.3624 -0.1354 0.0755 -0.0442 606 GLU A CG 1785 C CD . GLU A 223 ? 1.4165 1.3906 1.3916 -0.1438 0.0847 -0.0411 606 GLU A CD 1786 O OE1 . GLU A 223 ? 1.4250 1.4007 1.4163 -0.1404 0.0924 -0.0448 606 GLU A OE1 1787 O OE2 . GLU A 223 ? 1.4486 1.4147 1.4000 -0.1538 0.0846 -0.0351 606 GLU A OE2 1788 N N . GLU B 8 ? 1.8447 1.6576 1.7059 -0.0165 0.0543 -0.0214 391 GLU B N 1789 C CA . GLU B 8 ? 1.8895 1.6917 1.7369 -0.0151 0.0489 -0.0183 391 GLU B CA 1790 C C . GLU B 8 ? 1.9462 1.7322 1.7699 -0.0127 0.0392 -0.0137 391 GLU B C 1791 O O . GLU B 8 ? 1.9766 1.7618 1.7964 -0.0102 0.0298 -0.0109 391 GLU B O 1792 C CB . GLU B 8 ? 1.8983 1.6838 1.7376 -0.0180 0.0608 -0.0195 391 GLU B CB 1793 C CG . GLU B 8 ? 1.8723 1.6734 1.7377 -0.0203 0.0679 -0.0246 391 GLU B CG 1794 C CD . GLU B 8 ? 1.8657 1.6570 1.7291 -0.0216 0.0716 -0.0247 391 GLU B CD 1795 O OE1 . GLU B 8 ? 1.9087 1.6755 1.7518 -0.0234 0.0798 -0.0218 391 GLU B OE1 1796 O OE2 . GLU B 8 ? 1.7242 1.5315 1.6056 -0.0204 0.0665 -0.0276 391 GLU B OE2 1797 N N . LYS B 9 ? 1.9750 1.7474 1.7835 -0.0131 0.0411 -0.0137 392 LYS B N 1798 C CA . LYS B 9 ? 1.9785 1.7350 1.7648 -0.0107 0.0305 -0.0106 392 LYS B CA 1799 C C . LYS B 9 ? 1.9528 1.7137 1.7426 -0.0101 0.0260 -0.0117 392 LYS B C 1800 O O . LYS B 9 ? 1.9379 1.7066 1.7337 -0.0080 0.0129 -0.0095 392 LYS B O 1801 C CB . LYS B 9 ? 1.9963 1.7216 1.7498 -0.0110 0.0369 -0.0095 392 LYS B CB 1802 C CG . LYS B 9 ? 1.9812 1.6978 1.7270 -0.0103 0.0360 -0.0066 392 LYS B CG 1803 C CD . LYS B 9 ? 1.9886 1.6779 1.7086 -0.0119 0.0491 -0.0054 392 LYS B CD 1804 C CE . LYS B 9 ? 1.9749 1.6594 1.6955 -0.0121 0.0509 -0.0028 392 LYS B CE 1805 N NZ . LYS B 9 ? 1.9884 1.6516 1.6934 -0.0150 0.0681 -0.0017 392 LYS B NZ 1806 N N . GLU B 10 ? 1.9629 1.7182 1.7501 -0.0121 0.0372 -0.0151 393 GLU B N 1807 C CA . GLU B 10 ? 1.9318 1.6895 1.7227 -0.0116 0.0344 -0.0169 393 GLU B CA 1808 C C . GLU B 10 ? 1.9226 1.7077 1.7459 -0.0121 0.0341 -0.0177 393 GLU B C 1809 O O . GLU B 10 ? 1.9577 1.7468 1.7875 -0.0114 0.0298 -0.0183 393 GLU B O 1810 C CB . GLU B 10 ? 1.9588 1.6968 1.7316 -0.0130 0.0477 -0.0207 393 GLU B CB 1811 C CG . GLU B 10 ? 1.9815 1.6892 1.7177 -0.0122 0.0508 -0.0198 393 GLU B CG 1812 C CD . GLU B 10 ? 1.9664 1.6649 1.6961 -0.0145 0.0668 -0.0196 393 GLU B CD 1813 O OE1 . GLU B 10 ? 1.9220 1.6379 1.6754 -0.0165 0.0706 -0.0194 393 GLU B OE1 1814 O OE2 . GLU B 10 ? 1.9625 1.6350 1.6626 -0.0143 0.0757 -0.0197 393 GLU B OE2 1815 N N . TYR B 11 ? 1.8993 1.7017 1.7420 -0.0130 0.0388 -0.0182 394 TYR B N 1816 C CA . TYR B 11 ? 1.8246 1.6538 1.6966 -0.0124 0.0369 -0.0184 394 TYR B CA 1817 C C . TYR B 11 ? 1.8167 1.6580 1.6971 -0.0099 0.0232 -0.0138 394 TYR B C 1818 O O . TYR B 11 ? 1.7880 1.6418 1.6839 -0.0092 0.0209 -0.0131 394 TYR B O 1819 C CB . TYR B 11 ? 1.7612 1.6050 1.6485 -0.0129 0.0408 -0.0198 394 TYR B CB 1820 C CG . TYR B 11 ? 1.7072 1.5776 1.6218 -0.0116 0.0385 -0.0205 394 TYR B CG 1821 C CD1 . TYR B 11 ? 1.6642 1.5427 1.5949 -0.0130 0.0470 -0.0251 394 TYR B CD1 1822 C CD2 . TYR B 11 ? 1.6783 1.5654 1.6024 -0.0086 0.0280 -0.0163 394 TYR B CD2 1823 C CE1 . TYR B 11 ? 1.5829 1.4844 1.5363 -0.0110 0.0434 -0.0256 394 TYR B CE1 1824 C CE2 . TYR B 11 ? 1.6087 1.5183 1.5536 -0.0066 0.0259 -0.0163 394 TYR B CE2 1825 C CZ . TYR B 11 ? 1.5626 1.4789 1.5211 -0.0076 0.0328 -0.0210 394 TYR B CZ 1826 O OH . TYR B 11 ? 1.4922 1.4297 1.4695 -0.0050 0.0293 -0.0208 394 TYR B OH 1827 N N . PHE B 12 ? 1.8216 1.6583 1.6925 -0.0084 0.0145 -0.0105 395 PHE B N 1828 C CA . PHE B 12 ? 1.7931 1.6424 1.6750 -0.0061 0.0023 -0.0058 395 PHE B CA 1829 C C . PHE B 12 ? 1.8146 1.6560 1.6933 -0.0060 -0.0044 -0.0047 395 PHE B C 1830 O O . PHE B 12 ? 1.7945 1.6504 1.6906 -0.0049 -0.0112 -0.0010 395 PHE B O 1831 C CB . PHE B 12 ? 1.7560 1.6014 1.6302 -0.0045 -0.0047 -0.0032 395 PHE B CB 1832 C CG . PHE B 12 ? 1.6956 1.5475 1.5732 -0.0043 0.0007 -0.0047 395 PHE B CG 1833 C CD1 . PHE B 12 ? 1.6326 1.5080 1.5305 -0.0026 0.0002 -0.0039 395 PHE B CD1 1834 C CD2 . PHE B 12 ? 1.7120 1.5452 1.5716 -0.0056 0.0064 -0.0069 395 PHE B CD2 1835 C CE1 . PHE B 12 ? 1.6371 1.5177 1.5382 -0.0022 0.0042 -0.0065 395 PHE B CE1 1836 C CE2 . PHE B 12 ? 1.6988 1.5372 1.5636 -0.0057 0.0111 -0.0086 395 PHE B CE2 1837 C CZ . PHE B 12 ? 1.6594 1.5217 1.5453 -0.0040 0.0095 -0.0091 395 PHE B CZ 1838 N N . ASP B 13 ? 1.8407 1.6585 1.6971 -0.0070 -0.0024 -0.0080 396 ASP B N 1839 C CA . ASP B 13 ? 1.8556 1.6624 1.7059 -0.0066 -0.0094 -0.0087 396 ASP B CA 1840 C C . ASP B 13 ? 1.8398 1.6550 1.7057 -0.0074 -0.0049 -0.0104 396 ASP B C 1841 O O . ASP B 13 ? 1.8486 1.6586 1.7157 -0.0071 -0.0118 -0.0108 396 ASP B O 1842 C CB . ASP B 13 ? 1.8805 1.6578 1.6984 -0.0066 -0.0080 -0.0125 396 ASP B CB 1843 C CG . ASP B 13 ? 1.8909 1.6561 1.6912 -0.0051 -0.0157 -0.0103 396 ASP B CG 1844 O OD1 . ASP B 13 ? 1.8654 1.6323 1.6701 -0.0035 -0.0297 -0.0077 396 ASP B OD1 1845 O OD2 . ASP B 13 ? 1.9120 1.6659 1.6958 -0.0055 -0.0077 -0.0109 396 ASP B OD2 1846 N N . GLN B 14 ? 1.8142 1.6408 1.6918 -0.0084 0.0060 -0.0121 397 GLN B N 1847 C CA . GLN B 14 ? 1.8328 1.6697 1.7286 -0.0086 0.0100 -0.0133 397 GLN B CA 1848 C C . GLN B 14 ? 1.7081 1.5716 1.6300 -0.0076 0.0103 -0.0098 397 GLN B C 1849 O O . GLN B 14 ? 1.7022 1.5762 1.6412 -0.0069 0.0089 -0.0082 397 GLN B O 1850 C CB . GLN B 14 ? 1.9560 1.7800 1.8426 -0.0099 0.0231 -0.0197 397 GLN B CB 1851 C CG . GLN B 14 ? 2.0211 1.8555 1.9281 -0.0097 0.0280 -0.0218 397 GLN B CG 1852 C CD . GLN B 14 ? 2.0812 1.9131 1.9937 -0.0087 0.0198 -0.0209 397 GLN B CD 1853 O OE1 . GLN B 14 ? 2.1456 1.9653 2.0451 -0.0084 0.0107 -0.0200 397 GLN B OE1 1854 N NE2 . GLN B 14 ? 2.0948 1.9379 2.0282 -0.0081 0.0225 -0.0213 397 GLN B NE2 1855 N N . HIS B 15 ? 1.5666 1.4399 1.4911 -0.0073 0.0122 -0.0089 398 HIS B N 1856 C CA . HIS B 15 ? 1.4334 1.3311 1.3790 -0.0054 0.0098 -0.0051 398 HIS B CA 1857 C C . HIS B 15 ? 1.2703 1.1765 1.2242 -0.0036 -0.0006 0.0017 398 HIS B C 1858 O O . HIS B 15 ? 1.1790 1.0997 1.1500 -0.0022 -0.0022 0.0055 398 HIS B O 1859 C CB . HIS B 15 ? 1.4675 1.3735 1.4136 -0.0049 0.0126 -0.0064 398 HIS B CB 1860 C CG . HIS B 15 ? 1.5172 1.4453 1.4827 -0.0029 0.0135 -0.0060 398 HIS B CG 1861 N ND1 . HIS B 15 ? 1.5595 1.4925 1.5361 -0.0033 0.0196 -0.0100 398 HIS B ND1 1862 C CD2 . HIS B 15 ? 1.5360 1.4821 1.5109 0.0001 0.0086 -0.0021 398 HIS B CD2 1863 C CE1 . HIS B 15 ? 1.5603 1.5131 1.5517 -0.0005 0.0171 -0.0087 398 HIS B CE1 1864 N NE2 . HIS B 15 ? 1.5631 1.5237 1.5522 0.0017 0.0109 -0.0039 398 HIS B NE2 1865 N N . PHE B 16 ? 1.1253 1.0220 1.0683 -0.0037 -0.0074 0.0036 399 PHE B N 1866 C CA . PHE B 16 ? 1.0010 0.9043 0.9544 -0.0025 -0.0171 0.0099 399 PHE B CA 1867 C C . PHE B 16 ? 0.9398 0.8323 0.8941 -0.0036 -0.0219 0.0098 399 PHE B C 1868 O O . PHE B 16 ? 0.9464 0.8467 0.9154 -0.0031 -0.0286 0.0153 399 PHE B O 1869 C CB . PHE B 16 ? 0.9706 0.8752 0.9203 -0.0012 -0.0231 0.0126 399 PHE B CB 1870 C CG . PHE B 16 ? 0.9256 0.8449 0.8797 0.0004 -0.0184 0.0129 399 PHE B CG 1871 C CD1 . PHE B 16 ? 0.9399 0.8514 0.8805 0.0002 -0.0150 0.0087 399 PHE B CD1 1872 C CD2 . PHE B 16 ? 0.8848 0.8248 0.8561 0.0024 -0.0164 0.0166 399 PHE B CD2 1873 C CE1 . PHE B 16 ? 0.9311 0.8564 0.8776 0.0018 -0.0107 0.0076 399 PHE B CE1 1874 C CE2 . PHE B 16 ? 0.8809 0.8343 0.8554 0.0046 -0.0124 0.0156 399 PHE B CE2 1875 C CZ . PHE B 16 ? 0.9027 0.8491 0.8656 0.0042 -0.0098 0.0106 399 PHE B CZ 1876 N N . GLY B 17 ? 0.9049 0.7804 0.8454 -0.0051 -0.0173 0.0036 400 GLY B N 1877 C CA . GLY B 17 ? 0.8620 0.7327 0.8092 -0.0057 -0.0182 0.0023 400 GLY B CA 1878 C C . GLY B 17 ? 0.8366 0.6951 0.7802 -0.0060 -0.0293 0.0029 400 GLY B C 1879 O O . GLY B 17 ? 0.8536 0.7049 0.7865 -0.0058 -0.0359 0.0033 400 GLY B O 1880 N N . PRO B 18 ? 0.8171 0.6736 0.7717 -0.0064 -0.0324 0.0028 401 PRO B N 1881 C CA . PRO B 18 ? 0.8251 0.6683 0.7773 -0.0069 -0.0440 0.0018 401 PRO B CA 1882 C C . PRO B 18 ? 0.8007 0.6559 0.7710 -0.0067 -0.0542 0.0092 401 PRO B C 1883 O O . PRO B 18 ? 0.8714 0.7147 0.8385 -0.0071 -0.0652 0.0075 401 PRO B O 1884 C CB . PRO B 18 ? 0.8334 0.6731 0.7963 -0.0073 -0.0431 -0.0004 401 PRO B CB 1885 C CG . PRO B 18 ? 0.8131 0.6727 0.7948 -0.0066 -0.0345 0.0040 401 PRO B CG 1886 C CD . PRO B 18 ? 0.8138 0.6795 0.7846 -0.0062 -0.0263 0.0033 401 PRO B CD 1887 N N . PHE B 19 ? 0.7389 0.6165 0.7281 -0.0060 -0.0510 0.0169 402 PHE B N 1888 C CA . PHE B 19 ? 0.7149 0.6051 0.7253 -0.0058 -0.0586 0.0248 402 PHE B CA 1889 C C . PHE B 19 ? 0.6947 0.5924 0.7023 -0.0045 -0.0601 0.0275 402 PHE B C 1890 O O . PHE B 19 ? 0.6859 0.5935 0.7111 -0.0042 -0.0658 0.0335 402 PHE B O 1891 C CB . PHE B 19 ? 0.7034 0.6131 0.7392 -0.0053 -0.0545 0.0330 402 PHE B CB 1892 C CG . PHE B 19 ? 0.7107 0.6141 0.7516 -0.0061 -0.0526 0.0308 402 PHE B CG 1893 C CD1 . PHE B 19 ? 0.7185 0.6071 0.7630 -0.0078 -0.0609 0.0274 402 PHE B CD1 1894 C CD2 . PHE B 19 ? 0.6910 0.6025 0.7337 -0.0048 -0.0434 0.0310 402 PHE B CD2 1895 C CE1 . PHE B 19 ? 0.7125 0.5945 0.7620 -0.0082 -0.0591 0.0245 402 PHE B CE1 1896 C CE2 . PHE B 19 ? 0.7028 0.6083 0.7517 -0.0052 -0.0418 0.0286 402 PHE B CE2 1897 C CZ . PHE B 19 ? 0.7086 0.5990 0.7605 -0.0069 -0.0492 0.0253 402 PHE B CZ 1898 N N . PHE B 20 ? 0.6894 0.5828 0.6771 -0.0037 -0.0544 0.0233 403 PHE B N 1899 C CA . PHE B 20 ? 0.6897 0.5892 0.6742 -0.0021 -0.0554 0.0251 403 PHE B CA 1900 C C . PHE B 20 ? 0.7217 0.6005 0.6786 -0.0023 -0.0568 0.0183 403 PHE B C 1901 O O . PHE B 20 ? 0.7028 0.5685 0.6423 -0.0032 -0.0508 0.0127 403 PHE B O 1902 C CB . PHE B 20 ? 0.6650 0.5840 0.6559 -0.0003 -0.0458 0.0283 403 PHE B CB 1903 C CG . PHE B 20 ? 0.6336 0.5735 0.6489 0.0008 -0.0448 0.0367 403 PHE B CG 1904 C CD1 . PHE B 20 ? 0.6354 0.5811 0.6609 0.0005 -0.0410 0.0391 403 PHE B CD1 1905 C CD2 . PHE B 20 ? 0.6186 0.5719 0.6467 0.0027 -0.0469 0.0427 403 PHE B CD2 1906 C CE1 . PHE B 20 ? 0.6233 0.5868 0.6695 0.0021 -0.0395 0.0482 403 PHE B CE1 1907 C CE2 . PHE B 20 ? 0.6186 0.5902 0.6674 0.0042 -0.0443 0.0515 403 PHE B CE2 1908 C CZ . PHE B 20 ? 0.6050 0.5813 0.6620 0.0039 -0.0406 0.0546 403 PHE B CZ 1909 N N . ARG B 21 ? 0.7651 0.6404 0.7188 -0.0011 -0.0645 0.0192 404 ARG B N 1910 C CA . ARG B 21 ? 0.8219 0.6792 0.7496 -0.0004 -0.0654 0.0145 404 ARG B CA 1911 C C . ARG B 21 ? 0.7990 0.6690 0.7298 0.0013 -0.0608 0.0168 404 ARG B C 1912 O O . ARG B 21 ? 0.7744 0.6659 0.7264 0.0024 -0.0586 0.0217 404 ARG B O 1913 C CB . ARG B 21 ? 0.8853 0.7254 0.8045 0.0001 -0.0797 0.0128 404 ARG B CB 1914 C CG . ARG B 21 ? 0.9570 0.8092 0.8982 0.0015 -0.0899 0.0178 404 ARG B CG 1915 C CD . ARG B 21 ? 1.0542 0.8872 0.9831 0.0029 -0.1048 0.0149 404 ARG B CD 1916 N NE . ARG B 21 ? 1.1489 0.9940 1.0997 0.0047 -0.1136 0.0192 404 ARG B NE 1917 C CZ . ARG B 21 ? 1.2304 1.0903 1.2126 0.0040 -0.1194 0.0235 404 ARG B CZ 1918 N NH1 . ARG B 21 ? 1.2110 1.0758 1.2075 0.0015 -0.1180 0.0246 404 ARG B NH1 1919 N NH2 . ARG B 21 ? 1.2575 1.1277 1.2593 0.0060 -0.1263 0.0270 404 ARG B NH2 1920 N N . THR B 22 ? 0.8149 0.6709 0.7242 0.0018 -0.0591 0.0134 405 THR B N 1921 C CA . THR B 22 ? 0.8199 0.6853 0.7312 0.0037 -0.0551 0.0145 405 THR B CA 1922 C C . THR B 22 ? 0.8394 0.6927 0.7408 0.0057 -0.0643 0.0146 405 THR B C 1923 O O . THR B 22 ? 0.8300 0.6603 0.7090 0.0055 -0.0689 0.0118 405 THR B O 1924 C CB . THR B 22 ? 0.8255 0.6869 0.7236 0.0025 -0.0430 0.0105 405 THR B CB 1925 O OG1 . THR B 22 ? 0.8387 0.6742 0.7101 0.0013 -0.0422 0.0067 405 THR B OG1 1926 C CG2 . THR B 22 ? 0.8174 0.6916 0.7270 0.0010 -0.0346 0.0100 405 THR B CG2 1927 N N . GLU B 23 ? 0.8452 0.7139 0.7634 0.0082 -0.0672 0.0179 406 GLU B N 1928 C CA . GLU B 23 ? 0.8716 0.7317 0.7824 0.0108 -0.0734 0.0177 406 GLU B CA 1929 C C . GLU B 23 ? 0.8432 0.7044 0.7454 0.0112 -0.0630 0.0154 406 GLU B C 1930 O O . GLU B 23 ? 0.8296 0.7102 0.7458 0.0115 -0.0549 0.0157 406 GLU B O 1931 C CB . GLU B 23 ? 0.9136 0.7906 0.8495 0.0137 -0.0804 0.0218 406 GLU B CB 1932 C CG . GLU B 23 ? 0.9794 0.8585 0.9312 0.0131 -0.0911 0.0245 406 GLU B CG 1933 C CD . GLU B 23 ? 1.0585 0.9122 0.9915 0.0127 -0.1034 0.0215 406 GLU B CD 1934 O OE1 . GLU B 23 ? 1.0897 0.9258 1.0017 0.0145 -0.1074 0.0193 406 GLU B OE1 1935 O OE2 . GLU B 23 ? 1.1264 0.9771 1.0653 0.0109 -0.1094 0.0214 406 GLU B OE2 1936 N N . GLN B 24 ? 0.8392 0.6793 0.7187 0.0114 -0.0635 0.0131 407 GLN B N 1937 C CA . GLN B 24 ? 0.8229 0.6604 0.6937 0.0109 -0.0531 0.0104 407 GLN B CA 1938 C C . GLN B 24 ? 0.8038 0.6271 0.6627 0.0133 -0.0573 0.0105 407 GLN B C 1939 O O . GLN B 24 ? 0.8137 0.6159 0.6548 0.0143 -0.0657 0.0115 407 GLN B O 1940 C CB . GLN B 24 ? 0.8581 0.6820 0.7114 0.0073 -0.0439 0.0075 407 GLN B CB 1941 C CG . GLN B 24 ? 0.9054 0.7258 0.7522 0.0059 -0.0324 0.0045 407 GLN B CG 1942 C CD . GLN B 24 ? 0.9500 0.7614 0.7862 0.0022 -0.0215 0.0016 407 GLN B CD 1943 O OE1 . GLN B 24 ? 0.9860 0.7738 0.7989 0.0010 -0.0183 0.0009 407 GLN B OE1 1944 N NE2 . GLN B 24 ? 0.9526 0.7824 0.8059 0.0008 -0.0156 0.0000 407 GLN B NE2 1945 N N . LEU B 25 ? 0.7575 0.5914 0.6256 0.0147 -0.0518 0.0093 408 LEU B N 1946 C CA . LEU B 25 ? 0.7619 0.5841 0.6222 0.0173 -0.0547 0.0092 408 LEU B CA 1947 C C . LEU B 25 ? 0.7582 0.5731 0.6093 0.0151 -0.0431 0.0060 408 LEU B C 1948 O O . LEU B 25 ? 0.7443 0.5746 0.6068 0.0134 -0.0341 0.0030 408 LEU B O 1949 C CB . LEU B 25 ? 0.7459 0.5877 0.6290 0.0215 -0.0592 0.0101 408 LEU B CB 1950 C CG . LEU B 25 ? 0.7544 0.6076 0.6541 0.0236 -0.0695 0.0136 408 LEU B CG 1951 C CD1 . LEU B 25 ? 0.7395 0.6135 0.6626 0.0278 -0.0701 0.0141 408 LEU B CD1 1952 C CD2 . LEU B 25 ? 0.7867 0.6184 0.6728 0.0246 -0.0825 0.0156 408 LEU B CD2 1953 N N . ILE B 26 ? 0.7767 0.5679 0.6080 0.0154 -0.0436 0.0067 409 ILE B N 1954 C CA . ILE B 26 ? 0.7997 0.5841 0.6267 0.0137 -0.0331 0.0041 409 ILE B CA 1955 C C . ILE B 26 ? 0.7903 0.5748 0.6242 0.0177 -0.0382 0.0042 409 ILE B C 1956 O O . ILE B 26 ? 0.7968 0.5688 0.6224 0.0210 -0.0486 0.0077 409 ILE B O 1957 C CB . ILE B 26 ? 0.8536 0.6092 0.6530 0.0107 -0.0266 0.0053 409 ILE B CB 1958 C CG1 . ILE B 26 ? 0.8988 0.6556 0.6939 0.0067 -0.0188 0.0038 409 ILE B CG1 1959 C CG2 . ILE B 26 ? 0.8659 0.6136 0.6644 0.0091 -0.0165 0.0035 409 ILE B CG2 1960 C CD1 . ILE B 26 ? 0.9576 0.6856 0.7228 0.0046 -0.0132 0.0056 409 ILE B CD1 1961 N N . ILE B 27 ? 0.7734 0.5708 0.6220 0.0177 -0.0312 0.0000 410 ILE B N 1962 C CA . ILE B 27 ? 0.7883 0.5900 0.6478 0.0219 -0.0352 -0.0013 410 ILE B CA 1963 C C . ILE B 27 ? 0.8020 0.5918 0.6578 0.0200 -0.0266 -0.0045 410 ILE B C 1964 O O . ILE B 27 ? 0.7956 0.5927 0.6576 0.0164 -0.0169 -0.0089 410 ILE B O 1965 C CB . ILE B 27 ? 0.7755 0.6073 0.6597 0.0249 -0.0361 -0.0044 410 ILE B CB 1966 C CG1 . ILE B 27 ? 0.7813 0.6232 0.6717 0.0268 -0.0446 -0.0001 410 ILE B CG1 1967 C CG2 . ILE B 27 ? 0.7865 0.6231 0.6823 0.0297 -0.0386 -0.0071 410 ILE B CG2 1968 C CD1 . ILE B 27 ? 0.7801 0.6509 0.6924 0.0293 -0.0432 -0.0015 410 ILE B CD1 1969 N N . ARG B 28 ? 0.8134 0.5848 0.6606 0.0224 -0.0308 -0.0021 411 ARG B N 1970 C CA . ARG B 28 ? 0.8248 0.5839 0.6711 0.0210 -0.0236 -0.0046 411 ARG B CA 1971 C C . ARG B 28 ? 0.8118 0.5761 0.6718 0.0264 -0.0299 -0.0067 411 ARG B C 1972 O O . ARG B 28 ? 0.8104 0.5811 0.6754 0.0313 -0.0403 -0.0045 411 ARG B O 1973 C CB . ARG B 28 ? 0.8617 0.5884 0.6813 0.0185 -0.0205 0.0011 411 ARG B CB 1974 C CG . ARG B 28 ? 0.8928 0.6129 0.6983 0.0132 -0.0120 0.0023 411 ARG B CG 1975 C CD . ARG B 28 ? 0.9430 0.6305 0.7212 0.0109 -0.0058 0.0078 411 ARG B CD 1976 N NE . ARG B 28 ? 0.9815 0.6618 0.7445 0.0067 0.0024 0.0089 411 ARG B NE 1977 C CZ . ARG B 28 ? 1.0127 0.6883 0.7596 0.0079 -0.0040 0.0118 411 ARG B CZ 1978 N NH1 . ARG B 28 ? 1.0476 0.7257 0.7930 0.0128 -0.0196 0.0140 411 ARG B NH1 1979 N NH2 . ARG B 28 ? 1.0174 0.6859 0.7513 0.0041 0.0050 0.0119 411 ARG B NH2 1980 N N . ALA B 29 ? 0.7944 0.5564 0.6627 0.0256 -0.0235 -0.0116 412 ALA B N 1981 C CA . ALA B 29 ? 0.7876 0.5531 0.6696 0.0309 -0.0284 -0.0149 412 ALA B CA 1982 C C . ALA B 29 ? 0.8062 0.5432 0.6775 0.0305 -0.0270 -0.0120 412 ALA B C 1983 O O . ALA B 29 ? 0.8063 0.5399 0.6854 0.0279 -0.0193 -0.0169 412 ALA B O 1984 C CB . ALA B 29 ? 0.7618 0.5514 0.6656 0.0315 -0.0236 -0.0246 412 ALA B CB 1985 N N . PRO B 30 ? 0.8244 0.5405 0.6784 0.0332 -0.0351 -0.0040 413 PRO B N 1986 C CA . PRO B 30 ? 0.8619 0.5470 0.7001 0.0325 -0.0332 0.0009 413 PRO B CA 1987 C C . PRO B 30 ? 0.8753 0.5571 0.7288 0.0359 -0.0342 -0.0028 413 PRO B C 1988 O O . PRO B 30 ? 0.9225 0.5817 0.7683 0.0336 -0.0283 -0.0002 413 PRO B O 1989 C CB . PRO B 30 ? 0.8769 0.5443 0.6935 0.0362 -0.0449 0.0098 413 PRO B CB 1990 C CG . PRO B 30 ? 0.8492 0.5412 0.6825 0.0410 -0.0556 0.0073 413 PRO B CG 1991 C CD . PRO B 30 ? 0.8205 0.5405 0.6705 0.0376 -0.0475 0.0005 413 PRO B CD 1992 N N . LEU B 31 ? 0.8689 0.5725 0.7442 0.0413 -0.0405 -0.0088 414 LEU B N 1993 C CA . LEU B 31 ? 0.8746 0.5771 0.7664 0.0454 -0.0419 -0.0139 414 LEU B CA 1994 C C . LEU B 31 ? 0.8616 0.5831 0.7741 0.0434 -0.0336 -0.0254 414 LEU B C 1995 O O . LEU B 31 ? 0.8716 0.5990 0.8009 0.0479 -0.0356 -0.0321 414 LEU B O 1996 C CB . LEU B 31 ? 0.8629 0.5759 0.7662 0.0538 -0.0542 -0.0140 414 LEU B CB 1997 C CG . LEU B 31 ? 0.8964 0.5933 0.7828 0.0568 -0.0656 -0.0040 414 LEU B CG 1998 C CD1 . LEU B 31 ? 0.8942 0.6079 0.7987 0.0646 -0.0770 -0.0053 414 LEU B CD1 1999 C CD2 . LEU B 31 ? 0.9392 0.6014 0.8072 0.0569 -0.0672 0.0030 414 LEU B CD2 2000 N N . THR B 32 ? 0.8530 0.5837 0.7646 0.0373 -0.0248 -0.0281 415 THR B N 2001 C CA . THR B 32 ? 0.8508 0.6011 0.7815 0.0357 -0.0187 -0.0395 415 THR B CA 2002 C C . THR B 32 ? 0.8873 0.6237 0.8162 0.0279 -0.0079 -0.0405 415 THR B C 2003 O O . THR B 32 ? 0.9074 0.6296 0.8195 0.0228 -0.0028 -0.0330 415 THR B O 2004 C CB . THR B 32 ? 0.8275 0.6062 0.7635 0.0362 -0.0190 -0.0428 415 THR B CB 2005 O OG1 . THR B 32 ? 0.8227 0.6119 0.7590 0.0423 -0.0278 -0.0391 415 THR B OG1 2006 C CG2 . THR B 32 ? 0.8149 0.6147 0.7697 0.0371 -0.0158 -0.0550 415 THR B CG2 2007 N N . ASP B 33 ? 0.9216 0.6617 0.8686 0.0272 -0.0044 -0.0502 416 ASP B N 2008 C CA . ASP B 33 ? 0.9728 0.7016 0.9244 0.0196 0.0059 -0.0524 416 ASP B CA 2009 C C . ASP B 33 ? 0.9565 0.7086 0.9196 0.0164 0.0099 -0.0605 416 ASP B C 2010 O O . ASP B 33 ? 0.9469 0.7235 0.9162 0.0209 0.0044 -0.0660 416 ASP B O 2011 C CB . ASP B 33 ? 1.0125 0.7311 0.9805 0.0202 0.0067 -0.0591 416 ASP B CB 2012 C CG . ASP B 33 ? 1.0615 0.7535 1.0186 0.0232 0.0033 -0.0504 416 ASP B CG 2013 O OD1 . ASP B 33 ? 1.0864 0.7590 1.0212 0.0216 0.0045 -0.0381 416 ASP B OD1 2014 O OD2 . ASP B 33 ? 1.0991 0.7889 1.0698 0.0276 -0.0010 -0.0562 416 ASP B OD2 2015 N N . LYS B 34 ? 0.9818 0.7261 0.9484 0.0088 0.0198 -0.0610 417 LYS B N 2016 C CA . LYS B 34 ? 0.9817 0.7468 0.9641 0.0057 0.0232 -0.0704 417 LYS B CA 2017 C C . LYS B 34 ? 0.9569 0.7354 0.9617 0.0091 0.0185 -0.0842 417 LYS B C 2018 O O . LYS B 34 ? 0.9525 0.7225 0.9611 0.0130 0.0144 -0.0862 417 LYS B O 2019 C CB . LYS B 34 ? 1.0143 0.7670 0.9987 -0.0031 0.0354 -0.0679 417 LYS B CB 2020 C CG . LYS B 34 ? 1.0817 0.8142 1.0784 -0.0076 0.0425 -0.0697 417 LYS B CG 2021 C CD . LYS B 34 ? 1.1262 0.8507 1.1295 -0.0165 0.0560 -0.0682 417 LYS B CD 2022 C CE . LYS B 34 ? 1.1577 0.8665 1.1340 -0.0191 0.0632 -0.0548 417 LYS B CE 2023 N NZ . LYS B 34 ? 1.1787 0.8715 1.1595 -0.0274 0.0791 -0.0514 417 LYS B NZ 2024 N N . HIS B 35 ? 0.9420 0.7414 0.9611 0.0081 0.0184 -0.0941 418 HIS B N 2025 C CA . HIS B 35 ? 0.9346 0.7459 0.9738 0.0113 0.0136 -0.1087 418 HIS B CA 2026 C C . HIS B 35 ? 0.9133 0.7395 0.9689 0.0073 0.0155 -0.1182 418 HIS B C 2027 O O . HIS B 35 ? 0.9144 0.7471 0.9655 0.0037 0.0194 -0.1138 418 HIS B O 2028 C CB . HIS B 35 ? 0.9306 0.7592 0.9660 0.0209 0.0041 -0.1129 418 HIS B CB 2029 C CG . HIS B 35 ? 0.9411 0.7933 0.9697 0.0240 0.0013 -0.1124 418 HIS B CG 2030 N ND1 . HIS B 35 ? 0.9539 0.8060 0.9671 0.0220 0.0035 -0.1006 418 HIS B ND1 2031 C CD2 . HIS B 35 ? 0.9231 0.7986 0.9571 0.0293 -0.0037 -0.1220 418 HIS B CD2 2032 C CE1 . HIS B 35 ? 0.9170 0.7916 0.9286 0.0256 0.0002 -0.1025 418 HIS B CE1 2033 N NE2 . HIS B 35 ? 0.9114 0.8002 0.9342 0.0302 -0.0039 -0.1149 418 HIS B NE2 2034 N N . ILE B 36 ? 0.9187 0.7496 0.9944 0.0083 0.0120 -0.1319 419 ILE B N 2035 C CA . ILE B 36 ? 0.9059 0.7487 1.0017 0.0045 0.0123 -0.1428 419 ILE B CA 2036 C C . ILE B 36 ? 0.8765 0.7457 0.9725 0.0121 0.0023 -0.1531 419 ILE B C 2037 O O . ILE B 36 ? 0.8735 0.7486 0.9638 0.0201 -0.0043 -0.1577 419 ILE B O 2038 C CB . ILE B 36 ? 0.9246 0.7543 1.0446 0.0002 0.0141 -0.1523 419 ILE B CB 2039 C CG1 . ILE B 36 ? 0.9447 0.7459 1.0622 -0.0067 0.0251 -0.1405 419 ILE B CG1 2040 C CG2 . ILE B 36 ? 0.9302 0.7723 1.0745 -0.0040 0.0134 -0.1642 419 ILE B CG2 2041 C CD1 . ILE B 36 ? 0.9498 0.7446 1.0608 -0.0142 0.0362 -0.1295 419 ILE B CD1 2042 N N . TYR B 37 ? 0.8678 0.7520 0.9694 0.0100 0.0020 -0.1561 420 TYR B N 2043 C CA . TYR B 37 ? 0.8652 0.7732 0.9689 0.0166 -0.0073 -0.1669 420 TYR B CA 2044 C C . TYR B 37 ? 0.8886 0.8007 1.0181 0.0123 -0.0094 -0.1800 420 TYR B C 2045 O O . TYR B 37 ? 0.8592 0.7660 1.0004 0.0043 -0.0024 -0.1765 420 TYR B O 2046 C CB . TYR B 37 ? 0.8399 0.7624 0.9274 0.0187 -0.0073 -0.1580 420 TYR B CB 2047 C CG . TYR B 37 ? 0.8300 0.7744 0.9229 0.0224 -0.0146 -0.1673 420 TYR B CG 2048 C CD1 . TYR B 37 ? 