data_4MCZ # _entry.id 4MCZ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4MCZ RCSB RCSB081755 WWPDB D_1000081755 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCY . unspecified PDB 4MD0 . unspecified PDB 4MD4 . unspecified PDB 4MD5 . unspecified PDB 4MDI . unspecified PDB 4MDJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCZ _pdbx_database_status.recvd_initial_deposition_date 2013-08-22 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Scally, S.W.' 1 'Rossjohn, J.' 2 # _citation.id primary _citation.title 'A molecular basis for the association of the HLA-DRB1 locus, citrullination, and rheumatoid arthritis.' _citation.journal_abbrev J.Exp.Med. _citation.journal_volume 210 _citation.page_first 2569 _citation.page_last 2582 _citation.year 2013 _citation.journal_id_ASTM JEMEAV _citation.country US _citation.journal_id_ISSN 0022-1007 _citation.journal_id_CSD 0774 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24190431 _citation.pdbx_database_id_DOI 10.1084/jem.20131241 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Scally, S.W.' 1 primary 'Petersen, J.' 2 primary 'Law, S.C.' 3 primary 'Dudek, N.L.' 4 primary 'Nel, H.J.' 5 primary 'Loh, K.L.' 6 primary 'Wijeyewickrema, L.C.' 7 primary 'Eckle, S.B.' 8 primary 'van Heemst, J.' 9 primary 'Pike, R.N.' 10 primary 'McCluskey, J.' 11 primary 'Toes, R.E.' 12 primary 'La Gruta, N.L.' 13 primary 'Purcell, A.W.' 14 primary 'Reid, H.H.' 15 primary 'Thomas, R.' 16 primary 'Rossjohn, J.' 17 # _cell.entry_id 4MCZ _cell.length_a 67.110 _cell.length_b 183.430 _cell.length_c 77.280 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4MCZ _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'HLA class II histocompatibility antigen, DR alpha chain' 21919.594 1 ? ? 'Extracellular Domain, UNP residues 26-206' ? 2 polymer man 'HLA class II histocompatibility antigen, DRB1-4 beta chain' 23224.617 1 ? ? 'Extracellular Domain, UNP residues 30-219' ? 3 polymer syn 'Citrullinated Vimentin' 1438.634 1 ? ? 'Residues 59-71' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 5 water nat water 18.015 239 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'MHC class II antigen DRA' 2 'MHC class II antigen DRB1*4, DR-4, DR4' # 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 ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFDTSGDDDDK ; ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFDTSGDDDDK ; A ? 2 'polypeptide(L)' no no ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTY CRHNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTY CRHNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; B ? 3 'polypeptide(L)' no yes 'GVYAT(CIR)SSAVRLR' GVYATRSSAVRLR C ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ILE n 1 2 LYS n 1 3 GLU n 1 4 GLU n 1 5 HIS n 1 6 VAL n 1 7 ILE n 1 8 ILE n 1 9 GLN n 1 10 ALA n 1 11 GLU n 1 12 PHE n 1 13 TYR n 1 14 LEU n 1 15 ASN n 1 16 PRO n 1 17 ASP n 1 18 GLN n 1 19 SER n 1 20 GLY n 1 21 GLU n 1 22 PHE n 1 23 MET n 1 24 PHE n 1 25 ASP n 1 26 PHE n 1 27 ASP n 1 28 GLY n 1 29 ASP n 1 30 GLU n 1 31 ILE n 1 32 PHE n 1 33 HIS n 1 34 VAL n 1 35 ASP n 1 36 MET n 1 37 ALA n 1 38 LYS n 1 39 LYS n 1 40 GLU n 1 41 THR n 1 42 VAL n 1 43 TRP n 1 44 ARG n 1 45 LEU n 1 46 GLU n 1 47 GLU n 1 48 PHE n 1 49 GLY n 1 50 ARG n 1 51 PHE n 1 52 ALA n 1 53 SER n 1 54 PHE n 1 55 GLU n 1 56 ALA n 1 57 GLN n 1 58 GLY n 1 59 ALA n 1 60 LEU n 1 61 ALA n 1 62 ASN n 1 63 ILE n 1 64 ALA n 1 65 VAL n 1 66 ASP n 1 67 LYS n 1 68 ALA n 1 69 ASN n 1 70 LEU n 1 71 GLU n 1 72 ILE n 1 73 MET n 1 74 THR n 1 75 LYS n 1 76 ARG n 1 77 SER n 1 78 ASN n 1 79 TYR n 1 80 THR n 1 81 PRO n 1 82 ILE n 1 83 THR n 1 84 ASN n 1 85 VAL n 1 86 PRO n 1 87 PRO n 1 88 GLU n 1 89 VAL n 1 90 THR n 1 91 VAL n 1 92 LEU n 1 93 THR n 1 94 ASN n 1 95 SER n 1 96 PRO n 1 97 VAL n 1 98 GLU n 1 99 LEU n 1 100 ARG n 1 101 GLU n 1 102 PRO n 1 103 ASN n 1 104 VAL n 1 105 LEU n 1 106 ILE n 1 107 CYS n 1 108 PHE n 1 109 ILE n 1 110 ASP n 1 111 LYS n 1 112 PHE n 1 113 THR n 1 114 PRO n 1 115 PRO n 1 116 VAL n 1 117 VAL n 1 118 ASN n 1 119 VAL n 1 120 THR n 1 121 TRP n 1 122 LEU n 1 123 ARG n 1 124 ASN n 1 125 GLY n 1 126 LYS n 1 127 PRO n 1 128 VAL n 1 129 THR n 1 130 THR n 1 131 GLY n 1 132 VAL n 1 133 SER n 1 134 GLU n 1 135 THR n 1 136 VAL n 1 137 PHE n 1 138 LEU n 1 139 PRO n 1 140 ARG n 1 141 GLU n 1 142 ASP n 1 143 HIS n 1 144 LEU n 1 145 PHE n 1 146 ARG n 1 147 LYS n 1 148 PHE n 1 149 HIS n 1 150 TYR n 1 151 LEU n 1 152 PRO n 1 153 PHE n 1 154 LEU n 1 155 PRO n 1 156 SER n 1 157 THR n 1 158 GLU n 1 159 ASP n 1 160 VAL n 1 161 TYR n 1 162 ASP n 1 163 CYS n 1 164 ARG n 1 165 VAL n 1 166 GLU n 1 167 HIS n 1 168 TRP n 1 169 GLY n 1 170 LEU n 1 171 ASP n 1 172 GLU n 1 173 PRO n 1 174 LEU n 1 175 LEU n 1 176 LYS n 1 177 HIS n 1 178 TRP n 1 179 GLU n 1 180 PHE n 1 181 ASP n 1 182 THR n 1 183 SER n 1 184 GLY n 1 185 ASP n 1 186 ASP n 1 187 ASP n 1 188 ASP n 1 189 LYS n 2 1 GLY n 2 2 SER n 2 3 GLY n 2 4 ASP n 2 5 THR n 2 6 ARG n 2 7 PRO n 2 8 ARG n 2 9 PHE n 2 10 LEU n 2 11 GLU n 2 12 GLN n 2 13 VAL n 2 14 LYS n 2 15 HIS n 2 16 GLU n 2 17 CYS n 2 18 HIS n 2 19 PHE n 2 20 PHE n 2 21 ASN n 2 22 GLY n 2 23 THR n 2 24 GLU n 2 25 ARG n 2 26 VAL n 2 27 ARG n 2 28 PHE n 2 29 LEU n 2 30 ASP n 2 31 ARG n 2 32 TYR n 2 33 PHE n 2 34 TYR n 2 35 HIS n 2 36 GLN n 2 37 GLU n 2 38 GLU n 2 39 TYR n 2 40 VAL n 2 41 ARG n 2 42 PHE n 2 43 ASP n 2 44 SER n 2 45 ASP n 2 46 VAL n 2 47 GLY n 2 48 GLU n 2 49 TYR n 2 50 ARG n 2 51 ALA n 2 52 VAL n 2 53 THR n 2 54 GLU n 2 55 LEU n 2 56 GLY n 2 57 ARG n 2 58 PRO n 2 59 ASP n 2 60 ALA n 2 61 GLU n 2 62 TYR n 2 63 TRP n 2 64 ASN n 2 65 SER n 2 66 GLN n 2 67 LYS n 2 68 ASP n 2 69 LEU n 2 70 LEU n 2 71 GLU n 2 72 GLN n 2 73 LYS n 2 74 ARG n 2 75 ALA n 2 76 ALA n 2 77 VAL n 2 78 ASP n 2 79 THR n 2 80 TYR n 2 81 CYS n 2 82 ARG n 2 83 HIS n 2 84 ASN n 2 85 TYR n 2 86 GLY n 2 87 VAL n 2 88 GLY n 2 89 GLU n 2 90 SER n 2 91 PHE n 2 92 THR n 2 93 VAL n 2 94 GLN n 2 95 ARG n 2 96 ARG n 2 97 VAL n 2 98 TYR n 2 99 PRO n 2 100 GLU n 2 101 VAL n 2 102 THR n 2 103 VAL n 2 104 TYR n 2 105 PRO n 2 106 ALA n 2 107 LYS n 2 108 THR n 2 109 GLN n 2 110 PRO n 2 111 LEU n 2 112 GLN n 2 113 HIS n 2 114 HIS n 2 115 ASN n 2 116 LEU n 2 117 LEU n 2 118 VAL n 2 119 CYS n 2 120 SER n 2 121 VAL n 2 122 ASN n 2 123 GLY n 2 124 PHE n 2 125 TYR n 2 126 PRO n 2 127 GLY n 2 128 SER n 2 129 ILE n 2 130 GLU n 2 131 VAL n 2 132 ARG n 2 133 TRP n 2 134 PHE n 2 135 ARG n 2 136 ASN n 2 137 GLY n 2 138 GLN n 2 139 GLU n 2 140 GLU n 2 141 LYS n 2 142 THR n 2 143 GLY n 2 144 VAL n 2 145 VAL n 2 146 SER n 2 147 THR n 2 148 GLY n 2 149 LEU n 2 150 ILE n 2 151 GLN n 2 152 ASN n 2 153 GLY n 2 154 ASP n 2 155 TRP n 2 156 THR n 2 157 PHE n 2 158 GLN n 2 159 THR n 2 160 LEU n 2 161 VAL n 2 162 MET n 2 163 LEU n 2 164 GLU n 2 165 THR n 2 166 VAL n 2 167 PRO n 2 168 ARG n 2 169 SER n 2 170 GLY n 2 171 GLU n 2 172 VAL n 2 173 TYR n 2 174 THR n 2 175 CYS n 2 176 GLN n 2 177 VAL n 2 178 GLU n 2 179 HIS n 2 180 PRO n 2 181 SER n 2 182 LEU n 2 183 THR n 2 184 SER n 2 185 PRO n 2 186 LEU n 2 187 THR n 2 188 VAL n 2 189 GLU n 2 190 TRP n 2 191 ARG n 2 192 ALA n 2 193 THR n 2 194 GLY n 2 195 GLY n 2 196 ASP n 2 197 ASP n 2 198 ASP n 2 199 ASP n 2 200 LYS n 3 1 GLY n 3 2 VAL n 3 3 TYR n 3 4 ALA n 3 5 THR n 3 6 CIR n 3 7 SER n 3 8 SER n 3 9 ALA n 3 10 VAL n 3 11 ARG n 3 12 LEU n 3 13 ARG 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 ? ? ? human ? 'HLA-DRA, HLA-DRA1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? human ? HLA-DRB1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'Homo sapiens' _pdbx_entity_src_syn.organism_common_name ? _pdbx_entity_src_syn.ncbi_taxonomy_id 9606 _pdbx_entity_src_syn.details 'This sequence is from human vimentin and contains citrulline at position 64' # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP DRA_HUMAN P01903 1 ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFD ; 26 ? 2 UNP 2B14_HUMAN P13760 2 ;GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTYCR HNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVM LETVPRSGEVYTCQVEHPSLTSPLTVEWRA ; 30 ? 3 UNP VIME_HUMAN P08670 3 GVYATRSSAVRLR 59 ? # 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 4MCZ A 1 ? 181 ? P01903 26 ? 206 ? 1 181 2 2 4MCZ B 3 ? 192 ? P13760 30 ? 219 ? 1 190 3 3 4MCZ C 1 ? 13 ? P08670 59 ? 71 ? 1 13 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4MCZ THR A 182 ? UNP P01903 ? ? 'EXPRESSION TAG' 182 1 1 4MCZ SER A 183 ? UNP P01903 ? ? 'EXPRESSION TAG' 183 2 1 4MCZ GLY A 184 ? UNP P01903 ? ? 'EXPRESSION TAG' 184 3 1 4MCZ ASP A 185 ? UNP P01903 ? ? 'EXPRESSION TAG' 185 4 1 4MCZ ASP A 186 ? UNP P01903 ? ? 'EXPRESSION TAG' 186 5 1 4MCZ ASP A 187 ? UNP P01903 ? ? 'EXPRESSION TAG' 187 6 1 4MCZ ASP A 188 ? UNP P01903 ? ? 'EXPRESSION TAG' 188 7 1 4MCZ LYS A 189 ? UNP P01903 ? ? 'EXPRESSION TAG' 189 8 2 4MCZ GLY B 1 ? UNP P13760 ? ? 'EXPRESSION TAG' -1 9 2 4MCZ SER B 2 ? UNP P13760 ? ? 'EXPRESSION TAG' 0 10 2 4MCZ THR B 193 ? UNP P13760 ? ? 'EXPRESSION TAG' 191 11 2 4MCZ GLY B 194 ? UNP P13760 ? ? 'EXPRESSION TAG' 192 12 2 4MCZ GLY B 195 ? UNP P13760 ? ? 'EXPRESSION TAG' 193 13 2 4MCZ ASP B 196 ? UNP P13760 ? ? 'EXPRESSION TAG' 194 14 2 4MCZ ASP B 197 ? UNP P13760 ? ? 'EXPRESSION TAG' 195 15 2 4MCZ ASP B 198 ? UNP P13760 ? ? 'EXPRESSION TAG' 196 16 2 4MCZ ASP B 199 ? UNP P13760 ? ? 'EXPRESSION TAG' 197 17 2 4MCZ LYS B 200 ? UNP P13760 ? ? 'EXPRESSION TAG' 198 18 # 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 CIR 'L-peptide linking' n CITRULLINE ? 'C6 H13 N3 O3' 175.186 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4MCZ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_percent_sol 53.97 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 294 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.3 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '26% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 210r' _diffrn_detector.pdbx_collection_date 2012-02-17 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.95370 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' _diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' _diffrn_source.pdbx_synchrotron_beamline MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.95370 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MCZ _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 48.84 _reflns.d_resolution_high 2.41 _reflns.number_obs 18843 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs 0.158 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.41 _reflns_shell.d_res_low 2.54 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.493 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.0 _reflns_shell.pdbx_redundancy 4.8 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MCZ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 18841 _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 48.84 _refine.ls_d_res_high 2.410 _refine.ls_percent_reflns_obs 99.82 _refine.ls_R_factor_obs 0.1908 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1887 _refine.ls_R_factor_R_free 0.2309 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.14 _refine.ls_number_reflns_R_free 969 _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 ? _refine.details ? _refine.pdbx_starting_model ? _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 0.21 _refine.pdbx_overall_phase_error 20.87 _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.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3139 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 42 _refine_hist.number_atoms_solvent 239 _refine_hist.number_atoms_total 3420 _refine_hist.d_res_high 2.410 _refine_hist.d_res_low 48.84 # 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 0.003 ? ? 3285 'X-RAY DIFFRACTION' ? f_angle_d 1.020 ? ? 4466 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.338 ? ? 1204 'X-RAY DIFFRACTION' ? f_chiral_restr 0.065 ? ? 479 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 581 '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.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.4100 2.5371 2524 0.2128 100.00 0.2466 . . 123 . . . . 'X-RAY DIFFRACTION' . 2.5371 2.6960 2504 0.2199 100.00 0.2441 . . 157 . . . . 'X-RAY DIFFRACTION' . 2.6960 2.9042 2515 0.2146 100.00 0.2728 . . 145 . . . . 'X-RAY DIFFRACTION' . 2.9042 3.1964 2546 0.2057 100.00 0.2644 . . 131 . . . . 'X-RAY DIFFRACTION' . 3.1964 3.6588 2529 0.1783 100.00 0.2108 . . 148 . . . . 'X-RAY DIFFRACTION' . 3.6588 4.6091 2570 0.1573 100.00 0.1845 . . 136 . . . . 'X-RAY DIFFRACTION' . 4.6091 48.8515 2684 0.1839 99.00 0.2445 . . 129 . . . . # _struct.entry_id 4MCZ _struct.title 'Immune Receptor' _struct.pdbx_descriptor ;HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-4 beta chain, Citrullinated Vimentin ; _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MCZ _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'HLA-DR, Antigen presentation, T-cell receptor, Citrullination, Membrane, 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 4 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLU A 47 ? ALA A 52 ? GLU A 47 ALA A 52 1 ? 6 HELX_P HELX_P2 2 ALA A 56 ? SER A 77 ? ALA A 56 SER A 77 1 ? 22 HELX_P HELX_P3 3 THR B 53 ? LEU B 55 ? THR B 51 LEU B 53 5 ? 3 HELX_P HELX_P4 4 GLY B 56 ? SER B 65 ? GLY B 54 SER B 63 1 ? 10 HELX_P HELX_P5 5 GLN B 66 ? ALA B 75 ? GLN B 64 ALA B 73 1 ? 10 HELX_P HELX_P6 6 ALA B 75 ? TYR B 80 ? ALA B 73 TYR B 78 1 ? 6 HELX_P HELX_P7 7 TYR B 80 ? GLU B 89 ? TYR B 78 GLU B 87 1 ? 10 HELX_P HELX_P8 8 SER B 90 ? THR B 92 ? SER B 88 THR B 90 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 107 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107 A CYS 163 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.034 ? disulf3 disulf ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.026 ? covale1 covale ? ? C THR 5 C ? ? ? 1_555 C CIR 6 N2 ? ? C THR 5 C CIR 6 1_555 ? ? ? ? ? ? ? 1.351 ? covale2 covale ? ? C CIR 6 C1 ? ? ? 1_555 C SER 7 N ? ? C CIR 6 C SER 7 1_555 ? ? ? ? ? ? ? 1.317 ? covale3 covale ? ? B ASN 21 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 19 B NAG 500 1_555 ? ? ? ? ? ? ? 1.435 ? covale4 covale ? ? A ASN 78 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 78 A NAG 500 1_555 ? ? ? ? ? ? ? 1.440 ? covale5 covale ? ? A ASN 118 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 118 A NAG 501 1_555 ? ? ? ? ? ? ? 1.444 ? # 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 ASN 15 A . ? ASN 15 A PRO 16 A ? PRO 16 A 1 2.99 2 THR 113 A . ? THR 113 A PRO 114 A ? PRO 114 A 1 0.55 3 TYR 125 B . ? TYR 123 B PRO 126 B ? PRO 124 B 1 1.18 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLU A 40 ? TRP A 43 ? GLU A 40 TRP A 43 A 2 ASP A 29 ? ASP A 35 ? ASP A 29 ASP A 35 A 3 SER A 19 ? PHE A 26 ? SER A 19 PHE A 26 A 4 HIS A 5 ? ASN A 15 ? HIS A 5 ASN A 15 A 5 PHE B 9 ? PHE B 20 ? PHE B 7 PHE B 18 A 6 ARG B 25 ? TYR B 34 ? ARG B 23 TYR B 32 A 7 GLU B 37 ? ASP B 43 ? GLU B 35 ASP B 41 A 8 TYR B 49 ? ALA B 51 ? TYR B 47 ALA B 49 B 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 B 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 B 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 B 4 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 C 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 C 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 C 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 C 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 D 1 LYS A 126 ? VAL A 128 ? LYS A 126 VAL A 128 D 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 D 3 TYR A 161 ? GLU A 166 ? TYR A 161 GLU A 166 D 4 LEU A 174 ? TRP A 178 ? LEU A 174 TRP A 178 E 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 E 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 E 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 E 4 VAL B 144 ? SER B 146 ? VAL B 142 SER B 144 F 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 F 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 F 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 F 4 ILE B 150 ? GLN B 151 ? ILE B 148 GLN B 149 G 1 GLN B 138 ? GLU B 140 ? GLN B 136 GLU B 138 G 2 GLU B 130 ? ARG B 135 ? GLU B 128 ARG B 133 G 3 VAL B 172 ? GLU B 178 ? VAL B 170 GLU B 176 G 4 LEU B 186 ? ARG B 191 ? LEU B 184 ARG B 189 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O VAL A 42 ? O VAL A 42 N HIS A 33 ? N HIS A 33 A 2 3 O ASP A 29 ? O ASP A 29 N PHE A 26 ? N PHE A 26 A 3 4 O ASP A 25 ? O ASP A 25 N ILE A 8 ? N ILE A 8 A 4 5 N HIS A 5 ? N HIS A 5 O PHE B 19 ? O PHE B 17 A 5 6 N GLN B 12 ? N GLN B 10 O PHE B 33 ? O PHE B 31 A 6 7 N TYR B 34 ? N TYR B 32 O GLU B 37 ? O GLU B 35 A 7 8 N ARG B 41 ? N ARG B 39 O ARG B 50 ? O ARG B 48 B 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 B 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 B 3 4 O TYR A 150 ? O TYR A 150 N SER A 133 ? N SER A 133 C 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 C 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 C 3 4 O ARG A 146 ? O ARG A 146 N LEU A 138 ? N LEU A 138 D 1 2 O LYS A 126 ? O LYS A 126 N ARG A 123 ? N ARG A 123 D 2 3 N THR A 120 ? N THR A 120 O ARG A 164 ? O ARG A 164 D 3 4 N TYR A 161 ? N TYR A 161 O TRP A 178 ? O TRP A 178 E 1 2 N ALA B 106 ? N ALA B 104 O LEU B 116 ? O LEU B 114 E 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 E 3 4 O MET B 162 ? O MET B 160 N VAL B 145 ? N VAL B 143 F 1 2 N ALA B 106 ? N ALA B 104 O LEU B 116 ? O LEU B 114 F 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 F 3 4 O GLN B 158 ? O GLN B 156 N ILE B 150 ? N ILE B 148 G 1 2 O GLN B 138 ? O GLN B 136 N ARG B 135 ? N ARG B 133 G 2 3 N ARG B 132 ? N ARG B 130 O GLN B 176 ? O GLN B 174 G 3 4 N VAL B 177 ? N VAL B 175 O LEU B 186 ? O LEU B 184 # 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 ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A 500 BOUND TO ASN A 78' AC2 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A 501 BOUND TO ASN A 118' AC3 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG B 500 BOUND TO ASN B 19' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 4 ASN A 78 ? ASN A 78 . ? 1_555 ? 2 AC1 4 HOH G . ? HOH A 658 . ? 1_555 ? 3 AC1 4 HOH G . ? HOH A 672 . ? 1_555 ? 4 AC1 4 HOH G . ? HOH A 704 . ? 1_555 ? 5 AC2 6 VAL A 116 ? VAL A 116 . ? 1_555 ? 6 AC2 6 ASN A 118 ? ASN A 118 . ? 1_555 ? 7 AC2 6 GLU A 166 ? GLU A 166 . ? 1_555 ? 8 AC2 6 TRP A 168 ? TRP A 168 . ? 1_555 ? 9 AC2 6 HOH G . ? HOH A 648 . ? 1_555 ? 10 AC2 6 HOH G . ? HOH A 694 . ? 1_555 ? 11 AC3 3 ASN B 21 ? ASN B 19 . ? 1_555 ? 12 AC3 3 GLU B 24 ? GLU B 22 . ? 1_555 ? 13 AC3 3 HOH H . ? HOH B 661 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCZ _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4MCZ _atom_sites.fract_transf_matrix[1][1] 0.014901 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.005452 _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] 0.012940 _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 3 ? 35.879 12.676 -18.926 1.00 62.86 ? 3 GLU A N 1 ATOM 2 C CA . GLU A 1 3 ? 36.727 12.388 -17.779 1.00 61.67 ? 3 GLU A CA 1 ATOM 3 C C . GLU A 1 3 ? 35.900 11.777 -16.658 1.00 57.56 ? 3 GLU A C 1 ATOM 4 O O . GLU A 1 3 ? 34.688 12.034 -16.543 1.00 59.18 ? 3 GLU A O 1 ATOM 5 C CB . GLU A 1 3 ? 37.444 13.650 -17.299 1.00 61.63 ? 3 GLU A CB 1 ATOM 6 C CG . GLU A 1 3 ? 36.556 14.661 -16.595 1.00 60.84 ? 3 GLU A CG 1 ATOM 7 C CD . GLU A 1 3 ? 36.893 16.102 -16.948 1.00 59.94 ? 3 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 3 ? 35.983 16.956 -16.882 1.00 59.53 ? 3 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 3 ? 38.066 16.381 -17.278 1.00 59.20 ? 3 GLU A OE2 1 ATOM 10 N N . GLU A 1 4 ? 36.562 10.987 -15.814 1.00 51.74 ? 4 GLU A N 1 ATOM 11 C CA . GLU A 1 4 ? 35.858 10.367 -14.686 1.00 45.67 ? 4 GLU A CA 1 ATOM 12 C C . GLU A 1 4 ? 35.897 11.232 -13.439 1.00 37.81 ? 4 GLU A C 1 ATOM 13 O O . GLU A 1 4 ? 34.878 11.429 -12.756 1.00 38.51 ? 4 GLU A O 1 ATOM 14 C CB . GLU A 1 4 ? 36.473 9.017 -14.316 1.00 47.83 ? 4 GLU A CB 1 ATOM 15 C CG . GLU A 1 4 ? 36.329 7.886 -15.287 1.00 52.35 ? 4 GLU A CG 1 ATOM 16 C CD . GLU A 1 4 ? 36.825 6.603 -14.665 1.00 53.34 ? 4 GLU A CD 1 ATOM 17 O OE1 . GLU A 1 4 ? 37.423 6.675 -13.580 1.00 50.73 ? 4 GLU A OE1 1 ATOM 18 O OE2 . GLU A 1 4 ? 36.767 5.557 -15.324 1.00 56.25 ? 4 GLU A OE2 1 ATOM 19 N N . HIS A 1 5 ? 37.074 11.780 -13.161 1.00 27.01 ? 5 HIS A N 1 ATOM 20 C CA . HIS A 1 5 ? 37.244 12.551 -11.951 1.00 22.08 ? 5 HIS A CA 1 ATOM 21 C C . HIS A 1 5 ? 38.215 13.700 -12.149 1.00 21.36 ? 5 HIS A C 1 ATOM 22 O O . HIS A 1 5 ? 39.100 13.653 -13.002 1.00 22.22 ? 5 HIS A O 1 ATOM 23 C CB . HIS A 1 5 ? 37.749 11.654 -10.819 1.00 19.84 ? 5 HIS A CB 1 ATOM 24 C CG . HIS A 1 5 ? 36.853 10.491 -10.520 1.00 24.32 ? 5 HIS A CG 1 ATOM 25 N ND1 . HIS A 1 5 ? 35.601 10.627 -9.958 1.00 21.94 ? 5 HIS A ND1 1 ATOM 26 C CD2 . HIS A 1 5 ? 37.033 9.164 -10.720 1.00 28.92 ? 5 HIS A CD2 1 ATOM 27 C CE1 . HIS A 1 5 ? 35.047 9.434 -9.831 1.00 23.29 ? 5 HIS A CE1 1 ATOM 28 N NE2 . HIS A 1 5 ? 35.896 8.529 -10.283 1.00 29.15 ? 5 HIS A NE2 1 ATOM 29 N N . VAL A 1 6 ? 38.048 14.734 -11.334 1.00 17.58 ? 6 VAL A N 1 ATOM 30 C CA . VAL A 1 6 ? 38.960 15.867 -11.340 1.00 18.18 ? 6 VAL A CA 1 ATOM 31 C C . VAL A 1 6 ? 39.342 16.224 -9.911 1.00 17.28 ? 6 VAL A C 1 ATOM 32 O O . VAL A 1 6 ? 38.484 16.330 -9.035 1.00 19.22 ? 6 VAL A O 1 ATOM 33 C CB . VAL A 1 6 ? 38.323 17.100 -12.017 1.00 13.48 ? 6 VAL A CB 1 ATOM 34 C CG1 . VAL A 1 6 ? 39.282 18.276 -12.014 1.00 12.43 ? 6 VAL A CG1 1 ATOM 35 C CG2 . VAL A 1 6 ? 37.901 16.768 -13.445 1.00 14.68 ? 6 VAL A CG2 1 ATOM 36 N N . ILE A 1 7 ? 40.635 16.413 -9.683 1.00 16.23 ? 7 ILE A N 1 ATOM 37 C CA . ILE A 1 7 ? 41.113 16.877 -8.395 1.00 16.65 ? 7 ILE A CA 1 ATOM 38 C C . ILE A 1 7 ? 41.776 18.223 -8.603 1.00 16.98 ? 7 ILE A C 1 ATOM 39 O O . ILE A 1 7 ? 42.675 18.360 -9.433 1.00 15.96 ? 7 ILE A O 1 ATOM 40 C CB . ILE A 1 7 ? 42.131 15.903 -7.777 1.00 16.84 ? 7 ILE A CB 1 ATOM 41 C CG1 . ILE A 1 7 ? 41.493 14.532 -7.553 1.00 13.28 ? 7 ILE A CG1 1 ATOM 42 C CG2 . ILE A 1 7 ? 42.680 16.460 -6.471 1.00 12.83 ? 7 ILE A CG2 1 ATOM 43 C CD1 . ILE A 1 7 ? 42.461 13.498 -7.020 1.00 14.01 ? 7 ILE A CD1 1 ATOM 44 N N . ILE A 1 8 ? 41.337 19.223 -7.849 1.00 18.33 ? 8 ILE A N 1 ATOM 45 C CA . ILE A 1 8 ? 41.885 20.557 -8.023 1.00 17.07 ? 8 ILE A CA 1 ATOM 46 C C . ILE A 1 8 ? 42.426 21.077 -6.703 1.00 16.85 ? 8 ILE A C 1 ATOM 47 O O . ILE A 1 8 ? 41.741 21.050 -5.681 1.00 18.05 ? 8 ILE A O 1 ATOM 48 C CB . ILE A 1 8 ? 40.820 21.542 -8.548 1.00 15.46 ? 8 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 8 ? 40.244 21.056 -9.880 1.00 15.00 ? 8 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 8 ? 41.403 22.938 -8.686 1.00 11.60 ? 8 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 8 ? 39.130 21.927 -10.418 1.00 9.94 ? 8 ILE A CD1 1 ATOM 52 N N . GLN A 1 9 ? 43.664 21.552 -6.732 1.00 13.78 ? 9 GLN A N 1 ATOM 53 C CA . GLN A 1 9 ? 44.216 22.302 -5.621 1.00 13.71 ? 9 GLN A CA 1 ATOM 54 C C . GLN A 1 9 ? 43.998 23.768 -5.945 1.00 13.75 ? 9 GLN A C 1 ATOM 55 O O . GLN A 1 9 ? 44.650 24.319 -6.834 1.00 10.89 ? 9 GLN A O 1 ATOM 56 C CB . GLN A 1 9 ? 45.703 21.993 -5.488 1.00 17.17 ? 9 GLN A CB 1 ATOM 57 C CG . GLN A 1 9 ? 46.453 22.842 -4.482 1.00 16.33 ? 9 GLN A CG 1 ATOM 58 C CD . GLN A 1 9 ? 47.942 22.564 -4.512 1.00 18.18 ? 9 GLN A CD 1 ATOM 59 O OE1 . GLN A 1 9 ? 48.363 21.428 -4.725 1.00 20.08 ? 9 GLN A OE1 1 ATOM 60 N NE2 . GLN A 1 9 ? 48.745 23.597 -4.294 1.00 10.49 ? 9 GLN A NE2 1 ATOM 61 N N . ALA A 1 10 ? 43.073 24.398 -5.233 1.00 13.70 ? 10 ALA A N 1 ATOM 62 C CA . ALA A 1 10 ? 42.690 25.765 -5.547 1.00 12.18 ? 10 ALA A CA 1 ATOM 63 C C . ALA A 1 10 ? 43.166 26.708 -4.456 1.00 12.26 ? 10 ALA A C 1 ATOM 64 O O . ALA A 1 10 ? 42.994 26.446 -3.266 1.00 13.98 ? 10 ALA A O 1 ATOM 65 C CB . ALA A 1 10 ? 41.181 25.867 -5.710 1.00 13.37 ? 10 ALA A CB 1 ATOM 66 N N . GLU A 1 11 ? 43.762 27.815 -4.879 1.00 12.96 ? 11 GLU A N 1 ATOM 67 C CA . GLU A 1 11 ? 44.321 28.782 -3.953 1.00 12.70 ? 11 GLU A CA 1 ATOM 68 C C . GLU A 1 11 ? 43.864 30.172 -4.364 1.00 11.99 ? 11 GLU A C 1 ATOM 69 O O . GLU A 1 11 ? 43.635 30.428 -5.546 1.00 8.64 ? 11 GLU A O 1 ATOM 70 C CB . GLU A 1 11 ? 45.849 28.742 -4.024 1.00 9.75 ? 11 GLU A CB 1 ATOM 71 C CG . GLU A 1 11 ? 46.455 27.370 -3.766 1.00 15.10 ? 11 GLU A CG 1 ATOM 72 C CD . GLU A 1 11 ? 47.882 27.258 -4.267 1.00 16.33 ? 11 GLU A CD 1 ATOM 73 O OE1 . GLU A 1 11 ? 48.539 28.307 -4.439 1.00 15.54 ? 11 GLU A OE1 1 ATOM 74 O OE2 . GLU A 1 11 ? 48.346 26.121 -4.495 1.00 16.91 ? 11 GLU A OE2 1 ATOM 75 N N . PHE A 1 12 ? 43.733 31.074 -3.396 1.00 9.01 ? 12 PHE A N 1 ATOM 76 C CA . PHE A 1 12 ? 43.612 32.490 -3.724 1.00 13.44 ? 12 PHE A CA 1 ATOM 77 C C . PHE A 1 12 ? 44.264 33.406 -2.693 1.00 12.87 ? 12 PHE A C 1 ATOM 78 O O . PHE A 1 12 ? 44.469 33.023 -1.543 1.00 12.38 ? 12 PHE A O 1 ATOM 79 C CB . PHE A 1 12 ? 42.155 32.910 -4.014 1.00 16.34 ? 12 PHE A CB 1 ATOM 80 C CG . PHE A 1 12 ? 41.259 32.975 -2.798 1.00 16.77 ? 12 PHE A CG 1 ATOM 81 C CD1 . PHE A 1 12 ? 41.331 34.045 -1.914 1.00 14.61 ? 12 PHE A CD1 1 ATOM 82 C CD2 . PHE A 1 12 ? 40.303 31.998 -2.576 1.00 15.31 ? 12 PHE A CD2 1 ATOM 83 C CE1 . PHE A 1 12 ? 40.499 34.115 -0.810 1.00 13.24 ? 12 PHE A CE1 1 ATOM 84 C CE2 . PHE A 1 12 ? 39.460 32.068 -1.478 1.00 18.00 ? 12 PHE A CE2 1 ATOM 85 C CZ . PHE A 1 12 ? 39.563 33.128 -0.592 1.00 14.68 ? 12 PHE A CZ 1 ATOM 86 N N . TYR A 1 13 ? 44.589 34.618 -3.128 1.00 13.05 ? 13 TYR A N 1 ATOM 87 C CA . TYR A 1 13 ? 45.014 35.683 -2.230 1.00 13.11 ? 13 TYR A CA 1 ATOM 88 C C . TYR A 1 13 ? 44.334 36.977 -2.648 1.00 16.16 ? 13 TYR A C 1 ATOM 89 O O . TYR A 1 13 ? 44.289 37.310 -3.832 1.00 17.22 ? 13 TYR A O 1 ATOM 90 C CB . TYR A 1 13 ? 46.532 35.856 -2.240 1.00 14.04 ? 13 TYR A CB 1 ATOM 91 C CG . TYR A 1 13 ? 47.014 36.775 -1.141 1.00 17.06 ? 13 TYR A CG 1 ATOM 92 C CD1 . TYR A 1 13 ? 47.199 38.132 -1.376 1.00 17.83 ? 13 TYR A CD1 1 ATOM 93 C CD2 . TYR A 1 13 ? 47.258 36.293 0.138 1.00 16.22 ? 13 TYR A CD2 1 ATOM 94 C CE1 . TYR A 1 13 ? 47.629 38.978 -0.373 1.00 19.30 ? 13 TYR A CE1 1 ATOM 95 C CE2 . TYR A 1 13 ? 47.688 37.133 1.148 1.00 16.25 ? 13 TYR A CE2 1 ATOM 96 C CZ . TYR A 1 13 ? 47.871 38.474 0.886 1.00 19.95 ? 13 TYR A CZ 1 ATOM 97 O OH . TYR A 1 13 ? 48.298 39.315 1.889 1.00 26.45 ? 13 TYR A OH 1 ATOM 98 N N . LEU A 1 14 ? 43.807 37.705 -1.670 1.00 16.80 ? 14 LEU A N 1 ATOM 99 C CA . LEU A 1 14 ? 43.020 38.894 -1.953 1.00 16.89 ? 14 LEU A CA 1 ATOM 100 C C . LEU A 1 14 ? 43.563 40.128 -1.234 1.00 17.31 ? 14 LEU A C 1 ATOM 101 O O . LEU A 1 14 ? 43.758 40.120 -0.019 1.00 17.74 ? 14 LEU A O 1 ATOM 102 C CB . LEU A 1 14 ? 41.577 38.655 -1.514 1.00 17.43 ? 14 LEU A CB 1 ATOM 103 C CG . LEU A 1 14 ? 40.604 39.822 -1.663 1.00 16.42 ? 14 LEU A CG 1 ATOM 104 C CD1 . LEU A 1 14 ? 40.303 40.084 -3.133 1.00 14.08 ? 14 LEU A CD1 1 ATOM 105 C CD2 . LEU A 1 14 ? 39.334 39.535 -0.894 1.00 13.67 ? 14 LEU A CD2 1 ATOM 106 N N . ASN A 1 15 ? 43.807 41.185 -2.003 1.00 16.97 ? 15 ASN A N 1 ATOM 107 C CA . ASN A 1 15 ? 44.169 42.486 -1.454 1.00 17.39 ? 15 ASN A CA 1 ATOM 108 C C . ASN A 1 15 ? 42.987 43.439 -1.587 1.00 18.91 ? 15 ASN A C 1 ATOM 109 O O . ASN A 1 15 ? 42.187 43.303 -2.513 1.00 20.23 ? 15 ASN A O 1 ATOM 110 C CB . ASN A 1 15 ? 45.366 43.063 -2.215 1.00 18.30 ? 15 ASN A CB 1 ATOM 111 C CG . ASN A 1 15 ? 46.695 42.610 -1.643 1.00 22.31 ? 15 ASN A CG 1 ATOM 112 O OD1 . ASN A 1 15 ? 46.813 42.356 -0.445 1.00 23.53 ? 15 ASN A OD1 1 ATOM 113 N ND2 . ASN A 1 15 ? 47.704 42.507 -2.500 1.00 15.57 ? 15 ASN A ND2 1 ATOM 114 N N . PRO A 1 16 ? 42.864 44.409 -0.664 1.00 17.40 ? 16 PRO A N 1 ATOM 115 C CA . PRO A 1 16 ? 43.773 44.713 0.447 1.00 18.84 ? 16 PRO A CA 1 ATOM 116 C C . PRO A 1 16 ? 43.441 43.923 1.711 1.00 21.04 ? 16 PRO A C 1 ATOM 117 O O . PRO A 1 16 ? 44.034 44.168 2.762 1.00 20.91 ? 16 PRO A O 1 ATOM 118 C CB . PRO A 1 16 ? 43.526 46.200 0.687 1.00 20.41 ? 16 PRO A CB 1 ATOM 119 C CG . PRO A 1 16 ? 42.080 46.362 0.364 1.00 20.07 ? 16 PRO A CG 1 ATOM 120 C CD . PRO A 1 16 ? 41.820 45.440 -0.803 1.00 30.74 ? 16 PRO A CD 1 ATOM 121 N N . ASP A 1 17 ? 42.499 42.991 1.604 1.00 21.18 ? 17 ASP A N 1 ATOM 122 C CA . ASP A 1 17 ? 42.025 42.239 2.761 1.00 24.50 ? 17 ASP A CA 1 ATOM 123 C C . ASP A 1 17 ? 43.117 41.355 3.352 1.00 24.05 ? 17 ASP A C 1 ATOM 124 O O . ASP A 1 17 ? 43.053 40.981 4.525 1.00 23.33 ? 17 ASP A O 1 ATOM 125 C CB . ASP A 1 17 ? 40.805 41.393 2.386 1.00 23.42 ? 17 ASP A CB 1 ATOM 126 C CG . ASP A 1 17 ? 39.702 42.213 1.748 1.00 27.50 ? 17 ASP A CG 1 ATOM 127 O OD1 . ASP A 1 17 ? 39.834 42.564 0.558 1.00 24.58 ? 17 ASP A OD1 1 ATOM 128 O OD2 . ASP A 1 17 ? 38.701 42.503 2.436 1.00 33.23 ? 17 ASP A OD2 1 ATOM 129 N N . GLN A 1 18 ? 44.108 41.021 2.528 1.00 25.54 ? 18 GLN A N 1 ATOM 130 C CA . GLN A 1 18 ? 45.181 40.109 2.918 1.00 23.83 ? 18 GLN A CA 1 ATOM 131 C C . GLN A 1 18 ? 44.615 38.766 3.367 1.00 23.58 ? 18 GLN A C 1 ATOM 132 O O . GLN A 1 18 ? 45.063 38.184 4.356 1.00 24.90 ? 18 GLN A O 1 ATOM 133 C CB . GLN A 1 18 ? 46.076 40.734 3.995 1.00 26.56 ? 18 GLN A CB 1 ATOM 134 C CG . GLN A 1 18 ? 46.790 41.995 3.527 1.00 27.27 ? 18 GLN A CG 1 ATOM 135 C CD . GLN A 1 18 ? 47.883 42.441 4.478 1.00 29.95 ? 18 GLN A CD 1 ATOM 136 O OE1 . GLN A 1 18 ? 49.019 42.682 4.066 1.00 30.15 ? 18 GLN A OE1 1 ATOM 137 N NE2 . GLN A 1 18 ? 47.544 42.563 5.756 1.00 32.04 ? 18 GLN A NE2 1 ATOM 138 N N . SER A 1 19 ? 43.617 38.288 2.630 1.00 18.39 ? 19 SER A N 1 ATOM 139 C CA . SER A 1 19 ? 43.041 36.973 2.867 1.00 17.96 ? 19 SER A CA 1 ATOM 140 C C . SER A 1 19 ? 43.549 35.952 1.854 1.00 17.23 ? 19 SER A C 1 ATOM 141 O O . SER A 1 19 ? 43.519 36.194 0.647 1.00 17.72 ? 19 SER A O 1 ATOM 142 C CB . SER A 1 19 ? 41.512 37.041 2.831 1.00 22.39 ? 19 SER A CB 1 ATOM 143 O OG . SER A 1 19 ? 41.037 38.213 3.470 1.00 31.71 ? 19 SER A OG 1 ATOM 144 N N . GLY A 1 20 ? 44.011 34.808 2.350 1.00 18.07 ? 20 GLY A N 1 ATOM 145 C CA . GLY A 1 20 ? 44.476 33.742 1.483 1.00 23.19 ? 20 GLY A CA 1 ATOM 146 C C . GLY A 1 20 ? 43.916 32.381 1.850 1.00 26.39 ? 20 GLY A C 1 ATOM 147 O O . GLY A 1 20 ? 43.856 32.028 3.027 1.00 33.73 ? 20 GLY A O 1 ATOM 148 N N . GLU A 1 21 ? 43.497 31.621 0.842 1.00 20.77 ? 21 GLU A N 1 ATOM 149 C CA . GLU A 1 21 ? 42.872 30.322 1.068 1.00 21.61 ? 21 GLU A CA 1 ATOM 150 C C . GLU A 1 21 ? 43.576 29.229 0.260 1.00 16.34 ? 21 GLU A C 1 ATOM 151 O O . GLU A 1 21 ? 44.142 29.499 -0.799 1.00 12.22 ? 21 GLU A O 1 ATOM 152 C CB . GLU A 1 21 ? 41.393 30.376 0.692 1.00 23.76 ? 21 GLU A CB 1 ATOM 153 C CG . GLU A 1 21 ? 40.630 29.098 0.987 1.00 30.21 ? 21 GLU A CG 1 ATOM 154 C CD . GLU A 1 21 ? 39.212 29.140 0.481 1.00 32.45 ? 21 GLU A CD 1 ATOM 155 O OE1 . GLU A 1 21 ? 38.376 29.851 1.079 1.00 31.66 ? 21 GLU A OE1 1 ATOM 156 O OE2 . GLU A 1 21 ? 38.944 28.457 -0.524 1.00 30.72 ? 21 GLU A OE2 1 ATOM 157 N N . PHE A 1 22 ? 43.540 28.001 0.769 1.00 15.80 ? 22 PHE A N 1 ATOM 158 C CA . PHE A 1 22 ? 44.155 26.865 0.097 1.00 12.29 ? 22 PHE A CA 1 ATOM 159 C C . PHE A 1 22 ? 43.244 25.663 0.344 1.00 12.47 ? 22 PHE A C 1 ATOM 160 O O . PHE A 1 22 ? 42.927 25.359 1.493 1.00 12.19 ? 22 PHE A O 1 ATOM 161 C CB . PHE A 1 22 ? 45.536 26.611 0.712 1.00 14.47 ? 22 PHE A CB 1 ATOM 162 C CG . PHE A 1 22 ? 46.293 25.463 0.094 1.00 15.68 ? 22 PHE A CG 1 ATOM 163 C CD1 . PHE A 1 22 ? 45.959 24.144 0.369 1.00 15.81 ? 22 PHE A CD1 1 ATOM 164 C CD2 . PHE A 1 22 ? 47.374 25.712 -0.737 1.00 18.34 ? 22 PHE A CD2 1 ATOM 165 C CE1 . PHE A 1 22 ? 46.668 23.100 -0.198 1.00 17.24 ? 22 PHE A CE1 1 ATOM 166 C CE2 . PHE A 1 22 ? 48.090 24.671 -1.302 1.00 19.28 ? 22 PHE A CE2 1 ATOM 167 C CZ . PHE A 1 22 ? 47.737 23.365 -1.032 1.00 17.50 ? 22 PHE A CZ 1 ATOM 168 N N . MET A 1 23 ? 42.807 24.988 -0.717 1.00 10.30 ? 23 MET A N 1 ATOM 169 C CA . MET A 1 23 ? 41.940 23.818 -0.552 1.00 16.23 ? 23 MET A CA 1 ATOM 170 C C . MET A 1 23 ? 42.077 22.798 -1.682 1.00 16.00 ? 23 MET A C 1 ATOM 171 O O . MET A 1 23 ? 42.614 23.098 -2.748 1.00 17.43 ? 23 MET A O 1 ATOM 172 C CB . MET A 1 23 ? 40.474 24.257 -0.441 1.00 15.20 ? 23 MET A CB 1 ATOM 173 C CG . MET A 1 23 ? 39.934 25.005 -1.656 1.00 13.25 ? 23 MET A CG 1 ATOM 174 S SD . MET A 1 23 ? 39.252 23.935 -2.942 1.00 19.47 ? 23 MET A SD 1 ATOM 175 C CE . MET A 1 23 ? 37.802 23.278 -2.120 1.00 10.16 ? 23 MET A CE 1 ATOM 176 N N . PHE A 1 24 ? 41.588 21.587 -1.427 1.00 14.62 ? 24 PHE A N 1 ATOM 177 C CA . PHE A 1 24 ? 41.512 20.540 -2.440 1.00 14.74 ? 24 PHE A CA 1 ATOM 178 C C . PHE A 1 24 ? 40.064 20.182 -2.750 1.00 15.55 ? 24 PHE A C 1 ATOM 179 O O . PHE A 1 24 ? 39.233 20.075 -1.847 1.00 16.49 ? 24 PHE A O 1 ATOM 180 C CB . PHE A 1 24 ? 42.227 19.280 -1.951 1.00 11.23 ? 24 PHE A CB 1 ATOM 181 C CG . PHE A 1 24 ? 43.655 19.183 -2.399 1.00 19.61 ? 24 PHE A CG 1 ATOM 182 C CD1 . PHE A 1 24 ? 44.630 20.002 -1.855 1.00 18.53 ? 24 PHE A CD1 1 ATOM 183 C CD2 . PHE A 1 24 ? 44.022 18.268 -3.371 1.00 20.96 ? 24 PHE A CD2 1 ATOM 184 C CE1 . PHE A 1 24 ? 45.946 19.907 -2.271 1.00 19.84 ? 24 PHE A CE1 1 ATOM 185 C CE2 . PHE A 1 24 ? 45.335 18.169 -3.792 1.00 16.74 ? 24 PHE A CE2 1 ATOM 186 C CZ . PHE A 1 24 ? 46.297 18.989 -3.242 1.00 16.72 ? 24 PHE A CZ 1 ATOM 187 N N . ASP A 1 25 ? 39.768 20.006 -4.034 1.00 17.43 ? 25 ASP A N 1 ATOM 188 C CA . ASP A 1 25 ? 38.415 19.702 -4.472 1.00 15.35 ? 25 ASP A CA 1 ATOM 189 C C . ASP A 1 25 ? 38.411 18.376 -5.226 1.00 15.92 ? 25 ASP A C 1 ATOM 190 O O . ASP A 1 25 ? 39.290 18.119 -6.048 1.00 15.94 ? 25 ASP A O 1 ATOM 191 C CB . ASP A 1 25 ? 37.923 20.821 -5.394 1.00 17.85 ? 25 ASP A CB 1 ATOM 192 C CG . ASP A 1 25 ? 36.527 20.568 -5.937 1.00 24.18 ? 25 ASP A CG 1 ATOM 193 O OD1 . ASP A 1 25 ? 36.366 19.689 -6.811 1.00 22.68 ? 25 ASP A OD1 1 ATOM 194 O OD2 . ASP A 1 25 ? 35.588 21.267 -5.500 1.00 29.71 ? 25 ASP A OD2 1 ATOM 195 N N . PHE A 1 26 ? 37.416 17.540 -4.949 1.00 14.04 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 37.225 16.306 -5.700 1.00 14.74 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 35.824 16.333 -6.297 1.00 15.76 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 34.835 16.273 -5.564 1.00 17.37 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 37.368 15.091 -4.781 1.00 13.42 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 37.076 13.776 -5.459 1.00 15.30 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 38.077 13.099 -6.136 1.00 19.93 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 35.808 13.215 -5.413 1.00 16.04 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 37.820 11.891 -6.762 1.00 24.32 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 35.542 12.007 -6.038 1.00 18.18 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 36.552 11.344 -6.713 1.00 21.11 ? 26 PHE A CZ 1 ATOM 206 N N . ASP A 1 27 ? 35.747 16.398 -7.624 1.00 14.73 ? 27 ASP A N 1 ATOM 207 C CA . ASP A 1 27 ? 34.468 16.384 -8.335 1.00 15.55 ? 27 ASP A CA 1 ATOM 208 C C . ASP A 1 27 ? 33.462 17.409 -7.808 1.00 16.93 ? 27 ASP A C 1 ATOM 209 O O . ASP A 1 27 ? 32.257 17.170 -7.828 1.00 21.09 ? 27 ASP A O 1 ATOM 210 C CB . ASP A 1 27 ? 33.845 14.986 -8.310 1.00 15.38 ? 27 ASP A CB 1 ATOM 211 C CG . ASP A 1 27 ? 34.611 13.992 -9.155 1.00 20.01 ? 27 ASP A CG 1 ATOM 212 O OD1 . ASP A 1 27 ? 35.545 14.411 -9.869 1.00 15.53 ? 27 ASP A OD1 1 ATOM 213 O OD2 . ASP A 1 27 ? 34.273 12.790 -9.110 1.00 21.87 ? 27 ASP A OD2 1 ATOM 214 N N . GLY A 1 28 ? 33.963 18.545 -7.333 1.00 19.39 ? 28 GLY A N 1 ATOM 215 C CA . GLY A 1 28 ? 33.098 19.611 -6.861 1.00 16.40 ? 28 GLY A CA 1 ATOM 216 C C . GLY A 1 28 ? 32.871 19.623 -5.361 1.00 18.07 ? 28 GLY A C 1 ATOM 217 O O . GLY A 1 28 ? 32.216 20.524 -4.839 1.00 15.39 ? 28 GLY A O 1 ATOM 218 N N . ASP A 1 29 ? 33.419 18.633 -4.661 1.00 19.84 ? 29 ASP A N 1 ATOM 219 C CA . ASP A 1 29 ? 33.357 18.619 -3.202 1.00 17.53 ? 29 ASP A CA 1 ATOM 220 C C . ASP A 1 29 ? 34.724 18.873 -2.564 1.00 16.99 ? 29 ASP A C 1 ATOM 221 O O . ASP A 1 29 ? 35.758 18.503 -3.119 1.00 18.83 ? 29 ASP A O 1 ATOM 222 C CB . ASP A 1 29 ? 32.787 17.293 -2.691 1.00 18.47 ? 29 ASP A CB 1 ATOM 223 C CG . ASP A 1 29 ? 31.273 17.246 -2.748 1.00 21.72 ? 29 ASP A CG 1 ATOM 224 O OD1 . ASP A 1 29 ? 30.625 17.970 -1.962 1.00 21.69 ? 29 ASP A OD1 1 ATOM 225 O OD2 . ASP A 1 29 ? 30.731 16.485 -3.577 1.00 15.74 ? 29 ASP A OD2 1 ATOM 226 N N . GLU A 1 30 ? 34.719 19.506 -1.394 1.00 17.25 ? 30 GLU A N 1 ATOM 227 C CA . GLU A 1 30 ? 35.956 19.861 -0.705 1.00 17.05 ? 30 GLU A CA 1 ATOM 228 C C . GLU A 1 30 ? 36.526 18.667 0.045 1.00 18.74 ? 30 GLU A C 1 ATOM 229 O O . GLU A 1 30 ? 35.833 18.049 0.850 1.00 20.16 ? 30 GLU A O 1 ATOM 230 C CB . GLU A 1 30 ? 35.707 21.010 0.278 1.00 15.49 ? 30 GLU A CB 1 ATOM 231 C CG . GLU A 1 30 ? 36.903 21.338 1.167 1.00 18.70 ? 30 GLU A CG 1 ATOM 232 C CD . GLU A 1 30 ? 36.549 22.274 2.309 1.00 18.48 ? 30 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 30 ? 35.406 22.777 2.337 1.00 17.62 ? 30 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 30 ? 37.411 22.499 3.186 1.00 19.47 ? 30 GLU A OE2 1 ATOM 235 N N . ILE A 1 31 ? 37.783 18.330 -0.225 1.00 18.59 ? 31 ILE A N 1 ATOM 236 C CA . ILE A 1 31 ? 38.452 17.295 0.550 1.00 16.66 ? 31 ILE A CA 1 ATOM 237 C C . ILE A 1 31 ? 38.921 17.868 1.878 1.00 17.09 ? 31 ILE A C 1 ATOM 238 O O . ILE A 1 31 ? 38.624 17.333 2.946 1.00 16.90 ? 31 ILE A O 1 ATOM 239 C CB . ILE A 1 31 ? 39.668 16.716 -0.192 1.00 18.41 ? 31 ILE A CB 1 ATOM 240 C CG1 . ILE A 1 31 ? 39.265 16.212 -1.578 1.00 16.79 ? 31 ILE A CG1 1 ATOM 241 C CG2 . ILE A 1 31 ? 40.306 15.599 0.622 1.00 14.28 ? 31 ILE A CG2 1 ATOM 242 C CD1 . ILE A 1 31 ? 40.421 15.633 -2.369 1.00 14.01 ? 31 ILE A CD1 1 ATOM 243 N N . PHE A 1 32 ? 39.659 18.970 1.792 1.00 15.73 ? 32 PHE A N 1 ATOM 244 C CA . PHE A 1 32 ? 40.122 19.695 2.965 1.00 17.35 ? 32 PHE A CA 1 ATOM 245 C C . PHE A 1 32 ? 40.512 21.122 2.597 1.00 19.62 ? 32 PHE A C 1 ATOM 246 O O . PHE A 1 32 ? 40.665 21.453 1.422 1.00 21.83 ? 32 PHE A O 1 ATOM 247 C CB . PHE A 1 32 ? 41.307 18.973 3.620 1.00 16.95 ? 32 PHE A CB 1 ATOM 248 C CG . PHE A 1 32 ? 42.578 19.021 2.815 1.00 14.73 ? 32 PHE A CG 1 ATOM 249 C CD1 . PHE A 1 32 ? 43.487 20.055 2.978 1.00 14.74 ? 32 PHE A CD1 1 ATOM 250 C CD2 . PHE A 1 32 ? 42.868 18.020 1.900 1.00 17.11 ? 32 PHE A CD2 1 ATOM 251 C CE1 . PHE A 1 32 ? 44.658 20.095 2.239 1.00 15.76 ? 32 PHE A CE1 1 ATOM 252 C CE2 . PHE A 1 32 ? 44.037 18.053 1.160 1.00 17.63 ? 32 PHE A CE2 1 ATOM 253 C CZ . PHE A 1 32 ? 44.934 19.093 1.333 1.00 15.69 ? 32 PHE A CZ 1 ATOM 254 N N . HIS A 1 33 ? 40.666 21.965 3.610 1.00 20.19 ? 33 HIS A N 1 ATOM 255 C CA . HIS A 1 33 ? 41.320 23.251 3.428 1.00 18.61 ? 33 HIS A CA 1 ATOM 256 C C . HIS A 1 33 ? 42.330 23.439 4.548 1.00 22.08 ? 33 HIS A C 1 ATOM 257 O O . HIS A 1 33 ? 42.336 22.678 5.516 1.00 21.74 ? 33 HIS A O 1 ATOM 258 C CB . HIS A 1 33 ? 40.309 24.400 3.409 1.00 18.43 ? 33 HIS A CB 1 ATOM 259 C CG . HIS A 1 33 ? 39.669 24.668 4.736 1.00 18.35 ? 33 HIS A CG 1 ATOM 260 N ND1 . HIS A 1 33 ? 38.507 24.046 5.143 1.00 18.79 ? 33 HIS A ND1 1 ATOM 261 C CD2 . HIS A 1 33 ? 40.025 25.496 5.746 1.00 15.57 ? 33 HIS A CD2 1 ATOM 262 C CE1 . HIS A 1 33 ? 38.178 24.477 6.348 1.00 17.58 ? 33 HIS A CE1 1 ATOM 263 N NE2 . HIS A 1 33 ? 39.083 25.358 6.736 1.00 16.69 ? 33 HIS A NE2 1 ATOM 264 N N . VAL A 1 34 ? 43.185 24.446 4.420 1.00 21.17 ? 34 VAL A N 1 ATOM 265 C CA . VAL A 1 34 ? 44.140 24.752 5.475 1.00 20.86 ? 34 VAL A CA 1 ATOM 266 C C . VAL A 1 34 ? 43.737 26.010 6.234 1.00 22.64 ? 34 VAL A C 1 ATOM 267 O O . VAL A 1 34 ? 43.566 27.078 5.647 1.00 19.44 ? 34 VAL A O 1 ATOM 268 C CB . VAL A 1 34 ? 45.560 24.928 4.909 1.00 18.39 ? 34 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 34 ? 46.498 25.475 5.977 1.00 17.38 ? 34 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 34 ? 46.072 23.604 4.366 1.00 19.54 ? 34 VAL A CG2 1 ATOM 271 N N . ASP A 1 35 ? 43.586 25.871 7.546 1.00 26.01 ? 35 ASP A N 1 ATOM 272 C CA . ASP A 1 35 ? 43.383 27.015 8.416 1.00 29.63 ? 35 ASP A CA 1 ATOM 273 C C . ASP A 1 35 ? 44.709 27.758 8.474 1.00 32.97 ? 35 ASP A C 1 ATOM 274 O O . ASP A 1 35 ? 45.649 27.320 9.137 1.00 32.06 ? 35 ASP A O 1 ATOM 275 C CB . ASP A 1 35 ? 42.967 26.545 9.812 1.00 33.71 ? 35 ASP A CB 1 ATOM 276 C CG . ASP A 1 35 ? 42.557 27.691 10.727 1.00 35.44 ? 35 ASP A CG 1 ATOM 277 O OD1 . ASP A 1 35 ? 43.129 28.797 10.624 1.00 32.17 ? 35 ASP A OD1 1 ATOM 278 O OD2 . ASP A 1 35 ? 41.651 27.481 11.562 1.00 40.42 ? 35 ASP A OD2 1 ATOM 279 N N . MET A 1 36 ? 44.778 28.881 7.768 1.00 34.68 ? 36 MET A N 1 ATOM 280 C CA . MET A 1 36 ? 46.028 29.611 7.601 1.00 35.68 ? 36 MET A CA 1 ATOM 281 C C . MET A 1 36 ? 46.523 30.183 8.929 1.00 38.97 ? 36 MET A C 1 ATOM 282 O O . MET A 1 36 ? 47.724 30.197 9.197 1.00 39.10 ? 36 MET A O 1 ATOM 283 C CB . MET A 1 36 ? 45.882 30.715 6.549 1.00 34.85 ? 36 MET A CB 1 ATOM 284 C CG . MET A 1 36 ? 46.884 30.627 5.405 1.00 35.16 ? 36 MET A CG 1 ATOM 285 S SD . MET A 1 36 ? 46.767 29.089 4.466 1.00 34.80 ? 36 MET A SD 1 ATOM 286 C CE . MET A 1 36 ? 45.134 29.240 3.754 1.00 54.50 ? 36 MET A CE 1 ATOM 287 N N . ALA A 1 37 ? 45.590 30.656 9.750 1.00 38.09 ? 37 ALA A N 1 ATOM 288 C CA . ALA A 1 37 ? 45.919 31.251 11.043 1.00 37.12 ? 37 ALA A CA 1 ATOM 289 C C . ALA A 1 37 ? 46.454 30.222 12.042 1.00 36.30 ? 37 ALA A C 1 ATOM 290 O O . ALA A 1 37 ? 47.391 30.497 12.788 1.00 36.01 ? 37 ALA A O 1 ATOM 291 C CB . ALA A 1 37 ? 44.705 31.964 11.617 1.00 36.01 ? 37 ALA A CB 1 ATOM 292 N N . LYS A 1 38 ? 45.852 29.037 12.046 1.00 36.81 ? 38 LYS A N 1 ATOM 293 C CA . LYS A 1 38 ? 46.244 27.958 12.955 1.00 36.85 ? 38 LYS A CA 1 ATOM 294 C C . LYS A 1 38 ? 47.322 27.060 12.369 1.00 34.43 ? 38 LYS A C 1 ATOM 295 O O . LYS A 1 38 ? 47.895 26.232 13.081 1.00 34.35 ? 38 LYS A O 1 ATOM 296 C CB . LYS A 1 38 ? 45.035 27.104 13.342 1.00 37.44 ? 38 LYS A CB 1 ATOM 297 C CG . LYS A 1 38 ? 43.968 27.828 14.139 1.00 41.89 ? 38 LYS A CG 1 ATOM 298 C CD . LYS A 1 38 ? 42.951 26.832 14.674 1.00 45.72 ? 38 LYS A CD 1 ATOM 299 C CE . LYS A 1 38 ? 41.884 27.511 15.512 1.00 48.97 ? 38 LYS A CE 1 ATOM 300 N NZ . LYS A 1 38 ? 41.045 26.511 16.230 1.00 50.85 ? 38 LYS A NZ 1 ATOM 301 N N . LYS A 1 39 ? 47.591 27.230 11.078 1.00 33.65 ? 39 LYS A N 1 ATOM 302 C CA . LYS A 1 39 ? 48.544 26.391 10.359 1.00 34.48 ? 39 LYS A CA 1 ATOM 303 C C . LYS A 1 39 ? 48.130 24.929 10.512 1.00 34.31 ? 39 LYS A C 1 ATOM 304 O O . LYS A 1 39 ? 48.950 24.069 10.829 1.00 34.45 ? 39 LYS A O 1 ATOM 305 C CB . LYS A 1 39 ? 49.975 26.615 10.866 1.00 38.86 ? 39 LYS A CB 1 ATOM 306 C CG . LYS A 1 39 ? 50.493 28.043 10.762 1.00 44.84 ? 39 LYS A CG 1 ATOM 307 C CD . LYS A 1 39 ? 51.701 28.211 11.686 1.00 52.51 ? 39 LYS A CD 1 ATOM 308 C CE . LYS A 1 39 ? 52.333 29.598 11.623 1.00 55.69 ? 39 LYS A CE 1 ATOM 309 N NZ . LYS A 1 39 ? 52.342 30.214 10.277 1.00 54.67 ? 39 LYS A NZ 1 ATOM 310 N N . GLU A 1 40 ? 46.845 24.660 10.286 1.00 36.18 ? 40 GLU A N 1 ATOM 311 C CA . GLU A 1 40 ? 46.302 23.306 10.401 1.00 35.57 ? 40 GLU A CA 1 ATOM 312 C C . GLU A 1 40 ? 45.423 22.836 9.244 1.00 30.34 ? 40 GLU A C 1 ATOM 313 O O . GLU A 1 40 ? 44.721 23.627 8.614 1.00 28.02 ? 40 GLU A O 1 ATOM 314 C CB . GLU A 1 40 ? 45.516 23.162 11.708 1.00 40.46 ? 40 GLU A CB 1 ATOM 315 C CG . GLU A 1 40 ? 46.357 23.041 12.960 1.00 47.37 ? 40 GLU A CG 1 ATOM 316 C CD . GLU A 1 40 ? 45.503 22.975 14.210 1.00 55.64 ? 40 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 40 ? 44.337 22.536 14.108 1.00 58.31 ? 40 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 40 ? 45.994 23.357 15.292 1.00 58.88 ? 40 GLU A OE2 1 ATOM 319 N N . THR A 1 41 ? 45.474 21.535 8.980 1.00 28.62 ? 41 THR A N 1 ATOM 320 C CA . THR A 1 41 ? 44.662 20.910 7.947 1.00 25.67 ? 41 THR A CA 1 ATOM 321 C C . THR A 1 41 ? 43.276 20.616 8.522 1.00 25.25 ? 41 THR A C 1 ATOM 322 O O . THR A 1 41 ? 43.155 19.966 9.559 1.00 21.51 ? 41 THR A O 1 ATOM 323 C CB . THR A 1 41 ? 45.299 19.599 7.457 1.00 25.64 ? 41 THR A CB 1 ATOM 324 O OG1 . THR A 1 41 ? 46.551 19.885 6.823 1.00 27.89 ? 41 THR A OG1 1 ATOM 325 C CG2 . THR A 1 41 ? 44.387 18.897 6.461 1.00 21.33 ? 41 THR A CG2 1 ATOM 326 N N . VAL A 1 42 ? 42.235 21.092 7.844 1.00 24.09 ? 42 VAL A N 1 ATOM 327 C CA . VAL A 1 42 ? 40.859 20.881 8.292 1.00 23.26 ? 42 VAL A CA 1 ATOM 328 C C . VAL A 1 42 ? 40.141 19.984 7.297 1.00 21.96 ? 42 VAL A C 1 ATOM 329 O O . VAL A 1 42 ? 39.797 20.415 6.196 1.00 21.02 ? 42 VAL A O 1 ATOM 330 C CB . VAL A 1 42 ? 40.094 22.208 8.432 1.00 24.38 ? 42 VAL A CB 1 ATOM 331 C CG1 . VAL A 1 42 ? 38.691 21.953 8.960 1.00 24.13 ? 42 VAL A CG1 1 ATOM 332 C CG2 . VAL A 1 42 ? 40.847 23.162 9.343 1.00 24.70 ? 42 VAL A CG2 1 ATOM 333 N N . TRP A 1 43 ? 39.911 18.735 7.685 1.00 22.22 ? 43 TRP A N 1 ATOM 334 C CA . TRP A 1 43 ? 39.255 17.791 6.794 1.00 22.06 ? 43 TRP A CA 1 ATOM 335 C C . TRP A 1 43 ? 37.748 18.035 6.759 1.00 22.13 ? 43 TRP A C 1 ATOM 336 O O . TRP A 1 43 ? 37.137 18.297 7.796 1.00 21.17 ? 43 TRP A O 1 ATOM 337 C CB . TRP A 1 43 ? 39.559 16.358 7.232 1.00 24.00 ? 43 TRP A CB 1 ATOM 338 C CG . TRP A 1 43 ? 41.025 16.059 7.232 1.00 25.53 ? 43 TRP A CG 1 ATOM 339 C CD1 . TRP A 1 43 ? 41.873 16.170 8.297 1.00 26.62 ? 43 TRP A CD1 1 ATOM 340 C CD2 . TRP A 1 43 ? 41.836 15.685 6.112 1.00 23.51 ? 43 TRP A CD2 1 ATOM 341 N NE1 . TRP A 1 43 ? 43.152 15.844 7.922 1.00 27.76 ? 43 TRP A NE1 1 ATOM 342 C CE2 . TRP A 1 43 ? 43.159 15.547 6.584 1.00 24.95 ? 43 TRP A CE2 1 ATOM 343 C CE3 . TRP A 1 43 ? 41.573 15.434 4.763 1.00 19.92 ? 43 TRP A CE3 1 ATOM 344 C CZ2 . TRP A 1 43 ? 44.212 15.172 5.756 1.00 22.05 ? 43 TRP A CZ2 1 ATOM 345 C CZ3 . TRP A 1 43 ? 42.622 15.061 3.942 1.00 19.50 ? 43 TRP A CZ3 1 ATOM 346 C CH2 . TRP A 1 43 ? 43.924 14.934 4.441 1.00 17.88 ? 43 TRP A CH2 1 ATOM 347 N N . ARG A 1 44 ? 37.152 17.952 5.572 1.00 25.68 ? 44 ARG A N 1 ATOM 348 C CA . ARG A 1 44 ? 35.740 18.298 5.414 1.00 26.40 ? 44 ARG A CA 1 ATOM 349 C C . ARG A 1 44 ? 34.850 17.296 6.141 1.00 23.02 ? 44 ARG A C 1 ATOM 350 O O . ARG A 1 44 ? 33.872 17.666 6.789 1.00 22.13 ? 44 ARG A O 1 ATOM 351 C CB . ARG A 1 44 ? 35.361 18.372 3.935 1.00 24.10 ? 44 ARG A CB 1 ATOM 352 C CG . ARG A 1 44 ? 33.916 18.769 3.692 1.00 22.14 ? 44 ARG A CG 1 ATOM 353 C CD . ARG A 1 44 ? 33.624 20.138 4.280 1.00 18.98 ? 44 ARG A CD 1 ATOM 354 N NE . ARG A 1 44 ? 32.232 20.529 4.090 1.00 19.13 ? 44 ARG A NE 1 ATOM 355 C CZ . ARG A 1 44 ? 31.249 20.215 4.927 1.00 18.89 ? 44 ARG A CZ 1 ATOM 356 N NH1 . ARG A 1 44 ? 31.506 19.502 6.015 1.00 19.09 ? 44 ARG A NH1 1 ATOM 357 N NH2 . ARG A 1 44 ? 30.010 20.616 4.679 1.00 18.07 ? 44 ARG A NH2 1 ATOM 358 N N . LEU A 1 45 ? 35.209 16.022 6.025 1.00 23.98 ? 45 LEU A N 1 ATOM 359 C CA . LEU A 1 45 ? 34.632 14.971 6.848 1.00 24.62 ? 45 LEU A CA 1 ATOM 360 C C . LEU A 1 45 ? 35.743 14.420 7.726 1.00 27.39 ? 45 LEU A C 1 ATOM 361 O O . LEU A 1 45 ? 36.844 14.166 7.238 1.00 30.55 ? 45 LEU A O 1 ATOM 362 C CB . LEU A 1 45 ? 34.020 13.862 5.986 1.00 24.22 ? 45 LEU A CB 1 ATOM 363 C CG . LEU A 1 45 ? 32.884 14.249 5.035 1.00 27.91 ? 45 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 45 ? 32.220 13.007 4.450 1.00 30.87 ? 45 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 45 ? 31.856 15.132 5.734 1.00 22.25 ? 45 LEU A CD2 1 ATOM 366 N N . GLU A 1 46 ? 35.465 14.251 9.016 1.00 39.25 ? 46 GLU A N 1 ATOM 367 C CA . GLU A 1 46 ? 36.489 13.824 9.968 1.00 40.66 ? 46 GLU A CA 1 ATOM 368 C C . GLU A 1 46 ? 37.125 12.494 9.561 1.00 39.16 ? 46 GLU A C 1 ATOM 369 O O . GLU A 1 46 ? 38.305 12.256 9.823 1.00 34.23 ? 46 GLU A O 1 ATOM 370 C CB . GLU A 1 46 ? 35.926 13.743 11.396 1.00 45.90 ? 46 GLU A CB 1 ATOM 371 C CG . GLU A 1 46 ? 35.345 12.394 11.805 1.00 55.74 ? 46 GLU A CG 1 ATOM 372 C CD . GLU A 1 46 ? 36.384 11.467 12.415 1.00 62.28 ? 46 GLU A CD 1 ATOM 373 O OE1 . GLU A 1 46 ? 37.516 11.927 12.675 1.00 65.12 ? 46 GLU A OE1 1 ATOM 374 O OE2 . GLU A 1 46 ? 36.070 10.278 12.632 1.00 62.75 ? 46 GLU A OE2 1 ATOM 375 N N . GLU A 1 47 ? 36.332 11.632 8.929 1.00 39.44 ? 47 GLU A N 1 ATOM 376 C CA . GLU A 1 47 ? 36.800 10.323 8.491 1.00 40.68 ? 47 GLU A CA 1 ATOM 377 C C . GLU A 1 47 ? 37.987 10.435 7.534 1.00 38.96 ? 47 GLU A C 1 ATOM 378 O O . GLU A 1 47 ? 38.855 9.563 7.523 1.00 39.30 ? 47 GLU A O 1 ATOM 379 C CB . GLU A 1 47 ? 35.659 9.547 7.825 1.00 48.14 ? 47 GLU A CB 1 ATOM 380 C CG . GLU A 1 47 ? 35.072 10.197 6.583 1.00 53.35 ? 47 GLU A CG 1 ATOM 381 C CD . GLU A 1 47 ? 34.233 9.230 5.772 1.00 57.87 ? 47 GLU A CD 1 ATOM 382 O OE1 . GLU A 1 47 ? 33.060 9.010 6.139 1.00 58.21 ? 47 GLU A OE1 1 ATOM 383 O OE2 . GLU A 1 47 ? 34.749 8.686 4.774 1.00 58.61 ? 47 GLU A OE2 1 ATOM 384 N N . PHE A 1 48 ? 38.019 11.500 6.735 1.00 34.94 ? 48 PHE A N 1 ATOM 385 C CA . PHE A 1 48 ? 39.065 11.678 5.730 1.00 32.31 ? 48 PHE A CA 1 ATOM 386 C C . PHE A 1 48 ? 40.447 11.670 6.377 1.00 33.45 ? 48 PHE A C 1 ATOM 387 O O . PHE A 1 48 ? 41.402 11.124 5.823 1.00 28.24 ? 48 PHE A O 1 ATOM 388 C CB . PHE A 1 48 ? 38.882 12.993 4.965 1.00 26.01 ? 48 PHE A CB 1 ATOM 389 C CG . PHE A 1 48 ? 37.650 13.041 4.098 1.00 33.88 ? 48 PHE A CG 1 ATOM 390 C CD1 . PHE A 1 48 ? 36.863 11.917 3.907 1.00 27.44 ? 48 PHE A CD1 1 ATOM 391 C CD2 . PHE A 1 48 ? 37.293 14.218 3.458 1.00 23.75 ? 48 PHE A CD2 1 ATOM 392 C CE1 . PHE A 1 48 ? 35.738 11.969 3.105 1.00 27.38 ? 48 PHE A CE1 1 ATOM 393 C CE2 . PHE A 1 48 ? 36.171 14.277 2.655 1.00 23.61 ? 48 PHE A CE2 1 ATOM 394 C CZ . PHE A 1 48 ? 35.392 13.150 2.478 1.00 40.85 ? 48 PHE A CZ 1 ATOM 395 N N . GLY A 1 49 ? 40.544 12.284 7.552 1.00 32.82 ? 49 GLY A N 1 ATOM 396 C CA . GLY A 1 49 ? 41.815 12.445 8.232 1.00 29.82 ? 49 GLY A CA 1 ATOM 397 C C . GLY A 1 49 ? 42.356 11.183 8.877 1.00 32.12 ? 49 GLY A C 1 ATOM 398 O O . GLY A 1 49 ? 43.494 11.164 9.346 1.00 43.71 ? 49 GLY A O 1 ATOM 399 N N . ARG A 1 50 ? 41.547 10.128 8.913 1.00 35.30 ? 50 ARG A N 1 ATOM 400 C CA . ARG A 1 50 ? 42.006 8.849 9.442 1.00 39.56 ? 50 ARG A CA 1 ATOM 401 C C . ARG A 1 50 ? 42.760 8.077 8.366 1.00 39.75 ? 50 ARG A C 1 ATOM 402 O O . ARG A 1 50 ? 43.513 7.150 8.662 1.00 41.63 ? 50 ARG A O 1 ATOM 403 C CB . ARG A 1 50 ? 40.834 8.008 9.954 1.00 44.91 ? 50 ARG A CB 1 ATOM 404 C CG . ARG A 1 50 ? 40.073 8.622 11.120 1.00 51.76 ? 50 ARG A CG 1 ATOM 405 C CD . ARG A 1 50 ? 39.228 7.569 11.826 1.00 59.19 ? 50 ARG A CD 1 ATOM 406 N NE . ARG A 1 50 ? 38.254 6.926 10.948 1.00 63.53 ? 50 ARG A NE 1 ATOM 407 C CZ . ARG A 1 50 ? 36.972 7.267 10.867 1.00 64.87 ? 50 ARG A CZ 1 ATOM 408 N NH1 . ARG A 1 50 ? 36.494 8.246 11.621 1.00 65.69 ? 50 ARG A NH1 1 ATOM 409 N NH2 . ARG A 1 50 ? 36.164 6.619 10.038 1.00 65.18 ? 50 ARG A NH2 1 ATOM 410 N N . PHE A 1 51 ? 42.554 8.474 7.114 1.00 40.61 ? 51 PHE A N 1 ATOM 411 C CA . PHE A 1 51 ? 43.096 7.752 5.967 1.00 42.08 ? 51 PHE A CA 1 ATOM 412 C C . PHE A 1 51 ? 44.217 8.519 5.279 1.00 37.45 ? 51 PHE A C 1 ATOM 413 O O . PHE A 1 51 ? 45.036 7.933 4.571 1.00 41.21 ? 51 PHE A O 1 ATOM 414 C CB . PHE A 1 51 ? 41.988 7.434 4.959 1.00 43.64 ? 51 PHE A CB 1 ATOM 415 C CG . PHE A 1 51 ? 40.870 6.612 5.527 1.00 51.11 ? 51 PHE A CG 1 ATOM 416 C CD1 . PHE A 1 51 ? 41.042 5.259 5.766 1.00 54.56 ? 51 PHE A CD1 1 ATOM 417 C CD2 . PHE A 1 51 ? 39.643 7.186 5.809 1.00 53.57 ? 51 PHE A CD2 1 ATOM 418 C CE1 . PHE A 1 51 ? 40.016 4.496 6.287 1.00 58.58 ? 51 PHE A CE1 1 ATOM 419 C CE2 . PHE A 1 51 ? 38.610 6.429 6.331 1.00 57.64 ? 51 PHE A CE2 1 ATOM 420 C CZ . PHE A 1 51 ? 38.797 5.082 6.568 1.00 59.64 ? 51 PHE A CZ 1 ATOM 421 N N . ALA A 1 52 ? 44.252 9.829 5.485 1.00 30.82 ? 52 ALA A N 1 ATOM 422 C CA . ALA A 1 52 ? 45.230 10.668 4.810 1.00 29.46 ? 52 ALA A CA 1 ATOM 423 C C . ALA A 1 52 ? 45.752 11.764 5.725 1.00 29.85 ? 52 ALA A C 1 ATOM 424 O O . ALA A 1 52 ? 45.159 12.066 6.761 1.00 29.72 ? 52 ALA A O 1 ATOM 425 C CB . ALA A 1 52 ? 44.622 11.275 3.554 1.00 28.26 ? 52 ALA A CB 1 ATOM 426 N N . SER A 1 53 ? 46.868 12.359 5.324 1.00 29.12 ? 53 SER A N 1 ATOM 427 C CA . SER A 1 53 ? 47.456 13.472 6.050 1.00 29.83 ? 53 SER A CA 1 ATOM 428 C C . SER A 1 53 ? 47.859 14.545 5.051 1.00 29.98 ? 53 SER A C 1 ATOM 429 O O . SER A 1 53 ? 47.972 14.278 3.855 1.00 28.29 ? 53 SER A O 1 ATOM 430 C CB . SER A 1 53 ? 48.669 13.014 6.863 1.00 33.94 ? 53 SER A CB 1 ATOM 431 O OG . SER A 1 53 ? 49.701 12.536 6.020 1.00 40.96 ? 53 SER A OG 1 ATOM 432 N N . PHE A 1 54 ? 48.079 15.758 5.542 1.00 30.97 ? 54 PHE A N 1 ATOM 433 C CA . PHE A 1 54 ? 48.613 16.816 4.702 1.00 26.89 ? 54 PHE A CA 1 ATOM 434 C C . PHE A 1 54 ? 49.474 17.790 5.496 1.00 28.81 ? 54 PHE A C 1 ATOM 435 O O . PHE A 1 54 ? 49.050 18.312 6.528 1.00 31.92 ? 54 PHE A O 1 ATOM 436 C CB . PHE A 1 54 ? 47.484 17.569 3.995 1.00 24.41 ? 54 PHE A CB 1 ATOM 437 C CG . PHE A 1 54 ? 47.958 18.683 3.111 1.00 22.62 ? 54 PHE A CG 1 ATOM 438 C CD1 . PHE A 1 54 ? 48.521 18.407 1.877 1.00 22.36 ? 54 PHE A CD1 1 ATOM 439 C CD2 . PHE A 1 54 ? 47.844 20.003 3.513 1.00 18.22 ? 54 PHE A CD2 1 ATOM 440 C CE1 . PHE A 1 54 ? 48.956 19.424 1.058 1.00 15.54 ? 54 PHE A CE1 1 ATOM 441 C CE2 . PHE A 1 54 ? 48.280 21.028 2.697 1.00 16.85 ? 54 PHE A CE2 1 ATOM 442 C CZ . PHE A 1 54 ? 48.838 20.738 1.468 1.00 15.20 ? 54 PHE A CZ 1 ATOM 443 N N . GLU A 1 55 ? 50.682 18.038 5.004 1.00 27.17 ? 55 GLU A N 1 ATOM 444 C CA . GLU A 1 55 ? 51.582 18.981 5.650 1.00 29.58 ? 55 GLU A CA 1 ATOM 445 C C . GLU A 1 55 ? 51.131 20.405 5.358 1.00 28.12 ? 55 GLU A C 1 ATOM 446 O O . GLU A 1 55 ? 51.357 20.934 4.268 1.00 26.54 ? 55 GLU A O 1 ATOM 447 C CB . GLU A 1 55 ? 53.020 18.768 5.172 1.00 29.11 ? 55 GLU A CB 1 ATOM 448 C CG . GLU A 1 55 ? 54.003 19.788 5.723 1.00 31.47 ? 55 GLU A CG 1 ATOM 449 C CD . GLU A 1 55 ? 53.948 19.886 7.235 1.00 35.93 ? 55 GLU A CD 1 ATOM 450 O OE1 . GLU A 1 55 ? 54.280 18.886 7.904 1.00 39.99 ? 55 GLU A OE1 1 ATOM 451 O OE2 . GLU A 1 55 ? 53.564 20.955 7.753 1.00 38.18 ? 55 GLU A OE2 1 ATOM 452 N N . ALA A 1 56 ? 50.472 21.006 6.343 1.00 24.52 ? 56 ALA A N 1 ATOM 453 C CA . ALA A 1 56 ? 49.862 22.322 6.197 1.00 24.55 ? 56 ALA A CA 1 ATOM 454 C C . ALA A 1 56 ? 50.864 23.403 5.795 1.00 27.88 ? 56 ALA A C 1 ATOM 455 O O . ALA A 1 56 ? 50.496 24.385 5.149 1.00 26.15 ? 56 ALA A O 1 ATOM 456 C CB . ALA A 1 56 ? 49.143 22.714 7.479 1.00 21.13 ? 56 ALA A CB 1 ATOM 457 N N . GLN A 1 57 ? 52.124 23.216 6.178 1.00 28.27 ? 57 GLN A N 1 ATOM 458 C CA . GLN A 1 57 ? 53.161 24.206 5.905 1.00 30.41 ? 57 GLN A CA 1 ATOM 459 C C . GLN A 1 57 ? 53.317 24.488 4.419 1.00 27.22 ? 57 GLN A C 1 ATOM 460 O O . GLN A 1 57 ? 53.618 25.616 4.028 1.00 30.02 ? 57 GLN A O 1 ATOM 461 C CB . GLN A 1 57 ? 54.502 23.755 6.490 1.00 35.32 ? 57 GLN A CB 1 ATOM 462 C CG . GLN A 1 57 ? 55.547 24.859 6.549 1.00 41.07 ? 57 GLN A CG 1 ATOM 463 C CD . GLN A 1 57 ? 55.114 26.035 7.400 1.00 47.47 ? 57 GLN A CD 1 ATOM 464 O OE1 . GLN A 1 57 ? 54.786 25.879 8.576 1.00 51.69 ? 57 GLN A OE1 1 ATOM 465 N NE2 . GLN A 1 57 ? 55.107 27.222 6.806 1.00 46.04 ? 57 GLN A NE2 1 ATOM 466 N N . GLY A 1 58 ? 53.128 23.465 3.592 1.00 26.46 ? 58 GLY A N 1 ATOM 467 C CA . GLY A 1 58 ? 53.256 23.656 2.162 1.00 26.08 ? 58 GLY A CA 1 ATOM 468 C C . GLY A 1 58 ? 52.227 24.639 1.642 1.00 26.90 ? 58 GLY A C 1 ATOM 469 O O . GLY A 1 58 ? 52.492 25.370 0.688 1.00 27.40 ? 58 GLY A O 1 ATOM 470 N N . ALA A 1 59 ? 51.048 24.659 2.261 1.00 26.54 ? 59 ALA A N 1 ATOM 471 C CA . ALA A 1 59 ? 50.016 25.602 1.851 1.00 23.96 ? 59 ALA A CA 1 ATOM 472 C C . ALA A 1 59 ? 50.460 27.032 2.133 1.00 24.48 ? 59 ALA A C 1 ATOM 473 O O . ALA A 1 59 ? 50.192 27.947 1.355 1.00 23.43 ? 59 ALA A O 1 ATOM 474 C CB . ALA A 1 59 ? 48.703 25.298 2.550 1.00 21.56 ? 59 ALA A CB 1 ATOM 475 N N . LEU A 1 60 ? 51.130 27.205 3.268 1.00 26.80 ? 60 LEU A N 1 ATOM 476 C CA . LEU A 1 60 ? 51.616 28.512 3.693 1.00 30.39 ? 60 LEU A CA 1 ATOM 477 C C . LEU A 1 60 ? 52.613 29.090 2.699 1.00 28.13 ? 60 LEU A C 1 ATOM 478 O O . LEU A 1 60 ? 52.603 30.286 2.406 1.00 28.92 ? 60 LEU A O 1 ATOM 479 C CB . LEU A 1 60 ? 52.229 28.435 5.091 1.00 36.35 ? 60 LEU A CB 1 ATOM 480 C CG . LEU A 1 60 ? 51.267 28.561 6.276 1.00 39.50 ? 60 LEU A CG 1 ATOM 481 C CD1 . LEU A 1 60 ? 50.330 27.366 6.388 1.00 40.42 ? 60 LEU A CD1 1 ATOM 482 C CD2 . LEU A 1 60 ? 52.062 28.731 7.547 1.00 40.08 ? 60 LEU A CD2 1 ATOM 483 N N . ALA A 1 61 ? 53.482 28.217 2.195 1.00 26.43 ? 61 ALA A N 1 ATOM 484 C CA . ALA A 1 61 ? 54.504 28.602 1.233 1.00 26.51 ? 61 ALA A CA 1 ATOM 485 C C . ALA A 1 61 ? 53.880 29.058 -0.076 1.00 24.34 ? 61 ALA A C 1 ATOM 486 O O . ALA A 1 61 ? 54.303 30.051 -0.667 1.00 27.09 ? 61 ALA A O 1 ATOM 487 C CB . ALA A 1 61 ? 55.469 27.451 0.993 1.00 25.95 ? 61 ALA A CB 1 ATOM 488 N N . ASN A 1 62 ? 52.869 28.320 -0.522 1.00 21.96 ? 62 ASN A N 1 ATOM 489 C CA . ASN A 1 62 ? 52.150 28.655 -1.742 1.00 20.02 ? 62 ASN A CA 1 ATOM 490 C C . ASN A 1 62 ? 51.438 29.998 -1.648 1.00 17.73 ? 62 ASN A C 1 ATOM 491 O O . ASN A 1 62 ? 51.477 30.800 -2.583 1.00 15.26 ? 62 ASN A O 1 ATOM 492 C CB . ASN A 1 62 ? 51.152 27.553 -2.100 1.00 19.59 ? 62 ASN A CB 1 ATOM 493 C CG . ASN A 1 62 ? 51.767 26.470 -2.963 1.00 23.47 ? 62 ASN A CG 1 ATOM 494 O OD1 . ASN A 1 62 ? 52.987 26.315 -3.011 1.00 27.19 ? 62 ASN A OD1 1 ATOM 495 N ND2 . ASN A 1 62 ? 50.922 25.708 -3.646 1.00 22.84 ? 62 ASN A ND2 1 ATOM 496 N N . ILE A 1 63 ? 50.799 30.241 -0.507 1.00 15.66 ? 63 ILE A N 1 ATOM 497 C CA . ILE A 1 63 ? 50.062 31.479 -0.287 1.00 17.66 ? 63 ILE A CA 1 ATOM 498 C C . ILE A 1 63 ? 51.005 32.680 -0.294 1.00 18.82 ? 63 ILE A C 1 ATOM 499 O O . ILE A 1 63 ? 50.662 33.751 -0.797 1.00 25.27 ? 63 ILE A O 1 ATOM 500 C CB . ILE A 1 63 ? 49.257 31.429 1.032 1.00 20.26 ? 63 ILE A CB 1 ATOM 501 C CG1 . ILE A 1 63 ? 48.136 30.394 0.930 1.00 20.53 ? 63 ILE A CG1 1 ATOM 502 C CG2 . ILE A 1 63 ? 48.686 32.796 1.379 1.00 19.23 ? 63 ILE A CG2 1 ATOM 503 C CD1 . ILE A 1 63 ? 47.227 30.597 -0.263 1.00 18.74 ? 63 ILE A CD1 1 ATOM 504 N N . ALA A 1 64 ? 52.207 32.483 0.239 1.00 15.48 ? 64 ALA A N 1 ATOM 505 C CA . ALA A 1 64 ? 53.222 33.528 0.232 1.00 19.54 ? 64 ALA A CA 1 ATOM 506 C C . ALA A 1 64 ? 53.639 33.892 -1.190 1.00 21.44 ? 64 ALA A C 1 ATOM 507 O O . ALA A 1 64 ? 53.837 35.067 -1.505 1.00 21.21 ? 64 ALA A O 1 ATOM 508 C CB . ALA A 1 64 ? 54.436 33.098 1.047 1.00 17.05 ? 64 ALA A CB 1 ATOM 509 N N . VAL A 1 65 ? 53.771 32.881 -2.043 1.00 18.02 ? 65 VAL A N 1 ATOM 510 C CA . VAL A 1 65 ? 54.085 33.103 -3.451 1.00 14.63 ? 65 VAL A CA 1 ATOM 511 C C . VAL A 1 65 ? 52.939 33.829 -4.151 1.00 15.50 ? 65 VAL A C 1 ATOM 512 O O . VAL A 1 65 ? 53.163 34.739 -4.951 1.00 16.26 ? 65 VAL A O 1 ATOM 513 C CB . VAL A 1 65 ? 54.373 31.772 -4.178 1.00 14.01 ? 65 VAL A CB 1 ATOM 514 C CG1 . VAL A 1 65 ? 54.463 31.988 -5.680 1.00 14.96 ? 65 VAL A CG1 1 ATOM 515 C CG2 . VAL A 1 65 ? 55.660 31.155 -3.655 1.00 14.63 ? 65 VAL A CG2 1 ATOM 516 N N . ASP A 1 66 ? 51.711 33.424 -3.833 1.00 17.23 ? 66 ASP A N 1 ATOM 517 C CA . ASP A 1 66 ? 50.515 34.025 -4.416 1.00 15.65 ? 66 ASP A CA 1 ATOM 518 C C . ASP A 1 66 ? 50.398 35.497 -4.037 1.00 17.00 ? 66 ASP A C 1 ATOM 519 O O . ASP A 1 66 ? 49.967 36.322 -4.844 1.00 21.83 ? 66 ASP A O 1 ATOM 520 C CB . ASP A 1 66 ? 49.259 33.278 -3.969 1.00 17.83 ? 66 ASP A CB 1 ATOM 521 C CG . ASP A 1 66 ? 49.236 31.839 -4.444 1.00 20.38 ? 66 ASP A CG 1 ATOM 522 O OD1 . ASP A 1 66 ? 49.915 31.528 -5.445 1.00 22.53 ? 66 ASP A OD1 1 ATOM 523 O OD2 . ASP A 1 66 ? 48.537 31.021 -3.813 1.00 25.41 ? 66 ASP A OD2 1 ATOM 524 N N . LYS A 1 67 ? 50.777 35.816 -2.803 1.00 15.69 ? 67 LYS A N 1 ATOM 525 C CA . LYS A 1 67 ? 50.772 37.192 -2.328 1.00 17.83 ? 67 LYS A CA 1 ATOM 526 C C . LYS A 1 67 ? 51.757 38.039 -3.123 1.00 19.11 ? 67 LYS A C 1 ATOM 527 O O . LYS A 1 67 ? 51.437 39.146 -3.559 1.00 15.42 ? 67 LYS A O 1 ATOM 528 C CB . LYS A 1 67 ? 51.117 37.227 -0.839 1.00 20.86 ? 67 LYS A CB 1 ATOM 529 C CG . LYS A 1 67 ? 51.292 38.616 -0.255 1.00 24.16 ? 67 LYS A CG 1 ATOM 530 C CD . LYS A 1 67 ? 51.594 38.534 1.233 1.00 27.88 ? 67 LYS A CD 1 ATOM 531 C CE . LYS A 1 67 ? 51.633 39.911 1.872 1.00 34.85 ? 67 LYS A CE 1 ATOM 532 N NZ . LYS A 1 67 ? 50.402 40.697 1.595 1.00 40.60 ? 67 LYS A NZ 1 ATOM 533 N N . ALA A 1 68 ? 52.963 37.508 -3.297 1.00 19.08 ? 68 ALA A N 1 ATOM 534 C CA . ALA A 1 68 ? 53.998 38.178 -4.069 1.00 19.84 ? 68 ALA A CA 1 ATOM 535 C C . ALA A 1 68 ? 53.604 38.284 -5.533 1.00 20.94 ? 68 ALA A C 1 ATOM 536 O O . ALA A 1 68 ? 53.854 39.297 -6.185 1.00 20.60 ? 68 ALA A O 1 ATOM 537 C CB . ALA A 1 68 ? 55.326 37.450 -3.924 1.00 18.70 ? 68 ALA A CB 1 ATOM 538 N N . ASN A 1 69 ? 52.990 37.224 -6.046 1.00 19.53 ? 69 ASN A N 1 ATOM 539 C CA . ASN A 1 69 ? 52.514 37.216 -7.421 1.00 18.30 ? 69 ASN A CA 1 ATOM 540 C C . ASN A 1 69 ? 51.389 38.212 -7.698 1.00 15.24 ? 69 ASN A C 1 ATOM 541 O O . ASN A 1 69 ? 51.345 38.832 -8.760 1.00 16.58 ? 69 ASN A O 1 ATOM 542 C CB . ASN A 1 69 ? 52.089 35.804 -7.832 1.00 18.53 ? 69 ASN A CB 1 ATOM 543 C CG . ASN A 1 69 ? 53.271 34.892 -8.091 1.00 20.92 ? 69 ASN A CG 1 ATOM 544 O OD1 . ASN A 1 69 ? 54.417 35.332 -8.102 1.00 24.62 ? 69 ASN A OD1 1 ATOM 545 N ND2 . ASN A 1 69 ? 52.995 33.607 -8.292 1.00 18.60 ? 69 ASN A ND2 1 ATOM 546 N N . LEU A 1 70 ? 50.482 38.360 -6.737 1.00 13.56 ? 70 LEU A N 1 ATOM 547 C CA . LEU A 1 70 ? 49.385 39.319 -6.848 1.00 17.39 ? 70 LEU A CA 1 ATOM 548 C C . LEU A 1 70 ? 49.865 40.763 -6.991 1.00 21.89 ? 70 LEU A C 1 ATOM 549 O O . LEU A 1 70 ? 49.325 41.532 -7.785 1.00 24.07 ? 70 LEU A O 1 ATOM 550 C CB . LEU A 1 70 ? 48.451 39.208 -5.641 1.00 16.73 ? 70 LEU A CB 1 ATOM 551 C CG . LEU A 1 70 ? 47.276 40.189 -5.613 1.00 18.69 ? 70 LEU A CG 1 ATOM 552 C CD1 . LEU A 1 70 ? 46.423 40.043 -6.867 1.00 15.94 ? 70 LEU A CD1 1 ATOM 553 C CD2 . LEU A 1 70 ? 46.431 39.992 -4.360 1.00 21.09 ? 70 LEU A CD2 1 ATOM 554 N N . GLU A 1 71 ? 50.884 41.116 -6.210 1.00 20.06 ? 71 GLU A N 1 ATOM 555 C CA . GLU A 1 71 ? 51.504 42.437 -6.266 1.00 18.45 ? 71 GLU A CA 1 ATOM 556 C C . GLU A 1 71 ? 52.017 42.756 -7.661 1.00 18.38 ? 71 GLU A C 1 ATOM 557 O O . GLU A 1 71 ? 51.742 43.823 -8.213 1.00 20.00 ? 71 GLU A O 1 ATOM 558 C CB . GLU A 1 71 ? 52.657 42.507 -5.265 1.00 23.36 ? 71 GLU A CB 1 ATOM 559 C CG . GLU A 1 71 ? 53.637 43.640 -5.521 1.00 38.31 ? 71 GLU A CG 1 ATOM 560 C CD . GLU A 1 71 ? 54.794 43.641 -4.541 1.00 49.27 ? 71 GLU A CD 1 ATOM 561 O OE1 . GLU A 1 71 ? 55.797 44.336 -4.806 1.00 53.27 ? 71 GLU A OE1 1 ATOM 562 O OE2 . GLU A 1 71 ? 54.699 42.947 -3.506 1.00 51.80 ? 71 GLU A OE2 1 ATOM 563 N N . ILE A 1 72 ? 52.772 41.816 -8.215 1.00 19.06 ? 72 ILE A N 1 ATOM 564 C CA . ILE A 1 72 ? 53.347 41.942 -9.545 1.00 18.97 ? 72 ILE A CA 1 ATOM 565 C C . ILE A 1 72 ? 52.243 42.083 -10.590 1.00 20.42 ? 72 ILE A C 1 ATOM 566 O O . ILE A 1 72 ? 52.298 42.973 -11.440 1.00 23.55 ? 72 ILE A O 1 ATOM 567 C CB . ILE A 1 72 ? 54.241 40.735 -9.872 1.00 20.08 ? 72 ILE A CB 1 ATOM 568 C CG1 . ILE A 1 72 ? 55.540 40.826 -9.066 1.00 25.00 ? 72 ILE A CG1 1 ATOM 569 C CG2 . ILE A 1 72 ? 54.530 40.664 -11.365 1.00 17.52 ? 72 ILE A CG2 1 ATOM 570 C CD1 . ILE A 1 72 ? 56.406 39.595 -9.129 1.00 27.09 ? 72 ILE A CD1 1 ATOM 571 N N A MET A 1 73 ? 51.253 41.194 -10.527 0.62 16.29 ? 73 MET A N 1 ATOM 572 N N B MET A 1 73 ? 51.238 41.217 -10.514 0.38 16.44 ? 73 MET A N 1 ATOM 573 C CA A MET A 1 73 ? 50.155 41.184 -11.493 0.62 15.34 ? 73 MET A CA 1 ATOM 574 C CA B MET A 1 73 ? 50.180 41.204 -11.516 0.38 15.08 ? 73 MET A CA 1 ATOM 575 C C A MET A 1 73 ? 49.307 42.446 -11.409 0.62 14.81 ? 73 MET A C 1 ATOM 576 C C B MET A 1 73 ? 49.281 42.435 -11.411 0.38 15.15 ? 73 MET A C 1 ATOM 577 O O A MET A 1 73 ? 48.874 42.980 -12.430 0.62 16.54 ? 73 MET A O 1 ATOM 578 O O B MET A 1 73 ? 48.794 42.944 -12.421 0.38 16.22 ? 73 MET A O 1 ATOM 579 C CB A MET A 1 73 ? 49.267 39.952 -11.295 0.62 17.26 ? 73 MET A CB 1 ATOM 580 C CB B MET A 1 73 ? 49.354 39.920 -11.421 0.38 16.50 ? 73 MET A CB 1 ATOM 581 C CG A MET A 1 73 ? 49.954 38.629 -11.587 0.62 16.10 ? 73 MET A CG 1 ATOM 582 C CG B MET A 1 73 ? 48.263 39.818 -12.460 0.38 16.82 ? 73 MET A CG 1 ATOM 583 S SD A MET A 1 73 ? 50.695 38.572 -13.228 0.62 23.08 ? 73 MET A SD 1 ATOM 584 S SD B MET A 1 73 ? 48.930 39.833 -14.124 0.38 14.86 ? 73 MET A SD 1 ATOM 585 C CE A MET A 1 73 ? 49.262 38.869 -14.263 0.62 18.69 ? 73 MET A CE 1 ATOM 586 C CE B MET A 1 73 ? 50.040 38.440 -14.011 0.38 21.98 ? 73 MET A CE 1 ATOM 587 N N . THR A 1 74 ? 49.065 42.907 -10.187 1.00 13.14 ? 74 THR A N 1 ATOM 588 C CA . THR A 1 74 ? 48.306 44.132 -9.954 1.00 18.77 ? 74 THR A CA 1 ATOM 589 C C . THR A 1 74 ? 48.981 45.299 -10.661 1.00 24.28 ? 74 THR A C 1 ATOM 590 O O . THR A 1 74 ? 48.339 46.103 -11.338 1.00 26.39 ? 74 THR A O 1 ATOM 591 C CB . THR A 1 74 ? 48.165 44.435 -8.451 1.00 17.99 ? 74 THR A CB 1 ATOM 592 O OG1 . THR A 1 74 ? 47.454 43.368 -7.813 1.00 17.38 ? 74 THR A OG1 1 ATOM 593 C CG2 . THR A 1 74 ? 47.408 45.736 -8.241 1.00 17.69 ? 74 THR A CG2 1 ATOM 594 N N . LYS A 1 75 ? 50.295 45.370 -10.486 1.00 24.09 ? 75 LYS A N 1 ATOM 595 C CA . LYS A 1 75 ? 51.125 46.370 -11.135 1.00 27.30 ? 75 LYS A CA 1 ATOM 596 C C . LYS A 1 75 ? 51.098 46.254 -12.660 1.00 23.83 ? 75 LYS A C 1 ATOM 597 O O . LYS A 1 75 ? 50.957 47.252 -13.368 1.00 26.62 ? 75 LYS A O 1 ATOM 598 C CB . LYS A 1 75 ? 52.564 46.250 -10.626 1.00 32.27 ? 75 LYS A CB 1 ATOM 599 C CG . LYS A 1 75 ? 53.409 47.495 -10.704 1.00 38.30 ? 75 LYS A CG 1 ATOM 600 C CD . LYS A 1 75 ? 54.746 47.248 -10.020 1.00 41.81 ? 75 LYS A CD 1 ATOM 601 C CE . LYS A 1 75 ? 54.540 46.705 -8.609 1.00 44.28 ? 75 LYS A CE 1 ATOM 602 N NZ . LYS A 1 75 ? 55.821 46.490 -7.883 1.00 47.11 ? 75 LYS A NZ 1 ATOM 603 N N . ARG A 1 76 ? 51.244 45.028 -13.153 1.00 19.70 ? 76 ARG A N 1 ATOM 604 C CA . ARG A 1 76 ? 51.227 44.737 -14.585 1.00 21.44 ? 76 ARG A CA 1 ATOM 605 C C . ARG A 1 76 ? 49.924 45.170 -15.268 1.00 21.02 ? 76 ARG A C 1 ATOM 606 O O . ARG A 1 76 ? 49.928 45.609 -16.418 1.00 21.49 ? 76 ARG A O 1 ATOM 607 C CB . ARG A 1 76 ? 51.463 43.241 -14.820 1.00 22.83 ? 76 ARG A CB 1 ATOM 608 C CG . ARG A 1 76 ? 52.056 42.937 -16.189 1.00 25.92 ? 76 ARG A CG 1 ATOM 609 C CD . ARG A 1 76 ? 52.092 41.448 -16.504 1.00 26.84 ? 76 ARG A CD 1 ATOM 610 N NE . ARG A 1 76 ? 53.195 40.805 -15.792 1.00 25.99 ? 76 ARG A NE 1 ATOM 611 C CZ . ARG A 1 76 ? 53.313 39.495 -15.601 1.00 26.47 ? 76 ARG A CZ 1 ATOM 612 N NH1 . ARG A 1 76 ? 54.354 39.014 -14.934 1.00 27.97 ? 76 ARG A NH1 1 ATOM 613 N NH2 . ARG A 1 76 ? 52.408 38.661 -16.094 1.00 22.45 ? 76 ARG A NH2 1 ATOM 614 N N . SER A 1 77 ? 48.814 45.033 -14.548 1.00 17.39 ? 77 SER A N 1 ATOM 615 C CA . SER A 1 77 ? 47.484 45.347 -15.069 1.00 15.98 ? 77 SER A CA 1 ATOM 616 C C . SER A 1 77 ? 47.153 46.836 -14.990 1.00 17.80 ? 77 SER A C 1 ATOM 617 O O . SER A 1 77 ? 46.033 47.243 -15.299 1.00 15.83 ? 77 SER A O 1 ATOM 618 C CB . SER A 1 77 ? 46.422 44.561 -14.294 1.00 16.87 ? 77 SER A CB 1 ATOM 619 O OG . SER A 1 77 ? 46.188 45.134 -13.019 1.00 16.55 ? 77 SER A OG 1 ATOM 620 N N . ASN A 1 78 ? 48.129 47.634 -14.563 1.00 18.37 ? 78 ASN A N 1 ATOM 621 C CA . ASN A 1 78 ? 47.935 49.056 -14.278 1.00 20.56 ? 78 ASN A CA 1 ATOM 622 C C . ASN A 1 78 ? 46.868 49.264 -13.207 1.00 24.02 ? 78 ASN A C 1 ATOM 623 O O . ASN A 1 78 ? 46.027 50.158 -13.312 1.00 25.98 ? 78 ASN A O 1 ATOM 624 C CB . ASN A 1 78 ? 47.589 49.846 -15.548 1.00 24.65 ? 78 ASN A CB 1 ATOM 625 C CG . ASN A 1 78 ? 48.619 49.674 -16.649 1.00 30.66 ? 78 ASN A CG 1 ATOM 626 O OD1 . ASN A 1 78 ? 49.825 49.729 -16.404 1.00 25.17 ? 78 ASN A OD1 1 ATOM 627 N ND2 . ASN A 1 78 ? 48.141 49.471 -17.875 1.00 44.26 ? 78 ASN A ND2 1 ATOM 628 N N . TYR A 1 79 ? 46.920 48.418 -12.181 1.00 22.57 ? 79 TYR A N 1 ATOM 629 C CA . TYR A 1 79 ? 46.016 48.488 -11.033 1.00 17.95 ? 79 TYR A CA 1 ATOM 630 C C . TYR A 1 79 ? 44.533 48.409 -11.391 1.00 19.30 ? 79 TYR A C 1 ATOM 631 O O . TYR A 1 79 ? 43.712 49.148 -10.847 1.00 19.13 ? 79 TYR A O 1 ATOM 632 C CB . TYR A 1 79 ? 46.312 49.734 -10.196 1.00 16.66 ? 79 TYR A CB 1 ATOM 633 C CG . TYR A 1 79 ? 47.697 49.721 -9.591 1.00 14.99 ? 79 TYR A CG 1 ATOM 634 C CD1 . TYR A 1 79 ? 48.801 50.119 -10.331 1.00 15.95 ? 79 TYR A CD1 1 ATOM 635 C CD2 . TYR A 1 79 ? 47.901 49.290 -8.288 1.00 13.40 ? 79 TYR A CD2 1 ATOM 636 C CE1 . TYR A 1 79 ? 50.068 50.103 -9.787 1.00 17.48 ? 79 TYR A CE1 1 ATOM 637 C CE2 . TYR A 1 79 ? 49.165 49.269 -7.734 1.00 15.41 ? 79 TYR A CE2 1 ATOM 638 C CZ . TYR A 1 79 ? 50.245 49.676 -8.488 1.00 17.76 ? 79 TYR A CZ 1 ATOM 639 O OH . TYR A 1 79 ? 51.507 49.658 -7.941 1.00 19.67 ? 79 TYR A OH 1 ATOM 640 N N . THR A 1 80 ? 44.199 47.508 -12.307 1.00 19.70 ? 80 THR A N 1 ATOM 641 C CA . THR A 1 80 ? 42.808 47.258 -12.659 1.00 19.52 ? 80 THR A CA 1 ATOM 642 C C . THR A 1 80 ? 42.191 46.357 -11.598 1.00 20.65 ? 80 THR A C 1 ATOM 643 O O . THR A 1 80 ? 42.639 45.227 -11.405 1.00 21.92 ? 80 THR A O 1 ATOM 644 C CB . THR A 1 80 ? 42.697 46.576 -14.033 1.00 14.95 ? 80 THR A CB 1 ATOM 645 O OG1 . THR A 1 80 ? 43.289 47.414 -15.032 1.00 11.47 ? 80 THR A OG1 1 ATOM 646 C CG2 . THR A 1 80 ? 41.236 46.321 -14.386 1.00 11.04 ? 80 THR A CG2 1 ATOM 647 N N . PRO A 1 81 ? 41.161 46.857 -10.899 1.00 18.35 ? 81 PRO A N 1 ATOM 648 C CA . PRO A 1 81 ? 40.556 46.096 -9.801 1.00 18.07 ? 81 PRO A CA 1 ATOM 649 C C . PRO A 1 81 ? 39.499 45.106 -10.279 1.00 15.55 ? 81 PRO A C 1 ATOM 650 O O . PRO A 1 81 ? 39.071 45.159 -11.431 1.00 17.06 ? 81 PRO A O 1 ATOM 651 C CB . PRO A 1 81 ? 39.892 47.184 -8.957 1.00 18.90 ? 81 PRO A CB 1 ATOM 652 C CG . PRO A 1 81 ? 39.525 48.237 -9.951 1.00 16.09 ? 81 PRO A CG 1 ATOM 653 C CD . PRO A 1 81 ? 40.582 48.205 -11.026 1.00 14.38 ? 81 PRO A CD 1 ATOM 654 N N . ILE A 1 82 ? 39.087 44.212 -9.385 1.00 13.30 ? 82 ILE A N 1 ATOM 655 C CA . ILE A 1 82 ? 38.043 43.241 -9.689 1.00 17.57 ? 82 ILE A CA 1 ATOM 656 C C . ILE A 1 82 ? 36.673 43.907 -9.809 1.00 19.63 ? 82 ILE A C 1 ATOM 657 O O . ILE A 1 82 ? 36.386 44.896 -9.134 1.00 17.77 ? 82 ILE A O 1 ATOM 658 C CB . ILE A 1 82 ? 38.011 42.117 -8.620 1.00 10.91 ? 82 ILE A CB 1 ATOM 659 C CG1 . ILE A 1 82 ? 37.283 40.882 -9.153 1.00 9.80 ? 82 ILE A CG1 1 ATOM 660 C CG2 . ILE A 1 82 ? 37.368 42.603 -7.327 1.00 11.08 ? 82 ILE A CG2 1 ATOM 661 C CD1 . ILE A 1 82 ? 37.518 39.636 -8.324 1.00 7.89 ? 82 ILE A CD1 1 ATOM 662 N N . THR A 1 83 ? 35.839 43.371 -10.693 1.00 19.51 ? 83 THR A N 1 ATOM 663 C CA . THR A 1 83 ? 34.454 43.803 -10.792 1.00 19.61 ? 83 THR A CA 1 ATOM 664 C C . THR A 1 83 ? 33.618 42.910 -9.887 1.00 19.33 ? 