data_5BZW # _entry.id 5BZW # _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 5BZW WWPDB D_1000210826 # _pdbx_database_related.db_name PDB _pdbx_database_related.details . _pdbx_database_related.db_id 5BZD _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5BZW _pdbx_database_status.recvd_initial_deposition_date 2015-06-11 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _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 'Garces, F.' 1 'WILSON, I.A.' 2 # _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 US _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev Immunity _citation.journal_id_ASTM IUNIEH _citation.journal_id_CSD 2048 _citation.journal_id_ISSN 1074-7613 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 44 _citation.language ? _citation.page_first 1215 _citation.page_last 1226 _citation.title ;Early Antibody Lineage Diversification and Independent Limb Maturation Lead to Broad HIV-1 Neutralization Targeting the Env High-Mannose Patch ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI ? _citation.pdbx_database_id_PubMed ? _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'MacLead, D.' 1 primary 'Choi, N.M.' 2 primary 'Briney, B.' 3 primary 'Garces, F.' 4 primary 'Ver, L.S.' 5 primary 'Landais, E.' 6 primary 'Murrell, B.' 7 primary 'Wrin, T.' 8 primary 'Kilembe, W.' 9 primary 'Liang, C.-H.' 10 primary 'Ramos, A.' 11 primary 'Bian, C.' 12 primary 'Wickramasinghe, L.' 13 primary 'Kong, L.' 14 primary 'Eren, K.' 15 primary 'Wu, C.-Y.' 16 primary 'Wong, C.-H.' 17 primary 'The IAVI Protocol C Investigators & The IAVI African HIV Research Network' 18 primary 'Pond, S.L.K.' 19 primary 'Wilson, I.A.' 20 primary 'Burton, D.R.' 21 primary 'Poignard, P.' 22 # _cell.entry_id 5BZW _cell.length_a 89.354 _cell.length_b 89.354 _cell.length_c 211.301 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5BZW _symmetry.space_group_name_H-M 'P 61 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 178 # 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 '2B3 HIV Antibody light chain' 23306.898 1 ? ? ? ;EIVLTQSPGTLSLSPGERATLSCRASQSVSAKNLAWYQQKPGQTPRLLMYGVSLRNTGVP DRFSGSGSGTDFTLTISRLEPEDSAVYFCQQYGTSPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC ; 2 polymer man '2B3 HIV Antibody heavy chain' 25121.143 1 ? ? ? ;QVQLQQWGAGLLKPSETLSLTCAVYNESLSAFSWSWIRQFPGQGLEWIGEIDHTTSSNYN PSLKRRINISIDTSKKQFSLKLYSVTAADTAVYYCARGGRKVYHAYWSGYVNNCFDPWGQ GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCD ; 3 non-polymer syn 'SULFATE ION' 96.063 5 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 5 water nat water 18.015 1 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;EIVLTQSPGTLSLSPGERATLSCRASQSVSAKNLAWYQQKPGQTPRLLMYGVSLRNTGVPDRFSGSGSGTDFTLTISRLE PEDSAVYFCQQYGTSPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC ; ;EIVLTQSPGTLSLSPGERATLSCRASQSVSAKNLAWYQQKPGQTPRLLMYGVSLRNTGVPDRFSGSGSGTDFTLTISRLE PEDSAVYFCQQYGTSPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC ; A ? 2 'polypeptide(L)' no no ;QVQLQQWGAGLLKPSETLSLTCAVYNESLSAFSWSWIRQFPGQGLEWIGEIDHTTSSNYNPSLKRRINISIDTSKKQFSL KLYSVTAADTAVYYCARGGRKVYHAYWSGYVNNCFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDY FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCD ; ;QVQLQQWGAGLLKPSETLSLTCAVYNESLSAFSWSWIRQFPGQGLEWIGEIDHTTSSNYNPSLKRRINISIDTSKKQFSL KLYSVTAADTAVYYCARGGRKVYHAYWSGYVNNCFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDY FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCD ; B ? # 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 ILE n 1 3 VAL n 1 4 LEU n 1 5 THR n 1 6 GLN n 1 7 SER n 1 8 PRO n 1 9 GLY n 1 10 THR n 1 11 LEU n 1 12 SER n 1 13 LEU n 1 14 SER n 1 15 PRO n 1 16 GLY n 1 17 GLU n 1 18 ARG n 1 19 ALA n 1 20 THR n 1 21 LEU n 1 22 SER n 1 23 CYS n 1 24 ARG n 1 25 ALA n 1 26 SER n 1 27 GLN n 1 28 SER n 1 29 VAL n 1 30 SER n 1 31 ALA n 1 32 LYS n 1 33 ASN n 1 34 LEU n 1 35 ALA n 1 36 TRP n 1 37 TYR n 1 38 GLN n 1 39 GLN n 1 40 LYS n 1 41 PRO n 1 42 GLY n 1 43 GLN n 1 44 THR n 1 45 PRO n 1 46 ARG n 1 47 LEU n 1 48 LEU n 1 49 MET n 1 50 TYR n 1 51 GLY n 1 52 VAL n 1 53 SER n 1 54 LEU n 1 55 ARG n 1 56 ASN n 1 57 THR n 1 58 GLY n 1 59 VAL n 1 60 PRO n 1 61 ASP n 1 62 ARG n 1 63 PHE n 1 64 SER n 1 65 GLY n 1 66 SER n 1 67 GLY n 1 68 SER n 1 69 GLY n 1 70 THR n 1 71 ASP n 1 72 PHE n 1 73 THR n 1 74 LEU n 1 75 THR n 1 76 ILE n 1 77 SER n 1 78 ARG n 1 79 LEU n 1 80 GLU n 1 81 PRO n 1 82 GLU n 1 83 ASP n 1 84 SER n 1 85 ALA n 1 86 VAL n 1 87 TYR n 1 88 PHE n 1 89 CYS n 1 90 GLN n 1 91 GLN n 1 92 TYR n 1 93 GLY n 1 94 THR n 1 95 SER n 1 96 PRO n 1 97 THR n 1 98 PHE n 1 99 GLY n 1 100 GLN n 1 101 GLY n 1 102 THR n 1 103 LYS n 1 104 VAL n 1 105 GLU n 1 106 ILE n 1 107 LYS n 1 108 ARG n 1 109 THR n 1 110 VAL n 1 111 ALA n 1 112 ALA n 1 113 PRO n 1 114 SER n 1 115 VAL n 1 116 PHE n 1 117 ILE n 1 118 PHE n 1 119 PRO n 1 120 PRO n 1 121 SER n 1 122 ASP n 1 123 GLU n 1 124 GLN n 1 125 LEU n 1 126 LYS n 1 127 SER n 1 128 GLY n 1 129 THR n 1 130 ALA n 1 131 SER n 1 132 VAL n 1 133 VAL n 1 134 CYS n 1 135 LEU n 1 136 LEU n 1 137 ASN n 1 138 ASN n 1 139 PHE n 1 140 TYR n 1 141 PRO n 1 142 ARG n 1 143 GLU n 1 144 ALA n 1 145 LYS n 1 146 VAL n 1 147 GLN n 1 148 TRP n 1 149 LYS n 1 150 VAL n 1 151 ASP n 1 152 ASN n 1 153 ALA n 1 154 LEU n 1 155 GLN n 1 156 SER n 1 157 GLY n 1 158 ASN n 1 159 SER n 1 160 GLN n 1 161 GLU n 1 162 SER n 1 163 VAL n 1 164 THR n 1 165 GLU n 1 166 GLN n 1 167 ASP n 1 168 SER n 1 169 LYS n 1 170 ASP n 1 171 SER n 1 172 THR n 1 173 TYR n 1 174 SER n 1 175 LEU n 1 176 SER n 1 177 SER n 1 178 THR n 1 179 LEU n 1 180 THR n 1 181 LEU n 1 182 SER n 1 183 LYS n 1 184 ALA n 1 185 ASP n 1 186 TYR n 1 187 GLU n 1 188 LYS n 1 189 HIS n 1 190 LYS n 1 191 VAL n 1 192 TYR n 1 193 ALA n 1 194 CYS n 1 195 GLU n 1 196 VAL n 1 197 THR n 1 198 HIS n 1 199 GLN n 1 200 GLY n 1 201 LEU n 1 202 SER n 1 203 SER n 1 204 PRO n 1 205 VAL n 1 206 THR n 1 207 LYS n 1 208 SER n 1 209 PHE n 1 210 ASN n 1 211 ARG n 1 212 GLY n 1 213 GLU n 1 214 CYS n 2 1 GLN n 2 2 VAL n 2 3 GLN n 2 4 LEU n 2 5 GLN n 2 6 GLN n 2 7 TRP n 2 8 GLY n 2 9 ALA n 2 10 GLY n 2 11 LEU n 2 12 LEU n 2 13 LYS n 2 14 PRO n 2 15 SER n 2 16 GLU n 2 17 THR n 2 18 LEU n 2 19 SER n 2 20 LEU n 2 21 THR n 2 22 CYS n 2 23 ALA n 2 24 VAL n 2 25 TYR n 2 26 ASN n 2 27 GLU n 2 28 SER n 2 29 LEU n 2 30 SER n 2 31 ALA n 2 32 PHE n 2 33 SER n 2 34 TRP n 2 35 SER n 2 36 TRP n 2 37 ILE n 2 38 ARG n 2 39 GLN n 2 40 PHE n 2 41 PRO n 2 42 GLY n 2 43 GLN n 2 44 GLY n 2 45 LEU n 2 46 GLU n 2 47 TRP n 2 48 ILE n 2 49 GLY n 2 50 GLU n 2 51 ILE n 2 52 ASP n 2 53 HIS n 2 54 THR n 2 55 THR n 2 56 SER n 2 57 SER n 2 58 ASN n 2 59 TYR n 2 60 ASN n 2 61 PRO n 2 62 SER n 2 63 LEU n 2 64 LYS n 2 65 ARG n 2 66 ARG n 2 67 ILE n 2 68 ASN n 2 69 ILE n 2 70 SER n 2 71 ILE n 2 72 ASP n 2 73 THR n 2 74 SER n 2 75 LYS n 2 76 LYS n 2 77 GLN n 2 78 PHE n 2 79 SER n 2 80 LEU n 2 81 LYS n 2 82 LEU n 2 83 TYR n 2 84 SER n 2 85 VAL n 2 86 THR n 2 87 ALA n 2 88 ALA n 2 89 ASP n 2 90 THR n 2 91 ALA n 2 92 VAL n 2 93 TYR n 2 94 TYR n 2 95 CYS n 2 96 ALA n 2 97 ARG n 2 98 GLY n 2 99 GLY n 2 100 ARG n 2 101 LYS n 2 102 VAL n 2 103 TYR n 2 104 HIS n 2 105 ALA n 2 106 TYR n 2 107 TRP n 2 108 SER n 2 109 GLY n 2 110 TYR n 2 111 VAL n 2 112 ASN n 2 113 ASN n 2 114 CYS n 2 115 PHE n 2 116 ASP n 2 117 PRO n 2 118 TRP n 2 119 GLY n 2 120 GLN n 2 121 GLY n 2 122 THR n 2 123 LEU n 2 124 VAL n 2 125 THR n 2 126 VAL n 2 127 SER n 2 128 SER n 2 129 ALA n 2 130 SER n 2 131 THR n 2 132 LYS n 2 133 GLY n 2 134 PRO n 2 135 SER n 2 136 VAL n 2 137 PHE n 2 138 PRO n 2 139 LEU n 2 140 ALA n 2 141 PRO n 2 142 SER n 2 143 SER n 2 144 LYS n 2 145 SER n 2 146 THR n 2 147 SER n 2 148 GLY n 2 149 GLY n 2 150 THR n 2 151 ALA n 2 152 ALA n 2 153 LEU n 2 154 GLY n 2 155 CYS n 2 156 LEU n 2 157 VAL n 2 158 LYS n 2 159 ASP n 2 160 TYR n 2 161 PHE n 2 162 PRO n 2 163 GLU n 2 164 PRO n 2 165 VAL n 2 166 THR n 2 167 VAL n 2 168 SER n 2 169 TRP n 2 170 ASN n 2 171 SER n 2 172 GLY n 2 173 ALA n 2 174 LEU n 2 175 THR n 2 176 SER n 2 177 GLY n 2 178 VAL n 2 179 HIS n 2 180 THR n 2 181 PHE n 2 182 PRO n 2 183 ALA n 2 184 VAL n 2 185 LEU n 2 186 GLN n 2 187 SER n 2 188 SER n 2 189 GLY n 2 190 LEU n 2 191 TYR n 2 192 SER n 2 193 LEU n 2 194 SER n 2 195 SER n 2 196 VAL n 2 197 VAL n 2 198 THR n 2 199 VAL n 2 200 PRO n 2 201 SER n 2 202 SER n 2 203 SER n 2 204 LEU n 2 205 GLY n 2 206 THR n 2 207 GLN n 2 208 THR n 2 209 TYR n 2 210 ILE n 2 211 CYS n 2 212 ASN n 2 213 VAL n 2 214 ASN n 2 215 HIS n 2 216 LYS n 2 217 PRO n 2 218 SER n 2 219 ASN n 2 220 THR n 2 221 LYS n 2 222 VAL n 2 223 ASP n 2 224 LYS n 2 225 ARG n 2 226 VAL n 2 227 GLU n 2 228 PRO n 2 229 LYS n 2 230 SER n 2 231 CYS n 2 232 ASP 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' 1 214 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample 'Biological sequence' 1 232 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin 1 PDB 5BZW 5BZW ? 1 ? 1 2 PDB 5BZW 5BZW ? 2 ? 1 # 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 5BZW A 1 ? 214 ? 5BZW 1 ? 214 ? 1 214 2 2 5BZW B 1 ? 232 ? 5BZW 1 ? 217 ? 1 217 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 5BZW _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 2.51 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 51.08 _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 ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 293.15 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '20% (w/v) PEG 3350, 10% (v/v) ethylene glycol and 0.2M ammonium sulfate' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 273.15 _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 'PSI 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 2015-05-22 # _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 0.979 _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 'SSRL BEAMLINE BL12-2' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.979 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL12-2 _diffrn_source.pdbx_synchrotron_site SSRL # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5BZW _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.9 _reflns.d_resolution_low 43.629 _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 11743 _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 99.5 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 13.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value 0.28 _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 9.8 _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 2.90 _reflns_shell.d_res_low 2.95 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 2.8 _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 99.8 _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 0.993 _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 14.6 _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 5BZW _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 11669 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.35 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 43.629 _refine.ls_d_res_high 2.900 _refine.ls_percent_reflns_obs 99.34 _refine.ls_R_factor_obs 0.2364 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2333 _refine.ls_R_factor_R_free 0.2970 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.02 _refine.ls_number_reflns_R_free 586 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model 1RRH _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.41 _refine.pdbx_overall_phase_error 27.17 _refine.overall_SU_B ? _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 3372 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 39 _refine_hist.number_atoms_solvent 1 _refine_hist.number_atoms_total 3412 _refine_hist.d_res_high 2.900 _refine_hist.d_res_low 43.629 # 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 f_bond_d 0.002 ? ? 3450 'X-RAY DIFFRACTION' ? f_angle_d 0.664 ? ? 4692 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 11.545 ? ? 1235 'X-RAY DIFFRACTION' ? f_chiral_restr 0.026 ? ? 532 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 601 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.9000 3.1918 2692 0.2820 100.00 0.3641 . . 154 . . . . 'X-RAY DIFFRACTION' . 3.1918 3.6534 2669 0.2652 99.00 0.3473 . . 156 . . . . 'X-RAY DIFFRACTION' . 3.6534 4.6022 2797 0.2107 100.00 0.2991 . . 128 . . . . 'X-RAY DIFFRACTION' . 4.6022 43.6337 2925 0.2119 99.00 0.2275 . . 148 . . . . # _struct.entry_id 5BZW _struct.title 'Crystal Structure of PCDN-27B, an antibody from the PCDN family of HIV-1 antibodies' _struct.pdbx_descriptor '2B3 Fab light chain, 2B3 Fab heavy chain' _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 5BZW _struct_keywords.text 'HIV, Antibody, Fab, IMMUNE SYSTEM' _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 5 ? # 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 SER A 30 ? LYS A 32 ? SER A 29 LYS A 31 5 ? 3 HELX_P HELX_P2 AA2 SER A 121 ? LYS A 126 ? SER A 121 LYS A 126 1 ? 6 HELX_P HELX_P3 AA3 LYS A 183 ? HIS A 189 ? LYS A 183 HIS A 189 1 ? 7 HELX_P HELX_P4 AA4 PRO B 61 ? ARG B 65 ? PRO B 61 ARG B 65 5 ? 5 HELX_P HELX_P5 AA5 THR B 86 ? THR B 90 ? THR B 83 THR B 87 5 ? 5 HELX_P HELX_P6 AA6 LYS B 144 ? GLY B 148 ? LYS B 129 GLY B 133 5 ? 5 HELX_P HELX_P7 AA7 SER B 171 ? ALA B 173 ? SER B 156 ALA B 158 5 ? 3 HELX_P HELX_P8 AA8 SER B 202 ? LEU B 204 ? SER B 187 LEU B 189 5 ? 3 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 23 SG ? ? ? 1_555 A CYS 89 SG ? ? A CYS 23 A CYS 88 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? A CYS 134 SG ? ? ? 1_555 A CYS 194 SG ? ? A CYS 134 A CYS 194 1_555 ? ? ? ? ? ? ? 2.028 ? disulf3 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 95 SG ? ? B CYS 22 B CYS 92 1_555 ? ? ? ? ? ? ? 2.032 ? disulf4 disulf ? ? B CYS 155 SG ? ? ? 1_555 B CYS 211 SG ? ? B CYS 140 B CYS 196 1_555 ? ? ? ? ? ? ? 2.031 ? covale1 covale one ? B ASN 26 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 26 B NAG 305 1_555 ? ? ? ? ? ? ? 1.289 ? # 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 SER 7 A . ? SER 7 A PRO 8 A ? PRO 8 A 1 -7.83 2 TYR 140 A . ? TYR 140 A PRO 141 A ? PRO 141 A 1 1.76 3 HIS 104 B . A HIS 100 B ALA 105 B B ALA 100 B 1 3.92 4 ALA 105 B . B ALA 100 B TYR 106 B C TYR 100 B 1 -5.91 5 ASP 116 B . ? ASP 101 B PRO 117 B ? PRO 102 B 1 -6.98 6 PHE 161 B . ? PHE 146 B PRO 162 B ? PRO 147 B 1 -24.89 7 GLU 163 B . ? GLU 148 B PRO 164 B ? PRO 149 B 1 -0.57 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 3 ? AA2 ? 6 ? AA3 ? 4 ? AA4 ? 4 ? AA5 ? 4 ? AA6 ? 4 ? AA7 ? 6 ? AA8 ? 4 ? AA9 ? 4 ? AB1 ? 4 ? AB2 ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA2 1 2 ? parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA2 4 5 ? anti-parallel AA2 5 6 ? anti-parallel AA3 1 2 ? parallel AA3 2 3 ? anti-parallel AA3 3 4 ? anti-parallel AA4 1 2 ? anti-parallel AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA5 1 2 ? anti-parallel AA5 2 3 ? anti-parallel AA5 3 4 ? anti-parallel AA6 1 2 ? anti-parallel AA6 2 3 ? anti-parallel AA6 3 4 ? anti-parallel AA7 1 2 ? parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA7 5 6 ? anti-parallel AA8 1 2 ? parallel AA8 2 3 ? anti-parallel AA8 3 4 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel AB1 1 2 ? anti-parallel AB1 2 3 ? anti-parallel AB1 3 4 ? anti-parallel AB2 1 2 ? anti-parallel AB2 2 3 ? 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 4 ? SER A 7 ? LEU A 4 SER A 7 AA1 2 ALA A 19 ? VAL A 29 ? ALA A 19 VAL A 28 AA1 3 PHE A 63 ? ILE A 76 ? PHE A 62 ILE A 75 AA2 1 THR A 10 ? LEU A 13 ? THR A 10 LEU A 13 AA2 2 THR A 102 ? ILE A 106 ? THR A 102 ILE A 106 AA2 3 ALA A 85 ? GLN A 91 ? ALA A 84 GLN A 90 AA2 4 LEU A 34 ? GLN A 39 ? LEU A 33 GLN A 38 AA2 5 ARG A 46 ? TYR A 50 ? ARG A 45 TYR A 49 AA2 6 LEU A 54 ? ARG A 55 ? LEU A 53 ARG A 54 AA3 1 THR A 10 ? LEU A 13 ? THR A 10 LEU A 13 AA3 2 THR A 102 ? ILE A 106 ? THR A 102 ILE A 106 AA3 3 ALA A 85 ? GLN A 91 ? ALA A 84 GLN A 90 AA3 4 THR A 97 ? PHE A 98 ? THR A 97 PHE A 98 AA4 1 SER A 114 ? PHE A 118 ? SER A 114 PHE A 118 AA4 2 THR A 129 ? PHE A 139 ? THR A 129 PHE A 139 AA4 3 TYR A 173 ? SER A 182 ? TYR A 173 SER A 182 AA4 4 SER A 159 ? VAL A 163 ? SER A 159 VAL A 163 AA5 1 ALA A 153 ? LEU A 154 ? ALA A 153 LEU A 154 AA5 2 LYS A 145 ? VAL A 150 ? LYS A 145 VAL A 150 AA5 3 VAL A 191 ? THR A 197 ? VAL A 191 THR A 197 AA5 4 VAL A 205 ? ASN A 210 ? VAL A 205 ASN A 210 AA6 1 LEU B 4 ? GLY B 8 ? LEU B 4 GLY B 8 AA6 2 LEU B 18 ? VAL B 24 ? LEU B 18 VAL B 24 AA6 3 GLN B 77 ? LEU B 82 ? GLN B 77 LEU B 82 AA6 4 ILE B 67 ? ASP B 72 ? ILE B 67 ASP B 72 AA7 1 LEU B 11 ? LEU B 12 ? LEU B 11 LEU B 12 AA7 2 THR B 122 ? VAL B 126 ? THR B 107 VAL B 111 AA7 3 ALA B 91 ? VAL B 102 ? ALA B 88 VAL B 99 AA7 4 PHE B 32 ? GLN B 39 ? PHE B 32 GLN B 39 AA7 5 LEU B 45 ? ILE B 51 ? LEU B 45 ILE B 51 AA7 6 SER B 57 ? TYR B 59 ? SER B 57 TYR B 59 AA8 1 LEU B 11 ? LEU B 12 ? LEU B 11 LEU B 12 AA8 2 THR B 122 ? VAL B 126 ? THR B 107 VAL B 111 AA8 3 ALA B 91 ? VAL B 102 ? ALA B 88 VAL B 99 AA8 4 GLY B 109 F TYR B 110 G GLY B 100 TYR B 100 AA9 1 SER B 135 ? LEU B 139 ? SER B 120 LEU B 124 AA9 2 THR B 150 ? TYR B 160 ? THR B 135 TYR B 145 AA9 3 TYR B 191 ? PRO B 200 ? TYR B 176 PRO B 185 AA9 4 VAL B 178 ? THR B 180 ? VAL B 163 THR B 165 AB1 1 SER B 135 ? LEU B 139 ? SER B 120 LEU B 124 AB1 2 THR B 150 ? TYR B 160 ? THR B 135 TYR B 145 AB1 3 TYR B 191 ? PRO B 200 ? TYR B 176 PRO B 185 AB1 4 VAL B 184 ? LEU B 185 ? VAL B 169 LEU B 170 AB2 1 THR B 166 ? TRP B 169 ? THR B 151 TRP B 154 AB2 2 TYR B 209 ? HIS B 215 ? TYR B 194 HIS B 200 AB2 3 THR B 220 ? VAL B 226 ? THR B 205 VAL B 211 # 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 THR A 5 ? N THR A 5 O ARG A 24 ? O ARG A 24 AA1 2 3 N LEU A 21 ? N LEU A 21 O LEU A 74 ? O LEU A 73 AA2 1 2 N LEU A 11 ? N LEU A 11 O GLU A 105 ? O GLU A 105 AA2 2 3 O VAL A 104 ? O VAL A 104 N ALA A 85 ? N ALA A 84 AA2 3 4 O GLN A 90 ? O GLN A 89 N ALA A 35 ? N ALA A 34 AA2 4 5 N TRP A 36 ? N TRP A 35 O MET A 49 ? O MET A 48 AA2 5 6 N TYR A 50 ? N TYR A 49 O LEU A 54 ? O LEU A 53 AA3 1 2 N LEU A 11 ? N LEU A 11 O GLU A 105 ? O GLU A 105 AA3 2 3 O VAL A 104 ? O VAL A 104 N ALA A 85 ? N ALA A 84 AA3 3 4 N GLN A 91 ? N GLN A 90 O THR A 97 ? O THR A 97 AA4 1 2 N PHE A 116 ? N PHE A 116 O LEU A 135 ? O LEU A 135 AA4 2 3 N ALA A 130 ? N ALA A 130 O LEU A 181 ? O LEU A 181 AA4 3 4 O THR A 178 ? O THR A 178 N GLN A 160 ? N GLN A 160 AA5 1 2 O ALA A 153 ? O ALA A 153 N VAL A 150 ? N VAL A 150 AA5 2 3 N LYS A 145 ? N LYS A 145 O THR A 197 ? O THR A 197 AA5 3 4 N CYS A 194 ? N CYS A 194 O LYS A 207 ? O LYS A 207 AA6 1 2 N GLN B 5 ? N GLN B 5 O ALA B 23 ? O ALA B 23 AA6 2 3 N LEU B 18 ? N LEU B 18 O LEU B 82 ? O LEU B 82 AA6 3 4 O GLN B 77 ? O GLN B 77 N ASP B 72 ? N ASP B 72 AA7 1 2 N LEU B 12 ? N LEU B 12 O THR B 125 ? O THR B 110 AA7 2 3 O VAL B 124 ? O VAL B 109 N ALA B 91 ? N ALA B 88 AA7 3 4 O TYR B 94 ? O TYR B 91 N ILE B 37 ? N ILE B 37 AA7 4 5 N TRP B 36 ? N TRP B 36 O ILE B 48 ? O ILE B 48 AA7 5 6 N GLU B 50 ? N GLU B 50 O ASN B 58 ? O ASN B 58 AA8 1 2 N LEU B 12 ? N LEU B 12 O THR B 125 ? O THR B 110 AA8 2 3 O VAL B 124 ? O VAL B 109 N ALA B 91 ? N ALA B 88 AA8 3 4 N VAL B 102 ? N VAL B 99 O GLY B 109 F O GLY B 100 AA9 1 2 N PHE B 137 ? N PHE B 122 O LEU B 156 ? O LEU B 141 AA9 2 3 N ALA B 151 ? N ALA B 136 O VAL B 199 ? O VAL B 184 AA9 3 4 O VAL B 196 ? O VAL B 181 N HIS B 179 ? N HIS B 164 AB1 1 2 N PHE B 137 ? N PHE B 122 O LEU B 156 ? O LEU B 141 AB1 2 3 N ALA B 151 ? N ALA B 136 O VAL B 199 ? O VAL B 184 AB1 3 4 O SER B 192 ? O SER B 177 N VAL B 184 ? N VAL B 169 AB2 1 2 N SER B 168 ? N SER B 153 O ASN B 212 ? O ASN B 197 AB2 2 3 N VAL B 213 ? N VAL B 198 O VAL B 222 ? O VAL B 207 # 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 SO4 301 ? 2 'binding site for residue SO4 A 301' AC2 Software B SO4 301 ? 1 'binding site for residue SO4 B 301' AC3 Software B SO4 302 ? 3 'binding site for residue SO4 B 302' AC4 Software B SO4 303 ? 5 'binding site for residue SO4 B 303' AC5 Software B SO4 304 ? 4 'binding site for residue SO4 B 304' AC6 Software B NAG 305 ? 5 'binding site for Mono-Saccharide NAG B 305 bound to ASN B 26' # 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 2 SER A 53 ? SER A 52 . ? 1_555 ? 2 AC1 2 HOH I . ? HOH A 401 . ? 1_555 ? 3 AC2 1 ARG A 211 ? ARG A 211 . ? 6_655 ? 4 AC3 3 HIS B 53 ? HIS B 53 . ? 1_555 ? 5 AC3 3 THR B 54 ? THR B 54 . ? 1_555 ? 6 AC3 3 TYR B 103 ? TYR B 100 . ? 1_555 ? 7 AC4 5 ARG A 55 ? ARG A 54 . ? 8_555 ? 8 AC4 5 SER B 28 ? SER B 28 . ? 1_555 ? 9 AC4 5 LEU B 29 ? LEU B 29 . ? 1_555 ? 10 AC4 5 SER B 30 ? SER B 30 . ? 1_555 ? 11 AC4 5 LYS B 76 ? LYS B 76 . ? 1_555 ? 12 AC5 4 ARG B 97 ? ARG B 94 . ? 1_555 ? 13 AC5 4 ARG B 97 ? ARG B 94 . ? 8_555 ? 14 AC5 4 ARG B 100 ? ARG B 97 . ? 1_555 ? 15 AC5 4 ARG B 100 ? ARG B 97 . ? 8_555 ? 16 AC6 5 THR A 57 ? THR A 56 . ? 8_555 ? 17 AC6 5 GLY A 58 ? GLY A 57 . ? 8_555 ? 18 AC6 5 GLN B 1 ? GLN B 1 . ? 1_555 ? 19 AC6 5 GLN B 3 ? GLN B 3 . ? 1_555 ? 20 AC6 5 ASN B 26 ? ASN B 26 . ? 1_555 ? # _atom_sites.entry_id 5BZW _atom_sites.fract_transf_matrix[1][1] 0.011191 _atom_sites.fract_transf_matrix[1][2] 0.006461 _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] 0.012923 _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] 0.004733 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # 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 . GLU A 1 1 ? 46.265 18.054 -14.168 1.00 68.79 ? 1 GLU A N 1 ATOM 2 C CA . GLU A 1 1 ? 47.264 18.101 -15.230 1.00 50.93 ? 1 GLU A CA 1 ATOM 3 C C . GLU A 1 1 ? 46.925 17.116 -16.344 1.00 39.71 ? 1 GLU A C 1 ATOM 4 O O . GLU A 1 1 ? 47.234 17.355 -17.512 1.00 46.98 ? 1 GLU A O 1 ATOM 5 C CB . GLU A 1 1 ? 48.656 17.808 -14.667 1.00 49.98 ? 1 GLU A CB 1 ATOM 6 C CG . GLU A 1 1 ? 49.787 17.965 -15.674 1.00 56.51 ? 1 GLU A CG 1 ATOM 7 C CD . GLU A 1 1 ? 51.149 17.671 -15.071 1.00 76.39 ? 1 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 1 ? 52.132 17.569 -15.837 1.00 84.88 ? 1 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 1 ? 51.235 17.538 -13.831 1.00 98.31 ? 1 GLU A OE2 1 ATOM 10 N N . ILE A 1 2 ? 46.280 16.014 -15.977 1.00 28.36 ? 2 ILE A N 1 ATOM 11 C CA . ILE A 1 2 ? 45.885 15.000 -16.948 1.00 24.64 ? 2 ILE A CA 1 ATOM 12 C C . ILE A 1 2 ? 44.558 15.359 -17.610 1.00 22.17 ? 2 ILE A C 1 ATOM 13 O O . ILE A 1 2 ? 43.543 15.522 -16.934 1.00 21.53 ? 2 ILE A O 1 ATOM 14 C CB . ILE A 1 2 ? 45.763 13.608 -16.299 1.00 19.72 ? 2 ILE A CB 1 ATOM 15 C CG1 . ILE A 1 2 ? 47.106 13.170 -15.715 1.00 33.61 ? 2 ILE A CG1 1 ATOM 16 C CG2 . ILE A 1 2 ? 45.281 12.589 -17.317 1.00 21.34 ? 2 ILE A CG2 1 ATOM 17 C CD1 . ILE A 1 2 ? 47.091 11.776 -15.133 1.00 23.25 ? 2 ILE A CD1 1 ATOM 18 N N . VAL A 1 3 ? 44.573 15.479 -18.934 1.00 21.55 ? 3 VAL A N 1 ATOM 19 C CA . VAL A 1 3 ? 43.368 15.792 -19.694 1.00 20.05 ? 3 VAL A CA 1 ATOM 20 C C . VAL A 1 3 ? 42.770 14.531 -20.309 1.00 25.58 ? 3 VAL A C 1 ATOM 21 O O . VAL A 1 3 ? 43.467 13.761 -20.968 1.00 32.86 ? 3 VAL A O 1 ATOM 22 C CB . VAL A 1 3 ? 43.655 16.815 -20.812 1.00 14.08 ? 3 VAL A CB 1 ATOM 23 C CG1 . VAL A 1 3 ? 42.434 16.998 -21.698 1.00 9.91 ? 3 VAL A CG1 1 ATOM 24 C CG2 . VAL A 1 3 ? 44.089 18.144 -20.217 1.00 12.93 ? 3 VAL A CG2 1 ATOM 25 N N . LEU A 1 4 ? 41.476 14.324 -20.085 1.00 23.30 ? 4 LEU A N 1 ATOM 26 C CA . LEU A 1 4 ? 40.777 13.170 -20.638 1.00 14.40 ? 4 LEU A CA 1 ATOM 27 C C . LEU A 1 4 ? 39.949 13.568 -21.854 1.00 15.17 ? 4 LEU A C 1 ATOM 28 O O . LEU A 1 4 ? 39.125 14.480 -21.783 1.00 13.15 ? 4 LEU A O 1 ATOM 29 C CB . LEU A 1 4 ? 39.884 12.523 -19.577 1.00 15.36 ? 4 LEU A CB 1 ATOM 30 C CG . LEU A 1 4 ? 40.478 11.370 -18.763 1.00 14.13 ? 4 LEU A CG 1 ATOM 31 C CD1 . LEU A 1 4 ? 41.833 11.739 -18.186 1.00 19.16 ? 4 LEU A CD1 1 ATOM 32 C CD2 . LEU A 1 4 ? 39.527 10.957 -17.652 1.00 13.03 ? 4 LEU A CD2 1 ATOM 33 N N . THR A 1 5 ? 40.175 12.883 -22.970 1.00 19.18 ? 5 THR A N 1 ATOM 34 C CA . THR A 1 5 ? 39.439 13.158 -24.199 1.00 14.55 ? 5 THR A CA 1 ATOM 35 C C . THR A 1 5 ? 38.598 11.955 -24.610 1.00 18.50 ? 5 THR A C 1 ATOM 36 O O . THR A 1 5 ? 39.134 10.901 -24.951 1.00 22.26 ? 5 THR A O 1 ATOM 37 C CB . THR A 1 5 ? 40.385 13.528 -25.354 1.00 18.84 ? 5 THR A CB 1 ATOM 38 O OG1 . THR A 1 5 ? 41.207 14.635 -24.965 1.00 41.19 ? 5 THR A OG1 1 ATOM 39 C CG2 . THR A 1 5 ? 39.588 13.903 -26.594 1.00 22.74 ? 5 THR A CG2 1 ATOM 40 N N . GLN A 1 6 ? 37.281 12.111 -24.595 1.00 16.27 ? 6 GLN A N 1 ATOM 41 C CA . GLN A 1 6 ? 36.367 11.034 -24.974 1.00 16.44 ? 6 GLN A CA 1 ATOM 42 C C . GLN A 1 6 ? 35.933 11.132 -26.425 1.00 18.31 ? 6 GLN A C 1 ATOM 43 O O . GLN A 1 6 ? 35.792 12.220 -26.959 1.00 24.44 ? 6 GLN A O 1 ATOM 44 C CB . GLN A 1 6 ? 35.125 11.016 -24.086 1.00 16.32 ? 6 GLN A CB 1 ATOM 45 C CG . GLN A 1 6 ? 35.389 11.204 -22.615 1.00 16.52 ? 6 GLN A CG 1 ATOM 46 C CD . GLN A 1 6 ? 34.202 10.847 -21.766 1.00 24.96 ? 6 GLN A CD 1 ATOM 47 O OE1 . GLN A 1 6 ? 33.798 11.602 -20.909 1.00 22.66 ? 6 GLN A OE1 1 ATOM 48 N NE2 . GLN A 1 6 ? 33.646 9.688 -22.000 1.00 22.96 ? 6 GLN A NE2 1 ATOM 49 N N . SER A 1 7 ? 35.758 9.982 -27.062 1.00 24.74 ? 7 SER A N 1 ATOM 50 C CA . SER A 1 7 ? 35.261 9.905 -28.424 1.00 17.84 ? 7 SER A CA 1 ATOM 51 C C . SER A 1 7 ? 34.300 8.729 -28.566 1.00 16.16 ? 7 SER A C 1 ATOM 52 O O . SER A 1 7 ? 34.496 7.733 -27.908 1.00 24.77 ? 7 SER A O 1 ATOM 53 C CB . SER A 1 7 ? 36.421 9.737 -29.394 1.00 16.74 ? 7 SER A CB 1 ATOM 54 O OG . SER A 1 7 ? 36.177 10.445 -30.590 1.00 37.18 ? 7 SER A OG 1 ATOM 55 N N . PRO A 1 8 ? 33.225 8.775 -29.478 1.00 14.07 ? 8 PRO A N 1 ATOM 56 C CA . PRO A 1 8 ? 32.992 10.071 -30.133 1.00 18.65 ? 8 PRO A CA 1 ATOM 57 C C . PRO A 1 8 ? 32.167 11.039 -29.291 1.00 26.75 ? 8 PRO A C 1 ATOM 58 O O . PRO A 1 8 ? 31.676 10.696 -28.230 1.00 24.58 ? 8 PRO A O 1 ATOM 59 C CB . PRO A 1 8 ? 32.229 9.689 -31.381 1.00 20.00 ? 8 PRO A CB 1 ATOM 60 C CG . PRO A 1 8 ? 31.301 8.664 -30.915 1.00 20.00 ? 8 PRO A CG 1 ATOM 61 C CD . PRO A 1 8 ? 32.141 7.812 -30.035 1.00 20.00 ? 8 PRO A CD 1 ATOM 62 N N . GLY A 1 9 ? 32.035 12.267 -29.750 1.00 18.24 ? 9 GLY A N 1 ATOM 63 C CA . GLY A 1 9 ? 31.235 13.220 -29.004 1.00 19.69 ? 9 GLY A CA 1 ATOM 64 C C . GLY A 1 9 ? 29.793 12.772 -28.872 1.00 31.13 ? 9 GLY A C 1 ATOM 65 O O . GLY A 1 9 ? 29.198 12.871 -27.799 1.00 31.36 ? 9 GLY A O 1 ATOM 66 N N . THR A 1 10 ? 29.232 12.271 -29.969 1.00 37.86 ? 10 THR A N 1 ATOM 67 C CA . THR A 1 10 ? 27.853 11.799 -29.976 1.00 20.71 ? 10 THR A CA 1 ATOM 68 C C . THR A 1 10 ? 27.759 10.421 -30.624 1.00 17.67 ? 10 THR A C 1 ATOM 69 O O . THR A 1 10 ? 28.490 10.118 -31.567 1.00 20.01 ? 10 THR A O 1 ATOM 70 C CB . THR A 1 10 ? 26.927 12.779 -30.717 1.00 25.62 ? 10 THR A CB 1 ATOM 71 O OG1 . THR A 1 10 ? 27.348 14.125 -30.463 1.00 48.07 ? 10 THR A OG1 1 ATOM 72 C CG2 . THR A 1 10 ? 25.487 12.605 -30.257 1.00 36.58 ? 10 THR A CG2 1 ATOM 73 N N . LEU A 1 11 ? 26.857 9.589 -30.114 1.00 14.46 ? 11 LEU A N 1 ATOM 74 C CA . LEU A 1 11 ? 26.706 8.226 -30.608 1.00 12.72 ? 11 LEU A CA 1 ATOM 75 C C . LEU A 1 11 ? 25.232 7.883 -30.807 1.00 17.75 ? 11 LEU A C 1 ATOM 76 O O . LEU A 1 11 ? 24.438 7.962 -29.870 1.00 29.85 ? 11 LEU A O 1 ATOM 77 C CB . LEU A 1 11 ? 27.360 7.239 -29.638 1.00 15.37 ? 11 LEU A CB 1 ATOM 78 C CG . LEU A 1 11 ? 27.725 5.850 -30.165 1.00 27.13 ? 11 LEU A CG 1 ATOM 79 C CD1 . LEU A 1 11 ? 28.775 5.951 -31.261 1.00 23.44 ? 11 LEU A CD1 1 ATOM 80 C CD2 . LEU A 1 11 ? 28.216 4.963 -29.033 1.00 25.32 ? 11 LEU A CD2 1 ATOM 81 N N . SER A 1 12 ? 24.869 7.504 -32.029 1.00 18.71 ? 12 SER A N 1 ATOM 82 C CA . SER A 1 12 ? 23.485 7.169 -32.346 1.00 16.05 ? 12 SER A CA 1 ATOM 83 C C . SER A 1 12 ? 23.369 5.735 -32.855 1.00 24.02 ? 12 SER A C 1 ATOM 84 O O . SER A 1 12 ? 23.810 5.423 -33.961 1.00 37.28 ? 12 SER A O 1 ATOM 85 C CB . SER A 1 12 ? 22.925 8.146 -33.381 1.00 17.90 ? 12 SER A CB 1 ATOM 86 O OG . SER A 1 12 ? 21.549 7.911 -33.614 1.00 19.43 ? 12 SER A OG 1 ATOM 87 N N . LEU A 1 13 ? 22.771 4.867 -32.044 1.00 19.25 ? 13 LEU A N 1 ATOM 88 C CA . LEU A 1 13 ? 22.652 3.454 -32.385 1.00 18.00 ? 13 LEU A CA 1 ATOM 89 C C . LEU A 1 13 ? 21.288 2.883 -32.004 1.00 21.35 ? 13 LEU A C 1 ATOM 90 O O . LEU A 1 13 ? 20.638 3.368 -31.079 1.00 36.79 ? 13 LEU A O 1 ATOM 91 C CB . LEU A 1 13 ? 23.760 2.651 -31.700 1.00 17.00 ? 13 LEU A CB 1 ATOM 92 C CG . LEU A 1 13 ? 25.181 2.846 -32.232 1.00 19.26 ? 13 LEU A CG 1 ATOM 93 C CD1 . LEU A 1 13 ? 26.206 2.370 -31.217 1.00 30.92 ? 13 LEU A CD1 1 ATOM 94 C CD2 . LEU A 1 13 ? 25.354 2.109 -33.548 1.00 24.78 ? 13 LEU A CD2 1 ATOM 95 N N . SER A 1 14 ? 20.864 1.851 -32.726 1.00 21.32 ? 14 SER A N 1 ATOM 96 C CA . SER A 1 14 ? 19.608 1.166 -32.441 1.00 18.90 ? 14 SER A CA 1 ATOM 97 C C . SER A 1 14 ? 19.759 0.268 -31.216 1.00 18.22 ? 14 SER A C 1 ATOM 98 O O . SER A 1 14 ? 20.874 -0.125 -30.873 1.00 25.82 ? 14 SER A O 1 ATOM 99 C CB . SER A 1 14 ? 19.159 0.344 -33.654 1.00 18.11 ? 14 SER A CB 1 ATOM 100 O OG . SER A 1 14 ? 18.860 1.181 -34.757 1.00 26.82 ? 14 SER A OG 1 ATOM 101 N N . PRO A 1 15 ? 18.638 -0.055 -30.547 1.00 16.91 ? 15 PRO A N 1 ATOM 102 C CA . PRO A 1 15 ? 18.717 -0.969 -29.403 1.00 27.56 ? 15 PRO A CA 1 ATOM 103 C C . PRO A 1 15 ? 19.125 -2.373 -29.835 1.00 16.05 ? 15 PRO A C 1 ATOM 104 O O . PRO A 1 15 ? 18.669 -2.853 -30.873 1.00 14.94 ? 15 PRO A O 1 ATOM 105 C CB . PRO A 1 15 ? 17.292 -0.954 -28.841 1.00 13.21 ? 15 PRO A CB 1 ATOM 106 C CG . PRO A 1 15 ? 16.437 -0.562 -29.992 1.00 11.94 ? 15 PRO A CG 1 ATOM 107 C CD . PRO A 1 15 ? 17.259 0.403 -30.788 1.00 17.07 ? 15 PRO A CD 1 ATOM 108 N N . GLY A 1 16 ? 19.983 -3.012 -29.049 1.00 14.39 ? 16 GLY A N 1 ATOM 109 C CA . GLY A 1 16 ? 20.463 -4.343 -29.369 1.00 18.18 ? 16 GLY A CA 1 ATOM 110 C C . GLY A 1 16 ? 21.848 -4.326 -29.986 1.00 27.90 ? 16 GLY A C 1 ATOM 111 O O . GLY A 1 16 ? 22.457 -5.376 -30.188 1.00 25.07 ? 16 GLY A O 1 ATOM 112 N N . GLU A 1 17 ? 22.347 -3.131 -30.284 1.00 18.94 ? 17 GLU A N 1 ATOM 113 C CA . GLU A 1 17 ? 23.664 -2.984 -30.896 1.00 18.09 ? 17 GLU A CA 1 ATOM 114 C C . GLU A 1 17 ? 24.739 -2.682 -29.856 1.00 17.34 ? 17 GLU A C 1 ATOM 115 O O . GLU A 1 17 ? 24.436 -2.270 -28.737 1.00 20.90 ? 17 GLU A O 1 ATOM 116 C CB . GLU A 1 17 ? 23.640 -1.885 -31.959 1.00 17.89 ? 17 GLU A CB 1 ATOM 117 C CG . GLU A 1 17 ? 22.701 -2.172 -33.119 1.00 28.49 ? 17 GLU A CG 1 ATOM 118 C CD . GLU A 1 17 ? 22.914 -1.231 -34.289 1.00 58.23 ? 17 GLU A CD 1 ATOM 119 O OE1 . GLU A 1 17 ? 23.618 -1.622 -35.244 1.00 49.62 ? 17 GLU A OE1 1 ATOM 120 O OE2 . GLU A 1 17 ? 22.380 -0.102 -34.256 1.00 42.30 ? 17 GLU A OE2 1 ATOM 121 N N . ARG A 1 18 ? 25.995 -2.891 -30.237 1.00 18.13 ? 18 ARG A N 1 ATOM 122 C CA . ARG A 1 18 ? 27.118 -2.698 -29.327 1.00 14.41 ? 18 ARG A CA 1 ATOM 123 C C . ARG A 1 18 ? 27.622 -1.260 -29.362 1.00 17.46 ? 18 ARG A C 1 ATOM 124 O O . ARG A 1 18 ? 27.995 -0.748 -30.418 1.00 20.15 ? 18 ARG A O 1 ATOM 125 C CB . ARG A 1 18 ? 28.256 -3.659 -29.674 1.00 13.26 ? 18 ARG A CB 1 ATOM 126 C CG . ARG A 1 18 ? 28.846 -4.377 -28.472 1.00 25.61 ? 18 ARG A CG 1 ATOM 127 C CD . ARG A 1 18 ? 29.877 -5.411 -28.894 1.00 27.60 ? 18 ARG A CD 1 ATOM 128 N NE . ARG A 1 18 ? 31.146 -4.803 -29.281 1.00 23.40 ? 18 ARG A NE 1 ATOM 129 C CZ . ARG A 1 18 ? 32.256 -4.870 -28.554 1.00 43.99 ? 18 ARG A CZ 1 ATOM 130 N NH1 . ARG A 1 18 ? 33.367 -4.285 -28.980 1.00 29.48 ? 18 ARG A NH1 1 ATOM 131 N NH2 . ARG A 1 18 ? 32.257 -5.529 -27.402 1.00 30.06 ? 18 ARG A NH2 1 ATOM 132 N N . ALA A 1 19 ? 27.630 -0.614 -28.201 1.00 25.37 ? 19 ALA A N 1 ATOM 133 C CA . ALA A 1 19 ? 28.116 0.754 -28.091 1.00 18.38 ? 19 ALA A CA 1 ATOM 134 C C . ALA A 1 19 ? 29.521 0.783 -27.501 1.00 20.96 ? 19 ALA A C 1 ATOM 135 O O . ALA A 1 19 ? 29.721 0.433 -26.338 1.00 37.10 ? 19 ALA A O 1 ATOM 136 C CB . ALA A 1 19 ? 27.169 1.588 -27.247 1.00 18.06 ? 19 ALA A CB 1 ATOM 137 N N . THR A 1 20 ? 30.492 1.197 -28.308 1.00 31.99 ? 20 THR A N 1 ATOM 138 C CA . THR A 1 20 ? 31.870 1.302 -27.848 1.00 17.09 ? 20 THR A CA 1 ATOM 139 C C . THR A 1 20 ? 32.249 2.757 -27.607 1.00 15.96 ? 20 THR A C 1 ATOM 140 O O . THR A 1 20 ? 32.233 3.575 -28.526 1.00 17.45 ? 20 THR A O 1 ATOM 141 C CB . THR A 1 20 ? 32.858 0.684 -28.853 1.00 17.43 ? 20 THR A CB 1 ATOM 142 O OG1 . THR A 1 20 ? 32.665 -0.735 -28.907 1.00 25.26 ? 20 THR A OG1 1 ATOM 143 C CG2 . THR A 1 20 ? 34.290 0.975 -28.435 1.00 20.74 ? 20 THR A CG2 1 ATOM 144 N N . LEU A 1 21 ? 32.588 3.071 -26.361 1.00 18.09 ? 21 LEU A N 1 ATOM 145 C CA . LEU A 1 21 ? 32.967 4.425 -25.980 1.00 17.16 ? 21 LEU A CA 1 ATOM 146 C C . LEU A 1 21 ? 34.451 4.470 -25.635 1.00 21.91 ? 21 LEU A C 1 ATOM 147 O O . LEU A 1 21 ? 34.972 3.559 -24.993 1.00 17.75 ? 21 LEU A O 1 ATOM 148 C CB . LEU A 1 21 ? 32.126 4.912 -24.795 1.00 14.07 ? 21 LEU A CB 1 ATOM 149 C CG . LEU A 1 21 ? 30.700 5.414 -25.050 1.00 8.34 ? 21 LEU A CG 1 ATOM 150 C CD1 . LEU A 1 21 ? 29.800 4.343 -25.645 1.00 18.53 ? 21 LEU A CD1 1 ATOM 151 C CD2 . LEU A 1 21 ? 30.098 5.929 -23.761 1.00 12.24 ? 21 LEU A CD2 1 ATOM 152 N N . SER A 1 22 ? 35.133 5.526 -26.064 1.00 12.88 ? 22 SER A N 1 ATOM 153 C CA . SER A 1 22 ? 36.572 5.629 -25.852 1.00 16.24 ? 22 SER A CA 1 ATOM 154 C C . SER A 1 22 ? 36.932 6.770 -24.906 1.00 17.35 ? 22 SER A C 1 ATOM 155 O O . SER A 1 22 ? 36.189 7.743 -24.779 1.00 21.33 ? 22 SER A O 1 ATOM 156 C CB . SER A 1 22 ? 37.295 5.812 -27.188 1.00 17.29 ? 22 SER A CB 1 ATOM 157 O OG . SER A 1 22 ? 38.702 5.789 -27.015 1.00 41.09 ? 22 SER A OG 1 ATOM 158 N N . CYS A 1 23 ? 38.076 6.636 -24.244 1.00 16.84 ? 23 CYS A N 1 ATOM 159 C CA . CYS A 1 23 ? 38.586 7.675 -23.355 1.00 18.07 ? 23 CYS A CA 1 ATOM 160 C C . CYS A 1 23 ? 40.110 7.658 -23.345 1.00 21.07 ? 23 CYS A C 1 ATOM 161 O O . CYS A 1 23 ? 40.725 6.671 -22.941 1.00 22.66 ? 23 CYS A O 1 ATOM 162 C CB . CYS A 1 23 ? 38.042 7.491 -21.937 1.00 22.65 ? 23 CYS A CB 1 ATOM 163 S SG . CYS A 1 23 ? 38.498 8.809 -20.781 1.00 14.56 ? 23 CYS A SG 1 ATOM 164 N N . ARG A 1 24 ? 40.715 8.752 -23.794 1.00 20.09 ? 24 ARG A N 1 ATOM 165 C CA . ARG A 1 24 ? 42.167 8.843 -23.874 1.00 19.55 ? 24 ARG A CA 1 ATOM 166 C C . ARG A 1 24 ? 42.696 9.938 -22.959 1.00 19.53 ? 24 ARG A C 1 ATOM 167 O O . ARG A 1 24 ? 42.137 11.033 -22.900 1.00 30.14 ? 24 ARG A O 1 ATOM 168 C CB . ARG A 1 24 ? 42.609 9.096 -25.317 1.00 30.21 ? 24 ARG A CB 1 ATOM 169 C CG . ARG A 1 24 ? 42.127 8.037 -26.297 1.00 55.57 ? 24 ARG A CG 1 ATOM 170 C CD . ARG A 1 24 ? 42.531 8.361 -27.728 1.00 51.58 ? 24 ARG A CD 1 ATOM 171 N NE . ARG A 1 24 ? 42.019 7.374 -28.674 1.00 68.79 ? 24 ARG A NE 1 ATOM 172 C CZ . ARG A 1 24 ? 42.190 7.440 -29.990 1.00 56.19 ? 24 ARG A CZ 1 ATOM 173 N NH1 . ARG A 1 24 ? 42.863 8.451 -30.524 1.00 39.13 ? 24 ARG A NH1 1 ATOM 174 N NH2 . ARG A 1 24 ? 41.686 6.495 -30.774 1.00 41.42 ? 24 ARG A NH2 1 ATOM 175 N N . ALA A 1 25 ? 43.801 9.645 -22.304 1.00 20.47 ? 25 ALA A N 1 ATOM 176 C CA . ALA A 1 25 ? 44.389 10.541 -21.350 1.00 19.90 ? 25 ALA A CA 1 ATOM 177 C C . ALA A 1 25 ? 45.682 11.135 -21.850 1.00 19.00 ? 25 ALA A C 1 ATOM 178 O O . ALA A 1 25 ? 46.465 10.483 -22.480 1.00 18.96 ? 25 ALA A O 1 ATOM 179 C CB . ALA A 1 25 ? 44.609 9.827 -20.041 1.00 18.95 ? 25 ALA A CB 1 ATOM 180 N N . SER A 1 26 ? 45.880 12.404 -21.549 1.00 22.36 ? 26 SER A N 1 ATOM 181 C CA . SER A 1 26 ? 47.071 13.142 -21.913 1.00 23.18 ? 26 SER A CA 1 ATOM 182 C C . SER A 1 26 ? 48.307 12.541 -21.280 1.00 26.30 ? 26 SER A C 1 ATOM 183 O O . SER A 1 26 ? 49.375 12.576 -21.850 1.00 40.93 ? 26 SER A O 1 ATOM 184 C CB . SER A 1 26 ? 46.928 14.597 -21.514 1.00 21.46 ? 26 SER A CB 1 ATOM 185 O OG . SER A 1 26 ? 46.896 14.724 -20.123 1.00 23.87 ? 26 SER A OG 1 ATOM 186 N N . GLN A 1 27 ? 48.150 12.033 -20.070 1.00 28.28 ? 27 GLN A N 1 ATOM 187 C CA . GLN A 1 27 ? 49.216 11.402 -19.319 1.00 31.46 ? 27 GLN A CA 1 ATOM 188 C C . GLN A 1 27 ? 48.837 9.979 -18.965 1.00 29.57 ? 27 GLN A C 1 ATOM 189 O O . GLN A 1 27 ? 47.702 9.609 -19.070 1.00 46.01 ? 27 GLN A O 1 ATOM 190 C CB . GLN A 1 27 ? 49.471 12.182 -18.044 1.00 44.62 ? 27 GLN A CB 1 ATOM 191 C CG . GLN A 1 27 ? 50.256 13.467 -18.225 1.00 50.83 ? 27 GLN A CG 1 ATOM 192 C CD . GLN A 1 27 ? 50.599 14.106 -16.901 1.00 64.36 ? 27 GLN A CD 1 ATOM 193 O OE1 . GLN A 1 27 ? 50.196 13.616 -15.853 1.00 63.77 ? 27 GLN A OE1 1 ATOM 194 N NE2 . GLN A 1 27 ? 51.344 15.200 -16.939 1.00 51.25 ? 27 GLN A NE2 1 ATOM 195 N N . SER A 1 28 A 49.799 9.159 -18.588 1.00 31.54 ? 27 SER A N 1 ATOM 196 C CA . SER A 1 28 A 49.501 7.801 -18.144 1.00 38.75 ? 27 SER A CA 1 ATOM 197 C C . SER A 1 28 A 48.693 7.763 -16.871 1.00 36.75 ? 27 SER A C 1 ATOM 198 O O . SER A 1 28 A 48.893 8.573 -15.981 1.00 39.51 ? 27 SER A O 1 ATOM 199 C CB . SER A 1 28 A 50.773 7.017 -17.932 1.00 30.84 ? 27 SER A CB 1 ATOM 200 O OG . SER A 1 28 A 51.436 6.853 -19.156 1.00 53.09 ? 27 SER A OG 1 ATOM 201 N N . VAL A 1 29 ? 47.787 6.805 -16.782 1.00 27.25 ? 28 VAL A N 1 ATOM 202 C CA . VAL A 1 29 ? 46.907 6.718 -15.646 1.00 26.55 ? 28 VAL A CA 1 ATOM 203 C C . VAL A 1 29 ? 47.277 5.546 -14.764 1.00 30.71 ? 28 VAL A C 1 ATOM 204 O O . VAL A 1 29 ? 47.305 4.409 -15.187 1.00 33.91 ? 28 VAL A O 1 ATOM 205 C CB . VAL A 1 29 ? 45.448 6.636 -16.093 1.00 23.20 ? 28 VAL A CB 1 ATOM 206 C CG1 . VAL A 1 29 ? 44.542 6.379 -14.918 1.00 34.51 ? 28 VAL A CG1 1 ATOM 207 C CG2 . VAL A 1 29 ? 45.058 7.936 -16.747 1.00 23.42 ? 28 VAL A CG2 1 ATOM 208 N N . SER A 1 30 ? 47.562 5.853 -13.514 1.00 32.60 ? 29 SER A N 1 ATOM 209 C CA . SER A 1 30 ? 48.194 4.908 -12.628 1.00 36.17 ? 29 SER A CA 1 ATOM 210 C C . SER A 1 30 ? 47.241 3.870 -12.131 1.00 33.77 ? 29 SER A C 1 ATOM 211 O O . SER A 1 30 ? 46.165 4.181 -11.674 1.00 43.49 ? 29 SER A O 1 ATOM 212 C CB . SER A 1 30 ? 48.789 5.639 -11.434 1.00 52.82 ? 29 SER A CB 1 ATOM 213 O OG . SER A 1 30 ? 47.777 6.046 -10.551 1.00 32.11 ? 29 SER A OG 1 ATOM 214 N N . ALA A 1 31 ? 47.636 2.620 -12.273 1.00 33.16 ? 30 ALA A N 1 ATOM 215 C CA . ALA A 1 31 ? 47.088 1.528 -11.523 1.00 33.90 ? 30 ALA A CA 1 ATOM 216 C C . ALA A 1 31 ? 45.585 1.415 -11.582 1.00 32.56 ? 30 ALA A C 1 ATOM 217 O O . ALA A 1 31 ? 44.963 1.035 -10.606 1.00 56.89 ? 30 ALA A O 1 ATOM 218 C CB . ALA A 1 31 ? 47.551 1.621 -10.088 1.00 71.23 ? 30 ALA A CB 1 ATOM 219 N N . LYS A 1 32 ? 44.998 1.680 -12.729 1.00 25.68 ? 31 LYS A N 1 ATOM 220 C CA . LYS A 1 32 ? 43.562 1.488 -12.872 1.00 35.48 ? 31 LYS A CA 1 ATOM 221 C C . LYS A 1 32 ? 42.660 2.465 -12.154 1.00 19.62 ? 31 LYS A C 1 ATOM 222 O O . LYS A 1 32 ? 41.557 2.143 -11.830 1.00 17.76 ? 31 LYS A O 1 ATOM 223 C CB . LYS A 1 32 ? 43.199 0.080 -12.448 1.00 21.27 ? 31 LYS A CB 1 ATOM 224 C CG . LYS A 1 32 ? 43.708 -0.963 -13.401 1.00 22.70 ? 31 LYS A CG 1 ATOM 225 C CD . LYS A 1 32 ? 43.239 -2.327 -12.994 1.00 24.45 ? 31 LYS A CD 1 ATOM 226 C CE . LYS A 1 32 ? 43.480 -3.322 -14.098 1.00 26.84 ? 31 LYS A CE 1 ATOM 227 N NZ . LYS A 1 32 ? 43.355 -4.697 -13.574 1.00 43.07 ? 31 LYS A NZ 1 ATOM 228 N N . ASN A 1 33 ? 43.137 3.665 -11.915 1.00 19.94 ? 32 ASN A N 1 ATOM 229 C CA . ASN A 1 33 ? 42.309 4.687 -11.324 1.00 18.54 ? 