0.8266 0.7860 0.9132 0.0320 -0.0238 -0.1764 420 TYR B CD1 2049 C CD2 . TYR B 37 ? 0.8193 0.7691 0.9228 0.0169 -0.0124 -0.1670 420 TYR B CD2 2050 C CE1 . TYR B 37 ? 0.8180 0.7962 0.9064 0.0362 -0.0312 -0.1843 420 TYR B CE1 2051 C CE2 . TYR B 37 ? 0.8179 0.7872 0.9262 0.0209 -0.0203 -0.1751 420 TYR B CE2 2052 C CZ . TYR B 37 ? 0.8249 0.8078 0.9244 0.0306 -0.0301 -0.1835 420 TYR B CZ 2053 O OH . TYR B 37 ? 0.8681 0.8689 0.9695 0.0352 -0.0386 -0.1909 420 TYR B OH 2054 N N . GLN B 38 ? 0.9430 0.8644 1.0818 0.0181 -0.0191 -0.1955 421 GLN B N 2055 C CA . GLN B 38 ? 0.9760 0.9017 1.1417 0.0150 -0.0240 -0.2104 421 GLN B CA 2056 C C . GLN B 38 ? 0.9770 0.9263 1.1389 0.0216 -0.0344 -0.2188 421 GLN B C 2057 O O . GLN B 38 ? 0.9945 0.9540 1.1429 0.0312 -0.0428 -0.2256 421 GLN B O 2058 C CB . GLN B 38 ? 1.0065 0.9224 1.1862 0.0167 -0.0285 -0.2231 421 GLN B CB 2059 C CG . GLN B 38 ? 1.0387 0.9297 1.2223 0.0104 -0.0184 -0.2141 421 GLN B CG 2060 C CD . GLN B 38 ? 1.0918 0.9719 1.2910 0.0120 -0.0229 -0.2264 421 GLN B CD 2061 O OE1 . GLN B 38 ? 1.1112 0.9983 1.3022 0.0212 -0.0315 -0.2354 421 GLN B OE1 2062 N NE2 . GLN B 38 ? 1.1190 0.9811 1.3413 0.0032 -0.0161 -0.2266 421 GLN B NE2 2063 N N . PRO B 39 ? 0.9873 0.9448 1.1601 0.0170 -0.0336 -0.2180 422 PRO B N 2064 C CA . PRO B 39 ? 1.0135 0.9925 1.1808 0.0238 -0.0441 -0.2245 422 PRO B CA 2065 C C . PRO B 39 ? 1.0809 1.0677 1.2633 0.0286 -0.0576 -0.2448 422 PRO B C 2066 O O . PRO B 39 ? 1.0894 1.0670 1.2982 0.0233 -0.0583 -0.2548 422 PRO B O 2067 C CB . PRO B 39 ? 0.9812 0.9644 1.1598 0.0169 -0.0391 -0.2180 422 PRO B CB 2068 C CG . PRO B 39 ? 0.9761 0.9406 1.1736 0.0060 -0.0270 -0.2134 422 PRO B CG 2069 C CD . PRO B 39 ? 0.9874 0.9346 1.1776 0.0060 -0.0228 -0.2111 422 PRO B CD 2070 N N . TYR B 40 ? 1.1556 1.1587 1.3203 0.0389 -0.0681 -0.2504 423 TYR B N 2071 C CA . TYR B 40 ? 1.2319 1.2437 1.4033 0.0459 -0.0827 -0.2699 423 TYR B CA 2072 C C . TYR B 40 ? 1.2378 1.2643 1.4204 0.0460 -0.0915 -0.2754 423 TYR B C 2073 O O . TYR B 40 ? 1.1920 1.2269 1.3622 0.0464 -0.0884 -0.2635 423 TYR B O 2074 C CB . TYR B 40 ? 1.2838 1.3033 1.4242 0.0584 -0.0877 -0.2718 423 TYR B CB 2075 C CG . TYR B 40 ? 1.3598 1.3873 1.4996 0.0677 -0.1029 -0.2921 423 TYR B CG 2076 C CD1 . TYR B 40 ? 1.3829 1.4011 1.5282 0.0707 -0.1064 -0.3053 423 TYR B CD1 2077 C CD2 . TYR B 40 ? 1.3778 1.4213 1.5103 0.0742 -0.1145 -0.2986 423 TYR B CD2 2078 C CE1 . TYR B 40 ? 1.4222 1.4469 1.5652 0.0798 -0.1210 -0.3251 423 TYR B CE1 2079 C CE2 . TYR B 40 ? 1.4253 1.4750 1.5540 0.0835 -0.1296 -0.3177 423 TYR B CE2 2080 C CZ . TYR B 40 ? 1.4513 1.4916 1.5849 0.0863 -0.1327 -0.3314 423 TYR B CZ 2081 O OH . TYR B 40 ? 1.5163 1.5620 1.6445 0.0961 -0.1482 -0.3514 423 TYR B OH 2082 N N . PRO B 41 ? 1.3106 1.3400 1.5176 0.0459 -0.1033 -0.2934 424 PRO B N 2083 C CA . PRO B 41 ? 1.3311 1.3501 1.5571 0.0450 -0.1080 -0.3091 424 PRO B CA 2084 C C . PRO B 41 ? 1.3212 1.3235 1.5792 0.0318 -0.0966 -0.3059 424 PRO B C 2085 O O . PRO B 41 ? 1.3518 1.3401 1.6183 0.0300 -0.0942 -0.3109 424 PRO B O 2086 C CB . PRO B 41 ? 1.3628 1.3941 1.6027 0.0503 -0.1267 -0.3291 424 PRO B CB 2087 C CG . PRO B 41 ? 1.3540 1.3973 1.6001 0.0477 -0.1277 -0.3223 424 PRO B CG 2088 C CD . PRO B 41 ? 1.3328 1.3773 1.5502 0.0479 -0.1148 -0.3006 424 PRO B CD 2089 N N . SER B 42 ? 1.2872 1.2907 1.5628 0.0232 -0.0895 -0.2978 425 SER B N 2090 C CA . SER B 42 ? 1.2704 1.2583 1.5748 0.0106 -0.0763 -0.2928 425 SER B CA 2091 C C . SER B 42 ? 1.2211 1.2074 1.5160 0.0048 -0.0617 -0.2730 425 SER B C 2092 O O . SER B 42 ? 1.2301 1.2290 1.5032 0.0099 -0.0639 -0.2659 425 SER B O 2093 C CB . SER B 42 ? 1.2834 1.2754 1.6306 0.0054 -0.0842 -0.3086 425 SER B CB 2094 O OG . SER B 42 ? 1.2867 1.2657 1.6630 -0.0072 -0.0693 -0.3019 425 SER B OG 2095 N N . GLY B 43 ? 1.1624 1.1321 1.4734 -0.0056 -0.0465 -0.2645 426 GLY B N 2096 C CA . GLY B 43 ? 1.1068 1.0716 1.4099 -0.0118 -0.0314 -0.2468 426 GLY B CA 2097 C C . GLY B 43 ? 1.0752 1.0167 1.3711 -0.0180 -0.0157 -0.2343 426 GLY B C 2098 O O . GLY B 43 ? 1.0716 1.0028 1.3583 -0.0152 -0.0174 -0.2361 426 GLY B O 2099 N N . ALA B 44 ? 1.0336 0.9663 1.3325 -0.0260 -0.0005 -0.2215 427 ALA B N 2100 C CA . ALA B 44 ? 1.0251 0.9341 1.3141 -0.0319 0.0151 -0.2079 427 ALA B CA 2101 C C . ALA B 44 ? 1.0120 0.9161 1.2612 -0.0252 0.0142 -0.1971 427 ALA B C 2102 O O . ALA B 44 ? 1.0061 0.9250 1.2339 -0.0184 0.0075 -0.1944 427 ALA B O 2103 C CB . ALA B 44 ? 1.0172 0.9194 1.3128 -0.0403 0.0312 -0.1966 427 ALA B CB 2104 N N . ASP B 45 ? 1.0022 0.8855 1.2435 -0.0271 0.0210 -0.1908 428 ASP B N 2105 C CA . ASP B 45 ? 0.9947 0.8713 1.2017 -0.0214 0.0207 -0.1801 428 ASP B CA 2106 C C . ASP B 45 ? 0.9691 0.8447 1.1523 -0.0225 0.0287 -0.1644 428 ASP B C 2107 O O . ASP B 45 ? 0.9625 0.8310 1.1531 -0.0298 0.0401 -0.1581 428 ASP B O 2108 C CB . ASP B 45 ? 1.0322 0.8841 1.2377 -0.0239 0.0270 -0.1754 428 ASP B CB 2109 C CG . ASP B 45 ? 1.0748 0.9264 1.2995 -0.0211 0.0178 -0.1906 428 ASP B CG 2110 O OD1 . ASP B 45 ? 1.0988 0.9697 1.3322 -0.0156 0.0052 -0.2050 428 ASP B OD1 2111 O OD2 . ASP B 45 ? 1.1008 0.9317 1.3311 -0.0242 0.0231 -0.1883 428 ASP B OD2 2112 N N . VAL B 46 ? 0.9186 0.8012 1.0744 -0.0151 0.0228 -0.1586 429 VAL B N 2113 C CA . VAL B 46 ? 0.8749 0.7560 1.0068 -0.0153 0.0284 -0.1442 429 VAL B CA 2114 C C . VAL B 46 ? 0.8511 0.7174 0.9585 -0.0121 0.0292 -0.1341 429 VAL B C 2115 O O . VAL B 46 ? 0.8498 0.7243 0.9475 -0.0045 0.0201 -0.1369 429 VAL B O 2116 C CB . VAL B 46 ? 0.8473 0.7521 0.9710 -0.0095 0.0201 -0.1457 429 VAL B CB 2117 C CG1 . VAL B 46 ? 0.8282 0.7304 0.9316 -0.0109 0.0264 -0.1316 429 VAL B CG1 2118 C CG2 . VAL B 46 ? 0.8376 0.7582 0.9868 -0.0109 0.0158 -0.1577 429 VAL B CG2 2119 N N . PRO B 47 ? 0.8251 0.6690 0.9226 -0.0175 0.0401 -0.1225 430 PRO B N 2120 C CA . PRO B 47 ? 0.8358 0.6655 0.9088 -0.0141 0.0394 -0.1122 430 PRO B CA 2121 C C . PRO B 47 ? 0.8419 0.6809 0.8920 -0.0101 0.0362 -0.1035 430 PRO B C 2122 O O . PRO B 47 ? 0.8293 0.6744 0.8774 -0.0130 0.0404 -0.1001 430 PRO B O 2123 C CB . PRO B 47 ? 0.8435 0.6455 0.9128 -0.0212 0.0522 -0.1029 430 PRO B CB 2124 C CG . PRO B 47 ? 0.8333 0.6380 0.9184 -0.0284 0.0617 -0.1046 430 PRO B CG 2125 C CD . PRO B 47 ? 0.8149 0.6458 0.9218 -0.0264 0.0535 -0.1181 430 PRO B CD 2126 N N . PHE B 48 ? 0.8243 0.6645 0.8596 -0.0034 0.0288 -0.1002 431 PHE B N 2127 C CA . PHE B 48 ? 0.8033 0.6513 0.8193 0.0005 0.0252 -0.0918 431 PHE B CA 2128 C C . PHE B 48 ? 0.8133 0.6399 0.8096 0.0009 0.0264 -0.0804 431 PHE B C 2129 O O . PHE B 48 ? 0.8178 0.6337 0.8145 0.0034 0.0238 -0.0812 431 PHE B O 2130 C CB . PHE B 48 ? 0.7837 0.6544 0.8014 0.0086 0.0151 -0.0981 431 PHE B CB 2131 C CG . PHE B 48 ? 0.7664 0.6593 0.7936 0.0093 0.0128 -0.1048 431 PHE B CG 2132 C CD1 . PHE B 48 ? 0.7648 0.6633 0.8121 0.0071 0.0126 -0.1164 431 PHE B CD1 2133 C CD2 . PHE B 48 ? 0.7587 0.6660 0.7758 0.0122 0.0102 -0.0993 431 PHE B CD2 2134 C CE1 . PHE B 48 ? 0.7566 0.6750 0.8124 0.0083 0.0090 -0.1227 431 PHE B CE1 2135 C CE2 . PHE B 48 ? 0.7443 0.6710 0.7694 0.0133 0.0076 -0.1047 431 PHE B CE2 2136 C CZ . PHE B 48 ? 0.7418 0.6740 0.7855 0.0116 0.0066 -0.1165 431 PHE B CZ 2137 N N . GLY B 49 ? 0.8100 0.6304 0.7890 -0.0009 0.0293 -0.0703 432 GLY B N 2138 C CA . GLY B 49 ? 0.8027 0.6012 0.7606 -0.0004 0.0296 -0.0593 432 GLY B CA 2139 C C . GLY B 49 ? 0.7915 0.5956 0.7425 0.0070 0.0189 -0.0571 432 GLY B C 2140 O O . GLY B 49 ? 0.7724 0.5991 0.7326 0.0118 0.0128 -0.0628 432 GLY B O 2141 N N . PRO B 50 ? 0.8086 0.5922 0.7435 0.0084 0.0167 -0.0485 433 PRO B N 2142 C CA . PRO B 50 ? 0.8066 0.5937 0.7378 0.0156 0.0065 -0.0462 433 PRO B CA 2143 C C . PRO B 50 ? 0.7847 0.5959 0.7176 0.0200 0.0000 -0.0462 433 PRO B C 2144 O O . PRO B 50 ? 0.7744 0.6009 0.7177 0.0259 -0.0055 -0.0509 433 PRO B O 2145 C CB . PRO B 50 ? 0.8327 0.5928 0.7423 0.0151 0.0054 -0.0351 433 PRO B CB 2146 C CG . PRO B 50 ? 0.8434 0.5823 0.7487 0.0085 0.0163 -0.0335 433 PRO B CG 2147 C CD . PRO B 50 ? 0.8339 0.5888 0.7525 0.0036 0.0240 -0.0401 433 PRO B CD 2148 N N . PRO B 51 ? 0.7797 0.5945 0.7034 0.0172 0.0016 -0.0412 434 PRO B N 2149 C CA . PRO B 51 ? 0.7557 0.5922 0.6824 0.0213 -0.0042 -0.0401 434 PRO B CA 2150 C C . PRO B 51 ? 0.7400 0.6030 0.6827 0.0234 -0.0036 -0.0485 434 PRO B C 2151 O O . PRO B 51 ? 0.7314 0.6124 0.6769 0.0274 -0.0076 -0.0472 434 PRO B O 2152 C CB . PRO B 51 ? 0.7606 0.5911 0.6734 0.0175 -0.0025 -0.0330 434 PRO B CB 2153 C CG . PRO B 51 ? 0.7836 0.5947 0.6886 0.0111 0.0065 -0.0324 434 PRO B CG 2154 C CD . PRO B 51 ? 0.7883 0.5903 0.7016 0.0105 0.0098 -0.0374 434 PRO B CD 2155 N N . LEU B 52 ? 0.7363 0.6013 0.6892 0.0209 0.0011 -0.0568 435 LEU B N 2156 C CA . LEU B 52 ? 0.7314 0.6196 0.6976 0.0236 0.0002 -0.0657 435 LEU B CA 2157 C C . LEU B 52 ? 0.7504 0.6440 0.7265 0.0290 -0.0031 -0.0745 435 LEU B C 2158 O O . LEU B 52 ? 0.7445 0.6540 0.7304 0.0315 -0.0040 -0.0837 435 LEU B O 2159 C CB . LEU B 52 ? 0.7236 0.6133 0.6969 0.0178 0.0061 -0.0705 435 LEU B CB 2160 C CG . LEU B 52 ? 0.7194 0.6044 0.6838 0.0128 0.0104 -0.0629 435 LEU B CG 2161 C CD1 . LEU B 52 ? 0.7225 0.6060 0.6970 0.0068 0.0175 -0.0680 435 LEU B CD1 2162 C CD2 . LEU B 52 ? 0.7142 0.6179 0.6760 0.0162 0.0063 -0.0592 435 LEU B CD2 2163 N N . ASP B 53 ? 0.7922 0.6722 0.7654 0.0315 -0.0056 -0.0719 436 ASP B N 2164 C CA . ASP B 53 ? 0.8086 0.6949 0.7903 0.0383 -0.0096 -0.0791 436 ASP B CA 2165 C C . ASP B 53 ? 0.7964 0.7065 0.7791 0.0450 -0.0129 -0.0793 436 ASP B C 2166 O O . ASP B 53 ? 0.8017 0.7159 0.7779 0.0453 -0.0142 -0.0703 436 ASP B O 2167 C CB . ASP B 53 ? 0.8522 0.7188 0.8299 0.0399 -0.0122 -0.0742 436 ASP B CB 2168 C CG . ASP B 53 ? 0.8869 0.7611 0.8736 0.0480 -0.0167 -0.0803 436 ASP B CG 2169 O OD1 . ASP B 53 ? 0.9349 0.8076 0.9315 0.0492 -0.0162 -0.0905 436 ASP B OD1 2170 O OD2 . ASP B 53 ? 0.9075 0.7891 0.8927 0.0533 -0.0206 -0.0754 436 ASP B OD2 2171 N N . ILE B 54 ? 0.8117 0.7368 0.8025 0.0504 -0.0141 -0.0897 437 ILE B N 2172 C CA . ILE B 54 ? 0.8109 0.7589 0.8016 0.0573 -0.0154 -0.0904 437 ILE B CA 2173 C C . ILE B 54 ? 0.8197 0.7697 0.8087 0.0618 -0.0173 -0.0818 437 ILE B C 2174 O O . ILE B 54 ? 0.7988 0.7628 0.7856 0.0636 -0.0169 -0.0756 437 ILE B O 2175 C CB . ILE B 54 ? 0.8166 0.7767 0.8135 0.0638 -0.0165 -0.1041 437 ILE B CB 2176 C CG1 . ILE B 54 ? 0.8077 0.7911 0.8010 0.0709 -0.0163 -0.1044 437 ILE B CG1 2177 C CG2 . ILE B 54 ? 0.8233 0.7740 0.8261 0.0683 -0.0183 -0.1094 437 ILE B CG2 2178 C CD1 . ILE B 54 ? 0.8101 0.8045 0.7985 0.0680 -0.0152 -0.1006 437 ILE B CD1 2179 N N . GLN B 55 ? 0.8502 0.7860 0.8419 0.0634 -0.0196 -0.0811 438 GLN B N 2180 C CA . GLN B 55 ? 0.8714 0.8092 0.8653 0.0682 -0.0226 -0.0741 438 GLN B CA 2181 C C . GLN B 55 ? 0.8214 0.7511 0.8082 0.0635 -0.0248 -0.0617 438 GLN B C 2182 O O . GLN B 55 ? 0.8167 0.7567 0.8065 0.0664 -0.0266 -0.0553 438 GLN B O 2183 C CB . GLN B 55 ? 0.9225 0.8474 0.9229 0.0721 -0.0256 -0.0777 438 GLN B CB 2184 C CG . GLN B 55 ? 0.9619 0.8980 0.9708 0.0792 -0.0242 -0.0901 438 GLN B CG 2185 C CD . GLN B 55 ? 1.0060 0.9668 1.0176 0.0863 -0.0219 -0.0908 438 GLN B CD 2186 O OE1 . GLN B 55 ? 1.0385 1.0058 1.0529 0.0885 -0.0225 -0.0821 438 GLN B OE1 2187 N NE2 . GLN B 55 ? 1.0265 1.0009 1.0372 0.0899 -0.0191 -0.1010 438 GLN B NE2 2188 N N . ILE B 56 ? 0.7864 0.6977 0.7644 0.0564 -0.0242 -0.0586 439 ILE B N 2189 C CA . ILE B 56 ? 0.7657 0.6680 0.7339 0.0520 -0.0262 -0.0482 439 ILE B CA 2190 C C . ILE B 56 ? 0.7268 0.6470 0.6946 0.0506 -0.0240 -0.0454 439 ILE B C 2191 O O . ILE B 56 ? 0.7062 0.6290 0.6726 0.0506 -0.0270 -0.0376 439 ILE B O 2192 C CB . ILE B 56 ? 0.7655 0.6440 0.7224 0.0449 -0.0238 -0.0464 439 ILE B CB 2193 C CG1 . ILE B 56 ? 0.7846 0.6423 0.7405 0.0464 -0.0265 -0.0467 439 ILE B CG1 2194 C CG2 . ILE B 56 ? 0.7629 0.6327 0.7070 0.0402 -0.0246 -0.0373 439 ILE B CG2 2195 C CD1 . ILE B 56 ? 0.7967 0.6412 0.7463 0.0490 -0.0341 -0.0380 439 ILE B CD1 2196 N N . LEU B 57 ? 0.7106 0.6426 0.6806 0.0496 -0.0194 -0.0518 440 LEU B N 2197 C CA . LEU B 57 ? 0.7090 0.6586 0.6791 0.0492 -0.0175 -0.0491 440 LEU B CA 2198 C C . LEU B 57 ? 0.7063 0.6745 0.6832 0.0557 -0.0187 -0.0460 440 LEU B C 2199 O O . LEU B 57 ? 0.7021 0.6776 0.6790 0.0548 -0.0191 -0.0384 440 LEU B O 2200 C CB . LEU B 57 ? 0.7072 0.6662 0.6791 0.0481 -0.0138 -0.0573 440 LEU B CB 2201 C CG . LEU B 57 ? 0.7219 0.6665 0.6903 0.0406 -0.0109 -0.0591 440 LEU B CG 2202 C CD1 . LEU B 57 ? 0.7257 0.6812 0.7004 0.0406 -0.0090 -0.0689 440 LEU B CD1 2203 C CD2 . LEU B 57 ? 0.7248 0.6643 0.6859 0.0353 -0.0098 -0.0504 440 LEU B CD2 2204 N N . HIS B 58 ? 0.6997 0.6748 0.6834 0.0623 -0.0188 -0.0517 441 HIS B N 2205 C CA . HIS B 58 ? 0.6885 0.6801 0.6803 0.0691 -0.0184 -0.0486 441 HIS B CA 2206 C C . HIS B 58 ? 0.6787 0.6634 0.6746 0.0681 -0.0230 -0.0388 441 HIS B C 2207 O O . HIS B 58 ? 0.6898 0.6871 0.6920 0.0696 -0.0225 -0.0321 441 HIS B O 2208 C CB . HIS B 58 ? 0.6969 0.6938 0.6951 0.0766 -0.0173 -0.0572 441 HIS B CB 2209 C CG . HIS B 58 ? 0.6908 0.6999 0.6859 0.0801 -0.0136 -0.0671 441 HIS B CG 2210 N ND1 . HIS B 58 ? 0.6868 0.7151 0.6794 0.0837 -0.0098 -0.0658 441 HIS B ND1 2211 C CD2 . HIS B 58 ? 0.7027 0.7069 0.6967 0.0812 -0.0139 -0.0787 441 HIS B CD2 2212 C CE1 . HIS B 58 ? 0.6956 0.7302 0.6838 0.0871 -0.0086 -0.0764 441 HIS B CE1 2213 N NE2 . HIS B 58 ? 0.7015 0.7219 0.6915 0.0855 -0.0114 -0.0848 441 HIS B NE2 2214 N N . GLN B 59 ? 0.6794 0.6435 0.6722 0.0657 -0.0278 -0.0380 442 GLN B N 2215 C CA . GLN B 59 ? 0.6761 0.6308 0.6712 0.0651 -0.0344 -0.0298 442 GLN B CA 2216 C C . GLN B 59 ? 0.6779 0.6294 0.6660 0.0593 -0.0362 -0.0221 442 GLN B C 2217 O O . GLN B 59 ? 0.6629 0.6186 0.6580 0.0599 -0.0405 -0.0154 442 GLN B O 2218 C CB . GLN B 59 ? 0.6903 0.6215 0.6802 0.0646 -0.0396 -0.0308 442 GLN B CB 2219 C CG . GLN B 59 ? 0.6933 0.6272 0.6941 0.0714 -0.0399 -0.0370 442 GLN B CG 2220 C CD . GLN B 59 ? 0.7143 0.6241 0.7090 0.0705 -0.0436 -0.0388 442 GLN B CD 2221 O OE1 . GLN B 59 ? 0.7139 0.6047 0.6999 0.0677 -0.0495 -0.0322 442 GLN B OE1 2222 N NE2 . GLN B 59 ? 0.7402 0.6493 0.7387 0.0731 -0.0402 -0.0478 442 GLN B NE2 2223 N N . VAL B 60 ? 0.6728 0.6170 0.6489 0.0536 -0.0328 -0.0237 443 VAL B N 2224 C CA . VAL B 60 ? 0.6655 0.6071 0.6346 0.0483 -0.0332 -0.0178 443 VAL B CA 2225 C C . VAL B 60 ? 0.6529 0.6176 0.6315 0.0500 -0.0302 -0.0149 443 VAL B C 2226 O O . VAL B 60 ? 0.6617 0.6278 0.6422 0.0480 -0.0330 -0.0082 443 VAL B O 2227 C CB . VAL B 60 ? 0.6656 0.5941 0.6215 0.0422 -0.0290 -0.0208 443 VAL B CB 2228 C CG1 . VAL B 60 ? 0.6589 0.5870 0.6089 0.0374 -0.0282 -0.0158 443 VAL B CG1 2229 C CG2 . VAL B 60 ? 0.6785 0.5813 0.6234 0.0401 -0.0316 -0.0207 443 VAL B CG2 2230 N N . LEU B 61 ? 0.6411 0.6231 0.6254 0.0542 -0.0249 -0.0199 444 LEU B N 2231 C CA . LEU B 61 ? 0.6379 0.6410 0.6297 0.0569 -0.0213 -0.0161 444 LEU B CA 2232 C C . LEU B 61 ? 0.6524 0.6636 0.6580 0.0604 -0.0236 -0.0095 444 LEU B C 2233 O O . LEU B 61 ? 0.6527 0.6742 0.6649 0.0597 -0.0227 -0.0026 444 LEU B O 2234 C CB . LEU B 61 ? 0.6428 0.6611 0.6346 0.0617 -0.0156 -0.0231 444 LEU B CB 2235 C CG . LEU B 61 ? 0.6433 0.6828 0.6396 0.0654 -0.0108 -0.0188 444 LEU B CG 2236 C CD1 . LEU B 61 ? 0.6463 0.6866 0.6399 0.0602 -0.0108 -0.0120 444 LEU B CD1 2237 C CD2 . LEU B 61 ? 0.6461 0.6971 0.6375 0.0708 -0.0064 -0.0270 444 LEU B CD2 2238 N N . ASP B 62 ? 0.6729 0.6797 0.6852 0.0643 -0.0267 -0.0116 445 ASP B N 2239 C CA . ASP B 62 ? 0.6677 0.6820 0.6968 0.0679 -0.0295 -0.0060 445 ASP B CA 2240 C C . ASP B 62 ? 0.6489 0.6523 0.6797 0.0630 -0.0375 0.0012 445 ASP B C 2241 O O . ASP B 62 ? 0.6300 0.6443 0.6753 0.0635 -0.0383 0.0077 445 ASP B O 2242 C CB . ASP B 62 ? 0.6950 0.7058 0.7317 0.0734 -0.0317 -0.0107 445 ASP B CB 2243 C CG . ASP B 62 ? 0.7164 0.7428 0.7566 0.0802 -0.0234 -0.0175 445 ASP B CG 2244 O OD1 . ASP B 62 ? 0.7262 0.7706 0.7687 0.0824 -0.0161 -0.0156 445 ASP B OD1 2245 O OD2 . ASP B 62 ? 0.7265 0.7461 0.7664 0.0837 -0.0243 -0.0246 445 ASP B OD2 2246 N N . LEU B 63 ? 0.6607 0.6422 0.6767 0.0586 -0.0433 0.0000 446 LEU B N 2247 C CA . LEU B 63 ? 0.6791 0.6470 0.6901 0.0538 -0.0511 0.0055 446 LEU B CA 2248 C C . LEU B 63 ? 0.6541 0.6325 0.6668 0.0502 -0.0477 0.0099 446 LEU B C 2249 O O . LEU B 63 ? 0.6325 0.6137 0.6557 0.0491 -0.0525 0.0157 446 LEU B O 2250 C CB . LEU B 63 ? 0.7028 0.6455 0.6921 0.0497 -0.0542 0.0029 446 LEU B CB 2251 C CG . LEU B 63 ? 0.7228 0.6480 0.6997 0.0448 -0.0611 0.0072 446 LEU B CG 2252 C CD1 . LEU B 63 ? 0.7331 0.6540 0.7199 0.0470 -0.0728 0.0116 446 LEU B CD1 2253 C CD2 . LEU B 63 ? 0.7457 0.6468 0.6994 0.0414 -0.0606 0.0046 446 LEU B CD2 2254 N N . GLN B 64 ? 0.6493 0.6332 0.6532 0.0486 -0.0398 0.0069 447 GLN B N 2255 C CA . GLN B 64 ? 0.6425 0.6352 0.6467 0.0455 -0.0362 0.0107 447 GLN B CA 2256 C C . GLN B 64 ? 0.6321 0.6459 0.6550 0.0487 -0.0333 0.0166 447 GLN B C 2257 O O . GLN B 64 ? 0.6135 0.6298 0.6437 0.0460 -0.0354 0.0228 447 GLN B O 2258 C CB . GLN B 64 ? 0.6546 0.6505 0.6480 0.0444 -0.0290 0.0054 447 GLN B CB 2259 C CG . GLN B 64 ? 0.6677 0.6661 0.6575 0.0403 -0.0266 0.0082 447 GLN B CG 2260 C CD . GLN B 64 ? 0.6858 0.6850 0.6663 0.0392 -0.0212 0.0018 447 GLN B CD 2261 O OE1 . GLN B 64 ? 0.7314 0.7149 0.7013 0.0357 -0.0214 -0.0027 447 GLN B OE1 2262 N NE2 . GLN B 64 ? 0.6812 0.6982 0.6657 0.0424 -0.0164 0.0015 447 GLN B NE2 2263 N N . ILE B 65 ? 0.6465 0.6748 0.6774 0.0546 -0.0279 0.0146 448 ILE B N 2264 C CA . ILE B 65 ? 0.6313 0.6798 0.6798 0.0586 -0.0228 0.0205 448 ILE B CA 2265 C C . ILE B 65 ? 0.6461 0.6932 0.7132 0.0581 -0.0295 0.0264 448 ILE B C 2266 O O . ILE B 65 ? 0.6564 0.7149 0.7388 0.0576 -0.0275 0.0337 448 ILE B O 2267 C CB . ILE B 65 ? 0.6326 0.6947 0.6834 0.0659 -0.0152 0.0160 448 ILE B CB 2268 C CG1 . ILE B 65 ? 0.6473 0.7143 0.6820 0.0668 -0.0091 0.0110 448 ILE B CG1 2269 C CG2 . ILE B 65 ? 0.6188 0.6998 0.6892 0.0706 -0.0091 0.0227 448 ILE B CG2 2270 C CD1 . ILE B 65 ? 0.6560 0.7300 0.6866 0.0736 -0.0042 0.0029 448 ILE B CD1 2271 N N . ALA B 66 ? 0.6434 0.6764 0.7104 0.0583 -0.0379 0.0233 449 ALA B N 2272 C CA . ALA B 66 ? 0.6545 0.6852 0.7400 0.0583 -0.0467 0.0278 449 ALA B CA 2273 C C . ALA B 66 ? 0.6769 0.6983 0.7613 0.0522 -0.0540 0.0324 449 ALA B C 2274 O O . ALA B 66 ? 0.6828 0.7119 0.7884 0.0517 -0.0572 0.0382 449 ALA B O 2275 C CB . ALA B 66 ? 0.6504 0.6662 0.7332 0.0606 -0.0552 0.0232 449 ALA B CB 2276 N N . ILE B 67 ? 0.6763 0.6816 0.7375 0.0478 -0.0560 0.0295 450 ILE B N 2277 C CA . ILE B 67 ? 0.6769 0.6728 0.7332 0.0422 -0.0613 0.0326 450 ILE B CA 2278 C C . ILE B 67 ? 0.6981 0.7116 0.7687 0.0410 -0.0547 0.0387 450 ILE B C 2279 O O . ILE B 67 ? 0.7134 0.7268 0.7975 0.0385 -0.0604 0.0434 450 ILE B O 2280 C CB . ILE B 67 ? 0.6748 0.6519 0.7032 0.0383 -0.0611 0.0279 450 ILE B CB 2281 C CG1 . ILE B 67 ? 0.6873 0.6425 0.7014 0.0387 -0.0696 0.0242 450 ILE B CG1 2282 C CG2 . ILE B 67 ? 0.6800 0.6506 0.7035 0.0331 -0.0635 0.0305 450 ILE B CG2 2283 C CD1 . ILE B 67 ? 0.6872 0.6259 0.6755 0.0360 -0.0657 0.0193 450 ILE B CD1 2284 N N . GLU B 68 ? 0.7180 0.7457 0.7857 0.0430 -0.0433 0.0386 451 GLU B N 2285 C CA . GLU B 68 ? 0.7426 0.7873 0.8226 0.0430 -0.0360 0.0455 451 GLU B CA 2286 C C . GLU B 68 ? 0.7465 0.8050 0.8548 0.0451 -0.0356 0.0525 451 GLU B C 2287 O O . GLU B 68 ? 0.7455 0.8116 0.8675 0.0430 -0.0336 0.0596 451 GLU B O 2288 C CB . GLU B 68 ? 0.7695 0.8276 0.8408 0.0467 -0.0247 0.0439 451 GLU B CB 2289 C CG . GLU B 68 ? 0.8097 0.8591 0.8590 0.0442 -0.0234 0.0384 451 GLU B CG 2290 C CD . GLU B 68 ? 0.8579 0.9217 0.9007 0.0484 -0.0141 0.0371 451 GLU B CD 2291 O OE1 . GLU B 68 ? 0.8836 0.9601 0.9327 0.0495 -0.0089 0.0438 451 GLU B OE1 2292 O OE2 . GLU B 68 ? 0.9004 0.9623 0.9319 0.0510 -0.0125 0.0292 451 GLU B OE2 2293 N N . ASN B 69 ? 0.7809 0.8427 0.8994 0.0494 -0.0369 0.0505 452 ASN B N 2294 C CA . ASN B 69 ? 0.7940 0.8700 0.9426 0.0520 -0.0354 0.0563 452 ASN B CA 2295 C C . ASN B 69 ? 0.7751 0.8415 0.9415 0.0490 -0.0493 0.0579 452 ASN B C 2296 O O . ASN B 69 ? 0.7767 0.8550 0.9725 0.0505 -0.0491 0.0628 452 ASN B O 2297 C CB . ASN B 69 ? 0.8255 0.9109 0.9785 0.0590 -0.0294 0.0527 452 ASN B CB 2298 C CG . ASN B 69 ? 0.8817 0.9885 1.0622 0.0630 -0.0196 0.0596 452 ASN B CG 2299 O OD1 . ASN B 69 ? 0.9251 1.0440 1.1090 0.0628 -0.0098 0.0663 452 ASN B OD1 2300 N ND2 . ASN B 69 ? 0.9163 1.0276 1.1170 0.0671 -0.0215 0.0583 452 ASN B ND2 2301 N N . ILE B 70 ? 0.7429 0.7882 0.8923 0.0452 -0.0612 0.0535 453 ILE B N 2302 C CA . ILE B 70 ? 0.7528 0.7871 0.9153 0.0428 -0.0762 0.0541 453 ILE B CA 2303 C C . ILE B 70 ? 0.7750 0.8181 0.9605 0.0391 -0.0763 0.0611 453 ILE B C 2304 O O . ILE B 70 ? 0.7854 0.8307 0.9626 0.0361 -0.0697 0.0639 453 ILE B O 2305 C CB . ILE B 70 ? 0.7554 0.7634 0.8898 0.0395 -0.0878 0.0485 453 ILE B CB 2306 C CG1 . ILE B 70 ? 0.7449 0.7414 0.8602 0.0428 -0.0898 0.0424 453 ILE B CG1 2307 C CG2 . ILE B 70 ? 0.7555 0.7522 0.9019 0.0370 -0.1041 0.0492 453 ILE B CG2 2308 C CD1 . ILE B 70 ? 0.7532 0.7248 0.8355 0.0398 -0.0955 0.0377 453 ILE B CD1 2309 N N . THR B 71 ? 0.7796 0.8274 0.9956 0.0395 -0.0843 0.0639 454 THR B N 2310 C CA . THR B 71 ? 0.8032 0.8571 1.0456 0.0356 -0.0870 0.0700 454 THR B CA 2311 C C . THR B 71 ? 0.8153 0.8541 1.0681 0.0334 -0.1071 0.0667 454 THR B C 2312 O O . THR B 71 ? 