83 THR A C 1 ATOM 665 O O . THR A 1 83 ? 33.694 41.684 -9.979 1.00 18.20 ? 83 THR A O 1 ATOM 666 C CB . THR A 1 83 ? 33.939 43.702 -12.238 1.00 19.20 ? 83 THR A CB 1 ATOM 667 O OG1 . THR A 1 83 ? 34.688 44.589 -13.078 1.00 22.20 ? 83 THR A OG1 1 ATOM 668 C CG2 . THR A 1 83 ? 32.464 44.072 -12.306 1.00 19.29 ? 83 THR A CG2 1 ATOM 669 N N . ASN A 1 84 ? 32.828 43.521 -9.009 1.00 21.92 ? 84 ASN A N 1 ATOM 670 C CA . ASN A 1 84 ? 31.974 42.758 -8.108 1.00 20.84 ? 84 ASN A CA 1 ATOM 671 C C . ASN A 1 84 ? 30.899 41.979 -8.855 1.00 20.25 ? 84 ASN A C 1 ATOM 672 O O . ASN A 1 84 ? 30.221 42.516 -9.732 1.00 19.45 ? 84 ASN A O 1 ATOM 673 C CB . ASN A 1 84 ? 31.291 43.685 -7.104 1.00 22.07 ? 84 ASN A CB 1 ATOM 674 C CG . ASN A 1 84 ? 32.273 44.359 -6.168 1.00 23.43 ? 84 ASN A CG 1 ATOM 675 O OD1 . ASN A 1 84 ? 33.209 43.732 -5.673 1.00 26.68 ? 84 ASN A OD1 1 ATOM 676 N ND2 . ASN A 1 84 ? 32.055 45.642 -5.908 1.00 23.69 ? 84 ASN A ND2 1 ATOM 677 N N . VAL A 1 85 ? 30.750 40.708 -8.501 1.00 17.17 ? 85 VAL A N 1 ATOM 678 C CA . VAL A 1 85 ? 29.670 39.889 -9.027 1.00 19.80 ? 85 VAL A CA 1 ATOM 679 C C . VAL A 1 85 ? 28.838 39.408 -7.849 1.00 17.42 ? 85 VAL A C 1 ATOM 680 O O . VAL A 1 85 ? 29.306 38.594 -7.053 1.00 19.45 ? 85 VAL A O 1 ATOM 681 C CB . VAL A 1 85 ? 30.223 38.673 -9.792 1.00 22.78 ? 85 VAL A CB 1 ATOM 682 C CG1 . VAL A 1 85 ? 29.084 37.784 -10.275 1.00 6.30 ? 85 VAL A CG1 1 ATOM 683 C CG2 . VAL A 1 85 ? 31.085 39.126 -10.960 1.00 6.29 ? 85 VAL A CG2 1 ATOM 684 N N . PRO A 1 86 ? 27.601 39.913 -7.725 1.00 15.62 ? 86 PRO A N 1 ATOM 685 C CA . PRO A 1 86 ? 26.809 39.569 -6.540 1.00 13.06 ? 86 PRO A CA 1 ATOM 686 C C . PRO A 1 86 ? 26.317 38.127 -6.600 1.00 14.33 ? 86 PRO A C 1 ATOM 687 O O . PRO A 1 86 ? 26.143 37.587 -7.692 1.00 13.68 ? 86 PRO A O 1 ATOM 688 C CB . PRO A 1 86 ? 25.628 40.540 -6.625 1.00 13.73 ? 86 PRO A CB 1 ATOM 689 C CG . PRO A 1 86 ? 25.484 40.825 -8.084 1.00 11.29 ? 86 PRO A CG 1 ATOM 690 C CD . PRO A 1 86 ? 26.885 40.830 -8.630 1.00 13.28 ? 86 PRO A CD 1 ATOM 691 N N . PRO A 1 87 ? 26.103 37.505 -5.431 1.00 16.28 ? 87 PRO A N 1 ATOM 692 C CA . PRO A 1 87 ? 25.699 36.098 -5.345 1.00 15.48 ? 87 PRO A CA 1 ATOM 693 C C . PRO A 1 87 ? 24.226 35.815 -5.633 1.00 15.74 ? 87 PRO A C 1 ATOM 694 O O . PRO A 1 87 ? 23.365 36.680 -5.472 1.00 18.98 ? 87 PRO A O 1 ATOM 695 C CB . PRO A 1 87 ? 25.984 35.758 -3.882 1.00 15.75 ? 87 PRO A CB 1 ATOM 696 C CG . PRO A 1 87 ? 25.788 37.041 -3.162 1.00 16.96 ? 87 PRO A CG 1 ATOM 697 C CD . PRO A 1 87 ? 26.292 38.107 -4.098 1.00 14.58 ? 87 PRO A CD 1 ATOM 698 N N . GLU A 1 88 ? 23.963 34.587 -6.066 1.00 19.81 ? 88 GLU A N 1 ATOM 699 C CA . GLU A 1 88 ? 22.631 34.001 -6.021 1.00 20.28 ? 88 GLU A CA 1 ATOM 700 C C . GLU A 1 88 ? 22.555 33.237 -4.711 1.00 16.55 ? 88 GLU A C 1 ATOM 701 O O . GLU A 1 88 ? 23.500 32.545 -4.333 1.00 18.24 ? 88 GLU A O 1 ATOM 702 C CB . GLU A 1 88 ? 22.418 33.026 -7.176 1.00 25.22 ? 88 GLU A CB 1 ATOM 703 C CG . GLU A 1 88 ? 22.513 33.629 -8.563 1.00 34.43 ? 88 GLU A CG 1 ATOM 704 C CD . GLU A 1 88 ? 22.264 32.597 -9.647 1.00 40.05 ? 88 GLU A CD 1 ATOM 705 O OE1 . GLU A 1 88 ? 22.074 31.411 -9.305 1.00 43.59 ? 88 GLU A OE1 1 ATOM 706 O OE2 . GLU A 1 88 ? 22.248 32.969 -10.838 1.00 39.71 ? 88 GLU A OE2 1 ATOM 707 N N . VAL A 1 89 ? 21.433 33.363 -4.016 1.00 14.19 ? 89 VAL A N 1 ATOM 708 C CA . VAL A 1 89 ? 21.282 32.740 -2.710 1.00 14.32 ? 89 VAL A CA 1 ATOM 709 C C . VAL A 1 89 ? 20.060 31.840 -2.738 1.00 19.48 ? 89 VAL A C 1 ATOM 710 O O . VAL A 1 89 ? 19.003 32.215 -3.239 1.00 23.23 ? 89 VAL A O 1 ATOM 711 C CB . VAL A 1 89 ? 21.138 33.789 -1.590 1.00 11.66 ? 89 VAL A CB 1 ATOM 712 C CG1 . VAL A 1 89 ? 20.999 33.111 -0.238 1.00 13.78 ? 89 VAL A CG1 1 ATOM 713 C CG2 . VAL A 1 89 ? 22.330 34.730 -1.588 1.00 9.74 ? 89 VAL A CG2 1 ATOM 714 N N . THR A 1 90 ? 20.226 30.631 -2.218 1.00 17.92 ? 90 THR A N 1 ATOM 715 C CA . THR A 1 90 ? 19.124 29.692 -2.112 1.00 18.44 ? 90 THR A CA 1 ATOM 716 C C . THR A 1 90 ? 19.072 29.084 -0.723 1.00 18.71 ? 90 THR A C 1 ATOM 717 O O . THR A 1 90 ? 20.105 28.729 -0.153 1.00 19.54 ? 90 THR A O 1 ATOM 718 C CB . THR A 1 90 ? 19.220 28.567 -3.167 1.00 19.61 ? 90 THR A CB 1 ATOM 719 O OG1 . THR A 1 90 ? 19.658 29.112 -4.417 1.00 22.58 ? 90 THR A OG1 1 ATOM 720 C CG2 . THR A 1 90 ? 17.878 27.883 -3.358 1.00 18.89 ? 90 THR A CG2 1 ATOM 721 N N . VAL A 1 91 ? 17.867 28.960 -0.179 1.00 16.31 ? 91 VAL A N 1 ATOM 722 C CA . VAL A 1 91 ? 17.704 28.308 1.108 1.00 16.66 ? 91 VAL A CA 1 ATOM 723 C C . VAL A 1 91 ? 16.858 27.056 0.943 1.00 18.92 ? 91 VAL A C 1 ATOM 724 O O . VAL A 1 91 ? 15.779 27.089 0.350 1.00 21.84 ? 91 VAL A O 1 ATOM 725 C CB . VAL A 1 91 ? 17.058 29.245 2.149 1.00 16.02 ? 91 VAL A CB 1 ATOM 726 C CG1 . VAL A 1 91 ? 16.692 28.480 3.413 1.00 16.45 ? 91 VAL A CG1 1 ATOM 727 C CG2 . VAL A 1 91 ? 17.989 30.402 2.471 1.00 12.23 ? 91 VAL A CG2 1 ATOM 728 N N . LEU A 1 92 ? 17.360 25.952 1.481 1.00 19.32 ? 92 LEU A N 1 ATOM 729 C CA . LEU A 1 92 ? 16.661 24.678 1.431 1.00 21.38 ? 92 LEU A CA 1 ATOM 730 C C . LEU A 1 92 ? 16.961 23.848 2.669 1.00 20.13 ? 92 LEU A C 1 ATOM 731 O O . LEU A 1 92 ? 17.868 24.168 3.437 1.00 20.73 ? 92 LEU A O 1 ATOM 732 C CB . LEU A 1 92 ? 17.052 23.897 0.171 1.00 24.10 ? 92 LEU A CB 1 ATOM 733 C CG . LEU A 1 92 ? 18.512 23.449 0.021 1.00 29.70 ? 92 LEU A CG 1 ATOM 734 C CD1 . LEU A 1 92 ? 18.603 22.269 -0.933 1.00 33.85 ? 92 LEU A CD1 1 ATOM 735 C CD2 . LEU A 1 92 ? 19.415 24.582 -0.463 1.00 27.87 ? 92 LEU A CD2 1 ATOM 736 N N . THR A 1 93 ? 16.194 22.780 2.859 1.00 19.44 ? 93 THR A N 1 ATOM 737 C CA . THR A 1 93 ? 16.467 21.832 3.928 1.00 22.89 ? 93 THR A CA 1 ATOM 738 C C . THR A 1 93 ? 17.163 20.625 3.302 1.00 26.08 ? 93 THR A C 1 ATOM 739 O O . THR A 1 93 ? 16.995 20.368 2.109 1.00 26.56 ? 93 THR A O 1 ATOM 740 C CB . THR A 1 93 ? 15.191 21.398 4.666 1.00 21.67 ? 93 THR A CB 1 ATOM 741 O OG1 . THR A 1 93 ? 14.301 20.753 3.747 1.00 24.54 ? 93 THR A OG1 1 ATOM 742 C CG2 . THR A 1 93 ? 14.499 22.610 5.273 1.00 21.84 ? 93 THR A CG2 1 ATOM 743 N N . ASN A 1 94 ? 17.937 19.885 4.090 1.00 28.29 ? 94 ASN A N 1 ATOM 744 C CA . ASN A 1 94 ? 18.654 18.723 3.559 1.00 29.78 ? 94 ASN A CA 1 ATOM 745 C C . ASN A 1 94 ? 17.822 17.444 3.478 1.00 26.72 ? 94 ASN A C 1 ATOM 746 O O . ASN A 1 94 ? 18.249 16.452 2.887 1.00 26.54 ? 94 ASN A O 1 ATOM 747 C CB . ASN A 1 94 ? 19.972 18.485 4.306 1.00 38.22 ? 94 ASN A CB 1 ATOM 748 C CG . ASN A 1 94 ? 19.768 17.935 5.703 1.00 45.45 ? 94 ASN A CG 1 ATOM 749 O OD1 . ASN A 1 94 ? 18.706 18.099 6.301 1.00 48.98 ? 94 ASN A OD1 1 ATOM 750 N ND2 . ASN A 1 94 ? 20.792 17.275 6.231 1.00 47.91 ? 94 ASN A ND2 1 ATOM 751 N N . SER A 1 95 ? 16.635 17.479 4.071 1.00 27.01 ? 95 SER A N 1 ATOM 752 C CA . SER A 1 95 ? 15.685 16.379 3.965 1.00 31.74 ? 95 SER A CA 1 ATOM 753 C C . SER A 1 95 ? 14.264 16.932 4.041 1.00 29.41 ? 95 SER A C 1 ATOM 754 O O . SER A 1 95 ? 14.073 18.074 4.463 1.00 25.62 ? 95 SER A O 1 ATOM 755 C CB . SER A 1 95 ? 15.933 15.358 5.079 1.00 36.02 ? 95 SER A CB 1 ATOM 756 O OG . SER A 1 95 ? 15.745 15.943 6.355 1.00 40.60 ? 95 SER A OG 1 ATOM 757 N N . PRO A 1 96 ? 13.264 16.140 3.611 1.00 31.17 ? 96 PRO A N 1 ATOM 758 C CA . PRO A 1 96 ? 11.873 16.591 3.736 1.00 29.76 ? 96 PRO A CA 1 ATOM 759 C C . PRO A 1 96 ? 11.528 16.978 5.170 1.00 29.71 ? 96 PRO A C 1 ATOM 760 O O . PRO A 1 96 ? 11.948 16.307 6.114 1.00 29.45 ? 96 PRO A O 1 ATOM 761 C CB . PRO A 1 96 ? 11.065 15.351 3.322 1.00 26.48 ? 96 PRO A CB 1 ATOM 762 C CG . PRO A 1 96 ? 12.061 14.221 3.206 1.00 31.15 ? 96 PRO A CG 1 ATOM 763 C CD . PRO A 1 96 ? 13.358 14.867 2.882 1.00 28.21 ? 96 PRO A CD 1 ATOM 764 N N . VAL A 1 97 ? 10.767 18.058 5.320 1.00 29.83 ? 97 VAL A N 1 ATOM 765 C CA . VAL A 1 97 ? 10.475 18.625 6.633 1.00 30.40 ? 97 VAL A CA 1 ATOM 766 C C . VAL A 1 97 ? 9.268 17.973 7.303 1.00 31.73 ? 97 VAL A C 1 ATOM 767 O O . VAL A 1 97 ? 8.204 17.840 6.699 1.00 32.28 ? 97 VAL A O 1 ATOM 768 C CB . VAL A 1 97 ? 10.255 20.147 6.549 1.00 28.92 ? 97 VAL A CB 1 ATOM 769 C CG1 . VAL A 1 97 ? 9.922 20.711 7.920 1.00 28.71 ? 97 VAL A CG1 1 ATOM 770 C CG2 . VAL A 1 97 ? 11.488 20.824 5.983 1.00 27.25 ? 97 VAL A CG2 1 ATOM 771 N N . GLU A 1 98 ? 9.453 17.553 8.549 1.00 31.01 ? 98 GLU A N 1 ATOM 772 C CA . GLU A 1 98 ? 8.371 17.068 9.394 1.00 37.68 ? 98 GLU A CA 1 ATOM 773 C C . GLU A 1 98 ? 8.426 17.837 10.723 1.00 38.75 ? 98 GLU A C 1 ATOM 774 O O . GLU A 1 98 ? 9.508 18.075 11.249 1.00 36.34 ? 98 GLU A O 1 ATOM 775 C CB . GLU A 1 98 ? 8.520 15.563 9.633 1.00 46.04 ? 98 GLU A CB 1 ATOM 776 C CG . GLU A 1 98 ? 8.477 14.736 8.339 1.00 53.14 ? 98 GLU A CG 1 ATOM 777 C CD . GLU A 1 98 ? 8.759 13.257 8.549 1.00 62.87 ? 98 GLU A CD 1 ATOM 778 O OE1 . GLU A 1 98 ? 7.944 12.430 8.088 1.00 66.89 ? 98 GLU A OE1 1 ATOM 779 O OE2 . GLU A 1 98 ? 9.789 12.921 9.171 1.00 65.29 ? 98 GLU A OE2 1 ATOM 780 N N . LEU A 1 99 ? 7.267 18.224 11.252 1.00 39.07 ? 99 LEU A N 1 ATOM 781 C CA . LEU A 1 99 ? 7.166 18.988 12.497 1.00 41.92 ? 99 LEU A CA 1 ATOM 782 C C . LEU A 1 99 ? 7.918 18.284 13.623 1.00 44.60 ? 99 LEU A C 1 ATOM 783 O O . LEU A 1 99 ? 7.831 17.065 13.739 1.00 45.71 ? 99 LEU A O 1 ATOM 784 C CB . LEU A 1 99 ? 5.698 19.221 12.864 1.00 45.09 ? 99 LEU A CB 1 ATOM 785 C CG . LEU A 1 99 ? 4.897 20.206 12.014 1.00 45.31 ? 99 LEU A CG 1 ATOM 786 C CD1 . LEU A 1 99 ? 3.461 20.325 12.502 1.00 46.32 ? 99 LEU A CD1 1 ATOM 787 C CD2 . LEU A 1 99 ? 5.572 21.558 12.025 1.00 45.17 ? 99 LEU A CD2 1 ATOM 788 N N . ARG A 1 100 ? 8.702 19.028 14.411 1.00 45.73 ? 100 ARG A N 1 ATOM 789 C CA . ARG A 1 100 ? 9.524 18.440 15.502 1.00 48.13 ? 100 ARG A CA 1 ATOM 790 C C . ARG A 1 100 ? 10.379 17.194 15.186 1.00 44.98 ? 100 ARG A C 1 ATOM 791 O O . ARG A 1 100 ? 10.632 16.328 16.033 1.00 47.32 ? 100 ARG A O 1 ATOM 792 C CB . ARG A 1 100 ? 8.658 18.276 16.756 1.00 56.13 ? 100 ARG A CB 1 ATOM 793 C CG . ARG A 1 100 ? 7.634 17.195 16.727 1.00 62.87 ? 100 ARG A CG 1 ATOM 794 C CD . ARG A 1 100 ? 6.698 17.545 17.857 1.00 68.18 ? 100 ARG A CD 1 ATOM 795 N NE . ARG A 1 100 ? 5.881 18.733 17.535 1.00 69.98 ? 100 ARG A NE 1 ATOM 796 C CZ . ARG A 1 100 ? 4.712 18.787 16.883 1.00 71.17 ? 100 ARG A CZ 1 ATOM 797 N NH1 . ARG A 1 100 ? 4.145 17.680 16.410 1.00 71.88 ? 100 ARG A NH1 1 ATOM 798 N NH2 . ARG A 1 100 ? 4.119 19.982 16.679 1.00 70.25 ? 100 ARG A NH2 1 ATOM 799 N N . GLU A 1 101 ? 10.783 17.114 13.921 1.00 42.50 ? 101 GLU A N 1 ATOM 800 C CA . GLU A 1 101 ? 11.801 16.160 13.524 1.00 40.62 ? 101 GLU A CA 1 ATOM 801 C C . GLU A 1 101 ? 13.043 16.954 13.132 1.00 38.08 ? 101 GLU A C 1 ATOM 802 O O . GLU A 1 101 ? 12.987 17.750 12.192 1.00 32.96 ? 101 GLU A O 1 ATOM 803 C CB . GLU A 1 101 ? 11.325 15.298 12.357 1.00 42.04 ? 101 GLU A CB 1 ATOM 804 C CG . GLU A 1 101 ? 10.196 14.366 12.725 1.00 47.95 ? 101 GLU A CG 1 ATOM 805 C CD . GLU A 1 101 ? 10.622 13.380 13.795 1.00 55.56 ? 101 GLU A CD 1 ATOM 806 O OE1 . GLU A 1 101 ? 11.808 12.980 13.803 1.00 57.07 ? 101 GLU A OE1 1 ATOM 807 O OE2 . GLU A 1 101 ? 9.774 12.994 14.625 1.00 62.05 ? 101 GLU A OE2 1 ATOM 808 N N . PRO A 1 102 ? 14.154 16.757 13.863 1.00 38.03 ? 102 PRO A N 1 ATOM 809 C CA . PRO A 1 102 ? 15.391 17.518 13.648 1.00 36.47 ? 102 PRO A CA 1 ATOM 810 C C . PRO A 1 102 ? 15.795 17.575 12.176 1.00 32.71 ? 102 PRO A C 1 ATOM 811 O O . PRO A 1 102 ? 15.810 16.546 11.503 1.00 30.58 ? 102 PRO A O 1 ATOM 812 C CB . PRO A 1 102 ? 16.424 16.737 14.462 1.00 37.78 ? 102 PRO A CB 1 ATOM 813 C CG . PRO A 1 102 ? 15.627 16.144 15.568 1.00 38.22 ? 102 PRO A CG 1 ATOM 814 C CD . PRO A 1 102 ? 14.287 15.796 14.972 1.00 37.72 ? 102 PRO A CD 1 ATOM 815 N N . ASN A 1 103 ? 16.125 18.768 11.696 1.00 26.43 ? 103 ASN A N 1 ATOM 816 C CA . ASN A 1 103 ? 16.493 18.969 10.302 1.00 23.69 ? 103 ASN A CA 1 ATOM 817 C C . ASN A 1 103 ? 17.617 19.990 10.221 1.00 25.24 ? 103 ASN A C 1 ATOM 818 O O . ASN A 1 103 ? 18.095 20.476 11.246 1.00 28.69 ? 103 ASN A O 1 ATOM 819 C CB . ASN A 1 103 ? 15.275 19.446 9.508 1.00 24.65 ? 103 ASN A CB 1 ATOM 820 C CG . ASN A 1 103 ? 15.341 19.062 8.040 1.00 25.12 ? 103 ASN A CG 1 ATOM 821 O OD1 . ASN A 1 103 ? 16.365 19.243 7.384 1.00 25.12 ? 103 ASN A OD1 1 ATOM 822 N ND2 . ASN A 1 103 ? 14.244 18.522 7.519 1.00 23.55 ? 103 ASN A ND2 1 ATOM 823 N N . VAL A 1 104 ? 18.046 20.314 9.006 1.00 23.48 ? 104 VAL A N 1 ATOM 824 C CA . VAL A 1 104 ? 19.095 21.306 8.819 1.00 24.61 ? 104 VAL A CA 1 ATOM 825 C C . VAL A 1 104 ? 18.728 22.248 7.684 1.00 25.09 ? 104 VAL A C 1 ATOM 826 O O . VAL A 1 104 ? 18.411 21.812 6.578 1.00 24.65 ? 104 VAL A O 1 ATOM 827 C CB . VAL A 1 104 ? 20.464 20.660 8.498 1.00 30.40 ? 104 VAL A CB 1 ATOM 828 C CG1 . VAL A 1 104 ? 21.528 21.734 8.306 1.00 18.50 ? 104 VAL A CG1 1 ATOM 829 C CG2 . VAL A 1 104 ? 20.877 19.676 9.589 1.00 19.62 ? 104 VAL A CG2 1 ATOM 830 N N . LEU A 1 105 ? 18.778 23.545 7.966 1.00 23.49 ? 105 LEU A N 1 ATOM 831 C CA . LEU A 1 105 ? 18.634 24.543 6.921 1.00 21.51 ? 105 LEU A CA 1 ATOM 832 C C . LEU A 1 105 ? 19.970 24.781 6.241 1.00 21.40 ? 105 LEU A C 1 ATOM 833 O O . LEU A 1 105 ? 21.000 24.910 6.901 1.00 17.41 ? 105 LEU A O 1 ATOM 834 C CB . LEU A 1 105 ? 18.103 25.852 7.504 1.00 24.03 ? 105 LEU A CB 1 ATOM 835 C CG . LEU A 1 105 ? 16.601 25.920 7.787 1.00 25.69 ? 105 LEU A CG 1 ATOM 836 C CD1 . LEU A 1 105 ? 16.284 27.114 8.669 1.00 23.96 ? 105 LEU A CD1 1 ATOM 837 C CD2 . LEU A 1 105 ? 15.808 25.981 6.494 1.00 23.63 ? 105 LEU A CD2 1 ATOM 838 N N . ILE A 1 106 ? 19.946 24.841 4.915 1.00 16.43 ? 106 ILE A N 1 ATOM 839 C CA . ILE A 1 106 ? 21.147 25.122 4.150 1.00 17.23 ? 106 ILE A CA 1 ATOM 840 C C . ILE A 1 106 ? 21.001 26.438 3.402 1.00 18.14 ? 106 ILE A C 1 ATOM 841 O O . ILE A 1 106 ? 20.014 26.655 2.700 1.00 21.03 ? 106 ILE A O 1 ATOM 842 C CB . ILE A 1 106 ? 21.410 24.020 3.113 1.00 17.97 ? 106 ILE A CB 1 ATOM 843 C CG1 . ILE A 1 106 ? 21.416 22.646 3.785 1.00 20.52 ? 106 ILE A CG1 1 ATOM 844 C CG2 . ILE A 1 106 ? 22.726 24.271 2.390 1.00 19.77 ? 106 ILE A CG2 1 ATOM 845 C CD1 . ILE A 1 106 ? 21.454 21.495 2.808 1.00 20.59 ? 106 ILE A CD1 1 ATOM 846 N N . CYS A 1 107 ? 21.985 27.316 3.557 1.00 18.39 ? 107 CYS A N 1 ATOM 847 C CA . CYS A 1 107 ? 22.037 28.538 2.771 1.00 16.80 ? 107 CYS A CA 1 ATOM 848 C C . CYS A 1 107 ? 23.144 28.389 1.743 1.00 16.60 ? 107 CYS A C 1 ATOM 849 O O . CYS A 1 107 ? 24.322 28.301 2.090 1.00 14.72 ? 107 CYS A O 1 ATOM 850 C CB . CYS A 1 107 ? 22.317 29.747 3.660 1.00 15.58 ? 107 CYS A CB 1 ATOM 851 S SG . CYS A 1 107 ? 22.258 31.318 2.771 1.00 16.11 ? 107 CYS A SG 1 ATOM 852 N N . PHE A 1 108 ? 22.762 28.360 0.474 1.00 14.14 ? 108 PHE A N 1 ATOM 853 C CA . PHE A 1 108 ? 23.731 28.188 -0.590 1.00 15.24 ? 108 PHE A CA 1 ATOM 854 C C . PHE A 1 108 ? 23.993 29.532 -1.244 1.00 17.54 ? 108 PHE A C 1 ATOM 855 O O . PHE A 1 108 ? 23.088 30.154 -1.799 1.00 17.13 ? 108 PHE A O 1 ATOM 856 C CB . PHE A 1 108 ? 23.216 27.178 -1.620 1.00 15.78 ? 108 PHE A CB 1 ATOM 857 C CG . PHE A 1 108 ? 24.172 26.913 -2.747 1.00 17.58 ? 108 PHE A CG 1 ATOM 858 C CD1 . PHE A 1 108 ? 25.522 26.718 -2.503 1.00 18.03 ? 108 PHE A CD1 1 ATOM 859 C CD2 . PHE A 1 108 ? 23.713 26.829 -4.051 1.00 13.85 ? 108 PHE A CD2 1 ATOM 860 C CE1 . PHE A 1 108 ? 26.399 26.465 -3.542 1.00 18.50 ? 108 PHE A CE1 1 ATOM 861 C CE2 . PHE A 1 108 ? 24.583 26.574 -5.093 1.00 15.56 ? 108 PHE A CE2 1 ATOM 862 C CZ . PHE A 1 108 ? 25.929 26.391 -4.839 1.00 17.81 ? 108 PHE A CZ 1 ATOM 863 N N . ILE A 1 109 ? 25.245 29.970 -1.178 1.00 18.46 ? 109 ILE A N 1 ATOM 864 C CA . ILE A 1 109 ? 25.634 31.259 -1.722 1.00 18.52 ? 109 ILE A CA 1 ATOM 865 C C . ILE A 1 109 ? 26.532 30.961 -2.903 1.00 17.23 ? 109 ILE A C 1 ATOM 866 O O . ILE A 1 109 ? 27.571 30.328 -2.751 1.00 19.98 ? 109 ILE A O 1 ATOM 867 C CB . ILE A 1 109 ? 26.399 32.088 -0.671 1.00 18.88 ? 109 ILE A CB 1 ATOM 868 C CG1 . ILE A 1 109 ? 25.592 32.203 0.627 1.00 21.39 ? 109 ILE A CG1 1 ATOM 869 C CG2 . ILE A 1 109 ? 26.740 33.466 -1.217 1.00 16.68 ? 109 ILE A CG2 1 ATOM 870 C CD1 . ILE A 1 109 ? 25.995 31.206 1.697 1.00 22.57 ? 109 ILE A CD1 1 ATOM 871 N N . ASP A 1 110 ? 26.125 31.415 -4.082 1.00 12.43 ? 110 ASP A N 1 ATOM 872 C CA . ASP A 1 110 ? 26.709 30.909 -5.314 1.00 13.50 ? 110 ASP A CA 1 ATOM 873 C C . ASP A 1 110 ? 27.015 31.979 -6.347 1.00 17.02 ? 110 ASP A C 1 ATOM 874 O O . ASP A 1 110 ? 26.396 33.044 -6.362 1.00 15.77 ? 110 ASP A O 1 ATOM 875 C CB . ASP A 1 110 ? 25.749 29.888 -5.931 1.00 15.64 ? 110 ASP A CB 1 ATOM 876 C CG . ASP A 1 110 ? 26.413 29.023 -6.983 1.00 21.04 ? 110 ASP A CG 1 ATOM 877 O OD1 . ASP A 1 110 ? 27.661 28.965 -7.008 1.00 21.48 ? 110 ASP A OD1 1 ATOM 878 O OD2 . ASP A 1 110 ? 25.688 28.411 -7.793 1.00 26.25 ? 110 ASP A OD2 1 ATOM 879 N N . LYS A 1 111 ? 27.988 31.680 -7.204 1.00 20.13 ? 111 LYS A N 1 ATOM 880 C CA . LYS A 1 111 ? 28.262 32.484 -8.387 1.00 19.65 ? 111 LYS A CA 1 ATOM 881 C C . LYS A 1 111 ? 28.638 33.934 -8.080 1.00 18.26 ? 111 LYS A C 1 ATOM 882 O O . LYS A 1 111 ? 28.099 34.865 -8.681 1.00 21.35 ? 111 LYS A O 1 ATOM 883 C CB . LYS A 1 111 ? 27.057 32.403 -9.329 1.00 20.56 ? 111 LYS A CB 1 ATOM 884 C CG . LYS A 1 111 ? 27.334 32.485 -10.809 1.00 29.57 ? 111 LYS A CG 1 ATOM 885 C CD . LYS A 1 111 ? 26.074 32.052 -11.542 1.00 33.41 ? 111 LYS A CD 1 ATOM 886 C CE . LYS A 1 111 ? 25.590 30.711 -10.986 1.00 34.59 ? 111 LYS A CE 1 ATOM 887 N NZ . LYS A 1 111 ? 24.353 30.199 -11.634 1.00 34.49 ? 111 LYS A NZ 1 ATOM 888 N N . PHE A 1 112 ? 29.565 34.122 -7.144 1.00 11.84 ? 112 PHE A N 1 ATOM 889 C CA . PHE A 1 112 ? 29.973 35.465 -6.741 1.00 12.86 ? 112 PHE A CA 1 ATOM 890 C C . PHE A 1 112 ? 31.488 35.653 -6.664 1.00 18.80 ? 112 PHE A C 1 ATOM 891 O O . PHE A 1 112 ? 32.246 34.685 -6.562 1.00 16.51 ? 112 PHE A O 1 ATOM 892 C CB . PHE A 1 112 ? 29.340 35.845 -5.396 1.00 13.42 ? 112 PHE A CB 1 ATOM 893 C CG . PHE A 1 112 ? 29.853 35.045 -4.232 1.00 14.75 ? 112 PHE A CG 1 ATOM 894 C CD1 . PHE A 1 112 ? 29.366 33.774 -3.973 1.00 12.50 ? 112 PHE A CD1 1 ATOM 895 C CD2 . PHE A 1 112 ? 30.823 35.570 -3.390 1.00 15.71 ? 112 PHE A CD2 1 ATOM 896 C CE1 . PHE A 1 112 ? 29.841 33.039 -2.900 1.00 12.77 ? 112 PHE A CE1 1 ATOM 897 C CE2 . PHE A 1 112 ? 31.302 34.840 -2.317 1.00 18.39 ? 112 PHE A CE2 1 ATOM 898 C CZ . PHE A 1 112 ? 30.808 33.572 -2.072 1.00 19.44 ? 112 PHE A CZ 1 ATOM 899 N N . THR A 1 113 ? 31.909 36.915 -6.707 1.00 20.32 ? 113 THR A N 1 ATOM 900 C CA . THR A 1 113 ? 33.295 37.302 -6.466 1.00 18.98 ? 113 THR A CA 1 ATOM 901 C C . THR A 1 113 ? 33.321 38.807 -6.176 1.00 18.60 ? 113 THR A C 1 ATOM 902 O O . THR A 1 113 ? 32.459 39.541 -6.661 1.00 19.17 ? 113 THR A O 1 ATOM 903 C CB . THR A 1 113 ? 34.216 36.939 -7.663 1.00 24.10 ? 113 THR A CB 1 ATOM 904 O OG1 . THR A 1 113 ? 35.581 36.858 -7.230 1.00 11.90 ? 113 THR A OG1 1 ATOM 905 C CG2 . THR A 1 113 ? 34.098 37.967 -8.780 1.00 11.73 ? 113 THR A CG2 1 ATOM 906 N N . PRO A 1 114 ? 34.285 39.279 -5.363 1.00 18.42 ? 114 PRO A N 1 ATOM 907 C CA . PRO A 1 114 ? 35.383 38.589 -4.671 1.00 17.72 ? 114 PRO A CA 1 ATOM 908 C C . PRO A 1 114 ? 34.882 37.679 -3.545 1.00 17.17 ? 114 PRO A C 1 ATOM 909 O O . PRO A 1 114 ? 33.724 37.790 -3.147 1.00 17.64 ? 114 PRO A O 1 ATOM 910 C CB . PRO A 1 114 ? 36.210 39.749 -4.094 1.00 18.51 ? 114 PRO A CB 1 ATOM 911 C CG . PRO A 1 114 ? 35.254 40.871 -3.962 1.00 17.24 ? 114 PRO A CG 1 ATOM 912 C CD . PRO A 1 114 ? 34.302 40.730 -5.107 1.00 13.31 ? 114 PRO A CD 1 ATOM 913 N N . PRO A 1 115 ? 35.745 36.777 -3.047 1.00 20.46 ? 115 PRO A N 1 ATOM 914 C CA . PRO A 1 115 ? 35.353 35.853 -1.976 1.00 19.10 ? 115 PRO A CA 1 ATOM 915 C C . PRO A 1 115 ? 35.300 36.514 -0.599 1.00 20.51 ? 115 PRO A C 1 ATOM 916 O O . PRO A 1 115 ? 36.109 36.200 0.274 1.00 23.28 ? 115 PRO A O 1 ATOM 917 C CB . PRO A 1 115 ? 36.452 34.789 -2.025 1.00 18.79 ? 115 PRO A CB 1 ATOM 918 C CG . PRO A 1 115 ? 37.644 35.520 -2.540 1.00 17.92 ? 115 PRO A CG 1 ATOM 919 C CD . PRO A 1 115 ? 37.104 36.493 -3.546 1.00 16.24 ? 115 PRO A CD 1 ATOM 920 N N . VAL A 1 116 ? 34.349 37.427 -0.421 1.00 22.25 ? 116 VAL A N 1 ATOM 921 C CA . VAL A 1 116 ? 34.084 38.059 0.870 1.00 20.68 ? 116 VAL A CA 1 ATOM 922 C C . VAL A 1 116 ? 32.587 38.260 1.041 1.00 20.32 ? 116 VAL A C 1 ATOM 923 O O . VAL A 1 116 ? 31.945 38.917 0.222 1.00 22.70 ? 116 VAL A O 1 ATOM 924 C CB . VAL A 1 116 ? 34.728 39.456 0.974 1.00 17.58 ? 116 VAL A CB 1 ATOM 925 C CG1 . VAL A 1 116 ? 34.430 40.072 2.330 1.00 16.16 ? 116 VAL A CG1 1 ATOM 926 C CG2 . VAL A 1 116 ? 36.220 39.389 0.738 1.00 16.04 ? 116 VAL A CG2 1 ATOM 927 N N . VAL A 1 117 ? 32.040 37.715 2.122 1.00 20.45 ? 117 VAL A N 1 ATOM 928 C CA . VAL A 1 117 ? 30.609 37.809 2.393 1.00 20.73 ? 117 VAL A CA 1 ATOM 929 C C . VAL A 1 117 ? 30.334 37.849 3.888 1.00 21.68 ? 117 VAL A C 1 ATOM 930 O O . VAL A 1 117 ? 31.058 37.249 4.683 1.00 22.38 ? 117 VAL A O 1 ATOM 931 C CB . VAL A 1 117 ? 29.820 36.618 1.781 1.00 25.07 ? 117 VAL A CB 1 ATOM 932 C CG1 . VAL A 1 117 ? 29.697 36.746 0.269 1.00 25.45 ? 117 VAL A CG1 1 ATOM 933 C CG2 . VAL A 1 117 ? 30.460 35.291 2.170 1.00 15.12 ? 117 VAL A CG2 1 ATOM 934 N N . ASN A 1 118 ? 29.277 38.561 4.263 1.00 20.93 ? 118 ASN A N 1 ATOM 935 C CA . ASN A 1 118 ? 28.766 38.485 5.618 1.00 21.37 ? 118 ASN A CA 1 ATOM 936 C C . ASN A 1 118 ? 27.464 37.698 5.527 1.00 21.76 ? 118 ASN A C 1 ATOM 937 O O . ASN A 1 118 ? 26.566 38.064 4.769 1.00 21.98 ? 118 ASN A O 1 ATOM 938 C CB . ASN A 1 118 ? 28.512 39.881 6.196 1.00 26.39 ? 118 ASN A CB 1 ATOM 939 C CG . ASN A 1 118 ? 29.795 40.682 6.397 1.00 31.47 ? 118 ASN A CG 1 ATOM 940 O OD1 . ASN A 1 118 ? 30.844 40.131 6.728 1.00 28.74 ? 118 ASN A OD1 1 ATOM 941 N ND2 . ASN A 1 118 ? 29.710 41.996 6.172 1.00 41.23 ? 118 ASN A ND2 1 ATOM 942 N N . VAL A 1 119 ? 27.363 36.614 6.290 1.00 20.96 ? 119 VAL A N 1 ATOM 943 C CA . VAL A 1 119 ? 26.158 35.792 6.274 1.00 20.02 ? 119 VAL A CA 1 ATOM 944 C C . VAL A 1 119 ? 25.570 35.650 7.672 1.00 21.50 ? 119 VAL A C 1 ATOM 945 O O . VAL A 1 119 ? 26.273 35.291 8.616 1.00 25.78 ? 119 VAL A O 1 ATOM 946 C CB . VAL A 1 119 ? 26.442 34.386 5.710 1.00 22.60 ? 119 VAL A CB 1 ATOM 947 C CG1 . VAL A 1 119 ? 25.176 33.537 5.728 1.00 16.75 ? 119 VAL A CG1 1 ATOM 948 C CG2 . VAL A 1 119 ? 26.996 34.483 4.295 1.00 17.13 ? 119 VAL A CG2 1 ATOM 949 N N . THR A 1 120 ? 24.276 35.923 7.798 1.00 21.48 ? 120 THR A N 1 ATOM 950 C CA . THR A 1 120 ? 23.590 35.792 9.076 1.00 21.93 ? 120 THR A CA 1 ATOM 951 C C . THR A 1 120 ? 22.317 34.958 8.961 1.00 20.00 ? 120 THR A C 1 ATOM 952 O O . THR A 1 120 ? 21.508 35.169 8.058 1.00 18.37 ? 120 THR A O 1 ATOM 953 C CB . THR A 1 120 ? 23.202 37.174 9.638 1.00 23.48 ? 120 THR A CB 1 ATOM 954 O OG1 . THR A 1 120 ? 24.356 38.023 9.660 1.00 28.90 ? 120 THR A OG1 1 ATOM 955 C CG2 . THR A 1 120 ? 22.651 37.047 11.048 1.00 22.78 ? 120 THR A CG2 1 ATOM 956 N N . TRP A 1 121 ? 22.145 34.013 9.881 1.00 20.36 ? 121 TRP A N 1 ATOM 957 C CA . TRP A 1 121 ? 20.885 33.293 9.996 1.00 19.34 ? 121 TRP A CA 1 ATOM 958 C C . TRP A 1 121 ? 19.955 34.079 10.900 1.00 20.04 ? 121 TRP A C 1 ATOM 959 O O . TRP A 1 121 ? 20.351 34.534 11.974 1.00 20.76 ? 121 TRP A O 1 ATOM 960 C CB . TRP A 1 121 ? 21.099 31.910 10.610 1.00 19.61 ? 121 TRP A CB 1 ATOM 961 C CG . TRP A 1 121 ? 21.667 30.888 9.680 1.00 18.95 ? 121 TRP A CG 1 ATOM 962 C CD1 . TRP A 1 121 ? 22.921 30.355 9.712 1.00 24.31 ? 121 TRP A CD1 1 ATOM 963 C CD2 . TRP A 1 121 ? 20.992 30.261 8.583 1.00 18.29 ? 121 TRP A CD2 1 ATOM 964 N NE1 . TRP A 1 121 ? 23.071 29.436 8.701 1.00 23.63 ? 121 TRP A NE1 1 ATOM 965 C CE2 . TRP A 1 121 ? 21.901 29.361 7.993 1.00 24.66 ? 121 TRP A CE2 1 ATOM 966 C CE3 . TRP A 1 121 ? 19.708 30.376 8.041 1.00 18.06 ? 121 TRP A CE3 1 ATOM 967 C CZ2 . TRP A 1 121 ? 21.567 28.581 6.889 1.00 23.46 ? 121 TRP A CZ2 1 ATOM 968 C CZ3 . TRP A 1 121 ? 19.379 29.601 6.943 1.00 17.45 ? 121 TRP A CZ3 1 ATOM 969 C CH2 . TRP A 1 121 ? 20.304 28.715 6.379 1.00 22.58 ? 121 TRP A CH2 1 ATOM 970 N N . LEU A 1 122 ? 18.713 34.234 10.462 1.00 20.08 ? 122 LEU A N 1 ATOM 971 C CA . LEU A 1 122 ? 17.710 34.930 11.252 1.00 21.31 ? 122 LEU A CA 1 ATOM 972 C C . LEU A 1 122 ? 16.548 34.005 11.585 1.00 21.21 ? 122 LEU A C 1 ATOM 973 O O . LEU A 1 122 ? 16.020 33.322 10.709 1.00 20.28 ? 122 LEU A O 1 ATOM 974 C CB . LEU A 1 122 ? 17.177 36.141 10.481 1.00 21.44 ? 122 LEU A CB 1 ATOM 975 C CG . LEU A 1 122 ? 18.174 37.230 10.080 1.00 23.76 ? 122 LEU A CG 1 ATOM 976 C CD1 . LEU A 1 122 ? 17.549 38.176 9.068 1.00 23.27 ? 122 LEU A CD1 1 ATOM 977 C CD2 . LEU A 1 122 ? 18.647 37.992 11.304 1.00 25.81 ? 122 LEU A CD2 1 ATOM 978 N N . ARG A 1 123 ? 16.152 33.989 12.852 1.00 23.18 ? 123 ARG A N 1 ATOM 979 C CA . ARG A 1 123 ? 14.954 33.270 13.252 1.00 21.84 ? 123 ARG A CA 1 ATOM 980 C C . ARG A 1 123 ? 13.977 34.297 13.789 1.00 24.09 ? 123 ARG A C 1 ATOM 981 O O . ARG A 1 123 ? 14.250 34.957 14.794 1.00 23.13 ? 123 ARG A O 1 ATOM 982 C CB . ARG A 1 123 ? 15.250 32.227 14.331 1.00 30.79 ? 123 ARG A CB 1 ATOM 983 C CG . ARG A 1 123 ? 13.985 31.529 14.823 1.00 34.34 ? 123 ARG A CG 1 ATOM 984 C CD . ARG A 1 123 ? 14.218 30.649 16.042 1.00 42.04 ? 123 ARG A CD 1 ATOM 985 N NE . ARG A 1 123 ? 15.145 29.551 15.788 1.00 52.38 ? 123 ARG A NE 1 ATOM 986 C CZ . ARG A 1 123 ? 15.065 28.363 16.378 1.00 60.03 ? 123 ARG A CZ 1 ATOM 987 N NH1 . ARG A 1 123 ? 15.947 27.414 16.094 1.00 58.05 ? 123 ARG A NH1 1 ATOM 988 N NH2 . ARG A 1 123 ? 14.096 28.119 17.252 1.00 65.58 ? 123 ARG A NH2 1 ATOM 989 N N . ASN A 1 124 ? 12.837 34.420 13.117 1.00 24.58 ? 124 ASN A N 1 ATOM 990 C CA . ASN A 1 124 ? 11.850 35.442 13.437 1.00 25.40 ? 124 ASN A CA 1 ATOM 991 C C . ASN A 1 124 ? 12.462 36.843 13.463 1.00 23.29 ? 124 ASN A C 1 ATOM 992 O O . ASN A 1 124 ? 12.102 37.671 14.299 1.00 24.40 ? 124 ASN A O 1 ATOM 993 C CB . ASN A 1 124 ? 11.149 35.122 14.762 1.00 25.24 ? 124 ASN A CB 1 ATOM 994 C CG . ASN A 1 124 ? 10.483 33.760 14.754 1.00 27.28 ? 124 ASN A CG 1 ATOM 995 O OD1 . ASN A 1 124 ? 9.941 33.327 13.738 1.00 22.75 ? 124 ASN A OD1 1 ATOM 996 N ND2 . ASN A 1 124 ? 10.521 33.077 15.892 1.00 24.10 ? 124 ASN A ND2 1 ATOM 997 N N . GLY A 1 125 ? 13.386 37.099 12.539 1.00 22.04 ? 125 GLY A N 1 ATOM 998 C CA . GLY A 1 125 ? 13.998 38.411 12.420 1.00 22.72 ? 125 GLY A CA 1 ATOM 999 C C . GLY A 1 125 ? 15.160 38.663 13.365 1.00 23.25 ? 125 GLY A C 1 ATOM 1000 O O . GLY A 1 125 ? 15.711 39.763 13.395 1.00 25.56 ? 125 GLY A O 1 ATOM 1001 N N . LYS A 1 126 ? 15.543 37.646 14.131 1.00 22.96 ? 126 LYS A N 1 ATOM 1002 C CA . LYS A 1 126 ? 16.631 37.785 15.096 1.00 23.58 ? 126 LYS A CA 1 ATOM 1003 C C . LYS A 1 126 ? 17.810 36.892 14.738 1.00 29.35 ? 126 LYS A C 1 ATOM 1004 O O . LYS A 1 126 ? 17.624 35.737 14.355 1.00 27.42 ? 126 LYS A O 1 ATOM 1005 C CB . LYS A 1 126 ? 16.147 37.431 16.503 1.00 25.87 ? 126 LYS A CB 1 ATOM 1006 C CG . LYS A 1 126 ? 14.952 38.218 16.997 1.00 27.32 ? 126 LYS A CG 1 ATOM 1007 C CD . LYS A 1 126 ? 14.653 37.843 18.440 1.00 31.53 ? 126 LYS A CD 1 ATOM 1008 C CE . LYS A 1 126 ? 13.449 38.591 18.980 1.00 34.95 ? 126 LYS A CE 1 ATOM 1009 N NZ . LYS A 1 126 ? 13.215 38.271 20.416 1.00 38.92 ? 126 LYS A NZ 1 ATOM 1010 N N . PRO A 1 127 ? 19.034 37.426 14.872 1.00 29.22 ? 127 PRO A N 1 ATOM 1011 C CA . PRO A 1 127 ? 20.250 36.667 14.565 1.00 26.11 ? 127 PRO A CA 1 ATOM 1012 C C . PRO A 1 127 ? 20.403 35.448 15.467 1.00 27.66 ? 127 PRO A C 1 ATOM 1013 O O . PRO A 1 127 ? 20.222 35.543 16.682 1.00 29.23 ? 127 PRO A O 1 ATOM 1014 C CB . PRO A 1 127 ? 21.372 37.672 14.851 1.00 27.35 ? 127 PRO A CB 1 ATOM 1015 C CG . PRO A 1 127 ? 20.728 39.011 14.748 1.00 29.96 ? 127 PRO A CG 1 ATOM 1016 C CD . PRO A 1 127 ? 19.332 38.818 15.254 1.00 29.88 ? 127 PRO A CD 1 ATOM 1017 N N . VAL A 1 128 ? 20.739 34.312 14.867 1.00 28.09 ? 128 VAL A N 1 ATOM 1018 C CA . VAL A 1 128 ? 20.983 33.084 15.613 1.00 30.16 ? 128 VAL A CA 1 ATOM 1019 C C . VAL A 1 128 ? 22.334 32.492 15.233 1.00 31.26 ? 128 VAL A C 1 ATOM 1020 O O . VAL A 1 128 ? 22.729 32.527 14.068 1.00 30.52 ? 128 VAL A O 1 ATOM 1021 C CB . VAL A 1 128 ? 19.864 32.042 15.394 1.00 30.34 ? 128 VAL A CB 1 ATOM 1022 C CG1 . VAL A 1 128 ? 18.597 32.460 16.119 1.00 33.93 ? 128 VAL A CG1 1 ATOM 1023 C CG2 . VAL A 1 128 ? 19.593 31.850 13.910 1.00 25.92 ? 128 VAL A CG2 1 ATOM 1024 N N . THR A 1 129 ? 23.050 31.960 16.220 1.00 37.71 ? 129 THR A N 1 ATOM 1025 C CA . THR A 1 129 ? 24.395 31.444 15.983 1.00 39.55 ? 129 THR A CA 1 ATOM 1026 C C . THR A 1 129 ? 24.595 30.055 16.581 1.00 42.09 ? 129 THR A C 1 ATOM 1027 O O . THR A 1 129 ? 25.618 29.413 16.347 1.00 46.08 ? 129 THR A O 1 ATOM 1028 C CB . THR A 1 129 ? 25.477 32.381 16.562 1.00 38.74 ? 129 THR A CB 1 ATOM 1029 O OG1 . THR A 1 129 ? 25.357 32.428 17.989 1.00 38.78 ? 129 THR A OG1 1 ATOM 1030 C CG2 . THR A 1 129 ? 25.335 33.789 15.998 1.00 36.17 ? 129 THR A CG2 1 ATOM 1031 N N . THR A 1 130 ? 23.626 29.600 17.369 1.00 41.56 ? 130 THR A N 1 ATOM 1032 C CA . THR A 1 130 ? 23.725 28.295 18.016 1.00 42.25 ? 130 THR A CA 1 ATOM 1033 C C . THR A 1 130 ? 23.717 27.135 17.025 1.00 41.56 ? 130 THR A C 1 ATOM 1034 O O . THR A 1 130 ? 22.724 26.903 16.335 1.00 42.96 ? 130 THR A O 1 ATOM 1035 C CB . THR A 1 130 ? 22.592 28.084 19.038 1.00 42.54 ? 130 THR A CB 1 ATOM 1036 O OG1 . THR A 1 130 ? 22.718 29.039 20.099 1.00 44.12 ? 130 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 130 ? 22.654 26.677 19.619 1.00 43.52 ? 130 THR A CG2 1 ATOM 1038 N N . GLY A 1 131 ? 24.829 26.411 16.955 1.00 39.78 ? 131 GLY A N 1 ATOM 1039 C CA . GLY A 1 131 ? 24.904 25.212 16.142 1.00 36.41 ? 131 GLY A CA 1 ATOM 1040 C C . GLY A 1 131 ? 25.232 25.467 14.685 1.00 34.02 ? 131 GLY A C 1 ATOM 1041 O O . GLY A 1 131 ? 25.327 24.525 13.896 1.00 36.04 ? 131 GLY A O 1 ATOM 1042 N N . VAL A 1 132 ? 25.409 26.733 14.322 1.00 28.08 ? 132 VAL A N 1 ATOM 1043 C CA . VAL A 1 132 ? 25.690 27.070 12.932 1.00 25.68 ? 132 VAL A CA 1 ATOM 1044 C C . VAL A 1 132 ? 27.084 26.620 12.522 1.00 26.95 ? 132 VAL A C 1 ATOM 1045 O O . VAL A 1 132 ? 27.982 26.490 13.354 1.00 31.17 ? 132 VAL A O 1 ATOM 1046 C CB . VAL A 1 132 ? 25.536 28.579 12.638 1.00 24.75 ? 132 VAL A CB 1 ATOM 1047 C CG1 . VAL A 1 132 ? 24.137 29.053 13.001 1.00 21.11 ? 132 VAL A CG1 1 ATOM 1048 C CG2 . VAL A 1 132 ? 26.586 29.382 13.387 1.00 25.06 ? 132 VAL A CG2 1 ATOM 1049 N N . SER A 1 133 ? 27.249 26.381 11.229 1.00 22.91 ? 133 SER A N 1 ATOM 1050 C CA . SER A 1 133 ? 28.540 26.032 10.666 1.00 22.16 ? 133 SER A CA 1 ATOM 1051 C C . SER A 1 133 ? 28.597 26.546 9.238 1.00 22.53 ? 133 SER A C 1 ATOM 1052 O O . SER A 1 133 ? 27.587 26.996 8.698 1.00 22.62 ? 133 SER A O 1 ATOM 1053 C CB . SER A 1 133 ? 28.768 24.521 10.706 1.00 22.95 ? 133 SER A CB 1 ATOM 1054 O OG . SER A 1 133 ? 27.800 23.837 9.929 1.00 25.78 ? 133 SER A OG 1 ATOM 1055 N N . GLU A 1 134 ? 29.772 26.478 8.625 1.00 22.94 ? 134 GLU A N 1 ATOM 1056 C CA . GLU A 1 134 ? 29.939 27.022 7.288 1.00 21.99 ? 134 GLU A CA 1 ATOM 1057 C C . GLU A 1 134 ? 31.160 26.422 6.619 1.00 21.69 ? 134 GLU A C 1 ATOM 1058 O O . GLU A 1 134 ? 32.071 25.928 7.284 1.00 23.35 ? 134 GLU A O 1 ATOM 1059 C CB . GLU A 1 134 ? 30.095 28.543 7.349 1.00 20.69 ? 134 GLU A CB 1 ATOM 1060 C CG . GLU A 1 134 ? 31.427 29.002 7.920 1.00 23.49 ? 134 GLU A CG 1 ATOM 1061 C CD . GLU A 1 134 ? 31.472 30.495 8.172 1.00 23.92 ? 134 GLU A CD 1 ATOM 1062 O OE1 . GLU A 1 134 ? 30.776 30.966 9.096 1.00 24.46 ? 134 GLU A OE1 1 ATOM 1063 O OE2 . GLU A 1 134 ? 32.204 31.200 7.444 1.00 24.15 ? 134 GLU A OE2 1 ATOM 1064 N N . THR A 1 135 ? 31.169 26.469 5.294 1.00 16.30 ? 135 THR A N 1 ATOM 1065 C CA . THR A 1 135 ? 32.322 26.041 4.525 1.00 16.97 ? 135 THR A CA 1 ATOM 1066 C C . THR A 1 135 ? 33.196 27.245 4.211 1.00 16.88 ? 135 THR A C 1 ATOM 1067 O O . THR A 1 135 ? 32.783 28.390 4.396 1.00 13.55 ? 135 THR A O 1 ATOM 1068 C CB . THR A 1 135 ? 31.904 25.385 3.199 1.00 15.00 ? 135 THR A CB 1 ATOM 1069 O OG1 . THR A 1 135 ? 31.342 26.376 2.330 1.00 12.44 ? 135 THR A OG1 1 ATOM 1070 C CG2 . THR A 1 135 ? 30.873 24.288 3.445 1.00 15.59 ? 135 THR A CG2 1 ATOM 1071 N N . VAL A 1 136 ? 34.413 26.982 3.750 1.00 20.08 ? 136 VAL A N 1 ATOM 1072 C CA . VAL A 1 136 ? 35.243 28.026 3.170 1.00 16.94 ? 136 VAL A CA 1 ATOM 1073 C C . VAL A 1 136 ? 34.695 28.374 1.792 1.00 16.22 ? 136 VAL A C 1 ATOM 1074 O O . VAL A 1 136 ? 33.675 27.832 1.365 1.00 17.66 ? 136 VAL A O 1 ATOM 1075 C CB . VAL A 1 136 ? 36.716 27.595 3.055 1.00 14.84 ? 136 VAL A CB 1 ATOM 1076 C CG1 . VAL A 1 136 ? 37.299 27.321 4.433 1.00 15.93 ? 136 VAL A CG1 1 ATOM 1077 C CG2 . VAL A 1 136 ? 36.841 26.375 2.159 1.00 13.99 ? 136 VAL A CG2 1 ATOM 1078 N N . PHE A 1 137 ? 35.381 29.262 1.086 1.00 15.67 ? 137 PHE A N 1 ATOM 1079 C CA . PHE A 1 137 ? 34.972 29.616 -0.267 1.00 17.77 ? 137 PHE A CA 1 ATOM 1080 C C . PHE A 1 137 ? 35.350 28.502 -1.232 1.00 17.71 ? 137 PHE A C 1 ATOM 1081 O O . PHE A 1 137 ? 36.491 28.057 -1.262 1.00 18.30 ? 137 PHE A O 1 ATOM 1082 C CB . PHE A 1 137 ? 35.594 30.948 -0.685 1.00 15.55 ? 137 PHE A CB 1 ATOM 1083 C CG . PHE A 1 137 ? 35.130 32.110 0.142 1.00 13.26 ? 137 PHE A CG 1 ATOM 1084 C CD1 . PHE A 1 137 ? 35.827 32.498 1.274 1.00 14.58 ? 137 PHE A CD1 1 ATOM 1085 C CD2 . PHE A 1 137 ? 33.982 32.803 -0.204 1.00 12.20 ? 137 PHE A CD2 1 ATOM 1086 C CE1 . PHE A 1 137 ? 35.394 33.565 2.040 1.00 13.07 ? 137 PHE A CE1 1 ATOM 1087 C CE2 . PHE A 1 137 ? 33.542 33.869 0.557 1.00 11.63 ? 137 PHE A CE2 1 ATOM 1088 C CZ . PHE A 1 137 ? 34.250 34.250 1.683 1.00 13.23 ? 137 PHE A CZ 1 ATOM 1089 N N . LEU A 1 138 ? 34.385 28.048 -2.021 1.00 16.16 ? 138 LEU A N 1 ATOM 1090 C CA . LEU A 1 138 ? 34.613 26.903 -2.890 1.00 15.64 ? 138 LEU A CA 1 ATOM 1091 C C . LEU A 1 138 ? 34.696 27.369 -4.338 1.00 15.93 ? 138 LEU A C 1 ATOM 1092 O O . LEU A 1 138 ? 33.921 28.224 -4.763 1.00 12.35 ? 138 LEU A O 1 ATOM 1093 C CB . LEU A 1 138 ? 33.497 25.874 -2.706 1.00 14.29 ? 138 LEU A CB 1 ATOM 1094 C CG . LEU A 1 138 ? 33.261 25.433 -1.258 1.00 12.28 ? 138 LEU A CG 1 ATOM 1095 C CD1 . LEU A 1 138 ? 31.960 24.653 -1.128 1.00 12.52 ? 138 LEU A CD1 1 ATOM 1096 C CD2 . LEU A 1 138 ? 34.437 24.614 -0.738 1.00 13.15 ? 138 LEU A CD2 1 ATOM 1097 N N . PRO A 1 139 ? 35.639 26.799 -5.106 1.00 15.65 ? 139 PRO A N 1 ATOM 1098 C CA . PRO A 1 139 ? 35.870 27.275 -6.473 1.00 14.84 ? 139 PRO A CA 1 ATOM 1099 C C . PRO A 1 139 ? 34.826 26.801 -7.474 1.00 18.79 ? 139 PRO A C 1 ATOM 1100 O O . PRO A 1 139 ? 34.315 25.686 -7.368 1.00 19.67 ? 139 PRO A O 1 ATOM 1101 C CB . PRO A 1 139 ? 37.221 26.647 -6.823 1.00 14.33 ? 139 PRO A CB 1 ATOM 1102 C CG . PRO A 1 139 ? 37.250 25.384 -6.029 1.00 13.35 ? 139 PRO A CG 1 ATOM 1103 C CD . PRO A 1 139 ? 36.560 25.711 -4.733 1.00 12.42 ? 139 PRO A CD 1 ATOM 1104 N N . ARG A 1 140 ? 34.517 27.657 -8.443 1.00 16.95 ? 140 ARG A N 1 ATOM 1105 C CA . ARG A 1 140 ? 33.664 27.273 -9.555 1.00 13.83 ? 140 ARG A CA 1 ATOM 1106 C C . ARG A 1 140 ? 34.491 27.204 -10.830 1.00 14.18 ? 140 ARG A C 1 ATOM 1107 O O . ARG A 1 140 ? 35.560 27.809 -10.917 1.00 14.48 ? 140 ARG A O 1 ATOM 1108 C CB . ARG A 1 140 ? 32.535 28.284 -9.736 1.00 10.10 ? 140 ARG A CB 1 ATOM 1109 C CG . ARG A 1 140 ? 31.483 28.235 -8.646 1.00 10.02 ? 140 ARG A CG 1 ATOM 1110 C CD . ARG A 1 140 ? 30.517 29.392 -8.790 1.00 10.76 ? 140 ARG A CD 1 ATOM 1111 N NE . ARG A 1 140 ? 30.092 29.535 -10.177 1.00 11.35 ? 140 ARG A NE 1 ATOM 1112 C CZ . ARG A 1 140 ? 29.031 28.927 -10.697 1.00 11.37 ? 140 ARG A CZ 1 ATOM 1113 N NH1 . ARG A 1 140 ? 28.286 28.130 -9.943 1.00 10.50 ? 140 ARG A NH1 1 ATOM 1114 N NH2 . ARG A 1 140 ? 28.721 29.106 -11.974 1.00 10.33 ? 140 ARG A NH2 1 ATOM 1115 N N . GLU A 1 141 ? 34.003 26.455 -11.812 1.00 11.59 ? 141 GLU A N 1 ATOM 1116 C CA . GLU A 1 141 ? 34.702 26.306 -13.084 1.00 12.00 ? 141 GLU A CA 1 ATOM 1117 C C . GLU A 1 141 ? 34.740 27.606 -13.889 1.00 13.93 ? 141 GLU A C 1 ATOM 1118 O O . GLU A 1 141 ? 35.544 27.751 -14.810 1.00 12.39 ? 141 GLU A O 1 ATOM 1119 C CB . GLU A 1 141 ? 34.094 25.171 -13.905 1.00 13.89 ? 141 GLU A CB 1 ATOM 1120 C CG . GLU A 1 141 ? 34.234 23.811 -13.237 1.00 23.61 ? 141 GLU A CG 1 ATOM 1121 C CD . GLU A 1 141 ? 33.721 22.676 -14.098 1.00 29.94 ? 141 GLU A CD 1 ATOM 1122 O OE1 . GLU A 1 141 ? 34.019 22.665 -15.310 1.00 32.97 ? 141 GLU A OE1 1 ATOM 1123 O OE2 . GLU A 1 141 ? 33.021 21.792 -13.560 1.00 33.42 ? 141 GLU A OE2 1 ATOM 1124 N N . ASP A 1 142 ? 33.865 28.547 -13.545 1.00 11.66 ? 142 ASP A N 1 ATOM 1125 C CA . ASP A 1 142 ? 33.894 29.868 -14.164 1.00 12.18 ? 142 ASP A CA 1 ATOM 1126 C C . ASP A 1 142 ? 34.711 30.840 -13.319 1.00 15.47 ? 142 ASP A C 1 ATOM 1127 O O . ASP A 1 142 ? 34.740 32.045 -13.578 1.00 14.16 ? 142 ASP A O 1 ATOM 1128 C CB . ASP A 1 142 ? 32.487 30.404 -14.466 1.00 9.80 ? 142 ASP A CB 1 ATOM 1129 C CG . ASP A 1 142 ? 31.624 30.541 -13.222 1.00 17.25 ? 142 ASP A CG 1 ATOM 1130 O OD1 . ASP A 1 142 ? 32.142 30.387 -12.098 1.00 9.33 ? 142 ASP A OD1 1 ATOM 1131 O OD2 . ASP A 1 142 ? 30.414 30.809 -13.375 1.00 17.64 ? 142 ASP A OD2 1 ATOM 1132 N N . HIS A 1 143 ? 35.340 30.288 -12.284 1.00 14.91 ? 143 HIS A N 1 ATOM 1133 C CA . HIS A 1 143 ? 36.326 30.996 -11.468 1.00 13.65 ? 143 HIS A CA 1 ATOM 1134 C C . HIS A 1 143 ? 35.700 32.048 -10.555 1.00 12.08 ? 143 HIS A C 1 ATOM 1135 O O . HIS A 1 143 ? 36.392 32.899 -9.998 1.00 10.50 ? 143 HIS A O 1 ATOM 1136 C CB . HIS A 1 143 ? 37.461 31.541 -12.338 1.00 11.91 ? 143 HIS A CB 1 ATOM 1137 C CG . HIS A 1 143 ? 37.907 30.578 -13.394 1.00 17.41 ? 143 HIS A CG 1 ATOM 1138 N ND1 . HIS A 1 143 ? 38.400 29.325 -13.097 1.00 14.49 ? 143 HIS A ND1 1 ATOM 1139 C CD2 . HIS A 1 143 ? 37.913 30.674 -14.745 1.00 9.87 ? 143 HIS A CD2 1 ATOM 1140 C CE1 . HIS A 1 143 ? 38.693 28.692 -14.220 1.00 12.78 ? 143 HIS A CE1 1 ATOM 1141 N NE2 . HIS A 1 143 ? 38.412 29.491 -15.234 1.00 14.15 ? 143 HIS A NE2 1 ATOM 1142 N N . LEU A 1 144 ? 34.381 31.969 -10.408 1.00 16.90 ? 144 LEU A N 1 ATOM 1143 C CA . LEU A 1 144 ? 33.693 32.618 -9.303 1.00 8.24 ? 144 LEU A CA 1 ATOM 1144 C C . LEU A 1 144 ? 33.726 31.669 -8.112 1.00 8.59 ? 144 LEU A C 1 ATOM 1145 O O . LEU A 1 144 ? 34.463 30.682 -8.121 1.00 10.93 ? 144 LEU A O 1 ATOM 1146 C CB . LEU A 1 144 ? 32.250 32.944 -9.691 1.00 11.31 ? 144 LEU A CB 1 ATOM 1147 C CG . LEU A 1 144 ? 32.097 33.839 -10.920 1.00 11.95 ? 144 LEU A CG 1 ATOM 1148 C CD1 . LEU A 1 144 ? 30.636 33.976 -11.321 1.00 8.04 ? 144 LEU A CD1 1 ATOM 1149 C CD2 . LEU A 1 144 ? 32.706 35.203 -10.644 1.00 8.80 ? 144 LEU A CD2 1 ATOM 1150 N N . PHE A 1 145 ? 32.941 31.963 -7.082 1.00 8.52 ? 145 PHE A N 1 ATOM 1151 C CA . PHE A 1 145 ? 32.989 31.165 -5.863 1.00 10.37 ? 145 PHE A CA 1 ATOM 1152 C C . PHE A 1 145 ? 31.602 30.760 -5.382 1.00 10.54 ? 145 PHE A C 1 ATOM 1153 O O . PHE A 1 145 ? 30.597 31.327 -5.809 1.00 11.06 ? 145 PHE A O 1 ATOM 1154 C CB . PHE A 1 145 ? 33.689 31.946 -4.747 1.00 11.54 ? 145 PHE A CB 1 ATOM 1155 C CG . PHE A 1 145 ? 35.126 32.265 -5.034 1.00 10.14 ? 145 PHE A CG 1 ATOM 1156 C CD1 . PHE A 1 145 ? 36.132 31.369 -4.706 1.00 10.81 ? 145 PHE A CD1 1 ATOM 1157 C CD2 . PHE A 1 145 ? 35.473 33.470 -5.625 1.00 9.11 ? 145 PHE A CD2 1 ATOM 1158 C CE1 . PHE A 1 145 ? 37.458 31.667 -4.967 1.00 9.71 ? 145 PHE A CE1 1 ATOM 1159 C CE2 . PHE A 1 145 ? 36.795 33.775 -5.889 1.00 8.79 ? 145 PHE A CE2 1 ATOM 1160 C CZ . PHE A 1 145 ? 37.789 32.873 -5.559 1.00 9.59 ? 145 PHE A CZ 1 ATOM 1161 N N . ARG A 1 146 ? 31.551 29.770 -4.495 1.00 11.81 ? 146 ARG A N 1 ATOM 1162 C CA . ARG A 1 146 ? 30.301 29.418 -3.830 1.00 15.18 ? 146 ARG A CA 1 ATOM 1163 C C . ARG A 1 146 ? 30.611 29.084 -2.380 1.00 13.58 ? 146 ARG A C 1 ATOM 1164 O O . ARG A 1 146 ? 31.772 28.893 -2.018 1.00 13.14 ? 146 ARG A O 1 ATOM 1165 C CB . ARG A 1 146 ? 29.585 28.246 -4.507 1.00 15.32 ? 146 ARG A CB 1 ATOM 1166 C CG . ARG A 1 146 ? 30.432 27.269 -5.291 1.00 16.96 ? 146 ARG A CG 1 ATOM 1167 C CD . ARG A 1 146 ? 29.620 25.985 -5.453 1.00 23.19 ? 146 ARG A CD 1 ATOM 1168 N NE . ARG A 1 146 ? 30.435 24.775 -5.472 1.00 32.24 ? 146 ARG A NE 1 ATOM 1169 C CZ . ARG A 1 146 ? 29.928 23.545 -5.459 1.00 39.77 ? 146 ARG A CZ 1 ATOM 1170 N NH1 . ARG A 1 146 ? 28.614 23.366 -5.408 1.00 35.84 ? 146 ARG A NH1 1 ATOM 1171 N NH2 . ARG A 1 146 ? 30.734 22.492 -5.480 1.00 47.28 ? 146 ARG A NH2 1 ATOM 1172 N N . LYS A 1 147 ? 29.574 29.000 -1.555 1.00 11.89 ? 147 LYS A N 1 ATOM 1173 C CA . LYS A 1 147 ? 29.775 28.811 -0.129 1.00 14.40 ? 147 LYS A CA 1 ATOM 1174 C C . LYS A 1 147 ? 28.489 28.260 0.485 1.00 17.92 ? 147 LYS A C 1 ATOM 1175 O O . LYS A 1 147 ? 27.394 28.544 0.001 1.00 21.38 ? 147 LYS A O 1 ATOM 1176 C CB . LYS A 1 147 ? 30.117 30.166 0.494 1.00 13.58 ? 147 LYS A CB 1 ATOM 1177 C CG . LYS A 1 147 ? 30.786 30.132 1.855 1.00 17.35 ? 147 LYS A CG 1 ATOM 1178 C CD . LYS A 1 147 ? 31.021 31.558 2.342 1.00 18.92 ? 147 LYS A CD 1 ATOM 1179 C CE . LYS A 1 147 ? 32.055 31.623 3.455 1.00 19.03 ? 147 LYS A CE 1 ATOM 1180 N NZ . LYS A 1 147 ? 31.615 30.911 4.682 1.00 19.81 ? 147 LYS A NZ 1 ATOM 1181 N N . PHE A 1 148 ? 28.627 27.474 1.551 1.00 16.77 ? 148 PHE A N 1 ATOM 1182 C CA . PHE A 1 148 ? 27.473 26.914 2.245 1.00 14.66 ? 148 PHE A CA 1 ATOM 1183 C C . PHE A 1 148 ? 27.469 27.319 3.710 1.00 13.00 ? 148 PHE A C 1 ATOM 1184 O O . PHE A 1 148 ? 28.508 27.311 4.372 1.00 15.13 ? 148 PHE A O 1 ATOM 1185 C CB . PHE A 1 148 ? 27.487 25.383 2.190 1.00 17.45 ? 148 PHE A CB 1 ATOM 1186 C CG . PHE A 1 148 ? 27.377 24.809 0.807 1.00 18.24 ? 148 PHE A CG 1 ATOM 1187 C CD1 . PHE A 1 148 ? 28.487 24.714 -0.018 1.00 18.92 ? 148 PHE A CD1 1 ATOM 1188 C CD2 . PHE A 1 148 ? 26.162 24.328 0.345 1.00 19.22 ? 148 PHE A CD2 1 ATOM 1189 C CE1 . PHE A 1 148 ? 28.381 24.171 -1.285 1.00 14.09 ? 148 PHE A CE1 1 ATOM 1190 C CE2 . PHE A 1 148 ? 26.050 23.782 -0.918 1.00 19.73 ? 148 PHE A CE2 1 ATOM 1191 C CZ . PHE A 1 148 ? 27.160 23.702 -1.734 1.00 18.86 ? 148 PHE A CZ 1 ATOM 1192 N N . HIS A 1 149 ? 26.290 27.668 4.212 1.00 12.13 ? 149 HIS A N 1 ATOM 1193 C CA . HIS A 1 149 ? 26.097 27.899 5.637 1.00 13.94 ? 149 HIS A CA 1 ATOM 1194 C C . HIS A 1 149 ? 24.991 26.981 6.150 1.00 15.92 ? 149 HIS A C 1 ATOM 1195 O O . HIS A 1 149 ? 24.029 26.702 5.433 1.00 15.76 ? 149 HIS A O 1 ATOM 1196 C CB . HIS A 1 149 ? 25.755 29.365 5.895 1.00 12.39 ? 149 HIS A CB 1 ATOM 1197 C CG . HIS A 1 149 ? 26.950 30.269 5.872 1.00 15.42 ? 149 HIS A CG 1 ATOM 1198 N ND1 . HIS A 1 149 ? 27.385 30.962 6.982 1.00 16.09 ? 149 HIS A ND1 1 ATOM 1199 C CD2 . HIS A 1 149 ? 27.806 30.585 4.872 1.00 15.15 ? 149 HIS A CD2 1 ATOM 1200 C CE1 . HIS A 1 149 ? 28.457 31.666 6.665 1.00 16.00 ? 149 HIS A CE1 1 ATOM 1201 N NE2 . HIS A 1 149 ? 28.733 31.456 5.390 1.00 13.60 ? 149 HIS A NE2 1 ATOM 1202 N N . TYR A 1 150 ? 25.118 26.519 7.390 1.00 18.87 ? 150 TYR A N 1 ATOM 1203 C CA . TYR A 1 150 ? 24.190 25.521 7.909 1.00 18.34 ? 150 TYR A CA 1 ATOM 1204 C C . TYR A 1 150 ? 23.589 25.916 9.249 1.00 16.23 ? 150 TYR A C 1 ATOM 1205 O O . TYR A 1 150 ? 24.256 26.511 10.093 1.00 17.24 ? 150 TYR A O 1 ATOM 1206 C CB . TYR A 1 150 ? 24.902 24.176 8.085 1.00 19.22 ? 150 TYR A CB 1 ATOM 1207 C CG . TYR A 1 150 ? 25.559 23.634 6.842 1.00 17.05 ? 150 TYR A CG 1 ATOM 1208 C CD1 . TYR A 1 150 ? 24.817 22.982 5.867 1.00 17.88 ? 150 TYR A CD1 1 ATOM 1209 C CD2 . TYR A 1 150 ? 26.927 23.757 6.652 1.00 19.47 ? 150 TYR A CD2 1 ATOM 1210 C CE1 . TYR A 1 150 ? 25.419 22.479 4.730 1.00 20.35 ? 150 TYR A CE1 1 ATOM 1211 C CE2 . TYR A 1 150 ? 27.540 23.257 5.521 1.00 18.87 ? 150 TYR A CE2 1 ATOM 1212 C CZ . TYR A 1 150 ? 26.782 22.619 4.564 1.00 19.12 ? 150 TYR A CZ 1 ATOM 1213 O OH . TYR A 1 150 ? 27.389 22.121 3.435 1.00 14.56 ? 150 TYR A OH 1 ATOM 1214 N N . LEU A 1 151 ? 22.315 25.583 9.429 1.00 17.22 ? 151 LEU A N 1 ATOM 1215 C CA . LEU A 1 151 ? 21.631 25.813 10.691 1.00 21.27 ? 151 LEU A CA 1 ATOM 1216 C C . LEU A 1 151 ? 20.741 24.622 11.035 1.00 20.86 ? 151 LEU A C 1 ATOM 1217 O O . LEU A 1 151 ? 19.670 24.459 10.451 1.00 23.92 ? 151 LEU A O 1 ATOM 1218 C CB . LEU A 1 151 ? 20.792 27.091 10.628 1.00 21.16 ? 151 LEU A CB 1 ATOM 1219 C CG . LEU A 1 151 ? 19.912 27.371 11.850 1.00 23.34 ? 151 LEU A CG 1 ATOM 1220 C CD1 . LEU A 1 151 ? 20.758 27.494 13.111 1.00 22.69 ? 151 LEU A CD1 1 ATOM 1221 C CD2 . LEU A 1 151 ? 19.074 28.624 11.633 1.00 21.05 ? 151 LEU A CD2 1 ATOM 1222 N N . PRO A 1 152 ? 21.188 23.778 11.977 1.00 19.81 ? 152 PRO A N 1 ATOM 1223 C CA . PRO A 1 152 ? 20.331 22.715 12.512 1.00 22.88 ? 152 PRO A CA 1 ATOM 1224 C C . PRO A 1 152 ? 19.140 23.360 13.205 1.00 24.75 ? 152 PRO A C 1 ATOM 1225 O O . PRO A 1 152 ? 19.315 24.365 13.892 1.00 27.66 ? 152 PRO A O 1 ATOM 1226 C CB . PRO A 1 152 ? 21.231 22.012 13.534 1.00 21.22 ? 152 PRO A CB 1 ATOM 1227 C CG . PRO A 1 152 ? 22.329 22.986 13.829 1.00 23.10 ? 152 PRO A CG 1 ATOM 1228 C CD . PRO A 1 152 ? 22.538 23.745 12.562 1.00 21.68 ? 152 PRO A CD 1 ATOM 1229 N N . PHE A 1 153 ? 17.949 22.799 13.033 1.00 22.94 ? 153 PHE A N 1 ATOM 1230 C CA . PHE A 1 153 ? 16.760 23.392 13.633 1.00 22.31 ? 153 PHE A CA 1 ATOM 1231 C C . PHE A 1 153 ? 15.647 22.382 13.869 1.00 23.43 ? 153 PHE A C 1 ATOM 1232 O O . PHE A 1 153 ? 15.630 21.303 13.276 1.00 23.68 ? 153 PHE A O 1 ATOM 1233 C CB . PHE A 1 153 ? 16.236 24.545 12.768 1.00 19.02 ? 153 PHE A CB 1 ATOM 1234 C CG . PHE A 1 153 ? 15.453 24.097 11.565 1.00 19.93 ? 153 PHE A CG 1 ATOM 1235 C CD1 . PHE A 1 153 ? 16.075 23.447 10.512 1.00 22.08 ? 153 PHE A CD1 1 ATOM 1236 C CD2 . PHE A 1 153 ? 14.090 24.338 11.484 1.00 20.67 ? 153 PHE A CD2 1 ATOM 1237 C CE1 . PHE A 1 153 ? 15.350 23.036 9.406 1.00 19.04 ? 153 PHE A CE1 1 ATOM 1238 C CE2 . PHE A 1 153 ? 13.363 23.932 10.382 1.00 20.16 ? 153 PHE A CE2 1 ATOM 1239 C CZ . PHE A 1 153 ? 13.994 23.281 9.342 1.00 20.26 ? 153 PHE A CZ 1 ATOM 1240 N N . LEU A 1 154 ? 14.717 22.751 14.743 1.00 26.42 ? 154 LEU A N 1 ATOM 1241 C CA . LEU A 1 154 ? 13.550 21.932 15.021 1.00 27.21 ? 154 LEU A CA 1 ATOM 1242 C C . LEU A 1 154 ? 12.341 22.599 14.389 1.00 26.22 ? 154 LEU A C 1 ATOM 1243 O O . LEU A 1 154 ? 11.865 23.623 14.881 1.00 24.76 ? 154 LEU A O 1 ATOM 1244 C CB . LEU A 1 154 ? 13.344 21.798 16.530 1.00 32.06 ? 154 LEU A CB 1 ATOM 1245 C CG . LEU A 1 154 ? 13.623 20.450 17.195 1.00 41.56 ? 154 LEU A CG 1 ATOM 1246 C CD1 . LEU A 1 154 ? 13.259 20.515 18.669 1.00 44.61 ? 154 LEU A CD1 1 ATOM 1247 C CD2 . LEU A 1 154 ? 12.858 19.338 16.500 1.00 44.43 ? 154 LEU A CD2 1 ATOM 1248 N N . PRO A 1 155 ? 11.848 22.021 13.283 1.00 25.73 ? 155 PRO A N 1 ATOM 1249 C CA . PRO A 1 155 ? 10.770 22.615 12.490 1.00 26.77 ? 155 PRO A CA 1 ATOM 1250 C C . PRO A 1 155 ? 9.518 22.851 13.317 1.00 33.98 ? 155 PRO A C 1 ATOM 1251 O O . PRO A 1 155 ? 9.115 21.993 14.103 1.00 36.81 ? 155 PRO A O 1 ATOM 1252 C CB . PRO A 1 155 ? 10.502 21.559 11.416 1.00 25.16 ? 155 PRO A CB 1 ATOM 1253 C CG . PRO A 1 155 ? 11.788 20.822 11.292 1.00 21.50 ? 155 PRO A CG 1 ATOM 1254 C CD . PRO A 1 155 ? 12.343 20.771 12.684 1.00 23.88 ? 155 PRO A CD 1 ATOM 1255 N N . SER A 1 156 ? 8.911 24.016 13.133 1.00 36.06 ? 156 SER A N 1 ATOM 1256 C CA . SER A 1 156 ? 7.697 24.363 13.848 1.00 41.09 ? 156 SER A CA 1 ATOM 1257 C C . SER A 1 156 ? 6.878 25.342 13.025 1.00 41.43 ? 156 SER A C 1 ATOM 1258 O O . SER A 1 156 ? 7.402 26.013 12.135 1.00 43.95 ? 156 SER A O 1 ATOM 1259 C CB . SER A 1 156 ? 8.043 24.985 15.202 1.00 45.62 ? 156 SER A CB 1 ATOM 1260 O OG . SER A 1 156 ? 8.702 26.228 15.041 1.00 50.93 ? 156 SER A OG 1 ATOM 1261 N N . THR A 1 157 ? 5.587 25.418 13.324 1.00 40.30 ? 157 THR A N 1 ATOM 1262 C CA . THR A 1 157 ? 4.698 26.351 12.648 1.00 37.39 ? 157 THR A CA 1 ATOM 1263 C C . THR A 1 157 ? 4.928 27.774 13.150 1.00 38.67 ? 157 THR A C 1 ATOM 1264 O O . THR A 1 157 ? 4.450 28.738 12.553 1.00 33.86 ? 157 THR A O 1 ATOM 1265 C CB . THR A 1 157 ? 3.223 25.970 12.868 1.00 39.38 ? 157 THR A CB 1 ATOM 1266 O OG1 . THR A 1 157 ? 2.944 25.909 14.272 1.00 43.26 ? 157 THR A OG1 1 ATOM 1267 C CG2 . THR A 1 157 ? 2.924 24.617 12.236 1.00 31.04 ? 157 THR A CG2 1 ATOM 1268 N N . GLU A 1 158 ? 5.669 27.897 14.248 1.00 46.42 ? 158 GLU A N 1 ATOM 1269 C CA . GLU A 1 158 ? 5.833 29.177 14.935 1.00 51.85 ? 158 GLU A CA 1 ATOM 1270 C C . GLU A 1 158 ? 7.071 29.968 14.511 1.00 49.93 ? 158 GLU A C 1 ATOM 1271 O O . GLU A 1 158 ? 7.195 31.151 14.829 1.00 54.21 ? 158 GLU A O 1 ATOM 1272 C CB . GLU A 1 158 ? 5.843 28.966 16.453 1.00 57.96 ? 158 GLU A CB 1 ATOM 1273 C CG . GLU A 1 158 ? 4.566 28.366 17.036 1.00 65.88 ? 158 GLU A CG 1 ATOM 1274 C CD . GLU A 1 158 ? 3.305 29.096 16.609 1.00 71.92 ? 158 GLU A CD 1 ATOM 1275 O OE1 . GLU A 1 158 ? 2.824 29.946 17.386 1.00 75.85 ? 158 GLU A OE1 1 ATOM 1276 O OE2 . GLU A 1 158 ? 2.784 28.811 15.509 1.00 72.46 ? 158 GLU A OE2 1 ATOM 1277 N N . ASP A 1 159 ? 7.984 29.317 13.797 1.00 43.02 ? 159 ASP A N 1 ATOM 1278 C CA . ASP A 1 159 ? 9.234 29.960 13.401 1.00 38.11 ? 159 ASP A CA 1 ATOM 1279 C C . ASP A 1 159 ? 9.372 30.175 11.898 1.00 37.12 ? 159 ASP A C 1 ATOM 1280 O O . ASP A 1 159 ? 9.022 29.308 11.097 1.00 39.85 ? 159 ASP A O 1 ATOM 1281 C CB . ASP A 1 159 ? 10.429 29.144 13.896 1.00 37.46 ? 159 ASP A CB 1 ATOM 1282 C CG . ASP A 1 159 ? 10.499 29.075 15.407 1.00 40.34 ? 159 ASP A CG 1 ATOM 1283 O OD1 . ASP A 1 159 ? 10.051 30.035 16.067 1.00 41.21 ? 159 ASP A OD1 1 ATOM 1284 O OD2 . ASP A 1 159 ? 11.005 28.063 15.935 1.00 43.07 ? 159 ASP A OD2 1 ATOM 1285 N N . VAL A 1 160 ? 9.887 31.342 11.526 1.00 35.79 ? 160 VAL A N 1 ATOM 1286 C CA . VAL A 1 160 ? 10.306 31.588 10.153 1.00 25.31 ? 160 VAL A CA 1 ATOM 1287 C C . VAL A 1 160 ? 11.805 31.858 10.139 1.00 24.35 ? 160 VAL A C 1 ATOM 1288 O O . VAL A 1 160 ? 12.373 32.307 11.136 1.00 33.10 ? 160 VAL A O 1 ATOM 1289 C CB . VAL A 1 160 ? 9.555 32.772 9.509 1.00 26.14 ? 160 VAL A CB 1 ATOM 1290 C CG1 . VAL A 1 160 ? 8.052 32.540 9.559 1.00 27.32 ? 160 VAL A CG1 1 ATOM 1291 C CG2 . VAL A 1 160 ? 9.925 34.084 10.191 1.00 27.19 ? 160 VAL A CG2 1 ATOM 1292 N N . TYR A 1 161 ? 12.448 31.574 9.013 1.00 22.93 ? 161 TYR A N 1 ATOM 1293 C CA . TYR A 1 161 ? 13.886 31.769 8.910 1.00 25.01 ? 161 TYR A CA 1 ATOM 1294 C C . TYR A 1 161 ? 14.267 32.586 7.685 1.00 21.47 ? 161 TYR A C 1 ATOM 1295 O O . TYR A 1 161 ? 13.547 32.606 6.687 1.00 21.29 ? 161 TYR A O 1 ATOM 1296 C CB . TYR A 1 161 ? 14.613 30.424 8.874 1.00 23.37 ? 161 TYR A CB 1 ATOM 1297 C CG . TYR A 1 161 ? 14.485 29.625 10.148 1.00 25.45 ? 161 TYR A CG 1 ATOM 1298 C CD1 . TYR A 1 161 ? 13.401 28.782 10.355 1.00 26.81 ? 161 TYR A CD1 1 ATOM 1299 C CD2 . TYR A 1 161 ? 15.445 29.714 11.147 1.00 25.34 ? 161 TYR A CD2 1 ATOM 1300 C CE1 . TYR A 1 161 ? 13.280 28.047 11.516 1.00 25.54 ? 161 TYR A CE1 1 ATOM 1301 C CE2 . TYR A 1 161 ? 15.332 28.984 12.313 1.00 25.43 ? 161 TYR A CE2 1 ATOM 1302 C CZ . TYR A 1 161 ? 14.247 28.152 12.493 1.00 25.43 ? 161 TYR A CZ 1 ATOM 1303 O OH . TYR A 1 161 ? 14.125 27.420 13.651 1.00 27.17 ? 161 TYR A OH 1 ATOM 1304 N N . ASP A 1 162 ? 15.411 33.254 7.769 1.00 21.52 ? 162 ASP A N 1 ATOM 1305 C CA . ASP A 1 162 ? 15.988 33.929 6.619 1.00 20.67 ? 162 ASP A CA 1 ATOM 1306 C C . ASP A 1 162 ? 17.499 33.757 6.648 1.00 19.86 ? 162 ASP A C 1 ATOM 1307 O O . ASP A 1 162 ? 18.110 33.759 7.716 1.00 23.54 ? 162 ASP A O 1 ATOM 1308 C CB . ASP A 1 162 ? 15.663 35.422 6.646 1.00 21.89 ? 162 ASP A CB 1 ATOM 1309 C CG . ASP A 1 162 ? 14.179 35.700 6.514 1.00 24.05 ? 162 ASP A CG 1 ATOM 1310 O OD1 . ASP A 1 162 ? 13.671 35.699 5.374 1.00 24.33 ? 162 ASP A OD1 1 ATOM 1311 O OD2 . ASP A 1 162 ? 13.519 35.921 7.553 1.00 24.09 ? 162 ASP A OD2 1 ATOM 1312 N N . CYS A 1 163 ? 18.100 33.607 5.474 1.00 18.77 ? 163 CYS A N 1 ATOM 1313 C CA . CYS A 1 163 ? 19.542 33.730 5.345 1.00 21.60 ? 163 CYS A CA 1 ATOM 1314 C C . CYS A 1 163 ? 19.837 35.102 4.765 1.00 22.18 ? 163 CYS A C 1 ATOM 1315 O O . CYS A 1 163 ? 19.373 35.432 3.672 1.00 21.33 ? 163 CYS A O 1 ATOM 1316 C CB . CYS A 1 163 ? 20.094 32.647 4.420 1.00 16.83 ? 163 CYS A CB 1 ATOM 1317 S SG . CYS A 1 163 ? 21.883 32.723 4.189 1.00 25.05 ? 163 CYS A SG 1 ATOM 1318 N N . ARG A 1 164 ? 20.604 35.902 5.495 1.00 22.69 ? 164 ARG A N 1 ATOM 1319 C CA . ARG A 1 164 ? 20.927 37.245 5.040 1.00 25.53 ? 164 ARG A CA 1 ATOM 1320 C C . ARG A 1 164 ? 22.367 37.323 4.564 1.00 25.01 ? 164 ARG A C 1 ATOM 1321 O O . ARG A 1 164 ? 23.295 37.005 5.307 1.00 19.63 ? 164 ARG A O 1 ATOM 1322 C CB . ARG A 1 164 ? 20.715 38.264 6.157 1.00 21.79 ? 164 ARG A CB 1 ATOM 1323 C CG . ARG A 1 164 ? 21.012 39.691 5.726 1.00 24.93 ? 164 ARG A CG 1 ATOM 1324 C CD . ARG A 1 164 ? 20.776 40.666 6.857 1.00 24.97 ? 164 ARG A CD 1 ATOM 1325 N NE . ARG A 1 164 ? 21.769 40.499 7.914 1.00 24.83 ? 164 ARG A NE 1 ATOM 1326 C CZ . ARG A 1 164 ? 21.549 40.774 9.195 1.00 29.64 ? 164 ARG A CZ 1 ATOM 1327 N NH1 . ARG A 1 164 ? 20.362 41.218 9.584 1.00 27.21 ? 164 ARG A NH1 1 ATOM 1328 N NH2 . ARG A 1 164 ? 22.512 40.594 10.088 1.00 28.68 ? 164 ARG A NH2 1 ATOM 1329 N N . VAL A 1 165 ? 22.548 37.744 3.318 1.00 19.17 ? 165 VAL A N 1 ATOM 1330 C CA . VAL A 1 165 ? 23.870 37.762 2.713 1.00 21.01 ? 165 VAL A CA 1 ATOM 1331 C C . VAL A 1 165 ? 24.259 39.177 2.301 1.00 21.29 ? 165 VAL A C 1 ATOM 1332 O O . VAL A 1 165 ? 23.529 39.840 1.562 1.00 21.36 ? 165 VAL A O 1 ATOM 1333 C CB . VAL A 1 165 ? 23.923 36.828 1.488 1.00 20.08 ? 165 VAL A CB 1 ATOM 1334 C CG1 . VAL A 1 165 ? 25.249 36.984 0.754 1.00 18.27 ? 165 VAL A CG1 1 ATOM 1335 C CG2 . VAL A 1 165 ? 23.706 35.382 1.914 1.00 16.42 ? 165 VAL A CG2 1 ATOM 1336 N N . GLU A 1 166 ? 25.413 39.632 2.775 1.00 22.97 ? 166 GLU A N 1 ATOM 1337 C CA . GLU A 1 166 ? 25.942 40.926 2.368 1.00 21.07 ? 166 GLU A CA 1 ATOM 1338 C C . GLU A 1 166 ? 27.151 40.685 1.484 1.00 23.27 ? 166 GLU A C 1 ATOM 1339 O O . GLU A 1 166 ? 28.009 39.858 1.789 1.00 19.77 ? 166 GLU A O 1 ATOM 1340 C CB . GLU A 1 166 ? 26.350 41.764 3.580 1.00 32.52 ? 166 GLU A CB 1 ATOM 1341 C CG . GLU A 1 166 ? 25.317 41.858 4.687 1.00 39.74 ? 166 GLU A CG 1 ATOM 1342 C CD . GLU A 1 166 ? 25.909 42.393 5.977 1.00 45.99 ? 166 GLU A CD 1 ATOM 1343 O OE1 . GLU A 1 166 ? 27.092 42.793 5.966 1.00 45.64 ? 166 GLU A OE1 1 ATOM 1344 O OE2 . GLU A 1 166 ? 25.192 42.422 6.999 1.00 51.11 ? 166 GLU A OE2 1 ATOM 1345 N N . HIS A 1 167 ? 27.204 41.415 0.378 1.00 17.03 ? 167 HIS A N 1 ATOM 1346 C CA . HIS A 1 167 ? 28.312 41.320 -0.554 1.00 17.52 ? 167 HIS A CA 1 ATOM 1347 C C . HIS A 1 167 ? 28.413 42.671 -1.244 1.00 16.70 ? 167 HIS A C 1 ATOM 1348 O O . HIS A 1 167 ? 27.403 43.340 -1.455 1.00 18.03 ? 167 HIS A O 1 ATOM 1349 C CB . HIS A 1 167 ? 28.073 40.195 -1.566 1.00 16.24 ? 167 HIS A CB 1 ATOM 1350 C CG . HIS A 1 167 ? 29.239 39.921 -2.465 1.00 17.44 ? 167 HIS A CG 1 ATOM 1351 N ND1 . HIS A 1 167 ? 29.430 40.576 -3.664 1.00 19.34 ? 167 HIS A ND1 1 ATOM 1352 C CD2 . HIS A 1 167 ? 30.263 39.042 -2.350 1.00 17.02 ? 167 HIS A CD2 1 ATOM 1353 C CE1 . HIS A 1 167 ? 30.528 40.121 -4.242 1.00 18.14 ? 167 HIS A CE1 1 ATOM 1354 N NE2 . HIS A 1 167 ? 31.053 39.190 -3.465 1.00 18.47 ? 167 HIS A NE2 1 ATOM 1355 N N . TRP A 1 168 ? 29.631 43.075 -1.581 1.00 16.15 ? 168 TRP A N 1 ATOM 1356 C CA . TRP A 1 168 ? 29.868 44.393 -2.167 1.00 25.68 ? 168 TRP A CA 1 ATOM 1357 C C . TRP A 1 168 ? 29.156 44.606 -3.502 1.00 23.92 ? 168 TRP A C 1 ATOM 1358 O O . TRP A 1 168 ? 28.947 45.741 -3.927 1.00 24.36 ? 168 TRP A O 1 ATOM 1359 C CB . TRP A 1 168 ? 31.369 44.672 -2.287 1.00 22.80 ? 168 TRP A CB 1 ATOM 1360 C CG . TRP A 1 168 ? 32.053 44.716 -0.950 1.00 22.89 ? 168 TRP A CG 1 ATOM 1361 C CD1 . TRP A 1 168 ? 31.589 45.323 0.182 1.00 20.29 ? 168 TRP A CD1 1 ATOM 1362 C CD2 . TRP A 1 168 ? 33.310 44.123 -0.599 1.00 18.68 ? 168 TRP A CD2 1 ATOM 1363 N NE1 . TRP A 1 168 ? 32.480 45.152 1.211 1.00 21.24 ? 168 TRP A NE1 1 ATOM 1364 C CE2 . TRP A 1 168 ? 33.545 44.418 0.760 1.00 20.30 ? 168 TRP A CE2 1 ATOM 1365 C CE3 . TRP A 1 168 ? 34.261 43.375 -1.300 1.00 17.87 ? 168 TRP A CE3 1 ATOM 1366 C CZ2 . TRP A 1 168 ? 34.691 43.991 1.430 1.00 21.02 ? 168 TRP A CZ2 1 ATOM 1367 C CZ3 . TRP A 1 168 ? 35.398 42.951 -0.632 1.00 18.18 ? 168 TRP A CZ3 1 ATOM 1368 C CH2 . TRP A 1 168 ? 35.602 43.260 0.719 1.00 19.80 ? 168 TRP A CH2 1 ATOM 1369 N N . GLY A 1 169 ? 28.785 43.513 -4.162 1.00 16.79 ? 169 GLY A N 1 ATOM 1370 C CA . GLY A 1 169 ? 28.058 43.602 -5.414 1.00 21.53 ? 169 GLY A CA 1 ATOM 1371 C C . GLY A 1 169 ? 26.570 43.835 -5.207 1.00 22.89 ? 169 GLY A C 1 ATOM 1372 O O . GLY A 1 169 ? 25.835 44.070 -6.165 1.00 23.35 ? 169 GLY A O 1 ATOM 1373 N N . LEU A 1 170 ? 26.122 43.762 -3.956 1.00 22.72 ? 170 LEU A N 1 ATOM 1374 C CA . LEU A 1 170 ? 24.717 43.998 -3.631 1.00 22.53 ? 170 LEU A CA 1 ATOM 1375 C C . LEU A 1 170 ? 24.505 45.411 -3.093 1.00 25.86 ? 170 LEU A C 1 ATOM 1376 O O . LEU A 1 170 ? 25.308 45.911 -2.305 1.00 28.02 ? 170 LEU A O 1 ATOM 1377 C CB . LEU A 1 170 ? 24.234 42.988 -2.587 1.00 22.77 ? 170 LEU A CB 1 ATOM 1378 C CG . LEU A 1 170 ? 24.204 41.515 -3.003 1.00 24.76 ? 170 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 170 ? 24.002 40.619 -1.790 1.00 22.86 ? 170 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 170 ? 23.111 41.272 -4.041 1.00 21.69 ? 170 LEU A CD2 1 ATOM 1381 N N . ASP A 1 171 ? 23.419 46.048 -3.524 1.00 30.30 ? 171 ASP A N 1 ATOM 1382 C CA . ASP A 1 171 ? 23.058 47.379 -3.043 1.00 38.12 ? 171 ASP A CA 1 ATOM 1383 C C . ASP A 1 171 ? 22.489 47.321 -1.630 1.00 37.82 ? 171 ASP A C 1 ATOM 1384 O O . ASP A 1 171 ? 22.657 48.249 -0.840 1.00 44.70 ? 171 ASP A O 1 ATOM 1385 C CB . ASP A 1 171 ? 22.055 48.036 -3.991 1.00 45.27 ? 171 ASP A CB 1 ATOM 1386 C CG . ASP A 1 171 ? 22.695 48.512 -5.279 1.00 53.27 ? 171 ASP A CG 1 ATOM 1387 O OD1 . ASP A 1 171 ? 23.902 48.832 -5.262 1.00 56.12 ? 171 ASP A OD1 1 ATOM 1388 O OD2 . ASP A 1 171 ? 21.994 48.556 -6.312 1.00 58.13 ? 171 ASP A OD2 1 ATOM 1389 N N . GLU A 1 172 ? 21.813 46.219 -1.326 1.00 32.84 ? 172 GLU A N 1 ATOM 1390 C CA . GLU A 1 172 ? 21.261 45.976 -0.000 1.00 33.80 ? 172 GLU A CA 1 ATOM 1391 C C . GLU A 1 172 ? 21.447 44.502 0.325 1.00 30.11 ? 172 GLU A C 1 ATOM 1392 O O . GLU A 1 172 ? 21.679 43.699 -0.579 1.00 28.10 ? 172 GLU A O 1 ATOM 1393 C CB . GLU A 1 172 ? 19.779 46.362 0.045 1.00 40.44 ? 172 GLU A CB 1 ATOM 1394 C CG . GLU A 1 172 ? 19.521 47.856 -0.081 1.00 51.19 ? 172 GLU A CG 1 ATOM 1395 C CD . GLU A 1 172 ? 18.653 48.397 1.038 1.00 56.96 ? 172 GLU A CD 1 ATOM 1396 O OE1 . GLU A 1 172 ? 17.876 47.612 1.622 1.00 59.61 ? 172 GLU A OE1 1 ATOM 1397 O OE2 . GLU A 1 172 ? 18.752 49.605 1.338 1.00 58.95 ? 172 GLU A OE2 1 ATOM 1398 N N . PRO A 1 173 ? 21.359 44.135 1.615 1.00 28.33 ? 173 PRO A N 1 ATOM 1399 C CA . PRO A 1 173 ? 21.503 42.713 1.933 1.00 24.95 ? 173 PRO A CA 1 ATOM 1400 C C . PRO A 1 173 ? 20.411 41.875 1.283 1.00 23.61 ? 173 PRO A C 1 ATOM 1401 O O . PRO A 1 173 ? 19.271 42.323 1.153 1.00 26.63 ? 173 PRO A O 1 ATOM 1402 C CB . PRO A 1 173 ? 21.372 42.678 3.457 1.00 25.26 ? 173 PRO A CB 1 ATOM 1403 C CG . PRO A 1 173 ? 21.830 44.025 3.895 1.00 27.78 ? 173 PRO A CG 1 ATOM 1404 C CD . PRO A 1 173 ? 21.365 44.975 2.826 1.00 26.79 ? 173 PRO A CD 1 ATOM 1405 N N . LEU A 1 174 ? 20.767 40.660 0.886 1.00 21.33 ? 174 LEU A N 1 ATOM 1406 C CA . LEU A 1 174 ? 19.830 39.759 0.238 1.00 17.41 ? 174 LEU A CA 1 ATOM 1407 C C . LEU A 1 174 ? 19.253 38.804 1.270 1.00 26.60 ? 174 LEU A C 1 ATOM 1408 O O . LEU A 1 174 ? 19.992 38.095 1.951 1.00 25.24 ? 174 LEU A O 1 ATOM 1409 C CB . LEU A 1 174 ? 20.553 38.983 -0.867 1.00 15.90 ? 174 LEU A CB 1 ATOM 1410 C CG . LEU A 1 174 ? 19.773 38.154 -1.889 1.00 25.47 ? 174 LEU A CG 1 ATOM 1411 C CD1 . LEU A 1 174 ? 18.640 38.956 -2.500 1.00 24.06 ? 174 LEU A CD1 1 ATOM 1412 C CD2 . LEU A 1 174 ? 20.719 37.657 -2.972 1.00 26.03 ? 174 LEU A CD2 1 ATOM 1413 N N . LEU A 1 175 ? 17.929 38.785 1.386 1.00 25.79 ? 175 LEU A N 1 ATOM 1414 C CA . LEU A 1 175 ? 17.276 37.855 2.293 1.00 21.82 ? 175 LEU A CA 1 ATOM 1415 C C . LEU A 1 175 ? 16.497 36.781 1.551 1.00 20.20 ? 175 LEU A C 1 ATOM 1416 O O . LEU A 1 175 ? 15.630 37.081 0.731 1.00 24.23 ? 175 LEU A O 1 ATOM 1417 C CB . LEU A 1 175 ? 16.326 38.597 3.239 1.00 23.14 ? 175 LEU A CB 1 ATOM 1418 C CG . LEU A 1 175 ? 16.875 39.167 4.550 1.00 23.10 ? 175 LEU A CG 1 ATOM 1419 C CD1 . LEU A 1 175 ? 17.685 40.428 4.293 1.00 23.45 ? 175 LEU A CD1 1 ATOM 1420 C CD2 . LEU A 1 175 ? 15.744 39.447 5.530 1.00 25.67 ? 175 LEU A CD2 1 ATOM 1421 N N . LYS A 1 176 ? 16.811 35.525 1.846 1.00 18.52 ? 176 LYS A N 1 ATOM 1422 C CA . LYS A 1 176 ? 16.047 34.411 1.304 1.00 21.99 ? 176 LYS A CA 1 ATOM 1423 C C . LYS A 1 176 ? 15.345 33.708 2.452 1.00 23.06 ? 176 LYS A C 1 ATOM 1424 O O . LYS A 1 176 ? 15.959 33.327 3.446 1.00 23.76 ? 176 LYS A O 1 ATOM 1425 C CB . LYS A 1 176 ? 16.947 33.455 0.528 1.00 21.84 ? 176 LYS A CB 1 ATOM 1426 C CG . LYS A 1 176 ? 17.504 34.072 -0.741 1.00 25.95 ? 176 LYS A CG 1 ATOM 1427 C CD . LYS A 1 176 ? 16.347 34.394 -1.686 1.00 29.13 ? 176 LYS A CD 1 ATOM 1428 C CE . LYS A 1 176 ? 16.755 34.307 -3.146 1.00 29.79 ? 176 LYS A CE 1 ATOM 1429 N NZ . LYS A 1 176 ? 16.672 35.617 -3.842 1.00 28.23 ? 176 LYS A NZ 1 ATOM 1430 N N . HIS A 1 177 ? 14.039 33.544 2.278 1.00 22.92 ? 177 HIS A N 1 ATOM 1431 C CA . HIS A 1 177 ? 13.139 33.135 3.346 1.00 20.41 ? 177 HIS A CA 1 ATOM 1432 C C . HIS A 1 177 ? 12.888 31.634 3.309 1.00 25.41 ? 177 HIS A C 1 ATOM 1433 O O . HIS A 1 177 ? 12.932 31.011 2.252 1.00 25.22 ? 177 HIS A O 1 ATOM 1434 C CB . HIS A 1 177 ? 11.822 33.893 3.193 1.00 23.57 ? 177 HIS A CB 1 ATOM 1435 C CG . HIS A 1 177 ? 10.926 33.817 4.392 1.00 27.55 ? 177 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 177 ? 11.151 34.561 5.530 1.00 26.35 ? 177 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 177 ? 9.803 33.098 4.629 1.00 29.87 ? 177 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 177 ? 10.207 34.304 6.417 1.00 32.05 ? 177 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 177 ? 9.377 33.419 5.896 1.00 32.61 ? 177 HIS A NE2 1 ATOM 1440 N N . TRP A 1 178 ? 12.640 31.070 4.486 1.00 25.86 ? 178 TRP A N 1 ATOM 1441 C CA . TRP A 1 178 ? 12.085 29.720 4.577 1.00 24.23 ? 178 TRP A CA 1 ATOM 1442 C C . TRP A 1 178 ? 11.064 29.622 5.686 1.00 25.15 ? 178 TRP A C 1 ATOM 1443 O O . TRP A 1 178 ? 11.278 30.149 6.796 1.00 26.02 ? 178 TRP A O 1 ATOM 1444 C CB . TRP A 1 178 ? 13.175 28.675 4.810 1.00 20.81 ? 178 TRP A CB 1 ATOM 1445 C CG . TRP A 1 178 ? 12.605 27.286 4.899 1.00 25.67 ? 178 TRP A CG 1 ATOM 1446 C CD1 . TRP A 1 178 ? 12.467 26.394 3.878 1.00 25.77 ? 178 TRP A CD1 1 ATOM 1447 C CD2 . TRP A 1 178 ? 12.081 26.640 6.070 1.00 26.40 ? 178 TRP A CD2 1 ATOM 1448 N NE1 . TRP A 1 178 ? 11.891 25.235 4.336 1.00 25.47 ? 178 TRP A NE1 1 ATOM 1449 C CE2 . TRP A 1 178 ? 11.645 25.360 5.679 1.00 26.28 ? 178 TRP A CE2 1 ATOM 1450 C CE3 . TRP A 1 178 ? 11.942 27.019 7.410 1.00 26.79 ? 178 TRP A CE3 1 ATOM 1451 C CZ2 . TRP A 1 178 ? 11.079 24.456 6.577 1.00 27.89 ? 178 TRP A CZ2 1 ATOM 1452 C CZ3 . TRP A 1 178 ? 11.376 26.121 8.300 1.00 29.31 ? 178 TRP A CZ3 1 ATOM 1453 C CH2 . TRP A 1 178 ? 10.954 24.854 7.879 1.00 29.49 ? 178 TRP A CH2 1 ATOM 1454 N N . GLU A 1 179 ? 9.952 28.964 5.408 1.00 25.93 ? 179 GLU A N 1 ATOM 1455 C CA . GLU A 1 179 ? 8.993 28.609 6.440 1.00 31.32 ? 179 GLU A CA 1 ATOM 1456 C C . GLU A 1 179 ? 8.250 27.311 6.155 1.00 32.32 ? 179 GLU A C 1 ATOM 1457 O O . GLU A 1 179 ? 8.168 26.863 5.011 1.00 32.84 ? 179 GLU A O 1 ATOM 1458 C CB . GLU A 1 179 ? 7.990 29.756 6.667 1.00 35.52 ? 179 GLU A CB 1 ATOM 1459 C CG . GLU A 1 179 ? 7.058 29.974 5.501 1.00 41.83 ? 179 GLU A CG 1 ATOM 1460 C CD . GLU A 1 179 ? 6.169 31.175 5.729 1.00 47.65 ? 179 GLU A CD 1 ATOM 1461 O OE1 . GLU A 1 179 ? 6.709 32.256 6.073 1.00 47.60 ? 179 GLU A OE1 1 ATOM 1462 O OE2 . GLU A 1 179 ? 4.935 31.069 5.507 1.00 54.45 ? 179 GLU A OE2 1 ATOM 1463 N N . PHE A 1 180 ? 7.721 26.700 7.219 1.00 33.56 ? 180 PHE A N 1 ATOM 1464 C CA . PHE A 1 180 ? 7.040 25.411 7.158 1.00 39.80 ? 180 PHE A CA 1 ATOM 1465 C C . PHE A 1 180 ? 5.790 25.332 6.281 1.00 47.46 ? 180 PHE A C 1 ATOM 1466 O O . PHE A 1 180 ? 4.868 26.135 6.436 1.00 49.02 ? 180 PHE A O 1 ATOM 1467 C CB . PHE A 1 180 ? 6.656 24.974 8.570 1.00 40.92 ? 180 PHE A CB 1 ATOM 1468 C CG . PHE A 1 180 ? 6.036 23.603 8.614 1.00 43.51 ? 180 PHE A CG 1 ATOM 1469 C CD1 . PHE A 1 180 ? 6.810 22.466 8.452 1.00 38.44 ? 180 PHE A CD1 1 ATOM 1470 C CD2 . PHE A 1 180 ? 4.668 23.457 8.784 1.00 48.38 ? 180 PHE A CD2 1 ATOM 1471 C CE1 . PHE A 1 180 ? 6.235 21.210 8.476 1.00 40.24 ? 180 PHE A CE1 1 ATOM 1472 C CE2 . PHE A 1 180 ? 4.085 22.205 8.809 1.00 49.77 ? 180 PHE A CE2 1 ATOM 1473 C CZ . PHE A 1 180 ? 4.869 21.078 8.652 1.00 45.51 ? 180 PHE A CZ 1 ATOM 1474 N N . ASP A 1 181 ? 5.775 24.364 5.361 1.00 55.10 ? 181 ASP A N 1 ATOM 1475 C CA . ASP A 1 181 ? 4.700 24.190 4.383 1.00 65.71 ? 181 ASP A CA 1 ATOM 1476 C C . ASP A 1 181 ? 4.562 25.379 3.441 1.00 72.05 ? 181 ASP A C 1 ATOM 1477 O O . ASP A 1 181 ? 4.505 25.210 2.221 1.00 76.17 ? 181 ASP A O 1 ATOM 1478 C CB . ASP A 1 181 ? 3.369 23.920 5.111 1.00 70.15 ? 181 ASP A CB 1 ATOM 1479 C CG . ASP A 1 181 ? 2.199 23.696 4.161 1.00 76.21 ? 181 ASP A CG 1 ATOM 1480 O OD1 . ASP A 1 181 ? 2.425 23.341 2.984 1.00 79.04 ? 181 ASP A OD1 1 ATOM 1481 O OD2 . ASP A 1 181 ? 1.045 23.887 4.598 1.00 77.37 ? 181 ASP A OD2 1 ATOM 1482 N N . ASP B 2 4 ? 32.949 49.526 2.896 1.00 57.55 ? 2 ASP B N 1 ATOM 1483 C CA . ASP B 2 4 ? 34.294 49.440 2.339 1.00 55.95 ? 2 ASP B CA 1 ATOM 1484 C C . ASP B 2 4 ? 34.217 49.357 0.817 1.00 54.01 ? 2 ASP B C 1 ATOM 1485 O O . ASP B 2 4 ? 33.896 48.310 0.253 1.00 52.35 ? 2 ASP B O 1 ATOM 1486 C CB . ASP B 2 4 ? 35.025 48.220 2.902 1.00 54.80 ? 2 ASP B CB 1 ATOM 1487 C CG . ASP B 2 4 ? 36.532 48.316 2.742 1.00 52.40 ? 2 ASP B CG 1 ATOM 1488 O OD1 . ASP B 2 4 ? 36.999 49.134 1.922 1.00 50.58 ? 2 ASP B OD1 1 ATOM 1489 O OD2 . ASP B 2 4 ? 37.253 47.576 3.445 1.00 52.44 ? 2 ASP B OD2 1 ATOM 1490 N N . THR B 2 5 ? 34.517 50.473 0.161 1.00 51.85 ? 3 THR B N 1 ATOM 1491 C CA . THR B 2 5 ? 34.423 50.578 -1.291 1.00 47.32 ? 3 THR B CA 1 ATOM 1492 C C . THR B 2 5 ? 35.794 50.507 -1.955 1.00 41.30 ? 3 THR B C 1 ATOM 1493 O O . THR B 2 5 ? 35.909 50.669 -3.172 1.00 41.46 ? 3 THR B O 1 ATOM 1494 C CB . THR B 2 5 ? 33.714 51.877 -1.725 1.00 47.32 ? 3 THR B CB 1 ATOM 1495 O OG1 . THR B 2 5 ? 34.418 53.007 -1.195 1.00 47.18 ? 3 THR B OG1 1 ATOM 1496 C CG2 . THR B 2 5 ? 32.280 51.894 -1.222 1.00 47.04 ? 3 THR B CG2 1 ATOM 1497 N N . ARG B 2 6 ? 36.828 50.279 -1.148 1.00 35.59 ? 4 ARG B N 1 ATOM 1498 C CA . ARG B 2 6 ? 38.193 50.165 -1.654 1.00 32.87 ? 4 ARG B CA 1 ATOM 1499 C C . ARG B 2 6 ? 38.259 49.062 -2.699 1.00 31.34 ? 4 ARG B C 1 ATOM 1500 O O . ARG B 2 6 ? 37.656 48.002 -2.526 1.00 33.04 ? 4 ARG B O 1 ATOM 1501 C CB . ARG B 2 6 ? 39.180 49.856 -0.530 1.00 31.12 ? 4 ARG B CB 1 ATOM 1502 C CG . ARG B 2 6 ? 39.496 51.012 0.400 1.00 32.50 ? 4 ARG B CG 1 ATOM 1503 C CD . ARG B 2 6 ? 40.507 50.560 1.438 1.00 34.81 ? 4 ARG B CD 1 ATOM 1504 N NE . ARG B 2 6 ? 39.975 49.497 2.285 1.00 34.53 ? 4 ARG B NE 1 ATOM 1505 C CZ . ARG B 2 6 ? 40.719 48.728 3.072 1.00 32.19 ? 4 ARG B CZ 1 ATOM 1506 N NH1 . ARG B 2 6 ? 42.033 48.895 3.117 1.00 31.08 ? 4 ARG B NH1 1 ATOM 1507 N NH2 . ARG B 2 6 ? 40.149 47.786 3.812 1.00 33.18 ? 4 ARG B NH2 1 ATOM 1508 N N . PRO B 2 7 ? 38.996 49.308 -3.790 1.00 27.46 ? 5 PRO B N 1 ATOM 1509 C CA . PRO B 2 7 ? 39.154 48.303 -4.846 1.00 22.94 ? 5 PRO B CA 1 ATOM 1510 C C . PRO B 2 7 ? 39.854 47.041 -4.358 1.00 23.20 ? 5 PRO B C 1 ATOM 1511 O O . PRO B 2 7 ? 40.773 47.100 -3.540 1.00 25.80 ? 5 PRO B O 1 ATOM 1512 C CB . PRO B 2 7 ? 40.018 49.020 -5.889 1.00 22.93 ? 5 PRO B CB 1 ATOM 1513 C CG . PRO B 2 7 ? 40.679 50.136 -5.151 1.00 22.79 ? 5 PRO B CG 1 ATOM 1514 C CD . PRO B 2 7 ? 39.711 50.557 -4.098 1.00 25.03 ? 5 PRO B CD 1 ATOM 1515 N N . ARG B 2 8 ? 39.405 45.904 -4.876 1.00 16.86 ? 6 ARG B N 1 ATOM 1516 C CA . ARG B 2 8 ? 39.987 44.613 -4.545 1.00 15.78 ? 6 ARG B CA 1 ATOM 1517 C C . ARG B 2 8 ? 40.786 44.046 -5.708 1.00 16.36 ? 6 ARG B C 1 ATOM 1518 O O . ARG B 2 8 ? 40.509 44.338 -6.871 1.00 16.77 ? 6 ARG B O 1 ATOM 1519 C CB . ARG B 2 8 ? 38.895 43.619 -4.139 1.00 15.22 ? 6 ARG B CB 1 ATOM 1520 C CG . ARG B 2 8 ? 38.775 43.400 -2.642 1.00 15.76 ? 6 ARG B CG 1 ATOM 1521 C CD . ARG B 2 8 ? 38.403 44.687 -1.935 1.00 23.31 ? 6 ARG B CD 1 ATOM 1522 N NE . ARG B 2 8 ? 38.430 44.542 -0.484 1.00 17.99 ? 6 ARG B NE 1 ATOM 1523 C CZ . ARG B 2 8 ? 38.046 45.489 0.365 1.00 19.43 ? 6 ARG B CZ 1 ATOM 1524 N NH1 . ARG B 2 8 ? 37.602 46.652 -0.093 1.00 20.25 ? 6 ARG B NH1 1 ATOM 1525 N NH2 . ARG B 2 8 ? 38.103 45.273 1.672 1.00 20.20 ? 6 ARG B NH2 1 ATOM 1526 N N . PHE B 2 9 ? 41.782 43.230 -5.382 1.00 14.25 ? 7 PHE B N 1 ATOM 1527 C CA . PHE B 2 9 ? 42.600 42.581 -6.392 1.00 19.53 ? 7 PHE B CA 1 ATOM 1528 C C . PHE B 2 9 ? 42.771 41.132 -5.968 1.00 20.83 ? 7 PHE B C 1 ATOM 1529 O O . PHE B 2 9 ? 43.144 40.851 -4.829 1.00 21.26 ? 7 PHE B O 1 ATOM 1530 C CB . PHE B 2 9 ? 43.957 43.275 -6.517 1.00 14.03 ? 7 PHE B CB 1 ATOM 1531 C CG . PHE B 2 9 ? 43.859 44.763 -6.721 1.00 15.23 ? 7 PHE B CG 1 ATOM 1532 C CD1 . PHE B 2 9 ? 43.806 45.301 -7.997 1.00 15.40 ? 7 PHE B CD1 1 ATOM 1533 C CD2 . PHE B 2 9 ? 43.815 45.624 -5.634 1.00 16.36 ? 7 PHE B CD2 1 ATOM 1534 C CE1 . PHE B 2 9 ? 43.714 46.670 -8.185 1.00 20.15 ? 7 PHE B CE1 1 ATOM 1535 C CE2 . PHE B 2 9 ? 43.721 46.994 -5.814 1.00 18.78 ? 7 PHE B CE2 1 ATOM 1536 C CZ . PHE B 2 9 ? 43.671 47.518 -7.090 1.00 20.43 ? 7 PHE B CZ 1 ATOM 1537 N N . LEU B 2 10 ? 42.501 40.213 -6.886 1.00 20.56 ? 8 LEU B N 1 ATOM 1538 C CA . LEU B 2 10 ? 42.472 38.799 -6.545 1.00 17.44 ? 8 LEU B CA 1 ATOM 1539 C C . LEU B 2 10 ? 43.400 37.988 -7.438 1.00 17.18 ? 8 LEU B C 1 ATOM 1540 O O . LEU B 2 10 ? 43.374 38.118 -8.662 1.00 20.43 ? 8 LEU B O 1 ATOM 1541 C CB . LEU B 2 10 ? 41.046 38.263 -6.685 1.00 15.77 ? 8 LEU B CB 1 ATOM 1542 C CG . LEU B 2 10 ? 40.857 36.771 -6.398 1.00 14.53 ? 8 LEU B CG 1 ATOM 1543 C CD1 . LEU B 2 10 ? 41.003 36.490 -4.907 1.00 13.48 ? 8 LEU B CD1 1 ATOM 1544 C CD2 . LEU B 2 10 ? 39.507 36.288 -6.909 1.00 12.43 ? 8 LEU B CD2 1 ATOM 1545 N N . GLU B 2 11 ? 44.213 37.146 -6.809 1.00 11.58 ? 9 GLU B N 1 ATOM 1546 C CA . GLU B 2 11 ? 45.021 36.173 -7.526 1.00 12.63 ? 9 GLU B CA 1 ATOM 1547 C C . GLU B 2 11 ? 44.485 34.784 -7.211 1.00 12.50 ? 9 GLU B C 1 ATOM 1548 O O . GLU B 2 11 ? 44.216 34.469 -6.054 1.00 10.07 ? 9 GLU B O 1 ATOM 1549 C CB . GLU B 2 11 ? 46.478 36.271 -7.068 1.00 15.23 ? 9 GLU B CB 1 ATOM 1550 C CG . GLU B 2 11 ? 47.410 35.227 -7.661 1.00 15.50 ? 9 GLU B CG 1 ATOM 1551 C CD . GLU B 2 11 ? 47.867 35.583 -9.060 1.00 20.50 ? 9 GLU B CD 1 ATOM 1552 O OE1 . GLU B 2 11 ? 47.613 36.726 -9.495 1.00 15.75 ? 