data_4MD0 # _entry.id 4MD0 # _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 4MD0 RCSB RCSB081756 WWPDB D_1000081756 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCY . unspecified PDB 4MCZ . unspecified PDB 4MD4 . unspecified PDB 4MD5 . unspecified PDB 4MDI . unspecified PDB 4MDJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MD0 _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 4MD0 _cell.length_a 67.127 _cell.length_b 183.413 _cell.length_c 77.312 _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 4MD0 _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' 1438.588 1 ? ? 'Residues 59-71' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 5 water nat water 18.015 354 ? ? ? ? # 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)SSAV(CIR)L(CIR)' 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 CIR n 3 12 LEU n 3 13 CIR 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 64,69 and 71' # 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 4MD0 A 1 ? 181 ? P01903 26 ? 206 ? 1 181 2 2 4MD0 B 3 ? 192 ? P13760 30 ? 219 ? 1 190 3 3 4MD0 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 4MD0 THR A 182 ? UNP P01903 ? ? 'EXPRESSION TAG' 182 1 1 4MD0 SER A 183 ? UNP P01903 ? ? 'EXPRESSION TAG' 183 2 1 4MD0 GLY A 184 ? UNP P01903 ? ? 'EXPRESSION TAG' 184 3 1 4MD0 ASP A 185 ? UNP P01903 ? ? 'EXPRESSION TAG' 185 4 1 4MD0 ASP A 186 ? UNP P01903 ? ? 'EXPRESSION TAG' 186 5 1 4MD0 ASP A 187 ? UNP P01903 ? ? 'EXPRESSION TAG' 187 6 1 4MD0 ASP A 188 ? UNP P01903 ? ? 'EXPRESSION TAG' 188 7 1 4MD0 LYS A 189 ? UNP P01903 ? ? 'EXPRESSION TAG' 189 8 2 4MD0 GLY B 1 ? UNP P13760 ? ? 'EXPRESSION TAG' -1 9 2 4MD0 SER B 2 ? UNP P13760 ? ? 'EXPRESSION TAG' 0 10 2 4MD0 THR B 193 ? UNP P13760 ? ? 'EXPRESSION TAG' 191 11 2 4MD0 GLY B 194 ? UNP P13760 ? ? 'EXPRESSION TAG' 192 12 2 4MD0 GLY B 195 ? UNP P13760 ? ? 'EXPRESSION TAG' 193 13 2 4MD0 ASP B 196 ? UNP P13760 ? ? 'EXPRESSION TAG' 194 14 2 4MD0 ASP B 197 ? UNP P13760 ? ? 'EXPRESSION TAG' 195 15 2 4MD0 ASP B 198 ? UNP P13760 ? ? 'EXPRESSION TAG' 196 16 2 4MD0 ASP B 199 ? UNP P13760 ? ? 'EXPRESSION TAG' 197 17 2 4MD0 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 4MD0 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 2 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_percent_sol 54.00 _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 ;24% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane pH 7.3 , VAPOR DIFFUSION, HANGING DROP, temperature 294K ; # loop_ _diffrn.id _diffrn.ambient_temp _diffrn.ambient_temp_details _diffrn.crystal_id 1 100 ? 1 2 ? ? 1 # loop_ _diffrn_detector.diffrn_id _diffrn_detector.detector _diffrn_detector.type _diffrn_detector.pdbx_collection_date _diffrn_detector.details 1 CCD 'ADSC QUANTUM 315r' 2012-02-25 ? 2 ? ? ? ? # _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 0.95369 _diffrn_radiation_wavelength.wt 1.0 # loop_ _diffrn_source.diffrn_id _diffrn_source.source _diffrn_source.type _diffrn_source.pdbx_synchrotron_site _diffrn_source.pdbx_synchrotron_beamline _diffrn_source.pdbx_wavelength _diffrn_source.pdbx_wavelength_list 1 SYNCHROTRON 'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 'Australian Synchrotron' MX2 ? 0.95369 2 ? ? 'Australian Synchrotron' MX2 ? ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MD0 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 91.26 _reflns.d_resolution_high 2.19 _reflns.number_obs 23984 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs 0.155 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.6 _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 2.2 _reflns_shell.d_res_low 2.32 _reflns_shell.percent_possible_all 98.3 _reflns_shell.Rmerge_I_obs 0.6 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.6 _reflns_shell.pdbx_redundancy 4.6 _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 4MD0 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 23207 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.34 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 39.438 _refine.ls_d_res_high 2.194 _refine.ls_percent_reflns_obs 93.29 _refine.ls_R_factor_obs 0.1759 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1742 _refine.ls_R_factor_R_free 0.2077 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.02 _refine.ls_number_reflns_R_free 1164 _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 20.25 _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 56 _refine_hist.number_atoms_solvent 354 _refine_hist.number_atoms_total 3549 _refine_hist.d_res_high 2.194 _refine_hist.d_res_low 39.438 # 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 0.005 ? ? 3354 'X-RAY DIFFRACTION' ? f_angle_d 1.212 ? ? 4563 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.689 ? ? 1237 'X-RAY DIFFRACTION' ? f_chiral_restr 0.051 ? ? 490 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 594 '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' . 2.1943 2.2942 2747 0.2244 95.00 0.2624 . . 152 . . . . 'X-RAY DIFFRACTION' . 2.2942 2.4151 2820 0.2103 96.00 0.2674 . . 115 . . . . 'X-RAY DIFFRACTION' . 2.4151 2.5664 2806 0.2041 96.00 0.2314 . . 155 . . . . 'X-RAY DIFFRACTION' . 2.5664 2.7645 2795 0.1970 96.00 0.2480 . . 145 . . . . 'X-RAY DIFFRACTION' . 2.7645 3.0426 2744 0.1821 94.00 0.2262 . . 158 . . . . 'X-RAY DIFFRACTION' . 3.0426 3.4827 2729 0.1656 93.00 0.2098 . . 159 . . . . 'X-RAY DIFFRACTION' . 3.4827 4.3869 2693 0.1433 91.00 0.1665 . . 155 . . . . 'X-RAY DIFFRACTION' . 4.3869 39.4448 2709 0.1566 87.00 0.1712 . . 125 . . . . # _struct.entry_id 4MD0 _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 4MD0 _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 4 ? H N N 5 ? I N N 5 ? J 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 ? ? ? ? ? ? ? 2.038 ? disulf3 disulf ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.024 ? covale1 covale ? ? C THR 5 C ? ? ? 1_555 C CIR 6 N2 ? ? C THR 5 C CIR 6 1_555 ? ? ? ? ? ? ? 1.316 ? covale2 covale ? ? C CIR 6 C1 ? ? ? 1_555 C SER 7 N ? ? C CIR 6 C SER 7 1_555 ? ? ? ? ? ? ? 1.351 ? covale3 covale ? ? C VAL 10 C ? ? ? 1_555 C CIR 11 N2 ? ? C VAL 10 C CIR 11 1_555 ? ? ? ? ? ? ? 1.317 ? covale4 covale ? ? C CIR 11 C1 ? ? ? 1_555 C LEU 12 N ? ? C CIR 11 C LEU 12 1_555 ? ? ? ? ? ? ? 1.350 ? covale5 covale ? ? C LEU 12 C ? ? ? 1_555 C CIR 13 N2 ? ? C LEU 12 C CIR 13 1_555 ? ? ? ? ? ? ? 1.349 ? covale6 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.438 ? covale7 covale ? ? B ASN 21 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 19 B NAG 500 1_555 ? ? ? ? ? ? ? 1.440 ? covale8 covale ? ? A ASN 118 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 118 A NAG 501 1_555 ? ? ? ? ? ? ? 1.449 ? covale9 covale ? ? A ASN 78 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 78 A NAG 500 1_555 ? ? ? ? ? ? ? 1.452 ? covale10 covale ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.024 ? covale11 covale ? ? A CYS 107 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107 A CYS 163 1_555 ? ? ? ? ? ? ? 2.031 ? covale12 covale ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.038 ? # 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 4.03 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 1.05 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 2 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? H ? 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 ? 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 H 1 2 ? anti-parallel H 2 3 ? anti-parallel H 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 SER A 53 ? PHE A 54 ? SER A 53 PHE A 54 B 2 VAL C 2 ? TYR C 3 ? VAL C 2 TYR C 3 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 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 D 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 D 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 D 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 D 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 E 1 LYS A 126 ? VAL A 128 ? LYS A 126 VAL A 128 E 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 E 3 TYR A 161 ? GLU A 166 ? TYR A 161 GLU A 166 E 4 LEU A 174 ? TRP A 178 ? LEU A 174 TRP A 178 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 VAL B 144 ? SER B 146 ? VAL B 142 SER B 144 G 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 G 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 G 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 G 4 ILE B 150 ? GLN B 151 ? ILE B 148 GLN B 149 H 1 GLN B 138 ? GLU B 140 ? GLN B 136 GLU B 138 H 2 GLU B 130 ? ARG B 135 ? GLU B 128 ARG B 133 H 3 VAL B 172 ? GLU B 178 ? VAL B 170 GLU B 176 H 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 GLU A 40 ? O GLU A 40 N ASP A 35 ? N ASP A 35 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 SER A 53 ? N SER A 53 O TYR C 3 ? O TYR C 3 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 TYR A 150 ? O TYR A 150 N SER A 133 ? N SER A 133 D 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 D 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 D 3 4 O ARG A 146 ? O ARG A 146 N LEU A 138 ? N LEU A 138 E 1 2 O LYS A 126 ? O LYS A 126 N ARG A 123 ? N ARG A 123 E 2 3 N THR A 120 ? N THR A 120 O ARG A 164 ? O ARG A 164 E 3 4 N VAL A 165 ? N VAL A 165 O LEU A 174 ? O LEU A 174 F 1 2 N THR B 102 ? N THR B 100 O SER B 120 ? O SER B 118 F 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 F 3 4 O MET B 162 ? O MET B 160 N VAL B 145 ? N VAL B 143 G 1 2 N THR B 102 ? N THR B 100 O SER B 120 ? O SER B 118 G 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 G 3 4 O GLN B 158 ? O GLN B 156 N ILE B 150 ? N ILE B 148 H 1 2 O GLN B 138 ? O GLN B 136 N ARG B 135 ? N ARG B 133 H 2 3 N ARG B 132 ? N ARG B 130 O GLN B 176 ? O GLN B 174 H 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 ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 500 BOUND TO ASN A 78' AC2 Software ? ? ? ? 7 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 118 RESIDUES 501 TO 502' AC3 Software ? ? ? ? 2 '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 2 ASN A 78 ? ASN A 78 . ? 1_555 ? 2 AC1 2 LYS A 126 ? LYS A 126 . ? 8_555 ? 3 AC2 7 VAL A 116 ? VAL A 116 . ? 1_555 ? 4 AC2 7 ASN A 118 ? ASN A 118 . ? 1_555 ? 5 AC2 7 GLU A 166 ? GLU A 166 . ? 1_555 ? 6 AC2 7 TRP A 168 ? TRP A 168 . ? 1_555 ? 7 AC2 7 HOH H . ? HOH A 674 . ? 1_555 ? 8 AC2 7 HOH H . ? HOH A 717 . ? 1_555 ? 9 AC2 7 ASP B 4 ? ASP B 2 . ? 1_555 ? 10 AC3 2 ASN B 21 ? ASN B 19 . ? 1_555 ? 11 AC3 2 GLU B 24 ? GLU B 22 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MD0 _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 4MD0 _atom_sites.fract_transf_matrix[1][1] 0.014897 _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] 0.012935 _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 ? 35.972 12.569 -18.921 1.00 61.62 ? 3 GLU A N 1 ATOM 2 C CA . GLU A 1 3 ? 36.783 12.247 -17.751 1.00 58.90 ? 3 GLU A CA 1 ATOM 3 C C . GLU A 1 3 ? 35.951 11.632 -16.635 1.00 49.77 ? 3 GLU A C 1 ATOM 4 O O . GLU A 1 3 ? 34.745 11.855 -16.552 1.00 54.54 ? 3 GLU A O 1 ATOM 5 C CB . GLU A 1 3 ? 37.511 13.496 -17.248 1.00 60.58 ? 3 GLU A CB 1 ATOM 6 C CG . GLU A 1 3 ? 36.628 14.520 -16.566 1.00 60.38 ? 3 GLU A CG 1 ATOM 7 C CD . GLU A 1 3 ? 37.022 15.939 -16.926 1.00 61.82 ? 3 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 3 ? 38.135 16.130 -17.461 1.00 61.69 ? 3 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 3 ? 36.217 16.861 -16.681 1.00 62.19 ? 3 GLU A OE2 1 ATOM 10 N N . GLU A 1 4 ? 36.607 10.860 -15.774 1.00 40.08 ? 4 GLU A N 1 ATOM 11 C CA . GLU A 1 4 ? 35.928 10.241 -14.646 1.00 37.67 ? 4 GLU A CA 1 ATOM 12 C C . GLU A 1 4 ? 35.961 11.123 -13.413 1.00 31.22 ? 4 GLU A C 1 ATOM 13 O O . GLU A 1 4 ? 34.950 11.293 -12.732 1.00 34.27 ? 4 GLU A O 1 ATOM 14 C CB . GLU A 1 4 ? 36.576 8.900 -14.297 1.00 45.18 ? 4 GLU A CB 1 ATOM 15 C CG . GLU A 1 4 ? 36.386 7.795 -15.310 1.00 58.64 ? 4 GLU A CG 1 ATOM 16 C CD . GLU A 1 4 ? 36.905 6.468 -14.795 1.00 64.45 ? 4 GLU A CD 1 ATOM 17 O OE1 . GLU A 1 4 ? 37.585 6.468 -13.747 1.00 61.54 ? 4 GLU A OE1 1 ATOM 18 O OE2 . GLU A 1 4 ? 36.635 5.429 -15.434 1.00 70.97 ? 4 GLU A OE2 1 ATOM 19 N N . HIS A 1 5 ? 37.126 11.697 -13.134 1.00 25.13 ? 5 HIS A N 1 ATOM 20 C CA . HIS A 1 5 ? 37.286 12.502 -11.934 1.00 24.92 ? 5 HIS A CA 1 ATOM 21 C C . HIS A 1 5 ? 38.257 13.655 -12.135 1.00 21.67 ? 5 HIS A C 1 ATOM 22 O O . HIS A 1 5 ? 39.154 13.595 -12.976 1.00 17.88 ? 5 HIS A O 1 ATOM 23 C CB . HIS A 1 5 ? 37.753 11.620 -10.777 1.00 22.70 ? 5 HIS A CB 1 ATOM 24 C CG . HIS A 1 5 ? 36.818 10.491 -10.474 1.00 24.75 ? 5 HIS A CG 1 ATOM 25 N ND1 . HIS A 1 5 ? 35.563 10.685 -9.939 1.00 24.74 ? 5 HIS A ND1 1 ATOM 26 C CD2 . HIS A 1 5 ? 36.946 9.156 -10.658 1.00 27.62 ? 5 HIS A CD2 1 ATOM 27 C CE1 . HIS A 1 5 ? 34.964 9.517 -9.792 1.00 26.28 ? 5 HIS A CE1 1 ATOM 28 N NE2 . HIS A 1 5 ? 35.782 8.572 -10.220 1.00 30.98 ? 5 HIS A NE2 1 ATOM 29 N N . VAL A 1 6 ? 38.078 14.702 -11.340 1.00 19.94 ? 6 VAL A N 1 ATOM 30 C CA . VAL A 1 6 ? 38.992 15.829 -11.355 1.00 19.44 ? 6 VAL A CA 1 ATOM 31 C C . VAL A 1 6 ? 39.349 16.199 -9.926 1.00 17.70 ? 6 VAL A C 1 ATOM 32 O O . VAL A 1 6 ? 38.475 16.338 -9.070 1.00 18.41 ? 6 VAL A O 1 ATOM 33 C CB . VAL A 1 6 ? 38.380 17.062 -12.069 1.00 14.76 ? 6 VAL A CB 1 ATOM 34 C CG1 . VAL A 1 6 ? 39.359 18.229 -12.057 1.00 15.60 ? 6 VAL A CG1 1 ATOM 35 C CG2 . VAL A 1 6 ? 37.977 16.720 -13.500 1.00 12.93 ? 6 VAL A CG2 1 ATOM 36 N N . ILE A 1 7 ? 40.639 16.379 -9.679 1.00 12.38 ? 7 ILE A N 1 ATOM 37 C CA . ILE A 1 7 ? 41.098 16.852 -8.388 1.00 14.06 ? 7 ILE A CA 1 ATOM 38 C C . ILE A 1 7 ? 41.779 18.184 -8.590 1.00 15.62 ? 7 ILE A C 1 ATOM 39 O O . ILE A 1 7 ? 42.688 18.305 -9.407 1.00 12.69 ? 7 ILE A O 1 ATOM 40 C CB . ILE A 1 7 ? 42.081 15.879 -7.718 1.00 14.50 ? 7 ILE A CB 1 ATOM 41 C CG1 . ILE A 1 7 ? 41.437 14.507 -7.507 1.00 19.72 ? 7 ILE A CG1 1 ATOM 42 C CG2 . ILE A 1 7 ? 42.591 16.468 -6.410 1.00 12.78 ? 7 ILE A CG2 1 ATOM 43 C CD1 . ILE A 1 7 ? 42.387 13.479 -6.925 1.00 16.32 ? 7 ILE A CD1 1 ATOM 44 N N . ILE A 1 8 ? 41.338 19.189 -7.848 1.00 14.61 ? 8 ILE A N 1 ATOM 45 C CA . ILE A 1 8 ? 41.902 20.512 -8.016 1.00 14.19 ? 8 ILE A CA 1 ATOM 46 C C . ILE A 1 8 ? 42.428 21.029 -6.689 1.00 15.28 ? 8 ILE A C 1 ATOM 47 O O . ILE A 1 8 ? 41.732 21.001 -5.673 1.00 15.95 ? 8 ILE A O 1 ATOM 48 C CB . ILE A 1 8 ? 40.863 21.512 -8.576 1.00 8.02 ? 8 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 8 ? 40.324 21.030 -9.923 1.00 8.37 ? 8 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 8 ? 41.469 22.904 -8.705 1.00 11.32 ? 8 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 8 ? 39.233 21.917 -10.503 1.00 11.18 ? 8 ILE A CD1 1 ATOM 52 N N . GLN A 1 9 ? 43.670 21.493 -6.719 1.00 16.07 ? 9 GLN A N 1 ATOM 53 C CA . GLN A 1 9 ? 44.245 22.249 -5.625 1.00 7.71 ? 9 GLN A CA 1 ATOM 54 C C . GLN A 1 9 ? 44.036 23.711 -5.965 1.00 11.23 ? 9 GLN A C 1 ATOM 55 O O . GLN A 1 9 ? 44.702 24.248 -6.852 1.00 7.54 ? 9 GLN A O 1 ATOM 56 C CB . GLN A 1 9 ? 45.727 21.940 -5.459 1.00 8.22 ? 9 GLN A CB 1 ATOM 57 C CG . GLN A 1 9 ? 46.461 22.814 -4.463 1.00 11.68 ? 9 GLN A CG 1 ATOM 58 C CD . GLN A 1 9 ? 47.948 22.537 -4.476 1.00 12.21 ? 9 GLN A CD 1 ATOM 59 O OE1 . GLN A 1 9 ? 48.381 21.398 -4.664 1.00 13.78 ? 9 GLN A OE1 1 ATOM 60 N NE2 . GLN A 1 9 ? 48.743 23.586 -4.306 1.00 14.96 ? 9 GLN A NE2 1 ATOM 61 N N . ALA A 1 10 ? 43.125 24.355 -5.251 1.00 7.72 ? 10 ALA A N 1 ATOM 62 C CA . ALA A 1 10 ? 42.742 25.719 -5.573 1.00 11.26 ? 10 ALA A CA 1 ATOM 63 C C . ALA A 1 10 ? 43.234 26.671 -4.501 1.00 11.04 ? 10 ALA A C 1 ATOM 64 O O . ALA A 1 10 ? 43.065 26.416 -3.314 1.00 15.35 ? 10 ALA A O 1 ATOM 65 C CB . ALA A 1 10 ? 41.231 25.822 -5.729 1.00 14.01 ? 10 ALA A CB 1 ATOM 66 N N . GLU A 1 11 ? 43.822 27.781 -4.930 1.00 13.42 ? 11 GLU A N 1 ATOM 67 C CA . GLU A 1 11 ? 44.387 28.742 -4.003 1.00 15.98 ? 11 GLU A CA 1 ATOM 68 C C . GLU A 1 11 ? 43.907 30.127 -4.396 1.00 16.36 ? 11 GLU A C 1 ATOM 69 O O . GLU A 1 11 ? 43.671 30.384 -5.575 1.00 10.94 ? 11 GLU A O 1 ATOM 70 C CB . GLU A 1 11 ? 45.920 28.712 -4.071 1.00 10.30 ? 11 GLU A CB 1 ATOM 71 C CG . GLU A 1 11 ? 46.556 27.352 -3.831 1.00 17.32 ? 11 GLU A CG 1 ATOM 72 C CD . GLU A 1 11 ? 47.992 27.288 -4.339 1.00 18.74 ? 11 GLU A CD 1 ATOM 73 O OE1 . GLU A 1 11 ? 48.616 28.358 -4.493 1.00 16.02 ? 11 GLU A OE1 1 ATOM 74 O OE2 . GLU A 1 11 ? 48.494 26.173 -4.603 1.00 14.25 ? 11 GLU A OE2 1 ATOM 75 N N . PHE A 1 12 ? 43.763 31.029 -3.431 1.00 17.05 ? 12 PHE A N 1 ATOM 76 C CA . PHE A 1 12 ? 43.627 32.436 -3.781 1.00 15.86 ? 12 PHE A CA 1 ATOM 77 C C . PHE A 1 12 ? 44.269 33.338 -2.730 1.00 14.11 ? 12 PHE A C 1 ATOM 78 O O . PHE A 1 12 ? 44.459 32.946 -1.581 1.00 9.89 ? 12 PHE A O 1 ATOM 79 C CB . PHE A 1 12 ? 42.153 32.818 -4.055 1.00 19.31 ? 12 PHE A CB 1 ATOM 80 C CG . PHE A 1 12 ? 41.264 32.886 -2.836 1.00 19.27 ? 12 PHE A CG 1 ATOM 81 C CD1 . PHE A 1 12 ? 41.310 33.973 -1.969 1.00 16.29 ? 12 PHE A CD1 1 ATOM 82 C CD2 . PHE A 1 12 ? 40.324 31.895 -2.600 1.00 18.68 ? 12 PHE A CD2 1 ATOM 83 C CE1 . PHE A 1 12 ? 40.470 34.043 -0.863 1.00 14.78 ? 12 PHE A CE1 1 ATOM 84 C CE2 . PHE A 1 12 ? 39.479 31.960 -1.503 1.00 19.89 ? 12 PHE A CE2 1 ATOM 85 C CZ . PHE A 1 12 ? 39.552 33.031 -0.632 1.00 16.25 ? 12 PHE A CZ 1 ATOM 86 N N . TYR A 1 13 ? 44.600 34.550 -3.153 1.00 14.61 ? 13 TYR A N 1 ATOM 87 C CA . TYR A 1 13 ? 45.025 35.619 -2.262 1.00 15.51 ? 13 TYR A CA 1 ATOM 88 C C . TYR A 1 13 ? 44.356 36.917 -2.677 1.00 17.97 ? 13 TYR A C 1 ATOM 89 O O . TYR A 1 13 ? 44.299 37.240 -3.860 1.00 15.28 ? 13 TYR A O 1 ATOM 90 C CB . TYR A 1 13 ? 46.548 35.774 -2.253 1.00 13.38 ? 13 TYR A CB 1 ATOM 91 C CG . TYR A 1 13 ? 47.043 36.701 -1.163 1.00 18.34 ? 13 TYR A CG 1 ATOM 92 C CD1 . TYR A 1 13 ? 47.328 36.224 0.113 1.00 20.57 ? 13 TYR A CD1 1 ATOM 93 C CD2 . TYR A 1 13 ? 47.239 38.053 -1.415 1.00 20.48 ? 13 TYR A CD2 1 ATOM 94 C CE1 . TYR A 1 13 ? 47.780 37.078 1.112 1.00 19.57 ? 13 TYR A CE1 1 ATOM 95 C CE2 . TYR A 1 13 ? 47.691 38.908 -0.430 1.00 12.97 ? 13 TYR A CE2 1 ATOM 96 C CZ . TYR A 1 13 ? 47.960 38.420 0.829 1.00 22.43 ? 13 TYR A CZ 1 ATOM 97 O OH . TYR A 1 13 ? 48.410 39.288 1.798 1.00 22.55 ? 13 TYR A OH 1 ATOM 98 N N . LEU A 1 14 ? 43.840 37.651 -1.697 1.00 11.29 ? 14 LEU A N 1 ATOM 99 C CA . LEU A 1 14 ? 43.061 38.847 -1.977 1.00 14.09 ? 14 LEU A CA 1 ATOM 100 C C . LEU A 1 14 ? 43.632 40.066 -1.260 1.00 13.98 ? 14 LEU A C 1 ATOM 101 O O . LEU A 1 14 ? 43.833 40.047 -0.048 1.00 15.84 ? 14 LEU A O 1 ATOM 102 C CB . LEU A 1 14 ? 41.605 38.629 -1.565 1.00 14.89 ? 14 LEU A CB 1 ATOM 103 C CG . LEU A 1 14 ? 40.653 39.813 -1.720 1.00 19.97 ? 14 LEU A CG 1 ATOM 104 C CD1 . LEU A 1 14 ? 40.370 40.103 -3.182 1.00 11.92 ? 14 LEU A CD1 1 ATOM 105 C CD2 . LEU A 1 14 ? 39.371 39.538 -0.969 1.00 12.77 ? 14 LEU A CD2 1 ATOM 106 N N . ASN A 1 15 ? 43.884 41.120 -2.029 1.00 13.78 ? 15 ASN A N 1 ATOM 107 C CA . ASN A 1 15 ? 44.278 42.409 -1.478 1.00 15.99 ? 15 ASN A CA 1 ATOM 108 C C . ASN A 1 15 ? 43.097 43.368 -1.604 1.00 14.27 ? 15 ASN A C 1 ATOM 109 O O . ASN A 1 15 ? 42.290 43.226 -2.517 1.00 15.81 ? 15 ASN A O 1 ATOM 110 C CB . ASN A 1 15 ? 45.498 42.964 -2.219 1.00 13.56 ? 15 ASN A CB 1 ATOM 111 C CG . ASN A 1 15 ? 46.809 42.464 -1.643 1.00 25.38 ? 15 ASN A CG 1 ATOM 112 O OD1 . ASN A 1 15 ? 46.914 42.181 -0.449 1.00 18.85 ? 15 ASN A OD1 1 ATOM 113 N ND2 . ASN A 1 15 ? 47.825 42.367 -2.494 1.00 17.74 ? 15 ASN A ND2 1 ATOM 114 N N . PRO A 1 16 ? 42.973 44.337 -0.680 1.00 16.83 ? 16 PRO A N 1 ATOM 115 C CA . PRO A 1 16 ? 43.889 44.656 0.421 1.00 17.55 ? 16 PRO A CA 1 ATOM 116 C C . PRO A 1 16 ? 43.565 43.879 1.689 1.00 16.17 ? 16 PRO A C 1 ATOM 117 O O . PRO A 1 16 ? 44.155 44.136 2.735 1.00 22.63 ? 16 PRO A O 1 ATOM 118 C CB . PRO A 1 16 ? 43.645 46.149 0.639 1.00 21.11 ? 16 PRO A CB 1 ATOM 119 C CG . PRO A 1 16 ? 42.196 46.311 0.310 1.00 19.35 ? 16 PRO A CG 1 ATOM 120 C CD . PRO A 1 16 ? 41.935 45.371 -0.841 1.00 16.86 ? 16 PRO A CD 1 ATOM 121 N N . ASP A 1 17 ? 42.628 42.946 1.587 1.00 15.57 ? 17 ASP A N 1 ATOM 122 C CA . ASP A 1 17 ? 42.163 42.200 2.746 1.00 16.01 ? 17 ASP A CA 1 ATOM 123 C C . ASP A 1 17 ? 43.245 41.301 3.341 1.00 22.39 ? 17 ASP A C 1 ATOM 124 O O . ASP A 1 17 ? 43.177 40.949 4.518 1.00 16.82 ? 17 ASP A O 1 ATOM 125 C CB . ASP A 1 17 ? 40.936 41.368 2.367 1.00 15.48 ? 17 ASP A CB 1 ATOM 126 C CG . ASP A 1 17 ? 39.836 42.208 1.736 1.00 16.47 ? 17 ASP A CG 1 ATOM 127 O OD1 . ASP A 1 17 ? 39.968 42.576 0.547 1.00 18.32 ? 17 ASP A OD1 1 ATOM 128 O OD2 . ASP A 1 17 ? 38.838 42.504 2.425 1.00 21.04 ? 17 ASP A OD2 1 ATOM 129 N N . GLN A 1 18 ? 44.239 40.947 2.523 1.00 21.72 ? 18 GLN A N 1 ATOM 130 C CA . GLN A 1 18 ? 45.298 40.013 2.913 1.00 18.49 ? 18 GLN A CA 1 ATOM 131 C C . GLN A 1 18 ? 44.674 38.685 3.344 1.00 24.22 ? 18 GLN A C 1 ATOM 132 O O . GLN A 1 18 ? 45.088 38.068 4.331 1.00 22.61 ? 18 GLN A O 1 ATOM 133 C CB . GLN A 1 18 ? 46.184 40.607 4.016 1.00 17.00 ? 18 GLN A CB 1 ATOM 134 C CG . GLN A 1 18 ? 46.916 41.870 3.571 1.00 21.19 ? 18 GLN A CG 1 ATOM 135 C CD . GLN A 1 18 ? 48.010 42.303 4.529 1.00 25.85 ? 18 GLN A CD 1 ATOM 136 O OE1 . GLN A 1 18 ? 49.133 42.588 4.114 1.00 33.47 ? 18 GLN A OE1 1 ATOM 137 N NE2 . GLN A 1 18 ? 47.686 42.362 5.815 1.00 28.84 ? 18 GLN A NE2 1 ATOM 138 N N . SER A 1 19 ? 43.671 38.249 2.584 1.00 20.02 ? 19 SER A N 1 ATOM 139 C CA . SER A 1 19 ? 43.041 36.952 2.809 1.00 19.96 ? 19 SER A CA 1 ATOM 140 C C . SER A 1 19 ? 43.534 35.911 1.814 1.00 17.19 ? 19 SER A C 1 ATOM 141 O O . SER A 1 19 ? 43.557 36.153 0.603 1.00 16.40 ? 19 SER A O 1 ATOM 142 C CB . SER A 1 19 ? 41.522 37.076 2.699 1.00 23.36 ? 19 SER A CB 1 ATOM 143 O OG . SER A 1 19 ? 41.061 38.247 3.346 1.00 40.07 ? 19 SER A OG 1 ATOM 144 N N . GLY A 1 20 ? 43.941 34.756 2.330 1.00 16.46 ? 20 GLY A N 1 ATOM 145 C CA . GLY A 1 20 ? 44.387 33.663 1.489 1.00 22.30 ? 20 GLY A CA 1 ATOM 146 C C . GLY A 1 20 ? 43.821 32.290 1.801 1.00 25.72 ? 20 GLY A C 1 ATOM 147 O O . GLY A 1 20 ? 43.679 31.927 2.970 1.00 32.70 ? 20 GLY A O 1 ATOM 148 N N . GLU A 1 21 ? 43.433 31.544 0.771 1.00 18.64 ? 21 GLU A N 1 ATOM 149 C CA . GLU A 1 21 ? 42.834 30.235 0.997 1.00 17.01 ? 21 GLU A CA 1 ATOM 150 C C . GLU A 1 21 ? 43.556 29.155 0.191 1.00 18.62 ? 21 GLU A C 1 ATOM 151 O O . GLU A 1 21 ? 44.136 29.422 -0.856 1.00 9.48 ? 21 GLU A O 1 ATOM 152 C CB . GLU A 1 21 ? 41.330 30.233 0.724 1.00 10.49 ? 21 GLU A CB 1 ATOM 153 C CG . GLU A 1 21 ? 40.582 30.708 1.967 1.00 46.76 ? 21 GLU A CG 1 ATOM 154 C CD . GLU A 1 21 ? 39.074 30.625 1.886 1.00 38.88 ? 21 GLU A CD 1 ATOM 155 O OE1 . GLU A 1 21 ? 38.549 29.998 0.945 1.00 20.39 ? 21 GLU A OE1 1 ATOM 156 O OE2 . GLU A 1 21 ? 38.420 31.178 2.798 1.00 35.14 ? 21 GLU A OE2 1 ATOM 157 N N . PHE A 1 22 ? 43.525 27.938 0.715 1.00 15.91 ? 22 PHE A N 1 ATOM 158 C CA . PHE A 1 22 ? 44.152 26.796 0.075 1.00 12.01 ? 22 PHE A CA 1 ATOM 159 C C . PHE A 1 22 ? 43.228 25.622 0.340 1.00 14.44 ? 22 PHE A C 1 ATOM 160 O O . PHE A 1 22 ? 42.917 25.332 1.493 1.00 17.06 ? 22 PHE A O 1 ATOM 161 C CB . PHE A 1 22 ? 45.556 26.574 0.657 1.00 10.02 ? 22 PHE A CB 1 ATOM 162 C CG . PHE A 1 22 ? 46.311 25.416 0.064 1.00 13.04 ? 22 PHE A CG 1 ATOM 163 C CD1 . PHE A 1 22 ? 45.979 24.102 0.380 1.00 16.66 ? 22 PHE A CD1 1 ATOM 164 C CD2 . PHE A 1 22 ? 47.402 25.644 -0.757 1.00 9.54 ? 22 PHE A CD2 1 ATOM 165 C CE1 . PHE A 1 22 ? 46.693 23.041 -0.151 1.00 17.82 ? 22 PHE A CE1 1 ATOM 166 C CE2 . PHE A 1 22 ? 48.123 24.591 -1.286 1.00 11.24 ? 22 PHE A CE2 1 ATOM 167 C CZ . PHE A 1 22 ? 47.771 23.287 -0.984 1.00 17.12 ? 22 PHE A CZ 1 ATOM 168 N N . MET A 1 23 ? 42.796 24.942 -0.717 1.00 9.09 ? 23 MET A N 1 ATOM 169 C CA . MET A 1 23 ? 41.905 23.800 -0.538 1.00 12.69 ? 23 MET A CA 1 ATOM 170 C C . MET A 1 23 ? 42.059 22.778 -1.650 1.00 11.67 ? 23 MET A C 1 ATOM 171 O O . MET A 1 23 ? 42.597 23.073 -2.719 1.00 9.44 ? 23 MET A O 1 ATOM 172 C CB . MET A 1 23 ? 40.444 24.260 -0.476 1.00 12.99 ? 23 MET A CB 1 ATOM 173 C CG . MET A 1 23 ? 39.944 24.970 -1.738 1.00 13.97 ? 23 MET A CG 1 ATOM 174 S SD . MET A 1 23 ? 39.230 23.847 -2.965 1.00 13.38 ? 23 MET A SD 1 ATOM 175 C CE . MET A 1 23 ? 37.691 23.370 -2.179 1.00 9.39 ? 23 MET A CE 1 ATOM 176 N N . PHE A 1 24 ? 41.563 21.577 -1.386 1.00 11.73 ? 24 PHE A N 1 ATOM 177 C CA . PHE A 1 24 ? 41.505 20.529 -2.388 1.00 12.71 ? 24 PHE A CA 1 ATOM 178 C C . PHE A 1 24 ? 40.061 20.196 -2.705 1.00 12.75 ? 24 PHE A C 1 ATOM 179 O O . PHE A 1 24 ? 39.220 20.114 -1.809 1.00 9.28 ? 24 PHE A O 1 ATOM 180 C CB . PHE A 1 24 ? 42.232 19.275 -1.916 1.00 8.88 ? 24 PHE A CB 1 ATOM 181 C CG . PHE A 1 24 ? 43.660 19.192 -2.364 1.00 15.33 ? 24 PHE A CG 1 ATOM 182 C CD1 . PHE A 1 24 ? 44.624 20.039 -1.848 1.00 14.39 ? 24 PHE A CD1 1 ATOM 183 C CD2 . PHE A 1 24 ? 44.043 18.240 -3.291 1.00 20.04 ? 24 PHE A CD2 1 ATOM 184 C CE1 . PHE A 1 24 ? 45.940 19.939 -2.257 1.00 13.36 ? 24 PHE A CE1 1 ATOM 185 C CE2 . PHE A 1 24 ? 45.353 18.138 -3.703 1.00 14.40 ? 24 PHE A CE2 1 ATOM 186 C CZ . PHE A 1 24 ? 46.303 18.990 -3.185 1.00 17.41 ? 24 PHE A CZ 1 ATOM 187 N N . ASP A 1 25 ? 39.779 20.017 -3.990 1.00 13.62 ? 25 ASP A N 1 ATOM 188 C CA . ASP A 1 25 ? 38.436 19.728 -4.455 1.00 11.43 ? 25 ASP A CA 1 ATOM 189 C C . ASP A 1 25 ? 38.447 18.402 -5.201 1.00 19.61 ? 25 ASP A C 1 ATOM 190 O O . ASP A 1 25 ? 39.353 18.135 -5.988 1.00 18.66 ? 25 ASP A O 1 ATOM 191 C CB . ASP A 1 25 ? 37.937 20.855 -5.371 1.00 11.86 ? 25 ASP A CB 1 ATOM 192 C CG . ASP A 1 25 ? 36.548 20.592 -5.934 1.00 21.36 ? 25 ASP A CG 1 ATOM 193 O OD1 . ASP A 1 25 ? 36.401 19.684 -6.779 1.00 21.33 ? 25 ASP A OD1 1 ATOM 194 O OD2 . ASP A 1 25 ? 35.606 21.318 -5.556 1.00 22.73 ? 25 ASP A OD2 1 ATOM 195 N N . PHE A 1 26 ? 37.446 17.571 -4.938 1.00 14.25 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 37.255 16.336 -5.687 1.00 14.69 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 35.861 16.380 -6.283 1.00 16.64 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 34.880 16.347 -5.542 1.00 13.15 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 37.433 15.106 -4.792 1.00 14.89 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 37.135 13.802 -5.483 1.00 16.24 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 38.120 13.140 -6.201 1.00 18.25 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 35.872 13.234 -5.410 1.00 16.79 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 37.847 11.943 -6.840 1.00 17.44 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 35.592 12.038 -6.044 1.00 19.19 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 36.584 11.390 -6.761 1.00 18.33 ? 26 PHE A CZ 1 ATOM 206 N N . ASP A 1 27 ? 35.775 16.457 -7.609 1.00 15.95 ? 27 ASP A N 1 ATOM 207 C CA . ASP A 1 27 ? 34.491 16.457 -8.316 1.00 13.05 ? 27 ASP A CA 1 ATOM 208 C C . ASP A 1 27 ? 33.492 17.479 -7.766 1.00 10.54 ? 27 ASP A C 1 ATOM 209 O O . ASP A 1 27 ? 32.286 17.244 -7.776 1.00 16.75 ? 27 ASP A O 1 ATOM 210 C CB . ASP A 1 27 ? 33.875 15.056 -8.296 1.00 14.07 ? 27 ASP A CB 1 ATOM 211 C CG . ASP A 1 27 ? 34.646 14.073 -9.159 1.00 23.78 ? 27 ASP A CG 1 ATOM 212 O OD1 . ASP A 1 27 ? 35.572 14.516 -9.874 1.00 19.12 ? 27 ASP A OD1 1 ATOM 213 O OD2 . ASP A 1 27 ? 34.332 12.863 -9.122 1.00 18.64 ? 27 ASP A OD2 1 ATOM 214 N N . GLY A 1 28 ? 33.998 18.606 -7.275 1.00 13.16 ? 28 GLY A N 1 ATOM 215 C CA . GLY A 1 28 ? 33.139 19.670 -6.782 1.00 11.21 ? 28 GLY A CA 1 ATOM 216 C C . GLY A 1 28 ? 32.909 19.671 -5.281 1.00 22.87 ? 28 GLY A C 1 ATOM 217 O O . GLY A 1 28 ? 32.265 20.584 -4.756 1.00 21.92 ? 28 GLY A O 1 ATOM 218 N N . ASP A 1 29 ? 33.444 18.673 -4.581 1.00 20.04 ? 29 ASP A N 1 ATOM 219 C CA . ASP A 1 29 ? 33.372 18.672 -3.124 1.00 18.66 ? 29 ASP A CA 1 ATOM 220 C C . ASP A 1 29 ? 34.741 18.909 -2.494 1.00 15.27 ? 29 ASP A C 1 ATOM 221 O O . ASP A 1 29 ? 35.770 18.516 -3.047 1.00 22.12 ? 29 ASP A O 1 ATOM 222 C CB . ASP A 1 29 ? 32.790 17.353 -2.616 1.00 10.66 ? 29 ASP A CB 1 ATOM 223 C CG . ASP A 1 29 ? 31.283 17.322 -2.688 1.00 22.51 ? 29 ASP A CG 1 ATOM 224 O OD1 . ASP A 1 29 ? 30.637 18.058 -1.910 1.00 24.78 ? 29 ASP A OD1 1 ATOM 225 O OD2 . ASP A 1 29 ? 30.746 16.560 -3.517 1.00 15.38 ? 29 ASP A OD2 1 ATOM 226 N N . GLU A 1 30 ? 34.747 19.553 -1.333 1.00 12.45 ? 30 GLU A N 1 ATOM 227 C CA . GLU A 1 30 ? 35.995 19.887 -0.665 1.00 11.76 ? 30 GLU A CA 1 ATOM 228 C C . GLU A 1 30 ? 36.542 18.690 0.091 1.00 13.83 ? 30 GLU A C 1 ATOM 229 O O . GLU A 1 30 ? 35.826 18.083 0.881 1.00 14.33 ? 30 GLU A O 1 ATOM 230 C CB . GLU A 1 30 ? 35.796 21.062 0.294 1.00 16.42 ? 30 GLU A CB 1 ATOM 231 C CG . GLU A 1 30 ? 37.018 21.357 1.150 1.00 18.77 ? 30 GLU A CG 1 ATOM 232 C CD . GLU A 1 30 ? 36.726 22.322 2.275 1.00 19.46 ? 30 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 30 ? 35.603 22.867 2.311 1.00 18.29 ? 30 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 30 ? 37.617 22.532 3.125 1.00 23.92 ? 30 GLU A OE2 1 ATOM 235 N N . ILE A 1 31 ? 37.788 18.316 -0.182 1.00 18.10 ? 31 ILE A N 1 ATOM 236 C CA . ILE A 1 31 ? 38.440 17.271 0.601 1.00 13.40 ? 31 ILE A CA 1 ATOM 237 C C . ILE A 1 31 ? 38.931 17.874 1.909 1.00 24.37 ? 31 ILE A C 1 ATOM 238 O O . ILE A 1 31 ? 38.637 17.382 3.001 1.00 14.12 ? 31 ILE A O 1 ATOM 239 C CB . ILE A 1 31 ? 39.622 16.640 -0.141 1.00 16.89 ? 31 ILE A CB 1 ATOM 240 C CG1 . ILE A 1 31 ? 39.186 16.123 -1.513 1.00 19.35 ? 31 ILE A CG1 1 ATOM 241 C CG2 . ILE A 1 31 ? 40.223 15.522 0.690 1.00 14.55 ? 31 ILE A CG2 1 ATOM 242 C CD1 . ILE A 1 31 ? 40.317 15.489 -2.309 1.00 14.77 ? 31 ILE A CD1 1 ATOM 243 N N . PHE A 1 32 ? 39.682 18.960 1.776 1.00 12.63 ? 32 PHE A N 1 ATOM 244 C CA . PHE A 1 32 ? 40.163 19.712 2.923 1.00 15.76 ? 32 PHE A CA 1 ATOM 245 C C . PHE A 1 32 ? 40.561 21.125 2.522 1.00 18.08 ? 32 PHE A C 1 ATOM 246 O O . PHE A 1 32 ? 40.722 21.429 1.340 1.00 15.89 ? 32 PHE A O 1 ATOM 247 C CB . PHE A 1 32 ? 41.343 18.982 3.580 1.00 14.24 ? 32 PHE A CB 1 ATOM 248 C CG . PHE A 1 32 ? 42.602 18.983 2.753 1.00 17.45 ? 32 PHE A CG 1 ATOM 249 C CD1 . PHE A 1 32 ? 43.535 20.000 2.869 1.00 18.66 ? 32 PHE A CD1 1 ATOM 250 C CD2 . PHE A 1 32 ? 42.854 17.949 1.860 1.00 13.44 ? 32 PHE A CD2 1 ATOM 251 C CE1 . PHE A 1 32 ? 44.691 19.994 2.105 1.00 23.40 ? 32 PHE A CE1 1 ATOM 252 C CE2 . PHE A 1 32 ? 44.006 17.936 1.095 1.00 13.16 ? 32 PHE A CE2 1 ATOM 253 C CZ . PHE A 1 32 ? 44.927 18.957 1.220 1.00 13.19 ? 32 PHE A CZ 1 ATOM 254 N N . HIS A 1 33 ? 40.716 21.982 3.522 1.00 16.41 ? 33 HIS A N 1 ATOM 255 C CA . HIS A 1 33 ? 41.367 23.267 3.353 1.00 13.40 ? 33 HIS A CA 1 ATOM 256 C C . HIS A 1 33 ? 42.367 23.476 4.483 1.00 21.65 ? 33 HIS A C 1 ATOM 257 O O . HIS A 1 33 ? 42.381 22.724 5.455 1.00 15.44 ? 33 HIS A O 1 ATOM 258 C CB . HIS A 1 33 ? 40.345 24.407 3.327 1.00 16.48 ? 33 HIS A CB 1 ATOM 259 C CG . HIS A 1 33 ? 39.685 24.654 4.649 1.00 19.65 ? 33 HIS A CG 1 ATOM 260 N ND1 . HIS A 1 33 ? 38.523 24.019 5.033 1.00 16.03 ? 33 HIS A ND1 1 ATOM 261 C CD2 . HIS A 1 33 ? 40.039 25.450 5.686 1.00 15.50 ? 33 HIS A CD2 1 ATOM 262 C CE1 . HIS A 1 33 ? 38.181 24.424 6.243 1.00 17.63 ? 33 HIS A CE1 1 ATOM 263 N NE2 . HIS A 1 33 ? 39.085 25.291 6.663 1.00 19.87 ? 33 HIS A NE2 1 ATOM 264 N N . VAL A 1 34 ? 43.209 24.495 4.351 1.00 19.87 ? 34 VAL A N 1 ATOM 265 C CA . VAL A 1 34 ? 44.149 24.826 5.408 1.00 19.97 ? 34 VAL A CA 1 ATOM 266 C C . VAL A 1 34 ? 43.751 26.089 6.167 1.00 24.76 ? 34 VAL A C 1 ATOM 267 O O . VAL A 1 34 ? 43.572 27.155 5.578 1.00 20.10 ? 34 VAL A O 1 ATOM 268 C CB . VAL A 1 34 ? 45.569 24.997 4.851 1.00 19.61 ? 34 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 34 ? 46.491 25.579 5.915 1.00 19.76 ? 34 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 34 ? 46.087 23.661 4.342 1.00 15.35 ? 34 VAL A CG2 1 ATOM 271 N N . ASP A 1 35 ? 43.603 25.944 7.480 1.00 27.18 ? 35 ASP A N 1 ATOM 272 C CA . ASP A 1 35 ? 43.410 27.068 8.387 1.00 28.73 ? 35 ASP A CA 1 ATOM 273 C C . ASP A 1 35 ? 44.729 27.829 8.495 1.00 29.45 ? 35 ASP A C 1 ATOM 274 O O . ASP A 1 35 ? 45.648 27.364 9.162 1.00 31.05 ? 35 ASP A O 1 ATOM 275 C CB . ASP A 1 35 ? 42.943 26.556 9.758 1.00 32.11 ? 35 ASP A CB 1 ATOM 276 C CG . ASP A 1 35 ? 42.543 27.670 10.715 1.00 37.16 ? 35 ASP A CG 1 ATOM 277 O OD1 . ASP A 1 35 ? 43.145 28.764 10.681 1.00 27.98 ? 35 ASP A OD1 1 ATOM 278 O OD2 . ASP A 1 35 ? 41.620 27.435 11.522 1.00 45.48 ? 35 ASP A OD2 1 ATOM 279 N N . MET A 1 36 ? 44.827 28.985 7.839 1.00 31.29 ? 36 MET A N 1 ATOM 280 C CA . MET A 1 36 ? 46.100 29.707 7.750 1.00 34.96 ? 36 MET A CA 1 ATOM 281 C C . MET A 1 36 ? 46.586 30.230 9.100 1.00 40.94 ? 36 MET A C 1 ATOM 282 O O . MET A 1 36 ? 47.786 30.212 9.381 1.00 42.07 ? 36 MET A O 1 ATOM 283 C CB . MET A 1 36 ? 45.993 30.880 6.770 1.00 32.18 ? 36 MET A CB 1 ATOM 284 C CG . MET A 1 36 ? 45.481 30.522 5.390 1.00 37.08 ? 36 MET A CG 1 ATOM 285 S SD . MET A 1 36 ? 46.497 29.273 4.571 1.00 36.67 ? 36 MET A SD 1 ATOM 286 C CE . MET A 1 36 ? 45.643 29.164 3.010 1.00 50.52 ? 36 MET A CE 1 ATOM 287 N N . ALA A 1 37 ? 45.659 30.701 9.927 1.00 37.99 ? 37 ALA A N 1 ATOM 288 C CA . ALA A 1 37 ? 46.016 31.246 11.232 1.00 37.86 ? 37 ALA A CA 1 ATOM 289 C C . ALA A 1 37 ? 46.525 30.165 12.184 1.00 33.01 ? 37 ALA A C 1 ATOM 290 O O . ALA A 1 37 ? 47.490 30.377 12.914 1.00 38.95 ? 37 ALA A O 1 ATOM 291 C CB . ALA A 1 37 ? 44.826 31.965 11.843 1.00 41.67 ? 37 ALA A CB 1 ATOM 292 N N . LYS A 1 38 ? 45.886 29.000 12.159 1.00 32.90 ? 38 LYS A N 1 ATOM 293 C CA . LYS A 1 38 ? 46.278 27.901 13.034 1.00 36.02 ? 38 LYS A CA 1 ATOM 294 C C . LYS A 1 38 ? 47.326 27.008 12.386 1.00 34.42 ? 38 LYS A C 1 ATOM 295 O O . LYS A 1 38 ? 47.922 26.167 13.058 1.00 32.01 ? 38 LYS A O 1 ATOM 296 C CB . LYS A 1 38 ? 45.063 27.053 13.422 1.00 37.26 ? 38 LYS A CB 1 ATOM 297 C CG . LYS A 1 38 ? 44.010 27.769 14.250 1.00 42.67 ? 38 LYS A CG 1 ATOM 298 C CD . LYS A 1 38 ? 42.981 26.778 14.776 1.00 48.83 ? 38 LYS A CD 1 ATOM 299 C CE . LYS A 1 38 ? 41.933 27.460 15.638 1.00 56.24 ? 38 LYS A CE 1 ATOM 300 N NZ . LYS A 1 38 ? 41.075 26.473 16.350 1.00 63.20 ? 38 LYS A NZ 1 ATOM 301 N N . LYS A 1 39 ? 47.547 27.201 11.085 1.00 35.08 ? 39 LYS A N 1 ATOM 302 C CA . LYS A 1 39 ? 48.473 26.363 10.326 1.00 30.73 ? 39 LYS A CA 1 ATOM 303 C C . LYS A 1 39 ? 48.069 24.903 10.482 1.00 32.24 ? 39 LYS A C 1 ATOM 304 O O . LYS A 1 39 ? 48.901 24.039 10.751 1.00 36.07 ? 39 LYS A O 1 ATOM 305 C CB . LYS A 1 39 ? 49.914 26.587 10.786 1.00 38.64 ? 39 LYS A CB 1 ATOM 306 C CG . LYS A 1 39 ? 50.365 28.029 10.629 1.00 43.64 ? 39 LYS A CG 1 ATOM 307 C CD . LYS A 1 39 ? 51.594 28.339 11.465 1.00 52.90 ? 39 LYS A CD 1 ATOM 308 C CE . LYS A 1 39 ? 52.060 29.773 11.235 1.00 57.12 ? 39 LYS A CE 1 ATOM 309 N NZ . LYS A 1 39 ? 53.305 30.106 11.988 1.00 54.53 ? 39 LYS A NZ 1 ATOM 310 N N . GLU A 1 40 ? 46.779 24.634 10.290 1.00 32.53 ? 40 GLU A N 1 ATOM 311 C CA . GLU A 1 40 ? 46.247 23.279 10.417 1.00 33.09 ? 40 GLU A CA 1 ATOM 312 C C . GLU A 1 40 ? 45.356 22.833 9.261 1.00 27.48 ? 40 GLU A C 1 ATOM 313 O O . GLU A 1 40 ? 44.633 23.629 8.659 1.00 21.20 ? 40 GLU A O 1 ATOM 314 C CB . GLU A 1 40 ? 45.440 23.161 11.712 1.00 30.29 ? 40 GLU A CB 1 ATOM 315 C CG . GLU A 1 40 ? 46.260 23.106 12.976 1.00 37.88 ? 40 GLU A CG 1 ATOM 316 C CD . GLU A 1 40 ? 45.386 23.065 14.210 1.00 52.05 ? 40 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 40 ? 44.232 22.595 14.103 1.00 56.16 ? 40 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 40 ? 45.852 23.496 15.286 1.00 57.69 ? 40 GLU A OE2 1 ATOM 319 N N . THR A 1 41 ? 45.418 21.539 8.970 1.00 23.14 ? 41 THR A N 1 ATOM 320 C CA . THR A 1 41 ? 44.610 20.926 7.933 1.00 22.24 ? 41 THR A CA 1 ATOM 321 C C . THR A 1 41 ? 43.233 20.606 8.487 1.00 26.24 ? 41 THR A C 1 ATOM 322 O O . THR A 1 41 ? 43.109 19.944 9.516 1.00 30.90 ? 41 THR A O 1 ATOM 323 C CB . THR A 1 41 ? 45.267 19.652 7.397 1.00 24.48 ? 41 THR A CB 1 ATOM 324 O OG1 . THR A 1 41 ? 46.508 19.992 6.767 1.00 28.36 ? 41 THR A OG1 1 ATOM 325 C CG2 . THR A 1 41 ? 44.357 18.958 6.389 1.00 18.80 ? 41 THR A CG2 1 ATOM 326 N N . VAL A 1 42 ? 42.199 21.085 7.806 1.00 27.69 ? 42 VAL A N 1 ATOM 327 C CA . VAL A 1 42 ? 40.821 20.858 8.231 1.00 25.43 ? 42 VAL A CA 1 ATOM 328 C C . VAL A 1 42 ? 40.111 19.978 7.219 1.00 28.40 ? 42 VAL A C 1 ATOM 329 O O . VAL A 1 42 ? 39.766 20.421 6.123 1.00 28.96 ? 42 VAL A O 1 ATOM 330 C CB . VAL A 1 42 ? 40.057 22.179 8.410 1.00 23.33 ? 42 VAL A CB 1 ATOM 331 C CG1 . VAL A 1 42 ? 38.649 21.914 8.923 1.00 20.30 ? 42 VAL A CG1 1 ATOM 332 C CG2 . VAL A 1 42 ? 40.816 23.089 9.364 1.00 21.87 ? 42 VAL A CG2 1 ATOM 333 N N . TRP A 1 43 ? 39.885 18.727 7.599 1.00 25.88 ? 43 TRP A N 1 ATOM 334 C CA . TRP A 1 43 ? 39.238 17.778 6.710 1.00 25.14 ? 43 TRP A CA 1 ATOM 335 C C . TRP A 1 43 ? 37.739 18.045 6.690 1.00 25.05 ? 43 TRP A C 1 ATOM 336 O O . TRP A 1 43 ? 37.139 18.325 7.726 1.00 23.99 ? 43 TRP A O 1 ATOM 337 C CB . TRP A 1 43 ? 39.527 16.354 7.181 1.00 25.53 ? 43 TRP A CB 1 ATOM 338 C CG . TRP A 1 43 ? 40.993 16.063 7.195 1.00 27.80 ? 43 TRP A CG 1 ATOM 339 C CD1 . TRP A 1 43 ? 41.839 16.203 8.256 1.00 23.07 ? 43 TRP A CD1 1 ATOM 340 C CD2 . TRP A 1 43 ? 41.800 15.629 6.093 1.00 24.57 ? 43 TRP A CD2 1 ATOM 341 N NE1 . TRP A 1 43 ? 43.119 15.866 7.891 1.00 19.75 ? 43 TRP A NE1 1 ATOM 342 C CE2 . TRP A 1 43 ? 43.123 15.511 6.568 1.00 26.41 ? 43 TRP A CE2 1 ATOM 343 C CE3 . TRP A 1 43 ? 41.533 15.320 4.755 1.00 19.67 ? 43 TRP A CE3 1 ATOM 344 C CZ2 . TRP A 1 43 ? 44.174 15.097 5.752 1.00 23.23 ? 43 TRP A CZ2 1 ATOM 345 C CZ3 . TRP A 1 43 ? 42.581 14.908 3.948 1.00 18.81 ? 43 TRP A CZ3 1 ATOM 346 C CH2 . TRP A 1 43 ? 43.884 14.802 4.449 1.00 22.25 ? 43 TRP A CH2 1 ATOM 347 N N . ARG A 1 44 ? 37.138 17.969 5.508 1.00 23.12 ? 44 ARG A N 1 ATOM 348 C CA . ARG A 1 44 ? 35.734 18.336 5.352 1.00 23.95 ? 44 ARG A CA 1 ATOM 349 C C . ARG A 1 44 ? 34.821 17.361 6.085 1.00 19.65 ? 44 ARG A C 1 ATOM 350 O O . ARG A 1 44 ? 33.850 17.761 6.727 1.00 18.84 ? 44 ARG A O 1 ATOM 351 C CB . ARG A 1 44 ? 35.357 18.403 3.876 1.00 14.75 ? 44 ARG A CB 1 ATOM 352 C CG . ARG A 1 44 ? 33.915 18.818 3.642 1.00 16.34 ? 44 ARG A CG 1 ATOM 353 C CD . ARG A 1 44 ? 33.636 20.190 4.221 1.00 14.89 ? 44 ARG A CD 1 ATOM 354 N NE . ARG A 1 44 ? 32.241 20.571 4.029 1.00 14.97 ? 44 ARG A NE 1 ATOM 355 C CZ . ARG A 1 44 ? 31.265 20.257 4.873 1.00 24.43 ? 44 ARG A CZ 1 ATOM 356 N NH1 . ARG A 1 44 ? 31.535 19.554 5.965 1.00 25.11 ? 44 ARG A NH1 1 ATOM 357 N NH2 . ARG A 1 44 ? 30.020 20.646 4.630 1.00 21.83 ? 44 ARG A NH2 1 ATOM 358 N N . LEU A 1 45 ? 35.157 16.080 5.979 1.00 19.54 ? 45 LEU A N 1 ATOM 359 C CA . LEU A 1 45 ? 34.559 15.038 6.799 1.00 21.97 ? 45 LEU A CA 1 ATOM 360 C C . LEU A 1 45 ? 35.661 14.485 7.688 1.00 22.95 ? 45 LEU A C 1 ATOM 361 O O . LEU A 1 45 ? 36.764 14.222 7.205 1.00 22.71 ? 45 LEU A O 1 ATOM 362 C CB . LEU A 1 45 ? 33.951 13.932 5.935 1.00 22.97 ? 45 LEU A CB 1 ATOM 363 C CG . LEU A 1 45 ? 32.831 14.308 4.959 1.00 25.45 ? 45 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 45 ? 32.184 13.056 4.385 1.00 31.18 ? 45 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 45 ? 31.788 15.197 5.616 1.00 22.81 ? 45 LEU A CD2 1 ATOM 366 N N . GLU A 1 46 ? 35.377 14.322 8.979 1.00 25.78 ? 46 GLU A N 1 ATOM 367 C CA . GLU A 1 46 ? 36.405 13.898 9.927 1.00 34.05 ? 46 GLU A CA 1 ATOM 368 C C . GLU A 1 46 ? 37.063 12.577 9.554 1.00 29.49 ? 46 GLU A C 1 ATOM 369 O O . GLU A 1 46 ? 38.250 12.386 9.804 1.00 33.02 ? 46 GLU A O 1 ATOM 370 C CB . GLU A 1 46 ? 35.811 13.784 11.330 1.00 43.26 ? 46 GLU A CB 1 ATOM 371 C CG . GLU A 1 46 ? 35.962 15.040 12.172 1.00 61.14 ? 46 GLU A CG 1 ATOM 372 C CD . GLU A 1 46 ? 37.389 15.260 12.633 1.00 71.18 ? 46 GLU A CD 1 ATOM 373 O OE1 . GLU A 1 46 ? 38.210 15.743 11.824 1.00 69.76 ? 46 GLU A OE1 1 ATOM 374 O OE2 . GLU A 1 46 ? 37.690 14.951 13.808 1.00 70.77 ? 46 GLU A OE2 1 ATOM 375 N N . GLU A 1 47 ? 36.295 11.674 8.952 1.00 24.91 ? 47 GLU A N 1 ATOM 376 C CA . GLU A 1 47 ? 36.835 10.379 8.561 1.00 35.50 ? 47 GLU A CA 1 ATOM 377 C C . GLU A 1 47 ? 38.010 10.507 7.595 1.00 36.41 ? 47 GLU A C 1 ATOM 378 O O . GLU A 1 47 ? 38.897 9.654 7.596 1.00 31.77 ? 47 GLU A O 1 ATOM 379 C CB . GLU A 1 47 ? 35.738 9.481 7.986 1.00 42.10 ? 47 GLU A CB 1 ATOM 380 C CG . GLU A 1 47 ? 35.049 10.003 6.747 1.00 46.02 ? 47 GLU A CG 1 ATOM 381 C CD . GLU A 1 47 ? 33.563 10.191 6.986 1.00 48.32 ? 47 GLU A CD 1 ATOM 382 O OE1 . GLU A 1 47 ? 33.208 10.697 8.074 1.00 47.73 ? 47 GLU A OE1 1 ATOM 383 O OE2 . GLU A 1 47 ? 32.755 9.815 6.110 1.00 45.85 ? 47 GLU A OE2 1 ATOM 384 N N . PHE A 1 48 ? 38.014 11.563 6.777 1.00 32.64 ? 48 PHE A N 1 ATOM 385 C CA . PHE A 1 48 ? 39.060 11.735 5.767 1.00 28.26 ? 48 PHE A CA 1 ATOM 386 C C . PHE A 1 48 ? 40.430 11.754 6.434 1.00 26.85 ? 48 PHE A C 1 ATOM 387 O O . PHE A 1 48 ? 41.393 11.187 5.916 1.00 22.79 ? 48 PHE A O 1 ATOM 388 C CB . PHE A 1 48 ? 38.875 13.030 4.959 1.00 23.13 ? 48 PHE A CB 1 ATOM 389 C CG . PHE A 1 48 ? 37.651 13.055 4.078 1.00 20.29 ? 48 PHE A CG 1 ATOM 390 C CD1 . PHE A 1 48 ? 36.892 11.914 3.863 1.00 28.61 ? 48 PHE A CD1 1 ATOM 391 C CD2 . PHE A 1 48 ? 37.275 14.229 3.445 1.00 16.91 ? 48 PHE A CD2 1 ATOM 392 C CE1 . PHE A 1 48 ? 35.774 11.948 3.045 1.00 21.81 ? 48 PHE A CE1 1 ATOM 393 C CE2 . PHE A 1 48 ? 36.160 14.272 2.626 1.00 22.46 ? 48 PHE A CE2 1 ATOM 394 C CZ . PHE A 1 48 ? 35.409 13.133 2.425 1.00 21.30 ? 48 PHE A CZ 1 ATOM 395 N N . GLY A 1 49 ? 40.504 12.392 7.597 1.00 26.92 ? 49 GLY A N 1 ATOM 396 C CA . GLY A 1 49 ? 41.776 12.566 8.270 1.00 23.43 ? 49 GLY A CA 1 ATOM 397 C C . GLY A 1 49 ? 42.305 11.307 8.928 1.00 26.47 ? 49 GLY A C 1 ATOM 398 O O . GLY A 1 49 ? 43.441 11.288 9.400 1.00 26.12 ? 49 GLY A O 1 ATOM 399 N N . ARG A 1 50 ? 41.487 10.260 8.978 1.00 29.56 ? 50 ARG A N 1 ATOM 400 C CA . ARG A 1 50 ? 41.933 8.974 9.514 1.00 31.15 ? 50 ARG A CA 1 ATOM 401 C C . ARG A 1 50 ? 42.666 8.176 8.437 1.00 30.44 ? 50 ARG A C 1 ATOM 402 O O . ARG A 1 50 ? 43.389 7.228 8.739 1.00 33.71 ? 50 ARG A O 1 ATOM 403 C CB . ARG A 1 50 ? 40.767 8.162 10.087 1.00 34.93 ? 50 ARG A CB 1 ATOM 404 C CG . ARG A 1 50 ? 40.085 8.825 11.278 1.00 42.34 ? 50 ARG A CG 1 ATOM 405 C CD . ARG A 1 50 ? 39.234 7.840 12.073 1.00 49.61 ? 50 ARG A CD 1 ATOM 406 N NE . ARG A 1 50 ? 38.182 7.210 11.279 1.00 57.62 ? 50 ARG A NE 1 ATOM 407 C CZ . ARG A 1 50 ? 36.915 7.614 11.261 1.00 59.06 ? 50 ARG A CZ 1 ATOM 408 N NH1 . ARG A 1 50 ? 36.537 8.648 12.002 1.00 61.54 ? 50 ARG A NH1 1 ATOM 409 N NH2 . ARG A 1 50 ? 36.025 6.981 10.511 1.00 56.05 ? 50 ARG A NH2 1 ATOM 410 N N . PHE A 1 51 ? 42.459 8.562 7.180 1.00 35.65 ? 51 PHE A N 1 ATOM 411 C CA . PHE A 1 51 ? 42.980 7.823 6.028 1.00 40.03 ? 51 PHE A CA 1 ATOM 412 C C . PHE A 1 51 ? 44.111 8.566 5.314 1.00 32.59 ? 51 PHE A C 1 ATOM 413 O O . PHE A 1 51 ? 44.898 7.960 4.587 1.00 33.91 ? 51 PHE A O 1 ATOM 414 C CB . PHE A 1 51 ? 41.858 7.507 5.031 1.00 45.39 ? 51 PHE A CB 1 ATOM 415 C CG . PHE A 1 51 ? 40.736 6.697 5.616 1.00 58.23 ? 51 PHE A CG 1 ATOM 416 C CD1 . PHE A 1 51 ? 39.521 7.284 5.925 1.00 63.64 ? 51 PHE A CD1 1 ATOM 417 C CD2 . PHE A 1 51 ? 40.901 5.343 5.859 1.00 58.90 ? 51 PHE A CD2 1 ATOM 418 C CE1 . PHE A 1 51 ? 38.491 6.537 6.467 1.00 64.13 ? 51 PHE A CE1 1 ATOM 419 C CE2 . PHE A 1 51 ? 39.877 4.592 6.399 1.00 62.62 ? 51 PHE A CE2 1 ATOM 420 C CZ . PHE A 1 51 ? 38.669 5.190 6.704 1.00 63.60 ? 51 PHE A CZ 1 ATOM 421 N N . ALA A 1 52 ? 44.178 9.879 5.507 1.00 26.27 ? 52 ALA A N 1 ATOM 422 C CA . ALA A 1 52 ? 45.167 10.693 4.810 1.00 27.46 ? 52 ALA A CA 1 ATOM 423 C C . ALA A 1 52 ? 45.729 11.792 5.702 1.00 25.09 ? 52 ALA A C 1 ATOM 424 O O . ALA A 1 52 ? 45.160 12.119 6.743 1.00 29.17 ? 52 ALA A O 1 ATOM 425 C CB . ALA A 1 52 ? 44.558 11.301 3.549 1.00 24.99 ? 52 ALA A CB 1 ATOM 426 N N . SER A 1 53 ? 46.852 12.363 5.282 1.00 23.01 ? 53 SER A N 1 ATOM 427 C CA . SER A 1 53 ? 47.453 13.477 6.003 1.00 22.12 ? 53 SER A CA 1 ATOM 428 C C . SER A 1 53 ? 47.869 14.552 5.009 1.00 24.69 ? 53 SER A C 1 ATOM 429 O O . SER A 1 53 ? 47.975 14.299 3.808 1.00 21.77 ? 53 SER A O 1 ATOM 430 C CB . SER A 1 53 ? 48.656 13.022 6.826 1.00 23.67 ? 53 SER A CB 1 ATOM 431 O OG . SER A 1 53 ? 49.682 12.531 5.984 1.00 35.59 ? 53 SER A OG 1 ATOM 432 N N . PHE A 1 54 ? 48.094 15.757 5.515 1.00 29.55 ? 54 PHE A N 1 ATOM 433 C CA . PHE A 1 54 ? 48.640 16.822 4.695 1.00 28.36 ? 54 PHE A CA 1 ATOM 434 C C . PHE A 1 54 ? 49.494 17.784 5.501 1.00 33.67 ? 54 PHE A C 1 ATOM 435 O O . PHE A 1 54 ? 49.073 18.264 6.553 1.00 34.36 ? 54 PHE A O 1 ATOM 436 C CB . PHE A 1 54 ? 47.511 17.587 4.015 1.00 26.27 ? 54 PHE A CB 1 ATOM 437 C CG . PHE A 1 54 ? 47.981 18.713 3.151 1.00 18.38 ? 54 PHE A CG 1 ATOM 438 C CD1 . PHE A 1 54 ? 48.532 18.455 1.907 1.00 18.14 ? 54 PHE A CD1 1 ATOM 439 C CD2 . PHE A 1 54 ? 47.880 20.025 3.578 1.00 16.53 ? 54 PHE A CD2 1 ATOM 440 C CE1 . PHE A 1 54 ? 48.966 19.485 1.101 1.00 15.42 ? 54 PHE A CE1 1 ATOM 441 C CE2 . PHE A 1 54 ? 48.316 21.065 2.776 1.00 17.64 ? 54 PHE A CE2 1 ATOM 442 C CZ . PHE A 1 54 ? 48.860 20.794 1.536 1.00 14.53 ? 54 PHE A CZ 1 ATOM 443 N N . GLU A 1 55 ? 50.706 18.039 5.023 1.00 37.04 ? 55 GLU A N 1 ATOM 444 C CA . GLU A 1 55 ? 51.587 18.986 5.689 1.00 33.77 ? 55 GLU A CA 1 ATOM 445 C C . GLU A 1 55 ? 51.122 20.407 5.380 1.00 25.95 ? 55 GLU A C 1 ATOM 446 O O . GLU A 1 55 ? 51.381 20.937 4.296 1.00 25.02 ? 55 GLU A O 1 ATOM 447 C CB . GLU A 1 55 ? 53.041 18.787 5.258 1.00 33.83 ? 55 GLU A CB 1 ATOM 448 C CG . GLU A 1 55 ? 53.990 19.820 5.841 1.00 41.84 ? 55 GLU A CG 1 ATOM 449 C CD . GLU A 1 55 ? 53.878 19.923 7.353 1.00 45.02 ? 55 GLU A CD 1 ATOM 450 O OE1 . GLU A 1 55 ? 54.196 18.935 8.049 1.00 38.87 ? 55 GLU A OE1 1 ATOM 451 O OE2 . GLU A 1 55 ? 53.459 20.991 7.846 1.00 48.65 ? 55 GLU A OE2 1 ATOM 452 N N . ALA A 1 56 ? 50.430 21.011 6.341 1.00 18.99 ? 56 ALA A N 1 ATOM 453 C CA . ALA A 1 56 ? 49.810 22.322 6.169 1.00 17.98 ? 56 ALA A CA 1 ATOM 454 C C . ALA A 1 56 ? 50.823 23.397 5.786 1.00 23.58 ? 56 ALA A C 1 ATOM 455 O O . ALA A 1 56 ? 50.476 24.387 5.140 1.00 19.47 ? 56 ALA A O 1 ATOM 456 C CB . ALA A 1 56 ? 49.074 22.726 7.436 1.00 19.95 ? 56 ALA A CB 1 ATOM 457 N N . GLN A 1 57 ? 52.071 23.210 6.201 1.00 27.79 ? 57 GLN A N 1 ATOM 458 C CA . GLN A 1 57 ? 53.113 24.196 5.947 1.00 30.25 ? 57 GLN A CA 1 ATOM 459 C C . GLN A 1 57 ? 53.291 24.463 4.462 1.00 23.56 ? 57 GLN A C 1 ATOM 460 O O . GLN A 1 57 ? 53.605 25.583 4.063 1.00 24.66 ? 57 GLN A O 1 ATOM 461 C CB . GLN A 1 57 ? 54.447 23.739 6.540 1.00 40.44 ? 57 GLN A CB 1 ATOM 462 C CG . GLN A 1 57 ? 55.490 24.841 6.621 1.00 47.62 ? 57 GLN A CG 1 ATOM 463 C CD . GLN A 1 57 ? 55.043 26.001 7.487 1.00 54.16 ? 57 GLN A CD 1 ATOM 464 O OE1 . GLN A 1 57 ? 54.555 25.806 8.601 1.00 52.63 ? 57 GLN A OE1 1 ATOM 465 N NE2 . GLN A 1 57 ? 55.201 27.217 6.976 1.00 53.72 ? 57 GLN A NE2 1 ATOM 466 N N . GLY A 1 58 ? 53.110 23.431 3.643 1.00 22.40 ? 58 GLY A N 1 ATOM 467 C CA . GLY A 1 58 ? 53.261 23.609 2.214 1.00 22.07 ? 58 GLY A CA 1 ATOM 468 C C . GLY A 1 58 ? 52.248 24.595 1.666 1.00 26.36 ? 58 GLY A C 1 ATOM 469 O O . GLY A 1 58 ? 52.538 25.312 0.709 1.00 30.67 ? 58 GLY A O 1 ATOM 470 N N . ALA A 1 59 ? 51.057 24.634 2.261 1.00 21.44 ? 59 ALA A N 1 ATOM 471 C CA . ALA A 1 59 ? 50.044 25.585 1.816 1.00 24.04 ? 59 ALA A CA 1 ATOM 472 C C . ALA A 1 59 ? 50.491 27.019 2.085 1.00 23.92 ? 59 ALA A C 1 ATOM 473 O O . ALA A 1 59 ? 50.260 27.922 1.280 1.00 19.91 ? 59 ALA A O 1 ATOM 474 C CB . ALA A 1 59 ? 48.727 25.310 2.505 1.00 20.73 ? 59 ALA A CB 1 ATOM 475 N N . LEU A 1 60 ? 51.135 27.213 3.231 1.00 24.49 ? 60 LEU A N 1 ATOM 476 C CA . LEU A 1 60 ? 51.613 28.528 3.636 1.00 27.74 ? 60 LEU A CA 1 ATOM 477 C C . LEU A 1 60 ? 52.629 29.076 2.645 1.00 25.63 ? 60 LEU A C 1 ATOM 478 O O . LEU A 1 60 ? 52.626 30.264 2.330 1.00 25.82 ? 60 LEU A O 1 ATOM 479 C CB . LEU A 1 60 ? 52.193 28.483 5.050 1.00 29.40 ? 60 LEU A CB 1 ATOM 480 C CG . LEU A 1 60 ? 51.155 28.651 6.168 1.00 35.33 ? 60 LEU A CG 1 ATOM 481 C CD1 . LEU A 1 60 ? 50.196 27.472 6.271 1.00 36.09 ? 60 LEU A CD1 1 ATOM 482 C CD2 . LEU A 1 60 ? 51.847 28.897 7.501 1.00 39.20 ? 60 LEU A CD2 1 ATOM 483 N N . ALA A 1 61 ? 53.503 28.196 2.165 1.00 24.59 ? 61 ALA A N 1 ATOM 484 C CA . ALA A 1 61 ? 54.531 28.586 1.211 1.00 24.33 ? 61 ALA A CA 1 ATOM 485 C C . ALA A 1 61 ? 53.900 29.032 -0.100 1.00 21.92 ? 61 ALA A C 1 ATOM 486 O O . ALA A 1 61 ? 54.310 30.032 -0.687 1.00 22.43 ? 61 ALA A O 1 ATOM 487 C CB . ALA A 1 61 ? 55.501 27.434 0.969 1.00 23.56 ? 61 ALA A CB 1 ATOM 488 N N . ASN A 1 62 ? 52.896 28.288 -0.555 1.00 16.71 ? 62 ASN A N 1 ATOM 489 C CA . ASN A 1 62 ? 52.191 28.639 -1.783 1.00 17.90 ? 62 ASN A CA 1 ATOM 490 C C . ASN A 1 62 ? 51.473 29.982 -1.682 1.00 20.25 ? 62 ASN A C 1 ATOM 491 O O . ASN A 1 62 ? 51.491 30.775 -2.624 1.00 16.35 ? 62 ASN A O 1 ATOM 492 C CB . ASN A 1 62 ? 51.200 27.540 -2.170 1.00 19.17 ? 62 ASN A CB 1 ATOM 493 C CG . ASN A 1 62 ? 51.836 26.471 -3.042 1.00 23.75 ? 62 ASN A CG 1 ATOM 494 O OD1 . ASN A 1 62 ? 53.059 26.324 -3.066 1.00 29.50 ? 62 ASN A OD1 1 ATOM 495 N ND2 . ASN A 1 62 ? 51.011 25.747 -3.791 1.00 13.80 ? 62 ASN A ND2 1 ATOM 496 N N . ILE A 1 63 ? 50.820 30.222 -0.550 1.00 14.86 ? 63 ILE A N 1 ATOM 497 C CA . ILE A 1 63 ? 50.089 31.466 -0.356 1.00 12.16 ? 63 ILE A CA 1 ATOM 498 C C . ILE A 1 63 ? 51.047 32.652 -0.353 1.00 14.53 ? 63 ILE A C 1 ATOM 499 O O . ILE A 1 63 ? 50.723 33.716 -0.880 1.00 15.84 ? 63 ILE A O 1 ATOM 500 C CB . ILE A 1 63 ? 49.271 31.439 0.951 1.00 24.83 ? 63 ILE A CB 1 ATOM 501 C CG1 . ILE A 1 63 ? 48.150 30.408 0.830 1.00 25.77 ? 63 ILE A CG1 1 ATOM 502 C CG2 . ILE A 1 63 ? 48.696 32.821 1.282 1.00 16.57 ? 63 ILE A CG2 1 ATOM 503 C CD1 . ILE A 1 63 ? 47.269 30.606 -0.385 1.00 22.43 ? 63 ILE A CD1 1 ATOM 504 N N . ALA A 1 64 ? 52.239 32.455 0.205 1.00 13.24 ? 64 ALA A N 1 ATOM 505 C CA . ALA A 1 64 ? 53.254 33.502 0.195 1.00 17.81 ? 64 ALA A CA 1 ATOM 506 C C . ALA A 1 64 ? 53.663 33.814 -1.241 1.00 18.70 ? 64 ALA A C 1 ATOM 507 O O . ALA A 1 64 ? 53.861 34.975 -1.603 1.00 17.49 ? 64 ALA A O 1 ATOM 508 C CB . ALA A 1 64 ? 54.468 33.094 1.032 1.00 15.14 ? 64 ALA A CB 1 ATOM 509 N N . VAL A 1 65 ? 53.789 32.773 -2.058 1.00 15.08 ? 65 VAL A N 1 ATOM 510 C CA . VAL A 1 65 ? 54.092 32.962 -3.471 1.00 18.99 ? 65 VAL A CA 1 ATOM 511 C C . VAL A 1 65 ? 52.927 33.672 -4.171 1.00 12.26 ? 65 VAL A C 1 ATOM 512 O O . VAL A 1 65 ? 53.140 34.575 -4.980 1.00 14.01 ? 65 VAL A O 1 ATOM 513 C CB . VAL A 1 65 ? 54.397 31.620 -4.164 1.00 21.45 ? 65 VAL A CB 1 ATOM 514 C CG1 . VAL A 1 65 ? 54.465 31.794 -5.671 1.00 21.24 ? 65 VAL A CG1 1 ATOM 515 C CG2 . VAL A 1 65 ? 55.701 31.041 -3.630 1.00 20.97 ? 65 VAL A CG2 1 ATOM 516 N N . ASP A 1 66 ? 51.699 33.279 -3.836 1.00 12.00 ? 66 ASP A N 1 ATOM 517 C CA . ASP A 1 66 ? 50.513 33.888 -4.435 1.00 13.15 ? 66 ASP A CA 1 ATOM 518 C C . ASP A 1 66 ? 50.441 35.367 -4.077 1.00 14.95 ? 66 ASP A C 1 ATOM 519 O O . ASP A 1 66 ? 50.039 36.189 -4.898 1.00 13.91 ? 66 ASP A O 1 ATOM 520 C CB . ASP A 1 66 ? 49.232 33.176 -3.999 1.00 10.84 ? 66 ASP A CB 1 ATOM 521 C CG . ASP A 1 66 ? 49.174 31.740 -4.458 1.00 16.65 ? 66 ASP A CG 1 ATOM 522 O OD1 . ASP A 1 66 ? 49.857 31.399 -5.447 1.00 16.83 ? 66 ASP A OD1 1 ATOM 523 O OD2 . ASP A 1 66 ? 48.427 30.958 -3.836 1.00 17.06 ? 66 ASP A OD2 1 ATOM 524 N N . LYS A 1 67 ? 50.835 35.697 -2.851 1.00 16.41 ? 67 LYS A N 1 ATOM 525 C CA . LYS A 1 67 ? 50.874 37.085 -2.403 1.00 12.42 ? 67 LYS A CA 1 ATOM 526 C C . LYS A 1 67 ? 51.873 37.906 -3.215 1.00 14.74 ? 67 LYS A C 1 ATOM 527 O O . LYS A 1 67 ? 51.551 38.988 -3.708 1.00 14.66 ? 67 LYS A O 1 ATOM 528 C CB . LYS A 1 67 ? 51.250 37.123 -0.916 1.00 15.22 ? 67 LYS A CB 1 ATOM 529 C CG . LYS A 1 67 ? 51.501 38.505 -0.296 1.00 19.42 ? 67 LYS A CG 1 ATOM 530 C CD . LYS A 1 67 ? 51.830 38.340 1.199 1.00 15.57 ? 67 LYS A CD 1 ATOM 531 C CE . LYS A 1 67 ? 51.974 39.661 1.958 1.00 33.25 ? 67 LYS A CE 1 ATOM 532 N NZ . LYS A 1 67 ? 51.011 40.718 1.579 1.00 35.29 ? 67 LYS A NZ 1 ATOM 533 N N . ALA A 1 68 ? 53.072 37.368 -3.396 1.00 15.19 ? 68 ALA A N 1 ATOM 534 C CA . ALA A 1 68 ? 54.087 38.054 -4.182 1.00 21.46 ? 68 ALA A CA 1 ATOM 535 C C . ALA A 1 68 ? 53.679 38.180 -5.642 1.00 24.30 ? 68 ALA A C 1 ATOM 536 O O . ALA A 1 68 ? 53.914 39.207 -6.277 1.00 24.39 ? 68 ALA A O 1 ATOM 537 C CB . ALA A 1 68 ? 55.422 37.331 -4.074 1.00 17.16 ? 68 ALA A CB 1 ATOM 538 N N . ASN A 1 69 ? 53.067 37.132 -6.178 1.00 20.33 ? 69 ASN A N 1 ATOM 539 C CA . ASN A 1 69 ? 52.593 37.180 -7.554 1.00 19.59 ? 69 ASN A CA 1 ATOM 540 C C . ASN A 1 69 ? 51.466 38.185 -7.781 1.00 11.62 ? 69 ASN A C 1 ATOM 541 O O . ASN A 1 69 ? 51.434 38.865 -8.804 1.00 15.11 ? 69 ASN A O 1 ATOM 542 C CB . ASN A 1 69 ? 52.122 35.786 -7.988 1.00 11.59 ? 69 ASN A CB 1 ATOM 543 C CG . ASN A 1 69 ? 53.282 34.842 -8.267 1.00 20.32 ? 69 ASN A CG 1 ATOM 544 O OD1 . ASN A 1 69 ? 54.441 35.256 -8.266 1.00 20.55 ? 69 ASN A OD1 1 ATOM 545 N ND2 . ASN A 1 69 ? 52.975 33.574 -8.522 1.00 12.23 ? 69 ASN A ND2 1 ATOM 546 N N . LEU A 1 70 ? 50.558 38.300 -6.817 1.00 11.38 ? 70 LEU A N 1 ATOM 547 C CA . LEU A 1 70 ? 49.477 39.272 -6.935 1.00 16.23 ? 70 LEU A CA 1 ATOM 548 C C . LEU A 1 70 ? 49.979 40.706 -7.045 1.00 20.37 ? 70 LEU A C 1 ATOM 549 O O . LEU A 1 70 ? 49.462 41.486 -7.842 1.00 18.09 ? 70 LEU A O 1 ATOM 550 C CB . LEU A 1 70 ? 48.519 39.153 -5.748 1.00 13.52 ? 70 LEU A CB 1 ATOM 551 C CG . LEU A 1 70 ? 47.356 40.154 -5.728 1.00 17.51 ? 70 LEU A CG 1 ATOM 552 C CD1 . LEU A 1 70 ? 46.532 40.045 -7.001 1.00 12.83 ? 70 LEU A CD1 1 ATOM 553 C CD2 . LEU A 1 70 ? 46.475 39.957 -4.489 1.00 19.36 ? 70 LEU A CD2 1 ATOM 554 N N . GLU A 1 71 ? 50.986 41.041 -6.245 1.00 13.15 ? 71 GLU A N 1 ATOM 555 C CA . GLU A 1 71 ? 51.605 42.364 -6.293 1.00 13.86 ? 71 GLU A CA 1 ATOM 556 C C . GLU A 1 71 ? 52.130 42.663 -7.688 1.00 22.15 ? 71 GLU A C 1 ATOM 557 O O . GLU A 1 71 ? 51.901 43.743 -8.241 1.00 14.39 ? 71 GLU A O 1 ATOM 558 C CB . GLU A 1 71 ? 52.731 42.470 -5.264 1.00 14.96 ? 71 GLU A CB 1 ATOM 559 C CG . GLU A 1 71 ? 53.695 43.614 -5.522 1.00 53.33 ? 71 GLU A CG 1 ATOM 560 C CD . GLU A 1 71 ? 54.863 43.617 -4.555 1.00 67.02 ? 71 GLU A CD 1 ATOM 561 O OE1 . GLU A 1 71 ? 55.886 44.268 -4.860 1.00 72.93 ? 71 GLU A OE1 1 ATOM 562 O OE2 . GLU A 1 71 ? 54.757 42.970 -3.491 1.00 67.25 ? 71 GLU A OE2 1 ATOM 563 N N . ILE A 1 72 ? 52.841 41.691 -8.248 1.00 13.70 ? 72 ILE A N 1 ATOM 564 C CA . ILE A 1 72 ? 53.412 41.815 -9.580 1.00 14.01 ? 72 ILE A CA 1 ATOM 565 C C . ILE A 1 72 ? 52.308 42.014 -10.634 1.00 25.55 ? 72 ILE A C 1 ATOM 566 O O . ILE A 1 72 ? 52.415 42.901 -11.483 1.00 17.96 ? 72 ILE A O 1 ATOM 567 C CB . ILE A 1 72 ? 54.275 40.594 -9.929 1.00 21.89 ? 72 ILE A CB 1 ATOM 568 C CG1 . ILE A 1 72 ? 55.562 40.608 -9.095 1.00 22.74 ? 72 ILE A CG1 1 ATOM 569 C CG2 . ILE A 1 72 ? 54.550 40.553 -11.427 1.00 21.91 ? 72 ILE A CG2 1 ATOM 570 C CD1 . ILE A 1 72 ? 56.384 39.338 -9.198 1.00 27.96 ? 72 ILE A CD1 1 ATOM 571 N N A MET A 1 73 ? 51.267 41.189 -10.572 0.42 20.77 ? 73 MET A N 1 ATOM 572 N N B MET A 1 73 ? 51.266 41.182 -10.580 0.58 12.43 ? 73 MET A N 1 ATOM 573 C CA A MET A 1 73 ? 50.208 41.214 -11.577 0.42 17.19 ? 73 MET A CA 1 ATOM 574 C CA B MET A 1 73 ? 50.187 41.215 -11.572 0.58 17.00 ? 73 MET A CA 1 ATOM 575 C C A MET A 1 73 ? 49.296 42.435 -11.432 0.42 17.47 ? 73 MET A C 1 ATOM 576 C C B MET A 1 73 ? 49.319 42.456 -11.436 0.58 17.53 ? 73 MET A C 1 ATOM 577 O O A MET A 1 73 ? 48.749 42.931 -12.420 0.42 18.24 ? 73 MET A O 1 ATOM 578 O O B MET A 1 73 ? 48.817 42.984 -12.432 0.58 18.37 ? 73 MET A O 1 ATOM 579 C CB A MET A 1 73 ? 49.379 39.932 -11.510 0.42 15.97 ? 73 MET A CB 1 ATOM 580 C CB B MET A 1 73 ? 49.289 39.975 -11.462 0.58 15.91 ? 73 MET A CB 1 ATOM 581 C CG A MET A 1 73 ? 48.408 39.758 -12.667 0.42 17.36 ? 73 MET A CG 1 ATOM 582 C CG B MET A 1 73 ? 49.977 38.644 -11.673 0.58 15.10 ? 73 MET A CG 1 ATOM 583 S SD A MET A 1 73 ? 49.226 39.666 -14.268 0.42 17.18 ? 73 MET A SD 1 ATOM 584 S SD B MET A 1 73 ? 50.912 38.631 -13.213 0.58 28.46 ? 73 MET A SD 1 ATOM 585 C CE A MET A 1 73 ? 50.361 38.321 -13.955 0.42 27.40 ? 73 MET A CE 1 ATOM 586 C CE B MET A 1 73 ? 49.622 39.057 -14.390 0.58 24.72 ? 73 MET A CE 1 ATOM 587 N N . THR A 1 74 ? 49.129 42.908 -10.202 1.00 12.45 ? 74 THR A N 1 ATOM 588 C CA . THR A 1 74 ? 48.389 44.136 -9.954 1.00 13.04 ? 74 THR A CA 1 ATOM 589 C C . THR A 1 74 ? 49.080 45.286 -10.674 1.00 21.43 ? 74 THR A C 1 ATOM 590 O O . THR A 1 74 ? 48.444 46.084 -11.361 1.00 17.55 ? 74 THR A O 1 ATOM 591 C CB . THR A 1 74 ? 48.289 44.456 -8.451 1.00 15.77 ? 74 THR A CB 1 ATOM 592 O OG1 . THR A 1 74 ? 47.590 43.399 -7.779 1.00 14.97 ? 74 THR A OG1 1 ATOM 593 C CG2 . THR A 1 74 ? 47.545 45.769 -8.227 1.00 15.04 ? 74 THR A CG2 1 ATOM 594 N N . LYS A 1 75 ? 50.396 45.346 -10.518 1.00 22.24 ? 75 LYS A N 1 ATOM 595 C CA . LYS A 1 75 ? 51.228 46.336 -11.192 1.00 26.77 ? 75 LYS A CA 1 ATOM 596 C C . LYS A 1 75 ? 51.191 46.209 -12.718 1.00 21.09 ? 75 LYS A C 1 ATOM 597 O O . LYS A 1 75 ? 51.037 47.200 -13.432 1.00 22.01 ? 75 LYS A O 1 ATOM 598 C CB . LYS A 1 75 ? 52.665 46.186 -10.687 1.00 33.92 ? 75 LYS A CB 1 ATOM 599 C CG . LYS A 1 75 ? 53.563 47.385 -10.872 1.00 45.25 ? 75 LYS A CG 1 ATOM 600 C CD . LYS A 1 75 ? 54.899 47.137 -10.182 1.00 50.24 ? 75 LYS A CD 1 ATOM 601 C CE . LYS A 1 75 ? 54.692 46.722 -8.725 1.00 58.65 ? 75 LYS A CE 1 ATOM 602 N NZ . LYS A 1 75 ? 55.975 46.513 -7.991 1.00 61.60 ? 75 LYS A NZ 1 ATOM 603 N N . ARG A 1 76 ? 51.327 44.979 -13.208 1.00 19.32 ? 76 ARG A N 1 ATOM 604 C CA . ARG A 1 76 ? 51.300 44.700 -14.643 1.00 21.84 ? 76 ARG A CA 1 ATOM 605 C C . ARG A 1 76 ? 49.996 45.159 -15.296 1.00 15.96 ? 76 ARG A C 1 ATOM 606 O O . ARG A 1 76 ? 49.992 45.629 -16.431 1.00 16.56 ? 76 ARG A O 1 ATOM 607 C CB . ARG A 1 76 ? 51.549 43.210 -14.903 1.00 14.06 ? 76 ARG A CB 1 ATOM 608 C CG . ARG A 1 76 ? 52.407 42.952 -16.144 1.00 25.98 ? 76 ARG A CG 1 ATOM 609 C CD . ARG A 1 76 ? 52.474 41.474 -16.532 1.00 17.77 ? 76 ARG A CD 1 ATOM 610 N NE . ARG A 1 76 ? 53.387 40.725 -15.671 1.00 18.64 ? 76 ARG A NE 1 ATOM 611 C CZ . ARG A 1 76 ? 53.402 39.400 -15.568 1.00 18.02 ? 76 ARG A CZ 1 ATOM 612 N NH1 . ARG A 1 76 ? 52.558 38.669 -16.283 1.00 16.43 ? 76 ARG A NH1 1 ATOM 613 N NH2 . ARG A 1 76 ? 54.265 38.805 -14.756 1.00 19.74 ? 76 ARG A NH2 1 ATOM 614 N N . SER A 1 77 ? 48.897 45.026 -14.562 1.00 11.14 ? 77 SER A N 1 ATOM 615 C CA . SER A 1 77 ? 47.574 45.373 -15.068 1.00 10.77 ? 77 SER A CA 1 ATOM 616 C C . SER A 1 77 ? 47.275 46.870 -14.958 1.00 17.77 ? 77 SER A C 1 ATOM 617 O O . SER A 1 77 ? 46.163 47.306 -15.265 1.00 17.42 ? 77 SER A O 1 ATOM 618 C CB . SER A 1 77 ? 46.501 44.583 -14.311 1.00 10.58 ? 77 SER A CB 1 ATOM 619 O OG . SER A 1 77 ? 46.288 45.135 -13.020 1.00 19.91 ? 77 SER A OG 1 ATOM 620 N N . ASN A 1 78 ? 48.266 47.645 -14.516 1.00 14.06 ? 78 ASN A N 1 ATOM 621 C CA . ASN A 1 78 ? 48.069 49.066 -14.214 1.00 13.78 ? 78 ASN A CA 1 ATOM 622 C C . ASN A 1 78 ? 46.988 49.262 -13.149 1.00 17.19 ? 78 ASN A C 1 ATOM 623 O O . ASN A 1 78 ? 46.124 50.135 -13.263 1.00 20.61 ? 78 ASN A O 1 ATOM 624 C CB . ASN A 1 78 ? 47.768 49.882 -15.491 1.00 20.99 ? 78 ASN A CB 1 ATOM 625 C CG . ASN A 1 78 ? 48.853 49.723 -16.558 1.00 29.90 ? 78 ASN A CG 1 ATOM 626 O OD1 . ASN A 1 78 ? 50.042 49.774 -16.244 1.00 30.03 ? 78 ASN A OD1 1 ATOM 627 N ND2 . ASN A 1 78 ? 48.445 49.560 -17.822 1.00 43.52 ? 78 ASN A ND2 1 ATOM 628 N N . TYR A 1 79 ? 47.045 48.404 -12.130 1.00 12.52 ? 79 TYR A N 1 ATOM 629 C CA . TYR A 1 79 ? 46.137 48.451 -10.982 1.00 12.74 ? 79 TYR A CA 1 ATOM 630 C C . TYR A 1 79 ? 44.660 48.346 -11.359 1.00 18.11 ? 79 TYR A C 1 ATOM 631 O O . TYR A 1 79 ? 43.817 49.067 -10.828 1.00 22.32 ? 79 TYR A O 1 ATOM 632 C CB . TYR A 1 79 ? 46.405 49.717 -10.165 1.00 11.50 ? 79 TYR A CB 1 ATOM 633 C CG . TYR A 1 79 ? 47.802 49.719 -9.585 1.00 12.01 ? 79 TYR A CG 1 ATOM 634 C CD1 . TYR A 1 79 ? 48.887 50.121 -10.353 1.00 17.27 ? 79 TYR A CD1 1 ATOM 635 C CD2 . TYR A 1 79 ? 48.042 49.282 -8.290 1.00 12.30 ? 79 TYR A CD2 1 ATOM 636 C CE1 . TYR A 1 79 ? 50.167 50.106 -9.844 1.00 16.89 ? 79 TYR A CE1 1 ATOM 637 C CE2 . TYR A 1 79 ? 49.325 49.264 -7.768 1.00 17.38 ? 79 TYR A CE2 1 ATOM 638 C CZ . TYR A 1 79 ? 50.383 49.679 -8.553 1.00 18.33 ? 79 TYR A CZ 1 ATOM 639 O OH . TYR A 1 79 ? 51.663 49.665 -8.051 1.00 20.68 ? 79 TYR A OH 1 ATOM 640 N N . THR A 1 80 ? 44.362 47.435 -12.278 1.00 10.98 ? 80 THR A N 1 ATOM 641 C CA . THR A 1 80 ? 42.984 47.162 -12.659 1.00 12.51 ? 80 THR A CA 1 ATOM 642 C C . THR A 1 80 ? 42.341 46.266 -11.608 1.00 12.89 ? 80 THR A C 1 ATOM 643 O O . THR A 1 80 ? 42.773 45.133 -11.395 1.00 17.29 ? 80 THR A O 1 ATOM 644 C CB . THR A 1 80 ? 42.920 46.475 -14.039 1.00 16.72 ? 80 THR A CB 1 ATOM 645 O OG1 . THR A 1 80 ? 43.563 47.303 -15.016 1.00 15.31 ? 80 THR A OG1 1 ATOM 646 C CG2 . THR A 1 80 ? 41.479 46.190 -14.452 1.00 10.35 ? 80 THR A CG2 1 ATOM 647 N N . PRO A 1 81 ? 41.295 46.771 -10.945 1.00 15.92 ? 81 PRO A N 1 ATOM 648 C CA . PRO A 1 81 ? 40.667 46.014 -9.857 1.00 18.19 ? 81 PRO A CA 1 ATOM 649 C C . PRO A 1 81 ? 39.622 45.015 -10.329 1.00 15.47 ? 81 PRO A C 1 ATOM 650 O O . PRO A 1 81 ? 39.206 45.041 -11.482 1.00 15.48 ? 81 PRO A O 1 ATOM 651 C CB . PRO A 1 81 ? 40.007 47.107 -9.022 1.00 17.18 ? 81 PRO A CB 1 ATOM 652 C CG . PRO A 1 81 ? 39.665 48.163 -10.021 1.00 17.75 ? 81 PRO A CG 1 ATOM 653 C CD . PRO A 1 81 ? 40.730 48.125 -11.082 1.00 11.10 ? 81 PRO A CD 1 ATOM 654 N N . ILE A 1 82 ? 39.209 44.138 -9.424 1.00 14.52 ? 82 ILE A N 1 ATOM 655 C CA . ILE A 1 82 ? 38.172 43.166 -9.723 1.00 14.23 ? 82 ILE A CA 1 ATOM 656 C C . ILE A 1 82 ? 36.815 43.860 -9.854 1.00 16.38 ? 82 ILE A C 1 ATOM 657 O O . ILE A 1 82 ? 36.547 44.863 -9.192 1.00 13.84 ? 82 ILE A O 1 ATOM 658 C CB . ILE A 1 82 ? 38.106 42.060 -8.637 1.00 16.06 ? 82 ILE A CB 1 ATOM 659 C CG1 . ILE A 1 82 ? 37.392 40.812 -9.170 1.00 14.97 ? 82 ILE A CG1 1 ATOM 660 C CG2 . ILE A 1 82 ? 37.435 42.571 -7.361 1.00 18.60 ? 82 ILE A CG2 1 ATOM 661 C CD1 . ILE A 1 82 ? 37.601 39.569 -8.307 1.00 7.11 ? 82 ILE A CD1 1 ATOM 662 N N . THR A 1 83 ? 35.974 43.340 -10.737 1.00 10.13 ? 83 THR A N 1 ATOM 663 C CA . THR A 1 83 ? 34.600 43.798 -10.843 1.00 10.82 ? 83 THR A CA 1 ATOM 664 C C . THR A 1 83 ? 33.767 42.908 -9.926 1.00 10.41 ? 83 THR A C 1 ATOM 665 O O . THR A 1 83 ? 33.844 41.684 -10.017 1.00 14.97 ? 83 THR A O 1 ATOM 666 C CB . THR A 1 83 ? 34.081 43.744 -12.291 1.00 18.31 ? 83 THR A CB 1 ATOM 667 O OG1 . THR A 1 83 ? 34.851 44.641 -13.098 1.00 21.77 ? 83 THR A OG1 1 ATOM 668 C CG2 . THR A 1 83 ? 32.611 44.146 -12.352 1.00 17.07 ? 83 THR A CG2 1 ATOM 669 N N . ASN A 1 84 ? 32.979 43.517 -9.044 1.00 12.17 ? 84 ASN A N 1 ATOM 670 C CA . ASN A 1 84 ? 32.133 42.759 -8.131 1.00 11.42 ? 84 ASN A CA 1 ATOM 671 C C . ASN A 1 84 ? 31.075 41.974 -8.891 1.00 17.15 ? 84 ASN A C 1 ATOM 672 O O . ASN A 1 84 ? 30.411 42.507 -9.782 1.00 15.53 ? 84 ASN A O 1 ATOM 673 C CB . ASN A 1 84 ? 31.441 43.685 -7.131 1.00 14.98 ? 84 ASN A CB 1 ATOM 674 C CG . ASN A 1 84 ? 32.412 44.381 -6.202 1.00 23.32 ? 84 ASN A CG 1 ATOM 675 O OD1 . ASN A 1 84 ? 33.359 43.776 -5.701 1.00 25.50 ? 84 ASN A OD1 1 ATOM 676 N ND2 . ASN A 1 84 ? 32.169 45.663 -5.956 1.00 19.25 ? 84 ASN A ND2 1 ATOM 677 N N . VAL A 1 85 ? 30.926 40.704 -8.537 1.00 12.92 ? 85 VAL A N 1 ATOM 678 C CA . VAL A 1 85 ? 29.860 39.886 -9.084 1.00 15.51 ? 85 VAL A CA 1 ATOM 679 C C . VAL A 1 85 ? 29.014 39.421 -7.909 1.00 15.81 ? 85 VAL A C 1 ATOM 680 O O . VAL A 1 85 ? 29.469 38.625 -7.090 1.00 15.65 ? 85 VAL A O 1 ATOM 681 C CB . VAL A 1 85 ? 30.395 38.674 -9.881 1.00 12.54 ? 85 VAL A CB 1 ATOM 682 C CG1 . VAL A 1 85 ? 29.230 37.832 -10.408 1.00 7.43 ? 85 VAL A CG1 1 ATOM 683 C CG2 . VAL A 1 85 ? 31.256 39.143 -11.046 1.00 8.20 ? 85 VAL A CG2 1 ATOM 684 N N . PRO A 1 86 ? 27.778 39.930 -7.813 1.00 9.60 ? 86 PRO A N 1 ATOM 685 C CA . PRO A 1 86 ? 26.960 39.616 -6.638 1.00 8.62 ? 86 PRO A CA 1 ATOM 686 C C . PRO A 1 86 ? 26.460 38.180 -6.657 1.00 10.46 ? 86 PRO A C 1 ATOM 687 O O . PRO A 1 86 ? 26.298 37.599 -7.729 1.00 13.20 ? 86 PRO A O 1 ATOM 688 C CB . PRO A 1 86 ? 25.797 40.606 -6.754 1.00 18.94 ? 86 PRO A CB 1 ATOM 689 C CG . PRO A 1 86 ? 25.682 40.876 -8.232 1.00 17.56 ? 86 PRO A CG 1 ATOM 690 C CD . PRO A 1 86 ? 27.098 40.849 -8.746 1.00 8.98 ? 86 PRO A CD 1 ATOM 691 N N . PRO A 1 87 ? 26.223 37.604 -5.469 1.00 11.45 ? 87 PRO A N 1 ATOM 692 C CA . PRO A 1 87 ? 25.815 36.196 -5.373 1.00 11.99 ? 87 PRO A CA 1 ATOM 693 C C . PRO A 1 87 ? 24.359 35.887 -5.692 1.00 12.76 ? 87 PRO A C 1 ATOM 694 O O . PRO A 1 87 ? 23.482 36.737 -5.551 1.00 13.32 ? 87 PRO A O 1 ATOM 695 C CB . PRO A 1 87 ? 26.095 35.870 -3.905 1.00 16.38 ? 87 PRO A CB 1 ATOM 696 C CG . PRO A 1 87 ? 25.896 37.184 -3.190 1.00 8.83 ? 87 PRO A CG 1 ATOM 697 C CD . PRO A 1 87 ? 26.410 38.228 -4.145 1.00 8.75 ? 87 PRO A CD 1 ATOM 698 N N . GLU A 1 88 ? 24.117 34.652 -6.117 1.00 16.98 ? 88 GLU A N 1 ATOM 699 C CA . GLU A 1 88 ? 22.785 34.061 -6.092 1.00 19.39 ? 88 GLU A CA 1 ATOM 700 C C . GLU A 1 88 ? 22.631 33.292 -4.794 1.00 9.60 ? 88 GLU A C 1 ATOM 701 O O . GLU A 1 88 ? 23.544 32.580 -4.392 1.00 16.31 ? 88 GLU A O 1 ATOM 702 C CB . GLU A 1 88 ? 22.571 33.132 -7.284 1.00 9.28 ? 88 GLU A CB 1 ATOM 703 C CG . GLU A 1 88 ? 22.666 33.806 -8.637 1.00 49.52 ? 88 GLU A CG 1 ATOM 704 C CD . GLU A 1 88 ? 22.425 32.832 -9.777 1.00 53.10 ? 88 GLU A CD 1 ATOM 705 O OE1 . GLU A 1 88 ? 22.239 31.625 -9.507 1.00 47.55 ? 88 GLU A OE1 1 ATOM 706 O OE2 . GLU A 1 88 ? 22.423 33.269 -10.947 1.00 58.15 ? 88 GLU A OE2 1 ATOM 707 N N . VAL A 1 89 ? 21.491 33.431 -4.127 1.00 10.14 ? 89 VAL A N 1 ATOM 708 C CA . VAL A 1 89 ? 21.318 32.775 -2.836 1.00 10.68 ? 89 VAL A CA 1 ATOM 709 C C . VAL A 1 89 ? 20.084 31.883 -2.805 1.00 16.74 ? 89 VAL A C 1 ATOM 710 O O . VAL A 1 89 ? 19.001 32.284 -3.222 1.00 18.09 ? 89 VAL A O 1 ATOM 711 C CB . VAL A 1 89 ? 21.223 33.801 -1.690 1.00 14.04 ? 89 VAL A CB 1 ATOM 712 C CG1 . VAL A 1 89 ? 21.071 33.089 -0.357 1.00 11.69 ? 89 VAL A CG1 1 ATOM 713 C CG2 . VAL A 1 89 ? 22.457 34.684 -1.674 1.00 16.55 ? 89 VAL A CG2 1 ATOM 714 N N . THR A 1 90 ? 20.253 30.668 -2.299 1.00 11.93 ? 90 THR A N 1 ATOM 715 C CA A THR A 1 90 ? 19.161 29.712 -2.177 0.64 12.29 ? 90 THR A CA 1 ATOM 716 C CA B THR A 1 90 ? 19.115 29.778 -2.147 0.36 12.30 ? 90 THR A CA 1 ATOM 717 C C . THR A 1 90 ? 19.124 29.168 -0.758 1.00 19.26 ? 90 THR A C 1 ATOM 718 O O . THR A 1 90 ? 20.173 28.853 -0.196 1.00 16.64 ? 90 THR A O 1 ATOM 719 C CB A THR A 1 90 ? 19.317 28.536 -3.159 0.64 17.81 ? 90 THR A CB 1 ATOM 720 C CB B THR A 1 90 ? 19.108 28.664 -3.207 0.36 15.77 ? 90 THR A CB 1 ATOM 721 O OG1 A THR A 1 90 ? 19.715 29.023 -4.446 0.64 11.76 ? 90 THR A OG1 1 ATOM 722 O OG1 B THR A 1 90 ? 20.395 28.036 -3.253 0.36 12.09 ? 90 THR A OG1 1 ATOM 723 C CG2 A THR A 1 90 ? 18.011 27.753 -3.285 0.64 13.04 ? 90 THR A CG2 1 ATOM 724 C CG2 B THR A 1 90 ? 18.793 29.238 -4.576 0.36 13.27 ? 90 THR A CG2 1 ATOM 725 N N . VAL A 1 91 ? 17.929 29.029 -0.201 1.00 15.81 ? 91 VAL A N 1 ATOM 726 C CA . VAL A 1 91 ? 17.766 28.390 1.088 1.00 21.95 ? 91 VAL A CA 1 ATOM 727 C C . VAL A 1 91 ? 16.925 27.141 0.896 1.00 18.98 ? 91 VAL A C 1 ATOM 728 O O . VAL A 1 91 ? 15.878 27.169 0.259 1.00 22.15 ? 91 VAL A O 1 ATOM 729 C CB . VAL A 1 91 ? 17.098 29.327 2.111 1.00 21.44 ? 91 VAL A CB 1 ATOM 730 C CG1 . VAL A 1 91 ? 16.759 28.574 3.387 1.00 24.00 ? 91 VAL A CG1 1 ATOM 731 C CG2 . VAL A 1 91 ? 18.008 30.497 2.424 1.00 17.26 ? 91 VAL A CG2 1 ATOM 732 N N . LEU A 1 92 ? 17.414 26.037 1.434 1.00 17.47 ? 92 LEU A N 1 ATOM 733 C CA . LEU A 1 92 ? 16.707 24.775 1.350 1.00 20.24 ? 92 LEU A CA 1 ATOM 734 C C . LEU A 1 92 ? 16.974 23.941 2.599 1.00 21.74 ? 92 LEU A C 1 ATOM 735 O O . LEU A 1 92 ? 17.863 24.264 3.385 1.00 23.77 ? 92 LEU A O 1 ATOM 736 C CB . LEU A 1 92 ? 17.071 24.066 0.033 1.00 26.72 ? 92 LEU A CB 1 ATOM 737 C CG . LEU A 1 92 ? 18.440 23.545 -0.437 1.00 29.47 ? 92 LEU A CG 1 ATOM 738 C CD1 . LEU A 1 92 ? 19.340 23.044 0.659 1.00 34.61 ? 92 LEU A CD1 1 ATOM 739 C CD2 . LEU A 1 92 ? 18.253 22.467 -1.493 1.00 37.72 ? 92 LEU A CD2 1 ATOM 740 N N . THR A 1 93 ? 16.208 22.872 2.780 1.00 17.53 ? 93 THR A N 1 ATOM 741 C CA . THR A 1 93 ? 16.465 21.957 3.879 1.00 27.71 ? 93 THR A CA 1 ATOM 742 C C . THR A 1 93 ? 17.206 20.752 3.340 1.00 29.98 ? 93 THR A C 1 ATOM 743 O O . THR A 1 93 ? 17.131 20.439 2.154 1.00 18.22 ? 93 THR A O 1 ATOM 744 C CB . THR A 1 93 ? 15.180 21.504 4.576 1.00 19.35 ? 93 THR A CB 1 ATOM 745 O OG1 . THR A 1 93 ? 14.360 20.782 3.646 1.00 19.60 ? 93 THR A OG1 1 ATOM 746 C CG2 . THR A 1 93 ? 14.424 22.710 5.131 1.00 19.44 ? 93 THR A CG2 1 ATOM 747 N N . ASN A 1 94 ? 17.940 20.088 4.221 1.00 18.99 ? 94 ASN A N 1 ATOM 748 C CA . ASN A 1 94 ? 18.721 18.934 3.815 1.00 24.42 ? 94 ASN A CA 1 ATOM 749 C C . ASN A 1 94 ? 17.914 17.630 3.753 1.00 23.29 ? 94 ASN A C 1 ATOM 750 O O . ASN A 1 94 ? 18.355 16.652 3.154 1.00 24.25 ? 94 ASN A O 1 ATOM 751 C CB . ASN A 1 94 ? 19.909 18.829 4.787 1.00 40.02 ? 94 ASN A CB 1 ATOM 752 C CG . ASN A 1 94 ? 20.464 17.432 4.912 1.00 53.22 ? 94 ASN A CG 1 ATOM 753 O OD1 . ASN A 1 94 ? 21.026 16.880 3.965 1.00 62.37 ? 94 ASN A OD1 1 ATOM 754 N ND2 . ASN A 1 94 ? 20.324 16.854 6.097 1.00 55.59 ? 94 ASN A ND2 1 ATOM 755 N N . SER A 1 95 ? 16.694 17.649 4.283 1.00 24.25 ? 95 SER A N 1 ATOM 756 C CA . SER A 1 95 ? 15.781 16.512 4.162 1.00 27.95 ? 95 SER A CA 1 ATOM 757 C C . SER A 1 95 ? 14.334 17.008 4.162 1.00 27.53 ? 95 SER A C 1 ATOM 758 O O . SER A 1 95 ? 14.077 18.149 4.549 1.00 22.18 ? 95 SER A O 1 ATOM 759 C CB . SER A 1 95 ? 16.021 15.495 5.285 1.00 30.69 ? 95 SER A CB 1 ATOM 760 O OG . SER A 1 95 ? 15.777 16.066 6.557 1.00 43.74 ? 95 SER A OG 1 ATOM 761 N N . PRO A 1 96 ? 13.387 16.166 3.710 1.00 28.52 ? 96 PRO A N 1 ATOM 762 C CA . PRO A 1 96 ? 11.986 16.594 3.788 1.00 26.27 ? 96 PRO A CA 1 ATOM 763 C C . PRO A 1 96 ? 11.615 16.997 5.211 1.00 29.28 ? 96 PRO A C 1 ATOM 764 O O . PRO A 1 96 ? 12.030 16.345 6.169 1.00 33.05 ? 96 PRO A O 1 ATOM 765 C CB . PRO A 1 96 ? 11.215 15.354 3.337 1.00 25.65 ? 96 PRO A CB 1 ATOM 766 C CG . PRO A 1 96 ? 12.161 14.660 2.412 1.00 27.66 ? 96 PRO A CG 1 ATOM 767 C CD . PRO A 1 96 ? 13.532 14.883 2.994 1.00 27.39 ? 96 PRO A CD 1 ATOM 768 N N . VAL A 1 97 ? 10.835 18.062 5.338 1.00 23.31 ? 97 VAL A N 1 ATOM 769 C CA . VAL A 1 97 ? 10.537 18.632 6.644 1.00 26.63 ? 97 VAL A CA 1 ATOM 770 C C . VAL A 1 97 ? 