data_4MDI # _entry.id 4MDI # _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 4MDI RCSB RCSB081773 WWPDB D_1000081773 # 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 4MD5 . unspecified PDB 4MDJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MDI _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 4MDI _cell.length_a 67.021 _cell.length_b 182.930 _cell.length_c 77.377 _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 4MDI _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' 23253.588 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 1 ? ? ? ? 6 water nat water 18.015 397 ? ? ? ? # 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 ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDILEDERAAVDTY CRHNYGVVESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDILEDERAAVDTY 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 ILE n 2 70 LEU n 2 71 GLU n 2 72 ASP n 2 73 GLU 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 4MDI A 1 ? 181 ? P01903 26 ? 206 ? 1 181 2 2 4MDI B 3 ? 192 ? P13760 30 ? 219 ? 1 190 3 3 4MDI 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 4MDI THR A 182 ? UNP P01903 ? ? 'EXPRESSION TAG' 182 1 1 4MDI SER A 183 ? UNP P01903 ? ? 'EXPRESSION TAG' 183 2 1 4MDI GLY A 184 ? UNP P01903 ? ? 'EXPRESSION TAG' 184 3 1 4MDI ASP A 185 ? UNP P01903 ? ? 'EXPRESSION TAG' 185 4 1 4MDI ASP A 186 ? UNP P01903 ? ? 'EXPRESSION TAG' 186 5 1 4MDI ASP A 187 ? UNP P01903 ? ? 'EXPRESSION TAG' 187 6 1 4MDI ASP A 188 ? UNP P01903 ? ? 'EXPRESSION TAG' 188 7 1 4MDI LYS A 189 ? UNP P01903 ? ? 'EXPRESSION TAG' 189 8 2 4MDI GLY B 1 ? UNP P13760 ? ? 'EXPRESSION TAG' -1 9 2 4MDI SER B 2 ? UNP P13760 ? ? 'EXPRESSION TAG' 0 10 2 4MDI ILE B 69 ? UNP P13760 LEU 96 VARIANT 67 11 2 4MDI ASP B 72 ? UNP P13760 GLN 99 VARIANT 70 12 2 4MDI GLU B 73 ? UNP P13760 LYS 100 VARIANT 71 13 2 4MDI VAL B 88 ? UNP P13760 GLY 115 VARIANT 86 14 2 4MDI THR B 193 ? UNP P13760 ? ? 'EXPRESSION TAG' 191 15 2 4MDI GLY B 194 ? UNP P13760 ? ? 'EXPRESSION TAG' 192 16 2 4MDI GLY B 195 ? UNP P13760 ? ? 'EXPRESSION TAG' 193 17 2 4MDI ASP B 196 ? UNP P13760 ? ? 'EXPRESSION TAG' 194 18 2 4MDI ASP B 197 ? UNP P13760 ? ? 'EXPRESSION TAG' 195 19 2 4MDI ASP B 198 ? UNP P13760 ? ? 'EXPRESSION TAG' 196 20 2 4MDI ASP B 199 ? UNP P13760 ? ? 'EXPRESSION TAG' 197 21 2 4MDI LYS B 200 ? UNP P13760 ? ? 'EXPRESSION TAG' 198 22 # 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 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 4MDI _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 53.87 _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 '25% 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 2012-11-15 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.95370 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' _diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' _diffrn_source.pdbx_synchrotron_beamline MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.95370 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MDI _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 62.93 _reflns.d_resolution_high 2.0 _reflns.number_obs 32616 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs 0.122 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.0 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.0 _reflns_shell.d_res_low 2.11 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.472 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.5 _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 4MDI _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 32597 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.34 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 39.370 _refine.ls_d_res_high 2.000 _refine.ls_percent_reflns_obs 99.98 _refine.ls_R_factor_obs 0.1632 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1610 _refine.ls_R_factor_R_free 0.2031 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.17 _refine.ls_number_reflns_R_free 1684 _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 18.10 _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 3137 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 60 _refine_hist.number_atoms_solvent 397 _refine_hist.number_atoms_total 3594 _refine_hist.d_res_high 2.000 _refine_hist.d_res_low 39.370 # 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 0.007 ? ? 3380 'X-RAY DIFFRACTION' ? f_angle_d 1.141 ? ? 4608 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 17.217 ? ? 1264 'X-RAY DIFFRACTION' ? f_chiral_restr 0.081 ? ? 497 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 604 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.0000 2.0589 2513 0.1971 100.00 0.2450 . . 155 . . . . 'X-RAY DIFFRACTION' . 2.0589 2.1253 2541 0.1792 100.00 0.2138 . . 147 . . . . 'X-RAY DIFFRACTION' . 2.1253 2.2013 2539 0.1696 100.00 0.2410 . . 129 . . . . 'X-RAY DIFFRACTION' . 2.2013 2.2894 2551 0.1692 100.00 0.2209 . . 143 . . . . 'X-RAY DIFFRACTION' . 2.2894 2.3936 2575 0.1665 100.00 0.2184 . . 125 . . . . 'X-RAY DIFFRACTION' . 2.3936 2.5198 2565 0.1683 100.00 0.2005 . . 123 . . . . 'X-RAY DIFFRACTION' . 2.5198 2.6776 2558 0.1682 100.00 0.2090 . . 136 . . . . 'X-RAY DIFFRACTION' . 2.6776 2.8843 2569 0.1681 100.00 0.2348 . . 140 . . . . 'X-RAY DIFFRACTION' . 2.8843 3.1744 2551 0.1668 100.00 0.1991 . . 161 . . . . 'X-RAY DIFFRACTION' . 3.1744 3.6335 2593 0.1495 100.00 0.1935 . . 132 . . . . 'X-RAY DIFFRACTION' . 3.6335 4.5767 2630 0.1345 100.00 0.1657 . . 145 . . . . 'X-RAY DIFFRACTION' . 4.5767 39.3777 2728 0.1627 100.00 0.1984 . . 148 . . . . # _struct.entry_id 4MDI _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 4MDI _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'HLA-DR, Antigen presentation, T-cell receptor, Citrullination, Membrane, IMMUNE SYSTEM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 6 ? K N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLU A 47 ? ALA A 52 ? GLU A 47 ALA A 52 1 ? 6 HELX_P HELX_P2 2 ALA A 56 ? SER A 77 ? ALA A 56 SER A 77 1 ? 22 HELX_P HELX_P3 3 THR B 53 ? LEU B 55 ? THR B 51 LEU B 53 5 ? 3 HELX_P HELX_P4 4 GLY B 56 ? ASN B 64 ? GLY B 54 ASN B 62 1 ? 9 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 ? ? ? ? ? ? ? 2.020 ? disulf2 disulf ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.054 ? disulf3 disulf ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? C LEU 5 C ? ? ? 1_555 C CIR 6 N2 ? ? C LEU 5 C CIR 6 1_555 ? ? ? ? ? ? ? 1.317 ? covale2 covale ? ? C CIR 6 C1 ? ? ? 