32 ASN A CA 1 ATOM 230 C C . ASN A 1 33 ? 41.502 5.397 -12.376 1.00 16.74 ? 32 ASN A C 1 ATOM 231 O O . ASN A 1 33 ? 41.680 6.562 -12.626 1.00 16.73 ? 32 ASN A O 1 ATOM 232 C CB . ASN A 1 33 ? 43.172 5.661 -10.553 1.00 22.48 ? 32 ASN A CB 1 ATOM 233 C CG . ASN A 1 33 ? 43.844 5.017 -9.381 1.00 26.79 ? 32 ASN A CG 1 ATOM 234 O OD1 . ASN A 1 33 ? 44.951 5.353 -9.035 1.00 46.02 ? 32 ASN A OD1 1 ATOM 235 N ND2 . ASN A 1 33 ? 43.174 4.082 -8.767 1.00 24.50 ? 32 ASN A ND2 1 ATOM 236 N N . LEU A 1 34 ? 40.586 4.659 -12.974 1.00 16.11 ? 33 LEU A N 1 ATOM 237 C CA . LEU A 1 34 ? 39.685 5.225 -13.971 1.00 15.69 ? 33 LEU A CA 1 ATOM 238 C C . LEU A 1 34 ? 38.254 4.798 -13.665 1.00 13.94 ? 33 LEU A C 1 ATOM 239 O O . LEU A 1 34 ? 37.999 3.630 -13.371 1.00 21.68 ? 33 LEU A O 1 ATOM 240 C CB . LEU A 1 34 ? 40.094 4.781 -15.379 1.00 15.02 ? 33 LEU A CB 1 ATOM 241 C CG . LEU A 1 34 ? 39.713 5.630 -16.599 1.00 11.22 ? 33 LEU A CG 1 ATOM 242 C CD1 . LEU A 1 34 ? 38.232 5.530 -16.938 1.00 14.61 ? 33 LEU A CD1 1 ATOM 243 C CD2 . LEU A 1 34 ? 40.117 7.081 -16.391 1.00 11.79 ? 33 LEU A CD2 1 ATOM 244 N N . ALA A 1 35 ? 37.324 5.744 -13.736 1.00 14.52 ? 34 ALA A N 1 ATOM 245 C CA . ALA A 1 35 ? 35.924 5.455 -13.447 1.00 12.84 ? 34 ALA A CA 1 ATOM 246 C C . ALA A 1 35 ? 35.002 5.974 -14.544 1.00 12.62 ? 34 ALA A C 1 ATOM 247 O O . ALA A 1 35 ? 35.343 6.914 -15.261 1.00 21.60 ? 34 ALA A O 1 ATOM 248 C CB . ALA A 1 35 ? 35.530 6.048 -12.105 1.00 20.24 ? 34 ALA A CB 1 ATOM 249 N N . TRP A 1 36 ? 33.831 5.357 -14.668 1.00 16.49 ? 35 TRP A N 1 ATOM 250 C CA . TRP A 1 36 ? 32.837 5.779 -15.649 1.00 13.78 ? 35 TRP A CA 1 ATOM 251 C C . TRP A 1 36 ? 31.535 6.174 -14.965 1.00 9.47 ? 35 TRP A C 1 ATOM 252 O O . TRP A 1 36 ? 31.121 5.546 -13.991 1.00 11.12 ? 35 TRP A O 1 ATOM 253 C CB . TRP A 1 36 ? 32.574 4.669 -16.670 1.00 27.08 ? 35 TRP A CB 1 ATOM 254 C CG . TRP A 1 36 ? 33.717 4.418 -17.602 1.00 12.24 ? 35 TRP A CG 1 ATOM 255 C CD1 . TRP A 1 36 ? 34.764 3.566 -17.405 1.00 12.49 ? 35 TRP A CD1 1 ATOM 256 C CD2 . TRP A 1 36 ? 33.928 5.023 -18.883 1.00 12.52 ? 35 TRP A CD2 1 ATOM 257 N NE1 . TRP A 1 36 ? 35.615 3.604 -18.483 1.00 11.89 ? 35 TRP A NE1 1 ATOM 258 C CE2 . TRP A 1 36 ? 35.124 4.491 -19.404 1.00 13.28 ? 35 TRP A CE2 1 ATOM 259 C CE3 . TRP A 1 36 ? 33.223 5.964 -19.639 1.00 16.32 ? 35 TRP A CE3 1 ATOM 260 C CZ2 . TRP A 1 36 ? 35.630 4.868 -20.646 1.00 14.26 ? 35 TRP A CZ2 1 ATOM 261 C CZ3 . TRP A 1 36 ? 33.726 6.336 -20.872 1.00 15.99 ? 35 TRP A CZ3 1 ATOM 262 C CH2 . TRP A 1 36 ? 34.917 5.789 -21.363 1.00 13.41 ? 35 TRP A CH2 1 ATOM 263 N N . TYR A 1 37 ? 30.890 7.216 -15.480 1.00 9.58 ? 36 TYR A N 1 ATOM 264 C CA . TYR A 1 37 ? 29.618 7.667 -14.932 1.00 10.28 ? 36 TYR A CA 1 ATOM 265 C C . TYR A 1 37 ? 28.532 7.694 -16.001 1.00 12.64 ? 36 TYR A C 1 ATOM 266 O O . TYR A 1 37 ? 28.823 7.728 -17.197 1.00 18.02 ? 36 TYR A O 1 ATOM 267 C CB . TYR A 1 37 ? 29.765 9.054 -14.304 1.00 10.11 ? 36 TYR A CB 1 ATOM 268 C CG . TYR A 1 37 ? 30.735 9.103 -13.149 1.00 11.61 ? 36 TYR A CG 1 ATOM 269 C CD1 . TYR A 1 37 ? 30.312 8.849 -11.851 1.00 11.36 ? 36 TYR A CD1 1 ATOM 270 C CD2 . TYR A 1 37 ? 32.074 9.403 -13.355 1.00 13.15 ? 36 TYR A CD2 1 ATOM 271 C CE1 . TYR A 1 37 ? 31.195 8.892 -10.791 1.00 12.35 ? 36 TYR A CE1 1 ATOM 272 C CE2 . TYR A 1 37 ? 32.965 9.448 -12.302 1.00 22.72 ? 36 TYR A CE2 1 ATOM 273 C CZ . TYR A 1 37 ? 32.520 9.192 -11.022 1.00 15.34 ? 36 TYR A CZ 1 ATOM 274 O OH . TYR A 1 37 ? 33.406 9.236 -9.972 1.00 34.72 ? 36 TYR A OH 1 ATOM 275 N N . GLN A 1 38 ? 27.281 7.676 -15.556 1.00 9.71 ? 37 GLN A N 1 ATOM 276 C CA . GLN A 1 38 ? 26.134 7.763 -16.450 1.00 7.36 ? 37 GLN A CA 1 ATOM 277 C C . GLN A 1 38 ? 25.178 8.835 -15.949 1.00 8.55 ? 37 GLN A C 1 ATOM 278 O O . GLN A 1 38 ? 24.775 8.817 -14.786 1.00 11.52 ? 37 GLN A O 1 ATOM 279 C CB . GLN A 1 38 ? 25.417 6.416 -16.545 1.00 7.77 ? 37 GLN A CB 1 ATOM 280 C CG . GLN A 1 38 ? 24.159 6.441 -17.394 1.00 7.80 ? 37 GLN A CG 1 ATOM 281 C CD . GLN A 1 38 ? 23.306 5.206 -17.203 1.00 8.94 ? 37 GLN A CD 1 ATOM 282 O OE1 . GLN A 1 38 ? 22.898 4.885 -16.087 1.00 14.55 ? 37 GLN A OE1 1 ATOM 283 N NE2 . GLN A 1 38 ? 23.033 4.501 -18.294 1.00 15.56 ? 37 GLN A NE2 1 ATOM 284 N N . GLN A 1 39 ? 24.818 9.772 -16.819 1.00 6.66 ? 38 GLN A N 1 ATOM 285 C CA . GLN A 1 39 ? 23.916 10.847 -16.422 1.00 8.02 ? 38 GLN A CA 1 ATOM 286 C C . GLN A 1 39 ? 22.654 10.874 -17.276 1.00 9.92 ? 38 GLN A C 1 ATOM 287 O O . GLN A 1 39 ? 22.625 11.485 -18.345 1.00 23.19 ? 38 GLN A O 1 ATOM 288 C CB . GLN A 1 39 ? 24.626 12.200 -16.492 1.00 9.50 ? 38 GLN A CB 1 ATOM 289 C CG . GLN A 1 39 ? 23.842 13.329 -15.842 1.00 11.38 ? 38 GLN A CG 1 ATOM 290 C CD . GLN A 1 39 ? 24.623 14.625 -15.776 1.00 12.19 ? 38 GLN A CD 1 ATOM 291 O OE1 . GLN A 1 39 ? 24.474 15.406 -14.836 1.00 7.13 ? 38 GLN A OE1 1 ATOM 292 N NE2 . GLN A 1 39 ? 25.458 14.865 -16.780 1.00 8.91 ? 38 GLN A NE2 1 ATOM 293 N N . LYS A 1 40 ? 21.615 10.202 -16.794 1.00 13.68 ? 39 LYS A N 1 ATOM 294 C CA . LYS A 1 40 ? 20.310 10.228 -17.437 1.00 19.03 ? 39 LYS A CA 1 ATOM 295 C C . LYS A 1 40 ? 19.684 11.614 -17.274 1.00 23.00 ? 39 LYS A C 1 ATOM 296 O O . LYS A 1 40 ? 20.051 12.351 -16.358 1.00 22.99 ? 39 LYS A O 1 ATOM 297 C CB . LYS A 1 40 ? 19.409 9.141 -16.846 1.00 20.16 ? 39 LYS A CB 1 ATOM 298 C CG . LYS A 1 40 ? 19.866 7.728 -17.163 1.00 16.96 ? 39 LYS A CG 1 ATOM 299 C CD . LYS A 1 40 ? 18.923 6.690 -16.579 1.00 50.15 ? 39 LYS A CD 1 ATOM 300 C CE . LYS A 1 40 ? 19.368 5.280 -16.948 1.00 26.76 ? 39 LYS A CE 1 ATOM 301 N NZ . LYS A 1 40 ? 18.460 4.243 -16.377 1.00 31.77 ? 39 LYS A NZ 1 ATOM 302 N N . PRO A 1 41 ? 18.752 11.979 -18.173 1.00 32.71 ? 40 PRO A N 1 ATOM 303 C CA . PRO A 1 41 ? 18.095 13.293 -18.148 1.00 39.98 ? 40 PRO A CA 1 ATOM 304 C C . PRO A 1 41 ? 17.525 13.689 -16.785 1.00 38.11 ? 40 PRO A C 1 ATOM 305 O O . PRO A 1 41 ? 16.795 12.914 -16.166 1.00 48.28 ? 40 PRO A O 1 ATOM 306 C CB . PRO A 1 41 ? 16.968 13.129 -19.167 1.00 38.41 ? 40 PRO A CB 1 ATOM 307 C CG . PRO A 1 41 ? 17.506 12.151 -20.143 1.00 50.01 ? 40 PRO A CG 1 ATOM 308 C CD . PRO A 1 41 ? 18.338 11.187 -19.347 1.00 27.33 ? 40 PRO A CD 1 ATOM 309 N N . GLY A 1 42 ? 17.868 14.891 -16.331 1.00 48.41 ? 41 GLY A N 1 ATOM 310 C CA . GLY A 1 42 ? 17.338 15.428 -15.091 1.00 64.87 ? 41 GLY A CA 1 ATOM 311 C C . GLY A 1 42 ? 17.857 14.754 -13.836 1.00 35.33 ? 41 GLY A C 1 ATOM 312 O O . GLY A 1 42 ? 17.308 14.945 -12.751 1.00 50.25 ? 41 GLY A O 1 ATOM 313 N N . GLN A 1 43 ? 18.918 13.966 -13.977 1.00 30.13 ? 42 GLN A N 1 ATOM 314 C CA . GLN A 1 43 ? 19.490 13.257 -12.838 1.00 23.49 ? 42 GLN A CA 1 ATOM 315 C C . GLN A 1 43 ? 20.925 13.685 -12.563 1.00 26.18 ? 42 GLN A C 1 ATOM 316 O O . GLN A 1 43 ? 21.519 14.445 -13.328 1.00 30.81 ? 42 GLN A O 1 ATOM 317 C CB . GLN A 1 43 ? 19.444 11.745 -13.064 1.00 26.78 ? 42 GLN A CB 1 ATOM 318 C CG . GLN A 1 43 ? 18.054 11.136 -13.000 1.00 30.45 ? 42 GLN A CG 1 ATOM 319 C CD . GLN A 1 43 ? 18.084 9.618 -13.052 1.00 39.05 ? 42 GLN A CD 1 ATOM 320 O OE1 . GLN A 1 43 ? 19.149 9.011 -13.171 1.00 46.71 ? 42 GLN A OE1 1 ATOM 321 N NE2 . GLN A 1 43 ? 16.913 8.999 -12.960 1.00 43.38 ? 42 GLN A NE2 1 ATOM 322 N N . THR A 1 44 ? 21.471 13.186 -11.459 1.00 21.06 ? 43 THR A N 1 ATOM 323 C CA . THR A 1 44 ? 22.864 13.419 -11.102 1.00 16.65 ? 43 THR A CA 1 ATOM 324 C C . THR A 1 44 ? 23.723 12.293 -11.666 1.00 16.53 ? 43 THR A C 1 ATOM 325 O O . THR A 1 44 ? 23.221 11.192 -11.896 1.00 16.19 ? 43 THR A O 1 ATOM 326 C CB . THR A 1 44 ? 23.053 13.494 -9.576 1.00 14.62 ? 43 THR A CB 1 ATOM 327 O OG1 . THR A 1 44 ? 22.976 12.177 -9.018 1.00 18.15 ? 43 THR A OG1 1 ATOM 328 C CG2 . THR A 1 44 ? 21.982 14.371 -8.949 1.00 15.40 ? 43 THR A CG2 1 ATOM 329 N N . PRO A 1 45 ? 25.017 12.563 -11.905 1.00 22.93 ? 44 PRO A N 1 ATOM 330 C CA . PRO A 1 45 ? 25.908 11.495 -12.373 1.00 13.68 ? 44 PRO A CA 1 ATOM 331 C C . PRO A 1 45 ? 26.028 10.372 -11.350 1.00 15.63 ? 44 PRO A C 1 ATOM 332 O O . PRO A 1 45 ? 26.302 10.640 -10.181 1.00 33.49 ? 44 PRO A O 1 ATOM 333 C CB . PRO A 1 45 ? 27.250 12.208 -12.558 1.00 10.18 ? 44 PRO A CB 1 ATOM 334 C CG . PRO A 1 45 ? 26.896 13.642 -12.740 1.00 19.00 ? 44 PRO A CG 1 ATOM 335 C CD . PRO A 1 45 ? 25.693 13.872 -11.883 1.00 13.34 ? 44 PRO A CD 1 ATOM 336 N N . ARG A 1 46 ? 25.818 9.135 -11.784 1.00 14.98 ? 45 ARG A N 1 ATOM 337 C CA . ARG A 1 46 ? 25.896 7.991 -10.886 1.00 16.74 ? 45 ARG A CA 1 ATOM 338 C C . ARG A 1 46 ? 26.991 7.026 -11.327 1.00 15.07 ? 45 ARG A C 1 ATOM 339 O O . ARG A 1 46 ? 27.117 6.720 -12.513 1.00 16.23 ? 45 ARG A O 1 ATOM 340 C CB . ARG A 1 46 ? 24.543 7.281 -10.816 1.00 21.80 ? 45 ARG A CB 1 ATOM 341 C CG . ARG A 1 46 ? 23.426 8.188 -10.323 1.00 46.25 ? 45 ARG A CG 1 ATOM 342 C CD . ARG A 1 46 ? 22.050 7.583 -10.540 1.00 63.14 ? 45 ARG A CD 1 ATOM 343 N NE . ARG A 1 46 ? 21.008 8.604 -10.477 1.00 46.26 ? 45 ARG A NE 1 ATOM 344 C CZ . ARG A 1 46 ? 20.390 8.976 -9.361 1.00 52.38 ? 45 ARG A CZ 1 ATOM 345 N NH1 . ARG A 1 46 ? 20.703 8.406 -8.206 1.00 63.74 ? 45 ARG A NH1 1 ATOM 346 N NH2 . ARG A 1 46 ? 19.456 9.918 -9.400 1.00 61.98 ? 45 ARG A NH2 1 ATOM 347 N N . LEU A 1 47 ? 27.784 6.561 -10.365 1.00 21.80 ? 46 LEU A N 1 ATOM 348 C CA . LEU A 1 47 ? 28.928 5.702 -10.651 1.00 12.93 ? 46 LEU A CA 1 ATOM 349 C C . LEU A 1 47 ? 28.513 4.424 -11.369 1.00 12.26 ? 46 LEU A C 1 ATOM 350 O O . LEU A 1 47 ? 27.796 3.589 -10.817 1.00 14.30 ? 46 LEU A O 1 ATOM 351 C CB . LEU A 1 47 ? 29.671 5.356 -9.361 1.00 20.08 ? 46 LEU A CB 1 ATOM 352 C CG . LEU A 1 47 ? 30.964 4.557 -9.534 1.00 14.54 ? 46 LEU A CG 1 ATOM 353 C CD1 . LEU A 1 47 ? 31.961 5.333 -10.378 1.00 12.73 ? 46 LEU A CD1 1 ATOM 354 C CD2 . LEU A 1 47 ? 31.564 4.200 -8.183 1.00 23.66 ? 46 LEU A CD2 1 ATOM 355 N N . LEU A 1 48 ? 28.971 4.286 -12.607 1.00 16.03 ? 47 LEU A N 1 ATOM 356 C CA . LEU A 1 48 ? 28.649 3.129 -13.426 1.00 16.19 ? 47 LEU A CA 1 ATOM 357 C C . LEU A 1 48 ? 29.749 2.079 -13.323 1.00 21.01 ? 47 LEU A C 1 ATOM 358 O O . LEU A 1 48 ? 29.479 0.891 -13.145 1.00 29.13 ? 47 LEU A O 1 ATOM 359 C CB . LEU A 1 48 ? 28.454 3.554 -14.881 1.00 19.11 ? 47 LEU A CB 1 ATOM 360 C CG . LEU A 1 48 ? 27.846 2.542 -15.849 1.00 15.33 ? 47 LEU A CG 1 ATOM 361 C CD1 . LEU A 1 48 ? 26.412 2.235 -15.458 1.00 23.54 ? 47 LEU A CD1 1 ATOM 362 C CD2 . LEU A 1 48 ? 27.913 3.074 -17.270 1.00 16.93 ? 47 LEU A CD2 1 ATOM 363 N N . MET A 1 49 ? 30.991 2.487 -13.485 1.00 29.11 ? 48 MET A N 1 ATOM 364 C CA . MET A 1 49 ? 32.119 1.581 -13.461 1.00 17.39 ? 48 MET A CA 1 ATOM 365 C C . MET A 1 49 ? 33.273 2.233 -12.705 1.00 16.98 ? 48 MET A C 1 ATOM 366 O O . MET A 1 49 ? 33.424 3.424 -12.740 1.00 16.90 ? 48 MET A O 1 ATOM 367 C CB . MET A 1 49 ? 32.509 1.261 -14.906 1.00 20.70 ? 48 MET A CB 1 ATOM 368 C CG . MET A 1 49 ? 33.407 0.061 -15.103 1.00 27.59 ? 48 MET A CG 1 ATOM 369 S SD . MET A 1 49 ? 32.560 -1.489 -15.366 1.00 41.68 ? 48 MET A SD 1 ATOM 370 C CE . MET A 1 49 ? 31.119 -0.998 -16.268 1.00 19.19 ? 48 MET A CE 1 ATOM 371 N N . TYR A 1 50 ? 34.076 1.447 -12.004 1.00 13.98 ? 49 TYR A N 1 ATOM 372 C CA . TYR A 1 50 ? 35.244 1.960 -11.296 1.00 13.63 ? 49 TYR A CA 1 ATOM 373 C C . TYR A 1 50 ? 36.361 0.945 -11.302 1.00 14.06 ? 49 TYR A C 1 ATOM 374 O O . TYR A 1 50 ? 36.132 -0.211 -11.524 1.00 14.80 ? 49 TYR A O 1 ATOM 375 C CB . TYR A 1 50 ? 34.918 2.374 -9.871 1.00 12.74 ? 49 TYR A CB 1 ATOM 376 C CG . TYR A 1 50 ? 34.648 1.230 -8.945 1.00 15.18 ? 49 TYR A CG 1 ATOM 377 C CD1 . TYR A 1 50 ? 33.393 0.714 -8.817 1.00 15.93 ? 49 TYR A CD1 1 ATOM 378 C CD2 . TYR A 1 50 ? 35.649 0.668 -8.203 1.00 21.97 ? 49 TYR A CD2 1 ATOM 379 C CE1 . TYR A 1 50 ? 33.146 -0.338 -7.984 1.00 29.71 ? 49 TYR A CE1 1 ATOM 380 C CE2 . TYR A 1 50 ? 35.406 -0.384 -7.364 1.00 16.41 ? 49 TYR A CE2 1 ATOM 381 C CZ . TYR A 1 50 ? 34.150 -0.881 -7.260 1.00 18.69 ? 49 TYR A CZ 1 ATOM 382 O OH . TYR A 1 50 ? 33.896 -1.926 -6.417 1.00 16.56 ? 49 TYR A OH 1 ATOM 383 N N . GLY A 1 51 ? 37.580 1.402 -11.082 1.00 15.88 ? 50 GLY A N 1 ATOM 384 C CA . GLY A 1 51 ? 38.728 0.537 -11.102 1.00 11.99 ? 50 GLY A CA 1 ATOM 385 C C . GLY A 1 51 ? 38.930 -0.046 -12.465 1.00 16.11 ? 50 GLY A C 1 ATOM 386 O O . GLY A 1 51 ? 39.462 -1.129 -12.611 1.00 24.41 ? 50 GLY A O 1 ATOM 387 N N . VAL A 1 52 ? 38.503 0.707 -13.465 1.00 17.78 ? 51 VAL A N 1 ATOM 388 C CA . VAL A 1 52 ? 38.570 0.315 -14.867 1.00 15.57 ? 51 VAL A CA 1 ATOM 389 C C . VAL A 1 52 ? 37.558 -0.758 -15.210 1.00 18.53 ? 51 VAL A C 1 ATOM 390 O O . VAL A 1 52 ? 36.723 -0.552 -16.050 1.00 34.11 ? 51 VAL A O 1 ATOM 391 C CB . VAL A 1 52 ? 39.991 -0.114 -15.267 1.00 17.05 ? 51 VAL A CB 1 ATOM 392 C CG1 . VAL A 1 52 ? 40.025 -0.758 -16.636 1.00 24.35 ? 51 VAL A CG1 1 ATOM 393 C CG2 . VAL A 1 52 ? 40.921 1.074 -15.263 1.00 17.59 ? 51 VAL A CG2 1 ATOM 394 N N . SER A 1 53 ? 37.633 -1.909 -14.564 1.00 19.00 ? 52 SER A N 1 ATOM 395 C CA . SER A 1 53 ? 36.742 -3.008 -14.917 1.00 23.92 ? 52 SER A CA 1 ATOM 396 C C . SER A 1 53 ? 35.695 -3.369 -13.895 1.00 17.40 ? 52 SER A C 1 ATOM 397 O O . SER A 1 53 ? 34.812 -4.155 -14.161 1.00 14.90 ? 52 SER A O 1 ATOM 398 C CB . SER A 1 53 ? 37.540 -4.248 -15.347 1.00 20.01 ? 52 SER A CB 1 ATOM 399 O OG . SER A 1 53 ? 38.475 -4.690 -14.384 1.00 27.72 ? 52 SER A OG 1 ATOM 400 N N . LEU A 1 54 ? 35.792 -2.783 -12.721 1.00 18.98 ? 53 LEU A N 1 ATOM 401 C CA . LEU A 1 54 ? 34.907 -3.148 -11.643 1.00 23.57 ? 53 LEU A CA 1 ATOM 402 C C . LEU A 1 54 ? 33.545 -2.517 -11.804 1.00 22.29 ? 53 LEU A C 1 ATOM 403 O O . LEU A 1 54 ? 33.411 -1.334 -12.023 1.00 20.58 ? 53 LEU A O 1 ATOM 404 C CB . LEU A 1 54 ? 35.528 -2.778 -10.308 1.00 18.72 ? 53 LEU A CB 1 ATOM 405 C CG . LEU A 1 54 ? 36.800 -3.490 -9.878 1.00 19.04 ? 53 LEU A CG 1 ATOM 406 C CD1 . LEU A 1 54 ? 37.402 -2.942 -8.608 1.00 27.40 ? 53 LEU A CD1 1 ATOM 407 C CD2 . LEU A 1 54 ? 36.586 -4.972 -9.758 1.00 42.44 ? 53 LEU A CD2 1 ATOM 408 N N . ARG A 1 55 ? 32.523 -3.332 -11.677 1.00 24.47 ? 54 ARG A N 1 ATOM 409 C CA . ARG A 1 55 ? 31.201 -2.888 -11.960 1.00 20.47 ? 54 ARG A CA 1 ATOM 410 C C . ARG A 1 55 ? 30.526 -2.600 -10.662 1.00 28.70 ? 54 ARG A C 1 ATOM 411 O O . ARG A 1 55 ? 30.398 -3.437 -9.798 1.00 40.05 ? 54 ARG A O 1 ATOM 412 C CB . ARG A 1 55 ? 30.457 -3.961 -12.708 1.00 21.31 ? 54 ARG A CB 1 ATOM 413 C CG . ARG A 1 55 ? 29.308 -3.460 -13.533 1.00 24.09 ? 54 ARG A CG 1 ATOM 414 C CD . ARG A 1 55 ? 28.725 -4.588 -14.351 1.00 33.86 ? 54 ARG A CD 1 ATOM 415 N NE . ARG A 1 55 ? 29.670 -5.058 -15.347 1.00 42.73 ? 54 ARG A NE 1 ATOM 416 C CZ . ARG A 1 55 ? 30.215 -6.259 -15.352 1.00 36.08 ? 54 ARG A CZ 1 ATOM 417 N NH1 . ARG A 1 55 ? 29.908 -7.127 -14.410 1.00 31.92 ? 54 ARG A NH1 1 ATOM 418 N NH2 . ARG A 1 55 ? 31.073 -6.580 -16.295 1.00 23.36 ? 54 ARG A NH2 1 ATOM 419 N N . ASN A 1 56 ? 30.097 -1.371 -10.541 1.00 30.96 ? 55 ASN A N 1 ATOM 420 C CA . ASN A 1 56 ? 29.373 -0.898 -9.366 1.00 20.53 ? 55 ASN A CA 1 ATOM 421 C C . ASN A 1 56 ? 28.118 -1.726 -9.114 1.00 20.97 ? 55 ASN A C 1 ATOM 422 O O . ASN A 1 56 ? 27.570 -2.328 -10.037 1.00 38.57 ? 55 ASN A O 1 ATOM 423 C CB . ASN A 1 56 ? 29.005 0.579 -9.526 1.00 20.62 ? 55 ASN A CB 1 ATOM 424 C CG . ASN A 1 56 ? 28.579 1.222 -8.218 1.00 21.68 ? 55 ASN A CG 1 ATOM 425 O OD1 . ASN A 1 56 ? 28.977 0.785 -7.138 1.00 18.37 ? 55 ASN A OD1 1 ATOM 426 N ND2 . ASN A 1 56 ? 27.768 2.270 -8.311 1.00 18.33 ? 55 ASN A ND2 1 ATOM 427 N N . THR A 1 57 ? 27.669 -1.757 -7.864 1.00 22.45 ? 56 THR A N 1 ATOM 428 C CA . THR A 1 57 ? 26.498 -2.542 -7.491 1.00 21.80 ? 56 THR A CA 1 ATOM 429 C C . THR A 1 57 ? 25.228 -2.007 -8.149 1.00 23.66 ? 56 THR A C 1 ATOM 430 O O . THR A 1 57 ? 24.976 -0.802 -8.150 1.00 33.33 ? 56 THR A O 1 ATOM 431 C CB . THR A 1 57 ? 26.309 -2.572 -5.960 1.00 23.82 ? 56 THR A CB 1 ATOM 432 O OG1 . THR A 1 57 ? 25.003 -3.069 -5.644 1.00 29.15 ? 56 THR A OG1 1 ATOM 433 C CG2 . THR A 1 57 ? 26.471 -1.179 -5.370 1.00 25.07 ? 56 THR A CG2 1 ATOM 434 N N . GLY A 1 58 ? 24.438 -2.913 -8.715 1.00 27.62 ? 57 GLY A N 1 ATOM 435 C CA . GLY A 1 58 ? 23.195 -2.543 -9.367 1.00 24.02 ? 57 GLY A CA 1 ATOM 436 C C . GLY A 1 58 ? 23.358 -2.290 -10.853 1.00 32.28 ? 57 GLY A C 1 ATOM 437 O O . GLY A 1 58 ? 22.379 -2.060 -11.561 1.00 54.97 ? 57 GLY A O 1 ATOM 438 N N . VAL A 1 59 ? 24.599 -2.333 -11.327 1.00 25.40 ? 58 VAL A N 1 ATOM 439 C CA . VAL A 1 59 ? 24.891 -2.089 -12.735 1.00 25.76 ? 58 VAL A CA 1 ATOM 440 C C . VAL A 1 59 ? 24.851 -3.387 -13.538 1.00 26.38 ? 58 VAL A C 1 ATOM 441 O O . VAL A 1 59 ? 25.521 -4.357 -13.185 1.00 30.11 ? 58 VAL A O 1 ATOM 442 C CB . VAL A 1 59 ? 26.268 -1.419 -12.915 1.00 23.69 ? 58 VAL A CB 1 ATOM 443 C CG1 . VAL A 1 59 ? 26.604 -1.273 -14.388 1.00 32.36 ? 58 VAL A CG1 1 ATOM 444 C CG2 . VAL A 1 59 ? 26.292 -0.066 -12.223 1.00 28.13 ? 58 VAL A CG2 1 ATOM 445 N N . PRO A 1 60 ? 24.163 -3.402 -14.662 1.00 25.89 ? 59 PRO A N 1 ATOM 446 C CA . PRO A 1 60 ? 23.990 -4.637 -15.412 1.00 27.93 ? 59 PRO A CA 1 ATOM 447 C C . PRO A 1 60 ? 25.302 -5.161 -15.935 1.00 39.91 ? 59 PRO A C 1 ATOM 448 O O . PRO A 1 60 ? 26.221 -4.385 -16.082 1.00 38.20 ? 59 PRO A O 1 ATOM 449 C CB . PRO A 1 60 ? 23.120 -4.200 -16.568 1.00 36.00 ? 59 PRO A CB 1 ATOM 450 C CG . PRO A 1 60 ? 22.299 -3.109 -16.004 1.00 37.49 ? 59 PRO A CG 1 ATOM 451 C CD . PRO A 1 60 ? 23.192 -2.379 -15.069 1.00 35.92 ? 59 PRO A CD 1 ATOM 452 N N . ASP A 1 61 ? 25.404 -6.469 -16.144 1.00 30.56 ? 60 ASP A N 1 ATOM 453 C CA . ASP A 1 61 ? 26.479 -6.997 -16.896 1.00 30.24 ? 60 ASP A CA 1 ATOM 454 C C . ASP A 1 61 ? 27.192 -6.653 -18.194 1.00 32.06 ? 60 ASP A C 1 ATOM 455 O O . ASP A 1 61 ? 28.207 -7.061 -18.731 1.00 28.14 ? 60 ASP A O 1 ATOM 456 C CB . ASP A 1 61 ? 26.306 -8.517 -16.857 1.00 34.67 ? 60 ASP A CB 1 ATOM 457 C CG . ASP A 1 61 ? 25.577 -8.988 -15.614 1.00 62.56 ? 60 ASP A CG 1 ATOM 458 O OD1 . ASP A 1 61 ? 26.239 -9.199 -14.576 1.00 71.12 ? 60 ASP A OD1 1 ATOM 459 O OD2 . ASP A 1 61 ? 24.339 -9.149 -15.677 1.00 49.59 ? 60 ASP A OD2 1 ATOM 460 N N . ARG A 1 62 ? 26.221 -6.051 -18.861 1.00 24.75 ? 61 ARG A N 1 ATOM 461 C CA . ARG A 1 62 ? 26.388 -5.595 -20.227 1.00 19.32 ? 61 ARG A CA 1 ATOM 462 C C . ARG A 1 62 ? 27.390 -4.473 -20.397 1.00 25.20 ? 61 ARG A C 1 ATOM 463 O O . ARG A 1 62 ? 28.054 -4.391 -21.410 1.00 50.41 ? 61 ARG A O 1 ATOM 464 C CB . ARG A 1 62 ? 25.067 -5.351 -20.946 1.00 21.53 ? 61 ARG A CB 1 ATOM 465 C CG . ARG A 1 62 ? 24.196 -4.234 -20.444 1.00 29.02 ? 61 ARG A CG 1 ATOM 466 C CD . ARG A 1 62 ? 22.903 -4.228 -21.226 1.00 19.63 ? 61 ARG A CD 1 ATOM 467 N NE . ARG A 1 62 ? 22.019 -3.148 -20.835 1.00 19.05 ? 61 ARG A NE 1 ATOM 468 C CZ . ARG A 1 62 ? 21.209 -3.207 -19.802 1.00 23.70 ? 61 ARG A CZ 1 ATOM 469 N NH1 . ARG A 1 62 ? 21.181 -4.289 -19.058 1.00 25.10 ? 61 ARG A NH1 1 ATOM 470 N NH2 . ARG A 1 62 ? 20.431 -2.195 -19.522 1.00 36.43 ? 61 ARG A NH2 1 ATOM 471 N N . PHE A 1 63 ? 27.465 -3.576 -19.432 1.00 20.89 ? 62 PHE A N 1 ATOM 472 C CA . PHE A 1 63 ? 28.529 -2.600 -19.395 1.00 18.10 ? 62 PHE A CA 1 ATOM 473 C C . PHE A 1 63 ? 29.859 -3.234 -19.048 1.00 17.87 ? 62 PHE A C 1 ATOM 474 O O . PHE A 1 63 ? 29.927 -4.057 -18.186 1.00 21.25 ? 62 PHE A O 1 ATOM 475 C CB . PHE A 1 63 ? 28.208 -1.555 -18.365 1.00 17.38 ? 62 PHE A CB 1 ATOM 476 C CG . PHE A 1 63 ? 26.964 -0.800 -18.639 1.00 11.72 ? 62 PHE A CG 1 ATOM 477 C CD1 . PHE A 1 63 ? 25.759 -1.315 -18.311 1.00 15.21 ? 62 PHE A CD1 1 ATOM 478 C CD2 . PHE A 1 63 ? 27.018 0.435 -19.196 1.00 13.66 ? 62 PHE A CD2 1 ATOM 479 C CE1 . PHE A 1 63 ? 24.617 -0.611 -18.542 1.00 17.52 ? 62 PHE A CE1 1 ATOM 480 C CE2 . PHE A 1 63 ? 25.880 1.147 -19.434 1.00 12.68 ? 62 PHE A CE2 1 ATOM 481 C CZ . PHE A 1 63 ? 24.673 0.620 -19.114 1.00 12.62 ? 62 PHE A CZ 1 ATOM 482 N N . SER A 1 64 ? 30.920 -2.813 -19.709 1.00 16.00 ? 63 SER A N 1 ATOM 483 C CA . SER A 1 64 ? 32.259 -3.359 -19.517 1.00 13.86 ? 63 SER A CA 1 ATOM 484 C C . SER A 1 64 ? 33.328 -2.280 -19.640 1.00 16.95 ? 63 SER A C 1 ATOM 485 O O . SER A 1 64 ? 33.243 -1.406 -20.502 1.00 21.41 ? 63 SER A O 1 ATOM 486 C CB . SER A 1 64 ? 32.532 -4.474 -20.528 1.00 16.13 ? 63 SER A CB 1 ATOM 487 O OG . SER A 1 64 ? 31.552 -5.494 -20.439 1.00 32.91 ? 63 SER A OG 1 ATOM 488 N N . GLY A 1 65 ? 34.333 -2.348 -18.773 1.00 20.68 ? 64 GLY A N 1 ATOM 489 C CA . GLY A 1 65 ? 35.440 -1.409 -18.811 1.00 19.63 ? 64 GLY A CA 1 ATOM 490 C C . GLY A 1 65 ? 36.726 -2.076 -19.260 1.00 19.55 ? 64 GLY A C 1 ATOM 491 O O . GLY A 1 65 ? 36.982 -3.232 -18.924 1.00 18.55 ? 64 GLY A O 1 ATOM 492 N N . SER A 1 66 ? 37.537 -1.349 -20.022 1.00 19.80 ? 65 SER A N 1 ATOM 493 C CA . SER A 1 66 ? 38.769 -1.909 -20.568 1.00 20.96 ? 65 SER A CA 1 ATOM 494 C C . SER A 1 66 ? 39.864 -0.856 -20.696 1.00 21.82 ? 65 SER A C 1 ATOM 495 O O . SER A 1 66 ? 39.664 0.308 -20.347 1.00 26.54 ? 65 SER A O 1 ATOM 496 C CB . SER A 1 66 ? 38.502 -2.545 -21.934 1.00 35.91 ? 65 SER A CB 1 ATOM 497 O OG . SER A 1 66 ? 37.439 -3.479 -21.866 1.00 36.25 ? 65 SER A OG 1 ATOM 498 N N . GLY A 1 67 ? 41.021 -1.275 -21.199 1.00 33.77 ? 66 GLY A N 1 ATOM 499 C CA . GLY A 1 67 ? 42.117 -0.361 -21.470 1.00 54.12 ? 66 GLY A CA 1 ATOM 500 C C . GLY A 1 67 ? 43.020 -0.089 -20.283 1.00 27.43 ? 66 GLY A C 1 ATOM 501 O O . GLY A 1 67 ? 42.694 -0.432 -19.147 1.00 32.31 ? 66 GLY A O 1 ATOM 502 N N . SER A 1 68 ? 44.164 0.533 -20.554 1.00 23.73 ? 67 SER A N 1 ATOM 503 C CA . SER A 1 68 ? 45.122 0.892 -19.513 1.00 25.20 ? 67 SER A CA 1 ATOM 504 C C . SER A 1 68 ? 46.056 1.996 -19.991 1.00 28.34 ? 67 SER A C 1 ATOM 505 O O . SER A 1 68 ? 46.205 2.216 -21.193 1.00 46.04 ? 67 SER A O 1 ATOM 506 C CB . SER A 1 68 ? 45.935 -0.330 -19.080 1.00 29.20 ? 67 SER A CB 1 ATOM 507 O OG . SER A 1 68 ? 45.122 -1.274 -18.407 1.00 61.20 ? 67 SER A OG 1 ATOM 508 N N . GLY A 1 69 ? 46.680 2.688 -19.044 1.00 20.99 ? 68 GLY A N 1 ATOM 509 C CA . GLY A 1 69 ? 47.642 3.727 -19.363 1.00 23.71 ? 68 GLY A CA 1 ATOM 510 C C . GLY A 1 69 ? 47.033 4.958 -20.005 1.00 26.70 ? 68 GLY A C 1 ATOM 511 O O . GLY A 1 69 ? 46.627 5.892 -19.315 1.00 37.53 ? 68 GLY A O 1 ATOM 512 N N . THR A 1 70 ? 46.970 4.957 -21.333 1.00 35.18 ? 69 THR A N 1 ATOM 513 C CA . THR A 1 70 ? 46.491 6.114 -22.080 1.00 32.00 ? 69 THR A CA 1 ATOM 514 C C . THR A 1 70 ? 45.050 5.944 -22.553 1.00 30.39 ? 69 THR A C 1 ATOM 515 O O . THR A 1 70 ? 44.211 6.817 -22.338 1.00 40.48 ? 69 THR A O 1 ATOM 516 C CB . THR A 1 70 ? 47.385 6.394 -23.304 1.00 37.27 ? 69 THR A CB 1 ATOM 517 O OG1 . THR A 1 70 ? 48.715 6.699 -22.868 1.00 59.03 ? 69 THR A OG1 1 ATOM 518 C CG2 . THR A 1 70 ? 46.841 7.562 -24.113 1.00 48.44 ? 69 THR A CG2 1 ATOM 519 N N . ASP A 1 71 ? 44.769 4.815 -23.196 1.00 33.89 ? 70 ASP A N 1 ATOM 520 C CA . ASP A 1 71 ? 43.464 4.588 -23.812 1.00 44.79 ? 70 ASP A CA 1 ATOM 521 C C . ASP A 1 71 ? 42.585 3.649 -22.988 1.00 27.06 ? 70 ASP A C 1 ATOM 522 O O . ASP A 1 71 ? 43.008 2.555 -22.616 1.00 23.54 ? 70 ASP A O 1 ATOM 523 C CB . ASP A 1 71 ? 43.644 4.029 -25.227 1.00 33.96 ? 70 ASP A CB 1 ATOM 524 C CG . ASP A 1 71 ? 42.327 3.834 -25.951 1.00 55.87 ? 70 ASP A CG 1 ATOM 525 O OD1 . ASP A 1 71 ? 41.795 4.824 -26.496 1.00 54.74 ? 70 ASP A OD1 1 ATOM 526 O OD2 . ASP A 1 71 ? 41.827 2.689 -25.984 1.00 66.69 ? 70 ASP A OD2 1 ATOM 527 N N . PHE A 1 72 ? 41.361 4.087 -22.708 1.00 22.47 ? 71 PHE A N 1 ATOM 528 C CA . PHE A 1 72 ? 40.393 3.272 -21.979 1.00 21.04 ? 71 PHE A CA 1 ATOM 529 C C . PHE A 1 72 ? 39.127 3.082 -22.808 1.00 19.99 ? 71 PHE A C 1 ATOM 530 O O . PHE A 1 72 ? 38.883 3.827 -23.756 1.00 28.08 ? 71 PHE A O 1 ATOM 531 C CB . PHE A 1 72 ? 40.060 3.909 -20.630 1.00 17.14 ? 71 PHE A CB 1 ATOM 532 C CG . PHE A 1 72 ? 41.240 4.027 -19.711 1.00 14.69 ? 71 PHE A CG 1 ATOM 533 C CD1 . PHE A 1 72 ? 41.608 2.970 -18.896 1.00 15.27 ? 71 PHE A CD1 1 ATOM 534 C CD2 . PHE A 1 72 ? 41.985 5.193 -19.663 1.00 15.66 ? 71 PHE A CD2 1 ATOM 535 C CE1 . PHE A 1 72 ? 42.695 3.076 -18.050 1.00 20.09 ? 71 PHE A CE1 1 ATOM 536 C CE2 . PHE A 1 72 ? 43.073 5.302 -18.818 1.00 19.47 ? 71 PHE A CE2 1 ATOM 537 C CZ . PHE A 1 72 ? 43.428 4.243 -18.012 1.00 23.36 ? 71 PHE A CZ 1 ATOM 538 N N . THR A 1 73 ? 38.322 2.085 -22.450 1.00 17.42 ? 72 THR A N 1 ATOM 539 C CA . THR A 1 73 ? 37.155 1.735 -23.253 1.00 17.41 ? 72 THR A CA 1 ATOM 540 C C . THR A 1 73 ? 35.955 1.307 -22.412 1.00 20.31 ? 72 THR A C 1 ATOM 541 O O . THR A 1 73 ? 36.065 0.431 -21.553 1.00 35.42 ? 72 THR A O 1 ATOM 542 C CB . THR A 1 73 ? 37.487 0.598 -24.243 1.00 20.42 ? 72 THR A CB 1 ATOM 543 O OG1 . THR A 1 73 ? 38.674 0.927 -24.975 1.00 27.09 ? 72 THR A OG1 1 ATOM 544 C CG2 . THR A 1 73 ? 36.338 0.380 -25.217 1.00 28.21 ? 72 THR A CG2 1 ATOM 545 N N . LEU A 1 74 ? 34.809 1.933 -22.667 1.00 24.21 ? 73 LEU A N 1 ATOM 546 C CA . LEU A 1 74 ? 33.545 1.509 -22.073 1.00 22.07 ? 73 LEU A CA 1 ATOM 547 C C . LEU A 1 74 ? 32.669 0.872 -23.144 1.00 26.08 ? 73 LEU A C 1 ATOM 548 O O . LEU A 1 74 ? 32.454 1.456 -24.206 1.00 25.13 ? 73 LEU A O 1 ATOM 549 C CB . LEU A 1 74 ? 32.815 2.686 -21.424 1.00 18.47 ? 73 LEU A CB 1 ATOM 550 C CG . LEU A 1 74 ? 31.405 2.375 -20.911 1.00 14.77 ? 73 LEU A CG 1 ATOM 551 C CD1 . LEU A 1 74 ? 31.443 1.321 -19.815 1.00 12.14 ? 73 LEU A CD1 1 ATOM 552 C CD2 . LEU A 1 74 ? 30.707 3.635 -20.424 1.00 17.20 ? 73 LEU A CD2 1 ATOM 553 N N . THR A 1 75 ? 32.162 -0.324 -22.864 1.00 23.14 ? 74 THR A N 1 ATOM 554 C CA . THR A 1 75 ? 31.398 -1.067 -23.857 1.00 21.00 ? 74 THR A CA 1 ATOM 555 C C . THR A 1 75 ? 30.023 -1.490 -23.348 1.00 25.32 ? 74 THR A C 1 ATOM 556 O O . THR A 1 75 ? 29.903 -2.116 -22.295 1.00 24.98 ? 74 THR A O 1 ATOM 557 C CB . THR A 1 75 ? 32.160 -2.325 -24.316 1.00 24.61 ? 74 THR A CB 1 ATOM 558 O OG1 . THR A 1 75 ? 33.451 -1.951 -24.813 1.00 26.58 ? 74 THR A OG1 1 ATOM 559 C CG2 . THR A 1 75 ? 31.389 -3.043 -25.410 1.00 35.00 ? 74 THR A CG2 1 ATOM 560 N N . ILE A 1 76 ? 28.989 -1.140 -24.105 1.00 25.58 ? 75 ILE A N 1 ATOM 561 C CA . ILE A 1 76 ? 27.637 -1.598 -23.820 1.00 20.46 ? 75 ILE A CA 1 ATOM 562 C C . ILE A 1 76 ? 27.237 -2.630 -24.869 1.00 20.95 ? 75 ILE A C 1 ATOM 563 O O . ILE A 1 76 ? 27.021 -2.286 -26.031 1.00 27.75 ? 75 ILE A O 1 ATOM 564 C CB . ILE A 1 76 ? 26.627 -0.437 -23.817 1.00 19.10 ? 75 ILE A CB 1 ATOM 565 C CG1 . ILE A 1 76 ? 27.198 0.766 -23.063 1.00 22.17 ? 75 ILE A CG1 1 ATOM 566 C CG2 . ILE A 1 76 ? 25.305 -0.884 -23.211 1.00 25.76 ? 75 ILE A CG2 1 ATOM 567 C CD1 . ILE A 1 76 ? 26.286 1.973 -23.055 1.00 13.90 ? 75 ILE A CD1 1 ATOM 568 N N . SER A 1 77 ? 27.145 -3.891 -24.456 1.00 22.70 ? 76 SER A N 1 ATOM 569 C CA . SER A 1 77 ? 26.944 -4.998 -25.388 1.00 20.46 ? 76 SER A CA 1 ATOM 570 C C . SER A 1 77 ? 25.610 -4.925 -26.127 1.00 20.70 ? 76 SER A C 1 ATOM 571 O O . SER A 1 77 ? 25.565 -5.053 -27.350 1.00 34.87 ? 76 SER A O 1 ATOM 572 C CB . SER A 1 77 ? 27.045 -6.335 -24.651 1.00 24.53 ? 76 SER A CB 1 ATOM 573 O OG . SER A 1 77 ? 25.899 -6.564 -23.850 1.00 22.63 ? 76 SER A OG 1 ATOM 574 N N . ARG A 1 78 ? 24.528 -4.729 -25.383 1.00 19.38 ? 77 ARG A N 1 ATOM 575 C CA . ARG A 1 78 ? 23.198 -4.666 -25.980 1.00 17.00 ? 77 ARG A CA 1 ATOM 576 C C . ARG A 1 78 ? 22.438 -3.442 -25.490 1.00 17.62 ? 77 ARG A C 1 ATOM 577 O O . ARG A 1 78 ? 21.869 -3.451 -24.399 1.00 24.94 ? 77 ARG A O 1 ATOM 578 C CB . ARG A 1 78 ? 22.409 -5.939 -25.668 1.00 18.88 ? 77 ARG A CB 1 ATOM 579 C CG . ARG A 1 78 ? 22.962 -7.186 -26.335 1.00 26.05 ? 77 ARG A CG 1 ATOM 580 C CD . ARG A 1 78 ? 22.042 -7.676 -27.440 1.00 29.39 ? 77 ARG A CD 1 ATOM 581 N NE . ARG A 1 78 ? 20.815 -8.260 -26.908 1.00 36.37 ? 77 ARG A NE 1 ATOM 582 C CZ . ARG A 1 78 ? 19.872 -8.826 -27.654 1.00 73.63 ? 77 ARG A CZ 1 ATOM 583 N NH1 . ARG A 1 78 ? 20.013 -8.886 -28.972 1.00 48.81 ? 77 ARG A NH1 1 ATOM 584 N NH2 . ARG A 1 78 ? 18.789 -9.332 -27.082 1.00 87.14 ? 77 ARG A NH2 1 ATOM 585 N N . LEU A 1 79 ? 22.432 -2.393 -26.306 1.00 17.65 ? 78 LEU A N 1 ATOM 586 C CA . LEU A 1 79 ? 21.797 -1.132 -25.942 1.00 15.98 ? 78 LEU A CA 1 ATOM 587 C C . LEU A 1 79 ? 20.299 -1.279 -25.698 1.00 15.84 ? 78 LEU A C 1 ATOM 588 O O . LEU A 1 79 ? 19.619 -2.059 -26.365 1.00 21.17 ? 78 LEU A O 1 ATOM 589 C CB . LEU A 1 79 ? 22.040 -0.081 -27.028 1.00 16.05 ? 78 LEU A CB 1 ATOM 590 C CG . LEU A 1 79 ? 23.434 0.544 -27.072 1.00 20.89 ? 78 LEU A CG 1 ATOM 591 C CD1 . LEU A 1 79 ? 23.546 1.524 -28.227 1.00 20.02 ? 78 LEU A CD1 1 ATOM 592 C CD2 . LEU A 1 79 ? 23.737 1.235 -25.754 1.00 26.52 ? 78 LEU A CD2 1 ATOM 593 N N . GLU A 1 80 ? 19.800 -0.521 -24.727 1.00 16.34 ? 79 GLU A N 1 ATOM 594 C CA . GLU A 1 80 ? 18.379 -0.474 -24.417 1.00 12.86 ? 79 GLU A CA 1 ATOM 595 C C . GLU A 1 80 ? 17.899 0.967 -24.535 1.00 14.39 ? 79 GLU A C 1 ATOM 596 O O . GLU A 1 80 ? 18.704 1.893 -24.434 1.00 20.07 ? 79 GLU A O 1 ATOM 597 C CB . GLU A 1 80 ? 18.114 -1.028 -23.013 1.00 16.98 ? 79 GLU A CB 1 ATOM 598 C CG . GLU A 1 80 ? 18.334 -2.528 -22.882 1.00 18.92 ? 79 GLU A CG 1 ATOM 599 C CD . GLU A 1 80 ? 18.117 -3.029 -21.465 1.00 29.74 ? 79 GLU A CD 1 ATOM 600 O OE1 . GLU A 1 80 ? 17.690 -4.192 -21.304 1.00 49.32 ? 79 GLU A OE1 1 ATOM 601 O OE2 . GLU A 1 80 ? 18.373 -2.262 -20.513 1.00 30.83 ? 79 GLU A OE2 1 ATOM 602 N N . PRO A 1 81 ? 16.589 1.169 -24.758 1.00 12.08 ? 80 PRO A N 1 ATOM 603 C CA . PRO A 1 81 ? 16.054 2.533 -24.865 1.00 14.07 ? 80 PRO A CA 1 ATOM 604 C C . PRO A 1 81 ? 16.261 3.366 -23.600 1.00 25.00 ? 80 PRO A C 1 ATOM 605 O O . PRO A 1 81 ? 16.128 4.589 -23.652 1.00 29.83 ? 80 PRO A O 1 ATOM 606 C CB . PRO A 1 81 ? 14.559 2.305 -25.129 1.00 10.92 ? 80 PRO A CB 1 ATOM 607 C CG . PRO A 1 81 ? 14.294 0.898 -24.703 1.00 10.61 ? 80 PRO A CG 1 ATOM 608 C CD . PRO A 1 81 ? 15.550 0.156 -25.003 1.00 11.12 ? 80 PRO A CD 1 ATOM 609 N N . GLU A 1 82 ? 16.585 2.713 -22.487 1.00 19.16 ? 81 GLU A N 1 ATOM 610 C CA . GLU A 1 82 ? 16.846 3.416 -21.236 1.00 20.14 ? 81 GLU A CA 1 ATOM 611 C C . GLU A 1 82 ? 18.325 3.763 -21.088 1.00 19.83 ? 81 GLU A C 1 ATOM 612 O O . GLU A 1 82 ? 18.702 4.531 -20.203 1.00 20.12 ? 81 GLU A O 1 ATOM 613 C CB . GLU A 1 82 ? 16.393 2.579 -20.039 1.00 22.61 ? 81 GLU A CB 1 ATOM 614 C CG . GLU A 1 82 ? 17.226 1.330 -19.809 1.00 28.37 ? 81 GLU A CG 1 ATOM 615 C CD . GLU A 1 82 ? 17.115 0.812 -18.388 1.00 60.61 ? 81 GLU A CD 1 ATOM 616 O OE1 . GLU A 1 82 ? 16.424 1.459 -17.573 1.00 88.89 ? 81 GLU A OE1 1 ATOM 617 O OE2 . GLU A 1 82 ? 17.720 -0.237 -18.084 1.00 44.75 ? 81 GLU A OE2 1 ATOM 618 N N . ASP A 1 83 ? 19.157 3.198 -21.957 1.00 18.84 ? 82 ASP A N 1 ATOM 619 C CA . ASP A 1 83 ? 20.597 3.436 -21.909 1.00 18.22 ? 82 ASP A CA 1 ATOM 620 C C . ASP A 1 83 ? 20.968 4.788 -22.508 1.00 18.32 ? 82 ASP A C 1 ATOM 621 O O . ASP A 1 83 ? 22.141 5.162 -22.530 1.00 21.59 ? 82 ASP A O 1 ATOM 622 C CB . ASP A 1 83 ? 21.350 2.320 -22.637 1.00 16.18 ? 82 ASP A CB 1 ATOM 623 C CG . ASP A 1 83 ? 21.351 1.016 -21.863 1.00 30.47 ? 82 ASP A CG 1 ATOM 624 O OD1 . ASP A 1 83 ? 20.511 0.863 -20.951 1.00 45.14 ? 82 ASP A OD1 1 ATOM 625 O OD2 . ASP A 1 83 ? 22.189 0.141 -22.167 1.00 28.50 ? 82 ASP A OD2 1 ATOM 626 N N . SER A 1 84 ? 19.967 5.515 -22.993 1.00 17.27 ? 83 SER A N 1 ATOM 627 C CA . SER A 1 84 ? 20.192 6.826 -23.591 1.00 18.07 ? 83 SER A CA 1 ATOM 628 C C . SER A 1 84 ? 20.527 7.869 -22.532 1.00 17.28 ? 83 SER A C 1 ATOM 629 O O . SER A 1 84 ? 19.650 8.319 -21.794 1.00 24.39 ? 83 SER A O 1 ATOM 630 C CB . SER A 1 84 ? 18.966 7.271 -24.388 1.00 25.97 ? 83 SER A CB 1 ATOM 631 O OG . SER A 1 84 ? 17.831 7.393 -23.548 1.00 51.09 ? 83 SER A OG 1 ATOM 632 N N . ALA A 1 85 ? 21.799 8.250 -22.467 1.00 15.78 ? 84 ALA A N 1 ATOM 633 C CA . ALA A 1 85 ? 22.260 9.245 -21.505 1.00 12.86 ? 84 ALA A CA 1 ATOM 634 C C . ALA A 1 85 ? 23.622 9.799 -21.906 1.00 14.16 ? 84 ALA A C 1 ATOM 635 O O . ALA A 1 85 ? 24.114 9.530 -23.001 1.00 11.33 ? 84 ALA A O 1 ATOM 636 C CB . ALA A 1 85 ? 22.327 8.644 -20.110 1.00 19.02 ? 84 ALA A CB 1 ATOM 637 N N . VAL A 1 86 ? 24.226 10.576 -21.013 1.00 11.19 ? 85 VAL A N 1 ATOM 638 C CA . VAL A 1 86 ? 25.576 11.082 -21.230 1.00 11.06 ? 85 VAL A CA 1 ATOM 639 C C . VAL A 1 86 ? 26.552 10.314 -20.348 1.00 10.72 ? 85 VAL A C 1 ATOM 640 O O . VAL A 1 86 ? 26.304 10.127 -19.157 1.00 26.55 ? 85 VAL A O 1 ATOM 641 C CB . VAL A 1 86 ? 25.680 12.588 -20.931 1.00 9.98 ? 85 VAL A CB 1 ATOM 642 C CG1 . VAL A 1 86 ? 27.059 13.106 -21.303 1.00 10.10 ? 85 VAL A CG1 1 ATOM 643 C CG2 . VAL A 1 86 ? 24.607 13.353 -21.686 1.00 12.31 ? 85 VAL A CG2 1 ATOM 644 N N . TYR A 1 87 ? 27.657 9.866 -20.933 1.00 9.83 ? 86 TYR A N 1 ATOM 645 C CA . TYR A 1 87 ? 28.624 9.057 -20.201 1.00 8.58 ? 86 TYR A CA 1 ATOM 646 C C . TYR A 1 87 ? 29.956 9.779 -20.035 1.00 15.53 ? 86 TYR A C 1 ATOM 647 O O . TYR A 1 87 ? 30.600 10.151 -21.016 1.00 27.42 ? 86 TYR A O 1 ATOM 648 C CB . TYR A 1 87 ? 28.836 7.716 -20.906 1.00 8.42 ? 86 TYR A CB 1 ATOM 649 C CG . TYR A 1 87 ? 27.589 6.864 -20.994 1.00 9.28 ? 86 TYR A CG 1 ATOM 650 C CD1 . TYR A 1 87 ? 26.685 7.028 -22.036 1.00 8.43 ? 86 TYR A CD1 1 ATOM 651 C CD2 . TYR A 1 87 ? 27.319 5.892 -20.040 1.00 8.22 ? 86 TYR A CD2 1 ATOM 652 C CE1 . TYR A 1 87 ? 25.545 6.251 -22.121 1.00 9.51 ? 86 TYR A CE1 1 ATOM 653 C CE2 . TYR A 1 87 ? 26.181 5.109 -20.118 1.00 8.18 ? 86 TYR A CE2 1 ATOM 654 C CZ . TYR A 1 87 ? 25.299 5.293 -21.160 1.00 8.69 ? 86 TYR A CZ 1 ATOM 655 O OH . TYR A 1 87 ? 24.166 4.516 -21.242 1.00 12.44 ? 86 TYR A OH 1 ATOM 656 N N . PHE A 1 88 ? 30.363 9.974 -18.785 1.00 10.39 ? 87 PHE A N 1 ATOM 657 C CA . PHE A 1 88 ? 31.630 10.626 -18.484 1.00 8.26 ? 87 PHE A CA 1 ATOM 658 C C . PHE A 1 88 ? 32.650 9.619 -17.973 1.00 9.67 ? 87 PHE A C 1 ATOM 659 O O . PHE A 1 88 ? 32.298 8.678 -17.262 1.00 11.98 ? 87 PHE A O 1 ATOM 660 C CB . PHE A 1 88 ? 31.436 11.733 -17.444 1.00 8.41 ? 87 PHE A CB 1 ATOM 661 C CG . PHE A 1 88 ? 30.513 12.831 -17.885 1.00 7.76 ? 87 PHE A CG 1 ATOM 662 C CD1 . PHE A 1 88 ? 31.003 13.936 -18.556 1.00 13.46 ? 87 PHE A CD1 1 ATOM 663 C CD2 . PHE A 1 88 ? 29.157 12.764 -17.619 1.00 8.30 ? 87 PHE A CD2 1 ATOM 664 C CE1 . PHE A 1 88 ? 30.155 14.951 -18.959 1.00 14.76 ? 87 PHE A CE1 1 ATOM 665 C CE2 . PHE A 1 88 ? 28.308 13.777 -18.021 1.00 10.21 ? 87 PHE A CE2 1 ATOM 666 C CZ . PHE A 1 88 ? 28.807 14.870 -18.690 1.00 6.71 ? 87 PHE A CZ 1 ATOM 667 N N . CYS A 1 89 ? 33.911 9.815 -18.341 1.00 11.28 ? 88 CYS A N 1 ATOM 668 C CA . CYS A 1 89 ? 34.996 9.033 -17.764 1.00 11.20 ? 88 CYS A CA 1 ATOM 669 C C . CYS A 1 89 ? 35.817 9.931 -16.849 1.00 12.97 ? 88 CYS A C 1 ATOM 670 O O . CYS A 1 89 ? 35.950 11.129 -17.102 1.00 21.82 ? 88 CYS A O 1 ATOM 671 C CB . CYS A 1 89 ? 35.876 8.414 -18.853 1.00 15.66 ? 88 CYS A CB 1 ATOM 672 S SG . CYS A 1 89 ? 36.936 9.581 -19.737 1.00 33.03 ? 88 CYS A SG 1 ATOM 673 N N . GLN A 1 90 ? 36.360 9.354 -15.783 1.00 13.93 ? 89 GLN A N 1 ATOM 674 C CA . GLN A 1 90 ? 37.091 10.133 -14.793 1.00 13.80 ? 89 GLN A CA 1 ATOM 675 C C . GLN A 1 90 ? 38.290 9.369 -14.249 1.00 15.14 ? 89 GLN A C 1 ATOM 676 O O . GLN A 1 90 ? 38.198 8.174 -13.969 1.00 26.48 ? 89 GLN A O 1 ATOM 677 C CB . GLN A 1 90 ? 36.164 10.530 -13.643 1.00 15.18 ? 89 GLN A CB 1 ATOM 678 C CG . GLN A 1 90 ? 36.848 11.302 -12.528 1.00 23.60 ? 89 GLN A CG 1 ATOM 679 C CD . GLN A 1 90 ? 36.676 10.645 -11.174 1.00 26.72 ? 89 GLN A CD 1 ATOM 680 O OE1 . GLN A 1 90 ? 35.868 9.730 -11.012 1.00 23.30 ? 89 GLN A OE1 1 ATOM 681 N NE2 . GLN A 1 90 ? 37.441 11.106 -10.192 1.00 35.47 ? 89 GLN A NE2 1 ATOM 682 N N . GLN A 1 91 ? 39.414 10.062 -14.102 1.00 16.53 ? 90 GLN A N 1 ATOM 683 C CA . GLN A 1 91 ? 40.596 9.463 -13.499 1.00 22.82 ? 90 GLN A CA 1 ATOM 684 C C . GLN A 1 91 ? 40.810 10.019 -12.096 1.00 21.78 ? 90 GLN A C 1 ATOM 685 O O . GLN A 1 91 ? 40.575 11.200 -11.844 1.00 27.23 ? 90 GLN A O 1 ATOM 686 C CB . GLN A 1 91 ? 41.835 9.703 -14.370 1.00 26.70 ? 90 GLN A CB 1 ATOM 687 C CG . GLN A 1 91 ? 42.206 11.167 -14.578 1.00 18.96 ? 90 GLN A CG 1 ATOM 688 C CD . GLN A 1 91 ? 43.142 11.697 -13.508 1.00 22.45 ? 90 GLN A CD 1 ATOM 689 O OE1 . GLN A 1 91 ? 43.671 10.938 -12.696 1.00 32.03 ? 90 GLN A OE1 1 ATOM 690 N NE2 . GLN A 1 91 ? 43.350 13.009 -13.502 1.00 33.39 ? 90 GLN A NE2 1 ATOM 691 N N . TYR A 1 92 ? 41.075 9.122 -11.161 1.00 22.39 ? 91 TYR A N 1 ATOM 692 C CA . TYR A 1 92 ? 41.364 9.495 -9.797 1.00 26.93 ? 91 TYR A CA 1 ATOM 693 C C . TYR A 1 92 ? 42.802 9.234 -9.432 1.00 33.78 ? 91 TYR A C 1 ATOM 694 O O . TYR A 1 92 ? 43.175 9.313 -8.274 1.00 27.02 ? 91 TYR A O 1 ATOM 695 C CB . TYR A 1 92 ? 40.428 8.837 -8.789 1.00 22.38 ? 91 TYR A CB 1 ATOM 696 C CG . TYR A 1 92 ? 39.970 7.440 -9.061 1.00 21.54 ? 91 TYR A CG 1 ATOM 697 C CD1 . TYR A 1 92 ? 38.917 7.193 -9.893 1.00 37.39 ? 91 TYR A CD1 1 ATOM 698 C CD2 . TYR A 1 92 ? 40.540 6.377 -8.425 1.00 21.22 ? 91 TYR A CD2 1 ATOM 699 C CE1 . TYR A 1 92 ? 38.474 5.920 -10.110 1.00 17.98 ? 91 TYR A CE1 1 ATOM 700 C CE2 . TYR A 1 92 ? 40.101 5.107 -8.656 1.00 19.90 ? 91 TYR A CE2 1 ATOM 701 C CZ . TYR A 1 92 ? 39.067 4.896 -9.499 1.00 14.97 ? 91 TYR A CZ 1 ATOM 702 O OH . TYR A 1 92 ? 38.633 3.637 -9.722 1.00 19.45 ? 91 TYR A OH 1 ATOM 703 N N . GLY A 1 93 ? 43.594 8.895 -10.437 1.00 50.62 ? 92 GLY A N 1 ATOM 704 C CA . GLY A 1 93 ? 45.001 8.602 -10.262 1.00 46.18 ? 92 GLY A CA 1 ATOM 705 C C . GLY A 1 93 ? 45.779 9.799 -9.781 1.00 45.87 ? 92 GLY A C 1 ATOM 706 O O . GLY A 1 93 ? 46.676 9.688 -8.964 1.00 51.73 ? 92 GLY A O 1 ATOM 707 N N . THR A 1 94 ? 45.432 10.949 -10.334 1.00 38.47 ? 93 THR A N 1 ATOM 708 C CA . THR A 1 94 ? 45.993 12.213 -9.938 1.00 49.28 ? 93 THR A CA 1 ATOM 709 C C . THR A 1 94 ? 44.859 13.052 -9.395 1.00 54.71 ? 93 THR A C 1 ATOM 710 O O . THR A 1 94 ? 43.866 12.518 -8.930 1.00 42.57 ? 93 THR A O 1 ATOM 711 C CB . THR A 1 94 ? 46.655 12.927 -11.108 1.00 32.83 ? 93 THR A CB 1 ATOM 712 O OG1 . THR A 1 94 ? 47.532 12.024 -11.759 1.00 31.13 ? 93 THR A OG1 1 ATOM 713 C CG2 . THR A 1 94 ? 47.459 14.072 -10.616 1.00 38.79 ? 93 THR A CG2 1 ATOM 714 N N . SER A 1 95 ? 45.022 14.367 -9.424 1.00 44.16 ? 94 SER A N 1 ATOM 715 C CA . SER A 1 95 ? 43.973 15.259 -9.011 1.00 25.29 ? 94 SER A CA 1 ATOM 716 C C . SER A 1 95 ? 42.862 15.005 -9.982 1.00 32.37 ? 94 SER A C 1 ATOM 717 O O . SER A 1 95 ? 43.070 15.037 -11.179 1.00 31.96 ? 94 SER A O 1 ATOM 718 C CB . SER A 1 95 ? 44.453 16.685 -9.149 1.00 25.21 ? 94 SER A CB 1 ATOM 719 O OG . SER A 1 95 ? 43.565 17.597 -8.564 1.00 35.37 ? 94 SER A OG 1 ATOM 720 N N . PRO A 1 96 ? 41.606 14.762 -9.405 1.00 35.20 ? 96 PRO A N 1 ATOM 721 C CA . PRO A 1 96 ? 40.603 14.285 -10.369 1.00 21.51 ? 96 PRO A CA 1 ATOM 722 C C . PRO A 1 96 ? 40.188 15.189 -11.533 1.00 22.20 ? 96 PRO A C 1 ATOM 723 O O . PRO A 1 96 ? 40.083 16.398 -11.400 1.00 13.71 ? 96 PRO A O 1 ATOM 724 C CB . PRO A 1 96 ? 39.387 14.001 -9.489 1.00 20.39 ? 96 PRO A CB 1 ATOM 725 C CG . PRO A 1 96 ? 39.944 13.591 -8.206 1.00 19.83 ? 96 PRO A CG 1 ATOM 726 C CD . PRO A 1 96 ? 40.946 14.652 -8.012 1.00 22.52 ? 96 PRO A CD 1 ATOM 727 N N . THR A 1 97 ? 39.952 14.563 -12.684 1.00 16.01 ? 97 THR A N 1 ATOM 728 C CA . THR A 1 97 ? 39.492 15.279 -13.870 1.00 13.37 ? 97 THR A CA 1 ATOM 729 C C . THR A 1 97 ? 38.490 14.426 -14.640 1.00 11.27 ? 97 THR A C 1 ATOM 730 O O . THR A 1 97 ? 38.548 13.198 -14.593 1.00 13.12 ? 97 THR A O 1 ATOM 731 C CB . THR A 1 97 ? 