data_4MD5 # _entry.id 4MD5 # _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 4MD5 RCSB RCSB081761 WWPDB D_1000081761 # 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 4MD0 . unspecified PDB 4MD4 . unspecified PDB 4MDI . unspecified PDB 4MDJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MD5 _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 4MD5 _cell.length_a 67.420 _cell.length_b 183.001 _cell.length_c 77.516 _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 4MD5 _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' 23294.709 1 ? ? 'Extracellular Domain, UNP residues 30-219' ? 3 polymer syn 'Citrullinated Vimentin' 1386.602 1 ? ? 'Residues 66-78' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 5 non-polymer syn 1,2-ETHANEDIOL 62.068 8 ? ? ? ? 6 non-polymer syn 'TRIETHYLENE GLYCOL' 150.173 1 ? ? ? ? 7 water nat water 18.015 466 ? ? ? ? # 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 ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTY CRHNYGVVESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTY CRHNYGVVESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; B ? 3 'polypeptide(L)' no yes 'SAVRL(CIR)SSVPGVR' SAVRLRSSVPGVR 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 ARG 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 VAL 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 SER n 3 2 ALA n 3 3 VAL n 3 4 ARG n 3 5 LEU n 3 6 CIR n 3 7 SER n 3 8 SER n 3 9 VAL n 3 10 PRO n 3 11 GLY n 3 12 VAL n 3 13 ARG n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? human ? 'HLA-DRA, HLA-DRA1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? human ? HLA-DRB1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'Homo sapiens' _pdbx_entity_src_syn.organism_common_name ? _pdbx_entity_src_syn.ncbi_taxonomy_id 9606 _pdbx_entity_src_syn.details 'This sequence is from human vimentin and contains citrulline at position 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 SAVRLRSSVPGVR 66 ? # 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 4MD5 A 1 ? 181 ? P01903 26 ? 206 ? 1 181 2 2 4MD5 B 3 ? 192 ? P13760 30 ? 219 ? 1 190 3 3 4MD5 C 1 ? 13 ? P08670 66 ? 78 ? 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 4MD5 THR A 182 ? UNP P01903 ? ? 'EXPRESSION TAG' 182 1 1 4MD5 SER A 183 ? UNP P01903 ? ? 'EXPRESSION TAG' 183 2 1 4MD5 GLY A 184 ? UNP P01903 ? ? 'EXPRESSION TAG' 184 3 1 4MD5 ASP A 185 ? UNP P01903 ? ? 'EXPRESSION TAG' 185 4 1 4MD5 ASP A 186 ? UNP P01903 ? ? 'EXPRESSION TAG' 186 5 1 4MD5 ASP A 187 ? UNP P01903 ? ? 'EXPRESSION TAG' 187 6 1 4MD5 ASP A 188 ? UNP P01903 ? ? 'EXPRESSION TAG' 188 7 1 4MD5 LYS A 189 ? UNP P01903 ? ? 'EXPRESSION TAG' 189 8 2 4MD5 GLY B 1 ? UNP P13760 ? ? 'EXPRESSION TAG' -1 9 2 4MD5 SER B 2 ? UNP P13760 ? ? 'EXPRESSION TAG' 0 10 2 4MD5 ARG B 73 ? UNP P13760 LYS 100 VARIANT 71 11 2 4MD5 VAL B 88 ? UNP P13760 GLY 115 VARIANT 86 12 2 4MD5 THR B 193 ? UNP P13760 ? ? 'EXPRESSION TAG' 191 13 2 4MD5 GLY B 194 ? UNP P13760 ? ? 'EXPRESSION TAG' 192 14 2 4MD5 GLY B 195 ? UNP P13760 ? ? 'EXPRESSION TAG' 193 15 2 4MD5 ASP B 196 ? UNP P13760 ? ? 'EXPRESSION TAG' 194 16 2 4MD5 ASP B 197 ? UNP P13760 ? ? 'EXPRESSION TAG' 195 17 2 4MD5 ASP B 198 ? UNP P13760 ? ? 'EXPRESSION TAG' 196 18 2 4MD5 ASP B 199 ? UNP P13760 ? ? 'EXPRESSION TAG' 197 19 2 4MD5 LYS B 200 ? UNP P13760 ? ? 'EXPRESSION TAG' 198 20 # 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 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 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 PGE non-polymer . 'TRIETHYLENE GLYCOL' ? 'C6 H14 O4' 150.173 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 4MD5 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_percent_sol 53.99 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 294 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.3 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '26% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 210r' _diffrn_detector.pdbx_collection_date 2012-08-09 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength .95370 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' _diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' _diffrn_source.pdbx_synchrotron_beamline MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list .95370 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MD5 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 45.75 _reflns.d_resolution_high 1.65 _reflns.number_obs 58009 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs 0.1 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.2 _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 1.65 _reflns_shell.d_res_low 1.74 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.472 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.3 _reflns_shell.pdbx_redundancy 7.1 _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 4MD5 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 57973 _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 32.166 _refine.ls_d_res_high 1.650 _refine.ls_percent_reflns_obs 99.94 _refine.ls_R_factor_obs 0.1637 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1626 _refine.ls_R_factor_R_free 0.1858 _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 2908 _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 0.15 _refine.pdbx_overall_phase_error 17.00 _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 3148 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 98 _refine_hist.number_atoms_solvent 466 _refine_hist.number_atoms_total 3712 _refine_hist.d_res_high 1.650 _refine_hist.d_res_low 32.166 # 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 ? ? 3512 'X-RAY DIFFRACTION' ? f_angle_d 1.022 ? ? 4790 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 16.274 ? ? 1323 'X-RAY DIFFRACTION' ? f_chiral_restr 0.073 ? ? 517 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 627 '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' . 1.6500 1.6771 2573 0.1936 100.00 0.2114 . . 139 . . . . 'X-RAY DIFFRACTION' . 1.6771 1.7060 2579 0.1893 100.00 0.2096 . . 156 . . . . 'X-RAY DIFFRACTION' . 1.7060 1.7370 2593 0.1813 100.00 0.2332 . . 117 . . . . 'X-RAY DIFFRACTION' . 1.7370 1.7704 2613 0.1806 100.00 0.2289 . . 142 . . . . 'X-RAY DIFFRACTION' . 1.7704 1.8065 2590 0.1732 100.00 0.1950 . . 142 . . . . 'X-RAY DIFFRACTION' . 1.8065 1.8458 2593 0.1701 100.00 0.1884 . . 139 . . . . 'X-RAY DIFFRACTION' . 1.8458 1.8887 2591 0.1699 100.00 0.2332 . . 138 . . . . 'X-RAY DIFFRACTION' . 1.8887 1.9360 2594 0.1642 100.00 0.2300 . . 141 . . . . 'X-RAY DIFFRACTION' . 1.9360 1.9883 2619 0.1544 100.00 0.1619 . . 138 . . . . 'X-RAY DIFFRACTION' . 1.9883 2.0468 2604 0.1516 100.00 0.2021 . . 118 . . . . 'X-RAY DIFFRACTION' . 2.0468 2.1129 2616 0.1556 100.00 0.1771 . . 136 . . . . 'X-RAY DIFFRACTION' . 2.1129 2.1884 2604 0.1568 100.00 0.1867 . . 126 . . . . 'X-RAY DIFFRACTION' . 2.1884 2.2759 2634 0.1547 100.00 0.1821 . . 136 . . . . 'X-RAY DIFFRACTION' . 2.2759 2.3795 2624 0.1668 100.00 0.1668 . . 130 . . . . 'X-RAY DIFFRACTION' . 2.3795 2.5049 2630 0.1657 100.00 0.2039 . . 130 . . . . 'X-RAY DIFFRACTION' . 2.5049 2.6618 2621 0.1684 100.00 0.1906 . . 140 . . . . 'X-RAY DIFFRACTION' . 2.6618 2.8672 2635 0.1753 100.00 0.1923 . . 151 . . . . 'X-RAY DIFFRACTION' . 2.8672 3.1555 2626 0.1718 100.00 0.2275 . . 151 . . . . 'X-RAY DIFFRACTION' . 3.1555 3.6116 2661 0.1568 100.00 0.1707 . . 140 . . . . 'X-RAY DIFFRACTION' . 3.6116 4.5481 2676 0.1432 100.00 0.1506 . . 147 . . . . 'X-RAY DIFFRACTION' . 4.5481 32.1721 2789 0.1649 99.00 0.1675 . . 151 . . . . # _struct.entry_id 4MD5 _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 4MD5 _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'HLA-DR, Antigen presentation, T-cell receptor, Citrullination, Membrane, IMMUNE SYSTEM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 4 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 6 ? Q N N 7 ? R N N 7 ? S N N 7 ? # _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 LEU A 45 ? PHE A 51 ? LEU A 45 PHE A 51 5 ? 7 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 ? TYR B 80 ? GLN B 64 TYR B 78 1 ? 15 HELX_P HELX_P6 6 TYR B 80 ? GLU B 89 ? TYR B 78 GLU B 87 1 ? 10 HELX_P HELX_P7 7 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 ? ? ? ? ? ? ? 2.025 ? disulf2 disulf ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.085 ? disulf3 disulf ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.025 ? covale1 covale ? ? C LEU 5 C ? ? ? 1_555 C CIR 6 N2 ? ? C LEU 5 C CIR 6 1_555 ? ? ? ? ? ? ? 1.313 ? covale2 covale ? ? C CIR 6 C1 ? ? ? 1_555 C SER 7 N ? ? C CIR 6 C SER 7 1_555 ? ? ? ? ? ? ? 1.319 ? covale3 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 202 A NAG 203 1_555 ? ? ? ? ? ? ? 1.438 ? covale4 covale ? ? A ASN 118 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 118 A NAG 202 1_555 ? ? ? ? ? ? ? 1.440 ? covale5 covale ? ? B ASN 21 ND2 ? ? ? 1_555 L NAG . C1 ? ? B ASN 19 B NAG 201 1_555 ? ? ? ? ? ? ? 1.440 ? covale6 covale ? ? A ASN 78 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 78 A NAG 201 1_555 ? ? ? ? ? ? ? 1.441 ? covale7 covale ? ? A CYS 107 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107 A CYS 163 1_555 ? ? ? ? ? ? ? 2.025 ? covale8 covale ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.025 ? covale9 covale ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.085 ? # 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 3.38 2 THR 113 A . ? THR 113 A PRO 114 A ? PRO 114 A 1 0.61 3 TYR 125 B . ? TYR 123 B PRO 126 B ? PRO 124 B 1 1.88 4 ALA 192 B . ? ALA 190 B THR 193 B ? THR 191 B 1 3.72 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLU A 40 ? TRP A 43 ? GLU A 40 TRP A 43 A 2 ASP A 29 ? ASP A 35 ? ASP A 29 ASP A 35 A 3 SER A 19 ? PHE A 26 ? SER A 19 PHE A 26 A 4 HIS A 5 ? ASN A 15 ? HIS A 5 ASN A 15 A 5 PHE B 9 ? PHE B 20 ? PHE B 7 PHE B 18 A 6 ARG B 25 ? TYR B 34 ? ARG B 23 TYR B 32 A 7 GLU B 37 ? ASP B 43 ? GLU B 35 ASP B 41 A 8 TYR B 49 ? ALA B 51 ? TYR B 47 ALA B 49 B 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 B 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 B 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 B 4 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 C 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 C 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 C 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 C 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 D 1 LYS A 126 ? VAL A 128 ? LYS A 126 VAL A 128 D 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 D 3 VAL A 160 ? GLU A 166 ? VAL A 160 GLU A 166 D 4 LEU A 174 ? GLU A 179 ? LEU A 174 GLU A 179 E 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 E 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 E 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 E 4 VAL B 144 ? SER B 146 ? VAL B 142 SER B 144 F 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 F 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 F 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 F 4 ILE B 150 ? GLN B 151 ? ILE B 148 GLN B 149 G 1 GLN B 138 ? GLU B 140 ? GLN B 136 GLU B 138 G 2 GLU B 130 ? ARG B 135 ? GLU B 128 ARG B 133 G 3 VAL B 172 ? GLU B 178 ? VAL B 170 GLU B 176 G 4 LEU B 186 ? ARG B 191 ? LEU B 184 ARG B 189 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O VAL A 42 ? O VAL A 42 N HIS A 33 ? N HIS A 33 A 2 3 O ASP A 29 ? O ASP A 29 N PHE A 26 ? N PHE A 26 A 3 4 O ASP A 25 ? O ASP A 25 N ILE A 8 ? N ILE A 8 A 4 5 N HIS A 5 ? N HIS A 5 O PHE B 19 ? O PHE B 17 A 5 6 N GLU B 16 ? N GLU B 14 O LEU B 29 ? O LEU B 27 A 6 7 N ASP B 30 ? N ASP B 28 O PHE B 42 ? O PHE B 40 A 7 8 N ARG B 41 ? N ARG B 39 O ARG B 50 ? O ARG B 48 B 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 B 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 B 3 4 O TYR A 150 ? O TYR A 150 N SER A 133 ? N SER A 133 C 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 C 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 C 3 4 O ARG A 146 ? O ARG A 146 N LEU A 138 ? N LEU A 138 D 1 2 O LYS A 126 ? O LYS A 126 N ARG A 123 ? N ARG A 123 D 2 3 N THR A 120 ? N THR A 120 O ARG A 164 ? O ARG A 164 D 3 4 N TYR A 161 ? N TYR A 161 O TRP A 178 ? O TRP A 178 E 1 2 N THR B 102 ? N THR B 100 O SER B 120 ? O SER B 118 E 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 E 3 4 O MET B 162 ? O MET B 160 N VAL B 145 ? N VAL B 143 F 1 2 N 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 GLN B 158 ? O GLN B 156 N ILE B 150 ? N ILE B 148 G 1 2 O GLN B 138 ? O GLN B 136 N ARG B 135 ? N ARG B 133 G 2 3 N ARG B 132 ? N ARG B 130 O GLN B 176 ? O GLN B 174 G 3 4 N TYR B 173 ? N TYR B 171 O TRP B 190 ? O TRP B 188 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 204' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 205' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE EDO A 206' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE EDO A 207' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO A 208' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO B 202' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE EDO B 203' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO B 204' AC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PGE B 205' BC1 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A 201 BOUND TO ASN A 78' BC2 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 118 RESIDUES 202 TO 203' BC3 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 201 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 7 ARG A 44 ? ARG A 44 . ? 1_555 ? 2 AC1 7 GLU A 134 ? GLU A 134 . ? 1_555 ? 3 AC1 7 HOH Q . ? HOH A 310 . ? 1_555 ? 4 AC1 7 HOH Q . ? HOH A 344 . ? 1_555 ? 5 AC1 7 HOH Q . ? HOH A 366 . ? 1_555 ? 6 AC1 7 HOH Q . ? HOH A 420 . ? 1_555 ? 7 AC1 7 HOH Q . ? HOH A 438 . ? 1_555 ? 8 AC2 5 ARG A 140 ? ARG A 140 . ? 1_555 ? 9 AC2 5 GLU A 141 ? GLU A 141 . ? 1_555 ? 10 AC2 5 ASP A 142 ? ASP A 142 . ? 1_555 ? 11 AC2 5 ARG A 146 ? ARG A 146 . ? 1_555 ? 12 AC2 5 HOH Q . ? HOH A 472 . ? 1_555 ? 13 AC3 2 HIS A 33 ? HIS A 33 . ? 1_555 ? 14 AC3 2 HOH Q . ? HOH A 395 . ? 1_555 ? 15 AC4 3 ASP A 162 ? ASP A 162 . ? 1_555 ? 16 AC4 3 HIS A 177 ? HIS A 177 . ? 1_555 ? 17 AC4 3 HOH Q . ? HOH A 362 . ? 8_455 ? 18 AC5 6 VAL A 85 ? VAL A 85 . ? 1_555 ? 19 AC5 6 PRO A 86 ? PRO A 86 . ? 1_555 ? 20 AC5 6 HOH Q . ? HOH A 334 . ? 1_555 ? 21 AC5 6 HOH Q . ? HOH A 338 . ? 1_555 ? 22 AC5 6 HOH Q . ? HOH A 507 . ? 1_555 ? 23 AC5 6 HOH R . ? HOH B 418 . ? 3_654 ? 24 AC6 6 ASP B 78 ? ASP B 76 . ? 1_455 ? 25 AC6 6 ARG B 168 ? ARG B 166 . ? 1_555 ? 26 AC6 6 SER B 169 ? SER B 167 . ? 1_555 ? 27 AC6 6 HOH R . ? HOH B 469 . ? 1_455 ? 28 AC6 6 HOH R . ? HOH B 471 . ? 1_555 ? 29 AC6 6 ARG C 4 ? ARG C 4 . ? 1_455 ? 30 AC7 3 HIS B 179 ? HIS B 177 . ? 1_555 ? 31 AC7 3 PRO B 180 ? PRO B 178 . ? 1_555 ? 32 AC7 3 HOH R . ? HOH B 481 . ? 1_555 ? 33 AC8 4 TYR A 150 ? TYR A 150 . ? 1_555 ? 34 AC8 4 ASP B 154 ? ASP B 152 . ? 1_555 ? 35 AC8 4 HOH R . ? HOH B 324 . ? 1_555 ? 36 AC8 4 HOH R . ? HOH B 408 . ? 1_555 ? 37 AC9 7 SER B 44 ? SER B 42 . ? 3_654 ? 38 AC9 7 ASP B 45 ? ASP B 43 . ? 3_654 ? 39 AC9 7 SER B 146 ? SER B 144 . ? 1_555 ? 40 AC9 7 THR B 159 ? THR B 157 . ? 1_555 ? 41 AC9 7 HOH R . ? HOH B 311 . ? 3_654 ? 42 AC9 7 HOH R . ? HOH B 316 . ? 3_654 ? 43 AC9 7 HOH R . ? HOH B 448 . ? 1_555 ? 44 BC1 4 ARG A 76 ? ARG A 76 . ? 1_555 ? 45 BC1 4 ASN A 78 ? ASN A 78 . ? 1_555 ? 46 BC1 4 LYS A 126 ? LYS A 126 . ? 8_555 ? 47 BC1 4 HOH Q . ? HOH A 528 . ? 1_555 ? 48 BC2 8 ASN A 118 ? ASN A 118 . ? 1_555 ? 49 BC2 8 TRP A 168 ? TRP A 168 . ? 1_555 ? 50 BC2 8 HOH Q . ? HOH A 433 . ? 1_555 ? 51 BC2 8 HOH Q . ? HOH A 434 . ? 1_555 ? 52 BC2 8 HOH Q . ? HOH A 493 . ? 1_555 ? 53 BC2 8 HOH Q . ? HOH A 530 . ? 1_555 ? 54 BC2 8 ASP B 4 ? ASP B 2 . ? 1_555 ? 55 BC2 8 HOH R . ? HOH B 424 . ? 1_555 ? 56 BC3 2 ASN B 21 ? ASN B 19 . ? 1_555 ? 57 BC3 2 HOH R . ? HOH B 452 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MD5 _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 4MD5 _atom_sites.fract_transf_matrix[1][1] 0.014832 _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] 0.005464 _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] 0.012901 _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 ? 36.316 12.810 -18.882 1.00 47.89 ? 3 GLU A N 1 ATOM 2 C CA A GLU A 1 3 ? 37.055 12.547 -17.652 0.42 45.79 ? 3 GLU A CA 1 ATOM 3 C CA B GLU A 1 3 ? 37.063 12.516 -17.663 0.58 46.27 ? 3 GLU A CA 1 ATOM 4 C C . GLU A 1 3 ? 36.178 11.864 -16.609 1.00 45.18 ? 3 GLU A C 1 ATOM 5 O O . GLU A 1 3 ? 34.967 12.081 -16.570 1.00 53.75 ? 3 GLU A O 1 ATOM 6 C CB A GLU A 1 3 ? 37.652 13.841 -17.083 0.42 43.13 ? 3 GLU A CB 1 ATOM 7 C CB B GLU A 1 3 ? 37.702 13.785 -17.097 0.58 43.73 ? 3 GLU A CB 1 ATOM 8 C CG A GLU A 1 3 ? 36.925 15.117 -17.499 0.42 42.21 ? 3 GLU A CG 1 ATOM 9 C CG B GLU A 1 3 ? 36.711 14.736 -16.462 0.58 41.02 ? 3 GLU A CG 1 ATOM 10 C CD A GLU A 1 3 ? 37.380 15.641 -18.851 0.42 44.10 ? 3 GLU A CD 1 ATOM 11 C CD B GLU A 1 3 ? 37.080 16.186 -16.674 0.58 40.12 ? 3 GLU A CD 1 ATOM 12 O OE1 A GLU A 1 3 ? 38.507 16.176 -18.937 0.42 44.03 ? 3 GLU A OE1 1 ATOM 13 O OE1 B GLU A 1 3 ? 36.169 17.041 -16.637 0.58 36.99 ? 3 GLU A OE1 1 ATOM 14 O OE2 A GLU A 1 3 ? 36.614 15.514 -19.829 0.42 44.24 ? 3 GLU A OE2 1 ATOM 15 O OE2 B GLU A 1 3 ? 38.280 16.471 -16.877 0.58 23.56 ? 3 GLU A OE2 1 ATOM 16 N N . GLU A 1 4 ? 36.794 11.044 -15.767 1.00 42.81 ? 4 GLU A N 1 ATOM 17 C CA . GLU A 1 4 ? 36.071 10.378 -14.698 1.00 38.73 ? 4 GLU A CA 1 ATOM 18 C C . GLU A 1 4 ? 36.096 11.242 -13.449 1.00 24.95 ? 4 GLU A C 1 ATOM 19 O O . GLU A 1 4 ? 35.085 11.389 -12.771 1.00 26.63 ? 4 GLU A O 1 ATOM 20 C CB . GLU A 1 4 ? 36.685 9.017 -14.381 1.00 41.69 ? 4 GLU A CB 1 ATOM 21 C CG . GLU A 1 4 ? 36.464 7.961 -15.443 1.00 50.50 ? 4 GLU A CG 1 ATOM 22 C CD . GLU A 1 4 ? 36.957 6.600 -14.999 1.00 55.63 ? 4 GLU A CD 1 ATOM 23 O OE1 . GLU A 1 4 ? 37.650 6.534 -13.960 1.00 51.55 ? 4 GLU A OE1 1 ATOM 24 O OE2 . GLU A 1 4 ? 36.647 5.599 -15.681 1.00 59.83 ? 4 GLU A OE2 1 ATOM 25 N N . HIS A 1 5 ? 37.258 11.814 -13.149 1.00 18.00 ? 5 HIS A N 1 ATOM 26 C CA . HIS A 1 5 ? 37.418 12.600 -11.936 1.00 14.92 ? 5 HIS A CA 1 ATOM 27 C C . HIS A 1 5 ? 38.402 13.738 -12.109 1.00 13.60 ? 5 HIS A C 1 ATOM 28 O O . HIS A 1 5 ? 39.296 13.682 -12.951 1.00 13.75 ? 5 HIS A O 1 ATOM 29 C CB . HIS A 1 5 ? 37.897 11.713 -10.790 1.00 14.53 ? 5 HIS A CB 1 ATOM 30 C CG . HIS A 1 5 ? 36.968 10.588 -10.477 1.00 18.14 ? 5 HIS A CG 1 ATOM 31 N ND1 . HIS A 1 5 ? 35.721 10.797 -9.932 1.00 16.97 ? 5 HIS A ND1 1 ATOM 32 C CD2 . HIS A 1 5 ? 37.092 9.252 -10.646 1.00 19.00 ? 5 HIS A CD2 1 ATOM 33 C CE1 . HIS A 1 5 ? 35.114 9.634 -9.774 1.00 19.55 ? 5 HIS A CE1 1 ATOM 34 N NE2 . HIS A 1 5 ? 35.924 8.681 -10.197 1.00 20.73 ? 5 HIS A NE2 1 ATOM 35 N N . VAL A 1 6 ? 38.235 14.777 -11.301 1.00 12.13 ? 6 VAL A N 1 ATOM 36 C CA . VAL A 1 6 ? 39.180 15.887 -11.299 1.00 10.97 ? 6 VAL A CA 1 ATOM 37 C C . VAL A 1 6 ? 39.531 16.242 -9.865 1.00 12.44 ? 6 VAL A C 1 ATOM 38 O O . VAL A 1 6 ? 38.646 16.345 -9.015 1.00 14.11 ? 6 VAL A O 1 ATOM 39 C CB . VAL A 1 6 ? 38.593 17.124 -12.016 1.00 10.75 ? 6 VAL A CB 1 ATOM 40 C CG1 . VAL A 1 6 ? 39.585 18.269 -12.030 1.00 11.91 ? 6 VAL A CG1 1 ATOM 41 C CG2 . VAL A 1 6 ? 38.208 16.774 -13.445 1.00 16.85 ? 6 VAL A CG2 1 ATOM 42 N N . ILE A 1 7 ? 40.826 16.414 -9.594 1.00 9.60 ? 7 ILE A N 1 ATOM 43 C CA . ILE A 1 7 ? 41.270 16.872 -8.288 1.00 9.05 ? 7 ILE A CA 1 ATOM 44 C C . ILE A 1 7 ? 41.973 18.200 -8.492 1.00 9.64 ? 7 ILE A C 1 ATOM 45 O O . ILE A 1 7 ? 42.869 18.309 -9.329 1.00 9.43 ? 7 ILE A O 1 ATOM 46 C CB . ILE A 1 7 ? 42.243 15.872 -7.624 1.00 9.59 ? 7 ILE A CB 1 ATOM 47 C CG1 . ILE A 1 7 ? 41.559 14.525 -7.401 1.00 10.56 ? 7 ILE A CG1 1 ATOM 48 C CG2 . ILE A 1 7 ? 42.773 16.444 -6.310 1.00 9.49 ? 7 ILE A CG2 1 ATOM 49 C CD1 . ILE A 1 7 ? 42.501 13.455 -6.851 1.00 13.07 ? 7 ILE A CD1 1 ATOM 50 N N . ILE A 1 8 ? 41.540 19.221 -7.759 1.00 7.70 ? 8 ILE A N 1 ATOM 51 C CA . ILE A 1 8 ? 42.126 20.552 -7.917 1.00 7.05 ? 8 ILE A CA 1 ATOM 52 C C . ILE A 1 8 ? 42.638 21.077 -6.594 1.00 7.67 ? 8 ILE A C 1 ATOM 53 O O . ILE A 1 8 ? 41.942 21.042 -5.587 1.00 9.70 ? 8 ILE A O 1 ATOM 54 C CB . ILE A 1 8 ? 41.080 21.567 -8.474 1.00 7.76 ? 8 ILE A CB 1 ATOM 55 C CG1 . ILE A 1 8 ? 40.550 21.086 -9.828 1.00 8.80 ? 8 ILE A CG1 1 ATOM 56 C CG2 . ILE A 1 8 ? 41.709 22.966 -8.590 1.00 11.06 ? 8 ILE A CG2 1 ATOM 57 C CD1 . ILE A 1 8 ? 39.435 21.976 -10.418 1.00 9.69 ? 8 ILE A CD1 1 ATOM 58 N N . GLN A 1 9 ? 43.880 21.557 -6.606 1.00 6.85 ? 9 GLN A N 1 ATOM 59 C CA . GLN A 1 9 ? 44.436 22.319 -5.500 1.00 8.08 ? 9 GLN A CA 1 ATOM 60 C C . GLN A 1 9 ? 44.209 23.780 -5.871 1.00 8.45 ? 9 GLN A C 1 ATOM 61 O O . GLN A 1 9 ? 44.839 24.290 -6.792 1.00 7.13 ? 9 GLN A O 1 ATOM 62 C CB . GLN A 1 9 ? 45.933 22.011 -5.378 1.00 9.76 ? 9 GLN A CB 1 ATOM 63 C CG . GLN A 1 9 ? 46.700 22.867 -4.375 1.00 7.92 ? 9 GLN A CG 1 ATOM 64 C CD . GLN A 1 9 ? 48.195 22.602 -4.430 1.00 9.92 ? 9 GLN A CD 1 ATOM 65 O OE1 . GLN A 1 9 ? 48.629 21.465 -4.644 1.00 12.08 ? 9 GLN A OE1 1 ATOM 66 N NE2 . GLN A 1 9 ? 48.995 23.653 -4.225 1.00 10.99 ? 9 GLN A NE2 1 ATOM 67 N N . ALA A 1 10 ? 43.277 24.429 -5.176 1.00 6.63 ? 10 ALA A N 1 ATOM 68 C CA . ALA A 1 10 ? 42.873 25.794 -5.509 1.00 6.58 ? 10 ALA A CA 1 ATOM 69 C C . ALA A 1 10 ? 43.321 26.766 -4.435 1.00 8.64 ? 10 ALA A C 1 ATOM 70 O O . ALA A 1 10 ? 43.157 26.507 -3.244 1.00 10.09 ? 10 ALA A O 1 ATOM 71 C CB . ALA A 1 10 ? 41.352 25.877 -5.666 1.00 7.92 ? 10 ALA A CB 1 ATOM 72 N N . GLU A 1 11 ? 43.880 27.892 -4.866 1.00 6.86 ? 11 GLU A N 1 ATOM 73 C CA . GLU A 1 11 ? 44.414 28.879 -3.940 1.00 6.41 ? 11 GLU A CA 1 ATOM 74 C C . GLU A 1 11 ? 43.925 30.242 -4.367 1.00 6.83 ? 11 GLU A C 1 ATOM 75 O O . GLU A 1 11 ? 43.684 30.476 -5.550 1.00 8.06 ? 11 GLU A O 1 ATOM 76 C CB . GLU A 1 11 ? 45.942 28.906 -4.014 1.00 9.43 ? 11 GLU A CB 1 ATOM 77 C CG . GLU A 1 11 ? 46.613 27.580 -3.740 1.00 9.35 ? 11 GLU A CG 1 ATOM 78 C CD . GLU A 1 11 ? 48.048 27.533 -4.240 1.00 13.76 ? 11 GLU A CD 1 ATOM 79 O OE1 . GLU A 1 11 ? 48.674 28.604 -4.408 1.00 12.55 ? 11 GLU A OE1 1 ATOM 80 O OE2 . GLU A 1 11 ? 48.558 26.419 -4.453 1.00 12.76 ? 11 GLU A OE2 1 ATOM 81 N N . PHE A 1 12 ? 43.776 31.148 -3.408 1.00 7.32 ? 12 PHE A N 1 ATOM 82 C CA . PHE A 1 12 ? 43.618 32.554 -3.772 1.00 6.59 ? 12 PHE A CA 1 ATOM 83 C C . PHE A 1 12 ? 44.256 33.477 -2.758 1.00 9.44 ? 12 PHE A C 1 ATOM 84 O O . PHE A 1 12 ? 44.498 33.097 -1.617 1.00 9.29 ? 12 PHE A O 1 ATOM 85 C CB . PHE A 1 12 ? 42.148 32.948 -4.058 1.00 8.48 ? 12 PHE A CB 1 ATOM 86 C CG . PHE A 1 12 ? 41.252 33.019 -2.843 1.00 7.74 ? 12 PHE A CG 1 ATOM 87 C CD1 . PHE A 1 12 ? 41.309 34.102 -1.965 1.00 10.61 ? 12 PHE A CD1 1 ATOM 88 C CD2 . PHE A 1 12 ? 40.290 32.042 -2.624 1.00 11.94 ? 12 PHE A CD2 1 ATOM 89 C CE1 . PHE A 1 12 ? 40.459 34.181 -0.866 1.00 13.93 ? 12 PHE A CE1 1 ATOM 90 C CE2 . PHE A 1 12 ? 39.423 32.125 -1.530 1.00 12.44 ? 12 PHE A CE2 1 ATOM 91 C CZ . PHE A 1 12 ? 39.517 33.187 -0.648 1.00 12.77 ? 12 PHE A CZ 1 ATOM 92 N N . TYR A 1 13 ? 44.564 34.686 -3.207 1.00 7.60 ? 13 TYR A N 1 ATOM 93 C CA . TYR A 1 13 ? 44.975 35.747 -2.303 1.00 8.62 ? 13 TYR A CA 1 ATOM 94 C C . TYR A 1 13 ? 44.261 37.023 -2.738 1.00 8.56 ? 13 TYR A C 1 ATOM 95 O O . TYR A 1 13 ? 44.210 37.341 -3.930 1.00 9.67 ? 13 TYR A O 1 ATOM 96 C CB . TYR A 1 13 ? 46.498 35.934 -2.299 1.00 9.32 ? 13 TYR A CB 1 ATOM 97 C CG . TYR A 1 13 ? 46.953 36.841 -1.184 1.00 10.76 ? 13 TYR A CG 1 ATOM 98 C CD1 . TYR A 1 13 ? 47.253 36.330 0.072 1.00 13.52 ? 13 TYR A CD1 1 ATOM 99 C CD2 . TYR A 1 13 ? 47.052 38.211 -1.378 1.00 12.59 ? 13 TYR A CD2 1 ATOM 100 C CE1 . TYR A 1 13 ? 47.655 37.164 1.105 1.00 20.94 ? 13 TYR A CE1 1 ATOM 101 C CE2 . TYR A 1 13 ? 47.457 39.049 -0.356 1.00 18.25 ? 13 TYR A CE2 1 ATOM 102 C CZ . TYR A 1 13 ? 47.753 38.517 0.883 1.00 20.08 ? 13 TYR A CZ 1 ATOM 103 O OH . TYR A 1 13 ? 48.156 39.351 1.903 1.00 22.85 ? 13 TYR A OH 1 ATOM 104 N N . LEU A 1 14 ? 43.703 37.741 -1.769 1.00 9.37 ? 14 LEU A N 1 ATOM 105 C CA . LEU A 1 14 ? 42.885 38.913 -2.048 1.00 9.52 ? 14 LEU A CA 1 ATOM 106 C C . LEU A 1 14 ? 43.408 40.137 -1.310 1.00 10.80 ? 14 LEU A C 1 ATOM 107 O O . LEU A 1 14 ? 43.588 40.103 -0.097 1.00 11.88 ? 14 LEU A O 1 ATOM 108 C CB . LEU A 1 14 ? 41.447 38.642 -1.599 1.00 9.57 ? 14 LEU A CB 1 ATOM 109 C CG . LEU A 1 14 ? 40.458 39.798 -1.748 1.00 11.60 ? 14 LEU A CG 1 ATOM 110 C CD1 . LEU A 1 14 ? 40.148 40.034 -3.212 1.00 11.20 ? 14 LEU A CD1 1 ATOM 111 C CD2 . LEU A 1 14 ? 39.200 39.480 -0.978 1.00 11.48 ? 14 LEU A CD2 1 ATOM 112 N N . ASN A 1 15 ? 43.638 41.215 -2.057 1.00 10.89 ? 15 ASN A N 1 ATOM 113 C CA . ASN A 1 15 ? 43.974 42.515 -1.485 1.00 12.22 ? 15 ASN A CA 1 ATOM 114 C C . ASN A 1 15 ? 42.779 43.442 -1.625 1.00 12.45 ? 15 ASN A C 1 ATOM 115 O O . ASN A 1 15 ? 42.026 43.328 -2.587 1.00 13.09 ? 15 ASN A O 1 ATOM 116 C CB . ASN A 1 15 ? 45.155 43.136 -2.225 1.00 14.15 ? 15 ASN A CB 1 ATOM 117 C CG . ASN A 1 15 ? 46.491 42.704 -1.665 1.00 21.10 ? 15 ASN A CG 1 ATOM 118 O OD1 . ASN A 1 15 ? 46.622 42.431 -0.467 1.00 18.46 ? 15 ASN A OD1 1 ATOM 119 N ND2 . ASN A 1 15 ? 47.504 42.662 -2.530 1.00 16.41 ? 15 ASN A ND2 1 ATOM 120 N N . PRO A 1 16 ? 42.624 44.399 -0.699 1.00 13.86 ? 16 PRO A N 1 ATOM 121 C CA . PRO A 1 16 ? 43.519 44.714 0.421 1.00 15.35 ? 16 PRO A CA 1 ATOM 122 C C . PRO A 1 16 ? 43.224 43.916 1.687 1.00 16.53 ? 16 PRO A C 1 ATOM 123 O O . PRO A 1 16 ? 43.849 44.161 2.726 1.00 17.65 ? 16 PRO A O 1 ATOM 124 C CB . PRO A 1 16 ? 43.231 46.196 0.666 1.00 16.70 ? 16 PRO A CB 1 ATOM 125 C CG . PRO A 1 16 ? 41.773 46.325 0.331 1.00 16.20 ? 16 PRO A CG 1 ATOM 126 C CD . PRO A 1 16 ? 41.574 45.421 -0.864 1.00 14.36 ? 16 PRO A CD 1 ATOM 127 N N . ASP A 1 17 ? 42.293 42.971 1.595 1.00 15.06 ? 17 ASP A N 1 ATOM 128 C CA . ASP A 1 17 ? 41.843 42.214 2.757 1.00 15.85 ? 17 ASP A CA 1 ATOM 129 C C . ASP A 1 17 ? 42.955 41.357 3.352 1.00 17.27 ? 17 ASP A C 1 ATOM 130 O O . ASP A 1 17 ? 42.921 41.022 4.535 1.00 19.61 ? 17 ASP A O 1 ATOM 131 C CB . ASP A 1 17 ? 40.634 41.343 2.383 1.00 14.75 ? 17 ASP A CB 1 ATOM 132 C CG . ASP A 1 17 ? 39.519 42.150 1.749 1.00 19.04 ? 17 ASP A CG 1 ATOM 133 O OD1 . ASP A 1 17 ? 38.512 42.431 2.436 1.00 24.39 ? 17 ASP A OD1 1 ATOM 134 O OD2 . ASP A 1 17 ? 39.669 42.533 0.572 1.00 15.70 ? 17 ASP A OD2 1 ATOM 135 N N . GLN A 1 18 ? 43.943 41.034 2.524 1.00 15.35 ? 18 GLN A N 1 ATOM 136 C CA . GLN A 1 18 ? 45.036 40.138 2.899 1.00 15.73 ? 18 GLN A CA 1 ATOM 137 C C . GLN A 1 18 ? 44.501 38.783 3.334 1.00 20.10 ? 18 GLN A C 1 ATOM 138 O O . GLN A 1 18 ? 44.968 38.196 4.311 1.00 21.99 ? 18 GLN A O 1 ATOM 139 C CB . GLN A 1 18 ? 45.927 40.764 3.980 1.00 17.99 ? 18 GLN A CB 1 ATOM 140 C CG . GLN A 1 18 ? 46.583 42.057 3.526 1.00 18.94 ? 18 GLN A CG 1 ATOM 141 C CD . GLN A 1 18 ? 47.684 42.508 4.456 1.00 32.45 ? 18 GLN A CD 1 ATOM 142 O OE1 . GLN A 1 18 ? 47.429 42.906 5.591 1.00 38.09 ? 18 GLN A OE1 1 ATOM 143 N NE2 . GLN A 1 18 ? 48.919 42.450 3.978 1.00 35.71 ? 18 GLN A NE2 1 ATOM 144 N N . SER A 1 19 ? 43.504 38.294 2.604 1.00 14.88 ? 19 SER A N 1 ATOM 145 C CA . SER A 1 19 ? 42.984 36.960 2.861 1.00 18.10 ? 19 SER A CA 1 ATOM 146 C C . SER A 1 19 ? 43.535 35.981 1.832 1.00 15.29 ? 19 SER A C 1 ATOM 147 O O . SER A 1 19 ? 43.515 36.241 0.630 1.00 14.51 ? 19 SER A O 1 ATOM 148 C CB . SER A 1 19 ? 41.451 36.949 2.875 1.00 31.72 ? 19 SER A CB 1 ATOM 149 O OG . SER A 1 19 ? 40.915 37.508 1.692 1.00 40.84 ? 19 SER A OG 1 ATOM 150 N N . GLY A 1 20 ? 44.041 34.853 2.311 1.00 17.35 ? 20 GLY A N 1 ATOM 151 C CA . GLY A 1 20 ? 44.538 33.823 1.417 1.00 19.21 ? 20 GLY A CA 1 ATOM 152 C C . GLY A 1 20 ? 43.986 32.480 1.833 1.00 27.00 ? 20 GLY A C 1 ATOM 153 O O . GLY A 1 20 ? 43.927 32.182 3.023 1.00 33.19 ? 20 GLY A O 1 ATOM 154 N N A GLU A 1 21 ? 43.568 31.665 0.874 0.42 16.10 ? 21 GLU A N 1 ATOM 155 N N B GLU A 1 21 ? 43.591 31.674 0.846 0.58 15.44 ? 21 GLU A N 1 ATOM 156 C CA A GLU A 1 21 ? 43.045 30.351 1.219 0.42 12.07 ? 21 GLU A CA 1 ATOM 157 C CA B GLU A 1 21 ? 42.968 30.374 1.086 0.58 13.14 ? 21 GLU A CA 1 ATOM 158 C C A GLU A 1 21 ? 43.610 29.265 0.307 0.42 12.23 ? 21 GLU A C 1 ATOM 159 C C B GLU A 1 21 ? 43.677 29.268 0.300 0.58 9.27 ? 21 GLU A C 1 ATOM 160 O O A GLU A 1 21 ? 44.009 29.530 -0.825 0.42 8.36 ? 21 GLU A O 1 ATOM 161 O O B GLU A 1 21 ? 44.242 29.520 -0.763 0.58 12.88 ? 21 GLU A O 1 ATOM 162 C CB A GLU A 1 21 ? 41.514 30.349 1.206 0.42 20.75 ? 21 GLU A CB 1 ATOM 163 C CB B GLU A 1 21 ? 41.488 30.418 0.688 0.58 14.49 ? 21 GLU A CB 1 ATOM 164 C CG A GLU A 1 21 ? 40.873 31.483 2.007 0.42 17.11 ? 21 GLU A CG 1 ATOM 165 C CG B GLU A 1 21 ? 40.736 29.126 0.976 0.58 16.16 ? 21 GLU A CG 1 ATOM 166 C CD A GLU A 1 21 ? 41.189 31.449 3.501 0.42 23.64 ? 21 GLU A CD 1 ATOM 167 C CD B GLU A 1 21 ? 39.295 29.154 0.520 0.58 11.45 ? 21 GLU A CD 1 ATOM 168 O OE1 A GLU A 1 21 ? 41.442 30.358 4.052 0.42 13.24 ? 21 GLU A OE1 1 ATOM 169 O OE1 B GLU A 1 21 ? 38.987 28.414 -0.434 0.58 12.51 ? 21 GLU A OE1 1 ATOM 170 O OE2 A GLU A 1 21 ? 41.182 32.529 4.130 0.42 31.15 ? 21 GLU A OE2 1 ATOM 171 O OE2 B GLU A 1 21 ? 38.487 29.897 1.121 0.58 10.00 ? 21 GLU A OE2 1 ATOM 172 N N . PHE A 1 22 ? 43.646 28.046 0.828 1.00 11.04 ? 22 PHE A N 1 ATOM 173 C CA . PHE A 1 22 ? 44.274 26.911 0.163 1.00 11.39 ? 22 PHE A CA 1 ATOM 174 C C . PHE A 1 22 ? 43.379 25.716 0.439 1.00 9.66 ? 22 PHE A C 1 ATOM 175 O O . PHE A 1 22 ? 43.084 25.431 1.593 1.00 12.68 ? 22 PHE A O 1 ATOM 176 C CB . PHE A 1 22 ? 45.657 26.674 0.786 1.00 10.53 ? 22 PHE A CB 1 ATOM 177 C CG . PHE A 1 22 ? 46.425 25.510 0.196 1.00 13.81 ? 22 PHE A CG 1 ATOM 178 C CD1 . PHE A 1 22 ? 47.492 25.733 -0.659 1.00 11.64 ? 22 PHE A CD1 1 ATOM 179 C CD2 . PHE A 1 22 ? 46.111 24.200 0.533 1.00 12.31 ? 22 PHE A CD2 1 ATOM 180 C CE1 . PHE A 1 22 ? 48.217 24.670 -1.190 1.00 12.80 ? 22 PHE A CE1 1 ATOM 181 C CE2 . PHE A 1 22 ? 46.828 23.129 -0.003 1.00 13.21 ? 22 PHE A CE2 1 ATOM 182 C CZ . PHE A 1 22 ? 47.885 23.371 -0.859 1.00 13.38 ? 22 PHE A CZ 1 ATOM 183 N N . MET A 1 23 ? 42.942 25.025 -0.610 1.00 8.69 ? 23 MET A N 1 ATOM 184 C CA A MET A 1 23 ? 42.052 23.871 -0.456 0.81 9.21 ? 23 MET A CA 1 ATOM 185 C CA B MET A 1 23 ? 42.084 23.857 -0.441 0.19 9.88 ? 23 MET A CA 1 ATOM 186 C C . MET A 1 23 ? 42.255 22.867 -1.586 1.00 10.33 ? 23 MET A C 1 ATOM 187 O O . MET A 1 23 ? 42.809 23.206 -2.635 1.00 10.12 ? 23 MET A O 1 ATOM 188 C CB A MET A 1 23 ? 40.576 24.317 -0.401 0.81 9.38 ? 23 MET A CB 1 ATOM 189 C CB B MET A 1 23 ? 40.620 24.280 -0.346 0.19 9.76 ? 23 MET A CB 1 ATOM 190 C CG A MET A 1 23 ? 40.057 24.961 -1.695 0.81 9.31 ? 23 MET A CG 1 ATOM 191 C CG B MET A 1 23 ? 40.126 25.032 -1.568 0.19 9.69 ? 23 MET A CG 1 ATOM 192 S SD A MET A 1 23 ? 39.386 23.818 -2.931 0.81 9.45 ? 23 MET A SD 1 ATOM 193 S SD B MET A 1 23 ? 38.332 25.123 -1.623 0.19 16.62 ? 23 MET A SD 1 ATOM 194 C CE A MET A 1 23 ? 37.912 23.232 -2.096 0.81 13.09 ? 23 MET A CE 1 ATOM 195 C CE B MET A 1 23 ? 37.913 23.391 -1.805 0.19 14.11 ? 23 MET A CE 1 ATOM 196 N N . PHE A 1 24 ? 41.814 21.628 -1.360 1.00 9.36 ? 24 PHE A N 1 ATOM 197 C CA . PHE A 1 24 ? 41.762 20.614 -2.411 1.00 10.51 ? 24 PHE A CA 1 ATOM 198 C C . PHE A 1 24 ? 40.299 20.267 -2.665 1.00 10.44 ? 24 PHE A C 1 ATOM 199 O O . PHE A 1 24 ? 39.509 20.135 -1.722 1.00 10.90 ? 24 PHE A O 1 ATOM 200 C CB . PHE A 1 24 ? 42.504 19.336 -1.989 1.00 10.75 ? 24 PHE A CB 1 ATOM 201 C CG . PHE A 1 24 ? 43.946 19.280 -2.418 1.00 13.98 ? 24 PHE A CG 1 ATOM 202 C CD1 . PHE A 1 24 ? 44.344 18.428 -3.435 1.00 13.24 ? 24 PHE A CD1 1 ATOM 203 C CD2 . PHE A 1 24 ? 44.906 20.057 -1.790 1.00 14.40 ? 24 PHE A CD2 1 ATOM 204 C CE1 . PHE A 1 24 ? 45.687 18.351 -3.818 1.00 12.17 ? 24 PHE A CE1 1 ATOM 205 C CE2 . PHE A 1 24 ? 46.244 19.981 -2.167 1.00 13.43 ? 24 PHE A CE2 1 ATOM 206 C CZ . PHE A 1 24 ? 46.629 19.129 -3.181 1.00 12.90 ? 24 PHE A CZ 1 ATOM 207 N N . ASP A 1 25 ? 39.955 20.117 -3.940 1.00 9.74 ? 25 ASP A N 1 ATOM 208 C CA . ASP A 1 25 ? 38.585 19.831 -4.384 1.00 9.68 ? 25 ASP A CA 1 ATOM 209 C C . ASP A 1 25 ? 38.600 18.529 -5.179 1.00 10.40 ? 25 ASP A C 1 ATOM 210 O O . ASP A 1 25 ? 39.511 18.294 -5.979 1.00 11.10 ? 25 ASP A O 1 ATOM 211 C CB . ASP A 1 25 ? 38.107 20.983 -5.279 1.00 9.80 ? 25 ASP A CB 1 ATOM 212 C CG . ASP A 1 25 ? 36.714 20.765 -5.859 1.00 19.44 ? 25 ASP A CG 1 ATOM 213 O OD1 . ASP A 1 25 ? 35.761 21.426 -5.382 1.00 21.99 ? 25 ASP A OD1 1 ATOM 214 O OD2 . ASP A 1 25 ? 36.566 19.960 -6.806 1.00 19.10 ? 25 ASP A OD2 1 ATOM 215 N N . PHE A 1 26 ? 37.609 17.675 -4.936 1.00 9.87 ? 26 PHE A N 1 ATOM 216 C CA . PHE A 1 26 ? 37.418 16.458 -5.717 1.00 10.52 ? 26 PHE A CA 1 ATOM 217 C C . PHE A 1 26 ? 36.021 16.525 -6.318 1.00 11.13 ? 26 PHE A C 1 ATOM 218 O O . PHE A 1 26 ? 35.037 16.492 -5.583 1.00 11.84 ? 26 PHE A O 1 ATOM 219 C CB . PHE A 1 26 ? 37.522 15.221 -4.812 1.00 11.62 ? 26 PHE A CB 1 ATOM 220 C CG . PHE A 1 26 ? 37.205 13.925 -5.513 1.00 12.58 ? 26 PHE A CG 1 ATOM 221 C CD1 . PHE A 1 26 ? 38.187 13.246 -6.213 1.00 14.74 ? 26 PHE A CD1 1 ATOM 222 C CD2 . PHE A 1 26 ? 35.925 13.391 -5.471 1.00 14.80 ? 26 PHE A CD2 1 ATOM 223 C CE1 . PHE A 1 26 ? 37.900 12.055 -6.861 1.00 15.57 ? 26 PHE A CE1 1 ATOM 224 C CE2 . PHE A 1 26 ? 35.628 12.200 -6.119 1.00 15.94 ? 26 PHE A CE2 1 ATOM 225 C CZ . PHE A 1 26 ? 36.625 11.536 -6.818 1.00 15.17 ? 26 PHE A CZ 1 ATOM 226 N N . ASP A 1 27 ? 35.934 16.615 -7.642 1.00 11.58 ? 27 ASP A N 1 ATOM 227 C CA . ASP A 1 27 ? 34.634 16.621 -8.336 1.00 11.68 ? 27 ASP A CA 1 ATOM 228 C C . ASP A 1 27 ? 33.636 17.635 -7.771 1.00 14.32 ? 27 ASP A C 1 ATOM 229 O O . ASP A 1 27 ? 32.424 17.383 -7.761 1.00 16.31 ? 27 ASP A O 1 ATOM 230 C CB . ASP A 1 27 ? 34.011 15.213 -8.333 1.00 11.41 ? 27 ASP A CB 1 ATOM 231 C CG . ASP A 1 27 ? 34.751 14.226 -9.238 1.00 17.61 ? 27 ASP A CG 1 ATOM 232 O OD1 . ASP A 1 27 ? 35.695 14.635 -9.954 1.00 19.12 ? 27 ASP A OD1 1 ATOM 233 O OD2 . ASP A 1 27 ? 34.378 13.038 -9.236 1.00 16.05 ? 27 ASP A OD2 1 ATOM 234 N N . GLY A 1 28 ? 34.132 18.768 -7.283 1.00 14.91 ? 28 GLY A N 1 ATOM 235 C CA . GLY A 1 28 ? 33.252 19.812 -6.770 1.00 11.83 ? 28 GLY A CA 1 ATOM 236 C C . GLY A 1 28 ? 32.995 19.793 -5.270 1.00 17.81 ? 28 GLY A C 1 ATOM 237 O O . GLY A 1 28 ? 32.307 20.670 -4.744 1.00 18.20 ? 28 GLY A O 1 ATOM 238 N N . ASP A 1 29 ? 33.526 18.790 -4.575 1.00 11.14 ? 29 ASP A N 1 ATOM 239 C CA . ASP A 1 29 ? 33.447 18.758 -3.115 1.00 9.88 ? 29 ASP A CA 1 ATOM 240 C C . ASP A 1 29 ? 34.811 18.996 -2.479 1.00 11.65 ? 29 ASP A C 1 ATOM 241 O O . ASP A 1 29 ? 35.844 18.622 -3.032 1.00 12.37 ? 29 ASP A O 1 ATOM 242 C CB . ASP A 1 29 ? 32.868 17.435 -2.610 1.00 11.99 ? 29 ASP A CB 1 ATOM 243 C CG . ASP A 1 29 ? 31.362 17.397 -2.680 1.00 19.13 ? 29 ASP A CG 1 ATOM 244 O OD1 . ASP A 1 29 ? 30.700 18.126 -1.898 1.00 20.90 ? 29 ASP A OD1 1 ATOM 245 O OD2 . ASP A 1 29 ? 30.836 16.623 -3.501 1.00 14.05 ? 29 ASP A OD2 1 ATOM 246 N N . GLU A 1 30 ? 34.816 19.606 -1.302 1.00 11.19 ? 30 GLU A N 1 ATOM 247 C CA . GLU A 1 30 ? 36.080 19.939 -0.649 1.00 9.51 ? 30 GLU A CA 1 ATOM 248 C C . GLU A 1 30 ? 36.684 18.741 0.073 1.00 10.43 ? 30 GLU A C 1 ATOM 249 O O . GLU A 1 30 ? 36.034 18.139 0.915 1.00 11.54 ? 30 GLU A O 1 ATOM 250 C CB . GLU A 1 30 ? 35.857 21.075 0.353 1.00 10.94 ? 30 GLU A CB 1 ATOM 251 C CG . GLU A 1 30 ? 37.070 21.377 1.230 1.00 12.10 ? 30 GLU A CG 1 ATOM 252 C CD . GLU A 1 30 ? 36.737 22.292 2.389 1.00 18.49 ? 30 GLU A CD 1 ATOM 253 O OE1 . GLU A 1 30 ? 35.600 22.809 2.437 1.00 18.00 ? 30 GLU A OE1 1 ATOM 254 O OE2 . GLU A 1 30 ? 37.605 22.483 3.265 1.00 18.39 ? 30 GLU A OE2 1 ATOM 255 N N . ILE A 1 31 ? 37.929 18.392 -0.234 1.00 10.22 ? 31 ILE A N 1 ATOM 256 C CA . ILE A 1 31 ? 38.591 17.342 0.540 1.00 11.35 ? 31 ILE A CA 1 ATOM 257 C C . ILE A 1 31 ? 39.066 17.913 1.872 1.00 12.84 ? 31 ILE A C 1 ATOM 258 O O . ILE A 1 31 ? 38.779 17.369 2.944 1.00 13.52 ? 31 ILE A O 1 ATOM 259 C CB . ILE A 1 31 ? 39.796 16.743 -0.203 1.00 11.29 ? 31 ILE A CB 1 ATOM 260 C CG1 . ILE A 1 31 ? 39.383 16.237 -1.591 1.00 13.61 ? 31 ILE A CG1 1 ATOM 261 C CG2 . ILE A 1 31 ? 40.421 15.621 0.621 1.00 14.19 ? 31 ILE A CG2 1 ATOM 262 C CD1 . ILE A 1 31 ? 40.549 15.664 -2.407 1.00 12.29 ? 31 ILE A CD1 1 ATOM 263 N N . PHE A 1 32 ? 39.800 19.015 1.791 1.00 11.34 ? 32 PHE A N 1 ATOM 264 C CA . PHE A 1 32 ? 40.263 19.717 2.978 1.00 12.10 ? 32 PHE A CA 1 ATOM 265 C C . PHE A 1 32 ? 40.633 21.144 2.626 1.00 12.22 ? 32 PHE A C 1 ATOM 266 O O . PHE A 1 32 ? 40.778 21.483 1.455 1.00 10.47 ? 32 PHE A O 1 ATOM 267 C CB . PHE A 1 32 ? 41.463 19.000 3.623 1.00 13.22 ? 32 PHE A CB 1 ATOM 268 C CG . PHE A 1 32 ? 42.739 19.071 2.818 1.00 13.40 ? 32 PHE A CG 1 ATOM 269 C CD1 . PHE A 1 32 ? 43.630 20.122 2.994 1.00 14.07 ? 32 PHE A CD1 1 ATOM 270 C CD2 . PHE A 1 32 ? 43.063 18.070 1.911 1.00 17.00 ? 32 PHE A CD2 1 ATOM 271 C CE1 . PHE A 1 32 ? 44.811 20.192 2.263 1.00 17.01 ? 32 PHE A CE1 1 ATOM 272 C CE2 . PHE A 1 32 ? 44.247 18.130 1.171 1.00 15.01 ? 32 PHE A CE2 1 ATOM 273 C CZ . PHE A 1 32 ? 45.121 19.191 1.352 1.00 14.56 ? 32 PHE A CZ 1 ATOM 274 N N . HIS A 1 33 ? 40.778 21.980 3.644 1.00 12.16 ? 33 HIS A N 1 ATOM 275 C CA . HIS A 1 33 ? 41.439 23.265 3.459 1.00 12.82 ? 33 HIS A CA 1 ATOM 276 C C . HIS A 1 33 ? 42.442 23.444 4.587 1.00 14.74 ? 33 HIS A C 1 ATOM 277 O O . HIS A 1 33 ? 42.456 22.670 5.549 1.00 16.31 ? 33 HIS A O 1 ATOM 278 C CB . HIS A 1 33 ? 40.433 24.424 3.432 1.00 14.05 ? 33 HIS A CB 1 ATOM 279 C CG . HIS A 1 33 ? 39.777 24.691 4.751 1.00 14.47 ? 33 HIS A CG 1 ATOM 280 N ND1 . HIS A 1 33 ? 38.609 24.068 5.138 1.00 13.71 ? 33 HIS A ND1 1 ATOM 281 C CD2 . HIS A 1 33 ? 40.124 25.510 5.771 1.00 14.43 ? 33 HIS A CD2 1 ATOM 282 C CE1 . HIS A 1 33 ? 38.265 24.494 6.340 1.00 14.89 ? 33 HIS A CE1 1 ATOM 283 N NE2 . HIS A 1 33 ? 39.167 25.368 6.749 1.00 17.82 ? 33 HIS A NE2 1 ATOM 284 N N . VAL A 1 34 ? 43.290 24.454 4.465 1.00 14.36 ? 34 VAL A N 1 ATOM 285 C CA . VAL A 1 34 ? 44.236 24.769 5.525 1.00 15.36 ? 34 VAL A CA 1 ATOM 286 C C . VAL A 1 34 ? 43.791 26.030 6.251 1.00 17.16 ? 34 VAL A C 1 ATOM 287 O O . VAL A 1 34 ? 43.562 27.067 5.626 1.00 19.70 ? 34 VAL A O 1 ATOM 288 C CB . VAL A 1 34 ? 45.659 24.955 4.970 1.00 15.58 ? 34 VAL A CB 1 ATOM 289 C CG1 . VAL A 1 34 ? 46.580 25.522 6.044 1.00 19.45 ? 34 VAL A CG1 1 ATOM 290 C CG2 . VAL A 1 34 ? 46.191 23.618 4.456 1.00 17.72 ? 34 VAL A CG2 1 ATOM 291 N N . ASP A 1 35 ? 43.625 25.911 7.564 1.00 17.88 ? 35 ASP A N 1 ATOM 292 C CA . ASP A 1 35 ? 43.377 27.051 8.430 1.00 20.96 ? 35 ASP A CA 1 ATOM 293 C C . ASP A 1 35 ? 44.690 27.813 8.504 1.00 25.91 ? 35 ASP A C 1 ATOM 294 O O . ASP A 1 35 ? 45.628 27.371 9.162 1.00 26.32 ? 35 ASP A O 1 ATOM 295 C CB . ASP A 1 35 ? 42.949 26.558 9.819 1.00 24.35 ? 35 ASP A CB 1 ATOM 296 C CG . ASP A 1 35 ? 42.540 27.687 10.754 1.00 33.27 ? 35 ASP A CG 1 ATOM 297 O OD1 . ASP A 1 35 ? 43.077 28.805 10.637 1.00 28.86 ? 35 ASP A OD1 1 ATOM 298 O OD2 . ASP A 1 35 ? 41.676 27.449 11.624 1.00 47.01 ? 35 ASP A OD2 1 ATOM 299 N N . MET A 1 36 ? 44.764 28.948 7.816 1.00 24.40 ? 36 MET A N 1 ATOM 300 C CA . MET A 1 36 ? 46.037 29.651 7.673 1.00 32.33 ? 36 MET A CA 1 ATOM 301 C C . MET A 1 36 ? 46.529 30.227 9.002 1.00 34.32 ? 36 MET A C 1 ATOM 302 O O . MET A 1 36 ? 47.722 30.190 9.298 1.00 36.15 ? 36 MET A O 1 ATOM 303 C CB . MET A 1 36 ? 45.943 30.747 6.609 1.00 30.16 ? 36 MET A CB 1 ATOM 304 C CG . MET A 1 36 ? 45.449 30.273 5.238 1.00 29.01 ? 36 MET A CG 1 ATOM 305 S SD . MET A 1 36 ? 46.419 28.962 4.454 1.00 36.75 ? 36 MET A SD 1 ATOM 306 C CE . MET A 1 36 ? 48.023 29.740 4.353 1.00 39.78 ? 36 MET A CE 1 ATOM 307 N N . ALA A 1 37 ? 45.603 30.751 9.799 1.00 29.32 ? 37 ALA A N 1 ATOM 308 C CA . ALA A 1 37 ? 45.946 31.345 11.088 1.00 33.81 ? 37 ALA A CA 1 ATOM 309 C C . ALA A 1 37 ? 46.439 30.303 12.092 1.00 34.85 ? 37 ALA A C 1 ATOM 310 O O . ALA A 1 37 ? 47.374 30.554 12.856 1.00 32.95 ? 37 ALA A O 1 ATOM 311 C CB . ALA A 1 37 ? 44.753 32.101 11.652 1.00 36.19 ? 37 ALA A CB 1 ATOM 312 N N . LYS A 1 38 ? 45.804 29.136 12.093 1.00 29.83 ? 38 LYS A N 1 ATOM 313 C CA . LYS A 1 38 ? 46.186 28.071 13.012 1.00 30.54 ? 38 LYS A CA 1 ATOM 314 C C . LYS A 1 38 ? 47.254 27.159 12.422 1.00 30.72 ? 38 LYS A C 1 ATOM 315 O O . LYS A 1 38 ? 47.843 26.346 13.136 1.00 34.03 ? 38 LYS A O 1 ATOM 316 C CB . LYS A 1 38 ? 44.966 27.244 13.423 1.00 36.97 ? 38 LYS A CB 1 ATOM 317 C CG . LYS A 1 38 ? 43.962 27.998 14.278 1.00 38.72 ? 38 LYS A CG 1 ATOM 318 C CD . LYS A 1 38 ? 42.940 27.049 14.884 1.00 49.19 ? 38 LYS A CD 1 ATOM 319 C CE . LYS A 1 38 ? 41.932 27.802 15.737 1.00 55.79 ? 38 LYS A CE 1 ATOM 320 N NZ . LYS A 1 38 ? 41.115 26.883 16.577 1.00 61.74 ? 38 LYS A NZ 1 ATOM 321 N N . LYS A 1 39 ? 47.500 27.307 11.122 1.00 26.52 ? 39 LYS A N 1 ATOM 322 C CA . LYS A 1 39 ? 48.433 26.446 10.399 1.00 27.21 ? 39 LYS A CA 1 ATOM 323 C C . LYS A 1 39 ? 48.073 24.974 10.583 1.00 26.56 ? 39 LYS A C 1 ATOM 324 O O . LYS A 1 39 ? 48.930 24.159 10.909 1.00 29.27 ? 39 LYS A O 1 ATOM 325 C CB . LYS A 1 39 ? 49.875 26.704 10.846 1.00 33.45 ? 39 LYS A CB 1 ATOM 326 C CG . LYS A 1 39 ? 50.332 28.144 10.674 1.00 39.53 ? 39 LYS A CG 1 ATOM 327 C CD . LYS A 1 39 ? 51.580 28.427 11.495 1.00 55.71 ? 39 LYS A CD 1 ATOM 328 C CE . LYS A 1 39 ? 52.089 29.843 11.263 1.00 63.39 ? 39 LYS A CE 1 ATOM 329 N NZ . LYS A 1 39 ? 51.027 30.866 11.470 1.00 62.09 ? 39 LYS A NZ 1 ATOM 330 N N . GLU A 1 40 ? 46.799 24.641 10.381 1.00 28.62 ? 40 GLU A N 1 ATOM 331 C CA A GLU A 1 40 ? 46.321 23.269 10.551 0.54 27.05 ? 40 GLU A CA 1 ATOM 332 C CA B GLU A 1 40 ? 46.354 23.260 10.531 0.46 27.07 ? 40 GLU A CA 1 ATOM 333 C C . GLU A 1 40 ? 45.492 22.807 9.356 1.00 21.96 ? 40 GLU A C 1 ATOM 334 O O . GLU A 1 40 ? 44.778 23.603 8.745 1.00 21.33 ? 40 GLU A O 1 ATOM 335 C CB A GLU A 1 40 ? 45.484 23.142 11.826 0.54 28.30 ? 40 GLU A CB 1 ATOM 336 C CB B GLU A 1 40 ? 45.607 23.063 11.855 0.46 28.39 ? 40 GLU A CB 1 ATOM 337 C CG A GLU A 1 40 ? 46.275 23.230 13.119 0.54 33.24 ? 40 GLU A CG 1 ATOM 338 C CG B GLU A 1 40 ? 44.191 23.614 11.876 0.46 27.42 ? 40 GLU A CG 1 ATOM 339 C CD A GLU A 1 40 ? 45.395 23.092 14.347 0.54 39.79 ? 40 GLU A CD 1 ATOM 340 C CD B GLU A 1 40 ? 43.498 23.379 13.206 0.46 34.24 ? 40 GLU A CD 1 ATOM 341 O OE1 A GLU A 1 40 ? 44.166 22.939 14.182 0.54 42.96 ? 40 GLU A OE1 1 ATOM 342 O OE1 B GLU A 1 40 ? 44.183 23.430 14.249 0.46 41.98 ? 40 GLU A OE1 1 ATOM 343 O OE2 A GLU A 1 40 ? 45.928 23.139 15.476 0.54 40.67 ? 40 GLU A OE2 1 ATOM 344 O OE2 B GLU A 1 40 ? 42.273 23.137 13.209 0.46 34.00 ? 40 GLU A OE2 1 ATOM 345 N N . THR A 1 41 ? 45.587 21.519 9.037 1.00 20.66 ? 41 THR A N 1 ATOM 346 C CA . THR A 1 41 ? 44.793 20.915 7.976 1.00 18.84 ? 41 THR A CA 1 ATOM 347 C C . THR A 1 41 ? 43.417 20.574 8.527 1.00 21.00 ? 41 THR A C 1 ATOM 348 O O . THR A 1 41 ? 43.300 19.901 9.557 1.00 21.23 ? 41 THR A O 1 ATOM 349 C CB . THR A 1 41 ? 45.470 19.632 7.451 1.00 26.34 ? 41 THR A CB 1 ATOM 350 O OG1 . THR A 1 41 ? 46.731 19.968 6.858 1.00 26.36 ? 41 THR A OG1 1 ATOM 351 C CG2 . THR A 1 41 ? 44.597 18.920 6.423 1.00 18.37 ? 41 THR A CG2 1 ATOM 352 N N . VAL A 1 42 ? 42.378 21.059 7.851 1.00 17.58 ? 42 VAL A N 1 ATOM 353 C CA . VAL A 1 42 ? 41.002 20.808 8.263 1.00 17.81 ? 42 VAL A CA 1 ATOM 354 C C . VAL A 1 42 ? 40.285 19.939 7.238 1.00 16.61 ? 42 VAL A C 1 ATOM 355 O O . VAL A 1 42 ? 39.953 20.399 6.147 1.00 15.80 ? 42 VAL A O 1 ATOM 356 C CB . VAL A 1 42 ? 40.224 22.129 8.433 1.00 18.07 ? 42 VAL A CB 1 ATOM 357 C CG1 . VAL A 1 42 ? 38.816 21.847 8.925 1.00 21.11 ? 42 VAL A CG1 1 ATOM 358 C CG2 . VAL A 1 42 ? 40.956 23.056 9.392 1.00 20.19 ? 42 VAL A CG2 1 ATOM 359 N N . TRP A 1 43 ? 40.054 18.676 7.583 1.00 17.50 ? 43 TRP A N 1 ATOM 360 C CA . TRP A 1 43 ? 39.399 17.754 6.661 1.00 16.79 ? 43 TRP A CA 1 ATOM 361 C C . TRP A 1 43 ? 37.891 17.993 6.661 1.00 16.72 ? 43 TRP A C 1 ATOM 362 O O . TRP A 1 43 ? 37.293 18.244 7.707 1.00 17.94 ? 43 TRP A O 1 ATOM 363 C CB . TRP A 1 43 ? 39.719 16.299 7.035 1.00 18.13 ? 43 TRP A CB 1 ATOM 364 C CG . TRP A 1 43 ? 41.188 16.002 6.966 1.00 21.37 ? 43 TRP A CG 1 ATOM 365 C CD1 . TRP A 1 43 ? 42.085 16.075 7.991 1.00 21.79 ? 43 TRP A CD1 1 ATOM 366 C CD2 . TRP A 1 43 ? 41.933 15.601 5.807 1.00 17.60 ? 43 TRP A CD2 1 ATOM 367 N NE1 . TRP A 1 43 ? 43.341 15.740 7.545 1.00 26.20 ? 43 TRP A NE1 1 ATOM 368 C CE2 . TRP A 1 43 ? 43.275 15.442 6.210 1.00 20.00 ? 43 TRP A CE2 1 ATOM 369 C CE3 . TRP A 1 43 ? 41.596 15.356 4.474 1.00 16.53 ? 43 TRP A CE3 1 ATOM 370 C CZ2 . TRP A 1 43 ? 44.281 15.055 5.325 1.00 24.47 ? 43 TRP A CZ2 1 ATOM 371 C CZ3 . TRP A 1 43 ? 42.597 14.965 3.595 1.00 17.78 ? 43 TRP A CZ3 1 ATOM 372 C CH2 . TRP A 1 43 ? 43.925 14.819 4.027 1.00 17.19 ? 43 TRP A CH2 1 ATOM 373 N N . ARG A 1 44 ? 37.279 17.924 5.485 1.00 15.52 ? 44 ARG A N 1 ATOM 374 C CA . ARG A 1 44 ? 35.873 18.293 5.348 1.00 15.49 ? 44 ARG A CA 1 ATOM 375 C C . ARG A 1 44 ? 34.976 17.309 6.075 1.00 17.68 ? 44 ARG A C 1 ATOM 376 O O . ARG A 1 44 ? 33.991 17.700 6.704 1.00 18.69 ? 44 ARG A O 1 ATOM 377 C CB . ARG A 1 44 ? 35.479 18.381 3.875 1.00 14.07 ? 44 ARG A CB 1 ATOM 378 C CG . ARG A 1 44 ? 34.031 18.786 3.646 1.00 14.85 ? 44 ARG A CG 1 ATOM 379 C CD . ARG A 1 44 ? 33.757 20.148 4.248 1.00 15.98 ? 44 ARG A CD 1 ATOM 380 N NE . ARG A 1 44 ? 32.367 20.557 4.076 1.00 14.89 ? 44 ARG A NE 1 ATOM 381 C CZ . ARG A 1 44 ? 31.385 20.249 4.918 1.00 16.42 ? 44 ARG A CZ 1 ATOM 382 N NH1 . ARG A 1 44 ? 31.629 19.530 6.009 1.00 18.45 ? 44 ARG A NH1 1 ATOM 383 N NH2 . ARG A 1 44 ? 30.151 20.675 4.680 1.00 16.95 ? 44 ARG A NH2 1 ATOM 384 N N . LEU A 1 45 ? 35.322 16.030 5.965 1.00 17.77 ? 45 LEU A N 1 ATOM 385 C CA . LEU A 1 45 ? 34.729 14.991 6.792 1.00 19.73 ? 45 LEU A CA 1 ATOM 386 C C . LEU A 1 45 ? 35.827 14.428 7.676 1.00 23.72 ? 45 LEU A C 1 ATOM 387 O O . LEU A 1 45 ? 36.918 14.112 7.201 1.00 22.25 ? 45 LEU A O 1 ATOM 388 C CB . LEU A 1 45 ? 34.107 13.883 5.944 1.00 22.48 ? 45 LEU A CB 1 ATOM 389 C CG . LEU A 1 45 ? 32.987 14.308 4.984 1.00 23.38 ? 45 LEU A CG 1 ATOM 390 C CD1 . LEU A 1 45 ? 32.298 13.088 4.383 1.00 23.58 ? 45 LEU A CD1 1 ATOM 391 C CD2 . LEU A 1 45 ? 31.976 15.204 5.675 1.00 21.78 ? 45 LEU A CD2 1 ATOM 392 N N A GLU A 1 46 ? 35.541 14.286 8.967 0.54 23.73 ? 46 GLU A N 1 ATOM 393 N N B GLU A 1 46 ? 35.518 14.367 8.965 0.46 24.35 ? 46 GLU A N 1 ATOM 394 C CA A GLU A 1 46 ? 36.557 13.848 9.921 0.54 26.47 ? 46 GLU A CA 1 ATOM 395 C CA B GLU A 1 46 ? 36.341 13.779 10.012 0.46 30.37 ? 46 GLU A CA 1 ATOM 396 C C A GLU A 1 46 ? 37.197 12.512 9.537 0.54 28.35 ? 46 GLU A C 1 ATOM 397 C C B GLU A 1 46 ? 37.120 12.530 9.587 0.46 28.56 ? 46 GLU A C 1 ATOM 398 O O A GLU A 1 46 ? 38.378 12.289 9.812 0.54 30.10 ? 46 GLU A O 1 ATOM 399 O O B GLU A 1 46 ? 38.311 12.397 9.871 0.46 31.26 ? 46 GLU A O 1 ATOM 400 C CB A GLU A 1 46 ? 35.986 13.764 11.342 0.54 33.93 ? 46 GLU A CB 1 ATOM 401 C CB B GLU A 1 46 ? 35.433 13.452 11.210 0.46 33.28 ? 46 GLU A CB 1 ATOM 402 C CG A GLU A 1 46 ? 37.055 13.575 12.410 0.54 36.23 ? 46 GLU A CG 1 ATOM 403 C CG B GLU A 1 46 ? 34.086 12.767 10.852 0.46 41.17 ? 46 GLU A CG 1 ATOM 404 C CD A GLU A 1 46 ? 36.490 13.143 13.750 0.54 43.76 ? 46 GLU A CD 1 ATOM 405 C CD B GLU A 1 46 ? 33.053 13.695 10.188 0.46 34.90 ? 46 GLU A CD 1 ATOM 406 O OE1 A GLU A 1 46 ? 35.419 13.650 14.145 0.54 50.51 ? 46 GLU A OE1 1 ATOM 407 O OE1 B GLU A 1 46 ? 33.273 14.927 10.140 0.46 27.28 ? 46 GLU A OE1 1 ATOM 408 O OE2 A GLU A 1 46 ? 37.117 12.284 14.405 0.54 48.87 ? 46 GLU A OE2 1 ATOM 409 O OE2 B GLU A 1 46 ? 32.024 13.184 9.695 0.46 33.60 ? 46 GLU A OE2 1 ATOM 410 N N . GLU A 1 47 ? 36.431 11.633 8.892 1.00 28.79 ? 47 GLU A N 1 ATOM 411 C CA A GLU A 1 47 ? 36.969 10.330 8.508 0.48 32.01 ? 47 GLU A CA 1 ATOM 412 C CA B GLU A 1 47 ? 36.958 10.332 8.482 0.52 32.57 ? 47 GLU A CA 1 ATOM 413 C C . GLU A 1 47 ? 38.133 10.435 7.517 1.00 32.25 ? 47 GLU A C 1 ATOM 414 O O . GLU A 1 47 ? 38.993 9.557 7.475 1.00 27.79 ? 47 GLU A O 1 ATOM 415 C CB A GLU A 1 47 ? 35.870 9.427 7.942 0.48 35.32 ? 47 GLU A CB 1 ATOM 416 C CB B GLU A 1 47 ? 35.849 9.513 7.815 0.52 35.12 ? 47 GLU A CB 1 ATOM 417 C CG A GLU A 1 47 ? 34.582 9.436 8.744 0.48 40.62 ? 47 GLU A CG 1 ATOM 418 C CG B GLU A 1 47 ? 35.266 10.184 6.575 0.52 34.85 ? 47 GLU A CG 1 ATOM 419 C CD A GLU A 1 47 ? 33.608 10.490 8.257 0.48 26.98 ? 47 GLU A CD 1 ATOM 420 C CD B GLU A 1 47 ? 34.447 9.244 5.711 0.52 39.64 ? 47 GLU A CD 1 ATOM 421 O OE1 A GLU A 1 47 ? 33.541 11.574 8.873 0.48 26.13 ? 47 GLU A OE1 1 ATOM 422 O OE1 B GLU A 1 47 ? 34.953 8.817 4.649 0.52 24.50 ? 47 GLU A OE1 1 ATOM 423 O OE2 A GLU A 1 47 ? 32.913 10.232 7.253 0.48 30.71 ? 47 GLU A OE2 1 ATOM 424 O OE2 B GLU A 1 47 ? 33.294 8.946 6.085 0.52 36.05 ? 47 GLU A OE2 1 ATOM 425 N N . PHE A 1 48 ? 38.159 11.504 6.724 1.00 22.19 ? 48 PHE A N 1 ATOM 426 C CA . PHE A 1 48 ? 39.203 11.674 5.716 1.00 20.88 ? 48 PHE A CA 1 ATOM 427 C C . PHE A 1 48 ? 40.589 11.661 6.351 1.00 22.43 ? 48 PHE A C 1 ATOM 428 O O . PHE A 1 48 ? 41.536 11.119 5.780 1.00 25.57 ? 48 PHE A O 1 ATOM 429 C CB . PHE A 1 48 ? 39.032 12.988 4.951 1.00 18.70 ? 48 PHE A CB 1 ATOM 430 C CG . PHE A 1 48 ? 37.792 13.059 4.101 1.00 18.29 ? 48 PHE A CG 1 ATOM 431 C CD1 . PHE A 1 48 ? 37.450 14.251 3.478 1.00 19.42 ? 48 PHE A CD1 1 ATOM 432 C CD2 . PHE A 1 48 ? 36.970 11.956 3.922 1.00 20.62 ? 48 PHE A CD2 1 ATOM 433 C CE1 . PHE A 1 48 ? 36.318 14.342 2.691 1.00 18.38 ? 48 PHE A CE1 1 ATOM 434 C CE2 . PHE A 1 48 ? 35.832 12.040 3.133 1.00 22.29 ? 48 PHE A CE2 1 ATOM 435 C CZ . PHE A 1 48 ? 35.508 13.242 2.517 1.00 18.55 ? 48 PHE A CZ 1 ATOM 436 N N . GLY A 1 49 ? 40.693 12.258 7.535 1.00 24.42 ? 49 GLY A N 1 ATOM 437 C CA . GLY A 1 49 ? 41.969 12.425 8.209 1.00 24.06 ? 49 GLY A CA 1 ATOM 438 C C . GLY A 1 49 ? 42.530 11.163 8.837 1.00 25.46 ? 49 GLY A C 1 ATOM 439 O O . GLY A 1 49 ? 43.666 11.148 9.311 1.00 30.19 ? 49 GLY A O 1 ATOM 440 N N . ARG A 1 50 ? 41.735 10.100 8.854 1.00 26.60 ? 50 ARG A N 1 ATOM 441 C CA . ARG A 1 50 ? 42.217 8.821 9.358 1.00 28.93 ? 50 ARG A CA 1 ATOM 442 C C . ARG A 1 50 ? 42.970 8.077 8.264 1.00 40.02 ? 50 ARG A C 1 ATOM 443 O O . ARG A 1 50 ? 43.731 7.153 8.541 1.00 42.95 ? 50 ARG A O 1 ATOM 444 C CB . ARG A 1 50 ? 41.056 7.967 9.870 1.00 35.91 ? 50 ARG A CB 1 ATOM 445 C CG . ARG A 1 50 ? 40.326 8.558 11.067 1.00 45.76 ? 50 ARG A CG 1 ATOM 446 C CD . ARG A 1 50 ? 39.490 7.499 11.774 1.00 58.49 ? 50 ARG A CD 1 ATOM 447 N NE . ARG A 1 50 ? 38.473 6.924 10.895 1.00 65.09 ? 50 ARG A NE 1 ATOM 448 C CZ . ARG A 1 50 ? 37.205 7.322 10.854 1.00 62.77 ? 50 ARG A CZ 1 ATOM 449 N NH1 . ARG A 1 50 ? 36.791 8.299 11.649 1.00 62.33 ? 50 ARG A NH1 1 ATOM 450 N NH2 . ARG A 1 50 ? 36.351 6.740 10.021 1.00 61.92 ? 50 ARG A NH2 1 ATOM 451 N N . PHE A 1 51 ? 42.758 8.495 7.019 1.00 40.66 ? 51 PHE A N 1 ATOM 452 C CA . PHE A 1 51 ? 43.309 7.793 5.864 1.00 45.24 ? 51 PHE A CA 1 ATOM 453 C C . PHE A 1 51 ? 44.449 8.552 5.196 1.00 32.23 ? 51 PHE A C 1 ATOM 454 O O . PHE A 1 51 ? 45.301 7.964 4.529 1.00 34.56 ? 51 PHE A O 1 ATOM 455 C CB . PHE A 1 51 ? 42.203 7.522 4.840 1.00 46.82 ? 51 PHE A CB 1 ATOM 456 C CG . PHE A 1 51 ? 41.075 6.691 5.378 1.00 55.58 ? 51 PHE A CG 1 ATOM 457 C CD1 . PHE A 1 51 ? 41.262 5.347 5.659 1.00 59.59 ? 51 PHE A CD1 1 ATOM 458 C CD2 . PHE A 1 51 ? 39.830 7.253 5.605 1.00 51.49 ? 51 PHE A CD2 1 ATOM 459 C CE1 . PHE A 1 51 ? 40.228 4.580 6.158 1.00 59.94 ? 51 PHE A CE1 1 ATOM 460 C CE2 . PHE A 1 51 ? 38.791 6.491 6.103 1.00 59.93 ? 51 PHE A CE2 1 ATOM 461 C CZ . PHE A 1 51 ? 38.991 5.152 6.380 1.00 62.72 ? 51 PHE A CZ 1 ATOM 462 N N . ALA A 1 52 ? 44.466 9.861 5.384 1.00 30.43 ? 52 ALA A N 1 ATOM 463 C CA . ALA A 1 52 ? 45.425 10.699 4.686 1.00 27.66 ? 52 ALA A CA 1 ATOM 464 C C . ALA A 1 52 ? 45.916 11.814 5.591 1.00 23.42 ? 52 ALA A C 1 ATOM 465 O O . ALA A 1 52 ? 45.291 12.123 6.605 1.00 24.60 ? 52 ALA A O 1 ATOM 466 C CB . ALA A 1 52 ? 44.793 11.278 3.429 1.00 30.22 ? 52 ALA A CB 1 ATOM 467 N N . SER A 1 53 ? 47.039 12.415 5.217 1.00 22.97 ? 53 SER A N 1 ATOM 468 C CA . SER A 1 53 ? 47.569 13.558 5.942 1.00 25.06 ? 53 SER A CA 1 ATOM 469 C C . SER A 1 53 ? 47.977 14.657 4.968 1.00 25.95 ? 53 SER A C 1 ATOM 470 O O . SER A 1 53 ? 48.128 14.415 3.771 1.00 19.93 ? 53 SER A O 1 ATOM 471 C CB . SER A 1 53 ? 48.771 13.146 6.793 1.00 26.17 ? 53 SER A CB 1 ATOM 472 O OG . SER A 1 53 ? 49.830 12.670 5.981 1.00 25.27 ? 53 SER A OG 1 ATOM 473 N N . PHE A 1 54 ? 48.142 15.867 5.489 1.00 20.50 ? 54 PHE A N 1 ATOM 474 C CA . PHE A 1 54 ? 48.701 16.965 4.710 1.00 21.37 ? 54 PHE A CA 1 ATOM 475 C C . PHE A 1 54 ? 49.480 17.917 5.608 1.00 26.21 ? 54 PHE A C 1 ATOM 476 O O . PHE A 1 54 ? 48.970 18.373 6.631 1.00 24.57 ? 54 PHE A O 1 ATOM 477 C CB . PHE A 1 54 ? 47.621 17.736 3.951 1.00 19.01 ? 54 PHE A CB 1 ATOM 478 C CG . PHE A 1 54 ? 48.172 18.873 3.143 1.00 16.47 ? 54 PHE A CG 1 ATOM 479 C CD1 . PHE A 1 54 ? 48.839 18.626 1.955 1.00 20.08 ? 54 PHE A CD1 1 ATOM 480 C CD2 . PHE A 1 54 ? 48.051 20.186 3.579 1.00 16.29 ? 54 PHE A CD2 1 ATOM 481 C CE1 . PHE A 1 54 ? 49.365 19.663 1.208 1.00 18.02 ? 54 PHE A CE1 1 ATOM 482 C CE2 . PHE A 1 54 ? 48.579 21.228 2.836 1.00 17.97 ? 54 PHE A CE2 1 ATOM 483 C CZ . PHE A 1 54 ? 49.238 20.965 1.650 1.00 16.36 ? 54 PHE A CZ 1 ATOM 484 N N . GLU A 1 55 ? 50.719 18.206 5.221 1.00 21.34 ? 55 GLU A N 1 ATOM 485 C CA . GLU A 1 55 ? 51.561 19.130 5.968 1.00 26.51 ? 55 GLU A CA 1 ATOM 486 C C . GLU A 1 55 ? 51.128 20.563 5.686 1.00 25.42 ? 55 GLU A C 1 ATOM 487 O O . GLU A 1 55 ? 51.464 21.129 4.647 1.00 25.53 ? 55 GLU A O 1 ATOM 488 C CB . GLU A 1 55 ? 53.039 18.927 5.605 1.00 28.67 ? 55 GLU A CB 1 ATOM 489 C CG . GLU A 1 55 ? 53.983 19.926 6.251 1.00 38.28 ? 55 GLU A CG 1 ATOM 490 C CD . GLU A 1 55 ? 53.790 20.017 7.752 1.00 52.47 ? 55 GLU A CD 1 ATOM 491 O OE1 . GLU A 1 55 ? 54.074 19.021 8.451 1.00 54.94 ? 55 GLU A OE1 1 ATOM 492 O OE2 . GLU A 1 55 ? 53.345 21.084 8.231 1.00 51.37 ? 55 GLU A OE2 1 ATOM 493 N N . ALA A 1 56 ? 50.376 21.136 6.621 1.00 23.08 ? 56 ALA A N 1 ATOM 494 C CA . ALA A 1 56 ? 49.775 22.458 6.451 1.00 21.64 ? 56 ALA A CA 1 ATOM 495 C C . ALA A 1 56 ? 50.788 23.554 6.142 1.00 21.43 ? 56 ALA A C 1 ATOM 496 O O . ALA A 1 56 ? 50.466 24.531 5.477 1.00 20.48 ? 56 ALA A O 1 ATOM 497 C CB . ALA A 1 56 ? 48.960 22.828 7.688 1.00 27.07 ? 56 ALA A CB 1 ATOM 498 N N . GLN A 1 57 ? 52.015 23.385 6.628 1.00 27.27 ? 57 GLN A N 1 ATOM 499 C CA . GLN A 1 57 ? 53.057 24.390 6.452 1.00 27.77 ? 57 GLN A CA 1 ATOM 500 C C . GLN A 1 57 ? 53.323 24.710 4.985 1.00 27.78 ? 57 GLN A C 1 ATOM 501 O O . GLN A 1 57 ? 53.586 25.856 4.633 1.00 27.43 ? 57 GLN A O 1 ATOM 502 C CB . GLN A 1 57 ? 54.352 23.938 7.140 1.00 31.05 ? 57 GLN A CB 1 ATOM 503 C CG . GLN A 1 57 ? 55.382 25.037 7.290 1.00 45.47 ? 57 GLN A CG 1 ATOM 504 C CD . GLN A 1 57 ? 54.874 26.187 8.134 1.00 54.60 ? 57 GLN A CD 1 ATOM 505 O OE1 . GLN A 1 57 ? 54.801 27.327 7.673 1.00 54.49 ? 57 GLN A OE1 1 ATOM 506 N NE2 . GLN A 1 57 ? 54.518 25.893 9.381 1.00 58.26 ? 57 GLN A NE2 1 ATOM 507 N N . GLY A 1 58 ? 53.238 23.700 4.126 1.00 25.20 ? 58 GLY A N 1 ATOM 508 C CA . GLY A 1 58 ? 53.477 23.901 2.709 1.00 26.82 ? 58 GLY A CA 1 ATOM 509 C C . GLY A 1 58 ? 52.508 24.863 2.042 1.00 29.36 ? 58 GLY A C 1 ATOM 510 O O . GLY A 1 58 ? 52.862 25.565 1.093 1.00 32.10 ? 58 GLY A O 1 ATOM 511 N N . ALA A 1 59 ? 51.274 24.892 2.531 1.00 20.32 ? 59 ALA A N 1 ATOM 512 C CA . ALA A 1 59 ? 50.272 25.815 2.006 1.00 19.93 ? 59 ALA A CA 1 ATOM 513 C C . ALA A 1 59 ? 50.669 27.271 2.254 1.00 21.26 ? 59 ALA A C 1 ATOM 514 O O . ALA A 1 59 ? 50.440 28.135 1.414 1.00 17.57 ? 59 ALA A O 1 ATOM 515 C CB . ALA A 1 59 ? 48.912 25.521 2.612 1.00 20.77 ? 59 ALA A CB 1 ATOM 516 N N . LEU A 1 60 ? 51.267 27.536 3.409 1.00 19.18 ? 60 LEU A N 1 ATOM 517 C CA . LEU A 1 60 ? 51.668 28.894 3.755 1.00 15.99 ? 60 LEU A CA 1 ATOM 518 C C . LEU A 1 60 ? 52.658 29.456 2.738 1.00 20.06 ? 60 LEU A C 1 ATOM 519 O O . LEU A 1 60 ? 52.568 30.623 2.352 1.00 17.28 ? 60 LEU A O 1 ATOM 520 C CB . LEU A 1 60 ? 52.252 28.952 5.168 1.00 23.76 ? 60 LEU A CB 1 ATOM 521 C CG . LEU A 1 60 ? 51.243 29.114 6.307 1.00 30.33 ? 60 LEU A CG 1 ATOM 522 C CD1 . LEU A 1 60 ? 50.376 27.873 6.484 1.00 31.29 ? 60 LEU A CD1 1 ATOM 523 C CD2 . LEU A 1 60 ? 51.972 29.444 7.597 1.00 35.40 ? 60 LEU A CD2 1 ATOM 524 N N . ALA A 1 61 ? 53.588 28.620 2.288 1.00 15.51 ? 61 ALA A N 1 ATOM 525 C CA . ALA A 1 61 ? 54.592 29.060 1.327 1.00 22.50 ? 61 ALA A CA 1 ATOM 526 C C . ALA A 1 61 ? 53.949 29.422 -0.008 1.00 16.38 ? 61 ALA A C 1 ATOM 527 O O . ALA A 1 61 ? 54.308 30.424 -0.625 1.00 17.23 ? 61 ALA A O 1 ATOM 528 C CB . ALA A 1 61 ? 55.652 27.997 1.135 1.00 25.18 ? 61 ALA A CB 1 ATOM 529 N N . ASN A 1 62 ? 52.999 28.607 -0.452 1.00 16.36 ? 62 ASN A N 1 ATOM 530 C CA . ASN A 1 62 ? 52.304 28.898 -1.700 1.00 10.85 ? 62 ASN A CA 1 ATOM 531 C C . ASN A 1 62 ? 51.531 30.209 -1.628 1.00 10.15 ? 62 ASN A C 1 ATOM 532 O O . ASN A 1 62 ? 51.544 31.000 -2.572 1.00 12.52 ? 62 ASN A O 1 ATOM 533 C CB . ASN A 1 62 ? 51.357 27.757 -2.090 1.00 10.91 ? 62 ASN A CB 1 ATOM 534 C CG . ASN A 1 62 ? 52.052 26.693 -2.922 1.00 14.50 ? 62 ASN A CG 1 ATOM 535 O OD1 . ASN A 1 62 ? 53.287 26.586 -2.923 1.00 18.06 ? 62 ASN A OD1 1 ATOM 536 N ND2 . ASN A 1 62 ? 51.274 25.916 -3.648 1.00 10.87 ? 62 ASN A ND2 1 ATOM 537 N N . ILE A 1 63 ? 50.856 30.432 -0.507 1.00 12.55 ? 63 ILE A N 1 ATOM 538 C CA . ILE A 1 63 ? 50.059 31.635 -0.340 1.00 10.87 ? 63 ILE A CA 1 ATOM 539 C C . ILE A 1 63 ? 50.966 32.867 -0.344 1.00 10.96 ? 63 ILE A C 1 ATOM 540 O O . ILE A 1 63 ? 50.593 33.915 -0.869 1.00 13.50 ? 63 ILE A O 1 ATOM 541 C CB . ILE A 1 63 ? 49.210 31.585 0.952 1.00 15.94 ? 63 ILE A CB 1 ATOM 542 C CG1 . ILE A 1 63 ? 48.122 30.517 0.831 1.00 22.63 ? 63 ILE A CG1 1 ATOM 543 C CG2 . ILE A 1 63 ? 48.593 32.950 1.253 1.00 18.14 ? 63 ILE A CG2 1 ATOM 544 C CD1 . ILE A 1 63 ? 47.303 30.624 -0.420 1.00 26.75 ? 63 ILE A CD1 1 ATOM 545 N N . ALA A 1 64 ? 52.165 32.734 0.218 1.00 12.17 ? 64 ALA A N 1 ATOM 546 C CA . ALA A 1 64 ? 53.119 33.836 0.192 1.00 13.84 ? 64 ALA A CA 1 ATOM 547 C C . ALA A 1 64 ? 53.537 34.173 -1.239 1.00 15.49 ? 64 ALA A C 1 ATOM 548 O O . ALA A 1 64 ? 53.695 35.344 -1.589 1.00 15.45 ? 64 ALA A O 1 ATOM 549 C CB . ALA A 1 64 ? 54.350 33.511 1.041 1.00 16.23 ? 64 ALA A CB 1 ATOM 550 N N . VAL A 1 65 ? 53.742 33.145 -2.057 1.00 12.56 ? 65 VAL A N 1 ATOM 551 C CA . VAL A 1 65 ? 54.061 33.354 -3.466 1.00 11.68 ? 65 VAL A CA 1 ATOM 552 C C . VAL A 1 65 ? 52.887 34.013 -4.176 1.00 12.33 ? 65 VAL A C 1 ATOM 553 O O . VAL A 1 65 ? 53.067 34.915 -4.994 1.00 12.90 ? 65 VAL A O 1 ATOM 554 C CB . VAL A 1 65 ? 54.409 32.037 -4.177 1.00 15.04 ? 65 VAL A CB 1 ATOM 555 C CG1 . VAL A 1 65 ? 54.503 32.255 -5.686 1.00 15.19 ? 65 VAL A CG1 1 ATOM 556 C CG2 . VAL A 1 65 ? 55.714 31.484 -3.634 1.00 14.75 ? 65 VAL A CG2 1 ATOM 557 N N . ASP A 1 66 ? 51.679 33.565 -3.851 1.00 10.59 ? 66 ASP A N 1 ATOM 558 C CA . ASP A 1 66 ? 50.479 34.117 -4.479 1.00 8.07 ? 66 ASP A CA 1 ATOM 559 C C . ASP A 1 66 ? 50.311 35.594 -4.137 1.00 11.63 ? 66 ASP A C 1 ATOM 560 O O . ASP A 1 66 ? 49.880 36.385 -4.978 1.00 13.01 ? 66 ASP A O 1 ATOM 561 C CB . ASP A 1 66 ? 49.225 33.351 -4.043 1.00 10.83 ? 66 ASP A CB 1 ATOM 562 C CG . ASP A 1 66 ? 49.239 31.905 -4.478 1.00 12.48 ? 66 ASP A CG 1 ATOM 563 O OD1 . ASP A 1 66 ? 49.938 31.560 -5.453 1.00 10.06 ? 66 ASP A OD1 1 ATOM 564 O OD2 . ASP A 1 66 ? 48.528 31.106 -3.834 1.00 11.12 ? 66 ASP A OD2 1 ATOM 565 N N . LYS A 1 67 ? 50.658 35.958 -2.906 1.00 9.77 ? 67 LYS A N 1 ATOM 566 C CA . LYS A 1 67 ? 50.612 37.351 -2.469 1.00 10.95 ? 67 LYS A CA 1 ATOM 567 C C . LYS A 1 67 ? 51.602 38.193 -3.277 1.00 15.15 ? 67 LYS A C 1 ATOM 568 O O . LYS A 1 67 ? 51.259 39.271 -3.761 1.00 10.99 ? 67 LYS A O 1 ATOM 569 C CB . LYS A 1 67 ? 50.911 37.437 -0.967 1.00 13.50 ? 67 LYS A CB 1 ATOM 570 C CG . LYS A 1 67 ? 51.056 38.846 -0.406 1.00 16.20 ? 67 LYS A CG 1 ATOM 571 C CD . LYS A 1 67 ? 51.372 38.782 1.084 1.00 20.19 ? 67 LYS A CD 1 ATOM 572 C CE . LYS A 1 67 ? 51.319 40.155 1.739 1.00 31.00 ? 67 LYS A CE 1 ATOM 573 N NZ . LYS A 1 67 ? 52.522 40.968 1.433 1.00 36.24 ? 67 LYS A NZ 1 ATOM 574 N N . ALA A 1 68 ? 52.827 37.694 -3.436 1.00 12.49 ? 68 ALA A N 1 ATOM 575 C CA . ALA A 1 68 ? 53.824 38.403 -4.226 1.00 13.80 ? 68 ALA A CA 1 ATOM 576 C C . ALA A 1 68 ? 53.416 38.474 -5.696 1.00 13.01 ? 68 ALA A C 1 ATOM 577 O O . ALA A 1 68 ? 53.615 39.498 -6.354 1.00 15.85 ? 68 ALA A O 1 ATOM 578 C CB . ALA A 1 68 ? 55.187 37.742 -4.080 1.00 19.80 ? 68 ALA A CB 1 ATOM 579 N N . ASN A 1 69 ? 52.844 37.393 -6.214 1.00 12.76 ? 69 ASN A N 1 ATOM 580 C CA . ASN A 1 69 ? 52.361 37.410 -7.588 1.00 11.54 ? 69 ASN A CA 1 ATOM 581 C C . ASN A 1 69 ? 51.210 38.385 -7.790 1.00 11.09 ? 69 ASN A C 1 ATOM 582 O O . ASN A 1 69 ? 51.126 39.034 -8.835 1.00 11.88 ? 69 ASN A O 1 ATOM 583 C CB . ASN A 1 69 ? 51.965 36.008 -8.065 1.00 10.90 ? 69 ASN A CB 1 ATOM 584 C CG . ASN A 1 69 ? 53.176 35.142 -8.364 1.00 12.41 ? 69 ASN A CG 1 ATOM 585 O OD1 . ASN A 1 69 ? 54.311 35.632 -8.372 1.00 17.62 ? 69 ASN A OD1 1 ATOM 586 N ND2 . ASN A 1 69 ? 52.945 33.857 -8.622 1.00 12.93 ? 69 ASN A ND2 1 ATOM 587 N N . LEU A 1 70 ? 50.324 38.493 -6.801 1.00 9.42 ? 70 LEU A N 1 ATOM 588 C CA . LEU A 1 70 ? 49.225 39.457 -6.893 1.00 11.44 ? 70 LEU A CA 1 ATOM 589 C C . LEU A 1 70 ? 49.761 40.879 -7.040 1.00 11.29 ? 70 LEU A C 1 ATOM 590 O O . LEU A 1 70 ? 49.222 41.662 -7.826 1.00 13.22 ? 70 LEU A O 1 ATOM 591 C CB . LEU A 1 70 ? 48.285 39.369 -5.679 1.00 9.31 ? 70 LEU A CB 1 ATOM 592 C CG . LEU A 1 70 ? 47.127 40.378 -5.675 1.00 9.52 ? 70 LEU A CG 1 ATOM 593 C CD1 . LEU A 1 70 ? 46.279 40.209 -6.937 1.00 11.10 ? 70 LEU A CD1 1 ATOM 594 C CD2 . LEU A 1 70 ? 46.267 40.199 -4.419 1.00 11.76 ? 70 LEU A CD2 1 ATOM 595 N N . GLU A 1 71 ? 50.809 41.205 -6.285 1.00 10.74 ? 71 GLU A N 1 ATOM 596 C CA A GLU A 1 71 ? 51.478 42.503 -6.394 0.51 14.00 ? 71 GLU A CA 1 ATOM 597 C CA B GLU A 1 71 ? 51.435 42.516 -6.395 0.21 13.77 ? 71 GLU A CA 1 ATOM 598 C CA C GLU A 1 71 ? 51.450 42.509 -6.393 0.28 12.18 ? 71 GLU A CA 1 ATOM 599 C C . GLU A 1 71 ? 51.904 42.751 -7.829 1.00 14.28 ? 71 GLU A C 1 ATOM 600 O O . GLU A 1 71 ? 51.657 43.815 -8.403 1.00 14.17 ? 71 GLU A O 1 ATOM 601 C CB A GLU A 1 71 ? 52.741 42.533 -5.529 0.51 13.49 ? 71 GLU A CB 1 ATOM 602 C CB B GLU A 1 71 ? 52.606 42.636 -5.417 0.21 16.30 ? 71 GLU A CB 1 ATOM 603 C CB C GLU A 1 71 ? 52.644 42.586 -5.436 0.28 16.44 ? 71 GLU A CB 1 ATOM 604 C CG A GLU A 1 71 ? 52.515 42.532 -4.039 0.51 19.30 ? 71 GLU A CG 1 ATOM 605 C CG B GLU A 1 71 ? 53.115 44.057 -5.215 0.21 17.20 ? 71 GLU A CG 1 ATOM 606 C CG C GLU A 1 71 ? 53.657 43.670 -5.767 0.28 18.64 ? 71 GLU A CG 1 ATOM 607 C CD A GLU A 1 71 ? 53.820 42.503 -3.262 0.51 26.77 ? 71 GLU A CD 1 ATOM 608 C CD B GLU A 1 71 ? 54.413 44.330 -5.951 0.21 20.65 ? 71 GLU A CD 1 ATOM 609 C CD C GLU A 1 71 ? 53.099 45.071 -5.606 0.28 22.67 ? 71 GLU A CD 1 ATOM 610 O OE1 A GLU A 1 71 ? 53.989 41.607 -2.409 0.51 27.16 ? 71 GLU A OE1 1 ATOM 611 O OE1 B GLU A 1 71 ? 54.460 44.126 -7.182 0.21 21.79 ? 71 GLU A OE1 1 ATOM 612 O OE1 C GLU A 1 71 ? 52.123 45.246 -4.848 0.28 25.14 ? 71 GLU A OE1 1 ATOM 613 O OE2 A GLU A 1 71 ? 54.677 43.377 -3.511 0.51 32.12 ? 71 GLU A OE2 1 ATOM 614 O OE2 B GLU A 1 71 ? 55.391 44.748 -5.296 0.21 20.68 ? 71 GLU A OE2 1 ATOM 615 O OE2 C GLU A 1 71 ? 53.641 45.994 -6.244 0.28 18.32 ? 71 GLU A OE2 1 ATOM 616 N N . ILE A 1 72 ? 52.566 41.750 -8.402 1.00 13.96 ? 72 ILE A N 1 ATOM 617 C CA . ILE A 1 72 ? 53.064 41.833 -9.764 1.00 15.54 ? 72 ILE A CA 1 ATOM 618 C C . ILE A 1 72 ? 51.935 42.020 -10.771 1.00 12.08 ? 72 ILE A C 1 ATOM 619 O O . ILE A 1 72 ? 52.008 42.895 -11.643 1.00 15.49 ? 72 ILE A O 1 ATOM 620 C CB . ILE A 1 72 ? 53.873 40.569 -10.119 1.00 17.87 ? 72 ILE A CB 1 ATOM 621 C CG1 . ILE A 1 72 ? 55.193 40.574 -9.344 1.00 19.07 ? 72 ILE A CG1 1 ATOM 622 C CG2 . ILE A 1 72 ? 54.120 40.488 -11.615 1.00 26.55 ? 72 ILE A CG2 1 ATOM 623 C CD1 . ILE A 1 72 ? 55.971 39.277 -9.443 1.00 22.09 ? 72 ILE A CD1 1 ATOM 624 N N . MET A 1 73 ? 50.889 41.207 -10.644 1.00 10.80 ? 73 MET A N 1 ATOM 625 C CA . MET A 1 73 ? 49.801 41.236 -11.618 1.00 9.57 ? 73 MET A CA 1 ATOM 626 C C . MET A 1 73 ? 48.955 42.498 -11.503 1.00 10.22 ? 73 MET A C 1 ATOM 627 O O . MET A 1 73 ? 48.462 43.020 -12.504 1.00 13.30 ? 73 MET A O 1 ATOM 628 C CB . MET A 1 73 ? 48.920 39.979 -11.502 1.00 12.53 ? 73 MET A CB 1 ATOM 629 C CG . MET A 1 73 ? 49.682 38.679 -11.730 1.00 13.86 ? 73 MET A CG 1 ATOM 630 S SD . MET A 1 73 ? 50.646 38.643 -13.253 1.00 14.96 ? 73 MET A SD 1 ATOM 631 C CE . MET A 1 73 ? 49.377 39.018 -14.450 1.00 11.00 ? 73 MET A CE 1 ATOM 632 N N . THR A 1 74 ? 48.785 42.988 -10.281 1.00 10.54 ? 74 THR A N 1 ATOM 633 C CA . THR A 1 74 ? 48.073 44.242 -10.081 1.00 11.62 ? 74 THR A CA 1 ATOM 634 C C . THR A 1 74 ? 48.775 45.365 -10.845 1.00 12.89 ? 74 THR A C 1 ATOM 635 O O . THR A 1 74 ? 48.135 46.117 -11.574 1.00 13.63 ? 74 THR A O 1 ATOM 636 C CB . THR A 1 74 ? 47.963 44.585 -8.588 1.00 12.26 ? 74 THR A CB 1 ATOM 637 O OG1 . THR A 1 74 ? 47.223 43.547 -7.929 1.00 11.33 ? 74 THR A OG1 1 ATOM 638 C CG2 . THR A 1 74 ? 47.245 45.908 -8.384 1.00 13.82 ? 74 THR A CG2 1 ATOM 639 N N . LYS A 1 75 ? 50.094 45.457 -10.697 1.00 13.42 ? 75 LYS A N 1 ATOM 640 C CA . LYS A 1 75 ? 50.870 46.432 -11.460 1.00 14.90 ? 75 LYS A CA 1 ATOM 641 C C . LYS A 1 75 ? 50.776 46.245 -12.975 1.00 14.81 ? 75 LYS A C 1 ATOM 642 O O . LYS A 1 75 ? 50.594 47.218 -13.710 1.00 17.00 ? 75 LYS A O 1 ATOM 643 C CB . LYS A 1 75 ? 52.338 46.389 -11.043 1.00 20.19 ? 75 LYS A CB 1 ATOM 644 C CG . LYS A 1 75 ? 52.586 46.856 -9.631 1.00 26.79 ? 75 LYS A CG 1 ATOM 645 C CD . LYS A 1 75 ? 54.052 46.679 -9.267 1.00 29.29 ? 75 LYS A CD 1 ATOM 646 C CE . LYS A 1 75 ? 54.958 47.094 -10.412 1.00 32.10 ? 75 LYS A CE 1 ATOM 647 N NZ . LYS A 1 75 ? 56.394 46.851 -10.087 1.00 38.57 ? 75 LYS A NZ 1 ATOM 648 N N . ARG A 1 76 ? 50.919 45.007 -13.443 1.00 13.69 ? 76 ARG A N 1 ATOM 649 C CA . ARG A 1 76 ? 50.831 44.722 -14.877 1.00 16.37 ? 76 ARG A CA 1 ATOM 650 C C . ARG A 1 76 ? 49.508 45.170 -15.484 1.00 14.08 ? 76 ARG A C 1 ATOM 651 O O . ARG A 1 76 ? 49.461 45.634 -16.629 1.00 15.89 ? 76 ARG A O 1 ATOM 652 C CB . ARG A 1 76 ? 51.020 43.224 -15.153 1.00 16.06 ? 76 ARG A CB 1 ATOM 653 C CG . ARG A 1 76 ? 52.417 42.829 -15.526 1.00 22.53 ? 76 ARG A CG 1 ATOM 654 C CD . ARG A 1 76 ? 52.473 41.368 -15.975 1.00 19.96 ? 76 ARG A CD 1 ATOM 655 N NE . ARG A 1 76 ? 53.624 40.694 -15.388 1.00 21.21 ? 76 ARG A NE 1 ATOM 656 C CZ . ARG A 1 76 ? 53.770 39.375 -15.318 1.00 21.90 ? 76 ARG A CZ 1 ATOM 657 N NH1 . ARG A 1 76 ? 52.836 38.564 -15.810 1.00 18.75 ? 76 ARG A NH1 1 ATOM 658 N NH2 . ARG A 1 76 ? 54.855 38.864 -14.758 1.00 22.87 ? 76 ARG A NH2 1 ATOM 659 N N . SER A 1 77 ? 48.436 45.030 -14.711 1.00 12.44 ? 77 SER A N 1 ATOM 660 C CA . SER A 1 77 ? 47.095 45.380 -15.175 1.00 12.51 ? 77 SER A CA 1 ATOM 661 C C . SER A 1 77 ? 46.806 46.878 -15.083 1.00 11.96 ? 77 SER A C 1 ATOM 662 O O . SER A 1 77 ? 45.687 47.308 -15.369 1.00 15.51 ? 77 SER A O 1 ATOM 663 C CB . SER A 1 77 ? 46.038 44.621 -14.368 1.00 12.18 ? 77 SER A CB 1 ATOM 664 O OG . SER A 1 77 ? 45.860 45.221 -13.091 1.00 13.32 ? 77 SER A OG 1 ATOM 665 N N . ASN A 1 78 ? 47.805 47.663 -14.675 1.00 13.68 ? 78 ASN A N 1 ATOM 666 C CA . ASN A 1 78 ? 47.603 49.088 -14.370 1.00 14.40 ? 78 ASN A CA 1 ATOM 667 C C . ASN A 1 78 ? 46.548 49.299 -13.288 1.00 12.38 ? 78 ASN A C 1 ATOM 668 O O . ASN A 1 78 ? 45.693 50.188 -13.392 1.00 14.26 ? 78 ASN A O 1 ATOM 669 C CB . ASN A 1 78 ? 47.242 49.876 -15.625 1.00 17.68 ? 78 ASN A CB 1 ATOM 670 C CG . ASN A 1 78 ? 48.257 49.702 -16.718 1.00 19.63 ? 78 ASN A CG 1 ATOM 671 O OD1 . ASN A 1 78 ? 49.459 49.781 -16.471 1.00 22.24 ? 78 ASN A OD1 1 ATOM 672 N ND2 . ASN A 1 78 ? 47.783 49.449 -17.936 1.00 31.76 ? 78 ASN A ND2 1 ATOM 673 N N . TYR A 1 79 ? 46.623 48.462 -12.257 1.00 12.72 ? 79 TYR A N 1 ATOM 674 C CA . TYR A 1 79 ? 45.744 48.532 -11.092 1.00 11.25 ? 79 TYR A CA 1 ATOM 675 C C . TYR A 1 79 ? 44.261 48.441 -11.450 1.00 13.68 ? 79 TYR A C 1 ATOM 676 O O . TYR A 1 79 ? 43.432 49.172 -10.911 1.00 15.18 ? 79 TYR A O 1 ATOM 677 C CB . TYR A 1 79 ? 46.048 49.782 -10.257 1.00 12.64 ? 79 TYR A CB 1 ATOM 678 C CG . TYR A 1 79 ? 47.447 49.767 -9.673 1.00 15.26 ? 79 TYR A CG 1 ATOM 679 C CD1 . TYR A 1 79 ? 48.542 50.153 -10.435 1.00 14.69 ? 79 TYR A CD1 1 ATOM 680 C CD2 . TYR A 1 79 ? 47.674 49.348 -8.366 1.00 15.34 ? 79 TYR A CD2 1 ATOM 681 C CE1 . TYR A 1 79 ? 49.826 50.139 -9.915 1.00 15.75 ? 79 TYR A CE1 1 ATOM 682 C CE2 . TYR A 1 79 ? 48.966 49.330 -7.833 1.00 15.94 ? 79 TYR A CE2 1 ATOM 683 C CZ . TYR A 1 79 ? 50.031 49.721 -8.615 1.00 16.17 ? 79 TYR A CZ 1 ATOM 684 O OH . TYR A 1 79 ? 51.313 49.711 -8.115 1.00 19.49 ? 79 TYR A OH 1 ATOM 685 N N . THR A 1 80 ? 43.936 47.531 -12.362 1.00 11.92 ? 80 THR A N 1 ATOM 686 C CA . THR A 1 80 ? 42.547 47.288 -12.728 1.00 10.42 ? 80 THR A CA 1 ATOM 687 C C . THR A 1 80 ? 41.927 46.387 -11.665 1.00 11.66 ? 80 THR A C 1 ATOM 688 O O . THR A 1 80 ? 42.396 45.270 -11.457 1.00 13.99 ? 80 THR A O 1 ATOM 689 C CB . THR A 1 80 ? 42.459 46.610 -14.108 1.00 12.41 ? 80 THR A CB 1 ATOM 690 O OG1 . THR A 1 80 ? 43.066 47.454 -15.100 1.00 14.88 ? 80 THR A OG1 1 ATOM 691 C CG2 . THR A 1 80 ? 41.007 46.360 -14.484 1.00 13.88 ? 80 THR A CG2 1 ATOM 692 N N . PRO A 1 81 ? 40.888 46.873 -10.971 1.00 10.09 ? 81 PRO A N 1 ATOM 693 C CA . PRO A 1 81 ? 40.309 46.072 -9.886 1.00 9.60 ? 81 PRO A CA 1 ATOM 694 C C . PRO A 1 81 ? 39.270 45.073 -10.366 1.00 10.64 ? 81 PRO A C 1 ATOM 695 O O . PRO A 1 81 ? 38.796 45.133 -11.498 1.00 12.34 ? 81 PRO A O 1 ATOM 696 C CB . PRO A 1 81 ? 39.632 47.119 -9.009 1.00 12.87 ? 81 PRO A CB 1 ATOM 697 C CG . PRO A 1 81 ? 39.233 48.190 -9.965 1.00 21.49 ? 81 PRO A CG 1 ATOM 698 C CD . PRO A 1 81 ? 40.273 48.208 -11.062 1.00 17.62 ? 81 PRO A CD 1 ATOM 699 N N . ILE A 1 82 ? 38.917 44.156 -9.478 1.00 9.51 ? 82 ILE A N 1 ATOM 700 C CA . ILE A 1 82 ? 37.877 43.182 -9.761 1.00 8.11 ? 82 ILE A CA 1 ATOM 701 C C . ILE A 1 82 ? 36.503 43.857 -9.861 1.00 10.37 ? 82 ILE A C 1 ATOM 702 O O . ILE A 1 82 ? 36.226 44.854 -9.186 1.00 12.38 ? 82 ILE A O 1 ATOM 703 C CB . ILE A 1 82 ? 37.879 42.068 -8.686 1.00 7.26 ? 82 ILE A CB 1 ATOM 704 C CG1 . ILE A 1 82 ? 37.231 40.785 -9.227 1.00 8.37 ? 82 ILE A CG1 1 ATOM 705 C CG2 . ILE A 1 82 ? 37.231 42.546 -7.379 1.00 12.15 ? 82 ILE A CG2 1 ATOM 706 C CD1 . ILE A 1 82 ? 37.566 39.542 -8.399 1.00 10.56 ? 82 ILE A CD1 1 ATOM 707 N N . THR A 1 83 ? 35.654 43.318 -10.731 1.00 9.27 ? 83 THR A N 1 ATOM 708 C CA . THR A 1 83 ? 34.262 43.745 -10.818 1.00 10.68 ? 83 THR A CA 1 ATOM 709 C C . THR A 1 83 ? 33.450 42.845 -9.894 1.00 8.97 ? 83 THR A C 1 ATOM 710 O O . THR A 1 83 ? 33.566 41.619 -9.961 1.00 11.79 ? 83 THR A O 1 ATOM 711 C CB . THR A 1 83 ? 33.748 43.631 -12.261 1.00 16.05 ? 83 THR A CB 1 ATOM 712 O OG1 . THR A 1 83 ? 34.475 44.545 -13.094 1.00 16.80 ? 83 THR A OG1 1 ATOM 713 C CG2 . THR A 1 83 ? 32.259 43.968 -12.340 1.00 19.17 ? 83 THR A CG2 1 ATOM 714 N N . ASN A 1 84 ? 32.660 43.452 -9.008 1.00 10.79 ? 84 ASN A N 1 ATOM 715 C CA . ASN A 1 84 ? 31.827 42.676 -8.093 1.00 9.50 ? 84 ASN A CA 1 ATOM 716 C C . ASN A 1 84 ? 30.761 41.915 -8.867 1.00 9.61 ? 84 ASN A C 1 ATOM 717 O O . ASN A 1 84 ? 30.090 42.470 -9.742 1.00 13.10 ? 84 ASN A O 1 ATOM 718 C CB . ASN A 1 84 ? 31.128 43.577 -7.068 1.00 12.37 ? 84 ASN A CB 1 ATOM 719 C CG . ASN A 1 84 ? 32.092 44.271 -6.124 1.00 12.38 ? 84 ASN A CG 1 ATOM 720 O OD1 . ASN A 1 84 ? 33.034 43.667 -5.618 1.00 12.88 ? 84 ASN A OD1 1 ATOM 721 N ND2 . ASN A 1 84 ? 31.840 45.551 -5.865 1.00 14.94 ? 84 ASN A ND2 1 ATOM 722 N N . VAL A 1 85 ? 30.622 40.637 -8.534 1.00 10.61 ? 85 VAL A N 1 ATOM 723 C CA . VAL A 1 85 ? 29.563 39.798 -9.075 1.00 8.50 ? 85 VAL A CA 1 ATOM 724 C C . VAL A 1 85 ? 28.747 39.315 -7.882 1.00 8.25 ? 85 VAL A C 1 ATOM 725 O O . VAL A 1 85 ? 29.238 38.552 -7.062 1.00 8.82 ? 85 VAL A O 1 ATOM 726 C CB . VAL A 1 85 ? 30.153 38.593 -9.845 1.00 8.20 ? 85 VAL A CB 1 ATOM 727 C CG1 . VAL A 1 85 ? 29.043 37.664 -10.345 1.00 9.70 ? 85 VAL A CG1 1 ATOM 728 C CG2 . VAL A 1 85 ? 31.006 39.064 -10.998 1.00 10.49 ? 85 VAL A CG2 1 ATOM 729 N N . PRO A 1 86 ? 27.494 39.779 -7.762 1.00 9.16 ? 86 PRO A N 1 ATOM 730 C CA . PRO A 1 86 ? 26.731 39.441 -6.559 1.00 9.93 ? 86 PRO A CA 1 ATOM 731 C C . PRO A 1 86 ? 26.259 37.993 -6.591 1.00 8.79 ? 86 PRO A C 1 ATOM 732 O O . PRO A 1 86 ? 26.083 37.436 -7.679 1.00 11.21 ? 86 PRO A O 1 ATOM 733 C CB . PRO A 1 86 ? 25.533 40.394 -6.635 1.00 10.96 ? 86 PRO A CB 1 ATOM 734 C CG . PRO A 1 86 ? 25.353 40.654 -8.093 1.00 15.08 ? 86 PRO A CG 1 ATOM 735 C CD . PRO A 1 86 ? 26.747 40.659 -8.676 1.00 11.55 ? 86 PRO A CD 1 ATOM 736 N N . PRO A 1 87 ? 26.041 37.397 -5.413 1.00 8.39 ? 87 PRO A N 1 ATOM 737 C CA . PRO A 1 87 ? 25.642 35.988 -5.335 1.00 8.76 ? 87 PRO A CA 1 ATOM 738 C C . PRO A 1 87 ? 24.184 35.724 -5.665 1.00 9.19 ? 87 PRO A C 1 ATOM 739 O O . PRO A 1 87 ? 23.312 36.593 -5.550 1.00 12.24 ? 87 PRO A O 1 ATOM 740 C CB . PRO A 1 87 ? 25.880 35.640 -3.868 1.00 9.25 ? 87 PRO A CB 1 ATOM 741 C CG . PRO A 1 87 ? 25.656 36.957 -3.145 1.00 8.23 ? 87 PRO A CG 1 ATOM 742 C CD . PRO A 1 87 ? 26.185 38.016 -4.081 1.00 13.96 ? 87 PRO A CD 1 ATOM 743 N N . GLU A 1 88 ? 23.943 34.492 -6.094 1.00 9.25 ? 88 GLU A N 1 ATOM 744 C CA . GLU A 1 88 ? 22.617 33.903 -6.087 1.00 10.13 ? 88 GLU A CA 1 ATOM 745 C C . GLU A 1 88 ? 22.508 33.142 -4.776 1.00 10.65 ? 88 GLU A C 1 ATOM 746 O O . GLU A 1 88 ? 23.442 32.454 -4.369 1.00 13.82 ? 88 GLU A O 1 ATOM 747 C CB . GLU A 1 88 ? 22.464 32.919 -7.242 1.00 14.14 ? 88 GLU A CB 1 ATOM 748 C CG . GLU A 1 88 ? 22.614 33.546 -8.616 1.00 25.67 ? 88 GLU A CG 1 ATOM 749 C CD . GLU A 1 88 ? 22.427 32.536 -9.737 1.00 36.69 ? 88 GLU A CD 1 ATOM 750 O OE1 . GLU A 1 88 ? 22.250 31.334 -9.437 1.00 41.23 ? 88 GLU A OE1 1 ATOM 751 O OE2 . GLU A 1 88 ? 22.456 32.946 -10.915 1.00 37.85 ? 88 GLU A OE2 1 ATOM 752 N N . VAL A 1 89 ? 21.373 33.264 -4.105 1.00 10.30 ? 89 VAL A N 1 ATOM 753 C CA . VAL A 1 89 ? 21.218 32.632 -2.802 1.00 10.06 ? 89 VAL A CA 1 ATOM 754 C C . VAL A 1 89 ? 19.980 31.740 -2.791 1.00 10.91 ? 89 VAL A C 1 ATOM 755 O O . VAL A 1 89 ? 18.914 32.141 -3.251 1.00 12.85 ? 89 VAL A O 1 ATOM 756 C CB . VAL A 1 89 ? 21.092 33.701 -1.694 1.00 12.48 ? 89 VAL A CB 1 ATOM 757 C CG1 . VAL A 1 89 ? 20.917 33.045 -0.326 1.00 13.21 ? 89 VAL A CG1 1 ATOM 758 C CG2 . VAL A 1 89 ? 22.322 34.621 -1.708 1.00 12.91 ? 89 VAL A CG2 1 ATOM 759 N N . THR A 1 90 ? 20.133 30.522 -2.284 1.00 10.68 ? 90 THR A N 1 ATOM 760 C CA A THR A 1 90 ? 19.020 29.580 -2.154 0.63 11.54 ? 90 THR A CA 1 ATOM 761 C CA B THR A 1 90 ? 18.995 29.624 -2.129 0.37 13.02 ? 90 THR A CA 1 ATOM 762 C C . THR A 1 90 ? 18.991 29.021 -0.735 1.00 12.52 ? 90 THR A C 1 ATOM 763 O O . THR A 1 90 ? 20.041 28.752 -0.157 1.00 12.65 ? 90 THR A O 1 ATOM 764 C CB A THR A 1 90 ? 19.175 28.401 -3.143 0.63 11.83 ? 90 THR A CB 1 ATOM 765 C CB B THR A 1 90 ? 18.989 28.494 -3.183 0.37 15.26 ? 90 THR A CB 1 ATOM 766 O OG1 A THR A 1 90 ? 19.375 28.903 -4.468 0.63 15.15 ? 90 THR A OG1 1 ATOM 767 O OG1 B THR A 1 90 ? 20.275 27.864 -3.230 0.37 13.78 ? 90 THR A OG1 1 ATOM 768 C CG2 A THR A 1 90 ? 17.944 27.498 -3.122 0.63 17.22 ? 90 THR A CG2 1 ATOM 769 C CG2 B THR A 1 90 ? 18.650 29.044 -4.557 0.37 17.35 ? 90 THR A CG2 1 ATOM 770 N N . VAL A 1 91 ? 17.798 28.832 -0.181 1.00 13.13 ? 91 VAL A N 1 ATOM 771 C CA . VAL A 1 91 ? 17.668 28.166 1.109 1.00 12.57 ? 91 VAL A CA 1 ATOM 772 C C . VAL A 1 91 ? 16.871 26.887 0.942 1.00 13.97 ? 