1_555 C SER 7 N ? ? C CIR 6 C SER 7 1_555 ? ? ? ? ? ? ? 1.339 ? covale3 covale ? ? A ASN 118 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 118 A NAG 501 1_555 ? ? ? ? ? ? ? 1.444 ? covale4 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.447 ? covale5 covale ? ? A ASN 78 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 78 A NAG 500 1_555 ? ? ? ? ? ? ? 1.452 ? covale6 covale ? ? B ASN 21 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 19 B NAG 201 1_555 ? ? ? ? ? ? ? 1.452 ? covale7 covale ? ? A CYS 107 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107 A CYS 163 1_555 ? ? ? ? ? ? ? 2.020 ? covale8 covale ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.033 ? covale9 covale ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.054 ? # 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 3.99 2 THR 113 A . ? THR 113 A PRO 114 A ? PRO 114 A 1 0.44 3 TYR 125 B . ? TYR 123 B PRO 126 B ? PRO 124 B 1 1.03 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLU A 40 ? TRP A 43 ? GLU A 40 TRP A 43 A 2 ASP A 29 ? ASP A 35 ? ASP A 29 ASP A 35 A 3 SER A 19 ? PHE A 26 ? SER A 19 PHE A 26 A 4 HIS A 5 ? ASN A 15 ? HIS A 5 ASN A 15 A 5 PHE B 9 ? PHE B 20 ? PHE B 7 PHE B 18 A 6 ARG B 25 ? TYR B 34 ? ARG B 23 TYR B 32 A 7 GLU B 37 ? ASP B 43 ? GLU B 35 ASP B 41 A 8 TYR B 49 ? ALA B 51 ? TYR B 47 ALA B 49 B 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 B 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 B 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 B 4 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 C 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 C 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 C 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 C 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 D 1 LYS A 126 ? VAL A 128 ? LYS A 126 VAL A 128 D 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 D 3 TYR A 161 ? GLU A 166 ? TYR A 161 GLU A 166 D 4 LEU A 174 ? TRP A 178 ? LEU A 174 TRP A 178 E 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 E 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 E 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 E 4 VAL B 144 ? SER B 146 ? VAL B 142 SER B 144 F 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 F 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 F 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 F 4 ILE B 150 ? GLN B 151 ? ILE B 148 GLN B 149 G 1 GLN B 138 ? GLU B 140 ? GLN B 136 GLU B 138 G 2 GLU B 130 ? ARG B 135 ? GLU B 128 ARG B 133 G 3 VAL B 172 ? GLU B 178 ? VAL B 170 GLU B 176 G 4 LEU B 186 ? ARG B 191 ? LEU B 184 ARG B 189 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O VAL A 42 ? O VAL A 42 N HIS A 33 ? N HIS A 33 A 2 3 O ASP A 29 ? O ASP A 29 N PHE A 26 ? N PHE A 26 A 3 4 O ASP A 25 ? O ASP A 25 N ILE A 8 ? N ILE A 8 A 4 5 N HIS A 5 ? N HIS A 5 O PHE B 19 ? O PHE B 17 A 5 6 N HIS B 18 ? N HIS B 16 O ARG B 27 ? O ARG B 25 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 ILE A 109 ? N ILE A 109 O LYS A 147 ? O LYS A 147 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 ILE A 109 ? N ILE A 109 O LYS A 147 ? O LYS A 147 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 VAL A 165 ? N VAL A 165 O LEU A 174 ? O LEU A 174 E 1 2 N TYR B 104 ? N TYR B 102 O VAL B 118 ? O VAL B 116 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 TYR B 104 ? N TYR B 102 O VAL B 118 ? O VAL B 116 F 2 3 N VAL B 121 ? N VAL B 119 O THR B 159 ? O THR B 157 F 3 4 O GLN B 158 ? O GLN B 156 N ILE B 150 ? N ILE B 148 G 1 2 O GLN B 138 ? O GLN B 136 N ARG B 135 ? N ARG B 133 G 2 3 N ARG B 132 ? N ARG B 130 O GLN B 176 ? O GLN B 174 G 3 4 N VAL B 177 ? N VAL B 175 O LEU B 186 ? O LEU B 184 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO B 202' AC2 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 500 BOUND TO ASN A 78' AC3 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 118 RESIDUES 501 TO 502' AC4 Software ? ? ? ? 3 '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 6 THR B 79 ? THR B 77 . ? 1_555 ? 2 AC1 6 HIS B 113 ? HIS B 111 . ? 1_655 ? 3 AC1 6 HOH J . ? HOH B 324 . ? 1_555 ? 4 AC1 6 ARG C 4 ? ARG C 4 . ? 1_555 ? 5 AC1 6 LEU C 5 ? LEU C 5 . ? 1_555 ? 6 AC1 6 CIR C 6 ? CIR C 6 . ? 1_555 ? 7 AC2 3 ASN A 78 ? ASN A 78 . ? 1_555 ? 8 AC2 3 LYS A 126 ? LYS A 126 . ? 8_555 ? 9 AC2 3 HOH I . ? HOH A 770 . ? 1_555 ? 10 AC3 6 ASN A 118 ? ASN A 118 . ? 1_555 ? 11 AC3 6 TRP A 168 ? TRP A 168 . ? 1_555 ? 12 AC3 6 HOH I . ? HOH A 780 . ? 1_555 ? 13 AC3 6 ASP B 4 ? ASP B 2 . ? 1_555 ? 14 AC3 6 HOH J . ? HOH B 462 . ? 1_555 ? 15 AC3 6 ARG C 13 ? ARG C 13 . ? 8_455 ? 16 AC4 3 ASN B 21 ? ASN B 19 . ? 1_555 ? 17 AC4 3 GLU B 24 ? GLU B 22 . ? 1_555 ? 18 AC4 3 HOH J . ? HOH B 398 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MDI _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 4MDI _atom_sites.fract_transf_matrix[1][1] 0.014921 _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] 0.005467 _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] 0.012924 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLU A 1 3 ? 35.677 11.740 -19.244 1.00 68.41 ? 3 GLU A N 1 ATOM 2 C CA . GLU A 1 3 ? 36.456 12.131 -18.073 1.00 69.99 ? 3 GLU A CA 1 ATOM 3 C C . GLU A 1 3 ? 35.838 11.630 -16.776 1.00 65.93 ? 3 GLU A C 1 ATOM 4 O O . GLU A 1 3 ? 34.701 11.969 -16.454 1.00 70.71 ? 3 GLU A O 1 ATOM 5 C CB . GLU A 1 3 ? 36.594 13.645 -18.012 1.00 69.17 ? 3 GLU A CB 1 ATOM 6 C CG . GLU A 1 3 ? 37.471 14.136 -16.885 1.00 61.15 ? 3 GLU A CG 1 ATOM 7 C CD . GLU A 1 3 ? 37.562 15.635 -16.886 1.00 63.50 ? 3 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 3 ? 36.502 16.287 -17.007 1.00 70.05 ? 3 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 3 ? 38.688 16.163 -16.790 1.00 59.09 ? 3 GLU A OE2 1 ATOM 10 N N . GLU A 1 4 ? 36.594 10.838 -16.023 1.00 59.74 ? 4 GLU A N 1 ATOM 11 C CA . GLU A 1 4 ? 36.049 10.200 -14.831 1.00 56.44 ? 4 GLU A CA 1 ATOM 12 C C . GLU A 1 4 ? 36.070 11.095 -13.601 1.00 42.46 ? 4 GLU A C 1 ATOM 13 O O . GLU A 1 4 ? 35.038 11.288 -12.965 1.00 35.80 ? 4 GLU A O 1 ATOM 14 C CB . GLU A 1 4 ? 36.740 8.866 -14.542 1.00 63.11 ? 4 GLU A CB 1 ATOM 15 C CG . GLU A 1 4 ? 36.432 7.791 -15.564 1.00 69.66 ? 4 GLU A CG 1 ATOM 16 C CD . GLU A 1 4 ? 36.696 6.399 -15.029 1.00 74.61 ? 4 GLU A CD 1 ATOM 17 O OE1 . GLU A 1 4 ? 37.139 6.287 -13.865 1.00 74.50 ? 4 GLU A OE1 1 ATOM 18 O OE2 . GLU A 1 4 ? 36.457 5.422 -15.771 1.00 76.28 ? 4 GLU A OE2 1 ATOM 19 N N . HIS A 1 5 ? 