9 GLU B OE1 1 ATOM 1553 O OE2 . GLU B 2 11 ? 48.493 34.726 -9.719 1.00 25.34 ? 9 GLU B OE2 1 ATOM 1554 N N . GLN B 2 12 ? 44.327 33.955 -8.237 1.00 11.30 ? 10 GLN B N 1 ATOM 1555 C CA . GLN B 2 12 ? 43.967 32.560 -8.024 1.00 14.12 ? 10 GLN B CA 1 ATOM 1556 C C . GLN B 2 12 ? 44.938 31.631 -8.727 1.00 15.73 ? 10 GLN B C 1 ATOM 1557 O O . GLN B 2 12 ? 45.503 31.970 -9.767 1.00 14.73 ? 10 GLN B O 1 ATOM 1558 C CB . GLN B 2 12 ? 42.561 32.252 -8.543 1.00 15.53 ? 10 GLN B CB 1 ATOM 1559 C CG . GLN B 2 12 ? 41.455 33.153 -8.025 1.00 15.29 ? 10 GLN B CG 1 ATOM 1560 C CD . GLN B 2 12 ? 40.078 32.644 -8.409 1.00 13.17 ? 10 GLN B CD 1 ATOM 1561 O OE1 . GLN B 2 12 ? 39.674 31.551 -8.010 1.00 16.48 ? 10 GLN B OE1 1 ATOM 1562 N NE2 . GLN B 2 12 ? 39.354 33.432 -9.196 1.00 9.21 ? 10 GLN B NE2 1 ATOM 1563 N N . VAL B 2 13 ? 45.127 30.454 -8.144 1.00 11.41 ? 11 VAL B N 1 ATOM 1564 C CA . VAL B 2 13 ? 45.872 29.387 -8.791 1.00 11.14 ? 11 VAL B CA 1 ATOM 1565 C C . VAL B 2 13 ? 45.079 28.096 -8.658 1.00 12.53 ? 11 VAL B C 1 ATOM 1566 O O . VAL B 2 13 ? 44.581 27.774 -7.578 1.00 12.34 ? 11 VAL B O 1 ATOM 1567 C CB . VAL B 2 13 ? 47.265 29.189 -8.161 1.00 7.95 ? 11 VAL B CB 1 ATOM 1568 C CG1 . VAL B 2 13 ? 48.061 28.174 -8.961 1.00 11.58 ? 11 VAL B CG1 1 ATOM 1569 C CG2 . VAL B 2 13 ? 48.017 30.509 -8.079 1.00 8.28 ? 11 VAL B CG2 1 ATOM 1570 N N . LYS B 2 14 ? 44.961 27.353 -9.751 1.00 12.74 ? 12 LYS B N 1 ATOM 1571 C CA . LYS B 2 14 ? 44.308 26.054 -9.704 1.00 13.55 ? 12 LYS B CA 1 ATOM 1572 C C . LYS B 2 14 ? 45.184 24.991 -10.351 1.00 13.96 ? 12 LYS B C 1 ATOM 1573 O O . LYS B 2 14 ? 45.468 25.047 -11.548 1.00 12.78 ? 12 LYS B O 1 ATOM 1574 C CB . LYS B 2 14 ? 42.949 26.117 -10.406 1.00 11.12 ? 12 LYS B CB 1 ATOM 1575 C CG . LYS B 2 14 ? 41.942 27.039 -9.731 1.00 11.69 ? 12 LYS B CG 1 ATOM 1576 C CD . LYS B 2 14 ? 40.614 27.063 -10.474 1.00 12.24 ? 12 LYS B CD 1 ATOM 1577 C CE . LYS B 2 14 ? 39.598 27.935 -9.748 1.00 12.67 ? 12 LYS B CE 1 ATOM 1578 N NZ . LYS B 2 14 ? 38.287 27.975 -10.453 1.00 7.88 ? 12 LYS B NZ 1 ATOM 1579 N N . HIS B 2 15 ? 45.600 24.017 -9.549 1.00 15.20 ? 13 HIS B N 1 ATOM 1580 C CA . HIS B 2 15 ? 46.398 22.912 -10.048 1.00 14.35 ? 13 HIS B CA 1 ATOM 1581 C C . HIS B 2 15 ? 45.453 21.739 -10.226 1.00 12.76 ? 13 HIS B C 1 ATOM 1582 O O . HIS B 2 15 ? 44.984 21.155 -9.248 1.00 15.70 ? 13 HIS B O 1 ATOM 1583 C CB . HIS B 2 15 ? 47.484 22.536 -9.040 1.00 8.56 ? 13 HIS B CB 1 ATOM 1584 C CG . HIS B 2 15 ? 48.165 23.711 -8.409 1.00 14.93 ? 13 HIS B CG 1 ATOM 1585 N ND1 . HIS B 2 15 ? 49.309 24.278 -8.927 1.00 16.91 ? 13 HIS B ND1 1 ATOM 1586 C CD2 . HIS B 2 15 ? 47.864 24.422 -7.297 1.00 15.09 ? 13 HIS B CD2 1 ATOM 1587 C CE1 . HIS B 2 15 ? 49.684 25.286 -8.161 1.00 15.99 ? 13 HIS B CE1 1 ATOM 1588 N NE2 . HIS B 2 15 ? 48.823 25.396 -7.166 1.00 13.76 ? 13 HIS B NE2 1 ATOM 1589 N N . GLU B 2 16 ? 45.174 21.391 -11.478 1.00 13.74 ? 14 GLU B N 1 ATOM 1590 C CA . GLU B 2 16 ? 44.100 20.450 -11.770 1.00 15.50 ? 14 GLU B CA 1 ATOM 1591 C C . GLU B 2 16 ? 44.626 19.114 -12.281 1.00 18.32 ? 14 GLU B C 1 ATOM 1592 O O . GLU B 2 16 ? 45.528 19.068 -13.119 1.00 19.66 ? 14 GLU B O 1 ATOM 1593 C CB . GLU B 2 16 ? 43.144 21.041 -12.809 1.00 14.44 ? 14 GLU B CB 1 ATOM 1594 C CG . GLU B 2 16 ? 42.617 22.428 -12.466 1.00 15.28 ? 14 GLU B CG 1 ATOM 1595 C CD . GLU B 2 16 ? 41.555 22.902 -13.440 1.00 16.03 ? 14 GLU B CD 1 ATOM 1596 O OE1 . GLU B 2 16 ? 41.331 22.209 -14.456 1.00 19.58 ? 14 GLU B OE1 1 ATOM 1597 O OE2 . GLU B 2 16 ? 40.937 23.958 -13.188 1.00 19.18 ? 14 GLU B OE2 1 ATOM 1598 N N . CYS B 2 17 ? 44.049 18.030 -11.774 1.00 18.50 ? 15 CYS B N 1 ATOM 1599 C CA . CYS B 2 17 ? 44.369 16.693 -12.253 1.00 16.89 ? 15 CYS B CA 1 ATOM 1600 C C . CYS B 2 17 ? 43.105 16.051 -12.806 1.00 14.68 ? 15 CYS B C 1 ATOM 1601 O O . CYS B 2 17 ? 42.120 15.882 -12.087 1.00 14.53 ? 15 CYS B O 1 ATOM 1602 C CB . CYS B 2 17 ? 44.930 15.841 -11.116 1.00 12.66 ? 15 CYS B CB 1 ATOM 1603 S SG . CYS B 2 17 ? 46.553 16.367 -10.524 1.00 22.86 ? 15 CYS B SG 1 ATOM 1604 N N . HIS B 2 18 ? 43.139 15.692 -14.084 1.00 14.29 ? 16 HIS B N 1 ATOM 1605 C CA . HIS B 2 18 ? 41.981 15.105 -14.744 1.00 16.01 ? 16 HIS B CA 1 ATOM 1606 C C . HIS B 2 18 ? 42.219 13.633 -15.044 1.00 18.03 ? 16 HIS B C 1 ATOM 1607 O O . HIS B 2 18 ? 43.219 13.272 -15.664 1.00 19.63 ? 16 HIS B O 1 ATOM 1608 C CB . HIS B 2 18 ? 41.678 15.860 -16.039 1.00 15.13 ? 16 HIS B CB 1 ATOM 1609 C CG . HIS B 2 18 ? 41.310 17.295 -15.832 1.00 18.52 ? 16 HIS B CG 1 ATOM 1610 N ND1 . HIS B 2 18 ? 40.032 17.771 -16.026 1.00 23.42 ? 16 HIS B ND1 1 ATOM 1611 C CD2 . HIS B 2 18 ? 42.054 18.361 -15.454 1.00 15.60 ? 16 HIS B CD2 1 ATOM 1612 C CE1 . HIS B 2 18 ? 40.004 19.068 -15.774 1.00 20.49 ? 16 HIS B CE1 1 ATOM 1613 N NE2 . HIS B 2 18 ? 41.218 19.451 -15.424 1.00 13.90 ? 16 HIS B NE2 1 ATOM 1614 N N . PHE B 2 19 ? 41.300 12.782 -14.602 1.00 17.08 ? 17 PHE B N 1 ATOM 1615 C CA . PHE B 2 19 ? 41.507 11.345 -14.703 1.00 19.68 ? 17 PHE B CA 1 ATOM 1616 C C . PHE B 2 19 ? 40.505 10.685 -15.642 1.00 20.25 ? 17 PHE B C 1 ATOM 1617 O O . PHE B 2 19 ? 39.305 10.954 -15.595 1.00 23.54 ? 17 PHE B O 1 ATOM 1618 C CB . PHE B 2 19 ? 41.418 10.697 -13.320 1.00 20.52 ? 17 PHE B CB 1 ATOM 1619 C CG . PHE B 2 19 ? 42.409 11.243 -12.330 1.00 23.01 ? 17 PHE B CG 1 ATOM 1620 C CD1 . PHE B 2 19 ? 42.095 12.332 -11.533 1.00 21.91 ? 17 PHE B CD1 1 ATOM 1621 C CD2 . PHE B 2 19 ? 43.664 10.670 -12.208 1.00 22.69 ? 17 PHE B CD2 1 ATOM 1622 C CE1 . PHE B 2 19 ? 43.013 12.831 -10.624 1.00 21.31 ? 17 PHE B CE1 1 ATOM 1623 C CE2 . PHE B 2 19 ? 44.585 11.165 -11.304 1.00 23.36 ? 17 PHE B CE2 1 ATOM 1624 C CZ . PHE B 2 19 ? 44.259 12.246 -10.511 1.00 22.18 ? 17 PHE B CZ 1 ATOM 1625 N N . PHE B 2 20 ? 41.026 9.806 -16.489 1.00 23.06 ? 18 PHE B N 1 ATOM 1626 C CA . PHE B 2 20 ? 40.231 9.068 -17.457 1.00 31.52 ? 18 PHE B CA 1 ATOM 1627 C C . PHE B 2 20 ? 40.568 7.598 -17.296 1.00 31.92 ? 18 PHE B C 1 ATOM 1628 O O . PHE B 2 20 ? 41.744 7.235 -17.332 1.00 31.09 ? 18 PHE B O 1 ATOM 1629 C CB . PHE B 2 20 ? 40.567 9.497 -18.890 1.00 36.85 ? 18 PHE B CB 1 ATOM 1630 C CG . PHE B 2 20 ? 40.582 10.987 -19.109 1.00 40.60 ? 18 PHE B CG 1 ATOM 1631 C CD1 . PHE B 2 20 ? 41.665 11.755 -18.706 1.00 39.63 ? 18 PHE B CD1 1 ATOM 1632 C CD2 . PHE B 2 20 ? 39.534 11.614 -19.764 1.00 43.00 ? 18 PHE B CD2 1 ATOM 1633 C CE1 . PHE B 2 20 ? 41.685 13.122 -18.917 1.00 36.04 ? 18 PHE B CE1 1 ATOM 1634 C CE2 . PHE B 2 20 ? 39.551 12.980 -19.984 1.00 41.57 ? 18 PHE B CE2 1 ATOM 1635 C CZ . PHE B 2 20 ? 40.629 13.735 -19.558 1.00 37.13 ? 18 PHE B CZ 1 ATOM 1636 N N . ASN B 2 21 ? 39.552 6.758 -17.112 1.00 36.50 ? 19 ASN B N 1 ATOM 1637 C CA . ASN B 2 21 ? 39.775 5.323 -16.969 1.00 41.12 ? 19 ASN B CA 1 ATOM 1638 C C . ASN B 2 21 ? 40.737 4.987 -15.825 1.00 37.65 ? 19 ASN B C 1 ATOM 1639 O O . ASN B 2 21 ? 41.818 4.444 -16.045 1.00 38.27 ? 19 ASN B O 1 ATOM 1640 C CB . ASN B 2 21 ? 40.290 4.769 -18.305 1.00 50.17 ? 19 ASN B CB 1 ATOM 1641 C CG . ASN B 2 21 ? 40.430 3.260 -18.324 1.00 58.60 ? 19 ASN B CG 1 ATOM 1642 O OD1 . ASN B 2 21 ? 40.001 2.562 -17.407 1.00 55.81 ? 19 ASN B OD1 1 ATOM 1643 N ND2 . ASN B 2 21 ? 41.059 2.753 -19.383 1.00 69.97 ? 19 ASN B ND2 1 ATOM 1644 N N . GLY B 2 22 ? 40.336 5.315 -14.600 1.00 34.46 ? 20 GLY B N 1 ATOM 1645 C CA . GLY B 2 22 ? 41.219 5.173 -13.457 1.00 33.33 ? 20 GLY B CA 1 ATOM 1646 C C . GLY B 2 22 ? 42.367 6.158 -13.553 1.00 34.12 ? 20 GLY B C 1 ATOM 1647 O O . GLY B 2 22 ? 42.152 7.364 -13.666 1.00 35.38 ? 20 GLY B O 1 ATOM 1648 N N . THR B 2 23 ? 43.591 5.642 -13.506 1.00 32.72 ? 21 THR B N 1 ATOM 1649 C CA . THR B 2 23 ? 44.774 6.472 -13.693 1.00 28.61 ? 21 THR B CA 1 ATOM 1650 C C . THR B 2 23 ? 45.477 6.139 -15.007 1.00 29.57 ? 21 THR B C 1 ATOM 1651 O O . THR B 2 23 ? 46.648 6.467 -15.191 1.00 27.36 ? 21 THR B O 1 ATOM 1652 C CB . THR B 2 23 ? 45.776 6.295 -12.538 1.00 27.85 ? 21 THR B CB 1 ATOM 1653 O OG1 . THR B 2 23 ? 46.025 4.900 -12.325 1.00 26.09 ? 21 THR B OG1 1 ATOM 1654 C CG2 . THR B 2 23 ? 45.226 6.906 -11.258 1.00 29.76 ? 21 THR B CG2 1 ATOM 1655 N N . GLU B 2 24 ? 44.756 5.488 -15.916 1.00 30.38 ? 22 GLU B N 1 ATOM 1656 C CA . GLU B 2 24 ? 45.322 5.073 -17.199 1.00 33.89 ? 22 GLU B CA 1 ATOM 1657 C C . GLU B 2 24 ? 45.690 6.266 -18.076 1.00 31.86 ? 22 GLU B C 1 ATOM 1658 O O . GLU B 2 24 ? 46.737 6.270 -18.724 1.00 29.44 ? 22 GLU B O 1 ATOM 1659 C CB . GLU B 2 24 ? 44.333 4.176 -17.943 1.00 41.67 ? 22 GLU B CB 1 ATOM 1660 C CG . GLU B 2 24 ? 44.352 2.725 -17.489 1.00 48.89 ? 22 GLU B CG 1 ATOM 1661 C CD . GLU B 2 24 ? 45.645 2.020 -17.855 1.00 55.08 ? 22 GLU B CD 1 ATOM 1662 O OE1 . GLU B 2 24 ? 45.930 1.889 -19.064 1.00 56.41 ? 22 GLU B OE1 1 ATOM 1663 O OE2 . GLU B 2 24 ? 46.376 1.599 -16.935 1.00 56.45 ? 22 GLU B OE2 1 ATOM 1664 N N . ARG B 2 25 ? 44.825 7.276 -18.091 1.00 32.64 ? 23 ARG B N 1 ATOM 1665 C CA . ARG B 2 25 ? 45.093 8.501 -18.834 1.00 35.08 ? 23 ARG B CA 1 ATOM 1666 C C . ARG B 2 25 ? 44.893 9.680 -17.880 1.00 33.06 ? 23 ARG B C 1 ATOM 1667 O O . ARG B 2 25 ? 43.839 9.812 -17.258 1.00 32.64 ? 23 ARG B O 1 ATOM 1668 C CB . ARG B 2 25 ? 44.177 8.587 -20.061 1.00 42.93 ? 23 ARG B CB 1 ATOM 1669 C CG . ARG B 2 25 ? 43.966 9.960 -20.682 1.00 53.04 ? 23 ARG B CG 1 ATOM 1670 C CD . ARG B 2 25 ? 45.267 10.579 -21.171 1.00 61.38 ? 23 ARG B CD 1 ATOM 1671 N NE . ARG B 2 25 ? 45.025 11.839 -21.868 1.00 64.83 ? 23 ARG B NE 1 ATOM 1672 C CZ . ARG B 2 25 ? 45.926 12.805 -22.016 1.00 63.11 ? 23 ARG B CZ 1 ATOM 1673 N NH1 . ARG B 2 25 ? 47.147 12.663 -21.519 1.00 59.90 ? 23 ARG B NH1 1 ATOM 1674 N NH2 . ARG B 2 25 ? 45.606 13.914 -22.670 1.00 61.43 ? 23 ARG B NH2 1 ATOM 1675 N N . VAL B 2 26 ? 45.906 10.535 -17.772 1.00 29.07 ? 24 VAL B N 1 ATOM 1676 C CA . VAL B 2 26 ? 45.881 11.653 -16.830 1.00 26.25 ? 24 VAL B CA 1 ATOM 1677 C C . VAL B 2 26 ? 46.354 12.959 -17.466 1.00 22.23 ? 24 VAL B C 1 ATOM 1678 O O . VAL B 2 26 ? 47.330 12.976 -18.215 1.00 20.67 ? 24 VAL B O 1 ATOM 1679 C CB . VAL B 2 26 ? 46.785 11.359 -15.607 1.00 26.18 ? 24 VAL B CB 1 ATOM 1680 C CG1 . VAL B 2 26 ? 46.745 12.510 -14.616 1.00 24.71 ? 24 VAL B CG1 1 ATOM 1681 C CG2 . VAL B 2 26 ? 46.367 10.065 -14.923 1.00 26.99 ? 24 VAL B CG2 1 ATOM 1682 N N . ARG B 2 27 ? 45.658 14.051 -17.160 1.00 19.34 ? 25 ARG B N 1 ATOM 1683 C CA . ARG B 2 27 ? 46.055 15.374 -17.629 1.00 19.53 ? 25 ARG B CA 1 ATOM 1684 C C . ARG B 2 27 ? 46.226 16.346 -16.466 1.00 17.49 ? 25 ARG B C 1 ATOM 1685 O O . ARG B 2 27 ? 45.399 16.394 -15.555 1.00 17.32 ? 25 ARG B O 1 ATOM 1686 C CB . ARG B 2 27 ? 45.005 15.919 -18.597 1.00 22.40 ? 25 ARG B CB 1 ATOM 1687 C CG . ARG B 2 27 ? 45.348 17.264 -19.216 1.00 22.59 ? 25 ARG B CG 1 ATOM 1688 C CD . ARG B 2 27 ? 44.383 17.605 -20.340 1.00 25.50 ? 25 ARG B CD 1 ATOM 1689 N NE . ARG B 2 27 ? 44.557 18.972 -20.824 1.00 34.93 ? 25 ARG B NE 1 ATOM 1690 C CZ . ARG B 2 27 ? 43.831 19.517 -21.794 1.00 44.36 ? 25 ARG B CZ 1 ATOM 1691 N NH1 . ARG B 2 27 ? 42.878 18.810 -22.387 1.00 51.27 ? 25 ARG B NH1 1 ATOM 1692 N NH2 . ARG B 2 27 ? 44.054 20.768 -22.171 1.00 44.92 ? 25 ARG B NH2 1 ATOM 1693 N N . PHE B 2 28 ? 47.315 17.108 -16.497 1.00 16.55 ? 26 PHE B N 1 ATOM 1694 C CA . PHE B 2 28 ? 47.620 18.058 -15.434 1.00 15.13 ? 26 PHE B CA 1 ATOM 1695 C C . PHE B 2 28 ? 47.580 19.478 -15.982 1.00 16.95 ? 26 PHE B C 1 ATOM 1696 O O . PHE B 2 28 ? 48.190 19.777 -17.009 1.00 22.17 ? 26 PHE B O 1 ATOM 1697 C CB . PHE B 2 28 ? 48.999 17.768 -14.840 1.00 15.56 ? 26 PHE B CB 1 ATOM 1698 C CG . PHE B 2 28 ? 49.533 18.886 -13.991 1.00 10.06 ? 26 PHE B CG 1 ATOM 1699 C CD1 . PHE B 2 28 ? 48.948 19.179 -12.767 1.00 13.83 ? 26 PHE B CD1 1 ATOM 1700 C CD2 . PHE B 2 28 ? 50.612 19.646 -14.411 1.00 10.49 ? 26 PHE B CD2 1 ATOM 1701 C CE1 . PHE B 2 28 ? 49.428 20.209 -11.978 1.00 12.57 ? 26 PHE B CE1 1 ATOM 1702 C CE2 . PHE B 2 28 ? 51.100 20.679 -13.625 1.00 10.75 ? 26 PHE B CE2 1 ATOM 1703 C CZ . PHE B 2 28 ? 50.506 20.961 -12.408 1.00 10.90 ? 26 PHE B CZ 1 ATOM 1704 N N . LEU B 2 29 ? 46.862 20.354 -15.289 1.00 16.25 ? 27 LEU B N 1 ATOM 1705 C CA . LEU B 2 29 ? 46.818 21.761 -15.664 1.00 14.77 ? 27 LEU B CA 1 ATOM 1706 C C . LEU B 2 29 ? 47.247 22.666 -14.521 1.00 13.89 ? 27 LEU B C 1 ATOM 1707 O O . LEU B 2 29 ? 46.690 22.608 -13.425 1.00 15.97 ? 27 LEU B O 1 ATOM 1708 C CB . LEU B 2 29 ? 45.396 22.148 -16.072 1.00 16.01 ? 27 LEU B CB 1 ATOM 1709 C CG . LEU B 2 29 ? 44.769 21.425 -17.263 1.00 17.94 ? 27 LEU B CG 1 ATOM 1710 C CD1 . LEU B 2 29 ? 43.372 21.964 -17.530 1.00 16.50 ? 27 LEU B CD1 1 ATOM 1711 C CD2 . LEU B 2 29 ? 45.643 21.560 -18.495 1.00 18.36 ? 27 LEU B CD2 1 ATOM 1712 N N . ASP B 2 30 ? 48.243 23.503 -14.783 1.00 11.45 ? 28 ASP B N 1 ATOM 1713 C CA . ASP B 2 30 ? 48.696 24.468 -13.798 1.00 12.00 ? 28 ASP B CA 1 ATOM 1714 C C . ASP B 2 30 ? 48.182 25.806 -14.302 1.00 12.24 ? 28 ASP B C 1 ATOM 1715 O O . ASP B 2 30 ? 48.692 26.336 -15.286 1.00 10.11 ? 28 ASP B O 1 ATOM 1716 C CB . ASP B 2 30 ? 50.223 24.477 -13.736 1.00 11.28 ? 28 ASP B CB 1 ATOM 1717 C CG . ASP B 2 30 ? 50.753 24.841 -12.362 1.00 17.48 ? 28 ASP B CG 1 ATOM 1718 O OD1 . ASP B 2 30 ? 50.174 24.382 -11.357 1.00 17.08 ? 28 ASP B OD1 1 ATOM 1719 O OD2 . ASP B 2 30 ? 51.760 25.578 -12.290 1.00 16.64 ? 28 ASP B OD2 1 ATOM 1720 N N . ARG B 2 31 ? 47.186 26.363 -13.619 1.00 11.90 ? 29 ARG B N 1 ATOM 1721 C CA . ARG B 2 31 ? 46.432 27.494 -14.158 1.00 10.71 ? 29 ARG B CA 1 ATOM 1722 C C . ARG B 2 31 ? 46.544 28.686 -13.229 1.00 11.66 ? 29 ARG B C 1 ATOM 1723 O O . ARG B 2 31 ? 46.358 28.565 -12.019 1.00 11.65 ? 29 ARG B O 1 ATOM 1724 C CB . ARG B 2 31 ? 44.966 27.118 -14.346 1.00 15.71 ? 29 ARG B CB 1 ATOM 1725 C CG . ARG B 2 31 ? 44.745 25.804 -15.064 1.00 13.91 ? 29 ARG B CG 1 ATOM 1726 C CD . ARG B 2 31 ? 43.266 25.484 -15.129 1.00 9.98 ? 29 ARG B CD 1 ATOM 1727 N NE . ARG B 2 31 ? 42.576 26.406 -16.026 1.00 10.21 ? 29 ARG B NE 1 ATOM 1728 C CZ . ARG B 2 31 ? 41.256 26.493 -16.146 1.00 11.81 ? 29 ARG B CZ 1 ATOM 1729 N NH1 . ARG B 2 31 ? 40.468 25.719 -15.413 1.00 8.14 ? 29 ARG B NH1 1 ATOM 1730 N NH2 . ARG B 2 31 ? 40.721 27.358 -16.998 1.00 8.46 ? 29 ARG B NH2 1 ATOM 1731 N N . TYR B 2 32 ? 46.849 29.845 -13.799 1.00 13.43 ? 30 TYR B N 1 ATOM 1732 C CA . TYR B 2 32 ? 46.972 31.047 -12.992 1.00 13.09 ? 30 TYR B CA 1 ATOM 1733 C C . TYR B 2 32 ? 45.932 32.100 -13.388 1.00 13.54 ? 30 TYR B C 1 ATOM 1734 O O . TYR B 2 32 ? 45.689 32.313 -14.576 1.00 12.31 ? 30 TYR B O 1 ATOM 1735 C CB . TYR B 2 32 ? 48.387 31.603 -13.135 1.00 13.74 ? 30 TYR B CB 1 ATOM 1736 C CG . TYR B 2 32 ? 49.390 30.730 -12.413 1.00 15.61 ? 30 TYR B CG 1 ATOM 1737 C CD1 . TYR B 2 32 ? 49.767 29.508 -12.963 1.00 13.21 ? 30 TYR B CD1 1 ATOM 1738 C CD2 . TYR B 2 32 ? 49.922 31.084 -11.182 1.00 18.10 ? 30 TYR B CD2 1 ATOM 1739 C CE1 . TYR B 2 32 ? 50.662 28.680 -12.334 1.00 17.11 ? 30 TYR B CE1 1 ATOM 1740 C CE2 . TYR B 2 32 ? 50.825 30.250 -10.537 1.00 17.00 ? 30 TYR B CE2 1 ATOM 1741 C CZ . TYR B 2 32 ? 51.189 29.052 -11.122 1.00 17.95 ? 30 TYR B CZ 1 ATOM 1742 O OH . TYR B 2 32 ? 52.081 28.211 -10.498 1.00 18.27 ? 30 TYR B OH 1 ATOM 1743 N N . PHE B 2 33 ? 45.315 32.751 -12.403 1.00 9.48 ? 31 PHE B N 1 ATOM 1744 C CA . PHE B 2 33 ? 44.220 33.676 -12.681 1.00 8.93 ? 31 PHE B CA 1 ATOM 1745 C C . PHE B 2 33 ? 44.406 35.018 -11.984 1.00 11.35 ? 31 PHE B C 1 ATOM 1746 O O . PHE B 2 33 ? 44.873 35.084 -10.848 1.00 15.35 ? 31 PHE B O 1 ATOM 1747 C CB . PHE B 2 33 ? 42.882 33.101 -12.198 1.00 11.43 ? 31 PHE B CB 1 ATOM 1748 C CG . PHE B 2 33 ? 42.588 31.721 -12.697 1.00 8.48 ? 31 PHE B CG 1 ATOM 1749 C CD1 . PHE B 2 33 ? 43.142 30.610 -12.080 1.00 7.29 ? 31 PHE B CD1 1 ATOM 1750 C CD2 . PHE B 2 33 ? 41.751 31.533 -13.778 1.00 8.84 ? 31 PHE B CD2 1 ATOM 1751 C CE1 . PHE B 2 33 ? 42.866 29.340 -12.540 1.00 14.18 ? 31 PHE B CE1 1 ATOM 1752 C CE2 . PHE B 2 33 ? 41.475 30.269 -14.243 1.00 9.23 ? 31 PHE B CE2 1 ATOM 1753 C CZ . PHE B 2 33 ? 42.031 29.169 -13.623 1.00 9.77 ? 31 PHE B CZ 1 ATOM 1754 N N . TYR B 2 34 ? 44.043 36.088 -12.683 1.00 11.89 ? 32 TYR B N 1 ATOM 1755 C CA . TYR B 2 34 ? 43.940 37.414 -12.090 1.00 12.29 ? 32 TYR B CA 1 ATOM 1756 C C . TYR B 2 34 ? 42.484 37.840 -12.151 1.00 11.54 ? 32 TYR B C 1 ATOM 1757 O O . TYR B 2 34 ? 41.942 38.003 -13.242 1.00 9.94 ? 32 TYR B O 1 ATOM 1758 C CB . TYR B 2 34 ? 44.835 38.403 -12.841 1.00 10.11 ? 32 TYR B CB 1 ATOM 1759 C CG . TYR B 2 34 ? 44.804 39.812 -12.294 1.00 13.39 ? 32 TYR B CG 1 ATOM 1760 C CD1 . TYR B 2 34 ? 45.274 40.088 -11.018 1.00 11.11 ? 32 TYR B CD1 1 ATOM 1761 C CD2 . TYR B 2 34 ? 44.350 40.873 -13.069 1.00 11.66 ? 32 TYR B CD2 1 ATOM 1762 C CE1 . TYR B 2 34 ? 45.270 41.375 -10.514 1.00 12.02 ? 32 TYR B CE1 1 ATOM 1763 C CE2 . TYR B 2 34 ? 44.343 42.169 -12.572 1.00 13.90 ? 32 TYR B CE2 1 ATOM 1764 C CZ . TYR B 2 34 ? 44.803 42.413 -11.295 1.00 14.54 ? 32 TYR B CZ 1 ATOM 1765 O OH . TYR B 2 34 ? 44.803 43.693 -10.789 1.00 15.99 ? 32 TYR B OH 1 ATOM 1766 N N . HIS B 2 35 ? 41.856 38.020 -10.990 1.00 14.32 ? 33 HIS B N 1 ATOM 1767 C CA . HIS B 2 35 ? 40.394 38.104 -10.906 1.00 17.20 ? 33 HIS B CA 1 ATOM 1768 C C . HIS B 2 35 ? 39.739 36.823 -11.433 1.00 20.41 ? 33 HIS B C 1 ATOM 1769 O O . HIS B 2 35 ? 39.908 35.756 -10.849 1.00 22.69 ? 33 HIS B O 1 ATOM 1770 C CB . HIS B 2 35 ? 39.867 39.352 -11.618 1.00 16.48 ? 33 HIS B CB 1 ATOM 1771 C CG . HIS B 2 35 ? 40.560 40.616 -11.215 1.00 19.00 ? 33 HIS B CG 1 ATOM 1772 N ND1 . HIS B 2 35 ? 41.124 40.788 -9.969 1.00 16.77 ? 33 HIS B ND1 1 ATOM 1773 C CD2 . HIS B 2 35 ? 40.777 41.769 -11.891 1.00 20.38 ? 33 HIS B CD2 1 ATOM 1774 C CE1 . HIS B 2 35 ? 41.662 41.991 -9.896 1.00 18.47 ? 33 HIS B CE1 1 ATOM 1775 N NE2 . HIS B 2 35 ? 41.465 42.607 -11.048 1.00 20.14 ? 33 HIS B NE2 1 ATOM 1776 N N . GLN B 2 36 ? 39.006 36.931 -12.536 1.00 21.54 ? 34 GLN B N 1 ATOM 1777 C CA . GLN B 2 36 ? 38.413 35.759 -13.168 1.00 21.83 ? 34 GLN B CA 1 ATOM 1778 C C . GLN B 2 36 ? 39.169 35.346 -14.420 1.00 23.82 ? 34 GLN B C 1 ATOM 1779 O O . GLN B 2 36 ? 38.861 34.325 -15.037 1.00 27.73 ? 34 GLN B O 1 ATOM 1780 C CB . GLN B 2 36 ? 36.941 36.004 -13.535 1.00 25.73 ? 34 GLN B CB 1 ATOM 1781 C CG . GLN B 2 36 ? 35.983 36.180 -12.388 1.00 33.25 ? 34 GLN B CG 1 ATOM 1782 C CD . GLN B 2 36 ? 34.690 36.823 -12.872 1.00 42.53 ? 34 GLN B CD 1 ATOM 1783 O OE1 . GLN B 2 36 ? 33.878 36.182 -13.540 1.00 47.49 ? 34 GLN B OE1 1 ATOM 1784 N NE2 . GLN B 2 36 ? 34.495 38.095 -12.538 1.00 44.43 ? 34 GLN B NE2 1 ATOM 1785 N N . GLU B 2 37 ? 40.166 36.142 -14.778 1.00 23.77 ? 35 GLU B N 1 ATOM 1786 C CA . GLU B 2 37 ? 40.895 35.949 -16.023 1.00 22.96 ? 35 GLU B CA 1 ATOM 1787 C C . GLU B 2 37 ? 42.082 35.001 -15.942 1.00 17.79 ? 35 GLU B C 1 ATOM 1788 O O . GLU B 2 37 ? 43.085 35.317 -15.305 1.00 17.51 ? 35 GLU B O 1 ATOM 1789 C CB . GLU B 2 37 ? 41.382 37.319 -16.514 1.00 28.73 ? 35 GLU B CB 1 ATOM 1790 C CG . GLU B 2 37 ? 42.387 37.302 -17.637 1.00 37.17 ? 35 GLU B CG 1 ATOM 1791 C CD . GLU B 2 37 ? 42.991 38.672 -17.860 1.00 41.47 ? 35 GLU B CD 1 ATOM 1792 O OE1 . GLU B 2 37 ? 44.052 38.762 -18.512 1.00 40.74 ? 35 GLU B OE1 1 ATOM 1793 O OE2 . GLU B 2 37 ? 42.412 39.661 -17.358 1.00 41.42 ? 35 GLU B OE2 1 ATOM 1794 N N . GLU B 2 38 ? 41.970 33.832 -16.569 1.00 14.72 ? 36 GLU B N 1 ATOM 1795 C CA . GLU B 2 38 ? 43.123 32.949 -16.674 1.00 15.14 ? 36 GLU B CA 1 ATOM 1796 C C . GLU B 2 38 ? 44.104 33.639 -17.608 1.00 14.29 ? 36 GLU B C 1 ATOM 1797 O O . GLU B 2 38 ? 43.744 33.983 -18.731 1.00 13.18 ? 36 GLU B O 1 ATOM 1798 C CB . GLU B 2 38 ? 42.730 31.586 -17.243 1.00 8.59 ? 36 GLU B CB 1 ATOM 1799 C CG . GLU B 2 38 ? 43.860 30.558 -17.172 1.00 8.31 ? 36 GLU B CG 1 ATOM 1800 C CD . GLU B 2 38 ? 43.453 29.187 -17.681 1.00 16.02 ? 36 GLU B CD 1 ATOM 1801 O OE1 . GLU B 2 38 ? 42.392 29.079 -18.334 1.00 16.27 ? 36 GLU B OE1 1 ATOM 1802 O OE2 . GLU B 2 38 ? 44.205 28.218 -17.447 1.00 12.13 ? 36 GLU B OE2 1 ATOM 1803 N N . TYR B 2 39 ? 45.337 33.832 -17.159 1.00 11.53 ? 37 TYR B N 1 ATOM 1804 C CA . TYR B 2 39 ? 46.311 34.544 -17.978 1.00 13.09 ? 37 TYR B CA 1 ATOM 1805 C C . TYR B 2 39 ? 47.475 33.688 -18.485 1.00 13.10 ? 37 TYR B C 1 ATOM 1806 O O . TYR B 2 39 ? 48.098 34.017 -19.493 1.00 10.46 ? 37 TYR B O 1 ATOM 1807 C CB . TYR B 2 39 ? 46.793 35.827 -17.294 1.00 12.83 ? 37 TYR B CB 1 ATOM 1808 C CG . TYR B 2 39 ? 47.463 35.609 -15.963 1.00 15.53 ? 37 TYR B CG 1 ATOM 1809 C CD1 . TYR B 2 39 ? 48.819 35.350 -15.885 1.00 18.72 ? 37 TYR B CD1 1 ATOM 1810 C CD2 . TYR B 2 39 ? 46.737 35.678 -14.780 1.00 15.20 ? 37 TYR B CD2 1 ATOM 1811 C CE1 . TYR B 2 39 ? 49.434 35.154 -14.671 1.00 21.01 ? 37 TYR B CE1 1 ATOM 1812 C CE2 . TYR B 2 39 ? 47.348 35.488 -13.557 1.00 16.22 ? 37 TYR B CE2 1 ATOM 1813 C CZ . TYR B 2 39 ? 48.698 35.226 -13.508 1.00 19.33 ? 37 TYR B CZ 1 ATOM 1814 O OH . TYR B 2 39 ? 49.315 35.034 -12.293 1.00 23.49 ? 37 TYR B OH 1 ATOM 1815 N N . VAL B 2 40 ? 47.756 32.590 -17.790 1.00 13.71 ? 38 VAL B N 1 ATOM 1816 C CA . VAL B 2 40 ? 48.807 31.664 -18.210 1.00 15.69 ? 38 VAL B CA 1 ATOM 1817 C C . VAL B 2 40 ? 48.518 30.268 -17.656 1.00 17.59 ? 38 VAL B C 1 ATOM 1818 O O . VAL B 2 40 ? 47.913 30.125 -16.591 1.00 19.29 ? 38 VAL B O 1 ATOM 1819 C CB . VAL B 2 40 ? 50.207 32.165 -17.768 1.00 14.06 ? 38 VAL B CB 1 ATOM 1820 C CG1 . VAL B 2 40 ? 50.329 32.148 -16.256 1.00 13.86 ? 38 VAL B CG1 1 ATOM 1821 C CG2 . VAL B 2 40 ? 51.311 31.322 -18.399 1.00 16.18 ? 38 VAL B CG2 1 ATOM 1822 N N . ARG B 2 41 ? 48.942 29.240 -18.386 1.00 18.00 ? 39 ARG B N 1 ATOM 1823 C CA . ARG B 2 41 ? 48.707 27.861 -17.971 1.00 18.72 ? 39 ARG B CA 1 ATOM 1824 C C . ARG B 2 41 ? 49.780 26.887 -18.452 1.00 16.39 ? 39 ARG B C 1 ATOM 1825 O O . ARG B 2 41 ? 50.366 27.067 -19.520 1.00 11.88 ? 39 ARG B O 1 ATOM 1826 C CB . ARG B 2 41 ? 47.346 27.369 -18.471 1.00 20.00 ? 39 ARG B CB 1 ATOM 1827 C CG . ARG B 2 41 ? 47.236 27.265 -19.986 1.00 25.43 ? 39 ARG B CG 1 ATOM 1828 C CD . ARG B 2 41 ? 46.167 26.263 -20.394 1.00 26.20 ? 39 ARG B CD 1 ATOM 1829 N NE . ARG B 2 41 ? 44.847 26.602 -19.871 1.00 25.36 ? 39 ARG B NE 1 ATOM 1830 C CZ . ARG B 2 41 ? 43.726 25.987 -20.234 1.00 27.47 ? 39 ARG B CZ 1 ATOM 1831 N NH1 . ARG B 2 41 ? 43.766 25.001 -21.119 1.00 27.18 ? 39 ARG B NH1 1 ATOM 1832 N NH2 . ARG B 2 41 ? 42.565 26.356 -19.711 1.00 29.17 ? 39 ARG B NH2 1 ATOM 1833 N N . PHE B 2 42 ? 50.036 25.859 -17.647 1.00 18.70 ? 40 PHE B N 1 ATOM 1834 C CA . PHE B 2 42 ? 50.799 24.708 -18.109 1.00 14.03 ? 40 PHE B CA 1 ATOM 1835 C C . PHE B 2 42 ? 49.817 23.572 -18.364 1.00 16.14 ? 40 PHE B C 1 ATOM 1836 O O . PHE B 2 42 ? 49.059 23.177 -17.480 1.00 14.96 ? 40 PHE B O 1 ATOM 1837 C CB . PHE B 2 42 ? 51.828 24.285 -17.052 1.00 11.86 ? 40 PHE B CB 1 ATOM 1838 C CG . PHE B 2 42 ? 52.595 23.029 -17.400 1.00 16.81 ? 40 PHE B CG 1 ATOM 1839 C CD1 . PHE B 2 42 ? 52.072 21.774 -17.123 1.00 16.56 ? 40 PHE B CD1 1 ATOM 1840 C CD2 . PHE B 2 42 ? 53.852 23.108 -17.979 1.00 10.86 ? 40 PHE B CD2 1 ATOM 1841 C CE1 . PHE B 2 42 ? 52.773 20.625 -17.439 1.00 10.97 ? 40 PHE B CE1 1 ATOM 1842 C CE2 . PHE B 2 42 ? 54.560 21.962 -18.293 1.00 11.56 ? 40 PHE B CE2 1 ATOM 1843 C CZ . PHE B 2 42 ? 54.020 20.720 -18.022 1.00 11.62 ? 40 PHE B CZ 1 ATOM 1844 N N . ASP B 2 43 ? 49.844 23.049 -19.583 1.00 16.35 ? 41 ASP B N 1 ATOM 1845 C CA . ASP B 2 43 ? 49.030 21.906 -19.960 1.00 18.05 ? 41 ASP B CA 1 ATOM 1846 C C . ASP B 2 43 ? 49.992 20.754 -20.208 1.00 19.83 ? 41 ASP B C 1 ATOM 1847 O O . ASP B 2 43 ? 50.918 20.880 -21.009 1.00 22.47 ? 41 ASP B O 1 ATOM 1848 C CB . ASP B 2 43 ? 48.255 22.236 -21.239 1.00 17.46 ? 41 ASP B CB 1 ATOM 1849 C CG . ASP B 2 43 ? 47.269 21.144 -21.634 1.00 17.94 ? 41 ASP B CG 1 ATOM 1850 O OD1 . ASP B 2 43 ? 47.377 20.005 -21.130 1.00 12.18 ? 41 ASP B OD1 1 ATOM 1851 O OD2 . ASP B 2 43 ? 46.379 21.429 -22.462 1.00 21.24 ? 41 ASP B OD2 1 ATOM 1852 N N . SER B 2 44 ? 49.781 19.637 -19.518 1.00 18.80 ? 42 SER B N 1 ATOM 1853 C CA . SER B 2 44 ? 50.655 18.475 -19.670 1.00 16.26 ? 42 SER B CA 1 ATOM 1854 C C . SER B 2 44 ? 50.637 17.921 -21.096 1.00 16.94 ? 42 SER B C 1 ATOM 1855 O O . SER B 2 44 ? 51.560 17.218 -21.510 1.00 16.98 ? 42 SER B O 1 ATOM 1856 C CB . SER B 2 44 ? 50.311 17.387 -18.649 1.00 17.66 ? 42 SER B CB 1 ATOM 1857 O OG . SER B 2 44 ? 48.998 16.891 -18.848 1.00 20.84 ? 42 SER B OG 1 ATOM 1858 N N . ASP B 2 45 ? 49.582 18.242 -21.838 1.00 17.58 ? 43 ASP B N 1 ATOM 1859 C CA . ASP B 2 45 ? 49.485 17.884 -23.249 1.00 20.27 ? 43 ASP B CA 1 ATOM 1860 C C . ASP B 2 45 ? 50.543 18.607 -24.078 1.00 18.48 ? 43 ASP B C 1 ATOM 1861 O O . ASP B 2 45 ? 50.929 18.146 -25.151 1.00 15.67 ? 43 ASP B O 1 ATOM 1862 C CB . ASP B 2 45 ? 48.100 18.237 -23.794 1.00 25.95 ? 43 ASP B CB 1 ATOM 1863 C CG . ASP B 2 45 ? 47.051 17.209 -23.426 1.00 26.28 ? 43 ASP B CG 1 ATOM 1864 O OD1 . ASP B 2 45 ? 47.372 16.286 -22.648 1.00 28.08 ? 43 ASP B OD1 1 ATOM 1865 O OD2 . ASP B 2 45 ? 45.906 17.324 -23.911 1.00 26.16 ? 43 ASP B OD2 1 ATOM 1866 N N . VAL B 2 46 ? 51.012 19.741 -23.568 1.00 13.79 ? 44 VAL B N 1 ATOM 1867 C CA . VAL B 2 46 ? 51.963 20.578 -24.289 1.00 19.25 ? 44 VAL B CA 1 ATOM 1868 C C . VAL B 2 46 ? 53.374 20.445 -23.725 1.00 18.37 ? 44 VAL B C 1 ATOM 1869 O O . VAL B 2 46 ? 54.326 20.202 -24.467 1.00 15.30 ? 44 VAL B O 1 ATOM 1870 C CB . VAL B 2 46 ? 51.532 22.060 -24.256 1.00 19.22 ? 44 VAL B CB 1 ATOM 1871 C CG1 . VAL B 2 46 ? 52.609 22.940 -24.870 1.00 15.64 ? 44 VAL B CG1 1 ATOM 1872 C CG2 . VAL B 2 46 ? 50.211 22.243 -24.984 1.00 19.47 ? 44 VAL B CG2 1 ATOM 1873 N N . GLY B 2 47 ? 53.501 20.598 -22.410 1.00 15.55 ? 45 GLY B N 1 ATOM 1874 C CA . GLY B 2 47 ? 54.779 20.401 -21.753 1.00 16.99 ? 45 GLY B CA 1 ATOM 1875 C C . GLY B 2 47 ? 55.490 21.723 -21.549 1.00 19.74 ? 45 GLY B C 1 ATOM 1876 O O . GLY B 2 47 ? 56.652 21.765 -21.147 1.00 22.66 ? 45 GLY B O 1 ATOM 1877 N N . GLU B 2 48 ? 54.776 22.811 -21.821 1.00 19.79 ? 46 GLU B N 1 ATOM 1878 C CA . GLU B 2 48 ? 55.285 24.152 -21.567 1.00 19.78 ? 46 GLU B CA 1 ATOM 1879 C C . GLU B 2 48 ? 54.147 25.065 -21.146 1.00 17.51 ? 46 GLU B C 1 ATOM 1880 O O . GLU B 2 48 ? 52.977 24.755 -21.372 1.00 17.81 ? 46 GLU B O 1 ATOM 1881 C CB . GLU B 2 48 ? 55.943 24.723 -22.826 1.00 23.61 ? 46 GLU B CB 1 ATOM 1882 C CG . GLU B 2 48 ? 57.324 24.182 -23.144 1.00 28.66 ? 46 GLU B CG 1 ATOM 1883 C CD . GLU B 2 48 ? 57.930 24.853 -24.360 1.00 32.58 ? 46 GLU B CD 1 ATOM 1884 O OE1 . GLU B 2 48 ? 57.206 25.615 -25.036 1.00 29.09 ? 46 GLU B OE1 1 ATOM 1885 O OE2 . GLU B 2 48 ? 59.123 24.620 -24.643 1.00 33.71 ? 46 GLU B OE2 1 ATOM 1886 N N . TYR B 2 49 ? 54.489 26.192 -20.533 1.00 12.47 ? 47 TYR B N 1 ATOM 1887 C CA . TYR B 2 49 ? 53.498 27.215 -20.235 1.00 12.41 ? 47 TYR B CA 1 ATOM 1888 C C . TYR B 2 49 ? 53.104 27.954 -21.510 1.00 15.01 ? 47 TYR B C 1 ATOM 1889 O O . TYR B 2 49 ? 53.935 28.172 -22.392 1.00 12.91 ? 47 TYR B O 1 ATOM 1890 C CB . TYR B 2 49 ? 54.018 28.196 -19.183 1.00 10.96 ? 47 TYR B CB 1 ATOM 1891 C CG . TYR B 2 49 ? 53.976 27.655 -17.769 1.00 15.84 ? 47 TYR B CG 1 ATOM 1892 C CD1 . TYR B 2 49 ? 55.060 26.972 -17.232 1.00 13.23 ? 47 TYR B CD1 1 ATOM 1893 C CD2 . TYR B 2 49 ? 52.853 27.832 -16.967 1.00 13.87 ? 47 TYR B CD2 1 ATOM 1894 C CE1 . TYR B 2 49 ? 55.028 26.479 -15.941 1.00 12.75 ? 47 TYR B CE1 1 ATOM 1895 C CE2 . TYR B 2 49 ? 52.813 27.341 -15.673 1.00 9.37 ? 47 TYR B CE2 1 ATOM 1896 C CZ . TYR B 2 49 ? 53.902 26.666 -15.166 1.00 13.06 ? 47 TYR B CZ 1 ATOM 1897 O OH . TYR B 2 49 ? 53.864 26.172 -13.881 1.00 12.99 ? 47 TYR B OH 1 ATOM 1898 N N . ARG B 2 50 ? 51.835 28.336 -21.600 1.00 11.55 ? 48 ARG B N 1 ATOM 1899 C CA . ARG B 2 50 ? 51.354 29.152 -22.705 1.00 14.75 ? 48 ARG B CA 1 ATOM 1900 C C . ARG B 2 50 ? 50.498 30.284 -22.166 1.00 16.84 ? 48 ARG B C 1 ATOM 1901 O O . ARG B 2 50 ? 49.661 30.072 -21.288 1.00 18.49 ? 48 ARG B O 1 ATOM 1902 C CB . ARG B 2 50 ? 50.512 28.312 -23.665 1.00 16.58 ? 48 ARG B CB 1 ATOM 1903 C CG . ARG B 2 50 ? 51.264 27.215 -24.400 1.00 20.76 ? 48 ARG B CG 1 ATOM 1904 C CD . ARG B 2 50 ? 52.140 27.802 -25.497 1.00 24.88 ? 48 ARG B CD 1 ATOM 1905 N NE . ARG B 2 50 ? 52.837 26.769 -26.257 1.00 27.37 ? 48 ARG B NE 1 ATOM 1906 C CZ . ARG B 2 50 ? 54.123 26.466 -26.110 1.00 31.19 ? 48 ARG B CZ 1 ATOM 1907 N NH1 . ARG B 2 50 ? 54.866 27.120 -25.227 1.00 32.81 ? 48 ARG B NH1 1 ATOM 1908 N NH2 . ARG B 2 50 ? 54.666 25.507 -26.847 1.00 34.14 ? 48 ARG B NH2 1 ATOM 1909 N N . ALA B 2 51 ? 50.709 31.487 -22.685 1.00 17.20 ? 49 ALA B N 1 ATOM 1910 C CA . ALA B 2 51 ? 49.880 32.614 -22.289 1.00 17.27 ? 49 ALA B CA 1 ATOM 1911 C C . ALA B 2 51 ? 48.461 32.380 -22.788 1.00 16.46 ? 49 ALA B C 1 ATOM 1912 O O . ALA B 2 51 ? 48.255 31.975 -23.934 1.00 17.88 ? 49 ALA B O 1 ATOM 1913 C CB . ALA B 2 51 ? 50.439 33.908 -22.849 1.00 12.92 ? 49 ALA B CB 1 ATOM 1914 N N . VAL B 2 52 ? 47.487 32.630 -21.922 1.00 16.03 ? 50 VAL B N 1 ATOM 1915 C CA . VAL B 2 52 ? 46.083 32.539 -22.297 1.00 15.86 ? 50 VAL B CA 1 ATOM 1916 C C . VAL B 2 52 ? 45.582 33.910 -22.728 1.00 18.39 ? 50 VAL B C 1 ATOM 1917 O O . VAL B 2 52 ? 44.760 34.038 -23.635 1.00 22.53 ? 50 VAL B O 1 ATOM 1918 C CB . VAL B 2 52 ? 45.225 31.974 -21.148 1.00 13.98 ? 50 VAL B CB 1 ATOM 1919 C CG1 . VAL B 2 52 ? 43.757 31.919 -21.552 1.00 10.85 ? 50 VAL B CG1 1 ATOM 1920 C CG2 . VAL B 2 52 ? 45.718 30.594 -20.753 1.00 10.45 ? 50 VAL B CG2 1 ATOM 1921 N N . THR B 2 53 ? 46.111 34.937 -22.073 1.00 18.48 ? 51 THR B N 1 ATOM 1922 C CA . THR B 2 53 ? 45.855 36.317 -22.452 1.00 19.52 ? 51 THR B CA 1 ATOM 1923 C C . THR B 2 53 ? 47.169 37.075 -22.516 1.00 20.51 ? 51 THR B C 1 ATOM 1924 O O . THR B 2 53 ? 48.220 36.555 -22.137 1.00 19.81 ? 51 THR B O 1 ATOM 1925 C CB . THR B 2 53 ? 44.930 37.029 -21.444 1.00 20.03 ? 51 THR B CB 1 ATOM 1926 O OG1 . THR B 2 53 ? 45.606 37.168 -20.187 1.00 21.92 ? 51 THR B OG1 1 ATOM 1927 C CG2 . THR B 2 53 ? 43.640 36.245 -21.240 1.00 15.15 ? 51 THR B CG2 1 ATOM 1928 N N . GLU B 2 54 ? 47.096 38.302 -23.019 1.00 18.99 ? 52 GLU B N 1 ATOM 1929 C CA . GLU B 2 54 ? 48.261 39.159 -23.174 1.00 23.24 ? 52 GLU B CA 1 ATOM 1930 C C . GLU B 2 54 ? 48.977 39.380 -21.841 1.00 20.81 ? 52 GLU B C 1 ATOM 1931 O O . GLU B 2 54 ? 50.198 39.526 -21.788 1.00 17.18 ? 52 GLU B O 1 ATOM 1932 C CB . GLU B 2 54 ? 47.832 40.496 -23.785 1.00 31.99 ? 52 GLU B CB 1 ATOM 1933 C CG . GLU B 2 54 ? 48.759 41.122 -24.792 1.00 42.66 ? 52 GLU B CG 1 ATOM 1934 C CD . GLU B 2 54 ? 48.340 42.542 -25.117 1.00 52.90 ? 52 GLU B CD 1 ATOM 1935 O OE1 . GLU B 2 54 ? 48.310 42.900 -26.312 1.00 54.88 ? 52 GLU B OE1 1 ATOM 1936 O OE2 . GLU B 2 54 ? 48.027 43.297 -24.173 1.00 56.13 ? 52 GLU B OE2 1 ATOM 1937 N N . LEU B 2 55 ? 48.186 39.409 -20.772 1.00 19.48 ? 53 LEU B N 1 ATOM 1938 C CA . LEU B 2 55 ? 48.671 39.587 -19.407 1.00 17.55 ? 53 LEU B CA 1 ATOM 1939 C C . LEU B 2 55 ? 49.686 38.530 -18.950 1.00 16.85 ? 53 LEU B C 1 ATOM 1940 O O . LEU B 2 55 ? 50.522 38.798 -18.087 1.00 20.24 ? 53 LEU B O 1 ATOM 1941 C CB . LEU B 2 55 ? 47.472 39.573 -18.455 1.00 17.98 ? 53 LEU B CB 1 ATOM 1942 C CG . LEU B 2 55 ? 47.505 40.529 -17.262 1.00 23.76 ? 53 LEU B CG 1 ATOM 1943 C CD1 . LEU B 2 55 ? 47.808 41.948 -17.717 1.00 26.39 ? 53 LEU B CD1 1 ATOM 1944 C CD2 . LEU B 2 55 ? 46.188 40.475 -16.495 1.00 24.39 ? 53 LEU B CD2 1 ATOM 1945 N N . GLY B 2 56 ? 49.613 37.335 -19.535 1.00 14.87 ? 54 GLY B N 1 ATOM 1946 C CA . GLY B 2 56 ? 50.453 36.224 -19.113 1.00 14.16 ? 54 GLY B CA 1 ATOM 1947 C C . GLY B 2 56 ? 51.714 35.923 -19.901 1.00 14.35 ? 54 GLY B C 1 ATOM 1948 O O . GLY B 2 56 ? 52.461 35.010 -19.550 1.00 17.77 ? 54 GLY B O 1 ATOM 1949 N N . ARG B 2 57 ? 51.951 36.681 -20.967 1.00 16.22 ? 55 ARG B N 1 ATOM 1950 C CA . ARG B 2 57 ? 53.106 36.447 -21.836 1.00 22.48 ? 55 ARG B CA 1 ATOM 1951 C C . ARG B 2 57 ? 54.464 36.530 -21.117 1.00 22.98 ? 55 ARG B C 1 ATOM 1952 O O . ARG B 2 57 ? 55.333 35.698 -21.377 1.00 21.48 ? 55 ARG B O 1 ATOM 1953 C CB . ARG B 2 57 ? 53.066 37.361 -23.064 1.00 24.58 ? 55 ARG B CB 1 ATOM 1954 C CG . ARG B 2 57 ? 51.921 36.981 -23.986 1.00 33.18 ? 55 ARG B CG 1 ATOM 1955 C CD . ARG B 2 57 ? 51.689 37.942 -25.131 1.00 42.49 ? 55 ARG B CD 1 ATOM 1956 N NE . ARG B 2 57 ? 50.582 37.466 -25.956 1.00 51.60 ? 55 ARG B NE 1 ATOM 1957 C CZ . ARG B 2 57 ? 49.965 38.187 -26.885 1.00 58.77 ? 55 ARG B CZ 1 ATOM 1958 N NH1 . ARG B 2 57 ? 50.352 39.429 -27.132 1.00 60.30 ? 55 ARG B NH1 1 ATOM 1959 N NH2 . ARG B 2 57 ? 48.967 37.656 -27.580 1.00 62.56 ? 55 ARG B NH2 1 ATOM 1960 N N . PRO B 2 58 ? 54.669 37.536 -20.241 1.00 23.72 ? 56 PRO B N 1 ATOM 1961 C CA . PRO B 2 58 ? 55.971 37.587 -19.565 1.00 23.38 ? 56 PRO B CA 1 ATOM 1962 C C . PRO B 2 58 ? 56.203 36.348 -18.702 1.00 22.63 ? 56 PRO B C 1 ATOM 1963 O O . PRO B 2 58 ? 57.330 35.859 -18.620 1.00 22.77 ? 56 PRO B O 1 ATOM 1964 C CB . PRO B 2 58 ? 55.866 38.837 -18.686 1.00 18.35 ? 56 PRO B CB 1 ATOM 1965 C CG . PRO B 2 58 ? 54.878 39.693 -19.386 1.00 16.54 ? 56 PRO B CG 1 ATOM 1966 C CD . PRO B 2 58 ? 53.866 38.737 -19.941 1.00 18.09 ? 56 PRO B CD 1 ATOM 1967 N N . ASP B 2 59 ? 55.144 35.855 -18.066 1.00 23.40 ? 57 ASP B N 1 ATOM 1968 C CA . ASP B 2 59 ? 55.246 34.688 -17.198 1.00 18.87 ? 57 ASP B CA 1 ATOM 1969 C C . ASP B 2 59 ? 55.524 33.409 -17.977 1.00 20.10 ? 57 ASP B C 1 ATOM 1970 O O . ASP B 2 59 ? 56.320 32.574 -17.548 1.00 19.79 ? 57 ASP B O 1 ATOM 1971 C CB . ASP B 2 59 ? 53.981 34.534 -16.357 1.00 20.06 ? 57 ASP B CB 1 ATOM 1972 C CG . ASP B 2 59 ? 53.837 35.629 -15.334 1.00 23.09 ? 57 ASP B CG 1 ATOM 1973 O OD1 . ASP B 2 59 ? 54.874 36.123 -14.850 1.00 23.91 ? 57 ASP B OD1 1 ATOM 1974 O OD2 . ASP B 2 59 ? 52.688 36.003 -15.022 1.00 25.88 ? 57 ASP B OD2 1 ATOM 1975 N N . ALA B 2 60 ? 54.851 33.255 -19.113 1.00 20.76 ? 58 ALA B N 1 ATOM 1976 C CA . ALA B 2 60 ? 55.069 32.111 -19.993 1.00 17.73 ? 58 ALA B CA 1 ATOM 1977 C C . ALA B 2 60 ? 56.530 32.016 -20.411 1.00 19.61 ? 58 ALA B C 1 ATOM 1978 O O . ALA B 2 60 ? 57.140 30.950 -20.349 1.00 18.57 ? 58 ALA B O 1 ATOM 1979 C CB . ALA B 2 60 ? 54.164 32.184 -21.212 1.00 16.52 ? 58 ALA B CB 1 ATOM 1980 N N . GLU B 2 61 ? 57.084 33.150 -20.825 1.00 18.80 ? 59 GLU B N 1 ATOM 1981 C CA . GLU B 2 61 ? 58.461 33.221 -21.296 1.00 23.23 ? 59 GLU B CA 1 ATOM 1982 C C . GLU B 2 61 ? 59.486 33.009 -20.181 1.00 22.55 ? 59 GLU B C 1 ATOM 1983 O O . GLU B 2 61 ? 60.494 32.330 -20.380 1.00 22.02 ? 59 GLU B O 1 ATOM 1984 C CB . GLU B 2 61 ? 58.716 34.526 -22.059 1.00 29.91 ? 59 GLU B CB 1 ATOM 1985 C CG . GLU B 2 61 ? 57.751 34.745 -23.220 1.00 41.13 ? 59 GLU B CG 1 ATOM 1986 C CD . GLU B 2 61 ? 57.983 36.056 -23.944 1.00 48.14 ? 59 GLU B CD 1 ATOM 1987 O OE1 . GLU B 2 61 ? 58.840 36.844 -23.492 1.00 53.66 ? 59 GLU B OE1 1 ATOM 1988 O OE2 . GLU B 2 61 ? 57.303 36.300 -24.963 1.00 49.77 ? 59 GLU B OE2 1 ATOM 1989 N N . TYR B 2 62 ? 59.230 33.597 -19.015 1.00 18.64 ? 60 TYR B N 1 ATOM 1990 C CA . TYR B 2 62 ? 60.144 33.463 -17.885 1.00 19.25 ? 60 TYR B CA 1 ATOM 1991 C C . TYR B 2 62 ? 60.160 32.034 -17.355 1.00 19.85 ? 60 TYR B C 1 ATOM 1992 O O . TYR B 2 62 ? 61.223 31.459 -17.124 1.00 24.13 ? 60 TYR B O 1 ATOM 1993 C CB . TYR B 2 62 ? 59.746 34.428 -16.765 1.00 17.02 ? 60 TYR B CB 1 ATOM 1994 C CG . TYR B 2 62 ? 60.629 34.337 -15.542 1.00 20.47 ? 60 TYR B CG 1 ATOM 1995 C CD1 . TYR B 2 62 ? 62.012 34.394 -15.655 1.00 20.29 ? 60 TYR B CD1 1 ATOM 1996 C CD2 . TYR B 2 62 ? 60.082 34.199 -14.273 1.00 21.72 ? 60 TYR B CD2 1 ATOM 1997 C CE1 . TYR B 2 62 ? 62.825 34.310 -14.540 1.00 22.24 ? 60 TYR B CE1 1 ATOM 1998 C CE2 . TYR B 2 62 ? 60.886 34.118 -13.152 1.00 24.55 ? 60 TYR B CE2 1 ATOM 1999 C CZ . TYR B 2 62 ? 62.258 34.173 -13.291 1.00 26.13 ? 60 TYR B CZ 1 ATOM 2000 O OH . TYR B 2 62 ? 63.066 34.092 -12.180 1.00 31.62 ? 60 TYR B OH 1 ATOM 2001 N N . TRP B 2 63 ? 58.974 31.468 -17.156 1.00 18.72 ? 61 TRP B N 1 ATOM 2002 C CA . TRP B 2 63 ? 58.850 30.120 -16.615 1.00 17.15 ? 61 TRP B CA 1 ATOM 2003 C C . TRP B 2 63 ? 59.368 29.050 -17.575 1.00 20.11 ? 61 TRP B C 1 ATOM 2004 O O . TRP B 2 63 ? 59.949 28.055 -17.143 1.00 19.45 ? 61 TRP B O 1 ATOM 2005 C CB . TRP B 2 63 ? 57.394 29.850 -16.223 1.00 12.85 ? 61 TRP B CB 1 ATOM 2006 C CG . TRP B 2 63 ? 56.919 30.716 -15.094 1.00 17.05 ? 61 TRP B CG 1 ATOM 2007 C CD1 . TRP B 2 63 ? 57.688 31.511 -14.293 1.00 13.89 ? 61 TRP B CD1 1 ATOM 2008 C CD2 . TRP B 2 63 ? 55.566 30.889 -14.650 1.00 13.95 ? 61 TRP B CD2 1 ATOM 2009 N NE1 . TRP B 2 63 ? 56.901 32.155 -13.369 1.00 12.55 ? 61 TRP B NE1 1 ATOM 2010 C CE2 . TRP B 2 63 ? 55.594 31.794 -13.569 1.00 12.84 ? 61 TRP B CE2 1 ATOM 2011 C CE3 . TRP B 2 63 ? 54.335 30.365 -15.058 1.00 11.57 ? 61 TRP B CE3 1 ATOM 2012 C CZ2 . TRP B 2 63 ? 54.438 32.186 -12.892 1.00 16.40 ? 61 TRP B CZ2 1 ATOM 2013 C CZ3 . TRP B 2 63 ? 53.188 30.756 -14.383 1.00 9.67 ? 61 TRP B CZ3 1 ATOM 2014 C CH2 . TRP B 2 63 ? 53.249 31.657 -13.313 1.00 9.81 ? 61 TRP B CH2 1 ATOM 2015 N N . ASN B 2 64 ? 59.154 29.252 -18.872 1.00 22.12 ? 62 ASN B N 1 ATOM 2016 C CA . ASN B 2 64 ? 59.635 28.299 -19.868 1.00 21.66 ? 62 ASN B CA 1 ATOM 2017 C C . ASN B 2 64 ? 61.157 28.299 -20.006 1.00 22.16 ? 62 ASN B C 1 ATOM 2018 O O . ASN B 2 64 ? 61.729 27.370 -20.575 1.00 16.48 ? 62 ASN B O 1 ATOM 2019 C CB . ASN B 2 64 ? 58.990 28.553 -21.237 1.00 18.73 ? 62 ASN B CB 1 ATOM 2020 C CG . ASN B 2 64 ? 57.543 28.097 -21.300 1.00 16.30 ? 62 ASN B CG 1 ATOM 2021 O OD1 . ASN B 2 64 ? 57.093 27.306 -20.473 1.00 18.45 ? 62 ASN B OD1 1 ATOM 2022 N ND2 . ASN B 2 64 ? 56.807 28.599 -22.286 1.00 16.48 ? 62 ASN B ND2 1 ATOM 2023 N N . SER B 2 65 ? 61.811 29.338 -19.491 1.00 19.72 ? 63 SER B N 1 ATOM 2024 C CA . SER B 2 65 ? 63.269 29.403 -19.542 1.00 19.18 ? 63 SER B CA 1 ATOM 2025 C C . SER B 2 65 ? 63.912 28.631 -18.391 1.00 23.69 ? 63 SER B C 1 ATOM 2026 O O . SER B 2 65 ? 65.132 28.476 -18.341 1.00 27.27 ? 63 SER B O 1 ATOM 2027 C CB . SER B 2 65 ? 63.749 30.855 -19.524 1.00 19.29 ? 63 SER B CB 1 ATOM 2028 O OG . SER B 2 65 ? 63.681 31.398 -18.216 1.00 19.42 ? 63 SER B OG 1 ATOM 2029 N N . GLN B 2 66 ? 63.078 28.150 -17.475 1.00 23.17 ? 64 GLN B N 1 ATOM 2030 C CA . GLN B 2 66 ? 63.539 27.404 -16.309 1.00 23.17 ? 64 GLN B CA 1 ATOM 2031 C C . GLN B 2 66 ? 63.295 25.908 -16.463 1.00 24.18 ? 64 GLN B C 1 ATOM 2032 O O . GLN B 2 66 ? 62.200 25.415 -16.187 1.00 23.55 ? 64 GLN B O 1 ATOM 2033 C CB . GLN B 2 66 ? 62.852 27.923 -15.048 1.00 19.89 ? 64 GLN B CB 1 ATOM 2034 C CG . GLN B 2 66 ? 63.058 29.407 -14.818 1.00 25.04 ? 64 GLN B CG 1 ATOM 2035 C CD . GLN B 2 66 ? 62.296 29.921 -13.619 1.00 30.66 ? 64 GLN B CD 1 ATOM 2036 O OE1 . GLN B 2 66 ? 62.170 29.233 -12.607 1.00 35.06 ? 64 GLN B OE1 1 ATOM 2037 N NE2 . GLN B 2 66 ? 61.795 31.143 -13.720 1.00 31.49 ? 64 GLN B NE2 1 ATOM 2038 N N . LYS B 2 67 ? 64.321 25.196 -16.913 1.00 26.27 ? 65 LYS B N 1 ATOM 2039 C CA . LYS B 2 67 ? 64.216 23.771 -17.205 1.00 28.33 ? 65 LYS B CA 1 ATOM 2040 C C . LYS B 2 67 ? 63.826 22.910 -16.008 1.00 22.86 ? 65 LYS B C 1 ATOM 2041 O O . LYS B 2 67 ? 63.081 21.941 -16.148 1.00 18.25 ? 65 LYS B O 1 ATOM 2042 C CB . LYS B 2 67 ? 65.525 23.268 -17.805 1.00 33.62 ? 65 LYS B CB 1 ATOM 2043 C CG . LYS B 2 67 ? 66.695 23.386 -16.837 1.00 42.55 ? 65 LYS B CG 1 ATOM 2044 C CD . LYS B 2 67 ? 68.028 23.242 -17.524 1.00 47.47 ? 65 LYS B CD 1 ATOM 2045 C CE . LYS B 2 67 ? 69.175 23.551 -16.580 1.00 49.42 ? 65 LYS B CE 1 ATOM 2046 N NZ . LYS B 2 67 ? 70.490 23.464 -17.272 1.00 49.53 ? 65 LYS B NZ 1 ATOM 2047 N N . ASP B 2 68 ? 64.336 23.269 -14.836 1.00 22.43 ? 66 ASP B N 1 ATOM 2048 C CA . ASP B 2 68 ? 64.028 22.553 -13.608 1.00 25.52 ? 66 ASP B CA 1 ATOM 2049 C C . ASP B 2 68 ? 62.550 22.675 -13.246 1.00 25.39 ? 66 ASP B C 1 ATOM 2050 O O . ASP B 2 68 ? 61.914 21.704 -12.837 1.00 28.08 ? 66 ASP B O 1 ATOM 2051 C CB . ASP B 2 68 ? 64.928 23.025 -12.464 1.00 32.46 ? 66 ASP B CB 1 ATOM 2052 C CG . ASP B 2 68 ? 64.883 24.525 -12.270 1.00 36.40 ? 66 ASP B CG 1 ATOM 2053 O OD1 . ASP B 2 68 ? 64.522 25.238 -13.229 1.00 31.42 ? 66 ASP B OD1 1 ATOM 2054 O OD2 . ASP B 2 68 ? 65.216 24.992 -11.162 1.00 41.16 ? 66 ASP B OD2 1 ATOM 2055 N N . LEU B 2 69 ? 62.017 23.884 -13.396 1.00 25.52 ? 67 LEU B N 1 ATOM 2056 C CA . LEU B 2 69 ? 60.604 24.155 -13.159 1.00 21.09 ? 67 LEU B CA 1 ATOM 2057 C C . LEU B 2 69 ? 59.708 23.362 -14.114 1.00 21.10 ? 67 LEU B C 1 ATOM 2058 O O . LEU B 2 69 ? 58.717 22.764 -13.692 1.00 14.74 ? 67 LEU B O 1 ATOM 2059 C CB . LEU B 2 69 ? 60.319 25.649 -13.309 1.00 23.19 ? 67 LEU B CB 1 ATOM 2060 C CG . LEU B 2 69 ? 58.843 26.046 -13.356 1.00 28.92 ? 67 LEU B CG 1 ATOM 2061 C CD1 . LEU B 2 69 ? 58.163 25.709 -12.037 1.00 28.49 ? 67 LEU B CD1 1 ATOM 2062 C CD2 . LEU B 2 69 ? 58.699 27.523 -13.675 1.00 29.61 ? 67 LEU B CD2 1 ATOM 2063 N N . LEU B 2 70 ? 60.055 23.374 -15.399 1.00 23.52 ? 68 LEU B N 1 ATOM 2064 C CA . LEU B 2 70 ? 59.282 22.663 -16.416 1.00 22.30 ? 68 LEU B CA 1 ATOM 2065 C C . LEU B 2 70 ? 59.257 21.158 -16.167 1.00 23.88 ? 68 LEU B C 1 ATOM 2066 O O . LEU B 2 70 ? 58.221 20.515 -16.333 1.00 20.62 ? 68 LEU B O 1 ATOM 2067 C CB . LEU B 2 70 ? 59.804 22.959 -17.826 1.00 21.48 ? 68 LEU B CB 1 ATOM 2068 C CG . LEU B 2 70 ? 59.529 24.349 -18.402 1.00 23.26 ? 68 LEU B CG 1 ATOM 2069 C CD1 . LEU B 2 70 ? 60.010 24.430 -19.843 1.00 27.20 ? 68 LEU B CD1 1 ATOM 2070 C CD2 . LEU B 2 70 ? 58.050 24.685 -18.310 1.00 20.19 ? 68 LEU B CD2 1 ATOM 2071 N N . GLU B 2 71 ? 60.396 20.603 -15.763 1.00 20.16 ? 69 GLU B N 1 ATOM 2072 C CA . GLU B 2 71 ? 60.478 19.176 -15.465 1.00 18.37 ? 69 GLU B CA 1 ATOM 2073 C C . GLU B 2 71 ? 59.658 18.806 -14.235 1.00 21.16 ? 69 GLU B C 1 ATOM 2074 O O . GLU B 2 71 ? 59.143 17.692 -14.132 1.00 23.04 ? 69 GLU B O 1 ATOM 2075 C CB . GLU B 2 71 ? 61.931 18.701 -15.365 1.00 17.07 ? 69 GLU B CB 1 ATOM 2076 C CG . GLU B 2 71 ? 62.678 18.726 -16.690 1.00 22.53 ? 69 GLU B CG 1 ATOM 2077 C CD . GLU B 2 71 ? 62.024 17.863 -17.757 1.00 26.67 ? 69 GLU B CD 1 ATOM 2078 O OE1 . GLU B 2 71 ? 61.268 16.931 -17.406 1.00 29.96 ? 69 GLU B OE1 1 ATOM 2079 O OE2 . GLU B 2 71 ? 62.261 18.124 -18.954 1.00 29.14 ? 69 GLU B OE2 1 ATOM 2080 N N . GLN B 2 72 ? 59.551 19.745 -13.302 1.00 22.74 ? 70 GLN B N 1 ATOM 2081 C CA . GLN B 2 72 ? 58.692 19.563 -12.144 1.00 22.77 ? 70 GLN B CA 1 ATOM 2082 C C . GLN B 2 72 ? 57.256 19.433 -12.631 1.00 20.25 ? 70 GLN B C 1 ATOM 2083 O O . GLN B 2 72 ? 56.540 18.505 -12.258 1.00 20.54 ? 70 GLN B O 1 ATOM 2084 C CB . GLN B 2 72 ? 58.816 20.744 -11.175 1.00 26.69 ? 70 GLN B CB 1 ATOM 2085 C CG . GLN B 2 72 ? 59.910 20.606 -10.128 1.00 33.83 ? 70 GLN B CG 1 ATOM 2086 C CD . GLN B 2 72 ? 59.453 19.833 -8.905 1.00 41.27 ? 70 GLN B CD 1 ATOM 2087 O OE1 . GLN B 2 72 ? 59.176 20.415 -7.856 1.00 47.65 ? 70 GLN B OE1 1 ATOM 2088 N NE2 . GLN B 2 72 ? 59.374 18.514 -9.034 1.00 42.14 ? 70 GLN B NE2 1 ATOM 2089 N N . LYS B 2 73 ? 56.846 20.375 -13.475 1.00 19.92 ? 71 LYS B N 1 ATOM 2090 C CA . LYS B 2 73 ? 55.488 20.397 -14.004 1.00 15.22 ? 71 LYS B CA 1 ATOM 2091 C C . LYS B 2 73 ? 55.172 19.214 -14.930 1.00 14.21 ? 71 LYS B C 1 ATOM 2092 O O . LYS B 2 73 ? 54.057 18.695 -14.927 1.00 19.09 ? 71 LYS B O 1 ATOM 2093 C CB . LYS B 2 73 ? 55.237 21.719 -14.733 1.00 11.24 ? 71 LYS B CB 1 ATOM 2094 C CG . LYS B 2 73 ? 55.328 22.950 -13.842 1.00 13.56 ? 71 LYS B CG 1 ATOM 2095 C CD . LYS B 2 73 ? 54.302 22.954 -12.727 1.00 17.66 ? 71 LYS B CD 1 ATOM 2096 C CE . LYS B 2 73 ? 54.680 23.992 -11.678 1.00 16.62 ? 71 LYS B CE 1 ATOM 2097 N NZ . LYS B 2 73 ? 53.772 23.973 -10.499 1.00 17.58 ? 71 LYS B NZ 1 ATOM 2098 N N . ARG B 2 74 ? 56.158 18.799 -15.725 1.00 14.62 ? 72 ARG B N 1 ATOM 2099 C CA . ARG B 2 74 ? 56.005 17.667 -16.645 1.00 18.90 ? 72 ARG B CA 1 ATOM 2100 C C . ARG B 2 74 ? 55.854 16.314 -15.951 1.00 19.08 ? 72 ARG B C 1 ATOM 2101 O O . ARG B 2 74 ? 55.300 15.373 -16.521 1.00 17.68 ? 72 ARG B O 1 ATOM 2102 C CB . ARG B 2 74 ? 57.190 17.604 -17.613 1.00 19.58 ? 72 ARG B CB 1 ATOM 2103 C CG . ARG B 2 74 ? 57.167 18.678 -18.691 1.00 20.59 ? 72 ARG B CG 1 ATOM 2104 C CD . ARG B 2 74 ? 58.513 18.804 -19.388 1.00 15.28 ? 72 ARG B CD 1 ATOM 2105 N NE . ARG B 2 74 ? 58.558 19.968 -20.269 1.00 18.82 ? 72 ARG B NE 1 ATOM 2106 C CZ . ARG B 2 74 ? 59.643 20.375 -20.919 1.00 24.22 ? 72 ARG B CZ 1 ATOM 2107 N NH1 . ARG B 2 74 ? 60.782 19.707 -20.797 1.00 24.66 ? 72 ARG B NH1 1 ATOM 2108 N NH2 . ARG B 2 74 ? 59.588 21.447 -21.697 1.00 26.85 ? 72 ARG B NH2 1 ATOM 2109 N N . ALA B 2 75 ? 56.358 16.221 -14.726 1.00 16.40 ? 73 ALA B N 1 ATOM 2110 C CA . ALA B 2 75 ? 56.305 14.982 -13.962 1.00 17.22 ? 73 ALA B CA 1 ATOM 2111 C C . ALA B 2 75 ? 55.073 14.930 -13.069 1.00 18.50 ? 73 ALA B C 1 ATOM 2112 O O . ALA B 2 75 ? 54.797 13.909 -12.438 1.00 20.97 ? 73 ALA B O 1 ATOM 2113 C CB . ALA B 2 75 ? 57.569 14.817 -13.132 1.00 15.93 ? 73 ALA B CB 1 ATOM 2114 N N . ALA B 2 76 ? 54.343 16.040 -13.021 1.00 16.74 ? 74 ALA B N 1 ATOM 2115 C CA . ALA B 2 76 ? 53.229 16.199 -12.092 1.00 16.69 ? 74 ALA B CA 1 ATOM 2116 C C . ALA B 2 76 ? 52.138 15.138 -12.245 1.00 18.93 ? 74 ALA B C 1 ATOM 2117 O O . ALA B 2 76 ? 51.537 14.724 -11.258 1.00 15.74 ? 74 ALA B O 1 ATOM 2118 C CB . ALA B 2 76 ? 52.637 17.597 -12.206 1.00 13.44 ? 74 ALA B CB 1 ATOM 2119 N N . VAL B 2 77 ? 51.875 14.704 -13.474 1.00 20.29 ? 75 VAL B N 1 ATOM 2120 C CA . VAL B 2 77 ? 50.863 13.673 -13.698 1.00 16.77 ? 75 VAL B CA 1 ATOM 2121 C C . VAL B 2 77 ? 51.147 12.405 -12.888 1.00 18.83 ? 75 VAL B C 1 ATOM 2122 O O . VAL B 2 77 ? 50.224 11.698 -12.483 1.00 20.93 ? 75 VAL B O 1 ATOM 2123 C CB . VAL B 2 77 ? 50.710 13.303 -15.190 1.00 18.32 ? 75 VAL B CB 1 ATOM 2124 C CG1 . VAL B 2 77 ? 49.972 14.405 -15.939 1.00 13.08 ? 75 VAL B CG1 1 ATOM 2125 C CG2 . VAL B 2 77 ? 52.075 13.017 -15.819 1.00 14.68 ? 75 VAL B CG2 1 ATOM 2126 N N . ASP B 2 78 ? 52.427 12.124 -12.656 1.00 17.71 ? 76 ASP B N 1 ATOM 2127 C CA . ASP B 2 78 ? 52.832 10.970 -11.860 1.00 20.69 ? 76 ASP B CA 1 ATOM 2128 C C . ASP B 2 78 ? 53.006 11.308 -10.380 1.00 23.04 ? 76 ASP B C 1 ATOM 2129 O O . ASP B 2 78 ? 52.396 10.681 -9.515 1.00 26.91 ? 76 ASP B O 1 ATOM 2130 C CB . ASP B 2 78 ? 54.140 10.391 -12.401 1.00 18.28 ? 76 ASP B CB 1 ATOM 2131 C CG . ASP B 2 78 ? 53.975 9.765 -13.771 1.00 20.74 ? 76 ASP B CG 1 ATOM 2132 O OD1 . ASP B 2 78 ? 52.857 9.299 -14.083 1.00 22.21 ? 76 ASP B OD1 1 ATOM 2133 O OD2 . ASP B 2 78 ? 54.961 9.737 -14.535 1.00 24.93 ? 76 ASP B OD2 1 ATOM 2134 N N . THR B 2 79 ? 53.846 12.301 -10.098 1.00 20.72 ? 77 THR B N 1 ATOM 2135 C CA . THR B 2 79 ? 54.268 12.589 -8.729 1.00 21.16 ? 77 THR B CA 1 ATOM 2136 C C . THR B 2 79 ? 53.206 13.356 -7.948 1.00 21.42 ? 77 THR B C 1 ATOM 2137 O O . THR B 2 79 ? 53.249 13.415 -6.720 1.00 19.60 ? 77 THR B O 1 ATOM 2138 C CB . THR B 2 79 ? 55.569 13.416 -8.702 1.00 23.39 ? 77 THR B CB 1 ATOM 2139 O OG1 . THR B 2 79 ? 55.337 14.697 -9.301 1.00 23.57 ? 77 THR B OG1 1 ATOM 2140 C CG2 . THR B 2 79 ? 56.678 12.698 -9.455 1.00 22.74 ? 77 THR B CG2 1 ATOM 2141 N N . TYR B 2 80 ? 52.253 13.936 -8.667 1.00 19.38 ? 78 TYR B N 1 ATOM 2142 C CA . TYR B 2 80 ? 51.226 14.766 -8.052 1.00 17.70 ? 78 TYR B CA 1 ATOM 2143 C C . TYR B 2 80 ? 49.834 14.176 -8.280 1.00 19.57 ? 78 TYR B C 1 ATOM 2144 O O . TYR B 2 80 ? 49.154 13.797 -7.328 1.00 21.11 ? 78 TYR B O 1 ATOM 2145 C CB . TYR B 2 80 ? 51.325 16.188 -8.614 1.00 12.68 ? 78 TYR B CB 1 ATOM 2146 C CG . TYR B 2 80 ? 50.260 17.145 -8.139 1.00 15.56 ? 78 TYR B CG 1 ATOM 2147 C CD1 . TYR B 2 80 ? 50.154 17.488 -6.800 1.00 15.00 ? 78 TYR B CD1 1 ATOM 2148 C CD2 . TYR B 2 80 ? 49.386 17.738 -9.040 1.00 13.77 ? 78 TYR B CD2 1 ATOM 2149 C CE1 . TYR B 2 80 ? 49.185 18.372 -6.366 1.00 15.22 ? 78 TYR B CE1 1 ATOM 2150 C CE2 . TYR B 2 80 ? 48.419 18.624 -8.617 1.00 14.97 ? 78 TYR B CE2 1 ATOM 2151 C CZ . TYR B 2 80 ? 48.323 18.938 -7.280 1.00 16.03 ? 78 TYR B CZ 1 ATOM 2152 O OH . TYR B 2 80 ? 47.361 19.821 -6.859 1.00 17.45 ? 78 TYR B OH 1 ATOM 2153 N N . CYS B 2 81 ? 49.416 14.094 -9.539 1.00 13.27 ? 79 CYS B N 1 ATOM 2154 C CA . CYS B 2 81 ? 48.081 13.600 -9.872 1.00 19.18 ? 79 CYS B CA 1 ATOM 2155 C C . CYS B 2 81 ? 47.851 12.133 -9.496 1.00 18.07 ? 79 CYS B C 1 ATOM 2156 O O . CYS B 2 81 ? 46.948 11.828 -8.716 1.00 17.86 ? 79 CYS B O 1 ATOM 2157 C CB . CYS B 2 81 ? 47.783 13.816 -11.357 1.00 12.85 ? 79 CYS B CB 1 ATOM 2158 S SG . CYS B 2 81 ? 47.835 15.546 -11.873 1.00 15.85 ? 79 CYS B SG 1 ATOM 2159 N N . ARG B 2 82 ? 48.653 11.229 -10.052 1.00 18.97 ? 80 ARG B N 1 ATOM 2160 C CA . ARG B 2 82 ? 48.496 9.801 -9.767 1.00 18.63 ? 80 ARG B CA 1 ATOM 2161 C C . ARG B 2 82 ? 48.728 9.509 -8.286 1.00 21.85 ? 80 ARG B C 1 ATOM 2162 O O . ARG B 2 82 ? 48.062 8.646 -7.711 1.00 25.57 ? 80 ARG B O 1 ATOM 2163 C CB . ARG B 2 82 ? 49.406 8.950 -10.658 1.00 17.59 ? 80 ARG B CB 1 ATOM 2164 C CG . ARG B 2 82 ? 48.881 8.808 -12.087 1.00 24.72 ? 80 ARG B CG 1 ATOM 2165 C CD . ARG B 2 82 ? 49.783 7.939 -12.952 1.00 22.65 ? 80 ARG B CD 1 ATOM 2166 N NE . ARG B 2 82 ? 50.196 8.638 -14.168 1.00 30.41 ? 80 ARG B NE 1 ATOM 2167 C CZ . ARG B 2 82 ? 49.652 8.451 -15.366 1.00 28.09 ? 80 ARG B CZ 1 ATOM 2168 N NH1 . ARG B 2 82 ? 48.671 7.578 -15.521 1.00 20.54 ? 80 ARG B NH1 1 ATOM 2169 N NH2 . ARG B 2 82 ? 50.098 9.138 -16.411 1.00 32.74 ? 80 ARG B NH2 1 ATOM 2170 N N . HIS B 2 83 ? 49.682 10.210 -7.678 1.00 17.19 ? 81 HIS B N 1 ATOM 2171 C CA . HIS B 2 83 ? 49.954 10.038 -6.252 1.00 19.52 ? 81 HIS B CA 1 ATOM 2172 C C . HIS B 2 83 ? 48.739 10.378 -5.395 1.00 19.86 ? 81 HIS B C 1 ATOM 2173 O O . HIS B 2 83 ? 48.312 9.572 -4.569 1.00 24.16 ? 81 HIS B O 1 ATOM 2174 C CB . HIS B 2 83 ? 51.143 10.885 -5.795 1.00 17.83 ? 81 HIS B CB 1 ATOM 2175 C CG . HIS B 2 83 ? 51.384 10.828 -4.318 1.00 21.51 ? 81 HIS B CG 1 ATOM 2176 N ND1 . HIS B 2 83 ? 52.167 9.859 -3.725 1.00 24.19 ? 81 HIS B ND1 1 ATOM 2177 C CD2 . HIS B 2 83 ? 50.934 11.616 -3.312 1.00 20.93 ? 81 HIS B CD2 1 ATOM 2178 C CE1 . HIS B 2 83 ? 52.189 10.055 -2.418 1.00 26.28 ? 81 HIS B CE1 1 ATOM 2179 N NE2 . HIS B 2 83 ? 51.449 11.114 -2.142 1.00 20.00 ? 81 HIS B NE2 1 ATOM 2180 N N . ASN B 2 84 ? 48.186 11.571 -5.599 1.00 18.59 ? 82 ASN B N 1 ATOM 2181 C CA . ASN B 2 84 ? 47.063 12.039 -4.792 1.00 19.15 ? 82 ASN B CA 1 ATOM 2182 C C . ASN B 2 84 ? 45.800 11.216 -5.020 1.00 19.72 ? 82 ASN B C 1 ATOM 2183 O O . ASN B 2 84 ? 44.992 11.049 -4.106 1.00 21.41 ? 82 ASN B O 1 ATOM 2184 C CB . ASN B 2 84 ? 46.801 13.530 -5.027 1.00 21.96 ? 82 ASN B CB 1 ATOM 2185 C CG . ASN B 2 84 ? 47.829 14.414 -4.347 1.00 23.51 ? 82 ASN B CG 1 ATOM 2186 O OD1 . ASN B 2 84 ? 48.544 13.973 -3.446 1.00 23.22 ? 82 ASN B OD1 1 ATOM 2187 N ND2 . ASN B 2 84 ? 47.903 15.670 -4.769 1.00 13.57 ? 82 ASN B ND2 1 ATOM 2188 N N . TYR B 2 85 ? 45.629 10.719 -6.242 1.00 18.83 ? 83 TYR B N 1 ATOM 2189 C CA . TYR B 2 85 ? 44.507 9.845 -6.557 1.00 19.49 ? 83 TYR B CA 1 ATOM 2190 C C . TYR B 2 85 ? 44.586 8.610 -5.662 1.00 23.63 ? 83 TYR B C 1 ATOM 2191 O O . TYR B 2 85 ? 43.591 8.196 -5.075 1.00 27.19 ? 83 TYR B O 1 ATOM 2192 C CB . TYR B 2 85 ? 44.548 9.439 -8.035 1.00 22.09 ? 83 TYR B CB 1 ATOM 2193 C CG . TYR B 2 85 ? 43.334 8.680 -8.540 1.00 24.98 ? 83 TYR B CG 1 ATOM 2194 C CD1 . TYR B 2 85 ? 43.206 7.311 -8.331 1.00 23.44 ? 83 TYR B CD1 1 ATOM 2195 C CD2 . TYR B 2 85 ? 42.331 9.327 -9.253 1.00 22.53 ? 83 TYR B CD2 1 ATOM 2196 C CE1 . TYR B 2 85 ? 42.107 6.615 -8.799 1.00 23.18 ? 83 TYR B CE1 1 ATOM 2197 C CE2 . TYR B 2 85 ? 41.229 8.638 -9.725 1.00 20.29 ? 83 TYR B CE2 1 ATOM 2198 C CZ . TYR B 2 85 ? 41.122 7.282 -9.495 1.00 23.94 ? 83 TYR B CZ 1 ATOM 2199 O OH . TYR B 2 85 ? 40.028 6.589 -9.961 1.00 27.09 ? 83 TYR B OH 1 ATOM 2200 N N . GLY B 2 86 ? 45.784 8.039 -5.555 1.00 19.60 ? 84 GLY B N 1 ATOM 2201 C CA . GLY B 2 86 ? 46.032 6.869 -4.727 1.00 21.36 ? 84 GLY B CA 1 ATOM 2202 C C . GLY B 2 86 ? 45.762 7.086 -3.248 1.00 21.94 ? 84 GLY B C 1 ATOM 2203 O O . GLY B 2 86 ? 45.285 6.195 -2.547 1.00 35.58 ? 84 GLY B O 1 ATOM 2204 N N . VAL B 2 87 ? 46.086 8.287 -2.782 1.00 20.93 ? 85 VAL B N 1 ATOM 2205 C CA . VAL B 2 87 ? 45.954 8.680 -1.380 1.00 27.43 ? 85 VAL B CA 1 ATOM 2206 C C . VAL B 2 87 ? 44.496 8.786 -0.934 1.00 26.90 ? 85 VAL B C 1 ATOM 2207 O O . VAL B 2 87 ? 44.133 8.368 0.167 1.00 28.86 ? 85 VAL B O 1 ATOM 2208 C CB . VAL B 2 87 ? 46.681 10.020 -1.108 1.00 28.94 ? 85 VAL B CB 1 ATOM 2209 C CG1 . VAL B 2 87 ? 46.420 10.499 0.312 1.00 30.38 ? 85 VAL B CG1 1 ATOM 2210 C CG2 . VAL B 2 87 ? 48.174 9.869 -1.348 1.00 20.70 ? 85 VAL B CG2 1 ATOM 2211 N N . GLY B 2 88 ? 43.666 9.331 -1.815 1.00 23.89 ? 86 GLY B N 1 ATOM 2212 C CA . GLY B 2 88 ? 42.295 9.691 -1.504 1.00 20.18 ? 86 GLY B CA 1 ATOM 2213 C C . GLY B 2 88 ? 41.247 8.758 -2.083 1.00 22.65 ? 86 GLY B C 1 ATOM 2214 O O . GLY B 2 88 ? 40.060 8.909 -1.805 1.00 29.39 ? 86 GLY B O 1 ATOM 2215 N N . GLU B 2 89 ? 41.688 7.802 -2.895 1.00 23.54 ? 87 GLU B N 1 ATOM 2216 C CA . GLU B 2 89 ? 40.793 6.935 -3.662 1.00 27.18 ? 87 GLU B CA 1 ATOM 2217 C C . GLU B 2 89 ? 39.743 6.182 -2.840 1.00 28.46 ? 87 GLU B C 1 ATOM 2218 O O . GLU B 2 89 ? 38.581 6.107 -3.239 1.00 26.99 ? 87 GLU B O 1 ATOM 2219 C CB . GLU B 2 89 ? 41.605 5.935 -4.496 1.00 31.92 ? 87 GLU B CB 1 ATOM 2220 C CG . GLU B 2 89 ? 40.792 4.862 -5.197 1.00 40.47 ? 87 GLU B CG 1 ATOM 2221 C CD . GLU B 2 89 ? 41.651 3.975 -6.080 1.00 46.22 ? 87 GLU B CD 1 ATOM 2222 O OE1 . GLU B 2 89 ? 42.829 4.325 -6.309 1.00 48.04 ? 87 GLU B OE1 1 ATOM 2223 O OE2 . GLU B 2 89 ? 41.151 2.929 -6.544 1.00 50.60 ? 87 GLU B OE2 1 ATOM 2224 N N . SER B 2 90 ? 40.150 5.633 -1.700 1.00 30.32 ? 88 SER B N 1 ATOM 2225 C CA . SER B 2 90 ? 39.254 4.804 -0.890 1.00 31.88 ? 88 SER B CA 1 ATOM 2226 C C . SER B 2 90 ? 38.035 5.554 -0.339 1.00 31.36 ? 88 SER B C 1 ATOM 2227 O O . SER B 2 90 ? 36.994 4.950 -0.090 1.00 31.82 ? 88 SER B O 1 ATOM 2228 C CB . SER B 2 90 ? 40.016 4.127 0.251 1.00 28.36 ? 88 SER B CB 1 ATOM 2229 O OG . SER B 2 90 ? 40.297 5.047 1.293 1.00 40.49 ? 88 SER B OG 1 ATOM 2230 N N . PHE B 2 91 ? 38.166 6.864 -0.148 1.00 32.55 ? 89 PHE B N 1 ATOM 2231 C CA . PHE B 2 91 ? 37.065 7.659 0.402 1.00 31.84 ? 89 PHE B CA 1 ATOM 2232 C C . PHE B 2 91 ? 36.518 8.743 -0.530 1.00 30.41 ? 89 PHE B C 1 ATOM 2233 O O . PHE B 2 91 ? 35.705 9.571 -0.117 1.00 28.46 ? 89 PHE B O 1 ATOM 2234 C CB . PHE B 2 91 ? 37.444 8.261 1.758 1.00 25.10 ? 89 PHE B CB 1 ATOM 2235 C CG . PHE B 2 91 ? 38.691 9.103 1.728 1.00 23.84 ? 89 PHE B CG 1 ATOM 2236 C CD1 . PHE B 2 91 ? 38.619 10.453 1.430 1.00 22.19 ? 89 PHE B CD1 1 ATOM 2237 C CD2 . PHE B 2 91 ? 39.930 8.550 2.017 1.00 31.13 ? 89 PHE B CD2 1 ATOM 2238 C CE1 . PHE B 2 91 ? 39.757 11.238 1.407 1.00 24.83 ? 89 PHE B CE1 1 ATOM 2239 C CE2 . PHE B 2 91 ? 41.076 9.333 1.996 1.00 28.80 ? 89 PHE B CE2 1 ATOM 2240 C CZ . PHE B 2 91 ? 40.988 10.678 1.691 1.00 27.81 ? 89 PHE B CZ 1 ATOM 2241 N N . THR B 2 92 ? 36.974 8.750 -1.777 1.00 26.78 ? 90 THR B N 1 ATOM 2242 C CA . THR B 2 92 ? 36.472 9.706 -2.757 1.00 26.61 ? 90 THR B CA 1 ATOM 2243 C C . THR B 2 92 ? 35.940 8.955 -3.968 1.00 26.97 ? 90 THR B C 1 ATOM 2244 O O . THR B 2 92 ? 34.728 8.888 -4.185 1.00 27.16 ? 90 THR B O 1 ATOM 2245 C CB . THR B 2 92 ? 37.566 10.694 -3.205 1.00 23.42 ? 90 THR B CB 1 ATOM 2246 O OG1 . THR B 2 92 ? 38.680 9.966 -3.734 1.00 22.10 ? 90 THR B OG1 1 ATOM 2247 C CG2 . THR B 2 92 ? 38.031 11.545 -2.033 1.00 22.12 ? 90 THR B CG2 1 ATOM 2248 N N . VAL B 2 93 ? 36.856 8.400 -4.756 1.00 26.65 ? 91 VAL B N 1 ATOM 2249 C CA . VAL B 2 93 ? 36.508 7.604 -5.923 1.00 25.27 ? 91 VAL B CA 1 ATOM 2250 C C . VAL B 2 93 ? 35.554 6.471 -5.560 1.00 25.41 ? 91 VAL B C 1 ATOM 2251 O O . VAL B 2 93 ? 34.583 6.203 -6.269 1.00 22.68 ? 91 VAL B O 1 ATOM 2252 C CB . VAL B 2 93 ? 37.772 7.010 -6.582 1.00 24.70 ? 91 VAL B CB 1 ATOM 2253 C CG1 . VAL B 2 93 ? 37.390 6.044 -7.696 1.00 22.69 ? 91 VAL B CG1 1 ATOM 2254 C CG2 . VAL B 2 93 ? 38.662 8.115 -7.117 1.00 20.52 ? 91 VAL B CG2 1 ATOM 2255 N N . GLN B 2 94 ? 35.831 5.818 -4.439 1.00 27.86 ? 92 GLN B N 1 ATOM 2256 C CA . GLN B 2 94 ? 35.062 4.653 -4.022 1.00 30.00 ? 92 GLN B CA 1 ATOM 2257 C C . GLN B 2 94 ? 33.891 4.996 -3.101 1.00 28.11 ? 92 GLN B C 1 ATOM 2258 O O . GLN B 2 94 ? 33.185 4.100 -2.636 1.00 32.14 ? 92 GLN B O 1 ATOM 2259 C CB . GLN B 2 94 ? 35.983 3.625 -3.355 1.00 30.81 ? 92 GLN B CB 1 ATOM 2260 C CG . GLN B 2 94 ? 37.065 3.103 -4.295 1.00 33.27 ? 92 GLN B CG 1 ATOM 2261 C CD . GLN B 2 94 ? 38.044 2.161 -3.619 1.00 39.29 ? 92 GLN B CD 1 ATOM 2262 O OE1 . GLN B 2 94 ? 37.862 1.777 -2.463 1.00 43.30 ? 92 GLN B OE1 1 ATOM 2263 N NE2 . GLN B 2 94 ? 39.095 1.788 -4.340 1.00 40.10 ? 92 GLN B NE2 1 ATOM 2264 N N . ARG B 2 95 ? 33.693 6.284 -2.824 1.00 24.19 ? 93 ARG B N 1 ATOM 2265 C CA . ARG B 2 95 ? 32.599 6.698 -1.944 1.00 24.16 ? 93 ARG B CA 1 ATOM 2266 C C . ARG B 2 95 ? 31.241 6.410 -2.569 1.00 22.42 ? 93 ARG B C 1 ATOM 2267 O O . ARG B 2 95 ? 30.965 6.843 -3.689 1.00 22.76 ? 93 ARG B O 1 ATOM 2268 C CB . ARG B 2 95 ? 32.715 8.185 -1.601 1.00 23.42 ? 93 ARG B CB 1 ATOM 2269 C CG . ARG B 2 95 ? 31.597 8.716 -0.721 1.00 21.61 ? 93 ARG B CG 1 ATOM 2270 C CD . ARG B 2 95 ? 31.807 10.187 -0.399 1.00 20.46 ? 93 ARG B CD 1 ATOM 2271 N NE . ARG B 2 95 ? 30.639 10.780 0.243 1.00 17.51 ? 93 ARG B NE 1 ATOM 2272 C CZ . ARG B 2 95 ? 30.345 10.664 1.533 1.00 18.87 ? 93 ARG B CZ 1 ATOM 2273 N NH1 . ARG B 2 95 ? 31.141 9.974 2.340 1.00 19.66 ? 93 ARG B NH1 1 ATOM 2274 N NH2 . ARG B 2 95 ? 29.257 11.246 2.020 1.00 16.02 ? 93 ARG B NH2 1 ATOM 2275 N N . ARG B 2 96 ? 30.391 5.684 -1.848 1.00 25.38 ? 94 ARG B N 1 ATOM 2276 C CA . ARG B 2 96 ? 29.052 5.383 -2.341 1.00 26.93 ? 94 ARG B CA 1 ATOM 2277 C C . ARG B 2 96 ? 27.990 5.442 -1.242 1.00 24.81 ? 94 ARG B C 1 ATOM 2278 O O . ARG B 2 96 ? 28.078 4.677 -0.282 1.00 25.21 ? 94 ARG B O 1 ATOM 2279 C CB . ARG B 2 96 ? 29.035 3.969 -2.927 1.00 31.84 ? 94 ARG B CB 1 ATOM 2280 C CG . ARG B 2 96 ? 30.005 3.768 -4.082 1.00 38.37 ? 94 ARG B CG 1 ATOM 2281 C CD . ARG B 2 96 ? 29.491 4.349 -5.382 1.00 43.30 ? 94 ARG B CD 1 ATOM 2282 N NE . ARG B 2 96 ? 30.353 3.987 -6.504 1.00 50.49 ? 94 ARG B NE 1 ATOM 2283 C CZ . ARG B 2 96 ? 30.231 2.872 -7.216 1.00 57.97 ? 94 ARG B CZ 1 ATOM 2284 N NH1 . ARG B 2 96 ? 29.277 1.997 -6.930 1.00 58.91 ? 94 ARG B NH1 1 ATOM 2285 N NH2 . ARG B 2 96 ? 31.067 2.632 -8.218 1.00 61.33 ? 94 ARG B NH2 1 ATOM 2286 N N . VAL B 2 97 ? 26.998 6.323 -1.342 1.00 20.18 ? 95 VAL B N 1 ATOM 2287 C CA . VAL B 2 97 ? 25.946 6.293 -0.326 1.00 21.87 ? 95 VAL B CA 1 ATOM 2288 C C . VAL B 2 97 ? 24.586 6.236 -1.015 1.00 21.59 ? 95 VAL B C 1 ATOM 2289 O O . VAL B 2 97 ? 24.293 7.116 -1.831 1.00 18.94 ? 95 VAL B O 1 ATOM 2290 C CB . VAL B 2 97 ? 26.002 7.556 0.573 1.00 32.98 ? 95 VAL B CB 1 ATOM 2291 C CG1 . VAL B 2 97 ? 24.961 7.483 1.678 1.00 35.89 ? 95 VAL B CG1 1 ATOM 2292 C CG2 . VAL B 2 97 ? 27.400 7.767 1.144 1.00 33.96 ? 95 VAL B CG2 1 ATOM 2293 N N . TYR B 2 98 ? 23.764 5.216 -0.727 1.00 24.67 ? 96 TYR B N 1 ATOM 2294 C CA . TYR B 2 98 ? 22.446 5.178 -1.364 1.00 27.20 ? 96 TYR B CA 1 ATOM 2295 C C . TYR B 2 98 ? 21.681 6.431 -0.937 1.00 25.81 ? 96 TYR B C 1 ATOM 2296 O O . TYR B 2 98 ? 22.033 7.083 0.049 1.00 26.09 ? 96 TYR B O 1 ATOM 2297 C CB . TYR B 2 98 ? 21.600 3.949 -0.960 1.00 31.07 ? 96 TYR B CB 1 ATOM 2298 C CG . TYR B 2 98 ? 21.471 3.432 0.454 1.00 30.68 ? 96 TYR B CG 1 ATOM 2299 C CD1 . TYR B 2 98 ? 22.507 2.769 1.091 1.00 26.04 ? 96 TYR B CD1 1 ATOM 2300 C CD2 . TYR B 2 98 ? 20.266 3.579 1.135 1.00 32.30 ? 96 TYR B CD2 1 ATOM 2301 C CE1 . TYR B 2 98 ? 22.345 2.267 2.377 1.00 29.71 ? 96 TYR B CE1 1 ATOM 2302 C CE2 . TYR B 2 98 ? 20.101 3.096 2.416 1.00 35.96 ? 96 TYR B CE2 1 ATOM 2303 C CZ . TYR B 2 98 ? 21.141 2.443 3.035 1.00 35.71 ? 96 TYR B CZ 1 ATOM 2304 O OH . TYR B 2 98 ? 20.967 1.959 4.311 1.00 37.19 ? 96 TYR B OH 1 ATOM 2305 N N . PRO B 2 99 ? 20.621 6.769 -1.682 1.00 23.54 ? 97 PRO B N 1 ATOM 2306 C CA . PRO B 2 99 ? 19.570 7.739 -1.350 1.00 24.36 ? 97 PRO B CA 1 ATOM 2307 C C . PRO B 2 99 ? 18.443 7.213 -0.457 1.00 24.41 ? 97 PRO B C 1 ATOM 2308 O O . PRO B 2 99 ? 18.054 6.048 -0.548 1.00 21.78 ? 97 PRO B O 1 ATOM 2309 C CB . PRO B 2 99 ? 18.991 8.079 -2.720 1.00 22.83 ? 97 PRO B CB 1 ATOM 2310 C CG . PRO B 2 99 ? 19.227 6.884 -3.540 1.00 22.30 ? 97 PRO B CG 1 ATOM 2311 C CD . PRO B 2 99 ? 20.546 6.354 -3.096 1.00 20.47 ? 97 PRO B CD 1 ATOM 2312 N N . GLU B 2 100 ? 17.924 8.093 0.394 1.00 26.67 ? 98 GLU B N 1 ATOM 2313 C CA . GLU B 2 100 ? 16.658 7.846 1.070 1.00 33.47 ? 98 GLU B CA 1 ATOM 2314 C C . GLU B 2 100 ? 15.577 8.417 0.166 1.00 30.20 ? 98 GLU B C 1 ATOM 2315 O O . GLU B 2 100 ? 15.697 9.543 -0.314 1.00 27.82 ? 98 GLU B O 1 ATOM 2316 C CB . GLU B 2 100 ? 16.615 8.571 2.418 1.00 41.20 ? 98 GLU B CB 1 ATOM 2317 C CG . GLU B 2 100 ? 17.688 8.172 3.414 1.00 48.97 ? 98 GLU B CG 1 ATOM 2318 C CD . GLU B 2 100 ? 17.450 6.804 4.009 1.00 57.92 ? 98 GLU B CD 1 ATOM 2319 O OE1 . GLU B 2 100 ? 18.440 6.103 4.306 1.00 61.81 ? 98 GLU B OE1 1 ATOM 2320 O OE2 . GLU B 2 100 ? 16.271 6.433 4.190 1.00 61.54 ? 98 GLU B OE2 1 ATOM 2321 N N . VAL B 2 101 ? 14.521 7.645 -0.066 1.00 28.47 ? 99 VAL B N 1 ATOM 2322 C CA . VAL B 2 101 ? 13.459 8.084 -0.967 1.00 26.61 ? 99 VAL B CA 1 ATOM 2323 C C . VAL B 2 101 ? 12.096 8.179 -0.290 1.00 27.55 ? 99 VAL B C 1 ATOM 2324 O O . VAL B 2 101 ? 11.603 7.210 0.286 1.00 30.26 ? 99 VAL B O 1 ATOM 2325 C CB . VAL B 2 101 ? 13.358 7.169 -2.207 1.00 24.45 ? 99 VAL B CB 1 ATOM 2326 C CG1 . VAL B 2 101 ? 12.317 7.704 -3.179 1.00 18.82 ? 99 VAL B CG1 1 ATOM 2327 C CG2 . VAL B 2 101 ? 14.712 7.041 -2.887 1.00 20.63 ? 99 VAL B CG2 1 ATOM 2328 N N . THR B 2 102 ? 11.498 9.361 -0.374 1.00 25.44 ? 100 THR B N 1 ATOM 2329 C CA . THR B 2 102 ? 10.187 9.622 0.204 1.00 33.56 ? 100 THR B CA 1 ATOM 2330 C C . THR B 2 102 ? 9.260 10.187 -0.864 1.00 33.66 ? 100 THR B C 1 ATOM 2331 O O . THR B 2 102 ? 9.654 11.060 -1.638 1.00 33.58 ? 100 THR B O 1 ATOM 2332 C CB . THR B 2 102 ? 10.285 10.652 1.339 1.00 38.89 ? 100 THR B CB 1 ATOM 2333 O OG1 . THR B 2 102 ? 11.076 11.764 0.907 1.00 46.14 ? 100 THR B OG1 1 ATOM 2334 C CG2 . THR B 2 102 ? 10.933 10.031 2.565 1.00 39.14 ? 100 THR B CG2 1 ATOM 2335 N N . VAL B 2 103 ? 8.023 9.702 -0.898 1.00 32.79 ? 101 VAL B N 1 ATOM 2336 C CA . VAL B 2 103 ? 7.023 10.281 -1.785 1.00 33.69 ? 101 VAL B CA 1 ATOM 2337 C C . VAL B 2 103 ? 5.910 10.908 -0.952 1.00 36.01 ? 101 VAL B C 1 ATOM 2338 O O . VAL B 2 103 ? 5.349 10.276 -0.056 1.00 39.51 ? 101 VAL B O 1 ATOM 2339 C CB . VAL B 2 103 ? 6.436 9.244 -2.764 1.00 34.88 ? 101 VAL B CB 1 ATOM 2340 C CG1 . VAL B 2 103 ? 5.270 9.845 -3.536 1.00 34.39 ? 101 VAL B CG1 1 ATOM 2341 C CG2 . VAL B 2 103 ? 7.508 8.763 -3.729 1.00 33.33 ? 101 VAL B CG2 1 ATOM 2342 N N . TYR B 2 104 ? 5.603 12.161 -1.265 1.00 33.20 ? 102 TYR B N 1 ATOM 2343 C CA . TYR B 2 104 ? 4.514 12.899 -0.635 1.00 32.12 ? 102 TYR B CA 1 ATOM 2344 C C . TYR B 2 104 ? 3.768 13.797 -1.620 1.00 32.91 ? 102 TYR B C 1 ATOM 2345 O O . TYR B 2 104 ? 4.352 14.285 -2.587 1.00 29.82 ? 102 TYR B O 1 ATOM 2346 C CB . TYR B 2 104 ? 5.039 13.706 0.560 1.00 28.96 ? 102 TYR B CB 1 ATOM 2347 C CG . TYR B 2 104 ? 6.083 14.746 0.215 1.00 27.78 ? 102 TYR B CG 1 ATOM 2348 C CD1 . TYR B 2 104 ? 5.724 16.038 -0.148 1.00 28.25 ? 102 TYR B CD1 1 ATOM 2349 C CD2 . TYR B 2 104 ? 7.436 14.432 0.264 1.00 28.06 ? 102 TYR B CD2 1 ATOM 2350 C CE1 . TYR B 2 104 ? 6.685 16.987 -0.457 1.00 28.71 ? 102 TYR B CE1 1 ATOM 2351 C CE2 . TYR B 2 104 ? 8.401 15.372 -0.044 1.00 27.39 ? 102 TYR B CE2 1 ATOM 2352 C CZ . TYR B 2 104 ? 8.022 16.646 -0.403 1.00 31.50 ? 102 TYR B CZ 1 ATOM 2353 O OH . TYR B 2 104 ? 8.987 17.580 -0.709 1.00 35.35 ? 102 TYR B OH 1 ATOM 2354 N N . PRO B 2 105 ? 2.467 14.018 -1.374 1.00 36.26 ? 103 PRO B N 1 ATOM 2355 C CA . PRO B 2 105 ? 1.690 14.863 -2.282 1.00 36.11 ? 103 PRO B CA 1 ATOM 2356 C C . PRO B 2 105 ? 1.907 16.338 -1.977 1.00 36.86 ? 103 PRO B C 1 ATOM 2357 O O . PRO B 2 105 ? 2.216 16.712 -0.846 1.00 41.28 ? 103 PRO B O 1 ATOM 2358 C CB . PRO B 2 105 ? 0.248 14.464 -1.975 1.00 36.31 ? 103 PRO B CB 1 ATOM 2359 C CG . PRO B 2 105 ? 0.283 14.062 -0.540 1.00 38.08 ? 103 PRO B CG 1 ATOM 2360 C CD . PRO B 2 105 ? 1.624 13.405 -0.331 1.00 37.88 ? 103 PRO B CD 1 ATOM 2361 N N . ALA B 2 106 ? 1.734 17.166 -3.001 1.00 32.37 ? 104 ALA B N 1 ATOM 2362 C CA . ALA B 2 106 ? 1.876 18.609 -2.872 1.00 30.65 ? 104 ALA B CA 1 ATOM 2363 C C . ALA B 2 106 ? 0.886 19.350 -3.757 1.00 35.42 ? 104 ALA B C 1 ATOM 2364 O O . ALA B 2 106 ? 0.037 18.743 -4.411 1.00 32.97 ? 104 ALA B O 1 ATOM 2365 C CB . ALA B 2 106 ? 3.296 19.024 -3.219 1.00 20.01 ? 104 ALA B CB 1 ATOM 2366 N N . LYS B 2 107 ? 1.003 20.672 -3.763 1.00 39.53 ? 105 LYS B N 1 ATOM 2367 C CA . LYS B 2 107 ? 0.108 21.522 -4.528 1.00 41.14 ? 105 LYS B CA 1 ATOM 2368 C C . LYS B 2 107 ? 0.909 22.455 -5.432 1.00 41.34 ? 105 LYS B C 1 ATOM 2369 O O . LYS B 2 107 ? 1.938 23.003 -5.034 1.00 40.01 ? 105 LYS B O 1 ATOM 2370 C CB . LYS B 2 107 ? -0.774 22.347 -3.587 1.00 43.20 ? 105 LYS B CB 1 ATOM 2371 C CG . LYS B 2 107 ? -1.689 21.521 -2.692 1.00 44.80 ? 105 LYS B CG 1 ATOM 2372 C CD . LYS B 2 107 ? -2.481 22.417 -1.751 1.00 46.18 ? 105 LYS B CD 1 ATOM 2373 C CE . LYS B 2 107 ? -3.473 21.625 -0.910 1.00 47.53 ? 105 LYS B CE 1 ATOM 2374 N NZ . LYS B 2 107 ? -4.295 22.516 -0.042 1.00 48.78 ? 105 LYS B NZ 1 ATOM 2375 N N . THR B 2 108 ? 0.418 22.622 -6.655 1.00 45.48 ? 106 THR B N 1 ATOM 2376 C CA . THR B 2 108 ? 0.993 23.553 -7.620 1.00 49.36 ? 106 THR B CA 1 ATOM 2377 C C . THR B 2 108 ? 0.595 24.973 -7.245 1.00 57.32 ? 106 THR B C 1 ATOM 2378 O O . THR B 2 108 ? 1.362 25.920 -7.429 1.00 57.64 ? 106 THR B O 1 ATOM 2379 C CB . THR B 2 108 ? 0.530 23.242 -9.060 1.00 48.18 ? 106 THR B CB 1 ATOM 2380 O OG1 . THR B 2 108 ? -0.903 23.260 -9.126 1.00 48.64 ? 106 THR B OG1 1 ATOM 2381 C CG2 . THR B 2 108 ? 1.035 21.874 -9.502 1.00 47.00 ? 106 THR B CG2 1 ATOM 2382 N N . GLN B 2 109 ? -0.614 25.104 -6.713 1.00 63.76 ? 107 GLN B N 1 ATOM 2383 C CA . GLN B 2 109 ? -1.115 26.376 -6.212 1.00 71.22 ? 107 GLN B CA 1 ATOM 2384 C C . GLN B 2 109 ? -1.726 26.061 -4.847 1.00 77.27 ? 107 GLN B C 1 ATOM 2385 O O . GLN B 2 109 ? -2.332 24.999 -4.680 1.00 78.22 ? 107 GLN B O 1 ATOM 2386 C CB . GLN B 2 109 ? -2.133 26.988 -7.175 1.00 74.05 ? 107 GLN B CB 1 ATOM 2387 C CG . GLN B 2 109 ? -1.525 27.440 -8.502 1.00 74.74 ? 107 GLN B CG 1 ATOM 2388 C CD . GLN B 2 109 ? -2.516 28.139 -9.410 1.00 77.39 ? 107 GLN B CD 1 ATOM 2389 O OE1 . GLN B 2 109 ? -3.390 27.507 -9.997 1.00 78.15 ? 107 GLN B OE1 1 ATOM 2390 N NE2 . GLN B 2 109 ? -2.376 29.455 -9.535 1.00 78.41 ? 107 GLN B NE2 1 ATOM 2391 N N . PRO B 2 110 ? -1.559 26.963 -3.867 1.00 81.39 ? 108 PRO B N 1 ATOM 2392 C CA . PRO B 2 110 ? -1.983 26.726 -2.477 1.00 84.27 ? 108 PRO B CA 1 ATOM 2393 C C . PRO B 2 110 ? -3.441 26.286 -2.268 1.00 87.18 ? 108 PRO B C 1 ATOM 2394 O O . PRO B 2 110 ? -3.682 25.363 -1.487 1.00 88.01 ? 108 PRO B O 1 ATOM 2395 C CB . PRO B 2 110 ? -1.747 28.097 -1.816 1.00 84.28 ? 108 PRO B CB 1 ATOM 2396 C CG . PRO B 2 110 ? -0.694 28.750 -2.654 1.00 81.74 ? 108 PRO B CG 1 ATOM 2397 C CD . PRO B 2 110 ? -0.992 28.315 -4.056 1.00 80.79 ? 108 PRO B CD 1 ATOM 2398 N N . LEU B 2 111 ? -4.385 26.926 -2.949 1.00 88.47 ? 109 LEU B N 1 ATOM 2399 C CA . LEU B 2 111 ? -5.822 26.669 -2.751 1.00 89.06 ? 109 LEU B CA 1 ATOM 2400 C C . LEU B 2 111 ? -6.367 25.332 -3.275 1.00 87.30 ? 109 LEU B C 1 ATOM 2401 O O . LEU B 2 111 ? -7.321 24.787 -2.721 1.00 89.58 ? 109 LEU B O 1 ATOM 2402 C CB . LEU B 2 111 ? -6.633 27.811 -3.371 1.00 90.00 ? 109 LEU B CB 1 ATOM 2403 N N . GLN B 2 112 ? -5.738 24.812 -4.322 1.00 82.40 ? 110 GLN B N 1 ATOM 2404 C CA . GLN B 2 112 ? -6.209 23.622 -5.047 1.00 80.60 ? 110 GLN B CA 1 ATOM 2405 C C . GLN B 2 112 ? -5.949 22.289 -4.366 1.00 76.14 ? 110 GLN B C 1 ATOM 2406 O O . GLN B 2 112 ? -5.098 22.175 -3.492 1.00 78.97 ? 110 GLN B O 1 ATOM 2407 C CB . GLN B 2 112 ? -5.620 23.581 -6.460 1.00 82.42 ? 110 GLN B CB 1 ATOM 2408 C CG . GLN B 2 112 ? -6.385 24.433 -7.452 1.00 87.74 ? 110 GLN B CG 1 ATOM 2409 C CD . GLN B 2 112 ? -5.515 24.959 -8.571 1.00 90.25 ? 110 GLN B CD 1 ATOM 2410 O OE1 . GLN B 2 112 ? -4.558 24.300 -8.984 1.00 88.89 ? 110 GLN B OE1 1 ATOM 2411 N NE2 . GLN B 2 112 ? -5.838 26.144 -9.068 1.00 93.03 ? 110 GLN B NE2 1 ATOM 2412 N N . HIS B 2 113 ? -6.691 21.273 -4.803 1.00 67.90 ? 111 HIS B N 1 ATOM 2413 C CA . HIS B 2 113 ? -6.475 19.925 -4.307 1.00 59.33 ? 111 HIS B CA 1 ATOM 2414 C C . HIS B 2 113 ? -5.102 19.460 -4.735 1.00 52.22 ? 111 HIS B C 1 ATOM 2415 O O . HIS B 2 113 ? -4.452 20.075 -5.586 1.00 51.29 ? 111 HIS B O 1 ATOM 2416 C CB . HIS B 2 113 ? -7.528 18.962 -4.863 1.00 56.74 ? 111 HIS B CB 1 ATOM 2417 C CG . HIS B 2 113 ? -8.914 19.201 -4.359 1.00 57.75 ? 111 HIS B CG 1 ATOM 2418 N ND1 . HIS B 2 113 ? -9.587 20.385 -4.566 1.00 56.57 ? 111 HIS B ND1 1 ATOM 2419 C CD2 . HIS B 2 113 ? -9.775 18.388 -3.703 1.00 60.09 ? 111 HIS B CD2 1 ATOM 2420 C CE1 . HIS B 2 113 ? -10.792 20.301 -4.031 1.00 58.50 ? 111 HIS B CE1 1 ATOM 2421 N NE2 . HIS B 2 113 ? -10.932 19.099 -3.502 1.00 60.84 ? 111 HIS B NE2 1 ATOM 2422 N N . HIS B 2 114 ? -4.656 18.367 -4.134 1.00 49.86 ? 112 HIS B N 1 ATOM 2423 C CA . HIS B 2 114 ? -3.379 17.757 -4.463 1.00 49.22 ? 112 HIS B CA 1 ATOM 2424 C C . HIS B 2 114 ? -3.224 17.386 -5.939 1.00 46.84 ? 112 HIS B C 1 ATOM 2425 O O . HIS B 2 114 ? -3.975 16.564 -6.466 1.00 50.19 ? 112 HIS B O 1 ATOM 2426 C CB . HIS B 2 114 ? -3.202 16.497 -3.613 1.00 52.88 ? 112 HIS B CB 1 ATOM 2427 C CG . HIS B 2 114 ? -2.781 16.785 -2.205 1.00 56.25 ? 112 HIS B CG 1 ATOM 2428 N ND1 . HIS B 2 114 ? -3.008 15.914 -1.161 1.00 59.34 ? 112 HIS B ND1 1 ATOM 2429 C CD2 . HIS B 2 114 ? -2.151 17.858 -1.669 1.00 56.86 ? 112 HIS B CD2 1 ATOM 2430 C CE1 . HIS B 2 114 ? -2.531 16.436 -0.044 1.00 60.59 ? 112 HIS B CE1 1 ATOM 2431 N NE2 . HIS B 2 114 ? -2.006 17.615 -0.325 1.00 59.12 ? 112 HIS B NE2 1 ATOM 2432 N N . ASN B 2 115 ? -2.236 17.984 -6.600 1.00 41.26 ? 113 ASN B N 1 ATOM 2433 C CA . ASN B 2 115 ? -2.038 17.767 -8.025 1.00 37.37 ? 113 ASN B CA 1 ATOM 2434 C C . ASN B 2 115 ? -0.555 17.666 -8.344 1.00 32.32 ? 113 ASN B C 1 ATOM 2435 O O . ASN B 2 115 ? -0.138 17.814 -9.494 1.00 29.42 ? 113 ASN B O 1 ATOM 2436 C CB . ASN B 2 115 ? -2.684 18.879 -8.857 1.00 39.01 ? 113 ASN B CB 1 ATOM 2437 C CG . ASN B 2 115 ? -2.029 20.235 -8.648 1.00 41.66 ? 113 ASN B CG 1 ATOM 2438 O OD1 . ASN B 2 115 ? -1.232 20.419 -7.727 1.00 41.71 ? 113 ASN B OD1 1 ATOM 2439 N ND2 . ASN B 2 115 ? -2.373 21.196 -9.497 1.00 46.30 ? 113 ASN B ND2 1 ATOM 2440 N N . LEU B 2 116 ? 0.239 17.404 -7.314 1.00 32.03 ? 114 LEU B N 1 ATOM 2441 C CA . LEU B 2 116 ? 1.676 17.251 -7.479 1.00 32.51 ? 