9.353 17.956 7.326 1.00 27.22 ? 97 VAL A C 1 ATOM 771 O O . VAL A 1 97 ? 8.283 17.788 6.739 1.00 31.23 ? 97 VAL A O 1 ATOM 772 C CB . VAL A 1 97 ? 10.263 20.134 6.536 1.00 29.78 ? 97 VAL A CB 1 ATOM 773 C CG1 . VAL A 1 97 ? 9.953 20.710 7.903 1.00 33.03 ? 97 VAL A CG1 1 ATOM 774 C CG2 . VAL A 1 97 ? 11.467 20.833 5.943 1.00 27.00 ? 97 VAL A CG2 1 ATOM 775 N N . GLU A 1 98 ? 9.570 17.566 8.576 1.00 26.83 ? 98 GLU A N 1 ATOM 776 C CA . GLU A 1 98 ? 8.511 17.063 9.432 1.00 32.04 ? 98 GLU A CA 1 ATOM 777 C C . GLU A 1 98 ? 8.540 17.860 10.730 1.00 32.92 ? 98 GLU A C 1 ATOM 778 O O . GLU A 1 98 ? 9.616 18.148 11.255 1.00 31.62 ? 98 GLU A O 1 ATOM 779 C CB . GLU A 1 98 ? 8.714 15.574 9.702 1.00 39.03 ? 98 GLU A CB 1 ATOM 780 C CG . GLU A 1 98 ? 8.699 14.708 8.451 1.00 56.05 ? 98 GLU A CG 1 ATOM 781 C CD . GLU A 1 98 ? 9.045 13.261 8.746 1.00 76.23 ? 98 GLU A CD 1 ATOM 782 O OE1 . GLU A 1 98 ? 10.114 13.018 9.344 1.00 80.36 ? 98 GLU A OE1 1 ATOM 783 O OE2 . GLU A 1 98 ? 8.251 12.368 8.382 1.00 83.60 ? 98 GLU A OE2 1 ATOM 784 N N . LEU A 1 99 ? 7.366 18.229 11.236 1.00 30.13 ? 99 LEU A N 1 ATOM 785 C CA . LEU A 1 99 ? 7.279 19.020 12.465 1.00 33.39 ? 99 LEU A CA 1 ATOM 786 C C . LEU A 1 99 ? 8.016 18.372 13.627 1.00 37.06 ? 99 LEU A C 1 ATOM 787 O O . LEU A 1 99 ? 7.915 17.163 13.835 1.00 35.50 ? 99 LEU A O 1 ATOM 788 C CB . LEU A 1 99 ? 5.818 19.255 12.853 1.00 37.05 ? 99 LEU A CB 1 ATOM 789 C CG . LEU A 1 99 ? 5.058 20.239 11.964 1.00 43.23 ? 99 LEU A CG 1 ATOM 790 C CD1 . LEU A 1 99 ? 3.623 20.407 12.432 1.00 41.12 ? 99 LEU A CD1 1 ATOM 791 C CD2 . LEU A 1 99 ? 5.783 21.580 11.971 1.00 47.09 ? 99 LEU A CD2 1 ATOM 792 N N . ARG A 1 100 ? 8.779 19.189 14.352 1.00 42.90 ? 100 ARG A N 1 ATOM 793 C CA . ARG A 1 100 ? 9.605 18.746 15.483 1.00 45.02 ? 100 ARG A CA 1 ATOM 794 C C . ARG A 1 100 ? 10.473 17.505 15.212 1.00 43.05 ? 100 ARG A C 1 ATOM 795 O O . ARG A 1 100 ? 10.807 16.744 16.125 1.00 43.82 ? 100 ARG A O 1 ATOM 796 C CB . ARG A 1 100 ? 8.731 18.593 16.739 1.00 54.33 ? 100 ARG A CB 1 ATOM 797 C CG . ARG A 1 100 ? 7.794 17.413 16.822 1.00 63.40 ? 100 ARG A CG 1 ATOM 798 C CD . ARG A 1 100 ? 6.775 17.705 17.915 1.00 68.52 ? 100 ARG A CD 1 ATOM 799 N NE . ARG A 1 100 ? 5.825 18.733 17.497 1.00 70.83 ? 100 ARG A NE 1 ATOM 800 C CZ . ARG A 1 100 ? 4.709 18.504 16.816 1.00 72.82 ? 100 ARG A CZ 1 ATOM 801 N NH1 . ARG A 1 100 ? 4.376 17.267 16.471 1.00 76.68 ? 100 ARG A NH1 1 ATOM 802 N NH2 . ARG A 1 100 ? 3.917 19.519 16.486 1.00 69.21 ? 100 ARG A NH2 1 ATOM 803 N N . GLU A 1 101 ? 10.841 17.331 13.945 1.00 46.28 ? 101 GLU A N 1 ATOM 804 C CA . GLU A 1 101 ? 11.852 16.358 13.541 1.00 41.34 ? 101 GLU A CA 1 ATOM 805 C C . GLU A 1 101 ? 13.073 17.129 13.075 1.00 36.53 ? 101 GLU A C 1 ATOM 806 O O . GLU A 1 101 ? 13.003 17.870 12.099 1.00 31.85 ? 101 GLU A O 1 ATOM 807 C CB . GLU A 1 101 ? 11.356 15.439 12.422 1.00 38.26 ? 101 GLU A CB 1 ATOM 808 C CG . GLU A 1 101 ? 10.253 14.481 12.811 1.00 51.70 ? 101 GLU A CG 1 ATOM 809 C CD . GLU A 1 101 ? 10.700 13.507 13.887 1.00 60.63 ? 101 GLU A CD 1 ATOM 810 O OE1 . GLU A 1 101 ? 11.893 13.132 13.888 1.00 62.36 ? 101 GLU A OE1 1 ATOM 811 O OE2 . GLU A 1 101 ? 9.863 13.101 14.720 1.00 66.90 ? 101 GLU A OE2 1 ATOM 812 N N . PRO A 1 102 ? 14.205 16.939 13.772 1.00 27.54 ? 102 PRO A N 1 ATOM 813 C CA . PRO A 1 102 ? 15.455 17.670 13.534 1.00 27.73 ? 102 PRO A CA 1 ATOM 814 C C . PRO A 1 102 ? 15.821 17.716 12.060 1.00 24.50 ? 102 PRO A C 1 ATOM 815 O O . PRO A 1 102 ? 15.786 16.694 11.377 1.00 23.30 ? 102 PRO A O 1 ATOM 816 C CB . PRO A 1 102 ? 16.484 16.869 14.329 1.00 20.15 ? 102 PRO A CB 1 ATOM 817 C CG . PRO A 1 102 ? 15.696 16.288 15.451 1.00 24.34 ? 102 PRO A CG 1 ATOM 818 C CD . PRO A 1 102 ? 14.341 15.970 14.875 1.00 25.75 ? 102 PRO A CD 1 ATOM 819 N N . ASN A 1 103 ? 16.164 18.905 11.581 1.00 22.07 ? 103 ASN A N 1 ATOM 820 C CA . ASN A 1 103 ? 16.501 19.090 10.182 1.00 17.34 ? 103 ASN A CA 1 ATOM 821 C C . ASN A 1 103 ? 17.645 20.090 10.095 1.00 18.59 ? 103 ASN A C 1 ATOM 822 O O . ASN A 1 103 ? 18.130 20.573 11.117 1.00 15.90 ? 103 ASN A O 1 ATOM 823 C CB . ASN A 1 103 ? 15.274 19.569 9.404 1.00 23.70 ? 103 ASN A CB 1 ATOM 824 C CG . ASN A 1 103 ? 15.307 19.169 7.939 1.00 25.63 ? 103 ASN A CG 1 ATOM 825 O OD1 . ASN A 1 103 ? 16.318 19.331 7.259 1.00 27.25 ? 103 ASN A OD1 1 ATOM 826 N ND2 . ASN A 1 103 ? 14.189 18.642 7.446 1.00 21.07 ? 103 ASN A ND2 1 ATOM 827 N N . VAL A 1 104 ? 18.082 20.413 8.886 1.00 18.77 ? 104 VAL A N 1 ATOM 828 C CA . VAL A 1 104 ? 19.151 21.390 8.730 1.00 15.54 ? 104 VAL A CA 1 ATOM 829 C C . VAL A 1 104 ? 18.808 22.345 7.602 1.00 17.67 ? 104 VAL A C 1 ATOM 830 O O . VAL A 1 104 ? 18.510 21.919 6.484 1.00 15.09 ? 104 VAL A O 1 ATOM 831 C CB . VAL A 1 104 ? 20.521 20.716 8.435 1.00 19.08 ? 104 VAL A CB 1 ATOM 832 C CG1 . VAL A 1 104 ? 21.615 21.764 8.268 1.00 15.36 ? 104 VAL A CG1 1 ATOM 833 C CG2 . VAL A 1 104 ? 20.889 19.723 9.531 1.00 20.61 ? 104 VAL A CG2 1 ATOM 834 N N . LEU A 1 105 ? 18.865 23.641 7.894 1.00 17.22 ? 105 LEU A N 1 ATOM 835 C CA . LEU A 1 105 ? 18.744 24.640 6.847 1.00 14.83 ? 105 LEU A CA 1 ATOM 836 C C . LEU A 1 105 ? 20.086 24.866 6.189 1.00 17.16 ? 105 LEU A C 1 ATOM 837 O O . LEU A 1 105 ? 21.110 24.991 6.863 1.00 18.49 ? 105 LEU A O 1 ATOM 838 C CB . LEU A 1 105 ? 18.215 25.962 7.404 1.00 22.52 ? 105 LEU A CB 1 ATOM 839 C CG . LEU A 1 105 ? 16.713 26.060 7.657 1.00 28.75 ? 105 LEU A CG 1 ATOM 840 C CD1 . LEU A 1 105 ? 16.400 27.267 8.516 1.00 29.26 ? 105 LEU A CD1 1 ATOM 841 C CD2 . LEU A 1 105 ? 15.968 26.144 6.339 1.00 24.02 ? 105 LEU A CD2 1 ATOM 842 N N . ILE A 1 106 ? 20.068 24.920 4.864 1.00 19.50 ? 106 ILE A N 1 ATOM 843 C CA . ILE A 1 106 ? 21.264 25.194 4.093 1.00 16.06 ? 106 ILE A CA 1 ATOM 844 C C . ILE A 1 106 ? 21.107 26.510 3.344 1.00 15.35 ? 106 ILE A C 1 ATOM 845 O O . ILE A 1 106 ? 20.111 26.724 2.661 1.00 15.09 ? 106 ILE A O 1 ATOM 846 C CB . ILE A 1 106 ? 21.560 24.065 3.099 1.00 16.93 ? 106 ILE A CB 1 ATOM 847 C CG1 . ILE A 1 106 ? 21.578 22.716 3.824 1.00 23.53 ? 106 ILE A CG1 1 ATOM 848 C CG2 . ILE A 1 106 ? 22.872 24.322 2.375 1.00 14.78 ? 106 ILE A CG2 1 ATOM 849 C CD1 . ILE A 1 106 ? 21.650 21.522 2.902 1.00 24.62 ? 106 ILE A CD1 1 ATOM 850 N N . CYS A 1 107 ? 22.087 27.393 3.492 1.00 9.98 ? 107 CYS A N 1 ATOM 851 C CA . CYS A 1 107 ? 22.124 28.612 2.702 1.00 15.40 ? 107 CYS A CA 1 ATOM 852 C C . CYS A 1 107 ? 23.229 28.457 1.671 1.00 13.07 ? 107 CYS A C 1 ATOM 853 O O . CYS A 1 107 ? 24.401 28.363 2.019 1.00 10.62 ? 107 CYS A O 1 ATOM 854 C CB . CYS A 1 107 ? 22.355 29.846 3.573 1.00 9.93 ? 107 CYS A CB 1 ATOM 855 S SG . CYS A 1 107 ? 22.272 31.419 2.673 1.00 13.60 ? 107 CYS A SG 1 ATOM 856 N N . PHE A 1 108 ? 22.847 28.417 0.401 1.00 10.43 ? 108 PHE A N 1 ATOM 857 C CA . PHE A 1 108 ? 23.814 28.237 -0.668 1.00 10.54 ? 108 PHE A CA 1 ATOM 858 C C . PHE A 1 108 ? 24.071 29.583 -1.326 1.00 16.37 ? 108 PHE A C 1 ATOM 859 O O . PHE A 1 108 ? 23.169 30.195 -1.893 1.00 19.51 ? 108 PHE A O 1 ATOM 860 C CB . PHE A 1 108 ? 23.299 27.208 -1.686 1.00 11.82 ? 108 PHE A CB 1 ATOM 861 C CG . PHE A 1 108 ? 24.250 26.933 -2.823 1.00 16.47 ? 108 PHE A CG 1 ATOM 862 C CD1 . PHE A 1 108 ? 25.604 26.748 -2.591 1.00 18.24 ? 108 PHE A CD1 1 ATOM 863 C CD2 . PHE A 1 108 ? 23.780 26.842 -4.125 1.00 15.88 ? 108 PHE A CD2 1 ATOM 864 C CE1 . PHE A 1 108 ? 26.474 26.492 -3.639 1.00 20.39 ? 108 PHE A CE1 1 ATOM 865 C CE2 . PHE A 1 108 ? 24.644 26.584 -5.179 1.00 13.98 ? 108 PHE A CE2 1 ATOM 866 C CZ . PHE A 1 108 ? 25.992 26.408 -4.936 1.00 15.30 ? 108 PHE A CZ 1 ATOM 867 N N . ILE A 1 109 ? 25.322 30.020 -1.260 1.00 16.67 ? 109 ILE A N 1 ATOM 868 C CA . ILE A 1 109 ? 25.721 31.308 -1.800 1.00 13.88 ? 109 ILE A CA 1 ATOM 869 C C . ILE A 1 109 ? 26.618 31.005 -2.980 1.00 10.41 ? 109 ILE A C 1 ATOM 870 O O . ILE A 1 109 ? 27.644 30.353 -2.817 1.00 13.27 ? 109 ILE A O 1 ATOM 871 C CB . ILE A 1 109 ? 26.461 32.176 -0.767 1.00 14.03 ? 109 ILE A CB 1 ATOM 872 C CG1 . ILE A 1 109 ? 25.633 32.322 0.512 1.00 22.43 ? 109 ILE A CG1 1 ATOM 873 C CG2 . ILE A 1 109 ? 26.791 33.534 -1.351 1.00 11.24 ? 109 ILE A CG2 1 ATOM 874 C CD1 . ILE A 1 109 ? 26.035 31.361 1.617 1.00 33.70 ? 109 ILE A CD1 1 ATOM 875 N N . ASP A 1 110 ? 26.228 31.471 -4.163 1.00 9.66 ? 110 ASP A N 1 ATOM 876 C CA . ASP A 1 110 ? 26.795 30.970 -5.410 1.00 8.91 ? 110 ASP A CA 1 ATOM 877 C C . ASP A 1 110 ? 27.123 32.069 -6.416 1.00 10.16 ? 110 ASP A C 1 ATOM 878 O O . ASP A 1 110 ? 26.518 33.142 -6.393 1.00 11.07 ? 110 ASP A O 1 ATOM 879 C CB . ASP A 1 110 ? 25.797 29.982 -6.029 1.00 9.04 ? 110 ASP A CB 1 ATOM 880 C CG . ASP A 1 110 ? 26.409 29.107 -7.104 1.00 9.18 ? 110 ASP A CG 1 ATOM 881 O OD1 . ASP A 1 110 ? 27.649 28.995 -7.171 1.00 16.32 ? 110 ASP A OD1 1 ATOM 882 O OD2 . ASP A 1 110 ? 25.633 28.522 -7.888 1.00 20.69 ? 110 ASP A OD2 1 ATOM 883 N N . LYS A 1 111 ? 28.093 31.791 -7.289 1.00 12.68 ? 111 LYS A N 1 ATOM 884 C CA . LYS A 1 111 ? 28.388 32.639 -8.448 1.00 14.45 ? 111 LYS A CA 1 ATOM 885 C C . LYS A 1 111 ? 28.781 34.064 -8.086 1.00 11.43 ? 111 LYS A C 1 ATOM 886 O O . LYS A 1 111 ? 28.238 35.021 -8.643 1.00 11.22 ? 111 LYS A O 1 ATOM 887 C CB . LYS A 1 111 ? 27.195 32.671 -9.408 1.00 17.86 ? 111 LYS A CB 1 ATOM 888 C CG . LYS A 1 111 ? 26.792 31.309 -9.919 1.00 25.83 ? 111 LYS A CG 1 ATOM 889 C CD . LYS A 1 111 ? 25.436 31.359 -10.595 1.00 36.04 ? 111 LYS A CD 1 ATOM 890 C CE . LYS A 1 111 ? 24.953 29.969 -10.974 1.00 40.46 ? 111 LYS A CE 1 ATOM 891 N NZ . LYS A 1 111 ? 23.620 30.014 -11.633 1.00 45.78 ? 111 LYS A NZ 1 ATOM 892 N N . PHE A 1 112 ? 29.709 34.221 -7.151 1.00 14.96 ? 112 PHE A N 1 ATOM 893 C CA . PHE A 1 112 ? 30.100 35.562 -6.738 1.00 11.98 ? 112 PHE A CA 1 ATOM 894 C C . PHE A 1 112 ? 31.615 35.750 -6.670 1.00 14.85 ? 112 PHE A C 1 ATOM 895 O O . PHE A 1 112 ? 32.381 34.789 -6.576 1.00 12.00 ? 112 PHE A O 1 ATOM 896 C CB . PHE A 1 112 ? 29.453 35.912 -5.388 1.00 10.17 ? 112 PHE A CB 1 ATOM 897 C CG . PHE A 1 112 ? 29.965 35.096 -4.232 1.00 14.17 ? 112 PHE A CG 1 ATOM 898 C CD1 . PHE A 1 112 ? 29.449 33.836 -3.980 1.00 10.84 ? 112 PHE A CD1 1 ATOM 899 C CD2 . PHE A 1 112 ? 30.955 35.591 -3.395 1.00 15.54 ? 112 PHE A CD2 1 ATOM 900 C CE1 . PHE A 1 112 ? 29.917 33.077 -2.923 1.00 15.03 ? 112 PHE A CE1 1 ATOM 901 C CE2 . PHE A 1 112 ? 31.426 34.837 -2.333 1.00 13.90 ? 112 PHE A CE2 1 ATOM 902 C CZ . PHE A 1 112 ? 30.905 33.578 -2.096 1.00 14.02 ? 112 PHE A CZ 1 ATOM 903 N N . THR A 1 113 ? 32.030 37.011 -6.709 1.00 16.53 ? 113 THR A N 1 ATOM 904 C CA . THR A 1 113 ? 33.416 37.382 -6.477 1.00 8.71 ? 113 THR A CA 1 ATOM 905 C C . THR A 1 113 ? 33.418 38.877 -6.174 1.00 12.80 ? 113 THR A C 1 ATOM 906 O O . THR A 1 113 ? 32.544 39.601 -6.652 1.00 13.00 ? 113 THR A O 1 ATOM 907 C CB . THR A 1 113 ? 34.314 37.056 -7.699 1.00 16.21 ? 113 THR A CB 1 ATOM 908 O OG1 . THR A 1 113 ? 35.681 36.947 -7.287 1.00 10.35 ? 113 THR A OG1 1 ATOM 909 C CG2 . THR A 1 113 ? 34.188 38.123 -8.781 1.00 10.75 ? 113 THR A CG2 1 ATOM 910 N N . PRO A 1 114 ? 34.383 39.352 -5.366 1.00 18.35 ? 114 PRO A N 1 ATOM 911 C CA . PRO A 1 114 ? 35.475 38.635 -4.691 1.00 11.26 ? 114 PRO A CA 1 ATOM 912 C C . PRO A 1 114 ? 34.966 37.698 -3.594 1.00 13.44 ? 114 PRO A C 1 ATOM 913 O O . PRO A 1 114 ? 33.805 37.810 -3.194 1.00 14.53 ? 114 PRO A O 1 ATOM 914 C CB . PRO A 1 114 ? 36.322 39.768 -4.095 1.00 15.36 ? 114 PRO A CB 1 ATOM 915 C CG . PRO A 1 114 ? 35.377 40.895 -3.924 1.00 14.32 ? 114 PRO A CG 1 ATOM 916 C CD . PRO A 1 114 ? 34.412 40.796 -5.066 1.00 14.76 ? 114 PRO A CD 1 ATOM 917 N N . PRO A 1 115 ? 35.822 36.777 -3.121 1.00 15.49 ? 115 PRO A N 1 ATOM 918 C CA . PRO A 1 115 ? 35.440 35.825 -2.073 1.00 8.81 ? 115 PRO A CA 1 ATOM 919 C C . PRO A 1 115 ? 35.410 36.485 -0.697 1.00 14.39 ? 115 PRO A C 1 ATOM 920 O O . PRO A 1 115 ? 36.229 36.169 0.171 1.00 13.89 ? 115 PRO A O 1 ATOM 921 C CB . PRO A 1 115 ? 36.538 34.765 -2.148 1.00 8.86 ? 115 PRO A CB 1 ATOM 922 C CG . PRO A 1 115 ? 37.728 35.517 -2.645 1.00 8.89 ? 115 PRO A CG 1 ATOM 923 C CD . PRO A 1 115 ? 37.185 36.512 -3.625 1.00 8.83 ? 115 PRO A CD 1 ATOM 924 N N . VAL A 1 116 ? 34.458 37.396 -0.517 1.00 15.34 ? 116 VAL A N 1 ATOM 925 C CA . VAL A 1 116 ? 34.196 38.044 0.769 1.00 19.40 ? 116 VAL A CA 1 ATOM 926 C C . VAL A 1 116 ? 32.700 38.216 0.925 1.00 17.37 ? 116 VAL A C 1 ATOM 927 O O . VAL A 1 116 ? 32.041 38.834 0.088 1.00 14.76 ? 116 VAL A O 1 ATOM 928 C CB . VAL A 1 116 ? 34.854 39.437 0.898 1.00 24.96 ? 116 VAL A CB 1 ATOM 929 C CG1 . VAL A 1 116 ? 34.544 40.044 2.270 1.00 14.33 ? 116 VAL A CG1 1 ATOM 930 C CG2 . VAL A 1 116 ? 36.341 39.350 0.682 1.00 19.26 ? 116 VAL A CG2 1 ATOM 931 N N . VAL A 1 117 ? 32.164 37.670 2.009 1.00 16.71 ? 117 VAL A N 1 ATOM 932 C CA . VAL A 1 117 ? 30.735 37.741 2.243 1.00 21.28 ? 117 VAL A CA 1 ATOM 933 C C . VAL A 1 117 ? 30.417 37.790 3.741 1.00 20.69 ? 117 VAL A C 1 ATOM 934 O O . VAL A 1 117 ? 31.145 37.227 4.560 1.00 20.04 ? 117 VAL A O 1 ATOM 935 C CB . VAL A 1 117 ? 30.034 36.530 1.565 1.00 17.70 ? 117 VAL A CB 1 ATOM 936 C CG1 . VAL A 1 117 ? 30.091 35.290 2.448 1.00 11.60 ? 117 VAL A CG1 1 ATOM 937 C CG2 . VAL A 1 117 ? 28.617 36.869 1.194 1.00 28.74 ? 117 VAL A CG2 1 ATOM 938 N N . ASN A 1 118 ? 29.355 38.504 4.101 1.00 16.78 ? 118 ASN A N 1 ATOM 939 C CA . ASN A 1 118 ? 28.818 38.422 5.454 1.00 20.53 ? 118 ASN A CA 1 ATOM 940 C C . ASN A 1 118 ? 27.513 37.652 5.388 1.00 20.57 ? 118 ASN A C 1 ATOM 941 O O . ASN A 1 118 ? 26.591 38.039 4.668 1.00 17.84 ? 118 ASN A O 1 ATOM 942 C CB . ASN A 1 118 ? 28.613 39.815 6.069 1.00 18.85 ? 118 ASN A CB 1 ATOM 943 C CG . ASN A 1 118 ? 29.930 40.546 6.313 1.00 27.08 ? 118 ASN A CG 1 ATOM 944 O OD1 . ASN A 1 118 ? 30.931 39.922 6.640 1.00 30.67 ? 118 ASN A OD1 1 ATOM 945 N ND2 . ASN A 1 118 ? 29.933 41.868 6.143 1.00 35.00 ? 118 ASN A ND2 1 ATOM 946 N N . VAL A 1 119 ? 27.420 36.583 6.170 1.00 23.64 ? 119 VAL A N 1 ATOM 947 C CA . VAL A 1 119 ? 26.213 35.772 6.177 1.00 17.53 ? 119 VAL A CA 1 ATOM 948 C C . VAL A 1 119 ? 25.647 35.676 7.582 1.00 18.63 ? 119 VAL A C 1 ATOM 949 O O . VAL A 1 119 ? 26.351 35.327 8.529 1.00 18.46 ? 119 VAL A O 1 ATOM 950 C CB . VAL A 1 119 ? 26.485 34.348 5.647 1.00 23.78 ? 119 VAL A CB 1 ATOM 951 C CG1 . VAL A 1 119 ? 25.211 33.513 5.690 1.00 13.81 ? 119 VAL A CG1 1 ATOM 952 C CG2 . VAL A 1 119 ? 27.043 34.399 4.227 1.00 18.57 ? 119 VAL A CG2 1 ATOM 953 N N . THR A 1 120 ? 24.360 35.968 7.704 1.00 16.59 ? 120 THR A N 1 ATOM 954 C CA . THR A 1 120 ? 23.689 35.879 8.984 1.00 20.93 ? 120 THR A CA 1 ATOM 955 C C . THR A 1 120 ? 22.417 35.054 8.873 1.00 23.63 ? 120 THR A C 1 ATOM 956 O O . THR A 1 120 ? 21.615 35.255 7.963 1.00 18.60 ? 120 THR A O 1 ATOM 957 C CB . THR A 1 120 ? 23.336 37.277 9.533 1.00 22.46 ? 120 THR A CB 1 ATOM 958 O OG1 . THR A 1 120 ? 24.502 38.111 9.526 1.00 24.22 ? 120 THR A OG1 1 ATOM 959 C CG2 . THR A 1 120 ? 22.802 37.175 10.948 1.00 15.87 ? 120 THR A CG2 1 ATOM 960 N N . TRP A 1 121 ? 22.243 34.130 9.809 1.00 20.17 ? 121 TRP A N 1 ATOM 961 C CA . TRP A 1 121 ? 20.991 33.412 9.942 1.00 17.31 ? 121 TRP A CA 1 ATOM 962 C C . TRP A 1 121 ? 20.056 34.212 10.832 1.00 21.25 ? 121 TRP A C 1 ATOM 963 O O . TRP A 1 121 ? 20.464 34.715 11.881 1.00 23.37 ? 121 TRP A O 1 ATOM 964 C CB . TRP A 1 121 ? 21.196 32.018 10.535 1.00 14.92 ? 121 TRP A CB 1 ATOM 965 C CG . TRP A 1 121 ? 21.740 30.976 9.604 1.00 12.10 ? 121 TRP A CG 1 ATOM 966 C CD1 . TRP A 1 121 ? 22.986 30.421 9.633 1.00 20.05 ? 121 TRP A CD1 1 ATOM 967 C CD2 . TRP A 1 121 ? 21.044 30.340 8.527 1.00 11.39 ? 121 TRP A CD2 1 ATOM 968 N NE1 . TRP A 1 121 ? 23.111 29.483 8.638 1.00 11.13 ? 121 TRP A NE1 1 ATOM 969 C CE2 . TRP A 1 121 ? 21.933 29.416 7.943 1.00 19.43 ? 121 TRP A CE2 1 ATOM 970 C CE3 . TRP A 1 121 ? 19.756 30.466 7.996 1.00 14.68 ? 121 TRP A CE3 1 ATOM 971 C CZ2 . TRP A 1 121 ? 21.576 28.622 6.854 1.00 15.37 ? 121 TRP A CZ2 1 ATOM 972 C CZ3 . TRP A 1 121 ? 19.402 29.681 6.918 1.00 14.83 ? 121 TRP A CZ3 1 ATOM 973 C CH2 . TRP A 1 121 ? 20.309 28.769 6.357 1.00 22.83 ? 121 TRP A CH2 1 ATOM 974 N N . LEU A 1 122 ? 18.812 34.350 10.397 1.00 20.08 ? 122 LEU A N 1 ATOM 975 C CA . LEU A 1 122 ? 17.802 35.051 11.175 1.00 20.76 ? 122 LEU A CA 1 ATOM 976 C C . LEU A 1 122 ? 16.668 34.096 11.510 1.00 20.11 ? 122 LEU A C 1 ATOM 977 O O . LEU A 1 122 ? 16.169 33.381 10.641 1.00 20.20 ? 122 LEU A O 1 ATOM 978 C CB . LEU A 1 122 ? 17.265 36.273 10.421 1.00 18.69 ? 122 LEU A CB 1 ATOM 979 C CG . LEU A 1 122 ? 18.252 37.375 10.037 1.00 21.17 ? 122 LEU A CG 1 ATOM 980 C CD1 . LEU A 1 122 ? 17.613 38.330 9.038 1.00 12.95 ? 122 LEU A CD1 1 ATOM 981 C CD2 . LEU A 1 122 ? 18.713 38.131 11.275 1.00 18.13 ? 122 LEU A CD2 1 ATOM 982 N N . ARG A 1 123 ? 16.275 34.084 12.776 1.00 15.79 ? 123 ARG A N 1 ATOM 983 C CA . ARG A 1 123 ? 15.106 33.338 13.208 1.00 14.66 ? 123 ARG A CA 1 ATOM 984 C C . ARG A 1 123 ? 14.116 34.354 13.731 1.00 16.93 ? 123 ARG A C 1 ATOM 985 O O . ARG A 1 123 ? 14.399 35.044 14.711 1.00 18.25 ? 123 ARG A O 1 ATOM 986 C CB . ARG A 1 123 ? 15.458 32.343 14.313 1.00 17.10 ? 123 ARG A CB 1 ATOM 987 C CG . ARG A 1 123 ? 14.277 31.575 14.885 1.00 26.11 ? 123 ARG A CG 1 ATOM 988 C CD . ARG A 1 123 ? 14.695 30.790 16.127 1.00 33.24 ? 123 ARG A CD 1 ATOM 989 N NE . ARG A 1 123 ? 15.717 29.782 15.861 1.00 52.63 ? 123 ARG A NE 1 ATOM 990 C CZ . ARG A 1 123 ? 15.814 28.629 16.515 1.00 65.69 ? 123 ARG A CZ 1 ATOM 991 N NH1 . ARG A 1 123 ? 14.948 28.335 17.477 1.00 71.11 ? 123 ARG A NH1 1 ATOM 992 N NH2 . ARG A 1 123 ? 16.776 27.769 16.208 1.00 64.44 ? 123 ARG A NH2 1 ATOM 993 N N . ASN A 1 124 ? 12.965 34.450 13.076 1.00 15.03 ? 124 ASN A N 1 ATOM 994 C CA . ASN A 1 124 ? 11.976 35.465 13.412 1.00 24.74 ? 124 ASN A CA 1 ATOM 995 C C . ASN A 1 124 ? 12.584 36.862 13.426 1.00 24.15 ? 124 ASN A C 1 ATOM 996 O O . ASN A 1 124 ? 12.255 37.680 14.285 1.00 26.04 ? 124 ASN A O 1 ATOM 997 C CB . ASN A 1 124 ? 11.310 35.154 14.755 1.00 24.20 ? 124 ASN A CB 1 ATOM 998 C CG . ASN A 1 124 ? 10.654 33.792 14.770 1.00 25.01 ? 124 ASN A CG 1 ATOM 999 O OD1 . ASN A 1 124 ? 10.092 33.355 13.764 1.00 20.28 ? 124 ASN A OD1 1 ATOM 1000 N ND2 . ASN A 1 124 ? 10.713 33.114 15.912 1.00 19.78 ? 124 ASN A ND2 1 ATOM 1001 N N . GLY A 1 125 ? 13.492 37.124 12.489 1.00 21.76 ? 125 GLY A N 1 ATOM 1002 C CA . GLY A 1 125 ? 14.090 38.442 12.368 1.00 21.07 ? 125 GLY A CA 1 ATOM 1003 C C . GLY A 1 125 ? 15.256 38.699 13.305 1.00 21.47 ? 125 GLY A C 1 ATOM 1004 O O . GLY A 1 125 ? 15.801 39.805 13.335 1.00 18.97 ? 125 GLY A O 1 ATOM 1005 N N . LYS A 1 126 ? 15.647 37.680 14.063 1.00 13.92 ? 126 LYS A N 1 ATOM 1006 C CA . LYS A 1 126 ? 16.741 37.818 15.020 1.00 16.48 ? 126 LYS A CA 1 ATOM 1007 C C . LYS A 1 126 ? 17.922 36.933 14.657 1.00 19.03 ? 126 LYS A C 1 ATOM 1008 O O . LYS A 1 126 ? 17.740 35.777 14.278 1.00 25.52 ? 126 LYS A O 1 ATOM 1009 C CB . LYS A 1 126 ? 16.288 37.482 16.443 1.00 17.58 ? 126 LYS A CB 1 ATOM 1010 C CG . LYS A 1 126 ? 15.107 38.281 16.967 1.00 19.71 ? 126 LYS A CG 1 ATOM 1011 C CD . LYS A 1 126 ? 14.853 37.914 18.423 1.00 25.23 ? 126 LYS A CD 1 ATOM 1012 C CE . LYS A 1 126 ? 13.675 38.661 19.016 1.00 35.51 ? 126 LYS A CE 1 ATOM 1013 N NZ . LYS A 1 126 ? 13.520 38.327 20.461 1.00 39.75 ? 126 LYS A NZ 1 ATOM 1014 N N . PRO A 1 127 ? 19.142 37.475 14.792 1.00 23.06 ? 127 PRO A N 1 ATOM 1015 C CA . PRO A 1 127 ? 20.355 36.717 14.476 1.00 18.17 ? 127 PRO A CA 1 ATOM 1016 C C . PRO A 1 127 ? 20.484 35.501 15.376 1.00 21.22 ? 127 PRO A C 1 ATOM 1017 O O . PRO A 1 127 ? 20.270 35.602 16.586 1.00 22.66 ? 127 PRO A O 1 ATOM 1018 C CB . PRO A 1 127 ? 21.483 37.717 14.759 1.00 22.78 ? 127 PRO A CB 1 ATOM 1019 C CG . PRO A 1 127 ? 20.841 39.060 14.669 1.00 26.39 ? 127 PRO A CG 1 ATOM 1020 C CD . PRO A 1 127 ? 19.445 38.864 15.184 1.00 19.86 ? 127 PRO A CD 1 ATOM 1021 N N . VAL A 1 128 ? 20.811 34.358 14.784 1.00 22.37 ? 128 VAL A N 1 ATOM 1022 C CA . VAL A 1 128 ? 21.027 33.141 15.552 1.00 28.32 ? 128 VAL A CA 1 ATOM 1023 C C . VAL A 1 128 ? 22.375 32.532 15.194 1.00 32.09 ? 128 VAL A C 1 ATOM 1024 O O . VAL A 1 128 ? 22.790 32.550 14.033 1.00 34.56 ? 128 VAL A O 1 ATOM 1025 C CB . VAL A 1 128 ? 19.906 32.109 15.316 1.00 30.22 ? 128 VAL A CB 1 ATOM 1026 C CG1 . VAL A 1 128 ? 18.596 32.634 15.850 1.00 44.30 ? 128 VAL A CG1 1 ATOM 1027 C CG2 . VAL A 1 128 ? 19.773 31.781 13.844 1.00 23.88 ? 128 VAL A CG2 1 ATOM 1028 N N . THR A 1 129 ? 23.070 32.008 16.199 1.00 37.86 ? 129 THR A N 1 ATOM 1029 C CA . THR A 1 129 ? 24.409 31.476 15.982 1.00 41.51 ? 129 THR A CA 1 ATOM 1030 C C . THR A 1 129 ? 24.587 30.096 16.599 1.00 41.35 ? 129 THR A C 1 ATOM 1031 O O . THR A 1 129 ? 25.593 29.431 16.363 1.00 42.44 ? 129 THR A O 1 ATOM 1032 C CB . THR A 1 129 ? 25.485 32.408 16.569 1.00 42.59 ? 129 THR A CB 1 ATOM 1033 O OG1 . THR A 1 129 ? 25.345 32.463 17.994 1.00 39.84 ? 129 THR A OG1 1 ATOM 1034 C CG2 . THR A 1 129 ? 25.360 33.811 15.996 1.00 48.78 ? 129 THR A CG2 1 ATOM 1035 N N . THR A 1 130 ? 23.611 29.663 17.387 1.00 42.05 ? 130 THR A N 1 ATOM 1036 C CA . THR A 1 130 ? 23.707 28.365 18.042 1.00 44.97 ? 130 THR A CA 1 ATOM 1037 C C . THR A 1 130 ? 23.690 27.220 17.034 1.00 37.19 ? 130 THR A C 1 ATOM 1038 O O . THR A 1 130 ? 22.699 27.003 16.340 1.00 40.48 ? 130 THR A O 1 ATOM 1039 C CB . THR A 1 130 ? 22.574 28.166 19.062 1.00 44.47 ? 130 THR A CB 1 ATOM 1040 O OG1 . THR A 1 130 ? 22.718 29.125 20.118 1.00 49.60 ? 130 THR A OG1 1 ATOM 1041 C CG2 . THR A 1 130 ? 22.632 26.763 19.652 1.00 45.00 ? 130 THR A CG2 1 ATOM 1042 N N . GLY A 1 131 ? 24.801 26.498 16.954 1.00 35.30 ? 131 GLY A N 1 ATOM 1043 C CA . GLY A 1 131 ? 24.896 25.309 16.130 1.00 34.08 ? 131 GLY A CA 1 ATOM 1044 C C . GLY A 1 131 ? 25.235 25.546 14.668 1.00 33.45 ? 131 GLY A C 1 ATOM 1045 O O . GLY A 1 131 ? 25.360 24.588 13.902 1.00 33.49 ? 131 GLY A O 1 ATOM 1046 N N . VAL A 1 132 ? 25.409 26.805 14.277 1.00 22.47 ? 132 VAL A N 1 ATOM 1047 C CA . VAL A 1 132 ? 25.699 27.114 12.880 1.00 24.38 ? 132 VAL A CA 1 ATOM 1048 C C . VAL A 1 132 ? 27.098 26.670 12.471 1.00 22.03 ? 132 VAL A C 1 ATOM 1049 O O . VAL A 1 132 ? 28.001 26.554 13.297 1.00 28.09 ? 132 VAL A O 1 ATOM 1050 C CB . VAL A 1 132 ? 25.553 28.623 12.569 1.00 22.34 ? 132 VAL A CB 1 ATOM 1051 C CG1 . VAL A 1 132 ? 24.145 29.099 12.893 1.00 17.76 ? 132 VAL A CG1 1 ATOM 1052 C CG2 . VAL A 1 132 ? 26.599 29.437 13.316 1.00 28.15 ? 132 VAL A CG2 1 ATOM 1053 N N . SER A 1 133 ? 27.261 26.415 11.181 1.00 20.93 ? 133 SER A N 1 ATOM 1054 C CA . SER A 1 133 ? 28.554 26.072 10.618 1.00 19.39 ? 133 SER A CA 1 ATOM 1055 C C . SER A 1 133 ? 28.594 26.576 9.184 1.00 23.38 ? 133 SER A C 1 ATOM 1056 O O . SER A 1 133 ? 27.573 27.012 8.649 1.00 20.47 ? 133 SER A O 1 ATOM 1057 C CB . SER A 1 133 ? 28.802 24.566 10.683 1.00 17.92 ? 133 SER A CB 1 ATOM 1058 O OG . SER A 1 133 ? 27.844 23.846 9.927 1.00 27.17 ? 133 SER A OG 1 ATOM 1059 N N . GLU A 1 134 ? 29.768 26.516 8.566 1.00 21.66 ? 134 GLU A N 1 ATOM 1060 C CA . GLU A 1 134 ? 29.950 27.049 7.223 1.00 18.65 ? 134 GLU A CA 1 ATOM 1061 C C . GLU A 1 134 ? 31.179 26.456 6.561 1.00 20.23 ? 134 GLU A C 1 ATOM 1062 O O . GLU A 1 134 ? 32.081 25.965 7.236 1.00 25.05 ? 134 GLU A O 1 ATOM 1063 C CB . GLU A 1 134 ? 30.096 28.572 7.254 1.00 11.94 ? 134 GLU A CB 1 ATOM 1064 C CG . GLU A 1 134 ? 31.434 29.019 7.836 1.00 14.64 ? 134 GLU A CG 1 ATOM 1065 C CD . GLU A 1 134 ? 31.514 30.512 8.071 1.00 19.28 ? 134 GLU A CD 1 ATOM 1066 O OE1 . GLU A 1 134 ? 30.823 31.021 8.979 1.00 21.80 ? 134 GLU A OE1 1 ATOM 1067 O OE2 . GLU A 1 134 ? 32.282 31.179 7.347 1.00 25.89 ? 134 GLU A OE2 1 ATOM 1068 N N . THR A 1 135 ? 31.205 26.501 5.235 1.00 16.58 ? 135 THR A N 1 ATOM 1069 C CA . THR A 1 135 ? 32.376 26.081 4.484 1.00 11.87 ? 135 THR A CA 1 ATOM 1070 C C . THR A 1 135 ? 33.252 27.285 4.175 1.00 18.61 ? 135 THR A C 1 ATOM 1071 O O . THR A 1 135 ? 32.835 28.434 4.333 1.00 15.46 ? 135 THR A O 1 ATOM 1072 C CB . THR A 1 135 ? 31.997 25.398 3.165 1.00 11.34 ? 135 THR A CB 1 ATOM 1073 O OG1 . THR A 1 135 ? 31.431 26.369 2.275 1.00 16.64 ? 135 THR A OG1 1 ATOM 1074 C CG2 . THR A 1 135 ? 30.988 24.283 3.412 1.00 12.66 ? 135 THR A CG2 1 ATOM 1075 N N . VAL A 1 136 ? 34.472 27.017 3.733 1.00 21.56 ? 136 VAL A N 1 ATOM 1076 C CA . VAL A 1 136 ? 35.303 28.058 3.158 1.00 17.40 ? 136 VAL A CA 1 ATOM 1077 C C . VAL A 1 136 ? 34.753 28.389 1.776 1.00 15.01 ? 136 VAL A C 1 ATOM 1078 O O . VAL A 1 136 ? 33.739 27.837 1.347 1.00 12.47 ? 136 VAL A O 1 ATOM 1079 C CB . VAL A 1 136 ? 36.784 27.636 3.068 1.00 16.83 ? 136 VAL A CB 1 ATOM 1080 C CG1 . VAL A 1 136 ? 37.349 27.382 4.456 1.00 18.15 ? 136 VAL A CG1 1 ATOM 1081 C CG2 . VAL A 1 136 ? 36.937 26.407 2.185 1.00 11.21 ? 136 VAL A CG2 1 ATOM 1082 N N . PHE A 1 137 ? 35.434 29.275 1.067 1.00 12.78 ? 137 PHE A N 1 ATOM 1083 C CA . PHE A 1 137 ? 35.025 29.621 -0.284 1.00 15.23 ? 137 PHE A CA 1 ATOM 1084 C C . PHE A 1 137 ? 35.403 28.505 -1.244 1.00 14.35 ? 137 PHE A C 1 ATOM 1085 O O . PHE A 1 137 ? 36.548 28.057 -1.281 1.00 20.54 ? 137 PHE A O 1 ATOM 1086 C CB . PHE A 1 137 ? 35.642 30.950 -0.704 1.00 19.04 ? 137 PHE A CB 1 ATOM 1087 C CG . PHE A 1 137 ? 35.171 32.110 0.126 1.00 15.51 ? 137 PHE A CG 1 ATOM 1088 C CD1 . PHE A 1 137 ? 34.001 32.776 -0.190 1.00 8.45 ? 137 PHE A CD1 1 ATOM 1089 C CD2 . PHE A 1 137 ? 35.889 32.516 1.239 1.00 13.96 ? 137 PHE A CD2 1 ATOM 1090 C CE1 . PHE A 1 137 ? 33.565 33.834 0.576 1.00 15.63 ? 137 PHE A CE1 1 ATOM 1091 C CE2 . PHE A 1 137 ? 35.460 33.572 2.012 1.00 20.04 ? 137 PHE A CE2 1 ATOM 1092 C CZ . PHE A 1 137 ? 34.295 34.233 1.682 1.00 24.49 ? 137 PHE A CZ 1 ATOM 1093 N N . LEU A 1 138 ? 34.431 28.058 -2.027 1.00 8.09 ? 138 LEU A N 1 ATOM 1094 C CA . LEU A 1 138 ? 34.652 26.914 -2.885 1.00 8.73 ? 138 LEU A CA 1 ATOM 1095 C C . LEU A 1 138 ? 34.741 27.401 -4.323 1.00 12.16 ? 138 LEU A C 1 ATOM 1096 O O . LEU A 1 138 ? 33.973 28.270 -4.743 1.00 8.85 ? 138 LEU A O 1 ATOM 1097 C CB . LEU A 1 138 ? 33.513 25.903 -2.723 1.00 11.92 ? 138 LEU A CB 1 ATOM 1098 C CG . LEU A 1 138 ? 33.241 25.474 -1.277 1.00 13.16 ? 138 LEU A CG 1 ATOM 1099 C CD1 . LEU A 1 138 ? 31.929 24.715 -1.161 1.00 16.48 ? 138 LEU A CD1 1 ATOM 1100 C CD2 . LEU A 1 138 ? 34.389 24.658 -0.700 1.00 14.45 ? 138 LEU A CD2 1 ATOM 1101 N N . PRO A 1 139 ? 35.682 26.835 -5.086 1.00 9.30 ? 139 PRO A N 1 ATOM 1102 C CA . PRO A 1 139 ? 35.938 27.313 -6.445 1.00 9.58 ? 139 PRO A CA 1 ATOM 1103 C C . PRO A 1 139 ? 34.903 26.859 -7.465 1.00 20.73 ? 139 PRO A C 1 ATOM 1104 O O . PRO A 1 139 ? 34.367 25.755 -7.351 1.00 21.54 ? 139 PRO A O 1 ATOM 1105 C CB . PRO A 1 139 ? 37.304 26.699 -6.767 1.00 8.46 ? 139 PRO A CB 1 ATOM 1106 C CG . PRO A 1 139 ? 37.324 25.433 -5.973 1.00 9.03 ? 139 PRO A CG 1 ATOM 1107 C CD . PRO A 1 139 ? 36.602 25.751 -4.692 1.00 5.87 ? 139 PRO A CD 1 ATOM 1108 N N . ARG A 1 140 ? 34.614 27.720 -8.437 1.00 14.80 ? 140 ARG A N 1 ATOM 1109 C CA . ARG A 1 140 ? 33.769 27.339 -9.562 1.00 9.78 ? 140 ARG A CA 1 ATOM 1110 C C . ARG A 1 140 ? 34.582 27.255 -10.856 1.00 12.97 ? 140 ARG A C 1 ATOM 1111 O O . ARG A 1 140 ? 35.649 27.857 -10.966 1.00 11.52 ? 140 ARG A O 1 ATOM 1112 C CB . ARG A 1 140 ? 32.620 28.330 -9.726 1.00 10.31 ? 140 ARG A CB 1 ATOM 1113 C CG . ARG A 1 140 ? 31.579 28.228 -8.628 1.00 4.63 ? 140 ARG A CG 1 ATOM 1114 C CD . ARG A 1 140 ? 30.586 29.356 -8.742 1.00 18.53 ? 140 ARG A CD 1 ATOM 1115 N NE . ARG A 1 140 ? 30.156 29.492 -10.127 1.00 16.78 ? 140 ARG A NE 1 ATOM 1116 C CZ . ARG A 1 140 ? 29.112 28.854 -10.643 1.00 14.01 ? 140 ARG A CZ 1 ATOM 1117 N NH1 . ARG A 1 140 ? 28.386 28.049 -9.878 1.00 8.71 ? 140 ARG A NH1 1 ATOM 1118 N NH2 . ARG A 1 140 ? 28.790 29.023 -11.918 1.00 10.40 ? 140 ARG A NH2 1 ATOM 1119 N N . GLU A 1 141 ? 34.083 26.502 -11.830 1.00 5.91 ? 141 GLU A N 1 ATOM 1120 C CA . GLU A 1 141 ? 34.788 26.356 -13.099 1.00 14.56 ? 141 GLU A CA 1 ATOM 1121 C C . GLU A 1 141 ? 34.820 27.650 -13.906 1.00 11.41 ? 141 GLU A C 1 ATOM 1122 O O . GLU A 1 141 ? 35.629 27.792 -14.821 1.00 12.13 ? 141 GLU A O 1 ATOM 1123 C CB . GLU A 1 141 ? 34.178 25.217 -13.916 1.00 16.52 ? 141 GLU A CB 1 ATOM 1124 C CG . GLU A 1 141 ? 34.337 23.870 -13.224 1.00 22.63 ? 141 GLU A CG 1 ATOM 1125 C CD . GLU A 1 141 ? 33.831 22.709 -14.054 1.00 31.43 ? 141 GLU A CD 1 ATOM 1126 O OE1 . GLU A 1 141 ? 34.118 22.674 -15.269 1.00 37.00 ? 141 GLU A OE1 1 ATOM 1127 O OE2 . GLU A 1 141 ? 33.160 21.822 -13.485 1.00 37.76 ? 141 GLU A OE2 1 ATOM 1128 N N . ASP A 1 142 ? 33.943 28.594 -13.579 1.00 8.68 ? 142 ASP A N 1 ATOM 1129 C CA . ASP A 1 142 ? 33.984 29.905 -14.216 1.00 7.23 ? 142 ASP A CA 1 ATOM 1130 C C . ASP A 1 142 ? 34.800 30.868 -13.351 1.00 12.53 ? 142 ASP A C 1 ATOM 1131 O O . ASP A 1 142 ? 34.840 32.075 -13.617 1.00 9.93 ? 142 ASP A O 1 ATOM 1132 C CB . ASP A 1 142 ? 32.565 30.435 -14.488 1.00 9.73 ? 142 ASP A CB 1 ATOM 1133 C CG . ASP A 1 142 ? 31.728 30.594 -13.223 1.00 14.03 ? 142 ASP A CG 1 ATOM 1134 O OD1 . ASP A 1 142 ? 32.267 30.464 -12.105 1.00 11.23 ? 142 ASP A OD1 1 ATOM 1135 O OD2 . ASP A 1 142 ? 30.509 30.841 -13.353 1.00 18.18 ? 142 ASP A OD2 1 ATOM 1136 N N . HIS A 1 143 ? 35.409 30.317 -12.297 1.00 5.69 ? 143 HIS A N 1 ATOM 1137 C CA . HIS A 1 143 ? 36.391 31.022 -11.465 1.00 8.10 ? 143 HIS A CA 1 ATOM 1138 C C . HIS A 1 143 ? 35.765 32.083 -10.566 1.00 13.76 ? 143 HIS A C 1 ATOM 1139 O O . HIS A 1 143 ? 36.455 32.936 -10.008 1.00 16.57 ? 143 HIS A O 1 ATOM 1140 C CB . HIS A 1 143 ? 37.511 31.578 -12.345 1.00 9.35 ? 143 HIS A CB 1 ATOM 1141 C CG . HIS A 1 143 ? 37.945 30.608 -13.398 1.00 14.68 ? 143 HIS A CG 1 ATOM 1142 N ND1 . HIS A 1 143 ? 38.444 29.360 -13.084 1.00 14.14 ? 143 HIS A ND1 1 ATOM 1143 C CD2 . HIS A 1 143 ? 37.925 30.677 -14.750 1.00 9.47 ? 143 HIS A CD2 1 ATOM 1144 C CE1 . HIS A 1 143 ? 38.715 28.706 -14.198 1.00 10.48 ? 143 HIS A CE1 1 ATOM 1145 N NE2 . HIS A 1 143 ? 38.416 29.485 -15.223 1.00 11.17 ? 143 HIS A NE2 1 ATOM 1146 N N . LEU A 1 144 ? 34.443 32.006 -10.441 1.00 11.64 ? 144 LEU A N 1 ATOM 1147 C CA . LEU A 1 144 ? 33.723 32.650 -9.350 1.00 8.40 ? 144 LEU A CA 1 ATOM 1148 C C . LEU A 1 144 ? 33.737 31.688 -8.164 1.00 11.44 ? 144 LEU A C 1 ATOM 1149 O O . LEU A 1 144 ? 34.487 30.711 -8.170 1.00 8.95 ? 144 LEU A O 1 ATOM 1150 C CB . LEU A 1 144 ? 32.289 32.981 -9.763 1.00 9.16 ? 144 LEU A CB 1 ATOM 1151 C CG . LEU A 1 144 ? 32.127 33.884 -10.983 1.00 9.97 ? 144 LEU A CG 1 ATOM 1152 C CD1 . LEU A 1 144 ? 30.657 33.983 -11.365 1.00 11.43 ? 144 LEU A CD1 1 ATOM 1153 C CD2 . LEU A 1 144 ? 32.702 35.268 -10.678 1.00 8.01 ? 144 LEU A CD2 1 ATOM 1154 N N . PHE A 1 145 ? 32.926 31.963 -7.148 1.00 13.23 ? 145 PHE A N 1 ATOM 1155 C CA . PHE A 1 145 ? 32.938 31.158 -5.931 1.00 10.68 ? 145 PHE A CA 1 ATOM 1156 C C . PHE A 1 145 ? 31.563 30.706 -5.437 1.00 11.70 ? 145 PHE A C 1 ATOM 1157 O O . PHE A 1 145 ? 30.527 31.251 -5.817 1.00 6.75 ? 145 PHE A O 1 ATOM 1158 C CB . PHE A 1 145 ? 33.644 31.910 -4.795 1.00 11.80 ? 145 PHE A CB 1 ATOM 1159 C CG . PHE A 1 145 ? 35.104 32.180 -5.054 1.00 13.01 ? 145 PHE A CG 1 ATOM 1160 C CD1 . PHE A 1 145 ? 35.516 33.344 -5.687 1.00 9.74 ? 145 PHE A CD1 1 ATOM 1161 C CD2 . PHE A 1 145 ? 36.066 31.259 -4.663 1.00 11.59 ? 145 PHE A CD2 1 ATOM 1162 C CE1 . PHE A 1 145 ? 36.868 33.588 -5.919 1.00 6.57 ? 145 PHE A CE1 1 ATOM 1163 C CE2 . PHE A 1 145 ? 37.417 31.492 -4.891 1.00 9.36 ? 145 PHE A CE2 1 ATOM 1164 C CZ . PHE A 1 145 ? 37.818 32.662 -5.523 1.00 15.63 ? 145 PHE A CZ 1 ATOM 1165 N N . ARG A 1 146 ? 31.600 29.717 -4.547 1.00 10.01 ? 146 ARG A N 1 ATOM 1166 C CA A ARG A 1 146 ? 30.456 29.054 -3.920 0.64 12.55 ? 146 ARG A CA 1 ATOM 1167 C CA B ARG A 1 146 ? 30.374 29.325 -3.880 0.36 10.76 ? 146 ARG A CA 1 ATOM 1168 C C . ARG A 1 146 ? 30.693 29.044 -2.428 1.00 12.90 ? 146 ARG A C 1 ATOM 1169 O O . ARG A 1 146 ? 31.852 28.999 -2.017 1.00 11.70 ? 146 ARG A O 1 ATOM 1170 C CB A ARG A 1 146 ? 30.321 27.586 -4.362 0.64 13.44 ? 146 ARG A CB 1 ATOM 1171 C CB B ARG A 1 146 ? 29.714 28.105 -4.536 0.36 12.03 ? 146 ARG A CB 1 ATOM 1172 C CG A ARG A 1 146 ? 29.805 27.295 -5.743 0.64 16.47 ? 146 ARG A CG 1 ATOM 1173 C CG B ARG A 1 146 ? 30.639 27.172 -5.302 0.36 14.54 ? 146 ARG A CG 1 ATOM 1174 C CD A ARG A 1 146 ? 29.917 25.785 -6.036 0.64 13.53 ? 146 ARG A CD 1 ATOM 1175 C CD B ARG A 1 146 ? 29.860 25.980 -5.859 0.36 15.67 ? 146 ARG A CD 1 ATOM 1176 N NE A ARG A 1 146 ? 31.309 25.333 -6.043 0.64 11.98 ? 146 ARG A NE 1 ATOM 1177 N NE B ARG A 1 146 ? 29.790 24.875 -4.905 0.36 18.79 ? 146 ARG A NE 1 ATOM 1178 C CZ A ARG A 1 146 ? 31.763 24.243 -5.426 0.64 16.32 ? 146 ARG A CZ 1 ATOM 1179 C CZ B ARG A 1 146 ? 29.061 23.776 -5.075 0.36 12.91 ? 146 ARG A CZ 1 ATOM 1180 N NH1 A ARG A 1 146 ? 30.935 23.461 -4.746 0.64 14.43 ? 146 ARG A NH1 1 ATOM 1181 N NH1 B ARG A 1 146 ? 29.067 22.826 -4.150 0.36 11.55 ? 146 ARG A NH1 1 ATOM 1182 N NH2 A ARG A 1 146 ? 33.052 23.931 -5.495 0.64 5.81 ? 146 ARG A NH2 1 ATOM 1183 N NH2 B ARG A 1 146 ? 28.326 23.620 -6.168 0.36 13.37 ? 146 ARG A NH2 1 ATOM 1184 N N . LYS A 1 147 ? 29.636 28.975 -1.630 1.00 13.84 ? 147 LYS A N 1 ATOM 1185 C CA . LYS A 1 147 ? 29.813 28.837 -0.196 1.00 12.84 ? 147 LYS A CA 1 ATOM 1186 C C . LYS A 1 147 ? 28.533 28.282 0.424 1.00 10.30 ? 147 LYS A C 1 ATOM 1187 O O . LYS A 1 147 ? 27.436 28.549 -0.062 1.00 15.99 ? 147 LYS A O 1 ATOM 1188 C CB . LYS A 1 147 ? 30.175 30.205 0.401 1.00 8.49 ? 147 LYS A CB 1 ATOM 1189 C CG . LYS A 1 147 ? 30.825 30.205 1.773 1.00 11.84 ? 147 LYS A CG 1 ATOM 1190 C CD . LYS A 1 147 ? 31.076 31.648 2.222 1.00 18.46 ? 147 LYS A CD 1 ATOM 1191 C CE . LYS A 1 147 ? 32.101 31.739 3.348 1.00 22.16 ? 147 LYS A CE 1 ATOM 1192 N NZ . LYS A 1 147 ? 31.652 31.078 4.598 1.00 20.18 ? 147 LYS A NZ 1 ATOM 1193 N N . PHE A 1 148 ? 28.683 27.530 1.511 1.00 11.95 ? 148 PHE A N 1 ATOM 1194 C CA . PHE A 1 148 ? 27.534 26.967 2.213 1.00 8.14 ? 148 PHE A CA 1 ATOM 1195 C C . PHE A 1 148 ? 27.501 27.401 3.662 1.00 13.98 ? 148 PHE A C 1 ATOM 1196 O O . PHE A 1 148 ? 28.534 27.456 4.330 1.00 20.24 ? 148 PHE A O 1 ATOM 1197 C CB . PHE A 1 148 ? 27.531 25.436 2.171 1.00 7.87 ? 148 PHE A CB 1 ATOM 1198 C CG . PHE A 1 148 ? 27.404 24.853 0.794 1.00 12.75 ? 148 PHE A CG 1 ATOM 1199 C CD1 . PHE A 1 148 ? 28.504 24.736 -0.037 1.00 10.17 ? 148 PHE A CD1 1 ATOM 1200 C CD2 . PHE A 1 148 ? 26.175 24.406 0.339 1.00 12.84 ? 148 PHE A CD2 1 ATOM 1201 C CE1 . PHE A 1 148 ? 28.379 24.186 -1.302 1.00 12.30 ? 148 PHE A CE1 1 ATOM 1202 C CE2 . PHE A 1 148 ? 26.043 23.858 -0.923 1.00 18.26 ? 148 PHE A CE2 1 ATOM 1203 C CZ . PHE A 1 148 ? 27.146 23.746 -1.745 1.00 14.04 ? 148 PHE A CZ 1 ATOM 1204 N N . HIS A 1 149 ? 26.307 27.734 4.140 1.00 10.71 ? 149 HIS A N 1 ATOM 1205 C CA . HIS A 1 149 ? 26.118 27.977 5.559 1.00 9.01 ? 149 HIS A CA 1 ATOM 1206 C C . HIS A 1 149 ? 25.030 27.039 6.067 1.00 13.23 ? 149 HIS A C 1 ATOM 1207 O O . HIS A 1 149 ? 24.077 26.741 5.345 1.00 17.35 ? 149 HIS A O 1 ATOM 1208 C CB . HIS A 1 149 ? 25.792 29.447 5.806 1.00 15.95 ? 149 HIS A CB 1 ATOM 1209 C CG . HIS A 1 149 ? 27.001 30.331 5.779 1.00 17.33 ? 149 HIS A CG 1 ATOM 1210 N ND1 . HIS A 1 149 ? 27.443 31.025 6.885 1.00 17.44 ? 149 HIS A ND1 1 ATOM 1211 C CD2 . HIS A 1 149 ? 27.884 30.605 4.788 1.00 19.29 ? 149 HIS A CD2 1 ATOM 1212 C CE1 . HIS A 1 149 ? 28.536 31.698 6.574 1.00 19.95 ? 149 HIS A CE1 1 ATOM 1213 N NE2 . HIS A 1 149 ? 28.824 31.462 5.306 1.00 17.91 ? 149 HIS A NE2 1 ATOM 1214 N N . TYR A 1 150 ? 25.163 26.576 7.306 1.00 15.23 ? 150 TYR A N 1 ATOM 1215 C CA . TYR A 1 150 ? 24.259 25.556 7.823 1.00 16.95 ? 150 TYR A CA 1 ATOM 1216 C C . TYR A 1 150 ? 23.649 25.945 9.161 1.00 20.93 ? 150 TYR A C 1 ATOM 1217 O O . TYR A 1 150 ? 24.297 26.563 10.001 1.00 19.47 ? 150 TYR A O 1 ATOM 1218 C CB . TYR A 1 150 ? 24.988 24.216 7.975 1.00 16.03 ? 150 TYR A CB 1 ATOM 1219 C CG . TYR A 1 150 ? 25.638 23.685 6.710 1.00 13.00 ? 150 TYR A CG 1 ATOM 1220 C CD1 . TYR A 1 150 ? 24.896 22.980 5.768 1.00 10.97 ? 150 TYR A CD1 1 ATOM 1221 C CD2 . TYR A 1 150 ? 26.997 23.861 6.473 1.00 10.44 ? 150 TYR A CD2 1 ATOM 1222 C CE1 . TYR A 1 150 ? 25.485 22.481 4.619 1.00 13.53 ? 150 TYR A CE1 1 ATOM 1223 C CE2 . TYR A 1 150 ? 27.598 23.363 5.321 1.00 9.40 ? 150 TYR A CE2 1 ATOM 1224 C CZ . TYR A 1 150 ? 26.830 22.673 4.397 1.00 13.14 ? 150 TYR A CZ 1 ATOM 1225 O OH . TYR A 1 150 ? 27.399 22.168 3.246 1.00 10.62 ? 150 TYR A OH 1 ATOM 1226 N N . LEU A 1 151 ? 22.384 25.582 9.340 1.00 20.93 ? 151 LEU A N 1 ATOM 1227 C CA . LEU A 1 151 ? 21.684 25.810 10.593 1.00 21.64 ? 151 LEU A CA 1 ATOM 1228 C C . LEU A 1 151 ? 20.812 24.626 10.985 1.00 17.19 ? 151 LEU A C 1 ATOM 1229 O O . LEU A 1 151 ? 19.749 24.422 10.403 1.00 17.33 ? 151 LEU A O 1 ATOM 1230 C CB . LEU A 1 151 ? 20.836 27.084 10.512 1.00 18.36 ? 151 LEU A CB 1 ATOM 1231 C CG . LEU A 1 151 ? 19.935 27.372 11.715 1.00 20.59 ? 151 LEU A CG 1 ATOM 1232 C CD1 . LEU A 1 151 ? 20.747 27.509 12.991 1.00 21.02 ? 151 LEU A CD1 1 ATOM 1233 C CD2 . LEU A 1 151 ? 19.116 28.630 11.468 1.00 19.53 ? 151 LEU A CD2 1 ATOM 1234 N N . PRO A 1 152 ? 21.271 23.828 11.960 1.00 19.10 ? 152 PRO A N 1 ATOM 1235 C CA . PRO A 1 152 ? 20.398 22.793 12.512 1.00 17.08 ? 152 PRO A CA 1 ATOM 1236 C C . PRO A 1 152 ? 19.197 23.456 13.163 1.00 17.19 ? 152 PRO A C 1 ATOM 1237 O O . PRO A 1 152 ? 19.367 24.481 13.819 1.00 23.49 ? 152 PRO A O 1 ATOM 1238 C CB . PRO A 1 152 ? 21.280 22.106 13.557 1.00 26.50 ? 152 PRO A CB 1 ATOM 1239 C CG . PRO A 1 152 ? 22.674 22.361 13.094 1.00 28.64 ? 152 PRO A CG 1 ATOM 1240 C CD . PRO A 1 152 ? 22.642 23.736 12.488 1.00 22.45 ? 152 PRO A CD 1 ATOM 1241 N N . PHE A 1 153 ? 18.006 22.901 12.987 1.00 18.51 ? 153 PHE A N 1 ATOM 1242 C CA . PHE A 1 153 ? 16.829 23.525 13.570 1.00 21.22 ? 153 PHE A CA 1 ATOM 1243 C C . PHE A 1 153 ? 15.740 22.491 13.791 1.00 23.82 ? 153 PHE A C 1 ATOM 1244 O O . PHE A 1 153 ? 15.761 21.407 13.208 1.00 22.91 ? 153 PHE A O 1 ATOM 1245 C CB . PHE A 1 153 ? 16.308 24.671 12.687 1.00 17.90 ? 153 PHE A CB 1 ATOM 1246 C CG . PHE A 1 153 ? 15.506 24.219 11.492 1.00 20.52 ? 153 PHE A CG 1 ATOM 1247 C CD1 . PHE A 1 153 ? 16.119 23.634 10.394 1.00 20.86 ? 153 PHE A CD1 1 ATOM 1248 C CD2 . PHE A 1 153 ? 14.131 24.407 11.461 1.00 19.96 ? 153 PHE A CD2 1 ATOM 1249 C CE1 . PHE A 1 153 ? 15.373 23.227 9.291 1.00 17.79 ? 153 PHE A CE1 1 ATOM 1250 C CE2 . PHE A 1 153 ? 13.381 24.009 10.367 1.00 22.87 ? 153 PHE A CE2 1 ATOM 1251 C CZ . PHE A 1 153 ? 14.003 23.416 9.278 1.00 21.11 ? 153 PHE A CZ 1 ATOM 1252 N N . LEU A 1 154 ? 14.800 22.841 14.658 1.00 26.23 ? 154 LEU A N 1 ATOM 1253 C CA . LEU A 1 154 ? 13.646 22.006 14.936 1.00 25.85 ? 154 LEU A CA 1 ATOM 1254 C C . LEU A 1 154 ? 12.406 22.639 14.320 1.00 23.46 ? 154 LEU A C 1 ATOM 1255 O O . LEU A 1 154 ? 11.924 23.658 14.806 1.00 24.43 ? 154 LEU A O 1 ATOM 1256 C CB . LEU A 1 154 ? 13.472 21.823 16.443 1.00 26.96 ? 154 LEU A CB 1 ATOM 1257 C CG . LEU A 1 154 ? 12.573 20.681 16.908 1.00 36.42 ? 154 LEU A CG 1 ATOM 1258 C CD1 . LEU A 1 154 ? 13.193 19.345 16.539 1.00 33.85 ? 154 LEU A CD1 1 ATOM 1259 C CD2 . LEU A 1 154 ? 12.324 20.767 18.407 1.00 37.39 ? 154 LEU A CD2 1 ATOM 1260 N N . PRO A 1 155 ? 11.905 22.052 13.225 1.00 25.86 ? 155 PRO A N 1 ATOM 1261 C CA . PRO A 1 155 ? 10.795 22.652 12.479 1.00 24.51 ? 155 PRO A CA 1 ATOM 1262 C C . PRO A 1 155 ? 9.545 22.876 13.323 1.00 26.52 ? 155 PRO A C 1 ATOM 1263 O O . PRO A 1 155 ? 9.148 22.009 14.100 1.00 28.50 ? 155 PRO A O 1 ATOM 1264 C CB . PRO A 1 155 ? 10.521 21.622 11.381 1.00 23.80 ? 155 PRO A CB 1 ATOM 1265 C CG . PRO A 1 155 ? 11.819 20.914 11.204 1.00 27.62 ? 155 PRO A CG 1 ATOM 1266 C CD . PRO A 1 155 ? 12.410 20.832 12.579 1.00 30.34 ? 155 PRO A CD 1 ATOM 1267 N N . SER A 1 156 ? 8.938 24.045 13.154 1.00 28.94 ? 156 SER A N 1 ATOM 1268 C CA . SER A 1 156 ? 7.722 24.410 13.865 1.00 37.60 ? 156 SER A CA 1 ATOM 1269 C C . SER A 1 156 ? 6.927 25.406 13.030 1.00 38.18 ? 156 SER A C 1 ATOM 1270 O O . SER A 1 156 ? 7.480 26.063 12.149 1.00 36.68 ? 156 SER A O 1 ATOM 1271 C CB . SER A 1 156 ? 8.046 25.003 15.237 1.00 40.29 ? 156 SER A CB 1 ATOM 1272 O OG . SER A 1 156 ? 8.728 26.237 15.107 1.00 45.19 ? 156 SER A OG 1 ATOM 1273 N N . THR A 1 157 ? 5.633 25.516 13.305 1.00 35.42 ? 157 THR A N 1 ATOM 1274 C CA . THR A 1 157 ? 4.785 26.473 12.604 1.00 36.68 ? 157 THR A CA 1 ATOM 1275 C C . THR A 1 157 ? 5.024 27.904 13.084 1.00 36.73 ? 157 THR A C 1 ATOM 1276 O O . THR A 1 157 ? 4.571 28.860 12.453 1.00 40.19 ? 157 THR A O 1 ATOM 1277 C CB . THR A 1 157 ? 3.294 26.131 12.780 1.00 40.48 ? 157 THR A CB 1 ATOM 1278 O OG1 . THR A 1 157 ? 2.981 26.071 14.177 1.00 44.50 ? 157 THR A OG1 1 ATOM 1279 C CG2 . THR A 1 157 ? 2.974 24.791 12.141 1.00 37.94 ? 157 THR A CG2 1 ATOM 1280 N N . GLU A 1 158 ? 5.737 28.048 14.197 1.00 41.09 ? 158 GLU A N 1 ATOM 1281 C CA . GLU A 1 158 ? 5.886 29.350 14.843 1.00 49.13 ? 158 GLU A CA 1 ATOM 1282 C C . GLU A 1 158 ? 7.141 30.118 14.426 1.00 50.33 ? 158 GLU A C 1 ATOM 1283 O O . GLU A 1 158 ? 7.257 31.314 14.695 1.00 53.87 ? 158 GLU A O 1 ATOM 1284 C CB . GLU A 1 158 ? 5.886 29.185 16.368 1.00 55.44 ? 158 GLU A CB 1 ATOM 1285 C CG . GLU A 1 158 ? 4.612 28.596 16.979 1.00 65.93 ? 158 GLU A CG 1 ATOM 1286 C CD . GLU A 1 158 ? 3.324 29.290 16.548 1.00 77.72 ? 158 GLU A CD 1 ATOM 1287 O OE1 . GLU A 1 158 ? 3.366 30.446 16.072 1.00 75.48 ? 158 GLU A OE1 1 ATOM 1288 O OE2 . GLU A 1 158 ? 2.252 28.669 16.706 1.00 89.95 ? 158 GLU A OE2 1 ATOM 1289 N N . ASP A 1 159 ? 8.071 29.448 13.758 1.00 40.34 ? 159 ASP A N 1 ATOM 1290 C CA . ASP A 1 159 ? 9.323 30.095 13.387 1.00 34.29 ? 159 ASP A CA 1 ATOM 1291 C C . ASP A 1 159 ? 9.475 30.271 11.886 1.00 38.12 ? 159 ASP A C 1 ATOM 1292 O O . ASP A 1 159 ? 9.166 29.372 11.101 1.00 41.59 ? 159 ASP A O 1 ATOM 1293 C CB . ASP A 1 159 ? 10.522 29.305 13.921 1.00 31.48 ? 159 ASP A CB 1 ATOM 1294 C CG . ASP A 1 159 ? 10.570 29.259 15.433 1.00 40.26 ? 159 ASP A CG 1 ATOM 1295 O OD1 . ASP A 1 159 ? 10.099 30.221 16.078 1.00 41.49 ? 159 ASP A OD1 1 ATOM 1296 O OD2 . ASP A 1 159 ? 11.098 28.268 15.976 1.00 43.27 ? 159 ASP A OD2 1 ATOM 1297 N N . VAL A 1 160 ? 9.980 31.438 11.502 1.00 32.38 ? 160 VAL A N 1 ATOM 1298 C CA . VAL A 1 160 ? 10.414 31.672 10.137 1.00 19.04 ? 160 VAL A CA 1 ATOM 1299 C C . VAL A 1 160 ? 11.903 31.954 10.155 1.00 27.55 ? 160 VAL A C 1 ATOM 1300 O O . VAL A 1 160 ? 12.452 32.424 11.156 1.00 21.20 ? 160 VAL A O 1 ATOM 1301 C CB . VAL A 1 160 ? 9.669 32.844 9.464 1.00 19.48 ? 160 VAL A CB 1 ATOM 1302 C CG1 . VAL A 1 160 ? 8.172 32.605 9.491 1.00 23.92 ? 160 VAL A CG1 1 ATOM 1303 C CG2 . VAL A 1 160 ? 10.019 34.169 10.127 1.00 20.28 ? 160 VAL A CG2 1 ATOM 1304 N N . TYR A 1 161 ? 12.555 31.665 9.039 1.00 20.98 ? 161 TYR A N 1 ATOM 1305 C CA . TYR A 1 161 ? 13.990 31.853 8.928 1.00 18.73 ? 161 TYR A CA 1 ATOM 1306 C C . TYR A 1 161 ? 14.329 32.669 7.694 1.00 17.60 ? 161 TYR A C 1 ATOM 1307 O O . TYR A 1 161 ? 13.577 32.688 6.722 1.00 15.35 ? 161 TYR A O 1 ATOM 1308 C CB . TYR A 1 161 ? 14.704 30.497 8.887 1.00 16.43 ? 161 TYR A CB 1 ATOM 1309 C CG . TYR A 1 161 ? 14.574 29.703 10.169 1.00 17.93 ? 161 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 161 ? 13.481 28.880 10.390 1.00 17.16 ? 161 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 161 ? 15.556 29.767 11.150 1.00 25.68 ? 161 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 161 ? 13.359 28.151 11.559 1.00 23.39 ? 161 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 161 ? 15.446 29.041 12.320 1.00 24.91 ? 161 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 161 ? 14.346 28.236 12.520 1.00 26.38 ? 161 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 161 ? 14.233 27.515 13.687 1.00 28.90 ? 161 TYR A OH 1 ATOM 1316 N N . ASP A 1 162 ? 15.473 33.339 7.747 1.00 15.52 ? 162 ASP A N 1 ATOM 1317 C CA . ASP A 1 162 ? 16.019 34.019 6.587 1.00 16.13 ? 162 ASP A CA 1 ATOM 1318 C C . ASP A 1 162 ? 17.525 33.829 6.579 1.00 15.52 ? 162 ASP A C 1 ATOM 1319 O O . ASP A 1 162 ? 18.159 33.806 7.632 1.00 15.80 ? 162 ASP A O 1 ATOM 1320 C CB . ASP A 1 162 ? 15.693 35.516 6.616 1.00 25.85 ? 162 ASP A CB 1 ATOM 1321 C CG . ASP A 1 162 ? 14.210 35.797 6.517 1.00 24.60 ? 162 ASP A CG 1 ATOM 1322 O OD1 . ASP A 1 162 ? 13.675 35.792 5.389 1.00 29.69 ? 162 ASP A OD1 1 ATOM 1323 O OD2 . ASP A 1 162 ? 13.584 36.042 7.570 1.00 21.11 ? 162 ASP A OD2 1 ATOM 1324 N N . CYS A 1 163 ? 18.100 33.682 5.393 1.00 13.69 ? 163 CYS A N 1 ATOM 1325 C CA . CYS A 1 163 ? 19.544 33.791 5.259 1.00 19.61 ? 163 CYS A CA 1 ATOM 1326 C C . CYS A 1 163 ? 19.861 35.166 4.695 1.00 20.18 ? 163 CYS A C 1 ATOM 1327 O O . CYS A 1 163 ? 19.412 35.517 3.606 1.00 17.31 ? 163 CYS A O 1 ATOM 1328 C CB . CYS A 1 163 ? 20.102 32.688 4.361 1.00 15.71 ? 163 CYS A CB 1 ATOM 1329 S SG . CYS A 1 163 ? 21.884 32.765 4.144 1.00 21.62 ? 163 CYS A SG 1 ATOM 1330 N N . ARG A 1 164 ? 20.638 35.945 5.435 1.00 21.15 ? 164 ARG A N 1 ATOM 1331 C CA . ARG A 1 164 ? 20.970 37.288 4.985 1.00 21.35 ? 164 ARG A CA 1 ATOM 1332 C C . ARG A 1 164 ? 22.403 37.363 4.503 1.00 22.53 ? 164 ARG A C 1 ATOM 1333 O O . ARG A 1 164 ? 23.339 37.061 5.243 1.00 14.93 ? 164 ARG A O 1 ATOM 1334 C CB . ARG A 1 164 ? 20.770 38.308 6.102 1.00 15.47 ? 164 ARG A CB 1 ATOM 1335 C CG . ARG A 1 164 ? 21.082 39.733 5.657 1.00 15.94 ? 164 ARG A CG 1 ATOM 1336 C CD . ARG A 1 164 ? 20.860 40.702 6.791 1.00 20.72 ? 164 ARG A CD 1 ATOM 1337 N NE . ARG A 1 164 ? 21.873 40.489 7.821 1.00 24.40 ? 164 ARG A NE 1 ATOM 1338 C CZ . ARG A 1 164 ? 21.694 40.738 9.112 1.00 24.28 ? 164 ARG A CZ 1 ATOM 1339 N NH1 . ARG A 1 164 ? 20.532 41.209 9.541 1.00 22.53 ? 164 ARG A NH1 1 ATOM 1340 N NH2 . ARG A 1 164 ? 22.676 40.513 9.974 1.00 26.45 ? 164 ARG A NH2 1 ATOM 1341 N N . VAL A 1 165 ? 22.571 37.785 3.258 1.00 18.32 ? 165 VAL A N 1 ATOM 1342 C CA . VAL A 1 165 ? 23.887 37.797 2.647 1.00 18.19 ? 165 VAL A CA 1 ATOM 1343 C C . VAL A 1 165 ? 24.302 39.200 2.221 1.00 16.62 ? 165 VAL A C 1 ATOM 1344 O O . VAL A 1 165 ? 23.575 39.868 1.487 1.00 21.81 ? 165 VAL A O 1 ATOM 1345 C CB . VAL A 1 165 ? 23.913 36.844 1.434 1.00 13.78 ? 165 VAL A CB 1 ATOM 1346 C CG1 . VAL A 1 165 ? 25.198 36.985 0.643 1.00 14.16 ? 165 VAL A CG1 1 ATOM 1347 C CG2 . VAL A 1 165 ? 23.693 35.406 1.895 1.00 13.53 ? 165 VAL A CG2 1 ATOM 1348 N N . GLU A 1 166 ? 25.465 39.645 2.692 1.00 18.48 ? 166 GLU A N 1 ATOM 1349 C CA . GLU A 1 166 ? 26.028 40.925 2.269 1.00 16.12 ? 166 GLU A CA 1 ATOM 1350 C C . GLU A 1 166 ? 27.255 40.695 1.398 1.00 23.74 ? 166 GLU A C 1 ATOM 1351 O O . GLU A 1 166 ? 28.125 39.895 1.732 1.00 17.99 ? 166 GLU A O 1 ATOM 1352 C CB . GLU A 1 166 ? 26.386 41.835 3.447 1.00 22.30 ? 166 GLU A CB 1 ATOM 1353 C CG . GLU A 1 166 ? 25.303 42.008 4.497 1.00 40.43 ? 166 GLU A CG 1 ATOM 1354 C CD . GLU A 1 166 ? 25.838 42.623 5.782 1.00 51.02 ? 166 GLU A CD 1 ATOM 1355 O OE1 . GLU A 1 166 ? 27.073 42.669 5.957 1.00 45.97 ? 166 GLU A OE1 1 ATOM 1356 O OE2 . GLU A 1 166 ? 25.023 43.073 6.613 1.00 62.78 ? 166 GLU A OE2 1 ATOM 1357 N N . HIS A 1 167 ? 27.321 41.427 0.292 1.00 20.47 ? 167 HIS A N 1 ATOM 1358 C CA . HIS A 1 167 ? 28.438 41.350 -0.635 1.00 14.73 ? 167 HIS A CA 1 ATOM 1359 C C . HIS A 1 167 ? 28.540 42.701 -1.316 1.00 12.57 ? 167 HIS A C 1 ATOM 1360 O O . HIS A 1 167 ? 27.528 43.350 -1.561 1.00 20.38 ? 167 HIS A O 1 ATOM 1361 C CB . HIS A 1 167 ? 28.209 40.230 -1.656 1.00 11.78 ? 167 HIS A CB 1 ATOM 1362 C CG . HIS A 1 167 ? 29.374 39.972 -2.564 1.00 18.49 ? 167 HIS A CG 1 ATOM 1363 N ND1 . HIS A 1 167 ? 29.549 40.640 -3.759 1.00 17.74 ? 167 HIS A ND1 1 ATOM 1364 C CD2 . HIS A 1 167 ? 30.399 39.092 -2.472 1.00 13.98 ? 167 HIS A CD2 1 ATOM 1365 C CE1 . HIS A 1 167 ? 30.645 40.198 -4.352 1.00 16.20 ? 167 HIS A CE1 1 ATOM 1366 N NE2 . HIS A 1 167 ? 31.179 39.259 -3.592 1.00 22.55 ? 167 HIS A NE2 1 ATOM 1367 N N . TRP A 1 168 ? 29.759 43.116 -1.638 1.00 14.44 ? 168 TRP A N 1 ATOM 1368 C CA . TRP A 1 168 ? 29.994 44.441 -2.214 1.00 17.35 ? 168 TRP A CA 1 ATOM 1369 C C . TRP A 1 168 ? 29.296 44.634 -3.561 1.00 20.19 ? 168 TRP A C 1 ATOM 1370 O O . TRP A 1 168 ? 29.072 45.764 -3.987 1.00 18.90 ? 168 TRP A O 1 ATOM 1371 C CB . TRP A 1 168 ? 31.498 44.706 -2.339 1.00 12.92 ? 168 TRP A CB 1 ATOM 1372 C CG . TRP A 1 168 ? 32.164 44.734 -0.995 1.00 16.01 ? 168 TRP A CG 1 ATOM 1373 C CD1 . TRP A 1 168 ? 31.688 45.334 0.134 1.00 18.13 ? 168 TRP A CD1 1 ATOM 1374 C CD2 . TRP A 1 168 ? 33.414 44.132 -0.632 1.00 18.41 ? 168 TRP A CD2 1 ATOM 1375 N NE1 . TRP A 1 168 ? 32.560 45.147 1.175 1.00 21.30 ? 168 TRP A NE1 1 ATOM 1376 C CE2 . TRP A 1 168 ? 33.630 44.415 0.732 1.00 25.04 ? 168 TRP A CE2 1 ATOM 1377 C CE3 . TRP A 1 168 ? 34.372 43.386 -1.327 1.00 12.27 ? 168 TRP A CE3 1 ATOM 1378 C CZ2 . TRP A 1 168 ? 34.761 43.973 1.418 1.00 21.38 ? 168 TRP A CZ2 1 ATOM 1379 C CZ3 . TRP A 1 168 ? 35.498 42.951 -0.644 1.00 19.30 ? 168 TRP A CZ3 1 ATOM 1380 C CH2 . TRP A 1 168 ? 35.681 43.246 0.716 1.00 17.58 ? 168 TRP A CH2 1 ATOM 1381 N N . GLY A 1 169 ? 28.939 43.533 -4.215 1.00 13.76 ? 169 GLY A N 1 ATOM 1382 C CA . GLY A 1 169 ? 28.226 43.602 -5.478 1.00 14.92 ? 169 GLY A CA 1 ATOM 1383 C C . GLY A 1 169 ? 26.735 43.831 -5.288 1.00 15.96 ? 169 GLY A C 1 ATOM 1384 O O . GLY A 1 169 ? 26.014 44.059 -6.255 1.00 21.71 ? 169 GLY A O 1 ATOM 1385 N N . LEU A 1 170 ? 26.270 43.778 -4.042 1.00 20.56 ? 170 LEU A N 1 ATOM 1386 C CA . LEU A 1 170 ? 24.858 44.014 -3.736 1.00 18.71 ? 170 LEU A CA 1 ATOM 1387 C C . LEU A 1 170 ? 24.654 45.439 -3.235 1.00 25.79 ? 170 LEU A C 1 ATOM 1388 O O . LEU A 1 170 ? 25.457 45.946 -2.454 1.00 29.24 ? 170 LEU A O 1 ATOM 1389 C CB . LEU A 1 170 ? 24.357 43.018 -2.686 1.00 15.84 ? 170 LEU A CB 1 ATOM 1390 C CG . LEU A 1 170 ? 24.329 41.542 -3.080 1.00 26.26 ? 170 LEU A CG 1 ATOM 1391 C CD1 . LEU A 1 170 ? 24.110 40.678 -1.844 1.00 16.08 ? 170 LEU A CD1 1 ATOM 1392 C CD2 . LEU A 1 170 ? 23.247 41.275 -4.139 1.00 16.55 ? 170 LEU A CD2 1 ATOM 1393 N N . ASP A 1 171 ? 23.579 46.080 -3.684 1.00 31.49 ? 171 ASP A N 1 ATOM 1394 C CA . ASP A 1 171 ? 23.246 47.427 -3.228 1.00 38.52 ? 171 ASP A CA 1 ATOM 1395 C C . ASP A 1 171 ? 22.677 47.408 -1.817 1.00 39.42 ? 171 ASP A C 1 ATOM 1396 O O . ASP A 1 171 ? 22.880 48.338 -1.037 1.00 42.75 ? 171 ASP A O 1 ATOM 1397 C CB . ASP A 1 171 ? 22.244 48.072 -4.183 1.00 42.29 ? 171 ASP A CB 1 ATOM 1398 C CG . ASP A 1 171 ? 22.878 48.501 -5.487 1.00 56.26 ? 171 ASP A CG 1 ATOM 1399 O OD1 . ASP A 1 171 ? 24.091 48.803 -5.489 1.00 60.90 ? 171 ASP A OD1 1 ATOM 1400 O OD2 . ASP A 1 171 ? 22.166 48.519 -6.513 1.00 63.81 ? 171 ASP A OD2 1 ATOM 1401 N N . GLU A 1 172 ? 21.973 46.328 -1.499 1.00 31.90 ? 172 GLU A N 1 ATOM 1402 C CA . GLU A 1 172 ? 21.409 46.109 -0.175 1.00 30.11 ? 172 GLU A CA 1 ATOM 1403 C C . GLU A 1 172 ? 21.555 44.631 0.155 1.00 25.11 ? 172 GLU A C 1 ATOM 1404 O O . GLU A 1 172 ? 21.718 43.818 -0.753 1.00 22.39 ? 172 GLU A O 1 ATOM 1405 C CB . GLU A 1 172 ? 19.948 46.564 -0.133 1.00 46.10 ? 172 GLU A CB 1 ATOM 1406 C CG . GLU A 1 172 ? 19.075 45.945 -1.211 1.00 62.92 ? 172 GLU A CG 1 ATOM 1407 C CD . GLU A 1 172 ? 17.660 46.487 -1.199 1.00 80.52 ? 172 GLU A CD 1 ATOM 1408 O OE1 . GLU A 1 172 ? 17.457 47.614 -0.700 1.00 89.07 ? 172 GLU A OE1 1 ATOM 1409 O OE2 . GLU A 1 172 ? 16.752 45.789 -1.698 1.00 83.93 ? 172 GLU A OE2 1 ATOM 1410 N N . PRO A 1 173 ? 21.495 44.268 1.446 1.00 24.66 ? 173 PRO A N 1 ATOM 1411 C CA . PRO A 1 173 ? 21.611 42.839 1.758 1.00 24.13 ? 173 PRO A CA 1 ATOM 1412 C C . PRO A 1 173 ? 20.488 42.000 1.153 1.00 22.97 ? 173 PRO A C 1 ATOM 1413 O O . PRO A 1 173 ? 19.346 42.444 1.021 1.00 31.42 ? 173 PRO A O 1 ATOM 1414 C CB . PRO A 1 173 ? 21.562 42.806 3.292 1.00 24.41 ? 173 PRO A CB 1 ATOM 1415 C CG . PRO A 1 173 ? 20.986 44.127 3.695 1.00 27.40 ? 173 PRO A CG 1 ATOM 1416 C CD . PRO A 1 173 ? 21.443 45.097 2.661 1.00 24.63 ? 173 PRO A CD 1 ATOM 1417 N N . LEU A 1 174 ? 20.846 40.782 0.767 1.00 22.04 ? 174 LEU A N 1 ATOM 1418 C CA . LEU A 1 174 ? 19.910 39.850 0.159 1.00 19.59 ? 174 LEU A CA 1 ATOM 1419 C C . LEU A 1 174 ? 19.369 38.891 1.215 1.00 24.91 ? 174 LEU A C 1 ATOM 1420 O O . LEU A 1 174 ? 20.135 38.216 1.899 1.00 20.98 ? 174 LEU A O 1 ATOM 1421 C CB . LEU A 1 174 ? 20.605 39.082 -0.970 1.00 20.30 ? 174 LEU A CB 1 ATOM 1422 C CG . LEU A 1 174 ? 19.810 38.229 -1.957 1.00 21.27 ? 174 LEU A CG 1 ATOM 1423 C CD1 . LEU A 1 174 ? 18.643 39.014 -2.518 1.00 24.31 ? 174 LEU A CD1 1 ATOM 1424 C CD2 . LEU A 1 174 ? 20.725 37.774 -3.079 1.00 19.99 ? 174 LEU A CD2 1 ATOM 1425 N N . LEU A 1 175 ? 18.048 38.847 1.352 1.00 21.71 ? 175 LEU A N 1 ATOM 1426 C CA . LEU A 1 175 ? 17.404 37.917 2.274 1.00 22.71 ? 175 LEU A CA 1 ATOM 1427 C C . LEU A 1 175 ? 16.636 36.834 1.535 1.00 17.56 ? 175 LEU A C 1 ATOM 1428 O O . LEU A 1 175 ? 15.785 37.129 0.698 1.00 20.40 ? 175 LEU A O 1 ATOM 1429 C CB . LEU A 1 175 ? 16.455 38.650 3.229 1.00 20.01 ? 175 LEU A CB 1 ATOM 1430 C CG . LEU A 1 175 ? 17.041 39.212 4.526 1.00 21.89 ? 175 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 175 ? 17.846 40.481 4.265 1.00 26.80 ? 175 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 175 ? 15.947 39.458 5.562 1.00 23.18 ? 175 LEU A CD2 1 ATOM 1433 N N . LYS A 1 176 ? 16.944 35.580 1.839 1.00 20.32 ? 176 LYS A N 1 ATOM 1434 C CA . LYS A 1 176 ? 16.187 34.466 1.285 1.00 18.51 ? 176 LYS A CA 1 ATOM 1435 C C . LYS A 1 176 ? 15.448 33.763 2.411 1.00 22.12 ? 176 LYS A C 1 ATOM 1436 O O . LYS A 1 176 ? 16.041 33.379 3.420 1.00 20.44 ? 176 LYS A O 1 ATOM 1437 C CB . LYS A 1 176 ? 17.096 33.496 0.535 1.00 24.72 ? 176 LYS A CB 1 ATOM 1438 C CG . LYS A 1 176 ? 17.707 34.075 -0.728 1.00 29.22 ? 176 LYS A CG 1 ATOM 1439 C CD . LYS A 1 176 ? 16.643 34.418 -1.761 1.00 27.88 ? 176 LYS A CD 1 ATOM 1440 C CE . LYS A 1 176 ? 17.243 35.170 -2.942 1.00 31.86 ? 176 LYS A CE 1 ATOM 1441 N NZ . LYS A 1 176 ? 16.272 35.350 -4.060 1.00 28.45 ? 176 LYS A NZ 1 ATOM 1442 N N . HIS A 1 177 ? 14.147 33.592 2.215 1.00 23.08 ? 177 HIS A N 1 ATOM 1443 C CA . HIS A 1 177 ? 13.239 33.181 3.274 1.00 24.03 ? 177 HIS A CA 1 ATOM 1444 C C . HIS A 1 177 ? 12.987 31.683 3.270 1.00 28.39 ? 177 HIS A C 1 ATOM 1445 O O . HIS A 1 177 ? 13.031 31.041 2.223 1.00 30.07 ? 177 HIS A O 1 ATOM 1446 C CB . HIS A 1 177 ? 11.917 33.933 3.109 1.00 20.85 ? 177 HIS A CB 1 ATOM 1447 C CG . HIS A 1 177 ? 11.008 33.841 4.293 1.00 33.88 ? 177 HIS A CG 1 ATOM 1448 N ND1 . HIS A 1 177 ? 11.209 34.571 5.445 1.00 32.80 ? 177 HIS A ND1 1 ATOM 1449 C CD2 . HIS A 1 177 ? 9.872 33.129 4.490 1.00 33.19 ? 177 HIS A CD2 1 ATOM 1450 C CE1 . HIS A 1 177 ? 10.244 34.301 6.306 1.00 36.32 ? 177 HIS A CE1 1 ATOM 1451 N NE2 . HIS A 1 177 ? 9.420 33.430 5.752 1.00 34.99 ? 177 HIS A NE2 1 ATOM 1452 N N . TRP A 1 178 ? 12.738 31.129 4.452 1.00 29.93 ? 178 TRP A N 1 ATOM 1453 C CA . TRP A 1 178 ? 12.188 29.785 4.556 1.00 24.34 ? 178 TRP A CA 1 ATOM 1454 C C . TRP A 1 178 ? 11.173 29.730 5.690 1.00 22.45 ? 178 TRP A C 1 ATOM 1455 O O . TRP A 1 178 ? 11.399 30.281 6.769 1.00 24.52 ? 178 TRP A O 1 ATOM 1456 C CB . TRP A 1 178 ? 13.279 28.740 4.788 1.00 17.99 ? 178 TRP A CB 1 ATOM 1457 C CG . TRP A 1 178 ? 12.716 27.342 4.867 1.00 33.36 ? 178 TRP A CG 1 ATOM 1458 C CD1 . TRP A 1 178 ? 12.598 26.458 3.830 1.00 32.94 ? 178 TRP A CD1 1 ATOM 1459 C CD2 . TRP A 1 178 ? 12.164 26.682 6.017 1.00 25.95 ? 178 TRP A CD2 1 ATOM 1460 N NE1 . TRP A 1 178 ? 12.024 25.291 4.264 1.00 31.18 ? 178 TRP A NE1 1 ATOM 1461 C CE2 . TRP A 1 178 ? 11.747 25.400 5.601 1.00 30.76 ? 178 TRP A CE2 1 ATOM 1462 C CE3 . TRP A 1 178 ? 11.992 27.044 7.356 1.00 27.48 ? 178 TRP A CE3 1 ATOM 1463 C CZ2 . TRP A 1 178 ? 11.168 24.481 6.475 1.00 26.44 ? 178 TRP A CZ2 1 ATOM 1464 C CZ3 . TRP A 1 178 ? 11.411 26.129 8.223 1.00 29.85 ? 178 TRP A CZ3 1 ATOM 1465 C CH2 . TRP A 1 178 ? 11.007 24.864 7.778 1.00 27.93 ? 178 TRP A CH2 1 ATOM 1466 N N . GLU A 1 179 ? 10.051 29.071 5.444 1.00 21.72 ? 179 GLU A N 1 ATOM 1467 C CA . GLU A 1 179 ? 9.116 28.765 6.514 1.00 33.08 ? 179 GLU A CA 1 ATOM 1468 C C . GLU A 1 179 ? 8.399 27.453 6.214 1.00 33.43 ? 179 GLU A C 1 ATOM 1469 O O . GLU A 1 179 ? 8.346 27.009 5.063 1.00 30.46 ? 179 GLU A O 1 ATOM 1470 C CB . GLU A 1 179 ? 8.129 29.912 6.723 1.00 35.15 ? 179 GLU A CB 1 ATOM 1471 C CG . GLU A 1 179 ? 7.134 30.123 5.607 1.00 38.56 ? 179 GLU A CG 1 ATOM 1472 C CD . GLU A 1 179 ? 6.267 31.339 5.854 1.00 43.36 ? 179 GLU A CD 1 ATOM 1473 O OE1 . GLU A 1 179 ? 6.829 32.419 6.135 1.00 43.95 ? 179 GLU A OE1 1 ATOM 1474 O OE2 . GLU A 1 179 ? 5.028 31.215 5.778 1.00 50.36 ? 179 GLU A OE2 1 ATOM 1475 N N . PHE A 1 180 ? 7.864 26.833 7.261 1.00 25.75 ? 180 PHE A N 1 ATOM 1476 C CA . PHE A 1 180 ? 7.217 25.532 7.146 1.00 28.74 ? 180 PHE A CA 1 ATOM 1477 C C . PHE A 1 180 ? 6.018 25.530 6.203 1.00 36.87 ? 180 PHE A C 1 ATOM 1478 O O . PHE A 1 180 ? 5.081 26.314 6.351 1.00 40.88 ? 180 PHE A O 1 ATOM 1479 C CB . PHE A 1 180 ? 6.781 25.054 8.533 1.00 31.63 ? 180 PHE A CB 1 ATOM 1480 C CG . PHE A 1 180 ? 6.195 23.673 8.543 1.00 37.81 ? 180 PHE A CG 1 ATOM 1481 C CD1 . PHE A 1 180 ? 7.011 22.557 8.465 1.00 34.88 ? 180 PHE A CD1 1 ATOM 1482 C CD2 . PHE A 1 180 ? 4.825 23.493 8.636 1.00 41.05 ? 180 PHE A CD2 1 ATOM 1483 C CE1 . PHE A 1 180 ? 6.469 21.284 8.474 1.00 37.62 ? 180 PHE A CE1 1 ATOM 1484 C CE2 . PHE A 1 180 ? 4.277 22.224 8.646 1.00 44.61 ? 180 PHE A CE2 1 ATOM 1485 C CZ . PHE A 1 180 ? 5.100 21.118 8.563 1.00 41.07 ? 180 PHE A CZ 1 ATOM 1486 N N . ASP A 1 181 ? 6.069 24.625 5.230 1.00 47.77 ? 181 ASP A N 1 ATOM 1487 C CA . ASP A 1 181 ? 5.067 24.537 4.177 1.00 56.03 ? 181 ASP A CA 1 ATOM 1488 C C . ASP A 1 181 ? 3.829 23.843 4.740 1.00 57.97 ? 181 ASP A C 1 ATOM 1489 O O . ASP A 1 181 ? 2.797 24.475 4.965 1.00 61.32 ? 181 ASP A O 1 ATOM 1490 C CB . ASP A 1 181 ? 5.641 23.785 2.966 1.00 58.74 ? 181 ASP A CB 1 ATOM 1491 C CG . ASP A 1 181 ? 4.662 23.681 1.796 1.00 62.47 ? 181 ASP A CG 1 ATOM 1492 O OD1 . ASP A 1 181 ? 3.430 23.730 1.994 1.00 60.39 ? 181 ASP A OD1 1 ATOM 1493 O OD2 . ASP A 1 181 ? 5.145 23.551 0.650 1.00 64.49 ? 181 ASP A OD2 1 ATOM 1494 N N . ASP B 2 4 ? 33.052 49.748 2.736 1.00 53.15 ? 2 ASP B N 1 ATOM 1495 C CA . ASP B 2 4 ? 34.403 49.576 2.214 1.00 55.46 ? 2 ASP B CA 1 ATOM 1496 C C . ASP B 2 4 ? 34.362 49.555 0.688 1.00 59.12 ? 2 ASP B C 1 ATOM 1497 O O . ASP B 2 4 ? 33.976 48.555 0.082 1.00 58.48 ? 2 ASP B O 1 ATOM 1498 C CB . ASP B 2 4 ? 35.036 48.290 2.756 1.00 47.09 ? 2 ASP B CB 1 ATOM 1499 C CG . ASP B 2 4 ? 36.555 48.285 2.636 1.00 39.88 ? 2 ASP B CG 1 ATOM 1500 O OD1 . ASP B 2 4 ? 37.100 49.092 1.856 1.00 34.91 ? 2 ASP B OD1 1 ATOM 1501 O OD2 . ASP B 2 4 ? 37.207 47.480 3.336 1.00 39.61 ? 2 ASP B OD2 1 ATOM 1502 N N . THR B 2 5 ? 34.764 50.664 0.075 1.00 53.37 ? 3 THR B N 1 ATOM 1503 C CA . THR B 2 5 ? 34.711 50.807 -1.378 1.00 48.11 ? 3 THR B CA 1 ATOM 1504 C C . THR B 2 5 ? 36.085 50.649 -2.013 1.00 43.03 ? 3 THR B C 1 ATOM 1505 O O . THR B 2 5 ? 36.238 50.824 -3.225 1.00 42.81 ? 3 THR B O 1 ATOM 1506 C CB . THR B 2 5 ? 34.130 52.173 -1.806 1.00 51.32 ? 3 THR B CB 1 ATOM 1507 O OG1 . THR B 2 5 ? 34.921 53.230 -1.247 1.00 49.81 ? 3 THR B OG1 1 ATOM 1508 C CG2 . THR B 2 5 ? 32.690 52.318 -1.341 1.00 55.53 ? 3 THR B CG2 1 ATOM 1509 N N . ARG B 2 6 ? 37.084 50.333 -1.194 1.00 34.33 ? 4 ARG B N 1 ATOM 1510 C CA . ARG B 2 6 ? 38.439 50.138 -1.696 1.00 26.46 ? 4 ARG B CA 1 ATOM 1511 C C . ARG B 2 6 ? 38.461 49.056 -2.767 1.00 24.25 ? 4 ARG B C 1 ATOM 1512 O O . ARG B 2 6 ? 37.809 48.021 -2.625 1.00 22.26 ? 4 ARG B O 1 ATOM 1513 C CB . ARG B 2 6 ? 39.394 49.753 -0.569 1.00 25.62 ? 4 ARG B CB 1 ATOM 1514 C CG . ARG B 2 6 ? 39.770 50.879 0.371 1.00 29.43 ? 4 ARG B CG 1 ATOM 1515 C CD . ARG B 2 6 ? 40.740 50.364 1.416 1.00 34.07 ? 4 ARG B CD 1 ATOM 1516 N NE . ARG B 2 6 ? 40.137 49.332 2.254 1.00 28.83 ? 4 ARG B NE 1 ATOM 1517 C CZ . ARG B 2 6 ? 40.833 48.522 3.043 1.00 30.62 ? 4 ARG B CZ 1 ATOM 1518 N NH1 . ARG B 2 6 ? 42.154 48.626 3.093 1.00 26.97 ? 4 ARG B NH1 1 ATOM 1519 N NH2 . ARG B 2 6 ? 40.211 47.610 3.778 1.00 32.40 ? 4 ARG B NH2 1 ATOM 1520 N N . PRO B 2 7 ? 39.223 49.292 -3.842 1.00 21.40 ? 5 PRO B N 1 ATOM 1521 C CA . PRO B 2 7 ? 39.351 48.305 -4.917 1.00 21.11 ? 5 PRO B CA 1 ATOM 1522 C C . PRO B 2 7 ? 39.995 47.016 -4.427 1.00 18.41 ? 5 PRO B C 1 ATOM 1523 O O . PRO B 2 7 ? 40.894 47.043 -3.583 1.00 20.05 ? 5 PRO B O 1 ATOM 1524 C CB . PRO B 2 7 ? 40.258 49.005 -5.937 1.00 21.75 ? 5 PRO B CB 1 ATOM 1525 C CG . PRO B 2 7 ? 40.959 50.082 -5.160 1.00 23.78 ? 5 PRO B CG 1 ATOM 1526 C CD . PRO B 2 7 ? 39.993 50.516 -4.111 1.00 19.60 ? 5 PRO B CD 1 ATOM 1527 N N . ARG B 2 8 ? 39.525 45.893 -4.955 1.00 12.54 ? 6 ARG B N 1 ATOM 1528 C CA . ARG B 2 8 ? 40.082 44.598 -4.603 1.00 11.74 ? 6 ARG B CA 1 ATOM 1529 C C . ARG B 2 8 ? 40.889 44.030 -5.760 1.00 13.69 ? 6 ARG B C 1 ATOM 1530 O O . ARG B 2 8 ? 40.631 44.332 -6.924 1.00 14.91 ? 6 ARG B O 1 ATOM 1531 C CB . ARG B 2 8 ? 38.974 43.620 -4.203 1.00 14.65 ? 6 ARG B CB 1 ATOM 1532 C CG . ARG B 2 8 ? 38.825 43.406 -2.703 1.00 15.78 ? 6 ARG B CG 1 ATOM 1533 C CD . ARG B 2 8 ? 38.454 44.691 -1.977 1.00 19.96 ? 6 ARG B CD 1 ATOM 1534 N NE . ARG B 2 8 ? 38.459 44.517 -0.527 1.00 14.07 ? 6 ARG B NE 1 ATOM 1535 C CZ . ARG B 2 8 ? 38.073 45.450 0.338 1.00 20.23 ? 6 ARG B CZ 1 ATOM 1536 N NH1 . ARG B 2 8 ? 37.651 46.630 -0.099 1.00 19.41 ? 6 ARG B NH1 1 ATOM 1537 N NH2 . ARG B 2 8 ? 38.110 45.204 1.641 1.00 23.45 ? 6 ARG B NH2 1 ATOM 1538 N N . PHE B 2 9 ? 41.872 43.208 -5.423 1.00 16.40 ? 7 PHE B N 1 ATOM 1539 C CA . PHE B 2 9 ? 42.703 42.548 -6.414 1.00 15.91 ? 7 PHE B CA 1 ATOM 1540 C C . PHE B 2 9 ? 42.848 41.104 -5.975 1.00 17.56 ? 7 PHE B C 1 ATOM 1541 O O . PHE B 2 9 ? 43.186 40.829 -4.823 1.00 12.41 ? 7 PHE B O 1 ATOM 1542 C CB . PHE B 2 9 ? 44.064 43.233 -6.546 1.00 14.64 ? 7 PHE B CB 1 ATOM 1543 C CG . PHE B 2 9 ? 43.973 44.720 -6.778 1.00 16.36 ? 7 PHE B CG 1 ATOM 1544 C CD1 . PHE B 2 9 ? 43.841 45.228 -8.062 1.00 14.56 ? 7 PHE B CD1 1 ATOM 1545 C CD2 . PHE B 2 9 ? 44.020 45.607 -5.713 1.00 13.50 ? 7 PHE B CD2 1 ATOM 1546 C CE1 . PHE B 2 9 ? 43.757 46.596 -8.281 1.00 12.60 ? 7 PHE B CE1 1 ATOM 1547 C CE2 . PHE B 2 9 ? 43.935 46.976 -5.924 1.00 17.46 ? 7 PHE B CE2 1 ATOM 1548 C CZ . PHE B 2 9 ? 43.804 47.471 -7.208 1.00 14.72 ? 7 PHE B CZ 1 ATOM 1549 N N . LEU B 2 10 ? 42.590 40.182 -6.895 1.00 18.28 ? 8 LEU B N 1 ATOM 1550 C CA . LEU B 2 10 ? 42.534 38.769 -6.550 1.00 12.41 ? 8 LEU B CA 1 ATOM 1551 C C . LEU B 2 10 ? 43.476 37.944 -7.407 1.00 19.16 ? 8 LEU B C 1 ATOM 1552 O O . LEU B 2 10 ? 43.492 38.068 -8.631 1.00 13.58 ? 8 LEU B O 1 ATOM 1553 C CB . LEU B 2 10 ? 41.101 38.239 -6.683 1.00 10.29 ? 8 LEU B CB 1 ATOM 1554 C CG . LEU B 2 10 ? 40.859 36.753 -6.397 1.00 14.81 ? 8 LEU B CG 1 ATOM 1555 C CD1 . LEU B 2 10 ? 40.990 36.456 -4.909 1.00 8.06 ? 8 LEU B CD1 1 ATOM 1556 C CD2 . LEU B 2 10 ? 39.485 36.341 -6.896 1.00 12.86 ? 8 LEU B CD2 1 ATOM 1557 N N . GLU B 2 11 ? 44.252 37.093 -6.744 1.00 7.83 ? 9 GLU B N 1 ATOM 1558 C CA . GLU B 2 11 ? 45.065 36.111 -7.436 1.00 9.07 ? 9 GLU B CA 1 ATOM 1559 C C . GLU B 2 11 ? 44.492 34.731 -7.152 1.00 19.92 ? 9 GLU B C 1 ATOM 1560 O O . GLU B 2 11 ? 44.188 34.419 -6.002 1.00 15.62 ? 9 GLU B O 1 ATOM 1561 C CB . GLU B 2 11 ? 46.513 36.190 -6.941 1.00 15.81 ? 9 GLU B CB 1 ATOM 1562 C CG . GLU B 2 11 ? 47.465 35.144 -7.500 1.00 21.16 ? 9 GLU B CG 1 ATOM 1563 C CD . GLU B 2 11 ? 47.975 35.500 -8.876 1.00 24.42 ? 9 GLU B CD 1 ATOM 1564 O OE1 . GLU B 2 11 ? 47.741 36.644 -9.312 1.00 19.50 ? 9 GLU B OE1 1 ATOM 1565 O OE2 . GLU B 2 11 ? 48.612 34.638 -9.520 1.00 19.72 ? 9 GLU B OE2 1 ATOM 1566 N N . GLN B 2 12 ? 44.345 33.908 -8.191 1.00 11.09 ? 10 GLN B N 1 ATOM 1567 C CA . GLN B 2 12 ? 43.959 32.513 -7.995 1.00 7.91 ? 10 GLN B CA 1 ATOM 1568 C C . GLN B 2 12 ? 44.954 31.610 -8.700 1.00 12.81 ? 10 GLN B C 1 ATOM 1569 O O . GLN B 2 12 ? 45.531 31.978 -9.725 1.00 9.92 ? 10 GLN B O 1 ATOM 1570 C CB . GLN B 2 12 ? 42.547 32.219 -8.520 1.00 7.62 ? 10 GLN B CB 1 ATOM 1571 C CG . GLN B 2 12 ? 41.430 33.116 -8.006 1.00 6.91 ? 10 GLN B CG 1 ATOM 1572 C CD . GLN B 2 12 ? 40.057 32.601 -8.410 1.00 9.92 ? 10 GLN B CD 1 ATOM 1573 O OE1 . GLN B 2 12 ? 39.653 31.501 -8.021 1.00 9.41 ? 10 GLN B OE1 1 ATOM 1574 N NE2 . GLN B 2 12 ? 39.337 33.389 -9.200 1.00 7.21 ? 10 GLN B NE2 1 ATOM 1575 N N . VAL B 2 13 ? 45.150 30.424 -8.140 1.00 7.15 ? 11 VAL B N 1 ATOM 1576 C CA . VAL B 2 13 ? 45.919 29.376 -8.790 1.00 6.36 ? 11 VAL B CA 1 ATOM 1577 C C . VAL B 2 13 ? 45.122 28.091 -8.674 1.00 12.95 ? 11 VAL B C 1 ATOM 1578 O O . VAL B 2 13 ? 44.601 27.772 -7.606 1.00 12.35 ? 11 VAL B O 1 ATOM 1579 C CB . VAL B 2 13 ? 47.320 29.188 -8.171 1.00 6.50 ? 11 VAL B CB 1 ATOM 1580 C CG1 . VAL B 2 13 ? 48.129 28.206 -9.001 1.00 6.53 ? 11 VAL B CG1 1 ATOM 1581 C CG2 . VAL B 2 13 ? 48.053 30.519 -8.081 1.00 7.50 ? 11 VAL B CG2 1 ATOM 1582 N N . LYS B 2 14 ? 45.018 27.349 -9.766 1.00 9.68 ? 12 LYS B N 1 ATOM 1583 C CA . LYS B 2 14 ? 44.356 26.059 -9.714 1.00 15.90 ? 12 LYS B CA 1 ATOM 1584 C C . LYS B 2 14 ? 45.244 24.997 -10.333 1.00 12.35 ? 12 LYS B C 1 ATOM 1585 O O . LYS B 2 14 ? 45.570 25.053 -11.517 1.00 9.28 ? 12 LYS B O 1 ATOM 1586 C CB . LYS B 2 14 ? 42.995 26.111 -10.419 1.00 6.34 ? 12 LYS B CB 1 ATOM 1587 C CG . LYS B 2 14 ? 41.988 27.045 -9.749 1.00 8.22 ? 12 LYS B CG 1 ATOM 1588 C CD . LYS B 2 14 ? 40.648 27.070 -10.484 1.00 12.28 ? 12 LYS B CD 1 ATOM 1589 C CE . LYS B 2 14 ? 39.642 27.958 -9.756 1.00 6.59 ? 12 LYS B CE 1 ATOM 1590 N NZ . LYS B 2 14 ? 38.313 28.017 -10.434 1.00 7.59 ? 12 LYS B NZ 1 ATOM 1591 N N . HIS B 2 15 ? 45.643 24.034 -9.514 1.00 8.87 ? 13 HIS B N 1 ATOM 1592 C CA . HIS B 2 15 ? 46.451 22.933 -9.998 1.00 11.63 ? 13 HIS B CA 1 ATOM 1593 C C . HIS B 2 15 ? 45.509 21.762 -10.190 1.00 13.42 ? 13 HIS B C 1 ATOM 1594 O O . HIS B 2 15 ? 45.026 21.180 -9.214 1.00 14.64 ? 13 HIS B O 1 ATOM 1595 C CB . HIS B 2 15 ? 47.552 22.575 -9.000 1.00 6.95 ? 13 HIS B CB 1 ATOM 1596 C CG . HIS B 2 15 ? 48.233 23.760 -8.385 1.00 11.31 ? 13 HIS B CG 1 ATOM 1597 N ND1 . HIS B 2 15 ? 49.369 24.330 -8.920 1.00 12.25 ? 13 HIS B ND1 1 ATOM 1598 C CD2 . HIS B 2 15 ? 47.944 24.475 -7.271 1.00 9.03 ? 13 HIS B CD2 1 ATOM 1599 C CE1 . HIS B 2 15 ? 49.756 25.338 -8.159 1.00 8.98 ? 13 HIS B CE1 1 ATOM 1600 N NE2 . HIS B 2 15 ? 48.906 25.449 -7.153 1.00 7.17 ? 13 HIS B NE2 1 ATOM 1601 N N . GLU B 2 16 ? 45.240 21.415 -11.443 1.00 14.66 ? 14 GLU B N 1 ATOM 1602 C CA . GLU B 2 16 ? 44.169 20.472 -11.737 1.00 11.13 ? 14 GLU B CA 1 ATOM 1603 C C . GLU B 2 16 ? 44.693 19.141 -12.243 1.00 14.41 ? 14 GLU B C 1 ATOM 1604 O O . GLU B 2 16 ? 45.614 19.086 -13.063 1.00 17.97 ? 14 GLU B O 1 ATOM 1605 C CB . GLU B 2 16 ? 43.189 21.055 -12.753 1.00 9.83 ? 14 GLU B CB 1 ATOM 1606 C CG . GLU B 2 16 ? 42.639 22.426 -12.402 1.00 6.92 ? 14 GLU B CG 1 ATOM 1607 C CD . GLU B 2 16 ? 41.560 22.848 -13.373 1.00 12.34 ? 14 GLU B CD 1 ATOM 1608 O OE1 . GLU B 2 16 ? 41.360 22.124 -14.370 1.00 12.52 ? 14 GLU B OE1 1 ATOM 1609 O OE2 . GLU B 2 16 ? 40.918 23.895 -13.152 1.00 15.86 ? 14 GLU B OE2 1 ATOM 1610 N N . CYS B 2 17 ? 44.099 18.068 -11.737 1.00 11.29 ? 15 CYS B N 1 ATOM 1611 C CA . CYS B 2 17 ? 44.408 16.728 -12.208 1.00 13.17 ? 15 CYS B CA 1 ATOM 1612 C C . CYS B 2 17 ? 43.154 16.088 -12.779 1.00 12.91 ? 15 CYS B C 1 ATOM 1613 O O . CYS B 2 17 ? 42.161 15.915 -12.074 1.00 17.06 ? 15 CYS B O 1 ATOM 1614 C CB . CYS B 2 17 ? 44.978 15.875 -11.078 1.00 9.40 ? 15 CYS B CB 1 ATOM 1615 S SG . CYS B 2 17 ? 46.602 16.418 -10.533 1.00 19.37 ? 15 CYS B SG 1 ATOM 1616 N N . HIS B 2 18 ? 43.211 15.726 -14.055 1.00 10.97 ? 16 HIS B N 1 ATOM 1617 C CA . HIS B 2 18 ? 42.058 15.141 -14.728 1.00 17.27 ? 16 HIS B CA 1 ATOM 1618 C C . HIS B 2 18 ? 42.286 13.663 -15.020 1.00 10.14 ? 16 HIS B C 1 ATOM 1619 O O . HIS B 2 18 ? 43.286 13.293 -15.631 1.00 22.06 ? 16 HIS B O 1 ATOM 1620 C CB . HIS B 2 18 ? 41.770 15.893 -16.030 1.00 9.45 ? 16 HIS B CB 1 ATOM 1621 C CG . HIS B 2 18 ? 41.401 17.330 -15.828 1.00 19.30 ? 16 HIS B CG 1 ATOM 1622 N ND1 . HIS B 2 18 ? 40.125 17.807 -16.038 1.00 21.34 ? 16 HIS B ND1 1 ATOM 1623 C CD2 . HIS B 2 18 ? 42.135 18.392 -15.417 1.00 16.52 ? 16 HIS B CD2 1 ATOM 1624 C CE1 . HIS B 2 18 ? 40.091 19.101 -15.777 1.00 14.82 ? 16 HIS B CE1 1 ATOM 1625 N NE2 . HIS B 2 18 ? 41.298 19.481 -15.397 1.00 9.84 ? 16 HIS B NE2 1 ATOM 1626 N N . PHE B 2 19 ? 41.356 12.822 -14.579 1.00 14.49 ? 17 PHE B N 1 ATOM 1627 C CA . PHE B 2 19 ? 41.537 11.376 -14.669 1.00 11.26 ? 17 PHE B CA 1 ATOM 1628 C C . PHE B 2 19 ? 40.527 10.721 -15.603 1.00 22.36 ? 17 PHE B C 1 ATOM 1629 O O . PHE B 2 19 ? 39.335 11.019 -15.560 1.00 23.21 ? 17 PHE B O 1 ATOM 1630 C CB . PHE B 2 19 ? 41.461 10.738 -13.281 1.00 11.38 ? 17 PHE B CB 1 ATOM 1631 C CG . PHE B 2 19 ? 42.480 11.274 -12.318 1.00 13.96 ? 17 PHE B CG 1 ATOM 1632 C CD1 . PHE B 2 19 ? 43.765 10.753 -12.298 1.00 14.48 ? 17 PHE B CD1 1 ATOM 1633 C CD2 . PHE B 2 19 ? 42.163 12.292 -11.438 1.00 10.31 ? 17 PHE B CD2 1 ATOM 1634 C CE1 . PHE B 2 19 ? 44.714 11.238 -11.416 1.00 15.14 ? 17 PHE B CE1 1 ATOM 1635 C CE2 . PHE B 2 19 ? 43.112 12.783 -10.550 1.00 13.45 ? 17 PHE B CE2 1 ATOM 1636 C CZ . PHE B 2 19 ? 44.386 12.255 -10.540 1.00 13.00 ? 17 PHE B CZ 1 ATOM 1637 N N . PHE B 2 20 ? 41.033 9.825 -16.444 1.00 19.56 ? 18 PHE B N 1 ATOM 1638 C CA . PHE B 2 20 ? 40.228 9.088 -17.410 1.00 27.11 ? 18 PHE B CA 1 ATOM 1639 C C . PHE B 2 20 ? 40.552 7.608 -17.228 1.00 28.51 ? 18 PHE B C 1 ATOM 1640 O O . PHE B 2 20 ? 41.724 7.242 -17.260 1.00 27.74 ? 18 PHE B O 1 ATOM 1641 C CB . PHE B 2 20 ? 40.549 9.513 -18.849 1.00 34.58 ? 18 PHE B CB 1 ATOM 1642 C CG . PHE B 2 20 ? 40.576 11.008 -19.072 1.00 40.32 ? 18 PHE B CG 1 ATOM 1643 C CD1 . PHE B 2 20 ? 41.678 11.761 -18.683 1.00 35.51 ? 18 PHE B CD1 1 ATOM 1644 C CD2 . PHE B 2 20 ? 39.531 11.651 -19.712 1.00 44.82 ? 18 PHE B CD2 1 ATOM 1645 C CE1 . PHE B 2 20 ? 41.720 13.129 -18.895 1.00 31.10 ? 18 PHE B CE1 1 ATOM 1646 C CE2 . PHE B 2 20 ? 39.569 13.023 -19.929 1.00 43.34 ? 18 PHE B CE2 1 ATOM 1647 C CZ . PHE B 2 20 ? 40.666 13.761 -19.518 1.00 35.23 ? 18 PHE B CZ 1 ATOM 1648 N N . ASN B 2 21 ? 39.539 6.765 -17.036 1.00 34.93 ? 19 ASN B N 1 ATOM 1649 C CA . ASN B 2 21 ? 39.760 5.325 -16.866 1.00 35.81 ? 19 ASN B CA 1 ATOM 1650 C C . ASN B 2 21 ? 40.720 5.043 -15.713 1.00 30.95 ? 19 ASN B C 1 ATOM 1651 O O . ASN B 2 21 ? 41.814 4.525 -15.928 1.00 35.44 ? 19 ASN B O 1 ATOM 1652 C CB . ASN B 2 21 ? 40.300 4.711 -18.169 1.00 47.70 ? 19 ASN B CB 1 ATOM 1653 C CG . ASN B 2 21 ? 40.428 3.192 -18.119 1.00 55.39 ? 19 ASN B CG 1 ATOM 1654 O OD1 . ASN B 2 21 ? 