37.232 11.638 -13.253 1.00 28.31 ? 5 HIS A N 1 ATOM 20 C CA . HIS A 1 5 ? 37.306 12.469 -12.060 1.00 20.76 ? 5 HIS A CA 1 ATOM 21 C C . HIS A 1 5 ? 38.291 13.624 -12.178 1.00 19.31 ? 5 HIS A C 1 ATOM 22 O O . HIS A 1 5 ? 39.244 13.568 -12.953 1.00 20.02 ? 5 HIS A O 1 ATOM 23 C CB . HIS A 1 5 ? 37.649 11.617 -10.837 1.00 20.57 ? 5 HIS A CB 1 ATOM 24 C CG . HIS A 1 5 ? 36.655 10.532 -10.565 1.00 29.68 ? 5 HIS A CG 1 ATOM 25 N ND1 . HIS A 1 5 ? 35.433 10.773 -9.977 1.00 26.50 ? 5 HIS A ND1 1 ATOM 26 C CD2 . HIS A 1 5 ? 36.695 9.202 -10.816 1.00 34.49 ? 5 HIS A CD2 1 ATOM 27 C CE1 . HIS A 1 5 ? 34.766 9.635 -9.866 1.00 28.80 ? 5 HIS A CE1 1 ATOM 28 N NE2 . HIS A 1 5 ? 35.506 8.668 -10.375 1.00 28.20 ? 5 HIS A NE2 1 ATOM 29 N N . VAL A 1 6 ? 38.053 14.669 -11.389 1.00 18.26 ? 6 VAL A N 1 ATOM 30 C CA . VAL A 1 6 ? 38.941 15.823 -11.363 1.00 19.28 ? 6 VAL A CA 1 ATOM 31 C C . VAL A 1 6 ? 39.279 16.195 -9.924 1.00 21.76 ? 6 VAL A C 1 ATOM 32 O O . VAL A 1 6 ? 38.397 16.334 -9.071 1.00 21.93 ? 6 VAL A O 1 ATOM 33 C CB . VAL A 1 6 ? 38.309 17.042 -12.063 1.00 23.11 ? 6 VAL A CB 1 ATOM 34 C CG1 . VAL A 1 6 ? 39.285 18.211 -12.068 1.00 24.30 ? 6 VAL A CG1 1 ATOM 35 C CG2 . VAL A 1 6 ? 37.869 16.677 -13.493 1.00 22.27 ? 6 VAL A CG2 1 ATOM 36 N N . ILE A 1 7 ? 40.567 16.341 -9.651 1.00 14.70 ? 7 ILE A N 1 ATOM 37 C CA . ILE A 1 7 ? 41.003 16.820 -8.356 1.00 16.17 ? 7 ILE A CA 1 ATOM 38 C C . ILE A 1 7 ? 41.704 18.158 -8.563 1.00 16.27 ? 7 ILE A C 1 ATOM 39 O O . ILE A 1 7 ? 42.590 18.276 -9.410 1.00 15.99 ? 7 ILE A O 1 ATOM 40 C CB . ILE A 1 7 ? 41.944 15.820 -7.664 1.00 18.72 ? 7 ILE A CB 1 ATOM 41 C CG1 . ILE A 1 7 ? 41.227 14.477 -7.452 1.00 17.53 ? 7 ILE A CG1 1 ATOM 42 C CG2 . ILE A 1 7 ? 42.426 16.385 -6.341 1.00 16.57 ? 7 ILE A CG2 1 ATOM 43 C CD1 . ILE A 1 7 ? 42.160 13.355 -6.929 1.00 22.72 ? 7 ILE A CD1 1 ATOM 44 N N . ILE A 1 8 ? 41.285 19.161 -7.799 1.00 17.76 ? 8 ILE A N 1 ATOM 45 C CA . ILE A 1 8 ? 41.832 20.504 -7.934 1.00 17.17 ? 8 ILE A CA 1 ATOM 46 C C . ILE A 1 8 ? 42.310 21.034 -6.591 1.00 17.81 ? 8 ILE A C 1 ATOM 47 O O . ILE A 1 8 ? 41.580 21.008 -5.613 1.00 19.98 ? 8 ILE A O 1 ATOM 48 C CB . ILE A 1 8 ? 40.792 21.476 -8.486 1.00 14.22 ? 8 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 8 ? 40.284 20.991 -9.840 1.00 12.73 ? 8 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 8 ? 41.378 22.913 -8.588 1.00 11.65 ? 8 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 8 ? 39.227 21.907 -10.473 1.00 14.68 ? 8 ILE A CD1 1 ATOM 52 N N . GLN A 1 9 ? 43.558 21.486 -6.559 1.00 19.08 ? 9 GLN A N 1 ATOM 53 C CA . GLN A 1 9 ? 44.101 22.210 -5.422 1.00 13.42 ? 9 GLN A CA 1 ATOM 54 C C . GLN A 1 9 ? 43.905 23.677 -5.796 1.00 15.90 ? 9 GLN A C 1 ATOM 55 O O . GLN A 1 9 ? 44.603 24.198 -6.684 1.00 14.30 ? 9 GLN A O 1 ATOM 56 C CB . GLN A 1 9 ? 45.595 21.896 -5.268 1.00 15.86 ? 9 GLN A CB 1 ATOM 57 C CG . GLN A 1 9 ? 46.331 22.707 -4.211 1.00 15.97 ? 9 GLN A CG 1 ATOM 58 C CD . GLN A 1 9 ? 47.820 22.483 -4.282 1.00 21.65 ? 9 GLN A CD 1 ATOM 59 O OE1 . GLN A 1 9 ? 48.268 21.351 -4.457 1.00 19.23 ? 9 GLN A OE1 1 ATOM 60 N NE2 . GLN A 1 9 ? 48.604 23.561 -4.159 1.00 14.01 ? 9 GLN A NE2 1 ATOM 61 N N . ALA A 1 10 ? 42.931 24.319 -5.149 1.00 14.95 ? 10 ALA A N 1 ATOM 62 C CA . ALA A 1 10 ? 42.538 25.685 -5.490 1.00 15.47 ? 10 ALA A CA 1 ATOM 63 C C . ALA A 1 10 ? 42.973 26.656 -4.405 1.00 18.40 ? 10 ALA A C 1 ATOM 64 O O . ALA A 1 10 ? 42.761 26.393 -3.213 1.00 15.33 ? 10 ALA A O 1 ATOM 65 C CB . ALA A 1 10 ? 41.021 25.771 -5.694 1.00 15.63 ? 10 ALA A CB 1 ATOM 66 N N . GLU A 1 11 ? 43.580 27.766 -4.827 1.00 18.07 ? 11 GLU A N 1 ATOM 67 C CA . GLU A 1 11 ? 44.108 28.784 -3.918 1.00 18.22 ? 11 GLU A CA 1 ATOM 68 C C . GLU A 1 11 ? 43.616 30.158 -4.347 1.00 18.57 ? 11 GLU A C 1 ATOM 69 O O . GLU A 1 11 ? 43.377 30.395 -5.537 1.00 15.69 ? 11 GLU A O 1 ATOM 70 C CB . GLU A 1 11 ? 45.641 28.796 -3.976 1.00 11.08 ? 11 GLU A CB 1 ATOM 71 C CG . GLU A 1 11 ? 46.277 27.437 -3.727 1.00 16.55 ? 11 GLU A CG 1 ATOM 72 C CD . GLU A 1 11 ? 47.728 27.357 -4.164 1.00 18.75 ? 11 GLU A CD 1 ATOM 73 O OE1 . GLU A 1 11 ? 48.379 28.408 -4.410 1.00 20.26 ? 11 GLU A OE1 1 ATOM 74 O OE2 . GLU A 1 11 ? 48.226 26.223 -4.258 1.00 16.47 ? 11 GLU A OE2 1 ATOM 75 N N . PHE A 1 12 ? 43.440 31.060 -3.389 1.00 17.10 ? 12 PHE A N 1 ATOM 76 C CA . PHE A 1 12 ? 43.333 32.477 -3.745 1.00 14.91 ? 12 PHE A CA 1 ATOM 77 C C . PHE A 1 12 ? 43.982 33.397 -2.716 1.00 16.85 ? 12 PHE A C 1 ATOM 78 O O . PHE A 1 12 ? 44.250 32.998 -1.575 1.00 16.07 ? 12 PHE A O 1 ATOM 79 C CB . PHE A 1 12 ? 41.874 32.900 -4.033 1.00 12.64 ? 12 PHE A CB 1 ATOM 80 C CG . PHE A 1 12 ? 40.979 32.961 -2.805 1.00 16.64 ? 12 PHE A CG 1 ATOM 81 C CD1 . PHE A 1 12 ? 41.069 34.016 -1.899 1.00 15.64 ? 12 PHE A CD1 1 ATOM 82 C CD2 . PHE A 1 12 ? 40.003 31.999 -2.599 1.00 15.47 ? 12 PHE A CD2 1 ATOM 83 C CE1 . PHE A 1 12 ? 40.232 34.081 -0.789 1.00 13.57 ? 12 PHE A CE1 1 ATOM 84 C CE2 . PHE A 1 12 ? 39.140 32.073 -1.503 1.00 19.58 ? 12 PHE A CE2 1 ATOM 85 C CZ . PHE A 1 12 ? 39.270 33.107 -0.590 1.00 19.31 ? 12 PHE A CZ 1 ATOM 86 N N . TYR A 1 13 ? 44.235 34.636 -3.134 1.00 13.34 ? 13 TYR A N 1 ATOM 87 C CA . TYR A 1 13 ? 44.693 35.671 -2.220 1.00 16.45 ? 13 TYR A CA 1 ATOM 88 C C . TYR A 1 13 ? 44.021 36.959 -2.666 1.00 15.27 ? 13 TYR A C 1 ATOM 89 O O . TYR A 1 13 ? 44.012 37.282 -3.852 1.00 16.47 ? 13 TYR A O 1 ATOM 90 C CB . TYR A 1 13 ? 46.223 35.812 -2.215 1.00 17.93 ? 13 TYR A CB 1 ATOM 91 C CG . TYR A 1 13 ? 46.710 36.737 -1.116 1.00 16.96 ? 13 TYR A CG 1 ATOM 92 C CD1 . TYR A 1 13 ? 46.970 36.256 0.166 1.00 17.45 ? 13 TYR A CD1 1 ATOM 93 C CD2 . TYR A 1 13 ? 46.855 38.101 -1.341 1.00 17.69 ? 13 TYR A CD2 1 ATOM 94 C CE1 . TYR A 1 13 ? 47.393 37.107 1.182 1.00 23.56 ? 13 TYR A CE1 1 ATOM 95 C CE2 . TYR A 1 13 ? 47.277 38.950 -0.340 1.00 21.64 ? 13 TYR A CE2 1 ATOM 96 C CZ . TYR A 1 13 ? 47.544 38.449 0.920 1.00 24.63 ? 13 TYR A CZ 1 ATOM 97 O OH . TYR A 1 13 ? 47.961 39.305 1.910 1.00 33.40 ? 13 TYR A OH 1 ATOM 98 N N . LEU A 1 14 ? 43.436 37.674 -1.716 1.00 16.04 ? 14 LEU A N 1 ATOM 99 C CA . LEU A 1 14 ? 42.646 38.860 -2.028 1.00 15.75 ? 14 LEU A CA 1 ATOM 100 C C . LEU A 1 14 ? 43.213 40.099 -1.339 1.00 19.64 ? 14 LEU A C 1 ATOM 101 O O . LEU A 1 14 ? 43.447 40.083 -0.133 1.00 18.98 ? 14 LEU A O 1 ATOM 102 C CB . LEU A 1 14 ? 41.204 38.633 -1.563 1.00 14.59 ? 14 LEU A CB 1 ATOM 103 C CG . LEU A 1 14 ? 40.237 39.798 -1.767 1.00 20.19 ? 14 LEU A CG 1 ATOM 104 C CD1 . LEU A 1 14 ? 