40.655 15.653 -14.809 1.00 12.44 ? 97 THR A CB 1 ATOM 732 O OG1 . THR A 1 97 ? 41.439 14.486 -15.089 1.00 14.18 ? 97 THR A OG1 1 ATOM 733 C CG2 . THR A 1 97 ? 41.542 16.713 -14.176 1.00 12.99 ? 97 THR A CG2 1 ATOM 734 N N . PHE A 1 98 ? 37.574 15.080 -15.346 1.00 10.55 ? 98 PHE A N 1 ATOM 735 C CA . PHE A 1 98 ? 36.587 14.376 -16.158 1.00 10.41 ? 98 PHE A CA 1 ATOM 736 C C . PHE A 1 98 ? 36.854 14.572 -17.646 1.00 10.46 ? 98 PHE A C 1 ATOM 737 O O . PHE A 1 98 ? 37.678 15.401 -18.034 1.00 13.27 ? 98 PHE A O 1 ATOM 738 C CB . PHE A 1 98 ? 35.171 14.851 -15.822 1.00 9.39 ? 98 PHE A CB 1 ATOM 739 C CG . PHE A 1 98 ? 34.706 14.463 -14.447 1.00 8.99 ? 98 PHE A CG 1 ATOM 740 C CD1 . PHE A 1 98 ? 34.960 15.278 -13.359 1.00 10.85 ? 98 PHE A CD1 1 ATOM 741 C CD2 . PHE A 1 98 ? 34.004 13.287 -14.245 1.00 14.85 ? 98 PHE A CD2 1 ATOM 742 C CE1 . PHE A 1 98 ? 34.529 14.925 -12.093 1.00 9.76 ? 98 PHE A CE1 1 ATOM 743 C CE2 . PHE A 1 98 ? 33.570 12.928 -12.981 1.00 9.93 ? 98 PHE A CE2 1 ATOM 744 C CZ . PHE A 1 98 ? 33.833 13.748 -11.906 1.00 10.23 ? 98 PHE A CZ 1 ATOM 745 N N . GLY A 1 99 ? 36.157 13.803 -18.476 1.00 17.73 ? 99 GLY A N 1 ATOM 746 C CA . GLY A 1 99 ? 36.196 14.007 -19.912 1.00 12.88 ? 99 GLY A CA 1 ATOM 747 C C . GLY A 1 99 ? 35.128 15.009 -20.301 1.00 13.57 ? 99 GLY A C 1 ATOM 748 O O . GLY A 1 99 ? 34.339 15.434 -19.455 1.00 21.63 ? 99 GLY A O 1 ATOM 749 N N . GLN A 1 100 ? 35.089 15.392 -21.573 1.00 14.15 ? 100 GLN A N 1 ATOM 750 C CA . GLN A 1 100 ? 34.084 16.344 -22.033 1.00 13.88 ? 100 GLN A CA 1 ATOM 751 C C . GLN A 1 100 ? 32.707 15.689 -22.077 1.00 12.93 ? 100 GLN A C 1 ATOM 752 O O . GLN A 1 100 ? 31.685 16.370 -22.157 1.00 12.60 ? 100 GLN A O 1 ATOM 753 C CB . GLN A 1 100 ? 34.445 16.907 -23.411 1.00 14.86 ? 100 GLN A CB 1 ATOM 754 C CG . GLN A 1 100 ? 34.099 15.995 -24.580 1.00 26.32 ? 100 GLN A CG 1 ATOM 755 C CD . GLN A 1 100 ? 35.120 14.896 -24.793 1.00 26.12 ? 100 GLN A CD 1 ATOM 756 O OE1 . GLN A 1 100 ? 36.148 14.845 -24.118 1.00 32.34 ? 100 GLN A OE1 1 ATOM 757 N NE2 . GLN A 1 100 ? 34.843 14.010 -25.742 1.00 17.45 ? 100 GLN A NE2 1 ATOM 758 N N . GLY A 1 101 ? 32.688 14.361 -22.022 1.00 13.62 ? 101 GLY A N 1 ATOM 759 C CA . GLY A 1 101 ? 31.445 13.615 -22.046 1.00 12.57 ? 101 GLY A CA 1 ATOM 760 C C . GLY A 1 101 ? 31.066 13.156 -23.439 1.00 24.94 ? 101 GLY A C 1 ATOM 761 O O . GLY A 1 101 ? 31.286 13.865 -24.421 1.00 33.73 ? 101 GLY A O 1 ATOM 762 N N . THR A 1 102 ? 30.500 11.958 -23.523 1.00 15.27 ? 102 THR A N 1 ATOM 763 C CA . THR A 1 102 ? 30.018 11.426 -24.792 1.00 15.04 ? 102 THR A CA 1 ATOM 764 C C . THR A 1 102 ? 28.548 11.040 -24.675 1.00 13.38 ? 102 THR A C 1 ATOM 765 O O . THR A 1 102 ? 28.178 10.192 -23.863 1.00 14.53 ? 102 THR A O 1 ATOM 766 C CB . THR A 1 102 ? 30.844 10.208 -25.252 1.00 16.59 ? 102 THR A CB 1 ATOM 767 O OG1 . THR A 1 102 ? 30.474 9.853 -26.590 1.00 24.17 ? 102 THR A OG1 1 ATOM 768 C CG2 . THR A 1 102 ? 30.608 9.020 -24.340 1.00 29.61 ? 102 THR A CG2 1 ATOM 769 N N . LYS A 1 103 ? 27.711 11.675 -25.488 1.00 13.34 ? 103 LYS A N 1 ATOM 770 C CA . LYS A 1 103 ? 26.268 11.488 -25.403 1.00 13.14 ? 103 LYS A CA 1 ATOM 771 C C . LYS A 1 103 ? 25.789 10.377 -26.330 1.00 14.60 ? 103 LYS A C 1 ATOM 772 O O . LYS A 1 103 ? 26.228 10.279 -27.476 1.00 26.58 ? 103 LYS A O 1 ATOM 773 C CB . LYS A 1 103 ? 25.548 12.795 -25.731 1.00 16.46 ? 103 LYS A CB 1 ATOM 774 C CG . LYS A 1 103 ? 24.083 12.813 -25.339 1.00 27.88 ? 103 LYS A CG 1 ATOM 775 C CD . LYS A 1 103 ? 23.519 14.220 -25.414 1.00 29.46 ? 103 LYS A CD 1 ATOM 776 C CE . LYS A 1 103 ? 22.125 14.287 -24.818 1.00 51.96 ? 103 LYS A CE 1 ATOM 777 N NZ . LYS A 1 103 ? 21.612 15.684 -24.778 1.00 43.75 ? 103 LYS A NZ 1 ATOM 778 N N . VAL A 1 104 ? 24.885 9.544 -25.827 1.00 12.66 ? 104 VAL A N 1 ATOM 779 C CA . VAL A 1 104 ? 24.369 8.415 -26.593 1.00 11.20 ? 104 VAL A CA 1 ATOM 780 C C . VAL A 1 104 ? 22.848 8.452 -26.695 1.00 13.60 ? 104 VAL A C 1 ATOM 781 O O . VAL A 1 104 ? 22.153 8.516 -25.681 1.00 31.41 ? 104 VAL A O 1 ATOM 782 C CB . VAL A 1 104 ? 24.797 7.071 -25.965 1.00 9.62 ? 104 VAL A CB 1 ATOM 783 C CG1 . VAL A 1 104 ? 24.068 5.912 -26.628 1.00 9.69 ? 104 VAL A CG1 1 ATOM 784 C CG2 . VAL A 1 104 ? 26.302 6.891 -26.067 1.00 10.68 ? 104 VAL A CG2 1 ATOM 785 N N . GLU A 1 105 ? 22.333 8.414 -27.920 1.00 12.49 ? 105 GLU A N 1 ATOM 786 C CA . GLU A 1 105 ? 20.892 8.334 -28.125 1.00 13.56 ? 105 GLU A CA 1 ATOM 787 C C . GLU A 1 105 ? 20.518 7.003 -28.767 1.00 15.28 ? 105 GLU A C 1 ATOM 788 O O . GLU A 1 105 ? 21.336 6.371 -29.437 1.00 18.27 ? 105 GLU A O 1 ATOM 789 C CB . GLU A 1 105 ? 20.392 9.497 -28.984 1.00 13.55 ? 105 GLU A CB 1 ATOM 790 C CG . GLU A 1 105 ? 20.614 9.327 -30.477 1.00 27.51 ? 105 GLU A CG 1 ATOM 791 C CD . GLU A 1 105 ? 19.682 10.197 -31.300 1.00 20.25 ? 105 GLU A CD 1 ATOM 792 O OE1 . GLU A 1 105 ? 19.831 10.227 -32.540 1.00 17.69 ? 105 GLU A OE1 1 ATOM 793 O OE2 . GLU A 1 105 ? 18.795 10.847 -30.708 1.00 19.22 ? 105 GLU A OE2 1 ATOM 794 N N . ILE A 1 106 ? 19.277 6.580 -28.552 1.00 13.73 ? 106 ILE A N 1 ATOM 795 C CA . ILE A 1 106 ? 18.799 5.309 -29.078 1.00 13.79 ? 106 ILE A CA 1 ATOM 796 C C . ILE A 1 106 ? 17.908 5.524 -30.296 1.00 15.14 ? 106 ILE A C 1 ATOM 797 O O . ILE A 1 106 ? 16.914 6.246 -30.226 1.00 14.55 ? 106 ILE A O 1 ATOM 798 C CB . ILE A 1 106 ? 18.019 4.519 -28.011 1.00 19.99 ? 106 ILE A CB 1 ATOM 799 C CG1 . ILE A 1 106 ? 18.823 4.437 -26.712 1.00 14.91 ? 106 ILE A CG1 1 ATOM 800 C CG2 . ILE A 1 106 ? 17.676 3.130 -28.518 1.00 19.48 ? 106 ILE A CG2 1 ATOM 801 C CD1 . ILE A 1 106 ? 20.154 3.738 -26.860 1.00 12.96 ? 106 ILE A CD1 1 ATOM 802 N N . LYS A 1 107 ? 18.265 4.896 -31.411 1.00 17.13 ? 107 LYS A N 1 ATOM 803 C CA . LYS A 1 107 ? 17.485 5.024 -32.637 1.00 16.80 ? 107 LYS A CA 1 ATOM 804 C C . LYS A 1 107 ? 16.206 4.196 -32.573 1.00 21.25 ? 107 LYS A C 1 ATOM 805 O O . LYS A 1 107 ? 16.123 3.218 -31.830 1.00 13.81 ? 107 LYS A O 1 ATOM 806 C CB . LYS A 1 107 ? 18.319 4.609 -33.851 1.00 19.81 ? 107 LYS A CB 1 ATOM 807 C CG . LYS A 1 107 ? 19.573 5.442 -34.055 1.00 30.55 ? 107 LYS A CG 1 ATOM 808 C CD . LYS A 1 107 ? 19.739 5.851 -35.512 1.00 38.97 ? 107 LYS A CD 1 ATOM 809 C CE . LYS A 1 107 ? 19.936 4.644 -36.414 1.00 25.19 ? 107 LYS A CE 1 ATOM 810 N NZ . LYS A 1 107 ? 21.214 3.940 -36.121 1.00 37.63 ? 107 LYS A NZ 1 ATOM 811 N N . ARG A 1 108 ? 15.210 4.598 -33.357 1.00 22.54 ? 108 ARG A N 1 ATOM 812 C CA . ARG A 1 108 ? 13.947 3.873 -33.435 1.00 14.36 ? 108 ARG A CA 1 ATOM 813 C C . ARG A 1 108 ? 13.224 4.204 -34.734 1.00 14.38 ? 108 ARG A C 1 ATOM 814 O O . ARG A 1 108 ? 13.674 5.056 -35.501 1.00 14.07 ? 108 ARG A O 1 ATOM 815 C CB . ARG A 1 108 ? 13.053 4.204 -32.238 1.00 13.45 ? 108 ARG A CB 1 ATOM 816 C CG . ARG A 1 108 ? 12.708 5.678 -32.107 1.00 12.43 ? 108 ARG A CG 1 ATOM 817 C CD . ARG A 1 108 ? 11.359 5.858 -31.432 1.00 13.92 ? 108 ARG A CD 1 ATOM 818 N NE . ARG A 1 108 ? 10.279 5.306 -32.244 1.00 26.37 ? 108 ARG A NE 1 ATOM 819 C CZ . ARG A 1 108 ? 9.020 5.183 -31.836 1.00 20.83 ? 108 ARG A CZ 1 ATOM 820 N NH1 . ARG A 1 108 ? 8.675 5.569 -30.615 1.00 13.50 ? 108 ARG A NH1 1 ATOM 821 N NH2 . ARG A 1 108 ? 8.106 4.669 -32.648 1.00 27.36 ? 108 ARG A NH2 1 ATOM 822 N N . THR A 1 109 ? 12.107 3.525 -34.978 1.00 13.11 ? 109 THR A N 1 ATOM 823 C CA . THR A 1 109 ? 11.304 3.768 -36.171 1.00 12.20 ? 109 THR A CA 1 ATOM 824 C C . THR A 1 109 ? 10.784 5.200 -36.180 1.00 21.56 ? 109 THR A C 1 ATOM 825 O O . THR A 1 109 ? 10.549 5.782 -35.122 1.00 20.55 ? 109 THR A O 1 ATOM 826 C CB . THR A 1 109 ? 10.114 2.796 -36.263 1.00 11.83 ? 109 THR A CB 1 ATOM 827 O OG1 . THR A 1 109 ? 9.272 2.960 -35.115 1.00 42.97 ? 109 THR A OG1 1 ATOM 828 C CG2 . THR A 1 109 ? 10.601 1.358 -36.328 1.00 9.65 ? 109 THR A CG2 1 ATOM 829 N N . VAL A 1 110 ? 10.608 5.758 -37.374 1.00 15.81 ? 110 VAL A N 1 ATOM 830 C CA . VAL A 1 110 ? 10.169 7.143 -37.524 1.00 9.80 ? 110 VAL A CA 1 ATOM 831 C C . VAL A 1 110 ? 8.837 7.392 -36.829 1.00 11.11 ? 110 VAL A C 1 ATOM 832 O O . VAL A 1 110 ? 7.842 6.728 -37.119 1.00 15.07 ? 110 VAL A O 1 ATOM 833 C CB . VAL A 1 110 ? 10.024 7.537 -39.004 1.00 11.89 ? 110 VAL A CB 1 ATOM 834 C CG1 . VAL A 1 110 ? 10.246 9.030 -39.173 1.00 15.67 ? 110 VAL A CG1 1 ATOM 835 C CG2 . VAL A 1 110 ? 11.002 6.759 -39.854 1.00 48.83 ? 110 VAL A CG2 1 ATOM 836 N N . ALA A 1 111 ? 8.826 8.349 -35.909 1.00 10.90 ? 111 ALA A N 1 ATOM 837 C CA . ALA A 1 111 ? 7.605 8.714 -35.206 1.00 11.31 ? 111 ALA A CA 1 ATOM 838 C C . ALA A 1 111 ? 7.185 10.130 -35.570 1.00 11.47 ? 111 ALA A C 1 ATOM 839 O O . ALA A 1 111 ? 7.892 11.092 -35.276 1.00 13.33 ? 111 ALA A O 1 ATOM 840 C CB . ALA A 1 111 ? 7.794 8.584 -33.703 1.00 11.86 ? 111 ALA A CB 1 ATOM 841 N N . ALA A 1 112 ? 6.032 10.252 -36.219 1.00 9.04 ? 112 ALA A N 1 ATOM 842 C CA . ALA A 1 112 ? 5.495 11.558 -36.573 1.00 9.23 ? 112 ALA A CA 1 ATOM 843 C C . ALA A 1 112 ? 4.942 12.248 -35.333 1.00 11.61 ? 112 ALA A C 1 ATOM 844 O O . ALA A 1 112 ? 4.252 11.624 -34.528 1.00 24.49 ? 112 ALA A O 1 ATOM 845 C CB . ALA A 1 112 ? 4.420 11.423 -37.636 1.00 19.34 ? 112 ALA A CB 1 ATOM 846 N N . PRO A 1 113 ? 5.245 13.544 -35.174 1.00 10.25 ? 113 PRO A N 1 ATOM 847 C CA . PRO A 1 113 ? 4.807 14.293 -33.992 1.00 11.47 ? 113 PRO A CA 1 ATOM 848 C C . PRO A 1 113 ? 3.306 14.561 -33.973 1.00 12.41 ? 113 PRO A C 1 ATOM 849 O O . PRO A 1 113 ? 2.693 14.732 -35.026 1.00 22.01 ? 113 PRO A O 1 ATOM 850 C CB . PRO A 1 113 ? 5.584 15.606 -34.109 1.00 17.87 ? 113 PRO A CB 1 ATOM 851 C CG . PRO A 1 113 ? 5.805 15.771 -35.574 1.00 9.35 ? 113 PRO A CG 1 ATOM 852 C CD . PRO A 1 113 ? 6.021 14.383 -36.105 1.00 13.92 ? 113 PRO A CD 1 ATOM 853 N N . SER A 1 114 ? 2.724 14.588 -32.779 1.00 10.73 ? 114 SER A N 1 ATOM 854 C CA . SER A 1 114 ? 1.342 15.015 -32.615 1.00 11.18 ? 114 SER A CA 1 ATOM 855 C C . SER A 1 114 ? 1.324 16.499 -32.281 1.00 11.66 ? 114 SER A C 1 ATOM 856 O O . SER A 1 114 ? 1.836 16.910 -31.240 1.00 32.03 ? 114 SER A O 1 ATOM 857 C CB . SER A 1 114 ? 0.644 14.208 -31.522 1.00 12.13 ? 114 SER A CB 1 ATOM 858 O OG . SER A 1 114 ? 0.540 12.844 -31.885 1.00 26.64 ? 114 SER A OG 1 ATOM 859 N N . VAL A 1 115 ? 0.741 17.301 -33.164 1.00 9.48 ? 115 VAL A N 1 ATOM 860 C CA . VAL A 1 115 ? 0.787 18.750 -33.010 1.00 8.30 ? 115 VAL A CA 1 ATOM 861 C C . VAL A 1 115 ? -0.435 19.301 -32.282 1.00 8.86 ? 115 VAL A C 1 ATOM 862 O O . VAL A 1 115 ? -1.575 19.046 -32.669 1.00 15.51 ? 115 VAL A O 1 ATOM 863 C CB . VAL A 1 115 ? 0.909 19.451 -34.374 1.00 7.85 ? 115 VAL A CB 1 ATOM 864 C CG1 . VAL A 1 115 ? 1.184 20.932 -34.183 1.00 8.96 ? 115 VAL A CG1 1 ATOM 865 C CG2 . VAL A 1 115 ? 2.015 18.816 -35.193 1.00 9.76 ? 115 VAL A CG2 1 ATOM 866 N N . PHE A 1 116 ? -0.180 20.060 -31.221 1.00 9.20 ? 116 PHE A N 1 ATOM 867 C CA . PHE A 1 116 ? -1.232 20.746 -30.486 1.00 8.69 ? 116 PHE A CA 1 ATOM 868 C C . PHE A 1 116 ? -0.931 22.238 -30.443 1.00 11.96 ? 116 PHE A C 1 ATOM 869 O O . PHE A 1 116 ? 0.231 22.638 -30.381 1.00 13.89 ? 116 PHE A O 1 ATOM 870 C CB . PHE A 1 116 ? -1.361 20.192 -29.065 1.00 8.75 ? 116 PHE A CB 1 ATOM 871 C CG . PHE A 1 116 ? -1.712 18.732 -29.008 1.00 9.11 ? 116 PHE A CG 1 ATOM 872 C CD1 . PHE A 1 116 ? -0.722 17.765 -29.032 1.00 8.94 ? 116 PHE A CD1 1 ATOM 873 C CD2 . PHE A 1 116 ? -3.033 18.328 -28.920 1.00 16.32 ? 116 PHE A CD2 1 ATOM 874 C CE1 . PHE A 1 116 ? -1.044 16.422 -28.975 1.00 13.90 ? 116 PHE A CE1 1 ATOM 875 C CE2 . PHE A 1 116 ? -3.360 16.986 -28.863 1.00 19.13 ? 116 PHE A CE2 1 ATOM 876 C CZ . PHE A 1 116 ? -2.364 16.033 -28.891 1.00 12.24 ? 116 PHE A CZ 1 ATOM 877 N N . ILE A 1 117 ? -1.975 23.060 -30.477 1.00 15.94 ? 117 ILE A N 1 ATOM 878 C CA . ILE A 1 117 ? -1.798 24.507 -30.412 1.00 23.64 ? 117 ILE A CA 1 ATOM 879 C C . ILE A 1 117 ? -2.648 25.092 -29.286 1.00 20.82 ? 117 ILE A C 1 ATOM 880 O O . ILE A 1 117 ? -3.765 24.638 -29.032 1.00 17.10 ? 117 ILE A O 1 ATOM 881 C CB . ILE A 1 117 ? -2.146 25.186 -31.764 1.00 11.02 ? 117 ILE A CB 1 ATOM 882 C CG1 . ILE A 1 117 ? -1.757 26.667 -31.743 1.00 9.89 ? 117 ILE A CG1 1 ATOM 883 C CG2 . ILE A 1 117 ? -3.619 25.005 -32.112 1.00 11.79 ? 117 ILE A CG2 1 ATOM 884 C CD1 . ILE A 1 117 ? -1.878 27.347 -33.084 1.00 8.87 ? 117 ILE A CD1 1 ATOM 885 N N . PHE A 1 118 ? -2.104 26.089 -28.596 1.00 13.41 ? 118 PHE A N 1 ATOM 886 C CA . PHE A 1 118 ? -2.791 26.692 -27.462 1.00 9.50 ? 118 PHE A CA 1 ATOM 887 C C . PHE A 1 118 ? -2.888 28.203 -27.607 1.00 10.86 ? 118 PHE A C 1 ATOM 888 O O . PHE A 1 118 ? -1.872 28.881 -27.755 1.00 14.44 ? 118 PHE A O 1 ATOM 889 C CB . PHE A 1 118 ? -2.074 26.348 -26.154 1.00 9.42 ? 118 PHE A CB 1 ATOM 890 C CG . PHE A 1 118 ? -1.949 24.873 -25.896 1.00 12.34 ? 118 PHE A CG 1 ATOM 891 C CD1 . PHE A 1 118 ? -2.970 24.176 -25.275 1.00 12.29 ? 118 PHE A CD1 1 ATOM 892 C CD2 . PHE A 1 118 ? -0.806 24.186 -26.265 1.00 10.02 ? 118 PHE A CD2 1 ATOM 893 C CE1 . PHE A 1 118 ? -2.855 22.820 -25.032 1.00 12.92 ? 118 PHE A CE1 1 ATOM 894 C CE2 . PHE A 1 118 ? -0.687 22.830 -26.025 1.00 7.80 ? 118 PHE A CE2 1 ATOM 895 C CZ . PHE A 1 118 ? -1.713 22.148 -25.408 1.00 9.48 ? 118 PHE A CZ 1 ATOM 896 N N . PRO A 1 119 ? -4.118 28.737 -27.573 1.00 11.54 ? 119 PRO A N 1 ATOM 897 C CA . PRO A 1 119 ? -4.315 30.189 -27.545 1.00 8.05 ? 119 PRO A CA 1 ATOM 898 C C . PRO A 1 119 ? -3.898 30.766 -26.198 1.00 12.54 ? 119 PRO A C 1 ATOM 899 O O . PRO A 1 119 ? -3.943 30.049 -25.198 1.00 22.29 ? 119 PRO A O 1 ATOM 900 C CB . PRO A 1 119 ? -5.824 30.350 -27.766 1.00 9.06 ? 119 PRO A CB 1 ATOM 901 C CG . PRO A 1 119 ? -6.294 29.026 -28.288 1.00 13.48 ? 119 PRO A CG 1 ATOM 902 C CD . PRO A 1 119 ? -5.395 28.013 -27.666 1.00 16.87 ? 119 PRO A CD 1 ATOM 903 N N . PRO A 1 120 ? -3.491 32.042 -26.167 1.00 12.45 ? 120 PRO A N 1 ATOM 904 C CA . PRO A 1 120 ? -3.144 32.670 -24.889 1.00 24.42 ? 120 PRO A CA 1 ATOM 905 C C . PRO A 1 120 ? -4.373 32.852 -24.003 1.00 24.59 ? 120 PRO A C 1 ATOM 906 O O . PRO A 1 120 ? -5.435 33.232 -24.497 1.00 30.52 ? 120 PRO A O 1 ATOM 907 C CB . PRO A 1 120 ? -2.557 34.021 -25.309 1.00 14.73 ? 120 PRO A CB 1 ATOM 908 C CG . PRO A 1 120 ? -3.174 34.302 -26.633 1.00 12.34 ? 120 PRO A CG 1 ATOM 909 C CD . PRO A 1 120 ? -3.326 32.966 -27.303 1.00 13.74 ? 120 PRO A CD 1 ATOM 910 N N . SER A 1 121 ? -4.215 32.603 -22.720 1.00 18.16 ? 121 SER A N 1 ATOM 911 C CA . SER A 1 121 ? -5.308 32.689 -21.803 1.00 19.51 ? 121 SER A CA 1 ATOM 912 C C . SER A 1 121 ? -5.744 34.124 -21.632 1.00 29.56 ? 121 SER A C 1 ATOM 913 O O . SER A 1 121 ? -4.983 35.035 -21.881 1.00 29.73 ? 121 SER A O 1 ATOM 914 C CB . SER A 1 121 ? -4.906 32.096 -20.469 1.00 18.81 ? 121 SER A CB 1 ATOM 915 O OG . SER A 1 121 ? -4.017 32.936 -19.789 1.00 29.02 ? 121 SER A OG 1 ATOM 916 N N . ASP A 1 122 ? -6.997 34.301 -21.239 1.00 30.80 ? 122 ASP A N 1 ATOM 917 C CA . ASP A 1 122 ? -7.584 35.595 -20.939 1.00 25.31 ? 122 ASP A CA 1 ATOM 918 C C . ASP A 1 122 ? -6.939 36.303 -19.766 1.00 23.79 ? 122 ASP A C 1 ATOM 919 O O . ASP A 1 122 ? -6.855 37.513 -19.731 1.00 24.68 ? 122 ASP A O 1 ATOM 920 C CB . ASP A 1 122 ? -9.061 35.430 -20.694 1.00 29.70 ? 122 ASP A CB 1 ATOM 921 C CG . ASP A 1 122 ? -9.840 35.411 -21.958 1.00 46.80 ? 122 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 122 ? -9.314 34.883 -22.939 1.00 76.11 ? 122 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 122 ? -10.969 35.922 -21.986 1.00 45.39 ? 122 ASP A OD2 1 ATOM 924 N N . GLU A 1 123 ? -6.536 35.521 -18.783 1.00 24.73 ? 123 GLU A N 1 ATOM 925 C CA . GLU A 1 123 ? -5.868 36.016 -17.610 1.00 31.56 ? 123 GLU A CA 1 ATOM 926 C C . GLU A 1 123 ? -4.568 36.685 -17.988 1.00 28.23 ? 123 GLU A C 1 ATOM 927 O O . GLU A 1 123 ? -4.233 37.725 -17.479 1.00 28.52 ? 123 GLU A O 1 ATOM 928 C CB . GLU A 1 123 ? -5.569 34.832 -16.718 1.00 29.01 ? 123 GLU A CB 1 ATOM 929 C CG . GLU A 1 123 ? -5.345 35.159 -15.256 1.00 48.10 ? 123 GLU A CG 1 ATOM 930 C CD . GLU A 1 123 ? -4.733 33.998 -14.515 1.00 56.08 ? 123 GLU A CD 1 ATOM 931 O OE1 . GLU A 1 123 ? -4.866 32.869 -15.000 1.00 43.82 ? 123 GLU A OE1 1 ATOM 932 O OE2 . GLU A 1 123 ? -4.116 34.210 -13.460 1.00 48.97 ? 123 GLU A OE2 1 ATOM 933 N N . GLN A 1 124 ? -3.836 36.072 -18.895 1.00 22.93 ? 124 GLN A N 1 ATOM 934 C CA . GLN A 1 124 ? -2.595 36.620 -19.411 1.00 21.93 ? 124 GLN A CA 1 ATOM 935 C C . GLN A 1 124 ? -2.709 37.909 -20.208 1.00 25.04 ? 124 GLN A C 1 ATOM 936 O O . GLN A 1 124 ? -1.815 38.719 -20.182 1.00 37.34 ? 124 GLN A O 1 ATOM 937 C CB . GLN A 1 124 ? -1.863 35.586 -20.222 1.00 27.88 ? 124 GLN A CB 1 ATOM 938 C CG . GLN A 1 124 ? -0.537 36.093 -20.744 1.00 17.71 ? 124 GLN A CG 1 ATOM 939 C CD . GLN A 1 124 ? 0.234 35.066 -21.516 1.00 14.10 ? 124 GLN A CD 1 ATOM 940 O OE1 . GLN A 1 124 ? 1.401 35.235 -21.754 1.00 12.15 ? 124 GLN A OE1 1 ATOM 941 N NE2 . GLN A 1 124 ? -0.416 33.994 -21.892 1.00 16.53 ? 124 GLN A NE2 1 ATOM 942 N N . LEU A 1 125 ? -3.773 38.043 -20.977 1.00 23.14 ? 125 LEU A N 1 ATOM 943 C CA . LEU A 1 125 ? -4.018 39.197 -21.836 1.00 23.37 ? 125 LEU A CA 1 ATOM 944 C C . LEU A 1 125 ? -4.103 40.493 -21.034 1.00 33.03 ? 125 LEU A C 1 ATOM 945 O O . LEU A 1 125 ? -3.778 41.566 -21.541 1.00 35.55 ? 125 LEU A O 1 ATOM 946 C CB . LEU A 1 125 ? -5.296 38.996 -22.650 1.00 20.51 ? 125 LEU A CB 1 ATOM 947 C CG . LEU A 1 125 ? -5.204 37.954 -23.768 1.00 17.91 ? 125 LEU A CG 1 ATOM 948 C CD1 . LEU A 1 125 ? -6.531 37.820 -24.496 1.00 18.10 ? 125 LEU A CD1 1 ATOM 949 C CD2 . LEU A 1 125 ? -4.091 38.314 -24.739 1.00 16.40 ? 125 LEU A CD2 1 ATOM 950 N N . LYS A 1 126 ? -4.531 40.387 -19.780 1.00 32.93 ? 126 LYS A N 1 ATOM 951 C CA . LYS A 1 126 ? -4.613 41.550 -18.903 1.00 26.53 ? 126 LYS A CA 1 ATOM 952 C C . LYS A 1 126 ? -3.224 42.057 -18.527 1.00 29.58 ? 126 LYS A C 1 ATOM 953 O O . LYS A 1 126 ? -3.070 43.189 -18.068 1.00 43.23 ? 126 LYS A O 1 ATOM 954 C CB . LYS A 1 126 ? -5.412 41.218 -17.641 1.00 27.67 ? 126 LYS A CB 1 ATOM 955 C CG . LYS A 1 126 ? -6.881 40.923 -17.896 1.00 44.57 ? 126 LYS A CG 1 ATOM 956 C CD . LYS A 1 126 ? -7.655 40.765 -16.594 1.00 49.32 ? 126 LYS A CD 1 ATOM 957 C CE . LYS A 1 126 ? -7.134 39.597 -15.769 1.00 44.28 ? 126 LYS A CE 1 ATOM 958 N NZ . LYS A 1 126 ? -7.934 39.390 -14.529 1.00 45.00 ? 126 LYS A NZ 1 ATOM 959 N N . SER A 1 127 ? -2.216 41.213 -18.723 1.00 30.19 ? 127 SER A N 1 ATOM 960 C CA . SER A 1 127 ? -0.833 41.589 -18.453 1.00 31.81 ? 127 SER A CA 1 ATOM 961 C C . SER A 1 127 ? -0.264 42.458 -19.570 1.00 31.16 ? 127 SER A C 1 ATOM 962 O O . SER A 1 127 ? 0.637 43.266 -19.342 1.00 45.91 ? 127 SER A O 1 ATOM 963 C CB . SER A 1 127 ? 0.032 40.342 -18.265 1.00 43.18 ? 127 SER A CB 1 ATOM 964 O OG . SER A 1 127 ? -0.360 39.617 -17.112 1.00 74.14 ? 127 SER A OG 1 ATOM 965 N N . GLY A 1 128 ? -0.791 42.286 -20.778 1.00 27.19 ? 128 GLY A N 1 ATOM 966 C CA . GLY A 1 128 ? -0.340 43.061 -21.920 1.00 26.22 ? 128 GLY A CA 1 ATOM 967 C C . GLY A 1 128 ? 0.561 42.273 -22.852 1.00 29.82 ? 128 GLY A C 1 ATOM 968 O O . GLY A 1 128 ? 1.157 42.829 -23.773 1.00 26.69 ? 128 GLY A O 1 ATOM 969 N N . THR A 1 129 ? 0.659 40.970 -22.610 1.00 33.53 ? 129 THR A N 1 ATOM 970 C CA . THR A 1 129 ? 1.477 40.096 -23.441 1.00 22.55 ? 129 THR A CA 1 ATOM 971 C C . THR A 1 129 ? 0.710 38.826 -23.788 1.00 20.45 ? 129 THR A C 1 ATOM 972 O O . THR A 1 129 ? 0.028 38.255 -22.938 1.00 29.90 ? 129 THR A O 1 ATOM 973 C CB . THR A 1 129 ? 2.797 39.718 -22.741 1.00 24.86 ? 129 THR A CB 1 ATOM 974 O OG1 . THR A 1 129 ? 3.459 40.905 -22.286 1.00 41.44 ? 129 THR A OG1 1 ATOM 975 C CG2 . THR A 1 129 ? 3.715 38.967 -23.693 1.00 22.18 ? 129 THR A CG2 1 ATOM 976 N N . ALA A 1 130 ? 0.820 38.391 -25.039 1.00 21.10 ? 130 ALA A N 1 ATOM 977 C CA . ALA A 1 130 ? 0.152 37.174 -25.482 1.00 19.98 ? 130 ALA A CA 1 ATOM 978 C C . ALA A 1 130 ? 1.164 36.108 -25.884 1.00 20.85 ? 130 ALA A C 1 ATOM 979 O O . ALA A 1 130 ? 1.958 36.308 -26.803 1.00 29.09 ? 130 ALA A O 1 ATOM 980 C CB . ALA A 1 130 ? -0.787 37.476 -26.639 1.00 17.34 ? 130 ALA A CB 1 ATOM 981 N N . SER A 1 131 ? 1.132 34.975 -25.190 1.00 16.68 ? 131 SER A N 1 ATOM 982 C CA . SER A 1 131 ? 2.005 33.856 -25.516 1.00 11.22 ? 131 SER A CA 1 ATOM 983 C C . SER A 1 131 ? 1.212 32.712 -26.139 1.00 13.16 ? 131 SER A C 1 ATOM 984 O O . SER A 1 131 ? 0.348 32.118 -25.494 1.00 11.18 ? 131 SER A O 1 ATOM 985 C CB . SER A 1 131 ? 2.747 33.365 -24.271 1.00 11.81 ? 131 SER A CB 1 ATOM 986 O OG . SER A 1 131 ? 3.617 34.362 -23.762 1.00 16.73 ? 131 SER A OG 1 ATOM 987 N N . VAL A 1 132 ? 1.507 32.416 -27.401 1.00 9.64 ? 132 VAL A N 1 ATOM 988 C CA . VAL A 1 132 ? 0.876 31.303 -28.097 1.00 7.40 ? 132 VAL A CA 1 ATOM 989 C C . VAL A 1 132 ? 1.836 30.119 -28.148 1.00 8.88 ? 132 VAL A C 1 ATOM 990 O O . VAL A 1 132 ? 2.985 30.260 -28.566 1.00 12.64 ? 132 VAL A O 1 ATOM 991 C CB . VAL A 1 132 ? 0.453 31.696 -29.523 1.00 6.96 ? 132 VAL A CB 1 ATOM 992 C CG1 . VAL A 1 132 ? -0.393 30.600 -30.146 1.00 8.15 ? 132 VAL A CG1 1 ATOM 993 C CG2 . VAL A 1 132 ? -0.316 33.005 -29.498 1.00 9.44 ? 132 VAL A CG2 1 ATOM 994 N N . VAL A 1 133 ? 1.363 28.953 -27.719 1.00 5.62 ? 133 VAL A N 1 ATOM 995 C CA . VAL A 1 133 ? 2.221 27.779 -27.603 1.00 6.56 ? 133 VAL A CA 1 ATOM 996 C C . VAL A 1 133 ? 1.857 26.676 -28.592 1.00 9.53 ? 133 VAL A C 1 ATOM 997 O O . VAL A 1 133 ? 0.713 26.222 -28.638 1.00 12.22 ? 133 VAL A O 1 ATOM 998 C CB . VAL A 1 133 ? 2.169 27.197 -26.177 1.00 7.41 ? 133 VAL A CB 1 ATOM 999 C CG1 . VAL A 1 133 ? 2.997 25.924 -26.088 1.00 8.12 ? 133 VAL A CG1 1 ATOM 1000 C CG2 . VAL A 1 133 ? 2.650 28.227 -25.169 1.00 11.54 ? 133 VAL A CG2 1 ATOM 1001 N N . CYS A 1 134 ? 2.837 26.249 -29.382 1.00 12.24 ? 134 CYS A N 1 ATOM 1002 C CA . CYS A 1 134 ? 2.670 25.091 -30.252 1.00 9.91 ? 134 CYS A CA 1 ATOM 1003 C C . CYS A 1 134 ? 3.406 23.895 -29.660 1.00 22.62 ? 134 CYS A C 1 ATOM 1004 O O . CYS A 1 134 ? 4.574 24.000 -29.288 1.00 10.46 ? 134 CYS A O 1 ATOM 1005 C CB . CYS A 1 134 ? 3.182 25.387 -31.661 1.00 10.48 ? 134 CYS A CB 1 ATOM 1006 S SG . CYS A 1 134 ? 3.014 24.006 -32.813 1.00 34.65 ? 134 CYS A SG 1 ATOM 1007 N N . LEU A 1 135 ? 2.719 22.761 -29.574 1.00 16.24 ? 135 LEU A N 1 ATOM 1008 C CA . LEU A 1 135 ? 3.286 21.571 -28.951 1.00 7.01 ? 135 LEU A CA 1 ATOM 1009 C C . LEU A 1 135 ? 3.535 20.453 -29.958 1.00 16.69 ? 135 LEU A C 1 ATOM 1010 O O . LEU A 1 135 ? 2.656 20.105 -30.744 1.00 13.70 ? 135 LEU A O 1 ATOM 1011 C CB . LEU A 1 135 ? 2.363 21.070 -27.838 1.00 6.62 ? 135 LEU A CB 1 ATOM 1012 C CG . LEU A 1 135 ? 2.691 19.714 -27.210 1.00 7.07 ? 135 LEU A CG 1 ATOM 1013 C CD1 . LEU A 1 135 ? 4.039 19.747 -26.513 1.00 6.53 ? 135 LEU A CD1 1 ATOM 1014 C CD2 . LEU A 1 135 ? 1.597 19.300 -26.242 1.00 6.68 ? 135 LEU A CD2 1 ATOM 1015 N N . LEU A 1 136 ? 4.743 19.901 -29.927 1.00 13.30 ? 136 LEU A N 1 ATOM 1016 C CA . LEU A 1 136 ? 5.087 18.736 -30.734 1.00 8.02 ? 136 LEU A CA 1 ATOM 1017 C C . LEU A 1 136 ? 5.381 17.571 -29.798 1.00 10.05 ? 136 LEU A C 1 ATOM 1018 O O . LEU A 1 136 ? 6.377 17.586 -29.076 1.00 16.46 ? 136 LEU A O 1 ATOM 1019 C CB . LEU A 1 136 ? 6.289 19.021 -31.639 1.00 9.39 ? 136 LEU A CB 1 ATOM 1020 C CG . LEU A 1 136 ? 6.093 19.908 -32.873 1.00 7.43 ? 136 LEU A CG 1 ATOM 1021 C CD1 . LEU A 1 136 ? 5.888 21.374 -32.507 1.00 8.60 ? 136 LEU A CD1 1 ATOM 1022 C CD2 . LEU A 1 136 ? 7.273 19.755 -33.817 1.00 10.05 ? 136 LEU A CD2 1 ATOM 1023 N N . ASN A 1 137 ? 4.516 16.562 -29.811 1.00 10.34 ? 137 ASN A N 1 ATOM 1024 C CA . ASN A 1 137 ? 4.557 15.522 -28.789 1.00 11.92 ? 137 ASN A CA 1 ATOM 1025 C C . ASN A 1 137 ? 4.991 14.148 -29.299 1.00 13.19 ? 137 ASN A C 1 ATOM 1026 O O . ASN A 1 137 ? 4.375 13.587 -30.205 1.00 19.26 ? 137 ASN A O 1 ATOM 1027 C CB . ASN A 1 137 ? 3.185 15.414 -28.119 1.00 15.58 ? 137 ASN A CB 1 ATOM 1028 C CG . ASN A 1 137 ? 3.221 14.603 -26.842 1.00 23.41 ? 137 ASN A CG 1 ATOM 1029 O OD1 . ASN A 1 137 ? 2.607 13.541 -26.749 1.00 38.71 ? 137 ASN A OD1 1 ATOM 1030 N ND2 . ASN A 1 137 ? 3.945 15.100 -25.847 1.00 16.97 ? 137 ASN A ND2 1 ATOM 1031 N N . ASN A 1 138 ? 6.057 13.624 -28.696 1.00 15.34 ? 138 ASN A N 1 ATOM 1032 C CA . ASN A 1 138 ? 6.578 12.269 -28.971 1.00 14.27 ? 138 ASN A CA 1 ATOM 1033 C C . ASN A 1 138 ? 7.216 11.617 -30.192 1.00 15.53 ? 138 ASN A C 1 ATOM 1034 O O . ASN A 1 138 ? 6.915 10.466 -30.510 1.00 37.96 ? 138 ASN A O 1 ATOM 1035 C CB . ASN A 1 138 ? 5.585 11.227 -28.480 1.00 15.47 ? 138 ASN A CB 1 ATOM 1036 C CG . ASN A 1 138 ? 5.353 11.305 -26.984 1.00 17.01 ? 138 ASN A CG 1 ATOM 1037 O OD1 . ASN A 1 138 ? 4.215 11.294 -26.520 1.00 14.31 ? 138 ASN A OD1 1 ATOM 1038 N ND2 . ASN A 1 138 ? 6.436 11.390 -26.221 1.00 44.51 ? 138 ASN A ND2 1 ATOM 1039 N N . PHE A 1 139 ? 8.123 12.335 -30.846 1.00 14.90 ? 139 PHE A N 1 ATOM 1040 C CA . PHE A 1 139 ? 8.544 12.134 -32.230 1.00 12.22 ? 139 PHE A CA 1 ATOM 1041 C C . PHE A 1 139 ? 10.007 11.744 -32.356 1.00 14.11 ? 139 PHE A C 1 ATOM 1042 O O . PHE A 1 139 ? 10.798 11.948 -31.436 1.00 27.47 ? 139 PHE A O 1 ATOM 1043 C CB . PHE A 1 139 ? 8.289 13.415 -33.062 1.00 12.23 ? 139 PHE A CB 1 ATOM 1044 C CG . PHE A 1 139 ? 9.019 14.630 -32.556 1.00 9.46 ? 139 PHE A CG 1 ATOM 1045 C CD1 . PHE A 1 139 ? 8.431 15.469 -31.628 1.00 17.32 ? 139 PHE A CD1 1 ATOM 1046 C CD2 . PHE A 1 139 ? 10.287 14.940 -33.018 1.00 9.62 ? 139 PHE A CD2 1 ATOM 1047 C CE1 . PHE A 1 139 ? 9.096 16.587 -31.163 1.00 8.77 ? 139 PHE A CE1 1 ATOM 1048 C CE2 . PHE A 1 139 ? 10.956 16.058 -32.555 1.00 9.12 ? 139 PHE A CE2 1 ATOM 1049 C CZ . PHE A 1 139 ? 10.358 16.880 -31.627 1.00 6.99 ? 139 PHE A CZ 1 ATOM 1050 N N . TYR A 1 140 ? 10.370 11.143 -33.464 1.00 19.86 ? 140 TYR A N 1 ATOM 1051 C CA . TYR A 1 140 ? 11.753 10.874 -33.743 1.00 17.33 ? 140 TYR A CA 1 ATOM 1052 C C . TYR A 1 140 ? 11.884 10.939 -35.257 1.00 32.61 ? 140 TYR A C 1 ATOM 1053 O O . TYR A 1 140 ? 10.963 10.532 -35.931 1.00 28.45 ? 140 TYR A O 1 ATOM 1054 C CB . TYR A 1 140 ? 12.084 9.499 -33.210 1.00 11.98 ? 140 TYR A CB 1 ATOM 1055 C CG . TYR A 1 140 ? 13.493 9.103 -33.446 1.00 15.03 ? 140 TYR A CG 1 ATOM 1056 C CD1 . TYR A 1 140 ? 14.478 9.421 -32.550 1.00 14.32 ? 140 TYR A CD1 1 ATOM 1057 C CD2 . TYR A 1 140 ? 13.840 8.427 -34.575 1.00 30.16 ? 140 TYR A CD2 1 ATOM 1058 C CE1 . TYR A 1 140 ? 15.775 9.064 -32.776 1.00 14.00 ? 140 TYR A CE1 1 ATOM 1059 C CE2 . TYR A 1 140 ? 15.132 8.062 -34.798 1.00 23.57 ? 140 TYR A CE2 1 ATOM 1060 C CZ . TYR A 1 140 ? 16.084 8.389 -33.898 1.00 17.35 ? 140 TYR A CZ 1 ATOM 1061 O OH . TYR A 1 140 ? 17.351 8.013 -34.167 1.00 33.20 ? 140 TYR A OH 1 ATOM 1062 N N . PRO A 1 141 ? 13.044 11.455 -35.876 1.00 17.24 ? 141 PRO A N 1 ATOM 1063 C CA . PRO A 1 141 ? 14.119 11.882 -34.973 1.00 12.39 ? 141 PRO A CA 1 ATOM 1064 C C . PRO A 1 141 ? 13.988 13.286 -34.428 1.00 11.80 ? 141 PRO A C 1 ATOM 1065 O O . PRO A 1 141 ? 12.970 13.910 -34.620 1.00 11.18 ? 141 PRO A O 1 ATOM 1066 C CB . PRO A 1 141 ? 15.356 11.797 -35.873 1.00 20.00 ? 141 PRO A CB 1 ATOM 1067 C CG . PRO A 1 141 ? 14.852 12.111 -37.238 1.00 20.00 ? 141 PRO A CG 1 ATOM 1068 C CD . PRO A 1 141 ? 13.385 12.358 -37.075 1.00 20.00 ? 141 PRO A CD 1 ATOM 1069 N N . ARG A 1 142 ? 15.014 13.750 -33.719 1.00 20.73 ? 142 ARG A N 1 ATOM 1070 C CA . ARG A 1 142 ? 14.929 14.943 -32.904 1.00 14.38 ? 142 ARG A CA 1 ATOM 1071 C C . ARG A 1 142 ? 14.642 16.145 -33.731 1.00 11.47 ? 142 ARG A C 1 ATOM 1072 O O . ARG A 1 142 ? 14.155 17.136 -33.244 1.00 13.61 ? 142 ARG A O 1 ATOM 1073 C CB . ARG A 1 142 ? 16.219 15.149 -32.144 1.00 14.09 ? 142 ARG A CB 1 ATOM 1074 C CG . ARG A 1 142 ? 16.159 16.244 -31.114 1.00 17.65 ? 142 ARG A CG 1 ATOM 1075 C CD . ARG A 1 142 ? 17.536 16.463 -30.565 1.00 18.96 ? 142 ARG A CD 1 ATOM 1076 N NE . ARG A 1 142 ? 17.573 17.333 -29.414 1.00 18.37 ? 142 ARG A NE 1 ATOM 1077 C CZ . ARG A 1 142 ? 17.748 18.645 -29.465 1.00 24.92 ? 142 ARG A CZ 1 ATOM 1078 N NH1 . ARG A 1 142 ? 17.860 19.265 -30.616 1.00 41.93 ? 142 ARG A NH1 1 ATOM 1079 N NH2 . ARG A 1 142 ? 17.789 19.348 -28.353 1.00 58.79 ? 142 ARG A NH2 1 ATOM 1080 N N . GLU A 1 143 ? 15.003 16.064 -34.987 1.00 11.92 ? 143 GLU A N 1 ATOM 1081 C CA . GLU A 1 143 ? 14.990 17.213 -35.854 1.00 12.76 ? 143 GLU A CA 1 ATOM 1082 C C . GLU A 1 143 ? 13.597 17.578 -36.329 1.00 10.50 ? 143 GLU A C 1 ATOM 1083 O O . GLU A 1 143 ? 12.906 16.776 -36.894 1.00 18.28 ? 143 GLU A O 1 ATOM 1084 C CB . GLU A 1 143 ? 15.923 16.982 -37.049 1.00 28.90 ? 143 GLU A CB 1 ATOM 1085 C CG . GLU A 1 143 ? 17.414 16.848 -36.746 1.00 23.44 ? 143 GLU A CG 1 ATOM 1086 C CD . GLU A 1 143 ? 17.817 15.448 -36.366 1.00 39.85 ? 143 GLU A CD 1 ATOM 1087 O OE1 . GLU A 1 143 ? 16.942 14.583 -36.279 1.00 64.70 ? 143 GLU A OE1 1 ATOM 1088 O OE2 . GLU A 1 143 ? 19.007 15.207 -36.145 1.00 26.55 ? 143 GLU A OE2 1 ATOM 1089 N N . ALA A 1 144 ? 13.205 18.817 -36.104 1.00 9.36 ? 144 ALA A N 1 ATOM 1090 C CA . ALA A 1 144 ? 11.890 19.275 -36.472 1.00 8.03 ? 144 ALA A CA 1 ATOM 1091 C C . ALA A 1 144 ? 11.907 20.717 -36.924 1.00 15.06 ? 144 ALA A C 1 ATOM 1092 O O . ALA A 1 144 ? 12.734 21.481 -36.495 1.00 11.69 ? 144 ALA A O 1 ATOM 1093 C CB . ALA A 1 144 ? 10.950 19.106 -35.305 1.00 7.30 ? 144 ALA A CB 1 ATOM 1094 N N . LYS A 1 145 ? 10.975 21.082 -37.792 1.00 16.90 ? 145 LYS A N 1 ATOM 1095 C CA . LYS A 1 145 ? 10.831 22.466 -38.218 1.00 14.02 ? 145 LYS A CA 1 ATOM 1096 C C . LYS A 1 145 ? 9.471 23.042 -37.893 1.00 14.67 ? 145 LYS A C 1 ATOM 1097 O O . LYS A 1 145 ? 8.469 22.529 -38.289 1.00 21.33 ? 145 LYS A O 1 ATOM 1098 C CB . LYS A 1 145 ? 11.093 22.582 -39.704 1.00 19.82 ? 145 LYS A CB 1 ATOM 1099 C CG . LYS A 1 145 ? 10.754 23.939 -40.278 1.00 41.43 ? 145 LYS A CG 1 ATOM 1100 C CD . LYS A 1 145 ? 11.652 24.315 -41.438 1.00 42.00 ? 145 LYS A CD 1 ATOM 1101 C CE . LYS A 1 145 ? 10.949 25.275 -42.362 1.00 29.52 ? 145 LYS A CE 1 ATOM 1102 N NZ . LYS A 1 145 ? 10.578 24.595 -43.625 1.00 49.94 ? 145 LYS A NZ 1 ATOM 1103 N N . VAL A 1 146 ? 9.471 24.154 -37.185 1.00 32.31 ? 146 VAL A N 1 ATOM 1104 C CA . VAL A 1 146 ? 8.267 24.838 -36.746 1.00 13.30 ? 146 VAL A CA 1 ATOM 1105 C C . VAL A 1 146 ? 8.247 26.256 -37.288 1.00 11.84 ? 146 VAL A C 1 ATOM 1106 O O . VAL A 1 146 ? 9.232 26.950 -37.253 1.00 11.29 ? 146 VAL A O 1 ATOM 1107 C CB . VAL A 1 146 ? 8.171 24.834 -35.214 1.00 12.50 ? 146 VAL A CB 1 ATOM 1108 C CG1 . VAL A 1 146 ? 6.847 25.363 -34.737 1.00 11.87 ? 146 VAL A CG1 1 ATOM 1109 C CG2 . VAL A 1 146 ? 8.332 23.429 -34.707 1.00 18.53 ? 146 VAL A CG2 1 ATOM 1110 N N . GLN A 1 147 ? 7.116 26.650 -37.838 1.00 13.00 ? 147 GLN A N 1 ATOM 1111 C CA . GLN A 1 147 ? 6.944 27.978 -38.377 1.00 13.19 ? 147 GLN A CA 1 ATOM 1112 C C . GLN A 1 147 ? 5.675 28.570 -37.845 1.00 14.21 ? 147 GLN A C 1 ATOM 1113 O O . GLN A 1 147 ? 4.709 27.880 -37.671 1.00 15.75 ? 147 GLN A O 1 ATOM 1114 C CB . GLN A 1 147 ? 6.889 27.942 -39.890 1.00 19.22 ? 147 GLN A CB 1 ATOM 1115 C CG . GLN A 1 147 ? 8.249 27.829 -40.528 1.00 39.87 ? 147 GLN A CG 1 ATOM 1116 C CD . GLN A 1 147 ? 8.219 27.992 -42.015 1.00 43.41 ? 147 GLN A CD 1 ATOM 1117 O OE1 . GLN A 1 147 ? 7.260 27.629 -42.671 1.00 31.93 ? 147 GLN A OE1 1 ATOM 1118 N NE2 . GLN A 1 147 ? 9.287 28.539 -42.559 1.00 41.09 ? 147 GLN A NE2 1 ATOM 1119 N N . TRP A 1 148 ? 5.692 29.866 -37.599 1.00 13.79 ? 148 TRP A N 1 ATOM 1120 C CA . TRP A 1 148 ? 4.544 30.558 -37.079 1.00 10.30 ? 148 TRP A CA 1 ATOM 1121 C C . TRP A 1 148 ? 4.038 31.466 -38.170 1.00 15.08 ? 148 TRP A C 1 ATOM 1122 O O . TRP A 1 148 ? 4.806 32.055 -38.877 1.00 21.73 ? 148 TRP A O 1 ATOM 1123 C CB . TRP A 1 148 ? 4.899 31.343 -35.810 1.00 9.65 ? 148 TRP A CB 1 ATOM 1124 C CG . TRP A 1 148 ? 4.933 30.526 -34.550 1.00 9.84 ? 148 TRP A CG 1 ATOM 1125 C CD1 . TRP A 1 148 ? 6.027 30.066 -33.917 1.00 18.11 ? 148 TRP A CD1 1 ATOM 1126 C CD2 . TRP A 1 148 ? 3.824 30.079 -33.779 1.00 9.44 ? 148 TRP A CD2 1 ATOM 1127 N NE1 . TRP A 1 148 ? 5.690 29.364 -32.816 1.00 9.04 ? 148 TRP A NE1 1 ATOM 1128 C CE2 . TRP A 1 148 ? 4.333 29.358 -32.703 1.00 9.16 ? 148 TRP A CE2 1 ATOM 1129 C CE3 . TRP A 1 148 ? 2.449 30.210 -33.899 1.00 7.95 ? 148 TRP A CE3 1 ATOM 1130 C CZ2 . TRP A 1 148 ? 3.524 28.771 -31.762 1.00 8.45 ? 148 TRP A CZ2 1 ATOM 1131 C CZ3 . TRP A 1 148 ? 1.660 29.629 -32.960 1.00 6.64 ? 148 TRP A CZ3 1 ATOM 1132 C CH2 . TRP A 1 148 ? 2.196 28.920 -31.909 1.00 7.41 ? 148 TRP A CH2 1 ATOM 1133 N N . LYS A 1 149 ? 2.731 31.508 -38.343 1.00 27.50 ? 149 LYS A N 1 ATOM 1134 C CA . LYS A 1 149 ? 2.088 32.445 -39.231 1.00 17.68 ? 149 LYS A CA 1 ATOM 1135 C C . LYS A 1 149 ? 1.031 33.239 -38.495 1.00 16.32 ? 149 LYS A C 1 ATOM 1136 O O . LYS A 1 149 ? 0.221 32.674 -37.821 1.00 23.70 ? 149 LYS A O 1 ATOM 1137 C CB . LYS A 1 149 ? 1.435 31.698 -40.379 1.00 15.78 ? 149 LYS A CB 1 ATOM 1138 C CG . LYS A 1 149 ? 2.383 30.826 -41.154 1.00 16.31 ? 149 LYS A CG 1 ATOM 1139 C CD . LYS A 1 149 ? 1.662 30.089 -42.254 1.00 23.93 ? 149 LYS A CD 1 ATOM 1140 C CE . LYS A 1 149 ? 2.516 29.975 -43.497 1.00 24.21 ? 149 LYS A CE 1 ATOM 1141 N NZ . LYS A 1 149 ? 2.510 28.585 -44.002 1.00 40.19 ? 149 LYS A NZ 1 ATOM 1142 N N . VAL A 1 150 ? 1.033 34.553 -38.639 1.00 18.45 ? 150 VAL A N 1 ATOM 1143 C CA . VAL A 1 150 ? -0.115 35.346 -38.258 1.00 20.36 ? 150 VAL A CA 1 ATOM 1144 C C . VAL A 1 150 ? -0.732 35.901 -39.531 1.00 23.11 ? 150 VAL A C 1 ATOM 1145 O O . VAL A 1 150 ? -0.135 36.676 -40.228 1.00 29.24 ? 150 VAL A O 1 ATOM 1146 C CB . VAL A 1 150 ? 0.230 36.506 -37.297 1.00 20.36 ? 150 VAL A CB 1 ATOM 1147 C CG1 . VAL A 1 150 ? -1.029 37.188 -36.837 1.00 19.85 ? 150 VAL A CG1 1 ATOM 1148 C CG2 . VAL A 1 150 ? 0.936 36.010 -36.067 1.00 33.91 ? 150 VAL A CG2 1 ATOM 1149 N N . ASP A 1 151 ? -1.961 35.529 -39.804 1.00 33.20 ? 151 ASP A N 1 ATOM 1150 C CA . ASP A 1 151 ? -2.662 35.978 -41.000 1.00 40.23 ? 151 ASP A CA 1 ATOM 1151 C C . ASP A 1 151 ? -1.966 35.619 -42.304 1.00 28.43 ? 151 ASP A C 1 ATOM 1152 O O . ASP A 1 151 ? -1.964 36.401 -43.242 1.00 48.21 ? 151 ASP A O 1 ATOM 1153 C CB . ASP A 1 151 ? -2.942 37.475 -40.925 1.00 25.87 ? 151 ASP A CB 1 ATOM 1154 C CG . ASP A 1 151 ? -4.186 37.789 -40.151 1.00 23.74 ? 151 ASP A CG 1 ATOM 1155 O OD1 . ASP A 1 151 ? -4.984 36.895 -39.922 1.00 22.89 ? 151 ASP A OD1 1 ATOM 1156 O OD2 . ASP A 1 151 ? -4.373 38.935 -39.776 1.00 28.21 ? 151 ASP A OD2 1 ATOM 1157 N N . ASN A 1 152 ? -1.409 34.417 -42.357 1.00 29.82 ? 152 ASN A N 1 ATOM 1158 C CA . ASN A 1 152 ? -0.606 33.945 -43.486 1.00 22.82 ? 152 ASN A CA 1 ATOM 1159 C C . ASN A 1 152 ? 0.711 34.697 -43.660 1.00 23.93 ? 152 ASN A C 1 ATOM 1160 O O . ASN A 1 152 ? 1.278 34.719 -44.751 1.00 45.78 ? 152 ASN A O 1 ATOM 1161 C CB . ASN A 1 152 ? -1.415 34.023 -44.784 1.00 22.09 ? 152 ASN A CB 1 ATOM 1162 C CG . ASN A 1 152 ? -1.825 32.658 -45.297 1.00 25.90 ? 152 ASN A CG 1 ATOM 1163 O OD1 . ASN A 1 152 ? -1.103 31.676 -45.123 1.00 29.13 ? 152 ASN A OD1 1 ATOM 1164 N ND2 . ASN A 1 152 ? -2.988 32.589 -45.933 1.00 19.79 ? 152 ASN A ND2 1 ATOM 1165 N N . ALA A 1 153 ? 1.198 35.305 -42.583 1.00 22.65 ? 153 ALA A N 1 ATOM 1166 C CA . ALA A 1 153 ? 2.470 36.017 -42.620 1.00 23.03 ? 153 ALA A CA 1 ATOM 1167 C C . ALA A 1 153 ? 3.516 35.295 -41.777 1.00 29.59 ? 153 ALA A C 1 ATOM 1168 O O . ALA A 1 153 ? 3.296 35.028 -40.596 1.00 33.35 ? 153 ALA A O 1 ATOM 1169 C CB . ALA A 1 153 ? 2.293 37.449 -42.140 1.00 18.27 ? 153 ALA A CB 1 ATOM 1170 N N . LEU A 1 154 ? 4.621 34.911 -42.383 1.00 22.15 ? 154 LEU A N 1 ATOM 1171 C CA . LEU A 1 154 ? 5.635 34.189 -41.660 1.00 24.31 ? 154 LEU A CA 1 ATOM 1172 C C . LEU A 1 154 ? 6.193 35.062 -40.578 1.00 35.88 ? 154 LEU A C 1 ATOM 1173 O O . LEU A 1 154 ? 6.384 36.237 -40.786 1.00 41.14 ? 154 LEU A O 1 ATOM 1174 C CB . LEU A 1 154 ? 6.761 33.797 -42.590 1.00 25.79 ? 154 LEU A CB 1 ATOM 1175 C CG . LEU A 1 154 ? 6.929 32.314 -42.862 1.00 30.89 ? 154 LEU A CG 1 ATOM 1176 C CD1 . LEU A 1 154 ? 8.275 32.117 -43.512 1.00 46.99 ? 154 LEU A CD1 1 ATOM 1177 C CD2 . LEU A 1 154 ? 6.839 31.513 -41.585 1.00 38.60 ? 154 LEU A CD2 1 ATOM 1178 N N . GLN A 1 155 ? 6.478 34.470 -39.427 1.00 26.09 ? 155 GLN A N 1 ATOM 1179 C CA . GLN A 1 155 ? 6.921 35.197 -38.264 1.00 19.38 ? 155 GLN A CA 1 ATOM 1180 C C . GLN A 1 155 ? 8.358 34.868 -37.995 1.00 23.40 ? 155 GLN A C 1 ATOM 1181 O O . GLN A 1 155 ? 8.704 33.713 -37.981 1.00 46.68 ? 155 GLN A O 1 ATOM 1182 C CB . GLN A 1 155 ? 6.117 34.740 -37.071 1.00 18.48 ? 155 GLN A CB 1 ATOM 1183 C CG . GLN A 1 155 ? 4.657 35.091 -37.113 1.00 18.19 ? 155 GLN A CG 1 ATOM 1184 C CD . GLN A 1 155 ? 4.427 36.562 -37.219 1.00 20.66 ? 155 GLN A CD 1 ATOM 1185 O OE1 . GLN A 1 155 ? 4.393 37.263 -36.234 1.00 16.10 ? 155 GLN A OE1 1 ATOM 1186 N NE2 . GLN A 1 155 ? 4.255 37.036 -38.425 1.00 39.35 ? 155 GLN A NE2 1 ATOM 1187 N N . SER A 1 156 ? 9.213 35.864 -37.799 1.00 26.07 ? 156 SER A N 1 ATOM 1188 C CA . SER A 1 156 ? 10.601 35.573 -37.430 1.00 26.27 ? 156 SER A CA 1 ATOM 1189 C C . SER A 1 156 ? 11.175 36.379 -36.265 1.00 20.54 ? 156 SER A C 1 ATOM 1190 O O . SER A 1 156 ? 11.046 37.581 -36.200 1.00 17.30 ? 156 SER A O 1 ATOM 1191 C CB . SER A 1 156 ? 11.520 35.601 -38.648 1.00 22.63 ? 156 SER A CB 1 ATOM 1192 O OG . SER A 1 156 ? 12.218 36.817 -38.760 1.00 36.71 ? 156 SER A OG 1 ATOM 1193 N N . GLY A 1 157 ? 11.831 35.684 -35.355 1.00 27.81 ? 157 GLY A N 1 ATOM 1194 C CA . GLY A 1 157 ? 12.461 36.307 -34.211 1.00 22.82 ? 157 GLY A CA 1 ATOM 1195 C C . GLY A 1 157 ? 11.603 36.575 -32.999 1.00 18.74 ? 157 GLY A C 1 ATOM 1196 O O . GLY A 1 157 ? 12.063 37.156 -32.037 1.00 27.83 ? 157 GLY A O 1 ATOM 1197 N N . ASN A 1 158 ? 10.349 36.162 -33.060 1.00 22.14 ? 158 ASN A N 1 ATOM 1198 C CA . ASN A 1 158 ? 9.441 36.303 -31.945 1.00 16.87 ? 158 ASN A CA 1 ATOM 1199 C C . ASN A 1 158 ? 9.023 35.000 -31.301 1.00 21.87 ? 158 ASN A C 1 ATOM 1200 O O . ASN A 1 158 ? 8.072 34.974 -30.556 1.00 26.79 ? 158 ASN A O 1 ATOM 1201 C CB . ASN A 1 158 ? 8.235 37.144 -32.323 1.00 16.11 ? 158 ASN A CB 1 ATOM 1202 C CG . ASN A 1 158 ? 7.579 36.684 -33.583 1.00 16.29 ? 158 ASN A CG 1 ATOM 1203 O OD1 . ASN A 1 158 ? 8.023 35.763 -34.226 1.00 26.22 ? 158 ASN A OD1 1 ATOM 1204 N ND2 . ASN A 1 158 ? 6.507 37.323 -33.929 1.00 15.81 ? 158 ASN A ND2 1 ATOM 1205 N N . SER A 1 159 ? 9.739 33.926 -31.602 1.00 21.98 ? 159 SER A N 1 ATOM 1206 C CA . SER A 1 159 ? 9.491 32.632 -30.987 1.00 16.16 ? 159 SER A CA 1 ATOM 1207 C C . SER A 1 159 ? 10.746 32.024 -30.410 1.00 13.20 ? 159 SER A C 1 ATOM 1208 O O . SER A 1 159 ? 11.829 32.316 -30.841 1.00 31.42 ? 159 SER A O 1 ATOM 1209 C CB . SER A 1 159 ? 8.870 31.670 -31.967 1.00 13.44 ? 159 SER A CB 1 ATOM 1210 O OG . SER A 1 159 ? 9.711 31.493 -33.056 1.00 18.49 ? 159 SER A OG 1 ATOM 1211 N N . GLN A 1 160 ? 10.572 31.194 -29.399 1.00 9.86 ? 160 GLN A N 1 ATOM 1212 C CA . GLN A 1 160 ? 11.631 30.412 -28.819 1.00 7.67 ? 160 GLN A CA 1 ATOM 1213 C C . GLN A 1 160 ? 11.134 29.003 -28.668 1.00 9.24 ? 160 GLN A C 1 ATOM 1214 O O . GLN A 1 160 ? 9.961 28.791 -28.507 1.00 20.07 ? 160 GLN A O 1 ATOM 1215 C CB . GLN A 1 160 ? 11.989 30.935 -27.449 1.00 8.72 ? 160 GLN A CB 1 ATOM 1216 C CG . GLN A 1 160 ? 12.851 32.171 -27.444 1.00 8.53 ? 160 GLN A CG 1 ATOM 1217 C CD . GLN A 1 160 ? 