91 VAL A C 1 ATOM 773 O O . VAL A 1 91 ? 15.815 26.876 0.309 1.00 17.21 ? 91 VAL A O 1 ATOM 774 C CB . VAL A 1 91 ? 16.998 29.062 2.170 1.00 13.19 ? 91 VAL A CB 1 ATOM 775 C CG1 . VAL A 1 91 ? 16.693 28.266 3.439 1.00 22.79 ? 91 VAL A CG1 1 ATOM 776 C CG2 . VAL A 1 91 ? 17.896 30.236 2.485 1.00 20.18 ? 91 VAL A CG2 1 ATOM 777 N N . LEU A 1 92 ? 17.391 25.799 1.493 1.00 13.30 ? 92 LEU A N 1 ATOM 778 C CA . LEU A 1 92 ? 16.697 24.518 1.420 1.00 16.32 ? 92 LEU A CA 1 ATOM 779 C C . LEU A 1 92 ? 16.980 23.705 2.673 1.00 16.83 ? 92 LEU A C 1 ATOM 780 O O . LEU A 1 92 ? 17.837 24.071 3.473 1.00 16.90 ? 92 LEU A O 1 ATOM 781 C CB . LEU A 1 92 ? 17.122 23.745 0.169 1.00 16.29 ? 92 LEU A CB 1 ATOM 782 C CG . LEU A 1 92 ? 18.593 23.322 0.054 1.00 24.66 ? 92 LEU A CG 1 ATOM 783 C CD1 . LEU A 1 92 ? 18.711 22.137 -0.881 1.00 36.31 ? 92 LEU A CD1 1 ATOM 784 C CD2 . LEU A 1 92 ? 19.494 24.455 -0.431 1.00 25.82 ? 92 LEU A CD2 1 ATOM 785 N N . THR A 1 93 ? 16.234 22.624 2.866 1.00 15.56 ? 93 THR A N 1 ATOM 786 C CA . THR A 1 93 ? 16.522 21.718 3.971 1.00 16.17 ? 93 THR A CA 1 ATOM 787 C C . THR A 1 93 ? 17.274 20.508 3.433 1.00 18.17 ? 93 THR A C 1 ATOM 788 O O . THR A 1 93 ? 17.188 20.190 2.250 1.00 18.63 ? 93 THR A O 1 ATOM 789 C CB . THR A 1 93 ? 15.254 21.252 4.692 1.00 17.36 ? 93 THR A CB 1 ATOM 790 O OG1 . THR A 1 93 ? 14.406 20.551 3.773 1.00 19.06 ? 93 THR A OG1 1 ATOM 791 C CG2 . THR A 1 93 ? 14.495 22.454 5.276 1.00 20.31 ? 93 THR A CG2 1 ATOM 792 N N A ASN A 1 94 ? 18.009 19.866 4.335 0.53 18.29 ? 94 ASN A N 1 ATOM 793 N N B ASN A 1 94 ? 18.033 19.823 4.276 0.47 19.88 ? 94 ASN A N 1 ATOM 794 C CA A ASN A 1 94 ? 18.786 18.665 4.060 0.53 23.64 ? 94 ASN A CA 1 ATOM 795 C CA B ASN A 1 94 ? 18.758 18.664 3.766 0.47 20.34 ? 94 ASN A CA 1 ATOM 796 C C A ASN A 1 94 ? 17.874 17.501 3.695 0.53 21.55 ? 94 ASN A C 1 ATOM 797 C C B ASN A 1 94 ? 17.896 17.399 3.725 0.47 21.18 ? 94 ASN A C 1 ATOM 798 O O A ASN A 1 94 ? 18.191 16.688 2.827 0.53 19.67 ? 94 ASN A O 1 ATOM 799 O O B ASN A 1 94 ? 18.271 16.405 3.104 0.47 24.82 ? 94 ASN A O 1 ATOM 800 C CB A ASN A 1 94 ? 19.578 18.304 5.319 0.53 18.42 ? 94 ASN A CB 1 ATOM 801 C CB B ASN A 1 94 ? 20.078 18.442 4.510 0.47 23.03 ? 94 ASN A CB 1 ATOM 802 C CG A ASN A 1 94 ? 20.769 17.415 5.034 0.53 31.20 ? 94 ASN A CG 1 ATOM 803 C CG B ASN A 1 94 ? 19.881 17.925 5.915 0.47 23.35 ? 94 ASN A CG 1 ATOM 804 O OD1 A ASN A 1 94 ? 20.852 16.776 3.986 0.53 37.57 ? 94 ASN A OD1 1 ATOM 805 O OD1 B ASN A 1 94 ? 18.813 18.070 6.499 0.47 22.09 ? 94 ASN A OD1 1 ATOM 806 N ND2 A ASN A 1 94 ? 21.704 17.370 5.975 0.53 32.93 ? 94 ASN A ND2 1 ATOM 807 N ND2 B ASN A 1 94 ? 20.923 17.317 6.469 0.47 29.75 ? 94 ASN A ND2 1 ATOM 808 N N . SER A 1 95 ? 16.733 17.442 4.372 1.00 20.11 ? 95 SER A N 1 ATOM 809 C CA . SER A 1 95 ? 15.800 16.326 4.278 1.00 21.10 ? 95 SER A CA 1 ATOM 810 C C . SER A 1 95 ? 14.359 16.820 4.326 1.00 21.24 ? 95 SER A C 1 ATOM 811 O O . SER A 1 95 ? 14.110 17.955 4.730 1.00 20.41 ? 95 SER A O 1 ATOM 812 C CB . SER A 1 95 ? 16.059 15.322 5.412 1.00 25.26 ? 95 SER A CB 1 ATOM 813 O OG . SER A 1 95 ? 15.883 15.924 6.681 1.00 39.68 ? 95 SER A OG 1 ATOM 814 N N . PRO A 1 96 ? 13.402 15.977 3.891 1.00 22.51 ? 96 PRO A N 1 ATOM 815 C CA . PRO A 1 96 ? 11.995 16.380 3.976 1.00 22.98 ? 96 PRO A CA 1 ATOM 816 C C . PRO A 1 96 ? 11.625 16.777 5.393 1.00 24.97 ? 96 PRO A C 1 ATOM 817 O O . PRO A 1 96 ? 12.073 16.150 6.352 1.00 23.64 ? 96 PRO A O 1 ATOM 818 C CB . PRO A 1 96 ? 11.248 15.114 3.561 1.00 24.72 ? 96 PRO A CB 1 ATOM 819 C CG . PRO A 1 96 ? 12.191 14.426 2.642 1.00 24.89 ? 96 PRO A CG 1 ATOM 820 C CD . PRO A 1 96 ? 13.554 14.673 3.216 1.00 23.81 ? 96 PRO A CD 1 ATOM 821 N N . VAL A 1 97 ? 10.823 17.824 5.519 1.00 25.70 ? 97 VAL A N 1 ATOM 822 C CA . VAL A 1 97 ? 10.518 18.376 6.827 1.00 23.06 ? 97 VAL A CA 1 ATOM 823 C C . VAL A 1 97 ? 9.345 17.679 7.505 1.00 24.70 ? 97 VAL A C 1 ATOM 824 O O . VAL A 1 97 ? 8.283 17.495 6.913 1.00 30.80 ? 97 VAL A O 1 ATOM 825 C CB . VAL A 1 97 ? 10.246 19.885 6.736 1.00 25.46 ? 97 VAL A CB 1 ATOM 826 C CG1 . VAL A 1 97 ? 9.949 20.444 8.107 1.00 32.46 ? 97 VAL A CG1 1 ATOM 827 C CG2 . VAL A 1 97 ? 11.440 20.590 6.117 1.00 30.15 ? 97 VAL A CG2 1 ATOM 828 N N . GLU A 1 98 ? 9.564 17.273 8.749 1.00 27.06 ? 98 GLU A N 1 ATOM 829 C CA . GLU A 1 98 ? 8.504 16.756 9.598 1.00 27.63 ? 98 GLU A CA 1 ATOM 830 C C . GLU A 1 98 ? 8.543 17.517 10.912 1.00 27.37 ? 98 GLU A C 1 ATOM 831 O O . GLU A 1 98 ? 9.619 17.767 11.452 1.00 28.57 ? 98 GLU A O 1 ATOM 832 C CB . GLU A 1 98 ? 8.706 15.265 9.855 1.00 31.67 ? 98 GLU A CB 1 ATOM 833 C CG . GLU A 1 98 ? 8.735 14.416 8.601 1.00 35.23 ? 98 GLU A CG 1 ATOM 834 C CD . GLU A 1 98 ? 9.042 12.964 8.901 1.00 60.20 ? 98 GLU A CD 1 ATOM 835 O OE1 . GLU A 1 98 ? 8.205 12.095 8.570 1.00 67.56 ? 98 GLU A OE1 1 ATOM 836 O OE2 . GLU A 1 98 ? 10.122 12.691 9.470 1.00 63.65 ? 98 GLU A OE2 1 ATOM 837 N N . LEU A 1 99 ? 7.372 17.889 11.423 1.00 30.19 ? 99 LEU A N 1 ATOM 838 C CA . LEU A 1 99 ? 7.289 18.640 12.672 1.00 32.60 ? 99 LEU A CA 1 ATOM 839 C C . LEU A 1 99 ? 8.047 17.953 13.806 1.00 30.05 ? 99 LEU A C 1 ATOM 840 O O . LEU A 1 99 ? 7.954 16.737 13.980 1.00 31.00 ? 99 LEU A O 1 ATOM 841 C CB . LEU A 1 99 ? 5.829 18.883 13.064 1.00 34.82 ? 99 LEU A CB 1 ATOM 842 C CG . LEU A 1 99 ? 5.085 19.900 12.194 1.00 33.79 ? 99 LEU A CG 1 ATOM 843 C CD1 . LEU A 1 99 ? 3.655 20.085 12.680 1.00 38.55 ? 99 LEU A CD1 1 ATOM 844 C CD2 . LEU A 1 99 ? 5.829 21.238 12.159 1.00 34.56 ? 99 LEU A CD2 1 ATOM 845 N N . ARG A 1 100 ? 8.803 18.756 14.550 1.00 29.94 ? 100 ARG A N 1 ATOM 846 C CA . ARG A 1 100 ? 9.666 18.317 15.656 1.00 32.60 ? 100 ARG A CA 1 ATOM 847 C C . ARG A 1 100 ? 10.590 17.121 15.367 1.00 31.80 ? 100 ARG A C 1 ATOM 848 O O . ARG A 1 100 ? 10.968 16.381 16.275 1.00 36.07 ? 100 ARG A O 1 ATOM 849 C CB . ARG A 1 100 ? 8.879 18.145 16.968 1.00 51.34 ? 100 ARG A CB 1 ATOM 850 C CG . ARG A 1 100 ? 7.969 16.935 17.048 1.00 58.59 ? 100 ARG A CG 1 ATOM 851 C CD . ARG A 1 100 ? 6.940 17.099 18.158 1.00 65.77 ? 100 ARG A CD 1 ATOM 852 N NE . ARG A 1 100 ? 5.938 18.102 17.813 1.00 64.39 ? 100 ARG A NE 1 ATOM 853 C CZ . ARG A 1 100 ? 4.843 17.844 17.106 1.00 65.81 ? 100 ARG A CZ 1 ATOM 854 N NH1 . ARG A 1 100 ? 4.609 16.611 16.673 1.00 65.16 ? 100 ARG A NH1 1 ATOM 855 N NH2 . ARG A 1 100 ? 3.982 18.815 16.831 1.00 64.42 ? 100 ARG A NH2 1 ATOM 856 N N . GLU A 1 101 ? 10.961 16.952 14.102 1.00 29.26 ? 101 GLU A N 1 ATOM 857 C CA . GLU A 1 101 ? 12.014 16.012 13.727 1.00 29.12 ? 101 GLU A CA 1 ATOM 858 C C . GLU A 1 101 ? 13.223 16.810 13.258 1.00 27.52 ? 101 GLU A C 1 ATOM 859 O O . GLU A 1 101 ? 13.129 17.546 12.277 1.00 25.94 ? 101 GLU A O 1 ATOM 860 C CB . GLU A 1 101 ? 11.546 15.073 12.613 1.00 28.96 ? 101 GLU A CB 1 ATOM 861 C CG . GLU A 1 101 ? 10.422 14.133 13.019 1.00 32.61 ? 101 GLU A CG 1 ATOM 862 C CD . GLU A 1 101 ? 10.835 13.177 14.118 1.00 51.25 ? 101 GLU A CD 1 ATOM 863 O OE1 . GLU A 1 101 ? 12.033 12.826 14.184 1.00 50.72 ? 101 GLU A OE1 1 ATOM 864 O OE2 . GLU A 1 101 ? 9.961 12.779 14.917 1.00 57.12 ? 101 GLU A OE2 1 ATOM 865 N N . PRO A 1 102 ? 14.357 16.666 13.962 1.00 28.15 ? 102 PRO A N 1 ATOM 866 C CA . PRO A 1 102 ? 15.577 17.436 13.695 1.00 26.94 ? 102 PRO A CA 1 ATOM 867 C C . PRO A 1 102 ? 15.946 17.463 12.216 1.00 27.15 ? 102 PRO A C 1 ATOM 868 O O . PRO A 1 102 ? 15.944 16.425 11.549 1.00 25.39 ? 102 PRO A O 1 ATOM 869 C CB . PRO A 1 102 ? 16.642 16.688 14.493 1.00 32.67 ? 102 PRO A CB 1 ATOM 870 C CG . PRO A 1 102 ? 15.882 16.090 15.635 1.00 30.66 ? 102 PRO A CG 1 ATOM 871 C CD . PRO A 1 102 ? 14.540 15.714 15.074 1.00 30.37 ? 102 PRO A CD 1 ATOM 872 N N . ASN A 1 103 ? 16.251 18.658 11.716 1.00 23.58 ? 103 ASN A N 1 ATOM 873 C CA . ASN A 1 103 ? 16.596 18.853 10.314 1.00 21.96 ? 103 ASN A CA 1 ATOM 874 C C . ASN A 1 103 ? 17.708 19.899 10.222 1.00 20.85 ? 103 ASN A C 1 ATOM 875 O O . ASN A 1 103 ? 18.204 20.373 11.243 1.00 21.48 ? 103 ASN A O 1 ATOM 876 C CB . ASN A 1 103 ? 15.355 19.298 9.534 1.00 21.33 ? 103 ASN A CB 1 ATOM 877 C CG . ASN A 1 103 ? 15.397 18.901 8.064 1.00 22.63 ? 103 ASN A CG 1 ATOM 878 O OD1 . ASN A 1 103 ? 16.398 19.100 7.374 1.00 19.67 ? 103 ASN A OD1 1 ATOM 879 N ND2 . ASN A 1 103 ? 14.293 18.344 7.577 1.00 23.98 ? 103 ASN A ND2 1 ATOM 880 N N . VAL A 1 104 ? 18.115 20.246 9.006 1.00 19.43 ? 104 VAL A N 1 ATOM 881 C CA . VAL A 1 104 ? 19.152 21.255 8.821 1.00 18.37 ? 104 VAL A CA 1 ATOM 882 C C . VAL A 1 104 ? 18.781 22.182 7.674 1.00 17.40 ? 104 VAL A C 1 ATOM 883 O O . VAL A 1 104 ? 18.465 21.728 6.575 1.00 16.63 ? 104 VAL A O 1 ATOM 884 C CB . VAL A 1 104 ? 20.543 20.627 8.514 1.00 18.39 ? 104 VAL A CB 1 ATOM 885 C CG1 . VAL A 1 104 ? 21.593 21.717 8.347 1.00 17.39 ? 104 VAL A CG1 1 ATOM 886 C CG2 . VAL A 1 104 ? 20.958 19.654 9.613 1.00 20.46 ? 104 VAL A CG2 1 ATOM 887 N N . LEU A 1 105 ? 18.804 23.483 7.936 1.00 16.44 ? 105 LEU A N 1 ATOM 888 C CA . LEU A 1 105 ? 18.670 24.458 6.866 1.00 15.26 ? 105 LEU A CA 1 ATOM 889 C C . LEU A 1 105 ? 20.020 24.693 6.210 1.00 14.27 ? 105 LEU A C 1 ATOM 890 O O . LEU A 1 105 ? 21.034 24.806 6.895 1.00 14.76 ? 105 LEU A O 1 ATOM 891 C CB . LEU A 1 105 ? 18.114 25.778 7.411 1.00 15.46 ? 105 LEU A CB 1 ATOM 892 C CG . LEU A 1 105 ? 16.607 25.744 7.645 1.00 17.32 ? 105 LEU A CG 1 ATOM 893 C CD1 . LEU A 1 105 ? 16.169 26.917 8.504 1.00 25.63 ? 105 LEU A CD1 1 ATOM 894 C CD2 . LEU A 1 105 ? 15.882 25.767 6.313 1.00 22.22 ? 105 LEU A CD2 1 ATOM 895 N N . ILE A 1 106 ? 20.026 24.749 4.882 1.00 13.46 ? 106 ILE A N 1 ATOM 896 C CA . ILE A 1 106 ? 21.241 25.034 4.126 1.00 12.57 ? 106 ILE A CA 1 ATOM 897 C C . ILE A 1 106 ? 21.043 26.338 3.383 1.00 12.53 ? 106 ILE A C 1 ATOM 898 O O . ILE A 1 106 ? 20.029 26.527 2.710 1.00 13.10 ? 106 ILE A O 1 ATOM 899 C CB . ILE A 1 106 ? 21.538 23.936 3.092 1.00 13.37 ? 106 ILE A CB 1 ATOM 900 C CG1 . ILE A 1 106 ? 21.554 22.566 3.762 1.00 13.78 ? 106 ILE A CG1 1 ATOM 901 C CG2 . ILE A 1 106 ? 22.871 24.208 2.386 1.00 13.96 ? 106 ILE A CG2 1 ATOM 902 C CD1 . ILE A 1 106 ? 21.612 21.395 2.774 1.00 15.83 ? 106 ILE A CD1 1 ATOM 903 N N . CYS A 1 107 ? 22.004 27.243 3.522 1.00 11.20 ? 107 CYS A N 1 ATOM 904 C CA . CYS A 1 107 ? 21.998 28.466 2.742 1.00 10.55 ? 107 CYS A CA 1 ATOM 905 C C . CYS A 1 107 ? 23.110 28.322 1.726 1.00 12.75 ? 107 CYS A C 1 ATOM 906 O O . CYS A 1 107 ? 24.281 28.211 2.089 1.00 12.60 ? 107 CYS A O 1 ATOM 907 C CB . CYS A 1 107 ? 22.247 29.668 3.636 1.00 10.70 ? 107 CYS A CB 1 ATOM 908 S SG . CYS A 1 107 ? 22.123 31.239 2.755 1.00 13.48 ? 107 CYS A SG 1 ATOM 909 N N . PHE A 1 108 ? 22.745 28.271 0.454 1.00 10.56 ? 108 PHE A N 1 ATOM 910 C CA . PHE A 1 108 ? 23.738 28.093 -0.592 1.00 9.57 ? 108 PHE A CA 1 ATOM 911 C C . PHE A 1 108 ? 23.964 29.439 -1.259 1.00 10.80 ? 108 PHE A C 1 ATOM 912 O O . PHE A 1 108 ? 23.031 30.042 -1.786 1.00 10.37 ? 108 PHE A O 1 ATOM 913 C CB . PHE A 1 108 ? 23.252 27.072 -1.612 1.00 11.17 ? 108 PHE A CB 1 ATOM 914 C CG . PHE A 1 108 ? 24.237 26.804 -2.718 1.00 15.96 ? 108 PHE A CG 1 ATOM 915 C CD1 . PHE A 1 108 ? 25.590 26.665 -2.444 1.00 19.17 ? 108 PHE A CD1 1 ATOM 916 C CD2 . PHE A 1 108 ? 23.805 26.668 -4.024 1.00 19.57 ? 108 PHE A CD2 1 ATOM 917 C CE1 . PHE A 1 108 ? 26.495 26.406 -3.458 1.00 23.71 ? 108 PHE A CE1 1 ATOM 918 C CE2 . PHE A 1 108 ? 24.702 26.406 -5.044 1.00 16.06 ? 108 PHE A CE2 1 ATOM 919 C CZ . PHE A 1 108 ? 26.048 26.266 -4.761 1.00 16.22 ? 108 PHE A CZ 1 ATOM 920 N N . ILE A 1 109 ? 25.205 29.911 -1.218 1.00 8.13 ? 109 ILE A N 1 ATOM 921 C CA . ILE A 1 109 ? 25.551 31.218 -1.765 1.00 10.52 ? 109 ILE A CA 1 ATOM 922 C C . ILE A 1 109 ? 26.465 30.941 -2.949 1.00 11.58 ? 109 ILE A C 1 ATOM 923 O O . ILE A 1 109 ? 27.508 30.326 -2.783 1.00 10.76 ? 109 ILE A O 1 ATOM 924 C CB . ILE A 1 109 ? 26.275 32.059 -0.698 1.00 8.39 ? 109 ILE A CB 1 ATOM 925 C CG1 . ILE A 1 109 ? 25.416 32.152 0.567 1.00 10.25 ? 109 ILE A CG1 1 ATOM 926 C CG2 . ILE A 1 109 ? 26.588 33.447 -1.218 1.00 9.64 ? 109 ILE A CG2 1 ATOM 927 C CD1 . ILE A 1 109 ? 25.810 31.195 1.668 1.00 25.81 ? 109 ILE A CD1 1 ATOM 928 N N . ASP A 1 110 ? 26.065 31.364 -4.143 1.00 8.88 ? 110 ASP A N 1 ATOM 929 C CA . ASP A 1 110 ? 26.693 30.845 -5.360 1.00 7.79 ? 110 ASP A CA 1 ATOM 930 C C . ASP A 1 110 ? 27.005 31.938 -6.370 1.00 9.48 ? 110 ASP A C 1 ATOM 931 O O . ASP A 1 110 ? 26.371 32.995 -6.366 1.00 8.84 ? 110 ASP A O 1 ATOM 932 C CB . ASP A 1 110 ? 25.746 29.815 -5.994 1.00 10.07 ? 110 ASP A CB 1 ATOM 933 C CG . ASP A 1 110 ? 26.419 28.912 -7.015 1.00 14.97 ? 110 ASP A CG 1 ATOM 934 O OD1 . ASP A 1 110 ? 27.666 28.829 -7.055 1.00 12.10 ? 110 ASP A OD1 1 ATOM 935 O OD2 . ASP A 1 110 ? 25.678 28.242 -7.777 1.00 17.00 ? 110 ASP A OD2 1 ATOM 936 N N . LYS A 1 111 ? 28.011 31.673 -7.205 1.00 7.79 ? 111 LYS A N 1 ATOM 937 C CA A LYS A 1 111 ? 28.303 32.487 -8.387 0.41 8.07 ? 111 LYS A CA 1 ATOM 938 C CA B LYS A 1 111 ? 28.307 32.476 -8.390 0.59 8.07 ? 111 LYS A CA 1 ATOM 939 C C . LYS A 1 111 ? 28.665 33.929 -8.050 1.00 11.30 ? 111 LYS A C 1 ATOM 940 O O . LYS A 1 111 ? 28.123 34.871 -8.643 1.00 9.81 ? 111 LYS A O 1 ATOM 941 C CB A LYS A 1 111 ? 27.121 32.477 -9.367 0.41 13.33 ? 111 LYS A CB 1 ATOM 942 C CB B LYS A 1 111 ? 27.133 32.399 -9.386 0.59 9.19 ? 111 LYS A CB 1 ATOM 943 C CG A LYS A 1 111 ? 26.671 31.104 -9.824 0.41 10.05 ? 111 LYS A CG 1 ATOM 944 C CG B LYS A 1 111 ? 27.528 32.562 -10.851 0.59 10.65 ? 111 LYS A CG 1 ATOM 945 C CD A LYS A 1 111 ? 25.692 31.211 -10.991 0.41 18.40 ? 111 LYS A CD 1 ATOM 946 C CD B LYS A 1 111 ? 26.420 32.115 -11.818 0.59 18.56 ? 111 LYS A CD 1 ATOM 947 C CE A LYS A 1 111 ? 25.265 29.845 -11.510 0.41 22.09 ? 111 LYS A CE 1 ATOM 948 C CE B LYS A 1 111 ? 26.906 32.140 -13.277 0.59 25.61 ? 111 LYS A CE 1 ATOM 949 N NZ A LYS A 1 111 ? 24.332 29.153 -10.582 0.41 21.65 ? 111 LYS A NZ 1 ATOM 950 N NZ B LYS A 1 111 ? 25.848 31.722 -14.266 0.59 14.80 ? 111 LYS A NZ 1 ATOM 951 N N . PHE A 1 112 ? 29.589 34.106 -7.107 1.00 6.82 ? 112 PHE A N 1 ATOM 952 C CA . PHE A 1 112 ? 29.949 35.457 -6.687 1.00 7.93 ? 112 PHE A CA 1 ATOM 953 C C . PHE A 1 112 ? 31.456 35.682 -6.612 1.00 8.09 ? 112 PHE A C 1 ATOM 954 O O . PHE A 1 112 ? 32.241 34.735 -6.520 1.00 6.60 ? 112 PHE A O 1 ATOM 955 C CB . PHE A 1 112 ? 29.305 35.802 -5.339 1.00 7.70 ? 112 PHE A CB 1 ATOM 956 C CG . PHE A 1 112 ? 29.833 35.000 -4.184 1.00 7.95 ? 112 PHE A CG 1 ATOM 957 C CD1 . PHE A 1 112 ? 30.856 35.497 -3.388 1.00 9.65 ? 112 PHE A CD1 1 ATOM 958 C CD2 . PHE A 1 112 ? 29.302 33.749 -3.891 1.00 8.39 ? 112 PHE A CD2 1 ATOM 959 C CE1 . PHE A 1 112 ? 31.353 34.758 -2.329 1.00 8.63 ? 112 PHE A CE1 1 ATOM 960 C CE2 . PHE A 1 112 ? 29.797 33.002 -2.835 1.00 10.35 ? 112 PHE A CE2 1 ATOM 961 C CZ . PHE A 1 112 ? 30.805 33.515 -2.038 1.00 8.57 ? 112 PHE A CZ 1 ATOM 962 N N . THR A 1 113 ? 31.839 36.954 -6.650 1.00 7.16 ? 113 THR A N 1 ATOM 963 C CA . THR A 1 113 ? 33.214 37.362 -6.392 1.00 7.42 ? 113 THR A CA 1 ATOM 964 C C . THR A 1 113 ? 33.197 38.859 -6.084 1.00 7.95 ? 113 THR A C 1 ATOM 965 O O . THR A 1 113 ? 32.311 39.569 -6.551 1.00 8.16 ? 113 THR A O 1 ATOM 966 C CB . THR A 1 113 ? 34.152 37.018 -7.571 1.00 9.47 ? 113 THR A CB 1 ATOM 967 O OG1 . THR A 1 113 ? 35.505 36.962 -7.102 1.00 8.81 ? 113 THR A OG1 1 ATOM 968 C CG2 . THR A 1 113 ? 34.027 38.035 -8.709 1.00 9.18 ? 113 THR A CG2 1 ATOM 969 N N . PRO A 1 114 ? 34.146 39.349 -5.270 1.00 8.52 ? 114 PRO A N 1 ATOM 970 C CA . PRO A 1 114 ? 35.256 38.658 -4.604 1.00 8.74 ? 114 PRO A CA 1 ATOM 971 C C . PRO A 1 114 ? 34.764 37.736 -3.499 1.00 8.84 ? 114 PRO A C 1 ATOM 972 O O . PRO A 1 114 ? 33.594 37.818 -3.095 1.00 9.28 ? 114 PRO A O 1 ATOM 973 C CB . PRO A 1 114 ? 36.094 39.813 -4.030 1.00 10.26 ? 114 PRO A CB 1 ATOM 974 C CG . PRO A 1 114 ? 35.144 40.936 -3.867 1.00 10.86 ? 114 PRO A CG 1 ATOM 975 C CD . PRO A 1 114 ? 34.150 40.798 -4.996 1.00 10.37 ? 114 PRO A CD 1 ATOM 976 N N . PRO A 1 115 ? 35.642 36.848 -3.025 1.00 9.02 ? 115 PRO A N 1 ATOM 977 C CA . PRO A 1 115 ? 35.282 35.901 -1.968 1.00 10.79 ? 115 PRO A CA 1 ATOM 978 C C . PRO A 1 115 ? 35.261 36.540 -0.573 1.00 12.70 ? 115 PRO A C 1 ATOM 979 O O . PRO A 1 115 ? 36.105 36.250 0.290 1.00 11.52 ? 115 PRO A O 1 ATOM 980 C CB . PRO A 1 115 ? 36.380 34.836 -2.083 1.00 9.65 ? 115 PRO A CB 1 ATOM 981 C CG . PRO A 1 115 ? 37.583 35.600 -2.603 1.00 9.79 ? 115 PRO A CG 1 ATOM 982 C CD . PRO A 1 115 ? 36.996 36.595 -3.566 1.00 9.05 ? 115 PRO A CD 1 ATOM 983 N N . VAL A 1 116 ? 34.299 37.442 -0.374 1.00 10.26 ? 116 VAL A N 1 ATOM 984 C CA . VAL A 1 116 ? 34.042 38.071 0.917 1.00 11.16 ? 116 VAL A CA 1 ATOM 985 C C . VAL A 1 116 ? 32.536 38.231 1.029 1.00 12.49 ? 116 VAL A C 1 ATOM 986 O O . VAL A 1 116 ? 31.914 38.829 0.154 1.00 12.89 ? 116 VAL A O 1 ATOM 987 C CB . VAL A 1 116 ? 34.657 39.477 1.024 1.00 13.46 ? 116 VAL A CB 1 ATOM 988 C CG1 . VAL A 1 116 ? 34.393 40.074 2.412 1.00 17.06 ? 116 VAL A CG1 1 ATOM 989 C CG2 . VAL A 1 116 ? 36.149 39.443 0.737 1.00 15.20 ? 116 VAL A CG2 1 ATOM 990 N N . VAL A 1 117 ? 31.955 37.690 2.094 1.00 12.54 ? 117 VAL A N 1 ATOM 991 C CA A VAL A 1 117 ? 30.518 37.769 2.304 0.71 11.08 ? 117 VAL A CA 1 ATOM 992 C CA B VAL A 1 117 ? 30.507 37.764 2.307 0.29 14.84 ? 117 VAL A CA 1 ATOM 993 C C . VAL A 1 117 ? 30.208 37.787 3.805 1.00 17.49 ? 117 VAL A C 1 ATOM 994 O O . VAL A 1 117 ? 30.954 37.221 4.603 1.00 17.77 ? 117 VAL A O 1 ATOM 995 C CB A VAL A 1 117 ? 29.810 36.580 1.604 0.71 13.72 ? 117 VAL A CB 1 ATOM 996 C CB B VAL A 1 117 ? 29.753 36.561 1.648 0.29 17.38 ? 117 VAL A CB 1 ATOM 997 C CG1 A VAL A 1 117 ? 30.113 35.247 2.320 0.71 10.41 ? 117 VAL A CG1 1 ATOM 998 C CG1 B VAL A 1 117 ? 28.293 36.542 2.037 0.29 23.06 ? 117 VAL A CG1 1 ATOM 999 C CG2 A VAL A 1 117 ? 28.329 36.819 1.507 0.71 22.69 ? 117 VAL A CG2 1 ATOM 1000 C CG2 B VAL A 1 117 ? 29.843 36.605 0.144 0.29 9.46 ? 117 VAL A CG2 1 ATOM 1001 N N . ASN A 1 118 ? 29.131 38.468 4.193 1.00 14.25 ? 118 ASN A N 1 ATOM 1002 C CA . ASN A 1 118 ? 28.609 38.350 5.554 1.00 13.01 ? 118 ASN A CA 1 ATOM 1003 C C . ASN A 1 118 ? 27.309 37.560 5.465 1.00 15.21 ? 118 ASN A C 1 ATOM 1004 O O . ASN A 1 118 ? 26.427 37.910 4.682 1.00 17.77 ? 118 ASN A O 1 ATOM 1005 C CB . ASN A 1 118 ? 28.326 39.722 6.174 1.00 17.19 ? 118 ASN A CB 1 ATOM 1006 C CG . ASN A 1 118 ? 29.580 40.535 6.390 1.00 22.44 ? 118 ASN A CG 1 ATOM 1007 O OD1 . ASN A 1 118 ? 30.625 39.997 6.751 1.00 27.37 ? 118 ASN A OD1 1 ATOM 1008 N ND2 . ASN A 1 118 ? 29.482 41.843 6.156 1.00 28.67 ? 118 ASN A ND2 1 ATOM 1009 N N . VAL A 1 119 ? 27.197 36.482 6.238 1.00 15.50 ? 119 VAL A N 1 ATOM 1010 C CA . VAL A 1 119 ? 25.988 35.663 6.221 1.00 12.25 ? 119 VAL A CA 1 ATOM 1011 C C . VAL A 1 119 ? 25.419 35.542 7.628 1.00 14.28 ? 119 VAL A C 1 ATOM 1012 O O . VAL A 1 119 ? 26.145 35.213 8.569 1.00 17.84 ? 119 VAL A O 1 ATOM 1013 C CB . VAL A 1 119 ? 26.259 34.239 5.670 1.00 13.34 ? 119 VAL A CB 1 ATOM 1014 C CG1 . VAL A 1 119 ? 24.993 33.421 5.682 1.00 12.27 ? 119 VAL A CG1 1 ATOM 1015 C CG2 . VAL A 1 119 ? 26.808 34.307 4.257 1.00 14.74 ? 119 VAL A CG2 1 ATOM 1016 N N . THR A 1 120 ? 24.127 35.828 7.772 1.00 13.09 ? 120 THR A N 1 ATOM 1017 C CA . THR A 1 120 ? 23.451 35.706 9.062 1.00 14.21 ? 120 THR A CA 1 ATOM 1018 C C . THR A 1 120 ? 22.185 34.871 8.934 1.00 14.93 ? 120 THR A C 1 ATOM 1019 O O . THR A 1 120 ? 21.399 35.061 8.006 1.00 14.18 ? 120 THR A O 1 ATOM 1020 C CB . THR A 1 120 ? 23.044 37.080 9.627 1.00 17.01 ? 120 THR A CB 1 ATOM 1021 O OG1 . THR A 1 120 ? 24.174 37.959 9.629 1.00 18.75 ? 120 THR A OG1 1 ATOM 1022 C CG2 . THR A 1 120 ? 22.523 36.935 11.045 1.00 19.39 ? 120 THR A CG2 1 ATOM 1023 N N . TRP A 1 121 ? 22.001 33.939 9.863 1.00 15.72 ? 121 TRP A N 1 ATOM 1024 C CA . TRP A 1 121 ? 20.749 33.212 9.976 1.00 13.93 ? 121 TRP A CA 1 ATOM 1025 C C . TRP A 1 121 ? 19.817 33.982 10.885 1.00 14.59 ? 121 TRP A C 1 ATOM 1026 O O . TRP A 1 121 ? 20.221 34.419 11.960 1.00 15.48 ? 121 TRP A O 1 ATOM 1027 C CB . TRP A 1 121 ? 20.979 31.844 10.608 1.00 14.34 ? 121 TRP A CB 1 ATOM 1028 C CG . TRP A 1 121 ? 21.564 30.827 9.695 1.00 15.61 ? 121 TRP A CG 1 ATOM 1029 C CD1 . TRP A 1 121 ? 22.822 30.315 9.750 1.00 13.98 ? 121 TRP A CD1 1 ATOM 1030 C CD2 . TRP A 1 121 ? 20.905 30.167 8.607 1.00 14.55 ? 121 TRP A CD2 1 ATOM 1031 N NE1 . TRP A 1 121 ? 22.997 29.381 8.759 1.00 15.38 ? 121 TRP A NE1 1 ATOM 1032 C CE2 . TRP A 1 121 ? 21.833 29.267 8.042 1.00 12.92 ? 121 TRP A CE2 1 ATOM 1033 C CE3 . TRP A 1 121 ? 19.622 30.253 8.051 1.00 15.75 ? 121 TRP A CE3 1 ATOM 1034 C CZ2 . TRP A 1 121 ? 21.525 28.452 6.949 1.00 13.00 ? 121 TRP A CZ2 1 ATOM 1035 C CZ3 . TRP A 1 121 ? 19.314 29.446 6.959 1.00 15.14 ? 121 TRP A CZ3 1 ATOM 1036 C CH2 . TRP A 1 121 ? 20.264 28.559 6.421 1.00 18.84 ? 121 TRP A CH2 1 ATOM 1037 N N . LEU A 1 122 ? 18.565 34.130 10.464 1.00 14.34 ? 122 LEU A N 1 ATOM 1038 C CA . LEU A 1 122 ? 17.572 34.821 11.272 1.00 14.94 ? 122 LEU A CA 1 ATOM 1039 C C . LEU A 1 122 ? 16.440 33.870 11.598 1.00 15.75 ? 122 LEU A C 1 ATOM 1040 O O . LEU A 1 122 ? 15.946 33.166 10.716 1.00 16.62 ? 122 LEU A O 1 ATOM 1041 C CB . LEU A 1 122 ? 17.011 36.025 10.505 1.00 14.68 ? 122 LEU A CB 1 ATOM 1042 C CG . LEU A 1 122 ? 18.014 37.102 10.094 1.00 17.53 ? 122 LEU A CG 1 ATOM 1043 C CD1 . LEU A 1 122 ? 17.374 38.036 9.080 1.00 16.61 ? 122 LEU A CD1 1 ATOM 1044 C CD2 . LEU A 1 122 ? 18.501 37.884 11.309 1.00 19.22 ? 122 LEU A CD2 1 ATOM 1045 N N . ARG A 1 123 ? 16.046 33.843 12.865 1.00 15.94 ? 123 ARG A N 1 ATOM 1046 C CA . ARG A 1 123 ? 14.879 33.087 13.289 1.00 16.21 ? 123 ARG A CA 1 ATOM 1047 C C . ARG A 1 123 ? 13.877 34.076 13.862 1.00 19.51 ? 123 ARG A C 1 ATOM 1048 O O . ARG A 1 123 ? 14.167 34.752 14.847 1.00 17.58 ? 123 ARG A O 1 ATOM 1049 C CB . ARG A 1 123 ? 15.247 32.047 14.350 1.00 16.92 ? 123 ARG A CB 1 ATOM 1050 C CG . ARG A 1 123 ? 14.038 31.299 14.915 1.00 18.73 ? 123 ARG A CG 1 ATOM 1051 C CD . ARG A 1 123 ? 14.386 30.437 16.127 1.00 22.82 ? 123 ARG A CD 1 ATOM 1052 N NE . ARG A 1 123 ? 15.257 29.319 15.777 1.00 37.49 ? 123 ARG A NE 1 ATOM 1053 C CZ . ARG A 1 123 ? 15.261 28.146 16.405 1.00 56.14 ? 123 ARG A CZ 1 ATOM 1054 N NH1 . ARG A 1 123 ? 14.430 27.927 17.416 1.00 59.87 ? 123 ARG A NH1 1 ATOM 1055 N NH2 . ARG A 1 123 ? 16.090 27.184 16.012 1.00 42.51 ? 123 ARG A NH2 1 ATOM 1056 N N . ASN A 1 124 ? 12.708 34.163 13.235 1.00 16.91 ? 124 ASN A N 1 ATOM 1057 C CA . ASN A 1 124 ? 11.707 35.163 13.605 1.00 18.66 ? 124 ASN A CA 1 ATOM 1058 C C . ASN A 1 124 ? 12.287 36.576 13.626 1.00 19.78 ? 124 ASN A C 1 ATOM 1059 O O . ASN A 1 124 ? 11.960 37.384 14.498 1.00 19.37 ? 124 ASN A O 1 ATOM 1060 C CB . ASN A 1 124 ? 11.062 34.803 14.944 1.00 19.80 ? 124 ASN A CB 1 ATOM 1061 C CG . ASN A 1 124 ? 10.445 33.421 14.927 1.00 22.85 ? 124 ASN A CG 1 ATOM 1062 O OD1 . ASN A 1 124 ? 9.880 32.999 13.915 1.00 21.09 ? 124 ASN A OD1 1 ATOM 1063 N ND2 . ASN A 1 124 ? 10.559 32.704 16.036 1.00 24.84 ? 124 ASN A ND2 1 ATOM 1064 N N . GLY A 1 125 ? 13.157 36.858 12.659 1.00 16.60 ? 125 GLY A N 1 ATOM 1065 C CA . GLY A 1 125 ? 13.746 38.179 12.509 1.00 20.09 ? 125 GLY A CA 1 ATOM 1066 C C . GLY A 1 125 ? 14.923 38.483 13.419 1.00 18.60 ? 125 GLY A C 1 ATOM 1067 O O . GLY A 1 125 ? 15.427 39.606 13.411 1.00 18.28 ? 125 GLY A O 1 ATOM 1068 N N . LYS A 1 126 ? 15.361 37.492 14.197 1.00 17.76 ? 126 LYS A N 1 ATOM 1069 C CA . LYS A 1 126 ? 16.468 37.667 15.138 1.00 18.59 ? 126 LYS A CA 1 ATOM 1070 C C . LYS A 1 126 ? 17.648 36.778 14.768 1.00 18.07 ? 126 LYS A C 1 ATOM 1071 O O . LYS A 1 126 ? 17.454 35.621 14.404 1.00 17.53 ? 126 LYS A O 1 ATOM 1072 C CB . LYS A 1 126 ? 16.014 37.322 16.560 1.00 19.68 ? 126 LYS A CB 1 ATOM 1073 C CG . LYS A 1 126 ? 14.806 38.115 17.046 1.00 20.33 ? 126 LYS A CG 1 ATOM 1074 C CD . LYS A 1 126 ? 14.509 37.804 18.506 1.00 25.97 ? 126 LYS A CD 1 ATOM 1075 C CE . LYS A 1 126 ? 13.275 38.543 19.000 1.00 35.75 ? 126 LYS A CE 1 ATOM 1076 N NZ . LYS A 1 126 ? 13.042 38.313 20.460 1.00 38.14 ? 126 LYS A NZ 1 ATOM 1077 N N . PRO A 1 127 ? 18.877 37.314 14.863 1.00 18.43 ? 127 PRO A N 1 ATOM 1078 C CA . PRO A 1 127 ? 20.080 36.546 14.518 1.00 18.04 ? 127 PRO A CA 1 ATOM 1079 C C . PRO A 1 127 ? 20.242 35.335 15.428 1.00 18.59 ? 127 PRO A C 1 ATOM 1080 O O . PRO A 1 127 ? 20.053 35.439 16.643 1.00 21.46 ? 127 PRO A O 1 ATOM 1081 C CB . PRO A 1 127 ? 21.221 37.541 14.763 1.00 23.57 ? 127 PRO A CB 1 ATOM 1082 C CG . PRO A 1 127 ? 20.579 38.891 14.690 1.00 27.65 ? 127 PRO A CG 1 ATOM 1083 C CD . PRO A 1 127 ? 19.198 38.702 15.244 1.00 26.53 ? 127 PRO A CD 1 ATOM 1084 N N . VAL A 1 128 ? 20.569 34.189 14.840 1.00 19.03 ? 128 VAL A N 1 ATOM 1085 C CA . VAL A 1 128 ? 20.826 32.987 15.623 1.00 20.49 ? 128 VAL A CA 1 ATOM 1086 C C . VAL A 1 128 ? 22.166 32.378 15.240 1.00 24.98 ? 128 VAL A C 1 ATOM 1087 O O . VAL A 1 128 ? 22.548 32.386 14.071 1.00 30.68 ? 128 VAL A O 1 ATOM 1088 C CB . VAL A 1 128 ? 19.692 31.945 15.484 1.00 28.67 ? 128 VAL A CB 1 ATOM 1089 C CG1 . VAL A 1 128 ? 18.452 32.415 16.225 1.00 37.14 ? 128 VAL A CG1 1 ATOM 1090 C CG2 . VAL A 1 128 ? 19.365 31.691 14.029 1.00 23.29 ? 128 VAL A CG2 1 ATOM 1091 N N . THR A 1 129 ? 22.888 31.867 16.235 1.00 26.57 ? 129 THR A N 1 ATOM 1092 C CA . THR A 1 129 ? 24.235 31.350 16.005 1.00 28.83 ? 129 THR A CA 1 ATOM 1093 C C . THR A 1 129 ? 24.453 29.983 16.644 1.00 38.92 ? 129 THR A C 1 ATOM 1094 O O . THR A 1 129 ? 25.474 29.339 16.410 1.00 33.59 ? 129 THR A O 1 ATOM 1095 C CB . THR A 1 129 ? 25.316 32.306 16.550 1.00 34.11 ? 129 THR A CB 1 ATOM 1096 O OG1 . THR A 1 129 ? 25.194 32.403 17.974 1.00 36.79 ? 129 THR A OG1 1 ATOM 1097 C CG2 . THR A 1 129 ? 25.179 33.690 15.937 1.00 34.21 ? 129 THR A CG2 1 ATOM 1098 N N . THR A 1 130 ? 23.506 29.542 17.460 1.00 41.70 ? 130 THR A N 1 ATOM 1099 C CA . THR A 1 130 ? 23.663 28.262 18.133 1.00 36.30 ? 130 THR A CA 1 ATOM 1100 C C . THR A 1 130 ? 23.662 27.114 17.131 1.00 33.40 ? 130 THR A C 1 ATOM 1101 O O . THR A 1 130 ? 22.678 26.885 16.427 1.00 34.87 ? 130 THR A O 1 ATOM 1102 C CB . THR A 1 130 ? 22.581 28.036 19.206 1.00 38.71 ? 130 THR A CB 1 ATOM 1103 O OG1 . THR A 1 130 ? 22.738 29.009 20.247 1.00 38.00 ? 130 THR A OG1 1 ATOM 1104 C CG2 . THR A 1 130 ? 22.713 26.643 19.808 1.00 36.82 ? 130 THR A CG2 1 ATOM 1105 N N . GLY A 1 131 ? 24.787 26.416 17.055 1.00 27.73 ? 131 GLY A N 1 ATOM 1106 C CA . GLY A 1 131 ? 24.887 25.224 16.239 1.00 28.28 ? 131 GLY A CA 1 ATOM 1107 C C . GLY A 1 131 ? 25.201 25.481 14.780 1.00 28.61 ? 131 GLY A C 1 ATOM 1108 O O . GLY A 1 131 ? 25.302 24.538 13.994 1.00 29.64 ? 131 GLY A O 1 ATOM 1109 N N . VAL A 1 132 ? 25.371 26.746 14.408 1.00 20.07 ? 132 VAL A N 1 ATOM 1110 C CA . VAL A 1 132 ? 25.627 27.076 13.004 1.00 21.32 ? 132 VAL A CA 1 ATOM 1111 C C . VAL A 1 132 ? 27.019 26.642 12.567 1.00 19.49 ? 132 VAL A C 1 ATOM 1112 O O . VAL A 1 132 ? 27.930 26.518 13.385 1.00 25.01 ? 132 VAL A O 1 ATOM 1113 C CB . VAL A 1 132 ? 25.447 28.581 12.696 1.00 21.72 ? 132 VAL A CB 1 ATOM 1114 C CG1 . VAL A 1 132 ? 24.036 29.032 13.019 1.00 21.23 ? 132 VAL A CG1 1 ATOM 1115 C CG2 . VAL A 1 132 ? 26.479 29.420 13.438 1.00 28.11 ? 132 VAL A CG2 1 ATOM 1116 N N . SER A 1 133 ? 27.172 26.395 11.272 1.00 16.83 ? 133 SER A N 1 ATOM 1117 C CA . SER A 1 133 ? 28.473 26.075 10.699 1.00 17.71 ? 133 SER A CA 1 ATOM 1118 C C . SER A 1 133 ? 28.526 26.570 9.260 1.00 15.48 ? 133 SER A C 1 ATOM 1119 O O . SER A 1 133 ? 27.519 27.013 8.712 1.00 14.95 ? 133 SER A O 1 ATOM 1120 C CB . SER A 1 133 ? 28.744 24.573 10.757 1.00 18.83 ? 133 SER A CB 1 ATOM 1121 O OG . SER A 1 133 ? 27.790 23.846 10.002 1.00 18.63 ? 133 SER A OG 1 ATOM 1122 N N . GLU A 1 134 ? 29.704 26.511 8.650 1.00 15.35 ? 134 GLU A N 1 ATOM 1123 C CA . GLU A 1 134 ? 29.868 27.052 7.307 1.00 14.19 ? 134 GLU A CA 1 ATOM 1124 C C . GLU A 1 134 ? 31.101 26.474 6.641 1.00 14.22 ? 134 GLU A C 1 ATOM 1125 O O . GLU A 1 134 ? 32.010 25.993 7.315 1.00 16.95 ? 134 GLU A O 1 ATOM 1126 C CB . GLU A 1 134 ? 30.006 28.573 7.364 1.00 15.14 ? 134 GLU A CB 1 ATOM 1127 C CG . GLU A 1 134 ? 31.341 29.048 7.932 1.00 16.59 ? 134 GLU A CG 1 ATOM 1128 C CD . GLU A 1 134 ? 31.353 30.539 8.213 1.00 24.78 ? 134 GLU A CD 1 ATOM 1129 O OE1 . GLU A 1 134 ? 30.636 30.974 9.135 1.00 24.02 ? 134 GLU A OE1 1 ATOM 1130 O OE2 . GLU A 1 134 ? 32.069 31.275 7.503 1.00 26.37 ? 134 GLU A OE2 1 ATOM 1131 N N . THR A 1 135 ? 31.128 26.523 5.315 1.00 13.25 ? 135 THR A N 1 ATOM 1132 C CA . THR A 1 135 ? 32.313 26.118 4.570 1.00 13.21 ? 135 THR A CA 1 ATOM 1133 C C . THR A 1 135 ? 33.183 27.323 4.264 1.00 13.42 ? 135 THR A C 1 ATOM 1134 O O . THR A 1 135 ? 32.747 28.467 4.400 1.00 14.06 ? 135 THR A O 1 ATOM 1135 C CB . THR A 1 135 ? 31.942 25.453 3.231 1.00 12.48 ? 135 THR A CB 1 ATOM 1136 O OG1 . THR A 1 135 ? 31.406 26.433 2.335 1.00 11.46 ? 135 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 135 ? 30.918 24.340 3.448 1.00 12.85 ? 135 THR A CG2 1 ATOM 1138 N N . VAL A 1 136 ? 34.417 27.065 3.841 1.00 13.27 ? 136 VAL A N 1 ATOM 1139 C CA . VAL A 1 136 ? 35.223 28.120 3.246 1.00 12.65 ? 136 VAL A CA 1 ATOM 1140 C C . VAL A 1 136 ? 34.683 28.459 1.860 1.00 13.93 ? 136 VAL A C 1 ATOM 1141 O O . VAL A 1 136 ? 33.664 27.914 1.417 1.00 12.95 ? 136 VAL A O 1 ATOM 1142 C CB . VAL A 1 136 ? 36.703 27.728 3.152 1.00 15.13 ? 136 VAL A CB 1 ATOM 1143 C CG1 . VAL A 1 136 ? 37.256 27.473 4.542 1.00 17.69 ? 136 VAL A CG1 1 ATOM 1144 C CG2 . VAL A 1 136 ? 36.886 26.502 2.259 1.00 15.68 ? 136 VAL A CG2 1 ATOM 1145 N N . PHE A 1 137 ? 35.361 29.367 1.173 1.00 12.64 ? 137 PHE A N 1 ATOM 1146 C CA . PHE A 1 137 ? 34.967 29.722 -0.182 1.00 12.35 ? 137 PHE A CA 1 ATOM 1147 C C . PHE A 1 137 ? 35.403 28.625 -1.130 1.00 14.46 ? 137 PHE A C 1 ATOM 1148 O O . PHE A 1 137 ? 36.554 28.199 -1.119 1.00 18.10 ? 137 PHE A O 1 ATOM 1149 C CB . PHE A 1 137 ? 35.560 31.078 -0.581 1.00 11.70 ? 137 PHE A CB 1 ATOM 1150 C CG . PHE A 1 137 ? 35.040 32.221 0.244 1.00 10.32 ? 137 PHE A CG 1 ATOM 1151 C CD1 . PHE A 1 137 ? 35.701 32.622 1.394 1.00 15.55 ? 137 PHE A CD1 1 ATOM 1152 C CD2 . PHE A 1 137 ? 33.875 32.884 -0.119 1.00 9.61 ? 137 PHE A CD2 1 ATOM 1153 C CE1 . PHE A 1 137 ? 35.216 33.670 2.166 1.00 16.32 ? 137 PHE A CE1 1 ATOM 1154 C CE2 . PHE A 1 137 ? 33.389 33.928 0.644 1.00 13.08 ? 137 PHE A CE2 1 ATOM 1155 C CZ . PHE A 1 137 ? 34.059 34.320 1.790 1.00 14.75 ? 137 PHE A CZ 1 ATOM 1156 N N . LEU A 1 138 ? 34.478 28.149 -1.943 1.00 9.58 ? 138 LEU A N 1 ATOM 1157 C CA . LEU A 1 138 ? 34.762 27.004 -2.789 1.00 12.25 ? 138 LEU A CA 1 ATOM 1158 C C . LEU A 1 138 ? 34.838 27.447 -4.239 1.00 8.67 ? 138 LEU A C 1 ATOM 1159 O O . LEU A 1 138 ? 34.054 28.279 -4.679 1.00 9.86 ? 138 LEU A O 1 ATOM 1160 C CB . LEU A 1 138 ? 33.680 25.942 -2.596 1.00 12.78 ? 138 LEU A CB 1 ATOM 1161 C CG . LEU A 1 138 ? 33.450 25.506 -1.147 1.00 12.84 ? 138 LEU A CG 1 ATOM 1162 C CD1 . LEU A 1 138 ? 32.182 24.685 -1.053 1.00 15.10 ? 138 LEU A CD1 1 ATOM 1163 C CD2 . LEU A 1 138 ? 34.644 24.723 -0.621 1.00 14.56 ? 138 LEU A CD2 1 ATOM 1164 N N . PRO A 1 139 ? 35.790 26.894 -4.994 1.00 8.75 ? 139 PRO A N 1 ATOM 1165 C CA . PRO A 1 139 ? 35.994 27.375 -6.362 1.00 8.69 ? 139 PRO A CA 1 ATOM 1166 C C . PRO A 1 139 ? 34.953 26.851 -7.343 1.00 11.85 ? 139 PRO A C 1 ATOM 1167 O O . PRO A 1 139 ? 34.470 25.729 -7.203 1.00 13.99 ? 139 PRO A O 1 ATOM 1168 C CB . PRO A 1 139 ? 37.365 26.794 -6.723 1.00 12.16 ? 139 PRO A CB 1 ATOM 1169 C CG . PRO A 1 139 ? 37.431 25.518 -5.932 1.00 14.44 ? 139 PRO A CG 1 ATOM 1170 C CD . PRO A 1 139 ? 36.752 25.838 -4.623 1.00 11.49 ? 139 PRO A CD 1 ATOM 1171 N N . ARG A 1 140 ? 34.616 27.676 -8.328 1.00 9.33 ? 140 ARG A N 1 ATOM 1172 C CA . ARG A 1 140 ? 33.758 27.265 -9.436 1.00 9.74 ? 140 ARG A CA 1 ATOM 1173 C C . ARG A 1 140 ? 34.584 27.191 -10.711 1.00 9.32 ? 140 ARG A C 1 ATOM 1174 O O . ARG A 1 140 ? 35.628 27.848 -10.830 1.00 9.52 ? 140 ARG A O 1 ATOM 1175 C CB . ARG A 1 140 ? 32.614 28.268 -9.625 1.00 6.95 ? 140 ARG A CB 1 ATOM 1176 C CG . ARG A 1 140 ? 31.558 28.245 -8.536 1.00 7.70 ? 140 ARG A CG 1 ATOM 1177 C CD . ARG A 1 140 ? 30.589 29.422 -8.704 1.00 7.40 ? 140 ARG A CD 1 ATOM 1178 N NE . ARG A 1 140 ? 30.171 29.547 -10.103 1.00 8.96 ? 140 ARG A NE 1 ATOM 1179 C CZ . ARG A 1 140 ? 29.113 28.932 -10.618 1.00 11.80 ? 140 ARG A CZ 1 ATOM 1180 N NH1 . ARG A 1 140 ? 28.335 28.182 -9.842 1.00 12.53 ? 140 ARG A NH1 1 ATOM 1181 N NH2 . ARG A 1 140 ? 28.818 29.083 -11.903 1.00 15.90 ? 140 ARG A NH2 1 ATOM 1182 N N . GLU A 1 141 ? 34.105 26.419 -11.681 1.00 8.46 ? 141 GLU A N 1 ATOM 1183 C CA . GLU A 1 141 ? 34.828 26.270 -12.936 1.00 9.05 ? 141 GLU A CA 1 ATOM 1184 C C . GLU A 1 141 ? 34.866 27.563 -13.754 1.00 9.63 ? 141 GLU A C 1 ATOM 1185 O O . GLU A 1 141 ? 35.689 27.697 -14.659 1.00 11.15 ? 141 GLU A O 1 ATOM 1186 C CB . GLU A 1 141 ? 34.243 25.118 -13.768 1.00 13.03 ? 141 GLU A CB 1 ATOM 1187 C CG . GLU A 1 141 ? 34.389 23.764 -13.098 1.00 19.51 ? 141 GLU A CG 1 ATOM 1188 C CD . GLU A 1 141 ? 33.879 22.626 -13.964 1.00 34.83 ? 141 GLU A CD 1 ATOM 1189 O OE1 . GLU A 1 141 ? 34.185 22.614 -15.175 1.00 41.21 ? 141 GLU A OE1 1 ATOM 1190 O OE2 . GLU A 1 141 ? 33.168 21.750 -13.432 1.00 43.74 ? 141 GLU A OE2 1 ATOM 1191 N N . ASP A 1 142 ? 33.991 28.515 -13.428 1.00 9.33 ? 142 ASP A N 1 ATOM 1192 C CA . ASP A 1 142 ? 34.029 29.837 -14.065 1.00 8.50 ? 142 ASP A CA 1 ATOM 1193 C C . ASP A 1 142 ? 34.831 30.845 -13.237 1.00 7.69 ? 142 ASP A C 1 ATOM 1194 O O . ASP A 1 142 ? 34.880 32.038 -13.563 1.00 9.89 ? 142 ASP A O 1 ATOM 1195 C CB . ASP A 1 142 ? 32.619 30.367 -14.397 1.00 8.71 ? 142 ASP A CB 1 ATOM 1196 C CG . ASP A 1 142 ? 31.724 30.530 -13.168 1.00 11.43 ? 142 ASP A CG 1 ATOM 1197 O OD1 . ASP A 1 142 ? 32.211 30.393 -12.029 1.00 8.89 ? 142 ASP A OD1 1 ATOM 1198 O OD2 . ASP A 1 142 ? 30.507 30.800 -13.357 1.00 11.87 ? 142 ASP A OD2 1 ATOM 1199 N N . HIS A 1 143 ? 35.446 30.333 -12.171 1.00 6.75 ? 143 HIS A N 1 ATOM 1200 C CA . HIS A 1 143 ? 36.422 31.054 -11.354 1.00 6.27 ? 143 HIS A CA 1 ATOM 1201 C C . HIS A 1 143 ? 35.790 32.104 -10.470 1.00 6.24 ? 143 HIS A C 1 ATOM 1202 O O . HIS A 1 143 ? 36.482 32.933 -9.885 1.00 8.25 ? 143 HIS A O 1 ATOM 1203 C CB . HIS A 1 143 ? 37.572 31.574 -12.222 1.00 7.79 ? 143 HIS A CB 1 ATOM 1204 C CG . HIS A 1 143 ? 38.010 30.564 -13.228 1.00 6.40 ? 143 HIS A CG 1 ATOM 1205 N ND1 . HIS A 1 143 ? 38.476 29.323 -12.861 1.00 10.36 ? 143 HIS A ND1 1 ATOM 1206 C CD2 . HIS A 1 143 ? 37.975 30.572 -14.580 1.00 9.99 ? 143 HIS A CD2 1 ATOM 1207 C CE1 . HIS A 1 143 ? 38.737 28.616 -13.945 1.00 8.20 ? 143 HIS A CE1 1 ATOM 1208 N NE2 . HIS A 1 143 ? 38.452 29.357 -15.002 1.00 8.20 ? 143 HIS A NE2 1 ATOM 1209 N N . LEU A 1 144 ? 34.466 32.018 -10.352 1.00 6.19 ? 144 LEU A N 1 ATOM 1210 C CA . LEU A 1 144 ? 33.756 32.657 -9.261 1.00 8.25 ? 144 LEU A CA 1 ATOM 1211 C C . LEU A 1 144 ? 33.767 31.703 -8.066 1.00 6.93 ? 144 LEU A C 1 ATOM 1212 O O . LEU A 1 144 ? 34.498 30.718 -8.061 1.00 7.56 ? 144 LEU A O 1 ATOM 1213 C CB . LEU A 1 144 ? 32.325 32.978 -9.681 1.00 6.36 ? 144 LEU A CB 1 ATOM 1214 C CG . LEU A 1 144 ? 32.213 33.879 -10.915 1.00 6.87 ? 144 LEU A CG 1 ATOM 1215 C CD1 . LEU A 1 144 ? 30.757 34.008 -11.320 1.00 10.08 ? 144 LEU A CD1 1 ATOM 1216 C CD2 . LEU A 1 144 ? 32.794 35.254 -10.623 1.00 12.33 ? 144 LEU A CD2 1 ATOM 1217 N N . PHE A 1 145 ? 32.966 31.999 -7.048 1.00 7.15 ? 145 PHE A N 1 ATOM 1218 C CA . PHE A 1 145 ? 32.992 31.205 -5.825 1.00 7.22 ? 145 PHE A CA 1 ATOM 1219 C C . PHE A 1 145 ? 31.604 30.792 -5.374 1.00 7.44 ? 145 PHE A C 1 ATOM 1220 O O . PHE A 1 145 ? 30.592 31.345 -5.812 1.00 8.33 ? 145 PHE A O 1 ATOM 1221 C CB . PHE A 1 145 ? 33.655 31.990 -4.687 1.00 7.26 ? 145 PHE A CB 1 ATOM 1222 C CG . PHE A 1 145 ? 35.085 32.305 -4.947 1.00 7.83 ? 145 PHE A CG 1 ATOM 1223 C CD1 . PHE A 1 145 ? 35.442 33.472 -5.598 1.00 9.20 ? 145 PHE A CD1 1 ATOM 1224 C CD2 . PHE A 1 145 ? 36.075 31.410 -4.580 1.00 10.77 ? 145 PHE A CD2 1 ATOM 1225 C CE1 . PHE A 1 145 ? 36.771 33.758 -5.865 1.00 9.18 ? 145 PHE A CE1 1 ATOM 1226 C CE2 . PHE A 1 145 ? 37.409 31.683 -4.847 1.00 11.27 ? 145 PHE A CE2 1 ATOM 1227 C CZ . PHE A 1 145 ? 37.761 32.857 -5.481 1.00 11.52 ? 145 PHE A CZ 1 ATOM 1228 N N . ARG A 1 146 ? 31.587 29.794 -4.500 1.00 9.50 ? 146 ARG A N 1 ATOM 1229 C CA A ARG A 1 146 ? 30.360 29.403 -3.819 0.42 11.26 ? 146 ARG A CA 1 ATOM 1230 C CA B ARG A 1 146 ? 30.363 29.386 -3.825 0.40 11.40 ? 146 ARG A CA 1 ATOM 1231 C CA C ARG A 1 146 ? 30.371 29.338 -3.838 0.18 11.49 ? 146 ARG A CA 1 ATOM 1232 C C . ARG A 1 146 ? 30.670 29.063 -2.364 1.00 9.90 ? 146 ARG A C 1 ATOM 1233 O O . ARG A 1 146 ? 31.834 28.915 -1.976 1.00 10.04 ? 146 ARG A O 1 ATOM 1234 C CB A ARG A 1 146 ? 29.690 28.226 -4.527 0.42 12.79 ? 146 ARG A CB 1 ATOM 1235 C CB B ARG A 1 146 ? 29.681 28.213 -4.547 0.40 12.67 ? 146 ARG A CB 1 ATOM 1236 C CB C ARG A 1 146 ? 29.830 28.081 -4.523 0.18 13.16 ? 146 ARG A CB 1 ATOM 1237 C CG A ARG A 1 146 ? 30.499 26.961 -4.453 0.42 7.80 ? 146 ARG A CG 1 ATOM 1238 C CG B ARG A 1 146 ? 30.602 27.062 -4.929 0.40 14.72 ? 146 ARG A CG 1 ATOM 1239 C CG C ARG A 1 146 ? 30.916 27.187 -5.095 0.18 14.83 ? 146 ARG A CG 1 ATOM 1240 C CD A ARG A 1 146 ? 30.206 26.023 -5.612 0.42 16.95 ? 146 ARG A CD 1 ATOM 1241 C CD B ARG A 1 146 ? 29.919 26.094 -5.906 0.40 11.11 ? 146 ARG A CD 1 ATOM 1242 C CD C ARG A 1 146 ? 30.778 25.750 -4.622 0.18 19.21 ? 146 ARG A CD 1 ATOM 1243 N NE A ARG A 1 146 ? 31.420 25.300 -5.980 0.42 16.82 ? 146 ARG A NE 1 ATOM 1244 N NE B ARG A 1 146 ? 30.803 25.000 -6.311 0.40 15.88 ? 146 ARG A NE 1 ATOM 1245 N NE C ARG A 1 146 ? 29.668 25.050 -5.259 0.18 18.42 ? 146 ARG A NE 1 ATOM 1246 C CZ A ARG A 1 146 ? 31.882 24.239 -5.327 0.42 18.84 ? 146 ARG A CZ 1 ATOM 1247 C CZ B ARG A 1 146 ? 30.677 24.313 -7.443 0.40 21.83 ? 146 ARG A CZ 1 ATOM 1248 C CZ C ARG A 1 146 ? 29.375 23.772 -5.042 0.18 17.53 ? 146 ARG A CZ 1 ATOM 1249 N NH1 A ARG A 1 146 ? 31.221 23.760 -4.280 0.42 26.93 ? 146 ARG A NH1 1 ATOM 1250 N NH1 B ARG A 1 146 ? 31.527 23.334 -7.728 0.40 28.12 ? 146 ARG A NH1 1 ATOM 1251 N NH1 C ARG A 1 146 ? 28.348 23.209 -5.661 0.18 13.21 ? 146 ARG A NH1 1 ATOM 1252 N NH2 A ARG A 1 146 ? 33.003 23.656 -5.720 0.42 11.77 ? 146 ARG A NH2 1 ATOM 1253 N NH2 B ARG A 1 146 ? 29.705 24.607 -8.296 0.40 21.12 ? 146 ARG A NH2 1 ATOM 1254 N NH2 C ARG A 1 146 ? 30.110 23.057 -4.201 0.18 18.18 ? 146 ARG A NH2 1 ATOM 1255 N N . LYS A 1 147 ? 29.631 28.967 -1.544 1.00 7.97 ? 147 LYS A N 1 ATOM 1256 C CA . LYS A 1 147 ? 29.829 28.787 -0.117 1.00 7.64 ? 147 LYS A CA 1 ATOM 1257 C C . LYS A 1 147 ? 28.540 28.241 0.487 1.00 10.85 ? 147 LYS A C 1 ATOM 1258 O O . LYS A 1 147 ? 27.451 28.525 -0.015 1.00 9.92 ? 147 LYS A O 1 ATOM 1259 C CB . LYS A 1 147 ? 30.162 30.150 0.509 1.00 9.42 ? 147 LYS A CB 1 ATOM 1260 C CG . LYS A 1 147 ? 30.790 30.118 1.891 1.00 14.17 ? 147 LYS A CG 1 ATOM 1261 C CD . LYS A 1 147 ? 30.984 31.551 2.386 1.00 18.05 ? 147 LYS A CD 1 ATOM 1262 C CE . LYS A 1 147 ? 32.011 31.644 3.497 1.00 22.38 ? 147 LYS A CE 1 ATOM 1263 N NZ . LYS A 1 147 ? 31.576 30.913 4.718 1.00 18.31 ? 147 LYS A NZ 1 ATOM 1264 N N . PHE A 1 148 ? 28.663 27.465 1.562 1.00 9.16 ? 148 PHE A N 1 ATOM 1265 C CA . PHE A 1 148 ? 27.495 26.911 2.243 1.00 10.12 ? 148 PHE A CA 1 ATOM 1266 C C . PHE A 1 148 ? 27.482 27.304 3.710 1.00 11.45 ? 148 PHE A C 1 ATOM 1267 O O . PHE A 1 148 ? 28.515 27.271 4.387 1.00 12.48 ? 148 PHE A O 1 ATOM 1268 C CB . PHE A 1 148 ? 27.503 25.377 2.195 1.00 9.31 ? 148 PHE A CB 1 ATOM 1269 C CG . PHE A 1 148 ? 27.430 24.791 0.811 1.00 10.78 ? 148 PHE A CG 1 ATOM 1270 C CD1 . PHE A 1 148 ? 28.568 24.693 0.018 1.00 11.45 ? 148 PHE A CD1 1 ATOM 1271 C CD2 . PHE A 1 148 ? 26.232 24.285 0.326 1.00 13.58 ? 148 PHE A CD2 1 ATOM 1272 C CE1 . PHE A 1 148 ? 28.508 24.129 -1.251 1.00 11.08 ? 148 PHE A CE1 1 ATOM 1273 C CE2 . PHE A 1 148 ? 26.162 23.713 -0.938 1.00 12.04 ? 148 PHE A CE2 1 ATOM 1274 C CZ . PHE A 1 148 ? 27.297 23.638 -1.728 1.00 13.95 ? 148 PHE A CZ 1 ATOM 1275 N N . HIS A 1 149 ? 26.298 27.640 4.209 1.00 9.77 ? 149 HIS A N 1 ATOM 1276 C CA . HIS A 1 149 ? 26.093 27.872 5.629 1.00 12.00 ? 149 HIS A CA 1 ATOM 1277 C C . HIS A 1 149 ? 24.989 26.939 6.113 1.00 10.65 ? 149 HIS A C 1 ATOM 1278 O O . HIS A 1 149 ? 24.070 26.618 5.357 1.00 12.24 ? 149 HIS A O 1 ATOM 1279 C CB . HIS A 1 149 ? 25.732 29.342 5.880 1.00 11.33 ? 149 HIS A CB 1 ATOM 1280 C CG . HIS A 1 149 ? 26.922 30.250 5.876 1.00 11.77 ? 149 HIS A CG 1 ATOM 1281 N ND1 . HIS A 1 149 ? 27.334 30.939 6.997 1.00 15.45 ? 149 HIS A ND1 1 ATOM 1282 C CD2 . HIS A 1 149 ? 27.806 30.559 4.898 1.00 16.47 ? 149 HIS A CD2 1 ATOM 1283 C CE1 . HIS A 1 149 ? 28.414 31.641 6.705 1.00 18.06 ? 149 HIS A CE1 1 ATOM 1284 N NE2 . HIS A 1 149 ? 28.722 31.429 5.438 1.00 15.52 ? 149 HIS A NE2 1 ATOM 1285 N N . TYR A 1 150 ? 25.096 26.483 7.359 1.00 11.61 ? 150 TYR A N 1 ATOM 1286 C CA . TYR A 1 150 ? 24.188 25.457 7.865 1.00 12.32 ? 150 TYR A CA 1 ATOM 1287 C C . TYR A 1 150 ? 23.587 25.833 9.210 1.00 13.89 ? 150 TYR A C 1 ATOM 1288 O O . TYR A 1 150 ? 24.266 26.398 10.064 1.00 14.90 ? 150 TYR A O 1 ATOM 1289 C CB . TYR A 1 150 ? 24.941 24.135 8.035 1.00 12.99 ? 150 TYR A CB 1 ATOM 1290 C CG . TYR A 1 150 ? 25.604 23.608 6.785 1.00 12.42 ? 150 TYR A CG 1 ATOM 1291 C CD1 . TYR A 1 150 ? 26.981 23.699 6.616 1.00 12.41 ? 150 TYR A CD1 1 ATOM 1292 C CD2 . TYR A 1 150 ? 24.861 22.989 5.789 1.00 13.19 ? 150 TYR A CD2 1 ATOM 1293 C CE1 . TYR A 1 150 ? 27.598 23.206 5.480 1.00 12.72 ? 150 TYR A CE1 1 ATOM 1294 C CE2 . TYR A 1 150 ? 25.472 22.489 4.648 1.00 11.89 ? 150 TYR A CE2 1 ATOM 1295 C CZ . TYR A 1 150 ? 26.840 22.598 4.503 1.00 14.01 ? 150 TYR A CZ 1 ATOM 1296 O OH . TYR A 1 150 ? 27.450 22.104 3.371 1.00 12.81 ? 150 TYR A OH 1 ATOM 1297 N N . LEU A 1 151 ? 22.319 25.482 9.400 1.00 13.65 ? 151 LEU A N 1 ATOM 1298 C CA . LEU A 1 151 ? 21.633 25.706 10.667 1.00 14.74 ? 151 LEU A CA 1 ATOM 1299 C C . LEU A 1 151 ? 20.777 24.502 11.041 1.00 15.63 ? 151 LEU A C 1 ATOM 1300 O O . LEU A 1 151 ? 19.716 24.292 10.466 1.00 15.75 ? 151 LEU A O 1 ATOM 1301 C CB . LEU A 1 151 ? 20.754 26.961 10.583 1.00 14.58 ? 151 LEU A CB 1 ATOM 1302 C CG . LEU A 1 151 ? 19.857 27.267 11.785 1.00 19.29 ? 151 LEU A CG 1 ATOM 1303 C CD1 . LEU A 1 151 ? 20.688 27.434 13.043 1.00 22.00 ? 151 LEU A CD1 1 ATOM 1304 C CD2 . LEU A 1 151 ? 19.017 28.520 11.519 1.00 16.00 ? 151 LEU A CD2 1 ATOM 1305 N N . PRO A 1 152 ? 21.248 23.691 12.000 1.00 18.49 ? 152 PRO A N 1 ATOM 1306 C CA . PRO A 1 152 ? 20.397 22.632 12.545 1.00 19.43 ? 152 PRO A CA 1 ATOM 1307 C C . PRO A 1 152 ? 19.181 23.246 13.225 1.00 18.53 ? 152 PRO A C 1 ATOM 1308 O O . PRO A 1 152 ? 19.304 24.277 13.890 1.00 20.52 ? 152 PRO A O 1 ATOM 1309 C CB . PRO A 1 152 ? 21.301 21.962 13.586 1.00 23.35 ? 152 PRO A CB 1 ATOM 1310 C CG . PRO A 1 152 ? 22.688 22.231 13.099 1.00 28.20 ? 152 PRO A CG 1 ATOM 1311 C CD . PRO A 1 152 ? 22.627 23.615 12.508 1.00 21.80 ? 152 PRO A CD 1 ATOM 1312 N N . PHE A 1 153 ? 18.011 22.648 13.041 1.00 19.02 ? 153 PHE A N 1 ATOM 1313 C CA . PHE A 1 153 ? 16.807 23.203 13.653 1.00 19.84 ? 153 PHE A CA 1 ATOM 1314 C C . PHE A 1 153 ? 15.737 22.151 13.873 1.00 21.24 ? 153 PHE A C 1 ATOM 1315 O O . PHE A 1 153 ? 15.774 21.073 13.271 1.00 21.08 ? 153 PHE A O 1 ATOM 1316 C CB . PHE A 1 153 ? 16.245 24.356 12.810 1.00 18.93 ? 153 PHE A CB 1 ATOM 1317 C CG . PHE A 1 153 ? 15.475 23.908 11.597 1.00 18.57 ? 153 PHE A CG 1 ATOM 1318 C CD1 . PHE A 1 153 ? 14.105 24.103 11.516 1.00 19.86 ? 153 PHE A CD1 1 ATOM 1319 C CD2 . PHE A 1 153 ? 16.121 23.299 10.533 1.00 17.99 ? 153 PHE A CD2 1 ATOM 1320 C CE1 . PHE A 1 153 ? 13.395 23.698 10.397 1.00 19.81 ? 153 PHE A CE1 1 ATOM 1321 C CE2 . PHE A 1 153 ? 15.418 22.893 9.417 1.00 17.61 ? 153 PHE A CE2 1 ATOM 1322 C CZ . PHE A 1 153 ? 14.050 23.091 9.347 1.00 20.68 ? 153 PHE A CZ 1 ATOM 1323 N N . LEU A 1 154 ? 14.795 22.483 14.753 1.00 23.91 ? 154 LEU A N 1 ATOM 1324 C CA . LEU A 1 154 ? 13.643 21.640 15.038 1.00 25.81 ? 154 LEU A CA 1 ATOM 1325 C C . LEU A 1 154 ? 12.402 22.295 14.440 1.00 27.14 ? 154 LEU A C 1 ATOM 1326 O O . LEU A 1 154 ? 11.923 23.305 14.950 1.00 25.55 ? 154 LEU A O 1 ATOM 1327 C CB . LEU A 1 154 ? 13.477 21.470 16.548 1.00 27.47 ? 154 LEU A CB 1 ATOM 1328 C CG . LEU A 1 154 ? 12.570 20.337 17.025 1.00 37.68 ? 154 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 154 ? 13.197 18.990 16.704 1.00 31.96 ? 154 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 154 ? 12.290 20.462 18.518 1.00 44.86 ? 154 LEU A CD2 1 ATOM 1331 N N . PRO A 1 155 ? 11.882 21.723 13.346 1.00 24.83 ? 155 PRO A N 1 ATOM 1332 C CA . PRO A 1 155 ? 10.791 22.338 12.587 1.00 23.66 ? 155 PRO A CA 1 ATOM 1333 C C . PRO A 1 155 ? 9.540 22.534 13.427 1.00 25.42 ? 155 PRO A C 1 ATOM 1334 O O . PRO A 1 155 ? 9.153 21.651 14.196 1.00 26.77 ? 155 PRO A O 1 ATOM 1335 C CB . PRO A 1 155 ? 10.523 21.320 11.476 1.00 27.73 ? 155 PRO A CB 1 ATOM 1336 C CG . PRO A 1 155 ? 11.819 20.595 11.312 1.00 28.91 ? 155 PRO A CG 1 ATOM 1337 C CD . PRO A 1 155 ? 12.362 20.486 12.710 1.00 32.31 ? 155 PRO A CD 1 ATOM 1338 N N . SER A 1 156 ? 8.922 23.700 13.280 1.00 25.57 ? 156 SER A N 1 ATOM 1339 C CA . SER A 1 156 ? 7.705 24.022 14.005 1.00 27.39 ? 156 SER A CA 1 ATOM 1340 C C . SER A 1 156 ? 6.871 24.999 13.192 1.00 29.97 ? 156 SER A C 1 ATOM 1341 O O . SER A 1 156 ? 7.387 25.685 12.313 1.00 34.22 ? 156 SER A O 1 ATOM 1342 C CB . SER A 1 156 ? 8.038 24.628 15.368 1.00 47.80 ? 156 SER A CB 1 ATOM 1343 O OG . SER A 1 156 ? 8.676 25.882 15.223 1.00 50.73 ? 156 SER A OG 1 ATOM 1344 N N . THR A 1 157 ? 5.578 25.056 13.489 1.00 31.15 ? 157 THR A N 1 ATOM 1345 C CA . THR A 1 157 ? 4.684 25.977 12.806 1.00 40.94 ? 157 THR A CA 1 ATOM 1346 C C . THR A 1 157 ? 4.909 27.404 13.297 1.00 40.51 ? 157 THR A C 1 ATOM 1347 O O . THR A 1 157 ? 4.439 28.364 12.686 1.00 41.99 ? 157 THR A O 1 ATOM 1348 C CB . THR A 1 157 ? 3.212 25.583 13.026 1.00 43.07 ? 157 THR A CB 1 ATOM 1349 O OG1 . THR A 1 157 ? 2.942 25.493 14.432 1.00 43.90 ? 157 THR A OG1 1 ATOM 1350 C CG2 . THR A 1 157 ? 2.924 24.235 12.387 1.00 38.45 ? 157 THR A CG2 1 ATOM 1351 N N . GLU A 1 158 ? 5.645 27.534 14.396 1.00 29.97 ? 158 GLU A N 1 ATOM 1352 C CA . GLU A 1 158 ? 5.802 28.818 15.070 1.00 37.92 ? 158 GLU A CA 1 ATOM 1353 C C . GLU A 1 158 ? 7.020 29.628 14.621 1.00 33.62 ? 158 GLU A C 1 ATOM 1354 O O . GLU A 1 158 ? 7.099 30.824 14.897 1.00 39.17 ? 158 GLU A O 1 ATOM 1355 C CB . GLU A 1 158 ? 5.843 28.618 16.586 1.00 40.36 ? 158 GLU A CB 1 ATOM 1356 C CG . GLU A 1 158 ? 4.573 28.008 17.151 1.00 50.47 ? 158 GLU A CG 1 ATOM 1357 C CD . GLU A 1 158 ? 3.324 28.723 16.666 1.00 64.08 ? 158 GLU A CD 1 ATOM 1358 O OE1 . GLU A 1 158 ? 2.605 28.156 15.814 1.00 67.68 ? 158 GLU A OE1 1 ATOM 1359 O OE2 . GLU A 1 158 ? 3.059 29.852 17.133 1.00 70.98 ? 158 GLU A OE2 1 ATOM 1360 N N . ASP A 1 159 ? 7.962 28.987 13.932 1.00 27.08 ? 159 ASP A N 1 ATOM 1361 C CA . ASP A 1 159 ? 9.203 29.657 13.551 1.00 32.36 ? 159 ASP A CA 1 ATOM 1362 C C . ASP A 1 159 ? 9.337 29.864 12.050 1.00 36.43 ? 159 ASP A C 1 ATOM 1363 O O . ASP A 1 159 ? 9.029 28.972 11.263 1.00 40.98 ? 159 ASP A O 1 ATOM 1364 C CB . ASP A 1 159 ? 10.419 28.867 14.044 1.00 30.20 ? 159 ASP A CB 1 ATOM 1365 C CG . ASP A 1 159 ? 10.479 28.766 15.554 1.00 41.18 ? 159 ASP A CG 1 ATOM 1366 O OD1 . ASP A 1 159 ? 10.031 29.714 16.235 1.00 36.70 ? 159 ASP A OD1 1 ATOM 1367 O OD2 . ASP A 1 159 ? 10.982 27.737 16.059 1.00 40.72 ? 159 ASP A OD2 1 ATOM 1368 N N . VAL A 1 160 ? 9.811 31.044 11.660 1.00 27.29 ? 160 VAL A N 1 ATOM 1369 C CA . VAL A 1 160 ? 10.217 31.281 10.277 1.00 22.11 ? 160 VAL A CA 1 ATOM 1370 C C . VAL A 1 160 ? 11.705 31.587 10.254 1.00 21.17 ? 160 VAL A C 1 ATOM 1371 O O . VAL A 1 160 ? 12.262 32.050 11.248 1.00 20.78 ? 160 VAL A O 1 ATOM 1372 C CB . VAL A 1 160 ? 9.435 32.440 9.624 1.00 23.08 ? 160 VAL A CB 1 ATOM 1373 C CG1 . VAL A 1 160 ? 7.938 32.187 9.706 1.00 30.91 ? 160 VAL A CG1 1 ATOM 1374 C CG2 . VAL A 1 160 ? 9.796 33.775 10.265 1.00 25.68 ? 160 VAL A CG2 1 ATOM 1375 N N . TYR A 1 161 ? 12.351 31.305 9.127 1.00 19.13 ? 161 TYR A N 1 ATOM 1376 C CA . TYR A 1 161 ? 13.784 31.533 8.997 1.00 17.73 ? 161 TYR A CA 1 ATOM 1377 C C . TYR A 1 161 ? 14.133 32.345 7.763 1.00 19.07 ? 161 TYR A C 1 ATOM 1378 O O . TYR A 1 161 ? 13.399 32.356 6.776 1.00 18.63 ? 161 TYR A O 1 ATOM 1379 C CB . TYR A 1 161 ? 14.543 30.200 8.941 1.00 16.77 ? 161 TYR A CB 1 ATOM 1380 C CG . TYR A 1 161 ? 14.448 29.416 10.222 1.00 17.56 ? 161 TYR A CG 1 ATOM 1381 C CD1 . TYR A 1 161 ? 13.377 28.563 10.458 1.00 18.57 ? 161 TYR A CD1 1 ATOM 1382 C CD2 . TYR A 1 161 ? 15.422 29.535 11.203 1.00 17.54 ? 161 TYR A CD2 1 ATOM 1383 C CE1 . TYR A 1 161 ? 13.284 27.845 11.629 1.00 24.54 ? 161 TYR A CE1 1 ATOM 1384 C CE2 . TYR A 1 161 ? 15.333 28.825 12.383 1.00 18.81 ? 161 TYR A CE2 1 ATOM 1385 C CZ . TYR A 1 161 ? 14.265 27.975 12.586 1.00 19.42 ? 161 TYR A CZ 1 ATOM 1386 O OH . TYR A 1 161 ? 14.166 27.262 13.757 1.00 24.63 ? 161 TYR A OH 1 ATOM 1387 N N . ASP A 1 162 ? 15.264 33.035 7.838 1.00 16.24 ? 162 ASP A N 1 ATOM 1388 C CA . ASP A 1 162 ? 15.831 33.699 6.680 1.00 15.42 ? 162 ASP A CA 1 ATOM 1389 C C . ASP A 1 162 ? 17.332 33.537 6.713 1.00 16.16 ? 162 ASP A C 1 ATOM 1390 O O . ASP A 1 162 ? 17.942 33.529 7.785 1.00 14.48 ? 162 ASP A O 1 ATOM 1391 C CB . ASP A 1 162 ? 15.516 35.199 6.682 1.00 16.37 ? 162 ASP A CB 1 ATOM 1392 C CG . ASP A 1 162 ? 14.031 35.494 6.557 1.00 18.49 ? 162 ASP A CG 1 ATOM 1393 O OD1 . ASP A 1 162 ? 13.517 35.498 5.419 1.00 21.46 ? 162 ASP A OD1 1 ATOM 1394 O OD2 . ASP A 1 162 ? 13.386 35.750 7.596 1.00 21.22 ? 162 ASP A OD2 1 ATOM 1395 N N . CYS A 1 163 ? 17.926 33.405 5.532 1.00 13.69 ? 163 CYS A N 1 ATOM 1396 C CA . CYS A 1 163 ? 19.364 33.544 5.386 1.00 12.45 ? 163 CYS A CA 1 ATOM 1397 C C . CYS A 1 163 ? 19.615 34.925 4.811 1.00 14.95 ? 163 CYS A C 1 ATOM 1398 O O . CYS A 1 163 ? 19.102 35.254 3.739 1.00 15.12 ? 163 CYS A O 1 ATOM 1399 C CB . CYS A 1 163 ? 19.911 32.480 4.438 1.00 14.04 ? 163 CYS A CB 1 ATOM 1400 S SG . CYS A 1 163 ? 21.695 32.579 4.211 1.00 17.93 ? 163 CYS A SG 1 ATOM 1401 N N . ARG A 1 164 ? 20.382 35.741 5.526 1.00 12.68 ? 164 ARG A N 1 ATOM 1402 C CA . ARG A 1 164 ? 20.661 37.102 5.072 1.00 13.05 ? 164 ARG A CA 1 ATOM 1403 C C . ARG A 1 164 ? 22.092 37.204 4.586 1.00 13.69 ? 164 ARG A C 1 ATOM 1404 O O . ARG A 1 164 ? 23.021 36.916 5.331 1.00 15.83 ? 164 ARG A O 1 ATOM 1405 C CB . ARG A 1 164 ? 20.442 38.108 6.196 1.00 14.47 ? 164 ARG A CB 1 ATOM 1406 C CG . ARG A 1 164 ? 20.701 39.539 5.752 1.00 15.16 ? 164 ARG A CG 1 ATOM 1407 C CD . ARG A 1 164 ? 20.441 40.516 6.880 1.00 23.56 ? 164 ARG A CD 1 ATOM 1408 N NE . ARG A 1 164 ? 21.446 40.375 7.926 1.00 19.63 ? 164 ARG A NE 1 ATOM 1409 C CZ . ARG A 1 164 ? 21.230 40.634 9.209 1.00 18.50 ? 164 ARG A CZ 1 ATOM 1410 N NH1 . ARG A 1 164 ? 20.031 41.039 9.611 1.00 19.78 ? 164 ARG A NH1 1 ATOM 1411 N NH2 . ARG A 1 164 ? 22.210 40.483 10.088 1.00 22.92 ? 164 ARG A NH2 1 ATOM 1412 N N . VAL A 1 165 ? 22.262 37.626 3.339 1.00 11.76 ? 165 VAL A N 1 ATOM 1413 C CA . VAL A 1 165 ? 23.579 37.653 2.719 1.00 11.33 ? 165 VAL A CA 1 ATOM 1414 C C . VAL A 1 165 ? 23.958 39.082 2.314 1.00 14.29 ? 165 VAL A C 1 ATOM 1415 O O . VAL A 1 165 ? 23.197 39.754 1.615 1.00 14.69 ? 165 VAL A O 1 ATOM 1416 C CB . VAL A 1 165 ? 23.597 36.720 1.486 1.00 9.99 ? 165 VAL A CB 1 ATOM 1417 C CG1 . VAL A 1 165 ? 24.905 36.852 0.720 1.00 12.02 ? 165 VAL A CG1 1 ATOM 1418 C CG2 . VAL A 1 165 ? 23.377 35.270 1.917 1.00 11.44 ? 165 VAL A CG2 1 ATOM 1419 N N A GLU A 1 166 ? 25.120 39.542 2.775 0.44 11.83 ? 166 GLU A N 1 ATOM 1420 N N B GLU A 1 166 ? 25.125 39.535 2.768 0.56 11.82 ? 166 GLU A N 1 ATOM 1421 C CA A GLU A 1 166 ? 25.662 40.839 2.376 0.44 14.71 ? 166 GLU A CA 1 ATOM 1422 C CA B GLU A 1 166 ? 25.666 40.835 2.387 0.56 12.54 ? 166 GLU A CA 1 ATOM 1423 C C A GLU A 1 166 ? 26.894 40.648 1.501 0.44 13.05 ? 166 GLU A C 1 ATOM 1424 C C B GLU A 1 166 ? 26.877 40.620 1.484 0.56 12.43 ? 166 GLU A C 1 ATOM 1425 O O A GLU A 1 166 ? 27.787 39.880 1.843 0.44 14.36 ? 166 GLU A O 1 ATOM 1426 O O B GLU A 1 166 ? 27.733 39.794 1.783 0.56 14.10 ? 166 GLU A O 1 ATOM 1427 C CB A GLU A 1 166 ? 26.046 41.670 3.600 0.44 17.92 ? 166 GLU A CB 1 ATOM 1428 C CB B GLU A 1 166 ? 26.086 41.619 3.632 0.56 17.03 ? 166 GLU A CB 1 ATOM 1429 C CG A GLU A 1 166 ? 24.886 42.336 4.314 0.44 20.89 ? 166 GLU A CG 1 ATOM 1430 C CG B GLU A 1 166 ? 25.036 41.643 4.737 0.56 21.34 ? 166 GLU A CG 1 ATOM 1431 C CD A GLU A 1 166 ? 25.359 43.264 5.420 0.44 27.94 ? 166 GLU A CD 1 ATOM 1432 C CD B GLU A 1 166 ? 25.615 42.054 6.084 0.56 26.77 ? 166 GLU A CD 1 ATOM 1433 O OE1 A GLU A 1 166 ? 24.512 43.947 6.028 0.44 38.93 ? 166 GLU A OE1 1 ATOM 1434 O OE1 B GLU A 1 166 ? 25.129 41.549 7.119 0.56 25.12 ? 166 GLU A OE1 1 ATOM 1435 O OE2 A GLU A 1 166 ? 26.584 43.312 5.677 0.44 31.22 ? 166 GLU A OE2 1 ATOM 1436 O OE2 B GLU A 1 166 ? 26.558 42.877 6.107 0.56 31.23 ? 166 GLU A OE2 1 ATOM 1437 N N . HIS A 1 167 ? 26.945 41.365 0.383 1.00 11.97 ? 167 HIS A N 1 ATOM 1438 C CA . HIS A 1 167 ? 28.072 41.270 -0.544 1.00 11.26 ? 167 HIS A CA 1 ATOM 1439 C C . HIS A 1 167 ? 28.206 42.607 -1.247 1.00 12.61 ? 167 HIS A C 1 ATOM 1440 O O . HIS A 1 167 ? 27.201 43.273 -1.494 1.00 14.86 ? 167 HIS A O 1 ATOM 1441 C CB . HIS A 1 167 ? 27.835 40.150 -1.567 1.00 10.11 ? 167 HIS A CB 1 ATOM 1442 C CG . HIS A 1 167 ? 28.996 39.900 -2.476 1.00 9.60 ? 167 HIS A CG 1 ATOM 1443 N ND1 . HIS A 1 167 ? 29.176 40.572 -3.664 1.00 9.86 ? 167 HIS A ND1 1 ATOM 1444 C CD2 . HIS A 1 167 ? 30.040 39.037 -2.373 1.00 11.24 ? 167 HIS A CD2 1 ATOM 1445 C CE1 . HIS A 1 167 ? 30.286 40.151 -4.247 1.00 11.84 ? 167 HIS A CE1 1 ATOM 1446 N NE2 . HIS A 1 167 ? 30.825 39.214 -3.484 1.00 11.96 ? 167 HIS A NE2 1 ATOM 1447 N N . TRP A 1 168 ? 29.433 43.012 -1.572 1.00 12.35 ? 168 TRP A N 1 ATOM 1448 C CA . TRP A 1 168 ? 29.645 44.329 -2.170 1.00 14.41 ? 168 TRP A CA 1 ATOM 1449 C C . TRP A 1 168 ? 28.940 44.528 -3.513 1.00 14.82 ? 168 TRP A C 1 ATOM 1450 O O . TRP A 1 168 ? 28.703 45.666 -3.922 1.00 16.74 ? 168 TRP A O 1 ATOM 1451 C CB . TRP A 1 168 ? 31.142 44.639 -2.291 1.00 17.95 ? 168 TRP A CB 1 ATOM 1452 C CG . TRP A 1 168 ? 31.814 44.694 -0.961 1.00 15.69 ? 168 TRP A CG 1 ATOM 1453 C CD1 . TRP A 1 168 ? 31.341 45.297 0.174 1.00 18.68 ? 168 TRP A CD1 1 ATOM 1454 C CD2 . TRP A 1 168 ? 33.069 44.103 -0.609 1.00 15.05 ? 168 TRP A CD2 1 ATOM 1455 N NE1 . TRP A 1 168 ? 32.232 45.124 1.206 1.00 21.98 ? 168 TRP A NE1 1 ATOM 1456 C CE2 . TRP A 1 168 ? 33.301 44.393 0.750 1.00 19.46 ? 168 TRP A CE2 1 ATOM 1457 C CE3 . TRP A 1 168 ? 34.023 43.358 -1.314 1.00 17.77 ? 168 TRP A CE3 1 ATOM 1458 C CZ2 . TRP A 1 168 ? 34.444 43.962 1.422 1.00 17.73 ? 168 TRP A CZ2 1 ATOM 1459 C CZ3 . TRP A 1 168 ? 35.159 42.933 -0.645 1.00 16.18 ? 168 TRP A CZ3 1 ATOM 1460 C CH2 . TRP A 1 168 ? 35.357 43.235 0.709 1.00 16.40 ? 168 TRP A CH2 1 ATOM 1461 N N . GLY A 1 169 ? 28.592 43.430 -4.179 1.00 12.30 ? 169 GLY A N 1 ATOM 1462 C CA . GLY A 1 169 ? 27.875 43.497 -5.436 1.00 14.03 ? 169 GLY A CA 1 ATOM 1463 C C . GLY A 1 169 ? 26.380 43.706 -5.262 1.00 17.14 ? 169 GLY A C 1 ATOM 1464 O O . GLY A 1 169 ? 25.665 43.917 -6.242 1.00 15.91 ? 169 GLY A O 1 ATOM 1465 N N . LEU A 1 170 ? 25.907 43.640 -4.020 1.00 13.47 ? 170 LEU A N 1 ATOM 1466 C CA . LEU A 1 170 ? 24.485 43.851 -3.725 1.00 14.22 ? 170 LEU A CA 1 ATOM 1467 C C . LEU A 1 170 ? 24.230 45.262 -3.219 1.00 21.62 ? 170 LEU A C 1 ATOM 1468 O O . LEU A 1 170 ? 25.001 45.787 -2.421 1.00 29.12 ? 170 LEU A O 1 ATOM 1469 C CB . LEU A 1 170 ? 24.001 42.865 -2.664 1.00 13.53 ? 170 LEU A CB 1 ATOM 1470 C CG . LEU A 1 170 ? 24.013 41.381 -3.050 1.00 18.29 ? 170 LEU A CG 1 ATOM 1471 C CD1 . LEU A 1 170 ? 23.814 40.495 -1.824 1.00 17.74 ? 170 LEU A CD1 1 ATOM 1472 C CD2 . LEU A 1 170 ? 22.948 41.106 -4.103 1.00 17.37 ? 170 LEU A CD2 1 ATOM 1473 N N . ASP A 1 171 ? 23.138 45.867 -3.676 1.00 19.28 ? 171 ASP A N 1 ATOM 1474 C CA . ASP A 1 171 ? 22.758 47.195 -3.209 1.00 23.58 ? 171 ASP A CA 1 ATOM 1475 C C . ASP A 1 171 ? 22.184 47.133 -1.799 1.00 33.34 ? 171 ASP A C 1 ATOM 1476 O O . ASP A 1 171 ? 22.328 48.068 -1.010 1.00 32.08 ? 171 ASP A O 1 ATOM 1477 C CB . ASP A 1 171 ? 21.756 47.833 -4.170 1.00 30.35 ? 171 ASP A CB 1 ATOM 1478 C CG . ASP A 1 171 ? 22.399 48.270 -5.473 1.00 52.31 ? 171 ASP A CG 1 ATOM 1479 O OD1 . ASP A 1 171 ? 23.596 48.628 -5.453 1.00 50.93 ? 171 ASP A OD1 1 ATOM 1480 O OD2 . ASP A 1 171 ? 21.709 48.257 -6.514 1.00 62.77 ? 171 ASP A OD2 1 ATOM 1481 N N . GLU A 1 172 ? 21.514 46.029 -1.501 1.00 21.52 ? 172 GLU A N 1 ATOM 1482 C CA A GLU A 1 172 ? 20.963 45.784 -0.174 0.51 21.78 ? 172 GLU A CA 1 ATOM 1483 C CA B GLU A 1 172 ? 20.962 45.787 -0.177 0.49 21.81 ? 172 GLU A CA 1 ATOM 1484 C C . GLU A 1 172 ? 21.178 44.318 0.169 1.00 19.17 ? 172 GLU A C 1 ATOM 1485 O O . GLU A 1 172 ? 21.416 43.507 -0.720 1.00 18.71 ? 172 GLU A O 1 ATOM 1486 C CB A GLU A 1 172 ? 19.468 46.118 -0.133 0.51 24.82 ? 172 GLU A CB 1 ATOM 1487 C CB B GLU A 1 172 ? 19.470 46.132 -0.157 0.49 24.95 ? 172 GLU A CB 1 ATOM 1488 C CG A GLU A 1 172 ? 19.159 47.590 -0.306 0.51 29.56 ? 172 GLU A CG 1 ATOM 1489 C CG B GLU A 1 172 ? 18.661 45.435 -1.238 0.49 26.14 ? 172 GLU A CG 1 ATOM 1490 C CD A GLU A 1 172 ? 18.139 48.104 0.694 0.51 36.99 ? 172 GLU A CD 1 ATOM 1491 C CD B GLU A 1 172 ? 17.197 45.821 -1.215 0.49 33.95 ? 172 GLU A CD 1 ATOM 1492 O OE1 A GLU A 1 172 ? 17.452 47.279 1.332 0.51 53.39 ? 172 GLU A OE1 1 ATOM 1493 O OE1 B GLU A 1 172 ? 16.894 46.989 -0.897 0.49 32.33 ? 172 GLU A OE1 1 ATOM 1494 O OE2 A GLU A 1 172 ? 18.028 49.338 0.847 0.51 39.00 ? 172 GLU A OE2 1 ATOM 1495 O OE2 B GLU A 1 172 ? 16.349 44.953 -1.511 0.49 38.27 ? 172 GLU A OE2 1 ATOM 1496 N N . PRO A 1 173 ? 21.112 43.968 1.466 1.00 22.62 ? 173 PRO A N 1 ATOM 1497 C CA . PRO A 1 173 ? 21.273 42.545 1.776 1.00 22.00 ? 173 PRO A CA 1 ATOM 1498 C C . PRO A 1 173 ? 20.165 41.696 1.168 1.00 17.03 ? 173 PRO A C 1 ATOM 1499 O O . PRO A 1 173 ? 19.015 42.140 1.030 1.00 21.01 ? 173 PRO A O 1 ATOM 1500 C CB . PRO A 1 173 ? 21.194 42.499 3.307 1.00 25.47 ? 173 PRO A CB 1 ATOM 1501 C CG . PRO A 1 173 ? 20.585 43.790 3.710 1.00 33.84 ? 173 PRO A CG 1 ATOM 1502 C CD . PRO A 1 173 ? 21.013 44.785 2.687 1.00 33.10 ? 173 PRO A CD 1 ATOM 1503 N N . LEU A 1 174 ? 20.528 40.479 0.794 1.00 16.01 ? 174 LEU A N 1 ATOM 1504 C CA . LEU A 1 174 ? 19.591 39.554 0.193 1.00 13.79 ? 174 LEU A CA 1 ATOM 1505 C C . LEU A 1 174 ? 19.067 38.612 1.265 1.00 16.09 ? 174 LEU A C 1 ATOM 1506 O O . LEU A 1 174 ? 19.845 37.957 1.954 1.00 19.83 ? 174 LEU A O 1 ATOM 1507 C CB . LEU A 1 174 ? 20.297 38.767 -0.909 1.00 16.84 ? 174 LEU A CB 1 ATOM 1508 C CG . LEU A 1 174 ? 19.460 37.920 -1.860 1.00 25.41 ? 174 LEU A CG 1 ATOM 1509 C CD1 . LEU A 1 174 ? 18.281 38.710 -2.383 1.00 29.32 ? 174 LEU A CD1 1 ATOM 1510 C CD2 . LEU A 1 174 ? 20.338 37.434 -3.012 1.00 30.54 ? 174 LEU A CD2 1 ATOM 1511 N N . LEU A 1 175 ? 17.748 38.562 1.417 1.00 15.73 ? 175 LEU A N 1 ATOM 1512 C CA . LEU A 1 175 ? 17.121 37.637 2.356 1.00 15.59 ? 175 LEU A CA 1 ATOM 1513 C C . LEU A 1 175 ? 16.353 36.563 1.611 1.00 17.43 ? 175 LEU A C 1 ATOM 1514 O O . LEU A 1 175 ? 15.489 36.862 0.783 1.00 23.94 ? 175 LEU A O 1 ATOM 1515 C CB . LEU A 1 175 ? 16.162 38.366 3.302 1.00 22.11 ? 175 LEU A CB 1 ATOM 1516 C CG . LEU A 1 175 ? 16.757 38.929 4.589 1.00 26.52 ? 175 LEU A CG 1 ATOM 1517 C CD1 . LEU A 1 175 ? 17.554 40.186 4.270 1.00 27.38 ? 175 LEU A CD1 1 ATOM 1518 C CD2 . LEU A 1 175 ? 15.665 39.212 5.611 1.00 33.36 ? 175 LEU A CD2 1 ATOM 1519 N N . LYS A 1 176 ? 16.671 35.311 1.914 1.00 14.62 ? 176 LYS A N 1 ATOM 1520 C CA . LYS A 1 176 ? 15.934 34.182 1.370 1.00 14.04 ? 176 LYS A CA 1 ATOM 1521 C C . LYS A 1 176 ? 15.232 33.474 2.512 1.00 16.99 ? 176 LYS A C 1 ATOM 1522 O O . LYS A 1 176 ? 15.852 33.126 3.515 1.00 15.80 ? 176 LYS A O 1 ATOM 1523 C CB . LYS A 1 176 ? 16.874 33.232 0.628 1.00 15.95 ? 176 LYS A CB 1 ATOM 1524 C CG . LYS A 1 176 ? 17.461 33.847 -0.624 1.00 20.58 ? 176 LYS A CG 1 ATOM 1525 C CD . LYS A 1 176 ? 16.389 34.145 -1.658 1.00 21.43 ? 176 LYS A CD 1 ATOM 1526 C CE . LYS A 1 176 ? 16.960 34.960 -2.807 1.00 30.26 ? 176 LYS A CE 1 ATOM 1527 N NZ . LYS A 1 176 ? 15.987 35.111 -3.924 1.00 40.35 ? 176 LYS A NZ 1 ATOM 1528 N N . HIS A 1 177 ? 13.931 33.264 2.336 1.00 16.35 ? 177 HIS A N 1 ATOM 1529 C CA . HIS A 1 177 ? 13.037 32.837 3.399 1.00 17.15 ? 177 HIS A CA 1 ATOM 1530 C C . HIS A 1 177 ? 12.801 31.326 3.410 1.00 20.51 ? 177 HIS A C 1 ATOM 1531 O O . HIS A 1 177 ? 12.849 30.667 2.367 1.00 23.10 ? 177 HIS A O 1 ATOM 1532 C CB . HIS A 1 177 ? 11.702 33.562 3.202 1.00 18.71 ? 177 HIS A CB 1 ATOM 1533 C CG . HIS A 1 177 ? 10.766 33.462 4.366 1.00 23.83 ? 177 HIS A CG 1 ATOM 1534 N ND1 . HIS A 1 177 ? 10.920 34.216 5.509 1.00 24.67 ? 177 HIS A ND1 1 ATOM 1535 C CD2 . HIS A 1 177 ? 9.645 32.723 4.551 1.00 26.80 ? 177 HIS A CD2 1 ATOM 1536 C CE1 . HIS A 1 177 ? 9.943 33.936 6.354 1.00 28.65 ? 177 HIS A CE1 1 ATOM 1537 N NE2 . HIS A 1 177 ? 9.157 33.031 5.797 1.00 29.19 ? 177 HIS A NE2 1 ATOM 1538 N N . TRP A 1 178 ? 12.566 30.779 4.600 1.00 18.87 ? 178 TRP A N 1 ATOM 1539 C CA . TRP A 1 178 ? 12.017 29.435 4.728 1.00 18.20 ? 178 TRP A CA 1 ATOM 1540 C C . TRP A 1 178 ? 10.996 29.391 5.853 1.00 19.08 ? 178 TRP A C 1 ATOM 1541 O O . TRP A 1 178 ? 11.218 29.947 6.928 1.00 22.77 ? 178 TRP A O 1 ATOM 1542 C CB . TRP A 1 178 ? 13.107 28.384 4.987 1.00 20.29 ? 178 TRP A CB 1 ATOM 1543 C CG . TRP A 1 178 ? 12.524 26.990 5.112 1.00 20.77 ? 178 TRP A CG 1 ATOM 1544 C CD1 . TRP A 1 178 ? 12.382 26.066 4.110 1.00 26.24 ? 178 TRP A CD1 1 ATOM 1545 C CD2 . TRP A 1 178 ? 11.969 26.386 6.290 1.00 20.98 ? 178 TRP A CD2 1 ATOM 1546 N NE1 . TRP A 1 178 ? 11.786 24.931 4.594 1.00 26.45 ? 178 TRP A NE1 1 ATOM 1547 C CE2 . TRP A 1 178 ? 11.522 25.097 5.928 1.00 23.46 ? 178 TRP A CE2 1 ATOM 1548 C CE3 . TRP A 1 178 ? 11.814 26.804 7.616 1.00 24.23 ? 178 TRP A CE3 1 ATOM 1549 C CZ2 . TRP A 1 178 ? 10.932 24.227 6.843 1.00 23.39 ? 178 TRP A CZ2 1 ATOM 1550 C CZ3 . TRP A 1 178 ? 11.221 25.939 8.521 1.00 31.46 ? 178 TRP A CZ3 1 ATOM 1551 C CH2 . TRP A 1 178 ? 10.791 24.665 8.131 1.00 31.75 ? 178 TRP A CH2 1 ATOM 1552 N N . GLU A 1 179 ? 9.867 28.738 5.600 1.00 20.41 ? 179 GLU A N 1 ATOM 1553 C CA . GLU A 1 179 ? 8.938 28.418 6.671 1.00 21.85 ? 179 GLU A CA 1 ATOM 1554 C C . GLU A 1 179 ? 8.209 27.113 6.380 1.00 25.70 ? 179 GLU A C 1 ATOM 1555 O O . GLU A 1 179 ? 8.145 26.669 5.232 1.00 26.52 ? 179 GLU A O 1 ATOM 1556 C CB . GLU A 1 179 ? 7.954 29.562 6.924 1.00 25.86 ? 179 GLU A CB 1 ATOM 1557 C CG . GLU A 1 179 ? 6.956 29.804 5.815 1.00 30.45 ? 179 GLU A CG 1 ATOM 1558 C CD . GLU A 1 179 ? 6.070 31.002 6.097 1.00 36.07 ? 179 GLU A CD 1 ATOM 1559 O OE1 . GLU A 1 179 ? 6.610 32.121 6.231 1.00 32.90 ? 179 GLU A OE1 1 ATOM 1560 O OE2 . GLU A 1 179 ? 4.839 30.823 6.194 1.00 39.36 ? 179 GLU A OE2 1 ATOM 1561 N N . PHE A 1 180 ? 7.680 26.500 7.433 1.00 25.42 ? 180 PHE A N 1 ATOM 1562 C CA . PHE A 1 180 ? 7.015 25.209 7.327 1.00 29.41 ? 180 PHE A CA 1 ATOM 1563 C C . PHE A 1 180 ? 5.815 25.290 6.387 1.00 40.16 ? 180 PHE A C 1 ATOM 1564 O O . PHE A 1 180 ? 4.947 26.150 6.546 1.00 38.34 ? 180 PHE A O 1 ATOM 1565 C CB . PHE A 1 180 ? 6.591 24.721 8.713 1.00 26.07 ? 180 PHE A CB 1 ATOM 1566 C CG . PHE A 1 180 ? 6.008 23.340 8.715 1.00 31.11 ? 180 PHE A CG 1 ATOM 1567 C CD1 . PHE A 1 180 ? 4.642 23.151 8.817 1.00 41.29 ? 180 PHE A CD1 1 ATOM 1568 C CD2 . PHE A 1 180 ? 6.830 22.230 8.603 1.00 30.05 ? 180 PHE A CD2 1 ATOM 1569 C CE1 . PHE A 1 180 ? 4.104 21.876 8.816 1.00 45.98 ? 180 PHE A CE1 1 ATOM 1570 C CE2 . PHE A 1 180 ? 6.300 20.956 8.601 1.00 32.10 ? 180 PHE A CE2 1 ATOM 1571 C CZ . PHE A 1 180 ? 4.938 20.778 8.705 1.00 42.24 ? 180 PHE A CZ 1 ATOM 1572 N N . ASP A 1 181 ? 5.782 24.395 5.405 1.00 42.45 ? 181 ASP A N 1 ATOM 1573 C CA . ASP A 1 181 ? 4.759 24.424 4.363 1.00 57.40 ? 181 ASP A CA 1 ATOM 1574 C C . ASP A 1 181 ? 3.448 23.784 4.818 1.00 71.67 ? 181 ASP A C 1 ATOM 1575 O O . ASP A 1 181 ? 3.450 22.771 5.522 1.00 66.67 ? 181 ASP A O 1 ATOM 1576 C CB . ASP A 1 181 ? 5.275 23.743 3.092 1.00 57.21 ? 181 ASP A CB 1 ATOM 1577 C CG . ASP A 1 181 ? 4.242 23.723 1.978 1.00 70.26 ? 181 ASP A CG 1 ATOM 1578 O OD1 . ASP A 1 181 ? 3.364 24.613 1.954 1.00 73.08 ? 181 ASP A OD1 1 ATOM 1579 O OD2 . ASP A 1 181 ? 4.311 22.817 1.121 1.00 75.15 ? 181 ASP A OD2 1 ATOM 1580 N N . THR A 1 182 ? 2.321 24.395 4.389 1.00 55.71 ? 182 THR A N 1 ATOM 1581 C CA . THR A 1 182 ? 0.986 23.935 4.776 1.00 63.03 ? 182 THR A CA 1 ATOM 1582 C C . THR A 1 182 ? 0.817 23.903 6.293 1.00 61.00 ? 182 THR A C 1 ATOM 1583 O O . THR A 1 182 ? 1.194 24.848 6.986 1.00 55.85 ? 182 THR A O 1 ATOM 1584 C CB . THR A 1 182 ? 0.646 22.550 4.173 1.00 64.96 ? 182 THR A CB 1 ATOM 1585 O OG1 . THR A 1 182 ? 0.467 22.672 2.757 1.00 70.55 ? 182 THR A OG1 1 ATOM 1586 C CG2 . THR A 1 182 ? -0.628 21.995 4.793 1.00 60.40 ? 182 THR A CG2 1 ATOM 1587 N N . ASP B 2 4 ? 32.440 49.534 2.599 1.00 53.96 ? 2 ASP B N 1 ATOM 1588 C CA . ASP B 2 4 ? 33.803 49.372 2.107 1.00 44.25 ? 2 ASP B CA 1 ATOM 1589 C C . ASP B 2 4 ? 33.815 49.409 0.585 1.00 44.87 ? 2 ASP B C 1 ATOM 1590 O O . ASP B 2 4 ? 33.457 48.430 -0.070 1.00 52.40 ? 2 ASP B O 1 ATOM 1591 C CB . ASP B 2 4 ? 34.391 48.050 2.603 1.00 40.55 ? 2 ASP B CB 1 ATOM 1592 C CG . ASP B 2 4 ? 35.909 48.023 2.547 1.00 32.45 ? 2 ASP B CG 1 ATOM 1593 O OD1 . ASP B 2 4 ? 36.506 48.864 1.838 1.00 28.42 ? 2 ASP B OD1 1 ATOM 1594 O OD2 . ASP B 2 4 ? 36.508 47.158 3.219 1.00 36.91 ? 2 ASP B OD2 1 ATOM 1595 N N . THR B 2 5 ? 34.230 50.540 0.025 1.00 38.44 ? 3 THR B N 1 ATOM 1596 C CA . THR B 2 5 ? 34.238 50.713 -1.423 1.00 35.57 ? 3 THR B CA 1 ATOM 1597 C C . THR B 2 5 ? 35.637 50.592 -2.025 1.00 25.00 ? 3 THR B C 1 ATOM 1598 O O . THR B 2 5 ? 35.817 50.801 -3.226 1.00 34.72 ? 3 THR B O 1 ATOM 1599 C CB . THR B 2 5 ? 33.635 52.074 -1.830 1.00 40.86 ? 3 THR B CB 1 ATOM 1600 O OG1 . THR B 2 5 ? 34.326 53.126 -1.148 1.00 45.55 ? 3 THR B OG1 1 ATOM 1601 C CG2 . THR B 2 5 ? 32.161 52.129 -1.473 1.00 47.23 ? 3 THR B CG2 1 ATOM 1602 N N . ARG B 2 6 ? 36.624 50.265 -1.196 1.00 22.83 ? 4 ARG B N 1 ATOM 1603 C CA . ARG B 2 6 ? 37.996 50.124 -1.676 1.00 19.00 ? 4 ARG B CA 1 ATOM 1604 C C . ARG B 2 6 ? 38.065 49.073 -2.773 1.00 16.91 ? 4 ARG B C 1 ATOM 1605 O O . ARG B 2 6 ? 37.436 48.020 -2.662 1.00 20.18 ? 4 ARG B O 1 ATOM 1606 C CB . ARG B 2 6 ? 38.938 49.722 -0.540 1.00 20.24 ? 4 ARG B CB 1 ATOM 1607 C CG . ARG B 2 6 ? 39.248 50.839 0.452 1.00 26.30 ? 4 ARG B CG 1 ATOM 1608 C CD . ARG B 2 6 ? 40.211 50.338 1.510 1.00 30.07 ? 4 ARG B CD 1 ATOM 1609 N NE . ARG B 2 6 ? 39.619 49.270 2.313 1.00 33.33 ? 4 ARG B NE 1 ATOM 1610 C CZ . ARG B 2 6 ? 40.312 48.463 3.110 1.00 31.97 ? 4 ARG B CZ 1 ATOM 1611 N NH1 . ARG B 2 6 ? 41.628 48.595 3.204 1.00 30.00 ? 4 ARG B NH1 1 ATOM 1612 N NH2 . ARG B 2 6 ? 39.689 47.523 3.808 1.00 33.31 ? 4 ARG B NH2 1 ATOM 1613 N N . PRO B 2 7 ? 38.831 49.353 -3.838 1.00 16.54 ? 5 PRO B N 1 ATOM 1614 C CA . PRO B 2 7 ? 38.967 48.357 -4.906 1.00 15.20 ? 5 PRO B CA 1 ATOM 1615 C C . PRO B 2 7 ? 39.629 47.071 -4.422 1.00 16.92 ? 5 PRO B C 1 ATOM 1616 O O . PRO B 2 7 ? 40.523 47.106 -3.578 1.00 15.68 ? 5 PRO B O 1 ATOM 1617 C CB . PRO B 2 7 ? 39.859 49.057 -5.936 1.00 16.18 ? 5 PRO B CB 1 ATOM 1618 C CG . PRO B 2 7 ? 40.538 50.169 -5.181 1.00 22.42 ? 5 PRO B CG 1 ATOM 1619 C CD . PRO B 2 7 ? 39.559 50.598 -4.139 1.00 20.97 ? 5 PRO B CD 1 ATOM 1620 N N . ARG B 2 8 ? 39.178 45.943 -4.953 1.00 13.15 ? 6 ARG B N 1 ATOM 1621 C CA . ARG B 2 8 ? 39.771 44.656 -4.611 1.00 12.23 ? 6 ARG B CA 1 ATOM 1622 C C . ARG B 2 8 ? 40.590 44.098 -5.768 1.00 11.33 ? 6 ARG B C 1 ATOM 1623 O O . ARG B 2 8 ? 40.319 44.393 -6.931 1.00 11.56 ? 6 ARG B O 1 ATOM 1624 C CB . ARG B 2 8 ? 38.687 43.642 -4.208 1.00 11.87 ? 6 ARG B CB 1 ATOM 1625 C CG . ARG B 2 8 ? 38.550 43.453 -2.702 1.00 12.42 ? 6 ARG B CG 1 ATOM 1626 C CD . ARG B 2 8 ? 38.155 44.746 -1.999 1.00 13.73 ? 6 ARG B CD 1 ATOM 1627 N NE . ARG B 2 8 ? 38.179 44.563 -0.552 1.00 15.09 ? 6 ARG B NE 1 ATOM 1628 C CZ . ARG B 2 8 ? 37.792 45.481 0.330 1.00 15.70 ? 6 ARG B CZ 1 ATOM 1629 N NH1 . ARG B 2 8 ? 37.327 46.656 -0.079 1.00 17.57 ? 6 ARG B NH1 1 ATOM 1630 N NH2 . ARG B 2 8 ? 37.855 45.214 1.627 1.00 17.66 ? 6 ARG B NH2 1 ATOM 1631 N N . PHE B 2 9 ? 41.590 43.284 -5.437 1.00 10.80 ? 7 PHE B N 1 ATOM 1632 C CA . PHE B 2 9 ? 42.434 42.625 -6.435 1.00 10.02 ? 7 PHE B CA 1 ATOM 1633 C C . PHE B 2 9 ? 42.632 41.178 -6.016 1.00 9.30 ? 7 PHE B C 1 ATOM 1634 O O . PHE B 2 9 ? 42.974 40.903 -4.865 1.00 10.35 ? 7 PHE B O 1 ATOM 1635 C CB . PHE B 2 9 ? 43.786 43.342 -6.540 1.00 10.44 ? 7 PHE B CB 1 ATOM 1636 C CG . PHE B 2 9 ? 43.658 44.818 -6.753 1.00 11.38 ? 7 PHE B CG 1 ATOM 1637 C CD1 . PHE B 2 9 ? 43.584 45.681 -5.675 1.00 12.36 ? 7 PHE B CD1 1 ATOM 1638 C CD2 . PHE B 2 9 ? 43.594 45.338 -8.031 1.00 13.93 ? 7 PHE B CD2 1 ATOM 1639 C CE1 . PHE B 2 9 ? 43.449 47.043 -5.869 1.00 16.05 ? 7 PHE B CE1 1 ATOM 1640 C CE2 . PHE B 2 9 ? 43.456 46.699 -8.232 1.00 12.45 ? 7 PHE B CE2 1 ATOM 1641 C CZ . PHE B 2 9 ? 43.392 47.546 -7.153 1.00 13.75 ? 7 PHE B CZ 1 ATOM 1642 N N . LEU B 2 10 ? 42.394 40.253 -6.942 1.00 8.56 ? 8 LEU B N 1 ATOM 1643 C CA . LEU B 2 10 ? 42.401 38.824 -6.616 1.00 7.97 ? 8 LEU B CA 1 ATOM 1644 C C . LEU B 2 10 ? 43.357 38.023 -7.487 1.00 7.39 ? 8 LEU B C 1 ATOM 1645 O O . LEU B 2 10 ? 43.352 38.169 -8.710 1.00 8.72 ? 8 LEU B O 1 ATOM 1646 C CB . LEU B 2 10 ? 40.988 38.265 -6.818 1.00 7.80 ? 8 LEU B CB 1 ATOM 1647 C CG . LEU B 2 10 ? 40.801 36.774 -6.567 1.00 7.39 ? 8 LEU B CG 1 ATOM 1648 C CD1 . LEU B 2 10 ? 40.898 36.473 -5.074 1.00 9.01 ? 8 LEU B CD1 1 ATOM 1649 C CD2 . LEU B 2 10 ? 39.440 36.353 -7.124 1.00 10.65 ? 8 LEU B CD2 1 ATOM 1650 N N . GLU B 2 11 ? 44.185 37.192 -6.855 1.00 7.24 ? 9 GLU B N 1 ATOM 1651 C CA . GLU B 2 11 ? 45.014 36.228 -7.569 1.00 6.77 ? 9 GLU B CA 1 ATOM 1652 C C . GLU B 2 11 ? 44.483 34.834 -7.243 1.00 8.13 ? 9 GLU B C 1 ATOM 1653 O O . GLU B 2 11 ? 44.196 34.548 -6.081 1.00 9.32 ? 9 GLU B O 1 ATOM 1654 C CB . GLU B 2 11 ? 46.469 36.340 -7.094 1.00 8.74 ? 9 GLU B CB 1 ATOM 1655 C CG . GLU B 2 11 ? 47.424 35.296 -7.684 1.00 7.50 ? 9 GLU B CG 1 ATOM 1656 C CD . GLU B 2 11 ? 47.897 35.628 -9.087 1.00 10.26 ? 9 GLU B CD 1 ATOM 1657 O OE1 . GLU B 2 11 ? 47.652 36.761 -9.552 1.00 10.25 ? 9 GLU B OE1 1 ATOM 1658 O OE2 . GLU B 2 11 ? 48.528 34.747 -9.727 1.00 9.86 ? 9 GLU B OE2 1 ATOM 1659 N N . GLN B 2 12 ? 44.339 33.978 -8.256 1.00 6.31 ? 10 GLN B N 1 ATOM 1660 C CA . GLN B 2 12 ? 43.998 32.571 -8.019 1.00 7.12 ? 10 GLN B CA 1 ATOM 1661 C C . GLN B 2 12 ? 44.991 31.660 -8.721 1.00 7.51 ? 10 GLN B C 1 ATOM 1662 O O . GLN B 2 12 ? 45.545 32.010 -9.764 1.00 6.91 ? 10 GLN B O 1 ATOM 1663 C CB . GLN B 2 12 ? 42.603 32.199 -8.526 1.00 6.47 ? 10 GLN B CB 1 ATOM 1664 C CG . GLN B 2 12 ? 41.474 33.121 -8.073 1.00 6.00 ? 10 GLN B CG 1 ATOM 1665 C CD . GLN B 2 12 ? 40.112 32.588 -8.447 1.00 8.61 ? 10 GLN B CD 1 ATOM 1666 O OE1 . GLN B 2 12 ? 39.719 31.497 -8.021 1.00 9.25 ? 10 GLN B OE1 1 ATOM 1667 N NE2 . GLN B 2 12 ? 39.383 33.348 -9.267 1.00 7.02 ? 10 GLN B NE2 1 ATOM 1668 N N . VAL B 2 13 ? 45.200 30.479 -8.147 1.00 5.62 ? 11 VAL B N 1 ATOM 1669 C CA . VAL B 2 13 ? 45.979 29.445 -8.804 1.00 5.53 ? 11 VAL B CA 1 ATOM 1670 C C . VAL B 2 13 ? 45.197 28.149 -8.680 1.00 7.04 ? 11 VAL B C 1 ATOM 1671 O O . VAL B 2 13 ? 44.669 27.841 -7.613 1.00 7.79 ? 11 VAL B O 1 ATOM 1672 C CB . VAL B 2 13 ? 47.371 29.261 -8.166 1.00 7.96 ? 11 VAL B CB 1 ATOM 1673 C CG1 . VAL B 2 13 ? 48.194 28.311 -9.010 1.00 10.26 ? 11 VAL B CG1 1 ATOM 1674 C CG2 . VAL B 2 13 ? 48.094 30.585 -8.053 1.00 8.07 ? 11 VAL B CG2 1 ATOM 1675 N N . LYS B 2 14 ? 45.087 27.405 -9.773 1.00 5.88 ? 12 LYS B N 1 ATOM 1676 C CA . LYS B 2 14 ? 44.444 26.093 -9.699 1.00 5.62 ? 12 LYS B CA 1 ATOM 1677 C C . LYS B 2 14 ? 45.362 25.082 -10.343 1.00 5.78 ? 12 LYS B C 1 ATOM 1678 O O . LYS B 2 14 ? 45.677 25.185 -11.523 1.00 7.65 ? 12 LYS B O 1 ATOM 1679 C CB . LYS B 2 14 ? 43.088 26.128 -10.412 1.00 5.84 ? 12 LYS B CB 1 ATOM 1680 C CG . LYS B 2 14 ? 42.095 27.079 -9.717 1.00 5.59 ? 12 LYS B CG 1 ATOM 1681 C CD . LYS B 2 14 ? 40.739 27.130 -10.417 1.00 5.78 ? 12 LYS B CD 1 ATOM 1682 C CE . LYS B 2 14 ? 39.778 28.036 -9.647 1.00 10.51 ? 12 LYS B CE 1 ATOM 1683 N NZ . LYS B 2 14 ? 38.413 28.127 -10.250 1.00 8.07 ? 12 LYS B NZ 1 ATOM 1684 N N . HIS B 2 15 ? 45.811 24.122 -9.548 1.00 6.10 ? 13 HIS B N 1 ATOM 1685 C CA . HIS B 2 15 ? 46.661 23.059 -10.056 1.00 7.89 ? 13 HIS B CA 1 ATOM 1686 C C . HIS B 2 15 ? 45.732 21.866 -10.225 1.00 8.35 ? 13 HIS B C 1 ATOM 1687 O O . HIS B 2 15 ? 45.265 21.307 -9.233 1.00 8.01 ? 13 HIS B O 1 ATOM 1688 C CB . HIS B 2 15 ? 47.778 22.718 -9.061 1.00 9.15 ? 13 HIS B CB 1 ATOM 1689 C CG . HIS B 2 15 ? 48.420 23.906 -8.393 1.00 8.98 ? 13 HIS B CG 1 ATOM 1690 N ND1 . HIS B 2 15 ? 49.554 24.522 -8.893 1.00 9.91 ? 13 HIS B ND1 1 ATOM 1691 C CD2 . HIS B 2 15 ? 48.129 24.553 -7.239 1.00 9.95 ? 13 HIS B CD2 1 ATOM 1692 C CE1 . HIS B 2 15 ? 49.922 25.498 -8.083 1.00 10.97 ? 13 HIS B CE1 1 ATOM 1693 N NE2 . HIS B 2 15 ? 49.077 25.541 -7.068 1.00 9.59 ? 13 HIS B NE2 1 ATOM 1694 N N . GLU B 2 16 ? 45.439 21.490 -11.471 1.00 6.81 ? 14 GLU B N 1 ATOM 1695 C CA . GLU B 2 16 ? 44.362 20.531 -11.748 1.00 7.20 ? 14 GLU B CA 1 ATOM 1696 C C . GLU B 2 16 ? 44.881 19.192 -12.254 1.00 8.99 ? 14 GLU B C 1 ATOM 1697 O O . GLU B 2 16 ? 45.769 19.137 -13.098 1.00 10.10 ? 14 GLU B O 1 ATOM 1698 C CB . GLU B 2 16 ? 43.396 21.091 -12.798 1.00 7.51 ? 14 GLU B CB 1 ATOM 1699 C CG . GLU B 2 16 ? 42.863 22.490 -12.500 1.00 8.64 ? 14 GLU B CG 1 ATOM 1700 C CD . GLU B 2 16 ? 41.795 22.918 -13.486 1.00 9.85 ? 14 GLU B CD 1 ATOM 1701 O OE1 . GLU B 2 16 ? 41.574 22.204 -14.484 1.00 12.25 ? 14 GLU B OE1 1 ATOM 1702 O OE2 . GLU B 2 16 ? 41.161 23.970 -13.259 1.00 10.62 ? 14 GLU B OE2 1 ATOM 1703 N N . CYS B 2 17 ? 44.303 18.109 -11.743 1.00 8.37 ? 15 CYS B N 1 ATOM 1704 C CA . CYS B 2 17 ? 44.636 16.774 -12.218 1.00 9.15 ? 15 CYS B CA 1 ATOM 1705 C C . CYS B 2 17 ? 43.377 16.145 -12.766 1.00 10.81 ? 15 CYS B C 1 ATOM 1706 O O . CYS B 2 17 ? 42.391 16.014 -12.045 1.00 11.68 ? 15 CYS B O 1 ATOM 1707 C CB . CYS B 2 17 ? 45.179 15.930 -11.073 1.00 11.12 ? 15 CYS B CB 1 ATOM 1708 S SG . CYS B 2 17 ? 46.781 16.509 -10.502 1.00 13.58 ? 15 CYS B SG 1 ATOM 1709 N N . HIS B 2 18 ? 43.403 15.778 -14.044 1.00 11.94 ? 16 HIS B N 1 ATOM 1710 C CA . HIS B 2 18 ? 42.228 15.197 -14.698 1.00 12.78 ? 16 HIS B CA 1 ATOM 1711 C C . HIS B 2 18 ? 42.480 13.723 -14.981 1.00 11.81 ? 16 HIS B C 1 ATOM 1712 O O . HIS B 2 18 ? 43.490 13.371 -15.581 1.00 13.16 ? 16 HIS B O 1 ATOM 1713 C CB . HIS B 2 18 ? 41.931 15.955 -15.997 1.00 11.19 ? 16 HIS B CB 1 ATOM 1714 C CG . HIS B 2 18 ? 41.580 17.396 -15.782 1.00 12.25 ? 16 HIS B CG 1 ATOM 1715 N ND1 . HIS B 2 18 ? 40.300 17.880 -15.967 1.00 15.64 ? 16 HIS B ND1 1 ATOM 1716 C CD2 . HIS B 2 18 ? 42.323 18.447 -15.368 1.00 14.51 ? 16 HIS B CD2 1 ATOM 1717 C CE1 . HIS B 2 18 ? 40.279 19.171 -15.692 1.00 13.89 ? 16 HIS B CE1 1 ATOM 1718 N NE2 . HIS B 2 18 ? 41.493 19.543 -15.327 1.00 12.28 ? 16 HIS B NE2 1 ATOM 1719 N N . PHE B 2 19 ? 41.566 12.859 -14.540 1.00 12.52 ? 17 PHE B N 1 ATOM 1720 C CA . PHE B 2 19 ? 41.794 11.416 -14.611 1.00 14.41 ? 17 PHE B CA 1 ATOM 1721 C C . PHE B 2 19 ? 40.784 10.752 -15.532 1.00 14.71 ? 17 PHE B C 1 ATOM 1722 O O . PHE B 2 19 ? 39.593 11.055 -15.477 1.00 18.38 ? 17 PHE B O 1 ATOM 1723 C CB . PHE B 2 19 ? 41.693 10.796 -13.220 1.00 14.66 ? 17 PHE B CB 1 ATOM 1724 C CG . PHE B 2 19 ? 42.664 11.369 -12.230 1.00 15.63 ? 17 PHE B CG 1 ATOM 1725 C CD1 . PHE B 2 19 ? 42.319 12.474 -11.464 1.00 14.19 ? 17 PHE B CD1 1 ATOM 1726 C CD2 . PHE B 2 19 ? 