40.030 40.055 -3.238 1.00 14.26 ? 14 LEU A CD1 1 ATOM 105 C CD2 . LEU A 1 14 ? 38.905 39.489 -1.083 1.00 20.56 ? 14 LEU A CD2 1 ATOM 106 N N . ASN A 1 15 ? 43.427 41.167 -2.103 1.00 20.46 ? 15 ASN A N 1 ATOM 107 C CA . ASN A 1 15 ? 43.804 42.462 -1.540 1.00 21.16 ? 15 ASN A CA 1 ATOM 108 C C . ASN A 1 15 ? 42.624 43.414 -1.645 1.00 26.37 ? 15 ASN A C 1 ATOM 109 O O . ASN A 1 15 ? 41.857 43.310 -2.599 1.00 23.45 ? 15 ASN A O 1 ATOM 110 C CB . ASN A 1 15 ? 44.979 43.055 -2.308 1.00 23.50 ? 15 ASN A CB 1 ATOM 111 C CG . ASN A 1 15 ? 46.322 42.652 -1.728 1.00 29.65 ? 15 ASN A CG 1 ATOM 112 O OD1 . ASN A 1 15 ? 46.434 42.346 -0.540 1.00 24.29 ? 15 ASN A OD1 1 ATOM 113 N ND2 . ASN A 1 15 ? 47.350 42.655 -2.570 1.00 21.69 ? 15 ASN A ND2 1 ATOM 114 N N . PRO A 1 16 ? 42.494 44.374 -0.701 1.00 22.15 ? 16 PRO A N 1 ATOM 115 C CA . PRO A 1 16 ? 43.409 44.686 0.409 1.00 22.45 ? 16 PRO A CA 1 ATOM 116 C C . PRO A 1 16 ? 43.095 43.875 1.665 1.00 23.09 ? 16 PRO A C 1 ATOM 117 O O . PRO A 1 16 ? 43.718 44.068 2.705 1.00 26.43 ? 16 PRO A O 1 ATOM 118 C CB . PRO A 1 16 ? 43.123 46.166 0.673 1.00 24.30 ? 16 PRO A CB 1 ATOM 119 C CG . PRO A 1 16 ? 41.665 46.286 0.390 1.00 23.62 ? 16 PRO A CG 1 ATOM 120 C CD . PRO A 1 16 ? 41.405 45.360 -0.792 1.00 21.23 ? 16 PRO A CD 1 ATOM 121 N N . ASP A 1 17 ? 42.133 42.975 1.557 1.00 21.71 ? 17 ASP A N 1 ATOM 122 C CA . ASP A 1 17 ? 41.665 42.202 2.699 1.00 31.65 ? 17 ASP A CA 1 ATOM 123 C C . ASP A 1 17 ? 42.756 41.344 3.312 1.00 28.46 ? 17 ASP A C 1 ATOM 124 O O . ASP A 1 17 ? 42.694 41.023 4.495 1.00 27.04 ? 17 ASP A O 1 ATOM 125 C CB . ASP A 1 17 ? 40.488 41.323 2.275 1.00 27.21 ? 17 ASP A CB 1 ATOM 126 C CG . ASP A 1 17 ? 39.374 42.136 1.646 1.00 32.00 ? 17 ASP A CG 1 ATOM 127 O OD1 . ASP A 1 17 ? 38.391 42.431 2.356 1.00 30.27 ? 17 ASP A OD1 1 ATOM 128 O OD2 . ASP A 1 17 ? 39.512 42.523 0.459 1.00 26.66 ? 17 ASP A OD2 1 ATOM 129 N N . GLN A 1 18 ? 43.753 40.998 2.500 1.00 25.65 ? 18 GLN A N 1 ATOM 130 C CA . GLN A 1 18 ? 44.812 40.068 2.891 1.00 24.85 ? 18 GLN A CA 1 ATOM 131 C C . GLN A 1 18 ? 44.238 38.719 3.329 1.00 27.58 ? 18 GLN A C 1 ATOM 132 O O . GLN A 1 18 ? 44.667 38.127 4.318 1.00 24.76 ? 18 GLN A O 1 ATOM 133 C CB . GLN A 1 18 ? 45.739 40.674 3.954 1.00 28.88 ? 18 GLN A CB 1 ATOM 134 C CG . GLN A 1 18 ? 46.480 41.892 3.436 1.00 32.07 ? 18 GLN A CG 1 ATOM 135 C CD . GLN A 1 18 ? 47.576 42.363 4.372 1.00 40.15 ? 18 GLN A CD 1 ATOM 136 O OE1 . GLN A 1 18 ? 47.321 42.694 5.521 1.00 38.52 ? 18 GLN A OE1 1 ATOM 137 N NE2 . GLN A 1 18 ? 48.808 42.396 3.874 1.00 45.90 ? 18 GLN A NE2 1 ATOM 138 N N . SER A 1 19 ? 43.256 38.231 2.585 1.00 22.73 ? 19 SER A N 1 ATOM 139 C CA A SER A 1 19 ? 42.701 36.910 2.840 0.52 27.60 ? 19 SER A CA 1 ATOM 140 C CA B SER A 1 19 ? 42.736 36.904 2.861 0.48 27.06 ? 19 SER A CA 1 ATOM 141 C C . SER A 1 19 ? 43.248 35.910 1.828 1.00 21.08 ? 19 SER A C 1 ATOM 142 O O . SER A 1 19 ? 43.245 36.174 0.630 1.00 23.99 ? 19 SER A O 1 ATOM 143 C CB A SER A 1 19 ? 41.170 36.948 2.771 0.52 28.69 ? 19 SER A CB 1 ATOM 144 C CB B SER A 1 19 ? 41.204 36.893 2.942 0.48 28.64 ? 19 SER A CB 1 ATOM 145 O OG A SER A 1 19 ? 40.647 37.936 3.644 0.52 25.83 ? 19 SER A OG 1 ATOM 146 O OG B SER A 1 19 ? 40.612 37.455 1.788 0.48 27.23 ? 19 SER A OG 1 ATOM 147 N N . GLY A 1 20 ? 43.724 34.770 2.310 1.00 23.22 ? 20 GLY A N 1 ATOM 148 C CA . GLY A 1 20 ? 44.148 33.707 1.423 1.00 26.35 ? 20 GLY A CA 1 ATOM 149 C C . GLY A 1 20 ? 43.466 32.412 1.820 1.00 30.87 ? 20 GLY A C 1 ATOM 150 O O . GLY A 1 20 ? 43.177 32.195 2.996 1.00 36.10 ? 20 GLY A O 1 ATOM 151 N N A GLU A 1 21 ? 43.199 31.544 0.854 0.49 21.04 ? 21 GLU A N 1 ATOM 152 N N C GLU A 1 21 ? 43.228 31.551 0.837 0.51 20.90 ? 21 GLU A N 1 ATOM 153 C CA A GLU A 1 21 ? 42.602 30.247 1.167 0.49 18.62 ? 21 GLU A CA 1 ATOM 154 C CA C GLU A 1 21 ? 42.603 30.256 1.079 0.51 18.45 ? 21 GLU A CA 1 ATOM 155 C C A GLU A 1 21 ? 43.177 29.140 0.286 0.49 16.35 ? 21 GLU A C 1 ATOM 156 C C C GLU A 1 21 ? 43.362 29.164 0.345 0.51 16.12 ? 21 GLU A C 1 ATOM 157 O O A GLU A 1 21 ? 43.540 29.373 -0.865 0.49 16.97 ? 21 GLU A O 1 ATOM 158 O O C GLU A 1 21 ? 44.022 29.423 -0.661 0.51 17.42 ? 21 GLU A O 1 ATOM 159 C CB A GLU A 1 21 ? 41.066 30.292 1.079 0.49 20.55 ? 21 GLU A CB 1 ATOM 160 C CB C GLU A 1 21 ? 41.148 30.257 0.601 0.51 17.25 ? 21 GLU A CB 1 ATOM 161 C CG A GLU A 1 21 ? 40.388 30.992 2.273 0.49 23.91 ? 21 GLU A CG 1 ATOM 162 C CG C GLU A 1 21 ? 40.369 29.007 0.992 0.51 19.51 ? 21 GLU A CG 1 ATOM 163 C CD A GLU A 1 21 ? 38.878 30.746 2.355 0.49 22.95 ? 21 GLU A CD 1 ATOM 164 C CD C GLU A 1 21 ? 38.995 28.952 0.368 0.51 16.78 ? 21 GLU A CD 1 ATOM 165 O OE1 A GLU A 1 21 ? 38.320 30.066 1.464 0.49 19.95 ? 21 GLU A OE1 1 ATOM 166 O OE1 C GLU A 1 21 ? 38.101 29.694 0.822 0.51 19.00 ? 21 GLU A OE1 1 ATOM 167 O OE2 A GLU A 1 21 ? 38.249 31.235 3.318 0.49 16.40 ? 21 GLU A OE2 1 ATOM 168 O OE2 C GLU A 1 21 ? 38.817 28.165 -0.576 0.51 15.25 ? 21 GLU A OE2 1 ATOM 169 N N . PHE A 1 22 ? 43.258 27.939 0.846 1.00 14.90 ? 22 PHE A N 1 ATOM 170 C CA . PHE A 1 22 ? 43.901 26.804 0.196 1.00 15.48 ? 22 PHE A CA 1 ATOM 171 C C . PHE A 1 22 ? 42.995 25.621 0.460 1.00 14.89 ? 22 PHE A C 1 ATOM 172 O O . PHE A 1 22 ? 42.713 25.308 1.615 1.00 19.57 ? 22 PHE A O 1 ATOM 173 C CB . PHE A 1 22 ? 45.265 26.575 0.847 1.00 16.61 ? 22 PHE A CB 1 ATOM 174 C CG . PHE A 1 22 ? 46.051 25.447 0.254 1.00 19.08 ? 22 PHE A CG 1 ATOM 175 C CD1 . PHE A 1 22 ? 47.130 25.703 -0.566 1.00 17.70 ? 22 PHE A CD1 1 ATOM 176 C CD2 . PHE A 1 22 ? 45.732 24.123 0.542 1.00 27.73 ? 22 PHE A CD2 1 ATOM 177 C CE1 . PHE A 1 22 ? 47.885 24.653 -1.096 1.00 22.87 ? 22 PHE A CE1 1 ATOM 178 C CE2 . PHE A 1 22 ? 46.473 23.073 0.005 1.00 26.79 ? 22 PHE A CE2 1 ATOM 179 C CZ . PHE A 1 22 ? 47.550 23.344 -0.815 1.00 20.18 ? 22 PHE A CZ 1 ATOM 180 N N . MET A 1 23 ? 42.522 24.982 -0.600 1.00 16.15 ? 23 MET A N 1 ATOM 181 C CA . MET A 1 23 ? 41.671 23.797 -0.462 1.00 22.25 ? 23 MET A CA 1 ATOM 182 C C . MET A 1 23 ? 41.867 22.809 -1.609 1.00 18.39 ? 23 MET A C 1 ATOM 183 O O . MET A 1 23 ? 42.383 23.172 -2.672 1.00 17.85 ? 23 MET A O 1 ATOM 184 C CB . MET A 1 23 ? 40.197 24.200 -0.398 1.00 15.46 ? 23 MET A CB 1 ATOM 185 C CG . MET A 1 23 ? 39.689 24.875 -1.677 1.00 22.34 ? 23 MET A CG 1 ATOM 186 S SD . MET A 1 23 ? 39.040 23.759 -2.956 1.00 19.62 ? 23 MET A SD 1 ATOM 187 C CE . MET A 1 23 ? 37.514 23.163 -2.212 1.00 17.09 ? 23 MET A CE 1 ATOM 188 N N . PHE A 1 24 ? 41.448 21.564 -1.380 1.00 16.79 ? 