39.974 2.534 -17.177 1.00 51.21 ? 19 ASN B OD1 1 ATOM 1655 N ND2 . ASN B 2 21 ? 41.079 2.637 -19.150 1.00 64.08 ? 19 ASN B ND2 1 ATOM 1656 N N . GLY B 2 22 ? 40.330 5.403 -14.494 1.00 25.47 ? 20 GLY B N 1 ATOM 1657 C CA . GLY B 2 22 ? 41.240 5.289 -13.369 1.00 24.22 ? 20 GLY B CA 1 ATOM 1658 C C . GLY B 2 22 ? 42.387 6.267 -13.510 1.00 29.37 ? 20 GLY B C 1 ATOM 1659 O O . GLY B 2 22 ? 42.180 7.473 -13.641 1.00 33.63 ? 20 GLY B O 1 ATOM 1660 N N . THR B 2 23 ? 43.605 5.736 -13.481 1.00 25.16 ? 21 THR B N 1 ATOM 1661 C CA . THR B 2 23 ? 44.802 6.535 -13.709 1.00 30.62 ? 21 THR B CA 1 ATOM 1662 C C . THR B 2 23 ? 45.482 6.175 -15.034 1.00 27.90 ? 21 THR B C 1 ATOM 1663 O O . THR B 2 23 ? 46.665 6.455 -15.226 1.00 28.01 ? 21 THR B O 1 ATOM 1664 C CB . THR B 2 23 ? 45.813 6.373 -12.567 1.00 34.98 ? 21 THR B CB 1 ATOM 1665 O OG1 . THR B 2 23 ? 46.037 4.981 -12.318 1.00 32.06 ? 21 THR B OG1 1 ATOM 1666 C CG2 . THR B 2 23 ? 45.289 7.035 -11.298 1.00 33.54 ? 21 THR B CG2 1 ATOM 1667 N N . GLU B 2 24 ? 44.743 5.534 -15.936 1.00 26.80 ? 22 GLU B N 1 ATOM 1668 C CA . GLU B 2 24 ? 45.309 5.112 -17.217 1.00 33.92 ? 22 GLU B CA 1 ATOM 1669 C C . GLU B 2 24 ? 45.687 6.326 -18.062 1.00 30.83 ? 22 GLU B C 1 ATOM 1670 O O . GLU B 2 24 ? 46.745 6.354 -18.693 1.00 31.91 ? 22 GLU B O 1 ATOM 1671 C CB . GLU B 2 24 ? 44.332 4.215 -17.980 1.00 37.25 ? 22 GLU B CB 1 ATOM 1672 C CG . GLU B 2 24 ? 44.265 2.791 -17.452 1.00 52.11 ? 22 GLU B CG 1 ATOM 1673 C CD . GLU B 2 24 ? 45.592 2.061 -17.571 1.00 59.01 ? 22 GLU B CD 1 ATOM 1674 O OE1 . GLU B 2 24 ? 46.088 1.908 -18.707 1.00 63.80 ? 22 GLU B OE1 1 ATOM 1675 O OE2 . GLU B 2 24 ? 46.141 1.641 -16.529 1.00 55.01 ? 22 GLU B OE2 1 ATOM 1676 N N . ARG B 2 25 ? 44.824 7.336 -18.053 1.00 25.15 ? 23 ARG B N 1 ATOM 1677 C CA . ARG B 2 25 ? 45.095 8.584 -18.753 1.00 25.12 ? 23 ARG B CA 1 ATOM 1678 C C . ARG B 2 25 ? 44.893 9.743 -17.782 1.00 25.62 ? 23 ARG B C 1 ATOM 1679 O O . ARG B 2 25 ? 43.838 9.864 -17.158 1.00 24.52 ? 23 ARG B O 1 ATOM 1680 C CB . ARG B 2 25 ? 44.179 8.752 -19.971 1.00 33.91 ? 23 ARG B CB 1 ATOM 1681 C CG . ARG B 2 25 ? 44.318 7.695 -21.068 1.00 46.01 ? 23 ARG B CG 1 ATOM 1682 C CD . ARG B 2 25 ? 45.073 8.240 -22.283 1.00 56.97 ? 23 ARG B CD 1 ATOM 1683 N NE . ARG B 2 25 ? 45.310 7.220 -23.306 1.00 62.89 ? 23 ARG B NE 1 ATOM 1684 C CZ . ARG B 2 25 ? 44.669 7.172 -24.473 1.00 62.02 ? 23 ARG B CZ 1 ATOM 1685 N NH1 . ARG B 2 25 ? 43.758 8.090 -24.770 1.00 64.17 ? 23 ARG B NH1 1 ATOM 1686 N NH2 . ARG B 2 25 ? 44.941 6.214 -25.350 1.00 53.88 ? 23 ARG B NH2 1 ATOM 1687 N N . VAL B 2 26 ? 45.907 10.594 -17.660 1.00 21.10 ? 24 VAL B N 1 ATOM 1688 C CA . VAL B 2 26 ? 45.881 11.703 -16.708 1.00 17.72 ? 24 VAL B CA 1 ATOM 1689 C C . VAL B 2 26 ? 46.364 12.978 -17.379 1.00 15.52 ? 24 VAL B C 1 ATOM 1690 O O . VAL B 2 26 ? 47.345 12.963 -18.115 1.00 19.28 ? 24 VAL B O 1 ATOM 1691 C CB . VAL B 2 26 ? 46.760 11.423 -15.469 1.00 17.39 ? 24 VAL B CB 1 ATOM 1692 C CG1 . VAL B 2 26 ? 46.719 12.597 -14.498 1.00 15.99 ? 24 VAL B CG1 1 ATOM 1693 C CG2 . VAL B 2 26 ? 46.332 10.133 -14.783 1.00 20.49 ? 24 VAL B CG2 1 ATOM 1694 N N . ARG B 2 27 ? 45.683 14.085 -17.112 1.00 16.60 ? 25 ARG B N 1 ATOM 1695 C CA . ARG B 2 27 ? 46.109 15.375 -17.635 1.00 17.41 ? 25 ARG B CA 1 ATOM 1696 C C . ARG B 2 27 ? 46.282 16.355 -16.483 1.00 13.69 ? 25 ARG B C 1 ATOM 1697 O O . ARG B 2 27 ? 45.426 16.444 -15.604 1.00 19.04 ? 25 ARG B O 1 ATOM 1698 C CB . ARG B 2 27 ? 45.093 15.892 -18.657 1.00 25.36 ? 25 ARG B CB 1 ATOM 1699 C CG . ARG B 2 27 ? 45.454 17.198 -19.355 1.00 22.52 ? 25 ARG B CG 1 ATOM 1700 C CD . ARG B 2 27 ? 44.487 17.439 -20.513 1.00 22.50 ? 25 ARG B CD 1 ATOM 1701 N NE . ARG B 2 27 ? 44.632 18.756 -21.124 1.00 30.10 ? 25 ARG B NE 1 ATOM 1702 C CZ . ARG B 2 27 ? 43.626 19.597 -21.335 1.00 40.76 ? 25 ARG B CZ 1 ATOM 1703 N NH1 . ARG B 2 27 ? 42.395 19.262 -20.974 1.00 44.52 ? 25 ARG B NH1 1 ATOM 1704 N NH2 . ARG B 2 27 ? 43.851 20.778 -21.897 1.00 38.41 ? 25 ARG B NH2 1 ATOM 1705 N N . PHE B 2 28 ? 47.380 17.103 -16.509 1.00 17.51 ? 26 PHE B N 1 ATOM 1706 C CA . PHE B 2 28 ? 47.694 18.054 -15.447 1.00 12.67 ? 26 PHE B CA 1 ATOM 1707 C C . PHE B 2 28 ? 47.652 19.468 -16.004 1.00 13.62 ? 26 PHE B C 1 ATOM 1708 O O . PHE B 2 28 ? 48.227 19.754 -17.052 1.00 17.97 ? 26 PHE B O 1 ATOM 1709 C CB . PHE B 2 28 ? 49.062 17.765 -14.833 1.00 14.67 ? 26 PHE B CB 1 ATOM 1710 C CG . PHE B 2 28 ? 49.590 18.884 -13.979 1.00 17.10 ? 26 PHE B CG 1 ATOM 1711 C CD1 . PHE B 2 28 ? 48.989 19.178 -12.762 1.00 15.27 ? 26 PHE B CD1 1 ATOM 1712 C CD2 . PHE B 2 28 ? 50.677 19.641 -14.387 1.00 8.49 ? 26 PHE B CD2 1 ATOM 1713 C CE1 . PHE B 2 28 ? 49.469 20.206 -11.960 1.00 14.53 ? 26 PHE B CE1 1 ATOM 1714 C CE2 . PHE B 2 28 ? 51.164 20.672 -13.592 1.00 14.70 ? 26 PHE B CE2 1 ATOM 1715 C CZ . PHE B 2 28 ? 50.561 20.955 -12.377 1.00 9.06 ? 26 PHE B CZ 1 ATOM 1716 N N . LEU B 2 29 ? 46.947 20.344 -15.301 1.00 15.30 ? 27 LEU B N 1 ATOM 1717 C CA . LEU B 2 29 ? 46.870 21.752 -15.666 1.00 12.29 ? 27 LEU B CA 1 ATOM 1718 C C . LEU B 2 29 ? 47.327 22.663 -14.536 1.00 8.77 ? 27 LEU B C 1 ATOM 1719 O O . LEU B 2 29 ? 46.833 22.549 -13.416 1.00 8.82 ? 27 LEU B O 1 ATOM 1720 C CB . LEU B 2 29 ? 45.429 22.112 -16.041 1.00 17.04 ? 27 LEU B CB 1 ATOM 1721 C CG . LEU B 2 29 ? 44.750 21.397 -17.214 1.00 18.22 ? 27 LEU B CG 1 ATOM 1722 C CD1 . LEU B 2 29 ? 43.334 21.946 -17.412 1.00 19.85 ? 27 LEU B CD1 1 ATOM 1723 C CD2 . LEU B 2 29 ? 45.556 21.506 -18.503 1.00 9.70 ? 27 LEU B CD2 1 ATOM 1724 N N . ASP B 2 30 ? 48.297 23.529 -14.816 1.00 7.30 ? 28 ASP B N 1 ATOM 1725 C CA . ASP B 2 30 ? 48.766 24.497 -13.830 1.00 7.08 ? 28 ASP B CA 1 ATOM 1726 C C . ASP B 2 30 ? 48.209 25.842 -14.286 1.00 11.14 ? 28 ASP B C 1 ATOM 1727 O O . ASP B 2 30 ? 48.673 26.402 -15.274 1.00 10.41 ? 28 ASP B O 1 ATOM 1728 C CB . ASP B 2 30 ? 50.298 24.515 -13.761 1.00 7.33 ? 28 ASP B CB 1 ATOM 1729 C CG . ASP B 2 30 ? 50.825 24.877 -12.378 1.00 19.97 ? 28 ASP B CG 1 ATOM 1730 O OD1 . ASP B 2 30 ? 50.246 24.408 -11.374 1.00 17.28 ? 28 ASP B OD1 1 ATOM 1731 O OD2 . ASP B 2 30 ? 51.833 25.614 -12.297 1.00 13.09 ? 28 ASP B OD2 1 ATOM 1732 N N . ARG B 2 31 ? 47.234 26.373 -13.558 1.00 6.70 ? 29 ARG B N 1 ATOM 1733 C CA . ARG B 2 31 ? 46.460 27.492 -14.076 1.00 11.74 ? 29 ARG B CA 1 ATOM 1734 C C . ARG B 2 31 ? 46.588 28.694 -13.166 1.00 15.27 ? 29 ARG B C 1 ATOM 1735 O O . ARG B 2 31 ? 46.427 28.589 -11.952 1.00 16.16 ? 29 ARG B O 1 ATOM 1736 C CB . ARG B 2 31 ? 44.993 27.102 -14.252 1.00 6.66 ? 29 ARG B CB 1 ATOM 1737 C CG . ARG B 2 31 ? 44.795 25.782 -14.985 1.00 13.13 ? 29 ARG B CG 1 ATOM 1738 C CD . ARG B 2 31 ? 43.323 25.421 -15.062 1.00 6.92 ? 29 ARG B CD 1 ATOM 1739 N NE . ARG B 2 31 ? 42.629 26.342 -15.961 1.00 7.10 ? 29 ARG B NE 1 ATOM 1740 C CZ . ARG B 2 31 ? 41.308 26.409 -16.102 1.00 14.16 ? 29 ARG B CZ 1 ATOM 1741 N NH1 . ARG B 2 31 ? 40.519 25.609 -15.397 1.00 9.84 ? 29 ARG B NH1 1 ATOM 1742 N NH2 . ARG B 2 31 ? 40.773 27.276 -16.953 1.00 8.93 ? 29 ARG B NH2 1 ATOM 1743 N N . TYR B 2 32 ? 46.869 29.849 -13.761 1.00 12.16 ? 30 TYR B N 1 ATOM 1744 C CA . TYR B 2 32 ? 47.015 31.054 -12.969 1.00 12.30 ? 30 TYR B CA 1 ATOM 1745 C C . TYR B 2 32 ? 45.942 32.077 -13.364 1.00 16.99 ? 30 TYR B C 1 ATOM 1746 O O . TYR B 2 32 ? 45.692 32.282 -14.553 1.00 8.19 ? 30 TYR B O 1 ATOM 1747 C CB . TYR B 2 32 ? 48.436 31.591 -13.183 1.00 11.19 ? 30 TYR B CB 1 ATOM 1748 C CG . TYR B 2 32 ? 49.457 30.698 -12.500 1.00 8.13 ? 30 TYR B CG 1 ATOM 1749 C CD1 . TYR B 2 32 ? 49.781 29.471 -13.067 1.00 6.95 ? 30 TYR B CD1 1 ATOM 1750 C CD2 . TYR B 2 32 ? 50.047 31.032 -11.285 1.00 11.66 ? 30 TYR B CD2 1 ATOM 1751 C CE1 . TYR B 2 32 ? 50.678 28.615 -12.481 1.00 11.72 ? 30 TYR B CE1 1 ATOM 1752 C CE2 . TYR B 2 32 ? 50.960 30.166 -10.679 1.00 8.56 ? 30 TYR B CE2 1 ATOM 1753 C CZ . TYR B 2 32 ? 51.266 28.960 -11.289 1.00 10.93 ? 30 TYR B CZ 1 ATOM 1754 O OH . TYR B 2 32 ? 52.158 28.083 -10.718 1.00 17.79 ? 30 TYR B OH 1 ATOM 1755 N N . PHE B 2 33 ? 45.330 32.743 -12.387 1.00 16.15 ? 31 PHE B N 1 ATOM 1756 C CA . PHE B 2 33 ? 44.207 33.629 -12.687 1.00 12.59 ? 31 PHE B CA 1 ATOM 1757 C C . PHE B 2 33 ? 44.422 34.984 -12.032 1.00 13.27 ? 31 PHE B C 1 ATOM 1758 O O . PHE B 2 33 ? 44.918 35.070 -10.913 1.00 12.04 ? 31 PHE B O 1 ATOM 1759 C CB . PHE B 2 33 ? 42.882 33.042 -12.192 1.00 8.70 ? 31 PHE B CB 1 ATOM 1760 C CG . PHE B 2 33 ? 42.622 31.637 -12.646 1.00 7.03 ? 31 PHE B CG 1 ATOM 1761 C CD1 . PHE B 2 33 ? 43.201 30.565 -11.986 1.00 6.52 ? 31 PHE B CD1 1 ATOM 1762 C CD2 . PHE B 2 33 ? 41.793 31.384 -13.721 1.00 10.43 ? 31 PHE B CD2 1 ATOM 1763 C CE1 . PHE B 2 33 ? 42.958 29.272 -12.388 1.00 8.89 ? 31 PHE B CE1 1 ATOM 1764 C CE2 . PHE B 2 33 ? 41.550 30.091 -14.134 1.00 8.45 ? 31 PHE B CE2 1 ATOM 1765 C CZ . PHE B 2 33 ? 42.130 29.033 -13.467 1.00 6.66 ? 31 PHE B CZ 1 ATOM 1766 N N . TYR B 2 34 ? 44.045 36.044 -12.736 1.00 11.52 ? 32 TYR B N 1 ATOM 1767 C CA . TYR B 2 34 ? 43.996 37.372 -12.147 1.00 10.40 ? 32 TYR B CA 1 ATOM 1768 C C . TYR B 2 34 ? 42.549 37.834 -12.131 1.00 12.69 ? 32 TYR B C 1 ATOM 1769 O O . TYR B 2 34 ? 41.941 37.968 -13.196 1.00 8.37 ? 32 TYR B O 1 ATOM 1770 C CB . TYR B 2 34 ? 44.884 38.338 -12.927 1.00 8.98 ? 32 TYR B CB 1 ATOM 1771 C CG . TYR B 2 34 ? 44.912 39.741 -12.371 1.00 10.20 ? 32 TYR B CG 1 ATOM 1772 C CD1 . TYR B 2 34 ? 45.444 39.982 -11.116 1.00 8.75 ? 32 TYR B CD1 1 ATOM 1773 C CD2 . TYR B 2 34 ? 44.448 40.825 -13.107 1.00 9.28 ? 32 TYR B CD2 1 ATOM 1774 C CE1 . TYR B 2 34 ? 45.499 41.259 -10.590 1.00 12.91 ? 32 TYR B CE1 1 ATOM 1775 C CE2 . TYR B 2 34 ? 44.497 42.112 -12.589 1.00 9.80 ? 32 TYR B CE2 1 ATOM 1776 C CZ . TYR B 2 34 ? 45.026 42.321 -11.326 1.00 15.16 ? 32 TYR B CZ 1 ATOM 1777 O OH . TYR B 2 34 ? 45.092 43.587 -10.782 1.00 13.04 ? 32 TYR B OH 1 ATOM 1778 N N . HIS B 2 35 ? 41.994 38.045 -10.937 1.00 14.76 ? 33 HIS B N 1 ATOM 1779 C CA . HIS B 2 35 ? 40.548 38.165 -10.779 1.00 14.58 ? 33 HIS B CA 1 ATOM 1780 C C . HIS B 2 35 ? 39.837 36.895 -11.243 1.00 18.02 ? 33 HIS B C 1 ATOM 1781 O O . HIS B 2 35 ? 39.980 35.835 -10.631 1.00 16.37 ? 33 HIS B O 1 ATOM 1782 C CB . HIS B 2 35 ? 39.999 39.401 -11.501 1.00 15.03 ? 33 HIS B CB 1 ATOM 1783 C CG . HIS B 2 35 ? 40.730 40.667 -11.173 1.00 15.16 ? 33 HIS B CG 1 ATOM 1784 N ND1 . HIS B 2 35 ? 41.368 40.867 -9.967 1.00 9.31 ? 33 HIS B ND1 1 ATOM 1785 C CD2 . HIS B 2 35 ? 40.909 41.805 -11.887 1.00 17.69 ? 33 HIS B CD2 1 ATOM 1786 C CE1 . HIS B 2 35 ? 41.915 42.069 -9.956 1.00 16.32 ? 33 HIS B CE1 1 ATOM 1787 N NE2 . HIS B 2 35 ? 41.651 42.660 -11.108 1.00 17.52 ? 33 HIS B NE2 1 ATOM 1788 N N . GLN B 2 36 ? 39.070 37.003 -12.317 1.00 14.27 ? 34 GLN B N 1 ATOM 1789 C CA . GLN B 2 36 ? 38.388 35.849 -12.900 1.00 13.52 ? 34 GLN B CA 1 ATOM 1790 C C . GLN B 2 36 ? 39.053 35.319 -14.171 1.00 18.07 ? 34 GLN B C 1 ATOM 1791 O O . GLN B 2 36 ? 38.715 34.244 -14.667 1.00 22.89 ? 34 GLN B O 1 ATOM 1792 C CB . GLN B 2 36 ? 36.957 36.289 -13.221 1.00 24.88 ? 34 GLN B CB 1 ATOM 1793 C CG . GLN B 2 36 ? 35.847 35.282 -13.059 1.00 33.33 ? 34 GLN B CG 1 ATOM 1794 C CD . GLN B 2 36 ? 34.499 35.895 -13.419 1.00 39.77 ? 34 GLN B CD 1 ATOM 1795 O OE1 . GLN B 2 36 ? 34.251 37.068 -13.140 1.00 42.46 ? 34 GLN B OE1 1 ATOM 1796 N NE2 . GLN B 2 36 ? 33.633 35.112 -14.057 1.00 35.66 ? 34 GLN B NE2 1 ATOM 1797 N N . GLU B 2 37 ? 39.965 36.112 -14.716 1.00 23.16 ? 35 GLU B N 1 ATOM 1798 C CA A GLU B 2 37 ? 40.621 35.838 -15.995 0.39 22.33 ? 35 GLU B CA 1 ATOM 1799 C CA B GLU B 2 37 ? 40.594 35.791 -15.992 0.61 20.52 ? 35 GLU B CA 1 ATOM 1800 C C . GLU B 2 37 ? 41.856 34.932 -15.893 1.00 17.55 ? 35 GLU B C 1 ATOM 1801 O O . GLU B 2 37 ? 42.825 35.290 -15.227 1.00 12.84 ? 35 GLU B O 1 ATOM 1802 C CB A GLU B 2 37 ? 41.003 37.184 -16.622 0.39 27.87 ? 35 GLU B CB 1 ATOM 1803 C CB B GLU B 2 37 ? 40.887 37.077 -16.747 0.61 28.89 ? 35 GLU B CB 1 ATOM 1804 C CG A GLU B 2 37 ? 41.947 37.151 -17.806 0.39 27.29 ? 35 GLU B CG 1 ATOM 1805 C CG B GLU B 2 37 ? 39.625 37.837 -17.133 0.61 40.29 ? 35 GLU B CG 1 ATOM 1806 C CD A GLU B 2 37 ? 42.631 38.500 -18.023 0.39 24.44 ? 35 GLU B CD 1 ATOM 1807 C CD B GLU B 2 37 ? 39.892 38.976 -18.097 0.61 44.60 ? 35 GLU B CD 1 ATOM 1808 O OE1 A GLU B 2 37 ? 43.864 38.515 -18.217 0.39 24.11 ? 35 GLU B OE1 1 ATOM 1809 O OE1 B GLU B 2 37 ? 40.813 38.850 -18.928 0.61 46.61 ? 35 GLU B OE1 1 ATOM 1810 O OE2 A GLU B 2 37 ? 41.944 39.545 -17.998 0.39 23.95 ? 35 GLU B OE2 1 ATOM 1811 O OE2 B GLU B 2 37 ? 39.189 40.007 -18.013 0.61 42.88 ? 35 GLU B OE2 1 ATOM 1812 N N . GLU B 2 38 ? 41.823 33.764 -16.536 1.00 7.90 ? 36 GLU B N 1 ATOM 1813 C CA . GLU B 2 38 ? 43.018 32.914 -16.655 1.00 12.82 ? 36 GLU B CA 1 ATOM 1814 C C . GLU B 2 38 ? 44.025 33.624 -17.562 1.00 12.60 ? 36 GLU B C 1 ATOM 1815 O O . GLU B 2 38 ? 43.682 33.989 -18.686 1.00 9.90 ? 36 GLU B O 1 ATOM 1816 C CB . GLU B 2 38 ? 42.679 31.531 -17.218 1.00 7.63 ? 36 GLU B CB 1 ATOM 1817 C CG . GLU B 2 38 ? 43.849 30.545 -17.167 1.00 12.24 ? 36 GLU B CG 1 ATOM 1818 C CD . GLU B 2 38 ? 43.481 29.162 -17.676 1.00 13.36 ? 36 GLU B CD 1 ATOM 1819 O OE1 . GLU B 2 38 ? 42.413 29.016 -18.315 1.00 12.63 ? 36 GLU B OE1 1 ATOM 1820 O OE2 . GLU B 2 38 ? 44.260 28.219 -17.440 1.00 13.47 ? 36 GLU B OE2 1 ATOM 1821 N N . TYR B 2 39 ? 45.261 33.821 -17.105 1.00 9.49 ? 37 TYR B N 1 ATOM 1822 C CA A TYR B 2 39 ? 46.224 34.544 -17.935 0.50 8.24 ? 37 TYR B CA 1 ATOM 1823 C CA B TYR B 2 39 ? 46.246 34.558 -17.889 0.50 13.00 ? 37 TYR B CA 1 ATOM 1824 C C . TYR B 2 39 ? 47.414 33.707 -18.407 1.00 8.26 ? 37 TYR B C 1 ATOM 1825 O O . TYR B 2 39 ? 48.050 34.052 -19.400 1.00 12.66 ? 37 TYR B O 1 ATOM 1826 C CB A TYR B 2 39 ? 46.740 35.795 -17.212 0.50 15.11 ? 37 TYR B CB 1 ATOM 1827 C CB B TYR B 2 39 ? 46.786 35.721 -17.054 0.50 14.53 ? 37 TYR B CB 1 ATOM 1828 C CG A TYR B 2 39 ? 47.398 35.553 -15.873 0.50 14.25 ? 37 TYR B CG 1 ATOM 1829 C CG B TYR B 2 39 ? 45.893 36.949 -17.058 0.50 17.64 ? 37 TYR B CG 1 ATOM 1830 C CD1 A TYR B 2 39 ? 46.663 35.626 -14.701 0.50 10.32 ? 37 TYR B CD1 1 ATOM 1831 C CD1 B TYR B 2 39 ? 44.696 36.960 -17.759 0.50 22.21 ? 37 TYR B CD1 1 ATOM 1832 C CD2 A TYR B 2 39 ? 48.760 35.293 -15.777 0.50 12.94 ? 37 TYR B CD2 1 ATOM 1833 C CD2 B TYR B 2 39 ? 46.253 38.100 -16.369 0.50 16.07 ? 37 TYR B CD2 1 ATOM 1834 C CE1 A TYR B 2 39 ? 47.253 35.425 -13.477 0.50 11.11 ? 37 TYR B CE1 1 ATOM 1835 C CE1 B TYR B 2 39 ? 43.884 38.082 -17.783 0.50 25.21 ? 37 TYR B CE1 1 ATOM 1836 C CE2 A TYR B 2 39 ? 49.361 35.086 -14.548 0.50 11.14 ? 37 TYR B CE2 1 ATOM 1837 C CE2 B TYR B 2 39 ? 45.439 39.226 -16.379 0.50 21.06 ? 37 TYR B CE2 1 ATOM 1838 C CZ A TYR B 2 39 ? 48.597 35.156 -13.400 0.50 13.77 ? 37 TYR B CZ 1 ATOM 1839 C CZ B TYR B 2 39 ? 44.257 39.210 -17.088 0.50 22.75 ? 37 TYR B CZ 1 ATOM 1840 O OH A TYR B 2 39 ? 49.158 34.958 -12.161 0.50 16.55 ? 37 TYR B OH 1 ATOM 1841 O OH B TYR B 2 39 ? 43.451 40.324 -17.106 0.50 23.58 ? 37 TYR B OH 1 ATOM 1842 N N . VAL B 2 40 ? 47.716 32.605 -17.726 1.00 13.74 ? 38 VAL B N 1 ATOM 1843 C CA . VAL B 2 40 ? 48.784 31.706 -18.187 1.00 16.89 ? 38 VAL B CA 1 ATOM 1844 C C . VAL B 2 40 ? 48.520 30.304 -17.649 1.00 12.57 ? 38 VAL B C 1 ATOM 1845 O O . VAL B 2 40 ? 47.927 30.161 -16.584 1.00 7.58 ? 38 VAL B O 1 ATOM 1846 C CB . VAL B 2 40 ? 50.185 32.205 -17.746 1.00 14.00 ? 38 VAL B CB 1 ATOM 1847 C CG1 . VAL B 2 40 ? 50.326 32.162 -16.246 1.00 13.60 ? 38 VAL B CG1 1 ATOM 1848 C CG2 . VAL B 2 40 ? 51.286 31.399 -18.413 1.00 11.52 ? 38 VAL B CG2 1 ATOM 1849 N N . ARG B 2 41 ? 48.935 29.276 -18.392 1.00 12.32 ? 39 ARG B N 1 ATOM 1850 C CA . ARG B 2 41 ? 48.709 27.890 -17.972 1.00 16.15 ? 39 ARG B CA 1 ATOM 1851 C C . ARG B 2 41 ? 49.776 26.911 -18.473 1.00 13.81 ? 39 ARG B C 1 ATOM 1852 O O . ARG B 2 41 ? 50.339 27.080 -19.550 1.00 16.40 ? 39 ARG B O 1 ATOM 1853 C CB . ARG B 2 41 ? 47.342 27.378 -18.438 1.00 15.31 ? 39 ARG B CB 1 ATOM 1854 C CG . ARG B 2 41 ? 47.201 27.257 -19.942 1.00 25.70 ? 39 ARG B CG 1 ATOM 1855 C CD . ARG B 2 41 ? 46.137 26.234 -20.320 1.00 23.85 ? 39 ARG B CD 1 ATOM 1856 N NE . ARG B 2 41 ? 44.814 26.541 -19.788 1.00 21.35 ? 39 ARG B NE 1 ATOM 1857 C CZ . ARG B 2 41 ? 43.708 25.888 -20.135 1.00 28.58 ? 39 ARG B CZ 1 ATOM 1858 N NH1 . ARG B 2 41 ? 43.772 24.887 -21.003 1.00 18.71 ? 39 ARG B NH1 1 ATOM 1859 N NH2 . ARG B 2 41 ? 42.542 26.228 -19.608 1.00 32.88 ? 39 ARG B NH2 1 ATOM 1860 N N . PHE B 2 42 ? 50.036 25.886 -17.668 1.00 10.01 ? 40 PHE B N 1 ATOM 1861 C CA . PHE B 2 42 ? 50.789 24.724 -18.116 1.00 9.65 ? 40 PHE B CA 1 ATOM 1862 C C . PHE B 2 42 ? 49.806 23.589 -18.358 1.00 12.18 ? 40 PHE B C 1 ATOM 1863 O O . PHE B 2 42 ? 49.029 23.227 -17.478 1.00 12.65 ? 40 PHE B O 1 ATOM 1864 C CB . PHE B 2 42 ? 51.847 24.320 -17.080 1.00 8.29 ? 40 PHE B CB 1 ATOM 1865 C CG . PHE B 2 42 ? 52.600 23.055 -17.424 1.00 12.82 ? 40 PHE B CG 1 ATOM 1866 C CD1 . PHE B 2 42 ? 52.056 21.805 -17.160 1.00 9.81 ? 40 PHE B CD1 1 ATOM 1867 C CD2 . PHE B 2 42 ? 53.873 23.119 -17.970 1.00 9.24 ? 40 PHE B CD2 1 ATOM 1868 C CE1 . PHE B 2 42 ? 52.753 20.647 -17.466 1.00 14.70 ? 40 PHE B CE1 1 ATOM 1869 C CE2 . PHE B 2 42 ? 54.576 21.968 -18.273 1.00 9.77 ? 40 PHE B CE2 1 ATOM 1870 C CZ . PHE B 2 42 ? 54.014 20.729 -18.021 1.00 9.82 ? 40 PHE B CZ 1 ATOM 1871 N N . ASP B 2 43 ? 49.844 23.051 -19.570 1.00 14.48 ? 41 ASP B N 1 ATOM 1872 C CA . ASP B 2 43 ? 49.031 21.904 -19.953 1.00 15.64 ? 41 ASP B CA 1 ATOM 1873 C C . ASP B 2 43 ? 49.975 20.731 -20.177 1.00 13.43 ? 41 ASP B C 1 ATOM 1874 O O . ASP B 2 43 ? 50.897 20.837 -20.979 1.00 17.04 ? 41 ASP B O 1 ATOM 1875 C CB . ASP B 2 43 ? 48.226 22.244 -21.216 1.00 16.11 ? 41 ASP B CB 1 ATOM 1876 C CG . ASP B 2 43 ? 47.247 21.158 -21.622 1.00 16.94 ? 41 ASP B CG 1 ATOM 1877 O OD1 . ASP B 2 43 ? 47.363 20.007 -21.154 1.00 15.48 ? 41 ASP B OD1 1 ATOM 1878 O OD2 . ASP B 2 43 ? 46.342 21.474 -22.426 1.00 9.92 ? 41 ASP B OD2 1 ATOM 1879 N N . SER B 2 44 ? 49.757 19.616 -19.480 1.00 15.56 ? 42 SER B N 1 ATOM 1880 C CA . SER B 2 44 ? 50.640 18.454 -19.633 1.00 10.88 ? 42 SER B CA 1 ATOM 1881 C C . SER B 2 44 ? 50.613 17.902 -21.060 1.00 12.19 ? 42 SER B C 1 ATOM 1882 O O . SER B 2 44 ? 51.548 17.227 -21.489 1.00 13.97 ? 42 SER B O 1 ATOM 1883 C CB . SER B 2 44 ? 50.268 17.352 -18.634 1.00 12.30 ? 42 SER B CB 1 ATOM 1884 O OG . SER B 2 44 ? 48.962 16.852 -18.860 1.00 22.13 ? 42 SER B OG 1 ATOM 1885 N N . ASP B 2 45 ? 49.547 18.212 -21.794 1.00 10.84 ? 43 ASP B N 1 ATOM 1886 C CA . ASP B 2 45 ? 49.446 17.850 -23.204 1.00 16.76 ? 43 ASP B CA 1 ATOM 1887 C C . ASP B 2 45 ? 50.490 18.585 -24.040 1.00 20.99 ? 43 ASP B C 1 ATOM 1888 O O . ASP B 2 45 ? 50.862 18.138 -25.126 1.00 17.02 ? 43 ASP B O 1 ATOM 1889 C CB . ASP B 2 45 ? 48.053 18.164 -23.748 1.00 23.95 ? 43 ASP B CB 1 ATOM 1890 C CG . ASP B 2 45 ? 47.029 17.113 -23.379 1.00 25.35 ? 43 ASP B CG 1 ATOM 1891 O OD1 . ASP B 2 45 ? 47.361 16.197 -22.596 1.00 30.02 ? 43 ASP B OD1 1 ATOM 1892 O OD2 . ASP B 2 45 ? 45.893 17.195 -23.891 1.00 24.34 ? 43 ASP B OD2 1 ATOM 1893 N N . VAL B 2 46 ? 50.950 19.724 -23.533 1.00 11.39 ? 44 VAL B N 1 ATOM 1894 C CA . VAL B 2 46 ? 51.887 20.567 -24.265 1.00 12.82 ? 44 VAL B CA 1 ATOM 1895 C C . VAL B 2 46 ? 53.297 20.430 -23.692 1.00 13.03 ? 44 VAL B C 1 ATOM 1896 O O . VAL B 2 46 ? 54.263 20.222 -24.433 1.00 12.70 ? 44 VAL B O 1 ATOM 1897 C CB . VAL B 2 46 ? 51.443 22.048 -24.242 1.00 17.34 ? 44 VAL B CB 1 ATOM 1898 C CG1 . VAL B 2 46 ? 52.505 22.936 -24.865 1.00 11.63 ? 44 VAL B CG1 1 ATOM 1899 C CG2 . VAL B 2 46 ? 50.109 22.212 -24.971 1.00 17.30 ? 44 VAL B CG2 1 ATOM 1900 N N . GLY B 2 47 ? 53.425 20.582 -22.378 1.00 13.13 ? 45 GLY B N 1 ATOM 1901 C CA . GLY B 2 47 ? 54.706 20.369 -21.731 1.00 16.10 ? 45 GLY B CA 1 ATOM 1902 C C . GLY B 2 47 ? 55.452 21.671 -21.533 1.00 12.57 ? 45 GLY B C 1 ATOM 1903 O O . GLY B 2 47 ? 56.625 21.670 -21.161 1.00 18.68 ? 45 GLY B O 1 ATOM 1904 N N . GLU B 2 48 ? 54.767 22.778 -21.805 1.00 10.86 ? 46 GLU B N 1 ATOM 1905 C CA . GLU B 2 48 ? 55.288 24.120 -21.561 1.00 14.29 ? 46 GLU B CA 1 ATOM 1906 C C . GLU B 2 48 ? 54.143 25.029 -21.156 1.00 13.87 ? 46 GLU B C 1 ATOM 1907 O O . GLU B 2 48 ? 52.981 24.712 -21.400 1.00 12.79 ? 46 GLU B O 1 ATOM 1908 C CB . GLU B 2 48 ? 55.968 24.701 -22.806 1.00 16.11 ? 46 GLU B CB 1 ATOM 1909 C CG . GLU B 2 48 ? 57.354 24.178 -23.123 1.00 25.77 ? 46 GLU B CG 1 ATOM 1910 C CD . GLU B 2 48 ? 57.960 24.880 -24.330 1.00 31.80 ? 46 GLU B CD 1 ATOM 1911 O OE1 . GLU B 2 48 ? 57.232 25.646 -25.001 1.00 22.69 ? 46 GLU B OE1 1 ATOM 1912 O OE2 . GLU B 2 48 ? 59.164 24.674 -24.602 1.00 34.56 ? 46 GLU B OE2 1 ATOM 1913 N N . TYR B 2 49 ? 54.477 26.164 -20.550 1.00 14.66 ? 47 TYR B N 1 ATOM 1914 C CA . TYR B 2 49 ? 53.493 27.195 -20.260 1.00 9.39 ? 47 TYR B CA 1 ATOM 1915 C C . TYR B 2 49 ? 53.097 27.936 -21.537 1.00 17.30 ? 47 TYR B C 1 ATOM 1916 O O . TYR B 2 49 ? 53.920 28.138 -22.432 1.00 18.28 ? 47 TYR B O 1 ATOM 1917 C CB . TYR B 2 49 ? 54.030 28.171 -19.214 1.00 9.16 ? 47 TYR B CB 1 ATOM 1918 C CG . TYR B 2 49 ? 53.986 27.632 -17.801 1.00 8.76 ? 47 TYR B CG 1 ATOM 1919 C CD1 . TYR B 2 49 ? 55.063 26.936 -17.267 1.00 12.42 ? 47 TYR B CD1 1 ATOM 1920 C CD2 . TYR B 2 49 ? 52.864 27.815 -17.002 1.00 14.31 ? 47 TYR B CD2 1 ATOM 1921 C CE1 . TYR B 2 49 ? 55.027 26.446 -15.970 1.00 11.79 ? 47 TYR B CE1 1 ATOM 1922 C CE2 . TYR B 2 49 ? 52.819 27.329 -15.711 1.00 8.42 ? 47 TYR B CE2 1 ATOM 1923 C CZ . TYR B 2 49 ? 53.902 26.645 -15.198 1.00 12.61 ? 47 TYR B CZ 1 ATOM 1924 O OH . TYR B 2 49 ? 53.860 26.154 -13.910 1.00 14.56 ? 47 TYR B OH 1 ATOM 1925 N N . ARG B 2 50 ? 51.832 28.332 -21.620 1.00 12.15 ? 48 ARG B N 1 ATOM 1926 C CA . ARG B 2 50 ? 51.352 29.149 -22.729 1.00 16.00 ? 48 ARG B CA 1 ATOM 1927 C C . ARG B 2 50 ? 50.519 30.303 -22.189 1.00 16.51 ? 48 ARG B C 1 ATOM 1928 O O . ARG B 2 50 ? 49.708 30.113 -21.282 1.00 16.43 ? 48 ARG B O 1 ATOM 1929 C CB . ARG B 2 50 ? 50.521 28.313 -23.702 1.00 11.98 ? 48 ARG B CB 1 ATOM 1930 C CG . ARG B 2 50 ? 51.291 27.219 -24.430 1.00 18.65 ? 48 ARG B CG 1 ATOM 1931 C CD . ARG B 2 50 ? 52.184 27.787 -25.513 1.00 19.51 ? 48 ARG B CD 1 ATOM 1932 N NE . ARG B 2 50 ? 52.886 26.738 -26.248 1.00 27.57 ? 48 ARG B NE 1 ATOM 1933 C CZ . ARG B 2 50 ? 54.167 26.431 -26.073 1.00 30.31 ? 48 ARG B CZ 1 ATOM 1934 N NH1 . ARG B 2 50 ? 54.898 27.103 -25.194 1.00 39.02 ? 48 ARG B NH1 1 ATOM 1935 N NH2 . ARG B 2 50 ? 54.723 25.460 -26.784 1.00 31.95 ? 48 ARG B NH2 1 ATOM 1936 N N . ALA B 2 51 ? 50.739 31.500 -22.721 1.00 19.26 ? 49 ALA B N 1 ATOM 1937 C CA . ALA B 2 51 ? 49.933 32.642 -22.322 1.00 20.20 ? 49 ALA B CA 1 ATOM 1938 C C . ALA B 2 51 ? 48.502 32.438 -22.790 1.00 20.50 ? 49 ALA B C 1 ATOM 1939 O O . ALA B 2 51 ? 48.254 32.056 -23.936 1.00 20.09 ? 49 ALA B O 1 ATOM 1940 C CB . ALA B 2 51 ? 50.500 33.928 -22.886 1.00 14.93 ? 49 ALA B CB 1 ATOM 1941 N N . VAL B 2 52 ? 47.556 32.717 -21.905 1.00 20.15 ? 50 VAL B N 1 ATOM 1942 C CA . VAL B 2 52 ? 46.150 32.648 -22.263 1.00 13.39 ? 50 VAL B CA 1 ATOM 1943 C C . VAL B 2 52 ? 45.717 34.036 -22.701 1.00 15.11 ? 50 VAL B C 1 ATOM 1944 O O . VAL B 2 52 ? 44.871 34.182 -23.579 1.00 19.08 ? 50 VAL B O 1 ATOM 1945 C CB . VAL B 2 52 ? 45.290 32.116 -21.098 1.00 14.90 ? 50 VAL B CB 1 ATOM 1946 C CG1 . VAL B 2 52 ? 43.808 32.074 -21.482 1.00 9.14 ? 50 VAL B CG1 1 ATOM 1947 C CG2 . VAL B 2 52 ? 45.773 30.725 -20.694 1.00 10.86 ? 50 VAL B CG2 1 ATOM 1948 N N . THR B 2 53 ? 46.287 35.060 -22.073 1.00 9.88 ? 51 THR B N 1 ATOM 1949 C CA . THR B 2 53 ? 46.067 36.427 -22.526 1.00 19.86 ? 51 THR B CA 1 ATOM 1950 C C . THR B 2 53 ? 47.430 37.099 -22.600 1.00 20.06 ? 51 THR B C 1 ATOM 1951 O O . THR B 2 53 ? 48.418 36.541 -22.111 1.00 14.75 ? 51 THR B O 1 ATOM 1952 C CB . THR B 2 53 ? 45.160 37.221 -21.573 1.00 22.05 ? 51 THR B CB 1 ATOM 1953 O OG1 . THR B 2 53 ? 45.846 37.416 -20.333 1.00 23.36 ? 51 THR B OG1 1 ATOM 1954 C CG2 . THR B 2 53 ? 43.836 36.489 -21.323 1.00 16.56 ? 51 THR B CG2 1 ATOM 1955 N N . GLU B 2 54 ? 47.485 38.296 -23.181 1.00 11.34 ? 52 GLU B N 1 ATOM 1956 C CA . GLU B 2 54 ? 48.754 39.010 -23.315 1.00 25.11 ? 52 GLU B CA 1 ATOM 1957 C C . GLU B 2 54 ? 49.427 39.271 -21.981 1.00 20.50 ? 52 GLU B C 1 ATOM 1958 O O . GLU B 2 54 ? 50.653 39.260 -21.861 1.00 17.27 ? 52 GLU B O 1 ATOM 1959 C CB . GLU B 2 54 ? 48.525 40.363 -24.002 1.00 29.03 ? 52 GLU B CB 1 ATOM 1960 C CG . GLU B 2 54 ? 47.873 40.307 -25.365 1.00 53.41 ? 52 GLU B CG 1 ATOM 1961 C CD . GLU B 2 54 ? 47.917 41.650 -26.075 1.00 69.03 ? 52 GLU B CD 1 ATOM 1962 O OE1 . GLU B 2 54 ? 46.943 42.424 -25.944 1.00 66.58 ? 52 GLU B OE1 1 ATOM 1963 O OE2 . GLU B 2 54 ? 48.927 41.940 -26.752 1.00 76.65 ? 52 GLU B OE2 1 ATOM 1964 N N . LEU B 2 55 ? 48.583 39.494 -20.983 1.00 19.51 ? 53 LEU B N 1 ATOM 1965 C CA A LEU B 2 55 ? 49.002 39.755 -19.610 0.61 22.91 ? 53 LEU B CA 1 ATOM 1966 C CA B LEU B 2 55 ? 49.025 39.764 -19.623 0.39 22.08 ? 53 LEU B CA 1 ATOM 1967 C C . LEU B 2 55 ? 49.890 38.644 -19.032 1.00 19.26 ? 53 LEU B C 1 ATOM 1968 O O . LEU B 2 55 ? 50.691 38.879 -18.125 1.00 13.42 ? 53 LEU B O 1 ATOM 1969 C CB A LEU B 2 55 ? 47.758 39.928 -18.732 0.61 25.70 ? 53 LEU B CB 1 ATOM 1970 C CB B LEU B 2 55 ? 47.814 40.070 -18.746 0.39 25.29 ? 53 LEU B CB 1 ATOM 1971 C CG A LEU B 2 55 ? 47.827 40.772 -17.460 0.61 27.50 ? 53 LEU B CG 1 ATOM 1972 C CG B LEU B 2 55 ? 48.032 41.173 -17.705 0.39 26.83 ? 53 LEU B CG 1 ATOM 1973 C CD1 A LEU B 2 55 ? 47.871 42.255 -17.800 0.61 25.41 ? 53 LEU B CD1 1 ATOM 1974 C CD1 B LEU B 2 55 ? 49.284 41.982 -18.000 0.39 27.95 ? 53 LEU B CD1 1 ATOM 1975 C CD2 A LEU B 2 55 ? 46.641 40.453 -16.556 0.61 27.62 ? 53 LEU B CD2 1 ATOM 1976 C CD2 B LEU B 2 55 ? 46.824 42.094 -17.663 0.39 25.54 ? 53 LEU B CD2 1 ATOM 1977 N N . GLY B 2 56 ? 49.730 37.427 -19.548 1.00 13.34 ? 54 GLY B N 1 ATOM 1978 C CA . GLY B 2 56 ? 50.438 36.284 -19.000 1.00 13.62 ? 54 GLY B CA 1 ATOM 1979 C C . GLY B 2 56 ? 51.694 35.908 -19.768 1.00 17.05 ? 54 GLY B C 1 ATOM 1980 O O . GLY B 2 56 ? 52.404 34.976 -19.390 1.00 15.62 ? 54 GLY B O 1 ATOM 1981 N N . ARG B 2 57 ? 51.961 36.632 -20.851 1.00 10.34 ? 55 ARG B N 1 ATOM 1982 C CA . ARG B 2 57 ? 53.108 36.349 -21.720 1.00 21.62 ? 55 ARG B CA 1 ATOM 1983 C C . ARG B 2 57 ? 54.472 36.406 -21.018 1.00 23.08 ? 55 ARG B C 1 ATOM 1984 O O . ARG B 2 57 ? 55.306 35.534 -21.254 1.00 22.44 ? 55 ARG B O 1 ATOM 1985 C CB . ARG B 2 57 ? 53.134 37.278 -22.936 1.00 21.25 ? 55 ARG B CB 1 ATOM 1986 C CG . ARG B 2 57 ? 52.011 37.034 -23.917 1.00 39.51 ? 55 ARG B CG 1 ATOM 1987 C CD . ARG B 2 57 ? 51.982 38.096 -24.994 1.00 51.86 ? 55 ARG B CD 1 ATOM 1988 N NE . ARG B 2 57 ? 50.911 37.856 -25.953 1.00 58.61 ? 55 ARG B NE 1 ATOM 1989 C CZ . ARG B 2 57 ? 50.497 38.747 -26.845 1.00 69.32 ? 55 ARG B CZ 1 ATOM 1990 N NH1 . ARG B 2 57 ? 51.066 39.944 -26.902 1.00 75.95 ? 55 ARG B NH1 1 ATOM 1991 N NH2 . ARG B 2 57 ? 49.514 38.443 -27.679 1.00 71.62 ? 55 ARG B NH2 1 ATOM 1992 N N . PRO B 2 58 ? 54.710 37.419 -20.164 1.00 18.79 ? 56 PRO B N 1 ATOM 1993 C CA . PRO B 2 58 ? 56.024 37.450 -19.518 1.00 14.64 ? 56 PRO B CA 1 ATOM 1994 C C . PRO B 2 58 ? 56.245 36.215 -18.659 1.00 11.43 ? 56 PRO B C 1 ATOM 1995 O O . PRO B 2 58 ? 57.363 35.711 -18.584 1.00 16.61 ? 56 PRO B O 1 ATOM 1996 C CB . PRO B 2 58 ? 55.960 38.713 -18.649 1.00 16.76 ? 56 PRO B CB 1 ATOM 1997 C CG . PRO B 2 58 ? 54.968 39.584 -19.338 1.00 14.94 ? 56 PRO B CG 1 ATOM 1998 C CD . PRO B 2 58 ? 53.933 38.635 -19.856 1.00 15.98 ? 56 PRO B CD 1 ATOM 1999 N N . ASP B 2 59 ? 55.190 35.744 -18.010 1.00 18.11 ? 57 ASP B N 1 ATOM 2000 C CA . ASP B 2 59 ? 55.290 34.586 -17.139 1.00 15.00 ? 57 ASP B CA 1 ATOM 2001 C C . ASP B 2 59 ? 55.538 33.306 -17.922 1.00 14.84 ? 57 ASP B C 1 ATOM 2002 O O . ASP B 2 59 ? 56.358 32.490 -17.525 1.00 16.67 ? 57 ASP B O 1 ATOM 2003 C CB . ASP B 2 59 ? 53.993 34.454 -16.356 1.00 16.97 ? 57 ASP B CB 1 ATOM 2004 C CG . ASP B 2 59 ? 53.815 35.579 -15.380 1.00 20.32 ? 57 ASP B CG 1 ATOM 2005 O OD1 . ASP B 2 59 ? 54.838 36.089 -14.871 1.00 15.67 ? 57 ASP B OD1 1 ATOM 2006 O OD2 . ASP B 2 59 ? 52.658 35.982 -15.157 1.00 19.08 ? 57 ASP B OD2 1 ATOM 2007 N N . ALA B 2 60 ? 54.843 33.146 -19.046 1.00 15.69 ? 58 ALA B N 1 ATOM 2008 C CA . ALA B 2 60 ? 55.044 31.990 -19.916 1.00 9.88 ? 58 ALA B CA 1 ATOM 2009 C C . ALA B 2 60 ? 56.500 31.887 -20.359 1.00 18.88 ? 58 ALA B C 1 ATOM 2010 O O . ALA B 2 60 ? 57.116 30.829 -20.289 1.00 17.31 ? 58 ALA B O 1 ATOM 2011 C CB . ALA B 2 60 ? 54.130 32.072 -21.128 1.00 15.65 ? 58 ALA B CB 1 ATOM 2012 N N . GLU B 2 61 ? 57.040 33.013 -20.803 1.00 17.91 ? 59 GLU B N 1 ATOM 2013 C CA . GLU B 2 61 ? 58.405 33.088 -21.303 1.00 20.72 ? 59 GLU B CA 1 ATOM 2014 C C . GLU B 2 61 ? 59.434 32.908 -20.184 1.00 17.96 ? 59 GLU B C 1 ATOM 2015 O O . GLU B 2 61 ? 60.432 32.220 -20.370 1.00 23.28 ? 59 GLU B O 1 ATOM 2016 C CB . GLU B 2 61 ? 58.592 34.409 -22.053 1.00 24.22 ? 59 GLU B CB 1 ATOM 2017 C CG . GLU B 2 61 ? 57.590 34.515 -23.211 1.00 41.63 ? 59 GLU B CG 1 ATOM 2018 C CD . GLU B 2 61 ? 57.671 35.814 -23.986 1.00 48.82 ? 59 GLU B CD 1 ATOM 2019 O OE1 . GLU B 2 61 ? 58.332 36.758 -23.506 1.00 46.51 ? 59 GLU B OE1 1 ATOM 2020 O OE2 . GLU B 2 61 ? 57.063 35.888 -25.078 1.00 48.78 ? 59 GLU B OE2 1 ATOM 2021 N N . TYR B 2 62 ? 59.184 33.500 -19.020 1.00 19.75 ? 60 TYR B N 1 ATOM 2022 C CA . TYR B 2 62 ? 60.119 33.375 -17.903 1.00 20.08 ? 60 TYR B CA 1 ATOM 2023 C C . TYR B 2 62 ? 60.138 31.934 -17.400 1.00 16.05 ? 60 TYR B C 1 ATOM 2024 O O . TYR B 2 62 ? 61.201 31.344 -17.211 1.00 23.64 ? 60 TYR B O 1 ATOM 2025 C CB . TYR B 2 62 ? 59.746 34.336 -16.772 1.00 16.17 ? 60 TYR B CB 1 ATOM 2026 C CG . TYR B 2 62 ? 60.646 34.255 -15.554 1.00 19.09 ? 60 TYR B CG 1 ATOM 2027 C CD1 . TYR B 2 62 ? 62.030 34.318 -15.671 1.00 17.98 ? 60 TYR B CD1 1 ATOM 2028 C CD2 . TYR B 2 62 ? 60.103 34.116 -14.282 1.00 20.17 ? 60 TYR B CD2 1 ATOM 2029 C CE1 . TYR B 2 62 ? 62.849 34.239 -14.552 1.00 20.28 ? 60 TYR B CE1 1 ATOM 2030 C CE2 . TYR B 2 62 ? 60.908 34.042 -13.161 1.00 30.53 ? 60 TYR B CE2 1 ATOM 2031 C CZ . TYR B 2 62 ? 62.280 34.103 -13.297 1.00 32.53 ? 60 TYR B CZ 1 ATOM 2032 O OH . TYR B 2 62 ? 63.075 34.025 -12.173 1.00 37.22 ? 60 TYR B OH 1 ATOM 2033 N N . TRP B 2 63 ? 58.954 31.369 -17.199 1.00 15.27 ? 61 TRP B N 1 ATOM 2034 C CA . TRP B 2 63 ? 58.835 30.008 -16.690 1.00 15.01 ? 61 TRP B CA 1 ATOM 2035 C C . TRP B 2 63 ? 59.341 28.976 -17.694 1.00 18.68 ? 61 TRP B C 1 ATOM 2036 O O . TRP B 2 63 ? 59.957 27.981 -17.302 1.00 17.29 ? 61 TRP B O 1 ATOM 2037 C CB . TRP B 2 63 ? 57.386 29.725 -16.273 1.00 13.05 ? 61 TRP B CB 1 ATOM 2038 C CG . TRP B 2 63 ? 56.952 30.556 -15.087 1.00 15.21 ? 61 TRP B CG 1 ATOM 2039 C CD1 . TRP B 2 63 ? 57.758 31.303 -14.274 1.00 16.97 ? 61 TRP B CD1 1 ATOM 2040 C CD2 . TRP B 2 63 ? 55.611 30.780 -14.630 1.00 8.70 ? 61 TRP B CD2 1 ATOM 2041 N NE1 . TRP B 2 63 ? 57.010 31.932 -13.308 1.00 10.13 ? 61 TRP B NE1 1 ATOM 2042 C CE2 . TRP B 2 63 ? 55.688 31.638 -13.512 1.00 14.20 ? 61 TRP B CE2 1 ATOM 2043 C CE3 . TRP B 2 63 ? 54.356 30.327 -15.046 1.00 8.33 ? 61 TRP B CE3 1 ATOM 2044 C CZ2 . TRP B 2 63 ? 54.557 32.052 -12.809 1.00 15.38 ? 61 TRP B CZ2 1 ATOM 2045 C CZ3 . TRP B 2 63 ? 53.235 30.738 -14.345 1.00 9.76 ? 61 TRP B CZ3 1 ATOM 2046 C CH2 . TRP B 2 63 ? 53.343 31.586 -13.238 1.00 11.93 ? 61 TRP B CH2 1 ATOM 2047 N N . ASN B 2 64 ? 59.121 29.211 -18.984 1.00 17.77 ? 62 ASN B N 1 ATOM 2048 C CA . ASN B 2 64 ? 59.607 28.267 -19.983 1.00 19.06 ? 62 ASN B CA 1 ATOM 2049 C C . ASN B 2 64 ? 61.127 28.268 -20.104 1.00 17.61 ? 62 ASN B C 1 ATOM 2050 O O . ASN B 2 64 ? 61.709 27.338 -20.660 1.00 18.91 ? 62 ASN B O 1 ATOM 2051 C CB . ASN B 2 64 ? 58.975 28.556 -21.351 1.00 11.66 ? 62 ASN B CB 1 ATOM 2052 C CG . ASN B 2 64 ? 57.522 28.107 -21.428 1.00 11.46 ? 62 ASN B CG 1 ATOM 2053 O OD1 . ASN B 2 64 ? 57.070 27.302 -20.614 1.00 12.49 ? 62 ASN B OD1 1 ATOM 2054 N ND2 . ASN B 2 64 ? 56.792 28.614 -22.415 1.00 11.21 ? 62 ASN B ND2 1 ATOM 2055 N N . SER B 2 65 ? 61.772 29.303 -19.577 1.00 13.57 ? 63 SER B N 1 ATOM 2056 C CA . SER B 2 65 ? 63.229 29.365 -19.608 1.00 13.39 ? 63 SER B CA 1 ATOM 2057 C C . SER B 2 65 ? 63.854 28.594 -18.452 1.00 16.18 ? 63 SER B C 1 ATOM 2058 O O . SER B 2 65 ? 65.071 28.448 -18.386 1.00 17.29 ? 63 SER B O 1 ATOM 2059 C CB . SER B 2 65 ? 63.702 30.818 -19.553 1.00 19.70 ? 63 SER B CB 1 ATOM 2060 O OG . SER B 2 65 ? 63.613 31.327 -18.230 1.00 17.22 ? 63 SER B OG 1 ATOM 2061 N N . GLN B 2 66 ? 63.017 28.110 -17.539 1.00 14.39 ? 64 GLN B N 1 ATOM 2062 C CA . GLN B 2 66 ? 63.494 27.369 -16.377 1.00 16.21 ? 64 GLN B CA 1 ATOM 2063 C C . GLN B 2 66 ? 63.245 25.879 -16.560 1.00 19.36 ? 64 GLN B C 1 ATOM 2064 O O . GLN B 2 66 ? 62.157 25.376 -16.268 1.00 20.18 ? 64 GLN B O 1 ATOM 2065 C CB . GLN B 2 66 ? 62.843 27.886 -15.098 1.00 16.74 ? 64 GLN B CB 1 ATOM 2066 C CG . GLN B 2 66 ? 63.060 29.374 -14.883 1.00 17.75 ? 64 GLN B CG 1 ATOM 2067 C CD . GLN B 2 66 ? 62.337 29.898 -13.664 1.00 30.73 ? 64 GLN B CD 1 ATOM 2068 O OE1 . GLN B 2 66 ? 62.247 29.216 -12.642 1.00 36.38 ? 64 GLN B OE1 1 ATOM 2069 N NE2 . GLN B 2 66 ? 61.793 31.102 -13.770 1.00 31.02 ? 64 GLN B NE2 1 ATOM 2070 N N . LYS B 2 67 ? 64.274 25.187 -17.036 1.00 20.26 ? 65 LYS B N 1 ATOM 2071 C CA A LYS B 2 67 ? 64.216 23.760 -17.343 0.49 21.11 ? 65 LYS B CA 1 ATOM 2072 C CA B LYS B 2 67 ? 64.164 23.773 -17.364 0.51 21.14 ? 65 LYS B CA 1 ATOM 2073 C C . LYS B 2 67 ? 63.771 22.907 -16.162 1.00 17.93 ? 65 LYS B C 1 ATOM 2074 O O . LYS B 2 67 ? 62.943 22.006 -16.296 1.00 16.63 ? 65 LYS B O 1 ATOM 2075 C CB A LYS B 2 67 ? 65.588 23.277 -17.821 0.49 21.62 ? 65 LYS B CB 1 ATOM 2076 C CB B LYS B 2 67 ? 65.491 23.289 -17.950 0.51 20.15 ? 65 LYS B CB 1 ATOM 2077 C CG A LYS B 2 67 ? 66.737 23.669 -16.898 0.49 27.75 ? 65 LYS B CG 1 ATOM 2078 C CG B LYS B 2 67 ? 65.745 21.800 -17.818 0.51 21.71 ? 65 LYS B CG 1 ATOM 2079 C CD A LYS B 2 67 ? 68.080 23.216 -17.437 0.49 31.39 ? 65 LYS B CD 1 ATOM 2080 C CD B LYS B 2 67 ? 64.994 21.011 -18.869 0.51 21.36 ? 65 LYS B CD 1 ATOM 2081 C CE A LYS B 2 67 ? 69.224 23.878 -16.685 0.49 30.27 ? 65 LYS B CE 1 ATOM 2082 C CE B LYS B 2 67 ? 65.412 19.552 -18.834 0.51 15.95 ? 65 LYS B CE 1 ATOM 2083 N NZ A LYS B 2 67 ? 70.511 23.746 -17.424 0.49 24.20 ? 65 LYS B NZ 1 ATOM 2084 N NZ B LYS B 2 67 ? 64.736 18.754 -19.887 0.51 16.06 ? 65 LYS B NZ 1 ATOM 2085 N N . ASP B 2 68 ? 64.336 23.200 -14.996 1.00 18.03 ? 66 ASP B N 1 ATOM 2086 C CA . ASP B 2 68 ? 64.036 22.462 -13.779 1.00 19.69 ? 66 ASP B CA 1 ATOM 2087 C C . ASP B 2 68 ? 62.578 22.634 -13.385 1.00 20.74 ? 66 ASP B C 1 ATOM 2088 O O . ASP B 2 68 ? 61.919 21.674 -12.986 1.00 17.30 ? 66 ASP B O 1 ATOM 2089 C CB . ASP B 2 68 ? 64.973 22.896 -12.647 1.00 27.85 ? 66 ASP B CB 1 ATOM 2090 C CG . ASP B 2 68 ? 64.968 24.397 -12.421 1.00 33.97 ? 66 ASP B CG 1 ATOM 2091 O OD1 . ASP B 2 68 ? 64.604 25.145 -13.354 1.00 31.15 ? 66 ASP B OD1 1 ATOM 2092 O OD2 . ASP B 2 68 ? 65.350 24.828 -11.313 1.00 41.31 ? 66 ASP B OD2 1 ATOM 2093 N N . LEU B 2 69 ? 62.080 23.860 -13.503 1.00 16.20 ? 67 LEU B N 1 ATOM 2094 C CA . LEU B 2 69 ? 60.680 24.143 -13.224 1.00 19.89 ? 67 LEU B CA 1 ATOM 2095 C C . LEU B 2 69 ? 59.766 23.363 -14.173 1.00 22.00 ? 67 LEU B C 1 ATOM 2096 O O . LEU B 2 69 ? 58.790 22.751 -13.734 1.00 18.28 ? 67 LEU B O 1 ATOM 2097 C CB . LEU B 2 69 ? 60.399 25.645 -13.332 1.00 14.73 ? 67 LEU B CB 1 ATOM 2098 C CG . LEU B 2 69 ? 58.919 26.033 -13.332 1.00 24.55 ? 67 LEU B CG 1 ATOM 2099 C CD1 . LEU B 2 69 ? 58.269 25.662 -12.008 1.00 28.60 ? 67 LEU B CD1 1 ATOM 2100 C CD2 . LEU B 2 69 ? 58.745 27.516 -13.613 1.00 34.37 ? 67 LEU B CD2 1 ATOM 2101 N N . LEU B 2 70 ? 60.089 23.381 -15.464 1.00 16.00 ? 68 LEU B N 1 ATOM 2102 C CA . LEU B 2 70 ? 59.287 22.679 -16.462 1.00 20.76 ? 68 LEU B CA 1 ATOM 2103 C C . LEU B 2 70 ? 59.248 21.167 -16.221 1.00 23.77 ? 68 LEU B C 1 ATOM 2104 O O . LEU B 2 70 ? 58.196 20.546 -16.363 1.00 23.78 ? 68 LEU B O 1 ATOM 2105 C CB . LEU B 2 70 ? 59.818 22.966 -17.871 1.00 20.86 ? 68 LEU B CB 1 ATOM 2106 C CG . LEU B 2 70 ? 59.556 24.376 -18.407 1.00 18.81 ? 68 LEU B CG 1 ATOM 2107 C CD1 . LEU B 2 70 ? 60.021 24.500 -19.844 1.00 27.34 ? 68 LEU B CD1 1 ATOM 2108 C CD2 . LEU B 2 70 ? 58.082 24.736 -18.290 1.00 16.36 ? 68 LEU B CD2 1 ATOM 2109 N N . GLU B 2 71 ? 60.385 20.581 -15.850 1.00 16.13 ? 69 GLU B N 1 ATOM 2110 C CA . GLU B 2 71 ? 60.441 19.145 -15.563 1.00 12.43 ? 69 GLU B CA 1 ATOM 2111 C C . GLU B 2 71 ? 59.643 18.789 -14.311 1.00 12.49 ? 69 GLU B C 1 ATOM 2112 O O . GLU B 2 71 ? 59.111 17.685 -14.202 1.00 15.50 ? 69 GLU B O 1 ATOM 2113 C CB . GLU B 2 71 ? 61.887 18.660 -15.436 1.00 13.80 ? 69 GLU B CB 1 ATOM 2114 C CG . GLU B 2 71 ? 62.658 18.696 -16.752 1.00 15.60 ? 69 GLU B CG 1 ATOM 2115 C CD . GLU B 2 71 ? 62.013 17.845 -17.846 1.00 21.97 ? 69 GLU B CD 1 ATOM 2116 O OE1 . GLU B 2 71 ? 61.242 16.915 -17.519 1.00 25.77 ? 69 GLU B OE1 1 ATOM 2117 O OE2 . GLU B 2 71 ? 62.281 18.110 -19.038 1.00 22.96 ? 69 GLU B OE2 1 ATOM 2118 N N . GLN B 2 72 ? 59.573 19.710 -13.360 1.00 11.54 ? 70 GLN B N 1 ATOM 2119 C CA . GLN B 2 72 ? 58.727 19.496 -12.197 1.00 20.67 ? 70 GLN B CA 1 ATOM 2120 C C . GLN B 2 72 ? 57.281 19.386 -12.668 1.00 17.21 ? 70 GLN B C 1 ATOM 2121 O O . GLN B 2 72 ? 56.541 18.503 -12.236 1.00 10.46 ? 70 GLN B O 1 ATOM 2122 C CB . GLN B 2 72 ? 58.867 20.640 -11.186 1.00 17.29 ? 70 GLN B CB 1 ATOM 2123 C CG . GLN B 2 72 ? 60.120 20.584 -10.333 1.00 35.85 ? 70 GLN B CG 1 ATOM 2124 C CD . GLN B 2 72 ? 60.125 19.403 -9.379 1.00 49.82 ? 70 GLN B CD 1 ATOM 2125 O OE1 . GLN B 2 72 ? 59.087 19.024 -8.836 1.00 54.90 ? 70 GLN B OE1 1 ATOM 2126 N NE2 . GLN B 2 72 ? 61.295 18.810 -9.177 1.00 53.70 ? 70 GLN B NE2 1 ATOM 2127 N N . LYS B 2 73 ? 56.874 20.326 -13.515 1.00 11.18 ? 71 LYS B N 1 ATOM 2128 C CA . LYS B 2 73 ? 55.512 20.350 -14.027 1.00 11.66 ? 71 LYS B CA 1 ATOM 2129 C C . LYS B 2 73 ? 55.220 19.154 -14.939 1.00 11.84 ? 71 LYS B C 1 ATOM 2130 O O . LYS B 2 73 ? 54.117 18.613 -14.935 1.00 16.53 ? 71 LYS B O 1 ATOM 2131 C CB . LYS B 2 73 ? 55.255 21.655 -14.782 1.00 9.33 ? 71 LYS B CB 1 ATOM 2132 C CG . LYS B 2 73 ? 55.357 22.907 -13.917 1.00 13.33 ? 71 LYS B CG 1 ATOM 2133 C CD . LYS B 2 73 ? 54.341 22.949 -12.781 1.00 13.67 ? 71 LYS B CD 1 ATOM 2134 C CE . LYS B 2 73 ? 54.769 23.985 -11.747 1.00 16.29 ? 71 LYS B CE 1 ATOM 2135 N NZ . LYS B 2 73 ? 53.893 24.030 -10.543 1.00 15.50 ? 71 LYS B NZ 1 ATOM 2136 N N . ARG B 2 74 ? 56.216 18.745 -15.721 1.00 15.31 ? 72 ARG B N 1 ATOM 2137 C CA . ARG B 2 74 ? 56.069 17.602 -16.623 1.00 20.07 ? 72 ARG B CA 1 ATOM 2138 C C . ARG B 2 74 ? 55.920 16.263 -15.907 1.00 22.41 ? 72 ARG B C 1 ATOM 2139 O O . ARG B 2 74 ? 55.364 15.317 -16.462 1.00 12.92 ? 72 ARG B O 1 ATOM 2140 C CB . ARG B 2 74 ? 57.250 17.534 -17.594 1.00 25.37 ? 72 ARG B CB 1 ATOM 2141 C CG . ARG B 2 74 ? 57.207 18.586 -18.688 1.00 23.30 ? 72 ARG B CG 1 ATOM 2142 C CD . ARG B 2 74 ? 58.539 18.727 -19.395 1.00 19.30 ? 72 ARG B CD 1 ATOM 2143 N NE . ARG B 2 74 ? 58.539 19.877 -20.293 1.00 18.59 ? 72 ARG B NE 1 ATOM 2144 C CZ . ARG B 2 74 ? 59.606 20.299 -20.959 1.00 20.82 ? 72 ARG B CZ 1 ATOM 2145 N NH1 . ARG B 2 74 ? 60.764 19.672 -20.809 1.00 20.13 ? 72 ARG B NH1 1 ATOM 2146 N NH2 . ARG B 2 74 ? 59.521 21.355 -21.758 1.00 23.21 ? 72 ARG B NH2 1 ATOM 2147 N N . ALA B 2 75 ? 56.414 16.183 -14.677 1.00 16.62 ? 73 ALA B N 1 ATOM 2148 C CA . ALA B 2 75 ? 56.343 14.943 -13.916 1.00 17.90 ? 73 ALA B CA 1 ATOM 2149 C C . ALA B 2 75 ? 55.096 14.909 -13.039 1.00 13.76 ? 73 ALA B C 1 ATOM 2150 O O . ALA B 2 75 ? 54.795 13.889 -12.421 1.00 23.65 ? 73 ALA B O 1 ATOM 2151 C CB . ALA B 2 75 ? 57.600 14.767 -13.063 1.00 18.74 ? 73 ALA B CB 1 ATOM 2152 N N . ALA B 2 76 ? 54.374 16.026 -12.994 1.00 13.72 ? 74 ALA B N 1 ATOM 2153 C CA . ALA B 2 76 ? 53.252 16.180 -12.071 1.00 16.01 ? 74 ALA B CA 1 ATOM 2154 C C . ALA B 2 76 ? 52.162 15.119 -12.248 1.00 13.21 ? 74 ALA B C 1 ATOM 2155 O O . ALA B 2 76 ? 51.558 14.695 -11.264 1.00 16.92 ? 74 ALA B O 1 ATOM 2156 C CB . ALA B 2 76 ? 52.650 17.579 -12.208 1.00 12.00 ? 74 ALA B CB 1 ATOM 2157 N N . VAL B 2 77 ? 51.897 14.696 -13.483 1.00 14.24 ? 75 VAL B N 1 ATOM 2158 C CA . VAL B 2 77 ? 50.886 13.661 -13.710 1.00 13.70 ? 75 VAL B CA 1 ATOM 2159 C C . VAL B 2 77 ? 51.209 12.404 -12.899 1.00 12.12 ? 75 VAL B C 1 ATOM 2160 O O . VAL B 2 77 ? 50.307 11.686 -12.477 1.00 19.88 ? 75 VAL B O 1 ATOM 2161 C CB . VAL B 2 77 ? 50.739 13.285 -15.203 1.00 13.42 ? 75 VAL B CB 1 ATOM 2162 C CG1 . VAL B 2 77 ? 49.971 14.367 -15.959 1.00 15.09 ? 75 VAL B CG1 1 ATOM 2163 C CG2 . VAL B 2 77 ? 52.104 12.997 -15.843 1.00 13.53 ? 75 VAL B CG2 1 ATOM 2164 N N . ASP B 2 78 ? 52.497 12.154 -12.678 1.00 15.25 ? 76 ASP B N 1 ATOM 2165 C CA . ASP B 2 78 ? 52.930 11.009 -11.881 1.00 18.71 ? 76 ASP B CA 1 ATOM 2166 C C . ASP B 2 78 ? 53.096 11.369 -10.403 1.00 21.13 ? 76 ASP B C 1 ATOM 2167 O O . ASP B 2 78 ? 52.497 10.745 -9.529 1.00 19.80 ? 76 ASP B O 1 ATOM 2168 C CB . ASP B 2 78 ? 54.241 10.437 -12.431 1.00 18.93 ? 76 ASP B CB 1 ATOM 2169 C CG . ASP B 2 78 ? 54.069 9.796 -13.795 1.00 24.80 ? 76 ASP B CG 1 ATOM 2170 O OD1 . ASP B 2 78 ? 52.953 9.316 -14.092 1.00 26.50 ? 76 ASP B OD1 1 ATOM 2171 O OD2 . ASP B 2 78 ? 55.047 9.781 -14.574 1.00 32.18 ? 76 ASP B OD2 1 ATOM 2172 N N . THR B 2 79 ? 53.907 12.385 -10.127 1.00 19.37 ? 77 THR B N 1 ATOM 2173 C CA . THR B 2 79 ? 54.313 12.688 -8.756 1.00 21.27 ? 77 THR B CA 1 ATOM 2174 C C . THR B 2 79 ? 53.245 13.428 -7.957 1.00 19.00 ? 77 THR B C 1 ATOM 2175 O O . THR B 2 79 ? 53.302 13.490 -6.728 1.00 16.09 ? 77 THR B O 1 ATOM 2176 C CB . THR B 2 79 ? 55.580 13.552 -8.741 1.00 19.66 ? 77 THR B CB 1 ATOM 2177 O OG1 . THR B 2 79 ? 55.289 14.814 -9.354 1.00 19.85 ? 77 THR B OG1 1 ATOM 2178 C CG2 . THR B 2 79 ? 56.714 12.866 -9.496 1.00 21.55 ? 77 THR B CG2 1 ATOM 2179 N N . TYR B 2 80 ? 52.277 13.991 -8.666 1.00 15.16 ? 78 TYR B N 1 ATOM 2180 C CA . TYR B 2 80 ? 51.239 14.801 -8.043 1.00 17.51 ? 78 TYR B CA 1 ATOM 2181 C C . TYR B 2 80 ? 49.849 14.199 -8.257 1.00 16.46 ? 78 TYR B C 1 ATOM 2182 O O . TYR B 2 80 ? 49.177 13.819 -7.299 1.00 17.92 ? 78 TYR B O 1 ATOM 2183 C CB . TYR B 2 80 ? 51.322 16.233 -8.587 1.00 17.53 ? 78 TYR B CB 1 ATOM 2184 C CG . TYR B 2 80 ? 50.248 17.173 -8.106 1.00 10.88 ? 78 TYR B CG 1 ATOM 2185 C CD1 . TYR B 2 80 ? 50.131 17.507 -6.765 1.00 9.68 ? 78 TYR B CD1 1 ATOM 2186 C CD2 . TYR B 2 80 ? 49.363 17.749 -9.007 1.00 14.84 ? 78 TYR B CD2 1 ATOM 2187 C CE1 . TYR B 2 80 ? 49.140 18.377 -6.330 1.00 11.82 ? 78 TYR B CE1 1 ATOM 2188 C CE2 . TYR B 2 80 ? 48.379 18.616 -8.588 1.00 10.24 ? 78 TYR B CE2 1 ATOM 2189 C CZ . TYR B 2 80 ? 48.268 18.927 -7.253 1.00 13.78 ? 78 TYR B CZ 1 ATOM 2190 O OH . TYR B 2 80 ? 47.280 19.792 -6.861 1.00 13.35 ? 78 TYR B OH 1 ATOM 2191 N N . CYS B 2 81 ? 49.423 14.116 -9.514 1.00 11.12 ? 79 CYS B N 1 ATOM 2192 C CA . CYS B 2 81 ? 48.095 13.612 -9.845 1.00 11.97 ? 79 CYS B CA 1 ATOM 2193 C C . CYS B 2 81 ? 47.876 12.146 -9.480 1.00 10.68 ? 79 CYS B C 1 ATOM 2194 O O . CYS B 2 81 ? 46.978 11.834 -8.695 1.00 13.65 ? 79 CYS B O 1 ATOM 2195 C CB . CYS B 2 81 ? 47.809 13.808 -11.334 1.00 9.88 ? 79 CYS B CB 1 ATOM 2196 S SG . CYS B 2 81 ? 47.847 15.526 -11.878 1.00 13.43 ? 79 CYS B SG 1 ATOM 2197 N N . ARG B 2 82 ? 48.683 11.250 -10.043 1.00 18.83 ? 80 ARG B N 1 ATOM 2198 C CA . ARG B 2 82 ? 48.521 9.826 -9.761 1.00 15.36 ? 80 ARG B CA 1 ATOM 2199 C C . ARG B 2 82 ? 48.744 9.538 -8.284 1.00 21.76 ? 80 ARG B C 1 ATOM 2200 O O . ARG B 2 82 ? 48.055 8.697 -7.703 1.00 24.18 ? 80 ARG B O 1 ATOM 2201 C CB . ARG B 2 82 ? 49.451 8.972 -10.631 1.00 20.35 ? 80 ARG B CB 1 ATOM 2202 C CG . ARG B 2 82 ? 48.952 8.825 -12.064 1.00 17.85 ? 80 ARG B CG 1 ATOM 2203 C CD . ARG B 2 82 ? 49.861 7.956 -12.917 1.00 20.66 ? 80 ARG B CD 1 ATOM 2204 N NE . ARG B 2 82 ? 49.242 7.680 -14.210 1.00 20.27 ? 80 ARG B NE 1 ATOM 2205 C CZ . ARG B 2 82 ? 49.456 8.390 -15.310 1.00 25.08 ? 80 ARG B CZ 1 ATOM 2206 N NH1 . ARG B 2 82 ? 48.840 8.069 -16.439 1.00 23.20 ? 80 ARG B NH1 1 ATOM 2207 N NH2 . ARG B 2 82 ? 50.288 9.422 -15.279 1.00 27.08 ? 80 ARG B NH2 1 ATOM 2208 N N . HIS B 2 83 ? 49.699 10.234 -7.677 1.00 16.40 ? 81 HIS B N 1 ATOM 2209 C CA . HIS B 2 83 ? 49.963 10.061 -6.257 1.00 18.56 ? 81 HIS B CA 1 ATOM 2210 C C . HIS B 2 83 ? 48.742 10.410 -5.403 1.00 16.92 ? 81 HIS B C 1 ATOM 2211 O O . HIS B 2 83 ? 48.304 9.606 -4.583 1.00 20.15 ? 81 HIS B O 1 ATOM 2212 C CB . HIS B 2 83 ? 51.151 10.915 -5.816 1.00 22.32 ? 81 HIS B CB 1 ATOM 2213 C CG . HIS B 2 83 ? 51.404 10.867 -4.342 1.00 25.49 ? 81 HIS B CG 1 ATOM 2214 N ND1 . HIS B 2 83 ? 52.195 9.904 -3.754 1.00 26.48 ? 81 HIS B ND1 1 ATOM 2215 C CD2 . HIS B 2 83 ? 50.957 11.655 -3.335 1.00 22.86 ? 81 HIS B CD2 1 ATOM 2216 C CE1 . HIS B 2 83 ? 52.229 10.105 -2.448 1.00 26.07 ? 81 HIS B CE1 1 ATOM 2217 N NE2 . HIS B 2 83 ? 51.486 11.160 -2.168 1.00 25.11 ? 81 HIS B NE2 1 ATOM 2218 N N . ASN B 2 84 ? 48.194 11.605 -5.602 1.00 13.23 ? 82 ASN B N 1 ATOM 2219 C CA . ASN B 2 84 ? 47.068 12.072 -4.797 1.00 11.45 ? 82 ASN B CA 1 ATOM 2220 C C . ASN B 2 84 ? 45.812 11.246 -5.045 1.00 17.98 ? 82 ASN B C 1 ATOM 2221 O O . ASN B 2 84 ? 44.994 11.066 -4.143 1.00 19.07 ? 82 ASN B O 1 ATOM 2222 C CB . ASN B 2 84 ? 46.802 13.560 -5.036 1.00 11.14 ? 82 ASN B CB 1 ATOM 2223 C CG . ASN B 2 84 ? 47.835 14.449 -4.350 1.00 20.65 ? 82 ASN B CG 1 ATOM 2224 O OD1 . ASN B 2 84 ? 48.548 14.007 -3.445 1.00 21.97 ? 82 ASN B OD1 1 ATOM 2225 N ND2 . ASN B 2 84 ? 47.903 15.710 -4.762 1.00 17.61 ? 82 ASN B ND2 1 ATOM 2226 N N . TYR B 2 85 ? 45.655 10.758 -6.271 1.00 17.76 ? 83 TYR B N 1 ATOM 2227 C CA . TYR B 2 85 ? 44.536 9.880 -6.593 1.00 17.72 ? 83 TYR B CA 1 ATOM 2228 C C . TYR B 2 85 ? 44.604 8.644 -5.704 1.00 21.07 ? 83 TYR B C 1 ATOM 2229 O O . TYR B 2 85 ? 43.602 8.231 -5.123 1.00 23.61 ? 83 TYR B O 1 ATOM 2230 C CB . TYR B 2 85 ? 44.577 9.481 -8.074 1.00 13.54 ? 83 TYR B CB 1 ATOM 2231 C CG . TYR B 2 85 ? 43.372 8.708 -8.580 1.00 24.52 ? 83 TYR B CG 1 ATOM 2232 C CD1 . TYR B 2 85 ? 43.261 7.339 -8.354 1.00 23.13 ? 83 TYR B CD1 1 ATOM 2233 C CD2 . TYR B 2 85 ? 42.370 9.330 -9.317 1.00 19.68 ? 83 TYR B CD2 1 ATOM 2234 C CE1 . TYR B 2 85 ? 42.180 6.618 -8.820 1.00 21.08 ? 83 TYR B CE1 1 ATOM 2235 C CE2 . TYR B 2 85 ? 41.279 8.613 -9.790 1.00 19.21 ? 83 TYR B CE2 1 ATOM 2236 C CZ . TYR B 2 85 ? 41.193 7.258 -9.538 1.00 26.21 ? 83 TYR B CZ 1 ATOM 2237 O OH . TYR B 2 85 ? 40.117 6.536 -10.001 1.00 27.31 ? 83 TYR B OH 1 ATOM 2238 N N . GLY B 2 86 ? 45.803 8.079 -5.595 1.00 16.93 ? 84 GLY B N 1 ATOM 2239 C CA . GLY B 2 86 ? 46.059 6.904 -4.778 1.00 18.68 ? 84 GLY B CA 1 ATOM 2240 C C . GLY B 2 86 ? 45.774 7.118 -3.307 1.00 14.66 ? 84 GLY B C 1 ATOM 2241 O O . GLY B 2 86 ? 45.269 6.235 -2.623 1.00 23.76 ? 84 GLY B O 1 ATOM 2242 N N . VAL B 2 87 ? 46.078 8.322 -2.836 1.00 19.58 ? 85 VAL B N 1 ATOM 2243 C CA . VAL B 2 87 ? 45.929 8.705 -1.432 1.00 22.02 ? 85 VAL B CA 1 ATOM 2244 C C . VAL B 2 87 ? 44.466 8.776 -1.004 1.00 20.70 ? 85 VAL B C 1 ATOM 2245 O O . VAL B 2 87 ? 44.104 8.335 0.086 1.00 22.11 ? 85 VAL B O 1 ATOM 2246 C CB . VAL B 2 87 ? 46.602 10.074 -1.150 1.00 16.60 ? 85 VAL B CB 1 ATOM 2247 C CG1 . VAL B 2 87 ? 46.309 10.540 0.268 1.00 19.30 ? 85 VAL B CG1 1 ATOM 2248 C CG2 . VAL B 2 87 ? 48.104 9.991 -1.382 1.00 17.83 ? 85 VAL B CG2 1 ATOM 2249 N N . GLY B 2 88 ? 43.628 9.303 -1.888 1.00 28.70 ? 86 GLY B N 1 ATOM 2250 C CA . GLY B 2 88 ? 42.249 9.630 -1.580 1.00 29.05 ? 86 GLY B CA 1 ATOM 2251 C C . GLY B 2 88 ? 41.222 8.675 -2.157 1.00 25.07 ? 86 GLY B C 1 ATOM 2252 O O . GLY B 2 88 ? 40.034 8.788 -1.860 1.00 30.27 ? 86 GLY B O 1 ATOM 2253 N N . GLU B 2 89 ? 41.683 7.726 -2.964 1.00 23.75 ? 87 GLU B N 1 ATOM 2254 C CA . GLU B 2 89 ? 40.806 6.845 -3.728 1.00 25.88 ? 87 GLU B CA 1 ATOM 2255 C C . GLU B 2 89 ? 39.775 6.099 -2.878 1.00 29.63 ? 87 GLU B C 1 ATOM 2256 O O . GLU B 2 89 ? 38.616 5.991 -3.278 1.00 25.60 ? 87 GLU B O 1 ATOM 2257 C CB . GLU B 2 89 ? 41.664 5.828 -4.493 1.00 32.47 ? 87 GLU B CB 1 ATOM 2258 C CG . GLU B 2 89 ? 40.931 4.604 -5.010 1.00 41.27 ? 87 GLU B CG 1 ATOM 2259 C CD . GLU B 2 89 ? 41.827 3.705 -5.843 1.00 56.46 ? 87 GLU B CD 1 ATOM 2260 O OE1 . GLU B 2 89 ? 42.946 4.141 -6.194 1.00 61.29 ? 87 GLU B OE1 1 ATOM 2261 O OE2 . GLU B 2 89 ? 41.420 2.562 -6.137 1.00 63.26 ? 87 GLU B OE2 1 ATOM 2262 N N . SER B 2 90 ? 40.184 5.577 -1.726 1.00 25.90 ? 88 SER B N 1 ATOM 2263 C CA . SER B 2 90 ? 39.278 4.774 -0.913 1.00 22.07 ? 88 SER B CA 1 ATOM 2264 C C . SER B 2 90 ? 38.067 5.557 -0.382 1.00 23.86 ? 88 SER B C 1 ATOM 2265 O O . SER B 2 90 ? 37.008 4.971 -0.169 1.00 23.11 ? 88 SER B O 1 ATOM 2266 C CB . SER B 2 90 ? 40.028 4.138 0.261 1.00 28.65 ? 88 SER B CB 1 ATOM 2267 O OG . SER B 2 90 ? 40.296 5.079 1.284 1.00 36.07 ? 88 SER B OG 1 ATOM 2268 N N . PHE B 2 91 ? 38.198 6.871 -0.198 1.00 25.10 ? 89 PHE B N 1 ATOM 2269 C CA . PHE B 2 91 ? 37.080 7.657 0.339 1.00 28.78 ? 89 PHE B CA 1 ATOM 2270 C C . PHE B 2 91 ? 36.535 8.735 -0.603 1.00 27.93 ? 89 PHE B C 1 ATOM 2271 O O . PHE B 2 91 ? 35.706 9.549 -0.198 1.00 22.07 ? 89 PHE B O 1 ATOM 2272 C CB . PHE B 2 91 ? 37.455 8.308 1.680 1.00 26.03 ? 89 PHE B CB 1 ATOM 2273 C CG . PHE B 2 91 ? 38.681 9.181 1.633 1.00 28.77 ? 89 PHE B CG 1 ATOM 2274 C CD1 . PHE B 2 91 ? 38.578 10.526 1.304 1.00 22.57 ? 89 PHE B CD1 1 ATOM 2275 C CD2 . PHE B 2 91 ? 39.926 8.674 1.970 1.00 33.76 ? 89 PHE B CD2 1 ATOM 2276 C CE1 . PHE B 2 91 ? 39.697 11.341 1.281 1.00 21.59 ? 89 PHE B CE1 1 ATOM 2277 C CE2 . PHE B 2 91 ? 41.054 9.485 1.949 1.00 33.15 ? 89 PHE B CE2 1 ATOM 2278 C CZ . PHE B 2 91 ? 40.938 10.819 1.605 1.00 29.66 ? 89 PHE B CZ 1 ATOM 2279 N N . THR B 2 92 ? 36.996 8.749 -1.849 1.00 24.75 ? 90 THR B N 1 ATOM 2280 C CA . THR B 2 92 ? 36.489 9.706 -2.828 1.00 22.02 ? 90 THR B CA 1 ATOM 2281 C C . THR B 2 92 ? 35.960 8.942 -4.032 1.00 23.91 ? 90 THR B C 1 ATOM 2282 O O . THR B 2 92 ? 34.751 8.882 -4.260 1.00 20.26 ? 90 THR B O 1 ATOM 2283 C CB . THR B 2 92 ? 37.566 10.702 -3.296 1.00 18.97 ? 90 THR B CB 1 ATOM 2284 O OG1 . THR B 2 92 ? 38.677 9.986 -3.848 1.00 17.28 ? 90 THR B OG1 1 ATOM 2285 C CG2 . THR B 2 92 ? 38.041 11.568 -2.139 1.00 26.16 ? 90 THR B CG2 1 ATOM 2286 N N . VAL B 2 93 ? 36.878 8.378 -4.812 1.00 22.22 ? 91 VAL B N 1 ATOM 2287 C CA . VAL B 2 93 ? 36.524 7.572 -5.973 1.00 22.45 ? 91 VAL B CA 1 ATOM 2288 C C . VAL B 2 93 ? 35.560 6.437 -5.605 1.00 24.22 ? 91 VAL B C 1 ATOM 2289 O O . VAL B 2 93 ? 34.593 6.172 -6.318 1.00 23.13 ? 91 VAL B O 1 ATOM 2290 C CB . VAL B 2 93 ? 37.793 6.977 -6.624 1.00 21.18 ? 91 VAL B CB 1 ATOM 2291 C CG1 . VAL B 2 93 ? 37.427 5.986 -7.723 1.00 21.21 ? 91 VAL B CG1 1 ATOM 2292 C CG2 . VAL B 2 93 ? 38.683 8.094 -7.168 1.00 24.30 ? 91 VAL B CG2 1 ATOM 2293 N N . GLN B 2 94 ? 35.827 5.780 -4.480 1.00 27.08 ? 92 GLN B N 1 ATOM 2294 C CA . GLN B 2 94 ? 35.046 4.617 -4.054 1.00 27.62 ? 92 GLN B CA 1 ATOM 2295 C C . GLN B 2 94 ? 33.884 4.963 -3.121 1.00 22.73 ? 92 GLN B C 1 ATOM 2296 O O . GLN B 2 94 ? 33.188 4.074 -2.638 1.00 24.35 ? 92 GLN B O 1 ATOM 2297 C CB . GLN B 2 94 ? 35.963 3.579 -3.407 1.00 25.10 ? 92 GLN B CB 1 ATOM 2298 C CG . GLN B 2 94 ? 37.012 3.049 -4.378 1.00 32.17 ? 92 GLN B CG 1 ATOM 2299 C CD . GLN B 2 94 ? 37.996 2.090 -3.737 1.00 41.96 ? 92 GLN B CD 1 ATOM 2300 O OE1 . GLN B 2 94 ? 37.845 1.703 -2.578 1.00 43.82 ? 92 GLN B OE1 1 ATOM 2301 N NE2 . GLN B 2 94 ? 39.006 1.688 -4.500 1.00 51.09 ? 92 GLN B NE2 1 ATOM 2302 N N . ARG B 2 95 ? 33.692 6.250 -2.854 1.00 24.35 ? 93 ARG B N 1 ATOM 2303 C CA . ARG B 2 95 ? 32.616 6.683 -1.970 1.00 26.54 ? 93 ARG B CA 1 ATOM 2304 C C . ARG B 2 95 ? 31.247 6.391 -2.580 1.00 26.46 ? 93 ARG B C 1 ATOM 2305 O O . ARG B 2 95 ? 30.966 6.770 -3.716 1.00 23.69 ? 93 ARG B O 1 ATOM 2306 C CB . ARG B 2 95 ? 32.737 8.177 -1.659 1.00 20.92 ? 93 ARG B CB 1 ATOM 2307 C CG . ARG B 2 95 ? 31.624 8.719 -0.766 1.00 18.48 ? 93 ARG B CG 1 ATOM 2308 C CD . ARG B 2 95 ? 31.833 10.203 -0.466 1.00 22.88 ? 93 ARG B CD 1 ATOM 2309 N NE . ARG B 2 95 ? 30.672 10.804 0.187 1.00 18.09 ? 93 ARG B NE 1 ATOM 2310 C CZ . ARG B 2 95 ? 30.408 10.703 1.485 1.00 22.24 ? 93 ARG B CZ 1 ATOM 2311 N NH1 . ARG B 2 95 ? 31.228 10.029 2.280 1.00 19.44 ? 93 ARG B NH1 1 ATOM 2312 N NH2 . ARG B 2 95 ? 29.328 11.285 1.989 1.00 15.48 ? 93 ARG B NH2 1 ATOM 2313 N N . ARG B 2 96 ? 30.403 5.703 -1.819 1.00 25.13 ? 94 ARG B N 1 ATOM 2314 C CA . ARG B 2 96 ? 29.047 5.386 -2.257 1.00 28.81 ? 94 ARG B CA 1 ATOM 2315 C C . ARG B 2 96 ? 28.011 5.525 -1.160 1.00 26.56 ? 94 ARG B C 1 ATOM 2316 O O . ARG B 2 96 ? 28.093 4.828 -0.152 1.00 19.26 ? 94 ARG B O 1 ATOM 2317 C CB . ARG B 2 96 ? 28.971 3.948 -2.775 1.00 25.58 ? 94 ARG B CB 1 ATOM 2318 C CG . ARG B 2 96 ? 29.840 3.591 -3.960 1.00 30.16 ? 94 ARG B CG 1 ATOM 2319 C CD . ARG B 2 96 ? 29.204 4.110 -5.229 1.00 29.46 ? 94 ARG B CD 1 ATOM 2320 N NE . ARG B 2 96 ? 29.890 3.645 -6.428 1.00 39.21 ? 94 ARG B NE 1 ATOM 2321 C CZ . ARG B 2 96 ? 30.985 4.206 -6.926 1.00 51.28 ? 94 ARG B CZ 1 ATOM 2322 N NH1 . ARG B 2 96 ? 31.518 5.262 -6.331 1.00 54.56 ? 94 ARG B NH1 1 ATOM 2323 N NH2 . ARG B 2 96 ? 31.539 3.715 -8.027 1.00 58.75 ? 94 ARG B NH2 1 ATOM 2324 N N . VAL B 2 97 ? 27.037 6.416 -1.324 1.00 15.56 ? 95 VAL B N 1 ATOM 2325 C CA . VAL B 2 97 ? 26.011 6.464 -0.304 1.00 18.38 ? 95 VAL B CA 1 ATOM 2326 C C . VAL B 2 97 ? 24.649 6.381 -0.968 1.00 16.44 ? 95 VAL B C 1 ATOM 2327 O O . VAL B 2 97 ? 24.328 7.212 -1.822 1.00 15.00 ? 95 VAL B O 1 ATOM 2328 C CB . VAL B 2 97 ? 26.099 7.792 0.487 1.00 18.10 ? 95 VAL B CB 1 ATOM 2329 C CG1 . VAL B 2 97 ? 25.096 7.826 1.619 1.00 19.27 ? 95 VAL B CG1 1 ATOM 2330 C CG2 . VAL B 2 97 ? 27.518 8.031 1.005 1.00 22.54 ? 95 VAL B CG2 1 ATOM 2331 N N . TYR B 2 98 ? 23.853 5.378 -0.603 1.00 18.30 ? 96 TYR B N 1 ATOM 2332 C CA . TYR B 2 98 ? 22.507 5.235 -1.152 1.00 20.21 ? 96 TYR B CA 1 ATOM 2333 C C . TYR B 2 98 ? 21.667 6.452 -0.782 1.00 19.92 ? 96 TYR B C 1 ATOM 2334 O O . TYR B 2 98 ? 21.893 7.077 0.240 1.00 21.54 ? 96 TYR B O 1 ATOM 2335 C CB . TYR B 2 98 ? 21.858 3.870 -0.848 1.00 26.85 ? 96 TYR B CB 1 ATOM 2336 C CG . TYR B 2 98 ? 21.597 3.413 0.549 1.00 31.76 ? 96 TYR B CG 1 ATOM 2337 C CD1 . TYR B 2 98 ? 20.367 3.646 1.140 1.00 41.28 ? 96 TYR B CD1 1 ATOM 2338 C CD2 . TYR B 2 98 ? 22.519 2.626 1.226 1.00 25.38 ? 96 TYR B CD2 1 ATOM 2339 C CE1 . TYR B 2 98 ? 20.086 3.174 2.396 1.00 45.20 ? 96 TYR B CE1 1 ATOM 2340 C CE2 . TYR B 2 98 ? 22.247 2.146 2.488 1.00 34.11 ? 96 TYR B CE2 1 ATOM 2341 C CZ . TYR B 2 98 ? 21.024 2.426 3.067 1.00 40.70 ? 96 TYR B CZ 1 ATOM 2342 O OH . TYR B 2 98 ? 20.724 1.962 4.320 1.00 35.16 ? 96 TYR B OH 1 ATOM 2343 N N . PRO B 2 99 ? 20.677 6.773 -1.614 1.00 20.65 ? 97 PRO B N 1 ATOM 2344 C CA . PRO B 2 99 ? 19.630 7.746 -1.271 1.00 17.11 ? 97 PRO B CA 1 ATOM 2345 C C . PRO B 2 99 ? 18.482 7.230 -0.417 1.00 15.86 ? 97 PRO B C 1 ATOM 2346 O O . PRO B 2 99 ? 18.100 6.065 -0.495 1.00 22.09 ? 97 PRO B O 1 ATOM 2347 C CB . PRO B 2 99 ? 19.081 8.144 -2.640 1.00 14.81 ? 97 PRO B CB 1 ATOM 2348 C CG . PRO B 2 99 ? 19.326 6.942 -3.493 1.00 22.49 ? 97 PRO B CG 1 ATOM 2349 C CD . PRO B 2 99 ? 20.627 6.384 -3.034 1.00 20.92 ? 97 PRO B CD 1 ATOM 2350 N N . GLU B 2 100 ? 17.981 8.119 0.438 1.00 21.75 ? 98 GLU B N 1 ATOM 2351 C CA . GLU B 2 100 ? 16.701 7.904 1.096 1.00 26.40 ? 98 GLU B CA 1 ATOM 2352 C C . GLU B 2 100 ? 15.662 8.519 0.171 1.00 25.70 ? 98 GLU B C 1 ATOM 2353 O O . GLU B 2 100 ? 15.836 9.626 -0.346 1.00 21.96 ? 98 GLU B O 1 ATOM 2354 C CB . GLU B 2 100 ? 16.643 8.535 2.497 1.00 38.64 ? 98 GLU B CB 1 ATOM 2355 C CG . GLU B 2 100 ? 16.779 10.058 2.528 1.00 60.41 ? 98 GLU B CG 1 ATOM 2356 C CD . GLU B 2 100 ? 15.982 10.723 3.648 1.00 68.36 ? 98 GLU B CD 1 ATOM 2357 O OE1 . GLU B 2 100 ? 14.929 10.180 4.045 1.00 71.49 ? 98 GLU B OE1 1 ATOM 2358 O OE2 . GLU B 2 100 ? 16.411 11.793 4.132 1.00 61.88 ? 98 GLU B OE2 1 ATOM 2359 N N . VAL B 2 101 ? 14.593 7.773 -0.068 1.00 19.35 ? 99 VAL B N 1 ATOM 2360 C CA . VAL B 2 101 ? 13.549 8.200 -0.984 1.00 20.74 ? 99 VAL B CA 1 ATOM 2361 C C . VAL B 2 101 ? 12.201 8.330 -0.297 1.00 23.62 ? 99 VAL B C 1 ATOM 2362 O O . VAL B 2 101 ? 11.712 7.392 0.332 1.00 21.62 ? 99 VAL B O 1 ATOM 2363 C CB . VAL B 2 101 ? 13.438 7.243 -2.180 1.00 16.74 ? 99 VAL B CB 1 ATOM 2364 C CG1 . VAL B 2 101 ? 12.411 7.750 -3.177 1.00 19.15 ? 99 VAL B CG1 1 ATOM 2365 C CG2 . VAL B 2 101 ? 14.800 7.078 -2.838 1.00 15.95 ? 99 VAL B CG2 1 ATOM 2366 N N . THR B 2 102 ? 11.624 9.520 -0.429 1.00 20.13 ? 100 THR B N 1 ATOM 2367 C CA . THR B 2 102 ? 10.333 9.854 0.149 1.00 27.34 ? 100 THR B CA 1 ATOM 2368 C C . THR B 2 102 ? 9.375 10.372 -0.914 1.00 27.40 ? 100 THR B C 1 ATOM 2369 O O . THR B 2 102 ? 9.761 11.163 -1.771 1.00 26.19 ? 100 THR B O 1 ATOM 2370 C CB . THR B 2 102 ? 10.485 10.943 1.232 1.00 18.04 ? 100 THR B CB 1 ATOM 2371 O OG1 . THR B 2 102 ? 11.378 10.486 2.253 1.00 46.66 ? 100 THR B OG1 1 ATOM 2372 C CG2 . THR B 2 102 ? 9.140 11.302 1.850 1.00 19.37 ? 100 THR B CG2 1 ATOM 2373 N N . VAL B 2 103 ? 8.131 9.906 -0.875 1.00 25.45 ? 101 VAL B N 1 ATOM 2374 C CA . VAL B 2 103 ? 7.109 10.455 -1.749 1.00 22.63 ? 101 VAL B CA 1 ATOM 2375 C C . VAL B 2 103 ? 6.030 11.128 -0.909 1.00 29.09 ? 101 VAL B C 1 ATOM 2376 O O . VAL B 2 103 ? 5.495 10.533 0.028 1.00 26.68 ? 101 VAL B O 1 ATOM 2377 C CB . VAL B 2 103 ? 6.479 9.377 -2.640 1.00 24.88 ? 101 VAL B CB 1 ATOM 2378 C CG1 . VAL B 2 103 ? 5.294 9.955 -3.404 1.00 27.14 ? 101 VAL B CG1 1 ATOM 2379 C CG2 . VAL B 2 103 ? 7.515 8.832 -3.612 1.00 20.87 ? 101 VAL B CG2 1 ATOM 2380 N N . TYR B 2 104 ? 5.714 12.371 -1.249 1.00 28.10 ? 102 TYR B N 1 ATOM 2381 C CA . TYR B 2 104 ? 4.637 13.099 -0.597 1.00 27.14 ? 102 TYR B CA 1 ATOM 2382 C C . TYR B 2 104 ? 3.873 13.967 -1.591 1.00 27.84 ? 102 TYR B C 1 ATOM 2383 O O . TYR B 2 104 ? 4.444 14.433 -2.579 1.00 23.13 ? 102 TYR B O 1 ATOM 2384 C CB . TYR B 2 104 ? 5.175 13.934 0.572 1.00 27.15 ? 102 TYR B CB 1 ATOM 2385 C CG . TYR B 2 104 ? 6.192 14.999 0.222 1.00 29.42 ? 102 TYR B CG 1 ATOM 2386 C CD1 . TYR B 2 104 ? 5.798 16.284 -0.135 1.00 32.51 ? 102 TYR B CD1 1 ATOM 2387 C CD2 . TYR B 2 104 ? 7.554 14.732 0.299 1.00 28.22 ? 102 TYR B CD2 1 ATOM 2388 C CE1 . TYR B 2 104 ? 6.734 17.264 -0.434 1.00 34.96 ? 102 TYR B CE1 1 ATOM 2389 C CE2 . TYR B 2 104 ? 8.496 15.705 0.003 1.00 27.65 ? 102 TYR B CE2 1 ATOM 2390 C CZ . TYR B 2 104 ? 8.080 16.968 -0.362 1.00 32.10 ? 102 TYR B CZ 1 ATOM 2391 O OH . TYR B 2 104 ? 9.013 17.938 -0.659 1.00 34.60 ? 102 TYR B OH 1 ATOM 2392 N N . PRO B 2 105 ? 2.573 14.180 -1.336 1.00 25.09 ? 103 PRO B N 1 ATOM 2393 C CA . PRO B 2 105 ? 1.782 15.002 -2.251 1.00 22.32 ? 103 PRO B CA 1 ATOM 2394 C C . PRO B 2 105 ? 1.987 16.482 -1.965 1.00 28.63 ? 103 PRO B C 1 ATOM 2395 O O . PRO B 2 105 ? 2.312 16.867 -0.842 1.00 33.61 ? 103 PRO B O 1 ATOM 2396 C CB . PRO B 2 105 ? 0.346 14.569 -1.953 1.00 24.81 ? 103 PRO B CB 1 ATOM 2397 C CG . PRO B 2 105 ? 0.381 14.171 -0.512 1.00 25.76 ? 103 PRO B CG 1 ATOM 2398 C CD . PRO B 2 105 ? 1.740 13.548 -0.296 1.00 23.97 ? 103 PRO B CD 1 ATOM 2399 N N . ALA B 2 106 ? 1.803 17.296 -2.997 1.00 23.21 ? 104 ALA B N 1 ATOM 2400 C CA . ALA B 2 106 ? 1.923 18.745 -2.901 1.00 23.61 ? 104 ALA B CA 1 ATOM 2401 C C . ALA B 2 106 ? 0.909 19.415 -3.817 1.00 32.11 ? 104 ALA B C 1 ATOM 2402 O O . ALA B 2 106 ? 0.084 18.743 -4.435 1.00 28.09 ? 104 ALA B O 1 ATOM 2403 C CB . ALA B 2 106 ? 3.335 19.190 -3.244 1.00 21.05 ? 104 ALA B CB 1 ATOM 2404 N N . LYS B 2 107 ? 0.966 20.741 -3.892 1.00 38.58 ? 105 LYS B N 1 ATOM 2405 C CA . LYS B 2 107 ? 0.028 21.507 -4.703 1.00 38.23 ? 105 LYS B CA 1 ATOM 2406 C C . LYS B 2 107 ? 0.814 22.412 -5.640 1.00 37.66 ? 105 LYS B C 1 ATOM 2407 O O . LYS B 2 107 ? 1.803 23.021 -5.234 1.00 38.18 ? 105 LYS B O 1 ATOM 2408 C CB . LYS B 2 107 ? -0.885 22.333 -3.802 1.00 35.63 ? 105 LYS B CB 1 ATOM 2409 C CG . LYS B 2 107 ? -1.733 21.488 -2.875 1.00 40.11 ? 105 LYS B CG 1 ATOM 2410 C CD . LYS B 2 107 ? -2.577 22.347 -1.955 1.00 47.81 ? 105 LYS B CD 1 ATOM 2411 C CE . LYS B 2 107 ? -3.495 21.489 -1.097 1.00 52.56 ? 105 LYS B CE 1 ATOM 2412 N NZ . LYS B 2 107 ? -4.384 22.317 -0.236 1.00 56.29 ? 105 LYS B NZ 1 ATOM 2413 N N . THR B 2 108 ? 0.375 22.523 -6.890 1.00 39.65 ? 106 THR B N 1 ATOM 2414 C CA . THR B 2 108 ? 1.041 23.452 -7.791 1.00 42.96 ? 106 THR B CA 1 ATOM 2415 C C . THR B 2 108 ? 0.636 24.884 -7.484 1.00 45.48 ? 106 THR B C 1 ATOM 2416 O O . THR B 2 108 ? 1.452 25.799 -7.588 1.00 42.68 ? 106 THR B O 1 ATOM 2417 C CB . THR B 2 108 ? 0.710 23.131 -9.261 1.00 40.15 ? 106 THR B CB 1 ATOM 2418 O OG1 . THR B 2 108 ? -0.713 23.132 -9.439 1.00 37.23 ? 106 THR B OG1 1 ATOM 2419 C CG2 . THR B 2 108 ? 1.252 21.762 -9.645 1.00 38.75 ? 106 THR B CG2 1 ATOM 2420 N N . GLN B 2 109 ? -0.621 25.084 -7.111 1.00 49.48 ? 107 GLN B N 1 ATOM 2421 C CA . GLN B 2 109 ? -1.063 26.402 -6.687 1.00 62.01 ? 107 GLN B CA 1 ATOM 2422 C C . GLN B 2 109 ? -1.908 26.270 -5.437 1.00 69.58 ? 107 GLN B C 1 ATOM 2423 O O . GLN B 2 109 ? -2.656 25.300 -5.308 1.00 69.89 ? 107 GLN B O 1 ATOM 2424 C CB . GLN B 2 109 ? -1.868 27.110 -7.779 1.00 65.95 ? 107 GLN B CB 1 ATOM 2425 C CG . GLN B 2 109 ? -1.078 27.510 -9.007 1.00 71.59 ? 107 GLN B CG 1 ATOM 2426 C CD . GLN B 2 109 ? -1.914 28.308 -9.988 1.00 78.88 ? 107 GLN B CD 1 ATOM 2427 O OE1 . GLN B 2 109 ? -2.131 27.890 -11.126 1.00 78.11 ? 107 GLN B OE1 1 ATOM 2428 N NE2 . GLN B 2 109 ? -2.386 29.471 -9.550 1.00 82.68 ? 107 GLN B NE2 1 ATOM 2429 N N . PRO B 2 110 ? -1.764 27.213 -4.492 1.00 75.78 ? 108 PRO B N 1 ATOM 2430 C CA . PRO B 2 110 ? -2.476 27.128 -3.212 1.00 79.11 ? 108 PRO B CA 1 ATOM 2431 C C . PRO B 2 110 ? -3.991 26.963 -3.430 1.00 83.91 ? 108 PRO B C 1 ATOM 2432 O O . PRO B 2 110 ? -4.466 27.189 -4.547 1.00 84.89 ? 108 PRO B O 1 ATOM 2433 C CB . PRO B 2 110 ? -2.133 28.456 -2.523 1.00 80.06 ? 108 PRO B CB 1 ATOM 2434 C CG . PRO B 2 110 ? -1.588 29.341 -3.610 1.00 78.60 ? 108 PRO B CG 1 ATOM 2435 C CD . PRO B 2 110 ? -0.909 28.409 -4.560 1.00 73.68 ? 108 PRO B CD 1 ATOM 2436 N N . LEU B 2 111 ? -4.725 26.594 -2.383 1.00 84.71 ? 109 LEU B N 1 ATOM 2437 C CA . LEU B 2 111 ? -6.166 26.301 -2.448 1.00 81.89 ? 109 LEU B CA 1 ATOM 2438 C C . LEU B 2 111 ? -6.584 25.075 -3.275 1.00 76.47 ? 109 LEU B C 1 ATOM 2439 O O . LEU B 2 111 ? -7.607 24.461 -2.971 1.00 80.29 ? 109 LEU B O 1 ATOM 2440 C CB . LEU B 2 111 ? -6.929 27.529 -2.962 1.00 82.68 ? 109 LEU B CB 1 ATOM 2441 N N . GLN B 2 112 ? -5.827 24.708 -4.306 1.00 66.13 ? 110 GLN B N 1 ATOM 2442 C CA . GLN B 2 112 ? -6.269 23.624 -5.186 1.00 70.57 ? 110 GLN B CA 1 ATOM 2443 C C . GLN B 2 112 ? -6.020 22.298 -4.490 1.00 71.80 ? 110 GLN B C 1 ATOM 2444 O O . GLN B 2 112 ? -5.226 22.228 -3.558 1.00 77.68 ? 110 GLN B O 1 ATOM 2445 C CB . GLN B 2 112 ? -5.576 23.634 -6.552 1.00 75.78 ? 110 GLN B CB 1 ATOM 2446 C CG . GLN B 2 112 ? -6.191 24.580 -7.567 1.00 84.06 ? 110 GLN B CG 1 ATOM 2447 C CD . GLN B 2 112 ? -5.187 25.092 -8.577 1.00 87.62 ? 110 GLN B CD 1 ATOM 2448 O OE1 . GLN B 2 112 ? -4.240 24.392 -8.935 1.00 84.80 ? 110 GLN B OE1 1 ATOM 2449 N NE2 . GLN B 2 112 ? -5.399 26.311 -9.057 1.00 90.92 ? 110 GLN B NE2 1 ATOM 2450 N N . HIS B 2 113 ? -6.707 21.247 -4.928 1.00 62.06 ? 111 HIS B N 1 ATOM 2451 C CA . HIS B 2 113 ? -6.447 19.925 -4.381 1.00 46.56 ? 111 HIS B CA 1 ATOM 2452 C C . HIS B 2 113 ? -5.039 19.474 -4.759 1.00 38.55 ? 111 HIS B C 1 ATOM 2453 O O . HIS B 2 113 ? -4.397 20.080 -5.618 1.00 36.55 ? 111 HIS B O 1 ATOM 2454 C CB . HIS B 2 113 ? -7.477 18.926 -4.914 1.00 46.92 ? 111 HIS B CB 1 ATOM 2455 C CG . HIS B 2 113 ? -8.869 19.166 -4.418 1.00 52.61 ? 111 HIS B CG 1 ATOM 2456 N ND1 . HIS B 2 113 ? -9.553 20.338 -4.664 1.00 48.78 ? 111 HIS B ND1 1 ATOM 2457 C CD2 . HIS B 2 113 ? -9.712 18.382 -3.704 1.00 56.14 ? 111 HIS B CD2 1 ATOM 2458 C CE1 . HIS B 2 113 ? -10.753 20.268 -4.115 1.00 49.62 ? 111 HIS B CE1 1 ATOM 2459 N NE2 . HIS B 2 113 ? -10.874 19.092 -3.526 1.00 52.92 ? 111 HIS B NE2 1 ATOM 2460 N N . HIS B 2 114 ? -4.561 18.417 -4.108 1.00 39.69 ? 112 HIS B N 1 ATOM 2461 C CA . HIS B 2 114 ? -3.254 17.837 -4.413 1.00 37.28 ? 112 HIS B CA 1 ATOM 2462 C C . HIS B 2 114 ? -3.112 17.418 -5.875 1.00 35.22 ? 112 HIS B C 1 ATOM 2463 O O . HIS B 2 114 ? -3.865 16.575 -6.354 1.00 42.74 ? 112 HIS B O 1 ATOM 2464 C CB . HIS B 2 114 ? -2.979 16.645 -3.494 1.00 46.38 ? 112 HIS B CB 1 ATOM 2465 C CG . HIS B 2 114 ? -2.532 17.039 -2.121 1.00 57.75 ? 112 HIS B CG 1 ATOM 2466 N ND1 . HIS B 2 114 ? -2.876 16.327 -0.992 1.00 62.37 ? 112 HIS B ND1 1 ATOM 2467 C CD2 . HIS B 2 114 ? -1.769 18.074 -1.695 1.00 63.33 ? 112 HIS B CD2 1 ATOM 2468 C CE1 . HIS B 2 114 ? -2.345 16.907 0.070 1.00 66.57 ? 112 HIS B CE1 1 ATOM 2469 N NE2 . HIS B 2 114 ? -1.668 17.969 -0.329 1.00 66.04 ? 112 HIS B NE2 1 ATOM 2470 N N . ASN B 2 115 ? -2.152 18.007 -6.581 1.00 32.40 ? 113 ASN B N 1 ATOM 2471 C CA . ASN B 2 115 ? -1.990 17.735 -8.006 1.00 27.30 ? 113 ASN B CA 1 ATOM 2472 C C . ASN B 2 115 ? -0.510 17.636 -8.337 1.00 24.88 ? 113 ASN B C 1 ATOM 2473 O O . ASN B 2 115 ? -0.096 17.757 -9.493 1.00 21.41 ? 113 ASN B O 1 ATOM 2474 C CB . ASN B 2 115 ? -2.655 18.806 -8.872 1.00 32.09 ? 113 ASN B CB 1 ATOM 2475 C CG . ASN B 2 115 ? -2.003 20.169 -8.737 1.00 35.14 ? 113 ASN B CG 1 ATOM 2476 O OD1 . ASN B 2 115 ? -1.194 20.408 -7.840 1.00 29.05 ? 113 ASN B OD1 1 ATOM 2477 N ND2 . ASN B 2 115 ? -2.332 21.066 -9.661 1.00 40.05 ? 113 ASN B ND2 1 ATOM 2478 N N . LEU B 2 116 ? 0.285 17.414 -7.301 1.00 27.90 ? 114 LEU B N 1 ATOM 2479 C CA . LEU B 2 116 ? 1.717 17.274 -7.459 1.00 29.27 ? 114 LEU B CA 1 ATOM 2480 C C . LEU B 2 116 ? 2.242 16.161 -6.563 1.00 32.11 ? 114 LEU B C 1 ATOM 2481 O O . LEU B 2 116 ? 1.987 16.155 -5.361 1.00 39.79 ? 114 LEU B O 1 ATOM 2482 C CB . LEU B 2 116 ? 2.390 18.610 -7.129 1.00 31.52 ? 114 LEU B CB 1 ATOM 2483 C CG . LEU B 2 116 ? 3.792 18.928 -7.635 1.00 33.56 ? 114 LEU B CG 1 ATOM 2484 C CD1 . LEU B 2 116 ? 3.813 18.944 -9.153 1.00 31.07 ? 114 LEU B CD1 1 ATOM 2485 C CD2 . LEU B 2 116 ? 4.229 20.275 -7.085 1.00 34.29 ? 114 LEU B CD2 1 ATOM 2486 N N . LEU B 2 117 ? 2.974 15.217 -7.145 1.00 26.64 ? 115 LEU B N 1 ATOM 2487 C CA . LEU B 2 117 ? 3.617 14.178 -6.351 1.00 24.83 ? 115 LEU B CA 1 ATOM 2488 C C . LEU B 2 117 ? 5.106 14.442 -6.331 1.00 20.60 ? 115 LEU B C 1 ATOM 2489 O O . LEU B 2 117 ? 5.754 14.497 -7.373 1.00 17.52 ? 115 LEU B O 1 ATOM 2490 C CB . LEU B 2 117 ? 3.327 12.781 -6.908 1.00 20.80 ? 115 LEU B CB 1 ATOM 2491 C CG . LEU B 2 117 ? 1.873 12.313 -6.868 1.00 25.58 ? 115 LEU B CG 1 ATOM 2492 C CD1 . LEU B 2 117 ? 1.771 10.882 -7.355 1.00 23.91 ? 115 LEU B CD1 1 ATOM 2493 C CD2 . LEU B 2 117 ? 1.299 12.443 -5.464 1.00 26.72 ? 115 LEU B CD2 1 ATOM 2494 N N . VAL B 2 118 ? 5.649 14.577 -5.130 1.00 21.38 ? 116 VAL B N 1 ATOM 2495 C CA . VAL B 2 118 ? 7.060 14.864 -4.983 1.00 17.30 ? 116 VAL B CA 1 ATOM 2496 C C . VAL B 2 118 ? 7.829 13.613 -4.627 1.00 17.38 ? 116 VAL B C 1 ATOM 2497 O O . VAL B 2 118 ? 7.529 12.945 -3.641 1.00 19.61 ? 116 VAL B O 1 ATOM 2498 C CB . VAL B 2 118 ? 7.312 15.922 -3.892 1.00 22.17 ? 116 VAL B CB 1 ATOM 2499 C CG1 . VAL B 2 118 ? 8.803 16.251 -3.808 1.00 18.74 ? 116 VAL B CG1 1 ATOM 2500 C CG2 . VAL B 2 118 ? 6.493 17.177 -4.166 1.00 19.06 ? 116 VAL B CG2 1 ATOM 2501 N N . CYS B 2 119 ? 8.828 13.298 -5.439 1.00 17.97 ? 117 CYS B N 1 ATOM 2502 C CA . CYS B 2 119 ? 9.759 12.250 -5.076 1.00 20.71 ? 117 CYS B CA 1 ATOM 2503 C C . CYS B 2 119 ? 11.016 12.929 -4.568 1.00 20.50 ? 117 CYS B C 1 ATOM 2504 O O . CYS B 2 119 ? 11.789 13.488 -5.344 1.00 16.86 ? 117 CYS B O 1 ATOM 2505 C CB . CYS B 2 119 ? 10.075 11.327 -6.247 1.00 15.77 ? 117 CYS B CB 1 ATOM 2506 S SG . CYS B 2 119 ? 11.105 9.937 -5.739 1.00 22.59 ? 117 CYS B SG 1 ATOM 2507 N N . SER B 2 120 ? 11.214 12.877 -3.255 1.00 15.86 ? 118 SER B N 1 ATOM 2508 C CA . SER B 2 120 ? 12.366 13.522 -2.651 1.00 19.98 ? 118 SER B CA 1 ATOM 2509 C C . SER B 2 120 ? 13.476 12.498 -2.468 1.00 21.22 ? 118 SER B C 1 ATOM 2510 O O . SER B 2 120 ? 13.317 11.511 -1.753 1.00 26.07 ? 118 SER B O 1 ATOM 2511 C CB . SER B 2 120 ? 11.988 14.155 -1.315 1.00 20.23 ? 118 SER B CB 1 ATOM 2512 O OG . SER B 2 120 ? 13.073 14.904 -0.797 1.00 24.56 ? 118 SER B OG 1 ATOM 2513 N N . VAL B 2 121 ? 14.596 12.738 -3.136 1.00 15.37 ? 119 VAL B N 1 ATOM 2514 C CA . VAL B 2 121 ? 15.726 11.818 -3.111 1.00 14.60 ? 119 VAL B CA 1 ATOM 2515 C C . VAL B 2 121 ? 16.908 12.482 -2.418 1.00 17.75 ? 119 VAL B C 1 ATOM 2516 O O . VAL B 2 121 ? 17.452 13.461 -2.923 1.00 14.96 ? 119 VAL B O 1 ATOM 2517 C CB . VAL B 2 121 ? 16.103 11.371 -4.538 1.00 14.28 ? 119 VAL B CB 1 ATOM 2518 C CG1 . VAL B 2 121 ? 17.162 10.292 -4.506 1.00 14.24 ? 119 VAL B CG1 1 ATOM 2519 C CG2 . VAL B 2 121 ? 14.865 10.866 -5.274 1.00 14.52 ? 119 VAL B CG2 1 ATOM 2520 N N . ASN B 2 122 ? 17.286 11.967 -1.249 1.00 16.13 ? 120 ASN B N 1 ATOM 2521 C CA . ASN B 2 122 ? 18.214 12.672 -0.367 1.00 15.69 ? 120 ASN B CA 1 ATOM 2522 C C . ASN B 2 122 ? 19.430 11.868 0.078 1.00 14.89 ? 120 ASN B C 1 ATOM 2523 O O . ASN B 2 122 ? 19.355 10.661 0.294 1.00 18.84 ? 120 ASN B O 1 ATOM 2524 C CB . ASN B 2 122 ? 17.484 13.164 0.890 1.00 16.25 ? 120 ASN B CB 1 ATOM 2525 C CG . ASN B 2 122 ? 16.337 14.097 0.574 1.00 17.49 ? 120 ASN B CG 1 ATOM 2526 O OD1 . ASN B 2 122 ? 15.212 13.661 0.323 1.00 21.80 ? 120 ASN B OD1 1 ATOM 2527 N ND2 . ASN B 2 122 ? 16.609 15.395 0.610 1.00 22.94 ? 120 ASN B ND2 1 ATOM 2528 N N . GLY B 2 123 ? 20.550 12.568 0.216 1.00 18.55 ? 121 GLY B N 1 ATOM 2529 C CA . GLY B 2 123 ? 21.723 12.042 0.886 1.00 14.92 ? 121 GLY B CA 1 ATOM 2530 C C . GLY B 2 123 ? 22.631 11.138 0.076 1.00 21.59 ? 121 GLY B C 1 ATOM 2531 O O . GLY B 2 123 ? 23.428 10.399 0.647 1.00 24.40 ? 121 GLY B O 1 ATOM 2532 N N . PHE B 2 124 ? 22.525 11.182 -1.248 1.00 15.78 ? 122 PHE B N 1 ATOM 2533 C CA . PHE B 2 124 ? 23.273 10.226 -2.057 1.00 17.13 ? 122 PHE B CA 1 ATOM 2534 C C . PHE B 2 124 ? 24.615 10.775 -2.557 1.00 19.94 ? 122 PHE B C 1 ATOM 2535 O O . PHE B 2 124 ? 24.825 11.987 -2.625 1.00 21.69 ? 122 PHE B O 1 ATOM 2536 C CB . PHE B 2 124 ? 22.425 9.741 -3.241 1.00 14.75 ? 122 PHE B CB 1 ATOM 2537 C CG . PHE B 2 124 ? 21.943 10.836 -4.159 1.00 13.68 ? 122 PHE B CG 1 ATOM 2538 C CD1 . PHE B 2 124 ? 20.734 11.475 -3.927 1.00 15.20 ? 122 PHE B CD1 1 ATOM 2539 C CD2 . PHE B 2 124 ? 22.672 11.186 -5.286 1.00 13.52 ? 122 PHE B CD2 1 ATOM 2540 C CE1 . PHE B 2 124 ? 20.274 12.465 -4.785 1.00 16.03 ? 122 PHE B CE1 1 ATOM 2541 C CE2 . PHE B 2 124 ? 