114 LEU B CA 1 ATOM 2442 C C . LEU B 2 116 ? 2.181 16.120 -6.600 1.00 32.03 ? 114 LEU B C 1 ATOM 2443 O O . LEU B 2 116 ? 1.936 16.109 -5.392 1.00 32.67 ? 114 LEU B O 1 ATOM 2444 C CB . LEU B 2 116 ? 2.360 18.562 -7.079 1.00 35.91 ? 114 LEU B CB 1 ATOM 2445 C CG . LEU B 2 116 ? 3.773 18.862 -7.581 1.00 41.78 ? 114 LEU B CG 1 ATOM 2446 C CD1 . LEU B 2 116 ? 3.793 18.940 -9.095 1.00 42.82 ? 114 LEU B CD1 1 ATOM 2447 C CD2 . LEU B 2 116 ? 4.282 20.171 -6.982 1.00 43.09 ? 114 LEU B CD2 1 ATOM 2448 N N . LEU B 2 117 ? 2.898 15.173 -7.194 1.00 27.57 ? 115 LEU B N 1 ATOM 2449 C CA . LEU B 2 117 ? 3.525 14.117 -6.413 1.00 22.32 ? 115 LEU B CA 1 ATOM 2450 C C . LEU B 2 117 ? 5.024 14.360 -6.400 1.00 19.81 ? 115 LEU B C 1 ATOM 2451 O O . LEU B 2 117 ? 5.663 14.431 -7.450 1.00 19.26 ? 115 LEU B O 1 ATOM 2452 C CB . LEU B 2 117 ? 3.217 12.739 -7.000 1.00 19.74 ? 115 LEU B CB 1 ATOM 2453 C CG . LEU B 2 117 ? 1.752 12.304 -6.972 1.00 38.20 ? 115 LEU B CG 1 ATOM 2454 C CD1 . LEU B 2 117 ? 1.609 10.882 -7.488 1.00 39.60 ? 115 LEU B CD1 1 ATOM 2455 C CD2 . LEU B 2 117 ? 1.187 12.422 -5.563 1.00 38.45 ? 115 LEU B CD2 1 ATOM 2456 N N . VAL B 2 118 ? 5.580 14.481 -5.201 1.00 22.57 ? 116 VAL B N 1 ATOM 2457 C CA . VAL B 2 118 ? 7.002 14.741 -5.042 1.00 19.86 ? 116 VAL B CA 1 ATOM 2458 C C . VAL B 2 118 ? 7.780 13.490 -4.673 1.00 22.63 ? 116 VAL B C 1 ATOM 2459 O O . VAL B 2 118 ? 7.479 12.828 -3.681 1.00 22.58 ? 116 VAL B O 1 ATOM 2460 C CB . VAL B 2 118 ? 7.256 15.794 -3.947 1.00 21.03 ? 116 VAL B CB 1 ATOM 2461 C CG1 . VAL B 2 118 ? 8.746 16.101 -3.850 1.00 18.08 ? 116 VAL B CG1 1 ATOM 2462 C CG2 . VAL B 2 118 ? 6.462 17.060 -4.233 1.00 17.34 ? 116 VAL B CG2 1 ATOM 2463 N N . CYS B 2 119 ? 8.789 13.175 -5.474 1.00 21.85 ? 117 CYS B N 1 ATOM 2464 C CA . CYS B 2 119 ? 9.733 12.133 -5.111 1.00 22.57 ? 117 CYS B CA 1 ATOM 2465 C C . CYS B 2 119 ? 10.990 12.807 -4.596 1.00 23.98 ? 117 CYS B C 1 ATOM 2466 O O . CYS B 2 119 ? 11.771 13.363 -5.368 1.00 21.46 ? 117 CYS B O 1 ATOM 2467 C CB . CYS B 2 119 ? 10.061 11.234 -6.300 1.00 16.55 ? 117 CYS B CB 1 ATOM 2468 S SG . CYS B 2 119 ? 11.108 9.834 -5.845 1.00 23.06 ? 117 CYS B SG 1 ATOM 2469 N N . SER B 2 120 ? 11.186 12.744 -3.285 1.00 25.00 ? 118 SER B N 1 ATOM 2470 C CA . SER B 2 120 ? 12.334 13.382 -2.671 1.00 21.07 ? 118 SER B CA 1 ATOM 2471 C C . SER B 2 120 ? 13.446 12.366 -2.491 1.00 21.19 ? 118 SER B C 1 ATOM 2472 O O . SER B 2 120 ? 13.297 11.379 -1.770 1.00 20.30 ? 118 SER B O 1 ATOM 2473 C CB . SER B 2 120 ? 11.946 13.986 -1.320 1.00 24.06 ? 118 SER B CB 1 ATOM 2474 O OG . SER B 2 120 ? 13.015 14.734 -0.769 1.00 25.82 ? 118 SER B OG 1 ATOM 2475 N N . VAL B 2 121 ? 14.567 12.620 -3.155 1.00 18.53 ? 119 VAL B N 1 ATOM 2476 C CA . VAL B 2 121 ? 15.696 11.711 -3.133 1.00 16.26 ? 119 VAL B CA 1 ATOM 2477 C C . VAL B 2 121 ? 16.859 12.396 -2.429 1.00 18.32 ? 119 VAL B C 1 ATOM 2478 O O . VAL B 2 121 ? 17.408 13.369 -2.942 1.00 17.39 ? 119 VAL B O 1 ATOM 2479 C CB . VAL B 2 121 ? 16.093 11.327 -4.573 1.00 17.77 ? 119 VAL B CB 1 ATOM 2480 C CG1 . VAL B 2 121 ? 17.158 10.268 -4.571 1.00 15.70 ? 119 VAL B CG1 1 ATOM 2481 C CG2 . VAL B 2 121 ? 14.871 10.851 -5.349 1.00 19.32 ? 119 VAL B CG2 1 ATOM 2482 N N . ASN B 2 122 ? 17.235 11.894 -1.256 1.00 17.82 ? 120 ASN B N 1 ATOM 2483 C CA . ASN B 2 122 ? 18.143 12.629 -0.380 1.00 17.15 ? 120 ASN B CA 1 ATOM 2484 C C . ASN B 2 122 ? 19.371 11.850 0.084 1.00 15.39 ? 120 ASN B C 1 ATOM 2485 O O . ASN B 2 122 ? 19.309 10.644 0.317 1.00 22.03 ? 120 ASN B O 1 ATOM 2486 C CB . ASN B 2 122 ? 17.386 13.111 0.859 1.00 19.28 ? 120 ASN B CB 1 ATOM 2487 C CG . ASN B 2 122 ? 16.213 14.004 0.514 1.00 20.86 ? 120 ASN B CG 1 ATOM 2488 O OD1 . ASN B 2 122 ? 15.108 13.529 0.258 1.00 23.33 ? 120 ASN B OD1 1 ATOM 2489 N ND2 . ASN B 2 122 ? 16.452 15.311 0.500 1.00 22.33 ? 120 ASN B ND2 1 ATOM 2490 N N . GLY B 2 123 ? 20.486 12.564 0.217 1.00 19.46 ? 121 GLY B N 1 ATOM 2491 C CA . GLY B 2 123 ? 21.659 12.055 0.905 1.00 15.27 ? 121 GLY B CA 1 ATOM 2492 C C . GLY B 2 123 ? 22.575 11.142 0.113 1.00 19.28 ? 121 GLY B C 1 ATOM 2493 O O . GLY B 2 123 ? 23.372 10.408 0.698 1.00 19.05 ? 121 GLY B O 1 ATOM 2494 N N . PHE B 2 124 ? 22.470 11.171 -1.211 1.00 18.38 ? 122 PHE B N 1 ATOM 2495 C CA . PHE B 2 124 ? 23.217 10.213 -2.025 1.00 20.36 ? 122 PHE B CA 1 ATOM 2496 C C . PHE B 2 124 ? 24.563 10.740 -2.536 1.00 21.79 ? 122 PHE B C 1 ATOM 2497 O O . PHE B 2 124 ? 24.790 11.944 -2.611 1.00 23.71 ? 122 PHE B O 1 ATOM 2498 C CB . PHE B 2 124 ? 22.366 9.685 -3.183 1.00 17.11 ? 122 PHE B CB 1 ATOM 2499 C CG . PHE B 2 124 ? 21.853 10.758 -4.103 1.00 14.94 ? 122 PHE B CG 1 ATOM 2500 C CD1 . PHE B 2 124 ? 20.674 11.428 -3.823 1.00 13.87 ? 122 PHE B CD1 1 ATOM 2501 C CD2 . PHE B 2 124 ? 22.545 11.076 -5.258 1.00 13.67 ? 122 PHE B CD2 1 ATOM 2502 C CE1 . PHE B 2 124 ? 20.200 12.407 -4.678 1.00 15.42 ? 122 PHE B CE1 1 ATOM 2503 C CE2 . PHE B 2 124 ? 22.075 12.055 -6.117 1.00 16.24 ? 122 PHE B CE2 1 ATOM 2504 C CZ . PHE B 2 124 ? 20.900 12.721 -5.824 1.00 15.96 ? 122 PHE B CZ 1 ATOM 2505 N N . TYR B 2 125 ? 25.440 9.804 -2.881 1.00 19.54 ? 123 TYR B N 1 ATOM 2506 C CA . TYR B 2 125 ? 26.719 10.109 -3.514 1.00 16.96 ? 123 TYR B CA 1 ATOM 2507 C C . TYR B 2 125 ? 27.188 8.895 -4.308 1.00 20.03 ? 123 TYR B C 1 ATOM 2508 O O . TYR B 2 125 ? 27.090 7.769 -3.834 1.00 19.33 ? 123 TYR B O 1 ATOM 2509 C CB . TYR B 2 125 ? 27.772 10.468 -2.471 1.00 16.48 ? 123 TYR B CB 1 ATOM 2510 C CG . TYR B 2 125 ? 29.039 11.054 -3.064 1.00 17.03 ? 123 TYR B CG 1 ATOM 2511 C CD1 . TYR B 2 125 ? 30.068 10.229 -3.503 1.00 15.10 ? 123 TYR B CD1 1 ATOM 2512 C CD2 . TYR B 2 125 ? 29.198 12.428 -3.207 1.00 19.91 ? 123 TYR B CD2 1 ATOM 2513 C CE1 . TYR B 2 125 ? 31.218 10.750 -4.058 1.00 20.10 ? 123 TYR B CE1 1 ATOM 2514 C CE2 . TYR B 2 125 ? 30.353 12.961 -3.761 1.00 18.97 ? 123 TYR B CE2 1 ATOM 2515 C CZ . TYR B 2 125 ? 31.358 12.113 -4.185 1.00 20.78 ? 123 TYR B CZ 1 ATOM 2516 O OH . TYR B 2 125 ? 32.509 12.630 -4.735 1.00 24.75 ? 123 TYR B OH 1 ATOM 2517 N N . PRO B 2 126 ? 27.713 9.121 -5.522 1.00 22.04 ? 124 PRO B N 1 ATOM 2518 C CA . PRO B 2 126 ? 27.915 10.419 -6.179 1.00 21.69 ? 124 PRO B CA 1 ATOM 2519 C C . PRO B 2 126 ? 26.653 11.008 -6.804 1.00 19.81 ? 124 PRO B C 1 ATOM 2520 O O . PRO B 2 126 ? 25.552 10.526 -6.547 1.00 19.60 ? 124 PRO B O 1 ATOM 2521 C CB . PRO B 2 126 ? 28.960 10.101 -7.262 1.00 20.69 ? 124 PRO B CB 1 ATOM 2522 C CG . PRO B 2 126 ? 28.707 8.669 -7.589 1.00 15.93 ? 124 PRO B CG 1 ATOM 2523 C CD . PRO B 2 126 ? 28.309 8.019 -6.297 1.00 16.18 ? 124 PRO B CD 1 ATOM 2524 N N . GLY B 2 127 ? 26.833 12.050 -7.612 1.00 17.09 ? 125 GLY B N 1 ATOM 2525 C CA . GLY B 2 127 ? 25.730 12.841 -8.123 1.00 20.69 ? 125 GLY B CA 1 ATOM 2526 C C . GLY B 2 127 ? 24.937 12.180 -9.231 1.00 22.44 ? 125 GLY B C 1 ATOM 2527 O O . GLY B 2 127 ? 23.764 12.495 -9.434 1.00 28.48 ? 125 GLY B O 1 ATOM 2528 N N . SER B 2 128 ? 25.581 11.276 -9.962 1.00 20.31 ? 126 SER B N 1 ATOM 2529 C CA . SER B 2 128 ? 24.931 10.612 -11.086 1.00 26.38 ? 126 SER B CA 1 ATOM 2530 C C . SER B 2 128 ? 23.737 9.804 -10.593 1.00 26.28 ? 126 SER B C 1 ATOM 2531 O O . SER B 2 128 ? 23.887 8.875 -9.798 1.00 29.97 ? 126 SER B O 1 ATOM 2532 C CB . SER B 2 128 ? 25.910 9.689 -11.810 1.00 33.13 ? 126 SER B CB 1 ATOM 2533 O OG . SER B 2 128 ? 25.273 9.031 -12.890 1.00 40.47 ? 126 SER B OG 1 ATOM 2534 N N . ILE B 2 129 ? 22.552 10.168 -11.071 1.00 21.64 ? 127 ILE B N 1 ATOM 2535 C CA . ILE B 2 129 ? 21.322 9.499 -10.664 1.00 22.26 ? 127 ILE B CA 1 ATOM 2536 C C . ILE B 2 129 ? 20.239 9.574 -11.742 1.00 19.97 ? 127 ILE B C 1 ATOM 2537 O O . ILE B 2 129 ? 20.209 10.508 -12.545 1.00 17.70 ? 127 ILE B O 1 ATOM 2538 C CB . ILE B 2 129 ? 20.794 10.081 -9.329 1.00 19.45 ? 127 ILE B CB 1 ATOM 2539 C CG1 . ILE B 2 129 ? 19.886 9.075 -8.616 1.00 18.37 ? 127 ILE B CG1 1 ATOM 2540 C CG2 . ILE B 2 129 ? 20.082 11.410 -9.557 1.00 13.64 ? 127 ILE B CG2 1 ATOM 2541 C CD1 . ILE B 2 129 ? 19.649 9.403 -7.161 1.00 17.33 ? 127 ILE B CD1 1 ATOM 2542 N N . GLU B 2 130 ? 19.367 8.571 -11.765 1.00 21.70 ? 128 GLU B N 1 ATOM 2543 C CA . GLU B 2 130 ? 18.234 8.567 -12.680 1.00 23.29 ? 128 GLU B CA 1 ATOM 2544 C C . GLU B 2 130 ? 16.956 8.295 -11.896 1.00 20.11 ? 128 GLU B C 1 ATOM 2545 O O . GLU B 2 130 ? 16.832 7.268 -11.229 1.00 22.19 ? 128 GLU B O 1 ATOM 2546 C CB . GLU B 2 130 ? 18.422 7.506 -13.765 1.00 27.18 ? 128 GLU B CB 1 ATOM 2547 C CG . GLU B 2 130 ? 17.269 7.412 -14.752 1.00 34.04 ? 128 GLU B CG 1 ATOM 2548 C CD . GLU B 2 130 ? 17.437 8.348 -15.932 1.00 38.42 ? 128 GLU B CD 1 ATOM 2549 O OE1 . GLU B 2 130 ? 16.415 8.842 -16.455 1.00 38.45 ? 128 GLU B OE1 1 ATOM 2550 O OE2 . GLU B 2 130 ? 18.593 8.595 -16.334 1.00 38.86 ? 128 GLU B OE2 1 ATOM 2551 N N . VAL B 2 131 ? 16.008 9.221 -11.986 1.00 16.80 ? 129 VAL B N 1 ATOM 2552 C CA . VAL B 2 131 ? 14.737 9.094 -11.284 1.00 19.98 ? 129 VAL B CA 1 ATOM 2553 C C . VAL B 2 131 ? 13.585 9.113 -12.279 1.00 21.12 ? 129 VAL B C 1 ATOM 2554 O O . VAL B 2 131 ? 13.489 10.015 -13.110 1.00 21.82 ? 129 VAL B O 1 ATOM 2555 C CB . VAL B 2 131 ? 14.541 10.246 -10.286 1.00 21.27 ? 129 VAL B CB 1 ATOM 2556 C CG1 . VAL B 2 131 ? 13.258 10.051 -9.497 1.00 15.62 ? 129 VAL B CG1 1 ATOM 2557 C CG2 . VAL B 2 131 ? 15.737 10.345 -9.348 1.00 14.79 ? 129 VAL B CG2 1 ATOM 2558 N N . ARG B 2 132 ? 12.715 8.113 -12.197 1.00 21.19 ? 130 ARG B N 1 ATOM 2559 C CA . ARG B 2 132 ? 11.593 8.005 -13.122 1.00 26.05 ? 130 ARG B CA 1 ATOM 2560 C C . ARG B 2 132 ? 10.273 7.756 -12.402 1.00 25.11 ? 130 ARG B C 1 ATOM 2561 O O . ARG B 2 132 ? 10.235 7.121 -11.348 1.00 25.93 ? 130 ARG B O 1 ATOM 2562 C CB . ARG B 2 132 ? 11.852 6.908 -14.155 1.00 33.37 ? 130 ARG B CB 1 ATOM 2563 C CG . ARG B 2 132 ? 13.018 7.222 -15.075 1.00 41.44 ? 130 ARG B CG 1 ATOM 2564 C CD . ARG B 2 132 ? 13.290 6.098 -16.053 1.00 48.62 ? 130 ARG B CD 1 ATOM 2565 N NE . ARG B 2 132 ? 14.379 6.444 -16.961 1.00 54.09 ? 130 ARG B NE 1 ATOM 2566 C CZ . ARG B 2 132 ? 14.205 6.998 -18.156 1.00 56.04 ? 130 ARG B CZ 1 ATOM 2567 N NH1 . ARG B 2 132 ? 12.983 7.274 -18.589 1.00 58.42 ? 130 ARG B NH1 1 ATOM 2568 N NH2 . ARG B 2 132 ? 15.253 7.281 -18.917 1.00 56.08 ? 130 ARG B NH2 1 ATOM 2569 N N . TRP B 2 133 ? 9.191 8.260 -12.986 1.00 20.42 ? 131 TRP B N 1 ATOM 2570 C CA . TRP B 2 133 ? 7.860 8.084 -12.425 1.00 21.03 ? 131 TRP B CA 1 ATOM 2571 C C . TRP B 2 133 ? 7.055 7.050 -13.193 1.00 25.83 ? 131 TRP B C 1 ATOM 2572 O O . TRP B 2 133 ? 7.164 6.946 -14.414 1.00 30.55 ? 131 TRP B O 1 ATOM 2573 C CB . TRP B 2 133 ? 7.098 9.412 -12.431 1.00 18.67 ? 131 TRP B CB 1 ATOM 2574 C CG . TRP B 2 133 ? 7.306 10.259 -11.223 1.00 22.72 ? 131 TRP B CG 1 ATOM 2575 C CD1 . TRP B 2 133 ? 8.024 11.416 -11.148 1.00 20.76 ? 131 TRP B CD1 1 ATOM 2576 C CD2 . TRP B 2 133 ? 6.769 10.033 -9.914 1.00 22.17 ? 131 TRP B CD2 1 ATOM 2577 N NE1 . TRP B 2 133 ? 7.976 11.920 -9.871 1.00 16.69 ? 131 TRP B NE1 1 ATOM 2578 C CE2 . TRP B 2 133 ? 7.212 11.089 -9.094 1.00 21.87 ? 131 TRP B CE2 1 ATOM 2579 C CE3 . TRP B 2 133 ? 5.962 9.038 -9.356 1.00 19.51 ? 131 TRP B CE3 1 ATOM 2580 C CZ2 . TRP B 2 133 ? 6.874 11.178 -7.745 1.00 17.93 ? 131 TRP B CZ2 1 ATOM 2581 C CZ3 . TRP B 2 133 ? 5.628 9.128 -8.015 1.00 19.86 ? 131 TRP B CZ3 1 ATOM 2582 C CH2 . TRP B 2 133 ? 6.084 10.191 -7.226 1.00 19.08 ? 131 TRP B CH2 1 ATOM 2583 N N . PHE B 2 134 ? 6.248 6.282 -12.469 1.00 25.10 ? 132 PHE B N 1 ATOM 2584 C CA . PHE B 2 134 ? 5.378 5.297 -13.091 1.00 26.16 ? 132 PHE B CA 1 ATOM 2585 C C . PHE B 2 134 ? 3.966 5.429 -12.540 1.00 31.80 ? 132 PHE B C 1 ATOM 2586 O O . PHE B 2 134 ? 3.777 5.640 -11.343 1.00 30.38 ? 132 PHE B O 1 ATOM 2587 C CB . PHE B 2 134 ? 5.895 3.876 -12.847 1.00 27.75 ? 132 PHE B CB 1 ATOM 2588 C CG . PHE B 2 134 ? 7.202 3.572 -13.525 1.00 30.14 ? 132 PHE B CG 1 ATOM 2589 C CD1 . PHE B 2 134 ? 8.404 3.976 -12.966 1.00 26.38 ? 132 PHE B CD1 1 ATOM 2590 C CD2 . PHE B 2 134 ? 7.229 2.855 -14.711 1.00 30.93 ? 132 PHE B CD2 1 ATOM 2591 C CE1 . PHE B 2 134 ? 9.606 3.689 -13.588 1.00 26.65 ? 132 PHE B CE1 1 ATOM 2592 C CE2 . PHE B 2 134 ? 8.427 2.564 -15.338 1.00 28.63 ? 132 PHE B CE2 1 ATOM 2593 C CZ . PHE B 2 134 ? 9.616 2.982 -14.776 1.00 23.80 ? 132 PHE B CZ 1 ATOM 2594 N N . ARG B 2 135 ? 2.978 5.301 -13.417 1.00 37.38 ? 133 ARG B N 1 ATOM 2595 C CA . ARG B 2 135 ? 1.585 5.261 -13.000 1.00 40.38 ? 133 ARG B CA 1 ATOM 2596 C C . ARG B 2 135 ? 1.044 3.903 -13.428 1.00 43.99 ? 133 ARG B C 1 ATOM 2597 O O . ARG B 2 135 ? 0.965 3.607 -14.621 1.00 45.86 ? 133 ARG B O 1 ATOM 2598 C CB . ARG B 2 135 ? 0.774 6.398 -13.625 1.00 41.91 ? 133 ARG B CB 1 ATOM 2599 C CG . ARG B 2 135 ? -0.686 6.401 -13.178 1.00 45.53 ? 133 ARG B CG 1 ATOM 2600 C CD . ARG B 2 135 ? -1.563 7.344 -13.991 1.00 50.70 ? 133 ARG B CD 1 ATOM 2601 N NE . ARG B 2 135 ? -1.507 7.097 -15.427 1.00 60.18 ? 133 ARG B NE 1 ATOM 2602 C CZ . ARG B 2 135 ? -0.794 7.827 -16.279 1.00 66.74 ? 133 ARG B CZ 1 ATOM 2603 N NH1 . ARG B 2 135 ? -0.070 8.848 -15.837 1.00 64.30 ? 133 ARG B NH1 1 ATOM 2604 N NH2 . ARG B 2 135 ? -0.801 7.536 -17.573 1.00 71.23 ? 133 ARG B NH2 1 ATOM 2605 N N . ASN B 2 136 ? 0.662 3.092 -12.447 1.00 45.79 ? 134 ASN B N 1 ATOM 2606 C CA . ASN B 2 136 ? 0.223 1.714 -12.668 1.00 45.92 ? 134 ASN B CA 1 ATOM 2607 C C . ASN B 2 136 ? 1.157 0.876 -13.548 1.00 46.12 ? 134 ASN B C 1 ATOM 2608 O O . ASN B 2 136 ? 0.708 0.127 -14.416 1.00 48.78 ? 134 ASN B O 1 ATOM 2609 C CB . ASN B 2 136 ? -1.190 1.698 -13.262 1.00 45.28 ? 134 ASN B CB 1 ATOM 2610 C CG . ASN B 2 136 ? -2.223 2.297 -12.331 1.00 41.83 ? 134 ASN B CG 1 ATOM 2611 O OD1 . ASN B 2 136 ? -2.157 2.128 -11.115 1.00 38.40 ? 134 ASN B OD1 1 ATOM 2612 N ND2 . ASN B 2 136 ? -3.191 3.005 -12.903 1.00 42.39 ? 134 ASN B ND2 1 ATOM 2613 N N . GLY B 2 137 ? 2.459 1.008 -13.307 1.00 44.52 ? 135 GLY B N 1 ATOM 2614 C CA . GLY B 2 137 ? 3.471 0.207 -13.976 1.00 44.24 ? 135 GLY B CA 1 ATOM 2615 C C . GLY B 2 137 ? 3.947 0.725 -15.320 1.00 45.64 ? 135 GLY B C 1 ATOM 2616 O O . GLY B 2 137 ? 4.837 0.142 -15.940 1.00 48.50 ? 135 GLY B O 1 ATOM 2617 N N . GLN B 2 138 ? 3.357 1.826 -15.768 1.00 44.00 ? 136 GLN B N 1 ATOM 2618 C CA . GLN B 2 138 ? 3.738 2.445 -17.030 1.00 45.79 ? 136 GLN B CA 1 ATOM 2619 C C . GLN B 2 138 ? 4.466 3.750 -16.741 1.00 41.41 ? 136 GLN B C 1 ATOM 2620 O O . GLN B 2 138 ? 3.989 4.563 -15.949 1.00 41.99 ? 136 GLN B O 1 ATOM 2621 C CB . GLN B 2 138 ? 2.503 2.720 -17.885 1.00 52.02 ? 136 GLN B CB 1 ATOM 2622 C CG . GLN B 2 138 ? 2.794 3.539 -19.133 1.00 58.15 ? 136 GLN B CG 1 ATOM 2623 C CD . GLN B 2 138 ? 1.786 3.298 -20.236 1.00 64.81 ? 136 GLN B CD 1 ATOM 2624 O OE1 . GLN B 2 138 ? 1.141 2.251 -20.284 1.00 69.41 ? 136 GLN B OE1 1 ATOM 2625 N NE2 . GLN B 2 138 ? 1.644 4.268 -21.133 1.00 64.24 ? 136 GLN B NE2 1 ATOM 2626 N N . GLU B 2 139 ? 5.617 3.955 -17.373 1.00 36.32 ? 137 GLU B N 1 ATOM 2627 C CA . GLU B 2 139 ? 6.381 5.172 -17.127 1.00 36.44 ? 137 GLU B CA 1 ATOM 2628 C C . GLU B 2 139 ? 5.623 6.393 -17.623 1.00 35.51 ? 137 GLU B C 1 ATOM 2629 O O . GLU B 2 139 ? 5.098 6.411 -18.736 1.00 38.71 ? 137 GLU B O 1 ATOM 2630 C CB . GLU B 2 139 ? 7.785 5.131 -17.740 1.00 33.31 ? 137 GLU B CB 1 ATOM 2631 C CG . GLU B 2 139 ? 8.588 6.394 -17.417 1.00 28.60 ? 137 GLU B CG 1 ATOM 2632 C CD . GLU B 2 139 ? 10.015 6.360 -17.926 1.00 28.06 ? 137 GLU B CD 1 ATOM 2633 O OE1 . GLU B 2 139 ? 10.428 5.331 -18.500 1.00 32.11 ? 137 GLU B OE1 1 ATOM 2634 O OE2 . GLU B 2 139 ? 10.726 7.372 -17.749 1.00 28.47 ? 137 GLU B OE2 1 ATOM 2635 N N . GLU B 2 140 ? 5.579 7.414 -16.776 1.00 31.59 ? 138 GLU B N 1 ATOM 2636 C CA . GLU B 2 140 ? 4.973 8.686 -17.130 1.00 32.09 ? 138 GLU B CA 1 ATOM 2637 C C . GLU B 2 140 ? 6.090 9.689 -17.376 1.00 27.54 ? 138 GLU B C 1 ATOM 2638 O O . GLU B 2 140 ? 6.830 10.057 -16.465 1.00 19.40 ? 138 GLU B O 1 ATOM 2639 C CB . GLU B 2 140 ? 4.043 9.172 -16.019 1.00 36.40 ? 138 GLU B CB 1 ATOM 2640 C CG . GLU B 2 140 ? 3.301 10.451 -16.345 1.00 39.73 ? 138 GLU B CG 1 ATOM 2641 C CD . GLU B 2 140 ? 2.481 10.335 -17.611 1.00 43.43 ? 138 GLU B CD 1 ATOM 2642 O OE1 . GLU B 2 140 ? 1.507 9.553 -17.619 1.00 43.83 ? 138 GLU B OE1 1 ATOM 2643 O OE2 . GLU B 2 140 ? 2.810 11.023 -18.599 1.00 43.38 ? 138 GLU B OE2 1 ATOM 2644 N N . LYS B 2 141 ? 6.197 10.125 -18.626 1.00 26.54 ? 139 LYS B N 1 ATOM 2645 C CA . LYS B 2 141 ? 7.235 11.059 -19.044 1.00 28.64 ? 139 LYS B CA 1 ATOM 2646 C C . LYS B 2 141 ? 6.730 12.488 -19.211 1.00 28.73 ? 139 LYS B C 1 ATOM 2647 O O . LYS B 2 141 ? 7.522 13.417 -19.376 1.00 27.58 ? 139 LYS B O 1 ATOM 2648 C CB . LYS B 2 141 ? 7.883 10.576 -20.344 1.00 33.28 ? 139 LYS B CB 1 ATOM 2649 C CG . LYS B 2 141 ? 8.767 9.354 -20.168 1.00 35.55 ? 139 LYS B CG 1 ATOM 2650 C CD . LYS B 2 141 ? 9.475 8.979 -21.459 1.00 39.36 ? 139 LYS B CD 1 ATOM 2651 C CE . LYS B 2 141 ? 10.406 7.797 -21.242 1.00 38.77 ? 139 LYS B CE 1 ATOM 2652 N NZ . LYS B 2 141 ? 10.971 7.283 -22.520 1.00 37.59 ? 139 LYS B NZ 1 ATOM 2653 N N . THR B 2 142 ? 5.414 12.662 -19.167 1.00 29.16 ? 140 THR B N 1 ATOM 2654 C CA . THR B 2 142 ? 4.819 13.987 -19.292 1.00 29.04 ? 140 THR B CA 1 ATOM 2655 C C . THR B 2 142 ? 4.592 14.587 -17.906 1.00 25.74 ? 140 THR B C 1 ATOM 2656 O O . THR B 2 142 ? 4.346 13.863 -16.943 1.00 28.98 ? 140 THR B O 1 ATOM 2657 C CB . THR B 2 142 ? 3.476 13.938 -20.067 1.00 27.66 ? 140 THR B CB 1 ATOM 2658 O OG1 . THR B 2 142 ? 3.678 13.310 -21.338 1.00 25.02 ? 140 THR B OG1 1 ATOM 2659 C CG2 . THR B 2 142 ? 2.901 15.333 -20.285 1.00 29.00 ? 140 THR B CG2 1 ATOM 2660 N N . GLY B 2 143 ? 4.681 15.910 -17.808 1.00 23.76 ? 141 GLY B N 1 ATOM 2661 C CA . GLY B 2 143 ? 4.426 16.598 -16.557 1.00 23.38 ? 141 GLY B CA 1 ATOM 2662 C C . GLY B 2 143 ? 5.473 16.366 -15.486 1.00 25.19 ? 141 GLY B C 1 ATOM 2663 O O . GLY B 2 143 ? 5.166 16.429 -14.295 1.00 27.37 ? 141 GLY B O 1 ATOM 2664 N N . VAL B 2 144 ? 6.711 16.102 -15.892 1.00 24.21 ? 142 VAL B N 1 ATOM 2665 C CA . VAL B 2 144 ? 7.770 15.894 -14.912 1.00 23.15 ? 142 VAL B CA 1 ATOM 2666 C C . VAL B 2 144 ? 8.688 17.106 -14.836 1.00 23.12 ? 142 VAL B C 1 ATOM 2667 O O . VAL B 2 144 ? 9.247 17.548 -15.840 1.00 22.32 ? 142 VAL B O 1 ATOM 2668 C CB . VAL B 2 144 ? 8.598 14.632 -15.230 1.00 21.39 ? 142 VAL B CB 1 ATOM 2669 C CG1 . VAL B 2 144 ? 9.764 14.501 -14.261 1.00 21.84 ? 142 VAL B CG1 1 ATOM 2670 C CG2 . VAL B 2 144 ? 7.719 13.392 -15.181 1.00 20.78 ? 142 VAL B CG2 1 ATOM 2671 N N . VAL B 2 145 ? 8.836 17.631 -13.626 1.00 22.11 ? 143 VAL B N 1 ATOM 2672 C CA . VAL B 2 145 ? 9.698 18.773 -13.367 1.00 22.30 ? 143 VAL B CA 1 ATOM 2673 C C . VAL B 2 145 ? 10.572 18.448 -12.161 1.00 20.00 ? 143 VAL B C 1 ATOM 2674 O O . VAL B 2 145 ? 10.156 17.705 -11.271 1.00 23.07 ? 143 VAL B O 1 ATOM 2675 C CB . VAL B 2 145 ? 8.869 20.052 -13.083 1.00 30.54 ? 143 VAL B CB 1 ATOM 2676 C CG1 . VAL B 2 145 ? 7.976 19.862 -11.862 1.00 28.01 ? 143 VAL B CG1 1 ATOM 2677 C CG2 . VAL B 2 145 ? 9.769 21.270 -12.919 1.00 31.32 ? 143 VAL B CG2 1 ATOM 2678 N N . SER B 2 146 ? 11.787 18.984 -12.132 1.00 16.66 ? 144 SER B N 1 ATOM 2679 C CA . SER B 2 146 ? 12.698 18.686 -11.038 1.00 15.25 ? 144 SER B CA 1 ATOM 2680 C C . SER B 2 146 ? 13.440 19.928 -10.564 1.00 17.98 ? 144 SER B C 1 ATOM 2681 O O . SER B 2 146 ? 13.513 20.933 -11.271 1.00 17.26 ? 144 SER B O 1 ATOM 2682 C CB . SER B 2 146 ? 13.697 17.606 -11.459 1.00 16.01 ? 144 SER B CB 1 ATOM 2683 O OG . SER B 2 146 ? 14.647 17.365 -10.435 1.00 14.76 ? 144 SER B OG 1 ATOM 2684 N N . THR B 2 147 ? 13.991 19.843 -9.357 1.00 17.15 ? 145 THR B N 1 ATOM 2685 C CA . THR B 2 147 ? 14.900 20.855 -8.844 1.00 17.38 ? 145 THR B CA 1 ATOM 2686 C C . THR B 2 147 ? 16.226 20.758 -9.585 1.00 19.91 ? 145 THR B C 1 ATOM 2687 O O . THR B 2 147 ? 17.023 21.695 -9.577 1.00 22.66 ? 145 THR B O 1 ATOM 2688 C CB . THR B 2 147 ? 15.189 20.635 -7.350 1.00 12.19 ? 145 THR B CB 1 ATOM 2689 O OG1 . THR B 2 147 ? 15.674 19.302 -7.144 1.00 14.71 ? 145 THR B OG1 1 ATOM 2690 C CG2 . THR B 2 147 ? 13.929 20.851 -6.522 1.00 13.58 ? 145 THR B CG2 1 ATOM 2691 N N . GLY B 2 148 ? 16.456 19.614 -10.224 1.00 17.53 ? 146 GLY B N 1 ATOM 2692 C CA . GLY B 2 148 ? 17.765 19.275 -10.748 1.00 15.49 ? 146 GLY B CA 1 ATOM 2693 C C . GLY B 2 148 ? 18.632 18.709 -9.644 1.00 17.87 ? 146 GLY B C 1 ATOM 2694 O O . GLY B 2 148 ? 18.152 18.473 -8.536 1.00 17.08 ? 146 GLY B O 1 ATOM 2695 N N . LEU B 2 149 ? 19.908 18.481 -9.938 1.00 17.35 ? 147 LEU B N 1 ATOM 2696 C CA . LEU B 2 149 ? 20.809 17.918 -8.942 1.00 18.08 ? 147 LEU B CA 1 ATOM 2697 C C . LEU B 2 149 ? 21.315 19.003 -8.001 1.00 19.88 ? 147 LEU B C 1 ATOM 2698 O O . LEU B 2 149 ? 21.920 19.986 -8.432 1.00 19.02 ? 147 LEU B O 1 ATOM 2699 C CB . LEU B 2 149 ? 21.989 17.227 -9.623 1.00 18.19 ? 147 LEU B CB 1 ATOM 2700 C CG . LEU B 2 149 ? 22.966 16.534 -8.672 1.00 20.60 ? 147 LEU B CG 1 ATOM 2701 C CD1 . LEU B 2 149 ? 22.280 15.384 -7.948 1.00 18.74 ? 147 LEU B CD1 1 ATOM 2702 C CD2 . LEU B 2 149 ? 24.197 16.047 -9.422 1.00 22.91 ? 147 LEU B CD2 1 ATOM 2703 N N . ILE B 2 150 ? 21.067 18.813 -6.708 1.00 18.70 ? 148 ILE B N 1 ATOM 2704 C CA . ILE B 2 150 ? 21.482 19.774 -5.693 1.00 17.57 ? 148 ILE B CA 1 ATOM 2705 C C . ILE B 2 150 ? 22.618 19.234 -4.834 1.00 17.62 ? 148 ILE B C 1 ATOM 2706 O O . ILE B 2 150 ? 22.494 18.181 -4.209 1.00 16.63 ? 148 ILE B O 1 ATOM 2707 C CB . ILE B 2 150 ? 20.310 20.123 -4.761 1.00 20.06 ? 148 ILE B CB 1 ATOM 2708 C CG1 . ILE B 2 150 ? 19.152 20.723 -5.560 1.00 16.68 ? 148 ILE B CG1 1 ATOM 2709 C CG2 . ILE B 2 150 ? 20.761 21.090 -3.675 1.00 24.42 ? 148 ILE B CG2 1 ATOM 2710 C CD1 . ILE B 2 150 ? 17.896 20.933 -4.746 1.00 21.26 ? 148 ILE B CD1 1 ATOM 2711 N N . GLN B 2 151 ? 23.729 19.962 -4.809 1.00 22.24 ? 149 GLN B N 1 ATOM 2712 C CA . GLN B 2 151 ? 24.824 19.647 -3.903 1.00 23.26 ? 149 GLN B CA 1 ATOM 2713 C C . GLN B 2 151 ? 24.521 20.214 -2.520 1.00 21.24 ? 149 GLN B C 1 ATOM 2714 O O . GLN B 2 151 ? 24.098 21.362 -2.399 1.00 24.80 ? 149 GLN B O 1 ATOM 2715 C CB . GLN B 2 151 ? 26.138 20.218 -4.444 1.00 26.10 ? 149 GLN B CB 1 ATOM 2716 C CG . GLN B 2 151 ? 27.336 19.288 -4.343 1.00 31.39 ? 149 GLN B CG 1 ATOM 2717 C CD . GLN B 2 151 ? 28.478 19.728 -5.241 1.00 35.79 ? 149 GLN B CD 1 ATOM 2718 O OE1 . GLN B 2 151 ? 28.499 20.859 -5.725 1.00 37.21 ? 149 GLN B OE1 1 ATOM 2719 N NE2 . GLN B 2 151 ? 29.432 18.833 -5.472 1.00 35.05 ? 149 GLN B NE2 1 ATOM 2720 N N . ASN B 2 152 ? 24.731 19.412 -1.481 1.00 17.29 ? 150 ASN B N 1 ATOM 2721 C CA . ASN B 2 152 ? 24.491 19.872 -0.115 1.00 17.49 ? 150 ASN B CA 1 ATOM 2722 C C . ASN B 2 152 ? 25.742 20.459 0.531 1.00 21.25 ? 150 ASN B C 1 ATOM 2723 O O . ASN B 2 152 ? 25.677 21.062 1.603 1.00 21.52 ? 150 ASN B O 1 ATOM 2724 C CB . ASN B 2 152 ? 23.933 18.743 0.753 1.00 18.43 ? 150 ASN B CB 1 ATOM 2725 C CG . ASN B 2 152 ? 22.523 18.349 0.359 1.00 21.48 ? 150 ASN B CG 1 ATOM 2726 O OD1 . ASN B 2 152 ? 21.701 19.200 0.018 1.00 22.37 ? 150 ASN B OD1 1 ATOM 2727 N ND2 . ASN B 2 152 ? 22.233 17.055 0.410 1.00 17.21 ? 150 ASN B ND2 1 ATOM 2728 N N . GLY B 2 153 ? 26.880 20.270 -0.130 1.00 17.15 ? 151 GLY B N 1 ATOM 2729 C CA . GLY B 2 153 ? 28.137 20.836 0.324 1.00 16.12 ? 151 GLY B CA 1 ATOM 2730 C C . GLY B 2 153 ? 28.869 19.950 1.314 1.00 20.69 ? 151 GLY B C 1 ATOM 2731 O O . GLY B 2 153 ? 29.960 20.288 1.769 1.00 23.16 ? 151 GLY B O 1 ATOM 2732 N N . ASP B 2 154 ? 28.271 18.810 1.647 1.00 21.76 ? 152 ASP B N 1 ATOM 2733 C CA . ASP B 2 154 ? 28.820 17.930 2.674 1.00 19.55 ? 152 ASP B CA 1 ATOM 2734 C C . ASP B 2 154 ? 29.035 16.514 2.139 1.00 18.32 ? 152 ASP B C 1 ATOM 2735 O O . ASP B 2 154 ? 28.891 15.537 2.878 1.00 22.45 ? 152 ASP B O 1 ATOM 2736 C CB . ASP B 2 154 ? 27.894 17.895 3.897 1.00 21.02 ? 152 ASP B CB 1 ATOM 2737 C CG . ASP B 2 154 ? 26.533 17.287 3.597 1.00 17.94 ? 152 ASP B CG 1 ATOM 2738 O OD1 . ASP B 2 154 ? 26.223 17.032 2.415 1.00 14.13 ? 152 ASP B OD1 1 ATOM 2739 O OD2 . ASP B 2 154 ? 25.770 17.053 4.558 1.00 17.90 ? 152 ASP B OD2 1 ATOM 2740 N N . TRP B 2 155 ? 29.361 16.420 0.851 1.00 16.22 ? 153 TRP B N 1 ATOM 2741 C CA . TRP B 2 155 ? 29.561 15.135 0.175 1.00 17.63 ? 153 TRP B CA 1 ATOM 2742 C C . TRP B 2 155 ? 28.287 14.301 0.057 1.00 17.03 ? 153 TRP B C 1 ATOM 2743 O O . TRP B 2 155 ? 28.342 13.073 -0.002 1.00 18.22 ? 153 TRP B O 1 ATOM 2744 C CB . TRP B 2 155 ? 30.691 14.326 0.823 1.00 19.66 ? 153 TRP B CB 1 ATOM 2745 C CG . TRP B 2 155 ? 32.048 14.905 0.584 1.00 18.73 ? 153 TRP B CG 1 ATOM 2746 C CD1 . TRP B 2 155 ? 32.610 15.977 1.214 1.00 16.96 ? 153 TRP B CD1 1 ATOM 2747 C CD2 . TRP B 2 155 ? 33.024 14.431 -0.350 1.00 18.12 ? 153 TRP B CD2 1 ATOM 2748 N NE1 . TRP B 2 155 ? 33.873 16.205 0.723 1.00 16.79 ? 153 TRP B NE1 1 ATOM 2749 C CE2 . TRP B 2 155 ? 34.152 15.267 -0.237 1.00 16.24 ? 153 TRP B CE2 1 ATOM 2750 C CE3 . TRP B 2 155 ? 33.054 13.381 -1.273 1.00 19.75 ? 153 TRP B CE3 1 ATOM 2751 C CZ2 . TRP B 2 155 ? 35.296 15.087 -1.013 1.00 17.80 ? 153 TRP B CZ2 1 ATOM 2752 C CZ3 . TRP B 2 155 ? 34.189 13.203 -2.040 1.00 19.39 ? 153 TRP B CZ3 1 ATOM 2753 C CH2 . TRP B 2 155 ? 35.294 14.051 -1.906 1.00 18.90 ? 153 TRP B CH2 1 ATOM 2754 N N . THR B 2 156 ? 27.142 14.977 0.024 1.00 15.41 ? 154 THR B N 1 ATOM 2755 C CA . THR B 2 156 ? 25.883 14.325 -0.315 1.00 13.45 ? 154 THR B CA 1 ATOM 2756 C C . THR B 2 156 ? 25.095 15.192 -1.291 1.00 19.51 ? 154 THR B C 1 ATOM 2757 O O . THR B 2 156 ? 25.283 16.406 -1.349 1.00 12.50 ? 154 THR B O 1 ATOM 2758 C CB . THR B 2 156 ? 24.999 14.054 0.924 1.00 14.11 ? 154 THR B CB 1 ATOM 2759 O OG1 . THR B 2 156 ? 24.573 15.299 1.493 1.00 25.65 ? 154 THR B OG1 1 ATOM 2760 C CG2 . THR B 2 156 ? 25.751 13.248 1.976 1.00 14.94 ? 154 THR B CG2 1 ATOM 2761 N N . PHE B 2 157 ? 24.210 14.562 -2.055 1.00 22.88 ? 155 PHE B N 1 ATOM 2762 C CA . PHE B 2 157 ? 23.342 15.288 -2.970 1.00 19.57 ? 155 PHE B CA 1 ATOM 2763 C C . PHE B 2 157 ? 21.887 15.067 -2.610 1.00 17.25 ? 155 PHE B C 1 ATOM 2764 O O . PHE B 2 157 ? 21.556 14.194 -1.807 1.00 18.24 ? 155 PHE B O 1 ATOM 2765 C CB . PHE B 2 157 ? 23.539 14.789 -4.402 1.00 20.83 ? 155 PHE B CB 1 ATOM 2766 C CG . PHE B 2 157 ? 24.885 15.114 -4.987 1.00 19.00 ? 155 PHE B CG 1 ATOM 2767 C CD1 . PHE B 2 157 ? 25.958 14.252 -4.831 1.00 20.86 ? 155 PHE B CD1 1 ATOM 2768 C CD2 . PHE B 2 157 ? 25.064 16.275 -5.721 1.00 16.38 ? 155 PHE B CD2 1 ATOM 2769 C CE1 . PHE B 2 157 ? 27.195 14.554 -5.381 1.00 22.87 ? 155 PHE B CE1 1 ATOM 2770 C CE2 . PHE B 2 157 ? 26.293 16.581 -6.276 1.00 20.54 ? 155 PHE B CE2 1 ATOM 2771 C CZ . PHE B 2 157 ? 27.360 15.722 -6.106 1.00 19.36 ? 155 PHE B CZ 1 ATOM 2772 N N . GLN B 2 158 ? 21.019 15.871 -3.211 1.00 18.79 ? 156 GLN B N 1 ATOM 2773 C CA . GLN B 2 158 ? 19.594 15.595 -3.197 1.00 19.15 ? 156 GLN B CA 1 ATOM 2774 C C . GLN B 2 158 ? 18.958 16.069 -4.498 1.00 20.41 ? 156 GLN B C 1 ATOM 2775 O O . GLN B 2 158 ? 19.545 16.858 -5.238 1.00 16.24 ? 156 GLN B O 1 ATOM 2776 C CB . GLN B 2 158 ? 18.916 16.256 -1.998 1.00 16.77 ? 156 GLN B CB 1 ATOM 2777 C CG . GLN B 2 158 ? 18.993 17.771 -1.999 1.00 18.72 ? 156 GLN B CG 1 ATOM 2778 C CD . GLN B 2 158 ? 18.171 18.399 -0.894 1.00 19.10 ? 156 GLN B CD 1 ATOM 2779 O OE1 . GLN B 2 158 ? 16.941 18.334 -0.906 1.00 24.26 ? 156 GLN B OE1 1 ATOM 2780 N NE2 . GLN B 2 158 ? 18.847 19.007 0.072 1.00 14.52 ? 156 GLN B NE2 1 ATOM 2781 N N . THR B 2 159 ? 17.750 15.589 -4.762 1.00 21.29 ? 157 THR B N 1 ATOM 2782 C CA . THR B 2 159 ? 16.953 16.082 -5.874 1.00 19.63 ? 157 THR B CA 1 ATOM 2783 C C . THR B 2 159 ? 15.480 15.807 -5.614 1.00 20.13 ? 157 THR B C 1 ATOM 2784 O O . THR B 2 159 ? 15.122 14.782 -5.034 1.00 23.46 ? 157 THR B O 1 ATOM 2785 C CB . THR B 2 159 ? 17.377 15.444 -7.218 1.00 19.15 ? 157 THR B CB 1 ATOM 2786 O OG1 . THR B 2 159 ? 16.601 16.007 -8.282 1.00 24.36 ? 157 THR B OG1 1 ATOM 2787 C CG2 . THR B 2 159 ? 17.181 13.935 -7.195 1.00 20.44 ? 157 THR B CG2 1 ATOM 2788 N N . LEU B 2 160 ? 14.625 16.731 -6.031 1.00 18.98 ? 158 LEU B N 1 ATOM 2789 C CA . LEU B 2 160 ? 13.195 16.487 -5.976 1.00 19.41 ? 158 LEU B CA 1 ATOM 2790 C C . LEU B 2 160 ? 12.716 16.278 -7.399 1.00 18.45 ? 158 LEU B C 1 ATOM 2791 O O . LEU B 2 160 ? 13.002 17.087 -8.280 1.00 14.68 ? 158 LEU B O 1 ATOM 2792 C CB . LEU B 2 160 ? 12.448 17.674 -5.363 1.00 20.91 ? 158 LEU B CB 1 ATOM 2793 C CG . LEU B 2 160 ? 12.864 18.182 -3.981 1.00 24.93 ? 158 LEU B CG 1 ATOM 2794 C CD1 . LEU B 2 160 ? 11.820 19.143 -3.429 1.00 26.32 ? 158 LEU B CD1 1 ATOM 2795 C CD2 . LEU B 2 160 ? 13.089 17.032 -3.023 1.00 23.76 ? 158 LEU B CD2 1 ATOM 2796 N N . VAL B 2 161 ? 11.979 15.196 -7.625 1.00 19.19 ? 159 VAL B N 1 ATOM 2797 C CA . VAL B 2 161 ? 11.426 14.942 -8.945 1.00 14.00 ? 159 VAL B CA 1 ATOM 2798 C C . VAL B 2 161 ? 9.920 14.865 -8.806 1.00 21.79 ? 159 VAL B C 1 ATOM 2799 O O . VAL B 2 161 ? 9.370 13.951 -8.188 1.00 22.35 ? 159 VAL B O 1 ATOM 2800 C CB . VAL B 2 161 ? 11.976 13.646 -9.561 1.00 14.51 ? 159 VAL B CB 1 ATOM 2801 C CG1 . VAL B 2 161 ? 11.383 13.427 -10.945 1.00 14.58 ? 159 VAL B CG1 1 ATOM 2802 C CG2 . VAL B 2 161 ? 13.497 13.696 -9.626 1.00 13.71 ? 159 VAL B CG2 1 ATOM 2803 N N . MET B 2 162 ? 9.264 15.848 -9.402 1.00 21.30 ? 160 MET B N 1 ATOM 2804 C CA . MET B 2 162 ? 7.829 16.023 -9.271 1.00 21.87 ? 160 MET B CA 1 ATOM 2805 C C . MET B 2 162 ? 7.029 15.611 -10.501 1.00 22.82 ? 160 MET B C 1 ATOM 2806 O O . MET B 2 162 ? 7.443 15.846 -11.637 1.00 25.66 ? 160 MET B O 1 ATOM 2807 C CB . MET B 2 162 ? 7.549 17.475 -8.889 1.00 17.88 ? 160 MET B CB 1 ATOM 2808 C CG . MET B 2 162 ? 8.205 17.834 -7.558 1.00 16.39 ? 160 MET B CG 1 ATOM 2809 S SD . MET B 2 162 ? 8.382 19.591 -7.232 1.00 54.40 ? 160 MET B SD 1 ATOM 2810 C CE . MET B 2 162 ? 10.036 19.859 -7.867 1.00 17.68 ? 160 MET B CE 1 ATOM 2811 N N . LEU B 2 163 ? 5.875 15.000 -10.261 1.00 17.11 ? 161 LEU B N 1 ATOM 2812 C CA . LEU B 2 163 ? 4.979 14.598 -11.333 1.00 17.18 ? 161 LEU B CA 1 ATOM 2813 C C . LEU B 2 163 ? 3.674 15.361 -11.185 1.00 21.02 ? 161 LEU B C 1 ATOM 2814 O O . LEU B 2 163 ? 2.978 15.230 -10.178 1.00 19.77 ? 161 LEU B O 1 ATOM 2815 C CB . LEU B 2 163 ? 4.704 13.094 -11.268 1.00 18.55 ? 161 LEU B CB 1 ATOM 2816 C CG . LEU B 2 163 ? 3.679 12.538 -12.258 1.00 20.65 ? 161 LEU B CG 1 ATOM 2817 C CD1 . LEU B 2 163 ? 4.181 12.700 -13.680 1.00 18.55 ? 161 LEU B CD1 1 ATOM 2818 C CD2 . LEU B 2 163 ? 3.373 11.079 -11.952 1.00 19.71 ? 161 LEU B CD2 1 ATOM 2819 N N . GLU B 2 164 ? 3.342 16.163 -12.190 1.00 24.82 ? 162 GLU B N 1 ATOM 2820 C CA . GLU B 2 164 ? 2.057 16.838 -12.208 1.00 30.01 ? 162 GLU B CA 1 ATOM 2821 C C . GLU B 2 164 ? 0.997 15.856 -12.682 1.00 29.87 ? 162 GLU B C 1 ATOM 2822 O O . GLU B 2 164 ? 1.050 15.355 -13.806 1.00 28.61 ? 162 GLU B O 1 ATOM 2823 C CB . GLU B 2 164 ? 2.113 18.041 -13.144 1.00 32.83 ? 162 GLU B CB 1 ATOM 2824 C CG . GLU B 2 164 ? 3.212 19.026 -12.775 1.00 39.55 ? 162 GLU B CG 1 ATOM 2825 C CD . GLU B 2 164 ? 3.508 20.019 -13.878 1.00 43.74 ? 162 GLU B CD 1 ATOM 2826 O OE1 . GLU B 2 164 ? 2.928 19.880 -14.975 1.00 48.77 ? 162 GLU B OE1 1 ATOM 2827 O OE2 . GLU B 2 164 ? 4.328 20.933 -13.652 1.00 42.61 ? 162 GLU B OE2 1 ATOM 2828 N N . THR B 2 165 ? 0.033 15.590 -11.809 1.00 20.22 ? 163 THR B N 1 ATOM 2829 C CA . THR B 2 165 ? -0.988 14.586 -12.060 1.00 21.30 ? 163 THR B CA 1 ATOM 2830 C C . THR B 2 165 ? -2.170 14.807 -11.126 1.00 22.30 ? 163 THR B C 1 ATOM 2831 O O . THR B 2 165 ? -2.020 15.367 -10.044 1.00 22.20 ? 163 THR B O 1 ATOM 2832 C CB . THR B 2 165 ? -0.431 13.161 -11.849 1.00 21.86 ? 163 THR B CB 1 ATOM 2833 O OG1 . THR B 2 165 ? -1.412 12.198 -12.252 1.00 23.61 ? 163 THR B OG1 1 ATOM 2834 C CG2 . THR B 2 165 ? -0.073 12.929 -10.388 1.00 22.71 ? 163 THR B CG2 1 ATOM 2835 N N . VAL B 2 166 ? -3.348 14.369 -11.553 1.00 25.21 ? 164 VAL B N 1 ATOM 2836 C CA . VAL B 2 166 ? -4.519 14.368 -10.691 1.00 26.98 ? 164 VAL B CA 1 ATOM 2837 C C . VAL B 2 166 ? -4.784 12.928 -10.280 1.00 31.21 ? 164 VAL B C 1 ATOM 2838 O O . VAL B 2 166 ? -5.349 12.155 -11.051 1.00 34.14 ? 164 VAL B O 1 ATOM 2839 C CB . VAL B 2 166 ? -5.757 14.944 -11.395 1.00 25.54 ? 164 VAL B CB 1 ATOM 2840 C CG1 . VAL B 2 166 ? -6.937 14.992 -10.434 1.00 26.95 ? 164 VAL B CG1 1 ATOM 2841 C CG2 . VAL B 2 166 ? -5.455 16.330 -11.946 1.00 24.81 ? 164 VAL B CG2 1 ATOM 2842 N N . PRO B 2 167 ? -4.370 12.564 -9.054 1.00 30.01 ? 165 PRO B N 1 ATOM 2843 C CA . PRO B 2 167 ? -4.505 11.182 -8.586 1.00 30.49 ? 165 PRO B CA 1 ATOM 2844 C C . PRO B 2 167 ? -5.954 10.727 -8.546 1.00 31.64 ? 165 PRO B C 1 ATOM 2845 O O . PRO B 2 167 ? -6.824 11.441 -8.045 1.00 29.05 ? 165 PRO B O 1 ATOM 2846 C CB . PRO B 2 167 ? -3.925 11.235 -7.168 1.00 32.90 ? 165 PRO B CB 1 ATOM 2847 C CG . PRO B 2 167 ? -3.008 12.420 -7.180 1.00 32.06 ? 165 PRO B CG 1 ATOM 2848 C CD . PRO B 2 167 ? -3.702 13.418 -8.056 1.00 29.66 ? 165 PRO B CD 1 ATOM 2849 N N . ARG B 2 168 ? -6.200 9.534 -9.077 1.00 29.10 ? 166 ARG B N 1 ATOM 2850 C CA . ARG B 2 168 ? -7.521 8.930 -9.028 1.00 37.21 ? 166 ARG B CA 1 ATOM 2851 C C . ARG B 2 168 ? -7.509 7.732 -8.091 1.00 40.92 ? 166 ARG B C 1 ATOM 2852 O O . ARG B 2 168 ? -6.483 7.066 -7.949 1.00 44.98 ? 166 ARG B O 1 ATOM 2853 C CB . ARG B 2 168 ? -7.951 8.502 -10.432 1.00 37.40 ? 166 ARG B CB 1 ATOM 2854 C CG . ARG B 2 168 ? -8.410 9.641 -11.327 1.00 37.63 ? 166 ARG B CG 1 ATOM 2855 C CD . ARG B 2 168 ? -8.622 9.150 -12.752 1.00 38.34 ? 166 ARG B CD 1 ATOM 2856 N NE . ARG B 2 168 ? -9.396 10.090 -13.558 1.00 38.52 ? 166 ARG B NE 1 ATOM 2857 C CZ . ARG B 2 168 ? -8.874 11.133 -14.195 1.00 35.44 ? 166 ARG B CZ 1 ATOM 2858 N NH1 . ARG B 2 168 ? -7.571 11.370 -14.125 1.00 34.13 ? 166 ARG B NH1 1 ATOM 2859 N NH2 . ARG B 2 168 ? -9.652 11.933 -14.912 1.00 36.20 ? 166 ARG B NH2 1 ATOM 2860 N N . SER B 2 169 ? -8.638 7.476 -7.437 1.00 43.90 ? 167 SER B N 1 ATOM 2861 C CA . SER B 2 169 ? -8.747 6.355 -6.509 1.00 44.24 ? 167 SER B CA 1 ATOM 2862 C C . SER B 2 169 ? -8.353 5.041 -7.182 1.00 43.46 ? 167 SER B C 1 ATOM 2863 O O . SER B 2 169 ? -8.816 4.735 -8.281 1.00 44.21 ? 167 SER B O 1 ATOM 2864 C CB . SER B 2 169 ? -10.171 6.258 -5.959 1.00 47.19 ? 167 SER B CB 1 ATOM 2865 O OG . SER B 2 169 ? -11.115 6.120 -7.006 1.00 50.47 ? 167 SER B OG 1 ATOM 2866 N N . GLY B 2 170 ? -7.500 4.268 -6.521 1.00 44.12 ? 168 GLY B N 1 ATOM 2867 C CA . GLY B 2 170 ? -7.066 2.985 -7.045 1.00 45.51 ? 168 GLY B CA 1 ATOM 2868 C C . GLY B 2 170 ? -5.703 3.032 -7.707 1.00 43.06 ? 168 GLY B C 1 ATOM 2869 O O . GLY B 2 170 ? -4.970 2.042 -7.702 1.00 44.01 ? 168 GLY B O 1 ATOM 2870 N N . GLU B 2 171 ? -5.371 4.180 -8.291 1.00 40.87 ? 169 GLU B N 1 ATOM 2871 C CA . GLU B 2 171 ? -4.098 4.348 -8.984 1.00 40.24 ? 169 GLU B CA 1 ATOM 2872 C C . GLU B 2 171 ? -2.939 4.107 -8.029 1.00 38.47 ? 169 GLU B C 1 ATOM 2873 O O . GLU B 2 171 ? -2.985 4.519 -6.870 1.00 35.24 ? 169 GLU B O 1 ATOM 2874 C CB . GLU B 2 171 ? -3.976 5.741 -9.607 1.00 39.23 ? 169 GLU B CB 1 ATOM 2875 C CG . GLU B 2 171 ? -4.805 5.945 -10.866 1.00 39.09 ? 169 GLU B CG 1 ATOM 2876 C CD . GLU B 2 171 ? -4.654 7.341 -11.442 1.00 40.97 ? 169 GLU B CD 1 ATOM 2877 O OE1 . GLU B 2 171 ? -4.230 8.252 -10.699 1.00 38.46 ? 169 GLU B OE1 1 ATOM 2878 O OE2 . GLU B 2 171 ? -4.956 7.527 -12.639 1.00 43.93 ? 169 GLU B OE2 1 ATOM 2879 N N . VAL B 2 172 ? -1.902 3.438 -8.515 1.00 42.26 ? 170 VAL B N 1 ATOM 2880 C CA . VAL B 2 172 ? -0.676 3.323 -7.744 1.00 42.11 ? 170 VAL B CA 1 ATOM 2881 C C . VAL B 2 172 ? 0.462 3.971 -8.517 1.00 34.71 ? 170 VAL B C 1 ATOM 2882 O O . VAL B 2 172 ? 0.757 3.600 -9.653 1.00 33.12 ? 170 VAL B O 1 ATOM 2883 C CB . VAL B 2 172 ? -0.326 1.851 -7.421 1.00 44.97 ? 170 VAL B CB 1 ATOM 2884 C CG1 . VAL B 2 172 ? -0.576 0.953 -8.626 1.00 46.93 ? 170 VAL B CG1 1 ATOM 2885 C CG2 . VAL B 2 172 ? 1.114 1.734 -6.937 1.00 43.08 ? 170 VAL B CG2 1 ATOM 2886 N N . TYR B 2 173 ? 1.095 4.953 -7.888 1.00 30.88 ? 171 TYR B N 1 ATOM 2887 C CA . TYR B 2 173 ? 2.231 5.628 -8.490 1.00 30.34 ? 171 TYR B CA 1 ATOM 2888 C C . TYR B 2 173 ? 3.513 5.079 -7.891 1.00 30.66 ? 171 TYR B C 1 ATOM 2889 O O . TYR B 2 173 ? 3.554 4.719 -6.715 1.00 32.90 ? 171 TYR B O 1 ATOM 2890 C CB . TYR B 2 173 ? 2.143 7.135 -8.248 1.00 26.36 ? 171 TYR B CB 1 ATOM 2891 C CG . TYR B 2 173 ? 1.012 7.810 -8.994 1.00 27.16 ? 171 TYR B CG 1 ATOM 2892 C CD1 . TYR B 2 173 ? -0.292 7.750 -8.519 1.00 27.26 ? 171 TYR B CD1 1 ATOM 2893 C CD2 . TYR B 2 173 ? 1.250 8.513 -10.169 1.00 23.70 ? 171 TYR B CD2 1 ATOM 2894 C CE1 . TYR B 2 173 ? -1.327 8.365 -9.195 1.00 26.35 ? 171 TYR B CE1 1 ATOM 2895 C CE2 . TYR B 2 173 ? 0.219 9.132 -10.851 1.00 23.16 ? 171 TYR B CE2 1 ATOM 2896 C CZ . TYR B 2 173 ? -1.067 9.054 -10.360 1.00 25.27 ? 171 TYR B CZ 1 ATOM 2897 O OH . TYR B 2 173 ? -2.095 9.670 -11.035 1.00 24.67 ? 171 TYR B OH 1 ATOM 2898 N N . THR B 2 174 ? 4.557 5.016 -8.705 1.00 29.47 ? 172 THR B N 1 ATOM 2899 C CA . THR B 2 174 ? 5.838 4.498 -8.252 1.00 26.82 ? 172 THR B CA 1 ATOM 2900 C C . THR B 2 174 ? 6.973 5.420 -8.658 1.00 25.72 ? 172 THR B C 1 ATOM 2901 O O . THR B 2 174 ? 7.085 5.803 -9.824 1.00 28.12 ? 172 THR B O 1 ATOM 2902 C CB . THR B 2 174 ? 6.110 3.098 -8.834 1.00 26.32 ? 172 THR B CB 1 ATOM 2903 O OG1 . THR B 2 174 ? 5.063 2.202 -8.441 1.00 33.57 ? 172 THR B OG1 1 ATOM 2904 C CG2 . THR B 2 174 ? 7.445 2.563 -8.341 1.00 24.54 ? 172 THR B CG2 1 ATOM 2905 N N . CYS B 2 175 ? 7.815 5.780 -7.698 1.00 25.07 ? 173 CYS B N 1 ATOM 2906 C CA . CYS B 2 175 ? 9.041 6.489 -8.020 1.00 25.48 ? 173 CYS B CA 1 ATOM 2907 C C . CYS B 2 175 ? 10.186 5.488 -8.038 1.00 28.27 ? 173 CYS B C 1 ATOM 2908 O O . CYS B 2 175 ? 10.378 4.738 -7.082 1.00 30.82 ? 173 CYS B O 1 ATOM 2909 C CB . CYS B 2 175 ? 9.328 7.565 -6.981 1.00 21.16 ? 173 CYS B CB 1 ATOM 2910 S SG . CYS B 2 175 ? 10.837 8.486 -7.333 1.00 26.19 ? 173 CYS B SG 1 ATOM 2911 N N . GLN B 2 176 ? 10.950 5.485 -9.125 1.00 26.87 ? 174 GLN B N 1 ATOM 2912 C CA . GLN B 2 176 ? 12.032 4.527 -9.283 1.00 27.10 ? 174 GLN B CA 1 ATOM 2913 C C . GLN B 2 176 ? 13.371 5.244 -9.384 1.00 23.71 ? 174 GLN B C 1 ATOM 2914 O O . GLN B 2 176 ? 13.516 6.203 -10.140 1.00 23.50 ? 174 GLN B O 1 ATOM 2915 C CB . GLN B 2 176 ? 11.804 3.686 -10.539 1.00 26.42 ? 174 GLN B CB 1 ATOM 2916 C CG . GLN B 2 176 ? 12.867 2.636 -10.795 1.00 25.27 ? 174 GLN B CG 1 ATOM 2917 C CD . GLN B 2 176 ? 12.786 2.067 -12.197 1.00 27.74 ? 174 GLN B CD 1 ATOM 2918 O OE1 . GLN B 2 176 ? 13.297 2.658 -13.149 1.00 33.96 ? 174 GLN B OE1 1 ATOM 2919 N NE2 . GLN B 2 176 ? 12.140 0.916 -12.331 1.00 25.07 ? 174 GLN B NE2 1 ATOM 2920 N N . VAL B 2 177 ? 14.346 4.778 -8.610 1.00 23.22 ? 175 VAL B N 1 ATOM 2921 C CA . VAL B 2 177 ? 15.634 5.453 -8.523 1.00 23.44 ? 175 VAL B CA 1 ATOM 2922 C C . VAL B 2 177 ? 16.774 4.502 -8.864 1.00 23.53 ? 175 VAL B C 1 ATOM 2923 O O . VAL B 2 177 ? 16.878 3.413 -8.297 1.00 23.41 ? 175 VAL B O 1 ATOM 2924 C CB . VAL B 2 177 ? 15.856 6.037 -7.114 1.00 25.06 ? 175 VAL B CB 1 ATOM 2925 C CG1 . VAL B 2 177 ? 17.254 6.618 -6.993 1.00 23.43 ? 175 VAL B CG1 1 ATOM 2926 C CG2 . VAL B 2 177 ? 14.802 7.092 -6.804 1.00 24.05 ? 175 VAL B CG2 1 ATOM 2927 N N . GLU B 2 178 ? 17.629 4.914 -9.794 1.00 23.74 ? 176 GLU B N 1 ATOM 2928 C CA . GLU B 2 178 ? 18.820 4.145 -10.123 1.00 22.50 ? 176 GLU B CA 1 ATOM 2929 C C . GLU B 2 178 ? 20.061 4.963 -9.786 1.00 20.89 ? 176 GLU B C 1 ATOM 2930 O O . GLU B 2 178 ? 20.105 6.168 -10.030 1.00 20.86 ? 176 GLU B O 1 ATOM 2931 C CB . GLU B 2 178 ? 18.821 3.769 -11.605 1.00 23.35 ? 176 GLU B CB 1 ATOM 2932 C CG . GLU B 2 178 ? 17.772 2.726 -11.966 1.00 30.07 ? 176 GLU B CG 1 ATOM 2933 C CD . GLU B 2 178 ? 17.471 2.680 -13.450 1.00 35.88 ? 176 GLU B CD 1 ATOM 2934 O OE1 . GLU B 2 178 ? 17.615 1.596 -14.051 1.00 36.80 ? 176 GLU B OE1 1 ATOM 2935 O OE2 . GLU B 2 178 ? 17.088 3.727 -14.014 1.00 36.91 ? 176 GLU B OE2 1 ATOM 2936 N N . HIS B 2 179 ? 21.071 4.298 -9.235 1.00 24.07 ? 177 HIS B N 1 ATOM 2937 C CA . HIS B 2 179 ? 22.230 4.989 -8.688 1.00 22.60 ? 177 HIS B CA 1 ATOM 2938 C C . HIS B 2 179 ? 23.358 3.972 -8.530 1.00 24.13 ? 177 HIS B C 1 ATOM 2939 O O . HIS B 2 179 ? 23.091 2.794 -8.288 1.00 23.12 ? 177 HIS B O 1 ATOM 2940 C CB . HIS B 2 179 ? 21.858 5.603 -7.333 1.00 23.07 ? 177 HIS B CB 1 ATOM 2941 C CG . HIS B 2 179 ? 22.930 6.458 -6.732 1.00 22.01 ? 177 HIS B CG 1 ATOM 2942 N ND1 . HIS B 2 179 ? 23.788 6.001 -5.756 1.00 22.32 ? 177 HIS B ND1 1 ATOM 2943 C CD2 . HIS B 2 179 ? 23.273 7.748 -6.960 1.00 21.07 ? 177 HIS B CD2 1 ATOM 2944 C CE1 . HIS B 2 179 ? 24.620 6.969 -5.414 1.00 21.42 ? 177 HIS B CE1 1 ATOM 2945 N NE2 . HIS B 2 179 ? 24.328 8.040 -6.131 1.00 18.32 ? 177 HIS B NE2 1 ATOM 2946 N N . PRO B 2 180 ? 24.623 4.414 -8.671 1.00 22.88 ? 178 PRO B N 1 ATOM 2947 C CA . PRO B 2 180 ? 25.765 3.495 -8.572 1.00 20.10 ? 178 PRO B CA 1 ATOM 2948 C C . PRO B 2 180 ? 25.840 2.745 -7.243 1.00 25.34 ? 178 PRO B C 1 ATOM 2949 O O . PRO B 2 180 ? 26.443 1.673 -7.178 1.00 22.02 ? 178 PRO B O 1 ATOM 2950 C CB . PRO B 2 180 ? 26.974 4.422 -8.725 1.00 19.40 ? 178 PRO B CB 1 ATOM 2951 C CG . PRO B 2 180 ? 26.464 5.557 -9.538 1.00 18.49 ? 178 PRO B CG 1 ATOM 2952 C CD . PRO B 2 180 ? 25.044 5.762 -9.095 1.00 17.88 ? 178 PRO B CD 1 ATOM 2953 N N . SER B 2 181 ? 25.237 3.303 -6.200 1.00 23.41 ? 179 SER B N 1 ATOM 2954 C CA . SER B 2 181 ? 25.268 2.680 -4.885 1.00 25.11 ? 179 SER B CA 1 ATOM 2955 C C . SER B 2 181 ? 24.273 1.528 -4.811 1.00 25.30 ? 179 SER B C 1 ATOM 2956 O O . SER B 2 181 ? 24.301 0.731 -3.873 1.00 27.05 ? 179 SER B O 1 ATOM 2957 C CB . SER B 2 181 ? 24.930 3.706 -3.810 1.00 19.70 ? 179 SER B CB 1 ATOM 2958 O OG . SER B 2 181 ? 23.578 4.104 -3.943 1.00 19.25 ? 179 SER B OG 1 ATOM 2959 N N . LEU B 2 182 ? 23.389 1.448 -5.801 1.00 26.04 ? 180 LEU B N 1 ATOM 2960 C CA . LEU B 2 182 ? 22.337 0.437 -5.809 1.00 27.92 ? 180 LEU B CA 1 ATOM 2961 C C . LEU B 2 182 ? 22.659 -0.681 -6.798 1.00 28.55 ? 180 LEU B C 1 ATOM 2962 O O . LEU B 2 182 ? 23.287 -0.444 -7.830 1.00 31.44 ? 180 LEU B O 1 ATOM 2963 C CB . LEU B 2 182 ? 20.990 1.071 -6.162 1.00 26.90 ? 180 LEU B CB 1 ATOM 2964 C CG . LEU B 2 182 ? 20.524 2.236 -5.286 1.00 24.84 ? 180 LEU B CG 1 ATOM 2965 C CD1 . LEU B 2 182 ? 19.270 2.873 -5.868 1.00 20.56 ? 180 LEU B CD1 1 ATOM 2966 C CD2 . LEU B 2 182 ? 20.280 1.773 -3.856 1.00 27.65 ? 180 LEU B CD2 1 ATOM 2967 N N . THR B 2 183 ? 22.227 -1.898 -6.479 1.00 29.62 ? 181 THR B N 1 ATOM 2968 C CA . THR B 2 183 ? 22.461 -3.050 -7.346 1.00 30.88 ? 181 THR B CA 1 ATOM 2969 C C . THR B 2 183 ? 21.214 -3.396 -8.155 1.00 31.49 ? 181 THR B C 1 ATOM 2970 O O . THR B 2 183 ? 21.260 -4.205 -9.081 1.00 38.88 ? 181 THR B O 1 ATOM 2971 C CB . THR B 2 183 ? 22.896 -4.280 -6.531 1.00 34.21 ? 181 THR B CB 1 ATOM 2972 O OG1 . THR B 2 183 ? 21.991 -4.475 -5.437 1.00 35.10 ? 181 THR B OG1 1 ATOM 2973 C CG2 . THR B 2 183 ? 24.305 -4.091 -5.991 1.00 32.48 ? 181 THR B CG2 1 ATOM 2974 N N . SER B 2 184 ? 20.102 -2.768 -7.790 1.00 27.57 ? 182 SER B N 1 ATOM 2975 C CA . SER B 2 184 ? 18.845 -2.897 -8.514 1.00 32.29 ? 182 SER B CA 1 ATOM 2976 C C . SER B 2 184 ? 18.031 -1.645 -8.220 1.00 31.40 ? 182 SER B C 1 ATOM 2977 O O . SER B 2 184 ? 18.297 -0.966 -7.228 1.00 29.09 ? 182 SER B O 1 ATOM 2978 C CB . SER B 2 184 ? 18.099 -4.157 -8.069 1.00 35.04 ? 182 SER B CB 1 ATOM 2979 O OG . SER B 2 184 ? 17.648 -4.040 -6.731 1.00 36.91 ? 182 SER B OG 1 ATOM 2980 N N . PRO B 2 185 ? 17.047 -1.321 -9.078 1.00 32.98 ? 183 PRO B N 1 ATOM 2981 C CA . PRO B 2 185 ? 16.304 -0.077 -8.846 1.00 28.43 ? 183 PRO B CA 1 ATOM 2982 C C . PRO B 2 185 ? 15.606 -0.038 -7.489 1.00 29.44 ? 183 PRO B C 1 ATOM 2983 O O . PRO B 2 185 ? 15.060 -1.043 -7.031 1.00 31.65 ? 183 PRO B O 1 ATOM 2984 C CB . PRO B 2 185 ? 15.260 -0.082 -9.968 1.00 25.29 ? 183 PRO B CB 1 ATOM 2985 C CG . PRO B 2 185 ? 15.874 -0.906 -11.047 1.00 25.89 ? 183 PRO B CG 1 ATOM 2986 C CD . PRO B 2 185 ? 16.647 -1.977 -10.336 1.00 27.10 ? 183 PRO B CD 1 ATOM 2987 N N . LEU B 2 186 ? 15.633 1.133 -6.860 1.00 26.28 ? 184 LEU B N 1 ATOM 2988 C CA . LEU B 2 186 ? 14.927 1.368 -5.613 1.00 29.10 ? 184 LEU B CA 1 ATOM 2989 C C . LEU B 2 186 ? 13.569 1.979 -5.937 1.00 31.02 ? 184 LEU B C 1 ATOM 2990 O O . LEU B 2 186 ? 13.493 3.009 -6.605 1.00 24.76 ? 184 LEU B O 1 ATOM 2991 C CB . LEU B 2 186 ? 15.747 2.316 -4.737 1.00 29.50 ? 184 LEU B CB 1 ATOM 2992 C CG . LEU B 2 186 ? 15.239 2.727 -3.354 1.00 31.44 ? 184 LEU B CG 1 ATOM 2993 C CD1 . LEU B 2 186 ? 14.839 1.514 -2.529 1.00 36.88 ? 184 LEU B CD1 1 ATOM 2994 C CD2 . LEU B 2 186 ? 16.301 3.543 -2.635 1.00 29.00 ? 184 LEU B CD2 1 ATOM 2995 N N . THR B 2 187 ? 12.496 1.352 -5.464 1.00 31.10 ? 185 THR B N 1 ATOM 2996 C CA . THR B 2 187 ? 11.158 1.851 -5.762 1.00 29.65 ? 185 THR B CA 1 ATOM 2997 C C . THR B 2 187 ? 10.352 2.189 -4.513 1.00 29.24 ? 185 THR B C 1 ATOM 2998 O O . THR B 2 187 ? 10.419 1.486 -3.504 1.00 25.52 ? 185 THR B O 1 ATOM 2999 C CB . THR B 2 187 ? 10.360 0.846 -6.615 1.00 31.89 ? 185 THR B CB 1 ATOM 3000 O OG1 . THR B 2 187 ? 10.267 -0.405 -5.924 1.00 35.30 ? 185 THR B OG1 1 ATOM 3001 C CG2 . THR B 2 187 ? 11.039 0.630 -7.961 1.00 31.13 ? 185 THR B CG2 1 ATOM 3002 N N . VAL B 2 188 ? 9.588 3.273 -4.595 1.00 27.79 ? 186 VAL B N 1 ATOM 3003 C CA . VAL B 2 188 ? 8.667 3.655 -3.533 1.00 28.62 ? 186 VAL B CA 1 ATOM 3004 C C . VAL B 2 188 ? 7.287 3.916 -4.130 1.00 28.58 ? 186 VAL B C 1 ATOM 3005 O O . VAL B 2 188 ? 7.153 4.697 -5.072 1.00 27.31 ? 186 VAL B O 1 ATOM 3006 C CB . VAL B 2 188 ? 9.152 4.914 -2.786 1.00 31.68 ? 186 VAL B CB 1 ATOM 3007 C CG1 . VAL B 2 188 ? 8.080 5.411 -1.827 1.00 31.17 ? 186 VAL B CG1 1 ATOM 3008 C CG2 . VAL B 2 188 ? 10.445 4.623 -2.038 1.00 22.89 ? 186 VAL B CG2 1 ATOM 3009 N N . GLU B 2 189 ? 6.265 3.265 -3.585 1.00 30.02 ? 187 GLU B N 1 ATOM 3010 C CA . GLU B 2 189 ? 4.907 3.428 -4.093 1.00 29.50 ? 187 GLU B CA 1 ATOM 3011 C C . GLU B 2 189 ? 4.110 4.466 -3.307 1.00 28.72 ? 187 GLU B C 1 ATOM 3012 O O . GLU B 2 189 ? 4.355 4.690 -2.121 1.00 28.26 ? 187 GLU B O 1 ATOM 3013 C CB . GLU B 2 189 ? 4.166 2.090 -4.073 1.00 32.96 ? 187 GLU B CB 1 ATOM 3014 C CG . GLU B 2 189 ? 4.727 1.067 -5.047 1.00 37.60 ? 187 GLU B CG 1 ATOM 3015 C CD . GLU B 2 189 ? 3.966 -0.243 -5.023 1.00 42.85 ? 187 GLU B CD 1 ATOM 3016 O OE1 . GLU B 2 189 ? 4.225 -1.097 -5.896 1.00 45.68 ? 187 GLU B OE1 1 ATOM 3017 O OE2 . GLU B 2 189 ? 3.106 -0.415 -4.134 1.00 46.23 ? 187 GLU B OE2 1 ATOM 3018 N N . TRP B 2 190 ? 3.151 5.095 -3.981 1.00 28.53 ? 188 TRP B N 1 ATOM 3019 C CA . TRP B 2 190 ? 2.199 5.980 -3.322 1.00 28.47 ? 188 TRP B CA 1 ATOM 3020 C C . TRP B 2 190 ? 0.796 5.728 -3.859 1.00 32.98 ? 188 TRP B C 1 ATOM 3021 O O . TRP B 2 190 ? 0.578 5.717 -5.070 1.00 30.69 ? 188 TRP B O 1 ATOM 3022 C CB . TRP B 2 190 ? 2.577 7.439 -3.575 1.00 29.13 ? 188 TRP B CB 1 ATOM 3023 C CG . TRP B 2 190 ? 1.649 8.421 -2.922 1.00 30.71 ? 188 TRP B CG 1 ATOM 3024 C CD1 . TRP B 2 190 ? 1.756 8.936 -1.663 1.00 31.87 ? 188 TRP B CD1 1 ATOM 3025 C CD2 . TRP B 2 190 ? 0.463 8.993 -3.490 1.00 29.15 ? 188 TRP B CD2 1 ATOM 3026 N NE1 . TRP B 2 190 ? 0.717 9.800 -1.415 1.00 30.73 ? 188 TRP B NE1 1 ATOM 3027 C CE2 . TRP B 2 190 ? -0.092 9.852 -2.519 1.00 29.17 ? 188 TRP B CE2 1 ATOM 3028 C CE3 . TRP B 2 190 ? -0.181 8.866 -4.725 1.00 28.15 ? 188 TRP B CE3 1 ATOM 3029 C CZ2 . TRP B 2 190 ? -1.259 10.578 -2.745 1.00 31.58 ? 188 TRP B CZ2 1 ATOM 3030 C CZ3 . TRP B 2 190 ? -1.341 9.588 -4.946 1.00 26.06 ? 188 TRP B CZ3 1 ATOM 3031 C CH2 . TRP B 2 190 ? -1.867 10.433 -3.962 1.00 30.99 ? 188 TRP B CH2 1 ATOM 3032 N N . ARG B 2 191 ? -0.153 5.536 -2.948 1.00 38.13 ? 189 ARG B N 1 ATOM 3033 C CA . ARG B 2 191 ? -1.541 5.286 -3.319 1.00 41.13 ? 189 ARG B CA 1 ATOM 3034 C C . ARG B 2 191 ? -2.434 6.434 -2.859 1.00 39.70 ? 189 ARG B C 1 ATOM 3035 O O . ARG B 2 191 ? -2.258 6.972 -1.765 1.00 38.39 ? 189 ARG B O 1 ATOM 3036 C CB . ARG B 2 191 ? -2.028 3.968 -2.717 1.00 47.86 ? 189 ARG B CB 1 ATOM 3037 C CG . ARG B 2 191 ? -1.647 2.743 -3.532 1.00 53.65 ? 189 ARG B CG 1 ATOM 3038 C CD . ARG B 2 191 ? -2.015 1.458 -2.810 1.00 60.34 ? 189 ARG B CD 1 ATOM 3039 N NE . ARG B 2 191 ? -1.821 0.285 -3.657 1.00 65.60 ? 189 ARG B NE 1 ATOM 3040 C CZ . ARG B 2 191 ? -0.657 -0.338 -3.817 1.00 68.77 ? 189 ARG B CZ 1 ATOM 3041 N NH1 . ARG B 2 191 ? 0.426 0.100 -3.188 1.00 68.26 ? 189 ARG B NH1 1 ATOM 3042 N NH2 . ARG B 2 191 ? -0.576 -1.399 -4.607 1.00 70.18 ? 189 ARG B NH2 1 ATOM 3043 N N . ALA B 2 192 ? -3.386 6.810 -3.706 1.00 37.65 ? 190 ALA B N 1 ATOM 3044 C CA . ALA B 2 192 ? -4.446 7.726 -3.306 1.00 37.15 ? 190 ALA B CA 1 ATOM 3045 C C . ALA B 2 192 ? -5.556 6.964 -2.596 1.00 36.52 ? 190 ALA B C 1 ATOM 3046 O O . ALA B 2 192 ? -5.827 5.806 -2.910 1.00 41.27 ? 190 ALA B O 1 ATOM 3047 C CB . ALA B 2 192 ? -5.004 8.419 -4.533 1.00 37.65 ? 190 ALA B CB 1 ATOM 3048 N N . GLY C 3 1 ? 48.264 7.668 3.542 1.00 30.46 ? 1 GLY C N 1 ATOM 3049 C CA . GLY C 3 1 ? 49.145 8.360 2.621 1.00 26.42 ? 1 GLY C CA 1 ATOM 3050 C C . GLY C 3 1 ? 49.158 9.858 2.847 1.00 27.11 ? 1 GLY C C 1 ATOM 3051 O O . GLY C 3 1 ? 48.325 10.391 3.579 1.00 28.74 ? 1 GLY C O 1 ATOM 3052 N N . VAL C 3 2 ? 50.107 10.541 2.215 1.00 26.32 ? 2 VAL C N 1 ATOM 3053 C CA . VAL C 3 2 ? 50.236 11.985 2.362 1.00 25.75 ? 2 VAL C CA 1 ATOM 3054 C C . VAL C 3 2 ? 49.931 12.700 1.051 1.00 28.36 ? 2 VAL C C 1 ATOM 3055 O O . VAL C 3 2 ? 50.492 12.366 0.008 1.00 30.50 ? 2 VAL C O 1 ATOM 3056 C CB . VAL C 3 2 ? 51.653 12.380 2.821 1.00 25.55 ? 2 VAL C CB 1 ATOM 3057 C CG1 . VAL C 3 2 ? 51.705 13.860 3.164 1.00 24.16 ? 2 VAL C CG1 1 ATOM 3058 C CG2 . VAL C 3 2 ? 52.080 11.538 4.012 1.00 24.11 ? 2 VAL C CG2 1 ATOM 3059 N N . TYR C 3 3 ? 49.036 13.682 1.107 1.00 27.17 ? 3 TYR C N 1 ATOM 3060 C CA . TYR C 3 3 ? 48.735 14.503 -0.059 1.00 23.43 ? 3 TYR C CA 1 ATOM 3061 C C . TYR C 3 3 ? 49.933 15.369 -0.429 1.00 21.26 ? 3 TYR C C 1 ATOM 3062 O O . TYR C 3 3 ? 50.538 16.008 0.433 1.00 25.59 ? 3 TYR C O 1 ATOM 3063 C CB . TYR C 3 3 ? 47.519 15.393 0.204 1.00 22.44 ? 3 TYR C CB 1 ATOM 3064 C CG . TYR C 3 3 ? 46.189 14.758 -0.138 1.00 24.97 ? 3 TYR C CG 1 ATOM 3065 C CD1 . TYR C 3 3 ? 45.761 14.667 -1.457 1.00 26.05 ? 3 TYR C CD1 1 ATOM 3066 C CD2 . TYR C 3 3 ? 45.355 14.266 0.856 1.00 26.24 ? 3 TYR C CD2 1 ATOM 3067 C CE1 . TYR C 3 3 ? 44.545 14.093 -1.776 1.00 26.72 ? 3 TYR C CE1 1 ATOM 3068 C CE2 . TYR C 3 3 ? 44.136 13.691 0.547 1.00 28.18 ? 3 TYR C CE2 1 ATOM 3069 C CZ . TYR C 3 3 ? 43.736 13.608 -0.770 1.00 29.10 ? 3 TYR C CZ 1 ATOM 3070 O OH . TYR C 3 3 ? 42.524 13.037 -1.085 1.00 30.68 ? 3 TYR C OH 1 ATOM 3071 N N . ALA C 3 4 ? 50.276 15.386 -1.714 1.00 17.74 ? 4 ALA C N 1 ATOM 3072 C CA . ALA C 3 4 ? 51.378 16.208 -2.203 1.00 19.36 ? 4 ALA C CA 1 ATOM 3073 C C . ALA C 3 4 ? 50.872 17.556 -2.707 1.00 24.51 ? 4 ALA C C 1 ATOM 3074 O O . ALA C 3 4 ? 49.763 17.653 -3.235 1.00 25.07 ? 4 ALA C O 1 ATOM 3075 C CB . ALA C 3 4 ? 52.144 15.478 -3.299 1.00 17.63 ? 4 ALA C CB 1 ATOM 3076 N N . THR C 3 5 ? 51.688 18.592 -2.544 1.00 26.14 ? 5 THR C N 1 ATOM 3077 C CA . THR C 3 5 ? 51.300 19.944 -2.930 1.00 25.91 ? 5 THR C CA 1 ATOM 3078 C C . THR C 3 5 ? 51.871 20.354 -4.281 1.00 23.73 ? 5 THR C C 1 ATOM 3079 O O . THR C 3 5 ? 53.096 20.333 -4.400 1.00 25.06 ? 5 THR C O 1 ATOM 3080 C CB . THR C 3 5 ? 51.759 20.983 -1.888 1.00 31.20 ? 5 THR C CB 1 ATOM 3081 O OG1 . THR C 3 5 ? 51.074 20.761 -0.652 1.00 36.73 ? 5 THR C OG1 1 ATOM 3082 C CG2 . THR C 3 5 ? 51.461 22.396 -2.369 1.00 31.76 ? 5 THR C CG2 1 HETATM 3083 C C1 . CIR C 3 6 ? 52.346 22.445 -6.196 1.00 20.57 ? 6 CIR C C1 1 HETATM 3084 O O1 . CIR C 3 6 ? 51.643 23.277 -5.573 1.00 24.46 ? 6 CIR C O1 1 HETATM 3085 C C2 . CIR C 3 6 ? 51.768 21.110 -6.477 1.00 17.66 ? 6 CIR C C2 1 HETATM 3086 N N2 . CIR C 3 6 ? 51.054 20.735 -5.287 1.00 20.03 ? 6 CIR C N2 1 HETATM 3087 C C3 . CIR C 3 6 ? 50.827 21.195 -7.637 1.00 12.25 ? 6 CIR C C3 1 HETATM 3088 C C4 . CIR C 3 6 ? 51.549 21.772 -8.837 1.00 29.31 ? 6 CIR C C4 1 HETATM 3089 C C5 . CIR C 3 6 ? 52.200 20.659 -9.625 1.00 28.76 ? 6 CIR C C5 1 HETATM 3090 N N6 . CIR C 3 6 ? 53.280 20.062 -8.855 1.00 30.28 ? 6 CIR C N6 1 HETATM 3091 C C7 . CIR C 3 6 ? 54.564 20.706 -8.783 1.00 35.39 ? 6 CIR C C7 1 HETATM 3092 O O7 . CIR C 3 6 ? 54.758 21.756 -9.372 1.00 35.51 ? 6 CIR C O7 1 HETATM 3093 N N8 . CIR C 3 6 ? 55.627 20.106 -8.016 1.00 39.69 ? 6 CIR C N8 1 ATOM 3094 N N . SER C 3 7 ? 53.509 23.018 -6.427 1.00 20.68 ? 7 SER C N 1 ATOM 3095 C CA . SER C 3 7 ? 53.803 24.379 -5.990 1.00 19.80 ? 7 SER C CA 1 ATOM 3096 C C . SER C 3 7 ? 53.336 25.437 -6.982 1.00 18.19 ? 7 SER C C 1 ATOM 3097 O O . SER C 3 7 ? 53.009 25.134 -8.130 1.00 17.20 ? 7 SER C O 1 ATOM 3098 C CB . SER C 3 7 ? 55.300 24.538 -5.716 1.00 22.50 ? 7 SER C CB 1 ATOM 3099 O OG . SER C 3 7 ? 56.058 24.256 -6.877 1.00 27.65 ? 7 SER C OG 1 ATOM 3100 N N . SER C 3 8 ? 53.298 26.684 -6.523 1.00 17.10 ? 8 SER C N 1 ATOM 3101 C CA . SER C 3 8 ? 52.947 27.808 -7.379 1.00 18.34 ? 8 SER C CA 1 ATOM 3102 C C . SER C 3 8 ? 54.211 28.528 -7.835 1.00 20.12 ? 8 SER C C 1 ATOM 3103 O O . SER C 3 8 ? 55.055 28.894 -7.018 1.00 20.07 ? 8 SER C O 1 ATOM 3104 C CB . SER C 3 8 ? 52.021 28.776 -6.643 1.00 21.84 ? 8 SER C CB 1 ATOM 3105 O OG . SER C 3 8 ? 50.821 28.132 -6.247 1.00 24.75 ? 8 SER C OG 1 ATOM 3106 N N . ALA C 3 9 ? 54.336 28.727 -9.143 1.00 21.01 ? 9 ALA C N 1 ATOM 3107 C CA . ALA C 3 9 ? 55.529 29.343 -9.711 1.00 20.48 ? 9 ALA C CA 1 ATOM 3108 C C . ALA C 3 9 ? 55.616 30.832 -9.390 1.00 25.78 ? 9 ALA C C 1 ATOM 3109 O O . ALA C 3 9 ? 54.622 31.555 -9.467 1.00 28.14 ? 9 ALA C O 1 ATOM 3110 C CB . ALA C 3 9 ? 55.578 29.117 -11.213 1.00 20.34 ? 9 ALA C CB 1 ATOM 3111 N N . VAL C 3 10 ? 56.814 31.278 -9.028 1.00 25.00 ? 10 VAL C N 1 ATOM 3112 C CA . VAL C 3 10 ? 57.057 32.682 -8.730 1.00 27.68 ? 10 VAL C CA 1 ATOM 3113 C C . VAL C 3 10 ? 57.333 33.443 -10.019 1.00 27.26 ? 10 VAL C C 1 ATOM 3114 O O . VAL C 3 10 ? 58.179 33.035 -10.817 1.00 26.63 ? 10 VAL C O 1 ATOM 3115 C CB . VAL C 3 10 ? 58.269 32.851 -7.798 1.00 32.72 ? 10 VAL C CB 1 ATOM 3116 C CG1 . VAL C 3 10 ? 58.289 34.252 -7.205 1.00 37.19 ? 10 VAL C CG1 1 ATOM 3117 C CG2 . VAL C 3 10 ? 58.245 31.801 -6.699 1.00 32.45 ? 10 VAL C CG2 1 ATOM 3118 N N . ARG C 3 11 ? 56.628 34.541 -10.226 1.00 29.33 ? 11 ARG C N 1 ATOM 3119 C CA . ARG C 3 11 ? 56.835 35.374 -11.407 1.00 37.85 ? 11 ARG C CA 1 ATOM 3120 C C . ARG C 3 11 ? 57.989 36.354 -11.224 1.00 38.52 ? 11 ARG C C 1 ATOM 3121 O O . ARG C 3 11 ? 58.440 36.602 -10.107 1.00 33.79 ? 11 ARG C O 1 ATOM 3122 C CB . ARG C 3 11 ? 55.551 36.107 -11.813 1.00 43.17 ? 11 ARG C CB 1 ATOM 3123 C CG . ARG C 3 11 ? 54.853 36.852 -10.695 1.00 51.85 ? 11 ARG C CG 1 ATOM 3124 C CD . ARG C 3 11 ? 53.425 37.249 -11.069 1.00 60.50 ? 11 ARG C CD 1 ATOM 3125 N NE . ARG C 3 11 ? 52.907 36.485 -12.202 1.00 64.97 ? 11 ARG C NE 1 ATOM 3126 C CZ . ARG C 3 11 ? 52.434 35.245 -12.121 1.00 70.07 ? 11 ARG C CZ 1 ATOM 3127 N NH1 . ARG C 3 11 ? 51.988 34.632 -13.204 1.00 72.07 ? 11 ARG C NH1 1 ATOM 3128 N NH2 . ARG C 3 11 ? 52.424 34.607 -10.963 1.00 72.40 ? 11 ARG C NH2 1 ATOM 3129 N N . LEU C 3 12 ? 58.456 36.904 -12.339 1.00 42.38 ? 12 LEU C N 1 ATOM 3130 C CA . LEU C 3 12 ? 59.637 37.760 -12.359 1.00 47.11 ? 12 LEU C CA 1 ATOM 3131 C C . LEU C 3 12 ? 59.343 39.152 -11.798 1.00 53.24 ? 12 LEU C C 1 ATOM 3132 O O . LEU C 3 12 ? 58.194 39.593 -11.791 1.00 51.29 ? 12 LEU C O 1 ATOM 3133 C CB . LEU C 3 12 ? 60.175 37.853 -13.790 1.00 46.58 ? 12 LEU C CB 1 ATOM 3134 C CG . LEU C 3 12 ? 61.490 38.574 -14.082 1.00 46.68 ? 12 LEU C CG 1 ATOM 3135 C CD1 . LEU C 3 12 ? 62.604 38.047 -13.195 1.00 47.43 ? 12 LEU C CD1 1 ATOM 3136 C CD2 . LEU C 3 12 ? 61.848 38.411 -15.550 1.00 42.89 ? 12 LEU C CD2 1 ATOM 3137 N N . ARG C 3 13 ? 60.393 39.824 -11.325 1.00 61.45 ? 13 ARG C N 1 ATOM 3138 C CA . ARG C 3 13 ? 60.300 41.165 -10.743 1.00 69.07 ? 13 ARG C CA 1 ATOM 3139 C C . ARG C 3 13 ? 59.457 41.188 -9.473 1.00 72.57 ? 13 ARG C C 1 ATOM 3140 O O . ARG C 3 13 ? 59.983 41.045 -8.369 1.00 74.79 ? 13 ARG C O 1 ATOM 3141 C CB . ARG C 3 13 ? 59.773 42.180 -11.763 1.00 72.44 ? 13 ARG C CB 1 ATOM 3142 C CG . ARG C 3 13 ? 60.646 42.307 -12.996 1.00 74.77 ? 13 ARG C CG 1 ATOM 3143 C CD . ARG C 3 13 ? 59.913 42.978 -14.141 1.00 79.25 ? 13 ARG C CD 1 ATOM 3144 N NE . ARG C 3 13 ? 60.378 42.471 -15.427 1.00 79.82 ? 13 ARG C NE 1 ATOM 3145 C CZ . ARG C 3 13 ? 59.816 41.455 -16.073 1.00 78.54 ? 13 ARG C CZ 1 ATOM 3146 N NH1 . ARG C 3 13 ? 60.306 41.052 -17.238 1.00 77.53 ? 13 ARG C NH1 1 ATOM 3147 N NH2 . ARG C 3 13 ? 58.758 40.841 -15.557 1.00 77.19 ? 13 ARG C NH2 1 HETATM 3148 C C1 . NAG D 4 . ? 49.207 49.221 -18.810 1.00 44.12 ? 500 NAG A C1 1 HETATM 3149 C C2 . NAG D 4 . ? 48.500 48.603 -20.013 1.00 52.43 ? 500 NAG A C2 1 HETATM 3150 C C3 . NAG D 4 . ? 49.516 48.288 -21.103 1.00 56.83 ? 500 NAG A C3 1 HETATM 3151 C C4 . NAG D 4 . ? 50.306 49.543 -21.448 1.00 56.44 ? 500 NAG A C4 1 HETATM 3152 C C5 . NAG D 4 . ? 50.851 50.235 -20.202 1.00 55.01 ? 500 NAG A C5 1 HETATM 3153 C C6 . NAG D 4 . ? 51.408 51.602 -20.579 1.00 58.09 ? 500 NAG A C6 1 HETATM 3154 C C7 . NAG D 4 . ? 46.442 47.445 -19.492 1.00 54.89 ? 500 NAG A C7 1 HETATM 3155 C C8 . NAG D 4 . ? 45.722 46.135 -19.602 1.00 53.85 ? 500 NAG A C8 1 HETATM 3156 N N2 . NAG D 4 . ? 47.766 47.412 -19.627 1.00 53.82 ? 500 NAG A N2 1 HETATM 3157 O O3 . NAG D 4 . ? 48.853 47.815 -22.254 1.00 60.52 ? 500 NAG A O3 1 HETATM 3158 O O4 . NAG D 4 . ? 51.379 49.206 -22.299 1.00 57.37 ? 500 NAG A O4 1 HETATM 3159 O O5 . NAG D 4 . ? 49.855 50.410 -19.212 1.00 48.99 ? 500 NAG A O5 1 HETATM 3160 O O6 . NAG D 4 . ? 50.427 52.317 -21.298 1.00 59.63 ? 500 NAG A O6 1 HETATM 3161 O O7 . NAG D 4 . ? 45.819 48.485 -19.283 1.00 57.42 ? 500 NAG A O7 1 HETATM 3162 C C1 . NAG E 4 . ? 30.859 42.707 6.680 1.00 34.71 ? 501 NAG A C1 1 HETATM 3163 C C2 . NAG E 4 . ? 31.154 43.558 5.447 1.00 37.60 ? 501 NAG A C2 1 HETATM 3164 C C3 . NAG E 4 . ? 32.239 44.582 5.746 1.00 44.04 ? 501 NAG A C3 1 HETATM 3165 C C4 . NAG E 4 . ? 31.799 45.438 6.922 1.00 48.82 ? 501 NAG A C4 1 HETATM 3166 C C5 . NAG E 4 . ? 31.411 44.573 8.119 1.00 49.73 ? 501 NAG A C5 1 HETATM 3167 C C6 . NAG E 4 . ? 30.755 45.441 9.187 1.00 54.83 ? 501 NAG A C6 1 HETATM 3168 C C7 . NAG E 4 . ? 30.754 42.648 3.249 1.00 31.15 ? 501 NAG A C7 1 HETATM 3169 C C8 . NAG E 4 . ? 31.241 41.790 2.121 1.00 30.23 ? 501 NAG A C8 1 HETATM 3170 N N2 . NAG E 4 . ? 31.536 42.728 4.322 1.00 34.78 ? 501 NAG A N2 1 HETATM 3171 O O3 . NAG E 4 . ? 32.462 45.401 4.620 1.00 43.19 ? 501 NAG A O3 1 HETATM 3172 O O4 . NAG E 4 . ? 32.848 46.309 7.286 1.00 50.79 ? 501 NAG A O4 1 HETATM 3173 O O5 . NAG E 4 . ? 30.510 43.532 7.777 1.00 45.02 ? 501 NAG A O5 1 HETATM 3174 O O6 . NAG E 4 . ? 29.542 44.842 9.586 1.00 58.68 ? 501 NAG A O6 1 HETATM 3175 O O7 . NAG E 4 . ? 29.678 43.236 3.162 1.00 31.04 ? 501 NAG A O7 1 HETATM 3176 C C1 . NAG F 4 . ? 40.985 1.320 -19.388 1.00 52.10 ? 500 NAG B C1 1 HETATM 3177 C C2 . NAG F 4 . ? 41.032 0.867 -20.850 1.00 58.65 ? 500 NAG B C2 1 HETATM 3178 C C3 . NAG F 4 . ? 40.919 -0.652 -20.906 1.00 61.76 ? 500 NAG B C3 1 HETATM 3179 C C4 . NAG F 4 . ? 42.135 -1.202 -20.177 1.00 60.50 ? 500 NAG B C4 1 HETATM 3180 C C5 . NAG F 4 . ? 42.144 -0.698 -18.733 1.00 57.83 ? 500 NAG B C5 1 HETATM 3181 C C6 . NAG F 4 . ? 43.420 -1.150 -18.023 1.00 57.42 ? 500 NAG B C6 1 HETATM 3182 C C7 . NAG F 4 . ? 38.855 1.929 -21.736 1.00 63.36 ? 500 NAG B C7 1 HETATM 3183 C C8 . NAG F 4 . ? 37.881 1.318 -20.767 1.00 63.81 ? 500 NAG B C8 1 HETATM 3184 N N2 . NAG F 4 . ? 40.128 1.513 -21.808 1.00 61.24 ? 500 NAG B N2 1 HETATM 3185 O O3 . NAG F 4 . ? 40.882 -1.091 -22.247 1.00 64.17 ? 500 NAG B O3 1 HETATM 3186 O O4 . NAG F 4 . ? 42.127 -2.610 -20.193 1.00 60.96 ? 500 NAG B O4 1 HETATM 3187 O O5 . NAG F 4 . ? 42.034 0.720 -18.646 1.00 54.15 ? 500 NAG B O5 1 HETATM 3188 O O6 . NAG F 4 . ? 43.372 -0.750 -16.673 1.00 56.34 ? 500 NAG B O6 1 HETATM 3189 O O7 . NAG F 4 . ? 38.452 2.804 -22.502 1.00 63.35 ? 500 NAG B O7 1 HETATM 3190 O O . HOH G 5 . ? 28.161 18.138 -1.474 1.00 18.11 ? 601 HOH A O 1 HETATM 3191 O O . HOH G 5 . ? 35.118 24.278 4.668 1.00 13.00 ? 602 HOH A O 1 HETATM 3192 O O . HOH G 5 . ? 36.989 29.842 -8.413 1.00 17.78 ? 603 HOH A O 1 HETATM 3193 O O . HOH G 5 . ? 13.696 35.427 10.181 1.00 13.85 ? 604 HOH A O 1 HETATM 3194 O O . HOH G 5 . ? 20.077 15.627 1.357 1.00 15.18 ? 605 HOH A O 1 HETATM 3195 O O . HOH G 5 . ? 11.831 26.090 14.050 1.00 13.80 ? 606 HOH A O 1 HETATM 3196 O O . HOH G 5 . ? 47.126 43.881 -5.070 1.00 14.39 ? 607 HOH A O 1 HETATM 3197 O O . HOH G 5 . ? 50.354 32.969 -7.838 1.00 13.64 ? 608 HOH A O 1 HETATM 3198 O O . HOH G 5 . ? 32.709 22.347 1.560 1.00 15.64 ? 609 HOH A O 1 HETATM 3199 O O . HOH G 5 . ? 12.240 17.388 9.611 1.00 16.90 ? 610 HOH A O 1 HETATM 3200 O O . HOH G 5 . ? 37.171 21.168 5.515 1.00 24.62 ? 611 HOH A O 1 HETATM 3201 O O . HOH G 5 . ? 32.044 11.768 -7.673 1.00 12.71 ? 612 HOH A O 1 HETATM 3202 O O . HOH G 5 . ? 36.776 35.591 -9.193 1.00 13.42 ? 613 HOH A O 1 HETATM 3203 O O . HOH G 5 . ? 32.237 15.138 -5.124 1.00 21.85 ? 614 HOH A O 1 HETATM 3204 O O . HOH G 5 . ? 22.077 29.959 -4.914 1.00 13.89 ? 615 HOH A O 1 HETATM 3205 O O . HOH G 5 . ? 19.396 34.870 -5.459 1.00 16.00 ? 616 HOH A O 1 HETATM 3206 O O . HOH G 5 . ? 32.043 41.169 -1.016 1.00 17.76 ? 617 HOH A O 1 HETATM 3207 O O . HOH G 5 . ? 11.067 37.108 7.690 1.00 20.12 ? 618 HOH A O 1 HETATM 3208 O O . HOH G 5 . ? 37.581 25.950 -15.517 1.00 18.63 ? 619 HOH A O 1 HETATM 3209 O O . HOH G 5 . ? 31.789 26.255 10.682 1.00 24.64 ? 620 HOH A O 1 HETATM 3210 O O . HOH G 5 . ? 35.149 22.000 -8.588 1.00 22.43 ? 621 HOH A O 1 HETATM 3211 O O . HOH G 5 . ? 42.286 27.733 3.388 1.00 25.11 ? 622 HOH A O 1 HETATM 3212 O O . HOH G 5 . ? 35.166 23.996 -9.695 1.00 12.95 ? 623 HOH A O 1 HETATM 3213 O O . HOH G 5 . ? 15.724 29.790 -1.760 1.00 19.92 ? 624 HOH A O 1 HETATM 3214 O O . HOH G 5 . ? 52.528 20.016 1.805 1.00 21.19 ? 625 HOH A O 1 HETATM 3215 O O . HOH G 5 . ? 23.650 34.988 -11.299 1.00 27.51 ? 626 HOH A O 1 HETATM 3216 O O . HOH G 5 . ? 46.922 15.921 8.157 1.00 21.69 ? 627 HOH A O 1 HETATM 3217 O O . HOH G 5 . ? 25.912 23.145 11.485 1.00 19.85 ? 628 HOH A O 1 HETATM 3218 O O . HOH G 5 . ? 37.567 19.033 -8.799 1.00 18.51 ? 629 HOH A O 1 HETATM 3219 O O . HOH G 5 . ? 45.865 7.390 2.137 1.00 44.92 ? 630 HOH A O 1 HETATM 3220 O O . HOH G 5 . ? 55.549 42.505 -14.892 1.00 24.73 ? 631 HOH A O 1 HETATM 3221 O O . HOH G 5 . ? 22.451 32.218 -13.146 1.00 27.39 ? 632 HOH A O 1 HETATM 3222 O O . HOH G 5 . ? 26.115 35.873 -10.867 1.00 22.16 ? 633 HOH A O 1 HETATM 3223 O O . HOH G 5 . ? 56.842 30.762 -0.191 1.00 24.40 ? 634 HOH A O 1 HETATM 3224 O O . HOH G 5 . ? 34.070 36.787 4.019 1.00 22.21 ? 635 HOH A O 1 HETATM 3225 O O . HOH G 5 . ? 35.596 45.010 -4.737 1.00 19.98 ? 636 HOH A O 1 HETATM 3226 O O . HOH G 5 . ? 54.819 37.080 0.037 1.00 21.80 ? 637 HOH A O 1 HETATM 3227 O O . HOH G 5 . ? 22.806 28.500 -7.262 1.00 26.91 ? 638 HOH A O 1 HETATM 3228 O O . HOH G 5 . ? 29.838 35.592 7.554 1.00 21.65 ? 639 HOH A O 1 HETATM 3229 O O . HOH G 5 . ? 20.305 41.642 12.520 1.00 34.43 ? 640 HOH A O 1 HETATM 3230 O O . HOH G 5 . ? 51.559 32.519 3.958 1.00 22.54 ? 641 HOH A O 1 HETATM 3231 O O . HOH G 5 . ? 50.177 20.027 9.099 1.00 28.52 ? 642 HOH A O 1 HETATM 3232 O O . HOH G 5 . ? 29.720 46.951 -7.270 1.00 32.00 ? 643 HOH A O 1 HETATM 3233 O O . HOH G 5 . ? 28.381 21.725 9.076 1.00 26.25 ? 644 HOH A O 1 HETATM 3234 O O . HOH G 5 . ? 10.625 26.072 11.965 1.00 23.51 ? 645 HOH A O 1 HETATM 3235 O O . HOH G 5 . ? 36.976 41.508 -12.748 1.00 19.01 ? 646 HOH A O 1 HETATM 3236 O O . HOH G 5 . ? 12.998 34.528 -0.312 1.00 25.34 ? 647 HOH A O 1 HETATM 3237 O O . HOH G 5 . ? 34.041 41.798 5.225 1.00 40.96 ? 648 HOH A O 1 HETATM 3238 O O . HOH G 5 . ? 34.788 26.930 7.709 1.00 27.79 ? 649 HOH A O 1 HETATM 3239 O O . HOH G 5 . ? 12.361 37.967 4.281 1.00 28.68 ? 650 HOH A O 1 HETATM 3240 O O . HOH G 5 . ? 24.037 33.491 11.798 1.00 27.94 ? 651 HOH A O 1 HETATM 3241 O O . HOH G 5 . ? 14.966 25.002 16.254 1.00 36.34 ? 652 HOH A O 1 HETATM 3242 O O . HOH G 5 . ? 28.046 19.745 6.809 1.00 36.17 ? 653 HOH A O 1 HETATM 3243 O O . HOH G 5 . ? 30.710 9.397 5.128 1.00 30.38 ? 654 HOH A O 1 HETATM 3244 O O . HOH G 5 . ? 36.947 4.844 -11.986 1.00 32.94 ? 655 HOH A O 1 HETATM 3245 O O . HOH G 5 . ? 24.404 39.466 6.957 1.00 22.88 ? 656 HOH A O 1 HETATM 3246 O O . HOH G 5 . ? 32.440 46.332 -9.346 1.00 25.13 ? 657 HOH A O 1 HETATM 3247 O O . HOH G 5 . ? 47.945 50.034 -23.620 1.00 41.58 ? 658 HOH A O 1 HETATM 3248 O O . HOH G 5 . ? 33.815 8.749 2.097 1.00 27.61 ? 659 HOH A O 1 HETATM 3249 O O . HOH G 5 . ? 14.532 34.021 17.665 1.00 26.53 ? 660 HOH A O 1 HETATM 3250 O O . HOH G 5 . ? 26.268 40.175 -12.176 1.00 33.08 ? 661 HOH A O 1 HETATM 3251 O O . HOH G 5 . ? 42.512 30.043 6.858 1.00 34.34 ? 662 HOH A O 1 HETATM 3252 O O . HOH G 5 . ? 32.116 20.425 -0.480 1.00 33.74 ? 663 HOH A O 1 HETATM 3253 O O . HOH G 5 . ? 35.187 22.617 7.315 1.00 34.55 ? 664 HOH A O 1 HETATM 3254 O O . HOH G 5 . ? 33.538 47.559 -4.301 1.00 32.26 ? 665 HOH A O 1 HETATM 3255 O O . HOH G 5 . ? 15.146 18.701 1.169 1.00 27.29 ? 666 HOH A O 1 HETATM 3256 O O . HOH G 5 . ? 52.789 49.304 -16.446 1.00 33.80 ? 667 HOH A O 1 HETATM 3257 O O . HOH G 5 . ? 27.195 46.472 -0.396 1.00 41.80 ? 668 HOH A O 1 HETATM 3258 O O . HOH G 5 . ? 17.485 43.846 3.029 1.00 30.84 ? 669 HOH A O 1 HETATM 3259 O O . HOH G 5 . ? 5.148 23.397 0.440 1.00 48.69 ? 670 HOH A O 1 HETATM 3260 O O . HOH G 5 . ? 33.584 39.193 5.791 1.00 38.53 ? 671 HOH A O 1 HETATM 3261 O O . HOH G 5 . ? 44.725 50.254 -17.851 1.00 39.42 ? 672 HOH A O 1 HETATM 3262 O O . HOH G 5 . ? 17.888 34.542 18.505 1.00 46.39 ? 673 HOH A O 1 HETATM 3263 O O . HOH G 5 . ? 32.625 15.059 9.943 1.00 35.38 ? 674 HOH A O 1 HETATM 3264 O O . HOH G 5 . ? 40.010 18.146 10.481 1.00 28.25 ? 675 HOH A O 1 HETATM 3265 O O . HOH G 5 . ? 27.156 47.513 -5.657 1.00 32.98 ? 676 HOH A O 1 HETATM 3266 O O . HOH G 5 . ? 24.952 30.254 20.268 1.00 41.39 ? 677 HOH A O 1 HETATM 3267 O O . HOH G 5 . ? 38.738 31.179 3.162 1.00 22.86 ? 678 HOH A O 1 HETATM 3268 O O . HOH G 5 . ? 17.809 41.466 13.436 1.00 40.04 ? 679 HOH A O 1 HETATM 3269 O O . HOH G 5 . ? 38.114 29.097 -17.927 1.00 29.25 ? 680 HOH A O 1 HETATM 3270 O O . HOH G 5 . ? 36.214 30.986 4.705 1.00 24.66 ? 681 HOH A O 1 HETATM 3271 O O . HOH G 5 . ? 18.380 36.913 19.981 1.00 38.19 ? 682 HOH A O 1 HETATM 3272 O O . HOH G 5 . ? 41.099 30.473 4.323 1.00 42.22 ? 683 HOH A O 1 HETATM 3273 O O . HOH G 5 . ? 45.772 13.181 9.201 1.00 37.17 ? 684 HOH A O 1 HETATM 3274 O O . HOH G 5 . ? 34.616 15.865 -12.274 1.00 34.83 ? 685 HOH A O 1 HETATM 3275 O O . HOH G 5 . ? 6.034 20.910 -0.877 1.00 38.86 ? 686 HOH A O 1 HETATM 3276 O O . HOH G 5 . ? 18.155 16.442 8.545 1.00 32.85 ? 687 HOH A O 1 HETATM 3277 O O . HOH G 5 . ? 34.976 47.903 -10.123 1.00 30.86 ? 688 HOH A O 1 HETATM 3278 O O . HOH G 5 . ? 27.454 35.098 -12.935 1.00 30.93 ? 689 HOH A O 1 HETATM 3279 O O . HOH G 5 . ? 27.362 37.909 10.184 1.00 39.25 ? 690 HOH A O 1 HETATM 3280 O O . HOH G 5 . ? 55.962 26.942 -2.654 1.00 26.72 ? 691 HOH A O 1 HETATM 3281 O O . HOH G 5 . ? 26.533 30.328 9.510 1.00 27.76 ? 692 HOH A O 1 HETATM 3282 O O . HOH G 5 . ? 36.483 43.117 5.568 1.00 35.31 ? 693 HOH A O 1 HETATM 3283 O O . HOH G 5 . ? 29.509 41.687 9.800 1.00 57.10 ? 694 HOH A O 1 HETATM 3284 O O . HOH G 5 . ? 12.518 36.162 22.087 1.00 49.91 ? 695 HOH A O 1 HETATM 3285 O O . HOH G 5 . ? 36.776 36.861 3.651 1.00 38.96 ? 696 HOH A O 1 HETATM 3286 O O . HOH G 5 . ? 28.974 29.708 10.727 1.00 28.89 ? 697 HOH A O 1 HETATM 3287 O O . HOH G 5 . ? 16.067 40.638 -0.120 1.00 27.22 ? 698 HOH A O 1 HETATM 3288 O O . HOH G 5 . ? 31.497 34.069 6.205 1.00 45.71 ? 699 HOH A O 1 HETATM 3289 O O . HOH G 5 . ? 26.489 23.153 -6.552 1.00 43.06 ? 700 HOH A O 1 HETATM 3290 O O . HOH G 5 . ? 32.894 23.919 -5.273 1.00 20.86 ? 701 HOH A O 1 HETATM 3291 O O . HOH G 5 . ? 13.465 14.011 6.935 1.00 38.65 ? 702 HOH A O 1 HETATM 3292 O O . HOH G 5 . ? 5.587 30.350 2.681 1.00 44.45 ? 703 HOH A O 1 HETATM 3293 O O . HOH G 5 . ? 51.476 50.439 -24.470 1.00 39.59 ? 704 HOH A O 1 HETATM 3294 O O . HOH G 5 . ? 26.526 41.091 9.762 1.00 32.62 ? 705 HOH A O 1 HETATM 3295 O O . HOH G 5 . ? 28.964 42.075 -12.259 1.00 35.52 ? 706 HOH A O 1 HETATM 3296 O O . HOH G 5 . ? 26.011 32.557 10.028 1.00 44.74 ? 707 HOH A O 1 HETATM 3297 O O . HOH G 5 . ? 39.437 4.428 11.367 1.00 42.14 ? 708 HOH A O 1 HETATM 3298 O O . HOH G 5 . ? 10.418 38.874 15.689 1.00 45.53 ? 709 HOH A O 1 HETATM 3299 O O . HOH G 5 . ? 25.791 45.434 8.048 1.00 40.85 ? 710 HOH A O 1 HETATM 3300 O O . HOH G 5 . ? 33.581 6.179 1.467 1.00 31.37 ? 711 HOH A O 1 HETATM 3301 O O . HOH G 5 . ? 54.154 36.415 2.907 1.00 29.77 ? 712 HOH A O 1 HETATM 3302 O O . HOH G 5 . ? 5.905 15.523 12.727 1.00 37.19 ? 713 HOH A O 1 HETATM 3303 O O . HOH G 5 . ? 26.515 25.671 -8.408 1.00 34.39 ? 714 HOH A O 1 HETATM 3304 O O . HOH G 5 . ? 45.299 39.238 7.440 1.00 41.59 ? 715 HOH A O 1 HETATM 3305 O O . HOH G 5 . ? 55.196 39.619 -0.989 1.00 34.17 ? 716 HOH A O 1 HETATM 3306 O O . HOH G 5 . ? 54.997 44.106 -12.422 1.00 37.99 ? 717 HOH A O 1 HETATM 3307 O O . HOH G 5 . ? 44.086 39.340 10.113 1.00 40.92 ? 718 HOH A O 1 HETATM 3308 O O . HOH G 5 . ? 28.591 26.811 15.900 1.00 45.97 ? 719 HOH A O 1 HETATM 3309 O O . HOH G 5 . ? 47.163 38.834 10.447 1.00 42.45 ? 720 HOH A O 1 HETATM 3310 O O . HOH G 5 . ? 12.775 14.407 9.561 1.00 36.43 ? 721 HOH A O 1 HETATM 3311 O O . HOH G 5 . ? 24.530 35.967 -13.978 1.00 39.53 ? 722 HOH A O 1 HETATM 3312 O O . HOH G 5 . ? 34.808 33.054 5.598 1.00 42.49 ? 723 HOH A O 1 HETATM 3313 O O . HOH G 5 . ? 19.731 42.514 -2.340 1.00 28.40 ? 724 HOH A O 1 HETATM 3314 O O . HOH G 5 . ? 24.179 41.697 -11.283 1.00 44.65 ? 725 HOH A O 1 HETATM 3315 O O . HOH G 5 . ? 22.233 42.921 -9.407 1.00 50.45 ? 726 HOH A O 1 HETATM 3316 O O . HOH H 5 . ? 48.752 15.007 -21.120 1.00 17.78 ? 601 HOH B O 1 HETATM 3317 O O . HOH H 5 . ? 53.935 17.582 -20.045 1.00 8.91 ? 602 HOH B O 1 HETATM 3318 O O . HOH H 5 . ? 45.017 18.616 -7.810 1.00 9.89 ? 603 HOH B O 1 HETATM 3319 O O . HOH H 5 . ? 50.161 24.912 -21.890 1.00 16.16 ? 604 HOH B O 1 HETATM 3320 O O . HOH H 5 . ? 51.934 14.920 -24.790 1.00 27.42 ? 605 HOH B O 1 HETATM 3321 O O . HOH H 5 . ? 52.609 31.534 -25.035 1.00 17.05 ? 606 HOH B O 1 HETATM 3322 O O . HOH H 5 . ? 46.284 16.215 -7.058 1.00 11.14 ? 607 HOH B O 1 HETATM 3323 O O . HOH H 5 . ? 52.278 16.666 -15.787 1.00 15.21 ? 608 HOH B O 1 HETATM 3324 O O . HOH H 5 . ? 39.595 32.866 -17.954 1.00 14.78 ? 609 HOH B O 1 HETATM 3325 O O . HOH H 5 . ? 37.543 25.370 -10.707 1.00 11.62 ? 610 HOH B O 1 HETATM 3326 O O . HOH H 5 . ? 