0.8734 0.9041 1.1248 0.0365 -0.1172 0.0620 454 THR B O 2313 C CB . THR B 71 ? 0.8016 0.8805 1.0795 0.0380 -0.0749 0.0779 454 THR B CB 2314 O OG1 . THR B 71 ? 0.8260 0.9100 1.1242 0.0424 -0.0792 0.0760 454 THR B OG1 2315 C CG2 . THR B 71 ? 0.7923 0.8848 1.0565 0.0410 -0.0559 0.0811 454 THR B CG2 2316 N N . ALA B 72 ? 0.8148 0.8486 1.0759 0.0285 -0.1135 0.0687 455 ALA B N 2317 C CA . ALA B 72 ? 0.8286 0.8495 1.1033 0.0263 -0.1332 0.0657 455 ALA B CA 2318 C C . ALA B 72 ? 0.8300 0.8658 1.1470 0.0232 -0.1322 0.0726 455 ALA B C 2319 O O . ALA B 72 ? 0.8029 0.8534 1.1284 0.0218 -0.1166 0.0797 455 ALA B O 2320 C CB . ALA B 72 ? 0.8366 0.8328 1.0769 0.0231 -0.1431 0.0597 455 ALA B CB 2321 N N . SER B 73 ? 0.8951 0.9270 1.2392 0.0222 -0.1489 0.0708 456 SER B N 2322 C CA . SER B 73 ? 0.9276 0.9713 1.3146 0.0183 -0.1499 0.0768 456 SER B CA 2323 C C . SER B 73 ? 0.9667 0.9911 1.3500 0.0137 -0.1681 0.0717 456 SER B C 2324 O O . SER B 73 ? 0.9596 0.9634 1.3218 0.0148 -0.1858 0.0632 456 SER B O 2325 C CB . SER B 73 ? 0.9374 0.9972 1.3701 0.0209 -0.1528 0.0794 456 SER B CB 2326 O OG . SER B 73 ? 0.9710 1.0184 1.3977 0.0245 -0.1704 0.0716 456 SER B OG 2327 N N . TYR B 74 ? 1.0241 1.0542 1.4259 0.0089 -0.1631 0.0770 457 TYR B N 2328 C CA . TYR B 74 ? 1.1002 1.1138 1.5040 0.0045 -0.1793 0.0722 457 TYR B CA 2329 C C . TYR B 74 ? 1.1265 1.1554 1.5816 0.0002 -0.1770 0.0798 457 TYR B C 2330 O O . TYR B 74 ? 1.1213 1.1658 1.5877 -0.0012 -0.1580 0.0895 457 TYR B O 2331 C CB . TYR B 74 ? 1.1281 1.1266 1.4899 0.0025 -0.1748 0.0694 457 TYR B CB 2332 C CG . TYR B 74 ? 1.1838 1.1624 1.5420 -0.0011 -0.1922 0.0626 457 TYR B CG 2333 C CD1 . TYR B 74 ? 1.1963 1.1785 1.5771 -0.0059 -0.1894 0.0668 457 TYR B CD1 2334 C CD2 . TYR B 74 ? 1.2224 1.1773 1.5543 0.0006 -0.2118 0.0519 457 TYR B CD2 2335 C CE1 . TYR B 74 ? 1.2438 1.2072 1.6220 -0.0090 -0.2058 0.0594 457 TYR B CE1 2336 C CE2 . TYR B 74 ? 1.2690 1.2046 1.5955 -0.0020 -0.2282 0.0446 457 TYR B CE2 2337 C CZ . TYR B 74 ? 1.2881 1.2281 1.6384 -0.0069 -0.2253 0.0479 457 TYR B CZ 2338 O OH . TYR B 74 ? 1.3633 1.2835 1.7084 -0.0093 -0.2418 0.0397 457 TYR B OH 2339 N N . ASP B 75 ? 1.1669 1.1902 1.6521 -0.0015 -0.1969 0.0754 458 ASP B N 2340 C CA . ASP B 75 ? 1.1553 1.1961 1.6998 -0.0046 -0.1963 0.0822 458 ASP B CA 2341 C C . ASP B 75 ? 1.1406 1.2062 1.7082 -0.0009 -0.1784 0.0907 458 ASP B C 2342 O O . ASP B 75 ? 1.1365 1.2016 1.6924 0.0041 -0.1822 0.0864 458 ASP B O 2343 C CB . ASP B 75 ? 1.1432 1.1861 1.7032 -0.0105 -0.1889 0.0884 458 ASP B CB 2344 C CG . ASP B 75 ? 1.1709 1.1889 1.7103 -0.0137 -0.2073 0.0786 458 ASP B CG 2345 O OD1 . ASP B 75 ? 1.1708 1.1692 1.6813 -0.0111 -0.2255 0.0673 458 ASP B OD1 2346 O OD2 . ASP B 75 ? 1.1803 1.1976 1.7318 -0.0183 -0.2033 0.0824 458 ASP B OD2 2347 N N . ASN B 76 ? 1.1246 1.2106 1.7223 -0.0029 -0.1586 0.1027 459 ASN B N 2348 C CA . ASN B 76 ? 1.1215 1.2305 1.7374 0.0010 -0.1392 0.1110 459 ASN B CA 2349 C C . ASN B 76 ? 1.0944 1.2080 1.6691 0.0042 -0.1174 0.1157 459 ASN B C 2350 O O . ASN B 76 ? 1.0687 1.1985 1.6467 0.0088 -0.1013 0.1206 459 ASN B O 2351 C CB . ASN B 76 ? 1.1291 1.2582 1.8052 -0.0024 -0.1295 0.1220 459 ASN B CB 2352 C CG . ASN B 76 ? 1.1231 1.2709 1.8387 0.0013 -0.1251 0.1244 459 ASN B CG 2353 O OD1 . ASN B 76 ? 1.0895 1.2334 1.7949 0.0061 -0.1356 0.1162 459 ASN B OD1 2354 N ND2 . ASN B 76 ? 1.1207 1.2889 1.8833 -0.0005 -0.1091 0.1361 459 ASN B ND2 2355 N N . GLU B 77 ? 1.0977 1.1969 1.6343 0.0021 -0.1176 0.1135 460 GLU B N 2356 C CA . GLU B 77 ? 1.0723 1.1746 1.5704 0.0048 -0.0993 0.1172 460 GLU B CA 2357 C C . GLU B 77 ? 1.0236 1.1198 1.4834 0.0103 -0.1003 0.1091 460 GLU B C 2358 O O . GLU B 77 ? 1.0330 1.1175 1.4877 0.0116 -0.1171 0.1001 460 GLU B O 2359 C CB . GLU B 77 ? 1.1095 1.1974 1.5813 0.0009 -0.1010 0.1161 460 GLU B CB 2360 C CG . GLU B 77 ? 1.1366 1.2272 1.6409 -0.0047 -0.1000 0.1237 460 GLU B CG 2361 C CD . GLU B 77 ? 1.1740 1.2488 1.6505 -0.0078 -0.1028 0.1212 460 GLU B CD 2362 O OE1 . GLU B 77 ? 1.1742 1.2309 1.6130 -0.0070 -0.1132 0.1104 460 GLU B OE1 2363 O OE2 . GLU B 77 ? 1.2131 1.2931 1.7057 -0.0109 -0.0938 0.1303 460 GLU B OE2 2364 N N . THR B 78 ? 0.9477 1.0517 1.3815 0.0138 -0.0825 0.1127 461 THR B N 2365 C CA . THR B 78 ? 0.8821 0.9800 1.2772 0.0185 -0.0812 0.1054 461 THR B CA 2366 C C . THR B 78 ? 0.8400 0.9252 1.1934 0.0171 -0.0788 0.1025 461 THR B C 2367 O O . THR B 78 ? 0.8398 0.9313 1.1923 0.0155 -0.0675 0.1095 461 THR B O 2368 C CB . THR B 78 ? 0.8590 0.9769 1.2587 0.0244 -0.0626 0.1106 461 THR B CB 2369 O OG1 . THR B 78 ? 0.8704 0.9979 1.3056 0.0266 -0.0663 0.1107 461 THR B OG1 2370 C CG2 . THR B 78 ? 0.8597 0.9720 1.2173 0.0290 -0.0584 0.1037 461 THR B CG2 2371 N N . VAL B 79 ? 0.7988 0.8662 1.1189 0.0179 -0.0889 0.0925 462 VAL B N 2372 C CA . VAL B 79 ? 0.7662 0.8205 1.0475 0.0167 -0.0870 0.0884 462 VAL B CA 2373 C C . VAL B 79 ? 0.7411 0.7965 0.9928 0.0213 -0.0786 0.0844 462 VAL B C 2374 O O . VAL B 79 ? 0.7205 0.7691 0.9637 0.0240 -0.0854 0.0783 462 VAL B O 2375 C CB . VAL B 79 ? 0.7808 0.8106 1.0447 0.0134 -0.1048 0.0798 462 VAL B CB 2376 C CG1 . VAL B 79 ? 0.7871 0.8053 1.0162 0.0117 -0.1004 0.0766 462 VAL B CG1 2377 C CG2 . VAL B 79 ? 0.7955 0.8228 1.0906 0.0093 -0.1164 0.0816 462 VAL B CG2 2378 N N . THR B 80 ? 0.7154 0.7790 0.9525 0.0223 -0.0643 0.0879 463 THR B N 2379 C CA . THR B 80 ? 0.6900 0.7542 0.8985 0.0263 -0.0565 0.0834 463 THR B CA 2380 C C . THR B 80 ? 0.6795 0.7278 0.8563 0.0236 -0.0588 0.0777 463 THR B C 2381 O O . THR B 80 ? 0.6892 0.7298 0.8666 0.0195 -0.0628 0.0789 463 THR B O 2382 C CB . THR B 80 ? 0.6769 0.7615 0.8894 0.0301 -0.0392 0.0905 463 THR B CB 2383 O OG1 . THR B 80 ? 0.6587 0.7468 0.8737 0.0275 -0.0336 0.0974 463 THR B OG1 2384 C CG2 . THR B 80 ? 0.6890 0.7906 0.9323 0.0334 -0.0335 0.0964 463 THR B CG2 2385 N N . LEU B 81 ? 0.6588 0.7026 0.8096 0.0262 -0.0554 0.0715 464 LEU B N 2386 C CA . LEU B 81 ? 0.6490 0.6813 0.7719 0.0241 -0.0540 0.0667 464 LEU B CA 2387 C C . LEU B 81 ? 0.6641 0.7074 0.7883 0.0236 -0.0441 0.0725 464 LEU B C 2388 O O . LEU B 81 ? 0.6665 0.7002 0.7789 0.0205 -0.0454 0.0707 464 LEU B O 2389 C CB . LEU B 81 ? 0.6323 0.6606 0.7323 0.0271 -0.0508 0.0596 464 LEU B CB 2390 C CG . LEU B 81 ? 0.6172 0.6340 0.6906 0.0251 -0.0485 0.0538 464 LEU B CG 2391 C CD1 . LEU B 81 ? 0.6196 0.6153 0.6820 0.0206 -0.0578 0.0503 464 LEU B CD1 2392 C CD2 . LEU B 81 ? 0.6190 0.6332 0.6759 0.0281 -0.0454 0.0473 464 LEU B CD2 2393 N N . GLN B 82 ? 0.6777 0.7402 0.8166 0.0271 -0.0342 0.0798 465 GLN B N 2394 C CA . GLN B 82 ? 0.6978 0.7709 0.8370 0.0277 -0.0248 0.0866 465 GLN B CA 2395 C C . GLN B 82 ? 0.6991 0.7688 0.8545 0.0230 -0.0284 0.0928 465 GLN B C 2396 O O . GLN B 82 ? 0.7382 0.8090 0.8881 0.0223 -0.0242 0.0961 465 GLN B O 2397 C CB . GLN B 82 ? 0.7127 0.8058 0.8612 0.0332 -0.0130 0.0935 465 GLN B CB 2398 C CG . GLN B 82 ? 0.7420 0.8393 0.8719 0.0385 -0.0082 0.0868 465 GLN B CG 2399 C CD . GLN B 82 ? 0.7519 0.8452 0.8861 0.0399 -0.0134 0.0808 465 GLN B CD 2400 O OE1 . GLN B 82 ? 0.7214 0.8043 0.8374 0.0402 -0.0177 0.0717 465 GLN B OE1 2401 N NE2 . GLN B 82 ? 0.7857 0.8873 0.9457 0.0408 -0.0131 0.0862 465 GLN B NE2 2402 N N . ASP B 83 ? 0.6833 0.7484 0.8592 0.0202 -0.0369 0.0938 466 ASP B N 2403 C CA . ASP B 83 ? 0.6881 0.7474 0.8807 0.0154 -0.0426 0.0978 466 ASP B CA 2404 C C . ASP B 83 ? 0.6768 0.7164 0.8498 0.0117 -0.0510 0.0900 466 ASP B C 2405 O O . ASP B 83 ? 0.6789 0.7148 0.8590 0.0086 -0.0522 0.0930 466 ASP B O 2406 C CB . ASP B 83 ? 0.7044 0.7637 0.9260 0.0135 -0.0513 0.0996 466 ASP B CB 2407 C CG . ASP B 83 ? 0.7153 0.7947 0.9631 0.0165 -0.0417 0.1087 466 ASP B CG 2408 O OD1 . ASP B 83 ? 0.7378 0.8306 0.9891 0.0185 -0.0286 0.1175 466 ASP B OD1 2409 O OD2 . ASP B 83 ? 0.7434 0.8248 1.0082 0.0173 -0.0473 0.1070 466 ASP B OD2 2410 N N . ILE B 84 ? 0.6689 0.6956 0.8178 0.0121 -0.0560 0.0803 467 ILE B N 2411 C CA . ILE B 84 ? 0.6674 0.6734 0.7970 0.0088 -0.0636 0.0724 467 ILE B CA 2412 C C . ILE B 84 ? 0.6731 0.6739 0.7748 0.0096 -0.0573 0.0669 467 ILE B C 2413 O O . ILE B 84 ? 0.7012 0.6860 0.7876 0.0071 -0.0610 0.0611 467 ILE B O 2414 C CB . ILE B 84 ? 0.6792 0.6689 0.8037 0.0079 -0.0769 0.0656 467 ILE B CB 2415 C CG1 . ILE B 84 ? 0.6715 0.6606 0.7813 0.0114 -0.0760 0.0613 467 ILE B CG1 2416 C CG2 . ILE B 84 ? 0.6753 0.6693 0.8310 0.0067 -0.0852 0.0701 467 ILE B CG2 2417 C CD1 . ILE B 84 ? 0.6789 0.6493 0.7789 0.0110 -0.0894 0.0548 467 ILE B CD1 2418 N N . CYS B 85 ? 0.6689 0.6828 0.7647 0.0133 -0.0479 0.0682 468 CYS B N 2419 C CA . CYS B 85 ? 0.6612 0.6704 0.7329 0.0141 -0.0430 0.0616 468 CYS B CA 2420 C C . CYS B 85 ? 0.6428 0.6561 0.7122 0.0135 -0.0371 0.0636 468 CYS B C 2421 O O . CYS B 85 ? 0.6353 0.6574 0.7207 0.0134 -0.0351 0.0714 468 CYS B O 2422 C CB . CYS B 85 ? 0.6747 0.6949 0.7410 0.0185 -0.0371 0.0604 468 CYS B CB 2423 S SG . CYS B 85 ? 0.6893 0.7344 0.7684 0.0232 -0.0265 0.0693 468 CYS B SG 2424 N N . LEU B 86 ? 0.6223 0.6286 0.6728 0.0133 -0.0343 0.0565 469 LEU B N 2425 C CA . LEU B 86 ? 0.6079 0.6199 0.6554 0.0139 -0.0285 0.0569 469 LEU B CA 2426 C C . LEU B 86 ? 0.5933 0.6233 0.6410 0.0189 -0.0218 0.0598 469 LEU B C 2427 O O . LEU B 86 ? 0.6065 0.6375 0.6440 0.0209 -0.0203 0.0545 469 LEU B O 2428 C CB . LEU B 86 ? 0.6242 0.6217 0.6536 0.0117 -0.0279 0.0475 469 LEU B CB 2429 C CG . LEU B 86 ? 0.6200 0.6219 0.6468 0.0122 -0.0225 0.0458 469 LEU B CG 2430 C CD1 . LEU B 86 ? 0.5975 0.6022 0.6374 0.0115 -0.0230 0.0519 469 LEU B CD1 2431 C CD2 . LEU B 86 ? 0.6361 0.6223 0.6474 0.0096 -0.0212 0.0363 469 LEU B CD2 2432 N N . ALA B 87 ? 0.5837 0.6268 0.6423 0.0211 -0.0180 0.0683 470 ALA B N 2433 C CA . ALA B 87 ? 0.5697 0.6297 0.6270 0.0267 -0.0118 0.0721 470 ALA B CA 2434 C C . ALA B 87 ? 0.5528 0.6198 0.6098 0.0288 -0.0087 0.0763 470 ALA B C 2435 O O . ALA B 87 ? 0.5380 0.6129 0.6064 0.0302 -0.0062 0.0866 470 ALA B O 2436 C CB . ALA B 87 ? 0.5663 0.6368 0.6379 0.0289 -0.0096 0.0808 470 ALA B CB 2437 N N . PRO B 88 ? 0.5544 0.6183 0.5996 0.0291 -0.0088 0.0685 471 PRO B N 2438 C CA . PRO B 88 ? 0.5587 0.6260 0.6053 0.0303 -0.0080 0.0710 471 PRO B CA 2439 C C . PRO B 88 ? 0.5897 0.6725 0.6331 0.0370 -0.0045 0.0767 471 PRO B C 2440 O O . PRO B 88 ? 0.5928 0.6780 0.6366 0.0387 -0.0051 0.0784 471 PRO B O 2441 C CB . PRO B 88 ? 0.5408 0.5983 0.5782 0.0279 -0.0095 0.0593 471 PRO B CB 2442 C CG . PRO B 88 ? 0.5368 0.5929 0.5643 0.0283 -0.0091 0.0519 471 PRO B CG 2443 C CD . PRO B 88 ? 0.5429 0.5984 0.5753 0.0277 -0.0100 0.0568 471 PRO B CD 2444 N N . LEU B 89 ? 0.6306 0.7234 0.6702 0.0413 -0.0011 0.0794 472 LEU B N 2445 C CA . LEU B 89 ? 0.6661 0.7726 0.6992 0.0486 0.0024 0.0852 472 LEU B CA 2446 C C . LEU B 89 ? 0.7208 0.8330 0.7642 0.0502 0.0060 0.1001 472 LEU B C 2447 O O . LEU B 89 ? 0.7439 0.8632 0.7815 0.0554 0.0074 0.1058 472 LEU B O 2448 C CB . LEU B 89 ? 0.6544 0.7691 0.6777 0.0535 0.0058 0.0820 472 LEU B CB 2449 C CG . LEU B 89 ? 0.6484 0.7621 0.6580 0.0553 0.0028 0.0685 472 LEU B CG 2450 C CD1 . LEU B 89 ? 0.6513 0.7691 0.6545 0.0585 0.0054 0.0638 472 LEU B CD1 2451 C CD2 . LEU B 89 ? 0.6533 0.7742 0.6535 0.0609 0.0012 0.0677 472 LEU B CD2 2452 N N . SER B 90 ? 0.7721 0.8805 0.8312 0.0459 0.0069 0.1064 473 SER B N 2453 C CA . SER B 90 ? 0.8506 0.9637 0.9235 0.0465 0.0109 0.1212 473 SER B CA 2454 C C . SER B 90 ? 0.8827 0.9859 0.9757 0.0392 0.0074 0.1235 473 SER B C 2455 O O . SER B 90 ? 0.8597 0.9548 0.9539 0.0351 0.0031 0.1149 473 SER B O 2456 C CB . SER B 90 ? 0.8731 0.9992 0.9445 0.0523 0.0194 0.1299 473 SER B CB 2457 O OG . SER B 90 ? 0.9359 1.0637 1.0282 0.0496 0.0235 0.1407 473 SER B OG 2458 N N A PRO B 91 ? 0.9127 1.0156 1.0211 0.0379 0.0087 0.1348 474 PRO B N 2459 N N B PRO B 91 ? 0.9241 1.0270 1.0324 0.0380 0.0087 0.1348 474 PRO B N 2460 C CA A PRO B 91 ? 0.9306 1.0242 1.0600 0.0313 0.0047 0.1370 474 PRO B CA 2461 C CA B PRO B 91 ? 0.9490 1.0423 1.0782 0.0314 0.0045 0.1372 474 PRO B CA 2462 C C A PRO B 91 ? 0.9512 1.0462 1.0936 0.0289 0.0048 0.1373 474 PRO B C 2463 C C B PRO B 91 ? 0.9809 1.0741 1.1246 0.0282 0.0039 0.1375 474 PRO B C 2464 O O A PRO B 91 ? 0.9556 1.0408 1.1121 0.0233 -0.0015 0.1346 474 PRO B O 2465 O O B PRO B 91 ? 0.9875 1.0698 1.1433 0.0226 -0.0029 0.1337 474 PRO B O 2466 C CB A PRO B 91 ? 0.9251 1.0221 1.0691 0.0321 0.0085 0.1514 474 PRO B CB 2467 C CB B PRO B 91 ? 0.9418 1.0391 1.0846 0.0326 0.0088 0.1520 474 PRO B CB 2468 C CG A PRO B 91 ? 0.9227 1.0243 1.0493 0.0379 0.0104 0.1526 474 PRO B CG 2469 C CG B PRO B 91 ? 0.9386 1.0419 1.0633 0.0389 0.0114 0.1536 474 PRO B CG 2470 C CD A PRO B 91 ? 0.9180 1.0271 1.0238 0.0426 0.0125 0.1451 474 PRO B CD 2471 C CD B PRO B 91 ? 0.9312 1.0415 1.0361 0.0432 0.0132 0.1455 474 PRO B CD 2472 N N A TYR B 92 ? 0.9601 1.0669 1.0982 0.0335 0.0115 0.1402 475 TYR B N 2473 N N B TYR B 92 ? 1.0027 1.1077 1.1458 0.0322 0.0106 0.1416 475 TYR B N 2474 C CA A TYR B 92 ? 0.9699 1.0786 1.1189 0.0321 0.0112 0.1383 475 TYR B CA 2475 C CA B TYR B 92 ? 1.0204 1.1263 1.1791 0.0298 0.0097 0.1412 475 TYR B CA 2476 C C A TYR B 92 ? 0.9426 1.0593 1.0744 0.0375 0.0155 0.1326 475 TYR B C 2477 C C B TYR B 92 ? 0.9884 1.0937 1.1316 0.0314 0.0075 0.1296 475 TYR B C 2478 O O A TYR B 92 ? 0.9561 1.0828 1.0964 0.0403 0.0219 0.1375 475 TYR B O 2479 O O B TYR B 92 ? 0.9964 1.0949 1.1199 0.0316 0.0036 0.1192 475 TYR B O 2480 C CB A TYR B 92 ? 1.0073 1.1235 1.1836 0.0312 0.0169 0.1519 475 TYR B CB 2481 C CB B TYR B 92 ? 1.0574 1.1767 1.2343 0.0323 0.0197 0.1555 475 TYR B CB 2482 C CG A TYR B 92 ? 1.0293 1.1357 1.2272 0.0247 0.0104 0.1553 475 TYR B CG 2483 C CG B TYR B 92 ? 1.0783 1.1944 1.2870 0.0267 0.0175 0.1633 475 TYR B CG 2484 C CD1 A TYR B 92 ? 1.0166 1.1137 1.2299 0.0192 0.0010 0.1492 475 TYR B CD1 2485 C CD1 B TYR B 92 ? 1.0707 1.1843 1.2984 0.0229 0.0120 0.1595 475 TYR B CD1 2486 C CD2 A TYR B 92 ? 1.0382 1.1436 1.2407 0.0246 0.0128 0.1642 475 TYR B CD2 2487 C CD2 B TYR B 92 ? 1.0874 1.2023 1.3081 0.0253 0.0199 0.1740 475 TYR B CD2 2488 C CE1 A TYR B 92 ? 1.0099 1.0972 1.2423 0.0137 -0.0057 0.1510 475 TYR B CE1 2489 C CE1 B TYR B 92 ? 1.0685 1.1793 1.3274 0.0177 0.0086 0.1656 475 TYR B CE1 2490 C CE2 A TYR B 92 ? 1.0255 1.1211 1.2485 0.0188 0.0067 0.1665 475 TYR B CE2 2491 C CE2 B TYR B 92 ? 1.0863 1.1978 1.3382 0.0199 0.0173 0.1805 475 TYR B CE2 2492 C CZ A TYR B 92 ? 1.0105 1.0971 1.2483 0.0134 -0.0025 0.1594 475 TYR B CZ 2493 C CZ B TYR B 92 ? 1.0799 1.1896 1.3512 0.0160 0.0115 0.1759 475 TYR B CZ 2494 O OH A TYR B 92 ? 0.9787 1.0549 1.2364 0.0080 -0.0096 0.1604 475 TYR B OH 2495 O OH B TYR B 92 ? 1.0707 1.1770 1.3751 0.0105 0.0077 0.1814 475 TYR B OH 2496 N N A ASN B 93 ? 0.9065 1.0188 1.0159 0.0390 0.0122 0.1218 476 ASN B N 2497 N N B ASN B 93 ? 0.9567 1.0688 1.1112 0.0325 0.0103 0.1315 476 ASN B N 2498 C CA A ASN B 93 ? 0.8663 0.9848 0.9594 0.0441 0.0152 0.1150 476 ASN B CA 2499 C CA B ASN B 93 ? 0.9200 1.0315 1.0628 0.0344 0.0084 0.1214 476 ASN B CA 2500 C C A ASN B 93 ? 0.8284 0.9435 0.9272 0.0423 0.0121 0.1085 476 ASN B C 2501 C C B ASN B 93 ? 0.9008 1.0203 1.0202 0.0409 0.0148 0.1183 476 ASN B C 2502 O O A ASN B 93 ? 0.8169 0.9215 0.9268 0.0367 0.0050 0.1061 476 ASN B O 2503 O O B ASN B 93 ? 0.8954 1.0247 1.0110 0.0454 0.0227 0.1266 476 ASN B O 2504 C CB A ASN B 93 ? 0.8711 0.9847 0.9427 0.0452 0.0116 0.1044 476 ASN B CB 2505 C CB B ASN B 93 ? 0.9068 1.0255 1.0704 0.0350 0.0106 0.1251 476 ASN B CB 2506 C CG A ASN B 93 ? 0.8790 0.9993 0.9345 0.0508 0.0144 0.0971 476 ASN B CG 2507 C CG B ASN B 93 ? 0.8873 0.9980 1.0758 0.0287 0.0021 0.1266 476 ASN B CG 2508 O OD1 A ASN B 93 ? 0.9002 1.0162 0.9541 0.0497 0.0119 0.0891 476 ASN B OD1 2509 O OD1 B ASN B 93 ? 0.8789 0.9800 1.0708 0.0243 -0.0035 0.1272 476 ASN B OD1 2510 N ND2 A ASN B 93 ? 0.8742 1.0040 0.9171 0.0573 0.0189 0.0997 476 ASN B ND2 2511 N ND2 B ASN B 93 ? 0.8706 0.9849 1.0774 0.0286 0.0004 0.1266 476 ASN B ND2 2512 N N A THR B 94 ? 0.8038 0.9269 0.8936 0.0476 0.0167 0.1050 477 THR B N 2513 N N B THR B 94 ? 0.8861 1.0001 0.9894 0.0416 0.0108 0.1064 477 THR B N 2514 C CA A THR B 94 ? 0.7812 0.9023 0.8763 0.0473 0.0143 0.0991 477 THR B CA 2515 C CA B THR B 94 ? 0.8812 1.0021 0.9640 0.0477 0.0153 0.1013 477 THR B CA 2516 C C A THR B 94 ? 0.7789 0.8926 0.8544 0.0481 0.0101 0.0856 477 THR B C 2517 C C B THR B 94 ? 0.8618 0.9726 0.9329 0.0461 0.0090 0.0877 477 THR B C 2518 O O A THR B 94 ? 0.7568 0.8680 0.8343 0.0486 0.0079 0.0802 477 THR B O 2519 O O B THR B 94 ? 0.8812 0.9835 0.9610 0.0424 0.0035 0.0848 477 THR B O 2520 C CB A THR B 94 ? 0.7618 0.8977 0.8667 0.0528 0.0239 0.1056 477 THR B CB 2521 C CB B THR B 94 ? 0.8838 1.0071 0.9537 0.0500 0.0171 0.1036 477 THR B CB 2522 O OG1 A THR B 94 ? 0.7534 0.8872 0.8764 0.0506 0.0203 0.1042 477 THR B OG1 2523 O OG1 B THR B 94 ? 0.8808 1.0129 0.9326 0.0571 0.0215 0.0998 477 THR B OG1 2524 C CG2 A THR B 94 ? 0.7562 0.8993 0.8404 0.0600 0.0292 0.0994 477 THR B CG2 2525 C CG2 B THR B 94 ? 0.8833 0.9933 0.9469 0.0450 0.0092 0.0957 477 THR B CG2 2526 N N A ASN B 95 ? 0.7789 0.8892 0.8375 0.0483 0.0088 0.0803 478 ASN B N 2527 N N B ASN B 95 ? 0.8367 0.9477 0.8889 0.0492 0.0093 0.0796 478 ASN B N 2528 C CA A ASN B 95 ? 0.7942 0.8955 0.8374 0.0477 0.0045 0.0677 478 ASN B CA 2529 C CA B ASN B 95 ? 0.8284 0.9297 0.8704 0.0478 0.0045 0.0674 478 ASN B CA 2530 C C A ASN B 95 ? 0.7620 0.8465 0.8037 0.0408 -0.0027 0.0628 478 ASN B C 2531 C C B ASN B 95 ? 0.7813 0.8656 0.8230 0.0407 -0.0027 0.0629 478 ASN B C 2532 O O A ASN B 95 ? 0.7712 0.8517 0.8079 0.0387 -0.0037 0.0619 478 ASN B O 2533 O O B ASN B 95 ? 0.7885 0.8684 0.8260 0.0384 -0.0040 0.0623 478 ASN B O 2534 C CB A ASN B 95 ? 0.8342 0.9419 0.8611 0.0525 0.0073 0.0629 478 ASN B CB 2535 C CB B ASN B 95 ? 0.8637 0.9689 0.8882 0.0521 0.0062 0.0596 478 ASN B CB 2536 C CG A ASN B 95 ? 0.8935 1.0133 0.9150 0.0599 0.0131 0.0621 478 ASN B CG 2537 C CG B ASN B 95 ? 0.9200 1.0384 0.9401 0.0597 0.0124 0.0599 478 ASN B CG 2538 O OD1 A ASN B 95 ? 0.9016 1.0238 0.9314 0.0611 0.0152 0.0631 478 ASN B OD1 2539 O OD1 B ASN B 95 ? 0.9307 1.0516 0.9587 0.0611 0.0144 0.0609 478 ASN B OD1 2540 N ND2 A ASN B 95 ? 0.9761 1.1035 0.9839 0.0653 0.0155 0.0598 478 ASN B ND2 2541 N ND2 B ASN B 95 ? 0.9929 1.1195 1.0002 0.0651 0.0150 0.0587 478 ASN B ND2 2542 N N . CYS B 96 ? 0.7479 0.8220 0.7934 0.0378 -0.0076 0.0597 479 CYS B N 2543 C CA . CYS B 96 ? 0.7313 0.7874 0.7726 0.0319 -0.0144 0.0551 479 CYS B CA 2544 C C . CYS B 96 ? 0.6901 0.7369 0.7140 0.0308 -0.0147 0.0452 479 CYS B C 2545 O O . CYS B 96 ? 0.6884 0.7392 0.7048 0.0340 -0.0122 0.0398 479 CYS B O 2546 C CB . CYS B 96 ? 0.7476 0.7947 0.7957 0.0300 -0.0207 0.0545 479 CYS B CB 2547 S SG . CYS B 96 ? 0.8206 0.8755 0.8948 0.0293 -0.0225 0.0653 479 CYS B SG 2548 N N . THR B 97 ? 0.6497 0.6839 0.6686 0.0262 -0.0172 0.0427 480 THR B N 2549 C CA . THR B 97 ? 0.6431 0.6669 0.6482 0.0242 -0.0164 0.0338 480 THR B CA 2550 C C . THR B 97 ? 0.6512 0.6614 0.6477 0.0230 -0.0194 0.0284 480 THR B C 2551 O O . THR B 97 ? 0.6847 0.6831 0.6812 0.0206 -0.0247 0.0298 480 THR B O 2552 C CB . THR B 97 ? 0.6391 0.6523 0.6421 0.0198 -0.0171 0.0331 480 THR B CB 2553 O OG1 . THR B 97 ? 0.6168 0.6423 0.6290 0.0214 -0.0150 0.0389 480 THR B OG1 2554 C CG2 . THR B 97 ? 0.6356 0.6387 0.6266 0.0177 -0.0145 0.0241 480 THR B CG2 2555 N N . ILE B 98 ? 0.6515 0.6635 0.6412 0.0252 -0.0168 0.0223 481 ILE B N 2556 C CA . ILE B 98 ? 0.6589 0.6569 0.6396 0.0242 -0.0189 0.0170 481 ILE B CA 2557 C C . ILE B 98 ? 0.6464 0.6387 0.6178 0.0226 -0.0148 0.0091 481 ILE B C 2558 O O . ILE B 98 ? 0.6676 0.6715 0.6409 0.0257 -0.0118 0.0054 481 ILE B O 2559 C CB . ILE B 98 ? 0.6899 0.6963 0.6755 0.0289 -0.0195 0.0171 481 ILE B CB 2560 C CG1 . ILE B 98 ? 0.7038 0.7205 0.7038 0.0310 -0.0218 0.0254 481 ILE B CG1 2561 C CG2 . ILE B 98 ? 0.7124 0.7020 0.6895 0.0279 -0.0230 0.0128 481 ILE B CG2 2562 C CD1 . ILE B 98 ? 0.7055 0.7351 0.7133 0.0366 -0.0199 0.0260 481 ILE B CD1 2563 N N . LEU B 99 ? 0.6254 0.5996 0.5871 0.0181 -0.0146 0.0063 482 LEU B N 2564 C CA . LEU B 99 ? 0.6230 0.5904 0.5784 0.0160 -0.0097 -0.0009 482 LEU B CA 2565 C C . LEU B 99 ? 0.6340 0.5926 0.5833 0.0169 -0.0102 -0.0046 482 LEU B C 2566 O O . LEU B 99 ? 0.6630 0.6053 0.6032 0.0154 -0.0131 -0.0032 482 LEU B O 2567 C CB . LEU B 99 ? 0.6251 0.5767 0.5728 0.0110 -0.0070 -0.0020 482 LEU B CB 2568 C CG . LEU B 99 ? 0.6312 0.5894 0.5857 0.0102 -0.0071 0.0017 482 LEU B CG 2569 C CD1 . LEU B 99 ? 0.6595 0.6013 0.6058 0.0058 -0.0032 -0.0009 482 LEU B CD1 2570 C CD2 . LEU B 99 ? 0.6170 0.5955 0.5833 0.0131 -0.0052 0.0013 482 LEU B CD2 2571 N N . SER B 100 ? 0.6287 0.5980 0.5827 0.0198 -0.0082 -0.0096 483 SER B N 2572 C CA . SER B 100 ? 0.6333 0.5967 0.5844 0.0214 -0.0088 -0.0135 483 SER B CA 2573 C C . SER B 100 ? 0.6159 0.5890 0.5721 0.0232 -0.0057 -0.0214 483 SER B C 2574 O O . SER B 100 ? 0.6273 0.6168 0.5899 0.0257 -0.0051 -0.0223 483 SER B O 2575 C CB . SER B 100 ? 0.6401 0.6112 0.5959 0.0261 -0.0135 -0.0091 483 SER B CB 2576 O OG . SER B 100 ? 0.6558 0.6269 0.6124 0.0294 -0.0138 -0.0138 483 SER B OG 2577 N N . VAL B 101 ? 0.6241 0.5864 0.5776 0.0222 -0.0043 -0.0270 484 VAL B N 2578 C CA . VAL B 101 ? 0.6129 0.5834 0.5729 0.0242 -0.0028 -0.0358 484 VAL B CA 2579 C C . VAL B 101 ? 