22.220 12.171 -6.150 1.00 13.42 ? 122 PHE B CE2 1 ATOM 2542 C CZ . PHE B 2 124 ? 21.018 12.815 -5.899 1.00 13.45 ? 122 PHE B CZ 1 ATOM 2543 N N . TYR B 2 125 ? 25.511 9.852 -2.903 1.00 18.41 ? 123 TYR B N 1 ATOM 2544 C CA . TYR B 2 125 ? 26.800 10.156 -3.526 1.00 13.97 ? 123 TYR B CA 1 ATOM 2545 C C . TYR B 2 125 ? 27.257 8.927 -4.318 1.00 19.21 ? 123 TYR B C 1 ATOM 2546 O O . TYR B 2 125 ? 27.151 7.807 -3.824 1.00 14.63 ? 123 TYR B O 1 ATOM 2547 C CB . TYR B 2 125 ? 27.860 10.556 -2.489 1.00 15.27 ? 123 TYR B CB 1 ATOM 2548 C CG . TYR B 2 125 ? 29.118 11.140 -3.116 1.00 18.32 ? 123 TYR B CG 1 ATOM 2549 C CD1 . TYR B 2 125 ? 30.141 10.314 -3.575 1.00 16.66 ? 123 TYR B CD1 1 ATOM 2550 C CD2 . TYR B 2 125 ? 29.272 12.514 -3.267 1.00 18.73 ? 123 TYR B CD2 1 ATOM 2551 C CE1 . TYR B 2 125 ? 31.279 10.842 -4.166 1.00 14.50 ? 123 TYR B CE1 1 ATOM 2552 C CE2 . TYR B 2 125 ? 30.409 13.050 -3.851 1.00 17.25 ? 123 TYR B CE2 1 ATOM 2553 C CZ . TYR B 2 125 ? 31.408 12.209 -4.298 1.00 20.62 ? 123 TYR B CZ 1 ATOM 2554 O OH . TYR B 2 125 ? 32.540 12.737 -4.880 1.00 23.23 ? 123 TYR B OH 1 ATOM 2555 N N . PRO B 2 126 ? 27.794 9.127 -5.536 1.00 14.24 ? 124 PRO B N 1 ATOM 2556 C CA . PRO B 2 126 ? 28.026 10.407 -6.219 1.00 14.01 ? 124 PRO B CA 1 ATOM 2557 C C . PRO B 2 126 ? 26.774 10.995 -6.848 1.00 22.65 ? 124 PRO B C 1 ATOM 2558 O O . PRO B 2 126 ? 25.666 10.526 -6.572 1.00 13.74 ? 124 PRO B O 1 ATOM 2559 C CB . PRO B 2 126 ? 29.052 10.040 -7.292 1.00 17.10 ? 124 PRO B CB 1 ATOM 2560 C CG . PRO B 2 126 ? 28.764 8.605 -7.597 1.00 14.73 ? 124 PRO B CG 1 ATOM 2561 C CD . PRO B 2 126 ? 28.358 7.992 -6.289 1.00 14.72 ? 124 PRO B CD 1 ATOM 2562 N N . GLY B 2 127 ? 26.954 12.022 -7.675 1.00 13.79 ? 125 GLY B N 1 ATOM 2563 C CA . GLY B 2 127 ? 25.832 12.794 -8.173 1.00 23.14 ? 125 GLY B CA 1 ATOM 2564 C C . GLY B 2 127 ? 24.994 12.159 -9.264 1.00 20.00 ? 125 GLY B C 1 ATOM 2565 O O . GLY B 2 127 ? 23.812 12.470 -9.392 1.00 24.17 ? 125 GLY B O 1 ATOM 2566 N N . SER B 2 128 ? 25.595 11.265 -10.043 1.00 23.10 ? 126 SER B N 1 ATOM 2567 C CA . SER B 2 128 ? 24.892 10.629 -11.157 1.00 24.54 ? 126 SER B CA 1 ATOM 2568 C C . SER B 2 128 ? 23.716 9.815 -10.632 1.00 19.29 ? 126 SER B C 1 ATOM 2569 O O . SER B 2 128 ? 23.899 8.880 -9.858 1.00 22.76 ? 126 SER B O 1 ATOM 2570 C CB . SER B 2 128 ? 25.837 9.759 -11.988 1.00 30.62 ? 126 SER B CB 1 ATOM 2571 O OG . SER B 2 128 ? 26.028 8.487 -11.395 1.00 43.09 ? 126 SER B OG 1 ATOM 2572 N N . ILE B 2 129 ? 22.510 10.177 -11.053 1.00 17.17 ? 127 ILE B N 1 ATOM 2573 C CA . ILE B 2 129 ? 21.301 9.497 -10.600 1.00 24.69 ? 127 ILE B CA 1 ATOM 2574 C C . ILE B 2 129 ? 20.191 9.575 -11.641 1.00 24.86 ? 127 ILE B C 1 ATOM 2575 O O . ILE B 2 129 ? 20.139 10.507 -12.446 1.00 27.53 ? 127 ILE B O 1 ATOM 2576 C CB . ILE B 2 129 ? 20.794 10.098 -9.268 1.00 23.88 ? 127 ILE B CB 1 ATOM 2577 C CG1 . ILE B 2 129 ? 19.887 9.111 -8.534 1.00 24.75 ? 127 ILE B CG1 1 ATOM 2578 C CG2 . ILE B 2 129 ? 20.056 11.416 -9.504 1.00 15.54 ? 127 ILE B CG2 1 ATOM 2579 C CD1 . ILE B 2 129 ? 19.672 9.461 -7.081 1.00 23.35 ? 127 ILE B CD1 1 ATOM 2580 N N . GLU B 2 130 ? 19.323 8.569 -11.644 1.00 24.89 ? 128 GLU B N 1 ATOM 2581 C CA . GLU B 2 130 ? 18.173 8.576 -12.532 1.00 27.58 ? 128 GLU B CA 1 ATOM 2582 C C . GLU B 2 130 ? 16.904 8.302 -11.741 1.00 18.19 ? 128 GLU B C 1 ATOM 2583 O O . GLU B 2 130 ? 16.786 7.275 -11.072 1.00 17.35 ? 128 GLU B O 1 ATOM 2584 C CB . GLU B 2 130 ? 18.336 7.543 -13.648 1.00 32.52 ? 128 GLU B CB 1 ATOM 2585 C CG . GLU B 2 130 ? 17.153 7.489 -14.598 1.00 44.63 ? 128 GLU B CG 1 ATOM 2586 C CD . GLU B 2 130 ? 17.297 8.466 -15.754 1.00 51.14 ? 128 GLU B CD 1 ATOM 2587 O OE1 . GLU B 2 130 ? 16.266 8.987 -16.229 1.00 50.94 ? 128 GLU B OE1 1 ATOM 2588 O OE2 . GLU B 2 130 ? 18.442 8.708 -16.191 1.00 51.05 ? 128 GLU B OE2 1 ATOM 2589 N N . VAL B 2 131 ? 15.960 9.231 -11.823 1.00 15.20 ? 129 VAL B N 1 ATOM 2590 C CA . VAL B 2 131 ? 14.696 9.108 -11.115 1.00 20.91 ? 129 VAL B CA 1 ATOM 2591 C C . VAL B 2 131 ? 13.546 9.129 -12.115 1.00 23.70 ? 129 VAL B C 1 ATOM 2592 O O . VAL B 2 131 ? 13.449 10.044 -12.931 1.00 22.05 ? 129 VAL B O 1 ATOM 2593 C CB . VAL B 2 131 ? 14.518 10.251 -10.097 1.00 21.58 ? 129 VAL B CB 1 ATOM 2594 C CG1 . VAL B 2 131 ? 13.216 10.082 -9.324 1.00 17.69 ? 129 VAL B CG1 1 ATOM 2595 C CG2 . VAL B 2 131 ? 15.726 10.330 -9.156 1.00 16.61 ? 129 VAL B CG2 1 ATOM 2596 N N . ARG B 2 132 ? 12.672 8.128 -12.042 1.00 23.08 ? 130 ARG B N 1 ATOM 2597 C CA . ARG B 2 132 ? 11.555 8.025 -12.977 1.00 23.44 ? 130 ARG B CA 1 ATOM 2598 C C . ARG B 2 132 ? 10.231 7.773 -12.259 1.00 22.21 ? 130 ARG B C 1 ATOM 2599 O O . ARG B 2 132 ? 10.185 7.139 -11.202 1.00 17.01 ? 130 ARG B O 1 ATOM 2600 C CB . ARG B 2 132 ? 11.820 6.936 -14.026 1.00 28.37 ? 130 ARG B CB 1 ATOM 2601 C CG . ARG B 2 132 ? 12.999 7.275 -14.935 1.00 37.33 ? 130 ARG B CG 1 ATOM 2602 C CD . ARG B 2 132 ? 13.335 6.197 -15.964 1.00 47.67 ? 130 ARG B CD 1 ATOM 2603 N NE . ARG B 2 132 ? 13.063 4.831 -15.526 1.00 55.46 ? 130 ARG B NE 1 ATOM 2604 C CZ . ARG B 2 132 ? 13.746 3.771 -15.951 1.00 59.18 ? 130 ARG B CZ 1 ATOM 2605 N NH1 . ARG B 2 132 ? 14.752 3.931 -16.803 1.00 64.57 ? 130 ARG B NH1 1 ATOM 2606 N NH2 . ARG B 2 132 ? 13.444 2.555 -15.511 1.00 48.98 ? 130 ARG B NH2 1 ATOM 2607 N N . TRP B 2 133 ? 9.153 8.276 -12.845 1.00 17.33 ? 131 TRP B N 1 ATOM 2608 C CA . TRP B 2 133 ? 7.833 8.091 -12.275 1.00 17.69 ? 131 TRP B CA 1 ATOM 2609 C C . TRP B 2 133 ? 7.026 7.054 -13.027 1.00 23.73 ? 131 TRP B C 1 ATOM 2610 O O . TRP B 2 133 ? 7.107 6.953 -14.249 1.00 25.70 ? 131 TRP B O 1 ATOM 2611 C CB . TRP B 2 133 ? 7.056 9.407 -12.282 1.00 20.50 ? 131 TRP B CB 1 ATOM 2612 C CG . TRP B 2 133 ? 7.259 10.261 -11.082 1.00 22.88 ? 131 TRP B CG 1 ATOM 2613 C CD1 . TRP B 2 133 ? 7.961 11.428 -11.013 1.00 22.83 ? 131 TRP B CD1 1 ATOM 2614 C CD2 . TRP B 2 133 ? 6.726 10.032 -9.774 1.00 19.57 ? 131 TRP B CD2 1 ATOM 2615 N NE1 . TRP B 2 133 ? 7.908 11.935 -9.737 1.00 18.79 ? 131 TRP B NE1 1 ATOM 2616 C CE2 . TRP B 2 133 ? 7.154 11.096 -8.958 1.00 17.81 ? 131 TRP B CE2 1 ATOM 2617 C CE3 . TRP B 2 133 ? 5.933 9.026 -9.213 1.00 21.04 ? 131 TRP B CE3 1 ATOM 2618 C CZ2 . TRP B 2 133 ? 6.817 11.184 -7.610 1.00 16.98 ? 131 TRP B CZ2 1 ATOM 2619 C CZ3 . TRP B 2 133 ? 5.598 9.115 -7.874 1.00 23.94 ? 131 TRP B CZ3 1 ATOM 2620 C CH2 . TRP B 2 133 ? 6.041 10.186 -7.088 1.00 22.18 ? 131 TRP B CH2 1 ATOM 2621 N N . PHE B 2 134 ? 6.237 6.292 -12.281 1.00 18.99 ? 132 PHE B N 1 ATOM 2622 C CA . PHE B 2 134 ? 5.363 5.304 -12.880 1.00 26.00 ? 132 PHE B CA 1 ATOM 2623 C C . PHE B 2 134 ? 3.966 5.453 -12.295 1.00 25.96 ? 132 PHE B C 1 ATOM 2624 O O . PHE B 2 134 ? 3.798 5.686 -11.099 1.00 27.76 ? 132 PHE B O 1 ATOM 2625 C CB . PHE B 2 134 ? 5.901 3.886 -12.646 1.00 20.48 ? 132 PHE B CB 1 ATOM 2626 C CG . PHE B 2 134 ? 7.196 3.602 -13.361 1.00 27.43 ? 132 PHE B CG 1 ATOM 2627 C CD1 . PHE B 2 134 ? 8.407 4.025 -12.835 1.00 26.68 ? 132 PHE B CD1 1 ATOM 2628 C CD2 . PHE B 2 134 ? 7.201 2.893 -14.550 1.00 25.68 ? 132 PHE B CD2 1 ATOM 2629 C CE1 . PHE B 2 134 ? 9.597 3.766 -13.494 1.00 25.46 ? 132 PHE B CE1 1 ATOM 2630 C CE2 . PHE B 2 134 ? 8.387 2.628 -15.214 1.00 25.56 ? 132 PHE B CE2 1 ATOM 2631 C CZ . PHE B 2 134 ? 9.586 3.063 -14.685 1.00 22.96 ? 132 PHE B CZ 1 ATOM 2632 N N . ARG B 2 135 ? 2.969 5.325 -13.157 1.00 28.48 ? 133 ARG B N 1 ATOM 2633 C CA . ARG B 2 135 ? 1.580 5.300 -12.738 1.00 31.88 ? 133 ARG B CA 1 ATOM 2634 C C . ARG B 2 135 ? 1.031 3.942 -13.154 1.00 34.15 ? 133 ARG B C 1 ATOM 2635 O O . ARG B 2 135 ? 0.977 3.634 -14.344 1.00 33.45 ? 133 ARG B O 1 ATOM 2636 C CB . ARG B 2 135 ? 0.795 6.473 -13.338 1.00 32.15 ? 133 ARG B CB 1 ATOM 2637 C CG . ARG B 2 135 ? -0.671 6.543 -12.924 1.00 34.12 ? 133 ARG B CG 1 ATOM 2638 C CD . ARG B 2 135 ? -1.456 7.555 -13.761 1.00 39.29 ? 133 ARG B CD 1 ATOM 2639 N NE . ARG B 2 135 ? -1.455 7.254 -15.192 1.00 58.23 ? 133 ARG B NE 1 ATOM 2640 C CZ . ARG B 2 135 ? -0.609 7.783 -16.073 1.00 67.79 ? 133 ARG B CZ 1 ATOM 2641 N NH1 . ARG B 2 135 ? 0.318 8.646 -15.674 1.00 61.21 ? 133 ARG B NH1 1 ATOM 2642 N NH2 . ARG B 2 135 ? -0.686 7.447 -17.353 1.00 74.08 ? 133 ARG B NH2 1 ATOM 2643 N N . ASN B 2 136 ? 0.645 3.134 -12.171 1.00 38.49 ? 134 ASN B N 1 ATOM 2644 C CA . ASN B 2 136 ? 0.199 1.761 -12.405 1.00 44.48 ? 134 ASN B CA 1 ATOM 2645 C C . ASN B 2 136 ? 1.135 0.938 -13.292 1.00 42.48 ? 134 ASN B C 1 ATOM 2646 O O . ASN B 2 136 ? 0.685 0.222 -14.184 1.00 39.90 ? 134 ASN B O 1 ATOM 2647 C CB . ASN B 2 136 ? -1.198 1.760 -13.034 1.00 45.38 ? 134 ASN B CB 1 ATOM 2648 C CG . ASN B 2 136 ? -2.246 2.365 -12.126 1.00 47.24 ? 134 ASN B CG 1 ATOM 2649 O OD1 . ASN B 2 136 ? -2.208 2.188 -10.908 1.00 49.87 ? 134 ASN B OD1 1 ATOM 2650 N ND2 . ASN B 2 136 ? -3.196 3.081 -12.717 1.00 49.41 ? 134 ASN B ND2 1 ATOM 2651 N N . GLY B 2 137 ? 2.438 1.057 -13.054 1.00 44.48 ? 135 GLY B N 1 ATOM 2652 C CA . GLY B 2 137 ? 3.412 0.243 -13.760 1.00 42.17 ? 135 GLY B CA 1 ATOM 2653 C C . GLY B 2 137 ? 3.863 0.785 -15.099 1.00 41.31 ? 135 GLY B C 1 ATOM 2654 O O . GLY B 2 137 ? 4.711 0.186 -15.761 1.00 43.39 ? 135 GLY B O 1 ATOM 2655 N N . GLN B 2 138 ? 3.297 1.918 -15.501 1.00 44.38 ? 136 GLN B N 1 ATOM 2656 C CA . GLN B 2 138 ? 3.660 2.555 -16.762 1.00 40.54 ? 136 GLN B CA 1 ATOM 2657 C C . GLN B 2 138 ? 4.454 3.828 -16.503 1.00 30.77 ? 136 GLN B C 1 ATOM 2658 O O . GLN B 2 138 ? 4.047 4.654 -15.693 1.00 32.65 ? 136 GLN B O 1 ATOM 2659 C CB . GLN B 2 138 ? 2.408 2.891 -17.578 1.00 52.34 ? 136 GLN B CB 1 ATOM 2660 C CG . GLN B 2 138 ? 1.482 1.713 -17.843 1.00 64.68 ? 136 GLN B CG 1 ATOM 2661 C CD . GLN B 2 138 ? 2.094 0.677 -18.765 1.00 73.67 ? 136 GLN B CD 1 ATOM 2662 O OE1 . GLN B 2 138 ? 2.988 0.978 -19.554 1.00 76.42 ? 136 GLN B OE1 1 ATOM 2663 N NE2 . GLN B 2 138 ? 1.603 -0.556 -18.674 1.00 74.75 ? 136 GLN B NE2 1 ATOM 2664 N N . GLU B 2 139 ? 5.585 3.992 -17.179 1.00 29.17 ? 137 GLU B N 1 ATOM 2665 C CA . GLU B 2 139 ? 6.392 5.183 -16.951 1.00 29.50 ? 137 GLU B CA 1 ATOM 2666 C C . GLU B 2 139 ? 5.632 6.409 -17.431 1.00 27.56 ? 137 GLU B C 1 ATOM 2667 O O . GLU B 2 139 ? 5.081 6.422 -18.534 1.00 24.18 ? 137 GLU B O 1 ATOM 2668 C CB . GLU B 2 139 ? 7.757 5.109 -17.635 1.00 27.76 ? 137 GLU B CB 1 ATOM 2669 C CG . GLU B 2 139 ? 8.605 6.345 -17.326 1.00 27.77 ? 137 GLU B CG 1 ATOM 2670 C CD . GLU B 2 139 ? 10.003 6.286 -17.901 1.00 34.98 ? 137 GLU B CD 1 ATOM 2671 O OE1 . GLU B 2 139 ? 10.361 5.260 -18.512 1.00 38.17 ? 137 GLU B OE1 1 ATOM 2672 O OE2 . GLU B 2 139 ? 10.751 7.274 -17.729 1.00 38.65 ? 137 GLU B OE2 1 ATOM 2673 N N . GLU B 2 140 ? 5.613 7.439 -16.597 1.00 25.12 ? 138 GLU B N 1 ATOM 2674 C CA . GLU B 2 140 ? 5.005 8.706 -16.965 1.00 26.74 ? 138 GLU B CA 1 ATOM 2675 C C . GLU B 2 140 ? 6.104 9.719 -17.255 1.00 23.99 ? 138 GLU B C 1 ATOM 2676 O O . GLU B 2 140 ? 6.865 10.097 -16.365 1.00 20.02 ? 138 GLU B O 1 ATOM 2677 C CB . GLU B 2 140 ? 4.090 9.205 -15.844 1.00 29.21 ? 138 GLU B CB 1 ATOM 2678 C CG . GLU B 2 140 ? 3.348 10.483 -16.170 1.00 36.84 ? 138 GLU B CG 1 ATOM 2679 C CD . GLU B 2 140 ? 2.511 10.366 -17.426 1.00 45.27 ? 138 GLU B CD 1 ATOM 2680 O OE1 . GLU B 2 140 ? 1.531 9.591 -17.421 1.00 53.04 ? 138 GLU B OE1 1 ATOM 2681 O OE2 . GLU B 2 140 ? 2.834 11.048 -18.420 1.00 42.47 ? 138 GLU B OE2 1 ATOM 2682 N N . LYS B 2 141 ? 6.193 10.139 -18.515 1.00 23.08 ? 139 LYS B N 1 ATOM 2683 C CA . LYS B 2 141 ? 7.221 11.085 -18.933 1.00 26.82 ? 139 LYS B CA 1 ATOM 2684 C C . LYS B 2 141 ? 6.714 12.514 -19.128 1.00 32.15 ? 139 LYS B C 1 ATOM 2685 O O . LYS B 2 141 ? 7.512 13.434 -19.296 1.00 32.11 ? 139 LYS B O 1 ATOM 2686 C CB . LYS B 2 141 ? 7.884 10.596 -20.226 1.00 31.95 ? 139 LYS B CB 1 ATOM 2687 C CG . LYS B 2 141 ? 8.792 9.390 -20.035 1.00 36.69 ? 139 LYS B CG 1 ATOM 2688 C CD . LYS B 2 141 ? 9.507 9.029 -21.329 1.00 45.02 ? 139 LYS B CD 1 ATOM 2689 C CE . LYS B 2 141 ? 10.471 7.869 -21.128 1.00 44.12 ? 139 LYS B CE 1 ATOM 2690 N NZ . LYS B 2 141 ? 11.037 7.380 -22.417 1.00 40.78 ? 139 LYS B NZ 1 ATOM 2691 N N . THR B 2 142 ? 5.400 12.709 -19.113 1.00 30.67 ? 140 THR B N 1 ATOM 2692 C CA . THR B 2 142 ? 4.859 14.057 -19.269 1.00 26.55 ? 140 THR B CA 1 ATOM 2693 C C . THR B 2 142 ? 4.619 14.690 -17.905 1.00 19.44 ? 140 THR B C 1 ATOM 2694 O O . THR B 2 142 ? 4.308 13.996 -16.939 1.00 27.81 ? 140 THR B O 1 ATOM 2695 C CB . THR B 2 142 ? 3.532 14.069 -20.058 1.00 25.94 ? 140 THR B CB 1 ATOM 2696 O OG1 . THR B 2 142 ? 2.500 13.468 -19.267 1.00 43.11 ? 140 THR B OG1 1 ATOM 2697 C CG2 . THR B 2 142 ? 3.671 13.310 -21.366 1.00 19.97 ? 140 THR B CG2 1 ATOM 2698 N N . GLY B 2 143 ? 4.752 16.009 -17.828 1.00 21.00 ? 141 GLY B N 1 ATOM 2699 C CA . GLY B 2 143 ? 4.486 16.715 -16.590 1.00 16.06 ? 141 GLY B CA 1 ATOM 2700 C C . GLY B 2 143 ? 5.497 16.460 -15.486 1.00 21.72 ? 141 GLY B C 1 ATOM 2701 O O . GLY B 2 143 ? 5.157 16.531 -14.304 1.00 23.98 ? 141 GLY B O 1 ATOM 2702 N N . VAL B 2 144 ? 6.739 16.158 -15.857 1.00 20.27 ? 142 VAL B N 1 ATOM 2703 C CA . VAL B 2 144 ? 7.774 15.927 -14.855 1.00 22.67 ? 142 VAL B CA 1 ATOM 2704 C C . VAL B 2 144 ? 8.723 17.117 -14.772 1.00 17.08 ? 142 VAL B C 1 ATOM 2705 O O . VAL B 2 144 ? 9.303 17.535 -15.774 1.00 21.50 ? 142 VAL B O 1 ATOM 2706 C CB . VAL B 2 144 ? 8.591 14.651 -15.170 1.00 20.32 ? 142 VAL B CB 1 ATOM 2707 C CG1 . VAL B 2 144 ? 9.751 14.497 -14.202 1.00 15.93 ? 142 VAL B CG1 1 ATOM 2708 C CG2 . VAL B 2 144 ? 7.691 13.425 -15.148 1.00 19.15 ? 142 VAL B CG2 1 ATOM 2709 N N . VAL B 2 145 ? 8.875 17.659 -13.569 1.00 16.72 ? 143 VAL B N 1 ATOM 2710 C CA . VAL B 2 145 ? 9.775 18.786 -13.337 1.00 26.46 ? 143 VAL B CA 1 ATOM 2711 C C . VAL B 2 145 ? 10.657 18.492 -12.123 1.00 23.97 ? 143 VAL B C 1 ATOM 2712 O O . VAL B 2 145 ? 10.245 17.787 -11.205 1.00 17.70 ? 143 VAL B O 1 ATOM 2713 C CB . VAL B 2 145 ? 8.989 20.112 -13.144 1.00 18.81 ? 143 VAL B CB 1 ATOM 2714 C CG1 . VAL B 2 145 ? 8.202 20.095 -11.844 1.00 23.33 ? 143 VAL B CG1 1 ATOM 2715 C CG2 . VAL B 2 145 ? 9.924 21.312 -13.197 1.00 19.68 ? 143 VAL B CG2 1 ATOM 2716 N N . SER B 2 146 ? 11.873 19.029 -12.122 1.00 16.98 ? 144 SER B N 1 ATOM 2717 C CA . SER B 2 146 ? 12.807 18.762 -11.035 1.00 18.63 ? 144 SER B CA 1 ATOM 2718 C C . SER B 2 146 ? 13.578 19.986 -10.571 1.00 22.09 ? 144 SER B C 1 ATOM 2719 O O . SER B 2 146 ? 13.664 20.991 -11.274 1.00 18.22 ? 144 SER B O 1 ATOM 2720 C CB . SER B 2 146 ? 13.798 17.677 -11.455 1.00 13.14 ? 144 SER B CB 1 ATOM 2721 O OG . SER B 2 146 ? 14.776 17.454 -10.453 1.00 12.92 ? 144 SER B OG 1 ATOM 2722 N N . THR B 2 147 ? 14.143 19.879 -9.374 1.00 19.81 ? 145 THR B N 1 ATOM 2723 C CA . THR B 2 147 ? 15.082 20.871 -8.872 1.00 22.40 ? 145 THR B CA 1 ATOM 2724 C C . THR B 2 147 ? 16.403 20.769 -9.631 1.00 22.45 ? 145 THR B C 1 ATOM 2725 O O . THR B 2 147 ? 17.215 21.693 -9.612 1.00 19.83 ? 145 THR B O 1 ATOM 2726 C CB . THR B 2 147 ? 15.352 20.685 -7.371 1.00 12.48 ? 145 THR B CB 1 ATOM 2727 O OG1 . THR B 2 147 ? 15.769 19.336 -7.130 1.00 21.17 ? 145 THR B OG1 1 ATOM 2728 C CG2 . THR B 2 147 ? 14.104 20.966 -6.564 1.00 16.67 ? 145 THR B CG2 1 ATOM 2729 N N . GLY B 2 148 ? 16.619 19.634 -10.291 1.00 12.42 ? 146 GLY B N 1 ATOM 2730 C CA . GLY B 2 148 ? 17.930 19.316 -10.822 1.00 12.32 ? 146 GLY B CA 1 ATOM 2731 C C . GLY B 2 148 ? 18.783 18.734 -9.714 1.00 17.44 ? 146 GLY B C 1 ATOM 2732 O O . GLY B 2 148 ? 18.283 18.457 -8.624 1.00 14.44 ? 146 GLY B O 1 ATOM 2733 N N . LEU B 2 149 ? 20.064 18.523 -9.991 1.00 12.95 ? 147 LEU B N 1 ATOM 2734 C CA . LEU B 2 149 ? 20.950 17.950 -8.992 1.00 13.33 ? 147 LEU B CA 1 ATOM 2735 C C . LEU B 2 149 ? 21.420 19.025 -8.024 1.00 18.12 ? 147 LEU B C 1 ATOM 2736 O O . LEU B 2 149 ? 22.023 20.015 -8.430 1.00 16.54 ? 147 LEU B O 1 ATOM 2737 C CB . LEU B 2 149 ? 22.150 17.276 -9.653 1.00 14.45 ? 147 LEU B CB 1 ATOM 2738 C CG . LEU B 2 149 ? 23.096 16.580 -8.677 1.00 23.27 ? 147 LEU B CG 1 ATOM 2739 C CD1 . LEU B 2 149 ? 22.376 15.423 -7.999 1.00 17.97 ? 147 LEU B CD1 1 ATOM 2740 C CD2 . LEU B 2 149 ? 24.356 16.100 -9.383 1.00 29.27 ? 147 LEU B CD2 1 ATOM 2741 N N . ILE B 2 150 ? 21.154 18.818 -6.739 1.00 20.25 ? 148 ILE B N 1 ATOM 2742 C CA . ILE B 2 150 ? 21.544 19.786 -5.722 1.00 17.48 ? 148 ILE B CA 1 ATOM 2743 C C . ILE B 2 150 ? 22.678 19.267 -4.855 1.00 13.78 ? 148 ILE B C 1 ATOM 2744 O O . ILE B 2 150 ? 22.566 18.216 -4.229 1.00 12.47 ? 148 ILE B O 1 ATOM 2745 C CB . ILE B 2 150 ? 20.360 20.152 -4.817 1.00 18.02 ? 148 ILE B CB 1 ATOM 2746 C CG1 . ILE B 2 150 ? 19.217 20.740 -5.647 1.00 15.83 ? 148 ILE B CG1 1 ATOM 2747 C CG2 . ILE B 2 150 ? 20.804 21.127 -3.736 1.00 15.71 ? 148 ILE B CG2 1 ATOM 2748 C CD1 . ILE B 2 150 ? 17.947 20.965 -4.851 1.00 27.49 ? 148 ILE B CD1 1 ATOM 2749 N N . GLN B 2 151 ? 23.773 20.015 -4.827 1.00 11.54 ? 149 GLN B N 1 ATOM 2750 C CA . GLN B 2 151 ? 24.866 19.718 -3.918 1.00 18.81 ? 149 GLN B CA 1 ATOM 2751 C C . GLN B 2 151 ? 24.559 20.279 -2.530 1.00 18.23 ? 149 GLN B C 1 ATOM 2752 O O . GLN B 2 151 ? 24.128 21.423 -2.398 1.00 22.74 ? 149 GLN B O 1 ATOM 2753 C CB . GLN B 2 151 ? 26.165 20.301 -4.475 1.00 20.23 ? 149 GLN B CB 1 ATOM 2754 C CG . GLN B 2 151 ? 27.373 19.391 -4.377 1.00 38.99 ? 149 GLN B CG 1 ATOM 2755 C CD . GLN B 2 151 ? 28.501 19.827 -5.292 1.00 44.67 ? 149 GLN B CD 1 ATOM 2756 O OE1 . GLN B 2 151 ? 28.510 20.950 -5.797 1.00 43.06 ? 149 GLN B OE1 1 ATOM 2757 N NE2 . GLN B 2 151 ? 29.459 18.935 -5.515 1.00 50.93 ? 149 GLN B NE2 1 ATOM 2758 N N . ASN B 2 152 ? 24.774 19.474 -1.495 1.00 15.70 ? 150 ASN B N 1 ATOM 2759 C CA . ASN B 2 152 ? 24.531 19.930 -0.130 1.00 11.86 ? 150 ASN B CA 1 ATOM 2760 C C . ASN B 2 152 ? 25.792 20.516 0.500 1.00 13.06 ? 150 ASN B C 1 ATOM 2761 O O . ASN B 2 152 ? 25.739 21.106 1.580 1.00 13.59 ? 150 ASN B O 1 ATOM 2762 C CB . ASN B 2 152 ? 23.985 18.788 0.730 1.00 20.75 ? 150 ASN B CB 1 ATOM 2763 C CG . ASN B 2 152 ? 22.576 18.384 0.330 1.00 24.53 ? 150 ASN B CG 1 ATOM 2764 O OD1 . ASN B 2 152 ? 21.748 19.234 -0.004 1.00 23.63 ? 150 ASN B OD1 1 ATOM 2765 N ND2 . ASN B 2 152 ? 22.295 17.084 0.366 1.00 16.62 ? 150 ASN B ND2 1 ATOM 2766 N N . GLY B 2 153 ? 26.926 20.326 -0.174 1.00 13.16 ? 151 GLY B N 1 ATOM 2767 C CA . GLY B 2 153 ? 28.195 20.884 0.258 1.00 11.96 ? 151 GLY B CA 1 ATOM 2768 C C . GLY B 2 153 ? 28.933 19.990 1.236 1.00 14.57 ? 151 GLY B C 1 ATOM 2769 O O . GLY B 2 153 ? 30.029 20.319 1.696 1.00 15.23 ? 151 GLY B O 1 ATOM 2770 N N . ASP B 2 154 ? 28.323 18.859 1.569 1.00 15.76 ? 152 ASP B N 1 ATOM 2771 C CA . ASP B 2 154 ? 28.867 17.971 2.591 1.00 16.42 ? 152 ASP B CA 1 ATOM 2772 C C . ASP B 2 154 ? 29.079 16.545 2.084 1.00 16.51 ? 152 ASP B C 1 ATOM 2773 O O . ASP B 2 154 ? 28.937 15.583 2.847 1.00 19.87 ? 152 ASP B O 1 ATOM 2774 C CB . ASP B 2 154 ? 27.940 17.968 3.815 1.00 19.36 ? 152 ASP B CB 1 ATOM 2775 C CG . ASP B 2 154 ? 26.565 17.390 3.510 1.00 20.12 ? 152 ASP B CG 1 ATOM 2776 O OD1 . ASP B 2 154 ? 26.269 17.141 2.323 1.00 20.09 ? 152 ASP B OD1 1 ATOM 2777 O OD2 . ASP B 2 154 ? 25.779 17.175 4.458 1.00 27.15 ? 152 ASP B OD2 1 ATOM 2778 N N . TRP B 2 155 ? 29.402 16.424 0.797 1.00 11.78 ? 153 TRP B N 1 ATOM 2779 C CA . TRP B 2 155 ? 29.604 15.134 0.135 1.00 18.72 ? 153 TRP B CA 1 ATOM 2780 C C . TRP B 2 155 ? 28.322 14.306 0.047 1.00 20.45 ? 153 TRP B C 1 ATOM 2781 O O . TRP B 2 155 ? 28.368 13.074 0.008 1.00 17.91 ? 153 TRP B O 1 ATOM 2782 C CB . TRP B 2 155 ? 30.716 14.328 0.813 1.00 18.22 ? 153 TRP B CB 1 ATOM 2783 C CG . TRP B 2 155 ? 32.074 14.902 0.590 1.00 15.88 ? 153 TRP B CG 1 ATOM 2784 C CD1 . TRP B 2 155 ? 32.627 15.980 1.218 1.00 13.05 ? 153 TRP B CD1 1 ATOM 2785 C CD2 . TRP B 2 155 ? 33.053 14.434 -0.344 1.00 16.82 ? 153 TRP B CD2 1 ATOM 2786 N NE1 . TRP B 2 155 ? 33.897 16.205 0.738 1.00 15.63 ? 153 TRP B NE1 1 ATOM 2787 C CE2 . TRP B 2 155 ? 34.179 15.270 -0.223 1.00 14.34 ? 153 TRP B CE2 1 ATOM 2788 C CE3 . TRP B 2 155 ? 33.085 13.387 -1.270 1.00 13.20 ? 153 TRP B CE3 1 ATOM 2789 C CZ2 . TRP B 2 155 ? 35.326 15.091 -0.992 1.00 15.21 ? 153 TRP B CZ2 1 ATOM 2790 C CZ3 . TRP B 2 155 ? 34.223 13.210 -2.029 1.00 14.05 ? 153 TRP B CZ3 1 ATOM 2791 C CH2 . TRP B 2 155 ? 35.328 14.057 -1.887 1.00 16.56 ? 153 TRP B CH2 1 ATOM 2792 N N . THR B 2 156 ? 27.181 14.987 0.019 1.00 11.97 ? 154 THR B N 1 ATOM 2793 C CA . THR B 2 156 ? 25.919 14.327 -0.301 1.00 14.92 ? 154 THR B CA 1 ATOM 2794 C C . THR B 2 156 ? 25.150 15.201 -1.282 1.00 18.74 ? 154 THR B C 1 ATOM 2795 O O . THR B 2 156 ? 25.350 16.416 -1.335 1.00 13.58 ? 154 THR B O 1 ATOM 2796 C CB . THR B 2 156 ? 25.035 14.072 0.946 1.00 16.14 ? 154 THR B CB 1 ATOM 2797 O OG1 . THR B 2 156 ? 24.600 15.320 1.495 1.00 16.88 ? 154 THR B OG1 1 ATOM 2798 C CG2 . THR B 2 156 ? 25.786 13.284 2.011 1.00 13.25 ? 154 THR B CG2 1 ATOM 2799 N N . PHE B 2 157 ? 24.259 14.581 -2.048 1.00 12.09 ? 155 PHE B N 1 ATOM 2800 C CA . PHE B 2 157 ? 23.408 15.316 -2.970 1.00 12.00 ? 155 PHE B CA 1 ATOM 2801 C C . PHE B 2 157 ? 21.956 15.116 -2.602 1.00 13.96 ? 155 PHE B C 1 ATOM 2802 O O . PHE B 2 157 ? 21.618 14.228 -1.820 1.00 12.99 ? 155 PHE B O 1 ATOM 2803 C CB . PHE B 2 157 ? 23.597 14.850 -4.423 1.00 20.01 ? 155 PHE B CB 1 ATOM 2804 C CG . PHE B 2 157 ? 24.940 15.168 -5.014 1.00 16.97 ? 155 PHE B CG 1 ATOM 2805 C CD1 . PHE B 2 157 ? 25.130 16.333 -5.739 1.00 17.84 ? 155 PHE B CD1 1 ATOM 2806 C CD2 . PHE B 2 157 ? 25.996 14.283 -4.886 1.00 21.39 ? 155 PHE B CD2 1 ATOM 2807 C CE1 . PHE B 2 157 ? 26.359 16.624 -6.304 1.00 18.76 ? 155 PHE B CE1 1 ATOM 2808 C CE2 . PHE B 2 157 ? 27.229 14.567 -5.448 1.00 22.93 ? 155 PHE B CE2 1 ATOM 2809 C CZ . PHE B 2 157 ? 27.411 15.742 -6.158 1.00 22.57 ? 155 PHE B CZ 1 ATOM 2810 N N . GLN B 2 158 ? 21.097 15.927 -3.205 1.00 16.57 ? 156 GLN B N 1 ATOM 2811 C CA . GLN B 2 158 ? 19.673 15.654 -3.178 1.00 22.02 ? 156 GLN B CA 1 ATOM 2812 C C . GLN B 2 158 ? 19.044 16.123 -4.484 1.00 20.81 ? 156 GLN B C 1 ATOM 2813 O O . GLN B 2 158 ? 19.638 16.894 -5.242 1.00 14.40 ? 156 GLN B O 1 ATOM 2814 C CB . GLN B 2 158 ? 19.003 16.333 -1.984 1.00 12.58 ? 156 GLN B CB 1 ATOM 2815 C CG . GLN B 2 158 ? 19.080 17.842 -2.005 1.00 13.56 ? 156 GLN B CG 1 ATOM 2816 C CD . GLN B 2 158 ? 18.260 18.471 -0.899 1.00 20.95 ? 156 GLN B CD 1 ATOM 2817 O OE1 . GLN B 2 158 ? 17.030 18.399 -0.904 1.00 23.93 ? 156 GLN B OE1 1 ATOM 2818 N NE2 . GLN B 2 158 ? 18.938 19.085 0.062 1.00 16.82 ? 156 GLN B NE2 1 ATOM 2819 N N . THR B 2 159 ? 17.837 15.647 -4.745 1.00 17.66 ? 157 THR B N 1 ATOM 2820 C CA . THR B 2 159 ? 17.052 16.140 -5.861 1.00 12.64 ? 157 THR B CA 1 ATOM 2821 C C . THR B 2 159 ? 15.588 15.869 -5.593 1.00 13.73 ? 157 THR B C 1 ATOM 2822 O O . THR B 2 159 ? 15.240 14.854 -4.991 1.00 20.87 ? 157 THR B O 1 ATOM 2823 C CB . THR B 2 159 ? 17.486 15.505 -7.205 1.00 16.98 ? 157 THR B CB 1 ATOM 2824 O OG1 . THR B 2 159 ? 16.723 16.076 -8.277 1.00 18.77 ? 157 THR B OG1 1 ATOM 2825 C CG2 . THR B 2 159 ? 17.293 13.991 -7.196 1.00 19.61 ? 157 THR B CG2 1 ATOM 2826 N N . LEU B 2 160 ? 14.731 16.788 -6.013 1.00 12.98 ? 158 LEU B N 1 ATOM 2827 C CA . LEU B 2 160 ? 13.299 16.554 -5.955 1.00 13.39 ? 158 LEU B CA 1 ATOM 2828 C C . LEU B 2 160 ? 12.809 16.339 -7.376 1.00 16.20 ? 158 LEU B C 1 ATOM 2829 O O . LEU B 2 160 ? 13.106 17.137 -8.261 1.00 15.59 ? 158 LEU B O 1 ATOM 2830 C CB . LEU B 2 160 ? 12.558 17.740 -5.332 1.00 18.94 ? 158 LEU B CB 1 ATOM 2831 C CG . LEU B 2 160 ? 12.921 18.299 -3.956 1.00 26.97 ? 158 LEU B CG 1 ATOM 2832 C CD1 . LEU B 2 160 ? 11.830 19.249 -3.483 1.00 29.75 ? 158 LEU B CD1 1 ATOM 2833 C CD2 . LEU B 2 160 ? 13.147 17.202 -2.948 1.00 25.95 ? 158 LEU B CD2 1 ATOM 2834 N N . VAL B 2 161 ? 12.060 15.267 -7.600 1.00 20.54 ? 159 VAL B N 1 ATOM 2835 C CA . VAL B 2 161 ? 11.495 15.013 -8.918 1.00 16.38 ? 159 VAL B CA 1 ATOM 2836 C C . VAL B 2 161 ? 9.989 14.948 -8.767 1.00 22.09 ? 159 VAL B C 1 ATOM 2837 O O . VAL B 2 161 ? 9.440 14.047 -8.132 1.00 18.66 ? 159 VAL B O 1 ATOM 2838 C CB . VAL B 2 161 ? 12.031 13.721 -9.545 1.00 17.51 ? 159 VAL B CB 1 ATOM 2839 C CG1 . VAL B 2 161 ? 11.430 13.511 -10.920 1.00 18.67 ? 159 VAL B CG1 1 ATOM 2840 C CG2 . VAL B 2 161 ? 13.540 13.779 -9.625 1.00 13.80 ? 159 VAL B CG2 1 ATOM 2841 N N . MET B 2 162 ? 9.331 15.929 -9.365 1.00 19.90 ? 160 MET B N 1 ATOM 2842 C CA . MET B 2 162 ? 7.900 16.101 -9.212 1.00 21.19 ? 160 MET B CA 1 ATOM 2843 C C . MET B 2 162 ? 7.094 15.673 -10.429 1.00 19.70 ? 160 MET B C 1 ATOM 2844 O O . MET B 2 162 ? 7.492 15.891 -11.572 1.00 22.10 ? 160 MET B O 1 ATOM 2845 C CB . MET B 2 162 ? 7.633 17.559 -8.856 1.00 17.71 ? 160 MET B CB 1 ATOM 2846 C CG . MET B 2 162 ? 8.319 17.933 -7.551 1.00 14.27 ? 160 MET B CG 1 ATOM 2847 S SD . MET B 2 162 ? 8.514 19.687 -7.254 1.00 46.58 ? 160 MET B SD 1 ATOM 2848 C CE . MET B 2 162 ? 10.163 19.922 -7.915 1.00 31.78 ? 160 MET B CE 1 ATOM 2849 N N . LEU B 2 163 ? 5.940 15.075 -10.162 1.00 16.81 ? 161 LEU B N 1 ATOM 2850 C CA . LEU B 2 163 ? 5.030 14.656 -11.217 1.00 21.71 ? 161 LEU B CA 1 ATOM 2851 C C . LEU B 2 163 ? 3.724 15.418 -11.094 1.00 17.83 ? 161 LEU B C 1 ATOM 2852 O O . LEU B 2 163 ? 3.028 15.302 -10.088 1.00 19.04 ? 161 LEU B O 1 ATOM 2853 C CB . LEU B 2 163 ? 4.770 13.149 -11.168 1.00 19.55 ? 161 LEU B CB 1 ATOM 2854 C CG . LEU B 2 163 ? 3.719 12.661 -12.173 1.00 22.12 ? 161 LEU B CG 1 ATOM 2855 C CD1 . LEU B 2 163 ? 4.190 12.872 -13.606 1.00 16.81 ? 161 LEU B CD1 1 ATOM 2856 C CD2 . LEU B 2 163 ? 3.366 11.200 -11.940 1.00 22.18 ? 161 LEU B CD2 1 ATOM 2857 N N . GLU B 2 164 ? 3.390 16.188 -12.128 1.00 18.81 ? 162 GLU B N 1 ATOM 2858 C CA . GLU B 2 164 ? 2.097 16.860 -12.171 1.00 26.41 ? 162 GLU B CA 1 ATOM 2859 C C . GLU B 2 164 ? 1.050 15.854 -12.602 1.00 25.70 ? 162 GLU B C 1 ATOM 2860 O O . GLU B 2 164 ? 1.129 15.285 -13.689 1.00 29.51 ? 162 GLU B O 1 ATOM 2861 C CB . GLU B 2 164 ? 2.099 18.059 -13.123 1.00 19.88 ? 162 GLU B CB 1 ATOM 2862 C CG . GLU B 2 164 ? 3.154 19.108 -12.817 1.00 37.52 ? 162 GLU B CG 1 ATOM 2863 C CD . GLU B 2 164 ? 3.351 20.084 -13.965 1.00 48.85 ? 162 GLU B CD 1 ATOM 2864 O OE1 . GLU B 2 164 ? 4.478 20.182 -14.495 1.00 43.11 ? 162 GLU B OE1 1 ATOM 2865 O OE2 . GLU B 2 164 ? 2.371 20.766 -14.327 1.00 58.89 ? 162 GLU B OE2 1 ATOM 2866 N N . THR B 2 165 ? 0.083 15.621 -11.724 1.00 21.19 ? 163 THR B N 1 ATOM 2867 C CA . THR B 2 165 ? -0.921 14.599 -11.944 1.00 18.02 ? 163 THR B CA 1 ATOM 2868 C C . THR B 2 165 ? -2.125 14.839 -11.047 1.00 18.43 ? 163 THR B C 1 ATOM 2869 O O . THR B 2 165 ? -2.004 15.433 -9.984 1.00 18.25 ? 163 THR B O 1 ATOM 2870 C CB . THR B 2 165 ? -0.342 13.189 -11.675 1.00 20.91 ? 163 THR B CB 1 ATOM 2871 O OG1 . THR B 2 165 ? -1.305 12.192 -12.036 1.00 26.84 ? 163 THR B OG1 1 ATOM 2872 C CG2 . THR B 2 165 ? 0.013 13.023 -10.206 1.00 20.37 ? 163 THR B CG2 1 ATOM 2873 N N . VAL B 2 166 ? -3.285 14.374 -11.489 1.00 20.54 ? 164 VAL B N 1 ATOM 2874 C CA . VAL B 2 166 ? -4.484 14.378 -10.666 1.00 21.98 ? 164 VAL B CA 1 ATOM 2875 C C . VAL B 2 166 ? -4.759 12.950 -10.226 1.00 27.58 ? 164 VAL B C 1 ATOM 2876 O O . VAL B 2 166 ? -5.272 12.147 -11.007 1.00 27.00 ? 164 VAL B O 1 ATOM 2877 C CB . VAL B 2 166 ? -5.707 14.940 -11.405 1.00 19.95 ? 164 VAL B CB 1 ATOM 2878 C CG1 . VAL B 2 166 ? -6.904 14.986 -10.466 1.00 20.55 ? 164 VAL B CG1 1 ATOM 2879 C CG2 . VAL B 2 166 ? -5.402 16.324 -11.961 1.00 19.93 ? 164 VAL B CG2 1 ATOM 2880 N N . PRO B 2 167 ? -4.389 12.619 -8.981 1.00 27.20 ? 165 PRO B N 1 ATOM 2881 C CA . PRO B 2 167 ? -4.548 11.247 -8.497 1.00 31.65 ? 165 PRO B CA 1 ATOM 2882 C C . PRO B 2 167 ? -6.000 10.782 -8.491 1.00 31.75 ? 165 PRO B C 1 ATOM 2883 O O . PRO B 2 167 ? -6.891 11.505 -8.038 1.00 22.06 ? 165 PRO B O 1 ATOM 2884 C CB . PRO B 2 167 ? -4.003 11.320 -7.065 1.00 39.07 ? 165 PRO B CB 1 ATOM 2885 C CG . PRO B 2 167 ? -3.077 12.501 -7.070 1.00 33.72 ? 165 PRO B CG 1 ATOM 2886 C CD . PRO B 2 167 ? -3.745 13.487 -7.982 1.00 24.48 ? 165 PRO B CD 1 ATOM 2887 N N . ARG B 2 168 ? -6.225 9.580 -9.009 1.00 28.45 ? 166 ARG B N 1 ATOM 2888 C CA . ARG B 2 168 ? -7.543 8.965 -8.976 1.00 36.24 ? 166 ARG B CA 1 ATOM 2889 C C . ARG B 2 168 ? -7.527 7.780 -8.019 1.00 38.23 ? 166 ARG B C 1 ATOM 2890 O O . ARG B 2 168 ? -6.493 7.133 -7.847 1.00 36.26 ? 166 ARG B O 1 ATOM 2891 C CB . ARG B 2 168 ? -7.970 8.517 -10.378 1.00 37.27 ? 166 ARG B CB 1 ATOM 2892 C CG . ARG B 2 168 ? -8.445 9.641 -11.290 1.00 35.44 ? 166 ARG B CG 1 ATOM 2893 C CD . ARG B 2 168 ? -8.652 9.128 -12.707 1.00 34.45 ? 166 ARG B CD 1 ATOM 2894 N NE . ARG B 2 168 ? -9.444 10.041 -13.527 1.00 29.69 ? 166 ARG B NE 1 ATOM 2895 C CZ . ARG B 2 168 ? -8.950 11.086 -14.183 1.00 27.85 ? 166 ARG B CZ 1 ATOM 2896 N NH1 . ARG B 2 168 ? -7.655 11.363 -14.114 1.00 29.94 ? 166 ARG B NH1 1 ATOM 2897 N NH2 . ARG B 2 168 ? -9.753 11.853 -14.908 1.00 26.97 ? 166 ARG B NH2 1 ATOM 2898 N N . SER B 2 169 ? -8.662 7.518 -7.377 1.00 45.42 ? 167 SER B N 1 ATOM 2899 C CA . SER B 2 169 ? -8.766 6.408 -6.433 1.00 46.00 ? 167 SER B CA 1 ATOM 2900 C C . SER B 2 169 ? -8.342 5.096 -7.088 1.00 41.78 ? 167 SER B C 1 ATOM 2901 O O . SER B 2 169 ? -8.763 4.786 -8.199 1.00 41.67 ? 167 SER B O 1 ATOM 2902 C CB . SER B 2 169 ? -10.189 6.293 -5.880 1.00 49.93 ? 167 SER B CB 1 ATOM 2903 O OG . SER B 2 169 ? -11.132 6.126 -6.922 1.00 57.81 ? 167 SER B OG 1 ATOM 2904 N N . GLY B 2 170 ? -7.492 4.340 -6.405 1.00 43.03 ? 168 GLY B N 1 ATOM 2905 C CA . GLY B 2 170 ? -7.030 3.060 -6.912 1.00 47.57 ? 168 GLY B CA 1 ATOM 2906 C C . GLY B 2 170 ? -5.654 3.117 -7.542 1.00 46.36 ? 168 GLY B C 1 ATOM 2907 O O . GLY B 2 170 ? -4.919 2.129 -7.513 1.00 45.55 ? 168 GLY B O 1 ATOM 2908 N N . GLU B 2 171 ? -5.314 4.262 -8.129 1.00 42.93 ? 169 GLU B N 1 ATOM 2909 C CA . GLU B 2 171 ? -4.022 4.428 -8.786 1.00 40.12 ? 169 GLU B CA 1 ATOM 2910 C C . GLU B 2 171 ? -2.879 4.211 -7.810 1.00 37.36 ? 169 GLU B C 1 ATOM 2911 O O . GLU B 2 171 ? -2.938 4.639 -6.654 1.00 35.98 ? 169 GLU B O 1 ATOM 2912 C CB . GLU B 2 171 ? -3.895 5.801 -9.444 1.00 33.94 ? 169 GLU B CB 1 ATOM 2913 C CG . GLU B 2 171 ? -4.683 5.944 -10.730 1.00 35.79 ? 169 GLU B CG 1 ATOM 2914 C CD . GLU B 2 171 ? -4.536 7.318 -11.348 1.00 39.89 ? 169 GLU B CD 1 ATOM 2915 O OE1 . GLU B 2 171 ? -4.149 8.260 -10.621 1.00 47.02 ? 169 GLU B OE1 1 ATOM 2916 O OE2 . GLU B 2 171 ? -4.804 7.453 -12.559 1.00 43.18 ? 169 GLU B OE2 1 ATOM 2917 N N . VAL B 2 172 ? -1.836 3.545 -8.282 1.00 36.36 ? 170 VAL B N 1 ATOM 2918 C CA . VAL B 2 172 ? -0.614 3.439 -7.506 1.00 42.17 ? 170 VAL B CA 1 ATOM 2919 C C . VAL B 2 172 ? 0.520 4.089 -8.285 1.00 38.07 ? 170 VAL B C 1 ATOM 2920 O O . VAL B 2 172 ? 0.816 3.710 -9.420 1.00 37.51 ? 170 VAL B O 1 ATOM 2921 C CB . VAL B 2 172 ? -0.260 1.977 -7.187 1.00 41.84 ? 170 VAL B CB 1 ATOM 2922 C CG1 . VAL B 2 172 ? 1.101 1.900 -6.513 1.00 37.38 ? 170 VAL B CG1 1 ATOM 2923 C CG2 . VAL B 2 172 ? -1.325 1.368 -6.291 1.00 44.35 ? 170 VAL B CG2 1 ATOM 2924 N N . TYR B 2 173 ? 1.154 5.074 -7.663 1.00 21.43 ? 171 TYR B N 1 ATOM 2925 C CA . TYR B 2 173 ? 2.281 5.740 -8.283 1.00 25.43 ? 171 TYR B CA 1 ATOM 2926 C C . TYR B 2 173 ? 3.581 5.209 -7.720 1.00 33.16 ? 171 TYR B C 1 ATOM 2927 O O . TYR B 2 173 ? 3.665 4.853 -6.547 1.00 36.90 ? 171 TYR B O 1 ATOM 2928 C CB . TYR B 2 173 ? 2.203 7.248 -8.076 1.00 19.80 ? 171 TYR B CB 1 ATOM 2929 C CG . TYR B 2 173 ? 1.078 7.910 -8.826 1.00 26.25 ? 171 TYR B CG 1 ATOM 2930 C CD1 . TYR B 2 173 ? -0.222 7.872 -8.345 1.00 27.16 ? 171 TYR B CD1 1 ATOM 2931 C CD2 . TYR B 2 173 ? 1.321 8.591 -10.012 1.00 19.43 ? 171 TYR B CD2 1 ATOM 2932 C CE1 . TYR B 2 173 ? -1.257 8.489 -9.030 1.00 28.30 ? 171 TYR B CE1 1 ATOM 2933 C CE2 . TYR B 2 173 ? 0.297 9.211 -10.701 1.00 20.87 ? 171 TYR B CE2 1 ATOM 2934 C CZ . TYR B 2 173 ? -0.990 9.157 -10.207 1.00 26.45 ? 171 TYR B CZ 1 ATOM 2935 O OH . TYR B 2 173 ? -2.012 9.774 -10.892 1.00 28.88 ? 171 TYR B OH 1 ATOM 2936 N N . THR B 2 174 ? 4.598 5.155 -8.569 1.00 23.16 ? 172 THR B N 1 ATOM 2937 C CA . THR B 2 174 ? 5.882 4.651 -8.138 1.00 22.38 ? 172 THR B CA 1 ATOM 2938 C C . THR B 2 174 ? 7.008 5.573 -8.566 1.00 18.79 ? 172 THR B C 1 ATOM 2939 O O . THR B 2 174 ? 7.107 5.958 -9.730 1.00 22.95 ? 172 THR B O 1 ATOM 2940 C CB . THR B 2 174 ? 6.141 3.233 -8.691 1.00 27.21 ? 172 THR B CB 1 ATOM 2941 O OG1 . THR B 2 174 ? 5.109 2.346 -8.239 1.00 30.72 ? 172 THR B OG1 1 ATOM 2942 C CG2 . THR B 2 174 ? 7.485 2.707 -8.218 1.00 25.69 ? 172 THR B CG2 1 ATOM 2943 N N . CYS B 2 175 ? 7.850 5.925 -7.607 1.00 18.34 ? 173 CYS B N 1 ATOM 2944 C CA . CYS B 2 175 ? 9.075 6.627 -7.912 1.00 25.94 ? 173 CYS B CA 1 ATOM 2945 C C . CYS B 2 175 ? 10.210 5.619 -7.935 1.00 26.18 ? 173 CYS B C 1 ATOM 2946 O O . CYS B 2 175 ? 10.384 4.850 -6.993 1.00 24.66 ? 173 CYS B O 1 ATOM 2947 C CB . CYS B 2 175 ? 9.353 7.720 -6.888 1.00 20.38 ? 173 CYS B CB 1 ATOM 2948 S SG . CYS B 2 175 ? 10.864 8.605 -7.244 1.00 21.34 ? 173 CYS B SG 1 ATOM 2949 N N . GLN B 2 176 ? 10.978 5.623 -9.018 1.00 25.15 ? 174 GLN B N 1 ATOM 2950 C CA . GLN B 2 176 ? 12.052 4.654 -9.179 1.00 22.35 ? 174 GLN B CA 1 ATOM 2951 C C . GLN B 2 176 ? 13.405 5.340 -9.266 1.00 23.36 ? 174 GLN B C 1 ATOM 2952 O O . GLN B 2 176 ? 13.581 6.287 -10.033 1.00 19.85 ? 174 GLN B O 1 ATOM 2953 C CB . GLN B 2 176 ? 11.820 3.811 -10.427 1.00 22.15 ? 174 GLN B CB 1 ATOM 2954 C CG . GLN B 2 176 ? 12.886 2.764 -10.655 1.00 30.38 ? 174 GLN B CG 1 ATOM 2955 C CD . GLN B 2 176 ? 12.826 2.179 -12.044 1.00 33.22 ? 174 GLN B CD 1 ATOM 2956 O OE1 . GLN B 2 176 ? 13.349 2.760 -12.996 1.00 44.23 ? 174 GLN B OE1 1 ATOM 2957 N NE2 . GLN B 2 176 ? 12.173 1.034 -12.176 1.00 24.92 ? 174 GLN B NE2 1 ATOM 2958 N N . VAL B 2 177 ? 14.366 4.853 -8.491 1.00 16.91 ? 175 VAL B N 1 ATOM 2959 C CA . VAL B 2 177 ? 15.657 5.513 -8.408 1.00 18.82 ? 175 VAL B CA 1 ATOM 2960 C C . VAL B 2 177 ? 16.772 4.539 -8.757 1.00 22.65 ? 175 VAL B C 1 ATOM 2961 O O . VAL B 2 177 ? 16.858 3.445 -8.191 1.00 21.96 ? 175 VAL B O 1 ATOM 2962 C CB . VAL B 2 177 ? 15.910 6.100 -7.005 1.00 23.23 ? 175 VAL B CB 1 ATOM 2963 C CG1 . VAL B 2 177 ? 17.317 6.673 -6.918 1.00 15.34 ? 175 VAL B CG1 1 ATOM 2964 C CG2 . VAL B 2 177 ? 14.874 7.172 -6.678 1.00 15.70 ? 175 VAL B CG2 1 ATOM 2965 N N . GLU B 2 178 ? 17.623 4.943 -9.695 1.00 17.06 ? 176 GLU B N 1 ATOM 2966 C CA . GLU B 2 178 ? 18.804 4.169 -10.053 1.00 16.35 ? 176 GLU B CA 1 ATOM 2967 C C . GLU B 2 178 ? 20.047 4.985 -9.718 1.00 24.33 ? 176 GLU B C 1 ATOM 2968 O O . GLU B 2 178 ? 20.078 6.198 -9.938 1.00 29.62 ? 176 GLU B O 1 ATOM 2969 C CB . GLU B 2 178 ? 18.785 3.797 -11.536 1.00 24.26 ? 176 GLU B CB 1 ATOM 2970 C CG . GLU B 2 178 ? 17.735 2.762 -11.911 1.00 36.89 ? 176 GLU B CG 1 ATOM 2971 C CD . GLU B 2 178 ? 17.441 2.747 -13.400 1.00 49.14 ? 176 GLU B CD 1 ATOM 2972 O OE1 . GLU B 2 178 ? 17.587 1.675 -14.022 1.00 52.48 ? 176 GLU B OE1 1 ATOM 2973 O OE2 . GLU B 2 178 ? 17.061 3.806 -13.948 1.00 49.81 ? 176 GLU B OE2 1 ATOM 2974 N N . HIS B 2 179 ? 21.063 4.319 -9.187 1.00 19.57 ? 177 HIS B N 1 ATOM 2975 C CA . HIS B 2 179 ? 22.224 5.005 -8.643 1.00 21.79 ? 177 HIS B CA 1 ATOM 2976 C C . HIS B 2 179 ? 23.357 3.992 -8.502 1.00 24.37 ? 177 HIS B C 1 ATOM 2977 O O . HIS B 2 179 ? 23.088 2.814 -8.276 1.00 25.56 ? 177 HIS B O 1 ATOM 2978 C CB . HIS B 2 179 ? 21.855 5.656 -7.300 1.00 23.18 ? 177 HIS B CB 1 ATOM 2979 C CG . HIS B 2 179 ? 22.936 6.505 -6.707 1.00 19.31 ? 177 HIS B CG 1 ATOM 2980 N ND1 . HIS B 2 179 ? 23.775 6.056 -5.710 1.00 21.57 ? 177 HIS B ND1 1 ATOM 2981 C CD2 . HIS B 2 179 ? 23.320 7.775 -6.978 1.00 13.87 ? 177 HIS B CD2 1 ATOM 2982 C CE1 . HIS B 2 179 ? 24.623 7.016 -5.386 1.00 21.52 ? 177 HIS B CE1 1 ATOM 2983 N NE2 . HIS B 2 179 ? 24.371 8.067 -6.144 1.00 18.22 ? 177 HIS B NE2 1 ATOM 2984 N N . PRO B 2 180 ? 24.620 4.439 -8.647 1.00 25.44 ? 178 PRO B N 1 ATOM 2985 C CA . PRO B 2 180 ? 25.763 3.519 -8.564 1.00 19.31 ? 178 PRO B CA 1 ATOM 2986 C C . PRO B 2 180 ? 25.835 2.762 -7.242 1.00 22.28 ? 178 PRO B C 1 ATOM 2987 O O . PRO B 2 180 ? 26.441 1.694 -7.196 1.00 23.45 ? 178 PRO B O 1 ATOM 2988 C CB . PRO B 2 180 ? 26.969 4.447 -8.729 1.00 20.89 ? 178 PRO B CB 1 ATOM 2989 C CG . PRO B 2 180 ? 26.449 5.585 -9.532 1.00 25.53 ? 178 PRO B CG 1 ATOM 2990 C CD . PRO B 2 180 ? 25.036 5.789 -9.072 1.00 26.20 ? 178 PRO B CD 1 ATOM 2991 N N . SER B 2 181 ? 25.236 3.310 -6.189 1.00 25.63 ? 179 SER B N 1 ATOM 2992 C CA . SER B 2 181 ? 25.267 2.674 -4.876 1.00 23.95 ? 179 SER B CA 1 ATOM 2993 C C . SER B 2 181 ? 24.268 1.522 -4.789 1.00 22.35 ? 179 SER B C 1 ATOM 2994 O O . SER B 2 181 ? 24.301 0.733 -3.845 1.00 19.41 ? 179 SER B O 1 ATOM 2995 C CB . SER B 2 181 ? 24.975 3.699 -3.784 1.00 22.80 ? 179 SER B CB 1 ATOM 2996 O OG . SER B 2 181 ? 23.633 4.140 -3.885 1.00 24.94 ? 179 SER B OG 1 ATOM 2997 N N . LEU B 2 182 ? 23.371 1.439 -5.768 1.00 22.88 ? 180 LEU B N 1 ATOM 2998 C CA . LEU B 2 182 ? 22.318 0.428 -5.760 1.00 24.89 ? 180 LEU B CA 1 ATOM 2999 C C . LEU B 2 182 ? 22.626 -0.695 -6.751 1.00 20.43 ? 180 LEU B C 1 ATOM 3000 O O . LEU B 2 182 ? 23.223 -0.458 -7.798 1.00 23.89 ? 180 LEU B O 1 ATOM 3001 C CB . LEU B 2 182 ? 20.963 1.064 -6.089 1.00 18.87 ? 180 LEU B CB 1 ATOM 3002 C CG . LEU B 2 182 ? 20.497 2.231 -5.214 1.00 18.81 ? 180 LEU B CG 1 ATOM 3003 C CD1 . LEU B 2 182 ? 19.234 2.850 -5.796 1.00 16.79 ? 180 LEU B CD1 1 ATOM 3004 C CD2 . LEU B 2 182 ? 20.265 1.790 -3.770 1.00 17.21 ? 180 LEU B CD2 1 ATOM 3005 N N . THR B 2 183 ? 22.198 -1.911 -6.425 1.00 21.50 ? 181 THR B N 1 ATOM 3006 C CA . THR B 2 183 ? 22.422 -3.064 -7.295 1.00 20.61 ? 181 THR B CA 1 ATOM 3007 C C . THR B 2 183 ? 21.158 -3.388 -8.079 1.00 20.31 ? 181 THR B C 1 ATOM 3008 O O . THR B 2 183 ? 21.178 -4.187 -9.013 1.00 29.98 ? 181 THR B O 1 ATOM 3009 C CB . THR B 2 183 ? 22.871 -4.305 -6.507 1.00 27.84 ? 181 THR B CB 1 ATOM 3010 O OG1 . THR B 2 183 ? 21.988 -4.524 -5.401 1.00 25.00 ? 181 THR B OG1 1 ATOM 3011 C CG2 . THR B 2 183 ? 24.296 -4.118 -5.991 1.00 32.48 ? 181 THR B CG2 1 ATOM 3012 N N . SER B 2 184 ? 20.064 -2.743 -7.693 1.00 23.65 ? 182 SER B N 1 ATOM 3013 C CA . SER B 2 184 ? 18.796 -2.855 -8.402 1.00 27.35 ? 182 SER B CA 1 ATOM 3014 C C . SER B 2 184 ? 17.990 -1.593 -8.114 1.00 28.68 ? 182 SER B C 1 ATOM 3015 O O . SER B 2 184 ? 18.268 -0.906 -7.132 1.00 23.57 ? 182 SER B O 1 ATOM 3016 C CB . SER B 2 184 ? 18.034 -4.111 -7.965 1.00 23.14 ? 182 SER B CB 1 ATOM 3017 O OG . SER B 2 184 ? 17.599 -3.994 -6.624 1.00 32.68 ? 182 SER B OG 1 ATOM 3018 N N . PRO B 2 185 ? 17.003 -1.271 -8.972 1.00 28.22 ? 183 PRO B N 1 ATOM 3019 C CA . PRO B 2 185 ? 16.270 -0.019 -8.748 1.00 29.26 ? 183 PRO B CA 1 ATOM 3020 C C . PRO B 2 185 ? 15.575 0.044 -7.393 1.00 29.61 ? 183 PRO B C 1 ATOM 3021 O O . PRO B 2 185 ? 15.022 -0.948 -6.918 1.00 36.52 ? 183 PRO B O 1 ATOM 3022 C CB . PRO B 2 185 ? 15.240 -0.010 -9.885 1.00 29.49 ? 183 PRO B CB 1 ATOM 3023 C CG . PRO B 2 185 ? 15.860 -0.843 -10.960 1.00 32.62 ? 183 PRO B CG 1 ATOM 3024 C CD . PRO B 2 185 ? 16.612 -1.925 -10.233 1.00 32.19 ? 183 PRO B CD 1 ATOM 3025 N N . LEU B 2 186 ? 15.621 1.219 -6.780 1.00 25.95 ? 184 LEU B N 1 ATOM 3026 C CA . LEU B 2 186 ? 14.919 1.468 -5.535 1.00 25.97 ? 184 LEU B CA 1 ATOM 3027 C C . LEU B 2 186 ? 13.573 2.096 -5.882 1.00 35.73 ? 184 LEU B C 1 ATOM 3028 O O . LEU B 2 186 ? 13.521 3.112 -6.576 1.00 31.69 ? 184 LEU B O 1 ATOM 3029 C CB . LEU B 2 186 ? 15.768 2.362 -4.620 1.00 26.68 ? 184 LEU B CB 1 ATOM 3030 C CG . LEU B 2 186 ? 15.334 2.802 -3.218 1.00 33.95 ? 184 LEU B CG 1 ATOM 3031 C CD1 . LEU B 2 186 ? 16.512 3.479 -2.522 1.00 34.86 ? 184 LEU B CD1 1 ATOM 3032 C CD2 . LEU B 2 186 ? 14.109 3.706 -3.200 1.00 37.55 ? 184 LEU B CD2 1 ATOM 3033 N N . THR B 2 187 ? 12.490 1.491 -5.409 1.00 25.12 ? 185 THR B N 1 ATOM 3034 C CA . THR B 2 187 ? 11.155 1.987 -5.713 1.00 27.15 ? 185 THR B CA 1 ATOM 3035 C C . THR B 2 187 ? 10.382 2.339 -4.447 1.00 27.72 ? 185 THR B C 1 ATOM 3036 O O . THR B 2 187 ? 10.496 1.663 -3.423 1.00 23.64 ? 185 THR B O 1 ATOM 3037 C CB . THR B 2 187 ? 10.344 0.962 -6.530 1.00 31.96 ? 185 THR B CB 1 ATOM 3038 O OG1 . THR B 2 187 ? 10.250 -0.265 -5.796 1.00 37.43 ? 185 THR B OG1 1 ATOM 3039 C CG2 . THR B 2 187 ? 11.009 0.695 -7.879 1.00 22.38 ? 185 THR B CG2 1 ATOM 3040 N N . VAL B 2 188 ? 9.613 3.420 -4.523 1.00 29.56 ? 186 VAL B N 1 ATOM 3041 C CA . VAL B 2 188 ? 8.722 3.817 -3.444 1.00 23.19 ? 186 VAL B CA 1 ATOM 3042 C C . VAL B 2 188 ? 7.335 4.054 -4.019 1.00 30.17 ? 186 VAL B C 1 ATOM 3043 O O . VAL B 2 188 ? 7.177 4.799 -4.988 1.00 30.65 ? 186 VAL B O 1 ATOM 3044 C CB . VAL B 2 188 ? 9.202 5.086 -2.713 1.00 22.27 ? 186 VAL B CB 1 ATOM 3045 C CG1 . VAL B 2 188 ? 8.135 5.571 -1.740 1.00 22.34 ? 186 VAL B CG1 1 ATOM 3046 C CG2 . VAL B 2 188 ? 10.506 4.820 -1.980 1.00 19.51 ? 186 VAL B CG2 1 ATOM 3047 N N . GLU B 2 189 ? 6.332 3.413 -3.428 1.00 28.57 ? 187 GLU B N 1 ATOM 3048 C CA . GLU B 2 189 ? 4.968 3.555 -3.910 1.00 25.93 ? 187 GLU B CA 1 ATOM 3049 C C . GLU B 2 189 ? 4.214 4.621 -3.136 1.00 29.78 ? 187 GLU B C 1 ATOM 3050 O O . GLU B 2 189 ? 4.502 4.895 -1.968 1.00 31.00 ? 187 GLU B O 1 ATOM 3051 C CB . GLU B 2 189 ? 4.213 2.231 -3.827 1.00 28.72 ? 187 GLU B CB 1 ATOM 3052 C CG . GLU B 2 189 ? 4.726 1.162 -4.767 1.00 27.55 ? 187 GLU B CG 1 ATOM 3053 C CD . GLU B 2 189 ? 3.931 -0.119 -4.658 1.00 38.74 ? 187 GLU B CD 1 ATOM 3054 O OE1 . GLU B 2 189 ? 4.138 -1.022 -5.495 1.00 45.55 ? 187 GLU B OE1 1 ATOM 3055 O OE2 . GLU B 2 189 ? 3.094 -0.219 -3.737 1.00 46.35 ? 187 GLU B OE2 1 ATOM 3056 N N . TRP B 2 190 ? 3.243 5.223 -3.811 1.00 29.22 ? 188 TRP B N 1 ATOM 3057 C CA . TRP B 2 190 ? 2.313 6.142 -3.182 1.00 22.48 ? 188 TRP B CA 1 ATOM 3058 C C . TRP B 2 190 ? 0.917 5.829 -3.700 1.00 25.39 ? 188 TRP B C 1 ATOM 3059 O O . TRP B 2 190 ? 0.711 5.713 -4.905 1.00 31.06 ? 188 TRP B O 1 ATOM 3060 C CB . TRP B 2 190 ? 2.675 7.595 -3.480 1.00 31.53 ? 188 TRP B CB 1 ATOM 3061 C CG . TRP B 2 190 ? 1.746 8.571 -2.831 1.00 33.21 ? 188 TRP B CG 1 ATOM 3062 C CD1 . TRP B 2 190 ? 1.873 9.113 -1.586 1.00 32.49 ? 188 TRP B CD1 1 ATOM 3063 C CD2 . TRP B 2 190 ? 0.514 9.074 -3.364 1.00 26.87 ? 188 TRP B CD2 1 ATOM 3064 N NE1 . TRP B 2 190 ? 0.818 9.952 -1.326 1.00 34.73 ? 188 TRP B NE1 1 ATOM 3065 C CE2 . TRP B 2 190 ? -0.034 9.941 -2.399 1.00 36.48 ? 188 TRP B CE2 1 ATOM 3066 C CE3 . TRP B 2 190 ? -0.170 8.885 -4.568 1.00 27.07 ? 188 TRP B CE3 1 ATOM 3067 C CZ2 . TRP B 2 190 ? -1.235 10.620 -2.600 1.00 37.69 ? 188 TRP B CZ2 1 ATOM 3068 C CZ3 . TRP B 2 190 ? -1.364 9.560 -4.766 1.00 34.04 ? 188 TRP B CZ3 1 ATOM 3069 C CH2 . TRP B 2 190 ? -1.883 10.417 -3.787 1.00 34.80 ? 188 TRP B CH2 1 ATOM 3070 N N . ARG B 2 191 ? -0.030 5.682 -2.783 1.00 32.62 ? 189 ARG B N 1 ATOM 3071 C CA . ARG B 2 191 ? -1.406 5.376 -3.139 1.00 38.86 ? 189 ARG B CA 1 ATOM 3072 C C . ARG B 2 191 ? -2.311 6.546 -2.772 1.00 37.09 ? 189 ARG B C 1 ATOM 3073 O O . ARG B 2 191 ? -2.134 7.172 -1.730 1.00 36.14 ? 189 ARG B O 1 ATOM 3074 C CB . ARG B 2 191 ? -1.864 4.100 -2.432 1.00 47.70 ? 189 ARG B CB 1 ATOM 3075 C CG . ARG B 2 191 ? -2.531 3.077 -3.333 1.00 61.49 ? 189 ARG B CG 1 ATOM 3076 C CD . ARG B 2 191 ? -2.903 1.823 -2.553 1.00 73.01 ? 189 ARG B CD 1 ATOM 3077 N NE . ARG B 2 191 ? -1.771 1.307 -1.787 1.00 79.10 ? 189 ARG B NE 1 ATOM 3078 C CZ . ARG B 2 191 ? -0.914 0.394 -2.234 1.00 82.53 ? 189 ARG B CZ 1 ATOM 3079 N NH1 . ARG B 2 191 ? -1.056 -0.115 -3.449 1.00 84.61 ? 189 ARG B NH1 1 ATOM 3080 N NH2 . ARG B 2 191 ? 0.085 -0.013 -1.466 1.00 83.75 ? 189 ARG B NH2 1 ATOM 3081 N N . ALA B 2 192 ? -3.268 6.847 -3.647 1.00 38.96 ? 190 ALA B N 1 ATOM 3082 C CA . ALA B 2 192 ? -4.336 7.793 -3.319 1.00 37.99 ? 190 ALA B CA 1 ATOM 3083 C C . ALA B 2 192 ? -5.483 7.154 -2.541 1.00 32.19 ? 190 ALA B C 1 ATOM 3084 O O . ALA B 2 192 ? -5.661 5.939 -2.555 1.00 38.55 ? 190 ALA B O 1 ATOM 3085 C CB . ALA B 2 192 ? -4.859 8.435 -4.591 1.00 34.66 ? 190 ALA B CB 1 ATOM 3086 N N . GLY C 3 1 ? 48.300 7.528 3.332 1.00 36.86 ? 1 GLY C N 1 ATOM 3087 C CA . GLY C 3 1 ? 49.206 8.259 2.467 1.00 25.18 ? 1 GLY C CA 1 ATOM 3088 C C . GLY C 3 1 ? 49.182 9.753 2.730 1.00 30.25 ? 1 GLY C C 1 ATOM 3089 O O . GLY C 3 1 ? 48.322 10.251 3.457 1.00 29.21 ? 1 GLY C O 1 ATOM 3090 N N . VAL C 3 2 ? 50.126 10.470 2.128 1.00 27.36 ? 2 VAL C N 1 ATOM 3091 C CA . VAL C 3 2 ? 50.258 11.906 2.344 1.00 28.50 ? 2 VAL C CA 1 ATOM 3092 C C . VAL C 3 2 ? 49.968 12.690 1.067 1.00 26.41 ? 2 VAL C C 1 ATOM 3093 O O . VAL C 3 2 ? 50.609 12.467 0.040 1.00 25.08 ? 2 VAL C O 1 ATOM 3094 C CB . VAL C 3 2 ? 51.669 12.264 2.844 1.00 25.78 ? 2 VAL C CB 1 ATOM 3095 C CG1 . VAL C 3 2 ? 51.729 13.720 3.283 1.00 26.18 ? 2 VAL C CG1 1 ATOM 3096 C CG2 . VAL C 3 2 ? 52.081 11.342 3.982 1.00 25.27 ? 2 VAL C CG2 1 ATOM 3097 N N . TYR C 3 3 ? 49.004 13.605 1.135 1.00 19.81 ? 3 TYR C N 1 ATOM 3098 C CA . TYR C 3 3 ? 48.692 14.469 0.001 1.00 18.57 ? 3 TYR C CA 1 ATOM 3099 C C . TYR C 3 3 ? 49.874 15.363 -0.332 1.00 17.77 ? 3 TYR C C 1 ATOM 3100 O O . TYR C 3 3 ? 50.477 15.957 0.558 1.00 21.52 ? 3 TYR C O 1 ATOM 3101 C CB . TYR C 3 3 ? 47.465 15.330 0.290 1.00 19.07 ? 3 TYR C CB 1 ATOM 3102 C CG . TYR C 3 3 ? 46.151 14.680 -0.069 1.00 21.62 ? 3 TYR C CG 1 ATOM 3103 C CD1 . TYR C 3 3 ? 45.747 14.576 -1.393 1.00 27.11 ? 3 TYR C CD1 1 ATOM 3104 C CD2 . TYR C 3 3 ? 45.307 14.187 0.916 1.00 21.62 ? 3 TYR C CD2 1 ATOM 3105 C CE1 . TYR C 3 3 ? 44.542 13.989 -1.727 1.00 26.70 ? 3 TYR C CE1 1 ATOM 3106 C CE2 . TYR C 3 3 ? 44.104 13.601 0.593 1.00 25.33 ? 3 TYR C CE2 1 ATOM 3107 C CZ . TYR C 3 3 ? 43.724 13.504 -0.729 1.00 26.49 ? 3 TYR C CZ 1 ATOM 3108 O OH . TYR C 3 3 ? 42.520 12.917 -1.050 1.00 33.40 ? 3 TYR C OH 1 ATOM 3109 N N . ALA C 3 4 ? 50.202 15.451 -1.616 1.00 16.82 ? 4 ALA C N 1 ATOM 3110 C CA . ALA C 3 4 ? 51.305 16.289 -2.066 1.00 14.70 ? 4 ALA C CA 1 ATOM 3111 C C . ALA C 3 4 ? 50.791 17.611 -2.610 1.00 19.39 ? 4 ALA C C 1 ATOM 3112 O O . ALA C 3 4 ? 49.740 17.658 -3.251 1.00 22.26 ? 4 ALA C O 1 ATOM 3113 C CB . ALA C 3 4 ? 52.133 15.566 -3.115 1.00 17.86 ? 4 ALA C CB 1 ATOM 3114 N N . THR C 3 5 ? 51.542 18.676 -2.345 1.00 20.71 ? 5 THR C N 1 ATOM 3115 C CA . THR C 3 5 ? 51.242 20.009 -2.851 1.00 20.33 ? 5 THR C CA 1 ATOM 3116 C C . THR C 3 5 ? 51.929 20.257 -4.182 1.00 20.45 ? 5 THR C C 1 ATOM 3117 O O . THR C 3 5 ? 53.126 20.009 -4.292 1.00 19.93 ? 5 THR C O 1 ATOM 3118 C CB . THR C 3 5 ? 51.708 21.094 -1.862 1.00 21.44 ? 5 THR C CB 1 ATOM 3119 O OG1 . THR C 3 5 ? 50.915 21.033 -0.674 1.00 31.28 ? 5 THR C OG1 1 ATOM 3120 C CG2 . THR C 3 5 ? 51.571 22.482 -2.465 1.00 30.16 ? 5 THR C CG2 1 HETATM 3121 C C1 . CIR C 3 6 ? 52.443 22.352 -6.197 1.00 21.08 ? 6 CIR C C1 1 HETATM 3122 O O1 . CIR C 3 6 ? 51.775 23.217 -5.571 1.00 19.95 ? 6 CIR C O1 1 HETATM 3123 C C2 . CIR C 3 6 ? 51.790 21.047 -6.447 1.00 13.30 ? 6 CIR C C2 1 HETATM 3124 N N2 . CIR C 3 6 ? 51.205 20.743 -5.168 1.00 21.83 ? 6 CIR C N2 1 HETATM 3125 C C3 . CIR C 3 6 ? 50.800 21.171 -7.562 1.00 13.40 ? 6 CIR C C3 1 HETATM 3126 C C4 . CIR C 3 6 ? 51.538 21.582 -8.825 1.00 18.60 ? 6 CIR C C4 1 HETATM 3127 C C5 . CIR C 3 6 ? 52.161 20.374 -9.493 1.00 25.93 ? 6 CIR C C5 1 HETATM 3128 N N6 . CIR C 3 6 ? 53.332 19.938 -8.748 1.00 21.97 ? 6 CIR C N6 1 HETATM 3129 C C7 . CIR C 3 6 ? 54.539 20.722 -8.795 1.00 32.58 ? 6 CIR C C7 1 HETATM 3130 O O7 . CIR C 3 6 ? 54.578 21.741 -9.465 1.00 31.07 ? 6 CIR C O7 1 HETATM 3131 N N8 . CIR C 3 6 ? 55.705 20.305 -8.055 1.00 28.63 ? 6 CIR C N8 1 ATOM 3132 N N . SER C 3 7 ? 53.612 23.002 -6.384 1.00 20.52 ? 7 SER C N 1 ATOM 3133 C CA . SER C 3 7 ? 53.825 24.363 -5.899 1.00 19.30 ? 7 SER C CA 1 ATOM 3134 C C . SER C 3 7 ? 53.374 25.410 -6.903 1.00 13.89 ? 7 SER C C 1 ATOM 3135 O O . SER C 3 7 ? 53.098 25.095 -8.064 1.00 14.44 ? 7 SER C O 1 ATOM 3136 C CB . SER C 3 7 ? 55.299 24.571 -5.548 1.00 33.35 ? 7 SER C CB 1 ATOM 3137 O OG . SER C 3 7 ? 56.140 24.104 -6.586 1.00 37.50 ? 7 SER C OG 1 ATOM 3138 N N . SER C 3 8 ? 53.282 26.654 -6.446 1.00 13.37 ? 8 SER C N 1 ATOM 3139 C CA . SER C 3 8 ? 52.921 27.764 -7.315 1.00 16.28 ? 8 SER C CA 1 ATOM 3140 C C . SER C 3 8 ? 54.174 28.467 -7.803 1.00 17.94 ? 8 SER C C 1 ATOM 3141 O O . SER C 3 8 ? 55.052 28.808 -7.013 1.00 21.00 ? 8 SER C O 1 ATOM 3142 C CB . SER C 3 8 ? 52.001 28.746 -6.585 1.00 18.63 ? 8 SER C CB 1 ATOM 3143 O OG . SER C 3 8 ? 50.767 28.129 -6.249 1.00 21.04 ? 8 SER C OG 1 ATOM 3144 N N . ALA C 3 9 ? 54.253 28.679 -9.113 1.00 19.58 ? 9 ALA C N 1 ATOM 3145 C CA . ALA C 3 9 ? 55.450 29.248 -9.721 1.00 16.30 ? 9 ALA C CA 1 ATOM 3146 C C . ALA C 3 9 ? 55.610 30.731 -9.397 1.00 15.68 ? 9 ALA C C 1 ATOM 3147 O O . ALA C 3 9 ? 54.630 31.480 -9.328 1.00 14.38 ? 9 ALA C O 1 ATOM 3148 C CB . ALA C 3 9 ? 55.430 29.036 -11.225 1.00 14.46 ? 9 ALA C CB 1 ATOM 3149 N N . VAL C 3 10 ? 56.859 31.148 -9.207 1.00 16.74 ? 10 VAL C N 1 ATOM 3150 C CA . VAL C 3 10 ? 57.175 32.518 -8.819 1.00 15.71 ? 10 VAL C CA 1 ATOM 3151 C C . VAL C 3 10 ? 57.299 33.423 -10.047 1.00 25.20 ? 10 VAL C C 1 ATOM 3152 O O . VAL C 3 10 ? 58.063 33.149 -10.969 1.00 16.29 ? 10 VAL C O 1 ATOM 3153 C CB . VAL C 3 10 ? 58.482 32.569 -7.993 1.00 29.21 ? 10 VAL C CB 1 ATOM 3154 C CG1 . VAL C 3 10 ? 58.791 34.002 -7.555 1.00 26.04 ? 10 VAL C CG1 1 ATOM 3155 C CG2 . VAL C 3 10 ? 58.383 31.645 -6.794 1.00 28.02 ? 10 VAL C CG2 1 HETATM 3156 C C1 . CIR C 3 11 ? 57.705 36.274 -11.046 1.00 25.08 ? 11 CIR C C1 1 HETATM 3157 O O1 . CIR C 3 11 ? 58.332 36.428 -9.968 1.00 28.48 ? 11 CIR C O1 1 HETATM 3158 C C2 A CIR C 3 11 ? 56.474 35.457 -11.036 0.38 24.79 ? 11 CIR C C2 1 HETATM 3159 C C2 B CIR C 3 11 ? 56.463 35.448 -11.072 0.62 23.98 ? 11 CIR C C2 1 HETATM 3160 N N2 . CIR C 3 11 ? 56.513 34.478 -9.994 1.00 15.95 ? 11 CIR C N2 1 HETATM 3161 C C3 A CIR C 3 11 ? 55.345 36.378 -10.710 0.38 27.90 ? 11 CIR C C3 1 HETATM 3162 C C3 B CIR C 3 11 ? 55.269 36.334 -10.847 0.62 27.88 ? 11 CIR C C3 1 HETATM 3163 C C4 A CIR C 3 11 ? 55.148 37.393 -11.807 0.38 31.77 ? 11 CIR C C4 1 HETATM 3164 C C4 B CIR C 3 11 ? 54.336 36.401 -12.039 0.62 29.90 ? 11 CIR C C4 1 HETATM 3165 C C5 A CIR C 3 11 ? 53.658 37.447 -12.012 0.38 31.55 ? 11 CIR C C5 1 HETATM 3166 C C5 B CIR C 3 11 ? 53.302 35.302 -12.022 0.62 31.18 ? 11 CIR C C5 1 HETATM 3167 N N6 A CIR C 3 11 ? 53.286 36.131 -12.484 0.38 31.51 ? 11 CIR C N6 1 HETATM 3168 N N6 B CIR C 3 11 ? 51.951 35.849 -11.915 0.62 34.14 ? 11 CIR C N6 1 HETATM 3169 C C7 A CIR C 3 11 ? 52.053 35.499 -12.126 0.38 34.39 ? 11 CIR C C7 1 HETATM 3170 C C7 B CIR C 3 11 ? 50.812 35.059 -12.344 0.62 36.30 ? 11 CIR C C7 1 HETATM 3171 O O7 A CIR C 3 11 ? 51.256 36.052 -11.386 0.38 36.12 ? 11 CIR C O7 1 HETATM 3172 O O7 B CIR C 3 11 ? 49.668 35.498 -12.260 0.62 32.01 ? 11 CIR C O7 1 HETATM 3173 N N8 A CIR C 3 11 ? 51.774 34.190 -12.658 0.38 38.12 ? 11 CIR C N8 1 HETATM 3174 N N8 B CIR C 3 11 ? 51.008 33.727 -12.856 0.62 40.97 ? 11 CIR C N8 1 ATOM 3175 N N . LEU C 3 12 ? 58.244 36.893 -12.118 1.00 34.77 ? 12 LEU C N 1 ATOM 3176 C CA . LEU C 3 12 ? 59.468 37.692 -12.023 1.00 43.75 ? 12 LEU C CA 1 ATOM 3177 C C . LEU C 3 12 ? 59.135 39.163 -11.795 1.00 45.31 ? 12 LEU C C 1 ATOM 3178 O O . LEU C 3 12 ? 58.286 39.729 -12.484 1.00 31.58 ? 12 LEU C O 1 ATOM 3179 C CB . LEU C 3 12 ? 60.315 37.533 -13.288 1.00 47.65 ? 12 LEU C CB 1 ATOM 3180 C CG . LEU C 3 12 ? 61.612 38.341 -13.395 1.00 49.88 ? 12 LEU C CG 1 ATOM 3181 C CD1 . LEU C 3 12 ? 62.645 37.855 -12.384 1.00 51.44 ? 12 LEU C CD1 1 ATOM 3182 C CD2 . LEU C 3 12 ? 62.165 38.289 -14.816 1.00 46.60 ? 12 LEU C CD2 1 HETATM 3183 C C1 . CIR C 3 13 ? 60.265 41.952 -11.292 1.00 61.65 ? 13 CIR C C1 1 HETATM 3184 O O1 . CIR C 3 13 ? 60.676 41.623 -12.431 1.00 65.55 ? 13 CIR C O1 1 HETATM 3185 C C2 . CIR C 3 13 ? 59.877 40.935 -10.281 1.00 53.16 ? 13 CIR C C2 1 HETATM 3186 N N2 . CIR C 3 13 ? 59.925 39.583 -10.785 1.00 40.98 ? 13 CIR C N2 1 HETATM 3187 C C3 . CIR C 3 13 ? 60.763 41.032 -9.080 1.00 63.00 ? 13 CIR C C3 1 HETATM 3188 C C4 . CIR C 3 13 ? 60.211 40.093 -8.031 1.00 68.49 ? 13 CIR C C4 1 HETATM 3189 C C5 . CIR C 3 13 ? 61.021 40.148 -6.759 1.00 72.48 ? 13 CIR C C5 1 HETATM 3190 N N6 . CIR C 3 13 ? 60.780 38.918 -6.019 1.00 75.18 ? 13 CIR C N6 1 HETATM 3191 C C7 . CIR C 3 13 ? 59.461 38.598 -5.534 1.00 71.59 ? 13 CIR C C7 1 HETATM 3192 O O7 . CIR C 3 13 ? 58.530 39.361 -5.734 1.00 66.84 ? 13 CIR C O7 1 HETATM 3193 N N8 . CIR C 3 13 ? 59.240 37.371 -4.807 1.00 66.40 ? 13 CIR C N8 1 HETATM 3194 C C1 . NAG D 4 . ? 49.558 49.520 -18.754 1.00 46.33 ? 500 NAG A C1 1 HETATM 3195 C C2 . NAG D 4 . ? 49.103 48.812 -20.037 1.00 53.18 ? 500 NAG A C2 1 HETATM 3196 C C3 . NAG D 4 . ? 50.230 48.781 -21.076 1.00 58.01 ? 500 NAG A C3 1 HETATM 3197 C C4 . NAG D 4 . ? 50.803 50.172 -21.286 1.00 61.76 ? 500 NAG A C4 1 HETATM 3198 C C5 . NAG D 4 . ? 51.238 50.749 -19.950 1.00 61.71 ? 500 NAG A C5 1 HETATM 3199 C C6 . NAG D 4 . ? 51.788 52.147 -20.083 1.00 63.88 ? 500 NAG A C6 1 HETATM 3200 C C7 . NAG D 4 . ? 47.390 47.093 -19.671 1.00 50.05 ? 500 NAG A C7 1 HETATM 3201 C C8 . NAG D 4 . ? 47.140 45.647 -19.349 1.00 51.68 ? 500 NAG A C8 1 HETATM 3202 N N2 . NAG D 4 . ? 48.670 47.460 -19.739 1.00 50.36 ? 500 NAG A N2 1 HETATM 3203 O O3 . NAG D 4 . ? 49.745 48.277 -22.318 1.00 56.10 ? 500 NAG A O3 1 HETATM 3204 O O4 . NAG D 4 . ? 51.923 50.115 -22.159 1.00 66.49 ? 500 NAG A O4 1 HETATM 3205 O O5 . NAG D 4 . ? 50.100 50.816 -19.079 1.00 53.92 ? 500 NAG A O5 1 HETATM 3206 O O6 . NAG D 4 . ? 51.369 52.987 -19.018 1.00 66.95 ? 500 NAG A O6 1 HETATM 3207 O O7 . NAG D 4 . ? 46.476 47.889 -19.843 1.00 46.94 ? 500 NAG A O7 1 HETATM 3208 C C1 . NAG E 4 . ? 31.191 42.435 6.584 1.00 39.26 ? 501 NAG A C1 1 HETATM 3209 C C2 . NAG E 4 . ? 31.188 43.425 5.428 1.00 43.21 ? 501 NAG A C2 1 HETATM 3210 C C3 . NAG E 4 . ? 32.042 44.618 5.788 1.00 52.56 ? 501 NAG A C3 1 HETATM 3211 C C4 . NAG E 4 . ? 31.347 45.374 6.905 1.00 65.08 ? 501 NAG A C4 1 HETATM 3212 C C5 . NAG E 4 . ? 31.354 44.521 8.172 1.00 60.04 ? 501 NAG A C5 1 HETATM 3213 C C6 . NAG E 4 . ? 30.431 45.070 9.249 1.00 62.02 ? 501 NAG A C6 1 HETATM 3214 C C7 . NAG E 4 . ? 30.891 42.705 3.089 1.00 30.20 ? 501 NAG A C7 1 HETATM 3215 C C8 . NAG E 4 . ? 31.550 42.084 1.886 1.00 32.77 ? 501 NAG A C8 1 HETATM 3216 N N2 . NAG E 4 . ? 31.655 42.828 4.185 1.00 34.82 ? 501 NAG A N2 1 HETATM 3217 O O3 . NAG E 4 . ? 32.254 45.419 4.632 1.00 41.56 ? 501 NAG A O3 1 HETATM 3218 O O4 . NAG E 4 . ? 31.784 46.720 7.096 1.00 76.72 ? 501 NAG A O4 1 HETATM 3219 O O5 . NAG E 4 . ? 30.901 43.169 7.906 1.00 52.28 ? 501 NAG A O5 1 HETATM 3220 O O6 . NAG E 4 . ? 30.435 46.491 9.335 1.00 63.42 ? 501 NAG A O6 1 HETATM 3221 O O7 . NAG E 4 . ? 29.725 43.083 3.065 1.00 32.79 ? 501 NAG A O7 1 HETATM 3222 C C1 . NAG F 4 . ? 32.977 47.362 7.578 1.00 80.03 ? 502 NAG A C1 1 HETATM 3223 C C2 . NAG F 4 . ? 34.342 46.644 7.615 1.00 82.21 ? 502 NAG A C2 1 HETATM 3224 C C3 . NAG F 4 . ? 35.467 47.531 7.045 1.00 86.91 ? 502 NAG A C3 1 HETATM 3225 C C4 . NAG F 4 . ? 35.279 49.011 7.378 1.00 85.54 ? 502 NAG A C4 1 HETATM 3226 C C5 . NAG F 4 . ? 33.896 49.534 7.027 1.00 86.62 ? 502 NAG A C5 1 HETATM 3227 C C6 . NAG F 4 . ? 33.858 50.555 5.902 1.00 90.96 ? 502 NAG A C6 1 HETATM 3228 C C7 . NAG F 4 . ? 34.596 46.773 10.100 1.00 81.37 ? 502 NAG A C7 1 HETATM 3229 C C8 . NAG F 4 . ? 34.901 45.993 11.342 1.00 78.20 ? 502 NAG A C8 1 HETATM 3230 N N2 . NAG F 4 . ? 34.672 46.097 8.934 1.00 82.21 ? 502 NAG A N2 1 HETATM 3231 O O3 . NAG F 4 . ? 35.517 47.375 5.625 1.00 90.01 ? 502 NAG A O3 1 HETATM 3232 O O4 . NAG F 4 . ? 35.455 49.259 8.764 1.00 85.03 ? 502 NAG A O4 1 HETATM 3233 O O5 . NAG F 4 . ? 33.029 48.454 6.671 1.00 83.69 ? 502 NAG A O5 1 HETATM 3234 O O6 . NAG F 4 . ? 34.695 51.689 6.116 1.00 93.99 ? 502 NAG A O6 1 HETATM 3235 O O7 . NAG F 4 . ? 34.241 47.949 10.157 1.00 82.88 ? 502 NAG A O7 1 HETATM 3236 C C1 . NAG G 4 . ? 40.842 1.230 -19.341 1.00 51.42 ? 500 NAG B C1 1 HETATM 3237 C C2 . NAG G 4 . ? 41.104 0.912 -20.875 1.00 80.63 ? 500 NAG B C2 1 HETATM 3238 C C3 . NAG G 4 . ? 41.184 -0.585 -21.118 1.00 78.59 ? 500 NAG B C3 1 HETATM 3239 C C4 . NAG G 4 . ? 42.213 -1.205 -20.193 1.00 71.89 ? 500 NAG B C4 1 HETATM 3240 C C5 . NAG G 4 . ? 41.850 -0.966 -18.737 1.00 67.49 ? 500 NAG B C5 1 HETATM 3241 C C6 . NAG G 4 . ? 42.913 -1.555 -17.824 1.00 64.25 ? 500 NAG B C6 1 HETATM 3242 C C7 . NAG G 4 . ? 38.894 1.759 -21.873 1.00 82.33 ? 500 NAG B C7 1 HETATM 3243 C C8 . NAG G 4 . ? 38.124 1.336 -20.652 1.00 81.60 ? 500 NAG B C8 1 HETATM 3244 N N2 . NAG G 4 . ? 40.231 1.538 -21.882 1.00 82.55 ? 500 NAG B N2 1 HETATM 3245 O O3 . NAG G 4 . ? 41.598 -0.760 -22.474 1.00 83.65 ? 500 NAG B O3 1 HETATM 3246 O O4 . NAG G 4 . ? 42.286 -2.602 -20.440 1.00 69.63 ? 500 NAG B O4 1 HETATM 3247 O O5 . NAG G 4 . ? 41.786 0.450 -18.492 1.00 62.19 ? 500 NAG B O5 1 HETATM 3248 O O6 . NAG G 4 . ? 43.749 -0.633 -17.135 1.00 59.94 ? 500 NAG B O6 1 HETATM 3249 O O7 . NAG G 4 . ? 38.325 2.259 -22.835 1.00 81.01 ? 500 NAG B O7 1 HETATM 3250 O O . HOH H 5 . ? 13.932 35.452 10.191 1.00 10.43 ? 601 HOH A O 1 HETATM 3251 O O . HOH H 5 . ? 37.071 41.432 -12.849 1.00 13.67 ? 602 HOH A O 1 HETATM 3252 O O . HOH H 5 . ? 35.101 24.346 4.714 1.00 15.27 ? 603 HOH A O 1 HETATM 3253 O O . HOH H 5 . ? 37.283 46.071 -6.869 1.00 13.39 ? 604 HOH A O 1 HETATM 3254 O O . HOH H 5 . ? 34.186 36.548 4.053 1.00 14.80 ? 605 HOH A O 1 HETATM 3255 O O . HOH H 5 . ? 47.261 43.970 -5.148 1.00 16.63 ? 606 HOH A O 1 HETATM 3256 O O . HOH H 5 . ? 20.090 15.612 1.449 1.00 12.91 ? 607 HOH A O 1 HETATM 3257 O O . HOH H 5 . ? 42.205 27.841 3.276 1.00 19.26 ? 608 HOH A O 1 HETATM 3258 O O . HOH H 5 . ? 15.540 29.767 -1.635 1.00 17.26 ? 609 HOH A O 1 HETATM 3259 O O . HOH H 5 . ? 11.839 26.148 13.835 1.00 22.06 ? 610 HOH A O 1 HETATM 3260 O O . HOH H 5 . ? 23.982 35.086 -11.266 1.00 23.61 ? 611 HOH A O 1 HETATM 3261 O O . HOH H 5 . ? 32.225 11.648 -7.776 1.00 18.96 ? 612 HOH A O 1 HETATM 3262 O O . HOH H 5 . ? 51.750 32.103 3.831 1.00 17.61 ? 613 HOH A O 1 HETATM 3263 O O . HOH H 5 . ? 19.486 34.922 -5.549 1.00 27.83 ? 614 HOH A O 1 HETATM 3264 O O . HOH H 5 . ? 34.708 39.993 -12.058 1.00 22.11 ? 615 HOH A O 1 HETATM 3265 O O . HOH H 5 . ? 22.846 28.920 -7.474 1.00 24.72 ? 616 HOH A O 1 HETATM 3266 O O . HOH H 5 . ? 45.580 12.840 9.074 1.00 17.44 ? 617 HOH A O 1 HETATM 3267 O O . HOH H 5 . ? 32.770 46.325 -9.148 1.00 23.39 ? 618 HOH A O 1 HETATM 3268 O O . HOH H 5 . ? 39.104 28.204 -0.389 1.00 20.23 ? 619 HOH A O 1 HETATM 3269 O O . HOH H 5 . ? 35.768 45.003 -4.685 1.00 13.46 ? 620 HOH A O 1 HETATM 3270 O O . HOH H 5 . ? 37.062 21.270 5.523 1.00 18.15 ? 621 HOH A O 1 HETATM 3271 O O . HOH H 5 . ? 32.072 15.342 -5.204 1.00 23.01 ? 622 HOH A O 1 HETATM 3272 O O . HOH H 5 . ? 13.377 13.787 6.847 1.00 32.16 ? 623 HOH A O 1 HETATM 3273 O O . HOH H 5 . ? 32.133 41.200 -1.076 1.00 17.82 ? 624 HOH A O 1 HETATM 3274 O O . HOH H 5 . ? 29.752 35.537 7.627 1.00 20.84 ? 625 HOH A O 1 HETATM 3275 O O . HOH H 5 . ? 23.993 33.598 11.710 1.00 25.63 ? 626 HOH A O 1 HETATM 3276 O O . HOH H 5 . ? 40.190 18.011 10.486 1.00 25.51 ? 627 HOH A O 1 HETATM 3277 O O . HOH H 5 . ? 37.616 18.849 -8.729 1.00 18.97 ? 628 HOH A O 1 HETATM 3278 O O . HOH H 5 . ? 20.697 41.576 12.485 1.00 28.53 ? 629 HOH A O 1 HETATM 3279 O O . HOH H 5 . ? 28.407 19.569 6.924 1.00 23.62 ? 630 HOH A O 1 HETATM 3280 O O . HOH H 5 . ? 56.992 30.392 -0.299 1.00 26.84 ? 631 HOH A O 1 HETATM 3281 O O . HOH H 5 . ? 12.247 17.341 9.488 1.00 29.55 ? 632 HOH A O 1 HETATM 3282 O O . HOH H 5 . ? 40.138 14.281 11.294 1.00 43.29 ? 633 HOH A O 1 HETATM 3283 O O . HOH H 5 . ? 18.052 41.887 13.347 1.00 24.50 ? 634 HOH A O 1 HETATM 3284 O O . HOH H 5 . ? 54.907 36.832 0.003 1.00 21.59 ? 635 HOH A O 1 HETATM 3285 O O . HOH H 5 . ? 16.154 40.590 -0.045 1.00 27.92 ? 636 HOH A O 1 HETATM 3286 O O . HOH H 5 . ? 38.118 28.887 -17.886 1.00 20.87 ? 637 HOH A O 1 HETATM 3287 O O . HOH H 5 . ? 52.866 48.868 -16.115 1.00 33.19 ? 638 HOH A O 1 HETATM 3288 O O . HOH H 5 . ? 36.659 23.623 -16.691 1.00 32.90 ? 639 HOH A O 1 HETATM 3289 O O . HOH H 5 . ? 54.850 44.036 -12.574 1.00 27.28 ? 640 HOH A O 1 HETATM 3290 O O . HOH H 5 . ? 25.983 22.901 11.528 1.00 36.65 ? 641 HOH A O 1 HETATM 3291 O O . HOH H 5 . ? 26.361 35.805 -10.572 1.00 23.78 ? 642 HOH A O 1 HETATM 3292 O O . HOH H 5 . ? 50.836 35.388 6.480 1.00 38.39 ? 643 HOH A O 1 HETATM 3293 O O . HOH H 5 . ? 54.588 45.917 -14.462 1.00 32.58 ? 644 HOH A O 1 HETATM 3294 O O . HOH H 5 . ? 9.617 19.253 3.230 1.00 36.34 ? 645 HOH A O 1 HETATM 3295 O O . HOH H 5 . ? 33.495 47.223 -4.293 1.00 32.31 ? 646 HOH A O 1 HETATM 3296 O O . HOH H 5 . ? 15.161 25.180 16.200 1.00 32.37 ? 647 HOH A O 1 HETATM 3297 O O . HOH H 5 . ? 10.469 25.784 11.566 1.00 30.56 ? 648 HOH A O 1 HETATM 3298 O O . HOH H 5 . ? 37.241 4.901 -11.740 1.00 34.94 ? 649 HOH A O 1 HETATM 3299 O O . HOH H 5 . ? 13.084 34.732 -0.407 1.00 27.13 ? 650 HOH A O 1 HETATM 3300 O O . HOH H 5 . ? 55.677 42.342 -14.794 1.00 26.31 ? 651 HOH A O 1 HETATM 3301 O O . HOH H 5 . ? 12.516 37.704 3.754 1.00 35.21 ? 652 HOH A O 1 HETATM 3302 O O . HOH H 5 . ? 11.235 37.100 7.889 1.00 31.64 ? 653 HOH A O 1 HETATM 3303 O O . HOH H 5 . ? 52.330 48.033 -6.005 1.00 23.61 ? 654 HOH A O 1 HETATM 3304 O O . HOH H 5 . ? 49.142 41.797 0.766 1.00 24.14 ? 655 HOH A O 1 HETATM 3305 O O . HOH H 5 . ? 15.203 13.872 11.725 1.00 38.64 ? 656 HOH A O 1 HETATM 3306 O O . HOH H 5 . ? 29.016 29.536 10.541 1.00 22.48 ? 657 HOH A O 1 HETATM 3307 O O . HOH H 5 . ? 19.941 42.541 -2.477 1.00 23.08 ? 658 HOH A O 1 HETATM 3308 O O . HOH H 5 . ? 49.359 36.617 4.380 1.00 37.08 ? 659 HOH A O 1 HETATM 3309 O O . HOH H 5 . ? 33.596 39.309 6.039 1.00 29.18 ? 660 HOH A O 1 HETATM 3310 O O . HOH H 5 . ? 10.058 38.104 10.937 1.00 41.97 ? 661 HOH A O 1 HETATM 3311 O O . HOH H 5 . ? 34.454 15.793 -12.339 1.00 31.56 ? 662 HOH A O 1 HETATM 3312 O O . HOH H 5 . ? 29.503 31.529 -16.002 1.00 49.07 ? 663 HOH A O 1 HETATM 3313 O O . HOH H 5 . ? 42.431 30.017 7.067 1.00 33.91 ? 664 HOH A O 1 HETATM 3314 O O . HOH H 5 . ? 14.457 22.029 0.664 1.00 40.41 ? 665 HOH A O 1 HETATM 3315 O O . HOH H 5 . ? 42.411 50.232 -8.731 1.00 39.25 ? 666 HOH A O 1 HETATM 3316 O O . HOH H 5 . ? 30.001 47.048 -7.340 1.00 28.67 ? 667 HOH A O 1 HETATM 3317 O O . HOH H 5 . ? 37.857 40.912 4.264 1.00 36.41 ? 668 HOH A O 1 HETATM 3318 O O . HOH H 5 . ? 9.914 23.296 2.919 1.00 46.46 ? 669 HOH A O 1 HETATM 3319 O O . HOH H 5 . ? 13.853 31.600 -0.420 1.00 36.49 ? 670 HOH A O 1 HETATM 3320 O O . HOH H 5 . ? 40.522 51.692 -9.371 1.00 35.60 ? 671 HOH A O 1 HETATM 3321 O O . HOH H 5 . ? 31.080 25.492 -11.659 1.00 20.25 ? 672 HOH A O 1 HETATM 3322 O O . HOH H 5 . ? 9.114 39.589 12.367 1.00 34.14 ? 673 HOH A O 1 HETATM 3323 O O . HOH H 5 . ? 34.063 41.638 5.125 1.00 30.13 ? 674 HOH A O 1 HETATM 3324 O O . HOH H 5 . ? 55.190 39.150 -0.865 1.00 39.98 ? 675 HOH A O 1 HETATM 3325 O O . HOH H 5 . ? 26.379 29.975 9.366 1.00 26.21 ? 676 HOH A O 1 HETATM 3326 O O . HOH H 5 . ? 29.987 33.331 9.350 1.00 34.84 ? 677 HOH A O 1 HETATM 3327 O O . HOH H 5 . ? 36.553 48.628 -7.437 1.00 25.98 ? 678 HOH A O 1 HETATM 3328 O O . HOH H 5 . ? 56.267 27.198 4.601 1.00 54.13 ? 679 HOH A O 1 HETATM 3329 O O . HOH H 5 . ? 49.218 32.998 4.900 1.00 43.87 ? 680 HOH A O 1 HETATM 3330 O O . HOH H 5 . ? 53.833 32.161 5.416 1.00 33.27 ? 681 HOH A O 1 HETATM 3331 O O . HOH H 5 . ? 31.046 27.359 -13.420 1.00 36.00 ? 682 HOH A O 1 HETATM 3332 O O . HOH H 5 . ? 21.468 25.630 -6.836 1.00 36.20 ? 683 HOH A O 1 HETATM 3333 O O . HOH H 5 . ? 13.175 14.373 9.991 1.00 43.47 ? 684 HOH A O 1 HETATM 3334 O O . HOH H 5 . ? 46.876 25.931 16.012 1.00 40.45 ? 685 HOH A O 1 HETATM 3335 O O . HOH H 5 . ? 34.126 22.213 -3.144 1.00 55.62 ? 686 HOH A O 1 HETATM 3336 O O . HOH H 5 . ? 29.138 21.924 8.628 1.00 32.71 ? 687 HOH A O 1 HETATM 3337 O O . HOH H 5 . ? 38.974 26.630 9.542 1.00 36.32 ? 688 HOH A O 1 HETATM 3338 O O . HOH H 5 . ? 29.241 41.321 9.940 1.00 35.00 ? 689 HOH A O 1 HETATM 3339 O O . HOH H 5 . ? 20.386 28.713 21.913 1.00 34.30 ? 690 HOH A O 1 HETATM 3340 O O . HOH H 5 . ? 39.326 28.994 7.983 1.00 41.78 ? 691 HOH A O 1 HETATM 3341 O O . HOH H 5 . ? 4.778 23.613 15.392 1.00 33.70 ? 692 HOH A O 1 HETATM 3342 O O . HOH H 5 . ? 8.244 22.869 4.833 1.00 47.45 ? 693 HOH A O 1 HETATM 3343 O O . HOH H 5 . ? 9.399 22.432 16.832 1.00 35.32 ? 694 HOH A O 1 HETATM 3344 O O . HOH H 5 . ? 2.099 22.035 15.545 1.00 42.37 ? 695 HOH A O 1 HETATM 3345 O O . HOH H 5 . ? 19.552 19.137 13.130 1.00 37.48 ? 696 HOH A O 1 HETATM 3346 O O . HOH H 5 . ? 20.337 26.761 16.446 1.00 54.29 ? 697 HOH A O 1 HETATM 3347 O O . HOH H 5 . ? 26.557 40.607 9.539 1.00 44.00 ? 698 HOH A O 1 HETATM 3348 O O . HOH H 5 . ? 35.322 24.168 -9.569 1.00 10.97 ? 699 HOH A O 1 HETATM 3349 O O . HOH H 5 . ? 46.589 34.132 4.350 1.00 46.96 ? 700 HOH A O 1 HETATM 3350 O O . HOH H 5 . ? 38.347 38.324 3.548 1.00 32.62 ? 701 HOH A O 1 HETATM 3351 O O . HOH H 5 . ? 48.083 37.924 9.598 1.00 43.95 ? 702 HOH A O 1 HETATM 3352 O O . HOH H 5 . ? 55.884 27.151 -3.137 1.00 38.39 ? 703 HOH A O 1 HETATM 3353 O O . HOH H 5 . ? 22.073 29.898 -4.950 1.00 10.46 ? 704 HOH A O 1 HETATM 3354 O O . HOH H 5 . ? 37.086 29.940 -8.419 1.00 11.34 ? 705 HOH A O 1 HETATM 3355 O O . HOH H 5 . ? 36.927 35.530 -9.342 1.00 12.53 ? 706 HOH A O 1 HETATM 3356 O O . HOH H 5 . ? 20.606 25.059 -4.465 1.00 28.55 ? 707 HOH A O 1 HETATM 3357 O O . HOH H 5 . ? 34.521 33.752 5.580 1.00 40.13 ? 708 HOH A O 1 HETATM 3358 O O . HOH H 5 . ? 49.433 39.158 6.878 1.00 30.68 ? 709 HOH A O 1 HETATM 3359 O O . HOH H 5 . ? 14.653 38.234 -1.786 1.00 39.47 ? 710 HOH A O 1 HETATM 3360 O O . HOH H 5 . ? 22.939 12.747 4.731 1.00 35.45 ? 711 HOH A O 1 HETATM 3361 O O . HOH H 5 . ? 24.394 39.432 6.915 1.00 19.38 ? 712 HOH A O 1 HETATM 3362 O O . HOH H 5 . ? 52.507 19.950 1.819 1.00 24.58 ? 713 HOH A O 1 HETATM 3363 O O . HOH H 5 . ? 49.938 19.728 8.973 1.00 32.22 ? 714 HOH A O 1 HETATM 3364 O O . HOH H 5 . ? 47.590 37.905 7.079 1.00 44.54 ? 715 HOH A O 1 HETATM 3365 O O . HOH H 5 . ? 32.877 15.581 9.892 1.00 33.82 ? 716 HOH A O 1 HETATM 3366 O O . HOH H 5 . ? 28.636 45.244 1.439 1.00 52.30 ? 717 HOH A O 1 HETATM 3367 O O . HOH H 5 . ? 6.902 16.682 3.805 1.00 29.68 ? 718 HOH A O 1 HETATM 3368 O O . HOH H 5 . ? 39.257 33.976 3.356 1.00 37.84 ? 719 HOH A O 1 HETATM 3369 O O . HOH H 5 . ? 41.996 22.332 13.054 1.00 35.51 ? 720 HOH A O 1 HETATM 3370 O O . HOH H 5 . ? 32.880 36.170 7.239 1.00 50.83 ? 721 HOH A O 1 HETATM 3371 O O . HOH H 5 . ? 31.894 26.293 10.656 1.00 14.46 ? 722 HOH A O 1 HETATM 3372 O O . HOH H 5 . ? 31.286 31.824 -18.295 1.00 36.97 ? 723 HOH A O 1 HETATM 3373 O O . HOH H 5 . ? 57.110 25.278 -1.813 1.00 46.73 ? 724 HOH A O 1 HETATM 3374 O O . HOH H 5 . ? 52.061 42.939 4.317 1.00 36.59 ? 725 HOH A O 1 HETATM 3375 O O . HOH H 5 . ? 14.743 27.848 -3.033 1.00 40.37 ? 726 HOH A O 1 HETATM 3376 O O . HOH H 5 . ? 29.359 42.033 -12.487 1.00 32.98 ? 727 HOH A O 1 HETATM 3377 O O . HOH H 5 . ? 41.801 34.254 4.897 1.00 49.27 ? 728 HOH A O 1 HETATM 3378 O O . HOH H 5 . ? 41.841 30.725 4.730 1.00 44.07 ? 729 HOH A O 1 HETATM 3379 O O . HOH H 5 . ? 27.460 34.326 -12.808 1.00 35.59 ? 730 HOH A O 1 HETATM 3380 O O . HOH H 5 . ? 15.388 25.775 -2.410 1.00 43.29 ? 731 HOH A O 1 HETATM 3381 O O . HOH H 5 . ? 34.438 10.417 11.397 1.00 43.49 ? 732 HOH A O 1 HETATM 3382 O O . HOH H 5 . ? 31.916 22.664 8.183 1.00 33.81 ? 733 HOH A O 1 HETATM 3383 O O . HOH H 5 . ? 22.152 14.541 3.046 1.00 31.63 ? 734 HOH A O 1 HETATM 3384 O O . HOH H 5 . ? 5.495 29.232 9.671 1.00 43.46 ? 735 HOH A O 1 HETATM 3385 O O . HOH H 5 . ? 14.275 34.000 17.524 1.00 21.22 ? 736 HOH A O 1 HETATM 3386 O O . HOH H 5 . ? 34.723 7.802 4.462 1.00 44.93 ? 737 HOH A O 1 HETATM 3387 O O . HOH H 5 . ? 28.142 15.835 -2.837 1.00 38.64 ? 738 HOH A O 1 HETATM 3388 O O . HOH H 5 . ? 27.059 47.510 -5.650 1.00 42.43 ? 739 HOH A O 1 HETATM 3389 O O . HOH H 5 . ? 31.276 56.182 4.467 1.00 40.44 ? 740 HOH A O 1 HETATM 3390 O O . HOH H 5 . ? 5.548 15.847 12.355 1.00 35.53 ? 741 HOH A O 1 HETATM 3391 O O . HOH H 5 . ? 3.985 31.999 9.469 1.00 51.11 ? 742 HOH A O 1 HETATM 3392 O O . HOH H 5 . ? 33.800 54.750 5.198 1.00 48.62 ? 743 HOH A O 1 HETATM 3393 O O . HOH H 5 . ? 54.927 24.313 -1.481 1.00 52.03 ? 744 HOH A O 1 HETATM 3394 O O . HOH H 5 . ? 42.464 35.885 6.991 1.00 37.04 ? 745 HOH A O 1 HETATM 3395 O O . HOH H 5 . ? 8.397 38.184 15.169 1.00 42.04 ? 746 HOH A O 1 HETATM 3396 O O . HOH H 5 . ? 21.410 32.009 18.829 1.00 31.94 ? 747 HOH A O 1 HETATM 3397 O O . HOH H 5 . ? 10.906 38.858 16.086 1.00 36.92 ? 748 HOH A O 1 HETATM 3398 O O . HOH H 5 . ? 25.498 34.895 -14.834 1.00 32.96 ? 749 HOH A O 1 HETATM 3399 O O . HOH H 5 . ? 22.150 16.327 8.681 1.00 39.80 ? 750 HOH A O 1 HETATM 3400 O O . HOH H 5 . ? 35.135 22.082 -8.605 1.00 29.99 ? 751 HOH A O 1 HETATM 3401 O O . HOH H 5 . ? 35.258 22.109 7.033 1.00 33.41 ? 752 HOH A O 1 HETATM 3402 O O . HOH H 5 . ? 7.184 34.130 13.059 1.00 29.72 ? 753 HOH A O 1 HETATM 3403 O O . HOH H 5 . ? 19.562 14.654 5.375 1.00 42.85 ? 754 HOH A O 1 HETATM 3404 O O . HOH H 5 . ? 6.571 20.208 4.266 1.00 46.29 ? 755 HOH A O 1 HETATM 3405 O O . HOH H 5 . ? 25.017 38.102 -14.639 1.00 38.89 ? 756 HOH A O 1 HETATM 3406 O O . HOH H 5 . ? 45.727 39.129 7.489 1.00 47.92 ? 757 HOH A O 1 HETATM 3407 O O . HOH H 5 . ? 23.914 36.062 -13.361 1.00 45.90 ? 758 HOH A O 1 HETATM 3408 O O . HOH H 5 . ? 7.235 14.422 4.654 1.00 42.59 ? 759 HOH A O 1 HETATM 3409 O O . HOH H 5 . ? 42.445 38.938 6.462 1.00 38.55 ? 760 HOH A O 1 HETATM 3410 O O . HOH H 5 . ? 39.401 16.331 14.578 1.00 44.87 ? 761 HOH A O 1 HETATM 3411 O O . HOH H 5 . ? 36.614 31.398 4.706 1.00 24.88 ? 762 HOH A O 1 HETATM 3412 O O . HOH H 5 . ? 47.542 47.321 -4.301 1.00 34.32 ? 763 HOH A O 1 HETATM 3413 O O . HOH H 5 . ? 51.860 35.055 2.791 1.00 33.23 ? 764 HOH A O 1 HETATM 3414 O O . HOH H 5 . ? 22.374 39.131 -13.888 1.00 28.18 ? 765 HOH A O 1 HETATM 3415 O O . HOH H 5 . ? 17.627 43.879 3.104 1.00 41.04 ? 766 HOH A O 1 HETATM 3416 O O . HOH H 5 . ? 30.583 21.282 -2.602 1.00 35.47 ? 767 HOH A O 1 HETATM 3417 O O . HOH H 5 . ? 0.856 23.363 4.137 1.00 33.30 ? 768 HOH A O 1 HETATM 3418 O O . HOH H 5 . ? 35.933 19.990 -11.055 1.00 32.71 ? 769 HOH A O 1 HETATM 3419 O O . HOH H 5 . ? 9.295 28.535 2.252 1.00 32.71 ? 770 HOH A O 1 HETATM 3420 O O . HOH H 5 . ? 20.544 44.130 -4.010 1.00 37.57 ? 771 HOH A O 1 HETATM 3421 O O . HOH H 5 . ? 18.131 34.697 18.564 1.00 38.48 ? 772 HOH A O 1 HETATM 3422 O O . HOH H 5 . ? 15.690 38.800 21.949 1.00 46.22 ? 773 HOH A O 1 HETATM 3423 O O . HOH H 5 . ? 18.790 49.457 1.014 1.00 45.64 ? 774 HOH A O 1 HETATM 3424 O O . HOH H 5 . ? 19.026 29.902 18.893 1.00 46.32 ? 