40.901 29.628 -6.271 1.00 12.49 ? 611 HOH B O 1 HETATM 3327 O O . HOH H 5 . ? 45.937 24.170 -23.028 1.00 14.91 ? 612 HOH B O 1 HETATM 3328 O O . HOH H 5 . ? 16.814 11.910 -13.080 1.00 25.92 ? 613 HOH B O 1 HETATM 3329 O O . HOH H 5 . ? 20.320 1.260 -9.604 1.00 30.11 ? 614 HOH B O 1 HETATM 3330 O O . HOH H 5 . ? 37.080 46.108 -6.556 1.00 16.17 ? 615 HOH B O 1 HETATM 3331 O O . HOH H 5 . ? 17.267 15.355 -11.350 1.00 30.73 ? 616 HOH B O 1 HETATM 3332 O O . HOH H 5 . ? 7.606 15.645 -18.631 1.00 26.45 ? 617 HOH B O 1 HETATM 3333 O O . HOH H 5 . ? 38.386 24.087 -13.057 1.00 16.90 ? 618 HOH B O 1 HETATM 3334 O O . HOH H 5 . ? 23.525 1.154 -10.124 1.00 29.30 ? 619 HOH B O 1 HETATM 3335 O O . HOH H 5 . ? 38.592 39.041 -14.568 1.00 22.97 ? 620 HOH B O 1 HETATM 3336 O O . HOH H 5 . ? 13.797 11.494 1.087 1.00 23.56 ? 621 HOH B O 1 HETATM 3337 O O . HOH H 5 . ? 14.887 5.252 -12.809 1.00 25.83 ? 622 HOH B O 1 HETATM 3338 O O . HOH H 5 . ? 52.988 14.510 -22.762 1.00 32.30 ? 623 HOH B O 1 HETATM 3339 O O . HOH H 5 . ? 51.641 13.599 -19.753 1.00 26.03 ? 624 HOH B O 1 HETATM 3340 O O . HOH H 5 . ? 48.286 25.471 -23.575 1.00 9.97 ? 625 HOH B O 1 HETATM 3341 O O . HOH H 5 . ? 61.130 22.934 -23.504 1.00 22.54 ? 626 HOH B O 1 HETATM 3342 O O . HOH H 5 . ? 41.522 40.283 -14.900 1.00 30.81 ? 627 HOH B O 1 HETATM 3343 O O . HOH H 5 . ? -5.032 10.146 -13.047 1.00 29.83 ? 628 HOH B O 1 HETATM 3344 O O . HOH H 5 . ? 48.328 9.746 -19.213 1.00 27.53 ? 629 HOH B O 1 HETATM 3345 O O . HOH H 5 . ? 41.194 34.400 -19.863 1.00 24.60 ? 630 HOH B O 1 HETATM 3346 O O . HOH H 5 . ? 53.238 15.535 -18.308 1.00 31.79 ? 631 HOH B O 1 HETATM 3347 O O . HOH H 5 . ? 45.732 40.770 -21.375 1.00 37.60 ? 632 HOH B O 1 HETATM 3348 O O . HOH H 5 . ? 17.795 1.534 4.472 1.00 21.64 ? 633 HOH B O 1 HETATM 3349 O O . HOH H 5 . ? 61.277 31.237 -22.719 1.00 28.37 ? 634 HOH B O 1 HETATM 3350 O O . HOH H 5 . ? 7.391 7.833 1.064 1.00 20.42 ? 635 HOH B O 1 HETATM 3351 O O . HOH H 5 . ? 23.192 23.638 -3.718 1.00 16.64 ? 636 HOH B O 1 HETATM 3352 O O . HOH H 5 . ? 28.078 14.213 5.286 1.00 28.33 ? 637 HOH B O 1 HETATM 3353 O O . HOH H 5 . ? 22.750 13.055 -11.955 1.00 31.82 ? 638 HOH B O 1 HETATM 3354 O O . HOH H 5 . ? 25.053 14.729 5.385 1.00 37.53 ? 639 HOH B O 1 HETATM 3355 O O . HOH H 5 . ? 39.892 3.821 -9.601 1.00 45.99 ? 640 HOH B O 1 HETATM 3356 O O . HOH H 5 . ? 64.744 19.166 -20.042 1.00 27.17 ? 641 HOH B O 1 HETATM 3357 O O . HOH H 5 . ? 29.751 13.599 -7.982 1.00 29.12 ? 642 HOH B O 1 HETATM 3358 O O . HOH H 5 . ? 31.496 4.632 0.698 1.00 29.27 ? 643 HOH B O 1 HETATM 3359 O O . HOH H 5 . ? 45.136 4.070 -7.963 1.00 34.63 ? 644 HOH B O 1 HETATM 3360 O O . HOH H 5 . ? 48.906 4.876 -17.736 1.00 35.35 ? 645 HOH B O 1 HETATM 3361 O O . HOH H 5 . ? 1.865 14.185 -16.023 1.00 31.18 ? 646 HOH B O 1 HETATM 3362 O O . HOH H 5 . ? 46.586 21.470 -25.242 1.00 26.02 ? 647 HOH B O 1 HETATM 3363 O O . HOH H 5 . ? 21.316 19.173 -12.210 1.00 21.95 ? 648 HOH B O 1 HETATM 3364 O O . HOH H 5 . ? 14.085 4.874 1.022 1.00 31.31 ? 649 HOH B O 1 HETATM 3365 O O . HOH H 5 . ? 36.268 48.619 -7.664 1.00 25.68 ? 650 HOH B O 1 HETATM 3366 O O . HOH H 5 . ? 41.401 10.420 -5.268 1.00 47.62 ? 651 HOH B O 1 HETATM 3367 O O . HOH H 5 . ? 42.683 48.603 -2.532 1.00 25.00 ? 652 HOH B O 1 HETATM 3368 O O . HOH H 5 . ? 51.002 25.708 -27.823 1.00 31.23 ? 653 HOH B O 1 HETATM 3369 O O . HOH H 5 . ? 9.405 9.319 -15.539 1.00 30.73 ? 654 HOH B O 1 HETATM 3370 O O . HOH H 5 . ? 23.333 10.479 3.392 1.00 34.02 ? 655 HOH B O 1 HETATM 3371 O O . HOH H 5 . ? 47.005 29.749 -25.234 1.00 39.80 ? 656 HOH B O 1 HETATM 3372 O O . HOH H 5 . ? 9.544 5.794 1.754 1.00 33.99 ? 657 HOH B O 1 HETATM 3373 O O . HOH H 5 . ? 23.642 22.791 -5.912 1.00 22.66 ? 658 HOH B O 1 HETATM 3374 O O . HOH H 5 . ? 3.472 22.665 -2.941 1.00 41.93 ? 659 HOH B O 1 HETATM 3375 O O . HOH H 5 . ? 3.108 2.162 -10.776 1.00 27.90 ? 660 HOH B O 1 HETATM 3376 O O . HOH H 5 . ? 42.369 -4.896 -18.539 1.00 40.71 ? 661 HOH B O 1 HETATM 3377 O O . HOH H 5 . ? 52.495 11.709 -22.708 1.00 32.67 ? 662 HOH B O 1 HETATM 3378 O O . HOH H 5 . ? 16.913 4.008 1.169 1.00 24.87 ? 663 HOH B O 1 HETATM 3379 O O . HOH H 5 . ? 67.110 30.267 -19.320 0.50 38.52 ? 664 HOH B O 1 HETATM 3380 O O . HOH H 5 . ? 50.630 31.305 -26.281 1.00 30.26 ? 665 HOH B O 1 HETATM 3381 O O . HOH H 5 . ? 23.180 3.933 -11.823 1.00 37.35 ? 666 HOH B O 1 HETATM 3382 O O . HOH H 5 . ? 43.413 2.833 -12.576 1.00 39.03 ? 667 HOH B O 1 HETATM 3383 O O . HOH H 5 . ? 56.179 16.238 -21.253 1.00 30.83 ? 668 HOH B O 1 HETATM 3384 O O . HOH H 5 . ? 47.238 22.620 -27.495 1.00 28.77 ? 669 HOH B O 1 HETATM 3385 O O . HOH H 5 . ? 38.398 5.095 3.394 1.00 38.85 ? 670 HOH B O 1 HETATM 3386 O O . HOH H 5 . ? 13.177 17.573 0.610 1.00 32.86 ? 671 HOH B O 1 HETATM 3387 O O . HOH H 5 . ? 0.754 -2.466 -6.245 1.00 39.71 ? 672 HOH B O 1 HETATM 3388 O O . HOH H 5 . ? 37.650 21.483 -14.000 1.00 29.65 ? 673 HOH B O 1 HETATM 3389 O O . HOH H 5 . ? 48.165 25.292 -26.548 1.00 20.29 ? 674 HOH B O 1 HETATM 3390 O O . HOH H 5 . ? 25.205 4.367 2.352 1.00 26.14 ? 675 HOH B O 1 HETATM 3391 O O . HOH H 5 . ? 39.492 22.640 -16.724 1.00 36.38 ? 676 HOH B O 1 HETATM 3392 O O . HOH H 5 . ? 55.182 12.221 -4.723 1.00 35.99 ? 677 HOH B O 1 HETATM 3393 O O . HOH H 5 . ? 27.341 5.030 3.482 1.00 35.29 ? 678 HOH B O 1 HETATM 3394 O O . HOH H 5 . ? -2.274 6.818 -19.547 1.00 40.09 ? 679 HOH B O 1 HETATM 3395 O O . HOH H 5 . ? -11.098 9.158 -7.885 1.00 28.22 ? 680 HOH B O 1 HETATM 3396 O O . HOH H 5 . ? 18.773 13.745 -13.281 1.00 35.14 ? 681 HOH B O 1 HETATM 3397 O O . HOH H 5 . ? 54.484 10.681 -17.695 1.00 39.92 ? 682 HOH B O 1 HETATM 3398 O O . HOH H 5 . ? 54.807 30.438 -24.806 1.00 41.73 ? 683 HOH B O 1 HETATM 3399 O O . HOH H 5 . ? 57.950 22.463 -7.974 1.00 48.96 ? 684 HOH B O 1 HETATM 3400 O O . HOH H 5 . ? 9.285 3.345 0.799 1.00 46.61 ? 685 HOH B O 1 HETATM 3401 O O . HOH H 5 . ? 30.494 50.299 3.379 1.00 41.42 ? 686 HOH B O 1 HETATM 3402 O O . HOH H 5 . ? 13.143 -0.928 -3.848 1.00 37.21 ? 687 HOH B O 1 HETATM 3403 O O . HOH H 5 . ? 30.209 5.539 3.206 1.00 47.74 ? 688 HOH B O 1 HETATM 3404 O O . HOH H 5 . ? 0.897 5.560 -0.108 1.00 36.10 ? 689 HOH B O 1 HETATM 3405 O O . HOH H 5 . ? 48.033 5.826 -8.295 1.00 33.21 ? 690 HOH B O 1 HETATM 3406 O O . HOH H 5 . ? 26.531 7.211 5.519 1.00 32.14 ? 691 HOH B O 1 HETATM 3407 O O . HOH H 5 . ? 44.500 24.489 -24.842 1.00 35.28 ? 692 HOH B O 1 HETATM 3408 O O . HOH H 5 . ? 8.011 -0.646 -3.539 1.00 37.31 ? 693 HOH B O 1 HETATM 3409 O O . HOH H 5 . ? 22.585 6.356 -12.884 1.00 31.31 ? 694 HOH B O 1 HETATM 3410 O O . HOH H 5 . ? 0.594 16.319 -17.502 1.00 28.68 ? 695 HOH B O 1 HETATM 3411 O O . HOH H 5 . ? 41.338 23.043 -20.506 1.00 50.79 ? 696 HOH B O 1 HETATM 3412 O O . HOH H 5 . ? 35.594 5.048 3.340 1.00 36.85 ? 697 HOH B O 1 HETATM 3413 O O . HOH H 5 . ? 28.851 51.565 1.243 1.00 46.21 ? 698 HOH B O 1 HETATM 3414 O O . HOH H 5 . ? 44.550 3.330 -3.630 1.00 34.36 ? 699 HOH B O 1 HETATM 3415 O O . HOH H 5 . ? 28.980 15.234 7.668 1.00 37.12 ? 700 HOH B O 1 HETATM 3416 O O . HOH H 5 . ? 28.220 0.190 -4.197 1.00 39.37 ? 701 HOH B O 1 HETATM 3417 O O . HOH H 5 . ? 39.613 26.381 -20.916 1.00 40.14 ? 702 HOH B O 1 HETATM 3418 O O . HOH I 5 . ? 57.378 36.392 -14.481 1.00 23.52 ? 101 HOH C O 1 HETATM 3419 O O . HOH I 5 . ? 52.343 9.294 0.746 1.00 31.99 ? 102 HOH C O 1 HETATM 3420 O O . HOH I 5 . ? 42.386 12.125 -3.657 1.00 31.70 ? 103 HOH C O 1 HETATM 3421 O O . HOH I 5 . ? 60.056 31.216 -11.109 1.00 20.91 ? 104 HOH C O 1 HETATM 3422 O O . HOH I 5 . ? 51.765 17.371 2.309 1.00 28.32 ? 105 HOH C O 1 HETATM 3423 O O . HOH I 5 . ? 54.136 18.008 -0.869 1.00 41.25 ? 106 HOH C O 1 HETATM 3424 O O . HOH I 5 . ? 59.219 29.157 -9.399 1.00 26.92 ? 107 HOH C O 1 HETATM 3425 O O . HOH I 5 . ? 54.626 10.435 0.420 1.00 36.30 ? 108 HOH C O 1 HETATM 3426 O O . HOH I 5 . ? 56.392 17.778 3.061 1.00 38.23 ? 109 HOH C O 1 HETATM 3427 O O . HOH I 5 . ? 54.412 16.196 1.816 1.00 37.64 ? 110 HOH C O 1 HETATM 3428 O O . HOH I 5 . ? 58.068 37.856 -16.202 1.00 43.21 ? 111 HOH C O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . GLU A 3 ? 0.8437 0.7617 0.7830 -0.0966 -0.0094 -0.1402 3 GLU A N 2 C CA . GLU A 3 ? 0.8233 0.7362 0.7838 -0.0908 0.0070 -0.1331 3 GLU A CA 3 C C . GLU A 3 ? 0.7578 0.6788 0.7506 -0.0958 0.0060 -0.1286 3 GLU A C 4 O O . GLU A 3 ? 0.7696 0.7071 0.7718 -0.1017 -0.0081 -0.1271 3 GLU A O 5 C CB . GLU A 3 ? 0.8201 0.7434 0.7783 -0.0810 0.0093 -0.1230 3 GLU A CB 6 C CG . GLU A 3 ? 0.7976 0.7461 0.7680 -0.0810 -0.0035 -0.1147 3 GLU A CG 7 C CD . GLU A 3 ? 0.7882 0.7479 0.7414 -0.0739 -0.0086 -0.1095 3 GLU A CD 8 O OE1 . GLU A 3 ? 0.7750 0.7554 0.7315 -0.0746 -0.0217 -0.1044 3 GLU A OE1 9 O OE2 . GLU A 3 ? 0.7873 0.7355 0.7266 -0.0669 0.0014 -0.1093 3 GLU A OE2 10 N N . GLU A 4 ? 0.6812 0.5914 0.6932 -0.0927 0.0217 -0.1245 4 GLU A N 11 C CA . GLU A 4 ? 0.5917 0.5084 0.6350 -0.0958 0.0235 -0.1181 4 GLU A CA 12 C C . GLU A 4 ? 0.4817 0.4143 0.5406 -0.0895 0.0236 -0.1047 4 GLU A C 13 O O . GLU A 4 ? 0.4795 0.4277 0.5560 -0.0925 0.0171 -0.0990 4 GLU A O 14 C CB . GLU A 4 ? 0.6200 0.5182 0.6790 -0.0947 0.0405 -0.1176 4 GLU A CB 15 C CG . GLU A 4 ? 0.6857 0.5664 0.7369 -0.1020 0.0434 -0.1308 4 GLU A CG 16 C CD . GLU A 4 ? 0.6952 0.5620 0.7695 -0.0998 0.0611 -0.1270 4 GLU A CD 17 O OE1 . GLU A 4 ? 0.6549 0.5255 0.7472 -0.0913 0.0703 -0.1133 4 GLU A OE1 18 O OE2 . GLU A 4 ? 0.7381 0.5890 0.8103 -0.1057 0.0666 -0.1375 4 GLU A OE2 19 N N . HIS A 5 ? 0.3485 0.2766 0.4010 -0.0807 0.0312 -0.0994 5 HIS A N 20 C CA . HIS A 5 ? 0.2779 0.2185 0.3425 -0.0740 0.0314 -0.0859 5 HIS A CA 21 C C . HIS A 5 ? 0.2736 0.2181 0.3198 -0.0640 0.0297 -0.0806 5 HIS A C 22 O O . HIS A 5 ? 0.2939 0.2248 0.3254 -0.0623 0.0353 -0.0870 5 HIS A O 23 C CB . HIS A 5 ? 0.2448 0.1770 0.3320 -0.0696 0.0443 -0.0746 5 HIS A CB 24 C CG . HIS A 5 ? 0.2958 0.2250 0.4033 -0.0766 0.0478 -0.0758 5 HIS A CG 25 N ND1 . HIS A 5 ? 0.2560 0.2002 0.3775 -0.0810 0.0413 -0.0720 5 HIS A ND1 26 C CD2 . HIS A 5 ? 0.3561 0.2705 0.4724 -0.0781 0.0576 -0.0787 5 HIS A CD2 27 C CE1 . HIS A 5 ? 0.2697 0.2078 0.4076 -0.0851 0.0464 -0.0726 5 HIS A CE1 28 N NE2 . HIS A 5 ? 0.3510 0.2710 0.4857 -0.0837 0.0561 -0.0772 5 HIS A NE2 29 N N . VAL A 6 ? 0.2194 0.1812 0.2673 -0.0574 0.0233 -0.0690 6 VAL A N 30 C CA . VAL A 6 ? 0.2298 0.1959 0.2650 -0.0483 0.0217 -0.0628 6 VAL A CA 31 C C . VAL A 6 ? 0.2127 0.1858 0.2582 -0.0408 0.0229 -0.0480 6 VAL A C 32 O O . VAL A 6 ? 0.2312 0.2143 0.2847 -0.0415 0.0201 -0.0424 6 VAL A O 33 C CB . VAL A 6 ? 0.1705 0.1509 0.1906 -0.0485 0.0103 -0.0658 6 VAL A CB 34 C CG1 . VAL A 6 ? 0.1596 0.1430 0.1697 -0.0392 0.0100 -0.0593 6 VAL A CG1 35 C CG2 . VAL A 6 ? 0.1928 0.1673 0.1977 -0.0566 0.0064 -0.0799 6 VAL A CG2 36 N N . ILE A 7 ? 0.2013 0.1689 0.2465 -0.0338 0.0272 -0.0415 7 ILE A N 37 C CA . ILE A 7 ? 0.2026 0.1771 0.2529 -0.0275 0.0253 -0.0283 7 ILE A CA 38 C C . ILE A 7 ? 0.2085 0.1890 0.2478 -0.0222 0.0197 -0.0266 7 ILE A C 39 O O . ILE A 7 ? 0.1986 0.1725 0.2352 -0.0199 0.0230 -0.0292 7 ILE A O 40 C CB . ILE A 7 ? 0.2033 0.1682 0.2685 -0.0243 0.0333 -0.0191 7 ILE A CB 41 C CG1 . ILE A 7 ? 0.1561 0.1133 0.2353 -0.0293 0.0409 -0.0198 7 ILE A CG1 42 C CG2 . ILE A 7 ? 0.1494 0.1225 0.2156 -0.0186 0.0280 -0.0053 7 ILE A CG2 43 C CD1 . ILE A 7 ? 0.1626 0.1099 0.2597 -0.0256 0.0504 -0.0092 7 ILE A CD1 44 N N . ILE A 8 ? 0.2237 0.2152 0.2574 -0.0202 0.0129 -0.0223 8 ILE A N 45 C CA . ILE A 8 ? 0.2089 0.2053 0.2342 -0.0159 0.0080 -0.0213 8 ILE A CA 46 C C . ILE A 8 ? 0.2050 0.2047 0.2306 -0.0124 0.0041 -0.0122 8 ILE A C 47 O O . ILE A 8 ? 0.2200 0.2231 0.2428 -0.0130 0.0028 -0.0086 8 ILE A O 48 C CB . ILE A 8 ? 0.1884 0.1943 0.2046 -0.0169 0.0032 -0.0266 8 ILE A CB 49 C CG1 . ILE A 8 ? 0.1845 0.1885 0.1969 -0.0216 0.0038 -0.0357 8 ILE A CG1 50 C CG2 . ILE A 8 ? 0.1404 0.1499 0.1505 -0.0121 -0.0001 -0.0248 8 ILE A CG2 51 C CD1 . ILE A 8 ? 0.1183 0.1342 0.1250 -0.0229 -0.0026 -0.0384 8 ILE A CD1 52 N N . GLN A 9 ? 0.1656 0.1636 0.1942 -0.0090 0.0022 -0.0084 9 GLN A N 53 C CA . GLN A 9 ? 0.1644 0.1661 0.1904 -0.0071 -0.0047 -0.0019 9 GLN A CA 54 C C . GLN A 9 ? 0.1665 0.1724 0.1836 -0.0059 -0.0083 -0.0068 9 GLN A C 55 O O . GLN A 9 ? 0.1291 0.1343 0.1503 -0.0040 -0.0074 -0.0085 9 GLN A O 56 C CB . GLN A 9 ? 0.2044 0.2035 0.2445 -0.0049 -0.0059 0.0060 9 GLN A CB 57 C CG . GLN A 9 ? 0.1929 0.1963 0.2314 -0.0044 -0.0161 0.0119 9 GLN A CG 58 C CD . GLN A 9 ? 0.2094 0.2130 0.2683 -0.0025 -0.0183 0.0209 9 GLN A CD 59 O OE1 . GLN A 9 ? 0.2296 0.2297 0.3035 -0.0010 -0.0119 0.0267 9 GLN A OE1 60 N NE2 . GLN A 9 ? 0.1096 0.1169 0.1722 -0.0026 -0.0266 0.0226 9 GLN A NE2 61 N N . ALA A 10 ? 0.1683 0.1777 0.1746 -0.0066 -0.0104 -0.0084 10 ALA A N 62 C CA . ALA A 10 ? 0.1500 0.1626 0.1503 -0.0051 -0.0115 -0.0127 10 ALA A CA 63 C C . ALA A 10 ? 0.1541 0.1646 0.1470 -0.0049 -0.0167 -0.0114 10 ALA A C 64 O O . ALA A 10 ? 0.1798 0.1880 0.1633 -0.0063 -0.0185 -0.0088 10 ALA A O 65 C CB . ALA A 10 ? 0.1647 0.1822 0.1612 -0.0058 -0.0081 -0.0159 10 ALA A CB 66 N N . GLU A 11 ? 0.1621 0.1723 0.1580 -0.0035 -0.0186 -0.0133 11 GLU A N 67 C CA . GLU A 11 ? 0.1620 0.1686 0.1520 -0.0047 -0.0244 -0.0141 11 GLU A CA 68 C C . GLU A 11 ? 0.1536 0.1596 0.1423 -0.0028 -0.0209 -0.0192 11 GLU A C 69 O O . GLU A 11 ? 0.1072 0.1171 0.1040 0.0001 -0.0164 -0.0193 11 GLU A O 70 C CB . GLU A 11 ? 0.1203 0.1266 0.1237 -0.0056 -0.0309 -0.0099 11 GLU A CB 71 C CG . GLU A 11 ? 0.1851 0.1925 0.1963 -0.0063 -0.0332 -0.0025 11 GLU A CG 72 C CD . GLU A 11 ? 0.1929 0.2017 0.2259 -0.0054 -0.0357 0.0033 11 GLU A CD 73 O OE1 . GLU A 11 ? 0.1803 0.1893 0.2209 -0.0058 -0.0391 0.0020 11 GLU A OE1 74 O OE2 . GLU A 11 ? 0.1960 0.2052 0.2412 -0.0042 -0.0329 0.0096 11 GLU A OE2 75 N N . PHE A 12 ? 0.1216 0.1217 0.0992 -0.0044 -0.0225 -0.0230 12 PHE A N 76 C CA . PHE A 12 ? 0.1776 0.1748 0.1583 -0.0027 -0.0188 -0.0272 12 PHE A CA 77 C C . PHE A 12 ? 0.1764 0.1638 0.1488 -0.0069 -0.0243 -0.0324 12 PHE A C 78 O O . PHE A 12 ? 0.1771 0.1596 0.1338 -0.0110 -0.0306 -0.0335 12 PHE A O 79 C CB . PHE A 12 ? 0.2145 0.2139 0.1926 0.0010 -0.0091 -0.0285 12 PHE A CB 80 C CG . PHE A 12 ? 0.2275 0.2205 0.1890 0.0000 -0.0047 -0.0315 12 PHE A CG 81 C CD1 . PHE A 12 ? 0.2082 0.1892 0.1579 -0.0015 -0.0027 -0.0378 12 PHE A CD1 82 C CD2 . PHE A 12 ? 0.2088 0.2062 0.1666 0.0005 -0.0009 -0.0284 12 PHE A CD2 83 C CE1 . PHE A 12 ? 0.2000 0.1723 0.1309 -0.0018 0.0041 -0.0409 12 PHE A CE1 84 C CE2 . PHE A 12 ? 0.2501 0.2408 0.1932 0.0005 0.0059 -0.0300 12 PHE A CE2 85 C CZ . PHE A 12 ? 0.2175 0.1950 0.1454 -0.0002 0.0091 -0.0362 12 PHE A CZ 86 N N . TYR A 13 ? 0.1765 0.1605 0.1589 -0.0061 -0.0221 -0.0354 13 TYR A N 87 C CA . TYR A 13 ? 0.1838 0.1560 0.1585 -0.0108 -0.0256 -0.0430 13 TYR A CA 88 C C . TYR A 13 ? 0.2223 0.1891 0.2026 -0.0071 -0.0140 -0.0470 13 TYR A C 89 O O . TYR A 13 ? 0.2273 0.2008 0.2262 -0.0019 -0.0084 -0.0419 13 TYR A O 90 C CB . TYR A 13 ? 0.1903 0.1631 0.1799 -0.0156 -0.0371 -0.0419 13 TYR A CB 91 C CG . TYR A 13 ? 0.2365 0.1968 0.2149 -0.0232 -0.0446 -0.0512 13 TYR A CG 92 C CD1 . TYR A 13 ? 0.2455 0.1973 0.2348 -0.0243 -0.0402 -0.0575 13 TYR A CD1 93 C CD2 . TYR A 13 ? 0.2350 0.1907 0.1904 -0.0297 -0.0560 -0.0540 13 TYR A CD2 94 C CE1 . TYR A 13 ? 0.2725 0.2105 0.2504 -0.0327 -0.0471 -0.0682 13 TYR A CE1 95 C CE2 . TYR A 13 ? 0.2448 0.1876 0.1851 -0.0381 -0.0643 -0.0641 13 TYR A CE2 96 C CZ . TYR A 13 ? 0.2910 0.2243 0.2426 -0.0401 -0.0599 -0.0723 13 TYR A CZ 97 O OH . TYR A 13 ? 0.3837 0.3018 0.3193 -0.0498 -0.0684 -0.0846 13 TYR A OH 98 N N . LEU A 14 ? 0.2405 0.1940 0.2037 -0.0093 -0.0095 -0.0554 14 LEU A N 99 C CA . LEU A 14 ? 0.2419 0.1887 0.2113 -0.0049 0.0042 -0.0584 14 LEU A CA 100 C C . LEU A 14 ? 0.2548 0.1835 0.2194 -0.0105 0.0043 -0.0695 14 LEU A C 101 O O . LEU A 14 ? 0.2727 0.1887 0.2126 -0.0174 -0.0011 -0.0785 14 LEU A O 102 C CB . LEU A 14 ? 0.2537 0.1990 0.2095 -0.0008 0.0155 -0.0582 14 LEU A CB 103 C CG . LEU A 14 ? 0.2406 0.1789 0.2043 0.0047 0.0319 -0.0596 14 LEU A CG 104 C CD1 . LEU A 14 ? 0.1966 0.1501 0.1882 0.0120 0.0360 -0.0490 14 LEU A CD1 105 C CD2 . LEU A 14 ? 0.2123 0.1462 0.1609 0.0073 0.0430 -0.0603 14 LEU A CD2 106 N N . ASN A 15 ? 0.2435 0.1704 0.2309 -0.0079 0.0105 -0.0687 15 ASN A N 107 C CA . ASN A 15 ? 0.2551 0.1631 0.2427 -0.0128 0.0139 -0.0798 15 ASN A CA 108 C C . ASN A 15 ? 0.2758 0.1751 0.2676 -0.0058 0.0338 -0.0808 15 ASN A C 109 O O . ASN A 15 ? 0.2831 0.1958 0.2898 0.0035 0.0424 -0.0695 15 ASN A O 110 C CB . ASN A 15 ? 0.2559 0.1670 0.2723 -0.0148 0.0085 -0.0770 15 ASN A CB 111 C CG . ASN A 15 ? 0.3074 0.2190 0.3214 -0.0249 -0.0107 -0.0806 15 ASN A CG 112 O OD1 . ASN A 15 ? 0.3347 0.2372 0.3223 -0.0329 -0.0202 -0.0897 15 ASN A OD1 113 N ND2 . ASN A 15 ? 0.2089 0.1316 0.2511 -0.0245 -0.0163 -0.0722 15 ASN A ND2 114 N N . PRO A 16 ? 0.2687 0.1450 0.2475 -0.0103 0.0412 -0.0943 16 PRO A N 115 C CA . PRO A 16 ? 0.2994 0.1584 0.2579 -0.0224 0.0296 -0.1089 16 PRO A CA 116 C C . PRO A 16 ? 0.3420 0.1963 0.2612 -0.0261 0.0231 -0.1136 16 PRO A C 117 O O . PRO A 16 ? 0.3505 0.1944 0.2497 -0.0338 0.0119 -0.1225 16 PRO A O 118 C CB . PRO A 16 ? 0.3227 0.1656 0.2872 -0.0214 0.0418 -0.1140 16 PRO A CB 119 C CG . PRO A 16 ? 0.3156 0.1617 0.2854 -0.0103 0.0619 -0.1064 16 PRO A CG 120 C CD . PRO A 16 ? 0.4375 0.3045 0.4258 -0.0029 0.0621 -0.0938 16 PRO A CD 121 N N . ASP A 17 ? 0.3435 0.2069 0.2543 -0.0200 0.0299 -0.1068 17 ASP A N 122 C CA . ASP A 17 ? 0.3974 0.2581 0.2752 -0.0212 0.0275 -0.1080 17 ASP A CA 123 C C . ASP A 17 ? 0.3950 0.2615 0.2573 -0.0296 0.0052 -0.1086 17 ASP A C 124 O O . ASP A 17 ? 0.3960 0.2590 0.2315 -0.0321 0.0005 -0.1111 17 ASP A O 125 C CB . ASP A 17 ? 0.3799 0.2511 0.2590 -0.0128 0.0397 -0.0984 17 ASP A CB 126 C CG . ASP A 17 ? 0.4240 0.2953 0.3256 -0.0034 0.0601 -0.0939 17 ASP A CG 127 O OD1 . ASP A 17 ? 0.3731 0.2553 0.3054 0.0010 0.0615 -0.0872 17 ASP A OD1 128 O OD2 . ASP A 17 ? 0.5020 0.3661 0.3943 0.0001 0.0732 -0.0938 17 ASP A OD2 129 N N . GLN A 18 ? 0.4034 0.2808 0.2862 -0.0331 -0.0075 -0.1042 18 GLN A N 130 C CA . GLN A 18 ? 0.3803 0.2675 0.2576 -0.0398 -0.0290 -0.1004 18 GLN A CA 131 C C . GLN A 18 ? 0.3805 0.2766 0.2387 -0.0365 -0.0298 -0.0922 18 GLN A C 132 O O . GLN A 18 ? 0.4013 0.3014 0.2432 -0.0403 -0.0409 -0.0906 18 GLN A O 133 C CB . GLN A 18 ? 0.4195 0.3014 0.2882 -0.0482 -0.0412 -0.1096 18 GLN A CB 134 C CG . GLN A 18 ? 0.4230 0.2972 0.3160 -0.0525 -0.0424 -0.1171 18 GLN A CG 135 C CD . GLN A 18 ? 0.4578 0.3322 0.3479 -0.0631 -0.0573 -0.1256 18 GLN A CD 136 O OE1 . GLN A 18 ? 0.4496 0.3316 0.3644 -0.0710 -0.0665 -0.1236 18 GLN A OE1 137 N NE2 . GLN A 18 ? 0.4980 0.3632 0.3560 -0.0646 -0.0581 -0.1337 18 GLN A NE2 138 N N . SER A 19 ? 0.3082 0.2133 0.1773 -0.0275 -0.0166 -0.0841 19 SER A N 139 C CA . SER A 19 ? 0.3032 0.2175 0.1616 -0.0242 -0.0160 -0.0754 19 SER A CA 140 C C . SER A 19 ? 0.2782 0.2132 0.1634 -0.0215 -0.0239 -0.0632 19 SER A C 141 O O . SER A 19 ? 0.2722 0.2165 0.1845 -0.0170 -0.0195 -0.0593 19 SER A O 142 C CB . SER A 19 ? 0.3615 0.2730 0.2163 -0.0167 0.0041 -0.0744 19 SER A CB 143 O OG . SER A 19 ? 0.4917 0.3828 0.3303 -0.0174 0.0162 -0.0857 19 SER A OG 144 N N . GLY A 20 ? 0.2897 0.2307 0.1660 -0.0241 -0.0346 -0.0570 20 GLY A N 145 C CA . GLY A 20 ? 0.3412 0.2986 0.2412 -0.0215 -0.0399 -0.0460 20 GLY A CA 146 C C . GLY A 20 ? 0.3831 0.3458 0.2739 -0.0193 -0.0378 -0.0382 20 GLY A C 147 O O . GLY A 20 ? 0.4869 0.4429 0.3519 -0.0222 -0.0413 -0.0379 20 GLY A O 148 N N . GLU A 21 ? 0.3016 0.2754 0.2123 -0.0146 -0.0319 -0.0318 21 GLU A N 149 C CA . GLU A 21 ? 0.3118 0.2901 0.2190 -0.0127 -0.0280 -0.0247 21 GLU A CA 150 C C . GLU A 21 ? 0.2343 0.2230 0.1636 -0.0120 -0.0329 -0.0168 21 GLU A C 151 O O . GLU A 21 ? 0.1740 0.1674 0.1228 -0.0110 -0.0341 -0.0172 21 GLU A O 152 C CB . GLU A 21 ? 0.3377 0.3175 0.2474 -0.0084 -0.0136 -0.0259 21 GLU A CB 153 C CG . GLU A 21 ? 0.4186 0.4022 0.3271 -0.0072 -0.0082 -0.0192 21 GLU A CG 154 C CD . GLU A 21 ? 0.4420 0.4301 0.3607 -0.0038 0.0041 -0.0193 21 GLU A CD 155 O OE1 . GLU A 21 ? 0.4379 0.4193 0.3456 -0.0020 0.0137 -0.0223 21 GLU A OE1 156 O OE2 . GLU A 21 ? 0.4102 0.4084 0.3485 -0.0033 0.0043 -0.0165 21 GLU A OE2 157 N N . PHE A 22 ? 0.2279 0.2185 0.1540 -0.0122 -0.0337 -0.0093 22 PHE A N 158 C CA . PHE A 22 ? 0.1741 0.1717 0.1212 -0.0113 -0.0357 -0.0018 22 PHE A CA 159 C C . PHE A 22 ? 0.1767 0.1750 0.1222 -0.0099 -0.0277 0.0033 22 PHE A C 160 O O . PHE A 22 ? 0.1805 0.1747 0.1081 -0.0104 -0.0274 0.0073 22 PHE A O 161 C CB . PHE A 22 ? 0.2004 0.1992 0.1503 -0.0138 -0.0486 0.0053 22 PHE A CB 162 C CG . PHE A 22 ? 0.2055 0.2100 0.1801 -0.0121 -0.0489 0.0144 22 PHE A CG 163 C CD1 . PHE A 22 ? 0.2062 0.2112 0.1832 -0.0107 -0.0441 0.0224 22 PHE A CD1 164 C CD2 . PHE A 22 ? 0.2306 0.2386 0.2276 -0.0117 -0.0523 0.0157 22 PHE A CD2 165 C CE1 . PHE A 22 ? 0.2153 0.2232 0.2164 -0.0089 -0.0421 0.0303 22 PHE A CE1 166 C CE2 . PHE A 22 ? 0.2338 0.2448 0.2541 -0.0095 -0.0497 0.0241 22 PHE A CE2 167 C CZ . PHE A 22 ? 0.2108 0.2213 0.2330 -0.0081 -0.0445 0.0310 22 PHE A CZ 168 N N . MET A 23 ? 0.1420 0.1445 0.1049 -0.0086 -0.0209 0.0030 23 MET A N 169 C CA . MET A 23 ? 0.2159 0.2187 0.1820 -0.0084 -0.0132 0.0071 23 MET A CA 170 C C . MET A 23 ? 0.2052 0.2102 0.1924 -0.0088 -0.0096 0.0075 23 MET A C 171 O O . MET A 23 ? 0.2198 0.2261 0.2163 -0.0085 -0.0110 0.0033 23 MET A O 172 C CB . MET A 23 ? 0.2050 0.2082 0.1642 -0.0079 -0.0048 0.0026 23 MET A CB 173 C CG . MET A 23 ? 0.1753 0.1838 0.1443 -0.0074 -0.0029 -0.0049 23 MET A CG 174 S SD . MET A 23 ? 0.2453 0.2599 0.2344 -0.0094 0.0010 -0.0064 23 MET A SD 175 C CE . MET A 23 ? 0.1263 0.1422 0.1175 -0.0103 0.0098 -0.0024 23 MET A CE 176 N N . PHE A 24 ? 0.1860 0.1898 0.1797 -0.0095 -0.0037 0.0124 24 PHE A N 177 C CA . PHE A 24 ? 0.1818 0.1846 0.1936 -0.0110 0.0016 0.0105 24 PHE A CA 178 C C . PHE A 24 ? 0.1900 0.1949 0.2060 -0.0137 0.0081 0.0059 24 PHE A C 179 O O . PHE A 24 ? 0.2032 0.2088 0.2146 -0.0135 0.0121 0.0101 24 PHE A O 180 C CB . PHE A 24 ? 0.1352 0.1337 0.1579 -0.0103 0.0038 0.0207 24 PHE A CB 181 C CG . PHE A 24 ? 0.2382 0.2351 0.2719 -0.0085 0.0002 0.0239 24 PHE A CG 182 C CD1 . PHE A 24 ? 0.2253 0.2254 0.2533 -0.0069 -0.0095 0.0285 24 PHE A CD1 183 C CD2 . PHE A 24 ? 0.2513 0.2426 0.3024 -0.0089 0.0074 0.0222 24 PHE A CD2 184 C CE1 . PHE A 24 ? 0.2365 0.2367 0.2805 -0.0052 -0.0122 0.0331 24 PHE A CE1 185 C CE2 . PHE A 24 ? 0.1942 0.1834 0.2585 -0.0063 0.0071 0.0263 24 PHE A CE2 186 C CZ . PHE A 24 ? 0.1926 0.1873 0.2555 -0.0042 -0.0028 0.0327 24 PHE A CZ 187 N N . ASP A 25 ? 0.2105 0.2165 0.2353 -0.0165 0.0091 -0.0023 25 ASP A N 188 C CA . ASP A 25 ? 0.1802 0.1906 0.2123 -0.0205 0.0122 -0.0071 25 ASP A CA 189 C C . ASP A 25 ? 0.1849 0.1892 0.2307 -0.0252 0.0162 -0.0109 25 ASP A C 190 O O . ASP A 25 ? 0.1871 0.1852 0.2333 -0.0254 0.0162 -0.0150 25 ASP A O 191 C CB . ASP A 25 ? 0.2109 0.2289 0.2383 -0.0206 0.0075 -0.0142 25 ASP A CB 192 C CG . ASP A 25 ? 0.2851 0.3107 0.3231 -0.0255 0.0077 -0.0182 25 ASP A CG 193 O OD1 . ASP A 25 ? 0.2643 0.2877 0.3099 -0.0309 0.0072 -0.0240 25 ASP A OD1 194 O OD2 . ASP A 25 ? 0.3519 0.3854 0.3915 -0.0241 0.0085 -0.0155 25 ASP A OD2 195 N N . PHE A 26 ? 0.1569 0.1617 0.2148 -0.0293 0.0211 -0.0099 26 PHE A N 196 C CA . PHE A 26 ? 0.1634 0.1613 0.2354 -0.0356 0.0251 -0.0160 26 PHE A CA 197 C C . PHE A 26 ? 0.1707 0.1771 0.2511 -0.0424 0.0219 -0.0231 26 PHE A C 198 O O . PHE A 26 ? 0.1854 0.1984 0.2762 -0.0431 0.0249 -0.0175 26 PHE A O 199 C CB . PHE A 26 ? 0.1448 0.1349 0.2303 -0.0352 0.0342 -0.0068 26 PHE A CB 200 C CG . PHE A 26 ? 0.1658 0.1465 0.2689 -0.0424 0.0402 -0.0136 26 PHE A CG 201 C CD1 . PHE A 26 ? 0.2282 0.1957 0.3335 -0.0429 0.0445 -0.0180 26 PHE A CD1 202 C CD2 . PHE A 26 ? 0.1688 0.1527 0.2880 -0.0491 0.0428 -0.0157 26 PHE A CD2 203 C CE1 . PHE A 26 ? 0.2829 0.2383 0.4028 -0.0501 0.0516 -0.0261 26 PHE A CE1 204 C CE2 . PHE A 26 ? 0.1937 0.1673 0.3296 -0.0572 0.0479 -0.0236 26 PHE A CE2 205 C CZ . PHE A 26 ? 0.2364 0.1946 0.3710 -0.0579 0.0525 -0.0296 26 PHE A CZ 206 N N . ASP A 27 ? 0.1591 0.1654 0.2353 -0.0474 0.0162 -0.0346 27 ASP A N 207 C CA . ASP A 27 ? 0.1634 0.1794 0.2482 -0.0553 0.0098 -0.0415 27 ASP A CA 208 C C . ASP A 27 ? 0.1736 0.2063 0.2633 -0.0524 0.0063 -0.0345 27 ASP A C 209 O O . ASP A 27 ? 0.2171 0.2593 0.3250 -0.0580 0.0045 -0.0342 27 ASP A O 210 C CB . ASP A 27 ? 0.1564 0.1661 0.2619 -0.0640 0.0146 -0.0449 27 ASP A CB 211 C CG . ASP A 27 ? 0.2223 0.2143 0.3237 -0.0689 0.0181 -0.0555 27 ASP A CG 212 O OD1 . ASP A 27 ? 0.1741 0.1598 0.2561 -0.0657 0.0165 -0.0604 27 ASP A OD1 213 O OD2 . ASP A 27 ? 0.2431 0.2261 0.3618 -0.0759 0.0241 -0.0589 27 ASP A OD2 214 N N . GLY A 28 ? 0.2085 0.2440 0.2843 -0.0439 0.0062 -0.0289 28 GLY A N 215 C CA . GLY A 28 ? 0.1652 0.2135 0.2443 -0.0402 0.0054 -0.0229 28 GLY A CA 216 C C . GLY A 28 ? 0.1863 0.2324 0.2680 -0.0353 0.0153 -0.0130 28 GLY A C 217 O O . GLY A 28 ? 0.1496 0.2029 0.2322 -0.0311 0.0181 -0.0080 28 GLY A O 218 N N . ASP A 29 ? 0.2122 0.2474 0.2942 -0.0352 0.0218 -0.0094 29 ASP A N 219 C CA . ASP A 29 ? 0.1857 0.2169 0.2634 -0.0300 0.0311 0.0010 29 ASP A CA 220 C C . ASP A 29 ? 0.1893 0.2111 0.2453 -0.0244 0.0302 0.0044 29 ASP A C 221 O O . ASP A 29 ? 0.2152 0.2315 0.2686 -0.0252 0.0259 0.0012 29 ASP A O 222 C CB . ASP A 29 ? 0.1925 0.2201 0.2893 -0.0336 0.0399 0.0065 29 ASP A CB 223 C CG . ASP A 29 ? 0.2222 0.2605 0.3425 -0.0374 0.0435 0.0079 29 ASP A CG 224 O OD1 . ASP A 29 ? 0.2211 0.2637 0.3394 -0.0324 0.0501 0.0147 29 ASP A OD1 225 O OD2 . ASP A 29 ? 0.1383 0.1801 0.2797 -0.0457 0.0400 0.0021 29 ASP A OD2 226 N N . GLU A 30 ? 0.1984 0.2180 0.2391 -0.0191 0.0343 0.0110 30 GLU A N 227 C CA . GLU A 30 ? 0.2053 0.2177 0.2247 -0.0150 0.0306 0.0143 30 GLU A CA 228 C C . GLU A 30 ? 0.2287 0.2340 0.2495 -0.0145 0.0342 0.0238 30 GLU A C 229 O O . GLU A 30 ? 0.2460 0.2494 0.2705 -0.0139 0.0434 0.0317 30 GLU A O 230 C CB . GLU A 30 ? 0.1932 0.2037 0.1915 -0.0107 0.0332 0.0162 30 GLU A CB 231 C CG . GLU A 30 ? 0.2444 0.2473 0.2187 -0.0081 0.0277 0.0197 30 GLU A CG 232 C CD . GLU A 30 ? 0.2521 0.2490 0.2012 -0.0051 0.0324 0.0206 30 GLU A CD 233 O OE1 . GLU A 30 ? 0.2394 0.2379 0.1920 -0.0038 0.0415 0.0186 30 GLU A OE1 234 O OE2 . GLU A 30 ? 0.2746 0.2646 0.2005 -0.0041 0.0270 0.0235 30 GLU A OE2 235 N N . ILE A 31 ? 0.2280 0.2298 0.2486 -0.0142 0.0281 0.0248 31 ILE A N 236 C CA . ILE A 31 ? 0.2046 0.2008 0.2276 -0.0124 0.0307 0.0365 31 ILE A CA 237 C C . ILE A 31 ? 0.2192 0.2134 0.2166 -0.0083 0.0270 0.0451 31 ILE A C 238 O O . ILE A 31 ? 0.2203 0.2111 0.2106 -0.0062 0.0332 0.0560 31 ILE A O 239 C CB . ILE A 31 ? 0.2236 0.2168 0.2592 -0.0128 0.0267 0.0363 31 ILE A CB 240 C CG1 . ILE A 31 ? 0.1973 0.1893 0.2512 -0.0176 0.0301 0.0251 31 ILE A CG1 241 C CG2 . ILE A 31 ? 0.1702 0.1588 0.2134 -0.0102 0.0303 0.0511 31 ILE A CG2 242 C CD1 . ILE A 31 ? 0.1605 0.1463 0.2257 -0.0175 0.0300 0.0238 31 ILE A CD1 243 N N . PHE A 32 ? 0.2064 0.2020 0.1892 -0.0077 0.0169 0.0399 32 PHE A N 244 C CA . PHE A 32 ? 0.2372 0.2299 0.1923 -0.0057 0.0108 0.0444 32 PHE A CA 245 C C . PHE A 32 ? 0.2693 0.2632 0.2131 -0.0066 0.0024 0.0336 32 PHE A C 246 O O . PHE A 32 ? 0.2910 0.2887 0.2497 -0.0077 0.0004 0.0256 32 PHE A O 247 C CB . PHE A 32 ? 0.2325 0.2246 0.1868 -0.0044 0.0036 0.0574 32 PHE A CB 248 C CG . PHE A 32 ? 0.1976 0.1934 0.1685 -0.0051 -0.0061 0.0562 32 PHE A CG 249 C CD1 . PHE A 32 ? 0.2010 0.1987 0.1603 -0.0061 -0.0190 0.0534 32 PHE A CD1 250 C CD2 . PHE A 32 ? 0.2182 0.2142 0.2176 -0.0051 -0.0009 0.0578 32 PHE A CD2 251 C CE1 . PHE A 32 ? 0.2061 0.2077 0.1849 -0.0063 -0.0261 0.0538 32 PHE A CE1 252 C CE2 . PHE A 32 ? 0.2188 0.2167 0.2342 -0.0048 -0.0067 0.0576 32 PHE A CE2 253 C CZ . PHE A 32 ? 0.1960 0.1976 0.2025 -0.0050 -0.0191 0.0565 32 PHE A CZ 254 N N . HIS A 33 ? 0.2873 0.2764 0.2033 -0.0063 -0.0018 0.0334 33 HIS A N 255 C CA . HIS A 33 ? 0.2708 0.2592 0.1771 -0.0078 -0.0114 0.0246 33 HIS A CA 256 C C . HIS A 33 ? 0.3234 0.3081 0.2074 -0.0094 -0.0237 0.0301 33 HIS A C 257 O O . HIS A 33 ? 0.3241 0.3065 0.1953 -0.0084 -0.0234 0.0409 33 HIS A O 258 C CB . HIS A 33 ? 0.2737 0.2581 0.1683 -0.0072 -0.0037 0.0143 33 HIS A CB 259 C CG . HIS A 33 ? 0.2861 0.2606 0.1504 -0.0062 0.0033 0.0157 33 HIS A CG 260 N ND1 . HIS A 33 ? 0.2923 0.2650 0.1565 -0.0036 0.0177 0.0210 33 HIS A ND1 261 C CD2 . HIS A 33 ? 0.2652 0.2294 0.0971 -0.0076 -0.0013 0.0121 33 HIS A CD2 262 C CE1 . HIS A 33 ? 0.2917 0.2529 0.1234 -0.0024 0.0234 0.0213 33 HIS A CE1 263 N NE2 . HIS A 33 ? 0.2899 0.2450 0.0992 -0.0052 0.0117 0.0151 33 HIS A NE2 264 N N . VAL A 34 ? 0.3133 0.2979 0.1933 -0.0121 -0.0351 0.0236 34 VAL A N 265 C CA . VAL A 34 ? 0.3175 0.2993 0.1759 -0.0154 -0.0498 0.0272 34 VAL A CA 266 C C . VAL A 34 ? 0.3553 0.3253 0.1796 -0.0180 -0.0496 0.0158 34 VAL A C 267 O O . VAL A 34 ? 0.3143 0.2815 0.1429 -0.0189 -0.0470 0.0038 34 VAL A O 268 C CB . VAL A 34 ? 0.2759 0.2657 0.1572 -0.0179 -0.0647 0.0292 34 VAL A CB 269 C CG1 . VAL A 34 ? 0.2709 0.2588 0.1305 -0.0232 -0.0828 0.0308 34 VAL A CG1 270 C CG2 . VAL A 34 ? 0.2773 0.2759 0.1894 -0.0149 -0.0636 0.0420 34 VAL A CG2 271 N N . ASP A 35 ? 0.4125 0.3741 0.2017 -0.0191 -0.0512 0.0198 35 ASP A N 272 C CA . ASP A 35 ? 0.4738 0.4227 0.2293 -0.0218 -0.0510 0.0080 35 ASP A CA 273 C C . ASP A 35 ? 0.5112 0.4655 0.2759 -0.0268 -0.0690 0.0028 35 ASP A C 274 O O . ASP A 35 ? 0.4978 0.4589 0.2614 -0.0286 -0.0827 0.0110 35 ASP A O 275 C CB . ASP A 35 ? 0.5371 0.4807 0.2629 -0.0195 -0.0457 0.0143 35 ASP A CB 276 C CG . ASP A 35 ? 0.5720 0.5040 0.2705 -0.0205 -0.0397 0.0010 35 ASP A CG 277 O OD1 . ASP A 35 ? 0.5307 0.4605 0.2312 -0.0248 -0.0476 -0.0111 35 ASP A OD1 278 O OD2 . ASP A 35 ? 0.6449 0.5693 0.3214 -0.0172 -0.0258 0.0030 35 ASP A OD2 279 N N . MET A 36 ? 0.5302 0.4816 0.3060 -0.0289 -0.0682 -0.0097 36 MET A N 280 C CA . MET A 36 ? 0.5358 0.4924 0.3273 -0.0340 -0.0832 -0.0141 36 MET A CA 281 C C . MET A 36 ? 0.5872 0.5391 0.3542 -0.0383 -0.0918 -0.0192 36 MET A C 282 O O . MET A 36 ? 0.5829 0.5429 0.3598 -0.0426 -0.1082 -0.0157 36 MET A O 283 C CB . MET A 36 ? 0.5209 0.4740 0.3292 -0.0346 -0.0779 -0.0256 36 MET A CB 284 C CG . MET A 36 ? 0.5088 0.4734 0.3536 -0.0358 -0.0874 -0.0211 36 MET A CG 285 S SD . MET A 36 ? 0.4917 0.4687 0.3620 -0.0301 -0.0836 -0.0064 36 MET A SD 286 C CE . MET A 36 ? 0.7426 0.7154 0.6127 -0.0237 -0.0607 -0.0131 36 MET A CE 287 N N . ALA A 37 ? 0.5908 0.5295 0.3269 -0.0372 -0.0802 -0.0272 37 ALA A N 288 C CA . ALA A 37 ? 0.5905 0.5221 0.2978 -0.0415 -0.0868 -0.0341 37 ALA A CA 289 C C . ALA A 37 ? 0.5827 0.5218 0.2749 -0.0415 -0.0983 -0.0212 37 ALA A C 290 O O . ALA A 37 ? 0.5810 0.5230 0.2641 -0.0467 -0.1141 -0.0225 37 ALA A O 291 C CB . ALA A 37 ? 0.5914 0.5058 0.2709 -0.0393 -0.0686 -0.0450 37 ALA A CB 292 N N . LYS A 38 ? 0.5885 0.5311 0.2790 -0.0355 -0.0903 -0.0081 38 LYS A N 293 C CA . LYS A 38 ? 0.5910 0.5407 0.2686 -0.0336 -0.0985 0.0068 38 LYS A CA 294 C C . LYS A 38 ? 0.5438 0.5096 0.2549 -0.0334 -0.1128 0.0214 38 LYS A C 295 O O . LYS A 38 ? 0.5417 0.5152 0.2482 -0.0320 -0.1226 0.0349 38 LYS A O 296 C CB . LYS A 38 ? 0.6060 0.5504 0.2660 -0.0268 -0.0807 0.0153 38 LYS A CB 297 C CG . LYS A 38 ? 0.6788 0.6077 0.3053 -0.0260 -0.0648 0.0041 38 LYS A CG 298 C CD . LYS A 38 ? 0.7329 0.6594 0.3448 -0.0195 -0.0484 0.0163 38 LYS A CD 299 C CE . LYS A 38 ? 0.7896 0.7004 0.3707 -0.0184 -0.0308 0.0066 38 LYS A CE 300 N NZ . LYS A 38 ? 0.8187 0.7284 0.3849 -0.0129 -0.0162 0.0203 38 LYS A NZ 301 N N . LYS A 39 ? 0.5208 0.4916 0.2663 -0.0344 -0.1130 0.0194 39 LYS A N 302 C CA . LYS A 39 ? 0.5140 0.4993 0.2967 -0.0337 -0.1228 0.0331 39 LYS A CA 303 C C . LYS A 39 ? 0.5104 0.4991 0.2941 -0.0275 -0.1165 0.0505 39 LYS A C 304 O O . LYS A 39 ? 0.5044 0.5031 0.3016 -0.0262 -0.1261 0.0654 39 LYS A O 305 C CB . LYS A 39 ? 0.5631 0.5579 0.3556 -0.0387 -0.1426 0.0364 39 LYS A CB 306 C CG . LYS A 39 ? 0.6394 0.6308 0.4336 -0.0457 -0.1496 0.0205 39 LYS A CG 307 C CD . LYS A 39 ? 0.7350 0.7338 0.5262 -0.0513 -0.1694 0.0238 39 LYS A CD 308 C CE . LYS A 39 ? 0.7748 0.7707 0.5706 -0.0594 -0.1777 0.0090 39 LYS A CE 309 N NZ . LYS A 39 ? 0.7517 0.7468 0.5787 -0.0595 -0.1701 0.0025 39 LYS A NZ 310 N N . GLU A 40 ? 0.5409 0.5210 0.3127 -0.0238 -0.0992 0.0492 40 GLU A N 311 C CA . GLU A 40 ? 0.5322 0.5135 0.3057 -0.0184 -0.0900 0.0655 40 GLU A CA 312 C C . GLU A 40 ? 0.4604 0.4399 0.2524 -0.0168 -0.0758 0.0671 40 GLU A C 313 O O . GLU A 40 ? 0.4327 0.4066 0.2254 -0.0172 -0.0660 0.0523 40 GLU A O 314 C CB . GLU A 40 ? 0.6104 0.5825 0.3444 -0.0151 -0.0812 0.0675 40 GLU A CB 315 C CG . GLU A 40 ? 0.7028 0.6790 0.4180 -0.0150 -0.0952 0.0740 40 GLU A CG 316 C CD . GLU A 40 ? 0.8242 0.7915 0.4983 -0.0112 -0.0844 0.0753 40 GLU A CD 317 O OE1 . GLU A 40 ? 0.8618 0.8227 0.5311 -0.0071 -0.0650 0.0788 40 GLU A OE1 318 O OE2 . GLU A 40 ? 0.8741 0.8414 0.5217 -0.0128 -0.0949 0.0733 40 GLU A OE2 319 N N . THR A 41 ? 0.4276 0.4145 0.2452 -0.0126 -0.0707 0.0826 41 THR A N 320 C CA . THR A 41 ? 0.3797 0.3678 0.2279 -0.0086 -0.0524 0.0803 41 THR A CA 321 C C . THR A 41 ? 0.3840 0.3631 0.2121 -0.0055 -0.0344 0.0808 41 THR A C 322 O O . THR A 41 ? 0.3442 0.3201 0.1529 -0.0032 -0.0326 0.0942 41 THR A O 323 C CB . THR A 41 ? 0.3638 0.3608 0.2497 -0.0056 -0.0520 0.0953 41 THR A CB 324 O OG1 . THR A 41 ? 0.3817 0.3868 0.2913 -0.0076 -0.0655 0.0952 41 THR A OG1 325 C CG2 . THR A 41 ? 0.3007 0.2963 0.2136 -0.0030 -0.0334 0.0912 41 THR A CG2 326 N N . VAL A 42 ? 0.3683 0.3440 0.2029 -0.0050 -0.0210 0.0678 42 VAL A N 327 C CA . VAL A 42 ? 0.3643 0.3326 0.1870 -0.0020 -0.0024 0.0683 42 VAL A CA 328 C C . VAL A 42 ? 0.3328 0.3070 0.1944 -0.0004 0.0103 0.0696 42 VAL A C 329 O O . VAL A 42 ? 0.3130 0.2911 0.1947 -0.0019 0.0124 0.0580 42 VAL A O 330 C CB . VAL A 42 ? 0.3890 0.3486 0.1888 -0.0028 0.0041 0.0533 42 VAL A CB 331 C CG1 . VAL A 42 ? 0.3912 0.3435 0.1820 0.0010 0.0250 0.0562 42 VAL A CG1 332 C CG2 . VAL A 42 ? 0.4089 0.3602 0.1694 -0.0062 -0.0092 0.0486 42 VAL A CG2 333 N N . TRP A 43 ? 0.3329 0.3071 0.2044 0.0022 0.0183 0.0838 43 TRP A N 334 C CA . TRP A 43 ? 0.3171 0.2951 0.2258 0.0022 0.0297 0.0844 43 TRP A CA 335 C C . TRP A 43 ? 0.3183 0.2938 0.2287 0.0027 0.0456 0.0786 43 TRP A C 336 O O . TRP A 43 ? 0.3170 0.2854 0.2018 0.0054 0.0544 0.0830 43 TRP A O 337 C CB . TRP A 43 ? 0.3371 0.3150 0.2599 0.0047 0.0339 0.1022 43 TRP A CB 338 C CG . TRP A 43 ? 0.3532 0.3354 0.2814 0.0050 0.0192 0.1104 43 TRP A CG 339 C CD1 . TRP A 43 ? 0.3753 0.3578 0.2784 0.0065 0.0074 0.1224 43 TRP A CD1 340 C CD2 . TRP A 43 ? 0.3152 0.3023 0.2757 0.0035 0.0141 0.1074 43 TRP A CD2 341 N NE1 . TRP A 43 ? 0.3806 0.3701 0.3040 0.0063 -0.0051 0.1289 43 TRP A NE1 342 C CE2 . TRP A 43 ? 0.3327 0.3240 0.2914 0.0050 0.0004 0.1197 43 TRP A CE2 343 C CE3 . TRP A 43 ? 0.2598 0.2475 0.2495 0.0010 0.0200 0.0959 43 TRP A CE3 344 C CZ2 . TRP A 43 ? 0.2844 0.2802 0.2731 0.0049 -0.0049 0.1216 43 TRP A CZ2 345 C CZ3 . TRP A 43 ? 0.2459 0.2357 0.2593 0.0008 0.0151 0.0962 43 TRP A CZ3 346 C CH2 . TRP A 43 ? 0.2236 0.2173 0.2383 0.0032 0.0040 0.1093 43 TRP A CH2 347 N N . ARG A 44 ? 0.3514 0.3326 0.2918 0.0000 0.0493 0.0693 44 ARG A N 348 C CA . ARG A 44 ? 0.3576 0.3398 0.3057 -0.0001 0.0618 0.0640 44 ARG A CA 349 C C . ARG A 44 ? 0.3131 0.2919 0.2698 0.0019 0.0780 0.0765 44 ARG A C 350 O O . ARG A 44 ? 0.3062 0.2814 0.2533 0.0046 0.0908 0.0787 44 ARG A O 351 C CB . ARG A 44 ? 0.3155 0.3064 0.2938 -0.0044 0.0588 0.0525 44 ARG A CB 352 C CG . ARG A 44 ? 0.2846 0.2802 0.2765 -0.0050 0.0691 0.0486 44 ARG A CG 353 C CD . ARG A 44 ? 0.2544 0.2462 0.2206 -0.0013 0.0720 0.0448 44 ARG A CD 354 N NE . ARG A 44 ? 0.2488 0.2458 0.2323 -0.0007 0.0835 0.0435 44 ARG A NE 355 C CZ . ARG A 44 ? 0.2460 0.2394 0.2323 0.0022 0.1001 0.0522 44 ARG A CZ 356 N NH1 . ARG A 44 ? 0.2576 0.2414 0.2264 0.0049 0.1072 0.0628 44 ARG A NH1 357 N NH2 . ARG A 44 ? 0.2263 0.2263 0.2341 0.0029 0.1102 0.0519 44 ARG A NH2 358 N N . LEU A 45 ? 0.3183 0.2974 0.2954 0.0011 0.0790 0.0854 45 LEU A N 359 C CA . LEU A 45 ? 0.3255 0.3000 0.3099 0.0038 0.0939 0.1005 45 LEU A CA 360 C C . LEU A 45 ? 0.3685 0.3382 0.3340 0.0075 0.0887 0.1152 45 LEU A C 361 O O . LEU A 45 ? 0.4049 0.3775 0.3783 0.0062 0.0764 0.1147 45 LEU A O 362 C CB . LEU A 45 ? 0.3045 0.2824 0.3334 -0.0008 0.1012 0.0998 45 LEU A CB 363 C CG . LEU A 45 ? 0.3406 0.3261 0.3936 -0.0059 0.1038 0.0869 45 LEU A CG 364 C CD1 . LEU A 45 ? 0.3638 0.3507 0.4585 -0.0114 0.1116 0.0881 45 LEU A CD1 365 C CD2 . LEU A 45 ? 0.2736 0.2592 0.3127 -0.0023 0.1142 0.0884 45 LEU A CD2 366 N N . GLU A 46 ? 0.5025 0.5109 0.4780 0.0795 0.1568 0.2016 46 GLU A N 367 C CA . GLU A 46 ? 0.5427 0.5248 0.4773 0.0922 0.1489 0.2137 46 GLU A CA 368 C C . GLU A 46 ? 0.5237 0.4804 0.4838 0.0822 0.1394 0.2220 46 GLU A C 369 O O . GLU A 46 ? 0.4753 0.4118 0.4135 0.0920 0.1229 0.2212 46 GLU A O 370 C CB . GLU A 46 ? 0.6193 0.6039 0.5208 0.1022 0.1644 0.2307 46 GLU A CB 371 C CG . GLU A 46 ? 0.7385 0.7165 0.6630 0.0903 0.1771 0.2536 46 GLU A CG 372 C CD . GLU A 46 ? 0.8391 0.7858 0.7414 0.0953 0.1660 0.2647 46 GLU A CD 373 O OE1 . GLU A 46 ? 0.8905 0.8253 0.7584 0.1094 0.1481 0.2549 46 GLU A OE1 374 O OE2 . GLU A 46 ? 0.8432 0.7778 0.7633 0.0848 0.1733 0.2822 46 GLU A OE2 375 N N . GLU A 47 ? 0.5118 0.4689 0.5178 0.0630 0.1492 0.2303 47 GLU A N 376 C CA . GLU A 47 ? 0.5298 0.4569 0.5591 0.0529 0.1415 0.2379 47 GLU A CA 377 C C . GLU A 47 ? 0.5097 0.4246 0.5459 0.0567 0.1167 0.2128 47 GLU A C 378 O O . GLU A 47 ? 0.5242 0.4112 0.5580 0.0607 0.1068 0.2186 47 GLU A O 379 C CB . GLU A 47 ? 0.6063 0.5377 0.6851 0.0286 0.1513 0.2428 47 GLU A CB 380 C CG . GLU A 47 ? 0.6522 0.6068 0.7680 0.0165 0.1478 0.2210 47 GLU A CG 381 C CD . GLU A 47 ? 0.6951 0.6447 0.8589 -0.0085 0.1483 0.2225 47 GLU A CD 382 O OE1 . GLU A 47 ? 0.6874 0.6579 0.8666 -0.0193 0.1604 0.2329 47 GLU A OE1 383 O OE2 . GLU A 47 ? 0.7067 0.6314 0.8889 -0.0159 0.1329 0.2092 47 GLU A OE2 384 N N . PHE A 48 ? 0.4488 0.3852 0.4934 0.0566 0.1079 0.1863 48 PHE A N 385 C CA . PHE A 48 ? 0.4144 0.3442 0.4692 0.0592 0.0870 0.1630 48 PHE A CA 386 C C . PHE A 48 ? 0.4438 0.3608 0.4663 0.0768 0.0728 0.1661 48 PHE A C 387 O O . PHE A 48 ? 0.3792 0.2811 0.4127 0.0802 0.0596 0.1606 48 PHE A O 388 C CB . PHE A 48 ? 0.3240 0.2797 0.3845 0.0583 0.0815 0.1371 48 PHE A CB 389 C CG . PHE A 48 ? 0.4064 0.3774 0.5033 0.0420 0.0905 0.1302 48 PHE A CG 390 C CD1 . PHE A 48 ? 0.3183 0.2791 0.4451 0.0263 0.0998 0.1445 48 PHE A CD1 391 C CD2 . PHE A 48 ? 0.2688 0.2634 0.3703 0.0419 0.0880 0.1097 48 PHE A CD2 392 C CE1 . PHE A 48 ? 0.2999 0.2778 0.4627 0.0100 0.1051 0.1382 48 PHE A CE1 393 C CE2 . PHE A 48 ? 0.2501 0.2614 0.3855 0.0283 0.0943 0.1037 48 PHE A CE2 394 C CZ . PHE A 48 ? 0.4599 0.4648 0.6273 0.0118 0.1022 0.1178 48 PHE A CZ 395 N N . GLY A 49 ? 0.4470 0.3710 0.4290 0.0890 0.0753 0.1749 49 GLY A N 396 C CA . GLY A 49 ? 0.4224 0.3391 0.3717 0.1052 0.0588 0.1768 49 GLY A CA 397 C C . GLY A 49 ? 0.4630 0.3538 0.4035 0.1124 0.0581 0.2004 49 GLY A C 398 O O . GLY A 49 ? 0.6180 0.5048 0.5381 0.1249 0.0416 0.2008 49 GLY A O 399 N N . ARG A 50 ? 0.5032 0.3777 0.4604 0.1027 0.0747 0.2186 50 ARG A N 400 C CA . ARG A 50 ? 0.5669 0.4173 0.5188 0.1043 0.0718 0.2318 50 ARG A CA 401 C C . ARG A 50 ? 0.5651 0.3986 0.5466 0.1022 0.0590 0.2208 50 ARG A C 402 O O . ARG A 50 ? 0.5979 0.4120 0.5720 0.1086 0.0507 0.2267 50 ARG A O 403 C CB . ARG A 50 ? 0.6362 0.4769 0.5933 0.0917 0.0925 0.2517 50 ARG A CB 404 C CG . ARG A 50 ? 0.7275 0.5855 0.6538 0.0957 0.1076 0.2631 50 ARG A CG 405 C CD . ARG A 50 ? 0.8247 0.6712 0.7530 0.0863 0.1246 0.2851 50 ARG A CD 406 N NE . ARG A 50 ? 0.8652 0.7095 0.8392 0.0643 0.1348 0.2871 50 ARG A NE 407 C CZ . ARG A 50 ? 0.8674 0.7359 0.8616 0.0519 0.1519 0.2904 50 ARG A CZ 408 N NH1 . ARG A 50 ? 0.8769 0.7719 0.8471 0.0616 0.1631 0.2921 50 ARG A NH1 409 N NH2 . ARG A 50 ? 0.8574 0.7240 0.8951 0.0300 0.1562 0.2902 50 ARG A NH2 410 N N . PHE A 51 ? 0.5632 0.4039 0.5760 0.0945 0.0573 0.2036 51 PHE A N 411 C CA . PHE A 51 ? 0.5782 0.4028 0.6179 0.0915 0.0474 0.1893 51 PHE A CA 412 C C . PHE A 51 ? 0.5121 0.3545 0.5562 0.1023 0.0305 0.1682 51 PHE A C 413 O O . PHE A 51 ? 0.5594 0.3921 0.6143 0.1062 0.0203 0.1571 51 PHE A O 414 C CB . PHE A 51 ? 0.5892 0.4062 0.6627 0.0718 0.0568 0.1828 51 PHE A CB 415 C CG . PHE A 51 ? 0.6873 0.4910 0.7637 0.0569 0.0721 0.2023 51 PHE A CG 416 C CD1 . PHE A 51 ? 0.7433 0.5150 0.8146 0.0546 0.0705 0.2123 51 PHE A CD1 417 C CD2 . PHE A 51 ? 0.7086 0.5336 0.7932 0.0451 0.0880 0.2106 51 PHE A CD2 418 C CE1 . PHE A 51 ? 0.7969 0.5572 0.8718 0.0393 0.0836 0.2303 51 PHE A CE1 419 C CE2 . PHE A 51 ? 0.7598 0.5794 0.8507 0.0303 0.1019 0.2281 51 PHE A CE2 420 C CZ . PHE A 51 ? 0.7976 0.5843 0.8841 0.0266 0.0993 0.2381 51 PHE A CZ 421 N N . ALA A 52 ? 0.4228 0.2919 0.4562 0.1068 0.0278 0.1621 52 ALA A N 422 C CA . ALA A 52 ? 0.3963 0.2863 0.4367 0.1131 0.0121 0.1415 52 ALA A CA 423 C C . ALA A 52 ? 0.4043 0.3159 0.4138 0.1213 0.0020 0.1410 52 ALA A C 424 O O . ALA A 52 ? 0.4123 0.3243 0.3927 0.1217 0.0091 0.1519 52 ALA A O 425 C CB . ALA A 52 ? 0.3685 0.2709 0.4344 0.0998 0.0149 0.1185 52 ALA A CB 426 N N . SER A 53 ? 0.3874 0.3165 0.4025 0.1269 -0.0149 0.1274 53 SER A N 427 C CA . SER A 53 ? 0.3988 0.3471 0.3876 0.1316 -0.0289 0.1237 53 SER A CA 428 C C . SER A 53 ? 0.3872 0.3577 0.3942 0.1263 -0.0381 0.1014 53 SER A C 429 O O . SER A 53 ? 0.3544 0.3268 0.3936 0.1220 -0.0356 0.0903 53 SER A O 430 C CB . SER A 53 ? 0.4547 0.4032 0.4318 0.1388 -0.0444 0.1315 53 SER A CB 431 O OG . SER A 53 ? 0.5313 0.4858 0.5392 0.1398 -0.0533 0.1233 53 SER A OG 432 N N . PHE A 54 ? 0.4030 0.3875 0.3863 0.1251 -0.0491 0.0937 54 PHE A N 433 C CA . PHE A 54 ? 0.3397 0.3440 0.3380 0.1187 -0.0601 0.0743 54 PHE A CA 434 C C . PHE A 54 ? 0.3681 0.3833 0.3431 0.1158 -0.0792 0.0709 54 PHE A C 435 O O . PHE A 54 ? 0.4237 0.4302 0.3588 0.1177 -0.0809 0.0737 54 PHE A O 436 C CB . PHE A 54 ? 0.3070 0.3117 0.3087 0.1074 -0.0476 0.0584 54 PHE A CB 437 C CG . PHE A 54 ? 0.2748 0.2959 0.2888 0.1006 -0.0573 0.0396 54 PHE A CG 438 C CD1 . PHE A 54 ? 0.2562 0.2867 0.3068 0.0980 -0.0575 0.0322 54 PHE A CD1 439 C CD2 . PHE A 54 ? 0.2273 0.2513 0.2137 0.0965 -0.0651 0.0298 54 PHE A CD2 440 C CE1 . PHE A 54 ? 0.1621 0.2062 0.2221 0.0866 -0.0608 0.0179 54 PHE A CE1 441 C CE2 . PHE A 54 ? 0.2024 0.2381 0.1997 0.0889 -0.0739 0.0142 54 PHE A CE2 442 C CZ . PHE A 54 ? 0.1653 0.2117 0.2006 0.0819 -0.0697 0.0091 54 PHE A CZ 443 N N . GLU A 55 ? 0.3326 0.3664 0.3333 0.1090 -0.0912 0.0656 55 GLU A N 444 C CA . GLU A 55 ? 0.3637 0.4097 0.3504 0.1015 -0.1084 0.0634 55 GLU A CA 445 C C . GLU A 55 ? 0.3502 0.3964 0.3218 0.0912 -0.1097 0.0461 55 GLU A C 446 O O . GLU A 55 ? 0.3182 0.3759 0.3144 0.0824 -0.1074 0.0351 55 GLU A O 447 C CB . GLU A 55 ? 0.3375 0.4078 0.3606 0.0973 -0.1167 0.0680 55 GLU A CB 448 C CG . GLU A 55 ? 0.3640 0.4529 0.3787 0.0873 -0.1330 0.0673 55 GLU A CG 449 C CD . GLU A 55 ? 0.4380 0.5144 0.4126 0.0905 -0.1444 0.0743 55 GLU A CD 450 O OE1 . GLU A 55 ? 0.4910 0.5639 0.4646 0.1000 -0.1482 0.0894 55 GLU A OE1 451 O OE2 . GLU A 55 ? 0.4804 0.5473 0.4228 0.0837 -0.1488 0.0643 55 GLU A OE2 452 N N . ALA A 56 ? 0.3115 0.3857 0.2345 0.0146 -0.1086 0.0638 56 ALA A N 453 C CA . ALA A 56 ? 0.3129 0.3874 0.2325 0.0073 -0.0920 0.0561 56 ALA A CA 454 C C . ALA A 56 ? 0.3535 0.4411 0.2647 0.0035 -0.0946 0.0386 56 ALA A C 455 O O . ALA A 56 ? 0.3300 0.4164 0.2470 -0.0001 -0.0843 0.0293 56 ALA A O 456 C CB . ALA A 56 ? 0.2828 0.3451 0.1750 0.0040 -0.0739 0.0657 56 ALA A CB 457 N N . GLN A 57 ? 0.3590 0.4505 0.2645 0.0051 -0.1040 0.0335 57 GLN A N 458 C CA . GLN A 57 ? 0.3837 0.4812 0.2905 -0.0004 -0.1051 0.0210 57 GLN A CA 459 C C . GLN A 57 ? 0.3322 0.4350 0.2669 0.0032 -0.1021 0.0137 57 GLN A C 460 O O . GLN A 57 ? 0.3664 0.4729 0.3013 -0.0040 -0.0974 0.0054 57 GLN A O 461 C CB . GLN A 57 ? 0.4427 0.5480 0.3514 0.0020 -0.1174 0.0240 57 GLN A CB 462 C CG . GLN A 57 ? 0.5123 0.6274 0.4208 -0.0081 -0.1214 0.0175 57 GLN A CG 463 C CD . GLN A 57 ? 0.6123 0.7096 0.4818 -0.0220 -0.1172 0.0110 57 GLN A CD 464 O OE1 . GLN A 57 ? 0.6825 0.7644 0.5171 -0.0248 -0.1180 0.0148 57 GLN A OE1 465 N NE2 . GLN A 57 ? 0.5951 0.6893 0.4651 -0.0301 -0.1112 0.0017 57 GLN A NE2 466 N N . GLY A 58 ? 0.3182 0.4160 0.2711 0.0135 -0.1054 0.0178 58 GLY A N 467 C CA . GLY A 58 ? 0.3074 0.4061 0.2775 0.0162 -0.1014 0.0137 58 GLY A CA 468 C C . GLY A 58 ? 0.3191 0.4142 0.2887 0.0106 -0.0930 0.0064 58 GLY A C 469 O O . GLY A 58 ? 0.3220 0.4205 0.2987 0.0098 -0.0873 -0.0005 58 GLY A O 470 N N . ALA A 59 ? 0.3175 0.4110 0.2798 0.0081 -0.0913 0.0109 59 ALA A N 471 C CA . ALA A 59 ? 0.2840 0.3751 0.2511 0.0029 -0.0798 0.0087 59 ALA A CA 472 C C . ALA A 59 ? 0.2951 0.3903 0.2447 -0.0054 -0.0699 -0.0021 59 ALA A C 473 O O . ALA A 59 ? 0.2806 0.3735 0.2363 -0.0074 -0.0620 -0.0091 59 ALA A O 474 C CB . ALA A 59 ? 0.2561 0.3358 0.2274 0.0012 -0.0705 0.0237 59 ALA A CB 475 N N . LEU A 60 ? 0.3328 0.4293 0.2563 -0.0115 -0.0727 -0.0026 60 LEU A N 476 C CA . LEU A 60 ? 0.3898 0.4788 0.2861 -0.0233 -0.0684 -0.0123 60 LEU A CA 477 C C . LEU A 60 ? 0.3513 0.4467 0.2707 -0.0244 -0.0713 -0.0189 60 LEU A C 478 O O . LEU A 60 ? 0.3669 0.4546 0.2775 -0.0321 -0.0644 -0.0267 60 LEU A O 479 C CB . LEU A 60 ? 0.4802 0.5560 0.3451 -0.0289 -0.0746 -0.0097 60 LEU A CB 480 C CG . LEU A 60 ? 0.5442 0.5934 0.3634 -0.0304 -0.0615 -0.0050 60 LEU A CG 481 C CD1 . LEU A 60 ? 0.5469 0.5999 0.3888 -0.0176 -0.0546 0.0102 60 LEU A CD1 482 C CD2 . LEU A 60 ? 0.5701 0.6009 0.3519 -0.0367 -0.0706 -0.0064 60 LEU A CD2 483 N N . ALA A 61 ? 0.3171 0.4253 0.2617 -0.0164 -0.0796 -0.0136 61 ALA A N 484 C CA . ALA A 61 ? 0.3067 0.4288 0.2716 -0.0158 -0.0802 -0.0145 61 ALA A CA 485 C C . ALA A 61 ? 0.2770 0.3964 0.2515 -0.0121 -0.0707 -0.0200 61 ALA A C 486 O O . ALA A 61 ? 0.3085 0.4339 0.2869 -0.0175 -0.0665 -0.0240 61 ALA A O 487 C CB . ALA A 61 ? 0.2878 0.4263 0.2718 -0.0049 -0.0876 -0.0056 61 ALA A CB 488 N N . ASN A 62 ? 0.2489 0.3585 0.2269 -0.0037 -0.0695 -0.0189 62 ASN A N 489 C CA . ASN A 62 ? 0.2242 0.3271 0.2092 0.0000 -0.0643 -0.0232 62 ASN A CA 490 C C . ASN A 62 ? 0.1983 0.2994 0.1758 -0.0091 -0.0557 -0.0302 62 ASN A C 491 O O . ASN A 62 ? 0.1658 0.2665 0.1476 -0.0099 -0.0504 -0.0351 62 ASN A O 492 C CB . ASN A 62 ? 0.2218 0.3110 0.2115 0.0070 -0.0706 -0.0178 62 ASN A CB 493 C CG . ASN A 62 ? 0.2733 0.3553 0.2631 0.0186 -0.0757 -0.0158 62 ASN A CG 494 O OD1 . ASN A 62 ? 0.3155 0.4113 0.3063 0.0252 -0.0750 -0.0160 62 ASN A OD1 495 N ND2 . ASN A 62 ? 0.2734 0.3336 0.2607 0.0226 -0.0821 -0.0137 62 ASN A ND2 496 N N . ILE A 63 ? 0.1788 0.2761 0.1401 -0.0150 -0.0518 -0.0298 63 ILE A N 497 C CA . ILE A 63 ? 0.2150 0.2935 0.1624 -0.0200 -0.0352 -0.0328 63 ILE A CA 498 C C . ILE A 63 ? 0.2366 0.3129 0.1655 -0.0321 -0.0350 -0.0434 63 ILE A C 499 O O . ILE A 63 ? 0.3242 0.3869 0.2489 -0.0345 -0.0240 -0.0481 63 ILE A O 500 C CB . ILE A 63 ? 0.2610 0.3214 0.1875 -0.0189 -0.0232 -0.0257 63 ILE A CB 501 C CG1 . ILE A 63 ? 0.2536 0.3187 0.2077 -0.0097 -0.0219 -0.0101 63 ILE A CG1 502 C CG2 . ILE A 63 ? 0.2658 0.2988 0.1661 -0.0202 -0.0021 -0.0296 63 ILE A CG2 503 C CD1 . ILE A 63 ? 0.2197 0.2872 0.2051 -0.0057 -0.0193 -0.0045 63 ILE A CD1 504 N N . ALA A 64 ? 0.1933 0.2760 0.1190 -0.0376 -0.0463 -0.0413 64 ALA A N 505 C CA . ALA A 64 ? 0.2479 0.3266 0.1681 -0.0489 -0.0493 -0.0437 64 ALA A CA 506 C C . ALA A 64 ? 0.2576 0.3531 0.2039 -0.0467 -0.0469 -0.0438 64 ALA A C 507 O O . ALA A 64 ? 0.2599 0.3470 0.1991 -0.0565 -0.0430 -0.0480 64 ALA A O 508 C CB . ALA A 64 ? 0.2123 0.3017 0.1339 -0.0539 -0.0641 -0.0373 64 ALA A CB 509 N N . VAL A 65 ? 0.2000 0.3142 0.1706 -0.0334 -0.0488 -0.0392 65 VAL A N 510 C CA . VAL A 65 ? 0.1470 0.2747 0.1341 -0.0279 -0.0448 -0.0399 65 VAL A CA 511 C C . VAL A 65 ? 0.1655 0.2765 0.1469 -0.0273 -0.0359 -0.0471 65 VAL A C 512 O O . VAL A 65 ? 0.1736 0.2873 0.1569 -0.0317 -0.0309 -0.0505 65 VAL A O 513 C CB . VAL A 65 ? 0.1303 0.2707 0.1312 -0.0103 -0.0483 -0.0352 65 VAL A CB 514 C CG1 . VAL A 65 ? 0.1378 0.2863 0.1444 -0.0007 -0.0437 -0.0386 65 VAL A CG1 515 C CG2 . VAL A 65 ? 0.1261 0.2912 0.1384 -0.0088 -0.0553 -0.0262 65 VAL A CG2 516 N N . ASP A 66 ? 0.1933 0.2914 0.1699 -0.0228 -0.0346 -0.0481 66 ASP A N 517 C CA . ASP A 66 ? 0.1782 0.2604 0.1562 -0.0203 -0.0256 -0.0492 66 ASP A CA 518 C C . ASP A 66 ? 0.2073 0.2714 0.1671 -0.0301 -0.0125 -0.0542 66 ASP A C 519 O O . ASP A 66 ? 0.2709 0.3249 0.2338 -0.0287 -0.0042 -0.0547 66 ASP A O 520 C CB . ASP A 66 ? 0.2059 0.2795 0.1919 -0.0136 -0.0249 -0.0402 66 ASP A CB 521 C CG . ASP A 66 ? 0.2322 0.3116 0.2306 -0.0058 -0.0404 -0.0351 66 ASP A CG 522 O OD1 . ASP A 66 ? 0.2585 0.3411 0.2565 -0.0004 -0.0478 -0.0392 66 ASP A OD1 523 O OD2 . ASP A 66 ? 0.2947 0.3712 0.2995 -0.0041 -0.0440 -0.0260 66 ASP A OD2 524 N N . LYS A 67 ? 0.2026 0.2563 0.1371 -0.0400 -0.0118 -0.0577 67 LYS A N 525 C CA . LYS A 67 ? 0.2508 0.2733 0.1532 -0.0505 -0.0015 -0.0642 67 LYS A CA 526 C C . LYS A 67 ? 0.2626 0.2916 0.1719 -0.0612 -0.0067 -0.0662 67 LYS A C 527 O O . LYS A 67 ? 0.2271 0.2337 0.1249 -0.0644 0.0039 -0.0700 67 LYS A O 528 C CB . LYS A 67 ? 0.3074 0.3094 0.1757 -0.0581 -0.0052 -0.0651 67 LYS A CB 529 C CG . LYS A 67 ? 0.3753 0.3357 0.2071 -0.0669 0.0004 -0.0693 67 LYS A CG 530 C CD . LYS A 67 ? 0.4415 0.3794 0.2384 -0.0716 -0.0058 -0.0692 67 LYS A CD 531 C CE . LYS A 67 ? 0.5611 0.4490 0.3142 -0.0794 -0.0002 -0.0738 67 LYS A CE 532 N NZ . LYS A 67 ? 0.6499 0.5049 0.3877 -0.0654 0.0259 -0.0751 67 LYS A NZ 533 N N . ALA A 68 ? 0.2454 0.3045 0.1751 -0.0650 -0.0206 -0.0606 68 ALA A N 534 C CA . ALA A 68 ? 0.2454 0.3207 0.1879 -0.0753 -0.0242 -0.0583 68 ALA A CA 535 C C . ALA A 68 ? 0.2505 0.3366 0.2086 -0.0668 -0.0160 -0.0609 68 ALA A C 536 O O . ALA A 68 ? 0.2484 0.3289 0.2053 -0.0753 -0.0109 -0.0616 68 ALA A O 537 C CB . ALA A 68 ? 0.2114 0.3230 0.1763 -0.0778 -0.0374 -0.0483 68 ALA A CB 538 N N . ASN A 69 ? 0.2254 0.3200 0.1967 -0.0485 -0.0156 -0.0594 69 ASN A N 539 C CA . ASN A 69 ? 0.2077 0.2993 0.1884 -0.0356 -0.0099 -0.0577 69 ASN A CA 540 C C . ASN A 69 ? 0.1815 0.2441 0.1534 -0.0356 0.0009 -0.0593 69 ASN A C 541 O O . ASN A 69 ? 0.1994 0.2572 0.1733 -0.0335 0.0061 -0.0579 69 ASN A O 542 C CB . ASN A 69 ? 0.2067 0.3023 0.1949 -0.0187 -0.0172 -0.0549 69 ASN A CB 543 C CG . ASN A 69 ? 0.2261 0.3467 0.2222 -0.0106 -0.0226 -0.0513 69 ASN A CG 544 O OD1 . ASN A 69 ? 0.2620 0.4062 0.2671 -0.0171 -0.0203 -0.0475 69 ASN A OD1 545 N ND2 . ASN A 69 ? 0.1994 0.3142 0.1930 0.0039 -0.0300 -0.0500 69 ASN A ND2 546 N N . LEU A 70 ? 0.1700 0.2134 0.1319 -0.0357 0.0064 -0.0597 70 LEU A N 547 C CA . LEU A 70 ? 0.2293 0.2462 0.1851 -0.0317 0.0207 -0.0574 70 LEU A CA 548 C C . LEU A 70 ? 0.3001 0.2956 0.2361 -0.0430 0.0293 -0.0627 70 LEU A C 549 O O . LEU A 70 ? 0.3314 0.3134 0.2699 -0.0380 0.0381 -0.0594 70 LEU A O 550 C CB . LEU A 70 ? 0.2297 0.2301 0.1757 -0.0263 0.0305 -0.0540 70 LEU A CB 551 C CG . LEU A 70 ? 0.2650 0.2388 0.2065 -0.0167 0.0509 -0.0472 70 LEU A CG 552 C CD1 . LEU A 70 ? 0.2141 0.2020 0.1897 -0.0067 0.0479 -0.0350 70 LEU A CD1 553 C CD2 . LEU A 70 ? 0.3037 0.2634 0.2344 -0.0073 0.0657 -0.0405 70 LEU A CD2 554 N N . GLU A 71 ? 0.2851 0.2759 0.2010 -0.0599 0.0239 -0.0691 71 GLU A N 555 C CA . GLU A 71 ? 0.2798 0.2469 0.1742 -0.0768 0.0263 -0.0731 71 GLU A CA 556 C C . GLU A 71 ? 0.2646 0.2520 0.1819 -0.0778 0.0258 -0.0680 71 GLU A C 557 O O . GLU A 71 ? 0.2964 0.2594 0.2042 -0.0795 0.0355 -0.0675 71 GLU A O 558 C CB . GLU A 71 ? 0.3465 0.3149 0.2262 -0.0966 0.0114 -0.0741 71 GLU A CB 559 C CG . GLU A 71 ? 0.5415 0.5005 0.4136 -0.1184 0.0054 -0.0720 71 GLU A CG 560 C CD . GLU A 71 ? 0.6799 0.6454 0.5466 -0.1358 -0.0135 -0.0663 71 GLU A CD 561 O OE1 . GLU A 71 ? 0.7261 0.6986 0.5992 -0.1554 -0.0233 -0.0595 71 GLU A OE1 562 O OE2 . GLU A 71 ? 0.7155 0.6795 0.5730 -0.1304 -0.0192 -0.0667 71 GLU A OE2 563 N N . ILE A 72 ? 0.2504 0.2795 0.1943 -0.0743 0.0166 -0.0630 72 ILE A N 564 C CA . ILE A 72 ? 0.2364 0.2861 0.1981 -0.0709 0.0191 -0.0561 72 ILE A CA 565 C C . ILE A 72 ? 0.2609 0.2934 0.2216 -0.0542 0.0276 -0.0548 72 ILE A C 566 O O . ILE A 72 ? 0.3049 0.3272 0.2627 -0.0562 0.0350 -0.0513 72 ILE A O 567 C CB . ILE A 72 ? 0.2292 0.3207 0.2132 -0.0623 0.0122 -0.0499 72 ILE A CB 568 C CG1 . ILE A 72 ? 0.2790 0.3969 0.2740 -0.0817 0.0025 -0.0443 72 ILE A CG1 569 C CG2 . ILE A 72 ? 0.1901 0.2931 0.1824 -0.0488 0.0202 -0.0427 72 ILE A CG2 570 C CD1 . ILE A 72 ? 0.2830 0.4438 0.3026 -0.0704 -0.0027 -0.0353 72 ILE A CD1 571 N N A MET A 73 ? 0.2081 0.2382 0.1727 -0.0394 0.0243 -0.0550 73 MET A N 572 N N B MET A 73 ? 0.2103 0.2398 0.1746 -0.0396 0.0245 -0.0550 73 MET A N 573 C CA A MET A 73 ? 0.1993 0.2165 0.1670 -0.0260 0.0256 -0.0499 73 MET A CA 574 C CA B MET A 73 ? 0.1961 0.2134 0.1636 -0.0262 0.0257 -0.0499 73 MET A CA 575 C C A MET A 73 ? 0.2041 0.1935 0.1650 -0.0273 0.0378 -0.0474 73 MET A C 576 C C B MET A 73 ? 0.2084 0.1977 0.1695 -0.0270 0.0378 -0.0473 73 MET A C 577 O O A MET A 73 ? 0.2290 0.2086 0.1907 -0.0217 0.0407 -0.0414 73 MET A O 578 O O B MET A 73 ? 0.2248 0.2042 0.1872 -0.0210 0.0405 -0.0410 73 MET A O 579 C CB A MET A 73 ? 0.2190 0.2404 0.1965 -0.0153 0.0151 -0.0468 73 MET A CB 580 C CB B MET A 73 ? 0.2092 0.2315 0.1862 -0.0149 0.0145 -0.0469 73 MET A CB 581 C CG A MET A 73 ? 0.1987 0.2366 0.1763 -0.0093 0.0031 -0.0486 73 MET A CG 582 C CG B MET A 73 ? 0.2156 0.2260 0.1974 -0.0054 0.0082 -0.0382 73 MET A CG 583 S SD A MET A 73 ? 0.2920 0.3287 0.2561 -0.0001 0.0035 -0.0470 73 MET A SD 584 S SD B MET A 73 ? 0.1985 0.2036 0.1626 0.0004 0.0046 -0.0380 73 MET A SD 585 C CE A MET A 73 ? 0.2476 0.2567 0.2057 0.0055 -0.0037 -0.0403 73 MET A CE 586 C CE B MET A 73 ? 0.2861 0.3068 0.2424 0.0062 -0.0023 -0.0440 73 MET A CE 587 N N . THR A 74 ? 0.1927 0.1648 0.1419 -0.0325 0.0458 -0.0512 74 THR A N 588 C CA . THR A 74 ? 0.2805 0.2174 0.2154 -0.0299 0.0620 -0.0490 74 THR A CA 589 C C . THR A 74 ? 0.3600 0.2809 0.2817 -0.0404 0.0664 -0.0505 74 THR A C 590 O O . THR A 74 ? 0.3931 0.2954 0.3142 -0.0329 0.0757 -0.0438 74 THR A O 591 C CB . THR A 74 ? 0.2886 0.1983 0.1967 -0.0331 0.0717 -0.0552 74 THR A CB 592 O OG1 . THR A 74 ? 0.2705 0.1964 0.1934 -0.0220 0.0704 -0.0503 74 THR A OG1 593 C CG2 . THR A 74 ? 0.3081 0.1717 0.1925 -0.0257 0.0927 -0.0528 74 THR A CG2 594 N N . LYS A 75 ? 0.3564 0.2875 0.2713 -0.0586 0.0588 -0.0563 75 LYS A N 595 C CA . LYS A 75 ? 0.4018 0.3252 0.3103 -0.0730 0.0607 -0.0542 75 LYS A CA 596 C C . LYS A 75 ? 0.3457 0.2879 0.2717 -0.0621 0.0619 -0.0453 75 LYS A C 597 O O . LYS A 75 ? 0.3905 0.3121 0.3089 -0.0632 0.0701 -0.0403 75 LYS A O 598 C CB . LYS A 75 ? 0.4572 0.4014 0.3677 -0.0955 0.0488 -0.0557 75 LYS A CB 599 C CG . LYS A 75 ? 0.5442 0.4690 0.4420 -0.1199 0.0481 -0.0528 75 LYS A CG 600 C CD . LYS A 75 ? 0.5766 0.5282 0.4836 -0.1445 0.0312 -0.0498 75 LYS A CD 601 C CE . LYS A 75 ? 0.6194 0.5577 0.5055 -0.1475 0.0218 -0.0601 75 LYS A CE 602 N NZ . LYS A 75 ? 0.6437 0.6077 0.5387 -0.1716 0.0010 -0.0540 75 LYS A NZ 603 N N . ARG A 76 ? 0.2771 0.2518 0.2195 -0.0511 0.0538 -0.0432 76 ARG A N 604 C CA . ARG A 76 ? 0.2949 0.2789 0.2408 -0.0386 0.0535 -0.0361 76 ARG A CA 605 C C . ARG A 76 ? 0.2993 0.2587 0.2408 -0.0266 0.0554 -0.0304 76 ARG A C 606 O O . ARG A 76 ? 0.3102 0.2620 0.2443 -0.0222 0.0582 -0.0236 76 ARG A O 607 C CB . ARG A 76 ? 0.3025 0.3106 0.2544 -0.0265 0.0436 -0.0370 76 ARG A CB 608 C CG . ARG A 76 ? 0.3422 0.3574 0.2853 -0.0155 0.0464 -0.0308 76 ARG A CG 609 C CD . ARG A 76 ? 0.3544 0.3757 0.2897 0.0008 0.0371 -0.0329 76 ARG A CD 610 N NE . ARG A 76 ? 0.3287 0.3807 0.2781 -0.0012 0.0387 -0.0335 76 ARG A NE 611 C CZ . ARG A 76 ? 0.3338 0.3920 0.2801 0.0108 0.0311 -0.0364 76 ARG A CZ 612 N NH1 . ARG A 76 ? 0.3366 0.4260 0.3001 0.0094 0.0333 -0.0338 76 ARG A NH1 613 N NH2 . ARG A 76 ? 0.2986 0.3300 0.2244 0.0231 0.0193 -0.0398 76 ARG A NH2 614 N N . SER A 77 ? 0.2209 0.1928 0.2472 -0.0673 -0.0201 -0.0162 77 SER A N 615 C CA . SER A 77 ? 0.2103 0.1721 0.2249 -0.0682 -0.0184 -0.0038 77 SER A CA 616 C C . SER A 77 ? 0.2415 0.1847 0.2501 -0.0711 -0.0142 0.0010 77 SER A C 617 O O . SER A 77 ? 0.2224 0.1556 0.2236 -0.0689 -0.0127 0.0118 77 SER A O 618 C CB . SER A 77 ? 0.2240 0.1840 0.2331 -0.0616 -0.0245 0.0010 77 SER A CB 619 O OG . SER A 77 ? 0.2256 0.1731 0.2300 -0.0595 -0.0274 -0.0011 77 SER A OG 620 N N . ASN A 78 ? 0.2479 0.1877 0.2625 -0.0743 -0.0125 -0.0073 78 ASN A N 621 C CA . ASN A 78 ? 0.2819 0.2042 0.2950 -0.0761 -0.0088 -0.0054 78 ASN A CA 622 C C . ASN A 78 ? 0.3328 0.2415 0.3385 -0.0704 -0.0112 -0.0035 78 ASN A C 623 O O . ASN A 78 ? 0.3633 0.2575 0.3664 -0.0683 -0.0079 0.0039 78 ASN A O 624 C CB . ASN A 78 ? 0.3361 0.2527 0.3478 -0.0796 -0.0031 0.0057 78 ASN A CB 625 C CG . ASN A 78 ? 0.4060 0.3360 0.4228 -0.0861 -0.0008 0.0039 78 ASN A CG 626 O OD1 . ASN A 78 ? 0.3319 0.2680 0.3565 -0.0890 -0.0018 -0.0058 78 ASN A OD1 627 N ND2 . ASN A 78 ? 0.5782 0.5134 0.5902 -0.0876 0.0016 0.0133 78 ASN A ND2 628 N N . TYR A 79 ? 0.3129 0.2279 0.3167 -0.0669 -0.0173 -0.0101 79 TYR A N 629 C CA . TYR A 79 ? 0.2595 0.1660 0.2564 -0.0602 -0.0203 -0.0102 79 TYR A CA 630 C C . TYR A 79 ? 0.2805 0.1815 0.2713 -0.0527 -0.0189 0.0025 79 TYR A C 631 O O . TYR A 79 ? 0.2830 0.1725 0.2712 -0.0477 -0.0167 0.0039 79 TYR A O 632 C CB . TYR A 79 ? 0.2467 0.1409 0.2455 -0.0620 -0.0174 -0.0190 79 TYR A CB 633 C CG . TYR A 79 ? 0.2197 0.1242 0.2256 -0.0662 -0.0194 -0.0327 79 TYR A CG 634 C CD1 . TYR A 79 ? 0.2264 0.1366 0.2429 -0.0708 -0.0171 -0.0348 79 TYR A CD1 635 C CD2 . TYR A 79 ? 0.1982 0.1098 0.2011 -0.0635 -0.0250 -0.0417 79 TYR A CD2 636 C CE1 . TYR A 79 ? 0.2412 0.1603 0.2626 -0.0718 -0.0218 -0.0439 79 TYR A CE1 637 C CE2 . TYR A 79 ? 0.2170 0.1405 0.2280 -0.0643 -0.0287 -0.0517 79 TYR A CE2 638 C CZ . TYR A 79 ? 0.2445 0.1689 0.2613 -0.0685 -0.0278 -0.0511 79 TYR A CZ 639 O OH . TYR A 79 ? 0.2664 0.1981 0.2830 -0.0701 -0.0314 -0.0573 79 TYR A OH 640 N N . THR A 80 ? 0.2828 0.1931 0.2727 -0.0521 -0.0200 0.0107 80 THR A N 641 C CA . THR A 80 ? 0.2829 0.1910 0.2677 -0.0449 -0.0196 0.0223 80 THR A CA 642 C C . THR A 80 ? 0.2960 0.2113 0.2773 -0.0364 -0.0242 0.0206 80 THR A C 643 O O . THR A 80 ? 0.3068 0.2356 0.2904 -0.0363 -0.0290 0.0175 80 THR A O 644 C CB . THR A 80 ? 0.2215 0.1396 0.2070 -0.0479 -0.0191 0.0303 80 THR A CB 645 O OG1 . THR A 80 ? 0.1766 0.0941 0.1650 -0.0540 -0.0136 0.0310 80 THR A OG1 646 C CG2 . THR A 80 ? 0.1721 0.0935 0.1540 -0.0381 -0.0177 0.0396 80 THR A CG2 647 N N . PRO A 81 ? 0.2713 0.1777 0.2481 -0.0297 -0.0228 0.0228 81 PRO A N 648 C CA . PRO A 81 ? 0.2669 0.1804 0.2391 -0.0227 -0.0265 0.0213 81 PRO A CA 649 C C . PRO A 81 ? 0.2335 0.1540 0.2035 -0.0170 -0.0280 0.0314 81 PRO A C 650 O O . PRO A 81 ? 0.2524 0.1718 0.2240 -0.0174 -0.0256 0.0394 81 PRO A O 651 C CB . PRO A 81 ? 0.2823 0.1839 0.2519 -0.0189 -0.0229 0.0179 81 PRO A CB 652 C CG . PRO A 81 ? 0.2500 0.1376 0.2237 -0.0203 -0.0178 0.0244 81 PRO A CG 653 C CD . PRO A 81 ? 0.2264 0.1162 0.2039 -0.0288 -0.0176 0.0258 81 PRO A CD 654 N N . ILE A 82 ? 0.2031 0.1322 0.1699 -0.0120 -0.0318 0.0309 82 ILE A N 655 C CA . ILE A 82 ? 0.2540 0.1926 0.2211 -0.0062 -0.0318 0.0380 82 ILE A CA 656 C C . ILE A 82 ? 0.2810 0.2171 0.2479 0.0001 -0.0243 0.0407 82 ILE A C 657 O O . ILE A 82 ? 0.2643 0.1850 0.2260 0.0012 -0.0243 0.0405 82 ILE A O 658 C CB . ILE A 82 ? 0.1659 0.1165 0.1320 -0.0033 -0.0363 0.0358 82 ILE A CB 659 C CG1 . ILE A 82 ? 0.1436 0.1108 0.1180 0.0009 -0.0303 0.0354 82 ILE A CG1 660 C CG2 . ILE A 82 ? 0.1739 0.1177 0.1295 0.0004 -0.0375 0.0354 82 ILE A CG2 661 C CD1 . ILE A 82 ? 0.1149 0.0926 0.0921 0.0020 -0.0328 0.0328 82 ILE A CD1 662 N N . THR A 83 ? 0.2741 0.2218 0.2454 0.0043 -0.0183 0.0420 83 THR A N 663 C CA . THR A 83 ? 0.2765 0.2225 0.2461 0.0111 -0.0120 0.0441 83 THR A CA 664 C C . THR A 83 ? 0.2704 0.2256 0.2384 0.0160 -0.0114 0.0420 83 THR A C 665 O O . THR A 83 ? 0.2535 0.2164 0.2216 0.0153 -0.0139 0.0396 83 THR A O 666 C CB . THR A 83 ? 0.2715 0.2185 0.2395 0.0114 -0.0095 0.0442 83 THR A CB 667 O OG1 . THR A 83 ? 0.3111 0.2517 0.2806 0.0069 -0.0082 0.0464 83 THR A OG1 668 C CG2 . THR A 83 ? 0.2756 0.2177 0.2397 0.0148 -0.0092 0.0443 83 THR A CG2 669 N N . ASN A 84 ? 0.3033 0.2565 0.2732 0.0183 -0.0109 0.0447 84 ASN A N 670 C CA . ASN A 84 ? 0.2842 0.2503 0.2574 0.0198 -0.0108 0.0448 84 ASN A CA 671 C C . ASN A 84 ? 0.2869 0.2379 0.2446 0.0179 -0.0177 0.0361 84 ASN A C 672 O O . ASN A 84 ? 0.2758 0.2250 0.2381 0.0168 -0.0180 0.0388 84 ASN A O 673 C CB . ASN A 84 ? 0.3065 0.2578 0.2742 0.0199 -0.0168 0.0475 84 ASN A CB 674 C CG . ASN A 84 ? 0.3374 0.2677 0.2853 0.0219 -0.0199 0.0426 84 ASN A CG 675 O OD1 . ASN A 84 ? 0.3791 0.3140 0.3208 0.0186 -0.0251 0.0405 84 ASN A OD1 676 N ND2 . ASN A 84 ? 0.3451 0.2616 0.2933 0.0237 -0.0160 0.0372 84 ASN A ND2 677 N N . VAL A 85 ? 0.2439 0.2043 0.2042 0.0180 -0.0183 0.0358 85 VAL A N 678 C CA . VAL A 85 ? 0.2725 0.2403 0.2395 0.0174 -0.0181 0.0381 85 VAL A CA 679 C C . VAL A 85 ? 0.2414 0.2127 0.2079 0.0178 -0.0192 0.0391 85 VAL A C 680 O O . VAL A 85 ? 0.2667 0.2412 0.2311 0.0175 -0.0204 0.0381 85 VAL A O 681 C CB . VAL A 85 ? 0.3042 0.2825 0.2789 0.0158 -0.0169 0.0377 85 VAL A CB 682 C CG1 . VAL A 85 ? 0.0894 0.0773 0.0725 0.0152 -0.0149 0.0389 85 VAL A CG1 683 C CG2 . VAL A 85 ? 0.0946 0.0727 0.0718 0.0140 -0.0161 0.0379 85 VAL A CG2 684 N N . PRO A 86 ? 0.2173 0.1897 0.1863 0.0196 -0.0172 0.0413 86 PRO A N 685 C CA . PRO A 86 ? 0.1841 0.1611 0.1512 0.0211 -0.0163 0.0423 86 PRO A CA 686 C C . PRO A 86 ? 0.1954 0.1820 0.1669 0.0211 -0.0143 0.0423 86 PRO A C 687 O O . PRO A 86 ? 0.1832 0.1746 0.1618 0.0207 -0.0124 0.0421 86 PRO A O 688 C CB . PRO A 86 ? 0.1925 0.1674 0.1616 0.0250 -0.0132 0.0438 86 PRO A CB 689 C CG . PRO A 86 ? 0.1604 0.1339 0.1348 0.0252 -0.0121 0.0441 86 PRO A CG 690 C CD . PRO A 86 ? 0.1874 0.1570 0.1600 0.0216 -0.0151 0.0428 86 PRO A CD 691 N N . PRO A 87 ? 0.2201 0.2104 0.1881 0.0210 -0.0149 0.0431 87 PRO A N 692 C CA . PRO A 87 ? 0.2050 0.2044 0.1787 0.0205 -0.0135 0.0443 87 PRO A CA 693 C C . PRO A 87 ? 0.2042 0.2103 0.1835 0.0228 -0.0091 0.0457 87 PRO A C 694 O O . PRO A 87 ? 0.2468 0.2509 0.2235 0.0258 -0.0070 0.0460 87 PRO A O 695 C CB . PRO A 87 ? 0.2109 0.2109 0.1768 0.0195 -0.0161 0.0455 87 PRO A CB 696 C CG . PRO A 87 ? 0.2312 0.2257 0.1874 0.0204 -0.0166 0.0452 87 PRO A CG 697 C CD . PRO A 87 ? 0.2029 0.1900 0.1610 0.0207 -0.0171 0.0437 87 PRO A CD 698 N N . GLU A 88 ? 0.3221 0.2171 0.2133 0.0343 0.0658 0.0165 88 GLU A N 699 C CA . GLU A 88 ? 0.3277 0.2256 0.2173 0.0296 0.0656 0.0090 88 GLU A CA 700 C C . GLU A 88 ? 0.2760 0.1750 0.1779 0.0310 0.0697 0.0113 88 GLU A C 701 O O . GLU A 88 ? 0.2980 0.1887 0.2065 0.0344 0.0766 0.0178 88 GLU A O 702 C CB . GLU A 88 ? 0.3956 0.2855 0.2772 0.0243 0.0734 0.0045 88 GLU A CB 703 C CG . GLU A 88 ? 0.5189 0.4057 0.3834 0.0218 0.0705 0.0024 88 GLU A CG 704 C CD . GLU A 88 ? 0.5967 0.4746 0.4503 0.0164 0.0788 -0.0032 88 GLU A CD 705 O OE1 . GLU A 88 ? 0.6406 0.5139 0.5019 0.0145 0.0873 -0.0053 88 GLU A OE1 706 O OE2 . GLU A 88 ? 0.5998 0.4739 0.4352 0.0134 0.0767 -0.0056 88 GLU A OE2 707 N N . VAL A 89 ? 0.2412 0.1515 0.1465 0.0294 0.0657 0.0052 89 VAL A N 708 C CA . VAL A 89 ? 0.2393 0.1514 0.1533 0.0300 0.0694 0.0072 89 VAL A CA 709 C C . VAL A 89 ? 0.3013 0.2191 0.2197 0.0245 0.0742 -0.0018 89 VAL A C 710 O O . VAL A 89 ? 0.3447 0.2747 0.2632 0.0229 0.0696 -0.0125 89 VAL A O 711 C CB . VAL A 89 ? 0.2020 0.1239 0.1171 0.0339 0.0616 0.0072 89 VAL A CB 712 C CG1 . VAL A 89 ? 0.2267 0.1496 0.1472 0.0343 0.0664 0.0091 89 VAL A CG1 713 C CG2 . VAL A 89 ? 0.1804 0.0974 0.0921 0.0393 0.0565 0.0148 89 VAL A CG2 714 N N . THR A 90 ? 0.2832 0.1914 0.2062 0.0229 0.0835 0.0018 90 THR A N 715 C CA . THR A 90 ? 0.2869 0.1985 0.2153 0.0174 0.0895 -0.0060 90 THR A CA 716 C C . THR A 90 ? 0.2893 0.1983 0.2234 0.0183 0.0948 -0.0020 90 THR A C 717 O O . THR A 90 ? 0.3043 0.2007 0.2376 0.0227 0.0980 0.0077 90 THR A O 718 C CB . THR A 90 ? 0.3074 0.2049 0.2329 0.0123 0.0983 -0.0077 90 THR A CB 719 O OG1 . THR A 90 ? 0.3489 0.2441 0.2648 0.0127 0.0946 -0.0085 90 THR A OG1 720 C CG2 . THR A 90 ? 0.2941 0.1989 0.2248 0.0060 0.1021 -0.0190 90 THR A CG2 721 N N . VAL A 91 ? 0.2526 0.1742 0.1928 0.0156 0.0960 -0.0101 91 VAL A N 722 C CA . VAL A 91 ? 0.2568 0.1756 0.2005 0.0157 0.1028 -0.0071 91 VAL A CA 723 C C . VAL A 91 ? 0.2850 0.1988 0.2352 0.0090 0.1130 -0.0126 91 VAL A C 724 O O . VAL A 91 ? 0.3162 0.2416 0.2721 0.0049 0.1124 -0.0232 91 VAL A O 725 C CB . VAL A 91 ? 0.2422 0.1792 0.1872 0.0187 0.0978 -0.0116 91 VAL A CB 726 C CG1 . VAL A 91 ? 0.2477 0.1829 0.1944 0.0178 0.1067 -0.0099 91 VAL A CG1 727 C CG2 . VAL A 91 ? 0.1962 0.1344 0.1340 0.0246 0.0890 -0.0059 91 VAL A CG2 728 N N . LEU A 92 ? 0.2960 0.1921 0.2461 0.0090 0.1223 -0.0058 92 LEU A N 729 C CA . LEU A 92 ? 0.3229 0.2102 0.2792 0.0025 0.1336 -0.0102 92 LEU A CA 730 C C . LEU A 92 ? 0.3108 0.1867 0.2672 0.0057 0.1421 -0.0029 92 LEU A C 731 O O . LEU A 92 ? 0.3210 0.1946 0.2721 0.0135 0.1392 0.0061 92 LEU A O 732 C CB . LEU A 92 ? 0.3635 0.2341 0.3182 -0.0017 0.1386 -0.0113 92 LEU A CB 733 C CG . LEU A 92 ? 0.4433 0.2924 0.3928 0.0046 0.1421 -0.0006 92 LEU A CG 734 C CD1 . LEU A 92 ? 0.5022 0.3321 0.4518 -0.0011 0.1529 -0.0035 92 LEU A CD1 735 C CD2 . LEU A 92 ? 0.4204 0.2749 0.3637 0.0103 0.1319 0.0041 92 LEU A CD2 736 N N . THR A 93 ? 0.3020 0.1720 0.2647 0.0000 0.1529 -0.0072 93 THR A N 737 C CA . THR A 93 ? 0.3499 0.2076 0.3123 0.0035 0.1628 -0.0003 93 THR A CA 738 C C . THR A 93 ? 0.3985 0.2304 0.3622 0.0043 0.1718 0.0028 93 THR A C 739 O O . THR A 93 ? 0.4062 0.2314 0.3717 -0.0021 0.1731 -0.0036 93 THR A O 740 C CB . THR A 93 ? 0.3291 0.1964 0.2979 -0.0026 0.1710 -0.0061 93 THR A CB 741 O OG1 . THR A 93 ? 0.3631 0.2277 0.3415 -0.0121 0.1767 -0.0165 93 THR A OG1 742 C CG2 . THR A 93 ? 0.3229 0.2159 0.2912 -0.0022 0.1638 -0.0100 93 THR A CG2 743 N N . ASN A 94 ? 0.4309 0.2500 0.3939 0.0126 0.1788 0.0120 94 ASN A N 744 C CA . ASN A 94 ? 0.4568 0.2516 0.4232 0.0161 0.1889 0.0148 94 ASN A CA 745 C C . ASN A 94 ? 0.4196 0.2032 0.3924 0.0088 0.2023 0.0082 94 ASN A C 746 O O . ASN A 94 ? 0.4178 0.1963 0.3943 0.0087 0.2067 0.0079 94 ASN A O 747 C CB . ASN A 94 ? 0.5624 0.3601 0.5295 0.0297 0.1881 0.0270 94 ASN A CB 748 C CG . ASN A 94 ? 0.6544 0.4506 0.6219 0.0345 0.1975 0.0331 94 ASN A CG 749 O OD1 . ASN A 94 ? 0.6963 0.5036 0.6611 0.0266 0.1979 0.0292 94 ASN A OD1 750 N ND2 . ASN A 94 ? 0.6854 0.4775 0.6574 0.0461 0.2038 0.0433 94 ASN A ND2 751 N N . SER A 95 ? 0.4184 0.2140 0.3940 0.0015 0.2048 0.0028 95 SER A N 752 C CA . SER A 95 ? 0.4783 0.2658 0.4619 -0.0071 0.2176 -0.0050 95 SER A CA 753 C C . SER A 95 ? 0.4392 0.2496 0.4286 -0.0177 0.2146 -0.0148 95 SER A C 754 O O . SER A 95 ? 0.3853 0.2166 0.3715 -0.0161 0.2045 -0.0136 95 SER A O 755 C CB . SER A 95 ? 0.5346 0.3141 0.5199 -0.0007 0.2299 0.0037 95 SER A CB 756 O OG . SER A 95 ? 0.5878 0.3866 0.5683 0.0016 0.2262 0.0111 95 SER A OG 757 N N . PRO A 96 ? 0.4590 0.2665 0.4587 -0.0281 0.2239 -0.0252 96 PRO A N 758 C CA . PRO A 96 ? 0.4294 0.2617 0.4396 -0.0369 0.2228 -0.0345 96 PRO A CA 759 C C . PRO A 96 ? 0.4235 0.2728 0.4327 -0.0334 0.2242 -0.0272 96 PRO A C 760 O O . PRO A 96 ? 0.4250 0.2648 0.4293 -0.0290 0.2326 -0.0171 96 PRO A O 761 C CB . PRO A 96 ? 0.3871 0.2093 0.4097 -0.0471 0.2366 -0.0440 96 PRO A CB 762 C CG . PRO A 96 ? 0.4592 0.2485 0.4758 -0.0420 0.2475 -0.0388 96 PRO A CG 763 C CD . PRO A 96 ? 0.4284 0.2115 0.4321 -0.0321 0.2359 -0.0305 96 PRO A CD 764 N N . VAL A 97 ? 0.4149 0.2902 0.4283 -0.0350 0.2168 -0.0324 97 VAL A N 765 C CA . VAL A 97 ? 0.4175 0.3102 0.4273 -0.0314 0.2178 -0.0267 97 VAL A CA 766 C C . VAL A 97 ? 0.4265 0.3299 0.4492 -0.0391 0.2318 -0.0295 97 VAL A C 767 O O . VAL A 97 ? 0.4238 0.3383 0.4643 -0.0472 0.2347 -0.0407 97 VAL A O 768 C CB . VAL A 97 ? 0.3915 0.3072 0.4000 -0.0276 0.2047 -0.0312 97 VAL A CB 769 C CG1 . VAL A 97 ? 0.3849 0.3177 0.3883 -0.0241 0.2078 -0.0270 97 VAL A CG1 770 C CG2 . VAL A 97 ? 0.3775 0.2843 0.3734 -0.0205 0.1916 -0.0264 97 VAL A CG2 771 N N . GLU A 98 ? 0.4209 0.3223 0.4352 -0.0370 0.2406 -0.0186 98 GLU A N 772 C CA . GLU A 98 ? 0.4977 0.4122 0.5216 -0.0441 0.2546 -0.0183 98 GLU A CA 773 C C . GLU A 98 ? 0.5108 0.4410 0.5205 -0.0390 0.2550 -0.0110 98 GLU A C 774 O O . GLU A 98 ? 0.4896 0.4111 0.4802 -0.0315 0.2496 -0.0012 98 GLU A O 775 C CB . GLU A 98 ? 0.6097 0.5043 0.6353 -0.0487 0.2684 -0.0108 98 GLU A CB 776 C CG . GLU A 98 ? 0.7012 0.5786 0.7393 -0.0539 0.2699 -0.0195 98 GLU A CG 777 C CD . GLU A 98 ? 0.8313 0.6867 0.8706 -0.0567 0.2835 -0.0119 98 GLU A CD 778 O OE1 . GLU A 98 ? 0.8772 0.7308 0.9335 -0.0671 0.2928 -0.0189 98 GLU A OE1 779 O OE2 . GLU A 98 ? 0.8716 0.7130 0.8963 -0.0486 0.2847 0.0012 98 GLU A OE2 780 N N . LEU A 99 ? 0.5035 0.4575 0.5234 -0.0431 0.2621 -0.0163 99 LEU A N 781 C CA . LEU A 99 ? 0.5386 0.5092 0.5448 -0.0389 0.2648 -0.0120 99 LEU A CA 782 C C . LEU A 99 ? 0.5839 0.5417 0.5689 -0.0383 0.2724 0.0037 99 LEU A C 783 O O . LEU A 99 ? 0.6005 0.5462 0.5899 -0.0445 0.2834 0.0104 99 LEU A O 784 C CB . LEU A 99 ? 0.5640 0.5608 0.5885 -0.0441 0.2760 -0.0200 99 LEU A CB 785 C CG . LEU A 99 ? 0.5533 0.5699 0.5983 -0.0423 0.2678 -0.0350 99 LEU A CG 786 C CD1 . LEU A 99 ? 0.5501 0.5935 0.6164 -0.0465 0.2815 -0.0415 99 LEU A CD1 787 C CD2 . LEU A 99 ? 0.5555 0.5762 0.5847 -0.0312 0.2528 -0.0370 99 LEU A CD2 788 N N . ARG A 100 ? 0.6051 0.5653 0.5673 -0.0311 0.2660 0.0099 100 ARG A N 789 C CA . ARG A 100 ? 0.6464 0.5961 0.5863 -0.0304 0.2711 0.0259 100 ARG A CA 790 C C . ARG A 100 ? 0.6150 0.5392 0.5549 -0.0306 0.2723 0.0368 100 ARG A C 791 O O . ARG A 100 ? 0.6506 0.5676 0.5799 -0.0337 0.2817 0.0504 100 ARG A O 792 C CB . ARG A 100 ? 0.7449 0.7104 0.6775 -0.0366 0.2873 0.0299 100 ARG A CB 793 C CG . ARG A 100 ? 0.8237 0.7905 0.7747 -0.0468 0.3037 0.0306 100 ARG A CG 794 C CD . ARG A 100 ? 0.8852 0.8750 0.8303 -0.0507 0.3176 0.0305 100 ARG A CD 795 N NE . ARG A 100 ? 0.8961 0.9083 0.8545 -0.0467 0.3144 0.0143 100 ARG A NE 796 C CZ . ARG A 100 ? 0.8963 0.9233 0.8847 -0.0506 0.3195 0.0025 100 ARG A CZ 797 N NH1 . ARG A 100 ? 0.8999 0.9216 0.9097 -0.0602 0.3284 0.0036 100 ARG A NH1 798 N NH2 . ARG A 100 ? 0.8745 0.9219 0.8726 -0.0446 0.3149 -0.0108 100 ARG A NH2 799 N N . GLU A 101 ? 