24 PHE A N 1 ATOM 189 C CA . PHE A 1 24 ? 41.418 20.546 -2.429 1.00 19.28 ? 24 PHE A CA 1 ATOM 190 C C . PHE A 1 24 ? 39.952 20.215 -2.712 1.00 23.19 ? 24 PHE A C 1 ATOM 191 O O . PHE A 1 24 ? 39.153 20.056 -1.778 1.00 16.43 ? 24 PHE A O 1 ATOM 192 C CB . PHE A 1 24 ? 42.136 19.272 -1.972 1.00 15.59 ? 24 PHE A CB 1 ATOM 193 C CG . PHE A 1 24 ? 43.571 19.164 -2.427 1.00 19.22 ? 24 PHE A CG 1 ATOM 194 C CD1 . PHE A 1 24 ? 43.925 18.290 -3.447 1.00 20.94 ? 24 PHE A CD1 1 ATOM 195 C CD2 . PHE A 1 24 ? 44.578 19.904 -1.808 1.00 20.04 ? 24 PHE A CD2 1 ATOM 196 C CE1 . PHE A 1 24 ? 45.256 18.158 -3.849 1.00 19.52 ? 24 PHE A CE1 1 ATOM 197 C CE2 . PHE A 1 24 ? 45.901 19.781 -2.201 1.00 17.89 ? 24 PHE A CE2 1 ATOM 198 C CZ . PHE A 1 24 ? 46.245 18.907 -3.223 1.00 19.21 ? 24 PHE A CZ 1 ATOM 199 N N . ASP A 1 25 ? 39.610 20.129 -3.997 1.00 18.25 ? 25 ASP A N 1 ATOM 200 C CA . ASP A 1 25 ? 38.253 19.820 -4.468 1.00 16.42 ? 25 ASP A CA 1 ATOM 201 C C . ASP A 1 25 ? 38.297 18.494 -5.246 1.00 21.90 ? 25 ASP A C 1 ATOM 202 O O . ASP A 1 25 ? 39.227 18.260 -6.028 1.00 16.91 ? 25 ASP A O 1 ATOM 203 C CB . ASP A 1 25 ? 37.775 20.955 -5.384 1.00 16.05 ? 25 ASP A CB 1 ATOM 204 C CG . ASP A 1 25 ? 36.389 20.705 -5.986 1.00 24.34 ? 25 ASP A CG 1 ATOM 205 O OD1 . ASP A 1 25 ? 35.442 21.419 -5.597 1.00 25.17 ? 25 ASP A OD1 1 ATOM 206 O OD2 . ASP A 1 25 ? 36.245 19.810 -6.854 1.00 24.28 ? 25 ASP A OD2 1 ATOM 207 N N . PHE A 1 26 ? 37.314 17.630 -5.011 1.00 19.16 ? 26 PHE A N 1 ATOM 208 C CA . PHE A 1 26 ? 37.136 16.394 -5.771 1.00 20.04 ? 26 PHE A CA 1 ATOM 209 C C . PHE A 1 26 ? 35.730 16.424 -6.374 1.00 17.75 ? 26 PHE A C 1 ATOM 210 O O . PHE A 1 26 ? 34.748 16.377 -5.641 1.00 21.30 ? 26 PHE A O 1 ATOM 211 C CB . PHE A 1 26 ? 37.282 15.165 -4.859 1.00 17.62 ? 26 PHE A CB 1 ATOM 212 C CG . PHE A 1 26 ? 37.002 13.842 -5.551 1.00 17.74 ? 26 PHE A CG 1 ATOM 213 C CD1 . PHE A 1 26 ? 38.000 13.181 -6.248 1.00 22.34 ? 26 PHE A CD1 1 ATOM 214 C CD2 . PHE A 1 26 ? 35.736 13.275 -5.513 1.00 24.25 ? 26 PHE A CD2 1 ATOM 215 C CE1 . PHE A 1 26 ? 37.738 11.968 -6.898 1.00 24.19 ? 26 PHE A CE1 1 ATOM 216 C CE2 . PHE A 1 26 ? 35.470 12.075 -6.148 1.00 25.62 ? 26 PHE A CE2 1 ATOM 217 C CZ . PHE A 1 26 ? 36.471 11.418 -6.840 1.00 25.47 ? 26 PHE A CZ 1 ATOM 218 N N . ASP A 1 27 ? 35.647 16.498 -7.700 1.00 17.47 ? 27 ASP A N 1 ATOM 219 C CA . ASP A 1 27 ? 34.378 16.488 -8.433 1.00 16.27 ? 27 ASP A CA 1 ATOM 220 C C . ASP A 1 27 ? 33.366 17.487 -7.887 1.00 21.91 ? 27 ASP A C 1 ATOM 221 O O . ASP A 1 27 ? 32.171 17.222 -7.898 1.00 20.39 ? 27 ASP A O 1 ATOM 222 C CB . ASP A 1 27 ? 33.769 15.065 -8.491 1.00 18.04 ? 27 ASP A CB 1 ATOM 223 C CG . ASP A 1 27 ? 34.589 14.104 -9.357 1.00 18.91 ? 27 ASP A CG 1 ATOM 224 O OD1 . ASP A 1 27 ? 35.536 14.564 -10.035 1.00 21.56 ? 27 ASP A OD1 1 ATOM 225 O OD2 . ASP A 1 27 ? 34.273 12.887 -9.382 1.00 22.68 ? 27 ASP A OD2 1 ATOM 226 N N . GLY A 1 28 ? 33.842 18.633 -7.398 1.00 18.67 ? 28 GLY A N 1 ATOM 227 C CA . GLY A 1 28 ? 32.953 19.665 -6.891 1.00 19.75 ? 28 GLY A CA 1 ATOM 228 C C . GLY A 1 28 ? 32.681 19.624 -5.389 1.00 24.29 ? 28 GLY A C 1 ATOM 229 O O . GLY A 1 28 ? 31.925 20.448 -4.870 1.00 22.38 ? 28 GLY A O 1 ATOM 230 N N . ASP A 1 29 ? 33.277 18.668 -4.685 1.00 17.07 ? 29 ASP A N 1 ATOM 231 C CA . ASP A 1 29 ? 33.167 18.639 -3.226 1.00 17.13 ? 29 ASP A CA 1 ATOM 232 C C . ASP A 1 29 ? 34.528 18.881 -2.586 1.00 22.54 ? 29 ASP A C 1 ATOM 233 O O . ASP A 1 29 ? 35.551 18.507 -3.146 1.00 19.33 ? 29 ASP A O 1 ATOM 234 C CB . ASP A 1 29 ? 32.592 17.312 -2.739 1.00 16.89 ? 29 ASP A CB 1 ATOM 235 C CG . ASP A 1 29 ? 31.085 17.244 -2.889 1.00 22.78 ? 29 ASP A CG 1 ATOM 236 O OD1 . ASP A 1 29 ? 30.362 18.029 -2.227 1.00 29.63 ? 29 ASP A OD1 1 ATOM 237 O OD2 . ASP A 1 29 ? 30.626 16.406 -3.677 1.00 22.97 ? 29 ASP A OD2 1 ATOM 238 N N . GLU A 1 30 ? 34.536 19.513 -1.416 1.00 20.40 ? 30 GLU A N 1 ATOM 239 C CA . GLU A 1 30 ? 35.784 19.835 -0.723 1.00 18.15 ? 30 GLU A CA 1 ATOM 240 C C . GLU A 1 30 ? 36.350 18.627 0.018 1.00 18.63 ? 30 GLU A C 1 ATOM 241 O O . GLU A 1 30 ? 35.657 18.010 0.824 1.00 18.86 ? 30 GLU A O 1 ATOM 242 C CB . GLU A 1 30 ? 35.565 20.998 0.258 1.00 16.61 ? 30 GLU A CB 1 ATOM 243 C CG . GLU A 1 30 ? 36.739 21.203 1.211 1.00 20.20 ? 30 GLU A CG 1 ATOM 244 C CD . GLU A 1 30 ? 36.438 22.153 2.359 1.00 23.75 ? 30 GLU A CD 1 ATOM 245 O OE1 . GLU A 1 30 ? 35.280 22.629 2.483 1.00 22.73 ? 30 GLU A OE1 1 ATOM 246 O OE2 . GLU A 1 30 ? 37.375 22.402 3.157 1.00 23.72 ? 30 GLU A OE2 1 ATOM 247 N N . ILE A 1 31 ? 37.603 18.270 -0.261 1.00 16.43 ? 31 ILE A N 1 ATOM 248 C CA . ILE A 1 31 ? 38.250 17.211 0.507 1.00 16.14 ? 31 ILE A CA 1 ATOM 249 C C . ILE A 1 31 ? 38.705 17.769 1.849 1.00 18.35 ? 31 ILE A C 1 ATOM 250 O O . ILE A 1 31 ? 38.437 17.186 2.913 1.00 19.50 ? 31 ILE A O 1 ATOM 251 C CB . ILE A 1 31 ? 39.468 16.605 -0.235 1.00 20.49 ? 31 ILE A CB 1 ATOM 252 C CG1 . ILE A 1 31 ? 39.085 16.150 -1.650 1.00 17.52 ? 31 ILE A CG1 1 ATOM 253 C CG2 . ILE A 1 31 ? 40.051 15.448 0.568 1.00 22.18 ? 31 ILE A CG2 1 ATOM 254 C CD1 . ILE A 1 31 ? 40.264 15.584 -2.451 1.00 20.15 ? 31 ILE A CD1 1 ATOM 255 N N . PHE A 1 32 ? 39.393 18.907 1.792 1.00 17.90 ? 32 PHE A N 1 ATOM 256 C CA . PHE A 1 32 ? 39.859 19.592 2.996 1.00 16.56 ? 32 PHE A CA 1 ATOM 257 C C . PHE A 1 32 ? 40.266 21.011 2.645 1.00 19.14 ? 32 PHE A C 1 ATOM 258 O O . PHE A 1 32 ? 40.417 21.342 1.473 1.00 19.53 ? 32 PHE A O 1 ATOM 259 C CB . PHE A 1 32 ? 41.044 18.851 3.644 1.00 18.02 ? 32 PHE A CB 1 ATOM 260 C CG . PHE A 1 32 ? 42.338 18.948 2.864 1.00 17.14 ? 32 PHE A CG 1 ATOM 261 C CD1 . PHE A 1 32 ? 43.215 20.000 3.070 1.00 21.42 ? 32 PHE A CD1 1 ATOM 262 C CD2 . PHE A 1 32 ? 42.674 17.982 1.928 1.00 22.76 ? 32 PHE A CD2 1 ATOM 263 C CE1 . PHE A 1 32 ? 44.412 20.089 2.352 1.00 29.57 ? 32 PHE A CE1 1 ATOM 264 C CE2 . PHE A 1 32 ? 43.859 18.069 1.200 1.00 23.74 ? 32 PHE A CE2 1 ATOM 265 C CZ . PHE A 1 32 ? 44.729 19.116 1.416 1.00 29.25 ? 32 PHE A CZ 1 ATOM 266 N N . HIS A 1 33 ? 40.435 21.851 3.662 1.00 19.87 ? 33 HIS A N 1 ATOM 267 C CA . HIS A 1 33 ? 41.104 23.132 3.468 1.00 18.63 ? 33 HIS A CA 1 ATOM 268 C C . HIS A 1 33 ? 42.120 23.353 4.584 1.00 20.26 ? 33 HIS A C 1 ATOM 269 O O . HIS A 1 33 ? 42.147 22.620 5.574 1.00 19.71 ? 33 HIS A O 1 ATOM 270 C CB . HIS A 1 33 ? 40.103 24.291 3.428 1.00 16.76 ? 33 HIS A CB 1 ATOM 271 C CG . HIS A 1 33 ? 39.447 24.578 4.746 1.00 17.97 ? 33 HIS A CG 1 ATOM 272 N ND1 . HIS A 1 33 ? 38.241 24.023 5.112 1.00 20.52 ? 