775 HOH A O 1 HETATM 3425 O O . HOH H 5 . ? 31.829 13.479 9.118 1.00 50.43 ? 776 HOH A O 1 HETATM 3426 O O . HOH H 5 . ? 6.723 26.849 2.098 1.00 50.40 ? 777 HOH A O 1 HETATM 3427 O O . HOH H 5 . ? 56.850 23.992 9.288 1.00 52.81 ? 778 HOH A O 1 HETATM 3428 O O . HOH H 5 . ? 19.598 27.388 -7.054 1.00 42.46 ? 779 HOH A O 1 HETATM 3429 O O . HOH H 5 . ? 46.434 39.050 10.907 1.00 35.74 ? 780 HOH A O 1 HETATM 3430 O O . HOH H 5 . ? -0.069 25.981 4.634 1.00 49.76 ? 781 HOH A O 1 HETATM 3431 O O . HOH H 5 . ? 3.802 15.300 15.043 1.00 52.68 ? 782 HOH A O 1 HETATM 3432 O O . HOH I 5 . ? 45.909 24.125 -22.812 1.00 14.89 ? 601 HOH B O 1 HETATM 3433 O O . HOH I 5 . ? 27.842 18.173 -1.548 1.00 13.87 ? 602 HOH B O 1 HETATM 3434 O O . HOH I 5 . ? 46.183 16.206 -7.103 1.00 13.59 ? 603 HOH B O 1 HETATM 3435 O O . HOH I 5 . ? 50.249 32.959 -7.967 1.00 12.81 ? 604 HOH B O 1 HETATM 3436 O O . HOH I 5 . ? 41.352 34.224 -20.011 1.00 19.71 ? 605 HOH B O 1 HETATM 3437 O O . HOH I 5 . ? 39.541 32.862 -18.172 1.00 15.67 ? 606 HOH B O 1 HETATM 3438 O O . HOH I 5 . ? 40.954 29.674 -6.344 1.00 13.65 ? 607 HOH B O 1 HETATM 3439 O O . HOH I 5 . ? 48.862 15.143 -21.045 1.00 19.59 ? 608 HOH B O 1 HETATM 3440 O O . HOH I 5 . ? 37.637 25.368 -10.618 1.00 18.30 ? 609 HOH B O 1 HETATM 3441 O O . HOH I 5 . ? 63.050 19.726 -11.669 1.00 17.90 ? 610 HOH B O 1 HETATM 3442 O O . HOH I 5 . ? 52.630 32.067 -24.788 1.00 27.10 ? 611 HOH B O 1 HETATM 3443 O O . HOH I 5 . ? 38.261 24.129 -12.995 1.00 14.94 ? 612 HOH B O 1 HETATM 3444 O O . HOH I 5 . ? 38.617 38.933 -14.329 1.00 18.63 ? 613 HOH B O 1 HETATM 3445 O O . HOH I 5 . ? 7.666 15.708 -18.554 1.00 22.76 ? 614 HOH B O 1 HETATM 3446 O O . HOH I 5 . ? 48.195 25.474 -23.401 1.00 21.05 ? 615 HOH B O 1 HETATM 3447 O O . HOH I 5 . ? 56.768 16.817 -10.152 1.00 19.03 ? 616 HOH B O 1 HETATM 3448 O O . HOH I 5 . ? 60.991 23.200 -23.535 1.00 18.61 ? 617 HOH B O 1 HETATM 3449 O O . HOH I 5 . ? 51.933 13.459 -19.819 1.00 22.66 ? 618 HOH B O 1 HETATM 3450 O O . HOH I 5 . ? 23.886 22.617 -6.060 1.00 23.00 ? 619 HOH B O 1 HETATM 3451 O O . HOH I 5 . ? 14.931 4.976 -12.581 1.00 22.41 ? 620 HOH B O 1 HETATM 3452 O O . HOH I 5 . ? 3.091 2.504 -10.188 1.00 21.55 ? 621 HOH B O 1 HETATM 3453 O O . HOH I 5 . ? -4.978 10.296 -12.965 1.00 31.84 ? 622 HOH B O 1 HETATM 3454 O O . HOH I 5 . ? -8.836 13.517 -16.500 1.00 27.30 ? 623 HOH B O 1 HETATM 3455 O O . HOH I 5 . ? 1.576 14.320 -15.819 1.00 25.17 ? 624 HOH B O 1 HETATM 3456 O O . HOH I 5 . ? 60.038 15.617 -15.668 1.00 14.36 ? 625 HOH B O 1 HETATM 3457 O O . HOH I 5 . ? 14.227 5.024 0.954 1.00 23.33 ? 626 HOH B O 1 HETATM 3458 O O . HOH I 5 . ? 9.413 9.502 -15.318 1.00 23.15 ? 627 HOH B O 1 HETATM 3459 O O . HOH I 5 . ? 29.549 13.276 -7.930 1.00 23.56 ? 628 HOH B O 1 HETATM 3460 O O . HOH I 5 . ? 45.763 7.295 2.041 1.00 32.01 ? 629 HOH B O 1 HETATM 3461 O O . HOH I 5 . ? 15.157 18.747 1.133 1.00 29.13 ? 630 HOH B O 1 HETATM 3462 O O . HOH I 5 . ? 31.909 20.475 -0.532 1.00 23.88 ? 631 HOH B O 1 HETATM 3463 O O . HOH I 5 . ? 50.955 25.655 -27.581 1.00 36.76 ? 632 HOH B O 1 HETATM 3464 O O . HOH I 5 . ? 41.084 39.961 -15.048 1.00 23.67 ? 633 HOH B O 1 HETATM 3465 O O . HOH I 5 . ? 46.706 28.165 -24.027 1.00 28.03 ? 634 HOH B O 1 HETATM 3466 O O . HOH I 5 . ? 61.229 30.871 -22.540 1.00 32.73 ? 635 HOH B O 1 HETATM 3467 O O . HOH I 5 . ? 33.803 8.805 1.835 1.00 28.28 ? 636 HOH B O 1 HETATM 3468 O O . HOH I 5 . ? 54.958 30.231 -25.031 1.00 36.93 ? 637 HOH B O 1 HETATM 3469 O O . HOH I 5 . ? 7.292 7.821 1.114 1.00 25.75 ? 638 HOH B O 1 HETATM 3470 O O . HOH I 5 . ? 53.182 15.787 -18.292 1.00 27.33 ? 639 HOH B O 1 HETATM 3471 O O . HOH I 5 . ? 41.334 10.479 -5.127 1.00 32.58 ? 640 HOH B O 1 HETATM 3472 O O . HOH I 5 . ? 17.048 4.204 1.155 1.00 28.40 ? 641 HOH B O 1 HETATM 3473 O O . HOH I 5 . ? 23.229 23.681 -3.443 1.00 26.30 ? 642 HOH B O 1 HETATM 3474 O O . HOH I 5 . ? 17.263 15.620 -11.289 1.00 30.99 ? 643 HOH B O 1 HETATM 3475 O O . HOH I 5 . ? 21.294 19.165 -12.352 1.00 24.73 ? 644 HOH B O 1 HETATM 3476 O O . HOH I 5 . ? 31.409 4.622 0.736 1.00 29.37 ? 645 HOH B O 1 HETATM 3477 O O . HOH I 5 . ? 37.183 21.338 -13.674 1.00 45.95 ? 646 HOH B O 1 HETATM 3478 O O . HOH I 5 . ? 13.714 11.264 1.363 1.00 23.19 ? 647 HOH B O 1 HETATM 3479 O O . HOH I 5 . ? 42.829 48.462 -2.413 1.00 26.08 ? 648 HOH B O 1 HETATM 3480 O O . HOH I 5 . ? 35.365 47.132 -2.827 1.00 36.00 ? 649 HOH B O 1 HETATM 3481 O O . HOH I 5 . ? 45.416 4.359 -7.539 1.00 33.22 ? 650 HOH B O 1 HETATM 3482 O O . HOH I 5 . ? 19.418 -5.532 -5.310 1.00 41.07 ? 651 HOH B O 1 HETATM 3483 O O . HOH I 5 . ? 10.723 16.352 -17.237 1.00 24.92 ? 652 HOH B O 1 HETATM 3484 O O . HOH I 5 . ? 46.735 21.222 -25.244 1.00 31.10 ? 653 HOH B O 1 HETATM 3485 O O . HOH I 5 . ? -11.028 9.351 -7.991 1.00 31.31 ? 654 HOH B O 1 HETATM 3486 O O . HOH I 5 . ? 43.549 23.920 -24.644 1.00 31.70 ? 655 HOH B O 1 HETATM 3487 O O . HOH I 5 . ? 47.096 13.010 -21.080 1.00 33.10 ? 656 HOH B O 1 HETATM 3488 O O . HOH I 5 . ? 48.015 5.842 -8.384 1.00 37.99 ? 657 HOH B O 1 HETATM 3489 O O . HOH I 5 . ? 49.537 7.066 -4.168 1.00 35.45 ? 658 HOH B O 1 HETATM 3490 O O . HOH I 5 . ? 39.952 3.661 -9.945 1.00 40.75 ? 659 HOH B O 1 HETATM 3491 O O . HOH I 5 . ? 42.887 5.754 -0.301 1.00 36.36 ? 660 HOH B O 1 HETATM 3492 O O . HOH I 5 . ? 9.528 6.017 1.735 1.00 33.08 ? 661 HOH B O 1 HETATM 3493 O O . HOH I 5 . ? 10.611 13.595 -18.289 1.00 30.76 ? 662 HOH B O 1 HETATM 3494 O O . HOH I 5 . ? 45.079 3.452 -3.955 1.00 36.66 ? 663 HOH B O 1 HETATM 3495 O O . HOH I 5 . ? 57.866 16.593 -8.066 1.00 38.21 ? 664 HOH B O 1 HETATM 3496 O O . HOH I 5 . ? 11.036 11.661 -16.590 1.00 34.95 ? 665 HOH B O 1 HETATM 3497 O O . HOH I 5 . ? 23.069 5.571 2.775 1.00 36.97 ? 666 HOH B O 1 HETATM 3498 O O . HOH I 5 . ? 41.582 42.906 -15.261 1.00 18.97 ? 667 HOH B O 1 HETATM 3499 O O . HOH I 5 . ? 46.944 30.317 -25.278 1.00 33.74 ? 668 HOH B O 1 HETATM 3500 O O . HOH I 5 . ? 28.559 10.952 -10.657 1.00 32.09 ? 669 HOH B O 1 HETATM 3501 O O . HOH I 5 . ? 25.384 4.494 2.227 1.00 24.27 ? 670 HOH B O 1 HETATM 3502 O O . HOH I 5 . ? -3.572 12.637 -14.021 1.00 42.88 ? 671 HOH B O 1 HETATM 3503 O O . HOH I 5 . ? 23.351 18.024 4.113 1.00 34.50 ? 672 HOH B O 1 HETATM 3504 O O . HOH I 5 . ? 23.468 10.306 3.407 1.00 29.62 ? 673 HOH B O 1 HETATM 3505 O O . HOH I 5 . ? 4.888 8.940 -20.867 1.00 33.98 ? 674 HOH B O 1 HETATM 3506 O O . HOH I 5 . ? 48.445 24.964 -26.612 1.00 32.01 ? 675 HOH B O 1 HETATM 3507 O O . HOH I 5 . ? 43.726 43.475 -16.223 1.00 31.94 ? 676 HOH B O 1 HETATM 3508 O O . HOH I 5 . ? -7.405 14.210 -7.137 1.00 32.80 ? 677 HOH B O 1 HETATM 3509 O O . HOH I 5 . ? 16.199 24.038 -8.225 1.00 55.27 ? 678 HOH B O 1 HETATM 3510 O O . HOH I 5 . ? 27.486 5.017 3.559 1.00 26.20 ? 679 HOH B O 1 HETATM 3511 O O . HOH I 5 . ? 53.101 8.358 -8.922 1.00 36.25 ? 680 HOH B O 1 HETATM 3512 O O . HOH I 5 . ? 31.012 49.380 -0.263 1.00 49.25 ? 681 HOH B O 1 HETATM 3513 O O . HOH I 5 . ? 11.762 12.422 -20.971 1.00 40.21 ? 682 HOH B O 1 HETATM 3514 O O . HOH I 5 . ? 55.450 29.375 -27.837 1.00 58.09 ? 683 HOH B O 1 HETATM 3515 O O . HOH I 5 . ? 53.922 17.483 -20.166 1.00 11.39 ? 684 HOH B O 1 HETATM 3516 O O . HOH I 5 . ? 50.305 24.757 -21.906 1.00 9.52 ? 685 HOH B O 1 HETATM 3517 O O . HOH I 5 . ? 39.558 30.411 -18.930 1.00 30.28 ? 686 HOH B O 1 HETATM 3518 O O . HOH I 5 . ? 52.676 41.281 -22.158 1.00 35.04 ? 687 HOH B O 1 HETATM 3519 O O . HOH I 5 . ? 63.146 31.351 -10.680 1.00 31.31 ? 688 HOH B O 1 HETATM 3520 O O . HOH I 5 . ? 26.802 6.818 5.194 1.00 35.60 ? 689 HOH B O 1 HETATM 3521 O O . HOH I 5 . ? 61.745 33.086 -9.762 1.00 34.91 ? 690 HOH B O 1 HETATM 3522 O O . HOH I 5 . ? 12.664 -0.684 -3.170 1.00 31.19 ? 691 HOH B O 1 HETATM 3523 O O . HOH I 5 . ? 3.381 10.373 2.127 1.00 39.59 ? 692 HOH B O 1 HETATM 3524 O O . HOH I 5 . ? 21.650 8.807 3.141 1.00 41.42 ? 693 HOH B O 1 HETATM 3525 O O . HOH I 5 . ? 29.511 1.374 -8.548 1.00 39.94 ? 694 HOH B O 1 HETATM 3526 O O . HOH I 5 . ? 53.718 8.248 -5.987 1.00 38.16 ? 695 HOH B O 1 HETATM 3527 O O . HOH I 5 . ? 38.275 4.689 3.451 1.00 31.94 ? 696 HOH B O 1 HETATM 3528 O O . HOH I 5 . ? 27.593 4.821 7.342 1.00 39.92 ? 697 HOH B O 1 HETATM 3529 O O . HOH I 5 . ? 52.521 16.609 -15.777 1.00 9.38 ? 698 HOH B O 1 HETATM 3530 O O . HOH I 5 . ? 44.998 18.641 -7.907 1.00 10.28 ? 699 HOH B O 1 HETATM 3531 O O . HOH I 5 . ? 32.580 52.103 1.804 1.00 48.32 ? 700 HOH B O 1 HETATM 3532 O O . HOH I 5 . ? -0.000 11.807 -19.328 0.50 49.25 ? 701 HOH B O 1 HETATM 3533 O O . HOH I 5 . ? -0.286 20.622 -13.979 1.00 39.23 ? 702 HOH B O 1 HETATM 3534 O O . HOH I 5 . ? 48.834 4.897 -18.218 1.00 34.84 ? 703 HOH B O 1 HETATM 3535 O O . HOH I 5 . ? 31.301 37.110 -14.483 1.00 38.14 ? 704 HOH B O 1 HETATM 3536 O O . HOH I 5 . ? 49.386 5.099 -6.062 1.00 41.45 ? 705 HOH B O 1 HETATM 3537 O O . HOH I 5 . ? 50.960 12.535 -22.139 1.00 49.86 ? 706 HOH B O 1 HETATM 3538 O O . HOH I 5 . ? 17.657 -1.448 -4.586 1.00 26.34 ? 707 HOH B O 1 HETATM 3539 O O . HOH I 5 . ? 40.465 24.119 -18.740 1.00 31.53 ? 708 HOH B O 1 HETATM 3540 O O . HOH I 5 . ? 29.826 5.379 2.909 1.00 35.57 ? 709 HOH B O 1 HETATM 3541 O O . HOH I 5 . ? 39.590 25.891 -20.813 1.00 42.49 ? 710 HOH B O 1 HETATM 3542 O O . HOH I 5 . ? 67.038 26.747 -17.623 1.00 48.13 ? 711 HOH B O 1 HETATM 3543 O O . HOH I 5 . ? 37.632 33.677 -16.984 1.00 31.94 ? 712 HOH B O 1 HETATM 3544 O O . HOH I 5 . ? 50.153 31.131 -26.537 1.00 45.06 ? 713 HOH B O 1 HETATM 3545 O O . HOH I 5 . ? 6.789 1.592 -1.058 1.00 29.46 ? 714 HOH B O 1 HETATM 3546 O O . HOH I 5 . ? -8.566 6.345 -2.410 1.00 52.18 ? 715 HOH B O 1 HETATM 3547 O O . HOH I 5 . ? 47.315 2.397 -7.354 1.00 47.07 ? 716 HOH B O 1 HETATM 3548 O O . HOH I 5 . ? 39.249 22.705 -16.313 1.00 40.48 ? 717 HOH B O 1 HETATM 3549 O O . HOH I 5 . ? 43.966 3.802 -26.827 1.00 32.88 ? 718 HOH B O 1 HETATM 3550 O O . HOH I 5 . ? 54.016 40.335 -27.453 1.00 48.38 ? 719 HOH B O 1 HETATM 3551 O O . HOH I 5 . ? -6.249 12.802 -15.523 1.00 49.02 ? 720 HOH B O 1 HETATM 3552 O O . HOH I 5 . ? 41.806 45.902 5.660 1.00 40.86 ? 721 HOH B O 1 HETATM 3553 O O . HOH I 5 . ? 28.542 36.741 -14.138 1.00 43.28 ? 722 HOH B O 1 HETATM 3554 O O . HOH I 5 . ? 48.417 3.850 -14.891 1.00 45.22 ? 723 HOH B O 1 HETATM 3555 O O . HOH I 5 . ? 8.483 20.249 -1.771 1.00 43.44 ? 724 HOH B O 1 HETATM 3556 O O . HOH I 5 . ? 43.908 3.373 -10.830 1.00 43.89 ? 725 HOH B O 1 HETATM 3557 O O . HOH I 5 . ? 40.263 37.116 -21.027 1.00 35.84 ? 726 HOH B O 1 HETATM 3558 O O . HOH I 5 . ? -1.180 -0.475 -16.749 1.00 52.48 ? 727 HOH B O 1 HETATM 3559 O O . HOH I 5 . ? 22.660 13.069 -12.367 1.00 34.85 ? 728 HOH B O 1 HETATM 3560 O O . HOH I 5 . ? 37.636 25.841 -15.593 1.00 16.28 ? 729 HOH B O 1 HETATM 3561 O O . HOH I 5 . ? 45.133 14.168 -22.400 1.00 30.12 ? 730 HOH B O 1 HETATM 3562 O O . HOH I 5 . ? 45.973 40.908 -21.528 1.00 31.22 ? 731 HOH B O 1 HETATM 3563 O O . HOH I 5 . ? 15.538 15.080 -13.659 1.00 17.75 ? 732 HOH B O 1 HETATM 3564 O O . HOH I 5 . ? 12.727 10.369 -21.431 1.00 29.55 ? 733 HOH B O 1 HETATM 3565 O O . HOH I 5 . ? 1.214 -0.937 -16.040 1.00 46.90 ? 734 HOH B O 1 HETATM 3566 O O . HOH I 5 . ? 48.455 9.980 -18.931 1.00 27.64 ? 735 HOH B O 1 HETATM 3567 O O . HOH I 5 . ? 13.620 15.870 -14.561 1.00 31.59 ? 736 HOH B O 1 HETATM 3568 O O . HOH I 5 . ? 28.657 51.207 0.408 1.00 44.57 ? 737 HOH B O 1 HETATM 3569 O O . HOH I 5 . ? 11.515 1.055 -1.121 1.00 55.94 ? 738 HOH B O 1 HETATM 3570 O O . HOH I 5 . ? 28.845 15.986 7.569 1.00 47.63 ? 739 HOH B O 1 HETATM 3571 O O . HOH I 5 . ? 32.092 8.279 -8.616 1.00 39.86 ? 740 HOH B O 1 HETATM 3572 O O . HOH I 5 . ? 28.015 14.266 5.101 1.00 29.64 ? 741 HOH B O 1 HETATM 3573 O O . HOH I 5 . ? 19.437 14.155 -12.789 1.00 36.29 ? 742 HOH B O 1 HETATM 3574 O O . HOH I 5 . ? 68.000 29.322 -16.683 1.00 42.68 ? 743 HOH B O 1 HETATM 3575 O O . HOH I 5 . ? 32.183 7.919 -6.102 1.00 51.32 ? 744 HOH B O 1 HETATM 3576 O O . HOH I 5 . ? 2.813 16.168 1.847 1.00 43.22 ? 745 HOH B O 1 HETATM 3577 O O . HOH I 5 . ? 45.406 46.490 -2.397 1.00 30.95 ? 746 HOH B O 1 HETATM 3578 O O . HOH I 5 . ? 14.417 14.183 -16.159 1.00 35.08 ? 747 HOH B O 1 HETATM 3579 O O . HOH I 5 . ? 20.105 -0.884 -11.166 1.00 42.76 ? 748 HOH B O 1 HETATM 3580 O O . HOH I 5 . ? 20.863 1.224 -10.261 1.00 34.69 ? 749 HOH B O 1 HETATM 3581 O O . HOH I 5 . ? 12.140 22.954 -10.290 1.00 42.34 ? 750 HOH B O 1 HETATM 3582 O O . HOH I 5 . ? 16.895 11.925 -13.045 1.00 27.64 ? 751 HOH B O 1 HETATM 3583 O O . HOH I 5 . ? 43.630 32.343 -25.170 1.00 43.24 ? 752 HOH B O 1 HETATM 3584 O O . HOH I 5 . ? 6.853 21.517 -3.640 1.00 43.96 ? 753 HOH B O 1 HETATM 3585 O O . HOH I 5 . ? 54.895 12.133 -4.828 1.00 43.81 ? 754 HOH B O 1 HETATM 3586 O O . HOH I 5 . ? 1.660 6.625 -18.342 1.00 46.34 ? 755 HOH B O 1 HETATM 3587 O O . HOH I 5 . ? -4.026 29.176 -5.905 1.00 46.40 ? 756 HOH B O 1 HETATM 3588 O O . HOH I 5 . ? 32.442 2.125 -0.380 1.00 51.71 ? 757 HOH B O 1 HETATM 3589 O O . HOH J 5 . ? 52.380 9.416 0.852 1.00 28.49 ? 101 HOH C O 1 HETATM 3590 O O . HOH J 5 . ? 60.197 31.235 -11.166 1.00 25.54 ? 102 HOH C O 1 HETATM 3591 O O . HOH J 5 . ? 42.720 12.336 -3.615 1.00 34.77 ? 103 HOH C O 1 HETATM 3592 O O . HOH J 5 . ? 52.001 17.201 2.353 1.00 24.23 ? 104 HOH C O 1 HETATM 3593 O O . HOH J 5 . ? 56.364 25.867 -9.227 1.00 22.12 ? 105 HOH C O 1 HETATM 3594 O O . HOH J 5 . ? 57.629 23.117 -9.122 1.00 45.81 ? 106 HOH C O 1 HETATM 3595 O O . HOH J 5 . ? 58.497 26.658 -7.200 1.00 59.39 ? 107 HOH C O 1 HETATM 3596 O O . HOH J 5 . ? 54.951 10.704 0.726 1.00 39.35 ? 108 HOH C O 1 HETATM 3597 O O . HOH J 5 . ? 53.110 14.269 -0.011 1.00 37.01 ? 109 HOH C O 1 HETATM 3598 O O . HOH J 5 . ? 57.508 36.213 -14.276 1.00 32.16 ? 110 HOH C O 1 HETATM 3599 O O . HOH J 5 . ? 57.526 28.481 -5.817 1.00 49.78 ? 111 HOH C O 1 HETATM 3600 O O . HOH J 5 . ? 56.258 40.944 -5.462 1.00 25.56 ? 112 HOH C O 1 HETATM 3601 O O . HOH J 5 . ? 54.346 18.166 -1.202 1.00 31.89 ? 113 HOH C O 1 HETATM 3602 O O . HOH J 5 . ? 54.524 16.062 1.712 1.00 44.86 ? 114 HOH C O 1 HETATM 3603 O O . HOH J 5 . ? 59.117 29.285 -9.302 1.00 25.73 ? 115 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 ? 0.8034 0.7611 0.7769 -0.0498 -0.0468 -0.0748 3 GLU A N 2 C CA . GLU A 3 ? 0.7604 0.7272 0.7504 -0.0441 -0.0286 -0.0692 3 GLU A CA 3 C C . GLU A 3 ? 0.6272 0.6093 0.6545 -0.0429 -0.0261 -0.0663 3 GLU A C 4 O O . GLU A 3 ? 0.6786 0.6694 0.7242 -0.0445 -0.0380 -0.0660 3 GLU A O 5 C CB . GLU A 3 ? 0.7813 0.7556 0.7650 -0.0373 -0.0246 -0.0609 3 GLU A CB 6 C CG . GLU A 3 ? 0.7674 0.7579 0.7687 -0.0336 -0.0337 -0.0547 3 GLU A CG 7 C CD . GLU A 3 ? 0.7925 0.7816 0.7747 -0.0306 -0.0386 -0.0507 3 GLU A CD 8 O OE1 . GLU A 3 ? 0.8025 0.7803 0.7611 -0.0302 -0.0319 -0.0513 3 GLU A OE1 9 O OE2 . GLU A 3 ? 0.7906 0.7893 0.7831 -0.0284 -0.0482 -0.0467 3 GLU A OE2 10 N N . GLU A 4 ? 0.4995 0.4843 0.5391 -0.0398 -0.0101 -0.0634 4 GLU A N 11 C CA . GLU A 4 ? 0.4540 0.4510 0.5263 -0.0378 -0.0046 -0.0594 4 GLU A CA 12 C C . GLU A 4 ? 0.3638 0.3755 0.4469 -0.0300 -0.0006 -0.0495 4 GLU A C 13 O O . GLU A 4 ? 0.3914 0.4137 0.4971 -0.0285 -0.0029 -0.0461 4 GLU A O 14 C CB . GLU A 4 ? 0.5484 0.5397 0.6284 -0.0379 0.0108 -0.0603 4 GLU A CB 15 C CG . GLU A 4 ? 0.7254 0.7017 0.8008 -0.0459 0.0094 -0.0708 4 GLU A CG 16 C CD . GLU A 4 ? 0.7957 0.7679 0.8851 -0.0452 0.0260 -0.0703 4 GLU A CD 17 O OE1 . GLU A 4 ? 0.7534 0.7335 0.8513 -0.0381 0.0377 -0.0612 4 GLU A OE1 18 O OE2 . GLU A 4 ? 0.8815 0.8418 0.9732 -0.0517 0.0268 -0.0789 4 GLU A OE2 19 N N . HIS A 5 ? 0.2922 0.3032 0.3593 -0.0254 0.0058 -0.0452 5 HIS A N 20 C CA . HIS A 5 ? 0.2838 0.3059 0.3571 -0.0184 0.0096 -0.0368 5 HIS A CA 21 C C . HIS A 5 ? 0.2502 0.2707 0.3025 -0.0157 0.0077 -0.0346 5 HIS A C 22 O O . HIS A 5 ? 0.2113 0.2220 0.2459 -0.0177 0.0093 -0.0377 5 HIS A O 23 C CB . HIS A 5 ? 0.2504 0.2756 0.3366 -0.0143 0.0232 -0.0314 5 HIS A CB 24 C CG . HIS A 5 ? 0.2682 0.2946 0.3774 -0.0165 0.0274 -0.0325 5 HIS A CG 25 N ND1 . HIS A 5 ? 0.2587 0.2932 0.3879 -0.0158 0.0248 -0.0303 5 HIS A ND1 26 C CD2 . HIS A 5 ? 0.3039 0.3238 0.4217 -0.0195 0.0348 -0.0354 5 HIS A CD2 27 C CE1 . HIS A 5 ? 0.2717 0.3052 0.4216 -0.0184 0.0304 -0.0317 5 HIS A CE1 28 N NE2 . HIS A 5 ? 0.3366 0.3611 0.4793 -0.0207 0.0362 -0.0349 5 HIS A NE2 29 N N . VAL A 6 ? 0.2245 0.2536 0.2795 -0.0110 0.0057 -0.0293 6 VAL A N 30 C CA . VAL A 6 ? 0.2238 0.2522 0.2627 -0.0082 0.0045 -0.0268 6 VAL A CA 31 C C . VAL A 6 ? 0.1973 0.2331 0.2420 -0.0022 0.0103 -0.0203 6 VAL A C 32 O O . VAL A 6 ? 0.2003 0.2423 0.2569 0.0004 0.0109 -0.0176 6 VAL A O 33 C CB . VAL A 6 ? 0.1672 0.1956 0.1979 -0.0093 -0.0071 -0.0280 6 VAL A CB 34 C CG1 . VAL A 6 ? 0.1832 0.2103 0.1992 -0.0065 -0.0069 -0.0253 6 VAL A CG1 35 C CG2 . VAL A 6 ? 0.1505 0.1696 0.1710 -0.0153 -0.0152 -0.0343 6 VAL A CG2 36 N N . ILE A 7 ? 0.1333 0.1675 0.1694 -0.0002 0.0143 -0.0178 7 ILE A N 37 C CA . ILE A 7 ? 0.1527 0.1920 0.1896 0.0050 0.0169 -0.0122 7 ILE A CA 38 C C . ILE A 7 ? 0.1766 0.2152 0.2018 0.0057 0.0118 -0.0120 7 ILE A C 39 O O . ILE A 7 ? 0.1434 0.1774 0.1614 0.0037 0.0121 -0.0134 7 ILE A O 40 C CB . ILE A 7 ? 0.1570 0.1960 0.1982 0.0071 0.0245 -0.0082 7 ILE A CB 41 C CG1 . ILE A 7 ? 0.2189 0.2574 0.2729 0.0065 0.0310 -0.0080 7 ILE A CG1 42 C CG2 . ILE A 7 ? 0.1350 0.1777 0.1728 0.0120 0.0240 -0.0027 7 ILE A CG2 43 C CD1 . ILE A 7 ? 0.1743 0.2118 0.2339 0.0089 0.0388 -0.0032 7 ILE A CD1 44 N N . ILE A 8 ? 0.1630 0.2051 0.1869 0.0086 0.0086 -0.0102 8 ILE A N 45 C CA . ILE A 8 ? 0.1612 0.2022 0.1757 0.0091 0.0038 -0.0103 8 ILE A CA 46 C C . ILE A 8 ? 0.1752 0.2182 0.1871 0.0129 0.0044 -0.0071 8 ILE A C 47 O O . ILE A 8 ? 0.1828 0.2271 0.1962 0.0159 0.0065 -0.0055 8 ILE A O 48 C CB . ILE A 8 ? 0.0836 0.1246 0.0967 0.0084 -0.0023 -0.0122 8 ILE A CB 49 C CG1 . ILE A 8 ? 0.0893 0.1270 0.1018 0.0042 -0.0058 -0.0156 8 ILE A CG1 50 C CG2 . ILE A 8 ? 0.1290 0.1679 0.1333 0.0092 -0.0061 -0.0119 8 ILE A CG2 51 C CD1 . ILE A 8 ? 0.1244 0.1626 0.1378 0.0037 -0.0140 -0.0163 8 ILE A CD1 52 N N . GLN A 9 ? 0.1870 0.2288 0.1947 0.0126 0.0027 -0.0063 9 GLN A N 53 C CA . GLN A 9 ? 0.0826 0.1248 0.0856 0.0151 -0.0003 -0.0045 9 GLN A CA 54 C C . GLN A 9 ? 0.1297 0.1698 0.1273 0.0146 -0.0048 -0.0070 9 GLN A C 55 O O . GLN A 9 ? 0.0836 0.1220 0.0808 0.0122 -0.0065 -0.0079 9 GLN A O 56 C CB . GLN A 9 ? 0.0876 0.1306 0.0942 0.0148 -0.0010 -0.0019 9 GLN A CB 57 C CG . GLN A 9 ? 0.1329 0.1757 0.1350 0.0162 -0.0071 -0.0008 9 GLN A CG 58 C CD . GLN A 9 ? 0.1357 0.1807 0.1473 0.0152 -0.0092 0.0021 9 GLN A CD 59 O OE1 . GLN A 9 ? 0.1520 0.1989 0.1726 0.0154 -0.0048 0.0051 9 GLN A OE1 60 N NE2 . GLN A 9 ? 0.1705 0.2151 0.1828 0.0141 -0.0154 0.0013 9 GLN A NE2 61 N N . ALA A 10 ? 0.0866 0.1259 0.0807 0.0170 -0.0054 -0.0077 10 ALA A N 62 C CA . ALA A 10 ? 0.1333 0.1701 0.1245 0.0169 -0.0086 -0.0097 10 ALA A CA 63 C C . ALA A 10 ? 0.1343 0.1674 0.1177 0.0185 -0.0109 -0.0106 10 ALA A C 64 O O . ALA A 10 ? 0.1916 0.2227 0.1690 0.0211 -0.0090 -0.0100 10 ALA A O 65 C CB . ALA A 10 ? 0.1661 0.2039 0.1624 0.0182 -0.0070 -0.0101 10 ALA A CB 66 N N . GLU A 11 ? 0.1656 0.1963 0.1478 0.0169 -0.0147 -0.0121 11 GLU A N 67 C CA . GLU A 11 ? 0.2019 0.2280 0.1773 0.0174 -0.0182 -0.0141 11 GLU A CA 68 C C . GLU A 11 ? 0.2082 0.2300 0.1832 0.0174 -0.0188 -0.0163 11 GLU A C 69 O O . GLU A 11 ? 0.1374 0.1605 0.1178 0.0162 -0.0186 -0.0152 11 GLU A O 70 C CB . GLU A 11 ? 0.1282 0.1556 0.1074 0.0147 -0.0227 -0.0134 11 GLU A CB 71 C CG . GLU A 11 ? 0.2142 0.2462 0.1976 0.0148 -0.0222 -0.0101 11 GLU A CG 72 C CD . GLU A 11 ? 0.2275 0.2622 0.2223 0.0119 -0.0247 -0.0084 11 GLU A CD 73 O OE1 . GLU A 11 ? 0.1928 0.2253 0.1907 0.0100 -0.0284 -0.0101 11 GLU A OE1 74 O OE2 . GLU A 11 ? 0.1667 0.2053 0.1695 0.0117 -0.0220 -0.0053 11 GLU A OE2 75 N N . PHE A 12 ? 0.2217 0.2371 0.1891 0.0189 -0.0194 -0.0192 12 PHE A N 76 C CA . PHE A 12 ? 0.2078 0.2182 0.1766 0.0185 -0.0202 -0.0213 12 PHE A CA 77 C C . PHE A 12 ? 0.1914 0.1935 0.1512 0.0178 -0.0236 -0.0258 12 PHE A C 78 O O . PHE A 12 ? 0.1430 0.1415 0.0914 0.0187 -0.0249 -0.0275 12 PHE A O 79 C CB . PHE A 12 ? 0.2504 0.2599 0.2232 0.0215 -0.0154 -0.0205 12 PHE A CB 80 C CG . PHE A 12 ? 0.2540 0.2580 0.2203 0.0252 -0.0097 -0.0225 12 PHE A CG 81 C CD1 . PHE A 12 ? 0.2229 0.2163 0.1798 0.0263 -0.0084 -0.0268 12 PHE A CD1 82 C CD2 . PHE A 12 ? 0.2440 0.2517 0.2139 0.0277 -0.0044 -0.0201 12 PHE A CD2 83 C CE1 . PHE A 12 ? 0.2094 0.1947 0.1575 0.0300 -0.0007 -0.0287 12 PHE A CE1 84 C CE2 . PHE A 12 ? 0.2634 0.2644 0.2277 0.0315 0.0035 -0.0212 12 PHE A CE2 85 C CZ . PHE A 12 ? 0.2254 0.2145 0.1774 0.0329 0.0059 -0.0255 12 PHE A CZ 86 N N . TYR A 13 ? 0.1978 0.1958 0.1617 0.0161 -0.0254 -0.0277 13 TYR A N 87 C CA . TYR A 13 ? 0.2149 0.2031 0.1713 0.0150 -0.0284 -0.0332 13 TYR A CA 88 C C . TYR A 13 ? 0.2468 0.2287 0.2074 0.0162 -0.0243 -0.0345 13 TYR A C 89 O O . TYR A 13 ? 0.2078 0.1933 0.1795 0.0157 -0.0233 -0.0308 13 TYR A O 90 C CB . TYR A 13 ? 0.1858 0.1750 0.1475 0.0105 -0.0365 -0.0343 13 TYR A CB 91 C CG . TYR A 13 ? 0.2554 0.2339 0.2076 0.0085 -0.0422 -0.0411 13 TYR A CG 92 C CD1 . TYR A 13 ? 0.2906 0.2644 0.2268 0.0086 -0.0479 -0.0439 13 TYR A CD1 93 C CD2 . TYR A 13 ? 0.2829 0.2544 0.2409 0.0064 -0.0424 -0.0446 13 TYR A CD2 94 C CE1 . TYR A 13 ? 0.2860 0.2476 0.2098 0.0062 -0.0548 -0.0510 13 TYR A CE1 95 C CE2 . TYR A 13 ? 0.1946 0.1547 0.1436 0.0039 -0.0482 -0.0519 13 TYR A CE2 96 C CZ . TYR A 13 ? 0.3222 0.2770 0.2531 0.0036 -0.0550 -0.0556 13 TYR A CZ 97 O OH . TYR A 13 ? 0.3324 0.2736 0.2510 0.0005 -0.0622 -0.0638 13 TYR A OH 98 N N . LEU A 14 ? 0.1693 0.1402 0.1196 0.0180 -0.0214 -0.0395 14 LEU A N 99 C CA . LEU A 14 ? 0.2052 0.1693 0.1609 0.0200 -0.0159 -0.0405 14 LEU A CA 100 C C . LEU A 14 ? 0.2106 0.1613 0.1593 0.0177 -0.0178 -0.0477 14 LEU A C 101 O O . LEU A 14 ? 0.2430 0.1842 0.1745 0.0172 -0.0193 -0.0537 14 LEU A O 102 C CB . LEU A 14 ? 0.2167 0.1787 0.1703 0.0253 -0.0069 -0.0394 14 LEU A CB 103 C CG . LEU A 14 ? 0.2808 0.2355 0.2426 0.0285 0.0002 -0.0397 14 LEU A CG 104 C CD1 . LEU A 14 ? 0.1698 0.1330 0.1500 0.0288 -0.0017 -0.0328 14 LEU A CD1 105 C CD2 . LEU A 14 ? 0.1917 0.1423 0.1513 0.0336 0.0104 -0.0397 14 LEU A CD2 106 N N . ASN A 15 ? 0.2046 0.1533 0.1656 0.0162 -0.0178 -0.0472 15 ASN A N 107 C CA . ASN A 15 ? 0.2381 0.1731 0.1962 0.0139 -0.0183 -0.0542 15 ASN A CA 108 C C . ASN A 15 ? 0.2175 0.1445 0.1802 0.0184 -0.0085 -0.0539 15 ASN A C 109 O O . ASN A 15 ? 0.2304 0.1652 0.2053 0.0219 -0.0045 -0.0465 15 ASN A O 110 C CB . ASN A 15 ? 0.2020 0.1393 0.1740 0.0089 -0.0242 -0.0535 15 ASN A CB 111 C CG . ASN A 15 ? 0.3520 0.2915 0.3208 0.0038 -0.0346 -0.0571 15 ASN A CG 112 O OD1 . ASN A 15 ? 0.2771 0.2103 0.2288 0.0031 -0.0391 -0.0629 15 ASN A OD1 113 N ND2 . ASN A 15 ? 0.2471 0.1945 0.2323 0.0002 -0.0383 -0.0530 15 ASN A ND2 114 N N . PRO A 16 ? 0.2585 0.1691 0.2118 0.0183 -0.0049 -0.0620 16 PRO A N 115 C CA . PRO A 16 ? 0.2773 0.1756 0.2139 0.0136 -0.0113 -0.0719 16 PRO A CA 116 C C . PRO A 16 ? 0.2707 0.1620 0.1818 0.0153 -0.0104 -0.0763 16 PRO A C 117 O O . PRO A 16 ? 0.3636 0.2414 0.2550 0.0121 -0.0159 -0.0850 16 PRO A O 118 C CB . PRO A 16 ? 0.3273 0.2089 0.2660 0.0135 -0.0052 -0.0780 16 PRO A CB 119 C CG . PRO A 16 ? 0.3022 0.1840 0.2489 0.0205 0.0077 -0.0726 16 PRO A CG 120 C CD . PRO A 16 ? 0.2589 0.1609 0.2207 0.0226 0.0055 -0.0614 16 PRO A CD 121 N N . ASP A 17 ? 0.2603 0.1597 0.1715 0.0203 -0.0037 -0.0702 17 ASP A N 122 C CA . ASP A 17 ? 0.2764 0.1679 0.1641 0.0230 0.0005 -0.0729 17 ASP A CA 123 C C . ASP A 17 ? 0.3616 0.2557 0.2334 0.0193 -0.0119 -0.0744 17 ASP A C 124 O O . ASP A 17 ? 0.3040 0.1857 0.1492 0.0203 -0.0112 -0.0787 17 ASP A O 125 C CB . ASP A 17 ? 0.2628 0.1645 0.1608 0.0288 0.0106 -0.0649 17 ASP A CB 126 C CG . ASP A 17 ? 0.2689 0.1701 0.1869 0.0329 0.0211 -0.0619 17 ASP A CG 127 O OD1 . ASP A 17 ? 0.2818 0.1934 0.2209 0.0319 0.0170 -0.0568 17 ASP A OD1 128 O OD2 . ASP A 17 ? 0.3325 0.2219 0.2451 0.0375 0.0339 -0.0640 17 ASP A OD2 129 N N . GLN A 18 ? 0.3427 0.2517 0.2310 0.0152 -0.0225 -0.0703 18 GLN A N 130 C CA . GLN A 18 ? 0.3022 0.2171 0.1832 0.0120 -0.0347 -0.0696 18 GLN A CA 131 C C . GLN A 18 ? 0.3772 0.2963 0.2468 0.0164 -0.0300 -0.0648 18 GLN A C 132 O O . GLN A 18 ? 0.3656 0.2790 0.2146 0.0160 -0.0358 -0.0663 18 GLN A O 133 C CB . GLN A 18 ? 0.2950 0.1945 0.1565 0.0075 -0.0455 -0.0789 18 GLN A CB 134 C CG . GLN A 18 ? 0.3440 0.2401 0.2210 0.0023 -0.0509 -0.0837 18 GLN A CG 135 C CD . GLN A 18 ? 0.4101 0.2965 0.2755 -0.0039 -0.0647 -0.0913 18 GLN A CD 136 O OE1 . GLN A 18 ? 0.4977 0.3912 0.3829 -0.0094 -0.0751 -0.0912 18 GLN A OE1 137 N NE2 . GLN A 18 ? 0.4607 0.3351 0.3001 -0.0035 -0.0620 -0.0950 18 GLN A NE2 138 N N . SER A 19 ? 0.3160 0.2448 0.1998 0.0204 -0.0199 -0.0584 19 SER A N 139 C CA . SER A 19 ? 0.3147 0.2495 0.1942 0.0242 -0.0145 -0.0531 19 SER A CA 140 C C . SER A 19 ? 0.2674 0.2207 0.1651 0.0225 -0.0197 -0.0460 19 SER A C 141 O O . SER A 19 ? 0.2475 0.2104 0.1652 0.0213 -0.0201 -0.0429 19 SER A O 142 C CB . SER A 19 ? 0.3565 0.2891 0.2419 0.0295 0.0002 -0.0510 19 SER A CB 143 O OG . SER A 19 ? 0.5776 0.4929 0.4520 0.0310 0.0071 -0.0574 19 SER A OG 144 N N . GLY A 20 ? 0.2598 0.2165 0.1489 0.0228 -0.0233 -0.0433 20 GLY A N 145 C CA . GLY A 20 ? 0.3233 0.2956 0.2284 0.0216 -0.0265 -0.0370 20 GLY A CA 146 C C . GLY A 20 ? 0.3663 0.3428 0.2679 0.0249 -0.0209 -0.0320 20 GLY A C 147 O O . GLY A 20 ? 0.4646 0.4317 0.3461 0.0273 -0.0193 -0.0326 20 GLY A O 148 N N . GLU A 21 ? 0.2667 0.2553 0.1861 0.0252 -0.0173 -0.0272 21 GLU A N 149 C CA . GLU A 21 ? 0.2448 0.2373 0.1643 0.0280 -0.0112 -0.0227 21 GLU A CA 150 C C . GLU A 21 ? 0.2567 0.2612 0.1898 0.0257 -0.0152 -0.0184 21 GLU A C 151 O O . GLU A 21 ? 0.1347 0.1453 0.0802 0.0225 -0.0193 -0.0183 21 GLU A O 152 C CB . GLU A 21 ? 0.1591 0.1523 0.0873 0.0312 -0.0005 -0.0216 21 GLU A CB 153 C CG . GLU A 21 ? 0.6288 0.6078 0.5400 0.0351 0.0080 -0.0241 21 GLU A CG 154 C CD . GLU A 21 ? 0.5250 0.5042 0.4481 0.0389 0.0204 -0.0221 21 GLU A CD 155 O OE1 . GLU A 21 ? 0.2799 0.2710 0.2240 0.0383 0.0210 -0.0185 21 GLU A OE1 156 O OE2 . GLU A 21 ? 0.4858 0.4521 0.3972 0.0424 0.0297 -0.0244 21 GLU A OE2 157 N N . PHE A 22 ? 0.2230 0.2290 0.1526 0.0276 -0.0126 -0.0145 22 PHE A N 158 C CA . PHE A 22 ? 0.1662 0.1817 0.1083 0.0260 -0.0144 -0.0104 22 PHE A CA 159 C C . PHE A 22 ? 0.1961 0.2128 0.1399 0.0290 -0.0055 -0.0067 22 PHE A C 160 O O . PHE A 22 ? 0.2364 0.2457 0.1659 0.0323 -0.0017 -0.0052 22 PHE A O 161 C CB . PHE A 22 ? 0.1426 0.1579 0.0802 0.0247 -0.0236 -0.0088 22 PHE A CB 162 C CG . PHE A 22 ? 0.1729 0.1972 0.1255 0.0235 -0.0244 -0.0041 22 PHE A CG 163 C CD1 . PHE A 22 ? 0.2179 0.2439 0.1713 0.0261 -0.0188 0.0006 22 PHE A CD1 164 C CD2 . PHE A 22 ? 0.1219 0.1517 0.0887 0.0200 -0.0294 -0.0040 22 PHE A CD2 165 C CE1 . PHE A 22 ? 0.2254 0.2583 0.1934 0.0251 -0.0184 0.0048 22 PHE A CE1 166 C CE2 . PHE A 22 ? 0.1363 0.1728 0.1178 0.0192 -0.0282 0.0002 22 PHE A CE2 167 C CZ . PHE A 22 ? 0.2103 0.2482 0.1921 0.0218 -0.0229 0.0045 22 PHE A CZ 168 N N . MET A 23 ? 0.1202 0.1447 0.0803 0.0276 -0.0020 -0.0054 23 MET A N 169 C CA . MET A 23 ? 0.1634 0.1895 0.1293 0.0297 0.0064 -0.0022 23 MET A CA 170 C C . MET A 23 ? 0.1426 0.1764 0.1242 0.0269 0.0068 -0.0009 23 MET A C 171 O O . MET A 23 ? 0.1114 0.1486 0.0988 0.0235 0.0022 -0.0029 23 MET A O 172 C CB . MET A 23 ? 0.1666 0.1904 0.1365 0.0317 0.0135 -0.0036 23 MET A CB 173 C CG . MET A 23 ? 0.1730 0.2018 0.1559 0.0291 0.0102 -0.0064 23 MET A CG 174 S SD . MET A 23 ? 0.1560 0.1933 0.1591 0.0264 0.0113 -0.0053 23 MET A SD 175 C CE . MET A 23 ? 0.1022 0.1385 0.1160 0.0301 0.0221 -0.0031 23 MET A CE 176 N N . PHE A 24 ? 0.1411 0.1760 0.1286 0.0283 0.0136 0.0022 24 PHE A N 177 C CA . PHE A 24 ? 0.1469 0.1870 0.1490 0.0255 0.0154 0.0024 24 PHE A CA 178 C C . PHE A 24 ? 0.1428 0.1845 0.1571 0.0253 0.0208 0.0015 24 PHE A C 179 O O . PHE A 24 ? 0.0997 0.1387 0.1141 0.0287 0.0276 0.0035 24 PHE A O 180 C CB . PHE A 24 ? 0.0979 0.1381 0.1015 0.0267 0.0185 0.0071 24 PHE A CB 181 C CG . PHE A 24 ? 0.1785 0.2207 0.1833 0.0247 0.0131 0.0077 24 PHE A CG 182 C CD1 . PHE A 24 ? 0.1700 0.2109 0.1657 0.0253 0.0058 0.0082 24 PHE A CD1 183 C CD2 . PHE A 24 ? 0.2335 0.2780 0.2500 0.0221 0.0160 0.0077 24 PHE A CD2 184 C CE1 . PHE A 24 ? 0.1539 0.1976 0.1562 0.0235 0.0016 0.0095 24 PHE A CE1 185 C CE2 . PHE A 24 ? 0.1603 0.2060 0.1809 0.0207 0.0135 0.0088 24 PHE A CE2 186 C CZ . PHE A 24 ? 0.2000 0.2461 0.2154 0.0215 0.0063 0.0102 24 PHE A CZ 187 N N . ASP A 25 ? 0.1493 0.1945 0.1738 0.0213 0.0177 -0.0016 25 ASP A N 188 C CA . ASP A 25 ? 0.1157 0.1635 0.1551 0.0200 0.0195 -0.0029 25 ASP A CA 189 C C . ASP A 25 ? 0.2155 0.2646 0.2650 0.0165 0.0209 -0.0040 25 ASP A C 190 O O . ASP A 25 ? 0.2057 0.2534 0.2499 0.0136 0.0179 -0.0059 25 ASP A O 191 C CB . ASP A 25 ? 0.1203 0.1695 0.1610 0.0181 0.0118 -0.0061 25 ASP A CB 192 C CG . ASP A 25 ? 0.2332 0.2861 0.2924 0.0164 0.0106 -0.0072 25 ASP A CG 193 O OD1 . ASP A 25 ? 0.2300 0.2839 0.2964 0.0124 0.0081 -0.0093 25 ASP A OD1 194 O OD2 . ASP A 25 ? 0.2472 0.3015 0.3148 0.0189 0.0118 -0.0061 25 ASP A OD2 195 N N . PHE A 26 ? 0.1420 0.1925 0.2068 0.0166 0.0267 -0.0030 26 PHE A N 196 C CA . PHE A 26 ? 0.1435 0.1943 0.2202 0.0125 0.0277 -0.0052 26 PHE A CA 197 C C . PHE A 26 ? 0.1612 0.2154 0.2557 0.0097 0.0239 -0.0080 26 PHE A C 198 O O . PHE A 26 ? 0.1112 0.1679 0.2204 0.0123 0.0297 -0.0052 26 PHE A O 199 C CB . PHE A 26 ? 0.1447 0.1938 0.2272 0.0149 0.0383 -0.0008 26 PHE A CB 200 C CG . PHE A 26 ? 0.1571 0.2055 0.2545 0.0106 0.0408 -0.0034 26 PHE A CG 201 C CD1 . PHE A 26 ? 0.1856 0.2303 0.2774 0.0076 0.0403 -0.0058 26 PHE A CD1 202 C CD2 . PHE A 26 ? 0.1563 0.2067 0.2749 0.0093 0.0446 -0.0037 26 PHE A CD2 203 C CE1 . PHE A 26 ? 0.1723 0.2141 0.2763 0.0033 0.0432 -0.0093 26 PHE A CE1 204 C CE2 . PHE A 26 ? 0.1824 0.2312 0.3154 0.0046 0.0462 -0.0071 26 PHE A CE2 205 C CZ . PHE A 26 ? 0.1762 0.2200 0.3003 0.0015 0.0455 -0.0103 26 PHE A CZ 206 N N . ASP A 27 ? 0.1894 0.1451 0.2716 0.0165 0.0103 0.0052 27 ASP A N 207 C CA . ASP A 27 ? 0.1501 0.1089 0.2368 0.0138 0.0122 0.0009 27 ASP A CA 208 C C . ASP A 27 ? 0.1195 0.0782 0.2028 0.0127 0.0166 0.0012 27 ASP A C 209 O O . ASP A 27 ? 0.1949 0.1549 0.2865 0.0109 0.0200 0.0012 27 ASP A O 210 C CB . ASP A 27 ? 0.1598 0.1157 0.2590 0.0125 0.0127 0.0033 27 ASP A CB 211 C CG . ASP A 27 ? 0.2816 0.2373 0.3846 0.0143 0.0082 -0.0002 27 ASP A CG 212 O OD1 . ASP A 27 ? 0.2233 0.1831 0.3201 0.0165 0.0057 -0.0045 27 ASP A OD1 213 O OD2 . ASP A 27 ? 0.2148 0.1656 0.3278 0.0138 0.0073 0.0015 27 ASP A OD2 214 N N . GLY A 28 ? 0.1567 0.1136 0.2297 0.0142 0.0166 0.0011 28 GLY A N 215 C CA . GLY A 28 ? 0.1341 0.0896 0.2024 0.0146 0.0206 -0.0005 28 GLY A CA 216 C C . GLY A 28 ? 0.2846 0.2328 0.3515 0.0167 0.0274 0.0062 28 GLY A C 217 O O . GLY A 28 ? 0.2749 0.2247 0.3332 0.0178 0.0310 0.0035 28 GLY A O 218 N N . ASP A 29 ? 0.2491 0.1950 0.3173 0.0163 0.0274 0.0151 29 ASP A N 219 C CA . ASP A 29 ? 0.2350 0.1837 0.2902 0.0156 0.0309 0.0230 29 ASP A CA 220 C C . ASP A 29 ? 0.1967 0.1452 0.2383 0.0168 0.0252 0.0259 29 ASP A C 221 O O . ASP A 29 ? 0.2821 0.2285 0.3296 0.0178 0.0195 0.0260 29 ASP A O 222 C CB . ASP A 29 ? 0.1305 0.0789 0.1957 0.0131 0.0350 0.0339 29 ASP A CB 223 C CG . ASP A 29 ? 0.2758 0.2293 0.3500 0.0107 0.0422 0.0331 29 ASP A CG 224 O OD1 . ASP A 29 ? 0.3056 0.2673 0.3687 0.0114 0.0479 0.0326 29 ASP A OD1 225 O OD2 . ASP A 29 ? 0.1804 0.1308 0.2733 0.0085 0.0420 0.0324 29 ASP A OD2 226 N N . GLU A 30 ? 0.1656 0.1180 0.1894 0.0170 0.0267 0.0275 30 GLU A N 227 C CA . GLU A 30 ? 0.1611 0.1147 0.1710 0.0175 0.0204 0.0293 30 GLU A CA 228 C C . GLU A 30 ? 0.1868 0.1414 0.1972 0.0176 0.0191 0.0423 30 GLU A C 229 O O . GLU A 30 ? 0.1931 0.1501 0.2013 0.0167 0.0247 0.0510 30 GLU A O 230 C CB . GLU A 30 ? 0.2261 0.1827 0.2153 0.0181 0.0214 0.0242 30 GLU A CB 231 C CG . GLU A 30 ? 0.2601 0.2191 0.2339 0.0179 0.0142 0.0262 30 GLU A CG 232 C CD . GLU A 30 ? 0.2751 0.2373 0.2269 0.0189 0.0153 0.0211 30 GLU A CD 233 O OE1 . GLU A 30 ? 0.2610 0.2234 0.2104 0.0207 0.0218 0.0149 30 GLU A OE1 234 O OE2 . GLU A 30 ? 0.3353 0.3008 0.2727 0.0186 0.0094 0.0227 30 GLU A OE2 235 N N . ILE A 31 ? 0.2396 0.1936 0.2544 0.0189 0.0118 0.0444 31 ILE A N 236 C CA . ILE A 31 ? 0.1801 0.1348 0.1944 0.0203 0.0088 0.0571 31 ILE A CA 237 C C . ILE A 31 ? 0.3241 0.2858 0.3161 0.0201 0.0061 0.0603 31 ILE A C 238 O O . ILE A 31 ? 0.1964 0.1612 0.1787 0.0199 0.0086 0.0709 31 ILE A O 239 C CB . ILE A 31 ? 0.2200 0.1734 0.2481 0.0233 0.0016 0.0576 31 ILE A CB 240 C CG1 . ILE A 31 ? 0.2465 0.1939 0.2948 0.0242 0.0036 0.0516 31 ILE A CG1 241 C CG2 . ILE A 31 ? 0.1903 0.1431 0.2192 0.0259 -0.0021 0.0715 31 ILE A CG2 242 C CD1 . ILE A 31 ? 0.1837 0.1317 0.2458 0.0287 -0.0026 0.0501 31 ILE A CD1 243 N N . PHE A 32 ? 0.1771 0.1418 0.1609 0.0196 0.0005 0.0511 32 PHE A N 244 C CA . PHE A 32 ? 0.2220 0.1928 0.1841 0.0190 -0.0036 0.0505 32 PHE A CA 245 C C . PHE A 32 ? 0.2536 0.2236 0.2098 0.0167 -0.0082 0.0371 32 PHE A C 246 O O . PHE A 32 ? 0.2226 0.1892 0.1921 0.0156 -0.0093 0.0309 32 PHE A O 247 C CB . PHE A 32 ? 0.2014 0.1780 0.1615 0.0207 -0.0112 0.0612 32 PHE A CB 248 C CG . PHE A 32 ? 0.2368 0.2159 0.2102 0.0213 -0.0193 0.0583 32 PHE A CG 249 C CD1 . PHE A 32 ? 0.2528 0.2380 0.2183 0.0187 -0.0270 0.0514 32 PHE A CD1 250 C CD2 . PHE A 32 ? 0.1799 0.1562 0.1745 0.0244 -0.0193 0.0622 32 PHE A CD2 251 C CE1 . PHE A 32 ? 0.3061 0.2974 0.2854 0.0187 -0.0336 0.0498 32 PHE A CE1 252 C CE2 . PHE A 32 ? 0.1703 0.1524 0.1773 0.0259 -0.0257 0.0592 32 PHE A CE2 253 C CZ . PHE A 32 ? 0.1700 0.1611 0.1698 0.0228 -0.0324 0.0537 32 PHE A CZ 254 N N . HIS A 33 ? 0.2383 0.2112 0.1741 0.0159 -0.0113 0.0329 33 HIS A N 255 C CA . HIS A 33 ? 0.2028 0.1740 0.1322 0.0128 -0.0188 0.0219 33 HIS A CA 256 C C . HIS A 33 ? 0.3102 0.2889 0.2234 0.0117 -0.0277 0.0237 33 HIS A C 257 O O . HIS A 33 ? 0.2325 0.2179 0.1364 0.0142 -0.0269 0.0331 33 HIS A O 258 C CB . HIS A 33 ? 0.2475 0.2109 0.1679 0.0129 -0.0146 0.0099 33 HIS A CB 259 C CG . HIS A 33 ? 0.2936 0.2605 0.1925 0.0157 -0.0109 0.0080 33 HIS A CG 260 N ND1 . HIS A 33 ? 0.2469 0.2176 0.1443 0.0191 -0.0002 0.0132 33 HIS A ND1 261 C CD2 . HIS A 33 ? 0.2475 0.2163 0.1250 0.0157 -0.0165 0.0012 33 HIS A CD2 262 C CE1 . HIS A 33 ? 0.2726 0.2491 0.1481 0.0215 0.0015 0.0100 33 HIS A CE1 263 N NE2 . HIS A 33 ? 0.3060 0.2807 0.1682 0.0200 -0.0085 0.0020 33 HIS A NE2 264 N N . VAL A 34 ? 0.2889 0.2670 0.1992 0.0075 -0.0367 0.0155 34 VAL A N 265 C CA . VAL A 34 ? 0.2928 0.2785 0.1877 0.0057 -0.0466 0.0151 34 VAL A CA 266 C C . VAL A 34 ? 0.3626 0.3423 0.2360 0.0044 -0.0491 0.0019 34 VAL A C 267 O O . VAL A 34 ? 0.3063 0.2753 0.1821 0.0013 -0.0508 -0.0092 34 VAL A O 268 C CB . VAL A 34 ? 0.2815 0.2738 0.1897 0.0008 -0.0570 0.0160 34 VAL A CB 269 C CG1 . VAL A 34 ? 0.2864 0.2860 0.1786 -0.0025 -0.0688 0.0129 34 VAL A CG1 270 C CG2 . VAL A 34 ? 0.2186 0.2192 0.1454 0.0043 -0.0557 0.0284 34 VAL A CG2 271 N N . ASP A 35 ? 0.3982 0.3846 0.2501 0.0074 -0.0495 0.0032 35 ASP A N 272 C CA . ASP A 35 ? 0.4267 0.4099 0.2552 0.0074 -0.0537 -0.0105 35 ASP A CA 273 C C . ASP A 35 ? 0.4360 0.4200 0.2629 0.0007 -0.0690 -0.0166 35 ASP A C 274 O O . ASP A 35 ? 0.4539 0.4505 0.2755 -0.0002 -0.0767 -0.0096 35 ASP A O 275 C CB . ASP A 35 ? 0.4735 0.4678 0.2788 0.0127 -0.0495 -0.0057 35 ASP A CB 276 C CG . ASP A 35 ? 0.5470 0.5390 0.3260 0.0148 -0.0517 -0.0219 35 ASP A CG 277 O OD1 . ASP A 35 ? 0.4348 0.4186 0.2098 0.0108 -0.0626 -0.0354 35 ASP A OD1 278 O OD2 . ASP A 35 ? 0.6555 0.6546 0.4179 0.0207 -0.0426 -0.0212 35 ASP A OD2 279 N N . MET A 36 ? 0.4617 0.4327 0.2944 -0.0043 -0.0738 -0.0286 36 MET A N 280 C CA . MET A 36 ? 0.5067 0.4782 0.3433 -0.0129 -0.0883 -0.0330 36 MET A CA 281 C C . MET A 36 ? 0.5889 0.5650 0.4014 -0.0139 -0.0991 -0.0413 36 MET A C 282 O O . MET A 36 ? 0.5990 0.5857 0.4137 -0.0195 -0.1110 -0.0385 36 MET A O 283 C CB . MET A 36 ? 0.4737 0.4279 0.3211 -0.0187 -0.0910 -0.0430 36 MET A CB 284 C CG . MET A 36 ? 0.5300 0.4798 0.3991 -0.0179 -0.0814 -0.0366 36 MET A CG 285 S SD . MET A 36 ? 0.5108 0.4787 0.4039 -0.0199 -0.0809 -0.0200 36 MET A SD 286 C CE . MET A 36 ? 0.6828 0.6417 0.5952 -0.0183 -0.0699 -0.0181 36 MET A CE 287 N N . ALA A 37 ? 0.5613 0.5311 0.3510 -0.0082 -0.0953 -0.0522 37 ALA A N 288 C CA . ALA A 37 ? 0.5648 0.5409 0.3327 -0.0085 -0.1032 -0.0617 37 ALA A CA 289 C C . ALA A 37 ? 0.5004 0.4977 0.2563 -0.0056 -0.1053 -0.0489 37 ALA A C 290 O O . ALA A 37 ? 0.5724 0.5820 0.3253 -0.0104 -0.1148 -0.0500 37 ALA A O 291 C CB . ALA A 37 ? 0.6211 0.5891 0.3729 -0.0024 -0.0949 -0.0755 37 ALA A CB 292 N N . LYS A 38 ? 0.4969 0.5008 0.2525 0.0012 -0.0941 -0.0349 38 LYS A N 293 C CA . LYS A 38 ? 0.5334 0.5561 0.2791 0.0046 -0.0950 -0.0198 38 LYS A CA 294 C C . LYS A 38 ? 0.5022 0.5331 0.2724 0.0015 -0.0999 -0.0041 38 LYS A C 295 O O . LYS A 38 ? 0.4684 0.5144 0.2334 0.0036 -0.1045 0.0086 38 LYS A O 296 C CB . LYS A 38 ? 0.5505 0.5778 0.2874 0.0124 -0.0793 -0.0103 38 LYS A CB 297 C CG . LYS A 38 ? 0.6281 0.6538 0.3393 0.0173 -0.0727 -0.0240 38 LYS A CG 298 C CD . LYS A 38 ? 0.7052 0.7419 0.4080 0.0236 -0.0579 -0.0106 38 LYS A CD 299 C CE . LYS A 38 ? 0.8052 0.8422 0.4893 0.0271 -0.0490 -0.0233 38 LYS A CE 300 N NZ . LYS A 38 ? 0.8914 0.9424 0.5674 0.0312 -0.0357 -0.0084 38 LYS A NZ 301 N N . LYS A 39 ? 0.5049 0.5269 0.3012 -0.0029 -0.0992 -0.0051 39 LYS A N 302 C CA . LYS A 39 ? 0.4384 0.4692 0.2602 -0.0045 -0.1021 0.0081 39 LYS A CA 303 C C . LYS A 39 ? 0.4542 0.4914 0.2795 0.0029 -0.0931 0.0254 39 LYS A C 304 O O . LYS A 39 ? 0.4965 0.5464 0.3275 0.0049 -0.0989 0.0380 39 LYS A O 305 C CB . LYS A 39 ? 0.5339 0.5787 0.3556 -0.0096 -0.1185 0.0084 39 LYS A CB 306 C CG . LYS A 39 ? 0.5997 0.6374 0.4212 -0.0185 -0.1280 -0.0081 39 LYS A CG 307 C CD . LYS A 39 ? 0.7113 0.7655 0.5332 -0.0206 -0.1391 -0.0111 39 LYS A CD 308 C CE . LYS A 39 ? 0.7644 0.8121 0.5936 -0.0300 -0.1454 -0.0266 39 LYS A CE 309 N NZ . LYS A 39 ? 0.7255 0.7893 0.5569 -0.0328 -0.1570 -0.0300 39 LYS A NZ 310 N N . GLU A 40 ? 0.4615 0.4895 0.2849 0.0069 -0.0794 0.0262 40 GLU A N 311 C CA . GLU A 40 ? 0.4661 0.4974 0.2937 0.0126 -0.0702 0.0427 40 GLU A CA 312 C C . GLU A 40 ? 0.3919 0.4120 0.2402 0.0138 -0.0582 0.0447 40 GLU A C 313 O O . GLU A 40 ? 0.3150 0.3248 0.1655 0.0122 -0.0528 0.0329 40 GLU A O 314 C CB . GLU A 40 ? 0.4381 0.4747 0.2380 0.0163 -0.0650 0.0454 40 GLU A CB 315 C CG . GLU A 40 ? 0.5366 0.5877 0.3150 0.0170 -0.0759 0.0497 40 GLU A CG 316 C CD . GLU A 40 ? 0.7235 0.7818 0.4724 0.0209 -0.0694 0.0514 40 GLU A CD 317 O OE1 . GLU A 40 ? 0.7761 0.8311 0.5265 0.0234 -0.0554 0.0571 40 GLU A OE1 318 O OE2 . GLU A 40 ? 0.7998 0.8631 0.5290 0.0200 -0.0768 0.0459 40 GLU A OE2 319 N N . THR A 41 ? 0.3313 0.3532 0.1948 0.0171 -0.0549 0.0596 41 THR A N 320 C CA . THR A 41 ? 0.3165 0.3287 0.1999 0.0185 -0.0445 0.0625 41 THR A CA 321 C C . THR A 41 ? 0.3716 0.3813 0.2439 0.0203 -0.0328 0.0667 41 THR A C 322 O O . THR A 41 ? 0.4327 0.4495 0.2920 0.0224 -0.0318 0.0788 41 THR A O 323 C CB . THR A 41 ? 0.3371 0.3508 0.2422 0.0216 -0.0469 0.0754 41 THR A CB 324 O OG1 . THR A 41 ? 0.3801 0.3994 0.2980 0.0201 -0.0563 0.0706 41 THR A OG1 325 C CG2 . THR A 41 ? 0.2624 0.2653 0.1867 0.0230 -0.0368 0.0774 41 THR A CG2 326 N N . VAL A 42 ? 0.3909 0.3922 0.2688 0.0195 -0.0241 0.0576 42 VAL A N 327 C CA . VAL A 42 ? 0.3647 0.3662 0.2354 0.0210 -0.0121 0.0604 42 VAL A CA 328 C C . VAL A 42 ? 0.3968 0.3908 0.2916 0.0209 -0.0043 0.0664 42 VAL A C 329 O O . VAL A 42 ? 0.4018 0.3881 0.3105 0.0199 -0.0021 0.0565 42 VAL A O 330 C CB . VAL A 42 ? 0.3436 0.3432 0.1997 0.0212 -0.0083 0.0438 42 VAL A CB 331 C CG1 . VAL A 42 ? 0.3058 0.3105 0.1550 0.0234 0.0047 0.0473 42 VAL A CG1 332 C CG2 . VAL A 42 ? 0.3311 0.3360 0.1637 0.0210 -0.0178 0.0355 42 VAL A CG2 333 N N . TRP A 43 ? 0.3627 0.3586 0.2622 0.0216 -0.0008 0.0828 43 TRP A N 334 C CA . TRP A 43 ? 0.3482 0.3359 0.2712 0.0209 0.0052 0.0889 43 TRP A CA 335 C C . TRP A 43 ? 0.3469 0.3356 0.2691 0.0195 0.0171 0.0852 43 TRP A C 336 O O . TRP A 43 ? 0.3365 0.3348 0.2400 0.0197 0.0227 0.0874 43 TRP A O 337 C CB . TRP A 43 ? 0.3513 0.3385 0.2803 0.0217 0.0036 0.1085 43 TRP A CB 338 C CG . TRP A 43 ? 0.3789 0.3669 0.3106 0.0246 -0.0083 0.1122 43 TRP A CG 339 C CD1 . TRP A 43 ? 0.3219 0.3196 0.2352 0.0261 -0.0159 0.1178 43 TRP A CD1 340 C CD2 . TRP A 43 ? 0.3327 0.3140 0.2868 0.0269 -0.0143 0.1095 43 TRP A CD2 341 N NE1 . TRP A 43 ? 0.2759 0.2738 0.2006 0.0290 -0.0263 0.1196 43 TRP A NE1 342 C CE2 . TRP A 43 ? 0.3550 0.3435 0.3048 0.0299 -0.0251 0.1143 43 TRP A CE2 343 C CE3 . TRP A 43 ? 0.2661 0.2380 0.2433 0.0272 -0.0117 0.1030 43 TRP A CE3 344 C CZ2 . TRP A 43 ? 0.3086 0.2962 0.2776 0.0336 -0.0324 0.1130 43 TRP A CZ2 345 C CZ3 . TRP A 43 ? 0.2501 0.2205 0.2442 0.0310 -0.0189 0.1011 43 TRP A CZ3 346 C CH2 . TRP A 43 ? 0.2921 0.2708 0.2825 0.0343 -0.0287 0.1061 43 TRP A CH2 347 N N . ARG A 44 ? 0.3184 0.2993 0.2609 0.0184 0.0209 0.0791 44 ARG A N 348 C CA . ARG A 44 ? 0.3274 0.3107 0.2720 0.0175 0.0312 0.0737 44 ARG A CA 349 C C . ARG A 44 ? 0.2704 0.2603 0.2160 0.0152 0.0399 0.0891 44 ARG A C 350 O O . ARG A 44 ? 0.2601 0.2607 0.1951 0.0152 0.0487 0.0881 44 ARG A O 351 C CB . ARG A 44 ? 0.2064 0.1807 0.1733 0.0168 0.0319 0.0646 44 ARG A CB 352 C CG . ARG A 44 ? 0.2238 0.2019 0.1951 0.0164 0.0414 0.0585 44 ARG A CG 353 C CD . ARG A 44 ? 0.2101 0.1941 0.1615 0.0195 0.0432 0.0466 44 ARG A CD 354 N NE . ARG A 44 ? 0.2074 0.1970 0.1643 0.0206 0.0524 0.0408 44 ARG A NE 355 C CZ . ARG A 44 ? 0.3243 0.3270 0.2767 0.0204 0.0622 0.0475 44 ARG A CZ 356 N NH1 . ARG A 44 ? 0.3344 0.3447 0.2751 0.0188 0.0639 0.0613 44 ARG A NH1 357 N NH2 . ARG A 44 ? 0.2866 0.2965 0.2464 0.0220 0.0703 0.0414 44 ARG A NH2 358 N N . LEU A 45 ? 0.2665 0.2502 0.2256 0.0133 0.0373 0.1035 45 LEU A N 359 C CA . LEU A 45 ? 0.2957 0.2841 0.2549 0.0100 0.0433 0.1224 45 LEU A CA 360 C C . LEU A 45 ? 0.3120 0.3011 0.2589 0.0116 0.0356 0.1360 45 LEU A C 361 O O . LEU A 45 ? 0.3094 0.2895 0.2640 0.0144 0.0257 0.1348 45 LEU A O 362 C CB . LEU A 45 ? 0.3025 0.2801 0.2899 0.0059 0.0456 0.1291 45 LEU A CB 363 C CG . LEU A 45 ? 0.3288 0.3062 0.3320 0.0039 0.0520 0.1170 45 LEU A CG 364 C CD1 . LEU A 45 ? 0.3957 0.3642 0.4248 -0.0015 0.0539 0.1266 45 LEU A CD1 365 C CD2 . LEU A 45 ? 0.2944 0.2885 0.2836 0.0038 0.0622 0.1124 45 LEU A CD2 366 N N . GLU A 46 ? 0.3501 0.3517 0.2777 0.0105 0.0400 0.1489 46 GLU A N 367 C CA . GLU A 46 ? 0.4587 0.4627 0.3722 0.0122 0.0314 0.1590 46 GLU A CA 368 C C . GLU A 46 ? 0.3991 0.3881 0.3333 0.0117 0.0231 0.1671 46 GLU A C 369 O O . GLU A 46 ? 0.4459 0.4328 0.3758 0.0154 0.0130 0.1692 46 GLU A O 370 C CB . GLU A 46 ? 0.5772 0.5961 0.4704 0.0098 0.0375 0.1671 46 GLU A CB 371 C CG . GLU A 46 ? 0.8086 0.8433 0.6710 0.0135 0.0384 0.1575 46 GLU A CG 372 C CD . GLU A 46 ? 0.9406 0.9751 0.7887 0.0172 0.0252 0.1564 46 GLU A CD 373 O OE1 . GLU A 46 ? 0.9230 0.9507 0.7768 0.0202 0.0174 0.1481 46 GLU A OE1 374 O OE2 . GLU A 46 ? 0.9384 0.9805 0.7699 0.0170 0.0224 0.1640 46 GLU A OE2 375 N N . GLU A 47 ? 0.3368 0.3161 0.2935 0.0075 0.0270 0.1702 47 GLU A N 376 C CA . GLU A 47 ? 0.4697 0.4338 0.4455 0.0078 0.0194 0.1754 47 GLU A CA 377 C C . GLU A 47 ? 0.4806 0.4358 0.4669 0.0139 0.0100 0.1653 47 GLU A C 378 O O . GLU A 47 ? 0.4221 0.3695 0.4154 0.0171 0.0017 0.1690 47 GLU A O 379 C CB . GLU A 47 ? 0.5489 0.5045 0.5464 0.0020 0.0246 0.1772 47 GLU A CB 380 C CG . GLU A 47 ? 0.5943 0.5470 0.6073 0.0009 0.0291 0.1636 47 GLU A CG 381 C CD . GLU A 47 ? 0.6198 0.5825 0.6336 -0.0054 0.0405 0.1660 47 GLU A CD 382 O OE1 . GLU A 47 ? 0.6140 0.5921 0.6076 -0.0065 0.0468 0.1723 47 GLU A OE1 383 O OE2 . GLU A 47 ? 0.5837 0.5407 0.6178 -0.0091 0.0429 0.1608 47 GLU A OE2 384 N N . PHE A 48 ? 0.4317 0.3889 0.4195 0.0157 0.0114 0.1526 48 PHE A N 385 C CA . PHE A 48 ? 0.3745 0.3256 0.3738 0.0209 0.0034 0.1421 48 PHE A CA 386 C C . PHE A 48 ? 0.3584 0.3151 0.3465 0.0256 -0.0064 0.1463 48 PHE A C 387 O O . PHE A 48 ? 0.3045 0.2559 0.3054 0.0300 -0.0141 0.1435 48 PHE A O 388 C CB . PHE A 48 ? 0.3087 0.2631 0.3071 0.0215 0.0063 0.1282 48 PHE A CB 389 C CG . PHE A 48 ? 0.2697 0.2187 0.2824 0.0178 0.0145 0.1205 48 PHE A CG 390 C CD1 . PHE A 48 ? 0.3723 0.3138 0.4011 0.0142 0.0172 0.1257 48 PHE A CD1 391 C CD2 . PHE A 48 ? 0.2266 0.1797 0.2363 0.0173 0.0176 0.1036 48 PHE A CD2 392 C CE1 . PHE A 48 ? 0.2825 0.2212 0.3251 0.0105 0.0235 0.1183 48 PHE A CE1 393 C CE2 . PHE A 48 ? 0.2936 0.2434 0.3166 0.0145 0.0241 0.0967 48 PHE A CE2 394 C CZ . PHE A 48 ? 0.2755 0.2180 0.3158 0.0113 0.0275 0.1059 48 PHE A CZ 395 N N . GLY A 49 ? 0.3634 0.3325 0.3268 0.0250 -0.0062 0.1520 49 GLY A N 396 C CA . GLY A 49 ? 0.3208 0.2977 0.2718 0.0289 -0.0162 0.1542 49 GLY A CA 397 C C . GLY A 49 ? 0.3598 0.3322 0.3139 0.0307 -0.0215 0.1660 49 GLY A C 398 O O . GLY A 49 ? 0.3555 0.3336 0.3033 0.0347 -0.0307 0.1679 49 GLY A O 399 N N . ARG A 50 ? 0.3989 0.3615 0.3628 0.0275 -0.0162 0.1740 50 ARG A N 400 C CA . ARG A 50 ? 0.4199 0.3753 0.3883 0.0294 -0.0214 0.1858 50 ARG A CA 401 C C . ARG A 50 ? 0.4072 0.3498 0.3995 0.0347 -0.0277 0.1798 50 ARG A C 402 O O . ARG A 50 ? 0.4490 0.3859 0.4458 0.0390 -0.0344 0.1869 50 ARG A O 403 C CB . ARG A 50 ? 0.4694 0.4202 0.4377 0.0231 -0.0139 0.1979 50 ARG A CB 404 C CG . ARG A 50 ? 0.5665 0.5326 0.5096 0.0187 -0.0071 0.2044 50 ARG A CG 405 C CD . ARG A 50 ? 0.6596 0.6239 0.6016 0.0132 -0.0018 0.2199 50 ARG A CD 406 N NE . ARG A 50 ? 0.7574 0.7110 0.7209 0.0079 0.0045 0.2193 50 ARG A NE 407 C CZ . ARG A 50 ? 0.7733 0.7346 0.7361 0.0019 0.0152 0.2179 50 ARG A CZ 408 N NH1 . ARG A 50 ? 0.8061 0.7854 0.7468 0.0011 0.0215 0.2164 50 ARG A NH1 409 N NH2 . ARG A 50 ? 0.7312 0.6831 0.7153 -0.0031 0.0192 0.2169 50 ARG A NH2 410 N N . PHE A 51 ? 0.4696 0.4086 0.4764 0.0349 -0.0252 0.1662 51 PHE A N 411 C CA . PHE A 51 ? 0.5214 0.4497 0.5501 0.0398 -0.0293 0.1575 51 PHE A CA 412 C C . PHE A 51 ? 0.4229 0.3598 0.4556 0.0457 -0.0348 0.1457 51 PHE A C 413 O O . PHE A 51 ? 0.4362 0.3691 0.4832 0.0518 -0.0397 0.1397 51 PHE A O 414 C CB . PHE A 51 ? 0.5875 0.5057 0.6314 0.0353 -0.0225 0.1499 51 PHE A CB 415 C CG . PHE A 51 ? 0.7525 0.6634 0.7968 0.0287 -0.0174 0.1613 51 PHE A CG 416 C CD1 . PHE A 51 ? 0.8213 0.7382 0.8585 0.0215 -0.0085 0.1636 51 PHE A CD1 417 C CD2 . PHE A 51 ? 0.7623 0.6611 0.8146 0.0299 -0.0214 0.1700 51 PHE A CD2 418 C CE1 . PHE A 51 ? 0.8282 0.7414 0.8671 0.0149 -0.0035 0.1746 51 PHE A CE1 419 C CE2 . PHE A 51 ? 0.8110 0.7036 0.8646 0.0230 -0.0171 0.1815 51 PHE A CE2 420 C CZ . PHE A 51 ? 0.8228 0.7237 0.8701 0.0151 -0.0080 0.1839 51 PHE A CZ 421 N N . ALA A 52 ? 0.3430 0.2924 0.3628 0.0438 -0.0341 0.1421 52 ALA A N 422 C CA . ALA A 52 ? 0.3533 0.3124 0.3776 0.0476 -0.0391 0.1314 52 ALA A CA 423 C C . ALA A 52 ? 0.3247 0.2995 0.3292 0.0466 -0.0438 0.1340 52 ALA A C 424 O O . ALA A 52 ? 0.3818 0.3599 0.3665 0.0427 -0.0412 0.1414 52 ALA A O 425 C CB . ALA A 52 ? 0.3194 0.2758 0.3543 0.0454 -0.0334 0.1185 52 ALA A CB 426 N N . SER A 53 ? 0.2930 0.2790 0.3021 0.0497 -0.0509 0.1269 53 SER A N 427 C CA . SER A 53 ? 0.2824 0.2842 0.2739 0.0475 -0.0570 0.1264 53 SER A CA 428 C C . SER A 53 ? 0.3095 0.3198 0.3088 0.0456 -0.0590 0.1137 53 SER A C 429 O O . SER A 53 ? 0.2669 0.2738 0.2865 0.0481 -0.0568 0.1068 53 SER A O 430 C CB . SER A 53 ? 0.3003 0.3110 0.2882 0.0517 -0.0665 0.1322 53 SER A CB 431 O OG . SER A 53 ? 0.4430 0.4569 0.4522 0.0577 -0.0711 0.1272 53 SER A OG 432 N N . PHE A 54 ? 0.3737 0.3935 0.3554 0.0401 -0.0619 0.1065 54 PHE A N 433 C CA . PHE A 54 ? 0.3543 0.3813 0.3417 0.0360 -0.0641 0.0923 54 PHE A CA 434 C C . PHE A 54 ? 0.4220 0.4629 0.3944 0.0318 -0.0736 0.0892 54 PHE A C 435 O O . PHE A 54 ? 0.4387 0.4790 0.3879 0.0288 -0.0741 0.0897 54 PHE A O 436 C CB . PHE A 54 ? 0.3325 0.3487 0.3171 0.0307 -0.0545 0.0810 54 PHE A CB 437 C CG . PHE A 54 ? 0.2289 0.2504 0.2189 0.0257 -0.0566 0.0682 54 PHE A CG 438 C CD1 . PHE A 54 ? 0.2172 0.2432 0.2290 0.0278 -0.0565 0.0647 54 PHE A CD1 439 C CD2 . PHE A 54 ? 0.2110 0.2331 0.1842 0.0189 -0.0588 0.0597 54 PHE A CD2 440 C CE1 . PHE A 54 ? 0.1790 0.2113 0.1956 0.0222 -0.0580 0.0551 54 PHE A CE1 441 C CE2 . PHE A 54 ? 0.2220 0.2471 0.2011 0.0131 -0.0613 0.0496 54 PHE A CE2 442 C CZ . PHE A 54 ? 0.1735 0.2045 0.1743 0.0143 -0.0607 0.0484 54 PHE A CZ 443 N N . GLU A 55 ? 0.4557 0.5103 0.4414 0.0316 -0.0814 0.0859 55 GLU A N 444 C CA . GLU A 55 ? 0.4133 0.4819 0.3880 0.0261 -0.0918 0.0820 55 GLU A CA 445 C C . GLU A 55 ? 0.3195 0.3818 0.2846 0.0168 -0.0893 0.0679 55 GLU A C 446 O O . GLU A 55 ? 0.3024 0.3663 0.2821 0.0129 -0.0881 0.0605 55 GLU A O 447 C CB . GLU A 55 ? 0.4007 0.4888 0.3958 0.0283 -0.1009 0.0838 55 GLU A CB 448 C CG . GLU A 55 ? 0.5004 0.6020 0.4872 0.0209 -0.1108 0.0773 55 GLU A CG 449 C CD . GLU A 55 ? 0.5498 0.6499 0.5108 0.0208 -0.1157 0.0800 55 GLU A CD 450 O OE1 . GLU A 55 ? 0.4719 0.5737 0.4315 0.0283 -0.1173 0.0892 55 GLU A OE1 451 O OE2 . GLU A 55 ? 0.6036 0.6999 0.5450 0.0134 -0.1180 0.0723 55 GLU A OE2 452 N N . ALA A 56 ? 0.2259 0.2845 0.2111 0.0120 -0.0999 0.0397 56 ALA A N 453 C CA . ALA A 56 ? 0.2103 0.2801 0.1929 0.0065 -0.0927 0.0314 56 ALA A CA 454 C C . ALA A 56 ? 0.2762 0.3555 0.2641 0.0090 -0.0910 0.0170 56 ALA A C 455 O O . ALA A 56 ? 0.2239 0.3040 0.2117 0.0056 -0.0846 0.0078 56 ALA A O 456 C CB . ALA A 56 ? 0.2352 0.3180 0.2048 0.0047 -0.0902 0.0394 56 ALA A CB 457 N N . GLN A 57 ? 0.3243 0.4128 0.3188 0.0144 -0.0974 0.0172 57 GLN A N 458 C CA . GLN A 57 ? 0.3477 0.4499 0.3516 0.0141 -0.0982 0.0075 57 GLN A CA 459 C C . GLN A 57 ? 0.2616 0.3565 0.2769 0.0157 -0.0902 -0.0010 57 GLN A C 460 O O . GLN A 57 ? 0.2717 0.3742 0.2910 0.0116 -0.0871 -0.0100 57 GLN A O 461 C CB . GLN A 57 ? 0.4674 0.5854 0.4837 0.0197 -0.1079 0.0142 57 GLN A CB 462 C CG . GLN A 57 ? 0.5482 0.6863 0.5748 0.0145 -0.1131 0.0085 57 GLN A CG 463 C CD . GLN A 57 ? 0.6395 0.7762 0.6422 0.0037 -0.1171 0.0016 57 GLN A CD 464 O OE1 . GLN A 57 ? 0.6287 0.7612 0.6097 0.0031 -0.1216 0.0063 57 GLN A OE1 465 N NE2 . GLN A 57 ? 0.6339 0.7705 0.6369 -0.0036 -0.1145 -0.0092 57 GLN A NE2 466 N N . GLY A 58 ? 0.2526 0.3290 0.2695 0.0215 -0.0873 0.0019 58 GLY A N 467 C CA . GLY A 58 ? 0.2511 0.3156 0.2717 0.0245 -0.0794 -0.0060 58 GLY A CA 468 C C . GLY A 58 ? 0.3094 0.3698 0.3222 0.0152 -0.0743 -0.0137 58 GLY A C 469 O O . GLY A 58 ? 0.3627 0.4228 0.3797 0.0155 -0.0678 -0.0218 58 GLY A O 470 N N . ALA A 59 ? 0.2508 0.3099 0.2538 0.0081 -0.0760 -0.0090 59 ALA A N 471 C CA . ALA A 59 ? 0.2855 0.3445 0.2836 0.0016 -0.0704 -0.0131 59 ALA A CA 472 C C . ALA A 59 ? 0.2794 0.3520 0.2776 0.0004 -0.0663 -0.0220 59 ALA A C 473 O O . ALA A 59 ? 0.2296 0.2995 0.2276 -0.0017 -0.0601 -0.0290 59 ALA A O 474 C CB . ALA A 59 ? 0.2449 0.3060 0.2367 -0.0034 -0.0713 -0.0020 59 ALA A CB 475 N N . LEU A 60 ? 0.2837 0.3676 0.2793 0.0008 -0.0714 -0.0211 60 LEU A N 476 C CA . LEU A 60 ? 0.3247 0.4150 0.3144 -0.0031 -0.0714 -0.0292 60 LEU A CA 477 C C . LEU A 60 ? 0.2914 0.3856 0.2967 -0.0044 -0.0699 -0.0363 60 LEU A C 478 O O . LEU A 60 ? 0.2962 0.3876 0.2972 -0.0092 -0.0660 -0.0440 60 LEU A O 479 C CB . LEU A 60 ? 0.3462 0.4444 0.3263 -0.0042 -0.0813 -0.0259 60 LEU A CB 480 C CG . LEU A 60 ? 0.4319 0.5242 0.3863 -0.0032 -0.0789 -0.0220 60 LEU A CG 481 C CD1 . LEU A 60 ? 0.4406 0.5327 0.3979 0.0007 -0.0760 -0.0094 60 LEU A CD1 482 C CD2 . LEU A 60 ? 0.4861 0.5807 0.4224 -0.0055 -0.0897 -0.0220 60 LEU A CD2 483 N N . ALA A 61 ? 0.2706 0.3705 0.2932 0.0012 -0.0716 -0.0322 61 ALA A N 484 C CA . ALA A 61 ? 0.2586 0.3665 0.2991 0.0026 -0.0675 -0.0352 61 ALA A CA 485 C C . ALA A 61 ? 0.2346 0.3277 0.2704 0.0028 -0.0567 -0.0417 61 ALA A C 486 O O . ALA A 61 ? 0.2379 0.3351 0.2795 -0.0010 -0.0521 -0.0467 61 ALA A O 487 C CB . ALA A 61 ? 0.2407 0.3562 0.2984 0.0137 -0.0680 -0.0270 61 ALA A CB 488 N N . ASN A 62 ? 0.1783 0.2537 0.2029 0.0059 -0.0543 -0.0405 62 ASN A N 489 C CA . ASN A 62 ? 0.2008 0.2612 0.2180 0.0049 -0.0470 -0.0452 62 ASN A CA 490 C C . ASN A 62 ? 0.2321 0.2946 0.2427 -0.0021 -0.0438 -0.0498 62 ASN A C 491 O O . ASN A 62 ? 0.1842 0.2423 0.1947 -0.0032 -0.0372 -0.0548 62 ASN A O 492 C CB . ASN A 62 ? 0.2276 0.2679 0.2328 0.0057 -0.0499 -0.0409 62 ASN A CB 493 C CG . ASN A 62 ? 0.2931 0.3149 0.2944 0.0148 -0.0483 -0.0408 62 ASN A CG 494 O OD1 . ASN A 62 ? 0.3592 0.3899 0.3717 0.0236 -0.0445 -0.0405 62 ASN A OD1 495 N ND2 . ASN A 62 ? 0.1817 0.1766 0.1659 0.0130 -0.0512 -0.0400 62 ASN A ND2 496 N N . ILE A 63 ? 0.1652 0.2319 0.1676 -0.0050 -0.0470 -0.0472 63 ILE A N 497 C CA . ILE A 63 ? 0.1355 0.1997 0.1270 -0.0078 -0.0417 -0.0507 63 ILE A CA 498 C C . ILE A 63 ? 0.1651 0.2301 0.1569 -0.0120 -0.0409 -0.0588 63 ILE A C 499 O O . ILE A 63 ? 0.1865 0.2432 0.1722 -0.0135 -0.0345 -0.0635 63 ILE A O 500 C CB . ILE A 63 ? 0.2995 0.3662 0.2778 -0.0065 -0.0427 -0.0450 63 ILE A CB 501 C CG1 . ILE A 63 ? 0.3098 0.3779 0.2914 -0.0053 -0.0431 -0.0337 63 ILE A CG1 502 C CG2 . ILE A 63 ? 0.2029 0.2624 0.1642 -0.0054 -0.0351 -0.0493 63 ILE A CG2 503 C CD1 . ILE A 63 ? 0.2676 0.3312 0.2534 -0.0066 -0.0388 -0.0317 63 ILE A CD1 504 N N . ALA A 64 ? 0.1424 0.2178 0.1429 -0.0146 -0.0486 -0.0587 64 ALA A N 505 C CA . ALA A 64 ? 0.1975 0.2763 0.2027 -0.0225 -0.0513 -0.0635 64 ALA A CA 506 C C . ALA A 64 ? 0.2034 0.2834 0.2237 -0.0219 -0.0429 -0.0648 64 ALA A C 507 O O . ALA A 64 ? 0.1908 0.2650 0.2088 -0.0284 -0.0399 -0.0692 64 ALA A O 508 C CB . ALA A 64 ? 0.1538 0.2500 0.1714 -0.0265 -0.0636 -0.0589 64 ALA A CB 509 N N . VAL A 65 ? 0.1526 0.2362 0.1842 -0.0137 -0.0386 -0.0608 65 VAL A N 510 C CA . VAL A 65 ? 0.2005 0.2813 0.2396 -0.0103 -0.0286 -0.0616 65 VAL A CA 511 C C . VAL A 65 ? 0.1268 0.1898 0.1493 -0.0114 -0.0222 -0.0663 65 VAL A C 512 O O . VAL A 65 ? 0.1496 0.2092 0.1734 -0.0139 -0.0155 -0.0686 65 VAL A O 513 C CB . VAL A 65 ? 0.2307 0.3096 0.2748 0.0014 -0.0249 -0.0573 65 VAL A CB 514 C CG1 . VAL A 65 ? 0.2329 0.3008 0.2735 0.0067 -0.0133 -0.0592 65 VAL A CG1 515 C CG2 . VAL A 65 ? 0.2102 0.3107 0.2757 0.0055 -0.0285 -0.0500 65 VAL A CG2 516 N N . ASP A 66 ? 0.1307 0.1850 0.1400 -0.0098 -0.0244 -0.0652 66 ASP A N 517 C CA . ASP A 66 ? 0.1530 0.1960 0.1507 -0.0099 -0.0193 -0.0657 66 ASP A CA 518 C C . ASP A 66 ? 0.1795 0.2184 0.1701 -0.0138 -0.0156 -0.0700 66 ASP A C 519 O O . ASP A 66 ? 0.1709 0.2011 0.1567 -0.0135 -0.0089 -0.0713 66 ASP A O 520 C CB . ASP A 66 ? 0.1264 0.1681 0.1175 -0.0083 -0.0231 -0.0593 66 ASP A CB 521 C CG . ASP A 66 ? 0.2013 0.2377 0.1936 -0.0067 -0.0285 -0.0551 66 ASP A CG 522 O OD1 . ASP A 66 ? 0.2065 0.2343 0.1986 -0.0039 -0.0263 -0.0583 66 ASP A OD1 523 O OD2 . ASP A 66 ? 0.2064 0.2445 0.1973 -0.0079 -0.0344 -0.0480 66 ASP A OD2 524 N N . LYS A 67 ? 0.1987 0.2399 0.1847 -0.0173 -0.0206 -0.0721 67 LYS A N 525 C CA . LYS A 67 ? 0.1576 0.1856 0.1287 -0.0218 -0.0189 -0.0777 67 LYS A CA 526 C C . LYS A 67 ? 0.1843 0.2105 0.1650 -0.0293 -0.0172 -0.0807 67 LYS A C 527 O O . LYS A 67 ? 0.1918 0.2025 0.1625 -0.0304 -0.0108 -0.0834 67 LYS A O 528 C CB . LYS A 67 ? 0.1977 0.2242 0.1564 -0.0256 -0.0280 -0.0798 67 LYS A CB 529 C CG . LYS A 67 ? 0.2665 0.2698 0.2017 -0.0321 -0.0299 -0.0862 67 LYS A CG 530 C CD . LYS A 67 ? 0.2255 0.2233 0.1430 -0.0350 -0.0408 -0.0861 67 LYS A CD 531 C CE . LYS A 67 ? 0.4709 0.4357 0.3567 -0.0384 -0.0450 -0.0918 67 LYS A CE 532 N NZ . LYS A 67 ? 0.5103 0.4527 0.3777 -0.0292 -0.0317 -0.0958 67 LYS A NZ 533 N N . ALA A 68 ? 0.1771 0.2208 0.1791 -0.0333 -0.0218 -0.0780 68 ALA A N 534 C CA . ALA A 68 ? 0.2499 0.2986 0.2668 -0.0404 -0.0190 -0.0767 68 ALA A CA 535 C C . ALA A 68 ? 0.2875 0.3303 0.3053 -0.0340 -0.0065 -0.0757 68 ALA A C 536 O O . ALA A 68 ? 0.2913 0.3265 0.3088 -0.0392 -0.0012 -0.0761 68 ALA A O 537 C CB . ALA A 68 ? 0.1774 0.2528 0.2217 -0.0427 -0.0243 -0.0698 68 ALA A CB 538 N N . ASN A 69 ? 0.2378 0.2811 0.2537 -0.0237 -0.0032 -0.0740 69 ASN A N 539 C CA . ASN A 69 ? 0.2336 0.2672 0.2435 -0.0181 0.0060 -0.0732 69 ASN A CA 540 C C . ASN A 69 ? 0.1435 0.1609 0.1371 -0.0186 0.0094 -0.0750 69 ASN A C 541 O O . ASN A 69 ? 0.1916 0.2010 0.1818 -0.0184 0.0168 -0.0742 69 ASN A O 542 C CB . ASN A 69 ? 0.1348 0.1657 0.1398 -0.0095 0.0048 -0.0713 69 ASN A CB 543 C CG . ASN A 69 ? 0.2381 0.2786 0.2554 -0.0035 0.0071 -0.0685 69 ASN A CG 544 O OD1 . ASN A 69 ? 0.2299 0.2857 0.2650 -0.0055 0.0108 -0.0656 69 ASN A OD1 545 N ND2 . ASN A 69 ? 0.1420 0.1729 0.1500 0.0042 0.0050 -0.0677 69 ASN A ND2 546 N N . LEU A 70 ? 0.1453 0.1584 0.1286 -0.0176 0.0055 -0.0757 70 LEU A N 547 C CA . LEU A 70 ? 0.2160 0.2156 0.1851 -0.0145 0.0108 -0.0749 70 LEU A CA 548 C C . LEU A 70 ? 0.2757 0.2603 0.2381 -0.0198 0.0154 -0.0787 70 LEU A C 549 O O . LEU A 70 ? 0.2531 0.2261 0.2083 -0.0168 0.0225 -0.0768 70 LEU A O 550 C CB . LEU A 70 ? 0.1849 0.1845 0.1443 -0.0098 0.0087 -0.0730 70 LEU A CB 551 C CG . LEU A 70 ? 0.2441 0.2318 0.1894 -0.0021 0.0169 -0.0696 70 LEU A CG 552 C CD1 . LEU A 70 ? 0.1813 0.1735 0.1327 0.0018 0.0198 -0.0618 70 LEU A CD1 553 C CD2 . LEU A 70 ? 0.2695 0.2603 0.2057 0.0055 0.0179 -0.0654 70 LEU A CD2 554 N N . GLU A 71 ? 0.1840 0.1676 0.1481 -0.0290 0.0098 -0.0830 71 GLU A N 555 C CA . GLU A 71 ? 0.2011 0.1672 0.1584 -0.0385 0.0108 -0.0859 71 GLU A CA 556 C C . GLU A 71 ? 0.3001 0.2707 0.2709 -0.0410 0.0181 -0.0815 71 GLU A C 557 O O . GLU A 71 ? 0.2115 0.1631 0.1719 -0.0422 0.0243 -0.0811 71 GLU A O 558 C CB . GLU A 71 ? 0.2129 0.1818 0.1737 -0.0519 -0.0011 -0.0888 71 GLU A CB 559 C CG . GLU A 71 ? 0.7018 0.6594 0.6651 -0.0675 -0.0037 -0.0885 71 GLU A CG 560 C CD . GLU A 71 ? 0.8698 0.8356 0.8412 -0.0840 -0.0195 -0.0883 71 GLU A CD 561 O OE1 . GLU A 71 ? 0.9386 0.9078 0.9247 -0.0999 -0.0241 -0.0835 71 GLU A OE1 562 O OE2 . GLU A 71 ? 0.8736 0.8439 0.8376 -0.0820 -0.0283 -0.0912 71 GLU A OE2 563 N N . ILE A 72 ? 0.1785 0.1720 0.1701 -0.0400 0.0185 -0.0774 72 ILE A N 564 C CA . ILE A 72 ? 0.1768 0.1762 0.1793 -0.0395 0.0278 -0.0719 72 ILE A CA 565 C C . ILE A 72 ? 0.3333 0.3180 0.3194 -0.0301 0.0358 -0.0709 72 ILE A C 566 O O . ILE A 72 ? 0.2418 0.2165 0.2243 -0.0320 0.0434 -0.0679 72 ILE A O 567 C CB . ILE A 72 ? 0.2622 0.2854 0.2842 -0.0347 0.0293 -0.0674 72 ILE A CB 568 C CG1 . ILE A 72 ? 0.2582 0.3021 0.3036 -0.0452 0.0220 -0.0636 72 ILE A CG1 569 C CG2 . ILE A 72 ? 0.2621 0.2856 0.2850 -0.0279 0.0424 -0.0620 72 ILE A CG2 570 C CD1 . ILE A 72 ? 0.3089 0.3783 0.3749 -0.0370 0.0236 -0.0576 72 ILE A CD1 571 N N A MET A 73 ? 0.2757 0.2603 0.2530 -0.0214 0.0329 -0.0717 73 MET A N 572 N N B MET A 73 ? 0.1701 0.1547 0.1474 -0.0213 0.0329 -0.0717 73 MET A N 573 C CA A MET A 73 ? 0.2380 0.2131 0.2022 -0.0141 0.0365 -0.0683 73 MET A CA 574 C CA B MET A 73 ? 0.2356 0.2105 0.1996 -0.0141 0.0365 -0.0683 73 MET A CA 575 C C A MET A 73 ? 0.2506 0.2105 0.2028 -0.0125 0.0396 -0.0668 73 MET A C 576 C C B MET A 73 ? 0.2513 0.2111 0.2037 -0.0126 0.0397 -0.0669 73 MET A C 577 O O A MET A 73 ? 0.2659 0.2172 0.2098 -0.0085 0.0445 -0.0621 73 MET A O 578 O O B MET A 73 ? 0.2677 0.2186 0.2118 -0.0089 0.0449 -0.0623 73 MET A O 579 C CB A MET A 73 ? 0.2217 0.2024 0.1826 -0.0088 0.0293 -0.0670 73 MET A CB 580 C CB B MET A 73 ? 0.2212 0.2016 0.1816 -0.0087 0.0291 -0.0668 73 MET A CB 581 C CG A MET A 73 ? 0.2465 0.2190 0.1942 -0.0045 0.0288 -0.0618 73 MET A CG 582 C CG B MET A 73 ? 0.2073 0.1944 0.1722 -0.0071 0.0262 -0.0681 73 MET A CG 583 S SD A MET A 73 ? 0.2510 0.2134 0.1884 -0.0023 0.0367 -0.0615 73 MET A SD 584 S SD B MET A 73 ? 0.3805 0.3610 0.3400 -0.0033 0.0370 -0.0668 73 MET A SD 585 C CE A MET A 73 ? 0.3753 0.3454 0.3204 -0.0001 0.0360 -0.0656 73 MET A CE 586 C CE B MET A 73 ? 0.3465 0.3095 0.2834 -0.0009 0.0365 -0.0630 73 MET A CE 587 N N . THR A 74 ? 0.1903 0.1445 0.1385 -0.0138 0.0371 -0.0704 74 THR A N 588 C CA . THR A 74 ? 0.2098 0.1436 0.1422 -0.0094 0.0425 -0.0695 74 THR A CA 589 C C . THR A 74 ? 0.3231 0.2396 0.2515 -0.0158 0.0484 -0.0695 74 THR A C 590 O O . THR A 74 ? 0.2820 0.1844 0.2003 -0.0098 0.0552 -0.0646 74 THR A O 591 C CB . THR A 74 ? 0.2520 0.1748 0.1723 -0.0091 0.0397 -0.0751 74 THR A CB 592 O OG1 . THR A 74 ? 0.2346 0.1751 0.1592 -0.0026 0.0357 -0.0726 74 THR A OG1 593 C CG2 . THR A 74 ? 0.2592 0.1545 0.1577 -0.0008 0.0474 -0.0737 74 THR A CG2 594 N N . LYS A 75 ? 0.3288 0.2487 0.2676 -0.0285 0.0453 -0.0726 75 LYS A N 595 C CA . LYS A 75 ? 0.3893 0.2978 0.3302 -0.0381 0.0500 -0.0699 75 LYS A CA 596 C C . LYS A 75 ? 0.3134 0.2290 0.2589 -0.0330 0.0588 -0.0624 75 LYS A C 597 O O . LYS A 75 ? 0.3340 0.2321 0.2701 -0.0330 0.0657 -0.0580 75 LYS A O 598 C CB . LYS A 75 ? 0.4692 0.3912 0.4285 -0.0537 0.0430 -0.0707 75 LYS A CB 599 C CG . LYS A 75 ? 0.6168 0.5240 0.5783 -0.0696 0.0432 -0.0672 75 LYS A CG 600 C CD . LYS A 75 ? 0.6659 0.5929 0.6499 -0.0864 0.0324 -0.0653 75 LYS A CD 601 C CE . LYS A 75 ? 0.7775 0.7006 0.7505 -0.0876 0.0194 -0.0743 75 LYS A CE 602 N NZ . LYS A 75 ? 0.8011 0.7440 0.7954 -0.1052 0.0056 -0.0711 75 LYS A NZ 603 N N . ARG A 76 ? 0.2806 0.2177 0.2359 -0.0279 0.0585 -0.0611 76 ARG A N 604 C CA . ARG A 76 ? 0.3131 0.2524 0.2646 -0.0217 0.0662 -0.0552 76 ARG A CA 605 C C . ARG A 76 ? 0.2498 0.1740 0.1826 -0.0133 0.0677 -0.0514 76 ARG A C 606 O O . ARG A 76 ? 0.2630 0.1789 0.1871 -0.0112 0.0748 -0.0455 76 ARG A O 607 C CB . ARG A 76 ? 0.2076 0.1630 0.1635 -0.0159 0.0641 -0.0564 76 ARG A CB 608 C CG . ARG A 76 ? 0.3573 0.3166 0.3132 -0.0124 0.0751 -0.0510 76 ARG A CG 609 C CD . ARG A 76 ? 0.2545 0.2177 0.2029 -0.0028 0.0743 -0.0530 76 ARG A CD 610 N NE . ARG A 76 ? 0.2522 0.2344 0.2216 -0.0038 0.0722 -0.0546 76 ARG A NE 611 C CZ . ARG A 76 ? 0.2455 0.2291 0.2102 0.0040 0.0687 -0.0575 76 ARG A CZ 612 N NH1 . ARG A 76 ? 0.2409 0.2050 0.1783 0.0110 0.0654 -0.0601 76 ARG A NH1 613 N NH2 . ARG A 76 ? 0.2540 0.2563 0.2397 0.0040 0.0671 -0.0570 76 ARG A NH2 614 N N . SER A 77 ? 0.1749 0.0813 0.1669 -0.0600 0.0044 0.0100 77 SER A N 615 C CA . SER A 77 ? 0.1793 0.0812 0.1487 -0.0602 0.0012 0.0078 77 SER A CA 616 C C . SER A 77 ? 0.2758 0.1682 0.2312 -0.0599 -0.0102 0.0070 77 SER A C 617 O O . SER A 77 ? 0.2778 0.1659 0.2182 -0.0593 -0.0151 0.0072 77 SER A O 618 C CB . SER A 77 ? 0.1751 0.0823 0.1444 -0.0549 0.0025 0.0081 77 SER A CB 619 O OG . SER A 77 ? 0.2940 0.1989 0.2635 -0.0497 -0.0053 0.0079 77 SER A OG 620 N N . ASN A 78 ? 0.2280 0.1168 0.1894 -0.0603 -0.0147 0.0065 78 ASN A N 621 C CA . ASN A 78 ? 0.2312 0.1105 0.1818 -0.0590 -0.0259 0.0056 78 ASN A CA 622 C C . ASN A 78 ? 0.2769 0.1547 0.2214 -0.0521 -0.0326 0.0039 78 ASN A C 623 O O . ASN A 78 ? 0.3264 0.1964 0.2603 -0.0498 -0.0396 0.0037 78 ASN A O 624 C CB . ASN A 78 ? 0.3295 0.2009 0.2673 -0.0636 -0.0286 0.0074 78 ASN A CB 625 C CG . ASN A 78 ? 0.4407 0.3126 0.3826 -0.0710 -0.0217 0.0080 78 ASN A CG 626 O OD1 . ASN A 78 ? 0.4376 0.3108 0.3925 -0.0722 -0.0196 0.0070 78 ASN A OD1 627 N ND2 . ASN A 78 ? 0.6177 0.4880 0.5478 -0.0767 -0.0184 0.0095 78 ASN A ND2 628 N N . TYR A 79 ? 0.2147 0.0970 0.1639 -0.0499 -0.0315 0.0037 79 TYR A N 629 C CA . TYR A 79 ? 0.2240 0.0994 0.1606 -0.0450 -0.0408 0.0024 79 TYR A CA 630 C C . TYR A 79 ? 0.2965 0.1691 0.2224 -0.0415 -0.0408 0.0026 79 TYR A C 631 O O . TYR A 79 ? 0.3562 0.2196 0.2720 -0.0361 -0.0496 0.0001 79 TYR A O 632 C CB . TYR A 79 ? 0.2137 0.0792 0.1438 -0.0431 -0.0528 -0.0014 79 TYR A CB 633 C CG . TYR A 79 ? 0.2164 0.0847 0.1552 -0.0478 -0.0553 -0.0013 79 TYR A CG 634 C CD1 . TYR A 79 ? 0.2787 0.1497 0.2279 -0.0528 -0.0506 -0.0003 79 TYR A CD1 635 C CD2 . TYR A 79 ? 0.2203 0.0895 0.1575 -0.0481 -0.0631 -0.0018 79 TYR A CD2 636 C CE1 . TYR A 79 ? 0.2695 0.1438 0.2284 -0.0577 -0.0531 0.0005 79 TYR A CE1 637 C CE2 . TYR A 79 ? 0.2799 0.1538 0.2267 -0.0544 -0.0679 0.0002 79 TYR A CE2 638 C CZ . TYR A 79 ? 0.2873 0.1634 0.2456 -0.0590 -0.0625 0.0016 79 TYR A CZ 639 O OH . TYR A 79 ? 0.3112 0.1932 0.2813 -0.0655 -0.0675 0.0044 79 TYR A OH 640 N N . THR A 80 ? 0.2019 0.0832 0.1323 -0.0444 -0.0305 0.0048 80 THR A N 641 C CA . THR A 80 ? 0.2250 0.1050 0.1453 -0.0431 -0.0304 0.0056 80 THR A CA 642 C C . THR A 80 ? 0.2311 0.1108 0.1481 -0.0389 -0.0294 0.0047 80 THR A C 643 O O . THR A 80 ? 0.2806 0.1688 0.2075 -0.0404 -0.0198 0.0061 80 THR A O 644 C CB . THR A 80 ? 0.2737 0.1634 0.1982 -0.0488 -0.0201 0.0070 80 THR A CB 645 O OG1 . THR A 80 ? 0.2572 0.1438 0.1805 -0.0534 -0.0219 0.0080 80 THR A OG1 646 C CG2 . THR A 80 ? 0.1976 0.0859 0.1098 -0.0498 -0.0210 0.0082 80 THR A CG2 647 N N . PRO A 81 ? 0.2768 0.1464 0.1817 -0.0321 -0.0386 0.0024 81 PRO A N 648 C CA . PRO A 81 ? 0.3084 0.1754 0.2071 -0.0258 -0.0385 -0.0004 81 PRO A CA 649 C C . PRO A 81 ? 0.2729 0.1454 0.1695 -0.0268 -0.0293 0.0019 81 PRO A C 650 O O . PRO A 81 ? 0.2725 0.1471 0.1684 -0.0333 -0.0265 0.0045 81 PRO A O 651 C CB . PRO A 81 ? 0.3008 0.1607 0.1914 -0.0151 -0.0502 -0.0072 81 PRO A CB 652 C CG . PRO A 81 ? 0.3096 0.1636 0.2013 -0.0174 -0.0544 -0.0044 81 PRO A CG 653 C CD . PRO A 81 ? 0.2211 0.0807 0.1200 -0.0281 -0.0491 0.0010 81 PRO A CD 654 N N . ILE A 82 ? 0.2543 0.1425 0.1550 -0.0181 -0.0229 0.0018 82 ILE A N 655 C CA . ILE A 82 ? 0.2469 0.1455 0.1483 -0.0173 -0.0128 0.0034 82 ILE A CA 656 C C . ILE A 82 ? 0.2775 0.1741 0.1707 -0.0109 -0.0206 0.0007 82 ILE A C 657 O O . ILE A 82 ? 0.2483 0.1398 0.1378 -0.0017 -0.0310 -0.0037 82 ILE A O 658 C CB . ILE A 82 ? 0.2617 0.1776 0.1710 -0.0091 -0.0036 0.0051 82 ILE A CB 659 C CG1 . ILE A 82 ? 0.2432 0.1681 0.1573 -0.0130 0.0112 0.0075 82 ILE A CG1 660 C CG2 . ILE A 82 ? 0.2941 0.2160 0.1967 0.0050 -0.0117 0.0004 82 ILE A CG2 661 C CD1 . ILE A 82 ? 0.1347 0.0745 0.0611 -0.0079 0.0233 0.0119 82 ILE A CD1 662 N N . THR A 83 ? 0.1974 0.0984 0.0892 -0.0168 -0.0151 0.0033 83 THR A N 663 C CA . THR A 83 ? 0.2061 0.1102 0.0948 -0.0104 -0.0214 0.0029 83 THR A CA 664 C C . THR A 83 ? 0.1940 0.1147 0.0868 -0.0001 -0.0132 0.0007 83 THR A C 665 O O . THR A 83 ? 0.2473 0.1776 0.1440 -0.0050 -0.0003 0.0023 83 THR A O 666 C CB . THR A 83 ? 0.3027 0.2059 0.1871 -0.0240 -0.0217 0.0082 83 THR A CB 667 O OG1 . THR A 83 ? 0.3534 0.2408 0.2328 -0.0336 -0.0298 0.0110 83 THR A OG1 668 C CG2 . THR A 83 ? 0.2842 0.1946 0.1697 -0.0167 -0.0288 0.0102 83 THR A CG2 669 N N . ASN A 84 ? 0.2155 0.1386 0.1084 0.0137 -0.0194 -0.0034 84 ASN A N 670 C CA . ASN A 84 ? 0.1998 0.1384 0.0956 0.0236 -0.0117 -0.0058 84 ASN A CA 671 C C . ASN A 84 ? 0.2676 0.2175 0.1666 0.0188 -0.0050 -0.0023 84 ASN A C 672 O O . ASN A 84 ? 0.2478 0.1955 0.1468 0.0147 -0.0118 0.0007 84 ASN A O 673 C CB . ASN A 84 ? 0.2455 0.1830 0.1407 0.0380 -0.0185 -0.0122 84 ASN A CB 674 C CG . ASN A 84 ? 0.3558 0.2845 0.2457 0.0417 -0.0239 -0.0178 84 ASN A CG 675 O OD1 . ASN A 84 ? 0.3825 0.3159 0.2706 0.0388 -0.0199 -0.0165 84 ASN A OD1 676 N ND2 . ASN A 84 ? 0.3086 0.2254 0.1976 0.0477 -0.0327 -0.0236 84 ASN A ND2 677 N N . VAL A 85 ? 0.2086 0.1712 0.1110 0.0185 0.0083 -0.0019 85 VAL A N 678 C CA . VAL A 85 ? 0.2363 0.2112 0.1420 0.0141 0.0160 -0.0003 85 VAL A CA 679 C C . VAL A 85 ? 0.2331 0.2219 0.1458 0.0265 0.0212 -0.0031 85 VAL A C 680 O O . VAL A 85 ? 0.2250 0.2199 0.1498 0.0258 0.0267 -0.0029 85 VAL A O 681 C CB . VAL A 85 ? 0.1937 0.1742 0.1085 -0.0012 0.0277 0.0019 85 VAL A CB 682 C CG1 . VAL A 85 ? 0.1200 0.1172 0.0452 -0.0049 0.0320 0.0024 85 VAL A CG1 683 C CG2 . VAL A 85 ? 0.1458 0.1118 0.0539 -0.0148 0.0241 0.0038 85 VAL A CG2 684 N N . PRO A 86 ? 0.1525 0.1469 0.0652 0.0351 0.0165 -0.0048 86 PRO A N 685 C CA . PRO A 86 ? 0.1333 0.1391 0.0553 0.0454 0.0206 -0.0078 86 PRO A CA 686 C C . PRO A 86 ? 0.1480 0.1647 0.0848 0.0349 0.0297 -0.0056 86 PRO A C 687 O O . PRO A 86 ? 0.1816 0.2003 0.1195 0.0229 0.0336 -0.0041 86 PRO A O 688 C CB . PRO A 86 ? 0.2633 0.2709 0.1856 0.0560 0.0130 -0.0101 86 PRO A CB 689 C CG . PRO A 86 ? 0.2462 0.2510 0.1700 0.0435 0.0056 -0.0035 86 PRO A CG 690 C CD . PRO A 86 ? 0.1450 0.1363 0.0598 0.0323 0.0048 -0.0019 86 PRO A CD 691 N N . PRO A 87 ? 0.1562 0.1772 0.1016 0.0372 0.0320 -0.0063 87 PRO A N 692 C CA . PRO A 87 ? 0.1578 0.1837 0.1142 0.0276 0.0384 -0.0060 87 PRO A CA 693 C C . PRO A 87 ? 0.1636 0.1968 0.1243 0.0272 0.0411 -0.0072 87 PRO A C 694 O O . PRO A 87 ? 0.1696 0.2082 0.1283 0.0374 0.0381 -0.0077 87 PRO A O 695 C CB . PRO A 87 ? 0.2126 0.2402 0.1695 0.0349 0.0384 -0.0040 87 PRO A CB 696 C CG . PRO A 87 ? 0.1197 0.1460 0.0696 0.0444 0.0329 -0.0074 87 PRO A CG 697 C CD . PRO A 87 ? 0.1237 0.1434 0.0652 0.0474 0.0281 -0.0082 87 PRO A CD 698 N N . GLU A 88 ? 0.2144 0.2505 0.1803 0.0188 0.0471 -0.0070 88 GLU A N 699 C CA . GLU A 88 ? 0.2410 0.2842 0.2118 0.0186 0.0509 -0.0080 88 GLU A CA 700 C C . GLU A 88 ? 0.1148 0.1608 0.0891 0.0243 0.0529 -0.0065 88 GLU A C 701 O O . GLU A 88 ? 0.2006 0.2436 0.1756 0.0230 0.0545 -0.0042 88 GLU A O 702 C CB . GLU A 88 ? 0.1129 0.1546 0.0851 0.0052 0.0567 -0.0097 88 GLU A CB 703 C CG . GLU A 88 ? 0.6288 0.6599 0.5926 0.0013 0.0557 -0.0062 88 GLU A CG 704 C CD . GLU A 88 ? 0.6712 0.7094 0.6371 0.0026 0.0580 0.0027 88 GLU A CD 705 O OE1 . GLU A 88 ? 0.5952 0.6431 0.5685 0.0026 0.0606 0.0034 88 GLU A OE1 706 O OE2 . GLU A 88 ? 0.7351 0.7782 0.6962 -0.0066 0.0548 0.0025 88 GLU A OE2 707 N N . VAL A 89 ? 0.1190 0.1711 0.0952 0.0308 0.0533 -0.0072 89 VAL A N 708 C CA . VAL A 89 ? 0.1249 0.1792 0.1016 0.0356 0.0557 -0.0055 89 VAL A CA 709 C C . VAL A 89 ? 0.1976 0.2585 0.1802 0.0333 0.0613 -0.0069 89 VAL A C 710 O O . VAL A 89 ? 0.2116 0.2781 0.1977 0.0340 0.0617 -0.0093 89 VAL A O 711 C CB . VAL A 89 ? 0.1690 0.2241 0.1403 0.0457 0.0518 -0.0063 89 VAL A CB 712 C CG1 . VAL A 89 ? 0.1389 0.1970 0.1085 0.0492 0.0553 -0.0045 89 VAL A CG1 713 C CG2 . VAL A 89 ? 0.2051 0.2535 0.1700 0.0475 0.0465 -0.0060 89 VAL A CG2 714 N N . THR A 90 ? 0.1359 0.1969 0.1206 0.0311 0.0660 -0.0050 90 THR A N 715 C CA A THR A 90 ? 0.1365 0.2038 0.1266 0.0285 0.0719 -0.0068 90 THR A CA 716 C CA B THR A 90 ? 0.1367 0.2041 0.1267 0.0289 0.0717 -0.0069 90 THR A CA 717 C C . THR A 90 ? 0.2251 0.2933 0.2134 0.0347 0.0744 -0.0031 90 THR A C 718 O O . THR A 90 ? 0.1944 0.2581 0.1797 0.0369 0.0739 0.0020 90 THR A O 719 C CB A THR A 90 ? 0.2042 0.2736 0.1989 0.0177 0.0761 -0.0090 90 THR A CB 720 C CB B THR A 90 ? 0.1780 0.2481 0.1729 0.0177 0.0761 -0.0098 90 THR A CB 721 O OG1 A THR A 90 ? 0.1282 0.1969 0.1217 0.0105 0.0734 -0.0120 90 THR A OG1 722 O OG1 B THR A 90 ? 0.1335 0.1984 0.1276 0.0165 0.0759 -0.0056 90 THR A OG1 723 C CG2 A THR A 90 ? 