13.054 32.708 -26.069 1.00 8.66 ? 160 GLN A CD 1 ATOM 1218 O OE1 . GLN A 1 160 ? 12.119 33.075 -25.410 1.00 15.14 ? 160 GLN A OE1 1 ATOM 1219 N NE2 . GLN A 1 160 ? 14.273 32.741 -25.631 1.00 16.37 ? 160 GLN A NE2 1 ATOM 1220 N N . GLU A 1 161 ? 12.027 28.031 -28.713 1.00 8.45 ? 161 GLU A N 1 ATOM 1221 C CA . GLU A 1 161 ? 11.618 26.658 -28.511 1.00 9.01 ? 161 GLU A CA 1 ATOM 1222 C C . GLU A 1 161 ? 12.443 25.846 -27.553 1.00 7.99 ? 161 GLU A C 1 ATOM 1223 O O . GLU A 1 161 ? 13.592 26.091 -27.362 1.00 18.02 ? 161 GLU A O 1 ATOM 1224 C CB . GLU A 1 161 ? 11.496 25.923 -29.816 1.00 26.33 ? 161 GLU A CB 1 ATOM 1225 C CG . GLU A 1 161 ? 12.769 25.786 -30.594 1.00 20.85 ? 161 GLU A CG 1 ATOM 1226 C CD . GLU A 1 161 ? 12.519 25.152 -31.921 1.00 41.28 ? 161 GLU A CD 1 ATOM 1227 O OE1 . GLU A 1 161 ? 11.461 24.533 -32.077 1.00 23.80 ? 161 GLU A OE1 1 ATOM 1228 O OE2 . GLU A 1 161 ? 13.384 25.268 -32.794 1.00 82.00 ? 161 GLU A OE2 1 ATOM 1229 N N . SER A 1 162 ? 11.802 24.873 -26.945 1.00 8.86 ? 162 SER A N 1 ATOM 1230 C CA . SER A 1 162 ? 12.405 23.988 -25.989 1.00 5.75 ? 162 SER A CA 1 ATOM 1231 C C . SER A 1 162 ? 12.181 22.566 -26.428 1.00 7.12 ? 162 SER A C 1 ATOM 1232 O O . SER A 1 162 ? 11.099 22.204 -26.805 1.00 13.51 ? 162 SER A O 1 ATOM 1233 C CB . SER A 1 162 ? 11.744 24.181 -24.647 1.00 7.45 ? 162 SER A CB 1 ATOM 1234 O OG . SER A 1 162 ? 11.980 25.459 -24.135 1.00 14.30 ? 162 SER A OG 1 ATOM 1235 N N . VAL A 1 163 ? 13.222 21.759 -26.365 1.00 5.14 ? 163 VAL A N 1 ATOM 1236 C CA . VAL A 1 163 ? 13.144 20.365 -26.698 1.00 5.48 ? 163 VAL A CA 1 ATOM 1237 C C . VAL A 1 163 ? 13.506 19.632 -25.443 1.00 10.39 ? 163 VAL A C 1 ATOM 1238 O O . VAL A 1 163 ? 14.424 20.014 -24.766 1.00 12.79 ? 163 VAL A O 1 ATOM 1239 C CB . VAL A 1 163 ? 14.143 19.993 -27.808 1.00 13.64 ? 163 VAL A CB 1 ATOM 1240 C CG1 . VAL A 1 163 ? 13.707 18.749 -28.554 1.00 12.35 ? 163 VAL A CG1 1 ATOM 1241 C CG2 . VAL A 1 163 ? 14.319 21.138 -28.785 1.00 16.17 ? 163 VAL A CG2 1 ATOM 1242 N N . THR A 1 164 ? 12.733 18.611 -25.112 1.00 7.33 ? 164 THR A N 1 ATOM 1243 C CA . THR A 1 164 ? 13.000 17.707 -24.000 1.00 7.32 ? 164 THR A CA 1 ATOM 1244 C C . THR A 1 164 ? 14.114 16.741 -24.370 1.00 11.42 ? 164 THR A C 1 ATOM 1245 O O . THR A 1 164 ? 14.431 16.571 -25.547 1.00 13.17 ? 164 THR A O 1 ATOM 1246 C CB . THR A 1 164 ? 11.754 16.895 -23.599 1.00 7.45 ? 164 THR A CB 1 ATOM 1247 O OG1 . THR A 1 164 ? 11.339 16.073 -24.697 1.00 10.34 ? 164 THR A OG1 1 ATOM 1248 C CG2 . THR A 1 164 ? 10.617 17.814 -23.200 1.00 9.98 ? 164 THR A CG2 1 ATOM 1249 N N . GLU A 1 165 ? 14.705 16.108 -23.364 1.00 21.40 ? 165 GLU A N 1 ATOM 1250 C CA . GLU A 1 165 ? 15.673 15.050 -23.611 1.00 17.20 ? 165 GLU A CA 1 ATOM 1251 C C . GLU A 1 165 ? 14.948 13.788 -24.063 1.00 17.15 ? 165 GLU A C 1 ATOM 1252 O O . GLU A 1 165 ? 13.736 13.663 -23.881 1.00 11.18 ? 165 GLU A O 1 ATOM 1253 C CB . GLU A 1 165 ? 16.512 14.773 -22.364 1.00 22.49 ? 165 GLU A CB 1 ATOM 1254 C CG . GLU A 1 165 ? 17.434 15.916 -21.972 1.00 30.21 ? 165 GLU A CG 1 ATOM 1255 C CD . GLU A 1 165 ? 18.196 15.633 -20.690 1.00 62.82 ? 165 GLU A CD 1 ATOM 1256 O OE1 . GLU A 1 165 ? 17.868 14.638 -20.010 1.00 64.29 ? 165 GLU A OE1 1 ATOM 1257 O OE2 . GLU A 1 165 ? 19.122 16.404 -20.360 1.00 57.84 ? 165 GLU A OE2 1 ATOM 1258 N N . GLN A 1 166 ? 15.691 12.860 -24.658 1.00 12.70 ? 166 GLN A N 1 ATOM 1259 C CA . GLN A 1 166 ? 15.108 11.632 -25.185 1.00 10.86 ? 166 GLN A CA 1 ATOM 1260 C C . GLN A 1 166 ? 14.459 10.813 -24.076 1.00 11.25 ? 166 GLN A C 1 ATOM 1261 O O . GLN A 1 166 ? 15.033 10.645 -23.001 1.00 11.74 ? 166 GLN A O 1 ATOM 1262 C CB . GLN A 1 166 ? 16.172 10.798 -25.902 1.00 20.86 ? 166 GLN A CB 1 ATOM 1263 C CG . GLN A 1 166 ? 15.610 9.633 -26.698 1.00 12.63 ? 166 GLN A CG 1 ATOM 1264 C CD . GLN A 1 166 ? 16.689 8.836 -27.402 1.00 10.63 ? 166 GLN A CD 1 ATOM 1265 O OE1 . GLN A 1 166 ? 17.839 8.812 -26.969 1.00 14.71 ? 166 GLN A OE1 1 ATOM 1266 N NE2 . GLN A 1 166 ? 16.323 8.184 -28.500 1.00 10.61 ? 166 GLN A NE2 1 ATOM 1267 N N . ASP A 1 167 ? 13.255 10.315 -24.341 1.00 12.63 ? 167 ASP A N 1 ATOM 1268 C CA . ASP A 1 167 ? 12.512 9.539 -23.356 1.00 19.85 ? 167 ASP A CA 1 ATOM 1269 C C . ASP A 1 167 ? 13.183 8.191 -23.113 1.00 19.67 ? 167 ASP A C 1 ATOM 1270 O O . ASP A 1 167 ? 13.735 7.587 -24.032 1.00 12.91 ? 167 ASP A O 1 ATOM 1271 C CB . ASP A 1 167 ? 11.065 9.344 -23.813 1.00 16.44 ? 167 ASP A CB 1 ATOM 1272 C CG . ASP A 1 167 ? 10.167 8.827 -22.706 1.00 22.79 ? 167 ASP A CG 1 ATOM 1273 O OD1 . ASP A 1 167 ? 9.638 9.656 -21.934 1.00 50.47 ? 167 ASP A OD1 1 ATOM 1274 O OD2 . ASP A 1 167 ? 9.984 7.595 -22.609 1.00 17.08 ? 167 ASP A OD2 1 ATOM 1275 N N . SER A 1 168 ? 13.135 7.724 -21.870 1.00 15.73 ? 168 SER A N 1 ATOM 1276 C CA . SER A 1 168 ? 13.813 6.489 -21.495 1.00 16.28 ? 168 SER A CA 1 ATOM 1277 C C . SER A 1 168 ? 13.030 5.247 -21.911 1.00 18.42 ? 168 SER A C 1 ATOM 1278 O O . SER A 1 168 ? 13.592 4.154 -22.000 1.00 32.81 ? 168 SER A O 1 ATOM 1279 C CB . SER A 1 168 ? 14.070 6.463 -19.987 1.00 17.46 ? 168 SER A CB 1 ATOM 1280 O OG . SER A 1 168 ? 14.936 7.517 -19.604 1.00 29.42 ? 168 SER A OG 1 ATOM 1281 N N . LYS A 1 169 ? 11.737 5.414 -22.168 1.00 18.65 ? 169 LYS A N 1 ATOM 1282 C CA . LYS A 1 169 ? 10.893 4.290 -22.561 1.00 20.29 ? 169 LYS A CA 1 ATOM 1283 C C . LYS A 1 169 ? 10.776 4.138 -24.076 1.00 23.13 ? 169 LYS A C 1 ATOM 1284 O O . LYS A 1 169 ? 11.155 3.106 -24.631 1.00 12.89 ? 169 LYS A O 1 ATOM 1285 C CB . LYS A 1 169 ? 9.496 4.428 -21.954 1.00 26.07 ? 169 LYS A CB 1 ATOM 1286 C CG . LYS A 1 169 ? 9.408 4.038 -20.488 1.00 26.85 ? 169 LYS A CG 1 ATOM 1287 C CD . LYS A 1 169 ? 7.961 4.003 -20.025 1.00 51.74 ? 169 LYS A CD 1 ATOM 1288 C CE . LYS A 1 169 ? 7.753 4.870 -18.795 1.00 65.52 ? 169 LYS A CE 1 ATOM 1289 N NZ . LYS A 1 169 ? 6.324 4.908 -18.376 1.00 38.67 ? 169 LYS A NZ 1 ATOM 1290 N N . ASP A 1 170 ? 10.248 5.159 -24.744 1.00 17.24 ? 170 ASP A N 1 ATOM 1291 C CA . ASP A 1 170 ? 9.962 5.059 -26.173 1.00 16.85 ? 170 ASP A CA 1 ATOM 1292 C C . ASP A 1 170 ? 10.994 5.773 -27.045 1.00 18.76 ? 170 ASP A C 1 ATOM 1293 O O . ASP A 1 170 ? 10.863 5.796 -28.268 1.00 34.05 ? 170 ASP A O 1 ATOM 1294 C CB . ASP A 1 170 ? 8.558 5.600 -26.470 1.00 17.62 ? 170 ASP A CB 1 ATOM 1295 C CG . ASP A 1 170 ? 8.307 6.963 -25.850 1.00 21.81 ? 170 ASP A CG 1 ATOM 1296 O OD1 . ASP A 1 170 ? 9.206 7.826 -25.906 1.00 30.32 ? 170 ASP A OD1 1 ATOM 1297 O OD2 . ASP A 1 170 ? 7.203 7.171 -25.304 1.00 33.67 ? 170 ASP A OD2 1 ATOM 1298 N N . SER A 1 171 ? 12.010 6.352 -26.410 1.00 15.60 ? 171 SER A N 1 ATOM 1299 C CA . SER A 1 171 ? 13.119 6.995 -27.118 1.00 20.48 ? 171 SER A CA 1 ATOM 1300 C C . SER A 1 171 ? 12.683 8.113 -28.064 1.00 12.93 ? 171 SER A C 1 ATOM 1301 O O . SER A 1 171 ? 13.294 8.316 -29.113 1.00 11.11 ? 171 SER A O 1 ATOM 1302 C CB . SER A 1 171 ? 13.920 5.949 -27.902 1.00 12.64 ? 171 SER A CB 1 ATOM 1303 O OG . SER A 1 171 ? 14.466 4.971 -27.037 1.00 27.63 ? 171 SER A OG 1 ATOM 1304 N N . THR A 1 172 ? 11.637 8.843 -27.691 1.00 14.89 ? 172 THR A N 1 ATOM 1305 C CA . THR A 1 172 ? 11.156 9.950 -28.513 1.00 10.27 ? 172 THR A CA 1 ATOM 1306 C C . THR A 1 172 ? 11.518 11.299 -27.902 1.00 10.70 ? 172 THR A C 1 ATOM 1307 O O . THR A 1 172 ? 11.993 11.370 -26.769 1.00 18.34 ? 172 THR A O 1 ATOM 1308 C CB . THR A 1 172 ? 9.633 9.890 -28.708 1.00 11.80 ? 172 THR A CB 1 ATOM 1309 O OG1 . THR A 1 172 ? 8.980 10.099 -27.450 1.00 17.25 ? 172 THR A OG1 1 ATOM 1310 C CG2 . THR A 1 172 ? 9.221 8.543 -29.272 1.00 13.73 ? 172 THR A CG2 1 ATOM 1311 N N . TYR A 1 173 ? 11.290 12.365 -28.662 1.00 10.11 ? 173 TYR A N 1 ATOM 1312 C CA . TYR A 1 173 ? 11.506 13.721 -28.175 1.00 6.87 ? 173 TYR A CA 1 ATOM 1313 C C . TYR A 1 173 ? 10.199 14.504 -28.175 1.00 13.35 ? 173 TYR A C 1 ATOM 1314 O O . TYR A 1 173 ? 9.205 14.067 -28.752 1.00 12.06 ? 173 TYR A O 1 ATOM 1315 C CB . TYR A 1 173 ? 12.542 14.453 -29.030 1.00 7.24 ? 173 TYR A CB 1 ATOM 1316 C CG . TYR A 1 173 ? 13.923 13.841 -29.008 1.00 10.19 ? 173 TYR A CG 1 ATOM 1317 C CD1 . TYR A 1 173 ? 14.290 12.876 -29.936 1.00 10.43 ? 173 TYR A CD1 1 ATOM 1318 C CD2 . TYR A 1 173 ? 14.865 14.240 -28.070 1.00 9.91 ? 173 TYR A CD2 1 ATOM 1319 C CE1 . TYR A 1 173 ? 15.554 12.318 -29.925 1.00 11.86 ? 173 TYR A CE1 1 ATOM 1320 C CE2 . TYR A 1 173 ? 16.132 13.688 -28.050 1.00 11.99 ? 173 TYR A CE2 1 ATOM 1321 C CZ . TYR A 1 173 ? 16.471 12.727 -28.981 1.00 16.40 ? 173 TYR A CZ 1 ATOM 1322 O OH . TYR A 1 173 ? 17.731 12.174 -28.967 1.00 11.82 ? 173 TYR A OH 1 ATOM 1323 N N . SER A 1 174 ? 10.211 15.665 -27.531 1.00 15.23 ? 174 SER A N 1 ATOM 1324 C CA . SER A 1 174 ? 9.058 16.556 -27.532 1.00 5.95 ? 174 SER A CA 1 ATOM 1325 C C . SER A 1 174 ? 9.513 18.009 -27.599 1.00 7.04 ? 174 SER A C 1 ATOM 1326 O O . SER A 1 174 ? 10.473 18.396 -26.934 1.00 9.85 ? 174 SER A O 1 ATOM 1327 C CB . SER A 1 174 ? 8.193 16.323 -26.293 1.00 8.18 ? 174 SER A CB 1 ATOM 1328 O OG . SER A 1 174 ? 7.607 15.033 -26.324 1.00 20.50 ? 174 SER A OG 1 ATOM 1329 N N . LEU A 1 175 ? 8.825 18.808 -28.408 1.00 10.23 ? 175 LEU A N 1 ATOM 1330 C CA . LEU A 1 175 ? 9.214 20.198 -28.625 1.00 7.67 ? 175 LEU A CA 1 ATOM 1331 C C . LEU A 1 175 ? 8.043 21.136 -28.361 1.00 7.05 ? 175 LEU A C 1 ATOM 1332 O O . LEU A 1 175 ? 6.887 20.769 -28.568 1.00 6.25 ? 175 LEU A O 1 ATOM 1333 C CB . LEU A 1 175 ? 9.740 20.385 -30.055 1.00 7.35 ? 175 LEU A CB 1 ATOM 1334 C CG . LEU A 1 175 ? 10.361 21.723 -30.468 1.00 7.80 ? 175 LEU A CG 1 ATOM 1335 C CD1 . LEU A 1 175 ? 11.461 21.494 -31.486 1.00 9.26 ? 175 LEU A CD1 1 ATOM 1336 C CD2 . LEU A 1 175 ? 9.319 22.668 -31.044 1.00 11.66 ? 175 LEU A CD2 1 ATOM 1337 N N . SER A 1 176 ? 8.351 22.344 -27.900 1.00 9.18 ? 176 SER A N 1 ATOM 1338 C CA . SER A 1 176 ? 7.334 23.367 -27.683 1.00 8.61 ? 176 SER A CA 1 ATOM 1339 C C . SER A 1 176 ? 7.816 24.727 -28.175 1.00 12.74 ? 176 SER A C 1 ATOM 1340 O O . SER A 1 176 ? 8.833 25.239 -27.708 1.00 17.23 ? 176 SER A O 1 ATOM 1341 C CB . SER A 1 176 ? 6.955 23.452 -26.202 1.00 17.66 ? 176 SER A CB 1 ATOM 1342 O OG . SER A 1 176 ? 8.023 23.969 -25.427 1.00 29.93 ? 176 SER A OG 1 ATOM 1343 N N . SER A 1 177 ? 7.083 25.306 -29.121 1.00 24.01 ? 177 SER A N 1 ATOM 1344 C CA . SER A 1 177 ? 7.400 26.634 -29.630 1.00 10.85 ? 177 SER A CA 1 ATOM 1345 C C . SER A 1 177 ? 6.478 27.675 -29.009 1.00 9.28 ? 177 SER A C 1 ATOM 1346 O O . SER A 1 177 ? 5.258 27.517 -29.021 1.00 15.53 ? 177 SER A O 1 ATOM 1347 C CB . SER A 1 177 ? 7.287 26.669 -31.155 1.00 11.02 ? 177 SER A CB 1 ATOM 1348 O OG . SER A 1 177 ? 7.507 27.977 -31.653 1.00 13.44 ? 177 SER A OG 1 ATOM 1349 N N . THR A 1 178 ? 7.063 28.737 -28.467 1.00 9.37 ? 178 THR A N 1 ATOM 1350 C CA . THR A 1 178 ? 6.282 29.784 -27.818 1.00 11.38 ? 178 THR A CA 1 ATOM 1351 C C . THR A 1 178 ? 6.399 31.117 -28.551 1.00 28.17 ? 178 THR A C 1 ATOM 1352 O O . THR A 1 178 ? 7.435 31.780 -28.497 1.00 19.04 ? 178 THR A O 1 ATOM 1353 C CB . THR A 1 178 ? 6.713 29.979 -26.353 1.00 11.69 ? 178 THR A CB 1 ATOM 1354 O OG1 . THR A 1 178 ? 6.587 28.739 -25.647 1.00 32.11 ? 178 THR A OG1 1 ATOM 1355 C CG2 . THR A 1 178 ? 5.848 31.031 -25.679 1.00 11.80 ? 178 THR A CG2 1 ATOM 1356 N N . LEU A 1 179 ? 5.326 31.500 -29.235 1.00 22.33 ? 179 LEU A N 1 ATOM 1357 C CA . LEU A 1 179 ? 5.271 32.775 -29.939 1.00 11.26 ? 179 LEU A CA 1 ATOM 1358 C C . LEU A 1 179 ? 4.860 33.885 -28.980 1.00 13.22 ? 179 LEU A C 1 ATOM 1359 O O . LEU A 1 179 ? 3.806 33.807 -28.347 1.00 20.59 ? 179 LEU A O 1 ATOM 1360 C CB . LEU A 1 179 ? 4.295 32.697 -31.114 1.00 11.36 ? 179 LEU A CB 1 ATOM 1361 C CG . LEU A 1 179 ? 4.256 33.896 -32.063 1.00 13.00 ? 179 LEU A CG 1 ATOM 1362 C CD1 . LEU A 1 179 ? 5.522 33.958 -32.905 1.00 12.14 ? 179 LEU A CD1 1 ATOM 1363 C CD2 . LEU A 1 179 ? 3.018 33.851 -32.945 1.00 11.47 ? 179 LEU A CD2 1 ATOM 1364 N N . THR A 1 180 ? 5.692 34.915 -28.869 1.00 11.99 ? 180 THR A N 1 ATOM 1365 C CA . THR A 1 180 ? 5.429 36.003 -27.933 1.00 15.71 ? 180 THR A CA 1 ATOM 1366 C C . THR A 1 180 ? 5.059 37.297 -28.651 1.00 16.81 ? 180 THR A C 1 ATOM 1367 O O . THR A 1 180 ? 5.888 37.903 -29.328 1.00 26.17 ? 180 THR A O 1 ATOM 1368 C CB . THR A 1 180 ? 6.643 36.267 -27.021 1.00 22.51 ? 180 THR A CB 1 ATOM 1369 O OG1 . THR A 1 180 ? 6.891 35.113 -26.207 1.00 19.67 ? 180 THR A OG1 1 ATOM 1370 C CG2 . THR A 1 180 ? 6.381 37.464 -26.119 1.00 22.56 ? 180 THR A CG2 1 ATOM 1371 N N . LEU A 1 181 ? 3.805 37.708 -28.495 1.00 18.74 ? 181 LEU A N 1 ATOM 1372 C CA . LEU A 1 181 ? 3.319 38.960 -29.063 1.00 20.23 ? 181 LEU A CA 1 ATOM 1373 C C . LEU A 1 181 ? 2.755 39.861 -27.972 1.00 22.05 ? 181 LEU A C 1 ATOM 1374 O O . LEU A 1 181 ? 2.278 39.377 -26.946 1.00 35.53 ? 181 LEU A O 1 ATOM 1375 C CB . LEU A 1 181 ? 2.245 38.698 -30.122 1.00 22.21 ? 181 LEU A CB 1 ATOM 1376 C CG . LEU A 1 181 ? 2.660 38.603 -31.592 1.00 36.22 ? 181 LEU A CG 1 ATOM 1377 C CD1 . LEU A 1 181 ? 3.637 37.464 -31.815 1.00 27.01 ? 181 LEU A CD1 1 ATOM 1378 C CD2 . LEU A 1 181 ? 1.433 38.440 -32.478 1.00 21.18 ? 181 LEU A CD2 1 ATOM 1379 N N . SER A 1 182 ? 2.811 41.170 -28.194 1.00 29.48 ? 182 SER A N 1 ATOM 1380 C CA . SER A 1 182 ? 2.165 42.113 -27.292 1.00 22.07 ? 182 SER A CA 1 ATOM 1381 C C . SER A 1 182 ? 0.656 41.996 -27.459 1.00 19.65 ? 182 SER A C 1 ATOM 1382 O O . SER A 1 182 ? 0.181 41.507 -28.484 1.00 22.11 ? 182 SER A O 1 ATOM 1383 C CB . SER A 1 182 ? 2.629 43.544 -27.566 1.00 21.28 ? 182 SER A CB 1 ATOM 1384 O OG . SER A 1 182 ? 2.251 43.961 -28.866 1.00 31.53 ? 182 SER A OG 1 ATOM 1385 N N . LYS A 1 183 ? -0.094 42.439 -26.454 1.00 21.66 ? 183 LYS A N 1 ATOM 1386 C CA . LYS A 1 183 ? -1.549 42.353 -26.500 1.00 23.17 ? 183 LYS A CA 1 ATOM 1387 C C . LYS A 1 183 ? -2.109 43.143 -27.679 1.00 26.52 ? 183 LYS A C 1 ATOM 1388 O O . LYS A 1 183 ? -3.087 42.734 -28.304 1.00 35.02 ? 183 LYS A O 1 ATOM 1389 C CB . LYS A 1 183 ? -2.164 42.860 -25.195 1.00 37.47 ? 183 LYS A CB 1 ATOM 1390 C CG . LYS A 1 183 ? -3.680 42.751 -25.153 1.00 24.88 ? 183 LYS A CG 1 ATOM 1391 C CD . LYS A 1 183 ? -4.275 43.599 -24.044 1.00 25.26 ? 183 LYS A CD 1 ATOM 1392 C CE . LYS A 1 183 ? -5.793 43.580 -24.102 1.00 27.29 ? 183 LYS A CE 1 ATOM 1393 N NZ . LYS A 1 183 ? -6.403 44.527 -23.129 1.00 36.50 ? 183 LYS A NZ 1 ATOM 1394 N N . ALA A 1 184 ? -1.476 44.274 -27.976 1.00 33.94 ? 184 ALA A N 1 ATOM 1395 C CA . ALA A 1 184 ? -1.899 45.130 -29.076 1.00 25.61 ? 184 ALA A CA 1 ATOM 1396 C C . ALA A 1 184 ? -1.826 44.395 -30.410 1.00 40.49 ? 184 ALA A C 1 ATOM 1397 O O . ALA A 1 184 ? -2.809 44.330 -31.147 1.00 45.79 ? 184 ALA A O 1 ATOM 1398 C CB . ALA A 1 184 ? -1.050 46.390 -29.120 1.00 17.13 ? 184 ALA A CB 1 ATOM 1399 N N . ASP A 1 185 ? -0.658 43.835 -30.709 1.00 30.08 ? 185 ASP A N 1 ATOM 1400 C CA . ASP A 1 185 ? -0.442 43.131 -31.969 1.00 32.48 ? 185 ASP A CA 1 ATOM 1401 C C . ASP A 1 185 ? -1.287 41.863 -32.065 1.00 28.91 ? 185 ASP A C 1 ATOM 1402 O O . ASP A 1 185 ? -1.650 41.433 -33.160 1.00 27.27 ? 185 ASP A O 1 ATOM 1403 C CB . ASP A 1 185 ? 1.039 42.785 -32.141 1.00 29.79 ? 185 ASP A CB 1 ATOM 1404 C CG . ASP A 1 185 ? 1.909 44.015 -32.311 1.00 39.71 ? 185 ASP A CG 1 ATOM 1405 O OD1 . ASP A 1 185 ? 1.408 45.030 -32.841 1.00 47.56 ? 185 ASP A OD1 1 ATOM 1406 O OD2 . ASP A 1 185 ? 3.093 43.967 -31.915 1.00 55.24 ? 185 ASP A OD2 1 ATOM 1407 N N . TYR A 1 186 ? -1.599 41.269 -30.918 1.00 26.60 ? 186 TYR A N 1 ATOM 1408 C CA . TYR A 1 186 ? -2.405 40.055 -30.889 1.00 25.67 ? 186 TYR A CA 1 ATOM 1409 C C . TYR A 1 186 ? -3.850 40.337 -31.287 1.00 37.39 ? 186 TYR A C 1 ATOM 1410 O O . TYR A 1 186 ? -4.453 39.579 -32.048 1.00 27.32 ? 186 TYR A O 1 ATOM 1411 C CB . TYR A 1 186 ? -2.361 39.407 -29.502 1.00 22.02 ? 186 TYR A CB 1 ATOM 1412 C CG . TYR A 1 186 ? -3.257 38.193 -29.368 1.00 19.05 ? 186 TYR A CG 1 ATOM 1413 C CD1 . TYR A 1 186 ? -2.889 36.971 -29.915 1.00 12.65 ? 186 TYR A CD1 1 ATOM 1414 C CD2 . TYR A 1 186 ? -4.470 38.269 -28.694 1.00 24.54 ? 186 TYR A CD2 1 ATOM 1415 C CE1 . TYR A 1 186 ? -3.703 35.861 -29.798 1.00 9.37 ? 186 TYR A CE1 1 ATOM 1416 C CE2 . TYR A 1 186 ? -5.290 37.163 -28.571 1.00 14.01 ? 186 TYR A CE2 1 ATOM 1417 C CZ . TYR A 1 186 ? -4.901 35.964 -29.125 1.00 7.97 ? 186 TYR A CZ 1 ATOM 1418 O OH . TYR A 1 186 ? -5.714 34.862 -29.004 1.00 9.95 ? 186 TYR A OH 1 ATOM 1419 N N . GLU A 1 187 ? -4.398 41.433 -30.772 1.00 56.67 ? 187 GLU A N 1 ATOM 1420 C CA . GLU A 1 187 ? -5.797 41.779 -31.003 1.00 42.60 ? 187 GLU A CA 1 ATOM 1421 C C . GLU A 1 187 ? -6.055 42.268 -32.426 1.00 30.32 ? 187 GLU A C 1 ATOM 1422 O O . GLU A 1 187 ? -7.192 42.256 -32.895 1.00 30.31 ? 187 GLU A O 1 ATOM 1423 C CB . GLU A 1 187 ? -6.251 42.846 -30.003 1.00 31.17 ? 187 GLU A CB 1 ATOM 1424 C CG . GLU A 1 187 ? -6.266 42.386 -28.552 1.00 28.59 ? 187 GLU A CG 1 ATOM 1425 C CD . GLU A 1 187 ? -7.366 41.382 -28.265 1.00 39.13 ? 187 GLU A CD 1 ATOM 1426 O OE1 . GLU A 1 187 ? -7.280 40.685 -27.233 1.00 28.49 ? 187 GLU A OE1 1 ATOM 1427 O OE2 . GLU A 1 187 ? -8.319 41.292 -29.066 1.00 49.53 ? 187 GLU A OE2 1 ATOM 1428 N N . LYS A 1 188 ? -4.998 42.699 -33.109 1.00 27.84 ? 188 LYS A N 1 ATOM 1429 C CA . LYS A 1 188 ? -5.131 43.242 -34.458 1.00 34.53 ? 188 LYS A CA 1 ATOM 1430 C C . LYS A 1 188 ? -5.355 42.152 -35.502 1.00 40.99 ? 188 LYS A C 1 ATOM 1431 O O . LYS A 1 188 ? -6.018 42.379 -36.513 1.00 63.62 ? 188 LYS A O 1 ATOM 1432 C CB . LYS A 1 188 ? -3.893 44.063 -34.828 1.00 27.06 ? 188 LYS A CB 1 ATOM 1433 C CG . LYS A 1 188 ? -3.768 45.382 -34.089 1.00 26.83 ? 188 LYS A CG 1 ATOM 1434 C CD . LYS A 1 188 ? -2.517 46.131 -34.516 1.00 34.29 ? 188 LYS A CD 1 ATOM 1435 C CE . LYS A 1 188 ? -2.381 47.452 -33.771 1.00 28.40 ? 188 LYS A CE 1 ATOM 1436 N NZ . LYS A 1 188 ? -1.124 48.163 -34.141 1.00 36.43 ? 188 LYS A NZ 1 ATOM 1437 N N . HIS A 1 189 ? -4.801 40.970 -35.255 1.00 28.46 ? 189 HIS A N 1 ATOM 1438 C CA . HIS A 1 189 ? -4.885 39.874 -36.215 1.00 28.30 ? 189 HIS A CA 1 ATOM 1439 C C . HIS A 1 189 ? -5.905 38.819 -35.800 1.00 32.89 ? 189 HIS A C 1 ATOM 1440 O O . HIS A 1 189 ? -6.402 38.828 -34.673 1.00 36.57 ? 189 HIS A O 1 ATOM 1441 C CB . HIS A 1 189 ? -3.512 39.232 -36.399 1.00 22.84 ? 189 HIS A CB 1 ATOM 1442 C CG . HIS A 1 189 ? -2.476 40.168 -36.941 1.00 25.77 ? 189 HIS A CG 1 ATOM 1443 N ND1 . HIS A 1 189 ? -2.241 40.315 -38.291 1.00 33.34 ? 189 HIS A ND1 1 ATOM 1444 C CD2 . HIS A 1 189 ? -1.612 41.003 -36.316 1.00 25.80 ? 189 HIS A CD2 1 ATOM 1445 C CE1 . HIS A 1 189 ? -1.277 41.200 -38.474 1.00 23.61 ? 189 HIS A CE1 1 ATOM 1446 N NE2 . HIS A 1 189 ? -0.879 41.633 -37.292 1.00 35.60 ? 189 HIS A NE2 1 ATOM 1447 N N . LYS A 1 190 ? -6.210 37.907 -36.718 1.00 24.75 ? 190 LYS A N 1 ATOM 1448 C CA . LYS A 1 190 ? -7.249 36.909 -36.490 1.00 25.39 ? 190 LYS A CA 1 ATOM 1449 C C . LYS A 1 190 ? -6.714 35.479 -36.483 1.00 41.25 ? 190 LYS A C 1 ATOM 1450 O O . LYS A 1 190 ? -6.960 34.721 -35.545 1.00 31.34 ? 190 LYS A O 1 ATOM 1451 C CB . LYS A 1 190 ? -8.341 37.036 -37.553 1.00 26.68 ? 190 LYS A CB 1 ATOM 1452 C CG . LYS A 1 190 ? -9.330 35.881 -37.562 1.00 40.27 ? 190 LYS A CG 1 ATOM 1453 C CD . LYS A 1 190 ? -10.148 35.862 -38.843 1.00 81.72 ? 190 LYS A CD 1 ATOM 1454 C CE . LYS A 1 190 ? -11.014 34.616 -38.927 1.00 55.83 ? 190 LYS A CE 1 ATOM 1455 N NZ . LYS A 1 190 ? -11.732 34.521 -40.230 1.00 37.06 ? 190 LYS A NZ 1 ATOM 1456 N N . VAL A 1 191 ? -5.987 35.116 -37.535 1.00 43.62 ? 191 VAL A N 1 ATOM 1457 C CA . VAL A 1 191 ? -5.551 33.736 -37.724 1.00 39.77 ? 191 VAL A CA 1 ATOM 1458 C C . VAL A 1 191 ? -4.143 33.481 -37.194 1.00 25.35 ? 191 VAL A C 1 ATOM 1459 O O . VAL A 1 191 ? -3.196 34.184 -37.548 1.00 18.09 ? 191 VAL A O 1 ATOM 1460 C CB . VAL A 1 191 ? -5.597 33.340 -39.212 1.00 25.22 ? 191 VAL A CB 1 ATOM 1461 C CG1 . VAL A 1 191 ? -5.245 31.871 -39.382 1.00 22.02 ? 191 VAL A CG1 1 ATOM 1462 C CG2 . VAL A 1 191 ? -6.972 33.630 -39.793 1.00 39.04 ? 191 VAL A CG2 1 ATOM 1463 N N . TYR A 1 192 ? -4.015 32.464 -36.346 1.00 21.00 ? 192 TYR A N 1 ATOM 1464 C CA . TYR A 1 192 ? -2.721 32.066 -35.801 1.00 14.71 ? 192 TYR A CA 1 ATOM 1465 C C . TYR A 1 192 ? -2.459 30.594 -36.084 1.00 13.48 ? 192 TYR A C 1 ATOM 1466 O O . TYR A 1 192 ? -3.080 29.718 -35.484 1.00 18.52 ? 192 TYR A O 1 ATOM 1467 C CB . TYR A 1 192 ? -2.663 32.339 -34.297 1.00 11.51 ? 192 TYR A CB 1 ATOM 1468 C CG . TYR A 1 192 ? -2.803 33.801 -33.949 1.00 11.84 ? 192 TYR A CG 1 ATOM 1469 C CD1 . TYR A 1 192 ? -4.053 34.366 -33.739 1.00 12.90 ? 192 TYR A CD1 1 ATOM 1470 C CD2 . TYR A 1 192 ? -1.686 34.618 -33.841 1.00 14.15 ? 192 TYR A CD2 1 ATOM 1471 C CE1 . TYR A 1 192 ? -4.187 35.702 -33.426 1.00 18.76 ? 192 TYR A CE1 1 ATOM 1472 C CE2 . TYR A 1 192 ? -1.811 35.956 -33.528 1.00 15.41 ? 192 TYR A CE2 1 ATOM 1473 C CZ . TYR A 1 192 ? -3.063 36.492 -33.322 1.00 16.14 ? 192 TYR A CZ 1 ATOM 1474 O OH . TYR A 1 192 ? -3.193 37.824 -33.011 1.00 28.93 ? 192 TYR A OH 1 ATOM 1475 N N . ALA A 1 193 ? -1.536 30.327 -37.002 1.00 20.20 ? 193 ALA A N 1 ATOM 1476 C CA . ALA A 1 193 ? -1.267 28.963 -37.441 1.00 13.90 ? 193 ALA A CA 1 ATOM 1477 C C . ALA A 1 193 ? 0.105 28.471 -36.996 1.00 15.22 ? 193 ALA A C 1 ATOM 1478 O O . ALA A 1 193 ? 1.059 29.244 -36.914 1.00 14.59 ? 193 ALA A O 1 ATOM 1479 C CB . ALA A 1 193 ? -1.392 28.867 -38.954 1.00 28.08 ? 193 ALA A CB 1 ATOM 1480 N N . CYS A 1 194 ? 0.192 27.175 -36.715 1.00 9.67 ? 194 CYS A N 1 ATOM 1481 C CA . CYS A 1 194 ? 1.456 26.544 -36.362 1.00 7.83 ? 194 CYS A CA 1 ATOM 1482 C C . CYS A 1 194 ? 1.772 25.438 -37.359 1.00 12.13 ? 194 CYS A C 1 ATOM 1483 O O . CYS A 1 194 ? 1.131 24.388 -37.352 1.00 15.24 ? 194 CYS A O 1 ATOM 1484 C CB . CYS A 1 194 ? 1.404 25.983 -34.940 1.00 11.40 ? 194 CYS A CB 1 ATOM 1485 S SG . CYS A 1 194 ? 2.985 25.358 -34.324 1.00 36.53 ? 194 CYS A SG 1 ATOM 1486 N N . GLU A 1 195 ? 2.757 25.679 -38.219 1.00 16.40 ? 195 GLU A N 1 ATOM 1487 C CA . GLU A 1 195 ? 3.106 24.729 -39.269 1.00 14.69 ? 195 GLU A CA 1 ATOM 1488 C C . GLU A 1 195 ? 4.317 23.889 -38.885 1.00 16.86 ? 195 GLU A C 1 ATOM 1489 O O . GLU A 1 195 ? 5.355 24.421 -38.491 1.00 24.21 ? 195 GLU A O 1 ATOM 1490 C CB . GLU A 1 195 ? 3.370 25.460 -40.585 1.00 21.99 ? 195 GLU A CB 1 ATOM 1491 C CG . GLU A 1 195 ? 3.737 24.543 -41.739 1.00 48.48 ? 195 GLU A CG 1 ATOM 1492 C CD . GLU A 1 195 ? 3.853 25.287 -43.054 1.00 25.61 ? 195 GLU A CD 1 ATOM 1493 O OE1 . GLU A 1 195 ? 4.517 24.769 -43.975 1.00 38.31 ? 195 GLU A OE1 1 ATOM 1494 O OE2 . GLU A 1 195 ? 3.276 26.388 -43.167 1.00 26.25 ? 195 GLU A OE2 1 ATOM 1495 N N . VAL A 1 196 ? 4.179 22.573 -39.012 1.00 14.74 ? 196 VAL A N 1 ATOM 1496 C CA . VAL A 1 196 ? 5.219 21.644 -38.586 1.00 20.70 ? 196 VAL A CA 1 ATOM 1497 C C . VAL A 1 196 ? 5.710 20.760 -39.731 1.00 20.56 ? 196 VAL A C 1 ATOM 1498 O O . VAL A 1 196 ? 4.913 20.141 -40.437 1.00 19.83 ? 196 VAL A O 1 ATOM 1499 C CB . VAL A 1 196 ? 4.717 20.741 -37.438 1.00 20.86 ? 196 VAL A CB 1 ATOM 1500 C CG1 . VAL A 1 196 ? 5.754 19.680 -37.099 1.00 12.91 ? 196 VAL A CG1 1 ATOM 1501 C CG2 . VAL A 1 196 ? 4.370 21.579 -36.214 1.00 11.33 ? 196 VAL A CG2 1 ATOM 1502 N N . THR A 1 197 ? 7.027 20.705 -39.906 1.00 12.57 ? 197 THR A N 1 ATOM 1503 C CA . THR A 1 197 ? 7.633 19.838 -40.910 1.00 12.43 ? 197 THR A CA 1 ATOM 1504 C C . THR A 1 197 ? 8.552 18.811 -40.252 1.00 10.70 ? 197 THR A C 1 ATOM 1505 O O . THR A 1 197 ? 9.468 19.169 -39.511 1.00 15.73 ? 197 THR A O 1 ATOM 1506 C CB . THR A 1 197 ? 8.431 20.646 -41.949 1.00 12.97 ? 197 THR A CB 1 ATOM 1507 O OG1 . THR A 1 197 ? 7.597 21.671 -42.504 1.00 16.25 ? 197 THR A OG1 1 ATOM 1508 C CG2 . THR A 1 197 ? 8.921 19.739 -43.064 1.00 12.56 ? 197 THR A CG2 1 ATOM 1509 N N . HIS A 1 198 ? 8.303 17.532 -40.469 1.00 10.03 ? 198 HIS A N 1 ATOM 1510 C CA . HIS A 1 198 ? 9.095 16.469 -39.869 1.00 9.58 ? 198 HIS A CA 1 ATOM 1511 C C . HIS A 1 198 ? 9.247 15.317 -40.856 1.00 11.94 ? 198 HIS A C 1 ATOM 1512 O O . HIS A 1 198 ? 8.444 15.163 -41.735 1.00 17.61 ? 198 HIS A O 1 ATOM 1513 C CB . HIS A 1 198 ? 8.435 16.003 -38.572 1.00 13.62 ? 198 HIS A CB 1 ATOM 1514 C CG . HIS A 1 198 ? 9.297 15.126 -37.721 1.00 13.64 ? 198 HIS A CG 1 ATOM 1515 N ND1 . HIS A 1 198 ? 9.135 13.765 -37.656 1.00 15.67 ? 198 HIS A ND1 1 ATOM 1516 C CD2 . HIS A 1 198 ? 10.323 15.419 -36.897 1.00 8.17 ? 198 HIS A CD2 1 ATOM 1517 C CE1 . HIS A 1 198 ? 10.030 13.258 -36.838 1.00 13.78 ? 198 HIS A CE1 1 ATOM 1518 N NE2 . HIS A 1 198 ? 10.765 14.241 -36.366 1.00 10.79 ? 198 HIS A NE2 1 ATOM 1519 N N . GLN A 1 199 ? 10.274 14.505 -40.705 1.00 7.20 ? 199 GLN A N 1 ATOM 1520 C CA . GLN A 1 199 ? 10.553 13.424 -41.630 1.00 11.53 ? 199 GLN A CA 1 ATOM 1521 C C . GLN A 1 199 ? 9.494 12.331 -41.591 1.00 14.71 ? 199 GLN A C 1 ATOM 1522 O O . GLN A 1 199 ? 9.441 11.480 -42.450 1.00 24.79 ? 199 GLN A O 1 ATOM 1523 C CB . GLN A 1 199 ? 11.924 12.827 -41.357 1.00 15.23 ? 199 GLN A CB 1 ATOM 1524 C CG . GLN A 1 199 ? 13.101 13.534 -42.011 1.00 12.21 ? 199 GLN A CG 1 ATOM 1525 C CD . GLN A 1 199 ? 14.440 12.986 -41.583 1.00 15.95 ? 199 GLN A CD 1 ATOM 1526 O OE1 . GLN A 1 199 ? 14.565 11.860 -41.173 1.00 10.94 ? 199 GLN A OE1 1 ATOM 1527 N NE2 . GLN A 1 199 ? 15.432 13.793 -41.667 1.00 26.08 ? 199 GLN A NE2 1 ATOM 1528 N N . GLY A 1 200 ? 8.686 12.325 -40.548 1.00 13.46 ? 200 GLY A N 1 ATOM 1529 C CA . GLY A 1 200 ? 7.630 11.351 -40.389 1.00 12.85 ? 200 GLY A CA 1 ATOM 1530 C C . GLY A 1 200 ? 6.303 11.776 -40.967 1.00 19.03 ? 200 GLY A C 1 ATOM 1531 O O . GLY A 1 200 ? 5.334 11.060 -40.880 1.00 13.54 ? 200 GLY A O 1 ATOM 1532 N N . LEU A 1 201 ? 6.253 12.958 -41.549 1.00 27.06 ? 201 LEU A N 1 ATOM 1533 C CA . LEU A 1 201 ? 5.029 13.464 -42.134 1.00 19.90 ? 201 LEU A CA 1 ATOM 1534 C C . LEU A 1 201 ? 5.168 13.665 -43.628 1.00 23.46 ? 201 LEU A C 1 ATOM 1535 O O . LEU A 1 201 ? 6.117 14.261 -44.070 1.00 42.54 ? 201 LEU A O 1 ATOM 1536 C CB . LEU A 1 201 ? 4.652 14.796 -41.501 1.00 30.56 ? 201 LEU A CB 1 ATOM 1537 C CG . LEU A 1 201 ? 4.679 14.993 -40.007 1.00 13.33 ? 201 LEU A CG 1 ATOM 1538 C CD1 . LEU A 1 201 ? 4.622 16.467 -39.753 1.00 13.81 ? 201 LEU A CD1 1 ATOM 1539 C CD2 . LEU A 1 201 ? 3.469 14.334 -39.421 1.00 15.26 ? 201 LEU A CD2 1 ATOM 1540 N N . SER A 1 202 ? 4.209 13.176 -44.398 1.00 24.07 ? 202 SER A N 1 ATOM 1541 C CA . SER A 1 202 ? 4.196 13.346 -45.842 1.00 25.25 ? 202 SER A CA 1 ATOM 1542 C C . SER A 1 202 ? 4.067 14.775 -46.291 1.00 29.38 ? 202 SER A C 1 ATOM 1543 O O . SER A 1 202 ? 4.679 15.173 -47.245 1.00 44.02 ? 202 SER A O 1 ATOM 1544 C CB . SER A 1 202 ? 3.083 12.539 -46.456 1.00 22.58 ? 202 SER A CB 1 ATOM 1545 O OG . SER A 1 202 ? 1.848 13.024 -46.007 1.00 37.72 ? 202 SER A OG 1 ATOM 1546 N N . SER A 1 203 ? 3.243 15.549 -45.618 1.00 39.58 ? 203 SER A N 1 ATOM 1547 C CA . SER A 1 203 ? 3.123 16.955 -45.929 1.00 29.57 ? 203 SER A CA 1 ATOM 1548 C C . SER A 1 203 ? 3.014 17.722 -44.654 1.00 25.63 ? 203 SER A C 1 ATOM 1549 O O . SER A 1 203 ? 2.564 17.193 -43.662 1.00 30.80 ? 203 SER A O 1 ATOM 1550 C CB . SER A 1 203 ? 1.908 17.215 -46.796 1.00 34.53 ? 203 SER A CB 1 ATOM 1551 O OG . SER A 1 203 ? 0.795 16.502 -46.318 1.00 71.30 ? 203 SER A OG 1 ATOM 1552 N N . PRO A 1 204 ? 3.423 19.059 -44.727 1.00 23.05 ? 204 PRO A N 1 ATOM 1553 C CA . PRO A 1 204 ? 3.429 19.740 -43.426 1.00 26.98 ? 204 PRO A CA 1 ATOM 1554 C C . PRO A 1 204 ? 2.084 19.782 -42.761 1.00 43.92 ? 204 PRO A C 1 ATOM 1555 O O . PRO A 1 204 ? 1.089 19.917 -43.439 1.00 68.10 ? 204 PRO A O 1 ATOM 1556 C CB . PRO A 1 204 ? 3.804 21.164 -43.782 1.00 23.38 ? 204 PRO A CB 1 ATOM 1557 C CG . PRO A 1 204 ? 4.729 21.008 -44.893 1.00 25.52 ? 204 PRO A CG 1 ATOM 1558 C CD . PRO A 1 204 ? 3.955 20.090 -45.744 1.00 28.32 ? 204 PRO A CD 1 ATOM 1559 N N . VAL A 1 205 ? 2.065 19.670 -41.442 1.00 27.67 ? 205 VAL A N 1 ATOM 1560 C CA . VAL A 1 205 ? 0.831 19.698 -40.679 1.00 25.15 ? 205 VAL A CA 1 ATOM 1561 C C . VAL A 1 205 ? 0.672 21.026 -39.952 1.00 20.42 ? 205 VAL A C 1 ATOM 1562 O O . VAL A 1 205 ? 1.595 21.525 -39.352 1.00 19.31 ? 205 VAL A O 1 ATOM 1563 C CB . VAL A 1 205 ? 0.731 18.477 -39.743 1.00 24.95 ? 205 VAL A CB 1 ATOM 1564 C CG1 . VAL A 1 205 ? -0.491 18.572 -38.866 1.00 53.76 ? 205 VAL A CG1 1 ATOM 1565 C CG2 . VAL A 1 205 ? 0.755 17.161 -40.493 1.00 31.81 ? 205 VAL A CG2 1 ATOM 1566 N N . THR A 1 206 ? -0.514 21.598 -40.051 1.00 20.08 ? 206 THR A N 1 ATOM 1567 C CA . THR A 1 206 ? -0.815 22.900 -39.494 1.00 15.96 ? 206 THR A CA 1 ATOM 1568 C C . THR A 1 206 ? -1.929 22.816 -38.488 1.00 15.94 ? 206 THR A C 1 ATOM 1569 O O . THR A 1 206 ? -2.936 22.208 -38.738 1.00 29.95 ? 206 THR A O 1 ATOM 1570 C CB . THR A 1 206 ? -1.253 23.875 -40.598 1.00 21.42 ? 206 THR A CB 1 ATOM 1571 O OG1 . THR A 1 206 ? -0.189 24.061 -41.530 1.00 16.75 ? 206 THR A OG1 1 ATOM 1572 C CG2 . THR A 1 206 ? -1.635 25.202 -40.024 1.00 13.32 ? 206 THR A CG2 1 ATOM 1573 N N . LYS A 1 207 ? -1.733 23.440 -37.342 1.00 13.81 ? 207 LYS A N 1 ATOM 1574 C CA . LYS A 1 207 ? -2.764 23.579 -36.338 1.00 12.98 ? 207 LYS A CA 1 ATOM 1575 C C . LYS A 1 207 ? -2.958 25.049 -36.206 1.00 11.23 ? 207 LYS A C 1 ATOM 1576 O O . LYS A 1 207 ? -2.020 25.777 -36.098 1.00 15.64 ? 207 LYS A O 1 ATOM 1577 C CB . LYS A 1 207 ? -2.312 23.009 -35.003 1.00 12.01 ? 207 LYS A CB 1 ATOM 1578 C CG . LYS A 1 207 ? -2.133 21.511 -34.980 1.00 12.14 ? 207 LYS A CG 1 ATOM 1579 C CD . LYS A 1 207 ? -3.417 20.773 -35.210 1.00 17.01 ? 207 LYS A CD 1 ATOM 1580 C CE . LYS A 1 207 ? -3.139 19.439 -35.847 1.00 23.44 ? 207 LYS A CE 1 ATOM 1581 N NZ . LYS A 1 207 ? -4.401 18.707 -36.086 1.00 50.19 ? 207 LYS A NZ 1 ATOM 1582 N N . SER A 1 208 ? -4.192 25.489 -36.254 1.00 12.19 ? 208 SER A N 1 ATOM 1583 C CA . SER A 1 208 ? -4.491 26.913 -36.193 1.00 11.89 ? 208 SER A CA 1 ATOM 1584 C C . SER A 1 208 ? -5.775 27.207 -35.430 1.00 12.06 ? 208 SER A C 1 ATOM 1585 O O . SER A 1 208 ? -6.624 26.333 -35.258 1.00 19.55 ? 208 SER A O 1 ATOM 1586 C CB . SER A 1 208 ? -4.588 27.491 -37.607 1.00 10.58 ? 208 SER A CB 1 ATOM 1587 O OG . SER A 1 208 ? -5.538 26.778 -38.380 1.00 22.28 ? 208 SER A OG 1 ATOM 1588 N N . PHE A 1 209 ? -5.904 28.448 -34.971 1.00 14.69 ? 209 PHE A N 1 ATOM 1589 C CA . PHE A 1 209 ? -7.111 28.901 -34.295 1.00 13.06 ? 209 PHE A CA 1 ATOM 1590 C C . PHE A 1 209 ? -7.420 30.343 -34.676 1.00 16.16 ? 209 PHE A C 1 ATOM 1591 O O . PHE A 1 209 ? -6.538 31.082 -35.115 1.00 16.17 ? 209 PHE A O 1 ATOM 1592 C CB . PHE A 1 209 ? -6.969 28.776 -32.775 1.00 12.22 ? 209 PHE A CB 1 ATOM 1593 C CG . PHE A 1 209 ? -5.950 29.710 -32.178 1.00 15.12 ? 209 PHE A CG 1 ATOM 1594 C CD1 . PHE A 1 209 ? -4.616 29.348 -32.110 1.00 20.19 ? 209 PHE A CD1 1 ATOM 1595 C CD2 . PHE A 1 209 ? -6.327 30.946 -31.676 1.00 23.05 ? 209 PHE A CD2 1 ATOM 1596 C CE1 . PHE A 1 209 ? -3.678 30.201 -31.561 1.00 11.21 ? 209 PHE A CE1 1 ATOM 1597 C CE2 . PHE A 1 209 ? -5.391 31.804 -31.126 1.00 11.48 ? 209 PHE A CE2 1 ATOM 1598 C CZ . PHE A 1 209 ? -4.066 31.429 -31.069 1.00 10.35 ? 209 PHE A CZ 1 ATOM 1599 N N . ASN A 1 210 ? -8.676 30.737 -34.504 1.00 19.38 ? 210 ASN A N 1 ATOM 1600 C CA . ASN A 1 210 ? -9.080 32.115 -34.741 1.00 21.28 ? 210 ASN A CA 1 ATOM 1601 C C . ASN A 1 210 ? -9.228 32.849 -33.416 1.00 25.38 ? 210 ASN A C 1 ATOM 1602 O O . ASN A 1 210 ? -9.844 32.333 -32.485 1.00 34.77 ? 210 ASN A O 1 ATOM 1603 C CB . ASN A 1 210 ? -10.385 32.161 -35.534 1.00 32.47 ? 210 ASN A CB 1 ATOM 1604 C CG . ASN A 1 210 ? -10.298 31.394 -36.841 1.00 27.65 ? 210 ASN A CG 1 ATOM 1605 O OD1 . ASN A 1 210 ? -9.287 31.449 -37.540 1.00 36.86 ? 210 ASN A OD1 1 ATOM 1606 N ND2 . ASN A 1 210 ? -11.358 30.666 -37.171 1.00 25.86 ? 210 ASN A ND2 1 ATOM 1607 N N . ARG A 1 211 ? -8.653 34.045 -33.331 1.00 37.48 ? 211 ARG A N 1 ATOM 1608 C CA . ARG A 1 211 ? -8.662 34.813 -32.090 1.00 25.32 ? 211 ARG A CA 1 ATOM 1609 C C . ARG A 1 211 ? -10.078 35.129 -31.623 1.00 32.36 ? 211 ARG A C 1 ATOM 1610 O O . ARG A 1 211 ? -10.860 35.741 -32.351 1.00 49.05 ? 211 ARG A O 1 ATOM 1611 C CB . ARG A 1 211 ? -7.873 36.112 -32.255 1.00 21.38 ? 211 ARG A CB 1 ATOM 1612 C CG . ARG A 1 211 ? -8.009 37.056 -31.072 1.00 27.66 ? 211 ARG A CG 1 ATOM 1613 C CD . ARG A 1 211 ? -7.342 38.394 -31.345 1.00 29.55 ? 211 ARG A CD 1 ATOM 1614 N NE . ARG A 1 211 ? -7.739 38.946 -32.636 1.00 51.13 ? 211 ARG A NE 1 ATOM 1615 C CZ . ARG A 1 211 ? -8.869 39.612 -32.850 1.00 34.25 ? 211 ARG A CZ 1 ATOM 1616 N NH1 . ARG A 1 211 ? -9.723 39.809 -31.855 1.00 45.79 ? 211 ARG A NH1 1 ATOM 1617 N NH2 . ARG A 1 211 ? -9.147 40.077 -34.060 1.00 50.88 ? 211 ARG A NH2 1 ATOM 1618 N N . GLY A 1 212 ? -10.399 34.707 -30.404 1.00 35.31 ? 212 GLY A N 1 ATOM 1619 C CA . GLY A 1 212 ? -11.712 34.942 -29.834 1.00 52.68 ? 212 GLY A CA 1 ATOM 1620 C C . GLY A 1 212 ? -12.798 34.143 -30.525 1.00 52.06 ? 212 GLY A C 1 ATOM 1621 O O . GLY A 1 212 ? -13.844 34.684 -30.884 1.00 75.26 ? 212 GLY A O 1 ATOM 1622 N N . GLU A 1 213 ? -12.550 32.851 -30.712 1.00 47.95 ? 213 GLU A N 1 ATOM 1623 C CA . GLU A 1 213 ? -13.504 31.980 -31.387 1.00 43.86 ? 213 GLU A CA 1 ATOM 1624 C C . GLU A 1 213 ? -14.076 30.945 -30.424 1.00 54.11 ? 213 GLU A C 1 ATOM 1625 O O . GLU A 1 213 ? -13.399 30.511 -29.491 1.00 46.14 ? 213 GLU A O 1 ATOM 1626 C CB . GLU A 1 213 ? -12.842 31.283 -32.577 1.00 38.97 ? 213 GLU A CB 1 ATOM 1627 C CG . GLU A 1 213 ? -13.788 30.941 -33.719 1.00 42.28 ? 213 GLU A CG 1 ATOM 1628 C CD . GLU A 1 213 ? -14.011 32.106 -34.671 1.00 66.97 ? 213 GLU A CD 1 ATOM 1629 O OE1 . GLU A 1 213 ? -14.348 31.853 -35.847 1.00 70.38 ? 213 GLU A OE1 1 ATOM 1630 O OE2 . GLU A 1 213 ? -13.850 33.272 -34.251 1.00 54.80 ? 213 GLU A OE2 1 ATOM 1631 N N . GLN B 2 1 ? 22.674 2.508 2.725 1.00 59.14 ? 1 GLN B N 1 ATOM 1632 C CA . GLN B 2 1 ? 21.835 3.642 2.360 1.00 40.78 ? 1 GLN B CA 1 ATOM 1633 C C . GLN B 2 1 ? 22.353 4.944 2.969 1.00 45.45 ? 1 GLN B C 1 ATOM 1634 O O . GLN B 2 1 ? 21.841 5.417 3.984 1.00 37.67 ? 1 GLN B O 1 ATOM 1635 C CB . GLN B 2 1 ? 20.387 3.392 2.788 1.00 45.70 ? 1 GLN B CB 1 ATOM 1636 C CG . GLN B 2 1 ? 19.696 2.265 2.033 1.00 70.45 ? 1 GLN B CG 1 ATOM 1637 C CD . GLN B 2 1 ? 18.290 2.005 2.539 1.00 84.65 ? 1 GLN B CD 1 ATOM 1638 O OE1 . GLN B 2 1 ? 17.967 2.300 3.690 1.00 86.81 ? 1 GLN B OE1 1 ATOM 1639 N NE2 . GLN B 2 1 ? 17.445 1.449 1.678 1.00 53.93 ? 1 GLN B NE2 1 ATOM 1640 N N . VAL B 2 2 ? 23.374 5.518 2.342 1.00 33.79 ? 2 VAL B N 1 ATOM 1641 C CA . VAL B 2 2 ? 23.936 6.786 2.795 1.00 30.11 ? 2 VAL B CA 1 ATOM 1642 C C . VAL B 2 2 ? 23.152 7.954 2.206 1.00 28.74 ? 2 VAL B C 1 ATOM 1643 O O . VAL B 2 2 ? 22.812 7.949 1.023 1.00 35.58 ? 2 VAL B O 1 ATOM 1644 C CB . VAL B 2 2 ? 25.420 6.917 2.406 1.00 24.68 ? 2 VAL B CB 1 ATOM 1645 C CG1 . VAL B 2 2 ? 26.037 8.143 3.063 1.00 25.46 ? 2 VAL B CG1 1 ATOM 1646 C CG2 . VAL B 2 2 ? 26.178 5.663 2.802 1.00 26.27 ? 2 VAL B CG2 1 ATOM 1647 N N . GLN B 2 3 ? 22.865 8.953 3.034 1.00 29.27 ? 3 GLN B N 1 ATOM 1648 C CA . GLN B 2 3 ? 22.096 10.108 2.590 1.00 26.57 ? 3 GLN B CA 1 ATOM 1649 C C . GLN B 2 3 ? 22.938 11.377 2.595 1.00 20.57 ? 3 GLN B C 1 ATOM 1650 O O . GLN B 2 3 ? 23.651 11.656 3.559 1.00 22.17 ? 3 GLN B O 1 ATOM 1651 C CB . GLN B 2 3 ? 20.863 10.299 3.474 1.00 58.55 ? 3 GLN B CB 1 ATOM 1652 C CG . GLN B 2 3 ? 20.003 9.055 3.622 1.00 82.33 ? 3 GLN B CG 1 ATOM 1653 C CD . GLN B 2 3 ? 18.803 9.279 4.523 1.00 84.38 ? 3 GLN B CD 1 ATOM 1654 O OE1 . GLN B 2 3 ? 18.644 8.610 5.545 1.00 52.24 ? 3 GLN B OE1 1 ATOM 1655 N NE2 . GLN B 2 3 ? 17.949 10.223 4.146 1.00 80.93 ? 3 GLN B NE2 1 ATOM 1656 N N . LEU B 2 4 ? 22.852 12.141 1.512 1.00 18.49 ? 4 LEU B N 1 ATOM 1657 C CA . LEU B 2 4 ? 23.548 13.418 1.426 1.00 17.81 ? 4 LEU B CA 1 ATOM 1658 C C . LEU B 2 4 ? 22.570 14.557 1.161 1.00 17.41 ? 4 LEU B C 1 ATOM 1659 O O . LEU B 2 4 ? 21.885 14.580 0.139 1.00 22.42 ? 4 LEU B O 1 ATOM 1660 C CB . LEU B 2 4 ? 24.623 13.380 0.337 1.00 16.96 ? 4 LEU B CB 1 ATOM 1661 C CG . LEU B 2 4 ? 25.991 12.815 0.733 1.00 15.76 ? 4 LEU B CG 1 ATOM 1662 C CD1 . LEU B 2 4 ? 25.956 11.299 0.859 1.00 31.46 ? 4 LEU B CD1 1 ATOM 1663 C CD2 . LEU B 2 4 ? 27.059 13.249 -0.257 1.00 18.82 ? 4 LEU B CD2 1 ATOM 1664 N N . GLN B 2 5 ? 22.512 15.497 2.097 1.00 14.50 ? 5 GLN B N 1 ATOM 1665 C CA . GLN B 2 5 ? 21.642 16.660 1.978 1.00 14.47 ? 5 GLN B CA 1 ATOM 1666 C C . GLN B 2 5 ? 22.473 17.936 1.985 1.00 15.51 ? 5 GLN B C 1 ATOM 1667 O O . GLN B 2 5 ? 23.349 18.105 2.833 1.00 26.74 ? 5 GLN B O 1 ATOM 1668 C CB . GLN B 2 5 ? 20.619 16.679 3.116 1.00 24.08 ? 5 GLN B CB 1 ATOM 1669 C CG . GLN B 2 5 ? 19.871 17.993 3.268 1.00 50.82 ? 5 GLN B CG 1 ATOM 1670 C CD . GLN B 2 5 ? 19.026 18.037 4.529 1.00 54.80 ? 5 GLN B CD 1 ATOM 1671 O OE1 . GLN B 2 5 ? 18.756 17.006 5.146 1.00 41.98 ? 5 GLN B OE1 1 ATOM 1672 N NE2 . GLN B 2 5 ? 18.610 19.236 4.921 1.00 27.36 ? 5 GLN B NE2 1 ATOM 1673 N N . GLN B 2 6 ? 22.204 18.829 1.038 1.00 18.09 ? 6 GLN B N 1 ATOM 1674 C CA . GLN B 2 6 ? 22.958 20.073 0.942 1.00 18.53 ? 6 GLN B CA 1 ATOM 1675 C C . GLN B 2 6 ? 22.055 21.293 0.799 1.00 25.69 ? 6 GLN B C 1 ATOM 1676 O O . GLN B 2 6 ? 20.882 21.177 0.445 1.00 27.04 ? 6 GLN B O 1 ATOM 1677 C CB . GLN B 2 6 ? 23.938 20.013 -0.231 1.00 18.82 ? 6 GLN B CB 1 ATOM 1678 C CG . GLN B 2 6 ? 23.312 19.601 -1.549 1.00 18.21 ? 6 GLN B CG 1 ATOM 1679 C CD . GLN B 2 6 ? 24.285 19.698 -2.705 1.00 18.22 ? 6 GLN B CD 1 ATOM 1680 O OE1 . GLN B 2 6 ? 24.512 18.725 -3.423 1.00 26.43 ? 6 GLN B OE1 1 ATOM 1681 N NE2 . GLN B 2 6 ? 24.864 20.878 -2.895 1.00 22.92 ? 6 GLN B NE2 1 ATOM 1682 N N . TRP B 2 7 ? 22.619 22.464 1.076 1.00 17.23 ? 7 TRP B N 1 ATOM 1683 C CA . TRP B 2 7 ? 21.878 23.717 1.016 1.00 16.21 ? 7 TRP B CA 1 ATOM 1684 C C . TRP B 2 7 ? 22.821 24.889 0.773 1.00 19.29 ? 7 TRP B C 1 ATOM 1685 O O . TRP B 2 7 ? 24.039 24.715 0.724 1.00 17.67 ? 7 TRP B O 1 ATOM 1686 C CB . TRP B 2 7 ? 21.091 23.937 2.307 1.00 16.83 ? 7 TRP B CB 1 ATOM 1687 C CG . TRP B 2 7 ? 21.952 23.941 3.530 1.00 18.49 ? 7 TRP B CG 1 ATOM 1688 C CD1 . TRP B 2 7 ? 22.551 25.022 4.107 1.00 21.33 ? 7 TRP B CD1 1 ATOM 1689 C CD2 . TRP B 2 7 ? 22.319 22.807 4.324 1.00 19.59 ? 7 TRP B CD2 1 ATOM 1690 N NE1 . TRP B 2 7 ? 23.265 24.633 5.214 1.00 18.74 ? 7 TRP B NE1 1 ATOM 1691 C CE2 . TRP B 2 7 ? 23.138 23.278 5.369 1.00 24.59 ? 7 TRP B CE2 1 ATOM 1692 C CE3 . TRP B 2 7 ? 22.030 21.441 4.256 1.00 27.05 ? 7 TRP B CE3 1 ATOM 1693 C CZ2 . TRP B 2 7 ? 23.672 22.431 6.337 1.00 19.70 ? 7 TRP B CZ2 1 ATOM 1694 C CZ3 . TRP B 2 7 ? 22.563 20.602 5.218 1.00 20.02 ? 7 TRP B CZ3 1 ATOM 1695 C CH2 . TRP B 2 7 ? 23.375 21.100 6.244 1.00 20.25 ? 7 TRP B CH2 1 ATOM 1696 N N . GLY B 2 8 ? 22.284 26.078 0.630 1.00 19.21 ? 8 GLY B N 1 ATOM 1697 C CA . GLY B 2 8 ? 23.125 27.216 0.362 1.00 18.83 ? 8 GLY B CA 1 ATOM 1698 C C . GLY B 2 8 ? 22.316 28.201 -0.411 1.00 20.72 ? 8 GLY B C 1 ATOM 1699 O O . GLY B 2 8 ? 21.155 27.979 -0.616 1.00 43.46 ? 8 GLY B O 1 ATOM 1700 N N . ALA B 2 9 ? 22.934 29.277 -0.850 1.00 21.26 ? 9 ALA B N 1 ATOM 1701 C CA . ALA B 2 9 ? 22.247 30.274 -1.623 1.00 22.42 ? 9 ALA B CA 1 ATOM 1702 C C . ALA B 2 9 ? 22.504 30.052 -3.084 1.00 35.72 ? 9 ALA B C 1 ATOM 1703 O O . ALA B 2 9 ? 23.623 29.977 -3.491 1.00 78.58 ? 