33 HIS A ND1 1 ATOM 273 C CD2 . HIS A 1 33 ? 39.813 25.389 5.769 1.00 21.25 ? 33 HIS A CD2 1 ATOM 274 C CE1 . HIS A 1 33 ? 37.897 24.464 6.309 1.00 22.82 ? 33 HIS A CE1 1 ATOM 275 N NE2 . HIS A 1 33 ? 38.831 25.299 6.727 1.00 22.82 ? 33 HIS A NE2 1 ATOM 276 N N . VAL A 1 34 ? 42.960 24.364 4.425 1.00 19.62 ? 34 VAL A N 1 ATOM 277 C CA . VAL A 1 34 ? 43.884 24.717 5.485 1.00 21.76 ? 34 VAL A CA 1 ATOM 278 C C . VAL A 1 34 ? 43.418 25.971 6.215 1.00 23.74 ? 34 VAL A C 1 ATOM 279 O O . VAL A 1 34 ? 43.172 27.007 5.594 1.00 28.31 ? 34 VAL A O 1 ATOM 280 C CB . VAL A 1 34 ? 45.301 24.935 4.945 1.00 21.51 ? 34 VAL A CB 1 ATOM 281 C CG1 . VAL A 1 34 ? 46.182 25.537 6.032 1.00 25.23 ? 34 VAL A CG1 1 ATOM 282 C CG2 . VAL A 1 34 ? 45.866 23.622 4.445 1.00 24.50 ? 34 VAL A CG2 1 ATOM 283 N N . ASP A 1 35 ? 43.272 25.857 7.533 1.00 21.21 ? 35 ASP A N 1 ATOM 284 C CA . ASP A 1 35 ? 43.006 27.004 8.390 1.00 29.76 ? 35 ASP A CA 1 ATOM 285 C C . ASP A 1 35 ? 44.316 27.778 8.473 1.00 31.71 ? 35 ASP A C 1 ATOM 286 O O . ASP A 1 35 ? 45.252 27.338 9.133 1.00 30.19 ? 35 ASP A O 1 ATOM 287 C CB . ASP A 1 35 ? 42.562 26.510 9.776 1.00 32.79 ? 35 ASP A CB 1 ATOM 288 C CG . ASP A 1 35 ? 42.163 27.641 10.721 1.00 39.32 ? 35 ASP A CG 1 ATOM 289 O OD1 . ASP A 1 35 ? 42.713 28.759 10.620 1.00 32.48 ? 35 ASP A OD1 1 ATOM 290 O OD2 . ASP A 1 35 ? 41.291 27.402 11.584 1.00 43.69 ? 35 ASP A OD2 1 ATOM 291 N N . MET A 1 36 ? 44.390 28.923 7.798 1.00 32.06 ? 36 MET A N 1 ATOM 292 C CA . MET A 1 36 ? 45.676 29.604 7.660 1.00 29.32 ? 36 MET A CA 1 ATOM 293 C C . MET A 1 36 ? 46.144 30.173 8.993 1.00 40.90 ? 36 MET A C 1 ATOM 294 O O . MET A 1 36 ? 47.327 30.106 9.308 1.00 39.46 ? 36 MET A O 1 ATOM 295 C CB . MET A 1 36 ? 45.639 30.695 6.582 1.00 30.71 ? 36 MET A CB 1 ATOM 296 C CG . MET A 1 36 ? 45.167 30.240 5.188 1.00 34.70 ? 36 MET A CG 1 ATOM 297 S SD . MET A 1 36 ? 46.130 28.948 4.350 1.00 41.82 ? 36 MET A SD 1 ATOM 298 C CE . MET A 1 36 ? 47.711 29.741 4.196 1.00 42.32 ? 36 MET A CE 1 ATOM 299 N N . ALA A 1 37 ? 45.213 30.713 9.779 1.00 42.03 ? 37 ALA A N 1 ATOM 300 C CA . ALA A 1 37 ? 45.543 31.267 11.090 1.00 39.28 ? 37 ALA A CA 1 ATOM 301 C C . ALA A 1 37 ? 46.051 30.206 12.066 1.00 41.57 ? 37 ALA A C 1 ATOM 302 O O . ALA A 1 37 ? 47.030 30.426 12.782 1.00 45.73 ? 37 ALA A O 1 ATOM 303 C CB . ALA A 1 37 ? 44.347 32.010 11.679 1.00 37.64 ? 37 ALA A CB 1 ATOM 304 N N . LYS A 1 38 ? 45.392 29.053 12.091 1.00 41.33 ? 38 LYS A N 1 ATOM 305 C CA . LYS A 1 38 ? 45.783 27.990 13.014 1.00 42.63 ? 38 LYS A CA 1 ATOM 306 C C . LYS A 1 38 ? 46.862 27.087 12.424 1.00 43.76 ? 38 LYS A C 1 ATOM 307 O O . LYS A 1 38 ? 47.463 26.284 13.145 1.00 35.22 ? 38 LYS A O 1 ATOM 308 C CB . LYS A 1 38 ? 44.568 27.153 13.422 1.00 40.13 ? 38 LYS A CB 1 ATOM 309 C CG . LYS A 1 38 ? 43.566 27.891 14.295 1.00 48.01 ? 38 LYS A CG 1 ATOM 310 C CD . LYS A 1 38 ? 42.410 26.985 14.714 1.00 54.45 ? 38 LYS A CD 1 ATOM 311 C CE . LYS A 1 38 ? 41.441 27.729 15.626 1.00 60.68 ? 38 LYS A CE 1 ATOM 312 N NZ . LYS A 1 38 ? 40.349 26.859 16.137 1.00 65.48 ? 38 LYS A NZ 1 ATOM 313 N N . LYS A 1 39 ? 47.103 27.228 11.119 1.00 35.14 ? 39 LYS A N 1 ATOM 314 C CA . LYS A 1 39 ? 48.029 26.351 10.394 1.00 36.66 ? 39 LYS A CA 1 ATOM 315 C C . LYS A 1 39 ? 47.659 24.893 10.616 1.00 36.64 ? 39 LYS A C 1 ATOM 316 O O . LYS A 1 39 ? 48.498 24.092 11.013 1.00 36.04 ? 39 LYS A O 1 ATOM 317 C CB . LYS A 1 39 ? 49.481 26.562 10.840 1.00 38.54 ? 39 LYS A CB 1 ATOM 318 C CG . LYS A 1 39 ? 49.947 28.002 10.892 1.00 44.17 ? 39 LYS A CG 1 ATOM 319 C CD . LYS A 1 39 ? 51.350 28.081 11.482 1.00 60.90 ? 39 LYS A CD 1 ATOM 320 C CE . LYS A 1 39 ? 51.850 29.514 11.554 1.00 70.69 ? 39 LYS A CE 1 ATOM 321 N NZ . LYS A 1 39 ? 50.946 30.367 12.373 1.00 76.40 ? 39 LYS A NZ 1 ATOM 322 N N . GLU A 1 40 ? 46.395 24.554 10.391 1.00 36.35 ? 40 GLU A N 1 ATOM 323 C CA A GLU A 1 40 ? 45.925 23.184 10.575 0.53 34.74 ? 40 GLU A CA 1 ATOM 324 C CA B GLU A 1 40 ? 45.952 23.176 10.556 0.47 35.01 ? 40 GLU A CA 1 ATOM 325 C C . GLU A 1 40 ? 45.086 22.728 9.387 1.00 29.35 ? 40 GLU A C 1 ATOM 326 O O . GLU A 1 40 ? 44.342 23.518 8.806 1.00 28.55 ? 40 GLU A O 1 ATOM 327 C CB A GLU A 1 40 ? 45.115 23.061 11.870 0.53 34.54 ? 40 GLU A CB 1 ATOM 328 C CB B GLU A 1 40 ? 45.213 22.985 11.886 0.47 35.34 ? 40 GLU A CB 1 ATOM 329 C CG A GLU A 1 40 ? 45.949 23.121 13.144 0.53 38.78 ? 40 GLU A CG 1 ATOM 330 C CG B GLU A 1 40 ? 43.825 23.598 11.937 0.47 35.86 ? 40 GLU A CG 1 ATOM 331 C CD A GLU A 1 40 ? 45.093 23.147 14.393 0.53 43.18 ? 40 GLU A CD 1 ATOM 332 C CD B GLU A 1 40 ? 43.060 23.205 13.187 0.47 39.28 ? 40 GLU A CD 1 ATOM 333 O OE1 A GLU A 1 40 ? 43.851 23.156 14.259 0.53 45.52 ? 40 GLU A OE1 1 ATOM 334 O OE1 B GLU A 1 40 ? 41.886 22.796 13.068 0.47 29.30 ? 40 GLU A OE1 1 ATOM 335 O OE2 A GLU A 1 40 ? 45.657 23.165 15.506 0.53 49.41 ? 40 GLU A OE2 1 ATOM 336 O OE2 B GLU A 1 40 ? 43.632 23.307 14.292 0.47 44.68 ? 40 GLU A OE2 1 ATOM 337 N N . THR A 1 41 ? 45.212 21.452 9.037 1.00 26.86 ? 41 THR A N 1 ATOM 338 C CA . THR A 1 41 ? 44.434 20.853 7.967 1.00 24.70 ? 41 THR A CA 1 ATOM 339 C C . THR A 1 41 ? 43.047 20.512 8.502 1.00 30.35 ? 41 THR A C 1 ATOM 340 O O . THR A 1 41 ? 42.916 19.831 9.521 1.00 34.16 ? 41 THR A O 1 ATOM 341 C CB . THR A 1 41 ? 45.105 19.565 7.450 1.00 30.19 ? 41 THR A CB 1 ATOM 342 O OG1 . THR A 1 41 ? 46.417 19.873 6.952 1.00 31.98 ? 41 THR A OG1 1 ATOM 343 C CG2 . THR A 1 41 ? 44.267 18.924 6.341 1.00 27.61 ? 41 THR A CG2 1 ATOM 344 N N . VAL A 1 42 ? 42.017 20.991 7.815 1.00 26.95 ? 42 VAL A N 1 ATOM 345 C CA . VAL A 1 42 ? 40.637 20.765 8.229 1.00 24.95 ? 42 VAL A CA 1 ATOM 346 C C . VAL A 1 42 ? 39.913 19.876 7.217 1.00 23.31 ? 42 VAL A C 1 ATOM 347 O O . VAL A 1 42 ? 39.554 20.339 6.140 1.00 19.29 ? 42 VAL A O 1 ATOM 348 C CB . VAL A 1 42 ? 39.872 22.100 8.345 1.00 25.37 ? 42 VAL A CB 1 ATOM 349 C CG1 . VAL A 1 42 ? 38.435 21.851 8.777 1.00 29.68 ? 42 VAL A CG1 1 ATOM 350 C CG2 . VAL A 1 42 ? 40.580 23.043 9.329 1.00 21.15 ? 42 VAL A CG2 1 ATOM 351 N N . TRP A 1 43 ? 39.696 18.606 7.561 1.00 21.53 ? 43 TRP A N 1 ATOM 352 C CA . TRP A 1 43 ? 39.042 17.667 6.646 1.00 23.38 ? 43 TRP A CA 1 ATOM 353 C C . TRP A 1 43 ? 37.528 17.914 6.598 1.00 25.07 ? 43 TRP A C 1 ATOM 354 O O . TRP A 1 43 ? 36.909 18.180 7.621 1.00 24.44 ? 43 TRP A O 1 ATOM 355 C CB . TRP A 1 43 ? 39.350 16.215 7.036 1.00 20.25 ? 43 TRP A CB 1 ATOM 356 C CG . TRP A 1 43 ? 40.826 15.904 6.967 1.00 26.69 ? 43 TRP A CG 1 ATOM 357 C CD1 . TRP A 1 43 ? 