0.5838 0.4949 0.5360 -0.0274 0.2635 0.0305 101 GLU A N 800 C CA . GLU A 101 ? 0.5682 0.4552 0.5199 -0.0237 0.2629 0.0390 101 GLU A CA 801 C C . GLU A 101 ? 0.5407 0.4226 0.4835 -0.0132 0.2471 0.0404 101 GLU A C 802 O O . GLU A 101 ? 0.4725 0.3577 0.4221 -0.0111 0.2369 0.0296 101 GLU A O 803 C CB . GLU A 101 ? 0.5837 0.4578 0.5560 -0.0287 0.2681 0.0305 101 GLU A CB 804 C CG . GLU A 101 ? 0.6534 0.5312 0.6372 -0.0399 0.2845 0.0307 101 GLU A CG 805 C CD . GLU A 101 ? 0.7567 0.6251 0.7294 -0.0411 0.2950 0.0482 101 GLU A CD 806 O OE1 . GLU A 101 ? 0.7841 0.6360 0.7484 -0.0335 0.2910 0.0581 101 GLU A OE1 807 O OE2 . GLU A 101 ? 0.8352 0.7138 0.8086 -0.0500 0.3075 0.0530 101 GLU A OE2 808 N N . PRO A 102 ? 0.5470 0.4226 0.4752 -0.0073 0.2448 0.0545 102 PRO A N 809 C CA . PRO A 102 ? 0.5304 0.4042 0.4512 0.0025 0.2306 0.0575 102 PRO A CA 810 C C . PRO A 102 ? 0.4819 0.3438 0.4170 0.0073 0.2237 0.0493 102 PRO A C 811 O O . PRO A 102 ? 0.4565 0.3023 0.4031 0.0069 0.2312 0.0484 102 PRO A O 812 C CB . PRO A 102 ? 0.5529 0.4185 0.4639 0.0062 0.2333 0.0752 102 PRO A CB 813 C CG . PRO A 102 ? 0.5599 0.4306 0.4617 -0.0030 0.2458 0.0821 102 PRO A CG 814 C CD . PRO A 102 ? 0.5478 0.4194 0.4660 -0.0107 0.2557 0.0697 102 PRO A CD 815 N N . ASN A 103 ? 0.3801 0.3198 0.3045 0.0783 0.1539 0.0564 103 ASN A N 816 C CA . ASN A 103 ? 0.3394 0.2859 0.2747 0.0703 0.1486 0.0505 103 ASN A CA 817 C C . ASN A 103 ? 0.3634 0.3098 0.2859 0.0704 0.1432 0.0493 103 ASN A C 818 O O . ASN A 103 ? 0.4145 0.3559 0.3198 0.0766 0.1432 0.0528 103 ASN A O 819 C CB . ASN A 103 ? 0.3482 0.2980 0.2903 0.0655 0.1465 0.0436 103 ASN A CB 820 C CG . ASN A 103 ? 0.3458 0.3038 0.3047 0.0573 0.1434 0.0386 103 ASN A CG 821 O OD1 . ASN A 103 ? 0.3438 0.3062 0.3043 0.0536 0.1391 0.0368 103 ASN A OD1 822 N ND2 . ASN A 103 ? 0.3223 0.2798 0.2927 0.0557 0.1472 0.0373 103 ASN A ND2 823 N N . VAL A 104 ? 0.3366 0.2888 0.2668 0.0636 0.1384 0.0441 104 VAL A N 824 C CA . VAL A 104 ? 0.3549 0.3067 0.2736 0.0631 0.1331 0.0425 104 VAL A CA 825 C C . VAL A 104 ? 0.3585 0.3143 0.2806 0.0572 0.1281 0.0351 104 VAL A C 826 O O . VAL A 104 ? 0.3451 0.3081 0.2832 0.0509 0.1272 0.0315 104 VAL A O 827 C CB . VAL A 104 ? 0.4251 0.3803 0.3496 0.0610 0.1325 0.0453 104 VAL A CB 828 C CG1 . VAL A 104 ? 0.2791 0.2333 0.1906 0.0602 0.1269 0.0434 104 VAL A CG1 829 C CG2 . VAL A 104 ? 0.2902 0.2424 0.2127 0.0673 0.1377 0.0536 104 VAL A CG2 830 N N . LEU A 105 ? 0.3450 0.2963 0.2513 0.0594 0.1246 0.0329 105 LEU A N 831 C CA . LEU A 105 ? 0.3184 0.2727 0.2262 0.0546 0.1198 0.0269 105 LEU A CA 832 C C . LEU A 105 ? 0.3164 0.2731 0.2235 0.0508 0.1157 0.0259 105 LEU A C 833 O O . LEU A 105 ? 0.2714 0.2237 0.1663 0.0540 0.1146 0.0289 105 LEU A O 834 C CB . LEU A 105 ? 0.3578 0.3053 0.2498 0.0586 0.1179 0.0248 105 LEU A CB 835 C CG . LEU A 105 ? 0.3781 0.3247 0.2732 0.0605 0.1211 0.0238 105 LEU A CG 836 C CD1 . LEU A 105 ? 0.3649 0.3033 0.2423 0.0656 0.1200 0.0227 105 LEU A CD1 837 C CD2 . LEU A 105 ? 0.3443 0.2988 0.2548 0.0546 0.1198 0.0193 105 LEU A CD2 838 N N . ILE A 106 ? 0.2469 0.2110 0.1665 0.0440 0.1131 0.0217 106 ILE A N 839 C CA . ILE A 106 ? 0.2560 0.2227 0.1758 0.0397 0.1094 0.0202 106 ILE A CA 840 C C . ILE A 106 ? 0.2694 0.2360 0.1839 0.0373 0.1048 0.0154 106 ILE A C 841 O O . ILE A 106 ? 0.3016 0.2731 0.2243 0.0348 0.1045 0.0122 106 ILE A O 842 C CB . ILE A 106 ? 0.2555 0.2320 0.1954 0.0330 0.1100 0.0192 106 ILE A CB 843 C CG1 . ILE A 106 ? 0.2853 0.2615 0.2328 0.0354 0.1149 0.0239 106 ILE A CG1 844 C CG2 . ILE A 106 ? 0.2774 0.2562 0.2177 0.0285 0.1067 0.0181 106 ILE A CG2 845 C CD1 . ILE A 106 ? 0.2765 0.2617 0.2441 0.0291 0.1152 0.0220 106 ILE A CD1 846 N N . CYS A 107 ? 0.2793 0.2400 0.1794 0.0381 0.1011 0.0151 107 CYS A N 847 C CA . CYS A 107 ? 0.2612 0.2208 0.1562 0.0355 0.0966 0.0108 107 CYS A CA 848 C C . CYS A 107 ? 0.2550 0.2195 0.1564 0.0290 0.0943 0.0097 107 CYS A C 849 O O . CYS A 107 ? 0.2350 0.1956 0.1288 0.0293 0.0930 0.0115 107 CYS A O 850 C CB . CYS A 107 ? 0.2569 0.2051 0.1301 0.0407 0.0930 0.0101 107 CYS A CB 851 S SG . CYS A 107 ? 0.2668 0.2117 0.1336 0.0382 0.0877 0.0051 107 CYS A SG 852 N N . PHE A 108 ? 0.2161 0.1896 0.1315 0.0232 0.0937 0.0067 108 PHE A N 853 C CA . PHE A 108 ? 0.2255 0.2047 0.1487 0.0163 0.0917 0.0053 108 PHE A CA 854 C C . PHE A 108 ? 0.2592 0.2345 0.1728 0.0142 0.0875 0.0024 108 PHE A C 855 O O . PHE A 108 ? 0.2524 0.2304 0.1680 0.0139 0.0868 0.0003 108 PHE A O 856 C CB . PHE A 108 ? 0.2207 0.2135 0.1655 0.0109 0.0927 0.0038 108 PHE A CB 857 C CG . PHE A 108 ? 0.2378 0.2375 0.1925 0.0036 0.0904 0.0023 108 PHE A CG 858 C CD1 . PHE A 108 ? 0.2460 0.2416 0.1975 0.0021 0.0904 0.0039 108 PHE A CD1 859 C CD2 . PHE A 108 ? 0.1828 0.1934 0.1500 -0.0013 0.0881 -0.0004 108 PHE A CD2 860 C CE1 . PHE A 108 ? 0.2465 0.2481 0.2083 -0.0051 0.0883 0.0023 108 PHE A CE1 861 C CE2 . PHE A 108 ? 0.1997 0.2159 0.1757 -0.0077 0.0854 -0.0016 108 PHE A CE2 862 C CZ . PHE A 108 ? 0.2303 0.2419 0.2044 -0.0099 0.0856 -0.0006 108 PHE A CZ 863 N N . ILE A 109 ? 0.2768 0.2451 0.1794 0.0128 0.0847 0.0023 109 ILE A N 864 C CA . ILE A 109 ? 0.2836 0.2455 0.1747 0.0105 0.0800 -0.0006 109 ILE A CA 865 C C . ILE A 109 ? 0.2616 0.2299 0.1632 0.0014 0.0792 -0.0020 109 ILE A C 866 O O . ILE A 109 ? 0.2954 0.2639 0.2000 -0.0012 0.0787 -0.0009 109 ILE A O 867 C CB . ILE A 109 ? 0.3005 0.2479 0.1690 0.0153 0.0751 -0.0007 109 ILE A CB 868 C CG1 . ILE A 109 ? 0.3370 0.2793 0.1965 0.0239 0.0764 0.0008 109 ILE A CG1 869 C CG2 . ILE A 109 ? 0.2762 0.2185 0.1392 0.0122 0.0660 -0.0043 109 ILE A CG2 870 C CD1 . ILE A 109 ? 0.3527 0.2947 0.2103 0.0277 0.0789 0.0047 109 ILE A CD1 871 N N . ASP A 110 ? 0.1961 0.1709 0.1052 -0.0037 0.0780 -0.0044 110 ASP A N 872 C CA . ASP A 110 ? 0.2008 0.1864 0.1258 -0.0128 0.0773 -0.0059 110 ASP A CA 873 C C . ASP A 110 ? 0.2462 0.2318 0.1688 -0.0188 0.0716 -0.0084 110 ASP A C 874 O O . ASP A 110 ? 0.2348 0.2157 0.1488 -0.0157 0.0684 -0.0086 110 ASP A O 875 C CB . ASP A 110 ? 0.2161 0.2165 0.1618 -0.0132 0.0793 -0.0055 110 ASP A CB 876 C CG . ASP A 110 ? 0.2754 0.2858 0.2383 -0.0204 0.0777 -0.0066 110 ASP A CG 877 O OD1 . ASP A 110 ? 0.2824 0.2895 0.2443 -0.0249 0.0765 -0.0072 110 ASP A OD1 878 O OD2 . ASP A 110 ? 0.3334 0.3542 0.3099 -0.0214 0.0770 -0.0070 110 ASP A OD2 879 N N . LYS A 111 ? 0.2805 0.2718 0.2127 -0.0271 0.0691 -0.0098 111 LYS A N 880 C CA . LYS A 111 ? 0.2723 0.2673 0.2069 -0.0338 0.0636 -0.0116 111 LYS A CA 881 C C . LYS A 111 ? 0.2636 0.2461 0.1840 -0.0311 0.0546 -0.0115 111 LYS A C 882 O O . LYS A 111 ? 0.3035 0.2863 0.2213 -0.0315 0.0520 -0.0114 111 LYS A O 883 C CB . LYS A 111 ? 0.2769 0.2837 0.2206 -0.0351 0.0674 -0.0120 111 LYS A CB 884 C CG . LYS A 111 ? 0.3837 0.4010 0.3387 -0.0430 0.0635 -0.0135 111 LYS A CG 885 C CD . LYS A 111 ? 0.4247 0.4531 0.3915 -0.0406 0.0643 -0.0131 111 LYS A CD 886 C CE . LYS A 111 ? 0.4356 0.4666 0.4122 -0.0353 0.0676 -0.0121 111 LYS A CE 887 N NZ . LYS A 111 ? 0.4278 0.4682 0.4144 -0.0329 0.0680 -0.0117 111 LYS A NZ 888 N N . PHE A 112 ? 0.1888 0.1607 0.1005 -0.0285 0.0498 -0.0115 112 PHE A N 889 C CA . PHE A 112 ? 0.2101 0.1697 0.1088 -0.0258 0.0416 -0.0123 112 PHE A CA 890 C C . PHE A 112 ? 0.2872 0.2418 0.1852 -0.0300 0.0346 -0.0139 112 PHE A C 891 O O . PHE A 112 ? 0.2547 0.2130 0.1596 -0.0329 0.0359 -0.0137 112 PHE A O 892 C CB . PHE A 112 ? 0.2252 0.1749 0.1099 -0.0161 0.0423 -0.0117 112 PHE A CB 893 C CG . PHE A 112 ? 0.2447 0.1910 0.1248 -0.0122 0.0435 -0.0108 112 PHE A CG 894 C CD1 . PHE A 112 ? 0.2116 0.1649 0.0986 -0.0104 0.0518 -0.0085 112 PHE A CD1 895 C CD2 . PHE A 112 ? 0.2636 0.2002 0.1331 -0.0102 0.0364 -0.0121 112 PHE A CD2 896 C CE1 . PHE A 112 ? 0.2173 0.1677 0.1002 -0.0064 0.0530 -0.0065 112 PHE A CE1 897 C CE2 . PHE A 112 ? 0.2998 0.2342 0.1646 -0.0063 0.0370 -0.0106 112 PHE A CE2 898 C CZ . PHE A 112 ? 0.3086 0.2499 0.1800 -0.0043 0.0453 -0.0073 112 PHE A CZ 899 N N . THR A 113 ? 0.3119 0.2577 0.2023 -0.0302 0.0274 -0.0154 113 THR A N 900 C CA . THR A 113 ? 0.2981 0.2371 0.1859 -0.0330 0.0200 -0.0176 113 THR A CA 901 C C . THR A 113 ? 0.3009 0.2282 0.1778 -0.0301 0.0138 -0.0195 113 THR A C 902 O O . THR A 113 ? 0.3084 0.2355 0.1844 -0.0290 0.0149 -0.0186 113 THR A O 903 C CB . THR A 113 ? 0.3560 0.3025 0.2571 -0.0429 0.0188 -0.0183 113 THR A CB 904 O OG1 . THR A 113 ? 0.2031 0.1448 0.1042 -0.0450 0.0134 -0.0201 113 THR A OG1 905 C CG2 . THR A 113 ? 0.1986 0.1456 0.1016 -0.0474 0.0161 -0.0186 113 THR A CG2 906 N N . PRO A 114 ? 0.3042 0.2223 0.1735 -0.0287 0.0074 -0.0222 114 PRO A N 907 C CA . PRO A 114 ? 0.2956 0.2131 0.1647 -0.0292 0.0046 -0.0231 114 PRO A CA 908 C C . PRO A 114 ? 0.2902 0.2089 0.1534 -0.0223 0.0091 -0.0210 114 PRO A C 909 O O . PRO A 114 ? 0.2986 0.2161 0.1554 -0.0165 0.0136 -0.0198 114 PRO A O 910 C CB . PRO A 114 ? 0.3123 0.2186 0.1724 -0.0282 -0.0038 -0.0273 114 PRO A CB 911 C CG . PRO A 114 ? 0.3013 0.2007 0.1531 -0.0237 -0.0034 -0.0282 114 PRO A CG 912 C CD . PRO A 114 ? 0.2460 0.1531 0.1065 -0.0263 0.0022 -0.0249 114 PRO A CD 913 N N . PRO A 115 ? 0.3300 0.2513 0.1961 -0.0228 0.0082 -0.0200 115 PRO A N 914 C CA . PRO A 115 ? 0.3139 0.2368 0.1749 -0.0162 0.0126 -0.0169 115 PRO A CA 915 C C . PRO A 115 ? 0.3410 0.2545 0.1839 -0.0085 0.0086 -0.0186 115 PRO A C 916 O O . PRO A 115 ? 0.3782 0.2904 0.2161 -0.0064 0.0047 -0.0183 115 PRO A O 917 C CB . PRO A 115 ? 0.3045 0.2333 0.1762 -0.0202 0.0120 -0.0152 115 PRO A CB 918 C CG . PRO A 115 ? 0.2935 0.2190 0.1683 -0.0264 0.0038 -0.0190 115 PRO A CG 919 C CD . PRO A 115 ? 0.2724 0.1964 0.1484 -0.0299 0.0037 -0.0212 115 PRO A CD 920 N N . VAL A 116 ? 0.3680 0.2757 0.2017 -0.0045 0.0096 -0.0203 116 VAL A N 921 C CA . VAL A 116 ? 0.3566 0.2559 0.1731 0.0030 0.0074 -0.0225 116 VAL A CA 922 C C . VAL A 116 ? 0.3543 0.2521 0.1657 0.0085 0.0144 -0.0214 116 VAL A C 923 O O . VAL A 116 ? 0.3831 0.2803 0.1990 0.0066 0.0158 -0.0223 116 VAL A O 924 C CB . VAL A 116 ? 0.3227 0.2129 0.1324 0.0016 -0.0011 -0.0285 116 VAL A CB 925 C CG1 . VAL A 116 ? 0.3133 0.1955 0.1052 0.0090 -0.0027 -0.0317 116 VAL A CG1 926 C CG2 . VAL A 116 ? 0.3009 0.1921 0.1165 -0.0042 -0.0083 -0.0303 116 VAL A CG2 927 N N . VAL A 117 ? 0.3592 0.2565 0.1612 0.0154 0.0187 -0.0193 117 VAL A N 928 C CA . VAL A 117 ? 0.3648 0.2607 0.1621 0.0210 0.0261 -0.0183 117 VAL A CA 929 C C . VAL A 117 ? 0.3845 0.2748 0.1646 0.0291 0.0271 -0.0187 117 VAL A C 930 O O . VAL A 117 ? 0.3948 0.2863 0.1693 0.0309 0.0249 -0.0171 117 VAL A O 931 C CB . VAL A 117 ? 0.4122 0.3179 0.2224 0.0202 0.0354 -0.0133 117 VAL A CB 932 C CG1 . VAL A 117 ? 0.4099 0.3216 0.2353 0.0130 0.0358 -0.0135 117 VAL A CG1 933 C CG2 . VAL A 117 ? 0.2827 0.1944 0.0973 0.0201 0.0375 -0.0091 117 VAL A CG2 934 N N . ASN A 118 ? 0.3795 0.2642 0.1515 0.0339 0.0304 -0.0208 118 ASN A N 935 C CA . ASN A 118 ? 0.3906 0.2722 0.1493 0.0413 0.0333 -0.0207 118 ASN A CA 936 C C . ASN A 118 ? 0.3902 0.2782 0.1582 0.0441 0.0432 -0.0159 118 ASN A C 937 O O . ASN A 118 ? 0.3904 0.2788 0.1659 0.0432 0.0469 -0.0163 118 ASN A O 938 C CB . ASN A 118 ? 0.4597 0.3331 0.2098 0.0437 0.0295 -0.0267 118 ASN A CB 939 C CG . ASN A 118 ? 0.5283 0.3963 0.2712 0.0408 0.0196 -0.0323 118 ASN A CG 940 O OD1 . ASN A 118 ? 0.4938 0.3645 0.2338 0.0395 0.0150 -0.0314 118 ASN A OD1 941 N ND2 . ASN A 118 ? 0.6549 0.5154 0.3962 0.0397 0.0163 -0.0380 118 ASN A ND2 942 N N . VAL A 119 ? 0.3783 0.2714 0.1468 0.0473 0.0474 -0.0112 119 VAL A N 943 C CA . VAL A 119 ? 0.3607 0.2600 0.1398 0.0495 0.0565 -0.0069 119 VAL A CA 944 C C . VAL A 119 ? 0.3827 0.2804 0.1539 0.0557 0.0592 -0.0056 119 VAL A C 945 O O . VAL A 119 ? 0.4401 0.3375 0.2019 0.0581 0.0568 -0.0040 119 VAL A O 946 C CB . VAL A 119 ? 0.3864 0.2942 0.1780 0.0468 0.0613 -0.0017 119 VAL A CB 947 C CG1 . VAL A 119 ? 0.3058 0.2203 0.1104 0.0487 0.0701 0.0019 119 VAL A CG1 948 C CG2 . VAL A 119 ? 0.3137 0.2236 0.1134 0.0399 0.0595 -0.0032 119 VAL A CG2 949 N N . THR A 120 ? 0.3813 0.2786 0.1562 0.0583 0.0642 -0.0060 120 THR A N 950 C CA . THR A 120 ? 0.3899 0.2856 0.1579 0.0638 0.0675 -0.0048 120 THR A CA 951 C C . THR A 120 ? 0.3594 0.2603 0.1403 0.0652 0.0760 -0.0010 120 THR A C 952 O O . THR A 120 ? 0.3343 0.2374 0.1263 0.0631 0.0786 -0.0019 120 THR A O 953 C CB . THR A 120 ? 0.4158 0.3036 0.1729 0.0661 0.0648 -0.0106 120 THR A CB 954 O OG1 . THR A 120 ? 0.4893 0.3722 0.2365 0.0641 0.0564 -0.0152 120 THR A OG1 955 C CG2 . THR A 120 ? 0.4104 0.2967 0.1585 0.0713 0.0679 -0.0098 120 THR A CG2 956 N N . TRP A 121 ? 0.3635 0.2667 0.1432 0.0686 0.0801 0.0034 121 TRP A N 957 C CA . TRP A 121 ? 0.3460 0.2527 0.1363 0.0705 0.0877 0.0064 121 TRP A CA 958 C C . TRP A 121 ? 0.3598 0.2607 0.1410 0.0747 0.0892 0.0039 121 TRP A C 959 O O . TRP A 121 ? 0.3757 0.2718 0.1414 0.0778 0.0866 0.0024 121 TRP A O 960 C CB . TRP A 121 ? 0.3471 0.2579 0.1402 0.0726 0.0919 0.0126 121 TRP A CB 961 C CG . TRP A 121 ? 0.3317 0.2495 0.1390 0.0684 0.0932 0.0157 121 TRP A CG 962 C CD1 . TRP A 121 ? 0.3999 0.3194 0.2044 0.0676 0.0908 0.0184 121 TRP A CD1 963 C CD2 . TRP A 121 ? 0.3144 0.2390 0.1416 0.0643 0.0973 0.0162 121 TRP A CD2 964 N NE1 . TRP A 121 ? 0.3831 0.3096 0.2050 0.0631 0.0939 0.0205 121 TRP A NE1 965 C CE2 . TRP A 121 ? 0.3902 0.3204 0.2264 0.0608 0.0976 0.0188 121 TRP A CE2 966 C CE3 . TRP A 121 ? 0.3068 0.2340 0.1453 0.0630 0.1005 0.0144 121 TRP A CE3 967 C CZ2 . TRP A 121 ? 0.3656 0.3040 0.2218 0.0556 0.1007 0.0190 121 TRP A CZ2 968 C CZ3 . TRP A 121 ? 0.2898 0.2256 0.1475 0.0580 0.1029 0.0147 121 TRP A CZ3 969 C CH2 . TRP A 121 ? 0.3500 0.2914 0.2165 0.0542 0.1029 0.0167 121 TRP A CH2 970 N N . LEU A 122 ? 0.3566 0.2585 0.1478 0.0745 0.0934 0.0032 122 LEU A N 971 C CA . LEU A 122 ? 0.3761 0.2728 0.1608 0.0783 0.0959 0.0009 122 LEU A CA 972 C C . LEU A 122 ? 0.3706 0.2706 0.1646 0.0803 0.1032 0.0046 122 LEU A C 973 O O . LEU A 122 ? 0.3513 0.2576 0.1615 0.0775 0.1061 0.0065 122 LEU A O 974 C CB . LEU A 122 ? 0.3779 0.2716 0.1653 0.0768 0.0943 -0.0037 122 LEU A CB 975 C CG . LEU A 122 ? 0.4116 0.3005 0.1906 0.0749 0.0873 -0.0082 122 LEU A CG 976 C CD1 . LEU A 122 ? 0.4037 0.2910 0.1895 0.0733 0.0871 -0.0111 122 LEU A CD1 977 C CD2 . LEU A 122 ? 0.4459 0.3276 0.2071 0.0779 0.0841 -0.0118 122 LEU A CD2 978 N N . ARG A 123 ? 0.4002 0.2964 0.1840 0.0848 0.1060 0.0053 123 ARG A N 979 C CA . ARG A 123 ? 0.3803 0.2780 0.1714 0.0869 0.1130 0.0082 123 ARG A CA 980 C C . ARG A 123 ? 0.4128 0.3049 0.1977 0.0894 0.1148 0.0043 123 ARG A C 981 O O . ARG A 123 ? 0.4077 0.2944 0.1769 0.0923 0.1134 0.0018 123 ARG A O 982 C CB . ARG A 123 ? 0.4955 0.3936 0.2806 0.0904 0.1162 0.0133 123 ARG A CB 983 C CG . ARG A 123 ? 0.5382 0.4367 0.3300 0.0928 0.1236 0.0162 123 ARG A CG 984 C CD . ARG A 123 ? 0.6388 0.5364 0.4221 0.0973 0.1271 0.0212 123 ARG A CD 985 N NE . ARG A 123 ? 0.7665 0.6686 0.5552 0.0965 0.1268 0.0262 123 ARG A NE 986 C CZ . ARG A 123 ? 0.8620 0.7655 0.6534 0.0994 0.1320 0.0323 123 ARG A CZ 987 N NH1 . ARG A 123 ? 0.8336 0.7412 0.6308 0.0986 0.1318 0.0368 123 ARG A NH1 988 N NH2 . ARG A 123 ? 0.9342 0.8349 0.7228 0.1031 0.1377 0.0340 123 ARG A NH2 989 N N . ASN A 124 ? 0.4141 0.3081 0.2118 0.0882 0.1178 0.0035 124 ASN A N 990 C CA . ASN A 124 ? 0.4272 0.3164 0.2216 0.0902 0.1198 -0.0003 124 ASN A CA 991 C C . ASN A 124 ? 0.4064 0.2894 0.1890 0.0903 0.1147 -0.0057 124 ASN A C 992 O O . ASN A 124 ? 0.4258 0.3029 0.1983 0.0931 0.1157 -0.0093 124 ASN A O 993 C CB . ASN A 124 ? 0.4286 0.3147 0.2158 0.0944 0.1252 0.0010 124 ASN A CB 994 C CG . ASN A 124 ? 0.4488 0.3398 0.2479 0.0944 0.1306 0.0062 124 ASN A CG 995 O OD1 . ASN A 124 ? 0.3841 0.2807 0.1995 0.0912 0.1315 0.0071 124 ASN A OD1 996 N ND2 . ASN A 124 ? 0.4118 0.3011 0.2029 0.0978 0.1341 0.0094 124 ASN A ND2 997 N N . GLY A 125 ? 0.3894 0.2739 0.1740 0.0871 0.1093 -0.0067 125 GLY A N 998 C CA . GLY A 125 ? 0.4033 0.2817 0.1784 0.0868 0.1041 -0.0119 125 GLY A CA 999 C C . GLY A 125 ? 0.4168 0.2914 0.1751 0.0879 0.0997 -0.0140 125 GLY A C 1000 O O . GLY A 125 ? 0.4507 0.3199 0.2005 0.0874 0.0951 -0.0192 125 GLY A O 1001 N N . LYS A 126 ? 0.4138 0.2912 0.1675 0.0892 0.1009 -0.0101 126 LYS A N 1002 C CA . LYS A 126 ? 0.4277 0.3031 0.1652 0.0904 0.0965 -0.0116 126 LYS A CA 1003 C C . LYS A 126 ? 0.4986 0.3788 0.2376 0.0884 0.0929 -0.0076 126 LYS A C 1004 O O . LYS A 126 ? 0.4688 0.3544 0.2188 0.0878 0.0965 -0.0021 126 LYS A O 1005 C CB . LYS A 126 ? 0.4603 0.3347 0.1880 0.0946 0.1010 -0.0104 126 LYS A CB 1006 C CG . LYS A 126 ? 0.4807 0.3506 0.2067 0.0968 0.1055 -0.0142 126 LYS A CG 1007 C CD . LYS A 126 ? 0.5381 0.4074 0.2524 0.1006 0.1094 -0.0132 126 LYS A CD 1008 C CE . LYS A 126 ? 0.5834 0.4484 0.2960 0.1026 0.1145 -0.0172 126 LYS A CE 1009 N NZ . LYS A 126 ? 0.6381 0.5027 0.3380 0.1060 0.1183 -0.0166 126 LYS A NZ 1010 N N . PRO A 127 ? 0.5011 0.3795 0.2295 0.0870 0.0858 -0.0108 127 PRO A N 1011 C CA . PRO A 127 ? 0.4602 0.3429 0.1891 0.0850 0.0817 -0.0074 127 PRO A CA 1012 C C . PRO A 127 ? 0.4796 0.3663 0.2050 0.0881 0.0850 -0.0012 127 PRO A C 1013 O O . PRO A 127 ? 0.5040 0.3892 0.2174 0.0916 0.0862 -0.0016 127 PRO A O 1014 C CB . PRO A 127 ? 0.4815 0.3604 0.1973 0.0836 0.0733 -0.0132 127 PRO A CB 1015 C CG . PRO A 127 ? 0.5172 0.3898 0.2312 0.0835 0.0731 -0.0198 127 PRO A CG 1016 C CD . PRO A 127 ? 0.5154 0.3875 0.2323 0.0869 0.0810 -0.0183 127 PRO A CD 1017 N N . VAL A 128 ? 0.4796 0.3718 0.2158 0.0867 0.0867 0.0045 128 VAL A N 1018 C CA . VAL A 128 ? 0.5051 0.4011 0.2396 0.0897 0.0900 0.0112 128 VAL A CA 1019 C C . VAL A 128 ? 0.5175 0.4174 0.2528 0.0877 0.0856 0.0143 128 VAL A C 1020 O O . VAL A 128 ? 0.5043 0.4058 0.2494 0.0833 0.0834 0.0132 128 VAL A O 1021 C CB . VAL A 128 ? 0.5015 0.4005 0.2509 0.0909 0.0988 0.0162 128 VAL A CB 1022 C CG1 . VAL A 128 ? 0.5494 0.4445 0.2951 0.0940 0.1035 0.0143 128 VAL A CG1 1023 C CG2 . VAL A 128 ? 0.4382 0.3405 0.2061 0.0861 0.0998 0.0157 128 VAL A CG2 1024 N N . THR A 129 ? 0.6021 0.5039 0.3268 0.0908 0.0842 0.0182 129 THR A N 1025 C CA . THR A 129 ? 0.6245 0.5299 0.3484 0.0892 0.0794 0.0213 129 THR A CA 1026 C C . THR A 129 ? 0.6542 0.5645 0.3804 0.0929 0.0842 0.0303 129 THR A C 1027 O O . THR A 129 ? 0.7027 0.6168 0.4312 0.0920 0.0818 0.0346 129 THR A O 1028 C CB . THR A 129 ? 0.6205 0.5241 0.3274 0.0887 0.0696 0.0166 129 THR A CB 1029 O OG1 . THR A 129 ? 0.6258 0.5295 0.3180 0.0931 0.0697 0.0174 129 THR A OG1 1030 C CG2 . THR A 129 ? 0.5902 0.4885 0.2956 0.0852 0.0650 0.0076 129 THR A CG2 1031 N N . THR A 130 ? 0.6479 0.5578 0.3734 0.0971 0.0910 0.0335 130 THR A N 1032 C CA . THR A 130 ? 0.6546 0.5685 0.3823 0.1012 0.0963 0.0424 130 THR A CA 1033 C C . THR A 130 ? 0.6375 0.5555 0.3860 0.0993 0.1018 0.0475 130 THR A C 1034 O O . THR A 130 ? 0.6504 0.5680 0.4137 0.0975 0.1075 0.0464 130 THR A O 1035 C CB . THR A 130 ? 0.6604 0.5723 0.3837 0.1061 0.1030 0.0443 130 THR A CB 1036 O OG1 . THR A 130 ? 0.6879 0.5973 0.3912 0.1080 0.0983 0.0400 130 THR A OG1 1037 C CG2 . THR A 130 ? 0.6700 0.5859 0.3977 0.1104 0.1092 0.0540 130 THR A CG2 1038 N N . GLY A 131 ? 0.6129 0.5352 0.3633 0.0993 0.1000 0.0530 131 GLY A N 1039 C CA . GLY A 131 ? 0.5621 0.4888 0.3326 0.0976 0.1059 0.0584 131 GLY A CA 1040 C C . GLY A 131 ? 0.5272 0.4551 0.3102 0.0907 0.1036 0.0540 131 GLY A C 1041 O O . GLY A 131 ? 0.5453 0.4775 0.3465 0.0881 0.1083 0.0572 131 GLY A O 1042 N N . VAL A 132 ? 0.4561 0.3806 0.2301 0.0877 0.0966 0.0464 132 VAL A N 1043 C CA . VAL A 132 ? 0.4218 0.3473 0.2065 0.0811 0.0943 0.0420 132 VAL A CA 1044 C C . VAL A 132 ? 0.4362 0.3650 0.2227 0.0788 0.0908 0.0454 132 VAL A C 1045 O O . VAL A 132 ? 0.4936 0.4228 0.2679 0.0820 0.0866 0.0493 132 VAL A O 1046 C CB . VAL A 132 ? 0.4151 0.3353 0.1901 0.0787 0.0877 0.0333 132 VAL A CB 1047 C CG1 . VAL A 132 ? 0.3703 0.2872 0.1447 0.0808 0.0915 0.0303 132 VAL A CG1 1048 C CG2 . VAL A 132 ? 0.4266 0.3437 0.1818 0.0801 0.0785 0.0311 132 VAL A CG2 1049 N N . SER A 133 ? 0.3787 0.3107 0.1809 0.0729 0.0924 0.0439 133 SER A N 1050 C CA . SER A 133 ? 0.3671 0.3020 0.1727 0.0696 0.0895 0.0464 133 SER A CA 1051 C C . SER A 133 ? 0.3684 0.3039 0.1836 0.0622 0.0881 0.0403 133 SER A C 1052 O O . SER A 133 ? 0.3676 0.3026 0.1891 0.0601 0.0899 0.0353 133 SER A O 1053 C CB . SER A 133 ? 0.3698 0.3109 0.1913 0.0706 0.0970 0.0549 133 SER A CB 1054 O OG . SER A 133 ? 0.3971 0.3420 0.2404 0.0674 0.1048 0.0538 133 SER A OG 1055 N N . GLU A 134 ? 0.3727 0.3095 0.1893 0.0583 0.0847 0.0411 134 GLU A N 1056 C CA . GLU A 134 ? 0.3582 0.2951 0.1821 0.0511 0.0829 0.0352 134 GLU A CA 1057 C C . GLU A 134 ? 0.3472 0.2899 0.1872 0.0446 0.0793 0.0367 134 GLU A C 1058 O O . GLU A 134 ? 0.3684 0.3124 0.2065 0.0468 0.0760 0.0418 134 GLU A O 1059 C CB . GLU A 134 ? 0.3499 0.2794 0.1570 0.0505 0.0728 0.0277 134 GLU A CB 1060 C CG . GLU A 134 ? 0.3896 0.3168 0.1860 0.0502 0.0610 0.0269 134 GLU A CG 1061 C CD . GLU A 134 ? 0.4034 0.3227 0.1827 0.0506 0.0521 0.0192 134 GLU A CD 1062 O OE1 . GLU A 134 ? 0.4172 0.3317 0.1806 0.0567 0.0535 0.0182 134 GLU A OE1 1063 O OE2 . GLU A 134 ? 0.4053 0.3235 0.1889 0.0444 0.0440 0.0139 134 GLU A OE2 1064 N N . THR A 135 ? 0.2475 0.2293 0.1425 0.0315 -0.0281 0.0083 135 THR A N 1065 C CA . THR A 135 ? 0.2540 0.2352 0.1554 0.0379 -0.0297 0.0101 135 THR A CA 1066 C C . THR A 135 ? 0.2427 0.2415 0.1573 0.0383 -0.0353 0.0043 135 THR A C 1067 O O . THR A 135 ? 0.1960 0.2036 0.1151 0.0325 -0.0363 -0.0021 135 THR A O 1068 C CB . THR A 135 ? 0.2336 0.1995 0.1370 0.0351 -0.0240 0.0092 135 THR A CB 1069 O OG1 . THR A 135 ? 0.1950 0.1686 0.1090 0.0276 -0.0239 0.0024 135 THR A OG1 1070 C CG2 . THR A 135 ? 0.2514 0.1989 0.1421 0.0314 -0.0180 0.0135 135 THR A CG2 1071 N N . VAL A 136 ? 0.2794 0.2828 0.2006 0.0454 -0.0378 0.0074 136 VAL A N 1072 C CA . VAL A 136 ? 0.2296 0.2483 0.1656 0.0453 -0.0424 0.0027 136 VAL A CA 1073 C C . VAL A 136 ? 0.2190 0.2328 0.1646 0.0409 -0.0383 -0.0025 136 VAL A C 1074 O O . VAL A 136 ? 0.2436 0.2440 0.1834 0.0367 -0.0327 -0.0027 136 VAL A O 1075 C CB . VAL A 136 ? 0.1984 0.2256 0.1398 0.0550 -0.0459 0.0098 136 VAL A CB 1076 C CG1 . VAL A 136 ? 0.2111 0.2496 0.1444 0.0587 -0.0509 0.0169 136 VAL A CG1 1077 C CG2 . VAL A 136 ? 0.1941 0.2038 0.1335 0.0616 -0.0390 0.0151 136 VAL A CG2 1078 N N . PHE A 137 ? 0.2027 0.2292 0.1634 0.0412 -0.0411 -0.0059 137 PHE A N 1079 C CA . PHE A 137 ? 0.2261 0.2520 0.1972 0.0378 -0.0374 -0.0093 137 PHE A CA 1080 C C . PHE A 137 ? 0.2302 0.2445 0.1982 0.0428 -0.0338 -0.0059 137 PHE A C 1081 O O . PHE A 137 ? 0.2367 0.2525 0.2063 0.0515 -0.0352 -0.0015 137 PHE A O 1082 C CB . PHE A 137 ? 0.1861 0.2294 0.1753 0.0369 -0.0408 -0.0132 137 PHE A CB 1083 C CG . PHE A 137 ? 0.1540 0.2043 0.1456 0.0307 -0.0416 -0.0183 137 PHE A CG 1084 C CD1 . PHE A 137 ? 0.1694 0.2272 0.1572 0.0308 -0.0471 -0.0198 137 PHE A CD1 1085 C CD2 . PHE A 137 ? 0.1389 0.1886 0.1360 0.0245 -0.0361 -0.0210 137 PHE A CD2 1086 C CE1 . PHE A 137 ? 0.1495 0.2103 0.1367 0.0242 -0.0461 -0.0262 137 PHE A CE1 1087 C CE2 . PHE A 137 ? 0.1300 0.1829 0.1289 0.0198 -0.0341 -0.0256 137 PHE A CE2 1088 C CZ . PHE A 137 ? 0.1511 0.2075 0.1439 0.0194 -0.0388 -0.0293 137 PHE A CZ 1089 N N . LEU A 138 ? 0.2159 0.2190 0.1790 0.0368 -0.0283 -0.0077 138 LEU A N 1090 C CA . LEU A 138 ? 0.2171 0.2044 0.1726 0.0395 -0.0230 -0.0064 138 LEU A CA 1091 C C . LEU A 138 ? 0.2148 0.2096 0.1807 0.0367 -0.0215 -0.0100 138 LEU A C 1092 O O . LEU A 138 ? 0.1628 0.1694 0.1371 0.0288 -0.0222 -0.0127 138 LEU A O 1093 C CB . LEU A 138 ? 0.2122 0.1796 0.1510 0.0328 -0.0175 -0.0060 138 LEU A CB 1094 C CG . LEU A 138 ? 0.1922 0.1534 0.1208 0.0351 -0.0184 -0.0015 138 LEU A CG 1095 C CD1 . LEU A 138 ? 0.2051 0.1501 0.1204 0.0261 -0.0134 -0.0012 138 LEU A CD1 1096 C CD2 . LEU A 138 ? 0.2069 0.1614 0.1315 0.0474 -0.0177 0.0052 138 LEU A CD2 1097 N N . PRO A 139 ? 0.2134 0.2022 0.1791 0.0439 -0.0186 -0.0089 139 PRO A N 1098 C CA . PRO A 139 ? 0.1965 0.1949 0.1723 0.0425 -0.0175 -0.0118 139 PRO A CA 1099 C C . PRO A 139 ? 0.2529 0.2422 0.2188 0.0313 -0.0121 -0.0162 139 PRO A C 1100 O O . PRO A 139 ? 0.2773 0.2449 0.2253 0.0273 -0.0069 -0.0174 139 PRO A O 1101 C CB . PRO A 139 ? 0.1922 0.1842 0.1679 0.0549 -0.0146 -0.0083 139 PRO A CB 1102 C CG . PRO A 139 ? 0.1930 0.1623 0.1520 0.0593 -0.0100 -0.0047 139 PRO A CG 1103 C CD . PRO A 139 ? 0.1803 0.1543 0.1374 0.0548 -0.0152 -0.0036 139 PRO A CD 1104 N N . ARG A 140 ? 0.2196 0.2270 0.1974 0.0256 -0.0132 -0.0181 140 ARG A N 1105 C CA . ARG A 140 ? 0.1837 0.1886 0.1530 0.0142 -0.0090 -0.0215 140 ARG A CA 1106 C C . ARG A 140 ? 0.1862 0.1942 0.1582 0.0182 -0.0060 -0.0235 140 ARG A C 1107 O O . ARG A 140 ? 0.1813 0.2008 0.1680 0.0289 -0.0085 -0.0209 140 ARG A O 1108 C CB . ARG A 140 ? 0.1250 0.1523 0.1063 0.0039 -0.0117 -0.0197 140 ARG A CB 1109 C CG . ARG A 140 ? 0.1273 0.1503 0.1032 -0.0019 -0.0126 -0.0177 140 ARG A CG 1110 C CD . ARG A 140 ? 0.1233 0.1706 0.1150 -0.0087 -0.0137 -0.0136 140 ARG A CD 1111 N NE . ARG A 140 ? 0.1242 0.1868 0.1201 -0.0171 -0.0121 -0.0128 140 ARG A NE 1112 C CZ . ARG A 140 ? 0.1282 0.1910 0.1127 -0.0307 -0.0101 -0.0123 140 ARG A CZ 1113 N NH1 . ARG A 140 ? 0.1277 0.1742 0.0969 -0.0368 -0.0091 -0.0125 140 ARG A NH1 1114 N NH2 . ARG A 140 ? 0.1079 0.1886 0.0961 -0.0389 -0.0094 -0.0112 140 ARG A NH2 1115 N N . GLU A 141 ? 0.1619 0.1597 0.1186 0.0088 -0.0006 -0.0282 141 GLU A N 1116 C CA . GLU A 141 ? 0.1672 0.1662 0.1226 0.0114 0.0036 -0.0310 141 GLU A CA 1117 C C . GLU A 141 ? 0.1730 0.2056 0.1505 0.0106 -0.0008 -0.0279 141 GLU A C 1118 O O . GLU A 141 ? 0.1497 0.1889 0.1321 0.0164 0.0013 -0.0282 141 GLU A O 1119 C CB . GLU A 141 ? 0.2064 0.1849 0.1366 -0.0011 0.0111 -0.0384 141 GLU A CB 1120 C CG . GLU A 141 ? 0.3491 0.2902 0.2579 0.0015 0.0182 -0.0412 141 GLU A CG 1121 C CD . GLU A 141 ? 0.4462 0.3629 0.3285 -0.0119 0.0273 -0.0503 141 GLU A CD 1122 O OE1 . GLU A 141 ? 0.4851 0.4052 0.3625 -0.0148 0.0312 -0.0552 141 GLU A OE1 1123 O OE2 . GLU A 141 ? 0.5035 0.3972 0.3691 -0.0203 0.0309 -0.0528 141 GLU A OE2 1124 N N . ASP A 142 ? 0.1329 0.1861 0.1242 0.0042 -0.0058 -0.0240 142 ASP A N 1125 C CA . ASP A 142 ? 0.1208 0.2056 0.1364 0.0049 -0.0088 -0.0191 142 ASP A CA 1126 C C . ASP A 142 ? 0.1528 0.2462 0.1889 0.0168 -0.0131 -0.0152 142 ASP A C 1127 O O . ASP A 142 ? 0.1209 0.2378 0.1794 0.0182 -0.0150 -0.0107 142 ASP A O 1128 C CB . ASP A 142 ? 0.0820 0.1872 0.1032 -0.0086 -0.0096 -0.0151 142 ASP A CB 1129 C CG . ASP A 142 ? 0.1781 0.2784 0.1989 -0.0119 -0.0112 -0.0128 142 ASP A CG 1130 O OD1 . ASP A 142 ? 0.0840 0.1682 0.1022 -0.0037 -0.0127 -0.0144 142 ASP A OD1 1131 O OD2 . ASP A 142 ? 0.1773 0.2920 0.2008 -0.0227 -0.0109 -0.0084 142 ASP A OD2 1132 N N . HIS A 143 ? 0.1548 0.2290 0.1826 0.0244 -0.0141 -0.0166 143 HIS A N 1133 C CA . HIS A 143 ? 0.1316 0.2123 0.1746 0.0349 -0.0186 -0.0138 143 HIS A CA 1134 C C . HIS A 143 ? 0.1041 0.1957 0.1591 0.0311 -0.0220 -0.0124 143 HIS A C 1135 O O . HIS A 143 ? 0.0822 0.1716 0.1452 0.0322 -0.0228 -0.0091 143 HIS A O 1136 C CB . HIS A 143 ? 0.0997 0.1945 0.1585 0.0428 -0.0189 -0.0112 143 HIS A CB 1137 C CG . HIS A 143 ? 0.1765 0.2619 0.2230 0.0459 -0.0135 -0.0131 143 HIS A CG 1138 N ND1 . HIS A 143 ? 0.1542 0.2145 0.1818 0.0516 -0.0094 -0.0148 143 HIS A ND1 1139 C CD2 . HIS A 143 ? 0.0768 0.1727 0.1257 0.0437 -0.0102 -0.0136 143 HIS A CD2 1140 C CE1 . HIS A 143 ? 0.1382 0.1911 0.1561 0.0527 -0.0029 -0.0172 143 HIS A CE1 1141 N NE2 . HIS A 143 ? 0.1442 0.2194 0.1740 0.0476 -0.0038 -0.0169 143 HIS A NE2 1142 N N . LEU A 144 ? 0.1680 0.2581 0.2162 0.0213 -0.0201 -0.0125 144 LEU A N 1143 C CA . LEU A 144 ? 0.0563 0.1482 0.1087 0.0185 -0.0211 -0.0115 144 LEU A CA 1144 C C . LEU A 144 ? 0.0743 0.1448 0.1074 0.0201 -0.0224 -0.0138 144 LEU A C 1145 O O . LEU A 144 ? 0.1127 0.1689 0.1338 0.0254 -0.0224 -0.0149 144 LEU A O 1146 C CB . LEU A 144 ? 0.0906 0.1932 0.1459 0.0082 -0.0177 -0.0081 144 LEU A CB 1147 C CG . LEU A 144 ? 0.0921 0.2027 0.1593 0.0054 -0.0140 -0.0027 144 LEU A CG 1148 C CD1 . LEU A 144 ? 0.0412 0.1578 0.1064 -0.0035 -0.0103 0.0021 144 LEU A CD1 1149 C CD2 . LEU A 144 ? 0.0524 0.1512 0.1309 0.0091 -0.0126 -0.0003 144 LEU A CD2 1150 N N . PHE A 145 ? 0.0750 0.1432 0.1054 0.0165 -0.0224 -0.0134 145 PHE A N 1151 C CA . PHE A 145 ? 0.1098 0.1607 0.1234 0.0186 -0.0238 -0.0144 145 PHE A CA 1152 C C . PHE A 145 ? 0.1183 0.1617 0.1204 0.0104 -0.0208 -0.0131 145 PHE A C 1153 O O . PHE A 145 ? 0.1185 0.1732 0.1284 0.0034 -0.0180 -0.0107 145 PHE A O 1154 C CB . PHE A 145 ? 0.1209 0.1766 0.1408 0.0238 -0.0279 -0.0155 145 PHE A CB 1155 C CG . PHE A 145 ? 0.0968 0.1609 0.1275 0.0314 -0.0318 -0.0156 145 PHE A CG 1156 C CD1 . PHE A 145 ? 0.1109 0.1671 0.1328 0.0390 -0.0344 -0.0136 145 PHE A CD1 1157 C CD2 . PHE A 145 ? 0.0714 0.1522 0.1224 0.0314 -0.0323 -0.0160 145 PHE A CD2 1158 C CE1 . PHE A 145 ? 0.0896 0.1564 0.1229 0.0462 -0.0380 -0.0117 145 PHE A CE1 1159 C CE2 . PHE A 145 ? 0.0650 0.1469 0.1220 0.0343 -0.0330 -0.0133 145 PHE A CE2 1160 C CZ . PHE A 145 ? 0.0789 0.1568 0.1286 0.0418 -0.0366 -0.0116 145 PHE A CZ 1161 N N . ARG A 146 ? 0.1460 0.1720 0.1309 0.0117 -0.0210 -0.0130 146 ARG A N 1162 C CA . ARG A 146 ? 0.1944 0.2135 0.1689 0.0047 -0.0185 -0.0110 146 ARG A CA 1163 C C . ARG A 146 ? 0.1810 0.1900 0.1449 0.0102 -0.0204 -0.0105 146 ARG A C 1164 O O . ARG A 146 ? 0.1765 0.1832 0.1394 0.0184 -0.0237 -0.0109 146 ARG A O 1165 C CB . ARG A 146 ? 0.2048 0.2115 0.1657 -0.0033 -0.0150 -0.0104 146 ARG A CB 1166 C CG . ARG A 146 ? 0.2331 0.2259 0.1854 -0.0003 -0.0136 -0.0132 146 ARG A CG 1167 C CD . ARG A 146 ? 0.3248 0.2980 0.2583 -0.0095 -0.0090 -0.0136 146 ARG A CD 1168 N NE . ARG A 146 ? 0.4522 0.4011 0.3717 -0.0035 -0.0052 -0.0154 146 ARG A NE 1169 C CZ . ARG A 146 ? 0.5613 0.4869 0.4630 -0.0098 0.0002 -0.0162 146 ARG A CZ 1170 N NH1 . ARG A 146 ? 0.5133 0.4393 0.4091 -0.0233 0.0009 -0.0154 146 ARG A NH1 1171 N NH2 . ARG A 146 ? 0.6681 0.5699 0.5586 -0.0026 0.0058 -0.0169 146 ARG A NH2 1172 N N . LYS A 147 ? 0.1632 0.1687 0.1198 0.0057 -0.0184 -0.0083 147 LYS A N 1173 C CA . LYS A 147 ? 0.2003 0.1997 0.1470 0.0102 -0.0201 -0.0074 147 LYS A CA 1174 C C . LYS A 147 ? 0.2515 0.2426 0.1868 0.0044 -0.0164 -0.0035 147 LYS A C 1175 O O . LYS A 147 ? 0.2918 0.2886 0.2318 -0.0033 -0.0129 -0.0015 147 LYS A O 1176 C CB . LYS A 147 ? 0.1822 0.1949 0.1388 0.0124 -0.0222 -0.0107 147 LYS A CB 1177 C CG . LYS A 147 ? 0.2335 0.2449 0.1807 0.0174 -0.0261 -0.0114 147 LYS A CG 1178 C CD . LYS A 147 ? 0.2468 0.2697 0.2025 0.0163 -0.0269 -0.0169 147 LYS A CD 1179 C CE . LYS A 147 ? 0.2494 0.2762 0.1973 0.0197 -0.0330 -0.0188 147 LYS A CE 1180 N NZ . LYS A 147 ? 0.2677 0.2876 0.1975 0.0202 -0.0327 -0.0156 147 LYS A NZ 1181 N N . PHE A 148 ? 0.2452 0.2253 0.1668 0.0082 -0.0170 -0.0009 148 PHE A N 1182 C CA . PHE A 148 ? 0.2246 0.1970 0.1354 0.0034 -0.0134 0.0037 148 PHE A CA 1183 C C . PHE A 148 ? 0.2044 0.1804 0.1091 0.0076 -0.0145 0.0046 148 PHE A C 1184 O O . PHE A 148 ? 0.2320 0.2097 0.1333 0.0146 -0.0186 0.0036 148 PHE A O 1185 C CB . PHE A 148 ? 0.2707 0.2238 0.1684 0.0033 -0.0112 0.0074 148 PHE A CB 1186 C CG . PHE A 148 ? 0.2831 0.2284 0.1814 -0.0030 -0.0087 0.0053 148 PHE A CG 1187 C CD1 . PHE A 148 ? 0.2911 0.2344 0.1934 0.0022 -0.0098 0.0017 148 PHE A CD1 1188 C CD2 . PHE A 148 ? 0.2986 0.2392 0.1923 -0.0148 -0.0051 0.0072 148 PHE A CD2 1189 C CE1 . PHE A 148 ? 0.2333 0.1684 0.1335 -0.0042 -0.0066 -0.0013 148 PHE A CE1 1190 C CE2 . PHE A 148 ? 0.3081 0.2419 0.1996 -0.0229 -0.0029 0.0042 148 PHE A CE2 1191 C CZ . PHE A 148 ? 0.2976 0.2277 0.1913 -0.0175 -0.0033 -0.0007 148 PHE A CZ 1192 N N . HIS A 149 ? 0.1931 0.1716 0.0961 0.0029 -0.0104 0.0071 149 HIS A N 1193 C CA . HIS A 149 ? 0.2189 0.1984 0.1123 0.0058 -0.0098 0.0082 149 HIS A CA 1194 C C . HIS A 149 ? 0.2505 0.2211 0.1334 0.0026 -0.0057 0.0159 149 HIS A C 1195 O O . HIS A 149 ? 0.2476 0.2168 0.1344 -0.0046 -0.0022 0.0196 149 HIS A O 1196 C CB . HIS A 149 ? 0.1930 0.1834 0.0944 0.0046 -0.0068 0.0037 149 HIS A CB 1197 C CG . HIS A 149 ? 0.2267 0.2245 0.1345 0.0079 -0.0111 -0.0042 149 HIS A CG 1198 N ND1 . HIS A 149 ? 0.2365 0.2377 0.1372 0.0096 -0.0121 -0.0094 149 HIS A ND1 1199 C CD2 . HIS A 149 ? 0.2176 0.2204 0.1377 0.0089 -0.0146 -0.0077 149 HIS A CD2 1200 C CE1 . HIS A 149 ? 0.2303 0.2385 0.1392 0.0105 -0.0164 -0.0158 149 HIS A CE1 1201 N NE2 . HIS A 149 ? 0.1951 0.2047 0.1168 0.0109 -0.0179 -0.0144 149 HIS A NE2 1202 N N . TYR A 150 ? 0.2934 0.2602 0.1633 0.0070 -0.0063 0.0191 150 TYR A N 1203 C CA . TYR A 150 ? 0.2931 0.2507 0.1532 0.0048 -0.0025 0.0275 150 TYR A CA 1204 C C . TYR A 150 ? 0.2676 0.2301 0.1189 0.0066 0.0003 0.0302 150 TYR A C 1205 O O . TYR A 150 ? 0.2800 0.2492 0.1259 0.0114 -0.0022 0.0259 150 TYR A O 1206 C CB . TYR A 150 ? 0.3113 0.2561 0.1628 0.0095 -0.0042 0.0321 150 TYR A CB 1207 C CG . TYR A 150 ? 0.2850 0.2209 0.1420 0.0089 -0.0051 0.0296 150 TYR A CG 1208 C CD1 . TYR A 150 ? 0.2988 0.2238 0.1566 0.0001 -0.0013 0.0306 150 TYR A CD1 1209 C CD2 . TYR A 150 ? 0.3134 0.2525 0.1738 0.0164 -0.0094 0.0263 150 TYR A CD2 1210 C CE1 . TYR A 150 ? 0.3326 0.2479 0.1927 -0.0010 -0.0010 0.0270 150 TYR A CE1 1211 C CE2 . TYR A 150 ? 0.3073 0.2376 0.1720 0.0169 -0.0089 0.0243 150 TYR A CE2 1212 C CZ . TYR A 150 ? 0.3152 0.2324 0.1788 0.0082 -0.0043 0.0239 150 TYR A CZ 1213 O OH . TYR A 150 ? 0.2603 0.1671 0.1257 0.0081 -0.0026 0.0206 150 TYR A OH 1214 N N . LEU A 151 ? 0.2817 0.2416 0.1309 0.0020 0.0057 0.0373 151 LEU A N 1215 C CA . LEU A 151 ? 0.3350 0.2983 0.1748 0.0041 0.0099 0.0414 151 LEU A CA 1216 C C . LEU A 151 ? 0.3348 0.2898 0.1678 0.0015 0.0131 0.0526 151 LEU A C 1217 O O . LEU A 151 ? 0.3715 0.3266 0.2109 -0.0060 0.0170 0.0580 151 LEU A O 1218 C CB . LEU A 151 ? 0.3279 0.3006 0.1756 0.0016 0.0161 0.0394 151 LEU A CB 1219 C CG . LEU A 151 ? 0.3579 0.3329 0.1960 0.0037 0.0230 0.0442 151 LEU A CG 1220 C CD1 . LEU A 151 ? 0.3549 0.3301 0.1770 0.0099 0.0201 0.0390 151 LEU A CD1 1221 C CD2 . LEU A 151 ? 0.3230 0.3055 0.1713 0.0023 0.0316 0.0436 151 LEU A CD2 1222 N N . PRO A 152 ? 0.3274 0.2769 0.1482 0.0072 0.0115 0.0573 152 PRO A N 1223 C CA . PRO A 152 ? 0.3711 0.3131 0.1852 0.0056 0.0156 0.0688 152 PRO A CA 1224 C C . PRO A 152 ? 0.3924 0.3432 0.2048 0.0040 0.0216 0.0730 152 PRO A C 1225 O O . PRO A 152 ? 0.4277 0.3875 0.2359 0.0084 0.0225 0.0677 152 PRO A O 1226 C CB . PRO A 152 ? 0.3545 0.2944 0.1572 0.0146 0.0130 0.0728 152 PRO A CB 1227 C CG . PRO A 152 ? 0.3750 0.3266 0.1762 0.0199 0.0076 0.0634 152 PRO A CG 1228 C CD . PRO A 152 ? 0.3523 0.3047 0.1666 0.0152 0.0059 0.0538 152 PRO A CD 1229 N N . PHE A 153 ? 0.3694 0.3175 0.1846 -0.0025 0.0262 0.0826 153 PHE A N 1230 C CA . PHE A 153 ? 0.3569 0.3156 0.1750 -0.0040 0.0322 0.0876 153 PHE A CA 1231 C C . PHE A 153 ? 0.3709 0.3266 0.1926 -0.0111 0.0339 0.0974 153 PHE A C 1232 O O . PHE A 153 ? 0.3763 0.3236 0.1998 -0.0169 0.0322 0.1021 153 PHE A O 1233 C CB . PHE A 153 ? 0.3078 0.2762 0.1385 -0.0081 0.0356 0.0846 153 PHE A CB 1234 C CG . PHE A 153 ? 0.3153 0.2833 0.1587 -0.0187 0.0357 0.0888 153 PHE A CG 1235 C CD1 . PHE A 153 ? 0.3442 0.3056 0.1890 -0.0247 0.0304 0.0864 153 PHE A CD1 1236 C CD2 . PHE A 153 ? 0.3185 0.2929 0.1738 -0.0229 0.0406 0.0929 153 PHE A CD2 1237 C CE1 . PHE A 153 ? 0.3004 0.2647 0.1584 -0.0347 0.0303 0.0880 153 PHE A CE1 1238 C CE2 . PHE A 153 ? 0.3060 0.2847 0.1754 -0.0310 0.0402 0.0954 153 PHE A CE2 1239 C CZ . PHE A 153 ? 0.3079 0.2830 0.1789 -0.0375 0.0349 0.0928 153 PHE A CZ 1240 N N . LEU A 154 ? 0.3479 0.3747 0.2813 0.0389 0.1516 -0.0113 154 LEU A N 1241 C CA . LEU A 154 ? 0.3551 0.3743 0.3045 0.0427 0.1624 -0.0036 154 LEU A CA 1242 C C . LEU A 154 ? 0.3345 0.3479 0.3137 0.0458 0.1701 -0.0015 154 LEU A C 1243 O O . LEU A 154 ? 0.3184 0.3239 0.2986 0.0455 0.1789 -0.0048 154 LEU A O 1244 C CB . LEU A 154 ? 0.4241 0.4370 0.3571 0.0414 0.1726 -0.0038 154 LEU A CB 1245 C CG . LEU A 154 ? 0.5483 0.5623 0.4684 0.0415 0.1723 0.0014 154 LEU A CG 1246 C CD1 . LEU A 154 ? 0.5939 0.6011 0.5001 0.0407 0.1842 0.0012 154 LEU A CD1 1247 C CD2 . LEU A 154 ? 0.5783 0.5893 0.5204 0.0457 0.1750 0.0107 154 LEU A CD2 1248 N N . PRO A 155 ? 0.3185 0.3362 0.3230 0.0489 0.1664 0.0043 155 PRO A N 1249 C CA . PRO A 155 ? 0.3211 0.3379 0.3582 0.0514 0.1700 0.0070 155 PRO A CA 1250 C C . PRO A 155 ? 0.4107 0.4187 0.4617 0.0522 0.1854 0.0101 155 PRO A C 1251 O O . PRO A 155 ? 0.4482 0.4530 0.4974 0.0521 0.1931 0.0145 155 PRO A O 1252 C CB . PRO A 155 ? 0.2904 0.3154 0.3500 0.0537 0.1627 0.0137 155 PRO A CB 1253 C CG . PRO A 155 ? 0.2509 0.2809 0.2852 0.0532 0.1524 0.0121 155 PRO A CG 1254 C CD . PRO A 155 ? 0.2932 0.3175 0.2967 0.0503 0.1575 0.0088 155 PRO A CD 1255 N N . SER A 156 ? 0.4340 0.4376 0.4986 0.0535 0.1905 0.0082 156 SER A N 1256 C CA . SER A 156 ? 0.4954 0.4911 0.5746 0.0552 0.2056 0.0111 156 SER A CA 1257 C C . SER A 156 ? 0.4902 0.4862 0.5978 0.0580 0.2066 0.0125 156 SER A C 1258 O O . SER A 156 ? 0.5210 0.5199 0.6290 0.0582 0.1973 0.0093 156 SER A O 1259 C CB . SER A 156 ? 0.5665 0.5508 0.6160 0.0537 0.2152 0.0048 156 SER A CB 1260 O OG . SER A 156 ? 0.6400 0.6196 0.6755 0.0526 0.2121 -0.0030 156 SER A OG 1261 N N . THR A 157 ? 0.4686 0.4624 0.6002 0.0604 0.2181 0.0180 157 THR A N 1262 C CA . THR A 157 ? 0.4222 0.4169 0.5817 0.0637 0.2202 0.0204 157 THR A CA 1263 C C . THR A 157 ? 0.4486 0.4296 0.5910 0.0650 0.2282 0.0136 157 THR A C 1264 O O . THR A 157 ? 0.3826 0.3621 0.5420 0.0681 0.2292 0.0144 157 THR A O 1265 C CB . THR A 157 ? 0.4356 0.4338 0.6269 0.0660 0.2304 0.0289 157 THR A CB 1266 O OG1 . THR A 157 ? 0.4933 0.4810 0.6694 0.0663 0.2462 0.0281 157 THR A OG1 1267 C CG2 . THR A 157 ? 0.3186 0.3298 0.5310 0.0639 0.2219 0.0359 157 THR A CG2 1268 N N . GLU A 158 ? 0.5615 0.5324 0.6699 0.0625 0.2337 0.0069 158 GLU A N 1269 C CA . GLU A 158 ? 0.6415 0.5971 0.7316 0.0630 0.2435 -0.0001 158 GLU A CA 1270 C C . GLU A 158 ? 0.6257 0.5777 0.6937 0.0600 0.2341 -0.0083 158 GLU A C 1271 O O . GLU A 158 ? 0.6883 0.6266 0.7449 0.0601 0.2411 -0.0140 158 GLU A O 1272 C CB . GLU A 158 ? 0.7301 0.6761 0.7959 0.0618 0.2555 -0.0031 158 GLU A CB 1273 C CG . GLU A 158 ? 0.8234 0.7702 0.9094 0.0650 0.2685 0.0046 158 GLU A CG 1274 C CD . GLU A 158 ? 0.8894 0.8350 1.0084 0.0704 0.2774 0.0097 158 GLU A CD 1275 O OE1 . GLU A 158 ? 0.9451 0.8779 1.0588 0.0733 0.2921 0.0073 158 GLU A OE1 1276 O OE2 . GLU A 158 ? 0.8816 0.8396 1.0318 0.0719 0.2697 0.0163 158 GLU A OE2 1277 N N . ASP A 159 ? 0.5363 0.4999 0.5982 0.0572 0.2188 -0.0087 159 ASP A N 1278 C CA . ASP A 159 ? 0.4816 0.4442 0.5222 0.0538 0.2094 -0.0160 159 ASP A CA 1279 C C . ASP A 159 ? 0.4597 0.4310 0.5197 0.0555 0.1980 -0.0135 159 ASP A C 1280 O O . ASP A 159 ? 0.4829 0.4672 0.5642 0.0575 0.1901 -0.0069 159 ASP A O 1281 C CB . ASP A 159 ? 0.4807 0.4505 0.4920 0.0490 0.2006 -0.0196 159 ASP A CB 1282 C CG . ASP A 159 ? 0.5280 0.4896 0.5153 0.0469 0.2101 -0.0232 159 ASP A CG 1283 O OD1 . ASP A 159 ? 0.5453 0.4923 0.5283 0.0476 0.2224 -0.0268 159 ASP A OD1 1284 O OD2 . ASP A 159 ? 0.5648 0.5344 0.5373 0.0449 0.2054 -0.0223 159 ASP A OD2 1285 N N . VAL A 160 ? 0.4482 0.4115 0.5002 0.0546 0.1973 -0.0187 160 VAL A N 1286 C CA . VAL A 160 ? 0.3090 0.2803 0.3724 0.0556 0.1855 -0.0174 160 VAL A CA 1287 C C . VAL A 160 ? 0.3069 0.2784 0.3397 0.0500 0.1778 -0.0252 160 VAL A C 1288 O O . VAL A 160 ? 0.4302 0.3916 0.4360 0.0453 0.1830 -0.0321 160 VAL A O 1289 C CB . VAL A 160 ? 0.3151 0.2779 0.4003 0.0600 0.1910 -0.0151 160 VAL A CB 1290 C CG1 . VAL A 160 ? 0.3188 0.2841 0.4350 0.0652 0.1982 -0.0069 160 VAL A CG1 1291 C CG2 . VAL A 160 ? 0.3424 0.2846 0.4061 0.0575 0.2020 -0.0230 160 VAL A CG2 1292 N N . TYR A 161 ? 0.2834 0.2674 0.3205 0.0501 0.1647 -0.0238 161 TYR A N 1293 C CA . TYR A 161 ? 0.3178 0.3051 0.3275 0.0446 0.1565 -0.0301 161 TYR A CA 1294 C C . TYR A 161 ? 0.2702 0.2576 0.2878 0.0455 0.1514 -0.0304 161 TYR A C 1295 O O . TYR A 161 ? 0.2570 0.2487 0.3031 0.0515 0.1488 -0.0241 161 TYR A O 1296 C CB . TYR A 161 ? 0.2946 0.2996 0.2938 0.0431 0.1448 -0.0286 161 TYR A CB 1297 C CG . TYR A 161 ? 0.3252 0.3301 0.3115 0.0415 0.1491 -0.0288 161 TYR A CG 1298 C CD1 . TYR A 161 ? 0.3358 0.3415 0.3414 0.0454 0.1543 -0.0224 161 TYR A CD1 1299 C CD2 . TYR A 161 ? 0.3340 0.3391 0.2898 0.0358 0.1476 -0.0346 161 TYR A CD2 1300 C CE1 . TYR A 161 ? 0.3241 0.3287 0.3175 0.0441 0.1593 -0.0220 161 TYR A CE1 1301 C CE2 . TYR A 161 ? 0.3386 0.3445 0.2831 0.0350 0.1512 -0.0341 161 TYR A CE2 1302 C CZ . TYR A 161 ? 0.3330 0.3376 0.2956 0.0391 0.1578 -0.0279 161 TYR A CZ 1303 O OH . TYR A 161 ? 0.3591 0.3633 0.3099 0.0383 0.1625 -0.0269 161 TYR A OH 1304 N N . ASP A 162 ? 0.2808 0.2640 0.2730 0.0392 0.1492 -0.0373 162 ASP A N 1305 C CA . ASP A 162 ? 0.2688 0.2530 0.2636 0.0389 0.1440 -0.0379 162 ASP A CA 1306 C C . ASP A 162 ? 0.2650 0.2592 0.2302 0.0310 0.1339 -0.0428 162 ASP A C 1307 O O . ASP A 162 ? 0.3206 0.3129 0.2611 0.0246 0.1337 -0.0478 162 ASP A O 1308 C CB . ASP A 162 ? 0.2912 0.2528 0.2879 0.0381 0.1558 -0.0414 162 ASP A CB 1309 C CG . ASP A 162 ? 0.3106 0.2646 0.3386 0.0466 0.1644 -0.0349 162 ASP A CG 1310 O OD1 . ASP A 162 ? 0.3025 0.2641 0.3578 0.0534 0.1590 -0.0276 162 ASP A OD1 1311 O OD2 . ASP A 162 ? 0.3162 0.2579 0.3414 0.0465 0.1757 -0.0366 162 ASP A OD2 1312 N N . CYS A 163 ? 0.2460 0.2526 0.2147 0.0319 0.1243 -0.0403 163 CYS A N 1313 C CA . CYS A 163 ? 0.2877 0.3032 0.2297 0.0238 0.1147 -0.0442 163 CYS A CA 1314 C C . CYS A 163 ? 0.3009 0.3019 0.2398 0.0190 0.1199 -0.0481 163 CYS A C 1315 O O . CYS A 163 ? 0.2834 0.2830 0.2441 0.0250 0.1202 -0.0432 163 CYS A O 1316 C CB . CYS A 163 ? 0.2189 0.2574 0.1632 0.0272 0.1010 -0.0389 163 CYS A CB 1317 S SG . CYS A 163 ? 0.3304 0.3772 0.2440 0.0190 0.0865 -0.0389 163 CYS A SG 1318 N N . ARG A 164 ? 0.3190 0.3097 0.2333 0.0084 0.1213 -0.0553 164 ARG A N 1319 C CA . ARG A 164 ? 0.3628 0.3363 0.2709 0.0014 0.1273 -0.0602 164 ARG A CA 1320 C C . ARG A 164 ? 0.3577 0.3462 0.2465 -0.0089 0.1136 -0.0613 164 ARG A C 1321 O O . ARG A 164 ? 0.2920 0.2906 0.1631 -0.0149 0.1037 -0.0624 164 ARG A O 1322 C CB . ARG A 164 ? 0.3285 0.2758 0.2238 -0.0047 0.1397 -0.0680 164 ARG A CB 1323 C CG . ARG A 164 ? 0.3784 0.3031 0.2659 -0.0124 0.1476 -0.0738 164 ARG A CG 1324 C CD . ARG A 164 ? 0.3928 0.2895 0.2665 -0.0184 0.1603 -0.0820 164 ARG A CD 1325 N NE . ARG A 164 ? 0.3974 0.3014 0.2448 -0.0297 0.1522 -0.0875 164 ARG A NE 1326 C CZ . ARG A 164 ? 0.4671 0.3570 0.3020 -0.0325 0.1595 -0.0930 164 ARG A CZ 1327 N NH1 . ARG A 164 ? 0.4403 0.3082 0.2855 -0.0253 0.1753 -0.0936 164 ARG A NH1 1328 N NH2 . ARG A 164 ? 0.4591 0.3581 0.2725 -0.0415 0.1509 -0.0970 164 ARG A NH2 1329 N N . VAL A 165 ? 0.2794 0.2710 0.1781 -0.0087 0.1085 -0.0571 165 VAL A N 1330 C CA . VAL A 165 ? 0.3012 0.3110 0.1859 -0.0177 0.0940 -0.0558 165 VAL A CA 1331 C C . VAL A 165 ? 0.3123 0.3045 0.1921 -0.0274 0.0968 -0.0582 165 VAL A C 1332 O O . VAL A 165 ? 0.3113 0.2890 0.2112 -0.0210 0.1001 -0.0528 165 VAL A O 1333 C CB . VAL A 165 ? 0.2752 0.3099 0.1778 -0.0080 0.0778 -0.0446 165 VAL A CB 1334 C CG1 . VAL A 165 ? 0.2504 0.3030 0.1406 -0.0163 0.0645 -0.0424 165 VAL A CG1 1335 C CG2 . VAL A 165 ? 0.2229 0.2741 0.1267 -0.0002 0.0741 -0.0428 165 VAL A CG2 1336 N N . GLU A 166 ? 0.3418 0.3359 0.1952 -0.0430 0.0952 -0.0657 166 GLU A N 1337 C CA . GLU A 166 ? 0.3250 0.3037 0.1719 -0.0547 0.0967 -0.0678 166 GLU A CA 1338 C C . GLU A 166 ? 0.3447 0.3515 0.1878 -0.0609 0.0803 -0.0618 166 GLU A C 1339 O O . GLU A 166 ? 0.2938 0.3255 0.1317 -0.0617 0.0680 -0.0599 166 GLU A O 1340 C CB . GLU A 166 ? 0.4861 0.4434 0.3061 -0.0701 0.1075 -0.0814 166 GLU A CB 1341 C CG . GLU A 166 ? 0.5850 0.5186 0.4065 -0.0636 0.1217 -0.0870 166 GLU A CG 1342 C CD . GLU A 166 ? 0.6744 0.5972 0.4760 -0.0761 0.1225 -0.0955 166 GLU A CD 1343 O OE1 . GLU A 166 ? 0.6714 0.6026 0.4601 -0.0905 0.1135 -0.0977 166 GLU A OE1 1344 O OE2 . GLU A 166 ? 0.7451 0.6518 0.5449 -0.0717 0.1322 -0.0995 166 GLU A OE2 1345 N N . HIS A 167 ? 0.2824 0.1451 0.2197 0.0197 0.0052 -0.0861 167 HIS A N 1346 C CA . HIS A 167 ? 0.2913 0.1563 0.2179 0.0150 0.0037 -0.0819 167 HIS A CA 1347 C C . HIS A 167 ? 0.2761 0.1326 0.2259 0.0208 0.0107 -0.0860 167 HIS A C 1348 O O . HIS A 167 ? 0.2875 0.1369 0.2606 0.0255 0.0261 -0.0828 167 HIS A O 1349 C CB . HIS A 167 ? 0.2646 0.1541 0.1985 0.0050 0.0115 -0.0778 167 HIS A CB 1350 C CG . HIS A 167 ? 0.2751 0.1792 0.2082 0.0042 0.0043 -0.0798 167 HIS A CG 1351 N ND1 . HIS A 167 ? 0.2985 0.1972 0.2393 0.0126 0.0071 -0.0799 167 HIS A ND1 1352 C CD2 . HIS A 167 ? 0.2652 0.1883 0.1933 0.0031 -0.0072 -0.0794 167 HIS A CD2 1353 C CE1 . HIS A 167 ? 0.2806 0.1940 0.2148 0.0127 -0.0010 -0.0791 167 HIS A CE1 1354 N NE2 . HIS A 167 ? 0.2822 0.2100 0.2096 0.0066 -0.0085 -0.0777 167 HIS A NE2 1355 N N . TRP A 168 ? 0.2692 0.1246 0.2199 0.0147 0.0115 -0.0899 168 TRP A N 1356 C CA . TRP A 168 ? 0.3834 0.2291 0.3634 0.0105 0.0329 -0.0911 168 TRP A CA 1357 C C . TRP A 168 ? 0.3548 0.1986 0.3554 0.0228 0.0463 -0.0795 168 TRP A C 1358 O O . TRP A 168 ? 0.3572 0.1875 0.3810 0.0251 0.0680 -0.0694 168 TRP A O 1359 C CB . TRP A 168 ? 0.3455 0.1932 0.3276 -0.0005 0.0322 -0.0983 168 TRP A CB 1360 C CG . TRP A 168 ? 0.3526 0.1968 0.3204 -0.0114 0.0216 -0.1056 168 TRP A CG 1361 C CD1 . TRP A 168 ? 0.3256 0.1542 0.2912 -0.0161 0.0275 -0.1098 168 TRP A CD1 1362 C CD2 . TRP A 168 ? 0.2994 0.1544 0.2559 -0.0190 0.0076 -0.1098 168 TRP A CD2 1363 N NE1 . TRP A 168 ? 0.3411 0.1695 0.2963 -0.0274 0.0190 -0.1194 168 TRP A NE1 1364 C CE2 . TRP A 168 ? 0.3244 0.1706 0.2764 -0.0294 0.0062 -0.1188 168 TRP A CE2 1365 C CE3 . TRP A 168 ? 0.2836 0.1568 0.2386 -0.0197 0.0015 -0.1094 168 TRP A CE3 1366 C CZ2 . TRP A 168 ? 0.3332 0.1873 0.2780 -0.0391 -0.0055 -0.1247 168 TRP A CZ2 1367 C CZ3 . TRP A 168 ? 0.2869 0.1688 0.2349 -0.0289 -0.0095 -0.1126 168 TRP A CZ3 1368 C CH2 . TRP A 168 ? 0.3110 0.1849 0.2563 -0.0389 -0.0131 -0.1208 168 TRP A CH2 1369 N N . GLY A 169 ? 0.2645 0.1198 0.2537 0.0327 0.0329 -0.0769 169 GLY A N 1370 C CA . GLY A 169 ? 0.3195 0.1730 0.3254 0.0489 0.0410 -0.0581 169 GLY A CA 1371 C C . GLY A 169 ? 0.3312 0.1821 0.3564 0.0575 0.0487 -0.0428 169 GLY A C 1372 O O . GLY A 169 ? 0.3269 0.1917 0.3685 0.0695 0.0482 -0.0153 169 GLY A O 1373 N N . LEU A 170 ? 0.3319 0.1798 0.3514 0.0490 0.0484 -0.0541 170 LEU A N 1374 C CA . LEU A 170 ? 0.3230 0.1696 0.3634 0.0569 0.0595 -0.0390 170 LEU A CA 1375 C C . LEU A 170 ? 0.3650 0.1972 0.4203 0.0537 0.0847 -0.0329 170 LEU A C 1376 O O . LEU A 170 ? 0.4016 0.2217 0.4415 0.0408 0.0876 -0.0484 170 LEU A O 1377 C CB . LEU A 170 ? 0.3310 0.1813 0.3528 0.0518 0.0463 -0.0518 170 LEU A CB 1378 C CG . LEU A 170 ? 0.3595 0.2194 0.3619 0.0538 0.0233 -0.0584 170 LEU A CG 1379 C CD1 . LEU A 170 ? 0.3436 0.2064 0.3185 0.0398 0.0216 -0.0659 170 LEU A CD1 1380 C CD2 . LEU A 170 ? 0.3046 0.1911 0.3284 0.0634 0.0120 -0.0268 170 LEU A CD2 1381 N N . ASP A 171 ? 0.4102 0.2457 0.4952 0.0661 0.1016 -0.0074 171 ASP A N 1382 C CA . ASP A 171 ? 0.5111 0.3299 0.6073 0.0652 0.1296 0.0004 171 ASP A CA 1383 C C . ASP A 171 ? 0.5155 0.3219 0.5995 0.0598 0.1368 -0.0091 171 ASP A C 1384 O O . ASP A 171 ? 0.6137 0.3970 0.6877 0.0532 0.1547 -0.0150 171 ASP A O 1385 C CB . ASP A 171 ? 0.5853 0.4181 0.7165 0.0813 0.1445 0.0342 171 ASP A CB 1386 C CG . ASP A 171 ? 0.6820 0.5210 0.8211 0.0861 0.1437 0.0456 171 ASP A CG 1387 O OD1 . ASP A 171 ? 0.7287 0.5517 0.8518 0.0760 0.1451 0.0282 171 ASP A OD1 1388 O OD2 . ASP A 171 ? 0.7282 0.5910 0.8894 0.0992 0.1402 0.0736 171 ASP A OD2 1389 N N . GLU A 172 ? 0.4481 0.2680 0.5315 0.0633 0.1231 -0.0094 172 GLU A N 1390 C CA . GLU A 172 ? 0.4678 0.2780 0.5383 0.0595 0.1280 -0.0173 172 GLU A CA 1391 C C . GLU A 172 ? 0.4234 0.2466 0.4741 0.0551 0.1001 -0.0332 172 GLU A C 1392 O O . GLU A 172 ? 0.3922 0.2307 0.4449 0.0582 0.0819 -0.0328 172 GLU A O 1393 C CB . GLU A 172 ? 0.5399 0.3545 0.6423 0.0725 0.1514 0.0098 172 GLU A CB 1394 C CG . GLU A 172 ? 0.6764 0.4756 0.7930 0.0773 0.1828 0.0261 172 GLU A CG 1395 C CD . GLU A 172 ? 0.7568 0.5363 0.8713 0.0800 0.2103 0.0330 172 GLU A CD 1396 O OE1 . GLU A 172 ? 0.7861 0.5739 0.9048 0.0830 0.2076 0.0362 172 GLU A OE1 1397 O OE2 . GLU A 172 ? 0.7930 0.5465 0.9003 0.0794 0.2362 0.0357 172 GLU A OE2 1398 N N . PRO A 173 ? 0.4103 0.2264 0.4396 0.0489 0.0966 -0.0458 173 PRO A N 1399 C CA . PRO A 173 ? 0.3689 0.1998 0.3794 0.0460 0.0700 -0.0582 173 PRO A CA 1400 C C . PRO A 173 ? 0.3402 0.1835 0.3735 0.0559 0.0694 -0.0443 173 PRO A C 1401 O O . PRO A 173 ? 0.3664 0.2115 0.4339 0.0660 0.0901 -0.0215 173 PRO A O 1402 C CB . PRO A 173 ? 0.3824 0.2013 0.3761 0.0406 0.0760 -0.0661 173 PRO A CB 1403 C CG . PRO A 173 ? 0.4240 0.2185 0.4131 0.0352 0.0969 -0.0672 173 PRO A CG 1404 C CD . PRO A 173 ? 0.4028 0.1963 0.4187 0.0438 0.1128 -0.0505 173 PRO A CD 1405 N N . LEU A 174 ? 0.3133 0.1674 0.3296 0.0537 0.0448 -0.0541 174 LEU A N 1406 C CA . LEU A 174 ? 0.2525 0.1164 0.2925 0.0622 0.0397 -0.0407 174 LEU A CA 1407 C C . LEU A 174 ? 0.3739 0.2366 0.4000 0.0587 0.0356 -0.0486 174 LEU A C 1408 O O . LEU A 174 ? 0.3706 0.2355 0.3528 0.0486 0.0171 -0.0659 174 LEU A O 1409 C CB . LEU A 174 ? 0.2348 0.1144 0.2549 0.0568 0.0101 -0.0456 174 LEU A CB 1410 C CG . LEU A 174 ? 0.3404 0.2573 0.3699 0.0548 -0.0187 -0.0205 174 LEU A CG 1411 C CD1 . LEU A 174 ? 0.2965 0.2370 0.3808 0.0652 -0.0093 0.0184 174 LEU A CD1 1412 C CD2 . LEU A 174 ? 0.3572 0.2814 0.3505 0.0489 -0.0446 -0.0262 174 LEU A CD2 1413 N N . LEU A 175 ? 0.3465 0.2174 0.4161 0.0687 0.0500 -0.0248 175 LEU A N 1414 C CA . LEU A 175 ? 0.2988 0.1679 0.3624 0.0666 0.0495 -0.0293 175 LEU A CA 1415 C C . LEU A 175 ? 0.2585 0.1661 0.3428 0.0615 0.0214 -0.0086 175 LEU A C 1416 O O . LEU A 175 ? 0.2824 0.2250 0.4134 0.0654 0.0162 0.0269 175 LEU A O 1417 C CB . LEU A 175 ? 0.3096 0.1753 0.3942 0.0721 0.0786 -0.0138 175 LEU A CB 1418 C CG . LEU A 175 ? 0.3295 0.1740 0.3742 0.0638 0.0870 -0.0330 175 LEU A CG 1419 C CD1 . LEU A 175 ? 0.3395 0.1746 0.3769 0.0611 0.0930 -0.0361 175 LEU A CD1 1420 C CD2 . LEU A 175 ? 0.3594 0.1953 0.4207 0.0696 0.1147 -0.0179 175 LEU A CD2 1421 N N . LYS A 176 ? 0.2519 0.1562 0.2956 0.0499 -0.0004 -0.0296 176 LYS A N 1422 C CA . LYS A 176 ? 0.2825 0.2192 0.3339 0.0393 -0.0295 -0.0124 176 LYS A CA 1423 C C . LYS A 176 ? 0.2983 0.2256 0.3524 0.0390 -0.0181 -0.0164 176 LYS A C 1424 O O . LYS A 176 ? 0.3325 0.2256 0.3445 0.0391 -0.0085 -0.0475 176 LYS A O 1425 C CB . LYS A 176 ? 0.2983 0.2357 0.2958 0.0259 -0.0645 -0.0299 176 LYS A CB 1426 C CG . LYS A 176 ? 0.3467 0.2957 0.3436 0.0270 -0.0764 -0.0201 176 LYS A CG 1427 C CD . LYS A 176 ? 0.3572 0.3444 0.4052 0.0270 -0.0874 0.0215 176 LYS A CD 1428 C CE . LYS A 176 ? 0.3685 0.3680 0.3952 0.0214 -0.1158 0.0315 176 LYS A CE 1429 N NZ . LYS A 176 ? 0.3317 0.3442 0.3969 0.0336 -0.1027 0.0545 176 LYS A NZ 1430 N N . HIS A 177 ? 0.2681 0.2284 0.3745 0.0386 -0.0198 0.0180 177 HIS A N 1431 C CA . HIS A 177 ? 0.2304 0.1866 0.3583 0.0423 -0.0004 0.0247 177 HIS A CA 1432 C C . HIS A 177 ? 0.2980 0.2648 0.4025 0.0241 -0.0303 0.0196 177 HIS A C 1433 O O . HIS A 177 ? 0.2921 0.2816 0.3846 0.0083 -0.0671 0.0266 177 HIS A O 1434 C CB . HIS A 177 ? 0.2323 0.2226 0.4406 0.0538 0.0186 0.0706 177 HIS A CB 1435 C CG . HIS A 177 ? 0.2765 0.2566 0.5138 0.0649 0.0519 0.0810 177 HIS A CG 1436 N ND1 . HIS A 177 ? 0.2822 0.2139 0.5050 0.0834 0.0958 0.0653 177 HIS A ND1 1437 C CD2 . HIS A 177 ? 0.2823 0.2917 0.5609 0.0601 0.0492 0.1067 177 HIS A CD2 1438 C CE1 . HIS A 177 ? 0.3465 0.2776 0.5937 0.0897 0.1195 0.0800 177 HIS A CE1 1439 N NE2 . HIS A 177 ? 0.3235 0.3024 0.6131 0.0784 0.0939 0.1070 177 HIS A NE2 1440 N N . TRP A 178 ? 0.3154 0.2594 0.4077 0.0267 -0.0126 0.0068 178 TRP A N 1441 C CA . TRP A 178 ? 0.2935 0.2490 0.3782 0.0109 -0.0336 0.0100 178 TRP A CA 1442 C C . TRP A 178 ? 0.2932 0.2462 0.4161 0.0199 -0.0029 0.0247 178 TRP A C 1443 O O . TRP A 178 ? 0.3211 0.2361 0.4316 0.0375 0.0341 0.0092 178 TRP A O 1444 C CB . TRP A 178 ? 0.2885 0.2101 0.2920 0.0015 -0.0510 -0.0306 178 TRP A CB 1445 C CG . TRP A 178 ? 0.3525 0.2795 0.3434 -0.0152 -0.0705 -0.0277 178 TRP A CG 1446 C CD1 . TRP A 178 ? 0.3533 0.2980 0.3279 -0.0365 -0.1094 -0.0196 178 TRP A CD1 1447 C CD2 . TRP A 178 ? 0.3677 0.2774 0.3579 -0.0126 -0.0510 -0.0325 178 TRP A CD2 1448 N NE1 . TRP A 178 ? 0.3544 0.2941 0.3194 -0.0492 -0.1161 -0.0194 178 TRP A NE1 1449 C CE2 . TRP A 178 ? 0.3671 0.2876 0.3439 -0.0342 -0.0800 -0.0267 178 TRP A CE2 1450 C CE3 . TRP A 178 ? 0.3807 0.2618 0.3754 0.0056 -0.0110 -0.0412 178 TRP A CE3 1451 C CZ2 . TRP A 178 ? 0.3929 0.3006 0.3663 -0.0378 -0.0696 -0.0285 178 TRP A CZ2 1452 C CZ3 . TRP A 178 ? 0.4189 0.2866 0.4082 0.0039 -0.0001 -0.0427 178 TRP A CZ3 1453 C CH2 . TRP A 178 ? 0.4186 0.3016 0.4001 -0.0177 -0.0289 -0.0360 178 TRP A CH2 1454 N N . GLU A 179 ? 0.2756 0.2663 0.4434 0.0074 -0.0175 0.0554 179 GLU A N 1455 C CA . GLU A 179 ? 0.3329 0.3227 0.5344 0.0133 0.0088 0.0698 179 GLU A CA 1456 C C . GLU A 179 ? 0.3323 0.3498 0.5461 -0.0111 -0.0211 0.0850 179 GLU A C 1457 O O . GLU A 179 ? 0.3287 0.3761 0.5430 -0.0330 -0.0629 0.0963 179 GLU A O 1458 C CB . GLU A 179 ? 0.3510 0.3645 0.6340 0.0339 0.0449 0.1100 179 GLU A CB 1459 C CG . GLU A 179 ? 0.3839 0.4641 0.7413 0.0237 0.0204 0.1576 179 GLU A CG 1460 C CD . GLU A 179 ? 0.4241 0.5261 0.8602 0.0485 0.0600 0.1982 179 GLU A CD 1461 O OE1 . GLU A 179 ? 0.4407 0.5073 0.8604 0.0707 0.0925 0.1853 179 GLU A OE1 1462 O OE2 . GLU A 179 ? 0.4658 0.6215 0.9816 0.0455 0.0580 0.2453 179 GLU A OE2 1463 N N . PHE A 180 ? 0.3513 0.3536 0.5701 -0.0079 0.0010 0.0845 180 PHE A N 1464 C CA . PHE A 180 ? 0.4221 0.4420 0.6483 -0.0314 -0.0221 0.0956 180 PHE A CA 1465 C C . PHE A 180 ? 0.4691 0.5556 0.7784 -0.0500 -0.0465 0.1465 180 PHE A C 1466 O O . PHE A 180 ? 0.4498 0.5717 0.8409 -0.0358 -0.0220 0.1857 180 PHE A O 1467 C CB . PHE A 180 ? 0.4470 0.4367 0.6710 -0.0191 0.0154 0.0893 180 PHE A CB 1468 C CG . PHE A 180 ? 0.4759 0.4762 0.7012 -0.0436 -0.0050 0.0970 180 PHE A CG 1469 C CD1 . PHE A 180 ? 0.4492 0.4176 0.5936 -0.0617 -0.0333 0.0625 180 PHE A CD1 1470 C CD2 . PHE A 180 ? 0.4952 0.5381 0.8048 -0.0488 0.0046 0.1415 180 PHE A CD2 1471 C CE1 . PHE A 180 ? 0.4717 0.4442 0.6132 -0.0856 -0.0513 0.0694 180 PHE A CE1 1472 C CE2 . PHE A 180 ? 0.5085 0.5610 0.8215 -0.0745 -0.0152 0.1497 180 PHE A CE2 1473 C CZ . PHE A 180 ? 0.4963 0.5107 0.7223 -0.0937 -0.0434 0.1124 180 PHE A CZ 1474 N N . ASP A 181 ? 0.5691 0.6702 0.8544 -0.0818 -0.0949 0.1468 181 ASP A N 1475 C CA . ASP A 181 ? 0.6605 0.8233 1.0127 -0.1065 -0.1296 0.1925 181 ASP A CA 1476 C C . ASP A 181 ? 0.7126 0.9143 1.1107 -0.0975 -0.1368 0.2199 181 ASP A C 1477 O O . ASP A 181 ? 0.7793 0.9775 1.1375 -0.1112 -0.1668 0.2225 181 ASP A O 1478 C CB . ASP A 181 ? 0.6779 0.8751 1.1124 -0.1081 -0.1093 0.2306 181 ASP A CB 1479 C CG . ASP A 181 ? 0.7302 0.9672 1.1981 -0.1236 -0.1392 0.2697 181 ASP A CG 1480 O OD1 . ASP A 181 ? 0.7883 1.0144 1.2006 -0.1419 -0.1764 0.2618 181 ASP A OD1 1481 O OD2 . ASP A 181 ? 0.7109 0.9788 1.2499 -0.1141 -0.1194 0.3066 181 ASP A OD2 1482 N N . ASP B 4 ? 0.7914 0.6602 0.7350 0.0965 0.0750 -0.1349 2 ASP B N 1483 C CA . ASP B 4 ? 0.7748 0.6372 0.7138 0.0873 0.0663 -0.1347 2 ASP B CA 1484 C C . ASP B 4 ? 0.7478 0.6039 0.7005 0.0897 0.0630 -0.1183 2 ASP B C 1485 O O . ASP B 4 ? 0.7229 0.5902 0.6761 0.0908 0.0618 -0.1054 2 ASP B O 1486 C CB . ASP B 4 ? 0.7621 0.6375 0.6827 0.0769 0.0646 -0.1345 2 ASP B CB 1487 C CG . ASP B 4 ? 0.7364 0.6050 0.6496 0.0651 0.0572 -0.1385 2 ASP B CG 1488 O OD1 . ASP B 4 ? 0.7128 0.5701 0.6390 0.0658 0.0515 -0.1388 2 ASP B OD1 1489 O OD2 . ASP B 4 ? 0.7423 0.6161 0.6340 0.0574 0.0548 -0.1402 2 ASP B OD2 1490 N N . THR B 5 ? 0.7239 0.5611 0.6850 0.0914 0.0611 -0.1181 3 THR B N 1491 C CA . THR B 5 ? 0.6647 0.4948 0.6386 0.0939 0.0590 -0.1023 3 THR B CA 1492 C C . THR B 5 ? 0.5928 0.4145 0.5618 0.0844 0.0526 -0.1007 3 THR B C 1493 O O . THR B 5 ? 0.5948 0.4087 0.5717 0.0854 0.0509 -0.0881 3 THR B O 1494 C CB . THR B 5 ? 0.6653 0.4792 0.6533 0.1023 0.0632 -0.0988 3 THR B CB 1495 O OG1 . THR B 5 ? 0.6718 0.4662 0.6545 0.0985 0.0645 -0.1112 3 THR B OG1 1496 C CG2 . THR B 5 ? 0.6557 0.4797 0.6519 0.1126 0.0694 -0.0986 3 THR B CG2 1497 N N . ARG B 6 ? 0.5240 0.3483 0.4800 0.0755 0.0486 -0.1134 4 ARG B N 1498 C CA . ARG B 6 ? 0.4928 0.3114 0.4449 0.0658 0.0421 -0.1134 4 ARG B CA 1499 C C . ARG B 6 ? 0.4699 0.2978 0.4229 0.0648 0.0398 -0.0986 4 ARG B C 1500 O O . ARG B 6 ? 0.4884 0.3320 0.4349 0.0684 0.0395 -0.0930 4 ARG B O 1501 C CB . ARG B 6 ? 0.4741 0.2995 0.4089 0.0579 0.0357 -0.1268 4 ARG B CB 1502 C CG . ARG B 6 ? 0.5024 0.3080 0.4245 0.0569 0.0374 -0.1395 4 ARG B CG 1503 C CD . ARG B 6 ? 0.5385 0.3472 0.4370 0.0469 0.0333 -0.1474 4 ARG B CD 1504 N NE . ARG B 6 ? 0.5354 0.3592 0.4173 0.0467 0.0381 -0.1442 4 ARG B NE 1505 C CZ . ARG B 6 ? 0.5053 0.3430 0.3748 0.0368 0.0346 -0.1496 4 ARG B CZ 1506 N NH1 . ARG B 6 ? 0.4926 0.3286 0.3598 0.0281 0.0247 -0.1557 4 ARG B NH1 1507 N NH2 . ARG B 6 ? 0.5137 0.3708 0.3760 0.0376 0.0377 -0.1491 4 ARG B NH2 1508 N N . PRO B 7 ? 0.4230 0.2396 0.3806 0.0609 0.0375 -0.0910 5 PRO B N 1509 C CA . PRO B 7 ? 0.3649 0.1878 0.3188 0.0612 0.0336 -0.0772 5 PRO B CA 1510 C C . PRO B 7 ? 0.3673 0.2066 0.3076 0.0552 0.0265 -0.0815 5 PRO B C 1511 O O . PRO B 7 ? 0.4008 0.2427 0.3367 0.0465 0.0239 -0.0938 5 PRO B O 1512 C CB . PRO B 7 ? 0.3681 0.1741 0.3292 0.0557 0.0344 -0.0717 5 PRO B CB 1513 C CG . PRO B 7 ? 0.3686 0.1629 0.3343 0.0490 0.0361 -0.0856 5 PRO B CG 1514 C CD . PRO B 7 ? 0.3966 0.1930 0.3614 0.0561 0.0388 -0.0942 5 PRO B CD 1515 N N . ARG B 8 ? 0.2815 0.1385 0.2206 0.0583 0.0220 -0.0696 6 ARG B N 1516 C CA . ARG B 8 ? 0.2640 0.1403 0.1951 0.0528 0.0148 -0.0697 6 ARG B CA 1517 C C . ARG B 8 ? 0.2684 0.1496 0.2036 0.0469 0.0095 -0.0603 6 ARG B C 1518 O O . ARG B 8 ? 0.2736 0.1485 0.2151 0.0496 0.0108 -0.0499 6 ARG B O 1519 C CB . ARG B 8 ? 0.2525 0.1455 0.1803 0.0597 0.0150 -0.0648 6 ARG B CB 1520 C CG . ARG B 8 ? 0.2614 0.1602 0.1771 0.0604 0.0170 -0.0757 6 ARG B CG 1521 C CD . ARG B 8 ? 0.3610 0.2465 0.2783 0.0622 0.0247 -0.0858 6 ARG B CD 1522 N NE . ARG B 8 ? 0.2946 0.1883 0.2005 0.0593 0.0266 -0.0953 6 ARG B NE 1523 C CZ . ARG B 8 ? 0.3154 0.2018 0.2210 0.0598 0.0340 -0.1055 6 ARG B CZ 1524 N NH1 . ARG B 8 ? 0.3261 0.1976 0.2457 0.0635 0.0398 -0.1075 6 ARG B NH1 1525 N NH2 . ARG B 8 ? 0.3274 0.2213 0.2189 0.0570 0.0356 -0.1132 6 ARG B NH2 1526 N N . PHE B 9 ? 0.2393 0.1320 0.1702 0.0396 0.0036 -0.0638 7 PHE B N 1527 C CA . PHE B 9 ? 0.3027 0.2016 0.2376 0.0341 -0.0005 -0.0562 7 PHE B CA 1528 C C . PHE B 9 ? 0.3143 0.2328 0.2444 0.0332 -0.0062 -0.0547 7 PHE B C 1529 O O . PHE B 9 ? 0.3197 0.2449 0.2433 0.0315 -0.0091 -0.0627 7 PHE B O 1530 C CB . PHE B 9 ? 0.2343 0.1242 0.1747 0.0247 -0.0006 -0.0629 7 PHE B CB 1531 C CG . PHE B 9 ? 0.2550 0.1226 0.2010 0.0247 0.0063 -0.0660 7 PHE B CG 1532 C CD1 . PHE B 9 ? 0.2593 0.1148 0.2111 0.0256 0.0109 -0.0552 7 PHE B CD1 1533 C CD2 . PHE B 9 ? 0.2730 0.1310 0.2175 0.0242 0.0087 -0.0797 7 PHE B CD2 1534 C CE1 . PHE B 9 ? 0.3250 0.1578 0.2829 0.0262 0.0183 -0.0564 7 PHE B CE1 1535 C CE2 . PHE B 9 ? 0.3088 0.1441 0.2605 0.0243 0.0161 -0.0830 7 PHE B CE2 1536 C CZ . PHE B 9 ? 0.3316 0.1537 0.2909 0.0254 0.0212 -0.0706 7 PHE B CZ 1537 N N . LEU B 10 ? 0.3070 0.2343 0.2397 0.0345 -0.0080 -0.0445 8 LEU B N 1538 C CA . LEU B 10 ? 0.2629 0.2067 0.1932 0.0348 -0.0118 -0.0418 8 LEU B CA 1539 C C . LEU B 10 ? 0.2559 0.2060 0.1909 0.0295 -0.0152 -0.0374 8 LEU B C 1540 O O . LEU B 10 ? 0.2973 0.2434 0.2357 0.0289 -0.0138 -0.0315 8 LEU B O 1541 C CB . LEU B 10 ? 0.2393 0.1892 0.1705 0.0419 -0.0099 -0.0351 8 LEU B CB 1542 C CG . LEU B 10 ? 0.2187 0.1836 0.1498 0.0421 -0.0121 -0.0313 8 LEU B CG 1543 C CD1 . LEU B 10 ? 0.2068 0.1762 0.1292 0.0428 -0.0119 -0.0364 8 LEU B CD1 1544 C CD2 . LEU B 10 ? 0.1880 0.1590 0.1254 0.0471 -0.0103 -0.0246 8 LEU B CD2 1545 N N . GLU B 11 ? 0.1817 0.1421 0.1161 0.0263 -0.0192 -0.0400 9 GLU B N 1546 C CA . GLU B 11 ? 0.1904 0.1587 0.1307 0.0226 -0.0216 -0.0361 9 GLU B CA 1547 C C . GLU B 11 ? 0.1853 0.1650 0.1248 0.0261 -0.0231 -0.0313 9 GLU B C 1548 O O . GLU B 11 ? 0.1548 0.1392 0.0885 0.0289 -0.0241 -0.0327 9 GLU B O 1549 C CB . GLU B 11 ? 0.2207 0.1926 0.1654 0.0167 -0.0253 -0.0424 9 GLU B CB 1550 C CG . GLU B 11 ? 0.2181 0.1995 0.1713 0.0136 -0.0272 -0.0392 9 GLU B CG 1551 C CD . GLU B 11 ? 0.2814 0.2566 0.2410 0.0095 -0.0228 -0.0366 9 GLU B CD 1552 O OE1 . GLU B 11 ? 0.2259 0.1888 0.1836 0.0086 -0.0189 -0.0370 9 GLU B OE1 1553 O OE2 . GLU B 11 ? 0.3383 0.3201 0.3044 0.0076 -0.0224 -0.0340 9 GLU B OE2 1554 N N . GLN B 12 ? 0.1671 0.1505 0.1116 0.0257 -0.0225 -0.0257 10 GLN B N 1555 C CA . GLN B 12 ? 0.1989 0.1916 0.1459 0.0276 -0.0231 -0.0217 10 GLN B CA 1556 C C . GLN B 12 ? 0.2154 0.2127 0.1697 0.0241 -0.0242 -0.0205 10 GLN B C 1557 O O . GLN B 12 ? 0.2030 0.1968 0.1599 0.0207 -0.0231 -0.0212 10 GLN B O 1558 C CB . GLN B 12 ? 0.2159 0.2097 0.1645 0.0310 -0.0209 -0.0176 10 GLN B CB 1559 C CG . GLN B 12 ? 0.2154 0.2054 0.1601 0.0356 -0.0186 -0.0182 10 GLN B CG 1560 C CD . GLN B 12 ? 0.1847 0.1803 0.1354 0.0389 -0.0170 -0.0142 10 GLN B CD 1561 O OE1 . GLN B 12 ? 0.2227 0.2257 0.1778 0.0392 -0.0159 -0.0119 10 GLN B OE1 1562 N NE2 . GLN B 12 ? 0.1351 0.1275 0.0875 0.0415 -0.0171 -0.0130 10 GLN B NE2 1563 N N . VAL B 13 ? 0.1571 0.1617 0.1148 0.0253 -0.0253 -0.0181 11 VAL B N 1564 C CA . VAL B 13 ? 0.1492 0.1579 0.1161 0.0233 -0.0251 -0.0167 11 VAL B CA 1565 C C . VAL B 13 ? 0.1644 0.1764 0.1353 0.0258 -0.0232 -0.0122 11 VAL B C 1566 O O . VAL B 13 ? 0.1624 0.1766 0.1300 0.0292 -0.0231 -0.0090 11 VAL B O 1567 C CB . VAL B 13 ? 0.1055 0.1195 0.0772 0.0224 -0.0286 -0.0181 11 VAL B CB 1568 C CG1 . VAL B 13 ? 0.1462 0.1637 0.1299 0.0208 -0.0270 -0.0172 11 VAL B CG1 1569 C CG2 . VAL B 13 ? 0.1110 0.1225 0.0812 0.0189 -0.0306 -0.0238 11 VAL B CG2 1570 N N . LYS B 14 ? 0.1649 0.1768 0.1425 0.0238 -0.0211 -0.0123 12 LYS B N 1571 C CA . LYS B 14 ? 0.1720 0.1860 0.1570 0.0248 -0.0187 -0.0094 12 LYS B CA 1572 C C . LYS B 14 ? 0.1735 0.1881 0.1687 0.0229 -0.0170 -0.0106 12 LYS B C 1573 O O . LYS B 14 ? 0.1588 0.1719 0.1550 0.0198 -0.0159 -0.0149 12 LYS B O 1574 C CB . LYS B 14 ? 0.1411 0.1550 0.1263 0.0240 -0.0176 -0.0105 12 LYS B CB 1575 C CG . LYS B 14 ? 0.1504 0.1644 0.1292 0.0270 -0.0179 -0.0090 12 LYS B CG 1576 C CD . LYS B 14 ? 0.1552 0.1719 0.1381 0.0269 -0.0178 -0.0099 12 LYS B CD 1577 C CE . LYS B 14 ? 0.1614 0.1790 0.1411 0.0309 -0.0169 -0.0082 12 LYS B CE 1578 N NZ . LYS B 14 ? 0.0964 0.1195 0.0835 0.0315 -0.0179 -0.0087 12 LYS B NZ 1579 N N . HIS B 15 ? 0.1864 0.2027 0.1886 0.0255 -0.0163 -0.0062 13 HIS B N 1580 C CA . HIS B 15 ? 0.1715 0.1875 0.1861 0.0251 -0.0138 -0.0068 13 HIS B CA 1581 C C . HIS B 15 ? 0.1497 0.1626 0.1726 0.0246 -0.0094 -0.0055 13 HIS B C 1582 O O . HIS B 15 ? 0.1863 0.1986 0.2116 0.0275 -0.0078 0.0012 13 HIS B O 1583 C CB . HIS B 15 ? 0.0954 0.1151 0.1148 0.0293 -0.0161 -0.0017 13 HIS B CB 1584 C CG . HIS B 15 ? 0.1773 0.2017 0.1884 0.0299 -0.0218 -0.0027 13 HIS B CG 1585 N ND1 . HIS B 15 ? 0.1997 0.2274 0.2155 0.0273 -0.0234 -0.0076 13 HIS B ND1 1586 C CD2 . HIS B 15 ? 0.1825 0.2089 0.1819 0.0321 -0.0257 -0.0006 13 HIS B CD2 1587 C CE1 . HIS B 15 ? 0.1891 0.2204 0.1979 0.0274 -0.0288 -0.0088 13 HIS B CE1 1588 N NE2 . HIS B 15 ? 0.1650 0.1954 0.1626 0.0305 -0.0305 -0.0051 13 HIS B NE2 1589 N N . GLU B 16 ? 0.1614 0.1722 0.1884 0.0205 -0.0071 -0.0123 14 GLU B N 1590 C CA . GLU B 16 ? 0.1816 0.1903 0.2172 0.0182 -0.0038 -0.0139 14 GLU B CA 1591 C C . GLU B 16 ? 0.2140 0.2179 0.2640 0.0170 0.0012 -0.0170 14 GLU B C 1592 O O . GLU B 16 ? 0.2310 0.2341 0.2818 0.0159 0.0023 -0.0228 14 GLU B O 1593 C CB . GLU B 16 ? 0.1694 0.1804 0.1987 0.0143 -0.0062 -0.0206 14 GLU B CB 1594 C CG . GLU B 16 ? 0.1832 0.1975 0.1997 0.0161 -0.0105 -0.0180 14 GLU B CG 1595 C CD . GLU B 16 ? 0.1930 0.2106 0.2056 0.0138 -0.0135 -0.0229 14 GLU B CD 1596 O OE1 . GLU B 16 ? 0.2361 0.2544 0.2533 0.0102 -0.0134 -0.0295 14 GLU B OE1 1597 O OE2 . GLU B 16 ? 0.2345 0.2544 0.2397 0.0161 -0.0164 -0.0204 14 GLU B OE2 1598 N N . CYS B 17 ? 0.2135 0.2136 0.2759 0.0173 0.0055 -0.0134 15 CYS B N 1599 C CA . CYS B 17 ? 0.1900 0.1831 0.2685 0.0159 0.0114 -0.0171 15 CYS B CA 1600 C C . CYS B 17 ? 0.1596 0.1508 0.2472 0.0099 0.0140 -0.0237 15 CYS B C 1601 O O . CYS B 17 ? 0.1560 0.1477 0.2482 0.0095 0.0154 -0.0182 15 CYS B O 1602 C CB . CYS B 17 ? 0.1347 0.1230 0.2235 0.0218 0.0152 -0.0057 15 CYS B CB 1603 S SG . CYS B 17 ? 0.2638 0.2571 0.3476 0.0289 0.0109 0.0005 15 CYS B SG 1604 N N . HIS B 18 ? 0.1543 0.1440 0.2446 0.0050 0.0147 -0.0363 16 HIS B N 1605 C CA . HIS B 18 ? 0.1730 0.1629 0.2724 -0.0018 0.0153 -0.0456 16 HIS B CA 1606 C C . HIS B 18 ? 0.1956 0.1749 0.3144 -0.0044 0.0232 -0.0516 16 HIS B C 1607 O O . HIS B 18 ? 0.2174 0.1917 0.3369 -0.0036 0.0262 -0.0575 16 HIS B O 1608 C CB . HIS B 18 ? 0.1643 0.1614 0.2493 -0.0057 0.0089 -0.0570 16 HIS B CB 1609 C CG . HIS B 18 ? 0.2100 0.2157 0.2781 -0.0031 0.0018 -0.0514 16 HIS B CG 1610 N ND1 . HIS B 18 ? 0.2697 0.2838 0.3364 -0.0054 -0.0037 -0.0534 16 HIS B ND1 1611 C CD2 . HIS B 18 ? 0.1772 0.1842 0.2313 0.0016 -0.0004 -0.0444 16 HIS B CD2 1612 C CE1 . HIS B 18 ? 0.2360 0.2547 0.2879 -0.0015 -0.0083 -0.0473 16 HIS B CE1 1613 N NE2 . HIS B 18 ? 0.1569 0.1708 0.2006 0.0023 -0.0063 -0.0422 16 HIS B NE2 1614 N N . PHE B 19 ? 0.1792 0.1543 0.3155 -0.0078 0.0276 -0.0502 17 PHE B N 1615 C CA . PHE B 19 ? 0.2092 0.1714 0.3670 -0.0100 0.0366 -0.0540 17 PHE B CA 1616 C C . PHE B 19 ? 0.2123 0.1742 0.3829 -0.0199 0.0371 -0.0702 17 PHE B C 1617 O O . PHE B 19 ? 0.2500 0.2206 0.4237 -0.0247 0.0332 -0.0719 17 PHE B O 1618 C CB . PHE B 19 ? 0.2182 0.1723 0.3893 -0.0055 0.0438 -0.0375 17 PHE B CB 1619 C CG . PHE B 19 ? 0.2534 0.2087 0.4123 0.0045 0.0421 -0.0221 17 PHE B CG 1620 C CD1 . PHE B 19 ? 0.2416 0.2066 0.3841 0.0078 0.0365 -0.0127 17 PHE B CD1 1621 C CD2 . PHE B 19 ? 0.2498 0.1974 0.4148 0.0107 0.0459 -0.0181 17 PHE B CD2 1622 C CE1 . PHE B 19 ? 0.2372 0.2043 0.3681 0.0162 0.0339 -0.0006 17 PHE B CE1 1623 C CE2 . PHE B 19 ? 0.2603 0.2117 0.4156 0.0196 0.0426 -0.0050 17 PHE B CE2 1624 C CZ . PHE B 19 ? 0.2480 0.2093 0.3855 0.0220 0.0362 0.0033 17 PHE B CZ 1625 N N . PHE B 20 ? 0.2481 0.2008 0.4274 -0.0229 0.0419 -0.0830 18 PHE B N 1626 C CA . PHE B 20 ? 0.3516 0.3083 0.5379 -0.0311 0.0414 -0.0973 18 PHE B CA 1627 C C . PHE B 20 ? 0.3539 0.2989 0.5600 -0.0309 0.0521 -0.0959 18 PHE B C 1628 O O . PHE B 20 ? 0.3460 0.2839 0.5514 -0.0256 0.0571 -0.0931 18 PHE B O 1629 C CB . PHE B 20 ? 0.4232 0.3880 0.5888 -0.0330 0.0351 -0.1113 18 PHE B CB 1630 C CG . PHE B 20 ? 0.4751 0.4502 0.6174 -0.0310 0.0256 -0.1107 18 PHE B CG 1631 C CD1 . PHE B 20 ? 0.4676 0.4401 0.5980 -0.0239 0.0262 -0.1023 18 PHE B CD1 1632 C CD2 . PHE B 20 ? 0.5044 0.4931 0.6364 -0.0353 0.0157 -0.1175 18 PHE B CD2 1633 C CE1 . PHE B 20 ? 0.4262 0.4099 0.5331 -0.0212 0.0180 -0.0983 18 PHE B CE1 1634 C CE2 . PHE B 20 ? 0.4903 0.4885 0.6006 -0.0326 0.0071 -0.1155 18 PHE B CE2 1635 C CZ . PHE B 20 ? 0.4396 0.4348 0.5364 -0.0254 0.0089 -0.1047 18 PHE B CZ 1636 N N . ASN B 21 ? 0.4060 0.3498 0.6309 -0.0363 0.0559 -0.0977 19 ASN B N 1637 C CA . ASN B 21 ? 0.4616 0.3939 0.7067 -0.0365 0.0666 -0.0969 19 ASN B CA 1638 C C . ASN B 21 ? 0.4195 0.3402 0.6708 -0.0276 0.0745 -0.0785 19 ASN B C 1639 O O . ASN B 21 ? 0.4290 0.3432 0.6817 -0.0234 0.0789 -0.0782 19 ASN B O 1640 C CB . ASN B 21 ? 0.5778 0.5099 0.8185 -0.0394 0.0668 -0.1134 19 ASN B CB 1641 C CG . ASN B 21 ? 0.6811 0.6016 0.9440 -0.0408 0.0777 -0.1158 19 ASN B CG 1642 O OD1 . ASN B 21 ? 0.6417 0.5549 0.9240 -0.0404 0.0849 -0.1059 19 ASN B OD1 1643 N ND2 . ASN B 21 ? 0.8269 0.7452 1.0864 -0.0422 0.0795 -0.1287 19 ASN B ND2 1644 N N . GLY B 22 ? 0.3787 0.2978 0.6329 -0.0244 0.0759 -0.0623 20 GLY B N 1645 C CA . GLY B 22 ? 0.3670 0.2779 0.6214 -0.0146 0.0808 -0.0428 20 GLY B CA 1646 C C . GLY B 22 ? 0.3822 0.2968 0.6174 -0.0076 0.0741 -0.0406 20 GLY B C 1647 O O . GLY B 22 ? 0.4006 0.3229 0.6206 -0.0080 0.0662 -0.0431 20 GLY B O 1648 N N . THR B 23 ? 0.3655 0.2752 0.6027 -0.0011 0.0774 -0.0360 21 THR B N 1649 C CA . THR B 23 ? 0.3167 0.2315 0.5390 0.0053 0.0717 -0.0353 21 THR B CA 1650 C C . THR B 23 ? 0.3286 0.2443 0.5505 0.0023 0.0730 -0.0514 21 THR B C 1651 O O . THR B 23 ? 0.3018 0.2203 0.5175 0.0078 0.0717 -0.0504 21 THR B O 1652 C CB . THR B 23 ? 0.3075 0.2198 0.5308 0.0163 0.0729 -0.0160 21 THR B CB 1653 O OG1 . THR B 23 ? 0.2825 0.1853 0.5236 0.0176 0.0816 -0.0114 21 THR B OG1 1654 C CG2 . THR B 23 ? 0.3337 0.2480 0.5491 0.0207 0.0700 0.0004 21 THR B CG2 1655 N N . GLU B 24 ? 0.3371 0.2514 0.5657 -0.0062 0.0757 -0.0661 22 GLU B N 1656 C CA . GLU B 24 ? 0.3821 0.2967 0.6089 -0.0093 0.0779 -0.0817 22 GLU B CA 1657 C C . GLU B 24 ? 0.3607 0.2854 0.5645 -0.0100 0.0707 -0.0907 22 GLU B C 1658 O O . GLU B 24 ? 0.3316 0.2569 0.5302 -0.0076 0.0728 -0.0954 22 GLU B O 1659 C CB . GLU B 24 ? 0.4778 0.3903 0.7150 -0.0183 0.0809 -0.0957 22 GLU B CB 1660 C CG . GLU B 24 ? 0.5651 0.4657 0.8269 -0.0177 0.0913 -0.0911 22 GLU B CG 1661 C CD . GLU B 24 ? 0.6436 0.5376 0.9116 -0.0130 0.0979 -0.0924 22 GLU B CD 1662 O OE1 . GLU B 24 ? 0.6618 0.5576 0.9238 -0.0168 0.0984 -0.1084 22 GLU B OE1 1663 O OE2 . GLU B 24 ? 0.6596 0.5471 0.9380 -0.0053 0.1025 -0.0771 22 GLU B OE2 1664 N N . ARG B 25 ? 0.3724 0.3049 0.5627 -0.0133 0.0627 -0.0926 23 ARG B N 1665 C CA . ARG B 25 ? 0.4079 0.3500 0.5748 -0.0135 0.0557 -0.0990 23 ARG B CA 1666 C C . ARG B 25 ? 0.3837 0.3299 0.5425 -0.0095 0.0496 -0.0880 23 ARG B C 1667 O O . ARG B 25 ? 0.3766 0.3232 0.5402 -0.0118 0.0470 -0.0841 23 ARG B O 1668 C CB . ARG B 25 ? 0.5090 0.4579 0.6642 -0.0218 0.0508 -0.1148 23 ARG B CB 1669 C CG . ARG B 25 ? 0.6420 0.6020 0.7714 -0.0228 0.0416 -0.1185 23 ARG B CG 1670 C CD . ARG B 25 ? 0.7522 0.7135 0.8664 -0.0182 0.0435 -0.1180 23 ARG B CD 1671 N NE . ARG B 25 ? 0.8014 0.7723 0.8897 -0.0194 0.0358 -0.1209 23 ARG B NE 1672 C CZ . ARG B 25 ? 0.7835 0.7573 0.8570 -0.0154 0.0360 -0.1169 23 ARG B CZ 1673 N NH1 . ARG B 25 ? 0.7410 0.7106 0.8245 -0.0101 0.0428 -0.1109 23 ARG B NH1 1674 N NH2 . ARG B 25 ? 0.7676 0.7491 0.8173 -0.0166 0.0294 -0.1182 23 ARG B NH2 1675 N N . VAL B 26 ? 0.3356 0.2854 0.4835 -0.0034 0.0480 -0.0833 24 VAL B N 1676 C CA . VAL B 26 ? 0.3009 0.2577 0.4387 0.0013 0.0416 -0.0703 24 VAL B CA 1677 C C . VAL B 26 ? 0.2541 0.2214 0.3692 0.0014 0.0358 -0.0731 24 VAL B C 1678 O O . VAL B 26 ? 0.2355 0.2022 0.3478 0.0024 0.0399 -0.0797 24 VAL B O 1679 C CB . VAL B 26 ? 