9 ALA B O 1 ATOM 1704 C CB . ALA B 2 9 ? 22.749 31.639 -1.235 1.00 21.61 ? 9 ALA B CB 1 ATOM 1705 N N . GLY B 2 10 ? 21.456 29.955 -3.877 1.00 18.11 ? 10 GLY B N 1 ATOM 1706 C CA . GLY B 2 10 ? 21.607 29.764 -5.295 1.00 16.33 ? 10 GLY B CA 1 ATOM 1707 C C . GLY B 2 10 ? 21.694 30.998 -6.156 1.00 16.33 ? 10 GLY B C 1 ATOM 1708 O O . GLY B 2 10 ? 21.902 30.895 -7.341 1.00 15.57 ? 10 GLY B O 1 ATOM 1709 N N . LEU B 2 11 ? 21.510 32.162 -5.561 1.00 17.06 ? 11 LEU B N 1 ATOM 1710 C CA . LEU B 2 11 ? 21.609 33.408 -6.284 1.00 12.72 ? 11 LEU B CA 1 ATOM 1711 C C . LEU B 2 11 ? 22.593 34.293 -5.590 1.00 16.85 ? 11 LEU B C 1 ATOM 1712 O O . LEU B 2 11 ? 22.440 34.550 -4.429 1.00 16.47 ? 11 LEU B O 1 ATOM 1713 C CB . LEU B 2 11 ? 20.261 34.093 -6.301 1.00 12.20 ? 11 LEU B CB 1 ATOM 1714 C CG . LEU B 2 11 ? 20.145 35.455 -6.949 1.00 13.01 ? 11 LEU B CG 1 ATOM 1715 C CD1 . LEU B 2 11 ? 20.473 35.328 -8.420 1.00 9.67 ? 11 LEU B CD1 1 ATOM 1716 C CD2 . LEU B 2 11 ? 18.759 36.015 -6.755 1.00 14.64 ? 11 LEU B CD2 1 ATOM 1717 N N . LEU B 2 12 ? 23.588 34.763 -6.334 1.00 20.42 ? 12 LEU B N 1 ATOM 1718 C CA . LEU B 2 12 ? 24.612 35.686 -5.868 1.00 18.06 ? 12 LEU B CA 1 ATOM 1719 C C . LEU B 2 12 ? 24.843 36.806 -6.868 1.00 29.24 ? 12 LEU B C 1 ATOM 1720 O O . LEU B 2 12 ? 24.681 36.619 -8.073 1.00 55.67 ? 12 LEU B O 1 ATOM 1721 C CB . LEU B 2 12 ? 25.929 34.953 -5.625 1.00 18.82 ? 12 LEU B CB 1 ATOM 1722 C CG . LEU B 2 12 ? 25.909 33.682 -4.785 1.00 23.18 ? 12 LEU B CG 1 ATOM 1723 C CD1 . LEU B 2 12 ? 27.229 32.970 -4.956 1.00 27.29 ? 12 LEU B CD1 1 ATOM 1724 C CD2 . LEU B 2 12 ? 25.655 34.005 -3.323 1.00 42.52 ? 12 LEU B CD2 1 ATOM 1725 N N . LYS B 2 13 ? 25.229 37.969 -6.359 1.00 30.32 ? 13 LYS B N 1 ATOM 1726 C CA . LYS B 2 13 ? 25.689 39.056 -7.206 1.00 20.16 ? 13 LYS B CA 1 ATOM 1727 C C . LYS B 2 13 ? 27.158 38.805 -7.521 1.00 21.33 ? 13 LYS B C 1 ATOM 1728 O O . LYS B 2 13 ? 27.832 38.098 -6.773 1.00 22.72 ? 13 LYS B O 1 ATOM 1729 C CB . LYS B 2 13 ? 25.493 40.406 -6.514 1.00 22.28 ? 13 LYS B CB 1 ATOM 1730 C CG . LYS B 2 13 ? 24.064 40.666 -6.063 1.00 19.56 ? 13 LYS B CG 1 ATOM 1731 C CD . LYS B 2 13 ? 23.964 41.946 -5.250 1.00 21.92 ? 13 LYS B CD 1 ATOM 1732 C CE . LYS B 2 13 ? 22.546 42.176 -4.750 1.00 35.71 ? 13 LYS B CE 1 ATOM 1733 N NZ . LYS B 2 13 ? 21.579 42.351 -5.869 1.00 25.84 ? 13 LYS B NZ 1 ATOM 1734 N N . PRO B 2 14 ? 27.658 39.358 -8.637 1.00 21.37 ? 14 PRO B N 1 ATOM 1735 C CA . PRO B 2 14 ? 29.082 39.203 -8.955 1.00 19.04 ? 14 PRO B CA 1 ATOM 1736 C C . PRO B 2 14 ? 29.989 39.758 -7.859 1.00 24.12 ? 14 PRO B C 1 ATOM 1737 O O . PRO B 2 14 ? 29.542 40.576 -7.053 1.00 24.30 ? 14 PRO B O 1 ATOM 1738 C CB . PRO B 2 14 ? 29.238 40.003 -10.250 1.00 18.85 ? 14 PRO B CB 1 ATOM 1739 C CG . PRO B 2 14 ? 27.889 39.956 -10.875 1.00 19.19 ? 14 PRO B CG 1 ATOM 1740 C CD . PRO B 2 14 ? 26.917 40.009 -9.732 1.00 27.21 ? 14 PRO B CD 1 ATOM 1741 N N . SER B 2 15 ? 31.237 39.292 -7.831 1.00 39.28 ? 15 SER B N 1 ATOM 1742 C CA . SER B 2 15 ? 32.247 39.703 -6.849 1.00 48.24 ? 15 SER B CA 1 ATOM 1743 C C . SER B 2 15 ? 31.914 39.273 -5.419 1.00 27.86 ? 15 SER B C 1 ATOM 1744 O O . SER B 2 15 ? 32.661 39.579 -4.490 1.00 26.42 ? 15 SER B O 1 ATOM 1745 C CB . SER B 2 15 ? 32.461 41.221 -6.887 1.00 67.49 ? 15 SER B CB 1 ATOM 1746 O OG . SER B 2 15 ? 31.386 41.907 -6.268 1.00 38.12 ? 15 SER B OG 1 ATOM 1747 N N . GLU B 2 16 ? 30.803 38.565 -5.240 1.00 24.05 ? 16 GLU B N 1 ATOM 1748 C CA . GLU B 2 16 ? 30.441 38.048 -3.925 1.00 22.42 ? 16 GLU B CA 1 ATOM 1749 C C . GLU B 2 16 ? 31.089 36.690 -3.694 1.00 24.03 ? 16 GLU B C 1 ATOM 1750 O O . GLU B 2 16 ? 31.858 36.212 -4.528 1.00 38.24 ? 16 GLU B O 1 ATOM 1751 C CB . GLU B 2 16 ? 28.923 37.944 -3.774 1.00 21.78 ? 16 GLU B CB 1 ATOM 1752 C CG . GLU B 2 16 ? 28.207 39.284 -3.753 1.00 23.06 ? 16 GLU B CG 1 ATOM 1753 C CD . GLU B 2 16 ? 26.747 39.160 -3.357 1.00 28.44 ? 16 GLU B CD 1 ATOM 1754 O OE1 . GLU B 2 16 ? 26.271 38.018 -3.180 1.00 21.22 ? 16 GLU B OE1 1 ATOM 1755 O OE2 . GLU B 2 16 ? 26.076 40.204 -3.219 1.00 36.84 ? 16 GLU B OE2 1 ATOM 1756 N N . THR B 2 17 ? 30.780 36.071 -2.559 1.00 22.07 ? 17 THR B N 1 ATOM 1757 C CA . THR B 2 17 ? 31.384 34.792 -2.207 1.00 22.87 ? 17 THR B CA 1 ATOM 1758 C C . THR B 2 17 ? 30.337 33.694 -2.043 1.00 19.88 ? 17 THR B C 1 ATOM 1759 O O . THR B 2 17 ? 29.391 33.829 -1.267 1.00 17.39 ? 17 THR B O 1 ATOM 1760 C CB . THR B 2 17 ? 32.208 34.901 -0.911 1.00 30.40 ? 17 THR B CB 1 ATOM 1761 O OG1 . THR B 2 17 ? 31.341 35.212 0.186 1.00 56.91 ? 17 THR B OG1 1 ATOM 1762 C CG2 . THR B 2 17 ? 33.264 35.990 -1.043 1.00 21.65 ? 17 THR B CG2 1 ATOM 1763 N N . LEU B 2 18 ? 30.523 32.605 -2.782 1.00 23.89 ? 18 LEU B N 1 ATOM 1764 C CA . LEU B 2 18 ? 29.607 31.472 -2.749 1.00 20.62 ? 18 LEU B CA 1 ATOM 1765 C C . LEU B 2 18 ? 29.835 30.631 -1.499 1.00 20.44 ? 18 LEU B C 1 ATOM 1766 O O . LEU B 2 18 ? 30.972 30.322 -1.154 1.00 21.03 ? 18 LEU B O 1 ATOM 1767 C CB . LEU B 2 18 ? 29.778 30.625 -4.017 1.00 29.99 ? 18 LEU B CB 1 ATOM 1768 C CG . LEU B 2 18 ? 28.916 29.388 -4.297 1.00 17.75 ? 18 LEU B CG 1 ATOM 1769 C CD1 . LEU B 2 18 ? 29.560 28.130 -3.730 1.00 16.67 ? 18 LEU B CD1 1 ATOM 1770 C CD2 . LEU B 2 18 ? 27.495 29.554 -3.772 1.00 33.98 ? 18 LEU B CD2 1 ATOM 1771 N N . SER B 2 19 ? 28.750 30.265 -0.824 1.00 27.91 ? 19 SER B N 1 ATOM 1772 C CA . SER B 2 19 ? 28.837 29.416 0.357 1.00 23.11 ? 19 SER B CA 1 ATOM 1773 C C . SER B 2 19 ? 27.819 28.282 0.301 1.00 25.14 ? 19 SER B C 1 ATOM 1774 O O . SER B 2 19 ? 26.617 28.519 0.183 1.00 29.64 ? 19 SER B O 1 ATOM 1775 C CB . SER B 2 19 ? 28.632 30.240 1.628 1.00 24.59 ? 19 SER B CB 1 ATOM 1776 O OG . SER B 2 19 ? 28.674 29.413 2.777 1.00 46.07 ? 19 SER B OG 1 ATOM 1777 N N . LEU B 2 20 ? 28.310 27.049 0.382 1.00 21.49 ? 20 LEU B N 1 ATOM 1778 C CA . LEU B 2 20 ? 27.450 25.871 0.366 1.00 18.11 ? 20 LEU B CA 1 ATOM 1779 C C . LEU B 2 20 ? 27.868 24.887 1.453 1.00 20.88 ? 20 LEU B C 1 ATOM 1780 O O . LEU B 2 20 ? 29.033 24.844 1.844 1.00 28.00 ? 20 LEU B O 1 ATOM 1781 C CB . LEU B 2 20 ? 27.491 25.190 -1.003 1.00 17.84 ? 20 LEU B CB 1 ATOM 1782 C CG . LEU B 2 20 ? 27.018 26.020 -2.198 1.00 25.64 ? 20 LEU B CG 1 ATOM 1783 C CD1 . LEU B 2 20 ? 27.277 25.279 -3.493 1.00 13.76 ? 20 LEU B CD1 1 ATOM 1784 C CD2 . LEU B 2 20 ? 25.545 26.370 -2.072 1.00 26.44 ? 20 LEU B CD2 1 ATOM 1785 N N . THR B 2 21 ? 26.914 24.100 1.937 1.00 17.14 ? 21 THR B N 1 ATOM 1786 C CA . THR B 2 21 ? 27.193 23.116 2.977 1.00 16.56 ? 21 THR B CA 1 ATOM 1787 C C . THR B 2 21 ? 26.509 21.787 2.676 1.00 16.20 ? 21 THR B C 1 ATOM 1788 O O . THR B 2 21 ? 25.331 21.752 2.323 1.00 22.37 ? 21 THR B O 1 ATOM 1789 C CB . THR B 2 21 ? 26.741 23.616 4.364 1.00 17.73 ? 21 THR B CB 1 ATOM 1790 O OG1 . THR B 2 21 ? 27.348 24.884 4.640 1.00 16.96 ? 21 THR B OG1 1 ATOM 1791 C CG2 . THR B 2 21 ? 27.138 22.625 5.447 1.00 22.40 ? 21 THR B CG2 1 ATOM 1792 N N . CYS B 2 22 ? 27.258 20.698 2.815 1.00 15.73 ? 22 CYS B N 1 ATOM 1793 C CA . CYS B 2 22 ? 26.722 19.357 2.609 1.00 18.36 ? 22 CYS B CA 1 ATOM 1794 C C . CYS B 2 22 ? 26.634 18.619 3.941 1.00 25.71 ? 22 CYS B C 1 ATOM 1795 O O . CYS B 2 22 ? 27.437 18.860 4.841 1.00 16.55 ? 22 CYS B O 1 ATOM 1796 C CB . CYS B 2 22 ? 27.592 18.581 1.620 1.00 26.94 ? 22 CYS B CB 1 ATOM 1797 S SG . CYS B 2 22 ? 26.958 16.954 1.155 1.00 32.63 ? 22 CYS B SG 1 ATOM 1798 N N . ALA B 2 23 ? 25.661 17.722 4.066 1.00 29.22 ? 23 ALA B N 1 ATOM 1799 C CA . ALA B 2 23 ? 25.451 17.008 5.322 1.00 16.35 ? 23 ALA B CA 1 ATOM 1800 C C . ALA B 2 23 ? 25.370 15.497 5.132 1.00 18.91 ? 23 ALA B C 1 ATOM 1801 O O . ALA B 2 23 ? 24.449 14.992 4.491 1.00 17.83 ? 23 ALA B O 1 ATOM 1802 C CB . ALA B 2 23 ? 24.193 17.515 6.006 1.00 16.91 ? 23 ALA B CB 1 ATOM 1803 N N . VAL B 2 24 ? 26.341 14.785 5.696 1.00 23.92 ? 24 VAL B N 1 ATOM 1804 C CA . VAL B 2 24 ? 26.323 13.327 5.715 1.00 16.95 ? 24 VAL B CA 1 ATOM 1805 C C . VAL B 2 24 ? 25.467 12.869 6.889 1.00 20.05 ? 24 VAL B C 1 ATOM 1806 O O . VAL B 2 24 ? 25.570 13.425 7.981 1.00 24.69 ? 24 VAL B O 1 ATOM 1807 C CB . VAL B 2 24 ? 27.740 12.742 5.838 1.00 17.29 ? 24 VAL B CB 1 ATOM 1808 C CG1 . VAL B 2 24 ? 27.715 11.236 5.643 1.00 28.98 ? 24 VAL B CG1 1 ATOM 1809 C CG2 . VAL B 2 24 ? 28.667 13.395 4.826 1.00 16.47 ? 24 VAL B CG2 1 ATOM 1810 N N . TYR B 2 25 ? 24.607 11.914 6.551 1.00 26.78 ? 25 TYR B N 1 ATOM 1811 C CA . TYR B 2 25 ? 23.578 11.427 7.433 1.00 67.33 ? 25 TYR B CA 1 ATOM 1812 C C . TYR B 2 25 ? 23.602 9.955 7.876 1.00 43.48 ? 25 TYR B C 1 ATOM 1813 O O . TYR B 2 25 ? 23.237 9.680 9.006 1.00 79.05 ? 25 TYR B O 1 ATOM 1814 C CB . TYR B 2 25 ? 22.192 11.880 6.930 1.00 34.68 ? 25 TYR B CB 1 ATOM 1815 C CG . TYR B 2 25 ? 21.913 13.317 7.289 1.00 33.80 ? 25 TYR B CG 1 ATOM 1816 C CD1 . TYR B 2 25 ? 22.237 13.783 8.529 1.00 37.62 ? 25 TYR B CD1 1 ATOM 1817 C CD2 . TYR B 2 25 ? 21.357 14.205 6.392 1.00 30.32 ? 25 TYR B CD2 1 ATOM 1818 C CE1 . TYR B 2 25 ? 22.017 15.085 8.884 1.00 38.99 ? 25 TYR B CE1 1 ATOM 1819 C CE2 . TYR B 2 25 ? 21.124 15.518 6.747 1.00 28.28 ? 25 TYR B CE2 1 ATOM 1820 C CZ . TYR B 2 25 ? 21.460 15.941 8.005 1.00 34.42 ? 25 TYR B CZ 1 ATOM 1821 O OH . TYR B 2 25 ? 21.265 17.222 8.438 1.00 30.17 ? 25 TYR B OH 1 ATOM 1822 N N . ASN B 2 26 ? 24.032 9.019 7.045 1.00 24.60 ? 26 ASN B N 1 ATOM 1823 C CA . ASN B 2 26 ? 24.027 7.606 7.471 1.00 29.49 ? 26 ASN B CA 1 ATOM 1824 C C . ASN B 2 26 ? 25.366 6.896 7.471 1.00 25.80 ? 26 ASN B C 1 ATOM 1825 O O . ASN B 2 26 ? 25.430 5.708 7.298 1.00 21.89 ? 26 ASN B O 1 ATOM 1826 C CB . ASN B 2 26 ? 22.939 6.777 6.771 1.00 60.03 ? 26 ASN B CB 1 ATOM 1827 C CG . ASN B 2 26 ? 22.072 5.989 7.739 1.00 32.05 ? 26 ASN B CG 1 ATOM 1828 O OD1 . ASN B 2 26 ? 22.154 6.162 8.936 1.00 28.52 ? 26 ASN B OD1 1 ATOM 1829 N ND2 . ASN B 2 26 ? 21.234 5.120 7.209 1.00 36.98 ? 26 ASN B ND2 1 ATOM 1830 N N . GLU B 2 27 ? 26.437 7.647 7.635 1.00 25.99 ? 27 GLU B N 1 ATOM 1831 C CA . GLU B 2 27 ? 27.762 7.073 7.625 1.00 23.38 ? 27 GLU B CA 1 ATOM 1832 C C . GLU B 2 27 ? 28.789 7.855 8.367 1.00 24.99 ? 27 GLU B C 1 ATOM 1833 O O . GLU B 2 27 ? 28.555 8.975 8.750 1.00 29.77 ? 27 GLU B O 1 ATOM 1834 C CB . GLU B 2 27 ? 28.250 6.939 6.226 1.00 27.62 ? 27 GLU B CB 1 ATOM 1835 C CG . GLU B 2 27 ? 29.130 5.751 6.047 1.00 28.50 ? 27 GLU B CG 1 ATOM 1836 C CD . GLU B 2 27 ? 29.229 5.449 4.613 1.00 41.72 ? 27 GLU B CD 1 ATOM 1837 O OE1 . GLU B 2 27 ? 29.483 6.403 3.879 1.00 42.85 ? 27 GLU B OE1 1 ATOM 1838 O OE2 . GLU B 2 27 ? 29.008 4.290 4.227 1.00 64.82 ? 27 GLU B OE2 1 ATOM 1839 N N . SER B 2 28 ? 29.934 7.226 8.579 1.00 25.77 ? 28 SER B N 1 ATOM 1840 C CA . SER B 2 28 ? 31.084 7.862 9.199 1.00 46.88 ? 28 SER B CA 1 ATOM 1841 C C . SER B 2 28 ? 31.840 8.852 8.325 1.00 29.40 ? 28 SER B C 1 ATOM 1842 O O . SER B 2 28 ? 32.155 8.569 7.193 1.00 27.60 ? 28 SER B O 1 ATOM 1843 C CB . SER B 2 28 ? 32.051 6.802 9.713 1.00 50.79 ? 28 SER B CB 1 ATOM 1844 O OG . SER B 2 28 ? 33.005 6.452 8.740 1.00 36.55 ? 28 SER B OG 1 ATOM 1845 N N . LEU B 2 29 ? 32.138 10.012 8.892 1.00 31.46 ? 29 LEU B N 1 ATOM 1846 C CA . LEU B 2 29 ? 32.976 11.006 8.260 1.00 21.97 ? 29 LEU B CA 1 ATOM 1847 C C . LEU B 2 29 ? 34.393 10.524 8.094 1.00 24.75 ? 29 LEU B C 1 ATOM 1848 O O . LEU B 2 29 ? 35.068 10.852 7.144 1.00 31.48 ? 29 LEU B O 1 ATOM 1849 C CB . LEU B 2 29 ? 32.948 12.291 9.050 1.00 19.75 ? 29 LEU B CB 1 ATOM 1850 C CG . LEU B 2 29 ? 32.368 13.474 8.309 1.00 18.81 ? 29 LEU B CG 1 ATOM 1851 C CD1 . LEU B 2 29 ? 31.036 13.084 7.733 1.00 23.24 ? 29 LEU B CD1 1 ATOM 1852 C CD2 . LEU B 2 29 ? 32.223 14.636 9.255 1.00 19.55 ? 29 LEU B CD2 1 ATOM 1853 N N . SER B 2 30 ? 34.854 9.786 9.080 1.00 24.06 ? 30 SER B N 1 ATOM 1854 C CA . SER B 2 30 ? 36.207 9.285 9.119 1.00 23.83 ? 30 SER B CA 1 ATOM 1855 C C . SER B 2 30 ? 36.544 8.317 8.024 1.00 25.56 ? 30 SER B C 1 ATOM 1856 O O . SER B 2 30 ? 37.649 8.275 7.565 1.00 38.82 ? 30 SER B O 1 ATOM 1857 C CB . SER B 2 30 ? 36.466 8.670 10.461 1.00 22.83 ? 30 SER B CB 1 ATOM 1858 O OG . SER B 2 30 ? 35.813 9.444 11.423 1.00 42.26 ? 30 SER B OG 1 ATOM 1859 N N . ALA B 2 31 ? 35.587 7.491 7.661 1.00 25.63 ? 31 ALA B N 1 ATOM 1860 C CA . ALA B 2 31 ? 35.763 6.450 6.674 1.00 22.98 ? 31 ALA B CA 1 ATOM 1861 C C . ALA B 2 31 ? 36.096 6.969 5.285 1.00 29.88 ? 31 ALA B C 1 ATOM 1862 O O . ALA B 2 31 ? 36.845 6.358 4.552 1.00 27.77 ? 31 ALA B O 1 ATOM 1863 C CB . ALA B 2 31 ? 34.532 5.582 6.638 1.00 20.73 ? 31 ALA B CB 1 ATOM 1864 N N . PHE B 2 32 ? 35.511 8.090 4.918 1.00 28.69 ? 32 PHE B N 1 ATOM 1865 C CA . PHE B 2 32 ? 35.624 8.578 3.574 1.00 21.34 ? 32 PHE B CA 1 ATOM 1866 C C . PHE B 2 32 ? 36.131 10.003 3.475 1.00 25.06 ? 32 PHE B C 1 ATOM 1867 O O . PHE B 2 32 ? 36.083 10.759 4.421 1.00 20.87 ? 32 PHE B O 1 ATOM 1868 C CB . PHE B 2 32 ? 34.273 8.481 2.893 1.00 22.71 ? 32 PHE B CB 1 ATOM 1869 C CG . PHE B 2 32 ? 33.665 7.130 2.962 1.00 17.21 ? 32 PHE B CG 1 ATOM 1870 C CD1 . PHE B 2 32 ? 33.935 6.208 2.014 1.00 17.11 ? 32 PHE B CD1 1 ATOM 1871 C CD2 . PHE B 2 32 ? 32.830 6.794 3.985 1.00 20.67 ? 32 PHE B CD2 1 ATOM 1872 C CE1 . PHE B 2 32 ? 33.392 4.968 2.077 1.00 29.59 ? 32 PHE B CE1 1 ATOM 1873 C CE2 . PHE B 2 32 ? 32.271 5.558 4.058 1.00 19.93 ? 32 PHE B CE2 1 ATOM 1874 C CZ . PHE B 2 32 ? 32.558 4.643 3.098 1.00 23.07 ? 32 PHE B CZ 1 ATOM 1875 N N . SER B 2 33 ? 36.649 10.342 2.308 1.00 18.68 ? 33 SER B N 1 ATOM 1876 C CA . SER B 2 33 ? 36.960 11.724 1.966 1.00 22.65 ? 33 SER B CA 1 ATOM 1877 C C . SER B 2 33 ? 35.752 12.329 1.263 1.00 17.44 ? 33 SER B C 1 ATOM 1878 O O . SER B 2 33 ? 34.974 11.612 0.635 1.00 21.94 ? 33 SER B O 1 ATOM 1879 C CB . SER B 2 33 ? 38.204 11.808 1.079 1.00 24.31 ? 33 SER B CB 1 ATOM 1880 O OG . SER B 2 33 ? 37.998 11.141 -0.154 1.00 37.78 ? 33 SER B OG 1 ATOM 1881 N N . TRP B 2 34 ? 35.580 13.634 1.384 1.00 17.30 ? 34 TRP B N 1 ATOM 1882 C CA . TRP B 2 34 ? 34.398 14.284 0.861 1.00 15.76 ? 34 TRP B CA 1 ATOM 1883 C C . TRP B 2 34 ? 34.723 15.383 -0.129 1.00 18.36 ? 34 TRP B C 1 ATOM 1884 O O . TRP B 2 34 ? 35.471 16.285 0.175 1.00 31.75 ? 34 TRP B O 1 ATOM 1885 C CB . TRP B 2 34 ? 33.579 14.824 2.027 1.00 16.08 ? 34 TRP B CB 1 ATOM 1886 C CG . TRP B 2 34 ? 33.341 13.789 3.052 1.00 16.03 ? 34 TRP B CG 1 ATOM 1887 C CD1 . TRP B 2 34 ? 34.025 13.613 4.198 1.00 17.67 ? 34 TRP B CD1 1 ATOM 1888 C CD2 . TRP B 2 34 ? 32.356 12.761 3.011 1.00 14.85 ? 34 TRP B CD2 1 ATOM 1889 N NE1 . TRP B 2 34 ? 33.530 12.548 4.882 1.00 16.68 ? 34 TRP B NE1 1 ATOM 1890 C CE2 . TRP B 2 34 ? 32.500 12.007 4.168 1.00 14.51 ? 34 TRP B CE2 1 ATOM 1891 C CE3 . TRP B 2 34 ? 31.357 12.415 2.107 1.00 14.11 ? 34 TRP B CE3 1 ATOM 1892 C CZ2 . TRP B 2 34 ? 31.698 10.924 4.442 1.00 16.36 ? 34 TRP B CZ2 1 ATOM 1893 C CZ3 . TRP B 2 34 ? 30.567 11.359 2.383 1.00 17.99 ? 34 TRP B CZ3 1 ATOM 1894 C CH2 . TRP B 2 34 ? 30.736 10.620 3.537 1.00 14.14 ? 34 TRP B CH2 1 ATOM 1895 N N . SER B 2 35 ? 34.112 15.330 -1.304 1.00 30.00 ? 35 SER B N 1 ATOM 1896 C CA . SER B 2 35 ? 34.495 16.219 -2.394 1.00 30.00 ? 35 SER B CA 1 ATOM 1897 C C . SER B 2 35 ? 33.384 17.072 -2.965 1.00 30.00 ? 35 SER B C 1 ATOM 1898 O O . SER B 2 35 ? 32.225 16.740 -2.888 1.00 30.00 ? 35 SER B O 1 ATOM 1899 C CB . SER B 2 35 ? 35.129 15.421 -3.523 1.00 20.00 ? 35 SER B CB 1 ATOM 1900 O OG . SER B 2 35 ? 36.155 14.583 -3.042 1.00 20.00 ? 35 SER B OG 1 ATOM 1901 N N . TRP B 2 36 ? 33.763 18.191 -3.547 1.00 11.23 ? 36 TRP B N 1 ATOM 1902 C CA . TRP B 2 36 ? 32.802 19.095 -4.135 1.00 11.38 ? 36 TRP B CA 1 ATOM 1903 C C . TRP B 2 36 ? 32.930 19.098 -5.641 1.00 12.38 ? 36 TRP B C 1 ATOM 1904 O O . TRP B 2 36 ? 34.008 19.202 -6.159 1.00 14.75 ? 36 TRP B O 1 ATOM 1905 C CB . TRP B 2 36 ? 32.996 20.496 -3.569 1.00 17.13 ? 36 TRP B CB 1 ATOM 1906 C CG . TRP B 2 36 ? 32.295 20.700 -2.273 1.00 21.11 ? 36 TRP B CG 1 ATOM 1907 C CD1 . TRP B 2 36 ? 32.838 20.666 -1.033 1.00 13.58 ? 36 TRP B CD1 1 ATOM 1908 C CD2 . TRP B 2 36 ? 30.907 20.952 -2.094 1.00 13.32 ? 36 TRP B CD2 1 ATOM 1909 N NE1 . TRP B 2 36 ? 31.881 20.883 -0.093 1.00 12.80 ? 36 TRP B NE1 1 ATOM 1910 C CE2 . TRP B 2 36 ? 30.683 21.068 -0.720 1.00 12.73 ? 36 TRP B CE2 1 ATOM 1911 C CE3 . TRP B 2 36 ? 29.833 21.106 -2.967 1.00 12.06 ? 36 TRP B CE3 1 ATOM 1912 C CZ2 . TRP B 2 36 ? 29.439 21.325 -0.199 1.00 13.28 ? 36 TRP B CZ2 1 ATOM 1913 C CZ3 . TRP B 2 36 ? 28.606 21.359 -2.447 1.00 14.84 ? 36 TRP B CZ3 1 ATOM 1914 C CH2 . TRP B 2 36 ? 28.410 21.464 -1.080 1.00 14.89 ? 36 TRP B CH2 1 ATOM 1915 N N . ILE B 2 37 ? 31.819 18.951 -6.343 1.00 11.28 ? 37 ILE B N 1 ATOM 1916 C CA . ILE B 2 37 ? 31.854 18.894 -7.799 1.00 10.71 ? 37 ILE B CA 1 ATOM 1917 C C . ILE B 2 37 ? 30.795 19.821 -8.386 1.00 12.88 ? 37 ILE B C 1 ATOM 1918 O O . ILE B 2 37 ? 29.682 19.899 -7.868 1.00 32.52 ? 37 ILE B O 1 ATOM 1919 C CB . ILE B 2 37 ? 31.617 17.457 -8.318 1.00 9.62 ? 37 ILE B CB 1 ATOM 1920 C CG1 . ILE B 2 37 ? 32.516 16.459 -7.587 1.00 9.99 ? 37 ILE B CG1 1 ATOM 1921 C CG2 . ILE B 2 37 ? 31.846 17.380 -9.819 1.00 10.55 ? 37 ILE B CG2 1 ATOM 1922 C CD1 . ILE B 2 37 ? 32.211 15.023 -7.913 1.00 11.87 ? 37 ILE B CD1 1 ATOM 1923 N N . ARG B 2 38 ? 31.140 20.524 -9.460 1.00 10.51 ? 38 ARG B N 1 ATOM 1924 C CA . ARG B 2 38 ? 30.175 21.387 -10.132 1.00 11.39 ? 38 ARG B CA 1 ATOM 1925 C C . ARG B 2 38 ? 30.022 21.017 -11.605 1.00 11.22 ? 38 ARG B C 1 ATOM 1926 O O . ARG B 2 38 ? 30.946 20.488 -12.224 1.00 12.82 ? 38 ARG B O 1 ATOM 1927 C CB . ARG B 2 38 ? 30.576 22.857 -9.993 1.00 14.99 ? 38 ARG B CB 1 ATOM 1928 C CG . ARG B 2 38 ? 31.866 23.250 -10.695 1.00 13.74 ? 38 ARG B CG 1 ATOM 1929 C CD . ARG B 2 38 ? 32.159 24.723 -10.453 1.00 20.38 ? 38 ARG B CD 1 ATOM 1930 N NE . ARG B 2 38 ? 33.301 25.210 -11.217 1.00 16.60 ? 38 ARG B NE 1 ATOM 1931 C CZ . ARG B 2 38 ? 33.711 26.474 -11.213 1.00 22.05 ? 38 ARG B CZ 1 ATOM 1932 N NH1 . ARG B 2 38 ? 33.072 27.376 -10.481 1.00 14.91 ? 38 ARG B NH1 1 ATOM 1933 N NH2 . ARG B 2 38 ? 34.760 26.837 -11.939 1.00 27.68 ? 38 ARG B NH2 1 ATOM 1934 N N . GLN B 2 39 ? 28.845 21.297 -12.157 1.00 14.03 ? 39 GLN B N 1 ATOM 1935 C CA . GLN B 2 39 ? 28.543 20.960 -13.544 1.00 11.94 ? 39 GLN B CA 1 ATOM 1936 C C . GLN B 2 39 ? 28.012 22.170 -14.306 1.00 14.06 ? 39 GLN B C 1 ATOM 1937 O O . GLN B 2 39 ? 26.914 22.656 -14.034 1.00 10.23 ? 39 GLN B O 1 ATOM 1938 C CB . GLN B 2 39 ? 27.534 19.814 -13.605 1.00 11.27 ? 39 GLN B CB 1 ATOM 1939 C CG . GLN B 2 39 ? 27.266 19.299 -15.007 1.00 9.46 ? 39 GLN B CG 1 ATOM 1940 C CD . GLN B 2 39 ? 26.319 18.119 -15.019 1.00 8.37 ? 39 GLN B CD 1 ATOM 1941 O OE1 . GLN B 2 39 ? 26.422 17.236 -15.870 1.00 11.36 ? 39 GLN B OE1 1 ATOM 1942 N NE2 . GLN B 2 39 ? 25.387 18.097 -14.073 1.00 14.32 ? 39 GLN B NE2 1 ATOM 1943 N N . PHE B 2 40 ? 28.800 22.644 -15.265 1.00 16.19 ? 40 PHE B N 1 ATOM 1944 C CA . PHE B 2 40 ? 28.448 23.820 -16.053 1.00 17.66 ? 40 PHE B CA 1 ATOM 1945 C C . PHE B 2 40 ? 27.266 23.538 -16.984 1.00 26.44 ? 40 PHE B C 1 ATOM 1946 O O . PHE B 2 40 ? 27.040 22.389 -17.365 1.00 20.20 ? 40 PHE B O 1 ATOM 1947 C CB . PHE B 2 40 ? 29.667 24.290 -16.852 1.00 20.78 ? 40 PHE B CB 1 ATOM 1948 C CG . PHE B 2 40 ? 30.862 24.611 -15.999 1.00 18.78 ? 40 PHE B CG 1 ATOM 1949 C CD1 . PHE B 2 40 ? 30.987 25.852 -15.399 1.00 16.22 ? 40 PHE B CD1 1 ATOM 1950 C CD2 . PHE B 2 40 ? 31.859 23.671 -15.794 1.00 22.27 ? 40 PHE B CD2 1 ATOM 1951 C CE1 . PHE B 2 40 ? 32.085 26.152 -14.612 1.00 17.87 ? 40 PHE B CE1 1 ATOM 1952 C CE2 . PHE B 2 40 ? 32.958 23.965 -15.009 1.00 25.97 ? 40 PHE B CE2 1 ATOM 1953 C CZ . PHE B 2 40 ? 33.070 25.208 -14.418 1.00 23.70 ? 40 PHE B CZ 1 ATOM 1954 N N . PRO B 2 41 ? 26.499 24.589 -17.338 1.00 26.81 ? 41 PRO B N 1 ATOM 1955 C CA . PRO B 2 41 ? 25.320 24.471 -18.206 1.00 18.39 ? 41 PRO B CA 1 ATOM 1956 C C . PRO B 2 41 ? 25.581 23.697 -19.494 1.00 22.78 ? 41 PRO B C 1 ATOM 1957 O O . PRO B 2 41 ? 26.309 24.175 -20.365 1.00 22.47 ? 41 PRO B O 1 ATOM 1958 C CB . PRO B 2 41 ? 24.978 25.929 -18.519 1.00 14.64 ? 41 PRO B CB 1 ATOM 1959 C CG . PRO B 2 41 ? 25.434 26.670 -17.322 1.00 15.36 ? 41 PRO B CG 1 ATOM 1960 C CD . PRO B 2 41 ? 26.678 25.970 -16.851 1.00 13.96 ? 41 PRO B CD 1 ATOM 1961 N N . GLY B 2 42 ? 24.988 22.512 -19.604 1.00 37.81 ? 42 GLY B N 1 ATOM 1962 C CA . GLY B 2 42 ? 25.155 21.676 -20.778 1.00 49.87 ? 42 GLY B CA 1 ATOM 1963 C C . GLY B 2 42 ? 26.600 21.288 -21.025 1.00 38.33 ? 42 GLY B C 1 ATOM 1964 O O . GLY B 2 42 ? 26.998 21.042 -22.163 1.00 63.64 ? 42 GLY B O 1 ATOM 1965 N N . GLN B 2 43 ? 27.388 21.236 -19.956 1.00 31.27 ? 43 GLN B N 1 ATOM 1966 C CA . GLN B 2 43 ? 28.804 20.901 -20.063 1.00 44.89 ? 43 GLN B CA 1 ATOM 1967 C C . GLN B 2 43 ? 29.184 19.711 -19.193 1.00 29.75 ? 43 GLN B C 1 ATOM 1968 O O . GLN B 2 43 ? 28.325 19.048 -18.610 1.00 18.68 ? 43 GLN B O 1 ATOM 1969 C CB . GLN B 2 43 ? 29.675 22.099 -19.681 1.00 48.22 ? 43 GLN B CB 1 ATOM 1970 C CG . GLN B 2 43 ? 29.937 23.093 -20.799 1.00 43.45 ? 43 GLN B CG 1 ATOM 1971 C CD . GLN B 2 43 ? 31.108 24.008 -20.487 1.00 65.81 ? 43 GLN B CD 1 ATOM 1972 O OE1 . GLN B 2 43 ? 31.805 23.823 -19.488 1.00 58.85 ? 43 GLN B OE1 1 ATOM 1973 N NE2 . GLN B 2 43 ? 31.332 24.999 -21.342 1.00 63.30 ? 43 GLN B NE2 1 ATOM 1974 N N . GLY B 2 44 ? 30.485 19.456 -19.108 1.00 23.01 ? 44 GLY B N 1 ATOM 1975 C CA . GLY B 2 44 ? 31.005 18.353 -18.323 1.00 19.89 ? 44 GLY B CA 1 ATOM 1976 C C . GLY B 2 44 ? 31.143 18.700 -16.856 1.00 18.90 ? 44 GLY B C 1 ATOM 1977 O O . GLY B 2 44 ? 30.568 19.679 -16.380 1.00 22.37 ? 44 GLY B O 1 ATOM 1978 N N . LEU B 2 45 ? 31.920 17.898 -16.139 1.00 12.41 ? 45 LEU B N 1 ATOM 1979 C CA . LEU B 2 45 ? 32.060 18.054 -14.698 1.00 11.29 ? 45 LEU B CA 1 ATOM 1980 C C . LEU B 2 45 ? 33.451 18.545 -14.313 1.00 14.33 ? 45 LEU B C 1 ATOM 1981 O O . LEU B 2 45 ? 34.443 18.187 -14.948 1.00 25.23 ? 45 LEU B O 1 ATOM 1982 C CB . LEU B 2 45 ? 31.760 16.726 -14.003 1.00 11.12 ? 45 LEU B CB 1 ATOM 1983 C CG . LEU B 2 45 ? 30.439 16.069 -14.405 1.00 7.36 ? 45 LEU B CG 1 ATOM 1984 C CD1 . LEU B 2 45 ? 30.515 14.563 -14.236 1.00 11.28 ? 45 LEU B CD1 1 ATOM 1985 C CD2 . LEU B 2 45 ? 29.294 16.638 -13.587 1.00 8.50 ? 45 LEU B CD2 1 ATOM 1986 N N . GLU B 2 46 ? 33.518 19.366 -13.270 1.00 16.37 ? 46 GLU B N 1 ATOM 1987 C CA . GLU B 2 46 ? 34.792 19.858 -12.761 1.00 11.78 ? 46 GLU B CA 1 ATOM 1988 C C . GLU B 2 46 ? 34.932 19.551 -11.274 1.00 17.54 ? 46 GLU B C 1 ATOM 1989 O O . GLU B 2 46 ? 34.026 19.823 -10.486 1.00 13.45 ? 46 GLU B O 1 ATOM 1990 C CB . GLU B 2 46 ? 34.929 21.363 -13.002 1.00 14.45 ? 46 GLU B CB 1 ATOM 1991 C CG . GLU B 2 46 ? 36.291 21.927 -12.623 1.00 15.77 ? 46 GLU B CG 1 ATOM 1992 C CD . GLU B 2 46 ? 36.338 23.443 -12.680 1.00 34.08 ? 46 GLU B CD 1 ATOM 1993 O OE1 . GLU B 2 46 ? 37.384 23.994 -13.083 1.00 20.56 ? 46 GLU B OE1 1 ATOM 1994 O OE2 . GLU B 2 46 ? 35.332 24.086 -12.313 1.00 29.13 ? 46 GLU B OE2 1 ATOM 1995 N N . TRP B 2 47 ? 36.070 18.979 -10.897 1.00 18.49 ? 47 TRP B N 1 ATOM 1996 C CA . TRP B 2 47 ? 36.340 18.668 -9.500 1.00 11.27 ? 47 TRP B CA 1 ATOM 1997 C C . TRP B 2 47 ? 36.868 19.902 -8.776 1.00 16.97 ? 47 TRP B C 1 ATOM 1998 O O . TRP B 2 47 ? 37.825 20.535 -9.223 1.00 28.33 ? 47 TRP B O 1 ATOM 1999 C CB . TRP B 2 47 ? 37.332 17.509 -9.391 1.00 13.98 ? 47 TRP B CB 1 ATOM 2000 C CG . TRP B 2 47 ? 37.667 17.134 -7.983 1.00 19.69 ? 47 TRP B CG 1 ATOM 2001 C CD1 . TRP B 2 47 ? 36.875 16.453 -7.104 1.00 27.15 ? 47 TRP B CD1 1 ATOM 2002 C CD2 . TRP B 2 47 ? 38.890 17.408 -7.291 1.00 19.88 ? 47 TRP B CD2 1 ATOM 2003 N NE1 . TRP B 2 47 ? 37.528 16.292 -5.906 1.00 18.88 ? 47 TRP B NE1 1 ATOM 2004 C CE2 . TRP B 2 47 ? 38.768 16.869 -5.995 1.00 28.56 ? 47 TRP B CE2 1 ATOM 2005 C CE3 . TRP B 2 47 ? 40.077 18.059 -7.641 1.00 27.96 ? 47 TRP B CE3 1 ATOM 2006 C CZ2 . TRP B 2 47 ? 39.786 16.960 -5.050 1.00 35.94 ? 47 TRP B CZ2 1 ATOM 2007 C CZ3 . TRP B 2 47 ? 41.086 18.149 -6.700 1.00 24.42 ? 47 TRP B CZ3 1 ATOM 2008 C CH2 . TRP B 2 47 ? 40.934 17.603 -5.420 1.00 23.50 ? 47 TRP B CH2 1 ATOM 2009 N N . ILE B 2 48 ? 36.232 20.241 -7.659 1.00 21.02 ? 48 ILE B N 1 ATOM 2010 C CA . ILE B 2 48 ? 36.563 21.454 -6.919 1.00 15.97 ? 48 ILE B CA 1 ATOM 2011 C C . ILE B 2 48 ? 37.609 21.200 -5.834 1.00 21.25 ? 48 ILE B C 1 ATOM 2012 O O . ILE B 2 48 ? 38.639 21.873 -5.791 1.00 22.75 ? 48 ILE B O 1 ATOM 2013 C CB . ILE B 2 48 ? 35.298 22.073 -6.286 1.00 13.71 ? 48 ILE B CB 1 ATOM 2014 C CG1 . ILE B 2 48 ? 34.422 22.701 -7.371 1.00 8.76 ? 48 ILE B CG1 1 ATOM 2015 C CG2 . ILE B 2 48 ? 35.663 23.110 -5.244 1.00 18.55 ? 48 ILE B CG2 1 ATOM 2016 C CD1 . ILE B 2 48 ? 33.174 23.360 -6.839 1.00 9.59 ? 48 ILE B CD1 1 ATOM 2017 N N . GLY B 2 49 ? 37.349 20.229 -4.962 1.00 17.74 ? 49 GLY B N 1 ATOM 2018 C CA . GLY B 2 49 ? 38.278 19.910 -3.891 1.00 18.44 ? 49 GLY B CA 1 ATOM 2019 C C . GLY B 2 49 ? 37.733 18.906 -2.894 1.00 21.98 ? 49 GLY B C 1 ATOM 2020 O O . GLY B 2 49 ? 36.520 18.747 -2.764 1.00 41.84 ? 49 GLY B O 1 ATOM 2021 N N . GLU B 2 50 ? 38.595 18.254 -2.136 1.00 22.54 ? 50 GLU B N 1 ATOM 2022 C CA . GLU B 2 50 ? 38.162 17.258 -1.170 1.00 22.97 ? 50 GLU B CA 1 ATOM 2023 C C . GLU B 2 50 ? 38.651 17.561 0.230 1.00 23.73 ? 50 GLU B C 1 ATOM 2024 O O . GLU B 2 50 ? 39.553 18.340 0.407 1.00 27.30 ? 50 GLU B O 1 ATOM 2025 C CB . GLU B 2 50 ? 38.644 15.883 -1.577 1.00 27.22 ? 50 GLU B CB 1 ATOM 2026 C CG . GLU B 2 50 ? 40.002 15.849 -2.239 1.00 41.74 ? 50 GLU B CG 1 ATOM 2027 C CD . GLU B 2 50 ? 40.686 14.510 -2.090 1.00 65.61 ? 50 GLU B CD 1 ATOM 2028 O OE1 . GLU B 2 50 ? 40.104 13.612 -1.475 1.00 83.11 ? 50 GLU B OE1 1 ATOM 2029 O OE2 . GLU B 2 50 ? 41.807 14.337 -2.583 1.00 50.80 ? 50 GLU B OE2 1 ATOM 2030 N N . ILE B 2 51 ? 37.999 16.986 1.230 1.00 23.67 ? 51 ILE B N 1 ATOM 2031 C CA . ILE B 2 51 ? 38.439 17.117 2.608 1.00 33.66 ? 51 ILE B CA 1 ATOM 2032 C C . ILE B 2 51 ? 38.252 15.845 3.450 1.00 27.38 ? 51 ILE B C 1 ATOM 2033 O O . ILE B 2 51 ? 37.337 15.099 3.227 1.00 22.87 ? 51 ILE B O 1 ATOM 2034 C CB . ILE B 2 51 ? 37.772 18.334 3.243 1.00 20.10 ? 51 ILE B CB 1 ATOM 2035 C CG1 . ILE B 2 51 ? 38.251 18.547 4.661 1.00 23.69 ? 51 ILE B CG1 1 ATOM 2036 C CG2 . ILE B 2 51 ? 36.279 18.194 3.186 1.00 17.54 ? 51 ILE B CG2 1 ATOM 2037 C CD1 . ILE B 2 51 ? 38.255 19.989 5.069 1.00 21.81 ? 51 ILE B CD1 1 ATOM 2038 N N . ASP B 2 52 ? 39.161 15.602 4.396 1.00 27.81 ? 52 ASP B N 1 ATOM 2039 C CA . ASP B 2 52 ? 39.083 14.504 5.369 1.00 25.48 ? 52 ASP B CA 1 ATOM 2040 C C . ASP B 2 52 ? 38.500 14.978 6.661 1.00 27.28 ? 52 ASP B C 1 ATOM 2041 O O . ASP B 2 52 ? 38.276 16.147 6.848 1.00 25.57 ? 52 ASP B O 1 ATOM 2042 C CB . ASP B 2 52 ? 40.448 13.948 5.744 1.00 28.92 ? 52 ASP B CB 1 ATOM 2043 C CG . ASP B 2 52 ? 41.288 13.626 4.574 1.00 60.60 ? 52 ASP B CG 1 ATOM 2044 O OD1 . ASP B 2 52 ? 40.725 13.469 3.486 1.00 82.10 ? 52 ASP B OD1 1 ATOM 2045 O OD2 . ASP B 2 52 ? 42.513 13.517 4.735 1.00 49.73 ? 52 ASP B OD2 1 ATOM 2046 N N . HIS B 2 53 ? 38.268 14.046 7.565 1.00 27.32 ? 53 HIS B N 1 ATOM 2047 C CA . HIS B 2 53 ? 37.902 14.381 8.930 1.00 27.10 ? 53 HIS B CA 1 ATOM 2048 C C . HIS B 2 53 ? 39.018 15.106 9.652 1.00 27.09 ? 53 HIS B C 1 ATOM 2049 O O . HIS B 2 53 ? 38.773 15.899 10.517 1.00 49.18 ? 53 HIS B O 1 ATOM 2050 C CB . HIS B 2 53 ? 37.388 13.184 9.705 1.00 27.66 ? 53 HIS B CB 1 ATOM 2051 C CG . HIS B 2 53 ? 38.460 12.308 10.237 1.00 24.94 ? 53 HIS B CG 1 ATOM 2052 N ND1 . HIS B 2 53 ? 39.066 11.341 9.479 1.00 37.92 ? 53 HIS B ND1 1 ATOM 2053 C CD2 . HIS B 2 53 ? 39.034 12.248 11.453 1.00 28.27 ? 53 HIS B CD2 1 ATOM 2054 C CE1 . HIS B 2 53 ? 39.976 10.726 10.200 1.00 30.96 ? 53 HIS B CE1 1 ATOM 2055 N NE2 . HIS B 2 53 ? 39.979 11.261 11.402 1.00 52.19 ? 53 HIS B NE2 1 ATOM 2056 N N . THR B 2 54 ? 40.252 14.802 9.322 1.00 26.94 ? 54 THR B N 1 ATOM 2057 C CA . THR B 2 54 ? 41.352 15.621 9.751 1.00 29.21 ? 54 THR B CA 1 ATOM 2058 C C . THR B 2 54 ? 41.160 16.879 8.932 1.00 39.91 ? 54 THR B C 1 ATOM 2059 O O . THR B 2 54 ? 40.475 16.839 7.939 1.00 57.89 ? 54 THR B O 1 ATOM 2060 C CB . THR B 2 54 ? 42.703 14.955 9.462 1.00 25.71 ? 54 THR B CB 1 ATOM 2061 O OG1 . THR B 2 54 ? 43.066 15.152 8.102 1.00 39.40 ? 54 THR B OG1 1 ATOM 2062 C CG2 . THR B 2 54 ? 42.622 13.503 9.695 1.00 21.42 ? 54 THR B CG2 1 ATOM 2063 N N . THR B 2 55 ? 41.739 17.995 9.322 1.00 29.91 ? 55 THR B N 1 ATOM 2064 C CA . THR B 2 55 ? 41.430 19.254 8.670 1.00 33.19 ? 55 THR B CA 1 ATOM 2065 C C . THR B 2 55 ? 41.806 19.233 7.199 1.00 46.38 ? 55 THR B C 1 ATOM 2066 O O . THR B 2 55 ? 41.409 20.111 6.467 1.00 33.56 ? 55 THR B O 1 ATOM 2067 C CB . THR B 2 55 ? 42.227 20.391 9.286 1.00 32.59 ? 55 THR B CB 1 ATOM 2068 O OG1 . THR B 2 55 ? 43.481 19.879 9.715 1.00 48.76 ? 55 THR B OG1 1 ATOM 2069 C CG2 . THR B 2 55 ? 41.513 20.962 10.454 1.00 63.04 ? 55 THR B CG2 1 ATOM 2070 N N . SER B 2 56 ? 42.642 18.283 6.792 1.00 36.69 ? 56 SER B N 1 ATOM 2071 C CA . SER B 2 56 ? 43.337 18.323 5.513 1.00 37.67 ? 56 SER B CA 1 ATOM 2072 C C . SER B 2 56 ? 42.498 18.293 4.256 1.00 39.86 ? 56 SER B C 1 ATOM 2073 O O . SER B 2 56 ? 41.674 17.429 4.065 1.00 31.36 ? 56 SER B O 1 ATOM 2074 C CB . SER B 2 56 ? 44.291 17.154 5.455 1.00 34.99 ? 56 SER B CB 1 ATOM 2075 O OG . SER B 2 56 ? 43.553 15.965 5.482 1.00 54.33 ? 56 SER B OG 1 ATOM 2076 N N . SER B 2 57 ? 42.798 19.222 3.361 1.00 33.41 ? 57 SER B N 1 ATOM 2077 C CA . SER B 2 57 ? 42.053 19.385 2.144 1.00 23.26 ? 57 SER B CA 1 ATOM 2078 C C . SER B 2 57 ? 42.978 19.528 0.979 1.00 22.05 ? 57 SER B C 1 ATOM 2079 O O . SER B 2 57 ? 44.072 19.996 1.112 1.00 27.73 ? 57 SER B O 1 ATOM 2080 C CB . SER B 2 57 ? 41.123 20.589 2.216 1.00 27.20 ? 57 SER B CB 1 ATOM 2081 O OG . SER B 2 57 ? 41.830 21.794 2.343 1.00 37.59 ? 57 SER B OG 1 ATOM 2082 N N . ASN B 2 58 ? 42.499 19.107 -0.173 1.00 22.47 ? 58 ASN B N 1 ATOM 2083 C CA . ASN B 2 58 ? 43.227 19.182 -1.404 1.00 22.42 ? 58 ASN B CA 1 ATOM 2084 C C . ASN B 2 58 ? 42.343 19.899 -2.370 1.00 19.54 ? 58 ASN B C 1 ATOM 2085 O O . ASN B 2 58 ? 41.174 19.705 -2.355 1.00 31.13 ? 58 ASN B O 1 ATOM 2086 C CB . ASN B 2 58 ? 43.521 17.781 -1.906 1.00 23.00 ? 58 ASN B CB 1 ATOM 2087 C CG . ASN B 2 58 ? 44.793 17.222 -1.345 1.00 25.78 ? 58 ASN B CG 1 ATOM 2088 O OD1 . ASN B 2 58 ? 44.775 16.242 -0.635 1.00 21.88 ? 58 ASN B OD1 1 ATOM 2089 N ND2 . ASN B 2 58 ? 45.902 17.848 -1.661 1.00 33.66 ? 58 ASN B ND2 1 ATOM 2090 N N . TYR B 2 59 ? 42.907 20.743 -3.202 1.00 18.94 ? 59 TYR B N 1 ATOM 2091 C CA . TYR B 2 59 ? 42.135 21.578 -4.100 1.00 18.52 ? 59 TYR B CA 1 ATOM 2092 C C . TYR B 2 59 ? 42.539 21.371 -5.536 1.00 22.07 ? 59 TYR B C 1 ATOM 2093 O O . TYR B 2 59 ? 43.567 20.801 -5.811 1.00 31.54 ? 59 TYR B O 1 ATOM 2094 C CB . TYR B 2 59 ? 42.321 23.042 -3.768 1.00 17.60 ? 59 TYR B CB 1 ATOM 2095 C CG . TYR B 2 59 ? 41.800 23.464 -2.437 1.00 17.77 ? 59 TYR B CG 1 ATOM 2096 C CD1 . TYR B 2 59 ? 41.093 22.603 -1.651 1.00 26.35 ? 59 TYR B CD1 1 ATOM 2097 C CD2 . TYR B 2 59 ? 42.016 24.723 -1.967 1.00 20.99 ? 59 TYR B CD2 1 ATOM 2098 C CE1 . TYR B 2 59 ? 40.612 22.985 -0.430 1.00 27.06 ? 59 TYR B CE1 1 ATOM 2099 C CE2 . TYR B 2 59 ? 41.538 25.106 -0.749 1.00 22.30 ? 59 TYR B CE2 1 ATOM 2100 C CZ . TYR B 2 59 ? 40.840 24.224 0.005 1.00 21.91 ? 59 TYR B CZ 1 ATOM 2101 O OH . TYR B 2 59 ? 40.366 24.597 1.211 1.00 38.89 ? 59 TYR B OH 1 ATOM 2102 N N . ASN B 2 60 ? 41.683 21.793 -6.448 1.00 22.71 ? 60 ASN B N 1 ATOM 2103 C CA . ASN B 2 60 ? 42.026 21.860 -7.841 1.00 21.05 ? 60 ASN B CA 1 ATOM 2104 C C . ASN B 2 60 ? 43.002 22.978 -8.110 1.00 35.41 ? 60 ASN B C 1 ATOM 2105 O O . ASN B 2 60 ? 42.836 24.082 -7.623 1.00 63.56 ? 60 ASN B O 1 ATOM 2106 C CB . ASN B 2 60 ? 40.783 22.073 -8.670 1.00 23.90 ? 60 ASN B CB 1 ATOM 2107 C CG . ASN B 2 60 ? 41.047 21.955 -10.145 1.00 30.26 ? 60 ASN B CG 1 ATOM 2108 O OD1 . ASN B 2 60 ? 41.402 22.922 -10.800 1.00 27.98 ? 60 ASN B OD1 1 ATOM 2109 N ND2 . ASN B 2 60 ? 40.870 20.770 -10.677 1.00 21.89 ? 60 ASN B ND2 1 ATOM 2110 N N . PRO B 2 61 ? 44.049 22.661 -8.988 1.00 29.36 ? 61 PRO B N 1 ATOM 2111 C CA . PRO B 2 61 ? 45.017 23.755 -9.180 1.00 31.64 ? 61 PRO B CA 1 ATOM 2112 C C . PRO B 2 61 ? 44.487 25.083 -9.720 1.00 42.86 ? 61 PRO B C 1 ATOM 2113 O O . PRO B 2 61 ? 45.010 26.118 -9.345 1.00 36.18 ? 61 PRO B O 1 ATOM 2114 C CB . PRO B 2 61 ? 45.983 23.169 -10.180 1.00 24.23 ? 61 PRO B CB 1 ATOM 2115 C CG . PRO B 2 61 ? 46.086 21.775 -9.759 1.00 21.78 ? 61 PRO B CG 1 ATOM 2116 C CD . PRO B 2 61 ? 44.658 21.433 -9.703 1.00 25.70 ? 61 PRO B CD 1 ATOM 2117 N N . SER B 2 62 ? 43.515 25.045 -10.619 1.00 53.73 ? 62 SER B N 1 ATOM 2118 C CA . SER B 2 62 ? 42.873 26.228 -11.185 1.00 33.65 ? 62 SER B CA 1 ATOM 2119 C C . SER B 2 62 ? 42.150 27.089 -10.173 1.00 33.74 ? 62 SER B C 1 ATOM 2120 O O . SER B 2 62 ? 42.101 28.298 -10.299 1.00 35.01 ? 62 SER B O 1 ATOM 2121 C CB . SER B 2 62 ? 41.842 25.760 -12.171 1.00 36.67 ? 62 SER B CB 1 ATOM 2122 O OG . SER B 2 62 ? 41.117 24.714 -11.583 1.00 30.10 ? 62 SER B OG 1 ATOM 2123 N N . LEU B 2 63 ? 41.512 26.441 -9.214 1.00 34.54 ? 63 LEU B N 1 ATOM 2124 C CA . LEU B 2 63 ? 40.734 27.118 -8.193 1.00 37.41 ? 63 LEU B CA 1 ATOM 2125 C C . LEU B 2 63 ? 41.426 27.196 -6.844 1.00 43.58 ? 63 LEU B C 1 ATOM 2126 O O . LEU B 2 63 ? 40.815 27.552 -5.870 1.00 38.75 ? 63 LEU B O 1 ATOM 2127 C CB . LEU B 2 63 ? 39.379 26.437 -8.012 1.00 40.43 ? 63 LEU B CB 1 ATOM 2128 C CG . LEU B 2 63 ? 38.503 26.048 -9.202 1.00 39.34 ? 63 LEU B CG 1 ATOM 2129 C CD1 . LEU B 2 63 ? 38.578 24.566 -9.424 1.00 30.23 ? 63 LEU B CD1 1 ATOM 2130 C CD2 . LEU B 2 63 ? 37.065 26.447 -8.986 1.00 24.79 ? 63 LEU B CD2 1 ATOM 2131 N N . LYS B 2 64 ? 42.702 26.866 -6.781 1.00 55.25 ? 64 LYS B N 1 ATOM 2132 C CA . LYS B 2 64 ? 43.395 26.729 -5.503 1.00 42.95 ? 64 LYS B CA 1 ATOM 2133 C C . LYS B 2 64 ? 43.375 28.026 -4.706 1.00 51.55 ? 64 LYS B C 1 ATOM 2134 O O . LYS B 2 64 ? 43.325 28.009 -3.490 1.00 43.07 ? 64 LYS B O 1 ATOM 2135 C CB . LYS B 2 64 ? 44.831 26.221 -5.720 1.00 38.47 ? 64 LYS B CB 1 ATOM 2136 C CG . LYS B 2 64 ? 45.774 27.137 -6.498 1.00 48.71 ? 64 LYS B CG 1 ATOM 2137 C CD . LYS B 2 64 ? 47.168 26.577 -6.646 1.00 52.42 ? 64 LYS B CD 1 ATOM 2138 C CE . LYS B 2 64 ? 48.061 27.513 -7.419 1.00 41.85 ? 64 LYS B CE 1 ATOM 2139 N NZ . LYS B 2 64 ? 49.420 26.932 -7.545 1.00 57.81 ? 64 LYS B NZ 1 ATOM 2140 N N . ARG B 2 65 ? 43.488 29.142 -5.411 1.00 62.39 ? 65 ARG B N 1 ATOM 2141 C CA . ARG B 2 65 ? 43.583 30.454 -4.793 1.00 42.68 ? 65 ARG B CA 1 ATOM 2142 C C . ARG B 2 65 ? 42.256 31.135 -4.536 1.00 37.76 ? 65 ARG B C 1 ATOM 2143 O O . ARG B 2 65 ? 42.224 32.221 -3.993 1.00 41.85 ? 65 ARG B O 1 ATOM 2144 C CB . ARG B 2 65 ? 44.485 31.355 -5.614 1.00 74.99 ? 65 ARG B CB 1 ATOM 2145 C CG . ARG B 2 65 ? 45.961 31.172 -5.295 1.00 81.94 ? 65 ARG B CG 1 ATOM 2146 C CD . ARG B 2 65 ? 46.852 31.966 -6.231 1.00 52.95 ? 65 ARG B CD 1 ATOM 2147 N NE . ARG B 2 65 ? 46.613 31.640 -7.632 1.00 73.99 ? 65 ARG B NE 1 ATOM 2148 C CZ . ARG B 2 65 ? 46.256 32.533 -8.547 1.00 82.02 ? 65 ARG B CZ 1 ATOM 2149 N NH1 . ARG B 2 65 ? 46.084 33.795 -8.196 1.00 83.81 ? 65 ARG B NH1 1 ATOM 2150 N NH2 . ARG B 2 65 ? 46.054 32.161 -9.803 1.00 64.29 ? 65 ARG B NH2 1 ATOM 2151 N N . ARG B 2 66 ? 41.161 30.513 -4.938 1.00 35.05 ? 66 ARG B N 1 ATOM 2152 C CA . ARG B 2 66 ? 39.845 31.022 -4.570 1.00 31.71 ? 66 ARG B CA 1 ATOM 2153 C C . ARG B 2 66 ? 38.962 30.087 -3.769 1.00 28.80 ? 66 ARG B C 1 ATOM 2154 O O . ARG B 2 66 ? 37.778 30.282 -3.751 1.00 34.55 ? 66 ARG B O 1 ATOM 2155 C CB . ARG B 2 66 ? 39.071 31.508 -5.785 1.00 39.72 ? 66 ARG B CB 1 ATOM 2156 C CG . ARG B 2 66 ? 38.767 30.450 -6.827 1.00 44.47 ? 66 ARG B CG 1 ATOM 2157 C CD . ARG B 2 66 ? 37.997 31.067 -7.975 1.00 27.87 ? 66 ARG B CD 1 ATOM 2158 N NE . ARG B 2 66 ? 36.695 31.530 -7.540 1.00 25.35 ? 66 ARG B NE 1 ATOM 2159 C CZ . ARG B 2 66 ? 35.859 32.191 -8.312 1.00 26.21 ? 66 ARG B CZ 1 ATOM 2160 N NH1 . ARG B 2 66 ? 36.204 32.479 -9.542 1.00 32.76 ? 66 ARG B NH1 1 ATOM 2161 N NH2 . ARG B 2 66 ? 34.690 32.565 -7.852 1.00 28.80 ? 66 ARG B NH2 1 ATOM 2162 N N . ILE B 2 67 ? 39.515 29.063 -3.141 1.00 28.21 ? 67 ILE B N 1 ATOM 2163 C CA . ILE B 2 67 ? 38.697 28.050 -2.484 1.00 23.67 ? 67 ILE B CA 1 ATOM 2164 C C . ILE B 2 67 ? 38.965 27.902 -1.002 1.00 27.48 ? 67 ILE B C 1 ATOM 2165 O O . ILE B 2 67 ? 40.091 27.921 -0.577 1.00 45.51 ? 67 ILE B O 1 ATOM 2166 C CB . ILE B 2 67 ? 38.955 26.670 -3.092 1.00 23.49 ? 67 ILE B CB 1 ATOM 2167 C CG1 . ILE B 2 67 ? 38.630 26.655 -4.556 1.00 25.83 ? 67 ILE B CG1 1 ATOM 2168 C CG2 . ILE B 2 67 ? 38.065 25.630 -2.476 1.00 32.41 ? 67 ILE B CG2 1 ATOM 2169 C CD1 . ILE B 2 67 ? 39.025 25.361 -5.204 1.00 34.47 ? 67 ILE B CD1 1 ATOM 2170 N N . ASN B 2 68 ? 37.919 27.749 -0.217 1.00 24.96 ? 68 ASN B N 1 ATOM 2171 C CA . ASN B 2 68 ? 38.053 27.237 1.118 1.00 26.20 ? 68 ASN B CA 1 ATOM 2172 C C . ASN B 2 68 ? 37.106 26.076 1.334 1.00 31.86 ? 68 ASN B C 1 ATOM 2173 O O . ASN B 2 68 ? 35.952 26.160 0.992 1.00 33.64 ? 68 ASN B O 1 ATOM 2174 C CB . ASN B 2 68 ? 37.803 28.324 2.142 1.00 29.14 ? 68 ASN B CB 1 ATOM 2175 C CG . ASN B 2 68 ? 37.673 27.789 3.547 1.00 30.82 ? 68 ASN B CG 1 ATOM 2176 O OD1 . ASN B 2 68 ? 36.654 27.965 4.189 1.00 32.93 ? 68 ASN B OD1 1 ATOM 2177 N ND2 . ASN B 2 68 ? 38.710 27.146 4.032 1.00 42.06 ? 68 ASN B ND2 1 ATOM 2178 N N . ILE B 2 69 ? 37.611 24.995 1.910 1.00 40.04 ? 69 ILE B N 1 ATOM 2179 C CA . ILE B 2 69 ? 36.792 23.843 2.260 1.00 25.14 ? 69 ILE B CA 1 ATOM 2180 C C . ILE B 2 69 ? 37.070 23.422 3.699 1.00 28.00 ? 69 ILE B C 1 ATOM 2181 O O . ILE B 2 69 ? 38.223 23.262 4.098 1.00 32.31 ? 69 ILE B O 1 ATOM 2182 C CB . ILE B 2 69 ? 37.046 22.656 1.311 1.00 18.53 ? 69 ILE B CB 1 ATOM 2183 C CG1 . ILE B 2 69 ? 36.812 23.076 -0.141 1.00 18.46 ? 69 ILE B CG1 1 ATOM 2184 C CG2 . ILE B 2 69 ? 36.153 21.484 1.672 1.00 16.48 ? 69 ILE B CG2 1 ATOM 2185 C CD1 . ILE B 2 69 ? 36.966 21.952 -1.141 1.00 15.91 ? 69 ILE B CD1 1 ATOM 2186 N N . SER B 2 70 ? 36.007 23.249 4.477 1.00 21.08 ? 70 SER B N 1 ATOM 2187 C CA . SER B 2 70 ? 36.143 22.913 5.888 1.00 17.44 ? 70 SER B CA 1 ATOM 2188 C C . SER B 2 70 ? 35.236 21.755 6.285 1.00 17.71 ? 70 SER B C 1 ATOM 2189 O O . SER B 2 70 ? 34.302 21.413 5.562 1.00 17.59 ? 70 SER B O 1 ATOM 2190 C CB . SER B 2 70 ? 35.836 24.137 6.751 1.00 17.02 ? 70 SER B CB 1 ATOM 2191 O OG . SER B 2 70 ? 34.575 24.688 6.414 1.00 19.80 ? 70 SER B OG 1 ATOM 2192 N N . ILE B 2 71 ? 35.519 21.153 7.436 1.00 22.81 ? 71 ILE B N 1 ATOM 2193 C CA . ILE B 2 71 ? 34.680 20.087 7.972 1.00 19.95 ? 71 ILE B CA 1 ATOM 2194 C C . ILE B 2 71 ? 34.315 20.347 9.429 1.00 22.59 ? 71 ILE B C 1 ATOM 2195 O O . ILE B 2 71 ? 35.184 20.598 10.265 1.00 37.66 ? 71 ILE B O 1 ATOM 2196 C CB . ILE B 2 71 ? 35.366 18.707 7.863 1.00 22.48 ? 71 ILE B CB 1 ATOM 2197 C CG1 . ILE B 2 71 ? 35.243 18.172 6.436 1.00 36.95 ? 71 ILE B CG1 1 ATOM 2198 C CG2 . ILE B 2 71 ? 34.757 17.720 8.850 1.00 35.13 ? 71 ILE B CG2 1 ATOM 2199 C CD1 . ILE B 2 71 ? 35.102 16.664 6.337 1.00 20.07 ? 71 ILE B CD1 1 ATOM 2200 N N . ASP B 2 72 ? 33.031 20.342 9.724 1.00 21.62 ? 72 ASP B N 1 ATOM 2201 C CA . ASP B 2 72 ? 32.605 20.498 11.088 1.00 23.06 ? 72 ASP B CA 1 ATOM 2202 C C . ASP B 2 72 ? 