0.1387 0.2179 0.1389 0.0136 0.0815 -0.0130 90 THR A CG2 724 C CG2 B THR A 90 ? 0.1463 0.2164 0.1416 0.0103 0.0748 -0.0139 90 THR A CG2 725 N N . VAL A 91 ? 0.1785 0.2533 0.1691 0.0373 0.0778 -0.0052 91 VAL A N 726 C CA . VAL A 91 ? 0.2561 0.3331 0.2449 0.0418 0.0816 -0.0021 91 VAL A CA 727 C C . VAL A 91 ? 0.2146 0.2962 0.2104 0.0367 0.0885 -0.0033 91 VAL A C 728 O O . VAL A 91 ? 0.2509 0.3384 0.2523 0.0329 0.0905 -0.0087 91 VAL A O 729 C CB . VAL A 91 ? 0.2496 0.3310 0.2340 0.0494 0.0809 -0.0046 91 VAL A CB 730 C CG1 . VAL A 91 ? 0.2814 0.3669 0.2638 0.0522 0.0865 -0.0023 91 VAL A CG1 731 C CG2 . VAL A 91 ? 0.2006 0.2781 0.1771 0.0540 0.0746 -0.0044 91 VAL A CG2 732 N N . LEU A 92 ? 0.1961 0.2754 0.1922 0.0368 0.0925 0.0022 92 LEU A N 733 C CA . LEU A 92 ? 0.2279 0.3110 0.2302 0.0329 0.0994 0.0018 92 LEU A CA 734 C C . LEU A 92 ? 0.2481 0.3291 0.2489 0.0381 0.1042 0.0096 92 LEU A C 735 O O . LEU A 92 ? 0.2767 0.3545 0.2719 0.0436 0.1018 0.0154 92 LEU A O 736 C CB . LEU A 92 ? 0.3090 0.3900 0.3161 0.0249 0.1003 0.0007 92 LEU A CB 737 C CG . LEU A 92 ? 0.3476 0.4165 0.3555 0.0234 0.1007 0.0063 92 LEU A CG 738 C CD1 . LEU A 92 ? 0.4158 0.4759 0.4233 0.0300 0.1035 0.0158 92 LEU A CD1 739 C CD2 . LEU A 92 ? 0.4512 0.5171 0.4648 0.0164 0.1062 0.0050 92 LEU A CD2 740 N N . THR A 93 ? 0.1920 0.2763 0.1979 0.0362 0.1111 0.0100 93 THR A N 741 C CA . THR A 93 ? 0.3217 0.4036 0.3276 0.0408 0.1169 0.0185 93 THR A CA 742 C C . THR A 93 ? 0.3518 0.4227 0.3647 0.0383 0.1219 0.0247 93 THR A C 743 O O . THR A 93 ? 0.2024 0.2696 0.2202 0.0318 0.1228 0.0202 93 THR A O 744 C CB . THR A 93 ? 0.2124 0.3030 0.2198 0.0414 0.1230 0.0162 93 THR A CB 745 O OG1 . THR A 93 ? 0.2121 0.3055 0.2273 0.0347 0.1269 0.0112 93 THR A OG1 746 C CG2 . THR A 93 ? 0.2125 0.3116 0.2145 0.0444 0.1199 0.0095 93 THR A CG2 747 N N . ASN A 94 ? 0.2139 0.2797 0.2280 0.0437 0.1258 0.0352 94 ASN A N 748 C CA . ASN A 94 ? 0.2840 0.3362 0.3075 0.0430 0.1323 0.0423 94 ASN A CA 749 C C . ASN A 94 ? 0.2683 0.3165 0.3002 0.0404 0.1425 0.0427 94 ASN A C 750 O O . ASN A 94 ? 0.2821 0.3158 0.3236 0.0381 0.1497 0.0453 94 ASN A O 751 C CB . ASN A 94 ? 0.4820 0.5327 0.5058 0.0511 0.1320 0.0550 94 ASN A CB 752 C CG . ASN A 94 ? 0.6488 0.6879 0.6854 0.0538 0.1417 0.0657 94 ASN A CG 753 O OD1 . ASN A 94 ? 0.7666 0.7909 0.8124 0.0506 0.1459 0.0654 94 ASN A OD1 754 N ND2 . ASN A 94 ? 0.6761 0.7217 0.7142 0.0599 0.1462 0.0754 94 ASN A ND2 755 N N . SER A 95 ? 0.2775 0.3373 0.3065 0.0401 0.1440 0.0387 95 SER A N 756 C CA . SER A 95 ? 0.3226 0.3804 0.3590 0.0367 0.1534 0.0374 95 SER A CA 757 C C . SER A 95 ? 0.3130 0.3871 0.3459 0.0336 0.1514 0.0276 95 SER A C 758 O O . SER A 95 ? 0.2441 0.3290 0.2695 0.0358 0.1445 0.0235 95 SER A O 759 C CB . SER A 95 ? 0.3571 0.4105 0.3983 0.0431 0.1618 0.0494 95 SER A CB 760 O OG . SER A 95 ? 0.5208 0.5878 0.5534 0.0488 0.1588 0.0526 95 SER A OG 761 N N . PRO A 96 ? 0.3230 0.3981 0.3624 0.0284 0.1582 0.0236 96 PRO A N 762 C CA . PRO A 96 ? 0.2891 0.3822 0.3270 0.0265 0.1569 0.0155 96 PRO A CA 763 C C . PRO A 96 ? 0.3261 0.4279 0.3587 0.0328 0.1573 0.0178 96 PRO A C 764 O O . PRO A 96 ? 0.3757 0.4718 0.4081 0.0374 0.1628 0.0269 96 PRO A O 765 C CB . PRO A 96 ? 0.2792 0.3695 0.3257 0.0212 0.1663 0.0142 96 PRO A CB 766 C CG . PRO A 96 ? 0.3096 0.3801 0.3611 0.0170 0.1699 0.0161 96 PRO A CG 767 C CD . PRO A 96 ? 0.3107 0.3703 0.3596 0.0236 0.1675 0.0248 96 PRO A CD 768 N N . VAL A 97 ? 0.2470 0.3625 0.2761 0.0331 0.1525 0.0097 97 VAL A N 769 C CA . VAL A 97 ? 0.2892 0.4107 0.3120 0.0386 0.1534 0.0099 97 VAL A CA 770 C C . VAL A 97 ? 0.2923 0.4231 0.3188 0.0383 0.1619 0.0086 97 VAL A C 771 O O . VAL A 97 ? 0.3376 0.4781 0.3709 0.0342 0.1637 0.0017 97 VAL A O 772 C CB . VAL A 97 ? 0.3283 0.4559 0.3473 0.0397 0.1465 0.0015 97 VAL A CB 773 C CG1 . VAL A 97 ? 0.3703 0.5025 0.3823 0.0451 0.1491 0.0009 97 VAL A CG1 774 C CG2 . VAL A 97 ? 0.2975 0.4160 0.3122 0.0403 0.1383 0.0035 97 VAL A CG2 775 N N . GLU A 98 ? 0.2894 0.4189 0.3111 0.0428 0.1671 0.0158 98 GLU A N 776 C CA . GLU A 98 ? 0.3519 0.4906 0.3749 0.0430 0.1755 0.0147 98 GLU A CA 777 C C . GLU A 98 ? 0.3647 0.5091 0.3770 0.0475 0.1760 0.0142 98 GLU A C 778 O O . GLU A 98 ? 0.3528 0.4920 0.3566 0.0512 0.1728 0.0210 98 GLU A O 779 C CB . GLU A 98 ? 0.4412 0.5726 0.4693 0.0431 0.1841 0.0250 98 GLU A CB 780 C CG . GLU A 98 ? 0.6561 0.7790 0.6945 0.0380 0.1860 0.0247 98 GLU A CG 781 C CD . GLU A 98 ? 0.9136 1.0243 0.9587 0.0390 0.1959 0.0354 98 GLU A CD 782 O OE1 . GLU A 98 ? 0.9693 1.0716 1.0124 0.0442 0.1967 0.0464 98 GLU A OE1 783 O OE2 . GLU A 98 ? 1.0044 1.1142 1.0579 0.0348 0.2034 0.0333 98 GLU A OE2 784 N N . LEU A 99 ? 0.3254 0.4812 0.3382 0.0469 0.1805 0.0057 99 LEU A N 785 C CA . LEU A 99 ? 0.3686 0.5296 0.3706 0.0498 0.1830 0.0029 99 LEU A CA 786 C C . LEU A 99 ? 0.4189 0.5784 0.4110 0.0522 0.1876 0.0143 99 LEU A C 787 O O . LEU A 99 ? 0.3977 0.5568 0.3941 0.0516 0.1938 0.0223 99 LEU A O 788 C CB . LEU A 99 ? 0.4091 0.5827 0.4159 0.0483 0.1902 -0.0077 99 LEU A CB 789 C CG . LEU A 99 ? 0.4826 0.6610 0.4991 0.0475 0.1861 -0.0195 99 LEU A CG 790 C CD1 . LEU A 99 ? 0.4487 0.6413 0.4725 0.0470 0.1942 -0.0293 99 LEU A CD1 791 C CD2 . LEU A 99 ? 0.5363 0.7075 0.5454 0.0506 0.1795 -0.0225 99 LEU A CD2 792 N N . ARG A 100 ? 0.4973 0.6565 0.4763 0.0546 0.1845 0.0153 100 ARG A N 793 C CA . ARG A 100 ? 0.5274 0.6883 0.4949 0.0564 0.1875 0.0267 100 ARG A CA 794 C C . ARG A 100 ? 0.5022 0.6567 0.4769 0.0585 0.1873 0.0423 100 ARG A C 795 O O . ARG A 100 ? 0.5119 0.6703 0.4826 0.0598 0.1928 0.0535 100 ARG A O 796 C CB . ARG A 100 ? 0.6446 0.8159 0.6039 0.0541 0.1983 0.0234 100 ARG A CB 797 C CG . ARG A 100 ? 0.7549 0.9304 0.7238 0.0522 0.2074 0.0259 100 ARG A CG 798 C CD . ARG A 100 ? 0.8187 1.0053 0.7793 0.0490 0.2174 0.0172 100 ARG A CD 799 N NE . ARG A 100 ? 0.8451 1.0351 0.8111 0.0479 0.2170 0.0006 100 ARG A NE 800 C CZ . ARG A 100 ? 0.8635 1.0586 0.8448 0.0468 0.2191 -0.0065 100 ARG A CZ 801 N NH1 . ARG A 100 ? 0.9089 1.1047 0.9000 0.0460 0.2222 0.0004 100 ARG A NH1 802 N NH2 . ARG A 100 ? 0.8141 1.0141 0.8017 0.0468 0.2186 -0.0203 100 ARG A NH2 803 N N . GLU A 101 ? 0.5428 0.6874 0.5284 0.0585 0.1816 0.0428 101 GLU A N 804 C CA . GLU A 101 ? 0.4807 0.6159 0.4743 0.0608 0.1813 0.0561 101 GLU A CA 805 C C . GLU A 101 ? 0.4225 0.5523 0.4130 0.0630 0.1713 0.0579 101 GLU A C 806 O O . GLU A 101 ? 0.3643 0.4896 0.3564 0.0608 0.1649 0.0487 101 GLU A O 807 C CB . GLU A 101 ? 0.4397 0.5660 0.4482 0.0576 0.1848 0.0545 101 GLU A CB 808 C CG . GLU A 101 ? 0.6066 0.7371 0.6206 0.0555 0.1953 0.0545 101 GLU A CG 809 C CD . GLU A 101 ? 0.7195 0.8508 0.7334 0.0595 0.2030 0.0695 101 GLU A CD 810 O OE1 . GLU A 101 ? 0.7426 0.8670 0.7599 0.0637 0.2013 0.0818 101 GLU A OE1 811 O OE2 . GLU A 101 ? 0.7968 0.9366 0.8084 0.0585 0.2110 0.0697 101 GLU A OE2 812 N N . PRO A 102 ? 0.3893 0.3515 0.3057 0.1072 0.0840 0.0653 102 PRO A N 813 C CA . PRO A 102 ? 0.3925 0.3549 0.3063 0.1058 0.0796 0.0618 102 PRO A CA 814 C C . PRO A 102 ? 0.3514 0.3137 0.2660 0.0994 0.0761 0.0566 102 PRO A C 815 O O . PRO A 102 ? 0.3363 0.2970 0.2520 0.0960 0.0768 0.0549 102 PRO A O 816 C CB . PRO A 102 ? 0.2977 0.2585 0.2093 0.1086 0.0800 0.0632 102 PRO A CB 817 C CG . PRO A 102 ? 0.3506 0.3114 0.2628 0.1134 0.0849 0.0684 102 PRO A CG 818 C CD . PRO A 102 ? 0.3674 0.3281 0.2831 0.1115 0.0874 0.0693 102 PRO A CD 819 N N . ASN A 103 ? 0.3203 0.2841 0.2343 0.0976 0.0728 0.0539 103 ASN A N 820 C CA . ASN A 103 ? 0.2599 0.2243 0.1747 0.0915 0.0697 0.0488 103 ASN A CA 821 C C . ASN A 103 ? 0.2761 0.2410 0.1891 0.0909 0.0661 0.0464 103 ASN A C 822 O O . ASN A 103 ? 0.2427 0.2078 0.1539 0.0950 0.0661 0.0485 103 ASN A O 823 C CB . ASN A 103 ? 0.3387 0.3058 0.2561 0.0891 0.0701 0.0482 103 ASN A CB 824 C CG . ASN A 103 ? 0.3624 0.3305 0.2809 0.0821 0.0686 0.0431 103 ASN A CG 825 O OD1 . ASN A 103 ? 0.3836 0.3509 0.3009 0.0784 0.0659 0.0391 103 ASN A OD1 826 N ND2 . ASN A 103 ? 0.3032 0.2733 0.2241 0.0799 0.0708 0.0430 103 ASN A ND2 827 N N . VAL A 104 ? 0.2780 0.2436 0.1916 0.0855 0.0633 0.0419 104 VAL A N 828 C CA . VAL A 104 ? 0.2372 0.2034 0.1497 0.0846 0.0601 0.0397 104 VAL A CA 829 C C . VAL A 104 ? 0.2630 0.2313 0.1769 0.0806 0.0581 0.0366 104 VAL A C 830 O O . VAL A 104 ? 0.2298 0.1987 0.1449 0.0755 0.0579 0.0335 104 VAL A O 831 C CB . VAL A 104 ? 0.2832 0.2475 0.1945 0.0822 0.0587 0.0372 104 VAL A CB 832 C CG1 . VAL A 104 ? 0.2358 0.2014 0.1465 0.0812 0.0557 0.0349 104 VAL A CG1 833 C CG2 . VAL A 104 ? 0.3035 0.2660 0.2134 0.0865 0.0607 0.0404 104 VAL A CG2 834 N N . LEU A 105 ? 0.2571 0.2266 0.1706 0.0825 0.0570 0.0372 105 LEU A N 835 C CA . LEU A 105 ? 0.2257 0.1971 0.1404 0.0790 0.0549 0.0344 105 LEU A CA 836 C C . LEU A 105 ? 0.2556 0.2267 0.1698 0.0751 0.0522 0.0305 105 LEU A C 837 O O . LEU A 105 ? 0.2732 0.2435 0.1859 0.0770 0.0514 0.0309 105 LEU A O 838 C CB . LEU A 105 ? 0.3231 0.2953 0.2374 0.0826 0.0554 0.0368 105 LEU A CB 839 C CG . LEU A 105 ? 0.4013 0.3743 0.3167 0.0853 0.0582 0.0401 105 LEU A CG 840 C CD1 . LEU A 105 ? 0.4085 0.3807 0.3225 0.0895 0.0597 0.0429 105 LEU A CD1 841 C CD2 . LEU A 105 ? 0.3396 0.3154 0.2576 0.0812 0.0574 0.0379 105 LEU A CD2 842 N N . ILE A 106 ? 0.2845 0.2568 0.1999 0.0695 0.0510 0.0267 106 ILE A N 843 C CA . ILE A 106 ? 0.2410 0.2131 0.1561 0.0652 0.0489 0.0228 106 ILE A CA 844 C C . ILE A 106 ? 0.2310 0.2052 0.1470 0.0633 0.0473 0.0212 106 ILE A C 845 O O . ILE A 106 ? 0.2266 0.2030 0.1439 0.0615 0.0477 0.0206 106 ILE A O 846 C CB . ILE A 106 ? 0.2523 0.2235 0.1674 0.0594 0.0495 0.0192 106 ILE A CB 847 C CG1 . ILE A 106 ? 0.3371 0.3057 0.2511 0.0615 0.0515 0.0212 106 ILE A CG1 848 C CG2 . ILE A 106 ? 0.2255 0.1962 0.1400 0.0551 0.0479 0.0155 106 ILE A CG2 849 C CD1 . ILE A 106 ? 0.3516 0.3186 0.2652 0.0558 0.0530 0.0177 106 ILE A CD1 850 N N . CYS A 107 ? 0.1632 0.1373 0.0787 0.0636 0.0457 0.0205 107 CYS A N 851 C CA . CYS A 107 ? 0.2311 0.2066 0.1473 0.0613 0.0444 0.0186 107 CYS A CA 852 C C . CYS A 107 ? 0.2017 0.1771 0.1179 0.0555 0.0432 0.0143 107 CYS A C 853 O O . CYS A 107 ? 0.1713 0.1457 0.0867 0.0556 0.0426 0.0138 107 CYS A O 854 C CB . CYS A 107 ? 0.1623 0.1374 0.0775 0.0655 0.0440 0.0208 107 CYS A CB 855 S SG . CYS A 107 ? 0.2082 0.1844 0.1240 0.0634 0.0428 0.0191 107 CYS A SG 856 N N . PHE A 108 ? 0.1674 0.1444 0.0843 0.0503 0.0432 0.0112 108 PHE A N 857 C CA . PHE A 108 ? 0.1689 0.1460 0.0855 0.0441 0.0428 0.0069 108 PHE A CA 858 C C . PHE A 108 ? 0.2422 0.2207 0.1592 0.0424 0.0415 0.0054 108 PHE A C 859 O O . PHE A 108 ? 0.2810 0.2616 0.1987 0.0416 0.0415 0.0052 108 PHE A O 860 C CB . PHE A 108 ? 0.1849 0.1631 0.1012 0.0385 0.0441 0.0037 108 PHE A CB 861 C CG . PHE A 108 ? 0.2441 0.2224 0.1594 0.0318 0.0443 -0.0009 108 PHE A CG 862 C CD1 . PHE A 108 ? 0.2675 0.2434 0.1822 0.0316 0.0441 -0.0015 108 PHE A CD1 863 C CD2 . PHE A 108 ? 0.2356 0.2172 0.1505 0.0257 0.0448 -0.0046 108 PHE A CD2 864 C CE1 . PHE A 108 ? 0.2950 0.2711 0.2087 0.0259 0.0446 -0.0054 108 PHE A CE1 865 C CE2 . PHE A 108 ? 0.2118 0.1940 0.1255 0.0200 0.0451 -0.0086 108 PHE A CE2 866 C CZ . PHE A 108 ? 0.2298 0.2088 0.1429 0.0203 0.0452 -0.0088 108 PHE A CZ 867 N N . ILE A 109 ? 0.2465 0.2239 0.1631 0.0418 0.0407 0.0044 109 ILE A N 868 C CA . ILE A 109 ? 0.2108 0.1891 0.1276 0.0403 0.0397 0.0032 109 ILE A CA 869 C C . ILE A 109 ? 0.1668 0.1455 0.0831 0.0337 0.0400 -0.0011 109 ILE A C 870 O O . ILE A 109 ? 0.2036 0.1811 0.1195 0.0326 0.0403 -0.0021 109 ILE A O 871 C CB . ILE A 109 ? 0.2131 0.1904 0.1296 0.0446 0.0389 0.0053 109 ILE A CB 872 C CG1 . ILE A 109 ? 0.3198 0.2965 0.2360 0.0510 0.0393 0.0095 109 ILE A CG1 873 C CG2 . ILE A 109 ? 0.1776 0.1554 0.0942 0.0430 0.0382 0.0040 109 ILE A CG2 874 C CD1 . ILE A 109 ? 0.4631 0.4389 0.3785 0.0541 0.0397 0.0113 109 ILE A CD1 875 N N . ASP A 110 ? 0.1566 0.1375 0.0729 0.0294 0.0401 -0.0036 110 ASP A N 876 C CA . ASP A 110 ? 0.1469 0.1292 0.0623 0.0228 0.0408 -0.0079 110 ASP A CA 877 C C . ASP A 110 ? 0.1622 0.1464 0.0773 0.0196 0.0402 -0.0100 110 ASP A C 878 O O . ASP A 110 ? 0.1734 0.1583 0.0890 0.0215 0.0396 -0.0086 110 ASP A O 879 C CB . ASP A 110 ? 0.1479 0.1326 0.0628 0.0197 0.0418 -0.0094 110 ASP A CB 880 C CG . ASP A 110 ? 0.1500 0.1356 0.0633 0.0143 0.0427 -0.0131 110 ASP A CG 881 O OD1 . ASP A 110 ? 0.2414 0.2247 0.1541 0.0136 0.0429 -0.0140 110 ASP A OD1 882 O OD2 . ASP A 110 ? 0.2953 0.2836 0.2074 0.0115 0.0433 -0.0147 110 ASP A OD2 883 N N . LYS A 111 ? 0.1943 0.1792 0.1085 0.0154 0.0406 -0.0130 111 LYS A N 884 C CA . LYS A 111 ? 0.2163 0.2031 0.1295 0.0123 0.0403 -0.0151 111 LYS A CA 885 C C . LYS A 111 ? 0.1782 0.1641 0.0922 0.0144 0.0395 -0.0139 111 LYS A C 886 O O . LYS A 111 ? 0.1751 0.1625 0.0888 0.0138 0.0391 -0.0140 111 LYS A O 887 C CB . LYS A 111 ? 0.2586 0.2491 0.1707 0.0101 0.0403 -0.0162 111 LYS A CB 888 C CG . LYS A 111 ? 0.3602 0.3508 0.2705 0.0080 0.0413 -0.0174 111 LYS A CG 889 C CD . LYS A 111 ? 0.4882 0.4834 0.3976 0.0070 0.0411 -0.0177 111 LYS A CD 890 C CE . LYS A 111 ? 0.5456 0.5391 0.4525 0.0050 0.0424 -0.0185 111 LYS A CE 891 N NZ . LYS A 111 ? 0.6120 0.6100 0.5173 0.0043 0.0422 -0.0184 111 LYS A NZ 892 N N . PHE A 112 ? 0.2234 0.2068 0.1381 0.0169 0.0392 -0.0126 112 PHE A N 893 C CA . PHE A 112 ? 0.1859 0.1683 0.1010 0.0192 0.0385 -0.0113 112 PHE A CA 894 C C . PHE A 112 ? 0.2224 0.2043 0.1374 0.0181 0.0385 -0.0126 112 PHE A C 895 O O . PHE A 112 ? 0.1864 0.1681 0.1013 0.0170 0.0390 -0.0135 112 PHE A O 896 C CB . PHE A 112 ? 0.1634 0.1440 0.0792 0.0254 0.0379 -0.0074 112 PHE A CB 897 C CG . PHE A 112 ? 0.2143 0.1937 0.1303 0.0284 0.0378 -0.0058 112 PHE A CG 898 C CD1 . PHE A 112 ? 0.1722 0.1514 0.0883 0.0290 0.0383 -0.0052 112 PHE A CD1 899 C CD2 . PHE A 112 ? 0.2319 0.2107 0.1479 0.0307 0.0374 -0.0050 112 PHE A CD2 900 C CE1 . PHE A 112 ? 0.2256 0.2037 0.1417 0.0320 0.0383 -0.0036 112 PHE A CE1 901 C CE2 . PHE A 112 ? 0.2112 0.1897 0.1272 0.0336 0.0373 -0.0035 112 PHE A CE2 902 C CZ . PHE A 112 ? 0.2129 0.1909 0.1289 0.0345 0.0377 -0.0027 112 PHE A CZ 903 N N . THR A 113 ? 0.2439 0.2255 0.1588 0.0185 0.0382 -0.0125 113 THR A N 904 C CA . THR A 113 ? 0.1448 0.1265 0.0598 0.0180 0.0382 -0.0134 113 THR A CA 905 C C . THR A 113 ? 0.1969 0.1778 0.1117 0.0198 0.0378 -0.0123 113 THR A C 906 O O . THR A 113 ? 0.1998 0.1801 0.1140 0.0200 0.0378 -0.0118 113 THR A O 907 C CB . THR A 113 ? 0.2398 0.2223 0.1539 0.0136 0.0388 -0.0164 113 THR A CB 908 O OG1 . THR A 113 ? 0.1653 0.1482 0.0798 0.0135 0.0390 -0.0171 113 THR A OG1 909 C CG2 . THR A 113 ? 0.1710 0.1535 0.0839 0.0116 0.0389 -0.0174 113 THR A CG2 910 N N . PRO A 114 ? 0.2672 0.2480 0.1821 0.0213 0.0377 -0.0120 114 PRO A N 911 C CA . PRO A 114 ? 0.1768 0.1588 0.0923 0.0215 0.0377 -0.0125 114 PRO A CA 912 C C . PRO A 114 ? 0.2046 0.1859 0.1203 0.0254 0.0374 -0.0101 114 PRO A C 913 O O . PRO A 114 ? 0.2188 0.1989 0.1344 0.0284 0.0371 -0.0078 114 PRO A O 914 C CB . PRO A 114 ? 0.2286 0.2112 0.1439 0.0224 0.0376 -0.0126 114 PRO A CB 915 C CG . PRO A 114 ? 0.2163 0.1970 0.1307 0.0246 0.0376 -0.0109 114 PRO A CG 916 C CD . PRO A 114 ? 0.2223 0.2021 0.1365 0.0228 0.0377 -0.0112 114 PRO A CD 917 N N . PRO A 115 ? 0.2302 0.2124 0.1461 0.0255 0.0375 -0.0105 115 PRO A N 918 C CA . PRO A 115 ? 0.1457 0.1274 0.0616 0.0294 0.0372 -0.0081 115 PRO A CA 919 C C . PRO A 115 ? 0.2163 0.1986 0.1318 0.0342 0.0366 -0.0058 115 PRO A C 920 O O . PRO A 115 ? 0.2095 0.1934 0.1248 0.0359 0.0365 -0.0054 115 PRO A O 921 C CB . PRO A 115 ? 0.1460 0.1285 0.0620 0.0276 0.0378 -0.0097 115 PRO A CB 922 C CG . PRO A 115 ? 0.1457 0.1300 0.0619 0.0245 0.0380 -0.0122 115 PRO A CG 923 C CD . PRO A 115 ? 0.1451 0.1290 0.0613 0.0221 0.0380 -0.0132 115 PRO A CD 924 N N . VAL A 116 ? 0.2289 0.2100 0.1439 0.0362 0.0365 -0.0042 116 VAL A N 925 C CA . VAL A 116 ? 0.2806 0.2620 0.1945 0.0406 0.0366 -0.0021 116 VAL A CA 926 C C . VAL A 116 ? 0.2558 0.2352 0.1691 0.0436 0.0368 0.0004 116 VAL A C 927 O O . VAL A 116 ? 0.2231 0.2012 0.1366 0.0422 0.0369 0.0001 116 VAL A O 928 C CB . VAL A 116 ? 0.3511 0.3331 0.2641 0.0396 0.0370 -0.0034 116 VAL A CB 929 C CG1 . VAL A 116 ? 0.2171 0.1993 0.1282 0.0436 0.0377 -0.0016 116 VAL A CG1 930 C CG2 . VAL A 116 ? 0.2779 0.2623 0.1915 0.0364 0.0369 -0.0060 116 VAL A CG2 931 N N . VAL A 117 ? 0.2476 0.2270 0.1603 0.0478 0.0370 0.0029 117 VAL A N 932 C CA . VAL A 117 ? 0.3063 0.2840 0.2184 0.0509 0.0376 0.0054 117 VAL A CA 933 C C . VAL A 117 ? 0.2994 0.2771 0.2095 0.0557 0.0386 0.0079 117 VAL A C 934 O O . VAL A 117 ? 0.2908 0.2703 0.2005 0.0569 0.0385 0.0079 117 VAL A O 935 C CB . VAL A 117 ? 0.2605 0.2379 0.1741 0.0500 0.0373 0.0057 117 VAL A CB 936 C CG1 . VAL A 117 ? 0.1831 0.1610 0.0965 0.0527 0.0374 0.0073 117 VAL A CG1 937 C CG2 . VAL A 117 ? 0.4007 0.3768 0.3143 0.0512 0.0377 0.0073 117 VAL A CG2 938 N N . ASN A 118 ? 0.2510 0.2268 0.1597 0.0583 0.0399 0.0098 118 ASN A N 939 C CA . ASN A 118 ? 0.2994 0.2747 0.2058 0.0626 0.0417 0.0122 118 ASN A CA 940 C C . ASN A 118 ? 0.3002 0.2743 0.2073 0.0651 0.0421 0.0148 118 ASN A C 941 O O . ASN A 118 ? 0.2659 0.2385 0.1736 0.0649 0.0423 0.0155 118 ASN A O 942 C CB . ASN A 118 ? 0.2798 0.2533 0.1832 0.0637 0.0438 0.0124 118 ASN A CB 943 C CG . ASN A 118 ? 0.3838 0.3589 0.2862 0.0612 0.0438 0.0095 118 ASN A CG 944 O OD1 . ASN A 118 ? 0.4280 0.4062 0.3310 0.0604 0.0428 0.0083 118 ASN A OD1 945 N ND2 . ASN A 118 ? 0.4854 0.4586 0.3861 0.0600 0.0452 0.0085 118 ASN A ND2 946 N N . VAL A 119 ? 0.3388 0.3138 0.2456 0.0675 0.0424 0.0164 119 VAL A N 947 C CA . VAL A 119 ? 0.2615 0.2355 0.1690 0.0697 0.0431 0.0188 119 VAL A CA 948 C C . VAL A 119 ? 0.2766 0.2499 0.1814 0.0743 0.0456 0.0216 119 VAL A C 949 O O . VAL A 119 ? 0.2745 0.2492 0.1778 0.0755 0.0460 0.0216 119 VAL A O 950 C CB . VAL A 119 ? 0.3396 0.3148 0.2492 0.0681 0.0417 0.0182 119 VAL A CB 951 C CG1 . VAL A 119 ? 0.2134 0.1878 0.1236 0.0701 0.0427 0.0206 119 VAL A CG1 952 C CG2 . VAL A 119 ? 0.2727 0.2484 0.1844 0.0629 0.0399 0.0150 119 VAL A CG2 953 N N . THR A 120 ? 0.2516 0.2229 0.1558 0.0766 0.0476 0.0240 120 THR A N 954 C CA . THR A 120 ? 0.3079 0.2779 0.2093 0.0807 0.0508 0.0267 120 THR A CA 955 C C . THR A 120 ? 0.3419 0.3112 0.2446 0.0829 0.0518 0.0296 120 THR A C 956 O O . THR A 120 ? 0.2777 0.2466 0.1823 0.0821 0.0514 0.0300 120 THR A O 957 C CB . THR A 120 ? 0.3293 0.2967 0.2274 0.0818 0.0538 0.0271 120 THR A CB 958 O OG1 . THR A 120 ? 0.3517 0.3200 0.2487 0.0792 0.0529 0.0241 120 THR A OG1 959 C CG2 . THR A 120 ? 0.2474 0.2135 0.1420 0.0854 0.0579 0.0293 120 THR A CG2 960 N N . TRP A 121 ? 0.2983 0.2680 0.2001 0.0856 0.0533 0.0315 121 TRP A N 961 C CA . TRP A 121 ? 0.2621 0.2309 0.1646 0.0881 0.0552 0.0346 121 TRP A CA 962 C C . TRP A 121 ? 0.3138 0.2801 0.2135 0.0914 0.0596 0.0372 121 TRP A C 963 O O . TRP A 121 ? 0.3421 0.3076 0.2383 0.0926 0.0619 0.0370 121 TRP A O 964 C CB . TRP A 121 ? 0.2313 0.2013 0.1341 0.0896 0.0554 0.0357 121 TRP A CB 965 C CG . TRP A 121 ? 0.1943 0.1657 0.0999 0.0866 0.0523 0.0339 121 TRP A CG 966 C CD1 . TRP A 121 ? 0.2944 0.2671 0.2001 0.0852 0.0503 0.0320 121 TRP A CD1 967 C CD2 . TRP A 121 ? 0.1842 0.1558 0.0926 0.0845 0.0514 0.0336 121 TRP A CD2 968 N NE1 . TRP A 121 ? 0.1806 0.1535 0.0887 0.0822 0.0486 0.0306 121 TRP A NE1 969 C CE2 . TRP A 121 ? 0.2854 0.2577 0.1951 0.0814 0.0493 0.0312 121 TRP A CE2 970 C CE3 . TRP A 121 ? 0.2254 0.1969 0.1353 0.0846 0.0525 0.0349 121 TRP A CE3 971 C CZ2 . TRP A 121 ? 0.2331 0.2057 0.1450 0.0779 0.0485 0.0297 121 TRP A CZ2 972 C CZ3 . TRP A 121 ? 0.2260 0.1988 0.1385 0.0814 0.0514 0.0334 121 TRP A CZ3 973 C CH2 . TRP A 121 ? 0.3271 0.3002 0.2402 0.0778 0.0495 0.0306 121 TRP A CH2 974 N N . LEU A 122 ? 0.2989 0.2641 0.2001 0.0926 0.0611 0.0395 122 LEU A N 975 C CA . LEU A 122 ? 0.3092 0.2714 0.2080 0.0958 0.0661 0.0424 122 LEU A CA 976 C C . LEU A 122 ? 0.3006 0.2629 0.2007 0.0987 0.0687 0.0460 122 LEU A C 977 O O . LEU A 122 ? 0.2999 0.2642 0.2036 0.0977 0.0667 0.0465 122 LEU A O 978 C CB . LEU A 122 ? 0.2834 0.2439 0.1826 0.0952 0.0666 0.0425 122 LEU A CB 979 C CG . LEU A 122 ? 0.3156 0.2754 0.2134 0.0925 0.0647 0.0392 122 LEU A CG 980 C CD1 . LEU A 122 ? 0.2114 0.1701 0.1105 0.0919 0.0647 0.0397 122 LEU A CD1 981 C CD2 . LEU A 122 ? 0.2795 0.2368 0.1725 0.0934 0.0683 0.0386 122 LEU A CD2 982 N N . ARG A 123 ? 0.2475 0.2077 0.1446 0.1018 0.0734 0.0484 123 ARG A N 983 C CA . ARG A 123 ? 0.2329 0.1927 0.1313 0.1048 0.0770 0.0523 123 ARG A CA 984 C C . ARG A 123 ? 0.2634 0.2197 0.1600 0.1073 0.0828 0.0550 123 ARG A C 985 O O . ARG A 123 ? 0.2825 0.2362 0.1748 0.1081 0.0864 0.0544 123 ARG A O 986 C CB . ARG A 123 ? 0.2642 0.2247 0.1607 0.1066 0.0785 0.0531 123 ARG A CB 987 C CG . ARG A 123 ? 0.3782 0.3380 0.2758 0.1099 0.0830 0.0574 123 ARG A CG 988 C CD . ARG A 123 ? 0.4693 0.4295 0.3642 0.1119 0.0852 0.0581 123 ARG A CD 989 N NE . ARG A 123 ? 0.7136 0.6766 0.6096 0.1104 0.0806 0.0561 123 ARG A NE 990 C CZ . ARG A 123 ? 0.8787 0.8427 0.7746 0.1123 0.0816 0.0577 123 ARG A CZ 991 N NH1 . ARG A 123 ? 0.9481 0.9110 0.8429 0.1155 0.0871 0.0613 123 ARG A NH1 992 N NH2 . ARG A 123 ? 0.8618 0.8279 0.7587 0.1109 0.0776 0.0560 123 ARG A NH2 993 N N . ASN A 124 ? 0.2566 0.1627 0.1518 0.0406 0.0935 0.0136 124 ASN A N 994 C CA . ASN A 124 ? 0.3799 0.2829 0.2772 0.0403 0.0975 0.0118 124 ASN A CA 995 C C . ASN A 124 ? 0.3727 0.2785 0.2662 0.0381 0.0944 0.0043 124 ASN A C 996 O O . ASN A 124 ? 0.3981 0.3041 0.2871 0.0393 0.0967 0.0010 124 ASN A O 997 C CB . ASN A 124 ? 0.3754 0.2775 0.2667 0.0447 0.1026 0.0143 124 ASN A CB 998 C CG . ASN A 124 ? 0.3849 0.2841 0.2812 0.0472 0.1060 0.0216 124 ASN A CG 999 O OD1 . ASN A 124 ? 0.3224 0.2180 0.2300 0.0453 0.1067 0.0246 124 ASN A OD1 1000 N ND2 . ASN A 124 ? 0.3208 0.2216 0.2092 0.0516 0.1082 0.0243 124 ASN A ND2 1001 N N . GLY A 125 ? 0.3409 0.2492 0.2366 0.0349 0.0891 0.0015 125 GLY A N 1002 C CA . GLY A 125 ? 0.3319 0.2427 0.2261 0.0327 0.0857 -0.0055 125 GLY A CA 1003 C C . GLY A 125 ? 0.3389 0.2555 0.2213 0.0345 0.0818 -0.0105 125 GLY A C 1004 O O . GLY A 125 ? 0.3070 0.2260 0.1880 0.0330 0.0788 -0.0171 125 GLY A O 1005 N N . LYS A 126 ? 0.2451 0.1641 0.1197 0.0376 0.0817 -0.0075 126 LYS A N 1006 C CA . LYS A 126 ? 0.2792 0.2042 0.1426 0.0392 0.0780 -0.0116 126 LYS A CA 1007 C C . LYS A 126 ? 0.3112 0.2398 0.1722 0.0389 0.0731 -0.0097 126 LYS A C 1008 O O . LYS A 126 ? 0.3928 0.3196 0.2571 0.0398 0.0743 -0.0035 126 LYS A O 1009 C CB . LYS A 126 ? 0.2959 0.2217 0.1505 0.0432 0.0822 -0.0100 126 LYS A CB 1010 C CG . LYS A 126 ? 0.3234 0.2459 0.1794 0.0440 0.0877 -0.0117 126 LYS A CG 1011 C CD . LYS A 126 ? 0.3961 0.3205 0.2419 0.0480 0.0913 -0.0105 126 LYS A CD 1012 C CE . LYS A 126 ? 0.5272 0.4483 0.3738 0.0491 0.0972 -0.0121 126 LYS A CE 1013 N NZ . LYS A 126 ? 0.5836 0.5074 0.4192 0.0531 0.1005 -0.0114 126 LYS A NZ 1014 N N . PRO A 127 ? 0.3622 0.2960 0.2181 0.0377 0.0675 -0.0151 127 PRO A N 1015 C CA . PRO A 127 ? 0.2998 0.2373 0.1535 0.0373 0.0625 -0.0136 127 PRO A CA 1016 C C . PRO A 127 ? 0.3401 0.2792 0.1870 0.0410 0.0642 -0.0083 127 PRO A C 1017 O O . PRO A 127 ? 0.3604 0.3011 0.1993 0.0435 0.0665 -0.0090 127 PRO A O 1018 C CB . PRO A 127 ? 0.3579 0.3007 0.2069 0.0356 0.0570 -0.0211 127 PRO A CB 1019 C CG . PRO A 127 ? 0.4030 0.3437 0.2558 0.0341 0.0585 -0.0266 127 PRO A CG 1020 C CD . PRO A 127 ? 0.3217 0.2580 0.1750 0.0364 0.0655 -0.0232 127 PRO A CD 1021 N N . VAL A 128 ? 0.3537 0.2924 0.2040 0.0413 0.0632 -0.0031 128 VAL A N 1022 C CA . VAL A 128 ? 0.4302 0.3705 0.2754 0.0448 0.0646 0.0023 128 VAL A CA 1023 C C . VAL A 128 ? 0.4770 0.4212 0.3210 0.0442 0.0593 0.0030 128 VAL A C 1024 O O . VAL A 128 ? 0.5063 0.4499 0.3569 0.0414 0.0563 0.0022 128 VAL A O 1025 C CB . VAL A 128 ? 0.4537 0.3889 0.3056 0.0468 0.0702 0.0093 128 VAL A CB 1026 C CG1 . VAL A 128 ? 0.6331 0.5646 0.4854 0.0480 0.0757 0.0092 128 VAL A CG1 1027 C CG2 . VAL A 128 ? 0.3709 0.3029 0.2338 0.0440 0.0694 0.0108 128 VAL A CG2 1028 N N . THR A 129 ? 0.5515 0.4998 0.3870 0.0468 0.0581 0.0046 129 THR A N 1029 C CA . THR A 129 ? 0.5969 0.5493 0.4309 0.0464 0.0531 0.0052 129 THR A CA 1030 C C . THR A 129 ? 0.5954 0.5490 0.4266 0.0503 0.0550 0.0121 129 THR A C 1031 O O . THR A 129 ? 0.6083 0.5646 0.4397 0.0505 0.0516 0.0140 129 THR A O 1032 C CB . THR A 129 ? 0.6116 0.5691 0.4376 0.0449 0.0478 -0.0009 129 THR A CB 1033 O OG1 . THR A 129 ? 0.5794 0.5392 0.3952 0.0477 0.0497 -0.0009 129 THR A OG1 1034 C CG2 . THR A 129 ? 0.6891 0.6458 0.5185 0.0412 0.0460 -0.0079 129 THR A CG2 1035 N N . THR A 130 ? 0.6056 0.5572 0.4349 0.0536 0.0605 0.0160 130 THR A N 1036 C CA . THR A 130 ? 0.6428 0.5958 0.4701 0.0577 0.0629 0.0228 130 THR A CA 1037 C C . THR A 130 ? 0.5417 0.4921 0.3794 0.0579 0.0639 0.0278 130 THR A C 1038 O O . THR A 130 ? 0.5821 0.5275 0.4285 0.0573 0.0675 0.0295 130 THR A O 1039 C CB . THR A 130 ? 0.6381 0.5894 0.4622 0.0613 0.0690 0.0261 130 THR A CB 1040 O OG1 . THR A 130 ? 0.7056 0.6602 0.5188 0.0615 0.0681 0.0214 130 THR A OG1 1041 C CG2 . THR A 130 ? 0.6444 0.5971 0.4682 0.0657 0.0718 0.0338 130 THR A CG2 1042 N N . GLY A 131 ? 0.5168 0.4707 0.3537 0.0585 0.0606 0.0299 131 GLY A N 1043 C CA . GLY A 131 ? 0.4988 0.4510 0.3449 0.0591 0.0618 0.0347 131 GLY A CA 1044 C C . GLY A 131 ? 0.4889 0.4393 0.3427 0.0549 0.0587 0.0316 131 GLY A C 1045 O O . GLY A 131 ? 0.4873 0.4363 0.3489 0.0549 0.0596 0.0349 131 GLY A O 1046 N N . VAL A 132 ? 0.3504 0.3010 0.2024 0.0513 0.0552 0.0253 132 VAL A N 1047 C CA . VAL A 132 ? 0.3727 0.3218 0.2319 0.0473 0.0524 0.0223 132 VAL A CA 1048 C C . VAL A 132 ? 0.3418 0.2947 0.2007 0.0466 0.0476 0.0224 132 VAL A C 1049 O O . VAL A 132 ? 0.4194 0.3767 0.2713 0.0483 0.0450 0.0229 132 VAL A O 1050 C CB . VAL A 132 ? 0.3474 0.2961 0.2054 0.0437 0.0499 0.0156 132 VAL A CB 1051 C CG1 . VAL A 132 ? 0.2903 0.2351 0.1494 0.0442 0.0548 0.0155 132 VAL A CG1 1052 C CG2 . VAL A 132 ? 0.4221 0.3761 0.2713 0.0433 0.0450 0.0112 132 VAL A CG2 1053 N N . SER A 133 ? 0.3258 0.2768 0.1925 0.0441 0.0467 0.0221 133 SER A N 1054 C CA . SER A 133 ? 0.3050 0.2592 0.1726 0.0430 0.0423 0.0218 133 SER A CA 1055 C C . SER A 133 ? 0.3539 0.3063 0.2281 0.0387 0.0402 0.0183 133 SER A C 1056 O O . SER A 133 ? 0.3168 0.2655 0.1955 0.0369 0.0427 0.0169 133 SER A O 1057 C CB . SER A 133 ? 0.2853 0.2395 0.1560 0.0461 0.0448 0.0280 133 SER A CB 1058 O OG . SER A 133 ? 0.4009 0.3505 0.2808 0.0459 0.0495 0.0307 133 SER A OG 1059 N N . GLU A 134 ? 0.3310 0.2861 0.2059 0.0372 0.0358 0.0169 134 GLU A N 1060 C CA . GLU A 134 ? 0.2912 0.2456 0.1717 0.0331 0.0334 0.0134 134 GLU A CA 1061 C C . GLU A 134 ? 0.3098 0.2667 0.1921 0.0326 0.0302 0.0141 134 GLU A C 1062 O O . GLU A 134 ? 0.3712 0.3313 0.2495 0.0350 0.0284 0.0162 134 GLU A O 1063 C CB . GLU A 134 ? 0.2066 0.1627 0.0845 0.0304 0.0296 0.0075 134 GLU A CB 1064 C CG . GLU A 134 ? 0.2409 0.2023 0.1131 0.0305 0.0242 0.0051 134 GLU A CG 1065 C CD . GLU A 134 ? 0.2997 0.2629 0.1698 0.0282 0.0211 -0.0007 134 GLU A CD 1066 O OE1 . GLU A 134 ? 0.3334 0.2958 0.1991 0.0293 0.0232 -0.0018 134 GLU A OE1 1067 O OE2 . GLU A 134 ? 0.3817 0.3471 0.2548 0.0252 0.0167 -0.0042 134 GLU A OE2 1068 N N . THR A 135 ? 0.2621 0.2175 0.1506 0.0295 0.0295 0.0125 135 THR A N 1069 C CA . THR A 135 ? 0.2010 0.1587 0.0914 0.0286 0.0264 0.0125 135 THR A CA 1070 C C . THR A 135 ? 0.2856 0.2470 0.1746 0.0257 0.0204 0.0074 135 THR A C 1071 O O . THR A 135 ? 0.2459 0.2075 0.1341 0.0240 0.0191 0.0038 135 THR A O 1072 C CB . THR A 135 ? 0.1929 0.1473 0.0907 0.0267 0.0291 0.0135 135 THR A CB 1073 O OG1 . THR A 135 ? 0.2593 0.2126 0.1605 0.0227 0.0282 0.0095 135 THR A OG1 1074 C CG2 . THR A 135 ? 0.2097 0.1602 0.1111 0.0290 0.0354 0.0182 135 THR A CG2 1075 N N . VAL A 136 ? 0.3217 0.2861 0.2115 0.0254 0.0168 0.0074 136 VAL A N 1076 C CA . VAL A 136 ? 0.2674 0.2352 0.1586 0.0222 0.0114 0.0028 136 VAL A CA 1077 C C . VAL A 136 ? 0.2357 0.2013 0.1333 0.0186 0.0121 0.0007 136 VAL A C 1078 O O . VAL A 136 ? 0.2040 0.1655 0.1042 0.0185 0.0167 0.0025 136 VAL A O 1079 C CB . VAL A 136 ? 0.2589 0.2306 0.1498 0.0229 0.0074 0.0037 136 VAL A CB 1080 C CG1 . VAL A 136 ? 0.2768 0.2512 0.1614 0.0261 0.0062 0.0058 136 VAL A CG1 1081 C CG2 . VAL A 136 ? 0.1874 0.1570 0.0817 0.0237 0.0100 0.0070 136 VAL A CG2 1082 N N . PHE A 137 ? 0.2054 0.1741 0.1060 0.0155 0.0077 -0.0029 137 PHE A N 1083 C CA . PHE A 137 ? 0.2348 0.2024 0.1415 0.0120 0.0078 -0.0048 137 PHE A CA 1084 C C . PHE A 137 ? 0.2232 0.1897 0.1323 0.0118 0.0091 -0.0028 137 PHE A C 1085 O O . PHE A 137 ? 0.3010 0.2701 0.2093 0.0128 0.0067 -0.0020 137 PHE A O 1086 C CB . PHE A 137 ? 0.2805 0.2523 0.1906 0.0089 0.0029 -0.0089 137 PHE A CB 1087 C CG . PHE A 137 ? 0.2364 0.2084 0.1446 0.0088 0.0023 -0.0115 137 PHE A CG 1088 C CD1 . PHE A 137 ? 0.1471 0.1163 0.0576 0.0073 0.0046 -0.0128 137 PHE A CD1 1089 C CD2 . PHE A 137 ? 0.2172 0.1921 0.1211 0.0102 -0.0002 -0.0126 137 PHE A CD2 1090 C CE1 . PHE A 137 ? 0.2388 0.2078 0.1474 0.0074 0.0044 -0.0154 137 PHE A CE1 1091 C CE2 . PHE A 137 ? 0.2949 0.2699 0.1967 0.0100 -0.0004 -0.0154 137 PHE A CE2 1092 C CZ . PHE A 137 ? 0.3514 0.3234 0.2556 0.0087 0.0020 -0.0170 137 PHE A CZ 1093 N N . LEU A 138 ? 0.1441 0.1068 0.0565 0.0103 0.0132 -0.0022 138 LEU A N 1094 C CA . LEU A 138 ? 0.1511 0.1129 0.0676 0.0098 0.0153 -0.0005 138 LEU A CA 1095 C C . LEU A 138 ? 0.1911 0.1556 0.1152 0.0050 0.0129 -0.0036 138 LEU A C 1096 O O . LEU A 138 ? 0.1485 0.1127 0.0749 0.0022 0.0127 -0.0056 138 LEU A O 1097 C CB . LEU A 138 ? 0.1921 0.1495 0.1113 0.0110 0.0215 0.0027 138 LEU A CB 1098 C CG . LEU A 138 ? 0.2110 0.1660 0.1231 0.0159 0.0245 0.0064 138 LEU A CG 1099 C CD1 . LEU A 138 ? 0.2533 0.2036 0.1691 0.0166 0.0308 0.0093 138 LEU A CD1 1100 C CD2 . LEU A 138 ? 0.2277 0.1846 0.1365 0.0194 0.0235 0.0094 138 LEU A CD2 1101 N N . PRO A 139 ? 0.1526 0.1200 0.0808 0.0041 0.0113 -0.0038 139 PRO A N 1102 C CA . PRO A 139 ? 0.1529 0.1239 0.0873 -0.0001 0.0088 -0.0066 139 PRO A CA 1103 C C . PRO A 139 ? 0.2923 0.2621 0.2334 -0.0031 0.0120 -0.0070 139 PRO A C 1104 O O . PRO A 139 ? 0.3029 0.2695 0.2460 -0.0019 0.0162 -0.0052 139 PRO A O 1105 C CB . PRO A 139 ? 0.1371 0.1113 0.0731 0.0007 0.0069 -0.0062 139 PRO A CB 1106 C CG . PRO A 139 ? 0.1459 0.1171 0.0801 0.0046 0.0105 -0.0028 139 PRO A CG 1107 C CD . PRO A 139 ? 0.1093 0.0773 0.0366 0.0073 0.0119 -0.0011 139 PRO A CD 1108 N N . ARG A 140 ? 0.2149 0.1875 0.1599 -0.0070 0.0100 -0.0093 140 ARG A N 1109 C CA . ARG A 140 ? 0.1491 0.1220 0.1005 -0.0103 0.0120 -0.0101 140 ARG A CA 1110 C C . ARG A 140 ? 0.1863 0.1644 0.1420 -0.0131 0.0097 -0.0120 140 ARG A C 1111 O O . ARG A 140 ? 0.1672 0.1488 0.1216 -0.0131 0.0061 -0.0127 140 ARG A O 1112 C CB . ARG A 140 ? 0.1554 0.1279 0.1085 -0.0128 0.0120 -0.0106 140 ARG A CB 1113 C CG . ARG A 140 ? 0.0861 0.0532 0.0364 -0.0104 0.0156 -0.0087 140 ARG A CG 1114 C CD . ARG A 140 ? 0.2616 0.2286 0.2139 -0.0126 0.0152 -0.0092 140 ARG A CD 1115 N NE . ARG A 140 ? 0.2358 0.2064 0.1952 -0.0170 0.0143 -0.0103 140 ARG A NE 1116 C CZ . ARG A 140 ? 0.1996 0.1688 0.1640 -0.0187 0.0171 -0.0097 140 ARG A CZ 1117 N NH1 . ARG A 140 ? 0.1343 0.0984 0.0982 -0.0163 0.0214 -0.0080 140 ARG A NH1 1118 N NH2 . ARG A 140 ? 0.1505 0.1239 0.1207 -0.0227 0.0157 -0.0108 140 ARG A NH2 1119 N N . GLU A 141 ? 0.0951 0.0736 0.0558 -0.0154 0.0118 -0.0130 141 GLU A N 1120 C CA . GLU A 141 ? 0.2018 0.1854 0.1661 -0.0179 0.0102 -0.0151 141 GLU A CA 1121 C C . GLU A 141 ? 0.1596 0.1486 0.1253 -0.0212 0.0066 -0.0161 141 GLU A C 1122 O O . GLU A 141 ? 0.1664 0.1604 0.1340 -0.0228 0.0046 -0.0172 141 GLU A O 1123 C CB . GLU A 141 ? 0.2252 0.2081 0.1944 -0.0196 0.0134 -0.0166 141 GLU A CB 1124 C CG . GLU A 141 ? 0.3040 0.2821 0.2735 -0.0163 0.0172 -0.0154 141 GLU A CG 1125 C CD . GLU A 141 ? 0.4138 0.3912 0.3893 -0.0181 0.0204 -0.0175 141 GLU A CD 1126 O OE1 . GLU A 141 ? 0.4820 0.4638 0.4601 -0.0211 0.0192 -0.0206 141 GLU A OE1 1127 O OE2 . GLU A 141 ? 0.4949 0.4673 0.4726 -0.0164 0.0242 -0.0162 141 GLU A OE2 1128 N N . ASP A 142 ? 0.1255 0.1135 0.0909 -0.0221 0.0060 -0.0153 142 ASP A N 1129 C CA . ASP A 142 ? 0.1041 0.0973 0.0732 -0.0239 0.0027 -0.0146 142 ASP A CA 1130 C C . ASP A 142 ? 0.1719 0.1653 0.1388 -0.0215 -0.0001 -0.0139 142 ASP A C 1131 O O . ASP A 142 ? 0.1367 0.1333 0.1074 -0.0219 -0.0023 -0.0129 142 ASP A O 1132 C CB . ASP A 142 ? 0.1348 0.1277 0.1070 -0.0261 0.0037 -0.0139 142 ASP A CB 1133 C CG . ASP A 142 ? 0.1929 0.1791 0.1611 -0.0250 0.0057 -0.0137 142 ASP A CG 1134 O OD1 . ASP A 142 ? 0.1602 0.1431 0.1233 -0.0216 0.0060 -0.0134 142 ASP A OD1 1135 O OD2 . ASP A 142 ? 0.2448 0.2298 0.2161 -0.0266 0.0072 -0.0130 142 ASP A OD2 1136 N N . HIS A 143 ? 0.0886 0.0783 0.0492 -0.0188 0.0003 -0.0143 143 HIS A N 1137 C CA . HIS A 143 ? 0.1196 0.1102 0.0781 -0.0162 -0.0027 -0.0140 143 HIS A CA 1138 C C . HIS A 143 ? 0.1925 0.1808 0.1493 -0.0154 -0.0033 -0.0140 143 HIS A C 1139 O O . HIS A 143 ? 0.2276 0.2175 0.1845 -0.0137 -0.0061 -0.0144 143 HIS A O 1140 C CB . HIS A 143 ? 0.1315 0.1280 0.0958 -0.0165 -0.0058 -0.0138 143 HIS A CB 1141 C CG . HIS A 143 ? 0.1974 0.1964 0.1638 -0.0178 -0.0046 -0.0141 143 HIS A CG 1142 N ND1 . HIS A 143 ? 0.1928 0.1896 0.1549 -0.0168 -0.0030 -0.0149 143 HIS A ND1 1143 C CD2 . HIS A 143 ? 0.1281 0.1314 0.1001 -0.0198 -0.0044 -0.0138 143 HIS A CD2 1144 C CE1 . HIS A 143 ? 0.1444 0.1441 0.1099 -0.0185 -0.0019 -0.0158 143 HIS A CE1 1145 N NE2 . HIS A 143 ? 0.1498 0.1535 0.1210 -0.0201 -0.0029 -0.0150 143 HIS A NE2 1146 N N . LEU A 144 ? 0.1675 0.1519 0.1230 -0.0167 -0.0004 -0.0139 144 LEU A N 1147 C CA . LEU A 144 ? 0.1291 0.1093 0.0806 -0.0155 0.0006 -0.0141 144 LEU A CA 1148 C C . LEU A 144 ? 0.1716 0.1470 0.1159 -0.0115 0.0033 -0.0131 144 LEU A C 1149 O O . LEU A 144 ? 0.1405 0.1163 0.0834 -0.0099 0.0035 -0.0124 144 LEU A O 1150 C CB . LEU A 144 ? 0.1379 0.1167 0.0934 -0.0180 0.0030 -0.0137 144 LEU A CB 1151 C CG . LEU A 144 ? 0.1439 0.1279 0.1068 -0.0220 0.0007 -0.0138 144 LEU A CG 1152 C CD1 . LEU A 144 ? 0.1614 0.1440 0.1287 -0.0242 0.0033 -0.0127 144 LEU A CD1 1153 C CD2 . LEU A 144 ? 0.1175 0.1040 0.0829 -0.0212 -0.0026 -0.0141 144 LEU A CD2 1154 N N . PHE A 145 ? 0.1971 0.1682 0.1375 -0.0096 0.0055 -0.0128 145 PHE A N 1155 C CA . PHE A 145 ? 0.1684 0.1357 0.1018 -0.0053 0.0081 -0.0112 145 PHE A CA 1156 C C . PHE A 145 ? 0.1831 0.1455 0.1161 -0.0042 0.0134 -0.0092 145 PHE A C 1157 O O . PHE A 145 ? 0.1192 0.0807 0.0566 -0.0065 0.0147 -0.0095 145 PHE A O 1158 C CB . PHE A 145 ? 0.1837 0.1524 0.1123 -0.0027 0.0051 -0.0122 145 PHE A CB 1159 C CG . PHE A 145 ? 0.1964 0.1708 0.1271 -0.0028 0.0002 -0.0133 145 PHE A CG 1160 C CD1 . PHE A 145 ? 0.1516 0.1303 0.0883 -0.0052 -0.0034 -0.0154 145 PHE A CD1 1161 C CD2 . PHE A 145 ? 0.1793 0.1546 0.1065 -0.0003 -0.0003 -0.0119 145 PHE A CD2 1162 C CE1 . PHE A 145 ? 0.1086 0.0928 0.0484 -0.0051 -0.0073 -0.0161 145 PHE A CE1 1163 C CE2 . PHE A 145 ? 0.1486 0.1291 0.0782 -0.0006 -0.0045 -0.0127 145 PHE A CE2 1164 C CZ . PHE A 145 ? 0.2241 0.2093 0.1603 -0.0030 -0.0079 -0.0149 145 PHE A CZ 1165 N N . ARG A 146 ? 0.1642 0.1238 0.0924 -0.0004 0.0163 -0.0069 146 ARG A N 1166 C CA A ARG A 146 ? 0.1982 0.1530 0.1256 0.0016 0.0218 -0.0042 146 ARG A CA 1167 C CA B ARG A 146 ? 0.1756 0.1304 0.1027 0.0014 0.0215 -0.0046 146 ARG A CA 1168 C C . ARG A 146 ? 0.2059 0.1594 0.1250 0.0062 0.0224 -0.0028 146 ARG A C 1169 O O . ARG A 146 ? 0.1907 0.1475 0.1065 0.0078 0.0189 -0.0031 146 ARG A O 1170 C CB A ARG A 146 ? 0.2084 0.1620 0.1404 0.0020 0.0250 -0.0017 146 ARG A CB 1171 C CB B ARG A 146 ? 0.1901 0.1432 0.1238 0.0005 0.0253 -0.0024 146 ARG A CB 1172 C CG A ARG A 146 ? 0.2433 0.1981 0.1845 -0.0022 0.0254 -0.0027 146 ARG A CG 1173 C CG B ARG A 146 ? 0.2199 0.1756 0.1570 -0.0001 0.0240 -0.0025 146 ARG A CG 1174 C CD A ARG A 146 ? 0.2050 0.1587 0.1503 -0.0013 0.0283 -0.0010 146 ARG A CD 1175 C CD B ARG A 146 ? 0.2327 0.1861 0.1768 -0.0010 0.0282 -0.0009 146 ARG A CD 1176 N NE A ARG A 146 ? 0.1853 0.1415 0.1283 0.0002 0.0259 -0.0011 146 ARG A NE 1177 N NE B ARG A 146 ? 0.2740 0.2239 0.2159 0.0032 0.0324 0.0027 146 ARG A NE 1178 C CZ A ARG A 146 ? 0.2412 0.1958 0.1829 0.0037 0.0282 0.0017 146 ARG A CZ 1179 C CZ B ARG A 146 ? 0.1985 0.1454 0.1465 0.0035 0.0369 0.0047 146 ARG A CZ 1180 N NH1 A ARG A 146 ? 0.2185 0.1689 0.1609 0.0062 0.0332 0.0050 146 ARG A NH1 1181 N NH1 B ARG A 146 ? 0.1828 0.1269 0.1291 0.0076 0.0407 0.0087 146 ARG A NH1 1182 N NH2 A ARG A 146 ? 0.1076 0.0650 0.0480 0.0048 0.0257 0.0016 146 ARG A NH2 1183 N NH2 B ARG A 146 ? 0.2016 0.1488 0.1578 -0.0004 0.0375 0.0029 146 ARG A NH2 1184 N N . LYS A 147 ? 0.2191 0.1694 0.1373 0.0081 0.0263 -0.0010 147 LYS A N 1185 C CA . LYS A 147 ? 0.2083 0.1589 0.1205 0.0122 0.0267 0.0007 147 LYS A CA 1186 C C . LYS A 147 ? 0.1772 0.1236 0.0904 0.0143 0.0324 0.0039 147 LYS A C 1187 O O . LYS A 147 ? 0.2487 0.1922 0.1665 0.0122 0.0351 0.0037 147 LYS A O 1188 C CB . LYS A 147 ? 0.1535 0.1069 0.0621 0.0119 0.0227 -0.0029 147 LYS A CB 1189 C CG . LYS A 147 ? 0.1974 0.1532 0.0992 0.0153 0.0211 -0.0025 147 LYS A CG 1190 C CD . LYS A 147 ? 0.2811 0.2395 0.1809 0.0142 0.0176 -0.0068 147 LYS A CD 1191 C CE . LYS A 147 ? 0.3285 0.2910 0.2223 0.0164 0.0145 -0.0075 147 LYS A CE 1192 N NZ . LYS A 147 ? 0.3060 0.2670 0.1939 0.0201 0.0179 -0.0044 147 LYS A NZ 1193 N N . PHE A 148 ? 0.1996 0.1458 0.1087 0.0183 0.0341 0.0070 148 PHE A N 1194 C CA . PHE A 148 ? 0.1520 0.0948 0.0624 0.0207 0.0394 0.0105 148 PHE A CA 1195 C C . PHE A 148 ? 0.2281 0.1718 0.1311 0.0239 0.0393 0.0107 148 PHE A C 1196 O O . PHE A 148 ? 0.3081 0.2555 0.2052 0.0256 0.0360 0.0103 148 PHE A O 1197 C CB . PHE A 148 ? 0.1479 0.0892 0.0619 0.0228 0.0429 0.0149 148 PHE A CB 1198 C CG . PHE A 148 ? 0.2076 0.1474 0.1295 0.0197 0.0440 0.0147 148 PHE A CG 1199 C CD1 . PHE A 148 ? 0.1741 0.1163 0.0959 0.0179 0.0409 0.0130 148 PHE A CD1 1200 C CD2 . PHE A 148 ? 0.2072 0.1437 0.1371 0.0184 0.0483 0.0160 148 PHE A CD2 1201 C CE1 . PHE A 148 ? 0.1990 0.1402 0.1279 0.0148 0.0423 0.0124 148 PHE A CE1 1202 C CE2 . PHE A 148 ? 0.2735 0.2092 0.2113 0.0151 0.0492 0.0153 148 PHE A CE2 1203 C CZ . PHE A 148 ? 0.2194 0.1576 0.1564 0.0132 0.0464 0.0134 148 PHE A CZ 1204 N N . HIS A 149 ? 0.1875 0.1283 0.0912 0.0245 0.0428 0.0113 149 HIS A N 1205 C CA . HIS A 149 ? 0.1680 0.1095 0.0649 0.0278 0.0439 0.0120 149 HIS A CA 1206 C C . HIS A 149 ? 0.2216 0.1595 0.1214 0.0306 0.0497 0.0168 149 HIS A C 1207 O O . HIS A 149 ? 0.2724 0.2067 0.1800 0.0291 0.0529 0.0180 149 HIS A O 1208 C CB . HIS A 149 ? 0.2568 0.1984 0.1509 0.0262 0.0424 0.0076 149 HIS A CB 1209 C CG . HIS A 149 ? 0.2740 0.2202 0.1641 0.0247 0.0365 0.0032 149 HIS A CG 1210 N ND1 . HIS A 149 ? 0.2768 0.2260 0.1597 0.0261 0.0344 0.0007 149 HIS A ND1 1211 C CD2 . HIS A 149 ? 0.2972 0.2457 0.1901 0.0219 0.0322 0.0008 149 HIS A CD2 1212 C CE1 . HIS A 149 ? 0.3076 0.2606 0.1897 0.0241 0.0290 -0.0031 149 HIS A CE1 1213 N NE2 . HIS A 149 ? 0.2799 0.2326 0.1681 0.0216 0.0276 -0.0030 149 HIS A NE2 1214 N N . TYR A 150 ? 0.2485 0.1876 0.1425 0.0346 0.0511 0.0195 150 TYR A N 1215 C CA . TYR A 150 ? 0.2701 0.2065 0.1675 0.0378 0.0566 0.0246 150 TYR A CA 1216 C C . TYR A 150 ? 0.3226 0.2588 0.2136 0.0408 0.0590 0.0254 150 TYR A C 1217 O O . TYR A 150 ? 0.3059 0.2456 0.1881 0.0417 0.0563 0.0233 150 TYR A O 1218 C CB . TYR A 150 ? 0.2576 0.1957 0.1559 0.0404 0.0571 0.0288 150 TYR A CB 1219 C CG . TYR A 150 ? 0.2171 0.1553 0.1215 0.0379 0.0553 0.0283 150 TYR A CG 1220 C CD1 . TYR A 150 ? 0.1891 0.1240 0.1038 0.0363 0.0586 0.0296 150 TYR A CD1 1221 C CD2 . TYR A 150 ? 0.1848 0.1268 0.0850 0.0370 0.0504 0.0263 150 TYR A CD2 1222 C CE1 . TYR A 150 ? 0.2196 0.1548 0.1396 0.0339 0.0572 0.0288 150 TYR A CE1 1223 C CE2 . TYR A 150 ? 0.1699 0.1120 0.0755 0.0348 0.0491 0.0259 150 TYR A CE2 1224 C CZ . TYR A 150 ? 0.2151 0.1537 0.1303 0.0332 0.0527 0.0271 150 TYR A CZ 1225 O OH . TYR A 150 ? 0.1815 0.1201 0.1018 0.0308 0.0518 0.0265 150 TYR A OH 1226 N N . LEU A 151 ? 0.3223 0.2545 0.2183 0.0421 0.0642 0.0283 151 LEU A N 1227 C CA . LEU A 151 ? 0.3333 0.2650 0.2240 0.0453 0.0675 0.0298 151 LEU A CA 1228 C C . LEU A 151 ? 0.2759 0.2050 0.1721 0.0487 0.0731 0.0356 151 LEU A C 1229 O O . LEU A 151 ? 0.2761 0.2011 0.1814 0.0477 0.0764 0.0367 151 LEU A O 1230 C CB . LEU A 151 ? 0.2926 0.2217 0.1831 0.0431 0.0682 0.0261 151 LEU A CB 1231 C CG . LEU A 151 ? 0.3229 0.2506 0.2089 0.0461 0.0723 0.0275 151 LEU A CG 1232 C CD1 . LEU A 151 ? 0.3307 0.2632 0.2050 0.0489 0.0706 0.0270 151 LEU A CD1 1233 C CD2 . LEU A 151 ? 0.3099 0.2349 0.1974 0.0435 0.0732 0.0237 151 LEU A CD2 1234 N N . PRO A 152 ? 0.3008 0.2326 0.1924 0.0528 0.0741 0.0395 152 PRO A N 1235 C CA . PRO A 152 ? 0.2741 0.2041 0.1708 0.0566 0.0799 0.0452 152 PRO A CA 1236 C C . PRO A 152 ? 0.2771 0.2041 0.1720 0.0576 0.0835 0.0451 152 PRO A C 1237 O O . PRO A 152 ? 0.3594 0.2880 0.2449 0.0574 0.0818 0.0419 152 PRO A O 1238 C CB . PRO A 152 ? 0.3942 0.3289 0.2838 0.0606 0.0794 0.0487 152 PRO A CB 1239 C CG . PRO A 152 ? 0.4215 0.3598 0.3069 0.0583 0.0735 0.0456 152 PRO A CG 1240 C CD . PRO A 152 ? 0.3442 0.2814 0.2274 0.0540 0.0701 0.0392 152 PRO A CD 1241 N N . PHE A 153 ? 0.2919 0.2150 0.1963 0.0587 0.0885 0.0481 153 PHE A N 1242 C CA . PHE A 153 ? 0.3276 0.2475 0.2311 0.0597 0.0922 0.0483 153 PHE A CA 1243 C C . PHE A 153 ? 0.3584 0.2755 0.2713 0.0629 0.0982 0.0536 153 PHE A C 1244 O O . PHE A 153 ? 0.3437 0.2608 0.2661 0.0633 0.0992 0.0560 153 PHE A O 1245 C CB . PHE A 153 ? 0.2855 0.2023 0.1923 0.0551 0.0908 0.0434 153 PHE A CB 1246 C CG . PHE A 153 ? 0.3152 0.2284 0.2361 0.0528 0.0924 0.0439 153 PHE A CG 1247 C CD1 . PHE A 153 ? 0.3170 0.2314 0.2441 0.0503 0.0896 0.0430 153 PHE A CD1 1248 C CD2 . PHE A 153 ? 0.3071 0.2162 0.2350 0.0530 0.0966 0.0448 153 PHE A CD2 1249 C CE1 . PHE A 153 ? 0.2745 0.1869 0.2146 0.0479 0.0909 0.0425 153 PHE A CE1 1250 C CE2 . PHE A 153 ? 0.3402 0.2472 0.2815 0.0507 0.0976 0.0446 153 PHE A CE2 1251 C CZ . PHE A 153 ? 0.3151 0.2243 0.2625 0.0481 0.0947 0.0431 153 PHE A CZ 1252 N N . LEU A 154 ? 0.3904 0.3055 0.3008 0.0654 0.1022 0.0552 154 LEU A N 1253 C CA . LEU A 154 ? 0.3834 0.2958 0.3029 0.0686 0.1081 0.0600 154 LEU A CA 1254 C C . LEU A 154 ? 0.3522 0.2595 0.2797 0.0662 0.1102 0.0581 154 LEU A C 1255 O O . LEU A 154 ? 0.3671 0.2725 0.2888 0.0659 0.1112 0.0564 154 LEU A O 1256 C CB . LEU A 154 ? 0.3999 0.3139 0.3108 0.0738 0.1118 0.0641 154 LEU A CB 1257 C CG . LEU A 154 ? 0.5172 0.4299 0.4368 0.0783 0.1179 0.0704 154 LEU A CG 1258 C CD1 . LEU A 154 ? 0.4812 0.3969 0.4083 0.0795 0.1177 0.0736 154 LEU A CD1 1259 C CD2 . LEU A 154 ? 0.5322 0.4465 0.4419 0.0830 0.1214 0.0739 154 LEU A CD2 1260 N N . PRO A 155 ? 0.3764 0.2929 0.3133 0.0061 0.1548 0.0566 155 PRO A N 1261 C CA . PRO A 155 ? 0.3506 0.2689 0.3116 0.0071 0.1598 0.0472 155 PRO A CA 1262 C C . PRO A 155 ? 0.3715 0.2963 0.3398 0.0015 0.1703 0.0443 155 PRO A C 1263 O O . PRO A 155 ? 0.3984 0.3229 0.3615 -0.0039 0.1746 0.0523 155 PRO A O 1264 C CB . PRO A 155 ? 0.3392 0.2474 0.3177 0.0088 0.1576 0.0538 155 PRO A CB 1265 C CG . PRO A 155 ? 0.3952 0.2947 0.3596 0.0132 0.1494 0.0610 155 PRO A CG 1266 C CD . PRO A 155 ? 0.4350 0.3406 0.3773 0.0104 0.1497 0.0679 155 PRO A CD 1267 N N . SER A 156 ? 0.3960 0.3260 0.3776 0.0030 0.1747 0.0336 156 SER A N 1268 C CA . SER A 156 ? 0.4997 0.4357 0.4933 -0.0003 0.1866 0.0300 156 SER A CA 1269 C C . SER A 156 ? 0.4952 0.4351 0.5202 0.0046 0.1889 0.0231 156 SER A C 1270 O O . SER A 156 ? 0.4761 0.4136 0.5040 0.0093 0.1810 0.0190 156 SER A O 1271 C CB . SER A 156 ? 0.5433 0.4799 0.5076 -0.0054 0.1923 0.0244 156 SER A CB 1272 O OG . SER A 156 ? 0.6092 0.5438 0.5639 -0.0030 0.1884 0.0143 156 SER A OG 1273 N N . THR A 157 ? 0.4497 0.3964 0.4997 0.0035 0.1995 0.0233 157 THR A N 1274 C CA . THR A 157 ? 0.4521 0.4044 0.5374 0.0085 0.2019 0.0197 157 THR A CA 1275 C C . THR A 157 ? 0.4580 0.4054 0.5323 0.0111 0.2064 0.0084 157 THR A C 1276 O O . THR A 157 ? 0.4927 0.4417 0.5926 0.0161 0.2065 0.0057 157 THR A O 1277 C CB . THR A 157 ? 0.4846 0.4479 0.6056 0.0067 0.2121 0.0252 157 THR A CB 1278 O OG1 . THR A 157 ? 0.5418 0.5041 0.6448 0.0025 0.2257 0.0222 157 THR A OG1 1279 C CG2 . THR A 157 ? 0.4455 0.4134 0.5826 0.0021 0.2059 0.0368 157 THR A CG2 1280 N N . GLU A 158 ? 0.5277 0.4689 0.5646 0.0066 0.2096 0.0030 158 GLU A N 1281 C CA . GLU A 158 ? 0.6361 0.5707 0.6601 0.0063 0.2165 -0.0082 158 GLU A CA 1282 C C . GLU A 158 ? 0.6599 0.5880 0.6643 0.0073 0.2047 -0.0137 158 GLU A C 1283 O O . GLU A 158 ? 0.7088 0.6300 0.7079 0.0072 0.2090 -0.0228 158 GLU A O 1284 C CB . GLU A 158 ? 0.7272 0.6586 0.7208 -0.0016 0.2281 -0.0116 158 GLU A CB 1285 C CG . GLU A 158 ? 0.8525 0.7897 0.8627 -0.0038 0.2432 -0.0077 158 GLU A CG 1286 C CD . GLU A 158 ? 0.9860 0.9269 1.0401 0.0027 0.2539 -0.0095 158 GLU A CD 1287 O OE1 . GLU A 158 ? 0.9553 0.8911 1.0216 0.0079 0.2533 -0.0157 158 GLU A OE1 1288 O OE2 . GLU A 158 ? 1.1298 1.0795 1.2082 0.0021 0.2632 -0.0034 158 GLU A OE2 1289 N N . ASP A 159 ? 0.5361 0.4657 0.5310 0.0081 0.1910 -0.0082 159 ASP A N 1290 C CA . ASP A 159 ? 0.4668 0.3924 0.4437 0.0085 0.1800 -0.0125 159 ASP A CA 1291 C C . ASP A 159 ? 0.5082 0.4343 0.5061 0.0147 0.1699 -0.0101 159 ASP A C 1292 O O . ASP A 159 ? 0.5457 0.4749 0.5596 0.0173 0.1665 -0.0026 159 ASP A O 1293 C CB . ASP A 159 ? 0.4414 0.3682 0.3865 0.0038 0.1728 -0.0080 159 ASP A CB 1294 C CG . ASP A 159 ? 0.5621 0.4883 0.4793 -0.0047 0.1808 -0.0099 159 ASP A CG 1295 O OD1 . ASP A 159 ? 0.5806 0.5016 0.4942 -0.0074 0.1909 -0.0192 159 ASP A OD1 1296 O OD2 . ASP A 159 ? 0.6055 0.5350 0.5034 -0.0091 0.1773 -0.0012 159 ASP A OD2 1297 N N . VAL A 160 ? 0.4377 0.3595 0.4333 0.0160 0.1657 -0.0165 160 VAL A N 1298 C CA . VAL A 160 ? 0.2651 0.1865 0.2716 0.0203 0.1549 -0.0146 160 VAL A CA 1299 C C . VAL A 160 ? 0.3827 0.3018 0.3624 0.0179 0.1461 -0.0177 160 VAL A C 1300 O O . VAL A 160 ? 0.3101 0.2273 0.2680 0.0128 0.1488 -0.0231 160 VAL A O 1301 C CB . VAL A 160 ? 0.2625 0.1820 0.2956 0.0242 0.1571 -0.0170 160 VAL A CB 1302 C CG1 . VAL A 160 ? 0.3057 0.2310 0.3719 0.0268 0.1663 -0.0125 160 VAL A CG1 1303 C CG2 . VAL A 160 ? 0.2795 0.1914 0.2997 0.0217 0.1618 -0.0262 160 VAL A CG2 1304 N N . TYR A 161 ? 0.2987 0.2181 0.2802 0.0208 0.1362 -0.0142 161 TYR A N 1305 C CA . TYR A 161 ? 0.2768 0.1964 0.2383 0.0191 0.1283 -0.0156 161 TYR A CA 1306 C C . TYR A 161 ? 0.2611 0.1770 0.2306 0.0214 0.1218 -0.0176 161 TYR A C 1307 O O . TYR A 161 ? 0.2271 0.1405 0.2155 0.0250 0.1208 -0.0153 161 TYR A O 1308 C CB . TYR A 161 ? 0.2498 0.1729 0.2017 0.0202 0.1245 -0.0081 161 TYR A CB 1309 C CG . TYR A 161 ? 0.2719 0.1982 0.2112 0.0168 0.1302 -0.0041 161 TYR A CG 1310 C CD1 . TYR A 161 ? 0.2586 0.1843 0.2090 0.0174 0.1368 0.0003 161 TYR A CD1 1311 C CD2 . TYR A 161 ? 0.3766 0.3072 0.2920 0.0115 0.1292 -0.0034 161 TYR A CD2 1312 C CE1 . TYR A 161 ? 0.3413 0.2693 0.2783 0.0132 0.1421 0.0050 161 TYR A CE1 1313 C CE2 . TYR A 161 ? 0.3710 0.3043 0.2712 0.0067 0.1335 0.0022 161 TYR A CE2 1314 C CZ . TYR A 161 ? 0.3867 0.3181 0.2975 0.0078 0.1401 0.0062 161 TYR A CZ 1315 O OH . TYR A 161 ? 0.4233 0.3569 0.3178 0.0019 0.1443 0.0128 161 TYR A OH 1316 N N . ASP A 162 ? 0.2398 0.1554 0.1944 0.0185 0.1177 -0.0213 162 ASP A N 1317 C CA . ASP A 162 ? 0.2478 0.1596 0.2056 0.0197 0.1118 -0.0223 162 ASP A CA 1318 C C . ASP A 162 ? 0.2438 0.1605 0.1852 0.0174 0.1070 -0.0216 162 ASP A C 1319 O O . ASP A 162 ? 0.2508 0.1725 0.1771 0.0130 0.1087 -0.0228 162 ASP A O 1320 C CB . ASP A 162 ? 0.3716 0.2758 0.3346 0.0180 0.1152 -0.0287 162 ASP A CB 1321 C CG . ASP A 162 ? 0.3491 0.2504 0.3353 0.0219 0.1211 -0.0278 162 ASP A CG 1322 O OD1 . ASP A 162 ? 0.4083 0.3077 0.4121 0.0262 0.1174 -0.0234 162 ASP A OD1 1323 O OD2 . ASP A 162 ? 0.3046 0.2053 0.2920 0.0204 0.1298 -0.0313 162 ASP A OD2 1324 N N . CYS A 163 ? 0.2202 0.1359 0.1640 0.0196 0.1020 -0.0190 163 CYS A N 1325 C CA . CYS A 163 ? 0.2967 0.2181 0.2303 0.0175 0.0996 -0.0185 163 CYS A CA 1326 C C . CYS A 163 ? 0.3068 0.2212 0.2386 0.0137 0.0991 -0.0239 163 CYS A C 1327 O O . CYS A 163 ? 0.2711 0.1766 0.2099 0.0157 0.0977 -0.0236 163 CYS A O 1328 C CB . CYS A 163 ? 0.2454 0.1692 0.1822 0.0220 0.0972 -0.0124 163 CYS A CB 1329 S SG . CYS A 163 ? 0.3182 0.2529 0.2502 0.0210 0.0975 -0.0098 163 CYS A SG 1330 N N . ARG A 164 ? 0.3224 0.2388 0.2422 0.0072 0.1008 -0.0284 164 ARG A N 1331 C CA . ARG A 164 ? 0.3294 0.2360 0.2460 0.0022 0.1017 -0.0342 164 ARG A CA 1332 C C . ARG A 164 ? 0.3418 0.2589 0.2555 -0.0025 0.0960 -0.0305 164 ARG A C 1333 O O . ARG A 164 ? 0.2426 0.1740 0.1506 -0.0072 0.0929 -0.0278 164 ARG A O 1334 C CB . ARG A 164 ? 0.2608 0.1595 0.1676 -0.0050 0.1058 -0.0427 164 ARG A CB 1335 C CG . ARG A 164 ? 0.2725 0.1568 0.1764 -0.0106 0.1074 -0.0492 164 ARG A CG 1336 C CD . ARG A 164 ? 0.3402 0.2135 0.2334 -0.0184 0.1124 -0.0585 164 ARG A CD 1337 N NE . ARG A 164 ? 0.3920 0.2739 0.2612 -0.0297 0.1107 -0.0615 164 ARG A NE 1338 C CZ . ARG A 164 ? 0.3975 0.2749 0.2503 -0.0376 0.1138 -0.0676 164 ARG A CZ 1339 N NH1 . ARG A 164 ? 0.3768 0.2417 0.2375 -0.0338 0.1216 -0.0720 164 ARG A NH1 1340 N NH2 . ARG A 164 ? 0.4303 0.3166 0.2580 -0.0505 0.1093 -0.0683 164 ARG A NH2 1341 N N . VAL A 165 ? 0.2888 0.1999 0.2076 -0.0020 0.0940 -0.0289 165 VAL A N 1342 C CA . VAL A 165 ? 0.2833 0.2052 0.2028 -0.0060 0.0912 -0.0247 165 VAL A CA 1343 C C . VAL A 165 ? 0.2676 0.1806 0.1835 -0.0146 0.0900 -0.0279 165 VAL A C 1344 O O . VAL A 165 ? 0.3385 0.2347 0.2554 -0.0137 0.0902 -0.0290 165 VAL A O 1345 C CB . VAL A 165 ? 0.2257 0.1478 0.1501 0.0007 0.0924 -0.0193 165 VAL A CB 1346 C CG1 . VAL A 165 ? 0.2272 0.1577 0.1533 -0.0032 0.0935 -0.0159 165 VAL A CG1 1347 C CG2 . VAL A 165 ? 0.2186 0.1484 0.1471 0.0083 0.0940 -0.0158 165 VAL A CG2 1348 N N . GLU A 166 ? 0.2879 0.2126 0.2015 -0.0238 0.0875 -0.0278 166 GLU A N 1349 C CA . GLU A 166 ? 0.2616 0.1787 0.1723 -0.0339 0.0863 -0.0299 166 GLU A CA 1350 C C . GLU A 166 ? 0.3502 0.2831 0.2688 -0.0367 0.0860 -0.0226 166 GLU A C 1351 O O . GLU A 166 ? 0.2669 0.2224 0.1944 -0.0358 0.0851 -0.0171 166 GLU A O 1352 C CB . GLU A 166 ? 0.3440 0.2587 0.2445 -0.0461 0.0841 -0.0368 166 GLU A CB 1353 C CG . GLU A 166 ? 0.5821 0.4817 0.4723 -0.0445 0.0883 -0.0457 166 GLU A CG 1354 C CD . GLU A 166 ? 0.7223 0.6212 0.5951 -0.0591 0.0863 -0.0530 166 GLU A CD 1355 O OE1 . GLU A 166 ? 0.6526 0.5692 0.5247 -0.0699 0.0785 -0.0485 166 GLU A OE1 1356 O OE2 . GLU A 166 ? 0.8817 0.7621 0.7415 -0.0609 0.0931 -0.0632 166 GLU A OE2 1357 N N . HIS A 167 ? 0.3106 0.2192 0.2481 0.0434 0.0294 -0.0534 167 HIS A N 1358 C CA . HIS A 167 ? 0.2381 0.1505 0.1710 0.0397 0.0254 -0.0544 167 HIS A CA 1359 C C . HIS A 167 ? 0.2168 0.1182 0.1427 0.0453 0.0314 -0.0507 167 HIS A C 1360 O O . HIS A 167 ? 0.3205 0.2094 0.2446 0.0560 0.0380 -0.0442 167 HIS A O 1361 C CB . HIS A 167 ? 0.2028 0.1158 0.1290 0.0416 0.0183 -0.0543 167 HIS A CB 1362 C CG . HIS A 167 ? 0.2868 0.2048 0.2109 0.0357 0.0166 -0.0575 167 HIS A CG 1363 N ND1 . HIS A 167 ? 0.2845 0.1959 0.1937 0.0397 0.0166 -0.0567 167 HIS A ND1 1364 C CD2 . HIS A 167 ? 0.2265 0.1490 0.1555 0.0300 0.0157 -0.0609 167 HIS A CD2 1365 C CE1 . HIS A 167 ? 0.2610 0.1803 0.1742 0.0319 0.0168 -0.0616 167 HIS A CE1 1366 N NE2 . HIS A 167 ? 0.3368 0.2594 0.2605 0.0282 0.0165 -0.0639 167 HIS A NE2 1367 N N . TRP A 168 ? 0.2406 0.1445 0.1637 0.0403 0.0311 -0.0528 168 TRP A N 1368 C CA . TRP A 168 ? 0.2835 0.1755 0.2002 0.0445 0.0383 -0.0491 168 TRP A CA 1369 C C . TRP A 168 ? 0.3296 0.2069 0.2305 0.0572 0.0406 -0.0411 168 TRP A C 1370 O O . TRP A 168 ? 0.3194 0.1815 0.2170 0.0661 0.0511 -0.0328 168 TRP A O 1371 C CB . TRP A 168 ? 0.2287 0.1223 0.1399 0.0380 0.0375 -0.0520 168 TRP A CB 1372 C CG . TRP A 168 ? 0.2684 0.1618 0.1781 0.0310 0.0391 -0.0555 168 TRP A CG 1373 C CD1 . TRP A 168 ? 0.2983 0.1841 0.2064 0.0287 0.0466 -0.0563 168 TRP A CD1 1374 C CD2 . TRP A 168 ? 0.2969 0.1974 0.2053 0.0251 0.0343 -0.0588 168 TRP A CD2 1375 N NE1 . TRP A 168 ? 0.3401 0.2278 0.2416 0.0200 0.0460 -0.0603 168 TRP A NE1 1376 C CE2 . TRP A 168 ? 0.3835 0.2811 0.2866 0.0189 0.0376 -0.0612 168 TRP A CE2 1377 C CE3 . TRP A 168 ? 0.2156 0.1235 0.1270 0.0242 0.0291 -0.0601 168 TRP A CE3 1378 C CZ2 . TRP A 168 ? 0.3364 0.2399 0.2361 0.0125 0.0337 -0.0641 168 TRP A CZ2 1379 C CZ3 . TRP A 168 ? 0.3024 0.2157 0.2153 0.0197 0.0266 -0.0631 168 TRP A CZ3 1380 C CH2 . TRP A 168 ? 0.2833 0.1952 0.1896 0.0143 0.0278 -0.0646 168 TRP A CH2 1381 N N . GLY A 169 ? 0.2505 0.1316 0.1406 0.0598 0.0313 -0.0428 169 GLY A N 1382 C CA . GLY A 169 ? 0.2782 0.1467 0.1420 0.0758 0.0294 -0.0372 169 GLY A CA 1383 C C . GLY A 169 ? 0.2798 0.1590 0.1675 0.0840 0.0285 -0.0189 169 GLY A C 1384 O O . GLY A 169 ? 0.3432 0.2427 0.2389 0.0842 0.0197 0.0012 169 GLY A O 1385 N N . LEU A 170 ? 0.3365 0.2064 0.2384 0.0884 0.0374 -0.0235 170 LEU A N 1386 C CA . LEU A 170 ? 0.2998 0.1796 0.2316 0.0964 0.0403 -0.0061 170 LEU A CA 1387 C C . LEU A 170 ? 0.3859 0.2530 0.3409 0.1015 0.0613 0.0031 170 LEU A C 1388 O O . LEU A 170 ? 0.4332 0.2945 0.3833 0.0875 0.0680 -0.0109 170 LEU A O 1389 C CB . LEU A 170 ? 0.2616 0.1427 0.1976 0.0941 0.0382 -0.0168 170 LEU A CB 1390 C CG . LEU A 170 ? 0.3920 0.2896 0.3162 0.0853 0.0186 -0.0247 170 LEU A CG 1391 C CD1 . LEU A 170 ? 0.2629 0.1567 0.1914 0.0828 0.0202 -0.0359 170 LEU A CD1 1392 C CD2 . LEU A 170 ? 0.2555 0.1816 0.1918 0.0835 0.0034 -0.0059 170 LEU A CD2 1393 N N . ASP A 171 ? 0.4445 0.3202 0.4317 0.1143 0.0663 0.0298 171 ASP A N 1394 C CA . ASP A 171 ? 0.5260 0.3964 0.5411 0.1126 0.0855 0.0374 171 ASP A CA 1395 C C . ASP A 171 ? 0.5355 0.4022 0.5601 0.1043 0.0960 0.0250 171 ASP A C 1396 O O . ASP A 171 ? 0.5812 0.4348 0.6083 0.0965 0.1131 0.0179 171 ASP A O 1397 C CB . ASP A 171 ? 0.5545 0.4443 0.6082 0.1247 0.0848 0.0735 171 ASP A CB 1398 C CG . ASP A 171 ? 0.7327 0.6272 0.7778 0.1294 0.0771 0.0913 171 ASP A CG 1399 O OD1 . ASP A 171 ? 0.8084 0.6808 0.8250 0.1252 0.0838 0.0733 171 ASP A OD1 1400 O OD2 . ASP A 171 ? 0.8114 0.7370 0.8762 0.1333 0.0618 0.1244 171 ASP A OD2 1401 N N . GLU A 172 ? 0.4355 0.3133 0.4632 0.1059 0.0861 0.0237 172 GLU A N 1402 C CA . GLU A 172 ? 0.4121 0.2873 0.4447 0.0987 0.0943 0.0131 172 GLU A CA 1403 C C . GLU A 172 ? 0.3527 0.2349 0.3663 0.0944 0.0779 -0.0001 172 GLU A C 1404 O O . GLU A 172 ? 0.3187 0.2086 0.3236 0.1003 0.0626 0.0033 172 GLU A O 1405 C CB . GLU A 172 ? 0.5978 0.4822 0.6716 0.1074 0.1056 0.0343 172 GLU A CB 1406 C CG . GLU A 172 ? 0.7940 0.7052 0.8916 0.1191 0.0882 0.0590 172 GLU A CG 1407 C CD . GLU A 172 ? 0.9959 0.9232 1.1403 0.1248 0.0978 0.0837 172 GLU A CD 1408 O OE1 . GLU A 172 ? 1.1028 1.0167 1.2649 0.1236 0.1219 0.0858 172 GLU A OE1 1409 O OE2 . GLU A 172 ? 1.0231 0.9781 1.1878 0.1288 0.0815 0.1021 172 GLU A OE2 1410 N N . PRO A 173 ? 0.3504 0.2299 0.3567 0.0844 0.0819 -0.0136 173 PRO A N 1411 C CA . PRO A 173 ? 0.3451 0.2328 0.3388 0.0804 0.0671 -0.0232 173 PRO A CA 1412 C C . PRO A 173 ? 0.3202 0.2200 0.3327 0.0927 0.0590 -0.0103 173 PRO A C 1413 O O . PRO A 173 ? 0.4146 0.3221 0.4573 0.1014 0.0659 0.0068 173 PRO A O 1414 C CB . PRO A 173 ? 0.3522 0.2358 0.3393 0.0694 0.0761 -0.0333 173 PRO A CB 1415 C CG . PRO A 173 ? 0.3891 0.2613 0.3907 0.0700 0.0981 -0.0274 173 PRO A CG 1416 C CD . PRO A 173 ? 0.3540 0.2219 0.3601 0.0751 0.1003 -0.0199 173 PRO A CD 1417 N N . LEU A 174 ? 0.3122 0.2165 0.3087 0.0925 0.0434 -0.0166 174 LEU A N 1418 C CA . LEU A 174 ? 0.2698 0.1951 0.2796 0.0960 0.0276 -0.0057 174 LEU A CA 1419 C C . LEU A 174 ? 0.3345 0.2618 0.3500 0.0924 0.0280 -0.0124 174 LEU A C 1420 O O . LEU A 174 ? 0.2948 0.2121 0.2903 0.0851 0.0270 -0.0280 174 LEU A O 1421 C CB . LEU A 174 ? 0.2827 0.2182 0.2703 0.0872 0.0073 -0.0117 174 LEU A CB 1422 C CG . LEU A 174 ? 0.2836 0.2468 0.2779 0.0801 -0.0125 -0.0026 174 LEU A CG 1423 C CD1 . LEU A 174 ? 0.3046 0.2904 0.3286 0.0863 -0.0148 0.0253 174 LEU A CD1 1424 C CD2 . LEU A 174 ? 0.2761 0.2411 0.2423 0.0690 -0.0241 -0.0132 174 LEU A CD2 1425 N N . LEU A 175 ? 0.2788 0.2211 0.3250 0.0974 0.0296 0.0025 175 LEU A N 1426 C CA . LEU A 175 ? 0.2873 0.2341 0.3416 0.0938 0.0296 -0.0014 175 LEU A CA 1427 C C . LEU A 175 ? 0.2090 0.1825 0.2756 0.0889 0.0081 0.0069 175 LEU A C 1428 O O . LEU A 175 ? 0.2301 0.2257 0.3194 0.0917 0.0004 0.0260 175 LEU A O 1429 C CB . LEU A 175 ? 0.2460 0.1871 0.3270 0.1010 0.0528 0.0061 175 LEU A CB 1430 C CG . LEU A 175 ? 0.2845 0.2050 0.3421 0.0899 0.0701 -0.0105 175 LEU A CG 1431 C CD1 . LEU A 175 ? 0.3549 0.2634 0.3999 0.0869 0.0777 -0.0136 175 LEU A CD1 1432 C CD2 . LEU A 175 ? 0.2946 0.2147 0.3714 0.0885 0.0882 -0.0066 175 LEU A CD2 1433 N N . LYS A 176 ? 0.2486 0.2214 0.3021 0.0798 -0.0013 -0.0061 176 LYS A N 1434 C CA . LYS A 176 ? 0.2148 0.2090 0.2795 0.0721 -0.0182 -0.0022 176 LYS A CA 1435 C C . LYS A 176 ? 0.2545 0.2503 0.3357 0.0717 -0.0128 -0.0019 176 LYS A C 1436 O O . LYS A 176 ? 0.2425 0.2225 0.3117 0.0698 -0.0053 -0.0128 176 LYS A O 1437 C CB . LYS A 176 ? 0.3024 0.2933 0.3434 0.0606 -0.0309 -0.0176 176 LYS A CB 1438 C CG . LYS A 176 ? 0.3646 0.3579 0.3879 0.0578 -0.0372 -0.0177 176 LYS A CG 1439 C CD . LYS A 176 ? 0.3329 0.3558 0.3705 0.0541 -0.0493 0.0017 176 LYS A CD 1440 C CE . LYS A 176 ? 0.3881 0.4152 0.4072 0.0511 -0.0545 0.0057 176 LYS A CE 1441 N NZ . LYS A 176 ? 0.3294 0.3924 0.3591 0.0420 -0.0708 0.0275 176 LYS A NZ 1442 N N . HIS A 177 ? 0.2496 0.2679 0.3595 0.0721 -0.0178 0.0131 177 HIS A N 1443 C CA . HIS A 177 ? 0.2532 0.2750 0.3849 0.0737 -0.0094 0.0175 177 HIS A CA 1444 C C . HIS A 177 ? 0.3051 0.3356 0.4381 0.0623 -0.0228 0.0112 177 HIS A C 1445 O O . HIS A 177 ? 0.3245 0.3664 0.4517 0.0522 -0.0392 0.0082 177 HIS A O 1446 C CB . HIS A 177 ? 0.1929 0.2354 0.3638 0.0822 -0.0042 0.0405 177 HIS A CB 1447 C CG . HIS A 177 ? 0.3498 0.3920 0.5455 0.0865 0.0122 0.0451 177 HIS A CG 1448 N ND1 . HIS A 177 ? 0.3452 0.3640 0.5369 0.0924 0.0385 0.0383 177 HIS A ND1 1449 C CD2 . HIS A 177 ? 0.3247 0.3874 0.5488 0.0837 0.0075 0.0553 177 HIS A CD2 1450 C CE1 . HIS A 177 ? 0.3802 0.4042 0.5955 0.0933 0.0505 0.0435 177 HIS A CE1 1451 N NE2 . HIS A 177 ? 0.3471 0.3980 0.5844 0.0893 0.0316 0.0549 177 HIS A NE2 1452 N N . TRP A 178 ? 0.3247 0.3487 0.4639 0.0618 -0.0139 0.0086 178 TRP A N 1453 C CA . TRP A 178 ? 0.2463 0.2806 0.3978 0.0526 -0.0234 0.0075 178 TRP A CA 1454 C C . TRP A 178 ? 0.2128 0.2526 0.3876 0.0560 -0.0113 0.0169 178 TRP A C 1455 O O . TRP A 178 ? 0.2462 0.2719 0.4136 0.0607 0.0062 0.0150 178 TRP A O 1456 C CB . TRP A 178 ? 0.1778 0.1955 0.3104 0.0451 -0.0268 -0.0073 178 TRP A CB 1457 C CG . TRP A 178 ? 0.3644 0.3895 0.5138 0.0354 -0.0337 -0.0083 178 TRP A CG 1458 C CD1 . TRP A 178 ? 0.3560 0.3875 0.5080 0.0236 -0.0456 -0.0156 178 TRP A CD1 1459 C CD2 . TRP A 178 ? 0.2647 0.2911 0.4302 0.0345 -0.0273 -0.0027 178 TRP A CD2 1460 N NE1 . TRP A 178 ? 0.3264 0.3610 0.4974 0.0162 -0.0463 -0.0153 178 TRP A NE1 1461 C CE2 . TRP A 178 ? 0.3185 0.3511 0.4992 0.0237 -0.0362 -0.0059 178 TRP A CE2 1462 C CE3 . TRP A 178 ? 0.2851 0.3075 0.4514 0.0393 -0.0136 0.0038 178 TRP A CE3 1463 C CZ2 . TRP A 178 ? 0.2565 0.2917 0.4566 0.0201 -0.0328 -0.0005 178 TRP A CZ2 1464 C CZ3 . TRP A 178 ? 0.3083 0.3353 0.4907 0.0345 -0.0109 0.0094 178 TRP A CZ3 1465 C CH2 . TRP A 178 ? 0.2755 0.3091 0.4765 0.0262 -0.0210 0.0084 178 TRP A CH2 1466 N N . GLU A 179 ? 0.1876 0.2487 0.3891 0.0513 -0.0195 0.0260 179 GLU A N 1467 C CA . GLU A 179 ? 0.3221 0.3886 0.5464 0.0526 -0.0085 0.0335 179 GLU A CA 1468 C C . GLU A 179 ? 0.3150 0.3981 0.5572 0.0412 -0.0226 0.0355 179 GLU A C 1469 O O . GLU A 179 ? 0.2735 0.3689 0.5151 0.0318 -0.0397 0.0334 179 GLU A O 1470 C CB . GLU A 179 ? 0.3350 0.4123 0.5881 0.0639 0.0063 0.0496 179 GLU A CB 1471 C CG . GLU A 179 ? 0.3568 0.4658 0.6426 0.0644 -0.0074 0.0683 179 GLU A CG 1472 C CD . GLU A 179 ? 0.4020 0.5201 0.7252 0.0786 0.0111 0.0878 179 GLU A CD 1473 O OE1 . GLU A 179 ? 0.4198 0.5172 0.7329 0.0884 0.0292 0.0841 179 GLU A OE1 1474 O OE2 . GLU A 179 ? 0.4700 0.6129 0.8305 0.0782 0.0095 0.1058 179 GLU A OE2 1475 N N . PHE A 180 ? 0.2132 0.2961 0.4691 0.0395 -0.0141 0.0384 180 PHE A N 1476 C CA . PHE A 180 ? 0.2410 0.3360 0.5150 0.0281 -0.0245 0.0393 180 PHE A CA 1477 C C . PHE A 180 ? 0.3239 0.4503 0.6268 0.0228 -0.0372 0.0516 180 PHE A C 1478 O O . PHE A 180 ? 0.3596 0.5039 0.6899 0.0311 -0.0306 0.0685 180 PHE A O 1479 C CB . PHE A 180 ? 0.2751 0.3662 0.5605 0.0285 -0.0107 0.0440 180 PHE A CB 1480 C CG . PHE A 180 ? 0.3440 0.4438 0.6490 0.0169 -0.0190 0.0449 180 PHE A CG 1481 C CD1 . PHE A 180 ? 0.3155 0.4001 0.6098 0.0082 -0.0249 0.0342 180 PHE A CD1 1482 C CD2 . PHE A 180 ? 0.3659 0.4887 0.7049 0.0147 -0.0187 0.0576 180 PHE A CD2 1483 C CE1 . PHE A 180 ? 0.3415 0.4309 0.6570 -0.0031 -0.0294 0.0344 180 PHE A CE1 1484 C CE2 . PHE A 180 ? 0.4024 0.5326 0.7598 0.0025 -0.0255 0.0577 180 PHE A CE2 1485 C CZ . PHE A 180 ? 0.3678 0.4798 0.7127 -0.0067 -0.0302 0.0453 180 PHE A CZ 1486 N N . ASP A 181 ? 0.4610 0.5947 0.7593 0.0070 -0.0542 0.0435 181 ASP A N 1487 C CA . ASP A 181 ? 0.5478 0.7154 0.8658 -0.0051 -0.0709 0.0541 181 ASP A CA 1488 C C . ASP A 181 ? 0.5543 0.7405 0.9079 -0.0103 -0.0699 0.0651 181 ASP A C 1489 O O . ASP A 181 ? 0.5775 0.7880 0.9643 -0.0026 -0.0667 0.0863 181 ASP A O 1490 C CB . ASP A 181 ? 0.5913 0.7567 0.8840 -0.0254 -0.0861 0.0363 181 ASP A CB 1491 C CG . ASP A 181 ? 0.6213 0.8261 0.9261 -0.0450 -0.1061 0.0466 181 ASP A CG 1492 O OD1 . ASP A 181 ? 0.5729 0.8080 0.9135 -0.0459 -0.1102 0.0669 181 ASP A OD1 1493 O OD2 . ASP A 181 ? 0.6550 0.8626 0.9329 -0.0617 -0.1177 0.0349 181 ASP A OD2 1494 N N . ASP B 4 ? 0.7089 0.6193 0.6912 0.0796 0.0511 -0.0898 2 ASP B N 1495 C CA . ASP B 4 ? 0.7432 0.6477 0.7162 0.0734 0.0447 -0.0881 2 ASP B CA 1496 C C . ASP B 4 ? 0.7876 0.6901 0.7687 0.0773 0.0388 -0.0789 2 ASP B C 1497 O O . ASP B 4 ? 0.7741 0.6887 0.7591 0.0796 0.0353 -0.0718 2 ASP B O 1498 C CB . ASP B 4 ? 0.6370 0.5532 0.5989 0.0677 0.0417 -0.0875 2 ASP B CB 1499 C CG . ASP B 4 ? 0.5513 0.4612 0.5029 0.0597 0.0364 -0.0892 2 ASP B CG 1500 O OD1 . ASP B 4 ? 0.4917 0.3892 0.4456 0.0589 0.0342 -0.0887 2 ASP B OD1 1501 O OD2 . ASP B 4 ? 0.5484 0.4662 0.4903 0.0542 0.0343 -0.0908 2 ASP B OD2 1502 N N . THR B 5 ? 0.7191 0.6062 0.7025 0.0776 0.0378 -0.0791 3 THR B N 1503 C CA . THR B 5 ? 0.6520 0.5346 0.6414 0.0812 0.0329 -0.0698 3 THR B CA 1504 C C . THR B 5 ? 0.5931 0.4685 0.5732 0.0745 0.0278 -0.0678 3 THR B C 1505 O O . THR B 5 ? 0.5917 0.4610 0.5738 0.0762 0.0239 -0.0604 3 THR B O 1506 C CB . THR B 5 ? 0.6936 0.5634 0.6931 0.0871 0.0346 -0.0691 3 THR B CB 1507 O OG1 . THR B 5 ? 0.6811 0.5360 0.6756 0.0827 0.0362 -0.0775 3 THR B OG1 1508 C CG2 . THR B 5 ? 0.7400 0.6183 0.7517 0.0948 0.0388 -0.0704 3 THR B CG2 1509 N N . ARG B 6 ? 0.4861 0.3624 0.4560 0.0666 0.0277 -0.0743 4 ARG B N 1510 C CA . ARG B 6 ? 0.3907 0.2618 0.3530 0.0594 0.0230 -0.0733 4 ARG B CA 1511 C C . ARG B 6 ? 0.3594 0.2394 0.3227 0.0611 0.0177 -0.0647 4 ARG B C 1512 O O . ARG B 6 ? 0.3281 0.2236 0.2940 0.0642 0.0168 -0.0624 4 ARG B O 1513 C CB . ARG B 6 ? 0.3816 0.2574 0.3344 0.0511 0.0228 -0.0811 4 ARG B CB 1514 C CG . ARG B 6 ? 0.4342 0.2996 0.3842 0.0467 0.0266 -0.0908 4 ARG B CG 1515 C CD . ARG B 6 ? 0.4944 0.3664 0.4336 0.0380 0.0252 -0.0970 4 ARG B CD 1516 N NE . ARG B 6 ? 0.4247 0.3114 0.3593 0.0400 0.0264 -0.0966 4 ARG B NE 1517 C CZ . ARG B 6 ? 0.4473 0.3436 0.3725 0.0342 0.0235 -0.0983 4 ARG B CZ 1518 N NH1 . ARG B 6 ? 0.4041 0.2973 0.3235 0.0262 0.0190 -0.1006 4 ARG B NH1 1519 N NH2 . ARG B 6 ? 0.4663 0.3758 0.3888 0.0365 0.0247 -0.0973 4 ARG B NH2 1520 N N . PRO B 7 ? 0.3266 0.1979 0.2885 0.0581 0.0144 -0.0597 5 PRO B N 1521 C CA . PRO B 7 ? 0.3183 0.2010 0.2826 0.0567 0.0097 -0.0508 5 PRO B CA 1522 C C . PRO B 7 ? 0.2798 0.1784 0.2412 0.0505 0.0074 -0.0522 5 PRO B C 1523 O O . PRO B 7 ? 0.3026 0.2006 0.2586 0.0443 0.0077 -0.0584 5 PRO B O 1524 C CB . PRO B 7 ? 0.3317 0.2009 0.2938 0.0521 0.0083 -0.0466 5 PRO B CB 1525 C CG . PRO B 7 ? 0.3639 0.2178 0.3217 0.0478 0.0116 -0.0548 5 PRO B CG 1526 C CD . PRO B 7 ? 0.3113 0.1630 0.2704 0.0543 0.0157 -0.0616 5 PRO B CD 1527 N N . ARG B 8 ? 0.1995 0.1122 0.1646 0.0523 0.0048 -0.0463 6 ARG B N 1528 C CA . ARG B 8 ? 0.1851 0.1122 0.1487 0.0473 0.0027 -0.0464 6 ARG B CA 1529 C C . ARG B 8 ? 0.2090 0.1386 0.1727 0.0426 -0.0008 -0.0405 6 ARG B C 1530 O O . ARG B 8 ? 0.2255 0.1502 0.1909 0.0447 -0.0019 -0.0349 6 ARG B O 1531 C CB . ARG B 8 ? 0.2158 0.1572 0.1836 0.0520 0.0033 -0.0452 6 ARG B CB 1532 C CG . ARG B 8 ? 0.2296 0.1761 0.1938 0.0518 0.0063 -0.0518 6 ARG B CG 1533 C CD . ARG B 8 ? 0.2873 0.2219 0.2491 0.0552 0.0107 -0.0585 6 ARG B CD 1534 N NE . ARG B 8 ? 0.2134 0.1523 0.1689 0.0538 0.0137 -0.0655 6 ARG B NE 1535 C CZ . ARG B 8 ? 0.2948 0.2261 0.2475 0.0556 0.0186 -0.0720 6 ARG B CZ 1536 N NH1 . ARG B 8 ? 0.2872 0.2059 0.2446 0.0592 0.0211 -0.0724 6 ARG B NH1 1537 N NH2 . ARG B 8 ? 0.3360 0.2729 0.2820 0.0526 0.0213 -0.0770 6 ARG B NH2 1538 N N . PHE B 9 ? 0.2413 0.1787 0.2031 0.0365 -0.0023 -0.0418 7 PHE B N 1539 C CA . PHE B 9 ? 0.2336 0.1747 0.1961 0.0320 -0.0046 -0.0372 7 PHE B CA 1540 C C . PHE B 9 ? 0.2490 0.2050 0.2133 0.0305 -0.0060 -0.0368 7 PHE B C 1541 O O . PHE B 9 ? 0.1828 0.1435 0.1451 0.0287 -0.0059 -0.0408 7 PHE B O 1542 C CB . PHE B 9 ? 0.2211 0.1540 0.1812 0.0253 -0.0045 -0.0392 7 PHE B CB 1543 C CG . PHE B 9 ? 0.2492 0.1652 0.2073 0.0261 -0.0025 -0.0403 7 PHE B CG 1544 C CD1 . PHE B 9 ? 0.2292 0.1368 0.1873 0.0273 -0.0023 -0.0343 7 PHE B CD1 1545 C CD2 . PHE B 9 ? 0.2163 0.1245 0.1720 0.0256 -0.0006 -0.0473 7 PHE B CD2 1546 C CE1 . PHE B 9 ? 0.2105 0.1012 0.1671 0.0283 -0.0003 -0.0343 7 PHE B CE1 1547 C CE2 . PHE B 9 ? 0.2727 0.1636 0.2272 0.0264 0.0018 -0.0486 7 PHE B CE2 1548 C CZ . PHE B 9 ? 0.2406 0.1225 0.1960 0.0280 0.0020 -0.0416 7 PHE B CZ 1549 N N . LEU B 10 ? 0.2548 0.2176 0.2221 0.0312 -0.0074 -0.0318 8 LEU B N 1550 C CA . LEU B 10 ? 0.1755 0.1509 0.1453 0.0306 -0.0082 -0.0308 8 LEU B CA 1551 C C . LEU B 10 ? 0.2593 0.2384 0.2305 0.0264 -0.0094 -0.0280 8 LEU B C 1552 O O . LEU B 10 ? 0.1899 0.1654 0.1608 0.0260 -0.0098 -0.0249 8 LEU B O 1553 C CB . LEU B 10 ? 0.1453 0.1269 0.1189 0.0358 -0.0080 -0.0285 8 LEU B CB 1554 C CG . LEU B 10 ? 0.1975 0.1909 0.1744 0.0352 -0.0084 -0.0270 8 LEU B CG 1555 C CD1 . LEU B 10 ? 0.1111 0.1091 0.0861 0.0348 -0.0069 -0.0300 8 LEU B CD1 1556 C CD2 . LEU B 10 ? 0.1692 0.1681 0.1512 0.0392 -0.0086 -0.0244 8 LEU B CD2 1557 N N . GLU B 11 ? 0.1129 0.0993 0.0855 0.0235 -0.0100 -0.0291 9 GLU B N 1558 C CA . GLU B 11 ? 0.1259 0.1172 0.1016 0.0204 -0.0104 -0.0268 9 GLU B CA 1559 C C . GLU B 11 ? 0.2591 0.2596 0.2381 0.0223 -0.0106 -0.0250 9 GLU B C 1560 O O . GLU B 11 ? 0.2033 0.2082 0.1821 0.0236 -0.0107 -0.0260 9 GLU B O 1561 C CB . GLU B 11 ? 0.2104 0.2032 0.1872 0.0159 -0.0111 -0.0288 9 GLU B CB 1562 C CG . GLU B 11 ? 0.2743 0.2733 0.2562 0.0133 -0.0110 -0.0268 9 GLU B CG 1563 C CD . GLU B 11 ? 0.3174 0.3112 0.2992 0.0107 -0.0092 -0.0255 9 GLU B CD 1564 O OE1 . GLU B 11 ? 0.2594 0.2443 0.2370 0.0104 -0.0085 -0.0256 9 GLU B OE1 1565 O OE2 . GLU B 11 ? 0.2550 0.2533 0.2408 0.0091 -0.0080 -0.0241 9 GLU B OE2 1566 N N . GLN B 12 ? 0.1457 0.1485 0.1273 0.0220 -0.0104 -0.0225 10 GLN B N 1567 C CA . GLN B 12 ? 0.1015 0.1117 0.0871 0.0227 -0.0103 -0.0210 10 GLN B CA 1568 C C . GLN B 12 ? 0.1620 0.1740 0.1508 0.0199 -0.0096 -0.0202 10 GLN B C 1569 O O . GLN B 12 ? 0.1272 0.1352 0.1145 0.0178 -0.0089 -0.0203 10 GLN B O 1570 C CB . GLN B 12 ? 0.0970 0.1089 0.0838 0.0253 -0.0104 -0.0197 10 GLN B CB 1571 C CG . GLN B 12 ? 0.0888 0.0994 0.0743 0.0290 -0.0105 -0.0204 10 GLN B CG 1572 C CD . GLN B 12 ? 0.1238 0.1396 0.1134 0.0313 -0.0109 -0.0189 10 GLN B CD 1573 O OE1 . GLN B 12 ? 0.1139 0.1361 0.1076 0.0308 -0.0101 -0.0183 10 GLN B OE1 1574 N NE2 . GLN B 12 ? 0.0906 0.1036 0.0797 0.0337 -0.0123 -0.0181 10 GLN B NE2 1575 N N . VAL B 13 ? 0.0869 0.1046 0.0801 0.0200 -0.0093 -0.0191 11 VAL B N 1576 C CA . VAL B 13 ? 0.0748 0.0943 0.0726 0.0183 -0.0080 -0.0184 11 VAL B CA 1577 C C . VAL B 13 ? 0.1560 0.1786 0.1573 0.0195 -0.0072 -0.0170 11 VAL B C 1578 O O . VAL B 13 ? 0.1471 0.1729 0.1492 0.0211 -0.0076 -0.0156 11 VAL B O 1579 C CB . VAL B 13 ? 0.0741 0.0968 0.0760 0.0171 -0.0083 -0.0182 11 VAL B CB 1580 C CG1 . VAL B 13 ? 0.0721 0.0960 0.0800 0.0160 -0.0060 -0.0179 11 VAL B CG1 1581 C CG2 . VAL B 13 ? 0.0886 0.1086 0.0876 0.0151 -0.0092 -0.0201 11 VAL B CG2 1582 N N . LYS B 14 ? 0.1143 0.1358 0.1174 0.0182 -0.0058 -0.0175 12 LYS B N 1583 C CA . LYS B 14 ? 0.1910 0.2145 0.1984 0.0184 -0.0048 -0.0167 12 LYS B CA 1584 C C . LYS B 14 ? 0.1450 0.1673 0.1571 0.0171 -0.0023 -0.0174 12 LYS B C 1585 O O . LYS B 14 ? 0.1076 0.1271 0.1177 0.0153 -0.0009 -0.0197 12 LYS B O 1586 C CB . LYS B 14 ? 0.0707 0.0941 0.0761 0.0181 -0.0056 -0.0177 12 LYS B CB 1587 C CG . LYS B 14 ? 0.0946 0.1199 0.0977 0.0204 -0.0074 -0.0169 12 LYS B CG 1588 C CD . LYS B 14 ? 0.1453 0.1725 0.1487 0.0204 -0.0088 -0.0174 12 LYS B CD 1589 C CE . LYS B 14 ? 0.0724 0.1023 0.0757 0.0236 -0.0098 -0.0167 12 LYS B CE 1590 N NZ . LYS B 14 ? 0.0829 0.1166 0.0887 0.0241 -0.0117 -0.0168 12 LYS B NZ 1591 N N . HIS B 15 ? 0.0982 0.1225 0.1163 0.0182 -0.0014 -0.0151 13 HIS B N 1592 C CA . HIS B 15 ? 0.1316 0.1543 0.1559 0.0179 0.0015 -0.0156 13 HIS B CA 1593 C C . HIS B 15 ? 0.1540 0.1747 0.1812 0.0172 0.0031 -0.0157 13 HIS B C 1594 O O . HIS B 15 ? 0.1681 0.1901 0.1982 0.0183 0.0029 -0.0124 13 HIS B O 1595 C CB . HIS B 15 ? 0.0693 0.0952 0.0998 0.0201 0.0011 -0.0123 13 HIS B CB 1596 C CG . HIS B 15 ? 0.1241 0.1537 0.1519 0.0204 -0.0017 -0.0118 13 HIS B CG 1597 N ND1 . HIS B 15 ? 0.1351 0.1656 0.1648 0.0192 -0.0011 -0.0137 13 HIS B ND1 1598 C CD2 . HIS B 15 ? 0.0958 0.1282 0.1192 0.0211 -0.0048 -0.0102 13 HIS B CD2 1599 C CE1 . HIS B 15 ? 0.0935 0.1270 0.1206 0.0189 -0.0042 -0.0132 13 HIS B CE1 1600 N NE2 . HIS B 15 ? 0.0718 0.1061 0.0945 0.0202 -0.0065 -0.0115 13 HIS B NE2 1601 N N . GLU B 16 ? 0.1714 0.1886 0.1972 0.0148 0.0049 -0.0197 14 GLU B N 1602 C CA . GLU B 16 ? 0.1266 0.1420 0.1542 0.0128 0.0057 -0.0210 14 GLU B CA 1603 C C . GLU B 16 ? 0.1679 0.1782 0.2014 0.0119 0.0098 -0.0231 14 GLU B C 1604 O O . GLU B 16 ? 0.2140 0.2217 0.2472 0.0116 0.0123 -0.0262 14 GLU B O 1605 C CB . GLU B 16 ? 0.1122 0.1280 0.1331 0.0102 0.0036 -0.0243 14 GLU B CB 1606 C CG . GLU B 16 ? 