0.2974 0.2509 0.4466 0.0103 0.0444 -0.0543 24 VAL B CB 1680 C CG1 . VAL B 26 ? 0.2801 0.2438 0.4150 0.0143 0.0363 -0.0409 24 VAL B CG1 1681 C CG2 . VAL B 26 ? 0.3044 0.2454 0.4756 0.0114 0.0514 -0.0486 24 VAL B CG2 1682 N N . ARG B 27 ? 0.2196 0.1956 0.3196 0.0006 0.0277 -0.0675 25 ARG B N 1683 C CA . ARG B 27 ? 0.2263 0.2103 0.3056 0.0011 0.0228 -0.0675 25 ARG B CA 1684 C C . ARG B 27 ? 0.2005 0.1899 0.2741 0.0059 0.0177 -0.0536 25 ARG B C 1685 O O . ARG B 27 ? 0.1973 0.1878 0.2731 0.0068 0.0148 -0.0461 25 ARG B O 1686 C CB . ARG B 27 ? 0.2661 0.2553 0.3298 -0.0044 0.0171 -0.0762 25 ARG B CB 1687 C CG . ARG B 27 ? 0.2739 0.2691 0.3153 -0.0038 0.0131 -0.0756 25 ARG B CG 1688 C CD . ARG B 27 ? 0.3143 0.3142 0.3403 -0.0083 0.0077 -0.0846 25 ARG B CD 1689 N NE . ARG B 27 ? 0.4396 0.4439 0.4437 -0.0068 0.0038 -0.0808 25 ARG B NE 1690 C CZ . ARG B 27 ? 0.5632 0.5725 0.5498 -0.0087 -0.0020 -0.0854 25 ARG B CZ 1691 N NH1 . ARG B 27 ? 0.6489 0.6615 0.6377 -0.0128 -0.0058 -0.0957 25 ARG B NH1 1692 N NH2 . ARG B 27 ? 0.5761 0.5871 0.5436 -0.0064 -0.0042 -0.0796 25 ARG B NH2 1693 N N . PHE B 28 ? 0.1896 0.1825 0.2566 0.0086 0.0174 -0.0509 26 PHE B N 1694 C CA . PHE B 28 ? 0.1717 0.1698 0.2335 0.0126 0.0123 -0.0402 26 PHE B CA 1695 C C . PHE B 28 ? 0.1995 0.2020 0.2427 0.0104 0.0083 -0.0418 26 PHE B C 1696 O O . PHE B 28 ? 0.2676 0.2702 0.3047 0.0083 0.0114 -0.0478 26 PHE B O 1697 C CB . PHE B 28 ? 0.1726 0.1720 0.2467 0.0176 0.0146 -0.0351 26 PHE B CB 1698 C CG . PHE B 28 ? 0.1028 0.1093 0.1702 0.0203 0.0086 -0.0278 26 PHE B CG 1699 C CD1 . PHE B 28 ? 0.1515 0.1598 0.2143 0.0230 0.0033 -0.0192 26 PHE B CD1 1700 C CD2 . PHE B 28 ? 0.1071 0.1184 0.1731 0.0196 0.0090 -0.0304 26 PHE B CD2 1701 C CE1 . PHE B 28 ? 0.1357 0.1503 0.1915 0.0250 -0.0025 -0.0147 26 PHE B CE1 1702 C CE2 . PHE B 28 ? 0.1096 0.1274 0.1716 0.0209 0.0033 -0.0254 26 PHE B CE2 1703 C CZ . PHE B 28 ? 0.1129 0.1321 0.1691 0.0236 -0.0030 -0.0183 26 PHE B CZ 1704 N N . LEU B 29 ? 0.1925 0.1979 0.2269 0.0113 0.0025 -0.0358 27 LEU B N 1705 C CA . LEU B 29 ? 0.1784 0.1860 0.1968 0.0102 -0.0009 -0.0356 27 LEU B CA 1706 C C . LEU B 29 ? 0.1671 0.1772 0.1835 0.0131 -0.0045 -0.0285 27 LEU B C 1707 O O . LEU B 29 ? 0.1926 0.2037 0.2105 0.0157 -0.0073 -0.0230 27 LEU B O 1708 C CB . LEU B 29 ? 0.1970 0.2055 0.2057 0.0085 -0.0049 -0.0372 27 LEU B CB 1709 C CG . LEU B 29 ? 0.2218 0.2301 0.2296 0.0048 -0.0040 -0.0460 27 LEU B CG 1710 C CD1 . LEU B 29 ? 0.2047 0.2174 0.2049 0.0041 -0.0101 -0.0463 27 LEU B CD1 1711 C CD2 . LEU B 29 ? 0.2308 0.2373 0.2296 0.0028 -0.0001 -0.0523 27 LEU B CD2 1712 N N . ASP B 30 ? 0.1370 0.1480 0.1501 0.0122 -0.0038 -0.0291 28 ASP B N 1713 C CA . ASP B 30 ? 0.1438 0.1573 0.1550 0.0137 -0.0077 -0.0249 28 ASP B CA 1714 C C . ASP B 30 ? 0.1527 0.1629 0.1495 0.0116 -0.0090 -0.0254 28 ASP B C 1715 O O . ASP B 30 ? 0.1280 0.1360 0.1202 0.0088 -0.0055 -0.0278 28 ASP B O 1716 C CB . ASP B 30 ? 0.1295 0.1473 0.1518 0.0134 -0.0059 -0.0258 28 ASP B CB 1717 C CG . ASP B 30 ? 0.2047 0.2281 0.2314 0.0161 -0.0117 -0.0220 28 ASP B CG 1718 O OD1 . ASP B 30 ? 0.1997 0.2239 0.2252 0.0199 -0.0153 -0.0174 28 ASP B OD1 1719 O OD2 . ASP B 30 ? 0.1912 0.2186 0.2225 0.0142 -0.0126 -0.0237 28 ASP B OD2 1720 N N . ARG B 31 ? 0.1510 0.1603 0.1409 0.0136 -0.0129 -0.0224 29 ARG B N 1721 C CA . ARG B 31 ? 0.1414 0.1466 0.1190 0.0131 -0.0140 -0.0220 29 ARG B CA 1722 C C . ARG B 31 ? 0.1554 0.1584 0.1291 0.0142 -0.0164 -0.0202 29 ARG B C 1723 O O . ARG B 31 ? 0.1538 0.1594 0.1296 0.0167 -0.0190 -0.0187 29 ARG B O 1724 C CB . ARG B 31 ? 0.2052 0.2116 0.1801 0.0147 -0.0160 -0.0215 29 ARG B CB 1725 C CG . ARG B 31 ? 0.1796 0.1884 0.1606 0.0129 -0.0143 -0.0252 29 ARG B CG 1726 C CD . ARG B 31 ? 0.1283 0.1404 0.1104 0.0136 -0.0171 -0.0255 29 ARG B CD 1727 N NE . ARG B 31 ? 0.1349 0.1472 0.1057 0.0141 -0.0204 -0.0257 29 ARG B NE 1728 C CZ . ARG B 31 ? 0.1533 0.1705 0.1250 0.0156 -0.0243 -0.0255 29 ARG B CZ 1729 N NH1 . ARG B 31 ? 0.1011 0.1228 0.0852 0.0157 -0.0243 -0.0255 29 ARG B NH1 1730 N NH2 . ARG B 31 ? 0.1141 0.1320 0.0753 0.0173 -0.0281 -0.0245 29 ARG B NH2 1731 N N . TYR B 32 ? 0.1818 0.1792 0.1492 0.0123 -0.0148 -0.0203 30 TYR B N 1732 C CA . TYR B 32 ? 0.1797 0.1730 0.1447 0.0126 -0.0163 -0.0203 30 TYR B CA 1733 C C . TYR B 32 ? 0.1912 0.1770 0.1464 0.0148 -0.0162 -0.0178 30 TYR B C 1734 O O . TYR B 32 ? 0.1789 0.1611 0.1279 0.0146 -0.0142 -0.0156 30 TYR B O 1735 C CB . TYR B 32 ? 0.1864 0.1785 0.1573 0.0080 -0.0138 -0.0228 30 TYR B CB 1736 C CG . TYR B 32 ? 0.2028 0.2043 0.1859 0.0074 -0.0159 -0.0250 30 TYR B CG 1737 C CD1 . TYR B 32 ? 0.1684 0.1750 0.1586 0.0076 -0.0135 -0.0249 30 TYR B CD1 1738 C CD2 . TYR B 32 ? 0.2316 0.2371 0.2189 0.0074 -0.0205 -0.0273 30 TYR B CD2 1739 C CE1 . TYR B 32 ? 0.2107 0.2257 0.2137 0.0085 -0.0154 -0.0255 30 TYR B CE1 1740 C CE2 . TYR B 32 ? 0.2105 0.2264 0.2090 0.0082 -0.0238 -0.0281 30 TYR B CE2 1741 C CZ . TYR B 32 ? 0.2182 0.2385 0.2253 0.0091 -0.0210 -0.0264 30 TYR B CZ 1742 O OH . TYR B 32 ? 0.2147 0.2449 0.2346 0.0112 -0.0242 -0.0259 30 TYR B OH 1743 N N . PHE B 33 ? 0.1412 0.1247 0.0943 0.0178 -0.0182 -0.0179 31 PHE B N 1744 C CA . PHE B 33 ? 0.1385 0.1156 0.0852 0.0215 -0.0180 -0.0151 31 PHE B CA 1745 C C . PHE B 33 ? 0.1729 0.1406 0.1179 0.0218 -0.0167 -0.0172 31 PHE B C 1746 O O . PHE B 33 ? 0.2222 0.1916 0.1694 0.0206 -0.0180 -0.0218 31 PHE B O 1747 C CB . PHE B 33 ? 0.1676 0.1511 0.1154 0.0262 -0.0202 -0.0138 31 PHE B CB 1748 C CG . PHE B 33 ? 0.1259 0.1182 0.0780 0.0254 -0.0214 -0.0133 31 PHE B CG 1749 C CD1 . PHE B 33 ? 0.1070 0.1049 0.0652 0.0236 -0.0212 -0.0148 31 PHE B CD1 1750 C CD2 . PHE B 33 ? 0.1301 0.1251 0.0807 0.0266 -0.0230 -0.0117 31 PHE B CD2 1751 C CE1 . PHE B 33 ? 0.1904 0.1940 0.1545 0.0225 -0.0212 -0.0150 31 PHE B CE1 1752 C CE2 . PHE B 33 ? 0.1309 0.1334 0.0865 0.0248 -0.0241 -0.0134 31 PHE B CE2 1753 C CZ . PHE B 33 ? 0.1342 0.1399 0.0973 0.0225 -0.0224 -0.0153 31 PHE B CZ 1754 N N . TYR B 34 ? 0.1845 0.1419 0.1252 0.0234 -0.0144 -0.0139 32 TYR B N 1755 C CA . TYR B 34 ? 0.1936 0.1396 0.1338 0.0247 -0.0122 -0.0158 32 TYR B CA 1756 C C . TYR B 34 ? 0.1856 0.1293 0.1234 0.0324 -0.0126 -0.0118 32 TYR B C 1757 O O . TYR B 34 ? 0.1670 0.1089 0.1016 0.0355 -0.0128 -0.0051 32 TYR B O 1758 C CB . TYR B 34 ? 0.1700 0.1035 0.1105 0.0203 -0.0074 -0.0143 32 TYR B CB 1759 C CG . TYR B 34 ? 0.2160 0.1347 0.1580 0.0207 -0.0041 -0.0172 32 TYR B CG 1760 C CD1 . TYR B 34 ? 0.1857 0.1046 0.1320 0.0177 -0.0053 -0.0269 32 TYR B CD1 1761 C CD2 . TYR B 34 ? 0.1998 0.1041 0.1390 0.0241 0.0002 -0.0104 32 TYR B CD2 1762 C CE1 . TYR B 34 ? 0.2013 0.1057 0.1497 0.0173 -0.0018 -0.0317 32 TYR B CE1 1763 C CE2 . TYR B 34 ? 0.2323 0.1207 0.1750 0.0244 0.0045 -0.0134 32 TYR B CE2 1764 C CZ . TYR B 34 ? 0.2388 0.1270 0.1865 0.0205 0.0036 -0.0251 32 TYR B CZ 1765 O OH . TYR B 34 ? 0.2614 0.1330 0.2130 0.0202 0.0082 -0.0304 32 TYR B OH 1766 N N . HIS B 35 ? 0.2201 0.1648 0.1592 0.0359 -0.0126 -0.0158 33 HIS B N 1767 C CA . HIS B 35 ? 0.2550 0.2028 0.1957 0.0436 -0.0128 -0.0125 33 HIS B CA 1768 C C . HIS B 35 ? 0.2899 0.2524 0.2333 0.0446 -0.0165 -0.0088 33 HIS B C 1769 O O . HIS B 35 ? 0.3150 0.2869 0.2604 0.0421 -0.0175 -0.0114 33 HIS B O 1770 C CB . HIS B 35 ? 0.2501 0.1855 0.1905 0.0488 -0.0106 -0.0074 33 HIS B CB 1771 C CG . HIS B 35 ? 0.2879 0.2062 0.2277 0.0467 -0.0059 -0.0114 33 HIS B CG 1772 N ND1 . HIS B 35 ? 0.2603 0.1767 0.2003 0.0430 -0.0045 -0.0213 33 HIS B ND1 1773 C CD2 . HIS B 35 ? 0.3109 0.2129 0.2504 0.0475 -0.0020 -0.0072 33 HIS B CD2 1774 C CE1 . HIS B 35 ? 0.2868 0.1868 0.2281 0.0408 -0.0004 -0.0247 33 HIS B CE1 1775 N NE2 . HIS B 35 ? 0.3111 0.2012 0.2530 0.0434 0.0020 -0.0156 33 HIS B NE2 1776 N N . GLN B 36 ? 0.3035 0.2677 0.2472 0.0483 -0.0188 -0.0029 34 GLN B N 1777 C CA . GLN B 36 ? 0.3014 0.2796 0.2485 0.0481 -0.0231 -0.0012 34 GLN B CA 1778 C C . GLN B 36 ? 0.3289 0.3069 0.2691 0.0437 -0.0250 0.0005 34 GLN B C 1779 O O . GLN B 36 ? 0.3745 0.3629 0.3162 0.0421 -0.0285 -0.0001 34 GLN B O 1780 C CB . GLN B 36 ? 0.3464 0.3314 0.2997 0.0555 -0.0262 0.0029 34 GLN B CB 1781 C CG . GLN B 36 ? 0.4372 0.4261 0.4000 0.0604 -0.0233 0.0010 34 GLN B CG 1782 C CD . GLN B 36 ? 0.5508 0.5439 0.5214 0.0689 -0.0258 0.0059 34 GLN B CD 1783 O OE1 . GLN B 36 ? 0.6064 0.6136 0.5843 0.0702 -0.0313 0.0078 34 GLN B OE1 1784 N NE2 . GLN B 36 ? 0.5787 0.5601 0.5492 0.0749 -0.0219 0.0075 34 GLN B NE2 1785 N N . GLU B 37 ? 0.3346 0.3005 0.2679 0.0412 -0.0217 0.0019 35 GLU B N 1786 C CA . GLU B 37 ? 0.3277 0.2917 0.2528 0.0376 -0.0213 0.0043 35 GLU B CA 1787 C C . GLU B 37 ? 0.2605 0.2282 0.1874 0.0303 -0.0192 -0.0008 35 GLU B C 1788 O O . GLU B 37 ? 0.2576 0.2200 0.1878 0.0265 -0.0158 -0.0038 35 GLU B O 1789 C CB . GLU B 37 ? 0.4084 0.3566 0.3267 0.0384 -0.0168 0.0098 35 GLU B CB 1790 C CG . GLU B 37 ? 0.5199 0.4634 0.4291 0.0338 -0.0130 0.0126 35 GLU B CG 1791 C CD . GLU B 37 ? 0.5812 0.5071 0.4872 0.0332 -0.0062 0.0177 35 GLU B CD 1792 O OE1 . GLU B 37 ? 0.5752 0.4957 0.4770 0.0278 -0.0003 0.0191 35 GLU B OE1 1793 O OE2 . GLU B 37 ? 0.5825 0.4994 0.4919 0.0380 -0.0057 0.0201 35 GLU B OE2 1794 N N . GLU B 38 ? 0.2185 0.1959 0.1450 0.0286 -0.0216 -0.0027 36 GLU B N 1795 C CA . GLU B 38 ? 0.2221 0.2020 0.1511 0.0227 -0.0187 -0.0070 36 GLU B CA 1796 C C . GLU B 38 ? 0.2171 0.1882 0.1377 0.0199 -0.0134 -0.0044 36 GLU B C 1797 O O . GLU B 38 ? 0.2079 0.1763 0.1167 0.0219 -0.0135 0.0001 36 GLU B O 1798 C CB . GLU B 38 ? 0.1353 0.1252 0.0659 0.0215 -0.0213 -0.0104 36 GLU B CB 1799 C CG . GLU B 38 ? 0.1288 0.1211 0.0658 0.0167 -0.0176 -0.0153 36 GLU B CG 1800 C CD . GLU B 38 ? 0.2227 0.2227 0.1631 0.0153 -0.0192 -0.0200 36 GLU B CD 1801 O OE1 . GLU B 38 ? 0.2260 0.2303 0.1618 0.0169 -0.0236 -0.0203 36 GLU B OE1 1802 O OE2 . GLU B 38 ? 0.1700 0.1719 0.1191 0.0126 -0.0162 -0.0238 36 GLU B OE2 1803 N N . TYR B 39 ? 0.1812 0.1487 0.1081 0.0153 -0.0088 -0.0068 37 TYR B N 1804 C CA . TYR B 39 ? 0.2055 0.1645 0.1275 0.0118 -0.0019 -0.0041 37 TYR B CA 1805 C C . TYR B 39 ? 0.2026 0.1666 0.1287 0.0067 0.0031 -0.0080 37 TYR B C 1806 O O . TYR B 39 ? 0.1731 0.1321 0.0923 0.0042 0.0101 -0.0054 37 TYR B O 1807 C CB . TYR B 39 ? 0.2039 0.1525 0.1312 0.0102 0.0012 -0.0033 37 TYR B CB 1808 C CG . TYR B 39 ? 0.2317 0.1854 0.1730 0.0071 -0.0008 -0.0103 37 TYR B CG 1809 C CD1 . TYR B 39 ? 0.2673 0.2248 0.2191 0.0012 0.0027 -0.0143 37 TYR B CD1 1810 C CD2 . TYR B 39 ? 0.2260 0.1818 0.1697 0.0106 -0.0062 -0.0128 37 TYR B CD2 1811 C CE1 . TYR B 39 ? 0.2900 0.2542 0.2539 -0.0009 -0.0010 -0.0204 37 TYR B CE1 1812 C CE2 . TYR B 39 ? 0.2341 0.1951 0.1869 0.0084 -0.0088 -0.0189 37 TYR B CE2 1813 C CZ . TYR B 39 ? 0.2688 0.2344 0.2314 0.0028 -0.0071 -0.0225 37 TYR B CZ 1814 O OH . TYR B 39 ? 0.3161 0.2891 0.2873 0.0013 -0.0115 -0.0283 37 TYR B OH 1815 N N . VAL B 40 ? 0.2032 0.1768 0.1408 0.0057 0.0006 -0.0136 38 VAL B N 1816 C CA . VAL B 40 ? 0.2241 0.2033 0.1688 0.0022 0.0054 -0.0177 38 VAL B CA 1817 C C . VAL B 40 ? 0.2422 0.2305 0.1955 0.0038 0.0011 -0.0219 38 VAL B C 1818 O O . VAL B 40 ? 0.2613 0.2523 0.2193 0.0064 -0.0046 -0.0216 38 VAL B O 1819 C CB . VAL B 40 ? 0.1992 0.1780 0.1572 -0.0024 0.0101 -0.0193 38 VAL B CB 1820 C CG1 . VAL B 40 ? 0.1909 0.1747 0.1612 -0.0017 0.0036 -0.0220 38 VAL B CG1 1821 C CG2 . VAL B 40 ? 0.2213 0.2059 0.1877 -0.0055 0.0169 -0.0229 38 VAL B CG2 1822 N N . ARG B 41 ? 0.2456 0.2375 0.2010 0.0024 0.0050 -0.0257 39 ARG B N 1823 C CA . ARG B 41 ? 0.2493 0.2474 0.2145 0.0038 0.0025 -0.0294 39 ARG B CA 1824 C C . ARG B 41 ? 0.2155 0.2167 0.1907 0.0020 0.0091 -0.0343 39 ARG B C 1825 O O . ARG B 41 ? 0.1611 0.1601 0.1300 -0.0004 0.0161 -0.0361 39 ARG B O 1826 C CB . ARG B 41 ? 0.2683 0.2672 0.2245 0.0055 -0.0016 -0.0306 39 ARG B CB 1827 C CG . ARG B 41 ? 0.3424 0.3397 0.2843 0.0039 0.0017 -0.0337 39 ARG B CG 1828 C CD . ARG B 41 ? 0.3512 0.3527 0.2916 0.0042 -0.0026 -0.0389 39 ARG B CD 1829 N NE . ARG B 41 ? 0.3399 0.3440 0.2797 0.0069 -0.0106 -0.0355 39 ARG B NE 1830 C CZ . ARG B 41 ? 0.3649 0.3744 0.3045 0.0069 -0.0157 -0.0395 39 ARG B CZ 1831 N NH1 . ARG B 41 ? 0.3611 0.3725 0.2991 0.0039 -0.0142 -0.0479 39 ARG B NH1 1832 N NH2 . ARG B 41 ? 0.3843 0.3976 0.3266 0.0095 -0.0220 -0.0360 39 ARG B NH2 1833 N N . PHE B 42 ? 0.2380 0.2438 0.2287 0.0037 0.0076 -0.0357 40 PHE B N 1834 C CA . PHE B 42 ? 0.1743 0.1823 0.1764 0.0034 0.0138 -0.0407 40 PHE B CA 1835 C C . PHE B 42 ? 0.2018 0.2083 0.2030 0.0042 0.0124 -0.0445 40 PHE B C 1836 O O . PHE B 42 ? 0.1851 0.1924 0.1911 0.0063 0.0072 -0.0416 40 PHE B O 1837 C CB . PHE B 42 ? 0.1380 0.1520 0.1607 0.0056 0.0131 -0.0388 40 PHE B CB 1838 C CG . PHE B 42 ? 0.1948 0.2107 0.2331 0.0070 0.0195 -0.0431 40 PHE B CG 1839 C CD1 . PHE B 42 ? 0.1899 0.2038 0.2355 0.0097 0.0188 -0.0440 40 PHE B CD1 1840 C CD2 . PHE B 42 ? 0.1151 0.1344 0.1630 0.0055 0.0273 -0.0462 40 PHE B CD2 1841 C CE1 . PHE B 42 ? 0.1138 0.1277 0.1753 0.0115 0.0255 -0.0482 40 PHE B CE1 1842 C CE2 . PHE B 42 ? 0.1182 0.1391 0.1821 0.0077 0.0341 -0.0505 40 PHE B CE2 1843 C CZ . PHE B 42 ? 0.1178 0.1354 0.1884 0.0109 0.0330 -0.0517 40 PHE B CZ 1844 N N . ASP B 43 ? 0.2073 0.2117 0.2024 0.0022 0.0180 -0.0515 41 ASP B N 1845 C CA . ASP B 43 ? 0.2288 0.2317 0.2252 0.0016 0.0175 -0.0580 41 ASP B CA 1846 C C . ASP B 43 ? 0.2467 0.2483 0.2586 0.0019 0.0258 -0.0641 41 ASP B C 1847 O O . ASP B 43 ? 0.2810 0.2824 0.2903 0.0009 0.0336 -0.0680 41 ASP B O 1848 C CB . ASP B 43 ? 0.2289 0.2307 0.2039 -0.0010 0.0164 -0.0631 41 ASP B CB 1849 C CG . ASP B 43 ? 0.2343 0.2362 0.2110 -0.0028 0.0139 -0.0716 41 ASP B CG 1850 O OD1 . ASP B 43 ? 0.1558 0.1559 0.1510 -0.0026 0.0165 -0.0747 41 ASP B OD1 1851 O OD2 . ASP B 43 ? 0.2810 0.2849 0.2413 -0.0044 0.0092 -0.0752 41 ASP B OD2 1852 N N . SER B 44 ? 0.2285 0.2286 0.2572 0.0038 0.0254 -0.0644 42 SER B N 1853 C CA . SER B 44 ? 0.1912 0.1887 0.2379 0.0054 0.0335 -0.0696 42 SER B CA 1854 C C . SER B 44 ? 0.2039 0.1973 0.2424 0.0019 0.0408 -0.0827 42 SER B C 1855 O O . SER B 44 ? 0.2014 0.1925 0.2512 0.0031 0.0500 -0.0887 42 SER B O 1856 C CB . SER B 44 ? 0.2038 0.1981 0.2692 0.0086 0.0320 -0.0657 42 SER B CB 1857 O OG . SER B 44 ? 0.2466 0.2371 0.3081 0.0053 0.0293 -0.0701 42 SER B OG 1858 N N . ASP B 45 ? 0.2187 0.2117 0.2374 -0.0019 0.0363 -0.0876 43 ASP B N 1859 C CA . ASP B 45 ? 0.2583 0.2491 0.2629 -0.0054 0.0410 -0.0999 43 ASP B CA 1860 C C . ASP B 45 ? 0.2395 0.2314 0.2313 -0.0053 0.0485 -0.0992 43 ASP B C 1861 O O . ASP B 45 ? 0.2069 0.1967 0.1917 -0.0066 0.0543 -0.1051 43 ASP B O 1862 C CB . ASP B 45 ? 0.3357 0.3290 0.3211 -0.0085 0.0315 -0.1019 43 ASP B CB 1863 C CG . ASP B 45 ? 0.3358 0.3279 0.3349 -0.0106 0.0268 -0.1062 43 ASP B CG 1864 O OD1 . ASP B 45 ? 0.3524 0.3399 0.3746 -0.0092 0.0312 -0.1060 43 ASP B OD1 1865 O OD2 . ASP B 45 ? 0.3366 0.3326 0.3249 -0.0133 0.0188 -0.1089 43 ASP B OD2 1866 N N . VAL B 46 ? 0.1796 0.1749 0.1695 -0.0039 0.0477 -0.0900 44 VAL B N 1867 C CA . VAL B 46 ? 0.2521 0.2484 0.2311 -0.0047 0.0559 -0.0886 44 VAL B CA 1868 C C . VAL B 46 ? 0.2317 0.2311 0.2351 -0.0025 0.0636 -0.0857 44 VAL B C 1869 O O . VAL B 46 ? 0.1919 0.1913 0.1982 -0.0029 0.0750 -0.0908 44 VAL B O 1870 C CB . VAL B 46 ? 0.2575 0.2547 0.2181 -0.0054 0.0496 -0.0787 44 VAL B CB 1871 C CG1 . VAL B 46 ? 0.2145 0.2115 0.1681 -0.0067 0.0598 -0.0755 44 VAL B CG1 1872 C CG2 . VAL B 46 ? 0.2691 0.2653 0.2052 -0.0065 0.0421 -0.0813 44 VAL B CG2 1873 N N . GLY B 47 ? 0.1889 0.1919 0.2100 0.0001 0.0566 -0.0772 45 GLY B N 1874 C CA . GLY B 47 ? 0.1967 0.2054 0.2436 0.0029 0.0609 -0.0743 45 GLY B CA 1875 C C . GLY B 47 ? 0.2299 0.2439 0.2763 0.0011 0.0611 -0.0676 45 GLY B C 1876 O O . GLY B 47 ? 0.2573 0.2786 0.3252 0.0023 0.0648 -0.0659 45 GLY B O 1877 N N . GLU B 48 ? 0.2392 0.2498 0.2630 -0.0019 0.0569 -0.0638 46 GLU B N 1878 C CA . GLU B 48 ? 0.2386 0.2514 0.2617 -0.0043 0.0567 -0.0572 46 GLU B CA 1879 C C . GLU B 48 ? 0.2170 0.2255 0.2228 -0.0046 0.0463 -0.0511 46 GLU B C 1880 O O . GLU B 48 ? 0.2270 0.2316 0.2182 -0.0036 0.0410 -0.0523 46 GLU B O 1881 C CB . GLU B 48 ? 0.2916 0.3019 0.3037 -0.0080 0.0696 -0.0590 46 GLU B CB 1882 C CG . GLU B 48 ? 0.3463 0.3628 0.3798 -0.0081 0.0821 -0.0638 46 GLU B CG 1883 C CD . GLU B 48 ? 0.4011 0.4148 0.4220 -0.0121 0.0965 -0.0644 46 GLU B CD 1884 O OE1 . GLU B 48 ? 0.3691 0.3748 0.3615 -0.0140 0.0962 -0.0608 46 GLU B OE1 1885 O OE2 . GLU B 48 ? 0.4072 0.4268 0.4469 -0.0129 0.1085 -0.0676 46 GLU B OE2 1886 N N . TYR B 49 ? 0.1516 0.1611 0.1610 -0.0062 0.0436 -0.0455 47 TYR B N 1887 C CA . TYR B 49 ? 0.1581 0.1620 0.1515 -0.0063 0.0360 -0.0400 47 TYR B CA 1888 C C . TYR B 49 ? 0.2016 0.1976 0.1711 -0.0082 0.0416 -0.0380 47 TYR B C 1889 O O . TYR B 49 ? 0.1763 0.1709 0.1435 -0.0110 0.0526 -0.0388 47 TYR B O 1890 C CB . TYR B 49 ? 0.1350 0.1413 0.1402 -0.0078 0.0320 -0.0363 47 TYR B CB 1891 C CG . TYR B 49 ? 0.1896 0.2029 0.2095 -0.0045 0.0226 -0.0363 47 TYR B CG 1892 C CD1 . TYR B 49 ? 0.1457 0.1688 0.1883 -0.0035 0.0231 -0.0384 47 TYR B CD1 1893 C CD2 . TYR B 49 ? 0.1684 0.1792 0.1795 -0.0018 0.0135 -0.0334 47 TYR B CD2 1894 C CE1 . TYR B 49 ? 0.1339 0.1635 0.1871 0.0005 0.0141 -0.0367 47 TYR B CE1 1895 C CE2 . TYR B 49 ? 0.1060 0.1228 0.1272 0.0016 0.0059 -0.0323 47 TYR B CE2 1896 C CZ . TYR B 49 ? 0.1432 0.1691 0.1841 0.0028 0.0059 -0.0335 47 TYR B CZ 1897 O OH . TYR B 49 ? 0.1378 0.1697 0.1860 0.0071 -0.0020 -0.0309 47 TYR B OH 1898 N N . ARG B 50 ? 0.1652 0.1566 0.1170 -0.0062 0.0343 -0.0348 48 ARG B N 1899 C CA . ARG B 50 ? 0.2162 0.2003 0.1439 -0.0064 0.0372 -0.0306 48 ARG B CA 1900 C C . ARG B 50 ? 0.2467 0.2256 0.1676 -0.0043 0.0297 -0.0232 48 ARG B C 1901 O O . ARG B 50 ? 0.2649 0.2466 0.1909 -0.0016 0.0203 -0.0235 48 ARG B O 1902 C CB . ARG B 50 ? 0.2446 0.2300 0.1553 -0.0047 0.0352 -0.0354 48 ARG B CB 1903 C CG . ARG B 50 ? 0.2957 0.2840 0.2092 -0.0065 0.0442 -0.0442 48 ARG B CG 1904 C CD . ARG B 50 ? 0.3536 0.3376 0.2542 -0.0089 0.0572 -0.0422 48 ARG B CD 1905 N NE . ARG B 50 ? 0.3838 0.3704 0.2857 -0.0102 0.0673 -0.0517 48 ARG B NE 1906 C CZ . ARG B 50 ? 0.4243 0.4140 0.3467 -0.0120 0.0778 -0.0546 48 ARG B CZ 1907 N NH1 . ARG B 50 ? 0.4371 0.4291 0.3805 -0.0134 0.0784 -0.0492 48 ARG B NH1 1908 N NH2 . ARG B 50 ? 0.4608 0.4523 0.3840 -0.0123 0.0877 -0.0639 48 ARG B NH2 1909 N N . ALA B 51 ? 0.2577 0.2280 0.1679 -0.0054 0.0350 -0.0163 49 ALA B N 1910 C CA . ALA B 51 ? 0.2631 0.2263 0.1668 -0.0026 0.0292 -0.0091 49 ALA B CA 1911 C C . ALA B 51 ? 0.2582 0.2228 0.1445 0.0026 0.0208 -0.0075 49 ALA B C 1912 O O . ALA B 51 ? 0.2813 0.2472 0.1508 0.0033 0.0225 -0.0082 49 ALA B O 1913 C CB . ALA B 51 ? 0.2143 0.1659 0.1108 -0.0048 0.0383 -0.0013 49 ALA B CB 1914 N N . VAL B 52 ? 0.2507 0.2165 0.1418 0.0062 0.0116 -0.0060 50 VAL B N 1915 C CA . VAL B 52 ? 0.2514 0.2204 0.1308 0.0113 0.0029 -0.0040 50 VAL B CA 1916 C C . VAL B 52 ? 0.2912 0.2505 0.1571 0.0156 0.0027 0.0064 50 VAL B C 1917 O O . VAL B 52 ? 0.3488 0.3094 0.1980 0.0199 -0.0017 0.0107 50 VAL B O 1918 C CB . VAL B 52 ? 0.2202 0.1969 0.1139 0.0134 -0.0055 -0.0079 50 VAL B CB 1919 C CG1 . VAL B 52 ? 0.1814 0.1636 0.0671 0.0183 -0.0144 -0.0063 50 VAL B CG1 1920 C CG2 . VAL B 52 ? 0.1686 0.1530 0.0755 0.0099 -0.0046 -0.0164 50 VAL B CG2 1921 N N . THR B 53 ? 0.2929 0.2423 0.1668 0.0144 0.0073 0.0104 51 THR B N 1922 C CA . THR B 53 ? 0.3137 0.2501 0.1778 0.0179 0.0099 0.0210 51 THR B CA 1923 C C . THR B 53 ? 0.3286 0.2536 0.1972 0.0121 0.0218 0.0234 51 THR B C 1924 O O . THR B 53 ? 0.3138 0.2433 0.1956 0.0058 0.0264 0.0163 51 THR B O 1925 C CB . THR B 53 ? 0.3183 0.2515 0.1912 0.0229 0.0036 0.0229 51 THR B CB 1926 O OG1 . THR B 53 ? 0.3368 0.2683 0.2276 0.0184 0.0059 0.0167 51 THR B OG1 1927 C CG2 . THR B 53 ? 0.2518 0.1982 0.1257 0.0279 -0.0072 0.0198 51 THR B CG2 1928 N N . GLU B 54 ? 0.3174 0.2277 0.1765 0.0144 0.0269 0.0340 52 GLU B N 1929 C CA . GLU B 54 ? 0.3737 0.2712 0.2380 0.0084 0.0396 0.0377 52 GLU B CA 1930 C C . GLU B 54 ? 0.3345 0.2320 0.2241 0.0023 0.0403 0.0290 52 GLU B C 1931 O O . GLU B 54 ? 0.2850 0.1808 0.1868 -0.0054 0.0491 0.0260 52 GLU B O 1932 C CB . GLU B 54 ? 0.4949 0.3744 0.3463 0.0133 0.0441 0.0519 52 GLU B CB 1933 C CG . GLU B 54 ? 0.6374 0.5042 0.4794 0.0094 0.0589 0.0610 52 GLU B CG 1934 C CD . GLU B 54 ? 0.7765 0.6226 0.6107 0.0145 0.0636 0.0757 52 GLU B CD 1935 O OE1 . GLU B 54 ? 0.8118 0.6496 0.6238 0.0179 0.0702 0.0887 52 GLU B OE1 1936 O OE2 . GLU B 54 ? 0.8151 0.6527 0.6647 0.0155 0.0611 0.0743 52 GLU B OE2 1937 N N . LEU B 55 ? 0.3142 0.2146 0.2115 0.0060 0.0309 0.0247 53 LEU B N 1938 C CA . LEU B 55 ? 0.2825 0.1845 0.1998 0.0016 0.0290 0.0155 53 LEU B CA 1939 C C . LEU B 55 ? 0.2643 0.1809 0.1952 -0.0046 0.0285 0.0059 53 LEU B C 1940 O O . LEU B 55 ? 0.3012 0.2189 0.2488 -0.0101 0.0293 -0.0008 53 LEU B O 1941 C CB . LEU B 55 ? 0.2866 0.1917 0.2049 0.0080 0.0192 0.0130 53 LEU B CB 1942 C CG . LEU B 55 ? 0.3589 0.2552 0.2888 0.0069 0.0189 0.0081 53 LEU B CG 1943 C CD1 . LEU B 55 ? 0.3989 0.2749 0.3289 0.0053 0.0280 0.0146 53 LEU B CD1 1944 C CD2 . LEU B 55 ? 0.3664 0.2660 0.2943 0.0146 0.0111 0.0067 53 LEU B CD2 1945 N N . GLY B 56 ? 0.2375 0.1654 0.1621 -0.0033 0.0268 0.0048 54 GLY B N 1946 C CA . GLY B 56 ? 0.2194 0.1611 0.1576 -0.0071 0.0259 -0.0035 54 GLY B CA 1947 C C . GLY B 56 ? 0.2192 0.1634 0.1628 -0.0127 0.0361 -0.0044 54 GLY B C 1948 O O . GLY B 56 ? 0.2539 0.2097 0.2115 -0.0151 0.0357 -0.0110 54 GLY B O 1949 N N . ARG B 57 ? 0.2500 0.1833 0.1828 -0.0143 0.0459 0.0028 55 ARG B N 1950 C CA . ARG B 57 ? 0.3276 0.2627 0.2637 -0.0195 0.0582 0.0027 55 ARG B CA 1951 C C . ARG B 57 ? 0.3224 0.2639 0.2868 -0.0269 0.0623 -0.0040 55 ARG B C 1952 O O . ARG B 57 ? 0.2962 0.2485 0.2713 -0.0294 0.0673 -0.0087 55 ARG B O 1953 C CB . ARG B 57 ? 0.3655 0.2860 0.2826 -0.0195 0.0690 0.0135 55 ARG B CB 1954 C CG . ARG B 57 ? 0.4841 0.4036 0.3728 -0.0121 0.0645 0.0188 55 ARG B CG 1955 C CD . ARG B 57 ? 0.6147 0.5195 0.4803 -0.0098 0.0727 0.0319 55 ARG B CD 1956 N NE . ARG B 57 ? 0.7379 0.6458 0.5768 -0.0024 0.0654 0.0353 55 ARG B NE 1957 C CZ . ARG B 57 ? 0.8404 0.7382 0.6545 0.0030 0.0668 0.0476 55 ARG B CZ 1958 N NH1 . ARG B 57 ? 0.8659 0.7470 0.6782 0.0019 0.0772 0.0590 55 ARG B NH1 1959 N NH2 . ARG B 57 ? 0.8936 0.7981 0.6854 0.0096 0.0578 0.0487 55 ARG B NH2 1960 N N . PRO B 58 ? 0.3292 0.2651 0.3070 -0.0304 0.0604 -0.0052 56 PRO B N 1961 C CA . PRO B 58 ? 0.3123 0.2574 0.3186 -0.0379 0.0626 -0.0129 56 PRO B CA 1962 C C . PRO B 58 ? 0.2923 0.2561 0.3115 -0.0356 0.0524 -0.0212 56 PRO B C 1963 O O . PRO B 58 ? 0.2830 0.2592 0.3230 -0.0395 0.0557 -0.0262 56 PRO B O 1964 C CB . PRO B 58 ? 0.2493 0.1844 0.2637 -0.0411 0.0593 -0.0145 56 PRO B CB 1965 C CG . PRO B 58 ? 0.2402 0.1561 0.2322 -0.0370 0.0633 -0.0042 56 PRO B CG 1966 C CD . PRO B 58 ? 0.2658 0.1862 0.2354 -0.0285 0.0579 -0.0003 56 PRO B CD 1967 N N . ASP B 59 ? 0.3050 0.2708 0.3133 -0.0291 0.0409 -0.0219 57 ASP B N 1968 C CA . ASP B 59 ? 0.2391 0.2203 0.2576 -0.0260 0.0315 -0.0276 57 ASP B CA 1969 C C . ASP B 59 ? 0.2520 0.2412 0.2706 -0.0238 0.0360 -0.0280 57 ASP B C 1970 O O . ASP B 59 ? 0.2377 0.2399 0.2744 -0.0239 0.0343 -0.0326 57 ASP B O 1971 C CB . ASP B 59 ? 0.2588 0.2383 0.2650 -0.0198 0.0204 -0.0272 57 ASP B CB 1972 C CG . ASP B 59 ? 0.2980 0.2722 0.3073 -0.0215 0.0153 -0.0298 57 ASP B CG 1973 O OD1 . ASP B 59 ? 0.3012 0.2793 0.3279 -0.0274 0.0159 -0.0350 57 ASP B OD1 1974 O OD2 . ASP B 59 ? 0.3405 0.3069 0.3360 -0.0170 0.0111 -0.0275 57 ASP B OD2 1975 N N . ALA B 60 ? 0.2697 0.2512 0.2678 -0.0215 0.0412 -0.0237 58 ALA B N 1976 C CA . ALA B 60 ? 0.2305 0.2173 0.2257 -0.0200 0.0468 -0.0256 58 ALA B CA 1977 C C . ALA B 60 ? 0.2460 0.2391 0.2599 -0.0249 0.0581 -0.0284 58 ALA B C 1978 O O . ALA B 60 ? 0.2245 0.2282 0.2528 -0.0237 0.0594 -0.0334 58 ALA B O 1979 C CB . ALA B 60 ? 0.2275 0.2050 0.1952 -0.0176 0.0504 -0.0212 58 ALA B CB 1980 N N . GLU B 61 ? 0.2376 0.2236 0.2531 -0.0304 0.0671 -0.0250 59 GLU B N 1981 C CA . GLU B 61 ? 0.2854 0.2771 0.3202 -0.0361 0.0801 -0.0270 59 GLU B CA 1982 C C . GLU B 61 ? 0.2603 0.2675 0.3291 -0.0387 0.0747 -0.0335 59 GLU B C 1983 O O . GLU B 61 ? 0.2427 0.2620 0.3318 -0.0397 0.0811 -0.0375 59 GLU B O 1984 C CB . GLU B 61 ? 0.3769 0.3552 0.4043 -0.0417 0.0925 -0.0202 59 GLU B CB 1985 C CG . GLU B 61 ? 0.5356 0.4997 0.5275 -0.0380 0.0972 -0.0122 59 GLU B CG 1986 C CD . GLU B 61 ? 0.6322 0.5812 0.6156 -0.0424 0.1100 -0.0031 59 GLU B CD 1987 O OE1 . GLU B 61 ? 0.6945 0.6429 0.7015 -0.0495 0.1151 -0.0038 59 GLU B OE1 1988 O OE2 . GLU B 61 ? 0.6665 0.6043 0.6201 -0.0389 0.1146 0.0051 59 GLU B OE2 1989 N N . TYR B 62 ? 0.2086 0.2163 0.2835 -0.0394 0.0629 -0.0349 60 TYR B N 1990 C CA . TYR B 62 ? 0.2011 0.2249 0.3056 -0.0416 0.0551 -0.0413 60 TYR B CA 1991 C C . TYR B 62 ? 0.2018 0.2391 0.3134 -0.0344 0.0467 -0.0440 60 TYR B C 1992 O O . TYR B 62 ? 0.2420 0.2950 0.3798 -0.0347 0.0474 -0.0478 60 TYR B O 1993 C CB . TYR B 62 ? 0.1744 0.1940 0.2782 -0.0435 0.0440 -0.0432 60 TYR B CB 1994 C CG . TYR B 62 ? 0.2032 0.2406 0.3340 -0.0455 0.0335 -0.0507 60 TYR B CG 1995 C CD1 . TYR B 62 ? 0.1860 0.2372 0.3476 -0.0516 0.0390 -0.0551 60 TYR B CD1 1996 C CD2 . TYR B 62 ? 0.2194 0.2610 0.3448 -0.0412 0.0181 -0.0533 60 TYR B CD2 1997 C CE1 . TYR B 62 ? 0.1960 0.2660 0.3831 -0.0530 0.0275 -0.0622 60 TYR B CE1 1998 C CE2 . TYR B 62 ? 0.2422 0.3012 0.3892 -0.0425 0.0072 -0.0600 60 TYR B CE2 1999 C CZ . TYR B 62 ? 0.2469 0.3207 0.4251 -0.0483 0.0110 -0.0646 60 TYR B CZ 2000 O OH . TYR B 62 ? 0.3025 0.3961 0.5030 -0.0491 -0.0017 -0.0715 60 TYR B OH 2001 N N . TRP B 63 ? 0.1964 0.2279 0.2869 -0.0279 0.0393 -0.0415 61 TRP B N 2002 C CA . TRP B 63 ? 0.1715 0.2126 0.2674 -0.0210 0.0320 -0.0427 61 TRP B CA 2003 C C . TRP B 63 ? 0.2053 0.2503 0.3083 -0.0191 0.0424 -0.0442 61 TRP B C 2004 O O . TRP B 63 ? 0.1867 0.2434 0.3088 -0.0150 0.0398 -0.0461 61 TRP B O 2005 C CB . TRP B 63 ? 0.1276 0.1603 0.2004 -0.0158 0.0235 -0.0396 61 TRP B CB 2006 C CG . TRP B 63 ? 0.1830 0.2138 0.2509 -0.0162 0.0132 -0.0393 61 TRP B CG 2007 C CD1 . TRP B 63 ? 0.1360 0.1731 0.2187 -0.0203 0.0088 -0.0429 61 TRP B CD1 2008 C CD2 . TRP B 63 ? 0.1535 0.1757 0.2010 -0.0125 0.0067 -0.0366 61 TRP B CD2 2009 N NE1 . TRP B 63 ? 0.1247 0.1567 0.1953 -0.0193 0.0001 -0.0431 61 TRP B NE1 2010 C CE2 . TRP B 63 ? 0.1385 0.1613 0.1879 -0.0142 -0.0007 -0.0387 61 TRP B CE2 2011 C CE3 . TRP B 63 ? 0.1316 0.1468 0.1611 -0.0082 0.0064 -0.0333 61 TRP B CE3 2012 C CZ2 . TRP B 63 ? 0.1914 0.2073 0.2246 -0.0110 -0.0069 -0.0374 61 TRP B CZ2 2013 C CZ3 . TRP B 63 ? 0.1139 0.1237 0.1299 -0.0054 -0.0003 -0.0314 61 TRP B CZ3 2014 C CH2 . TRP B 63 ? 0.1152 0.1249 0.1327 -0.0064 -0.0062 -0.0331 61 TRP B CH2 2015 N N . ASN B 64 ? 0.2395 0.2744 0.3265 -0.0214 0.0543 -0.0431 62 ASN B N 2016 C CA . ASN B 64 ? 0.2317 0.2690 0.3224 -0.0199 0.0659 -0.0462 62 ASN B CA 2017 C C . ASN B 64 ? 0.2238 0.2735 0.3448 -0.0232 0.0753 -0.0493 62 ASN B C 2018 O O . ASN B 64 ? 0.1465 0.2015 0.2782 -0.0208 0.0842 -0.0530 62 ASN B O 2019 C CB . ASN B 64 ? 0.2088 0.2326 0.2702 -0.0214 0.0758 -0.0445 62 ASN B CB 2020 C CG . ASN B 64 ? 0.1890 0.2048 0.2256 -0.0170 0.0673 -0.0436 62 ASN B CG 2021 O OD1 . ASN B 64 ? 0.2129 0.2326 0.2555 -0.0127 0.0574 -0.0449 62 ASN B OD1 2022 N ND2 . ASN B 64 ? 0.2041 0.2092 0.2130 -0.0179 0.0713 -0.0408 62 ASN B ND2 2023 N N . SER B 65 ? 0.1860 0.2406 0.3226 -0.0288 0.0738 -0.0488 63 SER B N 2024 C CA . SER B 65 ? 0.1631 0.2323 0.3333 -0.0327 0.0819 -0.0523 63 SER B CA 2025 C C . SER B 65 ? 0.2041 0.2922 0.4038 -0.0278 0.0699 -0.0553 63 SER B C 2026 O O . SER B 65 ? 0.2333 0.3374 0.4656 -0.0292 0.0744 -0.0585 63 SER B O 2027 C CB . SER B 65 ? 0.1626 0.2296 0.3406 -0.0420 0.0861 -0.0514 63 SER B CB 2028 O OG . SER B 65 ? 0.1593 0.2319 0.3467 -0.0433 0.0702 -0.0529 63 SER B OG 2029 N N . GLN B 66 ? 0.2017 0.2885 0.3903 -0.0217 0.0550 -0.0534 64 GLN B N 2030 C CA . GLN B 66 ? 0.1888 0.2919 0.3996 -0.0156 0.0421 -0.0539 64 GLN B CA 2031 C C . GLN B 66 ? 0.2018 0.3044 0.4127 -0.0066 0.0433 -0.0528 64 GLN B C 2032 O O . GLN B 66 ? 0.2042 0.2967 0.3938 -0.0021 0.0371 -0.0498 64 GLN B O 2033 C CB . GLN B 66 ? 0.1516 0.2537 0.3504 -0.0148 0.0252 -0.0521 64 GLN B CB 2034 C CG . GLN B 66 ? 0.2170 0.3177 0.4166 -0.0238 0.0237 -0.0547 64 GLN B CG 2035 C CD . GLN B 66 ? 0.2942 0.3921 0.4787 -0.0228 0.0084 -0.0544 64 GLN B CD 2036 O OE1 . GLN B 66 ? 0.3464 0.4532 0.5324 -0.0160 -0.0040 -0.0530 64 GLN B OE1 2037 N NE2 . GLN B 66 ? 0.3140 0.3989 0.4836 -0.0291 0.0100 -0.0553 64 GLN B NE2 2038 N N . LYS B 67 ? 0.2160 0.3292 0.4530 -0.0041 0.0524 -0.0555 65 LYS B N 2039 C CA . LYS B 67 ? 0.2420 0.3525 0.4819 0.0041 0.0565 -0.0556 65 LYS B CA 2040 C C . LYS B 67 ? 0.1704 0.2844 0.4136 0.0129 0.0417 -0.0506 65 LYS B C 2041 O O . LYS B 67 ? 0.1192 0.2227 0.3517 0.0182 0.0431 -0.0494 65 LYS B O 2042 C CB . LYS B 67 ? 0.3013 0.4165 0.5596 0.0048 0.0657 -0.0572 65 LYS B CB 2043 C CG . LYS B 67 ? 0.3994 0.5324 0.6848 0.0065 0.0554 -0.0550 65 LYS B CG 2044 C CD . LYS B 67 ? 0.4530 0.5924 0.7583 0.0052 0.0661 -0.0575 65 LYS B CD 2045 C CE . LYS B 67 ? 0.4622 0.6211 0.7943 0.0056 0.0554 -0.0563 65 LYS B CE 2046 N NZ . LYS B 67 ? 0.4539 0.6201 0.8079 0.0040 0.0665 -0.0591 65 LYS B NZ 2047 N N . ASP B 68 ? 0.1563 0.2837 0.4121 0.0142 0.0277 -0.0474 66 ASP B N 2048 C CA . ASP B 68 ? 0.1946 0.3255 0.4496 0.0227 0.0133 -0.0408 66 ASP B CA 2049 C C . ASP B 68 ? 0.2073 0.3244 0.4329 0.0230 0.0075 -0.0379 66 ASP B C 2050 O O . ASP B 68 ? 0.2458 0.3565 0.4648 0.0301 0.0043 -0.0327 66 ASP B O 2051 C CB . ASP B 68 ? 0.2723 0.4204 0.5407 0.0232 -0.0007 -0.0387 66 ASP B CB 2052 C CG . ASP B 68 ? 0.3222 0.4742 0.5867 0.0136 -0.0049 -0.0438 66 ASP B CG 2053 O OD1 . ASP B 68 ? 0.2642 0.4075 0.5222 0.0059 0.0063 -0.0486 66 ASP B OD1 2054 O OD2 . ASP B 68 ? 0.3782 0.5410 0.6448 0.0136 -0.0190 -0.0431 66 ASP B OD2 2055 N N . LEU B 69 ? 0.2180 0.3281 0.4236 0.0150 0.0069 -0.0403 67 LEU B N 2056 C CA . LEU B 69 ? 0.1773 0.2724 0.3515 0.0142 0.0025 -0.0375 67 LEU B CA 2057 C C . LEU B 69 ? 0.1876 0.2673 0.3467 0.0155 0.0120 -0.0377 67 LEU B C 2058 O O . LEU B 69 ? 0.1141 0.1861 0.2600 0.0195 0.0077 -0.0339 67 LEU B O 2059 C CB . LEU B 69 ? 0.2107 0.3005 0.3701 0.0057 0.0022 -0.0405 67 LEU B CB 2060 C CG . LEU B 69 ? 0.2989 0.3726 0.4273 0.0046 0.0007 -0.0383 67 LEU B CG 2061 C CD1 . LEU B 69 ? 0.2958 0.3709 0.4157 0.0104 -0.0116 -0.0337 67 LEU B CD1 2062 C CD2 . LEU B 69 ? 0.3134 0.3806 0.4309 -0.0032 0.0028 -0.0408 67 LEU B CD2 2063 N N . LEU B 70 ? 0.2190 0.2948 0.3799 0.0117 0.0252 -0.0428 68 LEU B N 2064 C CA . LEU B 70 ? 0.2129 0.2755 0.3588 0.0120 0.0341 -0.0455 68 LEU B CA 2065 C C . LEU B 70 ? 0.2289 0.2909 0.3876 0.0196 0.0346 -0.0445 68 LEU B C 2066 O O . LEU B 70 ? 0.1959 0.2468 0.3408 0.0208 0.0347 -0.0446 68 LEU B O 2067 C CB . LEU B 70 ? 0.2040 0.2639 0.3484 0.0069 0.0488 -0.0515 68 LEU B CB 2068 C CG . LEU B 70 ? 0.2350 0.2890 0.3597 -0.0006 0.0517 -0.0513 68 LEU B CG 2069 C CD1 . LEU B 70 ? 0.2877 0.3379 0.4080 -0.0043 0.0679 -0.0560 68 LEU B CD1 2070 C CD2 . LEU B 70 ? 0.2097 0.2519 0.3057 -0.0010 0.0445 -0.0485 68 LEU B CD2 2071 N N . GLU B 71 ? 0.1682 0.2422 0.3554 0.0246 0.0348 -0.0435 69 GLU B N 2072 C CA . GLU B 71 ? 0.1408 0.2134 0.3436 0.0331 0.0357 -0.0411 69 GLU B CA 2073 C C . GLU B 71 ? 0.1798 0.2495 0.3747 0.0381 0.0236 -0.0323 69 GLU B C 2074 O O . GLU B 71 ? 0.2061 0.2666 0.4027 0.0430 0.0256 -0.0298 69 GLU B O 2075 C CB . GLU B 71 ? 0.1122 0.1958 0.3407 0.0368 0.0376 -0.0398 69 GLU B CB 2076 C CG . GLU B 71 ? 0.1806 0.2624 0.4132 0.0322 0.0520 -0.0477 69 GLU B CG 2077 C CD . GLU B 71 ? 0.2431 0.3083 0.4619 0.0312 0.0627 -0.0537 69 GLU B CD 2078 O OE1 . GLU B 71 ? 0.2893 0.3451 0.5039 0.0353 0.0596 -0.0512 69 GLU B OE1 2079 O OE2 . GLU B 71 ? 0.2782 0.3396 0.4893 0.0260 0.0742 -0.0608 69 GLU B OE2 2080 N N . GLN B 72 ? 0.2003 0.2770 0.3867 0.0367 0.0120 -0.0278 70 GLN B N 2081 C CA . GLN B 72 ? 0.2060 0.2796 0.3796 0.0407 0.0016 -0.0197 70 GLN B CA 2082 C C . GLN B 72 ? 0.1872 0.2444 0.3377 0.0371 0.0056 -0.0212 70 GLN B C 2083 O O . GLN B 72 ? 0.1943 0.2435 0.3428 0.0412 0.0056 -0.0164 70 GLN B O 2084 C CB . GLN B 72 ? 0.2550 0.3385 0.4205 0.0386 -0.0104 -0.0176 70 GLN B CB 2085 C CG . GLN B 72 ? 0.3328 0.4342 0.5183 0.0449 -0.0205 -0.0129 70 GLN B CG 2086 C CD . GLN B 72 ? 0.4291 0.5300 0.6088 0.0539 -0.0291 -0.0020 70 GLN B CD 2087 O OE1 . GLN B 72 ? 0.5130 0.6188 0.6785 0.0546 -0.0400 0.0014 70 GLN B OE1 2088 N NE2 . GLN B 72 ? 0.4391 0.5331 0.6289 0.0608 -0.0234 0.0034 70 GLN B NE2 2089 N N . LYS B 73 ? 0.1900 0.2425 0.3243 0.0293 0.0092 -0.0275 71 LYS B N 2090 C CA . LYS B 73 ? 0.1418 0.1817 0.2548 0.0257 0.0115 -0.0296 71 LYS B CA 2091 C C . LYS B 73 ? 0.1307 0.1614 0.2477 0.0261 0.0207 -0.0347 71 LYS B C 2092 O O . LYS B 73 ? 0.1984 0.2205 0.3066 0.0258 0.0204 -0.0344 71 LYS B O 2093 C CB . LYS B 73 ? 0.0979 0.1357 0.1935 0.0186 0.0128 -0.0339 71 LYS B CB 2094 C CG . LYS B 73 ? 0.1273 0.1707 0.2171 0.0171 0.0042 -0.0305 71 LYS B CG 2095 C CD . LYS B 73 ? 0.1839 0.2249 0.2622 0.0201 -0.0043 -0.0248 71 LYS B CD 2096 C CE . LYS B 73 ? 0.1689 0.2173 0.2454 0.0198 -0.0129 -0.0231 71 LYS B CE 2097 N NZ . LYS B 73 ? 0.1855 0.2325 0.2498 0.0235 -0.0202 -0.0177 71 LYS B NZ 2098 N N . ARG B 74 ? 0.1303 0.1632 0.2619 0.0264 0.0296 -0.0403 72 ARG B N 2099 C CA . ARG B 74 ? 0.1858 0.2098 0.3224 0.0268 0.0395 -0.0476 72 ARG B CA 2100 C C . ARG B 74 ? 0.1844 0.2033 0.3374 0.0334 0.0393 -0.0430 72 ARG B C 2101 O O . ARG B 74 ? 0.1699 0.1780 0.3239 0.0326 0.0457 -0.0489 72 ARG B O 2102 C CB . ARG B 74 ? 0.1890 0.2170 0.3378 0.0261 0.0505 -0.0550 72 ARG B CB 2103 C CG . ARG B 74 ? 0.2085 0.2361 0.3377 0.0188 0.0554 -0.0609 72 ARG B CG 2104 C CD . ARG B 74 ? 0.1339 0.1685 0.2780 0.0184 0.0666 -0.0656 72 ARG B CD 2105 N NE . ARG B 74 ? 0.1853 0.2195 0.3104 0.0116 0.0715 -0.0681 72 ARG B NE 2106 C CZ . ARG B 74 ? 0.2486 0.2889 0.3828 0.0094 0.0822 -0.0711 72 ARG B CZ 2107 N NH1 . ARG B 74 ? 0.2434 0.2904 0.4030 0.0129 0.0860 -0.0711 72 ARG B NH1 2108 N NH2 . ARG B 74 ? 0.2892 0.3269 0.4039 0.0034 0.0872 -0.0715 72 ARG B NH2 2109 N N . ALA B 75 ? 0.1436 0.1702 0.3095 0.0399 0.0321 -0.0326 73 ALA B N 2110 C CA . ALA B 75 ? 0.1507 0.1722 0.3315 0.0474 0.0318 -0.0250 73 ALA B CA 2111 C C . ALA B 75 ? 0.1734 0.1889 0.3405 0.0477 0.0253 -0.0170 73 ALA B C 2112 O O . ALA B 75 ? 0.2043 0.2127 0.3799 0.0529 0.0261 -0.0094 73 ALA B O 2113 C CB . ALA B 75 ? 0.1253 0.1584 0.3214 0.0540 0.0265 -0.0163 73 ALA B CB 2114 N N . ALA B 76 ? 0.1578 0.1753 0.3028 0.0419 0.0196 -0.0180 74 ALA B N 2115 C CA . ALA B 76 ? 0.1629 0.1774 0.2940 0.0421 0.0134 -0.0104 74 ALA B CA 2116 C C . ALA B 76 ? 0.1949 0.1963 0.3280 0.0410 0.0191 -0.0106 74 ALA B C 2117 O O . ALA B 76 ? 0.1559 0.1540 0.2883 0.0444 0.0170 -0.0007 74 ALA B O 2118 C CB . ALA B 76 ? 0.1277 0.1459 0.2371 0.0360 0.0081 -0.0134 74 ALA B CB 2119 N N . VAL B 77 ? 0.2139 0.2081 0.3491 0.0359 0.0266 -0.0221 75 VAL B N 2120 C CA . VAL B 77 ? 0.1716 0.1538 0.3119 0.0334 0.0320 -0.0249 75 VAL B CA 2121 C C . VAL B 77 ? 0.1934 0.1680 0.3542 0.0407 0.0361 -0.0153 75 VAL B C 2122 O O . VAL B 77 ? 0.2217 0.1872 0.3862 0.0399 0.0388 -0.0111 75 VAL B O 2123 C CB . VAL B 77 ? 0.1931 0.1693 0.3336 0.0271 0.0392 -0.0411 75 VAL B CB 2124 C CG1 . VAL B 77 ? 0.1327 0.1138 0.2503 0.0199 0.0346 -0.0484 75 VAL B CG1 2125 C CG2 . VAL B 77 ? 0.1424 0.1200 0.2953 0.0302 0.0457 -0.0467 75 VAL B CG2 2126 N N . ASP B 78 ? 0.1737 0.1528 0.3463 0.0470 0.0364 -0.0108 76 ASP B N 2127 C CA . ASP B 78 ? 0.2093 0.1833 0.3936 0.0529 0.0380 0.0005 76 ASP B CA 2128 C C . ASP B 78 ? 0.2384 0.2200 0.4172 0.0604 0.0293 0.0166 76 ASP B C 2129 O O . ASP B 78 ? 0.2901 0.2648 0.4676 0.0630 0.0299 0.0274 76 ASP B O 2130 C CB . ASP B 78 ? 0.1735 0.1494 0.3716 0.0553 0.0422 -0.0033 76 ASP B CB 2131 C CG . ASP B 78 ? 0.2062 0.1730 0.4088 0.0484 0.0520 -0.0182 76 ASP B CG 2132 O OD1 . ASP B 78 ? 0.2290 0.1857 0.4291 0.0427 0.0557 -0.0231 76 ASP B OD1 2133 O OD2 . ASP B 78 ? 0.2560 0.2267 0.4647 0.0483 0.0558 -0.0253 76 ASP B OD2 2134 N N . THR B 79 ? 0.2053 0.2016 0.3803 0.0634 0.0213 0.0178 77 THR B N 2135 C CA . THR B 79 ? 0.2097 0.2157 0.3787 0.0707 0.0115 0.0311 77 THR B CA 2136 C C . THR B 79 ? 0.2186 0.2258 0.3693 0.0699 0.0061 0.0369 77 THR B C 2137 O O . THR B 79 ? 0.1975 0.2092 0.3381 0.0753 -0.0006 0.0484 77 THR B O 2138 C CB . THR B 79 ? 0.2307 0.2539 0.4041 0.0729 0.0041 0.0284 77 THR B CB 2139 O OG1 . THR B 79 ? 0.2331 0.2628 0.3998 0.0667 0.0021 0.0191 77 THR B OG1 2140 C CG2 . THR B 79 ? 0.2162 0.2396 0.4084 0.0741 0.0103 0.0231 77 THR B CG2 2141 N N . TYR B 80 ? 0.1973 0.2005 0.3385 0.0617 0.0089 0.0277 78 TYR B N 2142 C CA . TYR B 80 ? 0.1828 0.1876 0.3020 0.0584 0.0042 0.0303 78 TYR B CA 2143 C C . TYR B 80 ? 0.2111 0.2036 0.3290 0.0536 0.0117 0.0296 78 TYR B C 2144 O O . TYR B 80 ? 0.2334 0.2216 0.3470 0.0566 0.0129 0.0405 78 TYR B O 2145 C CB . TYR B 80 ? 0.1208 0.1342 0.2266 0.0519 -0.0009 0.0198 78 TYR B CB 2146 C CG . TYR B 80 ? 0.1640 0.1785 0.2487 0.0483 -0.0047 0.0204 78 TYR B CG 2147 C CD1 . TYR B 80 ? 0.1593 0.1785 0.2320 0.0532 -0.0107 0.0299 78 TYR B CD1 2148 C CD2 . TYR B 80 ? 0.1453 0.1565 0.2214 0.0407 -0.0025 0.0111 78 TYR B CD2 2149 C CE1 . TYR B 80 ? 0.1681 0.1878 0.2223 0.0504 -0.0128 0.0294 78 TYR B CE1 2150 C CE2 . TYR B 80 ? 0.1656 0.1781 0.2251 0.0385 -0.0055 0.0117 78 TYR B CE2 2151 C CZ . TYR B 80 ? 0.1812 0.1975 0.2305 0.0432 -0.0100 0.0204 78 TYR B CZ 2152 O OH . TYR B 80 ? 0.2041 0.2211 0.2378 0.0414 -0.0116 0.0200 78 TYR B OH 2153 N N . CYS B 81 ? 0.1317 0.1191 0.2533 0.0461 0.0167 0.0166 79 CYS B N 2154 C CA . CYS B 81 ? 0.2092 0.1876 0.3320 0.0402 0.0224 0.0132 79 CYS B CA 2155 C C . CYS B 81 ? 0.1933 0.1590 0.3344 0.0432 0.0309 0.0205 79 CYS B C 2156 O O . CYS B 81 ? 0.1926 0.1538 0.3323 0.0434 0.0335 0.0293 79 CYS B O 2157 C CB . CYS B 81 ? 0.1297 0.1072 0.2515 0.0319 0.0244 -0.0033 79 CYS B CB 2158 S SG . CYS B 81 ? 0.1711 0.1602 0.2708 0.0279 0.0163 -0.0102 79 CYS B SG 2159 N N . ARG B 82 ? 0.2008 0.1598 0.3601 0.0455 0.0364 0.0168 80 ARG B N 2160 C CA . ARG B 82 ? 0.1955 0.1418 0.3706 0.0467 0.0447 0.0229 80 ARG B CA 2161 C C . ARG B 82 ? 0.2374 0.1848 0.4079 0.0549 0.0425 0.0423 80 ARG B C 2162 O O . ARG B 82 ? 0.2860 0.2242 0.4615 0.0546 0.0489 0.0509 80 ARG B O 2163 C CB . ARG B 82 ? 0.1790 0.1214 0.3678 0.0457 0.0497 0.0141 80 ARG B CB 2164 C CG . ARG B 82 ? 0.2698 0.2076 0.4620 0.0360 0.0545 -0.0050 80 ARG B CG 2165 C CD . ARG B 82 ? 0.2408 0.1749 0.4448 0.0353 0.0604 -0.0135 80 ARG B CD 2166 N NE . ARG B 82 ? 0.3398 0.2800 0.5356 0.0312 0.0593 -0.0288 80 ARG B NE 2167 C CZ . ARG B 82 ? 0.3123 0.2496 0.5055 0.0228 0.0627 -0.0449 80 ARG B CZ 2168 N NH1 . ARG B 82 ? 0.2167 0.1457 0.4179 0.0170 0.0669 -0.0492 80 ARG B NH1 2169 N NH2 . ARG B 82 ? 0.3729 0.3165 0.5547 0.0200 0.0619 -0.0566 80 ARG B NH2 2170 N N . HIS B 83 ? 0.1777 0.1370 0.3385 0.0618 0.0336 0.0486 81 HIS B N 2171 C CA . HIS B 83 ? 0.2092 0.1717 0.3608 0.0697 0.0295 0.0654 81 HIS B CA 2172 C C . HIS B 83 ? 0.2190 0.1797 0.3560 0.0688 0.0304 0.0741 81 HIS B C 2173 O O . HIS B 83 ? 0.2759 0.2294 0.4127 0.0711 0.0357 0.0858 81 HIS B O 2174 C CB . HIS B 83 ? 0.1855 0.1636 0.3284 0.0757 0.0178 0.0674 81 HIS B CB 2175 C CG . HIS B 83 ? 0.2350 0.2179 0.3643 0.0833 0.0116 0.0823 81 HIS B CG 2176 N ND1 . HIS B 83 ? 0.2673 0.2483 0.4036 0.0903 0.0114 0.0916 81 HIS B ND1 2177 C CD2 . HIS B 83 ? 0.2327 0.2221 0.3404 0.0849 0.0054 0.0888 81 HIS B CD2 2178 C CE1 . HIS B 83 ? 0.2977 0.2840 0.4167 0.0958 0.0048 0.1032 81 HIS B CE1 2179 N NE2 . HIS B 83 ? 0.2226 0.2140 0.3234 0.0923 0.0014 0.1011 81 HIS B NE2 2180 N N . ASN B 84 ? 0.2045 0.1720 0.3300 0.0657 0.0260 0.0683 82 ASN B N 2181 C CA . ASN B 84 ? 0.2166 0.1846 0.3264 0.0648 0.0268 0.0753 82 ASN B CA 2182 C C . ASN B 84 ? 0.2242 0.1794 0.3456 0.0587 0.0384 0.0754 82 ASN B C 2183 O O . ASN B 84 ? 0.2489 0.2009 0.3637 0.0600 0.0433 0.0867 82 ASN B O 2184 C CB . ASN B 84 ? 0.2544 0.2345 0.3453 0.0595 0.0188 0.0647 82 ASN B CB 2185 C CG . ASN B 84 ? 0.2747 0.2674 0.3511 0.0655 0.0077 0.0677 82 ASN B CG 2186 O OD1 . ASN B 84 ? 0.2705 0.2652 0.3464 0.0744 0.0048 0.0800 82 ASN B OD1 2187 N ND2 . ASN B 84 ? 0.1496 0.1512 0.2149 0.0607 0.0012 0.0565 82 ASN B ND2 2188 N N . TYR B 85 ? 0.2092 0.1580 0.3482 0.0515 0.0431 0.0620 83 TYR B N 2189 C CA . TYR B 85 ? 0.2161 0.1533 0.3710 0.0445 0.0536 0.0595 83 TYR B CA 2190 C C . TYR B 85 ? 0.2690 0.1968 0.4320 0.0488 0.0617 0.0744 83 TYR B C 2191 O O . TYR B 85 ? 0.3149 0.2376 0.4806 0.0464 0.0695 0.0820 83 TYR B O 2192 C CB . TYR B 85 ? 0.2452 0.1779 0.4162 0.0367 0.0559 0.0408 83 TYR B CB 2193 C CG . TYR B 85 ? 0.2792 0.2028 0.4673 0.0271 0.0645 0.0332 83 TYR B CG 2194 C CD1 . TYR B 85 ? 0.2574 0.1702 0.4632 0.0259 0.0743 0.0379 83 TYR B CD1 2195 C CD2 . TYR B 85 ? 0.2468 0.1791 0.4303 0.0177 0.0608 0.0197 83 TYR B CD2 2196 C CE1 . TYR B 85 ? 0.2501 0.1578 0.4729 0.0161 0.0815 0.0293 83 TYR B CE1 2197 C CE2 . TYR B 85 ? 0.2142 0.1410 0.4158 0.0083 0.0673 0.0114 83 TYR B CE2 2198 C CZ . TYR B 85 ? 0.2580 0.1705 0.4813 0.0073 0.0783 0.0159 83 TYR B CZ 2199 O OH . TYR B 85 ? 0.2923 0.2037 0.5334 -0.0028 0.0837 0.0061 83 TYR B OH 2200 N N . GLY B 86 ? 0.2170 0.1447 0.3832 0.0546 0.0597 0.0779 84 GLY B N 2201 C CA . GLY B 86 ? 0.2396 0.1603 0.4118 0.0595 0.0658 0.0915 84 GLY B CA 2202 C C . GLY B 86 ? 0.2520 0.1763 0.4053 0.0659 0.0649 0.1089 84 GLY B C 2203 O O . GLY B 86 ? 0.4258 0.3423 0.5836 0.0671 0.0737 0.1200 84 GLY B O 2204 N N . VAL B 87 ? 0.2424 0.1789 0.3740 0.0700 0.0543 0.1104 85 VAL B N 2205 C CA . VAL B 87 ? 0.3305 0.2730 0.4388 0.0761 0.0512 0.1242 85 VAL B CA 2206 C C . VAL B 87 ? 0.3267 0.2655 0.4300 0.0718 0.0604 0.1287 85 VAL B C 2207 O O . VAL B 87 ? 0.3554 0.2919 0.4493 0.0756 0.0658 0.1418 85 VAL B O 2208 C CB . VAL B 87 ? 0.3516 0.3093 0.4388 0.0800 0.0368 0.1206 85 VAL B CB 2209 C CG1 . VAL B 87 ? 0.3764 0.3405 0.4373 0.0848 0.0338 0.1315 85 VAL B CG1 2210 C CG2 . VAL B 87 ? 0.2432 0.2064 0.3368 0.0849 0.0281 0.1179 85 VAL B CG2 2211 N N . GLY B 88 ? 0.2864 0.2246 0.3969 0.0641 0.0626 0.1176 86 GLY B N 2212 C CA . GLY B 88 ? 0.2408 0.1783 0.3475 0.0596 0.0699 0.1198 86 GLY B CA 2213 C C . GLY B 88 ? 0.2669 0.1937 0.4000 0.0506 0.0826 0.1157 86 GLY B C 2214 O O . GLY B 88 ? 0.3518 0.2785 0.4864 0.0460 0.0902 0.1177 86 GLY B O 2215 N N . GLU B 89 ? 0.2736 0.1927 0.4281 0.0476 0.0849 0.1086 87 GLU B N 2216 C CA . GLU B 89 ? 0.3135 0.2241 0.4950 0.0376 0.0948 0.0994 87 GLU B CA 2217 C C . GLU B 89 ? 0.3288 0.2345 0.5182 0.0357 0.1077 0.1097 87 GLU B C 2218 O O . GLU B 89 ? 0.3051 0.2106 0.5098 0.0266 0.1139 0.1021 87 GLU B O 2219 C CB . GLU B 89 ? 0.3700 0.2734 0.5696 0.0365 0.0956 0.0912 87 GLU B CB 2220 C CG . GLU B 89 ? 0.4718 0.3670 0.6988 0.0269 0.1057 0.0811 87 GLU B CG 2221 C CD . GLU B 89 ? 0.5417 0.4307 0.7837 0.0262 0.1062 0.0713 87 GLU B CD 2222 O OE1 . GLU B 89 ? 0.5668 0.4590 0.7994 0.0319 0.0983 0.0702 87 GLU B OE1 2223 O OE2 . GLU B 89 ? 0.5924 0.4740 0.8562 0.0199 0.1147 0.0642 87 GLU B OE2 2224 N N . SER B 90 ? 0.3566 0.2594 0.5360 0.0443 0.1114 0.1264 88 SER B N 2225 C CA . SER B 90 ? 0.3758 0.2725 0.5629 0.0437 0.1247 0.1371 88 SER B CA 2226 C C . SER B 90 ? 0.3701 0.2733 0.5482 0.0406 0.1292 0.1397 88 SER B C 2227 O O . SER B 90 ? 0.3722 0.2714 0.5653 0.0360 0.1410 0.1419 88 SER B O 2228 C CB . SER B 90 ? 0.3367 0.2290 0.5118 0.0545 0.1267 0.1550 88 SER B CB 2229 O OG . SER B 90 ? 0.4979 0.3995 0.6412 0.0624 0.1198 0.1651 88 SER B OG 2230 N N . PHE B 91 ? 0.3894 0.3031 0.5442 0.0433 0.1203 0.1390 89 PHE B N 2231 C CA . PHE B 91 ? 0.3813 0.3024 0.5259 0.0413 0.1247 0.1413 89 PHE B CA 2232 C C . PHE B 91 ? 0.3591 0.2884 0.5078 0.0336 0.1193 0.1273 89 PHE B C 2233 O O . PHE B 91 ? 0.3349 0.2727 0.4738 0.0324 0.1218 0.1283 89 PHE B O 2234 C CB . PHE B 91 ? 0.3056 0.2325 0.4157 0.0517 0.1218 0.1546 89 PHE B CB 2235 C CG . PHE B 91 ? 0.2948 0.2287 0.3824 0.0584 0.1063 0.1527 89 PHE B CG 2236 C CD1 . PHE B 91 ? 0.2754 0.2191 0.3486 0.0575 0.0980 0.1448 89 PHE B CD1 2237 C CD2 . PHE B 91 ? 0.3898 0.3212 0.4719 0.0657 0.0999 0.1586 89 PHE B CD2 2238 C CE1 . PHE B 91 ? 0.3129 0.2637 0.3670 0.0633 0.0835 0.1416 89 PHE B CE1 2239 C CE2 . PHE B 91 ? 0.3634 0.3032 0.4276 0.0711 0.0850 0.1552 89 PHE B CE2 2240 C CZ . PHE B 91 ? 0.3523 0.3018 0.4027 0.0697 0.0767 0.1462 89 PHE B CZ 2241 N N . THR B 92 ? 0.2591 0.2539 0.5045 0.0385 0.0611 0.0872 90 THR B N 2242 C CA . THR B 92 ? 0.2649 0.2545 0.4917 0.0385 0.0670 0.0791 90 THR B CA 2243 C C . THR B 92 ? 0.2690 0.2525 0.5033 0.0375 0.0734 0.0679 90 THR B C 2244 O O . THR B 92 ? 0.2763 0.2560 0.4996 0.0368 0.0741 0.0665 90 THR B O 2245 C CB . THR B 92 ? 0.2241 0.2152 0.4506 0.0391 0.0696 0.0764 90 THR B CB 2246 O OG1 . THR B 92 ? 0.1982 0.1919 0.4496 0.0393 0.0732 0.0709 90 THR B OG1 2247 C CG2 . THR B 92 ? 0.2091 0.2050 0.4264 0.0399 0.0612 0.0862 90 THR B CG2 2248 N N . VAL B 93 ? 0.2586 0.2421 0.5117 0.0380 0.0777 0.0588 91 VAL B N 2249 C CA . VAL B 93 ? 0.2399 0.2192 0.5012 0.0379 0.0827 0.0449 91 VAL B CA 2250 C C . VAL B 93 ? 0.2396 0.2151 0.5108 0.0368 0.0778 0.0477 91 VAL B C 2251 O O . VAL B 93 ? 0.2082 0.1788 0.4747 0.0360 0.0798 0.0403 91 VAL B O 2252 C CB . VAL B 93 ? 0.2239 0.2076 0.5068 0.0398 0.0861 0.0340 91 VAL B CB 2253 C CG1 . VAL B 93 ? 0.1963 0.1773 0.4884 0.0406 0.0895 0.0177 91 VAL B CG1 2254 C CG2 . VAL B 93 ? 0.1712 0.1624 0.4459 0.0402 0.0924 0.0305 91 VAL B CG2 2255 N N . GLN B 94 ? 0.2644 0.2434 0.5506 0.0366 0.0711 0.0591 92 GLN B N 2256 C CA . GLN B 94 ? 0.2869 0.2647 0.5884 0.0352 0.0660 0.0639 92 GLN B CA 2257 C C . GLN B 94 ? 0.2671 0.2486 0.5525 0.0339 0.0626 0.0768 92 GLN B C 2258 O O . GLN B 94 ? 0.3132 0.2964 0.6116 0.0324 0.0584 0.0836 92 GLN B O 2259 C CB . GLN B 94 ? 0.2865 0.2673 0.6167 0.0355 0.0603 0.0696 92 GLN B CB 2260 C CG . GLN B 94 ? 0.3120 0.2902 0.6619 0.0379 0.0633 0.0549 92 GLN B CG 2261 C CD . GLN B 94 ? 0.3776 0.3584 0.7569 0.0386 0.0571 0.0606 92 GLN B CD 2262 O OE1 . GLN B 94 ? 0.4247 0.4091 0.8114 0.0366 0.0500 0.0762 92 GLN B OE1 2263 N NE2 . GLN B 94 ? 0.3822 0.3628 0.7788 0.0416 0.0597 0.0478 92 GLN B NE2 2264 N N . ARG B 95 ? 0.2255 0.2094 0.4842 0.0347 0.0642 0.0800 93 ARG B N 2265 C CA . ARG B 95 ? 0.2290 0.2181 0.4707 0.0348 0.0613 0.0901 93 ARG B CA 2266 C C . ARG B 95 ? 0.2095 0.1944 0.4479 0.0335 0.0634 0.0861 93 ARG B C 2267 O O . ARG B 95 ? 0.2195 0.1970 0.4482 0.0334 0.0682 0.0748 93 ARG B O 2268 C CB . ARG B 95 ? 0.2281 0.2193 0.4426 0.0367 0.0614 0.0915 93 ARG B CB 2269 C CG . ARG B 95 ? 0.2097 0.2065 0.4047 0.0380 0.0586 0.0994 93 ARG B CG 2270 C CD . ARG B 95 ? 0.2035 0.2005 0.3733 0.0406 0.0570 0.0986 93 ARG B CD 2271 N NE . ARG B 95 ? 0.1713 0.1726 0.3214 0.0427 0.0553 0.1027 93 ARG B NE 2272 C CZ . ARG B 95 ? 0.1859 0.1981 0.3329 0.0446 0.0513 0.1135 93 ARG B CZ 2273 N NH1 . ARG B 95 ? 0.1889 0.2078 0.3504 0.0439 0.0477 0.1219 93 ARG B NH1 2274 N NH2 . ARG B 95 ? 0.1539 0.1714 0.2833 0.0475 0.0512 0.1162 93 ARG B NH2 2275 N N . ARG B 96 ? 0.2421 0.2326 0.4896 0.0324 0.0596 0.0960 94 ARG B N 2276 C CA . ARG B 96 ? 0.2628 0.2506 0.5100 0.0310 0.0606 0.0939 94 ARG B CA 2277 C C . ARG B 96 ? 0.2342 0.2332 0.4753 0.0312 0.0579 0.1079 94 ARG B C 2278 O O . ARG B 96 ? 0.2309 0.2388 0.4881 0.0302 0.0534 0.1203 94 ARG B O 2279 C CB . ARG B 96 ? 0.3167 0.2992 0.5938 0.0287 0.0585 0.0893 94 ARG B CB 2280 C CG . ARG B 96 ? 0.3998 0.3728 0.6852 0.0294 0.0616 0.0733 94 ARG B CG 2281 C CD . ARG B 96 ? 0.4704 0.4352 0.7396 0.0296 0.0670 0.0588 94 ARG B CD 2282 N NE . ARG B 96 ? 0.5601 0.5189 0.8395 0.0306 0.0702 0.0423 94 ARG B NE 2283 C CZ . ARG B 96 ? 0.6493 0.6032 0.9501 0.0304 0.0682 0.0317 94 ARG B CZ 2284 N NH1 . ARG B 96 ? 0.6564 0.6093 0.9726 0.0283 0.0625 0.0372 94 ARG B NH1 2285 N NH2 . ARG B 96 ? 0.6905 0.6418 0.9979 0.0325 0.0717 0.0149 94 ARG B NH2 2286 N N . VAL B 97 ? 0.1825 0.1824 0.4019 0.0326 0.0603 0.1069 95 VAL B N 2287 C CA . VAL B 97 ? 0.2005 0.2134 0.4170 0.0332 0.0584 0.1200 95 VAL B CA 2288 C C . VAL B 97 ? 0.1983 0.2082 0.4137 0.0322 0.0603 0.1168 95 VAL B C 2289 O O . VAL B 97 ? 0.1737 0.1752 0.3708 0.0333 0.0635 0.1066 95 VAL B O 2290 C CB . VAL B 97 ? 0.3474 0.3684 0.5371 0.0374 0.0587 0.1242 95 VAL B CB 2291 C CG1 . VAL B 97 ? 0.3794 0.4174 0.5668 0.0389 0.0575 0.1379 95 VAL B CG1 2292 C CG2 . VAL B 97 ? 0.3600 0.3819 0.5486 0.0384 0.0561 0.1257 95 VAL B CG2 2293 N N . TYR B 98 ? 0.2282 0.2448 0.4643 0.0297 0.0575 0.1259 96 TYR B N 2294 C CA . TYR B 98 ? 0.2609 0.2752 0.4974 0.0285 0.0585 0.1235 96 TYR B CA 2295 C C . TYR B 98 ? 0.2495 0.2717 0.4594 0.0324 0.0616 0.1262 96 TYR B C 2296 O O . TYR B 98 ? 0.2544 0.2868 0.4500 0.0359 0.0619 0.1324 96 TYR B O 2297 C CB . TYR B 98 ? 0.2979 0.3209 0.5618 0.0251 0.0539 0.1356 96 TYR B CB 2298 C CG . TYR B 98 ? 0.2828 0.3250 0.5579 0.0249 0.0503 0.1548 96 TYR B CG 2299 C CD1 . TYR B 98 ? 0.2181 0.2635 0.5079 0.0238 0.0466 0.1613 96 TYR B CD1 2300 C CD2 . TYR B 98 ? 0.2990 0.3575 0.5708 0.0257 0.0504 0.1671 96 TYR B CD2 2301 C CE1 . TYR B 98 ? 0.2548 0.3190 0.5550 0.0228 0.0427 0.1802 96 TYR B CE1 2302 C CE2 . TYR B 98 ? 0.3355 0.4142 0.6168 0.0252 0.0472 0.1854 96 TYR B CE2 2303 C CZ . TYR B 98 ? 0.3268 0.4081 0.6218 0.0235 0.0432 0.1922 96 TYR B CZ 2304 O OH . TYR B 98 ? 0.3355 0.4381 0.6395 0.0222 0.0395 0.2117 96 TYR B OH 2305 N N . PRO B 99 ? 0.2244 0.2419 0.4282 0.0320 0.0634 0.1211 97 PRO B N 2306 C CA . PRO B 99 ? 0.2379 0.2642 0.4233 0.0357 0.0657 0.1248 97 PRO B CA 2307 C C . PRO B 99 ? 0.2280 0.2737 0.4257 0.0358 0.0643 0.1403 97 PRO B C 2308 O O . PRO B 99 ? 0.1859 0.2331 0.4087 0.0313 0.0610 0.1462 97 PRO B O 2309 C CB . PRO B 99 ? 0.2256 0.2366 0.4054 0.0338 0.0670 0.1125 97 PRO B CB 2310 C CG . PRO B 99 ? 0.2147 0.2150 0.4177 0.0286 0.0646 0.1070 97 PRO B CG 2311 C CD . PRO B 99 ? 0.1883 0.1889 0.4004 0.0285 0.0633 0.1080 97 PRO B CD 2312 N N . GLU B 100 ? 0.2575 0.3185 0.4374 0.0412 0.0664 0.1465 98 GLU B N 2313 C CA . GLU B 100 ? 0.3349 0.4157 0.5212 0.0421 0.0661 0.1594 98 GLU B CA 2314 C C . GLU B 100 ? 0.2976 0.3723 0.4776 0.0425 0.0684 0.1529 98 GLU B C 2315 O O . GLU B 100 ? 0.2774 0.3432 0.4363 0.0462 0.0712 0.1426 98 GLU B O 2316 C CB . GLU B 100 ? 0.4315 0.5345 0.5995 0.0488 0.0674 0.1676 98 GLU B CB 2317 C CG . GLU B 100 ? 0.5262 0.6373 0.6971 0.0485 0.0650 0.1747 98 GLU B CG 2318 C CD . GLU B 100 ? 0.6265 0.7503 0.8240 0.0432 0.0611 0.1904 98 GLU B CD 2319 O OE1 . GLU B 100 ? 0.6724 0.7934 0.8826 0.0400 0.0578 0.1942 98 GLU B OE1 2320 O OE2 . GLU B 100 ? 0.6650 0.8020 0.8714 0.0420 0.0607 0.1997 98 GLU B OE2 2321 N N . VAL B 101 ? 0.2676 0.3471 0.4670 0.0383 0.0666 0.1595 99 VAL B N 2322 C CA . VAL B 101 ? 0.2466 0.3206 0.4437 0.0373 0.0681 0.1540 99 VAL B CA 2323 C C . VAL B 101 ? 0.2504 0.3474 0.4491 0.0390 0.0688 0.1658 99 VAL B C 2324 O O . VAL B 101 ? 0.2739 0.3840 0.4917 0.0357 0.0657 0.1789 99 VAL B O 2325 C CB . VAL B 101 ? 0.2184 0.2735 0.4371 0.0296 0.0645 0.1469 99 VAL B CB 2326 C CG1 . VAL B 101 ? 0.1503 0.1992 0.3657 0.0279 0.0655 0.1407 99 VAL B CG1 2327 C CG2 . VAL B 101 ? 0.1780 0.2125 0.3935 0.0281 0.0640 0.1337 99 VAL B CG2 2328 N N . THR B 102 ? 0.2283 0.3312 0.4071 0.0441 0.0727 0.1605 100 THR B N 2329 C CA . THR B 102 ? 0.3238 0.4503 0.5010 0.0464 0.0742 0.1675 100 THR B CA 2330 C C . THR B 102 ? 0.3263 0.4480 0.5048 0.0454 0.0754 0.1584 100 THR B C 2331 O O . THR B 102 ? 0.3337 0.4423 0.5000 0.0482 0.0770 0.1450 100 THR B O 2332 C CB . THR B 102 ? 0.3936 0.5395 0.5447 0.0559 0.0771 0.1665 100 THR B CB 2333 O OG1 . THR B 102 ? 0.4970 0.6287 0.6273 0.0614 0.0786 0.1519 100 THR B OG1 2334 C CG2 . THR B 102 ? 0.3917 0.5508 0.5446 0.0564 0.0755 0.1784 100 THR B CG2 2335 N N . VAL B 103 ? 0.3055 0.4398 0.5006 0.0416 0.0741 0.1658 101 VAL B N 2336 C CA . VAL B 103 ? 0.3152 0.4508 0.5139 0.0415 0.0743 0.1575 101 VAL B CA 2337 C C . VAL B 103 ? 0.3380 0.5017 0.5284 0.0478 0.0767 0.1600 101 VAL B C 2338 O O . VAL B 103 ? 0.3734 0.5562 0.5716 0.0459 0.0771 0.1737 101 VAL B O 2339 C CB . VAL B 103 ? 0.3241 0.4489 0.5521 0.0310 0.0696 0.1606 101 VAL B CB 2340 C CG1 . VAL B 103 ? 0.3135 0.4455 0.5478 0.0314 0.0685 0.1536 101 VAL B CG1 2341 C CG2 . VAL B 103 ? 0.3122 0.4078 0.5462 0.0253 0.0672 0.1527 101 VAL B CG2 2342 N N . TYR B 104 ? 0.3064 0.4729 0.4821 0.0558 0.0774 0.1458 102 TYR B N 2343 C CA . TYR B 104 ? 0.2867 0.4782 0.4555 0.0631 0.0789 0.1431 102 TYR B CA 2344 C C . TYR B 104 ? 0.2972 0.4850 0.4682 0.0675 0.0754 0.1292 102 TYR B C 2345 O O . TYR B 104 ? 0.2668 0.4329 0.4332 0.0691 0.0716 0.1184 102 TYR B O 2346 C CB . TYR B 104 ? 0.2513 0.4549 0.3942 0.0730 0.0816 0.1386 102 TYR B CB 2347 C CG . TYR B 104 ? 0.2496 0.4340 0.3720 0.0801 0.0794 0.1228 102 TYR B CG 2348 C CD1 . TYR B 104 ? 0.2600 0.4419 0.3714 0.0893 0.0759 0.1059 102 TYR B CD1 2349 C CD2 . TYR B 104 ? 0.2608 0.4287 0.3766 0.0776 0.0796 0.1252 102 TYR B CD2 2350 C CE1 . TYR B 104 ? 0.2785 0.4404 0.3721 0.0954 0.0717 0.0924 102 TYR B CE1 2351 C CE2 . TYR B 104 ? 0.2642 0.4144 0.3621 0.0836 0.0770 0.1117 102 TYR B CE2 2352 C CZ . TYR B 104 ? 0.3213 0.4678 0.4077 0.0923 0.0726 0.0957 102 TYR B CZ 2353 O OH . TYR B 104 ? 0.3824 0.5087 0.4519 0.0976 0.0677 0.0832 102 TYR B OH 2354 N N . PRO B 105 ? 0.3298 0.5392 0.5087 0.0699 0.0757 0.1299 103 PRO B N 2355 C CA . PRO B 105 ? 0.3272 0.5340 0.5108 0.0747 0.0705 0.1174 103 PRO B CA 2356 C C . PRO B 105 ? 0.3447 0.5509 0.5050 0.0882 0.0684 0.1004 103 PRO B C 2357 O O . PRO B 105 ? 0.4022 0.6205 0.5459 0.0943 0.0723 0.0985 103 PRO B O 2358 C CB . PRO B 105 ? 0.3150 0.5473 0.5175 0.0719 0.0720 0.1255 103 PRO B CB 2359 C CG . PRO B 105 ? 0.3327 0.5866 0.5275 0.0724 0.0790 0.1363 103 PRO B CG 2360 C CD . PRO B 105 ? 0.3383 0.5754 0.5254 0.0675 0.0800 0.1435 103 PRO B CD 2361 N N . ALA B 106 ? 0.2930 0.4838 0.4531 0.0928 0.0606 0.0883 104 ALA B N 2362 C CA . ALA B 106 ? 0.2793 0.4642 0.4210 0.1050 0.0551 0.0715 104 ALA B CA 2363 C C . ALA B 106 ? 0.3372 0.5193 0.4894 0.1095 0.0460 0.0629 104 ALA B C 2364 O O . ALA B 106 ? 0.2971 0.4851 0.4706 0.1034 0.0445 0.0701 104 ALA B O 2365 C CB . ALA B 106 ? 0.1603 0.3171 0.2827 0.1062 0.0516 0.0655 104 ALA B CB 2366 N N . LYS B 107 ? 0.3971 0.5692 0.5357 0.1198 0.0384 0.0477 105 LYS B N 2367 C CA . LYS B 107 ? 0.4158 0.5835 0.5637 0.1252 0.0276 0.0390 105 LYS B CA 2368 C C . LYS B 107 ? 0.4355 0.5682 0.5672 0.1266 0.0149 0.0301 105 LYS B C 2369 O O . LYS B 107 ? 0.4289 0.5489 0.5423 0.1306 0.0141 0.0241 105 LYS B O 2370 C CB . LYS B 107 ? 0.4337 0.6231 0.5847 0.1353 0.0283 0.0284 105 LYS B CB 2371 C CG . LYS B 107 ? 0.4376 0.6621 0.6024 0.1329 0.0400 0.0374 105 LYS B CG 2372 C CD . LYS B 107 ? 0.4478 0.6932 0.6137 0.1441 0.0413 0.0256 105 LYS B CD 2373 C CE . LYS B 107 ? 0.4483 0.7300 0.6276 0.1416 0.0526 0.0356 105 LYS B CE 2374 N NZ . LYS B 107 ? 0.4562 0.7599 0.6375 0.1533 0.0544 0.0233 105 LYS B NZ 2375 N N . THR B 108 ? 0.4917 0.6073 0.6289 0.1202 0.0037 0.0294 106 THR B N 2376 C CA . THR B 108 ? 0.5570 0.6395 0.6790 0.1179 -0.0104 0.0226 106 THR B CA 2377 C C . THR B 108 ? 0.6563 0.7410 0.7806 0.1335 -0.0197 0.0104 106 THR B C 2378 O O . THR B 108 ? 0.6727 0.7345 0.7828 0.1360 -0.0291 0.0038 106 THR B O 2379 C CB . THR B 108 ? 0.5458 0.6126 0.6722 0.1056 -0.0200 0.0268 106 THR B CB 2380 O OG1 . THR B 108 ? 0.5371 0.6241 0.6868 0.1100 -0.0231 0.0274 106 THR B OG1 2381 C CG2 . THR B 108 ? 0.5337 0.5945 0.6574 0.0908 -0.0125 0.0355 106 THR B CG2 2382 N N . GLN B 109 ? 0.7223 0.8340 0.8661 0.1419 -0.0173 0.0075 107 GLN B N 2383 C CA . GLN B 109 ? 0.8154 0.9283 0.9622 0.1504 -0.0230 -0.0046 107 GLN B CA 2384 C C . GLN B 109 ? 0.8779 1.0253 1.0327 0.1562 -0.0089 -0.0070 107 GLN B C 2385 O O . GLN B 109 ? 0.8777 1.0488 1.0455 0.1524 0.0006 0.0022 107 GLN B O 2386 C CB . GLN B 109 ? 0.8483 0.9549 1.0102 0.1513 -0.0364 -0.0055 107 GLN B CB 2387 C CG . GLN B 109 ? 0.8730 0.9443 1.0224 0.1435 -0.0522 -0.0032 107 GLN B CG 2388 C CD . GLN B 109 ? 0.9049 0.9693 1.0661 0.1429 -0.0665 -0.0036 107 GLN B CD 2389 O OE1 . GLN B 109 ? 0.9058 0.9810 1.0827 0.1397 -0.0688 0.0023 107 GLN B OE1 2390 N NE2 . GLN B 109 ? 0.9261 0.9723 1.0810 0.1452 -0.0772 -0.0105 107 GLN B NE2 2391 N N . PRO B 110 ? 0.9320 1.0827 1.0779 0.1646 -0.0080 -0.0187 108 PRO B N 2392 C CA . PRO B 110 ? 0.9574 1.1405 1.1040 0.1704 0.0049 -0.0218 108 PRO B CA 2393 C C . PRO B 110 ? 0.9759 1.1907 1.1460 0.1723 0.0114 -0.0182 108 PRO B C 2394 O O . PRO B 110 ? 0.9767 1.2187 1.1484 0.1696 0.0245 -0.0104 108 PRO B O 2395 C CB . PRO B 110 ? 0.9635 1.1391 1.0995 0.1808 -0.0016 -0.0384 108 PRO B CB 2396 C CG . PRO B 110 ? 0.9483 1.0859 1.0717 0.1768 -0.0146 -0.0405 108 PRO B CG 2397 C CD . PRO B 110 ? 0.9372 1.0609 1.0716 0.1686 -0.0209 -0.0298 108 PRO B CD 2398 N N . LEU B 111 ? 0.9873 1.1987 1.1753 0.1761 0.0020 -0.0223 109 LEU B N 2399 C CA . LEU B 111 ? 0.9765 1.2180 1.1894 0.1790 0.0069 -0.0203 109 LEU B CA 2400 C C . LEU B 111 ? 0.9435 1.1998 1.1738 0.1685 0.0118 -0.0049 109 LEU B C 2401 O O . LEU B 111 ? 0.9566 1.2443 1.2028 0.1683 0.0209 -0.0006 109 LEU B O 2402 C CB . LEU B 111 ? 0.9869 1.2185 1.2143 0.1864 -0.0061 -0.0286 109 LEU B CB 2403 N N . GLN B 112 ? 0.8903 1.1242 1.1165 0.1596 0.0054 0.0031 110 GLN B N 2404 C CA . GLN B 112 ? 0.8593 1.1016 1.1014 0.1491 0.0062 0.0169 110 GLN B CA 2405 C C . GLN B 112 ? 0.7976 1.0584 1.0370 0.1400 0.0213 0.0305 110 GLN B C 2406 O O . GLN B 112 ? 0.8395 1.1011 1.0598 0.1406 0.0299 0.0306 110 GLN B O 2407 C CB . GLN B 112 ? 0.8945 1.1058 1.1313 0.1433 -0.0068 0.0209 110 GLN B CB 2408 C CG . GLN B 112 ? 0.9609 1.1611 1.2117 0.1473 -0.0236 0.0160 110 GLN B CG 2409 C CD . GLN B 112 ? 1.0113 1.1742 1.2434 0.1446 -0.0383 0.0151 110 GLN B CD 2410 O OE1 . GLN B 112 ? 1.0067 1.1501 1.2208 0.1327 -0.0361 0.0210 110 GLN B OE1 2411 N NE2 . GLN B 112 ? 1.0535 1.1992 1.2822 0.1479 -0.0513 0.0086 110 GLN B NE2 2412 N N . HIS B 113 ? 0.6821 0.9560 0.9417 0.1305 0.0230 0.0433 111 HIS B N 2413 C CA . HIS B 113 ? 0.5689 0.8553 0.8301 0.1191 0.0349 0.0596 111 HIS B CA 2414 C C . HIS B 113 ? 0.4933 0.7529 0.7380 0.1122 0.0345 0.0649 111 HIS B C 2415 O O . HIS B 113 ? 0.4940 0.7265 0.7283 0.1147 0.0248 0.0578 111 HIS B O 2416 C CB . HIS B 113 ? 0.5224 0.8219 0.8116 0.1084 0.0336 0.0723 111 HIS B CB 2417 C CG . HIS B 113 ? 0.5186 0.8488 0.8268 0.1135 0.0362 0.0700 111 HIS B CG 2418 N ND1 . HIS B 113 ? 0.5006 0.8333 0.8154 0.1255 0.0281 0.0548 111 HIS B ND1 2419 C CD2 . HIS B 113 ? 0.5332 0.8923 0.8576 0.1077 0.0451 0.0817 111 HIS B CD2 2420 C CE1 . HIS B 113 ? 0.5083 0.8717 0.8429 0.1276 0.0332 0.0560 111 HIS B CE1 2421 N NE2 . HIS B 113 ? 0.5305 0.9110 0.8703 0.1167 0.0437 0.0727 111 HIS B NE2 2422 N N . HIS B 114 ? 0.4616 0.7282 0.7046 0.1033 0.0447 0.0781 112 HIS B N 2423 C CA . HIS B 114 ? 0.4649 0.7085 0.6969 0.0959 0.0456 0.0842 112 HIS B CA 2424 C C . HIS B 114 ? 0.4388 0.6585 0.6825 0.0878 0.0357 0.0867 112 HIS B C 2425 O O . HIS B 114 ? 0.4716 0.6966 0.7388 0.0780 0.0329 0.0953 112 HIS B O 2426 C CB . HIS B 114 ? 0.5052 0.7625 0.7415 0.0864 0.0561 0.1005 112 HIS B CB 2427 C CG . HIS B 114 ? 0.5496 0.8217 0.7659 0.0931 0.0649 0.0993 112 HIS B CG 2428 N ND1 . HIS B 114 ? 0.5804 0.8743 0.8001 0.0879 0.0734 0.1138 112 HIS B ND1 2429 C CD2 . HIS B 114 ? 0.5666 0.8344 0.7595 0.1043 0.0648 0.0855 112 HIS B CD2 2430 C CE1 . HIS B 114 ? 0.5999 0.9040 0.7982 0.0960 0.0785 0.1091 112 HIS B CE1 2431 N NE2 . HIS B 114 ? 0.5919 0.8802 0.7743 0.1059 0.0734 0.0911 112 HIS B NE2 2432 N N . ASN B 115 ? 0.3879 0.5733 0.6065 0.0877 0.0283 0.0760 113 ASN B N 2433 C CA . ASN B 115 ? 0.3510 0.5043 0.5647 0.0763 0.0167 0.0725 113 ASN B CA 2434 C C . ASN B 115 ? 0.3055 0.4287 0.4938 0.0711 0.0169 0.0687 113 ASN B C 2435 O O . ASN B 115 ? 0.2822 0.3780 0.4577 0.0643 0.0077 0.0625 113 ASN B O 2436 C CB . ASN B 115 ? 0.3756 0.5195 0.5871 0.0814 0.0032 0.0623 113 ASN B CB 2437 C CG . ASN B 115 ? 0.4210 0.5520 0.6099 0.0927 -0.0007 0.0509 113 ASN B CG 2438 O OD1 . ASN B 115 ? 0.4246 0.5593 0.6010 0.0989 0.0075 0.0495 113 ASN B OD1 2439 N ND2 . ASN B 115 ? 0.4860 0.6020 0.6712 0.0951 -0.0147 0.0434 113 ASN B ND2 2440 N N . LEU B 116 ? 0.3016 0.4325 0.4830 0.0742 0.0275 0.0731 114 LEU B N 2441 C CA . LEU B 116 ? 0.3228 0.4290 0.4834 0.0698 0.0288 0.0705 114 LEU B CA 2442 C C . LEU B 116 ? 0.3099 0.4279 0.4791 0.0658 0.0399 0.0825 114 LEU B C 2443 O O . LEU B 116 ? 0.3070 0.4523 0.4820 0.0727 0.0484 0.0895 114 LEU B O 2444 C CB . LEU B 116 ? 0.3759 0.4748 0.5136 0.0808 0.0269 0.0606 114 LEU B CB 2445 C CG . LEU B 116 ? 0.4681 0.5373 0.5822 0.0769 0.0238 0.0548 114 LEU B CG 2446 C CD1 . LEU B 116 ? 0.4914 0.5362 0.5995 0.0676 0.0134 0.0501 114 LEU B CD1 2447 C CD2 . LEU B 116 ? 0.4912 0.5576 0.5885 0.0886 0.0211 0.0463 114 LEU B CD2 2448 N N . LEU B 117 ? 0.2597 0.3581 0.4299 0.0549 0.0393 0.0848 115 LEU B N 2449 C CA . LEU B 117 ? 0.1880 0.2930 0.3671 0.0509 0.0478 0.0964 115 LEU B CA 2450 C C . LEU B 117 ? 0.1706 0.2548 0.3271 0.0517 0.0491 0.0905 115 LEU B C 2451 O O . LEU B 117 ? 0.1761 0.2345 0.3212 0.0467 0.0436 0.0811 115 LEU B O 2452 C CB . LEU B 117 ? 0.1490 0.2486 0.3526 0.0384 0.0456 0.1037 115 LEU B CB 2453 C CG . LEU B 117 ? 0.3661 0.4877 0.5977 0.0353 0.0441 0.1125 115 LEU B CG 2454 C CD1 . LEU B 117 ? 0.3781 0.4911 0.6355 0.0224 0.0405 0.1194 115 LEU B CD1 2455 C CD2 . LEU B 117 ? 0.3537 0.5124 0.5949 0.0424 0.0537 0.1256 115 LEU B CD2 2456 N N . VAL B 118 ? 0.2031 0.3009 0.3534 0.0580 0.0564 0.0963 116 VAL B N 2457 C CA . VAL B 118 ? 0.1808 0.2620 0.3118 0.0594 0.0576 0.0917 116 VAL B CA 2458 C C . VAL B 118 ? 0.2127 0.2918 0.3554 0.0526 0.0626 0.1027 116 VAL B C 2459 O O . VAL B 118 ? 0.1997 0.3012 0.3572 0.0526 0.0684 0.1172 116 VAL B O 2460 C CB . VAL B 118 ? 0.1966 0.2918 0.3107 0.0716 0.0604 0.0888 116 VAL B CB 2461 C CG1 . VAL B 118 ? 0.1716 0.2483 0.2670 0.0722 0.0599 0.0840 116 VAL B CG1 2462 C CG2 . VAL B 118 ? 0.1518 0.2491 0.2580 0.0799 0.0542 0.0773 116 VAL B CG2 2463 N N . CYS B 119 ? 0.2130 0.2667 0.3504 0.0469 0.0600 0.0962 117 CYS B N 2464 C CA . CYS B 119 ? 0.2203 0.2693 0.3679 0.0423 0.0637 0.1042 117 CYS B CA 2465 C C . CYS B 119 ? 0.2471 0.2903 0.3738 0.0479 0.0656 0.1004 117 CYS B C 2466 O O . CYS B 119 ? 0.2270 0.2505 0.3379 0.0474 0.0625 0.0885 117 CYS B O 2467 C CB . CYS B 119 ? 0.1476 0.1747 0.3067 0.0331 0.0598 0.0980 117 CYS B CB 2468 S SG . CYS B 119 ? 0.2250 0.2465 0.4048 0.0282 0.0629 0.1078 117 CYS B SG 2469 N N . SER B 120 ? 0.2535 0.3157 0.3806 0.0526 0.0705 0.1114 118 SER B N 2470 C CA . SER B 120 ? 0.2111 0.2702 0.3194 0.0582 0.0714 0.1084 118 SER B CA 2471 C C . SER B 120 ? 0.2117 0.2624 0.3311 0.0531 0.0732 0.1160 118 SER B C 2472 O O . SER B 120 ? 0.1897 0.2540 0.3276 0.0503 0.0761 0.1317 118 SER B O 2473 C CB . SER B 120 ? 0.2428 0.3290 0.3422 0.0675 0.0747 0.1139 118 SER B CB 2474 O OG . SER B 120 ? 0.2731 0.3550 0.3530 0.0734 0.0735 0.1084 118 SER B OG 2475 N N . VAL B 121 ? 0.1884 0.2176 0.2979 0.0517 0.0710 0.1057 119 VAL B N 2476 C CA . VAL B 121 ? 0.1589 0.1784 0.2804 0.0476 0.0722 0.1100 119 VAL B CA 2477 C C . VAL B 121 ? 0.1904 0.2106 0.2952 0.0524 0.0719 0.1080 119 VAL B C 2478 O O . VAL B 121 ? 0.1888 0.1963 0.2757 0.0546 0.0697 0.0969 119 VAL B O 2479 C CB . VAL B 121 ? 0.1838 0.1810 0.3104 0.0414 0.0702 0.0976 119 VAL B CB 2480 C CG1 . VAL B 121 ? 0.1538 0.1472 0.2957 0.0367 0.0698 0.0962 119 VAL B CG1 2481 C CG2 . VAL B 121 ? 0.1995 0.1959 0.3387 0.0366 0.0681 0.0956 119 VAL B CG2 2482 N N . ASN B 122 ? 0.1765 0.2126 0.2881 0.0533 0.0727 0.1179 120 ASN B N 2483 C CA . ASN B 122 ? 0.1720 0.2129 0.2669 0.0588 0.0718 0.1176 120 ASN B CA 2484 C C . ASN B 122 ? 0.1460 0.1868 0.2520 0.0551 0.0702 0.1204 120 ASN B C 2485 O O . ASN B 122 ? 0.2206 0.2677 0.3486 0.0507 0.0696 0.1282 120 ASN B O 2486 C CB . ASN B 122 ? 0.1940 0.2597 0.2790 0.0667 0.0735 0.1269 120 ASN B CB 2487 C CG . ASN B 122 ? 0.2164 0.2863 0.2900 0.0715 0.0740 0.1200 120 ASN B CG 2488 O OD1 . ASN B 122 ? 0.2407 0.3188 0.3271 0.0688 0.0763 0.1247 120 ASN B OD1 2489 N ND2 . ASN B 122 ? 0.2440 0.3083 0.2963 0.0781 0.0699 0.1064 120 ASN B ND2 2490 N N . GLY B 123 ? 0.2047 0.2381 0.2965 0.0572 0.0682 0.1143 121 GLY B N 2491 C CA . GLY B 123 ? 0.1481 0.1849 0.2473 0.0555 0.0663 0.1186 121 GLY B CA 2492 C C . GLY B 123 ? 0.1972 0.2210 0.3143 0.0489 0.0657 0.1139 121 GLY B C 2493 O O . GLY B 123 ? 0.1884 0.2170 0.3186 0.0472 0.0639 0.1199 121 GLY B O 2494 N N . PHE B 124 ? 0.1906 0.1993 0.3086 0.0458 0.0670 0.1034 122 PHE B N 2495 C CA . PHE B 124 ? 0.2128 0.2117 0.3490 0.0408 0.0673 0.0981 122 PHE B CA 2496 C C . PHE B 124 ? 0.2366 0.2257 0.3655 0.0404 0.0674 0.0893 122 PHE B C 2497 O O . PHE B 124 ? 0.2689 0.2543 0.3777 0.0428 0.0666 0.0850 122 PHE B O 2498 C CB . PHE B 124 ? 0.1714 0.1618 0.3169 0.0373 0.0688 0.0920 122 PHE B CB 2499 C CG . PHE B 124 ? 0.1539 0.1346 0.2793 0.0382 0.0700 0.0829 122 PHE B CG 2500 C CD1 . PHE B 124 ? 0.1424 0.1283 0.2563 0.0412 0.0697 0.0867 122 PHE B CD1 2501 C CD2 . PHE B 124 ? 0.1442 0.1116 0.2635 0.0364 0.0714 0.0713 122 PHE B CD2 2502 C CE1 . PHE B 124 ? 0.1708 0.1471 0.2679 0.0422 0.0693 0.0787 122 PHE B CE1 2503 C CE2 . PHE B 124 ? 0.1857 0.1444 0.2871 0.0367 0.0716 0.0643 122 PHE B CE2 2504 C CZ . PHE B 124 ? 0.1846 0.1468 0.2750 0.0395 0.0697 0.0680 122 PHE B CZ 2505 N N . TYR B 125 ? 0.2029 0.1886 0.3508 0.0376 0.0679 0.0872 123 TYR B N 2506 C CA . TYR B 125 ? 0.1732 0.1514 0.3199 0.0370 0.0693 0.0792 123 TYR B CA 2507 C C . TYR B 125 ? 0.2059 0.1789 0.3764 0.0340 0.0712 0.0733 123 TYR B C 2508 O O . TYR B 125 ? 0.1886 0.1660 0.3799 0.0328 0.0688 0.0792 123 TYR B O 2509 C CB . TYR B 125 ? 0.1658 0.1505 0.3100 0.0390 0.0662 0.0853 123 TYR B CB 2510 C CG . TYR B 125 ? 0.1757 0.1544 0.3171 0.0387 0.0676 0.0785 123 TYR B CG 2511 C CD1 . TYR B 125 ? 0.1449 0.1218 0.3069 0.0371 0.0697 0.0753 123 TYR B CD1 2512 C CD2 . TYR B 125 ? 0.2204 0.1953 0.3407 0.0402 0.0665 0.0754 123 TYR B CD2 2513 C CE1 . TYR B 125 ? 0.2092 0.1830 0.3714 0.0371 0.0722 0.0700 123 TYR B CE1 2514 C CE2 . TYR B 125 ? 0.2097 0.1804 0.3305 0.0395 0.0679 0.0712 123 TYR B CE2 2515 C CZ . TYR B 125 ? 0.2255 0.1966 0.3676 0.0381 0.0717 0.0689 123 TYR B CZ 2516 O OH . TYR B 125 ? 0.2752 0.2444 0.4208 0.0378 0.0747 0.0657 123 TYR B OH 2517 N N . PRO B 126 ? 0.2349 0.1990 0.4034 0.0332 0.0753 0.0614 124 PRO B N 2518 C CA . PRO B 126 ? 0.2396 0.1983 0.3863 0.0340 0.0782 0.0556 124 PRO B CA 2519 C C . PRO B 126 ? 0.2231 0.1762 0.3534 0.0336 0.0788 0.0522 124 PRO B C 2520 O O . PRO B 126 ? 0.2184 0.1736 0.3527 0.0332 0.0767 0.0557 124 PRO B O 2521 C CB . PRO B 126 ? 0.2247 0.1791 0.3823 0.0330 0.0837 0.0446 124 PRO B CB 2522 C CG . PRO B 126 ? 0.1574 0.1107 0.3373 0.0317 0.0831 0.0395 124 PRO B CG 2523 C CD . PRO B 126 ? 0.1547 0.1146 0.3455 0.0316 0.0772 0.0527 124 PRO B CD 2524 N N . GLY B 127 ? 0.1965 0.1427 0.3101 0.0336 0.0815 0.0465 125 GLY B N 2525 C CA . GLY B 127 ? 0.2504 0.1904 0.3455 0.0332 0.0805 0.0447 125 GLY B CA 2526 C C . GLY B 127 ? 0.2723 0.2089 0.3713 0.0298 0.0825 0.0350 125 GLY B C 2527 O O . GLY B 127 ? 0.3527 0.2879 0.4414 0.0288 0.0793 0.0351 125 GLY B O 2528 N N . SER B 128 ? 0.2404 0.1763 0.3549 0.0286 0.0870 0.0254 126 SER B N 2529 C CA . SER B 128 ? 0.3172 0.2500 0.4352 0.0257 0.0881 0.0132 126 SER B CA 2530 C C . SER B 128 ? 0.3119 0.2414 0.4453 0.0266 0.0841 0.0189 126 SER B C 2531 O O . SER B 128 ? 0.3504 0.2844 0.5041 0.0271 0.0814 0.0256 126 SER B O 2532 C CB . SER B 128 ? 0.3962 0.3304 0.5320 0.0261 0.0935 0.0000 126 SER B CB 2533 O OG . SER B 128 ? 0.4891 0.4206 0.6278 0.0239 0.0935 -0.0141 126 SER B OG 2534 N N . ILE B 129 ? 0.2580 0.1861 0.3783 0.0239 0.0808 0.0170 127 ILE B N 2535 C CA . ILE B 129 ? 0.2613 0.1885 0.3960 0.0238 0.0769 0.0233 127 ILE B CA 2536 C C . ILE B 129 ? 0.2362 0.1607 0.3618 0.0197 0.0736 0.0139 127 ILE B C 2537 O O . ILE B 129 ? 0.2155 0.1402 0.3167 0.0173 0.0732 0.0075 127 ILE B O 2538 C CB . ILE B 129 ? 0.2250 0.1591 0.3549 0.0271 0.0749 0.0402 127 ILE B CB 2539 C CG1 . ILE B 129 ? 0.2017 0.1436 0.3527 0.0259 0.0713 0.0495 127 ILE B CG1 2540 C CG2 . ILE B 129 ? 0.1598 0.0958 0.2627 0.0269 0.0721 0.0396 127 ILE B CG2 2541 C CD1 . ILE B 129 ? 0.1847 0.1410 0.3328 0.0289 0.0703 0.0647 127 ILE B CD1 2542 N N . GLU B 130 ? 0.2519 0.1740 0.3987 0.0182 0.0703 0.0142 128 GLU B N 2543 C CA . GLU B 130 ? 0.2746 0.1946 0.4159 0.0141 0.0656 0.0065 128 GLU B CA 2544 C C . GLU B 130 ? 0.2280 0.1523 0.3836 0.0139 0.0613 0.0200 128 GLU B C 2545 O O . GLU B 130 ? 0.2450 0.1694 0.4286 0.0139 0.0604 0.0282 128 GLU B O 2546 C CB . GLU B 130 ? 0.3213 0.2346 0.4767 0.0116 0.0645 -0.0111 128 GLU B CB 2547 C CG . GLU B 130 ? 0.4105 0.3217 0.5610 0.0070 0.0583 -0.0203 128 GLU B CG 2548 C CD . GLU B 130 ? 0.4761 0.3897 0.5939 0.0043 0.0589 -0.0320 128 GLU B CD 2549 O OE1 . GLU B 130 ? 0.4806 0.3951 0.5851 0.0009 0.0532 -0.0324 128 GLU B OE1 2550 O OE2 . GLU B 130 ? 0.4847 0.4006 0.5912 0.0051 0.0648 -0.0395 128 GLU B OE2 2551 N N . VAL B 131 ? 0.1906 0.1194 0.3285 0.0134 0.0584 0.0231 129 VAL B N 2552 C CA . VAL B 131 ? 0.2240 0.1610 0.3741 0.0135 0.0553 0.0355 129 VAL B CA 2553 C C . VAL B 131 ? 0.2398 0.1749 0.3879 0.0090 0.0489 0.0279 129 VAL B C 2554 O O . VAL B 131 ? 0.2574 0.1902 0.3814 0.0081 0.0466 0.0195 129 VAL B O 2555 C CB . VAL B 131 ? 0.2423 0.1899 0.3761 0.0188 0.0571 0.0468 129 VAL B CB 2556 C CG1 . VAL B 131 ? 0.1614 0.1225 0.3097 0.0196 0.0555 0.0597 129 VAL B CG1 2557 C CG2 . VAL B 131 ? 0.1601 0.1097 0.2923 0.0230 0.0621 0.0532 129 VAL B CG2 2558 N N . ARG B 132 ? 0.2313 0.1678 0.4060 0.0057 0.0449 0.0318 130 ARG B N 2559 C CA . ARG B 132 ? 0.2927 0.2276 0.4695 0.0010 0.0375 0.0246 130 ARG B CA 2560 C C . ARG B 132 ? 0.2699 0.2168 0.4674 -0.0001 0.0345 0.0394 130 ARG B C 2561 O O . ARG B 132 ? 0.2703 0.2248 0.4901 0.0005 0.0372 0.0541 130 ARG B O 2562 C CB . ARG B 132 ? 0.3848 0.3075 0.5755 -0.0036 0.0334 0.0087 130 ARG B CB 2563 C CG . ARG B 132 ? 0.4970 0.4125 0.6650 -0.0028 0.0368 -0.0082 130 ARG B CG 2564 C CD . ARG B 132 ? 0.5862 0.4922 0.7688 -0.0057 0.0332 -0.0267 130 ARG B CD 2565 N NE . ARG B 132 ? 0.6639 0.5681 0.8230 -0.0048 0.0378 -0.0431 130 ARG B NE 2566 C CZ . ARG B 132 ? 0.6968 0.6027 0.8299 -0.0079 0.0352 -0.0559 130 ARG B CZ 2567 N NH1 . ARG B 132 ? 0.7283 0.6355 0.8560 -0.0119 0.0270 -0.0549 130 ARG B NH1 2568 N NH2 . ARG B 132 ? 0.7033 0.6114 0.8161 -0.0075 0.0407 -0.0688 130 ARG B NH2 2569 N N . TRP B 133 ? 0.2116 0.1621 0.4022 -0.0021 0.0286 0.0365 131 TRP B N 2570 C CA . TRP B 133 ? 