0.5923 0.5811 0.5570 0.0313 -0.0057 -0.0371 484 VAL B C 2580 O O . VAL B 101 ? 0.5894 0.5900 0.5586 0.0342 -0.0056 -0.0437 484 VAL B O 2581 C CB . VAL B 101 ? 0.6365 0.5895 0.5938 0.0216 -0.0007 -0.0409 484 VAL B CB 2582 C CG1 . VAL B 101 ? 0.6501 0.5960 0.6035 0.0248 -0.0043 -0.0388 484 VAL B CG1 2583 C CG2 . VAL B 101 ? 0.6498 0.6085 0.6162 0.0216 0.0012 -0.0510 484 VAL B CG2 2584 N N . LEU B 102 ? 0.6004 0.5916 0.5642 0.0344 -0.0082 -0.0308 485 LEU B N 2585 C CA . LEU B 102 ? 0.6003 0.6091 0.5684 0.0415 -0.0091 -0.0309 485 LEU B CA 2586 C C . LEU B 102 ? 0.5897 0.6161 0.5600 0.0441 -0.0080 -0.0280 485 LEU B C 2587 O O . LEU B 102 ? 0.6009 0.6420 0.5720 0.0504 -0.0074 -0.0300 485 LEU B O 2588 C CB . LEU B 102 ? 0.6205 0.6277 0.5907 0.0439 -0.0114 -0.0247 485 LEU B CB 2589 C CG . LEU B 102 ? 0.6506 0.6421 0.6186 0.0435 -0.0131 -0.0291 485 LEU B CG 2590 C CD1 . LEU B 102 ? 0.6855 0.6660 0.6533 0.0431 -0.0173 -0.0227 485 LEU B CD1 2591 C CD2 . LEU B 102 ? 0.6716 0.6706 0.6430 0.0491 -0.0122 -0.0377 485 LEU B CD2 2592 N N . ASN B 103 ? 0.5641 0.5885 0.5344 0.0398 -0.0076 -0.0232 486 ASN B N 2593 C CA . ASN B 103 ? 0.5639 0.6034 0.5363 0.0422 -0.0069 -0.0198 486 ASN B CA 2594 C C . ASN B 103 ? 0.5769 0.6236 0.5492 0.0440 -0.0071 -0.0283 486 ASN B C 2595 O O . ASN B 103 ? 0.5835 0.6443 0.5556 0.0483 -0.0075 -0.0265 486 ASN B O 2596 C CB . ASN B 103 ? 0.5584 0.5936 0.5323 0.0377 -0.0069 -0.0120 486 ASN B CB 2597 C CG . ASN B 103 ? 0.5608 0.6066 0.5391 0.0406 -0.0070 -0.0020 486 ASN B CG 2598 O OD1 . ASN B 103 ? 0.5550 0.6157 0.5343 0.0465 -0.0055 -0.0003 486 ASN B OD1 2599 N ND2 . ASN B 103 ? 0.5627 0.6004 0.5436 0.0365 -0.0083 0.0046 486 ASN B ND2 2600 N N . TYR B 104 ? 0.5866 0.6237 0.5596 0.0411 -0.0071 -0.0373 487 TYR B N 2601 C CA . TYR B 104 ? 0.5965 0.6410 0.5721 0.0436 -0.0088 -0.0474 487 TYR B CA 2602 C C . TYR B 104 ? 0.6091 0.6660 0.5808 0.0518 -0.0106 -0.0515 487 TYR B C 2603 O O . TYR B 104 ? 0.6382 0.7052 0.6093 0.0561 -0.0134 -0.0581 487 TYR B O 2604 C CB . TYR B 104 ? 0.5926 0.6235 0.5728 0.0384 -0.0078 -0.0563 487 TYR B CB 2605 C CG . TYR B 104 ? 0.5850 0.6035 0.5685 0.0307 -0.0044 -0.0542 487 TYR B CG 2606 C CD1 . TYR B 104 ? 0.5774 0.6014 0.5638 0.0292 -0.0040 -0.0502 487 TYR B CD1 2607 C CD2 . TYR B 104 ? 0.5851 0.5854 0.5683 0.0252 -0.0009 -0.0563 487 TYR B CD2 2608 C CE1 . TYR B 104 ? 0.5677 0.5801 0.5570 0.0227 0.0000 -0.0490 487 TYR B CE1 2609 C CE2 . TYR B 104 ? 0.5829 0.5711 0.5672 0.0186 0.0037 -0.0546 487 TYR B CE2 2610 C CZ . TYR B 104 ? 0.5821 0.5767 0.5697 0.0175 0.0044 -0.0513 487 TYR B CZ 2611 O OH . TYR B 104 ? 0.6172 0.5993 0.6056 0.0114 0.0100 -0.0501 487 TYR B OH 2612 N N . PHE B 105 ? 0.6069 0.6625 0.5761 0.0544 -0.0093 -0.0480 488 PHE B N 2613 C CA . PHE B 105 ? 0.6266 0.6939 0.5917 0.0628 -0.0092 -0.0505 488 PHE B CA 2614 C C . PHE B 105 ? 0.6286 0.7070 0.5918 0.0669 -0.0063 -0.0390 488 PHE B C 2615 O O . PHE B 105 ? 0.6345 0.7205 0.5958 0.0731 -0.0041 -0.0386 488 PHE B O 2616 C CB . PHE B 105 ? 0.6233 0.6811 0.5902 0.0633 -0.0092 -0.0561 488 PHE B CB 2617 C CG . PHE B 105 ? 0.6276 0.6727 0.5982 0.0585 -0.0109 -0.0658 488 PHE B CG 2618 C CD1 . PHE B 105 ? 0.6241 0.6525 0.5973 0.0507 -0.0098 -0.0628 488 PHE B CD1 2619 C CD2 . PHE B 105 ? 0.6314 0.6807 0.6029 0.0619 -0.0136 -0.0781 488 PHE B CD2 2620 C CE1 . PHE B 105 ? 0.6253 0.6416 0.6029 0.0461 -0.0097 -0.0707 488 PHE B CE1 2621 C CE2 . PHE B 105 ? 0.6259 0.6637 0.6043 0.0570 -0.0148 -0.0868 488 PHE B CE2 2622 C CZ . PHE B 105 ? 0.6257 0.6471 0.6077 0.0489 -0.0121 -0.0826 488 PHE B CZ 2623 N N . GLN B 106 ? 0.6297 0.7089 0.5949 0.0632 -0.0058 -0.0300 489 GLN B N 2624 C CA . GLN B 106 ? 0.6261 0.7147 0.5925 0.0657 -0.0028 -0.0180 489 GLN B CA 2625 C C . GLN B 106 ? 0.6249 0.7118 0.5967 0.0665 -0.0007 -0.0130 489 GLN B C 2626 O O . GLN B 106 ? 0.6364 0.7344 0.6100 0.0714 0.0031 -0.0064 489 GLN B O 2627 C CB . GLN B 106 ? 0.6368 0.7414 0.5958 0.0735 -0.0012 -0.0171 489 GLN B CB 2628 C CG . GLN B 106 ? 0.6371 0.7443 0.5928 0.0728 -0.0047 -0.0195 489 GLN B CG 2629 C CD . GLN B 106 ? 0.6584 0.7599 0.6137 0.0715 -0.0093 -0.0335 489 GLN B CD 2630 O OE1 . GLN B 106 ? 0.7244 0.8293 0.6742 0.0768 -0.0105 -0.0425 489 GLN B OE1 2631 N NE2 . GLN B 106 ? 0.6313 0.7238 0.5932 0.0644 -0.0114 -0.0358 489 GLN B NE2 2632 N N . ASN B 107 ? 0.6341 0.7062 0.6090 0.0617 -0.0031 -0.0158 490 ASN B N 2633 C CA . ASN B 107 ? 0.6382 0.7064 0.6196 0.0621 -0.0031 -0.0120 490 ASN B CA 2634 C C . ASN B 107 ? 0.6249 0.7047 0.6079 0.0703 0.0002 -0.0141 490 ASN B C 2635 O O . ASN B 107 ? 0.6200 0.7053 0.6116 0.0725 0.0024 -0.0073 490 ASN B O 2636 C CB . ASN B 107 ? 0.6298 0.6980 0.6187 0.0588 -0.0035 -0.0004 490 ASN B CB 2637 C CG . ASN B 107 ? 0.6323 0.6882 0.6185 0.0513 -0.0065 0.0010 490 ASN B CG 2638 O OD1 . ASN B 107 ? 0.6197 0.6630 0.6000 0.0476 -0.0082 -0.0056 490 ASN B OD1 2639 N ND2 . ASN B 107 ? 0.6333 0.6923 0.6248 0.0492 -0.0065 0.0098 490 ASN B ND2 2640 N N . SER B 108 ? 0.6204 0.7039 0.5961 0.0748 0.0007 -0.0242 491 SER B N 2641 C CA . SER B 108 ? 0.6304 0.7250 0.6045 0.0835 0.0046 -0.0280 491 SER B CA 2642 C C . SER B 108 ? 0.6437 0.7294 0.6175 0.0849 0.0022 -0.0397 491 SER B C 2643 O O . SER B 108 ? 0.6461 0.7243 0.6154 0.0823 -0.0013 -0.0485 491 SER B O 2644 C CB . SER B 108 ? 0.6296 0.7376 0.5926 0.0894 0.0071 -0.0302 491 SER B CB 2645 O OG . SER B 108 ? 0.6298 0.7456 0.5872 0.0982 0.0103 -0.0373 491 SER B OG 2646 N N . HIS B 109 ? 0.6589 0.7456 0.6394 0.0891 0.0042 -0.0397 492 HIS B N 2647 C CA . HIS B 109 ? 0.6764 0.7552 0.6579 0.0916 0.0022 -0.0507 492 HIS B CA 2648 C C . HIS B 109 ? 0.6780 0.7633 0.6495 0.0976 0.0027 -0.0628 492 HIS B C 2649 O O . HIS B 109 ? 0.6689 0.7443 0.6394 0.0961 -0.0012 -0.0734 492 HIS B O 2650 C CB . HIS B 109 ? 0.6783 0.7598 0.6703 0.0966 0.0048 -0.0484 492 HIS B CB 2651 C CG . HIS B 109 ? 0.6682 0.7413 0.6714 0.0914 0.0017 -0.0389 492 HIS B CG 2652 N ND1 . HIS B 109 ? 0.6660 0.7205 0.6711 0.0863 -0.0045 -0.0406 492 HIS B ND1 2653 C CD2 . HIS B 109 ? 0.6659 0.7461 0.6791 0.0908 0.0035 -0.0277 492 HIS B CD2 2654 C CE1 . HIS B 109 ? 0.6715 0.7216 0.6852 0.0833 -0.0075 -0.0315 492 HIS B CE1 2655 N NE2 . HIS B 109 ? 0.6741 0.7400 0.6945 0.0857 -0.0030 -0.0239 492 HIS B NE2 2656 N N . SER B 110 ? 0.6934 0.7944 0.6572 0.1043 0.0074 -0.0611 493 SER B N 2657 C CA . SER B 110 ? 0.7245 0.8317 0.6759 0.1112 0.0068 -0.0729 493 SER B CA 2658 C C . SER B 110 ? 0.7272 0.8302 0.6728 0.1067 0.0005 -0.0787 493 SER B C 2659 O O . SER B 110 ? 0.7798 0.8793 0.7222 0.1086 -0.0038 -0.0920 493 SER B O 2660 C CB . SER B 110 ? 0.7290 0.8530 0.6705 0.1205 0.0141 -0.0689 493 SER B CB 2661 O OG . SER B 110 ? 0.7419 0.8726 0.6814 0.1180 0.0164 -0.0561 493 SER B OG 2662 N N . VAL B 111 ? 0.7187 0.8216 0.6653 0.1005 -0.0003 -0.0695 494 VAL B N 2663 C CA . VAL B 111 ? 0.7074 0.8065 0.6519 0.0959 -0.0060 -0.0746 494 VAL B CA 2664 C C . VAL B 111 ? 0.7136 0.7966 0.6672 0.0888 -0.0100 -0.0825 494 VAL B C 2665 O O . VAL B 111 ? 0.7219 0.8018 0.6759 0.0879 -0.0145 -0.0934 494 VAL B O 2666 C CB . VAL B 111 ? 0.6830 0.7849 0.6282 0.0909 -0.0055 -0.0627 494 VAL B CB 2667 C CG1 . VAL B 111 ? 0.6823 0.7800 0.6289 0.0859 -0.0110 -0.0683 494 VAL B CG1 2668 C CG2 . VAL B 111 ? 0.6738 0.7910 0.6097 0.0981 -0.0013 -0.0547 494 VAL B CG2 2669 N N . LEU B 112 ? 0.7318 0.8040 0.6929 0.0840 -0.0084 -0.0767 495 LEU B N 2670 C CA . LEU B 112 ? 0.7473 0.8022 0.7151 0.0781 -0.0108 -0.0826 495 LEU B CA 2671 C C . LEU B 112 ? 0.7682 0.8210 0.7370 0.0831 -0.0128 -0.0964 495 LEU B C 2672 O O . LEU B 112 ? 0.7510 0.7927 0.7251 0.0789 -0.0156 -0.1047 495 LEU B O 2673 C CB . LEU B 112 ? 0.7412 0.7852 0.7138 0.0742 -0.0095 -0.0731 495 LEU B CB 2674 C CG . LEU B 112 ? 0.7482 0.7716 0.7247 0.0672 -0.0113 -0.0750 495 LEU B CG 2675 C CD1 . LEU B 112 ? 0.7425 0.7586 0.7186 0.0594 -0.0114 -0.0745 495 LEU B CD1 2676 C CD2 . LEU B 112 ? 0.7540 0.7683 0.7326 0.0657 -0.0114 -0.0655 495 LEU B CD2 2677 N N . ASP B 113 ? 0.7925 0.8558 0.7572 0.0921 -0.0108 -0.0990 496 ASP B N 2678 C CA . ASP B 113 ? 0.8123 0.8748 0.7768 0.0982 -0.0126 -0.1131 496 ASP B CA 2679 C C . ASP B 113 ? 0.8426 0.9137 0.7992 0.1030 -0.0166 -0.1250 496 ASP B C 2680 O O . ASP B 113 ? 0.8717 0.9398 0.8292 0.1071 -0.0197 -0.1386 496 ASP B O 2681 C CB . ASP B 113 ? 0.8045 0.8736 0.7685 0.1065 -0.0080 -0.1116 496 ASP B CB 2682 C CG . ASP B 113 ? 0.7957 0.8526 0.7707 0.1031 -0.0073 -0.1059 496 ASP B CG 2683 O OD1 . ASP B 113 ? 0.7856 0.8262 0.7664 0.0958 -0.0107 -0.1069 496 ASP B OD1 2684 O OD2 . ASP B 113 ? 0.8036 0.8670 0.7818 0.1081 -0.0031 -0.1002 496 ASP B OD2 2685 N N . HIS B 114 ? 0.8641 0.9451 0.8134 0.1030 -0.0174 -0.1205 497 HIS B N 2686 C CA . HIS B 114 ? 0.9064 0.9949 0.8478 0.1076 -0.0231 -0.1315 497 HIS B CA 2687 C C . HIS B 114 ? 0.9230 1.0008 0.8748 0.1039 -0.0296 -0.1461 497 HIS B C 2688 O O . HIS B 114 ? 0.9016 0.9676 0.8661 0.0945 -0.0298 -0.1440 497 HIS B O 2689 C CB . HIS B 114 ? 0.9414 1.0368 0.8790 0.1048 -0.0247 -0.1239 497 HIS B CB 2690 C CG . HIS B 114 ? 0.9878 1.0972 0.9109 0.1120 -0.0204 -0.1142 497 HIS B CG 2691 N ND1 . HIS B 114 ? 1.0244 1.1424 0.9396 0.1134 -0.0230 -0.1099 497 HIS B ND1 2692 C CD2 . HIS B 114 ? 1.0184 1.1345 0.9347 0.1184 -0.0131 -0.1076 497 HIS B CD2 2693 C CE1 . HIS B 114 ? 1.0374 1.1658 0.9402 0.1201 -0.0171 -0.1002 497 HIS B CE1 2694 N NE2 . HIS B 114 ? 1.0413 1.1693 0.9452 0.1231 -0.0105 -0.0988 497 HIS B NE2 2695 N N . LYS B 115 ? 0.9630 1.0446 0.9093 0.1115 -0.0345 -0.1609 498 LYS B N 2696 C CA . LYS B 115 ? 0.9922 1.0651 0.9501 0.1085 -0.0418 -0.1763 498 LYS B CA 2697 C C . LYS B 115 ? 1.0090 1.0907 0.9564 0.1179 -0.0497 -0.1915 498 LYS B C 2698 O O . LYS B 115 ? 1.0205 1.1114 0.9503 0.1282 -0.0477 -0.1925 498 LYS B O 2699 C CB . LYS B 115 ? 1.0292 1.0879 0.9989 0.1060 -0.0396 -0.1807 498 LYS B CB 2700 C CG . LYS B 115 ? 1.0830 1.1449 1.0444 0.1156 -0.0361 -0.1837 498 LYS B CG 2701 C CD . LYS B 115 ? 1.1255 1.1731 1.1001 0.1145 -0.0379 -0.1947 498 LYS B CD 2702 C CE . LYS B 115 ? 1.1625 1.2118 1.1319 0.1241 -0.0343 -0.1989 498 LYS B CE 2703 N NZ . LYS B 115 ? 1.1563 1.2035 1.1284 0.1226 -0.0267 -0.1837 498 LYS B NZ 2704 N N . LYS B 116 ? 1.0272 1.1060 0.9853 0.1143 -0.0585 -0.2030 499 LYS B N 2705 C CA . LYS B 116 ? 1.0563 1.1409 1.0072 0.1225 -0.0688 -0.2201 499 LYS B CA 2706 C C . LYS B 116 ? 1.0714 1.1440 1.0423 0.1185 -0.0744 -0.2361 499 LYS B C 2707 O O . LYS B 116 ? 1.0328 1.0965 1.0251 0.1080 -0.0750 -0.2356 499 LYS B O 2708 C CB . LYS B 116 ? 1.0704 1.1641 1.0185 0.1224 -0.0765 -0.2200 499 LYS B CB 2709 C CG . LYS B 116 ? 1.0894 1.1945 1.0185 0.1263 -0.0714 -0.2040 499 LYS B CG 2710 C CD . LYS B 116 ? 1.1258 1.2394 1.0285 0.1393 -0.0685 -0.2043 499 LYS B CD 2711 C CE . LYS B 116 ? 1.1435 1.2678 1.0289 0.1429 -0.0636 -0.1883 499 LYS B CE 2712 N NZ . LYS B 116 ? 1.1666 1.2975 1.0300 0.1534 -0.0551 -0.1835 499 LYS B NZ 2713 N N . GLY B 117 ? 1.1414 1.2130 1.1055 0.1271 -0.0778 -0.2500 500 GLY B N 2714 C CA . GLY B 117 ? 1.1829 1.2428 1.1661 0.1245 -0.0838 -0.2664 500 GLY B CA 2715 C C . GLY B 117 ? 1.2324 1.2943 1.2029 0.1366 -0.0894 -0.2836 500 GLY B C 2716 O O . GLY B 117 ? 1.2298 1.3006 1.1760 0.1470 -0.0855 -0.2810 500 GLY B O 2717 N N . ASP B 118 ? 1.3216 1.3747 1.3092 0.1351 -0.0982 -0.3016 501 ASP B N 2718 C CA . ASP B 118 ? 1.3882 1.4398 1.3677 0.1458 -0.1042 -0.3206 501 ASP B CA 2719 C C . ASP B 118 ? 1.4528 1.4920 1.4420 0.1449 -0.0961 -0.3201 501 ASP B C 2720 O O . ASP B 118 ? 1.4128 1.4471 1.4085 0.1381 -0.0857 -0.3034 501 ASP B O 2721 C CB . ASP B 118 ? 1.3819 1.4307 1.3761 0.1453 -0.1199 -0.3418 501 ASP B CB 2722 C CG . ASP B 118 ? 1.3635 1.3986 1.3946 0.1315 -0.1208 -0.3438 501 ASP B CG 2723 O OD1 . ASP B 118 ? 1.3691 1.4062 1.4157 0.1267 -0.1304 -0.3510 501 ASP B OD1 2724 O OD2 . ASP B 118 ? 1.3348 1.3571 1.3800 0.1254 -0.1121 -0.3379 501 ASP B OD2 2725 N N . ASP B 119 ? 1.5870 1.6211 1.5764 0.1525 -0.1018 -0.3389 502 ASP B N 2726 C CA . ASP B 119 ? 1.6635 1.6843 1.6655 0.1524 -0.0966 -0.3423 502 ASP B CA 2727 C C . ASP B 119 ? 1.6790 1.6841 1.7102 0.1384 -0.0923 -0.3334 502 ASP B C 2728 O O . ASP B 119 ? 1.6879 1.6845 1.7235 0.1367 -0.0835 -0.3237 502 ASP B O 2729 C CB . ASP B 119 ? 1.7053 1.7209 1.7104 0.1603 -0.1073 -0.3680 502 ASP B CB 2730 C CG . ASP B 119 ? 1.7498 1.7595 1.7505 0.1687 -0.1013 -0.3732 502 ASP B CG 2731 O OD1 . ASP B 119 ? 1.7970 1.7923 1.8187 0.1665 -0.1049 -0.3852 502 ASP B OD1 2732 O OD2 . ASP B 119 ? 1.7633 1.7827 1.7411 0.1778 -0.0927 -0.3659 502 ASP B OD2 2733 N N . PHE B 120 ? 1.7046 1.7049 1.7557 0.1289 -0.0989 -0.3376 503 PHE B N 2734 C CA . PHE B 120 ? 1.7089 1.6929 1.7877 0.1157 -0.0948 -0.3311 503 PHE B CA 2735 C C . PHE B 120 ? 1.6520 1.6383 1.7313 0.1060 -0.0873 -0.3104 503 PHE B C 2736 O O . PHE B 120 ? 1.6099 1.5872 1.6912 0.1004 -0.0775 -0.2945 503 PHE B O 2737 C CB . PHE B 120 ? 1.7555 1.7317 1.8607 0.1107 -0.1056 -0.3493 503 PHE B CB 2738 C CG . PHE B 120 ? 1.8367 1.8041 1.9496 0.1174 -0.1122 -0.3694 503 PHE B CG 2739 C CD1 . PHE B 120 ? 1.8592 1.8131 1.9770 0.1182 -0.1053 -0.3666 503 PHE B CD1 2740 C CD2 . PHE B 120 ? 1.8755 1.8475 1.9919 0.1230 -0.1265 -0.3921 503 PHE B CD2 2741 C CE1 . PHE B 120 ? 1.8768 1.8221 2.0028 0.1246 -0.1114 -0.3856 503 PHE B CE1 2742 C CE2 . PHE B 120 ? 1.8885 1.8516 2.0122 0.1293 -0.1332 -0.4118 503 PHE B CE2 2743 C CZ . PHE B 120 ? 1.8911 1.8408 2.0200 0.1300 -0.1252 -0.4085 503 PHE B CZ 2744 N N . PHE B 121 ? 1.5872 1.5853 1.6635 0.1048 -0.0927 -0.3113 504 PHE B N 2745 C CA . PHE B 121 ? 1.5024 1.5009 1.5870 0.0941 -0.0879 -0.2966 504 PHE B CA 2746 C C . PHE B 121 ? 1.3807 1.3928 1.4423 0.0966 -0.0826 -0.2801 504 PHE B C 2747 O O . PHE B 121 ? 1.3604 1.3858 1.3996 0.1070 -0.0854 -0.2824 504 PHE B O 2748 C CB . PHE B 121 ? 1.5437 1.5451 1.6478 0.0895 -0.0979 -0.3090 504 PHE B CB 2749 C CG . PHE B 121 ? 1.6100 1.5966 1.7440 0.0835 -0.1016 -0.3225 504 PHE B CG 2750 C CD1 . PHE B 121 ? 1.6248 1.5948 1.7790 0.0720 -0.0920 -0.3127 504 PHE B CD1 2751 C CD2 . PHE B 121 ? 1.6534 1.6418 1.7953 0.0895 -0.1148 -0.3450 504 PHE B CD2 2752 C CE1 . PHE B 121 ? 1.6510 1.6065 1.8342 0.0661 -0.0943 -0.3240 504 PHE B CE1 2753 C CE2 . PHE B 121 ? 1.6762 1.6505 1.8487 0.0835 -0.1183 -0.3576 504 PHE B CE2 2754 C CZ . PHE B 121 ? 1.6693 1.6272 1.8633 0.0716 -0.1075 -0.3465 504 PHE B CZ 2755 N N . VAL B 122 ? 1.2499 1.2574 1.3175 0.0868 -0.0745 -0.2636 505 VAL B N 2756 C CA . VAL B 122 ? 1.1316 1.1499 1.1825 0.0869 -0.0694 -0.2473 505 VAL B CA 2757 C C . VAL B 122 ? 1.0361 1.0616 1.0963 0.0821 -0.0744 -0.2487 505 VAL B C 2758 O O . VAL B 122 ? 0.9817 0.9980 1.0637 0.0720 -0.0727 -0.2485 505 VAL B O 2759 C CB . VAL B 122 ? 1.1119 1.1193 1.1629 0.0797 -0.0579 -0.2286 505 VAL B CB 2760 C CG1 . VAL B 122 ? 1.0884 1.1064 1.1245 0.0793 -0.0533 -0.2126 505 VAL B CG1 2761 C CG2 . VAL B 122 ? 1.1206 1.1203 1.1659 0.0845 -0.0540 -0.2275 505 VAL B CG2 2762 N N . TYR B 123 ? 0.9992 1.0407 1.0432 0.0894 -0.0800 -0.2497 506 TYR B N 2763 C CA . TYR B 123 ? 0.9932 1.0429 1.0450 0.0859 -0.0856 -0.2501 506 TYR B CA 2764 C C . TYR B 123 ? 0.9338 0.9840 0.9834 0.0791 -0.0762 -0.2307 506 TYR B C 2765 O O . TYR B 123 ? 0.9025 0.9496 0.9701 0.0703 -0.0749 -0.2281 506 TYR B O 2766 C CB . TYR B 123 ? 1.0293 1.0950 1.0623 0.0972 -0.0960 -0.2576 506 TYR B CB 2767 C CG . TYR B 123 ? 1.0786 1.1450 1.1064 0.1066 -0.1061 -0.2772 506 TYR B CG 2768 C CD1 . TYR B 123 ? 1.0993 1.1554 1.1512 0.1025 -0.1118 -0.2930 506 TYR B CD1 2769 C CD2 . TYR B 123 ? 1.1136 1.1905 1.1121 0.1197 -0.1098 -0.2802 506 TYR B CD2 2770 C CE1 . TYR B 123 ? 1.1452 1.2014 1.1923 0.1114 -0.1219 -0.3122 506 TYR B CE1 2771 C CE2 . TYR B 123 ? 1.1555 1.2324 1.1466 0.1291 -0.1191 -0.2991 506 TYR B CE2 2772 C CZ . TYR B 123 ? 1.1671 1.2336 1.1827 0.1250 -0.1257 -0.3156 506 TYR B CZ 2773 O OH . TYR B 123 ? 1.2108 1.2767 1.2190 0.1346 -0.1356 -0.3354 506 TYR B OH 2774 N N . ALA B 124 ? 0.8961 0.9506 0.9243 0.0836 -0.0696 -0.2176 507 ALA B N 2775 C CA . ALA B 124 ? 0.8622 0.9176 0.8855 0.0785 -0.0615 -0.1995 507 ALA B CA 2776 C C . ALA B 124 ? 0.8492 0.9007 0.8590 0.0805 -0.0528 -0.1877 507 ALA B C 2777 O O . ALA B 124 ? 0.8447 0.9007 0.8420 0.0893 -0.0536 -0.1917 507 ALA B O 2778 C CB . ALA B 124 ? 0.8517 0.9227 0.8630 0.0835 -0.0660 -0.1956 507 ALA B CB 2779 N N . ASP B 125 ? 0.8082 0.8511 0.8215 0.0727 -0.0448 -0.1738 508 ASP B N 2780 C CA . ASP B 125 ? 0.7836 0.8233 0.7863 0.0739 -0.0377 -0.1612 508 ASP B CA 2781 C C . ASP B 125 ? 0.7592 0.7938 0.7627 0.0659 -0.0317 -0.1459 508 ASP B C 2782 O O . ASP B 125 ? 0.7582 0.7960 0.7670 0.0616 -0.0327 -0.1447 508 ASP B O 2783 C CB . ASP B 125 ? 0.7850 0.8111 0.7937 0.0736 -0.0360 -0.1661 508 ASP B CB 2784 C CG . ASP B 125 ? 0.7857 0.7940 0.8108 0.0634 -0.0337 -0.1670 508 ASP B CG 2785 O OD1 . ASP B 125 ? 0.7708 0.7780 0.8047 0.0566 -0.0332 -0.1657 508 ASP B OD1 2786 O OD2 . ASP B 125 ? 0.8090 0.8040 0.8388 0.0625 -0.0318 -0.1686 508 ASP B OD2 2787 N N . TYR B 126 ? 0.7377 0.7645 0.7366 0.0642 -0.0261 -0.1350 509 TYR B N 2788 C CA . TYR B 126 ? 0.7211 0.7427 0.7181 0.0577 -0.0212 -0.1210 509 TYR B CA 2789 C C . TYR B 126 ? 0.7241 0.7328 0.7322 0.0480 -0.0188 -0.1212 509 TYR B C 2790 O O . TYR B 126 ? 0.7054 0.7144 0.7127 0.0435 -0.0161 -0.1133 509 TYR B O 2791 C CB . TYR B 126 ? 0.7197 0.7342 0.7106 0.0584 -0.0176 -0.1109 509 TYR B CB 2792 C CG . TYR B 126 ? 0.7420 0.7363 0.7382 0.0533 -0.0155 -0.1109 509 TYR B CG 2793 C CD1 . TYR B 126 ? 0.7505 0.7387 0.7520 0.0563 -0.0174 -0.1208 509 TYR B CD1 2794 C CD2 . TYR B 126 ? 0.7259 0.7058 0.7204 0.0460 -0.0118 -0.1009 509 TYR B CD2 2795 C CE1 . TYR B 126 ? 0.7527 0.7211 0.7588 0.0519 -0.0156 -0.1196 509 TYR B CE1 2796 C CE2 . TYR B 126 ? 0.7385 0.6984 0.7350 0.0420 -0.0099 -0.0998 509 TYR B CE2 2797 C CZ . TYR B 126 ? 0.7542 0.7083 0.7569 0.0448 -0.0117 -0.1087 509 TYR B CZ 2798 O OH . TYR B 126 ? 0.7617 0.6947 0.7660 0.0411 -0.0098 -0.1066 509 TYR B OH 2799 N N . HIS B 127 ? 0.7323 0.7295 0.7514 0.0449 -0.0191 -0.1304 510 HIS B N 2800 C CA . HIS B 127 ? 0.7335 0.7189 0.7658 0.0359 -0.0155 -0.1319 510 HIS B CA 2801 C C . HIS B 127 ? 0.7345 0.7327 0.7749 0.0349 -0.0184 -0.1364 510 HIS B C 2802 O O . HIS B 127 ? 0.7131 0.7077 0.7579 0.0287 -0.0139 -0.1307 510 HIS B O 2803 C CB . HIS B 127 ? 0.7502 0.7239 0.7964 0.0336 -0.0161 -0.1429 510 HIS B CB 2804 C CG . HIS B 127 ? 0.7663 0.7267 0.8072 0.0352 -0.0144 -0.1403 510 HIS B CG 2805 N ND1 . HIS B 127 ? 0.7728 0.7368 0.8139 0.0424 -0.0194 -0.1495 510 HIS B ND1 2806 C CD2 . HIS B 127 ? 0.7695 0.7125 0.8044 0.0312 -0.0089 -0.1299 510 HIS B CD2 2807 C CE1 . HIS B 127 ? 0.7683 0.7182 0.8059 0.0425 -0.0169 -0.1447 510 HIS B CE1 2808 N NE2 . HIS B 127 ? 0.7795 0.7163 0.8126 0.0359 -0.0111 -0.1326 510 HIS B NE2 2809 N N . THR B 128 ? 0.7465 0.7588 0.7887 0.0416 -0.0264 -0.1473 511 THR B N 2810 C CA . THR B 128 ? 0.7413 0.7665 0.7912 0.0423 -0.0318 -0.1531 511 THR B CA 2811 C C . THR B 128 ? 0.7092 0.7432 0.7488 0.0429 -0.0299 -0.1410 511 THR B C 2812 O O . THR B 128 ? 0.6983 0.7342 0.7475 0.0384 -0.0291 -0.1396 511 THR B O 2813 C CB . THR B 128 ? 0.7551 0.7933 0.8025 0.0514 -0.0420 -0.1662 511 THR B CB 2814 O OG1 . THR B 128 ? 0.7837 0.8129 0.8377 0.0520 -0.0434 -0.1765 511 THR B OG1 2815 C CG2 . THR B 128 ? 0.7673 0.8153 0.8282 0.0511 -0.0495 -0.1753 511 THR B CG2 2816 N N . HIS B 129 ? 0.6992 0.7383 0.7211 0.0485 -0.0289 -0.1324 512 HIS B N 2817 C CA . HIS B 129 ? 0.6900 0.7366 0.7024 0.0492 -0.0270 -0.1201 512 HIS B CA 2818 C C . HIS B 129 ? 0.6765 0.7107 0.6930 0.0403 -0.0197 -0.1105 512 HIS B C 2819 O O . HIS B 129 ? 0.6747 0.7128 0.6951 0.0377 -0.0190 -0.1066 512 HIS B O 2820 C CB . HIS B 129 ? 0.6881 0.7412 0.6841 0.0562 -0.0261 -0.1127 512 HIS B CB 2821 C CG . HIS B 129 ? 0.6821 0.7455 0.6699 0.0584 -0.0253 -0.1015 512 HIS B CG 2822 N ND1 . HIS B 129 ? 0.6848 0.7611 0.6713 0.0624 -0.0303 -0.1036 512 HIS B ND1 2823 C CD2 . HIS B 129 ? 0.6839 0.7462 0.6655 0.0571 -0.0206 -0.0882 512 HIS B CD2 2824 C CE1 . HIS B 129 ? 0.6765 0.7587 0.6561 0.0634 -0.0280 -0.0914 512 HIS B CE1 2825 N NE2 . HIS B 129 ? 0.6811 0.7552 0.6585 0.0600 -0.0221 -0.0822 512 HIS B NE2 2826 N N . PHE B 130 ? 0.6593 0.6777 0.6744 0.0363 -0.0146 -0.1072 513 PHE B N 2827 C CA . PHE B 130 ? 0.6546 0.6579 0.6704 0.0282 -0.0074 -0.0991 513 PHE B CA 2828 C C . PHE B 130 ? 0.6613 0.6617 0.6919 0.0219 -0.0047 -0.1035 513 PHE B C 2829 O O . PHE B 130 ? 0.6748 0.6748 0.7052 0.0185 -0.0011 -0.0970 513 PHE B O 2830 C CB . PHE B 130 ? 0.6502 0.6353 0.6626 0.0256 -0.0038 -0.0976 513 PHE B CB 2831 C CG . PHE B 130 ? 0.6371 0.6040 0.6459 0.0181 0.0034 -0.0893 513 PHE B CG 2832 C CD1 . PHE B 130 ? 0.6221 0.5844 0.6173 0.0181 0.0046 -0.0779 513 PHE B CD1 2833 C CD2 . PHE B 130 ? 0.6347 0.5883 0.6535 0.0114 0.0092 -0.0931 513 PHE B CD2 2834 C CE1 . PHE B 130 ? 0.6325 0.5769 0.6213 0.0121 0.0106 -0.0711 513 PHE B CE1 2835 C CE2 . PHE B 130 ? 0.6469 0.5826 0.6592 0.0052 0.0170 -0.0853 513 PHE B CE2 2836 C CZ . PHE B 130 ? 0.6473 0.5779 0.6428 0.0059 0.0172 -0.0746 513 PHE B CZ 2837 N N . LEU B 131 ? 0.6658 0.6646 0.7112 0.0204 -0.0062 -0.1150 514 LEU B N 2838 C CA . LEU B 131 ? 0.6523 0.6481 0.7167 0.0140 -0.0028 -0.1202 514 LEU B CA 2839 C C . LEU B 131 ? 