0.0758 0.0955 0.0915 0.0117 -0.0001 -0.0225 14 GLU B CG 1607 C CD . GLU B 16 ? 0.1457 0.1666 0.1565 0.0099 -0.0027 -0.0248 14 GLU B CD 1608 O OE1 . GLU B 16 ? 0.1490 0.1679 0.1589 0.0068 -0.0020 -0.0282 14 GLU B OE1 1609 O OE2 . GLU B 16 ? 0.1903 0.2140 0.1981 0.0116 -0.0056 -0.0232 14 GLU B OE2 1610 N N . CYS B 17 ? 0.1271 0.1355 0.1663 0.0115 0.0111 -0.0215 15 CYS B N 1611 C CA . CYS B 17 ? 0.1511 0.1528 0.1964 0.0104 0.0154 -0.0239 15 CYS B CA 1612 C C . CYS B 17 ? 0.1487 0.1481 0.1937 0.0059 0.0156 -0.0276 15 CYS B C 1613 O O . CYS B 17 ? 0.1997 0.2015 0.2469 0.0049 0.0143 -0.0247 15 CYS B O 1614 C CB . CYS B 17 ? 0.1011 0.1011 0.1551 0.0139 0.0172 -0.0181 15 CYS B CB 1615 S SG . CYS B 17 ? 0.2250 0.2289 0.2819 0.0188 0.0165 -0.0146 15 CYS B SG 1616 N N . HIS B 18 ? 0.1265 0.1214 0.1687 0.0027 0.0175 -0.0343 16 HIS B N 1617 C CA . HIS B 18 ? 0.2072 0.2005 0.2486 -0.0026 0.0170 -0.0391 16 HIS B CA 1618 C C . HIS B 18 ? 0.1178 0.1016 0.1659 -0.0046 0.0222 -0.0427 16 HIS B C 1619 O O . HIS B 18 ? 0.2707 0.2488 0.3189 -0.0036 0.0262 -0.0463 16 HIS B O 1620 C CB . HIS B 18 ? 0.1108 0.1064 0.1416 -0.0056 0.0143 -0.0446 16 HIS B CB 1621 C CG . HIS B 18 ? 0.2350 0.2385 0.2597 -0.0038 0.0092 -0.0411 16 HIS B CG 1622 N ND1 . HIS B 18 ? 0.2598 0.2693 0.2819 -0.0059 0.0044 -0.0414 16 HIS B ND1 1623 C CD2 . HIS B 18 ? 0.2001 0.2060 0.2218 0.0002 0.0083 -0.0373 16 HIS B CD2 1624 C CE1 . HIS B 18 ? 0.1771 0.1915 0.1946 -0.0028 0.0011 -0.0378 16 HIS B CE1 1625 N NE2 . HIS B 18 ? 0.1150 0.1269 0.1318 0.0005 0.0034 -0.0356 16 HIS B NE2 1626 N N . PHE B 19 ? 0.1716 0.1534 0.2258 -0.0075 0.0227 -0.0418 17 PHE B N 1627 C CA . PHE B 19 ? 0.1315 0.1026 0.1936 -0.0093 0.0280 -0.0443 17 PHE B CA 1628 C C . PHE B 19 ? 0.2735 0.2414 0.3345 -0.0168 0.0280 -0.0523 17 PHE B C 1629 O O . PHE B 19 ? 0.2823 0.2572 0.3425 -0.0207 0.0238 -0.0523 17 PHE B O 1630 C CB . PHE B 19 ? 0.1306 0.0996 0.2020 -0.0067 0.0298 -0.0359 17 PHE B CB 1631 C CG . PHE B 19 ? 0.1620 0.1343 0.2343 0.0004 0.0292 -0.0282 17 PHE B CG 1632 C CD1 . PHE B 19 ? 0.1688 0.1351 0.2463 0.0049 0.0329 -0.0272 17 PHE B CD1 1633 C CD2 . PHE B 19 ? 0.1138 0.0957 0.1823 0.0025 0.0249 -0.0224 17 PHE B CD2 1634 C CE1 . PHE B 19 ? 0.1751 0.1460 0.2542 0.0110 0.0315 -0.0203 17 PHE B CE1 1635 C CE2 . PHE B 19 ? 0.1524 0.1377 0.2211 0.0083 0.0239 -0.0161 17 PHE B CE2 1636 C CZ . PHE B 19 ? 0.1465 0.1269 0.2206 0.0123 0.0267 -0.0149 17 PHE B CZ 1637 N N . PHE B 20 ? 0.2413 0.1990 0.3030 -0.0189 0.0328 -0.0595 18 PHE B N 1638 C CA . PHE B 20 ? 0.3390 0.2919 0.3991 -0.0267 0.0332 -0.0687 18 PHE B CA 1639 C C . PHE B 20 ? 0.3582 0.2967 0.4283 -0.0276 0.0402 -0.0706 18 PHE B C 1640 O O . PHE B 20 ? 0.3501 0.2810 0.4230 -0.0227 0.0455 -0.0707 18 PHE B O 1641 C CB . PHE B 20 ? 0.4377 0.3908 0.4853 -0.0292 0.0326 -0.0777 18 PHE B CB 1642 C CG . PHE B 20 ? 0.5100 0.4747 0.5474 -0.0268 0.0269 -0.0747 18 PHE B CG 1643 C CD1 . PHE B 20 ? 0.4487 0.4154 0.4849 -0.0201 0.0281 -0.0694 18 PHE B CD1 1644 C CD2 . PHE B 20 ? 0.5668 0.5400 0.5962 -0.0313 0.0203 -0.0774 18 PHE B CD2 1645 C CE1 . PHE B 20 ? 0.3931 0.3686 0.4201 -0.0183 0.0235 -0.0668 18 PHE B CE1 1646 C CE2 . PHE B 20 ? 0.5482 0.5303 0.5684 -0.0286 0.0154 -0.0741 18 PHE B CE2 1647 C CZ . PHE B 20 ? 0.4457 0.4281 0.4646 -0.0223 0.0173 -0.0689 18 PHE B CZ 1648 N N . ASN B 21 ? 0.4386 0.3733 0.5152 -0.0336 0.0407 -0.0720 19 ASN B N 1649 C CA . ASN B 21 ? 0.4516 0.3707 0.5383 -0.0349 0.0476 -0.0738 19 ASN B CA 1650 C C . ASN B 21 ? 0.3889 0.3030 0.4841 -0.0264 0.0515 -0.0634 19 ASN B C 1651 O O . ASN B 21 ? 0.4478 0.3526 0.5461 -0.0218 0.0568 -0.0648 19 ASN B O 1652 C CB . ASN B 21 ? 0.6066 0.5187 0.6869 -0.0366 0.0509 -0.0833 19 ASN B CB 1653 C CG . ASN B 21 ? 0.7058 0.6051 0.7938 -0.0374 0.0568 -0.0837 19 ASN B CG 1654 O OD1 . ASN B 21 ? 0.6510 0.5453 0.7492 -0.0381 0.0584 -0.0779 19 ASN B OD1 1655 N ND2 . ASN B 21 ? 0.8193 0.7132 0.9023 -0.0372 0.0602 -0.0904 19 ASN B ND2 1656 N N . GLY B 22 ? 0.3159 0.2372 0.4146 -0.0239 0.0487 -0.0527 20 GLY B N 1657 C CA . GLY B 22 ? 0.2990 0.2180 0.4035 -0.0156 0.0508 -0.0421 20 GLY B CA 1658 C C . GLY B 22 ? 0.3636 0.2897 0.4626 -0.0088 0.0489 -0.0410 20 GLY B C 1659 O O . GLY B 22 ? 0.4164 0.3546 0.5068 -0.0088 0.0436 -0.0411 20 GLY B O 1660 N N . THR B 23 ? 0.3110 0.2292 0.4160 -0.0029 0.0534 -0.0398 21 THR B N 1661 C CA . THR B 23 ? 0.3790 0.3035 0.4810 0.0031 0.0527 -0.0397 21 THR B CA 1662 C C . THR B 23 ? 0.3473 0.2646 0.4483 0.0023 0.0579 -0.0505 21 THR B C 1663 O O . THR B 23 ? 0.3474 0.2677 0.4494 0.0076 0.0595 -0.0500 21 THR B O 1664 C CB . THR B 23 ? 0.4312 0.3561 0.5419 0.0116 0.0532 -0.0290 21 THR B CB 1665 O OG1 . THR B 23 ? 0.3951 0.3059 0.5171 0.0134 0.0589 -0.0270 21 THR B OG1 1666 C CG2 . THR B 23 ? 0.4105 0.3453 0.5184 0.0127 0.0475 -0.0189 21 THR B CG2 1667 N N . GLU B 24 ? 0.3367 0.2477 0.4340 -0.0049 0.0597 -0.0592 22 GLU B N 1668 C CA . GLU B 24 ? 0.4296 0.3378 0.5214 -0.0065 0.0631 -0.0675 22 GLU B CA 1669 C C . GLU B 24 ? 0.3913 0.3087 0.4715 -0.0068 0.0608 -0.0720 22 GLU B C 1670 O O . GLU B 24 ? 0.4053 0.3234 0.4837 -0.0039 0.0640 -0.0740 22 GLU B O 1671 C CB . GLU B 24 ? 0.4751 0.3764 0.5636 -0.0146 0.0641 -0.0752 22 GLU B CB 1672 C CG . GLU B 24 ? 0.6635 0.5535 0.7631 -0.0142 0.0685 -0.0722 22 GLU B CG 1673 C CD . GLU B 24 ? 0.7506 0.6349 0.8565 -0.0078 0.0741 -0.0710 22 GLU B CD 1674 O OE1 . GLU B 24 ? 0.8137 0.6968 0.9137 -0.0090 0.0769 -0.0788 22 GLU B OE1 1675 O OE2 . GLU B 24 ? 0.6973 0.5788 0.8139 -0.0016 0.0755 -0.0618 22 GLU B OE2 1676 N N . ARG B 25 ? 0.3195 0.2439 0.3922 -0.0102 0.0554 -0.0731 23 ARG B N 1677 C CA . ARG B 25 ? 0.3201 0.2532 0.3810 -0.0104 0.0527 -0.0760 23 ARG B CA 1678 C C . ARG B 25 ? 0.3228 0.2678 0.3828 -0.0073 0.0461 -0.0665 23 ARG B C 1679 O O . ARG B 25 ? 0.3073 0.2564 0.3679 -0.0095 0.0415 -0.0624 23 ARG B O 1680 C CB . ARG B 25 ? 0.4353 0.3703 0.4829 -0.0183 0.0496 -0.0842 23 ARG B CB 1681 C CG . ARG B 25 ? 0.5920 0.5198 0.6362 -0.0218 0.0537 -0.0911 23 ARG B CG 1682 C CD . ARG B 25 ? 0.7340 0.6647 0.7659 -0.0218 0.0551 -0.0953 23 ARG B CD 1683 N NE . ARG B 25 ? 0.8125 0.7358 0.8413 -0.0245 0.0598 -0.1022 23 ARG B NE 1684 C CZ . ARG B 25 ? 0.8056 0.7291 0.8216 -0.0308 0.0576 -0.1092 23 ARG B CZ 1685 N NH1 . ARG B 25 ? 0.8338 0.7652 0.8393 -0.0346 0.0504 -0.1094 23 ARG B NH1 1686 N NH2 . ARG B 25 ? 0.7058 0.6220 0.7193 -0.0329 0.0624 -0.1157 23 ARG B NH2 1687 N N . VAL B 26 ? 0.2640 0.2150 0.3228 -0.0023 0.0460 -0.0630 24 VAL B N 1688 C CA . VAL B 26 ? 0.2180 0.1794 0.2758 0.0009 0.0402 -0.0543 24 VAL B CA 1689 C C . VAL B 26 ? 0.1912 0.1595 0.2389 0.0010 0.0384 -0.0559 24 VAL B C 1690 O O . VAL B 26 ? 0.2399 0.2060 0.2866 0.0020 0.0432 -0.0600 24 VAL B O 1691 C CB . VAL B 26 ? 0.2098 0.1717 0.2794 0.0077 0.0414 -0.0459 24 VAL B CB 1692 C CG1 . VAL B 26 ? 0.1893 0.1619 0.2562 0.0102 0.0353 -0.0382 24 VAL B CG1 1693 C CG2 . VAL B 26 ? 0.2484 0.2022 0.3278 0.0079 0.0437 -0.0430 24 VAL B CG2 1694 N N . ARG B 27 ? 0.2046 0.1808 0.2452 0.0001 0.0322 -0.0524 25 ARG B N 1695 C CA . ARG B 27 ? 0.2161 0.1979 0.2475 0.0004 0.0302 -0.0525 25 ARG B CA 1696 C C . ARG B 27 ? 0.1658 0.1549 0.1994 0.0042 0.0260 -0.0446 25 ARG B C 1697 O O . ARG B 27 ? 0.2319 0.2240 0.2674 0.0045 0.0221 -0.0403 25 ARG B O 1698 C CB . ARG B 27 ? 0.3206 0.3038 0.3392 -0.0048 0.0266 -0.0569 25 ARG B CB 1699 C CG . ARG B 27 ? 0.2870 0.2741 0.2944 -0.0050 0.0249 -0.0568 25 ARG B CG 1700 C CD . ARG B 27 ? 0.2909 0.2784 0.2856 -0.0101 0.0216 -0.0615 25 ARG B CD 1701 N NE . ARG B 27 ? 0.3900 0.3807 0.3730 -0.0102 0.0190 -0.0597 25 ARG B NE 1702 C CZ . ARG B 27 ? 0.5260 0.5212 0.5015 -0.0113 0.0124 -0.0575 25 ARG B CZ 1703 N NH1 . ARG B 27 ? 0.5713 0.5698 0.5506 -0.0126 0.0077 -0.0571 25 ARG B NH1 1704 N NH2 . ARG B 27 ? 0.4992 0.4957 0.4643 -0.0111 0.0107 -0.0552 25 ARG B NH2 1705 N N . PHE B 28 ? 0.2133 0.2054 0.2466 0.0066 0.0270 -0.0431 26 PHE B N 1706 C CA . PHE B 28 ? 0.1492 0.1477 0.1843 0.0097 0.0232 -0.0367 26 PHE B CA 1707 C C . PHE B 28 ? 0.1637 0.1653 0.1883 0.0080 0.0206 -0.0372 26 PHE B C 1708 O O . PHE B 28 ? 0.2212 0.2212 0.2406 0.0063 0.0237 -0.0408 26 PHE B O 1709 C CB . PHE B 28 ? 0.1704 0.1707 0.2162 0.0138 0.0259 -0.0339 26 PHE B CB 1710 C CG . PHE B 28 ? 0.1987 0.2061 0.2448 0.0158 0.0221 -0.0291 26 PHE B CG 1711 C CD1 . PHE B 28 ? 0.1744 0.1852 0.2204 0.0173 0.0172 -0.0240 26 PHE B CD1 1712 C CD2 . PHE B 28 ? 0.0886 0.0991 0.1348 0.0158 0.0237 -0.0300 26 PHE B CD2 1713 C CE1 . PHE B 28 ? 0.1634 0.1800 0.2088 0.0186 0.0137 -0.0206 26 PHE B CE1 1714 C CE2 . PHE B 28 ? 0.1650 0.1817 0.2119 0.0168 0.0199 -0.0263 26 PHE B CE2 1715 C CZ . PHE B 28 ? 0.0929 0.1123 0.1389 0.0182 0.0148 -0.0219 26 PHE B CZ 1716 N N . LEU B 29 ? 0.1849 0.1904 0.2062 0.0087 0.0154 -0.0334 27 LEU B N 1717 C CA . LEU B 29 ? 0.1491 0.1565 0.1615 0.0078 0.0127 -0.0328 27 LEU B CA 1718 C C . LEU B 29 ? 0.1022 0.1137 0.1172 0.0103 0.0101 -0.0283 27 LEU B C 1719 O O . LEU B 29 ? 0.1009 0.1149 0.1194 0.0123 0.0076 -0.0252 27 LEU B O 1720 C CB . LEU B 29 ? 0.2115 0.2193 0.2164 0.0060 0.0086 -0.0333 27 LEU B CB 1721 C CG . LEU B 29 ? 0.2291 0.2340 0.2291 0.0024 0.0093 -0.0382 27 LEU B CG 1722 C CD1 . LEU B 29 ? 0.2505 0.2586 0.2451 0.0013 0.0038 -0.0374 27 LEU B CD1 1723 C CD2 . LEU B 29 ? 0.1249 0.1263 0.1175 0.0001 0.0130 -0.0421 27 LEU B CD2 1724 N N . ASP B 30 ? 0.0841 0.0961 0.0973 0.0099 0.0112 -0.0283 28 ASP B N 1725 C CA . ASP B 30 ? 0.0796 0.0950 0.0944 0.0113 0.0085 -0.0251 28 ASP B CA 1726 C C . ASP B 30 ? 0.1351 0.1482 0.1399 0.0099 0.0062 -0.0250 28 ASP B C 1727 O O . ASP B 30 ? 0.1285 0.1389 0.1280 0.0077 0.0083 -0.0263 28 ASP B O 1728 C CB . ASP B 30 ? 0.0793 0.0975 0.1014 0.0114 0.0114 -0.0252 28 ASP B CB 1729 C CG . ASP B 30 ? 0.2357 0.2593 0.2637 0.0133 0.0080 -0.0220 28 ASP B CG 1730 O OD1 . ASP B 30 ? 0.2005 0.2257 0.2303 0.0155 0.0053 -0.0195 28 ASP B OD1 1731 O OD2 . ASP B 30 ? 0.1467 0.1732 0.1773 0.0122 0.0082 -0.0220 28 ASP B OD2 1732 N N . ARG B 31 ? 0.0795 0.0934 0.0818 0.0114 0.0023 -0.0231 29 ARG B N 1733 C CA . ARG B 31 ? 0.1472 0.1581 0.1408 0.0109 -0.0001 -0.0228 29 ARG B CA 1734 C C . ARG B 31 ? 0.1922 0.2029 0.1850 0.0122 -0.0022 -0.0211 29 ARG B C 1735 O O . ARG B 31 ? 0.2012 0.2150 0.1977 0.0141 -0.0037 -0.0202 29 ARG B O 1736 C CB . ARG B 31 ? 0.0832 0.0950 0.0749 0.0117 -0.0025 -0.0228 29 ARG B CB 1737 C CG . ARG B 31 ? 0.1646 0.1765 0.1580 0.0099 -0.0005 -0.0253 29 ARG B CG 1738 C CD . ARG B 31 ? 0.0852 0.0994 0.0784 0.0099 -0.0035 -0.0255 29 ARG B CD 1739 N NE . ARG B 31 ? 0.0905 0.1039 0.0754 0.0095 -0.0066 -0.0252 29 ARG B NE 1740 C CZ . ARG B 31 ? 0.1789 0.1957 0.1636 0.0100 -0.0103 -0.0248 29 ARG B CZ 1741 N NH1 . ARG B 31 ? 0.1201 0.1413 0.1124 0.0103 -0.0107 -0.0250 29 ARG B NH1 1742 N NH2 . ARG B 31 ? 0.1152 0.1314 0.0926 0.0103 -0.0136 -0.0236 29 ARG B NH2 1743 N N . TYR B 32 ? 0.1563 0.1625 0.1432 0.0109 -0.0021 -0.0208 30 TYR B N 1744 C CA . TYR B 32 ? 0.1591 0.1633 0.1449 0.0115 -0.0038 -0.0201 30 TYR B CA 1745 C C . TYR B 32 ? 0.2225 0.2216 0.2013 0.0131 -0.0059 -0.0188 30 TYR B C 1746 O O . TYR B 32 ? 0.1141 0.1097 0.0872 0.0121 -0.0057 -0.0178 30 TYR B O 1747 C CB . TYR B 32 ? 0.1451 0.1478 0.1322 0.0083 -0.0014 -0.0207 30 TYR B CB 1748 C CG . TYR B 32 ? 0.1010 0.1104 0.0974 0.0079 -0.0003 -0.0215 30 TYR B CG 1749 C CD1 . TYR B 32 ? 0.0837 0.0960 0.0844 0.0078 0.0024 -0.0221 30 TYR B CD1 1750 C CD2 . TYR B 32 ? 0.1430 0.1560 0.1438 0.0079 -0.0023 -0.0217 30 TYR B CD2 1751 C CE1 . TYR B 32 ? 0.1389 0.1571 0.1492 0.0084 0.0033 -0.0221 30 TYR B CE1 1752 C CE2 . TYR B 32 ? 0.0985 0.1187 0.1082 0.0082 -0.0023 -0.0215 30 TYR B CE2 1753 C CZ . TYR B 32 ? 0.1258 0.1485 0.1409 0.0088 0.0006 -0.0213 30 TYR B CZ 1754 O OH . TYR B 32 ? 0.2072 0.2366 0.2323 0.0100 0.0008 -0.0205 30 TYR B OH 1755 N N . PHE B 33 ? 0.2119 0.2105 0.1910 0.0157 -0.0079 -0.0186 31 PHE B N 1756 C CA . PHE B 33 ? 0.1696 0.1641 0.1444 0.0184 -0.0099 -0.0172 31 PHE B CA 1757 C C . PHE B 33 ? 0.1810 0.1692 0.1539 0.0192 -0.0099 -0.0176 31 PHE B C 1758 O O . PHE B 33 ? 0.1640 0.1539 0.1396 0.0187 -0.0096 -0.0198 31 PHE B O 1759 C CB . PHE B 33 ? 0.1173 0.1177 0.0955 0.0218 -0.0116 -0.0170 31 PHE B CB 1760 C CG . PHE B 33 ? 0.0933 0.0995 0.0744 0.0205 -0.0115 -0.0173 31 PHE B CG 1761 C CD1 . PHE B 33 ? 0.0837 0.0941 0.0699 0.0193 -0.0098 -0.0184 31 PHE B CD1 1762 C CD2 . PHE B 33 ? 0.1368 0.1440 0.1157 0.0205 -0.0132 -0.0165 31 PHE B CD2 1763 C CE1 . PHE B 33 ? 0.1116 0.1255 0.1009 0.0181 -0.0091 -0.0189 31 PHE B CE1 1764 C CE2 . PHE B 33 ? 0.1093 0.1209 0.0907 0.0186 -0.0129 -0.0178 31 PHE B CE2 1765 C CZ . PHE B 33 ? 0.0840 0.0982 0.0709 0.0174 -0.0105 -0.0191 31 PHE B CZ 1766 N N . TYR B 34 ? 0.1630 0.1436 0.1310 0.0203 -0.0105 -0.0156 32 TYR B N 1767 C CA . TYR B 34 ? 0.1519 0.1248 0.1185 0.0217 -0.0104 -0.0162 32 TYR B CA 1768 C C . TYR B 34 ? 0.1812 0.1530 0.1478 0.0274 -0.0122 -0.0146 32 TYR B C 1769 O O . TYR B 34 ? 0.1280 0.0982 0.0918 0.0290 -0.0139 -0.0111 32 TYR B O 1770 C CB . TYR B 34 ? 0.1387 0.1018 0.1006 0.0183 -0.0087 -0.0147 32 TYR B CB 1771 C CG . TYR B 34 ? 0.1581 0.1109 0.1186 0.0191 -0.0081 -0.0157 32 TYR B CG 1772 C CD1 . TYR B 34 ? 0.1385 0.0918 0.1019 0.0175 -0.0075 -0.0203 32 TYR B CD1 1773 C CD2 . TYR B 34 ? 0.1515 0.0936 0.1076 0.0211 -0.0082 -0.0121 32 TYR B CD2 1774 C CE1 . TYR B 34 ? 0.1952 0.1382 0.1570 0.0176 -0.0066 -0.0225 32 TYR B CE1 1775 C CE2 . TYR B 34 ? 0.1621 0.0930 0.1174 0.0218 -0.0071 -0.0134 32 TYR B CE2 1776 C CZ . TYR B 34 ? 0.2289 0.1600 0.1871 0.0198 -0.0061 -0.0192 32 TYR B CZ 1777 O OH . TYR B 34 ? 0.2063 0.1255 0.1635 0.0198 -0.0047 -0.0217 32 TYR B OH 1778 N N . HIS B 35 ? 0.2058 0.1793 0.1756 0.0305 -0.0120 -0.0173 33 HIS B N 1779 C CA . HIS B 35 ? 0.2015 0.1779 0.1744 0.0363 -0.0132 -0.0163 33 HIS B CA 1780 C C . HIS B 35 ? 0.2403 0.2276 0.2168 0.0366 -0.0149 -0.0147 33 HIS B C 1781 O O . HIS B 35 ? 0.2159 0.2107 0.1955 0.0348 -0.0141 -0.0164 33 HIS B O 1782 C CB . HIS B 35 ? 0.2111 0.1782 0.1817 0.0400 -0.0142 -0.0131 33 HIS B CB 1783 C CG . HIS B 35 ? 0.2182 0.1725 0.1853 0.0389 -0.0121 -0.0147 33 HIS B CG 1784 N ND1 . HIS B 35 ? 0.1445 0.0974 0.1118 0.0367 -0.0099 -0.0199 33 HIS B ND1 1785 C CD2 . HIS B 35 ? 0.2557 0.1977 0.2189 0.0394 -0.0119 -0.0117 33 HIS B CD2 1786 C CE1 . HIS B 35 ? 0.2385 0.1788 0.2027 0.0354 -0.0084 -0.0209 33 HIS B CE1 1787 N NE2 . HIS B 35 ? 0.2570 0.1899 0.2189 0.0371 -0.0093 -0.0157 33 HIS B NE2 1788 N N . GLN B 36 ? 0.1928 0.1806 0.1688 0.0386 -0.0176 -0.0112 34 GLN B N 1789 C CA . GLN B 36 ? 0.1791 0.1766 0.1580 0.0380 -0.0198 -0.0102 34 GLN B CA 1790 C C . GLN B 36 ? 0.2391 0.2355 0.2121 0.0335 -0.0208 -0.0089 34 GLN B C 1791 O O . GLN B 36 ? 0.2974 0.3007 0.2718 0.0316 -0.0222 -0.0094 34 GLN B O 1792 C CB . GLN B 36 ? 0.3203 0.3216 0.3035 0.0434 -0.0230 -0.0077 34 GLN B CB 1793 C CG . GLN B 36 ? 0.4204 0.4343 0.4118 0.0443 -0.0245 -0.0082 34 GLN B CG 1794 C CD . GLN B 36 ? 0.4986 0.5169 0.4956 0.0500 -0.0279 -0.0054 34 GLN B CD 1795 O OE1 . GLN B 36 ? 0.5344 0.5467 0.5321 0.0550 -0.0274 -0.0041 34 GLN B OE1 1796 N NE2 . GLN B 36 ? 0.4415 0.4703 0.4432 0.0493 -0.0317 -0.0044 34 GLN B NE2 1797 N N . GLU B 37 ? 0.3090 0.2959 0.2750 0.0316 -0.0198 -0.0075 35 GLU B N 1798 C CA A GLU B 37 ? 0.3017 0.2862 0.2604 0.0276 -0.0198 -0.0060 35 GLU B CA 1799 C CA B GLU B 37 ? 0.2786 0.2635 0.2375 0.0276 -0.0198 -0.0061 35 GLU B CA 1800 C C . GLU B 37 ? 0.2406 0.2267 0.1997 0.0225 -0.0162 -0.0092 35 GLU B C 1801 O O . GLU B 37 ? 0.1815 0.1642 0.1420 0.0209 -0.0134 -0.0106 35 GLU B O 1802 C CB A GLU B 37 ? 0.3781 0.3512 0.3295 0.0279 -0.0195 -0.0022 35 GLU B CB 1803 C CB B GLU B 37 ? 0.3909 0.3650 0.3420 0.0280 -0.0200 -0.0020 35 GLU B CB 1804 C CG A GLU B 37 ? 0.3754 0.3438 0.3177 0.0231 -0.0177 -0.0005 35 GLU B CG 1805 C CG B GLU B 37 ? 0.5357 0.5087 0.4865 0.0336 -0.0243 0.0023 35 GLU B CG 1806 C CD A GLU B 37 ? 0.3452 0.3012 0.2823 0.0222 -0.0156 0.0025 35 GLU B CD 1807 C CD B GLU B 37 ? 0.5970 0.5588 0.5387 0.0339 -0.0248 0.0077 35 GLU B CD 1808 O OE1 A GLU B 37 ? 0.3429 0.2954 0.2776 0.0172 -0.0115 0.0015 35 GLU B OE1 1809 O OE1 B GLU B 37 ? 0.6265 0.5844 0.5600 0.0289 -0.0227 0.0087 35 GLU B OE1 1810 O OE2 A GLU B 37 ? 0.3414 0.2910 0.2777 0.0266 -0.0176 0.0060 35 GLU B OE2 1811 O OE2 B GLU B 37 ? 0.5766 0.5330 0.5195 0.0392 -0.0267 0.0112 35 GLU B OE2 1812 N N . GLU B 38 ? 0.1167 0.1083 0.0753 0.0200 -0.0163 -0.0104 36 GLU B N 1813 C CA . GLU B 38 ? 0.1786 0.1709 0.1377 0.0157 -0.0124 -0.0131 36 GLU B CA 1814 C C . GLU B 38 ? 0.1808 0.1658 0.1321 0.0127 -0.0098 -0.0116 36 GLU B C 1815 O O . GLU B 38 ? 0.1506 0.1324 0.0933 0.0122 -0.0112 -0.0090 36 GLU B O 1816 C CB . GLU B 38 ? 0.1106 0.1088 0.0706 0.0139 -0.0126 -0.0154 36 GLU B CB 1817 C CG . GLU B 38 ? 0.1676 0.1668 0.1309 0.0107 -0.0081 -0.0184 36 GLU B CG 1818 C CD . GLU B 38 ? 0.1800 0.1831 0.1446 0.0089 -0.0078 -0.0214 36 GLU B CD 1819 O OE1 . GLU B 38 ? 0.1713 0.1764 0.1323 0.0089 -0.0112 -0.0213 36 GLU B OE1 1820 O OE2 . GLU B 38 ? 0.1793 0.1835 0.1491 0.0075 -0.0041 -0.0238 36 GLU B OE2 1821 N N . TYR B 39 ? 0.1410 0.1241 0.0953 0.0103 -0.0062 -0.0129 37 TYR B N 1822 C CA A TYR B 39 ? 0.1296 0.1060 0.0777 0.0068 -0.0029 -0.0113 37 TYR B CA 1823 C CA B TYR B 39 ? 0.1897 0.1662 0.1381 0.0068 -0.0029 -0.0113 37 TYR B CA 1824 C C . TYR B 39 ? 0.1283 0.1077 0.0780 0.0027 0.0020 -0.0138 37 TYR B C 1825 O O . TYR B 39 ? 0.1876 0.1628 0.1306 -0.0005 0.0054 -0.0126 37 TYR B O 1826 C CB A TYR B 39 ? 0.2180 0.1884 0.1680 0.0066 -0.0023 -0.0103 37 TYR B CB 1827 C CB B TYR B 39 ? 0.2099 0.1811 0.1611 0.0067 -0.0023 -0.0108 37 TYR B CB 1828 C CG A TYR B 39 ? 0.2023 0.1773 0.1619 0.0063 -0.0017 -0.0137 37 TYR B CG 1829 C CG B TYR B 39 ? 0.2534 0.2169 0.2000 0.0100 -0.0051 -0.0074 37 TYR B CG 1830 C CD1 A TYR B 39 ? 0.1504 0.1277 0.1141 0.0099 -0.0046 -0.0148 37 TYR B CD1 1831 C CD1 B TYR B 39 ? 0.3130 0.2764 0.2544 0.0133 -0.0087 -0.0044 37 TYR B CD1 1832 C CD2 A TYR B 39 ? 0.1831 0.1607 0.1476 0.0023 0.0019 -0.0156 37 TYR B CD2 1833 C CD2 B TYR B 39 ? 0.2353 0.1917 0.1834 0.0098 -0.0044 -0.0074 37 TYR B CD2 1834 C CE1 A TYR B 39 ? 0.1567 0.1383 0.1271 0.0094 -0.0046 -0.0176 37 TYR B CE1 1835 C CE1 B TYR B 39 ? 0.3542 0.3109 0.2928 0.0172 -0.0113 -0.0008 37 TYR B CE1 1836 C CE2 A TYR B 39 ? 0.1557 0.1387 0.1289 0.0021 0.0013 -0.0181 37 TYR B CE2 1837 C CE2 B TYR B 39 ? 0.3025 0.2506 0.2472 0.0134 -0.0065 -0.0044 37 TYR B CE2 1838 C CZ A TYR B 39 ? 0.1879 0.1725 0.1629 0.0055 -0.0022 -0.0190 37 TYR B CZ 1839 C CZ B TYR B 39 ? 0.3252 0.2735 0.2656 0.0175 -0.0099 -0.0008 37 TYR B CZ 1840 O OH A TYR B 39 ? 0.2192 0.2092 0.2006 0.0052 -0.0032 -0.0212 37 TYR B OH 1841 O OH B TYR B 39 ? 0.3391 0.2794 0.2775 0.0221 -0.0120 0.0027 37 TYR B OH 1842 N N . VAL B 40 ? 0.1923 0.1786 0.1510 0.0031 0.0029 -0.0171 38 VAL B N 1843 C CA . VAL B 40 ? 0.2300 0.2195 0.1920 0.0002 0.0079 -0.0197 38 VAL B CA 1844 C C . VAL B 40 ? 0.1707 0.1665 0.1405 0.0021 0.0074 -0.0224 38 VAL B C 1845 O O . VAL B 40 ? 0.1048 0.1034 0.0797 0.0048 0.0040 -0.0219 38 VAL B O 1846 C CB . VAL B 40 ? 0.1911 0.1812 0.1598 -0.0022 0.0113 -0.0200 38 VAL B CB 1847 C CG1 . VAL B 40 ? 0.1811 0.1758 0.1597 -0.0002 0.0084 -0.0207 38 VAL B CG1 1848 C CG2 . VAL B 40 ? 0.1573 0.1507 0.1297 -0.0049 0.0173 -0.0224 38 VAL B CG2 1849 N N . ARG B 41 ? 0.1669 0.1641 0.1371 0.0004 0.0112 -0.0251 39 ARG B N 1850 C CA . ARG B 41 ? 0.2115 0.2127 0.1893 0.0020 0.0114 -0.0276 39 ARG B CA 1851 C C . ARG B 41 ? 0.1798 0.1822 0.1627 0.0006 0.0176 -0.0309 39 ARG B C 1852 O O . ARG B 41 ? 0.2154 0.2154 0.1923 -0.0022 0.0220 -0.0324 39 ARG B O 1853 C CB . ARG B 41 ? 0.2030 0.2036 0.1751 0.0023 0.0083 -0.0285 39 ARG B CB 1854 C CG . ARG B 41 ? 0.3395 0.3368 0.3003 -0.0007 0.0101 -0.0306 39 ARG B CG 1855 C CD . ARG B 41 ? 0.3162 0.3147 0.2754 -0.0013 0.0079 -0.0335 39 ARG B CD 1856 N NE . ARG B 41 ? 0.2833 0.2846 0.2433 0.0008 0.0015 -0.0311 39 ARG B NE 1857 C CZ . ARG B 41 ? 0.3746 0.3781 0.3332 -0.0002 -0.0017 -0.0330 39 ARG B CZ 1858 N NH1 . ARG B 41 ? 0.2511 0.2534 0.2064 -0.0035 0.0007 -0.0379 39 ARG B NH1 1859 N NH2 . ARG B 41 ? 0.4269 0.4343 0.3882 0.0020 -0.0070 -0.0305 39 ARG B NH2 1860 N N . PHE B 42 ? 0.1267 0.1328 0.1208 0.0028 0.0182 -0.0317 40 PHE B N 1861 C CA . PHE B 42 ? 0.1199 0.1264 0.1202 0.0026 0.0239 -0.0352 40 PHE B CA 1862 C C . PHE B 42 ? 0.1532 0.1574 0.1522 0.0028 0.0233 -0.0378 40 PHE B C 1863 O O . PHE B 42 ? 0.1574 0.1628 0.1604 0.0047 0.0193 -0.0360 40 PHE B O 1864 C CB . PHE B 42 ? 0.0960 0.1079 0.1112 0.0053 0.0250 -0.0337 40 PHE B CB 1865 C CG . PHE B 42 ? 0.1502 0.1625 0.1744 0.0064 0.0309 -0.0368 40 PHE B CG 1866 C CD1 . PHE B 42 ? 0.1113 0.1214 0.1400 0.0084 0.0310 -0.0379 40 PHE B CD1 1867 C CD2 . PHE B 42 ? 0.1023 0.1170 0.1318 0.0056 0.0369 -0.0386 40 PHE B CD2 1868 C CE1 . PHE B 42 ? 0.1706 0.1795 0.2083 0.0100 0.0369 -0.0409 40 PHE B CE1 1869 C CE2 . PHE B 42 ? 0.1057 0.1206 0.1448 0.0074 0.0430 -0.0417 40 PHE B CE2 1870 C CZ . PHE B 42 ? 0.1062 0.1177 0.1493 0.0099 0.0429 -0.0429 40 PHE B CZ 1871 N N . ASP B 43 ? 0.1856 0.1861 0.1784 0.0003 0.0275 -0.0424 41 ASP B N 1872 C CA . ASP B 43 ? 0.2018 0.1993 0.1933 -0.0006 0.0277 -0.0464 41 ASP B CA 1873 C C . ASP B 43 ? 0.1715 0.1670 0.1717 0.0001 0.0349 -0.0506 41 ASP B C 1874 O O . ASP B 43 ? 0.2182 0.2129 0.2162 -0.0011 0.0408 -0.0534 41 ASP B O 1875 C CB . ASP B 43 ? 0.2139 0.2086 0.1896 -0.0045 0.0262 -0.0491 41 ASP B CB 1876 C CG . ASP B 43 ? 0.2259 0.2182 0.1995 -0.0066 0.0251 -0.0537 41 ASP B CG 1877 O OD1 . ASP B 43 ? 0.2044 0.1952 0.1884 -0.0055 0.0278 -0.0560 41 ASP B OD1 1878 O OD2 . ASP B 43 ? 0.1410 0.1330 0.1027 -0.0095 0.0213 -0.0550 41 ASP B OD2 1879 N N . SER B 44 ? 0.1955 0.1899 0.2060 0.0023 0.0350 -0.0508 42 SER B N 1880 C CA . SER B 44 ? 0.1337 0.1253 0.1542 0.0039 0.0420 -0.0544 42 SER B CA 1881 C C . SER B 44 ? 0.1553 0.1409 0.1669 0.0003 0.0477 -0.0624 42 SER B C 1882 O O . SER B 44 ? 0.1767 0.1598 0.1942 0.0013 0.0553 -0.0666 42 SER B O 1883 C CB . SER B 44 ? 0.1486 0.1383 0.1806 0.0068 0.0408 -0.0523 42 SER B CB 1884 O OG . SER B 44 ? 0.2763 0.2620 0.3025 0.0037 0.0381 -0.0548 42 SER B OG 1885 N N . ASP B 45 ? 0.1436 0.1273 0.1409 -0.0040 0.0441 -0.0648 43 ASP B N 1886 C CA . ASP B 45 ? 0.2244 0.2031 0.2093 -0.0084 0.0483 -0.0726 43 ASP B CA 1887 C C . ASP B 45 ? 0.2798 0.2599 0.2580 -0.0092 0.0531 -0.0724 43 ASP B C 1888 O O . ASP B 45 ? 0.2326 0.2095 0.2047 -0.0114 0.0573 -0.0761 43 ASP B O 1889 C CB . ASP B 45 ? 0.3201 0.2988 0.2911 -0.0126 0.0414 -0.0736 43 ASP B CB 1890 C CG . ASP B 45 ? 0.3368 0.3130 0.3133 -0.0138 0.0385 -0.0761 43 ASP B CG 1891 O OD1 . ASP B 45 ? 0.3922 0.3658 0.3828 -0.0110 0.0416 -0.0758 43 ASP B OD1 1892 O OD2 . ASP B 45 ? 0.3270 0.3040 0.2939 -0.0178 0.0331 -0.0781 43 ASP B OD2 1893 N N . VAL B 46 ? 0.1561 0.1411 0.1358 -0.0076 0.0516 -0.0670 44 VAL B N 1894 C CA . VAL B 46 ? 0.1758 0.1621 0.1491 -0.0092 0.0566 -0.0668 44 VAL B CA 1895 C C . VAL B 46 ? 0.1715 0.1620 0.1616 -0.0058 0.0625 -0.0655 44 VAL B C 1896 O O . VAL B 46 ? 0.1669 0.1575 0.1581 -0.0065 0.0688 -0.0672 44 VAL B O 1897 C CB . VAL B 46 ? 0.2358 0.2243 0.1988 -0.0106 0.0503 -0.0606 44 VAL B CB 1898 C CG1 . VAL B 46 ? 0.1647 0.1541 0.1230 -0.0125 0.0560 -0.0594 44 VAL B CG1 1899 C CG2 . VAL B 46 ? 0.2418 0.2273 0.1882 -0.0138 0.0445 -0.0616 44 VAL B CG2 1900 N N . GLY B 47 ? 0.1666 0.1619 0.1702 -0.0020 0.0578 -0.0600 45 GLY B N 1901 C CA . GLY B 47 ? 0.1966 0.1974 0.2177 0.0016 0.0618 -0.0584 45 GLY B CA 1902 C C . GLY B 47 ? 0.1496 0.1564 0.1717 0.0005 0.0611 -0.0540 45 GLY B C 1903 O O . GLY B 47 ? 0.2201 0.2333 0.2564 0.0024 0.0647 -0.0530 45 GLY B O 1904 N N . GLU B 48 ? 0.1333 0.1381 0.1410 -0.0028 0.0565 -0.0515 46 GLU B N 1905 C CA . GLU B 48 ? 0.1758 0.1842 0.1831 -0.0044 0.0550 -0.0470 46 GLU B CA 1906 C C . GLU B 48 ? 0.1747 0.1804 0.1717 -0.0051 0.0464 -0.0429 46 GLU B C 1907 O O . GLU B 48 ? 0.1655 0.1670 0.1534 -0.0051 0.0427 -0.0438 46 GLU B O 1908 C CB . GLU B 48 ? 0.2023 0.2091 0.2006 -0.0087 0.0625 -0.0489 46 GLU B CB 1909 C CG . GLU B 48 ? 0.3188 0.3307 0.3297 -0.0084 0.0720 -0.0521 46 GLU B CG 1910 C CD . GLU B 48 ? 0.3992 0.4095 0.3996 -0.0133 0.0798 -0.0533 46 GLU B CD 1911 O OE1 . GLU B 48 ? 0.2920 0.2962 0.2737 -0.0168 0.0775 -0.0516 46 GLU B OE1 1912 O OE2 . GLU B 48 ? 0.4287 0.4444 0.4401 -0.0135 0.0882 -0.0554 46 GLU B OE2 1913 N N . TYR B 49 ? 0.1832 0.1913 0.1825 -0.0057 0.0434 -0.0387 47 TYR B N 1914 C CA . TYR B 49 ? 0.1209 0.1254 0.1104 -0.0061 0.0365 -0.0350 47 TYR B CA 1915 C C . TYR B 49 ? 0.2289 0.2271 0.2013 -0.0096 0.0381 -0.0345 47 TYR B C 1916 O O . TYR B 49 ? 0.2428 0.2402 0.2117 -0.0128 0.0447 -0.0356 47 TYR B O 1917 C CB . TYR B 49 ? 0.1143 0.1223 0.1115 -0.0060 0.0335 -0.0316 47 TYR B CB 1918 C CG . TYR B 49 ? 0.1033 0.1168 0.1126 -0.0022 0.0289 -0.0307 47 TYR B CG 1919 C CD1 . TYR B 49 ? 0.1423 0.1630 0.1666 -0.0006 0.0313 -0.0314 47 TYR B CD1 1920 C CD2 . TYR B 49 ? 0.1754 0.1873 0.1811 0.0000 0.0223 -0.0287 47 TYR B CD2 1921 C CE1 . TYR B 49 ? 0.1294 0.1551 0.1634 0.0029 0.0267 -0.0296 47 TYR B CE1 1922 C CE2 . TYR B 49 ? 0.0961 0.1129 0.1110 0.0032 0.0186 -0.0275 47 TYR B CE2 1923 C CZ . TYR B 49 ? 0.1425 0.1658 0.1707 0.0046 0.0205 -0.0277 47 TYR B CZ 1924 O OH . TYR B 49 ? 0.1631 0.1912 0.1991 0.0078 0.0164 -0.0255 47 TYR B OH 1925 N N . ARG B 50 ? 0.1685 0.1628 0.1305 -0.0090 0.0319 -0.0325 48 ARG B N 1926 C CA . ARG B 50 ? 0.2247 0.2132 0.1701 -0.0116 0.0316 -0.0304 48 ARG B CA 1927 C C . ARG B 50 ? 0.2334 0.2189 0.1750 -0.0100 0.0247 -0.0253 48 ARG B C 1928 O O . ARG B 50 ? 0.2297 0.2175 0.1768 -0.0067 0.0191 -0.0249 48 ARG B O 1929 C CB . ARG B 50 ? 0.1779 0.1647 0.1124 -0.0125 0.0311 -0.0337 48 ARG B CB 1930 C CG . ARG B 50 ? 0.2618 0.2494 0.1972 -0.0144 0.0390 -0.0397 48 ARG B CG 1931 C CD . ARG B 50 ? 0.2768 0.2618 0.2026 -0.0183 0.0463 -0.0395 48 ARG B CD 1932 N NE . ARG B 50 ? 0.3786 0.3642 0.3048 -0.0199 0.0547 -0.0460 48 ARG B NE 1933 C CZ . ARG B 50 ? 0.4079 0.3971 0.3467 -0.0198 0.0625 -0.0481 48 ARG B CZ 1934 N NH1 . ARG B 50 ? 0.5125 0.5058 0.4643 -0.0189 0.0622 -0.0443 48 ARG B NH1 1935 N NH2 . ARG B 50 ? 0.4285 0.4178 0.3676 -0.0208 0.0707 -0.0545 48 ARG B NH2 1936 N N . ALA B 51 ? 0.2730 0.2531 0.2059 -0.0122 0.0256 -0.0214 49 ALA B N 1937 C CA . ALA B 51 ? 0.2876 0.2632 0.2167 -0.0102 0.0197 -0.0167 49 ALA B CA 1938 C C . ALA B 51 ? 0.2946 0.2696 0.2146 -0.0079 0.0137 -0.0156 49 ALA B C 1939 O O . ALA B 51 ? 0.2935 0.2675 0.2022 -0.0098 0.0147 -0.0163 49 ALA B O 1940 C CB . ALA B 51 ? 0.2258 0.1942 0.1474 -0.0132 0.0226 -0.0123 49 ALA B CB 1941 N N . VAL B 52 ? 0.2882 0.2643 0.2130 -0.0039 0.0076 -0.0140 50 VAL B N 1942 C CA . VAL B 52 ? 0.2044 0.1814 0.1231 -0.0015 0.0015 -0.0125 50 VAL B CA 1943 C C . VAL B 52 ? 0.2316 0.2015 0.1411 -0.0002 -0.0015 -0.0063 50 VAL B C 1944 O O . VAL B 52 ? 0.2854 0.2545 0.1848 0.0004 -0.0054 -0.0036 50 VAL B O 1945 C CB . VAL B 52 ? 0.2178 0.2007 0.1476 0.0023 -0.0028 -0.0142 50 VAL B CB 1946 C CG1 . VAL B 52 ? 0.1453 0.1309 0.0709 0.0046 -0.0093 -0.0126 50 VAL B CG1 1947 C CG2 . VAL B 52 ? 0.1619 0.1503 0.1005 0.0011 0.0004 -0.0194 50 VAL B CG2 1948 N N . THR B 53 ? 0.1658 0.1304 0.0792 0.0001 0.0002 -0.0039 51 THR B N 1949 C CA . THR B 53 ? 0.2981 0.2535 0.2031 0.0009 -0.0012 0.0023 51 THR B CA 1950 C C . THR B 53 ? 0.3027 0.2519 0.2075 -0.0035 0.0053 0.0031 51 THR B C 1951 O O . THR B 53 ? 0.2311 0.1849 0.1445 -0.0062 0.0096 -0.0013 51 THR B O 1952 C CB . THR B 53 ? 0.3244 0.2777 0.2355 0.0063 -0.0061 0.0044 51 THR B CB 1953 O OG1 . THR B 53 ? 0.3375 0.2908 0.2594 0.0059 -0.0037 0.0012 51 THR B OG1 1954 C CG2 . THR B 53 ? 0.2508 0.2125 0.1658 0.0105 -0.0119 0.0031 51 THR B CG2 1955 N N . GLU B 54 ? 0.1986 0.1377 0.0946 -0.0042 0.0059 0.0090 52 GLU B N 1956 C CA . GLU B 54 ? 0.3752 0.3078 0.2710 -0.0093 0.0125 0.0102 52 GLU B CA 1957 C C . GLU B 54 ? 0.3117 0.2455 0.2219 -0.0100 0.0137 0.0064 52 GLU B C 1958 O O . GLU B 54 ? 0.2684 0.2036 0.1842 -0.0149 0.0192 0.0041 52 GLU B O 1959 C CB . GLU B 54 ? 0.4329 0.3524 0.3176 -0.0094 0.0122 0.0182 52 GLU B CB 1960 C CG . GLU B 54 ? 0.7479 0.6652 0.6161 -0.0088 0.0101 0.0235 52 GLU B CG 1961 C CD . GLU B 54 ? 0.9541 0.8575 0.8110 -0.0096 0.0113 0.0324 52 GLU B CD 1962 O OE1 . GLU B 54 ? 0.9256 0.8229 0.7810 -0.0042 0.0055 0.0376 52 GLU B OE1 1963 O OE2 . GLU B 54 ? 1.0545 0.9529 0.9048 -0.0156 0.0183 0.0345 52 GLU B OE2 1964 N N . LEU B 55 ? 0.2970 0.2312 0.2132 -0.0051 0.0085 0.0055 53 LEU B N 1965 C CA A LEU B 55 ? 0.3357 0.2712 0.2637 -0.0051 0.0084 0.0015 53 LEU B CA 1966 C CA B LEU B 55 ? 0.3252 0.2606 0.2532 -0.0052 0.0085 0.0016 53 LEU B CA 1967 C C . LEU B 55 ? 0.2822 0.2291 0.2204 -0.0075 0.0106 -0.0041 53 LEU B C 1968 O O . LEU B 55 ? 0.2047 0.1534 0.1518 -0.0098 0.0118 -0.0070 53 LEU B O 1969 C CB A LEU B 55 ? 0.3698 0.3056 0.3009 0.0013 0.0027 0.0011 53 LEU B CB 1970 C CB B LEU B 55 ? 0.3651 0.2997 0.2959 0.0010 0.0029 0.0014 53 LEU B CB 1971 C CG A LEU B 55 ? 0.3919 0.3232 0.3298 0.0023 0.0019 -0.0014 53 LEU B CG 1972 C CG B LEU B 55 ? 0.3855 0.3126 0.3214 0.0010 0.0030 0.0000 53 LEU B CG 1973 C CD1 A LEU B 55 ? 0.3722 0.2886 0.3048 0.0016 0.0032 0.0028 53 LEU B CD1 1974 C CD1 B LEU B 55 ? 0.4024 0.3219 0.3377 -0.0055 0.0080 0.0008 53 LEU B CD1 1975 C CD2 A LEU B 55 ? 0.3903 0.3267 0.3324 0.0085 -0.0025 -0.0034 53 LEU B CD2 1976 C CD2 B LEU B 55 ? 0.3733 0.2917 0.3055 0.0069 -0.0004 0.0036 53 LEU B CD2 1977 N N . GLY B 56 ? 0.2051 0.1597 0.1422 -0.0069 0.0110 -0.0056 54 GLY B N 1978 C CA . GLY B 56 ? 0.2018 0.1666 0.1492 -0.0079 0.0128 -0.0104 54 GLY B CA 1979 C C . GLY B 56 ? 0.2440 0.2113 0.1925 -0.0128 0.0194 -0.0115 54 GLY B C 1980 O O . GLY B 56 ? 0.2198 0.1956 0.1781 -0.0133 0.0216 -0.0151 54 GLY B O 1981 N N . ARG B 57 ? 0.1648 0.1247 0.1033 -0.0161 0.0231 -0.0081 55 ARG B N 1982 C CA . ARG B 57 ? 0.3071 0.2690 0.2452 -0.0210 0.0307 -0.0089 55 ARG B CA 1983 C C . ARG B 57 ? 0.3187 0.2867 0.2717 -0.0244 0.0345 -0.0117 55 ARG B C 1984 O O . ARG B 57 ? 0.3056 0.2814 0.2655 -0.0259 0.0394 -0.0148 55 ARG B O 1985 C CB . ARG B 57 ? 0.3106 0.2625 0.2341 -0.0243 0.0341 -0.0037 55 ARG B CB 1986 C CG . ARG B 57 ? 0.5482 0.4967 0.4562 -0.0219 0.0311 -0.0011 55 ARG B CG 1987 C CD . ARG B 57 ? 0.7133 0.6511 0.6062 -0.0246 0.0333 0.0056 55 ARG B CD 1988 N NE . ARG B 57 ? 0.8046 0.7403 0.6819 -0.0223 0.0294 0.0085 55 ARG B NE 1989 C CZ . ARG B 57 ? 0.9484 0.8748 0.8105 -0.0227 0.0284 0.0157 55 ARG B CZ 1990 N NH1 . ARG B 57 ? 1.0361 0.9528 0.8967 -0.0255 0.0319 0.0209 55 ARG B NH1 1991 N NH2 . ARG B 57 ? 0.9820 0.9087 0.8307 -0.0205 0.0237 0.0179 55 ARG B NH2 1992 N N . PRO B 58 ? 0.2636 0.2282 0.2220 -0.0258 0.0323 -0.0109 56 PRO B N 1993 C CA . PRO B 58 ? 0.2038 0.1757 0.1768 -0.0297 0.0352 -0.0137 56 PRO B CA 1994 C C . PRO B 58 ? 0.1547 0.1392 0.1402 -0.0264 0.0328 -0.0179 56 PRO B C 1995 O O . PRO B 58 ? 0.2134 0.2071 0.2107 -0.0285 0.0366 -0.0201 56 PRO B O 1996 C CB . PRO B 58 ? 0.2323 0.1974 0.2070 -0.0312 0.0316 -0.0131 56 PRO B CB 1997 C CG . PRO B 58 ? 0.2189 0.1703 0.1787 -0.0298 0.0306 -0.0082 56 PRO B CG 1998 C CD . PRO B 58 ? 0.2339 0.1876 0.1857 -0.0246 0.0281 -0.0076 56 PRO B CD 1999 N N . ASP B 59 ? 0.2399 0.2249 0.2234 -0.0210 0.0268 -0.0184 57 ASP B N 2000 C CA . ASP B 59 ? 0.1934 0.1888 0.1876 -0.0176 0.0243 -0.0212 57 ASP B CA 2001 C C . ASP B 59 ? 0.1891 0.1897 0.1851 -0.0165 0.0287 -0.0227 57 ASP B C 2002 O O . ASP B 59 ? 0.2050 0.2147 0.2136 -0.0159 0.0303 -0.0248 57 ASP B O 2003 C CB . ASP B 59 ? 0.2205 0.2139 0.2105 -0.0126 0.0177 -0.0209 57 ASP B CB 2004 C CG . ASP B 59 ? 0.2643 0.2537 0.2542 -0.0130 0.0137 -0.0207 57 ASP B CG 2005 O OD1 . ASP B 59 ? 0.2019 0.1941 0.1994 -0.0168 0.0144 -0.0221 57 ASP B OD1 2006 O OD2 . ASP B 59 ? 0.2530 0.2364 0.2356 -0.0099 0.0101 -0.0196 57 ASP B OD2 2007 N N . ALA B 60 ? 0.2061 0.2006 0.1895 -0.0163 0.0307 -0.0218 58 ALA B N 2008 C CA . ALA B 60 ? 0.1316 0.1292 0.1145 -0.0159 0.0356 -0.0243 58 ALA B CA 2009 C C . ALA B 60 ? 0.2411 0.2438 0.2326 -0.0196 0.0435 -0.0259 58 ALA B C 2010 O O . ALA B 60 ? 0.2152 0.2252 0.2173 -0.0180 0.0468 -0.0289 58 ALA B O 2011 C CB . ALA B 60 ? 0.2131 0.2030 0.1787 -0.0164 0.0362 -0.0232 58 ALA B CB 2012 N N . GLU B 61 ? 0.2313 0.2300 0.2191 -0.0243 0.0467 -0.0237 59 GLU B N 2013 C CA . GLU B 61 ? 0.2625 0.2663 0.2583 -0.0286 0.0549 -0.0247 59 GLU B CA 2014 C C . GLU B 61 ? 0.2169 0.2320 0.2334 -0.0285 0.0538 -0.0264 59 GLU B C 2015 O O . GLU B 61 ? 0.2772 0.3012 0.3061 -0.0288 0.0595 -0.0288 59 GLU B O 2016 C CB . GLU B 61 ? 0.3133 0.3084 0.2986 -0.0342 0.0585 -0.0210 59 GLU B CB 2017 C CG . GLU B 61 ? 0.5443 0.5292 0.5083 -0.0339 0.0590 -0.0186 59 GLU B CG 2018 C CD . GLU B 61 ? 0.6428 0.6176 0.5944 -0.0388 0.0621 -0.0135 59 GLU B CD 2019 O OE1 . GLU B 61 ? 0.6113 0.5851 0.5706 -0.0425 0.0629 -0.0118 59 GLU B OE1 2020 O OE2 . GLU B 61 ? 0.6505 0.6183 0.5845 -0.0392 0.0635 -0.0110 59 GLU B OE2 2021 N N . TYR B 62 ? 0.2382 0.2535 0.2587 -0.0278 0.0464 -0.0254 60 TYR B N 2022 C CA . TYR B 62 ? 0.2325 0.2593 0.2712 -0.0280 0.0439 -0.0268 60 TYR B CA 2023 C C . TYR B 62 ? 0.1752 0.2107 0.2238 -0.0221 0.0422 -0.0285 60 TYR B C 2024 O O . TYR B 62 ? 0.2624 0.3090 0.3271 -0.0217 0.0449 -0.0298 60 TYR B O 2025 C CB . TYR B 62 ? 0.1843 0.2081 0.2220 -0.0288 0.0361 -0.0260 60 TYR B CB 2026 C CG . TYR B 62 ? 0.2116 0.2476 0.2661 -0.0293 0.0320 -0.0276 60 TYR B CG 2027 C CD1 . TYR B 62 ? 0.1890 0.2353 0.2587 -0.0335 0.0362 -0.0287 60 TYR B CD1 2028 C CD2 . TYR B 62 ? 0.2245 0.2625 0.2795 -0.0258 0.0238 -0.0279 60 TYR B CD2 2029 C CE1 . TYR B 62 ? 0.2086 0.2676 0.2942 -0.0341 0.0313 -0.0299 60 TYR B CE1 2030 C CE2 . TYR B 62 ? 0.3472 0.3968 0.4158 -0.0265 0.0192 -0.0290 60 TYR B CE2 2031 C CZ . TYR B 62 ? 0.3639 0.4242 0.4479 -0.0305 0.0224 -0.0300 60 TYR B CZ 2032 O OH . TYR B 62 ? 0.4143 0.4877 0.5123 -0.0312 0.0166 -0.0310 60 TYR B OH 2033 N N . TRP B 63 ? 0.1699 0.2004 0.2098 -0.0175 0.0379 -0.0282 61 TRP B N 2034 C CA . TRP B 63 ? 0.1620 0.1984 0.2099 -0.0120 0.0362 -0.0292 61 TRP B CA 2035 C C . TRP B 63 ? 0.2063 0.2449 0.2584 -0.0111 0.0442 -0.0316 61 TRP B C 2036 O O . TRP B 63 ? 0.1814 0.2280 0.2477 -0.0076 0.0453 -0.0325 61 TRP B O 2037 C CB . TRP B 63 ? 0.1428 0.1729 0.1802 -0.0083 0.0303 -0.0282 61 TRP B CB 2038 C CG . TRP B 63 ? 0.1709 0.2004 0.2066 -0.0082 0.0229 -0.0265 61 TRP B CG 2039 C CD1 . TRP B 63 ? 0.1889 0.2236 0.2324 -0.0107 0.0203 -0.0264 61 TRP B CD1 2040 C CD2 . TRP B 63 ? 0.0940 0.1173 0.1194 -0.0058 0.0176 -0.0254 61 TRP B CD2 2041 N NE1 . TRP B 63 ? 0.1053 0.1368 0.1430 -0.0099 0.0140 -0.0258 61 TRP B NE1 2042 C CE2 . TRP B 63 ? 0.1627 0.1872 0.1896 -0.0066 0.0126 -0.0250 61 TRP B CE2 2043 C CE3 . TRP B 63 ? 0.0944 0.1119 0.1101 -0.0032 0.0167 -0.0251 61 TRP B CE3 2044 C CZ2 . TRP B 63 ? 0.1818 0.2016 0.2008 -0.0045 0.0077 -0.0243 61 TRP B CZ2 2045 C CZ3 . TRP B 63 ? 0.1158 0.1299 0.1252 -0.0012 0.0114 -0.0240 61 TRP B CZ3 2046 C CH2 . TRP B 63 ? 0.1424 0.1575 0.1534 -0.0015 0.0074 -0.0236 61 TRP B CH2 2047 N N . ASN B 64 ? 0.2015 0.2328 0.2410 -0.0140 0.0500 -0.0326 62 ASN B N 2048 C CA . ASN B 64 ? 0.2166 0.2493 0.2584 -0.0135 0.0586 -0.0360 62 ASN B CA 2049 C C . ASN B 64 ? 0.1894 0.2321 0.2477 -0.0154 0.0654 -0.0371 62 ASN B C 2050 O O . ASN B 64 ? 0.2021 0.2485 0.2678 -0.0136 0.0727 -0.0403 62 ASN B O 2051 C CB . ASN B 64 ? 0.1328 0.1555 0.1547 -0.0166 0.0629 -0.0368 62 ASN B CB 2052 C CG . ASN B 64 ? 0.1371 0.1525 0.1459 -0.0140 0.0574 -0.0370 62 ASN B CG 2053 O OD1 . ASN B 64 ? 0.1472 0.1648 0.1627 -0.0098 0.0528 -0.0375 62 ASN B OD1 2054 N ND2 . ASN B 64 ? 0.1428 0.1500 0.1331 -0.0167 0.0578 -0.0363 62 ASN B ND2 2055 N N . SER B 65 ? 0.1343 0.1817 0.1994 -0.0190 0.0634 -0.0349 63 SER B N 2056 C CA . SER B 65 ? 0.1222 0.1812 0.2054 -0.0212 0.0692 -0.0359 63 SER B CA 2057 C C . SER B 65 ? 0.1462 0.2180 0.2506 -0.0164 0.0647 -0.0357 63 SER B C 2058 O O . SER B 65 ? 0.1501 0.2339 0.2730 -0.0169 0.0686 -0.0365 63 SER B O 2059 C CB . SER B 65 ? 0.2024 0.2612 0.2849 -0.0282 0.0690 -0.0338 63 SER B CB 2060 O OG . SER B 65 ? 0.1678 0.2301 0.2563 -0.0279 0.0592 -0.0322 63 SER B OG 2061 N N . GLN B 66 ? 0.1252 0.1947 0.2269 -0.0116 0.0563 -0.0343 64 GLN B N 2062 C CA . GLN B 66 ? 0.1387 0.2192 0.2579 -0.0066 0.0509 -0.0329 64 GLN B CA 2063 C C . GLN B 66 ? 0.1777 0.2569 0.3008 0.0000 0.0537 -0.0340 64 GLN B C 2064 O O . GLN B 66 ? 0.1940 0.2654 0.3072 0.0031 0.0495 -0.0333 64 GLN B O 2065 C CB . GLN B 66 ? 0.1473 0.2270 0.2617 -0.0062 0.0399 -0.0302 64 GLN B CB 2066 C CG . GLN B 66 ? 0.1616 0.2408 0.2720 -0.0128 0.0373 -0.0299 64 GLN B CG 2067 C CD . GLN B 66 ? 0.3292 0.4060 0.4326 -0.0124 0.0274 -0.0283 64 GLN B CD 2068 O OE1 . GLN B 66 ? 0.3967 0.4794 0.5061 -0.0078 0.0214 -0.0267 64 GLN B OE1 2069 N NE2 . GLN B 66 ? 0.3403 0.4078 0.4306 -0.0169 0.0260 -0.0285 64 GLN B NE2 2070 N N . LYS B 67 ? 0.1814 0.2682 0.3201 0.0020 0.0612 -0.0360 65 LYS B N 2071 C CA A LYS B 67 ? 0.1918 0.2756 0.3346 0.0080 0.0651 -0.0375 65 LYS B CA 2072 C CA B LYS B 67 ? 0.1927 0.2759 0.3346 0.0079 0.0652 -0.0376 65 LYS B CA 2073 C C . LYS B 67 ? 0.1493 0.2340 0.2979 0.0143 0.0571 -0.0339 65 LYS B C 2074 O O . LYS B 67 ? 0.1384 0.2137 0.2797 0.0175 0.0574 -0.0347 65 LYS B O 2075 C CB A LYS B 67 ? 0.1921 0.2822 0.3473 0.0093 0.0705 -0.0378 65 LYS B CB 2076 C CB B LYS B 67 ? 0.1746 0.2633 0.3278 0.0089 0.0712 -0.0382 65 LYS B CB 2077 C CG A LYS B 67 ? 0.2584 0.3638 0.4321 0.0095 0.0657 -0.0343 65 LYS B CG 2078 C CG B LYS B 67 ? 0.1922 0.2795 0.3531 0.0160 0.0715 -0.0376 65 LYS B CG 2079 C CD A LYS B 67 ? 0.2979 0.4104 0.4844 0.0109 0.0716 -0.0349 65 LYS B CD 2080 C CD B LYS B 67 ? 0.1971 0.2706 0.3441 0.0164 0.0775 -0.0420 65 LYS B CD 2081 C CE A LYS B 67 ? 0.2728 0.4014 0.4760 0.0091 0.0673 -0.0320 65 LYS B CE 2082 C CE B LYS B 67 ? 0.1259 0.1977 0.2823 0.0226 0.0792 -0.0420 65 LYS B CE 2083 N NZ A LYS B 67 ? 0.1897 0.3256 0.4040 0.0086 0.0748 -0.0334 65 LYS B NZ 2084 N NZ B LYS B 67 ? 0.1361 0.1946 0.2796 0.0221 0.0849 -0.0470 65 LYS B NZ 2085 N N . ASP B 68 ? 0.1426 0.2386 0.3037 0.0155 0.0498 -0.0300 66 ASP B N 2086 C CA . ASP B 68 ? 0.1615 0.2595 0.3273 0.0212 0.0416 -0.0253 66 ASP B CA 2087 C C . ASP B 68 ? 0.1842 0.2716 0.3324 0.0206 0.0363 -0.0245 66 ASP B C 2088 O O . ASP B 68 ? 0.1428 0.2250 0.2895 0.0252 0.0344 -0.0225 66 ASP B O 2089 C CB . ASP B 68 ? 0.2555 0.3682 0.4347 0.0214 0.0339 -0.0213 66 ASP B CB 2090 C CG . ASP B 68 ? 0.3332 0.4497 0.5079 0.0143 0.0303 -0.0225 66 ASP B CG 2091 O OD1 . ASP B 68 ? 0.3046 0.4126 0.4663 0.0089 0.0354 -0.0259 66 ASP B OD1 2092 O OD2 . ASP B 68 ? 0.4209 0.5471 0.6016 0.0137 0.0218 -0.0197 66 ASP B OD2 2093 N N . LEU B 69 ? 0.1328 0.2162 0.2666 0.0147 0.0339 -0.0254 67 LEU B N 2094 C CA . LEU B 69 ? 0.1891 0.2620 0.3047 0.0138 0.0291 -0.0247 67 LEU B CA 2095 C C . LEU B 69 ? 0.2230 0.2844 0.3285 0.0149 0.0343 -0.0274 67 LEU B C 2096 O O . LEU B 69 ? 0.1797 0.2355 0.2795 0.0175 0.0310 -0.0259 67 LEU B O 2097 C CB . LEU B 69 ? 0.1288 0.1987 0.2323 0.0077 0.0268 -0.0255 67 LEU B CB 2098 C CG . LEU B 69 ? 0.2632 0.3217 0.3478 0.0068 0.0236 -0.0254 67 LEU B CG 2099 C CD1 . LEU B 69 ? 0.3143 0.3741 0.3983 0.0104 0.0161 -0.0221 67 LEU B CD1 2100 C CD2 . LEU B 69 ? 0.3925 0.4469 0.4666 0.0013 0.0228 -0.0262 67 LEU B CD2 2101 N N . LEU B 70 ? 0.1488 0.2072 0.2521 0.0125 0.0426 -0.0315 68 LEU B N 2102 C CA . LEU B 70 ? 0.2161 0.2640 0.3087 0.0125 0.0476 -0.0351 68 LEU B CA 2103 C C . LEU B 70 ? 0.2514 0.2978 0.3539 0.0182 0.0493 -0.0354 68 LEU B C 2104 O O . LEU B 70 ? 0.2574 0.2951 0.3511 0.0188 0.0486 -0.0365 68 LEU B O 2105 C CB . LEU B 70 ? 0.2194 0.2654 0.3077 0.0087 0.0567 -0.0397 68 LEU B CB 2106 C CG . LEU B 70 ? 0.1995 0.2421 0.2732 0.0027 0.0561 -0.0393 68 LEU B CG 2107 C CD1 . LEU B 70 ? 0.3104 0.3503 0.3780 -0.0010 0.0658 -0.0433 68 LEU B CD1 2108 C CD2 . LEU B 70 ? 0.1771 0.2110 0.2337 0.0018 0.0496 -0.0380 68 LEU B CD2 2109 N N . GLU B 71 ? 0.1455 0.2004 0.2670 0.0223 0.0516 -0.0342 69 GLU B N 2110 C CA . GLU B 71 ? 0.0972 0.1487 0.2264 0.0277 0.0520 -0.0327 69 GLU B CA 2111 C C . GLU B 71 ? 0.0979 0.1487 0.2281 0.0311 0.0445 -0.0277 69 GLU B C 2112 O O . GLU B 71 ? 0.1389 0.1818 0.2681 0.0338 0.0448 -0.0269 69 GLU B O 2113 C CB . GLU B 71 ? 0.1067 0.1662 0.2515 0.0309 0.0537 -0.0306 69 GLU B CB 2114 C CG . GLU B 71 ? 0.1299 0.1885 0.2742 0.0283 0.0625 -0.0357 69 GLU B CG 2115 C CD . GLU B 71 ? 0.2187 0.2642 0.3520 0.0274 0.0686 -0.0410 69 GLU B CD 2116 O OE1 . GLU B 71 ? 0.2700 0.3078 0.4012 0.0300 0.0666 -0.0404 69 GLU B OE1 2117 O OE2 . GLU B 71 ? 0.2344 0.2774 0.3607 0.0237 0.0754 -0.0458 69 GLU B OE2 2118 N N . GLN B 72 ? 0.0843 0.1416 0.2126 0.0299 0.0368 -0.0237 70 GLN B N 2119 C CA . GLN B 72 ? 0.2021 0.2576 0.3258 0.0318 0.0292 -0.0186 70 GLN B CA 2120 C C . GLN B 72 ? 0.1676 0.2113 0.2750 0.0292 0.0298 -0.0211 70 GLN B C 2121 O O . GLN B 72 ? 0.0842 0.1224 0.1909 0.0316 0.0286 -0.0190 70 GLN B O 2122 C CB . GLN B 72 ? 0.1574 0.2211 0.2783 0.0298 0.0212 -0.0152 70 GLN B CB 2123 C CG . GLN B 72 ? 0.3826 0.4596 0.5201 0.0329 0.0176 -0.0112 70 GLN B CG 2124 C CD . GLN B 72 ? 0.5562 0.6344 0.7023 0.0394 0.0144 -0.0052 70 GLN B CD 2125 O OE1 . GLN B 72 ? 0.6260 0.6972 0.7627 0.0403 0.0115 -0.0025 70 GLN B OE1 2126 N NE2 . GLN B 72 ? 0.5981 0.6838 0.7585 0.0432 0.0145 -0.0026 70 GLN B NE2 2127 N N . LYS B 73 ? 0.0966 0.1370 0.1913 0.0241 0.0312 -0.0251 71 LYS B N 2128 C CA . LYS B 73 ? 0.1107 0.1418 0.1904 0.0214 0.0309 -0.0274 71 LYS B CA 2129 C C . LYS B 73 ? 0.1156 0.1388 0.1956 0.0219 0.0372 -0.0318 71 LYS B C 2130 O O . LYS B 73 ? 0.1792 0.1959 0.2530 0.0214 0.0359 -0.0324 71 LYS B O 2131 C CB . LYS B 73 ? 0.0860 0.1157 0.1527 0.0164 0.0309 -0.0298 71 LYS B CB 2132 C CG . LYS B 73 ? 0.1357 0.1706 0.2002 0.0151 0.0248 -0.0265 71 LYS B CG 2133 C CD . LYS B 73 ? 0.1417 0.1759 0.2017 0.0167 0.0182 -0.0230 71 LYS B CD 2134 C CE . LYS B 73 ? 0.1724 0.2130 0.2335 0.0161 0.0128 -0.0203 71 LYS B CE 2135 N NZ . LYS B 73 ? 0.1639 0.2046 0.2205 0.0178 0.0070 -0.0171 71 LYS B NZ 2136 N N . ARG B 74 ? 0.1566 0.1806 0.2444 0.0227 0.0443 -0.0354 72 ARG B N 2137 C CA . ARG B 74 ? 0.2195 0.2353 0.3078 0.0231 0.0513 -0.0409 72 ARG B CA 2138 C C . ARG B 74 ? 0.2468 0.2588 0.3458 0.0279 0.0510 -0.0383 72 ARG B C 2139 O O . ARG B 74 ? 0.1311 0.1337 0.2261 0.0268 0.0540 -0.0418 72 ARG B O 2140 C CB . ARG B 74 ? 0.2845 0.3022 0.3772 0.0226 0.0587 -0.0447 72 ARG B CB 2141 C CG . ARG B 74 ? 0.2628 0.2802 0.3423 0.0172 0.0621 -0.0490 72 ARG B CG 2142 C CD . ARG B 74 ? 0.2089 0.2307 0.2938 0.0164 0.0681 -0.0503 72 ARG B CD 2143 N NE . ARG B 74 ? 0.2041 0.2261 0.2763 0.0111 0.0710 -0.0528 72 ARG B NE 2144 C CZ . ARG B 74 ? 0.2301 0.2563 0.3048 0.0091 0.0766 -0.0537 72 ARG B CZ 2145 N NH1 . ARG B 74 ? 0.2144 0.2459 0.3047 0.0124 0.0795 -0.0529 72 ARG B NH1 2146 N NH2 . ARG B 74 ? 0.2650 0.2902 0.3266 0.0039 0.0792 -0.0551 72 ARG B NH2 2147 N N . ALA B 75 ? 0.1675 0.1863 0.2779 0.0323 0.0465 -0.0314 73 ALA B N 2148 C CA . ALA B 75 ? 0.1824 0.1971 0.3007 0.0365 0.0451 -0.0268 73 ALA B CA 2149 C C . ALA B 75 ? 0.1327 0.1445 0.2457 0.0363 0.0399 -0.0230 73 ALA B C 2150 O O . ALA B 75 ? 0.2578 0.2645 0.3764 0.0394 0.0396 -0.0192 73 ALA B O 2151 C CB . ALA B 75 ? 0.1855 0.2092 0.3173 0.0413 0.0425 -0.0205 73 ALA B CB 2152 N N . ALA B 76 ? 0.1359 0.1500 0.2354 0.0320 0.0352 -0.0232 74 ALA B N 2153 C CA . ALA B 76 ? 0.1676 0.1809 0.2598 0.0311 0.0292 -0.0188 74 ALA B CA 2154 C C . ALA B 76 ? 0.1362 0.1396 0.2262 0.0299 0.0313 -0.0201 74 ALA B C 2155 O O . ALA B 76 ? 0.1832 0.1855 0.2741 0.0312 0.0282 -0.0147 74 ALA B O 2156 C CB . ALA B 76 ? 0.1202 0.1366 0.1990 0.0268 0.0251 -0.0202 74 ALA B CB 2157 N N . VAL B 77 ? 0.1527 0.1490 0.2393 0.0270 0.0365 -0.0275 75 VAL B N 2158 C CA . VAL B 77 ? 0.1495 0.1363 0.2348 0.0249 0.0386 -0.0298 75 VAL B CA 2159 C C . VAL B 77 ? 0.1267 0.1087 0.2251 0.0297 0.0405 -0.0248 75 VAL B C 2160 O O . VAL B 77 ? 0.2269 0.2029 0.3254 0.0285 0.0400 -0.0227 75 VAL B O 2161 C CB . VAL B 77 ? 0.1501 0.1296 0.2301 0.0210 0.0443 -0.0395 75 VAL B CB 2162 C CG1 . VAL B 77 ? 0.1754 0.1577 0.2401 0.0156 0.0411 -0.0433 75 VAL B CG1 2163 C CG2 . VAL B 77 ? 0.1490 0.1282 0.2371 0.0240 0.0510 -0.0430 75 VAL B CG2 2164 N N . ASP B 78 ? 0.1614 0.1465 0.2716 0.0350 0.0427 -0.0223 76 ASP B N 2165 C CA . ASP B 78 ? 0.2025 0.1838 0.3246 0.0401 0.0435 -0.0159 76 ASP B CA 2166 C C . ASP B 78 ? 0.2291 0.2187 0.3550 0.0443 0.0369 -0.0057 76 ASP B C 2167 O O . ASP B 78 ? 0.2135 0.1989 0.3400 0.0454 0.0351 0.0006 76 ASP B O 2168 C CB . ASP B 78 ? 0.2027 0.1841 0.3322 0.0425 0.0474 -0.0176 76 ASP B CB 2169 C CG . ASP B 78 ? 0.2816 0.2535 0.4073 0.0387 0.0542 -0.0268 76 ASP B CG 2170 O OD1 . ASP B 78 ? 0.3078 0.2707 0.4281 0.0349 0.0556 -0.0304 76 ASP B OD1 2171 O OD2 . ASP B 78 ? 0.3736 0.3474 0.5015 0.0392 0.0580 -0.0307 76 ASP B OD2 2172 N N . THR B 79 ? 0.2028 0.2041 0.3291 0.0456 0.0331 -0.0040 77 THR B N 2173 C CA . THR B 79 ? 0.2228 0.2331 0.3521 0.0492 0.0264 0.0052 77 THR B CA 2174 C C . THR B 79 ? 0.1979 0.2106 0.3135 0.0457 0.0206 0.0082 77 THR B C 2175 O O . THR B 79 ? 0.1594 0.1772 0.2746 0.0481 0.0154 0.0159 77 THR B O 2176 C CB . THR B 79 ? 0.1970 0.2195 0.3305 0.0504 0.0238 0.0050 77 THR B CB 2177 O OG1 . THR B 79 ? 0.2015 0.2275 0.3251 0.0453 0.0232 -0.0009 77 THR B OG1 2178 C CG2 . THR B 79 ? 0.2185 0.2397 0.3607 0.0521 0.0287 0.0020 77 THR B CG2 2179 N N . TYR B 80 ? 0.1541 0.1636 0.2582 0.0401 0.0215 0.0020 78 TYR B N 2180 C CA . TYR B 80 ? 0.1869 0.1993 0.2790 0.0369 0.0169 0.0037 78 TYR B CA 2181 C C . TYR B 80 ? 0.1781 0.1822 0.2652 0.0335 0.0191 0.0022 78 TYR B C 2182 O O . TYR B 80 ? 0.1974 0.2005 0.2830 0.0339 0.0175 0.0079 78 TYR B O 2183 C CB . TYR B 80 ? 0.1882 0.2062 0.2719 0.0336 0.0149 -0.0014 78 TYR B CB 2184 C CG . TYR B 80 ? 0.1071 0.1274 0.1789 0.0307 0.0108 -0.0010 78 TYR B CG 2185 C CD1 . TYR B 80 ? 0.0912 0.1166 0.1600 0.0322 0.0062 0.0049 78 TYR B CD1 2186 C CD2 . TYR B 80 ? 0.1611 0.1785 0.2243 0.0266 0.0117 -0.0066 78 TYR B CD2 2187 C CE1 . TYR B 80 ? 0.1212 0.1485 0.1795 0.0299 0.0035 0.0045 78 TYR B CE1 2188 C CE2 . TYR B 80 ? 0.1051 0.1249 0.1592 0.0247 0.0084 -0.0062 78 TYR B CE2 2189 C CZ . TYR B 80 ? 0.1491 0.1735 0.2011 0.0265 0.0048 -0.0010 78 TYR B CZ 2190 O OH . TYR B 80 ? 0.1459 0.1722 0.1892 0.0249 0.0025 -0.0014 78 TYR B OH 2191 N N . CYS B 81 ? 0.1132 0.1119 0.1974 0.0298 0.0227 -0.0056 79 CYS B N 2192 C CA . CYS B 81 ? 0.1275 0.1197 0.2076 0.0256 0.0242 -0.0082 79 CYS B CA 2193 C C . CYS B 81 ? 0.1113 0.0948 0.1998 0.0268 0.0277 -0.0049 79 CYS B C 2194 O O . CYS B 81 ? 0.1497 0.1321 0.2369 0.0256 0.0266 -0.0003 79 CYS B O 2195 C CB . CYS B 81 ? 0.1038 0.0928 0.1787 0.0213 0.0267 -0.0174 79 CYS B CB 2196 S SG . CYS B 81 ? 0.1498 0.1469 0.2134 0.0192 0.0230 -0.0207 79 CYS B SG 2197 N N . ARG B 82 ? 0.2138 0.1905 0.3112 0.0290 0.0326 -0.0073 80 ARG B N 2198 C CA . ARG B 82 ? 0.1704 0.1365 0.2767 0.0303 0.0366 -0.0044 80 ARG B CA 2199 C C . ARG B 82 ? 0.2493 0.2177 0.3598 0.0350 0.0337 0.0072 80 ARG B C 2200 O O . ARG B 82 ? 0.2816 0.2432 0.3942 0.0342 0.0351 0.0120 80 ARG B O 2201 C CB . ARG B 82 ? 0.2331 0.1913 0.3490 0.0329 0.0429 -0.0094 80 ARG B CB 2202 C CG . ARG B 82 ? 0.2053 0.1571 0.3159 0.0270 0.0470 -0.0210 80 ARG B CG 2203 C CD . ARG B 82 ? 0.2410 0.1849 0.3591 0.0290 0.0538 -0.0265 80 ARG B CD 2204 N NE . ARG B 82 ? 0.2409 0.1780 0.3514 0.0224 0.0572 -0.0374 80 ARG B NE 2205 C CZ . ARG B 82 ? 0.3034 0.2445 0.4050 0.0194 0.0579 -0.0450 80 ARG B CZ 2206 N NH1 . ARG B 82 ? 0.2842 0.2198 0.3777 0.0131 0.0602 -0.0541 80 ARG B NH1 2207 N NH2 . ARG B 82 ? 0.3259 0.2769 0.4261 0.0224 0.0561 -0.0432 80 ARG B NH2 2208 N N . HIS B 83 ? 0.1778 0.1560 0.2893 0.0395 0.0297 0.0118 81 HIS B N 2209 C CA . HIS B 83 ? 0.2032 0.1853 0.3167 0.0439 0.0258 0.0229 81 HIS B CA 2210 C C . HIS B 83 ? 0.1853 0.1694 0.2882 0.0403 0.0230 0.0268 81 HIS B C 2211 O O . HIS B 83 ? 0.2274 0.2064 0.3318 0.0411 0.0239 0.0342 81 HIS B O 2212 C CB . HIS B 83 ? 0.2463 0.2404 0.3613 0.0480 0.0209 0.0256 81 HIS B CB 2213 C CG . HIS B 83 ? 0.2847 0.2845 0.3992 0.0519 0.0156 0.0366 81 HIS B CG 2214 N ND1 . HIS B 83 ? 0.2943 0.2920 0.4198 0.0583 0.0155 0.0448 81 HIS B ND1 2215 C CD2 . HIS B 83 ? 0.2526 0.2599 0.3561 0.0505 0.0103 0.0407 81 HIS B CD2 2216 C CE1 . HIS B 83 ? 0.2887 0.2929 0.4090 0.0603 0.0097 0.0540 81 HIS B CE1 2217 N NE2 . HIS B 83 ? 0.2792 0.2891 0.3857 0.0555 0.0068 0.0512 81 HIS B NE2 2218 N N . ASN B 84 ? 0.1396 0.1309 0.2323 0.0365 0.0201 0.0221 82 ASN B N 2219 C CA . ASN B 84 ? 0.1190 0.1138 0.2023 0.0336 0.0179 0.0251 82 ASN B CA 2220 C C . ASN B 84 ? 0.2041 0.1908 0.2883 0.0291 0.0221 0.0239 82 ASN B C 2221 O O . ASN B 84 ? 0.2188 0.2060 0.2996 0.0279 0.0221 0.0295 82 ASN B O 2222 C CB . ASN B 84 ? 0.1153 0.1188 0.1890 0.0312 0.0143 0.0198 82 ASN B CB 2223 C CG . ASN B 84 ? 0.2336 0.2461 0.3049 0.0346 0.0094 0.0227 82 ASN B CG 2224 O OD1 . ASN B 84 ? 0.2485 0.2628 0.3234 0.0386 0.0075 0.0299 82 ASN B OD1 2225 N ND2 . ASN B 84 ? 0.1953 0.2133 0.2605 0.0328 0.0070 0.0172 82 ASN B ND2 2226 N N . TYR B 85 ? 0.2022 0.1820 0.2906 0.0263 0.0258 0.0163 83 TYR B N 2227 C CA . TYR B 85 ? 0.2036 0.1753 0.2944 0.0213 0.0296 0.0142 83 TYR B CA 2228 C C . TYR B 85 ? 0.2465 0.2098 0.3444 0.0235 0.0326 0.0230 83 TYR B C 2229 O O . TYR B 85 ? 0.2796 0.2408 0.3767 0.0202 0.0342 0.0270 83 TYR B O 2230 C CB . TYR B 85 ? 0.1519 0.1168 0.2458 0.0181 0.0330 0.0040 83 TYR B CB 2231 C CG . TYR B 85 ? 0.2927 0.2505 0.3885 0.0114 0.0361 -0.0004 83 TYR B CG 2232 C CD1 . TYR B 85 ? 0.2762 0.2220 0.3806 0.0108 0.0409 0.0024 83 TYR B CD1 2233 C CD2 . TYR B 85 ? 0.2316 0.1946 0.3214 0.0057 0.0341 -0.0075 83 TYR B CD2 2234 C CE1 . TYR B 85 ? 0.2515 0.1908 0.3585 0.0038 0.0438 -0.0023 83 TYR B CE1 2235 C CE2 . TYR B 85 ? 0.2264 0.1845 0.3190 -0.0009 0.0363 -0.0119 83 TYR B CE2 2236 C CZ . TYR B 85 ? 0.3162 0.2624 0.4174 -0.0023 0.0412 -0.0097 83 TYR B CZ 2237 O OH . TYR B 85 ? 0.3305 0.2717 0.4353 -0.0098 0.0434 -0.0146 83 TYR B OH 2238 N N . GLY B 86 ? 0.1929 0.1520 0.2982 0.0292 0.0336 0.0266 84 GLY B N 2239 C CA . GLY B 86 ? 0.2156 0.1659 0.3283 0.0328 0.0361 0.0362 84 GLY B CA 2240 C C . GLY B 86 ? 0.1648 0.1208 0.2713 0.0344 0.0329 0.0474 84 GLY B C 2241 O O . GLY B 86 ? 0.2819 0.2305 0.3904 0.0337 0.0357 0.0549 84 GLY B O 2242 N N . VAL B 87 ? 0.2256 0.1946 0.3237 0.0361 0.0273 0.0481 85 VAL B N 2243 C CA . VAL B 87 ? 0.2570 0.2330 0.3467 0.0377 0.0237 0.0575 85 VAL B CA 2244 C C . VAL B 87 ? 0.2425 0.2188 0.3253 0.0320 0.0259 0.0582 85 VAL B C 2245 O O . VAL B 87 ? 0.2619 0.2369 0.3412 0.0324 0.0269 0.0677 85 VAL B O 2246 C CB . VAL B 87 ? 0.1863 0.1758 0.2685 0.0399 0.0173 0.0557 85 VAL B CB 2247 C CG1 . VAL B 87 ? 0.2219 0.2186 0.2930 0.0406 0.0138 0.0635 85 VAL B CG1 2248 C CG2 . VAL B 87 ? 0.1985 0.1900 0.2890 0.0457 0.0148 0.0564 85 VAL B CG2 2249 N N . GLY B 88 ? 0.3437 0.3221 0.4249 0.0268 0.0271 0.0486 86 GLY B N 2250 C CA . GLY B 88 ? 0.3487 0.3309 0.4244 0.0216 0.0286 0.0478 86 GLY B CA 2251 C C . GLY B 88 ? 0.2986 0.2724 0.3815 0.0157 0.0339 0.0450 86 GLY B C 2252 O O . GLY B 88 ? 0.3640 0.3413 0.4449 0.0111 0.0358 0.0451 86 GLY B O 2253 N N . GLU B 89 ? 0.2222 0.2561 0.4240 0.0204 0.1173 0.0616 87 GLU B N 2254 C CA . GLU B 89 ? 0.2530 0.2728 0.4576 0.0253 0.1186 0.0574 87 GLU B CA 2255 C C . GLU B 89 ? 0.3002 0.3152 0.5104 0.0272 0.1120 0.0659 87 GLU B C 2256 O O . GLU B 89 ? 0.2566 0.2584 0.4576 0.0271 0.1113 0.0633 87 GLU B O 2257 C CB . GLU B 89 ? 0.3287 0.3516 0.5533 0.0322 0.1222 0.0516 87 GLU B CB 2258 C CG . GLU B 89 ? 0.4408 0.4506 0.6767 0.0385 0.1208 0.0472 87 GLU B CG 2259 C CD . GLU B 89 ? 0.6272 0.6393 0.8789 0.0447 0.1228 0.0374 87 GLU B CD 2260 O OE1 . GLU B 89 ? 0.6848 0.7094 0.9346 0.0440 0.1267 0.0334 87 GLU B OE1 2261 O OE2 . GLU B 89 ? 0.7126 0.7143 0.9769 0.0494 0.1190 0.0332 87 GLU B OE2 2262 N N . SER B 90 ? 0.2436 0.2713 0.4693 0.0283 0.1069 0.0773 88 SER B N 2263 C CA . SER B 90 ? 0.1925 0.2194 0.4265 0.0295 0.1006 0.0883 88 SER B CA 2264 C C . SER B 90 ? 0.2226 0.2484 0.4354 0.0246 0.0983 0.0905 88 SER B C 2265 O O . SER B 90 ? 0.2142 0.2347 0.4292 0.0251 0.0949 0.0960 88 SER B O 2266 C CB . SER B 90 ? 0.2629 0.3080 0.5176 0.0310 0.0952 0.1026 88 SER B CB 2267 O OG . SER B 90 ? 0.3547 0.4180 0.5977 0.0259 0.0933 0.1074 88 SER B OG 2268 N N . PHE B 91 ? 0.2430 0.2737 0.4370 0.0199 0.1000 0.0856 89 PHE B N 2269 C CA . PHE B 91 ? 0.2955 0.3265 0.4714 0.0164 0.0978 0.0857 89 PHE B CA 2270 C C . PHE B 91 ? 0.2967 0.3122 0.4523 0.0142 0.1017 0.0740 89 PHE B C 2271 O O . PHE B 91 ? 0.2272 0.2427 0.3686 0.0119 0.0999 0.0722 89 PHE B O 2272 C CB . PHE B 91 ? 0.2546 0.3071 0.4271 0.0132 0.0940 0.0905 89 PHE B CB 2273 C CG . PHE B 91 ? 0.2879 0.3467 0.4586 0.0101 0.0960 0.0845 89 PHE B CG 2274 C CD1 . PHE B 91 ? 0.2173 0.2688 0.3714 0.0060 0.0979 0.0742 89 PHE B CD1 2275 C CD2 . PHE B 91 ? 0.3408 0.4136 0.5282 0.0111 0.0952 0.0900 89 PHE B CD2 2276 C CE1 . PHE B 91 ? 0.2028 0.2602 0.3574 0.0020 0.0990 0.0696 89 PHE B CE1 2277 C CE2 . PHE B 91 ? 0.3307 0.4113 0.5175 0.0075 0.0968 0.0850 89 PHE B CE2 2278 C CZ . PHE B 91 ? 0.2946 0.3673 0.4651 0.0024 0.0986 0.0749 89 PHE B CZ 2279 N N . THR B 92 ? 0.2602 0.2647 0.4155 0.0150 0.1067 0.0665 90 THR B N 2280 C CA . THR B 92 ? 0.2359 0.2272 0.3735 0.0125 0.1100 0.0581 90 THR B CA 2281 C C . THR B 92 ? 0.2637 0.2423 0.4022 0.0158 0.1127 0.0534 90 THR B C 2282 O O . THR B 92 ? 0.2233 0.1928 0.3538 0.0163 0.1111 0.0525 90 THR B O 2283 C CB . THR B 92 ? 0.1979 0.1918 0.3313 0.0085 0.1137 0.0536 90 THR B CB 2284 O OG1 . THR B 92 ? 0.1700 0.1696 0.3169 0.0109 0.1175 0.0525 90 THR B OG1 2285 C CG2 . THR B 92 ? 0.2855 0.2909 0.4177 0.0045 0.1102 0.0558 90 THR B CG2 2286 N N . VAL B 93 ? 0.2385 0.2186 0.3871 0.0182 0.1168 0.0491 91 VAL B N 2287 C CA . VAL B 93 ? 0.2434 0.2146 0.3949 0.0219 0.1193 0.0418 91 VAL B CA 2288 C C . VAL B 93 ? 0.2645 0.2289 0.4267 0.0252 0.1143 0.0453 91 VAL B C 2289 O O . VAL B 93 ? 0.2561 0.2102 0.4125 0.0258 0.1140 0.0402 91 VAL B O 2290 C CB . VAL B 93 ? 0.2202 0.1989 0.3859 0.0255 0.1240 0.0360 91 VAL B CB 2291 C CG1 . VAL B 93 ? 0.2209 0.1924 0.3927 0.0305 0.1257 0.0259 91 VAL B CG1 2292 C CG2 . VAL B 93 ? 0.2605 0.2473 0.4155 0.0212 0.1294 0.0333 91 VAL B CG2 2293 N N . GLN B 94 ? 0.2927 0.2646 0.4715 0.0266 0.1099 0.0550 92 GLN B N 2294 C CA . GLN B 94 ? 0.2960 0.2633 0.4900 0.0289 0.1045 0.0616 92 GLN B CA 2295 C C . GLN B 94 ? 0.2364 0.2064 0.4208 0.0254 0.0999 0.0709 92 GLN B C 2296 O O . GLN B 94 ? 0.2530 0.2223 0.4500 0.0259 0.0950 0.0793 92 GLN B O 2297 C CB . GLN B 94 ? 0.2525 0.2276 0.4735 0.0327 0.1016 0.0694 92 GLN B CB 2298 C CG . GLN B 94 ? 0.3383 0.3113 0.5728 0.0379 0.1059 0.0584 92 GLN B CG 2299 C CD . GLN B 94 ? 0.4499 0.4311 0.7132 0.0426 0.1028 0.0661 92 GLN B CD 2300 O OE1 . GLN B 94 ? 0.4674 0.4554 0.7420 0.0416 0.0967 0.0815 92 GLN B OE1 2301 N NE2 . GLN B 94 ? 0.5619 0.5444 0.8348 0.0466 0.1058 0.0556 92 GLN B NE2 2302 N N . ARG B 95 ? 0.2622 0.2365 0.4263 0.0218 0.1014 0.0695 93 ARG B N 2303 C CA . ARG B 95 ? 0.2913 0.2713 0.4457 0.0194 0.0977 0.0758 93 ARG B CA 2304 C C . ARG B 95 ? 0.2959 0.2642 0.4451 0.0196 0.0966 0.0735 93 ARG B C 2305 O O . ARG B 95 ? 0.2686 0.2247 0.4068 0.0197 0.0997 0.0636 93 ARG B O 2306 C CB . ARG B 95 ? 0.2247 0.2096 0.3605 0.0166 0.0992 0.0714 93 ARG B CB 2307 C CG . ARG B 95 ? 0.1945 0.1875 0.3201 0.0153 0.0959 0.0747 93 ARG B CG 2308 C CD . ARG B 95 ? 0.2541 0.2504 0.3650 0.0132 0.0967 0.0678 93 ARG B CD 2309 N NE . ARG B 95 ? 0.1948 0.1972 0.2954 0.0134 0.0941 0.0671 93 ARG B NE 2310 C CZ . ARG B 95 ? 0.2396 0.2630 0.3423 0.0133 0.0908 0.0729 93 ARG B CZ 2311 N NH1 . ARG B 95 ? 0.1949 0.2344 0.3095 0.0126 0.0890 0.0816 93 ARG B NH1 2312 N NH2 . ARG B 95 ? 0.1548 0.1855 0.2480 0.0142 0.0892 0.0702 93 ARG B NH2 2313 N N . ARG B 96 ? 0.2743 0.2490 0.4315 0.0192 0.0913 0.0830 94 ARG B N 2314 C CA . ARG B 96 ? 0.3246 0.2923 0.4778 0.0189 0.0885 0.0812 94 ARG B CA 2315 C C . ARG B 96 ? 0.2926 0.2750 0.4416 0.0173 0.0837 0.0900 94 ARG B C 2316 O O . ARG B 96 ? 0.1911 0.1879 0.3526 0.0169 0.0788 0.1013 94 ARG B O 2317 C CB . ARG B 96 ? 0.2794 0.2400 0.4525 0.0202 0.0851 0.0810 94 ARG B CB 2318 C CG . ARG B 96 ? 0.3397 0.2870 0.5193 0.0227 0.0894 0.0700 94 ARG B CG 2319 C CD . ARG B 96 ? 0.3405 0.2750 0.5038 0.0224 0.0930 0.0578 94 ARG B CD 2320 N NE . ARG B 96 ? 0.4651 0.3904 0.6342 0.0253 0.0966 0.0455 94 ARG B NE 2321 C CZ . ARG B 96 ? 0.6193 0.5464 0.7826 0.0269 0.1026 0.0388 94 ARG B CZ 2322 N NH1 . ARG B 96 ? 0.6619 0.5974 0.8139 0.0249 0.1048 0.0436 94 ARG B NH1 2323 N NH2 . ARG B 96 ? 0.7134 0.6369 0.8821 0.0301 0.1058 0.0263 94 ARG B NH2 2324 N N . VAL B 97 ? 0.1594 0.1403 0.2917 0.0165 0.0850 0.0857 95 VAL B N 2325 C CA . VAL B 97 ? 0.1902 0.1876 0.3204 0.0153 0.0813 0.0939 95 VAL B CA 2326 C C . VAL B 97 ? 0.1698 0.1595 0.2955 0.0148 0.0804 0.0913 95 VAL B C 2327 O O . VAL B 97 ? 0.1599 0.1375 0.2724 0.0156 0.0843 0.0823 95 VAL B O 2328 C CB . VAL B 97 ? 0.1871 0.1977 0.3030 0.0154 0.0842 0.0918 95 VAL B CB 2329 C CG1 . VAL B 97 ? 0.1949 0.2282 0.3090 0.0148 0.0810 0.0994 95 VAL B CG1 2330 C CG2 . VAL B 97 ? 0.2399 0.2575 0.3589 0.0152 0.0854 0.0921 95 VAL B CG2 2331 N N . TYR B 98 ? 0.1869 0.1839 0.3244 0.0133 0.0749 0.0998 96 TYR B N 2332 C CA . TYR B 98 ? 0.2134 0.2059 0.3487 0.0120 0.0735 0.0986 96 TYR B CA 2333 C C . TYR B 98 ? 0.2119 0.2141 0.3309 0.0128 0.0766 0.0975 96 TYR B C 2334 O O . TYR B 98 ? 0.2285 0.2478 0.3423 0.0137 0.0777 0.1004 96 TYR B O 2335 C CB . TYR B 98 ? 0.2892 0.2879 0.4431 0.0092 0.0665 0.1082 96 TYR B CB 2336 C CG . TYR B 98 ? 0.3406 0.3632 0.5030 0.0075 0.0615 0.1227 96 TYR B CG 2337 C CD1 . TYR B 98 ? 0.4571 0.4965 0.6146 0.0059 0.0599 0.1289 96 TYR B CD1 2338 C CD2 . TYR B 98 ? 0.2524 0.2823 0.4298 0.0075 0.0579 0.1310 96 TYR B CD2 2339 C CE1 . TYR B 98 ? 0.4962 0.5601 0.6610 0.0041 0.0549 0.1424 96 TYR B CE1 2340 C CE2 . TYR B 98 ? 0.3523 0.4059 0.5379 0.0057 0.0526 0.1458 96 TYR B CE2 2341 C CZ . TYR B 98 ? 0.4323 0.5033 0.6107 0.0039 0.0511 0.1512 96 TYR B CZ 2342 O OH . TYR B 98 ? 0.3511 0.4484 0.5364 0.0020 0.0458 0.1660 96 TYR B OH 2343 N N . PRO B 99 ? 0.2265 0.2196 0.3387 0.0129 0.0779 0.0928 97 PRO B N 2344 C CA . PRO B 99 ? 0.1817 0.1864 0.2818 0.0148 0.0790 0.0912 97 PRO B CA 2345 C C . PRO B 99 ? 0.1559 0.1828 0.2641 0.0127 0.0761 0.1028 97 PRO B C 2346 O O . PRO B 99 ? 0.2302 0.2570 0.3520 0.0092 0.0709 0.1097 97 PRO B O 2347 C CB . PRO B 99 ? 0.1620 0.1479 0.2527 0.0161 0.0794 0.0811 97 PRO B CB 2348 C CG . PRO B 99 ? 0.2601 0.2314 0.3629 0.0130 0.0777 0.0817 97 PRO B CG 2349 C CD . PRO B 99 ? 0.2369 0.2082 0.3498 0.0125 0.0782 0.0849 97 PRO B CD 2350 N N . GLU B 100 ? 0.2266 0.2741 0.3256 0.0156 0.0772 0.1015 98 GLU B N 2351 C CA . GLU B 100 ? 0.2762 0.3477 0.3792 0.0146 0.0754 0.1098 98 GLU B CA 2352 C C . GLU B 100 ? 0.2738 0.3348 0.3680 0.0175 0.0753 0.1005 98 GLU B C 2353 O O . GLU B 100 ? 0.2349 0.2833 0.3161 0.0223 0.0772 0.0878 98 GLU B O 2354 C CB . GLU B 100 ? 0.4229 0.5253 0.5198 0.0172 0.0758 0.1104 98 GLU B CB 2355 C CG . GLU B 100 ? 0.7041 0.8055 0.7857 0.0239 0.0794 0.0944 98 GLU B CG 2356 C CD . GLU B 100 ? 0.7951 0.9304 0.8720 0.0280 0.0801 0.0919 98 GLU B CD 2357 O OE1 . GLU B 100 ? 0.8264 0.9816 0.9083 0.0261 0.0778 0.1004 98 GLU B OE1 2358 O OE2 . GLU B 100 ? 0.7142 0.8550 0.7821 0.0328 0.0815 0.0794 98 GLU B OE2 2359 N N . VAL B 101 ? 0.1886 0.2547 0.2920 0.0140 0.0725 0.1080 99 VAL B N 2360 C CA . VAL B 101 ? 0.2109 0.2690 0.3082 0.0161 0.0715 0.1010 99 VAL B CA 2361 C C . VAL B 101 ? 0.2370 0.3234 0.3369 0.0169 0.0706 0.1066 99 VAL B C 2362 O O . VAL B 101 ? 0.2009 0.3063 0.3143 0.0115 0.0686 0.1206 99 VAL B O 2363 C CB . VAL B 101 ? 0.1648 0.2012 0.2702 0.0113 0.0684 0.1014 99 VAL B CB 2364 C CG1 . VAL B 101 ? 0.2002 0.2299 0.2977 0.0134 0.0670 0.0939 99 VAL B CG1 2365 C CG2 . VAL B 101 ? 0.1633 0.1758 0.2670 0.0111 0.0699 0.0950 99 VAL B CG2 2366 N N . THR B 102 ? 0.1957 0.2852 0.2838 0.0238 0.0720 0.0961 100 THR B N 2367 C CA . THR B 102 ? 0.2773 0.3946 0.3667 0.0268 0.0718 0.0980 100 THR B CA 2368 C C . THR B 102 ? 0.2833 0.3893 0.3684 0.0303 0.0699 0.0909 100 THR B C 2369 O O . THR B 102 ? 0.2792 0.3616 0.3544 0.0343 0.0702 0.0805 100 THR B O 2370 C CB . THR B 102 ? 0.1551 0.2936 0.2366 0.0342 0.0750 0.0901 100 THR B CB 2371 O OG1 . THR B 102 ? 0.5118 0.6645 0.5964 0.0309 0.0763 0.0971 100 THR B OG1 2372 C CG2 . THR B 102 ? 0.1605 0.3314 0.2440 0.0385 0.0753 0.0903 100 THR B CG2 2373 N N . VAL B 103 ? 0.2498 0.3740 0.3432 0.0280 0.0677 0.0981 101 VAL B N 2374 C CA . VAL B 103 ? 0.2167 0.3364 0.3069 0.0320 0.0656 0.0922 101 VAL B CA 2375 C C . VAL B 103 ? 0.2872 0.4395 0.3787 0.0386 0.0669 0.0910 101 VAL B C 2376 O O . VAL B 103 ? 0.2433 0.4264 0.3440 0.0352 0.0675 0.1011 101 VAL B O 2377 C CB . VAL B 103 ? 0.2446 0.3567 0.3442 0.0239 0.0611 0.0993 101 VAL B CB 2378 C CG1 . VAL B 103 ? 0.2732 0.3878 0.3702 0.0281 0.0585 0.0947 101 VAL B CG1 2379 C CG2 . VAL B 103 ? 0.2051 0.2851 0.3027 0.0192 0.0599 0.0962 101 VAL B CG2 2380 N N . TYR B 104 ? 0.2791 0.4258 0.3627 0.0482 0.0671 0.0789 102 TYR B N 2381 C CA . TYR B 104 ? 0.2563 0.4323 0.3425 0.0566 0.0680 0.0747 102 TYR B CA 2382 C C . TYR B 104 ? 0.2702 0.4335 0.3540 0.0638 0.0651 0.0671 102 TYR B C 2383 O O . TYR B 104 ? 0.2235 0.3553 0.3000 0.0648 0.0634 0.0620 102 TYR B O 2384 C CB . TYR B 104 ? 0.2528 0.4443 0.3346 0.0639 0.0719 0.0652 102 TYR B CB 2385 C CG . TYR B 104 ? 0.2945 0.4565 0.3669 0.0697 0.0722 0.0519 102 TYR B CG 2386 C CD1 . TYR B 104 ? 0.3372 0.4903 0.4078 0.0802 0.0708 0.0392 102 TYR B CD1 2387 C CD2 . TYR B 104 ? 0.2868 0.4312 0.3543 0.0645 0.0735 0.0527 102 TYR B CD2 2388 C CE1 . TYR B 104 ? 0.3792 0.5053 0.4439 0.0844 0.0703 0.0287 102 TYR B CE1 2389 C CE2 . TYR B 104 ? 0.2903 0.4096 0.3507 0.0687 0.0736 0.0416 102 TYR B CE2 2390 C CZ . TYR B 104 ? 0.3502 0.4601 0.4095 0.0782 0.0719 0.0300 102 TYR B CZ 2391 O OH . TYR B 104 ? 0.3918 0.4762 0.4467 0.0812 0.0712 0.0207 102 TYR B OH 2392 N N . PRO B 105 ? 0.2240 0.4143 0.3148 0.0686 0.0643 0.0676 103 PRO B N 2393 C CA . PRO B 105 ? 0.1921 0.3730 0.2829 0.0761 0.0608 0.0618 103 PRO B CA 2394 C C . PRO B 105 ? 0.2748 0.4505 0.3624 0.0894 0.0618 0.0470 103 PRO B C 2395 O O . PRO B 105 ? 0.3323 0.5248 0.4200 0.0941 0.0654 0.0398 103 PRO B O 2396 C CB . PRO B 105 ? 0.2083 0.4241 0.3103 0.0759 0.0598 0.0686 103 PRO B CB 2397 C CG . PRO B 105 ? 0.2074 0.4577 0.3138 0.0745 0.0645 0.0720 103 PRO B CG 2398 C CD . PRO B 105 ? 0.1926 0.4247 0.2933 0.0662 0.0662 0.0760 103 PRO B CD 2399 N N . ALA B 106 ? 0.2144 0.3672 0.3001 0.0949 0.0579 0.0429 104 ALA B N 2400 C CA . ALA B 106 ? 0.2225 0.3654 0.3091 0.1074 0.0570 0.0299 104 ALA B CA 2401 C C . ALA B 106 ? 0.3298 0.4681 0.4222 0.1148 0.0518 0.0301 104 ALA B C 2402 O O . ALA B 106 ? 0.2753 0.4222 0.3699 0.1100 0.0493 0.0395 104 ALA B O 2403 C CB . ALA B 106 ? 0.2043 0.3134 0.2823 0.1052 0.0572 0.0260 104 ALA B CB 2404 N N . LYS B 107 ? 0.4148 0.5400 0.5112 0.1262 0.0494 0.0200 105 LYS B N 2405 C CA . LYS B 107 ? 0.4091 0.5300 0.5135 0.1348 0.0437 0.0207 105 LYS B CA 2406 C C . LYS B 107 ? 0.4156 0.4985 0.5168 0.1361 0.0395 0.0210 105 LYS B C 2407 O O . LYS B 107 ? 0.4282 0.4946 0.5280 0.1379 0.0409 0.0130 105 LYS B O 2408 C CB . LYS B 107 ? 0.3629 0.5096 0.4813 0.1497 0.0440 0.0084 105 LYS B CB 2409 C CG . LYS B 107 ? 0.4039 0.5938 0.5263 0.1483 0.0484 0.0097 105 LYS B CG 2410 C CD . LYS B 107 ? 0.4882 0.7051 0.6233 0.1625 0.0490 -0.0048 105 LYS B CD 2411 C CE . LYS B 107 ? 0.5343 0.7921 0.6705 0.1564 0.0522 -0.0011 105 LYS B CE 2412 N NZ . LYS B 107 ? 0.5723 0.8501 0.7165 0.1648 0.0516 -0.0153 105 LYS B NZ 2413 N N . THR B 108 ? 0.4449 0.5158 0.5456 0.1349 0.0341 0.0308 106 THR B N 2414 C CA . THR B 108 ? 0.4981 0.5367 0.5973 0.1363 0.0296 0.0336 106 THR B CA 2415 C C . THR B 108 ? 0.5261 0.5601 0.6418 0.1516 0.0254 0.0246 106 THR B C 2416 O O . THR B 108 ? 0.4981 0.5069 0.6168 0.1541 0.0233 0.0213 106 THR B O 2417 C CB . THR B 108 ? 0.4674 0.4980 0.5603 0.1299 0.0247 0.0479 106 THR B CB 2418 O OG1 . THR B 108 ? 0.4199 0.4724 0.5224 0.1362 0.0208 0.0508 106 THR B OG1 2419 C CG2 . THR B 108 ? 0.4544 0.4853 0.5325 0.1151 0.0282 0.0541 106 THR B CG2 2420 N N . GLN B 109 ? 0.5644 0.6230 0.6927 0.1618 0.0239 0.0204 107 GLN B N 2421 C CA . GLN B 109 ? 0.7173 0.7744 0.8645 0.1781 0.0200 0.0089 107 GLN B CA 2422 C C . GLN B 109 ? 0.7977 0.8918 0.9541 0.1872 0.0243 -0.0046 107 GLN B C 2423 O O . GLN B 109 ? 0.7935 0.9160 0.9462 0.1826 0.0272 0.0011 107 GLN B O 2424 C CB . GLN B 109 ? 0.7664 0.8145 0.9247 0.1850 0.0114 0.0188 107 GLN B CB 2425 C CG . GLN B 109 ? 0.8514 0.8654 1.0034 0.1781 0.0063 0.0324 107 GLN B CG 2426 C CD . GLN B 109 ? 0.9411 0.9494 1.1066 0.1861 -0.0030 0.0432 107 GLN B CD 2427 O OE1 . GLN B 109 ? 0.9346 0.9423 1.0910 0.1784 -0.0064 0.0594 107 GLN B OE1 2428 N NE2 . GLN B 109 ? 0.9831 0.9881 1.1701 0.1998 -0.0082 0.0327 107 GLN B NE2 2429 N N . PRO B 110 ? 0.8728 0.9661 1.0403 0.1943 0.0245 -0.0226 108 PRO B N 2430 C CA . PRO B 110 ? 0.9019 1.0295 1.0744 0.1968 0.0292 -0.0359 108 PRO B CA 2431 C C . PRO B 110 ? 0.9507 1.1048 1.1326 0.2016 0.0271 -0.0312 108 PRO B C 2432 O O . PRO B 110 ? 0.9650 1.1073 1.1529 0.2049 0.0208 -0.0202 108 PRO B O 2433 C CB . PRO B 110 ? 0.9151 1.0278 1.0989 0.2033 0.0282 -0.0529 108 PRO B CB 2434 C CG . PRO B 110 ? 0.9080 0.9799 1.0986 0.2054 0.0215 -0.0458 108 PRO B CG 2435 C CD . PRO B 110 ? 0.8550 0.9143 1.0302 0.1968 0.0208 -0.0298 108 PRO B CD 2436 N N . LEU B 111 ? 0.9487 1.1385 1.1314 0.2015 0.0320 -0.0386 109 LEU B N 2437 C CA . LEU B 111 ? 0.9004 1.1201 1.0910 0.2045 0.0310 -0.0341 109 LEU B CA 2438 C C . LEU B 111 ? 0.8300 1.0623 1.0133 0.1964 0.0305 -0.0150 109 LEU B C 2439 O O . LEU B 111 ? 0.8668 1.1316 1.0525 0.1940 0.0321 -0.0112 109 LEU B O 2440 C CB . LEU B 111 ? 0.9079 1.1157 1.1179 0.2167 0.0244 -0.0380 109 LEU B CB 2441 N N . GLN B 112 ? 0.7102 0.9178 0.8847 0.1915 0.0283 -0.0024 110 GLN B N 2442 C CA . GLN B 112 ? 0.7644 0.9828 0.9342 0.1841 0.0272 0.0157 110 GLN B CA 2443 C C . GLN B 112 ? 0.7756 1.0166 0.9360 0.1716 0.0342 0.0203 110 GLN B C 2444 O O . GLN B 112 ? 0.8521 1.0932 1.0062 0.1691 0.0395 0.0122 110 GLN B O 2445 C CB . GLN B 112 ? 0.8464 1.0269 1.0061 0.1765 0.0219 0.0277 110 GLN B CB 2446 C CG . GLN B 112 ? 0.9519 1.1196 1.1222 0.1859 0.0133 0.0326 110 GLN B CG 2447 C CD . GLN B 112 ? 1.0136 1.1402 1.1753 0.1816 0.0088 0.0395 110 GLN B CD 2448 O OE1 . GLN B 112 ? 0.9889 1.0995 1.1337 0.1678 0.0114 0.0453 110 GLN B OE1 2449 N NE2 . GLN B 112 ? 1.0562 1.1669 1.2313 0.1932 0.0019 0.0399 110 GLN B NE2 2450 N N . HIS B 113 ? 0.6471 0.9046 0.8064 0.1613 0.0331 0.0335 111 HIS B N 2451 C CA . HIS B 113 ? 0.4477 0.7213 0.6001 0.1469 0.0381 0.0406 111 HIS B CA 2452 C C . HIS B 113 ? 0.3633 0.6015 0.4999 0.1352 0.0391 0.0440 111 HIS B C 2453 O O . HIS B 113 ? 0.3515 0.5553 0.4818 0.1366 0.0355 0.0431 111 HIS B O 2454 C CB . HIS B 113 ? 0.4437 0.7380 0.6011 0.1376 0.0350 0.0541 111 HIS B CB 2455 C CG . HIS B 113 ? 0.4979 0.8312 0.6700 0.1458 0.0348 0.0520 111 HIS B CG 2456 N ND1 . HIS B 113 ? 0.4479 0.7778 0.6276 0.1592 0.0307 0.0436 111 HIS B ND1 2457 C CD2 . HIS B 113 ? 0.5305 0.8965 0.7062 0.1378 0.0370 0.0566 111 HIS B CD2 2458 C CE1 . HIS B 113 ? 0.4457 0.8064 0.6334 0.1600 0.0310 0.0421 111 HIS B CE1 2459 N NE2 . HIS B 113 ? 0.4812 0.8642 0.6655 0.1470 0.0348 0.0502 111 HIS B NE2 2460 N N . HIS B 114 ? 0.3761 0.6243 0.5077 0.1239 0.0438 0.0487 112 HIS B N 2461 C CA . HIS B 114 ? 0.3597 0.5782 0.4784 0.1126 0.0450 0.0522 112 HIS B CA 2462 C C . HIS B 114 ? 0.3449 0.5364 0.4570 0.1040 0.0395 0.0603 112 HIS B C 2463 O O . HIS B 114 ? 0.4348 0.6383 0.5509 0.0964 0.0365 0.0689 112 HIS B O 2464 C CB . HIS B 114 ? 0.4683 0.7067 0.5871 0.1017 0.0497 0.0588 112 HIS B CB 2465 C CG . HIS B 114 ? 0.6064 0.8629 0.7251 0.1077 0.0556 0.0502 112 HIS B CG 2466 N ND1 . HIS B 114 ? 0.6502 0.9449 0.7745 0.1037 0.0599 0.0554 112 HIS B ND1 2467 C CD2 . HIS B 114 ? 0.6827 0.9264 0.7971 0.1170 0.0576 0.0367 112 HIS B CD2 2468 C CE1 . HIS B 114 ? 0.7023 1.0048 0.8220 0.1093 0.0636 0.0443 112 HIS B CE1 2469 N NE2 . HIS B 114 ? 0.7060 0.9810 0.8221 0.1189 0.0630 0.0323 112 HIS B NE2 2470 N N . ASN B 115 ? 0.3237 0.4812 0.4261 0.1049 0.0381 0.0573 113 ASN B N 2471 C CA . ASN B 115 ? 0.2691 0.4043 0.3638 0.0978 0.0331 0.0639 113 ASN B CA 2472 C C . ASN B 115 ? 0.2527 0.3577 0.3348 0.0915 0.0353 0.0626 113 ASN B C 2473 O O . ASN B 115 ? 0.2186 0.3024 0.2923 0.0881 0.0321 0.0656 113 ASN B O 2474 C CB . ASN B 115 ? 0.3306 0.4601 0.4287 0.1074 0.0271 0.0643 113 ASN B CB 2475 C CG . ASN B 115 ? 0.3758 0.4851 0.4740 0.1181 0.0272 0.0573 113 ASN B CG 2476 O OD1 . ASN B 115 ? 0.3009 0.4050 0.3977 0.1200 0.0320 0.0496 113 ASN B OD1 2477 N ND2 . ASN B 115 ? 0.4412 0.5387 0.5420 0.1244 0.0211 0.0606 113 ASN B ND2 2478 N N . LEU B 116 ? 0.2910 0.3972 0.3719 0.0900 0.0409 0.0586 114 LEU B N 2479 C CA . LEU B 116 ? 0.3202 0.4012 0.3908 0.0843 0.0436 0.0572 114 LEU B CA 2480 C C . LEU B 116 ? 0.3526 0.4435 0.4240 0.0760 0.0482 0.0592 114 LEU B C 2481 O O . LEU B 116 ? 0.4403 0.5538 0.5179 0.0793 0.0514 0.0572 114 LEU B O 2482 C CB . LEU B 116 ? 0.3539 0.4202 0.4233 0.0937 0.0447 0.0489 114 LEU B CB 2483 C CG . LEU B 116 ? 0.3930 0.4294 0.4526 0.0899 0.0457 0.0479 114 LEU B CG 2484 C CD1 . LEU B 116 ? 0.3694 0.3889 0.4221 0.0857 0.0414 0.0549 114 LEU B CD1 2485 C CD2 . LEU B 116 ? 0.4041 0.4309 0.4677 0.0996 0.0458 0.0391 114 LEU B CD2 2486 N N . LEU B 117 ? 0.2901 0.3660 0.3561 0.0656 0.0483 0.0633 115 LEU B N 2487 C CA . LEU B 117 ? 0.2644 0.3457 0.3331 0.0579 0.0518 0.0664 115 LEU B CA 2488 C C . LEU B 117 ? 0.2213 0.2800 0.2814 0.0570 0.0550 0.0622 115 LEU B C 2489 O O . LEU B 117 ? 0.1924 0.2285 0.2447 0.0542 0.0539 0.0611 115 LEU B O 2490 C CB . LEU B 117 ? 0.2114 0.2938 0.2850 0.0468 0.0491 0.0736 115 LEU B CB 2491 C CG . LEU B 117 ? 0.2601 0.3671 0.3447 0.0450 0.0455 0.0794 115 LEU B CG 2492 C CD1 . LEU B 117 ? 0.2373 0.3418 0.3292 0.0328 0.0422 0.0854 115 LEU B CD1 2493 C CD2 . LEU B 117 ? 0.2613 0.3993 0.3546 0.0491 0.0487 0.0822 115 LEU B CD2 2494 N N . VAL B 118 ? 0.2275 0.2956 0.2893 0.0591 0.0590 0.0599 116 VAL B N 2495 C CA . VAL B 118 ? 0.1841 0.2340 0.2393 0.0583 0.0619 0.0557 116 VAL B CA 2496 C C . VAL B 118 ? 