43.917 10.797 -12.057 1.00 15.80 ? 17 PHE B CD2 1 ATOM 1727 C CE1 . PHE B 2 19 ? 43.201 13.009 -10.551 1.00 12.99 ? 17 PHE B CE1 1 ATOM 1728 C CE2 . PHE B 2 19 ? 44.816 11.328 -11.141 1.00 13.18 ? 17 PHE B CE2 1 ATOM 1729 C CZ . PHE B 2 19 ? 44.460 12.433 -10.387 1.00 12.40 ? 17 PHE B CZ 1 ATOM 1730 N N . PHE B 2 20 ? 41.274 9.847 -16.375 1.00 15.70 ? 18 PHE B N 1 ATOM 1731 C CA . PHE B 2 20 ? 40.439 9.117 -17.325 1.00 20.83 ? 18 PHE B CA 1 ATOM 1732 C C . PHE B 2 20 ? 40.733 7.625 -17.168 1.00 21.85 ? 18 PHE B C 1 ATOM 1733 O O . PHE B 2 20 ? 41.891 7.221 -17.231 1.00 22.30 ? 18 PHE B O 1 ATOM 1734 C CB . PHE B 2 20 ? 40.765 9.538 -18.768 1.00 26.28 ? 18 PHE B CB 1 ATOM 1735 C CG . PHE B 2 20 ? 40.825 11.037 -18.988 1.00 38.08 ? 18 PHE B CG 1 ATOM 1736 C CD1 . PHE B 2 20 ? 41.939 11.773 -18.604 1.00 37.43 ? 18 PHE B CD1 1 ATOM 1737 C CD2 . PHE B 2 20 ? 39.785 11.700 -19.619 1.00 44.23 ? 18 PHE B CD2 1 ATOM 1738 C CE1 . PHE B 2 20 ? 42.001 13.138 -18.814 1.00 31.15 ? 18 PHE B CE1 1 ATOM 1739 C CE2 . PHE B 2 20 ? 39.840 13.072 -19.832 1.00 40.65 ? 18 PHE B CE2 1 ATOM 1740 C CZ . PHE B 2 20 ? 40.950 13.789 -19.428 1.00 31.61 ? 18 PHE B CZ 1 ATOM 1741 N N . ASN B 2 21 ? 39.698 6.811 -16.965 1.00 23.01 ? 19 ASN B N 1 ATOM 1742 C CA . ASN B 2 21 ? 39.874 5.365 -16.805 1.00 29.17 ? 19 ASN B CA 1 ATOM 1743 C C . ASN B 2 21 ? 40.842 5.063 -15.664 1.00 27.48 ? 19 ASN B C 1 ATOM 1744 O O . ASN B 2 21 ? 41.923 4.511 -15.878 1.00 24.48 ? 19 ASN B O 1 ATOM 1745 C CB . ASN B 2 21 ? 40.359 4.744 -18.125 1.00 30.08 ? 19 ASN B CB 1 ATOM 1746 C CG . ASN B 2 21 ? 40.432 3.223 -18.083 1.00 40.92 ? 19 ASN B CG 1 ATOM 1747 O OD1 . ASN B 2 21 ? 39.954 2.585 -17.145 1.00 41.54 ? 19 ASN B OD1 1 ATOM 1748 N ND2 . ASN B 2 21 ? 41.038 2.640 -19.117 1.00 54.05 ? 19 ASN B ND2 1 ATOM 1749 N N . GLY B 2 22 ? 40.453 5.437 -14.451 1.00 30.94 ? 20 GLY B N 1 ATOM 1750 C CA . GLY B 2 22 ? 41.341 5.335 -13.307 1.00 35.16 ? 20 GLY B CA 1 ATOM 1751 C C . GLY B 2 22 ? 42.505 6.298 -13.450 1.00 33.49 ? 20 GLY B C 1 ATOM 1752 O O . GLY B 2 22 ? 42.303 7.494 -13.630 1.00 34.02 ? 20 GLY B O 1 ATOM 1753 N N . THR B 2 23 ? 43.726 5.772 -13.383 1.00 21.58 ? 21 THR B N 1 ATOM 1754 C CA . THR B 2 23 ? 44.928 6.574 -13.604 1.00 22.62 ? 21 THR B CA 1 ATOM 1755 C C . THR B 2 23 ? 45.615 6.186 -14.912 1.00 23.05 ? 21 THR B C 1 ATOM 1756 O O . THR B 2 23 ? 46.794 6.486 -15.118 1.00 23.03 ? 21 THR B O 1 ATOM 1757 C CB . THR B 2 23 ? 45.934 6.412 -12.456 1.00 21.21 ? 21 THR B CB 1 ATOM 1758 O OG1 . THR B 2 23 ? 46.154 5.021 -12.211 1.00 25.91 ? 21 THR B OG1 1 ATOM 1759 C CG2 . THR B 2 23 ? 45.405 7.056 -11.191 1.00 29.55 ? 21 THR B CG2 1 ATOM 1760 N N . GLU B 2 24 ? 44.873 5.524 -15.793 1.00 22.16 ? 22 GLU B N 1 ATOM 1761 C CA . GLU B 2 24 ? 45.422 5.073 -17.067 1.00 24.70 ? 22 GLU B CA 1 ATOM 1762 C C . GLU B 2 24 ? 45.825 6.265 -17.923 1.00 21.42 ? 22 GLU B C 1 ATOM 1763 O O . GLU B 2 24 ? 46.896 6.277 -18.523 1.00 25.35 ? 22 GLU B O 1 ATOM 1764 C CB . GLU B 2 24 ? 44.406 4.201 -17.811 1.00 31.44 ? 22 GLU B CB 1 ATOM 1765 C CG . GLU B 2 24 ? 45.007 3.341 -18.906 1.00 48.78 ? 22 GLU B CG 1 ATOM 1766 C CD . GLU B 2 24 ? 45.965 2.287 -18.371 1.00 58.66 ? 22 GLU B CD 1 ATOM 1767 O OE1 . GLU B 2 24 ? 45.883 1.947 -17.168 1.00 49.98 ? 22 GLU B OE1 1 ATOM 1768 O OE2 . GLU B 2 24 ? 46.806 1.800 -19.157 1.00 70.28 ? 22 GLU B OE2 1 ATOM 1769 N N . ARG B 2 25 ? 44.969 7.281 -17.951 1.00 18.36 ? 23 ARG B N 1 ATOM 1770 C CA . ARG B 2 25 ? 45.265 8.512 -18.669 1.00 17.38 ? 23 ARG B CA 1 ATOM 1771 C C . ARG B 2 25 ? 45.066 9.694 -17.727 1.00 17.28 ? 23 ARG B C 1 ATOM 1772 O O . ARG B 2 25 ? 44.025 9.820 -17.087 1.00 17.48 ? 23 ARG B O 1 ATOM 1773 C CB . ARG B 2 25 ? 44.381 8.633 -19.910 1.00 21.06 ? 23 ARG B CB 1 ATOM 1774 C CG . ARG B 2 25 ? 44.216 10.042 -20.470 1.00 42.54 ? 23 ARG B CG 1 ATOM 1775 C CD . ARG B 2 25 ? 45.510 10.671 -20.980 1.00 56.98 ? 23 ARG B CD 1 ATOM 1776 N NE . ARG B 2 25 ? 45.241 11.975 -21.591 1.00 61.49 ? 23 ARG B NE 1 ATOM 1777 C CZ . ARG B 2 25 ? 46.125 12.965 -21.694 1.00 50.22 ? 23 ARG B CZ 1 ATOM 1778 N NH1 . ARG B 2 25 ? 47.356 12.817 -21.219 1.00 37.67 ? 23 ARG B NH1 1 ATOM 1779 N NH2 . ARG B 2 25 ? 45.772 14.113 -22.269 1.00 37.62 ? 23 ARG B NH2 1 ATOM 1780 N N . VAL B 2 26 ? 46.081 10.550 -17.628 1.00 15.00 ? 24 VAL B N 1 ATOM 1781 C CA . VAL B 2 26 ? 46.044 11.666 -16.696 1.00 13.70 ? 24 VAL B CA 1 ATOM 1782 C C . VAL B 2 26 ? 46.539 12.928 -17.393 1.00 13.94 ? 24 VAL B C 1 ATOM 1783 O O . VAL B 2 26 ? 47.513 12.888 -18.148 1.00 17.74 ? 24 VAL B O 1 ATOM 1784 C CB . VAL B 2 26 ? 46.929 11.393 -15.447 1.00 13.86 ? 24 VAL B CB 1 ATOM 1785 C CG1 . VAL B 2 26 ? 46.881 12.570 -14.484 1.00 14.76 ? 24 VAL B CG1 1 ATOM 1786 C CG2 . VAL B 2 26 ? 46.508 10.099 -14.750 1.00 16.22 ? 24 VAL B CG2 1 ATOM 1787 N N . ARG B 2 27 ? 45.847 14.041 -17.151 1.00 11.96 ? 25 ARG B N 1 ATOM 1788 C CA . ARG B 2 27 ? 46.257 15.341 -17.671 1.00 11.71 ? 25 ARG B CA 1 ATOM 1789 C C . ARG B 2 27 ? 46.380 16.320 -16.523 1.00 12.65 ? 25 ARG B C 1 ATOM 1790 O O . ARG B 2 27 ? 45.514 16.384 -15.652 1.00 12.89 ? 25 ARG B O 1 ATOM 1791 C CB . ARG B 2 27 ? 45.240 15.852 -18.692 1.00 14.11 ? 25 ARG B CB 1 ATOM 1792 C CG . ARG B 2 27 ? 45.604 17.161 -19.359 1.00 16.29 ? 25 ARG B CG 1 ATOM 1793 C CD . ARG B 2 27 ? 44.670 17.422 -20.536 1.00 17.06 ? 25 ARG B CD 1 ATOM 1794 N NE . ARG B 2 27 ? 44.826 18.759 -21.110 1.00 16.23 ? 25 ARG B NE 1 ATOM 1795 C CZ . ARG B 2 27 ? 44.125 19.195 -22.153 1.00 39.45 ? 25 ARG B CZ 1 ATOM 1796 N NH1 . ARG B 2 27 ? 43.229 18.398 -22.728 1.00 44.56 ? 25 ARG B NH1 1 ATOM 1797 N NH2 . ARG B 2 27 ? 44.314 20.422 -22.623 1.00 31.50 ? 25 ARG B NH2 1 ATOM 1798 N N . PHE B 2 28 ? 47.465 17.086 -16.534 1.00 9.80 ? 26 PHE B N 1 ATOM 1799 C CA . PHE B 2 28 ? 47.749 18.052 -15.486 1.00 9.01 ? 26 PHE B CA 1 ATOM 1800 C C . PHE B 2 28 ? 47.712 19.446 -16.087 1.00 10.19 ? 26 PHE B C 1 ATOM 1801 O O . PHE B 2 28 ? 48.325 19.686 -17.128 1.00 10.37 ? 26 PHE B O 1 ATOM 1802 C CB . PHE B 2 28 ? 49.133 17.765 -14.887 1.00 9.24 ? 26 PHE B CB 1 ATOM 1803 C CG . PHE B 2 28 ? 49.678 18.886 -14.038 1.00 8.62 ? 26 PHE B CG 1 ATOM 1804 C CD1 . PHE B 2 28 ? 49.088 19.207 -12.824 1.00 12.13 ? 26 PHE B CD1 1 ATOM 1805 C CD2 . PHE B 2 28 ? 50.773 19.623 -14.463 1.00 10.31 ? 26 PHE B CD2 1 ATOM 1806 C CE1 . PHE B 2 28 ? 49.580 20.244 -12.047 1.00 14.39 ? 26 PHE B CE1 1 ATOM 1807 C CE2 . PHE B 2 28 ? 51.275 20.663 -13.685 1.00 11.47 ? 26 PHE B CE2 1 ATOM 1808 C CZ . PHE B 2 28 ? 50.684 20.969 -12.477 1.00 12.00 ? 26 PHE B CZ 1 ATOM 1809 N N . LEU B 2 29 ? 46.973 20.354 -15.443 1.00 8.34 ? 27 LEU B N 1 ATOM 1810 C CA . LEU B 2 29 ? 46.941 21.764 -15.838 1.00 7.35 ? 27 LEU B CA 1 ATOM 1811 C C . LEU B 2 29 ? 47.348 22.646 -14.664 1.00 11.80 ? 27 LEU B C 1 ATOM 1812 O O . LEU B 2 29 ? 46.748 22.571 -13.594 1.00 12.09 ? 27 LEU B O 1 ATOM 1813 C CB . LEU B 2 29 ? 45.523 22.165 -16.266 1.00 12.93 ? 27 LEU B CB 1 ATOM 1814 C CG . LEU B 2 29 ? 44.873 21.447 -17.439 1.00 16.35 ? 27 LEU B CG 1 ATOM 1815 C CD1 . LEU B 2 29 ? 43.479 22.043 -17.679 1.00 19.73 ? 27 LEU B CD1 1 ATOM 1816 C CD2 . LEU B 2 29 ? 45.717 21.559 -18.696 1.00 19.30 ? 27 LEU B CD2 1 ATOM 1817 N N . ASP B 2 30 ? 48.336 23.513 -14.870 1.00 6.68 ? 28 ASP B N 1 ATOM 1818 C CA . ASP B 2 30 ? 48.766 24.453 -13.835 1.00 8.76 ? 28 ASP B CA 1 ATOM 1819 C C . ASP B 2 30 ? 48.275 25.820 -14.279 1.00 11.32 ? 28 ASP B C 1 ATOM 1820 O O . ASP B 2 30 ? 48.779 26.348 -15.255 1.00 12.37 ? 28 ASP B O 1 ATOM 1821 C CB . ASP B 2 30 ? 50.298 24.462 -13.757 1.00 10.32 ? 28 ASP B CB 1 ATOM 1822 C CG . ASP B 2 30 ? 50.824 24.786 -12.371 1.00 12.78 ? 28 ASP B CG 1 ATOM 1823 O OD1 . ASP B 2 30 ? 50.238 24.298 -11.374 1.00 14.14 ? 28 ASP B OD1 1 ATOM 1824 O OD2 . ASP B 2 30 ? 51.847 25.504 -12.275 1.00 12.66 ? 28 ASP B OD2 1 ATOM 1825 N N . ARG B 2 31 ? 47.282 26.381 -13.587 1.00 6.21 ? 29 ARG B N 1 ATOM 1826 C CA . ARG B 2 31 ? 46.558 27.547 -14.108 1.00 5.67 ? 29 ARG B CA 1 ATOM 1827 C C . ARG B 2 31 ? 46.663 28.748 -13.175 1.00 6.36 ? 29 ARG B C 1 ATOM 1828 O O . ARG B 2 31 ? 46.448 28.616 -11.977 1.00 6.70 ? 29 ARG B O 1 ATOM 1829 C CB . ARG B 2 31 ? 45.084 27.178 -14.299 1.00 5.61 ? 29 ARG B CB 1 ATOM 1830 C CG . ARG B 2 31 ? 44.883 25.867 -15.074 1.00 5.96 ? 29 ARG B CG 1 ATOM 1831 C CD . ARG B 2 31 ? 43.403 25.529 -15.163 1.00 7.12 ? 29 ARG B CD 1 ATOM 1832 N NE . ARG B 2 31 ? 42.698 26.462 -16.035 1.00 7.86 ? 29 ARG B NE 1 ATOM 1833 C CZ . ARG B 2 31 ? 41.373 26.516 -16.139 1.00 7.77 ? 29 ARG B CZ 1 ATOM 1834 N NH1 . ARG B 2 31 ? 40.619 25.695 -15.417 1.00 10.88 ? 29 ARG B NH1 1 ATOM 1835 N NH2 . ARG B 2 31 ? 40.805 27.381 -16.971 1.00 8.33 ? 29 ARG B NH2 1 ATOM 1836 N N . TYR B 2 32 ? 47.000 29.915 -13.727 1.00 5.48 ? 30 TYR B N 1 ATOM 1837 C CA . TYR B 2 32 ? 47.094 31.150 -12.939 1.00 5.48 ? 30 TYR B CA 1 ATOM 1838 C C . TYR B 2 32 ? 46.077 32.185 -13.407 1.00 6.19 ? 30 TYR B C 1 ATOM 1839 O O . TYR B 2 32 ? 45.878 32.355 -14.608 1.00 7.12 ? 30 TYR B O 1 ATOM 1840 C CB . TYR B 2 32 ? 48.511 31.730 -13.040 1.00 6.92 ? 30 TYR B CB 1 ATOM 1841 C CG . TYR B 2 32 ? 49.529 30.941 -12.255 1.00 7.49 ? 30 TYR B CG 1 ATOM 1842 C CD1 . TYR B 2 32 ? 49.986 29.709 -12.704 1.00 7.36 ? 30 TYR B CD1 1 ATOM 1843 C CD2 . TYR B 2 32 ? 50.032 31.439 -11.063 1.00 10.40 ? 30 TYR B CD2 1 ATOM 1844 C CE1 . TYR B 2 32 ? 50.925 28.984 -11.959 1.00 8.90 ? 30 TYR B CE1 1 ATOM 1845 C CE2 . TYR B 2 32 ? 50.963 30.734 -10.325 1.00 12.19 ? 30 TYR B CE2 1 ATOM 1846 C CZ . TYR B 2 32 ? 51.399 29.517 -10.773 1.00 13.60 ? 30 TYR B CZ 1 ATOM 1847 O OH . TYR B 2 32 ? 52.315 28.832 -10.010 1.00 16.88 ? 30 TYR B OH 1 ATOM 1848 N N . PHE B 2 33 ? 45.438 32.864 -12.453 1.00 6.63 ? 31 PHE B N 1 ATOM 1849 C CA . PHE B 2 33 ? 44.344 33.791 -12.758 1.00 6.23 ? 31 PHE B CA 1 ATOM 1850 C C . PHE B 2 33 ? 44.509 35.132 -12.063 1.00 5.96 ? 31 PHE B C 1 ATOM 1851 O O . PHE B 2 33 ? 44.921 35.202 -10.913 1.00 7.87 ? 31 PHE B O 1 ATOM 1852 C CB . PHE B 2 33 ? 42.997 33.225 -12.280 1.00 7.63 ? 31 PHE B CB 1 ATOM 1853 C CG . PHE B 2 33 ? 42.703 31.834 -12.760 1.00 5.76 ? 31 PHE B CG 1 ATOM 1854 C CD1 . PHE B 2 33 ? 43.267 30.735 -12.121 1.00 5.43 ? 31 PHE B CD1 1 ATOM 1855 C CD2 . PHE B 2 33 ? 41.854 31.620 -13.835 1.00 7.33 ? 31 PHE B CD2 1 ATOM 1856 C CE1 . PHE B 2 33 ? 42.998 29.446 -12.550 1.00 6.48 ? 31 PHE B CE1 1 ATOM 1857 C CE2 . PHE B 2 33 ? 41.577 30.322 -14.271 1.00 8.08 ? 31 PHE B CE2 1 ATOM 1858 C CZ . PHE B 2 33 ? 42.154 29.237 -13.624 1.00 6.07 ? 31 PHE B CZ 1 ATOM 1859 N N . TYR B 2 34 ? 44.128 36.192 -12.763 1.00 6.29 ? 32 TYR B N 1 ATOM 1860 C CA . TYR B 2 34 ? 44.029 37.516 -12.160 1.00 6.71 ? 32 TYR B CA 1 ATOM 1861 C C . TYR B 2 34 ? 42.554 37.898 -12.235 1.00 10.50 ? 32 TYR B C 1 ATOM 1862 O O . TYR B 2 34 ? 41.995 38.007 -13.327 1.00 8.42 ? 32 TYR B O 1 ATOM 1863 C CB . TYR B 2 34 ? 44.928 38.508 -12.906 1.00 7.13 ? 32 TYR B CB 1 ATOM 1864 C CG . TYR B 2 34 ? 44.856 39.903 -12.337 1.00 7.72 ? 32 TYR B CG 1 ATOM 1865 C CD1 . TYR B 2 34 ? 45.312 40.169 -11.055 1.00 10.85 ? 32 TYR B CD1 1 ATOM 1866 C CD2 . TYR B 2 34 ? 44.327 40.955 -13.084 1.00 8.29 ? 32 TYR B CD2 1 ATOM 1867 C CE1 . TYR B 2 34 ? 45.239 41.448 -10.518 1.00 9.80 ? 32 TYR B CE1 1 ATOM 1868 C CE2 . TYR B 2 34 ? 44.259 42.252 -12.557 1.00 10.56 ? 32 TYR B CE2 1 ATOM 1869 C CZ . TYR B 2 34 ? 44.719 42.487 -11.274 1.00 9.12 ? 32 TYR B CZ 1 ATOM 1870 O OH . TYR B 2 34 ? 44.656 43.754 -10.730 1.00 11.53 ? 32 TYR B OH 1 ATOM 1871 N N . HIS B 2 35 ? 41.925 38.038 -11.064 1.00 7.67 ? 33 HIS B N 1 ATOM 1872 C CA . HIS B 2 35 ? 40.468 38.071 -10.926 1.00 8.01 ? 33 HIS B CA 1 ATOM 1873 C C . HIS B 2 35 ? 39.913 36.740 -11.469 1.00 8.70 ? 33 HIS B C 1 ATOM 1874 O O . HIS B 2 35 ? 40.230 35.688 -10.905 1.00 12.54 ? 33 HIS B O 1 ATOM 1875 C CB . HIS B 2 35 ? 39.842 39.312 -11.596 1.00 7.91 ? 33 HIS B CB 1 ATOM 1876 C CG . HIS B 2 35 ? 40.495 40.613 -11.223 1.00 9.07 ? 33 HIS B CG 1 ATOM 1877 N ND1 . HIS B 2 35 ? 41.099 40.842 -10.004 1.00 11.32 ? 33 HIS B ND1 1 ATOM 1878 C CD2 . HIS B 2 35 ? 40.612 41.772 -11.920 1.00 11.53 ? 33 HIS B CD2 1 ATOM 1879 C CE1 . HIS B 2 35 ? 41.573 42.079 -9.970 1.00 10.91 ? 33 HIS B CE1 1 ATOM 1880 N NE2 . HIS B 2 35 ? 41.287 42.663 -11.122 1.00 10.63 ? 33 HIS B NE2 1 ATOM 1881 N N . GLN B 2 36 ? 39.129 36.761 -12.552 1.00 9.37 ? 34 GLN B N 1 ATOM 1882 C CA . GLN B 2 36 ? 38.685 35.505 -13.185 1.00 10.45 ? 34 GLN B CA 1 ATOM 1883 C C . GLN B 2 36 ? 39.437 35.162 -14.465 1.00 11.99 ? 34 GLN B C 1 ATOM 1884 O O . GLN B 2 36 ? 39.124 34.173 -15.123 1.00 14.28 ? 34 GLN B O 1 ATOM 1885 C CB . GLN B 2 36 ? 37.189 35.538 -13.525 1.00 17.93 ? 34 GLN B CB 1 ATOM 1886 C CG . GLN B 2 36 ? 36.272 35.524 -12.342 1.00 16.93 ? 34 GLN B CG 1 ATOM 1887 C CD . GLN B 2 36 ? 35.946 36.915 -11.863 1.00 23.47 ? 34 GLN B CD 1 ATOM 1888 O OE1 . GLN B 2 36 ? 35.118 37.614 -12.455 1.00 32.41 ? 34 GLN B OE1 1 ATOM 1889 N NE2 . GLN B 2 36 ? 36.587 37.325 -10.778 1.00 17.51 ? 34 GLN B NE2 1 ATOM 1890 N N . GLU B 2 37 ? 40.406 35.992 -14.833 1.00 8.76 ? 35 GLU B N 1 ATOM 1891 C CA . GLU B 2 37 ? 41.073 35.869 -16.129 1.00 11.30 ? 35 GLU B CA 1 ATOM 1892 C C . GLU B 2 37 ? 42.286 34.959 -16.040 1.00 8.41 ? 35 GLU B C 1 ATOM 1893 O O . GLU B 2 37 ? 43.280 35.309 -15.402 1.00 9.19 ? 35 GLU B O 1 ATOM 1894 C CB . GLU B 2 37 ? 41.499 37.261 -16.630 1.00 12.78 ? 35 GLU B CB 1 ATOM 1895 C CG . GLU B 2 37 ? 42.430 37.262 -17.861 1.00 21.72 ? 35 GLU B CG 1 ATOM 1896 C CD . GLU B 2 37 ? 43.074 38.627 -18.141 1.00 29.93 ? 35 GLU B CD 1 ATOM 1897 O OE1 . GLU B 2 37 ? 44.102 38.675 -18.858 1.00 23.10 ? 35 GLU B OE1 1 ATOM 1898 O OE2 . GLU B 2 37 ? 42.561 39.655 -17.645 1.00 26.56 ? 35 GLU B OE2 1 ATOM 1899 N N . GLU B 2 38 ? 42.209 33.780 -16.659 1.00 7.82 ? 36 GLU B N 1 ATOM 1900 C CA . GLU B 2 38 ? 43.385 32.914 -16.725 1.00 6.32 ? 36 GLU B CA 1 ATOM 1901 C C . GLU B 2 38 ? 44.420 33.599 -17.603 1.00 7.66 ? 36 GLU B C 1 ATOM 1902 O O . GLU B 2 38 ? 44.107 33.976 -18.730 1.00 8.84 ? 36 GLU B O 1 ATOM 1903 C CB . GLU B 2 38 ? 43.006 31.572 -17.341 1.00 6.41 ? 36 GLU B CB 1 ATOM 1904 C CG . GLU B 2 38 ? 44.130 30.561 -17.233 1.00 6.65 ? 36 GLU B CG 1 ATOM 1905 C CD . GLU B 2 38 ? 43.740 29.208 -17.774 1.00 6.82 ? 36 GLU B CD 1 ATOM 1906 O OE1 . GLU B 2 38 ? 42.686 29.100 -18.454 1.00 10.36 ? 36 GLU B OE1 1 ATOM 1907 O OE2 . GLU B 2 38 ? 44.484 28.245 -17.492 1.00 8.33 ? 36 GLU B OE2 1 ATOM 1908 N N . TYR B 2 39 ? 45.648 33.764 -17.106 1.00 6.47 ? 37 TYR B N 1 ATOM 1909 C CA . TYR B 2 39 ? 46.651 34.484 -17.890 1.00 8.36 ? 37 TYR B CA 1 ATOM 1910 C C . TYR B 2 39 ? 47.812 33.630 -18.374 1.00 10.21 ? 37 TYR B C 1 ATOM 1911 O O . TYR B 2 39 ? 48.451 33.967 -19.357 1.00 8.86 ? 37 TYR B O 1 ATOM 1912 C CB . TYR B 2 39 ? 47.154 35.754 -17.180 1.00 7.13 ? 37 TYR B CB 1 ATOM 1913 C CG . TYR B 2 39 ? 47.812 35.575 -15.824 1.00 6.71 ? 37 TYR B CG 1 ATOM 1914 C CD1 . TYR B 2 39 ? 49.183 35.332 -15.718 1.00 9.31 ? 37 TYR B CD1 1 ATOM 1915 C CD2 . TYR B 2 39 ? 47.082 35.713 -14.650 1.00 7.92 ? 37 TYR B CD2 1 ATOM 1916 C CE1 . TYR B 2 39 ? 49.795 35.196 -14.476 1.00 8.44 ? 37 TYR B CE1 1 ATOM 1917 C CE2 . TYR B 2 39 ? 47.691 35.596 -13.409 1.00 6.36 ? 37 TYR B CE2 1 ATOM 1918 C CZ . TYR B 2 39 ? 49.048 35.326 -13.330 1.00 10.71 ? 37 TYR B CZ 1 ATOM 1919 O OH . TYR B 2 39 ? 49.659 35.198 -12.097 1.00 9.30 ? 37 TYR B OH 1 ATOM 1920 N N . VAL B 2 40 ? 48.072 32.526 -17.692 1.00 6.61 ? 38 VAL B N 1 ATOM 1921 C CA . VAL B 2 40 ? 49.123 31.611 -18.130 1.00 6.80 ? 38 VAL B CA 1 ATOM 1922 C C . VAL B 2 40 ? 48.812 30.208 -17.603 1.00 7.01 ? 38 VAL B C 1 ATOM 1923 O O . VAL B 2 40 ? 48.186 30.060 -16.545 1.00 7.11 ? 38 VAL B O 1 ATOM 1924 C CB . VAL B 2 40 ? 50.516 32.116 -17.668 1.00 8.00 ? 38 VAL B CB 1 ATOM 1925 C CG1 . VAL B 2 40 ? 50.609 32.115 -16.143 1.00 8.05 ? 38 VAL B CG1 1 ATOM 1926 C CG2 . VAL B 2 40 ? 51.644 31.299 -18.305 1.00 8.97 ? 38 VAL B CG2 1 ATOM 1927 N N . ARG B 2 41 ? 49.234 29.182 -18.342 1.00 6.82 ? 39 ARG B N 1 ATOM 1928 C CA . ARG B 2 41 ? 48.966 27.806 -17.925 1.00 6.95 ? 39 ARG B CA 1 ATOM 1929 C C . ARG B 2 41 ? 50.042 26.854 -18.429 1.00 11.09 ? 39 ARG B C 1 ATOM 1930 O O . ARG B 2 41 ? 50.602 27.056 -19.501 1.00 9.84 ? 39 ARG B O 1 ATOM 1931 C CB . ARG B 2 41 ? 47.609 27.320 -18.432 1.00 13.14 ? 39 ARG B CB 1 ATOM 1932 C CG . ARG B 2 41 ? 47.500 27.223 -19.937 1.00 15.59 ? 39 ARG B CG 1 ATOM 1933 C CD . ARG B 2 41 ? 46.409 26.229 -20.376 1.00 13.08 ? 39 ARG B CD 1 ATOM 1934 N NE . ARG B 2 41 ? 45.093 26.594 -19.858 1.00 11.97 ? 39 ARG B NE 1 ATOM 1935 C CZ . ARG B 2 41 ? 43.963 26.006 -20.225 1.00 16.34 ? 39 ARG B CZ 1 ATOM 1936 N NH1 . ARG B 2 41 ? 43.984 25.035 -21.129 1.00 15.62 ? 39 ARG B NH1 1 ATOM 1937 N NH2 . ARG B 2 41 ? 42.805 26.401 -19.706 1.00 16.55 ? 39 ARG B NH2 1 ATOM 1938 N N . PHE B 2 42 ? 50.331 25.826 -17.638 1.00 9.10 ? 40 PHE B N 1 ATOM 1939 C CA . PHE B 2 42 ? 51.084 24.674 -18.119 1.00 9.55 ? 40 PHE B CA 1 ATOM 1940 C C . PHE B 2 42 ? 50.079 23.540 -18.345 1.00 7.87 ? 40 PHE B C 1 ATOM 1941 O O . PHE B 2 42 ? 49.340 23.167 -17.439 1.00 8.65 ? 40 PHE B O 1 ATOM 1942 C CB . PHE B 2 42 ? 52.140 24.254 -17.085 1.00 7.79 ? 40 PHE B CB 1 ATOM 1943 C CG . PHE B 2 42 ? 52.896 22.991 -17.441 1.00 8.48 ? 40 PHE B CG 1 ATOM 1944 C CD1 . PHE B 2 42 ? 54.179 23.057 -17.966 1.00 9.06 ? 40 PHE B CD1 1 ATOM 1945 C CD2 . PHE B 2 42 ? 52.325 21.733 -17.238 1.00 8.68 ? 40 PHE B CD2 1 ATOM 1946 C CE1 . PHE B 2 42 ? 54.870 21.898 -18.289 1.00 9.82 ? 40 PHE B CE1 1 ATOM 1947 C CE2 . PHE B 2 42 ? 53.010 20.578 -17.554 1.00 9.44 ? 40 PHE B CE2 1 ATOM 1948 C CZ . PHE B 2 42 ? 54.284 20.656 -18.080 1.00 10.98 ? 40 PHE B CZ 1 ATOM 1949 N N . ASP B 2 43 ? 50.080 22.997 -19.555 1.00 8.51 ? 41 ASP B N 1 ATOM 1950 C CA . ASP B 2 43 ? 49.257 21.853 -19.928 1.00 8.94 ? 41 ASP B CA 1 ATOM 1951 C C . ASP B 2 43 ? 50.201 20.681 -20.175 1.00 10.46 ? 41 ASP B C 1 ATOM 1952 O O . ASP B 2 43 ? 51.121 20.785 -20.991 1.00 10.80 ? 41 ASP B O 1 ATOM 1953 C CB . ASP B 2 43 ? 48.509 22.204 -21.217 1.00 9.80 ? 41 ASP B CB 1 ATOM 1954 C CG . ASP B 2 43 ? 47.520 21.134 -21.656 1.00 11.77 ? 41 ASP B CG 1 ATOM 1955 O OD1 . ASP B 2 43 ? 47.598 19.970 -21.186 1.00 12.21 ? 41 ASP B OD1 1 ATOM 1956 O OD2 . ASP B 2 43 ? 46.650 21.471 -22.500 1.00 14.80 ? 41 ASP B OD2 1 ATOM 1957 N N . SER B 2 44 ? 49.997 19.567 -19.477 1.00 9.83 ? 42 SER B N 1 ATOM 1958 C CA . SER B 2 44 ? 50.877 18.405 -19.672 1.00 10.67 ? 42 SER B CA 1 ATOM 1959 C C . SER B 2 44 ? 50.839 17.863 -21.105 1.00 11.64 ? 42 SER B C 1 ATOM 1960 O O . SER B 2 44 ? 51.777 17.190 -21.545 1.00 12.46 ? 42 SER B O 1 ATOM 1961 C CB . SER B 2 44 ? 50.566 17.303 -18.656 1.00 10.81 ? 42 SER B CB 1 ATOM 1962 O OG . SER B 2 44 ? 49.246 16.809 -18.820 1.00 11.06 ? 42 SER B OG 1 ATOM 1963 N N . ASP B 2 45 ? 49.772 18.170 -21.842 1.00 11.81 ? 43 ASP B N 1 ATOM 1964 C CA . ASP B 2 45 ? 49.684 17.792 -23.253 1.00 12.73 ? 43 ASP B CA 1 ATOM 1965 C C . ASP B 2 45 ? 50.739 18.525 -24.087 1.00 13.04 ? 43 ASP B C 1 ATOM 1966 O O . ASP B 2 45 ? 51.113 18.064 -25.168 1.00 14.12 ? 43 ASP B O 1 ATOM 1967 C CB . ASP B 2 45 ? 48.304 18.126 -23.823 1.00 18.99 ? 43 ASP B CB 1 ATOM 1968 C CG . ASP B 2 45 ? 47.241 17.103 -23.462 1.00 24.56 ? 43 ASP B CG 1 ATOM 1969 O OD1 . ASP B 2 45 ? 47.511 16.183 -22.666 1.00 22.87 ? 43 ASP B OD1 1 ATOM 1970 O OD2 . ASP B 2 45 ? 46.116 17.231 -23.989 1.00 27.94 ? 43 ASP B OD2 1 ATOM 1971 N N . VAL B 2 46 ? 51.196 19.668 -23.578 1.00 12.20 ? 44 VAL B N 1 ATOM 1972 C CA . VAL B 2 46 ? 52.144 20.537 -24.277 1.00 12.46 ? 44 VAL B CA 1 ATOM 1973 C C . VAL B 2 46 ? 53.545 20.429 -23.678 1.00 14.40 ? 44 VAL B C 1 ATOM 1974 O O . VAL B 2 46 ? 54.524 20.225 -24.390 1.00 13.78 ? 44 VAL B O 1 ATOM 1975 C CB . VAL B 2 46 ? 51.664 22.010 -24.236 1.00 11.86 ? 44 VAL B CB 1 ATOM 1976 C CG1 . VAL B 2 46 ? 52.723 22.947 -24.808 1.00 13.97 ? 44 VAL B CG1 1 ATOM 1977 C CG2 . VAL B 2 46 ? 50.359 22.139 -25.000 1.00 12.75 ? 44 VAL B CG2 1 ATOM 1978 N N . GLY B 2 47 ? 53.648 20.581 -22.364 1.00 11.67 ? 45 GLY B N 1 ATOM 1979 C CA . GLY B 2 47 ? 54.931 20.384 -21.710 1.00 11.86 ? 45 GLY B CA 1 ATOM 1980 C C . GLY B 2 47 ? 55.698 21.669 -21.477 1.00 11.52 ? 45 GLY B C 1 ATOM 1981 O O . GLY B 2 47 ? 56.860 21.630 -21.076 1.00 12.51 ? 45 GLY B O 1 ATOM 1982 N N . GLU B 2 48 ? 55.051 22.803 -21.728 1.00 11.47 ? 46 GLU B N 1 ATOM 1983 C CA . GLU B 2 48 ? 55.634 24.109 -21.423 1.00 11.41 ? 46 GLU B CA 1 ATOM 1984 C C . GLU B 2 48 ? 54.516 25.045 -21.000 1.00 12.49 ? 46 GLU B C 1 ATOM 1985 O O . GLU B 2 48 ? 53.336 24.767 -21.240 1.00 11.20 ? 46 GLU B O 1 ATOM 1986 C CB . GLU B 2 48 ? 56.349 24.690 -22.646 1.00 11.47 ? 46 GLU B CB 1 ATOM 1987 C CG . GLU B 2 48 ? 57.705 24.072 -22.956 1.00 20.40 ? 46 GLU B CG 1 ATOM 1988 C CD . GLU B 2 48 ? 58.403 24.747 -24.130 1.00 34.34 ? 46 GLU B CD 1 ATOM 1989 O OE1 . GLU B 2 48 ? 57.760 25.579 -24.815 1.00 23.27 ? 46 GLU B OE1 1 ATOM 1990 O OE2 . GLU B 2 48 ? 59.595 24.442 -24.367 1.00 31.04 ? 46 GLU B OE2 1 ATOM 1991 N N . TYR B 2 49 ? 54.865 26.145 -20.347 1.00 9.93 ? 47 TYR B N 1 ATOM 1992 C CA . TYR B 2 49 ? 53.862 27.168 -20.071 1.00 8.81 ? 47 TYR B CA 1 ATOM 1993 C C . TYR B 2 49 ? 53.513 27.913 -21.348 1.00 10.07 ? 47 TYR B C 1 ATOM 1994 O O . TYR B 2 49 ? 54.361 28.116 -22.217 1.00 11.53 ? 47 TYR B O 1 ATOM 1995 C CB . TYR B 2 49 ? 54.351 28.153 -18.994 1.00 8.95 ? 47 TYR B CB 1 ATOM 1996 C CG . TYR B 2 49 ? 54.274 27.590 -17.596 1.00 8.33 ? 47 TYR B CG 1 ATOM 1997 C CD1 . TYR B 2 49 ? 55.345 26.900 -17.038 1.00 10.38 ? 47 TYR B CD1 1 ATOM 1998 C CD2 . TYR B 2 49 ? 53.111 27.741 -16.835 1.00 8.91 ? 47 TYR B CD2 1 ATOM 1999 C CE1 . TYR B 2 49 ? 55.268 26.377 -15.752 1.00 10.60 ? 47 TYR B CE1 1 ATOM 2000 C CE2 . TYR B 2 49 ? 53.019 27.220 -15.553 1.00 7.96 ? 47 TYR B CE2 1 ATOM 2001 C CZ . TYR B 2 49 ? 54.099 26.533 -15.023 1.00 11.31 ? 47 TYR B CZ 1 ATOM 2002 O OH . TYR B 2 49 ? 53.994 26.014 -13.756 1.00 11.06 ? 47 TYR B OH 1 ATOM 2003 N N . ARG B 2 50 ? 52.250 28.308 -21.464 1.00 8.84 ? 48 ARG B N 1 ATOM 2004 C CA . ARG B 2 50 ? 51.816 29.142 -22.579 1.00 9.55 ? 48 ARG B CA 1 ATOM 2005 C C . ARG B 2 50 ? 50.959 30.264 -22.043 1.00 12.63 ? 48 ARG B C 1 ATOM 2006 O O . ARG B 2 50 ? 50.104 30.037 -21.191 1.00 11.13 ? 48 ARG B O 1 ATOM 2007 C CB . ARG B 2 50 ? 50.983 28.326 -23.570 1.00 10.67 ? 48 ARG B CB 1 ATOM 2008 C CG . ARG B 2 50 ? 51.744 27.223 -24.280 1.00 12.13 ? 48 ARG B CG 1 ATOM 2009 C CD . ARG B 2 50 ? 52.698 27.776 -25.342 1.00 16.56 ? 48 ARG B CD 1 ATOM 2010 N NE . ARG B 2 50 ? 53.405 26.707 -26.047 1.00 17.94 ? 48 ARG B NE 1 ATOM 2011 C CZ . ARG B 2 50 ? 54.684 26.387 -25.848 1.00 23.09 ? 48 ARG B CZ 1 ATOM 2012 N NH1 . ARG B 2 50 ? 55.412 27.054 -24.961 1.00 24.40 ? 48 ARG B NH1 1 ATOM 2013 N NH2 . ARG B 2 50 ? 55.240 25.394 -26.533 1.00 23.51 ? 48 ARG B NH2 1 ATOM 2014 N N . ALA B 2 51 ? 51.188 31.476 -22.542 1.00 9.16 ? 49 ALA B N 1 ATOM 2015 C CA . ALA B 2 51 ? 50.363 32.611 -22.149 1.00 8.89 ? 49 ALA B CA 1 ATOM 2016 C C . ALA B 2 51 ? 48.943 32.401 -22.664 1.00 11.16 ? 49 ALA B C 1 ATOM 2017 O O . ALA B 2 51 ? 48.737 32.005 -23.820 1.00 13.38 ? 49 ALA B O 1 ATOM 2018 C CB . ALA B 2 51 ? 50.946 33.896 -22.706 1.00 12.95 ? 49 ALA B CB 1 ATOM 2019 N N . VAL B 2 52 ? 47.959 32.666 -21.814 1.00 8.91 ? 50 VAL B N 1 ATOM 2020 C CA . VAL B 2 52 ? 46.567 32.605 -22.249 1.00 11.25 ? 50 VAL B CA 1 ATOM 2021 C C . VAL B 2 52 ? 46.093 33.989 -22.700 1.00 12.70 ? 50 VAL B C 1 ATOM 2022 O O . VAL B 2 52 ? 45.300 34.114 -23.647 1.00 15.91 ? 50 VAL B O 1 ATOM 2023 C CB . VAL B 2 52 ? 45.658 32.032 -21.144 1.00 10.05 ? 50 VAL B CB 1 ATOM 2024 C CG1 . VAL B 2 52 ? 44.200 32.003 -21.612 1.00 12.58 ? 50 VAL B CG1 1 ATOM 2025 C CG2 . VAL B 2 52 ? 46.122 30.633 -20.769 1.00 10.92 ? 50 VAL B CG2 1 ATOM 2026 N N . THR B 2 53 ? 46.604 35.026 -22.040 1.00 8.90 ? 51 THR B N 1 ATOM 2027 C CA . THR B 2 53 ? 46.360 36.409 -22.450 1.00 12.03 ? 51 THR B CA 1 ATOM 2028 C C . THR B 2 53 ? 47.685 37.154 -22.430 1.00 15.43 ? 51 THR B C 1 ATOM 2029 O O . THR B 2 53 ? 48.687 36.626 -21.946 1.00 13.79 ? 51 THR B O 1 ATOM 2030 C CB . THR B 2 53 ? 45.385 37.131 -21.497 1.00 15.64 ? 51 THR B CB 1 ATOM 2031 O OG1 . THR B 2 53 ? 46.004 37.296 -20.215 1.00 15.46 ? 51 THR B OG1 1 ATOM 2032 C CG2 . THR B 2 53 ? 44.092 36.341 -21.337 1.00 12.73 ? 51 THR B CG2 1 ATOM 2033 N N . GLU B 2 54 ? 47.692 38.384 -22.941 1.00 11.50 ? 52 GLU B N 1 ATOM 2034 C CA . GLU B 2 54 ? 48.921 39.169 -22.998 1.00 15.25 ? 52 GLU B CA 1 ATOM 2035 C C . GLU B 2 54 ? 49.535 39.347 -21.614 1.00 14.78 ? 52 GLU B C 1 ATOM 2036 O O . GLU B 2 54 ? 50.759 39.373 -21.466 1.00 15.02 ? 52 GLU B O 1 ATOM 2037 C CB . GLU B 2 54 ? 48.658 40.535 -23.642 1.00 22.06 ? 52 GLU B CB 1 ATOM 2038 C CG . GLU B 2 54 ? 48.047 40.453 -25.024 1.00 41.92 ? 52 GLU B CG 1 ATOM 2039 C CD . GLU B 2 54 ? 48.037 41.787 -25.747 1.00 63.99 ? 52 GLU B CD 1 ATOM 2040 O OE1 . GLU B 2 54 ? 48.299 42.823 -25.098 1.00 68.61 ? 52 GLU B OE1 1 ATOM 2041 O OE2 . GLU B 2 54 ? 47.770 41.796 -26.968 1.00 70.12 ? 52 GLU B OE2 1 ATOM 2042 N N . LEU B 2 55 ? 48.673 39.445 -20.606 1.00 13.61 ? 53 LEU B N 1 ATOM 2043 C CA . LEU B 2 55 ? 49.089 39.583 -19.209 1.00 12.20 ? 53 LEU B CA 1 ATOM 2044 C C . LEU B 2 55 ? 50.044 38.474 -18.758 1.00 13.51 ? 53 LEU B C 1 ATOM 2045 O O . LEU B 2 55 ? 50.867 38.682 -17.863 1.00 14.51 ? 53 LEU B O 1 ATOM 2046 C CB . LEU B 2 55 ? 47.847 39.569 -18.320 1.00 18.72 ? 53 LEU B CB 1 ATOM 2047 C CG . LEU B 2 55 ? 47.776 40.515 -17.124 1.00 27.24 ? 53 LEU B CG 1 ATOM 2048 C CD1 . LEU B 2 55 ? 48.131 41.935 -17.516 1.00 23.74 ? 53 LEU B CD1 1 ATOM 2049 C CD2 . LEU B 2 55 ? 46.391 40.449 -16.485 1.00 24.33 ? 53 LEU B CD2 1 ATOM 2050 N N . GLY B 2 56 ? 49.942 37.303 -19.380 1.00 10.24 ? 54 GLY B N 1 ATOM 2051 C CA . GLY B 2 56 ? 50.745 36.163 -18.963 1.00 11.85 ? 54 GLY B CA 1 ATOM 2052 C C . GLY B 2 56 ? 52.021 35.928 -19.748 1.00 12.31 ? 54 GLY B C 1 ATOM 2053 O O . GLY B 2 56 ? 52.786 35.016 -19.434 1.00 12.62 ? 54 GLY B O 1 ATOM 2054 N N . ARG B 2 57 ? 52.261 36.743 -20.770 1.00 11.25 ? 55 ARG B N 1 ATOM 2055 C CA . ARG B 2 57 ? 53.425 36.532 -21.627 1.00 13.85 ? 55 ARG B CA 1 ATOM 2056 C C . ARG B 2 57 ? 54.765 36.582 -20.885 1.00 12.11 ? 55 ARG B C 1 ATOM 2057 O O . ARG B 2 57 ? 55.628 35.736 -21.130 1.00 13.79 ? 55 ARG B O 1 ATOM 2058 C CB . ARG B 2 57 ? 53.419 37.500 -22.814 1.00 17.01 ? 55 ARG B CB 1 ATOM 2059 C CG . ARG B 2 57 ? 52.272 37.263 -23.779 1.00 23.06 ? 55 ARG B CG 1 ATOM 2060 C CD . ARG B 2 57 ? 52.167 38.375 -24.809 1.00 34.40 ? 55 ARG B CD 1 ATOM 2061 N NE . ARG B 2 57 ? 51.097 38.116 -25.769 1.00 36.67 ? 55 ARG B NE 1 ATOM 2062 C CZ . ARG B 2 57 ? 50.598 39.031 -26.593 1.00 54.62 ? 55 ARG B CZ 1 ATOM 2063 N NH1 . ARG B 2 57 ? 51.060 40.273 -26.564 1.00 61.13 ? 55 ARG B NH1 1 ATOM 2064 N NH2 . ARG B 2 57 ? 49.624 38.709 -27.435 1.00 57.27 ? 55 ARG B NH2 1 ATOM 2065 N N . PRO B 2 58 ? 54.943 37.559 -19.974 1.00 12.86 ? 56 PRO B N 1 ATOM 2066 C CA . PRO B 2 58 ? 56.243 37.586 -19.301 1.00 11.62 ? 56 PRO B CA 1 ATOM 2067 C C . PRO B 2 58 ? 56.501 36.341 -18.470 1.00 10.26 ? 56 PRO B C 1 ATOM 2068 O O . PRO B 2 58 ? 57.627 35.844 -18.450 1.00 13.54 ? 56 PRO B O 1 ATOM 2069 C CB . PRO B 2 58 ? 56.136 38.817 -18.393 1.00 17.39 ? 56 PRO B CB 1 ATOM 2070 C CG . PRO B 2 58 ? 55.161 39.699 -19.084 1.00 15.78 ? 56 PRO B CG 1 ATOM 2071 C CD . PRO B 2 58 ? 54.143 38.757 -19.646 1.00 14.14 ? 56 PRO B CD 1 ATOM 2072 N N . ASP B 2 59 ? 55.471 35.837 -17.801 1.00 11.63 ? 57 ASP B N 1 ATOM 2073 C CA . ASP B 2 59 ? 55.632 34.640 -16.979 1.00 12.82 ? 57 ASP B CA 1 ATOM 2074 C C . ASP B 2 59 ? 55.883 33.389 -17.801 1.00 10.92 ? 57 ASP B C 1 ATOM 2075 O O . ASP B 2 59 ? 56.720 32.568 -17.431 1.00 10.06 ? 57 ASP B O 1 ATOM 2076 C CB . ASP B 2 59 ? 54.414 34.451 -16.071 1.00 12.40 ? 57 ASP B CB 1 ATOM 2077 C CG . ASP B 2 59 ? 54.312 35.531 -15.028 1.00 17.67 ? 57 ASP B CG 1 ATOM 2078 O OD1 . ASP B 2 59 ? 55.366 36.012 -14.576 1.00 16.63 ? 57 ASP B OD1 1 ATOM 2079 O OD2 . ASP B 2 59 ? 53.189 35.915 -14.666 1.00 13.58 ? 57 ASP B OD2 1 ATOM 2080 N N . ALA B 2 60 ? 55.168 33.229 -18.910 1.00 9.31 ? 58 ALA B N 1 ATOM 2081 C CA . ALA B 2 60 ? 55.423 32.082 -19.773 1.00 11.16 ? 58 ALA B CA 1 ATOM 2082 C C . ALA B 2 60 ? 56.886 32.033 -20.210 1.00 10.89 ? 58 ALA B C 1 ATOM 2083 O O . ALA B 2 60 ? 57.529 30.986 -20.131 1.00 13.20 ? 58 ALA B O 1 ATOM 2084 C CB . ALA B 2 60 ? 54.499 32.093 -20.993 1.00 14.32 ? 58 ALA B CB 1 ATOM 2085 N N . GLU B 2 61 ? 57.433 33.159 -20.656 1.00 10.72 ? 59 GLU B N 1 ATOM 2086 C CA A GLU B 2 61 ? 58.823 33.181 -21.103 0.60 11.67 ? 59 GLU B CA 1 ATOM 2087 C CA B GLU B 2 61 ? 58.819 33.147 -21.114 0.40 15.86 ? 59 GLU B CA 1 ATOM 2088 C C . GLU B 2 61 ? 59.798 32.921 -19.962 1.00 15.01 ? 59 GLU B C 1 ATOM 2089 O O . GLU B 2 61 ? 60.762 32.178 -20.113 1.00 15.06 ? 59 GLU B O 1 ATOM 2090 C CB A GLU B 2 61 ? 59.150 34.507 -21.791 0.60 17.64 ? 59 GLU B CB 1 ATOM 2091 C CB B GLU B 2 61 ? 59.171 34.403 -21.924 0.40 20.74 ? 59 GLU B CB 1 ATOM 2092 C CG A GLU B 2 61 ? 58.510 34.631 -23.161 0.60 28.19 ? 59 GLU B CG 1 ATOM 2093 C CG B GLU B 2 61 ? 58.776 35.709 -21.279 0.40 23.65 ? 59 GLU B CG 1 ATOM 2094 C CD A GLU B 2 61 ? 58.870 35.916 -23.873 0.60 36.07 ? 59 GLU B CD 1 ATOM 2095 C CD B GLU B 2 61 ? 59.098 36.919 -22.139 0.40 33.35 ? 59 GLU B CD 1 ATOM 2096 O OE1 A GLU B 2 61 ? 59.979 36.444 -23.635 0.60 39.58 ? 59 GLU B OE1 1 ATOM 2097 O OE1 B GLU B 2 61 ? 59.899 37.772 -21.695 0.40 31.31 ? 59 GLU B OE1 1 ATOM 2098 O OE2 A GLU B 2 61 ? 58.037 36.396 -24.670 0.60 32.70 ? 59 GLU B OE2 1 ATOM 2099 O OE2 B GLU B 2 61 ? 58.542 37.024 -23.253 0.40 34.69 ? 59 GLU B OE2 1 ATOM 2100 N N . TYR B 2 62 ? 59.544 33.545 -18.816 1.00 12.10 ? 60 TYR B N 1 ATOM 2101 C CA . TYR B 2 62 ? 60.436 33.399 -17.664 1.00 12.26 ? 60 TYR B CA 1 ATOM 2102 C C . TYR B 2 62 ? 60.412 31.970 -17.134 1.00 13.67 ? 60 TYR B C 1 ATOM 2103 O O . TYR B 2 62 ? 61.455 31.360 -16.905 1.00 15.55 ? 60 TYR B O 1 ATOM 2104 C CB . TYR B 2 62 ? 60.046 34.396 -16.567 1.00 16.90 ? 60 TYR B CB 1 ATOM 2105 C CG . TYR B 2 62 ? 60.882 34.328 -15.303 1.00 15.67 ? 60 TYR B CG 1 ATOM 2106 C CD1 . TYR B 2 62 ? 62.265 34.370 -15.357 1.00 20.02 ? 60 TYR B CD1 1 ATOM 2107 C CD2 . TYR B 2 62 ? 60.276 34.256 -14.052 1.00 14.59 ? 60 TYR B CD2 1 ATOM 2108 C CE1 . TYR B 2 62 ? 63.031 34.324 -14.202 1.00 25.96 ? 60 TYR B CE1 1 ATOM 2109 C CE2 . TYR B 2 62 ? 61.031 34.218 -12.889 1.00 18.87 ? 60 TYR B CE2 1 ATOM 2110 C CZ . TYR B 2 62 ? 62.408 34.247 -12.974 1.00 24.40 ? 60 TYR B CZ 1 ATOM 2111 O OH . TYR B 2 62 ? 63.166 34.203 -11.827 1.00 28.77 ? 60 TYR B OH 1 ATOM 2112 N N . TRP B 2 63 ? 59.218 31.430 -16.953 1.00 11.32 ? 61 TRP B N 1 ATOM 2113 C CA . TRP B 2 63 ? 59.100 30.092 -16.400 1.00 10.19 ? 61 TRP B CA 1 ATOM 2114 C C . TRP B 2 63 ? 59.652 29.033 -17.354 1.00 10.83 ? 61 TRP B C 1 ATOM 2115 O O . TRP B 2 63 ? 60.279 28.058 -16.917 1.00 11.80 ? 61 TRP B O 1 ATOM 2116 C CB . TRP B 2 63 ? 57.644 29.819 -16.029 1.00 9.56 ? 61 TRP B CB 1 ATOM 2117 C CG . TRP B 2 63 ? 57.175 30.718 -14.923 1.00 8.91 ? 61 TRP B CG 1 ATOM 2118 C CD1 . TRP B 2 63 ? 57.941 31.538 -14.139 1.00 11.70 ? 61 TRP B CD1 1 ATOM 2119 C CD2 . TRP B 2 63 ? 55.823 30.906 -14.502 1.00 8.18 ? 61 TRP B CD2 1 ATOM 2120 N NE1 . TRP B 2 63 ? 57.140 32.220 -13.244 1.00 12.15 ? 61 TRP B NE1 1 ATOM 2121 C CE2 . TRP B 2 63 ? 55.838 31.835 -13.442 1.00 11.29 ? 61 TRP B CE2 1 ATOM 2122 C CE3 . TRP B 2 63 ? 54.602 30.358 -14.906 1.00 9.78 ? 61 TRP B CE3 1 ATOM 2123 C CZ2 . TRP B 2 63 ? 54.674 32.243 -12.795 1.00 8.69 ? 61 TRP B CZ2 1 ATOM 2124 C CZ3 . TRP B 2 63 ? 53.446 30.772 -14.258 1.00 8.27 ? 61 TRP B CZ3 1 ATOM 2125 C CH2 . TRP B 2 63 ? 53.495 31.683 -13.207 1.00 9.24 ? 61 TRP B CH2 1 ATOM 2126 N N . ASN B 2 64 ? 59.454 29.238 -18.654 1.00 11.65 ? 62 ASN B N 1 ATOM 2127 C CA . ASN B 2 64 ? 59.960 28.295 -19.649 1.00 11.56 ? 62 ASN B CA 1 ATOM 2128 C C . ASN B 2 64 ? 61.483 28.312 -19.736 1.00 12.61 ? 62 ASN B C 1 ATOM 2129 O O . ASN B 2 64 ? 62.091 27.391 -20.280 1.00 14.57 ? 62 ASN B O 1 ATOM 2130 C CB . ASN B 2 64 ? 59.352 28.550 -21.032 1.00 11.69 ? 62 ASN B CB 1 ATOM 2131 C CG . ASN B 2 64 ? 57.907 28.080 -21.126 1.00 14.72 ? 62 ASN B CG 1 ATOM 2132 O OD1 . ASN B 2 64 ? 57.448 27.288 -20.301 1.00 12.06 ? 62 ASN B OD1 1 ATOM 2133 N ND2 . ASN B 2 64 ? 57.191 28.561 -22.135 1.00 12.18 ? 62 ASN B ND2 1 ATOM 2134 N N . SER B 2 65 ? 62.098 29.358 -19.192 1.00 12.85 ? 63 SER B N 1 ATOM 2135 C CA . SER B 2 65 ? 63.560 29.437 -19.174 1.00 13.97 ? 63 SER B CA 1 ATOM 2136 C C . SER B 2 65 ? 64.160 28.637 -18.022 1.00 16.60 ? 63 SER B C 1 ATOM 2137 O O . SER B 2 65 ? 65.386 28.502 -17.921 1.00 18.81 ? 63 SER B O 1 ATOM 2138 C CB . SER B 2 65 ? 64.038 30.892 -19.090 1.00 14.85 ? 63 SER B CB 1 ATOM 2139 O OG . SER B 2 65 ? 63.919 31.399 -17.771 1.00 15.06 ? 63 SER B OG 1 ATOM 2140 N N . GLN B 2 66 ? 63.296 28.108 -17.158 1.00 13.76 ? 64 GLN B N 1 ATOM 2141 C CA . GLN B 2 66 ? 63.748 27.352 -15.996 1.00 13.63 ? 64 GLN B CA 1 ATOM 2142 C C . GLN B 2 66 ? 63.561 25.857 -16.228 1.00 13.69 ? 64 GLN B C 1 ATOM 2143 O O . GLN B 2 66 ? 62.480 25.320 -16.000 1.00 14.01 ? 64 GLN B O 1 ATOM 2144 C CB . GLN B 2 66 ? 62.992 27.805 -14.749 1.00 15.05 ? 64 GLN B CB 1 ATOM 2145 C CG . GLN B 2 66 ? 63.109 29.311 -14.467 1.00 12.91 ? 64 GLN B CG 1 ATOM 2146 C CD . GLN B 2 66 ? 62.270 29.724 -13.277 1.00 18.26 ? 64 GLN B CD 1 ATOM 2147 O OE1 . GLN B 2 66 ? 62.153 28.981 -12.299 1.00 19.83 ? 64 GLN B OE1 1 ATOM 2148 N NE2 . GLN B 2 66 ? 61.662 30.903 -13.358 1.00 17.52 ? 64 GLN B NE2 1 ATOM 2149 N N . LYS B 2 67 ? 64.624 25.197 -16.692 1.00 17.43 ? 65 LYS B N 1 ATOM 2150 C CA . LYS B 2 67 ? 64.541 23.786 -17.059 1.00 21.52 ? 65 LYS B CA 1 ATOM 2151 C C . LYS B 2 67 ? 64.130 22.907 -15.883 1.00 17.30 ? 65 LYS B C 1 ATOM 2152 O O . LYS B 2 67 ? 63.391 21.937 -16.054 1.00 16.70 ? 65 LYS B O 1 ATOM 2153 C CB . LYS B 2 67 ? 65.864 23.299 -17.666 1.00 18.57 ? 65 LYS B CB 1 ATOM 2154 C CG . LYS B 2 67 ? 67.058 23.386 -16.725 1.00 32.10 ? 65 LYS B CG 1 ATOM 2155 C CD . LYS B 2 67 ? 68.370 23.204 -17.472 1.00 33.36 ? 65 LYS B CD 1 ATOM 2156 C CE . LYS B 2 67 ? 69.567 23.457 -16.567 1.00 34.07 ? 65 LYS B CE 1 ATOM 2157 N NZ . LYS B 2 67 ? 70.853 23.355 -17.312 1.00 32.74 ? 65 LYS B NZ 1 ATOM 2158 N N . ASP B 2 68 ? 64.602 23.248 -14.689 1.00 17.31 ? 66 ASP B N 1 ATOM 2159 C CA . ASP B 2 68 ? 64.252 22.486 -13.499 1.00 18.40 ? 66 ASP B CA 1 ATOM 2160 C C . ASP B 2 68 ? 62.758 22.555 -13.208 1.00 15.18 ? 66 ASP B C 1 ATOM 2161 O O . ASP B 2 68 ? 62.129 21.532 -12.902 1.00 15.37 ? 66 ASP B O 1 ATOM 2162 C CB . ASP B 2 68 ? 65.083 22.931 -12.285 1.00 23.37 ? 66 ASP B CB 1 ATOM 2163 C CG . ASP B 2 68 ? 65.012 24.432 -12.026 1.00 27.39 ? 66 ASP B CG 1 ATOM 2164 O OD1 . ASP B 2 68 ? 64.692 25.210 -12.953 1.00 22.74 ? 66 ASP B OD1 1 ATOM 2165 O OD2 . ASP B 2 68 ? 65.305 24.833 -10.879 1.00 31.02 ? 66 ASP B OD2 1 ATOM 2166 N N . LEU B 2 69 ? 62.199 23.760 -13.315 1.00 13.05 ? 67 LEU B N 1 ATOM 2167 C CA . LEU B 2 69 ? 60.775 23.972 -13.132 1.00 11.80 ? 67 LEU B CA 1 ATOM 2168 C C . LEU B 2 69 ? 59.982 23.186 -14.162 1.00 11.82 ? 67 LEU B C 1 ATOM 2169 O O . LEU B 2 69 ? 59.009 22.516 -13.821 1.00 11.58 ? 67 LEU B O 1 ATOM 2170 C CB . LEU B 2 69 ? 60.436 25.464 -13.247 1.00 11.23 ? 67 LEU B CB 1 ATOM 2171 C CG . LEU B 2 69 ? 58.935 25.768 -13.339 1.00 10.16 ? 67 LEU B CG 1 ATOM 2172 C CD1 . LEU B 2 69 ? 58.223 25.412 -12.036 1.00 18.11 ? 67 LEU B CD1 1 ATOM 2173 C CD2 . LEU B 2 69 ? 58.735 27.239 -13.651 1.00 12.38 ? 67 LEU B CD2 1 ATOM 2174 N N . LEU B 2 70 ? 60.398 23.253 -15.424 1.00 11.81 ? 68 LEU B N 1 ATOM 2175 C CA . LEU B 2 70 ? 59.676 22.522 -16.470 1.00 11.94 ? 68 LEU B CA 1 ATOM 2176 C C . LEU B 2 70 ? 59.722 21.012 -16.240 1.00 12.24 ? 68 LEU B C 1 ATOM 2177 O O . LEU B 2 70 ? 58.722 20.310 -16.425 1.00 12.23 ? 68 LEU B O 1 ATOM 2178 C CB . LEU B 2 70 ? 60.205 22.865 -17.863 1.00 12.76 ? 68 LEU B CB 1 ATOM 2179 C CG . LEU B 2 70 ? 59.886 24.269 -18.393 1.00 11.75 ? 68 LEU B CG 1 ATOM 2180 C CD1 . LEU B 2 70 ? 60.407 24.393 -19.811 1.00 18.39 ? 68 LEU B CD1 1 ATOM 2181 C CD2 . LEU B 2 70 ? 58.387 24.554 -18.337 1.00 13.98 ? 68 LEU B CD2 1 ATOM 2182 N N . GLU B 2 71 ? 60.868 20.492 -15.820 1.00 13.16 ? 69 GLU B N 1 ATOM 2183 C CA . GLU B 2 71 ? 60.916 19.055 -15.567 1.00 13.81 ? 69 GLU B CA 1 ATOM 2184 C C . GLU B 2 71 ? 60.056 18.640 -14.366 1.00 13.33 ? 69 GLU B C 1 ATOM 2185 O O . GLU B 2 71 ? 59.479 17.549 -14.363 1.00 14.03 ? 69 GLU B O 1 ATOM 2186 C CB . GLU B 2 71 ? 62.358 18.556 -15.472 1.00 19.77 ? 69 GLU B CB 1 ATOM 2187 C CG . GLU B 2 71 ? 63.099 18.631 -16.811 1.00 21.77 ? 69 GLU B CG 1 ATOM 2188 C CD . GLU B 2 71 ? 62.451 17.815 -17.945 1.00 24.41 ? 69 GLU B CD 1 ATOM 2189 O OE1 . GLU B 2 71 ? 61.673 16.878 -17.679 1.00 26.93 ? 69 GLU B OE1 1 ATOM 2190 O OE2 . GLU B 2 71 ? 62.731 18.119 -19.124 1.00 23.77 ? 69 GLU B OE2 1 ATOM 2191 N N . GLN B 2 72 ? 59.931 19.518 -13.373 1.00 12.79 ? 70 GLN B N 1 ATOM 2192 C CA A GLN B 2 72 ? 59.012 19.266 -12.264 0.58 14.44 ? 70 GLN B CA 1 ATOM 2193 C CA B GLN B 2 72 ? 59.019 19.274 -12.262 0.42 14.80 ? 70 GLN B CA 1 ATOM 2194 C C . GLN B 2 72 ? 57.586 19.156 -12.779 1.00 11.50 ? 70 GLN B C 1 ATOM 2195 O O . GLN B 2 72 ? 56.862 18.218 -12.447 1.00 13.07 ? 70 GLN B O 1 ATOM 2196 C CB A GLN B 2 72 ? 59.090 20.378 -11.213 0.58 14.41 ? 70 GLN B CB 1 ATOM 2197 C CB B GLN B 2 72 ? 59.113 20.418 -11.250 0.42 14.99 ? 70 GLN B CB 1 ATOM 2198 C CG A GLN B 2 72 ? 60.266 20.263 -10.274 0.58 15.98 ? 70 GLN B CG 1 ATOM 2199 C CG B GLN B 2 72 ? 58.344 20.186 -9.966 0.42 14.46 ? 70 GLN B CG 1 ATOM 2200 C CD A GLN B 2 72 ? 60.247 18.969 -9.476 0.58 21.12 ? 70 GLN B CD 1 ATOM 2201 C CD B GLN B 2 72 ? 59.055 19.231 -9.023 0.42 25.87 ? 70 GLN B CD 1 ATOM 2202 O OE1 A GLN B 2 72 ? 59.202 18.536 -8.996 0.58 25.28 ? 70 GLN B OE1 1 ATOM 2203 O OE1 B GLN B 2 72 ? 58.872 18.016 -9.094 0.42 29.50 ? 70 GLN B OE1 1 ATOM 2204 N NE2 A GLN B 2 72 ? 61.407 18.343 -9.341 0.58 21.88 ? 70 GLN B NE2 1 ATOM 2205 N NE2 B GLN B 2 72 ? 59.871 19.781 -8.132 0.42 29.61 ? 70 GLN B NE2 1 ATOM 2206 N N . ARG B 2 73 ? 57.185 20.123 -13.594 1.00 10.84 ? 71 ARG B N 1 ATOM 2207 C CA . ARG B 2 73 ? 55.831 20.155 -14.121 1.00 11.11 ? 71 ARG B CA 1 ATOM 2208 C C . ARG B 2 73 ? 55.560 18.989 -15.068 1.00 10.66 ? 71 ARG B C 1 ATOM 2209 O O . ARG B 2 73 ? 54.460 18.446 -15.074 1.00 12.36 ? 71 ARG B O 1 ATOM 2210 C CB . ARG B 2 73 ? 55.561 21.495 -14.806 1.00 11.39 ? 71 ARG B CB 1 ATOM 2211 C CG . ARG B 2 73 ? 55.617 22.703 -13.865 1.00 9.47 ? 71 ARG B CG 1 ATOM 2212 C CD . ARG B 2 73 ? 54.539 22.609 -12.782 1.00 13.94 ? 71 ARG B CD 1 ATOM 2213 N NE . ARG B 2 73 ? 54.602 23.755 -11.870 1.00 18.76 ? 71 ARG B NE 1 ATOM 2214 C CZ . ARG B 2 73 ? 55.190 23.741 -10.676 1.00 16.56 ? 71 ARG B CZ 1 ATOM 2215 N NH1 . ARG B 2 73 ? 55.760 22.638 -10.217 1.00 18.01 ? 71 ARG B NH1 1 ATOM 2216 N NH2 . ARG B 2 73 ? 55.197 24.833 -9.931 1.00 25.65 ? 71 ARG B NH2 1 ATOM 2217 N N . ARG B 2 74 ? 56.560 18.594 -15.855 1.00 11.46 ? 72 ARG B N 1 ATOM 2218 C CA . ARG B 2 74 ? 56.396 17.467 -16.773 1.00 12.16 ? 72 ARG B CA 1 ATOM 2219 C C . ARG B 2 74 ? 56.225 16.150 -16.036 1.00 12.72 ? 72 ARG B C 1 ATOM 2220 O O . ARG B 2 74 ? 55.661 15.192 -16.580 1.00 13.60 ? 72 ARG B O 1 ATOM 2221 C CB . ARG B 2 74 ? 57.603 17.369 -17.723 1.00 13.07 ? 72 ARG B CB 1 ATOM 2222 C CG . ARG B 2 74 ? 57.600 18.460 -18.780 1.00 12.78 ? 72 ARG B CG 1 ATOM 2223 C CD . ARG B 2 74 ? 58.944 18.615 -19.482 1.00 16.08 ? 72 ARG B CD 1 ATOM 2224 N NE . ARG B 2 74 ? 58.910 19.796 -20.332 1.00 15.97 ? 72 ARG B NE 1 ATOM 2225 C CZ . ARG B 2 74 ? 59.953 20.268 -21.001 1.00 15.40 ? 72 ARG B CZ 1 ATOM 2226 N NH1 . ARG B 2 74 ? 61.129 19.658 -20.918 1.00 17.95 ? 72 ARG B NH1 1 ATOM 2227 N NH2 . ARG B 2 74 ? 59.823 21.354 -21.749 1.00 20.35 ? 72 ARG B NH2 1 ATOM 2228 N N . ALA B 2 75 ? 56.730 16.086 -14.808 1.00 12.83 ? 73 ALA B N 1 ATOM 2229 C CA . ALA B 2 75 ? 56.620 14.862 -14.019 1.00 13.50 ? 73 ALA B CA 1 ATOM 2230 C C . ALA B 2 75 ? 55.366 14.829 -13.154 1.00 12.87 ? 73 ALA B C 1 ATOM 2231 O O . ALA B 2 75 ? 55.056 13.800 -12.548 1.00 15.49 ? 73 ALA B O 1 ATOM 2232 C CB . ALA B 2 75 ? 57.855 14.685 -13.150 1.00 14.26 ? 73 ALA B CB 1 ATOM 2233 N N . ALA B 2 76 ? 54.653 15.952 -13.106 1.00 13.47 ? 74 ALA B N 1 ATOM 2234 C CA . ALA B 2 76 ? 53.540 16.121 -12.177 1.00 11.23 ? 74 ALA B CA 1 ATOM 2235 C C . ALA B 2 76 ? 52.439 15.084 -12.350 1.00 11.50 ? 74 ALA B C 1 ATOM 2236 O O . ALA B 2 76 ? 51.832 14.660 -11.364 1.00 12.37 ? 74 ALA B O 1 ATOM 2237 C CB . ALA B 2 76 ? 52.956 17.541 -12.274 1.00 10.35 ? 74 ALA B CB 1 ATOM 2238 N N . VAL B 2 77 ? 52.175 14.665 -13.587 1.00 11.78 ? 75 VAL B N 1 ATOM 2239 C CA . VAL B 2 77 ? 51.134 13.651 -13.800 1.00 12.21 ? 75 VAL B CA 1 ATOM 2240 C C . VAL B 2 77 ? 51.407 12.412 -12.969 1.00 13.40 ? 75 VAL B C 1 ATOM 2241 O O . VAL B 2 77 ? 50.477 11.733 -12.535 1.00 13.46 ? 75 VAL B O 1 ATOM 2242 C CB . VAL B 2 77 ? 50.951 13.244 -15.284 1.00 13.51 ? 75 VAL B CB 1 ATOM 2243 C CG1 . VAL B 2 77 ? 50.228 14.350 -16.057 1.00 11.87 ? 75 VAL B CG1 1 ATOM 2244 C CG2 . VAL B 2 77 ? 52.286 12.886 -15.934 1.00 13.46 ? 75 VAL B CG2 1 ATOM 2245 N N . ASP B 2 78 ? 52.688 12.119 -12.746 1.00 13.96 ? 76 ASP B N 1 ATOM 2246 C CA . ASP B 2 78 ? 53.079 10.989 -11.913 1.00 15.08 ? 76 ASP B CA 1 ATOM 2247 C C . ASP B 2 78 ? 53.261 11.334 -10.435 1.00 14.91 ? 76 ASP B C 1 ATOM 2248 O O . ASP B 2 78 ? 52.679 10.686 -9.558 1.00 17.51 ? 76 ASP B O 1 ATOM 2249 C CB . ASP B 2 78 ? 54.392 10.391 -12.425 1.00 15.93 ? 76 ASP B CB 1 ATOM 2250 C CG . ASP B 2 78 ? 54.260 9.763 -13.797 1.00 25.01 ? 76 ASP B CG 1 ATOM 2251 O OD1 . ASP B 2 78 ? 53.164 9.270 -14.139 1.00 20.69 ? 76 ASP B OD1 1 ATOM 2252 O OD2 . ASP B 2 78 ? 55.267 9.752 -14.531 1.00 22.69 ? 76 ASP B OD2 1 ATOM 2253 N N . THR B 2 79 ? 54.102 12.329 -10.163 1.00 14.30 ? 77 THR B N 1 ATOM 2254 C CA . THR B 2 79 ? 54.536 12.621 -8.801 1.00 14.48 ? 77 THR B CA 1 ATOM 2255 C C . THR B 2 79 ? 53.497 13.385 -8.000 1.00 13.62 ? 77 THR B C 1 ATOM 2256 O O . THR B 2 79 ? 53.578 13.454 -6.777 1.00 16.26 ? 77 THR B O 1 ATOM 2257 C CB . THR B 2 79 ? 55.826 13.457 -8.795 1.00 15.60 ? 77 THR B CB 1 ATOM 2258 O OG1 . THR B 2 79 ? 55.563 14.720 -9.411 1.00 17.43 ? 77 THR B OG1 1 ATOM 2259 C CG2 . THR B 2 79 ? 56.947 12.744 -9.554 1.00 17.10 ? 77 THR B CG2 1 ATOM 2260 N N . TYR B 2 80 ? 52.523 13.960 -8.695 1.00 12.66 ? 78 TYR B N 1 ATOM 2261 C CA . TYR B 2 80 ? 51.511 14.791 -8.052 1.00 12.44 ? 78 TYR B CA 1 ATOM 2262 C C . TYR B 2 80 ? 50.126 14.185 -8.277 1.00 14.24 ? 78 TYR B C 1 ATOM 2263 O O . TYR B 2 80 ? 49.470 13.748 -7.332 1.00 13.58 ? 78 TYR B O 1 ATOM 2264 C CB . TYR B 2 80 ? 51.600 16.210 -8.609 1.00 11.40 ? 78 TYR B CB 1 ATOM 2265 C CG . TYR B 2 80 ? 50.540 17.184 -8.120 1.00 10.04 ? 78 TYR B CG 1 ATOM 2266 C CD1 . TYR B 2 80 ? 50.454 17.541 -6.782 1.00 10.65 ? 78 TYR B CD1 1 ATOM 2267 C CD2 . TYR B 2 80 ? 49.678 17.794 -9.019 1.00 9.46 ? 78 TYR B CD2 1 ATOM 2268 C CE1 . TYR B 2 80 ? 49.499 18.462 -6.346 1.00 10.29 ? 78 TYR B CE1 1 ATOM 2269 C CE2 . TYR B 2 80 ? 48.712 18.705 -8.596 1.00 9.00 ? 78 TYR B CE2 1 ATOM 2270 C CZ . TYR B 2 80 ? 48.638 19.037 -7.263 1.00 8.79 ? 78 TYR B CZ 1 ATOM 2271 O OH . TYR B 2 80 ? 47.695 19.954 -6.852 1.00 10.05 ? 78 TYR B OH 1 ATOM 2272 N N . CYS B 2 81 ? 49.703 14.125 -9.531 1.00 11.69 ? 79 CYS B N 1 ATOM 2273 C CA . CYS B 2 81 ? 48.374 13.607 -9.847 1.00 11.62 ? 79 CYS B CA 1 ATOM 2274 C C . CYS B 2 81 ? 48.166 12.135 -9.485 1.00 13.99 ? 79 CYS B C 1 ATOM 2275 O O . CYS B 2 81 ? 47.268 11.800 -8.710 1.00 14.84 ? 79 CYS B O 1 ATOM 2276 C CB . CYS B 2 81 ? 48.041 13.831 -11.320 1.00 13.62 ? 79 CYS B CB 1 ATOM 2277 S SG . CYS B 2 81 ? 48.089 15.560 -11.819 1.00 12.83 ? 79 CYS B SG 1 ATOM 2278 N N . ARG B 2 82 ? 48.970 11.251 -10.058 1.00 13.59 ? 80 ARG B N 1 ATOM 2279 C CA . ARG B 2 82 ? 48.793 9.832 -9.766 1.00 14.85 ? 80 ARG B CA 1 ATOM 2280 C C . ARG B 2 82 ? 49.034 9.552 -8.295 1.00 15.36 ? 80 ARG B C 1 ATOM 2281 O O . ARG B 2 82 ? 48.331 8.736 -7.689 1.00 17.28 ? 80 ARG B O 1 ATOM 2282 C CB . ARG B 2 82 ? 49.689 8.973 -10.650 1.00 15.77 ? 80 ARG B CB 1 ATOM 2283 C CG . ARG B 2 82 ? 49.161 8.853 -12.067 1.00 17.10 ? 80 ARG B CG 1 ATOM 2284 C CD . ARG B 2 82 ? 50.059 7.979 -12.930 1.00 18.04 ? 80 ARG B CD 1 ATOM 2285 N NE . ARG B 2 82 ? 49.426 7.702 -14.216 1.00 21.00 ? 80 ARG B NE 1 ATOM 2286 C CZ . ARG B 2 82 ? 49.621 8.404 -15.328 1.00 18.84 ? 80 ARG B CZ 1 ATOM 2287 N NH1 . ARG B 2 82 ? 48.983 8.059 -16.436 1.00 22.07 ? 80 ARG B NH1 1 ATOM 2288 N NH2 . ARG B 2 82 ? 50.453 9.444 -15.346 1.00 17.43 ? 80 ARG B NH2 1 ATOM 2289 N N . HIS B 2 83 ? 50.020 10.232 -7.712 1.00 15.82 ? 81 HIS B N 1 ATOM 2290 C CA . HIS B 2 83 ? 50.287 10.061 -6.284 1.00 15.82 ? 81 HIS B CA 1 ATOM 2291 C C . HIS B 2 83 ? 49.078 10.412 -5.422 1.00 15.35 ? 81 HIS B C 1 ATOM 2292 O O . HIS B 2 83 ? 48.656 9.614 -4.576 1.00 16.87 ? 81 HIS B O 1 ATOM 2293 C CB . HIS B 2 83 ? 51.487 10.890 -5.808 1.00 15.50 ? 81 HIS B CB 1 ATOM 2294 C CG . HIS B 2 83 ? 51.720 10.785 -4.330 1.00 16.25 ? 81 HIS B CG 1 ATOM 2295 N ND1 . HIS B 2 83 ? 52.516 9.807 -3.772 1.00 17.67 ? 81 HIS B ND1 1 ATOM 2296 C CD2 . HIS B 2 83 ? 51.217 11.500 -3.296 1.00 15.93 ? 81 HIS B CD2 1 ATOM 2297 C CE1 . HIS B 2 83 ? 52.514 9.944 -2.456 1.00 22.82 ? 81 HIS B CE1 1 ATOM 2298 N NE2 . HIS B 2 83 ? 51.735 10.961 -2.141 1.00 19.51 ? 81 HIS B NE2 1 ATOM 2299 N N . ASN B 2 84 ? 48.530 11.605 -5.626 1.00 14.13 ? 82 ASN B N 1 ATOM 2300 C CA . ASN B 2 84 ? 47.433 12.067 -4.796 1.00 13.84 ? 82 ASN B CA 1 ATOM 2301 C C . ASN B 2 84 ? 46.174 11.249 -5.026 1.00 14.25 ? 82 ASN B C 1 ATOM 2302 O O . ASN B 2 84 ? 45.403 11.034 -4.101 1.00 14.70 ? 82 ASN B O 1 ATOM 2303 C CB . ASN B 2 84 ? 47.180 13.560 -5.007 1.00 12.56 ? 82 ASN B CB 1 ATOM 2304 C CG . ASN B 2 84 ? 48.221 14.421 -4.314 1.00 12.40 ? 82 ASN B CG 1 ATOM 2305 O OD1 . ASN B 2 84 ? 48.932 13.945 -3.426 1.00 15.82 ? 82 ASN B OD1 1 ATOM 2306 N ND2 . ASN B 2 84 ? 48.315 15.690 -4.714 1.00 13.68 ? 82 ASN B ND2 1 ATOM 2307 N N . TYR B 2 85 ? 45.989 10.770 -6.251 1.00 16.98 ? 83 TYR B N 1 ATOM 2308 C CA . TYR B 2 85 ? 44.851 9.905 -6.549 1.00 14.89 ? 83 TYR B CA 1 ATOM 2309 C C . TYR B 2 85 ? 44.947 8.665 -5.666 1.00 16.30 ? 83 TYR B C 1 ATOM 2310 O O . TYR B 2 85 ? 43.969 8.250 -5.054 1.00 17.13 ? 83 TYR B O 1 ATOM 2311 C CB . TYR B 2 85 ? 44.854 9.503 -8.027 1.00 14.96 ? 83 TYR B CB 1 ATOM 2312 C CG . TYR B 2 85 ? 43.616 8.754 -8.511 1.00 16.91 ? 83 TYR B CG 1 ATOM 2313 C CD1 . TYR B 2 85 ? 42.589 9.426 -9.169 1.00 18.85 ? 83 TYR B CD1 1 ATOM 2314 C CD2 . TYR B 2 85 ? 43.492 7.383 -8.335 1.00 19.62 ? 83 TYR B CD2 1 ATOM 2315 C CE1 . TYR B 2 85 ? 41.474 8.753 -9.630 1.00 19.66 ? 83 TYR B CE1 1 ATOM 2316 C CE2 . TYR B 2 85 ? 42.380 6.704 -8.792 1.00 22.38 ? 83 TYR B CE2 1 ATOM 2317 C CZ . TYR B 2 85 ? 41.376 7.391 -9.437 1.00 22.83 ? 83 TYR B CZ 1 ATOM 2318 O OH . TYR B 2 85 ? 40.271 6.698 -9.892 1.00 25.64 ? 83 TYR B OH 1 ATOM 2319 N N . GLY B 2 86 ? 46.141 8.089 -5.588 1.00 18.00 ? 84 GLY B N 1 ATOM 2320 C CA . GLY B 2 86 ? 46.347 6.910 -4.768 1.00 18.48 ? 84 GLY B CA 1 ATOM 2321 C C . GLY B 2 86 ? 46.049 7.171 -3.305 1.00 18.75 ? 84 GLY B C 1 ATOM 2322 O O . GLY B 2 86 ? 45.503 6.314 -2.610 1.00 21.87 ? 84 GLY B O 1 ATOM 2323 N N . VAL B 2 87 ? 46.385 8.368 -2.840 1.00 17.80 ? 85 VAL B N 1 ATOM 2324 C CA . VAL B 2 87 ? 46.195 8.719 -1.439 1.00 18.14 ? 85 VAL B CA 1 ATOM 2325 C C . VAL B 2 87 ? 44.720 8.849 -1.065 1.00 18.07 ? 85 VAL B C 1 ATOM 2326 O O . VAL B 2 87 ? 44.297 8.393 0.002 1.00 19.10 ? 85 VAL B O 1 ATOM 2327 C CB . VAL B 2 87 ? 46.931 10.028 -1.101 1.00 17.23 ? 85 VAL B CB 1 ATOM 2328 C CG1 . VAL B 2 87 ? 46.607 10.484 0.317 1.00 20.23 ? 85 VAL B CG1 1 ATOM 2329 C CG2 . VAL B 2 87 ? 48.434 9.834 -1.272 1.00 20.90 ? 85 VAL B CG2 1 ATOM 2330 N N . VAL B 2 88 ? 43.933 9.447 -1.951 1.00 16.99 ? 86 VAL B N 1 ATOM 2331 C CA . VAL B 2 88 ? 42.551 9.771 -1.594 1.00 16.88 ? 86 VAL B CA 1 ATOM 2332 C C . VAL B 2 88 ? 41.475 8.881 -2.213 1.00 18.52 ? 86 VAL B C 1 ATOM 2333 O O . VAL B 2 88 ? 40.313 8.997 -1.840 1.00 17.66 ? 86 VAL B O 1 ATOM 2334 C CB . VAL B 2 88 ? 42.202 11.250 -1.920 1.00 15.42 ? 86 VAL B CB 1 ATOM 2335 C CG1 . VAL B 2 88 ? 43.234 12.193 -1.299 1.00 19.38 ? 86 VAL B CG1 1 ATOM 2336 C CG2 . VAL B 2 88 ? 42.088 11.480 -3.435 1.00 14.56 ? 86 VAL B CG2 1 ATOM 2337 N N . GLU B 2 89 ? 41.848 7.980 -3.120 1.00 20.60 ? 87 GLU B N 1 ATOM 2338 C CA A GLU B 2 89 ? 40.842 7.249 -3.885 0.55 18.48 ? 87 GLU B CA 1 ATOM 2339 C CA B GLU B 2 89 ? 40.865 7.212 -3.888 0.45 22.75 ? 87 GLU B CA 1 ATOM 2340 C C . GLU B 2 89 ? 39.863 6.456 -3.021 1.00 20.12 ? 87 GLU B C 1 ATOM 2341 O O . GLU B 2 89 ? 38.680 6.376 -3.351 1.00 20.65 ? 87 GLU B O 1 ATOM 2342 C CB A GLU B 2 89 ? 41.487 6.358 -4.953 0.55 24.61 ? 87 GLU B CB 1 ATOM 2343 C CB B GLU B 2 89 ? 41.560 6.238 -4.848 0.45 24.56 ? 87 GLU B CB 1 ATOM 2344 C CG A GLU B 2 89 ? 42.482 5.352 -4.419 0.55 27.35 ? 87 GLU B CG 1 ATOM 2345 C CG B GLU B 2 89 ? 42.524 5.276 -4.175 0.45 29.27 ? 87 GLU B CG 1 ATOM 2346 C CD A GLU B 2 89 ? 41.856 3.999 -4.172 0.55 28.97 ? 87 GLU B CD 1 ATOM 2347 C CD B GLU B 2 89 ? 43.149 4.292 -5.146 0.45 33.99 ? 87 GLU B CD 1 ATOM 2348 O OE1 A GLU B 2 89 ? 42.500 3.156 -3.515 0.55 26.50 ? 87 GLU B OE1 1 ATOM 2349 O OE1 B GLU B 2 89 ? 42.648 4.178 -6.285 0.45 34.47 ? 87 GLU B OE1 1 ATOM 2350 O OE2 A GLU B 2 89 ? 40.721 3.779 -4.642 0.55 31.00 ? 87 GLU B OE2 1 ATOM 2351 O OE2 B GLU B 2 89 ? 44.143 3.635 -4.768 0.45 33.08 ? 87 GLU B OE2 1 ATOM 2352 N N . SER B 2 90 ? 40.343 5.899 -1.909 1.00 20.80 ? 88 SER B N 1 ATOM 2353 C CA . SER B 2 90 ? 39.501 5.048 -1.063 1.00 23.13 ? 88 SER B CA 1 ATOM 2354 C C . SER B 2 90 ? 38.288 5.753 -0.458 1.00 25.16 ? 88 SER B C 1 ATOM 2355 O O . SER B 2 90 ? 37.278 5.106 -0.174 1.00 26.52 ? 88 SER B O 1 ATOM 2356 C CB . SER B 2 90 ? 40.324 4.389 0.051 1.00 23.53 ? 88 SER B CB 1 ATOM 2357 O OG . SER B 2 90 ? 40.599 5.307 1.097 1.00 27.85 ? 88 SER B OG 1 ATOM 2358 N N . PHE B 2 91 ? 38.380 7.070 -0.265 1.00 20.72 ? 89 PHE B N 1 ATOM 2359 C CA . PHE B 2 91 ? 37.269 7.812 0.335 1.00 22.10 ? 89 PHE B CA 1 ATOM 2360 C C . PHE B 2 91 ? 36.666 8.871 -0.584 1.00 20.13 ? 89 PHE B C 1 ATOM 2361 O O . PHE B 2 91 ? 35.814 9.660 -0.163 1.00 20.01 ? 89 PHE B O 1 ATOM 2362 C CB . PHE B 2 91 ? 37.659 8.420 1.689 1.00 20.68 ? 89 PHE B CB 1 ATOM 2363 C CG . PHE B 2 91 ? 38.872 9.314 1.645 1.00 19.56 ? 89 PHE B CG 1 ATOM 2364 C CD1 . PHE B 2 91 ? 38.747 10.668 1.377 1.00 20.27 ? 89 PHE B CD1 1 ATOM 2365 C CD2 . PHE B 2 91 ? 40.132 8.802 1.914 1.00 27.92 ? 89 PHE B CD2 1 ATOM 2366 C CE1 . PHE B 2 91 ? 39.857 11.489 1.355 1.00 23.92 ? 89 PHE B CE1 1 ATOM 2367 C CE2 . PHE B 2 91 ? 41.249 9.618 1.893 1.00 27.95 ? 89 PHE B CE2 1 ATOM 2368 C CZ . PHE B 2 91 ? 41.112 10.961 1.614 1.00 22.36 ? 89 PHE B CZ 1 ATOM 2369 N N . THR B 2 92 ? 37.095 8.883 -1.842 1.00 18.01 ? 90 THR B N 1 ATOM 2370 C CA . THR B 2 92 ? 36.547 9.827 -2.817 1.00 16.91 ? 90 THR B CA 1 ATOM 2371 C C . THR B 2 92 ? 36.013 9.066 -4.024 1.00 17.06 ? 90 THR B C 1 ATOM 2372 O O . THR B 2 92 ? 34.799 8.935 -4.210 1.00 16.69 ? 90 THR B O 1 ATOM 2373 C CB . THR B 2 92 ? 37.612 10.841 -3.277 1.00 17.21 ? 90 THR B CB 1 ATOM 2374 O OG1 . THR B 2 92 ? 38.751 10.139 -3.798 1.00 18.34 ? 90 THR B OG1 1 ATOM 2375 C CG2 . THR B 2 92 ? 38.066 11.704 -2.112 1.00 18.35 ? 90 THR B CG2 1 ATOM 2376 N N . VAL B 2 93 ? 36.938 8.541 -4.825 1.00 18.04 ? 91 VAL B N 1 ATOM 2377 C CA . VAL B 2 93 ? 36.599 7.737 -5.991 1.00 18.54 ? 91 VAL B CA 1 ATOM 2378 C C . VAL B 2 93 ? 35.668 6.580 -5.623 1.00 19.21 ? 91 VAL B C 1 ATOM 2379 O O . VAL B 2 93 ? 34.695 6.305 -6.325 1.00 20.06 ? 91 VAL B O 1 ATOM 2380 C CB . VAL B 2 93 ? 37.875 7.173 -6.657 1.00 19.97 ? 91 VAL B CB 1 ATOM 2381 C CG1 . VAL B 2 93 ? 37.515 6.221 -7.785 1.00 21.57 ? 91 VAL B CG1 1 ATOM 2382 C CG2 . VAL B 2 93 ? 38.742 8.310 -7.180 1.00 20.18 ? 91 VAL B CG2 1 ATOM 2383 N N . GLN B 2 94 ? 35.959 5.926 -4.505 1.00 19.15 ? 92 GLN B N 1 ATOM 2384 C CA . GLN B 2 94 ? 35.207 4.737 -4.102 1.00 19.31 ? 92 GLN B CA 1 ATOM 2385 C C . GLN B 2 94 ? 34.027 5.040 -3.181 1.00 23.65 ? 92 GLN B C 1 ATOM 2386 O O . GLN B 2 94 ? 33.330 4.126 -2.739 1.00 20.28 ? 92 GLN B O 1 ATOM 2387 C CB . GLN B 2 94 ? 36.142 3.726 -3.432 1.00 20.56 ? 92 GLN B CB 1 ATOM 2388 C CG . GLN B 2 94 ? 37.233 3.205 -4.347 1.00 21.81 ? 92 GLN B CG 1 ATOM 2389 C CD . GLN B 2 94 ? 38.197 2.277 -3.633 1.00 45.75 ? 92 GLN B CD 1 ATOM 2390 O OE1 . GLN B 2 94 ? 37.972 1.888 -2.487 1.00 51.36 ? 92 GLN B OE1 1 ATOM 2391 N NE2 . GLN B 2 94 ? 39.281 1.920 -4.308 1.00 47.04 ? 92 GLN B NE2 1 ATOM 2392 N N . ARG B 2 95 ? 33.800 6.319 -2.897 1.00 19.03 ? 93 ARG B N 1 ATOM 2393 C CA . ARG B 2 95 ? 32.718 6.714 -2.009 1.00 17.49 ? 93 ARG B CA 1 ATOM 2394 C C . ARG B 2 95 ? 31.360 6.420 -2.639 1.00 18.22 ? 93 ARG B C 1 ATOM 2395 O O . ARG B 2 95 ? 31.078 6.821 -3.777 1.00 16.26 ? 93 ARG B O 1 ATOM 2396 C CB . ARG B 2 95 ? 32.823 8.201 -1.644 1.00 19.03 ? 93 ARG B CB 1 ATOM 2397 C CG . ARG B 2 95 ? 31.699 8.719 -0.750 1.00 15.33 ? 93 ARG B CG 1 ATOM 2398 C CD . ARG B 2 95 ? 31.910 10.207 -0.436 1.00 14.78 ? 93 ARG B CD 1 ATOM 2399 N NE . ARG B 2 95 ? 30.755 10.802 0.237 1.00 14.37 ? 93 ARG B NE 1 ATOM 2400 C CZ . ARG B 2 95 ? 30.498 10.665 1.535 1.00 15.34 ? 93 ARG B CZ 1 ATOM 2401 N NH1 . ARG B 2 95 ? 31.321 9.958 2.300 1.00 17.22 ? 93 ARG B NH1 1 ATOM 2402 N NH2 . ARG B 2 95 ? 29.424 11.242 2.071 1.00 17.87 ? 93 ARG B NH2 1 ATOM 2403 N N . ARG B 2 96 ? 30.523 5.725 -1.880 1.00 16.61 ? 94 ARG B N 1 ATOM 2404 C CA . ARG B 2 96 ? 29.182 5.368 -2.316 1.00 18.43 ? 94 ARG B CA 1 ATOM 2405 C C . ARG B 2 96 ? 28.230 5.488 -1.138 1.00 19.19 ? 94 ARG B C 1 ATOM 2406 O O . ARG B 2 96 ? 28.381 4.791 -0.138 1.00 22.50 ? 94 ARG B O 1 ATOM 2407 C CB . ARG B 2 96 ? 29.150 3.919 -2.811 1.00 24.65 ? 94 ARG B CB 1 ATOM 2408 C CG . ARG B 2 96 ? 30.050 3.618 -3.989 1.00 28.76 ? 94 ARG B CG 1 ATOM 2409 C CD . ARG B 2 96 ? 29.443 4.088 -5.294 1.00 21.28 ? 94 ARG B CD 1 ATOM 2410 N NE . ARG B 2 96 ? 30.223 3.617 -6.435 1.00 25.81 ? 94 ARG B NE 1 ATOM 2411 C CZ . ARG B 2 96 ? 31.313 4.226 -6.890 1.00 33.95 ? 94 ARG B CZ 1 ATOM 2412 N NH1 . ARG B 2 96 ? 31.974 3.729 -7.930 1.00 36.90 ? 94 ARG B NH1 1 ATOM 2413 N NH2 . ARG B 2 96 ? 31.750 5.328 -6.296 1.00 34.49 ? 94 ARG B NH2 1 ATOM 2414 N N . VAL B 2 97 ? 27.247 6.375 -1.256 1.00 15.63 ? 95 VAL B N 1 ATOM 2415 C CA . VAL B 2 97 ? 26.244 6.548 -0.217 1.00 17.80 ? 95 VAL B CA 1 ATOM 2416 C C . VAL B 2 97 ? 24.871 6.448 -0.868 1.00 15.57 ? 95 VAL B C 1 ATOM 2417 O O . VAL B 2 97 ? 24.564 7.201 -1.796 1.00 14.84 ? 95 VAL B O 1 ATOM 2418 C CB . VAL B 2 97 ? 26.398 7.913 0.479 1.00 15.74 ? 95 VAL B CB 1 ATOM 2419 C CG1 . VAL B 2 97 ? 25.423 8.054 1.632 1.00 16.14 ? 95 VAL B CG1 1 ATOM 2420 C CG2 . VAL B 2 97 ? 27.834 8.098 0.966 1.00 19.75 ? 95 VAL B CG2 1 ATOM 2421 N N A TYR B 2 98 ? 24.055 5.494 -0.445 0.61 17.33 ? 96 TYR B N 1 ATOM 2422 N N B TYR B 2 98 ? 24.048 5.539 -0.339 0.39 16.72 ? 96 TYR B N 1 ATOM 2423 C CA A TYR B 2 98 ? 22.794 5.305 -1.148 0.61 16.39 ? 96 TYR B CA 1 ATOM 2424 C CA B TYR B 2 98 ? 22.684 5.302 -0.817 0.39 18.47 ? 96 TYR B CA 1 ATOM 2425 C C A TYR B 2 98 ? 21.748 6.322 -0.714 0.61 17.81 ? 96 TYR B C 1 ATOM 2426 C C B TYR B 2 98 ? 21.827 6.551 -0.728 0.39 19.04 ? 96 TYR B C 1 ATOM 2427 O O A TYR B 2 98 ? 21.769 6.796 0.420 0.61 16.12 ? 96 TYR B O 1 ATOM 2428 O O B TYR B 2 98 ? 22.019 7.374 0.167 0.39 15.60 ? 96 TYR B O 1 ATOM 2429 C CB A TYR B 2 98 ? 22.291 3.851 -1.073 0.61 17.60 ? 96 TYR B CB 1 ATOM 2430 C CB B TYR B 2 98 ? 21.970 4.257 0.048 0.39 17.73 ? 96 TYR B CB 1 ATOM 2431 C CG A TYR B 2 98 ? 21.874 3.364 0.290 0.61 18.58 ? 96 TYR B CG 1 ATOM 2432 C CG B TYR B 2 98 ? 22.726 2.992 0.386 0.39 18.80 ? 96 TYR B CG 1 ATOM 2433 C CD1 A TYR B 2 98 ? 20.596 3.614 0.777 0.61 18.87 ? 96 TYR B CD1 1 ATOM 2434 C CD1 B TYR B 2 98 ? 23.406 2.275 -0.584 0.39 19.01 ? 96 TYR B CD1 1 ATOM 2435 C CD2 A TYR B 2 98 ? 22.739 2.615 1.073 0.61 19.43 ? 96 TYR B CD2 1 ATOM 2436 C CD2 B TYR B 2 98 ? 22.728 2.503 1.684 0.39 22.42 ? 96 TYR B CD2 1 ATOM 2437 C CE1 A TYR B 2 98 ? 20.204 3.160 2.017 0.61 21.87 ? 96 TYR B CE1 1 ATOM 2438 C CE1 B TYR B 2 98 ? 24.081 1.107 -0.264 0.39 20.17 ? 96 TYR B CE1 1 ATOM 2439 C CE2 A TYR B 2 98 ? 22.349 2.144 2.319 0.61 21.96 ? 96 TYR B CE2 1 ATOM 2440 C CE2 B TYR B 2 98 ? 23.398 1.345 2.014 0.39 20.97 ? 96 TYR B CE2 1 ATOM 2441 C CZ A TYR B 2 98 ? 21.077 2.420 2.785 0.61 21.99 ? 96 TYR B CZ 1 ATOM 2442 C CZ B TYR B 2 98 ? 24.073 0.650 1.040 0.39 21.13 ? 96 TYR B CZ 1 ATOM 2443 O OH A TYR B 2 98 ? 20.672 1.972 4.024 0.61 22.20 ? 96 TYR B OH 1 ATOM 2444 O OH B TYR B 2 98 ? 24.744 -0.509 1.374 0.39 22.43 ? 96 TYR B OH 1 ATOM 2445 N N . PRO B 2 99 ? 20.852 6.685 -1.639 1.00 15.57 ? 97 PRO B N 1 ATOM 2446 C CA . PRO B 2 99 ? 19.825 7.697 -1.411 1.00 17.29 ? 97 PRO B CA 1 ATOM 2447 C C . PRO B 2 99 ? 18.720 7.205 -0.470 1.00 17.43 ? 97 PRO B C 1 ATOM 2448 O O . PRO B 2 99 ? 18.365 6.016 -0.459 1.00 18.99 ? 97 PRO B O 1 ATOM 2449 C CB . PRO B 2 99 ? 19.258 7.926 -2.810 1.00 18.48 ? 97 PRO B CB 1 ATOM 2450 C CG . PRO B 2 99 ? 19.484 6.649 -3.519 1.00 23.76 ? 97 PRO B CG 1 ATOM 2451 C CD . PRO B 2 99 ? 20.786 6.127 -3.003 1.00 17.70 ? 97 PRO B CD 1 ATOM 2452 N N . GLU B 2 100 ? 18.202 8.127 0.334 1.00 16.24 ? 98 GLU B N 1 ATOM 2453 C CA . GLU B 2 100 ? 16.952 7.931 1.046 1.00 18.83 ? 98 GLU B CA 1 ATOM 2454 C C . GLU B 2 100 ? 15.862 8.478 0.140 1.00 18.20 ? 98 GLU B C 1 ATOM 2455 O O . GLU B 2 100 ? 16.004 9.567 -0.423 1.00 20.68 ? 98 GLU B O 1 ATOM 2456 C CB . GLU B 2 100 ? 16.948 8.703 2.369 1.00 25.21 ? 98 GLU B CB 1 ATOM 2457 C CG . GLU B 2 100 ? 18.089 8.352 3.309 1.00 40.99 ? 98 GLU B CG 1 ATOM 2458 C CD . GLU B 2 100 ? 17.885 7.012 3.990 1.00 57.39 ? 98 GLU B CD 1 ATOM 2459 O OE1 . GLU B 2 100 ? 18.891 6.330 4.281 1.00 62.22 ? 98 GLU B OE1 1 ATOM 2460 O OE2 . GLU B 2 100 ? 16.714 6.648 4.232 1.00 59.24 ? 98 GLU B OE2 1 ATOM 2461 N N . VAL B 2 101 ? 14.781 7.729 -0.020 1.00 17.75 ? 99 VAL B N 1 ATOM 2462 C CA . VAL B 2 101 ? 13.717 8.150 -0.921 1.00 17.59 ? 99 VAL B CA 1 ATOM 2463 C C . VAL B 2 101 ? 12.377 8.302 -0.197 1.00 18.68 ? 99 VAL B C 1 ATOM 2464 O O . VAL B 2 101 ? 11.903 7.373 0.463 1.00 22.28 ? 99 VAL B O 1 ATOM 2465 C CB . VAL B 2 101 ? 13.577 7.184 -2.108 1.00 17.85 ? 99 VAL B CB 1 ATOM 2466 C CG1 . VAL B 2 101 ? 12.528 7.694 -3.079 1.00 18.54 ? 99 VAL B CG1 1 ATOM 2467 C CG2 . VAL B 2 101 ? 14.916 7.009 -2.811 1.00 19.07 ? 99 VAL B CG2 1 ATOM 2468 N N . THR B 2 102 ? 11.781 9.485 -0.320 1.00 18.38 ? 100 THR B N 1 ATOM 2469 C CA . THR B 2 102 ? 10.508 9.804 0.308 1.00 19.50 ? 100 THR B CA 1 ATOM 2470 C C . THR B 2 102 ? 9.561 10.328 -0.760 1.00 19.27 ? 100 THR B C 1 ATOM 2471 O O . THR B 2 102 ? 9.957 11.138 -1.590 1.00 19.98 ? 100 THR B O 1 ATOM 2472 C CB . THR B 2 102 ? 10.683 10.916 1.369 1.00 22.90 ? 100 THR B CB 1 ATOM 2473 O OG1 . THR B 2 102 ? 11.594 10.475 2.385 1.00 31.27 ? 100 THR B OG1 1 ATOM 2474 C CG2 . THR B 2 102 ? 9.345 11.281 2.011 1.00 28.74 ? 100 THR B CG2 1 ATOM 2475 N N . VAL B 2 103 ? 8.313 9.868 -0.745 1.00 20.45 ? 101 VAL B N 1 ATOM 2476 C CA . VAL B 2 103 ? 7.294 10.431 -1.623 1.00 21.07 ? 101 VAL B CA 1 ATOM 2477 C C . VAL B 2 103 ? 6.210 11.111 -0.800 1.00 24.35 ? 101 VAL B C 1 ATOM 2478 O O . VAL B 2 103 ? 5.687 10.532 0.160 1.00 23.09 ? 101 VAL B O 1 ATOM 2479 C CB . VAL B 2 103 ? 6.657 9.368 -2.550 1.00 20.96 ? 101 VAL B CB 1 ATOM 2480 C CG1 . VAL B 2 103 ? 5.444 9.948 -3.283 1.00 24.51 ? 101 VAL B CG1 1 ATOM 2481 C CG2 . VAL B 2 103 ? 7.682 8.828 -3.540 1.00 20.74 ? 101 VAL B CG2 1 ATOM 2482 N N . TYR B 2 104 ? 5.883 12.348 -1.165 1.00 21.57 ? 102 TYR B N 1 ATOM 2483 C CA . TYR B 2 104 ? 4.776 13.054 -0.527 1.00 25.90 ? 102 TYR B CA 1 ATOM 2484 C C . TYR B 2 104 ? 3.991 13.895 -1.536 1.00 27.44 ? 102 TYR B C 1 ATOM 2485 O O . TYR B 2 104 ? 4.542 14.357 -2.536 1.00 21.18 ? 102 TYR B O 1 ATOM 2486 C CB . TYR B 2 104 ? 5.273 13.912 0.645 1.00 24.57 ? 102 TYR B CB 1 ATOM 2487 C CG . TYR B 2 104 ? 6.276 14.985 0.276 1.00 22.62 ? 102 TYR B CG 1 ATOM 2488 C CD1 . TYR B 2 104 ? 5.856 16.258 -0.099 1.00 30.82 ? 102 TYR B CD1 1 ATOM 2489 C CD2 . TYR B 2 104 ? 7.644 14.733 0.314 1.00 28.23 ? 102 TYR B CD2 1 ATOM 2490 C CE1 . TYR B 2 104 ? 6.769 17.245 -0.431 1.00 30.64 ? 102 TYR B CE1 1 ATOM 2491 C CE2 . TYR B 2 104 ? 8.563 15.717 -0.017 1.00 33.00 ? 102 TYR B CE2 1 ATOM 2492 C CZ . TYR B 2 104 ? 8.119 16.971 -0.388 1.00 35.23 ? 102 TYR B CZ 1 ATOM 2493 O OH . TYR B 2 104 ? 9.022 17.957 -0.722 1.00 35.99 ? 102 TYR B OH 1 ATOM 2494 N N . PRO B 2 105 ? 2.690 14.078 -1.285 1.00 23.93 ? 103 PRO B N 1 ATOM 2495 C CA . PRO B 2 105 ? 1.851 14.875 -2.184 1.00 24.29 ? 103 PRO B CA 1 ATOM 2496 C C . PRO B 2 105 ? 1.969 16.368 -1.904 1.00 30.75 ? 103 PRO B C 1 ATOM 2497 O O . PRO B 2 105 ? 2.282 16.771 -0.785 1.00 28.61 ? 103 PRO B O 1 ATOM 2498 C CB . PRO B 2 105 ? 0.441 14.398 -1.845 1.00 25.93 ? 103 PRO B CB 1 ATOM 2499 C CG . PRO B 2 105 ? 0.530 14.002 -0.407 1.00 28.77 ? 103 PRO B CG 1 ATOM 2500 C CD . PRO B 2 105 ? 1.896 13.404 -0.241 1.00 25.75 ? 103 PRO B CD 1 ATOM 2501 N N . ALA B 2 106 ? 1.712 17.180 -2.922 1.00 24.70 ? 104 ALA B N 1 ATOM 2502 C CA . ALA B 2 106 ? 1.742 18.628 -2.769 1.00 27.37 ? 104 ALA B CA 1 ATOM 2503 C C . ALA B 2 106 ? 0.695 19.244 -3.677 1.00 35.19 ? 104 ALA B C 1 ATOM 2504 O O . ALA B 2 106 ? -0.048 18.526 -4.348 1.00 26.04 ? 104 ALA B O 1 ATOM 2505 C CB . ALA B 2 106 ? 3.123 19.171 -3.101 1.00 27.16 ? 104 ALA B CB 1 ATOM 2506 N N . LYS B 2 107 ? 0.637 20.572 -3.691 1.00 39.03 ? 105 LYS B N 1 ATOM 2507 C CA . LYS B 2 107 ? -0.355 21.299 -4.475 1.00 34.84 ? 105 LYS B CA 1 ATOM 2508 C C . LYS B 2 107 ? 0.318 22.340 -5.366 1.00 42.81 ? 105 LYS B C 1 ATOM 2509 O O . LYS B 2 107 ? 1.243 23.026 -4.936 1.00 42.83 ? 105 LYS B O 1 ATOM 2510 C CB . LYS B 2 107 ? -1.347 21.999 -3.548 1.00 32.26 ? 105 LYS B CB 1 ATOM 2511 C CG . LYS B 2 107 ? -2.191 21.070 -2.691 1.00 33.31 ? 105 LYS B CG 1 ATOM 2512 C CD . LYS B 2 107 ? -3.109 21.866 -1.774 1.00 39.74 ? 105 LYS B CD 1 ATOM 2513 C CE . LYS B 2 107 ? -4.028 20.955 -0.975 1.00 44.63 ? 105 LYS B CE 1 ATOM 2514 N NZ . LYS B 2 107 ? -4.968 21.740 -0.126 1.00 49.21 ? 105 LYS B NZ 1 ATOM 2515 N N . THR B 2 108 ? -0.148 22.458 -6.605 1.00 39.70 ? 106 THR B N 1 ATOM 2516 C CA . THR B 2 108 ? 0.349 23.501 -7.496 1.00 39.63 ? 106 THR B CA 1 ATOM 2517 C C . THR B 2 108 ? -0.272 24.842 -7.114 1.00 40.69 ? 106 THR B C 1 ATOM 2518 O O . THR B 2 108 ? 0.373 25.886 -7.203 1.00 45.20 ? 106 THR B O 1 ATOM 2519 C CB . THR B 2 108 ? 0.047 23.190 -8.975 1.00 32.97 ? 106 THR B CB 1 ATOM 2520 O OG1 . THR B 2 108 ? -1.364 23.016 -9.153 1.00 30.52 ? 106 THR B OG1 1 ATOM 2521 C CG2 . THR B 2 108 ? 0.768 21.928 -9.414 1.00 31.01 ? 106 THR B CG2 1 ATOM 2522 N N . GLN B 2 109 ? -1.530 24.798 -6.689 1.00 43.97 ? 107 GLN B N 1 ATOM 2523 C CA . GLN B 2 109 ? -2.229 25.978 -6.192 1.00 42.93 ? 107 GLN B CA 1 ATOM 2524 C C . GLN B 2 109 ? -2.944 25.636 -4.890 1.00 50.13 ? 107 GLN B C 1 ATOM 2525 O O . GLN B 2 109 ? -3.488 24.540 -4.752 1.00 46.02 ? 107 GLN B O 1 ATOM 2526 C CB . GLN B 2 109 ? -3.235 26.488 -7.225 1.00 43.16 ? 107 GLN B CB 1 ATOM 2527 C CG . GLN B 2 109 ? -2.606 27.119 -8.452 1.00 38.05 ? 107 GLN B CG 1 ATOM 2528 C CD . GLN B 2 109 ? -3.646 27.663 -9.415 1.00 43.57 ? 107 GLN B CD 1 ATOM 2529 O OE1 . GLN B 2 109 ? -3.783 27.176 -10.539 1.00 38.23 ? 107 GLN B OE1 1 ATOM 2530 N NE2 . GLN B 2 109 ? -4.387 28.675 -8.976 1.00 50.38 ? 107 GLN B NE2 1 ATOM 2531 N N . PRO B 2 110 ? -2.954 26.580 -3.934 1.00 57.09 ? 108 PRO B N 1 ATOM 2532 C CA . PRO B 2 110 ? -3.490 26.351 -2.586 1.00 56.84 ? 108 PRO B CA 1 ATOM 2533 C C . PRO B 2 110 ? -4.921 25.814 -2.562 1.00 59.68 ? 108 PRO B C 1 ATOM 2534 O O . PRO B 2 110 ? -5.223 24.925 -1.763 1.00 63.54 ? 108 PRO B O 1 ATOM 2535 C CB . PRO B 2 110 ? -3.433 27.746 -1.943 1.00 58.10 ? 108 PRO B CB 1 ATOM 2536 C CG . PRO B 2 110 ? -3.291 28.705 -3.088 1.00 55.22 ? 108 PRO B CG 1 ATOM 2537 C CD . PRO B 2 110 ? -2.491 27.966 -4.108 1.00 51.90 ? 108 PRO B CD 1 ATOM 2538 N N . LEU B 2 111 ? -5.781 26.335 -3.431 1.00 57.29 ? 109 LEU B N 1 ATOM 2539 C CA . LEU B 2 111 ? -7.199 25.985 -3.408 1.00 54.89 ? 109 LEU B CA 1 ATOM 2540 C C . LEU B 2 111 ? -7.497 24.580 -3.935 1.00 58.32 ? 109 LEU B C 1 ATOM 2541 O O . LEU B 2 111 ? -8.538 24.004 -3.621 1.00 65.26 ? 109 LEU B O 1 ATOM 2542 C CB . LEU B 2 111 ? -8.019 27.018 -4.191 1.00 42.91 ? 109 LEU B CB 1 ATOM 2543 N N . GLN B 2 112 ? -6.584 24.031 -4.729 1.00 52.89 ? 110 GLN B N 1 ATOM 2544 C CA . GLN B 2 112 ? -6.838 22.769 -5.421 1.00 53.95 ? 110 GLN B CA 1 ATOM 2545 C C . GLN B 2 112 ? -6.459 21.533 -4.609 1.00 53.35 ? 110 GLN B C 1 ATOM 2546 O O . GLN B 2 112 ? -5.673 21.614 -3.667 1.00 56.11 ? 110 GLN B O 1 ATOM 2547 C CB . GLN B 2 112 ? -6.116 22.755 -6.771 1.00 52.40 ? 110 GLN B CB 1 ATOM 2548 C CG . GLN B 2 112 ? -6.691 23.743 -7.771 1.00 61.72 ? 110 GLN B CG 1 ATOM 2549 C CD . GLN B 2 112 ? -5.781 23.972 -8.957 1.00 63.74 ? 110 GLN B CD 1 ATOM 2550 O OE1 . GLN B 2 112 ? -4.756 23.306 -9.108 1.00 64.14 ? 110 GLN B OE1 1 ATOM 2551 N NE2 . GLN B 2 112 ? -6.147 24.927 -9.806 1.00 67.19 ? 110 GLN B NE2 1 ATOM 2552 N N . HIS B 2 113 ? -7.031 20.392 -4.985 1.00 53.41 ? 111 HIS B N 1 ATOM 2553 C CA . HIS B 2 113 ? -6.689 19.109 -4.378 1.00 53.53 ? 111 HIS B CA 1 ATOM 2554 C C . HIS B 2 113 ? -5.236 18.776 -4.699 1.00 40.21 ? 111 HIS B C 1 ATOM 2555 O O . HIS B 2 113 ? -4.645 19.394 -5.585 1.00 47.67 ? 111 HIS B O 1 ATOM 2556 C CB . HIS B 2 113 ? -7.607 18.003 -4.906 1.00 48.40 ? 111 HIS B CB 1 ATOM 2557 C CG . HIS B 2 113 ? -9.035 18.137 -4.476 1.00 60.21 ? 111 HIS B CG 1 ATOM 2558 N ND1 . HIS B 2 113 ? -9.801 19.247 -4.763 1.00 65.70 ? 111 HIS B ND1 1 ATOM 2559 C CD2 . HIS B 2 113 ? -9.839 17.296 -3.783 1.00 66.42 ? 111 HIS B CD2 1 ATOM 2560 C CE1 . HIS B 2 113 ? -11.014 19.085 -4.263 1.00 68.51 ? 111 HIS B CE1 1 ATOM 2561 N NE2 . HIS B 2 113 ? -11.063 17.909 -3.663 1.00 70.69 ? 111 HIS B NE2 1 ATOM 2562 N N . HIS B 2 114 ? -4.665 17.812 -3.975 1.00 38.21 ? 112 HIS B N 1 ATOM 2563 C CA . HIS B 2 114 ? -3.286 17.369 -4.206 1.00 37.59 ? 112 HIS B CA 1 ATOM 2564 C C . HIS B 2 114 ? -3.100 16.953 -5.658 1.00 38.92 ? 112 HIS B C 1 ATOM 2565 O O . HIS B 2 114 ? -3.780 16.047 -6.137 1.00 41.00 ? 112 HIS B O 1 ATOM 2566 C CB . HIS B 2 114 ? -2.937 16.185 -3.300 1.00 37.64 ? 112 HIS B CB 1 ATOM 2567 C CG . HIS B 2 114 ? -2.587 16.572 -1.897 1.00 48.09 ? 112 HIS B CG 1 ATOM 2568 N ND1 . HIS B 2 114 ? -1.862 17.705 -1.595 1.00 50.06 ? 112 HIS B ND1 1 ATOM 2569 C CD2 . HIS B 2 114 ? -2.858 15.973 -0.713 1.00 49.15 ? 112 HIS B CD2 1 ATOM 2570 C CE1 . HIS B 2 114 ? -1.706 17.790 -0.286 1.00 52.72 ? 112 HIS B CE1 1 ATOM 2571 N NE2 . HIS B 2 114 ? -2.300 16.750 0.272 1.00 55.01 ? 112 HIS B NE2 1 ATOM 2572 N N . ASN B 2 115 ? -2.176 17.607 -6.353 1.00 28.11 ? 113 ASN B N 1 ATOM 2573 C CA . ASN B 2 115 ? -1.993 17.370 -7.780 1.00 26.46 ? 113 ASN B CA 1 ATOM 2574 C C . ASN B 2 115 ? -0.522 17.373 -8.173 1.00 23.24 ? 113 ASN B C 1 ATOM 2575 O O . ASN B 2 115 ? -0.167 17.549 -9.339 1.00 23.82 ? 113 ASN B O 1 ATOM 2576 C CB . ASN B 2 115 ? -2.770 18.399 -8.603 1.00 26.88 ? 113 ASN B CB 1 ATOM 2577 C CG . ASN B 2 115 ? -2.244 19.810 -8.420 1.00 33.74 ? 113 ASN B CG 1 ATOM 2578 O OD1 . ASN B 2 115 ? -1.422 20.074 -7.540 1.00 29.59 ? 113 ASN B OD1 1 ATOM 2579 N ND2 . ASN B 2 115 ? -2.725 20.728 -9.250 1.00 35.12 ? 113 ASN B ND2 1 ATOM 2580 N N . LEU B 2 116 ? 0.329 17.190 -7.175 1.00 22.71 ? 114 LEU B N 1 ATOM 2581 C CA . LEU B 2 116 ? 1.759 17.134 -7.392 1.00 23.18 ? 114 LEU B CA 1 ATOM 2582 C C . LEU B 2 116 ? 2.280 16.026 -6.496 1.00 24.28 ? 114 LEU B C 1 ATOM 2583 O O . LEU B 2 116 ? 1.981 15.993 -5.302 1.00 32.08 ? 114 LEU B O 1 ATOM 2584 C CB . LEU B 2 116 ? 2.388 18.477 -7.012 1.00 30.20 ? 114 LEU B CB 1 ATOM 2585 C CG . LEU B 2 116 ? 3.749 18.876 -7.581 1.00 38.41 ? 114 LEU B CG 1 ATOM 2586 C CD1 . LEU B 2 116 ? 3.696 18.957 -9.101 1.00 30.95 ? 114 LEU B CD1 1 ATOM 2587 C CD2 . LEU B 2 116 ? 4.176 20.215 -6.985 1.00 33.53 ? 114 LEU B CD2 1 ATOM 2588 N N . LEU B 2 117 ? 3.020 15.088 -7.073 1.00 20.28 ? 115 LEU B N 1 ATOM 2589 C CA . LEU B 2 117 ? 3.672 14.070 -6.266 1.00 21.29 ? 115 LEU B CA 1 ATOM 2590 C C . LEU B 2 117 ? 5.159 14.368 -6.258 1.00 22.62 ? 115 LEU B C 1 ATOM 2591 O O . LEU B 2 117 ? 5.770 14.499 -7.320 1.00 20.02 ? 115 LEU B O 1 ATOM 2592 C CB . LEU B 2 117 ? 3.420 12.673 -6.829 1.00 20.55 ? 115 LEU B CB 1 ATOM 2593 C CG . LEU B 2 117 ? 1.962 12.219 -6.816 1.00 26.49 ? 115 LEU B CG 1 ATOM 2594 C CD1 . LEU B 2 117 ? 1.858 10.801 -7.324 1.00 28.94 ? 115 LEU B CD1 1 ATOM 2595 C CD2 . LEU B 2 117 ? 1.372 12.341 -5.415 1.00 28.80 ? 115 LEU B CD2 1 ATOM 2596 N N . VAL B 2 118 ? 5.732 14.509 -5.067 1.00 18.77 ? 116 VAL B N 1 ATOM 2597 C CA . VAL B 2 118 ? 7.153 14.816 -4.942 1.00 17.63 ? 116 VAL B CA 1 ATOM 2598 C C . VAL B 2 118 ? 7.940 13.570 -4.569 1.00 18.27 ? 116 VAL B C 1 ATOM 2599 O O . VAL B 2 118 ? 7.630 12.910 -3.581 1.00 19.46 ? 116 VAL B O 1 ATOM 2600 C CB . VAL B 2 118 ? 7.417 15.896 -3.873 1.00 17.77 ? 116 VAL B CB 1 ATOM 2601 C CG1 . VAL B 2 118 ? 8.905 16.244 -3.821 1.00 20.53 ? 116 VAL B CG1 1 ATOM 2602 C CG2 . VAL B 2 118 ? 6.586 17.142 -4.151 1.00 18.23 ? 116 VAL B CG2 1 ATOM 2603 N N . CYS B 2 119 ? 8.943 13.241 -5.376 1.00 16.51 ? 117 CYS B N 1 ATOM 2604 C CA . CYS B 2 119 ? 9.881 12.196 -5.008 1.00 16.32 ? 117 CYS B CA 1 ATOM 2605 C C . CYS B 2 119 ? 11.150 12.885 -4.534 1.00 15.50 ? 117 CYS B C 1 ATOM 2606 O O . CYS B 2 119 ? 11.885 13.479 -5.328 1.00 14.68 ? 117 CYS B O 1 ATOM 2607 C CB . CYS B 2 119 ? 10.163 11.271 -6.185 1.00 17.64 ? 117 CYS B CB 1 ATOM 2608 S SG . CYS B 2 119 ? 11.225 9.889 -5.736 1.00 16.84 ? 117 CYS B SG 1 ATOM 2609 N N . SER B 2 120 ? 11.376 12.847 -3.227 1.00 15.88 ? 118 SER B N 1 ATOM 2610 C CA . SER B 2 120 ? 12.529 13.511 -2.638 1.00 15.70 ? 118 SER B CA 1 ATOM 2611 C C . SER B 2 120 ? 13.615 12.469 -2.451 1.00 15.07 ? 118 SER B C 1 ATOM 2612 O O . SER B 2 120 ? 13.422 11.472 -1.754 1.00 15.81 ? 118 SER B O 1 ATOM 2613 C CB . SER B 2 120 ? 12.151 14.147 -1.293 1.00 18.66 ? 118 SER B CB 1 ATOM 2614 O OG . SER B 2 120 ? 13.212 14.938 -0.777 1.00 18.49 ? 118 SER B OG 1 ATOM 2615 N N . VAL B 2 121 ? 14.747 12.693 -3.106 1.00 14.21 ? 119 VAL B N 1 ATOM 2616 C CA . VAL B 2 121 ? 15.849 11.748 -3.095 1.00 14.11 ? 119 VAL B CA 1 ATOM 2617 C C . VAL B 2 121 ? 17.019 12.424 -2.401 1.00 15.89 ? 119 VAL B C 1 ATOM 2618 O O . VAL B 2 121 ? 17.560 13.402 -2.910 1.00 14.51 ? 119 VAL B O 1 ATOM 2619 C CB . VAL B 2 121 ? 16.220 11.352 -4.535 1.00 13.62 ? 119 VAL B CB 1 ATOM 2620 C CG1 . VAL B 2 121 ? 17.254 10.255 -4.537 1.00 13.73 ? 119 VAL B CG1 1 ATOM 2621 C CG2 . VAL B 2 121 ? 14.968 10.894 -5.286 1.00 14.09 ? 119 VAL B CG2 1 ATOM 2622 N N . ASN B 2 122 ? 17.395 11.917 -1.229 1.00 14.13 ? 120 ASN B N 1 ATOM 2623 C CA . ASN B 2 122 ? 18.307 12.650 -0.350 1.00 14.01 ? 120 ASN B CA 1 ATOM 2624 C C . ASN B 2 122 ? 19.525 11.881 0.109 1.00 15.54 ? 120 ASN B C 1 ATOM 2625 O O . ASN B 2 122 ? 19.458 10.684 0.362 1.00 17.55 ? 120 ASN B O 1 ATOM 2626 C CB . ASN B 2 122 ? 17.558 13.115 0.905 1.00 16.10 ? 120 ASN B CB 1 ATOM 2627 C CG . ASN B 2 122 ? 16.388 14.015 0.589 1.00 17.32 ? 120 ASN B CG 1 ATOM 2628 O OD1 . ASN B 2 122 ? 15.275 13.546 0.351 1.00 17.36 ? 120 ASN B OD1 1 ATOM 2629 N ND2 . ASN B 2 122 ? 16.626 15.321 0.606 1.00 15.28 ? 120 ASN B ND2 1 ATOM 2630 N N . GLY B 2 123 ? 20.637 12.595 0.227 1.00 13.65 ? 121 GLY B N 1 ATOM 2631 C CA . GLY B 2 123 ? 21.809 12.097 0.919 1.00 14.43 ? 121 GLY B CA 1 ATOM 2632 C C . GLY B 2 123 ? 22.744 11.214 0.121 1.00 16.12 ? 121 GLY B C 1 ATOM 2633 O O . GLY B 2 123 ? 23.564 10.511 0.708 1.00 17.78 ? 121 GLY B O 1 ATOM 2634 N N . PHE B 2 124 ? 22.646 11.235 -1.206 1.00 13.17 ? 122 PHE B N 1 ATOM 2635 C CA . PHE B 2 124 ? 23.405 10.266 -2.004 1.00 13.25 ? 122 PHE B CA 1 ATOM 2636 C C . PHE B 2 124 ? 24.751 10.789 -2.492 1.00 14.49 ? 122 PHE B C 1 ATOM 2637 O O . PHE B 2 124 ? 24.986 11.995 -2.534 1.00 13.28 ? 122 PHE B O 1 ATOM 2638 C CB . PHE B 2 124 ? 22.575 9.728 -3.180 1.00 13.26 ? 122 PHE B CB 1 ATOM 2639 C CG . PHE B 2 124 ? 22.066 10.793 -4.115 1.00 12.69 ? 122 PHE B CG 1 ATOM 2640 C CD1 . PHE B 2 124 ? 22.810 11.183 -5.226 1.00 12.39 ? 122 PHE B CD1 1 ATOM 2641 C CD2 . PHE B 2 124 ? 20.840 11.400 -3.892 1.00 12.63 ? 122 PHE B CD2 1 ATOM 2642 C CE1 . PHE B 2 124 ? 22.342 12.146 -6.101 1.00 12.04 ? 122 PHE B CE1 1 ATOM 2643 C CE2 . PHE B 2 124 ? 20.368 12.379 -4.753 1.00 12.23 ? 122 PHE B CE2 1 ATOM 2644 C CZ . PHE B 2 124 ? 21.119 12.760 -5.864 1.00 13.41 ? 122 PHE B CZ 1 ATOM 2645 N N . TYR B 2 125 ? 25.637 9.854 -2.834 1.00 13.27 ? 123 TYR B N 1 ATOM 2646 C CA . TYR B 2 125 ? 26.924 10.177 -3.440 1.00 14.16 ? 123 TYR B CA 1 ATOM 2647 C C . TYR B 2 125 ? 27.381 8.961 -4.235 1.00 13.79 ? 123 TYR B C 1 ATOM 2648 O O . TYR B 2 125 ? 27.276 7.834 -3.737 1.00 14.40 ? 123 TYR B O 1 ATOM 2649 C CB . TYR B 2 125 ? 27.976 10.520 -2.378 1.00 13.53 ? 123 TYR B CB 1 ATOM 2650 C CG . TYR B 2 125 ? 29.205 11.121 -3.010 1.00 13.31 ? 123 TYR B CG 1 ATOM 2651 C CD1 . TYR B 2 125 ? 29.331 12.497 -3.154 1.00 16.44 ? 123 TYR B CD1 1 ATOM 2652 C CD2 . TYR B 2 125 ? 30.217 10.314 -3.510 1.00 13.88 ? 123 TYR B CD2 1 ATOM 2653 C CE1 . TYR B 2 125 ? 30.434 13.047 -3.759 1.00 13.05 ? 123 TYR B CE1 1 ATOM 2654 C CE2 . TYR B 2 125 ? 31.324 10.857 -4.117 1.00 14.94 ? 123 TYR B CE2 1 ATOM 2655 C CZ . TYR B 2 125 ? 31.435 12.215 -4.235 1.00 13.78 ? 123 TYR B CZ 1 ATOM 2656 O OH . TYR B 2 125 ? 32.540 12.752 -4.850 1.00 16.59 ? 123 TYR B OH 1 ATOM 2657 N N . PRO B 2 126 ? 27.894 9.167 -5.460 1.00 13.81 ? 124 PRO B N 1 ATOM 2658 C CA . PRO B 2 126 ? 28.129 10.430 -6.175 1.00 13.36 ? 124 PRO B CA 1 ATOM 2659 C C . PRO B 2 126 ? 26.874 11.011 -6.824 1.00 14.20 ? 124 PRO B C 1 ATOM 2660 O O . PRO B 2 126 ? 25.757 10.565 -6.540 1.00 14.03 ? 124 PRO B O 1 ATOM 2661 C CB . PRO B 2 126 ? 29.159 10.039 -7.242 1.00 14.95 ? 124 PRO B CB 1 ATOM 2662 C CG . PRO B 2 126 ? 28.856 8.595 -7.513 1.00 17.28 ? 124 PRO B CG 1 ATOM 2663 C CD . PRO B 2 126 ? 28.466 8.013 -6.185 1.00 14.64 ? 124 PRO B CD 1 ATOM 2664 N N . GLY B 2 127 ? 27.067 12.009 -7.682 1.00 15.14 ? 125 GLY B N 1 ATOM 2665 C CA . GLY B 2 127 ? 25.962 12.805 -8.193 1.00 16.41 ? 125 GLY B CA 1 ATOM 2666 C C . GLY B 2 127 ? 25.093 12.148 -9.248 1.00 15.47 ? 125 GLY B C 1 ATOM 2667 O O . GLY B 2 127 ? 23.919 12.509 -9.393 1.00 19.22 ? 125 GLY B O 1 ATOM 2668 N N . SER B 2 128 ? 25.663 11.198 -9.981 1.00 17.45 ? 126 SER B N 1 ATOM 2669 C CA . SER B 2 128 ? 24.974 10.520 -11.070 1.00 15.87 ? 126 SER B CA 1 ATOM 2670 C C . SER B 2 128 ? 23.772 9.764 -10.553 1.00 15.54 ? 126 SER B C 1 ATOM 2671 O O . SER B 2 128 ? 23.912 8.846 -9.748 1.00 19.68 ? 126 SER B O 1 ATOM 2672 C CB . SER B 2 128 ? 25.907 9.515 -11.750 1.00 20.68 ? 126 SER B CB 1 ATOM 2673 O OG . SER B 2 128 ? 26.965 10.174 -12.421 1.00 40.48 ? 126 SER B OG 1 ATOM 2674 N N . ILE B 2 129 ? 22.592 10.142 -11.020 1.00 16.09 ? 127 ILE B N 1 ATOM 2675 C CA . ILE B 2 129 ? 21.383 9.473 -10.574 1.00 13.71 ? 127 ILE B CA 1 ATOM 2676 C C . ILE B 2 129 ? 20.304 9.535 -11.652 1.00 15.57 ? 127 ILE B C 1 ATOM 2677 O O . ILE B 2 129 ? 20.283 10.451 -12.475 1.00 16.17 ? 127 ILE B O 1 ATOM 2678 C CB . ILE B 2 129 ? 20.884 10.080 -9.251 1.00 13.61 ? 127 ILE B CB 1 ATOM 2679 C CG1 . ILE B 2 129 ? 19.999 9.078 -8.495 1.00 16.08 ? 127 ILE B CG1 1 ATOM 2680 C CG2 . ILE B 2 129 ? 20.181 11.423 -9.493 1.00 15.98 ? 127 ILE B CG2 1 ATOM 2681 C CD1 . ILE B 2 129 ? 19.802 9.424 -7.036 1.00 23.21 ? 