0.6385 0.6507 0.7099 0.0160 -0.0075 -0.1218 514 LEU B C 2840 O O . LEU B 131 ? 0.6345 0.6444 0.7184 0.0106 -0.0026 -0.1212 514 LEU B O 2841 C CB . LEU B 131 ? 0.6635 0.6548 0.7453 0.0122 -0.0044 -0.1328 514 LEU B CB 2842 C CG . LEU B 131 ? 0.6853 0.6565 0.7642 0.0083 0.0019 -0.1305 514 LEU B CG 2843 C CD1 . LEU B 131 ? 0.7023 0.6715 0.7976 0.0085 -0.0020 -0.1438 514 LEU B CD1 2844 C CD2 . LEU B 131 ? 0.6883 0.6423 0.7692 -0.0003 0.0139 -0.1226 514 LEU B CD2 2845 N N . TYR B 132 ? 0.6407 0.6689 0.7038 0.0242 -0.0163 -0.1235 515 TYR B N 2846 C CA . TYR B 132 ? 0.6468 0.6898 0.7124 0.0273 -0.0213 -0.1225 515 TYR B CA 2847 C C . TYR B 132 ? 0.6480 0.6893 0.7020 0.0259 -0.0159 -0.1083 515 TYR B C 2848 O O . TYR B 132 ? 0.6246 0.6671 0.6874 0.0225 -0.0135 -0.1057 515 TYR B O 2849 C CB . TYR B 132 ? 0.6508 0.7097 0.7080 0.0372 -0.0321 -0.1282 515 TYR B CB 2850 C CG . TYR B 132 ? 0.6573 0.7303 0.7129 0.0415 -0.0377 -0.1250 515 TYR B CG 2851 C CD1 . TYR B 132 ? 0.6567 0.7346 0.6954 0.0451 -0.0361 -0.1125 515 TYR B CD1 2852 C CD2 . TYR B 132 ? 0.6578 0.7387 0.7306 0.0418 -0.0447 -0.1341 515 TYR B CD2 2853 C CE1 . TYR B 132 ? 0.6522 0.7417 0.6895 0.0491 -0.0408 -0.1083 515 TYR B CE1 2854 C CE2 . TYR B 132 ? 0.6594 0.7524 0.7306 0.0463 -0.0504 -0.1304 515 TYR B CE2 2855 C CZ . TYR B 132 ? 0.6541 0.7508 0.7067 0.0499 -0.0482 -0.1172 515 TYR B CZ 2856 O OH . TYR B 132 ? 0.6567 0.7642 0.7076 0.0544 -0.0536 -0.1126 515 TYR B OH 2857 N N . CYS B 133 ? 0.6415 0.6801 0.6776 0.0285 -0.0142 -0.0997 516 CYS B N 2858 C CA . CYS B 133 ? 0.6361 0.6743 0.6619 0.0280 -0.0109 -0.0868 516 CYS B CA 2859 C C . CYS B 133 ? 0.6512 0.6749 0.6805 0.0199 -0.0026 -0.0815 516 CYS B C 2860 O O . CYS B 133 ? 0.6495 0.6753 0.6777 0.0190 -0.0011 -0.0747 516 CYS B O 2861 C CB . CYS B 133 ? 0.6326 0.6705 0.6423 0.0322 -0.0109 -0.0795 516 CYS B CB 2862 S SG . CYS B 133 ? 0.6381 0.6950 0.6387 0.0430 -0.0182 -0.0814 516 CYS B SG 2863 N N . VAL B 134 ? 0.6630 0.6713 0.6960 0.0144 0.0031 -0.0847 517 VAL B N 2864 C CA . VAL B 134 ? 0.6687 0.6619 0.7035 0.0071 0.0121 -0.0806 517 VAL B CA 2865 C C . VAL B 134 ? 0.6819 0.6810 0.7344 0.0042 0.0142 -0.0848 517 VAL B C 2866 O O . VAL B 134 ? 0.6935 0.6841 0.7460 -0.0001 0.0215 -0.0802 517 VAL B O 2867 C CB . VAL B 134 ? 0.6753 0.6489 0.7085 0.0021 0.0189 -0.0820 517 VAL B CB 2868 C CG1 . VAL B 134 ? 0.6795 0.6457 0.6951 0.0049 0.0168 -0.0763 517 VAL B CG1 2869 C CG2 . VAL B 134 ? 0.6686 0.6436 0.7201 0.0006 0.0184 -0.0936 517 VAL B CG2 2870 N N . ARG B 135 ? 0.6946 0.7075 0.7622 0.0071 0.0076 -0.0941 518 ARG B N 2871 C CA . ARG B 135 ? 0.7110 0.7325 0.7982 0.0057 0.0071 -0.0987 518 ARG B CA 2872 C C . ARG B 135 ? 0.6730 0.7101 0.7570 0.0116 -0.0002 -0.0945 518 ARG B C 2873 O O . ARG B 135 ? 0.6714 0.7128 0.7681 0.0101 0.0008 -0.0946 518 ARG B O 2874 C CB . ARG B 135 ? 0.7740 0.8016 0.8822 0.0056 0.0025 -0.1120 518 ARG B CB 2875 C CG . ARG B 135 ? 0.8510 0.8629 0.9682 -0.0009 0.0108 -0.1164 518 ARG B CG 2876 C CD . ARG B 135 ? 0.9361 0.9549 1.0708 0.0006 0.0030 -0.1299 518 ARG B CD 2877 N NE . ARG B 135 ? 1.0140 1.0187 1.1645 -0.0064 0.0114 -0.1350 518 ARG B NE 2878 C CZ . ARG B 135 ? 1.0887 1.0909 1.2652 -0.0127 0.0182 -0.1396 518 ARG B CZ 2879 N NH1 . ARG B 135 ? 1.1134 1.1265 1.3045 -0.0128 0.0173 -0.1406 518 ARG B NH1 2880 N NH2 . ARG B 135 ? 1.1298 1.1181 1.3193 -0.0190 0.0266 -0.1431 518 ARG B NH2 2881 N N . ALA B 136 ? 0.6458 0.6912 0.7137 0.0182 -0.0070 -0.0907 519 ALA B N 2882 C CA . ALA B 136 ? 0.6213 0.6810 0.6845 0.0244 -0.0138 -0.0857 519 ALA B CA 2883 C C . ALA B 136 ? 0.6123 0.6726 0.6547 0.0282 -0.0139 -0.0749 519 ALA B C 2884 O O . ALA B 136 ? 0.6357 0.7068 0.6686 0.0354 -0.0202 -0.0744 519 ALA B O 2885 C CB . ALA B 136 ? 0.6245 0.6988 0.6943 0.0308 -0.0245 -0.0951 519 ALA B CB 2886 N N . PRO B 137 ? 0.5871 0.6356 0.6225 0.0238 -0.0070 -0.0662 520 PRO B N 2887 C CA . PRO B 137 ? 0.5728 0.6208 0.5920 0.0266 -0.0070 -0.0567 520 PRO B CA 2888 C C . PRO B 137 ? 0.5611 0.6221 0.5756 0.0322 -0.0112 -0.0486 520 PRO B C 2889 O O . PRO B 137 ? 0.5687 0.6317 0.5726 0.0352 -0.0114 -0.0414 520 PRO B O 2890 C CB . PRO B 137 ? 0.5775 0.6082 0.5923 0.0200 0.0001 -0.0511 520 PRO B CB 2891 C CG . PRO B 137 ? 0.5813 0.6071 0.6085 0.0151 0.0045 -0.0547 520 PRO B CG 2892 C CD . PRO B 137 ? 0.5780 0.6122 0.6196 0.0162 0.0013 -0.0655 520 PRO B CD 2893 N N . ALA B 138 ? 0.5652 0.6345 0.5885 0.0337 -0.0143 -0.0493 521 ALA B N 2894 C CA . ALA B 138 ? 0.5723 0.6535 0.5911 0.0396 -0.0186 -0.0412 521 ALA B CA 2895 C C . ALA B 138 ? 0.5860 0.6811 0.5997 0.0478 -0.0259 -0.0454 521 ALA B C 2896 O O . ALA B 138 ? 0.6107 0.7152 0.6167 0.0538 -0.0287 -0.0379 521 ALA B O 2897 C CB . ALA B 138 ? 0.5565 0.6385 0.5867 0.0377 -0.0186 -0.0386 521 ALA B CB 2898 N N . SER B 139 ? 0.6007 0.6962 0.6179 0.0484 -0.0288 -0.0573 522 SER B N 2899 C CA . SER B 139 ? 0.6207 0.7282 0.6322 0.0566 -0.0370 -0.0638 522 SER B CA 2900 C C . SER B 139 ? 0.6304 0.7437 0.6230 0.0634 -0.0366 -0.0568 522 SER B C 2901 O O . SER B 139 ? 0.6063 0.7134 0.5932 0.0613 -0.0308 -0.0530 522 SER B O 2902 C CB . SER B 139 ? 0.6208 0.7250 0.6396 0.0551 -0.0395 -0.0783 522 SER B CB 2903 O OG . SER B 139 ? 0.6140 0.7285 0.6256 0.0634 -0.0482 -0.0859 522 SER B OG 2904 N N . LEU B 140 ? 0.6858 0.8108 0.6689 0.0719 -0.0425 -0.0549 523 LEU B N 2905 C CA . LEU B 140 ? 0.7172 0.8489 0.6814 0.0798 -0.0414 -0.0494 523 LEU B CA 2906 C C . LEU B 140 ? 0.7652 0.9000 0.7210 0.0855 -0.0459 -0.0621 523 LEU B C 2907 O O . LEU B 140 ? 0.7916 0.9312 0.7314 0.0924 -0.0439 -0.0595 523 LEU B O 2908 C CB . LEU B 140 ? 0.7179 0.8590 0.6726 0.0868 -0.0443 -0.0396 523 LEU B CB 2909 C CG . LEU B 140 ? 0.7391 0.8776 0.7022 0.0822 -0.0405 -0.0267 523 LEU B CG 2910 C CD1 . LEU B 140 ? 0.7429 0.8902 0.6965 0.0898 -0.0440 -0.0171 523 LEU B CD1 2911 C CD2 . LEU B 140 ? 0.7338 0.8658 0.6974 0.0771 -0.0311 -0.0171 523 LEU B CD2 2912 N N . ASN B 141 ? 0.8105 0.9422 0.7783 0.0827 -0.0514 -0.0760 524 ASN B N 2913 C CA . ASN B 141 ? 0.8968 1.0319 0.8587 0.0886 -0.0582 -0.0897 524 ASN B CA 2914 C C . ASN B 141 ? 0.8816 1.0088 0.8629 0.0816 -0.0601 -0.1032 524 ASN B C 2915 O O . ASN B 141 ? 0.8340 0.9613 0.8319 0.0780 -0.0648 -0.1087 524 ASN B O 2916 C CB . ASN B 141 ? 0.9973 1.1432 0.9501 0.0978 -0.0689 -0.0927 524 ASN B CB 2917 C CG . ASN B 141 ? 1.1120 1.2621 1.0515 0.1065 -0.0764 -0.1058 524 ASN B CG 2918 O OD1 . ASN B 141 ? 1.1161 1.2611 1.0582 0.1049 -0.0746 -0.1149 524 ASN B OD1 2919 N ND2 . ASN B 141 ? 1.2483 1.4071 1.1725 0.1164 -0.0854 -0.1067 524 ASN B ND2 2920 N N . ASP B 142 ? 0.9277 1.0476 0.9080 0.0796 -0.0557 -0.1076 525 ASP B N 2921 C CA . ASP B 142 ? 0.9667 1.0787 0.9626 0.0746 -0.0575 -0.1212 525 ASP B CA 2922 C C . ASP B 142 ? 0.9853 1.1049 0.9861 0.0799 -0.0699 -0.1359 525 ASP B C 2923 O O . ASP B 142 ? 0.9740 1.1027 0.9578 0.0898 -0.0767 -0.1384 525 ASP B O 2924 C CB . ASP B 142 ? 0.9910 1.0964 0.9791 0.0756 -0.0527 -0.1234 525 ASP B CB 2925 C CG . ASP B 142 ? 1.0147 1.1081 1.0195 0.0685 -0.0513 -0.1333 525 ASP B CG 2926 O OD1 . ASP B 142 ? 1.0730 1.1646 1.0959 0.0640 -0.0553 -0.1419 525 ASP B OD1 2927 O OD2 . ASP B 142 ? 1.0119 1.0971 1.0125 0.0675 -0.0460 -0.1320 525 ASP B OD2 2928 N N . THR B 143 ? 1.0038 1.1190 1.0279 0.0735 -0.0728 -0.1456 526 THR B N 2929 C CA . THR B 143 ? 1.0373 1.1591 1.0718 0.0773 -0.0857 -0.1608 526 THR B CA 2930 C C . THR B 143 ? 1.0773 1.1965 1.1080 0.0813 -0.0904 -0.1749 526 THR B C 2931 O O . THR B 143 ? 1.1166 1.2423 1.1466 0.0880 -0.1030 -0.1879 526 THR B O 2932 C CB . THR B 143 ? 1.0281 1.1466 1.0939 0.0683 -0.0859 -0.1658 526 THR B CB 2933 O OG1 . THR B 143 ? 1.0657 1.1944 1.1409 0.0733 -0.1001 -0.1764 526 THR B OG1 2934 C CG2 . THR B 143 ? 1.0333 1.1395 1.1183 0.0598 -0.0804 -0.1742 526 THR B CG2 2935 N N . SER B 144 ? 1.0731 1.1822 1.1016 0.0775 -0.0811 -0.1726 527 SER B N 2936 C CA . SER B 144 ? 1.0766 1.1818 1.1012 0.0813 -0.0841 -0.1848 527 SER B CA 2937 C C . SER B 144 ? 1.0570 1.1713 1.0535 0.0939 -0.0887 -0.1858 527 SER B C 2938 O O . SER B 144 ? 1.0360 1.1595 1.0160 0.0998 -0.0899 -0.1769 527 SER B O 2939 C CB . SER B 144 ? 1.0940 1.1855 1.1225 0.0745 -0.0726 -0.1798 527 SER B CB 2940 O OG . SER B 144 ? 1.0956 1.1881 1.1023 0.0789 -0.0658 -0.1683 527 SER B OG 2941 N N . LEU B 145 ? 1.0695 1.1802 1.0602 0.0983 -0.0903 -0.1962 528 LEU B N 2942 C CA . LEU B 145 ? 1.1012 1.2192 1.0649 0.1109 -0.0936 -0.1994 528 LEU B CA 2943 C C . LEU B 145 ? 1.0804 1.2006 1.0243 0.1139 -0.0818 -0.1828 528 LEU B C 2944 O O . LEU B 145 ? 1.0717 1.1995 0.9917 0.1245 -0.0821 -0.1817 528 LEU B O 2945 C CB . LEU B 145 ? 1.1487 1.2614 1.1142 0.1145 -0.0983 -0.2167 528 LEU B CB 2946 C CG . LEU B 145 ? 1.1942 1.3056 1.1789 0.1134 -0.1119 -0.2359 528 LEU B CG 2947 C CD1 . LEU B 145 ? 1.1922 1.2913 1.2088 0.1011 -0.1083 -0.2402 528 LEU B CD1 2948 C CD2 . LEU B 145 ? 1.2419 1.3554 1.2111 0.1248 -0.1213 -0.2527 528 LEU B CD2 2949 N N . LEU B 146 ? 1.0410 1.1541 0.9949 0.1049 -0.0713 -0.1703 529 LEU B N 2950 C CA . LEU B 146 ? 1.0127 1.1274 0.9533 0.1064 -0.0607 -0.1545 529 LEU B CA 2951 C C . LEU B 146 ? 0.9703 1.0954 0.8981 0.1101 -0.0601 -0.1419 529 LEU B C 2952 O O . LEU B 146 ? 0.9242 1.0559 0.8338 0.1172 -0.0551 -0.1338 529 LEU B O 2953 C CB . LEU B 146 ? 1.0114 1.1145 0.9667 0.0957 -0.0519 -0.1456 529 LEU B CB 2954 C CG . LEU B 146 ? 1.0272 1.1173 0.9955 0.0911 -0.0508 -0.1550 529 LEU B CG 2955 C CD1 . LEU B 146 ? 1.0050 1.0826 0.9854 0.0804 -0.0432 -0.1449 529 LEU B CD1 2956 C CD2 . LEU B 146 ? 1.0365 1.1273 0.9934 0.0991 -0.0489 -0.1596 529 LEU B CD2 2957 N N . HIS B 147 ? 0.9881 1.1143 0.9269 0.1052 -0.0646 -0.1402 530 HIS B N 2958 C CA . HIS B 147 ? 1.0116 1.1459 0.9421 0.1074 -0.0646 -0.1277 530 HIS B CA 2959 C C . HIS B 147 ? 0.9682 1.1020 0.8936 0.1051 -0.0531 -0.1097 530 HIS B C 2960 O O . HIS B 147 ? 1.0365 1.1783 0.9471 0.1110 -0.0509 -0.0992 530 HIS B O 2961 C CB . HIS B 147 ? 1.0522 1.1971 0.9613 0.1198 -0.0727 -0.1319 530 HIS B CB 2962 C CG . HIS B 147 ? 1.1095 1.2555 1.0244 0.1227 -0.0865 -0.1500 530 HIS B CG 2963 N ND1 . HIS B 147 ? 1.1740 1.3222 1.0742 0.1320 -0.0931 -0.1636 530 HIS B ND1 2964 C CD2 . HIS B 147 ? 1.1194 1.2647 1.0548 0.1174 -0.0951 -0.1573 530 HIS B CD2 2965 C CE1 . HIS B 147 ? 1.1959 1.3445 1.1073 0.1324 -0.1065 -0.1788 530 HIS B CE1 2966 N NE2 . HIS B 147 ? 1.1733 1.3207 1.1075 0.1234 -0.1077 -0.1751 530 HIS B NE2 2967 N N . ASP B 148 ? 0.8706 0.9944 0.8083 0.0966 -0.0461 -0.1063 531 ASP B N 2968 C CA . ASP B 148 ? 0.8101 0.9318 0.7466 0.0933 -0.0368 -0.0907 531 ASP B CA 2969 C C . ASP B 148 ? 0.7448 0.8634 0.6925 0.0855 -0.0359 -0.0822 531 ASP B C 2970 O O . ASP B 148 ? 0.7116 0.8257 0.6722 0.0802 -0.0399 -0.0893 531 ASP B O 2971 C CB . ASP B 148 ? 0.8221 0.9335 0.7648 0.0889 -0.0311 -0.0916 531 ASP B CB 2972 C CG . ASP B 148 ? 0.8452 0.9604 0.7766 0.0971 -0.0290 -0.0957 531 ASP B CG 2973 O OD1 . ASP B 148 ? 0.8475 0.9732 0.7644 0.1053 -0.0268 -0.0902 531 ASP B OD1 2974 O OD2 . ASP B 148 ? 0.8740 0.9809 0.8113 0.0955 -0.0287 -0.1038 531 ASP B OD2 2975 N N . PRO B 149 ? 0.6907 0.8114 0.6349 0.0847 -0.0303 -0.0673 532 PRO B N 2976 C CA . PRO B 149 ? 0.6626 0.7788 0.6176 0.0773 -0.0291 -0.0599 532 PRO B CA 2977 C C . PRO B 149 ? 0.6428 0.7447 0.6089 0.0678 -0.0247 -0.0599 532 PRO B C 2978 O O . PRO B 149 ? 0.6456 0.7418 0.6098 0.0673 -0.0215 -0.0610 532 PRO B O 2979 C CB . PRO B 149 ? 0.6648 0.7873 0.6124 0.0802 -0.0248 -0.0446 532 PRO B CB 2980 C CG . PRO B 149 ? 0.6687 0.7956 0.6055 0.0863 -0.0205 -0.0426 532 PRO B CG 2981 C CD . PRO B 149 ? 0.6768 0.8025 0.6105 0.0895 -0.0238 -0.0572 532 PRO B CD 2982 N N . CYS B 150 ? 0.6108 0.7065 0.5877 0.0609 -0.0244 -0.0589 533 CYS B N 2983 C CA . CYS B 150 ? 0.5948 0.6757 0.5785 0.0522 -0.0192 -0.0564 533 CYS B CA 2984 C C . CYS B 150 ? 0.5874 0.6656 0.5690 0.0496 -0.0152 -0.0429 533 CYS B C 2985 O O . CYS B 150 ? 0.5984 0.6648 0.5799 0.0448 -0.0116 -0.0393 533 CYS B O 2986 C CB . CYS B 150 ? 0.5986 0.6732 0.5954 0.0461 -0.0197 -0.0635 533 CYS B CB 2987 S SG . CYS B 150 ? 0.6395 0.7136 0.6441 0.0469 -0.0241 -0.0802 533 CYS B SG 2988 N N . LEU B 151 ? 0.5911 0.6793 0.5708 0.0531 -0.0165 -0.0355 534 LEU B N 2989 C CA . LEU B 151 ? 0.5918 0.6779 0.5726 0.0505 -0.0136 -0.0233 534 LEU B CA 2990 C C . LEU B 151 ? 0.5899 0.6734 0.5664 0.0509 -0.0103 -0.0164 534 LEU B C 2991 O O . LEU B 151 ? 0.6101 0.7013 0.5807 0.0568 -0.0100 -0.0168 534 LEU B O 2992 C CB . LEU B 151 ? 0.5977 0.6961 0.5768 0.0557 -0.0158 -0.0163 534 LEU B CB 2993 C CG . LEU B 151 ? 0.5931 0.6887 0.5781 0.0521 -0.0140 -0.0058 534 LEU B CG 2994 C CD1 . LEU B 151 ? 0.5856 0.6749 0.5803 0.0471 -0.0152 -0.0110 534 LEU B CD1 2995 C CD2 . LEU B 151 ? 0.5872 0.6947 0.5683 0.0584 -0.0148 0.0040 534 LEU B CD2 2996 N N . GLY B 152 ? 0.5887 0.6615 0.5686 0.0451 -0.0082 -0.0106 535 GLY B N 2997 C CA . GLY B 152 ? 0.6047 0.6746 0.5836 0.0451 -0.0065 -0.0041 535 GLY B CA 2998 C C . GLY B 152 ? 0.6047 0.6874 0.5844 0.0500 -0.0052 0.0061 535 GLY B C 2999 O O . GLY B 152 ? 0.6085 0.6988 0.5888 0.0520 -0.0056 0.0101 535 GLY B O 3000 N N . THR B 153 ? 0.6020 0.6866 0.5831 0.0518 -0.0033 0.0109 536 THR B N 3001 C CA . THR B 153 ? 0.6121 0.7093 0.5955 0.0566 -0.0001 0.0211 536 THR B CA 3002 C C . THR B 153 ? 0.6088 0.7050 0.6005 0.0531 0.0000 0.0316 536 THR B C 3003 O O . THR B 153 ? 0.6134 0.7199 0.6077 0.0567 0.0031 0.0410 536 THR B O 3004 C CB . THR B 153 ? 0.6205 0.7201 0.6076 0.0591 0.0024 0.0236 536 THR B CB 3005 O OG1 . THR B 153 ? 0.6231 0.7111 0.6185 0.0531 0.0000 0.0263 536 THR B OG1 3006 C CG2 . THR B 153 ? 0.6304 0.7304 0.6105 0.0630 0.0024 0.0130 536 THR B CG2 3007 N N . PHE B 154 ? 0.5975 0.6803 0.5927 0.0463 -0.0029 0.0301 537 PHE B N 3008 C CA . PHE B 154 ? 0.5919 0.6715 0.5950 0.0425 -0.0037 0.0379 537 PHE B CA 3009 C C . PHE B 154 ? 0.5940 0.6776 0.5963 0.0433 -0.0041 0.0384 537 PHE B C 3010 O O . PHE B 154 ? 0.5927 0.6740 0.6021 0.0408 -0.0047 0.0449 537 PHE B O 3011 C CB . PHE B 154 ? 0.5809 0.6434 0.5860 0.0357 -0.0068 0.0355 537 PHE B CB 3012 C CG . PHE B 154 ? 0.5848 0.6358 0.5825 0.0321 -0.0076 0.0257 537 PHE B CG 3013 C CD1 . PHE B 154 ? 0.5768 0.6210 0.5676 0.0317 -0.0077 0.0176 537 PHE B CD1 3014 C CD2 . PHE B 154 ? 0.5873 0.6339 0.5866 0.0292 -0.0077 0.0249 537 PHE B CD2 3015 C CE1 . PHE B 154 ? 0.5884 0.6218 0.5742 0.0281 -0.0071 0.0094 537 PHE B CE1 3016 C CE2 . PHE B 154 ? 0.5883 0.6249 0.5831 0.0258 -0.0069 0.0161 537 PHE B CE2 3017 C CZ . PHE B 154 ? 0.5848 0.6147 0.5729 0.0251 -0.0062 0.0087 537 PHE B CZ 3018 N N . GLY B 155 ? 0.5823 0.6712 0.5772 0.0468 -0.0048 0.0310 538 GLY B N 3019 C CA . GLY B 155 ? 0.5798 0.6746 0.5746 0.0491 -0.0064 0.0315 538 GLY B CA 3020 C C . GLY B 155 ? 0.5736 0.6596 0.5718 0.0444 -0.0086 0.0234 538 GLY B C 3021 O O . GLY B 155 ? 0.5689 0.6589 0.5704 0.0457 -0.0105 0.0238 538 GLY B O 3022 N N . GLY B 156 ? 0.5745 0.6482 0.5721 0.0392 -0.0080 0.0162 539 GLY B N 3023 C CA . GLY B 156 ? 0.5655 0.6299 0.5663 0.0345 -0.0079 0.0083 539 GLY B CA 3024 C C . GLY B 156 ? 0.5615 0.6189 0.5585 0.0324 -0.0070 -0.0020 539 GLY B C 3025 O O . GLY B 156 ? 0.5521 0.6086 0.5435 0.0337 -0.0068 -0.0029 539 GLY B O 3026 N N . PRO B 157 ? 0.5733 0.6251 0.5750 0.0291 -0.0059 -0.0098 540 PRO B N 3027 C CA . PRO B 157 ? 0.5674 0.6116 0.5677 0.0266 -0.0042 -0.0193 540 PRO B CA 3028 C C . PRO B 157 ? 0.5602 0.5872 0.5540 0.0215 -0.0007 -0.0182 540 PRO B C 3029 O O . PRO B 157 ? 0.5921 0.6109 0.5843 0.0186 0.0003 -0.0125 540 PRO B O 3030 C CB . PRO B 157 ? 0.5828 0.6267 0.5935 0.0242 -0.0031 -0.0263 540 PRO B CB 3031 C CG . PRO B 157 ? 0.5881 0.6304 0.6031 0.0227 -0.0022 -0.0197 540 PRO B CG 3032 C CD . PRO B 157 ? 0.5699 0.6213 0.5805 0.0272 -0.0055 -0.0098 540 PRO B CD 3033 N N . VAL B 158 ? 0.5568 0.5775 0.5463 0.0208 0.0001 -0.0236 541 VAL B N 3034 C CA . VAL B 158 ? 0.5579 0.5605 0.5394 0.0165 0.0028 -0.0232 541 VAL B CA 3035 C C . VAL B 158 ? 0.5734 0.5657 0.5579 0.0120 0.0078 -0.0312 541 VAL B C 3036 O O . VAL B 158 ? 0.5914 0.5875 0.5806 0.0131 0.0076 -0.0384 541 VAL B O 3037 C CB . VAL B 158 ? 0.5676 0.5703 0.5432 0.0195 0.0003 -0.0226 541 VAL B CB 3038 C CG1 . VAL B 158 ? 0.5835 0.5661 0.5501 0.0156 0.0019 -0.0223 541 VAL B CG1 3039 C CG2 . VAL B 158 ? 0.5636 0.5777 0.5395 0.0238 -0.0031 -0.0144 541 VAL B CG2 3040 N N . PHE B 159 ? 0.5731 0.5521 0.5555 0.0072 0.0127 -0.0303 542 PHE B N 3041 C CA . PHE B 159 ? 0.5943 0.5634 0.5811 0.0027 0.0196 -0.0370 542 PHE B CA 3042 C C . PHE B 159 ? 0.6116 0.5642 0.5885 0.0003 0.0227 -0.0385 542 PHE B C 3043 O O . PHE B 159 ? 0.6437 0.5837 0.6063 0.0000 0.0218 -0.0332 542 PHE B O 3044 C CB . PHE B 159 ? 0.6095 0.5700 0.5971 -0.0010 0.0253 -0.0356 542 PHE B CB 3045 C CG . PHE B 159 ? 0.6008 0.5767 0.6012 0.0012 0.0227 -0.0351 542 PHE B CG 3046 C CD1 . PHE B 159 ? 0.6011 0.5907 0.6177 0.0026 0.0215 -0.0415 542 PHE B CD1 3047 C CD2 . PHE B 159 ? 0.6070 0.5835 0.6042 0.0021 0.0204 -0.0284 542 PHE B CD2 3048 C CE1 . PHE B 159 ? 0.5965 0.5999 0.6244 0.0054 0.0179 -0.0406 542 PHE B CE1 3049 C CE2 . PHE B 159 ? 0.5966 0.5864 0.6058 0.0044 0.0178 -0.0271 542 PHE B CE2 3050 C CZ . PHE B 159 ? 0.6087 0.6120 0.6325 0.0064 0.0164 -0.0329 542 PHE B CZ 3051 N N . PRO B 160 ? 0.6144 0.5664 0.5994 -0.0009 0.0256 -0.0459 543 PRO B N 3052 C CA . PRO B 160 ? 0.6214 0.5591 0.5986 -0.0023 0.0276 -0.0471 543 PRO B CA 3053 C C . PRO B 160 ? 0.6208 0.5341 0.5817 -0.0065 0.0339 -0.0424 543 PRO B C 3054 O O . PRO B 160 ? 0.6247 0.5263 0.5727 -0.0057 0.0318 -0.0392 543 PRO B O 3055 C CB . PRO B 160 ? 0.6281 0.5697 0.6217 -0.0040 0.0306 -0.0564 543 PRO B CB 3056 C CG . PRO B 160 ? 0.6292 0.5788 0.6365 -0.0059 0.0339 -0.0591 543 PRO B CG 3057 C CD . PRO B 160 ? 0.6085 0.5708 0.6121 -0.0018 0.0275 -0.0535 543 PRO B CD 3058 N N . TRP B 161 ? 0.6317 0.5373 0.5927 -0.0104 0.0416 -0.0422 544 TRP B N 3059 C CA . TRP B 161 ? 0.6434 0.5249 0.5857 -0.0138 0.0484 -0.0380 544 TRP B CA 3060 C C . TRP B 161 ? 0.6452 0.5195 0.5687 -0.0114 0.0414 -0.0307 544 TRP B C 3061 O O . TRP B 161 ? 0.6924 0.5453 0.5965 -0.0128 0.0440 -0.0272 544 TRP B O 3062 C CB . TRP B 161 ? 0.6420 0.5183 0.5896 -0.0178 0.0591 -0.0401 544 TRP B CB 3063 C CG . TRP B 161 ? 0.6500 0.5404 0.6060 -0.0162 0.0559 -0.0395 544 TRP B CG 3064 C CD1 . TRP B 161 ? 0.6501 0.5355 0.5935 -0.0151 0.0530 -0.0344 544 TRP B CD1 3065 C CD2 . TRP B 161 ? 0.6375 0.5485 0.6167 -0.0152 0.0545 -0.0443 544 TRP B CD2 3066 N NE1 . TRP B 161 ? 0.6332 0.5346 0.5912 -0.0138 0.0507 -0.0352 544 TRP B NE1 3067 C CE2 . TRP B 161 ? 0.6295 0.5467 0.6088 -0.0135 0.0514 -0.0408 544 TRP B CE2 3068 C CE3 . TRP B 161 ? 0.6328 0.5570 0.6332 -0.0153 0.0547 -0.0514 544 TRP B CE3 3069 C CZ2 . TRP B 161 ? 0.6217 0.5574 0.6203 -0.0117 0.0486 -0.0434 544 TRP B CZ2 3070 C CZ3 . TRP B 161 ? 0.6261 0.5691 0.6453 -0.0133 0.0511 -0.0546 544 TRP B CZ3 3071 C CH2 . TRP B 161 ? 0.6297 0.5782 0.6474 -0.0114 0.0482 -0.0501 544 TRP B CH2 3072 N N . LEU B 162 ? 0.6170 0.5082 0.5464 -0.0076 0.0325 -0.0284 545 LEU B N 3073 C CA . LEU B 162 ? 0.6215 0.5082 0.5385 -0.0054 0.0249 -0.0220 545 LEU B CA 3074 C C . LEU B 162 ? 0.6325 0.5182 0.5444 -0.0023 0.0177 -0.0198 545 LEU B C 3075 O O . LEU B 162 ? 0.6581 0.5347 0.5585 -0.0010 0.0117 -0.0149 545 LEU B O 3076 C CB . LEU B 162 ? 0.6074 0.5125 0.5354 -0.0030 0.0196 -0.0195 545 LEU B CB 3077 C CG . LEU B 162 ? 0.6013 0.5086 0.5360 -0.0052 0.0250 -0.0211 545 LEU B CG 3078 C CD1 . LEU B 162 ? 0.5774 0.5024 0.5230 -0.0023 0.0188 -0.0175 545 LEU B CD1 3079 C CD2 . LEU B 162 ? 0.6140 0.4988 0.5322 -0.0084 0.0301 -0.0201 545 LEU B CD2 3080 N N . VAL B 163 ? 0.6363 0.5310 0.5579 -0.0008 0.0177 -0.0239 546 VAL B N 3081 C CA . VAL B 163 ? 0.6467 0.5442 0.5673 0.0030 0.0110 -0.0226 546 VAL B CA 3082 C C . VAL B 163 ? 0.6543 0.5372 0.5697 0.0021 0.0137 -0.0254 546 VAL B C 3083 O O . VAL B 163 ? 0.6437 0.5285 0.5598 0.0056 0.0085 -0.0252 546 VAL B O 3084 C CB . VAL B 163 ? 0.6323 0.5551 0.5682 0.0075 0.0067 -0.0244 546 VAL B CB 3085 C CG1 . VAL B 163 ? 0.6312 0.5656 0.5706 0.0089 0.0033 -0.0191 546 VAL B CG1 3086 C CG2 . VAL B 163 ? 0.6318 0.5653 0.5802 0.0070 0.0109 -0.0319 546 VAL B CG2 3087 N N . LEU B 164 ? 0.6831 0.5509 0.5938 -0.0023 0.0223 -0.0275 547 LEU B N 3088 C CA . LEU B 164 ? 0.7059 0.5584 0.6128 -0.0038 0.0264 -0.0295 547 LEU B CA 3089 C C . LEU B 164 ? 0.7212 0.5482 0.6103 -0.0080 0.0343 -0.0260 547 LEU B C 3090 O O . LEU B 164 ? 0.7370 0.5618 0.6232 -0.0107 0.0398 -0.0255 547 LEU B O 3091 C CB . LEU B 164 ? 0.6932 0.5570 0.6195 -0.0052 0.0310 -0.0377 547 LEU B CB 3092 C CG . LEU B 164 ? 0.6755 0.5633 0.6165 -0.0002 0.0235 -0.0421 547 LEU B CG 3093 C CD1 . LEU B 164 ? 0.6765 0.5763 0.6363 -0.0016 0.0268 -0.0510 547 LEU B CD1 3094 C CD2 . LEU B 164 ? 0.6915 0.5760 0.6290 0.0037 0.0177 -0.0417 547 LEU B CD2 3095 N N . GLY B 165 ? 0.7490 0.5562 0.6254 -0.0081 0.0350 -0.0235 548 GLY B N 3096 C CA . GLY B 165 ? 0.7845 0.5644 0.6403 -0.0115 0.0435 -0.0195 548 GLY B CA 3097 C C . GLY B 165 ? 0.8015 0.5665 0.6579 -0.0136 0.0505 -0.0204 548 GLY B C 3098 O O . GLY B 165 ? 0.7783 0.5503 0.6464 -0.0114 0.0454 -0.0232 548 GLY B O 3099 N N . GLY B 166 ? 0.8373 0.5813 0.6812 -0.0178 0.0628 -0.0179 549 GLY B N 3100 C CA . GLY B 166 ? 