32.169 19.145 11.541 1.00 24.93 ? 72 ASP B C 1 ATOM 2203 O O . ASP B 2 72 ? 31.065 18.748 11.323 1.00 27.36 ? 72 ASP B O 1 ATOM 2204 C CB . ASP B 2 72 ? 31.469 21.508 11.129 1.00 26.59 ? 72 ASP B CB 1 ATOM 2205 C CG . ASP B 2 72 ? 30.646 21.418 12.359 1.00 40.03 ? 72 ASP B CG 1 ATOM 2206 O OD1 . ASP B 2 72 ? 29.688 20.646 12.335 1.00 39.74 ? 72 ASP B OD1 1 ATOM 2207 O OD2 . ASP B 2 72 ? 30.926 22.138 13.334 1.00 63.16 ? 72 ASP B OD2 1 ATOM 2208 N N . THR B 2 73 ? 33.069 18.452 12.206 1.00 25.01 ? 73 THR B N 1 ATOM 2209 C CA . THR B 2 73 ? 32.899 17.058 12.529 1.00 24.21 ? 73 THR B CA 1 ATOM 2210 C C . THR B 2 73 ? 31.870 16.802 13.594 1.00 28.93 ? 73 THR B C 1 ATOM 2211 O O . THR B 2 73 ? 31.422 15.683 13.768 1.00 43.49 ? 73 THR B O 1 ATOM 2212 C CB . THR B 2 73 ? 34.226 16.407 12.886 1.00 27.02 ? 73 THR B CB 1 ATOM 2213 O OG1 . THR B 2 73 ? 34.814 17.118 13.966 1.00 50.80 ? 73 THR B OG1 1 ATOM 2214 C CG2 . THR B 2 73 ? 35.150 16.479 11.730 1.00 22.78 ? 73 THR B CG2 1 ATOM 2215 N N . SER B 2 74 ? 31.555 17.822 14.368 1.00 28.97 ? 74 SER B N 1 ATOM 2216 C CA . SER B 2 74 ? 30.469 17.709 15.306 1.00 36.09 ? 74 SER B CA 1 ATOM 2217 C C . SER B 2 74 ? 29.132 17.532 14.612 1.00 30.80 ? 74 SER B C 1 ATOM 2218 O O . SER B 2 74 ? 28.354 16.691 14.994 1.00 54.36 ? 74 SER B O 1 ATOM 2219 C CB . SER B 2 74 ? 30.432 18.927 16.205 1.00 33.46 ? 74 SER B CB 1 ATOM 2220 O OG . SER B 2 74 ? 30.628 20.101 15.451 1.00 64.10 ? 74 SER B OG 1 ATOM 2221 N N . LYS B 2 75 ? 28.877 18.313 13.573 1.00 28.93 ? 75 LYS B N 1 ATOM 2222 C CA . LYS B 2 75 ? 27.620 18.225 12.847 1.00 26.05 ? 75 LYS B CA 1 ATOM 2223 C C . LYS B 2 75 ? 27.690 17.248 11.704 1.00 28.01 ? 75 LYS B C 1 ATOM 2224 O O . LYS B 2 75 ? 26.688 16.970 11.093 1.00 26.41 ? 75 LYS B O 1 ATOM 2225 C CB . LYS B 2 75 ? 27.211 19.568 12.278 1.00 23.20 ? 75 LYS B CB 1 ATOM 2226 C CG . LYS B 2 75 ? 27.146 20.707 13.252 1.00 38.96 ? 75 LYS B CG 1 ATOM 2227 C CD . LYS B 2 75 ? 26.273 21.801 12.692 1.00 30.99 ? 75 LYS B CD 1 ATOM 2228 C CE . LYS B 2 75 ? 26.130 22.960 13.654 1.00 67.84 ? 75 LYS B CE 1 ATOM 2229 N NZ . LYS B 2 75 ? 24.785 23.592 13.602 1.00 47.26 ? 75 LYS B NZ 1 ATOM 2230 N N . LYS B 2 76 ? 28.867 16.708 11.435 1.00 21.49 ? 76 LYS B N 1 ATOM 2231 C CA . LYS B 2 76 ? 29.051 15.826 10.312 1.00 19.90 ? 76 LYS B CA 1 ATOM 2232 C C . LYS B 2 76 ? 28.717 16.492 8.992 1.00 21.80 ? 76 LYS B C 1 ATOM 2233 O O . LYS B 2 76 ? 28.082 15.906 8.140 1.00 24.21 ? 76 LYS B O 1 ATOM 2234 C CB . LYS B 2 76 ? 28.209 14.591 10.499 1.00 22.86 ? 76 LYS B CB 1 ATOM 2235 C CG . LYS B 2 76 ? 28.994 13.373 10.925 1.00 46.36 ? 76 LYS B CG 1 ATOM 2236 C CD . LYS B 2 76 ? 28.719 12.997 12.361 1.00 31.70 ? 76 LYS B CD 1 ATOM 2237 C CE . LYS B 2 76 ? 27.903 11.727 12.424 1.00 34.70 ? 76 LYS B CE 1 ATOM 2238 N NZ . LYS B 2 76 ? 28.680 10.592 11.884 1.00 33.59 ? 76 LYS B NZ 1 ATOM 2239 N N . GLN B 2 77 ? 29.174 17.731 8.847 1.00 21.11 ? 77 GLN B N 1 ATOM 2240 C CA . GLN B 2 77 ? 28.943 18.542 7.676 1.00 16.23 ? 77 GLN B CA 1 ATOM 2241 C C . GLN B 2 77 ? 30.266 19.010 7.136 1.00 18.21 ? 77 GLN B C 1 ATOM 2242 O O . GLN B 2 77 ? 31.182 19.149 7.893 1.00 30.48 ? 77 GLN B O 1 ATOM 2243 C CB . GLN B 2 77 ? 28.138 19.773 8.058 1.00 15.74 ? 77 GLN B CB 1 ATOM 2244 C CG . GLN B 2 77 ? 26.761 19.500 8.615 1.00 15.42 ? 77 GLN B CG 1 ATOM 2245 C CD . GLN B 2 77 ? 26.045 20.757 8.991 1.00 13.27 ? 77 GLN B CD 1 ATOM 2246 O OE1 . GLN B 2 77 ? 26.500 21.828 8.693 1.00 12.83 ? 77 GLN B OE1 1 ATOM 2247 N NE2 . GLN B 2 77 ? 24.930 20.630 9.660 1.00 17.22 ? 77 GLN B NE2 1 ATOM 2248 N N . PHE B 2 78 ? 30.357 19.256 5.828 1.00 22.12 ? 78 PHE B N 1 ATOM 2249 C CA . PHE B 2 78 ? 31.512 19.894 5.206 1.00 17.95 ? 78 PHE B CA 1 ATOM 2250 C C . PHE B 2 78 ? 31.059 20.974 4.230 1.00 16.04 ? 78 PHE B C 1 ATOM 2251 O O . PHE B 2 78 ? 30.084 20.798 3.501 1.00 30.40 ? 78 PHE B O 1 ATOM 2252 C CB . PHE B 2 78 ? 32.408 18.863 4.508 1.00 17.57 ? 78 PHE B CB 1 ATOM 2253 C CG . PHE B 2 78 ? 31.754 18.143 3.363 1.00 18.90 ? 78 PHE B CG 1 ATOM 2254 C CD1 . PHE B 2 78 ? 30.887 17.089 3.592 1.00 19.24 ? 78 PHE B CD1 1 ATOM 2255 C CD2 . PHE B 2 78 ? 32.038 18.497 2.055 1.00 24.76 ? 78 PHE B CD2 1 ATOM 2256 C CE1 . PHE B 2 78 ? 30.297 16.419 2.537 1.00 26.48 ? 78 PHE B CE1 1 ATOM 2257 C CE2 . PHE B 2 78 ? 31.452 17.830 0.997 1.00 16.51 ? 78 PHE B CE2 1 ATOM 2258 C CZ . PHE B 2 78 ? 30.581 16.790 1.239 1.00 17.31 ? 78 PHE B CZ 1 ATOM 2259 N N . SER B 2 79 ? 31.771 22.097 4.232 1.00 16.58 ? 79 SER B N 1 ATOM 2260 C CA . SER B 2 79 ? 31.336 23.278 3.498 1.00 17.55 ? 79 SER B CA 1 ATOM 2261 C C . SER B 2 79 ? 32.284 23.658 2.366 1.00 15.06 ? 79 SER B C 1 ATOM 2262 O O . SER B 2 79 ? 33.419 23.186 2.304 1.00 19.77 ? 79 SER B O 1 ATOM 2263 C CB . SER B 2 79 ? 31.180 24.460 4.456 1.00 34.19 ? 79 SER B CB 1 ATOM 2264 O OG . SER B 2 79 ? 30.267 24.154 5.496 1.00 46.60 ? 79 SER B OG 1 ATOM 2265 N N . LEU B 2 80 ? 31.803 24.523 1.479 1.00 15.67 ? 80 LEU B N 1 ATOM 2266 C CA . LEU B 2 80 ? 32.570 24.965 0.320 1.00 15.27 ? 80 LEU B CA 1 ATOM 2267 C C . LEU B 2 80 ? 32.386 26.464 0.114 1.00 15.21 ? 80 LEU B C 1 ATOM 2268 O O . LEU B 2 80 ? 31.260 26.962 0.109 1.00 16.18 ? 80 LEU B O 1 ATOM 2269 C CB . LEU B 2 80 ? 32.141 24.188 -0.931 1.00 12.63 ? 80 LEU B CB 1 ATOM 2270 C CG . LEU B 2 80 ? 32.811 24.422 -2.292 1.00 12.66 ? 80 LEU B CG 1 ATOM 2271 C CD1 . LEU B 2 80 ? 32.132 25.536 -3.078 1.00 10.51 ? 80 LEU B CD1 1 ATOM 2272 C CD2 . LEU B 2 80 ? 34.297 24.707 -2.140 1.00 20.91 ? 80 LEU B CD2 1 ATOM 2273 N N . LYS B 2 81 ? 33.492 27.180 -0.055 1.00 18.73 ? 81 LYS B N 1 ATOM 2274 C CA . LYS B 2 81 ? 33.428 28.613 -0.313 1.00 18.23 ? 81 LYS B CA 1 ATOM 2275 C C . LYS B 2 81 ? 34.207 29.003 -1.566 1.00 17.49 ? 81 LYS B C 1 ATOM 2276 O O . LYS B 2 81 ? 35.341 28.569 -1.767 1.00 28.14 ? 81 LYS B O 1 ATOM 2277 C CB . LYS B 2 81 ? 33.944 29.400 0.895 1.00 23.92 ? 81 LYS B CB 1 ATOM 2278 C CG . LYS B 2 81 ? 32.989 29.395 2.081 1.00 39.43 ? 81 LYS B CG 1 ATOM 2279 C CD . LYS B 2 81 ? 33.375 30.438 3.118 1.00 44.55 ? 81 LYS B CD 1 ATOM 2280 C CE . LYS B 2 81 ? 34.710 30.113 3.763 1.00 68.60 ? 81 LYS B CE 1 ATOM 2281 N NZ . LYS B 2 81 ? 35.138 31.171 4.723 1.00 68.45 ? 81 LYS B NZ 1 ATOM 2282 N N . LEU B 2 82 ? 33.581 29.821 -2.408 1.00 18.03 ? 82 LEU B N 1 ATOM 2283 C CA . LEU B 2 82 ? 34.210 30.309 -3.629 1.00 18.63 ? 82 LEU B CA 1 ATOM 2284 C C . LEU B 2 82 ? 34.182 31.835 -3.659 1.00 19.76 ? 82 LEU B C 1 ATOM 2285 O O . LEU B 2 82 ? 33.113 32.442 -3.725 1.00 23.55 ? 82 LEU B O 1 ATOM 2286 C CB . LEU B 2 82 ? 33.507 29.735 -4.860 1.00 20.72 ? 82 LEU B CB 1 ATOM 2287 C CG . LEU B 2 82 ? 34.195 29.927 -6.213 1.00 25.41 ? 82 LEU B CG 1 ATOM 2288 C CD1 . LEU B 2 82 ? 35.537 29.215 -6.237 1.00 22.27 ? 82 LEU B CD1 1 ATOM 2289 C CD2 . LEU B 2 82 ? 33.304 29.429 -7.340 1.00 23.85 ? 82 LEU B CD2 1 ATOM 2290 N N . TYR B 2 83 A 35.361 32.448 -3.613 1.00 27.32 ? 82 TYR B N 1 ATOM 2291 C CA . TYR B 2 83 A 35.474 33.900 -3.498 1.00 32.25 ? 82 TYR B CA 1 ATOM 2292 C C . TYR B 2 83 A 35.501 34.597 -4.854 1.00 24.27 ? 82 TYR B C 1 ATOM 2293 O O . TYR B 2 83 A 35.856 33.989 -5.866 1.00 26.03 ? 82 TYR B O 1 ATOM 2294 C CB . TYR B 2 83 A 36.730 34.271 -2.708 1.00 26.82 ? 82 TYR B CB 1 ATOM 2295 C CG . TYR B 2 83 A 36.796 33.644 -1.334 1.00 25.47 ? 82 TYR B CG 1 ATOM 2296 C CD1 . TYR B 2 83 A 36.228 34.273 -0.235 1.00 33.65 ? 82 TYR B CD1 1 ATOM 2297 C CD2 . TYR B 2 83 A 37.429 32.424 -1.137 1.00 27.18 ? 82 TYR B CD2 1 ATOM 2298 C CE1 . TYR B 2 83 A 36.284 33.705 1.023 1.00 30.06 ? 82 TYR B CE1 1 ATOM 2299 C CE2 . TYR B 2 83 A 37.490 31.848 0.118 1.00 48.04 ? 82 TYR B CE2 1 ATOM 2300 C CZ . TYR B 2 83 A 36.916 32.494 1.194 1.00 39.96 ? 82 TYR B CZ 1 ATOM 2301 O OH . TYR B 2 83 A 36.975 31.927 2.446 1.00 30.63 ? 82 TYR B OH 1 ATOM 2302 N N . SER B 2 84 B 35.139 35.880 -4.851 1.00 26.45 ? 82 SER B N 1 ATOM 2303 C CA . SER B 2 84 B 35.098 36.707 -6.058 1.00 31.28 ? 82 SER B CA 1 ATOM 2304 C C . SER B 2 84 B 34.337 36.014 -7.180 1.00 39.73 ? 82 SER B C 1 ATOM 2305 O O . SER B 2 84 B 34.860 35.838 -8.280 1.00 43.19 ? 82 SER B O 1 ATOM 2306 C CB . SER B 2 84 B 36.515 37.058 -6.522 1.00 59.86 ? 82 SER B CB 1 ATOM 2307 O OG . SER B 2 84 B 37.209 35.911 -6.981 1.00 64.33 ? 82 SER B OG 1 ATOM 2308 N N . VAL B 2 85 C 33.100 35.624 -6.890 1.00 44.36 ? 82 VAL B N 1 ATOM 2309 C CA . VAL B 2 85 C 32.311 34.818 -7.812 1.00 27.41 ? 82 VAL B CA 1 ATOM 2310 C C . VAL B 2 85 C 32.012 35.573 -9.108 1.00 25.18 ? 82 VAL B C 1 ATOM 2311 O O . VAL B 2 85 C 31.976 36.805 -9.134 1.00 24.30 ? 82 VAL B O 1 ATOM 2312 C CB . VAL B 2 85 C 30.988 34.357 -7.154 1.00 23.93 ? 82 VAL B CB 1 ATOM 2313 C CG1 . VAL B 2 85 C 29.915 35.430 -7.271 1.00 36.01 ? 82 VAL B CG1 1 ATOM 2314 C CG2 . VAL B 2 85 C 30.513 33.055 -7.772 1.00 25.71 ? 82 VAL B CG2 1 ATOM 2315 N N . THR B 2 86 ? 31.828 34.819 -10.186 1.00 29.55 ? 83 THR B N 1 ATOM 2316 C CA . THR B 2 86 ? 31.528 35.387 -11.494 1.00 30.12 ? 83 THR B CA 1 ATOM 2317 C C . THR B 2 86 ? 30.510 34.497 -12.201 1.00 33.05 ? 83 THR B C 1 ATOM 2318 O O . THR B 2 86 ? 30.224 33.393 -11.740 1.00 42.81 ? 83 THR B O 1 ATOM 2319 C CB . THR B 2 86 ? 32.798 35.523 -12.360 1.00 24.44 ? 83 THR B CB 1 ATOM 2320 O OG1 . THR B 2 86 ? 33.934 35.751 -11.516 1.00 45.82 ? 83 THR B OG1 1 ATOM 2321 C CG2 . THR B 2 86 ? 32.663 36.678 -13.340 1.00 25.94 ? 83 THR B CG2 1 ATOM 2322 N N . ALA B 2 87 ? 29.966 34.976 -13.316 1.00 23.80 ? 84 ALA B N 1 ATOM 2323 C CA . ALA B 2 87 ? 28.979 34.216 -14.077 1.00 18.50 ? 84 ALA B CA 1 ATOM 2324 C C . ALA B 2 87 ? 29.565 32.903 -14.590 1.00 14.90 ? 84 ALA B C 1 ATOM 2325 O O . ALA B 2 87 ? 28.832 31.958 -14.878 1.00 18.77 ? 84 ALA B O 1 ATOM 2326 C CB . ALA B 2 87 ? 28.450 35.045 -15.232 1.00 16.36 ? 84 ALA B CB 1 ATOM 2327 N N . ALA B 2 88 ? 30.888 32.851 -14.697 1.00 16.48 ? 85 ALA B N 1 ATOM 2328 C CA . ALA B 2 88 ? 31.578 31.639 -15.121 1.00 17.26 ? 85 ALA B CA 1 ATOM 2329 C C . ALA B 2 88 ? 31.519 30.568 -14.037 1.00 22.93 ? 85 ALA B C 1 ATOM 2330 O O . ALA B 2 88 ? 31.815 29.400 -14.291 1.00 35.89 ? 85 ALA B O 1 ATOM 2331 C CB . ALA B 2 88 ? 33.022 31.949 -15.479 1.00 17.74 ? 85 ALA B CB 1 ATOM 2332 N N . ASP B 2 89 ? 31.141 30.971 -12.828 1.00 19.81 ? 86 ASP B N 1 ATOM 2333 C CA . ASP B 2 89 ? 31.024 30.038 -11.715 1.00 19.57 ? 86 ASP B CA 1 ATOM 2334 C C . ASP B 2 89 ? 29.591 29.535 -11.567 1.00 16.50 ? 86 ASP B C 1 ATOM 2335 O O . ASP B 2 89 ? 29.275 28.801 -10.630 1.00 20.42 ? 86 ASP B O 1 ATOM 2336 C CB . ASP B 2 89 ? 31.489 30.693 -10.412 1.00 19.51 ? 86 ASP B CB 1 ATOM 2337 C CG . ASP B 2 89 ? 32.876 31.296 -10.523 1.00 21.31 ? 86 ASP B CG 1 ATOM 2338 O OD1 . ASP B 2 89 ? 33.866 30.539 -10.444 1.00 35.25 ? 86 ASP B OD1 1 ATOM 2339 O OD2 . ASP B 2 89 ? 32.977 32.530 -10.682 1.00 21.92 ? 86 ASP B OD2 1 ATOM 2340 N N . THR B 2 90 ? 28.725 29.938 -12.493 1.00 22.96 ? 87 THR B N 1 ATOM 2341 C CA . THR B 2 90 ? 27.338 29.491 -12.485 1.00 16.73 ? 87 THR B CA 1 ATOM 2342 C C . THR B 2 90 ? 27.247 28.037 -12.927 1.00 13.47 ? 87 THR B C 1 ATOM 2343 O O . THR B 2 90 ? 27.518 27.714 -14.085 1.00 13.07 ? 87 THR B O 1 ATOM 2344 C CB . THR B 2 90 ? 26.454 30.357 -13.402 1.00 16.50 ? 87 THR B CB 1 ATOM 2345 O OG1 . THR B 2 90 ? 26.391 31.693 -12.888 1.00 26.66 ? 87 THR B OG1 1 ATOM 2346 C CG2 . THR B 2 90 ? 25.047 29.788 -13.481 1.00 40.03 ? 87 THR B CG2 1 ATOM 2347 N N . ALA B 2 91 ? 26.866 27.165 -11.998 1.00 10.19 ? 88 ALA B N 1 ATOM 2348 C CA . ALA B 2 91 ? 26.769 25.735 -12.270 1.00 12.16 ? 88 ALA B CA 1 ATOM 2349 C C . ALA B 2 91 ? 25.963 25.026 -11.188 1.00 11.59 ? 88 ALA B C 1 ATOM 2350 O O . ALA B 2 91 ? 25.486 25.658 -10.245 1.00 20.29 ? 88 ALA B O 1 ATOM 2351 C CB . ALA B 2 91 ? 28.157 25.123 -12.380 1.00 18.67 ? 88 ALA B CB 1 ATOM 2352 N N . VAL B 2 92 ? 25.812 23.713 -11.330 1.00 11.46 ? 89 VAL B N 1 ATOM 2353 C CA . VAL B 2 92 ? 25.142 22.909 -10.315 1.00 13.77 ? 89 VAL B CA 1 ATOM 2354 C C . VAL B 2 92 ? 26.180 22.204 -9.453 1.00 14.98 ? 89 VAL B C 1 ATOM 2355 O O . VAL B 2 92 ? 26.917 21.344 -9.933 1.00 27.55 ? 89 VAL B O 1 ATOM 2356 C CB . VAL B 2 92 ? 24.201 21.862 -10.937 1.00 10.95 ? 89 VAL B CB 1 ATOM 2357 C CG1 . VAL B 2 92 ? 23.483 21.090 -9.845 1.00 11.19 ? 89 VAL B CG1 1 ATOM 2358 C CG2 . VAL B 2 92 ? 23.196 22.529 -11.854 1.00 12.48 ? 89 VAL B CG2 1 ATOM 2359 N N . TYR B 2 93 ? 26.232 22.572 -8.178 1.00 28.58 ? 90 TYR B N 1 ATOM 2360 C CA . TYR B 2 93 ? 27.258 22.062 -7.276 1.00 17.38 ? 90 TYR B CA 1 ATOM 2361 C C . TYR B 2 93 ? 26.777 20.830 -6.516 1.00 14.82 ? 90 TYR B C 1 ATOM 2362 O O . TYR B 2 93 ? 25.688 20.830 -5.942 1.00 25.75 ? 90 TYR B O 1 ATOM 2363 C CB . TYR B 2 93 ? 27.691 23.159 -6.303 1.00 14.94 ? 90 TYR B CB 1 ATOM 2364 C CG . TYR B 2 93 ? 28.331 24.351 -6.984 1.00 18.14 ? 90 TYR B CG 1 ATOM 2365 C CD1 . TYR B 2 93 ? 27.555 25.321 -7.608 1.00 10.76 ? 90 TYR B CD1 1 ATOM 2366 C CD2 . TYR B 2 93 ? 29.711 24.507 -7.003 1.00 10.18 ? 90 TYR B CD2 1 ATOM 2367 C CE1 . TYR B 2 93 ? 28.135 26.408 -8.232 1.00 11.98 ? 90 TYR B CE1 1 ATOM 2368 C CE2 . TYR B 2 93 ? 30.299 25.594 -7.624 1.00 9.39 ? 90 TYR B CE2 1 ATOM 2369 C CZ . TYR B 2 93 ? 29.506 26.540 -8.237 1.00 10.91 ? 90 TYR B CZ 1 ATOM 2370 O OH . TYR B 2 93 ? 30.088 27.622 -8.856 1.00 15.85 ? 90 TYR B OH 1 ATOM 2371 N N . TYR B 2 94 ? 27.598 19.784 -6.512 1.00 13.81 ? 91 TYR B N 1 ATOM 2372 C CA . TYR B 2 94 ? 27.206 18.501 -5.937 1.00 15.80 ? 91 TYR B CA 1 ATOM 2373 C C . TYR B 2 94 ? 28.067 18.073 -4.753 1.00 15.43 ? 91 TYR B C 1 ATOM 2374 O O . TYR B 2 94 ? 29.282 18.269 -4.751 1.00 27.23 ? 91 TYR B O 1 ATOM 2375 C CB . TYR B 2 94 ? 27.260 17.406 -7.006 1.00 17.91 ? 91 TYR B CB 1 ATOM 2376 C CG . TYR B 2 94 ? 26.226 17.540 -8.098 1.00 17.78 ? 91 TYR B CG 1 ATOM 2377 C CD1 . TYR B 2 94 ? 24.907 17.169 -7.877 1.00 13.69 ? 91 TYR B CD1 1 ATOM 2378 C CD2 . TYR B 2 94 ? 26.571 18.020 -9.354 1.00 16.71 ? 91 TYR B CD2 1 ATOM 2379 C CE1 . TYR B 2 94 ? 23.958 17.284 -8.872 1.00 15.48 ? 91 TYR B CE1 1 ATOM 2380 C CE2 . TYR B 2 94 ? 25.628 18.138 -10.356 1.00 14.33 ? 91 TYR B CE2 1 ATOM 2381 C CZ . TYR B 2 94 ? 24.323 17.766 -10.109 1.00 17.85 ? 91 TYR B CZ 1 ATOM 2382 O OH . TYR B 2 94 ? 23.376 17.880 -11.101 1.00 46.63 ? 91 TYR B OH 1 ATOM 2383 N N . CYS B 2 95 ? 27.425 17.485 -3.749 1.00 15.12 ? 92 CYS B N 1 ATOM 2384 C CA . CYS B 2 95 ? 28.135 16.762 -2.701 1.00 13.81 ? 92 CYS B CA 1 ATOM 2385 C C . CYS B 2 95 ? 28.436 15.355 -3.199 1.00 13.20 ? 92 CYS B C 1 ATOM 2386 O O . CYS B 2 95 ? 27.721 14.833 -4.053 1.00 17.17 ? 92 CYS B O 1 ATOM 2387 C CB . CYS B 2 95 ? 27.313 16.704 -1.413 1.00 16.78 ? 92 CYS B CB 1 ATOM 2388 S SG . CYS B 2 95 ? 27.350 18.196 -0.405 1.00 58.87 ? 92 CYS B SG 1 ATOM 2389 N N . ALA B 2 96 ? 29.487 14.740 -2.666 1.00 11.37 ? 93 ALA B N 1 ATOM 2390 C CA . ALA B 2 96 ? 29.851 13.389 -3.076 1.00 10.14 ? 93 ALA B CA 1 ATOM 2391 C C . ALA B 2 96 ? 30.730 12.700 -2.042 1.00 11.46 ? 93 ALA B C 1 ATOM 2392 O O . ALA B 2 96 ? 31.444 13.356 -1.284 1.00 16.50 ? 93 ALA B O 1 ATOM 2393 C CB . ALA B 2 96 ? 30.553 13.419 -4.423 1.00 15.85 ? 93 ALA B CB 1 ATOM 2394 N N . ARG B 2 97 ? 30.669 11.373 -2.016 1.00 12.68 ? 94 ARG B N 1 ATOM 2395 C CA . ARG B 2 97 ? 31.537 10.582 -1.153 1.00 14.45 ? 94 ARG B CA 1 ATOM 2396 C C . ARG B 2 97 ? 32.741 10.086 -1.946 1.00 15.23 ? 94 ARG B C 1 ATOM 2397 O O . ARG B 2 97 ? 32.592 9.320 -2.898 1.00 21.38 ? 94 ARG B O 1 ATOM 2398 C CB . ARG B 2 97 ? 30.771 9.403 -0.548 1.00 16.54 ? 94 ARG B CB 1 ATOM 2399 C CG . ARG B 2 97 ? 31.584 8.577 0.437 1.00 15.63 ? 94 ARG B CG 1 ATOM 2400 C CD . ARG B 2 97 ? 30.785 7.401 0.978 1.00 16.34 ? 94 ARG B CD 1 ATOM 2401 N NE . ARG B 2 97 ? 30.425 6.455 -0.073 1.00 22.18 ? 94 ARG B NE 1 ATOM 2402 C CZ . ARG B 2 97 ? 29.843 5.281 0.146 1.00 19.79 ? 94 ARG B CZ 1 ATOM 2403 N NH1 . ARG B 2 97 ? 29.557 4.900 1.384 1.00 21.68 ? 94 ARG B NH1 1 ATOM 2404 N NH2 . ARG B 2 97 ? 29.551 4.484 -0.873 1.00 29.21 ? 94 ARG B NH2 1 ATOM 2405 N N . GLY B 2 98 ? 33.930 10.529 -1.550 1.00 17.62 ? 95 GLY B N 1 ATOM 2406 C CA . GLY B 2 98 ? 35.146 10.197 -2.272 1.00 14.45 ? 95 GLY B CA 1 ATOM 2407 C C . GLY B 2 98 ? 35.767 8.874 -1.868 1.00 13.81 ? 95 GLY B C 1 ATOM 2408 O O . GLY B 2 98 ? 35.069 7.874 -1.698 1.00 13.30 ? 95 GLY B O 1 ATOM 2409 N N . GLY B 2 99 ? 37.087 8.876 -1.715 1.00 18.39 ? 96 GLY B N 1 ATOM 2410 C CA . GLY B 2 99 ? 37.836 7.669 -1.415 1.00 21.68 ? 96 GLY B CA 1 ATOM 2411 C C . GLY B 2 99 ? 37.528 7.059 -0.063 1.00 20.24 ? 96 GLY B C 1 ATOM 2412 O O . GLY B 2 99 ? 36.947 7.708 0.805 1.00 18.18 ? 96 GLY B O 1 ATOM 2413 N N . ARG B 2 100 ? 37.924 5.801 0.111 1.00 23.46 ? 97 ARG B N 1 ATOM 2414 C CA . ARG B 2 100 ? 37.680 5.076 1.352 1.00 22.05 ? 97 ARG B CA 1 ATOM 2415 C C . ARG B 2 100 ? 38.931 5.041 2.222 1.00 26.47 ? 97 ARG B C 1 ATOM 2416 O O . ARG B 2 100 ? 40.032 4.806 1.723 1.00 23.53 ? 97 ARG B O 1 ATOM 2417 C CB . ARG B 2 100 ? 37.218 3.648 1.057 1.00 16.36 ? 97 ARG B CB 1 ATOM 2418 C CG . ARG B 2 100 ? 36.169 3.545 -0.036 1.00 23.99 ? 97 ARG B CG 1 ATOM 2419 C CD . ARG B 2 100 ? 35.771 2.100 -0.285 1.00 42.53 ? 97 ARG B CD 1 ATOM 2420 N NE . ARG B 2 100 ? 35.127 1.500 0.879 1.00 35.22 ? 97 ARG B NE 1 ATOM 2421 C CZ . ARG B 2 100 ? 33.816 1.515 1.097 1.00 43.72 ? 97 ARG B CZ 1 ATOM 2422 N NH1 . ARG B 2 100 ? 33.003 2.100 0.227 1.00 28.38 ? 97 ARG B NH1 1 ATOM 2423 N NH2 . ARG B 2 100 ? 33.317 0.944 2.185 1.00 50.23 ? 97 ARG B NH2 1 ATOM 2424 N N . LYS B 2 101 ? 38.803 5.194 3.527 1.00 26.12 ? 98 LYS B N 1 ATOM 2425 C CA . LYS B 2 101 ? 40.002 5.102 4.321 1.00 27.30 ? 98 LYS B CA 1 ATOM 2426 C C . LYS B 2 101 ? 40.433 3.656 4.357 1.00 26.35 ? 98 LYS B C 1 ATOM 2427 O O . LYS B 2 101 ? 39.670 2.790 4.730 1.00 24.32 ? 98 LYS B O 1 ATOM 2428 C CB . LYS B 2 101 ? 39.742 5.603 5.725 1.00 37.51 ? 98 LYS B CB 1 ATOM 2429 C CG . LYS B 2 101 ? 40.947 5.516 6.626 1.00 35.68 ? 98 LYS B CG 1 ATOM 2430 C CD . LYS B 2 101 ? 42.069 6.375 6.103 1.00 33.21 ? 98 LYS B CD 1 ATOM 2431 C CE . LYS B 2 101 ? 43.222 6.433 7.080 1.00 64.23 ? 98 LYS B CE 1 ATOM 2432 N NZ . LYS B 2 101 ? 44.456 7.085 6.558 1.00 35.75 ? 98 LYS B NZ 1 ATOM 2433 N N . VAL B 2 102 ? 41.673 3.405 3.974 1.00 29.21 ? 99 VAL B N 1 ATOM 2434 C CA . VAL B 2 102 ? 42.233 2.073 4.002 1.00 30.64 ? 99 VAL B CA 1 ATOM 2435 C C . VAL B 2 102 ? 43.526 2.143 4.788 1.00 36.98 ? 99 VAL B C 1 ATOM 2436 O O . VAL B 2 102 ? 44.393 2.944 4.486 1.00 40.75 ? 99 VAL B O 1 ATOM 2437 C CB . VAL B 2 102 ? 42.426 1.519 2.569 1.00 33.44 ? 99 VAL B CB 1 ATOM 2438 C CG1 . VAL B 2 102 ? 43.501 0.450 2.497 1.00 35.51 ? 99 VAL B CG1 1 ATOM 2439 C CG2 . VAL B 2 102 ? 41.112 0.969 2.035 1.00 26.79 ? 99 VAL B CG2 1 ATOM 2440 N N . TYR B 2 103 ? 43.645 1.291 5.794 1.00 41.70 ? 100 TYR B N 1 ATOM 2441 C CA . TYR B 2 103 ? 44.806 1.292 6.662 1.00 45.66 ? 100 TYR B CA 1 ATOM 2442 C C . TYR B 2 103 ? 45.797 0.210 6.321 1.00 53.33 ? 100 TYR B C 1 ATOM 2443 O O . TYR B 2 103 ? 46.742 0.019 7.043 1.00 84.65 ? 100 TYR B O 1 ATOM 2444 C CB . TYR B 2 103 ? 44.386 1.148 8.116 1.00 41.77 ? 100 TYR B CB 1 ATOM 2445 C CG . TYR B 2 103 ? 44.215 2.462 8.803 1.00 42.16 ? 100 TYR B CG 1 ATOM 2446 C CD1 . TYR B 2 103 ? 43.048 3.162 8.694 1.00 39.55 ? 100 TYR B CD1 1 ATOM 2447 C CD2 . TYR B 2 103 ? 45.230 3.007 9.548 1.00 67.43 ? 100 TYR B CD2 1 ATOM 2448 C CE1 . TYR B 2 103 ? 42.890 4.376 9.310 1.00 56.08 ? 100 TYR B CE1 1 ATOM 2449 C CE2 . TYR B 2 103 ? 45.082 4.222 10.171 1.00 69.86 ? 100 TYR B CE2 1 ATOM 2450 C CZ . TYR B 2 103 ? 43.913 4.902 10.045 1.00 59.07 ? 100 TYR B CZ 1 ATOM 2451 O OH . TYR B 2 103 ? 43.752 6.116 10.657 1.00 48.75 ? 100 TYR B OH 1 ATOM 2452 N N . HIS B 2 104 A 45.573 -0.513 5.235 1.00 51.71 ? 100 HIS B N 1 ATOM 2453 C CA . HIS B 2 104 A 46.408 -1.656 4.903 1.00 65.14 ? 100 HIS B CA 1 ATOM 2454 C C . HIS B 2 104 A 47.047 -1.573 3.520 1.00 77.58 ? 100 HIS B C 1 ATOM 2455 O O . HIS B 2 104 A 46.413 -1.102 2.592 1.00 82.37 ? 100 HIS B O 1 ATOM 2456 C CB . HIS B 2 104 A 45.597 -2.950 5.004 1.00 60.63 ? 100 HIS B CB 1 ATOM 2457 N N . ALA B 2 105 B 48.283 -2.049 3.367 1.00 71.55 ? 100 ALA B N 1 ATOM 2458 C CA . ALA B 2 105 B 49.011 -2.715 4.437 1.00 88.00 ? 100 ALA B CA 1 ATOM 2459 C C . ALA B 2 105 B 50.431 -2.207 4.588 1.00 86.05 ? 100 ALA B C 1 ATOM 2460 O O . ALA B 2 105 B 51.380 -2.962 4.415 1.00 103.64 ? 100 ALA B O 1 ATOM 2461 C CB . ALA B 2 105 B 48.997 -4.222 4.225 1.00 92.61 ? 100 ALA B CB 1 ATOM 2462 N N . TYR B 2 106 C 50.592 -0.953 4.989 1.00 89.64 ? 100 TYR B N 1 ATOM 2463 C CA . TYR B 2 106 C 49.505 -0.007 5.172 1.00 82.51 ? 100 TYR B CA 1 ATOM 2464 C C . TYR B 2 106 C 49.760 1.289 4.410 1.00 85.56 ? 100 TYR B C 1 ATOM 2465 O O . TYR B 2 106 C 50.785 1.927 4.599 1.00 67.31 ? 100 TYR B O 1 ATOM 2466 C CB . TYR B 2 106 C 49.434 0.308 6.651 1.00 75.46 ? 100 TYR B CB 1 ATOM 2467 C CG . TYR B 2 106 C 50.732 0.865 7.139 1.00 75.95 ? 100 TYR B CG 1 ATOM 2468 C CD1 . TYR B 2 106 C 51.874 0.090 7.160 1.00 69.04 ? 100 TYR B CD1 1 ATOM 2469 C CD2 . TYR B 2 106 C 50.826 2.182 7.534 1.00 66.94 ? 100 TYR B CD2 1 ATOM 2470 C CE1 . TYR B 2 106 C 53.073 0.611 7.588 1.00 74.84 ? 100 TYR B CE1 1 ATOM 2471 C CE2 . TYR B 2 106 C 52.013 2.713 7.962 1.00 63.26 ? 100 TYR B CE2 1 ATOM 2472 C CZ . TYR B 2 106 C 53.130 1.924 7.993 1.00 82.67 ? 100 TYR B CZ 1 ATOM 2473 O OH . TYR B 2 106 C 54.312 2.470 8.427 1.00 109.08 ? 100 TYR B OH 1 ATOM 2474 N N . TRP B 2 107 D 48.838 1.664 3.534 1.00 104.70 ? 100 TRP B N 1 ATOM 2475 C CA . TRP B 2 107 D 48.810 2.998 2.943 1.00 79.69 ? 100 TRP B CA 1 ATOM 2476 C C . TRP B 2 107 D 48.457 4.074 3.954 1.00 82.89 ? 100 TRP B C 1 ATOM 2477 O O . TRP B 2 107 D 49.048 5.137 3.974 1.00 78.78 ? 100 TRP B O 1 ATOM 2478 C CB . TRP B 2 107 D 47.810 3.053 1.786 1.00 57.34 ? 100 TRP B CB 1 ATOM 2479 N N . SER B 2 108 E 47.470 3.773 4.786 1.00 80.04 ? 100 SER B N 1 ATOM 2480 C CA . SER B 2 108 E 46.831 4.757 5.644 1.00 59.26 ? 100 SER B CA 1 ATOM 2481 C C . SER B 2 108 E 46.312 5.944 4.844 1.00 69.38 ? 100 SER B C 1 ATOM 2482 O O . SER B 2 108 E 46.455 7.086 5.253 1.00 69.14 ? 100 SER B O 1 ATOM 2483 C CB . SER B 2 108 E 47.751 5.221 6.755 1.00 58.58 ? 100 SER B CB 1 ATOM 2484 O OG . SER B 2 108 E 47.001 5.920 7.729 1.00 71.49 ? 100 SER B OG 1 ATOM 2485 N N . GLY B 2 109 F 45.703 5.666 3.703 1.00 47.48 ? 100 GLY B N 1 ATOM 2486 C CA . GLY B 2 109 F 45.260 6.703 2.793 1.00 53.52 ? 100 GLY B CA 1 ATOM 2487 C C . GLY B 2 109 F 43.908 6.418 2.198 1.00 34.43 ? 100 GLY B C 1 ATOM 2488 O O . GLY B 2 109 F 43.386 5.344 2.387 1.00 31.78 ? 100 GLY B O 1 ATOM 2489 N N . TYR B 2 110 G 43.316 7.389 1.516 1.00 30.43 ? 100 TYR B N 1 ATOM 2490 C CA . TYR B 2 110 G 42.060 7.130 0.825 1.00 27.17 ? 100 TYR B CA 1 ATOM 2491 C C . TYR B 2 110 G 42.335 6.620 -0.587 1.00 27.78 ? 100 TYR B C 1 ATOM 2492 O O . TYR B 2 110 G 43.136 7.200 -1.319 1.00 49.02 ? 100 TYR B O 1 ATOM 2493 C CB . TYR B 2 110 G 41.198 8.393 0.805 1.00 25.09 ? 100 TYR B CB 1 ATOM 2494 C CG . TYR B 2 110 G 40.887 8.919 2.192 1.00 25.57 ? 100 TYR B CG 1 ATOM 2495 C CD1 . TYR B 2 110 G 41.755 9.791 2.837 1.00 28.17 ? 100 TYR B CD1 1 ATOM 2496 C CD2 . TYR B 2 110 G 39.733 8.531 2.863 1.00 40.06 ? 100 TYR B CD2 1 ATOM 2497 C CE1 . TYR B 2 110 G 41.480 10.267 4.106 1.00 29.79 ? 100 TYR B CE1 1 ATOM 2498 C CE2 . TYR B 2 110 G 39.449 9.004 4.134 1.00 37.40 ? 100 TYR B CE2 1 ATOM 2499 C CZ . TYR B 2 110 G 40.326 9.872 4.749 1.00 28.20 ? 100 TYR B CZ 1 ATOM 2500 O OH . TYR B 2 110 G 40.050 10.346 6.012 1.00 23.78 ? 100 TYR B OH 1 ATOM 2501 N N . VAL B 2 111 H 41.665 5.533 -0.964 1.00 28.58 ? 100 VAL B N 1 ATOM 2502 C CA . VAL B 2 111 H 42.038 4.776 -2.158 1.00 29.86 ? 100 VAL B CA 1 ATOM 2503 C C . VAL B 2 111 H 41.202 5.085 -3.403 1.00 43.20 ? 100 VAL B C 1 ATOM 2504 O O . VAL B 2 111 H 41.725 5.602 -4.391 1.00 67.28 ? 100 VAL B O 1 ATOM 2505 C CB . VAL B 2 111 H 41.959 3.259 -1.883 1.00 29.49 ? 100 VAL B CB 1 ATOM 2506 C CG1 . VAL B 2 111 H 42.098 2.468 -3.176 1.00 72.99 ? 100 VAL B CG1 1 ATOM 2507 C CG2 . VAL B 2 111 H 43.034 2.852 -0.891 1.00 30.89 ? 100 VAL B CG2 1 ATOM 2508 N N . ASN B 2 112 I 39.934 4.694 -3.432 1.00 29.62 ? 100 ASN B N 1 ATOM 2509 C CA . ASN B 2 112 I 39.156 4.853 -4.668 1.00 27.26 ? 100 ASN B CA 1 ATOM 2510 C C . ASN B 2 112 I 38.478 6.204 -4.740 1.00 28.44 ? 100 ASN B C 1 ATOM 2511 O O . ASN B 2 112 I 37.347 6.356 -4.335 1.00 41.49 ? 100 ASN B O 1 ATOM 2512 C CB . ASN B 2 112 I 38.067 3.795 -4.792 1.00 34.58 ? 100 ASN B CB 1 ATOM 2513 C CG . ASN B 2 112 I 38.597 2.406 -4.956 1.00 36.02 ? 100 ASN B CG 1 ATOM 2514 O OD1 . ASN B 2 112 I 39.499 2.169 -5.730 1.00 29.91 ? 100 ASN B OD1 1 ATOM 2515 N ND2 . ASN B 2 112 I 38.012 1.471 -4.232 1.00 25.85 ? 100 ASN B ND2 1 ATOM 2516 N N . ASN B 2 113 J 39.166 7.187 -5.275 1.00 24.20 ? 100 ASN B N 1 ATOM 2517 C CA . ASN B 2 113 J 38.663 8.533 -5.257 1.00 18.47 ? 100 ASN B CA 1 ATOM 2518 C C . ASN B 2 113 J 37.741 8.780 -6.426 1.00 20.04 ? 100 ASN B C 1 ATOM 2519 O O . ASN B 2 113 J 38.039 9.541 -7.321 1.00 26.50 ? 100 ASN B O 1 ATOM 2520 C CB . ASN B 2 113 J 39.819 9.506 -5.251 1.00 15.19 ? 100 ASN B CB 1 ATOM 2521 C CG . ASN B 2 113 J 39.418 10.872 -4.806 1.00 21.81 ? 100 ASN B CG 1 ATOM 2522 O OD1 . ASN B 2 113 J 38.371 11.052 -4.216 1.00 34.05 ? 100 ASN B OD1 1 ATOM 2523 N ND2 . ASN B 2 113 J 40.256 11.847 -5.079 1.00 20.45 ? 100 ASN B ND2 1 ATOM 2524 N N . CYS B 2 114 K 36.597 8.120 -6.389 1.00 20.15 ? 100 CYS B N 1 ATOM 2525 C CA . CYS B 2 114 K 35.536 8.335 -7.340 1.00 18.73 ? 100 CYS B CA 1 ATOM 2526 C C . CYS B 2 114 K 34.279 8.464 -6.540 1.00 18.06 ? 100 CYS B C 1 ATOM 2527 O O . CYS B 2 114 K 34.218 8.013 -5.427 1.00 15.90 ? 100 CYS B O 1 ATOM 2528 C CB . CYS B 2 114 K 35.427 7.220 -8.363 1.00 12.20 ? 100 CYS B CB 1 ATOM 2529 S SG . CYS B 2 114 K 35.373 5.549 -7.754 1.00 20.97 ? 100 CYS B SG 1 ATOM 2530 N N . PHE B 2 115 L 33.280 9.107 -7.115 1.00 23.74 ? 100 PHE B N 1 ATOM 2531 C CA . PHE B 2 115 L 32.212 9.672 -6.331 1.00 19.68 ? 100 PHE B CA 1 ATOM 2532 C C . PHE B 2 115 L 30.871 8.965 -6.430 1.00 23.64 ? 100 PHE B C 1 ATOM 2533 O O . PHE B 2 115 L 30.220 8.987 -7.433 1.00 15.93 ? 100 PHE B O 1 ATOM 2534 C CB . PHE B 2 115 L 32.096 11.163 -6.657 1.00 27.47 ? 100 PHE B CB 1 ATOM 2535 C CG . PHE B 2 115 L 33.419 11.818 -6.965 1.00 30.87 ? 100 PHE B CG 1 ATOM 2536 C CD1 . PHE B 2 115 L 34.304 12.120 -5.964 1.00 19.91 ? 100 PHE B CD1 1 ATOM 2537 C CD2 . PHE B 2 115 L 33.783 12.081 -8.259 1.00 19.01 ? 100 PHE B CD2 1 ATOM 2538 C CE1 . PHE B 2 115 L 35.514 12.690 -6.252 1.00 24.17 ? 100 PHE B CE1 1 ATOM 2539 C CE2 . PHE B 2 115 L 34.987 12.652 -8.542 1.00 17.65 ? 100 PHE B CE2 1 ATOM 2540 C CZ . PHE B 2 115 L 35.852 12.950 -7.538 1.00 19.46 ? 100 PHE B CZ 1 ATOM 2541 N N . ASP B 2 116 ? 30.500 8.319 -5.337 1.00 32.39 ? 101 ASP B N 1 ATOM 2542 C CA . ASP B 2 116 ? 29.198 7.728 -5.121 1.00 28.90 ? 101 ASP B CA 1 ATOM 2543 C C . ASP B 2 116 ? 29.079 7.597 -3.612 1.00 33.82 ? 101 ASP B C 1 ATOM 2544 O O . ASP B 2 116 ? 30.008 7.097 -3.017 1.00 37.03 ? 101 ASP B O 1 ATOM 2545 C CB . ASP B 2 116 ? 29.188 6.350 -5.775 1.00 21.12 ? 101 ASP B CB 1 ATOM 2546 C CG . ASP B 2 116 ? 27.962 5.556 -5.457 1.00 28.25 ? 101 ASP B CG 1 ATOM 2547 O OD1 . ASP B 2 116 ? 26.865 5.908 -5.894 1.00 22.31 ? 101 ASP B OD1 1 ATOM 2548 O OD2 . ASP B 2 116 ? 28.096 4.544 -4.780 1.00 20.86 ? 101 ASP B OD2 1 ATOM 2549 N N . PRO B 2 117 ? 27.900 7.964 -2.927 1.00 27.76 ? 102 PRO B N 1 ATOM 2550 C CA . PRO B 2 117 ? 26.866 8.623 -3.736 1.00 19.82 ? 102 PRO B CA 1 ATOM 2551 C C . PRO B 2 117 ? 27.073 10.096 -3.960 1.00 18.11 ? 102 PRO B C 1 ATOM 2552 O O . PRO B 2 117 ? 27.926 10.696 -3.366 1.00 32.70 ? 102 PRO B O 1 ATOM 2553 C CB . PRO B 2 117 ? 25.593 8.473 -2.907 1.00 20.42 ? 102 PRO B CB 1 ATOM 2554 C CG . PRO B 2 117 ? 25.895 7.532 -1.821 1.00 27.29 ? 102 PRO B CG 1 ATOM 2555 C CD . PRO B 2 117 ? 27.291 7.859 -1.516 1.00 33.32 ? 102 PRO B CD 1 ATOM 2556 N N . TRP B 2 118 ? 26.276 10.664 -4.845 1.00 20.95 ? 103 TRP B N 1 ATOM 2557 C CA . TRP B 2 118 ? 26.265 12.090 -5.071 1.00 13.82 ? 103 TRP B CA 1 ATOM 2558 C C . TRP B 2 118 ? 25.217 12.804 -4.264 1.00 14.03 ? 103 TRP B C 1 ATOM 2559 O O . TRP B 2 118 ? 24.262 12.224 -3.814 1.00 18.24 ? 103 TRP B O 1 ATOM 2560 C CB . TRP B 2 118 ? 26.052 12.402 -6.539 1.00 13.24 ? 103 TRP B CB 1 ATOM 2561 C CG . TRP B 2 118 ? 27.167 12.011 -7.373 1.00 12.74 ? 103 TRP B CG 1 ATOM 2562 C CD1 . TRP B 2 118 ? 27.711 10.789 -7.455 1.00 13.09 ? 103 TRP B CD1 1 ATOM 2563 C CD2 . TRP B 2 118 ? 27.893 12.836 -8.271 1.00 9.71 ? 103 TRP B CD2 1 ATOM 2564 N NE1 . TRP B 2 118 ? 28.734 10.786 -8.333 1.00 15.32 ? 103 TRP B NE1 1 ATOM 2565 C CE2 . TRP B 2 118 ? 28.866 12.040 -8.857 1.00 10.42 ? 103 TRP B CE2 1 ATOM 2566 C CE3 . TRP B 2 118 ? 27.814 14.172 -8.639 1.00 9.51 ? 103 TRP B CE3 1 ATOM 2567 C CZ2 . TRP B 2 118 ? 29.757 12.532 -9.785 1.00 10.83 ? 103 TRP B CZ2 1 ATOM 2568 C CZ3 . TRP B 2 118 ? 28.692 14.646 -9.561 1.00 14.79 ? 103 TRP B CZ3 1 ATOM 2569 C CH2 . TRP B 2 118 ? 29.646 13.835 -10.128 1.00 9.81 ? 103 TRP B CH2 1 ATOM 2570 N N . GLY B 2 119 ? 25.428 14.089 -4.085 1.00 14.16 ? 104 GLY B N 1 ATOM 2571 C CA . GLY B 2 119 ? 24.447 14.967 -3.512 1.00 12.41 ? 104 GLY B CA 1 ATOM 2572 C C . GLY B 2 119 ? 23.376 15.262 -4.524 1.00 13.69 ? 104 GLY B C 1 ATOM 2573 O O . GLY B 2 119 ? 23.520 14.997 -5.688 1.00 13.50 ? 104 GLY B O 1 ATOM 2574 N N . GLN B 2 120 ? 22.267 15.772 -4.039 1.00 26.69 ? 105 GLN B N 1 ATOM 2575 C CA . GLN B 2 120 ? 21.156 16.218 -4.854 1.00 17.50 ? 105 GLN B CA 1 ATOM 2576 C C . GLN B 2 120 ? 21.495 17.377 -5.750 1.00 14.36 ? 105 GLN B C 1 ATOM 2577 O O . GLN B 2 120 ? 21.074 17.423 -6.878 1.00 18.28 ? 105 GLN B O 1 ATOM 2578 C CB . GLN B 2 120 ? 20.003 16.619 -3.957 1.00 20.28 ? 105 GLN B CB 1 ATOM 2579 C CG . GLN B 2 120 ? 20.319 17.810 -3.066 1.00 24.19 ? 105 GLN B CG 1 ATOM 2580 C CD . GLN B 2 120 ? 19.186 18.211 -2.178 1.00 34.56 ? 105 GLN B CD 1 ATOM 2581 O OE1 . GLN B 2 120 ? 18.294 17.430 -1.934 1.00 72.30 ? 105 GLN B OE1 1 ATOM 2582 N NE2 . GLN B 2 120 ? 19.206 19.436 -1.700 1.00 70.09 ? 105 GLN B NE2 1 ATOM 2583 N N . GLY B 2 121 ? 22.238 18.338 -5.246 1.00 14.07 ? 106 GLY B N 1 ATOM 2584 C CA . GLY B 2 121 ? 22.703 19.405 -6.110 1.00 15.06 ? 106 GLY B CA 1 ATOM 2585 C C . GLY B 2 121 ? 22.113 20.747 -5.729 1.00 16.78 ? 106 GLY B C 1 ATOM 2586 O O . GLY B 2 121 ? 20.986 20.824 -5.239 1.00 33.88 ? 106 GLY B O 1 ATOM 2587 N N . THR B 2 122 ? 22.881 21.808 -5.949 1.00 16.77 ? 107 THR B N 1 ATOM 2588 C CA . THR B 2 122 ? 22.418 23.163 -5.680 1.00 15.40 ? 107 THR B CA 1 ATOM 2589 C C . THR B 2 122 ? 22.791 24.085 -6.834 1.00 14.96 ? 107 THR B C 1 ATOM 2590 O O . THR B 2 122 ? 23.965 24.399 -7.033 1.00 23.74 ? 107 THR B O 1 ATOM 2591 C CB . THR B 2 122 ? 23.009 23.719 -4.371 1.00 16.20 ? 107 THR B CB 1 ATOM 2592 O OG1 . THR B 2 122 ? 22.622 22.882 -3.275 1.00 26.91 ? 107 THR B OG1 1 ATOM 2593 C CG2 . THR B 2 122 ? 22.511 25.134 -4.121 1.00 13.97 ? 107 THR B CG2 1 ATOM 2594 N N . LEU B 2 123 ? 21.790 24.511 -7.596 1.00 15.49 ? 108 LEU B N 1 ATOM 2595 C CA . LEU B 2 123 ? 22.027 25.374 -8.745 1.00 15.74 ? 108 LEU B CA 1 ATOM 2596 C C . LEU B 2 123 ? 22.306 26.807 -8.309 1.00 16.18 ? 108 LEU B C 1 ATOM 2597 O O . LEU B 2 123 ? 21.406 27.522 -7.871 1.00 37.39 ? 108 LEU B O 1 ATOM 2598 C CB . LEU B 2 123 ? 20.834 25.336 -9.701 1.00 15.77 ? 108 LEU B CB 1 ATOM 2599 C CG . LEU B 2 123 ? 20.919 26.237 -10.934 1.00 20.68 ? 108 LEU B CG 1 ATOM 2600 C CD1 . LEU B 2 123 ? 22.240 26.046 -11.662 1.00 40.76 ? 108 LEU B CD1 1 ATOM 2601 C CD2 . LEU B 2 123 ? 19.759 25.957 -11.869 1.00 37.37 ? 108 LEU B CD2 1 ATOM 2602 N N . VAL B 2 124 ? 23.564 27.217 -8.434 1.00 12.87 ? 109 VAL B N 1 ATOM 2603 C CA . VAL B 2 124 ? 23.970 28.567 -8.073 1.00 13.19 ? 109 VAL B CA 1 ATOM 2604 C C . VAL B 2 124 ? 23.994 29.470 -9.299 1.00 15.43 ? 109 VAL B C 1 ATOM 2605 O O . VAL B 2 124 ? 24.690 29.188 -10.274 1.00 22.33 ? 109 VAL B O 1 ATOM 2606 C CB . VAL B 2 124 ? 25.355 28.578 -7.406 1.00 11.23 ? 109 VAL B CB 1 ATOM 2607 C CG1 . VAL B 2 124 ? 25.780 30.002 -7.087 1.00 14.12 ? 109 VAL B CG1 1 ATOM 2608 C CG2 . VAL B 2 124 ? 25.341 27.727 -6.149 1.00 12.82 ? 109 VAL B CG2 1 ATOM 2609 N N . THR B 2 125 ? 23.228 30.555 -9.244 1.00 15.79 ? 110 THR B N 1 ATOM 2610 C CA . THR B 2 125 ? 23.148 31.494 -10.355 1.00 15.19 ? 110 THR B CA 1 ATOM 2611 C C . THR B 2 125 ? 23.811 32.820 -10.003 1.00 16.20 ? 110 THR B C 1 ATOM 2612 O O . THR B 2 125 ? 23.400 33.500 -9.062 1.00 29.99 ? 110 THR B O 1 ATOM 2613 C CB . THR B 2 125 ? 21.687 31.755 -10.765 1.00 14.56 ? 110 THR B CB 1 ATOM 2614 O OG1 . THR B 2 125 ? 21.034 30.509 -11.037 1.00 24.93 ? 110 THR B OG1 1 ATOM 2615 C CG2 . THR B 2 125 ? 21.628 32.635 -12.002 1.00 12.14 ? 110 THR B CG2 1 ATOM 2616 N N . VAL B 2 126 ? 24.837 33.186 -10.761 1.00 11.31 ? 111 VAL B N 1 ATOM 2617 C CA . VAL B 2 126 ? 25.553 34.429 -10.510 1.00 15.87 ? 111 VAL B CA 1 ATOM 2618 C C . VAL B 2 126 ? 25.026 35.550 -11.398 1.00 21.86 ? 111 VAL B C 1 ATOM 2619 O O . VAL B 2 126 ? 25.396 35.659 -12.568 1.00 20.13 ? 111 VAL B O 1 ATOM 2620 C CB . VAL B 2 126 ? 27.063 34.264 -10.736 1.00 19.46 ? 111 VAL B CB 1 ATOM 2621 C CG1 . VAL B 2 126 ? 27.797 35.533 -10.340 1.00 25.94 ? 111 VAL B CG1 1 ATOM 2622 C CG2 . VAL B 2 126 ? 27.582 33.080 -9.942 1.00 19.41 ? 111 VAL B CG2 1 ATOM 2623 N N . SER B 2 127 ? 24.156 36.378 -10.830 1.00 19.24 ? 112 SER B N 1 ATOM 2624 C CA . SER B 2 127 ? 23.564 37.496 -11.553 1.00 16.74 ? 112 SER B CA 1 ATOM 2625 C C . SER B 2 127 ? 23.163 38.610 -10.593 1.00 22.78 ? 112 SER B C 1 ATOM 2626 O O . SER B 2 127 ? 22.938 38.368 -9.408 1.00 41.22 ? 112 SER B O 1 ATOM 2627 C CB . SER B 2 127 ? 22.349 37.034 -12.357 1.00 15.77 ? 112 SER B CB 1 ATOM 2628 O OG . SER B 2 127 ? 21.709 38.128 -12.989 1.00 15.82 ? 112 SER B OG 1 ATOM 2629 N N . SER B 2 128 ? 23.071 39.830 -11.111 1.00 22.81 ? 113 SER B N 1 ATOM 2630 C CA . SER B 2 128 ? 22.683 40.974 -10.296 1.00 46.19 ? 113 SER B CA 1 ATOM 2631 C C . SER B 2 128 ? 21.184 41.243 -10.404 1.00 24.45 ? 113 SER B C 1 ATOM 2632 O O . SER B 2 128 ? 20.660 42.163 -9.775 1.00 19.67 ? 113 SER B O 1 ATOM 2633 C CB . SER B 2 128 ? 23.477 42.214 -10.705 1.00 26.67 ? 113 SER B CB 1 ATOM 2634 O OG . SER B 2 128 ? 23.415 42.414 -12.105 1.00 46.39 ? 113 SER B OG 1 ATOM 2635 N N . ALA B 2 129 ? 20.507 40.451 -11.209 1.00 14.62 ? 114 ALA B N 1 ATOM 2636 C CA . ALA B 2 129 ? 19.075 40.537 -11.352 1.00 16.24 ? 114 ALA B CA 1 ATOM 2637 C C . ALA B 2 129 ? 18.408 40.091 -10.083 1.00 15.36 ? 114 ALA B C 1 ATOM 2638 O O . ALA B 2 129 ? 18.897 39.218 -9.434 1.00 22.33 ? 114 ALA B O 1 ATOM 2639 C CB . ALA B 2 129 ? 18.626 39.671 -12.505 1.00 15.03 ? 114 ALA B CB 1 ATOM 2640 N N . SER B 2 130 ? 17.292 40.706 -9.730 1.00 20.83 ? 115 SER B N 1 ATOM 2641 C CA . SER B 2 130 ? 16.551 40.343 -8.540 1.00 16.49 ? 115 SER B CA 1 ATOM 2642 C C . SER B 2 130 ? 15.542 39.240 -8.760 1.00 19.15 ? 115 SER B C 1 ATOM 2643 O O . SER B 2 130 ? 15.029 39.059 -9.850 1.00 35.64 ? 115 SER B O 1 ATOM 2644 C CB . SER B 2 130 ? 15.844 41.550 -7.981 1.00 20.03 ? 115 SER B CB 1 ATOM 2645 O OG . SER B 2 130 ? 15.333 42.314 -9.036 1.00 53.32 ? 115 SER B OG 1 ATOM 2646 N N . THR B 2 131 ? 15.249 38.501 -7.709 1.00 19.24 ? 116 THR B N 1 ATOM 2647 C CA . THR B 2 131 ? 14.318 37.410 -7.829 1.00 14.58 ? 116 THR B CA 1 ATOM 2648 C C . THR B 2 131 ? 12.881 37.867 -8.090 1.00 22.16 ? 116 THR B C 1 ATOM 2649 O O . THR B 2 131 ? 12.431 38.881 -7.590 1.00 22.48 ? 116 THR B O 1 ATOM 2650 C CB . THR B 2 131 ? 14.467 36.348 -6.711 1.00 13.34 ? 116 THR B CB 1 ATOM 2651 O OG1 . THR B 2 131 ? 13.672 35.206 -6.997 1.00 20.33 ? 116 THR B OG1 1 ATOM 2652 C CG2 . THR B 2 131 ? 14.117 36.874 -5.378 1.00 45.72 ? 116 THR B CG2 1 ATOM 2653 N N . LYS B 2 132 ? 12.192 37.101 -8.926 1.00 21.45 ? 117 LYS B N 1 ATOM 2654 C CA . LYS B 2 132 ? 10.830 37.363 -9.305 1.00 12.06 ? 117 LYS B CA 1 ATOM 2655 C C . LYS B 2 132 ? 10.023 36.110 -9.194 1.00 13.37 ? 117 LYS B C 1 ATOM 2656 O O . LYS B 2 132 ? 10.466 35.064 -9.590 1.00 13.12 ? 117 LYS B O 1 ATOM 2657 C CB . LYS B 2 132 ? 10.790 37.855 -10.735 1.00 11.07 ? 117 LYS B CB 1 ATOM 2658 C CG . LYS B 2 132 ? 9.415 38.230 -11.218 1.00 11.96 ? 117 LYS B CG 1 ATOM 2659 C CD . LYS B 2 132 ? 9.426 38.471 -12.700 1.00 15.40 ? 117 LYS B CD 1 ATOM 2660 C CE . LYS B 2 132 ? 8.072 38.918 -13.181 1.00 12.54 ? 117 LYS B CE 1 ATOM 2661 N NZ . LYS B 2 132 ? 7.797 40.275 -12.664 1.00 35.51 ? 117 LYS B NZ 1 ATOM 2662 N N . GLY B 2 133 ? 8.827 36.215 -8.655 1.00 9.91 ? 118 GLY B N 1 ATOM 2663 C CA . GLY B 2 133 ? 7.906 35.095 -8.703 1.00 17.96 ? 118 GLY B CA 1 ATOM 2664 C C . GLY B 2 133 ? 7.275 34.922 -10.071 1.00 10.10 ? 118 GLY B C 1 ATOM 2665 O O . GLY B 2 133 ? 7.127 35.888 -10.818 1.00 14.35 ? 118 GLY B O 1 ATOM 2666 N N . PRO B 2 134 ? 6.901 33.680 -10.410 1.00 7.26 ? 119 PRO B N 1 ATOM 2667 C CA . PRO B 2 134 ? 6.321 33.339 -11.712 1.00 6.60 ? 119 PRO B CA 1 ATOM 2668 C C . PRO B 2 134 ? 4.816 33.570 -11.794 1.00 11.83 ? 119 PRO B C 1 ATOM 2669 O O . PRO B 2 134 ? 4.131 33.590 -10.771 1.00 26.12 ? 119 PRO B O 1 ATOM 2670 C CB . PRO B 2 134 ? 6.631 31.850 -11.839 1.00 7.11 ? 119 PRO B CB 1 ATOM 2671 C CG . PRO B 2 134 ? 6.590 31.361 -10.436 1.00 9.03 ? 119 PRO B CG 1 ATOM 2672 C CD . PRO B 2 134 ? 7.133 32.482 -9.584 1.00 12.88 ? 119 PRO B CD 1 ATOM 2673 N N . SER B 2 135 ? 4.318 33.742 -13.013 1.00 13.37 ? 120 SER B N 1 ATOM 2674 C CA . SER B 2 135 ? 2.884 33.773 -13.265 1.00 9.57 ? 120 SER B CA 1 ATOM 2675 C C . SER B 2 135 ? 2.480 32.490 -13.979 1.00 13.33 ? 120 SER B C 1 ATOM 2676 O O . SER B 2 135 ? 3.147 32.063 -14.921 1.00 18.99 ? 120 SER B O 1 ATOM 2677 C CB . SER B 2 135 ? 2.498 34.995 -14.100 1.00 13.64 ? 120 SER B CB 1 ATOM 2678 O OG . SER B 2 135 ? 2.866 36.199 -13.450 1.00 26.92 ? 120 SER B OG 1 ATOM 2679 N N . VAL B 2 136 ? 1.394 31.871 -13.530 1.00 8.24 ? 121 VAL B N 1 ATOM 2680 C CA . VAL B 2 136 ? 0.949 30.614 -14.119 1.00 8.27 ? 121 VAL B CA 1 ATOM 2681 C C . VAL B 2 136 ? -0.325 30.799 -14.934 1.00 10.37 ? 121 VAL B C 1 ATOM 2682 O O . VAL B 2 136 ? -1.342 31.265 -14.420 1.00 22.22 ? 121 VAL B O 1 ATOM 2683 C CB . VAL B 2 136 ? 0.706 29.544 -13.042 1.00 8.03 ? 121 VAL B CB 1 ATOM 2684 C CG1 . VAL B 2 136 ? 0.332 28.220 -13.687 1.00 13.37 ? 121 VAL B CG1 1 ATOM 2685 C CG2 . VAL B 2 136 ? 1.940 29.384 -12.174 1.00 6.53 ? 121 VAL B CG2 1 ATOM 2686 N N . PHE B 2 137 ? -0.261 30.429 -16.209 1.00 10.99 ? 122 PHE B N 1 ATOM 2687 C CA . PHE B 2 137 ? -1.413 30.533 -17.096 1.00 11.96 ? 122 PHE B CA 1 ATOM 2688 C C . PHE B 2 137 ? -1.787 29.163 -17.649 1.00 13.27 ? 122 PHE B C 1 ATOM 2689 O O . PHE B 2 137 ? -0.914 28.332 -17.896 1.00 14.25 ? 122 PHE B O 1 ATOM 2690 C CB . PHE B 2 137 ? -1.124 31.509 -18.238 1.00 11.44 ? 122 PHE B CB 1 ATOM 2691 C CG . PHE B 2 137 ? -0.681 32.865 -17.775 1.00 13.16 ? 122 PHE B CG 1 ATOM 2692 C CD1 . PHE B 2 137 ? -1.559 33.707 -17.116 1.00 16.51 ? 122 PHE B CD1 1 ATOM 2693 C CD2 . PHE B 2 137 ? 0.613 33.299 -18.001 1.00 23.32 ? 122 PHE B CD2 1 ATOM 2694 C CE1 . PHE B 2 137 ? -1.153 34.956 -16.686 1.00 14.50 ? 122 PHE B CE1 1 ATOM 2695 C CE2 . PHE B 2 137 ? 