127 ILE B CD1 1 ATOM 2682 N N . GLU B 2 130 ? 19.429 8.540 -11.668 1.00 15.10 ? 128 GLU B N 1 ATOM 2683 C CA . GLU B 2 130 ? 18.305 8.542 -12.589 1.00 14.94 ? 128 GLU B CA 1 ATOM 2684 C C . GLU B 2 130 ? 17.033 8.287 -11.796 1.00 16.90 ? 128 GLU B C 1 ATOM 2685 O O . GLU B 2 130 ? 16.923 7.283 -11.090 1.00 16.37 ? 128 GLU B O 1 ATOM 2686 C CB . GLU B 2 130 ? 18.493 7.475 -13.673 1.00 21.88 ? 128 GLU B CB 1 ATOM 2687 C CG . GLU B 2 130 ? 17.357 7.388 -14.687 1.00 34.23 ? 128 GLU B CG 1 ATOM 2688 C CD . GLU B 2 130 ? 17.557 8.303 -15.885 1.00 52.58 ? 128 GLU B CD 1 ATOM 2689 O OE1 . GLU B 2 130 ? 16.546 8.704 -16.505 1.00 53.66 ? 128 GLU B OE1 1 ATOM 2690 O OE2 . GLU B 2 130 ? 18.724 8.613 -16.211 1.00 56.12 ? 128 GLU B OE2 1 ATOM 2691 N N . VAL B 2 131 ? 16.079 9.206 -11.904 1.00 14.69 ? 129 VAL B N 1 ATOM 2692 C CA . VAL B 2 131 ? 14.810 9.091 -11.194 1.00 14.90 ? 129 VAL B CA 1 ATOM 2693 C C . VAL B 2 131 ? 13.654 9.092 -12.189 1.00 16.07 ? 129 VAL B C 1 ATOM 2694 O O . VAL B 2 131 ? 13.554 9.990 -13.034 1.00 16.95 ? 129 VAL B O 1 ATOM 2695 C CB . VAL B 2 131 ? 14.613 10.279 -10.227 1.00 15.91 ? 129 VAL B CB 1 ATOM 2696 C CG1 . VAL B 2 131 ? 13.311 10.112 -9.434 1.00 17.72 ? 129 VAL B CG1 1 ATOM 2697 C CG2 . VAL B 2 131 ? 15.810 10.412 -9.296 1.00 17.38 ? 129 VAL B CG2 1 ATOM 2698 N N . ARG B 2 132 ? 12.782 8.097 -12.087 1.00 16.45 ? 130 ARG B N 1 ATOM 2699 C CA . ARG B 2 132 ? 11.657 7.971 -13.008 1.00 18.54 ? 130 ARG B CA 1 ATOM 2700 C C . ARG B 2 132 ? 10.340 7.749 -12.271 1.00 17.75 ? 130 ARG B C 1 ATOM 2701 O O . ARG B 2 132 ? 10.301 7.137 -11.200 1.00 17.82 ? 130 ARG B O 1 ATOM 2702 C CB . ARG B 2 132 ? 11.888 6.822 -13.999 1.00 20.50 ? 130 ARG B CB 1 ATOM 2703 C CG . ARG B 2 132 ? 13.123 6.996 -14.877 1.00 30.67 ? 130 ARG B CG 1 ATOM 2704 C CD . ARG B 2 132 ? 13.264 5.858 -15.886 1.00 45.07 ? 130 ARG B CD 1 ATOM 2705 N NE . ARG B 2 132 ? 14.374 6.080 -16.813 1.00 58.28 ? 130 ARG B NE 1 ATOM 2706 C CZ . ARG B 2 132 ? 14.309 6.858 -17.892 1.00 62.38 ? 130 ARG B CZ 1 ATOM 2707 N NH1 . ARG B 2 132 ? 13.186 7.499 -18.186 1.00 66.27 ? 130 ARG B NH1 1 ATOM 2708 N NH2 . ARG B 2 132 ? 15.369 6.999 -18.676 1.00 65.63 ? 130 ARG B NH2 1 ATOM 2709 N N . TRP B 2 133 ? 9.259 8.240 -12.864 1.00 17.90 ? 131 TRP B N 1 ATOM 2710 C CA . TRP B 2 133 ? 7.935 8.057 -12.296 1.00 18.65 ? 131 TRP B CA 1 ATOM 2711 C C . TRP B 2 133 ? 7.125 7.020 -13.063 1.00 20.65 ? 131 TRP B C 1 ATOM 2712 O O . TRP B 2 133 ? 7.222 6.918 -14.287 1.00 20.54 ? 131 TRP B O 1 ATOM 2713 C CB . TRP B 2 133 ? 7.174 9.384 -12.302 1.00 18.36 ? 131 TRP B CB 1 ATOM 2714 C CG . TRP B 2 133 ? 7.397 10.245 -11.097 1.00 17.72 ? 131 TRP B CG 1 ATOM 2715 C CD1 . TRP B 2 133 ? 8.117 11.407 -11.036 1.00 16.78 ? 131 TRP B CD1 1 ATOM 2716 C CD2 . TRP B 2 133 ? 6.864 10.035 -9.784 1.00 18.20 ? 131 TRP B CD2 1 ATOM 2717 N NE1 . TRP B 2 133 ? 8.077 11.922 -9.765 1.00 16.62 ? 131 TRP B NE1 1 ATOM 2718 C CE2 . TRP B 2 133 ? 7.305 11.106 -8.978 1.00 17.50 ? 131 TRP B CE2 1 ATOM 2719 C CE3 . TRP B 2 133 ? 6.058 9.046 -9.209 1.00 19.33 ? 131 TRP B CE3 1 ATOM 2720 C CZ2 . TRP B 2 133 ? 6.970 11.213 -7.630 1.00 18.44 ? 131 TRP B CZ2 1 ATOM 2721 C CZ3 . TRP B 2 133 ? 5.727 9.155 -7.870 1.00 22.48 ? 131 TRP B CZ3 1 ATOM 2722 C CH2 . TRP B 2 133 ? 6.185 10.231 -7.096 1.00 22.68 ? 131 TRP B CH2 1 ATOM 2723 N N . PHE B 2 134 ? 6.319 6.257 -12.328 1.00 20.87 ? 132 PHE B N 1 ATOM 2724 C CA . PHE B 2 134 ? 5.441 5.253 -12.913 1.00 22.30 ? 132 PHE B CA 1 ATOM 2725 C C . PHE B 2 134 ? 4.037 5.384 -12.345 1.00 27.64 ? 132 PHE B C 1 ATOM 2726 O O . PHE B 2 134 ? 3.865 5.663 -11.160 1.00 24.22 ? 132 PHE B O 1 ATOM 2727 C CB . PHE B 2 134 ? 5.971 3.843 -12.630 1.00 23.07 ? 132 PHE B CB 1 ATOM 2728 C CG . PHE B 2 134 ? 7.273 3.537 -13.311 1.00 24.40 ? 132 PHE B CG 1 ATOM 2729 C CD1 . PHE B 2 134 ? 8.470 3.986 -12.778 1.00 26.38 ? 132 PHE B CD1 1 ATOM 2730 C CD2 . PHE B 2 134 ? 7.300 2.799 -14.482 1.00 26.96 ? 132 PHE B CD2 1 ATOM 2731 C CE1 . PHE B 2 134 ? 9.669 3.714 -13.404 1.00 25.46 ? 132 PHE B CE1 1 ATOM 2732 C CE2 . PHE B 2 134 ? 8.496 2.520 -15.114 1.00 24.27 ? 132 PHE B CE2 1 ATOM 2733 C CZ . PHE B 2 134 ? 9.684 2.976 -14.575 1.00 26.48 ? 132 PHE B CZ 1 ATOM 2734 N N . ARG B 2 135 ? 3.037 5.192 -13.202 1.00 31.01 ? 133 ARG B N 1 ATOM 2735 C CA . ARG B 2 135 ? 1.641 5.162 -12.783 1.00 26.95 ? 133 ARG B CA 1 ATOM 2736 C C . ARG B 2 135 ? 1.095 3.790 -13.141 1.00 29.70 ? 133 ARG B C 1 ATOM 2737 O O . ARG B 2 135 ? 1.057 3.419 -14.315 1.00 29.36 ? 133 ARG B O 1 ATOM 2738 C CB . ARG B 2 135 ? 0.832 6.256 -13.489 1.00 27.95 ? 133 ARG B CB 1 ATOM 2739 C CG . ARG B 2 135 ? -0.650 6.283 -13.110 1.00 26.67 ? 133 ARG B CG 1 ATOM 2740 C CD . ARG B 2 135 ? -1.463 7.193 -14.035 1.00 26.87 ? 133 ARG B CD 1 ATOM 2741 N NE . ARG B 2 135 ? -1.135 8.607 -13.877 1.00 42.05 ? 133 ARG B NE 1 ATOM 2742 C CZ . ARG B 2 135 ? -0.404 9.308 -14.740 1.00 47.42 ? 133 ARG B CZ 1 ATOM 2743 N NH1 . ARG B 2 135 ? -0.156 10.594 -14.514 1.00 40.27 ? 133 ARG B NH1 1 ATOM 2744 N NH2 . ARG B 2 135 ? 0.081 8.724 -15.829 1.00 42.28 ? 133 ARG B NH2 1 ATOM 2745 N N . ASN B 2 136 ? 0.692 3.037 -12.124 1.00 30.72 ? 134 ASN B N 1 ATOM 2746 C CA . ASN B 2 136 ? 0.249 1.659 -12.310 1.00 36.30 ? 134 ASN B CA 1 ATOM 2747 C C . ASN B 2 136 ? 1.188 0.855 -13.208 1.00 37.06 ? 134 ASN B C 1 ATOM 2748 O O . ASN B 2 136 ? 0.743 0.139 -14.102 1.00 43.09 ? 134 ASN B O 1 ATOM 2749 C CB . ASN B 2 136 ? -1.181 1.621 -12.860 1.00 41.44 ? 134 ASN B CB 1 ATOM 2750 C CG . ASN B 2 136 ? -2.184 2.268 -11.924 1.00 37.47 ? 134 ASN B CG 1 ATOM 2751 O OD1 . ASN B 2 136 ? -2.091 2.129 -10.704 1.00 41.92 ? 134 ASN B OD1 1 ATOM 2752 N ND2 . ASN B 2 136 ? -3.148 2.982 -12.491 1.00 44.01 ? 134 ASN B ND2 1 ATOM 2753 N N . GLY B 2 137 ? 2.491 1.002 -12.986 1.00 34.61 ? 135 GLY B N 1 ATOM 2754 C CA . GLY B 2 137 ? 3.476 0.203 -13.696 1.00 41.33 ? 135 GLY B CA 1 ATOM 2755 C C . GLY B 2 137 ? 3.890 0.723 -15.062 1.00 44.03 ? 135 GLY B C 1 ATOM 2756 O O . GLY B 2 137 ? 4.730 0.116 -15.730 1.00 43.70 ? 135 GLY B O 1 ATOM 2757 N N . GLN B 2 138 ? 3.307 1.841 -15.483 1.00 31.92 ? 136 GLN B N 1 ATOM 2758 C CA . GLN B 2 138 ? 3.650 2.445 -16.766 1.00 31.80 ? 136 GLN B CA 1 ATOM 2759 C C . GLN B 2 138 ? 4.428 3.728 -16.514 1.00 25.13 ? 136 GLN B C 1 ATOM 2760 O O . GLN B 2 138 ? 3.994 4.554 -15.714 1.00 28.74 ? 136 GLN B O 1 ATOM 2761 C CB . GLN B 2 138 ? 2.382 2.770 -17.555 1.00 38.22 ? 136 GLN B CB 1 ATOM 2762 C CG . GLN B 2 138 ? 1.450 1.588 -17.758 1.00 55.25 ? 136 GLN B CG 1 ATOM 2763 C CD . GLN B 2 138 ? 2.036 0.539 -18.678 1.00 63.93 ? 136 GLN B CD 1 ATOM 2764 O OE1 . GLN B 2 138 ? 2.952 0.819 -19.453 1.00 63.53 ? 136 GLN B OE1 1 ATOM 2765 N NE2 . GLN B 2 138 ? 1.513 -0.681 -18.595 1.00 64.32 ? 136 GLN B NE2 1 ATOM 2766 N N . GLU B 2 139 ? 5.563 3.907 -17.189 1.00 28.31 ? 137 GLU B N 1 ATOM 2767 C CA . GLU B 2 139 ? 6.359 5.113 -16.970 1.00 27.07 ? 137 GLU B CA 1 ATOM 2768 C C . GLU B 2 139 ? 5.632 6.363 -17.446 1.00 30.17 ? 137 GLU B C 1 ATOM 2769 O O . GLU B 2 139 ? 5.060 6.397 -18.537 1.00 26.81 ? 137 GLU B O 1 ATOM 2770 C CB . GLU B 2 139 ? 7.754 5.042 -17.613 1.00 32.42 ? 137 GLU B CB 1 ATOM 2771 C CG . GLU B 2 139 ? 8.597 6.295 -17.312 1.00 24.28 ? 137 GLU B CG 1 ATOM 2772 C CD . GLU B 2 139 ? 10.012 6.241 -17.859 1.00 43.59 ? 137 GLU B CD 1 ATOM 2773 O OE1 . GLU B 2 139 ? 10.395 5.211 -18.450 1.00 45.27 ? 137 GLU B OE1 1 ATOM 2774 O OE2 . GLU B 2 139 ? 10.741 7.243 -17.692 1.00 46.43 ? 137 GLU B OE2 1 ATOM 2775 N N . GLU B 2 140 ? 5.645 7.383 -16.602 1.00 21.52 ? 138 GLU B N 1 ATOM 2776 C CA . GLU B 2 140 ? 5.081 8.672 -16.967 1.00 21.20 ? 138 GLU B CA 1 ATOM 2777 C C . GLU B 2 140 ? 6.207 9.656 -17.222 1.00 20.08 ? 138 GLU B C 1 ATOM 2778 O O . GLU B 2 140 ? 6.944 10.024 -16.305 1.00 21.07 ? 138 GLU B O 1 ATOM 2779 C CB . GLU B 2 140 ? 4.164 9.193 -15.866 1.00 26.60 ? 138 GLU B CB 1 ATOM 2780 C CG . GLU B 2 140 ? 3.476 10.501 -16.217 1.00 37.27 ? 138 GLU B CG 1 ATOM 2781 C CD . GLU B 2 140 ? 2.667 10.405 -17.496 1.00 44.37 ? 138 GLU B CD 1 ATOM 2782 O OE1 . GLU B 2 140 ? 3.101 10.975 -18.519 1.00 40.73 ? 138 GLU B OE1 1 ATOM 2783 O OE2 . GLU B 2 140 ? 1.598 9.759 -17.476 1.00 43.98 ? 138 GLU B OE2 1 ATOM 2784 N N . LYS B 2 141 ? 6.339 10.076 -18.474 1.00 25.91 ? 139 LYS B N 1 ATOM 2785 C CA . LYS B 2 141 ? 7.384 11.015 -18.851 1.00 22.14 ? 139 LYS B CA 1 ATOM 2786 C C . LYS B 2 141 ? 6.871 12.445 -19.003 1.00 23.38 ? 139 LYS B C 1 ATOM 2787 O O . LYS B 2 141 ? 7.664 13.377 -19.089 1.00 27.81 ? 139 LYS B O 1 ATOM 2788 C CB . LYS B 2 141 ? 8.079 10.565 -20.140 1.00 27.68 ? 139 LYS B CB 1 ATOM 2789 C CG . LYS B 2 141 ? 8.957 9.328 -19.977 1.00 34.40 ? 139 LYS B CG 1 ATOM 2790 C CD . LYS B 2 141 ? 9.742 9.037 -21.251 1.00 40.10 ? 139 LYS B CD 1 ATOM 2791 C CE . LYS B 2 141 ? 10.699 7.870 -21.065 1.00 42.63 ? 139 LYS B CE 1 ATOM 2792 N NZ . LYS B 2 141 ? 11.259 7.405 -22.367 1.00 40.51 ? 139 LYS B NZ 1 ATOM 2793 N N . THR B 2 142 ? 5.551 12.625 -19.022 1.00 23.74 ? 140 THR B N 1 ATOM 2794 C CA . THR B 2 142 ? 4.989 13.970 -19.140 1.00 21.60 ? 140 THR B CA 1 ATOM 2795 C C . THR B 2 142 ? 4.705 14.588 -17.773 1.00 20.35 ? 140 THR B C 1 ATOM 2796 O O . THR B 2 142 ? 4.397 13.882 -16.811 1.00 24.46 ? 140 THR B O 1 ATOM 2797 C CB . THR B 2 142 ? 3.686 13.968 -19.959 1.00 32.99 ? 140 THR B CB 1 ATOM 2798 O OG1 . THR B 2 142 ? 2.654 13.322 -19.206 1.00 38.91 ? 140 THR B OG1 1 ATOM 2799 C CG2 . THR B 2 142 ? 3.883 13.233 -21.274 1.00 29.46 ? 140 THR B CG2 1 ATOM 2800 N N . GLY B 2 143 ? 4.799 15.911 -17.696 1.00 21.11 ? 141 GLY B N 1 ATOM 2801 C CA . GLY B 2 143 ? 4.483 16.626 -16.472 1.00 22.56 ? 141 GLY B CA 1 ATOM 2802 C C . GLY B 2 143 ? 5.495 16.400 -15.363 1.00 18.52 ? 141 GLY B C 1 ATOM 2803 O O . GLY B 2 143 ? 5.172 16.503 -14.180 1.00 18.41 ? 141 GLY B O 1 ATOM 2804 N N . VAL B 2 144 ? 6.732 16.102 -15.743 1.00 17.20 ? 142 VAL B N 1 ATOM 2805 C CA . VAL B 2 144 ? 7.794 15.892 -14.763 1.00 17.30 ? 142 VAL B CA 1 ATOM 2806 C C . VAL B 2 144 ? 8.739 17.091 -14.709 1.00 15.98 ? 142 VAL B C 1 ATOM 2807 O O . VAL B 2 144 ? 9.246 17.531 -15.737 1.00 15.83 ? 142 VAL B O 1 ATOM 2808 C CB . VAL B 2 144 ? 8.581 14.604 -15.070 1.00 16.25 ? 142 VAL B CB 1 ATOM 2809 C CG1 . VAL B 2 144 ? 9.752 14.451 -14.117 1.00 15.89 ? 142 VAL B CG1 1 ATOM 2810 C CG2 . VAL B 2 144 ? 7.649 13.395 -14.973 1.00 16.99 ? 142 VAL B CG2 1 ATOM 2811 N N . VAL B 2 145 ? 8.928 17.640 -13.510 1.00 15.38 ? 143 VAL B N 1 ATOM 2812 C CA A VAL B 2 145 ? 9.836 18.758 -13.302 0.67 15.43 ? 143 VAL B CA 1 ATOM 2813 C CA B VAL B 2 145 ? 9.830 18.770 -13.285 0.33 16.48 ? 143 VAL B CA 1 ATOM 2814 C C . VAL B 2 145 ? 10.716 18.454 -12.087 1.00 16.66 ? 143 VAL B C 1 ATOM 2815 O O . VAL B 2 145 ? 10.305 17.741 -11.181 1.00 17.60 ? 143 VAL B O 1 ATOM 2816 C CB A VAL B 2 145 ? 9.057 20.088 -13.119 0.67 16.80 ? 143 VAL B CB 1 ATOM 2817 C CB B VAL B 2 145 ? 9.056 20.081 -13.003 0.33 18.05 ? 143 VAL B CB 1 ATOM 2818 C CG1 A VAL B 2 145 ? 8.233 20.058 -11.831 0.67 16.02 ? 143 VAL B CG1 1 ATOM 2819 C CG1 B VAL B 2 145 ? 10.005 21.272 -12.902 0.33 20.54 ? 143 VAL B CG1 1 ATOM 2820 C CG2 A VAL B 2 145 ? 9.995 21.294 -13.149 0.67 20.12 ? 143 VAL B CG2 1 ATOM 2821 C CG2 B VAL B 2 145 ? 8.036 20.336 -14.078 0.33 18.57 ? 143 VAL B CG2 1 ATOM 2822 N N . SER B 2 146 ? 11.935 18.981 -12.076 1.00 13.83 ? 144 SER B N 1 ATOM 2823 C CA . SER B 2 146 ? 12.870 18.675 -11.005 1.00 13.31 ? 144 SER B CA 1 ATOM 2824 C C . SER B 2 146 ? 13.660 19.903 -10.551 1.00 13.76 ? 144 SER B C 1 ATOM 2825 O O . SER B 2 146 ? 13.742 20.912 -11.263 1.00 13.65 ? 144 SER B O 1 ATOM 2826 C CB . SER B 2 146 ? 13.836 17.579 -11.474 1.00 14.37 ? 144 SER B CB 1 ATOM 2827 O OG . SER B 2 146 ? 14.828 17.299 -10.502 1.00 12.58 ? 144 SER B OG 1 ATOM 2828 N N . THR B 2 147 ? 14.234 19.812 -9.355 1.00 13.08 ? 145 THR B N 1 ATOM 2829 C CA . THR B 2 147 ? 15.204 20.802 -8.895 1.00 13.37 ? 145 THR B CA 1 ATOM 2830 C C . THR B 2 147 ? 16.508 20.700 -9.674 1.00 12.65 ? 145 THR B C 1 ATOM 2831 O O . THR B 2 147 ? 17.314 21.646 -9.690 1.00 14.97 ? 145 THR B O 1 ATOM 2832 C CB . THR B 2 147 ? 15.558 20.577 -7.415 1.00 13.69 ? 145 THR B CB 1 ATOM 2833 O OG1 . THR B 2 147 ? 15.988 19.222 -7.238 1.00 13.25 ? 145 THR B OG1 1 ATOM 2834 C CG2 . THR B 2 147 ? 14.360 20.835 -6.535 1.00 14.95 ? 145 THR B CG2 1 ATOM 2835 N N . GLY B 2 148 ? 16.721 19.559 -10.319 1.00 12.71 ? 146 GLY B N 1 ATOM 2836 C CA . GLY B 2 148 ? 18.029 19.224 -10.847 1.00 13.97 ? 146 GLY B CA 1 ATOM 2837 C C . GLY B 2 148 ? 18.862 18.675 -9.706 1.00 11.74 ? 146 GLY B C 1 ATOM 2838 O O . GLY B 2 148 ? 18.348 18.464 -8.607 1.00 12.78 ? 146 GLY B O 1 ATOM 2839 N N . LEU B 2 149 ? 20.144 18.443 -9.962 1.00 11.67 ? 147 LEU B N 1 ATOM 2840 C CA . LEU B 2 149 ? 21.032 17.884 -8.952 1.00 11.45 ? 147 LEU B CA 1 ATOM 2841 C C . LEU B 2 149 ? 21.522 18.983 -8.031 1.00 11.43 ? 147 LEU B C 1 ATOM 2842 O O . LEU B 2 149 ? 22.108 19.963 -8.488 1.00 13.94 ? 147 LEU B O 1 ATOM 2843 C CB . LEU B 2 149 ? 22.226 17.199 -9.617 1.00 12.61 ? 147 LEU B CB 1 ATOM 2844 C CG . LEU B 2 149 ? 23.226 16.492 -8.699 1.00 15.18 ? 147 LEU B CG 1 ATOM 2845 C CD1 . LEU B 2 149 ? 22.578 15.319 -7.984 1.00 16.21 ? 147 LEU B CD1 1 ATOM 2846 C CD2 . LEU B 2 149 ? 24.427 16.008 -9.494 1.00 19.48 ? 147 LEU B CD2 1 ATOM 2847 N N . ILE B 2 150 ? 21.272 18.822 -6.738 1.00 11.38 ? 148 ILE B N 1 ATOM 2848 C CA . ILE B 2 150 ? 21.675 19.809 -5.737 1.00 11.54 ? 148 ILE B CA 1 ATOM 2849 C C . ILE B 2 150 ? 22.813 19.259 -4.878 1.00 11.50 ? 148 ILE B C 1 ATOM 2850 O O . ILE B 2 150 ? 22.679 18.201 -4.263 1.00 12.77 ? 148 ILE B O 1 ATOM 2851 C CB . ILE B 2 150 ? 20.499 20.154 -4.814 1.00 12.98 ? 148 ILE B CB 1 ATOM 2852 C CG1 . ILE B 2 150 ? 19.335 20.717 -5.622 1.00 17.59 ? 148 ILE B CG1 1 ATOM 2853 C CG2 . ILE B 2 150 ? 20.936 21.134 -3.725 1.00 16.29 ? 148 ILE B CG2 1 ATOM 2854 C CD1 . ILE B 2 150 ? 18.076 20.893 -4.807 1.00 23.56 ? 148 ILE B CD1 1 ATOM 2855 N N . GLN B 2 151 ? 23.940 19.966 -4.852 1.00 11.63 ? 149 GLN B N 1 ATOM 2856 C CA . GLN B 2 151 ? 25.019 19.637 -3.925 1.00 13.50 ? 149 GLN B CA 1 ATOM 2857 C C . GLN B 2 151 ? 24.688 20.225 -2.545 1.00 23.46 ? 149 GLN B C 1 ATOM 2858 O O . GLN B 2 151 ? 24.252 21.373 -2.436 1.00 24.81 ? 149 GLN B O 1 ATOM 2859 C CB . GLN B 2 151 ? 26.363 20.175 -4.460 1.00 22.24 ? 149 GLN B CB 1 ATOM 2860 C CG . GLN B 2 151 ? 27.525 19.198 -4.322 1.00 35.81 ? 149 GLN B CG 1 ATOM 2861 C CD . GLN B 2 151 ? 28.710 19.531 -5.220 1.00 42.71 ? 149 GLN B CD 1 ATOM 2862 O OE1 . GLN B 2 151 ? 28.803 20.632 -5.764 1.00 42.49 ? 149 GLN B OE1 1 ATOM 2863 N NE2 . GLN B 2 151 ? 29.620 18.569 -5.382 1.00 36.90 ? 149 GLN B NE2 1 ATOM 2864 N N . ASN B 2 152 ? 24.867 19.433 -1.492 1.00 13.22 ? 150 ASN B N 1 ATOM 2865 C CA . ASN B 2 152 ? 24.608 19.911 -0.134 1.00 12.76 ? 150 ASN B CA 1 ATOM 2866 C C . ASN B 2 152 ? 25.856 20.504 0.522 1.00 18.50 ? 150 ASN B C 1 ATOM 2867 O O . ASN B 2 152 ? 25.773 21.117 1.595 1.00 15.43 ? 150 ASN B O 1 ATOM 2868 C CB . ASN B 2 152 ? 24.040 18.803 0.741 1.00 14.54 ? 150 ASN B CB 1 ATOM 2869 C CG . ASN B 2 152 ? 22.639 18.393 0.323 1.00 17.29 ? 150 ASN B CG 1 ATOM 2870 O OD1 . ASN B 2 152 ? 21.815 19.237 -0.044 1.00 19.19 ? 150 ASN B OD1 1 ATOM 2871 N ND2 . ASN B 2 152 ? 22.367 17.098 0.363 1.00 15.04 ? 150 ASN B ND2 1 ATOM 2872 N N . GLY B 2 153 ? 27.005 20.303 -0.121 1.00 12.93 ? 151 GLY B N 1 ATOM 2873 C CA . GLY B 2 153 ? 28.263 20.879 0.328 1.00 13.38 ? 151 GLY B CA 1 ATOM 2874 C C . GLY B 2 153 ? 29.007 20.000 1.316 1.00 13.65 ? 151 GLY B C 1 ATOM 2875 O O . GLY B 2 153 ? 30.099 20.358 1.770 1.00 15.30 ? 151 GLY B O 1 ATOM 2876 N N . ASP B 2 154 ? 28.417 18.853 1.646 1.00 13.66 ? 152 ASP B N 1 ATOM 2877 C CA . ASP B 2 154 ? 28.950 17.959 2.671 1.00 13.93 ? 152 ASP B CA 1 ATOM 2878 C C . ASP B 2 154 ? 29.174 16.545 2.142 1.00 13.65 ? 152 ASP B C 1 ATOM 2879 O O . ASP B 2 154 ? 29.041 15.571 2.891 1.00 14.30 ? 152 ASP B O 1 ATOM 2880 C CB . ASP B 2 154 ? 27.996 17.906 3.874 1.00 18.70 ? 152 ASP B CB 1 ATOM 2881 C CG . ASP B 2 154 ? 26.646 17.291 3.523 1.00 23.42 ? 152 ASP B CG 1 ATOM 2882 O OD1 . ASP B 2 154 ? 26.394 17.034 2.323 1.00 14.54 ? 152 ASP B OD1 1 ATOM 2883 O OD2 . ASP B 2 154 ? 25.834 17.069 4.444 1.00 24.01 ? 152 ASP B OD2 1 ATOM 2884 N N . TRP B 2 155 ? 29.511 16.446 0.857 1.00 13.21 ? 153 TRP B N 1 ATOM 2885 C CA . TRP B 2 155 ? 29.726 15.160 0.186 1.00 13.10 ? 153 TRP B CA 1 ATOM 2886 C C . TRP B 2 155 ? 28.444 14.337 0.063 1.00 12.93 ? 153 TRP B C 1 ATOM 2887 O O . TRP B 2 155 ? 28.481 13.107 0.003 1.00 13.15 ? 153 TRP B O 1 ATOM 2888 C CB . TRP B 2 155 ? 30.850 14.346 0.844 1.00 13.66 ? 153 TRP B CB 1 ATOM 2889 C CG . TRP B 2 155 ? 32.196 14.955 0.619 1.00 14.00 ? 153 TRP B CG 1 ATOM 2890 C CD1 . TRP B 2 155 ? 32.726 16.035 1.258 1.00 14.68 ? 153 TRP B CD1 1 ATOM 2891 C CD2 . TRP B 2 155 ? 33.182 14.519 -0.322 1.00 14.09 ? 153 TRP B CD2 1 ATOM 2892 N NE1 . TRP B 2 155 ? 33.988 16.305 0.768 1.00 15.16 ? 153 TRP B NE1 1 ATOM 2893 C CE2 . TRP B 2 155 ? 34.291 15.380 -0.198 1.00 14.48 ? 153 TRP B CE2 1 ATOM 2894 C CE3 . TRP B 2 155 ? 33.233 13.483 -1.258 1.00 14.14 ? 153 TRP B CE3 1 ATOM 2895 C CZ2 . TRP B 2 155 ? 35.439 15.234 -0.969 1.00 15.48 ? 153 TRP B CZ2 1 ATOM 2896 C CZ3 . TRP B 2 155 ? 34.375 13.338 -2.022 1.00 14.61 ? 153 TRP B CZ3 1 ATOM 2897 C CH2 . TRP B 2 155 ? 35.462 14.209 -1.875 1.00 15.00 ? 153 TRP B CH2 1 ATOM 2898 N N . THR B 2 156 ? 27.310 15.027 0.024 1.00 12.69 ? 154 THR B N 1 ATOM 2899 C CA . THR B 2 156 ? 26.047 14.383 -0.328 1.00 12.56 ? 154 THR B CA 1 ATOM 2900 C C . THR B 2 156 ? 25.278 15.272 -1.299 1.00 12.13 ? 154 THR B C 1 ATOM 2901 O O . THR B 2 156 ? 25.495 16.482 -1.347 1.00 13.65 ? 154 THR B O 1 ATOM 2902 C CB . THR B 2 156 ? 25.146 14.091 0.891 1.00 15.54 ? 154 THR B CB 1 ATOM 2903 O OG1 . THR B 2 156 ? 24.677 15.318 1.465 1.00 15.42 ? 154 THR B OG1 1 ATOM 2904 C CG2 . THR B 2 156 ? 25.884 13.280 1.945 1.00 17.84 ? 154 THR B CG2 1 ATOM 2905 N N . PHE B 2 157 ? 24.380 14.660 -2.063 1.00 11.99 ? 155 PHE B N 1 ATOM 2906 C CA . PHE B 2 157 ? 23.513 15.385 -2.985 1.00 11.70 ? 155 PHE B CA 1 ATOM 2907 C C . PHE B 2 157 ? 22.058 15.156 -2.628 1.00 11.89 ? 155 PHE B C 1 ATOM 2908 O O . PHE B 2 157 ? 21.733 14.262 -1.859 1.00 12.28 ? 155 PHE B O 1 ATOM 2909 C CB . PHE B 2 157 ? 23.697 14.870 -4.411 1.00 11.53 ? 155 PHE B CB 1 ATOM 2910 C CG . PHE B 2 157 ? 25.046 15.169 -5.008 1.00 11.52 ? 155 PHE B CG 1 ATOM 2911 C CD1 . PHE B 2 157 ? 26.106 14.293 -4.841 1.00 14.40 ? 155 PHE B CD1 1 ATOM 2912 C CD2 . PHE B 2 157 ? 25.237 16.312 -5.756 1.00 11.44 ? 155 PHE B CD2 1 ATOM 2913 C CE1 . PHE B 2 157 ? 27.342 14.564 -5.408 1.00 15.76 ? 155 PHE B CE1 1 ATOM 2914 C CE2 . PHE B 2 157 ? 26.469 16.591 -6.321 1.00 14.37 ? 155 PHE B CE2 1 ATOM 2915 C CZ . PHE B 2 157 ? 27.519 15.716 -6.142 1.00 15.50 ? 155 PHE B CZ 1 ATOM 2916 N N . GLN B 2 158 ? 21.179 15.958 -3.214 1.00 11.78 ? 156 GLN B N 1 ATOM 2917 C CA . GLN B 2 158 ? 19.760 15.644 -3.179 1.00 12.04 ? 156 GLN B CA 1 ATOM 2918 C C . GLN B 2 158 ? 19.119 16.094 -4.482 1.00 11.83 ? 156 GLN B C 1 ATOM 2919 O O . GLN B 2 158 ? 19.717 16.842 -5.248 1.00 11.56 ? 156 GLN B O 1 ATOM 2920 C CB . GLN B 2 158 ? 19.073 16.302 -1.983 1.00 12.53 ? 156 GLN B CB 1 ATOM 2921 C CG . GLN B 2 158 ? 19.170 17.815 -2.005 1.00 12.51 ? 156 GLN B CG 1 ATOM 2922 C CD . GLN B 2 158 ? 18.321 18.446 -0.935 1.00 18.74 ? 156 GLN B CD 1 ATOM 2923 O OE1 . GLN B 2 158 ? 17.092 18.396 -1.004 1.00 22.86 ? 156 GLN B OE1 1 ATOM 2924 N NE2 . GLN B 2 158 ? 18.960 19.027 0.073 1.00 15.64 ? 156 GLN B NE2 1 ATOM 2925 N N . THR B 2 159 ? 17.919 15.601 -4.754 1.00 12.09 ? 157 THR B N 1 ATOM 2926 C CA . THR B 2 159 ? 17.134 16.117 -5.869 1.00 12.06 ? 157 THR B CA 1 ATOM 2927 C C . THR B 2 159 ? 15.659 15.854 -5.591 1.00 12.58 ? 157 THR B C 1 ATOM 2928 O O . THR B 2 159 ? 15.317 14.845 -4.973 1.00 14.36 ? 157 THR B O 1 ATOM 2929 C CB . THR B 2 159 ? 17.537 15.473 -7.210 1.00 11.89 ? 157 THR B CB 1 ATOM 2930 O OG1 . THR B 2 159 ? 16.762 16.055 -8.267 1.00 15.10 ? 157 THR B OG1 1 ATOM 2931 C CG2 . THR B 2 159 ? 17.309 13.957 -7.187 1.00 12.95 ? 157 THR B CG2 1 ATOM 2932 N N . LEU B 2 160 ? 14.791 16.774 -6.011 1.00 12.76 ? 158 LEU B N 1 ATOM 2933 C CA . LEU B 2 160 ? 13.348 16.548 -5.946 1.00 13.38 ? 158 LEU B CA 1 ATOM 2934 C C . LEU B 2 160 ? 12.857 16.373 -7.367 1.00 14.11 ? 158 LEU B C 1 ATOM 2935 O O . LEU B 2 160 ? 13.176 17.184 -8.235 1.00 13.10 ? 158 LEU B O 1 ATOM 2936 C CB . LEU B 2 160 ? 12.607 17.741 -5.330 1.00 15.21 ? 158 LEU B CB 1 ATOM 2937 C CG . LEU B 2 160 ? 13.019 18.247 -3.953 1.00 30.60 ? 158 LEU B CG 1 ATOM 2938 C CD1 . LEU B 2 160 ? 11.937 19.145 -3.371 1.00 29.82 ? 158 LEU B CD1 1 ATOM 2939 C CD2 . LEU B 2 160 ? 13.280 17.084 -3.059 1.00 30.13 ? 158 LEU B CD2 1 ATOM 2940 N N . VAL B 2 161 ? 12.082 15.321 -7.606 1.00 13.78 ? 159 VAL B N 1 ATOM 2941 C CA . VAL B 2 161 ? 11.520 15.078 -8.925 1.00 13.96 ? 159 VAL B CA 1 ATOM 2942 C C . VAL B 2 161 ? 10.008 15.012 -8.772 1.00 14.76 ? 159 VAL B C 1 ATOM 2943 O O . VAL B 2 161 ? 9.481 14.098 -8.136 1.00 15.99 ? 159 VAL B O 1 ATOM 2944 C CB . VAL B 2 161 ? 12.060 13.784 -9.549 1.00 13.95 ? 159 VAL B CB 1 ATOM 2945 C CG1 . VAL B 2 161 ? 11.452 13.560 -10.917 1.00 18.85 ? 159 VAL B CG1 1 ATOM 2946 C CG2 . VAL B 2 161 ? 13.584 13.853 -9.640 1.00 13.32 ? 159 VAL B CG2 1 ATOM 2947 N N . MET B 2 162 ? 9.323 15.997 -9.345 1.00 14.98 ? 160 MET B N 1 ATOM 2948 C CA A MET B 2 162 ? 7.878 16.168 -9.173 0.53 15.86 ? 160 MET B CA 1 ATOM 2949 C CA B MET B 2 162 ? 7.887 16.107 -9.151 0.47 17.42 ? 160 MET B CA 1 ATOM 2950 C C . MET B 2 162 ? 7.084 15.647 -10.362 1.00 18.59 ? 160 MET B C 1 ATOM 2951 O O . MET B 2 162 ? 7.483 15.840 -11.507 1.00 21.34 ? 160 MET B O 1 ATOM 2952 C CB A MET B 2 162 ? 7.537 17.649 -8.997 0.53 16.05 ? 160 MET B CB 1 ATOM 2953 C CB B MET B 2 162 ? 7.535 17.539 -8.764 0.47 20.43 ? 160 MET B CB 1 ATOM 2954 C CG A MET B 2 162 ? 7.678 18.187 -7.588 0.53 29.33 ? 160 MET B CG 1 ATOM 2955 C CG B MET B 2 162 ? 8.232 17.978 -7.489 0.47 22.87 ? 160 MET B CG 1 ATOM 2956 S SD A MET B 2 162 ? 9.383 18.329 -7.033 0.53 26.52 ? 160 MET B SD 1 ATOM 2957 S SD B MET B 2 162 ? 8.292 19.764 -7.292 0.47 24.67 ? 160 MET B SD 1 ATOM 2958 C CE A MET B 2 162 ? 10.050 19.524 -8.190 0.53 16.15 ? 160 MET B CE 1 ATOM 2959 C CE B MET B 2 162 ? 8.854 19.907 -5.596 0.47 29.00 ? 160 MET B CE 1 ATOM 2960 N N . LEU B 2 163 ? 5.944 15.017 -10.088 1.00 17.24 ? 161 LEU B N 1 ATOM 2961 C CA . LEU B 2 163 ? 5.051 14.573 -11.143 1.00 17.91 ? 161 LEU B CA 1 ATOM 2962 C C . LEU B 2 163 ? 3.734 15.327 -11.014 1.00 18.81 ? 161 LEU B C 1 ATOM 2963 O O . LEU B 2 163 ? 3.071 15.226 -9.986 1.00 19.49 ? 161 LEU B O 1 ATOM 2964 C CB . LEU B 2 163 ? 4.781 13.070 -11.026 1.00 18.48 ? 161 LEU B CB 1 ATOM 2965 C CG . LEU B 2 163 ? 3.747 12.514 -12.007 1.00 19.44 ? 161 LEU B CG 1 ATOM 2966 C CD1 . LEU B 2 163 ? 4.231 12.629 -13.448 1.00 19.12 ? 161 LEU B CD1 1 ATOM 2967 C CD2 . LEU B 2 163 ? 3.397 11.071 -11.670 1.00 20.26 ? 161 LEU B CD2 1 ATOM 2968 N N . GLU B 2 164 ? 3.373 16.088 -12.044 1.00 18.96 ? 162 GLU B N 1 ATOM 2969 C CA . GLU B 2 164 ? 2.066 16.750 -12.094 1.00 20.00 ? 162 GLU B CA 1 ATOM 2970 C C . GLU B 2 164 ? 1.027 15.731 -12.535 1.00 21.01 ? 162 GLU B C 1 ATOM 2971 O O . GLU B 2 164 ? 1.117 15.191 -13.634 1.00 22.48 ? 162 GLU B O 1 ATOM 2972 C CB . GLU B 2 164 ? 2.095 17.909 -13.086 1.00 19.94 ? 162 GLU B CB 1 ATOM 2973 C CG . GLU B 2 164 ? 3.168 18.944 -12.792 1.00 19.09 ? 162 GLU B CG 1 ATOM 2974 C CD . GLU B 2 164 ? 3.428 19.873 -13.967 1.00 43.32 ? 162 GLU B CD 1 ATOM 2975 O OE1 . GLU B 2 164 ? 2.826 19.662 -15.041 1.00 47.86 ? 162 GLU B OE1 1 ATOM 2976 O OE2 . GLU B 2 164 ? 4.237 20.812 -13.814 1.00 39.55 ? 162 GLU B OE2 1 ATOM 2977 N N . THR B 2 165 ? 0.036 15.478 -11.686 1.00 22.03 ? 163 THR B N 1 ATOM 2978 C CA . THR B 2 165 ? -0.940 14.433 -11.958 1.00 23.16 ? 163 THR B CA 1 ATOM 2979 C C . THR B 2 165 ? -2.162 14.658 -11.090 1.00 24.52 ? 163 THR B C 1 ATOM 2980 O O . THR B 2 165 ? -2.070 15.275 -10.034 1.00 24.54 ? 163 THR B O 1 ATOM 2981 C CB . THR B 2 165 ? -0.333 13.025 -11.669 1.00 22.93 ? 163 THR B CB 1 ATOM 2982 O OG1 . THR B 2 165 ? -1.223 11.997 -12.116 1.00 26.06 ? 163 THR B OG1 1 ATOM 2983 C CG2 . THR B 2 165 ? -0.071 12.852 -10.190 1.00 22.94 ? 163 THR B CG2 1 ATOM 2984 N N . VAL B 2 166 ? -3.315 14.188 -11.554 1.00 25.82 ? 164 VAL B N 1 ATOM 2985 C CA . VAL B 2 166 ? -4.515 14.193 -10.732 1.00 27.40 ? 164 VAL B CA 1 ATOM 2986 C C . VAL B 2 166 ? -4.782 12.755 -10.304 1.00 28.24 ? 164 VAL B C 1 ATOM 2987 O O . VAL B 2 166 ? -5.288 11.955 -11.088 1.00 28.94 ? 164 VAL B O 1 ATOM 2988 C CB . VAL B 2 166 ? -5.733 14.739 -11.489 1.00 28.61 ? 164 VAL B CB 1 ATOM 2989 C CG1 . VAL B 2 166 ? -6.940 14.794 -10.564 1.00 30.41 ? 164 VAL B CG1 1 ATOM 2990 C CG2 . VAL B 2 166 ? -5.436 16.120 -12.042 1.00 27.91 ? 164 VAL B CG2 1 ATOM 2991 N N . PRO B 2 167 ? -4.428 12.421 -9.057 1.00 28.31 ? 165 PRO B N 1 ATOM 2992 C CA . PRO B 2 167 ? -4.575 11.044 -8.573 1.00 29.19 ? 165 PRO B CA 1 ATOM 2993 C C . PRO B 2 167 ? -6.025 10.587 -8.549 1.00 34.09 ? 165 PRO B C 1 ATOM 2994 O O . PRO B 2 167 ? -6.912 11.328 -8.120 1.00 32.36 ? 165 PRO B O 1 ATOM 2995 C CB . PRO B 2 167 ? -4.018 11.113 -7.148 1.00 30.29 ? 165 PRO B CB 1 ATOM 2996 C CG . PRO B 2 167 ? -3.087 12.286 -7.160 1.00 27.76 ? 165 PRO B CG 1 ATOM 2997 C CD . PRO B 2 167 ? -3.774 13.286 -8.061 1.00 27.61 ? 165 PRO B CD 1 ATOM 2998 N N . ARG B 2 168 ? -6.257 9.369 -9.024 1.00 32.00 ? 166 ARG B N 1 ATOM 2999 C CA . ARG B 2 168 ? -7.580 8.774 -8.980 1.00 34.15 ? 166 ARG B CA 1 ATOM 3000 C C . ARG B 2 168 ? -7.547 7.613 -8.002 1.00 35.24 ? 166 ARG B C 1 ATOM 3001 O O . ARG B 2 168 ? -6.511 6.969 -7.836 1.00 36.42 ? 166 ARG B O 1 ATOM 3002 C CB . ARG B 2 168 ? -8.001 8.307 -10.374 1.00 44.00 ? 166 ARG B CB 1 ATOM 3003 C CG . ARG B 2 168 ? -8.445 9.440 -11.298 1.00 43.83 ? 166 ARG B CG 1 ATOM 3004 C CD . ARG B 2 168 ? -8.638 8.938 -12.716 1.00 47.03 ? 166 ARG B CD 1 ATOM 3005 N NE . ARG B 2 168 ? -9.399 9.863 -13.555 1.00 36.63 ? 166 ARG B NE 1 ATOM 3006 C CZ . ARG B 2 168 ? -8.867 10.894 -14.201 1.00 33.51 ? 166 ARG B CZ 1 ATOM 3007 N NH1 . ARG B 2 168 ? -7.571 11.151 -14.091 1.00 31.69 ? 166 ARG B NH1 1 ATOM 3008 N NH2 . ARG B 2 168 ? -9.628 11.671 -14.954 1.00 34.15 ? 166 ARG B NH2 1 ATOM 3009 N N . SER B 2 169 ? -8.673 7.367 -7.341 1.00 37.37 ? 167 SER B N 1 ATOM 3010 C CA . SER B 2 169 ? -8.786 6.278 -6.381 1.00 38.84 ? 167 SER B CA 1 ATOM 3011 C C . SER B 2 169 ? -8.348 4.958 -7.002 1.00 38.83 ? 167 SER B C 1 ATOM 3012 O O . SER B 2 169 ? -8.740 4.624 -8.119 1.00 49.96 ? 167 SER B O 1 ATOM 3013 C CB . SER B 2 169 ? -10.225 6.166 -5.882 1.00 48.04 ? 167 SER B CB 1 ATOM 3014 O OG . SER B 2 169 ? -11.112 5.959 -6.967 1.00 58.65 ? 167 SER B OG 1 ATOM 3015 N N . GLY B 2 170 ? -7.510 4.224 -6.283 1.00 38.62 ? 168 GLY B N 1 ATOM 3016 C CA . GLY B 2 170 ? -7.037 2.939 -6.760 1.00 41.82 ? 168 GLY B CA 1 ATOM 3017 C C . GLY B 2 170 ? -5.640 2.992 -7.348 1.00 41.27 ? 168 GLY B C 1 ATOM 3018 O O . GLY B 2 170 ? -4.901 2.015 -7.272 1.00 36.52 ? 168 GLY B O 1 ATOM 3019 N N . GLU B 2 171 ? -5.279 4.133 -7.930 1.00 38.84 ? 169 GLU B N 1 ATOM 3020 C CA . GLU B 2 171 ? -3.976 4.291 -8.574 1.00 34.18 ? 169 GLU B CA 1 ATOM 3021 C C . GLU B 2 171 ? -2.809 4.113 -7.608 1.00 31.81 ? 169 GLU B C 1 ATOM 3022 O O . GLU B 2 171 ? -2.860 4.553 -6.458 1.00 36.98 ? 169 GLU B O 1 ATOM 3023 C CB . GLU B 2 171 ? -3.864 5.669 -9.236 1.00 32.04 ? 169 GLU B CB 1 ATOM 3024 C CG . GLU B 2 171 ? -4.659 5.843 -10.522 1.00 31.74 ? 169 GLU B CG 1 ATOM 3025 C CD . GLU B 2 171 ? -4.512 7.242 -11.085 1.00 30.69 ? 169 GLU B CD 1 ATOM 3026 O OE1 . GLU B 2 171 ? -4.141 8.147 -10.311 1.00 31.56 ? 169 GLU B OE1 1 ATOM 3027 O OE2 . GLU B 2 171 ? -4.755 7.442 -12.295 1.00 39.37 ? 169 GLU B OE2 1 ATOM 3028 N N . VAL B 2 172 ? -1.756 3.462 -8.085 1.00 30.97 ? 170 VAL B N 1 ATOM 3029 C CA . VAL B 2 172 ? -0.512 3.394 -7.337 1.00 29.89 ? 170 VAL B CA 1 ATOM 3030 C C . VAL B 2 172 ? 0.597 4.032 -8.159 1.00 28.32 ? 170 VAL B C 1 ATOM 3031 O O . VAL B 2 172 ? 0.840 3.650 -9.304 1.00 27.69 ? 170 VAL B O 1 ATOM 3032 C CB . VAL B 2 172 ? -0.124 1.947 -6.969 1.00 30.97 ? 170 VAL B CB 1 ATOM 3033 C CG1 . VAL B 2 172 ? 1.266 1.914 -6.350 1.00 33.20 ? 170 VAL B CG1 1 ATOM 3034 C CG2 . VAL B 2 172 ? -1.153 1.351 -6.019 1.00 34.46 ? 170 VAL B CG2 1 ATOM 3035 N N . TYR B 2 173 ? 1.259 5.019 -7.571 1.00 26.58 ? 171 TYR B N 1 ATOM 3036 C CA . TYR B 2 173 ? 2.366 5.681 -8.233 1.00 26.96 ? 171 TYR B CA 1 ATOM 3037 C C . TYR B 2 173 ? 3.661 5.155 -7.643 1.00 25.45 ? 171 TYR B C 1 ATOM 3038 O O . TYR B 2 173 ? 3.715 4.817 -6.460 1.00 26.57 ? 171 TYR B O 1 ATOM 3039 C CB . TYR B 2 173 ? 2.271 7.187 -8.031 1.00 23.88 ? 171 TYR B CB 1 ATOM 3040 C CG . TYR B 2 173 ? 1.120 7.839 -8.761 1.00 24.39 ? 171 TYR B CG 1 ATOM 3041 C CD1 . TYR B 2 173 ? -0.172 7.796 -8.248 1.00 25.88 ? 171 TYR B CD1 1 ATOM 3042 C CD2 . TYR B 2 173 ? 1.327 8.510 -9.958 1.00 23.61 ? 171 TYR B CD2 1 ATOM 3043 C CE1 . TYR B 2 173 ? -1.226 8.403 -8.917 1.00 26.45 ? 171 TYR B CE1 1 ATOM 3044 C CE2 . TYR B 2 173 ? 0.284 9.123 -10.629 1.00 24.54 ? 171 TYR B CE2 1 ATOM 3045 C CZ . TYR B 2 173 ? -0.989 9.062 -10.106 1.00 25.53 ? 171 TYR B CZ 1 ATOM 3046 O OH . TYR B 2 173 ? -2.029 9.675 -10.777 1.00 27.18 ? 171 TYR B OH 1 ATOM 3047 N N . THR B 2 174 ? 4.697 5.076 -8.467 1.00 23.15 ? 172 THR B N 1 ATOM 3048 C CA . THR B 2 174 ? 5.983 4.566 -8.010 1.00 22.61 ? 172 THR B CA 1 ATOM 3049 C C . THR B 2 174 ? 7.093 5.490 -8.478 1.00 20.99 ? 172 THR B C 1 ATOM 3050 O O . THR B 2 174 ? 7.155 5.841 -9.649 1.00 20.56 ? 172 THR B O 1 ATOM 3051 C CB . THR B 2 174 ? 6.250 3.154 -8.549 1.00 23.54 ? 172 THR B CB 1 ATOM 3052 O OG1 . THR B 2 174 ? 5.219 2.270 -8.092 1.00 25.25 ? 172 THR B OG1 1 ATOM 3053 C CG2 . THR B 2 174 ? 7.585 2.633 -8.050 1.00 23.13 ? 172 THR B CG2 1 ATOM 3054 N N . CYS B 2 175 ? 7.953 5.882 -7.550 1.00 20.24 ? 173 CYS B N 1 ATOM 3055 C CA . CYS B 2 175 ? 9.165 6.599 -7.903 1.00 18.89 ? 173 CYS B CA 1 ATOM 3056 C C . CYS B 2 175 ? 10.294 5.591 -7.904 1.00 18.94 ? 173 CYS B C 1 ATOM 3057 O O . CYS B 2 175 ? 10.462 4.859 -6.930 1.00 19.54 ? 173 CYS B O 1 ATOM 3058 C CB . CYS B 2 175 ? 9.465 7.688 -6.882 1.00 18.17 ? 173 CYS B CB 1 ATOM 3059 S SG . CYS B 2 175 ? 10.954 8.609 -7.281 1.00 21.04 ? 173 CYS B SG 1 ATOM 3060 N N . GLN B 2 176 ? 11.060 5.552 -8.990 1.00 18.48 ? 174 GLN B N 1 ATOM 3061 C CA . GLN B 2 176 ? 12.139 4.574 -9.132 1.00 18.72 ? 174 GLN B CA 1 ATOM 3062 C C . GLN B 2 176 ? 13.478 5.275 -9.257 1.00 17.60 ? 174 GLN B C 1 ATOM 3063 O O . GLN B 2 176 ? 13.633 6.183 -10.063 1.00 16.93 ? 174 GLN B O 1 ATOM 3064 C CB . GLN B 2 176 ? 11.908 3.721 -10.372 1.00 20.79 ? 174 GLN B CB 1 ATOM 3065 C CG . GLN B 2 176 ? 12.975 2.665 -10.607 1.00 24.34 ? 174 GLN B CG 1 ATOM 3066 C CD . GLN B 2 176 ? 12.881 2.076 -11.996 1.00 23.85 ? 174 GLN B CD 1 ATOM 3067 O OE1 . GLN B 2 176 ? 13.386 2.652 -12.961 1.00 38.66 ? 174 GLN B OE1 1 ATOM 3068 N NE2 . GLN B 2 176 ? 12.204 0.948 -12.111 1.00 22.99 ? 174 GLN B NE2 1 ATOM 3069 N N . VAL B 2 177 ? 14.455 4.818 -8.483 1.00 17.58 ? 175 VAL B N 1 ATOM 3070 C CA . VAL B 2 177 ? 15.743 5.485 -8.414 1.00 16.64 ? 175 VAL B CA 1 ATOM 3071 C C . VAL B 2 177 ? 16.871 4.521 -8.760 1.00 17.11 ? 175 VAL B C 1 ATOM 3072 O O . VAL B 2 177 ? 16.947 3.422 -8.210 1.00 18.34 ? 175 VAL B O 1 ATOM 3073 C CB . VAL B 2 177 ? 15.967 6.077 -7.012 1.00 16.16 ? 175 VAL B CB 1 ATOM 3074 C CG1 . VAL B 2 177 ? 17.361 6.658 -6.887 1.00 16.84 ? 175 VAL B CG1 1 ATOM 3075 C CG2 . VAL B 2 177 ? 14.901 7.140 -6.708 1.00 15.84 ? 175 VAL B CG2 1 ATOM 3076 N N . GLU B 2 178 ? 17.721 4.927 -9.698 1.00 16.72 ? 176 GLU B N 1 ATOM 3077 C CA . GLU B 2 178 ? 18.925 4.167 -10.041 1.00 17.23 ? 176 GLU B CA 1 ATOM 3078 C C . GLU B 2 178 ? 20.155 5.005 -9.714 1.00 16.38 ? 176 GLU B C 1 ATOM 3079 O O . GLU B 2 178 ? 20.172 6.210 -9.949 1.00 17.27 ? 176 GLU B O 1 ATOM 3080 C CB . GLU B 2 178 ? 18.927 3.796 -11.523 1.00 18.44 ? 176 GLU B CB 1 ATOM 3081 C CG . GLU B 2 178 ? 17.873 2.769 -11.913 1.00 28.39 ? 176 GLU B CG 1 ATOM 3082 C CD . GLU B 2 178 ? 17.615 2.740 -13.410 1.00 40.60 ? 176 GLU B CD 1 ATOM 3083 O OE1 . GLU B 2 178 ? 17.843 1.681 -14.034 1.00 52.55 ? 176 GLU B OE1 1 ATOM 3084 O OE2 . GLU B 2 178 ? 17.180 3.776 -13.961 1.00 46.20 ? 176 GLU B OE2 1 ATOM 3085 N N . HIS B 2 179 ? 21.189 4.358 -9.187 1.00 16.75 ? 177 HIS B N 1 ATOM 3086 C CA . HIS B 2 179 ? 22.331 5.081 -8.638 1.00 16.07 ? 177 HIS B CA 1 ATOM 3087 C C . HIS B 2 179 ? 23.483 4.089 -8.504 1.00 18.02 ? 177 HIS B C 1 ATOM 3088 O O . HIS B 2 179 ? 23.241 2.902 -8.304 1.00 18.52 ? 177 HIS B O 1 ATOM 3089 C CB . HIS B 2 179 ? 21.957 5.669 -7.269 1.00 15.45 ? 177 HIS B CB 1 ATOM 3090 C CG . HIS B 2 179 ? 23.025 6.527 -6.669 1.00 14.81 ? 177 HIS B CG 1 ATOM 3091 N ND1 . HIS B 2 179 ? 23.903 6.063 -5.707 1.00 15.63 ? 177 HIS B ND1 1 ATOM 3092 C CD2 . HIS B 2 179 ? 23.371 7.814 -6.900 1.00 14.74 ? 177 HIS B CD2 1 ATOM 3093 C CE1 . HIS B 2 179 ? 24.741 7.027 -5.381 1.00 19.31 ? 177 HIS B CE1 1 ATOM 3094 N NE2 . HIS B 2 179 ? 24.444 8.102 -6.093 1.00 16.45 ? 177 HIS B NE2 1 ATOM 3095 N N . PRO B 2 180 ? 24.742 4.558 -8.640 1.00 16.68 ? 178 PRO B N 1 ATOM 3096 C CA . PRO B 2 180 ? 25.866 3.608 -8.565 1.00 17.63 ? 178 PRO B CA 1 ATOM 3097 C C . PRO B 2 180 ? 25.970 2.833 -7.248 1.00 19.90 ? 178 PRO B C 1 ATOM 3098 O O . PRO B 2 180 ? 26.587 1.766 -7.220 1.00 22.21 ? 178 PRO B O 1 ATOM 3099 C CB . PRO B 2 180 ? 27.095 4.507 -8.742 1.00 17.21 ? 178 PRO B CB 1 ATOM 3100 C CG . PRO B 2 180 ? 26.589 5.686 -9.506 1.00 17.62 ? 178 PRO B CG 1 ATOM 3101 C CD . PRO B 2 180 ? 25.189 5.907 -9.031 1.00 19.86 ? 178 PRO B CD 1 ATOM 3102 N N . SER B 2 181 ? 25.386 3.356 -6.177 1.00 17.38 ? 179 SER B N 1 ATOM 3103 C CA . SER B 2 181 ? 25.456 2.696 -4.878 1.00 17.92 ? 179 SER B CA 1 ATOM 3104 C C . SER B 2 181 ? 24.481 1.537 -4.793 1.00 19.77 ? 179 SER B C 1 ATOM 3105 O O . SER B 2 181 ? 24.542 0.739 -3.855 1.00 22.08 ? 179 SER B O 1 ATOM 3106 C CB . SER B 2 181 ? 25.126 3.684 -3.765 1.00 23.04 ? 179 SER B CB 1 ATOM 3107 O OG . SER B 2 181 ? 23.769 4.080 -3.863 1.00 18.14 ? 179 SER B OG 1 ATOM 3108 N N . LEU B 2 182 ? 23.570 1.464 -5.760 1.00 18.98 ? 180 LEU B N 1 ATOM 3109 C CA . LEU B 2 182 ? 22.516 0.453 -5.756 1.00 20.16 ? 180 LEU B CA 1 ATOM 3110 C C . LEU B 2 182 ? 22.802 -0.651 -6.764 1.00 26.68 ? 180 LEU B C 1 ATOM 3111 O O . LEU B 2 182 ? 23.372 -0.404 -7.826 1.00 30.06 ? 180 LEU B O 1 ATOM 3112 C CB . LEU B 2 182 ? 21.170 1.095 -6.082 1.00 19.43 ? 180 LEU B CB 1 ATOM 3113 C CG . LEU B 2 182 ? 20.733 2.253 -5.182 1.00 18.38 ? 180 LEU B CG 1 ATOM 3114 C CD1 . LEU B 2 182 ? 19.485 2.911 -5.730 1.00 17.93 ? 180 LEU B CD1 1 ATOM 3115 C CD2 . LEU B 2 182 ? 20.503 1.760 -3.753 1.00 20.40 ? 180 LEU B CD2 1 ATOM 3116 N N . THR B 2 183 ? 22.388 -1.866 -6.428 1.00 23.54 ? 181 THR B N 1 ATOM 3117 C CA . THR B 2 183 ? 22.587 -3.014 -7.303 1.00 24.14 ? 181 THR B CA 1 ATOM 3118 C C . THR B 2 183 ? 21.314 -3.334 -8.080 1.00 27.16 ? 181 THR B C 1 ATOM 3119 O O . THR B 2 183 ? 21.323 -4.151 -8.998 1.00 28.61 ? 181 THR B O 1 ATOM 3120 C CB . THR B 2 183 ? 23.018 -4.249 -6.497 1.00 25.68 ? 181 THR B CB 1 ATOM 3121 O OG1 . THR B 2 183 ? 22.141 -4.404 -5.377 1.00 26.31 ? 181 THR B OG1 1 ATOM 3122 C CG2 . THR B 2 183 ? 24.439 -4.074 -5.985 1.00 31.56 ? 181 THR B CG2 1 ATOM 3123 N N . SER B 2 184 ? 20.220 -2.688 -7.693 1.00 23.90 ? 182 SER B N 1 ATOM 3124 C CA . SER B 2 184 ? 18.949 -2.803 -8.397 1.00 24.28 ? 182 SER B CA 1 ATOM 3125 C C . SER B 2 184 ? 18.158 -1.539 -8.060 1.00 23.34 ? 182 SER B C 1 ATOM 3126 O O . SER B 2 184 ? 18.468 -0.874 -7.071 1.00 23.17 ? 182 SER B O 1 ATOM 3127 C CB . SER B 2 184 ? 18.202 -4.072 -7.966 1.00 27.35 ? 182 SER B CB 1 ATOM 3128 O OG . SER B 2 184 ? 17.780 -3.986 -6.620 1.00 36.89 ? 182 SER B OG 1 ATOM 3129 N N . PRO B 2 185 ? 17.158 -1.183 -8.888 1.00 22.70 ? 183 PRO B N 1 ATOM 3130 C CA . PRO B 2 185 ? 16.432 0.069 -8.644 1.00 21.44 ? 183 PRO B CA 1 ATOM 3131 C C . PRO B 2 185 ? 15.751 0.101 -7.283 1.00 21.58 ? 183 PRO B C 1 ATOM 3132 O O . PRO B 2 185 ? 15.226 -0.916 -6.816 1.00 23.85 ? 183 PRO B O 1 ATOM 3133 C CB . PRO B 2 185 ? 15.373 0.081 -9.750 1.00 27.85 ? 183 PRO B CB 1 ATOM 3134 C CG . PRO B 2 185 ? 15.942 -0.755 -10.833 1.00 28.52 ? 183 PRO B CG 1 ATOM 3135 C CD . PRO B 2 185 ? 16.714 -1.840 -10.132 1.00 26.97 ? 183 PRO B CD 1 ATOM 3136 N N . LEU B 2 186 ? 15.775 1.268 -6.656 1.00 20.38 ? 184 LEU B N 1 ATOM 3137 C CA . LEU B 2 186 ? 15.088 1.494 -5.402 1.00 20.56 ? 184 LEU B CA 1 ATOM 3138 C C . LEU B 2 186 ? 13.732 2.095 -5.743 1.00 20.48 ? 184 LEU B C 1 ATOM 3139 O O . LEU B 2 186 ? 13.656 3.083 -6.469 1.00 21.96 ? 184 LEU B O 1 ATOM 3140 C CB . LEU B 2 186 ? 15.910 2.453 -4.538 1.00 24.19 ? 184 LEU B CB 1 ATOM 3141 C CG . LEU B 2 186 ? 15.382 2.876 -3.170 1.00 34.85 ? 184 LEU B CG 1 ATOM 3142 C CD1 . LEU B 2 186 ? 14.974 1.663 -2.360 1.00 39.65 ? 184 LEU B CD1 1 ATOM 3143 C CD2 . LEU B 2 186 ? 16.449 3.680 -2.432 1.00 30.79 ? 184 LEU B CD2 1 ATOM 3144 N N . THR B 2 187 ? 12.660 1.480 -5.256 1.00 21.70 ? 185 THR B N 1 ATOM 3145 C CA . THR B 2 187 ? 11.327 1.983 -5.561 1.00 21.86 ? 185 THR B CA 1 ATOM 3146 C C . THR B 2 187 ? 10.558 2.326 -4.299 1.00 28.73 ? 185 THR B C 1 ATOM 3147 O O . THR B 2 187 ? 10.672 1.637 -3.278 1.00 24.28 ? 185 THR B O 1 ATOM 3148 C CB . THR B 2 187 ? 10.509 0.980 -6.393 1.00 23.16 ? 185 THR B CB 1 ATOM 3149 O OG1 . THR B 2 187 ? 10.404 -0.257 -5.680 1.00 28.65 ? 185 THR B OG1 1 ATOM 3150 C CG2 . THR B 2 187 ? 11.182 0.730 -7.735 1.00 28.07 ? 185 THR B CG2 1 ATOM 3151 N N . VAL B 2 188 ? 9.782 3.403 -4.383 1.00 21.85 ? 186 VAL B N 1 ATOM 3152 C CA . VAL B 2 188 ? 8.878 3.811 -3.321 1.00 22.56 ? 186 VAL B CA 1 ATOM 3153 C C . VAL B 2 188 ? 7.497 4.055 -3.921 1.00 23.14 ? 186 VAL B C 1 ATOM 3154 O O . VAL B 2 188 ? 7.359 4.797 -4.895 1.00 22.24 ? 186 VAL B O 1 ATOM 3155 C CB . VAL B 2 188 ? 9.369 5.093 -2.609 1.00 21.97 ? 186 VAL B CB 1 ATOM 3156 C CG1 . VAL B 2 188 ? 8.296 5.629 -1.663 1.00 22.56 ? 186 VAL B CG1 1 ATOM 3157 C CG2 . VAL B 2 188 ? 10.664 4.829 -1.866 1.00 23.39 ? 186 VAL B CG2 1 ATOM 3158 N N . GLU B 2 189 ? 6.482 3.412 -3.349 1.00 24.77 ? 187 GLU B N 1 ATOM 3159 C CA . GLU B 2 189 ? 5.114 3.561 -3.828 1.00 26.79 ? 187 GLU B CA 1 ATOM 3160 C C . GLU B 2 189 ? 4.341 4.605 -3.039 1.00 29.06 ? 187 GLU B C 1 ATOM 3161 O O . GLU B 2 189 ? 4.628 4.868 -1.870 1.00 26.94 ? 187 GLU B O 1 ATOM 3162 C CB . GLU B 2 189 ? 4.365 2.225 -3.756 1.00 32.29 ? 187 GLU B CB 1 ATOM 3163 C CG . GLU B 2 189 ? 4.911 1.151 -4.678 1.00 32.54 ? 187 GLU B CG 1 ATOM 3164 C CD . GLU B 2 189 ? 4.148 -0.154 -4.562 1.00 41.26 ? 187 GLU B CD 1 ATOM 3165 O OE1 . GLU B 2 189 ? 4.365 -1.048 -5.405 1.00 43.63 ? 187 GLU B OE1 1 ATOM 3166 O OE2 . GLU B 2 189 ? 3.329 -0.283 -3.627 1.00 38.76 ? 187 GLU B OE2 1 ATOM 3167 N N . TRP B 2 190 ? 3.357 5.200 -3.702 1.00 25.99 ? 188 TRP B N 1 ATOM 3168 C CA . TRP B 2 190 ? 2.411 6.095 -3.062 1.00 26.65 ? 188 TRP B CA 1 ATOM 3169 C C . TRP B 2 190 ? 1.039 5.756 -3.616 1.00 28.03 ? 188 TRP B C 1 ATOM 3170 O O . TRP B 2 190 ? 0.865 5.647 -4.831 1.00 27.64 ? 188 TRP B O 1 ATOM 3171 C CB . TRP B 2 190 ? 2.759 7.556 -3.369 1.00 25.15 ? 188 TRP B CB 1 ATOM 3172 C CG . TRP B 2 190 ? 1.817 8.536 -2.743 1.00 25.94 ? 188 TRP B CG 1 ATOM 3173 C CD1 . TRP B 2 190 ? 1.921 9.097 -1.502 1.00 29.37 ? 188 TRP B CD1 1 ATOM 3174 C CD2 . TRP B 2 190 ? 0.627 9.076 -3.330 1.00 26.58 ? 188 TRP B CD2 1 ATOM 3175 N NE1 . TRP B 2 190 ? 0.871 9.953 -1.281 1.00 28.71 ? 188 TRP B NE1 1 ATOM 3176 C CE2 . TRP B 2 190 ? 0.058 9.955 -2.385 1.00 31.14 ? 188 TRP B CE2 1 ATOM 3177 C CE3 . TRP B 2 190 ? -0.016 8.898 -4.557 1.00 26.67 ? 188 TRP B CE3 1 ATOM 3178 C CZ2 . TRP B 2 190 ? -1.119 10.659 -2.633 1.00 30.41 ? 188 TRP B CZ2 1 ATOM 3179 C CZ3 . TRP B 2 190 ? -1.188 9.593 -4.799 1.00 27.52 ? 188 TRP B CZ3 1 ATOM 3180 C CH2 . TRP B 2 190 ? -1.726 10.463 -3.843 1.00 28.35 ? 188 TRP B CH2 1 ATOM 3181 N N . ARG B 2 191 ? 0.069 5.565 -2.727 1.00 29.84 ? 189 ARG B N 1 ATOM 3182 C CA . ARG B 2 191 ? -1.279 5.230 -3.156 1.00 34.56 ? 189 ARG B CA 1 ATOM 3183 C C . ARG B 2 191 ? -2.257 6.340 -2.808 1.00 32.05 ? 189 ARG B C 1 ATOM 3184 O O . ARG B 2 191 ? -2.188 6.920 -1.727 1.00 38.70 ? 189 ARG B O 1 ATOM 3185 C CB . ARG B 2 191 ? -1.740 3.919 -2.514 1.00 34.92 ? 189 ARG B CB 1 ATOM 3186 N N . ALA B 2 192 ? -3.153 6.641 -3.740 1.00 34.52 ? 190 ALA B N 1 ATOM 3187 C CA . ALA B 2 192 ? -4.280 7.512 -3.457 1.00 43.55 ? 190 ALA B CA 1 ATOM 3188 C C . ALA B 2 192 ? -5.337 6.669 -2.752 1.00 43.01 ? 190 ALA B C 1 ATOM 3189 O O . ALA B 2 192 ? -5.696 5.596 -3.239 1.00 43.16 ? 190 ALA B O 1 ATOM 3190 C CB . ALA B 2 192 ? -4.833 8.099 -4.743 1.00 46.16 ? 190 ALA B CB 1 ATOM 3191 N N . THR B 2 193 ? -5.840 7.136 -1.612 1.00 61.04 ? 191 THR B N 1 ATOM 3192 C CA . THR B 2 193 ? -5.494 8.436 -1.048 1.00 57.86 ? 191 THR B CA 1 ATOM 3193 C C . THR B 2 193 ? -4.250 8.354 -0.168 1.00 60.58 ? 191 THR B C 1 ATOM 3194 O O . THR B 2 193 ? -3.319 9.150 -0.311 1.00 59.98 ? 191 THR B O 1 ATOM 3195 C CB . THR B 2 193 ? -6.650 8.974 -0.186 1.00 64.79 ? 191 THR B CB 1 ATOM 3196 O OG1 . THR B 2 193 ? -6.667 8.287 1.072 1.00 68.25 ? 191 THR B OG1 1 ATOM 3197 C CG2 . THR B 2 193 ? -7.987 8.767 -0.890 1.00 58.70 ? 191 THR B CG2 1 ATOM 3198 N N . SER C 3 1 ? 48.909 8.107 4.542 1.00 35.92 ? 1 SER C N 1 ATOM 3199 C CA . SER C 3 1 ? 49.641 8.554 3.364 1.00 30.08 ? 1 SER C CA 1 ATOM 3200 C C . SER C 3 1 ? 49.459 10.056 3.164 1.00 26.58 ? 1 SER C C 1 ATOM 3201 O O . SER C 3 1 ? 48.386 10.600 3.420 1.00 27.43 ? 1 SER C O 1 ATOM 3202 C CB . SER C 3 1 ? 49.168 7.792 2.127 1.00 42.18 ? 1 SER C CB 1 ATOM 3203 O OG . SER C 3 1 ? 50.111 7.898 1.077 1.00 53.90 ? 1 SER C OG 1 ATOM 3204 N N . ALA C 3 2 ? 50.510 10.721 2.694 1.00 22.34 ? 2 ALA C N 1 ATOM 3205 C CA . ALA C 3 2 ? 50.511 12.178 2.605 1.00 19.44 ? 2 ALA C CA 1 ATOM 3206 C C . ALA C 3 2 ? 50.116 12.710 1.231 1.00 19.53 ? 2 ALA C C 1 ATOM 3207 O O . ALA C 3 2 ? 50.644 12.278 0.208 1.00 20.65 ? 2 ALA C O 1 ATOM 3208 C CB . ALA C 3 2 ? 51.876 12.724 3.009 1.00 25.33 ? 2 ALA C CB 1 ATOM 3209 N N . VAL C 3 3 ? 49.176 13.653 1.220 1.00 16.70 ? 3 VAL C N 1 ATOM 3210 C CA . VAL C 3 3 ? 48.854 14.399 0.013 1.00 15.47 ? 3 VAL C CA 1 ATOM 3211 C C . VAL C 3 3 ? 50.009 15.344 -0.284 1.00 16.16 ? 3 VAL C C 1 ATOM 3212 O O . VAL C 3 3 ? 50.535 15.979 0.627 1.00 18.16 ? 3 VAL C O 1 ATOM 3213 C CB . VAL C 3 3 ? 47.556 15.206 0.199 1.00 14.67 ? 3 VAL C CB 1 ATOM 3214 C CG1 . VAL C 3 3 ? 47.323 16.156 -0.975 1.00 15.51 ? 3 VAL C CG1 1 ATOM 3215 C CG2 . VAL C 3 3 ? 46.389 14.256 0.351 1.00 17.22 ? 3 VAL C CG2 1 ATOM 3216 N N . ARG C 3 4 ? 50.416 15.424 -1.549 1.00 14.69 ? 4 ARG C N 1 ATOM 3217 C CA . ARG C 3 4 ? 51.510 16.308 -1.940 1.00 14.39 ? 4 ARG C CA 1 ATOM 3218 C C . ARG C 3 4 ? 50.973 17.570 -2.574 1.00 14.89 ? 4 ARG C C 1 ATOM 3219 O O . ARG C 3 4 ? 50.026 17.524 -3.347 1.00 15.01 ? 4 ARG C O 1 ATOM 3220 C CB . ARG C 3 4 ? 52.420 15.623 -2.962 1.00 15.31 ? 4 ARG C CB 1 ATOM 3221 C CG . ARG C 3 4 ? 53.202 14.436 -2.417 1.00 17.31 ? 4 ARG C CG 1 ATOM 3222 C CD . ARG C 3 4 ? 53.948 13.716 -3.525 1.00 18.78 ? 4 ARG C CD 1 ATOM 3223 N NE . ARG C 3 4 ? 54.683 12.552 -3.020 1.00 21.15 ? 4 ARG C NE 1 ATOM 3224 C CZ . ARG C 3 4 ? 55.293 11.661 -3.795 1.00 23.25 ? 4 ARG C CZ 1 ATOM 3225 N NH1 . ARG C 3 4 ? 55.260 11.799 -5.115 1.00 23.17 ? 4 ARG C NH1 1 ATOM 3226 N NH2 . ARG C 3 4 ? 55.938 10.632 -3.252 1.00 25.78 ? 4 ARG C NH2 1 ATOM 3227 N N . LEU C 3 5 ? 51.576 18.709 -2.267 1.00 14.41 ? 5 LEU C N 1 ATOM 3228 C CA A LEU C 3 5 ? 51.187 19.916 -2.979 0.40 14.95 ? 5 LEU C CA 1 ATOM 3229 C CA B LEU C 3 5 ? 51.215 19.940 -2.959 0.60 16.27 ? 5 LEU C CA 1 ATOM 3230 C C . LEU C 3 5 ? 52.101 20.131 -4.181 1.00 12.91 ? 5 LEU C C 1 ATOM 3231 O O . LEU C 3 5 ? 53.253 19.679 -4.195 1.00 14.82 ? 5 LEU C O 1 ATOM 3232 C CB A LEU C 3 5 ? 51.158 21.136 -2.054 0.40 22.51 ? 5 LEU C CB 1 ATOM 3233 C CB B LEU C 3 5 ? 51.311 21.146 -2.025 0.60 24.77 ? 5 LEU C CB 1 ATOM 3234 C CG A LEU C 3 5 ? 52.415 21.983 -1.866 0.40 23.92 ? 5 LEU C CG 1 ATOM 3235 C CG B LEU C 3 5 ? 52.681 21.527 -1.463 0.60 23.19 ? 5 LEU C CG 1 ATOM 3236 C CD1 A LEU C 3 5 ? 52.060 23.251 -1.107 0.40 19.29 ? 5 LEU C CD1 1 ATOM 3237 C CD1 B LEU C 3 5 ? 53.395 22.561 -2.334 0.60 20.10 ? 5 LEU C CD1 1 ATOM 3238 C CD2 A LEU C 3 5 ? 53.504 21.203 -1.147 0.40 26.01 ? 5 LEU C CD2 1 ATOM 3239 C CD2 B LEU C 3 5 ? 52.503 22.058 -0.064 0.60 25.98 ? 5 LEU C CD2 1 HETATM 3240 C C1 . CIR C 3 6 ? 52.567 22.875 -5.842 1.00 11.75 ? 6 CIR C C1 1 HETATM 3241 O O1 . CIR C 3 6 ? 51.708 23.687 -5.420 1.00 10.14 ? 6 CIR C O1 1 HETATM 3242 C C2 . CIR C 3 6 ? 52.212 21.473 -6.175 1.00 9.98 ? 6 CIR C C2 1 HETATM 3243 N N2 . CIR C 3 6 ? 51.515 20.935 -5.038 1.00 10.62 ? 6 CIR C N2 1 HETATM 3244 C C3 . CIR C 3 6 ? 51.341 21.400 -7.397 1.00 11.38 ? 6 CIR C C3 1 HETATM 3245 C C4 . CIR C 3 6 ? 52.123 21.880 -8.609 1.00 17.77 ? 6 CIR C C4 1 HETATM 3246 C C5 . CIR C 3 6 ? 52.465 20.736 -9.544 1.00 23.73 ? 6 CIR C C5 1 HETATM 3247 N N6 . CIR C 3 6 ? 53.337 19.750 -8.925 1.00 14.25 ? 6 CIR C N6 1 HETATM 3248 C C7 . CIR C 3 6 ? 54.618 19.453 -9.495 1.00 18.95 ? 6 CIR C C7 1 HETATM 3249 O O7 . CIR C 3 6 ? 55.009 20.034 -10.501 1.00 17.66 ? 6 CIR C O7 1 HETATM 3250 N N8 . CIR C 3 6 ? 55.453 18.466 -8.858 1.00 25.31 ? 6 CIR C N8 1 ATOM 3251 N N . SER C 3 7 ? 53.821 23.266 -5.964 1.00 13.82 ? 7 SER C N 1 ATOM 3252 C CA . SER C 3 7 ? 54.232 24.616 -5.636 1.00 12.83 ? 7 SER C CA 1 ATOM 3253 C C . SER C 3 7 ? 53.629 25.637 -6.591 1.00 16.65 ? 7 SER C C 1 ATOM 3254 O O . SER C 3 7 ? 53.311 25.327 -7.742 1.00 15.72 ? 7 SER C O 1 ATOM 3255 C CB . SER C 3 7 ? 55.753 24.714 -5.697 1.00 15.26 ? 7 SER C CB 1 ATOM 3256 O OG . SER C 3 7 ? 56.188 24.580 -7.039 1.00 19.76 ? 7 SER C OG 1 ATOM 3257 N N . SER C 3 8 ? 53.476 26.858 -6.099 1.00 10.71 ? 8 SER C N 1 ATOM 3258 C CA . SER C 3 8 ? 53.151 27.990 -6.951 1.00 9.06 ? 8 SER C CA 1 ATOM 3259 C C . SER C 3 8 ? 54.447 28.742 -7.234 1.00 15.64 ? 8 SER C C 1 ATOM 3260 O O . SER C 3 8 ? 55.339 28.774 -6.388 1.00 20.23 ? 8 SER C O 1 ATOM 3261 C CB . SER C 3 8 ? 52.122 28.893 -6.270 1.00 10.67 ? 8 SER C CB 1 ATOM 3262 O OG . SER C 3 8 ? 50.887 28.194 -6.143 1.00 12.72 ? 8 SER C OG 1 ATOM 3263 N N . VAL C 3 9 ? 54.546 29.317 -8.431 1.00 10.45 ? 9 VAL C N 1 ATOM 3264 C CA . VAL C 3 9 ? 55.803 29.812 -8.988 1.00 14.36 ? 9 VAL C CA 1 ATOM 3265 C C . VAL C 3 9 ? 55.847 31.333 -8.933 1.00 11.20 ? 9 VAL C C 1 ATOM 3266 O O . VAL C 3 9 ? 54.895 31.976 -9.329 1.00 10.17 ? 9 VAL C O 1 ATOM 3267 C CB . VAL C 3 9 ? 55.912 29.424 -10.495 1.00 12.81 ? 9 VAL C CB 1 ATOM 3268 C CG1 . VAL C 3 9 ? 57.269 29.807 -11.040 1.00 19.44 ? 9 VAL C CG1 1 ATOM 3269 C CG2 . VAL C 3 9 ? 55.651 27.941 -10.702 1.00 18.11 ? 9 VAL C CG2 1 ATOM 3270 N N . PRO C 3 10 ? 56.955 31.912 -8.448 1.00 13.77 ? 10 PRO C N 1 ATOM 3271 C CA . PRO C 3 10 ? 57.097 33.371 -8.477 1.00 12.39 ? 10 PRO C CA 1 ATOM 3272 C C . PRO C 3 10 ? 57.135 33.910 -9.903 1.00 12.71 ? 10 PRO C C 1 ATOM 3273 O O . PRO C 3 10 ? 57.919 33.425 -10.719 1.00 12.28 ? 10 PRO C O 1 ATOM 3274 C CB . PRO C 3 10 ? 58.454 33.602 -7.795 1.00 15.46 ? 10 PRO C CB 1 ATOM 3275 C CG . PRO C 3 10 ? 58.670 32.397 -6.957 1.00 23.37 ? 10 PRO C CG 1 ATOM 3276 C CD . PRO C 3 10 ? 58.066 31.262 -7.734 1.00 21.01 ? 10 PRO C CD 1 ATOM 3277 N N . GLY C 3 11 ? 56.309 34.912 -10.197 1.00 12.15 ? 11 GLY C N 1 ATOM 3278 C CA . GLY C 3 11 ? 56.285 35.503 -11.524 1.00 12.23 ? 11 GLY C CA 1 ATOM 3279 C C . GLY C 3 11 ? 57.425 36.476 -11.740 1.00 13.40 ? 11 GLY C C 1 ATOM 3280 O O . GLY C 3 11 ? 58.203 36.743 -10.821 1.00 15.74 ? 11 GLY C O 1 ATOM 3281 N N . VAL C 3 12 ? 57.531 37.017 -12.951 1.00 11.61 ? 12 VAL C N 1 ATOM 3282 C CA . VAL C 3 12 ? 58.566 38.015 -13.230 1.00 15.65 ? 12 VAL C CA 1 ATOM 3283 C C . VAL C 3 12 ? 58.209 39.375 -12.657 1.00 19.22 ? 12 VAL C C 1 ATOM 3284 O O . VAL C 3 12 ? 57.083 39.850 -12.807 1.00 18.58 ? 12 VAL C O 1 ATOM 3285 C CB . VAL C 3 12 ? 58.855 38.192 -14.737 1.00 32.86 ? 12 VAL C CB 1 ATOM 3286 C CG1 . VAL C 3 12 ? 60.270 37.736 -15.064 1.00 44.58 ? 12 VAL C CG1 1 ATOM 3287 C CG2 . VAL C 3 12 ? 57.857 37.454 -15.570 1.00 40.39 ? 12 VAL C CG2 1 ATOM 3288 N N A ARG C 3 13 ? 59.178 40.015 -12.011 0.56 17.38 ? 13 ARG C N 1 ATOM 3289 N N B ARG C 3 13 ? 59.179 40.000 -11.997 0.44 17.85 ? 13 ARG C N 1 ATOM 3290 C CA A ARG C 3 13 ? 58.962 41.332 -11.421 0.56 23.03 ? 13 ARG C CA 1 ATOM 3291 C CA B ARG C 3 13 ? 59.000 41.338 -11.452 0.44 24.11 ? 13 ARG C CA 1 ATOM 3292 C C A ARG C 3 13 ? 59.181 42.454 -12.430 0.56 27.77 ? 13 ARG C C 1 ATOM 3293 C C B ARG C 3 13 ? 59.347 42.388 -12.504 0.44 28.44 ? 13 ARG C C 1 ATOM 3294 O O A ARG C 3 13 ? 58.609 43.534 -12.297 0.56 23.74 ? 13 ARG C O 1 ATOM 3295 O O B ARG C 3 13 ? 59.822 42.055 -13.592 0.44 21.60 ? 13 ARG C O 1 ATOM 3296 C CB . ARG C 3 13 ? 59.874 41.530 -10.209 1.00 28.55 ? 13 ARG C CB 1 ATOM 3297 C CG . ARG C 3 13 ? 59.663 40.483 -9.137 1.00 39.11 ? 13 ARG C CG 1 ATOM 3298 C CD . ARG C 3 13 ? 60.477 40.755 -7.885 1.00 58.87 ? 13 ARG C CD 1 ATOM 3299 N NE . ARG C 3 13 ? 60.093 39.839 -6.813 1.00 72.97 ? 13 ARG C NE 1 ATOM 3300 C CZ . ARG C 3 13 ? 59.051 40.029 -6.008 1.00 75.42 ? 13 ARG C CZ 1 ATOM 3301 N NH1 . ARG C 3 13 ? 58.292 41.108 -6.147 1.00 78.38 ? 13 ARG C NH1 1 ATOM 3302 N NH2 . ARG C 3 13 ? 58.770 39.143 -5.061 1.00 68.58 ? 13 ARG C NH2 1 HETATM 3303 C C1 . NAG D 4 . ? 48.873 49.240 -18.855 1.00 38.06 ? 201 NAG A C1 1 HETATM 3304 C C2 . NAG D 4 . ? 48.341 48.339 -19.969 1.00 48.28 ? 201 NAG A C2 1 HETATM 3305 C C3 . NAG D 4 . ? 49.411 48.123 -21.036 1.00 59.20 ? 201 NAG A C3 1 HETATM 3306 C C4 . NAG D 4 . ? 49.980 49.454 -21.512 1.00 59.51 ? 201 NAG A C4 1 HETATM 3307 C C5 . NAG D 4 . ? 50.427 50.299 -20.323 1.00 54.27 ? 201 NAG A C5 1 HETATM 3308 C C6 . NAG D 4 . ? 50.874 51.686 -20.721 1.00 52.00 ? 201 NAG A C6 1 HETATM 3309 C C7 . NAG D 4 . ? 46.619 46.673 -19.423 1.00 49.25 ? 201 NAG A C7 1 HETATM 3310 C C8 . NAG D 4 . ? 46.348 45.321 -18.831 1.00 47.23 ? 201 NAG A C8 1 HETATM 3311 N N2 . NAG D 4 . ? 47.897 47.060 -19.433 1.00 48.80 ? 201 NAG A N2 1 HETATM 3312 O O3 . NAG D 4 . ? 48.835 47.424 -22.134 1.00 62.29 ? 201 NAG A O3 1 HETATM 3313 O O4 . NAG D 4 . ? 51.096 49.223 -22.364 1.00 60.31 ? 201 NAG A O4 1 HETATM 3314 O O5 . NAG D 4 . ? 49.332 50.465 -19.412 1.00 46.73 ? 201 NAG A O5 1 HETATM 3315 O O6 . NAG D 4 . ? 49.904 52.324 -21.541 1.00 48.80 ? 201 NAG A O6 1 HETATM 3316 O O7 . NAG D 4 . ? 45.721 47.379 -19.869 1.00 52.86 ? 201 NAG A O7 1 HETATM 3317 C C1 . NAG E 4 . ? 30.636 42.556 6.638 1.00 30.11 ? 202 NAG A C1 1 HETATM 3318 C C2 . NAG E 4 . ? 30.998 43.518 5.508 1.00 31.07 ? 202 NAG A C2 1 HETATM 3319 C C3 . NAG E 4 . ? 32.157 44.424 5.920 1.00 42.85 ? 202 NAG A C3 1 HETATM 3320 C C4 . NAG E 4 . ? 31.905 45.064 7.282 1.00 51.24 ? 202 NAG A C4 1 HETATM 3321 C C5 . NAG E 4 . ? 31.444 44.029 8.305 1.00 49.06 ? 202 NAG A C5 1 HETATM 3322 C C6 . NAG E 4 . ? 30.997 44.645 9.611 1.00 54.22 ? 202 NAG A C6 1 HETATM 3323 C C7 . NAG E 4 . ? 30.557 42.712 3.226 1.00 24.72 ? 202 NAG A C7 1 HETATM 3324 C C8 . NAG E 4 . ? 31.083 41.902 2.080 1.00 20.30 ? 202 NAG A C8 1 HETATM 3325 N N2 . NAG E 4 . ? 31.347 42.777 4.299 1.00 27.49 ? 202 NAG A N2 1 HETATM 3326 O O3 . NAG E 4 . ? 32.330 45.433 4.932 1.00 39.20 ? 202 NAG A O3 1 HETATM 3327 O O4 . NAG E 4 . ? 33.121 45.634 7.755 1.00 66.06 ? 202 NAG A O4 1 HETATM 3328 O O5 . NAG E 4 . ? 30.325 43.298 7.792 1.00 38.93 ? 202 NAG A O5 1 HETATM 3329 O O6 . NAG E 4 . ? 31.374 43.843 10.721 1.00 61.95 ? 202 NAG A O6 1 HETATM 3330 O O7 . NAG E 4 . ? 29.464 43.273 3.180 1.00 28.16 ? 202 NAG A O7 1 HETATM 3331 C C1 . NAG F 4 . ? 33.011 47.059 7.915 1.00 70.42 ? 203 NAG A C1 1 HETATM 3332 C C2 . NAG F 4 . ? 34.390 47.622 8.246 1.00 75.37 ? 203 NAG A C2 1 HETATM 3333 C C3 . NAG F 4 . ? 34.300 49.116 8.537 1.00 78.56 ? 203 NAG A C3 1 HETATM 3334 C C4 . NAG F 4 . ? 33.590 49.833 7.392 1.00 81.38 ? 203 NAG A C4 1 HETATM 3335 C C5 . NAG F 4 . ? 32.257 49.154 7.080 1.00 77.79 ? 203 NAG A C5 1 HETATM 3336 C C6 . NAG F 4 . ? 31.561 49.739 5.874 1.00 76.62 ? 203 NAG A C6 1 HETATM 3337 C C7 . NAG F 4 . ? 34.467 46.812 10.587 1.00 75.67 ? 203 NAG A C7 1 HETATM 3338 C C8 . NAG F 4 . ? 35.263 46.026 11.587 1.00 73.82 ? 203 NAG A C8 1 HETATM 3339 N N2 . NAG F 4 . ? 35.003 46.908 9.365 1.00 77.76 ? 203 NAG A N2 1 HETATM 3340 O O3 . NAG F 4 . ? 35.607 49.650 8.705 1.00 81.13 ? 203 NAG A O3 1 HETATM 3341 O O4 . NAG F 4 . ? 33.356 51.191 7.746 1.00 88.18 ? 203 NAG A O4 1 HETATM 3342 O O5 . NAG F 4 . ? 32.471 47.763 6.803 1.00 73.14 ? 203 NAG A O5 1 HETATM 3343 O O6 . NAG F 4 . ? 32.496 50.194 4.907 1.00 76.74 ? 203 NAG A O6 1 HETATM 3344 O O7 . NAG F 4 . ? 33.394 47.334 10.882 1.00 76.28 ? 203 NAG A O7 1 HETATM 3345 C C1 . EDO G 5 . ? 31.349 22.977 7.412 1.00 46.51 ? 204 EDO A C1 1 HETATM 3346 O O1 . EDO G 5 . ? 31.707 22.783 8.783 1.00 49.59 ? 204 EDO A O1 1 HETATM 3347 C C2 . EDO G 5 . ? 32.600 22.908 6.543 1.00 51.62 ? 204 EDO A C2 1 HETATM 3348 O O2 . EDO G 5 . ? 33.650 23.665 7.149 1.00 64.68 ? 204 EDO A O2 1 HETATM 3349 C C1 . EDO H 5 . ? 30.411 26.253 -12.385 1.00 31.00 ? 205 EDO A C1 1 HETATM 3350 O O1 . EDO H 5 . ? 31.338 27.089 -13.094 1.00 19.97 ? 205 EDO A O1 1 HETATM 3351 C C2 . EDO H 5 . ? 31.014 24.880 -12.123 1.00 34.55 ? 205 EDO A C2 1 HETATM 3352 O O2 . EDO H 5 . ? 31.793 24.910 -10.923 1.00 25.05 ? 205 EDO A O2 1 HETATM 3353 C C1 . EDO I 5 . ? 38.241 27.807 9.109 1.00 40.79 ? 206 EDO A C1 1 HETATM 3354 O O1 . EDO I 5 . ? 38.756 26.486 9.322 1.00 28.70 ? 206 EDO A O1 1 HETATM 3355 C C2 . EDO I 5 . ? 39.390 28.797 8.960 1.00 50.74 ? 206 EDO A C2 1 HETATM 3356 O O2 . EDO I 5 . ? 40.022 28.621 7.687 1.00 49.94 ? 206 EDO A O2 1 HETATM 3357 C C1 . EDO J 5 . ? 11.624 38.178 8.442 1.00 34.78 ? 207 EDO A C1 1 HETATM 3358 O O1 . EDO J 5 . ? 11.055 36.935 8.002 1.00 33.68 ? 207 EDO A O1 1 HETATM 3359 C C2 . EDO J 5 . ? 11.824 39.103 7.248 1.00 40.77 ? 207 EDO A C2 1 HETATM 3360 O O2 . EDO J 5 . ? 10.686 39.962 7.093 1.00 37.64 ? 207 EDO A O2 1 HETATM 3361 C C1 . EDO K 5 . ? 26.368 38.954 -12.131 1.00 47.77 ? 208 EDO A C1 1 HETATM 3362 O O1 . EDO K 5 . ? 26.755 40.322 -12.321 1.00 49.25 ? 208 EDO A O1 1 HETATM 3363 C C2 . EDO K 5 . ? 25.115 38.876 -11.271 1.00 43.57 ? 208 EDO A C2 1 HETATM 3364 O O2 . EDO K 5 . ? 25.260 37.872 -10.252 1.00 31.45 ? 208 EDO A O2 1 HETATM 3365 C C1 . NAG L 4 . ? 41.012 1.205 -19.000 1.00 50.21 ? 201 NAG B C1 1 HETATM 3366 C C2 . NAG L 4 . ? 41.054 0.893 -20.498 1.00 59.28 ? 201 NAG B C2 1 HETATM 3367 C C3 . NAG L 4 . ? 41.235 -0.604 -20.727 1.00 65.77 ? 201 NAG B C3 1 HETATM 3368 C C4 . NAG L 4 . ? 42.448 -1.116 -19.961 1.00 61.93 ? 201 NAG B C4 1 HETATM 3369 C C5 . NAG L 4 . ? 42.348 -0.720 -18.490 1.00 57.86 ? 201 NAG B C5 1 HETATM 3370 C C6 . NAG L 4 . ? 43.575 -1.096 -17.691 1.00 57.17 ? 201 NAG B C6 1 HETATM 3371 C C7 . NAG L 4 . ? 39.848 1.913 -22.383 1.00 66.32 ? 201 NAG B C7 1 HETATM 3372 C C8 . NAG L 4 . ? 38.512 2.344 -22.911 1.00 64.31 ? 201 NAG B C8 1 HETATM 3373 N N2 . NAG L 4 . ? 39.844 1.368 -21.161 1.00 63.12 ? 201 NAG B N2 1 HETATM 3374 O O3 . NAG L 4 . ? 41.399 -0.859 -22.117 1.00 72.55 ? 201 NAG B O3 1 HETATM 3375 O O4 . NAG L 4 . ? 42.524 -2.534 -20.065 1.00 65.13 ? 201 NAG B O4 1 HETATM 3376 O O5 . NAG L 4 . ? 42.202 0.702 -18.380 1.00 53.65 ? 201 NAG B O5 1 HETATM 3377 O O6 . NAG L 4 . ? 43.391 -0.839 -16.306 1.00 58.56 ? 201 NAG B O6 1 HETATM 3378 O O7 . NAG L 4 . ? 40.880 2.055 -23.030 1.00 68.88 ? 201 NAG B O7 1 HETATM 3379 C C1 . EDO M 5 . ? -11.326 8.781 -9.363 1.00 35.30 ? 202 EDO B C1 1 HETATM 3380 O O1 . EDO M 5 . ? -12.061 7.743 -10.022 1.00 43.67 ? 202 EDO B O1 1 HETATM 3381 C C2 . EDO M 5 . ? -11.947 9.061 -8.004 1.00 33.24 ? 202 EDO B C2 1 HETATM 3382 O O2 . EDO M 5 . ? -10.976 9.675 -7.159 1.00 20.74 ? 202 EDO B O2 1 HETATM 3383 C C1 . EDO N 5 . ? 22.934 6.629 -12.640 1.00 42.03 ? 203 EDO B C1 1 HETATM 3384 O O1 . EDO N 5 . ? 21.892 5.882 -13.274 1.00 46.13 ? 203 EDO B O1 1 HETATM 3385 C C2 . EDO N 5 . ? 24.129 5.707 -12.448 1.00 48.40 ? 203 EDO B C2 1 HETATM 3386 O O2 . EDO N 5 . ? 23.700 4.530 -11.749 1.00 45.57 ? 203 EDO B O2 1 HETATM 3387 C C1 . EDO O 5 . ? 24.598 19.527 8.224 1.00 44.60 ? 204 EDO B C1 1 HETATM 3388 O O1 . EDO O 5 . ? 25.600 19.814 9.204 1.00 48.61 ? 204 EDO B O1 1 HETATM 3389 C C2 . EDO O 5 . ? 25.214 19.565 6.831 1.00 36.84 ? 204 EDO B C2 1 HETATM 3390 O O2 . EDO O 5 . ? 26.072 18.432 6.652 1.00 35.37 ? 204 EDO B O2 1 HETATM 3391 C C1 . PGE P 6 . ? 17.253 15.351 -11.756 1.00 47.08 ? 205 PGE B C1 1 HETATM 3392 O O1 . PGE P 6 . ? 17.293 14.774 -10.510 1.00 51.83 ? 205 PGE B O1 1 HETATM 3393 C C2 . PGE P 6 . ? 16.983 14.274 -12.785 1.00 42.00 ? 205 PGE B C2 1 HETATM 3394 O O2 . PGE P 6 . ? 16.123 14.801 -13.793 1.00 33.72 ? 205 PGE B O2 1 HETATM 3395 C C3 . PGE P 6 . ? 14.748 14.578 -13.737 1.00 29.64 ? 205 PGE B C3 1 HETATM 3396 C C4 . PGE P 6 . ? 14.098 15.073 -14.972 1.00 29.74 ? 205 PGE B C4 1 HETATM 3397 O O4 . PGE P 6 . ? 14.986 13.486 -18.796 1.00 29.01 ? 205 PGE B O4 1 HETATM 3398 C C6 . PGE P 6 . ? 15.768 13.156 -17.714 1.00 47.91 ? 205 PGE B C6 1 HETATM 3399 C C5 . PGE P 6 . ? 15.675 14.241 -16.600 1.00 26.15 ? 205 PGE B C5 1 HETATM 3400 O O3 . PGE P 6 . ? 14.409 14.227 -16.037 1.00 41.99 ? 205 PGE B O3 1 HETATM 3401 O O . HOH Q 7 . ? 50.251 33.118 -7.832 1.00 11.59 ? 301 HOH A O 1 HETATM 3402 O O . HOH Q 7 . ? 45.260 18.546 -7.710 1.00 10.08 ? 302 HOH A O 1 HETATM 3403 O O . HOH Q 7 . ? 36.862 46.037 -6.733 1.00 11.54 ? 303 HOH A O 1 HETATM 3404 O O . HOH Q 7 . ? 20.030 15.534 1.301 1.00 13.14 ? 304 HOH A O 1 HETATM 3405 O O . HOH Q 7 . ? 42.323 28.006 3.410 1.00 15.02 ? 305 HOH A O 1 HETATM 3406 O O . HOH Q 7 . ? 13.543 35.106 10.293 1.00 15.56 ? 306 HOH A O 1 HETATM 3407 O O . HOH Q 7 . ? 32.342 11.959 -7.782 1.00 15.44 ? 307 HOH A O 1 HETATM 3408 O O . HOH Q 7 . ? 24.216 39.186 7.028 1.00 18.06 ? 308 HOH A O 1 HETATM 3409 O O . HOH Q 7 . ? 34.016 36.818 4.272 1.00 17.36 ? 309 HOH A O 1 HETATM 3410 O O . HOH Q 7 . ? 35.005 24.287 4.698 1.00 16.27 ? 310 HOH A O 1 HETATM 3411 O O . HOH Q 7 . ? 47.000 44.147 -5.060 1.00 16.61 ? 311 HOH A O 1 HETATM 3412 O O . HOH Q 7 . ? 35.353 44.881 -4.713 1.00 16.07 ? 312 HOH A O 1 HETATM 3413 O O . HOH Q 7 . ? 32.931 22.301 1.780 1.00 15.08 ? 313 HOH A O 1 HETATM 3414 O O . HOH Q 7 . ? 37.627 25.794 -15.297 1.00 14.29 ? 314 HOH A O 1 HETATM 3415 O O . HOH Q 7 . ? 37.811 19.196 -8.893 1.00 14.59 ? 315 HOH A O 1 HETATM 3416 O O . HOH Q 7 . ? 19.338 34.989 -5.301 1.00 19.59 ? 316 HOH A O 1 HETATM 3417 O O . HOH Q 7 . ? 22.030 29.649 -4.840 1.00 12.58 ? 317 HOH A O 1 HETATM 3418 O O . HOH Q 7 . ? 32.360 15.387 -5.126 1.00 18.43 ? 318 HOH A O 1 HETATM 3419 O O . HOH Q 7 . ? 32.367 46.308 -9.258 1.00 18.56 ? 319 HOH A O 1 HETATM 3420 O O . HOH Q 7 . ? 54.503 43.854 -12.512 1.00 17.27 ? 320 HOH A O 1 HETATM 3421 O O . HOH Q 7 . ? 37.249 21.264 5.594 1.00 17.84 ? 321 HOH A O 1 HETATM 3422 O O . HOH Q 7 . ? 31.932 26.106 10.712 1.00 20.53 ? 322 HOH A O 1 HETATM 3423 O O . HOH Q 7 . ? 35.471 24.100 -9.499 1.00 19.28 ? 323 HOH A O 1 HETATM 3424 O O . HOH Q 7 . ? 31.773 41.239 -1.020 1.00 17.18 ? 324 HOH A O 1 HETATM 3425 O O . HOH Q 7 . ? 12.033 25.968 14.264 1.00 24.03 ? 325 HOH A O 1 HETATM 3426 O O . HOH Q 7 . ? 54.728 37.320 -0.051 1.00 20.73 ? 326 HOH A O 1 HETATM 3427 O O . HOH Q 7 . ? 15.517 29.853 -1.679 1.00 17.37 ? 327 HOH A O 1 HETATM 3428 O O . HOH Q 7 . ? 52.694 20.397 2.430 1.00 26.87 ? 328 HOH A O 1 HETATM 3429 O O . HOH Q 7 . ? 17.459 41.488 13.428 1.00 18.30 ? 329 HOH A O 1 HETATM 3430 O O . HOH Q 7 . ? 56.888 31.310 -0.064 1.00 20.68 ? 330 HOH A O 1 HETATM 3431 O O . HOH Q 7 . ? 38.413 31.105 3.292 1.00 25.07 ? 331 HOH A O 1 HETATM 3432 O O . HOH Q 7 . ? 40.379 17.895 10.390 1.00 25.41 ? 332 HOH A O 1 HETATM 3433 O O . HOH Q 7 . ? 23.853 34.682 -11.171 1.00 30.66 ? 333 HOH A O 1 HETATM 3434 O O . HOH Q 7 . ? 26.038 35.746 -10.120 1.00 17.55 ? 334 HOH A O 1 HETATM 3435 O O . HOH Q 7 . ? 22.846 28.540 -7.192 1.00 23.53 ? 335 HOH A O 1 HETATM 3436 O O . HOH Q 7 . ? 51.569 32.683 3.839 1.00 22.39 ? 336 HOH A O 1 HETATM 3437 O O . HOH Q 7 . ? 48.741 42.557 0.794 1.00 29.04 ? 337 HOH A O 1 HETATM 3438 O O . HOH Q 7 . ? 28.899 42.261 -12.188 1.00 25.62 ? 338 HOH A O 1 HETATM 3439 O O . HOH Q 7 . ? 14.469 33.970 17.495 1.00 28.72 ? 339 HOH A O 1 HETATM 3440 O O . HOH Q 7 . ? 46.858 46.743 -4.224 1.00 28.47 ? 340 HOH A O 1 HETATM 3441 O O . HOH Q 7 . ? 23.894 33.467 12.006 1.00 27.71 ? 341 HOH A O 1 HETATM 3442 O O . HOH Q 7 . ? 19.968 41.465 12.335 1.00 21.96 ? 342 HOH A O 1 HETATM 3443 O O . HOH Q 7 . ? 55.883 42.097 -14.248 1.00 23.65 ? 343 HOH A O 1 HETATM 3444 O O . HOH Q 7 . ? 29.074 21.680 8.920 1.00 29.23 ? 344 HOH A O 1 HETATM 3445 O O . HOH Q 7 . ? 32.153 20.426 -0.367 1.00 27.58 ? 345 HOH A O 1 HETATM 3446 O O . HOH Q 7 . ? 25.899 23.152 11.676 1.00 27.29 ? 346 HOH A O 1 HETATM 3447 O O . HOH Q 7 . ? 19.651 42.254 -2.592 1.00 26.88 ? 347 HOH A O 1 HETATM 3448 O O . HOH Q 7 . ? 12.433 17.182 9.723 1.00 20.39 ? 348 HOH A O 1 HETATM 3449 O O . HOH Q 7 . ? 32.994 47.594 -4.303 1.00 26.55 ? 349 HOH A O 1 HETATM 3450 O O . HOH Q 7 . ? 36.096 48.515 -7.270 1.00 24.53 ? 350 HOH A O 1 HETATM 3451 O O . HOH Q 7 . ? 29.011 29.582 10.680 1.00 27.91 ? 351 HOH A O 1 HETATM 3452 O O . HOH Q 7 . ? 38.923 33.834 3.443 1.00 28.45 ? 352 HOH A O 1 HETATM 3453 O O . HOH Q 7 . ? 26.432 44.510 -8.906 1.00 28.88 ? 353 HOH A O 1 HETATM 3454 O O . HOH Q 7 . ? 13.503 13.967 7.022 1.00 31.51 ? 354 HOH A O 1 HETATM 3455 O O . HOH Q 7 . ? 12.772 34.255 -0.092 1.00 27.02 ? 355 HOH A O 1 HETATM 3456 O O . HOH Q 7 . ? 26.544 30.195 9.461 1.00 29.59 ? 356 HOH A O 1 HETATM 3457 O O . HOH Q 7 . ? 51.635 14.593 5.628 1.00 32.94 ? 357 HOH A O 1 HETATM 3458 O O . HOH Q 7 . ? 47.493 20.069 10.612 1.00 31.63 ? 358 HOH A O 1 HETATM 3459 O O . HOH Q 7 . ? 15.128 24.677 16.559 1.00 31.44 ? 359 HOH A O 1 HETATM 3460 O O . HOH Q 7 . ? 51.721 48.427 -5.845 1.00 26.40 ? 360 HOH A O 1 HETATM 3461 O O . HOH Q 7 . ? 29.671 35.621 7.626 1.00 26.51 ? 361 HOH A O 1 HETATM 3462 O O . HOH Q 7 . ? 42.508 50.601 -8.859 1.00 25.64 ? 362 HOH A O 1 HETATM 3463 O O . HOH Q 7 . ? 10.543 25.522 11.866 1.00 27.67 ? 363 HOH A O 1 HETATM 3464 O O . HOH Q 7 . ? 21.538 31.626 18.850 1.00 29.12 ? 364 HOH A O 1 HETATM 3465 O O . HOH Q 7 . ? 54.508 45.878 -14.440 1.00 27.17 ? 365 HOH A O 1 HETATM 3466 O O . HOH Q 7 . ? 35.547 22.290 7.151 1.00 35.98 ? 366 HOH A O 1 HETATM 3467 O O . HOH Q 7 . ? 11.995 33.679 18.421 1.00 52.54 ? 367 HOH A O 1 HETATM 3468 O O . HOH Q 7 . ? 13.645 31.006 -0.308 1.00 31.11 ? 368 HOH A O 1 HETATM 3469 O O . HOH Q 7 . ? 49.822 19.833 9.270 1.00 30.96 ? 369 HOH A O 1 HETATM 3470 O O . HOH Q 7 . ? 53.811 36.701 2.799 1.00 27.31 ? 370 HOH A O 1 HETATM 3471 O O . HOH Q 7 . ? 9.350 28.300 2.552 1.00 32.28 ? 371 HOH A O 1 HETATM 3472 O O . HOH Q 7 . ? 7.808 27.395 10.298 1.00 41.06 ? 372 HOH A O 1 HETATM 3473 O O . HOH Q 7 . ? 30.389 21.156 -2.359 1.00 21.07 ? 373 HOH A O 1 HETATM 3474 O O . HOH Q 7 . ? 34.640 15.920 -12.091 1.00 33.90 ? 374 HOH A O 1 HETATM 3475 O O . HOH Q 7 . ? 28.301 16.035 -3.039 1.00 27.90 ? 375 HOH A O 1 HETATM 3476 O O . HOH Q 7 . ? 29.582 46.655 -7.597 1.00 26.72 ? 376 HOH A O 1 HETATM 3477 O O . HOH Q 7 . ? 36.752 36.973 4.027 1.00 35.73 ? 377 HOH A O 1 HETATM 3478 O O . HOH Q 7 . ? 9.692 19.006 3.200 1.00 37.43 ? 378 HOH A O 1 HETATM 3479 O O . HOH Q 7 . ? 51.395 35.316 3.046 1.00 29.22 ? 379 HOH A O 1 HETATM 3480 O O . HOH Q 7 . ? 18.451 16.447 8.330 1.00 33.83 ? 380 HOH A O 1 HETATM 3481 O O . HOH Q 7 . ? 45.740 13.021 9.139 1.00 39.23 ? 381 HOH A O 1 HETATM 3482 O O . HOH Q 7 . ? 16.048 40.358 -0.165 1.00 32.56 ? 382 HOH A O 1 HETATM 3483 O O . HOH Q 7 . ? 54.822 39.884 -0.855 1.00 28.73 ? 383 HOH A O 1 HETATM 3484 O O . HOH Q 7 . ? 29.642 30.735 -15.862 1.00 36.17 ? 384 HOH A O 1 HETATM 3485 O O . HOH Q 7 . ? 23.530 43.235 8.370 1.00 37.97 ? 385 HOH A O 1 HETATM 3486 O O . HOH Q 7 . ? 12.330 37.355 3.864 1.00 28.79 ? 386 HOH A O 1 HETATM 3487 O O . HOH Q 7 . ? 36.691 23.767 -16.631 1.00 43.54 ? 387 HOH A O 1 HETATM 3488 O O . HOH Q 7 . ? 36.218 19.879 -10.994 1.00 24.93 ? 388 HOH A O 1 HETATM 3489 O O . HOH Q 7 . ? 56.478 35.925 -6.457 1.00 30.21 ? 389 HOH A O 1 HETATM 3490 O O . HOH Q 7 . ? 33.319 33.836 -14.842 1.00 32.51 ? 390 HOH A O 1 HETATM 3491 O O . HOH Q 7 . ? 40.164 51.869 -9.175 1.00 36.51 ? 391 HOH A O 1 HETATM 3492 O O . HOH Q 7 . ? 57.244 36.505 0.284 1.00 41.05 ? 392 HOH A O 1 HETATM 3493 O O . HOH Q 7 . ? 23.033 12.998 4.724 1.00 41.29 ? 393 HOH A O 1 HETATM 3494 O O . HOH Q 7 . ? 38.145 35.991 2.059 1.00 26.95 ? 394 HOH A O 1 HETATM 3495 O O . HOH Q 7 . ? 42.258 30.207 6.884 1.00 29.32 ? 395 HOH A O 1 HETATM 3496 O O . HOH Q 7 . ? 33.323 34.676 5.529 1.00 40.30 ? 396 HOH A O 1 HETATM 3497 O O . HOH Q 7 . ? 14.170 41.365 1.077 1.00 43.61 ? 397 HOH A O 1 HETATM 3498 O O . HOH Q 7 . ? 54.697 48.537 -14.308 1.00 33.40 ? 398 HOH A O 1 HETATM 3499 O O . HOH Q 7 . ? 46.040 45.851 3.246 1.00 35.48 ? 399 HOH A O 1 HETATM 3500 O O . HOH Q 7 . ? 57.544 33.897 -1.225 1.00 39.96 ? 400 HOH A O 1 HETATM 3501 O O . HOH Q 7 . ? 23.121 41.071 12.691 1.00 43.11 ? 401 HOH A O 1 HETATM 3502 O O . HOH Q 7 . ? 28.876 44.939 -9.663 1.00 28.43 ? 402 HOH A O 1 HETATM 3503 O O . HOH Q 7 . ? 53.834 32.726 5.559 1.00 31.83 ? 403 HOH A O 1 HETATM 3504 O O . HOH Q 7 . ? 34.634 22.437 -3.374 1.00 25.78 ? 404 HOH A O 1 HETATM 3505 O O . HOH Q 7 . ? 19.676 18.812 13.105 1.00 33.88 ? 405 HOH A O 1 HETATM 3506 O O . HOH Q 7 . ? 29.839 48.210 -3.291 1.00 43.41 ? 406 HOH A O 1 HETATM 3507 O O . HOH Q 7 . ? 7.258 33.583 13.455 1.00 32.62 ? 407 HOH A O 1 HETATM 3508 O O . HOH Q 7 . ? 37.385 21.439 -13.304 1.00 28.72 ? 408 HOH A O 1 HETATM 3509 O O . HOH Q 7 . ? 24.978 43.816 0.793 1.00 24.18 ? 409 HOH A O 1 HETATM 3510 O O . HOH Q 7 . ? 39.222 28.608 -3.998 1.00 29.84 ? 410 HOH A O 1 HETATM 3511 O O . HOH Q 7 . ? 16.123 31.332 -3.879 1.00 38.78 ? 411 HOH A O 1 HETATM 3512 O O . HOH Q 7 . ? 49.538 36.597 4.178 1.00 34.64 ? 412 HOH A O 1 HETATM 3513 O O . HOH Q 7 . ? 57.735 31.535 2.227 1.00 38.34 ? 413 HOH A O 1 HETATM 3514 O O . HOH Q 7 . ? 12.876 14.566 9.278 1.00 36.35 ? 414 HOH A O 1 HETATM 3515 O O . HOH Q 7 . ? 28.623 26.925 16.128 1.00 45.51 ? 415 HOH A O 1 HETATM 3516 O O . HOH Q 7 . ? 34.580 6.284 -10.431 1.00 43.40 ? 416 HOH A O 1 HETATM 3517 O O . HOH Q 7 . ? 29.676 33.113 -14.609 1.00 53.75 ? 417 HOH A O 1 HETATM 3518 O O . HOH Q 7 . ? 40.945 28.355 -2.185 1.00 31.80 ? 418 HOH A O 1 HETATM 3519 O O . HOH Q 7 . ? 39.343 51.789 -11.942 1.00 41.35 ? 419 HOH A O 1 HETATM 3520 O O . HOH Q 7 . ? 35.817 24.399 8.955 1.00 39.15 ? 420 HOH A O 1 HETATM 3521 O O . HOH Q 7 . ? 16.971 42.032 -1.924 1.00 41.30 ? 421 HOH A O 1 HETATM 3522 O O . HOH Q 7 . ? 37.549 40.889 4.320 1.00 37.01 ? 422 HOH A O 1 HETATM 3523 O O . HOH Q 7 . ? 28.754 44.888 -13.172 1.00 46.35 ? 423 HOH A O 1 HETATM 3524 O O . HOH Q 7 . ? 30.309 40.940 -14.311 1.00 33.72 ? 424 HOH A O 1 HETATM 3525 O O . HOH Q 7 . ? 14.794 37.745 -1.958 1.00 45.27 ? 425 HOH A O 1 HETATM 3526 O O . HOH Q 7 . ? 7.885 22.439 5.248 1.00 38.63 ? 426 HOH A O 1 HETATM 3527 O O . HOH Q 7 . ? 6.251 14.762 13.098 1.00 38.77 ? 427 HOH A O 1 HETATM 3528 O O . HOH Q 7 . ? 15.710 15.316 9.182 1.00 40.84 ? 428 HOH A O 1 HETATM 3529 O O . HOH Q 7 . ? 5.683 21.144 -0.878 1.00 46.64 ? 429 HOH A O 1 HETATM 3530 O O . HOH Q 7 . ? 5.071 17.041 9.845 1.00 36.42 ? 430 HOH A O 1 HETATM 3531 O O . HOH Q 7 . ? 33.248 38.903 5.910 1.00 24.59 ? 431 HOH A O 1 HETATM 3532 O O . HOH Q 7 . ? 20.510 25.099 -4.251 1.00 25.06 ? 432 HOH A O 1 HETATM 3533 O O . HOH Q 7 . ? 28.122 44.771 1.617 1.00 30.94 ? 433 HOH A O 1 HETATM 3534 O O . HOH Q 7 . ? 33.723 41.587 5.280 1.00 32.67 ? 434 HOH A O 1 HETATM 3535 O O . HOH Q 7 . ? 30.839 9.762 5.286 1.00 33.59 ? 435 HOH A O 1 HETATM 3536 O O . HOH Q 7 . ? 26.386 23.272 -6.726 1.00 32.02 ? 436 HOH A O 1 HETATM 3537 O O . HOH Q 7 . ? 10.771 35.602 18.907 1.00 46.13 ? 437 HOH A O 1 HETATM 3538 O O . HOH Q 7 . ? 32.865 23.676 10.760 1.00 47.39 ? 438 HOH A O 1 HETATM 3539 O O . HOH Q 7 . ? 10.354 29.942 19.003 1.00 45.84 ? 439 HOH A O 1 HETATM 3540 O O . HOH Q 7 . ? 56.548 43.434 -7.963 1.00 44.59 ? 440 HOH A O 1 HETATM 3541 O O . HOH Q 7 . ? 50.459 10.131 6.580 1.00 40.37 ? 441 HOH A O 1 HETATM 3542 O O . HOH Q 7 . ? 22.364 14.855 3.044 1.00 24.86 ? 442 HOH A O 1 HETATM 3543 O O . HOH Q 7 . ? 26.624 25.591 -8.281 1.00 27.74 ? 443 HOH A O 1 HETATM 3544 O O . HOH Q 7 . ? 34.774 26.588 7.871 1.00 40.44 ? 444 HOH A O 1 HETATM 3545 O O . HOH Q 7 . ? 12.783 37.654 1.535 1.00 41.24 ? 445 HOH A O 1 HETATM 3546 O O . HOH Q 7 . ? 31.163 34.190 6.179 1.00 43.97 ? 446 HOH A O 1 HETATM 3547 O O . HOH Q 7 . ? 55.806 30.508 4.696 1.00 45.98 ? 447 HOH A O 1 HETATM 3548 O O . HOH Q 7 . ? 30.164 20.843 -8.949 1.00 43.98 ? 448 HOH A O 1 HETATM 3549 O O . HOH Q 7 . ? 44.343 17.444 10.909 1.00 47.37 ? 449 HOH A O 1 HETATM 3550 O O . HOH Q 7 . ? 49.095 32.543 5.148 1.00 44.68 ? 450 HOH A O 1 HETATM 3551 O O . HOH Q 7 . ? 13.102 35.841 21.335 1.00 48.68 ? 451 HOH A O 1 HETATM 3552 O O . HOH Q 7 . ? 5.190 17.512 6.737 1.00 47.86 ? 452 HOH A O 1 HETATM 3553 O O . HOH Q 7 . ? 7.555 13.866 4.440 1.00 45.81 ? 453 HOH A O 1 HETATM 3554 O O . HOH Q 7 . ? 9.608 12.176 6.023 1.00 38.15 ? 454 HOH A O 1 HETATM 3555 O O . HOH Q 7 . ? 46.604 33.567 4.670 1.00 31.89 ? 455 HOH A O 1 HETATM 3556 O O . HOH Q 7 . ? 32.628 10.140 -12.438 1.00 45.17 ? 456 HOH A O 1 HETATM 3557 O O . HOH Q 7 . ? 29.326 36.423 -14.096 1.00 44.64 ? 457 HOH A O 1 HETATM 3558 O O . HOH Q 7 . ? 19.429 37.021 18.651 1.00 41.91 ? 458 HOH A O 1 HETATM 3559 O O . HOH Q 7 . ? 17.116 36.676 -5.530 1.00 44.61 ? 459 HOH A O 1 HETATM 3560 O O . HOH Q 7 . ? 31.698 37.673 -14.541 1.00 43.30 ? 460 HOH A O 1 HETATM 3561 O O . HOH Q 7 . ? 56.619 21.606 0.495 1.00 39.74 ? 461 HOH A O 1 HETATM 3562 O O . HOH Q 7 . ? 7.595 26.212 2.664 1.00 49.38 ? 462 HOH A O 1 HETATM 3563 O O . HOH Q 7 . ? 21.757 44.685 -5.999 1.00 34.33 ? 463 HOH A O 1 HETATM 3564 O O . HOH Q 7 . ? 25.275 43.373 -10.831 1.00 47.21 ? 464 HOH A O 1 HETATM 3565 O O . HOH Q 7 . ? 16.449 49.871 2.582 1.00 22.92 ? 465 HOH A O 1 HETATM 3566 O O . HOH Q 7 . ? 39.400 8.043 -12.761 1.00 29.94 ? 466 HOH A O 1 HETATM 3567 O O . HOH Q 7 . ? 43.302 34.515 5.310 1.00 37.99 ? 467 HOH A O 1 HETATM 3568 O O . HOH Q 7 . ? 31.213 31.497 -18.079 1.00 38.21 ? 468 HOH A O 1 HETATM 3569 O O . HOH Q 7 . ? 10.467 38.226 16.295 1.00 41.59 ? 469 HOH A O 1 HETATM 3570 O O . HOH Q 7 . ? 29.867 33.375 9.620 1.00 35.24 ? 470 HOH A O 1 HETATM 3571 O O . HOH Q 7 . ? 20.262 44.345 -4.109 1.00 38.22 ? 471 HOH A O 1 HETATM 3572 O O . HOH Q 7 . ? 30.249 27.053 -15.536 1.00 45.06 ? 472 HOH A O 1 HETATM 3573 O O . HOH Q 7 . ? 28.383 22.162 -9.981 1.00 52.22 ? 473 HOH A O 1 HETATM 3574 O O . HOH Q 7 . ? 47.489 26.489 16.038 1.00 45.52 ? 474 HOH A O 1 HETATM 3575 O O . HOH Q 7 . ? 35.289 21.946 -8.892 1.00 40.28 ? 475 HOH A O 1 HETATM 3576 O O . HOH Q 7 . ? 25.206 39.009 12.031 1.00 47.22 ? 476 HOH A O 1 HETATM 3577 O O . HOH Q 7 . ? 37.264 4.966 -11.877 1.00 48.29 ? 477 HOH A O 1 HETATM 3578 O O . HOH Q 7 . ? 55.350 20.682 3.084 1.00 41.33 ? 478 HOH A O 1 HETATM 3579 O O . HOH Q 7 . ? 21.028 24.964 15.754 1.00 37.17 ? 479 HOH A O 1 HETATM 3580 O O . HOH Q 7 . ? 28.066 18.067 -1.511 1.00 16.22 ? 480 HOH A O 1 HETATM 3581 O O . HOH Q 7 . ? 19.666 16.128 11.124 1.00 47.12 ? 481 HOH A O 1 HETATM 3582 O O . HOH Q 7 . ? 55.476 25.711 -1.778 1.00 38.83 ? 482 HOH A O 1 HETATM 3583 O O . HOH Q 7 . ? 15.560 13.744 11.930 1.00 44.85 ? 483 HOH A O 1 HETATM 3584 O O . HOH Q 7 . ? 21.156 25.970 -6.767 1.00 34.76 ? 484 HOH A O 1 HETATM 3585 O O . HOH Q 7 . ? 41.308 17.133 -19.665 1.00 34.27 ? 485 HOH A O 1 HETATM 3586 O O . HOH Q 7 . ? 31.481 10.074 -10.072 1.00 43.98 ? 486 HOH A O 1 HETATM 3587 O O . HOH Q 7 . ? 47.205 49.274 -4.332 1.00 50.14 ? 487 HOH A O 1 HETATM 3588 O O . HOH Q 7 . ? 52.457 49.439 -16.448 1.00 35.54 ? 488 HOH A O 1 HETATM 3589 O O . HOH Q 7 . ? 59.683 33.264 -3.512 1.00 42.71 ? 489 HOH A O 1 HETATM 3590 O O . HOH Q 7 . ? 37.486 34.424 5.546 1.00 46.82 ? 490 HOH A O 1 HETATM 3591 O O . HOH Q 7 . ? 27.104 27.022 18.756 1.00 44.59 ? 491 HOH A O 1 HETATM 3592 O O . HOH Q 7 . ? 22.039 38.206 -7.112 1.00 34.84 ? 492 HOH A O 1 HETATM 3593 O O . HOH Q 7 . ? 30.493 47.289 3.672 1.00 39.55 ? 493 HOH A O 1 HETATM 3594 O O . HOH Q 7 . ? 12.707 24.679 18.334 1.00 41.42 ? 494 HOH A O 1 HETATM 3595 O O . HOH Q 7 . ? 36.765 41.248 -12.928 1.00 18.16 ? 495 HOH A O 1 HETATM 3596 O O . HOH Q 7 . ? 55.908 24.478 0.432 1.00 48.59 ? 496 HOH A O 1 HETATM 3597 O O . HOH Q 7 . ? 51.852 43.078 3.748 1.00 44.82 ? 497 HOH A O 1 HETATM 3598 O O . HOH Q 7 . ? 47.136 29.060 16.658 1.00 48.24 ? 498 HOH A O 1 HETATM 3599 O O . HOH Q 7 . ? 36.459 50.159 -9.753 1.00 40.84 ? 499 HOH A O 1 HETATM 3600 O O . HOH Q 7 . ? 7.332 16.644 3.822 1.00 41.16 ? 500 HOH A O 1 HETATM 3601 O O . HOH Q 7 . ? 22.939 43.579 -7.587 1.00 42.85 ? 501 HOH A O 1 HETATM 3602 O O . HOH Q 7 . ? 21.814 16.160 8.608 1.00 40.83 ? 502 HOH A O 1 HETATM 3603 O O . HOH Q 7 . ? 19.529 42.528 -5.356 1.00 54.45 ? 503 HOH A O 1 HETATM 3604 O O . HOH Q 7 . ? 10.129 22.898 3.126 1.00 47.46 ? 504 HOH A O 1 HETATM 3605 O O . HOH Q 7 . ? 35.517 43.137 4.955 1.00 54.72 ? 505 HOH A O 1 HETATM 3606 O O . HOH Q 7 . ? 19.944 39.893 -6.529 1.00 38.59 ? 506 HOH A O 1 HETATM 3607 O O . HOH Q 7 . ? 22.661 38.069 -9.812 1.00 48.06 ? 507 HOH A O 1 HETATM 3608 O O . HOH Q 7 . ? 25.064 30.148 20.405 1.00 54.89 ? 508 HOH A O 1 HETATM 3609 O O . HOH Q 7 . ? 41.865 20.424 12.158 1.00 46.43 ? 509 HOH A O 1 HETATM 3610 O O . HOH Q 7 . ? 50.804 45.969 -6.702 1.00 39.79 ? 510 HOH A O 1 HETATM 3611 O O . HOH Q 7 . ? 42.077 48.875 -16.957 1.00 48.91 ? 511 HOH A O 1 HETATM 3612 O O . HOH Q 7 . ? 27.429 35.061 -12.744 1.00 33.14 ? 512 HOH A O 1 HETATM 3613 O O . HOH Q 7 . ? 51.583 51.180 -24.764 1.00 54.03 ? 513 HOH A O 1 HETATM 3614 O O . HOH Q 7 . ? 12.571 43.230 -0.084 1.00 47.59 ? 514 HOH A O 1 HETATM 3615 O O . HOH Q 7 . ? 33.030 47.216 -13.971 1.00 46.71 ? 515 HOH A O 1 HETATM 3616 O O . HOH Q 7 . ? 36.370 31.163 4.840 1.00 38.07 ? 516 HOH A O 1 HETATM 3617 O O . HOH Q 7 . ? 34.226 18.239 -11.643 1.00 50.95 ? 517 HOH A O 1 HETATM 3618 O O . HOH Q 7 . ? 35.115 30.041 6.858 1.00 35.71 ? 518 HOH A O 1 HETATM 3619 O O . HOH Q 7 . ? 28.369 29.130 16.340 1.00 57.07 ? 519 HOH A O 1 HETATM 3620 O O . HOH Q 7 . ? 34.018 27.683 10.273 1.00 51.50 ? 520 HOH A O 1 HETATM 3621 O O . HOH Q 7 . ? 8.567 30.759 2.023 1.00 45.24 ? 521 HOH A O 1 HETATM 3622 O O . HOH Q 7 . ? 37.181 47.091 -12.693 1.00 52.53 ? 522 HOH A O 1 HETATM 3623 O O . HOH Q 7 . ? 5.396 29.081 9.753 1.00 49.79 ? 523 HOH A O 1 HETATM 3624 O O . HOH Q 7 . ? 46.929 16.088 8.295 1.00 28.31 ? 524 HOH A O 1 HETATM 3625 O O . HOH Q 7 . ? 37.595 43.735 -13.548 1.00 33.68 ? 525 HOH A O 1 HETATM 3626 O O . HOH Q 7 . ? 26.486 45.960 -0.234 1.00 40.71 ? 526 HOH A O 1 HETATM 3627 O O . HOH Q 7 . ? 52.079 47.194 -17.399 1.00 40.39 ? 527 HOH A O 1 HETATM 3628 O O . HOH Q 7 . ? 51.339 47.778 -24.653 1.00 48.39 ? 528 HOH A O 1 HETATM 3629 O O . HOH Q 7 . ? 31.858 37.730 7.741 1.00 48.10 ? 529 HOH A O 1 HETATM 3630 O O . HOH Q 7 . ? 33.626 52.895 4.563 1.00 47.43 ? 530 HOH A O 1 HETATM 3631 O O . HOH Q 7 . ? 44.889 49.915 -18.084 1.00 54.35 ? 531 HOH A O 1 HETATM 3632 O O . HOH Q 7 . ? 24.102 45.697 2.012 1.00 43.05 ? 532 HOH A O 1 HETATM 3633 O O . HOH Q 7 . ? 