0.8788 0.6028 0.7189 -0.0202 0.0709 -0.0163 549 GLY B CA 3101 C C . GLY B 166 ? 0.8887 0.6244 0.7579 -0.0236 0.0777 -0.0237 549 GLY B C 3102 O O . GLY B 166 ? 0.9426 0.6689 0.8164 -0.0241 0.0790 -0.0240 549 GLY B O 3103 N N . TYR B 167 ? 0.8703 0.6257 0.7599 -0.0259 0.0813 -0.0299 550 TYR B N 3104 C CA . TYR B 167 ? 0.8522 0.6205 0.7719 -0.0291 0.0864 -0.0382 550 TYR B CA 3105 C C . TYR B 167 ? 0.8708 0.6302 0.7955 -0.0351 0.1028 -0.0384 550 TYR B C 3106 O O . TYR B 167 ? 0.8903 0.6405 0.7974 -0.0359 0.1084 -0.0336 550 TYR B O 3107 C CB . TYR B 167 ? 0.8150 0.6142 0.7561 -0.0260 0.0763 -0.0459 550 TYR B CB 3108 C CG . TYR B 167 ? 0.7966 0.6073 0.7352 -0.0255 0.0755 -0.0448 550 TYR B CG 3109 C CD1 . TYR B 167 ? 0.7905 0.6044 0.7123 -0.0211 0.0659 -0.0397 550 TYR B CD1 3110 C CD2 . TYR B 167 ? 0.7938 0.6117 0.7485 -0.0293 0.0843 -0.0489 550 TYR B CD2 3111 C CE1 . TYR B 167 ? 0.7812 0.6043 0.7016 -0.0207 0.0651 -0.0385 550 TYR B CE1 3112 C CE2 . TYR B 167 ? 0.7806 0.6079 0.7333 -0.0285 0.0834 -0.0478 550 TYR B CE2 3113 C CZ . TYR B 167 ? 0.7802 0.6096 0.7152 -0.0243 0.0739 -0.0425 550 TYR B CZ 3114 O OH . TYR B 167 ? 0.7881 0.6258 0.7223 -0.0236 0.0729 -0.0414 550 TYR B OH 3115 N N . ASP B 168 ? 0.8777 0.6404 0.8281 -0.0393 0.1102 -0.0445 551 ASP B N 3116 C CA . ASP B 168 ? 0.8931 0.6489 0.8554 -0.0456 0.1272 -0.0454 551 ASP B CA 3117 C C . ASP B 168 ? 0.8789 0.6615 0.8713 -0.0465 0.1255 -0.0545 551 ASP B C 3118 O O . ASP B 168 ? 0.8479 0.6514 0.8592 -0.0437 0.1136 -0.0620 551 ASP B O 3119 C CB . ASP B 168 ? 0.9012 0.6424 0.8765 -0.0502 0.1371 -0.0461 551 ASP B CB 3120 C CG . ASP B 168 ? 0.8766 0.6356 0.8816 -0.0494 0.1273 -0.0560 551 ASP B CG 3121 O OD1 . ASP B 168 ? 0.8592 0.6242 0.8567 -0.0440 0.1131 -0.0567 551 ASP B OD1 3122 O OD2 . ASP B 168 ? 0.8778 0.6452 0.9142 -0.0539 0.1335 -0.0635 551 ASP B OD2 3123 N N . ASP B 169 ? 0.9158 0.6965 0.9118 -0.0498 0.1377 -0.0540 552 ASP B N 3124 C CA . ASP B 169 ? 0.9270 0.7313 0.9505 -0.0504 0.1365 -0.0617 552 ASP B CA 3125 C C . ASP B 169 ? 0.8763 0.7038 0.8997 -0.0441 0.1180 -0.0645 552 ASP B C 3126 O O . ASP B 169 ? 0.8396 0.6631 0.8374 -0.0404 0.1121 -0.0582 552 ASP B O 3127 C CB . ASP B 169 ? 0.9660 0.7783 1.0278 -0.0552 0.1426 -0.0704 552 ASP B CB 3128 C CG . ASP B 169 ? 1.0256 0.8182 1.0925 -0.0619 0.1641 -0.0673 552 ASP B CG 3129 O OD1 . ASP B 169 ? 1.0773 0.8615 1.1313 -0.0630 0.1753 -0.0627 552 ASP B OD1 3130 O OD2 . ASP B 169 ? 1.0499 0.8357 1.1351 -0.0661 0.1704 -0.0698 552 ASP B OD2 3131 N N . GLN B 170 ? 0.8515 0.7017 0.9024 -0.0427 0.1089 -0.0736 553 GLN B N 3132 C CA . GLN B 170 ? 0.8376 0.7087 0.8874 -0.0363 0.0923 -0.0758 553 GLN B CA 3133 C C . GLN B 170 ? 0.8041 0.6816 0.8602 -0.0334 0.0820 -0.0810 553 GLN B C 3134 O O . GLN B 170 ? 0.7860 0.6841 0.8525 -0.0289 0.0701 -0.0869 553 GLN B O 3135 C CB . GLN B 170 ? 0.8560 0.7489 0.9280 -0.0354 0.0892 -0.0817 553 GLN B CB 3136 C CG . GLN B 170 ? 0.9060 0.7935 0.9719 -0.0374 0.0986 -0.0770 553 GLN B CG 3137 C CD . GLN B 170 ? 0.9132 0.8219 1.0019 -0.0359 0.0947 -0.0824 553 GLN B CD 3138 O OE1 . GLN B 170 ? 0.9158 0.8385 0.9991 -0.0308 0.0834 -0.0810 553 GLN B OE1 3139 N NE2 . GLN B 170 ? 0.9358 0.8465 1.0511 -0.0403 0.1043 -0.0881 553 GLN B NE2 3140 N N . ASN B 171 ? 0.7929 0.6517 0.8410 -0.0355 0.0866 -0.0785 554 ASN B N 3141 C CA . ASN B 171 ? 0.7925 0.6539 0.8448 -0.0326 0.0778 -0.0831 554 ASN B CA 3142 C C . ASN B 171 ? 0.7905 0.6502 0.8166 -0.0267 0.0684 -0.0765 554 ASN B C 3143 O O . ASN B 171 ? 0.7984 0.6394 0.8079 -0.0267 0.0701 -0.0708 554 ASN B O 3144 C CB . ASN B 171 ? 0.8167 0.6582 0.8758 -0.0378 0.0875 -0.0835 554 ASN B CB 3145 C CG . ASN B 171 ? 0.8131 0.6587 0.9048 -0.0437 0.0959 -0.0914 554 ASN B CG 3146 O OD1 . ASN B 171 ? 0.7999 0.6663 0.9154 -0.0423 0.0881 -0.1014 554 ASN B OD1 3147 N ND2 . ASN B 171 ? 0.8263 0.6518 0.9193 -0.0500 0.1119 -0.0868 554 ASN B ND2 3148 N N . TYR B 172 ? 0.7495 0.6286 0.7735 -0.0216 0.0585 -0.0772 555 TYR B N 3149 C CA . TYR B 172 ? 0.7383 0.6183 0.7405 -0.0163 0.0504 -0.0703 555 TYR B CA 3150 C C . TYR B 172 ? 0.7413 0.6182 0.7398 -0.0125 0.0439 -0.0717 555 TYR B C 3151 O O . TYR B 172 ? 0.7445 0.6128 0.7247 -0.0097 0.0403 -0.0648 555 TYR B O 3152 C CB . TYR B 172 ? 0.7082 0.6112 0.7134 -0.0117 0.0422 -0.0711 555 TYR B CB 3153 C CG . TYR B 172 ? 0.7011 0.6061 0.7081 -0.0146 0.0477 -0.0685 555 TYR B CG 3154 C CD1 . TYR B 172 ? 0.7119 0.6026 0.6999 -0.0163 0.0524 -0.0598 555 TYR B CD1 3155 C CD2 . TYR B 172 ? 0.6708 0.5916 0.6989 -0.0153 0.0476 -0.0753 555 TYR B CD2 3156 C CE1 . TYR B 172 ? 0.7181 0.6100 0.7080 -0.0186 0.0577 -0.0583 555 TYR B CE1 3157 C CE2 . TYR B 172 ? 0.6820 0.6047 0.7135 -0.0175 0.0527 -0.0732 555 TYR B CE2 3158 C CZ . TYR B 172 ? 0.7130 0.6211 0.7253 -0.0192 0.0582 -0.0648 555 TYR B CZ 3159 O OH . TYR B 172 ? 0.7366 0.6463 0.7528 -0.0211 0.0636 -0.0635 555 TYR B OH 3160 N N . ASN B 173 ? 0.7432 0.6271 0.7605 -0.0122 0.0418 -0.0814 556 ASN B N 3161 C CA . ASN B 173 ? 0.7488 0.6276 0.7665 -0.0093 0.0372 -0.0847 556 ASN B CA 3162 C C . ASN B 173 ? 0.7693 0.6215 0.7727 -0.0119 0.0429 -0.0772 556 ASN B C 3163 O O . ASN B 173 ? 0.7698 0.6172 0.7656 -0.0077 0.0373 -0.0759 556 ASN B O 3164 C CB . ASN B 173 ? 0.7591 0.6457 0.8017 -0.0104 0.0359 -0.0973 556 ASN B CB 3165 C CG . ASN B 173 ? 0.7795 0.6549 0.8378 -0.0185 0.0471 -0.0992 556 ASN B CG 3166 O OD1 . ASN B 173 ? 0.7805 0.6622 0.8457 -0.0215 0.0516 -0.0990 556 ASN B OD1 3167 N ND2 . ASN B 173 ? 0.7908 0.6492 0.8557 -0.0219 0.0522 -0.1006 556 ASN B ND2 3168 N N . ASN B 174 ? 0.7814 0.6159 0.7803 -0.0181 0.0542 -0.0719 557 ASN B N 3169 C CA . ASN B 174 ? 0.8264 0.6335 0.8085 -0.0202 0.0600 -0.0638 557 ASN B CA 3170 C C . ASN B 174 ? 0.8425 0.6387 0.7959 -0.0178 0.0578 -0.0528 557 ASN B C 3171 O O . ASN B 174 ? 0.8950 0.6666 0.8304 -0.0199 0.0638 -0.0450 557 ASN B O 3172 C CB . ASN B 174 ? 0.8617 0.6521 0.8511 -0.0278 0.0748 -0.0629 557 ASN B CB 3173 C CG . ASN B 174 ? 0.8970 0.6937 0.9163 -0.0309 0.0770 -0.0733 557 ASN B CG 3174 O OD1 . ASN B 174 ? 0.8846 0.6891 0.9148 -0.0273 0.0681 -0.0804 557 ASN B OD1 3175 N ND2 . ASN B 174 ? 0.9382 0.7314 0.9725 -0.0375 0.0892 -0.0749 557 ASN B ND2 3176 N N . ALA B 175 ? 0.8175 0.6309 0.7663 -0.0133 0.0489 -0.0521 558 ALA B N 3177 C CA . ALA B 175 ? 0.8054 0.6106 0.7306 -0.0111 0.0452 -0.0428 558 ALA B CA 3178 C C . ALA B 175 ? 0.7968 0.5860 0.7078 -0.0076 0.0394 -0.0377 558 ALA B C 3179 O O . ALA B 175 ? 0.7754 0.5711 0.6966 -0.0041 0.0336 -0.0420 558 ALA B O 3180 C CB . ALA B 175 ? 0.7876 0.6164 0.7163 -0.0070 0.0367 -0.0436 558 ALA B CB 3181 N N . THR B 176 ? 0.8045 0.5719 0.6914 -0.0082 0.0409 -0.0289 559 THR B N 3182 C CA . THR B 176 ? 0.8144 0.5656 0.6856 -0.0042 0.0335 -0.0230 559 THR B CA 3183 C C . THR B 176 ? 0.8135 0.5701 0.6727 0.0001 0.0225 -0.0181 559 THR B C 3184 O O . THR B 176 ? 0.8467 0.5905 0.6931 0.0038 0.0147 -0.0130 559 THR B O 3185 C CB . THR B 176 ? 0.8464 0.5654 0.6969 -0.0074 0.0417 -0.0160 559 THR B CB 3186 O OG1 . THR B 176 ? 0.8579 0.5682 0.6924 -0.0107 0.0489 -0.0121 559 THR B OG1 3187 C CG2 . THR B 176 ? 0.8632 0.5755 0.7290 -0.0117 0.0520 -0.0202 559 THR B CG2 3188 N N . ALA B 177 ? 0.7827 0.5581 0.6479 0.0000 0.0213 -0.0198 560 ALA B N 3189 C CA . ALA B 177 ? 0.7771 0.5591 0.6351 0.0036 0.0113 -0.0155 560 ALA B CA 3190 C C . ALA B 177 ? 0.7539 0.5638 0.6287 0.0044 0.0094 -0.0192 560 ALA B C 3191 O O . ALA B 177 ? 0.7481 0.5673 0.6326 0.0012 0.0167 -0.0235 560 ALA B O 3192 C CB . ALA B 177 ? 0.7978 0.5586 0.6310 0.0017 0.0125 -0.0092 560 ALA B CB 3193 N N . LEU B 178 ? 0.7339 0.5570 0.6132 0.0091 -0.0002 -0.0173 561 LEU B N 3194 C CA . LEU B 178 ? 0.7005 0.5475 0.5923 0.0103 -0.0024 -0.0183 561 LEU B CA 3195 C C . LEU B 178 ? 0.6843 0.5256 0.5649 0.0098 -0.0068 -0.0123 561 LEU B C 3196 O O . LEU B 178 ? 0.6887 0.5136 0.5557 0.0111 -0.0129 -0.0078 561 LEU B O 3197 C CB . LEU B 178 ? 0.6921 0.5584 0.5983 0.0160 -0.0088 -0.0200 561 LEU B CB 3198 C CG . LEU B 178 ? 0.6984 0.5685 0.6143 0.0181 -0.0071 -0.0264 561 LEU B CG 3199 C CD1 . LEU B 178 ? 0.6981 0.5872 0.6258 0.0245 -0.0130 -0.0274 561 LEU B CD1 3200 C CD2 . LEU B 178 ? 0.6987 0.5767 0.6238 0.0151 0.0002 -0.0336 561 LEU B CD2 3201 N N . VAL B 179 ? 0.6740 0.5284 0.5609 0.0083 -0.0046 -0.0126 562 VAL B N 3202 C CA . VAL B 179 ? 0.6614 0.5130 0.5414 0.0078 -0.0090 -0.0079 562 VAL B CA 3203 C C . VAL B 179 ? 0.6462 0.5231 0.5440 0.0107 -0.0133 -0.0069 562 VAL B C 3204 O O . VAL B 179 ? 0.6417 0.5359 0.5521 0.0109 -0.0090 -0.0102 562 VAL B O 3205 C CB . VAL B 179 ? 0.6708 0.5120 0.5414 0.0032 -0.0011 -0.0088 562 VAL B CB 3206 C CG1 . VAL B 179 ? 0.6928 0.5290 0.5553 0.0030 -0.0064 -0.0048 562 VAL B CG1 3207 C CG2 . VAL B 179 ? 0.6849 0.5010 0.5379 0.0004 0.0056 -0.0092 562 VAL B CG2 3208 N N . ILE B 180 ? 0.6629 0.5413 0.5618 0.0131 -0.0220 -0.0021 563 ILE B N 3209 C CA . ILE B 180 ? 0.6584 0.5591 0.5743 0.0157 -0.0254 0.0004 563 ILE B CA 3210 C C . ILE B 180 ? 0.6767 0.5733 0.5902 0.0137 -0.0294 0.0045 563 ILE B C 3211 O O . ILE B 180 ? 0.6836 0.5631 0.5856 0.0133 -0.0359 0.0065 563 ILE B O 3212 C CB . ILE B 180 ? 0.6776 0.5854 0.6026 0.0205 -0.0319 0.0023 563 ILE B CB 3213 C CG1 . ILE B 180 ? 0.6945 0.6075 0.6231 0.0229 -0.0278 -0.0027 563 ILE B CG1 3214 C CG2 . ILE B 180 ? 0.6764 0.6057 0.6190 0.0231 -0.0344 0.0065 563 ILE B CG2 3215 C CD1 . ILE B 180 ? 0.7006 0.6211 0.6392 0.0282 -0.0329 -0.0017 563 ILE B CD1 3216 N N . THR B 181 ? 0.6823 0.5939 0.6064 0.0130 -0.0265 0.0055 564 THR B N 3217 C CA . THR B 181 ? 0.6955 0.6031 0.6188 0.0109 -0.0295 0.0086 564 THR B CA 3218 C C . THR B 181 ? 0.7029 0.6314 0.6457 0.0127 -0.0316 0.0134 564 THR B C 3219 O O . THR B 181 ? 0.7077 0.6536 0.6605 0.0141 -0.0264 0.0133 564 THR B O 3220 C CB . THR B 181 ? 0.7074 0.6067 0.6220 0.0071 -0.0220 0.0052 564 THR B CB 3221 O OG1 . THR B 181 ? 0.6947 0.5748 0.5921 0.0054 -0.0181 0.0016 564 THR B OG1 3222 C CG2 . THR B 181 ? 0.7406 0.6313 0.6513 0.0051 -0.0254 0.0073 564 THR B CG2 3223 N N . PHE B 182 ? 0.7505 0.6766 0.6986 0.0128 -0.0395 0.0178 565 PHE B N 3224 C CA . PHE B 182 ? 0.7498 0.6933 0.7179 0.0140 -0.0415 0.0236 565 PHE B CA 3225 C C . PHE B 182 ? 0.7341 0.6690 0.7012 0.0107 -0.0443 0.0248 565 PHE B C 3226 O O . PHE B 182 ? 0.7451 0.6637 0.7046 0.0094 -0.0521 0.0241 565 PHE B O 3227 C CB . PHE B 182 ? 0.7933 0.7411 0.7738 0.0166 -0.0492 0.0275 565 PHE B CB 3228 C CG . PHE B 182 ? 0.8574 0.8105 0.8388 0.0202 -0.0480 0.0258 565 PHE B CG 3229 C CD1 . PHE B 182 ? 0.8899 0.8255 0.8568 0.0205 -0.0521 0.0220 565 PHE B CD1 3230 C CD2 . PHE B 182 ? 0.8902 0.8648 0.8864 0.0240 -0.0428 0.0281 565 PHE B CD2 3231 C CE1 . PHE B 182 ? 0.9129 0.8528 0.8822 0.0241 -0.0512 0.0202 565 PHE B CE1 3232 C CE2 . PHE B 182 ? 0.8931 0.8723 0.8904 0.0279 -0.0416 0.0256 565 PHE B CE2 3233 C CZ . PHE B 182 ? 0.8957 0.8576 0.8807 0.0278 -0.0460 0.0215 565 PHE B CZ 3234 N N . PRO B 183 ? 0.6888 0.6333 0.6626 0.0097 -0.0388 0.0260 566 PRO B N 3235 C CA . PRO B 183 ? 0.6883 0.6267 0.6659 0.0072 -0.0422 0.0279 566 PRO B CA 3236 C C . PRO B 183 ? 0.6860 0.6339 0.6839 0.0080 -0.0489 0.0346 566 PRO B C 3237 O O . PRO B 183 ? 0.7130 0.6797 0.7263 0.0105 -0.0457 0.0397 566 PRO B O 3238 C CB . PRO B 183 ? 0.6686 0.6166 0.6503 0.0067 -0.0343 0.0278 566 PRO B CB 3239 C CG . PRO B 183 ? 0.6673 0.6196 0.6412 0.0080 -0.0275 0.0234 566 PRO B CG 3240 C CD . PRO B 183 ? 0.6703 0.6275 0.6456 0.0108 -0.0301 0.0244 566 PRO B CD 3241 N N . VAL B 184 ? 0.6983 0.6327 0.6961 0.0060 -0.0577 0.0342 567 VAL B N 3242 C CA . VAL B 184 ? 0.7156 0.6575 0.7363 0.0059 -0.0645 0.0401 567 VAL B CA 3243 C C . VAL B 184 ? 0.7344 0.6659 0.7571 0.0028 -0.0689 0.0393 567 VAL B C 3244 O O . VAL B 184 ? 0.7165 0.6298 0.7190 0.0013 -0.0697 0.0329 567 VAL B O 3245 C CB . VAL B 184 ? 0.7286 0.6654 0.7534 0.0071 -0.0747 0.0401 567 VAL B CB 3246 C CG1 . VAL B 184 ? 0.7395 0.6845 0.7611 0.0104 -0.0705 0.0398 567 VAL B CG1 3247 C CG2 . VAL B 184 ? 0.7490 0.6604 0.7537 0.0056 -0.0845 0.0338 567 VAL B CG2 3248 N N . ASN B 185 ? 0.7532 0.6961 0.8006 0.0022 -0.0706 0.0458 568 ASN B N 3249 C CA . ASN B 185 ? 0.7819 0.7168 0.8363 -0.0005 -0.0748 0.0456 568 ASN B CA 3250 C C . ASN B 185 ? 0.8002 0.7128 0.8428 -0.0019 -0.0870 0.0388 568 ASN B C 3251 O O . ASN B 185 ? 0.7883 0.6981 0.8351 -0.0012 -0.0960 0.0386 568 ASN B O 3252 C CB . ASN B 185 ? 0.7983 0.7488 0.8848 -0.0010 -0.0756 0.0547 568 ASN B CB 3253 C CG . ASN B 185 ? 0.8163 0.7814 0.9113 -0.0004 -0.0649 0.0610 568 ASN B CG 3254 O OD1 . ASN B 185 ? 0.8366 0.7953 0.9298 -0.0019 -0.0638 0.0595 568 ASN B OD1 3255 N ND2 . ASN B 185 ? 0.8174 0.8016 0.9212 0.0024 -0.0572 0.0679 568 ASN B ND2 3256 N N . ASN B 186 ? 0.8528 0.7491 0.8797 -0.0035 -0.0873 0.0328 569 ASN B N 3257 C CA . ASN B 186 ? 0.9253 0.7992 0.9405 -0.0045 -0.0995 0.0261 569 ASN B CA 3258 C C . ASN B 186 ? 0.9525 0.8288 0.9947 -0.0062 -0.1096 0.0288 569 ASN B C 3259 O O . ASN B 186 ? 0.9855 0.8473 1.0249 -0.0064 -0.1233 0.0243 569 ASN B O 3260 C CB . ASN B 186 ? 0.9541 0.8103 0.9456 -0.0054 -0.0952 0.0187 569 ASN B CB 3261 C CG . ASN B 186 ? 0.9950 0.8333 0.9519 -0.0041 -0.0930 0.0122 569 ASN B CG 3262 O OD1 . ASN B 186 ? 1.0515 0.8872 0.9926 -0.0042 -0.0813 0.0096 569 ASN B OD1 3263 N ND2 . ASN B 186 ? 1.0220 0.8467 0.9675 -0.0029 -0.1047 0.0096 569 ASN B ND2 3264 N N . TYR B 187 ? 0.9806 0.8733 1.0479 -0.0074 -0.1035 0.0359 570 TYR B N 3265 C CA . TYR B 187 ? 1.0073 0.9035 1.1048 -0.0095 -0.1114 0.0398 570 TYR B CA 3266 C C . TYR B 187 ? 1.0443 0.9176 1.1342 -0.0111 -0.1235 0.0308 570 TYR B C 3267 O O . TYR B 187 ? 1.0441 0.9140 1.1531 -0.0125 -0.1362 0.0304 570 TYR B O 3268 C CB . TYR B 187 ? 0.9948 0.9033 1.1168 -0.0092 -0.1177 0.0455 570 TYR B CB 3269 C CG . TYR B 187 ? 0.9753 0.9083 1.1127 -0.0075 -0.1060 0.0555 570 TYR B CG 3270 C CD1 . TYR B 187 ? 0.9543 0.8939 1.0882 -0.0049 -0.1057 0.0562 570 TYR B CD1 3271 C CD2 . TYR B 187 ? 0.9710 0.9197 1.1261 -0.0079 -0.0955 0.0644 570 TYR B CD2 3272 C CE1 . TYR B 187 ? 0.9387 0.8999 1.0854 -0.0028 -0.0948 0.0644 570 TYR B CE1 3273 C CE2 . TYR B 187 ? 0.9436 0.9135 1.1095 -0.0055 -0.0847 0.0734 570 TYR B CE2 3274 C CZ . TYR B 187 ? 0.9468 0.9229 1.1081 -0.0029 -0.0842 0.0729 570 TYR B CZ 3275 O OH . TYR B 187 ? 0.9150 0.9111 1.0851 0.0000 -0.0732 0.0808 570 TYR B OH 3276 N N . TYR B 188 ? 1.1148 0.9726 1.1777 -0.0108 -0.1195 0.0233 571 TYR B N 3277 C CA . TYR B 188 ? 1.2124 1.0464 1.2625 -0.0115 -0.1296 0.0135 571 TYR B CA 3278 C C . TYR B 188 ? 1.2193 1.0543 1.3002 -0.0139 -0.1376 0.0150 571 TYR B C 3279 O O . TYR B 188 ? 1.2129 1.0302 1.2904 -0.0143 -0.1514 0.0072 571 TYR B O 3280 C CB . TYR B 188 ? 1.2867 1.1052 1.3044 -0.0105 -0.1207 0.0057 571 TYR B CB 3281 C CG . TYR B 188 ? 1.3721 1.1769 1.3534 -0.0083 -0.1191 0.0003 571 TYR B CG 3282 C CD1 . TYR B 188 ? 1.4174 1.2041 1.3815 -0.0070 -0.1331 -0.0052 571 TYR B CD1 3283 C CD2 . TYR B 188 ? 1.3932 1.2023 1.3577 -0.0075 -0.1041 0.0008 571 TYR B CD2 3284 C CE1 . TYR B 188 ? 1.4506 1.2234 1.3807 -0.0048 -0.1315 -0.0090 571 TYR B CE1 3285 C CE2 . TYR B 188 ? 1.4190 1.2145 1.3518 -0.0059 -0.1019 -0.0033 571 TYR B CE2 3286 C CZ . TYR B 188 ? 1.4467 1.2237 1.3615 -0.0044 -0.1152 -0.0077 571 TYR B CZ 3287 O OH . TYR B 188 ? 1.4628 1.2249 1.3452 -0.0025 -0.1129 -0.0108 571 TYR B OH 3288 N N . ASN B 189 ? 1.2078 1.0627 1.3184 -0.0153 -0.1296 0.0250 572 ASN B N 3289 C CA . ASN B 189 ? 1.2213 1.0784 1.3651 -0.0180 -0.1359 0.0283 572 ASN B CA 3290 C C . ASN B 189 ? 1.1871 1.0625 1.3680 -0.0196 -0.1392 0.0387 572 ASN B C 3291 O O . ASN B 189 ? 1.2045 1.0818 1.4163 -0.0222 -0.1445 0.0422 572 ASN B O 3292 C CB . ASN B 189 ? 1.2532 1.1141 1.4037 -0.0184 -0.1252 0.0313 572 ASN B CB 3293 C CG . ASN B 189 ? 1.2989 1.1374 1.4381 -0.0188 -0.1314 0.0201 572 ASN B CG 3294 O OD1 . ASN B 189 ? 1.3111 1.1306 1.4183 -0.0173 -0.1352 0.0089 572 ASN B OD1 3295 N ND2 . ASN B 189 ? 1.3059 1.1457 1.4710 -0.0206 -0.1321 0.0231 572 ASN B ND2 3296 N N . ASP B 190 ? 1.1437 1.0315 1.3230 -0.0180 -0.1361 0.0434 573 ASP B N 3297 C CA . ASP B 190 ? 1.1209 1.0248 1.3348 -0.0191 -0.1394 0.0520 573 ASP B CA 3298 C C . ASP B 190 ? 1.1387 1.0350 1.3463 -0.0180 -0.1527 0.0459 573 ASP B C 3299 O O . ASP B 190 ? 1.1519 1.0506 1.3393 -0.0152 -0.1493 0.0450 573 ASP B O 3300 C CB . ASP B 190 ? 1.0867 1.0148 1.3112 -0.0176 -0.1233 0.0645 573 ASP B CB 3301 C CG . ASP B 190 ? 1.0893 1.0346 1.3563 -0.0193 -0.1227 0.0757 573 ASP B CG 3302 O OD1 . ASP B 190 ? 1.1240 1.0675 1.4099 -0.0206 -0.1346 0.0737 573 ASP B OD1 3303 O OD2 . ASP B 190 ? 1.1032 1.0635 1.3854 -0.0193 -0.1103 0.0868 573 ASP B OD2 3304 N N . THR B 191 ? 1.1279 1.0153 1.3553 -0.0200 -0.1687 0.0417 574 THR B N 3305 C CA . THR B 191 ? 1.1209 0.9986 1.3441 -0.0187 -0.1848 0.0348 574 THR B CA 3306 C C . THR B 191 ? 1.1323 1.0300 1.3801 -0.0178 -0.1827 0.0431 574 THR B C 3307 O O . THR B 191 ? 1.1632 1.0572 1.3945 -0.0149 -0.1881 0.0394 574 THR B O 3308 C CB . THR B 191 ? 1.1374 1.0002 1.3780 -0.0211 -0.2036 0.0274 574 THR B CB 3309 O OG1 . THR B 191 ? 1.1200 0.9598 1.3275 -0.0205 -0.2069 0.0168 574 THR B OG1 3310 C CG2 . THR B 191 ? 1.1912 1.0475 1.4381 -0.0198 -0.2224 0.0219 574 THR B CG2 3311 N N . GLU B 192 ? 1.1322 1.0504 1.4196 -0.0200 -0.1748 0.0542 575 GLU B N 3312 C CA . GLU B 192 ? 1.1387 1.0768 1.4544 -0.0191 -0.1719 0.0623 575 GLU B CA 3313 C C . GLU B 192 ? 1.0932 1.0432 1.3866 -0.0153 -0.1566 0.0666 575 GLU B C 3314 O O . GLU B 192 ? 1.0591 1.0167 1.3576 -0.0128 -0.1582 0.0674 575 GLU B O 3315 C CB . GLU B 192 ? 1.1592 1.1153 1.5227 -0.0225 -0.1651 0.0740 575 GLU B CB 3316 C CG . GLU B 192 ? 1.1909 1.1370 1.5824 -0.0270 -0.1785 0.0710 575 GLU B CG 3317 C CD . GLU B 192 ? 1.2134 1.1591 1.6082 -0.0295 -0.1684 0.0762 575 GLU B CD 3318 O OE1 . GLU B 192 ? 1.2112 1.1665 1.6467 -0.0330 -0.1656 0.0850 575 GLU B OE1 3319 O OE2 . GLU B 192 ? 1.1765 1.1124 1.5348 -0.0278 -0.1627 0.0719 575 GLU B OE2 3320 N N . LYS B 193 ? 1.0645 1.0158 1.3346 -0.0145 -0.1427 0.0687 576 LYS B N 3321 C CA . LYS B 193 ? 1.0515 1.0124 1.2987 -0.0109 -0.1290 0.0713 576 LYS B CA 3322 C C . LYS B 193 ? 1.0212 0.9652 1.2293 -0.0084 -0.1350 0.0608 576 LYS B C 3323 O O . LYS B 193 ? 1.0200 0.9708 1.2161 -0.0053 -0.1290 0.0615 576 LYS B O 3324 C CB . LYS B 193 ? 1.0722 1.0410 1.3111 -0.0108 -0.1132 0.0772 576 LYS B CB 3325 C CG . LYS B 193 ? 1.1052 1.0921 1.3795 -0.0123 -0.1043 0.0900 576 LYS B CG 3326 C CD . LYS B 193 ? 1.1301 1.1219 1.3949 -0.0118 -0.0913 0.0955 576 LYS B CD 3327 C CE . LYS B 193 ? 1.1370 1.1467 1.3932 -0.0076 -0.0760 0.1029 576 LYS B CE 3328 N NZ . LYS B 193 ? 1.1410 1.1697 1.4295 -0.0073 -0.0675 0.1162 576 LYS B NZ 3329 N N . LEU B 194 ? 0.9894 0.9107 1.1772 -0.0096 -0.1460 0.0512 577 LEU B N 3330 C CA . LEU B 194 ? 0.9897 0.8922 1.1390 -0.0072 -0.1517 0.0418 577 LEU B CA 3331 C C . LEU B 194 ? 0.9783 0.8784 1.1327 -0.0050 -0.1642 0.0397 577 LEU B C 3332 O O . LEU B 194 ? 0.9343 0.8310 1.0664 -0.0020 -0.1624 0.0376 577 LEU B O 3333 C CB . LEU B 194 ? 1.0298 0.9077 1.1564 -0.0085 -0.1604 0.0323 577 LEU B CB 3334 C CG . LEU B 194 ? 1.0793 0.9340 1.1615 -0.0060 -0.1644 0.0229 577 LEU B CG 3335 C CD1 . LEU B 194 ? 1.0900 0.9508 1.1508 -0.0037 -0.1511 0.0250 577 LEU B CD1 3336 C CD2 . LEU B 194 ? 1.1115 0.9476 1.1720 -0.0072 -0.1641 0.0157 577 LEU B CD2 3337 N N . GLN B 195 ? 0.9885 0.8903 1.1744 -0.0065 -0.1773 0.0401 578 GLN B N 3338 C CA . GLN B 195 ? 0.9909 0.8929 1.1899 -0.0044 -0.1906 0.0387 578 GLN B CA 3339 C C . GLN B 195 ? 0.9426 0.8657 1.1533 -0.0017 -0.1789 0.0460 578 GLN B C 3340 O O . GLN B 195 ? 0.9386 0.8573 1.1380 0.0016 -0.1847 0.0431 578 GLN B O 3341 C CB . GLN B 195 ? 1.0015 0.9061 1.2415 -0.0071 -0.2050 0.0389 578 GLN B CB 3342 C CG . GLN B 195 ? 1.0446 0.9247 1.2720 -0.0086 -0.2223 0.0288 578 GLN B CG 3343 C CD . GLN B 195 ? 1.0986 0.9550 1.2948 -0.0050 -0.2405 0.0184 578 GLN B CD 3344 O OE1 . GLN B 195 ? 1.1389 0.9947 1.3188 -0.0013 -0.2402 0.0186 578 GLN B OE1 3345 N NE2 . GLN B 195 ? 1.1381 0.9729 1.3238 -0.0057 -0.2566 0.0092 578 GLN B NE2 3346 N N . ARG B 196 ? 0.9110 0.8558 1.1425 -0.0028 -0.1624 0.0554 579 ARG B N 3347 C CA . ARG B 196 ? 0.9045 0.8694 1.1435 0.0001 -0.1489 0.0620 579 ARG B CA 3348 C C . ARG B 196 ? 0.8514 0.8094 1.0497 0.0032 -0.1415 0.0579 579 ARG B C 3349 O O . ARG B 196 ? 0.8316 0.7938 1.0265 0.0067 -0.1408 0.0574 579 ARG B O 3350 C CB . ARG B 196 ? 0.9403 0.9272 1.2043 -0.0011 -0.1324 0.0730 579 ARG B CB 3351 C CG . ARG B 196 ? 1.0024 1.0002 1.3133 -0.0040 -0.1367 0.0793 579 ARG B CG 3352 C CD . ARG B 196 ? 1.0310 1.0467 1.3626 -0.0055 -0.1200 0.0910 579 ARG B CD 3353 N NE . ARG B 196 ? 1.0695 1.1050 1.4021 -0.0016 -0.1030 0.0985 579 ARG B NE 3354 C CZ . ARG B 196 ? 1.0833 1.1240 1.3900 0.0008 -0.0887 0.1009 579 ARG B CZ 3355 N NH1 . ARG B 196 ? 1.0696 1.0987 1.3483 -0.0002 -0.0877 0.0971 579 ARG B NH1 3356 N NH2 . ARG B 196 ? 1.0747 1.1329 1.3844 0.0049 -0.0753 0.1067 579 ARG B NH2 3357 N N . ALA B 197 ? 0.8053 0.7523 0.9751 0.0019 -0.1363 0.0546 580 ALA B N 3358 C CA . ALA B 197 ? 0.8019 0.7410 0.9350 0.0041 -0.1291 0.0503 580 ALA B CA 3359 C C . ALA B 197 ? 0.8137 0.7328 0.9237 0.0062 -0.1416 0.0428 580 ALA B C 3360 O O . ALA B 197 ? 