1.024 34.547 -17.575 1.00 21.09 ? 122 PHE B CE2 1 ATOM 2696 C CZ . PHE B 2 137 ? 0.138 35.376 -16.918 1.00 14.08 ? 122 PHE B CZ 1 ATOM 2697 N N . PRO B 2 138 ? -3.093 28.922 -17.842 1.00 13.73 ? 123 PRO B N 1 ATOM 2698 C CA . PRO B 2 138 ? -3.565 27.618 -18.316 1.00 11.11 ? 123 PRO B CA 1 ATOM 2699 C C . PRO B 2 138 ? -3.386 27.425 -19.817 1.00 11.51 ? 123 PRO B C 1 ATOM 2700 O O . PRO B 2 138 ? -3.461 28.387 -20.581 1.00 16.94 ? 123 PRO B O 1 ATOM 2701 C CB . PRO B 2 138 ? -5.049 27.637 -17.951 1.00 9.57 ? 123 PRO B CB 1 ATOM 2702 C CG . PRO B 2 138 ? -5.419 29.074 -18.028 1.00 12.78 ? 123 PRO B CG 1 ATOM 2703 C CD . PRO B 2 138 ? -4.210 29.839 -17.555 1.00 24.79 ? 123 PRO B CD 1 ATOM 2704 N N . LEU B 2 139 ? -2.946 26.248 -20.217 1.00 18.66 ? 124 LEU B N 1 ATOM 2705 C CA . LEU B 2 139 ? -2.805 25.940 -21.617 1.00 14.24 ? 124 LEU B CA 1 ATOM 2706 C C . LEU B 2 139 ? -3.965 25.039 -21.891 1.00 26.78 ? 124 LEU B C 1 ATOM 2707 O O . LEU B 2 139 ? -3.854 23.833 -21.854 1.00 28.87 ? 124 LEU B O 1 ATOM 2708 C CB . LEU B 2 139 ? -1.511 25.220 -21.904 1.00 12.93 ? 124 LEU B CB 1 ATOM 2709 C CG . LEU B 2 139 ? -0.213 26.002 -21.962 1.00 15.96 ? 124 LEU B CG 1 ATOM 2710 C CD1 . LEU B 2 139 ? 0.925 25.042 -22.128 1.00 6.67 ? 124 LEU B CD1 1 ATOM 2711 C CD2 . LEU B 2 139 ? -0.207 27.026 -23.065 1.00 9.04 ? 124 LEU B CD2 1 ATOM 2712 N N . ALA B 2 140 ? -5.104 25.656 -22.129 1.00 20.18 ? 125 ALA B N 1 ATOM 2713 C CA . ALA B 2 140 ? -6.349 24.964 -22.156 1.00 29.14 ? 125 ALA B CA 1 ATOM 2714 C C . ALA B 2 140 ? -6.435 24.004 -23.304 1.00 35.46 ? 125 ALA B C 1 ATOM 2715 O O . ALA B 2 140 ? -5.915 24.246 -24.389 1.00 32.11 ? 125 ALA B O 1 ATOM 2716 C CB . ALA B 2 140 ? -7.485 25.943 -22.195 1.00 60.05 ? 125 ALA B CB 1 ATOM 2717 N N . PRO B 2 141 ? -7.191 22.929 -23.112 1.00 39.61 ? 126 PRO B N 1 ATOM 2718 C CA . PRO B 2 141 ? -7.381 21.939 -24.167 1.00 59.08 ? 126 PRO B CA 1 ATOM 2719 C C . PRO B 2 141 ? -8.536 22.263 -25.097 1.00 83.51 ? 126 PRO B C 1 ATOM 2720 O O . PRO B 2 141 ? -9.664 22.419 -24.683 1.00 92.73 ? 126 PRO B O 1 ATOM 2721 C CB . PRO B 2 141 ? -7.703 20.668 -23.393 1.00 51.13 ? 126 PRO B CB 1 ATOM 2722 C CG . PRO B 2 141 ? -8.322 21.149 -22.150 1.00 35.93 ? 126 PRO B CG 1 ATOM 2723 C CD . PRO B 2 141 ? -7.634 22.422 -21.808 1.00 35.90 ? 126 PRO B CD 1 ATOM 2724 N N . SER B 2 142 ? -8.230 22.357 -26.376 1.00 65.71 ? 127 SER B N 1 ATOM 2725 C CA . SER B 2 142 ? -9.220 22.638 -27.385 1.00 76.46 ? 127 SER B CA 1 ATOM 2726 C C . SER B 2 142 ? -10.220 21.505 -27.451 1.00 110.47 ? 127 SER B C 1 ATOM 2727 O O . SER B 2 142 ? -11.408 21.713 -27.697 1.00 120.51 ? 127 SER B O 1 ATOM 2728 C CB . SER B 2 142 ? -8.549 22.842 -28.749 1.00 99.24 ? 127 SER B CB 1 ATOM 2729 O OG . SER B 2 142 ? -8.498 21.652 -29.525 1.00 73.16 ? 127 SER B OG 1 ATOM 2730 N N . SER B 2 143 ? -9.700 20.297 -27.269 1.00 110.35 ? 128 SER B N 1 ATOM 2731 C CA . SER B 2 143 ? -10.387 19.078 -27.629 1.00 117.53 ? 128 SER B CA 1 ATOM 2732 C C . SER B 2 143 ? -11.685 18.860 -26.904 1.00 118.58 ? 128 SER B C 1 ATOM 2733 O O . SER B 2 143 ? -11.786 19.036 -25.689 1.00 100.94 ? 128 SER B O 1 ATOM 2734 C CB . SER B 2 143 ? -9.488 17.879 -27.404 1.00 104.45 ? 128 SER B CB 1 ATOM 2735 O OG . SER B 2 143 ? -10.198 16.700 -27.719 1.00 84.31 ? 128 SER B OG 1 ATOM 2736 N N . LYS B 2 144 ? -12.680 18.454 -27.684 1.00 115.55 ? 129 LYS B N 1 ATOM 2737 C CA . LYS B 2 144 ? -13.984 18.131 -27.157 1.00 117.94 ? 129 LYS B CA 1 ATOM 2738 C C . LYS B 2 144 ? -13.854 16.859 -26.351 1.00 129.38 ? 129 LYS B C 1 ATOM 2739 O O . LYS B 2 144 ? -13.045 15.999 -26.641 1.00 123.32 ? 129 LYS B O 1 ATOM 2740 C CB . LYS B 2 144 ? -15.007 17.970 -28.281 1.00 20.00 ? 129 LYS B CB 1 ATOM 2741 C CG . LYS B 2 144 ? -15.321 19.253 -29.034 1.00 20.00 ? 129 LYS B CG 1 ATOM 2742 C CD . LYS B 2 144 ? -16.325 19.020 -30.152 1.00 20.00 ? 129 LYS B CD 1 ATOM 2743 C CE . LYS B 2 144 ? -16.660 20.302 -30.891 1.00 20.00 ? 129 LYS B CE 1 ATOM 2744 N NZ . LYS B 2 144 ? -17.620 20.051 -31.990 1.00 20.00 ? 129 LYS B NZ 1 ATOM 2745 N N . SER B 2 145 ? -14.665 16.757 -25.323 1.00 30.00 ? 130 SER B N 1 ATOM 2746 C CA . SER B 2 145 ? -14.613 15.632 -24.421 1.00 30.00 ? 130 SER B CA 1 ATOM 2747 C C . SER B 2 145 ? -14.925 14.362 -25.188 1.00 30.00 ? 130 SER B C 1 ATOM 2748 O O . SER B 2 145 ? -14.376 13.320 -24.897 1.00 30.00 ? 130 SER B O 1 ATOM 2749 C CB . SER B 2 145 ? -15.571 15.852 -23.257 1.00 20.00 ? 130 SER B CB 1 ATOM 2750 O OG . SER B 2 145 ? -15.962 14.629 -22.697 1.00 20.00 ? 130 SER B OG 1 ATOM 2751 N N . THR B 2 146 ? -15.819 14.454 -26.161 1.00 117.40 ? 131 THR B N 1 ATOM 2752 C CA . THR B 2 146 ? -16.307 13.288 -26.898 1.00 125.67 ? 131 THR B CA 1 ATOM 2753 C C . THR B 2 146 ? -15.632 12.956 -28.237 1.00 134.21 ? 131 THR B C 1 ATOM 2754 O O . THR B 2 146 ? -16.140 12.161 -28.998 1.00 108.36 ? 131 THR B O 1 ATOM 2755 C CB . THR B 2 146 ? -17.809 13.388 -27.101 1.00 80.61 ? 131 THR B CB 1 ATOM 2756 O OG1 . THR B 2 146 ? -18.086 14.587 -27.822 1.00 61.89 ? 131 THR B OG1 1 ATOM 2757 C CG2 . THR B 2 146 ? -18.504 13.437 -25.762 1.00 73.94 ? 131 THR B CG2 1 ATOM 2758 N N . SER B 2 147 ? -14.498 13.578 -28.520 1.00 141.37 ? 132 SER B N 1 ATOM 2759 C CA . SER B 2 147 ? -13.748 13.304 -29.729 1.00 135.39 ? 132 SER B CA 1 ATOM 2760 C C . SER B 2 147 ? -13.346 11.842 -29.722 1.00 126.63 ? 132 SER B C 1 ATOM 2761 O O . SER B 2 147 ? -13.284 11.216 -30.766 1.00 117.73 ? 132 SER B O 1 ATOM 2762 C CB . SER B 2 147 ? -12.536 14.235 -29.833 1.00 121.31 ? 132 SER B CB 1 ATOM 2763 O OG . SER B 2 147 ? -11.576 14.051 -28.799 1.00 112.01 ? 132 SER B OG 1 ATOM 2764 N N . GLY B 2 148 ? -13.034 11.325 -28.537 1.00 127.61 ? 133 GLY B N 1 ATOM 2765 C CA . GLY B 2 148 ? -12.737 9.920 -28.340 1.00 112.89 ? 133 GLY B CA 1 ATOM 2766 C C . GLY B 2 148 ? -11.316 9.451 -28.550 1.00 108.52 ? 133 GLY B C 1 ATOM 2767 O O . GLY B 2 148 ? -11.066 8.252 -28.584 1.00 94.77 ? 133 GLY B O 1 ATOM 2768 N N . GLY B 2 149 ? -10.391 10.387 -28.725 1.00 82.78 ? 134 GLY B N 1 ATOM 2769 C CA . GLY B 2 149 ? -8.971 10.094 -28.802 1.00 50.23 ? 134 GLY B CA 1 ATOM 2770 C C . GLY B 2 149 ? -8.198 10.657 -27.628 1.00 44.65 ? 134 GLY B C 1 ATOM 2771 O O . GLY B 2 149 ? -8.664 10.673 -26.505 1.00 50.14 ? 134 GLY B O 1 ATOM 2772 N N . THR B 2 150 ? -6.996 11.132 -27.912 1.00 42.70 ? 135 THR B N 1 ATOM 2773 C CA . THR B 2 150 ? -6.147 11.781 -26.921 1.00 40.71 ? 135 THR B CA 1 ATOM 2774 C C . THR B 2 150 ? -6.183 13.328 -26.980 1.00 34.44 ? 135 THR B C 1 ATOM 2775 O O . THR B 2 150 ? -6.271 13.919 -28.035 1.00 34.10 ? 135 THR B O 1 ATOM 2776 C CB . THR B 2 150 ? -4.710 11.211 -26.953 1.00 35.66 ? 135 THR B CB 1 ATOM 2777 O OG1 . THR B 2 150 ? -3.953 11.700 -25.853 1.00 63.50 ? 135 THR B OG1 1 ATOM 2778 C CG2 . THR B 2 150 ? -4.000 11.569 -28.215 1.00 58.41 ? 135 THR B CG2 1 ATOM 2779 N N . ALA B 2 151 ? -6.146 13.965 -25.818 1.00 41.84 ? 136 ALA B N 1 ATOM 2780 C CA . ALA B 2 151 ? -6.182 15.413 -25.721 1.00 26.05 ? 136 ALA B CA 1 ATOM 2781 C C . ALA B 2 151 ? -5.003 15.905 -24.911 1.00 19.40 ? 136 ALA B C 1 ATOM 2782 O O . ALA B 2 151 ? -4.520 15.202 -24.061 1.00 18.29 ? 136 ALA B O 1 ATOM 2783 C CB . ALA B 2 151 ? -7.468 15.858 -25.068 1.00 24.53 ? 136 ALA B CB 1 ATOM 2784 N N . ALA B 2 152 ? -4.544 17.119 -25.187 1.00 21.75 ? 137 ALA B N 1 ATOM 2785 C CA . ALA B 2 152 ? -3.407 17.689 -24.472 1.00 15.92 ? 137 ALA B CA 1 ATOM 2786 C C . ALA B 2 152 ? -3.739 19.028 -23.819 1.00 16.47 ? 137 ALA B C 1 ATOM 2787 O O . ALA B 2 152 ? -4.344 19.903 -24.437 1.00 22.33 ? 137 ALA B O 1 ATOM 2788 C CB . ALA B 2 152 ? -2.223 17.846 -25.412 1.00 22.43 ? 137 ALA B CB 1 ATOM 2789 N N . LEU B 2 153 ? -3.333 19.172 -22.562 1.00 15.14 ? 138 LEU B N 1 ATOM 2790 C CA . LEU B 2 153 ? -3.485 20.424 -21.830 1.00 14.71 ? 138 LEU B CA 1 ATOM 2791 C C . LEU B 2 153 ? -2.215 20.686 -21.028 1.00 10.81 ? 138 LEU B C 1 ATOM 2792 O O . LEU B 2 153 ? -1.357 19.810 -20.920 1.00 10.59 ? 138 LEU B O 1 ATOM 2793 C CB . LEU B 2 153 ? -4.724 20.392 -20.918 1.00 23.67 ? 138 LEU B CB 1 ATOM 2794 C CG . LEU B 2 153 ? -4.951 19.419 -19.741 1.00 22.30 ? 138 LEU B CG 1 ATOM 2795 C CD1 . LEU B 2 153 ? -4.218 19.824 -18.462 1.00 15.12 ? 138 LEU B CD1 1 ATOM 2796 C CD2 . LEU B 2 153 ? -6.434 19.156 -19.460 1.00 27.25 ? 138 LEU B CD2 1 ATOM 2797 N N . GLY B 2 154 ? -2.088 21.885 -20.466 1.00 13.59 ? 139 GLY B N 1 ATOM 2798 C CA . GLY B 2 154 ? -0.897 22.212 -19.704 1.00 12.09 ? 139 GLY B CA 1 ATOM 2799 C C . GLY B 2 154 ? -0.900 23.538 -18.968 1.00 20.14 ? 139 GLY B C 1 ATOM 2800 O O . GLY B 2 154 ? -1.902 24.252 -18.938 1.00 24.43 ? 139 GLY B O 1 ATOM 2801 N N . CYS B 2 155 ? 0.241 23.858 -18.364 1.00 13.35 ? 140 CYS B N 1 ATOM 2802 C CA . CYS B 2 155 ? 0.420 25.114 -17.644 1.00 8.16 ? 140 CYS B CA 1 ATOM 2803 C C . CYS B 2 155 ? 1.618 25.893 -18.178 1.00 10.66 ? 140 CYS B C 1 ATOM 2804 O O . CYS B 2 155 ? 2.653 25.313 -18.509 1.00 13.83 ? 140 CYS B O 1 ATOM 2805 C CB . CYS B 2 155 ? 0.599 24.856 -16.146 1.00 11.16 ? 140 CYS B CB 1 ATOM 2806 S SG . CYS B 2 155 ? -0.900 24.336 -15.283 1.00 64.83 ? 140 CYS B SG 1 ATOM 2807 N N . LEU B 2 156 ? 1.472 27.211 -18.259 1.00 13.77 ? 141 LEU B N 1 ATOM 2808 C CA . LEU B 2 156 ? 2.559 28.069 -18.706 1.00 7.37 ? 141 LEU B CA 1 ATOM 2809 C C . LEU B 2 156 ? 3.126 28.870 -17.540 1.00 8.20 ? 141 LEU B C 1 ATOM 2810 O O . LEU B 2 156 ? 2.445 29.723 -16.973 1.00 14.06 ? 141 LEU B O 1 ATOM 2811 C CB . LEU B 2 156 ? 2.083 29.007 -19.815 1.00 7.52 ? 141 LEU B CB 1 ATOM 2812 C CG . LEU B 2 156 ? 3.127 29.963 -20.395 1.00 7.37 ? 141 LEU B CG 1 ATOM 2813 C CD1 . LEU B 2 156 ? 4.330 29.198 -20.921 1.00 13.74 ? 141 LEU B CD1 1 ATOM 2814 C CD2 . LEU B 2 156 ? 2.517 30.816 -21.494 1.00 11.99 ? 141 LEU B CD2 1 ATOM 2815 N N . VAL B 2 157 ? 4.372 28.581 -17.183 1.00 9.82 ? 142 VAL B N 1 ATOM 2816 C CA . VAL B 2 157 ? 5.056 29.302 -16.116 1.00 6.99 ? 142 VAL B CA 1 ATOM 2817 C C . VAL B 2 157 ? 5.911 30.419 -16.705 1.00 6.76 ? 142 VAL B C 1 ATOM 2818 O O . VAL B 2 157 ? 6.977 30.165 -17.264 1.00 10.48 ? 142 VAL B O 1 ATOM 2819 C CB . VAL B 2 157 ? 5.936 28.360 -15.282 1.00 8.06 ? 142 VAL B CB 1 ATOM 2820 C CG1 . VAL B 2 157 ? 6.618 29.121 -14.161 1.00 19.74 ? 142 VAL B CG1 1 ATOM 2821 C CG2 . VAL B 2 157 ? 5.102 27.219 -14.728 1.00 7.01 ? 142 VAL B CG2 1 ATOM 2822 N N . LYS B 2 158 ? 5.442 31.655 -16.571 1.00 7.94 ? 143 LYS B N 1 ATOM 2823 C CA . LYS B 2 158 ? 6.057 32.781 -17.265 1.00 9.15 ? 143 LYS B CA 1 ATOM 2824 C C . LYS B 2 158 ? 6.732 33.789 -16.341 1.00 14.12 ? 143 LYS B C 1 ATOM 2825 O O . LYS B 2 158 ? 6.238 34.077 -15.251 1.00 9.76 ? 143 LYS B O 1 ATOM 2826 C CB . LYS B 2 158 ? 5.006 33.500 -18.114 1.00 11.19 ? 143 LYS B CB 1 ATOM 2827 C CG . LYS B 2 158 ? 4.955 33.053 -19.563 1.00 19.41 ? 143 LYS B CG 1 ATOM 2828 C CD . LYS B 2 158 ? 5.775 33.975 -20.451 1.00 16.50 ? 143 LYS B CD 1 ATOM 2829 C CE . LYS B 2 158 ? 5.215 35.390 -20.427 1.00 19.14 ? 143 LYS B CE 1 ATOM 2830 N NZ . LYS B 2 158 ? 5.974 36.312 -21.314 1.00 35.07 ? 143 LYS B NZ 1 ATOM 2831 N N . ASP B 2 159 ? 7.866 34.312 -16.801 1.00 10.33 ? 144 ASP B N 1 ATOM 2832 C CA . ASP B 2 159 ? 8.548 35.440 -16.171 1.00 8.58 ? 144 ASP B CA 1 ATOM 2833 C C . ASP B 2 159 ? 8.920 35.213 -14.707 1.00 11.84 ? 144 ASP B C 1 ATOM 2834 O O . ASP B 2 159 ? 8.311 35.792 -13.808 1.00 18.14 ? 144 ASP B O 1 ATOM 2835 C CB . ASP B 2 159 ? 7.684 36.699 -16.288 1.00 11.81 ? 144 ASP B CB 1 ATOM 2836 C CG . ASP B 2 159 ? 7.421 37.095 -17.730 1.00 19.65 ? 144 ASP B CG 1 ATOM 2837 O OD1 . ASP B 2 159 ? 8.320 36.904 -18.577 1.00 37.20 ? 144 ASP B OD1 1 ATOM 2838 O OD2 . ASP B 2 159 ? 6.314 37.596 -18.020 1.00 19.36 ? 144 ASP B OD2 1 ATOM 2839 N N . TYR B 2 160 ? 9.963 34.446 -14.461 1.00 12.09 ? 145 TYR B N 1 ATOM 2840 C CA . TYR B 2 160 ? 10.481 34.236 -13.130 1.00 5.82 ? 145 TYR B CA 1 ATOM 2841 C C . TYR B 2 160 ? 11.989 34.198 -13.150 1.00 6.14 ? 145 TYR B C 1 ATOM 2842 O O . TYR B 2 160 ? 12.581 34.007 -14.170 1.00 9.83 ? 145 TYR B O 1 ATOM 2843 C CB . TYR B 2 160 ? 9.933 32.949 -12.539 1.00 9.25 ? 145 TYR B CB 1 ATOM 2844 C CG . TYR B 2 160 ? 10.400 31.705 -13.212 1.00 13.53 ? 145 TYR B CG 1 ATOM 2845 C CD1 . TYR B 2 160 ? 9.709 31.178 -14.274 1.00 8.96 ? 145 TYR B CD1 1 ATOM 2846 C CD2 . TYR B 2 160 ? 11.533 31.053 -12.783 1.00 11.17 ? 145 TYR B CD2 1 ATOM 2847 C CE1 . TYR B 2 160 ? 10.143 30.037 -14.890 1.00 9.06 ? 145 TYR B CE1 1 ATOM 2848 C CE2 . TYR B 2 160 ? 11.971 29.921 -13.403 1.00 8.29 ? 145 TYR B CE2 1 ATOM 2849 C CZ . TYR B 2 160 ? 11.275 29.424 -14.441 1.00 14.06 ? 145 TYR B CZ 1 ATOM 2850 O OH . TYR B 2 160 ? 11.714 28.307 -15.048 1.00 20.20 ? 145 TYR B OH 1 ATOM 2851 N N . PHE B 2 161 ? 12.610 34.464 -12.020 1.00 10.81 ? 146 PHE B N 1 ATOM 2852 C CA . PHE B 2 161 ? 14.041 34.375 -11.894 1.00 9.46 ? 146 PHE B CA 1 ATOM 2853 C C . PHE B 2 161 ? 14.238 33.998 -10.433 1.00 9.73 ? 146 PHE B C 1 ATOM 2854 O O . PHE B 2 161 ? 13.431 34.390 -9.642 1.00 11.78 ? 146 PHE B O 1 ATOM 2855 C CB . PHE B 2 161 ? 14.668 35.670 -12.337 1.00 8.68 ? 146 PHE B CB 1 ATOM 2856 C CG . PHE B 2 161 ? 16.143 35.602 -12.520 1.00 10.70 ? 146 PHE B CG 1 ATOM 2857 C CD1 . PHE B 2 161 ? 16.671 35.095 -13.663 1.00 6.84 ? 146 PHE B CD1 1 ATOM 2858 C CD2 . PHE B 2 161 ? 16.980 36.027 -11.536 1.00 9.00 ? 146 PHE B CD2 1 ATOM 2859 C CE1 . PHE B 2 161 ? 18.015 35.021 -13.821 1.00 5.56 ? 146 PHE B CE1 1 ATOM 2860 C CE2 . PHE B 2 161 ? 18.318 35.950 -11.683 1.00 7.24 ? 146 PHE B CE2 1 ATOM 2861 C CZ . PHE B 2 161 ? 18.834 35.451 -12.831 1.00 10.44 ? 146 PHE B CZ 1 ATOM 2862 N N . PRO B 2 162 ? 15.371 33.293 -10.006 1.00 10.54 ? 147 PRO B N 1 ATOM 2863 C CA . PRO B 2 162 ? 16.002 32.483 -11.057 1.00 12.61 ? 147 PRO B CA 1 ATOM 2864 C C . PRO B 2 162 ? 15.424 31.077 -11.177 1.00 8.63 ? 147 PRO B C 1 ATOM 2865 O O . PRO B 2 162 ? 14.280 30.850 -10.869 1.00 12.05 ? 147 PRO B O 1 ATOM 2866 C CB . PRO B 2 162 ? 17.460 32.372 -10.619 1.00 11.61 ? 147 PRO B CB 1 ATOM 2867 C CG . PRO B 2 162 ? 17.524 32.774 -9.205 1.00 8.72 ? 147 PRO B CG 1 ATOM 2868 C CD . PRO B 2 162 ? 16.144 32.929 -8.715 1.00 7.55 ? 147 PRO B CD 1 ATOM 2869 N N . GLU B 2 163 ? 16.214 30.177 -11.730 1.00 14.04 ? 148 GLU B N 1 ATOM 2870 C CA . GLU B 2 163 ? 15.915 28.760 -11.747 1.00 11.40 ? 148 GLU B CA 1 ATOM 2871 C C . GLU B 2 163 ? 16.148 28.166 -10.377 1.00 11.91 ? 148 GLU B C 1 ATOM 2872 O O . GLU B 2 163 ? 16.945 28.700 -9.645 1.00 24.42 ? 148 GLU B O 1 ATOM 2873 C CB . GLU B 2 163 ? 16.825 28.070 -12.732 1.00 22.79 ? 148 GLU B CB 1 ATOM 2874 C CG . GLU B 2 163 ? 16.627 28.506 -14.160 1.00 20.39 ? 148 GLU B CG 1 ATOM 2875 C CD . GLU B 2 163 ? 15.839 27.503 -14.932 1.00 20.47 ? 148 GLU B CD 1 ATOM 2876 O OE1 . GLU B 2 163 ? 14.781 27.113 -14.441 1.00 16.97 ? 148 GLU B OE1 1 ATOM 2877 O OE2 . GLU B 2 163 ? 16.280 27.116 -16.016 1.00 17.21 ? 148 GLU B OE2 1 ATOM 2878 N N . PRO B 2 164 ? 15.480 26.999 -9.962 1.00 8.79 ? 149 PRO B N 1 ATOM 2879 C CA . PRO B 2 164 ? 14.549 26.405 -10.911 1.00 9.92 ? 149 PRO B CA 1 ATOM 2880 C C . PRO B 2 164 ? 13.088 26.495 -10.529 1.00 12.24 ? 149 PRO B C 1 ATOM 2881 O O . PRO B 2 164 ? 12.755 27.086 -9.532 1.00 12.08 ? 149 PRO B O 1 ATOM 2882 C CB . PRO B 2 164 ? 14.947 24.953 -10.867 1.00 23.02 ? 149 PRO B CB 1 ATOM 2883 C CG . PRO B 2 164 ? 15.253 24.694 -9.448 1.00 11.46 ? 149 PRO B CG 1 ATOM 2884 C CD . PRO B 2 164 ? 15.511 25.998 -8.785 1.00 10.58 ? 149 PRO B CD 1 ATOM 2885 N N . VAL B 2 165 ? 12.215 25.923 -11.350 1.00 15.46 ? 150 VAL B N 1 ATOM 2886 C CA . VAL B 2 165 ? 10.806 25.828 -10.988 1.00 12.29 ? 150 VAL B CA 1 ATOM 2887 C C . VAL B 2 165 ? 10.326 24.402 -11.219 1.00 14.01 ? 150 VAL B C 1 ATOM 2888 O O . VAL B 2 165 ? 10.443 23.872 -12.324 1.00 25.03 ? 150 VAL B O 1 ATOM 2889 C CB . VAL B 2 165 ? 9.929 26.806 -11.794 1.00 14.80 ? 150 VAL B CB 1 ATOM 2890 C CG1 . VAL B 2 165 ? 8.483 26.341 -11.804 1.00 25.46 ? 150 VAL B CG1 1 ATOM 2891 C CG2 . VAL B 2 165 ? 10.027 28.201 -11.217 1.00 37.15 ? 150 VAL B CG2 1 ATOM 2892 N N . THR B 2 166 ? 9.800 23.777 -10.171 1.00 12.32 ? 151 THR B N 1 ATOM 2893 C CA . THR B 2 166 ? 9.297 22.414 -10.277 1.00 11.67 ? 151 THR B CA 1 ATOM 2894 C C . THR B 2 166 ? 7.790 22.405 -10.486 1.00 9.93 ? 151 THR B C 1 ATOM 2895 O O . THR B 2 166 ? 7.056 23.119 -9.803 1.00 17.03 ? 151 THR B O 1 ATOM 2896 C CB . THR B 2 166 ? 9.641 21.585 -9.028 1.00 10.73 ? 151 THR B CB 1 ATOM 2897 O OG1 . THR B 2 166 ? 9.131 22.241 -7.861 1.00 45.28 ? 151 THR B OG1 1 ATOM 2898 C CG2 . THR B 2 166 ? 11.145 21.427 -8.896 1.00 9.84 ? 151 THR B CG2 1 ATOM 2899 N N . VAL B 2 167 ? 7.335 21.596 -11.436 1.00 11.61 ? 152 VAL B N 1 ATOM 2900 C CA . VAL B 2 167 ? 5.915 21.500 -11.745 1.00 8.17 ? 152 VAL B CA 1 ATOM 2901 C C . VAL B 2 167 ? 5.417 20.068 -11.604 1.00 18.68 ? 152 VAL B C 1 ATOM 2902 O O . VAL B 2 167 ? 5.963 19.148 -12.214 1.00 14.59 ? 152 VAL B O 1 ATOM 2903 C CB . VAL B 2 167 ? 5.611 21.995 -13.172 1.00 7.11 ? 152 VAL B CB 1 ATOM 2904 C CG1 . VAL B 2 167 ? 4.141 21.799 -13.499 1.00 8.96 ? 152 VAL B CG1 1 ATOM 2905 C CG2 . VAL B 2 167 ? 6.005 23.453 -13.326 1.00 13.95 ? 152 VAL B CG2 1 ATOM 2906 N N . SER B 2 168 ? 4.380 19.886 -10.794 1.00 11.49 ? 153 SER B N 1 ATOM 2907 C CA . SER B 2 168 ? 3.726 18.591 -10.665 1.00 6.25 ? 153 SER B CA 1 ATOM 2908 C C . SER B 2 168 ? 2.245 18.728 -10.993 1.00 10.17 ? 153 SER B C 1 ATOM 2909 O O . SER B 2 168 ? 1.700 19.831 -10.980 1.00 16.89 ? 153 SER B O 1 ATOM 2910 C CB . SER B 2 168 ? 3.910 18.021 -9.257 1.00 6.09 ? 153 SER B CB 1 ATOM 2911 O OG . SER B 2 168 ? 3.241 18.812 -8.291 1.00 8.45 ? 153 SER B OG 1 ATOM 2912 N N . TRP B 2 169 ? 1.599 17.606 -11.290 1.00 10.52 ? 154 TRP B N 1 ATOM 2913 C CA . TRP B 2 169 ? 0.179 17.612 -11.614 1.00 8.18 ? 154 TRP B CA 1 ATOM 2914 C C . TRP B 2 169 ? -0.617 16.819 -10.585 1.00 9.02 ? 154 TRP B C 1 ATOM 2915 O O . TRP B 2 169 ? -0.293 15.666 -10.296 1.00 13.64 ? 154 TRP B O 1 ATOM 2916 C CB . TRP B 2 169 ? -0.052 17.048 -13.015 1.00 9.87 ? 154 TRP B CB 1 ATOM 2917 C CG . TRP B 2 169 ? 0.404 17.960 -14.108 1.00 8.21 ? 154 TRP B CG 1 ATOM 2918 C CD1 . TRP B 2 169 ? 1.644 18.006 -14.676 1.00 6.85 ? 154 TRP B CD1 1 ATOM 2919 C CD2 . TRP B 2 169 ? -0.376 18.963 -14.769 1.00 10.01 ? 154 TRP B CD2 1 ATOM 2920 N NE1 . TRP B 2 169 ? 1.684 18.974 -15.650 1.00 5.73 ? 154 TRP B NE1 1 ATOM 2921 C CE2 . TRP B 2 169 ? 0.456 19.577 -15.727 1.00 6.73 ? 154 TRP B CE2 1 ATOM 2922 C CE3 . TRP B 2 169 ? -1.698 19.402 -14.644 1.00 21.67 ? 154 TRP B CE3 1 ATOM 2923 C CZ2 . TRP B 2 169 ? 0.011 20.604 -16.553 1.00 8.15 ? 154 TRP B CZ2 1 ATOM 2924 C CZ3 . TRP B 2 169 ? -2.138 20.423 -15.467 1.00 14.15 ? 154 TRP B CZ3 1 ATOM 2925 C CH2 . TRP B 2 169 ? -1.287 21.011 -16.408 1.00 11.16 ? 154 TRP B CH2 1 ATOM 2926 N N . ASN B 2 170 ? -1.656 17.451 -10.044 1.00 8.58 ? 155 ASN B N 1 ATOM 2927 C CA . ASN B 2 170 ? -2.478 16.865 -8.988 1.00 10.22 ? 155 ASN B CA 1 ATOM 2928 C C . ASN B 2 170 ? -1.634 16.341 -7.830 1.00 14.15 ? 155 ASN B C 1 ATOM 2929 O O . ASN B 2 170 ? -1.854 15.233 -7.341 1.00 15.69 ? 155 ASN B O 1 ATOM 2930 C CB . ASN B 2 170 ? -3.356 15.746 -9.552 1.00 12.64 ? 155 ASN B CB 1 ATOM 2931 C CG . ASN B 2 170 ? -4.363 16.252 -10.567 1.00 12.51 ? 155 ASN B CG 1 ATOM 2932 O OD1 . ASN B 2 170 ? -4.583 17.457 -10.692 1.00 12.80 ? 155 ASN B OD1 1 ATOM 2933 N ND2 . ASN B 2 170 ? -4.988 15.331 -11.291 1.00 13.37 ? 155 ASN B ND2 1 ATOM 2934 N N . SER B 2 171 ? -0.657 17.150 -7.420 1.00 15.63 ? 156 SER B N 1 ATOM 2935 C CA . SER B 2 171 ? 0.250 16.837 -6.314 1.00 10.53 ? 156 SER B CA 1 ATOM 2936 C C . SER B 2 171 ? 1.092 15.589 -6.566 1.00 11.79 ? 156 SER B C 1 ATOM 2937 O O . SER B 2 171 ? 1.730 15.070 -5.650 1.00 9.37 ? 156 SER B O 1 ATOM 2938 C CB . SER B 2 171 ? -0.533 16.684 -5.007 1.00 11.47 ? 156 SER B CB 1 ATOM 2939 O OG . SER B 2 171 ? -1.270 17.861 -4.722 1.00 15.53 ? 156 SER B OG 1 ATOM 2940 N N . GLY B 2 172 ? 1.107 15.122 -7.810 1.00 11.27 ? 157 GLY B N 1 ATOM 2941 C CA . GLY B 2 172 ? 1.883 13.952 -8.177 1.00 6.95 ? 157 GLY B CA 1 ATOM 2942 C C . GLY B 2 172 ? 1.028 12.715 -8.366 1.00 8.52 ? 157 GLY B C 1 ATOM 2943 O O . GLY B 2 172 ? 1.545 11.600 -8.431 1.00 8.16 ? 157 GLY B O 1 ATOM 2944 N N . ALA B 2 173 ? -0.267 12.887 -8.368 1.00 12.02 ? 158 ALA B N 1 ATOM 2945 C CA . ALA B 2 173 ? -1.154 11.783 -8.614 1.00 16.36 ? 158 ALA B CA 1 ATOM 2946 C C . ALA B 2 173 ? -0.959 11.314 -10.030 1.00 18.13 ? 158 ALA B C 1 ATOM 2947 O O . ALA B 2 173 ? -1.064 10.136 -10.330 1.00 27.75 ? 158 ALA B O 1 ATOM 2948 C CB . ALA B 2 173 ? -2.589 12.182 -8.359 1.00 32.72 ? 158 ALA B CB 1 ATOM 2949 N N . LEU B 2 174 ? -0.725 12.280 -10.906 1.00 18.44 ? 159 LEU B N 1 ATOM 2950 C CA . LEU B 2 174 ? -0.591 12.039 -12.320 1.00 36.96 ? 159 LEU B CA 1 ATOM 2951 C C . LEU B 2 174 ? 0.812 12.307 -12.763 1.00 17.07 ? 159 LEU B C 1 ATOM 2952 O O . LEU B 2 174 ? 1.266 13.420 -12.726 1.00 14.74 ? 159 LEU B O 1 ATOM 2953 C CB . LEU B 2 174 ? -1.534 12.999 -13.017 1.00 32.19 ? 159 LEU B CB 1 ATOM 2954 C CG . LEU B 2 174 ? -1.542 13.235 -14.499 1.00 14.68 ? 159 LEU B CG 1 ATOM 2955 C CD1 . LEU B 2 174 ? -2.111 12.026 -15.181 1.00 12.10 ? 159 LEU B CD1 1 ATOM 2956 C CD2 . LEU B 2 174 ? -2.421 14.427 -14.725 1.00 38.76 ? 159 LEU B CD2 1 ATOM 2957 N N . THR B 2 175 ? 1.504 11.275 -13.200 1.00 19.63 ? 160 THR B N 1 ATOM 2958 C CA . THR B 2 175 ? 2.843 11.452 -13.711 1.00 15.65 ? 160 THR B CA 1 ATOM 2959 C C . THR B 2 175 ? 3.022 10.934 -15.113 1.00 18.49 ? 160 THR B C 1 ATOM 2960 O O . THR B 2 175 ? 4.006 11.240 -15.743 1.00 25.38 ? 160 THR B O 1 ATOM 2961 C CB . THR B 2 175 ? 3.853 10.739 -12.835 1.00 29.58 ? 160 THR B CB 1 ATOM 2962 O OG1 . THR B 2 175 ? 3.720 9.337 -13.046 1.00 62.43 ? 160 THR B OG1 1 ATOM 2963 C CG2 . THR B 2 175 ? 3.601 11.038 -11.392 1.00 14.25 ? 160 THR B CG2 1 ATOM 2964 N N . SER B 2 176 ? 2.061 10.164 -15.599 1.00 18.90 ? 161 SER B N 1 ATOM 2965 C CA . SER B 2 176 ? 2.150 9.502 -16.892 1.00 16.56 ? 161 SER B CA 1 ATOM 2966 C C . SER B 2 176 ? 1.780 10.388 -18.049 1.00 20.37 ? 161 SER B C 1 ATOM 2967 O O . SER B 2 176 ? 0.755 11.033 -17.995 1.00 26.13 ? 161 SER B O 1 ATOM 2968 C CB . SER B 2 176 ? 1.237 8.305 -16.896 1.00 19.89 ? 161 SER B CB 1 ATOM 2969 O OG . SER B 2 176 ? 1.990 7.120 -16.814 1.00 85.69 ? 161 SER B OG 1 ATOM 2970 N N . GLY B 2 177 ? 2.593 10.405 -19.105 1.00 15.81 ? 162 GLY B N 1 ATOM 2971 C CA . GLY B 2 177 ? 2.352 11.295 -20.226 1.00 12.88 ? 162 GLY B CA 1 ATOM 2972 C C . GLY B 2 177 ? 2.561 12.760 -19.896 1.00 18.64 ? 162 GLY B C 1 ATOM 2973 O O . GLY B 2 177 ? 1.958 13.636 -20.516 1.00 11.16 ? 162 GLY B O 1 ATOM 2974 N N . VAL B 2 178 ? 3.419 13.033 -18.918 1.00 18.89 ? 163 VAL B N 1 ATOM 2975 C CA . VAL B 2 178 ? 3.701 14.407 -18.518 1.00 8.18 ? 163 VAL B CA 1 ATOM 2976 C C . VAL B 2 178 ? 5.048 14.876 -19.055 1.00 7.71 ? 163 VAL B C 1 ATOM 2977 O O . VAL B 2 178 ? 6.074 14.236 -18.826 1.00 10.21 ? 163 VAL B O 1 ATOM 2978 C CB . VAL B 2 178 ? 3.696 14.567 -16.987 1.00 8.30 ? 163 VAL B CB 1 ATOM 2979 C CG1 . VAL B 2 178 ? 4.046 15.995 -16.603 1.00 5.86 ? 163 VAL B CG1 1 ATOM 2980 C CG2 . VAL B 2 178 ? 2.344 14.178 -16.419 1.00 10.35 ? 163 VAL B CG2 1 ATOM 2981 N N . HIS B 2 179 ? 5.034 15.995 -19.771 1.00 5.31 ? 164 HIS B N 1 ATOM 2982 C CA . HIS B 2 179 ? 6.259 16.585 -20.297 1.00 4.62 ? 164 HIS B CA 1 ATOM 2983 C C . HIS B 2 179 ? 6.482 17.991 -19.752 1.00 4.52 ? 164 HIS B C 1 ATOM 2984 O O . HIS B 2 179 ? 5.691 18.898 -20.009 1.00 9.45 ? 164 HIS B O 1 ATOM 2985 C CB . HIS B 2 179 ? 6.226 16.626 -21.828 1.00 10.24 ? 164 HIS B CB 1 ATOM 2986 C CG . HIS B 2 179 ? 6.461 15.297 -22.476 1.00 5.93 ? 164 HIS B CG 1 ATOM 2987 N ND1 . HIS B 2 179 ? 7.692 14.679 -22.478 1.00 8.58 ? 164 HIS B ND1 1 ATOM 2988 C CD2 . HIS B 2 179 ? 5.625 14.475 -23.151 1.00 8.85 ? 164 HIS B CD2 1 ATOM 2989 C CE1 . HIS B 2 179 ? 7.603 13.528 -23.123 1.00 21.10 ? 164 HIS B CE1 1 ATOM 2990 N NE2 . HIS B 2 179 ? 6.360 13.381 -23.541 1.00 14.80 ? 164 HIS B NE2 1 ATOM 2991 N N . THR B 2 180 ? 7.562 18.167 -18.998 1.00 3.72 ? 165 THR B N 1 ATOM 2992 C CA . THR B 2 180 ? 7.957 19.491 -18.530 1.00 7.53 ? 165 THR B CA 1 ATOM 2993 C C . THR B 2 180 ? 9.226 19.936 -19.245 1.00 8.85 ? 165 THR B C 1 ATOM 2994 O O . THR B 2 180 ? 10.314 19.421 -18.983 1.00 12.40 ? 165 THR B O 1 ATOM 2995 C CB . THR B 2 180 ? 8.189 19.521 -17.010 1.00 5.18 ? 165 THR B CB 1 ATOM 2996 O OG1 . THR B 2 180 ? 6.972 19.186 -16.332 1.00 12.02 ? 165 THR B OG1 1 ATOM 2997 C CG2 . THR B 2 180 ? 8.640 20.906 -16.572 1.00 3.28 ? 165 THR B CG2 1 ATOM 2998 N N . PHE B 2 181 ? 9.076 20.894 -20.153 1.00 4.77 ? 166 PHE B N 1 ATOM 2999 C CA . PHE B 2 181 ? 10.186 21.369 -20.970 1.00 5.88 ? 166 PHE B CA 1 ATOM 3000 C C . PHE B 2 181 ? 11.179 22.187 -20.153 1.00 9.47 ? 166 PHE B C 1 ATOM 3001 O O . PHE B 2 181 ? 10.787 22.889 -19.222 1.00 8.29 ? 166 PHE B O 1 ATOM 3002 C CB . PHE B 2 181 ? 9.662 22.207 -22.139 1.00 6.96 ? 166 PHE B CB 1 ATOM 3003 C CG . PHE B 2 181 ? 8.785 21.443 -23.087 1.00 10.75 ? 166 PHE B CG 1 ATOM 3004 C CD1 . PHE B 2 181 ? 7.427 21.313 -22.848 1.00 22.59 ? 166 PHE B CD1 1 ATOM 3005 C CD2 . PHE B 2 181 ? 9.318 20.859 -24.220 1.00 11.74 ? 166 PHE B CD2 1 ATOM 3006 C CE1 . PHE B 2 181 ? 6.619 20.610 -23.721 1.00 12.69 ? 166 PHE B CE1 1 ATOM 3007 C CE2 . PHE B 2 181 ? 8.514 20.154 -25.096 1.00 8.62 ? 166 PHE B CE2 1 ATOM 3008 C CZ . PHE B 2 181 ? 7.164 20.030 -24.846 1.00 10.36 ? 166 PHE B CZ 1 ATOM 3009 N N . PRO B 2 182 ? 12.473 22.091 -20.498 1.00 14.37 ? 167 PRO B N 1 ATOM 3010 C CA . PRO B 2 182 ? 13.493 22.934 -19.867 1.00 3.48 ? 167 PRO B CA 1 ATOM 3011 C C . PRO B 2 182 ? 13.222 24.408 -20.135 1.00 4.79 ? 167 PRO B C 1 ATOM 3012 O O . PRO B 2 182 ? 12.852 24.763 -21.254 1.00 10.64 ? 167 PRO B O 1 ATOM 3013 C CB . PRO B 2 182 ? 14.796 22.479 -20.533 1.00 2.35 ? 167 PRO B CB 1 ATOM 3014 C CG . PRO B 2 182 ? 14.370 21.820 -21.803 1.00 3.05 ? 167 PRO B CG 1 ATOM 3015 C CD . PRO B 2 182 ? 13.055 21.179 -21.496 1.00 5.30 ? 167 PRO B CD 1 ATOM 3016 N N . ALA B 2 183 ? 13.399 25.247 -19.120 1.00 5.00 ? 168 ALA B N 1 ATOM 3017 C CA . ALA B 2 183 ? 13.085 26.667 -19.230 1.00 12.63 ? 168 ALA B CA 1 ATOM 3018 C C . ALA B 2 183 ? 13.955 27.364 -20.267 1.00 6.12 ? 168 ALA B C 1 ATOM 3019 O O . ALA B 2 183 ? 15.061 26.917 -20.570 1.00 10.92 ? 168 ALA B O 1 ATOM 3020 C CB . ALA B 2 183 ? 13.239 27.343 -17.882 1.00 11.13 ? 168 ALA B CB 1 ATOM 3021 N N . VAL B 2 184 ? 13.441 28.461 -20.815 1.00 4.83 ? 169 VAL B N 1 ATOM 3022 C CA . VAL B 2 184 ? 14.197 29.264 -21.766 1.00 4.94 ? 169 VAL B CA 1 ATOM 3023 C C . VAL B 2 184 ? 14.390 30.678 -21.226 1.00 8.95 ? 169 VAL B C 1 ATOM 3024 O O . VAL B 2 184 ? 13.464 31.278 -20.677 1.00 6.88 ? 169 VAL B O 1 ATOM 3025 C CB . VAL B 2 184 ? 13.505 29.317 -23.149 1.00 6.01 ? 169 VAL B CB 1 ATOM 3026 C CG1 . VAL B 2 184 ? 13.561 27.954 -23.821 1.00 8.44 ? 169 VAL B CG1 1 ATOM 3027 C CG2 . VAL B 2 184 ? 12.065 29.791 -23.021 1.00 4.66 ? 169 VAL B CG2 1 ATOM 3028 N N . LEU B 2 185 ? 15.602 31.202 -21.369 1.00 6.60 ? 170 LEU B N 1 ATOM 3029 C CA . LEU B 2 185 ? 15.911 32.540 -20.883 1.00 6.13 ? 170 LEU B CA 1 ATOM 3030 C C . LEU B 2 185 ? 15.481 33.582 -21.910 1.00 9.26 ? 170 LEU B C 1 ATOM 3031 O O . LEU B 2 185 ? 16.116 33.741 -22.952 1.00 20.97 ? 170 LEU B O 1 ATOM 3032 C CB . LEU B 2 185 ? 17.404 32.667 -20.570 1.00 9.11 ? 170 LEU B CB 1 ATOM 3033 C CG . LEU B 2 185 ? 17.862 33.797 -19.640 1.00 7.55 ? 170 LEU B CG 1 ATOM 3034 C CD1 . LEU B 2 185 ? 18.150 35.071 -20.410 1.00 9.80 ? 170 LEU B CD1 1 ATOM 3035 C CD2 . LEU B 2 185 ? 16.824 34.058 -18.562 1.00 14.98 ? 170 LEU B CD2 1 ATOM 3036 N N . GLN B 2 186 ? 14.395 34.285 -21.606 1.00 17.83 ? 171 GLN B N 1 ATOM 3037 C CA . GLN B 2 186 ? 13.837 35.281 -22.514 1.00 21.25 ? 171 GLN B CA 1 ATOM 3038 C C . GLN B 2 186 ? 14.735 36.511 -22.631 1.00 9.87 ? 171 GLN B C 1 ATOM 3039 O O . GLN B 2 186 ? 15.720 36.644 -21.905 1.00 9.64 ? 171 GLN B O 1 ATOM 3040 C CB . GLN B 2 186 ? 12.440 35.692 -22.048 1.00 11.41 ? 171 GLN B CB 1 ATOM 3041 C CG . GLN B 2 186 ? 11.457 34.536 -21.951 1.00 7.71 ? 171 GLN B CG 1 ATOM 3042 C CD . GLN B 2 186 ? 10.132 34.949 -21.342 1.00 13.64 ? 171 GLN B CD 1 ATOM 3043 O OE1 . GLN B 2 186 ? 9.077 34.432 -21.710 1.00 15.57 ? 171 GLN B OE1 1 ATOM 3044 N NE2 . GLN B 2 186 ? 10.180 35.882 -20.399 1.00 17.64 ? 171 GLN B NE2 1 ATOM 3045 N N . SER B 2 187 ? 14.388 37.410 -23.546 1.00 10.50 ? 172 SER B N 1 ATOM 3046 C CA . SER B 2 187 ? 15.172 38.621 -23.755 1.00 12.95 ? 172 SER B CA 1 ATOM 3047 C C . SER B 2 187 ? 15.002 39.595 -22.593 1.00 12.05 ? 172 SER B C 1 ATOM 3048 O O . SER B 2 187 ? 15.793 40.524 -22.430 1.00 16.29 ? 172 SER B O 1 ATOM 3049 C CB . SER B 2 187 ? 14.779 39.297 -25.069 1.00 11.90 ? 172 SER B CB 1 ATOM 3050 O OG . SER B 2 187 ? 13.428 39.722 -25.034 1.00 39.36 ? 172 SER B OG 1 ATOM 3051 N N . SER B 2 188 ? 13.968 39.375 -21.787 1.00 14.08 ? 173 SER B N 1 ATOM 3052 C CA . SER B 2 188 ? 13.697 40.226 -20.635 1.00 9.81 ? 173 SER B CA 1 ATOM 3053 C C . SER B 2 188 ? 14.589 39.863 -19.454 1.00 8.62 ? 173 SER B C 1 ATOM 3054 O O . SER B 2 188 ? 14.625 40.576 -18.452 1.00 17.87 ? 173 SER B O 1 ATOM 3055 C CB . SER B 2 188 ? 12.226 40.125 -20.225 1.00 16.12 ? 173 SER B CB 1 ATOM 3056 O OG . SER B 2 188 ? 11.892 38.801 -19.846 1.00 10.42 ? 173 SER B OG 1 ATOM 3057 N N . GLY B 2 189 ? 15.307 38.751 -19.578 1.00 8.09 ? 174 GLY B N 1 ATOM 3058 C CA . GLY B 2 189 ? 16.165 38.275 -18.510 1.00 7.01 ? 174 GLY B CA 1 ATOM 3059 C C . GLY B 2 189 ? 15.414 37.368 -17.557 1.00 9.93 ? 174 GLY B C 1 ATOM 3060 O O . GLY B 2 189 ? 15.953 36.936 -16.538 1.00 24.35 ? 174 GLY B O 1 ATOM 3061 N N . LEU B 2 190 ? 14.161 37.078 -17.893 1.00 9.96 ? 175 LEU B N 1 ATOM 3062 C CA . LEU B 2 190 ? 13.316 36.231 -17.062 1.00 7.90 ? 175 LEU B CA 1 ATOM 3063 C C . LEU B 2 190 ? 13.092 34.875 -17.720 1.00 12.11 ? 175 LEU B C 1 ATOM 3064 O O . LEU B 2 190 ? 12.962 34.782 -18.940 1.00 12.13 ? 175 LEU B O 1 ATOM 3065 C CB . LEU B 2 190 ? 11.974 36.915 -16.792 1.00 7.25 ? 175 LEU B CB 1 ATOM 3066 C CG . LEU B 2 190 ? 12.051 38.266 -16.081 1.00 6.76 ? 175 LEU B CG 1 ATOM 3067 C CD1 . LEU B 2 190 ? 10.666 38.857 -15.883 1.00 5.14 ? 175 LEU B CD1 1 ATOM 3068 C CD2 . LEU B 2 190 ? 12.767 38.119 -14.751 1.00 9.22 ? 175 LEU B CD2 1 ATOM 3069 N N . TYR B 2 191 ? 13.046 33.826 -16.906 1.00 6.55 ? 176 TYR B N 1 ATOM 3070 C CA . TYR B 2 191 ? 12.878 32.472 -17.418 1.00 6.99 ? 176 TYR B CA 1 ATOM 3071 C C . TYR B 2 191 ? 11.416 32.134 -17.682 1.00 9.64 ? 176 TYR B C 1 ATOM 3072 O O . TYR B 2 191 ? 10.512 32.742 -17.108 1.00 6.49 ? 176 TYR B O 1 ATOM 3073 C CB . TYR B 2 191 ? 13.481 31.457 -16.447 1.00 7.61 ? 176 TYR B CB 1 ATOM 3074 C CG . TYR B 2 191 ? 14.990 31.420 -16.470 1.00 9.93 ? 176 TYR B CG 1 ATOM 3075 C CD1 . TYR B 2 191 ? 15.668 30.667 -17.419 1.00 8.00 ? 176 TYR B CD1 1 ATOM 3076 C CD2 . TYR B 2 191 ? 15.737 32.138 -15.546 1.00 5.94 ? 176 TYR B CD2 1 ATOM 3077 C CE1 . TYR B 2 191 ? 17.047 30.630 -17.448 1.00 10.04 ? 176 TYR B CE1 1 ATOM 3078 C CE2 . TYR B 2 191 ? 17.118 32.106 -15.565 1.00 9.66 ? 176 TYR B CE2 1 ATOM 3079 C CZ . TYR B 2 191 ? 17.767 31.350 -16.519 1.00 8.45 ? 176 TYR B CZ 1 ATOM 3080 O OH . TYR B 2 191 ? 19.142 31.314 -16.545 1.00 22.18 ? 176 TYR B OH 1 ATOM 3081 N N . SER B 2 192 ? 11.198 31.157 -18.556 1.00 16.90 ? 177 SER B N 1 ATOM 3082 C CA . SER B 2 192 ? 9.854 30.709 -18.898 1.00 6.50 ? 177 SER B CA 1 ATOM 3083 C C . SER B 2 192 ? 9.861 29.258 -19.360 1.00 6.85 ? 177 SER B C 1 ATOM 3084 O O . SER B 2 192 ? 10.690 28.864 -20.179 1.00 16.63 ? 177 SER B O 1 ATOM 3085 C CB . SER B 2 192 ? 9.253 31.599 -19.986 1.00 5.97 ? 177 SER B CB 1 ATOM 3086 O OG . SER B 2 192 ? 8.026 31.068 -20.452 1.00 13.99 ? 177 SER B OG 1 ATOM 3087 N N . LEU B 2 193 ? 8.938 28.464 -18.826 1.00 6.74 ? 178 LEU B N 1 ATOM 3088 C CA . LEU B 2 193 ? 8.763 27.090 -19.278 1.00 5.07 ? 178 LEU B CA 1 ATOM 3089 C C . LEU B 2 193 ? 7.287 26.722 -19.267 1.00 11.31 ? 178 LEU B C 1 ATOM 3090 O O . LEU B 2 193 ? 6.468 27.424 -18.675 1.00 20.48 ? 178 LEU B O 1 ATOM 3091 C CB . LEU B 2 193 ? 9.568 26.114 -18.408 1.00 10.98 ? 178 LEU B CB 1 ATOM 3092 C CG . LEU B 2 193 ? 9.213 25.882 -16.934 1.00 6.98 ? 178 LEU B CG 1 ATOM 3093 C CD1 . LEU B 2 193 ? 8.196 24.761 -16.767 1.00 10.67 ? 178 LEU B CD1 1 ATOM 3094 C CD2 . LEU B 2 193 ? 10.466 25.571 -16.135 1.00 11.63 ? 178 LEU B CD2 1 ATOM 3095 N N . SER B 2 194 ? 6.955 25.619 -19.926 1.00 17.38 ? 179 SER B N 1 ATOM 3096 C CA . SER B 2 194 ? 5.588 25.122 -19.938 1.00 7.39 ? 179 SER B CA 1 ATOM 3097 C C . SER B 2 194 ? 5.568 23.621 -19.681 1.00 4.28 ? 179 SER B C 1 ATOM 3098 O O . SER B 2 194 ? 6.428 22.888 -20.169 1.00 5.31 ? 179 SER B O 1 ATOM 3099 C CB . SER B 2 194 ? 4.906 25.444 -21.270 1.00 8.83 ? 179 SER B CB 1 ATOM 3100 O OG . SER B 2 194 ? 5.686 24.994 -22.364 1.00 21.63 ? 179 SER B OG 1 ATOM 3101 N N . SER B 2 195 ? 4.592 23.171 -18.901 1.00 4.04 ? 180 SER B N 1 ATOM 3102 C CA . SER B 2 195 ? 4.432 21.749 -18.631 1.00 4.24 ? 180 SER B CA 1 ATOM 3103 C C . SER B 2 195 ? 3.133 21.240 -19.232 1.00 4.08 ? 180 SER B C 1 ATOM 3104 O O . SER B 2 195 ? 2.053 21.690 -18.855 1.00 8.39 ? 180 SER B O 1 ATOM 3105 C CB . SER B 2 195 ? 4.460 21.475 -17.127 1.00 6.41 ? 180 SER B CB 1 ATOM 3106 O OG . SER B 2 195 ? 4.322 20.089 -16.864 1.00 6.19 ? 180 SER B OG 1 ATOM 3107 N N . VAL B 2 196 ? 3.240 20.304 -20.168 1.00 7.35 ? 181 VAL B N 1 ATOM 3108 C CA . VAL B 2 196 ? 2.064 19.751 -20.827 1.00 5.74 ? 181 VAL B CA 1 ATOM 3109 C C . VAL B 2 196 ? 1.853 18.291 -20.447 1.00 11.30 ? 181 VAL B C 1 ATOM 3110 O O . VAL B 2 196 ? 2.774 17.619 -19.982 1.00 8.70 ? 181 VAL B O 1 ATOM 3111 C CB . VAL B 2 196 ? 2.171 19.862 -22.358 1.00 4.75 ? 181 VAL B CB 1 ATOM 3112 C CG1 . VAL B 2 196 ? 2.272 21.318 -22.777 1.00 3.65 ? 181 VAL B CG1 1 ATOM 3113 C CG2 . VAL B 2 196 ? 3.371 19.075 -22.862 1.00 5.15 ? 181 VAL B CG2 1 ATOM 3114 N N . VAL B 2 197 ? 0.633 17.806 -20.652 1.00 6.34 ? 182 VAL B N 1 ATOM 3115 C CA . VAL B 2 197 ? 0.296 16.419 -20.359 1.00 9.17 ? 182 VAL B CA 1 ATOM 3116 C C . VAL B 2 197 ? -0.822 15.932 -21.278 1.00 13.56 ? 182 VAL B C 1 ATOM 3117 O O . VAL B 2 197 ? -1.822 16.622 -21.476 1.00 37.53 ? 182 VAL B O 1 ATOM 3118 C CB . VAL B 2 197 ? -0.121 16.240 -18.878 1.00 13.50 ? 182 VAL B CB 1 ATOM 3119 C CG1 . VAL B 2 197 ? -1.143 17.292 -18.471 1.00 16.67 ? 182 VAL B CG1 1 ATOM 3120 C CG2 . VAL B 2 197 ? -0.653 14.836 -18.630 1.00 23.62 ? 182 VAL B CG2 1 ATOM 3121 N N . THR B 2 198 ? -0.640 14.747 -21.850 1.00 12.03 ? 183 THR B N 1 ATOM 3122 C CA . THR B 2 198 ? -1.639 14.170 -22.740 1.00 13.20 ? 183 THR B CA 1 ATOM 3123 C C . THR B 2 198 ? -2.549 13.204 -21.987 1.00 13.58 ? 183 THR B C 1 ATOM 3124 O O . THR B 2 198 ? -2.082 12.233 -21.391 1.00 16.21 ? 183 THR B O 1 ATOM 3125 C CB . THR B 2 198 ? -0.985 13.436 -23.924 1.00 13.26 ? 183 THR B CB 1 ATOM 3126 O OG1 . THR B 2 198 ? -0.103 12.420 -23.430 1.00 15.19 ? 183 THR B OG1 1 ATOM 3127 C CG2 . THR B 2 198 ? -0.193 14.411 -24.783 1.00 12.54 ? 183 THR B CG2 1 ATOM 3128 N N . VAL B 2 199 ? -3.848 13.482 -22.018 1.00 16.12 ? 184 VAL B N 1 ATOM 3129 C CA . VAL B 2 199 ? -4.833 12.660 -21.322 1.00 17.68 ? 184 VAL B CA 1 ATOM 3130 C C . VAL B 2 199 ? -5.956 12.246 -22.271 1.00 25.21 ? 184 VAL B C 1 ATOM 3131 O O . VAL B 2 199 ? -6.164 12.888 -23.300 1.00 22.71 ? 184 VAL B O 1 ATOM 3132 C CB . VAL B 2 199 ? -5.436 13.408 -20.114 1.00 16.04 ? 184 VAL B CB 1 ATOM 3133 C CG1 . VAL B 2 199 ? -4.356 13.733 -19.095 1.00 21.69 ? 184 VAL B CG1 1 ATOM 3134 C CG2 . VAL B 2 199 ? -6.150 14.672 -20.572 1.00 15.84 ? 184 VAL B CG2 1 ATOM 3135 N N . PRO B 2 200 ? -6.671 11.156 -21.939 1.00 20.74 ? 185 PRO B N 1 ATOM 3136 C CA . PRO B 2 200 ? -7.843 10.757 -22.726 1.00 21.85 ? 185 PRO B CA 1 ATOM 3137 C C . PRO B 2 200 ? -8.881 11.871 -22.823 1.00 26.91 ? 185 PRO B C 1 ATOM 3138 O O . PRO B 2 200 ? -9.148 12.547 -21.830 1.00 29.03 ? 185 PRO B O 1 ATOM 3139 C CB . PRO B 2 200 ? -8.396 9.564 -21.944 1.00 23.04 ? 185 PRO B CB 1 ATOM 3140 C CG . PRO B 2 200 ? -7.202 8.978 -21.283 1.00 21.54 ? 185 PRO B CG 1 ATOM 3141 C CD . PRO B 2 200 ? -6.324 10.145 -20.923 1.00 19.85 ? 185 PRO B CD 1 ATOM 3142 N N . SER B 2 201 ? -9.455 12.052 -24.009 1.00 42.42 ? 186 SER B N 1 ATOM 3143 C CA . SER B 2 201 ? -10.399 13.138 -24.255 1.00 30.64 ? 186 SER B CA 1 ATOM 3144 C C . SER B 2 201 ? -11.710 12.957 -23.495 1.00 32.66 ? 186 SER B C 1 ATOM 3145 O O . SER B 2 201 ? -12.458 13.915 -23.293 1.00 43.38 ? 186 SER B O 1 ATOM 3146 C CB . SER B 2 201 ? -10.686 13.259 -25.754 1.00 28.70 ? 186 SER B CB 1 ATOM 3147 O OG . SER B 2 201 ? -9.493 13.470 -26.486 1.00 36.74 ? 186 SER B OG 1 ATOM 3148 N N . SER B 2 202 ? -11.981 11.728 -23.072 1.00 32.92 ? 187 SER B N 1 ATOM 3149 C CA . SER B 2 202 ? -13.236 11.409 -22.402 1.00 35.84 ? 187 SER B CA 1 ATOM 3150 C C . SER B 2 202 ? -13.206 11.734 -20.911 1.00 44.28 ? 187 SER B C 1 ATOM 3151 O O . SER B 2 202 ? -14.169 11.466 -20.193 1.00 55.14 ? 187 SER B O 1 ATOM 3152 C CB . SER B 2 202 ? -13.579 9.932 -22.602 1.00 48.82 ? 187 SER B CB 1 ATOM 3153 O OG . SER B 2 202 ? -12.517 9.099 -22.171 1.00 45.20 ? 187 SER B OG 1 ATOM 3154 N N . SER B 2 203 ? -12.103 12.312 -20.448 1.00 37.29 ? 188 SER B N 1 ATOM 3155 C CA . SER B 2 203 ? -11.958 12.638 -19.034 1.00 31.10 ? 188 SER B CA 1 ATOM 3156 C C . SER B 2 203 ? -11.809 14.139 -18.810 1.00 32.72 ? 188 SER B C 1 ATOM 3157 O O . SER B 2 203 ? -11.450 14.578 -17.717 1.00 52.30 ? 188 SER B O 1 ATOM 3158 C CB . SER B 2 203 ? -10.758 11.902 -18.437 1.00 26.52 ? 188 SER B CB 1 ATOM 3159 O OG . SER B 2 203 ? -9.555 12.288 -19.078 1.00 33.53 ? 188 SER B OG 1 ATOM 3160 N N . LEU B 2 204 ? -12.089 14.924 -19.846 1.00 30.61 ? 189 LEU B N 1 ATOM 3161 C CA . LEU B 2 204 ? -12.002 16.377 -19.745 1.00 29.33 ? 189 LEU B CA 1 ATOM 3162 C C . LEU B 2 204 ? -13.248 16.963 -19.087 1.00 32.71 ? 189 LEU B C 1 ATOM 3163 O O . LEU B 2 204 ? -13.316 18.163 -18.821 1.00 43.56 ? 189 LEU B O 1 ATOM 3164 C CB . LEU B 2 204 ? -11.797 17.002 -21.127 1.00 27.32 ? 189 LEU B CB 1 ATOM 3165 C CG . LEU B 2 204 ? -10.470 16.705 -21.829 1.00 27.28 ? 189 LEU B CG 1 ATOM 3166 C CD1 . LEU B 2 204 ? -10.416 17.389 -23.185 1.00 31.65 ? 189 LEU B CD1 1 ATOM 3167 C CD2 . LEU B 2 204 ? -9.295 17.137 -20.966 1.00 24.22 ? 189 LEU B CD2 1 ATOM 3168 N N . GLY B 2 205 ? -14.232 16.109 -18.826 1.00 31.83 ? 190 GLY B N 1 ATOM 3169 C CA . GLY B 2 205 ? -15.472 16.541 -18.208 1.00 35.59 ? 190 GLY B CA 1 ATOM 3170 C C . GLY B 2 205 ? -15.683 15.948 -16.828 1.00 48.28 ? 190 GLY B C 1 ATOM 3171 O O . GLY B 2 205 ? -16.592 16.351 -16.102 1.00 70.14 ? 190 GLY B O 1 ATOM 3172 N N . THR B 2 206 ? -14.841 14.985 -16.466 1.00 40.42 ? 191 THR B N 1 ATOM 3173 C CA . THR B 2 206 ? -14.939 14.335 -15.164 1.00 47.45 ? 191 THR B CA 1 ATOM 3174 C C . THR B 2 206 ? -13.734 14.668 -14.291 1.00 54.88 ? 191 THR B C 1 ATOM 3175 O O . THR B 2 206 ? -13.870 15.285 -13.235 1.00 60.26 ? 191 THR B O 1 ATOM 3176 C CB . THR B 2 206 ? -15.050 12.806 -15.302 1.00 40.42 ? 191 THR B CB 1 ATOM 3177 O OG1 . THR B 2 206 ? -13.838 12.283 -15.861 1.00 58.74 ? 