41.722 15.963 7.990 1.00 29.36 ? 43 TRP A CD1 1 ATOM 358 C CD2 . TRP A 1 43 ? 41.569 15.516 5.803 1.00 23.24 ? 43 TRP A CD2 1 ATOM 359 N NE1 . TRP A 1 43 ? 42.979 15.633 7.539 1.00 28.94 ? 43 TRP A NE1 1 ATOM 360 C CE2 . TRP A 1 43 ? 42.911 15.358 6.197 1.00 29.22 ? 43 TRP A CE2 1 ATOM 361 C CE3 . TRP A 1 43 ? 41.232 15.302 4.461 1.00 23.66 ? 43 TRP A CE3 1 ATOM 362 C CZ2 . TRP A 1 43 ? 43.914 14.984 5.302 1.00 33.13 ? 43 TRP A CZ2 1 ATOM 363 C CZ3 . TRP A 1 43 ? 42.227 14.917 3.574 1.00 22.98 ? 43 TRP A CZ3 1 ATOM 364 C CH2 . TRP A 1 43 ? 43.552 14.772 3.996 1.00 23.23 ? 43 TRP A CH2 1 ATOM 365 N N . ARG A 1 44 ? 36.937 17.844 5.410 1.00 21.40 ? 44 ARG A N 1 ATOM 366 C CA . ARG A 1 44 ? 35.513 18.171 5.261 1.00 21.27 ? 44 ARG A CA 1 ATOM 367 C C . ARG A 1 44 ? 34.632 17.177 5.999 1.00 24.91 ? 44 ARG A C 1 ATOM 368 O O . ARG A 1 44 ? 33.662 17.562 6.654 1.00 31.79 ? 44 ARG A O 1 ATOM 369 C CB . ARG A 1 44 ? 35.118 18.228 3.789 1.00 19.57 ? 44 ARG A CB 1 ATOM 370 C CG . ARG A 1 44 ? 33.677 18.662 3.553 1.00 20.06 ? 44 ARG A CG 1 ATOM 371 C CD . ARG A 1 44 ? 33.393 20.028 4.172 1.00 22.04 ? 44 ARG A CD 1 ATOM 372 N NE . ARG A 1 44 ? 31.994 20.417 3.986 1.00 20.52 ? 44 ARG A NE 1 ATOM 373 C CZ . ARG A 1 44 ? 31.021 20.122 4.837 1.00 23.56 ? 44 ARG A CZ 1 ATOM 374 N NH1 . ARG A 1 44 ? 31.290 19.439 5.947 1.00 25.40 ? 44 ARG A NH1 1 ATOM 375 N NH2 . ARG A 1 44 ? 29.777 20.515 4.586 1.00 24.82 ? 44 ARG A NH2 1 ATOM 376 N N . LEU A 1 45 ? 34.966 15.894 5.858 1.00 20.59 ? 45 LEU A N 1 ATOM 377 C CA . LEU A 1 45 ? 34.382 14.838 6.669 1.00 22.65 ? 45 LEU A CA 1 ATOM 378 C C . LEU A 1 45 ? 35.468 14.301 7.584 1.00 30.80 ? 45 LEU A C 1 ATOM 379 O O . LEU A 1 45 ? 36.619 14.143 7.176 1.00 31.23 ? 45 LEU A O 1 ATOM 380 C CB . LEU A 1 45 ? 33.813 13.712 5.805 1.00 27.30 ? 45 LEU A CB 1 ATOM 381 C CG . LEU A 1 45 ? 32.665 14.093 4.868 1.00 32.74 ? 45 LEU A CG 1 ATOM 382 C CD1 . LEU A 1 45 ? 32.018 12.844 4.291 1.00 33.66 ? 45 LEU A CD1 1 ATOM 383 C CD2 . LEU A 1 45 ? 31.644 14.929 5.616 1.00 34.15 ? 45 LEU A CD2 1 ATOM 384 N N A GLU A 1 46 ? 35.117 14.009 8.834 0.48 43.28 ? 46 GLU A N 1 ATOM 385 N N B GLU A 1 46 ? 35.058 14.062 8.821 0.52 43.22 ? 46 GLU A N 1 ATOM 386 C CA A GLU A 1 46 ? 36.111 13.535 9.803 0.48 44.39 ? 46 GLU A CA 1 ATOM 387 C CA B GLU A 1 46 ? 35.890 13.582 9.908 0.52 45.37 ? 46 GLU A CA 1 ATOM 388 C C A GLU A 1 46 ? 36.783 12.229 9.372 0.48 43.44 ? 46 GLU A C 1 ATOM 389 C C B GLU A 1 46 ? 36.733 12.390 9.467 0.52 43.54 ? 46 GLU A C 1 ATOM 390 O O A GLU A 1 46 ? 37.964 12.013 9.650 0.48 43.92 ? 46 GLU A O 1 ATOM 391 O O B GLU A 1 46 ? 37.951 12.369 9.653 0.52 42.56 ? 46 GLU A O 1 ATOM 392 C CB A GLU A 1 46 ? 35.501 13.397 11.206 0.48 49.17 ? 46 GLU A CB 1 ATOM 393 C CB B GLU A 1 46 ? 34.982 13.182 11.081 0.52 50.75 ? 46 GLU A CB 1 ATOM 394 C CG A GLU A 1 46 ? 34.496 12.261 11.371 0.48 54.41 ? 46 GLU A CG 1 ATOM 395 C CG B GLU A 1 46 ? 33.956 14.260 11.525 0.52 54.48 ? 46 GLU A CG 1 ATOM 396 C CD A GLU A 1 46 ? 35.151 10.946 11.754 0.48 57.59 ? 46 GLU A CD 1 ATOM 397 C CD B GLU A 1 46 ? 32.881 14.588 10.475 0.52 50.03 ? 46 GLU A CD 1 ATOM 398 O OE1 A GLU A 1 46 ? 34.499 9.890 11.616 0.48 61.95 ? 46 GLU A OE1 1 ATOM 399 O OE1 B GLU A 1 46 ? 32.353 13.660 9.825 0.52 49.56 ? 46 GLU A OE1 1 ATOM 400 O OE2 A GLU A 1 46 ? 36.319 10.968 12.194 0.48 57.36 ? 46 GLU A OE2 1 ATOM 401 O OE2 B GLU A 1 46 ? 32.583 15.784 10.284 0.52 46.13 ? 46 GLU A OE2 1 ATOM 402 N N A GLU A 1 47 ? 36.030 11.374 8.683 0.48 43.93 ? 47 GLU A N 1 ATOM 403 N N B GLU A 1 47 ? 36.071 11.417 8.847 0.52 44.13 ? 47 GLU A N 1 ATOM 404 C CA A GLU A 1 47 ? 36.533 10.078 8.233 0.48 44.85 ? 47 GLU A CA 1 ATOM 405 C CA B GLU A 1 47 ? 36.701 10.162 8.449 0.52 44.86 ? 47 GLU A CA 1 ATOM 406 C C A GLU A 1 47 ? 37.755 10.230 7.331 0.48 40.45 ? 47 GLU A C 1 ATOM 407 C C B GLU A 1 47 ? 37.840 10.293 7.428 0.52 40.06 ? 47 GLU A C 1 ATOM 408 O O A GLU A 1 47 ? 38.624 9.356 7.302 0.48 38.43 ? 47 GLU A O 1 ATOM 409 O O B GLU A 1 47 ? 38.725 9.435 7.388 0.52 38.06 ? 47 GLU A O 1 ATOM 410 C CB A GLU A 1 47 ? 35.440 9.294 7.493 0.48 47.20 ? 47 GLU A CB 1 ATOM 411 C CB B GLU A 1 47 ? 35.644 9.171 7.944 0.52 47.09 ? 47 GLU A CB 1 ATOM 412 C CG A GLU A 1 47 ? 35.116 9.837 6.101 0.48 45.46 ? 47 GLU A CG 1 ATOM 413 C CG B GLU A 1 47 ? 34.748 9.710 6.835 0.52 47.76 ? 47 GLU A CG 1 ATOM 414 C CD A GLU A 1 47 ? 34.149 8.966 5.320 0.48 48.01 ? 47 GLU A CD 1 ATOM 415 C CD B GLU A 1 47 ? 33.363 10.107 7.330 0.52 50.58 ? 47 GLU A CD 1 ATOM 416 O OE1 A GLU A 1 47 ? 34.544 8.449 4.250 0.48 38.44 ? 47 GLU A OE1 1 ATOM 417 O OE1 B GLU A 1 47 ? 33.270 10.837 8.344 0.52 42.52 ? 47 GLU A OE1 1 ATOM 418 O OE2 A GLU A 1 47 ? 32.991 8.812 5.766 0.48 47.81 ? 47 GLU A OE2 1 ATOM 419 O OE2 B GLU A 1 47 ? 32.367 9.684 6.702 0.52 48.60 ? 47 GLU A OE2 1 ATOM 420 N N . PHE A 1 48 ? 37.814 11.345 6.606 1.00 34.35 ? 48 PHE A N 1 ATOM 421 C CA . PHE A 1 48 ? 38.869 11.570 5.613 1.00 33.83 ? 48 PHE A CA 1 ATOM 422 C C . PHE A 1 48 ? 40.256 11.583 6.255 1.00 31.12 ? 48 PHE A C 1 ATOM 423 O O . PHE A 1 48 ? 41.211 11.034 5.699 1.00 28.45 ? 48 PHE A O 1 ATOM 424 C CB . PHE A 1 48 ? 38.673 12.894 4.850 1.00 26.21 ? 48 PHE A CB 1 ATOM 425 C CG . PHE A 1 48 ? 37.465 12.925 3.935 1.00 30.37 ? 48 PHE A CG 1 ATOM 426 C CD1 . PHE A 1 48 ? 36.685 11.795 3.727 1.00 28.20 ? 48 PHE A CD1 1 ATOM 427 C CD2 . PHE A 1 48 ? 37.130 14.096 3.268 1.00 25.09 ? 48 PHE A CD2 1 ATOM 428 C CE1 . PHE A 1 48 ? 35.587 11.838 2.880 1.00 31.72 ? 48 PHE A CE1 1 ATOM 429 C CE2 . PHE A 1 48 ? 36.033 14.149 2.417 1.00 25.69 ? 48 PHE A CE2 1 ATOM 430 C CZ . PHE A 1 48 ? 35.261 13.018 2.222 1.00 27.68 ? 48 PHE A CZ 1 ATOM 431 N N . GLY A 1 49 ? 40.359 12.212 7.424 1.00 33.11 ? 49 GLY A N 1 ATOM 432 C CA . GLY A 1 49 ? 41.643 12.387 8.093 1.00 32.26 ? 49 GLY A CA 1 ATOM 433 C C . GLY A 1 49 ? 42.212 11.132 8.721 1.00 35.13 ? 49 GLY A C 1 ATOM 434 O O . GLY A 1 49 ? 43.372 11.102 9.140 1.00 34.08 ? 49 GLY A O 1 ATOM 435 N N . ARG A 1 50 ? 41.396 10.089 8.813 1.00 35.02 ? 50 ARG A N 1 ATOM 436 C CA . ARG A 1 50 ? 41.889 8.810 9.304 1.00 39.43 ? 50 ARG A CA 1 ATOM 437 C C . ARG A 1 50 ? 42.631 8.067 8.199 1.00 38.87 ? 50 ARG A C 1 ATOM 438 O O . ARG A 1 50 ? 43.475 7.220 8.470 1.00 44.33 ? 50 ARG A O 1 ATOM 439 C CB . ARG A 1 50 ? 40.748 7.960 9.868 1.00 49.46 ? 50 ARG A CB 1 ATOM 440 C CG . ARG A 1 50 ? 40.215 8.460 11.203 1.00 56.04 ? 50 ARG A CG 1 ATOM 441 C CD . ARG A 1 50 ? 39.391 7.392 11.896 1.00 68.80 ? 