49.224 47.982 -4.042 1.00 54.82 ? 533 HOH A O 1 HETATM 3634 O O . HOH Q 7 . ? 10.729 23.913 17.433 1.00 46.53 ? 534 HOH A O 1 HETATM 3635 O O . HOH Q 7 . ? 32.302 13.167 -11.652 1.00 52.49 ? 535 HOH A O 1 HETATM 3636 O O . HOH Q 7 . ? 51.738 15.817 8.015 1.00 37.65 ? 536 HOH A O 1 HETATM 3637 O O . HOH Q 7 . ? 26.145 32.459 10.740 1.00 45.94 ? 537 HOH A O 1 HETATM 3638 O O . HOH Q 7 . ? 40.596 25.223 12.523 1.00 50.07 ? 538 HOH A O 1 HETATM 3639 O O . HOH Q 7 . ? 22.644 41.581 -10.346 1.00 49.56 ? 539 HOH A O 1 HETATM 3640 O O . HOH Q 7 . ? 23.680 16.984 10.779 1.00 50.96 ? 540 HOH A O 1 HETATM 3641 O O . HOH Q 7 . ? 43.323 14.765 11.522 1.00 57.86 ? 541 HOH A O 1 HETATM 3642 O O . HOH Q 7 . ? 26.339 26.503 -11.794 1.00 36.33 ? 542 HOH A O 1 HETATM 3643 O O . HOH Q 7 . ? 26.683 47.404 -5.638 1.00 41.83 ? 543 HOH A O 1 HETATM 3644 O O . HOH Q 7 . ? 30.597 15.567 -7.605 1.00 32.32 ? 544 HOH A O 1 HETATM 3645 O O . HOH Q 7 . ? 36.847 19.844 -18.303 1.00 48.61 ? 545 HOH A O 1 HETATM 3646 O O . HOH Q 7 . ? 2.013 17.477 10.052 1.00 56.39 ? 546 HOH A O 1 HETATM 3647 O O . HOH R 7 . ? 46.089 24.083 -22.987 1.00 12.82 ? 301 HOH B O 1 HETATM 3648 O O . HOH R 7 . ? 37.350 30.015 -8.266 1.00 8.81 ? 302 HOH B O 1 HETATM 3649 O O . HOH R 7 . ? 54.281 17.361 -20.248 1.00 11.81 ? 303 HOH B O 1 HETATM 3650 O O . HOH R 7 . ? 52.604 16.546 -15.876 1.00 11.12 ? 304 HOH B O 1 HETATM 3651 O O . HOH R 7 . ? 50.692 24.734 -21.848 1.00 12.74 ? 305 HOH B O 1 HETATM 3652 O O . HOH R 7 . ? 36.795 35.635 -9.066 1.00 11.63 ? 306 HOH B O 1 HETATM 3653 O O . HOH R 7 . ? 37.677 25.293 -10.428 1.00 11.83 ? 307 HOH B O 1 HETATM 3654 O O . HOH R 7 . ? 52.274 35.337 -12.039 1.00 13.60 ? 308 HOH B O 1 HETATM 3655 O O . HOH R 7 . ? 40.983 29.654 -6.285 1.00 14.13 ? 309 HOH B O 1 HETATM 3656 O O . HOH R 7 . ? 46.518 16.199 -7.044 1.00 14.26 ? 310 HOH B O 1 HETATM 3657 O O . HOH R 7 . ? 53.646 15.493 -18.256 1.00 15.50 ? 311 HOH B O 1 HETATM 3658 O O . HOH R 7 . ? 52.708 26.356 -10.182 1.00 19.70 ? 312 HOH B O 1 HETATM 3659 O O . HOH R 7 . ? 48.520 25.586 -23.437 1.00 15.06 ? 313 HOH B O 1 HETATM 3660 O O . HOH R 7 . ? 60.295 15.437 -15.989 1.00 19.50 ? 314 HOH B O 1 HETATM 3661 O O . HOH R 7 . ? 63.325 19.523 -11.506 1.00 17.87 ? 315 HOH B O 1 HETATM 3662 O O . HOH R 7 . ? 49.090 15.151 -20.887 1.00 18.99 ? 316 HOH B O 1 HETATM 3663 O O . HOH R 7 . ? 39.719 32.954 -18.051 1.00 16.91 ? 317 HOH B O 1 HETATM 3664 O O . HOH R 7 . ? 34.412 40.089 -11.991 1.00 18.36 ? 318 HOH B O 1 HETATM 3665 O O . HOH R 7 . ? 38.504 24.243 -12.885 1.00 15.17 ? 319 HOH B O 1 HETATM 3666 O O . HOH R 7 . ? 41.582 34.191 -20.075 1.00 18.76 ? 320 HOH B O 1 HETATM 3667 O O . HOH R 7 . ? 59.893 37.429 -19.053 1.00 17.60 ? 321 HOH B O 1 HETATM 3668 O O . HOH R 7 . ? 57.179 16.638 -10.281 1.00 18.91 ? 322 HOH B O 1 HETATM 3669 O O . HOH R 7 . ? 33.904 8.863 1.840 1.00 17.38 ? 323 HOH B O 1 HETATM 3670 O O . HOH R 7 . ? 28.528 19.759 6.989 1.00 23.29 ? 324 HOH B O 1 HETATM 3671 O O . HOH R 7 . ? 42.700 48.541 -2.475 1.00 20.28 ? 325 HOH B O 1 HETATM 3672 O O . HOH R 7 . ? 28.212 14.280 5.077 1.00 23.86 ? 326 HOH B O 1 HETATM 3673 O O . HOH R 7 . ? 38.391 38.989 -14.504 1.00 16.53 ? 327 HOH B O 1 HETATM 3674 O O . HOH R 7 . ? 7.643 7.831 1.175 1.00 22.79 ? 328 HOH B O 1 HETATM 3675 O O . HOH R 7 . ? 45.013 46.830 -2.371 1.00 24.68 ? 329 HOH B O 1 HETATM 3676 O O . HOH R 7 . ? 49.759 7.139 -3.871 1.00 20.18 ? 330 HOH B O 1 HETATM 3677 O O . HOH R 7 . ? 9.597 9.466 -15.478 1.00 20.31 ? 331 HOH B O 1 HETATM 3678 O O . HOH R 7 . ? 11.107 16.333 -17.254 1.00 17.38 ? 332 HOH B O 1 HETATM 3679 O O . HOH R 7 . ? 41.475 40.219 -15.181 1.00 18.43 ? 333 HOH B O 1 HETATM 3680 O O . HOH R 7 . ? 14.449 5.271 1.182 1.00 24.69 ? 334 HOH B O 1 HETATM 3681 O O . HOH R 7 . ? 21.381 18.902 -12.558 1.00 20.90 ? 335 HOH B O 1 HETATM 3682 O O . HOH R 7 . ? 61.724 22.716 -23.319 1.00 25.22 ? 336 HOH B O 1 HETATM 3683 O O . HOH R 7 . ? 20.940 1.406 -9.852 1.00 27.06 ? 337 HOH B O 1 HETATM 3684 O O . HOH R 7 . ? 39.783 22.546 -16.669 1.00 19.33 ? 338 HOH B O 1 HETATM 3685 O O . HOH R 7 . ? 15.026 5.038 -12.666 1.00 23.16 ? 339 HOH B O 1 HETATM 3686 O O . HOH R 7 . ? -7.471 13.964 -7.171 1.00 28.44 ? 340 HOH B O 1 HETATM 3687 O O . HOH R 7 . ? 61.735 31.184 -22.494 1.00 25.08 ? 341 HOH B O 1 HETATM 3688 O O . HOH R 7 . ? 41.682 43.046 -15.003 1.00 22.88 ? 342 HOH B O 1 HETATM 3689 O O . HOH R 7 . ? 51.217 25.676 -27.629 1.00 28.37 ? 343 HOH B O 1 HETATM 3690 O O . HOH R 7 . ? 48.746 25.272 -26.237 1.00 26.33 ? 344 HOH B O 1 HETATM 3691 O O . HOH R 7 . ? 25.265 4.318 2.119 1.00 21.74 ? 345 HOH B O 1 HETATM 3692 O O . HOH R 7 . ? 31.698 4.709 0.781 1.00 29.29 ? 346 HOH B O 1 HETATM 3693 O O . HOH R 7 . ? 40.451 31.781 -21.814 1.00 27.36 ? 347 HOH B O 1 HETATM 3694 O O . HOH R 7 . ? 17.946 -1.462 -4.273 1.00 28.73 ? 348 HOH B O 1 HETATM 3695 O O . HOH R 7 . ? 60.688 29.205 -10.060 1.00 25.77 ? 349 HOH B O 1 HETATM 3696 O O . HOH R 7 . ? 10.468 13.710 -18.445 1.00 28.63 ? 350 HOH B O 1 HETATM 3697 O O . HOH R 7 . ? 44.199 32.368 -25.304 1.00 29.94 ? 351 HOH B O 1 HETATM 3698 O O . HOH R 7 . ? 59.779 40.143 -18.818 1.00 37.50 ? 352 HOH B O 1 HETATM 3699 O O . HOH R 7 . ? 45.432 7.143 1.913 1.00 32.80 ? 353 HOH B O 1 HETATM 3700 O O . HOH R 7 . ? 48.451 9.690 -19.258 1.00 26.73 ? 354 HOH B O 1 HETATM 3701 O O . HOH R 7 . ? 34.856 46.962 -2.772 1.00 30.00 ? 355 HOH B O 1 HETATM 3702 O O . HOH R 7 . ? 7.643 15.624 -18.541 1.00 30.06 ? 356 HOH B O 1 HETATM 3703 O O . HOH R 7 . ? 65.944 31.332 -15.711 1.00 29.02 ? 357 HOH B O 1 HETATM 3704 O O . HOH R 7 . ? 3.255 2.330 -10.219 1.00 28.75 ? 358 HOH B O 1 HETATM 3705 O O . HOH R 7 . ? 70.820 20.736 -17.335 1.00 38.66 ? 359 HOH B O 1 HETATM 3706 O O . HOH R 7 . ? 43.030 5.782 -0.740 1.00 23.31 ? 360 HOH B O 1 HETATM 3707 O O . HOH R 7 . ? 27.598 4.999 3.392 1.00 29.43 ? 361 HOH B O 1 HETATM 3708 O O . HOH R 7 . ? -4.930 9.955 -12.812 1.00 28.38 ? 362 HOH B O 1 HETATM 3709 O O . HOH R 7 . ? 1.829 13.977 -15.783 1.00 34.38 ? 363 HOH B O 1 HETATM 3710 O O . HOH R 7 . ? 47.568 29.897 -25.012 1.00 36.21 ? 364 HOH B O 1 HETATM 3711 O O . HOH R 7 . ? 39.952 25.735 -20.592 1.00 36.40 ? 365 HOH B O 1 HETATM 3712 O O . HOH R 7 . ? -8.683 13.389 -16.666 1.00 24.58 ? 366 HOH B O 1 HETATM 3713 O O . HOH R 7 . ? 32.556 40.308 -14.093 1.00 31.45 ? 367 HOH B O 1 HETATM 3714 O O . HOH R 7 . ? 23.219 23.551 -3.410 1.00 24.56 ? 368 HOH B O 1 HETATM 3715 O O . HOH R 7 . ? -3.668 13.040 -14.159 1.00 28.27 ? 369 HOH B O 1 HETATM 3716 O O . HOH R 7 . ? 40.382 3.913 -9.609 1.00 32.56 ? 370 HOH B O 1 HETATM 3717 O O . HOH R 7 . ? 43.853 42.115 -18.608 1.00 43.48 ? 371 HOH B O 1 HETATM 3718 O O . HOH R 7 . ? 53.887 7.969 -5.461 1.00 28.85 ? 372 HOH B O 1 HETATM 3719 O O . HOH R 7 . ? 9.911 6.342 1.842 1.00 27.12 ? 373 HOH B O 1 HETATM 3720 O O . HOH R 7 . ? 22.626 24.200 -7.897 1.00 28.81 ? 374 HOH B O 1 HETATM 3721 O O . HOH R 7 . ? 40.513 36.655 -20.867 1.00 41.55 ? 375 HOH B O 1 HETATM 3722 O O . HOH R 7 . ? 70.683 25.479 -18.773 1.00 27.37 ? 376 HOH B O 1 HETATM 3723 O O . HOH R 7 . ? 47.346 28.049 -23.443 1.00 27.02 ? 377 HOH B O 1 HETATM 3724 O O . HOH R 7 . ? 25.554 14.569 5.493 1.00 39.56 ? 378 HOH B O 1 HETATM 3725 O O . HOH R 7 . ? 36.617 2.420 0.189 1.00 37.41 ? 379 HOH B O 1 HETATM 3726 O O . HOH R 7 . ? -6.123 13.109 -15.201 1.00 27.11 ? 380 HOH B O 1 HETATM 3727 O O . HOH R 7 . ? 17.031 4.074 1.024 1.00 31.80 ? 381 HOH B O 1 HETATM 3728 O O . HOH R 7 . ? 46.797 21.100 -25.407 1.00 30.83 ? 382 HOH B O 1 HETATM 3729 O O . HOH R 7 . ? 16.669 24.098 -8.818 1.00 34.22 ? 383 HOH B O 1 HETATM 3730 O O . HOH R 7 . ? 55.330 16.033 -6.226 1.00 35.05 ? 384 HOH B O 1 HETATM 3731 O O . HOH R 7 . ? 34.019 6.134 1.307 1.00 31.68 ? 385 HOH B O 1 HETATM 3732 O O . HOH R 7 . ? 62.152 33.478 -9.561 1.00 33.39 ? 386 HOH B O 1 HETATM 3733 O O . HOH R 7 . ? 13.052 -0.812 -3.574 1.00 28.57 ? 387 HOH B O 1 HETATM 3734 O O . HOH R 7 . ? 25.032 20.166 -8.892 1.00 46.38 ? 388 HOH B O 1 HETATM 3735 O O . HOH R 7 . ? 48.013 6.025 -8.054 1.00 30.78 ? 389 HOH B O 1 HETATM 3736 O O . HOH R 7 . ? 28.926 15.393 7.405 1.00 38.05 ? 390 HOH B O 1 HETATM 3737 O O . HOH R 7 . ? 23.414 0.966 -10.116 1.00 35.83 ? 391 HOH B O 1 HETATM 3738 O O . HOH R 7 . ? 26.716 7.373 5.118 1.00 40.06 ? 392 HOH B O 1 HETATM 3739 O O . HOH R 7 . ? 48.931 4.748 -18.074 1.00 34.38 ? 393 HOH B O 1 HETATM 3740 O O . HOH R 7 . ? 24.084 19.349 -12.352 1.00 32.92 ? 394 HOH B O 1 HETATM 3741 O O . HOH R 7 . ? 62.401 36.618 -18.380 1.00 32.83 ? 395 HOH B O 1 HETATM 3742 O O . HOH R 7 . ? 50.422 31.353 -26.151 1.00 40.96 ? 396 HOH B O 1 HETATM 3743 O O . HOH R 7 . ? 43.431 43.679 -16.579 1.00 38.84 ? 397 HOH B O 1 HETATM 3744 O O . HOH R 7 . ? 32.221 7.530 -6.307 1.00 34.55 ? 398 HOH B O 1 HETATM 3745 O O . HOH R 7 . ? 7.142 1.756 -0.850 1.00 24.12 ? 399 HOH B O 1 HETATM 3746 O O . HOH R 7 . ? 23.513 18.297 4.270 1.00 31.40 ? 400 HOH B O 1 HETATM 3747 O O . HOH R 7 . ? 44.556 24.549 -24.917 1.00 34.40 ? 401 HOH B O 1 HETATM 3748 O O . HOH R 7 . ? 5.567 -0.436 -7.477 1.00 39.61 ? 402 HOH B O 1 HETATM 3749 O O . HOH R 7 . ? 11.076 18.699 0.961 1.00 37.54 ? 403 HOH B O 1 HETATM 3750 O O . HOH R 7 . ? 55.936 12.733 -17.790 1.00 27.75 ? 404 HOH B O 1 HETATM 3751 O O . HOH R 7 . ? 6.901 8.974 3.854 1.00 39.36 ? 405 HOH B O 1 HETATM 3752 O O . HOH R 7 . ? 28.719 10.935 -10.689 1.00 31.94 ? 406 HOH B O 1 HETATM 3753 O O . HOH R 7 . ? 63.826 37.877 -16.181 1.00 35.04 ? 407 HOH B O 1 HETATM 3754 O O . HOH R 7 . ? 25.089 20.584 11.508 1.00 51.26 ? 408 HOH B O 1 HETATM 3755 O O . HOH R 7 . ? 65.038 18.773 -19.741 1.00 37.65 ? 409 HOH B O 1 HETATM 3756 O O . HOH R 7 . ? 20.009 -0.676 -10.925 1.00 42.70 ? 410 HOH B O 1 HETATM 3757 O O . HOH R 7 . ? 11.085 11.530 -16.677 1.00 32.06 ? 411 HOH B O 1 HETATM 3758 O O . HOH R 7 . ? -5.614 16.210 -7.490 1.00 39.27 ? 412 HOH B O 1 HETATM 3759 O O . HOH R 7 . ? 26.081 10.495 5.124 1.00 33.72 ? 413 HOH B O 1 HETATM 3760 O O . HOH R 7 . ? 5.096 6.832 0.055 1.00 44.75 ? 414 HOH B O 1 HETATM 3761 O O . HOH R 7 . ? 66.964 28.961 -14.492 1.00 40.93 ? 415 HOH B O 1 HETATM 3762 O O . HOH R 7 . ? 65.971 27.621 -12.383 1.00 39.34 ? 416 HOH B O 1 HETATM 3763 O O . HOH R 7 . ? 67.260 26.495 -16.597 1.00 29.11 ? 417 HOH B O 1 HETATM 3764 O O . HOH R 7 . ? 43.055 38.152 -24.537 1.00 46.79 ? 418 HOH B O 1 HETATM 3765 O O . HOH R 7 . ? 53.134 31.682 -24.606 1.00 19.90 ? 419 HOH B O 1 HETATM 3766 O O . HOH R 7 . ? 55.457 30.146 -24.691 1.00 26.66 ? 420 HOH B O 1 HETATM 3767 O O . HOH R 7 . ? 47.721 22.672 -27.494 1.00 30.51 ? 421 HOH B O 1 HETATM 3768 O O . HOH R 7 . ? 28.495 11.518 4.698 1.00 28.39 ? 422 HOH B O 1 HETATM 3769 O O . HOH R 7 . ? 5.215 8.940 -20.911 1.00 43.07 ? 423 HOH B O 1 HETATM 3770 O O . HOH R 7 . ? 35.337 46.064 5.199 1.00 46.46 ? 424 HOH B O 1 HETATM 3771 O O . HOH R 7 . ? 23.039 5.700 2.743 1.00 33.25 ? 425 HOH B O 1 HETATM 3772 O O . HOH R 7 . ? 45.259 39.079 -24.691 1.00 27.57 ? 426 HOH B O 1 HETATM 3773 O O . HOH R 7 . ? 50.078 5.462 -5.932 1.00 43.87 ? 427 HOH B O 1 HETATM 3774 O O . HOH R 7 . ? 42.528 39.866 -22.568 1.00 45.33 ? 428 HOH B O 1 HETATM 3775 O O . HOH R 7 . ? 51.778 9.793 -17.849 1.00 41.21 ? 429 HOH B O 1 HETATM 3776 O O . HOH R 7 . ? 11.569 -0.442 -14.340 1.00 41.70 ? 430 HOH B O 1 HETATM 3777 O O . HOH R 7 . ? 21.692 22.285 -9.798 1.00 41.76 ? 431 HOH B O 1 HETATM 3778 O O . HOH R 7 . ? 65.333 18.310 -12.807 1.00 37.47 ? 432 HOH B O 1 HETATM 3779 O O . HOH R 7 . ? 5.004 21.928 -11.391 1.00 40.66 ? 433 HOH B O 1 HETATM 3780 O O . HOH R 7 . ? 23.601 10.351 3.367 1.00 25.61 ? 434 HOH B O 1 HETATM 3781 O O . HOH R 7 . ? 40.399 3.358 -7.028 1.00 46.31 ? 435 HOH B O 1 HETATM 3782 O O . HOH R 7 . ? 45.443 40.520 -20.770 1.00 29.98 ? 436 HOH B O 1 HETATM 3783 O O . HOH R 7 . ? 35.531 38.059 -16.121 1.00 40.17 ? 437 HOH B O 1 HETATM 3784 O O . HOH R 7 . ? 43.554 2.584 -13.697 1.00 41.85 ? 438 HOH B O 1 HETATM 3785 O O . HOH R 7 . ? 29.690 13.321 -8.147 1.00 22.15 ? 439 HOH B O 1 HETATM 3786 O O . HOH R 7 . ? 40.396 24.048 -18.847 1.00 46.01 ? 440 HOH B O 1 HETATM 3787 O O . HOH R 7 . ? 56.853 39.286 -22.608 1.00 45.85 ? 441 HOH B O 1 HETATM 3788 O O . HOH R 7 . ? 54.668 41.238 -22.817 1.00 40.15 ? 442 HOH B O 1 HETATM 3789 O O . HOH R 7 . ? 16.448 1.543 1.108 1.00 44.11 ? 443 HOH B O 1 HETATM 3790 O O . HOH R 7 . ? 14.049 11.285 1.396 1.00 19.37 ? 444 HOH B O 1 HETATM 3791 O O . HOH R 7 . ? 40.865 34.238 -22.370 1.00 41.79 ? 445 HOH B O 1 HETATM 3792 O O . HOH R 7 . ? 40.074 20.572 -18.961 1.00 43.36 ? 446 HOH B O 1 HETATM 3793 O O . HOH R 7 . ? -0.000 11.996 -19.379 0.50 44.93 ? 447 HOH B O 1 HETATM 3794 O O . HOH R 7 . ? 19.144 13.149 -13.369 1.00 41.66 ? 448 HOH B O 1 HETATM 3795 O O . HOH R 7 . ? 20.418 14.764 -12.033 1.00 51.65 ? 449 HOH B O 1 HETATM 3796 O O . HOH R 7 . ? 28.381 14.782 -9.976 1.00 54.40 ? 450 HOH B O 1 HETATM 3797 O O . HOH R 7 . ? 19.278 25.851 -8.224 1.00 45.50 ? 451 HOH B O 1 HETATM 3798 O O . HOH R 7 . ? 41.743 -4.894 -18.388 1.00 49.96 ? 452 HOH B O 1 HETATM 3799 O O . HOH R 7 . ? 23.800 22.802 -5.878 1.00 24.70 ? 453 HOH B O 1 HETATM 3800 O O . HOH R 7 . ? 37.806 37.360 -17.305 1.00 43.82 ? 454 HOH B O 1 HETATM 3801 O O . HOH R 7 . ? 2.144 16.072 1.730 1.00 45.06 ? 455 HOH B O 1 HETATM 3802 O O . HOH R 7 . ? 54.454 10.563 -17.624 1.00 36.35 ? 456 HOH B O 1 HETATM 3803 O O . HOH R 7 . ? 62.194 25.990 -22.654 1.00 39.48 ? 457 HOH B O 1 HETATM 3804 O O . HOH R 7 . ? 30.117 5.581 2.888 1.00 45.16 ? 458 HOH B O 1 HETATM 3805 O O . HOH R 7 . ? 21.307 7.684 2.872 1.00 46.27 ? 459 HOH B O 1 HETATM 3806 O O . HOH R 7 . ? -5.212 4.309 -0.276 1.00 44.38 ? 460 HOH B O 1 HETATM 3807 O O . HOH R 7 . ? 60.401 24.015 -26.875 1.00 54.36 ? 461 HOH B O 1 HETATM 3808 O O . HOH R 7 . ? 23.253 18.633 12.743 1.00 44.78 ? 462 HOH B O 1 HETATM 3809 O O . HOH R 7 . ? 25.459 10.910 7.553 1.00 47.16 ? 463 HOH B O 1 HETATM 3810 O O . HOH R 7 . ? -3.296 2.870 -14.935 1.00 50.22 ? 464 HOH B O 1 HETATM 3811 O O . HOH R 7 . ? 43.497 35.587 -24.927 1.00 39.65 ? 465 HOH B O 1 HETATM 3812 O O . HOH R 7 . ? 30.346 5.761 -9.706 1.00 37.61 ? 466 HOH B O 1 HETATM 3813 O O . HOH R 7 . ? 37.764 1.828 2.093 1.00 52.30 ? 467 HOH B O 1 HETATM 3814 O O . HOH R 7 . ? 52.122 41.497 -20.586 1.00 34.78 ? 468 HOH B O 1 HETATM 3815 O O . HOH R 7 . ? 52.731 7.987 -8.748 1.00 39.08 ? 469 HOH B O 1 HETATM 3816 O O . HOH R 7 . ? -0.202 12.693 -16.670 1.00 44.93 ? 470 HOH B O 1 HETATM 3817 O O . HOH R 7 . ? -14.437 6.697 -11.273 1.00 48.88 ? 471 HOH B O 1 HETATM 3818 O O . HOH R 7 . ? 34.697 41.495 -15.687 1.00 47.57 ? 472 HOH B O 1 HETATM 3819 O O . HOH R 7 . ? 22.707 13.095 -11.830 1.00 26.24 ? 473 HOH B O 1 HETATM 3820 O O . HOH R 7 . ? 15.323 11.664 3.955 1.00 36.60 ? 474 HOH B O 1 HETATM 3821 O O . HOH R 7 . ? 37.487 33.667 -17.036 1.00 32.33 ? 475 HOH B O 1 HETATM 3822 O O . HOH R 7 . ? 67.288 20.598 -13.686 1.00 32.17 ? 476 HOH B O 1 HETATM 3823 O O . HOH R 7 . ? 32.392 7.352 -8.520 1.00 37.77 ? 477 HOH B O 1 HETATM 3824 O O . HOH R 7 . ? 43.539 3.604 -11.469 1.00 48.33 ? 478 HOH B O 1 HETATM 3825 O O . HOH R 7 . ? 33.051 1.536 -3.294 1.00 39.08 ? 479 HOH B O 1 HETATM 3826 O O . HOH R 7 . ? 43.028 50.223 -0.409 1.00 46.08 ? 480 HOH B O 1 HETATM 3827 O O . HOH R 7 . ? 20.660 4.641 -15.013 1.00 44.38 ? 481 HOH B O 1 HETATM 3828 O O . HOH R 7 . ? 39.023 28.447 -20.298 1.00 46.59 ? 482 HOH B O 1 HETATM 3829 O O . HOH R 7 . ? 43.715 49.883 1.955 1.00 52.00 ? 483 HOH B O 1 HETATM 3830 O O . HOH R 7 . ? 42.715 14.863 -22.137 1.00 38.23 ? 484 HOH B O 1 HETATM 3831 O O . HOH R 7 . ? 38.825 5.119 3.220 1.00 41.30 ? 485 HOH B O 1 HETATM 3832 O O . HOH R 7 . ? 17.086 4.370 3.924 1.00 47.23 ? 486 HOH B O 1 HETATM 3833 O O . HOH R 7 . ? 23.631 19.000 15.250 1.00 53.03 ? 487 HOH B O 1 HETATM 3834 O O . HOH R 7 . ? 2.656 -2.580 -3.178 1.00 42.47 ? 488 HOH B O 1 HETATM 3835 O O . HOH R 7 . ? 4.550 23.036 -4.395 1.00 51.57 ? 489 HOH B O 1 HETATM 3836 O O . HOH R 7 . ? 67.420 29.834 -19.379 0.50 23.75 ? 490 HOH B O 1 HETATM 3837 O O . HOH R 7 . ? 40.577 30.497 -19.529 1.00 29.45 ? 491 HOH B O 1 HETATM 3838 O O . HOH R 7 . ? 58.470 30.511 -23.940 1.00 33.11 ? 492 HOH B O 1 HETATM 3839 O O . HOH R 7 . ? 33.422 9.382 -6.781 1.00 33.58 ? 493 HOH B O 1 HETATM 3840 O O . HOH R 7 . ? 0.077 26.616 -10.115 1.00 49.93 ? 494 HOH B O 1 HETATM 3841 O O . HOH R 7 . ? 1.595 21.990 -1.083 1.00 49.21 ? 495 HOH B O 1 HETATM 3842 O O . HOH R 7 . ? 8.342 -0.525 -3.100 1.00 46.74 ? 496 HOH B O 1 HETATM 3843 O O . HOH R 7 . ? 13.188 23.317 -10.615 1.00 42.69 ? 497 HOH B O 1 HETATM 3844 O O . HOH R 7 . ? 45.718 4.517 -7.618 1.00 37.16 ? 498 HOH B O 1 HETATM 3845 O O . HOH R 7 . ? 66.834 31.732 -21.213 1.00 51.45 ? 499 HOH B O 1 HETATM 3846 O O . HOH R 7 . ? 12.214 9.914 -18.702 1.00 50.60 ? 500 HOH B O 1 HETATM 3847 O O . HOH R 7 . ? -5.548 14.425 -4.809 1.00 41.42 ? 501 HOH B O 1 HETATM 3848 O O . HOH R 7 . ? 13.630 2.160 -15.863 1.00 49.37 ? 502 HOH B O 1 HETATM 3849 O O . HOH R 7 . ? 63.585 34.606 -20.090 1.00 43.76 ? 503 HOH B O 1 HETATM 3850 O O . HOH S 7 . ? 60.190 31.779 -10.723 1.00 16.81 ? 101 HOH C O 1 HETATM 3851 O O . HOH S 7 . ? 51.811 16.603 2.974 1.00 28.65 ? 102 HOH C O 1 HETATM 3852 O O . HOH S 7 . ? 53.898 18.123 -6.392 1.00 21.41 ? 103 HOH C O 1 HETATM 3853 O O . HOH S 7 . ? 55.843 21.173 -6.635 1.00 25.91 ? 104 HOH C O 1 HETATM 3854 O O . HOH S 7 . ? 56.569 44.104 -10.755 1.00 25.61 ? 105 HOH C O 1 HETATM 3855 O O . HOH S 7 . ? 53.029 9.439 1.251 1.00 37.73 ? 106 HOH C O 1 HETATM 3856 O O . HOH S 7 . ? 52.824 18.559 0.654 1.00 31.00 ? 107 HOH C O 1 HETATM 3857 O O . HOH S 7 . ? 54.685 17.796 -0.752 1.00 37.32 ? 108 HOH C O 1 HETATM 3858 O O . HOH S 7 . ? 56.024 41.099 -5.805 1.00 29.14 ? 109 HOH C O 1 HETATM 3859 O O . HOH S 7 . ? 54.536 11.849 -0.193 1.00 37.30 ? 110 HOH C O 1 HETATM 3860 O O . HOH S 7 . ? 54.201 16.035 2.973 1.00 37.94 ? 111 HOH C O 1 HETATM 3861 O O . HOH S 7 . ? 55.066 14.255 0.904 1.00 42.68 ? 112 HOH C O 1 HETATM 3862 O O . HOH S 7 . ? 54.339 9.792 3.488 1.00 48.85 ? 113 HOH C O 1 HETATM 3863 O O . HOH S 7 . ? 62.251 41.198 -12.830 1.00 40.67 ? 114 HOH C O 1 HETATM 3864 O O . HOH S 7 . ? 58.411 37.167 -7.945 1.00 34.13 ? 115 HOH C O 1 HETATM 3865 O O . HOH S 7 . ? 61.795 38.410 -11.310 1.00 31.61 ? 116 HOH C O 1 HETATM 3866 O O . HOH S 7 . ? 60.966 36.277 -7.166 1.00 38.34 ? 117 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 ? 0.6692 0.5358 0.6146 -0.0737 -0.0516 -0.1099 3 GLU A N 2 C CA A GLU A 3 ? 0.6380 0.5018 0.6001 -0.0699 -0.0356 -0.0974 3 GLU A CA 3 C CA B GLU A 3 ? 0.6442 0.5076 0.6063 -0.0699 -0.0354 -0.0976 3 GLU A CA 4 C C . GLU A 3 ? 0.6114 0.4878 0.6174 -0.0755 -0.0335 -0.0910 3 GLU A C 5 O O . GLU A 3 ? 0.7089 0.6005 0.7329 -0.0803 -0.0476 -0.0903 3 GLU A O 6 C CB A GLU A 3 ? 0.6041 0.4803 0.5543 -0.0638 -0.0303 -0.0859 3 GLU A CB 7 C CB B GLU A 3 ? 0.6122 0.4874 0.5621 -0.0638 -0.0294 -0.0861 3 GLU A CB 8 C CG A GLU A 3 ? 0.5914 0.4828 0.5295 -0.0619 -0.0493 -0.0829 3 GLU A CG 9 C CG B GLU A 3 ? 0.5639 0.4621 0.5327 -0.0640 -0.0451 -0.0783 3 GLU A CG 10 C CD A GLU A 3 ? 0.6340 0.5128 0.5288 -0.0585 -0.0515 -0.0866 3 GLU A CD 11 C CD B GLU A 3 ? 0.5591 0.4643 0.5009 -0.0568 -0.0497 -0.0707 3 GLU A CD 12 O OE1 A GLU A 3 ? 0.6434 0.5141 0.5156 -0.0527 -0.0382 -0.0810 3 GLU A OE1 13 O OE1 B GLU A 3 ? 0.5106 0.4332 0.4616 -0.0551 -0.0642 -0.0654 3 GLU A OE1 14 O OE2 A GLU A 3 ? 0.6402 0.5163 0.5245 -0.0624 -0.0652 -0.0943 3 GLU A OE2 15 O OE2 B GLU A 3 ? 0.3618 0.2557 0.2775 -0.0523 -0.0360 -0.0689 3 GLU A OE2 16 N N . GLU A 4 ? 0.5720 0.4505 0.6040 -0.0714 -0.0112 -0.0854 4 GLU A N 17 C CA . GLU A 4 ? 0.4992 0.3936 0.5789 -0.0709 -0.0043 -0.0771 4 GLU A CA 18 C C . GLU A 4 ? 0.3109 0.2261 0.4108 -0.0637 0.0011 -0.0624 4 GLU A C 19 O O . GLU A 4 ? 0.3166 0.2486 0.4465 -0.0633 -0.0027 -0.0554 4 GLU A O 20 C CB . GLU A 4 ? 0.5349 0.4193 0.6297 -0.0685 0.0169 -0.0753 4 GLU A CB 21 C CG . GLU A 4 ? 0.6566 0.5210 0.7411 -0.0762 0.0132 -0.0895 4 GLU A CG 22 C CD . GLU A 4 ? 0.7156 0.5746 0.8235 -0.0730 0.0351 -0.0862 4 GLU A CD 23 O OE1 . GLU A 4 ? 0.6552 0.5237 0.7796 -0.0637 0.0523 -0.0719 4 GLU A OE1 24 O OE2 . GLU A 4 ? 0.7733 0.6178 0.8820 -0.0795 0.0342 -0.0972 4 GLU A OE2 25 N N . HIS A 5 ? 0.2300 0.1466 0.3074 -0.0549 0.0104 -0.0539 5 HIS A N 26 C CA . HIS A 5 ? 0.1820 0.1185 0.2665 -0.0450 0.0147 -0.0369 5 HIS A CA 27 C C . HIS A 5 ? 0.1749 0.1143 0.2275 -0.0388 0.0124 -0.0337 5 HIS A C 28 O O . HIS A 5 ? 0.1895 0.1142 0.2187 -0.0397 0.0158 -0.0409 5 HIS A O 29 C CB . HIS A 5 ? 0.1695 0.1067 0.2758 -0.0382 0.0339 -0.0241 5 HIS A CB 30 C CG . HIS A 5 ? 0.2047 0.1382 0.3465 -0.0432 0.0408 -0.0246 5 HIS A CG 31 N ND1 . HIS A 5 ? 0.1773 0.1228 0.3448 -0.0452 0.0374 -0.0206 5 HIS A ND1 32 C CD2 . HIS A 5 ? 0.2150 0.1359 0.3709 -0.0452 0.0517 -0.0283 5 HIS A CD2 33 C CE1 . HIS A 5 ? 0.2026 0.1452 0.3950 -0.0466 0.0451 -0.0214 5 HIS A CE1 34 N NE2 . HIS A 5 ? 0.2247 0.1532 0.4097 -0.0466 0.0531 -0.0260 5 HIS A NE2 35 N N . VAL A 6 ? 0.1503 0.1071 0.2036 -0.0328 0.0087 -0.0234 6 VAL A N 36 C CA . VAL A 6 ? 0.1422 0.1030 0.1715 -0.0270 0.0075 -0.0197 6 VAL A CA 37 C C . VAL A 6 ? 0.1533 0.1279 0.1913 -0.0182 0.0138 -0.0056 6 VAL A C 38 O O . VAL A 6 ? 0.1667 0.1505 0.2190 -0.0167 0.0140 0.0009 6 VAL A O 39 C CB . VAL A 6 ? 0.1441 0.1085 0.1557 -0.0296 -0.0081 -0.0244 6 VAL A CB 40 C CG1 . VAL A 6 ? 0.1652 0.1321 0.1553 -0.0241 -0.0069 -0.0208 6 VAL A CG1 41 C CG2 . VAL A 6 ? 0.2326 0.1800 0.2277 -0.0381 -0.0179 -0.0383 6 VAL A CG2 42 N N . ILE A 7 ? 0.1203 0.0947 0.1499 -0.0124 0.0192 -0.0011 7 ILE A N 43 C CA . ILE A 7 ? 0.1091 0.0947 0.1400 -0.0043 0.0205 0.0108 7 ILE A CA 44 C C . ILE A 7 ? 0.1201 0.1113 0.1347 -0.0024 0.0140 0.0089 7 ILE A C 45 O O . ILE A 7 ? 0.1217 0.1064 0.1302 -0.0035 0.0161 0.0036 7 ILE A O 46 C CB . ILE A 7 ? 0.1133 0.0953 0.1556 0.0017 0.0294 0.0193 7 ILE A CB 47 C CG1 . ILE A 7 ? 0.1222 0.0964 0.1826 0.0001 0.0385 0.0221 7 ILE A CG1 48 C CG2 . ILE A 7 ? 0.1108 0.1024 0.1473 0.0101 0.0257 0.0308 7 ILE A CG2 49 C CD1 . ILE A 7 ? 0.1515 0.1199 0.2252 0.0066 0.0480 0.0317 7 ILE A CD1 50 N N . ILE A 8 ? 0.0943 0.0954 0.1028 0.0002 0.0085 0.0128 8 ILE A N 51 C CA . ILE A 8 ? 0.0887 0.0946 0.0845 0.0014 0.0029 0.0106 8 ILE A CA 52 C C . ILE A 8 ? 0.0949 0.1086 0.0879 0.0076 0.0007 0.0177 8 ILE A C 53 O O . ILE A 8 ? 0.1207 0.1364 0.1114 0.0102 0.0018 0.0233 8 ILE A O 54 C CB . ILE A 8 ? 0.0995 0.1075 0.0877 -0.0022 -0.0038 0.0060 8 ILE A CB 55 C CG1 . ILE A 8 ? 0.1170 0.1151 0.1024 -0.0085 -0.0066 -0.0017 8 ILE A CG1 56 C CG2 . ILE A 8 ? 0.1442 0.1552 0.1209 -0.0006 -0.0073 0.0045 8 ILE A CG2 57 C CD1 . ILE A 8 ? 0.1289 0.1292 0.1100 -0.0114 -0.0170 -0.0046 8 ILE A CD1 58 N N . GLN A 9 ? 0.0837 0.0998 0.0766 0.0096 -0.0019 0.0169 9 GLN A N 59 C CA . GLN A 9 ? 0.0988 0.1218 0.0865 0.0140 -0.0086 0.0204 9 GLN A CA 60 C C . GLN A 9 ? 0.1055 0.1311 0.0845 0.0112 -0.0119 0.0140 9 GLN A C 61 O O . GLN A 9 ? 0.0881 0.1122 0.0706 0.0088 -0.0108 0.0090 9 GLN A O 62 C CB . GLN A 9 ? 0.1143 0.1401 0.1163 0.0171 -0.0114 0.0225 9 GLN A CB 63 C CG . GLN A 9 ? 0.0895 0.1226 0.0889 0.0203 -0.0230 0.0237 9 GLN A CG 64 C CD . GLN A 9 ? 0.1048 0.1430 0.1290 0.0226 -0.0273 0.0252 9 GLN A CD 65 O OE1 . GLN A 9 ? 0.1273 0.1633 0.1683 0.0251 -0.0222 0.0303 9 GLN A OE1 66 N NE2 . GLN A 9 ? 0.1136 0.1586 0.1452 0.0218 -0.0361 0.0208 9 GLN A NE2 67 N N . ALA A 10 ? 0.0856 0.1125 0.0538 0.0120 -0.0131 0.0148 10 ALA A N 68 C CA . ALA A 10 ? 0.0865 0.1145 0.0489 0.0099 -0.0147 0.0097 10 ALA A CA 69 C C . ALA A 10 ? 0.1150 0.1437 0.0694 0.0117 -0.0187 0.0082 10 ALA A C 70 O O . ALA A 10 ? 0.1376 0.1626 0.0832 0.0141 -0.0189 0.0114 10 ALA A O 71 C CB . ALA A 10 ? 0.1037 0.1308 0.0666 0.0086 -0.0114 0.0106 10 ALA A CB 72 N N . GLU A 11 ? 0.0914 0.1207 0.0487 0.0096 -0.0207 0.0028 11 GLU A N 73 C CA . GLU A 11 ? 0.0875 0.1152 0.0408 0.0092 -0.0251 -0.0008 11 GLU A CA 74 C C . GLU A 11 ? 0.0938 0.1197 0.0461 0.0074 -0.0218 -0.0053 11 GLU A C 75 O O . GLU A 11 ? 0.1076 0.1344 0.0642 0.0065 -0.0187 -0.0057 11 GLU A O 76 C CB . GLU A 11 ? 0.1194 0.1545 0.0844 0.0097 -0.0333 -0.0035 11 GLU A CB 77 C CG . GLU A 11 ? 0.1144 0.1539 0.0868 0.0132 -0.0380 0.0022 11 GLU A CG 78 C CD . GLU A 11 ? 0.1595 0.2045 0.1589 0.0123 -0.0408 0.0004 11 GLU A CD 79 O OE1 . GLU A 11 ? 0.1397 0.1870 0.1501 0.0094 -0.0429 -0.0059 11 GLU A OE1 80 O OE2 . GLU A 11 ? 0.1417 0.1880 0.1551 0.0144 -0.0393 0.0055 11 GLU A OE2 81 N N . PHE A 12 ? 0.1042 0.1263 0.0477 0.0072 -0.0225 -0.0087 12 PHE A N 82 C CA . PHE A 12 ? 0.0949 0.1165 0.0391 0.0065 -0.0203 -0.0146 12 PHE A CA 83 C C . PHE A 12 ? 0.1343 0.1522 0.0721 0.0050 -0.0250 -0.0221 12 PHE A C 84 O O . PHE A 12 ? 0.1375 0.1513 0.0642 0.0045 -0.0294 -0.0213 12 PHE A O 85 C CB . PHE A 12 ? 0.1204 0.1408 0.0611 0.0086 -0.0128 -0.0125 12 PHE A CB 86 C CG . PHE A 12 ? 0.1172 0.1320 0.0447 0.0112 -0.0073 -0.0125 12 PHE A CG 87 C CD1 . PHE A 12 ? 0.1602 0.1669 0.0761 0.0111 -0.0047 -0.0197 12 PHE A CD1 88 C CD2 . PHE A 12 ? 0.1706 0.1859 0.0971 0.0136 -0.0021 -0.0059 12 PHE A CD2 89 C CE1 . PHE A 12 ? 0.2107 0.2075 0.1112 0.0133 0.0045 -0.0199 12 PHE A CE1 90 C CE2 . PHE A 12 ? 0.1836 0.1905 0.0985 0.0164 0.0080 -0.0051 12 PHE A CE2 91 C CZ . PHE A 12 ? 0.1965 0.1931 0.0956 0.0166 0.0120 -0.0121 12 PHE A CZ 92 N N . TYR A 13 ? 0.1084 0.1267 0.0535 0.0035 -0.0243 -0.0298 13 TYR A N 93 C CA . TYR A 13 ? 0.1252 0.1375 0.0650 0.0011 -0.0278 -0.0397 13 TYR A CA 94 C C . TYR A 13 ? 0.1250 0.1305 0.0698 0.0007 -0.0166 -0.0424 13 TYR A C 95 O O . TYR A 13 ? 0.1333 0.1403 0.0938 0.0004 -0.0106 -0.0380 13 TYR A O 96 C CB . TYR A 13 ? 0.1261 0.1439 0.0843 -0.0027 -0.0387 -0.0458 13 TYR A CB 97 C CG . TYR A 13 ? 0.1492 0.1591 0.1006 -0.0065 -0.0449 -0.0545 13 TYR A CG 98 C CD1 . TYR A 13 ? 0.1910 0.1978 0.1248 -0.0074 -0.0536 -0.0524 13 TYR A CD1 99 C CD2 . TYR A 13 ? 0.1706 0.1752 0.1324 -0.0098 -0.0409 -0.0652 13 TYR A CD2 100 C CE1 . TYR A 13 ? 0.2911 0.2903 0.2141 -0.0118 -0.0601 -0.0614 13 TYR A CE1 101 C CE2 . TYR A 13 ? 0.2479 0.2434 0.2020 -0.0141 -0.0465 -0.0739 13 TYR A CE2 102 C CZ . TYR A 13 ? 0.2793 0.2720 0.2118 -0.0154 -0.0569 -0.0723 13 TYR A CZ 103 O OH . TYR A 13 ? 0.3214 0.3047 0.2422 -0.0208 -0.0633 -0.0823 13 TYR A OH 104 N N . LEU A 14 ? 0.1438 0.1392 0.0732 0.0010 -0.0127 -0.0489 14 LEU A N 105 C CA . LEU A 14 ? 0.1460 0.1336 0.0822 0.0016 0.0001 -0.0502 14 LEU A CA 106 C C . LEU A 14 ? 0.1668 0.1435 0.1000 -0.0024 0.0001 -0.0641 14 LEU A C 107 O O . LEU A 14 ? 0.1912 0.1591 0.1009 -0.0035 -0.0052 -0.0721 14 LEU A O 108 C CB . LEU A 14 ? 0.1520 0.1347 0.0769 0.0062 0.0105 -0.0448 14 LEU A CB 109 C CG . LEU A 14 ? 0.1767 0.1512 0.1127 0.0083 0.0248 -0.0450 14 LEU A CG 110 C CD1 . LEU A 14 ? 0.1609 0.1429 0.1216 0.0099 0.0257 -0.0351 14 LEU A CD1 111 C CD2 . LEU A 14 ? 0.1805 0.1486 0.1072 0.0125 0.0367 -0.0419 14 LEU A CD2 112 N N . ASN A 15 ? 0.1615 0.1358 0.1166 -0.0044 0.0064 -0.0661 15 ASN A N 113 C CA . ASN A 15 ? 0.1815 0.1435 0.1393 -0.0086 0.0098 -0.0797 15 ASN A CA 114 C C . ASN A 15 ? 0.1867 0.1379 0.1485 -0.0049 0.0274 -0.0772 15 ASN A C 115 O O . ASN A 15 ? 0.1888 0.1451 0.1634 -0.0001 0.0341 -0.0639 15 ASN A O 116 C CB . ASN A 15 ? 0.1952 0.1606 0.1818 -0.0136 0.0072 -0.0834 15 ASN A CB 117 C CG . ASN A 15 ? 0.2798 0.2520 0.2700 -0.0190 -0.0106 -0.0926 15 ASN A CG 118 O OD1 . ASN A 15 ? 0.2558 0.2237 0.2219 -0.0197 -0.0216 -0.0958 15 ASN A OD1 119 N ND2 . ASN A 15 ? 0.2074 0.1883 0.2278 -0.0217 -0.0122 -0.0901 15 ASN A ND2 120 N N . PRO A 16 ? 0.2127 0.1486 0.1655 -0.0068 0.0334 -0.0886 16 PRO A N 121 C CA . PRO A 16 ? 0.2393 0.1676 0.1763 -0.0115 0.0211 -0.1005 16 PRO A CA 122 C C . PRO A 16 ? 0.2687 0.1909 0.1686 -0.0079 0.0138 -0.1013 16 PRO A C 123 O O . PRO A 16 ? 0.2931 0.2045 0.1731 -0.0097 0.0020 -0.1110 16 PRO A O 124 C CB . PRO A 16 ? 0.2582 0.1723 0.2040 -0.0128 0.0332 -0.1072 16 PRO A CB 125 C CG . PRO A 16 ? 0.2508 0.1627 0.2019 -0.0062 0.0516 -0.0971 16 PRO A CG 126 C CD . PRO A 16 ? 0.2183 0.1444 0.1831 -0.0030 0.0512 -0.0850 16 PRO A CD 127 N N . ASP A 17 ? 0.2506 0.1791 0.1426 -0.0024 0.0203 -0.0911 17 ASP A N 128 C CA . ASP A 17 ? 0.2703 0.1972 0.1348 0.0017 0.0189 -0.0901 17 ASP A CA 129 C C . ASP A 17 ? 0.2878 0.2269 0.1416 -0.0009 -0.0011 -0.0938 17 ASP A C 130 O O . ASP A 17 ? 0.3262 0.2628 0.1562 -0.0022 -0.0026 -0.0962 17 ASP A O 131 C CB . ASP A 17 ? 0.2534 0.1859 0.1213 0.0061 0.0317 -0.0763 17 ASP A CB 132 C CG . ASP A 17 ? 0.3023 0.2295 0.1918 0.0083 0.0508 -0.0720 17 ASP A CG 133 O OD1 . ASP A 17 ? 0.3748 0.2920 0.2599 0.0110 0.0652 -0.0705 17 ASP A OD1 134 O OD2 . ASP A 17 ? 0.2498 0.1830 0.1638 0.0074 0.0519 -0.0696 17 ASP A OD2 135 N N . GLN A 18 ? 0.2590 0.1997 0.1245 -0.0122 -0.0085 -0.0873 18 GLN A N 136 C CA . GLN A 18 ? 0.2607 0.2137 0.1233 -0.0162 -0.0265 -0.0860 18 GLN A CA 137 C C . GLN A 18 ? 0.3166 0.2799 0.1671 -0.0102 -0.0259 -0.0754 18 GLN A C 138 O O . GLN A 18 ? 0.3456 0.3103 0.1797 -0.0104 -0.0357 -0.0744 18 GLN A O 139 C CB . GLN A 18 ? 0.2948 0.2426 0.1461 -0.0234 -0.0376 -0.0982 18 GLN A CB 140 C CG . GLN A 18 ? 0.3060 0.2403 0.1734 -0.0282 -0.0408 -0.1068 18 GLN A CG 141 C CD . GLN A 18 ? 0.4787 0.4122 0.3419 -0.0368 -0.0562 -0.1178 18 GLN A CD 142 O OE1 . GLN A 18 ? 0.5615 0.4870 0.3986 -0.0404 -0.0537 -0.1281 18 GLN A OE1 143 N NE2 . GLN A 18 ? 0.5043 0.4521 0.4004 -0.0387 -0.0712 -0.1175 18 GLN A NE2 144 N N . SER A 19 ? 0.2471 0.2136 0.1046 -0.0045 -0.0146 -0.0664 19 SER A N 145 C CA . SER A 19 ? 0.2892 0.2601 0.1384 0.0000 -0.0129 -0.0544 19 SER A CA 146 C C . SER A 19 ? 0.2436 0.2258 0.1116 -0.0001 -0.0208 -0.0448 19 SER A C 147 O O . SER A 19 ? 0.2261 0.2124 0.1127 0.0008 -0.0191 -0.0439 19 SER A O 148 C CB . SER A 19 ? 0.4651 0.4294 0.3106 0.0063 0.0050 -0.0500 19 SER A CB 149 O OG . SER A 19 ? 0.5735 0.5394 0.4388 0.0080 0.0128 -0.0493 19 SER A OG 150 N N . GLY A 20 ? 0.2696 0.2568 0.1330 0.0005 -0.0291 -0.0381 20 GLY A N 151 C CA . GLY A 20 ? 0.2834 0.2808 0.1657 0.0015 -0.0344 -0.0296 20 GLY A CA 152 C C . GLY A 20 ? 0.3850 0.3822 0.2587 0.0050 -0.0309 -0.0197 20 GLY A C 153 O O . GLY A 20 ? 0.4722 0.4637 0.3250 0.0064 -0.0320 -0.0188 20 GLY A O 154 N N A GLU A 21 ? 0.2407 0.2424 0.1286 0.0070 -0.0264 -0.0129 21 GLU A N 155 N N B GLU A 21 ? 0.2321 0.2340 0.1205 0.0069 -0.0266 -0.0129 21 GLU A N 156 C CA A GLU A 21 ? 0.1922 0.1922 0.0743 0.0102 -0.0225 -0.0042 21 GLU A CA 157 C CA B GLU A 21 ? 0.2050 0.2054 0.0889 0.0102 -0.0217 -0.0042 21 GLU A CA 158 C C A GLU A 21 ? 0.1855 0.1931 0.0860 0.0110 -0.0271 0.0013 21 GLU A C 159 C C B GLU A 21 ? 0.1479 0.1557 0.0487 0.0109 -0.0276 0.0012 21 GLU A C 160 O O A GLU A 21 ? 0.1286 0.1425 0.0466 0.0097 -0.0288 -0.0011 21 GLU A O 161 O O B GLU A 21 ? 0.1855 0.2000 0.1040 0.0095 -0.0306 -0.0013 21 GLU A O 162 C CB A GLU A 21 ? 0.3054 0.3000 0.1829 0.0133 -0.0077 -0.0020 21 GLU A CB 163 C CB B GLU A 21 ? 0.2224 0.2201 0.1079 0.0130 -0.0079 -0.0022 21 GLU A CB 164 C CG A GLU A 21 ? 0.2677 0.2530 0.1294 0.0137 0.0006 -0.0081 21 GLU A CG 165 C CG B GLU A 21 ? 0.2457 0.2405 0.1279 0.0168 -0.0004 0.0064 21 GLU A CG 166 C CD A GLU A 21 ? 0.3624 0.3380 0.1977 0.0142 -0.0015 -0.0095 21 GLU A CD 167 C CD B GLU A 21 ? 0.1834 0.1780 0.0736 0.0200 0.0138 0.0094 21 GLU A CD 168 O OE1 A GLU A 21 ? 0.2344 0.2080 0.0607 0.0162 -0.0047 -0.0025 21 GLU A OE1 169 O OE1 B GLU A 21 ? 0.1885 0.1918 0.0949 0.0209 0.0144 0.0141 21 GLU A OE1 170 O OE2 A GLU A 21 ? 0.4645 0.4329 0.2863 0.0133 0.0002 -0.0177 21 GLU A OE2 171 O OE2 B GLU A 21 ? 0.1704 0.1567 0.0528 0.0214 0.0250 0.0074 21 GLU A OE2 172 N N . PHE A 22 ? 0.1731 0.1788 0.0677 0.0138 -0.0278 0.0086 22 PHE A N 173 C CA . PHE A 22 ? 0.1706 0.1819 0.0803 0.0157 -0.0319 0.0138 22 PHE A CA 174 C C . PHE A 22 ? 0.1525 0.1586 0.0558 0.0199 -0.0231 0.0219 22 PHE A C 175 O O . PHE A 22 ? 0.1999 0.1974 0.0844 0.0220 -0.0208 0.0261 22 PHE A O 176 C CB . PHE A 22 ? 0.1577 0.1733 0.0691 0.0161 -0.0456 0.0159 22 PHE A CB 177 C CG . PHE A 22 ? 0.1909 0.2126 0.1211 0.0196 -0.0502 0.0221 22 PHE A CG 178 C CD1 . PHE A 22 ? 0.1515 0.1844 0.1063 0.0192 -0.0562 0.0189 22 PHE A CD1 179 C CD2 . PHE A 22 ? 0.1755 0.1915 0.1006 0.0243 -0.0470 0.0313 22 PHE A CD2 180 C CE1 . PHE A 22 ? 0.1569 0.1963 0.1333 0.0239 -0.0588 0.0245 22 PHE A CE1 181 C CE2 . PHE A 22 ? 0.1789 0.1995 0.1236 0.0290 -0.0500 0.0372 22 PHE A CE2 182 C CZ . PHE A 22 ? 0.1683 0.2006 0.1394 0.0290 -0.0560 0.0335 22 PHE A CZ 183 N N . MET A 23 ? 0.1336 0.1448 0.0518 0.0212 -0.0173 0.0244 23 MET A N 184 C CA A MET A 23 ? 0.1417 0.1491 0.0590 0.0249 -0.0070 0.0331 23 MET A CA 185 C CA B MET A 23 ? 0.1503 0.1577 0.0674 0.0250 -0.0072 0.0331 23 MET A CA 186 C C . MET A 23 ? 0.1470 0.1613 0.0843 0.0251 -0.0058 0.0366 23 MET A C 187 O O . MET A 23 ? 0.1377 0.1585 0.0883 0.0213 -0.0105 0.0300 23 MET A O 188 C CB A MET A 23 ? 0.1458 0.1502 0.0604 0.0248 0.0056 0.0331 23 MET A CB 189 C CB B MET A 23 ? 0.1509 0.1550 0.0649 0.0249 0.0054 0.0333 23 MET A CB 190 C CG A MET A 23 ? 0.1356 0.1496 0.0685 0.0206 0.0054 0.0273 23 MET A CG 191 C CG B MET A 23 ? 0.1416 0.1550 0.0717 0.0210 0.0051 0.0272 23 MET A CG 192 S SD A MET A 23 ? 0.1263 0.1446 0.0881 0.0162 0.0085 0.0282 23 MET A SD 193 S SD B MET A 23 ? 0.2245 0.2364 0.1705 0.0197 0.0191 0.0290 23 MET A SD 194 C CE A MET A 23 ? 0.1717 0.1837 0.1418 0.0179 0.0244 0.0354 23 MET A CE 195 C CE B MET A 23 ? 0.1871 0.1974 0.1517 0.0191 0.0258 0.0361 23 MET A CE 196 N N . PHE A 24 ? 0.1347 0.1433 0.0777 0.0271 0.0027 0.0445 24 PHE A N 197 C CA . PHE A 24 ? 0.1407 0.1508 0.1077 0.0236 0.0067 0.0437 24 PHE A CA 198 C C . PHE A 24 ? 0.1367 0.1444 0.1157 0.0200 0.0173 0.0434 24 PHE A C 199 O O . PHE A 24 ? 0.1466 0.1481 0.1194 0.0230 0.0268 0.0500 24 PHE A O 200 C CB . PHE A 24 ? 0.1436 0.1489 0.1159 0.0284 0.0081 0.0530 24 PHE A CB 201 C CG . PHE A 24 ? 0.1794 0.1900 0.1616 0.0296 -0.0010 0.0513 24 PHE A CG 202 C CD1 . PHE A 24 ? 0.1631 0.1726 0.1673 0.0269 0.0041 0.0488 24 PHE A CD1 203 C CD2 . PHE A 24 ? 0.1865 0.2019 0.1587 0.0330 -0.0138 0.0517 24 PHE A CD2 204 C CE1 . PHE A 24 ? 0.1434 0.1567 0.1623 0.0285 -0.0003 0.0479 24 PHE A CE1 205 C CE2 . PHE A 24 ? 0.1659 0.1877 0.1568 0.0341 -0.0213 0.0507 24 PHE A CE2 206 C CZ . PHE A 24 ? 0.1513 0.1720 0.1669 0.0322 -0.0130 0.0494 24 PHE A CZ 207 N N . ASP A 25 ? 0.1211 0.1319 0.1172 0.0135 0.0157 0.0357 25 ASP A N 208 C CA . ASP A 25 ? 0.1140 0.1250 0.1288 0.0087 0.0205 0.0334 25 ASP A CA 209 C C . ASP A 25 ? 0.1190 0.1251 0.1512 0.0043 0.0227 0.0308 25 ASP A C 210 O O . ASP A 25 ? 0.1298 0.1336 0.1584 0.0027 0.0183 0.0257 25 ASP A O 211 C CB . ASP A 25 ? 0.1130 0.1305 0.1287 0.0044 0.0116 0.0250 25 ASP A CB 212 C CG . ASP A 25 ? 0.2262 0.2461 0.2662 -0.0009 0.0112 0.0220 25 ASP A CG 213 O OD1 . ASP A 25 ? 0.2540 0.2781 0.3036 0.0002 0.0147 0.0245 25 ASP A OD1 214 O OD2 . ASP A 25 ? 0.2191 0.2362 0.2704 -0.0065 0.0068 0.0166 25 ASP A OD2 215 N N . PHE A 26 ? 0.1065 0.1093 0.1591 0.0024 0.0316 0.0338 26 PHE A N 216 C CA . PHE A 26 ? 0.1102 0.1069 0.1828 -0.0033 0.0338 0.0291 26 PHE A CA 217 C C . PHE A 26 ? 0.1084 0.1092 0.2053 -0.0108 0.0299 0.0223 26 PHE A C 218 O O . PHE A 26 ? 0.1104 0.1135 0.2260 -0.0098 0.0388 0.0282 26 PHE A O 219 C CB . PHE A 26 ? 0.1237 0.1115 0.2062 0.0010 0.0486 0.0399 26 PHE A CB 220 C CG . PHE A 26 ? 0.1301 0.1100 0.2380 -0.0054 0.0536 0.0346 26 PHE A CG 221 C CD1 . PHE A 26 ? 0.1609 0.1334 0.2658 -0.0066 0.0527 0.0297 26 PHE A CD1 222 C CD2 . PHE A 26 ? 0.1486 0.1274 0.2865 -0.0107 0.0604 0.0337 26 PHE A CD2 223 C CE1 . PHE A 26 ? 0.1677 0.1298 0.2942 -0.0131 0.0584 0.0230 26 PHE A CE1 224 C CE2 . PHE A 26 ? 0.1573 0.1278 0.3206 -0.0178 0.0641 0.0269 26 PHE A CE2 225 C CZ . PHE A 26 ? 0.1535 0.1146 0.3082 -0.0191 0.0629 0.0210 26 PHE A CZ 226 N N . ASP A 27 ? 0.1634 0.0885 0.1881 0.0024 0.0308 -0.0095 27 ASP A N 227 C CA . ASP A 27 ? 0.1611 0.0962 0.1865 -0.0060 0.0279 -0.0132 27 ASP A CA 228 C C . ASP A 27 ? 0.1847 0.1506 0.2088 -0.0050 0.0306 -0.0069 27 ASP A C 229 O O . ASP A 27 ? 0.2014 0.1846 0.2338 -0.0140 0.0282 -0.0019 27 ASP A O 230 C CB . ASP A 27 ? 0.1583 0.0808 0.1944 -0.0205 0.0224 -0.0088 27 ASP A CB 231 C CG . ASP A 27 ? 0.2497 0.1367 0.2827 -0.0204 0.0196 -0.0197 27 ASP A CG 232 O OD1 . ASP A 27 ? 0.2739 0.1571 0.2956 -0.0080 0.0209 -0.0287 27 ASP A OD1 233 O OD2 . ASP A 27 ? 0.2343 0.1020 0.2734 -0.0321 0.0149 -0.0172 27 ASP A OD2 234 N N . GLY A 28 ? 0.1932 0.1662 0.2072 0.0057 0.0355 -0.0070 28 GLY A N 235 C CA . GLY A 28 ? 0.1479 0.1448 0.1566 0.0106 0.0397 -0.0029 28 GLY A CA 236 C C . GLY A 28 ? 0.2195 0.2294 0.2277 0.0105 0.0434 0.0097 28 GLY A C 237 O O . GLY A 28 ? 0.2206 0.2491 0.2217 0.0171 0.0487 0.0126 28 GLY A O 238 N N . ASP A 29 ? 0.1365 0.1363 0.1506 0.0045 0.0412 0.0177 29 ASP A N 239 C CA . ASP A 29 ? 0.1185 0.1290 0.1278 0.0052 0.0446 0.0305 29 ASP A CA 240 C C . ASP A 29 ? 0.1490 0.1461 0.1476 0.0114 0.0427 0.0295 29 ASP A C 241 O O . ASP A 29 ? 0.1624 0.1417 0.1660 0.0121 0.0386 0.0243 29 ASP A O 242 C CB . ASP A 29 ? 0.1395 0.1530 0.1631 -0.0071 0.0434 0.0452 29 ASP A CB 243 C CG . ASP A 29 ? 0.2174 0.2577 0.2518 -0.0143 0.0466 0.0516 29 ASP A CG 244 O OD1 . ASP A 29 ? 0.2337 0.2992 0.2613 -0.0080 0.0540 0.0577 29 ASP A OD1 245 O OD2 . ASP A 29 ? 0.1491 0.1862 0.1986 -0.0262 0.0416 0.0505 29 ASP A OD2 246 N N . GLU A 30 ? 0.1446 0.1522 0.1283 0.0162 0.0457 0.0347 30 GLU A N 247 C CA . GLU A 30 ? 0.1301 0.1288 0.1024 0.0204 0.0417 0.0334 30 GLU A CA 248 C C . GLU A 30 ? 0.1409 0.1347 0.1208 0.0165 0.0368 0.0470 30 GLU A C 249 O O . GLU A 30 ? 0.1521 0.1550 0.1313 0.0128 0.0390 0.0609 30 GLU A O 250 C CB . GLU A 30 ? 0.1532 0.1614 0.1012 0.0268 0.0454 0.0319 30 GLU A CB 251 C CG . GLU A 30 ? 0.1746 0.1768 0.1084 0.0282 0.0388 0.0316 30 GLU A CG 252 C CD . GLU A 30 ? 0.2625 0.2711 0.1690 0.0327 0.0413 0.0299 30 GLU A CD 253 O OE1 . GLU A 30 ? 0.2534 0.2687 0.1620 0.0336 0.0451 0.0254 30 GLU A OE1 254 O OE2 . GLU A 30 ? 0.2674 0.2737 0.1576 0.0327 0.0351 0.0310 30 GLU A OE2 255 N N . ILE A 31 ? 0.1399 0.1209 0.1277 0.0183 0.0308 0.0447 31 ILE A N 256 C CA . ILE A 31 ? 0.1536 0.1303 0.1473 0.0180 0.0256 0.0590 31 ILE A CA 257 C C . ILE A 31 ? 0.1746 0.1636 0.1496 0.0210 0.0219 0.0650 31 ILE A C 258 O O . ILE A 31 ? 0.1835 0.1790 0.1512 0.0197 0.0215 0.0802 31 ILE A O 259 C CB . ILE A 31 ? 0.1522 0.1143 0.1623 0.0220 0.0211 0.0559 31 ILE A CB 260 C CG1 . ILE A 31 ? 0.1827 0.1291 0.2052 0.0197 0.0246 0.0467 31 ILE A CG1 261 C CG2 . ILE A 31 ? 0.1884 0.1455 0.2052 0.0244 0.0159 0.0729 31 ILE A CG2 262 C CD1 . ILE A 31 ? 0.1666 0.0976 0.2027 0.0265 0.0229 0.0418 31 ILE A CD1 263 N N . PHE A 32 ? 0.1579 0.1493 0.1235 0.0239 0.0188 0.0530 32 PHE A N 264 C CA . PHE A 32 ? 0.1717 0.1725 0.1154 0.0250 0.0134 0.0543 32 PHE A CA 265 C C . PHE A 32 ? 0.1784 0.1761 0.1097 0.0251 0.0126 0.0371 32 PHE A C 266 O O . PHE A 32 ? 0.1549 0.1448 0.0981 0.0251 0.0155 0.0268 32 PHE A O 267 C CB . PHE A 32 ? 0.1820 0.1870 0.1332 0.0263 0.0027 0.0661 32 PHE A CB 268 C CG . PHE A 32 ? 0.1781 0.1815 0.1494 0.0279 -0.0031 0.0595 32 PHE A CG 269 C CD1 . PHE A 32 ? 0.1865 0.1975 0.1505 0.0254 -0.0102 0.0505 32 PHE A CD1 270 C CD2 . PHE A 32 ? 0.2181 0.2124 0.2153 0.0315 -0.0010 0.0627 32 PHE A CD2 271 C CE1 . PHE A 32 ? 0.2150 0.2302 0.2010 0.0260 -0.0142 0.0466 32 PHE A CE1 272 C CE2 . PHE A 32 ? 0.1858 0.1824 0.2020 0.0351 -0.0039 0.0575 32 PHE A CE2 273 C CZ . PHE A 32 ? 0.1768 0.1869 0.1894 0.0320 -0.0101 0.0506 32 PHE A CZ 274 N N . HIS A 33 ? 0.1852 0.1866 0.0901 0.0249 0.0088 0.0340 33 HIS A N 275 C CA . HIS A 33 ? 0.2001 0.1942 0.0929 0.0223 0.0046 0.0188 33 HIS A CA 276 C C . HIS A 33 ? 0.2266 0.2282 0.1054 0.0182 -0.0087 0.0215 33 HIS A C 277 O O . HIS A 33 ? 0.2445 0.2571 0.1181 0.0197 -0.0130 0.0351 33 HIS A O 278 C CB . HIS A 33 ? 0.2275 0.2113 0.0952 0.0259 0.0137 0.0067 33 HIS A CB 279 C CG . HIS A 33 ? 0.2402 0.2286 0.0811 0.0282 0.0154 0.0087 33 HIS A CG 280 N ND1 . HIS A 33 ? 0.2247 0.2240 0.0722 0.0305 0.0234 0.0179 33 HIS A ND1 281 C CD2 . HIS A 33 ? 0.2481 0.2332 0.0670 0.0242 0.0092 0.0016 33 HIS A CD2 282 C CE1 . HIS A 33 ? 0.2451 0.2469 0.0739 0.0296 0.0232 0.0166 33 HIS A CE1 283 N NE2 . HIS A 33 ? 0.2912 0.2841 0.1017 0.0259 0.0150 0.0065 33 HIS A NE2 284 N N . VAL A 34 ? 0.2256 0.2218 0.0983 0.0120 -0.0159 0.0096 34 VAL A N 285 C CA . VAL A 34 ? 0.2406 0.2450 0.0980 0.0055 -0.0310 0.0099 34 VAL A CA 286 C C . VAL A 34 ? 0.2830 0.2712 0.0977 0.0033 -0.0311 -0.0046 34 VAL A C 287 O O . VAL A 34 ? 0.3246 0.2931 0.1308 0.0017 -0.0255 -0.0189 34 VAL A O 288 C CB . VAL A 34 ? 0.2317 0.2449 0.1152 -0.0030 -0.0416 0.0080 34 VAL A CB 289 C CG1 . VAL A 34 ? 0.2839 0.3061 0.1491 -0.0131 -0.0594 0.0054 34 VAL A CG1 290 C CG2 . VAL A 34 ? 0.2405 0.2703 0.1626 0.0027 -0.0418 0.0232 34 VAL A CG2 291 N N . ASP A 35 ? 0.2999 0.2942 0.0851 0.0048 -0.0365 -0.0003 35 ASP A N 292 C CA . ASP A 35 ? 0.3491 0.3373 0.1100 0.0012 -0.0355 -0.0140 35 ASP A CA 293 C C . ASP A 35 ? 0.4144 0.3983 0.1719 -0.0096 -0.0524 -0.0245 35 ASP A C 294 O O . ASP A 35 ? 0.4143 0.4138 0.1718 -0.0147 -0.0687 -0.0172 35 ASP A O 295 C CB . ASP A 35 ? 0.3939 0.3951 0.1362 0.0016 -0.0355 -0.0041 35 ASP A CB 296 C CG . ASP A 35 ? 0.5168 0.5132 0.2342 0.0003 -0.0319 -0.0184 35 ASP A CG 297 O OD1 . ASP A 35 ? 0.4665 0.4518 0.1784 -0.0024 -0.0374 -0.0350 35 ASP A OD1 298 O OD2 . ASP A 35 ? 0.6958 0.6931 0.3971 0.0023 -0.0241 -0.0128 35 ASP A OD2 299 N N . MET A 36 ? 0.4013 0.3648 0.1610 -0.0145 -0.0487 -0.0394 36 MET A N 300 C CA . MET A 36 ? 0.5020 0.4605 0.2660 -0.0299 -0.0638 -0.0474 36 MET A CA 301 C C . MET A 36 ? 0.5334 0.4951 0.2754 -0.0352 -0.0761 -0.0545 36 MET A C 302 O O . MET A 36 ? 0.5497 0.5245 0.2993 -0.0479 -0.0941 -0.0528 36 MET A O 303 C CB . MET A 36 ? 0.4802 0.4139 0.2519 -0.0336 -0.0551 -0.0591 36 MET A CB 304 C CG . MET A 36 ? 0.4602 0.3899 0.2521 -0.0274 -0.0424 -0.0540 36 MET A CG 305 S SD . MET A 36 ? 0.5348 0.4933 0.3683 -0.0319 -0.0489 -0.0385 36 MET A SD 306 C CE . MET A 36 ? 0.5662 0.5315 0.4139 -0.0537 -0.0656 -0.0433 36 MET A CE 307 N N . ALA A 37 ? 0.4808 0.4347 0.1986 -0.0262 -0.0665 -0.0620 37 ALA A N 308 C CA . ALA A 37 ? 0.5464 0.5007 0.2375 -0.0300 -0.0768 -0.0710 37 ALA A CA 309 C C . ALA A 37 ? 0.5523 0.5346 0.2373 -0.0280 -0.0899 -0.0584 37 ALA A C 310 O O . ALA A 37 ? 0.5295 0.5178 0.2045 -0.0366 -0.1075 -0.0624 37 ALA A O 311 C CB . ALA A 37 ? 0.5886 0.5299 0.2564 -0.0208 -0.0617 -0.0808 37 ALA A CB 312 N N . LYS A 38 ? 0.4809 0.4797 0.1728 -0.0166 -0.0816 -0.0420 38 LYS A N 313 C CA . LYS A 38 ? 0.4851 0.5042 0.1710 -0.0103 -0.0926 -0.0263 38 LYS A CA 314 C C . LYS A 38 ? 0.4727 0.5041 0.1903 -0.0177 -0.1065 -0.0110 38 LYS A C 315 O O . LYS A 38 ? 0.5082 0.5566 0.2283 -0.0165 -0.1186 0.0031 38 LYS A O 316 C CB . LYS A 38 ? 0.5647 0.5925 0.2476 0.0034 -0.0752 -0.0127 38 LYS A CB 317 C CG . LYS A 38 ? 0.5938 0.6244 0.2530 -0.0054 -0.0618 -0.0207 38 LYS A CG 318 C CD . LYS A 38 ? 0.7374 0.7520 0.3796 -0.0120 -0.0517 -0.0017 38 LYS A CD 319 C CE . LYS A 38 ? 0.8326 0.8423 0.4450 -0.0086 -0.0392 -0.0123 38 LYS A CE 320 N NZ . LYS A 38 ? 0.9171 0.9193 0.5093 -0.0042 -0.0321 0.0039 38 LYS A NZ 321 N N . LYS A 39 ? 0.4115 0.4394 0.1566 -0.0257 -0.1036 -0.0129 39 LYS A N 322 C CA . LYS A 39 ? 0.3991 0.4506 0.1842 -0.0316 -0.1129 0.0025 39 LYS A CA 323 C C . LYS A 39 ? 0.3812 0.4486 0.1792 -0.0189 -0.1085 0.0251 39 LYS A C 324 O O . LYS A 39 ? 0.4002 0.4919 0.2202 -0.0176 -0.1198 0.0402 39 LYS A O 325 C CB . LYS A 39 ? 0.4665 0.5390 0.2655 -0.0440 -0.1337 0.0022 39 LYS A CB 326 C CG . LYS A 39 ? 0.5518 0.6076 0.3424 -0.0594 -0.1385 -0.0185 39 LYS A CG 327 C CD . LYS A 39 ? 0.7486 0.8246 0.5435 -0.0711 -0.1594 -0.0194 39 LYS A CD 328 C CE . LYS A 39 ? 0.8533 0.9115 0.6439 -0.0887 -0.1641 -0.0383 39 LYS A CE 329 N NZ . LYS A 39 ? 0.8631 0.8813 0.6146 -0.0844 -0.1512 -0.0570 39 LYS A NZ 330 N N . GLU A 40 ? 0.4159 0.4687 0.2029 -0.0088 -0.0909 0.0277 40 GLU A N 331 C CA A GLU A 40 ? 0.3885 0.4507 0.1887 0.0018 -0.0839 0.0488 40 GLU A CA 332 C CA B GLU A 40 ? 0.3882 0.4510 0.1894 0.0016 -0.0842 0.0490 40 GLU A CA 333 C C . GLU A 40 ? 0.3187 0.3752 0.1405 0.0072 -0.0672 0.0526 40 GLU A C 334 O O . GLU A 40 ? 0.3197 0.3578 0.1331 0.0068 -0.0555 0.0373 40 GLU A O 335 C CB A GLU A 40 ? 0.4199 0.4702 0.1851 0.0076 -0.0784 0.0511 40 GLU A CB 336 C CB B GLU A 40 ? 0.4195 0.4722 0.1870 0.0075 -0.0800 0.0526 40 GLU A CB 337 C CG A GLU A 40 ? 0.4869 0.5444 0.2318 0.0060 -0.0947 0.0523 40 GLU A CG 338 C CG B GLU A 40 ? 0.4234 0.4527 0.1658 0.0097 -0.0620 0.0429 40 GLU A CG 339 C CD A GLU A 40 ? 0.5868 0.6306 0.2944 0.0107 -0.0882 0.0558 40 GLU A CD 340 C CD B GLU A 40 ? 0.5214 0.5451 0.2343 0.0117 -0.0577 0.0489 40 GLU A CD 341 O OE1 A GLU A 40 ? 0.6323 0.6647 0.3352 0.0130 -0.0702 0.0576 40 GLU A OE1 342 O OE1 B GLU A 40 ? 0.6257 0.6515 0.3177 0.0112 -0.0714 0.0501 40 GLU A OE1 343 O OE2 A GLU A 40 ? 0.6042 0.6518 0.2892 0.0108 -0.1009 0.0571 40 GLU A OE2 344 O OE2 B GLU A 40 ? 0.5192 0.5405 0.2323 0.0144 -0.0407 0.0523 40 GLU A OE2 345 N N . THR A 41 ? 0.2890 0.3542 0.1419 0.0139 -0.0646 0.0707 41 THR A N 346 C CA . THR A 41 ? 0.2621 0.3151 0.1387 0.0191 -0.0484 0.0727 41 THR A CA 347 C C . THR A 41 ? 0.2985 0.3460 0.1535 0.0232 -0.0361 0.0799 41 THR A C 348 O O . THR A 41 ? 0.3031 0.3540 0.1494 0.0246 -0.0381 0.0920 41 THR A O 349 C CB . THR A 41 ? 0.3420 0.4014 0.2574 0.0247 -0.0509 0.0883 41 THR A CB 350 O OG1 . THR A 41 ? 0.3309 0.4005 0.2702 0.0222 -0.0598 0.0822 41 THR A OG1 351 C CG2 . THR A 41 ? 0.2400 0.2830 0.1748 0.0286 -0.0356 0.0894 41 THR A CG2 352 N N . VAL A 42 ? 0.2600 0.2956 0.1124 0.0238 -0.0219 0.0687 42 VAL A N 353 C CA . VAL A 42 ? 0.2674 0.3003 0.1091 0.0258 -0.0085 0.0728 42 VAL A CA 354 C C . VAL A 42 ? 0.2438 0.2741 0.1133 0.0272 0.0019 0.0808 42 VAL A C 355 O O . VAL A 42 ? 0.2323 0.2549 0.1130 0.0271 0.0082 0.0686 42 VAL A O 356 C CB . VAL A 42 ? 0.2815 0.3054 0.0995 0.0252 -0.0008 0.0538 42 VAL A CB 357 C CG1 . VAL A 42 ? 0.3194 0.3468 0.1357 0.0266 0.0121 0.0583 42 VAL A CG1 358 C CG2 . VAL A 42 ? 0.3196 0.3392 0.1082 0.0211 -0.0117 0.0438 42 VAL A CG2 359 N N . TRP A 43 ? 0.2499 0.2816 0.1333 0.0261 0.0028 0.0977 43 TRP A N 360 C CA . TRP A 43 ? 0.2345 0.2593 0.1442 0.0242 0.0106 0.1048 43 TRP A CA 361 C C . TRP A 43 ? 0.2332 0.2630 0.1389 0.0214 0.0231 0.1006 43 TRP A C 362 O O . TRP A 43 ? 0.2518 0.2899 0.1398 0.0213 0.0264 0.1012 43 TRP A O 363 C CB . TRP A 43 ? 0.2480 0.2672 0.1736 0.0231 0.0063 0.1223 43 TRP A CB 364 C CG . TRP A 43 ? 0.2861 0.3032 0.2225 0.0281 -0.0059 0.1262 43 TRP A CG 365 C CD1 . TRP A 43 ? 0.2923 0.3194 0.2164 0.0308 -0.0168 0.1311 43 TRP A CD1 366 C CD2 . TRP A 43 ? 0.2329 0.2393 0.1965 0.0319 -0.0083 0.1242 43 TRP A CD2 367 N NE1 . TRP A 43 ? 0.3409 0.3685 0.2860 0.0359 -0.0262 0.1335 43 TRP A NE1 368 C CE2 . TRP A 43 ? 0.2587 0.2730 0.2283 0.0375 -0.0203 0.1289 43 TRP A CE2 369 C CE3 . TRP A 43 ? 0.2179 0.2088 0.2015 0.0306 -0.0014 0.1147 43 TRP A CE3 370 C CZ2 . TRP A 43 ? 0.3078 0.3174 0.3046 0.0438 -0.0237 0.1269 43 TRP A CZ2 371 C CZ3 . TRP A 43 ? 0.2292 0.2110 0.2353 0.0364 -0.0048 0.1101 43 TRP A CZ3 372 C CH2 . TRP A 43 ? 0.2158 0.2079 0.2294 0.0439 -0.0149 0.1172 43 TRP A CH2 373 N N . ARG A 44 ? 0.2135 0.2393 0.1367 0.0195 0.0297 0.0964 44 ARG A N 374 C CA . ARG A 44 ? 0.2097 0.2455 0.1334 0.0177 0.0397 0.0910 44 ARG A CA 375 C C . ARG A 44 ? 0.2325 0.2767 0.1627 0.0117 0.0436 0.1057 44 ARG A C 376 O O . ARG A 44 ? 0.2434 0.3016 0.1652 0.0127 0.0503 0.1046 44 ARG A O 377 C CB . ARG A 44 ? 0.1872 0.2186 0.1289 0.0163 0.0439 0.0838 44 ARG A CB 378 C CG . ARG A 44 ? 0.1907 0.2367 0.1369 0.0153 0.0518 0.0786 44 ARG A CG 379 C CD . ARG A 44 ? 0.2102 0.2613 0.1355 0.0235 0.0536 0.0653 44 ARG A CD 380 N NE . ARG A 44 ? 0.1894 0.2547 0.1216 0.0252 0.0601 0.0622 44 ARG A NE 381 C CZ . ARG A 44 ? 0.2030 0.2847 0.1360 0.0242 0.0654 0.0714 44 ARG A CZ 382 N NH1 . ARG A 44 ? 0.2306 0.3144 0.1561 0.0209 0.0653 0.0836 44 ARG A NH1 383 N NH2 . ARG A 44 ? 0.2020 0.2990 0.1432 0.0273 0.0709 0.0694 44 ARG A NH2 384 N N . LEU A 45 ? 0.2319 0.2653 0.1779 0.0061 0.0396 0.1191 45 LEU A N 385 C CA . LEU A 45 ? 0.2546 0.2912 0.2038 -0.0001 0.0418 0.1348 45 LEU A CA 386 C C . LEU A 45 ? 0.3112 0.3389 0.2510 0.0033 0.0336 0.1448 45 LEU A C 387 O O . LEU A 45 ? 0.2947 0.3080 0.2427 0.0063 0.0257 0.1446 45 LEU A O 388 C CB . LEU A 45 ? 0.2844 0.3109 0.2590 -0.0109 0.0432 0.1412 45 LEU A CB 389 C CG . LEU A 45 ? 0.2876 0.3257 0.2752 -0.0159 0.0493 0.1327 45 LEU A CG 390 C CD1 . LEU A 45 ? 0.2859 0.3143 0.2957 -0.0301 0.0489 0.1403 45 LEU A CD1 391 C CD2 . LEU A 45 ? 0.2623 0.3271 0.2382 -0.0117 0.0573 0.1299 45 LEU A CD2 392 N N A GLU A 46 ? 0.3137 0.3511 0.2369 0.0037 0.0356 0.1541 46 GLU A N 393 N N B GLU A 46 ? 0.3215 0.3597 0.2439 0.0040 0.0359 0.1532 46 GLU A N 394 C CA A GLU A 46 ? 0.3542 0.3865 0.2650 0.0078 0.0272 0.1640 46 GLU A CA 395 C CA B GLU A 46 ? 0.4033 0.4370 0.3138 0.0068 0.0289 0.1655 46 GLU A CA 396 C C A GLU A 46 ? 0.3781 0.3905 0.3084 0.0061 0.0212 0.1757 46 GLU A C 397 C C B GLU A 46 ? 0.3808 0.3942 0.3103 0.0058 0.0218 0.1759 46 GLU A C 398 O O A GLU A 46 ? 0.4032 0.4095 0.3311 0.0125 0.0115 0.1792 46 GLU A O 399 O O B GLU A 46 ? 0.4179 0.4262 0.3438 0.0125 0.0121 0.1785 46 GLU A O 400 C CB A GLU A 46 ? 0.4518 0.4961 0.3414 0.0077 0.0318 0.1740 46 GLU A CB 401 C CB B GLU A 46 ? 0.4406 0.4860 0.3378 0.0040 0.0363 0.1775 46 GLU A CB 402 C CG A GLU A 46 ? 0.4879 0.5301 0.3584 0.0131 0.0220 0.1819 46 GLU A CG 403 C CG B GLU A 46 ? 0.5328 0.5823 0.4490 -0.0057 0.0463 0.1851 46 GLU A CG 404 C CD A GLU A 46 ? 0.5870 0.6369 0.4389 0.0120 0.0269 0.1963 46 GLU A CD 405 C CD B GLU A 46 ? 0.4462 0.5114 0.3686 -0.0064 0.0545 0.1716 46 GLU A CD 406 O OE1 A GLU A 46 ? 0.6714 0.7345 0.5131 0.0106 0.0376 0.1932 46 GLU A OE1 407 O OE1 B GLU A 46 ? 0.3525 0.4235 0.2606 0.0016 0.0543 0.1562 46 GLU A OE1 408 O OE2 A GLU A 46 ? 0.6553 0.6984 0.5031 0.0134 0.0205 0.2113 46 GLU A OE2 409 O OE2 B GLU A 46 ? 0.4213 0.4921 0.3633 -0.0152 0.0604 0.1764 46 GLU A OE2 410 N N . GLU A 47 ? 0.3810 0.3824 0.3306 -0.0023 0.0263 0.1805 47 GLU A N 411 C CA A GLU A 47 ? 0.4252 0.4008 0.3903 -0.0036 0.0213 0.1890 47 GLU A CA 412 C CA B GLU A 47 ? 0.4322 0.4077 0.3976 -0.0037 0.0214 0.1888 47 GLU A CA 413 C C . GLU A 47 ? 0.4290 0.3905 0.4060 0.0040 0.0139 0.1784 47 GLU A C 414 O O . GLU A 47 ? 0.3762 0.3196 0.3602 0.0094 0.0081 0.1842 47 GLU A O 415 C CB A GLU A 47 ? 0.4661 0.4293 0.4467 -0.0164 0.0275 0.1933 47 GLU A CB 416 C CB B GLU A 47 ? 0.4630 0.4266 0.4447 -0.0165 0.0276 0.1914 47 GLU A CB 417 C CG A GLU A 47 ? 0.5288 0.5116 0.5030 -0.0248 0.0364 0.2026 47 GLU A CG 418 C CG B GLU A 47 ? 0.4541 0.4220 0.4480 -0.0210 0.0309 0.1755 47 GLU A CG 419 C CD A GLU A 47 ? 0.3472 0.3534 0.3245 -0.0276 0.0433 0.1904 47 GLU A CD 420 C CD B GLU A 47 ? 0.5147 0.4652 0.5262 -0.0343 0.0329 0.1757 47 GLU A CD 421 O OE1 A GLU A 47 ? 0.3350 0.3627 0.2953 -0.0202 0.0463 0.1850 47 GLU A OE1 422 O OE1 B GLU A 47 ? 0.3279 0.2533 0.3497 -0.0341 0.0284 0.1666 47 GLU A OE1 423 O OE2 A GLU A 47 ? 0.3899 0.3916 0.3854 -0.0370 0.0453 0.1855 47 GLU A OE2 424 O OE2 B GLU A 47 ? 0.4644 0.4267 0.4787 -0.0451 0.0389 0.1840 47 GLU A OE2 425 N N . PHE A 48 ? 0.2980 0.2680 0.2773 0.0057 0.0150 0.1631 48 PHE A N 426 C CA . PHE A 48 ? 0.2808 0.2397 0.2728 0.0128 0.0097 0.1524 48 PHE A CA 427 C C . PHE A 48 ? 0.3004 0.2635 0.2885 0.0234 0.0001 0.1573 48 PHE A C 428 O O . PHE A 48 ? 0.3395 0.2897 0.3425 0.0304 -0.0044 0.1555 48 PHE A O 429 C CB . PHE A 48 ? 0.2501 0.2200 0.2404 0.0134 0.0128 0.1372 48 PHE A CB 430 C CG . PHE A 48 ? 0.2430 0.2108 0.2411 0.0045 0.0209 0.1308 48 PHE A CG 431 C CD1 . PHE A 48 ? 0.2551 0.2338 0.2491 0.0056 0.0254 0.1186 48 PHE A CD1 432 C CD2 . PHE A 48 ? 0.2731 0.2286 0.2817 -0.0053 0.0234 0.1370 48 PHE A CD2 433 C CE1 . PHE A 48 ? 0.2384 0.2193 0.2407 -0.0019 0.0320 0.1132 48 PHE A CE1 434 C CE2 . PHE A 48 ? 0.2906 0.2485 0.3079 -0.0150 0.0288 0.1312 48 PHE A CE2 435 C CZ . PHE A 48 ? 0.2389 0.2116 0.2543 -0.0129 0.0329 0.1196 48 PHE A CZ 436 N N . GLY A 49 ? 0.3259 0.3086 0.2934 0.0248 -0.0029 0.1624 49 GLY A N 437 C CA . GLY A 49 ? 0.3199 0.3125 0.2818 0.0330 -0.0140 0.1662 49 GLY A CA 438 C C . GLY A 49 ? 0.3394 0.3223 0.3057 0.0379 -0.0190 0.1820 49 GLY A C 439 O O . GLY A 49 ? 0.3962 0.3883 0.3626 0.0458 -0.0291 0.1864 49 GLY A O 440 N N . ARG A 50 ? 0.3586 0.3236 0.3286 0.0329 -0.0125 0.1912 50 ARG A N 441 C CA . ARG A 50 ? 0.3922 0.3418 0.3653 0.0380 -0.0164 0.2067 50 ARG A CA 442 C C . ARG A 50 ? 0.5326 0.4599 0.5279 0.0454 -0.0181 0.2016 50 ARG A C 443 O O . ARG A 50 ? 0.5723 0.4878 0.5718 0.0543 -0.0230 0.2118 50 ARG A O 444 C CB . ARG A 50 ? 0.4871 0.4242 0.4530 0.0286 -0.0087 0.2195 50 ARG A CB 445 C CG . ARG A 50 ? 0.6122 0.5716 0.5547 0.0234 -0.0053 0.2259 50 ARG A CG 446 C CD . ARG A 50 ? 0.7791 0.7273 0.7158 0.0164 0.0007 0.2438 50 ARG A CD 447 N NE . ARG A 50 ? 0.8633 0.7943 0.8155 0.0050 0.0090 0.2415 50 ARG A NE 448 C CZ . ARG A 50 ? 0.8297 0.7740 0.7811 -0.0059 0.0184 0.2387 50 ARG A CZ 449 N NH1 . ARG A 50 ? 0.8206 0.7930 0.7548 -0.0051 0.0221 0.2370 50 ARG A NH1 450 N NH2 . ARG A 50 ? 0.8187 0.7480 0.7859 -0.0174 0.0238 0.2368 50 ARG A NH2 451 N N . PHE A 51 ? 0.5387 0.4600 0.5462 0.0427 -0.0137 0.1853 51 PHE A N 452 C CA . PHE A 51 ? 0.5990 0.4964 0.6236 0.0492 -0.0132 0.1769 51 PHE A CA 453 C C . PHE A 51 ? 0.4251 0.3373 0.4621 0.0591 -0.0169 0.1646 51 PHE A C 454 O O . PHE A 51 ? 0.4543 0.3544 0.5043 0.0694 -0.0179 0.1603 51 PHE A O 455 C CB . PHE A 51 ? 0.6249 0.5008 0.6531 0.0381 -0.0054 0.1666 51 PHE A CB 456 C CG . PHE A 51 ? 0.7434 0.6049 0.7636 0.0262 -0.0014 0.1788 51 PHE A CG 457 C CD1 . PHE A 51 ? 0.8041 0.6375 0.8226 0.0286 -0.0029 0.1904 51 PHE A CD1 458 C CD2 . PHE A 51 ? 0.6885 0.5649 0.7028 0.0130 0.0043 0.1792 51 PHE A CD2 459 C CE1 . PHE A 51 ? 0.8156 0.6350 0.8269 0.0162 0.0012 0.2026 51 PHE A CE1 460 C CE2 . PHE A 51 ? 0.7999 0.6674 0.8096 0.0011 0.0087 0.1912 51 PHE A CE2 461 C CZ . PHE A 51 ? 0.8455 0.6839 0.8538 0.0018 0.0072 0.2032 51 PHE A CZ 462 N N . ALA A 52 ? 0.3952 0.3338 0.4271 0.0562 -0.0187 0.1591 52 ALA A N 463 C CA . ALA A 52 ? 0.3510 0.3046 0.3952 0.0626 -0.0214 0.1473 52 ALA A CA 464 C C . ALA A 52 ? 0.2905 0.2753 0.3242 0.0620 -0.0300 0.1503 52 ALA A C 465 O O . ALA A 52 ? 0.3097 0.3028 0.3223 0.0557 -0.0315 0.1571 52 ALA A O 466 C CB . ALA A 52 ? 0.3848 0.3297 0.4337 0.0571 -0.0134 0.1304 52 ALA A CB 467 N N . SER A 53 ? 0.2743 0.2769 0.3217 0.0678 -0.0356 0.1442 53 SER A N 468 C CA . SER A 53 ? 0.2942 0.3262 0.3317 0.0646 -0.0459 0.1441 53 SER A CA 469 C C . SER A 53 ? 0.2976 0.3411 0.3472 0.0629 -0.0456 0.1301 53 SER A C 470 O O . SER A 53 ? 0.2188 0.2507 0.2878 0.0674 -0.0374 0.1217 53 SER A O 471 C CB . SER A 53 ? 0.3002 0.3507 0.3436 0.0716 -0.0579 0.1551 53 SER A CB 472 O OG . SER A 53 ? 0.2782 0.3315 0.3504 0.0819 -0.0573 0.1532 53 SER A OG 473 N N . PHE A 54 ? 0.2264 0.2910 0.2614 0.0557 -0.0544 0.1263 54 PHE A N 474 C CA . PHE A 54 ? 0.2304 0.3063 0.2751 0.0503 -0.0550 0.1099 54 PHE A CA 475 C C . PHE A 54 ? 0.2867 0.3891 0.3200 0.0419 -0.0708 0.1084 54 PHE A C 476 O O . PHE A 54 ? 0.2767 0.3794 0.2774 0.0353 -0.0764 0.1083 54 PHE A O 477 C CB . PHE A 54 ? 0.2122 0.2680 0.2422 0.0422 -0.0424 0.0912 54 PHE A CB 478 C CG . PHE A 54 ? 0.1755 0.2378 0.2126 0.0357 -0.0415 0.0744 54 PHE A CG 479 C CD1 . PHE A 54 ? 0.2110 0.2747 0.2771 0.0413 -0.0355 0.0709 54 PHE A CD1 480 C CD2 . PHE A 54 ? 0.1802 0.2453 0.1933 0.0242 -0.0462 0.0627 54 PHE A CD2 481 C CE1 . PHE A 54 ? 0.1802 0.2510 0.2533 0.0343 -0.0336 0.0580 54 PHE A CE1 482 C CE2 . PHE A 54 ? 0.1985 0.2661 0.2183 0.0166 -0.0454 0.0491 54 PHE A CE2 483 C CZ . PHE A 54 ? 0.1662 0.2384 0.2171 0.0210 -0.0389 0.0478 54 PHE A CZ 484 N N . GLU A 55 ? 0.2086 0.3341 0.2682 0.0417 -0.0780 0.1070 55 GLU A N 485 C CA . GLU A 55 ? 0.2672 0.4197 0.3202 0.0303 -0.0952 0.1046 55 GLU A CA 486 C C . GLU A 55 ? 0.2653 0.4046 0.2959 0.0145 -0.0920 0.0826 55 GLU A C 487 O O . GLU A 55 ? 0.2611 0.3995 0.3095 0.0099 -0.0854 0.0717 55 GLU A O 488 C CB . GLU A 55 ? 0.2710 0.4546 0.3639 0.0341 -0.1019 0.1105 55 GLU A CB 489 C CG . GLU A 55 ? 0.3846 0.5951 0.4746 0.0186 -0.1189 0.1051 55 GLU A CG 490 C CD . GLU A 55 ? 0.5768 0.7861 0.6306 0.0138 -0.1317 0.1074 55 GLU A CD 491 O OE1 . GLU A 55 ? 0.6057 0.8198 0.6620 0.0251 -0.1346 0.1211 55 GLU A OE1 492 O OE2 . GLU A 55 ? 0.5771 0.7774 0.5974 -0.0007 -0.1377 0.0944 55 GLU A OE2 493 N N . ALA A 56 ? 0.3449 0.3009 0.2313 0.0197 -0.1088 0.1102 56 ALA A N 494 C CA . ALA A 56 ? 0.3299 0.2945 0.1978 0.0149 -0.0977 0.0974 56 ALA A CA 495 C C . ALA A 56 ? 0.3203 0.2972 0.1968 0.0170 -0.1077 0.0782 56 ALA A C 496 O O . ALA A 56 ? 0.3033 0.2884 0.1864 0.0152 -0.0953 0.0616 56 ALA A O 497 C CB . ALA A 56 ? 0.4173 0.3762 0.2351 0.0113 -0.0858 0.1052 56 ALA A CB 498 N N . GLN A 57 ? 0.3893 0.3721 0.2749 0.0204 -0.1241 0.0786 57 GLN A N 499 C CA . GLN A 57 ? 0.3860 0.3837 0.2855 0.0191 -0.1334 0.0636 57 GLN A CA 500 C C . GLN A 57 ? 0.3678 0.3778 0.3098 0.0216 -0.1285 0.0515 57 GLN A C 501 O O . GLN A 57 ? 0.3593 0.3782 0.3049 0.0173 -0.1272 0.0373 57 GLN A O 502 C CB . GLN A 57 ? 0.4207 0.4263 0.3328 0.0219 -0.1518 0.0710 57 GLN A CB 503 C CG . GLN A 57 ? 0.5961 0.6160 0.5156 0.0164 -0.1631 0.0594 57 GLN A CG 504 C CD . GLN A 57 ? 0.7324 0.7401 0.6020 0.0075 -0.1614 0.0495 57 GLN A CD 505 O OE1 . GLN A 57 ? 0.7305 0.7398 0.6002 0.0022 -0.1559 0.0342 57 GLN A OE1 506 N NE2 . GLN A 57 ? 0.7984 0.7916 0.6237 0.0067 -0.1645 0.0582 57 GLN A NE2 507 N N . GLY A 58 ? 0.3260 0.3333 0.2982 0.0286 -0.1243 0.0568 58 GLY A N 508 C CA . GLY A 58 ? 0.3312 0.3478 0.3400 0.0326 -0.1155 0.0444 58 GLY A CA 509 C C . GLY A 58 ? 0.3669 0.3839 0.3649 0.0259 -0.0967 0.0303 58 GLY A C 510 O O . GLY A 58 ? 0.3910 0.4191 0.4094 0.0259 -0.0904 0.0177 58 GLY A O 511 N N . ALA A 59 ? 0.2658 0.2723 0.2341 0.0206 -0.0868 0.0346 59 ALA A N 512 C CA . ALA A 59 ? 0.2624 0.2713 0.2234 0.0160 -0.0696 0.0245 59 ALA A CA 513 C C . ALA A 59 ? 0.2817 0.2964 0.2297 0.0132 -0.0711 0.0117 59 ALA A C 514 O O . ALA A 59 ? 0.2300 0.2495 0.1880 0.0117 -0.0614 0.0003 59 ALA A O 515 C CB . ALA A 59 ? 0.2832 0.2847 0.2212 0.0125 -0.0578 0.0354 59 ALA A CB 516 N N . LEU A 60 ? 0.2651 0.2756 0.1880 0.0116 -0.0854 0.0140 60 LEU A N 517 C CA . LEU A 60 ? 0.2315 0.2398 0.1361 0.0067 -0.0906 0.0012 60 LEU A CA 518 C C . LEU A 60 ? 0.2649 0.2884 0.2090 0.0046 -0.0960 -0.0082 60 LEU A C 519 O O . LEU A 60 ? 0.2311 0.2526 0.1729 0.0003 -0.0901 -0.0202 60 LEU A O 520 C CB . LEU A 60 ? 0.3446 0.3435 0.2146 0.0032 -0.1084 0.0057 60 LEU A CB 521 C CG . LEU A 60 ? 0.4525 0.4321 0.2678 0.0036 -0.0973 0.0084 60 LEU A CG 522 C CD1 . LEU A 60 ? 0.4679 0.4446 0.2763 0.0082 -0.0884 0.0264 60 LEU A CD1 523 C CD2 . LEU A 60 ? 0.5278 0.5010 0.3163 -0.0010 -0.1104 0.0075 60 LEU A CD2 524 N N . ALA A 61 ? 0.1900 0.2280 0.1714 0.0087 -0.1053 -0.0013 61 ALA A N 525 C CA . ALA A 61 ? 0.2586 0.3153 0.2811 0.0079 -0.1059 -0.0070 61 ALA A CA 526 C C . ALA A 61 ? 0.1769 0.2340 0.2114 0.0092 -0.0851 -0.0159 61 ALA A C 527 O O . ALA A 61 ? 0.1811 0.2454 0.2283 0.0042 -0.0816 -0.0239 61 ALA A O 528 C CB . ALA A 61 ? 0.2756 0.3469 0.3343 0.0157 -0.1112 0.0036 61 ALA A CB 529 N N . ASN A 62 ? 0.1813 0.2293 0.2109 0.0143 -0.0726 -0.0131 62 ASN A N 530 C CA . ASN A 62 ? 0.1100 0.1563 0.1458 0.0141 -0.0559 -0.0201 62 ASN A CA 531 C C . ASN A 62 ? 0.1095 0.1507 0.1255 0.0082 -0.0486 -0.0272 62 ASN A C 532 O O . ASN A 62 ? 0.1351 0.1795 0.1611 0.0060 -0.0409 -0.0338 62 ASN A O 533 C CB . ASN A 62 ? 0.1159 0.1506 0.1480 0.0173 -0.0489 -0.0147 62 ASN A CB 534 C CG . ASN A 62 ? 0.1546 0.1873 0.2091 0.0250 -0.0487 -0.0142 62 ASN A CG 535 O OD1 . ASN A 62 ? 0.1885 0.2328 0.2649 0.0308 -0.0540 -0.0137 62 ASN A OD1 536 N ND2 . ASN A 62 ? 0.1151 0.1326 0.1653 0.0253 -0.0425 -0.0142 62 ASN A ND2 537 N N . ILE A 63 ? 0.1532 0.1844 0.1393 0.0070 -0.0495 -0.0249 63 ILE A N 538 C CA . ILE A 63 ? 0.1416 0.1642 0.1072 0.0052 -0.0399 -0.0317 63 ILE A CA 539 C C . ILE A 63 ? 0.1435 0.1636 0.1095 -0.0005 -0.0476 -0.0419 63 ILE A C 540 O O . ILE A 63 ? 0.1779 0.1922 0.1430 -0.0019 -0.0390 -0.0487 63 ILE A O 541 C CB . ILE A 63 ? 0.2219 0.2325 0.1513 0.0076 -0.0357 -0.0273 63 ILE A CB 542 C CG1 . ILE A 63 ? 0.3032 0.3184 0.2384 0.0105 -0.0254 -0.0147 63 ILE A CG1 543 C CG2 . ILE A 63 ? 0.2623 0.2595 0.1676 0.0090 -0.0250 -0.0366 63 ILE A CG2 544 C CD1 . ILE A 63 ? 0.3447 0.3677 0.3039 0.0104 -0.0145 -0.0148 63 ILE A CD1 545 N N . ALA A 64 ? 0.1555 0.1804 0.1264 -0.0047 -0.0655 -0.0411 64 ALA A N 546 C CA . ALA A 64 ? 0.1743 0.1990 0.1525 -0.0139 -0.0758 -0.0481 64 ALA A CA 547 C C . ALA A 64 ? 0.1776 0.2175 0.1936 -0.0155 -0.0675 -0.0494 64 ALA A C 548 O O . ALA A 64 ? 0.1792 0.2120 0.1958 -0.0225 -0.0645 -0.0540 64 ALA A O 549 C CB . ALA A 64 ? 0.1996 0.2328 0.1842 -0.0194 -0.0938 -0.0407 64 ALA A CB 550 N N . VAL A 65 ? 0.1259 0.1823 0.1692 -0.0089 -0.0612 -0.0432 65 VAL A N 551 C CA . VAL A 65 ? 0.1017 0.1697 0.1724 -0.0087 -0.0491 -0.0439 65 VAL A CA 552 C C . VAL A 65 ? 0.1201 0.1744 0.1738 -0.0086 -0.0347 -0.0482 65 VAL A C 553 O O . VAL A 65 ? 0.1242 0.1792 0.1867 -0.0133 -0.0285 -0.0503 65 VAL A O 554 C CB . VAL A 65 ? 0.1330 0.2128 0.2256 0.0010 -0.0430 -0.0386 65 VAL A CB 555 C CG1 . VAL A 65 ? 0.1287 0.2133 0.2350 0.0025 -0.0265 -0.0408 65 VAL A CG1 556 C CG2 . VAL A 65 ? 0.1140 0.2122 0.2344 0.0032 -0.0561 -0.0318 65 VAL A CG2 557 N N . ASP A 66 ? 0.1088 0.1524 0.1413 -0.0036 -0.0299 -0.0470 66 ASP A N 558 C CA . ASP A 66 ? 0.0830 0.1180 0.1057 -0.0024 -0.0182 -0.0478 66 ASP A CA 559 C C . ASP A 66 ? 0.1367 0.1587 0.1464 -0.0059 -0.0173 -0.0536 66 ASP A C 560 O O . ASP A 66 ? 0.1546 0.1721 0.1675 -0.0065 -0.0096 -0.0540 66 ASP A O 561 C CB . ASP A 66 ? 0.1235 0.1548 0.1333 0.0025 -0.0141 -0.0423 66 ASP A CB 562 C CG . ASP A 66 ? 0.1394 0.1755 0.1593 0.0045 -0.0158 -0.0369 66 ASP A CG 563 O OD1 . ASP A 66 ? 0.1028 0.1427 0.1368 0.0048 -0.0152 -0.0389 66 ASP A OD1 564 O OD2 . ASP A 66 ? 0.1257 0.1592 0.1377 0.0061 -0.0164 -0.0302 66 ASP A OD2 565 N N . LYS A 67 ? 0.1226 0.1343 0.1142 -0.0082 -0.0262 -0.0581 67 LYS A N 566 C CA . LYS A 67 ? 0.1510 0.1412 0.1239 -0.0118 -0.0273 -0.0664 67 LYS A CA 567 C C . LYS A 67 ? 0.1960 0.1888 0.1910 -0.0221 -0.0320 -0.0679 67 LYS A C 568 O O . LYS A 67 ? 0.1492 0.1272 0.1412 -0.0235 -0.0257 -0.0703 67 LYS A O 569 C CB . LYS A 67 ? 0.1991 0.1733 0.1407 -0.0140 -0.0382 -0.0704 67 LYS A CB 570 C CG . LYS A 67 ? 0.2496 0.1971 0.1688 -0.0204 -0.0391 -0.0778 67 LYS A CG 571 C CD . LYS A 67 ? 0.3127 0.2511 0.2032 -0.0226 -0.0486 -0.0815 67 LYS A CD 572 C CE . LYS A 67 ? 0.4664 0.3780 0.3336 -0.0246 -0.0482 -0.0920 67 LYS A CE 573 N NZ . LYS A 67 ? 0.5269 0.4375 0.4124 -0.0389 -0.0624 -0.0944 67 LYS A NZ 574 N N . ALA A 68 ? 0.1473 0.1598 0.1673 -0.0283 -0.0414 -0.0633 68 ALA A N 575 C CA . ALA A 68 ? 0.1524 0.1734 0.1986 -0.0382 -0.0427 -0.0600 68 ALA A CA 576 C C . ALA A 68 ? 0.1348 0.1635 0.1961 -0.0353 -0.0266 -0.0572 68 ALA A C 577 O O . ALA A 68 ? 0.1706 0.1928 0.2387 -0.0426 -0.0228 -0.0559 68 ALA A O 578 C CB . ALA A 68 ? 0.2106 0.2567 0.2851 -0.0424 -0.0526 -0.0522 68 ALA A CB 579 N N . ASN A 69 ? 0.1286 0.1667 0.1897 -0.0253 -0.0177 -0.0539 69 ASN A N 580 C CA . ASN A 69 ? 0.1118 0.1514 0.1754 -0.0226 -0.0043 -0.0499 69 ASN A CA 581 C C . ASN A 69 ? 0.1184 0.1385 0.1643 -0.0214 0.0002 -0.0502 69 ASN A C 582 O O . ASN A 69 ? 0.1287 0.1455 0.1773 -0.0242 0.0068 -0.0458 69 ASN A O 583 C CB . ASN A 69 ? 0.1016 0.1488 0.1638 -0.0140 0.0006 -0.0479 69 ASN A CB 584 C CG . ASN A 69 ? 0.1075 0.1724 0.1915 -0.0118 0.0021 -0.0462 69 ASN A CG 585 O OD1 . ASN A 69 ? 0.1616 0.2398 0.2681 -0.0173 0.0010 -0.0441 69 ASN A OD1 586 N ND2 . ASN A 69 ? 0.1154 0.1802 0.1957 -0.0036 0.0048 -0.0463 69 ASN A ND2 587 N N . LEU A 70 ? 0.1074 0.1150 0.1354 -0.0161 -0.0020 -0.0538 70 LEU A N 588 C CA . LEU A 70 ? 0.1428 0.1330 0.1590 -0.0114 0.0041 -0.0532 70 LEU A CA 589 C C . LEU A 70 ? 0.1471 0.1189 0.1631 -0.0189 0.0024 -0.0557 70 LEU A C 590 O O . LEU A 70 ? 0.1745 0.1365 0.1914 -0.0173 0.0082 -0.0506 70 LEU A O 591 C CB . LEU A 70 ? 0.1253 0.1058 0.1227 -0.0024 0.0062 -0.0566 70 LEU A CB 592 C CG . LEU A 70 ? 0.1361 0.1000 0.1257 0.0067 0.0156 -0.0553 70 LEU A CG 593 C CD1 . LEU A 70 ? 0.1460 0.1232 0.1526 0.0098 0.0202 -0.0435 70 LEU A CD1 594 C CD2 . LEU A 70 ? 0.1728 0.1302 0.1438 0.0177 0.0227 -0.0579 70 LEU A CD2 595 N N . GLU A 71 ? 0.1422 0.1082 0.1578 -0.0281 -0.0077 -0.0622 71 GLU A N 596 C CA A GLU A 71 ? 0.1889 0.1359 0.2073 -0.0396 -0.0127 -0.0640 71 GLU A CA 597 C CA B GLU A 71 ? 0.1864 0.1327 0.2041 -0.0392 -0.0124 -0.0640 71 GLU A CA 598 C CA C GLU A 71 ? 0.1660 0.1126 0.1840 -0.0394 -0.0125 -0.0640 71 GLU A CA 599 C C . GLU A 71 ? 0.1807 0.1405 0.2215 -0.0460 -0.0058 -0.0530 71 GLU A C 600 O O . GLU A 71 ? 0.1862 0.1271 0.2250 -0.0488 -0.0021 -0.0490 71 GLU A O 601 C CB A GLU A 71 ? 0.1806 0.1297 0.2022 -0.0518 -0.0287 -0.0670 71 GLU A CB 602 C CB B GLU A 71 ? 0.2195 0.1636 0.2361 -0.0508 -0.0287 -0.0681 71 GLU A CB 603 C CB C GLU A 71 ? 0.2203 0.1660 0.2382 -0.0510 -0.0287 -0.0678 71 GLU A CB 604 C CG A GLU A 71 ? 0.2725 0.2013 0.2596 -0.0487 -0.0367 -0.0747 71 GLU A CG 605 C CG B GLU A 71 ? 0.2436 0.1590 0.2510 -0.0635 -0.0360 -0.0693 71 GLU A CG 606 C CG C GLU A 71 ? 0.2465 0.1843 0.2773 -0.0675 -0.0357 -0.0633 71 GLU A CG 607 C CD A GLU A 71 ? 0.3619 0.3006 0.3547 -0.0628 -0.0514 -0.0752 71 GLU A CD 608 C CD B GLU A 71 ? 0.2692 0.2051 0.3102 -0.0799 -0.0401 -0.0595 71 GLU A CD 609 C CD C GLU A 71 ? 0.3198 0.2157 0.3259 -0.0689 -0.0341 -0.0684 71 GLU A CD 610 O OE1 A GLU A 71 ? 0.3652 0.3156 0.3512 -0.0596 -0.0579 -0.0759 71 GLU A OE1 611 O OE1 B GLU A 71 ? 0.2687 0.2239 0.3352 -0.0793 -0.0294 -0.0506 71 GLU A OE1 612 O OE1 C GLU A 71 ? 0.3675 0.2422 0.3455 -0.0566 -0.0283 -0.0778 71 GLU A OE1 613 O OE2 A GLU A 71 ? 0.4249 0.3624 0.4333 -0.0760 -0.0567 -0.0741 71 GLU A OE2 614 O OE2 B GLU A 71 ? 0.2677 0.2051 0.3129 -0.0925 -0.0501 -0.0619 71 GLU A OE2 615 O OE2 C GLU A 71 ? 0.2625 0.1514 0.2821 -0.0811 -0.0339 -0.0630 71 GLU A OE2 616 N N . ILE A 72 ? 0.1602 0.1501 0.2203 -0.0472 -0.0029 -0.0477 72 ILE A N 617 C CA . ILE A 72 ? 0.1702 0.1737 0.2465 -0.0519 0.0072 -0.0374 72 ILE A CA 618 C C . ILE A 72 ? 0.1352 0.1284 0.1955 -0.0444 0.0165 -0.0315 72 ILE A C 619 O O . ILE A 72 ? 0.1811 0.1653 0.2421 -0.0501 0.0216 -0.0230 72 ILE A O 620 C CB . ILE A 72 ? 0.1833 0.2176 0.2780 -0.0492 0.0120 -0.0349 72 ILE A CB 621 C CG1 . ILE A 72 ? 0.1840 0.2346 0.3060 -0.0587 0.0016 -0.0351 72 ILE A CG1 622 C CG2 . ILE A 72 ? 0.2886 0.3326 0.3874 -0.0492 0.0277 -0.0256 72 ILE A CG2 623 C CD1 . ILE A 72 ? 0.2048 0.2855 0.3491 -0.0521 0.0052 -0.0326 72 ILE A CD1 624 N N . MET A 73 ? 0.1228 0.1177 0.1700 -0.0330 0.0169 -0.0338 73 MET A N 625 C CA . MET A 73 ? 0.1127 0.1025 0.1483 -0.0273 0.0213 -0.0264 73 MET A CA 626 C C . MET A 73 ? 0.1304 0.0977 0.1602 -0.0243 0.0203 -0.0228 73 MET A C 627 O O . MET A 73 ? 0.1731 0.1335 0.1987 -0.0239 0.0225 -0.0124 73 MET A O 628 C CB . MET A 73 ? 0.1492 0.1488 0.1781 -0.0188 0.0194 -0.0279 73 MET A CB 629 C CG . MET A 73 ? 0.1600 0.1749 0.1919 -0.0193 0.0211 -0.0314 73 MET A CG 630 S SD . MET A 73 ? 0.1729 0.1928 0.2027 -0.0242 0.0319 -0.0263 73 MET A SD 631 C CE . MET A 73 ? 0.1354 0.1410 0.1415 -0.0237 0.0303 -0.0172 73 MET A CE 632 N N . THR A 74 ? 0.1403 0.0932 0.1669 -0.0210 0.0171 -0.0312 74 THR A N 633 C CA . THR A 74 ? 0.1653 0.0908 0.1854 -0.0155 0.0184 -0.0299 74 THR A CA 634 C C . THR A 74 ? 0.1855 0.0946 0.2098 -0.0267 0.0181 -0.0231 74 THR A C 635 O O . THR A 74 ? 0.1998 0.0952 0.2227 -0.0227 0.0205 -0.0126 74 THR A O 636 C CB . THR A 74 ? 0.1843 0.0901 0.1914 -0.0104 0.0166 -0.0433 74 THR A CB 637 O OG1 . THR A 74 ? 0.1683 0.0907 0.1715 0.0001 0.0195 -0.0459 74 THR A OG1 638 C CG2 . THR A 74 ? 0.2187 0.0898 0.2166 -0.0016 0.0207 -0.0438 74 THR A CG2 639 N N . LYS A 75 ? 0.1882 0.1008 0.2210 -0.0413 0.0145 -0.0264 75 LYS A N 640 C CA . LYS A 75 ? 0.2075 0.1094 0.2493 -0.0552 0.0153 -0.0168 75 LYS A CA 641 C C . LYS A 75 ? 0.2013 0.1173 0.2442 -0.0560 0.0241 -0.0010 75 LYS A C 642 O O . LYS A 75 ? 0.2364 0.1335 0.2760 -0.0593 0.0261 0.0109 75 LYS A O 643 C CB . LYS A 75 ? 0.2646 0.1782 0.3245 -0.0719 0.0095 -0.0202 75 LYS A CB 644 C CG . LYS A 75 ? 0.3585 0.2488 0.4107 -0.0765 -0.0038 -0.0346 75 LYS A CG 645 C CD . LYS A 75 ? 0.3766 0.2878 0.4483 -0.0926 -0.0141 -0.0332 75 LYS A CD 646 C CE . LYS A 75 ? 0.3986 0.3264 0.4945 -0.1062 -0.0072 -0.0165 75 LYS A CE 647 N NZ . LYS A 75 ? 0.4634 0.4202 0.5820 -0.1190 -0.0133 -0.0137 75 LYS A NZ 648 N N . ARG A 76 ? 0.1775 0.1221 0.2206 -0.0529 0.0289 -0.0008 76 ARG A N 649 C CA . ARG A 76 ? 0.2118 0.1651 0.2451 -0.0532 0.0372 0.0117 76 ARG A CA 650 C C . ARG A 76 ? 0.1938 0.1306 0.2105 -0.0451 0.0336 0.0210 76 ARG A C 651 O O . ARG A 76 ? 0.2228 0.1526 0.2282 -0.0490 0.0370 0.0354 76 ARG A O 652 C CB . ARG A 76 ? 0.2012 0.1789 0.2300 -0.0483 0.0417 0.0062 76 ARG A CB 653 C CG . ARG A 76 ? 0.2718 0.2696 0.3145 -0.0554 0.0528 0.0077 76 ARG A CG 654 C CD . ARG A 76 ? 0.2379 0.2508 0.2695 -0.0469 0.0593 0.0022 76 ARG A CD 655 N NE . ARG A 76 ? 0.2376 0.2730 0.2952 -0.0470 0.0635 -0.0037 76 ARG A NE 656 C CZ . ARG A 76 ? 0.2434 0.2897 0.2991 -0.0376 0.0664 -0.0114 76 ARG A CZ 657 N NH1 . ARG A 76 ? 0.2173 0.2517 0.2434 -0.0299 0.0647 -0.0155 76 ARG A NH1 658 N NH2 . ARG A 76 ? 0.2386 0.3067 0.3236 -0.0366 0.0692 -0.0139 76 ARG A NH2 659 N N . SER A 77 ? 0.1893 0.1164 0.1670 -0.0588 0.0280 -0.0380 77 SER A N 660 C CA . SER A 77 ? 0.1994 0.1224 0.1534 -0.0595 0.0239 -0.0289 77 SER A CA 661 C C . SER A 77 ? 0.1967 0.1103 0.1476 -0.0586 0.0193 -0.0191 77 SER A C 662 O O . SER A 77 ? 0.2462 0.1578 0.1854 -0.0570 0.0154 -0.0073 77 SER A O 663 C CB . SER A 77 ? 0.1962 0.1207 0.1459 -0.0499 0.0164 -0.0285 77 SER A CB 664 O OG . SER A 77 ? 0.2102 0.1293 0.1665 -0.0406 0.0074 -0.0274 77 SER A OG 665 N N . ASN A 78 ? 0.2153 0.1239 0.1804 -0.0599 0.0207 -0.0231 78 ASN A N 666 C CA . ASN A 78 ? 0.2283 0.1235 0.1953 -0.0589 0.0195 -0.0170 78 ASN A CA 667 C C . ASN A 78 ? 0.2058 0.0935 0.1709 -0.0489 0.0131 -0.0157 78 ASN A C 668 O O . ASN A 78 ? 0.2336 0.1106 0.1976 -0.0456 0.0146 -0.0051 78 ASN A O 669 C CB . ASN A 78 ? 0.2741 0.1654 0.2321 -0.0653 0.0246 -0.0021 78 ASN A CB 670 C CG . ASN A 78 ? 0.2974 0.1952 0.2533 -0.0777 0.0332 -0.0045 78 ASN A CG 671 O OD1 . ASN A 78 ? 0.3256 0.2235 0.2961 -0.0812 0.0377 -0.0150 78 ASN A OD1 672 N ND2 . ASN A 78 ? 0.4546 0.3600 0.3922 -0.0863 0.0360 0.0053 78 ASN A ND2 673 N N . TYR A 79 ? 0.2074 0.1013 0.1747 -0.0442 0.0073 -0.0251 79 TYR A N 674 C CA . TYR A 79 ? 0.1920 0.0799 0.1556 -0.0367 0.0025 -0.0270 79 TYR A CA 675 C C . TYR A 79 ? 0.2264 0.1118 0.1817 -0.0296 0.0021 -0.0157 79 TYR A C 676 O O . TYR A 79 ? 0.2487 0.1224 0.2057 -0.0244 0.0041 -0.0124 79 TYR A O 677 C CB . TYR A 79 ? 0.2129 0.0862 0.1812 -0.0403 0.0057 -0.0334 79 TYR A CB 678 C CG . TYR A 79 ? 0.2403 0.1227 0.2169 -0.0489 0.0025 -0.0444 79 TYR A CG 679 C CD1 . TYR A 79 ? 0.2284 0.1141 0.2155 -0.0566 0.0066 -0.0445 79 TYR A CD1 680 C CD2 . TYR A 79 ? 0.2381 0.1312 0.2137 -0.0494 -0.0058 -0.0518 79 TYR A CD2 681 C CE1 . TYR A 79 ? 0.2334 0.1326 0.2326 -0.0637 0.0025 -0.0515 79 TYR A CE1 682 C CE2 . TYR A 79 ? 0.2377 0.1450 0.2231 -0.0587 -0.0114 -0.0577 79 TYR A CE2 683 C CZ . TYR A 79 ? 0.2349 0.1455 0.2338 -0.0654 -0.0073 -0.0575 79 TYR A CZ 684 O OH . TYR A 79 ? 0.2667 0.1943 0.2796 -0.0753 -0.0133 -0.0618 79 TYR A OH 685 N N . THR A 80 ? 0.2025 0.0998 0.1505 -0.0309 0.0010 -0.0103 80 THR A N 686 C CA . THR A 80 ? 0.1846 0.0861 0.1251 -0.0268 -0.0017 0.0011 80 THR A CA 687 C C . THR A 80 ? 0.2002 0.1039 0.1388 -0.0190 -0.0060 -0.0055 80 THR A C 688 O O . THR A 80 ? 0.2277 0.1388 0.1651 -0.0199 -0.0072 -0.0140 80 THR A O 689 C CB . THR A 80 ? 0.2092 0.1245 0.1379 -0.0363 -0.0009 0.0068 80 THR A CB 690 O OG1 . THR A 80 ? 0.2411 0.1552 0.1690 -0.0452 0.0035 0.0140 80 THR A OG1 691 C CG2 . THR A 80 ? 0.2270 0.1521 0.1484 -0.0350 -0.0060 0.0200 80 THR A CG2 692 N N . PRO A 81 ? 0.1819 0.0784 0.1232 -0.0112 -0.0065 -0.0009 81 PRO A N 693 C CA . PRO A 81 ? 0.1763 0.0741 0.1142 -0.0049 -0.0095 -0.0074 81 PRO A CA 694 C C . PRO A 81 ? 0.1873 0.0973 0.1196 -0.0033 -0.0126 -0.0007 81 PRO A C 695 O O . PRO A 81 ? 0.2066 0.1256 0.1367 -0.0077 -0.0135 0.0104 81 PRO A O 696 C CB . PRO A 81 ? 0.2207 0.1036 0.1647 0.0008 -0.0046 -0.0069 81 PRO A CB 697 C CG . PRO A 81 ? 0.3277 0.2063 0.2826 0.0013 -0.0001 0.0081 81 PRO A CG 698 C CD . PRO A 81 ? 0.2776 0.1627 0.2290 -0.0077 -0.0017 0.0102 81 PRO A CD 699 N N . ILE A 82 ? 0.1734 0.0853 0.1026 0.0012 -0.0146 -0.0070 82 ILE A N 700 C CA . ILE A 82 ? 0.1537 0.0758 0.0785 0.0021 -0.0165 -0.0027 82 ILE A CA 701 C C . ILE A 82 ? 0.1799 0.1036 0.1107 0.0070 -0.0168 0.0103 82 ILE A C 702 O O . ILE A 82 ? 0.2062 0.1181 0.1459 0.0134 -0.0128 0.0120 82 ILE A O 703 C CB . ILE A 82 ? 0.1438 0.0658 0.0664 0.0062 -0.0174 -0.0111 82 ILE A CB 704 C CG1 . ILE A 82 ? 0.1557 0.0878 0.0745 0.0032 -0.0168 -0.0105 82 ILE A CG1 705 C CG2 . ILE A 82 ? 0.2086 0.1220 0.1312 0.0134 -0.0169 -0.0123 82 ILE A CG2 706 C CD1 . ILE A 82 ? 0.1830 0.1144 0.1039 0.0062 -0.0156 -0.0173 82 ILE A CD1 707 N N . THR A 83 ? 0.1618 0.1009 0.0897 0.0026 -0.0202 0.0195 83 THR A N 708 C CA . THR A 83 ? 0.1731 0.1206 0.1122 0.0073 -0.0220 0.0351 83 THR A CA 709 C C . THR A 83 ? 0.1513 0.0996 0.0899 0.0128 -0.0214 0.0290 83 THR A C 710 O O . THR A 83 ? 0.1889 0.1429 0.1163 0.0074 -0.0225 0.0204 83 THR A O 711 C CB . THR A 83 ? 0.2348 0.2048 0.1701 -0.0040 -0.0286 0.0506 83 THR A CB 712 O OG1 . THR A 83 ? 0.2447 0.2137 0.1800 -0.0093 -0.0286 0.0586 83 THR A OG1 713 C CG2 . THR A 83 ? 0.2633 0.2486 0.2166 0.0011 -0.0318 0.0689 83 THR A CG2 714 N N . ASN A 84 ? 0.1724 0.1130 0.1245 0.0231 -0.0168 0.0327 84 ASN A N 715 C CA . ASN A 84 ? 0.1560 0.0972 0.1078 0.0278 -0.0147 0.0278 84 ASN A CA 716 C C . ASN A 84 ? 0.1489 0.1126 0.1035 0.0229 -0.0205 0.0385 84 ASN A C 717 O O . ASN A 84 ? 0.1836 0.1632 0.1511 0.0209 -0.0248 0.0564 84 ASN A O 718 C CB . ASN A 84 ? 0.1917 0.1195 0.1588 0.0381 -0.0050 0.0289 84 ASN A CB 719 C CG . ASN A 84 ? 0.2016 0.1072 0.1615 0.0388 0.0022 0.0145 84 ASN A CG 720 O OD1 . ASN A 84 ? 0.2151 0.1170 0.1571 0.0342 -0.0010 0.0017 84 ASN A OD1 721 N ND2 . ASN A 84 ? 0.2330 0.1249 0.2097 0.0434 0.0130 0.0173 84 ASN A ND2 722 N N . VAL A 85 ? 0.1644 0.1309 0.1079 0.0197 -0.0208 0.0287 85 VAL A N 723 C CA . VAL A 85 ? 0.1305 0.1170 0.0753 0.0129 -0.0246 0.0350 85 VAL A CA 724 C C . VAL A 85 ? 0.1274 0.1084 0.0777 0.0212 -0.0192 0.0310 85 VAL A C 725 O O . VAL A 85 ? 0.1425 0.1109 0.0819 0.0228 -0.0152 0.0182 85 VAL A O 726 C CB . VAL A 85 ? 0.1310 0.1229 0.0576 -0.0014 -0.0256 0.0245 85 VAL A CB 727 C CG1 . VAL A 85 ? 0.1439 0.1557 0.0691 -0.0121 -0.0280 0.0275 85 VAL A CG1 728 C CG2 . VAL A 85 ? 0.1613 0.1575 0.0797 -0.0113 -0.0285 0.0265 85 VAL A CG2 729 N N . PRO A 86 ? 0.1287 0.1205 0.0990 0.0266 -0.0183 0.0440 86 PRO A N 730 C CA . PRO A 86 ? 0.1389 0.1234 0.1149 0.0345 -0.0104 0.0393 86 PRO A CA 731 C C . PRO A 86 ? 0.1242 0.1186 0.0912 0.0267 -0.0120 0.0341 86 PRO A C 732 O O . PRO A 86 ? 0.1499 0.1628 0.1133 0.0144 -0.0189 0.0378 86 PRO A O 733 C CB . PRO A 86 ? 0.1379 0.1336 0.1450 0.0420 -0.0075 0.0570 86 PRO A CB 734 C CG . PRO A 86 ? 0.1788 0.2001 0.1942 0.0336 -0.0195 0.0748 86 PRO A CG 735 C CD . PRO A 86 ? 0.1452 0.1570 0.1368 0.0260 -0.0239 0.0657 86 PRO A CD 736 N N . PRO A 87 ? 