0.2079 0.1725 0.4188 -0.0033 0.0257 0.0495 131 TRP B CA 2571 C C . TRP B 133 ? 0.2623 0.2214 0.4979 -0.0110 0.0167 0.0443 131 TRP B C 2572 O O . TRP B 133 ? 0.3293 0.2759 0.5554 -0.0144 0.0108 0.0273 131 TRP B O 2573 C CB . TRP B 133 ? 0.1814 0.1560 0.3721 0.0008 0.0243 0.0509 131 TRP B CB 2574 C CG . TRP B 133 ? 0.2316 0.2196 0.4120 0.0089 0.0315 0.0616 131 TRP B CG 2575 C CD1 . TRP B 133 ? 0.2173 0.2017 0.3696 0.0147 0.0340 0.0570 131 TRP B CD1 2576 C CD2 . TRP B 133 ? 0.2119 0.2206 0.4100 0.0120 0.0366 0.0784 131 TRP B CD2 2577 N NE1 . TRP B 133 ? 0.1610 0.1610 0.3121 0.0220 0.0396 0.0676 131 TRP B NE1 2578 C CE2 . TRP B 133 ? 0.2122 0.2290 0.3897 0.0207 0.0420 0.0808 131 TRP B CE2 2579 C CE3 . TRP B 133 ? 0.1629 0.1855 0.3928 0.0078 0.0367 0.0922 131 TRP B CE3 2580 C CZ2 . TRP B 133 ? 0.1521 0.1920 0.3372 0.0261 0.0483 0.0948 131 TRP B CZ2 2581 C CZ3 . TRP B 133 ? 0.1565 0.2034 0.3945 0.0122 0.0436 0.1087 131 TRP B CZ3 2582 C CH2 . TRP B 133 ? 0.1515 0.2076 0.3658 0.0217 0.0496 0.1090 131 TRP B CH2 2583 N N . PHE B 134 ? 0.2386 0.2087 0.5064 -0.0141 0.0153 0.0594 132 PHE B N 2584 C CA . PHE B 134 ? 0.2439 0.2098 0.5401 -0.0220 0.0052 0.0566 132 PHE B CA 2585 C C . PHE B 134 ? 0.3024 0.2891 0.6168 -0.0238 0.0032 0.0726 132 PHE B C 2586 O O . PHE B 134 ? 0.2760 0.2817 0.5965 -0.0204 0.0107 0.0907 132 PHE B O 2587 C CB . PHE B 134 ? 0.2566 0.2125 0.5853 -0.0263 0.0032 0.0594 132 PHE B CB 2588 C CG . PHE B 134 ? 0.2972 0.2334 0.6144 -0.0245 0.0041 0.0407 132 PHE B CG 2589 C CD1 . PHE B 134 ? 0.2555 0.1911 0.5556 -0.0183 0.0137 0.0426 132 PHE B CD1 2590 C CD2 . PHE B 134 ? 0.3099 0.2301 0.6351 -0.0287 -0.0050 0.0204 132 PHE B CD2 2591 C CE1 . PHE B 134 ? 0.2667 0.1872 0.5587 -0.0165 0.0151 0.0255 132 PHE B CE1 2592 C CE2 . PHE B 134 ? 0.2888 0.1946 0.6043 -0.0261 -0.0033 0.0017 132 PHE B CE2 2593 C CZ . PHE B 134 ? 0.2327 0.1392 0.5324 -0.0200 0.0072 0.0048 132 PHE B CZ 2594 N N . ARG B 135 ? 0.3708 0.3557 0.6937 -0.0291 -0.0071 0.0655 133 ARG B N 2595 C CA . ARG B 135 ? 0.3941 0.3994 0.7409 -0.0320 -0.0103 0.0802 133 ARG B CA 2596 C C . ARG B 135 ? 0.4294 0.4271 0.8148 -0.0423 -0.0214 0.0805 133 ARG B C 2597 O O . ARG B 135 ? 0.4595 0.4402 0.8426 -0.0465 -0.0319 0.0622 133 ARG B O 2598 C CB . ARG B 135 ? 0.4182 0.4298 0.7443 -0.0292 -0.0146 0.0731 133 ARG B CB 2599 C CG . ARG B 135 ? 0.4472 0.4829 0.8000 -0.0312 -0.0174 0.0878 133 ARG B CG 2600 C CD . ARG B 135 ? 0.5162 0.5551 0.8551 -0.0296 -0.0253 0.0791 133 ARG B CD 2601 N NE . ARG B 135 ? 0.6465 0.6637 0.9762 -0.0357 -0.0378 0.0605 133 ARG B NE 2602 C CZ . ARG B 135 ? 0.7471 0.7486 1.0403 -0.0329 -0.0395 0.0446 133 ARG B CZ 2603 N NH1 . ARG B 135 ? 0.7251 0.7278 0.9902 -0.0245 -0.0303 0.0455 133 ARG B NH1 2604 N NH2 . ARG B 135 ? 0.8118 0.7977 1.0968 -0.0389 -0.0507 0.0282 133 ARG B NH2 2605 N N . ASN B 136 ? 0.4365 0.4479 0.8553 -0.0457 -0.0196 0.1012 134 ASN B N 2606 C CA . ASN B 136 ? 0.4313 0.4363 0.8771 -0.0500 -0.0307 0.1017 134 ASN B CA 2607 C C . ASN B 136 ? 0.4432 0.4215 0.8878 -0.0507 -0.0376 0.0808 134 ASN B C 2608 O O . ASN B 136 ? 0.4757 0.4432 0.9344 -0.0551 -0.0501 0.0691 134 ASN B O 2609 C CB . ASN B 136 ? 0.4154 0.4277 0.8775 -0.0558 -0.0412 0.1017 134 ASN B CB 2610 C CG . ASN B 136 ? 0.3592 0.4019 0.8282 -0.0541 -0.0346 0.1228 134 ASN B CG 2611 O OD1 . ASN B 136 ? 0.3094 0.3683 0.7814 -0.0501 -0.0257 0.1415 134 ASN B OD1 2612 N ND2 . ASN B 136 ? 0.3629 0.4150 0.8329 -0.0565 -0.0396 0.1190 134 ASN B ND2 2613 N N . GLY B 137 ? 0.4315 0.4011 0.8589 -0.0457 -0.0295 0.0757 135 GLY B N 2614 C CA . GLY B 137 ? 0.4351 0.3841 0.8617 -0.0445 -0.0337 0.0568 135 GLY B CA 2615 C C . GLY B 137 ? 0.4674 0.3980 0.8686 -0.0450 -0.0363 0.0297 135 GLY B C 2616 O O . GLY B 137 ? 0.5098 0.4258 0.9071 -0.0429 -0.0384 0.0116 135 GLY B O 2617 N N . GLN B 138 ? 0.4516 0.3846 0.8357 -0.0474 -0.0365 0.0268 136 GLN B N 2618 C CA . GLN B 138 ? 0.4893 0.4108 0.8396 -0.0462 -0.0392 0.0025 136 GLN B CA 2619 C C . GLN B 138 ? 0.4452 0.3732 0.7550 -0.0384 -0.0268 0.0047 136 GLN B C 2620 O O . GLN B 138 ? 0.4494 0.3932 0.7530 -0.0352 -0.0212 0.0212 136 GLN B O 2621 C CB . GLN B 138 ? 0.5675 0.4930 0.9160 -0.0512 -0.0509 -0.0034 136 GLN B CB 2622 C CG . GLN B 138 ? 0.6610 0.5806 0.9678 -0.0495 -0.0534 -0.0244 136 GLN B CG 2623 C CD . GLN B 138 ? 0.7446 0.6616 1.0563 -0.0562 -0.0691 -0.0368 136 GLN B CD 2624 O OE1 . GLN B 138 ? 0.7921 0.7051 1.1402 -0.0623 -0.0794 -0.0370 136 GLN B OE1 2625 N NE2 . GLN B 138 ? 0.7485 0.6678 1.0244 -0.0556 -0.0722 -0.0464 136 GLN B NE2 2626 N N . GLU B 139 ? 0.3932 0.3101 0.6768 -0.0351 -0.0229 -0.0124 137 GLU B N 2627 C CA . GLU B 139 ? 0.4051 0.3268 0.6527 -0.0287 -0.0124 -0.0100 137 GLU B CA 2628 C C . GLU B 139 ? 0.3995 0.3290 0.6206 -0.0285 -0.0159 -0.0098 137 GLU B C 2629 O O . GLU B 139 ? 0.4440 0.3697 0.6570 -0.0328 -0.0255 -0.0225 137 GLU B O 2630 C CB . GLU B 139 ? 0.3759 0.2868 0.6031 -0.0260 -0.0073 -0.0273 137 GLU B CB 2631 C CG . GLU B 139 ? 0.3257 0.2417 0.5193 -0.0204 0.0027 -0.0224 137 GLU B CG 2632 C CD . GLU B 139 ? 0.3269 0.2358 0.5033 -0.0181 0.0090 -0.0368 137 GLU B CD 2633 O OE1 . GLU B 139 ? 0.3763 0.2768 0.5668 -0.0196 0.0065 -0.0521 137 GLU B OE1 2634 O OE2 . GLU B 139 ? 0.3397 0.2521 0.4900 -0.0146 0.0161 -0.0332 137 GLU B OE2 2635 N N . GLU B 140 ? 0.3505 0.2908 0.5590 -0.0230 -0.0090 0.0043 138 GLU B N 2636 C CA . GLU B 140 ? 0.3627 0.3093 0.5473 -0.0212 -0.0124 0.0053 138 GLU B CA 2637 C C . GLU B 140 ? 0.3185 0.2600 0.4678 -0.0173 -0.0066 -0.0002 138 GLU B C 2638 O O . GLU B 140 ? 0.2163 0.1603 0.3606 -0.0118 0.0025 0.0076 138 GLU B O 2639 C CB . GLU B 140 ? 0.4069 0.3708 0.6052 -0.0171 -0.0101 0.0234 138 GLU B CB 2640 C CG . GLU B 140 ? 0.4531 0.4235 0.6331 -0.0143 -0.0153 0.0241 138 GLU B CG 2641 C CD . GLU B 140 ? 0.5016 0.4675 0.6810 -0.0209 -0.0284 0.0144 138 GLU B CD 2642 O OE1 . GLU B 140 ? 0.4953 0.4670 0.7032 -0.0255 -0.0345 0.0176 138 GLU B OE1 2643 O OE2 . GLU B 140 ? 0.5132 0.4710 0.6641 -0.0222 -0.0332 0.0045 138 GLU B OE2 2644 N N . LYS B 141 ? 0.3160 0.2514 0.4411 -0.0208 -0.0127 -0.0128 139 LYS B N 2645 C CA . LYS B 141 ? 0.3549 0.2864 0.4469 -0.0191 -0.0085 -0.0173 139 LYS B CA 2646 C C . LYS B 141 ? 0.3616 0.2971 0.4330 -0.0175 -0.0139 -0.0106 139 LYS B C 2647 O O . LYS B 141 ? 0.3560 0.2889 0.4029 -0.0161 -0.0113 -0.0101 139 LYS B O 2648 C CB . LYS B 141 ? 0.4208 0.3456 0.4980 -0.0245 -0.0106 -0.0353 139 LYS B CB 2649 C CG . LYS B 141 ? 0.4457 0.3650 0.5399 -0.0239 -0.0040 -0.0442 139 LYS B CG 2650 C CD . LYS B 141 ? 0.5008 0.4167 0.5781 -0.0275 -0.0048 -0.0647 139 LYS B CD 2651 C CE . LYS B 141 ? 0.4886 0.3989 0.5857 -0.0252 0.0016 -0.0748 139 LYS B CE 2652 N NZ . LYS B 141 ? 0.4780 0.3875 0.5627 -0.0276 0.0004 -0.0983 139 LYS B NZ 2653 N N . THR B 142 ? 0.3607 0.3026 0.4446 -0.0177 -0.0221 -0.0051 140 THR B N 2654 C CA . THR B 142 ? 0.3627 0.3081 0.4326 -0.0152 -0.0289 0.0012 140 THR B CA 2655 C C . THR B 142 ? 0.3144 0.2684 0.3951 -0.0061 -0.0232 0.0134 140 THR B C 2656 O O . THR B 142 ? 0.3449 0.3069 0.4493 -0.0034 -0.0168 0.0193 140 THR B O 2657 C CB . THR B 142 ? 0.3414 0.2905 0.4191 -0.0197 -0.0423 -0.0004 140 THR B CB 2658 O OG1 . THR B 142 ? 0.3137 0.2564 0.3805 -0.0279 -0.0480 -0.0136 140 THR B OG1 2659 C CG2 . THR B 142 ? 0.3620 0.3134 0.4263 -0.0169 -0.0511 0.0058 140 THR B CG2 2660 N N . GLY B 143 ? 0.2952 0.2484 0.3591 -0.0014 -0.0260 0.0172 141 GLY B N 2661 C CA . GLY B 143 ? 0.2846 0.2469 0.3569 0.0085 -0.0220 0.0256 141 GLY B CA 2662 C C . GLY B 143 ? 0.3072 0.2702 0.3797 0.0132 -0.0096 0.0284 141 GLY B C 2663 O O . GLY B 143 ? 0.3263 0.3016 0.4121 0.0206 -0.0041 0.0351 141 GLY B O 2664 N N . VAL B 144 ? 0.3033 0.2554 0.3611 0.0091 -0.0051 0.0234 142 VAL B N 2665 C CA . VAL B 144 ? 0.2896 0.2420 0.3480 0.0132 0.0055 0.0263 142 VAL B CA 2666 C C . VAL B 144 ? 0.2991 0.2445 0.3350 0.0164 0.0051 0.0263 142 VAL B C 2667 O O . VAL B 144 ? 0.2982 0.2343 0.3154 0.0110 0.0011 0.0220 142 VAL B O 2668 C CB . VAL B 144 ? 0.2674 0.2140 0.3315 0.0075 0.0116 0.0209 142 VAL B CB 2669 C CG1 . VAL B 144 ? 0.2730 0.2195 0.3372 0.0117 0.0214 0.0246 142 VAL B CG1 2670 C CG2 . VAL B 144 ? 0.2488 0.2009 0.3398 0.0042 0.0107 0.0219 142 VAL B CG2 2671 N N . VAL B 145 ? 0.2833 0.2347 0.3220 0.0250 0.0090 0.0316 143 VAL B N 2672 C CA . VAL B 145 ? 0.2937 0.2383 0.3154 0.0288 0.0075 0.0317 143 VAL B CA 2673 C C . VAL B 145 ? 0.2617 0.2108 0.2875 0.0339 0.0172 0.0348 143 VAL B C 2674 O O . VAL B 145 ? 0.2910 0.2523 0.3331 0.0374 0.0232 0.0393 143 VAL B O 2675 C CB . VAL B 145 ? 0.3978 0.3448 0.4178 0.0363 -0.0016 0.0329 143 VAL B CB 2676 C CG1 . VAL B 145 ? 0.3539 0.3186 0.3919 0.0456 0.0026 0.0360 143 VAL B CG1 2677 C CG2 . VAL B 145 ? 0.4163 0.3531 0.4207 0.0392 -0.0058 0.0326 143 VAL B CG2 2678 N N . SER B 146 ? 0.2269 0.1674 0.2388 0.0335 0.0182 0.0338 144 SER B N 2679 C CA . SER B 146 ? 0.2067 0.1510 0.2219 0.0378 0.0262 0.0367 144 SER B CA 2680 C C . SER B 146 ? 0.2476 0.1863 0.2494 0.0426 0.0222 0.0365 144 SER B C 2681 O O . SER B 146 ? 0.2457 0.1746 0.2356 0.0403 0.0137 0.0346 144 SER B O 2682 C CB . SER B 146 ? 0.2168 0.1566 0.2350 0.0310 0.0333 0.0352 144 SER B CB 2683 O OG . SER B 146 ? 0.1988 0.1416 0.2206 0.0348 0.0397 0.0389 144 SER B OG 2684 N N . THR B 147 ? 0.2338 0.1791 0.2388 0.0488 0.0272 0.0391 145 THR B N 2685 C CA . THR B 147 ? 0.2423 0.1817 0.2365 0.0527 0.0235 0.0380 145 THR B CA 2686 C C . THR B 147 ? 0.2805 0.2087 0.2673 0.0443 0.0252 0.0378 145 THR B C 2687 O O . THR B 147 ? 0.3211 0.2413 0.2987 0.0440 0.0200 0.0375 145 THR B O 2688 C CB . THR B 147 ? 0.1709 0.1225 0.1699 0.0609 0.0288 0.0407 145 THR B CB 2689 O OG1 . THR B 147 ? 0.1977 0.1545 0.2069 0.0569 0.0382 0.0458 145 THR B OG1 2690 C CG2 . THR B 147 ? 0.1811 0.1486 0.1862 0.0703 0.0280 0.0405 145 THR B CG2 2691 N N . GLY B 148 ? 0.2482 0.1770 0.2409 0.0375 0.0322 0.0376 146 GLY B N 2692 C CA . GLY B 148 ? 0.2250 0.1488 0.2147 0.0312 0.0368 0.0365 146 GLY B CA 2693 C C . GLY B 148 ? 0.2504 0.1793 0.2492 0.0353 0.0433 0.0398 146 GLY B C 2694 O O . GLY B 148 ? 0.2351 0.1724 0.2414 0.0420 0.0446 0.0437 146 GLY B O 2695 N N . LEU B 149 ? 0.2451 0.1708 0.2435 0.0311 0.0473 0.0390 147 LEU B N 2696 C CA . LEU B 149 ? 0.2493 0.1796 0.2579 0.0345 0.0524 0.0428 147 LEU B CA 2697 C C . LEU B 149 ? 0.2751 0.2048 0.2756 0.0396 0.0469 0.0456 147 LEU B C 2698 O O . LEU B 149 ? 0.2699 0.1925 0.2601 0.0366 0.0417 0.0444 147 LEU B O 2699 C CB . LEU B 149 ? 0.2493 0.1780 0.2638 0.0289 0.0587 0.0397 147 LEU B CB 2700 C CG . LEU B 149 ? 0.2737 0.2067 0.3023 0.0321 0.0633 0.0440 147 LEU B CG 2701 C CD1 . LEU B 149 ? 0.2424 0.1813 0.2882 0.0356 0.0663 0.0486 147 LEU B CD1 2702 C CD2 . LEU B 149 ? 0.3010 0.2334 0.3359 0.0273 0.0689 0.0393 147 LEU B CD2 2703 N N . ILE B 150 ? 0.2556 0.1938 0.2612 0.0470 0.0474 0.0498 148 ILE B N 2704 C CA . ILE B 150 ? 0.2435 0.1829 0.2413 0.0532 0.0415 0.0505 148 ILE B CA 2705 C C . ILE B 150 ? 0.2400 0.1844 0.2452 0.0545 0.0450 0.0553 148 ILE B C 2706 O O . ILE B 150 ? 0.2202 0.1749 0.2367 0.0557 0.0504 0.0605 148 ILE B O 2707 C CB . ILE B 150 ? 0.2724 0.2220 0.2676 0.0622 0.0387 0.0503 148 ILE B CB 2708 C CG1 . ILE B 150 ? 0.2329 0.1779 0.2231 0.0619 0.0339 0.0455 148 ILE B CG1 2709 C CG2 . ILE B 150 ? 0.3298 0.2816 0.3165 0.0698 0.0320 0.0480 148 ILE B CG2 2710 C CD1 . ILE B 150 ? 0.2861 0.2444 0.2773 0.0709 0.0327 0.0446 148 ILE B CD1 2711 N N . GLN B 151 ? 0.3023 0.2404 0.3025 0.0530 0.0405 0.0541 149 GLN B N 2712 C CA . GLN B 151 ? 0.3111 0.2551 0.3175 0.0541 0.0410 0.0577 149 GLN B CA 2713 C C . GLN B 151 ? 0.2855 0.2372 0.2843 0.0634 0.0353 0.0583 149 GLN B C 2714 O O . GLN B 151 ? 0.3359 0.2829 0.3234 0.0680 0.0273 0.0528 149 GLN B O 2715 C CB . GLN B 151 ? 0.3501 0.2853 0.3561 0.0488 0.0383 0.0570 149 GLN B CB 2716 C CG . GLN B 151 ? 0.4105 0.3511 0.4311 0.0454 0.0440 0.0602 149 GLN B CG 2717 C CD . GLN B 151 ? 0.4679 0.4017 0.4904 0.0389 0.0445 0.0600 149 GLN B CD 2718 O OE1 . GLN B 151 ? 0.4917 0.4185 0.5035 0.0355 0.0378 0.0581 149 GLN B OE1 2719 N NE2 . GLN B 151 ? 0.4518 0.3903 0.4895 0.0361 0.0516 0.0614 149 GLN B NE2 2720 N N . ASN B 152 ? 0.2289 0.1937 0.2344 0.0662 0.0386 0.0644 150 ASN B N 2721 C CA . ASN B 152 ? 0.2307 0.2067 0.2272 0.0761 0.0341 0.0657 150 ASN B CA 2722 C C . ASN B 152 ? 0.2804 0.2538 0.2733 0.0778 0.0269 0.0650 150 ASN B C 2723 O O . ASN B 152 ? 0.2845 0.2662 0.2670 0.0855 0.0205 0.0620 150 ASN B O 2724 C CB . ASN B 152 ? 0.2339 0.2286 0.2378 0.0785 0.0409 0.0754 150 ASN B CB 2725 C CG . ASN B 152 ? 0.2696 0.2697 0.2767 0.0793 0.0462 0.0768 150 ASN B CG 2726 O OD1 . ASN B 152 ? 0.2851 0.2822 0.2828 0.0826 0.0429 0.0685 150 ASN B OD1 2727 N ND2 . ASN B 152 ? 0.2076 0.2162 0.2301 0.0747 0.0531 0.0859 150 ASN B ND2 2728 N N . GLY B 153 ? 0.2284 0.1927 0.2304 0.0695 0.0274 0.0658 151 GLY B N 2729 C CA . GLY B 153 ? 0.2166 0.1772 0.2185 0.0697 0.0200 0.0660 151 GLY B CA 2730 C C . GLY B 153 ? 0.2674 0.2406 0.2782 0.0703 0.0217 0.0738 151 GLY B C 2731 O O . GLY B 153 ? 0.2984 0.2704 0.3112 0.0705 0.0154 0.0751 151 GLY B O 2732 N N . ASP B 154 ? 0.2747 0.2598 0.2923 0.0701 0.0291 0.0800 152 ASP B N 2733 C CA . ASP B 154 ? 0.2395 0.2377 0.2658 0.0704 0.0297 0.0891 152 ASP B CA 2734 C C . ASP B 154 ? 0.2163 0.2158 0.2639 0.0628 0.0375 0.0938 152 ASP B C 2735 O O . ASP B 154 ? 0.2616 0.2731 0.3183 0.0626 0.0396 0.1028 152 ASP B O 2736 C CB . ASP B 154 ? 0.2559 0.2719 0.2708 0.0785 0.0292 0.0945 152 ASP B CB 2737 C CG . ASP B 154 ? 0.2138 0.2363 0.2315 0.0783 0.0372 0.0973 152 ASP B CG 2738 O OD1 . ASP B 154 ? 0.1668 0.1778 0.1924 0.0727 0.0416 0.0931 152 ASP B OD1 2739 O OD2 . ASP B 154 ? 0.2089 0.2504 0.2210 0.0837 0.0388 0.1041 152 ASP B OD2 2740 N N . TRP B 155 ? 0.1909 0.1790 0.2464 0.0571 0.0411 0.0877 153 TRP B N 2741 C CA . TRP B 155 ? 0.2018 0.1902 0.2778 0.0517 0.0478 0.0889 153 TRP B CA 2742 C C . TRP B 155 ? 0.1910 0.1842 0.2720 0.0513 0.0526 0.0914 153 TRP B C 2743 O O . TRP B 155 ? 0.1984 0.1952 0.2985 0.0483 0.0557 0.0953 153 TRP B O 2744 C CB . TRP B 155 ? 0.2198 0.2146 0.3127 0.0505 0.0463 0.0953 153 TRP B CB 2745 C CG . TRP B 155 ? 0.2088 0.1986 0.3044 0.0493 0.0433 0.0925 153 TRP B CG 2746 C CD1 . TRP B 155 ? 0.1907 0.1794 0.2743 0.0520 0.0355 0.0928 153 TRP B CD1 2747 C CD2 . TRP B 155 ? 0.1961 0.1824 0.3098 0.0455 0.0477 0.0893 153 TRP B CD2 2748 N NE1 . TRP B 155 ? 0.1862 0.1711 0.2805 0.0491 0.0347 0.0912 153 TRP B NE1 2749 C CE2 . TRP B 155 ? 0.1732 0.1577 0.2860 0.0455 0.0431 0.0893 153 TRP B CE2 2750 C CE3 . TRP B 155 ? 0.2112 0.1963 0.3430 0.0428 0.0551 0.0862 153 TRP B CE3 2751 C CZ2 . TRP B 155 ? 0.1874 0.1711 0.3180 0.0428 0.0470 0.0876 153 TRP B CZ2 2752 C CZ3 . TRP B 155 ? 0.2018 0.1851 0.3497 0.0411 0.0591 0.0828 153 TRP B CZ3 2753 C CH2 . TRP B 155 ? 0.1955 0.1793 0.3434 0.0412 0.0558 0.0842 153 TRP B CH2 2754 N N . THR B 156 ? 0.1756 0.1685 0.2415 0.0545 0.0525 0.0894 154 THR B N 2755 C CA . THR B 156 ? 0.1480 0.1439 0.2193 0.0536 0.0570 0.0910 154 THR B CA 2756 C C . THR B 156 ? 0.2325 0.2185 0.2904 0.0540 0.0573 0.0826 154 THR B C 2757 O O . THR B 156 ? 0.1511 0.1309 0.1931 0.0568 0.0528 0.0775 154 THR B O 2758 C CB . THR B 156 ? 0.1512 0.1640 0.2211 0.0581 0.0572 0.1015 154 THR B CB 2759 O OG1 . THR B 156 ? 0.3035 0.3198 0.3514 0.0656 0.0539 0.0994 154 THR B OG1 2760 C CG2 . THR B 156 ? 0.1539 0.1779 0.2358 0.0573 0.0556 0.1115 154 THR B CG2 2761 N N . PHE B 157 ? 0.2733 0.2573 0.3389 0.0512 0.0612 0.0814 155 PHE B N 2762 C CA . PHE B 157 ? 0.2380 0.2135 0.2922 0.0515 0.0609 0.0748 155 PHE B CA 2763 C C . PHE B 157 ? 0.2052 0.1896 0.2605 0.0547 0.0624 0.0798 155 PHE B C 2764 O O . PHE B 157 ? 0.2095 0.2067 0.2770 0.0552 0.0647 0.0892 155 PHE B O 2765 C CB . PHE B 157 ? 0.2551 0.2195 0.3170 0.0454 0.0643 0.0681 155 PHE B CB 2766 C CG . PHE B 157 ? 0.2348 0.1916 0.2954 0.0427 0.0646 0.0633 155 PHE B CG 2767 C CD1 . PHE B 157 ? 0.2519 0.2118 0.3289 0.0409 0.0671 0.0647 155 PHE B CD1 2768 C CD2 . PHE B 157 ? 0.2100 0.1571 0.2551 0.0417 0.0623 0.0585 155 PHE B CD2 2769 C CE1 . PHE B 157 ? 0.2787 0.2335 0.3569 0.0391 0.0688 0.0612 155 PHE B CE1 2770 C CE2 . PHE B 157 ? 0.2644 0.2061 0.3100 0.0386 0.0637 0.0565 155 PHE B CE2 2771 C CZ . PHE B 157 ? 0.2423 0.1884 0.3048 0.0377 0.0677 0.0577 155 PHE B CZ 2772 N N . GLN B 158 ? 0.2304 0.2090 0.2744 0.0568 0.0606 0.0746 156 GLN B N 2773 C CA . GLN B 158 ? 0.2310 0.2170 0.2797 0.0592 0.0625 0.0785 156 GLN B CA 2774 C C . GLN B 158 ? 0.2528 0.2273 0.2954 0.0557 0.0601 0.0692 156 GLN B C 2775 O O . GLN B 158 ? 0.2080 0.1701 0.2389 0.0535 0.0566 0.0616 156 GLN B O 2776 C CB . GLN B 158 ? 0.1985 0.2013 0.2375 0.0679 0.0609 0.0819 156 GLN B CB 2777 C CG . GLN B 158 ? 0.2316 0.2287 0.2510 0.0732 0.0539 0.0712 156 GLN B CG 2778 C CD . GLN B 158 ? 0.2330 0.2486 0.2441 0.0831 0.0523 0.0705 156 GLN B CD 2779 O OE1 . GLN B 158 ? 0.2934 0.3200 0.3082 0.0854 0.0542 0.0709 156 GLN B OE1 2780 N NE2 . GLN B 158 ? 0.1768 0.1976 0.1772 0.0892 0.0487 0.0686 156 GLN B NE2 2781 N N . THR B 159 ? 0.2593 0.2393 0.3103 0.0545 0.0613 0.0709 157 THR B N 2782 C CA . THR B 159 ? 0.2429 0.2151 0.2877 0.0518 0.0575 0.0629 157 THR B CA 2783 C C . THR B 159 ? 0.2418 0.2272 0.2957 0.0539 0.0579 0.0670 157 THR B C 2784 O O . THR B 159 ? 0.2746 0.2715 0.3454 0.0530 0.0622 0.0764 157 THR B O 2785 C CB . THR B 159 ? 0.2398 0.1986 0.2893 0.0433 0.0587 0.0569 157 THR B CB 2786 O OG1 . THR B 159 ? 0.3107 0.2635 0.3512 0.0404 0.0539 0.0500 157 THR B OG1 2787 C CG2 . THR B 159 ? 0.2473 0.2093 0.3199 0.0398 0.0631 0.0616 157 THR B CG2 2788 N N . LEU B 160 ? 0.2307 0.2153 0.2753 0.0563 0.0526 0.0611 158 LEU B N 2789 C CA . LEU B 160 ? 0.2283 0.2256 0.2835 0.0575 0.0525 0.0640 158 LEU B CA 2790 C C . LEU B 160 ? 0.2195 0.2045 0.2770 0.0500 0.0486 0.0582 158 LEU B C 2791 O O . LEU B 160 ? 0.1812 0.1525 0.2241 0.0480 0.0431 0.0505 158 LEU B O 2792 C CB . LEU B 160 ? 0.2467 0.2548 0.2928 0.0672 0.0487 0.0608 158 LEU B CB 2793 C CG . LEU B 160 ? 0.2958 0.3171 0.3343 0.0765 0.0506 0.0624 158 LEU B CG 2794 C CD1 . LEU B 160 ? 0.3096 0.3460 0.3446 0.0869 0.0475 0.0573 158 LEU B CD1 2795 C CD2 . LEU B 160 ? 0.2716 0.3091 0.3221 0.0754 0.0588 0.0749 158 LEU B CD2 2796 N N . VAL B 161 ? 0.2209 0.2113 0.2970 0.0453 0.0506 0.0625 159 VAL B N 2797 C CA . VAL B 161 ? 0.1576 0.1380 0.2362 0.0384 0.0458 0.0560 159 VAL B CA 2798 C C . VAL B 161 ? 0.2472 0.2416 0.3390 0.0397 0.0435 0.0601 159 VAL B C 2799 O O . VAL B 161 ? 0.2429 0.2509 0.3554 0.0388 0.0473 0.0694 159 VAL B O 2800 C CB . VAL B 161 ? 0.1628 0.1341 0.2544 0.0306 0.0483 0.0543 159 VAL B CB 2801 C CG1 . VAL B 161 ? 0.1666 0.1291 0.2582 0.0239 0.0425 0.0454 159 VAL B CG1 2802 C CG2 . VAL B 161 ? 0.1595 0.1205 0.2409 0.0301 0.0517 0.0504 159 VAL B CG2 2803 N N . MET B 162 ? 0.2454 0.2371 0.3268 0.0415 0.0364 0.0542 160 MET B N 2804 C CA . MET B 162 ? 0.2439 0.2501 0.3370 0.0444 0.0333 0.0568 160 MET B CA 2805 C C . MET B 162 ? 0.2555 0.2552 0.3563 0.0366 0.0264 0.0531 160 MET B C 2806 O O . MET B 162 ? 0.3017 0.2847 0.3885 0.0312 0.0210 0.0451 160 MET B O 2807 C CB . MET B 162 ? 0.1964 0.2066 0.2765 0.0541 0.0289 0.0529 160 MET B CB 2808 C CG . MET B 162 ? 0.1763 0.1963 0.2503 0.0627 0.0350 0.0555 160 MET B CG 2809 S SD . MET B 162 ? 0.6652 0.6809 0.7208 0.0738 0.0277 0.0465 160 MET B SD 2810 C CE . MET B 162 ? 0.2151 0.2048 0.2518 0.0672 0.0254 0.0429 160 MET B CE 2811 N N . LEU B 163 ? 0.1707 0.1857 0.2936 0.0357 0.0265 0.0593 161 LEU B N 2812 C CA . LEU B 163 ? 0.1695 0.1806 0.3025 0.0285 0.0187 0.0560 161 LEU B CA 2813 C C . LEU B 163 ? 0.2109 0.2371 0.3508 0.0341 0.0137 0.0578 161 LEU B C 2814 O O . LEU B 163 ? 0.1820 0.2307 0.3385 0.0393 0.0189 0.0662 161 LEU B O 2815 C CB . LEU B 163 ? 0.1768 0.1921 0.3360 0.0211 0.0212 0.0621 161 LEU B CB 2816 C CG . LEU B 163 ? 0.1988 0.2123 0.3735 0.0134 0.0123 0.0591 161 LEU B CG 2817 C CD1 . LEU B 163 ? 0.1860 0.1780 0.3408 0.0078 0.0049 0.0451 161 LEU B CD1 2818 C CD2 . LEU B 163 ? 0.1746 0.1937 0.3805 0.0068 0.0141 0.0673 161 LEU B CD2 2819 N N . GLU B 164 ? 0.2666 0.2822 0.3944 0.0332 0.0035 0.0504 162 GLU B N 2820 C CA . GLU B 164 ? 0.3247 0.3532 0.4624 0.0381 -0.0033 0.0512 162 GLU B CA 2821 C C . GLU B 164 ? 0.3123 0.3487 0.4741 0.0305 -0.0071 0.0546 162 GLU B C 2822 O O . GLU B 164 ? 0.3020 0.3240 0.4609 0.0212 -0.0140 0.0495 162 GLU B O 2823 C CB . GLU B 164 ? 0.3723 0.3853 0.4899 0.0390 -0.0149 0.0438 162 GLU B CB 2824 C CG . GLU B 164 ? 0.4683 0.4706 0.5638 0.0449 -0.0133 0.0407 162 GLU B CG 2825 C CD . GLU B 164 ? 0.5344 0.5179 0.6098 0.0417 -0.0252 0.0361 162 GLU B CD 2826 O OE1 . GLU B 164 ? 0.5995 0.5783 0.6752 0.0345 -0.0342 0.0349 162 GLU B OE1 2827 O OE2 . GLU B 164 ? 0.5283 0.5024 0.5882 0.0459 -0.0264 0.0344 162 GLU B OE2 2828 N N . THR B 165 ? 0.1736 0.2350 0.3597 0.0346 -0.0027 0.0632 163 THR B N 2829 C CA . THR B 165 ? 0.1741 0.2464 0.3887 0.0271 -0.0056 0.0692 163 THR B CA 2830 C C . THR B 165 ? 0.1684 0.2727 0.4062 0.0343 -0.0017 0.0780 163 THR B C 2831 O O . THR B 165 ? 0.1632 0.2836 0.3968 0.0446 0.0069 0.0807 163 THR B O 2832 C CB . THR B 165 ? 0.1781 0.2466 0.4058 0.0184 0.0004 0.0750 163 THR B CB 2833 O OG1 . THR B 165 ? 0.1884 0.2635 0.4451 0.0097 -0.0054 0.0797 163 THR B OG1 2834 C CG2 . THR B 165 ? 0.1804 0.2675 0.4150 0.0240 0.0136 0.0864 163 THR B CG2 2835 N N . VAL B 166 ? 0.1934 0.3086 0.4560 0.0292 -0.0083 0.0818 164 VAL B N 2836 C CA . VAL B 166 ? 0.1950 0.3449 0.4852 0.0343 -0.0036 0.0919 164 VAL B CA 2837 C C . VAL B 166 ? 0.2346 0.3975 0.5537 0.0243 0.0016 0.1060 164 VAL B C 2838 O O . VAL B 166 ? 0.2672 0.4243 0.6057 0.0137 -0.0072 0.1075 164 VAL B O 2839 C CB . VAL B 166 ? 0.1702 0.3271 0.4731 0.0358 -0.0154 0.0882 164 VAL B CB 2840 C CG1 . VAL B 166 ? 0.1647 0.3618 0.4973 0.0425 -0.0088 0.0981 164 VAL B CG1 2841 C CG2 . VAL B 166 ? 0.1757 0.3151 0.4517 0.0439 -0.0237 0.0755 164 VAL B CG2 2842 N N . PRO B 167 ? 0.2122 0.3928 0.5352 0.0273 0.0149 0.1170 165 PRO B N 2843 C CA . PRO B 167 ? 0.2049 0.3970 0.5564 0.0170 0.0193 0.1334 165 PRO B CA 2844 C C . PRO B 167 ? 0.1997 0.4169 0.5855 0.0120 0.0163 0.1441 165 PRO B C 2845 O O . PRO B 167 ? 0.1604 0.3997 0.5438 0.0201 0.0196 0.1438 165 PRO B O 2846 C CB . PRO B 167 ? 0.2321 0.4433 0.5747 0.0239 0.0338 0.1431 165 PRO B CB 2847 C CG . PRO B 167 ? 0.2383 0.4346 0.5453 0.0351 0.0352 0.1282 165 PRO B CG 2848 C CD . PRO B 167 ? 0.2121 0.4018 0.5129 0.0398 0.0250 0.1149 165 PRO B CD 2849 N N . ARG B 168 ? 0.1634 0.3698 0.5723 -0.0016 0.0090 0.1500 166 ARG B N 2850 C CA . ARG B 168 ? 0.2534 0.4739 0.6864 -0.0081 0.0050 0.1595 166 ARG B CA 2851 C C . ARG B 168 ? 0.2956 0.5209 0.7383 -0.0147 0.0111 0.1770 166 ARG B C 2852 O O . ARG B 168 ? 0.3543 0.5621 0.7926 -0.0182 0.0124 0.1795 166 ARG B O 2853 C CB . ARG B 168 ? 0.2553 0.4578 0.7080 -0.0183 -0.0118 0.1518 166 ARG B CB 2854 C CG . ARG B 168 ? 0.2601 0.4628 0.7069 -0.0124 -0.0213 0.1381 166 ARG B CG 2855 C CD . ARG B 168 ? 0.2767 0.4524 0.7277 -0.0232 -0.0388 0.1270 166 ARG B CD 2856 N NE . ARG B 168 ? 0.2811 0.4570 0.7253 -0.0192 -0.0498 0.1171 166 ARG B NE 2857 C CZ . ARG B 168 ? 0.2607 0.4171 0.6687 -0.0124 -0.0541 0.1023 166 ARG B CZ 2858 N NH1 . ARG B 168 ? 0.2617 0.3977 0.6372 -0.0090 -0.0476 0.0950 166 ARG B NH1 2859 N NH2 . ARG B 168 ? 0.2705 0.4283 0.6767 -0.0096 -0.0657 0.0960 166 ARG B NH2 2860 N N . SER B 169 ? 0.3206 0.5703 0.7770 -0.0156 0.0140 0.1894 167 SER B N 2861 C CA . SER B 169 ? 0.3187 0.5761 0.7861 -0.0214 0.0181 0.2086 167 SER B CA 2862 C C . SER B 169 ? 0.3119 0.5406 0.7987 -0.0330 0.0068 0.2116 167 SER B C 2863 O O . SER B 169 ? 0.3203 0.5347 0.8246 -0.0398 -0.0056 0.2041 167 SER B O 2864 C CB . SER B 169 ? 0.3402 0.6282 0.8247 -0.0222 0.0204 0.2206 167 SER B CB 2865 O OG . SER B 169 ? 0.3758 0.6589 0.8831 -0.0284 0.0086 0.2160 167 SER B OG 2866 N N . GLY B 170 ? 0.3241 0.5446 0.8078 -0.0344 0.0099 0.2211 168 GLY B N 2867 C CA . GLY B 170 ? 0.3441 0.5380 0.8472 -0.0431 -0.0010 0.2227 168 GLY B CA 2868 C C . GLY B 170 ? 0.3274 0.4919 0.8167 -0.0421 -0.0034 0.2065 168 GLY B C 2869 O O . GLY B 170 ? 0.3427 0.4889 0.8404 -0.0453 -0.0080 0.2084 168 GLY B O 2870 N N . GLU B 171 ? 0.3072 0.4686 0.7771 -0.0373 -0.0008 0.1904 169 GLU B N 2871 C CA . GLU B 171 ? 0.3125 0.4480 0.7684 -0.0369 -0.0024 0.1743 169 GLU B CA 2872 C C . GLU B 171 ? 0.2958 0.4285 0.7373 -0.0323 0.0066 0.1812 169 GLU B C 2873 O O . GLU B 171 ? 0.2520 0.4066 0.6805 -0.0258 0.0170 0.1930 169 GLU B O 2874 C CB . GLU B 171 ? 0.3049 0.4432 0.7425 -0.0314 -0.0006 0.1591 169 GLU B CB 2875 C CG . GLU B 171 ? 0.3006 0.4335 0.7510 -0.0368 -0.0139 0.1473 169 GLU B CG 2876 C CD . GLU B 171 ? 0.3381 0.4652 0.7534 -0.0274 -0.0145 0.1304 169 GLU B CD 2877 O OE1 . GLU B 171 ? 0.3104 0.4481 0.7028 -0.0166 -0.0038 0.1315 169 GLU B OE1 2878 O OE2 . GLU B 171 ? 0.3835 0.4938 0.7918 -0.0305 -0.0268 0.1158 169 GLU B OE2 2879 N N . VAL B 172 ? 0.3522 0.4585 0.7950 -0.0352 0.0020 0.1726 170 VAL B N 2880 C CA . VAL B 172 ? 0.3567 0.4586 0.7846 -0.0302 0.0094 0.1762 170 VAL B CA 2881 C C . VAL B 172 ? 0.2767 0.3577 0.6844 -0.0284 0.0114 0.1571 170 VAL B C 2882 O O . VAL B 172 ? 0.2628 0.3199 0.6756 -0.0336 0.0029 0.1412 170 VAL B O 2883 C CB . VAL B 172 ? 0.3892 0.4813 0.8383 -0.0337 0.0028 0.1847 170 VAL B CB 2884 C CG1 . VAL B 172 ? 0.4137 0.4838 0.8855 -0.0412 -0.0111 0.1722 170 VAL B CG1 2885 C CG2 . VAL B 172 ? 0.3730 0.4558 0.8081 -0.0289 0.0079 0.1828 170 VAL B CG2 2886 N N . TYR B 173 ? 0.2334 0.3238 0.6162 -0.0206 0.0224 0.1580 171 TYR B N 2887 C CA . TYR B 173 ? 0.2412 0.3119 0.5996 -0.0176 0.0250 0.1414 171 TYR B CA 2888 C C . TYR B 173 ? 0.2503 0.3108 0.6040 -0.0156 0.0292 0.1449 171 TYR B C 2889 O O . TYR B 173 ? 0.2729 0.3490 0.6283 -0.0119 0.0327 0.1600 171 TYR B O 2890 C CB . TYR B 173 ? 0.1981 0.2805 0.5230 -0.0066 0.0311 0.1352 171 TYR B CB 2891 C CG . TYR B 173 ? 0.2074 0.2947 0.5299 -0.0059 0.0246 0.1270 171 TYR B CG 2892 C CD1 . TYR B 173 ? 0.1914 0.3068 0.5376 -0.0070 0.0250 0.1403 171 TYR B CD1 2893 C CD2 . TYR B 173 ? 0.1790 0.2449 0.4765 -0.0045 0.0178 0.1071 171 TYR B CD2 2894 C CE1 . TYR B 173 ? 0.1781 0.2985 0.5247 -0.0060 0.0182 0.1330 171 TYR B CE1 2895 C CE2 . TYR B 173 ? 0.1712 0.2414 0.4673 -0.0041 0.0104 0.1009 171 TYR B CE2 2896 C CZ . TYR B 173 ? 0.1806 0.2774 0.5020 -0.0045 0.0103 0.1134 171 TYR B CZ 2897 O OH . TYR B 173 ? 0.1711 0.2726 0.4935 -0.0037 0.0022 0.1075 171 TYR B OH 2898 N N . THR B 174 ? 0.2479 0.2816 0.5904 -0.0164 0.0272 0.1285 172 THR B N 2899 C CA . THR B 174 ? 0.2190 0.2431 0.5569 -0.0133 0.0297 0.1283 172 THR B CA 2900 C C . THR B 174 ? 0.2209 0.2296 0.5267 -0.0081 0.0349 0.1137 172 THR B C 2901 O O . THR B 174 ? 0.2623 0.2552 0.5511 -0.0083 0.0306 0.0943 172 THR B O 2902 C CB . THR B 174 ? 0.2105 0.2182 0.5712 -0.0182 0.0199 0.1206 172 THR B CB 2903 O OG1 . THR B 174 ? 0.2886 0.3094 0.6776 -0.0221 0.0134 0.1344 172 THR B OG1 2904 C CG2 . THR B 174 ? 0.1906 0.1926 0.5492 -0.0144 0.0222 0.1199 172 THR B CG2 2905 N N . CYS B 175 ? 0.2146 0.2303 0.5075 -0.0023 0.0427 0.1216 173 CYS B N 2906 C CA . CYS B 175 ? 0.2345 0.2359 0.4976 0.0032 0.0459 0.1073 173 CYS B CA 2907 C C . CYS B 175 ? 0.2701 0.2588 0.5452 0.0017 0.0447 0.1038 173 CYS B C 2908 O O . CYS B 175 ? 0.2933 0.2946 0.5831 0.0024 0.0442 0.1157 173 CYS B O 2909 C CB . CYS B 175 ? 0.1824 0.1997 0.4218 0.0115 0.0533 0.1144 173 CYS B CB 2910 S SG . CYS B 175 ? 0.2629 0.2634 0.4687 0.0173 0.0561 0.0988 173 CYS B SG 2911 N N . GLN B 176 ? 0.2625 0.2298 0.5286 0.0010 0.0431 0.0853 174 GLN B N 2912 C CA . GLN B 176 ? 0.2649 0.2236 0.5413 0.0007 0.0411 0.0772 174 GLN B CA 2913 C C . GLN B 176 ? 0.2326 0.1838 0.4845 0.0056 0.0473 0.0684 174 GLN B C 2914 O O . GLN B 176 ? 0.2410 0.1826 0.4693 0.0071 0.0496 0.0575 174 GLN B O 2915 C CB . GLN B 176 ? 0.2564 0.1997 0.5478 -0.0043 0.0334 0.0606 174 GLN B CB 2916 C CG . GLN B 176 ? 0.2399 0.1752 0.5450 -0.0038 0.0309 0.0504 174 GLN B CG 2917 C CD . GLN B 176 ? 0.2743 0.1941 0.5856 -0.0067 0.0244 0.0283 174 GLN B CD 2918 O OE1 . GLN B 176 ? 0.3638 0.2730 0.6537 -0.0054 0.0274 0.0106 174 GLN B OE1 2919 N NE2 . GLN B 176 ? 0.2309 0.1505 0.5711 -0.0105 0.0152 0.0288 174 GLN B NE2 2920 N N . VAL B 177 ? 0.2226 0.1794 0.4803 0.0079 0.0489 0.0737 175 VAL B N 2921 C CA . VAL B 177 ? 0.2335 0.1867 0.4704 0.0123 0.0544 0.0681 175 VAL B CA 2922 C C . VAL B 177 ? 0.2324 0.1783 0.4835 0.0117 0.0529 0.0584 175 VAL B C 2923 O O . VAL B 177 ? 0.2206 0.1722 0.4966 0.0102 0.0489 0.0658 175 VAL B O 2924 C CB . VAL B 177 ? 0.2518 0.2215 0.4788 0.0165 0.0582 0.0839 175 VAL B CB 2925 C CG1 . VAL B 177 ? 0.2383 0.2042 0.4478 0.0202 0.0620 0.0783 175 VAL B CG1 2926 C CG2 . VAL B 177 ? 0.2415 0.2195 0.4528 0.0188 0.0604 0.0913 175 VAL B CG2 2927 N N . GLU B 178 ? 0.2438 0.1783 0.4801 0.0131 0.0561 0.0421 176 GLU B N 2928 C CA . GLU B 178 ? 0.2256 0.1556 0.4737 0.0138 0.0560 0.0319 176 GLU B CA 2929 C C . GLU B 178 ? 0.2105 0.1430 0.4401 0.0176 0.0622 0.0323 176 GLU B C 2930 O O . GLU B 178 ? 0.2194 0.1500 0.4233 0.0193 0.0666 0.0302 176 GLU B O 2931 C CB . GLU B 178 ? 0.2398 0.1576 0.4899 0.0125 0.0545 0.0098 176 GLU B CB 2932 C CG . GLU B 178 ? 0.3181 0.2326 0.5918 0.0085 0.0461 0.0072 176 GLU B CG 2933 C CD . GLU B 178 ? 0.3974 0.3011 0.6646 0.0070 0.0440 -0.0154 176 GLU B CD 2934 O OE1 . GLU B 178 ? 0.4040 0.3036 0.6905 0.0064 0.0385 -0.0285 176 GLU B OE1 2935 O OE2 . GLU B 178 ? 0.4198 0.3200 0.6626 0.0064 0.0473 -0.0206 176 GLU B OE2 2936 N N . HIS B 179 ? 0.2446 0.1811 0.4889 0.0186 0.0617 0.0352 177 HIS B N 2937 C CA . HIS B 179 ? 0.2290 0.1699 0.4599 0.0215 0.0661 0.0388 177 HIS B CA 2938 C C . HIS B 179 ? 0.2406 0.1823 0.4941 0.0218 0.0644 0.0362 177 HIS B C 2939 O O . HIS B 179 ? 0.2187 0.1613 0.4985 0.0201 0.0587 0.0396 177 HIS B O 2940 C CB . HIS B 179 ? 0.2341 0.1869 0.4554 0.0228 0.0659 0.0572 177 HIS B CB 2941 C CG . HIS B 179 ? 0.2246 0.1817 0.4298 0.0257 0.0690 0.0605 177 HIS B CG 2942 N ND1 . HIS B 179 ? 0.2221 0.1870 0.4390 0.0265 0.0673 0.0691 177 HIS B ND1 2943 C CD2 . HIS B 179 ? 0.2221 0.1768 0.4016 0.0278 0.0724 0.0568 177 HIS B CD2 2944 C CE1 . HIS B 179 ? 0.2160 0.1829 0.4150 0.0289 0.0697 0.0698 177 HIS B CE1 2945 N NE2 . HIS B 179 ? 0.1862 0.1470 0.3629 0.0298 0.0726 0.0625 177 HIS B NE2 2946 N N . PRO B 180 ? 0.2275 0.1690 0.4728 0.0240 0.0687 0.0306 178 PRO B N 2947 C CA . PRO B 180 ? 0.1847 0.1270 0.4521 0.0249 0.0671 0.0272 178 PRO B CA 2948 C C . PRO B 180 ? 0.2417 0.1918 0.5292 0.0240 0.0616 0.0444 178 PRO B C 2949 O O . PRO B 180 ? 0.1913 0.1407 0.5047 0.0239 0.0577 0.0425 178 PRO B O 2950 C CB . PRO B 180 ? 0.1809 0.1247 0.4317 0.0272 0.0732 0.0229 178 PRO B CB 2951 C CG . PRO B 180 ? 0.1795 0.1196 0.4034 0.0272 0.0781 0.0157 178 PRO B CG 2952 C CD . PRO B 180 ? 0.1740 0.1140 0.3912 0.0257 0.0748 0.0257 178 PRO B CD 2953 N N . SER B 181 ? 0.2182 0.1768 0.4943 0.0238 0.0611 0.0603 179 SER B N 2954 C CA . SER B 181 ? 0.2308 0.2000 0.5232 0.0230 0.0563 0.0775 179 SER B CA 2955 C C . SER B 181 ? 0.2243 0.1948 0.5423 0.0200 0.0502 0.0831 179 SER B C 2956 O O . SER B 181 ? 0.2367 0.2156 0.5754 0.0186 0.0450 0.0969 179 SER B O 2957 C CB . SER B 181 ? 0.1660 0.1465 0.4360 0.0247 0.0580 0.0908 179 SER B CB 2958 O OG . SER B 181 ? 0.1633 0.1454 0.4226 0.0242 0.0588 0.0930 179 SER B OG 2959 N N . LEU B 182 ? 0.2366 0.1990 0.5539 0.0187 0.0501 0.0730 180 LEU B N 2960 C CA . LEU B 182 ? 0.2521 0.2152 0.5936 0.0155 0.0436 0.0779 180 LEU B CA 2961 C C . LEU B 182 ? 0.2555 0.2072 0.6220 0.0146 0.0387 0.0625 180 LEU B C 2962 O O . LEU B 182 ? 0.2982 0.2406 0.6557 0.0166 0.0423 0.0439 180 LEU B O 2963 C CB . LEU B 182 ? 0.2443 0.2073 0.5703 0.0143 0.0451 0.0782 180 LEU B CB 2964 C CG . LEU B 182 ? 0.2229 0.1974 0.5236 0.0162 0.0497 0.0908 180 LEU B CG 2965 C CD1 . LEU B 182 ? 0.1741 0.1461 0.4611 0.0154 0.0512 0.0877 180 LEU B CD1 2966 C CD2 . LEU B 182 ? 0.2483 0.2399 0.5624 0.0158 0.0464 0.1118 180 LEU B CD2 2967 N N . THR B 183 ? 0.2577 0.2113 0.6563 0.0119 0.0303 0.0699 181 THR B N 2968 C CA . THR B 183 ? 0.2679 0.2112 0.6941 0.0116 0.0237 0.0550 181 THR B CA 2969 C C . THR B 183 ? 0.2755 0.2124 0.7085 0.0091 0.0191 0.0476 181 THR B C 2970 O O . THR B 183 ? 0.3663 0.2936 0.8172 0.0094 0.0137 0.0310 181 THR B O 2971 C CB . THR B 183 ? 0.2964 0.2444 0.7591 0.0102 0.0151 0.0669 181 THR B CB 2972 O OG1 . THR B 183 ? 0.3004 0.2609 0.7722 0.0068 0.0111 0.0904 181 THR B OG1 2973 C CG2 . THR B 183 ? 0.2743 0.2256 0.7343 0.0128 0.0185 0.0690 181 THR B CG2 2974 N N . SER B 184 ? 0.2284 0.1716 0.6474 0.0070 0.0208 0.0595 182 SER B N 2975 C CA . SER B 184 ? 0.2890 0.2271 0.7109 0.0043 0.0168 0.0540 182 SER B CA 2976 C C . SER B 184 ? 0.2853 0.2300 0.6778 0.0039 0.0234 0.0629 182 SER B C 2977 O O . SER B 184 ? 0.2572 0.2129 0.6351 0.0056 0.0287 0.0769 182 SER B O 2978 C CB . SER B 184 ? 0.3100 0.2522 0.7693 0.0005 0.0057 0.0662 182 SER B CB 2979 O OG . SER B 184 ? 0.3272 0.2859 0.7894 -0.0011 0.0060 0.0919 182 SER B OG 2980 N N . PRO B 185 ? 0.3102 0.2486 0.6942 0.0021 0.0225 0.0541 183 PRO B N 2981 C CA . PRO B 185 ? 0.2597 0.2040 0.6167 0.0022 0.0286 0.0616 183 PRO B CA 2982 C C . PRO B 185 ? 0.2642 0.2267 0.6276 0.0013 0.0284 0.0865 183 PRO B C 2983 O O . PRO B 185 ? 0.2806 0.2497 0.6724 -0.0016 0.0212 0.0979 183 PRO B O 2984 C CB . PRO B 185 ? 0.2230 0.1578 0.5801 -0.0010 0.0244 0.0494 183 PRO B CB 2985 C CG . PRO B 185 ? 0.2310 0.1525 0.6001 -0.0006 0.0198 0.0278 183 PRO B CG 2986 C CD . PRO B 185 ? 0.2359 0.1615 0.6322 0.0003 0.0160 0.0351 183 PRO B CD 2987 N N . LEU B 186 ? 0.2301 0.2015 0.5670 0.0044 0.0359 0.0943 184 LEU B N 2988 C CA . LEU B 186 ? 0.2591 0.2504 0.5961 0.0050 0.0370 0.1155 184 LEU B CA 2989 C C . LEU B 186 ? 0.2850 0.2795 0.6141 0.0036 0.0377 0.1174 184 LEU B C 2990 O O . LEU B 186 ? 0.2162 0.2029 0.5216 0.0050 0.0421 0.1068 184 LEU B O 2991 C CB . LEU B 186 ? 0.2694 0.2694 0.5819 0.0101 0.0440 0.1208 184 LEU B CB 2992 C CG . LEU B 186 ? 0.2886 0.3112 0.5946 0.0127 0.0461 0.1403 184 LEU B CG 2993 C CD1 . LEU B 186 ? 0.3432 0.3791 0.6790 0.0097 0.0397 0.1575 184 LEU B CD1 2994 C CD2 . LEU B 186 ? 0.2637 0.2910 0.5473 0.0178 0.0511 0.1409 184 LEU B CD2 2995 N N . THR B 187 ? 0.2750 0.2818 0.6250 0.0006 0.0329 0.1316 185 THR B N 2996 C CA . THR B 187 ? 0.2561 0.2678 0.6028 -0.0013 0.0330 0.1343 185 THR B CA 2997 C C . THR B 187 ? 0.2433 0.2801 0.5874 0.0010 0.0359 0.1553 185 THR B C 2998 O O . THR B 187 ? 0.1867 0.2375 0.5453 0.0011 0.0334 0.1708 185 THR B O 2999 C CB . THR B 187 ? 0.2783 0.2809 0.6523 -0.0074 0.0236 0.1294 185 THR B CB 3000 O OG1 . THR B 187 ? 0.3087 0.3197 0.7130 -0.0096 0.0166 0.1434 185 THR B OG1 3001 C CG2 . THR B 187 ? 0.2774 0.2561 0.6493 -0.0087 0.0207 0.1054 185 THR B CG2 3002 N N . VAL B 188 ? 0.2288 0.2724 0.5546 0.0029 0.0409 0.1554 186 VAL B N 3003 C CA . VAL B 188 ? 0.2322 0.3012 0.5539 0.0056 0.0439 0.1726 186 VAL B CA 3004 C C . VAL B 188 ? 0.2284 0.3013 0.5563 0.0021 0.0425 0.1726 186 VAL B C 3005 O O . VAL B 188 ? 0.2198 0.2816 0.5361 0.0016 0.0443 0.1593 186 VAL B O 3006 C CB . VAL B 188 ? 0.2782 0.3574 0.5680 0.0135 0.0523 0.1730 186 VAL B CB 3007 C CG1 . VAL B 188 ? 0.2653 0.3715 0.5476 0.0169 0.0556 0.1865 186 VAL B CG1 3008 C CG2 . VAL B 188 ? 0.1682 0.2474 0.4541 0.0164 0.0526 0.1753 186 VAL B CG2 3009 N N . GLU B 189 ? 0.2349 0.3242 0.5817 -0.0007 0.0389 0.1881 187 GLU B N 3010 C CA . GLU B 189 ? 0.2231 0.3187 0.5791 -0.0046 0.0369 0.1892 187 GLU B CA 3011 C C . GLU B 189 ? 0.2108 0.3323 0.5483 0.0007 0.0446 0.1972 187 GLU B C 3012 O O . GLU B 189 ? 0.2036 0.3426 0.5276 0.0060 0.0495 0.2072 187 GLU B O 3013 C CB . GLU B 189 ? 0.2549 0.3530 0.6445 -0.0113 0.0276 0.2005 187 GLU B CB 3014 C CG . GLU B 189 ? 0.3152 0.3879 0.7257 -0.0163 0.0183 0.1883 187 GLU B CG 3015 C CD . GLU B 189 ? 0.3691 0.4442 0.8147 -0.0225 0.0078 0.1994 187 GLU B CD 3016 O OE1 . GLU B 189 ? 0.4052 0.4605 0.8699 -0.0265 -0.0012 0.1878 187 GLU B OE1 3017 O OE2 . GLU B 189 ? 0.4020 0.4992 0.8555 -0.0233 0.0083 0.2192 187 GLU B OE2 3018 N N . TRP B 190 ? 0.2070 0.3323 0.5447 -0.0006 0.0449 0.1910 188 TRP B N 3019 C CA . TRP B 190 ? 0.2013 0.3537 0.5266 0.0045 0.0510 0.1963 188 TRP B CA 3020 C C . TRP B 190 ? 0.2485 0.4091 0.5955 -0.0012 0.0462 0.1992 188 TRP B C 3021 O O . TRP B 190 ? 0.2210 0.3658 0.5794 -0.0061 0.0403 0.1879 188 TRP B O 3022 C CB . TRP B 190 ? 0.2187 0.3711 0.5170 0.0126 0.0573 0.1815 188 TRP B CB 3023 C CG . TRP B 190 ? 0.2339 0.4140 0.5191 0.0202 0.0625 0.1820 188 TRP B CG 3024 C CD1 . TRP B 190 ? 0.2486 0.4490 0.5134 0.0283 0.0689 0.1864 188 TRP B CD1 3025 C CD2 . TRP B 190 ? 0.2079 0.3990 0.5007 0.0212 0.0609 0.1762 188 TRP B CD2 3026 N NE1 . TRP B 190 ? 0.2286 0.4515 0.4875 0.0345 0.0719 0.1822 188 TRP B NE1 3027 C CE2 . TRP B 190 ? 0.2048 0.4223 0.4812 0.0305 0.0670 0.1763 188 TRP B CE2 3028 C CE3 . TRP B 190 ? 0.1917 0.3733 0.5044 0.0152 0.0536 0.1699 188 TRP B CE3 3029 C CZ2 . TRP B 190 ? 0.2285 0.4626 0.5088 0.0348 0.0665 0.1702 188 TRP B CZ2 3030 C CZ3 . TRP B 190 ? 0.1584 0.3569 0.4747 0.0191 0.0523 0.1655 188 TRP B CZ3 3031 C CH2 . TRP B 190 ? 0.2176 0.4417 0.5181 0.0292 0.0590 0.1656 188 TRP B CH2 3032 N N . ARG B 191 ? 0.3032 0.4897 0.6559 -0.0008 0.0484 0.2140 189 ARG B N 3033 C CA . ARG B 191 ? 0.3304 0.5281 0.7044 -0.0060 0.0442 0.2186 189 ARG B CA 3034 C C . ARG B 191 ? 0.3077 0.5334 0.6674 0.0014 0.0517 0.2163 189 ARG B C 3035 O O . ARG B 191 ? 0.2914 0.5365 0.6308 0.0091 0.0597 0.2197 189 ARG B O 3036 C CB . ARG B 191 ? 0.4046 0.6104 0.8033 -0.0126 0.0394 0.2386 189 ARG B CB 3037 C CG . ARG B 191 ? 0.4785 0.6569 0.9029 -0.0208 0.0279 0.2374 189 ARG B CG 3038 C CD . ARG B 191 ? 0.5517 0.7395 1.0013 -0.0260 0.0224 0.2585 189 ARG B CD 3039 N NE . ARG B 191 ? 0.6172 0.7800 1.0952 -0.0330 0.0097 0.2550 189 ARG B NE 3040 C CZ . ARG B 191 ? 0.6629 0.8055 1.1447 -0.0327 0.0053 0.2493 189 ARG B CZ 3041 N NH1 . ARG B 191 ? 0.6634 0.8072 1.1228 -0.0264 0.0126 0.2479 189 ARG B NH1 3042 N NH2 . ARG B 191 ? 0.6787 0.8006 1.1874 -0.0383 -0.0067 0.2437 189 ARG B NH2 3043 N N . ALA B 192 ? 0.2771 0.5051 0.6483 -0.0003 0.0478 0.2087 190 ALA B N 3044 C CA . ALA B 192 ? 0.2632 0.5197 0.6288 0.0066 0.0530 0.2068 190 ALA B CA 3045 C C . ALA B 192 ? 0.2407 0.5212 0.6258 0.0016 0.0537 0.2250 190 ALA B C 3046 O O . ALA B 192 ? 0.2956 0.5666 0.7057 -0.0085 0.0462 0.2360 190 ALA B O 3047 C CB . ALA B 192 ? 0.2695 0.5189 0.6421 0.0072 0.0467 0.1917 190 ALA B CB 3048 N N . GLY C 1 ? 0.3224 0.3871 0.4477 -0.0254 -0.1153 0.1169 1 GLY C N 3049 C CA . GLY C 1 ? 0.2730 0.3347 0.3963 -0.0125 -0.1095 0.1045 1 GLY C CA 3050 C C . GLY C 1 ? 0.2826 0.3564 0.3912 -0.0147 -0.1014 0.0957 1 GLY C C 3051 O O . GLY C 1 ? 0.3041 0.3854 0.4025 -0.0240 -0.0990 0.0969 1 GLY C O 3052 N N . VAL C 2 ? 0.2716 0.3484 0.3800 -0.0057 -0.0972 0.0868 2 VAL C N 3053 C CA . VAL C 2 ? 0.2646 0.3527 0.3612 -0.0077 -0.0907 0.0774 2 VAL C CA 3054 C C . VAL C 2 ? 0.3069 0.3764 0.3942 0.0019 -0.0844 0.0639 2 VAL C C 3055 O O . VAL C 2 ? 0.3362 0.3952 0.4273 0.0112 -0.0840 0.0600 2 VAL C O 3056 C CB . VAL C 2 ? 0.2509 0.3649 0.3550 -0.0098 -0.0915 0.0795 2 VAL C CB 3057 C CG1 . VAL C 2 ? 0.2328 0.3606 0.3247 -0.0174 -0.0858 0.0686 2 VAL C CG1 3058 C CG2 . VAL C 2 ? 0.2213 0.3573 0.3374 -0.0201 -0.0982 0.0985 2 VAL C CG2 3059 N N . TYR C 3 ? 0.2962 0.3636 0.3725 -0.0002 -0.0795 0.0584 3 TYR C N 3060 C CA . TYR C 3 ? 0.2559 0.3094 0.3250 0.0077 -0.0737 0.0499 3 TYR C CA 3061 C C . TYR C 3 ? 0.2251 0.2877 0.2951 0.0117 -0.0707 0.0425 3 TYR C C 3062 O O . TYR C 3 ? 0.2714 0.3556 0.3453 0.0039 -0.0720 0.0405 3 TYR C O 3063 C CB . TYR C 3 ? 0.2456 0.2990 0.3082 0.0066 -0.0697 0.0487 3 TYR C CB 3064 C CG . TYR C 3 ? 0.2820 0.3239 0.3429 0.0056 -0.0707 0.0539 3 TYR C CG 3065 C CD1 . TYR C 3 ? 0.3016 0.3289 0.3591 0.0101 -0.0693 0.0528 3 TYR C CD1 3066 C CD2 . TYR C 3 ? 0.2948 0.3450 0.3571 -0.0020 -0.0736 0.0605 3 TYR C CD2 3067 C CE1 . TYR C 3 ? 0.3118 0.3351 0.3683 0.0067 -0.0717 0.0578 3 TYR C CE1 3068 C CE2 . TYR C 3 ? 0.3216 0.3658 0.3834 -0.0044 -0.0752 0.0655 3 TYR C CE2 3069 C CZ . TYR C 3 ? 0.3382 0.3699 0.3975 -0.0002 -0.0746 0.0640 3 TYR C CZ 3070 O OH . TYR C 3 ? 0.3587 0.3895 0.4175 -0.0048 -0.0774 0.0699 3 TYR C OH 3071 N N . ALA C 4 ? 0.1854 0.2349 0.2539 0.0196 -0.0680 0.0391 4 ALA C N 3072 C CA . ALA C 4 ? 0.2011 0.2585 0.2759 0.0210 -0.0674 0.0351 4 ALA C CA 3073 C C . ALA C 4 ? 0.2702 0.3158 0.3452 0.0202 -0.0658 0.0350 4 ALA C C 3074 O O . ALA C 4 ? 0.2869 0.3142 0.3516 0.0248 -0.0612 0.0369 4 ALA C O 3075 C CB . ALA C 4 ? 0.1802 0.2306 0.2589 0.0293 -0.0668 0.0335 4 ALA C CB 3076 N N . THR C 5 ? 0.2819 0.3415 0.3699 0.0125 -0.0681 0.0328 5 THR C N 3077 C CA . THR C 5 ? 0.2934 0.3260 0.3650 0.0096 -0.0480 0.0243 5 THR C CA 3078 C C . THR C 5 ? 0.2747 0.2879 0.3391 0.0146 -0.0411 0.0193 5 THR C C 3079 O O . THR C 5 ? 0.2860 0.3146 0.3514 0.0079 -0.0396 0.0114 5 THR C O 3080 C CB . THR C 5 ? 0.3612 0.4027 0.4214 -0.0115 -0.0308 0.0113 5 THR C CB 3081 O OG1 . THR C 5 ? 0.4248 0.4835 0.4873 -0.0198 -0.0336 0.0141 5 THR C OG1 3082 C CG2 . THR C 5 ? 0.3858 0.3899 0.4311 -0.0130 -0.0062 0.0023 5 THR C CG2 3083 C C1 . CIR C 6 ? 0.2596 0.2244 0.2975 0.0105 -0.0114 0.0102 6 CIR C C1 3084 O O1 . CIR C 6 ? 0.3153 0.2638 0.3504 0.0085 0.0018 0.0110 6 CIR C O1 3085 C C2 . CIR C 6 ? 0.2155 0.1906 0.2649 0.0232 -0.0314 0.0207 6 CIR C C2 3086 N N2 . CIR C 6 ? 0.2389 0.2251 0.2971 0.0241 -0.0372 0.0258 6 CIR C N2 3087 C C3 . CIR C 6 ? 0.1550 0.1110 0.1995 0.0317 -0.0338 0.0336 6 CIR C C3 3088 C C4 . CIR C 6 ? 0.3785 0.3245 0.4105 0.0262 -0.0259 0.0291 6 CIR C C4 3089 C C5 . CIR C 6 ? 0.3675 0.3258 0.3993 0.0264 -0.0361 0.0223 6 CIR C C5 3090 N N6 . CIR C 6 ? 0.3757 0.3553 0.4196 0.0254 -0.0379 0.0101 6 CIR C N6 3091 C C7 . CIR C 6 ? 0.4373 0.4288 0.4785 0.0154 -0.0267 -0.0022 6 CIR C C7 3092 O O7 . CIR C 6 ? 0.4485 0.4265 0.4743 0.0070 -0.0150 -0.0047 6 CIR C O7 3093 N N8 . CIR C 6 ? 0.4756 0.4988 0.5338 0.0143 -0.0300 -0.0084 6 CIR C N8 3094 N N . SER C 7 ? 0.2631 0.2311 0.2916 -0.0019 -0.0016 -0.0017 7 SER C N 3095 C CA . SER C 7 ? 0.2629 0.2132 0.2762 -0.0177 0.0201 -0.0117 7 SER C CA 3096 C C . SER C 7 ? 0.2588 0.1700 0.2625 -0.0139 0.0340 -0.0051 7 SER C C 3097 O O . SER C 7 ? 0.2470 0.1537 0.2530 -0.0031 0.0250 0.0070 7 SER C O 3098 C CB . SER C 7 ? 0.2910 0.2673 0.2967 -0.0375 0.0240 -0.0259 7 SER C CB 3099 O OG . SER C 7 ? 0.3534 0.3376 0.3594 -0.0342 0.0189 -0.0262 7 SER C OG 3100 N N . SER C 8 ? 0.2582 0.1409 0.2507 -0.0249 0.0571 -0.0123 8 SER C N 3101 C CA . SER C 8 ? 0.2894 0.1315 0.2759 -0.0217 0.0731 -0.0032 8 SER C CA 3102 C C . SER C 8 ? 0.3209 0.1568 0.2868 -0.0426 0.0836 -0.0154 8 SER C C 3103 O O . SER C 8 ? 0.3228 0.1652 0.2747 -0.0645 0.0945 -0.0346 8 SER C O 3104 C CB . SER C 8 ? 0.3447 0.1498 0.3353 -0.0179 0.0970 -0.0023 8 SER C CB 3105 O OG . SER C 8 ? 0.3712 0.1870 0.3820 0.0010 0.0877 0.0103 8 SER C OG 3106 N N . ALA C 9 ? 0.3361 0.1640 0.2982 -0.0394 0.0796 -0.0035 9 ALA C N 3107 C CA . ALA C 9 ? 0.3365 0.1630 0.2787 -0.0600 0.0875 -0.0133 9 ALA C CA 3108 C C . ALA C 9 ? 0.4247 0.2041 0.3509 -0.0753 0.1156 -0.0187 9 ALA C C 3109 O O . ALA C 9 ? 0.4656 0.2035 0.4001 -0.0628 0.1290 -0.0042 9 ALA C O 3110 C CB . ALA C 9 ? 0.3330 0.1663 0.2736 -0.0553 0.0757 0.0012 9 ALA C CB 3111 N N . VAL C 10 ? 0.4196 0.2060 0.3244 -0.1029 0.1257 -0.0389 10 VAL C N 3112 C CA . VAL C 10 ? 0.4739 0.2196 0.3582 -0.1205 0.1519 -0.0481 10 VAL C CA 3113 C C . VAL C 10 ? 0.4780 0.2046 0.3533 -0.1222 0.1537 -0.0351 10 VAL C C 3114 O O . VAL C 10 ? 0.4650 0.2156 0.3312 -0.1357 0.1437 -0.0354 10 VAL C O 3115 C CB . VAL C 10 ? 0.5363 0.3095 0.3976 -0.1515 0.1586 -0.0739 10 VAL C CB 3116 C CG1 . VAL C 10 ? 0.6115 0.3503 0.4512 -0.1619 0.1846 -0.0852 10 VAL C CG1 3117 C CG2 . VAL C 10 ? 0.5160 0.3284 0.3887 -0.1552 0.1481 -0.0830 10 VAL C CG2 3118 N N . ARG C 11 ? 0.5152 0.2037 0.3954 -0.1096 0.1666 -0.0231 11 ARG C N 3119 C CA . ARG C 11 ? 0.6314 0.3013 0.5054 -0.1126 0.1676 -0.0077 11 ARG C CA 3120 C C . ARG C 11 ? 0.6541 0.3123 0.4972 -0.1407 0.1832 -0.0274 11 ARG C C 3121 O O . ARG C 11 ? 0.5995 0.2584 0.4259 -0.1557 0.1970 -0.0514 11 ARG C O 3122 C CB . ARG C 11 ? 0.6997 0.3412 0.5995 -0.0867 0.1712 0.0189 11 ARG C CB 3123 C CG . ARG C 11 ? 0.8155 0.4303 0.7242 -0.0767 0.1936 0.0096 11 ARG C CG 3124 C CD . ARG C 11 ? 0.9175 0.5205 0.8608 -0.0471 0.1927 0.0381 11 ARG C CD 3125 N NE . ARG C 11 ? 0.9591 0.5900 0.9194 -0.0340 0.1647 0.0670 11 ARG C NE 3126 C CZ . ARG C 11 ? 1.0092 0.6729 0.9803 -0.0234 0.1463 0.0712 11 ARG C CZ 3127 N NH1 . ARG C 11 ? 1.0232 0.7117 1.0035 -0.0161 0.1229 0.0964 11 ARG C NH1 3128 N NH2 . ARG C 11 ? 1.0361 0.7087 1.0060 -0.0231 0.1510 0.0503 11 ARG C NH2 3129 N N . LEU C 12 ? 0.7087 0.3597 0.5420 -0.1499 0.1802 -0.0158 12 LEU C N 3130 C CA . LEU C 12 ? 0.7813 0.4260 0.5828 -0.1784 0.1914 -0.0324 12 LEU C CA 3131 C C . LEU C 12 ? 0.8780 0.4725 0.6722 -0.1792 0.2169 -0.0373 12 LEU C C 3132 O O . LEU C 12 ? 0.8550 0.4190 0.6747 -0.1551 0.2241 -0.0202 12 LEU C O 3133 C CB . LEU C 12 ? 0.7730 0.4293 0.5675 -0.1885 0.1791 -0.0167 12 LEU C CB 3134 C CG . LEU C 12 ? 0.7840 0.4445 0.5452 -0.2194 0.1848 -0.0310 12 LEU C CG 3135 C CD1 . LEU C 12 ? 0.7868 0.4881 0.5273 -0.2408 0.1845 -0.0615 12 LEU C CD1 3136 C CD2 . LEU C 12 ? 0.7295 0.4115 0.4888 -0.2265 0.1698 -0.0132 12 LEU C CD2 3137 N N . ARG C 13 ? 0.9953 0.5851 0.7546 -0.2079 0.2311 -0.0607 13 ARG C N 3138 C CA . ARG C 13 ? 1.1132 0.6541 0.8570 -0.2157 0.2599 -0.0707 13 ARG C CA 3139 C C . ARG C 13 ? 1.1591 0.6856 0.9127 -0.2039 0.2786 -0.0821 13 ARG C C 3140 O O . ARG C 13 ? 1.1895 0.7335 0.9186 -0.2244 0.2889 -0.1076 13 ARG C O 3141 C CB . ARG C 13 ? 1.1655 0.6623 0.9247 -0.2036 0.2646 -0.0442 13 ARG C CB 3142 C CG . ARG C 13 ? 1.1950 0.7055 0.9403 -0.2208 0.2492 -0.0329 13 ARG C CG 3143 C CD . ARG C 13 ? 1.2526 0.7341 1.0245 -0.2045 0.2445 0.0040 13 ARG C CD 3144 N NE . ARG C 13 ? 1.2480 0.7653 1.0196 -0.2126 0.2203 0.0226 13 ARG C NE 3145 C CZ . ARG C 13 ? 1.2125 0.7641 1.0076 -0.1962 0.1986 0.0430 13 ARG C CZ 3146 N NH1 . ARG C 13 ? 1.1904 0.7757 0.9795 -0.2081 0.1811 0.0565 13 ARG C NH1 3147 N NH2 . ARG C 13 ? 1.1854 0.7397 1.0078 -0.1697 0.1955 0.0488 13 ARG C NH2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ILE 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 GLU 3 3 3 GLU GLU A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 HIS 5 5 5 HIS HIS A . n A 1 6 VAL 6 6 6 VAL VAL A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 ILE 8 8 8 ILE ILE A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 GLU 11 11 11 GLU GLU A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 TYR 13 13 13 TYR TYR A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 ASN 15 15 15 ASN ASN A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 PHE 22 22 22 PHE PHE A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 PHE 24 24 24 PHE PHE A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 GLU 30 30 30 GLU GLU A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 HIS 33 33 33 HIS HIS A . n A 1 34 VAL 34 34 34 VAL VAL A . n A 1 35 ASP 35 35 35 ASP ASP A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 LYS 38 38 38 LYS LYS A . n A 1 39 LYS 39 39 39 LYS LYS A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 TRP 43 43 43 TRP TRP A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 PHE 48 48 48 PHE PHE A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 GLU 55 55 55 GLU GLU A . n A 1 56 ALA 56 56 56 ALA ALA A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 ASP 66 66 66 ASP ASP A . n A 1 67 LYS 67 67 67 LYS LYS A . n A 1 68 ALA 68 68 68 ALA ALA A . n A 1 69 ASN 69 69 69 ASN ASN A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 ASN 78 78 78 ASN ASN A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 PRO 87 87 87 PRO PRO A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 THR 93 93 93 THR THR A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 GLU 101 101 101 GLU GLU A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 CYS 107 107 107 CYS CYS A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ILE 109 109 109 ILE ILE A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LYS 111 111 111 LYS LYS A . n A 1 112 PHE 112 112 112 PHE PHE A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 TRP 121 121 121 TRP TRP A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 ASN 124 124 124 ASN ASN A . n A 1 125 GLY 125 125 125 GLY GLY A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 PRO 127 127 127 PRO PRO A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 THR 129 129 129 THR THR A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 LEU 138 138 138 LEU LEU A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 ARG 140 140 140 ARG ARG A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 HIS 143 143 143 HIS HIS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 LYS 147 147 147 LYS LYS A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 HIS 149 149 149 HIS HIS A . n A 1 150 TYR 150 150 150 TYR TYR A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 CYS 163 163 163 CYS CYS A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 HIS 167 167 167 HIS HIS A . n A 1 168 TRP 168 168 168 TRP TRP A . n A 1 169 GLY 169 169 169 GLY GLY A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 PRO 173 173 173 PRO PRO A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 HIS 177 177 177 HIS HIS A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 PHE 180 180 180 PHE PHE A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 THR 182 182 ? ? ? A . n A 1 183 SER 183 183 ? ? ? A . n A 1 184 GLY 184 184 ? ? ? A . n A 1 185 ASP 185 185 ? ? ? A . n A 1 186 ASP 186 186 ? ? ? A . n A 1 187 ASP 187 187 ? ? ? A . n A 1 188 ASP 188 188 ? ? ? A . n A 1 189 LYS 189 189 ? ? ? A . n B 2 1 GLY 1 -1 ? ? ? B . n B 2 2 SER 2 0 ? ? ? B . n B 2 3 GLY 3 1 ? ? ? B . n B 2 4 ASP 4 2 2 ASP ASP B . n B 2 5 THR 5 3 3 THR THR B . n B 2 6 ARG 6 4 4 ARG ARG B . n B 2 7 PRO 7 5 5 PRO PRO B . n B 2 8 ARG 8 6 6 ARG ARG B . n B 2 9 PHE 9 7 7 PHE PHE B . n B 2 10 LEU 10 8 8 LEU LEU B . n B 2 11 GLU 11 9 9 GLU GLU B . n B 2 12 GLN 12 10 10 GLN GLN B . n B 2 13 VAL 13 11 11 VAL VAL B . n B 2 14 LYS 14 12 12 LYS LYS B . n B 2 15 HIS 15 13 13 HIS HIS B . n B 2 16 GLU 16 14 14 GLU GLU B . n B 2 17 CYS 17 15 15 CYS CYS B . n B 2 18 HIS 18 16 16 HIS HIS B . n B 2 19 PHE 19 17 17 PHE PHE B . n B 2 20 PHE 20 18 18 PHE PHE B . n B 2 21 ASN 21 19 19 ASN ASN B . n B 2 22 GLY 22 20 20 GLY GLY B . n B 2 23 THR 23 21 21 THR THR B . n B 2 24 GLU 24 22 22 GLU GLU B . n B 2 25 ARG 25 23 23 ARG ARG B . n B 2 26 VAL 26 24 24 VAL VAL B . n B 2 27 ARG 27 25 25 ARG ARG B . n B 2 28 PHE 28 26 26 PHE PHE B . n B 2 29 LEU 29 27 27 LEU LEU B . n B 2 30 ASP 30 28 28 ASP ASP B . n B 2 31 ARG 31 29 29 ARG ARG B . n B 2 32 TYR 32 30 30 TYR TYR B . n B 2 33 PHE 33 31 31 PHE PHE B . n B 2 34 TYR 34 32 32 TYR TYR B . n B 2 35 HIS 35 33 33 HIS HIS B . n B 2 36 GLN 36 34 34 GLN GLN B . n B 2 37 GLU 37 35 35 GLU GLU B . n B 2 38 GLU 38 36 36 GLU GLU B . n B 2 39 TYR 39 37 37 TYR TYR B . n B 2 40 VAL 40 38 38 VAL VAL B . n B 2 41 ARG 41 39 39 ARG ARG B . n B 2 42 PHE 42 40 40 PHE PHE B . n B 2 43 ASP 43 41 41 ASP ASP B . n B 2 44 SER 44 42 42 SER SER B . n B 2 45 ASP 45 43 43 ASP ASP B . n B 2 46 VAL 46 44 44 VAL VAL B . n B 2 47 GLY 47 45 45 GLY GLY B . n B 2 48 GLU 48 46 46 GLU GLU B . n B 2 49 TYR 49 47 47 TYR TYR B . n B 2 50 ARG 50 48 48 ARG ARG B . n B 2 51 ALA 51 49 49 ALA ALA B . n B 2 52 VAL 52 50 50 VAL VAL B . n B 2 53 THR 53 51 51 THR THR B . n B 2 54 GLU 54 52 52 GLU GLU B . n B 2 55 LEU 55 53 53 LEU LEU B . n B 2 56 GLY 56 54 54 GLY GLY B . n B 2 57 ARG 57 55 55 ARG ARG B . n B 2 58 PRO 58 56 56 PRO PRO B . n B 2 59 ASP 59 57 57 ASP ASP B . n B 2 60 ALA 60 58 58 ALA ALA B . n B 2 61 GLU 61 59 59 GLU GLU B . n B 2 62 TYR 62 60 60 TYR TYR B . n B 2 63 TRP 63 61 61 TRP TRP B . n B 2 64 ASN 64 62 62 ASN ASN B . n B 2 65 SER 65 63 63 SER SER B . n B 2 66 GLN 66 64 64 GLN GLN B . n B 2 67 LYS 67 65 65 LYS LYS B . n B 2 68 ASP 68 66 66 ASP ASP B . n B 2 69 LEU 69 67 67 LEU LEU B . n B 2 70 LEU 70 68 68 LEU LEU B . n B 2 71 GLU 71 69 69 GLU GLU B . n B 2 72 GLN 72 70 70 GLN GLN B . n B 2 73 LYS 73 71 71 LYS LYS B . n B 2 74 ARG 74 72 72 ARG ARG B . n B 2 75 ALA 75 73 73 ALA ALA B . n B 2 76 ALA 76 74 74 ALA ALA B . n B 2 77 VAL 77 75 75 VAL VAL B . n B 2 78 ASP 78 76 76 ASP ASP B . n B 2 79 THR 79 77 77 THR THR B . n B 2 80 TYR 80 78 78 TYR TYR B . n B 2 81 CYS 81 79 79 CYS CYS B . n B 2 82 ARG 82 80 80 ARG ARG B . n B 2 83 HIS 83 81 81 HIS HIS B . n B 2 84 ASN 84 82 82 ASN ASN B . n B 2 85 TYR 85 83 83 TYR TYR B . n B 2 86 GLY 86 84 84 GLY GLY B . n B 2 87 VAL 87 85 85 VAL VAL B . n B 2 88 GLY 88 86 86 GLY GLY B . n B 2 89 GLU 89 87 87 GLU GLU B . n B 2 90 SER 90 88 88 SER SER B . n B 2 91 PHE 91 89 89 PHE PHE B . n B 2 92 THR 92 90 90 THR THR B . n B 2 93 VAL 93 91 91 VAL VAL B . n B 2 94 GLN 94 92 92 GLN GLN B . n B 2 95 ARG 95 93 93 ARG ARG B . n B 2 96 ARG 96 94 94 ARG ARG B . n B 2 97 VAL 97 95 95 VAL VAL B . n B 2 98 TYR 98 96 96 TYR TYR B . n B 2 99 PRO 99 97 97 PRO PRO B . n B 2 100 GLU 100 98 98 GLU GLU B . n B 2 101 VAL 101 99 99 VAL VAL B . n B 2 102 THR 102 100 100 THR THR B . n B 2 103 VAL 103 101 101 VAL VAL B . n B 2 104 TYR 104 102 102 TYR TYR B . n B 2 105 PRO 105 103 103 PRO PRO B . n B 2 106 ALA 106 104 104 ALA ALA B . n B 2 107 LYS 107 105 105 LYS LYS B . n B 2 108 THR 108 106 106 THR THR B . n B 2 109 GLN 109 107 107 GLN GLN B . n B 2 110 PRO 110 108 108 PRO PRO B . n B 2 111 LEU 111 109 109 LEU LEU B . n B 2 112 GLN 112 110 110 GLN GLN B . n B 2 113 HIS 113 111 111 HIS HIS B . n B 2 114 HIS 114 112 112 HIS HIS B . n B 2 115 ASN 115 113 113 ASN ASN B . n B 2 116 LEU 116 114 114 LEU LEU B . n B 2 117 LEU 117 115 115 LEU LEU B . n B 2 118 VAL 118 116 116 VAL VAL B . n B 2 119 CYS 119 117 117 CYS CYS B . n B 2 120 SER 120 118 118 SER SER B . n B 2 121 VAL 121 119 119 VAL VAL B . n B 2 122 ASN 122 120 120 ASN ASN B . n B 2 123 GLY 123 121 121 GLY GLY B . n B 2 124 PHE 124 122 122 PHE PHE B . n B 2 125 TYR 125 123 123 TYR TYR B . n B 2 126 PRO 126 124 124 PRO PRO B . n B 2 127 GLY 127 125 125 GLY GLY B . n B 2 128 SER 128 126 126 SER SER B . n B 2 129 ILE 129 127 127 ILE ILE B . n B 2 130 GLU 130 128 128 GLU GLU B . n B 2 131 VAL 131 129 129 VAL VAL B . n B 2 132 ARG 132 130 130 ARG ARG B . n B 2 133 TRP 133 131 131 TRP TRP B . n B 2 134 PHE 134 132 132 PHE PHE B . n B 2 135 ARG 135 133 133 ARG ARG B . n B 2 136 ASN 136 134 134 ASN ASN B . n B 2 137 GLY 137 135 135 GLY GLY B . n B 2 138 GLN 138 136 136 GLN GLN B . n B 2 139 GLU 139 137 137 GLU GLU B . n B 2 140 GLU 140 138 138 GLU GLU B . n B 2 141 LYS 141 139 139 LYS LYS B . n B 2 142 THR 142 140 140 THR THR B . n B 2 143 GLY 143 141 141 GLY GLY B . n B 2 144 VAL 144 142 142 VAL VAL B . n B 2 145 VAL 145 143 143 VAL VAL B . n B 2 146 SER 146 144 144 SER SER B . n B 2 147 THR 147 145 145 THR THR B . n B 2 148 GLY 148 146 146 GLY GLY B . n B 2 149 LEU 149 147 147 LEU LEU B . n B 2 150 ILE 150 148 148 ILE ILE B . n B 2 151 GLN 151 149 149 GLN GLN B . n B 2 152 ASN 152 150 150 ASN ASN B . n B 2 153 GLY 153 151 151 GLY GLY B . n B 2 154 ASP 154 152 152 ASP ASP B . n B 2 155 TRP 155 153 153 TRP TRP B . n B 2 156 THR 156 154 154 THR THR B . n B 2 157 PHE 157 155 155 PHE PHE B . n B 2 158 GLN 158 156 156 GLN GLN B . n B 2 159 THR 159 157 157 THR THR B . n B 2 160 LEU 160 158 158 LEU LEU B . n B 2 161 VAL 161 159 159 VAL VAL B . n B 2 162 MET 162 160 160 MET MET B . n B 2 163 LEU 163 161 161 LEU LEU B . n B 2 164 GLU 164 162 162 GLU GLU B . n B 2 165 THR 165 163 163 THR THR B . n B 2 166 VAL 166 164 164 VAL VAL B . n B 2 167 PRO 167 165 165 PRO PRO B . n B 2 168 ARG 168 166 166 ARG ARG B . n B 2 169 SER 169 167 167 SER SER B . n B 2 170 GLY 170 168 168 GLY GLY B . n B 2 171 GLU 171 169 169 GLU GLU B . n B 2 172 VAL 172 170 170 VAL VAL B . n B 2 173 TYR 173 171 171 TYR TYR B . n B 2 174 THR 174 172 172 THR THR B . n B 2 175 CYS 175 173 173 CYS CYS B . n B 2 176 GLN 176 174 174 GLN GLN B . n B 2 177 VAL 177 175 175 VAL VAL B . n B 2 178 GLU 178 176 176 GLU GLU B . n B 2 179 HIS 179 177 177 HIS HIS B . n B 2 180 PRO 180 178 178 PRO PRO B . n B 2 181 SER 181 179 179 SER SER B . n B 2 182 LEU 182 180 180 LEU LEU B . n B 2 183 THR 183 181 181 THR THR B . n B 2 184 SER 184 182 182 SER SER B . n B 2 185 PRO 185 183 183 PRO PRO B . n B 2 186 LEU 186 184 184 LEU LEU B . n B 2 187 THR 187 185 185 THR THR B . n B 2 188 VAL 188 186 186 VAL VAL B . n B 2 189 GLU 189 187 187 GLU GLU B . n B 2 190 TRP 190 188 188 TRP TRP B . n B 2 191 ARG 191 189 189 ARG ARG B . n B 2 192 ALA 192 190 190 ALA ALA B . n B 2 193 THR 193 191 ? ? ? B . n B 2 194 GLY 194 192 ? ? ? B . n B 2 195 GLY 195 193 ? ? ? B . n B 2 196 ASP 196 194 ? ? ? B . n B 2 197 ASP 197 195 ? ? ? B . n B 2 198 ASP 198 196 ? ? ? B . n B 2 199 ASP 199 197 ? ? ? B . n B 2 200 LYS 200 198 ? ? ? B . n C 3 1 GLY 1 1 1 GLY GLY C . n C 3 2 VAL 2 2 2 VAL VAL C . n C 3 3 TYR 3 3 3 TYR TYR C . n C 3 4 ALA 4 4 4 ALA ALA C . n C 3 5 THR 5 5 5 THR THR C . n C 3 6 CIR 6 6 6 CIR CIR C . n C 3 7 SER 7 7 7 SER SER C . n C 3 8 SER 8 8 8 SER SER C . n C 3 9 ALA 9 9 9 ALA ALA C . n C 3 10 VAL 10 10 10 VAL VAL C . n C 3 11 ARG 11 11 11 ARG ARG C . n C 3 12 LEU 12 12 12 LEU LEU C . n C 3 13 ARG 13 13 13 ARG ARG C . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 B ASN 21 B ASN 19 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 78 A ASN 78 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 118 A ASN 118 ? ASN 'GLYCOSYLATION SITE' 4 C CIR 6 C CIR 6 ? ARG CITRULLINE # _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 trimeric _pdbx_struct_assembly.oligomeric_count 3 # _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)' 7360 ? 1 MORE -24 ? 1 'SSA (A^2)' 18060 ? # _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 HOH _pdbx_struct_special_symmetry.auth_seq_id 664 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id H _pdbx_struct_special_symmetry.label_comp_id HOH _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 2013-12-04 2 'Structure model' 1 1 2013-12-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 41.3202 24.3940 -0.0499 0.1503 0.1514 0.1041 -0.0082 -0.0109 0.0047 2.2239 2.9698 0.9318 0.0512 -0.8730 -0.8830 -0.0335 -0.2880 -0.1886 0.3934 -0.0381 -0.0479 -0.0278 -0.0111 0.0604 'X-RAY DIFFRACTION' 2 ? refined 42.4934 12.3855 6.7608 0.3810 0.2993 0.3688 0.0992 0.0443 0.1548 1.6971 2.8282 3.2858 -0.9052 0.3399 -0.9727 -0.2111 -0.6998 -0.7858 0.7885 0.2001 0.1763 0.4757 -0.0861 -0.1583 'X-RAY DIFFRACTION' 3 ? refined 51.6271 35.8123 -4.7135 0.1376 0.2187 0.1020 -0.0364 -0.0186 -0.0578 1.5637 5.4319 4.4860 -0.4527 0.2539 -3.3921 0.2368 -0.1886 0.0540 0.3580 -0.0876 -0.0367 -0.3447 0.4355 0.0114 'X-RAY DIFFRACTION' 4 ? refined 37.9444 44.2823 -10.1702 0.1391 0.0644 0.1050 -0.0080 -0.0289 0.0406 2.0387 0.7372 0.4873 0.5433 0.0903 0.3883 0.0260 -0.0896 0.2733 0.0774 0.1385 -0.0696 -0.2847 0.0585 -0.0892 'X-RAY DIFFRACTION' 5 ? refined 14.3727 21.4268 5.6496 0.2848 0.1883 0.2301 -0.0022 0.3288 -0.0154 2.2338 3.2439 1.7560 0.4383 0.1492 -0.3645 -0.2671 -0.3119 -0.5421 0.1875 -0.2120 0.3671 0.3719 -0.3427 0.1316 'X-RAY DIFFRACTION' 6 ? refined 24.0338 31.8463 6.1698 0.3111 0.2252 0.1053 0.0584 0.0930 0.0092 1.0393 0.5374 0.1571 0.0694 -0.3838 0.0963 -0.2019 -0.2317 -0.0773 0.3607 0.0965 0.0368 -0.1497 0.0025 0.0111 'X-RAY DIFFRACTION' 7 ? refined 30.0351 27.6829 -1.2439 0.1594 0.1471 0.1009 0.0094 -0.0184 -0.0070 1.7849 0.8039 1.6635 0.3254 -1.0622 -1.0910 -0.0827 -0.0821 -0.0772 0.1376 0.0723 -0.0633 0.3846 0.0092 0.0125 'X-RAY DIFFRACTION' 8 ? refined 14.3800 31.4277 9.9108 0.2950 0.2733 0.2781 0.0523 0.2072 -0.0432 1.1484 1.3544 1.6828 -0.1004 -0.3207 -0.3978 0.1486 -0.2779 0.2626 0.5284 0.0404 0.7104 -0.3520 0.0797 -0.2306 'X-RAY DIFFRACTION' 9 ? refined 17.7654 36.7093 1.5970 0.2354 0.1204 0.2726 0.0556 0.0143 -0.0394 0.8328 3.9208 3.2241 -0.2614 -1.1534 -2.1610 0.3379 0.4032 0.8280 0.2912 0.4750 0.9760 -0.2463 -0.4626 -0.3263 'X-RAY DIFFRACTION' 10 ? refined 48.5019 24.8223 -13.7143 0.0936 0.1067 0.1013 0.0136 -0.0088 -0.0243 2.1532 1.9778 1.2250 -0.2211 -0.5632 0.1559 -0.0747 0.0167 -0.1919 -0.0772 0.0589 -0.1729 -0.0224 0.0556 0.0331 'X-RAY DIFFRACTION' 11 ? refined 11.7410 10.8999 -6.9124 0.1496 0.1520 0.3010 0.0302 0.0601 0.0886 2.9458 1.2868 1.0562 0.0645 1.0523 -0.1725 -0.0721 -0.2827 -0.5785 -0.0869 0.1238 0.1903 0.0299 -0.2505 -0.0569 'X-RAY DIFFRACTION' 12 ? refined 53.7202 26.0256 -6.5433 0.2411 0.1468 0.2366 -0.0255 0.0456 -0.0142 4.5126 1.8358 4.1631 2.8323 -1.5515 -1.4038 0.4570 -0.2109 0.4240 -0.0136 0.0634 0.2152 -0.7199 0.4265 -0.1434 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 3 through 45 ) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 46 through 55 ) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 56 through 76 ) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 77 through 87 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 88 through 102 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 103 through 134 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 135 through 153 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 154 through 166 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 167 through 181 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 2 through 89 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 90 through 190 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1 through 13 ) ; # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal Blu-Ice 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.8.1_1168)' ? 3 MOSFLM 'data reduction' . ? 4 SCALA 'data scaling' . ? 5 # 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 ARG A 100 ? ? 47.73 29.02 2 1 HIS B 33 ? ? 59.69 -114.45 3 1 THR B 90 ? ? -124.17 -72.33 4 1 ASN B 113 ? ? -140.48 18.56 5 1 PRO B 124 ? ? -79.07 -168.19 # 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 LEU 109 ? CG ? B LEU 111 CG 2 1 Y 1 B LEU 109 ? CD1 ? B LEU 111 CD1 3 1 Y 1 B LEU 109 ? CD2 ? B LEU 111 CD2 # 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 ILE 1 ? A ILE 1 2 1 Y 1 A LYS 2 ? A LYS 2 3 1 Y 1 A THR 182 ? A THR 182 4 1 Y 1 A SER 183 ? A SER 183 5 1 Y 1 A GLY 184 ? A GLY 184 6 1 Y 1 A ASP 185 ? A ASP 185 7 1 Y 1 A ASP 186 ? A ASP 186 8 1 Y 1 A ASP 187 ? A ASP 187 9 1 Y 1 A ASP 188 ? A ASP 188 10 1 Y 1 A LYS 189 ? A LYS 189 11 1 Y 1 B GLY -1 ? B GLY 1 12 1 Y 1 B SER 0 ? B SER 2 13 1 Y 1 B GLY 1 ? B GLY 3 14 1 Y 1 B THR 191 ? B THR 193 15 1 Y 1 B GLY 192 ? B GLY 194 16 1 Y 1 B GLY 193 ? B GLY 195 17 1 Y 1 B ASP 194 ? B ASP 196 18 1 Y 1 B ASP 195 ? B ASP 197 19 1 Y 1 B ASP 196 ? B ASP 198 20 1 Y 1 B ASP 197 ? B ASP 199 21 1 Y 1 B LYS 198 ? B LYS 200 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 water HOH # 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 D 4 NAG 1 500 500 NAG NAG A . E 4 NAG 1 501 501 NAG NAG A . F 4 NAG 1 500 500 NAG NAG B . G 5 HOH 1 601 1 HOH HOH A . G 5 HOH 2 602 3 HOH HOH A . G 5 HOH 3 603 4 HOH HOH A . G 5 HOH 4 604 7 HOH HOH A . G 5 HOH 5 605 8 HOH HOH A . G 5 HOH 6 606 9 HOH HOH A . G 5 HOH 7 607 11 HOH HOH A . G 5 HOH 8 608 12 HOH HOH A . G 5 HOH 9 609 13 HOH HOH A . G 5 HOH 10 610 16 HOH HOH A . G 5 HOH 11 611 18 HOH HOH A . G 5 HOH 12 612 20 HOH HOH A . G 5 HOH 13 613 22 HOH HOH A . G 5 HOH 14 614 24 HOH HOH A . G 5 HOH 15 615 25 HOH HOH A . G 5 HOH 16 616 28 HOH HOH A . G 5 HOH 17 617 29 HOH HOH A . G 5 HOH 18 618 31 HOH HOH A . G 5 HOH 19 619 36 HOH HOH A . G 5 HOH 20 620 40 HOH HOH A . G 5 HOH 21 621 41 HOH HOH A . G 5 HOH 22 622 43 HOH HOH A . G 5 HOH 23 623 44 HOH HOH A . G 5 HOH 24 624 45 HOH HOH A . G 5 HOH 25 625 46 HOH HOH A . G 5 HOH 26 626 48 HOH HOH A . G 5 HOH 27 627 52 HOH HOH A . G 5 HOH 28 628 54 HOH HOH A . G 5 HOH 29 629 57 HOH HOH A . G 5 HOH 30 630 58 HOH HOH A . G 5 HOH 31 631 59 HOH HOH A . G 5 HOH 32 632 61 HOH HOH A . G 5 HOH 33 633 62 HOH HOH A . G 5 HOH 34 634 63 HOH HOH A . G 5 HOH 35 635 64 HOH HOH A . G 5 HOH 36 636 68 HOH HOH A . G 5 HOH 37 637 69 HOH HOH A . G 5 HOH 38 638 70 HOH HOH A . G 5 HOH 39 639 71 HOH HOH A . G 5 HOH 40 640 72 HOH HOH A . G 5 HOH 41 641 73 HOH HOH A . G 5 HOH 42 642 74 HOH HOH A . G 5 HOH 43 643 78 HOH HOH A . G 5 HOH 44 644 80 HOH HOH A . G 5 HOH 45 645 81 HOH HOH A . G 5 HOH 46 646 82 HOH HOH A . G 5 HOH 47 647 83 HOH HOH A . G 5 HOH 48 648 85 HOH HOH A . G 5 HOH 49 649 86 HOH HOH A . G 5 HOH 50 650 87 HOH HOH A . G 5 HOH 51 651 88 HOH HOH A . G 5 HOH 52 652 90 HOH HOH A . G 5 HOH 53 653 92 HOH HOH A . G 5 HOH 54 654 93 HOH HOH A . G 5 HOH 55 655 95 HOH HOH A . G 5 HOH 56 656 97 HOH HOH A . G 5 HOH 57 657 98 HOH HOH A . G 5 HOH 58 658 99 HOH HOH A . G 5 HOH 59 659 103 HOH HOH A . G 5 HOH 60 660 104 HOH HOH A . G 5 HOH 61 661 106 HOH HOH A . G 5 HOH 62 662 110 HOH HOH A . G 5 HOH 63 663 111 HOH HOH A . G 5 HOH 64 664 112 HOH HOH A . G 5 HOH 65 665 113 HOH HOH A . G 5 HOH 66 666 115 HOH HOH A . G 5 HOH 67 667 117 HOH HOH A . G 5 HOH 68 668 120 HOH HOH A . G 5 HOH 69 669 122 HOH HOH A . G 5 HOH 70 670 123 HOH HOH A . G 5 HOH 71 671 127 HOH HOH A . G 5 HOH 72 672 129 HOH HOH A . G 5 HOH 73 673 133 HOH HOH A . G 5 HOH 74 674 135 HOH HOH A . G 5 HOH 75 675 140 HOH HOH A . G 5 HOH 76 676 146 HOH HOH A . G 5 HOH 77 677 148 HOH HOH A . G 5 HOH 78 678 156 HOH HOH A . G 5 HOH 79 679 158 HOH HOH A . G 5 HOH 80 680 159 HOH HOH A . G 5 HOH 81 681 161 HOH HOH A . G 5 HOH 82 682 166 HOH HOH A . G 5 HOH 83 683 167 HOH HOH A . G 5 HOH 84 684 168 HOH HOH A . G 5 HOH 85 685 170 HOH HOH A . G 5 HOH 86 686 171 HOH HOH A . G 5 HOH 87 687 175 HOH HOH A . G 5 HOH 88 688 176 HOH HOH A . G 5 HOH 89 689 177 HOH HOH A . G 5 HOH 90 690 179 HOH HOH A . G 5 HOH 91 691 182 HOH HOH A . G 5 HOH 92 692 185 HOH HOH A . G 5 HOH 93 693 188 HOH HOH A . G 5 HOH 94 694 189 HOH HOH A . G 5 HOH 95 695 192 HOH HOH A . G 5 HOH 96 696 194 HOH HOH A . G 5 HOH 97 697 195 HOH HOH A . G 5 HOH 98 698 197 HOH HOH A . G 5 HOH 99 699 201 HOH HOH A . G 5 HOH 100 700 203 HOH HOH A . G 5 HOH 101 701 204 HOH HOH A . G 5 HOH 102 702 212 HOH HOH A . G 5 HOH 103 703 213 HOH HOH A . G 5 HOH 104 704 214 HOH HOH A . G 5 HOH 105 705 215 HOH HOH A . G 5 HOH 106 706 219 HOH HOH A . G 5 HOH 107 707 222 HOH HOH A . G 5 HOH 108 708 224 HOH HOH A . G 5 HOH 109 709 225 HOH HOH A . G 5 HOH 110 710 226 HOH HOH A . G 5 HOH 111 711 227 HOH HOH A . G 5 HOH 112 712 228 HOH HOH A . G 5 HOH 113 713 233 HOH HOH A . G 5 HOH 114 714 237 HOH HOH A . G 5 HOH 115 715 242 HOH HOH A . G 5 HOH 116 716 245 HOH HOH A . G 5 HOH 117 717 249 HOH HOH A . G 5 HOH 118 718 252 HOH HOH A . G 5 HOH 119 719 258 HOH HOH A . G 5 HOH 120 720 259 HOH HOH A . G 5 HOH 121 721 262 HOH HOH A . G 5 HOH 122 722 263 HOH HOH A . G 5 HOH 123 723 265 HOH HOH A . G 5 HOH 124 724 266 HOH HOH A . G 5 HOH 125 725 268 HOH HOH A . G 5 HOH 126 726 269 HOH HOH A . H 5 HOH 1 601 2 HOH HOH B . H 5 HOH 2 602 5 HOH HOH B . H 5 HOH 3 603 6 HOH HOH B . H 5 HOH 4 604 10 HOH HOH B . H 5 HOH 5 605 14 HOH HOH B . H 5 HOH 6 606 15 HOH HOH B . H 5 HOH 7 607 17 HOH HOH B . H 5 HOH 8 608 21 HOH HOH B . H 5 HOH 9 609 23 HOH HOH B . H 5 HOH 10 610 26 HOH HOH B . H 5 HOH 11 611 27 HOH HOH B . H 5 HOH 12 612 30 HOH HOH B . H 5 HOH 13 613 33 HOH HOH B . H 5 HOH 14 614 35 HOH HOH B . H 5 HOH 15 615 37 HOH HOH B . H 5 HOH 16 616 38 HOH HOH B . H 5 HOH 17 617 39 HOH HOH B . H 5 HOH 18 618 42 HOH HOH B . H 5 HOH 19 619 50 HOH HOH B . H 5 HOH 20 620 51 HOH HOH B . H 5 HOH 21 621 55 HOH HOH B . H 5 HOH 22 622 56 HOH HOH B . H 5 HOH 23 623 60 HOH HOH B . H 5 HOH 24 624 65 HOH HOH B . H 5 HOH 25 625 66 HOH HOH B . H 5 HOH 26 626 67 HOH HOH B . H 5 HOH 27 627 75 HOH HOH B . H 5 HOH 28 628 76 HOH HOH B . H 5 HOH 29 629 79 HOH HOH B . H 5 HOH 30 630 84 HOH HOH B . H 5 HOH 31 631 89 HOH HOH B . H 5 HOH 32 632 91 HOH HOH B . H 5 HOH 33 633 94 HOH HOH B . H 5 HOH 34 634 100 HOH HOH B . H 5 HOH 35 635 101 HOH HOH B . H 5 HOH 36 636 102 HOH HOH B . H 5 HOH 37 637 105 HOH HOH B . H 5 HOH 38 638 107 HOH HOH B . H 5 HOH 39 639 108 HOH HOH B . H 5 HOH 40 640 109 HOH HOH B . H 5 HOH 41 641 114 HOH HOH B . H 5 HOH 42 642 118 HOH HOH B . H 5 HOH 43 643 119 HOH HOH B . H 5 HOH 44 644 125 HOH HOH B . H 5 HOH 45 645 126 HOH HOH B . H 5 HOH 46 646 128 HOH HOH B . H 5 HOH 47 647 130 HOH HOH B . H 5 HOH 48 648 131 HOH HOH B . H 5 HOH 49 649 132 HOH HOH B . H 5 HOH 50 650 134 HOH HOH B . H 5 HOH 51 651 136 HOH HOH B . H 5 HOH 52 652 138 HOH HOH B . H 5 HOH 53 653 139 HOH HOH B . H 5 HOH 54 654 142 HOH HOH B . H 5 HOH 55 655 143 HOH HOH B . H 5 HOH 56 656 144 HOH HOH B . H 5 HOH 57 657 147 HOH HOH B . H 5 HOH 58 658 150 HOH HOH B . H 5 HOH 59 659 151 HOH HOH B . H 5 HOH 60 660 152 HOH HOH B . H 5 HOH 61 661 153 HOH HOH B . H 5 HOH 62 662 154 HOH HOH B . H 5 HOH 63 663 162 HOH HOH B . H 5 HOH 64 664 163 HOH HOH B . H 5 HOH 65 665 165 HOH HOH B . H 5 HOH 66 666 172 HOH HOH B . H 5 HOH 67 667 173 HOH HOH B . H 5 HOH 68 668 174 HOH HOH B . H 5 HOH 69 669 178 HOH HOH B . H 5 HOH 70 670 180 HOH HOH B . H 5 HOH 71 671 183 HOH HOH B . H 5 HOH 72 672 186 HOH HOH B . H 5 HOH 73 673 191 HOH HOH B . H 5 HOH 74 674 193 HOH HOH B . H 5 HOH 75 675 196 HOH HOH B . H 5 HOH 76 676 198 HOH HOH B . H 5 HOH 77 677 199 HOH HOH B . H 5 HOH 78 678 200 HOH HOH B . H 5 HOH 79 679 202 HOH HOH B . H 5 HOH 80 680 205 HOH HOH B . H 5 HOH 81 681 206 HOH HOH B . H 5 HOH 82 682 218 HOH HOH B . H 5 HOH 83 683 220 HOH HOH B . H 5 HOH 84 684 221 HOH HOH B . H 5 HOH 85 685 223 HOH HOH B . H 5 HOH 86 686 229 HOH HOH B . H 5 HOH 87 687 230 HOH HOH B . H 5 HOH 88 688 231 HOH HOH B . H 5 HOH 89 689 232 HOH HOH B . H 5 HOH 90 690 234 HOH HOH B . H 5 HOH 91 691 236 HOH HOH B . H 5 HOH 92 692 238 HOH HOH B . H 5 HOH 93 693 240 HOH HOH B . H 5 HOH 94 694 243 HOH HOH B . H 5 HOH 95 695 244 HOH HOH B . H 5 HOH 96 696 246 HOH HOH B . H 5 HOH 97 697 248 HOH HOH B . H 5 HOH 98 698 254 HOH HOH B . H 5 HOH 99 699 256 HOH HOH B . H 5 HOH 100 700 260 HOH HOH B . H 5 HOH 101 701 264 HOH HOH B . H 5 HOH 102 702 267 HOH HOH B . I 5 HOH 1 101 32 HOH HOH C . I 5 HOH 2 102 34 HOH HOH C . I 5 HOH 3 103 77 HOH HOH C . I 5 HOH 4 104 116 HOH HOH C . I 5 HOH 5 105 121 HOH HOH C . I 5 HOH 6 106 124 HOH HOH C . I 5 HOH 7 107 164 HOH HOH C . I 5 HOH 8 108 181 HOH HOH C . I 5 HOH 9 109 241 HOH HOH C . I 5 HOH 10 110 247 HOH HOH C . I 5 HOH 11 111 250 HOH HOH C . #