191 THR B OG1 1 ATOM 3178 C CG2 . THR B 2 206 ? -16.219 12.436 -16.201 1.00 47.44 ? 191 THR B CG2 1 ATOM 3179 N N . GLN B 2 207 ? -12.554 14.255 -14.744 1.00 50.51 ? 192 GLN B N 1 ATOM 3180 C CA . GLN B 2 207 ? -11.321 14.484 -14.001 1.00 33.98 ? 192 GLN B CA 1 ATOM 3181 C C . GLN B 2 207 ? -10.942 15.961 -13.962 1.00 29.65 ? 192 GLN B C 1 ATOM 3182 O O . GLN B 2 207 ? -11.041 16.667 -14.966 1.00 31.63 ? 192 GLN B O 1 ATOM 3183 C CB . GLN B 2 207 ? -10.175 13.668 -14.608 1.00 37.19 ? 192 GLN B CB 1 ATOM 3184 C CG . GLN B 2 207 ? -8.788 14.022 -14.082 1.00 42.69 ? 192 GLN B CG 1 ATOM 3185 C CD . GLN B 2 207 ? -8.542 13.540 -12.664 1.00 30.04 ? 192 GLN B CD 1 ATOM 3186 O OE1 . GLN B 2 207 ? -9.231 13.942 -11.726 1.00 31.96 ? 192 GLN B OE1 1 ATOM 3187 N NE2 . GLN B 2 207 ? -7.547 12.676 -12.501 1.00 33.33 ? 192 GLN B NE2 1 ATOM 3188 N N . THR B 2 208 ? -10.515 16.419 -12.790 1.00 29.87 ? 193 THR B N 1 ATOM 3189 C CA . THR B 2 208 ? -10.037 17.783 -12.619 1.00 26.99 ? 193 THR B CA 1 ATOM 3190 C C . THR B 2 208 ? -8.514 17.821 -12.672 1.00 22.92 ? 193 THR B C 1 ATOM 3191 O O . THR B 2 208 ? -7.842 17.117 -11.918 1.00 38.39 ? 193 THR B O 1 ATOM 3192 C CB . THR B 2 208 ? -10.518 18.383 -11.286 1.00 30.92 ? 193 THR B CB 1 ATOM 3193 O OG1 . THR B 2 208 ? -11.934 18.595 -11.338 1.00 38.44 ? 193 THR B OG1 1 ATOM 3194 C CG2 . THR B 2 208 ? -9.824 19.706 -11.014 1.00 25.64 ? 193 THR B CG2 1 ATOM 3195 N N . TYR B 2 209 ? -7.972 18.642 -13.565 1.00 18.74 ? 194 TYR B N 1 ATOM 3196 C CA . TYR B 2 209 ? -6.526 18.734 -13.727 1.00 16.53 ? 194 TYR B CA 1 ATOM 3197 C C . TYR B 2 209 ? -5.966 20.024 -13.137 1.00 24.01 ? 194 TYR B C 1 ATOM 3198 O O . TYR B 2 209 ? -6.346 21.123 -13.542 1.00 17.67 ? 194 TYR B O 1 ATOM 3199 C CB . TYR B 2 209 ? -6.150 18.623 -15.205 1.00 16.38 ? 194 TYR B CB 1 ATOM 3200 C CG . TYR B 2 209 ? -6.484 17.279 -15.809 1.00 19.55 ? 194 TYR B CG 1 ATOM 3201 C CD1 . TYR B 2 209 ? -5.669 16.177 -15.588 1.00 19.04 ? 194 TYR B CD1 1 ATOM 3202 C CD2 . TYR B 2 209 ? -7.613 17.112 -16.598 1.00 20.81 ? 194 TYR B CD2 1 ATOM 3203 C CE1 . TYR B 2 209 ? -5.969 14.947 -16.135 1.00 16.22 ? 194 TYR B CE1 1 ATOM 3204 C CE2 . TYR B 2 209 ? -7.922 15.884 -17.150 1.00 18.64 ? 194 TYR B CE2 1 ATOM 3205 C CZ . TYR B 2 209 ? -7.095 14.807 -16.917 1.00 16.58 ? 194 TYR B CZ 1 ATOM 3206 O OH . TYR B 2 209 ? -7.398 13.582 -17.462 1.00 37.68 ? 194 TYR B OH 1 ATOM 3207 N N . ILE B 2 210 ? -5.061 19.874 -12.175 1.00 13.65 ? 195 ILE B N 1 ATOM 3208 C CA . ILE B 2 210 ? -4.427 21.010 -11.516 1.00 12.40 ? 195 ILE B CA 1 ATOM 3209 C C . ILE B 2 210 ? -2.909 20.866 -11.535 1.00 11.11 ? 195 ILE B C 1 ATOM 3210 O O . ILE B 2 210 ? -2.372 19.850 -11.097 1.00 14.59 ? 195 ILE B O 1 ATOM 3211 C CB . ILE B 2 210 ? -4.901 21.156 -10.053 1.00 14.10 ? 195 ILE B CB 1 ATOM 3212 C CG1 . ILE B 2 210 ? -6.414 21.374 -9.996 1.00 20.23 ? 195 ILE B CG1 1 ATOM 3213 C CG2 . ILE B 2 210 ? -4.171 22.298 -9.363 1.00 16.66 ? 195 ILE B CG2 1 ATOM 3214 C CD1 . ILE B 2 210 ? -6.959 21.536 -8.594 1.00 12.97 ? 195 ILE B CD1 1 ATOM 3215 N N . CYS B 2 211 ? -2.219 21.881 -12.048 1.00 12.05 ? 196 CYS B N 1 ATOM 3216 C CA . CYS B 2 211 ? -0.761 21.874 -12.044 1.00 15.19 ? 196 CYS B CA 1 ATOM 3217 C C . CYS B 2 211 ? -0.238 22.583 -10.800 1.00 11.85 ? 196 CYS B C 1 ATOM 3218 O O . CYS B 2 211 ? -0.796 23.590 -10.366 1.00 20.95 ? 196 CYS B O 1 ATOM 3219 C CB . CYS B 2 211 ? -0.205 22.530 -13.312 1.00 12.74 ? 196 CYS B CB 1 ATOM 3220 S SG . CYS B 2 211 ? -0.283 24.338 -13.348 1.00 11.35 ? 196 CYS B SG 1 ATOM 3221 N N . ASN B 2 212 ? 0.833 22.048 -10.225 1.00 12.97 ? 197 ASN B N 1 ATOM 3222 C CA . ASN B 2 212 ? 1.404 22.614 -9.011 1.00 10.68 ? 197 ASN B CA 1 ATOM 3223 C C . ASN B 2 212 ? 2.769 23.234 -9.269 1.00 19.58 ? 197 ASN B C 1 ATOM 3224 O O . ASN B 2 212 ? 3.764 22.527 -9.426 1.00 15.03 ? 197 ASN B O 1 ATOM 3225 C CB . ASN B 2 212 ? 1.506 21.543 -7.930 1.00 8.05 ? 197 ASN B CB 1 ATOM 3226 C CG . ASN B 2 212 ? 0.233 20.737 -7.795 1.00 14.56 ? 197 ASN B CG 1 ATOM 3227 O OD1 . ASN B 2 212 ? 0.234 19.522 -7.982 1.00 10.22 ? 197 ASN B OD1 1 ATOM 3228 N ND2 . ASN B 2 212 ? -0.865 21.412 -7.474 1.00 17.34 ? 197 ASN B ND2 1 ATOM 3229 N N . VAL B 2 213 ? 2.808 24.560 -9.311 1.00 12.82 ? 198 VAL B N 1 ATOM 3230 C CA . VAL B 2 213 ? 4.036 25.281 -9.616 1.00 12.47 ? 198 VAL B CA 1 ATOM 3231 C C . VAL B 2 213 ? 4.690 25.814 -8.349 1.00 16.97 ? 198 VAL B C 1 ATOM 3232 O O . VAL B 2 213 ? 4.061 26.527 -7.567 1.00 37.10 ? 198 VAL B O 1 ATOM 3233 C CB . VAL B 2 213 ? 3.770 26.447 -10.583 1.00 12.18 ? 198 VAL B CB 1 ATOM 3234 C CG1 . VAL B 2 213 ? 5.043 27.238 -10.830 1.00 11.26 ? 198 VAL B CG1 1 ATOM 3235 C CG2 . VAL B 2 213 ? 3.198 25.924 -11.890 1.00 10.88 ? 198 VAL B CG2 1 ATOM 3236 N N . ASN B 2 214 ? 5.956 25.462 -8.151 1.00 15.56 ? 199 ASN B N 1 ATOM 3237 C CA . ASN B 2 214 ? 6.704 25.918 -6.987 1.00 17.85 ? 199 ASN B CA 1 ATOM 3238 C C . ASN B 2 214 ? 7.957 26.688 -7.384 1.00 17.35 ? 199 ASN B C 1 ATOM 3239 O O . ASN B 2 214 ? 8.664 26.304 -8.315 1.00 22.95 ? 199 ASN B O 1 ATOM 3240 C CB . ASN B 2 214 ? 7.079 24.731 -6.095 1.00 21.78 ? 199 ASN B CB 1 ATOM 3241 C CG . ASN B 2 214 ? 7.845 25.153 -4.854 1.00 32.02 ? 199 ASN B CG 1 ATOM 3242 O OD1 . ASN B 2 214 ? 9.073 25.070 -4.811 1.00 56.32 ? 199 ASN B OD1 1 ATOM 3243 N ND2 . ASN B 2 214 ? 7.122 25.612 -3.839 1.00 25.86 ? 199 ASN B ND2 1 ATOM 3244 N N . HIS B 2 215 ? 8.176 27.842 -6.789 1.00 17.17 ? 200 HIS B N 1 ATOM 3245 C CA . HIS B 2 215 ? 9.412 28.551 -6.987 1.00 14.60 ? 200 HIS B CA 1 ATOM 3246 C C . HIS B 2 215 ? 9.983 28.828 -5.631 1.00 18.54 ? 200 HIS B C 1 ATOM 3247 O O . HIS B 2 215 ? 9.506 29.680 -4.955 1.00 20.43 ? 200 HIS B O 1 ATOM 3248 C CB . HIS B 2 215 ? 9.111 29.857 -7.672 1.00 15.64 ? 200 HIS B CB 1 ATOM 3249 C CG . HIS B 2 215 ? 10.312 30.553 -8.203 1.00 14.12 ? 200 HIS B CG 1 ATOM 3250 N ND1 . HIS B 2 215 ? 10.469 31.912 -8.124 1.00 17.45 ? 200 HIS B ND1 1 ATOM 3251 C CD2 . HIS B 2 215 ? 11.409 30.081 -8.823 1.00 11.54 ? 200 HIS B CD2 1 ATOM 3252 C CE1 . HIS B 2 215 ? 11.614 32.249 -8.671 1.00 21.20 ? 200 HIS B CE1 1 ATOM 3253 N NE2 . HIS B 2 215 ? 12.208 31.154 -9.093 1.00 17.26 ? 200 HIS B NE2 1 ATOM 3254 N N . LYS B 2 216 ? 11.016 28.109 -5.239 1.00 19.04 ? 201 LYS B N 1 ATOM 3255 C CA . LYS B 2 216 ? 11.584 28.247 -3.915 1.00 18.97 ? 201 LYS B CA 1 ATOM 3256 C C . LYS B 2 216 ? 12.234 29.592 -3.665 1.00 21.83 ? 201 LYS B C 1 ATOM 3257 O O . LYS B 2 216 ? 12.163 30.121 -2.554 1.00 40.39 ? 201 LYS B O 1 ATOM 3258 C CB . LYS B 2 216 ? 12.542 27.105 -3.613 1.00 23.46 ? 201 LYS B CB 1 ATOM 3259 C CG . LYS B 2 216 ? 11.927 25.720 -3.483 1.00 33.62 ? 201 LYS B CG 1 ATOM 3260 C CD . LYS B 2 216 ? 12.936 24.612 -3.204 1.00 86.30 ? 201 LYS B CD 1 ATOM 3261 C CE . LYS B 2 216 ? 12.287 23.230 -3.053 1.00 103.21 ? 201 LYS B CE 1 ATOM 3262 N NZ . LYS B 2 216 ? 13.289 22.154 -2.805 1.00 66.26 ? 201 LYS B NZ 1 ATOM 3263 N N . PRO B 2 217 ? 12.929 30.135 -4.756 1.00 16.82 ? 202 PRO B N 1 ATOM 3264 C CA . PRO B 2 217 ? 13.568 31.413 -4.454 1.00 19.37 ? 202 PRO B CA 1 ATOM 3265 C C . PRO B 2 217 ? 12.617 32.497 -3.986 1.00 26.18 ? 202 PRO B C 1 ATOM 3266 O O . PRO B 2 217 ? 12.986 33.257 -3.106 1.00 39.35 ? 202 PRO B O 1 ATOM 3267 C CB . PRO B 2 217 ? 14.149 31.816 -5.786 1.00 22.96 ? 202 PRO B CB 1 ATOM 3268 C CG . PRO B 2 217 ? 14.624 30.567 -6.349 1.00 14.96 ? 202 PRO B CG 1 ATOM 3269 C CD . PRO B 2 217 ? 13.421 29.743 -6.166 1.00 17.88 ? 202 PRO B CD 1 ATOM 3270 N N . SER B 2 218 ? 11.439 32.598 -4.573 1.00 20.21 ? 203 SER B N 1 ATOM 3271 C CA . SER B 2 218 ? 10.494 33.614 -4.180 1.00 24.14 ? 203 SER B CA 1 ATOM 3272 C C . SER B 2 218 ? 9.498 33.122 -3.144 1.00 23.17 ? 203 SER B C 1 ATOM 3273 O O . SER B 2 218 ? 8.624 33.855 -2.722 1.00 27.36 ? 203 SER B O 1 ATOM 3274 C CB . SER B 2 218 ? 9.782 34.161 -5.396 1.00 17.35 ? 203 SER B CB 1 ATOM 3275 O OG . SER B 2 218 ? 8.790 33.275 -5.850 1.00 22.96 ? 203 SER B OG 1 ATOM 3276 N N . ASN B 2 219 ? 9.647 31.878 -2.729 1.00 24.03 ? 204 ASN B N 1 ATOM 3277 C CA . ASN B 2 219 ? 8.667 31.209 -1.888 1.00 26.25 ? 204 ASN B CA 1 ATOM 3278 C C . ASN B 2 219 ? 7.252 31.212 -2.459 1.00 22.65 ? 204 ASN B C 1 ATOM 3279 O O . ASN B 2 219 ? 6.296 31.531 -1.783 1.00 28.74 ? 204 ASN B O 1 ATOM 3280 C CB . ASN B 2 219 ? 8.712 31.712 -0.449 1.00 33.40 ? 204 ASN B CB 1 ATOM 3281 C CG . ASN B 2 219 ? 7.728 30.996 0.444 1.00 82.86 ? 204 ASN B CG 1 ATOM 3282 O OD1 . ASN B 2 219 ? 7.890 29.829 0.768 1.00 93.20 ? 204 ASN B OD1 1 ATOM 3283 N ND2 . ASN B 2 219 ? 6.676 31.690 0.814 1.00 83.48 ? 204 ASN B ND2 1 ATOM 3284 N N . THR B 2 220 ? 7.149 30.867 -3.733 1.00 20.46 ? 205 THR B N 1 ATOM 3285 C CA . THR B 2 220 ? 5.912 30.937 -4.470 1.00 18.23 ? 205 THR B CA 1 ATOM 3286 C C . THR B 2 220 ? 5.383 29.549 -4.743 1.00 20.44 ? 205 THR B C 1 ATOM 3287 O O . THR B 2 220 ? 6.048 28.749 -5.343 1.00 33.78 ? 205 THR B O 1 ATOM 3288 C CB . THR B 2 220 ? 6.159 31.602 -5.827 1.00 16.44 ? 205 THR B CB 1 ATOM 3289 O OG1 . THR B 2 220 ? 6.616 32.940 -5.640 1.00 14.15 ? 205 THR B OG1 1 ATOM 3290 C CG2 . THR B 2 220 ? 4.923 31.616 -6.657 1.00 16.15 ? 205 THR B CG2 1 ATOM 3291 N N . LYS B 2 221 ? 4.171 29.268 -4.305 1.00 21.63 ? 206 LYS B N 1 ATOM 3292 C CA . LYS B 2 221 ? 3.526 28.020 -4.636 1.00 22.48 ? 206 LYS B CA 1 ATOM 3293 C C . LYS B 2 221 ? 2.192 28.345 -5.251 1.00 25.34 ? 206 LYS B C 1 ATOM 3294 O O . LYS B 2 221 ? 1.447 29.105 -4.695 1.00 45.32 ? 206 LYS B O 1 ATOM 3295 C CB . LYS B 2 221 ? 3.333 27.183 -3.386 1.00 28.28 ? 206 LYS B CB 1 ATOM 3296 C CG . LYS B 2 221 ? 4.632 26.697 -2.775 1.00 51.32 ? 206 LYS B CG 1 ATOM 3297 C CD . LYS B 2 221 ? 4.390 25.882 -1.511 1.00 69.53 ? 206 LYS B CD 1 ATOM 3298 C CE . LYS B 2 221 ? 5.692 25.368 -0.903 1.00 92.42 ? 206 LYS B CE 1 ATOM 3299 N NZ . LYS B 2 221 ? 5.475 24.589 0.349 1.00 74.78 ? 206 LYS B NZ 1 ATOM 3300 N N . VAL B 2 222 ? 1.896 27.795 -6.413 1.00 31.26 ? 207 VAL B N 1 ATOM 3301 C CA . VAL B 2 222 ? 0.625 28.051 -7.073 1.00 21.52 ? 207 VAL B CA 1 ATOM 3302 C C . VAL B 2 222 ? -0.026 26.771 -7.516 1.00 19.05 ? 207 VAL B C 1 ATOM 3303 O O . VAL B 2 222 ? 0.620 25.956 -8.116 1.00 28.62 ? 207 VAL B O 1 ATOM 3304 C CB . VAL B 2 222 ? 0.827 28.901 -8.321 1.00 14.37 ? 207 VAL B CB 1 ATOM 3305 C CG1 . VAL B 2 222 ? -0.494 29.351 -8.867 1.00 12.14 ? 207 VAL B CG1 1 ATOM 3306 C CG2 . VAL B 2 222 ? 1.683 30.097 -7.999 1.00 19.36 ? 207 VAL B CG2 1 ATOM 3307 N N . ASP B 2 223 ? -1.310 26.607 -7.248 1.00 18.35 ? 208 ASP B N 1 ATOM 3308 C CA . ASP B 2 223 ? -2.063 25.524 -7.843 1.00 17.35 ? 208 ASP B CA 1 ATOM 3309 C C . ASP B 2 223 ? -3.003 26.132 -8.855 1.00 23.28 ? 208 ASP B C 1 ATOM 3310 O O . ASP B 2 223 ? -3.813 26.963 -8.519 1.00 19.56 ? 208 ASP B O 1 ATOM 3311 C CB . ASP B 2 223 ? -2.872 24.776 -6.792 1.00 18.91 ? 208 ASP B CB 1 ATOM 3312 C CG . ASP B 2 223 ? -2.024 23.952 -5.879 1.00 27.22 ? 208 ASP B CG 1 ATOM 3313 O OD1 . ASP B 2 223 ? -0.863 24.294 -5.676 1.00 41.08 ? 208 ASP B OD1 1 ATOM 3314 O OD2 . ASP B 2 223 ? -2.518 22.959 -5.350 1.00 35.30 ? 208 ASP B OD2 1 ATOM 3315 N N . LYS B 2 224 ? -2.903 25.710 -10.102 1.00 16.54 ? 209 LYS B N 1 ATOM 3316 C CA . LYS B 2 224 ? -3.741 26.277 -11.151 1.00 18.73 ? 209 LYS B CA 1 ATOM 3317 C C . LYS B 2 224 ? -4.720 25.262 -11.732 1.00 15.21 ? 209 LYS B C 1 ATOM 3318 O O . LYS B 2 224 ? -4.323 24.196 -12.200 1.00 15.13 ? 209 LYS B O 1 ATOM 3319 C CB . LYS B 2 224 ? -2.873 26.855 -12.271 1.00 14.32 ? 209 LYS B CB 1 ATOM 3320 C CG . LYS B 2 224 ? -3.656 27.652 -13.300 1.00 17.18 ? 209 LYS B CG 1 ATOM 3321 C CD . LYS B 2 224 ? -4.416 28.789 -12.638 1.00 22.87 ? 209 LYS B CD 1 ATOM 3322 C CE . LYS B 2 224 ? -5.275 29.543 -13.639 1.00 37.41 ? 209 LYS B CE 1 ATOM 3323 N NZ . LYS B 2 224 ? -6.015 30.665 -12.995 1.00 45.00 ? 209 LYS B NZ 1 ATOM 3324 N N . ARG B 2 225 ? -5.997 25.575 -11.776 1.00 16.15 ? 210 ARG B N 1 ATOM 3325 C CA . ARG B 2 225 ? -6.907 24.683 -12.448 1.00 19.44 ? 210 ARG B CA 1 ATOM 3326 C C . ARG B 2 225 ? -6.884 24.865 -13.953 1.00 22.83 ? 210 ARG B C 1 ATOM 3327 O O . ARG B 2 225 ? -6.956 25.969 -14.445 1.00 23.35 ? 210 ARG B O 1 ATOM 3328 C CB . ARG B 2 225 ? -8.308 24.885 -11.934 1.00 31.30 ? 210 ARG B CB 1 ATOM 3329 C CG . ARG B 2 225 ? -9.315 23.967 -12.576 1.00 48.53 ? 210 ARG B CG 1 ATOM 3330 C CD . ARG B 2 225 ? -10.657 24.185 -11.957 1.00 34.75 ? 210 ARG B CD 1 ATOM 3331 N NE . ARG B 2 225 ? -11.662 23.308 -12.523 1.00 51.17 ? 210 ARG B NE 1 ATOM 3332 C CZ . ARG B 2 225 ? -12.885 23.154 -12.034 1.00 87.38 ? 210 ARG B CZ 1 ATOM 3333 N NH1 . ARG B 2 225 ? -13.740 22.343 -12.636 1.00 56.02 ? 210 ARG B NH1 1 ATOM 3334 N NH2 . ARG B 2 225 ? -13.255 23.813 -10.949 1.00 59.04 ? 210 ARG B NH2 1 ATOM 3335 N N . VAL B 2 226 ? -6.771 23.764 -14.682 1.00 21.63 ? 211 VAL B N 1 ATOM 3336 C CA . VAL B 2 226 ? -6.810 23.820 -16.126 1.00 22.94 ? 211 VAL B CA 1 ATOM 3337 C C . VAL B 2 226 ? -8.095 23.181 -16.637 1.00 28.60 ? 211 VAL B C 1 ATOM 3338 O O . VAL B 2 226 ? -8.267 21.979 -16.598 1.00 35.30 ? 211 VAL B O 1 ATOM 3339 C CB . VAL B 2 226 ? -5.559 23.160 -16.731 1.00 18.31 ? 211 VAL B CB 1 ATOM 3340 C CG1 . VAL B 2 226 ? -5.489 23.378 -18.225 1.00 17.44 ? 211 VAL B CG1 1 ATOM 3341 C CG2 . VAL B 2 226 ? -4.325 23.743 -16.096 1.00 20.45 ? 211 VAL B CG2 1 ATOM 3342 N N . GLU B 2 227 ? -8.984 24.004 -17.163 1.00 32.88 ? 212 GLU B N 1 ATOM 3343 C CA . GLU B 2 227 ? -10.287 23.525 -17.555 1.00 39.63 ? 212 GLU B CA 1 ATOM 3344 C C . GLU B 2 227 ? -10.587 23.902 -18.976 1.00 40.99 ? 212 GLU B C 1 ATOM 3345 O O . GLU B 2 227 ? -10.102 24.904 -19.464 1.00 41.50 ? 212 GLU B O 1 ATOM 3346 C CB . GLU B 2 227 ? -11.387 24.068 -16.638 1.00 62.98 ? 212 GLU B CB 1 ATOM 3347 C CG . GLU B 2 227 ? -10.921 24.930 -15.478 1.00 61.09 ? 212 GLU B CG 1 ATOM 3348 C CD . GLU B 2 227 ? -11.636 26.265 -15.409 1.00 90.17 ? 212 GLU B CD 1 ATOM 3349 O OE1 . GLU B 2 227 ? -12.582 26.467 -16.200 1.00 97.19 ? 212 GLU B OE1 1 ATOM 3350 O OE2 . GLU B 2 227 ? -11.247 27.116 -14.575 1.00 86.37 ? 212 GLU B OE2 1 ATOM 3351 N N . PRO B 2 228 ? -11.433 23.013 -19.654 1.00 42.07 ? 213 PRO B N 1 ATOM 3352 C CA . PRO B 2 228 ? -11.719 23.421 -21.037 1.00 45.70 ? 213 PRO B CA 1 ATOM 3353 C C . PRO B 2 228 ? -12.451 24.738 -21.147 1.00 48.06 ? 213 PRO B C 1 ATOM 3354 O O . PRO B 2 228 ? -13.334 25.026 -20.376 1.00 51.78 ? 213 PRO B O 1 ATOM 3355 C CB . PRO B 2 228 ? -12.625 22.316 -21.547 1.00 54.84 ? 213 PRO B CB 1 ATOM 3356 C CG . PRO B 2 228 ? -12.169 21.121 -20.831 1.00 52.07 ? 213 PRO B CG 1 ATOM 3357 C CD . PRO B 2 228 ? -12.125 21.649 -19.457 1.00 38.86 ? 213 PRO B CD 1 ATOM 3358 N N . LYS B 2 229 ? -12.063 25.543 -22.118 1.00 55.82 ? 214 LYS B N 1 ATOM 3359 C CA . LYS B 2 229 ? -12.655 26.860 -22.292 1.00 71.95 ? 214 LYS B CA 1 ATOM 3360 C C . LYS B 2 229 ? -14.074 26.721 -22.789 1.00 83.48 ? 214 LYS B C 1 ATOM 3361 O O . LYS B 2 229 ? -14.387 25.811 -23.552 1.00 71.59 ? 214 LYS B O 1 ATOM 3362 C CB . LYS B 2 229 ? -11.830 27.722 -23.244 1.00 67.27 ? 214 LYS B CB 1 ATOM 3363 C CG . LYS B 2 229 ? -12.369 29.132 -23.401 1.00 88.35 ? 214 LYS B CG 1 ATOM 3364 C CD . LYS B 2 229 ? -11.690 29.907 -24.531 1.00 107.72 ? 214 LYS B CD 1 ATOM 3365 C CE . LYS B 2 229 ? -12.163 31.354 -24.664 1.00 78.78 ? 214 LYS B CE 1 ATOM 3366 N NZ . LYS B 2 229 ? -11.731 32.211 -23.525 1.00 65.96 ? 214 LYS B NZ 1 ATOM 3367 N N . SER B 2 230 ? -14.932 27.632 -22.355 1.00 80.83 ? 215 SER B N 1 ATOM 3368 C CA . SER B 2 230 ? -16.343 27.512 -22.622 1.00 88.03 ? 215 SER B CA 1 ATOM 3369 C C . SER B 2 230 ? -16.724 28.145 -23.942 1.00 70.69 ? 215 SER B C 1 ATOM 3370 O O . SER B 2 230 ? -17.283 27.477 -24.805 1.00 66.82 ? 215 SER B O 1 ATOM 3371 C CB . SER B 2 230 ? -17.141 28.119 -21.472 1.00 102.40 ? 215 SER B CB 1 ATOM 3372 O OG . SER B 2 230 ? -16.758 27.542 -20.229 1.00 97.66 ? 215 SER B OG 1 HETATM 3373 S S . SO4 C 3 . ? 35.325 -7.035 -17.588 1.00 30.00 ? 301 SO4 A S 1 HETATM 3374 O O1 . SO4 C 3 . ? 36.766 -7.004 -17.858 1.00 30.00 ? 301 SO4 A O1 1 HETATM 3375 O O2 . SO4 C 3 . ? 34.536 -7.396 -18.769 1.00 30.00 ? 301 SO4 A O2 1 HETATM 3376 O O3 . SO4 C 3 . ? 35.105 -8.047 -16.553 1.00 30.00 ? 301 SO4 A O3 1 HETATM 3377 O O4 . SO4 C 3 . ? 34.820 -5.732 -17.139 1.00 30.00 ? 301 SO4 A O4 1 HETATM 3378 S S . SO4 D 3 . ? 48.032 9.713 0.541 1.00 30.00 ? 301 SO4 B S 1 HETATM 3379 O O1 . SO4 D 3 . ? 49.310 10.108 0.024 1.00 30.00 ? 301 SO4 B O1 1 HETATM 3380 O O2 . SO4 D 3 . ? 47.410 9.148 -0.633 1.00 30.00 ? 301 SO4 B O2 1 HETATM 3381 O O3 . SO4 D 3 . ? 48.134 8.689 1.561 1.00 30.00 ? 301 SO4 B O3 1 HETATM 3382 O O4 . SO4 D 3 . ? 47.246 10.793 1.107 1.00 30.00 ? 301 SO4 B O4 1 HETATM 3383 S S . SO4 E 3 . ? 43.383 9.339 11.009 1.00 30.00 ? 302 SO4 B S 1 HETATM 3384 O O1 . SO4 E 3 . ? 44.697 8.746 10.729 1.00 30.00 ? 302 SO4 B O1 1 HETATM 3385 O O2 . SO4 E 3 . ? 42.579 9.276 9.781 1.00 30.00 ? 302 SO4 B O2 1 HETATM 3386 O O3 . SO4 E 3 . ? 42.726 8.590 12.088 1.00 30.00 ? 302 SO4 B O3 1 HETATM 3387 O O4 . SO4 E 3 . ? 43.520 10.740 11.415 1.00 30.00 ? 302 SO4 B O4 1 HETATM 3388 S S . SO4 F 3 . ? 32.048 9.555 12.623 1.00 30.00 ? 303 SO4 B S 1 HETATM 3389 O O1 . SO4 F 3 . ? 33.485 9.543 12.629 1.00 30.00 ? 303 SO4 B O1 1 HETATM 3390 O O2 . SO4 F 3 . ? 31.512 10.036 11.379 1.00 30.00 ? 303 SO4 B O2 1 HETATM 3391 O O3 . SO4 F 3 . ? 31.558 8.211 12.813 1.00 30.00 ? 303 SO4 B O3 1 HETATM 3392 O O4 . SO4 F 3 . ? 31.647 10.438 13.709 1.00 30.00 ? 303 SO4 B O4 1 HETATM 3393 S S . SO4 G 3 . ? 29.348 0.040 0.008 0.50 30.00 ? 304 SO4 B S 1 HETATM 3394 O O1 . SO4 G 3 . ? 30.137 -0.322 -1.182 1.00 30.00 ? 304 SO4 B O1 1 HETATM 3395 O O2 . SO4 G 3 . ? 28.445 1.151 -0.318 1.00 30.00 ? 304 SO4 B O2 1 HETATM 3396 O O3 . SO4 G 3 . ? 30.160 0.477 1.159 1.00 30.00 ? 304 SO4 B O3 1 HETATM 3397 O O4 . SO4 G 3 . ? 28.573 -1.155 0.362 1.00 30.00 ? 304 SO4 B O4 1 HETATM 3398 C C1 . NAG H 4 . ? 20.587 4.202 6.576 1.00 56.80 ? 305 NAG B C1 1 HETATM 3399 C C2 . NAG H 4 . ? 20.272 2.707 6.622 1.00 59.50 ? 305 NAG B C2 1 HETATM 3400 C C3 . NAG H 4 . ? 18.851 2.360 6.168 1.00 59.81 ? 305 NAG B C3 1 HETATM 3401 C C4 . NAG H 4 . ? 17.832 3.461 6.438 1.00 57.47 ? 305 NAG B C4 1 HETATM 3402 C C5 . NAG H 4 . ? 18.474 4.817 6.153 1.00 56.65 ? 305 NAG B C5 1 HETATM 3403 C C6 . NAG H 4 . ? 17.571 6.032 6.262 1.00 58.36 ? 305 NAG B C6 1 HETATM 3404 C C7 . NAG H 4 . ? 21.728 0.856 6.220 1.00 88.97 ? 305 NAG B C7 1 HETATM 3405 C C8 . NAG H 4 . ? 21.278 -0.372 5.484 1.00 100.83 ? 305 NAG B C8 1 HETATM 3406 N N2 . NAG H 4 . ? 21.239 2.012 5.796 1.00 69.87 ? 305 NAG B N2 1 HETATM 3407 O O3 . NAG H 4 . ? 18.403 1.174 6.788 1.00 67.97 ? 305 NAG B O3 1 HETATM 3408 O O4 . NAG H 4 . ? 16.786 3.196 5.540 1.00 62.60 ? 305 NAG B O4 1 HETATM 3409 O O5 . NAG H 4 . ? 19.524 4.984 7.055 1.00 49.61 ? 305 NAG B O5 1 HETATM 3410 O O6 . NAG H 4 . ? 17.364 5.911 7.663 1.00 58.92 ? 305 NAG B O6 1 HETATM 3411 O O7 . NAG H 4 . ? 22.483 0.767 7.183 1.00 88.74 ? 305 NAG B O7 1 HETATM 3412 O O . HOH I 5 . ? 35.645 -7.131 -17.595 1.00 30.00 ? 401 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLU 1 1 1 GLU GLU A . n A 1 2 ILE 2 2 2 ILE ILE A . n A 1 3 VAL 3 3 3 VAL VAL A . n A 1 4 LEU 4 4 4 LEU LEU A . n A 1 5 THR 5 5 5 THR THR A . n A 1 6 GLN 6 6 6 GLN GLN A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 PRO 8 8 8 PRO PRO A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 LEU 11 11 11 LEU LEU A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 SER 14 14 14 SER SER A . n A 1 15 PRO 15 15 15 PRO PRO A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 GLU 17 17 17 GLU GLU A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 THR 20 20 20 THR THR A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 SER 22 22 22 SER SER A . n A 1 23 CYS 23 23 23 CYS CYS A . n A 1 24 ARG 24 24 24 ARG ARG A . n A 1 25 ALA 25 25 25 ALA ALA A . n A 1 26 SER 26 26 26 SER SER A . n A 1 27 GLN 27 27 27 GLN GLN A . n A 1 28 SER 28 27 27 SER SER A A n A 1 29 VAL 29 28 28 VAL VAL A . n A 1 30 SER 30 29 29 SER SER A . n A 1 31 ALA 31 30 30 ALA ALA A . n A 1 32 LYS 32 31 31 LYS LYS A . n A 1 33 ASN 33 32 32 ASN ASN A . n A 1 34 LEU 34 33 33 LEU LEU A . n A 1 35 ALA 35 34 34 ALA ALA A . n A 1 36 TRP 36 35 35 TRP TRP A . n A 1 37 TYR 37 36 36 TYR TYR A . n A 1 38 GLN 38 37 37 GLN GLN A . n A 1 39 GLN 39 38 38 GLN GLN A . n A 1 40 LYS 40 39 39 LYS LYS A . n A 1 41 PRO 41 40 40 PRO PRO A . n A 1 42 GLY 42 41 41 GLY GLY A . n A 1 43 GLN 43 42 42 GLN GLN A . n A 1 44 THR 44 43 43 THR THR A . n A 1 45 PRO 45 44 44 PRO PRO A . n A 1 46 ARG 46 45 45 ARG ARG A . n A 1 47 LEU 47 46 46 LEU LEU A . n A 1 48 LEU 48 47 47 LEU LEU A . n A 1 49 MET 49 48 48 MET MET A . n A 1 50 TYR 50 49 49 TYR TYR A . n A 1 51 GLY 51 50 50 GLY GLY A . n A 1 52 VAL 52 51 51 VAL VAL A . n A 1 53 SER 53 52 52 SER SER A . n A 1 54 LEU 54 53 53 LEU LEU A . n A 1 55 ARG 55 54 54 ARG ARG A . n A 1 56 ASN 56 55 55 ASN ASN A . n A 1 57 THR 57 56 56 THR THR A . n A 1 58 GLY 58 57 57 GLY GLY A . n A 1 59 VAL 59 58 58 VAL VAL A . n A 1 60 PRO 60 59 59 PRO PRO A . n A 1 61 ASP 61 60 60 ASP ASP A . n A 1 62 ARG 62 61 61 ARG ARG A . n A 1 63 PHE 63 62 62 PHE PHE A . n A 1 64 SER 64 63 63 SER SER A . n A 1 65 GLY 65 64 64 GLY GLY A . n A 1 66 SER 66 65 65 SER SER A . n A 1 67 GLY 67 66 66 GLY GLY A . n A 1 68 SER 68 67 67 SER SER A . n A 1 69 GLY 69 68 68 GLY GLY A . n A 1 70 THR 70 69 69 THR THR A . n A 1 71 ASP 71 70 70 ASP ASP A . n A 1 72 PHE 72 71 71 PHE PHE A . n A 1 73 THR 73 72 72 THR THR A . n A 1 74 LEU 74 73 73 LEU LEU A . n A 1 75 THR 75 74 74 THR THR A . n A 1 76 ILE 76 75 75 ILE ILE A . n A 1 77 SER 77 76 76 SER SER A . n A 1 78 ARG 78 77 77 ARG ARG A . n A 1 79 LEU 79 78 78 LEU LEU A . n A 1 80 GLU 80 79 79 GLU GLU A . n A 1 81 PRO 81 80 80 PRO PRO A . n A 1 82 GLU 82 81 81 GLU GLU A . n A 1 83 ASP 83 82 82 ASP ASP A . n A 1 84 SER 84 83 83 SER SER A . n A 1 85 ALA 85 84 84 ALA ALA A . n A 1 86 VAL 86 85 85 VAL VAL A . n A 1 87 TYR 87 86 86 TYR TYR A . n A 1 88 PHE 88 87 87 PHE PHE A . n A 1 89 CYS 89 88 88 CYS CYS A . n A 1 90 GLN 90 89 89 GLN GLN A . n A 1 91 GLN 91 90 90 GLN GLN A . n A 1 92 TYR 92 91 91 TYR TYR A . n A 1 93 GLY 93 92 92 GLY GLY A . n A 1 94 THR 94 93 93 THR THR A . n A 1 95 SER 95 94 94 SER SER A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 THR 97 97 97 THR THR A . n A 1 98 PHE 98 98 98 PHE PHE A . n A 1 99 GLY 99 99 99 GLY GLY A . n A 1 100 GLN 100 100 100 GLN GLN A . n A 1 101 GLY 101 101 101 GLY GLY A . n A 1 102 THR 102 102 102 THR THR A . n A 1 103 LYS 103 103 103 LYS LYS A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 GLU 105 105 105 GLU GLU A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 LYS 107 107 107 LYS LYS A . n A 1 108 ARG 108 108 108 ARG ARG A . n A 1 109 THR 109 109 109 THR THR A . n A 1 110 VAL 110 110 110 VAL VAL A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 ALA 112 112 112 ALA ALA A . n A 1 113 PRO 113 113 113 PRO PRO A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 VAL 115 115 115 VAL VAL A . n A 1 116 PHE 116 116 116 PHE PHE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PHE 118 118 118 PHE PHE A . n A 1 119 PRO 119 119 119 PRO PRO A . n A 1 120 PRO 120 120 120 PRO PRO A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 ASP 122 122 122 ASP ASP A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 GLN 124 124 124 GLN GLN A . n A 1 125 LEU 125 125 125 LEU LEU A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 SER 127 127 127 SER SER A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 THR 129 129 129 THR THR A . n A 1 130 ALA 130 130 130 ALA ALA A . n A 1 131 SER 131 131 131 SER SER A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 VAL 133 133 133 VAL VAL A . n A 1 134 CYS 134 134 134 CYS CYS A . n A 1 135 LEU 135 135 135 LEU LEU A . n A 1 136 LEU 136 136 136 LEU LEU A . n A 1 137 ASN 137 137 137 ASN ASN A . n A 1 138 ASN 138 138 138 ASN ASN A . n A 1 139 PHE 139 139 139 PHE PHE A . n A 1 140 TYR 140 140 140 TYR TYR A . n A 1 141 PRO 141 141 141 PRO PRO A . n A 1 142 ARG 142 142 142 ARG ARG A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 ALA 144 144 144 ALA ALA A . n A 1 145 LYS 145 145 145 LYS LYS A . n A 1 146 VAL 146 146 146 VAL VAL A . n A 1 147 GLN 147 147 147 GLN GLN A . n A 1 148 TRP 148 148 148 TRP TRP A . n A 1 149 LYS 149 149 149 LYS LYS A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 ASP 151 151 151 ASP ASP A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 ALA 153 153 153 ALA ALA A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 GLN 155 155 155 GLN GLN A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 ASN 158 158 158 ASN ASN A . n A 1 159 SER 159 159 159 SER SER A . n A 1 160 GLN 160 160 160 GLN GLN A . n A 1 161 GLU 161 161 161 GLU GLU A . n A 1 162 SER 162 162 162 SER SER A . n A 1 163 VAL 163 163 163 VAL VAL A . n A 1 164 THR 164 164 164 THR THR A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 GLN 166 166 166 GLN GLN A . n A 1 167 ASP 167 167 167 ASP ASP A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 LYS 169 169 169 LYS LYS A . n A 1 170 ASP 170 170 170 ASP ASP A . n A 1 171 SER 171 171 171 SER SER A . n A 1 172 THR 172 172 172 THR THR A . n A 1 173 TYR 173 173 173 TYR TYR A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 SER 177 177 177 SER SER A . n A 1 178 THR 178 178 178 THR THR A . n A 1 179 LEU 179 179 179 LEU LEU A . n A 1 180 THR 180 180 180 THR THR A . n A 1 181 LEU 181 181 181 LEU LEU A . n A 1 182 SER 182 182 182 SER SER A . n A 1 183 LYS 183 183 183 LYS LYS A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ASP 185 185 185 ASP ASP A . n A 1 186 TYR 186 186 186 TYR TYR A . n A 1 187 GLU 187 187 187 GLU GLU A . n A 1 188 LYS 188 188 188 LYS LYS A . n A 1 189 HIS 189 189 189 HIS HIS A . n A 1 190 LYS 190 190 190 LYS LYS A . n A 1 191 VAL 191 191 191 VAL VAL A . n A 1 192 TYR 192 192 192 TYR TYR A . n A 1 193 ALA 193 193 193 ALA ALA A . n A 1 194 CYS 194 194 194 CYS CYS A . n A 1 195 GLU 195 195 195 GLU GLU A . n A 1 196 VAL 196 196 196 VAL VAL A . n A 1 197 THR 197 197 197 THR THR A . n A 1 198 HIS 198 198 198 HIS HIS A . n A 1 199 GLN 199 199 199 GLN GLN A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 SER 202 202 202 SER SER A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 PRO 204 204 204 PRO PRO A . n A 1 205 VAL 205 205 205 VAL VAL A . n A 1 206 THR 206 206 206 THR THR A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 PHE 209 209 209 PHE PHE A . n A 1 210 ASN 210 210 210 ASN ASN A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 GLU 213 213 213 GLU GLU A . n A 1 214 CYS 214 214 ? ? ? A . n B 2 1 GLN 1 1 1 GLN GLN B . n B 2 2 VAL 2 2 2 VAL VAL B . n B 2 3 GLN 3 3 3 GLN GLN B . n B 2 4 LEU 4 4 4 LEU LEU B . n B 2 5 GLN 5 5 5 GLN GLN B . n B 2 6 GLN 6 6 6 GLN GLN B . n B 2 7 TRP 7 7 7 TRP TRP B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 ALA 9 9 9 ALA ALA B . n B 2 10 GLY 10 10 10 GLY GLY B . n B 2 11 LEU 11 11 11 LEU LEU B . n B 2 12 LEU 12 12 12 LEU LEU B . n B 2 13 LYS 13 13 13 LYS LYS B . n B 2 14 PRO 14 14 14 PRO PRO B . n B 2 15 SER 15 15 15 SER SER B . n B 2 16 GLU 16 16 16 GLU GLU B . n B 2 17 THR 17 17 17 THR THR B . n B 2 18 LEU 18 18 18 LEU LEU B . n B 2 19 SER 19 19 19 SER SER B . n B 2 20 LEU 20 20 20 LEU LEU B . n B 2 21 THR 21 21 21 THR THR B . n B 2 22 CYS 22 22 22 CYS CYS B . n B 2 23 ALA 23 23 23 ALA ALA B . n B 2 24 VAL 24 24 24 VAL VAL B . n B 2 25 TYR 25 25 25 TYR TYR B . n B 2 26 ASN 26 26 26 ASN ASN B . n B 2 27 GLU 27 27 27 GLU GLU B . n B 2 28 SER 28 28 28 SER SER B . n B 2 29 LEU 29 29 29 LEU LEU B . n B 2 30 SER 30 30 30 SER SER B . n B 2 31 ALA 31 31 31 ALA ALA B . n B 2 32 PHE 32 32 32 PHE PHE B . n B 2 33 SER 33 33 33 SER SER B . n B 2 34 TRP 34 34 34 TRP TRP B . n B 2 35 SER 35 35 35 SER SER B . n B 2 36 TRP 36 36 36 TRP TRP B . n B 2 37 ILE 37 37 37 ILE ILE B . n B 2 38 ARG 38 38 38 ARG ARG B . n B 2 39 GLN 39 39 39 GLN GLN B . n B 2 40 PHE 40 40 40 PHE PHE B . n B 2 41 PRO 41 41 41 PRO PRO B . n B 2 42 GLY 42 42 42 GLY GLY B . n B 2 43 GLN 43 43 43 GLN GLN B . n B 2 44 GLY 44 44 44 GLY GLY B . n B 2 45 LEU 45 45 45 LEU LEU B . n B 2 46 GLU 46 46 46 GLU GLU B . n B 2 47 TRP 47 47 47 TRP TRP B . n B 2 48 ILE 48 48 48 ILE ILE B . n B 2 49 GLY 49 49 49 GLY GLY B . n B 2 50 GLU 50 50 50 GLU GLU B . n B 2 51 ILE 51 51 51 ILE ILE B . n B 2 52 ASP 52 52 52 ASP ASP B . n B 2 53 HIS 53 53 53 HIS HIS B . n B 2 54 THR 54 54 54 THR THR B . n B 2 55 THR 55 55 55 THR THR B . n B 2 56 SER 56 56 56 SER SER B . n B 2 57 SER 57 57 57 SER SER B . n B 2 58 ASN 58 58 58 ASN ASN B . n B 2 59 TYR 59 59 59 TYR TYR B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 PRO 61 61 61 PRO PRO B . n B 2 62 SER 62 62 62 SER SER B . n B 2 63 LEU 63 63 63 LEU LEU B . n B 2 64 LYS 64 64 64 LYS LYS B . n B 2 65 ARG 65 65 65 ARG ARG B . n B 2 66 ARG 66 66 66 ARG ARG B . n B 2 67 ILE 67 67 67 ILE ILE B . n B 2 68 ASN 68 68 68 ASN ASN B . n B 2 69 ILE 69 69 69 ILE ILE B . n B 2 70 SER 70 70 70 SER SER B . n B 2 71 ILE 71 71 71 ILE ILE B . n B 2 72 ASP 72 72 72 ASP ASP B . n B 2 73 THR 73 73 73 THR THR B . n B 2 74 SER 74 74 74 SER SER B . n B 2 75 LYS 75 75 75 LYS LYS B . n B 2 76 LYS 76 76 76 LYS LYS B . n B 2 77 GLN 77 77 77 GLN GLN B . n B 2 78 PHE 78 78 78 PHE PHE B . n B 2 79 SER 79 79 79 SER SER B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 LYS 81 81 81 LYS LYS B . n B 2 82 LEU 82 82 82 LEU LEU B . n B 2 83 TYR 83 82 82 TYR TYR B A n B 2 84 SER 84 82 82 SER SER B B n B 2 85 VAL 85 82 82 VAL VAL B C n B 2 86 THR 86 83 83 THR THR B . n B 2 87 ALA 87 84 84 ALA ALA B . n B 2 88 ALA 88 85 85 ALA ALA B . n B 2 89 ASP 89 86 86 ASP ASP B . n B 2 90 THR 90 87 87 THR THR B . n B 2 91 ALA 91 88 88 ALA ALA B . n B 2 92 VAL 92 89 89 VAL VAL B . n B 2 93 TYR 93 90 90 TYR TYR B . n B 2 94 TYR 94 91 91 TYR TYR B . n B 2 95 CYS 95 92 92 CYS CYS B . n B 2 96 ALA 96 93 93 ALA ALA B . n B 2 97 ARG 97 94 94 ARG ARG B . n B 2 98 GLY 98 95 95 GLY GLY B . n B 2 99 GLY 99 96 96 GLY GLY B . n B 2 100 ARG 100 97 97 ARG ARG B . n B 2 101 LYS 101 98 98 LYS LYS B . n B 2 102 VAL 102 99 99 VAL VAL B . n B 2 103 TYR 103 100 100 TYR TYR B . n B 2 104 HIS 104 100 100 HIS HIS B A n B 2 105 ALA 105 100 100 ALA ALA B B n B 2 106 TYR 106 100 100 TYR TYR B C n B 2 107 TRP 107 100 100 TRP TRP B D n B 2 108 SER 108 100 100 SER SER B E n B 2 109 GLY 109 100 100 GLY GLY B F n B 2 110 TYR 110 100 100 TYR TYR B G n B 2 111 VAL 111 100 100 VAL VAL B H n B 2 112 ASN 112 100 100 ASN ASN B I n B 2 113 ASN 113 100 100 ASN ASN B J n B 2 114 CYS 114 100 100 CYS CYS B K n B 2 115 PHE 115 100 100 PHE PHE B L n B 2 116 ASP 116 101 101 ASP ASP B . n B 2 117 PRO 117 102 102 PRO PRO B . n B 2 118 TRP 118 103 103 TRP TRP B . n B 2 119 GLY 119 104 104 GLY GLY B . n B 2 120 GLN 120 105 105 GLN GLN B . n B 2 121 GLY 121 106 106 GLY GLY B . n B 2 122 THR 122 107 107 THR THR B . n B 2 123 LEU 123 108 108 LEU LEU B . n B 2 124 VAL 124 109 109 VAL VAL B . n B 2 125 THR 125 110 110 THR THR B . n B 2 126 VAL 126 111 111 VAL VAL B . n B 2 127 SER 127 112 112 SER SER B . n B 2 128 SER 128 113 113 SER SER B . n B 2 129 ALA 129 114 114 ALA ALA B . n B 2 130 SER 130 115 115 SER SER B . n B 2 131 THR 131 116 116 THR THR B . n B 2 132 LYS 132 117 117 LYS LYS B . n B 2 133 GLY 133 118 118 GLY GLY B . n B 2 134 PRO 134 119 119 PRO PRO B . n B 2 135 SER 135 120 120 SER SER B . n B 2 136 VAL 136 121 121 VAL VAL B . n B 2 137 PHE 137 122 122 PHE PHE B . n B 2 138 PRO 138 123 123 PRO PRO B . n B 2 139 LEU 139 124 124 LEU LEU B . n B 2 140 ALA 140 125 125 ALA ALA B . n B 2 141 PRO 141 126 126 PRO PRO B . n B 2 142 SER 142 127 127 SER SER B . n B 2 143 SER 143 128 128 SER SER B . n B 2 144 LYS 144 129 129 LYS LYS B . n B 2 145 SER 145 130 130 SER SER B . n B 2 146 THR 146 131 131 THR THR B . n B 2 147 SER 147 132 132 SER SER B . n B 2 148 GLY 148 133 133 GLY GLY B . n B 2 149 GLY 149 134 134 GLY GLY B . n B 2 150 THR 150 135 135 THR THR B . n B 2 151 ALA 151 136 136 ALA ALA B . n B 2 152 ALA 152 137 137 ALA ALA B . n B 2 153 LEU 153 138 138 LEU LEU B . n B 2 154 GLY 154 139 139 GLY GLY B . n B 2 155 CYS 155 140 140 CYS CYS B . n B 2 156 LEU 156 141 141 LEU LEU B . n B 2 157 VAL 157 142 142 VAL VAL B . n B 2 158 LYS 158 143 143 LYS LYS B . n B 2 159 ASP 159 144 144 ASP ASP B . n B 2 160 TYR 160 145 145 TYR TYR B . n B 2 161 PHE 161 146 146 PHE PHE B . n B 2 162 PRO 162 147 147 PRO PRO B . n B 2 163 GLU 163 148 148 GLU GLU B . n B 2 164 PRO 164 149 149 PRO PRO B . n B 2 165 VAL 165 150 150 VAL VAL B . n B 2 166 THR 166 151 151 THR THR B . n B 2 167 VAL 167 152 152 VAL VAL B . n B 2 168 SER 168 153 153 SER SER B . n B 2 169 TRP 169 154 154 TRP TRP B . n B 2 170 ASN 170 155 155 ASN ASN B . n B 2 171 SER 171 156 156 SER SER B . n B 2 172 GLY 172 157 157 GLY GLY B . n B 2 173 ALA 173 158 158 ALA ALA B . n B 2 174 LEU 174 159 159 LEU LEU B . n B 2 175 THR 175 160 160 THR THR B . n B 2 176 SER 176 161 161 SER SER B . n B 2 177 GLY 177 162 162 GLY GLY B . n B 2 178 VAL 178 163 163 VAL VAL B . n B 2 179 HIS 179 164 164 HIS HIS B . n B 2 180 THR 180 165 165 THR THR B . n B 2 181 PHE 181 166 166 PHE PHE B . n B 2 182 PRO 182 167 167 PRO PRO B . n B 2 183 ALA 183 168 168 ALA ALA B . n B 2 184 VAL 184 169 169 VAL VAL B . n B 2 185 LEU 185 170 170 LEU LEU B . n B 2 186 GLN 186 171 171 GLN GLN B . n B 2 187 SER 187 172 172 SER SER B . n B 2 188 SER 188 173 173 SER SER B . n B 2 189 GLY 189 174 174 GLY GLY B . n B 2 190 LEU 190 175 175 LEU LEU B . n B 2 191 TYR 191 176 176 TYR TYR B . n B 2 192 SER 192 177 177 SER SER B . n B 2 193 LEU 193 178 178 LEU LEU B . n B 2 194 SER 194 179 179 SER SER B . n B 2 195 SER 195 180 180 SER SER B . n B 2 196 VAL 196 181 181 VAL VAL B . n B 2 197 VAL 197 182 182 VAL VAL B . n B 2 198 THR 198 183 183 THR THR B . n B 2 199 VAL 199 184 184 VAL VAL B . n B 2 200 PRO 200 185 185 PRO PRO B . n B 2 201 SER 201 186 186 SER SER B . n B 2 202 SER 202 187 187 SER SER B . n B 2 203 SER 203 188 188 SER SER B . n B 2 204 LEU 204 189 189 LEU LEU B . n B 2 205 GLY 205 190 190 GLY GLY B . n B 2 206 THR 206 191 191 THR THR B . n B 2 207 GLN 207 192 192 GLN GLN B . n B 2 208 THR 208 193 193 THR THR B . n B 2 209 TYR 209 194 194 TYR TYR B . n B 2 210 ILE 210 195 195 ILE ILE B . n B 2 211 CYS 211 196 196 CYS CYS B . n B 2 212 ASN 212 197 197 ASN ASN B . n B 2 213 VAL 213 198 198 VAL VAL B . n B 2 214 ASN 214 199 199 ASN ASN B . n B 2 215 HIS 215 200 200 HIS HIS B . n B 2 216 LYS 216 201 201 LYS LYS B . n B 2 217 PRO 217 202 202 PRO PRO B . n B 2 218 SER 218 203 203 SER SER B . n B 2 219 ASN 219 204 204 ASN ASN B . n B 2 220 THR 220 205 205 THR THR B . n B 2 221 LYS 221 206 206 LYS LYS B . n B 2 222 VAL 222 207 207 VAL VAL B . n B 2 223 ASP 223 208 208 ASP ASP B . n B 2 224 LYS 224 209 209 LYS LYS B . n B 2 225 ARG 225 210 210 ARG ARG B . n B 2 226 VAL 226 211 211 VAL VAL B . n B 2 227 GLU 227 212 212 GLU GLU B . n B 2 228 PRO 228 213 213 PRO PRO B . n B 2 229 LYS 229 214 214 LYS LYS B . n B 2 230 SER 230 215 215 SER SER B . n B 2 231 CYS 231 216 ? ? ? B . n B 2 232 ASP 232 217 ? ? ? 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 3 SO4 1 301 1 SO4 SO4 A . D 3 SO4 1 301 1 SO4 SO4 B . E 3 SO4 1 302 1 SO4 SO4 B . F 3 SO4 1 303 1 SO4 SO4 B . G 3 SO4 1 304 1 SO4 SO4 B . H 4 NAG 1 305 302 NAG NAG B . I 5 HOH 1 401 1 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 4000 ? 1 MORE -57 ? 1 'SSA (A^2)' 20790 ? # _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 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id B _pdbx_struct_special_symmetry.auth_comp_id SO4 _pdbx_struct_special_symmetry.auth_seq_id 304 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id G _pdbx_struct_special_symmetry.label_comp_id SO4 _pdbx_struct_special_symmetry.label_seq_id . # 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 2016-05-25 2 'Structure model' 1 1 2016-07-27 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Data collection' # 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 ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.9_1692 1 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 3 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 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 S A SO4 301 ? ? O A HOH 401 ? ? 0.33 2 1 O1 A SO4 301 ? ? O A HOH 401 ? ? 1.16 3 1 O3 A SO4 301 ? ? O A HOH 401 ? ? 1.49 4 1 O2 A SO4 301 ? ? O A HOH 401 ? ? 1.64 5 1 O4 A SO4 301 ? ? O A HOH 401 ? ? 1.69 6 1 ND2 B ASN 26 ? ? O5 B NAG 305 ? ? 1.72 7 1 CB A PRO 40 ? ? OE1 A GLU 165 ? ? 1.95 8 1 OD1 B ASN 60 ? ? OG B SER 62 ? ? 1.98 9 1 CB B CYS 22 ? ? SG B CYS 92 ? ? 2.08 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O2 B SO4 304 ? ? 1_555 O4 B SO4 304 ? ? 8_555 0.14 2 1 O1 B SO4 304 ? ? 1_555 O3 B SO4 304 ? ? 8_555 0.16 3 1 S B SO4 304 ? ? 1_555 O4 B SO4 304 ? ? 8_555 1.41 4 1 S B SO4 304 ? ? 1_555 O1 B SO4 304 ? ? 8_555 1.44 5 1 S B SO4 304 ? ? 1_555 O3 B SO4 304 ? ? 8_555 1.51 6 1 S B SO4 304 ? ? 1_555 O2 B SO4 304 ? ? 8_555 1.53 7 1 CB A SER 12 ? ? 1_555 NZ B LYS 206 ? ? 5_554 1.95 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 C A SER 7 ? ? N A PRO 8 ? ? CD A PRO 8 ? ? 138.03 120.60 17.43 2.20 Y 2 1 N A ASP 60 ? ? CA A ASP 60 ? ? C A ASP 60 ? ? 136.55 111.00 25.55 2.70 N 3 1 CA A ASP 60 ? ? C A ASP 60 ? ? O A ASP 60 ? ? 133.71 120.10 13.61 2.10 N 4 1 CA A ASP 60 ? ? C A ASP 60 ? ? N A ARG 61 ? ? 100.91 117.20 -16.29 2.20 Y 5 1 N A ASN 138 ? ? CA A ASN 138 ? ? C A ASN 138 ? ? 133.55 111.00 22.55 2.70 N 6 1 C A TYR 140 ? ? N A PRO 141 ? ? CD A PRO 141 ? ? 137.53 120.60 16.93 2.20 Y 7 1 CA A PRO 141 ? ? N A PRO 141 ? ? CD A PRO 141 ? ? 98.41 111.50 -13.09 1.40 N 8 1 C B ASP 101 ? ? N B PRO 102 ? ? CD B PRO 102 ? ? 139.18 120.60 18.58 2.20 Y 9 1 C B PHE 146 ? ? N B PRO 147 ? ? CD B PRO 147 ? ? 140.92 120.60 20.32 2.20 Y 10 1 C B GLU 148 ? ? N B PRO 149 ? ? CD B PRO 149 ? ? 138.78 120.60 18.18 2.20 Y # 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 VAL A 51 ? ? 72.74 -59.90 2 1 THR A 93 ? ? -117.42 -156.29 3 1 LYS A 169 ? ? -93.85 -60.71 4 1 VAL B 100 H ? -98.90 -69.79 5 1 ASP B 144 ? ? 57.35 76.56 6 1 PRO B 147 ? ? -87.95 -156.90 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 B HIS 100 A CG ? B HIS 104 CG 2 1 Y 1 B HIS 100 A ND1 ? B HIS 104 ND1 3 1 Y 1 B HIS 100 A CD2 ? B HIS 104 CD2 4 1 Y 1 B HIS 100 A CE1 ? B HIS 104 CE1 5 1 Y 1 B HIS 100 A NE2 ? B HIS 104 NE2 6 1 Y 1 B TRP 100 D CG ? B TRP 107 CG 7 1 Y 1 B TRP 100 D CD1 ? B TRP 107 CD1 8 1 Y 1 B TRP 100 D CD2 ? B TRP 107 CD2 9 1 Y 1 B TRP 100 D NE1 ? B TRP 107 NE1 10 1 Y 1 B TRP 100 D CE2 ? B TRP 107 CE2 11 1 Y 1 B TRP 100 D CE3 ? B TRP 107 CE3 12 1 Y 1 B TRP 100 D CZ2 ? B TRP 107 CZ2 13 1 Y 1 B TRP 100 D CZ3 ? B TRP 107 CZ3 14 1 Y 1 B TRP 100 D CH2 ? B TRP 107 CH2 # 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 CYS 214 ? A CYS 214 2 1 Y 1 B CYS 216 ? B CYS 231 3 1 Y 1 B ASP 217 ? B ASP 232 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'SULFATE ION' SO4 4 N-ACETYL-D-GLUCOSAMINE NAG 5 water HOH #