0.1247 0.1071 0.0871 0.0317 -0.0045 0.0254 87 PRO A N 737 C CA . PRO A 87 ? 0.1299 0.1176 0.0855 0.0250 -0.0035 0.0201 87 PRO A CA 738 C C . PRO A 87 ? 0.1225 0.1319 0.0949 0.0213 -0.0044 0.0299 87 PRO A C 739 O O . PRO A 87 ? 0.1507 0.1693 0.1449 0.0282 -0.0031 0.0417 87 PRO A O 740 C CB . PRO A 87 ? 0.1455 0.1139 0.0919 0.0323 0.0046 0.0116 87 PRO A CB 741 C CG . PRO A 87 ? 0.1330 0.0925 0.0873 0.0417 0.0103 0.0138 87 PRO A CG 742 C CD . PRO A 87 ? 0.2023 0.1647 0.1633 0.0416 0.0047 0.0194 87 PRO A CD 743 N N . GLU A 88 ? 0.1227 0.1408 0.0879 0.0094 -0.0052 0.0248 88 GLU A N 744 C CA . GLU A 88 ? 0.1237 0.1595 0.1016 0.0043 -0.0040 0.0298 88 GLU A CA 745 C C . GLU A 88 ? 0.1383 0.1552 0.1112 0.0111 0.0070 0.0210 88 GLU A C 746 O O . GLU A 88 ? 0.1901 0.1881 0.1470 0.0112 0.0109 0.0109 88 GLU A O 747 C CB . GLU A 88 ? 0.1716 0.2249 0.1409 -0.0163 -0.0086 0.0259 88 GLU A CB 748 C CG . GLU A 88 ? 0.3109 0.3861 0.2782 -0.0281 -0.0203 0.0348 88 GLU A CG 749 C CD . GLU A 88 ? 0.4494 0.5424 0.4024 -0.0538 -0.0227 0.0276 88 GLU A CD 750 O OE1 . GLU A 88 ? 0.5117 0.5960 0.4589 -0.0610 -0.0133 0.0141 88 GLU A OE1 751 O OE2 . GLU A 88 ? 0.4587 0.5741 0.4055 -0.0685 -0.0329 0.0353 88 GLU A OE2 752 N N . VAL A 89 ? 0.1263 0.1495 0.1154 0.0166 0.0125 0.0269 89 VAL A N 753 C CA . VAL A 89 ? 0.1314 0.1372 0.1137 0.0222 0.0236 0.0202 89 VAL A CA 754 C C . VAL A 89 ? 0.1331 0.1537 0.1278 0.0151 0.0278 0.0224 89 VAL A C 755 O O . VAL A 89 ? 0.1421 0.1865 0.1598 0.0132 0.0249 0.0328 89 VAL A O 756 C CB . VAL A 89 ? 0.1650 0.1578 0.1515 0.0353 0.0320 0.0214 89 VAL A CB 757 C CG1 . VAL A 89 ? 0.1835 0.1606 0.1577 0.0377 0.0434 0.0151 89 VAL A CG1 758 C CG2 . VAL A 89 ? 0.1793 0.1578 0.1535 0.0399 0.0283 0.0179 89 VAL A CG2 759 N N . THR A 90 ? 0.1384 0.1465 0.1210 0.0109 0.0346 0.0145 90 THR A N 760 C CA A THR A 90 ? 0.1425 0.1607 0.1354 0.0033 0.0408 0.0148 90 THR A CA 761 C CA B THR A 90 ? 0.1609 0.1793 0.1544 0.0038 0.0409 0.0151 90 THR A CA 762 C C . THR A 90 ? 0.1647 0.1622 0.1489 0.0103 0.0532 0.0120 90 THR A C 763 O O . THR A 90 ? 0.1792 0.1561 0.1454 0.0145 0.0548 0.0085 90 THR A O 764 C CB A THR A 90 ? 0.1461 0.1697 0.1335 -0.0142 0.0395 0.0072 90 THR A CB 765 C CB B THR A 90 ? 0.1874 0.2149 0.1776 -0.0145 0.0388 0.0086 90 THR A CB 766 O OG1 A THR A 90 ? 0.1819 0.2242 0.1695 -0.0241 0.0278 0.0089 90 THR A OG1 767 O OG1 B THR A 90 ? 0.1819 0.1869 0.1547 -0.0156 0.0417 -0.0006 90 THR A OG1 768 C CG2 A THR A 90 ? 0.2058 0.2428 0.2057 -0.0252 0.0457 0.0069 90 THR A CG2 769 C CG2 B THR A 90 ? 0.2013 0.2581 0.1997 -0.0261 0.0260 0.0142 90 THR A CG2 770 N N . VAL A 91 ? 0.1653 0.1705 0.1631 0.0104 0.0615 0.0154 91 VAL A N 771 C CA . VAL A 91 ? 0.1674 0.1551 0.1550 0.0136 0.0740 0.0137 91 VAL A CA 772 C C . VAL A 91 ? 0.1800 0.1741 0.1767 0.0026 0.0804 0.0125 91 VAL A C 773 O O . VAL A 91 ? 0.2062 0.2238 0.2239 -0.0049 0.0789 0.0149 91 VAL A O 774 C CB . VAL A 91 ? 0.1745 0.1598 0.1669 0.0229 0.0840 0.0163 91 VAL A CB 775 C CG1 . VAL A 91 ? 0.3050 0.2762 0.2849 0.0222 0.0975 0.0154 91 VAL A CG1 776 C CG2 . VAL A 91 ? 0.2714 0.2447 0.2507 0.0313 0.0811 0.0142 91 VAL A CG2 777 N N . LEU A 92 ? 0.1823 0.1571 0.1659 0.0007 0.0873 0.0103 92 LEU A N 778 C CA . LEU A 92 ? 0.2174 0.1929 0.2099 -0.0103 0.0967 0.0082 92 LEU A CA 779 C C . LEU A 92 ? 0.2352 0.1881 0.2161 -0.0058 0.1081 0.0126 92 LEU A C 780 O O . LEU A 92 ? 0.2463 0.1858 0.2100 0.0035 0.1060 0.0174 92 LEU A O 781 C CB . LEU A 92 ? 0.2155 0.1928 0.2105 -0.0239 0.0940 0.0000 92 LEU A CB 782 C CG . LEU A 92 ? 0.3330 0.2881 0.3160 -0.0209 0.0942 -0.0028 92 LEU A CG 783 C CD1 . LEU A 92 ? 0.4801 0.4300 0.4696 -0.0373 0.1027 -0.0135 92 LEU A CD1 784 C CD2 . LEU A 92 ? 0.3492 0.3082 0.3238 -0.0143 0.0808 -0.0028 92 LEU A CD2 785 N N . THR A 93 ? 0.2167 0.1676 0.2069 -0.0139 0.1197 0.0125 93 THR A N 786 C CA . THR A 93 ? 0.2343 0.1644 0.2158 -0.0108 0.1296 0.0197 93 THR A CA 787 C C . THR A 93 ? 0.2625 0.1773 0.2504 -0.0163 0.1338 0.0177 93 THR A C 788 O O . THR A 93 ? 0.2629 0.1834 0.2614 -0.0275 0.1342 0.0069 93 THR A O 789 C CB . THR A 93 ? 0.2453 0.1796 0.2347 -0.0142 0.1379 0.0213 93 THR A CB 790 O OG1 . THR A 93 ? 0.2564 0.2021 0.2656 -0.0275 0.1415 0.0136 93 THR A OG1 791 C CG2 . THR A 93 ? 0.2788 0.2260 0.2667 -0.0082 0.1373 0.0222 93 THR A CG2 792 N N A ASN A 94 ? 0.2719 0.1687 0.2542 -0.0091 0.1369 0.0286 94 ASN A N 793 N N B ASN A 94 ? 0.2920 0.1884 0.2751 -0.0095 0.1371 0.0282 94 ASN A N 794 C CA A ASN A 94 ? 0.3409 0.2211 0.3361 -0.0101 0.1433 0.0299 94 ASN A CA 795 C CA B ASN A 94 ? 0.2981 0.1792 0.2954 -0.0123 0.1436 0.0266 94 ASN A CA 796 C C A ASN A 94 ? 0.3101 0.1869 0.3219 -0.0210 0.1549 0.0210 94 ASN A C 797 C C B ASN A 94 ? 0.3055 0.1810 0.3183 -0.0208 0.1557 0.0214 94 ASN A C 798 O O A ASN A 94 ? 0.2848 0.1530 0.3097 -0.0277 0.1617 0.0107 94 ASN A O 799 O O B ASN A 94 ? 0.3508 0.2145 0.3779 -0.0252 0.1641 0.0142 94 ASN A O 800 C CB A ASN A 94 ? 0.2798 0.1508 0.2694 0.0011 0.1415 0.0485 94 ASN A CB 801 C CB B ASN A 94 ? 0.3370 0.2066 0.3316 -0.0001 0.1401 0.0420 94 ASN A CB 802 C CG A ASN A 94 ? 0.4393 0.2993 0.4467 0.0056 0.1441 0.0535 94 ASN A CG 803 C CG B ASN A 94 ? 0.3433 0.2107 0.3333 0.0050 0.1415 0.0577 94 ASN A CG 804 O OD1 A ASN A 94 ? 0.5164 0.3700 0.5411 -0.0004 0.1529 0.0405 94 ASN A OD1 805 O OD1 B ASN A 94 ? 0.3283 0.2011 0.3101 0.0017 0.1444 0.0572 94 ASN A OD1 806 N ND2 A ASN A 94 ? 0.4618 0.3233 0.4662 0.0150 0.1362 0.0716 94 ASN A ND2 807 N ND2 B ASN A 94 ? 0.4234 0.2862 0.4207 0.0123 0.1389 0.0726 94 ASN A ND2 808 N N . SER A 95 ? 0.2900 0.1737 0.3004 -0.0232 0.1579 0.0234 95 SER A N 809 C CA . SER A 95 ? 0.2989 0.1794 0.3233 -0.0328 0.1688 0.0174 95 SER A CA 810 C C . SER A 95 ? 0.2934 0.1944 0.3191 -0.0400 0.1674 0.0130 95 SER A C 811 O O . SER A 95 ? 0.2815 0.1957 0.2983 -0.0341 0.1606 0.0174 95 SER A O 812 C CB . SER A 95 ? 0.3562 0.2199 0.3836 -0.0251 0.1773 0.0315 95 SER A CB 813 O OG . SER A 95 ? 0.5426 0.4115 0.5534 -0.0177 0.1726 0.0454 95 SER A OG 814 N N . PRO A 96 ? 0.3038 0.2086 0.3430 -0.0528 0.1746 0.0040 96 PRO A N 815 C CA . PRO A 96 ? 0.2996 0.2275 0.3459 -0.0593 0.1736 0.0026 96 PRO A CA 816 C C . PRO A 96 ? 0.3281 0.2541 0.3665 -0.0481 0.1765 0.0149 96 PRO A C 817 O O . PRO A 96 ? 0.3205 0.2269 0.3507 -0.0415 0.1826 0.0240 96 PRO A O 818 C CB . PRO A 96 ? 0.3182 0.2432 0.3777 -0.0737 0.1831 -0.0067 96 PRO A CB 819 C CG . PRO A 96 ? 0.3258 0.2348 0.3850 -0.0792 0.1858 -0.0174 96 PRO A CG 820 C CD . PRO A 96 ? 0.3216 0.2116 0.3716 -0.0625 0.1846 -0.0067 96 PRO A CD 821 N N . VAL A 97 ? 0.3291 0.2766 0.3708 -0.0465 0.1726 0.0156 97 VAL A N 822 C CA . VAL A 97 ? 0.3001 0.2448 0.3312 -0.0370 0.1763 0.0236 97 VAL A CA 823 C C . VAL A 97 ? 0.3174 0.2636 0.3576 -0.0422 0.1873 0.0250 97 VAL A C 824 O O . VAL A 97 ? 0.3814 0.3460 0.4427 -0.0516 0.1892 0.0198 97 VAL A O 825 C CB . VAL A 97 ? 0.3236 0.2867 0.3570 -0.0308 0.1706 0.0228 97 VAL A CB 826 C CG1 . VAL A 97 ? 0.4189 0.3756 0.4390 -0.0233 0.1769 0.0271 97 VAL A CG1 827 C CG2 . VAL A 97 ? 0.3874 0.3479 0.4102 -0.0254 0.1602 0.0219 97 VAL A CG2 828 N N . GLU A 98 ? 0.3583 0.2873 0.3824 -0.0374 0.1939 0.0333 98 GLU A N 829 C CA . GLU A 98 ? 0.3641 0.2933 0.3924 -0.0413 0.2051 0.0358 98 GLU A CA 830 C C . GLU A 98 ? 0.3691 0.2949 0.3758 -0.0348 0.2079 0.0415 98 GLU A C 831 O O . GLU A 98 ? 0.3955 0.3109 0.3790 -0.0294 0.2027 0.0479 98 GLU A O 832 C CB . GLU A 98 ? 0.4210 0.3318 0.4504 -0.0455 0.2127 0.0408 98 GLU A CB 833 C CG . GLU A 98 ? 0.4604 0.3698 0.5085 -0.0542 0.2129 0.0317 98 GLU A CG 834 C CD . GLU A 98 ? 0.7829 0.6700 0.8346 -0.0560 0.2231 0.0364 98 GLU A CD 835 O OE1 . GLU A 98 ? 0.8708 0.7579 0.9383 -0.0663 0.2317 0.0294 98 GLU A OE1 836 O OE2 . GLU A 98 ? 0.8355 0.7066 0.8762 -0.0473 0.2225 0.0481 98 GLU A OE2 837 N N . LEU A 99 ? 0.3989 0.3348 0.4135 -0.0367 0.2164 0.0387 99 LEU A N 838 C CA . LEU A 99 ? 0.4375 0.3699 0.4314 -0.0335 0.2221 0.0404 99 LEU A CA 839 C C . LEU A 99 ? 0.4203 0.3368 0.3846 -0.0351 0.2238 0.0515 99 LEU A C 840 O O . LEU A 99 ? 0.4336 0.3425 0.4016 -0.0393 0.2283 0.0588 99 LEU A O 841 C CB . LEU A 99 ? 0.4561 0.3993 0.4675 -0.0365 0.2347 0.0358 99 LEU A CB 842 C CG . LEU A 99 ? 0.4261 0.3900 0.4676 -0.0334 0.2329 0.0289 99 LEU A CG 843 C CD1 . LEU A 99 ? 0.4759 0.4504 0.5386 -0.0355 0.2469 0.0266 99 LEU A CD1 844 C CD2 . LEU A 99 ? 0.4402 0.4024 0.4704 -0.0252 0.2267 0.0256 99 LEU A CD2 845 N N . ARG A 100 ? 0.4291 0.3428 0.3655 -0.0329 0.2196 0.0535 100 ARG A N 846 C CA . ARG A 100 ? 0.4756 0.3820 0.3809 -0.0364 0.2172 0.0670 100 ARG A CA 847 C C . ARG A 100 ? 0.4674 0.3652 0.3756 -0.0354 0.2101 0.0815 100 ARG A C 848 O O . ARG A 100 ? 0.5277 0.4219 0.4209 -0.0398 0.2104 0.0973 100 ARG A O 849 C CB . ARG A 100 ? 0.7177 0.6251 0.6079 -0.0443 0.2300 0.0700 100 ARG A CB 850 C CG . ARG A 100 ? 0.8047 0.7089 0.7126 -0.0485 0.2407 0.0749 100 ARG A CG 851 C CD . ARG A 100 ? 0.8979 0.8050 0.7959 -0.0555 0.2556 0.0723 100 ARG A CD 852 N NE . ARG A 100 ? 0.8720 0.7857 0.7889 -0.0527 0.2635 0.0555 100 ARG A NE 853 C CZ . ARG A 100 ? 0.8764 0.7962 0.8279 -0.0518 0.2700 0.0492 100 ARG A CZ 854 N NH1 . ARG A 100 ? 0.8636 0.7811 0.8312 -0.0546 0.2704 0.0551 100 ARG A NH1 855 N NH2 . ARG A 100 ? 0.8489 0.7779 0.8210 -0.0488 0.2762 0.0378 100 ARG A NH2 856 N N . GLU A 101 ? 0.4290 0.3244 0.3583 -0.0303 0.2042 0.0767 101 GLU A N 857 C CA . GLU A 101 ? 0.4287 0.3140 0.3638 -0.0274 0.1983 0.0879 101 GLU A CA 858 C C . GLU A 101 ? 0.4109 0.2979 0.3369 -0.0213 0.1848 0.0876 101 GLU A C 859 O O . GLU A 101 ? 0.3861 0.2778 0.3218 -0.0185 0.1815 0.0742 101 GLU A O 860 C CB . GLU A 101 ? 0.4181 0.2977 0.3847 -0.0287 0.2047 0.0806 101 GLU A CB 861 C CG . GLU A 101 ? 0.4615 0.3382 0.4395 -0.0354 0.2181 0.0814 101 GLU A CG 862 C CD . GLU A 101 ? 0.7041 0.5709 0.6721 -0.0361 0.2217 0.1010 101 GLU A CD 863 O OE1 . GLU A 101 ? 0.7006 0.5609 0.6658 -0.0313 0.2144 0.1141 101 GLU A OE1 864 O OE2 . GLU A 101 ? 0.7795 0.6468 0.7441 -0.0419 0.2315 0.1047 101 GLU A OE2 865 N N . PRO A 102 ? 0.4253 0.3107 0.3335 -0.0205 0.1758 0.1038 102 PRO A N 866 C CA . PRO A 102 ? 0.4126 0.3012 0.3098 -0.0159 0.1618 0.1054 102 PRO A CA 867 C C . PRO A 102 ? 0.4090 0.2931 0.3296 -0.0092 0.1594 0.0951 102 PRO A C 868 O O . PRO A 102 ? 0.3815 0.2568 0.3264 -0.0081 0.1652 0.0957 102 PRO A O 869 C CB . PRO A 102 ? 0.4883 0.3759 0.3772 -0.0172 0.1534 0.1289 102 PRO A CB 870 C CG . PRO A 102 ? 0.4662 0.3549 0.3439 -0.0259 0.1615 0.1387 102 PRO A CG 871 C CD . PRO A 102 ? 0.4573 0.3401 0.3564 -0.0254 0.1773 0.1239 102 PRO A CD 872 N N . ASN A 103 ? 0.3644 0.2544 0.2771 -0.0063 0.1521 0.0846 103 ASN A N 873 C CA . ASN A 103 ? 0.3386 0.2270 0.2689 -0.0023 0.1491 0.0746 103 ASN A CA 874 C C . ASN A 103 ? 0.3286 0.2207 0.2430 0.0024 0.1361 0.0750 103 ASN A C 875 O O . ASN A 103 ? 0.3430 0.2394 0.2339 0.0011 0.1293 0.0826 103 ASN A O 876 C CB . ASN A 103 ? 0.3233 0.2194 0.2676 -0.0058 0.1554 0.0584 103 ASN A CB 877 C CG . ASN A 103 ? 0.3324 0.2282 0.2994 -0.0084 0.1557 0.0493 103 ASN A CG 878 O OD1 . ASN A 103 ? 0.2957 0.1885 0.2631 -0.0053 0.1491 0.0485 103 ASN A OD1 879 N ND2 . ASN A 103 ? 0.3417 0.2425 0.3270 -0.0163 0.1634 0.0416 103 ASN A ND2 880 N N . VAL A 104 ? 0.3068 0.1986 0.2327 0.0055 0.1324 0.0665 104 VAL A N 881 C CA . VAL A 104 ? 0.2968 0.1917 0.2094 0.0100 0.1205 0.0658 104 VAL A CA 882 C C . VAL A 104 ? 0.2802 0.1809 0.1999 0.0106 0.1197 0.0508 104 VAL A C 883 O O . VAL A 104 ? 0.2638 0.1649 0.2030 0.0074 0.1240 0.0443 104 VAL A O 884 C CB . VAL A 104 ? 0.2960 0.1852 0.2176 0.0143 0.1133 0.0766 104 VAL A CB 885 C CG1 . VAL A 104 ? 0.2862 0.1803 0.1941 0.0181 0.1000 0.0755 104 VAL A CG1 886 C CG2 . VAL A 104 ? 0.3226 0.2108 0.2440 0.0138 0.1119 0.0954 104 VAL A CG2 887 N N . LEU A 105 ? 0.2710 0.1778 0.1759 0.0128 0.1144 0.0449 105 LEU A N 888 C CA . LEU A 105 ? 0.2507 0.1651 0.1642 0.0150 0.1111 0.0344 105 LEU A CA 889 C C . LEU A 105 ? 0.2411 0.1517 0.1495 0.0188 0.1009 0.0359 105 LEU A C 890 O O . LEU A 105 ? 0.2541 0.1602 0.1465 0.0209 0.0934 0.0430 105 LEU A O 891 C CB . LEU A 105 ? 0.2535 0.1738 0.1601 0.0166 0.1120 0.0273 105 LEU A CB 892 C CG . LEU A 105 ? 0.2693 0.1969 0.1918 0.0140 0.1234 0.0239 105 LEU A CG 893 C CD1 . LEU A 105 ? 0.3770 0.3045 0.2923 0.0149 0.1286 0.0178 105 LEU A CD1 894 C CD2 . LEU A 105 ? 0.3169 0.2592 0.2681 0.0134 0.1241 0.0208 105 LEU A CD2 895 N N . ILE A 106 ? 0.2226 0.1399 0.1489 0.0175 0.0960 0.0281 106 ILE A N 896 C CA . ILE A 106 ? 0.2119 0.1277 0.1380 0.0200 0.0848 0.0262 106 ILE A CA 897 C C . ILE A 106 ? 0.2067 0.1342 0.1352 0.0214 0.0773 0.0180 106 ILE A C 898 O O . ILE A 106 ? 0.2046 0.1451 0.1479 0.0176 0.0790 0.0138 106 ILE A O 899 C CB . ILE A 106 ? 0.2175 0.1294 0.1611 0.0144 0.0880 0.0233 106 ILE A CB 900 C CG1 . ILE A 106 ? 0.2251 0.1236 0.1748 0.0132 0.0995 0.0327 106 ILE A CG1 901 C CG2 . ILE A 106 ? 0.2259 0.1348 0.1699 0.0170 0.0793 0.0213 106 ILE A CG2 902 C CD1 . ILE A 106 ? 0.2468 0.1374 0.2172 0.0051 0.1097 0.0262 106 ILE A CD1 903 N N . CYS A 107 ? 0.1949 0.1197 0.1111 0.0263 0.0687 0.0178 107 CYS A N 904 C CA . CYS A 107 ? 0.1822 0.1156 0.1032 0.0282 0.0618 0.0120 107 CYS A CA 905 C C . CYS A 107 ? 0.2093 0.1422 0.1330 0.0269 0.0529 0.0101 107 CYS A C 906 O O . CYS A 107 ? 0.2132 0.1377 0.1277 0.0296 0.0487 0.0132 107 CYS A O 907 C CB . CYS A 107 ? 0.1909 0.1193 0.0964 0.0327 0.0620 0.0106 107 CYS A CB 908 S SG . CYS A 107 ? 0.2193 0.1554 0.1373 0.0366 0.0576 0.0058 107 CYS A SG 909 N N . PHE A 108 ? 0.1736 0.1174 0.1103 0.0210 0.0505 0.0059 108 PHE A N 910 C CA . PHE A 108 ? 0.1610 0.1037 0.0989 0.0170 0.0452 0.0018 108 PHE A CA 911 C C . PHE A 108 ? 0.1739 0.1257 0.1109 0.0189 0.0357 0.0009 108 PHE A C 912 O O . PHE A 108 ? 0.1603 0.1274 0.1065 0.0166 0.0332 0.0028 108 PHE A O 913 C CB . PHE A 108 ? 0.1760 0.1245 0.1238 0.0042 0.0505 -0.0042 108 PHE A CB 914 C CG . PHE A 108 ? 0.2378 0.1832 0.1854 -0.0031 0.0496 -0.0115 108 PHE A CG 915 C CD1 . PHE A 108 ? 0.2837 0.2146 0.2300 0.0038 0.0502 -0.0101 108 PHE A CD1 916 C CD2 . PHE A 108 ? 0.2783 0.2375 0.2276 -0.0186 0.0490 -0.0192 108 PHE A CD2 917 C CE1 . PHE A 108 ? 0.3414 0.2685 0.2908 -0.0029 0.0528 -0.0178 108 PHE A CE1 918 C CE2 . PHE A 108 ? 0.2363 0.1913 0.1825 -0.0280 0.0515 -0.0283 108 PHE A CE2 919 C CZ . PHE A 108 ? 0.2438 0.1810 0.1914 -0.0192 0.0549 -0.0283 108 PHE A CZ 920 N N . ILE A 109 ? 0.1453 0.0891 0.0744 0.0232 0.0304 0.0004 109 ILE A N 921 C CA . ILE A 109 ? 0.1742 0.1231 0.1023 0.0254 0.0227 0.0001 109 ILE A CA 922 C C . ILE A 109 ? 0.1871 0.1373 0.1157 0.0187 0.0191 -0.0042 109 ILE A C 923 O O . ILE A 109 ? 0.1806 0.1205 0.1076 0.0195 0.0211 -0.0060 109 ILE A O 924 C CB . ILE A 109 ? 0.1547 0.0930 0.0712 0.0331 0.0211 0.0008 109 ILE A CB 925 C CG1 . ILE A 109 ? 0.1812 0.1156 0.0926 0.0364 0.0286 0.0022 109 ILE A CG1 926 C CG2 . ILE A 109 ? 0.1692 0.1097 0.0873 0.0352 0.0159 -0.0001 109 ILE A CG2 927 C CD1 . ILE A 109 ? 0.3850 0.3113 0.2844 0.0360 0.0313 0.0054 109 ILE A CD1 928 N N . ASP A 110 ? 0.1467 0.1112 0.0794 0.0111 0.0147 -0.0044 110 ASP A N 929 C CA . ASP A 110 ? 0.1330 0.0999 0.0631 -0.0008 0.0151 -0.0112 110 ASP A CA 930 C C . ASP A 110 ? 0.1517 0.1294 0.0792 -0.0045 0.0065 -0.0085 110 ASP A C 931 O O . ASP A 110 ? 0.1381 0.1264 0.0712 0.0001 0.0001 0.0008 110 ASP A O 932 C CB . ASP A 110 ? 0.1575 0.1347 0.0904 -0.0154 0.0205 -0.0157 110 ASP A CB 933 C CG . ASP A 110 ? 0.2227 0.1952 0.1509 -0.0306 0.0283 -0.0279 110 ASP A CG 934 O OD1 . ASP A 110 ? 0.1912 0.1494 0.1190 -0.0268 0.0322 -0.0321 110 ASP A OD1 935 O OD2 . ASP A 110 ? 0.2453 0.2290 0.1715 -0.0482 0.0322 -0.0342 110 ASP A OD2 936 N N . LYS A 111 ? 0.1336 0.1072 0.0551 -0.0126 0.0083 -0.0158 111 LYS A N 937 C CA A LYS A 111 ? 0.1351 0.1205 0.0509 -0.0211 0.0017 -0.0139 111 LYS A CA 938 C CA B LYS A 111 ? 0.1352 0.1205 0.0509 -0.0212 0.0017 -0.0140 111 LYS A CA 939 C C . LYS A 111 ? 0.1757 0.1592 0.0945 -0.0087 -0.0060 -0.0049 111 LYS A C 940 O O . LYS A 111 ? 0.1506 0.1490 0.0730 -0.0106 -0.0135 0.0056 111 LYS A O 941 C CB A LYS A 111 ? 0.1938 0.2046 0.1081 -0.0366 -0.0038 -0.0088 111 LYS A CB 942 C CB B LYS A 111 ? 0.1417 0.1521 0.0555 -0.0374 -0.0032 -0.0096 111 LYS A CB 943 C CG A LYS A 111 ? 0.1529 0.1672 0.0619 -0.0543 0.0049 -0.0202 111 LYS A CG 944 C CG B LYS A 111 ? 0.1587 0.1813 0.0647 -0.0543 -0.0056 -0.0114 111 LYS A CG 945 C CD A LYS A 111 ? 0.2493 0.2939 0.1560 -0.0739 -0.0030 -0.0142 111 LYS A CD 946 C CD B LYS A 111 ? 0.2502 0.2979 0.1570 -0.0739 -0.0082 -0.0086 111 LYS A CD 947 C CE A LYS A 111 ? 0.2959 0.3430 0.2004 -0.0936 0.0078 -0.0269 111 LYS A CE 948 C CE B LYS A 111 ? 0.3383 0.3944 0.2405 -0.0908 -0.0062 -0.0106 111 LYS A CE 949 N NZ A LYS A 111 ? 0.2896 0.3359 0.1970 -0.0920 0.0115 -0.0294 111 LYS A NZ 950 N NZ B LYS A 111 ? 0.1934 0.2760 0.0928 -0.1130 -0.0078 -0.0066 111 LYS A NZ 951 N N . PHE A 112 ? 0.1247 0.0910 0.0436 0.0028 -0.0040 -0.0078 112 PHE A N 952 C CA . PHE A 112 ? 0.1397 0.1013 0.0602 0.0122 -0.0086 -0.0027 112 PHE A CA 953 C C . PHE A 112 ? 0.1466 0.0972 0.0634 0.0139 -0.0088 -0.0080 112 PHE A C 954 O O . PHE A 112 ? 0.1295 0.0743 0.0468 0.0122 -0.0046 -0.0138 112 PHE A O 955 C CB . PHE A 112 ? 0.1380 0.0929 0.0617 0.0230 -0.0064 0.0000 112 PHE A CB 956 C CG . PHE A 112 ? 0.1471 0.0903 0.0645 0.0269 -0.0028 -0.0051 112 PHE A CG 957 C CD1 . PHE A 112 ? 0.1740 0.1076 0.0852 0.0309 -0.0046 -0.0072 112 PHE A CD1 958 C CD2 . PHE A 112 ? 0.1521 0.0960 0.0707 0.0250 0.0019 -0.0059 112 PHE A CD2 959 C CE1 . PHE A 112 ? 0.1644 0.0929 0.0706 0.0328 -0.0040 -0.0072 112 PHE A CE1 960 C CE2 . PHE A 112 ? 0.1810 0.1160 0.0963 0.0287 0.0045 -0.0058 112 PHE A CE2 961 C CZ . PHE A 112 ? 0.1625 0.0917 0.0715 0.0326 0.0005 -0.0050 112 PHE A CZ 962 N N . THR A 113 ? 0.1020 0.0960 0.0742 0.0108 0.0006 -0.0034 113 THR A N 963 C CA . THR A 113 ? 0.1055 0.1015 0.0749 0.0074 -0.0038 -0.0068 113 THR A CA 964 C C . THR A 113 ? 0.1144 0.1024 0.0853 0.0036 0.0018 -0.0102 113 THR A C 965 O O . THR A 113 ? 0.1161 0.0997 0.0942 0.0055 0.0087 -0.0070 113 THR A O 966 C CB . THR A 113 ? 0.1249 0.1326 0.1023 0.0083 -0.0091 -0.0043 113 THR A CB 967 O OG1 . THR A 113 ? 0.1165 0.1288 0.0894 0.0058 -0.0145 -0.0070 113 THR A OG1 968 C CG2 . THR A 113 ? 0.1160 0.1273 0.1054 0.0085 -0.0058 -0.0013 113 THR A CG2 969 N N . PRO A 114 ? 0.1242 0.1109 0.0886 -0.0019 0.0000 -0.0167 114 PRO A N 970 C CA . PRO A 114 ? 0.1267 0.1226 0.0826 -0.0038 -0.0079 -0.0195 114 PRO A CA 971 C C . PRO A 114 ? 0.1327 0.1270 0.0762 -0.0010 -0.0086 -0.0192 114 PRO A C 972 O O . PRO A 114 ? 0.1426 0.1267 0.0832 0.0007 -0.0027 -0.0189 114 PRO A O 973 C CB . PRO A 114 ? 0.1469 0.1424 0.1007 -0.0123 -0.0068 -0.0281 114 PRO A CB 974 C CG . PRO A 114 ? 0.1590 0.1387 0.1151 -0.0144 0.0037 -0.0311 114 PRO A CG 975 C CD . PRO A 114 ? 0.1502 0.1270 0.1170 -0.0071 0.0075 -0.0218 114 PRO A CD 976 N N . PRO A 115 ? 0.1335 0.1388 0.0706 0.0005 -0.0149 -0.0178 115 PRO A N 977 C CA . PRO A 115 ? 0.1595 0.1649 0.0854 0.0046 -0.0148 -0.0154 115 PRO A CA 978 C C . PRO A 115 ? 0.1881 0.1933 0.1011 0.0001 -0.0134 -0.0222 115 PRO A C 979 O O . PRO A 115 ? 0.1717 0.1906 0.0754 -0.0005 -0.0181 -0.0230 115 PRO A O 980 C CB . PRO A 115 ? 0.1405 0.1599 0.0662 0.0088 -0.0209 -0.0098 115 PRO A CB 981 C CG . PRO A 115 ? 0.1369 0.1668 0.0683 0.0035 -0.0259 -0.0133 115 PRO A CG 982 C CD . PRO A 115 ? 0.1277 0.1468 0.0693 0.0000 -0.0217 -0.0163 115 PRO A CD 983 N N . VAL A 116 ? 0.1620 0.1534 0.0746 -0.0029 -0.0063 -0.0269 116 VAL A N 984 C CA . VAL A 116 ? 0.1788 0.1666 0.0788 -0.0074 -0.0027 -0.0345 116 VAL A CA 985 C C . VAL A 116 ? 0.2010 0.1720 0.1014 -0.0042 0.0061 -0.0328 116 VAL A C 986 O O . VAL A 116 ? 0.2057 0.1670 0.1172 -0.0040 0.0112 -0.0314 116 VAL A O 987 C CB . VAL A 116 ? 0.2079 0.1946 0.1089 -0.0176 -0.0006 -0.0457 116 VAL A CB 988 C CG1 . VAL A 116 ? 0.2594 0.2430 0.1459 -0.0234 0.0040 -0.0558 116 VAL A CG1 989 C CG2 . VAL A 116 ? 0.2230 0.2276 0.1268 -0.0218 -0.0090 -0.0476 116 VAL A CG2 990 N N . VAL A 117 ? 0.2060 0.1756 0.0948 -0.0011 0.0081 -0.0317 117 VAL A N 991 C CA A VAL A 117 ? 0.1924 0.1475 0.0811 0.0022 0.0165 -0.0296 117 VAL A CA 992 C CA B VAL A 117 ? 0.2400 0.1951 0.1287 0.0022 0.0166 -0.0295 117 VAL A CA 993 C C . VAL A 117 ? 0.2794 0.2335 0.1515 0.0017 0.0197 -0.0337 117 VAL A C 994 O O . VAL A 117 ? 0.2821 0.2498 0.1434 0.0022 0.0143 -0.0338 117 VAL A O 995 C CB A VAL A 117 ? 0.2233 0.1778 0.1201 0.0096 0.0163 -0.0194 117 VAL A CB 996 C CB B VAL A 117 ? 0.2699 0.2241 0.1664 0.0097 0.0166 -0.0193 117 VAL A CB 997 C CG1 A VAL A 117 ? 0.1816 0.1440 0.0700 0.0147 0.0130 -0.0140 117 VAL A CG1 998 C CG1 B VAL A 117 ? 0.3459 0.2887 0.2415 0.0128 0.0249 -0.0169 117 VAL A CG1 999 C CG2 A VAL A 117 ? 0.3394 0.2820 0.2408 0.0119 0.0248 -0.0170 117 VAL A CG2 1000 C CG2 B VAL A 117 ? 0.1637 0.1199 0.0759 0.0100 0.0147 -0.0161 117 VAL A CG2 1001 N N . ASN A 118 ? 0.2438 0.1835 0.1140 0.0012 0.0289 -0.0366 118 ASN A N 1002 C CA . ASN A 118 ? 0.2340 0.1716 0.0888 0.0023 0.0331 -0.0390 118 ASN A CA 1003 C C . ASN A 118 ? 0.2630 0.1927 0.1221 0.0103 0.0381 -0.0292 118 ASN A C 1004 O O . ASN A 118 ? 0.2948 0.2145 0.1659 0.0117 0.0435 -0.0262 118 ASN A O 1005 C CB . ASN A 118 ? 0.2927 0.2189 0.1414 -0.0046 0.0418 -0.0506 118 ASN A CB 1006 C CG . ASN A 118 ? 0.3572 0.2925 0.2030 -0.0144 0.0379 -0.0622 118 ASN A CG 1007 O OD1 . ASN A 118 ? 0.4152 0.3700 0.2549 -0.0157 0.0284 -0.0629 118 ASN A OD1 1008 N ND2 . ASN A 118 ? 0.4373 0.3606 0.2916 -0.0206 0.0453 -0.0696 118 ASN A ND2 1009 N N . VAL A 119 ? 0.2677 0.2034 0.1180 0.0156 0.0367 -0.0234 119 VAL A N 1010 C CA . VAL A 119 ? 0.2274 0.1558 0.0822 0.0222 0.0422 -0.0147 119 VAL A CA 1011 C C . VAL A 119 ? 0.2590 0.1850 0.0986 0.0250 0.0478 -0.0148 119 VAL A C 1012 O O . VAL A 119 ? 0.3037 0.2424 0.1319 0.0255 0.0438 -0.0152 119 VAL A O 1013 C CB . VAL A 119 ? 0.2365 0.1717 0.0985 0.0274 0.0379 -0.0054 119 VAL A CB 1014 C CG1 . VAL A 119 ? 0.2238 0.1511 0.0914 0.0323 0.0449 0.0018 119 VAL A CG1 1015 C CG2 . VAL A 119 ? 0.2485 0.1870 0.1247 0.0248 0.0326 -0.0057 119 VAL A CG2 1016 N N . THR A 120 ? 0.2465 0.1607 0.0901 0.0266 0.0562 -0.0133 120 THR A N 1017 C CA . THR A 120 ? 0.2634 0.1771 0.0993 0.0289 0.0606 -0.0122 120 THR A CA 1018 C C . THR A 120 ? 0.2720 0.1787 0.1166 0.0348 0.0664 -0.0025 120 THR A C 1019 O O . THR A 120 ? 0.2606 0.1602 0.1179 0.0348 0.0701 -0.0004 120 THR A O 1020 C CB . THR A 120 ? 0.3023 0.2087 0.1352 0.0238 0.0661 -0.0213 120 THR A CB 1021 O OG1 . THR A 120 ? 0.3241 0.2361 0.1522 0.0165 0.0619 -0.0320 120 THR A OG1 1022 C CG2 . THR A 120 ? 0.3351 0.2441 0.1577 0.0259 0.0696 -0.0212 120 THR A CG2 1023 N N . TRP A 121 ? 0.2824 0.1935 0.1215 0.0396 0.0673 0.0035 121 TRP A N 1024 C CA . TRP A 121 ? 0.2594 0.1635 0.1063 0.0442 0.0739 0.0113 121 TRP A CA 1025 C C . TRP A 121 ? 0.2713 0.1692 0.1138 0.0439 0.0799 0.0087 121 TRP A C 1026 O O . TRP A 121 ? 0.2852 0.1882 0.1146 0.0427 0.0791 0.0038 121 TRP A O 1027 C CB . TRP A 121 ? 0.2635 0.1736 0.1079 0.0502 0.0738 0.0198 121 TRP A CB 1028 C CG . TRP A 121 ? 0.2759 0.1886 0.1285 0.0520 0.0713 0.0249 121 TRP A CG 1029 C CD1 . TRP A 121 ? 0.2534 0.1765 0.1013 0.0540 0.0655 0.0271 121 TRP A CD1 1030 C CD2 . TRP A 121 ? 0.2597 0.1656 0.1274 0.0516 0.0753 0.0283 121 TRP A CD2 1031 N NE1 . TRP A 121 ? 0.2683 0.1889 0.1272 0.0554 0.0664 0.0319 121 TRP A NE1 1032 C CE2 . TRP A 121 ? 0.2367 0.1469 0.1074 0.0532 0.0725 0.0318 121 TRP A CE2 1033 C CE3 . TRP A 121 ? 0.2732 0.1722 0.1530 0.0495 0.0810 0.0284 121 TRP A CE3 1034 C CZ2 . TRP A 121 ? 0.2345 0.1404 0.1190 0.0518 0.0761 0.0341 121 TRP A CZ2 1035 C CZ3 . TRP A 121 ? 0.2610 0.1594 0.1549 0.0476 0.0834 0.0305 121 TRP A CZ3 1036 C CH2 . TRP A 121 ? 0.3064 0.2073 0.2022 0.0483 0.0815 0.0326 121 TRP A CH2 1037 N N . LEU A 122 ? 0.2673 0.1563 0.1211 0.0448 0.0859 0.0119 122 LEU A N 1038 C CA . LEU A 122 ? 0.2781 0.1602 0.1293 0.0454 0.0925 0.0109 122 LEU A CA 1039 C C . LEU A 122 ? 0.2871 0.1666 0.1449 0.0504 0.0976 0.0196 122 LEU A C 1040 O O . LEU A 122 ? 0.2935 0.1732 0.1649 0.0511 0.0984 0.0247 122 LEU A O 1041 C CB . LEU A 122 ? 0.2742 0.1489 0.1348 0.0424 0.0962 0.0080 122 LEU A CB 1042 C CG . LEU A 122 ? 0.3113 0.1859 0.1688 0.0369 0.0933 -0.0008 122 LEU A CG 1043 C CD1 . LEU A 122 ? 0.2971 0.1654 0.1685 0.0361 0.0980 0.0008 122 LEU A CD1 1044 C CD2 . LEU A 122 ? 0.3379 0.2119 0.1803 0.0335 0.0944 -0.0100 122 LEU A CD2 1045 N N . ARG A 123 ? 0.2929 0.1713 0.1413 0.0532 0.1012 0.0204 123 ARG A N 1046 C CA . ARG A 123 ? 0.2955 0.1702 0.1501 0.0580 0.1072 0.0282 123 ARG A CA 1047 C C . ARG A 123 ? 0.3404 0.2076 0.1933 0.0581 0.1135 0.0264 123 ARG A C 1048 O O . ARG A 123 ? 0.3206 0.1879 0.1596 0.0572 0.1145 0.0209 123 ARG A O 1049 C CB . ARG A 123 ? 0.3055 0.1860 0.1513 0.0630 0.1071 0.0330 123 ARG A CB 1050 C CG . ARG A 123 ? 0.3279 0.2036 0.1800 0.0682 0.1143 0.0406 123 ARG A CG 1051 C CD . ARG A 123 ? 0.3810 0.2628 0.2234 0.0742 0.1154 0.0461 123 ARG A CD 1052 N NE . ARG A 123 ? 0.5636 0.4512 0.4098 0.0768 0.1125 0.0509 123 ARG A NE 1053 C CZ . ARG A 123 ? 0.7983 0.6884 0.6462 0.0836 0.1163 0.0595 123 ARG A CZ 1054 N NH1 . ARG A 123 ? 0.8470 0.7351 0.6928 0.0885 0.1225 0.0641 123 ARG A NH1 1055 N NH2 . ARG A 123 ? 0.6227 0.5169 0.4755 0.0862 0.1147 0.0640 123 ARG A NH2 1056 N N . ASN A 124 ? 0.3042 0.1667 0.1716 0.0588 0.1180 0.0307 124 ASN A N 1057 C CA . ASN A 124 ? 0.3286 0.1836 0.1968 0.0595 0.1246 0.0305 124 ASN A CA 1058 C C . ASN A 124 ? 0.3468 0.1973 0.2074 0.0553 0.1249 0.0222 124 ASN A C 1059 O O . ASN A 124 ? 0.3466 0.1906 0.1989 0.0553 0.1304 0.0188 124 ASN A O 1060 C CB . ASN A 124 ? 0.3466 0.1990 0.2068 0.0639 0.1297 0.0335 124 ASN A CB 1061 C CG . ASN A 124 ? 0.3810 0.2364 0.2508 0.0679 0.1310 0.0415 124 ASN A CG 1062 O OD1 . ASN A 124 ? 0.3524 0.2102 0.2387 0.0669 0.1311 0.0449 124 ASN A OD1 1063 N ND2 . ASN A 124 ? 0.4087 0.2657 0.2693 0.0719 0.1325 0.0443 124 ASN A ND2 1064 N N . GLY A 125 ? 0.3044 0.1580 0.1684 0.0515 0.1198 0.0186 125 GLY A N 1065 C CA . GLY A 125 ? 0.3515 0.2003 0.2114 0.0469 0.1208 0.0106 125 GLY A CA 1066 C C . GLY A 125 ? 0.3374 0.1894 0.1801 0.0429 0.1175 0.0001 125 GLY A C 1067 O O . GLY A 125 ? 0.3358 0.1835 0.1753 0.0378 0.1192 -0.0085 125 GLY A O 1068 N N . LYS A 126 ? 0.3270 0.1881 0.1596 0.0449 0.1132 0.0009 126 LYS A N 1069 C CA . LYS A 126 ? 0.3399 0.2107 0.1558 0.0414 0.1092 -0.0083 126 LYS A CA 1070 C C . LYS A 126 ? 0.3297 0.2134 0.1433 0.0413 0.1000 -0.0070 126 LYS A C 1071 O O . LYS A 126 ? 0.3201 0.2058 0.1402 0.0462 0.0982 0.0026 126 LYS A O 1072 C CB . LYS A 126 ? 0.3561 0.2311 0.1604 0.0449 0.1127 -0.0071 126 LYS A CB 1073 C CG . LYS A 126 ? 0.3682 0.2304 0.1738 0.0459 0.1224 -0.0075 126 LYS A CG 1074 C CD . LYS A 126 ? 0.4420 0.3105 0.2342 0.0488 0.1254 -0.0077 126 LYS A CD 1075 C CE . LYS A 126 ? 0.5698 0.4251 0.3633 0.0504 0.1355 -0.0075 126 LYS A CE 1076 N NZ . LYS A 126 ? 0.6025 0.4652 0.3816 0.0529 0.1386 -0.0089 126 LYS A NZ 1077 N N . PRO A 127 ? 0.3341 0.2270 0.1392 0.0354 0.0947 -0.0169 127 PRO A N 1078 C CA . PRO A 127 ? 0.3255 0.2321 0.1280 0.0352 0.0857 -0.0154 127 PRO A CA 1079 C C . PRO A 127 ? 0.3307 0.2502 0.1254 0.0410 0.0836 -0.0073 127 PRO A C 1080 O O . PRO A 127 ? 0.3684 0.2949 0.1521 0.0415 0.0862 -0.0094 127 PRO A O 1081 C CB . PRO A 127 ? 0.3953 0.3113 0.1889 0.0270 0.0817 -0.0292 127 PRO A CB 1082 C CG . PRO A 127 ? 0.4508 0.3512 0.2486 0.0228 0.0893 -0.0371 127 PRO A CG 1083 C CD . PRO A 127 ? 0.4394 0.3300 0.2385 0.0283 0.0973 -0.0303 127 PRO A CD 1084 N N . VAL A 128 ? 0.3330 0.2557 0.1344 0.0457 0.0798 0.0022 128 VAL A N 1085 C CA . VAL A 128 ? 0.3492 0.2835 0.1460 0.0522 0.0787 0.0118 128 VAL A CA 1086 C C . VAL A 128 ? 0.4015 0.3496 0.1979 0.0527 0.0707 0.0146 128 VAL A C 1087 O O . VAL A 128 ? 0.4724 0.4160 0.2774 0.0508 0.0675 0.0137 128 VAL A O 1088 C CB . VAL A 128 ? 0.4527 0.3755 0.2611 0.0598 0.0852 0.0235 128 VAL A CB 1089 C CG1 . VAL A 128 ? 0.5637 0.4776 0.3700 0.0606 0.0927 0.0226 128 VAL A CG1 1090 C CG2 . VAL A 128 ? 0.3830 0.2944 0.2075 0.0589 0.0856 0.0256 128 VAL A CG2 1091 N N . THR A 129 ? 0.4189 0.3850 0.2057 0.0553 0.0676 0.0184 129 THR A N 1092 C CA . THR A 129 ? 0.4423 0.4242 0.2288 0.0560 0.0598 0.0217 129 THR A CA 1093 C C . THR A 129 ? 0.5660 0.5579 0.3549 0.0665 0.0610 0.0362 129 THR A C 1094 O O . THR A 129 ? 0.4933 0.4970 0.2859 0.0699 0.0562 0.0420 129 THR A O 1095 C CB . THR A 129 ? 0.5079 0.5075 0.2806 0.0466 0.0531 0.0102 129 THR A CB 1096 O OG1 . THR A 129 ? 0.5428 0.5535 0.3017 0.0465 0.0551 0.0093 129 THR A OG1 1097 C CG2 . THR A 129 ? 0.5127 0.5024 0.2849 0.0364 0.0536 -0.0049 129 THR A CG2 1098 N N . THR A 130 ? 0.6031 0.5902 0.3911 0.0725 0.0681 0.0423 130 THR A N 1099 C CA . THR A 130 ? 0.5307 0.5266 0.3220 0.0835 0.0711 0.0564 130 THR A CA 1100 C C . THR A 130 ? 0.4917 0.4769 0.3005 0.0900 0.0746 0.0658 130 THR A C 1101 O O . THR A 130 ? 0.5134 0.4788 0.3328 0.0899 0.0807 0.0662 130 THR A O 1102 C CB . THR A 130 ? 0.5638 0.5558 0.3513 0.0887 0.0789 0.0610 130 THR A CB 1103 O OG1 . THR A 130 ? 0.5564 0.5613 0.3262 0.0827 0.0761 0.0521 130 THR A OG1 1104 C CG2 . THR A 130 ? 0.5352 0.5347 0.3292 0.1016 0.0837 0.0766 130 THR A CG2 1105 N N . GLY A 131 ? 0.4140 0.4133 0.2263 0.0950 0.0711 0.0727 131 GLY A N 1106 C CA . GLY A 131 ? 0.4185 0.4088 0.2471 0.1017 0.0762 0.0817 131 GLY A CA 1107 C C . GLY A 131 ? 0.4235 0.4040 0.2594 0.0952 0.0726 0.0755 131 GLY A C 1108 O O . GLY A 131 ? 0.4350 0.4071 0.2842 0.0991 0.0773 0.0811 131 GLY A O 1109 N N . VAL A 132 ? 0.3177 0.2993 0.1455 0.0852 0.0651 0.0636 132 VAL A N 1110 C CA . VAL A 132 ? 0.3342 0.3072 0.1688 0.0792 0.0617 0.0576 132 VAL A CA 1111 C C . VAL A 132 ? 0.3052 0.2918 0.1434 0.0813 0.0557 0.0612 132 VAL A C 1112 O O . VAL A 132 ? 0.3703 0.3770 0.2029 0.0844 0.0514 0.0648 132 VAL A O 1113 C CB . VAL A 132 ? 0.3430 0.3128 0.1696 0.0688 0.0567 0.0440 132 VAL A CB 1114 C CG1 . VAL A 132 ? 0.3420 0.2974 0.1674 0.0672 0.0636 0.0408 132 VAL A CG1 1115 C CG2 . VAL A 132 ? 0.4217 0.4115 0.2349 0.0638 0.0485 0.0373 132 VAL A CG2 1116 N N . SER A 133 ? 0.2715 0.2482 0.1196 0.0795 0.0558 0.0603 133 SER A N 1117 C CA . SER A 133 ? 0.2774 0.2656 0.1300 0.0808 0.0502 0.0628 133 SER A CA 1118 C C . SER A 133 ? 0.2509 0.2289 0.1083 0.0740 0.0471 0.0555 133 SER A C 1119 O O . SER A 133 ? 0.2489 0.2114 0.1078 0.0693 0.0503 0.0499 133 SER A O 1120 C CB . SER A 133 ? 0.2879 0.2759 0.1517 0.0913 0.0581 0.0753 133 SER A CB 1121 O OG . SER A 133 ? 0.2890 0.2551 0.1639 0.0919 0.0682 0.0768 133 SER A OG 1122 N N . GLU A 134 ? 0.2447 0.2330 0.1055 0.0736 0.0408 0.0558 134 GLU A N 1123 C CA . GLU A 134 ? 0.2311 0.2124 0.0956 0.0673 0.0368 0.0489 134 GLU A CA 1124 C C . GLU A 134 ? 0.2258 0.2165 0.0980 0.0701 0.0332 0.0533 134 GLU A C 1125 O O . GLU A 134 ? 0.2549 0.2617 0.1275 0.0752 0.0314 0.0596 134 GLU A O 1126 C CB . GLU A 134 ? 0.2445 0.2313 0.0996 0.0584 0.0289 0.0371 134 GLU A CB 1127 C CG . GLU A 134 ? 0.2571 0.2664 0.1068 0.0557 0.0197 0.0346 134 GLU A CG 1128 C CD . GLU A 134 ? 0.3630 0.3754 0.2031 0.0457 0.0149 0.0215 134 GLU A CD 1129 O OE1 . GLU A 134 ? 0.3573 0.3668 0.1885 0.0440 0.0183 0.0180 134 GLU A OE1 1130 O OE2 . GLU A 134 ? 0.3811 0.3978 0.2231 0.0394 0.0087 0.0143 134 GLU A OE2 1131 N N . THR A 135 ? 0.2145 0.1960 0.0930 0.0669 0.0327 0.0501 135 THR A N 1132 C CA . THR A 135 ? 0.2087 0.1987 0.0945 0.0687 0.0288 0.0529 135 THR A CA 1133 C C . THR A 135 ? 0.2081 0.2117 0.0902 0.0615 0.0170 0.0445 135 THR A C 1134 O O . THR A 135 ? 0.2192 0.2213 0.0939 0.0548 0.0134 0.0355 135 THR A O 1135 C CB . THR A 135 ? 0.2008 0.1745 0.0988 0.0678 0.0347 0.0526 135 THR A CB 1136 O OG1 . THR A 135 ? 0.1878 0.1566 0.0910 0.0575 0.0295 0.0404 135 THR A OG1 1137 C CG2 . THR A 135 ? 0.2092 0.1663 0.1126 0.0720 0.0482 0.0583 135 THR A CG2 1138 N N . VAL A 136 ? 0.1999 0.2160 0.0884 0.0628 0.0122 0.0471 136 VAL A N 1139 C CA . VAL A 136 ? 0.1885 0.2146 0.0775 0.0551 0.0023 0.0389 136 VAL A CA 1140 C C . VAL A 136 ? 0.2071 0.2188 0.1033 0.0505 0.0026 0.0327 136 VAL A C 1141 O O . VAL A 136 ? 0.1979 0.1933 0.1008 0.0509 0.0098 0.0329 136 VAL A O 1142 C CB . VAL A 136 ? 0.2117 0.2553 0.1079 0.0573 -0.0020 0.0434 136 VAL A CB 1143 C CG1 . VAL A 136 ? 0.2398 0.3007 0.1316 0.0607 -0.0024 0.0484 136 VAL A CG1 1144 C CG2 . VAL A 136 ? 0.2178 0.2535 0.1245 0.0646 0.0045 0.0513 136 VAL A CG2 1145 N N . PHE A 137 ? 0.1872 0.2060 0.0870 0.0439 -0.0051 0.0258 137 PHE A N 1146 C CA . PHE A 137 ? 0.1829 0.1918 0.0946 0.0385 -0.0052 0.0198 137 PHE A CA 1147 C C . PHE A 137 ? 0.2068 0.2143 0.1285 0.0430 -0.0027 0.0251 137 PHE A C 1148 O O . PHE A 137 ? 0.2490 0.2680 0.1709 0.0475 -0.0053 0.0308 137 PHE A O 1149 C CB . PHE A 137 ? 0.1718 0.1881 0.0848 0.0306 -0.0125 0.0117 137 PHE A CB 1150 C CG . PHE A 137 ? 0.1580 0.1717 0.0624 0.0249 -0.0124 0.0043 137 PHE A CG 1151 C CD1 . PHE A 137 ? 0.2238 0.2507 0.1164 0.0233 -0.0160 0.0023 137 PHE A CD1 1152 C CD2 . PHE A 137 ? 0.1523 0.1520 0.0607 0.0212 -0.0080 -0.0005 137 PHE A CD2 1153 C CE1 . PHE A 137 ? 0.2375 0.2607 0.1218 0.0171 -0.0145 -0.0063 137 PHE A CE1 1154 C CE2 . PHE A 137 ? 0.2003 0.1952 0.1013 0.0165 -0.0059 -0.0070 137 PHE A CE2 1155 C CZ . PHE A 137 ? 0.2222 0.2275 0.1109 0.0140 -0.0088 -0.0108 137 PHE A CZ 1156 N N . LEU A 138 ? 0.1464 0.1409 0.0766 0.0417 0.0032 0.0231 138 LEU A N 1157 C CA . LEU A 138 ? 0.1785 0.1692 0.1177 0.0451 0.0081 0.0264 138 LEU A CA 1158 C C . LEU A 138 ? 0.1293 0.1220 0.0782 0.0392 0.0045 0.0196 138 LEU A C 1159 O O . LEU A 138 ? 0.1441 0.1353 0.0954 0.0333 0.0027 0.0134 138 LEU A O 1160 C CB . LEU A 138 ? 0.1893 0.1652 0.1311 0.0473 0.0192 0.0283 138 LEU A CB 1161 C CG . LEU A 138 ? 0.1939 0.1674 0.1264 0.0539 0.0242 0.0362 138 LEU A CG 1162 C CD1 . LEU A 138 ? 0.2264 0.1841 0.1634 0.0537 0.0354 0.0361 138 LEU A CD1 1163 C CD2 . LEU A 138 ? 0.2139 0.1956 0.1436 0.0636 0.0259 0.0474 138 LEU A CD2 1164 N N . PRO A 139 ? 0.1269 0.1241 0.0815 0.0417 0.0042 0.0218 139 PRO A N 1165 C CA . PRO A 139 ? 0.1218 0.1239 0.0846 0.0367 0.0002 0.0160 139 PRO A CA 1166 C C . PRO A 139 ? 0.1616 0.1566 0.1322 0.0326 0.0063 0.0102 139 PRO A C 1167 O O . PRO A 139 ? 0.1914 0.1763 0.1639 0.0343 0.0152 0.0108 139 PRO A O 1168 C CB . PRO A 139 ? 0.1624 0.1715 0.1280 0.0417 -0.0007 0.0211 139 PRO A CB 1169 C CG . PRO A 139 ? 0.1946 0.1962 0.1577 0.0495 0.0080 0.0289 139 PRO A CG 1170 C CD . PRO A 139 ? 0.1612 0.1604 0.1151 0.0502 0.0081 0.0308 139 PRO A CD 1171 N N . ARG A 140 ? 0.1257 0.1275 0.1014 0.0271 0.0021 0.0046 140 ARG A N 1172 C CA . ARG A 140 ? 0.1279 0.1306 0.1115 0.0224 0.0062 -0.0016 140 ARG A CA 1173 C C . ARG A 140 ? 0.1174 0.1296 0.1070 0.0216 0.0037 -0.0037 140 ARG A C 1174 O O . ARG A 140 ? 0.1178 0.1371 0.1067 0.0237 -0.0027 -0.0005 140 ARG A O 1175 C CB . ARG A 140 ? 0.0904 0.0981 0.0757 0.0179 0.0041 -0.0046 140 ARG A CB 1176 C CG . ARG A 140 ? 0.1044 0.1028 0.0852 0.0179 0.0083 -0.0036 140 ARG A CG 1177 C CD . ARG A 140 ? 0.0980 0.1024 0.0808 0.0150 0.0063 -0.0047 140 ARG A CD 1178 N NE . ARG A 140 ? 0.1099 0.1284 0.1020 0.0113 0.0055 -0.0081 140 ARG A NE 1179 C CZ . ARG A 140 ? 0.1423 0.1660 0.1400 0.0071 0.0101 -0.0124 140 ARG A CZ 1180 N NH1 . ARG A 140 ? 0.1555 0.1688 0.1517 0.0061 0.0164 -0.0136 140 ARG A NH1 1181 N NH2 . ARG A 140 ? 0.1857 0.2272 0.1911 0.0037 0.0086 -0.0156 140 ARG A NH2 1182 N N . GLU A 141 ? 0.1041 0.1176 0.0998 0.0178 0.0090 -0.0100 141 GLU A N 1183 C CA . GLU A 141 ? 0.1067 0.1298 0.1074 0.0168 0.0076 -0.0130 141 GLU A CA 1184 C C . GLU A 141 ? 0.1076 0.1472 0.1111 0.0150 -0.0005 -0.0129 141 GLU A C 1185 O O . GLU A 141 ? 0.1227 0.1716 0.1294 0.0157 -0.0033 -0.0129 141 GLU A O 1186 C CB . GLU A 141 ? 0.1558 0.1773 0.1618 0.0116 0.0164 -0.0220 141 GLU A CB 1187 C CG . GLU A 141 ? 0.2444 0.2471 0.2498 0.0143 0.0273 -0.0213 141 GLU A CG 1188 C CD . GLU A 141 ? 0.4375 0.4368 0.4490 0.0075 0.0379 -0.0324 141 GLU A CD 1189 O OE1 . GLU A 141 ? 0.5133 0.5242 0.5282 0.0038 0.0367 -0.0389 141 GLU A OE1 1190 O OE2 . GLU A 141 ? 0.5545 0.5399 0.5676 0.0053 0.0482 -0.0351 141 GLU A OE2 1191 N N . ASP A 142 ? 0.1029 0.1457 0.1058 0.0133 -0.0031 -0.0117 142 ASP A N 1192 C CA . ASP A 142 ? 0.0868 0.1431 0.0932 0.0131 -0.0087 -0.0092 142 ASP A CA 1193 C C . ASP A 142 ? 0.0795 0.1307 0.0821 0.0161 -0.0133 -0.0036 142 ASP A C 1194 O O . ASP A 142 ? 0.1039 0.1620 0.1097 0.0161 -0.0160 -0.0009 142 ASP A O 1195 C CB . ASP A 142 ? 0.0851 0.1508 0.0952 0.0102 -0.0073 -0.0103 142 ASP A CB 1196 C CG . ASP A 142 ? 0.1250 0.1786 0.1307 0.0102 -0.0046 -0.0090 142 ASP A CG 1197 O OD1 . ASP A 142 ? 0.0999 0.1390 0.0989 0.0126 -0.0046 -0.0070 142 ASP A OD1 1198 O OD2 . ASP A 142 ? 0.1268 0.1880 0.1361 0.0082 -0.0024 -0.0095 142 ASP A OD2 1199 N N . HIS A 143 ? 0.0733 0.1136 0.0695 0.0185 -0.0131 -0.0019 143 HIS A N 1200 C CA . HIS A 143 ? 0.0692 0.1081 0.0610 0.0201 -0.0176 0.0016 143 HIS A CA 1201 C C . HIS A 143 ? 0.0718 0.1057 0.0597 0.0183 -0.0179 0.0016 143 HIS A C 1202 O O . HIS A 143 ? 0.0980 0.1323 0.0830 0.0174 -0.0211 0.0022 143 HIS A O 1203 C CB . HIS A 143 ? 0.0831 0.1327 0.0803 0.0205 -0.0221 0.0032 143 HIS A CB 1204 C CG . HIS A 143 ? 0.0624 0.1168 0.0638 0.0222 -0.0205 0.0024 143 HIS A CG 1205 N ND1 . HIS A 143 ? 0.1156 0.1637 0.1142 0.0255 -0.0171 0.0034 143 HIS A ND1 1206 C CD2 . HIS A 143 ? 0.1023 0.1670 0.1102 0.0211 -0.0203 0.0005 143 HIS A CD2 1207 C CE1 . HIS A 143 ? 0.0853 0.1374 0.0887 0.0258 -0.0144 0.0010 143 HIS A CE1 1208 N NE2 . HIS A 143 ? 0.0800 0.1433 0.0884 0.0228 -0.0169 -0.0012 143 HIS A NE2 1209 N N . LEU A 144 ? 0.0727 0.1021 0.0605 0.0172 -0.0136 0.0001 144 LEU A N 1210 C CA . LEU A 144 ? 0.1034 0.1245 0.0856 0.0164 -0.0117 0.0000 144 LEU A CA 1211 C C . LEU A 144 ? 0.0926 0.1047 0.0661 0.0186 -0.0097 0.0007 144 LEU A C 1212 O O . LEU A 144 ? 0.1007 0.1133 0.0732 0.0213 -0.0099 0.0024 144 LEU A O 1213 C CB . LEU A 144 ? 0.0773 0.0998 0.0644 0.0152 -0.0075 -0.0003 144 LEU A CB 1214 C CG . LEU A 144 ? 0.0766 0.1113 0.0731 0.0149 -0.0082 0.0015 144 LEU A CG 1215 C CD1 . LEU A 144 ? 0.1134 0.1544 0.1151 0.0146 -0.0040 0.0025 144 LEU A CD1 1216 C CD2 . LEU A 144 ? 0.1468 0.1783 0.1435 0.0147 -0.0089 0.0033 144 LEU A CD2 1217 N N . PHE A 145 ? 0.1379 0.0978 0.0358 0.0098 -0.0028 0.0062 145 PHE A N 1218 C CA . PHE A 145 ? 0.1366 0.1009 0.0370 0.0135 -0.0013 0.0062 145 PHE A CA 1219 C C . PHE A 145 ? 0.1411 0.0997 0.0420 0.0131 -0.0024 0.0053 145 PHE A C 1220 O O . PHE A 145 ? 0.1537 0.1083 0.0545 0.0100 -0.0055 0.0049 145 PHE A O 1221 C CB . PHE A 145 ? 0.1318 0.1089 0.0351 0.0134 -0.0032 0.0053 145 PHE A CB 1222 C CG . PHE A 145 ? 0.1373 0.1223 0.0378 0.0139 -0.0023 0.0065 145 PHE A CG 1223 C CD1 . PHE A 145 ? 0.1557 0.1404 0.0534 0.0098 -0.0032 0.0049 145 PHE A CD1 1224 C CD2 . PHE A 145 ? 0.1723 0.1647 0.0721 0.0207 0.0005 0.0106 145 PHE A CD2 1225 C CE1 . PHE A 145 ? 0.1542 0.1469 0.0477 0.0102 -0.0012 0.0061 145 PHE A CE1 1226 C CE2 . PHE A 145 ? 0.1748 0.1796 0.0739 0.0237 0.0021 0.0134 145 PHE A CE2 1227 C CZ . PHE A 145 ? 0.1786 0.1845 0.0747 0.0175 0.0013 0.0105 145 PHE A CZ 1228 N N . ARG A 146 ? 0.1678 0.1256 0.0674 0.0171 0.0006 0.0062 146 ARG A N 1229 C CA A ARG A 146 ? 0.1923 0.1450 0.0907 0.0171 0.0009 0.0056 146 ARG A CA 1230 C CA B ARG A 146 ? 0.1941 0.1467 0.0924 0.0171 0.0009 0.0057 146 ARG A CA 1231 C CA C ARG A 146 ? 0.1954 0.1477 0.0935 0.0172 0.0011 0.0057 146 ARG A CA 1232 C C . ARG A 146 ? 0.1725 0.1319 0.0718 0.0217 0.0029 0.0071 146 ARG A C 1233 O O . ARG A 146 ? 0.1712 0.1391 0.0711 0.0253 0.0035 0.0094 146 ARG A O 1234 C CB A ARG A 146 ? 0.2198 0.1572 0.1091 0.0157 0.0042 0.0056 146 ARG A CB 1235 C CB B ARG A 146 ? 0.2184 0.1556 0.1075 0.0157 0.0043 0.0056 146 ARG A CB 1236 C CB C ARG A 146 ? 0.2249 0.1615 0.1135 0.0165 0.0051 0.0058 146 ARG A CB 1237 C CG A ARG A 146 ? 0.1619 0.0901 0.0442 0.0216 0.0117 0.0077 146 ARG A CG 1238 C CG B ARG A 146 ? 0.2503 0.1773 0.1317 0.0200 0.0113 0.0070 146 ARG A CG 1239 C CG C ARG A 146 ? 0.2509 0.1796 0.1330 0.0203 0.0111 0.0072 146 ARG A CG 1240 C CD A ARG A 146 ? 0.2890 0.1970 0.1579 0.0174 0.0168 0.0058 146 ARG A CD 1241 C CD B ARG A 146 ? 0.2162 0.1225 0.0835 0.0144 0.0156 0.0047 146 ARG A CD 1242 C CD C ARG A 146 ? 0.3147 0.2277 0.1875 0.0255 0.0199 0.0091 146 ARG A CD 1243 N NE A ARG A 146 ? 0.2921 0.1914 0.1554 0.0239 0.0249 0.0079 146 ARG A NE 1244 N NE B ARG A 146 ? 0.2854 0.1753 0.1425 0.0191 0.0258 0.0058 146 ARG A NE 1245 N NE C ARG A 146 ? 0.3151 0.2089 0.1759 0.0178 0.0229 0.0059 146 ARG A NE 1246 C CZ A ARG A 146 ? 0.3224 0.2120 0.1816 0.0335 0.0346 0.0121 146 ARG A CZ 1247 C CZ B ARG A 146 ? 0.3721 0.2424 0.2151 0.0124 0.0313 0.0026 146 ARG A CZ 1248 C CZ C ARG A 146 ? 0.3145 0.1875 0.1639 0.0190 0.0332 0.0064 146 ARG A CZ 1249 N NH1 A ARG A 146 ? 0.4255 0.3129 0.2850 0.0363 0.0368 0.0139 146 ARG A NH1 1250 N NH1 B ARG A 146 ? 0.4608 0.3129 0.2949 0.0180 0.0436 0.0042 146 ARG A NH1 1251 N NH1 C ARG A 146 ? 0.2699 0.1254 0.1066 0.0075 0.0362 0.0019 146 ARG A NH1 1252 N NH2 A ARG A 146 ? 0.2367 0.1185 0.0920 0.0416 0.0437 0.0157 146 ARG A NH2 1253 N NH2 B ARG A 146 ? 0.3652 0.2344 0.2027 0.0000 0.0252 -0.0017 146 ARG A NH2 1254 N NH2 C ARG A 146 ? 0.3235 0.1933 0.1741 0.0309 0.0414 0.0116 146 ARG A NH2 1255 N N . LYS A 147 ? 0.1495 0.1059 0.0474 0.0219 0.0037 0.0066 147 LYS A N 1256 C CA . LYS A 147 ? 0.1433 0.1068 0.0402 0.0252 0.0053 0.0080 147 LYS A CA 1257 C C . LYS A 147 ? 0.1888 0.1426 0.0809 0.0263 0.0093 0.0084 147 LYS A C 1258 O O . LYS A 147 ? 0.1801 0.1259 0.0708 0.0232 0.0091 0.0065 147 LYS A O 1259 C CB . LYS A 147 ? 0.1614 0.1365 0.0602 0.0211 0.0015 0.0044 147 LYS A CB 1260 C CG . LYS A 147 ? 0.2192 0.2055 0.1137 0.0214 0.0012 0.0053 147 LYS A CG 1261 C CD . LYS A 147 ? 0.2671 0.2601 0.1585 0.0141 -0.0012 -0.0012 147 LYS A CD 1262 C CE . LYS A 147 ? 0.3214 0.3249 0.2041 0.0112 -0.0040 -0.0008 147 LYS A CE 1263 N NZ . LYS A 147 ? 0.2718 0.2764 0.1474 0.0140 -0.0016 0.0020 147 LYS A NZ 1264 N N . PHE A 148 ? 0.1684 0.1231 0.0566 0.0310 0.0133 0.0118 148 PHE A N 1265 C CA . PHE A 148 ? 0.1857 0.1305 0.0685 0.0321 0.0192 0.0129 148 PHE A CA 1266 C C . PHE A 148 ? 0.2003 0.1546 0.0803 0.0330 0.0198 0.0131 148 PHE A C 1267 O O . PHE A 148 ? 0.2098 0.1762 0.0882 0.0348 0.0173 0.0155 148 PHE A O 1268 C CB . PHE A 148 ? 0.1819 0.1130 0.0589 0.0372 0.0271 0.0178 148 PHE A CB 1269 C CG . PHE A 148 ? 0.2066 0.1227 0.0802 0.0344 0.0294 0.0164 148 PHE A CG 1270 C CD1 . PHE A 148 ? 0.2140 0.1321 0.0891 0.0369 0.0278 0.0169 148 PHE A CD1 1271 C CD2 . PHE A 148 ? 0.2502 0.1492 0.1167 0.0280 0.0347 0.0145 148 PHE A CD2 1272 C CE1 . PHE A 148 ? 0.2173 0.1186 0.0852 0.0332 0.0314 0.0148 148 PHE A CE1 1273 C CE2 . PHE A 148 ? 0.2384 0.1219 0.0970 0.0219 0.0373 0.0119 148 PHE A CE2 1274 C CZ . PHE A 148 ? 0.2627 0.1462 0.1212 0.0247 0.0356 0.0117 148 PHE A CZ 1275 N N . HIS A 149 ? 0.1819 0.1304 0.0590 0.0312 0.0240 0.0108 149 HIS A N 1276 C CA . HIS A 149 ? 0.2103 0.1641 0.0814 0.0314 0.0272 0.0104 149 HIS A CA 1277 C C . HIS A 149 ? 0.1990 0.1398 0.0660 0.0339 0.0370 0.0140 149 HIS A C 1278 O O . HIS A 149 ? 0.2223 0.1509 0.0918 0.0324 0.0417 0.0141 149 HIS A O 1279 C CB . HIS A 149 ? 0.2006 0.1580 0.0717 0.0267 0.0268 0.0027 149 HIS A CB 1280 C CG . HIS A 149 ? 0.2017 0.1725 0.0731 0.0222 0.0197 -0.0015 149 HIS A CG 1281 N ND1 . HIS A 149 ? 0.2477 0.2286 0.1106 0.0168 0.0198 -0.0065 149 HIS A ND1 1282 C CD2 . HIS A 149 ? 0.2575 0.2331 0.1352 0.0206 0.0133 -0.0016 149 HIS A CD2 1283 C CE1 . HIS A 149 ? 0.2775 0.2680 0.1408 0.0110 0.0139 -0.0098 149 HIS A CE1 1284 N NE2 . HIS A 149 ? 0.2430 0.2305 0.1163 0.0141 0.0101 -0.0064 149 HIS A NE2 1285 N N . TYR A 150 ? 0.2126 0.1564 0.0720 0.0364 0.0406 0.0175 150 TYR A N 1286 C CA . TYR A 150 ? 0.2274 0.1578 0.0830 0.0392 0.0512 0.0222 150 TYR A CA 1287 C C . TYR A 150 ? 0.2489 0.1817 0.0971 0.0379 0.0571 0.0210 150 TYR A C 1288 O O . TYR A 150 ? 0.2599 0.2061 0.1002 0.0363 0.0525 0.0191 150 TYR A O 1289 C CB . TYR A 150 ? 0.2384 0.1652 0.0900 0.0462 0.0532 0.0305 150 TYR A CB 1290 C CG . TYR A 150 ? 0.2311 0.1527 0.0880 0.0484 0.0508 0.0316 150 TYR A CG 1291 C CD1 . TYR A 150 ? 0.2259 0.1608 0.0847 0.0524 0.0436 0.0337 150 TYR A CD1 1292 C CD2 . TYR A 150 ? 0.2465 0.1496 0.1052 0.0453 0.0572 0.0302 150 TYR A CD2 1293 C CE1 . TYR A 150 ? 0.2306 0.1593 0.0933 0.0551 0.0437 0.0345 150 TYR A CE1 1294 C CE2 . TYR A 150 ? 0.2321 0.1278 0.0917 0.0461 0.0566 0.0299 150 TYR A CE2 1295 C CZ . TYR A 150 ? 0.2542 0.1621 0.1161 0.0521 0.0504 0.0321 150 TYR A CZ 1296 O OH . TYR A 150 ? 0.2420 0.1408 0.1039 0.0536 0.0522 0.0318 150 TYR A OH 1297 N N . LEU A 151 ? 0.2494 0.1696 0.0997 0.0370 0.0683 0.0217 151 LEU A N 1298 C CA . LEU A 151 ? 0.2655 0.1852 0.1093 0.0362 0.0767 0.0208 151 LEU A CA 1299 C C . LEU A 151 ? 0.2817 0.1869 0.1252 0.0380 0.0891 0.0272 151 LEU A C 1300 O O . LEU A 151 ? 0.2825 0.1782 0.1377 0.0344 0.0976 0.0265 151 LEU A O 1301 C CB . LEU A 151 ? 0.2608 0.1806 0.1125 0.0320 0.0813 0.0127 151 LEU A CB 1302 C CG . LEU A 151 ? 0.3229 0.2393 0.1709 0.0308 0.0932 0.0105 151 LEU A CG 1303 C CD1 . LEU A 151 ? 0.3605 0.2866 0.1888 0.0303 0.0894 0.0093 151 LEU A CD1 1304 C CD2 . LEU A 151 ? 0.2772 0.1922 0.1387 0.0284 0.0998 0.0031 151 LEU A CD2 1305 N N . PRO A 152 ? 0.3222 0.2270 0.1534 0.0428 0.0909 0.0340 152 PRO A N 1306 C CA . PRO A 152 ? 0.3398 0.2293 0.1693 0.0444 0.1047 0.0399 152 PRO A CA 1307 C C . PRO A 152 ? 0.3282 0.2156 0.1604 0.0397 0.1149 0.0355 152 PRO A C 1308 O O . PRO A 152 ? 0.3522 0.2500 0.1775 0.0380 0.1122 0.0301 152 PRO A O 1309 C CB . PRO A 152 ? 0.3934 0.2874 0.2065 0.0515 0.1031 0.0483 152 PRO A CB 1310 C CG . PRO A 152 ? 0.4500 0.3588 0.2625 0.0541 0.0890 0.0487 152 PRO A CG 1311 C CD . PRO A 152 ? 0.3632 0.2820 0.1830 0.0468 0.0812 0.0380 152 PRO A CD 1312 N N . PHE A 153 ? 0.3349 0.2094 0.1784 0.0365 0.1279 0.0368 153 PHE A N 1313 C CA . PHE A 153 ? 0.3429 0.2168 0.1940 0.0326 0.1395 0.0333 153 PHE A CA 1314 C C . PHE A 153 ? 0.3624 0.2229 0.2219 0.0299 0.1550 0.0376 153 PHE A C 1315 O O . PHE A 153 ? 0.3626 0.2128 0.2255 0.0287 0.1573 0.0412 153 PHE A O 1316 C CB . PHE A 153 ? 0.3221 0.2045 0.1928 0.0281 0.1384 0.0260 153 PHE A CB 1317 C CG . PHE A 153 ? 0.3102 0.1915 0.2038 0.0220 0.1428 0.0266 153 PHE A CG 1318 C CD1 . PHE A 153 ? 0.3164 0.2026 0.2355 0.0165 0.1551 0.0256 153 PHE A CD1 1319 C CD2 . PHE A 153 ? 0.3045 0.1827 0.1963 0.0205 0.1349 0.0280 153 PHE A CD2 1320 C CE1 . PHE A 153 ? 0.3053 0.1980 0.2494 0.0075 0.1579 0.0263 153 PHE A CE1 1321 C CE2 . PHE A 153 ? 0.2930 0.1721 0.2040 0.0111 0.1389 0.0274 153 PHE A CE2 1322 C CZ . PHE A 153 ? 0.3197 0.2082 0.2580 0.0034 0.1496 0.0267 153 PHE A CZ 1323 N N . LEU A 154 ? 0.3953 0.2551 0.2581 0.0283 0.1667 0.0364 154 LEU A N 1324 C CA . LEU A 154 ? 0.4189 0.2685 0.2934 0.0244 0.1828 0.0395 154 LEU A CA 1325 C C . LEU A 154 ? 0.4217 0.2814 0.3281 0.0172 0.1899 0.0346 154 LEU A C 1326 O O . LEU A 154 ? 0.3973 0.2639 0.3096 0.0184 0.1943 0.0311 154 LEU A O 1327 C CB . LEU A 154 ? 0.4483 0.2912 0.3041 0.0285 0.1922 0.0431 154 LEU A CB 1328 C CG . LEU A 154 ? 0.5809 0.4095 0.4414 0.0263 0.2089 0.0484 154 LEU A CG 1329 C CD1 . LEU A 154 ? 0.5160 0.3309 0.3676 0.0291 0.2079 0.0550 154 LEU A CD1 1330 C CD2 . LEU A 154 ? 0.6793 0.5035 0.5218 0.0297 0.2190 0.0509 154 LEU A CD2 1331 N N . PRO A 155 ? 0.3840 0.2466 0.3128 0.0091 0.1914 0.0345 155 PRO A N 1332 C CA . PRO A 155 ? 0.3506 0.2322 0.3162 0.0014 0.1948 0.0317 155 PRO A CA 1333 C C . PRO A 155 ? 0.3653 0.2514 0.3490 0.0004 0.2099 0.0324 155 PRO A C 1334 O O . PRO A 155 ? 0.3893 0.2624 0.3653 -0.0008 0.2208 0.0352 155 PRO A O 1335 C CB . PRO A 155 ? 0.3968 0.2795 0.3773 -0.0107 0.1937 0.0320 155 PRO A CB 1336 C CG . PRO A 155 ? 0.4285 0.2922 0.3777 -0.0060 0.1858 0.0331 155 PRO A CG 1337 C CD . PRO A 155 ? 0.4852 0.3355 0.4068 0.0059 0.1890 0.0370 155 PRO A CD 1338 N N . SER A 156 ? 0.3533 0.2566 0.3616 0.0020 0.2113 0.0304 156 SER A N 1339 C CA . SER A 156 ? 0.3673 0.2766 0.3968 0.0023 0.2259 0.0313 156 SER A CA 1340 C C . SER A 156 ? 0.3761 0.3131 0.4495 0.0016 0.2245 0.0319 156 SER A C 1341 O O . SER A 156 ? 0.4242 0.3718 0.5041 0.0034 0.2127 0.0309 156 SER A O 1342 C CB . SER A 156 ? 0.6411 0.5339 0.6410 0.0111 0.2321 0.0291 156 SER A CB 1343 O OG . SER A 156 ? 0.6797 0.5753 0.6725 0.0168 0.2238 0.0244 156 SER A OG 1344 N N . THR A 157 ? 0.3762 0.3262 0.4812 -0.0004 0.2363 0.0349 157 THR A N 1345 C CA . THR A 157 ? 0.4747 0.4548 0.6259 0.0010 0.2349 0.0384 157 THR A CA 1346 C C . THR A 157 ? 0.4745 0.4461 0.6186 0.0140 0.2382 0.0361 157 THR A C 1347 O O . THR A 157 ? 0.4757 0.4673 0.6526 0.0190 0.2353 0.0398 157 THR A O 1348 C CB . THR A 157 ? 0.4831 0.4819 0.6716 -0.0047 0.2465 0.0433 157 THR A CB 1349 O OG1 . THR A 157 ? 0.5084 0.4835 0.6762 0.0005 0.2641 0.0416 157 THR A OG1 1350 C CG2 . THR A 157 ? 0.4175 0.4271 0.6165 -0.0212 0.2420 0.0443 157 THR A CG2 1351 N N . GLU A 158 ? 0.3654 0.3075 0.4659 0.0186 0.2434 0.0305 158 GLU A N 1352 C CA . GLU A 158 ? 0.4742 0.4037 0.5629 0.0270 0.2493 0.0262 158 GLU A CA 1353 C C . GLU A 158 ? 0.4288 0.3521 0.4964 0.0303 0.2357 0.0210 158 GLU A C 1354 O O . GLU A 158 ? 0.5024 0.4182 0.5676 0.0356 0.2396 0.0173 158 GLU A O 1355 C CB . GLU A 158 ? 0.5247 0.4297 0.5791 0.0276 0.2625 0.0224 158 GLU A CB 1356 C CG . GLU A 158 ? 0.6445 0.5530 0.7202 0.0255 0.2792 0.0271 158 GLU A CG 1357 C CD . GLU A 158 ? 0.7925 0.7229 0.9193 0.0289 0.2868 0.0323 158 GLU A CD 1358 O OE1 . GLU A 158 ? 0.8166 0.7736 0.9813 0.0241 0.2829 0.0387 158 GLU A OE1 1359 O OE2 . GLU A 158 ? 0.8817 0.8041 1.0112 0.0359 0.2965 0.0305 158 GLU A OE2 1360 N N . ASP A 159 ? 0.3506 0.2756 0.4029 0.0266 0.2211 0.0205 159 ASP A N 1361 C CA . ASP A 159 ? 0.4268 0.3460 0.4566 0.0290 0.2079 0.0154 159 ASP A CA 1362 C C . ASP A 159 ? 0.4629 0.4017 0.5194 0.0289 0.1961 0.0188 159 ASP A C 1363 O O . ASP A 159 ? 0.5094 0.4632 0.5846 0.0231 0.1919 0.0239 159 ASP A O 1364 C CB . ASP A 159 ? 0.4191 0.3238 0.4046 0.0264 0.1992 0.0124 159 ASP A CB 1365 C CG . ASP A 159 ? 0.5733 0.4620 0.5292 0.0268 0.2082 0.0095 159 ASP A CG 1366 O OD1 . ASP A 159 ? 0.5179 0.4009 0.4755 0.0289 0.2187 0.0054 159 ASP A OD1 1367 O OD2 . ASP A 159 ? 0.5780 0.4597 0.5093 0.0253 0.2054 0.0121 159 ASP A OD2 1368 N N . VAL A 160 ? 0.3471 0.2853 0.4045 0.0341 0.1908 0.0159 160 VAL A N 1369 C CA . VAL A 160 ? 0.2704 0.2244 0.3451 0.0349 0.1779 0.0190 160 VAL A CA 1370 C C . VAL A 160 ? 0.2765 0.2151 0.3127 0.0352 0.1670 0.0112 160 VAL A C 1371 O O . VAL A 160 ? 0.2875 0.2084 0.2936 0.0353 0.1692 0.0039 160 VAL A O 1372 C CB . VAL A 160 ? 0.2635 0.2339 0.3796 0.0420 0.1794 0.0254 160 VAL A CB 1373 C CG1 . VAL A 160 ? 0.3427 0.3328 0.4990 0.0419 0.1884 0.0342 160 VAL A CG1 1374 C CG2 . VAL A 160 ? 0.3093 0.2582 0.4083 0.0476 0.1856 0.0190 160 VAL A CG2 1375 N N . TYR A 161 ? 0.2471 0.1947 0.2851 0.0340 0.1549 0.0130 161 TYR A N 1376 C CA . TYR A 161 ? 0.2448 0.1803 0.2485 0.0341 0.1432 0.0064 161 TYR A CA 1377 C C . TYR A 161 ? 0.2534 0.1981 0.2732 0.0364 0.1298 0.0080 161 TYR A C 1378 O O . TYR A 161 ? 0.2300 0.1940 0.2837 0.0357 0.1221 0.0164 161 TYR A O 1379 C CB . TYR A 161 ? 0.2432 0.1739 0.2202 0.0292 0.1357 0.0072 161 TYR A CB 1380 C CG . TYR A 161 ? 0.2639 0.1835 0.2199 0.0271 0.1414 0.0071 161 TYR A CG 1381 C CD1 . TYR A 161 ? 0.2704 0.1925 0.2427 0.0240 0.1522 0.0123 161 TYR A CD1 1382 C CD2 . TYR A 161 ? 0.2779 0.1879 0.2008 0.0277 0.1358 0.0026 161 TYR A CD2 1383 C CE1 . TYR A 161 ? 0.3563 0.2668 0.3093 0.0233 0.1584 0.0131 161 TYR A CE1 1384 C CE2 . TYR A 161 ? 0.3020 0.2051 0.2077 0.0271 0.1411 0.0043 161 TYR A CE2 1385 C CZ . TYR A 161 ? 0.3058 0.2068 0.2252 0.0257 0.1529 0.0097 161 TYR A CZ 1386 O OH . TYR A 161 ? 0.3805 0.2730 0.2824 0.0258 0.1594 0.0120 161 TYR A OH 1387 N N . ASP A 162 ? 0.2300 0.1624 0.2246 0.0377 0.1247 0.0006 162 ASP A N 1388 C CA . ASP A 162 ? 0.2153 0.1528 0.2177 0.0383 0.1093 0.0022 162 ASP A CA 1389 C C . ASP A 162 ? 0.2397 0.1680 0.2063 0.0348 0.0984 -0.0048 162 ASP A C 1390 O O . ASP A 162 ? 0.2316 0.1490 0.1696 0.0334 0.1045 -0.0124 162 ASP A O 1391 C CB . ASP A 162 ? 0.2234 0.1553 0.2432 0.0451 0.1197 0.0011 162 ASP A CB 1392 C CG . ASP A 162 ? 0.2315 0.1770 0.2939 0.0516 0.1310 0.0112 162 ASP A CG 1393 O OD1 . ASP A 162 ? 0.2521 0.2186 0.3445 0.0530 0.1189 0.0228 162 ASP A OD1 1394 O OD2 . ASP A 162 ? 0.2689 0.2061 0.3313 0.0519 0.1454 0.0088 162 ASP A OD2 1395 N N . CYS A 163 ? 0.2054 0.1406 0.1742 0.0327 0.0813 -0.0013 163 CYS A N 1396 C CA . CYS A 163 ? 0.2002 0.1298 0.1431 0.0306 0.0715 -0.0069 163 CYS A CA 1397 C C . CYS A 163 ? 0.2294 0.1559 0.1826 0.0323 0.0701 -0.0088 163 CYS A C 1398 O O . CYS A 163 ? 0.2208 0.1555 0.1981 0.0344 0.0642 -0.0008 163 CYS A O 1399 C CB . CYS A 163 ? 0.2201 0.1559 0.1573 0.0274 0.0569 -0.0020 163 CYS A CB 1400 S SG . CYS A 163 ? 0.2791 0.2123 0.1900 0.0262 0.0460 -0.0066 163 CYS A SG 1401 N N . ARG A 164 ? 0.2108 0.1257 0.1452 0.0305 0.0761 -0.0190 164 ARG A N 1402 C CA . ARG A 164 ? 0.2157 0.1221 0.1580 0.0309 0.0786 -0.0221 164 ARG A CA 1403 C C . ARG A 164 ? 0.2293 0.1369 0.1538 0.0253 0.0658 -0.0262 164 ARG A C 1404 O O . ARG A 164 ? 0.2644 0.1730 0.1639 0.0198 0.0634 -0.0340 164 ARG A O 1405 C CB . ARG A 164 ? 0.2399 0.1325 0.1775 0.0287 0.0945 -0.0313 164 ARG A CB 1406 C CG . ARG A 164 ? 0.2496 0.1304 0.1961 0.0280 0.0990 -0.0337 164 ARG A CG 1407 C CD . ARG A 164 ? 0.3616 0.2297 0.3037 0.0229 0.1128 -0.0413 164 ARG A CD 1408 N NE . ARG A 164 ? 0.3212 0.1909 0.2337 0.0117 0.1075 -0.0529 164 ARG A NE 1409 C CZ . ARG A 164 ? 0.3132 0.1766 0.2133 0.0065 0.1164 -0.0600 164 ARG A CZ 1410 N NH1 . ARG A 164 ? 0.3284 0.1808 0.2423 0.0112 0.1328 -0.0573 164 ARG A NH1 1411 N NH2 . ARG A 164 ? 0.3752 0.2452 0.2504 -0.0028 0.1090 -0.0689 164 ARG A NH2 1412 N N . VAL A 165 ? 0.1994 0.1096 0.1380 0.0267 0.0576 -0.0197 165 VAL A N 1413 C CA . VAL A 165 ? 0.1975 0.1103 0.1228 0.0218 0.0461 -0.0219 165 VAL A CA 1414 C C . VAL A 165 ? 0.2372 0.1375 0.1682 0.0201 0.0515 -0.0252 165 VAL A C 1415 O O . VAL A 165 ? 0.2367 0.1324 0.1892 0.0261 0.0555 -0.0167 165 VAL A O 1416 C CB . VAL A 165 ? 0.1745 0.0993 0.1058 0.0233 0.0318 -0.0113 165 VAL A CB 1417 C CG1 . VAL A 165 ? 0.2032 0.1296 0.1240 0.0195 0.0227 -0.0124 165 VAL A CG1 1418 C CG2 . VAL A 165 ? 0.1934 0.1253 0.1161 0.0235 0.0291 -0.0095 165 VAL A CG2 1419 N N A GLU A 166 ? 0.2137 0.1096 0.1263 0.0115 0.0521 -0.0367 166 GLU A N 1420 N N B GLU A 166 ? 0.2135 0.1095 0.1261 0.0115 0.0520 -0.0366 166 GLU A N 1421 C CA A GLU A 166 ? 0.2539 0.1359 0.1693 0.0069 0.0580 -0.0413 166 GLU A CA 1422 C CA B GLU A 166 ? 0.2264 0.1084 0.1417 0.0069 0.0580 -0.0414 166 GLU A CA 1423 C C A GLU A 166 ? 0.2314 0.1235 0.1410 0.0021 0.0449 -0.0395 166 GLU A C 1424 C C B GLU A 166 ? 0.2233 0.1158 0.1332 0.0023 0.0447 -0.0391 166 GLU A C 1425 O O A GLU A 166 ? 0.2480 0.1550 0.1428 -0.0026 0.0359 -0.0432 166 GLU A O 1426 O O B GLU A 166 ? 0.2443 0.1519 0.1397 -0.0018 0.0352 -0.0421 166 GLU A O 1427 C CB A GLU A 166 ? 0.3004 0.1755 0.2051 -0.0032 0.0675 -0.0550 166 GLU A CB 1428 C CB B GLU A 166 ? 0.2890 0.1652 0.1928 -0.0035 0.0669 -0.0553 166 GLU A CB 1429 C CG A GLU A 166 ? 0.3389 0.2007 0.2540 0.0003 0.0835 -0.0554 166 GLU A CG 1430 C CG B GLU A 166 ? 0.3442 0.2163 0.2503 -0.0009 0.0776 -0.0568 166 GLU A CG 1431 C CD A GLU A 166 ? 0.4344 0.2892 0.3379 -0.0119 0.0914 -0.0677 166 GLU A CD 1432 C CD B GLU A 166 ? 0.4178 0.2920 0.3075 -0.0126 0.0798 -0.0685 166 GLU A CD 1433 O OE1 A GLU A 166 ? 0.5765 0.4170 0.4857 -0.0106 0.1066 -0.0690 166 GLU A OE1 1434 O OE1 B GLU A 166 ? 0.3979 0.2766 0.2801 -0.0119 0.0819 -0.0700 166 GLU A OE1 1435 O OE2 A GLU A 166 ? 0.4775 0.3418 0.3668 -0.0229 0.0828 -0.0754 166 GLU A OE2 1436 O OE2 B GLU A 166 ? 0.4772 0.3484 0.3611 -0.0229 0.0797 -0.0760 166 GLU A OE2 1437 N N . HIS A 167 ? 0.2160 0.1006 0.1382 0.0042 0.0452 -0.0323 167 HIS A N 1438 C CA . HIS A 167 ? 0.2060 0.0980 0.1237 -0.0001 0.0355 -0.0298 167 HIS A CA 1439 C C . HIS A 167 ? 0.2261 0.1000 0.1531 -0.0015 0.0445 -0.0278 167 HIS A C 1440 O O . HIS A 167 ? 0.2541 0.1146 0.1960 0.0065 0.0535 -0.0201 167 HIS A O 1441 C CB . HIS A 167 ? 0.1859 0.0917 0.1067 0.0066 0.0224 -0.0169 167 HIS A CB 1442 C CG . HIS A 167 ? 0.1793 0.0921 0.0933 0.0029 0.0144 -0.0147 167 HIS A CG 1443 N ND1 . HIS A 167 ? 0.1831 0.0887 0.1028 0.0033 0.0146 -0.0073 167 HIS A ND1 1444 C CD2 . HIS A 167 ? 0.1992 0.1259 0.1021 -0.0003 0.0075 -0.0177 167 HIS A CD2 1445 C CE1 . HIS A 167 ? 0.2083 0.1220 0.1197 -0.0006 0.0089 -0.0073 167 HIS A CE1 1446 N NE2 . HIS A 167 ? 0.2081 0.1353 0.1110 -0.0022 0.0047 -0.0133 167 HIS A NE2 1447 N N . TRP A 168 ? 0.2251 0.0989 0.1454 -0.0108 0.0433 -0.0330 168 TRP A N 1448 C CA . TRP A 168 ? 0.2556 0.1086 0.1833 -0.0136 0.0546 -0.0319 168 TRP A CA 1449 C C . TRP A 168 ? 0.2581 0.1058 0.1993 -0.0015 0.0530 -0.0124 168 TRP A C 1450 O O . TRP A 168 ? 0.2862 0.1131 0.2369 0.0011 0.0655 -0.0070 168 TRP A O 1451 C CB . TRP A 168 ? 0.3018 0.1592 0.2212 -0.0276 0.0533 -0.0411 168 TRP A CB 1452 C CG . TRP A 168 ? 0.2750 0.1392 0.1818 -0.0416 0.0552 -0.0598 168 TRP A CG 1453 C CD1 . TRP A 168 ? 0.3162 0.1721 0.2215 -0.0457 0.0653 -0.0690 168 TRP A CD1 1454 C CD2 . TRP A 168 ? 0.2612 0.1519 0.1589 -0.0520 0.0443 -0.0670 168 TRP A CD2 1455 N NE1 . TRP A 168 ? 0.3538 0.2315 0.2497 -0.0578 0.0590 -0.0794 168 TRP A NE1 1456 C CE2 . TRP A 168 ? 0.3152 0.2159 0.2084 -0.0611 0.0458 -0.0777 168 TRP A CE2 1457 C CE3 . TRP A 168 ? 0.2875 0.2010 0.1867 -0.0513 0.0324 -0.0601 168 TRP A CE3 1458 C CZ2 . TRP A 168 ? 0.2845 0.2157 0.1735 -0.0699 0.0352 -0.0821 168 TRP A CZ2 1459 C CZ3 . TRP A 168 ? 0.2602 0.2013 0.1534 -0.0613 0.0245 -0.0679 168 TRP A CZ3 1460 C CH2 . TRP A 168 ? 0.2600 0.2120 0.1511 -0.0691 0.0247 -0.0766 168 TRP A CH2 1461 N N . GLY A 169 ? 0.2201 0.0863 0.1611 0.0052 0.0385 -0.0016 169 GLY A N 1462 C CA . GLY A 169 ? 0.2384 0.1058 0.1889 0.0148 0.0338 0.0169 169 GLY A CA 1463 C C . GLY A 169 ? 0.2721 0.1386 0.2404 0.0260 0.0378 0.0269 169 GLY A C 1464 O O . GLY A 169 ? 0.2514 0.1222 0.2310 0.0346 0.0341 0.0444 169 GLY A O 1465 N N . LEU A 170 ? 0.2256 0.0893 0.1970 0.0260 0.0455 0.0169 170 LEU A N 1466 C CA . LEU A 170 ? 0.2282 0.0921 0.2199 0.0371 0.0523 0.0258 170 LEU A CA 1467 C C . LEU A 170 ? 0.3265 0.1661 0.3290 0.0401 0.0735 0.0233 170 LEU A C 1468 O O . LEU A 170 ? 0.4308 0.2554 0.4204 0.0297 0.0837 0.0063 170 LEU A O 1469 C CB . LEU A 170 ? 0.2168 0.0921 0.2052 0.0357 0.0501 0.0171 170 LEU A CB 1470 C CG . LEU A 170 ? 0.2722 0.1705 0.2522 0.0332 0.0320 0.0197 170 LEU A CG 1471 C CD1 . LEU A 170 ? 0.2661 0.1696 0.2382 0.0304 0.0336 0.0091 170 LEU A CD1 1472 C CD2 . LEU A 170 ? 0.2494 0.1638 0.2468 0.0404 0.0227 0.0378 170 LEU A CD2 1473 N N . ASP A 171 ? 0.2867 0.1338 0.3120 0.0509 0.0770 0.0387 171 ASP A N 1474 C CA . ASP A 171 ? 0.3425 0.1749 0.3785 0.0531 0.0966 0.0370 171 ASP A CA 1475 C C . ASP A 171 ? 0.4675 0.2952 0.5041 0.0515 0.1090 0.0252 171 ASP A C 1476 O O . ASP A 171 ? 0.4592 0.2685 0.4913 0.0461 0.1265 0.0147 171 ASP A O 1477 C CB . ASP A 171 ? 0.4166 0.2602 0.4765 0.0662 0.0970 0.0589 171 ASP A CB 1478 C CG . ASP A 171 ? 0.6965 0.5390 0.7519 0.0663 0.0900 0.0691 171 ASP A CG 1479 O OD1 . ASP A 171 ? 0.6906 0.5152 0.7292 0.0566 0.0943 0.0580 171 ASP A OD1 1480 O OD2 . ASP A 171 ? 0.8186 0.6798 0.8867 0.0750 0.0801 0.0880 171 ASP A OD2 1481 N N . GLU A 172 ? 0.3107 0.1552 0.3519 0.0552 0.1003 0.0274 172 GLU A N 1482 C CA A GLU A 172 ? 0.3154 0.1575 0.3547 0.0533 0.1107 0.0168 172 GLU A CA 1483 C CA B GLU A 172 ? 0.3157 0.1578 0.3551 0.0533 0.1107 0.0168 172 GLU A CA 1484 C C . GLU A 172 ? 0.2828 0.1366 0.3088 0.0499 0.0978 0.0102 172 GLU A C 1485 O O . GLU A 172 ? 0.2733 0.1389 0.2986 0.0520 0.0819 0.0182 172 GLU A O 1486 C CB A GLU A 172 ? 0.3410 0.1929 0.4091 0.0652 0.1197 0.0311 172 GLU A CB 1487 C CB B GLU A 172 ? 0.3425 0.1945 0.4108 0.0653 0.1196 0.0314 172 GLU A CB 1488 C CG A GLU A 172 ? 0.4015 0.2394 0.4824 0.0698 0.1369 0.0378 172 GLU A CG 1489 C CG B GLU A 172 ? 0.3408 0.2214 0.4311 0.0750 0.1032 0.0513 172 GLU A CG 1490 C CD A GLU A 172 ? 0.4938 0.3245 0.5870 0.0735 0.1572 0.0374 172 GLU A CD 1491 C CD B GLU A 172 ? 0.4247 0.3193 0.5460 0.0857 0.1118 0.0663 172 GLU A CD 1492 O OE1 A GLU A 172 ? 0.6962 0.5384 0.7939 0.0747 0.1557 0.0361 172 GLU A OE1 1493 O OE1 B GLU A 172 ? 0.4066 0.2859 0.5359 0.0892 0.1305 0.0679 172 GLU A OE1 1494 O OE2 A GLU A 172 ? 0.5240 0.3359 0.6221 0.0749 0.1763 0.0385 172 GLU A OE2 1495 O OE2 B GLU A 172 ? 0.4648 0.3861 0.6032 0.0898 0.1005 0.0770 172 GLU A OE2 1496 N N . PRO A 173 ? 0.3322 0.1823 0.3450 0.0440 0.1050 -0.0036 173 PRO A N 1497 C CA . PRO A 173 ? 0.3248 0.1867 0.3243 0.0420 0.0942 -0.0084 173 PRO A CA 1498 C C . PRO A 173 ? 0.2467 0.1308 0.2695 0.0514 0.0852 0.0079 173 PRO A C 1499 O O . PRO A 173 ? 0.2860 0.1755 0.3367 0.0608 0.0931 0.0197 173 PRO A O 1500 C CB . PRO A 173 ? 0.3759 0.2328 0.3592 0.0345 0.1044 -0.0224 173 PRO A CB 1501 C CG . PRO A 173 ? 0.4822 0.3255 0.4779 0.0357 0.1217 -0.0215 173 PRO A CG 1502 C CD . PRO A 173 ? 0.4728 0.3077 0.4773 0.0375 0.1223 -0.0154 173 PRO A CD 1503 N N . LEU A 174 ? 0.2317 0.1338 0.2428 0.0458 0.0670 0.0088 174 LEU A N 1504 C CA . LEU A 174 ? 0.1901 0.1155 0.2185 0.0489 0.0561 0.0214 174 LEU A CA 1505 C C . LEU A 174 ? 0.2191 0.1489 0.2433 0.0468 0.0613 0.0154 174 LEU A C 1506 O O . LEU A 174 ? 0.2771 0.2016 0.2749 0.0402 0.0597 0.0044 174 LEU A O 1507 C CB . LEU A 174 ? 0.2291 0.1660 0.2446 0.0428 0.0363 0.0248 174 LEU A CB 1508 C CG . LEU A 174 ? 0.3252 0.2854 0.3550 0.0421 0.0226 0.0371 174 LEU A CG 1509 C CD1 . LEU A 174 ? 0.3592 0.3323 0.4225 0.0513 0.0249 0.0532 174 LEU A CD1 1510 C CD2 . LEU A 174 ? 0.3951 0.3586 0.4067 0.0355 0.0071 0.0383 174 LEU A CD2 1511 N N . LEU A 175 ? 0.2017 0.1426 0.2533 0.0530 0.0682 0.0241 175 LEU A N 1512 C CA . LEU A 175 ? 0.1986 0.1444 0.2492 0.0509 0.0745 0.0203 175 LEU A CA 1513 C C . LEU A 175 ? 0.2079 0.1790 0.2752 0.0477 0.0613 0.0307 175 LEU A C 1514 O O . LEU A 175 ? 0.2740 0.2643 0.3715 0.0519 0.0563 0.0442 175 LEU A O 1515 C CB . LEU A 175 ? 0.2775 0.2156 0.3469 0.0589 0.0970 0.0202 175 LEU A CB 1516 C CG . LEU A 175 ? 0.3513 0.2626 0.3936 0.0563 0.1140 0.0038 175 LEU A CG 1517 C CD1 . LEU A 175 ? 0.3702 0.2659 0.4042 0.0543 0.1143 -0.0002 175 LEU A CD1 1518 C CD2 . LEU A 175 ? 0.4350 0.3440 0.4885 0.0574 0.1302 0.0043 175 LEU A CD2 1519 N N . LYS A 176 ? 0.1791 0.1503 0.2262 0.0397 0.0562 0.0246 176 LYS A N 1520 C CA . LYS A 176 ? 0.1613 0.1517 0.2205 0.0332 0.0472 0.0309 176 LYS A CA 1521 C C . LYS A 176 ? 0.1983 0.1872 0.2601 0.0319 0.0609 0.0277 176 LYS A C 1522 O O . LYS A 176 ? 0.1979 0.1693 0.2330 0.0314 0.0692 0.0187 176 LYS A O 1523 C CB . LYS A 176 ? 0.1950 0.1824 0.2286 0.0244 0.0325 0.0273 176 LYS A CB 1524 C CG . LYS A 176 ? 0.2530 0.2440 0.2849 0.0245 0.0192 0.0316 176 LYS A CG 1525 C CD . LYS A 176 ? 0.2454 0.2614 0.3074 0.0243 0.0102 0.0449 176 LYS A CD 1526 C CE . LYS A 176 ? 0.3579 0.3752 0.4167 0.0266 -0.0006 0.0512 176 LYS A CE 1527 N NZ . LYS A 176 ? 0.4678 0.5139 0.5515 0.0253 -0.0129 0.0661 176 LYS A NZ 1528 N N . HIS A 177 ? 0.1722 0.1821 0.2670 0.0312 0.0631 0.0364 177 HIS A N 1529 C CA . HIS A 177 ? 0.1782 0.1891 0.2843 0.0315 0.0797 0.0356 177 HIS A CA 1530 C C . HIS A 177 ? 0.2219 0.2367 0.3207 0.0195 0.0766 0.0339 177 HIS A C 1531 O O . HIS A 177 ? 0.2509 0.2767 0.3501 0.0098 0.0611 0.0360 177 HIS A O 1532 C CB . HIS A 177 ? 0.1743 0.2092 0.3273 0.0384 0.0860 0.0477 177 HIS A CB 1533 C CG . HIS A 177 ? 0.2339 0.2685 0.4030 0.0418 0.1079 0.0475 177 HIS A CG 1534 N ND1 . HIS A 177 ? 0.2562 0.2673 0.4139 0.0508 0.1289 0.0406 177 HIS A ND1 1535 C CD2 . HIS A 177 ? 0.2558 0.3107 0.4516 0.0365 0.1134 0.0529 177 HIS A CD2 1536 C CE1 . HIS A 177 ? 0.2993 0.3149 0.4745 0.0521 0.1472 0.0422 177 HIS A CE1 1537 N NE2 . HIS A 177 ? 0.2886 0.3315 0.4888 0.0438 0.1382 0.0502 177 HIS A NE2 1538 N N . TRP A 178 ? 0.2084 0.2110 0.2977 0.0193 0.0931 0.0297 178 TRP A N 1539 C CA . TRP A 178 ? 0.1981 0.2042 0.2893 0.0086 0.0961 0.0301 178 TRP A CA 1540 C C . TRP A 178 ? 0.2029 0.2107 0.3112 0.0114 0.1175 0.0319 178 TRP A C 1541 O O . TRP A 178 ? 0.2601 0.2512 0.3538 0.0202 0.1326 0.0278 178 TRP A O 1542 C CB . TRP A 178 ? 0.2464 0.2283 0.2962 0.0044 0.0946 0.0236 178 TRP A CB 1543 C CG . TRP A 178 ? 0.2526 0.2326 0.3039 -0.0069 0.1012 0.0243 178 TRP A CG 1544 C CD1 . TRP A 178 ? 0.3190 0.3044 0.3736 -0.0206 0.0912 0.0240 178 TRP A CD1 1545 C CD2 . TRP A 178 ? 0.2592 0.2295 0.3083 -0.0070 0.1211 0.0249 178 TRP A CD2 1546 N NE1 . TRP A 178 ? 0.3238 0.3019 0.3794 -0.0297 0.1042 0.0237 178 TRP A NE1 1547 C CE2 . TRP A 178 ? 0.2897 0.2590 0.3427 -0.0209 0.1226 0.0253 178 TRP A CE2 1548 C CE3 . TRP A 178 ? 0.3062 0.2666 0.3477 0.0021 0.1391 0.0244 178 TRP A CE3 1549 C CZ2 . TRP A 178 ? 0.2928 0.2514 0.3446 -0.0249 0.1418 0.0267 178 TRP A CZ2 1550 C CZ3 . TRP A 178 ? 0.4017 0.3531 0.4405 -0.0013 0.1573 0.0263 178 TRP A CZ3 1551 C CH2 . TRP A 178 ? 0.4036 0.3541 0.4485 -0.0142 0.1587 0.0280 178 TRP A CH2 1552 N N . GLU A 179 ? 0.2026 0.2313 0.3416 0.0023 0.1195 0.0373 179 GLU A N 1553 C CA . GLU A 179 ? 0.2161 0.2448 0.3692 0.0024 0.1415 0.0387 179 GLU A CA 1554 C C . GLU A 179 ? 0.2564 0.2966 0.4235 -0.0141 0.1414 0.0404 179 GLU A C 1555 O O . GLU A 179 ? 0.2585 0.3147 0.4346 -0.0261 0.1236 0.0412 179 GLU A O 1556 C CB . GLU A 179 ? 0.2471 0.2951 0.4405 0.0131 0.1529 0.0457 179 GLU A CB 1557 C CG . GLU A 179 ? 0.2745 0.3643 0.5182 0.0093 0.1402 0.0571 179 GLU A CG 1558 C CD . GLU A 179 ? 0.3305 0.4330 0.6070 0.0237 0.1493 0.0651 179 GLU A CD 1559 O OE1 . GLU A 179 ? 0.3001 0.3855 0.5646 0.0367 0.1517 0.0638 179 GLU A OE1 1560 O OE2 . GLU A 179 ? 0.3541 0.4790 0.6625 0.0211 0.1525 0.0716 179 GLU A OE2 1561 N N . PHE A 180 ? 0.2565 0.2866 0.4226 -0.0160 0.1625 0.0401 180 PHE A N 1562 C CA . PHE A 180 ? 0.3026 0.3369 0.4778 -0.0327 0.1661 0.0402 180 PHE A CA 1563 C C . PHE A 180 ? 0.4068 0.4850 0.6340 -0.0441 0.1561 0.0463 180 PHE A C 1564 O O . PHE A 180 ? 0.3649 0.4668 0.6249 -0.0352 0.1580 0.0526 180 PHE A O 1565 C CB . PHE A 180 ? 0.2726 0.2861 0.4317 -0.0284 0.1837 0.0383 180 PHE A CB 1566 C CG . PHE A 180 ? 0.3367 0.3473 0.4981 -0.0441 0.1882 0.0373 180 PHE A CG 1567 C CD1 . PHE A 180 ? 0.4452 0.4800 0.6436 -0.0518 0.1940 0.0406 180 PHE A CD1 1568 C CD2 . PHE A 180 ? 0.3440 0.3269 0.4707 -0.0508 0.1871 0.0332 180 PHE A CD2 1569 C CE1 . PHE A 180 ? 0.5054 0.5365 0.7051 -0.0679 0.1988 0.0387 180 PHE A CE1 1570 C CE2 . PHE A 180 ? 0.3722 0.3479 0.4995 -0.0650 0.1927 0.0314 180 PHE A CE2 1571 C CZ . PHE A 180 ? 0.4806 0.4803 0.6440 -0.0746 0.1985 0.0336 180 PHE A CZ 1572 N N . ASP A 181 ? 0.4322 0.5193 0.6613 -0.0635 0.1429 0.0436 181 ASP A N 1573 C CA . ASP A 181 ? 0.5911 0.7246 0.8653 -0.0779 0.1280 0.0489 181 ASP A CA 1574 C C . ASP A 181 ? 0.7580 0.9086 1.0567 -0.0885 0.1376 0.0501 181 ASP A C 1575 O O . ASP A 181 ? 0.7117 0.8341 0.9873 -0.0950 0.1516 0.0442 181 ASP A O 1576 C CB . ASP A 181 ? 0.5954 0.7283 0.8499 -0.0959 0.1063 0.0421 181 ASP A CB 1577 C CG . ASP A 181 ? 0.7297 0.9140 1.0260 -0.1143 0.0882 0.0470 181 ASP A CG 1578 O OD1 . ASP A 181 ? 0.7371 0.9618 1.0777 -0.1057 0.0854 0.0590 181 ASP A OD1 1579 O OD2 . ASP A 181 ? 0.7960 0.9803 1.0792 -0.1373 0.0769 0.0388 181 ASP A OD2 1587 N N . ASP B 4 ? 0.7410 0.6091 0.7000 0.0624 0.0862 -0.0992 2 ASP B N 1588 C CA . ASP B 4 ? 0.6215 0.4870 0.5727 0.0541 0.0761 -0.1000 2 ASP B CA 1589 C C . ASP B 4 ? 0.6246 0.4883 0.5921 0.0555 0.0715 -0.0894 2 ASP B C 1590 O O . ASP B 4 ? 0.7133 0.5889 0.6886 0.0577 0.0689 -0.0804 2 ASP B O 1591 C CB . ASP B 4 ? 0.5746 0.4542 0.5118 0.0491 0.0709 -0.1003 2 ASP B CB 1592 C CG . ASP B 4 ? 0.4768 0.3539 0.4022 0.0399 0.0610 -0.1046 2 ASP B CG 1593 O OD1 . ASP B 4 ? 0.4277 0.2933 0.3588 0.0369 0.0578 -0.1050 2 ASP B OD1 1594 O OD2 . ASP B 4 ? 0.5347 0.4220 0.4459 0.0358 0.0566 -0.1067 2 ASP B OD2 1595 N N . THR B 5 ? 0.5464 0.3953 0.5187 0.0543 0.0707 -0.0901 3 THR B N 1596 C CA . THR B 5 ? 0.5064 0.3524 0.4928 0.0562 0.0668 -0.0793 3 THR B CA 1597 C C . THR B 5 ? 0.3757 0.2183 0.3557 0.0472 0.0587 -0.0793 3 THR B C 1598 O O . THR B 5 ? 0.4973 0.3358 0.4862 0.0478 0.0556 -0.0707 3 THR B O 1599 C CB . THR B 5 ? 0.5738 0.4058 0.5728 0.0621 0.0723 -0.0768 3 THR B CB 1600 O OG1 . THR B 5 ? 0.6413 0.4580 0.6315 0.0570 0.0750 -0.0877 3 THR B OG1 1601 C CG2 . THR B 5 ? 0.6489 0.4869 0.6588 0.0719 0.0798 -0.0742 3 THR B CG2 1602 N N . ARG B 6 ? 0.3526 0.1975 0.3172 0.0392 0.0551 -0.0883 4 ARG B N 1603 C CA . ARG B 6 ? 0.3061 0.1499 0.2660 0.0301 0.0473 -0.0887 4 ARG B CA 1604 C C . ARG B 6 ? 0.2745 0.1280 0.2399 0.0306 0.0424 -0.0783 4 ARG B C 1605 O O . ARG B 6 ? 0.3119 0.1777 0.2771 0.0343 0.0426 -0.0749 4 ARG B O 1606 C CB . ARG B 6 ? 0.3252 0.1751 0.2687 0.0226 0.0427 -0.0985 4 ARG B CB 1607 C CG . ARG B 6 ? 0.4082 0.2467 0.3442 0.0198 0.0453 -0.1101 4 ARG B CG 1608 C CD . ARG B 6 ? 0.4588 0.3055 0.3781 0.0129 0.0387 -0.1182 4 ARG B CD 1609 N NE . ARG B 6 ? 0.4988 0.3593 0.4082 0.0170 0.0397 -0.1179 4 ARG B NE 1610 C CZ . ARG B 6 ? 0.4827 0.3544 0.3777 0.0131 0.0333 -0.1207 4 ARG B CZ 1611 N NH1 . ARG B 6 ? 0.4595 0.3310 0.3493 0.0050 0.0247 -0.1242 4 ARG B NH1 1612 N NH2 . ARG B 6 ? 0.4985 0.3820 0.3850 0.0174 0.0357 -0.1191 4 ARG B NH2 1613 N N . PRO B 7 ? 0.2703 0.1178 0.2404 0.0266 0.0386 -0.0734 5 PRO B N 1614 C CA . PRO B 7 ? 0.2496 0.1050 0.2229 0.0268 0.0341 -0.0641 5 PRO B CA 1615 C C . PRO B 7 ? 0.2703 0.1395 0.2331 0.0211 0.0288 -0.0675 5 PRO B C 1616 O O . PRO B 7 ? 0.2567 0.1284 0.2105 0.0142 0.0257 -0.0755 5 PRO B O 1617 C CB . PRO B 7 ? 0.2642 0.1091 0.2416 0.0221 0.0321 -0.0599 5 PRO B CB 1618 C CG . PRO B 7 ? 0.3475 0.1823 0.3220 0.0163 0.0338 -0.0694 5 PRO B CG 1619 C CD . PRO B 7 ? 0.3304 0.1631 0.3034 0.0221 0.0393 -0.0754 5 PRO B CD 1620 N N . ARG B 8 ? 0.2188 0.0977 0.1831 0.0245 0.0269 -0.0604 6 ARG B N 1621 C CA . ARG B 8 ? 0.2042 0.0995 0.1610 0.0196 0.0205 -0.0604 6 ARG B CA 1622 C C . ARG B 8 ? 0.1896 0.0913 0.1496 0.0154 0.0132 -0.0528 6 ARG B C 1623 O O . ARG B 8 ? 0.1912 0.0893 0.1589 0.0182 0.0126 -0.0448 6 ARG B O 1624 C CB . ARG B 8 ? 0.1945 0.1035 0.1530 0.0255 0.0218 -0.0563 6 ARG B CB 1625 C CG . ARG B 8 ? 0.2047 0.1158 0.1513 0.0253 0.0262 -0.0649 6 ARG B CG 1626 C CD . ARG B 8 ? 0.2257 0.1244 0.1715 0.0277 0.0333 -0.0729 6 ARG B CD 1627 N NE . ARG B 8 ? 0.2453 0.1497 0.1783 0.0264 0.0351 -0.0801 6 ARG B NE 1628 C CZ . ARG B 8 ? 0.2564 0.1543 0.1859 0.0286 0.0403 -0.0871 6 ARG B CZ 1629 N NH1 . ARG B 8 ? 0.2809 0.1663 0.2204 0.0321 0.0446 -0.0875 6 ARG B NH1 1630 N NH2 . ARG B 8 ? 0.2839 0.1877 0.1993 0.0278 0.0413 -0.0930 6 ARG B NH2 1631 N N . PHE B 9 ? 0.1818 0.0933 0.1354 0.0090 0.0079 -0.0550 7 PHE B N 1632 C CA . PHE B 9 ? 0.1685 0.0872 0.1252 0.0050 0.0021 -0.0488 7 PHE B CA 1633 C C . PHE B 9 ? 0.1551 0.0900 0.1084 0.0042 -0.0023 -0.0471 7 PHE B C 1634 O O . PHE B 9 ? 0.1693 0.1088 0.1151 0.0020 -0.0030 -0.0528 7 PHE B O 1635 C CB . PHE B 9 ? 0.1763 0.0879 0.1323 -0.0031 0.0009 -0.0536 7 PHE B CB 1636 C CG . PHE B 9 ? 0.1933 0.0864 0.1527 -0.0030 0.0065 -0.0564 7 PHE B CG 1637 C CD1 . PHE B 9 ? 0.2098 0.0943 0.1656 -0.0042 0.0099 -0.0664 7 PHE B CD1 1638 C CD2 . PHE B 9 ? 0.2262 0.1112 0.1920 -0.0013 0.0082 -0.0482 7 PHE B CD2 1639 C CE1 . PHE B 9 ? 0.2596 0.1291 0.2211 -0.0033 0.0145 -0.0672 7 PHE B CE1 1640 C CE2 . PHE B 9 ? 0.2122 0.0786 0.1821 -0.0006 0.0141 -0.0492 7 PHE B CE2 1641 C CZ . PHE B 9 ? 0.2316 0.0905 0.2005 -0.0018 0.0172 -0.0589 7 PHE B CZ 1642 N N . LEU B 10 ? 0.1413 0.0843 0.0997 0.0060 -0.0050 -0.0392 8 LEU B N 1643 C CA . LEU B 10 ? 0.1296 0.0862 0.0872 0.0062 -0.0078 -0.0367 8 LEU B CA 1644 C C . LEU B 10 ? 0.1193 0.0820 0.0795 0.0026 -0.0120 -0.0328 8 LEU B C 1645 O O . LEU B 10 ? 0.1359 0.0957 0.0997 0.0027 -0.0125 -0.0288 8 LEU B O 1646 C CB . LEU B 10 ? 0.1240 0.0851 0.0872 0.0122 -0.0059 -0.0318 8 LEU B CB 1647 C CG . LEU B 10 ? 0.1143 0.0874 0.0792 0.0125 -0.0074 -0.0284 8 LEU B CG 1648 C CD1 . LEU B 10 ? 0.1363 0.1128 0.0934 0.0125 -0.0051 -0.0317 8 LEU B CD1 1649 C CD2 . LEU B 10 ? 0.1509 0.1283 0.1254 0.0170 -0.0064 -0.0237 8 LEU B CD2 1650 N N . GLU B 11 ? 0.1153 0.0866 0.0733 -0.0002 -0.0147 -0.0338 9 GLU B N 1651 C CA . GLU B 11 ? 0.1056 0.0839 0.0678 -0.0024 -0.0175 -0.0301 9 GLU B CA 1652 C C . GLU B 11 ? 0.1194 0.1063 0.0832 0.0007 -0.0177 -0.0263 9 GLU B C 1653 O O . GLU B 11 ? 0.1347 0.1251 0.0943 0.0023 -0.0171 -0.0271 9 GLU B O 1654 C CB . GLU B 11 ? 0.1292 0.1115 0.0912 -0.0075 -0.0203 -0.0334 9 GLU B CB 1655 C CG . GLU B 11 ? 0.1087 0.0994 0.0770 -0.0090 -0.0223 -0.0296 9 GLU B CG 1656 C CD . GLU B 11 ? 0.1436 0.1298 0.1164 -0.0112 -0.0204 -0.0278 9 GLU B CD 1657 O OE1 . GLU B 11 ? 0.1473 0.1237 0.1183 -0.0122 -0.0183 -0.0289 9 GLU B OE1 1658 O OE2 . GLU B 11 ? 0.1351 0.1268 0.1129 -0.0116 -0.0203 -0.0250 9 GLU B OE2 1659 N N . GLN B 12 ? 0.0937 0.0831 0.0628 0.0013 -0.0181 -0.0223 10 GLN B N 1660 C CA . GLN B 12 ? 0.1004 0.0967 0.0733 0.0031 -0.0179 -0.0190 10 GLN B CA 1661 C C . GLN B 12 ? 0.1028 0.1025 0.0800 0.0012 -0.0190 -0.0173 10 GLN B C 1662 O O . GLN B 12 ? 0.0960 0.0928 0.0738 -0.0009 -0.0192 -0.0180 10 GLN B O 1663 C CB . GLN B 12 ? 0.0907 0.0869 0.0682 0.0057 -0.0165 -0.0170 10 GLN B CB 1664 C CG . GLN B 12 ? 0.0861 0.0792 0.0627 0.0087 -0.0144 -0.0181 10 GLN B CG 1665 C CD . GLN B 12 ? 0.1152 0.1119 0.1001 0.0111 -0.0136 -0.0156 10 GLN B CD 1666 O OE1 . GLN B 12 ? 0.1199 0.1219 0.1097 0.0114 -0.0119 -0.0136 10 GLN B OE1 1667 N NE2 . GLN B 12 ? 0.0948 0.0891 0.0827 0.0129 -0.0148 -0.0153 10 GLN B NE2 1668 N N . VAL B 13 ? 0.0759 0.0812 0.0563 0.0024 -0.0187 -0.0145 11 VAL B N 1669 C CA . VAL B 13 ? 0.0719 0.0797 0.0587 0.0017 -0.0183 -0.0127 11 VAL B CA 1670 C C . VAL B 13 ? 0.0889 0.0977 0.0810 0.0038 -0.0160 -0.0096 11 VAL B C 1671 O O . VAL B 13 ? 0.0979 0.1090 0.0891 0.0059 -0.0149 -0.0069 11 VAL B O 1672 C CB . VAL B 13 ? 0.0999 0.1139 0.0888 0.0012 -0.0201 -0.0115 11 VAL B CB 1673 C CG1 . VAL B 13 ? 0.1256 0.1412 0.1229 0.0012 -0.0183 -0.0100 11 VAL B CG1 1674 C CG2 . VAL B 13 ? 0.1025 0.1162 0.0878 -0.0019 -0.0225 -0.0152 11 VAL B CG2 1675 N N . LYS B 14 ? 0.0733 0.0798 0.0704 0.0029 -0.0147 -0.0105 12 LYS B N 1676 C CA . LYS B 14 ? 0.0676 0.0739 0.0720 0.0038 -0.0121 -0.0084 12 LYS B CA 1677 C C . LYS B 14 ? 0.0681 0.0731 0.0785 0.0036 -0.0099 -0.0086 12 LYS B C 1678 O O . LYS B 14 ? 0.0932 0.0953 0.1021 0.0016 -0.0098 -0.0127 12 LYS B O 1679 C CB . LYS B 14 ? 0.0706 0.0748 0.0766 0.0025 -0.0125 -0.0111 12 LYS B CB 1680 C CG . LYS B 14 ? 0.0678 0.0737 0.0709 0.0039 -0.0133 -0.0104 12 LYS B CG 1681 C CD . LYS B 14 ? 0.0684 0.0750 0.0764 0.0032 -0.0145 -0.0122 12 LYS B CD 1682 C CE . LYS B 14 ? 0.1277 0.1364 0.1354 0.0057 -0.0138 -0.0110 12 LYS B CE 1683 N NZ . LYS B 14 ? 0.0929 0.1050 0.1089 0.0057 -0.0154 -0.0119 12 LYS B NZ 1684 N N . HIS B 15 ? 0.0695 0.0763 0.0860 0.0061 -0.0077 -0.0038 13 HIS B N 1685 C CA . HIS B 15 ? 0.0900 0.0949 0.1148 0.0070 -0.0045 -0.0033 13 HIS B CA 1686 C C . HIS B 15 ? 0.0953 0.0945 0.1276 0.0065 -0.0006 -0.0033 13 HIS B C 1687 O O . HIS B 15 ? 0.0895 0.0893 0.1257 0.0085 0.0013 0.0024 13 HIS B O 1688 C CB . HIS B 15 ? 0.1026 0.1134 0.1318 0.0109 -0.0048 0.0032 13 HIS B CB 1689 C CG . HIS B 15 ? 0.1003 0.1185 0.1224 0.0107 -0.0099 0.0038 13 HIS B CG 1690 N ND1 . HIS B 15 ? 0.1104 0.1323 0.1340 0.0092 -0.0115 0.0012 13 HIS B ND1 1691 C CD2 . HIS B 15 ? 0.1138 0.1362 0.1279 0.0113 -0.0133 0.0060 13 HIS B CD2 1692 C CE1 . HIS B 15 ? 0.1236 0.1516 0.1416 0.0084 -0.0163 0.0014 13 HIS B CE1 1693 N NE2 . HIS B 15 ? 0.1084 0.1366 0.1195 0.0097 -0.0176 0.0038 13 HIS B NE2 1694 N N . GLU B 16 ? 