0.8074 0.7261 0.9010 0.0091 -0.1372 0.0416 580 ALA B O 3361 C CB . ALA B 197 ? 0.8061 0.7369 0.9175 0.0020 -0.1217 0.0480 580 ALA B CB 3362 N N . GLN B 198 ? 0.8434 0.7452 0.9517 0.0050 -0.1577 0.0378 581 GLN B N 3363 C CA . GLN B 198 ? 0.8494 0.7302 0.9353 0.0076 -0.1721 0.0311 581 GLN B CA 3364 C C . GLN B 198 ? 0.8229 0.7131 0.9298 0.0108 -0.1793 0.0334 581 GLN B C 3365 O O . GLN B 198 ? 0.8462 0.7243 0.9322 0.0142 -0.1849 0.0302 581 GLN B O 3366 C CB . GLN B 198 ? 0.8899 0.7497 0.9688 0.0061 -0.1886 0.0246 581 GLN B CB 3367 C CG . GLN B 198 ? 0.9221 0.7660 0.9699 0.0043 -0.1824 0.0200 581 GLN B CG 3368 C CD . GLN B 198 ? 0.9919 0.8132 1.0290 0.0035 -0.1987 0.0123 581 GLN B CD 3369 O OE1 . GLN B 198 ? 1.0613 0.8828 1.1231 0.0032 -0.2145 0.0112 581 GLN B OE1 3370 N NE2 . GLN B 198 ? 1.0024 0.8040 1.0034 0.0035 -0.1949 0.0065 581 GLN B NE2 3371 N N . ALA B 199 ? 0.7746 0.6860 0.9235 0.0100 -0.1786 0.0393 582 ALA B N 3372 C CA . ALA B 199 ? 0.7650 0.6895 0.9389 0.0132 -0.1819 0.0422 582 ALA B CA 3373 C C . ALA B 199 ? 0.7522 0.6866 0.9129 0.0165 -0.1668 0.0445 582 ALA B C 3374 O O . ALA B 199 ? 0.7437 0.6746 0.8998 0.0204 -0.1721 0.0426 582 ALA B O 3375 C CB . ALA B 199 ? 0.7471 0.6935 0.9698 0.0113 -0.1805 0.0489 582 ALA B CB 3376 N N . TRP B 200 ? 0.7340 0.6799 0.8888 0.0151 -0.1491 0.0482 583 TRP B N 3377 C CA . TRP B 200 ? 0.7373 0.6913 0.8774 0.0181 -0.1351 0.0491 583 TRP B CA 3378 C C . TRP B 200 ? 0.7559 0.6880 0.8570 0.0196 -0.1389 0.0423 583 TRP B C 3379 O O . TRP B 200 ? 0.7291 0.6622 0.8242 0.0232 -0.1370 0.0413 583 TRP B O 3380 C CB . TRP B 200 ? 0.7191 0.6872 0.8575 0.0165 -0.1176 0.0534 583 TRP B CB 3381 C CG . TRP B 200 ? 0.6916 0.6708 0.8202 0.0200 -0.1043 0.0539 583 TRP B CG 3382 C CD1 . TRP B 200 ? 0.6832 0.6837 0.8329 0.0233 -0.0953 0.0588 583 TRP B CD1 3383 C CD2 . TRP B 200 ? 0.6842 0.6529 0.7800 0.0208 -0.0990 0.0488 583 TRP B CD2 3384 N NE1 . TRP B 200 ? 0.6829 0.6865 0.8139 0.0264 -0.0858 0.0562 583 TRP B NE1 3385 C CE2 . TRP B 200 ? 0.6798 0.6643 0.7792 0.0246 -0.0881 0.0501 583 TRP B CE2 3386 C CE3 . TRP B 200 ? 0.6859 0.6333 0.7505 0.0188 -0.1018 0.0430 583 TRP B CE3 3387 C CZ2 . TRP B 200 ? 0.6664 0.6460 0.7412 0.0261 -0.0811 0.0456 583 TRP B CZ2 3388 C CZ3 . TRP B 200 ? 0.6860 0.6289 0.7270 0.0200 -0.0935 0.0393 583 TRP B CZ3 3389 C CH2 . TRP B 200 ? 0.6739 0.6330 0.7212 0.0234 -0.0840 0.0404 583 TRP B CH2 3390 N N . GLU B 201 ? 0.8004 0.7124 0.8756 0.0170 -0.1432 0.0379 584 GLU B N 3391 C CA . GLU B 201 ? 0.8472 0.7364 0.8836 0.0181 -0.1449 0.0324 584 GLU B CA 3392 C C . GLU B 201 ? 0.8399 0.7160 0.8715 0.0218 -0.1596 0.0300 584 GLU B C 3393 O O . GLU B 201 ? 0.8423 0.7081 0.8516 0.0243 -0.1576 0.0281 584 GLU B O 3394 C CB . GLU B 201 ? 0.9146 0.7838 0.9260 0.0150 -0.1474 0.0281 584 GLU B CB 3395 C CG . GLU B 201 ? 0.9929 0.8400 0.9634 0.0158 -0.1441 0.0235 584 GLU B CG 3396 C CD . GLU B 201 ? 1.0888 0.9146 1.0332 0.0134 -0.1460 0.0188 584 GLU B CD 3397 O OE1 . GLU B 201 ? 1.1319 0.9628 1.0894 0.0106 -0.1461 0.0189 584 GLU B OE1 3398 O OE2 . GLU B 201 ? 1.1487 0.9518 1.0589 0.0145 -0.1467 0.0151 584 GLU B OE2 3399 N N . LYS B 202 ? 0.8359 0.7118 0.8895 0.0222 -0.1750 0.0301 585 LYS B N 3400 C CA . LYS B 202 ? 0.8447 0.7097 0.8984 0.0263 -0.1911 0.0281 585 LYS B CA 3401 C C . LYS B 202 ? 0.8179 0.6993 0.8886 0.0302 -0.1849 0.0311 585 LYS B C 3402 O O . LYS B 202 ? 0.8207 0.6893 0.8738 0.0339 -0.1897 0.0292 585 LYS B O 3403 C CB . LYS B 202 ? 0.8602 0.7218 0.9367 0.0257 -0.2101 0.0266 585 LYS B CB 3404 C CG . LYS B 202 ? 0.8928 0.7273 0.9373 0.0243 -0.2208 0.0207 585 LYS B CG 3405 C CD . LYS B 202 ? 0.9098 0.7379 0.9744 0.0244 -0.2430 0.0175 585 LYS B CD 3406 C CE . LYS B 202 ? 0.8973 0.7400 0.9928 0.0196 -0.2400 0.0193 585 LYS B CE 3407 N NZ . LYS B 202 ? 0.9170 0.7555 1.0383 0.0195 -0.2619 0.0160 585 LYS B NZ 3408 N N . GLU B 203 ? 0.7974 0.7057 0.8995 0.0296 -0.1728 0.0359 586 GLU B N 3409 C CA . GLU B 203 ? 0.8116 0.7363 0.9272 0.0336 -0.1637 0.0382 586 GLU B CA 3410 C C . GLU B 203 ? 0.7812 0.7000 0.8656 0.0347 -0.1512 0.0361 586 GLU B C 3411 O O . GLU B 203 ? 0.7926 0.7100 0.8738 0.0388 -0.1512 0.0348 586 GLU B O 3412 C CB . GLU B 203 ? 0.8139 0.7680 0.9667 0.0331 -0.1517 0.0441 586 GLU B CB 3413 C CG . GLU B 203 ? 0.8399 0.8040 1.0331 0.0332 -0.1627 0.0467 586 GLU B CG 3414 C CD . GLU B 203 ? 0.8662 0.8263 1.0711 0.0381 -0.1758 0.0444 586 GLU B CD 3415 O OE1 . GLU B 203 ? 0.8813 0.8493 1.0866 0.0424 -0.1677 0.0445 586 GLU B OE1 3416 O OE2 . GLU B 203 ? 0.8916 0.8401 1.1050 0.0381 -0.1948 0.0419 586 GLU B OE2 3417 N N . PHE B 204 ? 0.7381 0.6535 0.8022 0.0310 -0.1411 0.0355 587 PHE B N 3418 C CA . PHE B 204 ? 0.7248 0.6335 0.7606 0.0312 -0.1298 0.0329 587 PHE B CA 3419 C C . PHE B 204 ? 0.7395 0.6219 0.7463 0.0329 -0.1386 0.0291 587 PHE B C 3420 O O . PHE B 204 ? 0.7281 0.6078 0.7248 0.0355 -0.1335 0.0277 587 PHE B O 3421 C CB . PHE B 204 ? 0.7163 0.6245 0.7380 0.0267 -0.1195 0.0326 587 PHE B CB 3422 C CG . PHE B 204 ? 0.7033 0.6011 0.6959 0.0261 -0.1098 0.0291 587 PHE B CG 3423 C CD1 . PHE B 204 ? 0.6805 0.5922 0.6763 0.0280 -0.0980 0.0288 587 PHE B CD1 3424 C CD2 . PHE B 204 ? 0.7133 0.5873 0.6761 0.0237 -0.1121 0.0257 587 PHE B CD2 3425 C CE1 . PHE B 204 ? 0.6829 0.5853 0.6556 0.0271 -0.0895 0.0251 587 PHE B CE1 3426 C CE2 . PHE B 204 ? 0.7225 0.5873 0.6618 0.0228 -0.1020 0.0229 587 PHE B CE2 3427 C CZ . PHE B 204 ? 0.6941 0.5734 0.6399 0.0242 -0.0911 0.0225 587 PHE B CZ 3428 N N . ILE B 205 ? 0.7675 0.6295 0.7600 0.0318 -0.1518 0.0274 588 ILE B N 3429 C CA . ILE B 205 ? 0.8117 0.6460 0.7731 0.0340 -0.1610 0.0247 588 ILE B CA 3430 C C . ILE B 205 ? 0.8162 0.6515 0.7905 0.0394 -0.1702 0.0255 588 ILE B C 3431 O O . ILE B 205 ? 0.8028 0.6247 0.7573 0.0419 -0.1690 0.0247 588 ILE B O 3432 C CB . ILE B 205 ? 0.8394 0.6515 0.7825 0.0327 -0.1748 0.0224 588 ILE B CB 3433 C CG1 . ILE B 205 ? 0.8448 0.6523 0.7697 0.0280 -0.1638 0.0208 588 ILE B CG1 3434 C CG2 . ILE B 205 ? 0.8736 0.6564 0.7845 0.0362 -0.1863 0.0206 588 ILE B CG2 3435 C CD1 . ILE B 205 ? 0.8681 0.6620 0.7860 0.0262 -0.1756 0.0182 588 ILE B CD1 3436 N N . ASN B 206 ? 0.8086 0.6599 0.8180 0.0411 -0.1788 0.0273 589 ASN B N 3437 C CA . ASN B 206 ? 0.8093 0.6653 0.8383 0.0465 -0.1874 0.0279 589 ASN B CA 3438 C C . ASN B 206 ? 0.7917 0.6618 0.8269 0.0489 -0.1727 0.0285 589 ASN B C 3439 O O . ASN B 206 ? 0.8015 0.6626 0.8305 0.0532 -0.1768 0.0275 589 ASN B O 3440 C CB . ASN B 206 ? 0.7994 0.6745 0.8715 0.0471 -0.1959 0.0299 589 ASN B CB 3441 C CG . ASN B 206 ? 0.8058 0.6656 0.8777 0.0464 -0.2163 0.0281 589 ASN B CG 3442 O OD1 . ASN B 206 ? 0.7738 0.6479 0.8796 0.0451 -0.2221 0.0294 589 ASN B OD1 3443 N ND2 . ASN B 206 ? 0.8300 0.6605 0.8641 0.0475 -0.2270 0.0252 589 ASN B ND2 3444 N N . PHE B 207 ? 0.7838 0.6755 0.8314 0.0465 -0.1564 0.0298 590 PHE B N 3445 C CA . PHE B 207 ? 0.7892 0.6951 0.8418 0.0490 -0.1421 0.0293 590 PHE B CA 3446 C C . PHE B 207 ? 0.8148 0.7010 0.8336 0.0492 -0.1380 0.0261 590 PHE B C 3447 O O . PHE B 207 ? 0.8142 0.6991 0.8340 0.0533 -0.1371 0.0247 590 PHE B O 3448 C CB . PHE B 207 ? 0.7734 0.7025 0.8384 0.0464 -0.1262 0.0312 590 PHE B CB 3449 C CG . PHE B 207 ? 0.7815 0.7260 0.8519 0.0497 -0.1127 0.0299 590 PHE B CG 3450 C CD1 . PHE B 207 ? 0.7723 0.7368 0.8728 0.0543 -0.1101 0.0315 590 PHE B CD1 3451 C CD2 . PHE B 207 ? 0.7970 0.7354 0.8431 0.0486 -0.1027 0.0265 590 PHE B CD2 3452 C CE1 . PHE B 207 ? 0.7740 0.7515 0.8774 0.0581 -0.0979 0.0292 590 PHE B CE1 3453 C CE2 . PHE B 207 ? 0.8002 0.7517 0.8509 0.0520 -0.0918 0.0240 590 PHE B CE2 3454 C CZ . PHE B 207 ? 0.7886 0.7593 0.8665 0.0570 -0.0895 0.0251 590 PHE B CZ 3455 N N . VAL B 208 ? 0.8339 0.7044 0.8245 0.0448 -0.1352 0.0251 591 VAL B N 3456 C CA . VAL B 208 ? 0.8549 0.7066 0.8148 0.0441 -0.1294 0.0227 591 VAL B CA 3457 C C . VAL B 208 ? 0.8832 0.7106 0.8274 0.0478 -0.1424 0.0228 591 VAL B C 3458 O O . VAL B 208 ? 0.8934 0.7131 0.8284 0.0500 -0.1385 0.0217 591 VAL B O 3459 C CB . VAL B 208 ? 0.8611 0.7015 0.7965 0.0387 -0.1229 0.0218 591 VAL B CB 3460 C CG1 . VAL B 208 ? 0.8815 0.6989 0.7852 0.0377 -0.1176 0.0200 591 VAL B CG1 3461 C CG2 . VAL B 208 ? 0.8320 0.6957 0.7813 0.0358 -0.1092 0.0217 591 VAL B CG2 3462 N N . LYS B 209 ? 0.9384 0.7531 0.8795 0.0486 -0.1583 0.0240 592 LYS B N 3463 C CA . LYS B 209 ? 0.9892 0.7790 0.9132 0.0529 -0.1732 0.0245 592 LYS B CA 3464 C C . LYS B 209 ? 0.9889 0.7869 0.9353 0.0588 -0.1779 0.0249 592 LYS B C 3465 O O . LYS B 209 ? 0.9948 0.7741 0.9240 0.0621 -0.1814 0.0253 592 LYS B O 3466 C CB . LYS B 209 ? 1.0249 0.7988 0.9394 0.0529 -0.1908 0.0247 592 LYS B CB 3467 C CG . LYS B 209 ? 1.0660 0.8184 0.9423 0.0488 -0.1861 0.0238 592 LYS B CG 3468 C CD . LYS B 209 ? 1.1172 0.8455 0.9724 0.0501 -0.2045 0.0229 592 LYS B CD 3469 C CE . LYS B 209 ? 1.1089 0.8523 0.9957 0.0501 -0.2179 0.0220 592 LYS B CE 3470 N NZ . LYS B 209 ? 1.1296 0.8516 0.9931 0.0494 -0.2309 0.0194 592 LYS B NZ 3471 N N . ASN B 210 ? 0.9735 0.7994 0.9578 0.0602 -0.1758 0.0250 593 ASN B N 3472 C CA . ASN B 210 ? 0.9908 0.8279 1.0006 0.0661 -0.1783 0.0248 593 ASN B CA 3473 C C . ASN B 210 ? 0.9468 0.7997 0.9639 0.0670 -0.1606 0.0227 593 ASN B C 3474 O O . ASN B 210 ? 0.9415 0.8042 0.9797 0.0723 -0.1611 0.0218 593 ASN B O 3475 C CB . ASN B 210 ? 1.0258 0.8838 1.0753 0.0679 -0.1864 0.0261 593 ASN B CB 3476 C CG . ASN B 210 ? 1.0978 0.9401 1.1443 0.0680 -0.2071 0.0269 593 ASN B CG 3477 O OD1 . ASN B 210 ? 1.1478 0.9662 1.1755 0.0715 -0.2215 0.0267 593 ASN B OD1 3478 N ND2 . ASN B 210 ? 1.0944 0.9488 1.1587 0.0644 -0.2094 0.0277 593 ASN B ND2 3479 N N . TYR B 211 ? 0.9167 0.7718 0.9174 0.0624 -0.1458 0.0214 594 TYR B N 3480 C CA . TYR B 211 ? 0.8858 0.7558 0.8930 0.0635 -0.1304 0.0183 594 TYR B CA 3481 C C . TYR B 211 ? 0.9129 0.7650 0.9061 0.0668 -0.1316 0.0163 594 TYR B C 3482 O O . TYR B 211 ? 0.9181 0.7449 0.8827 0.0647 -0.1346 0.0171 594 TYR B O 3483 C CB . TYR B 211 ? 0.8504 0.7260 0.8440 0.0579 -0.1163 0.0170 594 TYR B CB 3484 C CG . TYR B 211 ? 0.8076 0.7043 0.8131 0.0593 -0.1018 0.0136 594 TYR B CG 3485 C CD1 . TYR B 211 ? 0.7961 0.6851 0.7870 0.0591 -0.0938 0.0092 594 TYR B CD1 3486 C CD2 . TYR B 211 ? 0.7833 0.7069 0.8142 0.0609 -0.0961 0.0146 594 TYR B CD2 3487 C CE1 . TYR B 211 ? 0.7688 0.6762 0.7694 0.0608 -0.0821 0.0049 594 TYR B CE1 3488 C CE2 . TYR B 211 ? 0.7678 0.7094 0.8060 0.0630 -0.0834 0.0111 594 TYR B CE2 3489 C CZ . TYR B 211 ? 0.7683 0.7017 0.7908 0.0632 -0.0771 0.0057 594 TYR B CZ 3490 O OH . TYR B 211 ? 0.7725 0.7232 0.8013 0.0658 -0.0659 0.0011 594 TYR B OH 3491 N N . LYS B 212 ? 0.9350 0.7998 0.9489 0.0721 -0.1288 0.0138 595 LYS B N 3492 C CA . LYS B 212 ? 1.0148 0.8638 1.0206 0.0759 -0.1306 0.0117 595 LYS B CA 3493 C C . LYS B 212 ? 0.9898 0.8473 0.9937 0.0753 -0.1150 0.0064 595 LYS B C 3494 O O . LYS B 212 ? 1.0056 0.8871 1.0307 0.0780 -0.1069 0.0031 595 LYS B O 3495 C CB . LYS B 212 ? 1.0654 0.9209 1.0979 0.0834 -0.1402 0.0117 595 LYS B CB 3496 C CG . LYS B 212 ? 1.1182 0.9695 1.1611 0.0851 -0.1574 0.0159 595 LYS B CG 3497 C CD . LYS B 212 ? 1.1720 0.9904 1.1845 0.0844 -0.1712 0.0191 595 LYS B CD 3498 C CE . LYS B 212 ? 1.2075 1.0231 1.2319 0.0865 -0.1900 0.0220 595 LYS B CE 3499 N NZ . LYS B 212 ? 1.2620 1.0451 1.2529 0.0862 -0.2044 0.0250 595 LYS B NZ 3500 N N . ASN B 213 ? 0.9639 0.8015 0.9423 0.0719 -0.1107 0.0055 596 ASN B N 3501 C CA . ASN B 213 ? 0.9417 0.7828 0.9191 0.0718 -0.0988 -0.0003 596 ASN B CA 3502 C C . ASN B 213 ? 0.9505 0.7619 0.9028 0.0695 -0.0993 0.0006 596 ASN B C 3503 O O . ASN B 213 ? 0.9709 0.7686 0.9013 0.0638 -0.0968 0.0032 596 ASN B O 3504 C CB . ASN B 213 ? 0.9130 0.7728 0.8909 0.0674 -0.0860 -0.0035 596 ASN B CB 3505 C CG . ASN B 213 ? 0.8946 0.7606 0.8752 0.0683 -0.0754 -0.0110 596 ASN B CG 3506 O OD1 . ASN B 213 ? 0.8928 0.7431 0.8682 0.0697 -0.0760 -0.0134 596 ASN B OD1 3507 N ND2 . ASN B 213 ? 0.8832 0.7715 0.8719 0.0677 -0.0663 -0.0147 596 ASN B ND2 3508 N N . PRO B 214 ? 0.9610 0.7619 0.9170 0.0740 -0.1019 -0.0011 597 PRO B N 3509 C CA . PRO B 214 ? 0.9726 0.7442 0.9057 0.0718 -0.1011 0.0007 597 PRO B CA 3510 C C . PRO B 214 ? 0.9654 0.7354 0.8873 0.0653 -0.0870 -0.0028 597 PRO B C 3511 O O . PRO B 214 ? 1.0065 0.7524 0.9062 0.0614 -0.0845 0.0004 597 PRO B O 3512 C CB . PRO B 214 ? 0.9782 0.7448 0.9247 0.0784 -0.1049 -0.0018 597 PRO B CB 3513 C CG . PRO B 214 ? 0.9572 0.7489 0.9325 0.0845 -0.1091 -0.0045 597 PRO B CG 3514 C CD . PRO B 214 ? 0.9453 0.7606 0.9276 0.0814 -0.1046 -0.0048 597 PRO B CD 3515 N N . ASN B 215 ? 0.9315 0.7265 0.8689 0.0645 -0.0779 -0.0095 598 ASN B N 3516 C CA . ASN B 215 ? 0.9262 0.7226 0.8575 0.0589 -0.0657 -0.0142 598 ASN B CA 3517 C C . ASN B 215 ? 0.8976 0.6918 0.8132 0.0520 -0.0611 -0.0109 598 ASN B C 3518 O O . ASN B 215 ? 0.9024 0.6930 0.8116 0.0469 -0.0517 -0.0139 598 ASN B O 3519 C CB . ASN B 215 ? 0.9364 0.7603 0.8877 0.0612 -0.0590 -0.0228 598 ASN B CB 3520 C CG . ASN B 215 ? 0.9590 0.7863 0.9263 0.0680 -0.0610 -0.0283 598 ASN B CG 3521 O OD1 . ASN B 215 ? 0.9762 0.7837 0.9398 0.0688 -0.0626 -0.0287 598 ASN B OD1 3522 N ND2 . ASN B 215 ? 0.9729 0.8251 0.9583 0.0732 -0.0600 -0.0326 598 ASN B ND2 3523 N N . LEU B 216 ? 0.8676 0.6645 0.7792 0.0520 -0.0678 -0.0055 599 LEU B N 3524 C CA . LEU B 216 ? 0.8472 0.6432 0.7456 0.0461 -0.0641 -0.0029 599 LEU B CA 3525 C C . LEU B 216 ? 0.8740 0.6469 0.7513 0.0455 -0.0728 0.0041 599 LEU B C 3526 O O . LEU B 216 ? 0.9066 0.6770 0.7880 0.0501 -0.0849 0.0073 599 LEU B O 3527 C CB . LEU B 216 ? 0.8014 0.6253 0.7160 0.0466 -0.0635 -0.0040 599 LEU B CB 3528 C CG . LEU B 216 ? 0.7667 0.6164 0.7015 0.0491 -0.0567 -0.0106 599 LEU B CG 3529 C CD1 . LEU B 216 ? 0.7438 0.6177 0.6924 0.0503 -0.0573 -0.0089 599 LEU B CD1 3530 C CD2 . LEU B 216 ? 0.7601 0.6104 0.6904 0.0448 -0.0460 -0.0162 599 LEU B CD2 3531 N N . THR B 217 ? 0.8802 0.6362 0.7353 0.0401 -0.0672 0.0063 600 THR B N 3532 C CA . THR B 217 ? 0.9210 0.6590 0.7546 0.0393 -0.0747 0.0120 600 THR B CA 3533 C C . THR B 217 ? 0.8916 0.6445 0.7275 0.0354 -0.0708 0.0110 600 THR B C 3534 O O . THR B 217 ? 0.8923 0.6494 0.7262 0.0306 -0.0589 0.0083 600 THR B O 3535 C CB . THR B 217 ? 0.9684 0.6730 0.7713 0.0373 -0.0716 0.0161 600 THR B CB 3536 O OG1 . THR B 217 ? 1.0075 0.7113 0.8078 0.0318 -0.0559 0.0132 600 THR B OG1 3537 C CG2 . THR B 217 ? 1.0059 0.6935 0.8057 0.0421 -0.0783 0.0187 600 THR B CG2 3538 N N . ILE B 218 ? 0.8701 0.6314 0.7130 0.0374 -0.0814 0.0131 601 ILE B N 3539 C CA . ILE B 218 ? 0.8642 0.6402 0.7127 0.0344 -0.0797 0.0127 601 ILE B CA 3540 C C . ILE B 218 ? 0.8838 0.6379 0.7078 0.0330 -0.0866 0.0160 601 ILE B C 3541 O O . ILE B 218 ? 0.8818 0.6230 0.6991 0.0366 -0.1000 0.0189 601 ILE B O 3542 C CB . ILE B 218 ? 0.8504 0.6524 0.7277 0.0377 -0.0863 0.0127 601 ILE B CB 3543 C CG1 . ILE B 218 ? 0.8445 0.6670 0.7433 0.0404 -0.0795 0.0090 601 ILE B CG1 3544 C CG2 . ILE B 218 ? 0.8373 0.6537 0.7214 0.0345 -0.0844 0.0132 601 ILE B CG2 3545 C CD1 . ILE B 218 ? 0.8360 0.6808 0.7619 0.0450 -0.0852 0.0096 601 ILE B CD1 3546 N N . SER B 219 ? 0.8875 0.6377 0.6988 0.0282 -0.0781 0.0152 602 SER B N 3547 C CA . SER B 219 ? 0.9189 0.6487 0.7056 0.0270 -0.0834 0.0172 602 SER B CA 3548 C C . SER B 219 ? 0.9079 0.6520 0.7029 0.0237 -0.0808 0.0155 602 SER B C 3549 O O . SER B 219 ? 0.8951 0.6589 0.7063 0.0211 -0.0703 0.0132 602 SER B O 3550 C CB . SER B 219 ? 0.9488 0.6519 0.7048 0.0246 -0.0738 0.0180 602 SER B CB 3551 O OG . SER B 219 ? 0.9970 0.6877 0.7475 0.0269 -0.0736 0.0198 602 SER B OG 3552 N N . PHE B 220 ? 0.9499 0.6829 0.7335 0.0243 -0.0911 0.0166 603 PHE B N 3553 C CA . PHE B 220 ? 0.9762 0.7155 0.7613 0.0209 -0.0882 0.0149 603 PHE B CA 3554 C C . PHE B 220 ? 1.0430 0.7632 0.8008 0.0176 -0.0760 0.0135 603 PHE B C 3555 O O . PHE B 220 ? 1.0784 0.7737 0.8094 0.0186 -0.0751 0.0150 603 PHE B O 3556 C CB . PHE B 220 ? 0.9810 0.7134 0.7637 0.0229 -0.1046 0.0155 603 PHE B CB 3557 C CG . PHE B 220 ? 0.9730 0.7230 0.7846 0.0261 -0.1168 0.0171 603 PHE B CG 3558 C CD1 . PHE B 220 ? 0.9859 0.7232 0.7926 0.0307 -0.1312 0.0188 603 PHE B CD1 3559 C CD2 . PHE B 220 ? 0.9445 0.7237 0.7888 0.0249 -0.1134 0.0174 603 PHE B CD2 3560 C CE1 . PHE B 220 ? 0.9840 0.7384 0.8205 0.0338 -0.1418 0.0200 603 PHE B CE1 3561 C CE2 . PHE B 220 ? 0.9417 0.7375 0.8139 0.0279 -0.1227 0.0193 603 PHE B CE2 3562 C CZ . PHE B 220 ? 0.9722 0.7561 0.8420 0.0322 -0.1368 0.0203 603 PHE B CZ 3563 N N . THR B 221 ? 1.1310 0.8628 0.8963 0.0138 -0.0659 0.0111 604 THR B N 3564 C CA . THR B 221 ? 1.2577 0.9733 1.0009 0.0106 -0.0531 0.0094 604 THR B CA 3565 C C . THR B 221 ? 1.4013 1.0973 1.1213 0.0112 -0.0599 0.0087 604 THR B C 3566 O O . THR B 221 ? 1.4174 1.1211 1.1484 0.0122 -0.0716 0.0082 604 THR B O 3567 C CB . THR B 221 ? 1.2455 0.9819 1.0082 0.0068 -0.0395 0.0065 604 THR B CB 3568 O OG1 . THR B 221 ? 1.2162 0.9720 0.9995 0.0067 -0.0453 0.0061 604 THR B OG1 3569 C CG2 . THR B 221 ? 1.2365 0.9890 1.0179 0.0067 -0.0331 0.0061 604 THR B CG2 3570 N N . ALA B 222 ? 1.5412 1.2111 1.2292 0.0105 -0.0521 0.0085 605 ALA B N 3571 C CA . ALA B 222 ? 1.6413 1.2879 1.3005 0.0120 -0.0586 0.0072 605 ALA B CA 3572 C C . ALA B 222 ? 1.6358 1.2936 1.3061 0.0094 -0.0550 0.0032 605 ALA B C 3573 O O . ALA B 222 ? 1.6425 1.3092 1.3209 0.0059 -0.0393 0.0013 605 ALA B O 3574 C CB . ALA B 222 ? 1.6995 1.3157 1.3207 0.0122 -0.0479 0.0085 605 ALA B CB 3575 N N . GLU B 223 ? 1.6470 1.3050 1.3202 0.0112 -0.0702 0.0016 606 GLU B N 3576 C CA . GLU B 223 ? 1.6675 1.3308 1.3474 0.0093 -0.0689 -0.0023 606 GLU B CA 3577 C C . GLU B 223 ? 1.7057 1.3390 1.3497 0.0118 -0.0760 -0.0056 606 GLU B C 3578 O O . GLU B 223 ? 1.7008 1.3271 1.3349 0.0105 -0.0686 -0.0098 606 GLU B O 3579 C CB . GLU B 223 ? 1.6444 1.3332 1.3606 0.0091 -0.0803 -0.0017 606 GLU B CB 3580 C CG . GLU B 223 ? 1.6404 1.3399 1.3712 0.0065 -0.0761 -0.0048 606 GLU B CG 3581 C CD . GLU B 223 ? 1.6219 1.3391 1.3827 0.0067 -0.0899 -0.0038 606 GLU B CD 3582 O OE1 . GLU B 223 ? 1.6095 1.3191 1.3679 0.0066 -0.0972 -0.0072 606 GLU B OE1 3583 O OE2 . GLU B 223 ? 1.5908 1.3291 1.3780 0.0069 -0.0929 0.0003 606 GLU B OE2 # 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 GLU 1 384 ? ? ? A . n A 1 2 THR 2 385 ? ? ? A . n A 1 3 GLY 3 386 ? ? ? A . n A 1 4 GLN 4 387 ? ? ? A . n A 1 5 ALA 5 388 ? ? ? A . n A 1 6 ARG 6 389 ? ? ? A . n A 1 7 LEU 7 390 ? ? ? A . n A 1 8 GLU 8 391 ? ? ? A . n A 1 9 LYS 9 392 392 LYS LYS A . n A 1 10 GLU 10 393 393 GLU GLU A . n A 1 11 TYR 11 394 394 TYR TYR A . n A 1 12 PHE 12 395 395 PHE PHE A . n A 1 13 ASP 13 396 396 ASP ASP A . n A 1 14 GLN 14 397 397 GLN GLN A . n A 1 15 HIS 15 398 398 HIS HIS A . n A 1 16 PHE 16 399 399 PHE PHE A . n A 1 17 GLY 17 400 400 GLY GLY A . n A 1 18 PRO 18 401 401 PRO PRO A . n A 1 19 PHE 19 402 402 PHE PHE A . n A 1 20 PHE 20 403 403 PHE PHE A . n A 1 21 ARG 21 404 404 ARG ARG A . n A 1 22 THR 22 405 405 THR THR A . n A 1 23 GLU 23 406 406 GLU GLU A . n A 1 24 GLN 24 407 407 GLN GLN A . n A 1 25 LEU 25 408 408 LEU LEU A . n A 1 26 ILE 26 409 409 ILE ILE A . n A 1 27 ILE 27 410 410 ILE ILE A . n A 1 28 ARG 28 411 411 ARG ARG A . n A 1 29 ALA 29 412 412 ALA ALA A . n A 1 30 PRO 30 413 413 PRO PRO A . n A 1 31 LEU 31 414 414 LEU LEU A . n A 1 32 THR 32 415 415 THR THR A . n A 1 33 ASP 33 416 416 ASP ASP A . n A 1 34 LYS 34 417 417 LYS LYS A . n A 1 35 HIS 35 418 418 HIS HIS A . n A 1 36 ILE 36 419 419 ILE ILE A . n A 1 37 TYR 37 420 420 TYR TYR A . n A 1 38 GLN 38 421 421 GLN GLN A . n A 1 39 PRO 39 422 422 PRO PRO A . n A 1 40 TYR 40 423 423 TYR TYR A . n A 1 41 PRO 41 424 424 PRO PRO A . n A 1 42 SER 42 425 425 SER SER A . n A 1 43 GLY 43 426 426 GLY GLY A . n A 1 44 ALA 44 427 427 ALA ALA A . n A 1 45 ASP 45 428 428 ASP ASP A . n A 1 46 VAL 46 429 429 VAL VAL A . n A 1 47 PRO 47 430 430 PRO PRO A . n A 1 48 PHE 48 431 431 PHE PHE A . n A 1 49 GLY 49 432 432 GLY GLY A . n A 1 50 PRO 50 433 433 PRO PRO A . n A 1 51 PRO 51 434 434 PRO PRO A . n A 1 52 LEU 52 435 435 LEU LEU A . n A 1 53 ASP 53 436 436 ASP ASP A . n A 1 54 ILE 54 437 437 ILE ILE A . n A 1 55 GLN 55 438 438 GLN GLN A . n A 1 56 ILE 56 439 439 ILE ILE A . n A 1 57 LEU 57 440 440 LEU LEU A . n A 1 58 HIS 58 441 441 HIS HIS A . n A 1 59 GLN 59 442 442 GLN GLN A . n A 1 60 VAL 60 443 443 VAL VAL A . n A 1 61 LEU 61 444 444 LEU LEU A . n A 1 62 ASP 62 445 445 ASP ASP A . n A 1 63 LEU 63 446 446 LEU LEU A . n A 1 64 GLN 64 447 447 GLN GLN A . n A 1 65 ILE 65 448 448 ILE ILE A . n A 1 66 ALA 66 449 449 ALA ALA A . n A 1 67 ILE 67 450 450 ILE ILE A . n A 1 68 GLU 68 451 451 GLU GLU A . n A 1 69 ASN 69 452 452 ASN ASN A . n A 1 70 ILE 70 453 453 ILE ILE A . n A 1 71 THR 71 454 454 THR THR A . n A 1 72 ALA 72 455 455 ALA ALA A . n A 1 73 SER 73 456 456 SER SER A . n A 1 74 TYR 74 457 457 TYR TYR A . n A 1 75 ASP 75 458 458 ASP ASP A . n A 1 76 ASN 76 459 459 ASN ASN A . n A 1 77 GLU 77 460 460 GLU GLU A . n A 1 78 THR 78 461 461 THR THR A . n A 1 79 VAL 79 462 462 VAL VAL A . n A 1 80 THR 80 463 463 THR THR A . n A 1 81 LEU 81 464 464 LEU LEU A . n A 1 82 GLN 82 465 465 GLN GLN A . n A 1 83 ASP 83 466 466 ASP ASP A . n A 1 84 ILE 84 467 467 ILE ILE A . n A 1 85 CYS 85 468 468 CYS CYS A . n A 1 86 LEU 86 469 469 LEU LEU A . n A 1 87 ALA 87 470 470 ALA ALA A . n A 1 