0.1841 0.2342 0.2420 0.0492 0.0639 0.0617 116 VAL B C 2497 O O . VAL B 118 ? 0.2022 0.2747 0.2680 0.0467 0.0650 0.0674 116 VAL B O 2498 C CB . VAL B 118 ? 0.2428 0.3016 0.2980 0.0667 0.0643 0.0474 116 VAL B CB 2499 C CG1 . VAL B 118 ? 0.2079 0.2471 0.2570 0.0651 0.0666 0.0431 116 VAL B CG1 2500 C CG2 . VAL B 118 ? 0.2030 0.2614 0.2597 0.0771 0.0616 0.0407 116 VAL B CG2 2501 N N . CYS B 119 ? 0.2011 0.2279 0.2537 0.0444 0.0642 0.0612 117 CYS B N 2502 C CA . CYS B 119 ? 0.2353 0.2596 0.2921 0.0375 0.0661 0.0654 117 CYS B CA 2503 C C . CYS B 119 ? 0.2374 0.2533 0.2885 0.0401 0.0695 0.0603 117 CYS B C 2504 O O . CYS B 119 ? 0.2006 0.1961 0.2440 0.0407 0.0701 0.0555 117 CYS B O 2505 C CB . CYS B 119 ? 0.1784 0.1854 0.2355 0.0307 0.0643 0.0664 117 CYS B CB 2506 S SG . CYS B 119 ? 0.2620 0.2666 0.3298 0.0233 0.0656 0.0719 117 CYS B SG 2507 N N . SER B 120 ? 0.1709 0.2053 0.2262 0.0411 0.0716 0.0620 118 SER B N 2508 C CA . SER B 120 ? 0.2260 0.2562 0.2770 0.0433 0.0742 0.0565 118 SER B CA 2509 C C . SER B 120 ? 0.2419 0.2674 0.2970 0.0366 0.0756 0.0624 118 SER B C 2510 O O . SER B 120 ? 0.2947 0.3369 0.3589 0.0325 0.0754 0.0715 118 SER B O 2511 C CB . SER B 120 ? 0.2202 0.2760 0.2725 0.0490 0.0753 0.0526 118 SER B CB 2512 O OG . SER B 120 ? 0.2781 0.3289 0.3261 0.0512 0.0770 0.0449 118 SER B OG 2513 N N . VAL B 121 ? 0.1769 0.1805 0.2267 0.0354 0.0769 0.0582 119 VAL B N 2514 C CA . VAL B 121 ? 0.1676 0.1648 0.2224 0.0301 0.0783 0.0623 119 VAL B CA 2515 C C . VAL B 121 ? 0.2085 0.2059 0.2600 0.0316 0.0806 0.0581 119 VAL B C 2516 O O . VAL B 121 ? 0.1806 0.1633 0.2246 0.0337 0.0815 0.0508 119 VAL B O 2517 C CB . VAL B 121 ? 0.1716 0.1467 0.2244 0.0269 0.0781 0.0604 119 VAL B CB 2518 C CG1 . VAL B 121 ? 0.1698 0.1399 0.2312 0.0225 0.0791 0.0639 119 VAL B CG1 2519 C CG2 . VAL B 121 ? 0.1736 0.1494 0.2286 0.0256 0.0749 0.0624 119 VAL B CG2 2520 N N . ASN B 122 ? 0.1798 0.1954 0.2379 0.0300 0.0811 0.0637 120 ASN B N 2521 C CA . ASN B 122 ? 0.1728 0.1956 0.2279 0.0317 0.0825 0.0590 120 ASN B CA 2522 C C . ASN B 122 ? 0.1594 0.1848 0.2215 0.0275 0.0834 0.0654 120 ASN B C 2523 O O . ASN B 122 ? 0.2036 0.2362 0.2761 0.0238 0.0823 0.0765 120 ASN B O 2524 C CB . ASN B 122 ? 0.1706 0.2218 0.2250 0.0356 0.0821 0.0571 120 ASN B CB 2525 C CG . ASN B 122 ? 0.1881 0.2387 0.2376 0.0415 0.0811 0.0490 120 ASN B CG 2526 O OD1 . ASN B 122 ? 0.2395 0.2968 0.2918 0.0416 0.0800 0.0540 120 ASN B OD1 2527 N ND2 . ASN B 122 ? 0.2615 0.3044 0.3055 0.0465 0.0810 0.0366 120 ASN B ND2 2528 N N . GLY B 123 ? 0.2092 0.2284 0.2672 0.0280 0.0847 0.0589 121 GLY B N 2529 C CA . GLY B 123 ? 0.1584 0.1857 0.2227 0.0251 0.0852 0.0640 121 GLY B CA 2530 C C . GLY B 123 ? 0.2462 0.2565 0.3177 0.0218 0.0862 0.0685 121 GLY B C 2531 O O . GLY B 123 ? 0.2757 0.2947 0.3567 0.0196 0.0859 0.0758 121 GLY B O 2532 N N . PHE B 124 ? 0.1811 0.1695 0.2490 0.0217 0.0872 0.0640 122 PHE B N 2533 C CA . PHE B 124 ? 0.1999 0.1752 0.2756 0.0193 0.0883 0.0662 122 PHE B CA 2534 C C . PHE B 124 ? 0.2403 0.2047 0.3124 0.0189 0.0913 0.0601 122 PHE B C 2535 O O . PHE B 124 ? 0.2671 0.2277 0.3295 0.0197 0.0922 0.0536 122 PHE B O 2536 C CB . PHE B 124 ? 0.1744 0.1366 0.2495 0.0189 0.0876 0.0645 122 PHE B CB 2537 C CG . PHE B 124 ? 0.1692 0.1202 0.2302 0.0207 0.0884 0.0565 122 PHE B CG 2538 C CD1 . PHE B 124 ? 0.1885 0.1454 0.2435 0.0230 0.0865 0.0559 122 PHE B CD1 2539 C CD2 . PHE B 124 ? 0.1741 0.1106 0.2290 0.0200 0.0909 0.0508 122 PHE B CD2 2540 C CE1 . PHE B 124 ? 0.2061 0.1525 0.2504 0.0250 0.0863 0.0502 122 PHE B CE1 2541 C CE2 . PHE B 124 ? 0.1797 0.1073 0.2228 0.0211 0.0910 0.0464 122 PHE B CE2 2542 C CZ . PHE B 124 ? 0.1803 0.1118 0.2188 0.0237 0.0883 0.0465 122 PHE B CZ 2543 N N . TYR B 125 ? 0.2191 0.1791 0.3014 0.0176 0.0924 0.0623 123 TYR B N 2544 C CA . TYR B 125 ? 0.1660 0.1177 0.2472 0.0170 0.0958 0.0572 123 TYR B CA 2545 C C . TYR B 125 ? 0.2309 0.1754 0.3236 0.0170 0.0969 0.0571 123 TYR B C 2546 O O . TYR B 125 ? 0.1663 0.1157 0.2739 0.0172 0.0943 0.0637 123 TYR B O 2547 C CB . TYR B 125 ? 0.1774 0.1409 0.2618 0.0162 0.0960 0.0591 123 TYR B CB 2548 C CG . TYR B 125 ? 0.2192 0.1757 0.3011 0.0148 0.0994 0.0537 123 TYR B CG 2549 C CD1 . TYR B 125 ? 0.1952 0.1503 0.2877 0.0148 0.1018 0.0544 123 TYR B CD1 2550 C CD2 . TYR B 125 ? 0.2295 0.1814 0.3005 0.0135 0.1001 0.0482 123 TYR B CD2 2551 C CE1 . TYR B 125 ? 0.1693 0.1215 0.2600 0.0133 0.1054 0.0501 123 TYR B CE1 2552 C CE2 . TYR B 125 ? 0.2127 0.1598 0.2830 0.0110 0.1030 0.0453 123 TYR B CE2 2553 C CZ . TYR B 125 ? 0.2518 0.2006 0.3312 0.0107 0.1061 0.0464 123 TYR B CZ 2554 O OH . TYR B 125 ? 0.2853 0.2330 0.3645 0.0080 0.1094 0.0441 123 TYR B OH 2555 N N . PRO B 126 ? 0.1731 0.1074 0.2606 0.0170 0.1004 0.0495 124 PRO B N 2556 C CA . PRO B 126 ? 0.1770 0.1059 0.2494 0.0158 0.1031 0.0443 124 PRO B CA 2557 C C . PRO B 126 ? 0.2928 0.2152 0.3527 0.0160 0.1016 0.0423 124 PRO B C 2558 O O . PRO B 126 ? 0.1787 0.1026 0.2406 0.0170 0.0985 0.0447 124 PRO B O 2559 C CB . PRO B 126 ? 0.2163 0.1421 0.2912 0.0156 0.1074 0.0391 124 PRO B CB 2560 C CG . PRO B 126 ? 0.1828 0.1068 0.2702 0.0176 0.1062 0.0374 124 PRO B CG 2561 C CD . PRO B 126 ? 0.1766 0.1065 0.2761 0.0181 0.1018 0.0460 124 PRO B CD 2562 N N . GLY B 127 ? 0.1863 0.1028 0.2348 0.0147 0.1036 0.0394 125 GLY B N 2563 C CA . GLY B 127 ? 0.3103 0.2213 0.3477 0.0152 0.1014 0.0392 125 GLY B CA 2564 C C . GLY B 127 ? 0.2727 0.1807 0.3064 0.0155 0.1008 0.0369 125 GLY B C 2565 O O . GLY B 127 ? 0.3279 0.2344 0.3561 0.0167 0.0977 0.0379 125 GLY B O 2566 N N . SER B 128 ? 0.3106 0.2191 0.3481 0.0149 0.1035 0.0326 126 SER B N 2567 C CA . SER B 128 ? 0.3303 0.2377 0.3644 0.0150 0.1027 0.0278 126 SER B CA 2568 C C . SER B 128 ? 0.2613 0.1686 0.3032 0.0160 0.0980 0.0292 126 SER B C 2569 O O . SER B 128 ? 0.2998 0.2087 0.3561 0.0165 0.0968 0.0309 126 SER B O 2570 C CB . SER B 128 ? 0.4047 0.3148 0.4440 0.0150 0.1064 0.0201 126 SER B CB 2571 O OG . SER B 128 ? 0.5569 0.4665 0.6137 0.0167 0.1051 0.0182 126 SER B OG 2572 N N . ILE B 129 ? 0.2374 0.1440 0.2710 0.0160 0.0949 0.0298 127 ILE B N 2573 C CA . ILE B 129 ? 0.3296 0.2382 0.3704 0.0162 0.0903 0.0321 127 ILE B CA 2574 C C . ILE B 129 ? 0.3345 0.2432 0.3668 0.0157 0.0874 0.0291 127 ILE B C 2575 O O . ILE B 129 ? 0.3731 0.2811 0.3918 0.0158 0.0883 0.0287 127 ILE B O 2576 C CB . ILE B 129 ? 0.3170 0.2308 0.3594 0.0177 0.0885 0.0395 127 ILE B CB 2577 C CG1 . ILE B 129 ? 0.3218 0.2420 0.3768 0.0169 0.0847 0.0442 127 ILE B CG1 2578 C CG2 . ILE B 129 ? 0.2159 0.1290 0.2454 0.0195 0.0874 0.0405 127 ILE B CG2 2579 C CD1 . ILE B 129 ? 0.2991 0.2303 0.3579 0.0182 0.0840 0.0514 127 ILE B CD1 2580 N N . GLU B 130 ? 0.3313 0.2415 0.3729 0.0145 0.0835 0.0280 128 GLU B N 2581 C CA . GLU B 130 ? 0.3669 0.2792 0.4019 0.0136 0.0798 0.0254 128 GLU B CA 2582 C C . GLU B 130 ? 0.2434 0.1610 0.2867 0.0131 0.0751 0.0317 128 GLU B C 2583 O O . GLU B 130 ? 0.2270 0.1458 0.2863 0.0113 0.0730 0.0342 128 GLU B O 2584 C CB . GLU B 130 ? 0.4287 0.3399 0.4671 0.0116 0.0790 0.0145 128 GLU B CB 2585 C CG . GLU B 130 ? 0.5828 0.4985 0.6144 0.0100 0.0745 0.0107 128 GLU B CG 2586 C CD . GLU B 130 ? 0.6703 0.5905 0.6822 0.0105 0.0765 0.0088 128 GLU B CD 2587 O OE1 . GLU B 130 ? 0.6689 0.5943 0.6721 0.0102 0.0729 0.0118 128 GLU B OE1 2588 O OE2 . GLU B 130 ? 0.6711 0.5913 0.6771 0.0108 0.0815 0.0054 128 GLU B OE2 2589 N N . VAL B 131 ? 0.2073 0.1293 0.2410 0.0149 0.0732 0.0353 129 VAL B N 2590 C CA . VAL B 131 ? 0.2745 0.2052 0.3150 0.0150 0.0693 0.0413 129 VAL B CA 2591 C C . VAL B 131 ? 0.3103 0.2447 0.3455 0.0141 0.0649 0.0390 129 VAL B C 2592 O O . VAL B 131 ? 0.2943 0.2277 0.3160 0.0160 0.0650 0.0378 129 VAL B O 2593 C CB . VAL B 131 ? 0.2824 0.2185 0.3190 0.0194 0.0706 0.0470 129 VAL B CB 2594 C CG1 . VAL B 131 ? 0.2260 0.1760 0.2703 0.0200 0.0673 0.0527 129 VAL B CG1 2595 C CG2 . VAL B 131 ? 0.2189 0.1532 0.2590 0.0201 0.0746 0.0483 129 VAL B CG2 2596 N N . ARG B 132 ? 0.2966 0.2364 0.3438 0.0106 0.0605 0.0396 130 ARG B N 2597 C CA . ARG B 132 ? 0.3004 0.2456 0.3444 0.0088 0.0555 0.0369 130 ARG B CA 2598 C C . ARG B 132 ? 0.2771 0.2346 0.3320 0.0077 0.0513 0.0443 130 ARG B C 2599 O O . ARG B 132 ? 0.2051 0.1669 0.2743 0.0057 0.0512 0.0504 130 ARG B O 2600 C CB . ARG B 132 ? 0.3633 0.3035 0.4112 0.0043 0.0533 0.0262 130 ARG B CB 2601 C CG . ARG B 132 ? 0.4833 0.4170 0.5181 0.0058 0.0577 0.0181 130 ARG B CG 2602 C CD . ARG B 132 ? 0.6136 0.5452 0.6525 0.0024 0.0561 0.0044 130 ARG B CD 2603 N NE . ARG B 132 ? 0.7061 0.6339 0.7673 -0.0013 0.0518 0.0016 130 ARG B NE 2604 C CZ . ARG B 132 ? 0.7516 0.6728 0.8242 -0.0029 0.0514 -0.0104 130 ARG B CZ 2605 N NH1 . ARG B 132 ? 0.8238 0.7443 0.8855 -0.0006 0.0559 -0.0211 130 ARG B NH1 2606 N NH2 . ARG B 132 ? 0.6162 0.5321 0.7125 -0.0065 0.0464 -0.0113 130 ARG B NH2 2607 N N . TRP B 133 ? 0.2148 0.1803 0.2634 0.0088 0.0476 0.0448 131 TRP B N 2608 C CA . TRP B 133 ? 0.2110 0.1913 0.2698 0.0079 0.0436 0.0515 131 TRP B CA 2609 C C . TRP B 133 ? 0.2833 0.2674 0.3510 0.0012 0.0372 0.0479 131 TRP B C 2610 O O . TRP B 133 ? 0.3125 0.2922 0.3720 -0.0004 0.0350 0.0392 131 TRP B O 2611 C CB . TRP B 133 ? 0.2469 0.2360 0.2960 0.0145 0.0433 0.0552 131 TRP B CB 2612 C CG . TRP B 133 ? 0.2757 0.2689 0.3247 0.0207 0.0474 0.0599 131 TRP B CG 2613 C CD1 . TRP B 133 ? 0.2814 0.2663 0.3198 0.0267 0.0509 0.0584 131 TRP B CD1 2614 C CD2 . TRP B 133 ? 0.2246 0.2337 0.2854 0.0212 0.0481 0.0663 131 TRP B CD2 2615 N NE1 . TRP B 133 ? 0.2258 0.2194 0.2687 0.0315 0.0535 0.0611 131 TRP B NE1 2616 C CE2 . TRP B 133 ? 0.2036 0.2140 0.2592 0.0284 0.0522 0.0661 131 TRP B CE2 2617 C CE3 . TRP B 133 ? 0.2330 0.2571 0.3091 0.0158 0.0454 0.0725 131 TRP B CE3 2618 C CZ2 . TRP B 133 ? 0.1845 0.2130 0.2477 0.0310 0.0542 0.0704 131 TRP B CZ2 2619 C CZ3 . TRP B 133 ? 0.2609 0.3037 0.3449 0.0178 0.0476 0.0795 131 TRP B CZ3 2620 C CH2 . TRP B 133 ? 0.2400 0.2861 0.3165 0.0256 0.0522 0.0777 131 TRP B CH2 2621 N N . PHE B 134 ? 0.2140 0.2085 0.2991 -0.0031 0.0340 0.0547 132 PHE B N 2622 C CA . PHE B 134 ? 0.2973 0.2963 0.3944 -0.0104 0.0269 0.0520 132 PHE B CA 2623 C C . PHE B 134 ? 0.2869 0.3067 0.3926 -0.0111 0.0236 0.0620 132 PHE B C 2624 O O . PHE B 134 ? 0.3040 0.3349 0.4157 -0.0090 0.0266 0.0721 132 PHE B O 2625 C CB . PHE B 134 ? 0.2241 0.2131 0.3410 -0.0176 0.0248 0.0503 132 PHE B CB 2626 C CG . PHE B 134 ? 0.3202 0.2909 0.4312 -0.0167 0.0273 0.0379 132 PHE B CG 2627 C CD1 . PHE B 134 ? 0.3156 0.2779 0.4202 -0.0120 0.0341 0.0393 132 PHE B CD1 2628 C CD2 . PHE B 134 ? 0.2995 0.2639 0.4124 -0.0206 0.0227 0.0239 132 PHE B CD2 2629 C CE1 . PHE B 134 ? 0.3062 0.2546 0.4064 -0.0110 0.0368 0.0281 132 PHE B CE1 2630 C CE2 . PHE B 134 ? 0.3040 0.2553 0.4119 -0.0191 0.0256 0.0112 132 PHE B CE2 2631 C CZ . PHE B 134 ? 0.2756 0.2192 0.3775 -0.0142 0.0328 0.0139 132 PHE B CZ 2632 N N . ARG B 135 ? 0.3161 0.3438 0.4222 -0.0141 0.0175 0.0587 133 ARG B N 2633 C CA . ARG B 135 ? 0.3483 0.3975 0.4653 -0.0160 0.0134 0.0675 133 ARG B CA 2634 C C . ARG B 135 ? 0.3706 0.4206 0.5066 -0.0271 0.0057 0.0652 133 ARG B C 2635 O O . ARG B 135 ? 0.3653 0.4089 0.4969 -0.0302 0.0009 0.0538 133 ARG B O 2636 C CB . ARG B 135 ? 0.3529 0.4131 0.4555 -0.0090 0.0123 0.0670 133 ARG B CB 2637 C CG . ARG B 135 ? 0.3656 0.4510 0.4796 -0.0096 0.0084 0.0756 133 ARG B CG 2638 C CD . ARG B 135 ? 0.4320 0.5267 0.5341 -0.0033 0.0054 0.0740 133 ARG B CD 2639 N NE . ARG B 135 ? 0.6767 0.7647 0.7709 -0.0077 -0.0003 0.0649 133 ARG B NE 2640 C CZ . ARG B 135 ? 0.8086 0.8823 0.8846 -0.0043 0.0014 0.0579 133 ARG B CZ 2641 N NH1 . ARG B 135 ? 0.7329 0.7949 0.7980 0.0032 0.0083 0.0593 133 ARG B NH1 2642 N NH2 . ARG B 135 ? 0.8908 0.9641 0.9597 -0.0088 -0.0039 0.0494 133 ARG B NH2 2643 N N . ASN B 136 ? 0.3572 0.3811 0.7242 -0.0132 0.0049 0.0654 134 ASN B N 2644 C CA . ASN B 136 ? 0.4221 0.4448 0.8231 -0.0177 0.0013 0.0657 134 ASN B CA 2645 C C . ASN B 136 ? 0.3991 0.4108 0.8041 -0.0208 -0.0032 0.0524 134 ASN B C 2646 O O . ASN B 136 ? 0.3623 0.3702 0.7835 -0.0242 -0.0105 0.0432 134 ASN B O 2647 C CB . ASN B 136 ? 0.4275 0.4540 0.8426 -0.0205 -0.0049 0.0633 134 ASN B CB 2648 C CG . ASN B 136 ? 0.4462 0.4853 0.8636 -0.0174 -0.0006 0.0772 134 ASN B CG 2649 O OD1 . ASN B 136 ? 0.4763 0.5214 0.8969 -0.0137 0.0063 0.0912 134 ASN B OD1 2650 N ND2 . ASN B 136 ? 0.4747 0.5170 0.8856 -0.0174 -0.0051 0.0726 134 ASN B ND2 2651 N N . GLY B 137 ? 0.4315 0.4388 0.8197 -0.0187 0.0008 0.0506 135 GLY B N 2652 C CA . GLY B 137 ? 0.4038 0.4023 0.7962 -0.0207 -0.0026 0.0389 135 GLY B CA 2653 C C . GLY B 137 ? 0.4021 0.3953 0.7723 -0.0216 -0.0084 0.0213 135 GLY B C 2654 O O . GLY B 137 ? 0.4301 0.4173 0.8010 -0.0226 -0.0113 0.0101 135 GLY B O 2655 N N . GLN B 138 ? 0.4466 0.4427 0.7971 -0.0210 -0.0100 0.0190 136 GLN B N 2656 C CA . GLN B 138 ? 0.4065 0.3993 0.7344 -0.0217 -0.0152 0.0040 136 GLN B CA 2657 C C . GLN B 138 ? 0.2939 0.2868 0.5885 -0.0188 -0.0106 0.0060 136 GLN B C 2658 O O . GLN B 138 ? 0.3193 0.3163 0.6051 -0.0163 -0.0064 0.0163 136 GLN B O 2659 C CB . GLN B 138 ? 0.5541 0.5496 0.8851 -0.0234 -0.0220 -0.0011 136 GLN B CB 2660 C CG . GLN B 138 ? 0.6988 0.6948 1.0639 -0.0266 -0.0274 -0.0028 136 GLN B CG 2661 C CD . GLN B 138 ? 0.8109 0.8010 1.1871 -0.0286 -0.0333 -0.0172 136 GLN B CD 2662 O OE1 . GLN B 138 ? 0.8534 0.8409 1.2091 -0.0279 -0.0350 -0.0288 136 GLN B OE1 2663 N NE2 . GLN B 138 ? 0.8139 0.8025 1.2237 -0.0311 -0.0366 -0.0166 136 GLN B NE2 2664 N N . GLU B 139 ? 0.2808 0.2698 0.5576 -0.0191 -0.0114 -0.0041 137 GLU B N 2665 C CA . GLU B 139 ? 0.2952 0.2840 0.5419 -0.0170 -0.0074 -0.0022 137 GLU B CA 2666 C C . GLU B 139 ? 0.2759 0.2665 0.5049 -0.0168 -0.0106 -0.0031 137 GLU B C 2667 O O . GLU B 139 ? 0.2329 0.2236 0.4620 -0.0188 -0.0172 -0.0122 137 GLU B O 2668 C CB . GLU B 139 ? 0.2791 0.2647 0.5109 -0.0176 -0.0078 -0.0125 137 GLU B CB 2669 C CG . GLU B 139 ? 0.2890 0.2745 0.4916 -0.0160 -0.0036 -0.0092 137 GLU B CG 2670 C CD . GLU B 139 ? 0.3855 0.3696 0.5740 -0.0167 -0.0032 -0.0178 137 GLU B CD 2671 O OE1 . GLU B 139 ? 0.4219 0.4053 0.6229 -0.0178 -0.0059 -0.0268 137 GLU B OE1 2672 O OE2 . GLU B 139 ? 0.4397 0.4236 0.6053 -0.0160 -0.0004 -0.0156 137 GLU B OE2 2673 N N . GLU B 140 ? 0.2495 0.2416 0.4633 -0.0139 -0.0062 0.0062 138 GLU B N 2674 C CA . GLU B 140 ? 0.2760 0.2687 0.4713 -0.0131 -0.0091 0.0059 138 GLU B CA 2675 C C . GLU B 140 ? 0.2520 0.2412 0.4184 -0.0129 -0.0083 0.0027 138 GLU B C 2676 O O . GLU B 140 ? 0.2050 0.1935 0.3621 -0.0107 -0.0029 0.0088 138 GLU B O 2677 C CB . GLU B 140 ? 0.3043 0.3017 0.5039 -0.0096 -0.0058 0.0181 138 GLU B CB 2678 C CG . GLU B 140 ? 0.4063 0.4042 0.5893 -0.0081 -0.0093 0.0181 138 GLU B CG 2679 C CD . GLU B 140 ? 0.5114 0.5095 0.6990 -0.0110 -0.0169 0.0094 138 GLU B CD 2680 O OE1 . GLU B 140 ? 0.6008 0.6029 0.8116 -0.0119 -0.0187 0.0106 138 GLU B OE1 2681 O OE2 . GLU B 140 ? 0.4835 0.4784 0.6520 -0.0124 -0.0211 0.0017 138 GLU B OE2 2682 N N . LYS B 141 ? 0.2454 0.2333 0.3985 -0.0153 -0.0138 -0.0069 139 LYS B N 2683 C CA . LYS B 141 ? 0.3023 0.2877 0.4291 -0.0159 -0.0136 -0.0098 139 LYS B CA 2684 C C . LYS B 141 ? 0.3766 0.3608 0.4842 -0.0150 -0.0163 -0.0071 139 LYS B C 2685 O O . LYS B 141 ? 0.3840 0.3656 0.4704 -0.0154 -0.0160 -0.0071 139 LYS B O 2686 C CB . LYS B 141 ? 0.3683 0.3543 0.4914 -0.0189 -0.0173 -0.0219 139 LYS B CB 2687 C CG . LYS B 141 ? 0.4239 0.4100 0.5600 -0.0193 -0.0143 -0.0255 139 LYS B CG 2688 C CD . LYS B 141 ? 0.5310 0.5191 0.6606 -0.0214 -0.0181 -0.0383 139 LYS B CD 2689 C CE . LYS B 141 ? 0.5155 0.5035 0.6573 -0.0212 -0.0153 -0.0423 139 LYS B CE 2690 N NZ . LYS B 141 ? 0.4730 0.4647 0.6117 -0.0223 -0.0196 -0.0561 139 LYS B NZ 2691 N N . THR B 142 ? 0.3545 0.3406 0.4701 -0.0137 -0.0194 -0.0046 140 THR B N 2692 C CA . THR B 142 ? 0.3085 0.2931 0.4071 -0.0123 -0.0225 -0.0019 140 THR B CA 2693 C C . THR B 142 ? 0.2191 0.2035 0.3160 -0.0078 -0.0181 0.0085 140 THR B C 2694 O O . THR B 142 ? 0.3182 0.3062 0.4322 -0.0057 -0.0139 0.0142 140 THR B O 2695 C CB . THR B 142 ? 0.2974 0.2849 0.4033 -0.0127 -0.0288 -0.0053 140 THR B CB 2696 O OG1 . THR B 142 ? 0.5061 0.4976 0.6340 -0.0106 -0.0272 0.0002 140 THR B OG1 2697 C CG2 . THR B 142 ? 0.2197 0.2090 0.3300 -0.0163 -0.0335 -0.0165 140 THR B CG2 2698 N N . GLY B 143 ? 0.2468 0.2276 0.3236 -0.0062 -0.0195 0.0109 141 GLY B N 2699 C CA . GLY B 143 ? 0.1851 0.1662 0.2590 -0.0011 -0.0165 0.0192 141 GLY B CA 2700 C C . GLY B 143 ? 0.2567 0.2379 0.3306 0.0007 -0.0098 0.0237 141 GLY B C 2701 O O . GLY B 143 ? 0.2821 0.2671 0.3619 0.0056 -0.0060 0.0308 141 GLY B O 2702 N N . VAL B 144 ? 0.2414 0.2198 0.3088 -0.0027 -0.0083 0.0197 142 VAL B N 2703 C CA . VAL B 144 ? 0.2721 0.2507 0.3387 -0.0010 -0.0022 0.0235 142 VAL B CA 2704 C C . VAL B 144 ? 0.2106 0.1839 0.2546 -0.0010 -0.0027 0.0236 142 VAL B C 2705 O O . VAL B 144 ? 0.2721 0.2418 0.3031 -0.0052 -0.0060 0.0185 142 VAL B O 2706 C CB . VAL B 144 ? 0.2383 0.2181 0.3156 -0.0044 0.0005 0.0193 142 VAL B CB 2707 C CG1 . VAL B 144 ? 0.1836 0.1636 0.2581 -0.0027 0.0064 0.0230 142 VAL B CG1 2708 C CG2 . VAL B 144 ? 0.2137 0.1979 0.3160 -0.0045 0.0007 0.0197 142 VAL B CG2 2709 N N . VAL B 145 ? 0.2071 0.1809 0.2472 0.0038 0.0004 0.0296 143 VAL B N 2710 C CA . VAL B 145 ? 0.3387 0.3073 0.3595 0.0041 -0.0004 0.0300 143 VAL B CA 2711 C C . VAL B 145 ? 0.3056 0.2769 0.3282 0.0073 0.0057 0.0338 143 VAL B C 2712 O O . VAL B 145 ? 0.2194 0.1970 0.2561 0.0113 0.0100 0.0385 143 VAL B O 2713 C CB . VAL B 145 ? 0.2463 0.2115 0.2568 0.0078 -0.0050 0.0321 143 VAL B CB 2714 C CG1 . VAL B 145 ? 0.2985 0.2698 0.3182 0.0152 -0.0020 0.0380 143 VAL B CG1 2715 C CG2 . VAL B 145 ? 0.2662 0.2242 0.2573 0.0067 -0.0077 0.0314 143 VAL B CG2 2716 N N . SER B 146 ? 0.2230 0.1904 0.2318 0.0054 0.0059 0.0323 144 SER B N 2717 C CA . SER B 146 ? 0.2427 0.2129 0.2522 0.0082 0.0113 0.0353 144 SER B CA 2718 C C . SER B 146 ? 0.2937 0.2593 0.2863 0.0095 0.0097 0.0357 144 SER B C 2719 O O . SER B 146 ? 0.2512 0.2103 0.2307 0.0065 0.0044 0.0334 144 SER B O 2720 C CB . SER B 146 ? 0.1706 0.1426 0.1860 0.0039 0.0147 0.0321 144 SER B CB 2721 O OG . SER B 146 ? 0.1670 0.1417 0.1822 0.0065 0.0197 0.0349 144 SER B OG 2722 N N . THR B 147 ? 0.2631 0.2326 0.2570 0.0140 0.0140 0.0390 145 THR B N 2723 C CA . THR B 147 ? 0.3018 0.2677 0.2815 0.0150 0.0128 0.0386 145 THR B CA 2724 C C . THR B 147 ? 0.3059 0.2686 0.2784 0.0081 0.0129 0.0349 145 THR B C 2725 O O . THR B 147 ? 0.2785 0.2367 0.2384 0.0064 0.0104 0.0338 145 THR B O 2726 C CB . THR B 147 ? 0.1726 0.1452 0.1562 0.0222 0.0175 0.0427 145 THR B CB 2727 O OG1 . THR B 147 ? 0.2763 0.2555 0.2727 0.0217 0.0237 0.0445 145 THR B OG1 2728 C CG2 . THR B 147 ? 0.2224 0.1999 0.2111 0.0298 0.0172 0.0465 145 THR B CG2 2729 N N . GLY B 148 ? 0.1749 0.1407 0.1563 0.0042 0.0157 0.0328 146 GLY B N 2730 C CA . GLY B 148 ? 0.1750 0.1411 0.1519 -0.0009 0.0173 0.0294 146 GLY B CA 2731 C C . GLY B 148 ? 0.2365 0.2076 0.2184 0.0026 0.0230 0.0318 146 GLY B C 2732 O O . GLY B 148 ? 0.1945 0.1696 0.1844 0.0088 0.0259 0.0362 146 GLY B O 2733 N N . LEU B 149 ? 0.1809 0.1529 0.1583 -0.0011 0.0247 0.0291 147 LEU B N 2734 C CA . LEU B 149 ? 0.1824 0.1596 0.1644 0.0022 0.0300 0.0311 147 LEU B CA 2735 C C . LEU B 149 ? 0.2471 0.2230 0.2184 0.0055 0.0289 0.0333 147 LEU B C 2736 O O . LEU B 149 ? 0.2329 0.2042 0.1914 0.0017 0.0251 0.0312 147 LEU B O 2737 C CB . LEU B 149 ? 0.1958 0.1755 0.1778 -0.0026 0.0321 0.0269 147 LEU B CB 2738 C CG . LEU B 149 ? 0.3037 0.2890 0.2914 0.0008 0.0375 0.0288 147 LEU B CG 2739 C CD1 . LEU B 149 ? 0.2294 0.2188 0.2347 0.0058 0.0415 0.0327 147 LEU B CD1 2740 C CD2 . LEU B 149 ? 0.3795 0.3674 0.3651 -0.0039 0.0390 0.0239 147 LEU B CD2 2741 N N . ILE B 150 ? 0.2705 0.2513 0.2478 0.0127 0.0321 0.0376 148 ILE B N 2742 C CA . ILE B 150 ? 0.2383 0.2193 0.2065 0.0172 0.0309 0.0389 148 ILE B CA 2743 C C . ILE B 150 ? 0.1887 0.1760 0.1588 0.0198 0.0356 0.0400 148 ILE B C 2744 O O . ILE B 150 ? 0.1657 0.1602 0.1477 0.0238 0.0409 0.0436 148 ILE B O 2745 C CB . ILE B 150 ? 0.2434 0.2268 0.2144 0.0250 0.0302 0.0426 148 ILE B CB 2746 C CG1 . ILE B 150 ? 0.2186 0.1957 0.1873 0.0229 0.0250 0.0414 148 ILE B CG1 2747 C CG2 . ILE B 150 ? 0.2170 0.2014 0.1787 0.0306 0.0285 0.0426 148 ILE B CG2 2748 C CD1 . ILE B 150 ? 0.3633 0.3443 0.3367 0.0306 0.0247 0.0450 148 ILE B CD1 2749 N N . GLN B 151 ? 0.1648 0.1498 0.1239 0.0173 0.0335 0.0373 149 GLN B N 2750 C CA . GLN B 151 ? 0.2547 0.2460 0.2141 0.0203 0.0372 0.0380 149 GLN B CA 2751 C C . GLN B 151 ? 0.2466 0.2419 0.2039 0.0292 0.0369 0.0406 149 GLN B C 2752 O O . GLN B 151 ? 0.3082 0.2986 0.2573 0.0308 0.0316 0.0391 149 GLN B O 2753 C CB . GLN B 151 ? 0.2771 0.2651 0.2264 0.0137 0.0348 0.0340 149 GLN B CB 2754 C CG . GLN B 151 ? 0.5112 0.5057 0.4647 0.0124 0.0398 0.0333 149 GLN B CG 2755 C CD . GLN B 151 ? 0.5866 0.5789 0.5318 0.0043 0.0376 0.0295 149 GLN B CD 2756 O OE1 . GLN B 151 ? 0.5715 0.5574 0.5070 0.0000 0.0322 0.0281 149 GLN B OE1 2757 N NE2 . GLN B 151 ? 0.6625 0.6606 0.6121 0.0023 0.0417 0.0280 149 GLN B NE2 2758 N N . ASN B 152 ? 0.2089 0.2139 0.1739 0.0354 0.0424 0.0443 150 ASN B N 2759 C CA . ASN B 152 ? 0.1587 0.1703 0.1216 0.0448 0.0425 0.0467 150 ASN B CA 2760 C C . ASN B 152 ? 0.1762 0.1897 0.1304 0.0461 0.0412 0.0437 150 ASN B C 2761 O O . ASN B 152 ? 0.1828 0.2011 0.1327 0.0537 0.0399 0.0437 150 ASN B O 2762 C CB . ASN B 152 ? 0.2631 0.2859 0.2392 0.0517 0.0491 0.0537 150 ASN B CB 2763 C CG . ASN B 152 ? 0.3081 0.3304 0.2935 0.0518 0.0496 0.0572 150 ASN B CG 2764 O OD1 . ASN B 152 ? 0.3002 0.3171 0.2803 0.0517 0.0449 0.0552 150 ASN B OD1 2765 N ND2 . ASN B 152 ? 0.2011 0.2289 0.2014 0.0521 0.0550 0.0625 150 ASN B ND2 2766 N N . GLY B 153 ? 0.1792 0.1897 0.1311 0.0389 0.0415 0.0408 151 GLY B N 2767 C CA . GLY B 153 ? 0.1662 0.1779 0.1104 0.0385 0.0398 0.0376 151 GLY B CA 2768 C C . GLY B 153 ? 0.1935 0.2167 0.1436 0.0440 0.0457 0.0403 151 GLY B C 2769 O O . GLY B 153 ? 0.2025 0.2286 0.1475 0.0444 0.0449 0.0378 151 GLY B O 2770 N N . ASP B 154 ? 0.2025 0.2323 0.1640 0.0482 0.0514 0.0459 152 ASP B N 2771 C CA . ASP B 154 ? 0.2048 0.2461 0.1730 0.0545 0.0571 0.0501 152 ASP B CA 2772 C C . ASP B 154 ? 0.2011 0.2443 0.1819 0.0513 0.0625 0.0531 152 ASP B C 2773 O O . ASP B 154 ? 0.2376 0.2884 0.2291 0.0565 0.0662 0.0587 152 ASP B O 2774 C CB . ASP B 154 ? 0.2378 0.2885 0.2092 0.0650 0.0589 0.0556 152 ASP B CB 2775 C CG . ASP B 154 ? 0.2442 0.2945 0.2258 0.0656 0.0609 0.0608 152 ASP B CG 2776 O OD1 . ASP B 154 ? 0.2457 0.2871 0.2305 0.0578 0.0598 0.0589 152 ASP B OD1 2777 O OD2 . ASP B 154 ? 0.3284 0.3878 0.3152 0.0735 0.0630 0.0666 152 ASP B OD2 2778 N N . TRP B 155 ? 0.1440 0.1793 0.1243 0.0424 0.0610 0.0487 153 TRP B N 2779 C CA . TRP B 155 ? 0.2279 0.2635 0.2198 0.0389 0.0649 0.0494 153 TRP B CA 2780 C C . TRP B 155 ? 0.2454 0.2810 0.2506 0.0408 0.0671 0.0545 153 TRP B C 2781 O O . TRP B 155 ? 0.2078 0.2463 0.2265 0.0413 0.0711 0.0575 153 TRP B O 2782 C CB . TRP B 155 ? 0.2171 0.2611 0.2140 0.0422 0.0694 0.0512 153 TRP B CB 2783 C CG . TRP B 155 ? 0.1909 0.2348 0.1775 0.0383 0.0675 0.0455 153 TRP B CG 2784 C CD1 . TRP B 155 ? 0.1584 0.2039 0.1336 0.0401 0.0645 0.0434 153 TRP B CD1 2785 C CD2 . TRP B 155 ? 0.2029 0.2458 0.1903 0.0319 0.0682 0.0409 153 TRP B CD2 2786 N NE1 . TRP B 155 ? 0.1929 0.2384 0.1625 0.0347 0.0634 0.0385 153 TRP B NE1 2787 C CE2 . TRP B 155 ? 0.1746 0.2192 0.1511 0.0297 0.0659 0.0370 153 TRP B CE2 2788 C CE3 . TRP B 155 ? 0.1544 0.1958 0.1513 0.0282 0.0702 0.0392 153 TRP B CE3 2789 C CZ2 . TRP B 155 ? 0.1859 0.2317 0.1604 0.0238 0.0662 0.0323 153 TRP B CZ2 2790 C CZ3 . TRP B 155 ? 0.1656 0.2083 0.1598 0.0230 0.0703 0.0337 153 TRP B CZ3 2791 C CH2 . TRP B 155 ? 0.2002 0.2456 0.1832 0.0208 0.0686 0.0307 153 TRP B CH2 2792 N N . THR B 156 ? 0.1401 0.1724 0.1423 0.0419 0.0642 0.0555 154 THR B N 2793 C CA . THR B 156 ? 0.1737 0.2049 0.1882 0.0420 0.0652 0.0593 154 THR B CA 2794 C C . THR B 156 ? 0.2277 0.2498 0.2347 0.0370 0.0597 0.0548 154 THR B C 2795 O O . THR B 156 ? 0.1683 0.1864 0.1613 0.0361 0.0554 0.0511 154 THR B O 2796 C CB . THR B 156 ? 0.1834 0.2239 0.2057 0.0508 0.0684 0.0680 154 THR B CB 2797 O OG1 . THR B 156 ? 0.1966 0.2379 0.2070 0.0550 0.0650 0.0671 154 THR B OG1 2798 C CG2 . THR B 156 ? 0.1416 0.1915 0.1702 0.0562 0.0728 0.0730 154 THR B CG2 2799 N N . PHE B 157 ? 0.1412 0.1600 0.1581 0.0340 0.0596 0.0553 155 PHE B N 2800 C CA . PHE B 157 ? 0.1445 0.1557 0.1557 0.0299 0.0545 0.0518 155 PHE B CA 2801 C C . PHE B 157 ? 0.1652 0.1791 0.1861 0.0341 0.0550 0.0573 155 PHE B C 2802 O O . PHE B 157 ? 0.1460 0.1675 0.1802 0.0388 0.0596 0.0640 155 PHE B O 2803 C CB . PHE B 157 ? 0.2473 0.2526 0.2606 0.0219 0.0528 0.0460 155 PHE B CB 2804 C CG . PHE B 157 ? 0.2130 0.2162 0.2158 0.0168 0.0517 0.0402 155 PHE B CG 2805 C CD1 . PHE B 157 ? 0.2308 0.2281 0.2189 0.0119 0.0467 0.0360 155 PHE B CD1 2806 C CD2 . PHE B 157 ? 0.2656 0.2732 0.2738 0.0166 0.0555 0.0394 155 PHE B CD2 2807 C CE1 . PHE B 157 ? 0.2456 0.2424 0.2249 0.0068 0.0459 0.0317 155 PHE B CE1 2808 C CE2 . PHE B 157 ? 0.2883 0.2956 0.2873 0.0120 0.0547 0.0342 155 PHE B CE2 2809 C CZ . PHE B 157 ? 0.2902 0.2925 0.2747 0.0069 0.0500 0.0306 155 PHE B CZ 2810 N N . GLN B 158 ? 0.2022 0.2103 0.2170 0.0321 0.0503 0.0549 156 GLN B N 2811 C CA . GLN B 158 ? 0.2672 0.2772 0.2923 0.0344 0.0502 0.0589 156 GLN B CA 2812 C C . GLN B 158 ? 0.2562 0.2575 0.2770 0.0283 0.0448 0.0536 156 GLN B C 2813 O O . GLN B 158 ? 0.1817 0.1761 0.1894 0.0235 0.0409 0.0479 156 GLN B O 2814 C CB . GLN B 158 ? 0.1464 0.1630 0.1686 0.0427 0.0506 0.0639 156 GLN B CB 2815 C CG . GLN B 158 ? 0.1665 0.1775 0.1711 0.0435 0.0449 0.0591 156 GLN B CG 2816 C CD . GLN B 158 ? 0.2583 0.2764 0.2612 0.0526 0.0447 0.0629 156 GLN B CD 2817 O OE1 . GLN B 158 ? 0.2928 0.3137 0.3026 0.0550 0.0444 0.0660 156 GLN B OE1 2818 N NE2 . GLN B 158 ? 0.2077 0.2298 0.2016 0.0581 0.0446 0.0623 156 GLN B NE2 2819 N N . THR B 159 ? 0.2119 0.2144 0.2445 0.0286 0.0446 0.0561 157 THR B N 2820 C CA . THR B 159 ? 0.1519 0.1476 0.1808 0.0242 0.0392 0.0518 157 THR B CA 2821 C C . THR B 159 ? 0.1601 0.1602 0.2013 0.0276 0.0394 0.0567 157 THR B C 2822 O O . THR B 159 ? 0.2428 0.2500 0.3002 0.0304 0.0439 0.0626 157 THR B O 2823 C CB . THR B 159 ? 0.2077 0.1985 0.2391 0.0165 0.0378 0.0456 157 THR B CB 2824 O OG1 . THR B 159 ? 0.2339 0.2191 0.2602 0.0127 0.0323 0.0416 157 THR B OG1 2825 C CG2 . THR B 159 ? 0.2328 0.2277 0.2845 0.0163 0.0416 0.0477 157 THR B CG2 2826 N N . LEU B 160 ? 0.1543 0.1505 0.1882 0.0276 0.0345 0.0549 158 LEU B N 2827 C CA . LEU B 160 ? 0.1543 0.1546 0.1999 0.0301 0.0340 0.0586 158 LEU B CA 2828 C C . LEU B 160 ? 0.1910 0.1850 0.2395 0.0233 0.0297 0.0533 158 LEU B C 2829 O O . LEU B 160 ? 0.1905 0.1768 0.2250 0.0193 0.0249 0.0474 158 LEU B O 2830 C CB . LEU B 160 ? 0.2270 0.2290 0.2635 0.0362 0.0314 0.0604 158 LEU B CB 2831 C CG . LEU B 160 ? 0.3288 0.3372 0.3586 0.0442 0.0338 0.0639 158 LEU B CG 2832 C CD1 . LEU B 160 ? 0.3645 0.3760 0.3901 0.0508 0.0307 0.0652 158 LEU B CD1 2833 C CD2 . LEU B 160 ? 0.3077 0.3272 0.3511 0.0481 0.0410 0.0711 158 LEU B CD2 2834 N N . VAL B 161 ? 0.2386 0.2363 0.3056 0.0222 0.0311 0.0554 159 VAL B N 2835 C CA . VAL B 161 ? 0.1861 0.1791 0.2571 0.0165 0.0266 0.0497 159 VAL B CA 2836 C C . VAL B 161 ? 0.2529 0.2507 0.3358 0.0191 0.0254 0.0539 159 VAL B C 2837 O O . VAL B 161 ? 0.2009 0.2060 0.3022 0.0214 0.0291 0.0602 159 VAL B O 2838 C CB . VAL B 161 ? 0.1964 0.1887 0.2801 0.0118 0.0280 0.0462 159 VAL B CB 2839 C CG1 . VAL B 161 ? 0.2113 0.1997 0.2984 0.0066 0.0227 0.0393 159 VAL B CG1 2840 C CG2 . VAL B 161 ? 0.1543 0.1436 0.2266 0.0098 0.0297 0.0425 159 VAL B CG2 2841 N N . MET B 162 ? 0.2300 0.2238 0.3024 0.0187 0.0200 0.0507 160 MET B N 2842 C CA . MET B 162 ? 0.2420 0.2405 0.3226 0.0218 0.0183 0.0542 160 MET B CA 2843 C C . MET B 162 ? 0.2209 0.2172 0.3103 0.0169 0.0137 0.0495 160 MET B C 2844 O O . MET B 162 ? 0.2568 0.2462 0.3368 0.0118 0.0095 0.0422 160 MET B O 2845 C CB . MET B 162 ? 0.2042 0.2009 0.2679 0.0265 0.0151 0.0544 160 MET B CB 2846 C CG . MET B 162 ? 0.1615 0.1621 0.2185 0.0325 0.0193 0.0586 160 MET B CG 2847 S SD . MET B 162 ? 0.5803 0.5750 0.6145 0.0368 0.0145 0.0559 160 MET B SD 2848 C CE . MET B 162 ? 0.4012 0.3855 0.4208 0.0301 0.0134 0.0501 160 MET B CE 2849 N N . LEU B 163 ? 0.1759 0.1793 0.2836 0.0185 0.0145 0.0541 161 LEU B N 2850 C CA . LEU B 163 ? 0.2347 0.2373 0.3529 0.0145 0.0099 0.0500 161 LEU B CA 2851 C C . LEU B 163 ? 0.1844 0.1911 0.3021 0.0182 0.0069 0.0526 161 LEU B C 2852 O O . LEU B 163 ? 0.1932 0.2089 0.3213 0.0233 0.0103 0.0605 161 LEU B O 2853 C CB . LEU B 163 ? 0.1972 0.2045 0.3410 0.0120 0.0125 0.0523 161 LEU B CB 2854 C CG . LEU B 163 ? 0.2251 0.2328 0.3827 0.0082 0.0073 0.0480 161 LEU B CG 2855 C CD1 . LEU B 163 ? 0.1647 0.1641 0.3100 0.0031 0.0015 0.0367 161 LEU B CD1 2856 C CD2 . LEU B 163 ? 0.2148 0.2272 0.4005 0.0063 0.0096 0.0518 161 LEU B CD2 2857 N N . GLU B 164 ? 0.2027 0.2034 0.3085 0.0161 0.0004 0.0463 162 GLU B N 2858 C CA . GLU B 164 ? 0.2977 0.3018 0.4041 0.0194 -0.0033 0.0479 162 GLU B CA 2859 C C . GLU B 164 ? 0.2792 0.2892 0.4081 0.0168 -0.0045 0.0481 162 GLU B C 2860 O O . GLU B 164 ? 0.3272 0.3334 0.4606 0.0112 -0.0080 0.0415 162 GLU B O 2861 C CB . GLU B 164 ? 0.2246 0.2202 0.3107 0.0181 -0.0101 0.0418 162 GLU B CB 2862 C CG . GLU B 164 ? 0.4575 0.4460 0.5220 0.0196 -0.0101 0.0411 162 GLU B CG 2863 C CD . GLU B 164 ? 0.6100 0.5894 0.6565 0.0163 -0.0169 0.0354 162 GLU B CD 2864 O OE1 . GLU B 164 ? 0.5431 0.5164 0.5784 0.0119 -0.0172 0.0318 162 GLU B OE1 2865 O OE2 . GLU B 164 ? 0.7383 0.7173 0.7820 0.0182 -0.0220 0.0350 162 GLU B OE2 2866 N N . THR B 165 ? 0.2137 0.2340 0.3574 0.0212 -0.0017 0.0559 163 THR B N 2867 C CA . THR B 165 ? 0.1629 0.1902 0.3314 0.0188 -0.0022 0.0579 163 THR B CA 2868 C C . THR B 165 ? 0.1608 0.2003 0.3393 0.0247 -0.0003 0.0664 163 THR B C 2869 O O . THR B 165 ? 0.1594 0.2039 0.3300 0.0311 0.0036 0.0722 163 THR B O 2870 C CB . THR B 165 ? 0.1928 0.2216 0.3801 0.0152 0.0023 0.0604 163 THR B CB 2871 O OG1 . THR B 165 ? 0.2578 0.2916 0.4703 0.0119 0.0005 0.0614 163 THR B OG1 2872 C CG2 . THR B 165 ? 0.1821 0.2184 0.3732 0.0203 0.0100 0.0708 163 THR B CG2 2873 N N . VAL B 166 ? 0.1798 0.2249 0.3758 0.0228 -0.0033 0.0668 164 VAL B N 2874 C CA . VAL B 166 ? 0.1887 0.2478 0.3988 0.0277 -0.0010 0.0756 164 VAL B CA 2875 C C . VAL B 166 ? 0.2470 0.3146 0.4862 0.0247 0.0033 0.0831 164 VAL B C 2876 O O . VAL B 166 ? 0.2340 0.3009 0.4909 0.0190 -0.0004 0.0800 164 VAL B O 2877 C CB . VAL B 166 ? 0.1622 0.2233 0.3727 0.0281 -0.0076 0.0719 164 VAL B CB 2878 C CG1 . VAL B 166 ? 0.1595 0.2370 0.3841 0.0340 -0.0046 0.0815 164 VAL B CG1 2879 C CG2 . VAL B 166 ? 0.1746 0.2257 0.3571 0.0304 -0.0127 0.0646 164 VAL B CG2 2880 N N . PRO B 167 ? 0.2377 0.3134 0.4825 0.0285 0.0107 0.0930 165 PRO B N 2881 C CA . PRO B 167 ? 0.2821 0.3654 0.5550 0.0256 0.0151 0.1017 165 PRO B CA 2882 C C . PRO B 167 ? 0.2712 0.3667 0.5685 0.0248 0.0138 0.1077 165 PRO B C 2883 O O . PRO B 167 ? 0.1458 0.2521 0.4402 0.0304 0.0142 0.1120 165 PRO B O 2884 C CB . PRO B 167 ? 0.3744 0.4666 0.6436 0.0319 0.0232 0.1120 165 PRO B CB 2885 C CG . PRO B 167 ? 0.3200 0.4031 0.5582 0.0357 0.0222 0.1049 165 PRO B CG 2886 C CD . PRO B 167 ? 0.2091 0.2868 0.4344 0.0357 0.0150 0.0964 165 PRO B CD 2887 N N . ARG B 168 ? 0.2218 0.3157 0.5436 0.0178 0.0119 0.1075 166 ARG B N 2888 C CA . ARG B 168 ? 0.3073 0.4130 0.6566 0.0159 0.0108 0.1141 166 ARG B CA 2889 C C . ARG B 168 ? 0.3222 0.4354 0.6948 0.0144 0.0171 0.1272 166 ARG B C 2890 O O . ARG B 168 ? 0.2994 0.4051 0.6731 0.0122 0.0197 0.1275 166 ARG B O 2891 C CB . ARG B 168 ? 0.3199 0.4169 0.6793 0.0087 0.0023 0.1030 166 ARG B CB 2892 C CG . ARG B 168 ? 0.3049 0.3975 0.6442 0.0101 -0.0044 0.0925 166 ARG B CG 2893 C CD . ARG B 168 ? 0.2926 0.3763 0.6401 0.0032 -0.0128 0.0804 166 ARG B CD 2894 N NE . ARG B 168 ? 0.2364 0.3199 0.5719 0.0044 -0.0194 0.0730 166 ARG B NE 2895 C CZ . ARG B 168 ? 0.2258 0.2998 0.5325 0.0062 -0.0229 0.0639 166 ARG B CZ 2896 N NH1 . ARG B 168 ? 0.2620 0.3263 0.5491 0.0066 -0.0204 0.0608 166 ARG B NH1 2897 N NH2 . ARG B 168 ? 0.2173 0.2920 0.5156 0.0074 -0.0291 0.0584 166 ARG B NH2 2898 N N . SER B 169 ? 0.4076 0.5299 0.7883 0.0151 0.0192 0.1365 167 SER B N 2899 C CA . SER B 169 ? 0.4106 0.5342 0.8030 0.0135 0.0243 0.1485 167 SER B CA 2900 C C . SER B 169 ? 0.3547 0.4658 0.7670 0.0063 0.0208 0.1451 167 SER B C 2901 O O . SER B 169 ? 0.3507 0.4567 0.7761 0.0011 0.0138 0.1363 167 SER B O 2902 C CB . SER B 169 ? 0.4534 0.5889 0.8548 0.0147 0.0255 0.1579 167 SER B CB 2903 O OG . SER B 169 ? 0.5482 0.6831 0.9650 0.0101 0.0185 0.1517 167 SER B OG 2904 N N . GLY B 170 ? 0.3717 0.4778 0.7853 0.0065 0.0250 0.1513 168 GLY B N 2905 C CA . GLY B 170 ? 0.4272 0.5212 0.8589 0.0012 0.0216 0.1483 168 GLY B CA 2906 C C . GLY B 170 ? 0.4183 0.5016 0.8417 -0.0003 0.0203 0.1372 168 GLY B C 2907 O O . GLY B 170 ? 0.4080 0.4827 0.8402 -0.0020 0.0202 0.1371 168 GLY B O 2908 N N . GLU B 171 ? 0.3797 0.4644 0.7871 0.0007 0.0189 0.1278 169 GLU B N 2909 C CA . GLU B 171 ? 0.3498 0.4259 0.7486 -0.0011 0.0175 0.1170 169 GLU B CA 2910 C C . GLU B 171 ? 0.3189 0.3929 0.7079 0.0024 0.0244 0.1236 169 GLU B C 2911 O O . GLU B 171 ? 0.3026 0.3845 0.6801 0.0081 0.0305 0.1341 169 GLU B O 2912 C CB . GLU B 171 ? 0.2818 0.3550 0.6529 0.0014 0.0144 0.1063 169 GLU B CB 2913 C CG . GLU B 171 ? 0.3059 0.3745 0.6793 -0.0027 0.0057 0.0949 169 GLU B CG 2914 C CD . GLU B 171 ? 0.3704 0.4336 0.7117 0.0002 0.0024 0.0850 169 GLU B CD 2915 O OE1 . GLU B 171 ? 0.4669 0.5326 0.7871 0.0059 0.0068 0.0890 169 GLU B OE1 2916 O OE2 . GLU B 171 ? 0.4154 0.4721 0.7530 -0.0033 -0.0050 0.0733 169 GLU B OE2 2917 N N . VAL B 172 ? 0.3084 0.3720 0.7010 -0.0010 0.0230 0.1167 170 VAL B N 2918 C CA . VAL B 172 ? 0.3864 0.4477 0.7681 0.0022 0.0288 0.1208 170 VAL B CA 2919 C C . VAL B 172 ? 0.3447 0.3969 0.7050 0.0012 0.0269 0.1073 170 VAL B C 2920 O O . VAL B 172 ? 0.3406 0.3820 0.7024 -0.0036 0.0209 0.0946 170 VAL B O 2921 C CB . VAL B 172 ? 0.3790 0.4334 0.7773 0.0013 0.0288 0.1251 170 VAL B CB 2922 C CG1 . VAL B 172 ? 0.3272 0.3793 0.7139 0.0045 0.0340 0.1274 170 VAL B CG1 2923 C CG2 . VAL B 172 ? 0.4042 0.4652 0.8159 0.0036 0.0303 0.1391 170 VAL B CG2 2924 N N . TYR B 173 ? 0.1418 0.1960 0.4765 0.0067 0.0313 0.1089 171 TYR B N 2925 C CA . TYR B 173 ? 0.2052 0.2483 0.5129 0.0065 0.0294 0.0968 171 TYR B CA 2926 C C . TYR B 173 ? 0.3044 0.3447 0.6107 0.0075 0.0341 0.0992 171 TYR B C 2927 O O . TYR B 173 ? 0.3458 0.3948 0.6612 0.0111 0.0403 0.1119 171 TYR B O 2928 C CB . TYR B 173 ? 0.1424 0.1877 0.4220 0.0115 0.0298 0.0953 171 TYR B CB 2929 C CG . TYR B 173 ? 0.2250 0.2708 0.5014 0.0106 0.0241 0.0903 171 TYR B CG 2930 C CD1 . TYR B 173 ? 0.2275 0.2849 0.5194 0.0125 0.0249 0.0992 171 TYR B CD1 2931 C CD2 . TYR B 173 ? 0.1482 0.1840 0.4060 0.0079 0.0180 0.0772 171 TYR B CD2 2932 C CE1 . TYR B 173 ? 0.2427 0.3010 0.5317 0.0120 0.0195 0.0945 171 TYR B CE1 2933 C CE2 . TYR B 173 ? 0.1672 0.2038 0.4218 0.0074 0.0126 0.0729 171 TYR B CE2 2934 C CZ . TYR B 173 ? 0.2291 0.2765 0.4992 0.0095 0.0132 0.0813 171 TYR B CZ 2935 O OH . TYR B 173 ? 0.2606 0.3091 0.5277 0.0093 0.0076 0.0769 171 TYR B OH 2936 N N . THR B 174 ? 0.1853 0.2145 0.4800 0.0046 0.0311 0.0871 172 THR B N 2937 C CA . THR B 174 ? 0.1772 0.2032 0.4700 0.0054 0.0350 0.0880 172 THR B CA 2938 C C . THR B 174 ? 0.1439 0.1631 0.4068 0.0061 0.0344 0.0781 172 THR B C 2939 O O . THR B 174 ? 0.2029 0.2150 0.4542 0.0028 0.0289 0.0660 172 THR B O 2940 C CB . THR B 174 ? 0.2323 0.2522 0.5492 0.0007 0.0323 0.0841 172 THR B CB 2941 O OG1 . THR B 174 ? 0.2647 0.2908 0.6117 -0.0004 0.0328 0.0946 172 THR B OG1 2942 C CG2 . THR B 174 ? 0.2146 0.2316 0.5298 0.0021 0.0364 0.0852 172 THR B CG2 2943 N N . CYS B 175 ? 0.1413 0.1636 0.3921 0.0104 0.0400 0.0838 173 CYS B N 2944 C CA . CYS B 175 ? 0.2478 0.2640 0.4737 0.0106 0.0398 0.0756 173 CYS B CA 2945 C C . CYS B 175 ? 0.2496 0.2618 0.4835 0.0091 0.0416 0.0734 173 CYS B C 2946 O O . CYS B 175 ? 0.2237 0.2408 0.4726 0.0115 0.0463 0.0831 173 CYS B O 2947 C CB . CYS B 175 ? 0.1821 0.2038 0.3886 0.0165 0.0439 0.0816 173 CYS B CB 2948 S SG . CYS B 175 ? 0.2063 0.2205 0.3840 0.0161 0.0434 0.0721 173 CYS B SG 2949 N N . GLN B 176 ? 0.2424 0.2467 0.4665 0.0055 0.0378 0.0608 174 GLN B N 2950 C CA . GLN B 176 ? 0.2056 0.2062 0.4374 0.0042 0.0387 0.0568 174 GLN B CA 2951 C C . GLN B 176 ? 0.2273 0.2255 0.4347 0.0050 0.0403 0.0511 174 GLN B C 2952 O O . GLN B 176 ? 0.1906 0.1859 0.3778 0.0032 0.0371 0.0432 174 GLN B O 2953 C CB . GLN B 176 ? 0.2004 0.1952 0.4461 -0.0005 0.0326 0.0460 174 GLN B CB 2954 C CG . GLN B 176 ? 0.3028 0.2937 0.5579 -0.0013 0.0328 0.0406 174 GLN B CG 2955 C CD . GLN B 176 ? 0.3383 0.3237 0.6004 -0.0052 0.0259 0.0264 174 GLN B CD 2956 O OE1 . GLN B 176 ? 0.4848 0.4682 0.7277 -0.0067 0.0230 0.0153 174 GLN B OE1 2957 N NE2 . GLN B 176 ? 0.2243 0.2080 0.5144 -0.0068 0.0230 0.0269 174 GLN B NE2 2958 N N . VAL B 177 ? 0.1441 0.1441 0.3543 0.0075 0.0449 0.0555 175 VAL B N 2959 C CA . VAL B 177 ? 0.1759 0.1751 0.3642 0.0085 0.0469 0.0516 175 VAL B CA 2960 C C . VAL B 177 ? 0.2229 0.2193 0.4183 0.0074 0.0472 0.0456 175 VAL B C 2961 O O . VAL B 177 ? 0.2071 0.2046 0.4226 0.0089 0.0496 0.0513 175 VAL B O 2962 C CB . VAL B 177 ? 0.2324 0.2381 0.4123 0.0140 0.0525 0.0624 175 VAL B CB 2963 C CG1 . VAL B 177 ? 0.1394 0.1443 0.2993 0.0147 0.0542 0.0579 175 VAL B CG1 2964 C CG2 . VAL B 177 ? 0.1389 0.1479 0.3097 0.0160 0.0518 0.0668 175 VAL B CG2 2965 N N . GLU B 178 ? 0.1587 0.1518 0.3376 0.0048 0.0447 0.0344 176 GLU B N 2966 C CA . GLU B 178 ? 0.1492 0.1409 0.3312 0.0043 0.0451 0.0276 176 GLU B CA 2967 C C . GLU B 178 ? 0.2568 0.2508 0.4168 0.0055 0.0482 0.0270 176 GLU B C 2968 O O . GLU B 178 ? 0.3307 0.3247 0.4701 0.0043 0.0472 0.0254 176 GLU B O 2969 C CB . GLU B 178 ? 0.2500 0.2380 0.4337 0.0003 0.0393 0.0139 176 GLU B CB 2970 C CG . GLU B 178 ? 0.4024 0.3877 0.6115 -0.0009 0.0354 0.0127 176 GLU B CG 2971 C CD . GLU B 178 ? 0.5592 0.5423 0.7657 -0.0045 0.0288 -0.0009 176 GLU B CD 2972 O OE1 . GLU B 178 ? 0.5970 0.5778 0.8193 -0.0051 0.0254 -0.0092 176 GLU B OE1 2973 O OE2 . GLU B 178 ? 0.5734 0.5571 0.7621 -0.0063 0.0266 -0.0036 176 GLU B OE2 2974 N N . HIS B 179 ? 0.1942 0.1900 0.3594 0.0078 0.0517 0.0285 177 HIS B N 2975 C CA . HIS B 179 ? 0.2272 0.2262 0.3745 0.0096 0.0552 0.0297 177 HIS B CA 2976 C C . HIS B 179 ? 0.2565 0.2567 0.4128 0.0112 0.0574 0.0273 177 HIS B C 2977 O O . HIS B 179 ? 0.2645 0.2635 0.4430 0.0127 0.0577 0.0301 177 HIS B O 2978 C CB . HIS B 179 ? 0.2449 0.2480 0.3878 0.0137 0.0590 0.0417 177 HIS B CB 2979 C CG . HIS B 179 ? 0.2011 0.2075 0.3250 0.0157 0.0617 0.0427 177 HIS B CG 2980 N ND1 . HIS B 179 ? 0.2269 0.2380 0.3547 0.0198 0.0663 0.0482 177 HIS B ND1 2981 C CD2 . HIS B 179 ? 0.1398 0.1455 0.2416 0.0139 0.0601 0.0388 177 HIS B CD2 2982 C CE1 . HIS B 179 ? 0.2319 0.2453 0.3406 0.0206 0.0673 0.0471 177 HIS B CE1 2983 N NE2 . HIS B 179 ? 0.1964 0.2063 0.2896 0.0168 0.0635 0.0416 177 HIS B NE2 2984 N N . PRO B 180 ? 0.2746 0.2771 0.4148 0.0109 0.0586 0.0224 178 PRO B N 2985 C CA . PRO B 180 ? 0.1938 0.1982 0.3415 0.0128 0.0605 0.0193 178 PRO B CA 2986 C C . PRO B 180 ? 0.2256 0.2323 0.3886 0.0178 0.0649 0.0304 178 PRO B C 2987 O O . PRO B 180 ? 0.2359 0.2424 0.4127 0.0196 0.0657 0.0289 178 PRO B O 2988 C CB . PRO B 180 ? 0.2202 0.2283 0.3452 0.0116 0.0616 0.0148 178 PRO B CB 2989 C CG . PRO B 180 ? 0.2851 0.2914 0.3937 0.0074 0.0582 0.0108 178 PRO B CG 2990 C CD . PRO B 180 ? 0.2922 0.2956 0.4076 0.0082 0.0574 0.0183 178 PRO B CD 2991 N N . SER B 181 ? 0.2678 0.2773 0.4285 0.0204 0.0677 0.0415 179 SER B N 2992 C CA . SER B 181 ? 0.2407 0.2545 0.4146 0.0256 0.0722 0.0536 179 SER B CA 2993 C C . SER B 181 ? 0.2124 0.2237 0.4131 0.0259 0.0715 0.0593 179 SER B C 2994 O O . SER B 181 ? 0.1689 0.1835 0.3852 0.0297 0.0748 0.0695 179 SER B O 2995 C CB . SER B 181 ? 0.2284 0.2481 0.3896 0.0291 0.0753 0.0629 179 SER B CB 2996 O OG . SER B 181 ? 0.2554 0.2739 0.4183 0.0279 0.0734 0.0660 179 SER B OG 2997 N N . LEU B 182 ? 0.2190 0.2249 0.4254 0.0218 0.0669 0.0534 180 LEU B N 2998 C CA . LEU B 182 ? 0.2366 0.2399 0.4692 0.0212 0.0652 0.0584 180 LEU B CA 2999 C C . LEU B 182 ? 0.1770 0.1737 0.4254 0.0189 0.0609 0.0479 180 LEU B C 3000 O O . LEU B 182 ? 0.2256 0.2200 0.4622 0.0165 0.0578 0.0346 180 LEU B O 3001 C CB . LEU B 182 ? 0.1612 0.1636 0.3921 0.0186 0.0626 0.0595 180 LEU B CB 3002 C CG . LEU B 182 ? 0.1635 0.1722 0.3790 0.0212 0.0658 0.0683 180 LEU B CG 3003 C CD1 . LEU B 182 ? 0.1393 0.1461 0.3524 0.0184 0.0621 0.0665 180 LEU B CD1 3004 C CD2 . LEU B 182 ? 0.1365 0.1527 0.3647 0.0264 0.0712 0.0841 180 LEU B CD2 3005 N N . THR B 183 ? 0.1822 0.1766 0.4581 0.0198 0.0605 0.0540 181 THR B N 3006 C CA . THR B 183 ? 0.1671 0.1548 0.4614 0.0182 0.0556 0.0440 181 THR B CA 3007 C C . THR B 183 ? 0.1598 0.1425 0.4693 0.0143 0.0499 0.0401 181 THR B C 3008 O O . THR B 183 ? 0.2799 0.2567 0.6026 0.0126 0.0443 0.0290 181 THR B O 3009 C CB . THR B 183 ? 0.2512 0.2381 0.5686 0.0217 0.0576 0.0521 181 THR B CB 3010 O OG1 . THR B 183 ? 0.2093 0.2003 0.5404 0.0225 0.0608 0.0692 181 THR B OG1 3011 C CG2 . THR B 183 ? 0.3133 0.3045 0.6161 0.0255 0.0619 0.0520 181 THR B CG2 3012 N N . SER B 184 ? 0.2020 0.1876 0.5092 0.0133 0.0511 0.0488 182 SER B N 3013 C CA . SER B 184 ? 0.2460 0.2283 0.5648 0.0095 0.0459 0.0457 182 SER B CA 3014 C C . SER B 184 ? 0.2669 0.2543 0.5684 0.0091 0.0478 0.0515 182 SER B C 3015 O O . SER B 184 ? 0.2047 0.1981 0.4928 0.0123 0.0534 0.0609 182 SER B O 3016 C CB . SER B 184 ? 0.1821 0.1619 0.5353 0.0092 0.0446 0.0548 182 SER B CB 3017 O OG . SER B 184 ? 0.2987 0.2884 0.6547 0.0114 0.0503 0.0722 182 SER B OG 3018 N N . PRO B 185 ? 0.2619 0.2470 0.5633 0.0056 0.0429 0.0454 183 PRO B N 3019 C CA . PRO B 185 ? 0.2794 0.2690 0.5634 0.0056 0.0443 0.0500 183 PRO B CA 3020 C C . PRO B 185 ? 0.2785 0.2752 0.5713 0.0087 0.0496 0.0675 183 PRO B C 3021 O O . PRO B 185 ? 0.3569 0.3546 0.6760 0.0088 0.0501 0.0764 183 PRO B O 3022 C CB . PRO B 185 ? 0.2816 0.2675 0.5713 0.0014 0.0376 0.0413 183 PRO B CB 3023 C CG . PRO B 185 ? 0.3208 0.3007 0.6178 -0.0005 0.0326 0.0271 183 PRO B CG 3024 C CD . PRO B 185 ? 0.3100 0.2889 0.6243 0.0020 0.0355 0.0325 183 PRO B CD 3025 N N . LEU B 186 ? 0.2375 0.2398 0.5086 0.0114 0.0532 0.0723 184 LEU B N 3026 C CA . LEU B 186 ? 0.2333 0.2445 0.5088 0.0153 0.0580 0.0877 184 LEU B CA 3027 C C . LEU B 186 ? 0.3567 0.3695 0.6315 0.0136 0.0551 0.0880 184 LEU B C 3028 O O . LEU B 186 ? 0.3133 0.3233 0.5675 0.0122 0.0521 0.0792 184 LEU B O 3029 C CB . LEU B 186 ? 0.2479 0.2649 0.5010 0.0201 0.0632 0.0919 184 LEU B CB 3030 C CG . LEU B 186 ? 0.3367 0.3652 0.5881 0.0259 0.0688 0.1065 184 LEU B CG 3031 C CD1 . LEU B 186 ? 0.3541 0.3861 0.5844 0.0303 0.0725 0.1066 184 LEU B CD1 3032 C CD2 . LEU B 186 ? 0.3829 0.4156 0.6281 0.0265 0.0675 0.1088 184 LEU B CD2 3033 N N . THR B 187 ? 0.2130 0.2308 0.5108 0.0137 0.0558 0.0986 185 THR B N 3034 C CA . THR B 187 ? 0.2371 0.2574 0.5369 0.0122 0.0530 0.0995 185 THR B CA 3035 C C . THR B 187 ? 0.2392 0.2722 0.5420 0.0171 0.0583 0.1150 185 THR B C 3036 O O . THR B 187 ? 0.1837 0.2214 0.4931 0.0222 0.0606 0.1245 185 THR B O 3037 C CB . THR B 187 ? 0.2908 0.3062 0.6173 0.0070 0.0476 0.0962 185 THR B CB 3038 O OG1 . THR B 187 ? 0.3513 0.3712 0.6997 0.0096 0.0486 0.1049 185 THR B OG1 3039 C CG2 . THR B 187 ? 0.1747 0.1790 0.4964 0.0030 0.0416 0.0789 185 THR B CG2 3040 N N . VAL B 188 ? 0.2658 0.3025 0.5548 0.0183 0.0572 0.1142 186 VAL B N 3041 C CA . VAL B 188 ? 0.1814 0.2295 0.4700 0.0235 0.0605 0.1266 186 VAL B CA 3042 C C . VAL B 188 ? 0.2658 0.3164 0.5640 0.0208 0.0569 0.1259 186 VAL B C 3043 O O . VAL B 188 ? 0.2786 0.3229 0.5633 0.0183 0.0521 0.1146 186 VAL B O 3044 C CB . VAL B 188 ? 0.1765 0.2307 0.4388 0.0294 0.0642 0.1276 186 VAL B CB 3045 C CG1 . VAL B 188 ? 0.1767 0.2395 0.4326 0.0339 0.0655 0.1373 186 VAL B CG1 3046 C CG2 . VAL B 188 ? 0.1455 0.1980 0.3979 0.0324 0.0676 0.1296 186 VAL B CG2 3047 N N . GLU B 189 ? 0.2400 0.2941 0.5514 0.0222 0.0565 0.1358 187 GLU B N 3048 C CA . GLU B 189 ? 0.2022 0.2592 0.5238 0.0198 0.0530 0.1360 187 GLU B CA 3049 C C . GLU B 189 ? 0.2527 0.3200 0.5590 0.0247 0.0557 0.1424 187 GLU B C 3050 O O . GLU B 189 ? 0.2709 0.3436 0.5633 0.0300 0.0602 0.1502 187 GLU B O 3051 C CB . GLU B 189 ? 0.2297 0.2851 0.5764 0.0181 0.0504 0.1422 187 GLU B CB 3052 C CG . GLU B 189 ? 0.2122 0.2582 0.5765 0.0133 0.0458 0.1331 187 GLU B CG 3053 C CD . GLU B 189 ? 0.3450 0.3913 0.7356 0.0127 0.0426 0.1390 187 GLU B CD 3054 O OE1 . GLU B 189 ? 0.4281 0.4675 0.8350 0.0087 0.0377 0.1306 187 GLU B OE1 3055 O OE2 . GLU B 189 ? 0.4376 0.4913 0.8322 0.0162 0.0448 0.1519 187 GLU B OE2 3056 N N . TRP B 190 ? 0.2437 0.3142 0.5524 0.0231 0.0523 0.1383 188 TRP B N 3057 C CA . TRP B 190 ? 0.1587 0.2393 0.4561 0.0279 0.0537 0.1435 188 TRP B CA 3058 C C . TRP B 190 ? 0.1888 0.2720 0.5039 0.0244 0.0498 0.1448 188 TRP B C 3059 O O . TRP B 190 ? 0.2586 0.3367 0.5848 0.0195 0.0446 0.1357 188 TRP B O 3060 C CB . TRP B 190 ? 0.2801 0.3621 0.5557 0.0321 0.0528 0.1352 188 TRP B CB 3061 C CG . TRP B 190 ? 0.3024 0.3940 0.5654 0.0377 0.0535 0.1391 188 TRP B CG 3062 C CD1 . TRP B 190 ? 0.2966 0.3955 0.5422 0.0439 0.0579 0.1448 188 TRP B CD1 3063 C CD2 . TRP B 190 ? 0.2191 0.3150 0.4868 0.0378 0.0495 0.1372 188 TRP B CD2 3064 N NE1 . TRP B 190 ? 0.3245 0.4319 0.5633 0.0480 0.0569 0.1458 188 TRP B NE1 3065 C CE2 . TRP B 190 ? 0.3428 0.4483 0.5947 0.0444 0.0519 0.1416 188 TRP B CE2 3066 C CE3 . TRP B 190 ? 0.2189 0.3100 0.4995 0.0325 0.0435 0.1307 188 TRP B CE3 3067 C CZ2 . TRP B 190 ? 0.3563 0.4682 0.6077 0.0467 0.0489 0.1407 188 TRP B CZ2 3068 C CZ3 . TRP B 190 ? 0.3055 0.4026 0.5851 0.0345 0.0405 0.1303 188 TRP B CZ3 3069 C CH2 . TRP B 190 ? 0.3157 0.4240 0.5825 0.0421 0.0434 0.1359 188 TRP B CH2 3070 N N . ARG B 191 ? 0.2767 0.3683 0.5944 0.0270 0.0522 0.1558 189 ARG B N 3071 C CA . ARG B 191 ? 0.3489 0.4443 0.6833 0.0243 0.0490 0.1584 189 ARG B CA 3072 C C . ARG B 191 ? 0.3272 0.4340 0.6480 0.0291 0.0498 0.1598 189 ARG B C 3073 O O . ARG B 191 ? 0.3186 0.4327 0.6217 0.0352 0.0543 0.1647 189 ARG B O 3074 C CB . ARG B 191 ? 0.4545 0.5508 0.8071 0.0234 0.0504 0.1708 189 ARG B CB 3075 C CG . ARG B 191 ? 0.6224 0.7125 1.0013 0.0173 0.0447 0.1684 189 ARG B CG 3076 C CD . ARG B 191 ? 0.7618 0.8532 1.1591 0.0180 0.0458 0.1814 189 ARG B CD 3077 N NE . ARG B 191 ? 0.8412 0.9297 1.2344 0.0214 0.0493 0.1864 189 ARG B NE 3078 C CZ . ARG B 191 ? 0.8839 0.9626 1.2890 0.0195 0.0468 0.1816 189 ARG B CZ 3079 N NH1 . ARG B 191 ? 0.9078 0.9783 1.3288 0.0139 0.0406 0.1709 189 ARG B NH1 3080 N NH2 . ARG B 191 ? 0.9011 0.9796 1.3013 0.0230 0.0501 0.1859 189 ARG B NH2 3081 N N . ALA B 192 ? 0.3477 0.4560 0.6767 0.0268 0.0450 0.1546 190 ALA B N 3082 C CA . ALA B 192 ? 0.3346 0.4541 0.6548 0.0314 0.0450 0.1565 190 ALA B CA 3083 C C . ALA B 192 ? 0.2538 0.3827 0.5866 0.0314 0.0474 0.1688 190 ALA B C 3084 O O . ALA B 192 ? 0.3289 0.4541 0.6816 0.0268 0.0470 0.1746 190 ALA B O 3085 C CB . ALA B 192 ? 0.2923 0.4096 0.6150 0.0297 0.0382 0.1458 190 ALA B CB 3086 N N . GLY C 1 ? 0.4808 0.4514 0.4682 -0.0772 -0.0672 0.1231 1 GLY C N 3087 C CA . GLY C 1 ? 0.3286 0.3016 0.3264 -0.0699 -0.0639 0.1126 1 GLY C CA 3088 C C . GLY C 1 ? 0.3894 0.3771 0.3829 -0.0701 -0.0581 0.1061 1 GLY C C 3089 O O . GLY C 1 ? 0.3787 0.3715 0.3598 -0.0751 -0.0528 0.1088 1 GLY C O 3090 N N . VAL C 2 ? 0.3483 0.3395 0.3518 -0.0645 -0.0562 0.0981 2 VAL C N 3091 C CA . VAL C 2 ? 0.3614 0.3622 0.3593 -0.0653 -0.0513 0.0914 2 VAL C CA 3092 C C . VAL C 2 ? 0.3322 0.3349 0.3362 -0.0617 -0.0416 0.0822 2 VAL C C 3093 O O . VAL C 2 ? 0.3141 0.3106 0.3283 -0.0568 -0.0402 0.0778 2 VAL C O 3094 C CB . VAL C 2 ? 0.3231 0.3283 0.3283 -0.0649 -0.0602 0.0923 2 VAL C CB 3095 C CG1 . VAL C 2 ? 0.3325 0.3404 0.3218 -0.0699 -0.0568 0.0857 2 VAL C CG1 3096 C CG2 . VAL C 2 ? 0.3188 0.3208 0.3207 -0.0696 -0.0747 0.1051 2 VAL C CG2 3097 N N . TYR C 3 ? 0.2491 0.2575 0.2463 -0.0639 -0.0332 0.0807 3 TYR C N 3098 C CA . TYR C 3 ? 0.2303 0.2415 0.2337 -0.0615 -0.0263 0.0748 3 TYR C CA 3099 C C . TYR C 3 ? 0.2188 0.2308 0.2254 -0.0576 -0.0242 0.0655 3 TYR C C 3100 O O . TYR C 3 ? 0.2676 0.2820 0.2681 -0.0592 -0.0253 0.0638 3 TYR C O 3101 C CB . TYR C 3 ? 0.2340 0.2531 0.2375 -0.0627 -0.0159 0.0789 3 TYR C CB 3102 C CG . TYR C 3 ? 0.2611 0.2848 0.2758 -0.0669 -0.0177 0.0907 3 TYR C CG 3103 C CD1 . TYR C 3 ? 0.3285 0.3505 0.3511 -0.0702 -0.0241 0.0928 3 TYR C CD1 3104 C CD2 . TYR C 3 ? 0.2594 0.2871 0.2750 -0.0699 -0.0139 0.1015 3 TYR C CD2 3105 C CE1 . TYR C 3 ? 0.3179 0.3443 0.3521 -0.0781 -0.0308 0.1067 3 TYR C CE1 3106 C CE2 . TYR C 3 ? 0.2981 0.3334 0.3309 -0.0754 -0.0169 0.1155 3 TYR C CE2 3107 C CZ . TYR C 3 ? 0.3090 0.3448 0.3526 -0.0804 -0.0274 0.1188 3 TYR C CZ 3108 O OH . TYR C 3 ? 0.3885 0.4322 0.4485 -0.0848 -0.0353 0.1291 3 TYR C OH 3109 N N . ALA C 4 ? 0.2067 0.2133 0.2192 -0.0545 -0.0216 0.0602 4 ALA C N 3110 C CA . ALA C 4 ? 0.1770 0.1850 0.1964 -0.0507 -0.0173 0.0528 4 ALA C CA 3111 C C . ALA C 4 ? 0.2368 0.2476 0.2522 -0.0509 -0.0096 0.0479 4 ALA C C 3112 O O . ALA C 4 ? 0.2750 0.2836 0.2873 -0.0528 -0.0083 0.0509 4 ALA C O 3113 C CB . ALA C 4 ? 0.2189 0.2140 0.2455 -0.0460 -0.0140 0.0504 4 ALA C CB 3114 N N . THR C 5 ? 0.2514 0.2665 0.2688 -0.0503 -0.0063 0.0426 5 THR C N 3115 C CA . THR C 5 ? 0.2477 0.2628 0.2620 -0.0497 0.0022 0.0378 5 THR C CA 3116 C C . THR C 5 ? 0.2492 0.2587 0.2692 -0.0470 0.0065 0.0327 5 THR C C 3117 O O . THR C 5 ? 0.2388 0.2485 0.2698 -0.0451 0.0065 0.0309 5 THR C O 3118 C CB . THR C 5 ? 0.2645 0.2797 0.2706 -0.0528 0.0044 0.0339 5 THR C CB 3119 O OG1 . THR C 5 ? 0.3957 0.4070 0.3859 -0.0558 0.0062 0.0376 5 THR C OG1 3120 C CG2 . THR C 5 ? 0.3768 0.3884 0.3808 -0.0513 0.0146 0.0284 5 THR C CG2 3121 C C1 . CIR C 6 ? 0.2614 0.2606 0.2790 -0.0451 0.0222 0.0228 6 CIR C C1 3122 O O1 . CIR C 6 ? 0.2460 0.2505 0.2614 -0.0458 0.0236 0.0239 6 CIR C O1 3123 C C2 . CIR C 6 ? 0.1673 0.1598 0.1783 -0.0463 0.0162 0.0278 6 CIR C C2 3124 N N2 . CIR C 6 ? 0.2702 0.2743 0.2848 -0.0472 0.0105 0.0326 6 CIR C N2 3125 C C3 . CIR C 6 ? 0.1768 0.1579 0.1745 -0.0505 0.0142 0.0316 6 CIR C C3 3126 C C4 . CIR C 6 ? 0.2527 0.2158 0.2383 -0.0508 0.0222 0.0256 6 CIR C C4 3127 C C5 . CIR C 6 ? 0.3585 0.2977 0.3293 -0.0511 0.0265 0.0223 6 CIR C C5 3128 N N6 . CIR C 6 ? 0.2976 0.2468 0.2905 -0.0436 0.0328 0.0198 6 CIR C N6 3129 C C7 . CIR C 6 ? 0.4230 0.3803 0.4347 -0.0388 0.0436 0.0162 6 CIR C C7 3130 O O7 . CIR C 6 ? 0.4076 0.3606 0.4123 -0.0404 0.0495 0.0131 6 CIR C O7 3131 N N8 . CIR C 6 ? 0.3579 0.3295 0.4003 -0.0332 0.0458 0.0192 6 CIR C N8 3132 N N . SER C 7 ? 0.2511 0.2512 0.2773 -0.0443 0.0277 0.0179 7 SER C N 3133 C CA . SER C 7 ? 0.2342 0.2383 0.2607 -0.0467 0.0303 0.0146 7 SER C CA 3134 C C . SER C 7 ? 0.1710 0.1668 0.1901 -0.0458 0.0384 0.0127 7 SER C C 3135 O O . SER C 7 ? 0.1834 0.1696 0.1956 -0.0451 0.0405 0.0141 7 SER C O 3136 C CB . SER C 7 ? 0.4042 0.4154 0.4476 -0.0494 0.0284 0.0137 7 SER C CB 3137 O OG . SER C 7 ? 0.4525 0.4616 0.5108 -0.0451 0.0362 0.0143 7 SER C OG 3138 N N . SER C 8 ? 0.1660 0.1604 0.1816 -0.0473 0.0426 0.0102 8 SER C N 3139 C CA . SER C 8 ? 0.2069 0.1932 0.2184 -0.0459 0.0504 0.0100 8 SER C CA 3140 C C . SER C 8 ? 0.2275 0.2104 0.2436 -0.0487 0.0554 0.0045 8 SER C C 3141 O O . SER C 8 ? 0.2633 0.2498 0.2849 -0.0535 0.0531 0.0014 8 SER C O 3142 C CB . SER C 8 ? 0.2399 0.2220 0.2460 -0.0441 0.0568 0.0117 8 SER C CB 3143 O OG . SER C 8 ? 0.2673 0.2551 0.2769 -0.0406 0.0553 0.0201 8 SER C OG 3144 N N . ALA C 9 ? 0.2524 0.2266 0.2648 -0.0477 0.0612 0.0050 9 ALA C N 3145 C CA . ALA C 9 ? 0.2099 0.1804 0.2290 -0.0498 0.0694 0.0015 9 ALA C CA 3146 C C . ALA C 9 ? 0.2034 0.1705 0.2218 -0.0532 0.0730 -0.0013 9 ALA C C 3147 O O . ALA C 9 ? 0.1929 0.1525 0.2009 -0.0514 0.0747 0.0002 9 ALA C O 3148 C CB . ALA C 9 ? 0.1967 0.1507 0.2019 -0.0490 0.0771 0.0025 9 ALA C CB 3149 N N . VAL C 10 ? 0.2107 0.1822 0.2431 -0.0586 0.0746 -0.0034 10 VAL C N 3150 C CA . VAL C 10 ? 0.2014 0.1654 0.2301 -0.0653 0.0763 -0.0064 10 VAL C CA 3151 C C . VAL C 10 ? 0.3267 0.2790 0.3518 -0.0645 0.0880 -0.0064 10 VAL C C 3152 O O . VAL C 10 ? 0.2099 0.1638 0.2453 -0.0640 0.0955 -0.0047 10 VAL C O 3153 C CB . VAL C 10 ? 0.3627 0.3373 0.4098 -0.0759 0.0675 -0.0054 10 VAL C CB 3154 C CG1 . VAL C 10 ? 0.3315 0.2913 0.3667 -0.0869 0.0670 -0.0091 10 VAL C CG1 3155 C CG2 . VAL C 10 ? 0.3447 0.3283 0.3916 -0.0784 0.0536 -0.0035 10 VAL C CG2 3156 C C1 . CIR C 11 ? 0.3395 0.2615 0.3518 -0.0723 0.1048 -0.0086 11 CIR C C1 3157 O O1 . CIR C 11 ? 0.3794 0.3054 0.3974 -0.0809 0.0974 -0.0116 11 CIR C O1 3158 C C2 A CIR C 11 ? 0.3380 0.2625 0.3414 -0.0633 0.1008 -0.0059 11 CIR C C2 3159 C C2 B CIR C 11 ? 0.3279 0.2522 0.3312 -0.0632 0.1009 -0.0057 11 CIR C C2 3160 N N2 . CIR C 11 ? 0.2195 0.1575 0.2290 -0.0637 0.0916 -0.0074 11 CIR C N2 3161 C C3 A CIR C 11 ? 0.3860 0.2966 0.3774 -0.0592 0.1042 -0.0041 11 CIR C C3 3162 C C3 B CIR C 11 ? 0.3857 0.2965 0.3771 -0.0584 0.1042 -0.0033 11 CIR C C3 3163 C C4 A CIR C 11 ? 0.4417 0.3377 0.4278 -0.0579 0.1119 0.0005 11 CIR C C4 3164 C C4 B CIR C 11 ? 0.4146 0.3199 0.4015 -0.0526 0.1053 0.0063 11 CIR C C4 3165 C C5 A CIR C 11 ? 0.4399 0.3335 0.4253 -0.0489 0.1110 0.0108 11 CIR C C5 3166 C C5 B CIR C 11 ? 0.4266 0.3426 0.4156 -0.0477 0.0963 0.0134 11 CIR C C5 3167 N N6 A CIR C 11 ? 0.4350 0.3412 0.4211 -0.0479 0.1010 0.0157 11 CIR C N6 3168 N N6 B CIR C 11 ? 0.4625 0.3765 0.4581 -0.0408 0.0971 0.0247 11 CIR C N6 3169 C C7 A CIR C 11 ? 0.4656 0.3817 0.4593 -0.0422 0.0941 0.0246 11 CIR C C7 3170 C C7 B CIR C 11 ? 0.4845 0.4079 0.4867 -0.0385 0.0861 0.0384 11 CIR C C7 3171 O O7 A CIR C 11 ? 0.4846 0.4000 0.4877 -0.0357 0.0999 0.0290 11 CIR C O7 3172 O O7 B CIR C 11 ? 0.4237 0.3503 0.4422 -0.0322 0.0866 0.0524 11 CIR C O7 3173 N N8 A CIR C 11 ? 0.5119 0.4353 0.5013 -0.0447 0.0823 0.0290 11 CIR C N8 3174 N N8 B CIR C 11 ? 0.5458 0.4733 0.5375 -0.0443 0.0746 0.0375 11 CIR C N8 3175 N N . LEU C 12 ? 0.4644 0.3785 0.4781 -0.0742 0.1145 -0.0068 12 LEU C N 3176 C CA . LEU C 12 ? 0.5730 0.4891 0.6003 -0.0826 0.1152 -0.0077 12 LEU C CA 3177 C C . LEU C 12 ? 0.6055 0.5002 0.6158 -0.0868 0.1174 -0.0105 12 LEU C C 3178 O O . LEU C 12 ? 0.4415 0.3217 0.4365 -0.0795 0.1235 -0.0087 12 LEU C O 3179 C CB . LEU C 12 ? 0.6177 0.5375 0.6553 -0.0787 0.1241 -0.0041 12 LEU C CB 3180 C CG . LEU C 12 ? 0.6373 0.5626 0.6953 -0.0863 0.1264 -0.0012 12 LEU C CG 3181 C CD1 . LEU C 12 ? 0.6378 0.5868 0.7300 -0.0952 0.1161 0.0036 12 LEU C CD1 3182 C CD2 . LEU C 12 ? 0.5974 0.5175 0.6558 -0.0799 0.1408 0.0017 12 LEU C CD2 # 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 CIR 11 11 11 CIR CIR C . n C 3 12 LEU 12 12 12 LEU LEU C . n C 3 13 CIR 13 13 13 CIR CIR 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 118 A ASN 118 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 78 A ASN 78 ? ASN 'GLYCOSYLATION SITE' 4 C CIR 6 C CIR 6 ? ARG CITRULLINE 5 C CIR 11 C CIR 11 ? ARG CITRULLINE 6 C CIR 13 C CIR 13 ? 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,J # 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)' 7910 ? 1 MORE -19 ? 1 'SSA (A^2)' 18000 ? # _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 701 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id I _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 41.8312 26.5059 -4.0986 0.0965 0.1295 0.0816 0.0212 -0.0064 -0.0105 1.1824 2.8098 0.4986 -0.0520 -0.4403 -0.3321 -0.0807 -0.0881 -0.0097 0.1594 0.0402 0.1021 -0.0776 -0.0092 0.0292 'X-RAY DIFFRACTION' 2 ? refined 41.3224 18.5607 5.7517 0.2341 0.2205 0.1657 0.0218 -0.0118 0.0761 2.1894 1.0940 1.6579 -0.1606 0.5783 -0.0943 -0.0242 -0.6031 -0.2940 0.4449 -0.0070 -0.0289 0.0395 0.0798 0.0486 'X-RAY DIFFRACTION' 3 ? refined 51.6868 35.7673 -4.7580 0.1328 0.1753 0.1351 -0.0172 -0.0131 -0.0727 1.4367 3.2531 3.6584 -0.3704 0.1846 -2.2236 0.0891 -0.1586 0.0227 0.0742 -0.0327 -0.3018 -0.1525 0.2172 -0.0283 'X-RAY DIFFRACTION' 4 ? refined 24.5256 31.4244 -1.5207 0.0970 0.1908 0.0435 0.0692 0.1220 0.0062 2.3130 1.6892 0.9101 1.2326 -0.8766 -0.4061 -0.3788 -0.2622 -0.0885 0.1188 0.0686 0.0262 -0.1315 -0.1899 0.0502 'X-RAY DIFFRACTION' 5 ? refined 24.6631 31.3669 3.1035 0.0281 0.1306 -0.5429 0.1468 0.3704 -0.0925 0.7813 0.9346 0.4051 0.4023 -0.3017 -0.2540 -0.0680 -0.0989 -0.1605 -0.0303 0.2302 0.3337 0.0163 -0.0819 -0.0296 'X-RAY DIFFRACTION' 6 ? refined 27.2845 28.6458 3.4800 0.1615 0.0984 0.0467 0.0245 0.0439 0.0078 0.7971 0.4558 0.0818 -0.0534 -0.1316 -0.1318 -0.1077 -0.2118 -0.0647 0.2279 0.0860 0.0919 0.0144 0.0831 0.0143 'X-RAY DIFFRACTION' 7 ? refined 14.5284 32.2721 9.3974 0.2577 0.1708 0.1991 0.0199 0.1482 -0.0232 2.2675 3.4318 1.9597 1.3710 -0.4876 -0.9356 0.1415 -0.4055 0.1222 0.4021 -0.0909 0.4251 -0.1368 0.0475 -0.0978 'X-RAY DIFFRACTION' 8 ? refined 17.9023 36.6944 1.4208 0.2082 0.1666 0.2449 0.0840 0.0057 -0.0086 4.2178 2.8578 1.6876 2.3875 -1.8873 -1.4220 0.1721 0.3311 0.2940 -0.0244 0.2446 0.6237 -0.1684 -0.3728 -0.1956 'X-RAY DIFFRACTION' 9 ? refined 48.8512 25.7110 -14.2972 0.0819 0.0958 0.0897 0.0097 0.0078 -0.0253 1.1462 1.0942 0.9198 0.1496 -0.2294 -0.0058 -0.0622 0.0446 -0.1071 -0.1224 0.0381 -0.1167 -0.0192 0.0358 0.0170 'X-RAY DIFFRACTION' 10 ? refined 14.6013 11.9652 -5.0025 0.1746 0.1538 0.2229 0.0304 0.0754 0.0588 3.0777 0.6032 1.1477 0.1029 0.5625 -0.1346 -0.0074 -0.2566 -0.1284 -0.1107 0.0468 0.0368 -0.0661 -0.2282 -0.0086 'X-RAY DIFFRACTION' 11 ? refined 10.9093 9.8377 -8.1341 0.1440 0.1519 0.2987 0.0141 0.0383 0.0630 1.2964 0.3049 0.5456 -0.3340 0.3853 -0.0462 -0.1021 -0.0845 -0.4359 -0.0728 0.1309 0.2291 -0.0282 -0.0752 -0.0287 'X-RAY DIFFRACTION' 12 ? refined 52.9105 25.0366 -6.2279 0.1613 0.1610 0.1789 -0.0460 0.0343 0.0151 1.4141 5.7940 2.4923 1.4599 -0.7098 -2.4790 0.1136 -0.1322 -0.0060 -0.0104 0.0394 -0.1671 -0.0541 0.0302 -0.1337 # 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 26 ) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 27 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 101 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 102 through 123 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 124 through 154 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 155 through 166 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 167 through 181 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 2 through 86 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 87 through 133 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 134 through 190 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1 through 12 ) ; # 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_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 ND2 A ASN 118 ? ? C2 A NAG 501 ? ? 2.12 2 1 O4 A NAG 501 ? ? O5 A NAG 502 ? ? 2.18 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 100 ? ? 47.98 28.21 2 1 HIS B 33 ? ? 60.01 -113.42 3 1 THR B 90 ? ? -123.72 -71.84 4 1 LEU B 109 ? ? 65.77 -29.06 5 1 PRO B 124 ? ? -78.73 -168.59 # 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 2 502 502 NAG NAG A . G 4 NAG 1 500 500 NAG NAG B . H 5 HOH 1 601 1 HOH HOH A . H 5 HOH 2 602 3 HOH HOH A . H 5 HOH 3 603 4 HOH HOH A . H 5 HOH 4 604 5 HOH HOH A . H 5 HOH 5 605 8 HOH HOH A . H 5 HOH 6 606 9 HOH HOH A . H 5 HOH 7 607 12 HOH HOH A . H 5 HOH 8 608 16 HOH HOH A . H 5 HOH 9 609 17 HOH HOH A . H 5 HOH 10 610 19 HOH HOH A . H 5 HOH 11 611 20 HOH HOH A . H 5 HOH 12 612 22 HOH HOH A . H 5 HOH 13 613 23 HOH HOH A . H 5 HOH 14 614 24 HOH HOH A . H 5 HOH 15 615 27 HOH HOH A . H 5 HOH 16 616 28 HOH HOH A . H 5 HOH 17 617 29 HOH HOH A . H 5 HOH 18 618 30 HOH HOH A . H 5 HOH 19 619 31 HOH HOH A . H 5 HOH 20 620 32 HOH HOH A . H 5 HOH 21 621 36 HOH HOH A . H 5 HOH 22 622 39 HOH HOH A . H 5 HOH 23 623 42 HOH HOH A . H 5 HOH 24 624 43 HOH HOH A . H 5 HOH 25 625 44 HOH HOH A . H 5 HOH 26 626 47 HOH HOH A . H 5 HOH 27 627 49 HOH HOH A . H 5 HOH 28 628 51 HOH HOH A . H 5 HOH 29 629 53 HOH HOH A . H 5 HOH 30 630 54 HOH HOH A . H 5 HOH 31 631 55 HOH HOH A . H 5 HOH 32 632 57 HOH HOH A . H 5 HOH 33 633 62 HOH HOH A . H 5 HOH 34 634 63 HOH HOH A . H 5 HOH 35 635 64 HOH HOH A . H 5 HOH 36 636 65 HOH HOH A . H 5 HOH 37 637 68 HOH HOH A . H 5 HOH 38 638 72 HOH HOH A . H 5 HOH 39 639 73 HOH HOH A . H 5 HOH 40 640 75 HOH HOH A . H 5 HOH 41 641 77 HOH HOH A . H 5 HOH 42 642 78 HOH HOH A . H 5 HOH 43 643 79 HOH HOH A . H 5 HOH 44 644 80 HOH HOH A . H 5 HOH 45 645 81 HOH HOH A . H 5 HOH 46 646 85 HOH HOH A . H 5 HOH 47 647 90 HOH HOH A . H 5 HOH 48 648 94 HOH HOH A . H 5 HOH 49 649 96 HOH HOH A . H 5 HOH 50 650 98 HOH HOH A . H 5 HOH 51 651 100 HOH HOH A . H 5 HOH 52 652 101 HOH HOH A . H 5 HOH 53 653 105 HOH HOH A . H 5 HOH 54 654 107 HOH HOH A . H 5 HOH 55 655 108 HOH HOH A . H 5 HOH 56 656 109 HOH HOH A . H 5 HOH 57 657 115 HOH HOH A . H 5 HOH 58 658 117 HOH HOH A . H 5 HOH 59 659 121 HOH HOH A . H 5 HOH 60 660 124 HOH HOH A . H 5 HOH 61 661 126 HOH HOH A . H 5 HOH 62 662 128 HOH HOH A . H 5 HOH 63 663 129 HOH HOH A . H 5 HOH 64 664 130 HOH HOH A . H 5 HOH 65 665 132 HOH HOH A . H 5 HOH 66 666 133 HOH HOH A . H 5 HOH 67 667 138 HOH HOH A . H 5 HOH 68 668 140 HOH HOH A . H 5 HOH 69 669 141 HOH HOH A . H 5 HOH 70 670 142 HOH HOH A . H 5 HOH 71 671 145 HOH HOH A . H 5 HOH 72 672 149 HOH HOH A . H 5 HOH 73 673 150 HOH HOH A . H 5 HOH 74 674 152 HOH HOH A . H 5 HOH 75 675 154 HOH HOH A . H 5 HOH 76 676 158 HOH HOH A . H 5 HOH 77 677 159 HOH HOH A . H 5 HOH 78 678 162 HOH HOH A . H 5 HOH 79 679 166 HOH HOH A . H 5 HOH 80 680 167 HOH HOH A . H 5 HOH 81 681 169 HOH HOH A . H 5 HOH 82 682 171 HOH HOH A . H 5 HOH 83 683 172 HOH HOH A . H 5 HOH 84 684 173 HOH HOH A . H 5 HOH 85 685 175 HOH HOH A . H 5 HOH 86 686 176 HOH HOH A . H 5 HOH 87 687 178 HOH HOH A . H 5 HOH 88 688 185 HOH HOH A . H 5 HOH 89 689 186 HOH HOH A . H 5 HOH 90 690 190 HOH HOH A . H 5 HOH 91 691 191 HOH HOH A . H 5 HOH 92 692 192 HOH HOH A . H 5 HOH 93 693 195 HOH HOH A . H 5 HOH 94 694 199 HOH HOH A . H 5 HOH 95 695 200 HOH HOH A . H 5 HOH 96 696 202 HOH HOH A . H 5 HOH 97 697 203 HOH HOH A . H 5 HOH 98 698 204 HOH HOH A . H 5 HOH 99 699 206 HOH HOH A . H 5 HOH 100 700 210 HOH HOH A . H 5 HOH 101 701 211 HOH HOH A . H 5 HOH 102 702 213 HOH HOH A . H 5 HOH 103 703 214 HOH HOH A . H 5 HOH 104 704 216 HOH HOH A . H 5 HOH 105 705 218 HOH HOH A . H 5 HOH 106 706 220 HOH HOH A . H 5 HOH 107 707 221 HOH HOH A . H 5 HOH 108 708 223 HOH HOH A . H 5 HOH 109 709 225 HOH HOH A . H 5 HOH 110 710 227 HOH HOH A . H 5 HOH 111 711 229 HOH HOH A . H 5 HOH 112 712 232 HOH HOH A . H 5 HOH 113 713 233 HOH HOH A . H 5 HOH 114 714 234 HOH HOH A . H 5 HOH 115 715 235 HOH HOH A . H 5 HOH 116 716 237 HOH HOH A . H 5 HOH 117 717 238 HOH HOH A . H 5 HOH 118 718 242 HOH HOH A . H 5 HOH 119 719 245 HOH HOH A . H 5 HOH 120 720 251 HOH HOH A . H 5 HOH 121 721 254 HOH HOH A . H 5 HOH 122 722 259 HOH HOH A . H 5 HOH 123 723 262 HOH HOH A . H 5 HOH 124 724 267 HOH HOH A . H 5 HOH 125 725 269 HOH HOH A . H 5 HOH 126 726 272 HOH HOH A . H 5 HOH 127 727 273 HOH HOH A . H 5 HOH 128 728 274 HOH HOH A . H 5 HOH 129 729 276 HOH HOH A . H 5 HOH 130 730 277 HOH HOH A . H 5 HOH 131 731 279 HOH HOH A . H 5 HOH 132 732 281 HOH HOH A . H 5 HOH 133 733 288 HOH HOH A . H 5 HOH 134 734 290 HOH HOH A . H 5 HOH 135 735 291 HOH HOH A . H 5 HOH 136 736 293 HOH HOH A . H 5 HOH 137 737 296 HOH HOH A . H 5 HOH 138 738 297 HOH HOH A . H 5 HOH 139 739 299 HOH HOH A . H 5 HOH 140 740 301 HOH HOH A . H 5 HOH 141 741 303 HOH HOH A . H 5 HOH 142 742 304 HOH HOH A . H 5 HOH 143 743 305 HOH HOH A . H 5 HOH 144 744 306 HOH HOH A . H 5 HOH 145 745 307 HOH HOH A . H 5 HOH 146 746 308 HOH HOH A . H 5 HOH 147 747 310 HOH HOH A . H 5 HOH 148 748 313 HOH HOH A . H 5 HOH 149 749 315 HOH HOH A . H 5 HOH 150 750 317 HOH HOH A . H 5 HOH 151 751 320 HOH HOH A . H 5 HOH 152 752 323 HOH HOH A . H 5 HOH 153 753 325 HOH HOH A . H 5 HOH 154 754 326 HOH HOH A . H 5 HOH 155 755 327 HOH HOH A . H 5 HOH 156 756 328 HOH HOH A . H 5 HOH 157 757 329 HOH HOH A . H 5 HOH 158 758 330 HOH HOH A . H 5 HOH 159 759 332 HOH HOH A . H 5 HOH 160 760 333 HOH HOH A . H 5 HOH 161 761 338 HOH HOH A . H 5 HOH 162 762 341 HOH HOH A . H 5 HOH 163 763 342 HOH HOH A . H 5 HOH 164 764 343 HOH HOH A . H 5 HOH 165 765 344 HOH HOH A . H 5 HOH 166 766 351 HOH HOH A . H 5 HOH 167 767 354 HOH HOH A . H 5 HOH 168 768 355 HOH HOH A . H 5 HOH 169 769 356 HOH HOH A . H 5 HOH 170 770 360 HOH HOH A . H 5 HOH 171 771 361 HOH HOH A . H 5 HOH 172 772 362 HOH HOH A . H 5 HOH 173 773 363 HOH HOH A . H 5 HOH 174 774 364 HOH HOH A . H 5 HOH 175 775 365 HOH HOH A . H 5 HOH 176 776 367 HOH HOH A . H 5 HOH 177 777 368 HOH HOH A . H 5 HOH 178 778 369 HOH HOH A . H 5 HOH 179 779 370 HOH HOH A . H 5 HOH 180 780 373 HOH HOH A . H 5 HOH 181 781 376 HOH HOH A . H 5 HOH 182 782 378 HOH HOH A . I 5 HOH 1 601 2 HOH HOH B . I 5 HOH 2 602 6 HOH HOH B . I 5 HOH 3 603 7 HOH HOH B . I 5 HOH 4 604 10 HOH HOH B . I 5 HOH 5 605 11 HOH HOH B . I 5 HOH 6 606 13 HOH HOH B . I 5 HOH 7 607 14 HOH HOH B . I 5 HOH 8 608 15 HOH HOH B . I 5 HOH 9 609 18 HOH HOH B . I 5 HOH 10 610 21 HOH HOH B . I 5 HOH 11 611 25 HOH HOH B . I 5 HOH 12 612 26 HOH HOH B . I 5 HOH 13 613 33 HOH HOH B . I 5 HOH 14 614 34 HOH HOH B . I 5 HOH 15 615 35 HOH HOH B . I 5 HOH 16 616 37 HOH HOH B . I 5 HOH 17 617 40 HOH HOH B . I 5 HOH 18 618 41 HOH HOH B . I 5 HOH 19 619 45 HOH HOH B . I 5 HOH 20 620 48 HOH HOH B . I 5 HOH 21 621 50 HOH HOH B . I 5 HOH 22 622 52 HOH HOH B . I 5 HOH 23 623 56 HOH HOH B . I 5 HOH 24 624 58 HOH HOH B . I 5 HOH 25 625 59 HOH HOH B . I 5 HOH 26 626 60 HOH HOH B . I 5 HOH 27 627 61 HOH HOH B . I 5 HOH 28 628 66 HOH HOH B . I 5 HOH 29 629 67 HOH HOH B . I 5 HOH 30 630 69 HOH HOH B . I 5 HOH 31 631 70 HOH HOH B . I 5 HOH 32 632 71 HOH HOH B . I 5 HOH 33 633 74 HOH HOH B . I 5 HOH 34 634 76 HOH HOH B . I 5 HOH 35 635 82 HOH HOH B . I 5 HOH 36 636 83 HOH HOH B . I 5 HOH 37 637 84 HOH HOH B . I 5 HOH 38 638 86 HOH HOH B . I 5 HOH 39 639 88 HOH HOH B . I 5 HOH 40 640 89 HOH HOH B . I 5 HOH 41 641 91 HOH HOH B . I 5 HOH 42 642 92 HOH HOH B . I 5 HOH 43 643 93 HOH HOH B . I 5 HOH 44 644 95 HOH HOH B . I 5 HOH 45 645 97 HOH HOH B . I 5 HOH 46 646 102 HOH HOH B . I 5 HOH 47 647 103 HOH HOH B . I 5 HOH 48 648 104 HOH HOH B . I 5 HOH 49 649 106 HOH HOH B . I 5 HOH 50 650 110 HOH HOH B . I 5 HOH 51 651 111 HOH HOH B . I 5 HOH 52 652 113 HOH HOH B . I 5 HOH 53 653 114 HOH HOH B . I 5 HOH 54 654 116 HOH HOH B . I 5 HOH 55 655 119 HOH HOH B . I 5 HOH 56 656 122 HOH HOH B . I 5 HOH 57 657 125 HOH HOH B . I 5 HOH 58 658 127 HOH HOH B . I 5 HOH 59 659 131 HOH HOH B . I 5 HOH 60 660 134 HOH HOH B . I 5 HOH 61 661 135 HOH HOH B . I 5 HOH 62 662 136 HOH HOH B . I 5 HOH 63 663 139 HOH HOH B . I 5 HOH 64 664 143 HOH HOH B . I 5 HOH 65 665 144 HOH HOH B . I 5 HOH 66 666 146 HOH HOH B . I 5 HOH 67 667 148 HOH HOH B . I 5 HOH 68 668 151 HOH HOH B . I 5 HOH 69 669 153 HOH HOH B . I 5 HOH 70 670 155 HOH HOH B . I 5 HOH 71 671 156 HOH HOH B . I 5 HOH 72 672 157 HOH HOH B . I 5 HOH 73 673 160 HOH HOH B . I 5 HOH 74 674 161 HOH HOH B . I 5 HOH 75 675 163 HOH HOH B . I 5 HOH 76 676 164 HOH HOH B . I 5 HOH 77 677 165 HOH HOH B . I 5 HOH 78 678 168 HOH HOH B . I 5 HOH 79 679 170 HOH HOH B . I 5 HOH 80 680 174 HOH HOH B . I 5 HOH 81 681 177 HOH HOH B . I 5 HOH 82 682 179 HOH HOH B . I 5 HOH 83 683 180 HOH HOH B . I 5 HOH 84 684 182 HOH HOH B . I 5 HOH 85 685 183 HOH HOH B . I 5 HOH 86 686 184 HOH HOH B . I 5 HOH 87 687 187 HOH HOH B . I 5 HOH 88 688 188 HOH HOH B . I 5 HOH 89 689 189 HOH HOH B . I 5 HOH 90 690 194 HOH HOH B . I 5 HOH 91 691 197 HOH HOH B . I 5 HOH 92 692 198 HOH HOH B . I 5 HOH 93 693 201 HOH HOH B . I 5 HOH 94 694 205 HOH HOH B . I 5 HOH 95 695 207 HOH HOH B . I 5 HOH 96 696 208 HOH HOH B . I 5 HOH 97 697 212 HOH HOH B . I 5 HOH 98 698 215 HOH HOH B . I 5 HOH 99 699 217 HOH HOH B . I 5 HOH 100 700 222 HOH HOH B . I 5 HOH 101 701 224 HOH HOH B . I 5 HOH 102 702 226 HOH HOH B . I 5 HOH 103 703 228 HOH HOH B . I 5 HOH 104 704 231 HOH HOH B . I 5 HOH 105 705 239 HOH HOH B . I 5 HOH 106 706 240 HOH HOH B . I 5 HOH 107 707 241 HOH HOH B . I 5 HOH 108 708 243 HOH HOH B . I 5 HOH 109 709 244 HOH HOH B . I 5 HOH 110 710 246 HOH HOH B . I 5 HOH 111 711 247 HOH HOH B . I 5 HOH 112 712 248 HOH HOH B . I 5 HOH 113 713 249 HOH HOH B . I 5 HOH 114 714 250 HOH HOH B . I 5 HOH 115 715 252 HOH HOH B . I 5 HOH 116 716 253 HOH HOH B . I 5 HOH 117 717 255 HOH HOH B . I 5 HOH 118 718 256 HOH HOH B . I 5 HOH 119 719 258 HOH HOH B . I 5 HOH 120 720 261 HOH HOH B . I 5 HOH 121 721 263 HOH HOH B . I 5 HOH 122 722 264 HOH HOH B . I 5 HOH 123 723 270 HOH HOH B . I 5 HOH 124 724 271 HOH HOH B . I 5 HOH 125 725 275 HOH HOH B . I 5 HOH 126 726 278 HOH HOH B . I 5 HOH 127 727 283 HOH HOH B . I 5 HOH 128 728 284 HOH HOH B . I 5 HOH 129 729 285 HOH HOH B . I 5 HOH 130 730 286 HOH HOH B . I 5 HOH 131 731 287 HOH HOH B . I 5 HOH 132 732 292 HOH HOH B . I 5 HOH 133 733 295 HOH HOH B . I 5 HOH 134 734 300 HOH HOH B . I 5 HOH 135 735 309 HOH HOH B . I 5 HOH 136 736 311 HOH HOH B . I 5 HOH 137 737 312 HOH HOH B . I 5 HOH 138 738 314 HOH HOH B . I 5 HOH 139 739 318 HOH HOH B . I 5 HOH 140 740 319 HOH HOH B . I 5 HOH 141 741 321 HOH HOH B . I 5 HOH 142 742 322 HOH HOH B . I 5 HOH 143 743 324 HOH HOH B . I 5 HOH 144 744 331 HOH HOH B . I 5 HOH 145 745 337 HOH HOH B . I 5 HOH 146 746 339 HOH HOH B . I 5 HOH 147 747 340 HOH HOH B . I 5 HOH 148 748 347 HOH HOH B . I 5 HOH 149 749 348 HOH HOH B . I 5 HOH 150 750 366 HOH HOH B . I 5 HOH 151 751 371 HOH HOH B . I 5 HOH 152 752 372 HOH HOH B . I 5 HOH 153 753 374 HOH HOH B . I 5 HOH 154 754 375 HOH HOH B . I 5 HOH 155 755 377 HOH HOH B . I 5 HOH 156 756 379 HOH HOH B . I 5 HOH 157 757 380 HOH HOH B . J 5 HOH 1 101 38 HOH HOH C . J 5 HOH 2 102 46 HOH HOH C . J 5 HOH 3 103 99 HOH HOH C . J 5 HOH 4 104 118 HOH HOH C . J 5 HOH 5 105 147 HOH HOH C . J 5 HOH 6 106 181 HOH HOH C . J 5 HOH 7 107 219 HOH HOH C . J 5 HOH 8 108 257 HOH HOH C . J 5 HOH 9 109 266 HOH HOH C . J 5 HOH 10 110 268 HOH HOH C . J 5 HOH 11 111 289 HOH HOH C . J 5 HOH 12 112 294 HOH HOH C . J 5 HOH 13 113 298 HOH HOH C . J 5 HOH 14 114 352 HOH HOH C . J 5 HOH 15 115 353 HOH HOH C . #