0.0771 0.0709 0.1109 0.0035 0.0008 -0.0100 14 GLU B N 1695 C CA . GLU B 16 ? 0.0813 0.0699 0.1223 0.0010 0.0033 -0.0124 14 GLU B CA 1696 C C . GLU B 16 ? 0.1034 0.0845 0.1538 0.0011 0.0091 -0.0145 14 GLU B C 1697 O O . GLU B 16 ? 0.1189 0.0976 0.1673 0.0012 0.0107 -0.0188 14 GLU B O 1698 C CB . GLU B 16 ? 0.0871 0.0756 0.1225 -0.0033 -0.0007 -0.0199 14 GLU B CB 1699 C CG . GLU B 16 ? 0.1023 0.0967 0.1293 -0.0029 -0.0058 -0.0184 14 GLU B CG 1700 C CD . GLU B 16 ? 0.1183 0.1137 0.1423 -0.0061 -0.0102 -0.0239 14 GLU B CD 1701 O OE1 . GLU B 16 ? 0.1492 0.1413 0.1749 -0.0094 -0.0103 -0.0299 14 GLU B OE1 1702 O OE2 . GLU B 16 ? 0.1280 0.1275 0.1482 -0.0052 -0.0137 -0.0223 14 GLU B OE2 1703 N N . CYS B 17 ? 0.0933 0.0699 0.1548 0.0011 0.0133 -0.0116 15 CYS B N 1704 C CA . CYS B 17 ? 0.1028 0.0697 0.1752 0.0009 0.0198 -0.0143 15 CYS B CA 1705 C C . CYS B 17 ? 0.1236 0.0849 0.2021 -0.0053 0.0206 -0.0213 15 CYS B C 1706 O O . CYS B 17 ? 0.1320 0.0953 0.2166 -0.0066 0.0208 -0.0171 15 CYS B O 1707 C CB . CYS B 17 ? 0.1249 0.0900 0.2076 0.0066 0.0250 -0.0032 15 CYS B CB 1708 S SG . CYS B 17 ? 0.1545 0.1282 0.2333 0.0135 0.0228 0.0042 15 CYS B SG 1709 N N . HIS B 18 ? 0.1405 0.0956 0.2174 -0.0094 0.0212 -0.0324 16 HIS B N 1710 C CA . HIS B 18 ? 0.1507 0.1017 0.2332 -0.0165 0.0204 -0.0414 16 HIS B CA 1711 C C . HIS B 18 ? 0.1387 0.0771 0.2330 -0.0177 0.0285 -0.0453 16 HIS B C 1712 O O . HIS B 18 ? 0.1587 0.0925 0.2489 -0.0153 0.0323 -0.0483 16 HIS B O 1713 C CB . HIS B 18 ? 0.1341 0.0888 0.2022 -0.0209 0.0133 -0.0519 16 HIS B CB 1714 C CG . HIS B 18 ? 0.1473 0.1136 0.2047 -0.0194 0.0056 -0.0475 16 HIS B CG 1715 N ND1 . HIS B 18 ? 0.1877 0.1612 0.2454 -0.0232 -0.0012 -0.0498 16 HIS B ND1 1716 C CD2 . HIS B 18 ? 0.1772 0.1489 0.2252 -0.0145 0.0040 -0.0410 16 HIS B CD2 1717 C CE1 . HIS B 18 ? 0.1659 0.1474 0.2144 -0.0200 -0.0059 -0.0447 16 HIS B CE1 1718 N NE2 . HIS B 18 ? 0.1482 0.1281 0.1902 -0.0152 -0.0029 -0.0398 16 HIS B NE2 1719 N N . PHE B 19 ? 0.1441 0.0805 0.2511 -0.0207 0.0312 -0.0432 17 PHE B N 1720 C CA . PHE B 19 ? 0.1676 0.0949 0.2849 -0.0204 0.0390 -0.0435 17 PHE B CA 1721 C C . PHE B 19 ? 0.1714 0.0973 0.2904 -0.0281 0.0371 -0.0542 17 PHE B C 1722 O O . PHE B 19 ? 0.2147 0.1471 0.3365 -0.0329 0.0319 -0.0559 17 PHE B O 1723 C CB . PHE B 19 ? 0.1669 0.0916 0.2985 -0.0166 0.0455 -0.0303 17 PHE B CB 1724 C CG . PHE B 19 ? 0.1792 0.1060 0.3085 -0.0084 0.0466 -0.0180 17 PHE B CG 1725 C CD1 . PHE B 19 ? 0.1601 0.0951 0.2839 -0.0070 0.0417 -0.0115 17 PHE B CD1 1726 C CD2 . PHE B 19 ? 0.1819 0.1047 0.3139 -0.0018 0.0518 -0.0126 17 PHE B CD2 1727 C CE1 . PHE B 19 ? 0.1449 0.0868 0.2617 0.0007 0.0405 -0.0002 17 PHE B CE1 1728 C CE2 . PHE B 19 ? 0.1477 0.0753 0.2776 0.0062 0.0510 -0.0008 17 PHE B CE2 1729 C CZ . PHE B 19 ? 0.1375 0.0749 0.2588 0.0073 0.0450 0.0052 17 PHE B CZ 1730 N N . PHE B 20 ? 0.1870 0.1047 0.3050 -0.0290 0.0412 -0.0615 18 PHE B N 1731 C CA . PHE B 20 ? 0.2526 0.1674 0.3714 -0.0362 0.0395 -0.0726 18 PHE B CA 1732 C C . PHE B 20 ? 0.2648 0.1677 0.3976 -0.0357 0.0495 -0.0725 18 PHE B C 1733 O O . PHE B 20 ? 0.2727 0.1691 0.4054 -0.0306 0.0560 -0.0707 18 PHE B O 1734 C CB . PHE B 20 ? 0.3280 0.2431 0.4275 -0.0384 0.0342 -0.0837 18 PHE B CB 1735 C CG . PHE B 20 ? 0.4793 0.4046 0.5630 -0.0371 0.0259 -0.0826 18 PHE B CG 1736 C CD1 . PHE B 20 ? 0.4725 0.3990 0.5507 -0.0307 0.0280 -0.0764 18 PHE B CD1 1737 C CD2 . PHE B 20 ? 0.5574 0.4910 0.6323 -0.0421 0.0158 -0.0875 18 PHE B CD2 1738 C CE1 . PHE B 20 ? 0.3948 0.3298 0.4590 -0.0298 0.0210 -0.0756 18 PHE B CE1 1739 C CE2 . PHE B 20 ? 0.5138 0.4563 0.5746 -0.0404 0.0085 -0.0855 18 PHE B CE2 1740 C CZ . PHE B 20 ? 0.4011 0.3438 0.4563 -0.0344 0.0115 -0.0798 18 PHE B CZ 1741 N N . ASN B 21 ? 0.2759 0.1764 0.4220 -0.0409 0.0511 -0.0740 19 ASN B N 1742 C CA . ASN B 21 ? 0.3529 0.2416 0.5137 -0.0409 0.0610 -0.0740 19 ASN B CA 1743 C C . ASN B 21 ? 0.3298 0.2147 0.4995 -0.0320 0.0696 -0.0597 19 ASN B C 1744 O O . ASN B 21 ? 0.2941 0.1717 0.4644 -0.0275 0.0759 -0.0594 19 ASN B O 1745 C CB . ASN B 21 ? 0.3700 0.2499 0.5229 -0.0436 0.0626 -0.0872 19 ASN B CB 1746 C CG . ASN B 21 ? 0.5065 0.3731 0.6752 -0.0447 0.0727 -0.0893 19 ASN B CG 1747 O OD1 . ASN B 21 ? 0.5095 0.3735 0.6953 -0.0445 0.0781 -0.0814 19 ASN B OD1 1748 N ND2 . ASN B 21 ? 0.6778 0.5353 0.8405 -0.0457 0.0760 -0.0998 19 ASN B ND2 1749 N N . GLY B 22 ? 0.3696 0.2602 0.5456 -0.0293 0.0697 -0.0474 20 GLY B N 1750 C CA . GLY B 22 ? 0.4218 0.3114 0.6027 -0.0204 0.0757 -0.0323 20 GLY B CA 1751 C C . GLY B 22 ? 0.4034 0.2978 0.5711 -0.0147 0.0720 -0.0303 20 GLY B C 1752 O O . GLY B 22 ? 0.4114 0.3139 0.5674 -0.0160 0.0641 -0.0327 20 GLY B O 1753 N N . THR B 23 ? 0.2532 0.1427 0.4239 -0.0083 0.0778 -0.0258 21 THR B N 1754 C CA . THR B 23 ? 0.2683 0.1623 0.4288 -0.0029 0.0752 -0.0246 21 THR B CA 1755 C C . THR B 23 ? 0.2772 0.1653 0.4332 -0.0043 0.0780 -0.0367 21 THR B C 1756 O O . THR B 23 ? 0.2776 0.1675 0.4298 0.0010 0.0792 -0.0350 21 THR B O 1757 C CB . THR B 23 ? 0.2475 0.1438 0.4146 0.0066 0.0789 -0.0085 21 THR B CB 1758 O OG1 . THR B 23 ? 0.3052 0.1927 0.4865 0.0088 0.0878 -0.0042 21 THR B OG1 1759 C CG2 . THR B 23 ? 0.3511 0.2548 0.5168 0.0088 0.0751 0.0037 21 THR B CG2 1760 N N . GLU B 24 ? 0.2681 0.1495 0.4245 -0.0114 0.0790 -0.0487 22 GLU B N 1761 C CA . GLU B 24 ? 0.3045 0.1790 0.4551 -0.0132 0.0821 -0.0609 22 GLU B CA 1762 C C . GLU B 24 ? 0.2671 0.1484 0.3985 -0.0137 0.0756 -0.0676 22 GLU B C 1763 O O . GLU B 24 ? 0.3191 0.1984 0.4456 -0.0102 0.0794 -0.0703 22 GLU B O 1764 C CB . GLU B 24 ? 0.3915 0.2583 0.5446 -0.0215 0.0828 -0.0730 22 GLU B CB 1765 C CG . GLU B 24 ? 0.6154 0.4714 0.7667 -0.0225 0.0892 -0.0840 22 GLU B CG 1766 C CD . GLU B 24 ? 0.7379 0.5853 0.9056 -0.0158 0.1007 -0.0762 22 GLU B CD 1767 O OE1 . GLU B 24 ? 0.6231 0.4710 0.8050 -0.0119 0.1038 -0.0631 22 GLU B OE1 1768 O OE2 . GLU B 24 ? 0.8881 0.7282 1.0540 -0.0140 0.1068 -0.0828 22 GLU B OE2 1769 N N . ARG B 25 ? 0.2289 0.1185 0.3502 -0.0177 0.0663 -0.0694 23 ARG B N 1770 C CA . ARG B 25 ? 0.2203 0.1169 0.3231 -0.0180 0.0597 -0.0740 23 ARG B CA 1771 C C . ARG B 25 ? 0.2162 0.1229 0.3174 -0.0156 0.0536 -0.0648 23 ARG B C 1772 O O . ARG B 25 ? 0.2158 0.1259 0.3223 -0.0185 0.0498 -0.0615 23 ARG B O 1773 C CB . ARG B 25 ? 0.2715 0.1682 0.3604 -0.0257 0.0533 -0.0872 23 ARG B CB 1774 C CG . ARG B 25 ? 0.5469 0.4529 0.6166 -0.0270 0.0441 -0.0896 23 ARG B CG 1775 C CD . ARG B 25 ? 0.7333 0.6402 0.7914 -0.0221 0.0470 -0.0895 23 ARG B CD 1776 N NE . ARG B 25 ? 0.7940 0.7090 0.8332 -0.0239 0.0384 -0.0918 23 ARG B NE 1777 C CZ . ARG B 25 ? 0.6529 0.5725 0.6829 -0.0199 0.0388 -0.0885 23 ARG B CZ 1778 N NH1 . ARG B 25 ? 0.4914 0.4095 0.5304 -0.0141 0.0468 -0.0831 23 ARG B NH1 1779 N NH2 . ARG B 25 ? 0.4968 0.4230 0.5097 -0.0218 0.0311 -0.0899 23 ARG B NH2 1780 N N . VAL B 26 ? 0.1878 0.0992 0.2828 -0.0104 0.0534 -0.0607 24 VAL B N 1781 C CA . VAL B 26 ? 0.1691 0.0887 0.2628 -0.0076 0.0483 -0.0521 24 VAL B CA 1782 C C . VAL B 26 ? 0.1755 0.1012 0.2529 -0.0074 0.0438 -0.0564 24 VAL B C 1783 O O . VAL B 26 ? 0.2259 0.1500 0.2981 -0.0054 0.0479 -0.0601 24 VAL B O 1784 C CB . VAL B 26 ? 0.1665 0.0868 0.2735 0.0006 0.0530 -0.0384 24 VAL B CB 1785 C CG1 . VAL B 26 ? 0.1759 0.1045 0.2803 0.0037 0.0473 -0.0300 24 VAL B CG1 1786 C CG2 . VAL B 26 ? 0.1933 0.1073 0.3155 0.0010 0.0585 -0.0325 24 VAL B CG2 1787 N N . ARG B 27 ? 0.1506 0.0833 0.2206 -0.0096 0.0360 -0.0557 25 ARG B N 1788 C CA . ARG B 27 ? 0.1504 0.0893 0.2053 -0.0094 0.0317 -0.0582 25 ARG B CA 1789 C C . ARG B 27 ? 0.1586 0.1084 0.2138 -0.0056 0.0267 -0.0464 25 ARG B C 1790 O O . ARG B 27 ? 0.1589 0.1121 0.2189 -0.0062 0.0232 -0.0409 25 ARG B O 1791 C CB . ARG B 27 ? 0.1849 0.1271 0.2243 -0.0157 0.0240 -0.0660 25 ARG B CB 1792 C CG . ARG B 27 ? 0.2164 0.1644 0.2383 -0.0156 0.0198 -0.0674 25 ARG B CG 1793 C CD . ARG B 27 ? 0.2306 0.1806 0.2369 -0.0204 0.0126 -0.0736 25 ARG B CD 1794 N NE . ARG B 27 ? 0.2239 0.1795 0.2132 -0.0199 0.0078 -0.0724 25 ARG B NE 1795 C CZ . ARG B 27 ? 0.5224 0.4801 0.4964 -0.0225 0.0010 -0.0753 25 ARG B CZ 1796 N NH1 . ARG B 27 ? 0.5878 0.5433 0.5618 -0.0263 -0.0024 -0.0809 25 ARG B NH1 1797 N NH2 . ARG B 27 ? 0.4253 0.3870 0.3847 -0.0211 -0.0024 -0.0723 25 ARG B NH2 1798 N N . PHE B 28 ? 0.1223 0.0779 0.1722 -0.0019 0.0269 -0.0427 26 PHE B N 1799 C CA . PHE B 28 ? 0.1091 0.0752 0.1582 0.0012 0.0220 -0.0327 26 PHE B CA 1800 C C . PHE B 28 ? 0.1272 0.0989 0.1609 -0.0012 0.0166 -0.0352 26 PHE B C 1801 O O . PHE B 28 ? 0.1327 0.1024 0.1588 -0.0021 0.0193 -0.0404 26 PHE B O 1802 C CB . PHE B 28 ? 0.1074 0.0768 0.1670 0.0073 0.0264 -0.0257 26 PHE B CB 1803 C CG . PHE B 28 ? 0.0966 0.0778 0.1533 0.0095 0.0208 -0.0181 26 PHE B CG 1804 C CD1 . PHE B 28 ? 0.1394 0.1258 0.1957 0.0104 0.0156 -0.0112 26 PHE B CD1 1805 C CD2 . PHE B 28 ? 0.1168 0.1036 0.1713 0.0101 0.0213 -0.0188 26 PHE B CD2 1806 C CE1 . PHE B 28 ? 0.1661 0.1624 0.2183 0.0117 0.0103 -0.0061 26 PHE B CE1 1807 C CE2 . PHE B 28 ? 0.1285 0.1258 0.1816 0.0109 0.0158 -0.0132 26 PHE B CE2 1808 C CZ . PHE B 28 ? 0.1344 0.1361 0.1856 0.0116 0.0100 -0.0075 26 PHE B CZ 1809 N N . LEU B 29 ? 0.1034 0.0811 0.1324 -0.0019 0.0100 -0.0311 27 LEU B N 1810 C CA . LEU B 29 ? 0.0937 0.0758 0.1099 -0.0034 0.0052 -0.0315 27 LEU B CA 1811 C C . LEU B 29 ? 0.1472 0.1365 0.1647 -0.0008 0.0022 -0.0241 27 LEU B C 1812 O O . LEU B 29 ? 0.1486 0.1405 0.1701 0.0004 0.0000 -0.0197 27 LEU B O 1813 C CB . LEU B 29 ? 0.1667 0.1487 0.1758 -0.0067 -0.0005 -0.0349 27 LEU B CB 1814 C CG . LEU B 29 ? 0.2130 0.1898 0.2186 -0.0105 -0.0005 -0.0437 27 LEU B CG 1815 C CD1 . LEU B 29 ? 0.2560 0.2369 0.2569 -0.0131 -0.0081 -0.0450 27 LEU B CD1 1816 C CD2 . LEU B 29 ? 0.2554 0.2282 0.2496 -0.0113 0.0028 -0.0491 27 LEU B CD2 1817 N N . ASP B 30 ? 0.0826 0.0750 0.0963 -0.0006 0.0023 -0.0232 28 ASP B N 1818 C CA . ASP B 30 ? 0.1065 0.1056 0.1206 0.0005 -0.0012 -0.0182 28 ASP B CA 1819 C C . ASP B 30 ? 0.1432 0.1411 0.1459 -0.0020 -0.0047 -0.0199 28 ASP B C 1820 O O . ASP B 30 ? 0.1590 0.1548 0.1561 -0.0037 -0.0028 -0.0220 28 ASP B O 1821 C CB . ASP B 30 ? 0.1222 0.1263 0.1437 0.0018 0.0016 -0.0162 28 ASP B CB 1822 C CG . ASP B 30 ? 0.1487 0.1614 0.1756 0.0037 -0.0025 -0.0108 28 ASP B CG 1823 O OD1 . ASP B 30 ? 0.1650 0.1789 0.1934 0.0059 -0.0045 -0.0071 28 ASP B OD1 1824 O OD2 . ASP B 30 ? 0.1442 0.1630 0.1740 0.0027 -0.0034 -0.0102 28 ASP B OD2 1825 N N . ARG B 31 ? 0.0793 0.0780 0.0788 -0.0018 -0.0088 -0.0184 29 ARG B N 1826 C CA . ARG B 31 ? 0.0764 0.0725 0.0666 -0.0032 -0.0117 -0.0196 29 ARG B CA 1827 C C . ARG B 31 ? 0.0852 0.0830 0.0733 -0.0029 -0.0140 -0.0175 29 ARG B C 1828 O O . ARG B 31 ? 0.0874 0.0885 0.0785 -0.0014 -0.0151 -0.0157 29 ARG B O 1829 C CB . ARG B 31 ? 0.0761 0.0712 0.0660 -0.0031 -0.0140 -0.0209 29 ARG B CB 1830 C CG . ARG B 31 ? 0.0801 0.0731 0.0732 -0.0044 -0.0121 -0.0246 29 ARG B CG 1831 C CD . ARG B 31 ? 0.0936 0.0876 0.0895 -0.0053 -0.0153 -0.0262 29 ARG B CD 1832 N NE . ARG B 31 ? 0.1056 0.1000 0.0929 -0.0060 -0.0200 -0.0274 29 ARG B NE 1833 C CZ . ARG B 31 ? 0.1022 0.1002 0.0928 -0.0063 -0.0243 -0.0279 29 ARG B CZ 1834 N NH1 . ARG B 31 ? 0.1367 0.1375 0.1392 -0.0068 -0.0235 -0.0279 29 ARG B NH1 1835 N NH2 . ARG B 31 ? 0.1115 0.1106 0.0945 -0.0059 -0.0292 -0.0278 29 ARG B NH2 1836 N N . TYR B 32 ? 0.0771 0.0717 0.0595 -0.0045 -0.0141 -0.0180 30 TYR B N 1837 C CA . TYR B 32 ? 0.0780 0.0718 0.0584 -0.0049 -0.0157 -0.0175 30 TYR B CA 1838 C C . TYR B 32 ? 0.0911 0.0790 0.0652 -0.0042 -0.0170 -0.0171 30 TYR B C 1839 O O . TYR B 32 ? 0.1058 0.0900 0.0748 -0.0044 -0.0166 -0.0164 30 TYR B O 1840 C CB . TYR B 32 ? 0.0952 0.0899 0.0780 -0.0079 -0.0140 -0.0178 30 TYR B CB 1841 C CG . TYR B 32 ? 0.0967 0.0997 0.0883 -0.0079 -0.0142 -0.0174 30 TYR B CG 1842 C CD1 . TYR B 32 ? 0.0920 0.0981 0.0895 -0.0065 -0.0115 -0.0165 30 TYR B CD1 1843 C CD2 . TYR B 32 ? 0.1310 0.1390 0.1250 -0.0089 -0.0173 -0.0179 30 TYR B CD2 1844 C CE1 . TYR B 32 ? 0.1055 0.1198 0.1128 -0.0052 -0.0119 -0.0147 30 TYR B CE1 1845 C CE2 . TYR B 32 ? 0.1479 0.1654 0.1499 -0.0083 -0.0190 -0.0164 30 TYR B CE2 1846 C CZ . TYR B 32 ? 0.1622 0.1830 0.1717 -0.0060 -0.0163 -0.0140 30 TYR B CZ 1847 O OH . TYR B 32 ? 0.1972 0.2281 0.2162 -0.0042 -0.0182 -0.0112 30 TYR B OH 1848 N N . PHE B 33 ? 0.0971 0.0840 0.0709 -0.0027 -0.0183 -0.0174 31 PHE B N 1849 C CA . PHE B 33 ? 0.0948 0.0765 0.0654 -0.0005 -0.0191 -0.0163 31 PHE B CA 1850 C C . PHE B 33 ? 0.0938 0.0698 0.0628 -0.0008 -0.0180 -0.0176 31 PHE B C 1851 O O . PHE B 33 ? 0.1172 0.0951 0.0869 -0.0018 -0.0178 -0.0204 31 PHE B O 1852 C CB . PHE B 33 ? 0.1098 0.0957 0.0843 0.0027 -0.0203 -0.0159 31 PHE B CB 1853 C CG . PHE B 33 ? 0.0832 0.0743 0.0614 0.0023 -0.0212 -0.0158 31 PHE B CG 1854 C CD1 . PHE B 33 ? 0.0763 0.0713 0.0586 0.0013 -0.0197 -0.0162 31 PHE B CD1 1855 C CD2 . PHE B 33 ? 0.1028 0.0947 0.0809 0.0028 -0.0238 -0.0155 31 PHE B CD2 1856 C CE1 . PHE B 33 ? 0.0872 0.0848 0.0743 0.0007 -0.0195 -0.0167 31 PHE B CE1 1857 C CE2 . PHE B 33 ? 0.1097 0.1055 0.0918 0.0013 -0.0246 -0.0172 31 PHE B CE2 1858 C CZ . PHE B 33 ? 0.0821 0.0796 0.0691 0.0001 -0.0218 -0.0180 31 PHE B CZ 1859 N N . TYR B 34 ? 0.1015 0.0698 0.0677 0.0004 -0.0174 -0.0157 32 TYR B N 1860 C CA . TYR B 34 ? 0.1097 0.0697 0.0755 0.0008 -0.0154 -0.0172 32 TYR B CA 1861 C C . TYR B 34 ? 0.1579 0.1159 0.1252 0.0066 -0.0158 -0.0148 32 TYR B C 1862 O O . TYR B 34 ? 0.1321 0.0892 0.0986 0.0091 -0.0174 -0.0101 32 TYR B O 1863 C CB . TYR B 34 ? 0.1186 0.0698 0.0824 -0.0024 -0.0130 -0.0158 32 TYR B CB 1864 C CG . TYR B 34 ? 0.1296 0.0697 0.0942 -0.0026 -0.0102 -0.0181 32 TYR B CG 1865 C CD1 . TYR B 34 ? 0.1689 0.1090 0.1345 -0.0056 -0.0098 -0.0250 32 TYR B CD1 1866 C CD2 . TYR B 34 ? 0.1407 0.0699 0.1044 0.0004 -0.0079 -0.0134 32 TYR B CD2 1867 C CE1 . TYR B 34 ? 0.1593 0.0878 0.1252 -0.0063 -0.0067 -0.0290 32 TYR B CE1 1868 C CE2 . TYR B 34 ? 0.1729 0.0896 0.1386 0.0004 -0.0042 -0.0159 32 TYR B CE2 1869 C CZ . TYR B 34 ? 0.1546 0.0706 0.1215 -0.0034 -0.0033 -0.0246 32 TYR B CZ 1870 O OH . TYR B 34 ? 0.1891 0.0914 0.1576 -0.0040 0.0008 -0.0290 32 TYR B OH 1871 N N . HIS B 35 ? 0.1210 0.0798 0.0906 0.0088 -0.0143 -0.0179 33 HIS B N 1872 C CA . HIS B 35 ? 0.1228 0.0840 0.0975 0.0146 -0.0140 -0.0160 33 HIS B CA 1873 C C . HIS B 35 ? 0.1265 0.0988 0.1052 0.0150 -0.0176 -0.0133 33 HIS B C 1874 O O . HIS B 35 ? 0.1730 0.1515 0.1520 0.0127 -0.0176 -0.0152 33 HIS B O 1875 C CB . HIS B 35 ? 0.1238 0.0762 0.1005 0.0189 -0.0130 -0.0122 33 HIS B CB 1876 C CG . HIS B 35 ? 0.1441 0.0829 0.1178 0.0174 -0.0088 -0.0152 33 HIS B CG 1877 N ND1 . HIS B 35 ? 0.1745 0.1103 0.1452 0.0140 -0.0060 -0.0226 33 HIS B ND1 1878 C CD2 . HIS B 35 ? 0.1792 0.1060 0.1527 0.0187 -0.0069 -0.0116 33 HIS B CD2 1879 C CE1 . HIS B 35 ? 0.1741 0.0966 0.1439 0.0124 -0.0027 -0.0249 33 HIS B CE1 1880 N NE2 . HIS B 35 ? 0.1719 0.0880 0.1440 0.0153 -0.0025 -0.0178 33 HIS B NE2 1881 N N . GLN B 36 ? 0.1333 0.1078 0.1149 0.0177 -0.0209 -0.0091 34 GLN B N 1882 C CA . GLN B 36 ? 0.1426 0.1270 0.1276 0.0166 -0.0250 -0.0083 34 GLN B CA 1883 C C . GLN B 36 ? 0.1651 0.1483 0.1421 0.0134 -0.0280 -0.0073 34 GLN B C 1884 O O . GLN B 36 ? 0.1916 0.1813 0.1697 0.0119 -0.0314 -0.0079 34 GLN B O 1885 C CB . GLN B 36 ? 0.2318 0.2231 0.2263 0.0210 -0.0281 -0.0053 34 GLN B CB 1886 C CG . GLN B 36 ? 0.2143 0.2098 0.2191 0.0241 -0.0242 -0.0063 34 GLN B CG 1887 C CD . GLN B 36 ? 0.2993 0.2871 0.3053 0.0292 -0.0203 -0.0054 34 GLN B CD 1888 O OE1 . GLN B 36 ? 0.4103 0.3987 0.4225 0.0342 -0.0223 -0.0012 34 GLN B OE1 1889 N NE2 . GLN B 36 ? 0.2282 0.2087 0.2284 0.0281 -0.0147 -0.0095 34 GLN B NE2 1890 N N . GLU B 37 ? 0.1296 0.1042 0.0990 0.0120 -0.0259 -0.0062 35 GLU B N 1891 C CA . GLU B 37 ? 0.1654 0.1379 0.1259 0.0098 -0.0271 -0.0043 35 GLU B CA 1892 C C . GLU B 37 ? 0.1289 0.1030 0.0876 0.0050 -0.0246 -0.0080 35 GLU B C 1893 O O . GLU B 37 ? 0.1397 0.1104 0.0991 0.0026 -0.0211 -0.0096 35 GLU B O 1894 C CB . GLU B 37 ? 0.1897 0.1515 0.1443 0.0108 -0.0247 0.0002 35 GLU B CB 1895 C CG . GLU B 37 ? 0.3078 0.2659 0.2517 0.0080 -0.0233 0.0027 35 GLU B CG 1896 C CD . GLU B 37 ? 0.4170 0.3630 0.3571 0.0078 -0.0186 0.0072 35 GLU B CD 1897 O OE1 . GLU B 37 ? 0.3340 0.2763 0.2674 0.0043 -0.0148 0.0087 35 GLU B OE1 1898 O OE2 . GLU B 37 ? 0.3750 0.3144 0.3197 0.0110 -0.0177 0.0093 35 GLU B OE2 1899 N N . GLU B 38 ? 0.1200 0.0996 0.0775 0.0035 -0.0266 -0.0100 36 GLU B N 1900 C CA . GLU B 38 ? 0.1010 0.0813 0.0577 -0.0001 -0.0233 -0.0130 36 GLU B CA 1901 C C . GLU B 38 ? 0.1228 0.0971 0.0710 -0.0019 -0.0199 -0.0110 36 GLU B C 1902 O O . GLU B 38 ? 0.1418 0.1133 0.0806 -0.0009 -0.0212 -0.0082 36 GLU B O 1903 C CB . GLU B 38 ? 0.1005 0.0855 0.0574 -0.0013 -0.0252 -0.0162 36 GLU B CB 1904 C CG . GLU B 38 ? 0.1025 0.0881 0.0620 -0.0038 -0.0208 -0.0193 36 GLU B CG 1905 C CD . GLU B 38 ? 0.1035 0.0914 0.0643 -0.0051 -0.0216 -0.0236 36 GLU B CD 1906 O OE1 . GLU B 38 ? 0.1488 0.1385 0.1064 -0.0052 -0.0264 -0.0248 36 GLU B OE1 1907 O OE2 . GLU B 38 ? 0.1207 0.1087 0.0870 -0.0061 -0.0176 -0.0258 36 GLU B OE2 1908 N N . TYR B 39 ? 0.1071 0.0801 0.0588 -0.0045 -0.0156 -0.0119 37 TYR B N 1909 C CA . TYR B 39 ? 0.1346 0.1021 0.0810 -0.0067 -0.0110 -0.0095 37 TYR B CA 1910 C C . TYR B 39 ? 0.1568 0.1273 0.1040 -0.0093 -0.0063 -0.0117 37 TYR B C 1911 O O . TYR B 39 ? 0.1432 0.1098 0.0836 -0.0108 -0.0017 -0.0097 37 TYR B O 1912 C CB . TYR B 39 ? 0.1193 0.0816 0.0701 -0.0082 -0.0090 -0.0083 37 TYR B CB 1913 C CG . TYR B 39 ? 0.1088 0.0761 0.0699 -0.0104 -0.0092 -0.0122 37 TYR B CG 1914 C CD1 . TYR B 39 ? 0.1383 0.1097 0.1058 -0.0142 -0.0061 -0.0137 37 TYR B CD1 1915 C CD2 . TYR B 39 ? 0.1227 0.0913 0.0869 -0.0085 -0.0125 -0.0142 37 TYR B CD2 1916 C CE1 . TYR B 39 ? 0.1222 0.1000 0.0985 -0.0159 -0.0079 -0.0168 37 TYR B CE1 1917 C CE2 . TYR B 39 ? 0.0993 0.0728 0.0696 -0.0104 -0.0134 -0.0177 37 TYR B CE2 1918 C CZ . TYR B 39 ? 0.1508 0.1294 0.1269 -0.0141 -0.0119 -0.0188 37 TYR B CZ 1919 O OH . TYR B 39 ? 0.1287 0.1141 0.1106 -0.0158 -0.0144 -0.0217 37 TYR B OH 1920 N N . VAL B 40 ? 0.1062 0.0831 0.0619 -0.0094 -0.0067 -0.0151 38 VAL B N 1921 C CA . VAL B 40 ? 0.1065 0.0863 0.0655 -0.0107 -0.0016 -0.0172 38 VAL B CA 1922 C C . VAL B 40 ? 0.1053 0.0899 0.0712 -0.0092 -0.0032 -0.0202 38 VAL B C 1923 O O . VAL B 40 ? 0.1038 0.0912 0.0751 -0.0078 -0.0073 -0.0199 38 VAL B O 1924 C CB . VAL B 40 ? 0.1176 0.1001 0.0861 -0.0133 0.0024 -0.0162 38 VAL B CB 1925 C CG1 . VAL B 40 ? 0.1127 0.1011 0.0919 -0.0132 -0.0019 -0.0169 38 VAL B CG1 1926 C CG2 . VAL B 40 ? 0.1273 0.1130 0.1004 -0.0141 0.0092 -0.0176 38 VAL B CG2 1927 N N . ARG B 41 ? 0.1030 0.0875 0.0686 -0.0092 0.0010 -0.0231 39 ARG B N 1928 C CA . ARG B 41 ? 0.1013 0.0880 0.0746 -0.0078 0.0008 -0.0259 39 ARG B CA 1929 C C . ARG B 41 ? 0.1521 0.1388 0.1305 -0.0076 0.0080 -0.0284 39 ARG B C 1930 O O . ARG B 41 ? 0.1397 0.1234 0.1106 -0.0087 0.0132 -0.0300 39 ARG B O 1931 C CB . ARG B 41 ? 0.1829 0.1669 0.1494 -0.0080 -0.0032 -0.0290 39 ARG B CB 1932 C CG . ARG B 41 ? 0.2200 0.1996 0.1726 -0.0095 -0.0015 -0.0328 39 ARG B CG 1933 C CD . ARG B 41 ? 0.1893 0.1679 0.1397 -0.0105 -0.0050 -0.0385 39 ARG B CD 1934 N NE . ARG B 41 ? 0.1733 0.1554 0.1262 -0.0101 -0.0127 -0.0364 39 ARG B NE 1935 C CZ . ARG B 41 ? 0.2282 0.2117 0.1808 -0.0117 -0.0176 -0.0406 39 ARG B CZ 1936 N NH1 . ARG B 41 ? 0.2218 0.2022 0.1696 -0.0143 -0.0161 -0.0480 39 ARG B NH1 1937 N NH2 . ARG B 41 ? 0.2276 0.2159 0.1855 -0.0109 -0.0238 -0.0379 39 ARG B NH2 1938 N N . PHE B 42 ? 0.1215 0.1113 0.1130 -0.0055 0.0091 -0.0282 40 PHE B N 1939 C CA . PHE B 42 ? 0.1255 0.1136 0.1237 -0.0041 0.0163 -0.0312 40 PHE B CA 1940 C C . PHE B 42 ? 0.1066 0.0890 0.1036 -0.0041 0.0158 -0.0359 40 PHE B C 1941 O O . PHE B 42 ? 0.1139 0.0976 0.1172 -0.0033 0.0116 -0.0337 40 PHE B O 1942 C CB . PHE B 42 ? 0.0948 0.0904 0.1108 -0.0010 0.0180 -0.0267 40 PHE B CB 1943 C CG . PHE B 42 ? 0.1006 0.0944 0.1273 0.0019 0.0260 -0.0288 40 PHE B CG 1944 C CD1 . PHE B 42 ? 0.1046 0.1017 0.1380 0.0028 0.0333 -0.0289 40 PHE B CD1 1945 C CD2 . PHE B 42 ? 0.1031 0.0915 0.1351 0.0038 0.0272 -0.0305 40 PHE B CD2 1946 C CE1 . PHE B 42 ? 0.1112 0.1062 0.1559 0.0064 0.0418 -0.0309 40 PHE B CE1 1947 C CE2 . PHE B 42 ? 0.1103 0.0952 0.1532 0.0070 0.0355 -0.0325 40 PHE B CE2 1948 C CZ . PHE B 42 ? 0.1266 0.1147 0.1758 0.0087 0.0429 -0.0329 40 PHE B CZ 1949 N N . ASP B 43 ? 0.1194 0.0954 0.1084 -0.0055 0.0205 -0.0427 41 ASP B N 1950 C CA . ASP B 43 ? 0.1271 0.0967 0.1157 -0.0068 0.0208 -0.0494 41 ASP B CA 1951 C C . ASP B 43 ? 0.1447 0.1095 0.1432 -0.0045 0.0306 -0.0530 41 ASP B C 1952 O O . ASP B 43 ? 0.1511 0.1144 0.1449 -0.0040 0.0377 -0.0557 41 ASP B O 1953 C CB . ASP B 43 ? 0.1459 0.1117 0.1149 -0.0105 0.0180 -0.0559 41 ASP B CB 1954 C CG . ASP B 43 ? 0.1730 0.1334 0.1408 -0.0134 0.0163 -0.0644 41 ASP B CG 1955 O OD1 . ASP B 43 ? 0.1752 0.1315 0.1572 -0.0127 0.0204 -0.0666 41 ASP B OD1 1956 O OD2 . ASP B 43 ? 0.2160 0.1767 0.1696 -0.0161 0.0099 -0.0674 41 ASP B OD2 1957 N N . SER B 44 ? 0.1329 0.0948 0.1458 -0.0028 0.0321 -0.0526 42 SER B N 1958 C CA . SER B 44 ? 0.1416 0.0976 0.1663 0.0004 0.0422 -0.0555 42 SER B CA 1959 C C . SER B 44 ? 0.1610 0.1075 0.1737 -0.0025 0.0481 -0.0670 42 SER B C 1960 O O . SER B 44 ? 0.1705 0.1141 0.1887 0.0002 0.0566 -0.0683 42 SER B O 1961 C CB . SER B 44 ? 0.1386 0.0915 0.1808 0.0030 0.0429 -0.0517 42 SER B CB 1962 O OG . SER B 44 ? 0.1451 0.0915 0.1837 -0.0016 0.0394 -0.0574 42 SER B OG 1963 N N . ASP B 45 ? 0.1693 0.1147 0.1649 -0.0075 0.0410 -0.0718 43 ASP B N 1964 C CA . ASP B 45 ? 0.1876 0.1280 0.1682 -0.0099 0.0426 -0.0791 43 ASP B CA 1965 C C . ASP B 45 ? 0.1947 0.1368 0.1638 -0.0085 0.0487 -0.0789 43 ASP B C 1966 O O . ASP B 45 ? 0.2129 0.1504 0.1731 -0.0087 0.0539 -0.0844 43 ASP B O 1967 C CB . ASP B 45 ? 0.2715 0.2130 0.2372 -0.0145 0.0320 -0.0824 43 ASP B CB 1968 C CG . ASP B 45 ? 0.3397 0.2781 0.3154 -0.0173 0.0280 -0.0854 43 ASP B CG 1969 O OD1 . ASP B 45 ? 0.3135 0.2482 0.3071 -0.0156 0.0334 -0.0839 43 ASP B OD1 1970 O OD2 . ASP B 45 ? 0.3853 0.3250 0.3514 -0.0210 0.0195 -0.0886 43 ASP B OD2 1971 N N . VAL B 46 ? 0.1818 0.1303 0.1513 -0.0073 0.0484 -0.0728 44 VAL B N 1972 C CA . VAL B 46 ? 0.1876 0.1384 0.1473 -0.0067 0.0544 -0.0711 44 VAL B CA 1973 C C . VAL B 46 ? 0.2043 0.1592 0.1837 -0.0024 0.0642 -0.0670 44 VAL B C 1974 O O . VAL B 46 ? 0.1965 0.1508 0.1764 -0.0009 0.0733 -0.0679 44 VAL B O 1975 C CB . VAL B 46 ? 0.1832 0.1383 0.1293 -0.0091 0.0475 -0.0666 44 VAL B CB 1976 C CG1 . VAL B 46 ? 0.2113 0.1688 0.1508 -0.0087 0.0549 -0.0626 44 VAL B CG1 1977 C CG2 . VAL B 46 ? 0.2010 0.1544 0.1291 -0.0119 0.0376 -0.0693 44 VAL B CG2 1978 N N . GLY B 47 ? 0.1614 0.1235 0.1586 -0.0002 0.0594 -0.0593 45 GLY B N 1979 C CA . GLY B 47 ? 0.1540 0.1235 0.1732 0.0044 0.0653 -0.0534 45 GLY B CA 1980 C C . GLY B 47 ? 0.1454 0.1254 0.1670 0.0036 0.0639 -0.0462 45 GLY B C 1981 O O . GLY B 47 ? 0.1488 0.1373 0.1891 0.0066 0.0686 -0.0417 45 GLY B O 1982 N N . GLU B 48 ? 0.1504 0.1302 0.1551 -0.0006 0.0574 -0.0450 46 GLU B N 1983 C CA . GLU B 48 ? 0.1462 0.1340 0.1535 -0.0024 0.0554 -0.0383 46 GLU B CA 1984 C C . GLU B 48 ? 0.1640 0.1510 0.1597 -0.0052 0.0441 -0.0357 46 GLU B C 1985 O O . GLU B 48 ? 0.1538 0.1346 0.1371 -0.0059 0.0391 -0.0391 46 GLU B O 1986 C CB . GLU B 48 ? 0.1510 0.1366 0.1482 -0.0043 0.0653 -0.0397 46 GLU B CB 1987 C CG . GLU B 48 ? 0.2574 0.2470 0.2706 -0.0014 0.0780 -0.0406 46 GLU B CG 1988 C CD . GLU B 48 ? 0.4380 0.4258 0.4408 -0.0036 0.0891 -0.0410 46 GLU B CD 1989 O OE1 . GLU B 48 ? 0.3075 0.2891 0.2874 -0.0070 0.0868 -0.0406 46 GLU B OE1 1990 O OE2 . GLU B 48 ? 0.3894 0.3825 0.4076 -0.0015 0.1005 -0.0408 46 GLU B OE2 1991 N N . TYR B 49 ? 0.1276 0.1210 0.1287 -0.0067 0.0401 -0.0300 47 TYR B N 1992 C CA . TYR B 49 ? 0.1180 0.1090 0.1076 -0.0090 0.0315 -0.0278 47 TYR B CA 1993 C C . TYR B 49 ? 0.1432 0.1268 0.1126 -0.0112 0.0342 -0.0285 47 TYR B C 1994 O O . TYR B 49 ? 0.1632 0.1455 0.1294 -0.0122 0.0431 -0.0284 47 TYR B O 1995 C CB . TYR B 49 ? 0.1137 0.1120 0.1144 -0.0105 0.0270 -0.0229 47 TYR B CB 1996 C CG . TYR B 49 ? 0.0991 0.1045 0.1130 -0.0081 0.0207 -0.0214 47 TYR B CG 1997 C CD1 . TYR B 49 ? 0.1159 0.1303 0.1481 -0.0058 0.0231 -0.0197 47 TYR B CD1 1998 C CD2 . TYR B 49 ? 0.1089 0.1124 0.1171 -0.0077 0.0128 -0.0208 47 TYR B CD2 1999 C CE1 . TYR B 49 ? 0.1133 0.1342 0.1554 -0.0030 0.0170 -0.0169 47 TYR B CE1 2000 C CE2 . TYR B 49 ? 0.0918 0.1012 0.1094 -0.0053 0.0079 -0.0186 47 TYR B CE2 2001 C CZ . TYR B 49 ? 0.1262 0.1440 0.1595 -0.0029 0.0098 -0.0163 47 TYR B CZ 2002 O OH . TYR B 49 ? 0.1186 0.1424 0.1592 0.0000 0.0047 -0.0128 47 TYR B OH 2003 N N . ARG B 50 ? 0.1335 0.1127 0.0895 -0.0117 0.0267 -0.0284 48 ARG B N 2004 C CA . ARG B 50 ? 0.1512 0.1242 0.0874 -0.0130 0.0272 -0.0269 48 ARG B CA 2005 C C . ARG B 50 ? 0.1915 0.1635 0.1249 -0.0131 0.0190 -0.0221 48 ARG B C 2006 O O . ARG B 50 ? 0.1698 0.1442 0.1088 -0.0119 0.0116 -0.0228 48 ARG B O 2007 C CB . ARG B 50 ? 0.1723 0.1407 0.0923 -0.0126 0.0260 -0.0327 48 ARG B CB 2008 C CG . ARG B 50 ? 0.1917 0.1582 0.1110 -0.0123 0.0355 -0.0391 48 ARG B CG 2009 C CD . ARG B 50 ? 0.2525 0.2160 0.1607 -0.0132 0.0459 -0.0373 48 ARG B CD 2010 N NE . ARG B 50 ? 0.2713 0.2323 0.1782 -0.0125 0.0564 -0.0444 48 ARG B NE 2011 C CZ . ARG B 50 ? 0.3297 0.2944 0.2534 -0.0114 0.0667 -0.0441 48 ARG B CZ 2012 N NH1 . ARG B 50 ? 0.3374 0.3095 0.2803 -0.0116 0.0665 -0.0373 48 ARG B NH1 2013 N NH2 . ARG B 50 ? 0.3365 0.2978 0.2588 -0.0100 0.0771 -0.0510 48 ARG B NH2 2014 N N . ALA B 51 ? 0.1515 0.1194 0.0771 -0.0143 0.0214 -0.0169 49 ALA B N 2015 C CA . ALA B 51 ? 0.1500 0.1149 0.0728 -0.0138 0.0149 -0.0121 49 ALA B CA 2016 C C . ALA B 51 ? 0.1838 0.1471 0.0933 -0.0114 0.0075 -0.0128 49 ALA B C 2017 O O . ALA B 51 ? 0.2177 0.1790 0.1118 -0.0111 0.0086 -0.0143 49 ALA B O 2018 C CB . ALA B 51 ? 0.2054 0.1641 0.1227 -0.0155 0.0206 -0.0058 49 ALA B CB 2019 N N . VAL B 52 ? 0.1527 0.1178 0.0682 -0.0097 -0.0002 -0.0120 50 VAL B N 2020 C CA . VAL B 52 ? 0.1850 0.1508 0.0918 -0.0073 -0.0079 -0.0117 50 VAL B CA 2021 C C . VAL B 52 ? 0.2081 0.1685 0.1059 -0.0051 -0.0099 -0.0039 50 VAL B C 2022 O O . VAL B 52 ? 0.2533 0.2135 0.1377 -0.0031 -0.0146 -0.0015 50 VAL B O 2023 C CB . VAL B 52 ? 0.1636 0.1351 0.0833 -0.0062 -0.0141 -0.0147 50 VAL B CB 2024 C CG1 . VAL B 52 ? 0.1965 0.1709 0.1107 -0.0042 -0.0223 -0.0144 50 VAL B CG1 2025 C CG2 . VAL B 52 ? 0.1706 0.1457 0.0988 -0.0079 -0.0114 -0.0209 50 VAL B CG2 2026 N N . THR B 53 ? 0.1589 0.1149 0.0643 -0.0055 -0.0066 0.0000 51 THR B N 2027 C CA . THR B 53 ? 0.2034 0.1513 0.1022 -0.0035 -0.0060 0.0081 51 THR B CA 2028 C C . THR B 53 ? 0.2475 0.1891 0.1497 -0.0071 0.0031 0.0107 51 THR B C 2029 O O . THR B 53 ? 0.2221 0.1677 0.1340 -0.0108 0.0073 0.0060 51 THR B O 2030 C CB . THR B 53 ? 0.2463 0.1933 0.1546 -0.0003 -0.0113 0.0099 51 THR B CB 2031 O OG1 . THR B 53 ? 0.2394 0.1863 0.1617 -0.0029 -0.0085 0.0059 51 THR B OG1 2032 C CG2 . THR B 53 ? 0.2060 0.1615 0.1163 0.0026 -0.0196 0.0069 51 THR B CG2 2033 N N . GLU B 54 ? 0.2030 0.1350 0.0991 -0.0061 0.0061 0.0187 52 GLU B N 2034 C CA . GLU B 54 ? 0.2512 0.1763 0.1518 -0.0105 0.0156 0.0217 52 GLU B CA 2035 C C . GLU B 54 ? 0.2381 0.1654 0.1582 -0.0144 0.0162 0.0159 52 GLU B C 2036 O O . GLU B 54 ? 0.2376 0.1664 0.1666 -0.0195 0.0225 0.0140 52 GLU B O 2037 C CB . GLU B 54 ? 0.3443 0.2568 0.2369 -0.0083 0.0186 0.0322 52 GLU B CB 2038 C CG . GLU B 54 ? 0.6037 0.5147 0.4745 -0.0039 0.0170 0.0394 52 GLU B CG 2039 C CD . GLU B 54 ? 0.8905 0.7881 0.7527 -0.0017 0.0221 0.0520 52 GLU B CD 2040 O OE1 . GLU B 54 ? 0.9478 0.8361 0.8230 -0.0033 0.0261 0.0544 52 GLU B OE1 2041 O OE2 . GLU B 54 ? 0.9755 0.8714 0.8173 0.0015 0.0223 0.0594 52 GLU B OE2 2042 N N . LEU B 55 ? 0.2206 0.1493 0.1473 -0.0120 0.0094 0.0128 53 LEU B N 2043 C CA . LEU B 55 ? 0.1968 0.1282 0.1385 -0.0152 0.0084 0.0065 53 LEU B CA 2044 C C . LEU B 55 ? 0.2068 0.1497 0.1568 -0.0186 0.0090 0.0005 53 LEU B C 2045 O O . LEU B 55 ? 0.2144 0.1604 0.1764 -0.0228 0.0097 -0.0034 53 LEU B O 2046 C CB . LEU B 55 ? 0.2783 0.2110 0.2219 -0.0108 0.0015 0.0041 53 LEU B CB 2047 C CG . LEU B 55 ? 0.3852 0.3123 0.3376 -0.0120 0.0015 0.0007 53 LEU B CG 2048 C CD1 . LEU B 55 ? 0.3455 0.2584 0.2983 -0.0139 0.0072 0.0053 53 LEU B CD1 2049 C CD2 . LEU B 55 ? 0.3479 0.2763 0.3002 -0.0063 -0.0037 -0.0004 53 LEU B CD2 2050 N N . GLY B 56 ? 0.1651 0.1145 0.1093 -0.0168 0.0084 -0.0004 54 GLY B N 2051 C CA . GLY B 56 ? 0.1792 0.1387 0.1324 -0.0185 0.0091 -0.0053 54 GLY B CA 2052 C C . GLY B 56 ? 0.1837 0.1451 0.1391 -0.0216 0.0174 -0.0045 54 GLY B C 2053 O O . GLY B 56 ? 0.1814 0.1515 0.1467 -0.0224 0.0189 -0.0079 54 GLY B O 2054 N N . ARG B 57 ? 0.1758 0.1291 0.1226 -0.0228 0.0235 0.0007 55 ARG B N 2055 C CA . ARG B 57 ? 0.2080 0.1627 0.1556 -0.0254 0.0333 0.0020 55 ARG B CA 2056 C C . ARG B 57 ? 0.1761 0.1388 0.1451 -0.0302 0.0369 -0.0005 55 ARG B C 2057 O O . ARG B 57 ? 0.1923 0.1629 0.1687 -0.0306 0.0421 -0.0026 55 ARG B O 2058 C CB . ARG B 57 ? 0.2564 0.2001 0.1898 -0.0258 0.0400 0.0096 55 ARG B CB 2059 C CG . ARG B 57 ? 0.3421 0.2811 0.2530 -0.0209 0.0364 0.0124 55 ARG B CG 2060 C CD . ARG B 57 ? 0.4944 0.4220 0.3905 -0.0203 0.0417 0.0220 55 ARG B CD 2061 N NE . ARG B 57 ? 0.5314 0.4568 0.4050 -0.0154 0.0367 0.0249 55 ARG B NE 2062 C CZ . ARG B 57 ? 0.7670 0.6834 0.6248 -0.0126 0.0373 0.0345 55 ARG B CZ 2063 N NH1 . ARG B 57 ? 0.8511 0.7577 0.7140 -0.0145 0.0439 0.0423 55 ARG B NH1 2064 N NH2 . ARG B 57 ? 0.8071 0.7243 0.6447 -0.0081 0.0309 0.0366 55 ARG B NH2 2065 N N . PRO B 58 ? 0.1825 0.1438 0.1625 -0.0338 0.0341 -0.0009 56 PRO B N 2066 C CA . PRO B 58 ? 0.1564 0.1277 0.1575 -0.0390 0.0362 -0.0038 56 PRO B CA 2067 C C . PRO B 58 ? 0.1309 0.1163 0.1425 -0.0368 0.0307 -0.0086 56 PRO B C 2068 O O . PRO B 58 ? 0.1639 0.1599 0.1906 -0.0385 0.0347 -0.0094 56 PRO B O 2069 C CB . PRO B 58 ? 0.2289 0.1950 0.2367 -0.0433 0.0321 -0.0052 56 PRO B CB 2070 C CG . PRO B 58 ? 0.2194 0.1694 0.2109 -0.0410 0.0339 0.0000 56 PRO B CG 2071 C CD . PRO B 58 ? 0.2040 0.1542 0.1790 -0.0340 0.0306 0.0013 56 PRO B CD 2072 N N . ASP B 59 ? 0.1505 0.1360 0.1552 -0.0326 0.0224 -0.0108 57 ASP B N 2073 C CA . ASP B 59 ? 0.1589 0.1560 0.1723 -0.0298 0.0175 -0.0138 57 ASP B CA 2074 C C . ASP B 59 ? 0.1341 0.1344 0.1465 -0.0263 0.0229 -0.0136 57 ASP B C 2075 O O . ASP B 59 ? 0.1148 0.1257 0.1416 -0.0253 0.0238 -0.0145 57 ASP B O 2076 C CB . ASP B 59 ? 0.1566 0.1520 0.1625 -0.0264 0.0088 -0.0155 57 ASP B CB 2077 C CG . ASP B 59 ? 0.2229 0.2167 0.2316 -0.0296 0.0038 -0.0175 57 ASP B CG 2078 O OD1 . ASP B 59 ? 0.2036 0.2034 0.2250 -0.0345 0.0039 -0.0192 57 ASP B OD1 2079 O OD2 . ASP B 59 ? 0.1767 0.1636 0.1758 -0.0274 0.0000 -0.0181 57 ASP B OD2 2080 N N . ALA B 60 ? 0.1223 0.1135 0.1180 -0.0241 0.0263 -0.0127 58 ALA B N 2081 C CA . ALA B 60 ? 0.1463 0.1386 0.1391 -0.0214 0.0324 -0.0142 58 ALA B CA 2082 C C . ALA B 60 ? 0.1363 0.1348 0.1425 -0.0236 0.0423 -0.0134 58 ALA B C 2083 O O . ALA B 60 ? 0.1594 0.1652 0.1771 -0.0212 0.0456 -0.0154 58 ALA B O 2084 C CB . ALA B 60 ? 0.1973 0.1792 0.1677 -0.0199 0.0342 -0.0139 58 ALA B CB 2085 N N . GLU B 61 ? 0.1351 0.1305 0.1417 -0.0279 0.0477 -0.0102 59 GLU B N 2086 C CA A GLU B 61 ? 0.1400 0.1420 0.1613 -0.0305 0.0583 -0.0090 59 GLU B CA 2087 C CA B GLU B 61 ? 0.1931 0.1951 0.2143 -0.0304 0.0584 -0.0091 59 GLU B CA 2088 C C . GLU B 61 ? 0.1681 0.1856 0.2166 -0.0318 0.0547 -0.0103 59 GLU B C 2089 O O . GLU B 61 ? 0.1604 0.1876 0.2244 -0.0303 0.0610 -0.0107 59 GLU B O 2090 C CB A GLU B 61 ? 0.2196 0.2140 0.2365 -0.0355 0.0655 -0.0043 59 GLU B CB 2091 C CB B GLU B 61 ? 0.2593 0.2536 0.2751 -0.0351 0.0666 -0.0043 59 GLU B CB 2092 C CG A GLU B 61 ? 0.3664 0.3480 0.3568 -0.0335 0.0718 -0.0014 59 GLU B CG 2093 C CG B GLU B 61 ? 0.2979 0.2866 0.3142 -0.0392 0.0602 -0.0023 59 GLU B CG 2094 C CD A GLU B 61 ? 0.4706 0.4438 0.4562 -0.0379 0.0803 0.0052 59 GLU B CD 2095 C CD B GLU B 61 ? 0.4257 0.4045 0.4369 -0.0436 0.0696 0.0036 59 GLU B CD 2096 O OE1 A GLU B 61 ? 0.5063 0.4852 0.5124 -0.0430 0.0864 0.0067 59 GLU B OE1 2097 O OE1 B GLU B 61 ? 0.3930 0.3745 0.4221 -0.0498 0.0718 0.0043 59 GLU B OE1 2098 O OE2 A GLU B 61 ? 0.4397 0.4008 0.4019 -0.0361 0.0806 0.0094 59 GLU B OE2 2099 O OE2 B GLU B 61 ? 0.4536 0.4216 0.4427 -0.0410 0.0746 0.0076 59 GLU B OE2 2100 N N . TYR B 62 ? 0.1285 0.1487 0.1825 -0.0343 0.0445 -0.0110 60 TYR B N 2101 C CA . TYR B 62 ? 0.1173 0.1536 0.1950 -0.0360 0.0388 -0.0122 60 TYR B CA 2102 C C . TYR B 62 ? 0.1303 0.1752 0.2140 -0.0294 0.0349 -0.0130 60 TYR B C 2103 O O . TYR B 62 ? 0.1426 0.2013 0.2470 -0.0280 0.0369 -0.0122 60 TYR B O 2104 C CB . TYR B 62 ? 0.1765 0.2118 0.2538 -0.0402 0.0285 -0.0141 60 TYR B CB 2105 C CG . TYR B 62 ? 0.1483 0.2006 0.2465 -0.0425 0.0203 -0.0161 60 TYR B CG 2106 C CD1 . TYR B 62 ? 0.1905 0.2571 0.3129 -0.0462 0.0241 -0.0156 60 TYR B CD1 2107 C CD2 . TYR B 62 ? 0.1354 0.1903 0.2287 -0.0411 0.0086 -0.0185 60 TYR B CD2 2108 C CE1 . TYR B 62 ? 0.2534 0.3378 0.3952 -0.0484 0.0149 -0.0173 60 TYR B CE1 2109 C CE2 . TYR B 62 ? 0.1787 0.2500 0.2881 -0.0432 0.0000 -0.0203 60 TYR B CE2 2110 C CZ . TYR B 62 ? 0.2356 0.3221 0.3693 -0.0468 0.0023 -0.0197 60 TYR B CZ 2111 O OH . TYR B 62 ? 0.2793 0.3843 0.4295 -0.0489 -0.0079 -0.0214 60 TYR B OH 2112 N N . TRP B 63 ? 0.1086 0.1456 0.1759 -0.0251 0.0297 -0.0140 61 TRP B N 2113 C CA . TRP B 63 ? 0.0904 0.1334 0.1633 -0.0190 0.0264 -0.0140 61 TRP B CA 2114 C C . TRP B 63 ? 0.0967 0.1399 0.1750 -0.0151 0.0370 -0.0142 61 TRP B C 2115 O O . TRP B 63 ? 0.1002 0.1530 0.1950 -0.0107 0.0374 -0.0130 61 TRP B O 2116 C CB . TRP B 63 ? 0.0915 0.1251 0.1468 -0.0163 0.0197 -0.0150 61 TRP B CB 2117 C CG . TRP B 63 ? 0.0839 0.1185 0.1360 -0.0190 0.0102 -0.0152 61 TRP B CG 2118 C CD1 . TRP B 63 ? 0.1126 0.1560 0.1760 -0.0233 0.0059 -0.0155 61 TRP B CD1 2119 C CD2 . TRP B 63 ? 0.0825 0.1089 0.1194 -0.0177 0.0045 -0.0160 61 TRP B CD2 2120 N NE1 . TRP B 63 ? 0.1227 0.1623 0.1765 -0.0247 -0.0018 -0.0172 61 TRP B NE1 2121 C CE2 . TRP B 63 ? 0.1204 0.1499 0.1586 -0.0209 -0.0022 -0.0171 61 TRP B CE2 2122 C CE3 . TRP B 63 ? 0.1102 0.1277 0.1337 -0.0145 0.0045 -0.0165 61 TRP B CE3 2123 C CZ2 . TRP B 63 ? 0.0936 0.1167 0.1197 -0.0201 -0.0075 -0.0183 61 TRP B CZ2 2124 C CZ3 . TRP B 63 ? 0.0959 0.1088 0.1097 -0.0140 -0.0015 -0.0170 61 TRP B CZ3 2125 C CH2 . TRP B 63 ? 0.1069 0.1224 0.1219 -0.0163 -0.0068 -0.0176 61 TRP B CH2 2126 N N . ASN B 64 ? 0.1153 0.1479 0.1795 -0.0163 0.0459 -0.0156 62 ASN B N 2127 C CA . ASN B 64 ? 0.1140 0.1450 0.1801 -0.0129 0.0574 -0.0174 62 ASN B CA 2128 C C . ASN B 64 ? 0.1149 0.1588 0.2054 -0.0135 0.0656 -0.0154 62 ASN B C 2129 O O . ASN B 64 ? 0.1362 0.1821 0.2353 -0.0094 0.0753 -0.0167 62 ASN B O 2130 C CB . ASN B 64 ? 0.1287 0.1455 0.1700 -0.0142 0.0645 -0.0196 62 ASN B CB 2131 C CG . ASN B 64 ? 0.1773 0.1836 0.1983 -0.0122 0.0578 -0.0227 62 ASN B CG 2132 O OD1 . ASN B 64 ? 0.1410 0.1495 0.1679 -0.0092 0.0512 -0.0237 62 ASN B OD1 2133 N ND2 . ASN B 64 ? 0.1563 0.1522 0.1543 -0.0139 0.0595 -0.0237 62 ASN B ND2 2134 N N . SER B 65 ? 0.1107 0.1635 0.2139 -0.0187 0.0621 -0.0128 63 SER B N 2135 C CA . SER B 65 ? 0.1107 0.1787 0.2414 -0.0201 0.0685 -0.0108 63 SER B CA 2136 C C . SER B 65 ? 0.1302 0.2152 0.2853 -0.0158 0.0609 -0.0091 63 SER B C 2137 O O . SER B 65 ? 0.1440 0.2449 0.3259 -0.0155 0.0650 -0.0070 63 SER B O 2138 C CB . SER B 65 ? 0.1187 0.1899 0.2558 -0.0287 0.0680 -0.0093 63 SER B CB 2139 O OG . SER B 65 ? 0.1162 0.1952 0.2607 -0.0316 0.0538 -0.0096 63 SER B OG 2140 N N . GLN B 66 ? 0.0980 0.1805 0.2445 -0.0121 0.0500 -0.0091 64 GLN B N 2141 C CA . GLN B 66 ? 0.0848 0.1823 0.2507 -0.0072 0.0417 -0.0058 64 GLN B CA 2142 C C . GLN B 66 ? 0.0867 0.1796 0.2539 0.0016 0.0471 -0.0051 64 GLN B C 2143 O O . GLN B 66 ? 0.1000 0.1817 0.2507 0.0043 0.0430 -0.0060 64 GLN B O 2144 C CB . GLN B 66 ? 0.1058 0.2041 0.2618 -0.0091 0.0267 -0.0054 64 GLN B CB 2145 C CG . GLN B 66 ? 0.0788 0.1791 0.2328 -0.0181 0.0215 -0.0075 64 GLN B CG 2146 C CD . GLN B 66 ? 0.1513 0.2501 0.2925 -0.0194 0.0083 -0.0085 64 GLN B CD 2147 O OE1 . GLN B 66 ? 0.1677 0.2740 0.3118 -0.0144 0.0004 -0.0058 64 GLN B OE1 2148 N NE2 . GLN B 66 ? 0.1503 0.2385 0.2767 -0.0256 0.0066 -0.0118 64 GLN B NE2 2149 N N . LYS B 67 ? 0.1241 0.2253 0.3127 0.0058 0.0570 -0.0038 65 LYS B N 2150 C CA . LYS B 67 ? 0.1791 0.2717 0.3668 0.0138 0.0636 -0.0041 65 LYS B CA 2151 C C . LYS B 67 ? 0.1231 0.2187 0.3155 0.0199 0.0536 0.0005 65 LYS B C 2152 O O . LYS B 67 ? 0.1227 0.2053 0.3064 0.0244 0.0568 -0.0009 65 LYS B O 2153 C CB . LYS B 67 ? 0.1356 0.2327 0.3374 0.0169 0.0724 -0.0029 65 LYS B CB 2154 C CG . LYS B 67 ? 0.2922 0.4096 0.5179 0.0182 0.0645 0.0031 65 LYS B CG 2155 C CD . LYS B 67 ? 0.3014 0.4242 0.5418 0.0195 0.0746 0.0035 65 LYS B CD 2156 C CE . LYS B 67 ? 0.2949 0.4400 0.5595 0.0195 0.0661 0.0087 65 LYS B CE 2157 N NZ . LYS B 67 ? 0.2705 0.4220 0.5515 0.0204 0.0765 0.0091 65 LYS B NZ 2158 N N . ASP B 68 ? 0.1140 0.2257 0.3181 0.0197 0.0414 0.0060 66 ASP B N 2159 C CA . ASP B 68 ? 0.1264 0.2412 0.3317 0.0255 0.0315 0.0117 66 ASP B CA 2160 C C . ASP B 68 ? 0.0966 0.1988 0.2813 0.0241 0.0269 0.0099 66 ASP B C 2161 O O . ASP B 68 ? 0.1031 0.1969 0.2840 0.0298 0.0271 0.0125 66 ASP B O 2162 C CB . ASP B 68 ? 0.1787 0.3135 0.3956 0.0247 0.0185 0.0169 66 ASP B CB 2163 C CG . ASP B 68 ? 0.2284 0.3706 0.4416 0.0152 0.0113 0.0133 66 ASP B CG 2164 O OD1 . ASP B 68 ? 0.1744 0.3084 0.3814 0.0090 0.0185 0.0078 66 ASP B OD1 2165 O OD2 . ASP B 68 ? 0.2693 0.4246 0.4846 0.0137 -0.0014 0.0156 66 ASP B OD2 2166 N N . LEU B 69 ? 0.0771 0.1746 0.2440 0.0160 0.0227 0.0054 67 LEU B N 2167 C CA . LEU B 69 ? 0.0745 0.1576 0.2162 0.0136 0.0181 0.0028 67 LEU B CA 2168 C C . LEU B 69 ? 0.0846 0.1500 0.2144 0.0155 0.0274 -0.0015 67 LEU B C 2169 O O . LEU B 69 ? 0.0876 0.1441 0.2083 0.0180 0.0252 -0.0009 67 LEU B O 2170 C CB . LEU B 69 ? 0.0728 0.1535 0.2004 0.0052 0.0140 -0.0015 67 LEU B CB 2171 C CG . LEU B 69 ? 0.0728 0.1379 0.1755 0.0030 0.0115 -0.0047 67 LEU B CG 2172 C CD1 . LEU B 69 ? 0.1745 0.2414 0.2723 0.0059 0.0022 -0.0011 67 LEU B CD1 2173 C CD2 . LEU B 69 ? 0.1058 0.1671 0.1975 -0.0043 0.0100 -0.0083 67 LEU B CD2 2174 N N . LEU B 70 ? 0.0863 0.1466 0.2158 0.0140 0.0383 -0.0061 68 LEU B N 2175 C CA . LEU B 70 ? 0.0979 0.1416 0.2141 0.0150 0.0467 -0.0119 68 LEU B CA 2176 C C . LEU B 70 ? 0.0988 0.1391 0.2270 0.0224 0.0509 -0.0102 68 LEU B C 2177 O O . LEU B 70 ? 0.1068 0.1338 0.2239 0.0230 0.0517 -0.0135 68 LEU B O 2178 C CB . LEU B 70 ? 0.1112 0.1505 0.2230 0.0124 0.0584 -0.0170 68 LEU B CB 2179 C CG . LEU B 70 ? 0.1053 0.1415 0.1997 0.0051 0.0567 -0.0189 68 LEU B CG 2180 C CD1 . LEU B 70 ? 0.1931 0.2239 0.2817 0.0037 0.0700 -0.0229 68 LEU B CD1 2181 C CD2 . LEU B 70 ? 0.1450 0.1699 0.2162 0.0025 0.0489 -0.0212 68 LEU B CD2 2182 N N . GLU B 71 ? 0.0983 0.1506 0.2510 0.0281 0.0534 -0.0047 69 GLU B N 2183 C CA . GLU B 71 ? 0.1047 0.1518 0.2683 0.0355 0.0572 -0.0018 69 GLU B CA 2184 C C . GLU B 71 ? 0.0995 0.1456 0.2612 0.0382 0.0480 0.0043 69 GLU B C 2185 O O . GLU B 71 ? 0.1135 0.1467 0.2727 0.0411 0.0511 0.0042 69 GLU B O 2186 C CB . GLU B 71 ? 0.1708 0.2274 0.3530 0.0399 0.0598 0.0033 69 GLU B CB 2187 C CG . GLU B 71 ? 0.1975 0.2502 0.3796 0.0380 0.0718 -0.0030 69 GLU B CG 2188 C CD . GLU B 71 ? 0.2427 0.2748 0.4100 0.0376 0.0820 -0.0116 69 GLU B CD 2189 O OE1 . GLU B 71 ? 0.2797 0.3007 0.4430 0.0397 0.0810 -0.0120 69 GLU B OE1 2190 O OE2 . GLU B 71 ? 0.2391 0.2662 0.3978 0.0345 0.0908 -0.0181 69 GLU B OE2 2191 N N . GLN B 72 ? 0.0905 0.1477 0.2478 0.0355 0.0359 0.0089 70 GLN B N 2192 C CA A GLN B 72 ? 0.1149 0.1698 0.2639 0.0367 0.0273 0.0142 70 GLN B CA 2193 C CA B GLN B 72 ? 0.1195 0.1745 0.2685 0.0367 0.0272 0.0142 70 GLN B CA 2194 C C . GLN B 72 ? 0.0903 0.1275 0.2192 0.0325 0.0293 0.0075 70 GLN B C 2195 O O . GLN B 72 ? 0.1134 0.1415 0.2418 0.0354 0.0305 0.0098 70 GLN B O 2196 C CB A GLN B 72 ? 0.1117 0.1804 0.2554 0.0334 0.0147 0.0178 70 GLN B CB 2197 C CB B GLN B 72 ? 0.1189 0.1878 0.2627 0.0332 0.0149 0.0175 70 GLN B CB 2198 C CG A GLN B 72 ? 0.1186 0.2068 0.2819 0.0384 0.0087 0.0265 70 GLN B CG 2199 C CG B GLN B 72 ? 0.1148 0.1842 0.2505 0.0354 0.0064 0.0241 70 GLN B CG 2200 C CD A GLN B 72 ? 0.1827 0.2687 0.3511 0.0463 0.0081 0.0354 70 GLN B CD 2201 C CD B GLN B 72 ? 0.2501 0.3298 0.4030 0.0441 0.0040 0.0353 70 GLN B CD 2202 O OE1 A GLN B 72 ? 0.2419 0.3186 0.4001 0.0477 0.0070 0.0382 70 GLN B OE1 2203 O OE1 B GLN B 72 ? 0.2981 0.3674 0.4553 0.0492 0.0103 0.0386 70 GLN B OE1 2204 N NE2 A GLN B 72 ? 0.1853 0.2783 0.3677 0.0508 0.0093 0.0397 70 GLN B NE2 2205 N NE2 B GLN B 72 ? 0.2904 0.3874 0.4474 0.0442 -0.0057 0.0397 70 GLN B NE2 2206 N N . ARG B 73 ? 0.0885 0.1213 0.2019 0.0257 0.0294 -0.0001 71 ARG B N 2207 C CA . ARG B 73 ? 0.1027 0.1217 0.1976 0.0214 0.0295 -0.0064 71 ARG B CA 2208 C C . ARG B 73 ? 0.1012 0.1065 0.1973 0.0228 0.0392 -0.0123 71 ARG B C 2209 O O . ARG B 73 ? 0.1284 0.1236 0.2176 0.0215 0.0386 -0.0148 71 ARG B O 2210 C CB . ARG B 73 ? 0.1118 0.1301 0.1907 0.0148 0.0273 -0.0117 71 ARG B CB 2211 C CG . ARG B 73 ? 0.0853 0.1136 0.1611 0.0123 0.0179 -0.0078 71 ARG B CG 2212 C CD . ARG B 73 ? 0.1446 0.1716 0.2136 0.0129 0.0107 -0.0045 71 ARG B CD 2213 N NE . ARG B 73 ? 0.2042 0.2397 0.2688 0.0105 0.0025 -0.0024 71 ARG B NE 2214 C CZ . ARG B 73 ? 0.1700 0.2169 0.2422 0.0130 -0.0032 0.0034 71 ARG B CZ 2215 N NH1 . ARG B 73 ? 0.1823 0.2341 0.2680 0.0190 -0.0019 0.0095 71 ARG B NH1 2216 N NH2 . ARG B 73 ? 0.2853 0.3383 0.3511 0.0098 -0.0104 0.0031 71 ARG B NH2 2217 N N . ARG B 74 ? 0.1082 0.1132 0.2140 0.0253 0.0485 -0.0151 72 ARG B N 2218 C CA . ARG B 74 ? 0.1215 0.1124 0.2282 0.0267 0.0588 -0.0223 72 ARG B CA 2219 C C . ARG B 74 ? 0.1255 0.1108 0.2469 0.0324 0.0608 -0.0174 72 ARG B C 2220 O O . ARG B 74 ? 0.1428 0.1142 0.2598 0.0306 0.0654 -0.0231 72 ARG B O 2221 C CB . ARG B 74 ? 0.1298 0.1222 0.2445 0.0288 0.0699 -0.0261 72 ARG B CB 2222 C CG . ARG B 74 ? 0.1323 0.1244 0.2287 0.0227 0.0714 -0.0326 72 ARG B CG 2223 C CD . ARG B 74 ? 0.1692 0.1672 0.2747 0.0243 0.0812 -0.0331 72 ARG B CD 2224 N NE . ARG B 74 ? 0.1733 0.1717 0.2616 0.0186 0.0827 -0.0370 72 ARG B NE 2225 C CZ . ARG B 74 ? 0.1630 0.1669 0.2551 0.0181 0.0907 -0.0369 72 ARG B CZ 2226 N NH1 . ARG B 74 ? 0.1870 0.1969 0.2983 0.0224 0.0954 -0.0330 72 ARG B NH1 2227 N NH2 . ARG B 74 ? 0.2319 0.2345 0.3067 0.0127 0.0922 -0.0391 72 ARG B NH2 2228 N N . ALA B 75 ? 0.1184 0.1152 0.2538 0.0376 0.0555 -0.0058 73 ALA B N 2229 C CA . ALA B 75 ? 0.1257 0.1177 0.2696 0.0418 0.0555 0.0019 73 ALA B CA 2230 C C . ALA B 75 ? 0.1210 0.1091 0.2588 0.0408 0.0496 0.0057 73 ALA B C 2231 O O . ALA B 75 ? 0.1546 0.1365 0.2973 0.0430 0.0508 0.0117 73 ALA B O 2232 C CB . ALA B 75 ? 0.1257 0.1316 0.2847 0.0479 0.0524 0.0131 73 ALA B CB 2233 N N . ALA B 76 ? 0.1326 0.1246 0.2547 0.0351 0.0423 0.0025 74 ALA B N 2234 C CA . ALA B 76 ? 0.1073 0.0989 0.2206 0.0331 0.0353 0.0070 74 ALA B CA 2235 C C . ALA B 76 ? 0.1156 0.0918 0.2296 0.0315 0.0402 0.0041 74 ALA B C 2236 O O . ALA B 76 ? 0.1262 0.1013 0.2426 0.0332 0.0385 0.0120 74 ALA B O 2237 C CB . ALA B 76 ? 0.1003 0.0973 0.1956 0.0265 0.0275 0.0026 74 ALA B CB 2238 N N . VAL B 77 ? 0.1238 0.0883 0.2355 0.0277 0.0466 -0.0073 75 VAL B N 2239 C CA . VAL B 77 ? 0.1332 0.0831 0.2475 0.0249 0.0511 -0.0118 75 VAL B CA 2240 C C . VAL B 77 ? 0.1447 0.0920 0.2724 0.0294 0.0549 -0.0016 75 VAL B C 2241 O O . VAL B 77 ? 0.1469 0.0875 0.2771 0.0273 0.0560 0.0007 75 VAL B O 2242 C CB . VAL B 77 ? 0.1555 0.0957 0.2622 0.0190 0.0559 -0.0259 75 VAL B CB 2243 C CG1 . VAL B 77 ? 0.1401 0.0816 0.2293 0.0126 0.0505 -0.0356 75 VAL B CG1 2244 C CG2 . VAL B 77 ? 0.1530 0.0940 0.2645 0.0224 0.0626 -0.0273 75 VAL B CG2 2245 N N . ASP B 78 ? 0.1467 0.1000 0.2836 0.0355 0.0572 0.0050 76 ASP B N 2246 C CA . ASP B 78 ? 0.1573 0.1092 0.3064 0.0405 0.0603 0.0159 76 ASP B CA 2247 C C . ASP B 78 ? 0.1508 0.1147 0.3010 0.0458 0.0533 0.0305 76 ASP B C 2248 O O . ASP B 78 ? 0.1843 0.1448 0.3363 0.0470 0.0539 0.0388 76 ASP B O 2249 C CB . ASP B 78 ? 0.1644 0.1169 0.3238 0.0446 0.0663 0.0157 76 ASP B CB 2250 C CG . ASP B 78 ? 0.2842 0.2238 0.4422 0.0400 0.0746 0.0023 76 ASP B CG 2251 O OD1 . ASP B 78 ? 0.2345 0.1633 0.3882 0.0344 0.0765 -0.0044 76 ASP B OD1 2252 O OD2 . ASP B 78 ? 0.2533 0.1944 0.4144 0.0418 0.0790 -0.0015 76 ASP B OD2 2253 N N . THR B 79 ? 0.1387 0.1172 0.2873 0.0487 0.0469 0.0336 77 THR B N 2254 C CA . THR B 79 ? 0.1365 0.1288 0.2850 0.0537 0.0392 0.0466 77 THR B CA 2255 C C . THR B 79 ? 0.1286 0.1243 0.2646 0.0517 0.0325 0.0498 77 THR B C 2256 O O . THR B 79 ? 0.1605 0.1648 0.2926 0.0550 0.0270 0.0604 77 THR B O 2257 C CB . THR B 79 ? 0.1440 0.1528 0.2960 0.0562 0.0336 0.0476 77 THR B CB 2258 O OG1 . THR B 79 ? 0.1682 0.1813 0.3127 0.0516 0.0305 0.0388 77 THR B OG1 2259 C CG2 . THR B 79 ? 0.1591 0.1661 0.3246 0.0588 0.0407 0.0453 77 THR B CG2 2260 N N . TYR B 80 ? 0.1210 0.1100 0.2500 0.0462 0.0332 0.0402 78 TYR B N 2261 C CA . TYR B 80 ? 0.1221 0.1148 0.2359 0.0421 0.0268 0.0408 78 TYR B CA 2262 C C . TYR B 80 ? 0.1499 0.1287 0.2626 0.0376 0.0320 0.0372 78 TYR B C 2263 O O . TYR B 80 ? 0.1422 0.1188 0.2549 0.0392 0.0331 0.0459 78 TYR B O 2264 C CB . TYR B 80 ? 0.1106 0.1112 0.2115 0.0363 0.0205 0.0314 78 TYR B CB 2265 C CG . TYR B 80 ? 0.0978 0.1012 0.1825 0.0315 0.0146 0.0297 78 TYR B CG 2266 C CD1 . TYR B 80 ? 0.1050 0.1169 0.1828 0.0341 0.0093 0.0384 78 TYR B CD1 2267 C CD2 . TYR B 80 ? 0.0951 0.0933 0.1709 0.0248 0.0143 0.0192 78 TYR B CD2 2268 C CE1 . TYR B 80 ? 0.1047 0.1184 0.1680 0.0301 0.0053 0.0359 78 TYR B CE1 2269 C CE2 . TYR B 80 ? 0.0925 0.0934 0.1559 0.0213 0.0096 0.0178 78 TYR B CE2 2270 C CZ . TYR B 80 ? 0.0894 0.0975 0.1470 0.0240 0.0058 0.0258 78 TYR B CZ 2271 O OH . TYR B 80 ? 0.1087 0.1187 0.1545 0.0210 0.0026 0.0236 78 TYR B OH 2272 N N . CYS B 81 ? 0.1209 0.0906 0.2328 0.0317 0.0354 0.0244 79 CYS B N 2273 C CA . CYS B 81 ? 0.1235 0.0820 0.2360 0.0260 0.0390 0.0190 79 CYS B CA 2274 C C . CYS B 81 ? 0.1525 0.0992 0.2797 0.0284 0.0474 0.0251 79 CYS B C 2275 O O . CYS B 81 ? 0.1636 0.1081 0.2920 0.0273 0.0487 0.0314 79 CYS B O 2276 C CB . CYS B 81 ? 0.1525 0.1053 0.2598 0.0191 0.0395 0.0035 79 CYS B CB 2277 S SG . CYS B 81 ? 0.1447 0.1094 0.2333 0.0153 0.0303 -0.0028 79 CYS B SG 2278 N N . ARG B 82 ? 0.1464 0.0886 0.2814 0.0298 0.0528 0.0225 80 ARG B N 2279 C CA . ARG B 82 ? 0.1614 0.0954 0.3073 0.0302 0.0601 0.0270 80 ARG B CA 2280 C C . ARG B 82 ? 0.1650 0.1052 0.3133 0.0368 0.0594 0.0438 80 ARG B C 2281 O O . ARG B 82 ? 0.1894 0.1243 0.3429 0.0361 0.0640 0.0497 80 ARG B O 2282 C CB . ARG B 82 ? 0.1724 0.1004 0.3263 0.0313 0.0664 0.0213 80 ARG B CB 2283 C CG . ARG B 82 ? 0.1933 0.1128 0.3435 0.0236 0.0688 0.0045 80 ARG B CG 2284 C CD . ARG B 82 ? 0.2053 0.1183 0.3620 0.0249 0.0760 -0.0011 80 ARG B CD 2285 N NE . ARG B 82 ? 0.2474 0.1520 0.3985 0.0173 0.0781 -0.0168 80 ARG B NE 2286 C CZ . ARG B 82 ? 0.2237 0.1296 0.3625 0.0141 0.0759 -0.0281 80 ARG B CZ 2287 N NH1 . ARG B 82 ? 0.2691 0.1682 0.4012 0.0072 0.0769 -0.0415 80 ARG B NH1 2288 N NH2 . ARG B 82 ? 0.2048 0.1197 0.3376 0.0177 0.0725 -0.0259 80 ARG B NH2 2289 N N . HIS B 83 ? 0.1682 0.1206 0.3121 0.0428 0.0534 0.0513 81 HIS B N 2290 C CA . HIS B 83 ? 0.1661 0.1266 0.3083 0.0488 0.0509 0.0667 81 HIS B CA 2291 C C . HIS B 83 ? 0.1630 0.1240 0.2961 0.0466 0.0494 0.0717 81 HIS B C 2292 O O . HIS B 83 ? 0.1824 0.1405 0.3180 0.0483 0.0538 0.0810 81 HIS B O 2293 C CB . HIS B 83 ? 0.1584 0.1347 0.2957 0.0541 0.0424 0.0719 81 HIS B CB 2294 C CG . HIS B 83 ? 0.1666 0.1523 0.2984 0.0595 0.0382 0.0863 81 HIS B CG 2295 N ND1 . HIS B 83 ? 0.1813 0.1684 0.3217 0.0654 0.0406 0.0960 81 HIS B ND1 2296 C CD2 . HIS B 83 ? 0.1648 0.1584 0.2822 0.0598 0.0323 0.0921 81 HIS B CD2 2297 C CE1 . HIS B 83 ? 0.2467 0.2428 0.3775 0.0691 0.0356 0.1072 81 HIS B CE1 2298 N NE2 . HIS B 83 ? 0.2085 0.2084 0.3245 0.0656 0.0307 0.1046 81 HIS B NE2 2299 N N . ASN B 84 ? 0.1497 0.1146 0.2726 0.0433 0.0439 0.0659 82 ASN B N 2300 C CA . ASN B 84 ? 0.1485 0.1151 0.2622 0.0417 0.0427 0.0708 82 ASN B CA 2301 C C . ASN B 84 ? 0.1550 0.1096 0.2769 0.0360 0.0507 0.0678 82 ASN B C 2302 O O . ASN B 84 ? 0.1615 0.1163 0.2809 0.0361 0.0536 0.0758 82 ASN B O 2303 C CB . ASN B 84 ? 0.1340 0.1093 0.2340 0.0384 0.0347 0.0635 82 ASN B CB 2304 C CG . ASN B 84 ? 0.1305 0.1208 0.2200 0.0431 0.0260 0.0685 82 ASN B CG 2305 O OD1 . ASN B 84 ? 0.1716 0.1669 0.2624 0.0497 0.0252 0.0801 82 ASN B OD1 2306 N ND2 . ASN B 84 ? 0.1476 0.1460 0.2261 0.0388 0.0190 0.0588 82 ASN B ND2 2307 N N . TYR B 85 ? 0.1895 0.1346 0.3209 0.0307 0.0543 0.0557 83 TYR B N 2308 C CA . TYR B 85 ? 0.1630 0.0986 0.3042 0.0243 0.0610 0.0510 83 TYR B CA 2309 C C . TYR B 85 ? 0.1791 0.1116 0.3288 0.0284 0.0682 0.0627 83 TYR B C 2310 O O . TYR B 85 ? 0.1890 0.1194 0.3423 0.0264 0.0728 0.0674 83 TYR B O 2311 C CB . TYR B 85 ? 0.1644 0.0921 0.3120 0.0185 0.0627 0.0353 83 TYR B CB 2312 C CG . TYR B 85 ? 0.1885 0.1088 0.3452 0.0105 0.0671 0.0272 83 TYR B CG 2313 C CD1 . TYR B 85 ? 0.2136 0.1356 0.3669 0.0028 0.0625 0.0163 83 TYR B CD1 2314 C CD2 . TYR B 85 ? 0.2210 0.1339 0.3905 0.0107 0.0751 0.0302 83 TYR B CD2 2315 C CE1 . TYR B 85 ? 0.2221 0.1403 0.3845 -0.0046 0.0649 0.0085 83 TYR B CE1 2316 C CE2 . TYR B 85 ? 0.2548 0.1619 0.4336 0.0033 0.0786 0.0221 83 TYR B CE2 2317 C CZ . TYR B 85 ? 0.2606 0.1711 0.4357 -0.0043 0.0730 0.0112 83 TYR B CZ 2318 O OH . TYR B 85 ? 0.2941 0.2009 0.4793 -0.0118 0.0752 0.0032 83 TYR B OH 2319 N N . GLY B 86 ? 0.1992 0.1319 0.3528 0.0344 0.0695 0.0676 84 GLY B N 2320 C CA . GLY B 86 ? 0.2035 0.1332 0.3655 0.0391 0.0761 0.0793 84 GLY B CA 2321 C C . GLY B 86 ? 0.2076 0.1449 0.3601 0.0435 0.0747 0.0936 84 GLY B C 2322 O O . GLY B 86 ? 0.2466 0.1796 0.4048 0.0445 0.0816 0.1016 84 GLY B O 2323 N N . VAL B 87 ? 0.1968 0.1455 0.3340 0.0460 0.0661 0.0963 85 VAL B N 2324 C CA . VAL B 87 ? 0.2027 0.1600 0.3267 0.0502 0.0638 0.1087 85 VAL B CA 2325 C C . VAL B 87 ? 0.2036 0.1578 0.3251 0.0455 0.0685 0.1088 85 VAL B C 2326 O O . VAL B 87 ? 0.2175 0.1723 0.3359 0.0482 0.0730 0.1194 85 VAL B O 2327 C CB . VAL B 87 ? 0.1921 0.1630 0.2995 0.0532 0.0527 0.1092 85 VAL B CB 2328 C CG1 . VAL B 87 ? 0.2329 0.2126 0.3231 0.0563 0.0501 0.1193 85 VAL B CG1 2329 C CG2 . VAL B 87 ? 0.2352 0.2118 0.3470 0.0584 0.0482 0.1109 85 VAL B CG2 2330 N N . VAL B 88 ? 0.1904 0.1414 0.3139 0.0384 0.0677 0.0971 86 VAL B N 2331 C CA . VAL B 88 ? 0.1897 0.1404 0.3111 0.0338 0.0711 0.0969 86 VAL B CA 2332 C C . VAL B 88 ? 0.2078 0.1488 0.3472 0.0267 0.0788 0.0900 86 VAL B C 2333 O O . VAL B 88 ? 0.1961 0.1379 0.3371 0.0231 0.0826 0.0907 86 VAL B O 2334 C CB . VAL B 88 ? 0.1731 0.1299 0.2830 0.0305 0.0642 0.0901 86 VAL B CB 2335 C CG1 . VAL B 88 ? 0.2257 0.1933 0.3172 0.0370 0.0556 0.0955 86 VAL B CG1 2336 C CG2 . VAL B 88 ? 0.1610 0.1121 0.2802 0.0239 0.0615 0.0750 86 VAL B CG2 2337 N N . GLU B 89 ? 0.2323 0.1650 0.3854 0.0248 0.0814 0.0831 87 GLU B N 2338 C CA A GLU B 89 ? 0.2029 0.1275 0.3717 0.0170 0.0865 0.0732 87 GLU B CA 2339 C CA B GLU B 89 ? 0.2569 0.1814 0.4261 0.0171 0.0867 0.0733 87 GLU B CA 2340 C C . GLU B 89 ? 0.2218 0.1437 0.3991 0.0164 0.0951 0.0812 87 GLU B C 2341 O O . GLU B 89 ? 0.2259 0.1465 0.4122 0.0093 0.0973 0.0743 87 GLU B O 2342 C CB A GLU B 89 ? 0.2798 0.1957 0.4594 0.0155 0.0884 0.0642 87 GLU B CB 2343 C CB B GLU B 89 ? 0.2792 0.1948 0.4593 0.0164 0.0892 0.0658 87 GLU B CB 2344 C CG A GLU B 89 ? 0.3142 0.2262 0.4986 0.0230 0.0937 0.0748 87 GLU B CG 2345 C CG B GLU B 89 ? 0.3385 0.2510 0.5226 0.0243 0.0944 0.0779 87 GLU B CG 2346 C CD A GLU B 89 ? 0.3327 0.2354 0.5328 0.0215 0.1037 0.0780 87 GLU B CD 2347 C CD B GLU B 89 ? 0.3974 0.3003 0.5936 0.0234 0.0984 0.0701 87 GLU B CD 2348 O OE1 A GLU B 89 ? 0.3009 0.2005 0.5056 0.0281 0.1090 0.0894 87 GLU B OE1 2349 O OE1 B GLU B 89 ? 0.4035 0.3012 0.6051 0.0159 0.0982 0.0551 87 GLU B OE1 2350 O OE2 A GLU B 89 ? 0.3568 0.2556 0.5655 0.0137 0.1061 0.0692 87 GLU B OE2 2351 O OE2 B GLU B 89 ? 0.3854 0.2866 0.5850 0.0303 0.1015 0.0789 87 GLU B OE2 2352 N N . SER B 90 ? 0.2313 0.1534 0.4057 0.0239 0.0996 0.0959 88 SER B N 2353 C CA . SER B 90 ? 0.2594 0.1775 0.4419 0.0242 0.1089 0.1047 88 SER B CA 2354 C C . SER B 90 ? 0.2849 0.2091 0.4621 0.0212 0.1100 0.1064 88 SER B C 2355 O O . SER B 90 ? 0.2996 0.2198 0.4884 0.0179 0.1177 0.1081 88 SER B O 2356 C CB . SER B 90 ? 0.2662 0.1841 0.4439 0.0336 0.1126 0.1210 88 SER B CB 2357 O OG . SER B 90 ? 0.3242 0.2527 0.4811 0.0391 0.1078 0.1305 88 SER B OG 2358 N N . PHE B 91 ? 0.2310 0.1647 0.3915 0.0221 0.1028 0.1058 89 PHE B N 2359 C CA . PHE B 91 ? 0.2483 0.1885 0.4029 0.0198 0.1045 0.1073 89 PHE B CA 2360 C C . PHE B 91 ? 0.2214 0.1666 0.3770 0.0128 0.0984 0.0943 89 PHE B C 2361 O O . PHE B 91 ? 0.2192 0.1714 0.3697 0.0111 0.0991 0.0946 89 PHE B O 2362 C CB . PHE B 91 ? 0.2352 0.1831 0.3674 0.0275 0.1037 0.1200 89 PHE B CB 2363 C CG . PHE B 91 ? 0.2247 0.1790 0.3394 0.0320 0.0938 0.1200 89 PHE B CG 2364 C CD1 . PHE B 91 ? 0.2351 0.1967 0.3382 0.0299 0.0873 0.1135 89 PHE B CD1 2365 C CD2 . PHE B 91 ? 0.3321 0.2860 0.4428 0.0386 0.0911 0.1268 89 PHE B CD2 2366 C CE1 . PHE B 91 ? 0.2846 0.2522 0.3720 0.0339 0.0780 0.1133 89 PHE B CE1 2367 C CE2 . PHE B 91 ? 0.3348 0.2961 0.4309 0.0425 0.0813 0.1263 89 PHE B CE2 2368 C CZ . PHE B 91 ? 0.2657 0.2336 0.3501 0.0401 0.0746 0.1194 89 PHE B CZ 2369 N N . THR B 92 ? 0.1490 0.1737 0.3617 0.0043 0.0416 0.0346 90 THR B N 2370 C CA . THR B 92 ? 0.1425 0.1682 0.3318 -0.0018 0.0496 0.0290 90 THR B CA 2371 C C . THR B 92 ? 0.1389 0.1700 0.3393 -0.0003 0.0574 0.0169 90 THR B C 2372 O O . THR B 92 ? 0.1414 0.1624 0.3303 0.0006 0.0592 0.0182 90 THR B O 2373 C CB . THR B 92 ? 0.1436 0.1817 0.3285 -0.0092 0.0512 0.0255 90 THR B CB 2374 O OG1 . THR B 92 ? 0.1409 0.1987 0.3573 -0.0078 0.0540 0.0160 90 THR B OG1 2375 C CG2 . THR B 92 ? 0.1652 0.1952 0.3368 -0.0113 0.0413 0.0365 90 THR B CG2 2376 N N . VAL B 93 ? 0.1377 0.1860 0.3617 0.0007 0.0615 0.0042 91 VAL B N 2377 C CA . VAL B 93 ? 0.1376 0.1928 0.3740 0.0037 0.0679 -0.0106 91 VAL B CA 2378 C C . VAL B 93 ? 0.1465 0.1868 0.3965 0.0104 0.0625 -0.0087 91 VAL B C 2379 O O . VAL B 93 ? 0.1609 0.1961 0.4052 0.0106 0.0654 -0.0143 91 VAL B O 2380 C CB . VAL B 93 ? 0.1386 0.2166 0.4037 0.0069 0.0718 -0.0253 91 VAL B CB 2381 C CG1 . VAL B 93 ? 0.1524 0.2363 0.4309 0.0124 0.0768 -0.0432 91 VAL B CG1 2382 C CG2 . VAL B 93 ? 0.1389 0.2356 0.3921 -0.0016 0.0784 -0.0263 91 VAL B CG2 2383 N N . GLN B 94 ? 0.1421 0.1755 0.4102 0.0151 0.0537 0.0009 92 GLN B N 2384 C CA . GLN B 94 ? 0.1423 0.1627 0.4287 0.0203 0.0470 0.0053 92 GLN B CA 2385 C C . GLN B 94 ? 0.2094 0.2147 0.4745 0.0180 0.0441 0.0236 92 GLN B C 2386 O O . GLN B 94 ? 0.1652 0.1608 0.4444 0.0206 0.0385 0.0314 92 GLN B O 2387 C CB . GLN B 94 ? 0.1461 0.1677 0.4672 0.0267 0.0378 0.0069 92 GLN B CB 2388 C CG . GLN B 94 ? 0.1475 0.1855 0.4955 0.0314 0.0404 -0.0131 92 GLN B CG 2389 C CD . GLN B 94 ? 0.4434 0.4792 0.8157 0.0354 0.0289 -0.0108 92 GLN B CD 2390 O OE1 . GLN B 94 ? 0.5174 0.5402 0.8937 0.0354 0.0190 0.0060 92 GLN B OE1 2391 N NE2 . GLN B 94 ? 0.4502 0.5001 0.8371 0.0383 0.0303 -0.0271 92 GLN B NE2 2392 N N . ARG B 95 ? 0.1620 0.1663 0.3946 0.0133 0.0475 0.0303 93 ARG B N 2393 C CA . ARG B 95 ? 0.1534 0.1468 0.3642 0.0126 0.0458 0.0457 93 ARG B CA 2394 C C . ARG B 95 ? 0.1654 0.1536 0.3731 0.0119 0.0495 0.0441 93 ARG B C 2395 O O . ARG B 95 ? 0.1426 0.1338 0.3415 0.0092 0.0554 0.0323 93 ARG B O 2396 C CB . ARG B 95 ? 0.1842 0.1768 0.3620 0.0090 0.0474 0.0498 93 ARG B CB 2397 C CG . ARG B 95 ? 0.1485 0.1324 0.3016 0.0101 0.0466 0.0629 93 ARG B CG 2398 C CD . ARG B 95 ? 0.1527 0.1338 0.2750 0.0079 0.0460 0.0637 93 ARG B CD 2399 N NE . ARG B 95 ? 0.1580 0.1324 0.2555 0.0105 0.0465 0.0721 93 ARG B NE 2400 C CZ . ARG B 95 ? 0.1734 0.1462 0.2634 0.0151 0.0426 0.0843 93 ARG B CZ 2401 N NH1 . ARG B 95 ? 0.1914 0.1665 0.2964 0.0166 0.0366 0.0908 93 ARG B NH1 2402 N NH2 . ARG B 95 ? 0.2138 0.1841 0.2811 0.0185 0.0446 0.0899 93 ARG B NH2 2403 N N . ARG B 96 ? 0.1447 0.1263 0.3602 0.0138 0.0455 0.0573 94 ARG B N 2404 C CA . ARG B 96 ? 0.1688 0.1460 0.3855 0.0128 0.0474 0.0587 94 ARG B CA 2405 C C . ARG B 96 ? 0.1831 0.1577 0.3883 0.0131 0.0465 0.0785 94 ARG B C 2406 O O . ARG B 96 ? 0.2208 0.1987 0.4354 0.0143 0.0400 0.0893 94 ARG B O 2407 C CB . ARG B 96 ? 0.2365 0.2107 0.4893 0.0147 0.0421 0.0530 94 ARG B CB 2408 C CG . ARG B 96 ? 0.2821 0.2614 0.5493 0.0164 0.0433 0.0313 94 ARG B CG 2409 C CD . ARG B 96 ? 0.1915 0.1731 0.4439 0.0137 0.0498 0.0171 94 ARG B CD 2410 N NE . ARG B 96 ? 0.2414 0.2305 0.5089 0.0163 0.0512 -0.0043 94 ARG B NE 2411 C CZ . ARG B 96 ? 0.3428 0.3446 0.6026 0.0159 0.0570 -0.0145 94 ARG B CZ 2412 N NH1 . ARG B 96 ? 0.3718 0.3839 0.6462 0.0192 0.0594 -0.0344 94 ARG B NH1 2413 N NH2 . ARG B 96 ? 0.3556 0.3609 0.5939 0.0123 0.0600 -0.0049 94 ARG B NH2 2414 N N . VAL B 97 ? 0.1461 0.1210 0.3268 0.0119 0.0519 0.0802 95 VAL B N 2415 C CA . VAL B 97 ? 0.1767 0.1579 0.3418 0.0136 0.0513 0.0928 95 VAL B CA 2416 C C . VAL B 97 ? 0.1475 0.1305 0.3134 0.0124 0.0539 0.0909 95 VAL B C 2417 O O . VAL B 97 ? 0.1436 0.1223 0.2980 0.0109 0.0585 0.0822 95 VAL B O 2418 C CB . VAL B 97 ? 0.1616 0.1426 0.2938 0.0158 0.0539 0.0957 95 VAL B CB 2419 C CG1 . VAL B 97 ? 0.1688 0.1583 0.2861 0.0190 0.0538 0.1063 95 VAL B CG1 2420 C CG2 . VAL B 97 ? 0.2134 0.1912 0.3457 0.0163 0.0504 0.0967 95 VAL B CG2 2421 N N A TYR B 98 ? 0.1625 0.1520 0.3439 0.0120 0.0502 0.0992 96 TYR B N 2422 N N B TYR B 98 ? 0.1552 0.1452 0.3349 0.0123 0.0503 0.1001 96 TYR B N 2423 C CA A TYR B 98 ? 0.1481 0.1391 0.3354 0.0105 0.0513 0.0974 96 TYR B CA 2424 C CA B TYR B 98 ? 0.1743 0.1677 0.3597 0.0110 0.0511 0.1009 96 TYR B CA 2425 C C A TYR B 98 ? 0.1721 0.1694 0.3351 0.0129 0.0563 0.1022 96 TYR B C 2426 C C B TYR B 98 ? 0.1895 0.1860 0.3478 0.0133 0.0571 0.1012 96 TYR B C 2427 O O A TYR B 98 ? 0.1540 0.1576 0.3008 0.0161 0.0577 0.1102 96 TYR B O 2428 O O B TYR B 98 ? 0.1523 0.1519 0.2887 0.0166 0.0594 0.1053 96 TYR B O 2429 C CB A TYR B 98 ? 0.1521 0.1468 0.3698 0.0082 0.0443 0.1034 96 TYR B CB 2430 C CB B TYR B 98 ? 0.1560 0.1592 0.3584 0.0102 0.0464 0.1146 96 TYR B CB 2431 C CG A TYR B 98 ? 0.1599 0.1658 0.3802 0.0086 0.0417 0.1202 96 TYR B CG 2432 C CG B TYR B 98 ? 0.1613 0.1636 0.3895 0.0083 0.0384 0.1187 96 TYR B CG 2433 C CD1 A TYR B 98 ? 0.1625 0.1790 0.3753 0.0093 0.0448 0.1295 96 TYR B CD1 2434 C CD1 B TYR B 98 ? 0.1595 0.1526 0.4102 0.0068 0.0336 0.1072 96 TYR B CD1 2435 C CD2 A TYR B 98 ? 0.1665 0.1732 0.3986 0.0080 0.0359 0.1269 96 TYR B CD2 2436 C CD2 B TYR B 98 ? 0.2035 0.2144 0.4340 0.0081 0.0350 0.1337 96 TYR B CD2 2437 C CE1 A TYR B 98 ? 0.1956 0.2242 0.4111 0.0093 0.0434 0.1452 96 TYR B CE1 2438 C CE1 B TYR B 98 ? 0.1662 0.1582 0.4421 0.0057 0.0248 0.1100 96 TYR B CE1 2439 C CE2 A TYR B 98 ? 0.1943 0.2118 0.4282 0.0073 0.0334 0.1432 96 TYR B CE2 2440 C CE2 B TYR B 98 ? 0.1775 0.1870 0.4321 0.0059 0.0263 0.1383 96 TYR B CE2 2441 C CZ A TYR B 98 ? 0.1938 0.2228 0.4191 0.0079 0.0377 0.1524 96 TYR B CZ 2442 C CZ B TYR B 98 ? 0.1751 0.1747 0.4530 0.0049 0.0208 0.1263 96 TYR B CZ 2443 O OH A TYR B 98 ? 0.1916 0.2334 0.4184 0.0071 0.0364 0.1690 96 TYR B OH 2444 O OH B TYR B 98 ? 0.1838 0.1815 0.4871 0.0032 0.0109 0.1298 96 TYR B OH 2445 N N . PRO B 99 ? 0.1451 0.1404 0.3059 0.0118 0.0587 0.0964 97 PRO B N 2446 C CA . PRO B 99 ? 0.1719 0.1724 0.3128 0.0147 0.0630 0.0989 97 PRO B CA 2447 C C . PRO B 99 ? 0.1661 0.1808 0.3155 0.0167 0.0628 0.1122 97 PRO B C 2448 O O . PRO B 99 ? 0.1762 0.1949 0.3506 0.0136 0.0585 0.1184 97 PRO B O 2449 C CB . PRO B 99 ? 0.1881 0.1819 0.3320 0.0116 0.0636 0.0894 97 PRO B CB 2450 C CG . PRO B 99 ? 0.2471 0.2367 0.4190 0.0073 0.0587 0.0857 97 PRO B CG 2451 C CD . PRO B 99 ? 0.1688 0.1563 0.3474 0.0078 0.0566 0.0861 97 PRO B CD 2452 N N . GLU B 100 ? 0.1552 0.1776 0.2843 0.0219 0.0674 0.1167 98 GLU B N 2453 C CA . GLU B 100 ? 0.1810 0.2189 0.3156 0.0244 0.0695 0.1279 98 GLU B CA 2454 C C . GLU B 100 ? 0.1729 0.2105 0.3081 0.0248 0.0718 0.1235 98 GLU B C 2455 O O . GLU B 100 ? 0.2132 0.2424 0.3303 0.0268 0.0742 0.1142 98 GLU B O 2456 C CB . GLU B 100 ? 0.2661 0.3139 0.3779 0.0311 0.0739 0.1335 98 GLU B CB 2457 C CG . GLU B 100 ? 0.4677 0.5151 0.5747 0.0308 0.0714 0.1377 98 GLU B CG 2458 C CD . GLU B 100 ? 0.6644 0.7226 0.7934 0.0271 0.0681 0.1515 98 GLU B CD 2459 O OE1 . GLU B 100 ? 0.7247 0.7782 0.8613 0.0240 0.0632 0.1540 98 GLU B OE1 2460 O OE2 . GLU B 100 ? 0.6798 0.7515 0.8197 0.0272 0.0699 0.1606 98 GLU B OE2 2461 N N . VAL B 101 ? 0.1570 0.2035 0.3140 0.0225 0.0703 0.1309 99 VAL B N 2462 C CA . VAL B 101 ? 0.1534 0.2000 0.3148 0.0221 0.0714 0.1278 99 VAL B CA 2463 C C . VAL B 101 ? 0.1597 0.2252 0.3250 0.0263 0.0755 0.1393 99 VAL B C 2464 O O . VAL B 101 ? 0.1955 0.2732 0.3777 0.0246 0.0739 0.1516 99 VAL B O 2465 C CB . VAL B 101 ? 0.1513 0.1894 0.3377 0.0147 0.0647 0.1235 99 VAL B CB 2466 C CG1 . VAL B 101 ? 0.1589 0.1965 0.3490 0.0136 0.0651 0.1199 99 VAL B CG1 2467 C CG2 . VAL B 101 ? 0.1733 0.1951 0.3563 0.0113 0.0617 0.1115 99 VAL B CG2 2468 N N . THR B 102 ? 0.1600 0.2284 0.3100 0.0320 0.0807 0.1358 100 THR B N 2469 C CA . THR B 102 ? 0.1671 0.2549 0.3191 0.0375 0.0857 0.1447 100 THR B CA 2470 C C . THR B 102 ? 0.1618 0.2487 0.3218 0.0371 0.0859 0.1405 100 THR B C 2471 O O . THR B 102 ? 0.1791 0.2527 0.3273 0.0376 0.0860 0.1298 100 THR B O 2472 C CB . THR B 102 ? 0.2170 0.3124 0.3407 0.0478 0.0922 0.1433 100 THR B CB 2473 O OG1 . THR B 102 ? 0.3252 0.4220 0.4410 0.0478 0.0915 0.1473 100 THR B OG1 2474 C CG2 . THR B 102 ? 0.2830 0.4009 0.4080 0.0546 0.0981 0.1505 100 THR B CG2 2475 N N . VAL B 103 ? 0.1648 0.2665 0.3456 0.0358 0.0858 0.1498 101 VAL B N 2476 C CA . VAL B 103 ? 0.1685 0.2735 0.3586 0.0364 0.0861 0.1469 101 VAL B CA 2477 C C . VAL B 103 ? 0.2040 0.3315 0.3895 0.0454 0.0932 0.1524 101 VAL B C 2478 O O . VAL B 103 ? 0.1801 0.3248 0.3726 0.0459 0.0957 0.1641 101 VAL B O 2479 C CB . VAL B 103 ? 0.1574 0.2599 0.3792 0.0266 0.0781 0.1506 101 VAL B CB 2480 C CG1 . VAL B 103 ? 0.1954 0.3062 0.4297 0.0276 0.0779 0.1495 101 VAL B CG1 2481 C CG2 . VAL B 103 ? 0.1608 0.2412 0.3859 0.0190 0.0707 0.1407 101 VAL B CG2 2482 N N . TYR B 104 ? 0.1723 0.3008 0.3466 0.0532 0.0963 0.1433 102 TYR B N 2483 C CA . TYR B 104 ? 0.2206 0.3708 0.3927 0.0631 0.1020 0.1447 102 TYR B CA 2484 C C . TYR B 104 ? 0.2370 0.3875 0.4180 0.0672 0.0994 0.1362 102 TYR B C 2485 O O . TYR B 104 ? 0.1646 0.2976 0.3424 0.0665 0.0947 0.1268 102 TYR B O 2486 C CB . TYR B 104 ? 0.2124 0.3673 0.3539 0.0748 0.1081 0.1399 102 TYR B CB 2487 C CG . TYR B 104 ? 0.2026 0.3375 0.3195 0.0809 0.1066 0.1256 102 TYR B CG 2488 C CD1 . TYR B 104 ? 0.3100 0.4432 0.4180 0.0921 0.1058 0.1135 102 TYR B CD1 2489 C CD2 . TYR B 104 ? 0.2842 0.4010 0.3875 0.0761 0.1046 0.1238 102 TYR B CD2 2490 C CE1 . TYR B 104 ? 0.3220 0.4345 0.4076 0.0986 0.1025 0.1008 102 TYR B CE1 2491 C CE2 . TYR B 104 ? 0.3582 0.4567 0.4389 0.0812 0.1034 0.1117 102 TYR B CE2 2492 C CZ . TYR B 104 ? 0.3914 0.4853 0.4617 0.0916 0.1006 0.0998 102 TYR B CZ 2493 O OH . TYR B 104 ? 0.4190 0.4856 0.4627 0.0933 0.0917 0.0861 102 TYR B OH 2494 N N . PRO B 105 ? 0.1810 0.3528 0.3753 0.0719 0.1017 0.1397 103 PRO B N 2495 C CA . PRO B 105 ? 0.1813 0.3549 0.3868 0.0771 0.0972 0.1315 103 PRO B CA 2496 C C . PRO B 105 ? 0.2721 0.4429 0.4532 0.0932 0.0983 0.1173 103 PRO B C 2497 O O . PRO B 105 ? 0.2503 0.4273 0.4094 0.1014 0.1047 0.1150 103 PRO B O 2498 C CB . PRO B 105 ? 0.1855 0.3847 0.4152 0.0757 0.0996 0.1416 103 PRO B CB 2499 C CG . PRO B 105 ? 0.2199 0.4350 0.4382 0.0779 0.1087 0.1505 103 PRO B CG 2500 C CD . PRO B 105 ? 0.1929 0.3887 0.3969 0.0712 0.1073 0.1529 103 PRO B CD 2501 N N . ALA B 106 ? 0.1981 0.3576 0.3829 0.0981 0.0897 0.1074 104 ALA B N 2502 C CA . ALA B 106 ? 0.2417 0.3932 0.4052 0.1140 0.0865 0.0930 104 ALA B CA 2503 C C . ALA B 106 ? 0.3347 0.4865 0.5159 0.1188 0.0767 0.0877 104 ALA B C 2504 O O . ALA B 106 ? 0.2065 0.3671 0.4157 0.1097 0.0734 0.0956 104 ALA B O 2505 C CB . ALA B 106 ? 0.2599 0.3786 0.3936 0.1130 0.0801 0.0837 104 ALA B CB 2506 N N . LYS B 107 ? 0.3926 0.5330 0.5575 0.1328 0.0700 0.0743 105 LYS B N 2507 C CA . LYS B 107 ? 0.3351 0.4736 0.5149 0.1392 0.0585 0.0684 105 LYS B CA 2508 C C . LYS B 107 ? 0.4577 0.5564 0.6125 0.1386 0.0413 0.0568 105 LYS B C 2509 O O . LYS B 107 ? 0.4738 0.5539 0.5995 0.1433 0.0400 0.0486 105 LYS B O 2510 C CB . LYS B 107 ? 0.2938 0.4551 0.4769 0.1536 0.0630 0.0607 105 LYS B CB 2511 C CG . LYS B 107 ? 0.2883 0.4863 0.4910 0.1497 0.0771 0.0713 105 LYS B CG 2512 C CD . LYS B 107 ? 0.3619 0.5820 0.5661 0.1652 0.0818 0.0620 105 LYS B CD 2513 C CE . LYS B 107 ? 0.4047 0.6620 0.6289 0.1608 0.0953 0.0742 105 LYS B CE 2514 N NZ . LYS B 107 ? 0.4537 0.7347 0.6813 0.1765 0.1006 0.0644 105 LYS B NZ 2515 N N . THR B 108 ? 0.4195 0.5046 0.5845 0.1312 0.0270 0.0565 106 THR B N 2516 C CA . THR B 108 ? 0.4382 0.4872 0.5802 0.1292 0.0092 0.0474 106 THR B CA 2517 C C . THR B 108 ? 0.4522 0.5004 0.5935 0.1489 0.0020 0.0371 106 THR B C 2518 O O . THR B 108 ? 0.5269 0.5471 0.6435 0.1527 -0.0088 0.0283 106 THR B O 2519 C CB . THR B 108 ? 0.3556 0.3908 0.5063 0.1146 -0.0049 0.0511 106 THR B CB 2520 O OG1 . THR B 108 ? 0.3055 0.3641 0.4902 0.1201 -0.0069 0.0548 106 THR B OG1 2521 C CG2 . THR B 108 ? 0.3324 0.3645 0.4812 0.0963 0.0001 0.0578 106 THR B CG2 2522 N N . GLN B 109 ? 0.4735 0.5531 0.6440 0.1616 0.0077 0.0381 107 GLN B N 2523 C CA . GLN B 109 ? 0.4575 0.5419 0.6316 0.1816 0.0026 0.0261 107 GLN B CA 2524 C C . GLN B 109 ? 0.5313 0.6544 0.7190 0.1885 0.0207 0.0246 107 GLN B C 2525 O O . GLN B 109 ? 0.4628 0.6141 0.6718 0.1808 0.0319 0.0358 107 GLN B O 2526 C CB . GLN B 109 ? 0.4551 0.5341 0.6506 0.1842 -0.0146 0.0253 107 GLN B CB 2527 C CG . GLN B 109 ? 0.4119 0.4476 0.5862 0.1734 -0.0362 0.0238 107 GLN B CG 2528 C CD . GLN B 109 ? 0.4769 0.5076 0.6708 0.1755 -0.0543 0.0236 107 GLN B CD 2529 O OE1 . GLN B 109 ? 0.4102 0.4322 0.6101 0.1602 -0.0642 0.0313 107 GLN B OE1 2530 N NE2 . GLN B 109 ? 0.5597 0.5956 0.7589 0.1892 -0.0558 0.0161 107 GLN B NE2 2531 N N . PRO B 110 ? 0.6237 0.7472 0.7982 0.2018 0.0227 0.0115 108 PRO B N 2532 C CA . PRO B 110 ? 0.6074 0.7657 0.7867 0.2091 0.0402 0.0096 108 PRO B CA 2533 C C . PRO B 110 ? 0.6189 0.8137 0.8348 0.2097 0.0469 0.0155 108 PRO B C 2534 O O . PRO B 110 ? 0.6553 0.8809 0.8780 0.2057 0.0633 0.0243 108 PRO B O 2535 C CB . PRO B 110 ? 0.6334 0.7786 0.7955 0.2249 0.0345 -0.0078 108 PRO B CB 2536 C CG . PRO B 110 ? 0.6100 0.7183 0.7698 0.2251 0.0127 -0.0130 108 PRO B CG 2537 C CD . PRO B 110 ? 0.5764 0.6657 0.7300 0.2095 0.0071 -0.0015 108 PRO B CD 2538 N N . LEU B 111 ? 0.5824 0.7729 0.8215 0.2138 0.0334 0.0120 109 LEU B N 2539 C CA . LEU B 111 ? 0.5284 0.7532 0.8039 0.2160 0.0376 0.0153 109 LEU B CA 2540 C C . LEU B 111 ? 0.5598 0.8018 0.8544 0.1995 0.0420 0.0326 109 LEU B C 2541 O O . LEU B 111 ? 0.6277 0.9033 0.9486 0.1981 0.0505 0.0389 109 LEU B O 2542 C CB . LEU B 111 ? 0.3738 0.5869 0.6698 0.2255 0.0200 0.0067 109 LEU B CB 2543 N N . GLN B 112 ? 0.5032 0.7212 0.7853 0.1863 0.0362 0.0410 110 GLN B N 2544 C CA . GLN B 112 ? 0.5070 0.7334 0.8093 0.1690 0.0369 0.0572 110 GLN B CA 2545 C C . GLN B 112 ? 0.4942 0.7383 0.7946 0.1573 0.0545 0.0704 110 GLN B C 2546 O O . GLN B 112 ? 0.5377 0.7806 0.8136 0.1606 0.0649 0.0681 110 GLN B O 2547 C CB . GLN B 112 ? 0.5020 0.6930 0.7959 0.1591 0.0208 0.0599 110 GLN B CB 2548 C CG . GLN B 112 ? 0.6235 0.7976 0.9238 0.1662 0.0004 0.0523 110 GLN B CG 2549 C CD . GLN B 112 ? 0.6686 0.8023 0.9509 0.1568 -0.0159 0.0537 110 GLN B CD 2550 O OE1 . GLN B 112 ? 0.6832 0.8033 0.9504 0.1441 -0.0117 0.0593 110 GLN B OE1 2551 N NE2 . GLN B 112 ? 0.7198 0.8328 1.0002 0.1611 -0.0355 0.0477 110 GLN B NE2 2552 N N . HIS B 113 ? 0.4816 0.7401 0.8078 0.1431 0.0560 0.0846 111 HIS B N 2553 C CA . HIS B 113 ? 0.4788 0.7488 0.8063 0.1296 0.0687 0.0994 111 HIS B CA 2554 C C . HIS B 113 ? 0.3275 0.5683 0.6320 0.1210 0.0668 0.1009 111 HIS B C 2555 O O . HIS B 113 ? 0.4350 0.6484 0.7279 0.1227 0.0549 0.0930 111 HIS B O 2556 C CB . HIS B 113 ? 0.3975 0.6819 0.7595 0.1154 0.0660 0.1134 111 HIS B CB 2557 C CG . HIS B 113 ? 0.5276 0.8453 0.9148 0.1221 0.0702 0.1147 111 HIS B CG 2558 N ND1 . HIS B 113 ? 0.5927 0.9156 0.9880 0.1365 0.0627 0.1017 111 HIS B ND1 2559 C CD2 . HIS B 113 ? 0.5896 0.9370 0.9969 0.1163 0.0805 0.1279 111 HIS B CD2 2560 C CE1 . HIS B 113 ? 0.6087 0.9653 1.0291 0.1397 0.0694 0.1057 111 HIS B CE1 2561 N NE2 . HIS B 113 ? 0.6286 1.0009 1.0563 0.1272 0.0805 0.1222 111 HIS B NE2 2562 N N . HIS B 114 ? 0.3025 0.5488 0.6005 0.1119 0.0778 0.1116 112 HIS B N 2563 C CA . HIS B 114 ? 0.3090 0.5307 0.5885 0.1033 0.0769 0.1135 112 HIS B CA 2564 C C . HIS B 114 ? 0.3279 0.5289 0.6219 0.0918 0.0631 0.1146 112 HIS B C 2565 O O . HIS B 114 ? 0.3426 0.5512 0.6639 0.0806 0.0590 0.1236 112 HIS B O 2566 C CB . HIS B 114 ? 0.3065 0.5386 0.5852 0.0933 0.0878 0.1274 112 HIS B CB 2567 C CG . HIS B 114 ? 0.4433 0.6868 0.6970 0.1032 0.0997 0.1256 112 HIS B CG 2568 N ND1 . HIS B 114 ? 0.4824 0.7130 0.7068 0.1158 0.0998 0.1114 112 HIS B ND1 2569 C CD2 . HIS B 114 ? 0.4495 0.7150 0.7028 0.1021 0.1103 0.1363 112 HIS B CD2 2570 C CE1 . HIS B 114 ? 0.5172 0.7619 0.7241 0.1222 0.1100 0.1123 112 HIS B CE1 2571 N NE2 . HIS B 114 ? 0.5333 0.8001 0.7569 0.1141 0.1168 0.1278 112 HIS B NE2 2572 N N . ASN B 115 ? 0.2065 0.3802 0.4815 0.0945 0.0549 0.1055 113 ASN B N 2573 C CA . ASN B 115 ? 0.1925 0.3416 0.4713 0.0829 0.0390 0.1028 113 ASN B CA 2574 C C . ASN B 115 ? 0.1748 0.2901 0.4180 0.0745 0.0354 0.0952 113 ASN B C 2575 O O . ASN B 115 ? 0.1953 0.2845 0.4251 0.0664 0.0219 0.0880 113 ASN B O 2576 C CB . ASN B 115 ? 0.1998 0.3408 0.4808 0.0897 0.0246 0.0944 113 ASN B CB 2577 C CG . ASN B 115 ? 0.3041 0.4258 0.5520 0.1021 0.0211 0.0818 113 ASN B CG 2578 O OD1 . ASN B 115 ? 0.2599 0.3789 0.4853 0.1079 0.0309 0.0789 113 ASN B OD1 2579 N ND2 . ASN B 115 ? 0.3272 0.4343 0.5730 0.1062 0.0055 0.0746 113 ASN B ND2 2580 N N . LEU B 116 ? 0.1722 0.2906 0.4002 0.0768 0.0477 0.0974 114 LEU B N 2581 C CA . LEU B 116 ? 0.1972 0.2883 0.3951 0.0695 0.0461 0.0914 114 LEU B CA 2582 C C . LEU B 116 ? 0.2042 0.3084 0.4099 0.0646 0.0586 0.1018 114 LEU B C 2583 O O . LEU B 116 ? 0.2928 0.4215 0.5046 0.0732 0.0709 0.1093 114 LEU B O 2584 C CB . LEU B 116 ? 0.3023 0.3783 0.4670 0.0805 0.0452 0.0809 114 LEU B CB 2585 C CG . LEU B 116 ? 0.4279 0.4716 0.5599 0.0734 0.0384 0.0724 114 LEU B CG 2586 C CD1 . LEU B 116 ? 0.3409 0.3648 0.4704 0.0628 0.0236 0.0679 114 LEU B CD1 2587 C CD2 . LEU B 116 ? 0.3784 0.4113 0.4842 0.0856 0.0371 0.0639 114 LEU B CD2 2588 N N . LEU B 117 ? 0.1583 0.2477 0.3647 0.0512 0.0549 0.1024 115 LEU B N 2589 C CA . LEU B 117 ? 0.1667 0.2635 0.3789 0.0464 0.0642 0.1117 115 LEU B CA 2590 C C . LEU B 117 ? 0.2022 0.2755 0.3817 0.0449 0.0640 0.1028 115 LEU B C 2591 O O . LEU B 117 ? 0.1815 0.2318 0.3475 0.0381 0.0549 0.0927 115 LEU B O 2592 C CB . LEU B 117 ? 0.1466 0.2450 0.3892 0.0332 0.0593 0.1191 115 LEU B CB 2593 C CG . LEU B 117 ? 0.2009 0.3242 0.4815 0.0322 0.0586 0.1305 115 LEU B CG 2594 C CD1 . LEU B 117 ? 0.2228 0.3435 0.5331 0.0183 0.0516 0.1373 115 LEU B CD1 2595 C CD2 . LEU B 117 ? 0.2223 0.3702 0.5019 0.0402 0.0707 0.1409 115 LEU B CD2 2596 N N . VAL B 118 ? 0.1553 0.2361 0.3219 0.0512 0.0740 0.1067 116 VAL B N 2597 C CA . VAL B 118 ? 0.1572 0.2178 0.2950 0.0501 0.0737 0.0992 116 VAL B CA 2598 C C . VAL B 118 ? 0.1617 0.2232 0.3094 0.0418 0.0777 0.1070 116 VAL B C 2599 O O . VAL B 118 ? 0.1650 0.2466 0.3278 0.0432 0.0858 0.1204 116 VAL B O 2600 C CB . VAL B 118 ? 0.1659 0.2301 0.2791 0.0633 0.0794 0.0959 116 VAL B CB 2601 C CG1 . VAL B 118 ? 0.2174 0.2597 0.3030 0.0608 0.0769 0.0884 116 VAL B CG1 2602 C CG2 . VAL B 118 ? 0.1743 0.2377 0.2808 0.0735 0.0743 0.0878 116 VAL B CG2 2603 N N . CYS B 119 ? 0.1488 0.1895 0.2889 0.0333 0.0716 0.0991 117 CYS B N 2604 C CA . CYS B 119 ? 0.1449 0.1831 0.2919 0.0272 0.0740 0.1038 117 CYS B CA 2605 C C . CYS B 119 ? 0.1481 0.1750 0.2657 0.0308 0.0761 0.0975 117 CYS B C 2606 O O . CYS B 119 ? 0.1499 0.1591 0.2489 0.0282 0.0707 0.0856 117 CYS B O 2607 C CB . CYS B 119 ? 0.1610 0.1865 0.3226 0.0166 0.0659 0.0978 117 CYS B CB 2608 S SG . CYS B 119 ? 0.1471 0.1696 0.3230 0.0108 0.0665 0.1024 117 CYS B SG 2609 N N . SER B 120 ? 0.1506 0.1890 0.2636 0.0365 0.0835 0.1063 118 SER B N 2610 C CA . SER B 120 ? 0.1605 0.1893 0.2466 0.0405 0.0844 0.1011 118 SER B CA 2611 C C . SER B 120 ? 0.1519 0.1756 0.2452 0.0338 0.0820 0.1023 118 SER B C 2612 O O . SER B 120 ? 0.1523 0.1872 0.2613 0.0330 0.0813 0.1103 118 SER B O 2613 C CB . SER B 120 ? 0.1972 0.2415 0.2702 0.0522 0.0914 0.1067 118 SER B CB 2614 O OG . SER B 120 ? 0.2082 0.2407 0.2535 0.0566 0.0898 0.0996 118 SER B OG 2615 N N . VAL B 121 ? 0.1504 0.1571 0.2323 0.0292 0.0789 0.0932 119 VAL B N 2616 C CA . VAL B 121 ? 0.1479 0.1500 0.2381 0.0239 0.0754 0.0909 119 VAL B CA 2617 C C . VAL B 121 ? 0.1798 0.1761 0.2478 0.0270 0.0758 0.0880 119 VAL B C 2618 O O . VAL B 121 ? 0.1727 0.1568 0.2218 0.0264 0.0751 0.0809 119 VAL B O 2619 C CB . VAL B 121 ? 0.1428 0.1329 0.2419 0.0156 0.0720 0.0819 119 VAL B CB 2620 C CG1 . VAL B 121 ? 0.1403 0.1280 0.2533 0.0117 0.0693 0.0796 119 VAL B CG1 2621 C CG2 . VAL B 121 ? 0.1409 0.1348 0.2596 0.0126 0.0703 0.0839 119 VAL B CG2 2622 N N . ASN B 122 ? 0.1541 0.1586 0.2243 0.0297 0.0759 0.0946 120 ASN B N 2623 C CA . ASN B 122 ? 0.1610 0.1621 0.2093 0.0340 0.0760 0.0937 120 ASN B CA 2624 C C . ASN B 122 ? 0.1787 0.1782 0.2337 0.0307 0.0730 0.0954 120 ASN B C 2625 O O . ASN B 122 ? 0.1948 0.2014 0.2707 0.0281 0.0716 0.1018 120 ASN B O 2626 C CB . ASN B 122 ? 0.1870 0.2011 0.2238 0.0432 0.0798 0.1007 120 ASN B CB 2627 C CG . ASN B 122 ? 0.2040 0.2211 0.2331 0.0491 0.0836 0.0992 120 ASN B CG 2628 O OD1 . ASN B 122 ? 0.1950 0.2231 0.2415 0.0487 0.0858 0.1043 120 ASN B OD1 2629 N ND2 . ASN B 122 ? 0.1902 0.1970 0.1935 0.0553 0.0836 0.0929 120 ASN B ND2 2630 N N . GLY B 123 ? 0.1637 0.1534 0.2017 0.0309 0.0712 0.0905 121 GLY B N 2631 C CA . GLY B 123 ? 0.1727 0.1620 0.2135 0.0298 0.0684 0.0938 121 GLY B CA 2632 C C . GLY B 123 ? 0.1891 0.1732 0.2502 0.0231 0.0663 0.0902 121 GLY B C 2633 O O . GLY B 123 ? 0.2061 0.1920 0.2773 0.0224 0.0635 0.0948 121 GLY B O 2634 N N . PHE B 124 ? 0.1515 0.1297 0.2191 0.0185 0.0674 0.0819 122 PHE B N 2635 C CA . PHE B 124 ? 0.1459 0.1212 0.2362 0.0133 0.0667 0.0773 122 PHE B CA 2636 C C . PHE B 124 ? 0.1657 0.1357 0.2492 0.0101 0.0660 0.0683 122 PHE B C 2637 O O . PHE B 124 ? 0.1594 0.1254 0.2199 0.0099 0.0654 0.0645 122 PHE B O 2638 C CB . PHE B 124 ? 0.1414 0.1159 0.2467 0.0099 0.0676 0.0720 122 PHE B CB 2639 C CG . PHE B 124 ? 0.1418 0.1118 0.2286 0.0080 0.0694 0.0642 122 PHE B CG 2640 C CD1 . PHE B 124 ? 0.1416 0.1080 0.2213 0.0034 0.0687 0.0514 122 PHE B CD1 2641 C CD2 . PHE B 124 ? 0.1438 0.1159 0.2202 0.0113 0.0704 0.0690 122 PHE B CD2 2642 C CE1 . PHE B 124 ? 0.1444 0.1070 0.2062 0.0009 0.0682 0.0454 122 PHE B CE1 2643 C CE2 . PHE B 124 ? 0.1458 0.1128 0.2062 0.0099 0.0697 0.0620 122 PHE B CE2 2644 C CZ . PHE B 124 ? 0.1654 0.1267 0.2176 0.0042 0.0678 0.0507 122 PHE B CZ 2645 N N . TYR B 125 ? 0.1425 0.1142 0.2476 0.0080 0.0645 0.0637 123 TYR B N 2646 C CA . TYR B 125 ? 0.1539 0.1265 0.2577 0.0048 0.0641 0.0530 123 TYR B CA 2647 C C . TYR B 125 ? 0.1385 0.1150 0.2704 0.0038 0.0639 0.0441 123 TYR B C 2648 O O . TYR B 125 ? 0.1387 0.1148 0.2935 0.0064 0.0608 0.0498 123 TYR B O 2649 C CB . TYR B 125 ? 0.1476 0.1205 0.2460 0.0065 0.0606 0.0586 123 TYR B CB 2650 C CG . TYR B 125 ? 