88 PRO 88 471 471 PRO PRO A . n A 1 89 LEU 89 472 472 LEU LEU A . n A 1 90 SER 90 473 473 SER SER A . n A 1 91 PRO 91 474 474 PRO PRO A . n A 1 92 TYR 92 475 475 TYR TYR A . n A 1 93 ASN 93 476 476 ASN ASN A . n A 1 94 THR 94 477 477 THR THR A . n A 1 95 ASN 95 478 478 ASN ASN A . n A 1 96 CYS 96 479 479 CYS CYS A . n A 1 97 THR 97 480 480 THR THR A . n A 1 98 ILE 98 481 481 ILE ILE A . n A 1 99 LEU 99 482 482 LEU LEU A . n A 1 100 SER 100 483 483 SER SER A . n A 1 101 VAL 101 484 484 VAL VAL A . n A 1 102 LEU 102 485 485 LEU LEU A . n A 1 103 ASN 103 486 486 ASN ASN A . n A 1 104 TYR 104 487 487 TYR TYR A . n A 1 105 PHE 105 488 488 PHE PHE A . n A 1 106 GLN 106 489 489 GLN GLN A . n A 1 107 ASN 107 490 490 ASN ASN A . n A 1 108 SER 108 491 491 SER SER A . n A 1 109 HIS 109 492 492 HIS HIS A . n A 1 110 SER 110 493 493 SER SER A . n A 1 111 VAL 111 494 494 VAL VAL A . n A 1 112 LEU 112 495 495 LEU LEU A . n A 1 113 ASP 113 496 496 ASP ASP A . n A 1 114 HIS 114 497 497 HIS HIS A . n A 1 115 LYS 115 498 498 LYS LYS A . n A 1 116 LYS 116 499 499 LYS LYS A . n A 1 117 GLY 117 500 500 GLY GLY A . n A 1 118 ASP 118 501 501 ASP ASP A . n A 1 119 ASP 119 502 502 ASP ASP A . n A 1 120 PHE 120 503 503 PHE PHE A . n A 1 121 PHE 121 504 504 PHE PHE A . n A 1 122 VAL 122 505 505 VAL VAL A . n A 1 123 TYR 123 506 506 TYR TYR A . n A 1 124 ALA 124 507 507 ALA ALA A . n A 1 125 ASP 125 508 508 ASP ASP A . n A 1 126 TYR 126 509 509 TYR TYR A . n A 1 127 HIS 127 510 510 HIS HIS A . n A 1 128 THR 128 511 511 THR THR A . n A 1 129 HIS 129 512 512 HIS HIS A . n A 1 130 PHE 130 513 513 PHE PHE A . n A 1 131 LEU 131 514 514 LEU LEU A . n A 1 132 TYR 132 515 515 TYR TYR A . n A 1 133 CYS 133 516 516 CYS CYS A . n A 1 134 VAL 134 517 517 VAL VAL A . n A 1 135 ARG 135 518 518 ARG ARG A . n A 1 136 ALA 136 519 519 ALA ALA A . n A 1 137 PRO 137 520 520 PRO PRO A . n A 1 138 ALA 138 521 521 ALA ALA A . n A 1 139 SER 139 522 522 SER SER A . n A 1 140 LEU 140 523 523 LEU LEU A . n A 1 141 ASN 141 524 524 ASN ASN A . n A 1 142 ASP 142 525 525 ASP ASP A . n A 1 143 THR 143 526 526 THR THR A . n A 1 144 SER 144 527 527 SER SER A . n A 1 145 LEU 145 528 528 LEU LEU A . n A 1 146 LEU 146 529 529 LEU LEU A . n A 1 147 HIS 147 530 530 HIS HIS A . n A 1 148 ASP 148 531 531 ASP ASP A . n A 1 149 PRO 149 532 532 PRO PRO A . n A 1 150 CYS 150 533 533 CYS CYS A . n A 1 151 LEU 151 534 534 LEU LEU A . n A 1 152 GLY 152 535 535 GLY GLY A . n A 1 153 THR 153 536 536 THR THR A . n A 1 154 PHE 154 537 537 PHE PHE A . n A 1 155 GLY 155 538 538 GLY GLY A . n A 1 156 GLY 156 539 539 GLY GLY A . n A 1 157 PRO 157 540 540 PRO PRO A . n A 1 158 VAL 158 541 541 VAL VAL A . n A 1 159 PHE 159 542 542 PHE PHE A . n A 1 160 PRO 160 543 543 PRO PRO A . n A 1 161 TRP 161 544 544 TRP TRP A . n A 1 162 LEU 162 545 545 LEU LEU A . n A 1 163 VAL 163 546 546 VAL VAL A . n A 1 164 LEU 164 547 547 LEU LEU A . n A 1 165 GLY 165 548 548 GLY GLY A . n A 1 166 GLY 166 549 549 GLY GLY A . n A 1 167 TYR 167 550 550 TYR TYR A . n A 1 168 ASP 168 551 551 ASP ASP A . n A 1 169 ASP 169 552 552 ASP ASP A . n A 1 170 GLN 170 553 553 GLN GLN A . n A 1 171 ASN 171 554 554 ASN ASN A . n A 1 172 TYR 172 555 555 TYR TYR A . n A 1 173 ASN 173 556 556 ASN ASN A . n A 1 174 ASN 174 557 557 ASN ASN A . n A 1 175 ALA 175 558 558 ALA ALA A . n A 1 176 THR 176 559 559 THR THR A . n A 1 177 ALA 177 560 560 ALA ALA A . n A 1 178 LEU 178 561 561 LEU LEU A . n A 1 179 VAL 179 562 562 VAL VAL A . n A 1 180 ILE 180 563 563 ILE ILE A . n A 1 181 THR 181 564 564 THR THR A . n A 1 182 PHE 182 565 565 PHE PHE A . n A 1 183 PRO 183 566 566 PRO PRO A . n A 1 184 VAL 184 567 567 VAL VAL A . n A 1 185 ASN 185 568 568 ASN ASN A . n A 1 186 ASN 186 569 569 ASN ASN A . n A 1 187 TYR 187 570 570 TYR TYR A . n A 1 188 TYR 188 571 571 TYR TYR A . n A 1 189 ASN 189 572 572 ASN ASN A . n A 1 190 ASP 190 573 573 ASP ASP A . n A 1 191 THR 191 574 574 THR THR A . n A 1 192 GLU 192 575 575 GLU GLU A . n A 1 193 LYS 193 576 576 LYS LYS A . n A 1 194 LEU 194 577 577 LEU LEU A . n A 1 195 GLN 195 578 578 GLN GLN A . n A 1 196 ARG 196 579 579 ARG ARG A . n A 1 197 ALA 197 580 580 ALA ALA A . n A 1 198 GLN 198 581 581 GLN GLN A . n A 1 199 ALA 199 582 582 ALA ALA A . n A 1 200 TRP 200 583 583 TRP TRP A . n A 1 201 GLU 201 584 584 GLU GLU A . n A 1 202 LYS 202 585 585 LYS LYS A . n A 1 203 GLU 203 586 586 GLU GLU A . n A 1 204 PHE 204 587 587 PHE PHE A . n A 1 205 ILE 205 588 588 ILE ILE A . n A 1 206 ASN 206 589 589 ASN ASN A . n A 1 207 PHE 207 590 590 PHE PHE A . n A 1 208 VAL 208 591 591 VAL VAL A . n A 1 209 LYS 209 592 592 LYS LYS A . n A 1 210 ASN 210 593 593 ASN ASN A . n A 1 211 TYR 211 594 594 TYR TYR A . n A 1 212 LYS 212 595 595 LYS LYS A . n A 1 213 ASN 213 596 596 ASN ASN A . n A 1 214 PRO 214 597 597 PRO PRO A . n A 1 215 ASN 215 598 598 ASN ASN A . n A 1 216 LEU 216 599 599 LEU LEU A . n A 1 217 THR 217 600 600 THR THR A . n A 1 218 ILE 218 601 601 ILE ILE A . n A 1 219 SER 219 602 602 SER SER A . n A 1 220 PHE 220 603 603 PHE PHE A . n A 1 221 THR 221 604 604 THR THR A . n A 1 222 ALA 222 605 605 ALA ALA A . n A 1 223 GLU 223 606 606 GLU GLU A . n A 1 224 ARG 224 607 ? ? ? A . n A 1 225 SER 225 608 ? ? ? A . n A 1 226 ILE 226 609 ? ? ? A . n A 1 227 GLU 227 610 ? ? ? A . n A 1 228 ASP 228 611 ? ? ? A . n A 1 229 GLU 229 612 ? ? ? A . n A 1 230 LEU 230 613 ? ? ? A . n A 1 231 ASN 231 614 ? ? ? A . n A 1 232 ARG 232 615 ? ? ? A . n A 1 233 GLU 233 616 ? ? ? A . n A 1 234 SER 234 617 ? ? ? A . n A 1 235 ASP 235 618 ? ? ? A . n A 1 236 THR 236 619 ? ? ? A . n A 1 237 GLY 237 620 ? ? ? A . n A 1 238 THR 238 621 ? ? ? A . n A 1 239 LEU 239 622 ? ? ? A . n A 1 240 GLU 240 623 ? ? ? A . n A 1 241 VAL 241 624 ? ? ? A . n A 1 242 LEU 242 625 ? ? ? A . n A 1 243 PHE 243 626 ? ? ? A . n A 1 244 GLN 244 627 ? ? ? A . n B 1 1 GLU 1 384 ? ? ? B . n B 1 2 THR 2 385 ? ? ? B . n B 1 3 GLY 3 386 ? ? ? B . n B 1 4 GLN 4 387 ? ? ? B . n B 1 5 ALA 5 388 ? ? ? B . n B 1 6 ARG 6 389 ? ? ? B . n B 1 7 LEU 7 390 ? ? ? B . n B 1 8 GLU 8 391 391 GLU GLU B . n B 1 9 LYS 9 392 392 LYS LYS B . n B 1 10 GLU 10 393 393 GLU GLU B . n B 1 11 TYR 11 394 394 TYR TYR B . n B 1 12 PHE 12 395 395 PHE PHE B . n B 1 13 ASP 13 396 396 ASP ASP B . n B 1 14 GLN 14 397 397 GLN GLN B . n B 1 15 HIS 15 398 398 HIS HIS B . n B 1 16 PHE 16 399 399 PHE PHE B . n B 1 17 GLY 17 400 400 GLY GLY B . n B 1 18 PRO 18 401 401 PRO PRO B . n B 1 19 PHE 19 402 402 PHE PHE B . n B 1 20 PHE 20 403 403 PHE PHE B . n B 1 21 ARG 21 404 404 ARG ARG B . n B 1 22 THR 22 405 405 THR THR B . n B 1 23 GLU 23 406 406 GLU GLU B . n B 1 24 GLN 24 407 407 GLN GLN B . n B 1 25 LEU 25 408 408 LEU LEU B . n B 1 26 ILE 26 409 409 ILE ILE B . n B 1 27 ILE 27 410 410 ILE ILE B . n B 1 28 ARG 28 411 411 ARG ARG B . n B 1 29 ALA 29 412 412 ALA ALA B . n B 1 30 PRO 30 413 413 PRO PRO B . n B 1 31 LEU 31 414 414 LEU LEU B . n B 1 32 THR 32 415 415 THR THR B . n B 1 33 ASP 33 416 416 ASP ASP B . n B 1 34 LYS 34 417 417 LYS LYS B . n B 1 35 HIS 35 418 418 HIS HIS B . n B 1 36 ILE 36 419 419 ILE ILE B . n B 1 37 TYR 37 420 420 TYR TYR B . n B 1 38 GLN 38 421 421 GLN GLN B . n B 1 39 PRO 39 422 422 PRO PRO B . n B 1 40 TYR 40 423 423 TYR TYR B . n B 1 41 PRO 41 424 424 PRO PRO B . n B 1 42 SER 42 425 425 SER SER B . n B 1 43 GLY 43 426 426 GLY GLY B . n B 1 44 ALA 44 427 427 ALA ALA B . n B 1 45 ASP 45 428 428 ASP ASP B . n B 1 46 VAL 46 429 429 VAL VAL B . n B 1 47 PRO 47 430 430 PRO PRO B . n B 1 48 PHE 48 431 431 PHE PHE B . n B 1 49 GLY 49 432 432 GLY GLY B . n B 1 50 PRO 50 433 433 PRO PRO B . n B 1 51 PRO 51 434 434 PRO PRO B . n B 1 52 LEU 52 435 435 LEU LEU B . n B 1 53 ASP 53 436 436 ASP ASP B . n B 1 54 ILE 54 437 437 ILE ILE B . n B 1 55 GLN 55 438 438 GLN GLN B . n B 1 56 ILE 56 439 439 ILE ILE B . n B 1 57 LEU 57 440 440 LEU LEU B . n B 1 58 HIS 58 441 441 HIS HIS B . n B 1 59 GLN 59 442 442 GLN GLN B . n B 1 60 VAL 60 443 443 VAL VAL B . n B 1 61 LEU 61 444 444 LEU LEU B . n B 1 62 ASP 62 445 445 ASP ASP B . n B 1 63 LEU 63 446 446 LEU LEU B . n B 1 64 GLN 64 447 447 GLN GLN B . n B 1 65 ILE 65 448 448 ILE ILE B . n B 1 66 ALA 66 449 449 ALA ALA B . n B 1 67 ILE 67 450 450 ILE ILE B . n B 1 68 GLU 68 451 451 GLU GLU B . n B 1 69 ASN 69 452 452 ASN ASN B . n B 1 70 ILE 70 453 453 ILE ILE B . n B 1 71 THR 71 454 454 THR THR B . n B 1 72 ALA 72 455 455 ALA ALA B . n B 1 73 SER 73 456 456 SER SER B . n B 1 74 TYR 74 457 457 TYR TYR B . n B 1 75 ASP 75 458 458 ASP ASP B . n B 1 76 ASN 76 459 459 ASN ASN B . n B 1 77 GLU 77 460 460 GLU GLU B . n B 1 78 THR 78 461 461 THR THR B . n B 1 79 VAL 79 462 462 VAL VAL B . n B 1 80 THR 80 463 463 THR THR B . n B 1 81 LEU 81 464 464 LEU LEU B . n B 1 82 GLN 82 465 465 GLN GLN B . n B 1 83 ASP 83 466 466 ASP ASP B . n B 1 84 ILE 84 467 467 ILE ILE B . n B 1 85 CYS 85 468 468 CYS CYS B . n B 1 86 LEU 86 469 469 LEU LEU B . n B 1 87 ALA 87 470 470 ALA ALA B . n B 1 88 PRO 88 471 471 PRO PRO B . n B 1 89 LEU 89 472 472 LEU LEU B . n B 1 90 SER 90 473 473 SER SER B . n B 1 91 PRO 91 474 474 PRO PRO B . n B 1 92 TYR 92 475 475 TYR TYR B . n B 1 93 ASN 93 476 476 ASN ASN B . n B 1 94 THR 94 477 477 THR THR B . n B 1 95 ASN 95 478 478 ASN ASN B . n B 1 96 CYS 96 479 479 CYS CYS B . n B 1 97 THR 97 480 480 THR THR B . n B 1 98 ILE 98 481 481 ILE ILE B . n B 1 99 LEU 99 482 482 LEU LEU B . n B 1 100 SER 100 483 483 SER SER B . n B 1 101 VAL 101 484 484 VAL VAL B . n B 1 102 LEU 102 485 485 LEU LEU B . n B 1 103 ASN 103 486 486 ASN ASN B . n B 1 104 TYR 104 487 487 TYR TYR B . n B 1 105 PHE 105 488 488 PHE PHE B . n B 1 106 GLN 106 489 489 GLN GLN B . n B 1 107 ASN 107 490 490 ASN ASN B . n B 1 108 SER 108 491 491 SER SER B . n B 1 109 HIS 109 492 492 HIS HIS B . n B 1 110 SER 110 493 493 SER SER B . n B 1 111 VAL 111 494 494 VAL VAL B . n B 1 112 LEU 112 495 495 LEU LEU B . n B 1 113 ASP 113 496 496 ASP ASP B . n B 1 114 HIS 114 497 497 HIS HIS B . n B 1 115 LYS 115 498 498 LYS LYS B . n B 1 116 LYS 116 499 499 LYS LYS B . n B 1 117 GLY 117 500 500 GLY GLY B . n B 1 118 ASP 118 501 501 ASP ASP B . n B 1 119 ASP 119 502 502 ASP ASP B . n B 1 120 PHE 120 503 503 PHE PHE B . n B 1 121 PHE 121 504 504 PHE PHE B . n B 1 122 VAL 122 505 505 VAL VAL B . n B 1 123 TYR 123 506 506 TYR TYR B . n B 1 124 ALA 124 507 507 ALA ALA B . n B 1 125 ASP 125 508 508 ASP ASP B . n B 1 126 TYR 126 509 509 TYR TYR B . n B 1 127 HIS 127 510 510 HIS HIS B . n B 1 128 THR 128 511 511 THR THR B . n B 1 129 HIS 129 512 512 HIS HIS B . n B 1 130 PHE 130 513 513 PHE PHE B . n B 1 131 LEU 131 514 514 LEU LEU B . n B 1 132 TYR 132 515 515 TYR TYR B . n B 1 133 CYS 133 516 516 CYS CYS B . n B 1 134 VAL 134 517 517 VAL VAL B . n B 1 135 ARG 135 518 518 ARG ARG B . n B 1 136 ALA 136 519 519 ALA ALA B . n B 1 137 PRO 137 520 520 PRO PRO B . n B 1 138 ALA 138 521 521 ALA ALA B . n B 1 139 SER 139 522 522 SER SER B . n B 1 140 LEU 140 523 523 LEU LEU B . n B 1 141 ASN 141 524 524 ASN ASN B . n B 1 142 ASP 142 525 525 ASP ASP B . n B 1 143 THR 143 526 526 THR THR B . n B 1 144 SER 144 527 527 SER SER B . n B 1 145 LEU 145 528 528 LEU LEU B . n B 1 146 LEU 146 529 529 LEU LEU B . n B 1 147 HIS 147 530 530 HIS HIS B . n B 1 148 ASP 148 531 531 ASP ASP B . n B 1 149 PRO 149 532 532 PRO PRO B . n B 1 150 CYS 150 533 533 CYS CYS B . n B 1 151 LEU 151 534 534 LEU LEU B . n B 1 152 GLY 152 535 535 GLY GLY B . n B 1 153 THR 153 536 536 THR THR B . n B 1 154 PHE 154 537 537 PHE PHE B . n B 1 155 GLY 155 538 538 GLY GLY B . n B 1 156 GLY 156 539 539 GLY GLY B . n B 1 157 PRO 157 540 540 PRO PRO B . n B 1 158 VAL 158 541 541 VAL VAL B . n B 1 159 PHE 159 542 542 PHE PHE B . n B 1 160 PRO 160 543 543 PRO PRO B . n B 1 161 TRP 161 544 544 TRP TRP B . n B 1 162 LEU 162 545 545 LEU LEU B . n B 1 163 VAL 163 546 546 VAL VAL B . n B 1 164 LEU 164 547 547 LEU LEU B . n B 1 165 GLY 165 548 548 GLY GLY B . n B 1 166 GLY 166 549 549 GLY GLY B . n B 1 167 TYR 167 550 550 TYR TYR B . n B 1 168 ASP 168 551 551 ASP ASP B . n B 1 169 ASP 169 552 552 ASP ASP B . n B 1 170 GLN 170 553 553 GLN GLN B . n B 1 171 ASN 171 554 554 ASN ASN B . n B 1 172 TYR 172 555 555 TYR TYR B . n B 1 173 ASN 173 556 556 ASN ASN B . n B 1 174 ASN 174 557 557 ASN ASN B . n B 1 175 ALA 175 558 558 ALA ALA B . n B 1 176 THR 176 559 559 THR THR B . n B 1 177 ALA 177 560 560 ALA ALA B . n B 1 178 LEU 178 561 561 LEU LEU B . n B 1 179 VAL 179 562 562 VAL VAL B . n B 1 180 ILE 180 563 563 ILE ILE B . n B 1 181 THR 181 564 564 THR THR B . n B 1 182 PHE 182 565 565 PHE PHE B . n B 1 183 PRO 183 566 566 PRO PRO B . n B 1 184 VAL 184 567 567 VAL VAL B . n B 1 185 ASN 185 568 568 ASN ASN B . n B 1 186 ASN 186 569 569 ASN ASN B . n B 1 187 TYR 187 570 570 TYR TYR B . n B 1 188 TYR 188 571 571 TYR TYR B . n B 1 189 ASN 189 572 572 ASN ASN B . n B 1 190 ASP 190 573 573 ASP ASP B . n B 1 191 THR 191 574 574 THR THR B . n B 1 192 GLU 192 575 575 GLU GLU B . n B 1 193 LYS 193 576 576 LYS LYS B . n B 1 194 LEU 194 577 577 LEU LEU B . n B 1 195 GLN 195 578 578 GLN GLN B . n B 1 196 ARG 196 579 579 ARG ARG B . n B 1 197 ALA 197 580 580 ALA ALA B . n B 1 198 GLN 198 581 581 GLN GLN B . n B 1 199 ALA 199 582 582 ALA ALA B . n B 1 200 TRP 200 583 583 TRP TRP B . n B 1 201 GLU 201 584 584 GLU GLU B . n B 1 202 LYS 202 585 585 LYS LYS B . n B 1 203 GLU 203 586 586 GLU GLU B . n B 1 204 PHE 204 587 587 PHE PHE B . n B 1 205 ILE 205 588 588 ILE ILE B . n B 1 206 ASN 206 589 589 ASN ASN B . n B 1 207 PHE 207 590 590 PHE PHE B . n B 1 208 VAL 208 591 591 VAL VAL B . n B 1 209 LYS 209 592 592 LYS LYS B . n B 1 210 ASN 210 593 593 ASN ASN B . n B 1 211 TYR 211 594 594 TYR TYR B . n B 1 212 LYS 212 595 595 LYS LYS B . n B 1 213 ASN 213 596 596 ASN ASN B . n B 1 214 PRO 214 597 597 PRO PRO B . n B 1 215 ASN 215 598 598 ASN ASN B . n B 1 216 LEU 216 599 599 LEU LEU B . n B 1 217 THR 217 600 600 THR THR B . n B 1 218 ILE 218 601 601 ILE ILE B . n B 1 219 SER 219 602 602 SER SER B . n B 1 220 PHE 220 603 603 PHE PHE B . n B 1 221 THR 221 604 604 THR THR B . n B 1 222 ALA 222 605 605 ALA ALA B . n B 1 223 GLU 223 606 606 GLU GLU B . n B 1 224 ARG 224 607 ? ? ? B . n B 1 225 SER 225 608 ? ? ? B . n B 1 226 ILE 226 609 ? ? ? B . n B 1 227 GLU 227 610 ? ? ? B . n B 1 228 ASP 228 611 ? ? ? B . n B 1 229 GLU 229 612 ? ? ? B . n B 1 230 LEU 230 613 ? ? ? B . n B 1 231 ASN 231 614 ? ? ? B . n B 1 232 ARG 232 615 ? ? ? B . n B 1 233 GLU 233 616 ? ? ? B . n B 1 234 SER 234 617 ? ? ? B . n B 1 235 ASP 235 618 ? ? ? B . n B 1 236 THR 236 619 ? ? ? B . n B 1 237 GLY 237 620 ? ? ? B . n B 1 238 THR 238 621 ? ? ? B . n B 1 239 LEU 239 622 ? ? ? B . n B 1 240 GLU 240 623 ? ? ? B . n B 1 241 VAL 241 624 ? ? ? B . n B 1 242 LEU 242 625 ? ? ? B . n B 1 243 PHE 243 626 ? ? ? B . n B 1 244 GLN 244 627 ? ? ? 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 1 701 524 NAG NAG A . D 2 NAG 2 702 525 NAG NAG A . E 2 NAG 1 703 557 NAG NAG A . F 2 NAG 2 704 558 NAG NAG A . G 3 BMA 3 705 559 BMA BMA A . H 4 MAN 4 706 560 MAN MAN A . I 2 NAG 1 707 572 NAG NAG A . J 2 NAG 1 708 598 NAG NAG A . K 2 NAG 2 709 599 NAG NAG A . L 2 NAG 1 710 478 NAG NAG A . M 2 NAG 2 711 479 NAG NAG A . N 5 SCN 1 712 1 SCN SCN A . O 5 SCN 1 713 4 SCN SCN A . P 2 NAG 1 701 478 NAG NAG B . Q 2 NAG 2 702 479 NAG NAG B . R 2 NAG 1 703 524 NAG NAG B . S 2 NAG 2 704 525 NAG NAG B . T 2 NAG 1 705 557 NAG NAG B . U 2 NAG 2 706 558 NAG NAG B . V 3 BMA 3 707 559 BMA BMA B . W 4 MAN 4 708 560 MAN MAN B . X 4 MAN 5 709 561 MAN MAN B . Y 2 NAG 1 710 598 NAG NAG B . Z 2 NAG 2 711 599 NAG NAG B . AA 3 BMA 3 712 600 BMA BMA B . BA 5 SCN 1 713 2 SCN SCN B . CA 5 SCN 1 714 3 SCN SCN B . DA 6 HOH 1 801 2 HOH HOH A . DA 6 HOH 2 802 44 HOH HOH A . DA 6 HOH 3 803 48 HOH HOH A . DA 6 HOH 4 804 49 HOH HOH A . DA 6 HOH 5 805 20 HOH HOH A . DA 6 HOH 6 806 7 HOH HOH A . DA 6 HOH 7 807 8 HOH HOH A . DA 6 HOH 8 808 5 HOH HOH A . DA 6 HOH 9 809 15 HOH HOH A . DA 6 HOH 10 810 33 HOH HOH A . DA 6 HOH 11 811 6 HOH HOH A . DA 6 HOH 12 812 21 HOH HOH A . DA 6 HOH 13 813 41 HOH HOH A . EA 6 HOH 1 801 29 HOH HOH B . EA 6 HOH 2 802 22 HOH HOH B . EA 6 HOH 3 803 45 HOH HOH B . EA 6 HOH 4 804 42 HOH HOH B . EA 6 HOH 5 805 14 HOH HOH B . EA 6 HOH 6 806 23 HOH HOH B . EA 6 HOH 7 807 39 HOH HOH B . EA 6 HOH 8 808 37 HOH HOH B . EA 6 HOH 9 809 38 HOH HOH B . EA 6 HOH 10 810 32 HOH HOH B . EA 6 HOH 11 811 51 HOH HOH B . EA 6 HOH 12 812 35 HOH HOH B . EA 6 HOH 13 813 31 HOH HOH B . EA 6 HOH 14 814 34 HOH HOH B . EA 6 HOH 15 815 13 HOH HOH B . EA 6 HOH 16 816 50 HOH HOH B . EA 6 HOH 17 817 26 HOH HOH B . EA 6 HOH 18 818 47 HOH HOH B . EA 6 HOH 19 819 12 HOH HOH B . EA 6 HOH 20 820 30 HOH HOH B . EA 6 HOH 21 821 25 HOH HOH B . EA 6 HOH 22 822 17 HOH HOH B . EA 6 HOH 23 823 3 HOH HOH B . EA 6 HOH 24 824 27 HOH HOH B . EA 6 HOH 25 825 36 HOH HOH B . EA 6 HOH 26 826 16 HOH HOH B . EA 6 HOH 27 827 46 HOH HOH B . EA 6 HOH 28 828 52 HOH HOH B . EA 6 HOH 29 829 28 HOH HOH B . EA 6 HOH 30 830 9 HOH HOH B . EA 6 HOH 31 831 43 HOH HOH B . # 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_defined_assembly ? monomeric 1 2 author_defined_assembly ? 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,O,DA 2 1 B,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,EA # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2016-02-10 2 'Structure model' 1 1 2016-03-02 3 'Structure model' 1 2 2016-03-16 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 76.6654 21.7124 88.3181 0.0520 0.1541 0.1337 0.0308 0.0103 -0.0352 1.5182 1.3117 0.7355 -0.0831 -0.6276 -0.0244 -0.2170 -0.2259 -0.0642 -0.0377 0.3960 -0.1361 0.1392 0.1099 -0.1790 'X-RAY DIFFRACTION' 2 ? refined 58.7347 43.2528 86.3575 0.0870 0.0532 0.0409 0.0262 -0.0144 -0.0098 1.1846 1.9283 0.4593 -0.4201 0.0647 0.1469 -0.0531 -0.2282 0.0744 -0.1970 0.1266 0.0713 -0.1327 -0.0533 -0.0735 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 392 ? ? A 606 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 391 ? ? B 606 ? ? ? ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0135 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2 ? ? ? . 2 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? . 4 # 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 ND2 A ASN 557 ? ? C2 A NAG 703 ? ? 2.11 2 1 ND2 B ASN 598 ? ? O5 B NAG 710 ? ? 2.18 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 398 ? ? 64.59 -69.27 2 1 PHE A 399 ? ? -162.07 64.38 3 1 ASP A 458 ? ? 53.81 -127.77 4 1 TYR A 475 ? B -141.30 37.85 5 1 ASN A 476 ? A -9.88 145.86 6 1 THR A 477 ? A -169.71 -144.92 7 1 PHE A 503 ? ? -137.44 -33.66 8 1 SER A 527 ? ? -66.79 -174.88 9 1 ASP A 552 ? ? 44.67 -123.06 10 1 LYS B 392 ? ? -133.89 -57.89 11 1 ASP B 458 ? ? 53.41 -127.67 12 1 TYR B 475 ? A -143.78 47.65 13 1 TYR B 475 ? B -107.50 -151.29 14 1 THR B 477 ? B 179.80 -154.45 15 1 SER B 527 ? ? -67.48 -174.37 16 1 ASP B 552 ? ? 44.99 -123.64 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 PHE _pdbx_validate_peptide_omega.auth_asym_id_1 B _pdbx_validate_peptide_omega.auth_seq_id_1 399 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 GLY _pdbx_validate_peptide_omega.auth_asym_id_2 B _pdbx_validate_peptide_omega.auth_seq_id_2 400 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 149.18 # 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 GLU 384 ? A GLU 1 2 1 Y 1 A THR 385 ? A THR 2 3 1 Y 1 A GLY 386 ? A GLY 3 4 1 Y 1 A GLN 387 ? A GLN 4 5 1 Y 1 A ALA 388 ? A ALA 5 6 1 Y 1 A ARG 389 ? A ARG 6 7 1 Y 1 A LEU 390 ? A LEU 7 8 1 Y 1 A GLU 391 ? A GLU 8 9 1 Y 1 A ARG 607 ? A ARG 224 10 1 Y 1 A SER 608 ? A SER 225 11 1 Y 1 A ILE 609 ? A ILE 226 12 1 Y 1 A GLU 610 ? A GLU 227 13 1 Y 1 A ASP 611 ? A ASP 228 14 1 Y 1 A GLU 612 ? A GLU 229 15 1 Y 1 A LEU 613 ? A LEU 230 16 1 Y 1 A ASN 614 ? A ASN 231 17 1 Y 1 A ARG 615 ? A ARG 232 18 1 Y 1 A GLU 616 ? A GLU 233 19 1 Y 1 A SER 617 ? A SER 234 20 1 Y 1 A ASP 618 ? A ASP 235 21 1 Y 1 A THR 619 ? A THR 236 22 1 Y 1 A GLY 620 ? A GLY 237 23 1 Y 1 A THR 621 ? A THR 238 24 1 Y 1 A LEU 622 ? A LEU 239 25 1 Y 1 A GLU 623 ? A GLU 240 26 1 Y 1 A VAL 624 ? A VAL 241 27 1 Y 1 A LEU 625 ? A LEU 242 28 1 Y 1 A PHE 626 ? A PHE 243 29 1 Y 1 A GLN 627 ? A GLN 244 30 1 Y 1 B GLU 384 ? B GLU 1 31 1 Y 1 B THR 385 ? B THR 2 32 1 Y 1 B GLY 386 ? B GLY 3 33 1 Y 1 B GLN 387 ? B GLN 4 34 1 Y 1 B ALA 388 ? B ALA 5 35 1 Y 1 B ARG 389 ? B ARG 6 36 1 Y 1 B LEU 390 ? B LEU 7 37 1 Y 1 B ARG 607 ? B ARG 224 38 1 Y 1 B SER 608 ? B SER 225 39 1 Y 1 B ILE 609 ? B ILE 226 40 1 Y 1 B GLU 610 ? B GLU 227 41 1 Y 1 B ASP 611 ? B ASP 228 42 1 Y 1 B GLU 612 ? B GLU 229 43 1 Y 1 B LEU 613 ? B LEU 230 44 1 Y 1 B ASN 614 ? B ASN 231 45 1 Y 1 B ARG 615 ? B ARG 232 46 1 Y 1 B GLU 616 ? B GLU 233 47 1 Y 1 B SER 617 ? B SER 234 48 1 Y 1 B ASP 618 ? B ASP 235 49 1 Y 1 B THR 619 ? B THR 236 50 1 Y 1 B GLY 620 ? B GLY 237 51 1 Y 1 B THR 621 ? B THR 238 52 1 Y 1 B LEU 622 ? B LEU 239 53 1 Y 1 B GLU 623 ? B GLU 240 54 1 Y 1 B VAL 624 ? B VAL 241 55 1 Y 1 B LEU 625 ? B LEU 242 56 1 Y 1 B PHE 626 ? B PHE 243 57 1 Y 1 B GLN 627 ? B GLN 244 # 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 'THIOCYANATE ION' SCN 6 water HOH #