0.1450 0.1208 0.2399 0.0020 0.0605 0.0490 123 TYR B CG 2651 C CD1 . TYR B 125 ? 0.1943 0.1662 0.2643 -0.0012 0.0596 0.0475 123 TYR B CD1 2652 C CD2 . TYR B 125 ? 0.1418 0.1252 0.2602 0.0009 0.0608 0.0414 123 TYR B CD2 2653 C CE1 . TYR B 125 ? 0.1502 0.1267 0.2189 -0.0070 0.0594 0.0411 123 TYR B CE1 2654 C CE2 . TYR B 125 ? 0.1533 0.1440 0.2703 -0.0036 0.0621 0.0335 123 TYR B CE2 2655 C CZ . TYR B 125 ? 0.1478 0.1355 0.2402 -0.0084 0.0615 0.0345 123 TYR B CZ 2656 O OH . TYR B 125 ? 0.1802 0.1771 0.2732 -0.0145 0.0626 0.0290 123 TYR B OH 2657 N N . PRO B 126 ? 0.1379 0.1185 0.2685 0.0002 0.0667 0.0301 124 PRO B N 2658 C CA . PRO B 126 ? 0.1399 0.1219 0.2460 -0.0048 0.0695 0.0246 124 PRO B CA 2659 C C . PRO B 126 ? 0.1579 0.1348 0.2470 -0.0068 0.0704 0.0241 124 PRO B C 2660 O O . PRO B 126 ? 0.1552 0.1280 0.2497 -0.0038 0.0694 0.0296 124 PRO B O 2661 C CB . PRO B 126 ? 0.1523 0.1454 0.2704 -0.0074 0.0726 0.0107 124 PRO B CB 2662 C CG . PRO B 126 ? 0.1727 0.1662 0.3178 -0.0031 0.0713 0.0045 124 PRO B CG 2663 C CD . PRO B 126 ? 0.1377 0.1237 0.2949 0.0013 0.0664 0.0184 124 PRO B CD 2664 N N . GLY B 127 ? 0.1759 0.1538 0.2457 -0.0123 0.0718 0.0190 125 GLY B N 2665 C CA . GLY B 127 ? 0.2004 0.1719 0.2513 -0.0143 0.0708 0.0203 125 GLY B CA 2666 C C . GLY B 127 ? 0.1857 0.1584 0.2435 -0.0152 0.0714 0.0131 125 GLY B C 2667 O O . GLY B 127 ? 0.2381 0.2049 0.2873 -0.0147 0.0693 0.0164 125 GLY B O 2668 N N . SER B 128 ? 0.2029 0.1836 0.2766 -0.0158 0.0736 0.0021 126 SER B N 2669 C CA . SER B 128 ? 0.1804 0.1623 0.2604 -0.0165 0.0729 -0.0078 126 SER B CA 2670 C C . SER B 128 ? 0.1734 0.1479 0.2693 -0.0123 0.0688 -0.0017 126 SER B C 2671 O O . SER B 128 ? 0.2186 0.1925 0.3368 -0.0083 0.0675 0.0025 126 SER B O 2672 C CB . SER B 128 ? 0.2320 0.2241 0.3296 -0.0153 0.0753 -0.0224 126 SER B CB 2673 O OG . SER B 128 ? 0.4835 0.4873 0.5673 -0.0200 0.0804 -0.0286 126 SER B OG 2674 N N . ILE B 129 ? 0.1850 0.1550 0.2713 -0.0138 0.0663 -0.0001 127 ILE B N 2675 C CA . ILE B 129 ? 0.1506 0.1165 0.2539 -0.0110 0.0626 0.0070 127 ILE B CA 2676 C C . ILE B 129 ? 0.1763 0.1399 0.2752 -0.0137 0.0584 0.0014 127 ILE B C 2677 O O . ILE B 129 ? 0.1917 0.1550 0.2675 -0.0174 0.0584 -0.0030 127 ILE B O 2678 C CB . ILE B 129 ? 0.1517 0.1159 0.2496 -0.0076 0.0637 0.0230 127 ILE B CB 2679 C CG1 . ILE B 129 ? 0.1741 0.1395 0.2972 -0.0047 0.0618 0.0331 127 ILE B CG1 2680 C CG2 . ILE B 129 ? 0.1911 0.1520 0.2640 -0.0084 0.0630 0.0257 127 ILE B CG2 2681 C CD1 . ILE B 129 ? 0.2645 0.2329 0.3844 -0.0004 0.0647 0.0486 127 ILE B CD1 2682 N N . GLU B 130 ? 0.1634 0.1251 0.2853 -0.0125 0.0537 0.0023 128 GLU B N 2683 C CA . GLU B 130 ? 0.1625 0.1217 0.2833 -0.0150 0.0480 -0.0019 128 GLU B CA 2684 C C . GLU B 130 ? 0.1816 0.1406 0.3200 -0.0133 0.0453 0.0124 128 GLU B C 2685 O O . GLU B 130 ? 0.1657 0.1256 0.3305 -0.0119 0.0440 0.0191 128 GLU B O 2686 C CB . GLU B 130 ? 0.2464 0.2046 0.3804 -0.0161 0.0429 -0.0186 128 GLU B CB 2687 C CG . GLU B 130 ? 0.4042 0.3592 0.5373 -0.0189 0.0350 -0.0243 128 GLU B CG 2688 C CD . GLU B 130 ? 0.6465 0.6035 0.7477 -0.0227 0.0354 -0.0342 128 GLU B CD 2689 O OE1 . GLU B 130 ? 0.6640 0.6182 0.7567 -0.0253 0.0292 -0.0334 128 GLU B OE1 2690 O OE2 . GLU B 130 ? 0.6947 0.6573 0.7802 -0.0235 0.0415 -0.0416 128 GLU B OE2 2691 N N . VAL B 131 ? 0.1579 0.1172 0.2830 -0.0135 0.0443 0.0180 129 VAL B N 2692 C CA . VAL B 131 ? 0.1537 0.1173 0.2951 -0.0114 0.0430 0.0315 129 VAL B CA 2693 C C . VAL B 131 ? 0.1675 0.1297 0.3132 -0.0142 0.0350 0.0275 129 VAL B C 2694 O O . VAL B 131 ? 0.1876 0.1462 0.3104 -0.0158 0.0325 0.0209 129 VAL B O 2695 C CB . VAL B 131 ? 0.1710 0.1385 0.2950 -0.0066 0.0488 0.0423 129 VAL B CB 2696 C CG1 . VAL B 131 ? 0.1845 0.1618 0.3269 -0.0034 0.0495 0.0562 129 VAL B CG1 2697 C CG2 . VAL B 131 ? 0.1923 0.1601 0.3080 -0.0040 0.0550 0.0452 129 VAL B CG2 2698 N N . ARG B 132 ? 0.1614 0.1263 0.3372 -0.0155 0.0299 0.0326 130 ARG B N 2699 C CA . ARG B 132 ? 0.1855 0.1493 0.3698 -0.0186 0.0205 0.0289 130 ARG B CA 2700 C C . ARG B 132 ? 0.1634 0.1374 0.3737 -0.0179 0.0195 0.0452 130 ARG B C 2701 O O . ARG B 132 ? 0.1549 0.1364 0.3859 -0.0169 0.0239 0.0582 130 ARG B O 2702 C CB . ARG B 132 ? 0.2081 0.1642 0.4067 -0.0226 0.0114 0.0145 130 ARG B CB 2703 C CG . ARG B 132 ? 0.3471 0.2976 0.5207 -0.0230 0.0130 -0.0033 130 ARG B CG 2704 C CD . ARG B 132 ? 0.5270 0.4713 0.7141 -0.0249 0.0034 -0.0205 130 ARG B CD 2705 N NE . ARG B 132 ? 0.7030 0.6468 0.8646 -0.0247 0.0062 -0.0384 130 ARG B NE 2706 C CZ . ARG B 132 ? 0.7644 0.7089 0.8967 -0.0274 0.0045 -0.0470 130 ARG B CZ 2707 N NH1 . ARG B 132 ? 0.8163 0.7596 0.9421 -0.0299 -0.0014 -0.0401 130 ARG B NH1 2708 N NH2 . ARG B 132 ? 0.8117 0.7597 0.9221 -0.0277 0.0086 -0.0617 130 ARG B NH2 2709 N N . TRP B 133 ? 0.1647 0.1408 0.3747 -0.0186 0.0134 0.0452 131 TRP B N 2710 C CA . TRP B 133 ? 0.1608 0.1500 0.3979 -0.0181 0.0122 0.0599 131 TRP B CA 2711 C C . TRP B 133 ? 0.1770 0.1638 0.4438 -0.0245 -0.0008 0.0574 131 TRP B C 2712 O O . TRP B 133 ? 0.1826 0.1579 0.4400 -0.0277 -0.0106 0.0421 131 TRP B O 2713 C CB . TRP B 133 ? 0.1605 0.1557 0.3815 -0.0132 0.0137 0.0630 131 TRP B CB 2714 C CG . TRP B 133 ? 0.1539 0.1581 0.3612 -0.0053 0.0257 0.0720 131 TRP B CG 2715 C CD1 . TRP B 133 ? 0.1556 0.1524 0.3294 -0.0008 0.0297 0.0663 131 TRP B CD1 2716 C CD2 . TRP B 133 ? 0.1475 0.1705 0.3736 -0.0010 0.0345 0.0882 131 TRP B CD2 2717 N NE1 . TRP B 133 ? 0.1511 0.1589 0.3214 0.0069 0.0394 0.0758 131 TRP B NE1 2718 C CE2 . TRP B 133 ? 0.1464 0.1718 0.3469 0.0073 0.0434 0.0892 131 TRP B CE2 2719 C CE3 . TRP B 133 ? 0.1445 0.1834 0.4067 -0.0039 0.0353 0.1026 131 TRP B CE3 2720 C CZ2 . TRP B 133 ? 0.1498 0.1941 0.3569 0.0141 0.0537 0.1023 131 TRP B CZ2 2721 C CZ3 . TRP B 133 ? 0.1750 0.2345 0.4445 0.0016 0.0465 0.1180 131 TRP B CZ3 2722 C CH2 . TRP B 133 ? 0.1863 0.2487 0.4269 0.0111 0.0560 0.1169 131 TRP B CH2 2723 N N . PHE B 134 ? 0.1638 0.1627 0.4664 -0.0266 -0.0013 0.0731 132 PHE B N 2724 C CA . PHE B 134 ? 0.1711 0.1687 0.5074 -0.0333 -0.0150 0.0736 132 PHE B CA 2725 C C . PHE B 134 ? 0.2245 0.2426 0.5830 -0.0320 -0.0144 0.0907 132 PHE B C 2726 O O . PHE B 134 ? 0.1757 0.2102 0.5343 -0.0267 -0.0026 0.1055 132 PHE B O 2727 C CB . PHE B 134 ? 0.1776 0.1710 0.5280 -0.0332 -0.0195 0.0725 132 PHE B CB 2728 C CG . PHE B 134 ? 0.2056 0.1810 0.5403 -0.0338 -0.0219 0.0535 132 PHE B CG 2729 C CD1 . PHE B 134 ? 0.2386 0.2114 0.5524 -0.0306 -0.0102 0.0520 132 PHE B CD1 2730 C CD2 . PHE B 134 ? 0.2406 0.2026 0.5813 -0.0368 -0.0360 0.0363 132 PHE B CD2 2731 C CE1 . PHE B 134 ? 0.2357 0.1943 0.5374 -0.0307 -0.0115 0.0343 132 PHE B CE1 2732 C CE2 . PHE B 134 ? 0.2159 0.1641 0.5423 -0.0360 -0.0372 0.0171 132 PHE B CE2 2733 C CZ . PHE B 134 ? 0.2502 0.1973 0.5585 -0.0331 -0.0246 0.0163 132 PHE B CZ 2734 N N . ARG B 135 ? 0.2618 0.2792 0.6373 -0.0361 -0.0275 0.0877 133 ARG B N 2735 C CA . ARG B 135 ? 0.1959 0.2322 0.5960 -0.0352 -0.0288 0.1032 133 ARG B CA 2736 C C . ARG B 135 ? 0.2241 0.2547 0.6495 -0.0393 -0.0430 0.1040 133 ARG B C 2737 O O . ARG B 135 ? 0.2242 0.2398 0.6514 -0.0435 -0.0577 0.0892 133 ARG B O 2738 C CB . ARG B 135 ? 0.2064 0.2486 0.6069 -0.0359 -0.0334 0.1001 133 ARG B CB 2739 C CG . ARG B 135 ? 0.1748 0.2377 0.6007 -0.0337 -0.0346 0.1148 133 ARG B CG 2740 C CD . ARG B 135 ? 0.1753 0.2417 0.6038 -0.0338 -0.0447 0.1086 133 ARG B CD 2741 N NE . ARG B 135 ? 0.3803 0.4461 0.7714 -0.0233 -0.0354 0.1033 133 ARG B NE 2742 C CZ . ARG B 135 ? 0.4686 0.5128 0.8202 -0.0218 -0.0400 0.0870 133 ARG B CZ 2743 N NH1 . ARG B 135 ? 0.3882 0.4318 0.7102 -0.0130 -0.0329 0.0845 133 ARG B NH1 2744 N NH2 . ARG B 135 ? 0.4135 0.4374 0.7557 -0.0291 -0.0522 0.0732 133 ARG B NH2 2745 N N . ASN B 136 ? 0.2273 0.2693 0.6706 -0.0379 -0.0392 0.1210 134 ASN B N 2746 C CA . ASN B 136 ? 0.2910 0.3275 0.7609 -0.0418 -0.0527 0.1245 134 ASN B CA 2747 C C . ASN B 136 ? 0.3093 0.3238 0.7752 -0.0439 -0.0645 0.1052 134 ASN B C 2748 O O . ASN B 136 ? 0.3840 0.3883 0.8649 -0.0473 -0.0806 0.0971 134 ASN B O 2749 C CB . ASN B 136 ? 0.3469 0.3889 0.8389 -0.0452 -0.0633 0.1295 134 ASN B CB 2750 C CG . ASN B 136 ? 0.2862 0.3523 0.7853 -0.0427 -0.0515 0.1489 134 ASN B CG 2751 O OD1 . ASN B 136 ? 0.3383 0.4176 0.8367 -0.0399 -0.0394 0.1639 134 ASN B OD1 2752 N ND2 . ASN B 136 ? 0.3648 0.4376 0.8698 -0.0434 -0.0554 0.1477 134 ASN B ND2 2753 N N . GLY B 137 ? 0.2876 0.2952 0.7323 -0.0414 -0.0564 0.0968 135 GLY B N 2754 C CA . GLY B 137 ? 0.3803 0.3692 0.8210 -0.0421 -0.0652 0.0786 135 GLY B CA 2755 C C . GLY B 137 ? 0.4269 0.4005 0.8457 -0.0436 -0.0714 0.0548 135 GLY B C 2756 O O . GLY B 137 ? 0.4298 0.3886 0.8421 -0.0431 -0.0779 0.0370 135 GLY B O 2757 N N . GLN B 138 ? 0.2761 0.2536 0.6831 -0.0450 -0.0698 0.0541 136 GLN B N 2758 C CA . GLN B 138 ? 0.2875 0.2510 0.6699 -0.0471 -0.0763 0.0329 136 GLN B CA 2759 C C . GLN B 138 ? 0.2126 0.1764 0.5659 -0.0458 -0.0621 0.0317 136 GLN B C 2760 O O . GLN B 138 ? 0.2533 0.2311 0.6076 -0.0440 -0.0518 0.0474 136 GLN B O 2761 C CB . GLN B 138 ? 0.3652 0.3309 0.7560 -0.0505 -0.0890 0.0327 136 GLN B CB 2762 C CG . GLN B 138 ? 0.5705 0.5363 0.9923 -0.0519 -0.1034 0.0367 136 GLN B CG 2763 C CD . GLN B 138 ? 0.6875 0.6355 1.1062 -0.0518 -0.1163 0.0164 136 GLN B CD 2764 O OE1 . GLN B 138 ? 0.6958 0.6320 1.0861 -0.0511 -0.1164 -0.0037 136 GLN B OE1 2765 N NE2 . GLN B 138 ? 0.6831 0.6295 1.1311 -0.0521 -0.1273 0.0214 136 GLN B NE2 2766 N N . GLU B 139 ? 0.2669 0.2175 0.5911 -0.0447 -0.0608 0.0130 137 GLU B N 2767 C CA . GLU B 139 ? 0.2635 0.2169 0.5482 -0.0395 -0.0464 0.0121 137 GLU B CA 2768 C C . GLU B 139 ? 0.3085 0.2660 0.5717 -0.0384 -0.0479 0.0139 137 GLU B C 2769 O O . GLU B 139 ? 0.2692 0.2213 0.5280 -0.0415 -0.0610 0.0045 137 GLU B O 2770 C CB . GLU B 139 ? 0.3444 0.2871 0.6004 -0.0380 -0.0436 -0.0073 137 GLU B CB 2771 C CG . GLU B 139 ? 0.2526 0.1988 0.4713 -0.0341 -0.0294 -0.0056 137 GLU B CG 2772 C CD . GLU B 139 ? 0.5074 0.4479 0.7011 -0.0331 -0.0248 -0.0223 137 GLU B CD 2773 O OE1 . GLU B 139 ? 0.5272 0.4614 0.7313 -0.0338 -0.0317 -0.0371 137 GLU B OE1 2774 O OE2 . GLU B 139 ? 0.5521 0.4951 0.7168 -0.0313 -0.0147 -0.0208 137 GLU B OE2 2775 N N . GLU B 140 ? 0.2002 0.1668 0.4506 -0.0336 -0.0357 0.0258 138 GLU B N 2776 C CA . GLU B 140 ? 0.2025 0.1713 0.4317 -0.0311 -0.0371 0.0274 138 GLU B CA 2777 C C . GLU B 140 ? 0.2050 0.1660 0.3918 -0.0290 -0.0301 0.0196 138 GLU B C 2778 O O . GLU B 140 ? 0.2198 0.1836 0.3973 -0.0250 -0.0177 0.0250 138 GLU B O 2779 C CB . GLU B 140 ? 0.2594 0.2446 0.5066 -0.0260 -0.0303 0.0453 138 GLU B CB 2780 C CG . GLU B 140 ? 0.3996 0.3864 0.6302 -0.0221 -0.0339 0.0465 138 GLU B CG 2781 C CD . GLU B 140 ? 0.4901 0.4710 0.7246 -0.0272 -0.0512 0.0392 138 GLU B CD 2782 O OE1 . GLU B 140 ? 0.4590 0.4271 0.6616 -0.0293 -0.0577 0.0281 138 GLU B OE1 2783 O OE2 . GLU B 140 ? 0.4705 0.4606 0.7401 -0.0296 -0.0588 0.0456 138 GLU B OE2 2784 N N . LYS B 141 ? 0.2904 0.2424 0.4517 -0.0324 -0.0387 0.0077 139 LYS B N 2785 C CA . LYS B 141 ? 0.2578 0.2038 0.3798 -0.0325 -0.0334 0.0019 139 LYS B CA 2786 C C . LYS B 141 ? 0.2805 0.2250 0.3828 -0.0307 -0.0366 0.0086 139 LYS B C 2787 O O . LYS B 141 ? 0.3481 0.2878 0.4209 -0.0308 -0.0322 0.0082 139 LYS B O 2788 C CB . LYS B 141 ? 0.3368 0.2759 0.4391 -0.0378 -0.0392 -0.0154 139 LYS B CB 2789 C CG . LYS B 141 ? 0.4176 0.3564 0.5332 -0.0377 -0.0346 -0.0251 139 LYS B CG 2790 C CD . LYS B 141 ? 0.4989 0.4341 0.5906 -0.0410 -0.0383 -0.0443 139 LYS B CD 2791 C CE . LYS B 141 ? 0.5263 0.4616 0.6320 -0.0390 -0.0336 -0.0557 139 LYS B CE 2792 N NZ . LYS B 141 ? 0.5059 0.4400 0.5933 -0.0405 -0.0388 -0.0774 139 LYS B NZ 2793 N N . THR B 142 ? 0.2775 0.2262 0.3983 -0.0290 -0.0452 0.0154 140 THR B N 2794 C CA . THR B 142 ? 0.2559 0.2025 0.3622 -0.0259 -0.0501 0.0215 140 THR B CA 2795 C C . THR B 142 ? 0.2334 0.1887 0.3512 -0.0167 -0.0401 0.0330 140 THR B C 2796 O O . THR B 142 ? 0.2721 0.2395 0.4177 -0.0133 -0.0324 0.0394 140 THR B O 2797 C CB . THR B 142 ? 0.3956 0.3428 0.5151 -0.0279 -0.0662 0.0218 140 THR B CB 2798 O OG1 . THR B 142 ? 0.4524 0.4132 0.6129 -0.0244 -0.0655 0.0300 140 THR B OG1 2799 C CG2 . THR B 142 ? 0.3568 0.2967 0.4660 -0.0362 -0.0771 0.0090 140 THR B CG2 2800 N N . GLY B 143 ? 0.2523 0.2015 0.3484 -0.0127 -0.0411 0.0357 141 GLY B N 2801 C CA . GLY B 143 ? 0.2656 0.2222 0.3694 -0.0021 -0.0335 0.0437 141 GLY B CA 2802 C C . GLY B 143 ? 0.2147 0.1744 0.3144 0.0009 -0.0184 0.0452 141 GLY B C 2803 O O . GLY B 143 ? 0.2048 0.1763 0.3183 0.0095 -0.0097 0.0518 141 GLY B O 2804 N N . VAL B 144 ? 0.2075 0.1583 0.2878 -0.0058 -0.0152 0.0389 142 VAL B N 2805 C CA . VAL B 144 ? 0.2097 0.1623 0.2854 -0.0036 -0.0024 0.0399 142 VAL B CA 2806 C C . VAL B 144 ? 0.2073 0.1483 0.2517 -0.0031 -0.0017 0.0384 142 VAL B C 2807 O O . VAL B 144 ? 0.2162 0.1468 0.2385 -0.0103 -0.0081 0.0338 142 VAL B O 2808 C CB . VAL B 144 ? 0.1941 0.1472 0.2763 -0.0105 0.0012 0.0340 142 VAL B CB 2809 C CG1 . VAL B 144 ? 0.1911 0.1451 0.2677 -0.0085 0.0127 0.0352 142 VAL B CG1 2810 C CG2 . VAL B 144 ? 0.1885 0.1516 0.3056 -0.0113 -0.0010 0.0370 142 VAL B CG2 2811 N N . VAL B 145 ? 0.1993 0.1428 0.2421 0.0053 0.0054 0.0430 143 VAL B N 2812 C CA A VAL B 145 ? 0.2128 0.1442 0.2292 0.0061 0.0049 0.0419 143 VAL B CA 2813 C CA B VAL B 145 ? 0.2260 0.1575 0.2425 0.0063 0.0050 0.0420 143 VAL B CA 2814 C C . VAL B 145 ? 0.2266 0.1629 0.2436 0.0100 0.0165 0.0435 143 VAL B C 2815 O O . VAL B 145 ? 0.2276 0.1772 0.2641 0.0156 0.0241 0.0478 143 VAL B O 2816 C CB A VAL B 145 ? 0.2342 0.1594 0.2447 0.0143 -0.0033 0.0441 143 VAL B CB 2817 C CB B VAL B 145 ? 0.2495 0.1754 0.2608 0.0151 -0.0025 0.0443 143 VAL B CB 2818 C CG1 A VAL B 145 ? 0.2132 0.1527 0.2426 0.0276 0.0035 0.0478 143 VAL B CG1 2819 C CG1 B VAL B 145 ? 0.2952 0.2050 0.2802 0.0145 -0.0064 0.0433 143 VAL B CG1 2820 C CG2 A VAL B 145 ? 0.2910 0.1993 0.2743 0.0127 -0.0082 0.0431 143 VAL B CG2 2821 C CG2 B VAL B 145 ? 0.2558 0.1786 0.2711 0.0126 -0.0148 0.0443 143 VAL B CG2 2822 N N . SER B 146 ? 0.2010 0.1275 0.1970 0.0063 0.0172 0.0412 144 SER B N 2823 C CA . SER B 146 ? 0.1934 0.1235 0.1890 0.0091 0.0265 0.0424 144 SER B CA 2824 C C . SER B 146 ? 0.2103 0.1285 0.1839 0.0111 0.0235 0.0420 144 SER B C 2825 O O . SER B 146 ? 0.2186 0.1239 0.1761 0.0073 0.0142 0.0410 144 SER B O 2826 C CB . SER B 146 ? 0.2043 0.1376 0.2041 0.0003 0.0315 0.0388 144 SER B CB 2827 O OG . SER B 146 ? 0.1807 0.1166 0.1805 0.0023 0.0389 0.0402 144 SER B OG 2828 N N . THR B 147 ? 0.2006 0.1222 0.1740 0.0168 0.0302 0.0435 145 THR B N 2829 C CA . THR B 147 ? 0.2146 0.1245 0.1688 0.0174 0.0268 0.0423 145 THR B CA 2830 C C . THR B 147 ? 0.2103 0.1151 0.1551 0.0048 0.0264 0.0406 145 THR B C 2831 O O . THR B 147 ? 0.2489 0.1423 0.1776 0.0012 0.0207 0.0407 145 THR B O 2832 C CB . THR B 147 ? 0.2157 0.1324 0.1719 0.0261 0.0339 0.0440 145 THR B CB 2833 O OG1 . THR B 147 ? 0.2011 0.1299 0.1723 0.0223 0.0429 0.0464 145 THR B OG1 2834 C CG2 . THR B 147 ? 0.2269 0.1519 0.1891 0.0397 0.0355 0.0453 145 THR B CG2 2835 N N . GLY B 148 ? 0.2043 0.1184 0.1602 -0.0018 0.0319 0.0389 146 GLY B N 2836 C CA . GLY B 148 ? 0.2214 0.1369 0.1726 -0.0113 0.0349 0.0361 146 GLY B CA 2837 C C . GLY B 148 ? 0.1887 0.1097 0.1477 -0.0075 0.0418 0.0372 146 GLY B C 2838 O O . GLY B 148 ? 0.1981 0.1227 0.1649 0.0017 0.0446 0.0406 146 GLY B O 2839 N N . LEU B 149 ? 0.1875 0.1112 0.1446 -0.0143 0.0446 0.0348 147 LEU B N 2840 C CA . LEU B 149 ? 0.1802 0.1091 0.1459 -0.0114 0.0498 0.0359 147 LEU B CA 2841 C C . LEU B 149 ? 0.1878 0.1075 0.1391 -0.0083 0.0452 0.0392 147 LEU B C 2842 O O . LEU B 149 ? 0.2268 0.1386 0.1641 -0.0146 0.0394 0.0392 147 LEU B O 2843 C CB . LEU B 149 ? 0.1900 0.1270 0.1622 -0.0191 0.0542 0.0309 147 LEU B CB 2844 C CG . LEU B 149 ? 0.2162 0.1593 0.2011 -0.0165 0.0586 0.0316 147 LEU B CG 2845 C CD1 . LEU B 149 ? 0.2210 0.1691 0.2258 -0.0095 0.0620 0.0342 147 LEU B CD1 2846 C CD2 . LEU B 149 ? 0.2655 0.2181 0.2567 -0.0237 0.0623 0.0251 147 LEU B CD2 2847 N N . ILE B 150 ? 0.1855 0.1067 0.1403 0.0012 0.0470 0.0424 148 ILE B N 2848 C CA . ILE B 150 ? 0.1952 0.1076 0.1357 0.0063 0.0416 0.0437 148 ILE B CA 2849 C C . ILE B 150 ? 0.1911 0.1087 0.1370 0.0064 0.0445 0.0453 148 ILE B C 2850 O O . ILE B 150 ? 0.1993 0.1270 0.1589 0.0106 0.0507 0.0484 148 ILE B O 2851 C CB . ILE B 150 ? 0.2148 0.1269 0.1513 0.0189 0.0410 0.0451 148 ILE B CB 2852 C CG1 . ILE B 150 ? 0.2757 0.1831 0.2096 0.0199 0.0370 0.0435 148 ILE B CG1 2853 C CG2 . ILE B 150 ? 0.2653 0.1681 0.1855 0.0258 0.0346 0.0437 148 ILE B CG2 2854 C CD1 . ILE B 150 ? 0.3491 0.2617 0.2844 0.0330 0.0384 0.0443 148 ILE B CD1 2855 N N . GLN B 151 ? 0.1981 0.1087 0.1351 0.0010 0.0389 0.0443 149 GLN B N 2856 C CA . GLN B 151 ? 0.2194 0.1334 0.1603 0.0020 0.0390 0.0460 149 GLN B CA 2857 C C . GLN B 151 ? 0.3520 0.2596 0.2796 0.0131 0.0342 0.0471 149 GLN B C 2858 O O . GLN B 151 ? 0.3786 0.2738 0.2904 0.0168 0.0266 0.0444 149 GLN B O 2859 C CB . GLN B 151 ? 0.3316 0.2428 0.2706 -0.0088 0.0344 0.0449 149 GLN B CB 2860 C CG . GLN B 151 ? 0.4935 0.4172 0.4498 -0.0124 0.0393 0.0452 149 GLN B CG 2861 C CD . GLN B 151 ? 0.5782 0.5066 0.5378 -0.0244 0.0383 0.0440 149 GLN B CD 2862 O OE1 . GLN B 151 ? 0.5825 0.5027 0.5294 -0.0312 0.0320 0.0452 149 GLN B OE1 2863 N NE2 . GLN B 151 ? 0.4935 0.4364 0.4720 -0.0271 0.0442 0.0422 149 GLN B NE2 2864 N N . ASN B 152 ? 0.2176 0.1336 0.1512 0.0190 0.0381 0.0508 150 ASN B N 2865 C CA . ASN B 152 ? 0.2176 0.1309 0.1362 0.0301 0.0345 0.0515 150 ASN B CA 2866 C C . ASN B 152 ? 0.2964 0.2012 0.2054 0.0286 0.0252 0.0499 150 ASN B C 2867 O O . ASN B 152 ? 0.2648 0.1643 0.1572 0.0377 0.0192 0.0479 150 ASN B O 2868 C CB . ASN B 152 ? 0.2323 0.1606 0.1597 0.0372 0.0429 0.0585 150 ASN B CB 2869 C CG . ASN B 152 ? 0.2615 0.1982 0.1973 0.0403 0.0503 0.0607 150 ASN B CG 2870 O OD1 . ASN B 152 ? 0.2905 0.2216 0.2170 0.0439 0.0480 0.0561 150 ASN B OD1 2871 N ND2 . ASN B 152 ? 0.2221 0.1717 0.1776 0.0387 0.0577 0.0680 150 ASN B ND2 2872 N N . GLY B 153 ? 0.2219 0.1272 0.1422 0.0176 0.0238 0.0502 151 GLY B N 2873 C CA . GLY B 153 ? 0.2315 0.1298 0.1471 0.0138 0.0141 0.0493 151 GLY B CA 2874 C C . GLY B 153 ? 0.2291 0.1365 0.1531 0.0165 0.0150 0.0537 151 GLY B C 2875 O O . GLY B 153 ? 0.2518 0.1550 0.1745 0.0136 0.0064 0.0535 151 GLY B O 2876 N N . ASP B 154 ? 0.2219 0.1412 0.1559 0.0216 0.0241 0.0586 152 ASP B N 2877 C CA . ASP B 154 ? 0.2201 0.1477 0.1616 0.0250 0.0243 0.0650 152 ASP B CA 2878 C C . ASP B 154 ? 0.2032 0.1428 0.1728 0.0204 0.0321 0.0692 152 ASP B C 2879 O O . ASP B 154 ? 0.2058 0.1532 0.1842 0.0245 0.0345 0.0770 152 ASP B O 2880 C CB . ASP B 154 ? 0.2847 0.2157 0.2102 0.0368 0.0259 0.0693 152 ASP B CB 2881 C CG . ASP B 154 ? 0.3389 0.2792 0.2717 0.0398 0.0367 0.0730 152 ASP B CG 2882 O OD1 . ASP B 154 ? 0.2216 0.1621 0.1687 0.0334 0.0412 0.0704 152 ASP B OD1 2883 O OD2 . ASP B 154 ? 0.3465 0.2951 0.2707 0.0484 0.0404 0.0787 152 ASP B OD2 2884 N N . TRP B 155 ? 0.1925 0.1336 0.1757 0.0121 0.0352 0.0640 153 TRP B N 2885 C CA . TRP B 155 ? 0.1787 0.1302 0.1890 0.0086 0.0418 0.0641 153 TRP B CA 2886 C C . TRP B 155 ? 0.1727 0.1283 0.1904 0.0125 0.0487 0.0677 153 TRP B C 2887 O O . TRP B 155 ? 0.1657 0.1280 0.2060 0.0125 0.0515 0.0707 153 TRP B O 2888 C CB . TRP B 155 ? 0.1778 0.1354 0.2058 0.0088 0.0383 0.0681 153 TRP B CB 2889 C CG . TRP B 155 ? 0.1813 0.1391 0.2115 0.0028 0.0327 0.0637 153 TRP B CG 2890 C CD1 . TRP B 155 ? 0.1984 0.1482 0.2110 0.0023 0.0237 0.0641 153 TRP B CD1 2891 C CD2 . TRP B 155 ? 0.1715 0.1395 0.2243 -0.0037 0.0356 0.0580 153 TRP B CD2 2892 N NE1 . TRP B 155 ? 0.1989 0.1536 0.2235 -0.0055 0.0204 0.0608 153 TRP B NE1 2893 C CE2 . TRP B 155 ? 0.1778 0.1454 0.2270 -0.0089 0.0286 0.0571 153 TRP B CE2 2894 C CE3 . TRP B 155 ? 0.1609 0.1392 0.2371 -0.0050 0.0430 0.0527 153 TRP B CE3 2895 C CZ2 . TRP B 155 ? 0.1794 0.1599 0.2487 -0.0158 0.0305 0.0525 153 TRP B CZ2 2896 C CZ3 . TRP B 155 ? 0.1569 0.1473 0.2510 -0.0104 0.0448 0.0459 153 TRP B CZ3 2897 C CH2 . TRP B 155 ? 0.1620 0.1551 0.2530 -0.0159 0.0395 0.0466 153 TRP B CH2 2898 N N . THR B 156 ? 0.1768 0.1280 0.1774 0.0158 0.0502 0.0674 154 THR B N 2899 C CA . THR B 156 ? 0.1707 0.1267 0.1800 0.0178 0.0564 0.0700 154 THR B CA 2900 C C . THR B 156 ? 0.1711 0.1214 0.1684 0.0159 0.0571 0.0634 154 THR B C 2901 O O . THR B 156 ? 0.1996 0.1411 0.1778 0.0155 0.0521 0.0593 154 THR B O 2902 C CB . THR B 156 ? 0.2080 0.1699 0.2127 0.0259 0.0585 0.0805 154 THR B CB 2903 O OG1 . THR B 156 ? 0.2169 0.1741 0.1950 0.0323 0.0562 0.0785 154 THR B OG1 2904 C CG2 . THR B 156 ? 0.2325 0.1994 0.2459 0.0275 0.0563 0.0894 154 THR B CG2 2905 N N . PHE B 157 ? 0.1639 0.1181 0.1734 0.0145 0.0616 0.0628 155 PHE B N 2906 C CA . PHE B 157 ? 0.1650 0.1146 0.1649 0.0131 0.0614 0.0578 155 PHE B CA 2907 C C . PHE B 157 ? 0.1648 0.1195 0.1676 0.0193 0.0646 0.0634 155 PHE B C 2908 O O . PHE B 157 ? 0.1624 0.1260 0.1780 0.0227 0.0680 0.0716 155 PHE B O 2909 C CB . PHE B 157 ? 0.1583 0.1095 0.1704 0.0051 0.0631 0.0508 155 PHE B CB 2910 C CG . PHE B 157 ? 0.1592 0.1097 0.1689 -0.0019 0.0616 0.0448 155 PHE B CG 2911 C CD1 . PHE B 157 ? 0.1876 0.1450 0.2145 -0.0033 0.0632 0.0437 155 PHE B CD1 2912 C CD2 . PHE B 157 ? 0.1659 0.1103 0.1584 -0.0074 0.0583 0.0411 155 PHE B CD2 2913 C CE1 . PHE B 157 ? 0.2035 0.1644 0.2308 -0.0096 0.0629 0.0383 155 PHE B CE1 2914 C CE2 . PHE B 157 ? 0.2022 0.1497 0.1942 -0.0152 0.0577 0.0375 155 PHE B CE2 2915 C CZ . PHE B 157 ? 0.2073 0.1645 0.2170 -0.0160 0.0607 0.0357 155 PHE B CZ 2916 N N . GLN B 158 ? 0.1681 0.1185 0.1608 0.0203 0.0631 0.0598 156 GLN B N 2917 C CA . GLN B 158 ? 0.1661 0.1240 0.1674 0.0247 0.0664 0.0641 156 GLN B CA 2918 C C . GLN B 158 ? 0.1659 0.1182 0.1653 0.0205 0.0634 0.0579 156 GLN B C 2919 O O . GLN B 158 ? 0.1701 0.1125 0.1568 0.0152 0.0588 0.0515 156 GLN B O 2920 C CB . GLN B 158 ? 0.1751 0.1375 0.1636 0.0356 0.0675 0.0685 156 GLN B CB 2921 C CG . GLN B 158 ? 0.1871 0.1368 0.1515 0.0394 0.0608 0.0610 156 GLN B CG 2922 C CD . GLN B 158 ? 0.2678 0.2233 0.2208 0.0523 0.0619 0.0621 156 GLN B CD 2923 O OE1 . GLN B 158 ? 0.3143 0.2794 0.2748 0.0573 0.0654 0.0641 156 GLN B OE1 2924 N NE2 . GLN B 158 ? 0.2357 0.1873 0.1714 0.0583 0.0588 0.0603 156 GLN B NE2 2925 N N . THR B 159 ? 0.1622 0.1216 0.1754 0.0220 0.0654 0.0608 157 THR B N 2926 C CA . THR B 159 ? 0.1645 0.1190 0.1746 0.0195 0.0611 0.0559 157 THR B CA 2927 C C . THR B 159 ? 0.1629 0.1282 0.1867 0.0253 0.0633 0.0617 157 THR B C 2928 O O . THR B 159 ? 0.1752 0.1528 0.2178 0.0266 0.0685 0.0696 157 THR B O 2929 C CB . THR B 159 ? 0.1607 0.1123 0.1787 0.0095 0.0594 0.0496 157 THR B CB 2930 O OG1 . THR B 159 ? 0.2052 0.1518 0.2168 0.0070 0.0541 0.0457 157 THR B OG1 2931 C CG2 . THR B 159 ? 0.1622 0.1228 0.2070 0.0079 0.0628 0.0524 157 THR B CG2 2932 N N . LEU B 160 ? 0.1690 0.1307 0.1850 0.0286 0.0589 0.0589 158 LEU B N 2933 C CA . LEU B 160 ? 0.1674 0.1413 0.1995 0.0334 0.0603 0.0637 158 LEU B CA 2934 C C . LEU B 160 ? 0.1761 0.1445 0.2154 0.0259 0.0539 0.0593 158 LEU B C 2935 O O . LEU B 160 ? 0.1734 0.1284 0.1959 0.0221 0.0470 0.0527 158 LEU B O 2936 C CB . LEU B 160 ? 0.1941 0.1696 0.2144 0.0450 0.0590 0.0628 158 LEU B CB 2937 C CG . LEU B 160 ? 0.3926 0.3716 0.3986 0.0548 0.0631 0.0638 158 LEU B CG 2938 C CD1 . LEU B 160 ? 0.3812 0.3682 0.3835 0.0684 0.0631 0.0621 158 LEU B CD1 2939 C CD2 . LEU B 160 ? 0.3773 0.3714 0.3961 0.0541 0.0720 0.0732 158 LEU B CD2 2940 N N . VAL B 161 ? 0.1602 0.1391 0.2243 0.0232 0.0552 0.0636 159 VAL B N 2941 C CA . VAL B 161 ? 0.1614 0.1359 0.2332 0.0166 0.0479 0.0589 159 VAL B CA 2942 C C . VAL B 161 ? 0.1607 0.1481 0.2521 0.0213 0.0470 0.0652 159 VAL B C 2943 O O . VAL B 161 ? 0.1632 0.1656 0.2787 0.0222 0.0521 0.0741 159 VAL B O 2944 C CB . VAL B 161 ? 0.1569 0.1301 0.2429 0.0079 0.0474 0.0557 159 VAL B CB 2945 C CG1 . VAL B 161 ? 0.2189 0.1875 0.3099 0.0018 0.0388 0.0492 159 VAL B CG1 2946 C CG2 . VAL B 161 ? 0.1575 0.1219 0.2266 0.0043 0.0495 0.0494 159 VAL B CG2 2947 N N . MET B 162 ? 0.1680 0.1505 0.2507 0.0241 0.0400 0.0616 160 MET B N 2948 C CA A MET B 162 ? 0.1686 0.1646 0.2695 0.0305 0.0387 0.0667 160 MET B CA 2949 C CA B MET B 162 ? 0.1879 0.1844 0.2897 0.0303 0.0390 0.0670 160 MET B CA 2950 C C . MET B 162 ? 0.1979 0.1931 0.3153 0.0232 0.0296 0.0652 160 MET B C 2951 O O . MET B 162 ? 0.2426 0.2226 0.3455 0.0161 0.0212 0.0574 160 MET B O 2952 C CB A MET B 162 ? 0.1785 0.1693 0.2621 0.0402 0.0347 0.0632 160 MET B CB 2953 C CB B MET B 162 ? 0.2321 0.2261 0.3179 0.0412 0.0369 0.0645 160 MET B CB 2954 C CG A MET B 162 ? 0.3463 0.3458 0.4222 0.0521 0.0432 0.0653 160 MET B CG 2955 C CG B MET B 162 ? 0.2674 0.2635 0.3382 0.0494 0.0451 0.0652 160 MET B CG 2956 S SD A MET B 162 ? 0.3240 0.3098 0.3740 0.0496 0.0470 0.0621 160 MET B SD 2957 S SD B MET B 162 ? 0.3037 0.2854 0.3484 0.0601 0.0378 0.0571 160 MET B SD 2958 C CE A MET B 162 ? 0.2105 0.1692 0.2341 0.0440 0.0339 0.0528 160 MET B CE 2959 C CE B MET B 162 ? 0.3587 0.3502 0.3930 0.0711 0.0487 0.0585 160 MET B CE 2960 N N . LEU B 163 ? 0.1648 0.1779 0.3122 0.0248 0.0309 0.0731 161 LEU B N 2961 C CA . LEU B 163 ? 0.1671 0.1804 0.3329 0.0187 0.0205 0.0720 161 LEU B CA 2962 C C . LEU B 163 ? 0.1704 0.1960 0.3482 0.0271 0.0174 0.0758 161 LEU B C 2963 O O . LEU B 163 ? 0.1656 0.2129 0.3621 0.0344 0.0261 0.0848 161 LEU B O 2964 C CB . LEU B 163 ? 0.1603 0.1841 0.3579 0.0119 0.0220 0.0788 161 LEU B CB 2965 C CG . LEU B 163 ? 0.1638 0.1894 0.3854 0.0057 0.0100 0.0783 161 LEU B CG 2966 C CD1 . LEU B 163 ? 0.1738 0.1781 0.3745 -0.0014 -0.0019 0.0645 161 LEU B CD1 2967 C CD2 . LEU B 163 ? 0.1584 0.1954 0.4161 -0.0005 0.0109 0.0875 161 LEU B CD2 2968 N N . GLU B 164 ? 0.1800 0.1934 0.3471 0.0262 0.0050 0.0693 162 GLU B N 2969 C CA . GLU B 164 ? 0.1845 0.2085 0.3669 0.0339 -0.0008 0.0720 162 GLU B CA 2970 C C . GLU B 164 ? 0.1808 0.2186 0.3987 0.0278 -0.0061 0.0775 162 GLU B C 2971 O O . GLU B 164 ? 0.2037 0.2291 0.4212 0.0175 -0.0167 0.0727 162 GLU B O 2972 C CB . GLU B 164 ? 0.1984 0.2021 0.3570 0.0340 -0.0146 0.0643 162 GLU B CB 2973 C CG . GLU B 164 ? 0.2047 0.1915 0.3291 0.0377 -0.0126 0.0593 162 GLU B CG 2974 C CD . GLU B 164 ? 0.5276 0.4914 0.6269 0.0326 -0.0276 0.0540 162 GLU B CD 2975 O OE1 . GLU B 164 ? 0.5840 0.5449 0.6896 0.0262 -0.0392 0.0535 162 GLU B OE1 2976 O OE2 . GLU B 164 ? 0.4935 0.4424 0.5669 0.0345 -0.0287 0.0513 162 GLU B OE2 2977 N N . THR B 165 ? 0.1746 0.2389 0.4234 0.0341 0.0009 0.0875 163 THR B N 2978 C CA . THR B 165 ? 0.1708 0.2507 0.4583 0.0273 -0.0036 0.0954 163 THR B CA 2979 C C . THR B 165 ? 0.1673 0.2792 0.4850 0.0371 0.0035 0.1058 163 THR B C 2980 O O . THR B 165 ? 0.1660 0.2909 0.4754 0.0487 0.0160 0.1078 163 THR B O 2981 C CB . THR B 165 ? 0.1635 0.2444 0.4635 0.0172 0.0020 0.1008 163 THR B CB 2982 O OG1 . THR B 165 ? 0.1874 0.2779 0.5250 0.0086 -0.0065 0.1072 163 THR B OG1 2983 C CG2 . THR B 165 ? 0.1557 0.2559 0.4601 0.0233 0.0195 0.1113 163 THR B CG2 2984 N N . VAL B 166 ? 0.1675 0.2934 0.5202 0.0330 -0.0049 0.1117 164 VAL B N 2985 C CA . VAL B 166 ? 0.1635 0.3258 0.5519 0.0407 0.0030 0.1237 164 VAL B CA 2986 C C . VAL B 166 ? 0.1639 0.3360 0.5730 0.0282 0.0082 0.1355 164 VAL B C 2987 O O . VAL B 166 ? 0.1670 0.3342 0.5983 0.0172 -0.0042 0.1377 164 VAL B O 2988 C CB . VAL B 166 ? 0.1718 0.3384 0.5767 0.0435 -0.0106 0.1208 164 VAL B CB 2989 C CG1 . VAL B 166 ? 0.1790 0.3755 0.6009 0.0495 0.0002 0.1279 164 VAL B CG1 2990 C CG2 . VAL B 166 ? 0.1802 0.3256 0.5547 0.0529 -0.0196 0.1079 164 VAL B CG2 2991 N N . PRO B 167 ? 0.1643 0.3472 0.5640 0.0301 0.0245 0.1432 165 PRO B N 2992 C CA . PRO B 167 ? 0.1688 0.3562 0.5840 0.0191 0.0276 0.1562 165 PRO B CA 2993 C C . PRO B 167 ? 0.2149 0.4206 0.6597 0.0157 0.0243 0.1660 165 PRO B C 2994 O O . PRO B 167 ? 0.1845 0.4117 0.6332 0.0249 0.0301 0.1667 165 PRO B O 2995 C CB . PRO B 167 ? 0.1863 0.3841 0.5805 0.0256 0.0447 0.1621 165 PRO B CB 2996 C CG . PRO B 167 ? 0.1674 0.3553 0.5322 0.0360 0.0484 0.1493 165 PRO B CG 2997 C CD . PRO B 167 ? 0.1636 0.3510 0.5346 0.0426 0.0383 0.1397 165 PRO B CD 2998 N N . ARG B 168 ? 0.1843 0.3809 0.6505 0.0030 0.0143 0.1726 166 ARG B N 2999 C CA . ARG B 168 ? 0.1962 0.4088 0.6926 -0.0017 0.0104 0.1840 166 ARG B CA 3000 C C . ARG B 168 ? 0.2052 0.4246 0.7092 -0.0072 0.0171 0.2003 166 ARG B C 3001 O O . ARG B 168 ? 0.2296 0.4321 0.7222 -0.0110 0.0169 0.2006 166 ARG B O 3002 C CB . ARG B 168 ? 0.3200 0.5152 0.8366 -0.0110 -0.0100 0.1784 166 ARG B CB 3003 C CG . ARG B 168 ? 0.3185 0.5130 0.8338 -0.0054 -0.0193 0.1660 166 ARG B CG 3004 C CD . ARG B 168 ? 0.3617 0.5349 0.8903 -0.0153 -0.0414 0.1586 166 ARG B CD 3005 N NE . ARG B 168 ? 0.2278 0.4031 0.7610 -0.0110 -0.0530 0.1508 166 ARG B NE 3006 C CZ . ARG B 168 ? 0.1990 0.3628 0.7113 -0.0050 -0.0595 0.1380 166 ARG B CZ 3007 N NH1 . ARG B 168 ? 0.1886 0.3400 0.6754 -0.0026 -0.0543 0.1315 166 ARG B NH1 3008 N NH2 . ARG B 168 ? 0.2056 0.3697 0.7223 -0.0011 -0.0723 0.1325 166 ARG B NH2 3009 N N . SER B 169 ? 0.2169 0.4623 0.7408 -0.0070 0.0224 0.2140 167 SER B N 3010 C CA . SER B 169 ? 0.2287 0.4843 0.7629 -0.0121 0.0274 0.2322 167 SER B CA 3011 C C . SER B 169 ? 0.2327 0.4621 0.7807 -0.0236 0.0122 0.2351 167 SER B C 3012 O O . SER B 169 ? 0.3724 0.5872 0.9385 -0.0299 -0.0035 0.2296 167 SER B O 3013 C CB . SER B 169 ? 0.3257 0.6133 0.8862 -0.0122 0.0317 0.2461 167 SER B CB 3014 O OG . SER B 169 ? 0.4528 0.7351 1.0406 -0.0185 0.0169 0.2443 167 SER B OG 3015 N N . GLY B 170 ? 0.2350 0.4582 0.7740 -0.0252 0.0157 0.2422 168 GLY B N 3016 C CA . GLY B 170 ? 0.2788 0.4786 0.8315 -0.0338 0.0011 0.2439 168 GLY B CA 3017 C C . GLY B 170 ? 0.2887 0.4601 0.8193 -0.0329 -0.0035 0.2268 168 GLY B C 3018 O O . GLY B 170 ? 0.2325 0.3892 0.7659 -0.0364 -0.0099 0.2281 168 GLY B O 3019 N N . GLU B 171 ? 0.2666 0.4320 0.7771 -0.0280 -0.0007 0.2107 169 GLU B N 3020 C CA . GLU B 171 ? 0.2226 0.3634 0.7125 -0.0276 -0.0046 0.1938 169 GLU B CA 3021 C C . GLU B 171 ? 0.2004 0.3389 0.6693 -0.0240 0.0055 0.1964 169 GLU B C 3022 O O . GLU B 171 ? 0.2638 0.4210 0.7203 -0.0181 0.0197 0.2058 169 GLU B O 3023 C CB . GLU B 171 ? 0.2016 0.3413 0.6744 -0.0226 -0.0024 0.1792 169 GLU B CB 3024 C CG . GLU B 171 ? 0.1943 0.3281 0.6837 -0.0268 -0.0176 0.1708 169 GLU B CG 3025 C CD . GLU B 171 ? 0.1862 0.3208 0.6589 -0.0207 -0.0166 0.1580 169 GLU B CD 3026 O OE1 . GLU B 171 ? 0.2000 0.3460 0.6530 -0.0117 -0.0022 0.1585 169 GLU B OE1 3027 O OE2 . GLU B 171 ? 0.2979 0.4216 0.7764 -0.0242 -0.0317 0.1471 169 GLU B OE2 3028 N N . VAL B 172 ? 0.1985 0.3148 0.6633 -0.0271 -0.0024 0.1867 170 VAL B N 3029 C CA . VAL B 172 ? 0.1935 0.3052 0.6371 -0.0235 0.0057 0.1857 170 VAL B CA 3030 C C . VAL B 172 ? 0.1871 0.2802 0.6088 -0.0223 0.0049 0.1658 170 VAL B C 3031 O O . VAL B 172 ? 0.1827 0.2584 0.6110 -0.0272 -0.0076 0.1525 170 VAL B O 3032 C CB . VAL B 172 ? 0.2038 0.3091 0.6637 -0.0277 -0.0022 0.1933 170 VAL B CB 3033 C CG1 . VAL B 172 ? 0.2415 0.3402 0.6798 -0.0241 0.0043 0.1892 170 VAL B CG1 3034 C CG2 . VAL B 172 ? 0.2341 0.3604 0.7147 -0.0295 -0.0003 0.2157 170 VAL B CG2 3035 N N . TYR B 173 ? 0.1725 0.2701 0.5672 -0.0157 0.0179 0.1634 171 TYR B N 3036 C CA . TYR B 173 ? 0.1899 0.2716 0.5627 -0.0150 0.0187 0.1468 171 TYR B CA 3037 C C . TYR B 173 ? 0.1784 0.2510 0.5375 -0.0139 0.0221 0.1451 171 TYR B C 3038 O O . TYR B 173 ? 0.1895 0.2730 0.5472 -0.0107 0.0283 0.1576 171 TYR B O 3039 C CB . TYR B 173 ? 0.1541 0.2460 0.5072 -0.0078 0.0296 0.1447 171 TYR B CB 3040 C CG . TYR B 173 ? 0.1529 0.2539 0.5198 -0.0077 0.0246 0.1431 171 TYR B CG 3041 C CD1 . TYR B 173 ? 0.1598 0.2806 0.5430 -0.0055 0.0265 0.1552 171 TYR B CD1 3042 C CD2 . TYR B 173 ? 0.1484 0.2383 0.5103 -0.0097 0.0168 0.1288 171 TYR B CD2 3043 C CE1 . TYR B 173 ? 0.1597 0.2891 0.5562 -0.0045 0.0209 0.1528 171 TYR B CE1 3044 C CE2 . TYR B 173 ? 0.1563 0.2513 0.5249 -0.0076 0.0090 0.1257 171 TYR B CE2 3045 C CZ . TYR B 173 ? 0.1526 0.2710 0.5463 -0.0053 0.0114 0.1389 171 TYR B CZ 3046 O OH . TYR B 173 ? 0.1667 0.2928 0.5731 -0.0031 0.0030 0.1363 171 TYR B OH 3047 N N . THR B 174 ? 0.1590 0.2124 0.5081 -0.0168 0.0175 0.1294 172 THR B N 3048 C CA . THR B 174 ? 0.1588 0.2035 0.4969 -0.0158 0.0197 0.1260 172 THR B CA 3049 C C . THR B 174 ? 0.1519 0.1838 0.4617 -0.0145 0.0249 0.1117 172 THR B C 3050 O O . THR B 174 ? 0.1521 0.1717 0.4574 -0.0184 0.0196 0.0988 172 THR B O 3051 C CB . THR B 174 ? 0.1674 0.2002 0.5268 -0.0210 0.0066 0.1207 172 THR B CB 3052 O OG1 . THR B 174 ? 0.1763 0.2200 0.5630 -0.0228 0.0007 0.1359 172 THR B OG1 3053 C CG2 . THR B 174 ? 0.1672 0.1930 0.5185 -0.0194 0.0086 0.1175 172 THR B CG2 3054 N N . CYS B 175 ? 0.1485 0.1827 0.4380 -0.0094 0.0345 0.1145 173 CYS B N 3055 C CA . CYS B 175 ? 0.1446 0.1652 0.4078 -0.0086 0.0388 0.1022 173 CYS B CA 3056 C C . CYS B 175 ? 0.1473 0.1578 0.4144 -0.0105 0.0347 0.0960 173 CYS B C 3057 O O . CYS B 175 ? 0.1494 0.1674 0.4258 -0.0086 0.0349 0.1057 173 CYS B O 3058 C CB . CYS B 175 ? 0.1411 0.1699 0.3794 -0.0011 0.0504 0.1079 173 CYS B CB 3059 S SG . CYS B 175 ? 0.1943 0.2054 0.3997 -0.0004 0.0547 0.0945 173 CYS B SG 3060 N N . GLN B 176 ? 0.1490 0.1430 0.4100 -0.0141 0.0307 0.0799 174 GLN B N 3061 C CA . GLN B 176 ? 0.1527 0.1375 0.4210 -0.0151 0.0264 0.0716 174 GLN B CA 3062 C C . GLN B 176 ? 0.1498 0.1257 0.3934 -0.0136 0.0334 0.0619 174 GLN B C 3063 O O . GLN B 176 ? 0.1506 0.1210 0.3716 -0.0139 0.0350 0.0510 174 GLN B O 3064 C CB . GLN B 176 ? 0.1767 0.1506 0.4628 -0.0198 0.0142 0.0582 174 GLN B CB 3065 C CG . GLN B 176 ? 0.2211 0.1859 0.5178 -0.0194 0.0087 0.0471 174 GLN B CG 3066 C CD . GLN B 176 ? 0.2160 0.1686 0.5216 -0.0221 -0.0026 0.0278 174 GLN B CD 3067 O OE1 . GLN B 176 ? 0.4128 0.3560 0.7002 -0.0230 -0.0012 0.0108 174 GLN B OE1 3068 N NE2 . GLN B 176 ? 0.1961 0.1493 0.5283 -0.0233 -0.0145 0.0300 174 GLN B NE2 3069 N N . VAL B 177 ? 0.1487 0.1259 0.3932 -0.0109 0.0355 0.0645 175 VAL B N 3070 C CA . VAL B 177 ? 0.1459 0.1172 0.3691 -0.0092 0.0424 0.0578 175 VAL B CA 3071 C C . VAL B 177 ? 0.1498 0.1132 0.3870 -0.0097 0.0382 0.0466 175 VAL B C 3072 O O . VAL B 177 ? 0.1571 0.1240 0.4157 -0.0086 0.0324 0.0521 175 VAL B O 3073 C CB . VAL B 177 ? 0.1415 0.1231 0.3494 -0.0042 0.0493 0.0710 175 VAL B CB 3074 C CG1 . VAL B 177 ? 0.1583 0.1341 0.3474 -0.0028 0.0545 0.0648 175 VAL B CG1 3075 C CG2 . VAL B 177 ? 0.1397 0.1292 0.3329 -0.0017 0.0539 0.0787 175 VAL B CG2 3076 N N . GLU B 178 ? 0.1522 0.1103 0.3728 -0.0096 0.0398 0.0291 176 GLU B N 3077 C CA . GLU B 178 ? 0.1565 0.1106 0.3874 -0.0080 0.0376 0.0156 176 GLU B CA 3078 C C . GLU B 178 ? 0.1520 0.1104 0.3598 -0.0059 0.0458 0.0135 176 GLU B C 3079 O O . GLU B 178 ? 0.1720 0.1332 0.3510 -0.0068 0.0510 0.0124 176 GLU B O 3080 C CB . GLU B 178 ? 0.1732 0.1231 0.4045 -0.0090 0.0320 -0.0060 176 GLU B CB 3081 C CG . GLU B 178 ? 0.2921 0.2353 0.5512 -0.0111 0.0207 -0.0069 176 GLU B CG 3082 C CD . GLU B 178 ? 0.4509 0.3911 0.7006 -0.0121 0.0152 -0.0276 176 GLU B CD 3083 O OE1 . GLU B 178 ? 0.5979 0.5315 0.8673 -0.0104 0.0065 -0.0431 176 GLU B OE1 3084 O OE2 . GLU B 178 ? 0.5298 0.4736 0.7521 -0.0144 0.0186 -0.0288 176 GLU B OE2 3085 N N . HIS B 179 ? 0.1519 0.1100 0.3744 -0.0033 0.0453 0.0130 177 HIS B N 3086 C CA . HIS B 179 ? 0.1474 0.1102 0.3530 -0.0015 0.0518 0.0146 177 HIS B CA 3087 C C . HIS B 179 ? 0.1644 0.1268 0.3934 0.0017 0.0486 0.0076 177 HIS B C 3088 O O . HIS B 179 ? 0.1627 0.1194 0.4215 0.0029 0.0411 0.0099 177 HIS B O 3089 C CB . HIS B 179 ? 0.1420 0.1069 0.3383 -0.0008 0.0549 0.0351 177 HIS B CB 3090 C CG . HIS B 179 ? 0.1394 0.1074 0.3161 0.0007 0.0596 0.0369 177 HIS B CG 3091 N ND1 . HIS B 179 ? 0.1455 0.1144 0.3338 0.0031 0.0582 0.0438 177 HIS B ND1 3092 C CD2 . HIS B 179 ? 0.1476 0.1171 0.2955 -0.0004 0.0639 0.0331 177 HIS B CD2 3093 C CE1 . HIS B 179 ? 0.1983 0.1697 0.3656 0.0036 0.0617 0.0433 177 HIS B CE1 3094 N NE2 . HIS B 179 ? 0.1702 0.1416 0.3134 0.0012 0.0650 0.0370 177 HIS B NE2 3095 N N . PRO B 180 ? 0.1490 0.1176 0.3670 0.0030 0.0534 -0.0007 178 PRO B N 3096 C CA . PRO B 180 ? 0.1523 0.1222 0.3953 0.0073 0.0502 -0.0090 178 PRO B CA 3097 C C . PRO B 180 ? 0.1750 0.1396 0.4414 0.0094 0.0441 0.0076 178 PRO B C 3098 O O . PRO B 180 ? 0.1956 0.1575 0.4908 0.0133 0.0377 0.0018 178 PRO B O 3099 C CB . PRO B 180 ? 0.1496 0.1302 0.3740 0.0070 0.0576 -0.0157 178 PRO B CB 3100 C CG . PRO B 180 ? 0.1645 0.1481 0.3569 0.0020 0.0633 -0.0185 178 PRO B CG 3101 C CD . PRO B 180 ? 0.1979 0.1729 0.3838 0.0003 0.0608 -0.0045 178 PRO B CD 3102 N N . SER B 181 ? 0.1474 0.1113 0.4015 0.0075 0.0457 0.0277 179 SER B N 3103 C CA . SER B 181 ? 0.1492 0.1142 0.4174 0.0083 0.0399 0.0450 179 SER B CA 3104 C C . SER B 181 ? 0.1653 0.1320 0.4539 0.0063 0.0310 0.0506 179 SER B C 3105 O O . SER B 181 ? 0.1885 0.1593 0.4910 0.0059 0.0243 0.0626 179 SER B O 3106 C CB . SER B 181 ? 0.2212 0.1912 0.4630 0.0078 0.0448 0.0618 179 SER B CB 3107 O OG . SER B 181 ? 0.1625 0.1351 0.3917 0.0061 0.0471 0.0671 179 SER B OG 3108 N N . LEU B 182 ? 0.1559 0.1192 0.4461 0.0045 0.0305 0.0426 180 LEU B N 3109 C CA . LEU B 182 ? 0.1638 0.1285 0.4737 0.0021 0.0215 0.0484 180 LEU B CA 3110 C C . LEU B 182 ? 0.2403 0.1985 0.5748 0.0029 0.0122 0.0308 180 LEU B C 3111 O O . LEU B 182 ? 0.2862 0.2400 0.6161 0.0053 0.0150 0.0106 180 LEU B O 3112 C CB . LEU B 182 ? 0.1586 0.1249 0.4548 -0.0004 0.0252 0.0527 180 LEU B CB 3113 C CG . LEU B 182 ? 0.1517 0.1257 0.4211 0.0002 0.0340 0.0672 180 LEU B CG 3114 C CD1 . LEU B 182 ? 0.1494 0.1244 0.4074 -0.0016 0.0369 0.0673 180 LEU B CD1 3115 C CD2 . LEU B 182 ? 0.1718 0.1562 0.4472 0.0008 0.0312 0.0860 180 LEU B CD2 3116 N N . THR B 183 ? 0.1918 0.1509 0.5518 0.0014 0.0009 0.0377 181 THR B N 3117 C CA . THR B 183 ? 0.1933 0.1461 0.5779 0.0027 -0.0104 0.0212 181 THR B CA 3118 C C . THR B 183 ? 0.2303 0.1800 0.6217 0.0002 -0.0164 0.0179 181 THR B C 3119 O O . THR B 183 ? 0.2453 0.1890 0.6527 0.0018 -0.0260 0.0014 181 THR B O 3120 C CB . THR B 183 ? 0.2034 0.1569 0.6156 0.0024 -0.0218 0.0299 181 THR B CB 3121 O OG1 . THR B 183 ? 0.2078 0.1683 0.6234 -0.0019 -0.0235 0.0547 181 THR B OG1 3122 C CG2 . THR B 183 ? 0.2784 0.2331 0.6876 0.0056 -0.0184 0.0277 181 THR B CG2 3123 N N . SER B 184 ? 0.1915 0.1460 0.5705 -0.0032 -0.0114 0.0331 182 SER B N 3124 C CA . SER B 184 ? 0.1955 0.1482 0.5789 -0.0060 -0.0161 0.0316 182 SER B CA 3125 C C . SER B 184 ? 0.1898 0.1489 0.5482 -0.0078 -0.0049 0.0435 182 SER B C 3126 O O . SER B 184 ? 0.1904 0.1564 0.5335 -0.0069 0.0038 0.0561 182 SER B O 3127 C CB . SER B 184 ? 0.2233 0.1783 0.6375 -0.0087 -0.0295 0.0437 182 SER B CB 3128 O OG . SER B 184 ? 0.3403 0.3067 0.7547 -0.0109 -0.0261 0.0684 182 SER B OG 3129 N N . PRO B 185 ? 0.1842 0.1409 0.5375 -0.0100 -0.0058 0.0386 183 PRO B N 3130 C CA . PRO B 185 ? 0.1740 0.1367 0.5040 -0.0112 0.0044 0.0482 183 PRO B CA 3131 C C . PRO B 185 ? 0.1703 0.1469 0.5026 -0.0113 0.0073 0.0719 183 PRO B C 3132 O O . PRO B 185 ? 0.1894 0.1710 0.5459 -0.0129 -0.0009 0.0826 183 PRO B O 3133 C CB . PRO B 185 ? 0.2554 0.2135 0.5891 -0.0142 -0.0016 0.0399 183 PRO B CB 3134 C CG . PRO B 185 ? 0.2637 0.2105 0.6093 -0.0132 -0.0111 0.0184 183 PRO B CG 3135 C CD . PRO B 185 ? 0.2366 0.1847 0.6033 -0.0109 -0.0166 0.0223 183 PRO B CD 3136 N N . LEU B 186 ? 0.1615 0.1447 0.4681 -0.0093 0.0186 0.0792 184 LEU B N 3137 C CA . LEU B 186 ? 0.1601 0.1580 0.4630 -0.0079 0.0229 0.0987 184 LEU B CA 3138 C C . LEU B 186 ? 0.1584 0.1620 0.4579 -0.0088 0.0249 0.1023 184 LEU B C 3139 O O . LEU B 186 ? 0.1848 0.1833 0.4663 -0.0087 0.0294 0.0930 184 LEU B O 3140 C CB . LEU B 186 ? 0.2139 0.2153 0.4898 -0.0038 0.0327 0.1018 184 LEU B CB 3141 C CG . LEU B 186 ? 0.3475 0.3643 0.6125 -0.0007 0.0384 0.1186 184 LEU B CG 3142 C CD1 . LEU B 186 ? 0.3969 0.4230 0.6868 -0.0027 0.0318 0.1335 184 LEU B CD1 3143 C CD2 . LEU B 186 ? 0.3045 0.3209 0.5443 0.0033 0.0449 0.1177 184 LEU B CD2 3144 N N . THR B 187 ? 0.1638 0.1782 0.4825 -0.0102 0.0207 0.1163 185 THR B N 3145 C CA . THR B 187 ? 0.1630 0.1844 0.4830 -0.0109 0.0219 0.1207 185 THR B CA 3146 C C . THR B 187 ? 0.2453 0.2854 0.5610 -0.0077 0.0288 0.1391 185 THR B C 3147 O O . THR B 187 ? 0.1830 0.2318 0.5077 -0.0076 0.0277 0.1519 185 THR B O 3148 C CB . THR B 187 ? 0.1710 0.1883 0.5205 -0.0159 0.0094 0.1190 185 THR B CB 3149 O OG1 . THR B 187 ? 0.2304 0.2533 0.6049 -0.0175 0.0021 0.1317 185 THR B OG1 3150 C CG2 . THR B 187 ? 0.2390 0.2381 0.5895 -0.0181 0.0024 0.0978 185 THR B CG2 3151 N N . VAL B 188 ? 0.1605 0.2073 0.4625 -0.0052 0.0356 0.1399 186 VAL B N 3152 C CA . VAL B 188 ? 0.1642 0.2302 0.4626 -0.0013 0.0425 0.1553 186 VAL B CA 3153 C C . VAL B 188 ? 0.1651 0.2376 0.4764 -0.0028 0.0409 0.1582 186 VAL B C 3154 O O . VAL B 188 ? 0.1587 0.2234 0.4631 -0.0032 0.0410 0.1470 186 VAL B O 3155 C CB . VAL B 188 ? 0.1663 0.2365 0.4319 0.0059 0.0536 0.1532 186 VAL B CB 3156 C CG1 . VAL B 188 ? 0.1684 0.2593 0.4293 0.0109 0.0610 0.1661 186 VAL B CG1 3157 C CG2 . VAL B 188 ? 0.1894 0.2554 0.4438 0.0072 0.0544 0.1527 186 VAL B CG2 3158 N N . GLU B 189 ? 0.1742 0.2615 0.5056 -0.0043 0.0389 0.1740 187 GLU B N 3159 C CA . GLU B 189 ? 0.1918 0.2873 0.5387 -0.0061 0.0370 0.1787 187 GLU B CA 3160 C C . GLU B 189 ? 0.2188 0.3340 0.5514 0.0003 0.0487 0.1866 187 GLU B C 3161 O O . GLU B 189 ? 0.1934 0.3202 0.5100 0.0053 0.0569 0.1936 187 GLU B O 3162 C CB . GLU B 189 ? 0.2487 0.3492 0.6289 -0.0122 0.0270 0.1916 187 GLU B CB 3163 C CG . GLU B 189 ? 0.2519 0.3334 0.6509 -0.0179 0.0131 0.1820 187 GLU B CG 3164 C CD . GLU B 189 ? 0.3495 0.4356 0.7826 -0.0235 0.0019 0.1956 187 GLU B CD 3165 O OE1 . GLU B 189 ? 0.3782 0.4493 0.8301 -0.0277 -0.0115 0.1872 187 GLU B OE1 3166 O OE2 . GLU B 189 ? 0.3087 0.4142 0.7498 -0.0236 0.0061 0.2145 187 GLU B OE2 3167 N N . TRP B 190 ? 0.1762 0.2960 0.5153 0.0002 0.0488 0.1844 188 TRP B N 3168 C CA . TRP B 190 ? 0.1799 0.3210 0.5118 0.0065 0.0587 0.1912 188 TRP B CA 3169 C C . TRP B 190 ? 0.1849 0.3352 0.5451 0.0018 0.0529 0.1977 188 TRP B C 3170 O O . TRP B 190 ? 0.1800 0.3169 0.5533 -0.0033 0.0434 0.1890 188 TRP B O 3171 C CB . TRP B 190 ? 0.1705 0.3080 0.4769 0.0136 0.0655 0.1778 188 TRP B CB 3172 C CG . TRP B 190 ? 0.1755 0.3354 0.4746 0.0221 0.0750 0.1812 188 TRP B CG 3173 C CD1 . TRP B 190 ? 0.2210 0.3959 0.4992 0.0309 0.0854 0.1846 188 TRP B CD1 3174 C CD2 . TRP B 190 ? 0.1752 0.3461 0.4887 0.0235 0.0740 0.1798 188 TRP B CD2 3175 N NE1 . TRP B 190 ? 0.2059 0.4007 0.4841 0.0384 0.0915 0.1841 188 TRP B NE1 3176 C CE2 . TRP B 190 ? 0.2297 0.4229 0.5304 0.0341 0.0847 0.1816 188 TRP B CE2 3177 C CE3 . TRP B 190 ? 0.1707 0.3354 0.5073 0.0172 0.0640 0.1762 188 TRP B CE3 3178 C CZ2 . TRP B 190 ? 0.2115 0.4212 0.5229 0.0393 0.0861 0.1794 188 TRP B CZ2 3179 C CZ3 . TRP B 190 ? 0.1726 0.3534 0.5198 0.0215 0.0646 0.1755 188 TRP B CZ3 3180 C CH2 . TRP B 190 ? 0.1795 0.3827 0.5148 0.0328 0.0759 0.1770 188 TRP B CH2 3181 N N . ARG B 191 ? 0.1965 0.3704 0.5667 0.0030 0.0582 0.2130 189 ARG B N 3182 C CA . ARG B 191 ? 0.2431 0.4282 0.6417 -0.0016 0.0531 0.2208 189 ARG B CA 3183 C C . ARG B 191 ? 0.2053 0.4141 0.5985 0.0059 0.0635 0.2213 189 ARG B C 3184 O O . ARG B 191 ? 0.2902 0.5161 0.6643 0.0139 0.0755 0.2242 189 ARG B O 3185 C CB . ARG B 191 ? 0.2362 0.4317 0.6588 -0.0078 0.0489 0.2397 189 ARG B CB 3186 N N . ALA B 192 ? 0.2304 0.4405 0.6408 0.0040 0.0578 0.2169 190 ALA B N 3187 C CA . ALA B 192 ? 0.3350 0.5707 0.7490 0.0108 0.0656 0.2181 190 ALA B CA 3188 C C . ALA B 192 ? 0.3120 0.5715 0.7506 0.0065 0.0674 0.2374 190 ALA B C 3189 O O . ALA B 192 ? 0.3076 0.5597 0.7725 -0.0036 0.0562 0.2458 190 ALA B O 3190 C CB . ALA B 192 ? 0.3665 0.5950 0.7925 0.0102 0.0567 0.2066 190 ALA B CB 3191 N N . THR B 193 ? 0.5333 0.8219 0.9641 0.0142 0.0808 0.2441 191 THR B N 3192 C CA . THR B 193 ? 0.5002 0.7974 0.9009 0.0275 0.0924 0.2322 191 THR B CA 3193 C C . THR B 193 ? 0.5469 0.8358 0.9189 0.0305 0.0979 0.2323 191 THR B C 3194 O O . THR B 193 ? 0.5533 0.8264 0.8993 0.0367 0.0993 0.2181 191 THR B O 3195 C CB . THR B 193 ? 0.5737 0.9082 0.9797 0.0358 0.1040 0.2372 191 THR B CB 3196 O OG1 . THR B 193 ? 0.6117 0.9656 1.0160 0.0344 0.1117 0.2537 191 THR B OG1 3197 C CG2 . THR B 193 ? 0.4807 0.8279 0.9217 0.0310 0.0982 0.2419 191 THR B CG2 3198 N N . SER C 1 ? 0.4233 0.4339 0.5076 0.0270 -0.0362 0.1764 1 SER C N 3199 C CA . SER C 1 ? 0.3557 0.3468 0.4404 0.0355 -0.0280 0.1676 1 SER C CA 3200 C C . SER C 1 ? 0.3096 0.3196 0.3807 0.0306 -0.0343 0.1542 1 SER C C 3201 O O . SER C 1 ? 0.3235 0.3418 0.3771 0.0216 -0.0396 0.1481 1 SER C O 3202 C CB . SER C 1 ? 0.5335 0.4680 0.6010 0.0352 -0.0177 0.1614 1 SER C CB 3203 O OG . SER C 1 ? 0.6897 0.5987 0.7596 0.0469 -0.0034 0.1543 1 SER C OG 3204 N N . ALA C 2 ? 0.2507 0.2673 0.3309 0.0375 -0.0314 0.1508 2 ALA C N 3205 C CA . ALA C 2 ? 0.2127 0.2462 0.2796 0.0327 -0.0374 0.1393 2 ALA C CA 3206 C C . ALA C 2 ? 0.2248 0.2356 0.2815 0.0351 -0.0320 0.1259 2 ALA C C 3207 O O . ALA C 2 ? 0.2448 0.2303 0.3095 0.0436 -0.0218 0.1241 2 ALA C O 3208 C CB . ALA C 2 ? 0.2737 0.3336 0.3551 0.0329 -0.0412 0.1461 2 ALA C CB 3209 N N . VAL C 3 ? 0.1929 0.2111 0.2305 0.0277 -0.0358 0.1172 3 VAL C N 3210 C CA . VAL C 3 ? 0.1840 0.1910 0.2127 0.0263 -0.0308 0.1017 3 VAL C CA 3211 C C . VAL C 3 ? 0.1873 0.2044 0.2224 0.0318 -0.0303 0.0941 3 VAL C C 3212 O O . VAL C 3 ? 0.2064 0.2444 0.2391 0.0297 -0.0376 0.0994 3 VAL C O 3213 C CB . VAL C 3 ? 0.1750 0.1944 0.1879 0.0193 -0.0310 0.0991 3 VAL C CB 3214 C CG1 . VAL C 3 ? 0.1882 0.2046 0.1966 0.0176 -0.0256 0.0851 3 VAL C CG1 3215 C CG2 . VAL C 3 ? 0.2090 0.2246 0.2205 0.0112 -0.0332 0.1116 3 VAL C CG2 3216 N N . ARG C 4 ? 0.1728 0.1735 0.2117 0.0357 -0.0223 0.0831 4 ARG C N 3217 C CA . ARG C 4 ? 0.1618 0.1747 0.2103 0.0408 -0.0217 0.0785 4 ARG C CA 3218 C C . ARG C 4 ? 0.1723 0.1875 0.2060 0.0350 -0.0210 0.0620 4 ARG C C 3219 O O . ARG C 4 ? 0.1813 0.1839 0.2051 0.0301 -0.0166 0.0544 4 ARG C O 3220 C CB . ARG C 4 ? 0.1748 0.1682 0.2386 0.0526 -0.0087 0.0797 4 ARG C CB 3221 C CG . ARG C 4 ? 0.1932 0.1844 0.2802 0.0647 -0.0032 0.1019 4 ARG C CG 3222 C CD . ARG C 4 ? 0.2205 0.1808 0.3124 0.0777 0.0188 0.0988 4 ARG C CD 3223 N NE . ARG C 4 ? 0.2446 0.2047 0.3543 0.0862 0.0286 0.1151 4 ARG C NE 3224 C CZ . ARG C 4 ? 0.2814 0.2105 0.3916 0.0984 0.0523 0.1154 4 ARG C CZ 3225 N NH1 . ARG C 4 ? 0.2997 0.1933 0.3875 0.1006 0.0671 0.0977 4 ARG C NH1 3226 N NH2 . ARG C 4 ? 0.3052 0.2387 0.4358 0.1075 0.0631 0.1342 4 ARG C NH2 3227 N N . LEU C 5 ? 0.1616 0.1927 0.1932 0.0330 -0.0258 0.0594 5 LEU C N 3228 C CA A LEU C 5 ? 0.1726 0.2021 0.1935 0.0302 -0.0217 0.0452 5 LEU C CA 3229 C CA B LEU C 5 ? 0.1891 0.2190 0.2100 0.0301 -0.0219 0.0453 5 LEU C CA 3230 C C . LEU C 5 ? 0.1419 0.1708 0.1778 0.0350 -0.0178 0.0396 5 LEU C C 3231 O O . LEU C 5 ? 0.1576 0.1933 0.2122 0.0413 -0.0185 0.0492 5 LEU C O 3232 C CB A LEU C 5 ? 0.2742 0.3078 0.2733 0.0235 -0.0249 0.0425 5 LEU C CB 3233 C CB B LEU C 5 ? 0.3021 0.3368 0.3021 0.0231 -0.0259 0.0430 5 LEU C CB 3234 C CG A LEU C 5 ? 0.2904 0.3315 0.2870 0.0165 -0.0333 0.0425 5 LEU C CG 3235 C CG B LEU C 5 ? 0.2779 0.3246 0.2787 0.0156 -0.0378 0.0499 5 LEU C CG 3236 C CD1 A LEU C 5 ? 0.2500 0.2753 0.2075 0.0062 -0.0313 0.0342 5 LEU C CD1 3237 C CD1 B LEU C 5 ? 0.2362 0.2855 0.2419 0.0137 -0.0379 0.0422 5 LEU C CD1 3238 C CD2 A LEU C 5 ? 0.3054 0.3652 0.3178 0.0132 -0.0458 0.0613 5 LEU C CD2 3239 C CD2 B LEU C 5 ? 0.3274 0.3678 0.2921 0.0020 -0.0436 0.0518 5 LEU C CD2 3240 C C1 . CIR C 6 ? 0.1248 0.1634 0.1584 0.0309 -0.0136 0.0184 6 CIR C C1 3241 O O1 . CIR C 6 ? 0.1115 0.1456 0.1282 0.0271 -0.0110 0.0147 6 CIR C O1 3242 C C2 . CIR C 6 ? 0.1044 0.1322 0.1426 0.0349 -0.0092 0.0216 6 CIR C C2 3243 N N2 . CIR C 6 ? 0.1163 0.1422 0.1452 0.0324 -0.0130 0.0285 6 CIR C N2 3244 C C3 . CIR C 6 ? 0.1277 0.1454 0.1593 0.0306 -0.0026 0.0141 6 CIR C C3 3245 C C4 . CIR C 6 ? 0.2059 0.2245 0.2446 0.0331 0.0025 0.0073 6 CIR C C4 3246 C C5 . CIR C 6 ? 0.2920 0.2854 0.3244 0.0356 0.0127 0.0044 6 CIR C C5 3247 N N6 . CIR C 6 ? 0.1713 0.1558 0.2143 0.0478 0.0175 0.0137 6 CIR C N6 3248 C C7 . CIR C 6 ? 0.2276 0.2073 0.2852 0.0626 0.0308 0.0188 6 CIR C C7 3249 O O7 . CIR C 6 ? 0.2104 0.1921 0.2684 0.0640 0.0372 0.0126 6 CIR C O7 3250 N N8 . CIR C 6 ? 0.3029 0.2793 0.3793 0.0779 0.0387 0.0361 6 CIR C N8 3251 N N . SER C 7 ? 0.1429 0.1932 0.1889 0.0311 -0.0185 0.0222 7 SER C N 3252 C CA . SER C 7 ? 0.1329 0.1870 0.1675 0.0216 -0.0249 0.0195 7 SER C CA 3253 C C . SER C 7 ? 0.1851 0.2324 0.2152 0.0222 -0.0162 0.0076 7 SER C C 3254 O O . SER C 7 ? 0.1682 0.2179 0.2110 0.0281 -0.0090 0.0043 7 SER C O 3255 C CB . SER C 7 ? 0.1495 0.2253 0.2049 0.0189 -0.0346 0.0326 7 SER C CB 3256 O OG . SER C 7 ? 0.1962 0.2792 0.2754 0.0300 -0.0255 0.0317 7 SER C OG 3257 N N . SER C 8 ? 0.1213 0.1564 0.1292 0.0144 -0.0157 0.0026 8 SER C N 3258 C CA . SER C 8 ? 0.1019 0.1322 0.1100 0.0156 -0.0070 -0.0042 8 SER C CA 3259 C C . SER C 8 ? 0.1809 0.2187 0.1945 0.0068 -0.0169 -0.0032 8 SER C C 3260 O O . SER C 8 ? 0.2422 0.2813 0.2453 -0.0056 -0.0303 0.0031 8 SER C O 3261 C CB . SER C 8 ? 0.1410 0.1447 0.1198 0.0158 0.0065 -0.0080 8 SER C CB 3262 O OG . SER C 8 ? 0.1642 0.1715 0.1475 0.0248 0.0158 -0.0023 8 SER C OG 3263 N N . VAL C 9 ? 0.1063 0.1534 0.1373 0.0107 -0.0122 -0.0056 9 VAL C N 3264 C CA . VAL C 9 ? 0.1447 0.2088 0.1921 0.0051 -0.0212 -0.0006 9 VAL C CA 3265 C C . VAL C 9 ? 0.1175 0.1628 0.1452 -0.0060 -0.0206 -0.0057 9 VAL C C 3266 O O . VAL C 9 ? 0.1111 0.1420 0.1332 0.0001 -0.0063 -0.0119 9 VAL C O 3267 C CB . VAL C 9 ? 0.1085 0.1930 0.1854 0.0166 -0.0139 -0.0001 9 VAL C CB 3268 C CG1 . VAL C 9 ? 0.1776 0.2847 0.2762 0.0142 -0.0209 0.0094 9 VAL C CG1 3269 C CG2 . VAL C 9 ? 0.1727 0.2586 0.2568 0.0267 -0.0084 0.0011 9 VAL C CG2 3270 N N . PRO C 10 ? 0.1534 0.1988 0.1710 -0.0240 -0.0358 0.0004 10 PRO C N 3271 C CA . PRO C 10 ? 0.1527 0.1720 0.1461 -0.0382 -0.0353 -0.0049 10 PRO C CA 3272 C C . PRO C 10 ? 0.1396 0.1781 0.1652 -0.0282 -0.0282 -0.0043 10 PRO C C 3273 O O . PRO C 10 ? 0.1091 0.1861 0.1713 -0.0229 -0.0348 0.0056 10 PRO C O 3274 C CB . PRO C 10 ? 0.1925 0.2201 0.1747 -0.0651 -0.0597 0.0080 10 PRO C CB 3275 C CG . PRO C 10 ? 0.2852 0.3308 0.2719 -0.0654 -0.0693 0.0181 10 PRO C CG 3276 C CD . PRO C 10 ? 0.2354 0.3030 0.2600 -0.0356 -0.0547 0.0164 10 PRO C CD 3277 N N . GLY C 11 ? 0.1461 0.1574 0.1582 -0.0244 -0.0123 -0.0121 11 GLY C N 3278 C CA . GLY C 11 ? 0.1305 0.1617 0.1726 -0.0169 -0.0061 -0.0089 11 GLY C CA 3279 C C . GLY C 11 ? 0.1452 0.1771 0.1868 -0.0342 -0.0189 -0.0039 11 GLY C C 3280 O O . GLY C 11 ? 0.1899 0.2045 0.2035 -0.0559 -0.0339 -0.0020 11 GLY C O 3281 N N . VAL C 12 ? 0.1056 0.1592 0.1762 -0.0285 -0.0149 0.0008 12 VAL C N 3282 C CA . VAL C 12 ? 0.1552 0.2113 0.2280 -0.0456 -0.0269 0.0079 12 VAL C CA 3283 C C . VAL C 12 ? 0.2347 0.2314 0.2643 -0.0589 -0.0183 0.0002 12 VAL C C 3284 O O . VAL C 12 ? 0.2376 0.2078 0.2604 -0.0444 0.0051 -0.0051 12 VAL C O 3285 C CB . VAL C 12 ? 0.3443 0.4431 0.4613 -0.0357 -0.0248 0.0168 12 VAL C CB 3286 C CG1 . VAL C 12 ? 0.4857 0.6031 0.6050 -0.0333 -0.0338 0.0237 12 VAL C CG1 3287 C CG2 . VAL C 12 ? 0.4349 0.5426 0.5570 -0.0134 -0.0085 0.0102 12 VAL C CG2 3288 N N A ARG C 13 ? 0.2293 0.2032 0.2280 -0.0880 -0.0359 0.0028 13 ARG C N 3289 N N B ARG C 13 ? 0.2352 0.2091 0.2338 -0.0880 -0.0360 0.0028 13 ARG C N 3290 C CA A ARG C 13 ? 0.3438 0.2449 0.2864 -0.1061 -0.0264 -0.0067 13 ARG C CA 3291 C CA B ARG C 13 ? 0.3565 0.2593 0.3004 -0.1065 -0.0271 -0.0062 13 ARG C CA 3292 C C A ARG C 13 ? 0.3973 0.2990 0.3590 -0.1075 -0.0220 -0.0005 13 ARG C C 3293 C C B ARG C 13 ? 0.4009 0.3115 0.3682 -0.1090 -0.0260 0.0015 13 ARG C C 3294 O O A ARG C 13 ? 0.3780 0.2185 0.3056 -0.1083 -0.0010 -0.0081 13 ARG C O 3295 O O B ARG C 13 ? 0.2739 0.2490 0.2979 -0.0990 -0.0349 0.0144 13 ARG C O 3296 C CB . ARG C 13 ? 0.4433 0.3112 0.3304 -0.1453 -0.0497 -0.0065 13 ARG C CB 3297 C CG . ARG C 13 ? 0.5840 0.4515 0.4504 -0.1448 -0.0538 -0.0101 13 ARG C CG 3298 C CD . ARG C 13 ? 0.8588 0.7046 0.6735 -0.1711 -0.0691 -0.0033 13 ARG C CD 3299 N NE . ARG C 13 ? 1.0475 0.8856 0.8394 -0.1703 -0.0683 -0.0066 13 ARG C NE 3300 C CZ . ARG C 13 ? 1.1156 0.8938 0.8561 -0.1649 -0.0449 -0.0238 13 ARG C CZ 3301 N NH1 . ARG C 13 ? 1.1829 0.9037 0.8915 -0.1564 -0.0172 -0.0371 13 ARG C NH1 3302 N NH2 . ARG C 13 ? 1.0339 0.8126 0.7594 -0.1645 -0.0461 -0.0240 13 ARG C NH2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ILE 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 GLU 3 3 3 GLU GLU A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 HIS 5 5 5 HIS HIS A . n A 1 6 VAL 6 6 6 VAL VAL A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 ILE 8 8 8 ILE ILE A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 GLU 11 11 11 GLU GLU A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 TYR 13 13 13 TYR TYR A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 ASN 15 15 15 ASN ASN A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 PHE 22 22 22 PHE PHE A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 PHE 24 24 24 PHE PHE A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 GLU 30 30 30 GLU GLU A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 HIS 33 33 33 HIS HIS A . n A 1 34 VAL 34 34 34 VAL VAL A . n A 1 35 ASP 35 35 35 ASP ASP A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 LYS 38 38 38 LYS LYS A . n A 1 39 LYS 39 39 39 LYS LYS A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 TRP 43 43 43 TRP TRP A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 PHE 48 48 48 PHE PHE A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 GLU 55 55 55 GLU GLU A . n A 1 56 ALA 56 56 56 ALA ALA A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 ASP 66 66 66 ASP ASP A . n A 1 67 LYS 67 67 67 LYS LYS A . n A 1 68 ALA 68 68 68 ALA ALA A . n A 1 69 ASN 69 69 69 ASN ASN A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 ASN 78 78 78 ASN ASN A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 PRO 87 87 87 PRO PRO A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 THR 93 93 93 THR THR A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 GLU 101 101 101 GLU GLU A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 CYS 107 107 107 CYS CYS A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ILE 109 109 109 ILE ILE A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LYS 111 111 111 LYS LYS A . n A 1 112 PHE 112 112 112 PHE PHE A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 TRP 121 121 121 TRP TRP A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 ASN 124 124 124 ASN ASN A . n A 1 125 GLY 125 125 125 GLY GLY A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 PRO 127 127 127 PRO PRO A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 THR 129 129 129 THR THR A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 LEU 138 138 138 LEU LEU A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 ARG 140 140 140 ARG ARG A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 HIS 143 143 143 HIS HIS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 LYS 147 147 147 LYS LYS A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 HIS 149 149 149 HIS HIS A . n A 1 150 TYR 150 150 150 TYR TYR A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 CYS 163 163 163 CYS CYS A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 HIS 167 167 167 HIS HIS A . n A 1 168 TRP 168 168 168 TRP TRP A . n A 1 169 GLY 169 169 169 GLY GLY A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 PRO 173 173 173 PRO PRO A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 HIS 177 177 177 HIS HIS A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 PHE 180 180 180 PHE PHE A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 THR 182 182 182 THR THR 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 ARG 73 71 71 ARG ARG 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 VAL 88 86 86 VAL VAL 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 193 191 191 THR THR 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 SER 1 1 1 SER SER C . n C 3 2 ALA 2 2 2 ALA ALA C . n C 3 3 VAL 3 3 3 VAL VAL C . n C 3 4 ARG 4 4 4 ARG ARG C . n C 3 5 LEU 5 5 5 LEU LEU 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 VAL 9 9 9 VAL VAL C . n C 3 10 PRO 10 10 10 PRO PRO C . n C 3 11 GLY 11 11 11 GLY GLY C . n C 3 12 VAL 12 12 12 VAL VAL C . n C 3 13 ARG 13 13 13 ARG ARG C . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 118 A ASN 118 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 21 B ASN 19 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 78 A ASN 78 ? ASN 'GLYCOSYLATION SITE' 4 C CIR 6 C CIR 6 ? ARG CITRULLINE # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S # 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)' 8820 ? 1 MORE -8 ? 1 'SSA (A^2)' 18180 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 B HOH 447 ? R HOH . 2 1 B HOH 490 ? R HOH . # 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 41.7017 26.3749 -4.1731 0.0854 0.1126 0.0360 0.0127 -0.0120 0.0124 2.1335 4.8211 0.8722 -0.1817 -0.8565 -0.1666 -0.0821 -0.2048 -0.1329 0.2492 0.0765 0.0350 0.0203 0.0303 0.0527 'X-RAY DIFFRACTION' 2 ? refined 41.1092 18.2772 6.1038 0.2233 0.2452 0.1422 0.0272 -0.0027 0.0943 2.4589 2.3202 3.5281 -0.2859 -0.0506 -0.8594 -0.0095 -0.7324 -0.4659 0.5022 0.0222 -0.1779 0.0711 0.0355 0.0152 'X-RAY DIFFRACTION' 3 ? refined 51.7914 36.2469 -4.3418 0.0993 0.1269 0.1267 -0.0151 -0.0260 -0.0567 2.7534 4.8120 3.3969 0.0781 0.3546 -1.6784 0.0067 -0.2077 0.1329 0.4023 -0.0064 -0.4131 -0.2832 0.2450 0.0518 'X-RAY DIFFRACTION' 4 ? refined 23.8625 29.6415 -0.6676 0.1494 0.0981 0.0835 0.0228 0.0370 0.0027 3.8799 2.7435 1.7146 2.0502 -1.7592 -0.9031 -0.1779 0.0476 -0.1320 0.1733 0.1176 0.1917 0.0957 -0.2220 0.0330 'X-RAY DIFFRACTION' 5 ? refined 27.6256 32.0997 3.8314 0.1915 0.1401 0.0733 0.0322 0.0282 0.0060 2.1397 0.5105 1.4548 -0.0798 -1.3996 -0.3030 -0.0600 -0.3285 -0.0342 0.3035 0.0472 0.0840 -0.0204 0.2325 0.0768 'X-RAY DIFFRACTION' 6 ? refined 19.4549 32.3827 4.3740 0.1836 0.1217 0.1291 0.0274 0.0585 -0.0000 2.4929 2.3569 2.6998 0.5733 -1.7609 -0.6868 0.0110 -0.1254 0.2124 0.2958 0.0903 0.5248 -0.0296 -0.1200 -0.1120 'X-RAY DIFFRACTION' 7 ? refined 48.8267 24.6646 -13.5928 0.0749 0.0754 0.0889 0.0006 -0.0021 -0.0172 1.8008 1.7259 1.1205 -0.0650 -0.5173 -0.1120 -0.0792 -0.0046 -0.2111 -0.1046 0.0109 -0.1132 0.0416 0.0758 0.0516 'X-RAY DIFFRACTION' 8 ? refined 11.8774 10.9141 -6.7206 0.1413 0.1468 0.2891 0.0107 0.0630 0.0861 2.5631 1.6117 1.3814 -0.0714 1.2597 -0.1943 -0.0572 -0.2221 -0.5053 -0.0277 0.1711 0.3194 -0.0647 -0.2357 -0.0899 'X-RAY DIFFRACTION' 9 ? refined 54.2879 25.3681 -5.8802 0.1006 0.1531 0.1306 0.0184 -0.0244 0.0149 2.6908 4.0539 5.0325 1.8473 -1.6560 -4.4961 0.1098 -0.3030 -0.1988 0.4134 -0.2499 -0.3274 -0.1357 0.3470 0.1577 # 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 112 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 113 through 144 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 145 through 181 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 2 through 89 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 90 through 191 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1 through 13 ) ; # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal Blu-Ice 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.8.2_1309)' ? 3 MOSFLM 'data reduction' . ? 4 SCALA 'data scaling' . ? 5 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 100 ? ? 48.37 27.54 2 1 HIS B 33 ? ? 59.80 -115.57 3 1 THR B 90 ? ? -124.63 -72.29 4 1 ASN B 113 ? ? -140.77 18.98 5 1 PRO B 124 ? ? -79.92 -168.08 # 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 4 1 Y 1 B ARG 189 ? CG ? B ARG 191 CG 5 1 Y 1 B ARG 189 ? CD ? B ARG 191 CD 6 1 Y 1 B ARG 189 ? NE ? B ARG 191 NE 7 1 Y 1 B ARG 189 ? CZ ? B ARG 191 CZ 8 1 Y 1 B ARG 189 ? NH1 ? B ARG 191 NH1 9 1 Y 1 B ARG 189 ? NH2 ? B ARG 191 NH2 # 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 SER 183 ? A SER 183 4 1 Y 1 A GLY 184 ? A GLY 184 5 1 Y 1 A ASP 185 ? A ASP 185 6 1 Y 1 A ASP 186 ? A ASP 186 7 1 Y 1 A ASP 187 ? A ASP 187 8 1 Y 1 A ASP 188 ? A ASP 188 9 1 Y 1 A LYS 189 ? A LYS 189 10 1 Y 1 B GLY -1 ? B GLY 1 11 1 Y 1 B SER 0 ? B SER 2 12 1 Y 1 B GLY 1 ? B GLY 3 13 1 Y 1 B GLY 192 ? B GLY 194 14 1 Y 1 B GLY 193 ? B GLY 195 15 1 Y 1 B ASP 194 ? B ASP 196 16 1 Y 1 B ASP 195 ? B ASP 197 17 1 Y 1 B ASP 196 ? B ASP 198 18 1 Y 1 B ASP 197 ? B ASP 199 19 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 1,2-ETHANEDIOL EDO 6 'TRIETHYLENE GLYCOL' PGE 7 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 1 201 500 NAG NAG A . E 4 NAG 1 202 501 NAG NAG A . F 4 NAG 2 203 502 NAG NAG A . G 5 EDO 1 204 1 EDO EDO A . H 5 EDO 1 205 5 EDO EDO A . I 5 EDO 1 206 7 EDO EDO A . J 5 EDO 1 207 8 EDO EDO A . K 5 EDO 1 208 11 EDO EDO A . L 4 NAG 1 201 500 NAG NAG B . M 5 EDO 1 202 6 EDO EDO B . N 5 EDO 1 203 9 EDO EDO B . O 5 EDO 1 204 10 EDO EDO B . P 6 PGE 1 205 1 PGE PGE B . Q 7 HOH 1 301 1 HOH HOH A . Q 7 HOH 2 302 3 HOH HOH A . Q 7 HOH 3 303 8 HOH HOH A . Q 7 HOH 4 304 10 HOH HOH A . Q 7 HOH 5 305 11 HOH HOH A . Q 7 HOH 6 306 12 HOH HOH A . Q 7 HOH 7 307 14 HOH HOH A . Q 7 HOH 8 308 16 HOH HOH A . Q 7 HOH 9 309 21 HOH HOH A . Q 7 HOH 10 310 22 HOH HOH A . Q 7 HOH 11 311 23 HOH HOH A . Q 7 HOH 12 312 28 HOH HOH A . Q 7 HOH 13 313 29 HOH HOH A . Q 7 HOH 14 314 31 HOH HOH A . Q 7 HOH 15 315 34 HOH HOH A . Q 7 HOH 16 316 35 HOH HOH A . Q 7 HOH 17 317 37 HOH HOH A . Q 7 HOH 18 318 38 HOH HOH A . Q 7 HOH 19 319 39 HOH HOH A . Q 7 HOH 20 320 40 HOH HOH A . Q 7 HOH 21 321 41 HOH HOH A . Q 7 HOH 22 322 45 HOH HOH A . Q 7 HOH 23 323 46 HOH HOH A . Q 7 HOH 24 324 51 HOH HOH A . Q 7 HOH 25 325 52 HOH HOH A . Q 7 HOH 26 326 55 HOH HOH A . Q 7 HOH 27 327 56 HOH HOH A . Q 7 HOH 28 328 61 HOH HOH A . Q 7 HOH 29 329 62 HOH HOH A . Q 7 HOH 30 330 63 HOH HOH A . Q 7 HOH 31 331 64 HOH HOH A . Q 7 HOH 32 332 68 HOH HOH A . Q 7 HOH 33 333 69 HOH HOH A . Q 7 HOH 34 334 71 HOH HOH A . Q 7 HOH 35 335 73 HOH HOH A . Q 7 HOH 36 336 76 HOH HOH A . Q 7 HOH 37 337 77 HOH HOH A . Q 7 HOH 38 338 78 HOH HOH A . Q 7 HOH 39 339 79 HOH HOH A . Q 7 HOH 40 340 82 HOH HOH A . Q 7 HOH 41 341 83 HOH HOH A . Q 7 HOH 42 342 84 HOH HOH A . Q 7 HOH 43 343 85 HOH HOH A . Q 7 HOH 44 344 86 HOH HOH A . Q 7 HOH 45 345 91 HOH HOH A . Q 7 HOH 46 346 92 HOH HOH A . Q 7 HOH 47 347 93 HOH HOH A . Q 7 HOH 48 348 94 HOH HOH A . Q 7 HOH 49 349 96 HOH HOH A . Q 7 HOH 50 350 98 HOH HOH A . Q 7 HOH 51 351 100 HOH HOH A . Q 7 HOH 52 352 101 HOH HOH A . Q 7 HOH 53 353 104 HOH HOH A . Q 7 HOH 54 354 105 HOH HOH A . Q 7 HOH 55 355 108 HOH HOH A . Q 7 HOH 56 356 110 HOH HOH A . Q 7 HOH 57 357 111 HOH HOH A . Q 7 HOH 58 358 112 HOH HOH A . Q 7 HOH 59 359 115 HOH HOH A . Q 7 HOH 60 360 116 HOH HOH A . Q 7 HOH 61 361 122 HOH HOH A . Q 7 HOH 62 362 125 HOH HOH A . Q 7 HOH 63 363 133 HOH HOH A . Q 7 HOH 64 364 134 HOH HOH A . Q 7 HOH 65 365 135 HOH HOH A . Q 7 HOH 66 366 140 HOH HOH A . Q 7 HOH 67 367 142 HOH HOH A . Q 7 HOH 68 368 143 HOH HOH A . Q 7 HOH 69 369 145 HOH HOH A . Q 7 HOH 70 370 146 HOH HOH A . Q 7 HOH 71 371 148 HOH HOH A . Q 7 HOH 72 372 149 HOH HOH A . Q 7 HOH 73 373 150 HOH HOH A . Q 7 HOH 74 374 151 HOH HOH A . Q 7 HOH 75 375 153 HOH HOH A . Q 7 HOH 76 376 158 HOH HOH A . Q 7 HOH 77 377 161 HOH HOH A . Q 7 HOH 78 378 162 HOH HOH A . Q 7 HOH 79 379 164 HOH HOH A . Q 7 HOH 80 380 168 HOH HOH A . Q 7 HOH 81 381 169 HOH HOH A . Q 7 HOH 82 382 172 HOH HOH A . Q 7 HOH 83 383 173 HOH HOH A . Q 7 HOH 84 384 174 HOH HOH A . Q 7 HOH 85 385 177 HOH HOH A . Q 7 HOH 86 386 178 HOH HOH A . Q 7 HOH 87 387 179 HOH HOH A . Q 7 HOH 88 388 180 HOH HOH A . Q 7 HOH 89 389 184 HOH HOH A . Q 7 HOH 90 390 185 HOH HOH A . Q 7 HOH 91 391 186 HOH HOH A . Q 7 HOH 92 392 187 HOH HOH A . Q 7 HOH 93 393 189 HOH HOH A . Q 7 HOH 94 394 190 HOH HOH A . Q 7 HOH 95 395 193 HOH HOH A . Q 7 HOH 96 396 195 HOH HOH A . Q 7 HOH 97 397 196 HOH HOH A . Q 7 HOH 98 398 197 HOH HOH A . Q 7 HOH 99 399 198 HOH HOH A . Q 7 HOH 100 400 199 HOH HOH A . Q 7 HOH 101 401 201 HOH HOH A . Q 7 HOH 102 402 205 HOH HOH A . Q 7 HOH 103 403 207 HOH HOH A . Q 7 HOH 104 404 208 HOH HOH A . Q 7 HOH 105 405 213 HOH HOH A . Q 7 HOH 106 406 214 HOH HOH A . Q 7 HOH 107 407 216 HOH HOH A . Q 7 HOH 108 408 218 HOH HOH A . Q 7 HOH 109 409 220 HOH HOH A . Q 7 HOH 110 410 223 HOH HOH A . Q 7 HOH 111 411 224 HOH HOH A . Q 7 HOH 112 412 225 HOH HOH A . Q 7 HOH 113 413 226 HOH HOH A . Q 7 HOH 114 414 229 HOH HOH A . Q 7 HOH 115 415 230 HOH HOH A . Q 7 HOH 116 416 231 HOH HOH A . Q 7 HOH 117 417 233 HOH HOH A . Q 7 HOH 118 418 234 HOH HOH A . Q 7 HOH 119 419 235 HOH HOH A . Q 7 HOH 120 420 237 HOH HOH A . Q 7 HOH 121 421 238 HOH HOH A . Q 7 HOH 122 422 240 HOH HOH A . Q 7 HOH 123 423 241 HOH HOH A . Q 7 HOH 124 424 245 HOH HOH A . Q 7 HOH 125 425 246 HOH HOH A . Q 7 HOH 126 426 250 HOH HOH A . Q 7 HOH 127 427 251 HOH HOH A . Q 7 HOH 128 428 255 HOH HOH A . Q 7 HOH 129 429 256 HOH HOH A . Q 7 HOH 130 430 257 HOH HOH A . Q 7 HOH 131 431 260 HOH HOH A . Q 7 HOH 132 432 261 HOH HOH A . Q 7 HOH 133 433 263 HOH HOH A . Q 7 HOH 134 434 264 HOH HOH A . Q 7 HOH 135 435 265 HOH HOH A . Q 7 HOH 136 436 267 HOH HOH A . Q 7 HOH 137 437 269 HOH HOH A . Q 7 HOH 138 438 271 HOH HOH A . Q 7 HOH 139 439 273 HOH HOH A . Q 7 HOH 140 440 274 HOH HOH A . Q 7 HOH 141 441 275 HOH HOH A . Q 7 HOH 142 442 276 HOH HOH A . Q 7 HOH 143 443 277 HOH HOH A . Q 7 HOH 144 444 279 HOH HOH A . Q 7 HOH 145 445 280 HOH HOH A . Q 7 HOH 146 446 285 HOH HOH A . Q 7 HOH 147 447 286 HOH HOH A . Q 7 HOH 148 448 288 HOH HOH A . Q 7 HOH 149 449 289 HOH HOH A . Q 7 HOH 150 450 293 HOH HOH A . Q 7 HOH 151 451 294 HOH HOH A . Q 7 HOH 152 452 297 HOH HOH A . Q 7 HOH 153 453 300 HOH HOH A . Q 7 HOH 154 454 304 HOH HOH A . Q 7 HOH 155 455 306 HOH HOH A . Q 7 HOH 156 456 307 HOH HOH A . Q 7 HOH 157 457 308 HOH HOH A . Q 7 HOH 158 458 309 HOH HOH A . Q 7 HOH 159 459 310 HOH HOH A . Q 7 HOH 160 460 311 HOH HOH A . Q 7 HOH 161 461 313 HOH HOH A . Q 7 HOH 162 462 314 HOH HOH A . Q 7 HOH 163 463 315 HOH HOH A . Q 7 HOH 164 464 316 HOH HOH A . Q 7 HOH 165 465 317 HOH HOH A . Q 7 HOH 166 466 318 HOH HOH A . Q 7 HOH 167 467 323 HOH HOH A . Q 7 HOH 168 468 325 HOH HOH A . Q 7 HOH 169 469 326 HOH HOH A . Q 7 HOH 170 470 329 HOH HOH A . Q 7 HOH 171 471 330 HOH HOH A . Q 7 HOH 172 472 331 HOH HOH A . Q 7 HOH 173 473 332 HOH HOH A . Q 7 HOH 174 474 334 HOH HOH A . Q 7 HOH 175 475 335 HOH HOH A . Q 7 HOH 176 476 338 HOH HOH A . Q 7 HOH 177 477 340 HOH HOH A . Q 7 HOH 178 478 341 HOH HOH A . Q 7 HOH 179 479 342 HOH HOH A . Q 7 HOH 180 480 343 HOH HOH A . Q 7 HOH 181 481 344 HOH HOH A . Q 7 HOH 182 482 346 HOH HOH A . Q 7 HOH 183 483 350 HOH HOH A . Q 7 HOH 184 484 352 HOH HOH A . Q 7 HOH 185 485 353 HOH HOH A . Q 7 HOH 186 486 354 HOH HOH A . Q 7 HOH 187 487 355 HOH HOH A . Q 7 HOH 188 488 357 HOH HOH A . Q 7 HOH 189 489 358 HOH HOH A . Q 7 HOH 190 490 359 HOH HOH A . Q 7 HOH 191 491 362 HOH HOH A . Q 7 HOH 192 492 364 HOH HOH A . Q 7 HOH 193 493 365 HOH HOH A . Q 7 HOH 194 494 366 HOH HOH A . Q 7 HOH 195 495 369 HOH HOH A . Q 7 HOH 196 496 370 HOH HOH A . Q 7 HOH 197 497 371 HOH HOH A . Q 7 HOH 198 498 372 HOH HOH A . Q 7 HOH 199 499 373 HOH HOH A . Q 7 HOH 200 500 377 HOH HOH A . Q 7 HOH 201 501 380 HOH HOH A . Q 7 HOH 202 502 381 HOH HOH A . Q 7 HOH 203 503 384 HOH HOH A . Q 7 HOH 204 504 387 HOH HOH A . Q 7 HOH 205 505 389 HOH HOH A . Q 7 HOH 206 506 390 HOH HOH A . Q 7 HOH 207 507 392 HOH HOH A . Q 7 HOH 208 508 395 HOH HOH A . Q 7 HOH 209 509 396 HOH HOH A . Q 7 HOH 210 510 398 HOH HOH A . Q 7 HOH 211 511 399 HOH HOH A . Q 7 HOH 212 512 403 HOH HOH A . Q 7 HOH 213 513 406 HOH HOH A . Q 7 HOH 214 514 409 HOH HOH A . Q 7 HOH 215 515 415 HOH HOH A . Q 7 HOH 216 516 417 HOH HOH A . Q 7 HOH 217 517 421 HOH HOH A . Q 7 HOH 218 518 424 HOH HOH A . Q 7 HOH 219 519 429 HOH HOH A . Q 7 HOH 220 520 430 HOH HOH A . Q 7 HOH 221 521 433 HOH HOH A . Q 7 HOH 222 522 436 HOH HOH A . Q 7 HOH 223 523 437 HOH HOH A . Q 7 HOH 224 524 438 HOH HOH A . Q 7 HOH 225 525 439 HOH HOH A . Q 7 HOH 226 526 441 HOH HOH A . Q 7 HOH 227 527 442 HOH HOH A . Q 7 HOH 228 528 443 HOH HOH A . Q 7 HOH 229 529 444 HOH HOH A . Q 7 HOH 230 530 446 HOH HOH A . Q 7 HOH 231 531 448 HOH HOH A . Q 7 HOH 232 532 449 HOH HOH A . Q 7 HOH 233 533 450 HOH HOH A . Q 7 HOH 234 534 452 HOH HOH A . Q 7 HOH 235 535 455 HOH HOH A . Q 7 HOH 236 536 460 HOH HOH A . Q 7 HOH 237 537 463 HOH HOH A . Q 7 HOH 238 538 466 HOH HOH A . Q 7 HOH 239 539 468 HOH HOH A . Q 7 HOH 240 540 471 HOH HOH A . Q 7 HOH 241 541 474 HOH HOH A . Q 7 HOH 242 542 475 HOH HOH A . Q 7 HOH 243 543 480 HOH HOH A . Q 7 HOH 244 544 482 HOH HOH A . Q 7 HOH 245 545 490 HOH HOH A . Q 7 HOH 246 546 492 HOH HOH A . R 7 HOH 1 301 2 HOH HOH B . R 7 HOH 2 302 4 HOH HOH B . R 7 HOH 3 303 5 HOH HOH B . R 7 HOH 4 304 6 HOH HOH B . R 7 HOH 5 305 7 HOH HOH B . R 7 HOH 6 306 9 HOH HOH B . R 7 HOH 7 307 13 HOH HOH B . R 7 HOH 8 308 15 HOH HOH B . R 7 HOH 9 309 17 HOH HOH B . R 7 HOH 10 310 18 HOH HOH B . R 7 HOH 11 311 19 HOH HOH B . R 7 HOH 12 312 20 HOH HOH B . R 7 HOH 13 313 24 HOH HOH B . R 7 HOH 14 314 25 HOH HOH B . R 7 HOH 15 315 26 HOH HOH B . R 7 HOH 16 316 27 HOH HOH B . R 7 HOH 17 317 32 HOH HOH B . R 7 HOH 18 318 33 HOH HOH B . R 7 HOH 19 319 36 HOH HOH B . R 7 HOH 20 320 42 HOH HOH B . R 7 HOH 21 321 43 HOH HOH B . R 7 HOH 22 322 44 HOH HOH B . R 7 HOH 23 323 47 HOH HOH B . R 7 HOH 24 324 48 HOH HOH B . R 7 HOH 25 325 49 HOH HOH B . R 7 HOH 26 326 50 HOH HOH B . R 7 HOH 27 327 53 HOH HOH B . R 7 HOH 28 328 54 HOH HOH B . R 7 HOH 29 329 57 HOH HOH B . R 7 HOH 30 330 58 HOH HOH B . R 7 HOH 31 331 59 HOH HOH B . R 7 HOH 32 332 60 HOH HOH B . R 7 HOH 33 333 65 HOH HOH B . R 7 HOH 34 334 67 HOH HOH B . R 7 HOH 35 335 70 HOH HOH B . R 7 HOH 36 336 72 HOH HOH B . R 7 HOH 37 337 75 HOH HOH B . R 7 HOH 38 338 80 HOH HOH B . R 7 HOH 39 339 81 HOH HOH B . R 7 HOH 40 340 87 HOH HOH B . R 7 HOH 41 341 88 HOH HOH B . R 7 HOH 42 342 89 HOH HOH B . R 7 HOH 43 343 90 HOH HOH B . R 7 HOH 44 344 95 HOH HOH B . R 7 HOH 45 345 97 HOH HOH B . R 7 HOH 46 346 99 HOH HOH B . R 7 HOH 47 347 102 HOH HOH B . R 7 HOH 48 348 103 HOH HOH B . R 7 HOH 49 349 106 HOH HOH B . R 7 HOH 50 350 107 HOH HOH B . R 7 HOH 51 351 113 HOH HOH B . R 7 HOH 52 352 114 HOH HOH B . R 7 HOH 53 353 118 HOH HOH B . R 7 HOH 54 354 119 HOH HOH B . R 7 HOH 55 355 120 HOH HOH B . R 7 HOH 56 356 121 HOH HOH B . R 7 HOH 57 357 123 HOH HOH B . R 7 HOH 58 358 124 HOH HOH B . R 7 HOH 59 359 126 HOH HOH B . R 7 HOH 60 360 127 HOH HOH B . R 7 HOH 61 361 128 HOH HOH B . R 7 HOH 62 362 129 HOH HOH B . R 7 HOH 63 363 130 HOH HOH B . R 7 HOH 64 364 131 HOH HOH B . R 7 HOH 65 365 132 HOH HOH B . R 7 HOH 66 366 136 HOH HOH B . R 7 HOH 67 367 137 HOH HOH B . R 7 HOH 68 368 138 HOH HOH B . R 7 HOH 69 369 139 HOH HOH B . R 7 HOH 70 370 141 HOH HOH B . R 7 HOH 71 371 144 HOH HOH B . R 7 HOH 72 372 147 HOH HOH B . R 7 HOH 73 373 152 HOH HOH B . R 7 HOH 74 374 154 HOH HOH B . R 7 HOH 75 375 155 HOH HOH B . R 7 HOH 76 376 156 HOH HOH B . R 7 HOH 77 377 157 HOH HOH B . R 7 HOH 78 378 159 HOH HOH B . R 7 HOH 79 379 160 HOH HOH B . R 7 HOH 80 380 163 HOH HOH B . R 7 HOH 81 381 165 HOH HOH B . R 7 HOH 82 382 166 HOH HOH B . R 7 HOH 83 383 170 HOH HOH B . R 7 HOH 84 384 171 HOH HOH B . R 7 HOH 85 385 175 HOH HOH B . R 7 HOH 86 386 176 HOH HOH B . R 7 HOH 87 387 181 HOH HOH B . R 7 HOH 88 388 182 HOH HOH B . R 7 HOH 89 389 183 HOH HOH B . R 7 HOH 90 390 188 HOH HOH B . R 7 HOH 91 391 191 HOH HOH B . R 7 HOH 92 392 192 HOH HOH B . R 7 HOH 93 393 194 HOH HOH B . R 7 HOH 94 394 200 HOH HOH B . R 7 HOH 95 395 202 HOH HOH B . R 7 HOH 96 396 203 HOH HOH B . R 7 HOH 97 397 204 HOH HOH B . R 7 HOH 98 398 206 HOH HOH B . R 7 HOH 99 399 209 HOH HOH B . R 7 HOH 100 400 210 HOH HOH B . R 7 HOH 101 401 215 HOH HOH B . R 7 HOH 102 402 217 HOH HOH B . R 7 HOH 103 403 219 HOH HOH B . R 7 HOH 104 404 221 HOH HOH B . R 7 HOH 105 405 227 HOH HOH B . R 7 HOH 106 406 228 HOH HOH B . R 7 HOH 107 407 232 HOH HOH B . R 7 HOH 108 408 236 HOH HOH B . R 7 HOH 109 409 239 HOH HOH B . R 7 HOH 110 410 242 HOH HOH B . R 7 HOH 111 411 243 HOH HOH B . R 7 HOH 112 412 244 HOH HOH B . R 7 HOH 113 413 247 HOH HOH B . R 7 HOH 114 414 248 HOH HOH B . R 7 HOH 115 415 249 HOH HOH B . R 7 HOH 116 416 252 HOH HOH B . R 7 HOH 117 417 253 HOH HOH B . R 7 HOH 118 418 254 HOH HOH B . R 7 HOH 119 419 258 HOH HOH B . R 7 HOH 120 420 259 HOH HOH B . R 7 HOH 121 421 262 HOH HOH B . R 7 HOH 122 422 268 HOH HOH B . R 7 HOH 123 423 270 HOH HOH B . R 7 HOH 124 424 272 HOH HOH B . R 7 HOH 125 425 278 HOH HOH B . R 7 HOH 126 426 281 HOH HOH B . R 7 HOH 127 427 290 HOH HOH B . R 7 HOH 128 428 291 HOH HOH B . R 7 HOH 129 429 292 HOH HOH B . R 7 HOH 130 430 296 HOH HOH B . R 7 HOH 131 431 298 HOH HOH B . R 7 HOH 132 432 299 HOH HOH B . R 7 HOH 133 433 302 HOH HOH B . R 7 HOH 134 434 303 HOH HOH B . R 7 HOH 135 435 312 HOH HOH B . R 7 HOH 136 436 319 HOH HOH B . R 7 HOH 137 437 320 HOH HOH B . R 7 HOH 138 438 321 HOH HOH B . R 7 HOH 139 439 322 HOH HOH B . R 7 HOH 140 440 324 HOH HOH B . R 7 HOH 141 441 327 HOH HOH B . R 7 HOH 142 442 328 HOH HOH B . R 7 HOH 143 443 333 HOH HOH B . R 7 HOH 144 444 336 HOH HOH B . R 7 HOH 145 445 337 HOH HOH B . R 7 HOH 146 446 339 HOH HOH B . R 7 HOH 147 447 345 HOH HOH B . R 7 HOH 148 448 347 HOH HOH B . R 7 HOH 149 449 348 HOH HOH B . R 7 HOH 150 450 351 HOH HOH B . R 7 HOH 151 451 356 HOH HOH B . R 7 HOH 152 452 360 HOH HOH B . R 7 HOH 153 453 361 HOH HOH B . R 7 HOH 154 454 367 HOH HOH B . R 7 HOH 155 455 368 HOH HOH B . R 7 HOH 156 456 375 HOH HOH B . R 7 HOH 157 457 378 HOH HOH B . R 7 HOH 158 458 382 HOH HOH B . R 7 HOH 159 459 383 HOH HOH B . R 7 HOH 160 460 386 HOH HOH B . R 7 HOH 161 461 388 HOH HOH B . R 7 HOH 162 462 391 HOH HOH B . R 7 HOH 163 463 393 HOH HOH B . R 7 HOH 164 464 394 HOH HOH B . R 7 HOH 165 465 397 HOH HOH B . R 7 HOH 166 466 401 HOH HOH B . R 7 HOH 167 467 402 HOH HOH B . R 7 HOH 168 468 404 HOH HOH B . R 7 HOH 169 469 405 HOH HOH B . R 7 HOH 170 470 407 HOH HOH B . R 7 HOH 171 471 408 HOH HOH B . R 7 HOH 172 472 411 HOH HOH B . R 7 HOH 173 473 412 HOH HOH B . R 7 HOH 174 474 413 HOH HOH B . R 7 HOH 175 475 414 HOH HOH B . R 7 HOH 176 476 423 HOH HOH B . R 7 HOH 177 477 425 HOH HOH B . R 7 HOH 178 478 426 HOH HOH B . R 7 HOH 179 479 427 HOH HOH B . R 7 HOH 180 480 428 HOH HOH B . R 7 HOH 181 481 431 HOH HOH B . R 7 HOH 182 482 432 HOH HOH B . R 7 HOH 183 483 434 HOH HOH B . R 7 HOH 184 484 435 HOH HOH B . R 7 HOH 185 485 440 HOH HOH B . R 7 HOH 186 486 445 HOH HOH B . R 7 HOH 187 487 451 HOH HOH B . R 7 HOH 188 488 453 HOH HOH B . R 7 HOH 189 489 454 HOH HOH B . R 7 HOH 190 490 456 HOH HOH B . R 7 HOH 191 491 457 HOH HOH B . R 7 HOH 192 492 458 HOH HOH B . R 7 HOH 193 493 459 HOH HOH B . R 7 HOH 194 494 464 HOH HOH B . R 7 HOH 195 495 469 HOH HOH B . R 7 HOH 196 496 470 HOH HOH B . R 7 HOH 197 497 478 HOH HOH B . R 7 HOH 198 498 479 HOH HOH B . R 7 HOH 199 499 483 HOH HOH B . R 7 HOH 200 500 484 HOH HOH B . R 7 HOH 201 501 485 HOH HOH B . R 7 HOH 202 502 486 HOH HOH B . R 7 HOH 203 503 487 HOH HOH B . S 7 HOH 1 101 30 HOH HOH C . S 7 HOH 2 102 66 HOH HOH C . S 7 HOH 3 103 74 HOH HOH C . S 7 HOH 4 104 109 HOH HOH C . S 7 HOH 5 105 117 HOH HOH C . S 7 HOH 6 106 167 HOH HOH C . S 7 HOH 7 107 211 HOH HOH C . S 7 HOH 8 108 212 HOH HOH C . S 7 HOH 9 109 266 HOH HOH C . S 7 HOH 10 110 282 HOH HOH C . S 7 HOH 11 111 287 HOH HOH C . S 7 HOH 12 112 295 HOH HOH C . S 7 HOH 13 113 301 HOH HOH C . S 7 HOH 14 114 305 HOH HOH C . S 7 HOH 15 115 374 HOH HOH C . S 7 HOH 16 116 410 HOH HOH C . S 7 HOH 17 117 477 HOH HOH C . #