50 ARG A CD 1 ATOM 442 N NE . ARG A 1 50 ? 38.221 7.024 11.106 1.00 73.77 ? 50 ARG A NE 1 ATOM 443 C CZ . ARG A 1 50 ? 37.013 7.549 11.276 1.00 75.21 ? 50 ARG A CZ 1 ATOM 444 N NH1 . ARG A 1 50 ? 36.814 8.459 12.219 1.00 76.01 ? 50 ARG A NH1 1 ATOM 445 N NH2 . ARG A 1 50 ? 36.005 7.159 10.509 1.00 74.50 ? 50 ARG A NH2 1 ATOM 446 N N . PHE A 1 51 ? 42.334 8.424 6.953 1.00 42.20 ? 51 PHE A N 1 ATOM 447 C CA . PHE A 1 51 ? 42.881 7.731 5.793 1.00 44.48 ? 51 PHE A CA 1 ATOM 448 C C . PHE A 1 51 ? 44.047 8.482 5.159 1.00 37.07 ? 51 PHE A C 1 ATOM 449 O O . PHE A 1 51 ? 44.830 7.910 4.399 1.00 40.03 ? 51 PHE A O 1 ATOM 450 C CB . PHE A 1 51 ? 41.778 7.532 4.747 1.00 45.06 ? 51 PHE A CB 1 ATOM 451 C CG . PHE A 1 51 ? 40.568 6.806 5.274 1.00 59.20 ? 51 PHE A CG 1 ATOM 452 C CD1 . PHE A 1 51 ? 40.710 5.643 6.019 1.00 63.04 ? 51 PHE A CD1 1 ATOM 453 C CD2 . PHE A 1 51 ? 39.290 7.296 5.038 1.00 61.74 ? 51 PHE A CD2 1 ATOM 454 C CE1 . PHE A 1 51 ? 39.600 4.977 6.509 1.00 67.47 ? 51 PHE A CE1 1 ATOM 455 C CE2 . PHE A 1 51 ? 38.176 6.636 5.525 1.00 67.56 ? 51 PHE A CE2 1 ATOM 456 C CZ . PHE A 1 51 ? 38.331 5.475 6.263 1.00 69.45 ? 51 PHE A CZ 1 ATOM 457 N N . ALA A 1 52 ? 44.160 9.766 5.474 1.00 30.84 ? 52 ALA A N 1 ATOM 458 C CA . ALA A 1 52 ? 45.092 10.632 4.761 1.00 30.02 ? 52 ALA A CA 1 ATOM 459 C C . ALA A 1 52 ? 45.588 11.775 5.640 1.00 31.75 ? 52 ALA A C 1 ATOM 460 O O . ALA A 1 52 ? 45.000 12.087 6.675 1.00 27.86 ? 52 ALA A O 1 ATOM 461 C CB . ALA A 1 52 ? 44.427 11.180 3.495 1.00 25.68 ? 52 ALA A CB 1 ATOM 462 N N . SER A 1 53 ? 46.683 12.391 5.223 1.00 31.32 ? 53 SER A N 1 ATOM 463 C CA . SER A 1 53 ? 47.256 13.496 5.969 1.00 27.74 ? 53 SER A CA 1 ATOM 464 C C . SER A 1 53 ? 47.668 14.585 4.990 1.00 25.15 ? 53 SER A C 1 ATOM 465 O O . SER A 1 53 ? 47.847 14.318 3.798 1.00 26.30 ? 53 SER A O 1 ATOM 466 C CB . SER A 1 53 ? 48.473 13.021 6.768 1.00 30.69 ? 53 SER A CB 1 ATOM 467 O OG . SER A 1 53 ? 49.501 12.587 5.898 1.00 36.19 ? 53 SER A OG 1 ATOM 468 N N . PHE A 1 54 ? 47.783 15.814 5.487 1.00 26.62 ? 54 PHE A N 1 ATOM 469 C CA . PHE A 1 54 ? 48.362 16.906 4.712 1.00 27.89 ? 54 PHE A CA 1 ATOM 470 C C . PHE A 1 54 ? 49.140 17.851 5.625 1.00 30.48 ? 54 PHE A C 1 ATOM 471 O O . PHE A 1 54 ? 48.618 18.328 6.631 1.00 28.96 ? 54 PHE A O 1 ATOM 472 C CB . PHE A 1 54 ? 47.292 17.674 3.920 1.00 23.39 ? 54 PHE A CB 1 ATOM 473 C CG . PHE A 1 54 ? 47.856 18.815 3.101 1.00 20.32 ? 54 PHE A CG 1 ATOM 474 C CD1 . PHE A 1 54 ? 48.556 18.567 1.928 1.00 24.54 ? 54 PHE A CD1 1 ATOM 475 C CD2 . PHE A 1 54 ? 47.717 20.127 3.529 1.00 22.16 ? 54 PHE A CD2 1 ATOM 476 C CE1 . PHE A 1 54 ? 49.084 19.625 1.175 1.00 27.10 ? 54 PHE A CE1 1 ATOM 477 C CE2 . PHE A 1 54 ? 48.241 21.186 2.789 1.00 25.86 ? 54 PHE A CE2 1 ATOM 478 C CZ . PHE A 1 54 ? 48.926 20.933 1.611 1.00 21.25 ? 54 PHE A CZ 1 ATOM 479 N N . GLU A 1 55 ? 50.399 18.099 5.279 1.00 30.72 ? 55 GLU A N 1 ATOM 480 C CA . GLU A 1 55 ? 51.218 19.060 6.007 1.00 31.03 ? 55 GLU A CA 1 ATOM 481 C C . GLU A 1 55 ? 50.753 20.481 5.695 1.00 29.03 ? 55 GLU A C 1 ATOM 482 O O . GLU A 1 55 ? 51.015 21.003 4.606 1.00 30.12 ? 55 GLU A O 1 ATOM 483 C CB . GLU A 1 55 ? 52.693 18.893 5.626 1.00 35.78 ? 55 GLU A CB 1 ATOM 484 C CG . GLU A 1 55 ? 53.626 19.887 6.287 1.00 45.05 ? 55 GLU A CG 1 ATOM 485 C CD . GLU A 1 55 ? 53.394 19.977 7.777 1.00 53.88 ? 55 GLU A CD 1 ATOM 486 O OE1 . GLU A 1 55 ? 53.404 18.920 8.446 1.00 58.51 ? 55 GLU A OE1 1 ATOM 487 O OE2 . GLU A 1 55 ? 53.183 21.105 8.273 1.00 58.15 ? 55 GLU A OE2 1 ATOM 488 N N . ALA A 1 56 ? 50.063 21.106 6.646 1.00 25.05 ? 56 ALA A N 1 ATOM 489 C CA . ALA A 1 56 ? 49.461 22.426 6.416 1.00 23.87 ? 56 ALA A CA 1 ATOM 490 C C . ALA A 1 56 ? 50.469 23.526 6.070 1.00 30.33 ? 56 ALA A C 1 ATOM 491 O O . ALA A 1 56 ? 50.129 24.489 5.385 1.00 28.62 ? 56 ALA A O 1 ATOM 492 C CB . ALA A 1 56 ? 48.612 22.846 7.616 1.00 28.66 ? 56 ALA A CB 1 ATOM 493 N N . GLN A 1 57 ? 51.700 23.379 6.549 1.00 32.51 ? 57 GLN A N 1 ATOM 494 C CA . GLN A 1 57 ? 52.743 24.377 6.332 1.00 36.53 ? 57 GLN A CA 1 ATOM 495 C C . GLN A 1 57 ? 52.962 24.692 4.855 1.00 33.43 ? 57 GLN A C 1 ATOM 496 O O . GLN A 1 57 ? 53.187 25.846 4.486 1.00 37.22 ? 57 GLN A O 1 ATOM 497 C CB . GLN A 1 57 ? 54.053 23.930 6.993 1.00 47.60 ? 57 GLN A CB 1 ATOM 498 C CG . GLN A 1 57 ? 55.127 25.003 7.032 1.00 59.20 ? 57 GLN A CG 1 ATOM 499 C CD . GLN A 1 57 ? 54.653 26.271 7.721 1.00 65.92 ? 57 GLN A CD 1 ATOM 500 O OE1 . GLN A 1 57 ? 54.000 26.218 8.766 1.00 66.73 ? 57 GLN A OE1 1 ATOM 501 N NE2 . GLN A 1 57 ? 54.966 27.420 7.127 1.00 65.58 ? 57 GLN A NE2 1 ATOM 502 N N . GLY A 1 58 ? 52.863 23.677 4.004 1.00 31.49 ? 58 GLY A N 1 ATOM 503 C CA . GLY A 1 58 ? 53.026 23.878 2.572 1.00 28.80 ? 58 GLY A CA 1 ATOM 504 C C . GLY A 1 58 ? 52.018 24.825 1.955 1.00 29.13 ? 58 GLY A C 1 ATOM 505 O O . GLY A 1 58 ? 52.331 25.541 1.000 1.00 28.66 ? 58 GLY A O 1 ATOM 506 N N . ALA A 1 59 ? 50.801 24.837 2.494 1.00 26.97 ? 59 ALA A N 1 ATOM 507 C CA . ALA A 1 59 ? 49.777 25.779 2.037 1.00 28.27 ? 59 ALA A CA 1 ATOM 508 C C . ALA A 1 59 ? 50.194 27.233 2.278 1.00 23.64 ? 59 ALA A C 1 ATOM 509 O O . ALA A 1 59 ? 50.001 28.100 1.418 1.00 19.26 ? 59 ALA A O 1 ATOM 510 C CB . ALA A 1 59 ? 48.440 25.500 2.716 1.00 24.00 ? 59 ALA A CB 1 ATOM 511 N N . LEU A 1 60 ? 50.748 27.492 3.456 1.00 32.29 ? 60 LEU A N 1 ATOM 512 C CA . LEU A 1 60 ? 51.174 28.837 3.828 1.00 31.83 ? 60 LEU A CA 1 ATOM 513 C C . LEU A 1 60 ? 52.229 29.349 2.861 1.00 28.79 ? 60 LEU A C 1 ATOM 514 O O . LEU A 1 60 ? 52.194 30.514 2.447 1.00 28.15 ? 60 LEU A O 1 ATOM 515 C CB . LEU A 1 60 ? 51.704 28.864 5.267 1.00 36.12 ? 60 LEU A CB 1 ATOM 516 C CG . LEU A 1 60 ? 50.673 28.919 6.402 1.00 41.89 ? 60 LEU A CG 1 ATOM 517 C CD1 . LEU A 1 60 ? 49.790 27.680 6.451 1.00 43.87 ? 60 LEU A CD1 1 ATOM 518 C CD2 . LEU A 1 60 ? 51.375 29.107 7.729 1.00 45.83 ? 60 LEU A CD2 1 ATOM 519 N N . ALA A 1 61 ? 53.152 28.468 2.484 1.00 20.80 ? 61 ALA A N 1 ATOM 520 C CA . ALA A 1 61 ? 54.194 28.812 1.518 1.00 24.79 ? 61 ALA A CA 1 ATOM 521 C C . ALA A 1 61 ? 53.593 29.217 0.171 1.00 27.04 ? 61 ALA A C 1 ATOM 522 O O . ALA A 1 61 ? 53.973 30.238 -0.416 1.00 24.23 ? 61 ALA A O 1 ATOM 523 C CB . ALA A 1 61 ? 55.154 27.653 1.341 1.00 24.73 ? 61 ALA A CB 1 ATOM 524 N N . ASN A 1 62 ? 52.660 28.411 -0.325 1.00 21.47 ? 62 ASN A N 1 ATOM 525 C CA . ASN A 1 62 ? 51.971 28.738 -1.571 1.00 23.38 ? 62 ASN A CA 1 ATOM 526 C C . ASN A 1 62 ? 51.213 30.060 -1.528 1.00 18.49 ? 62 ASN A C 1 ATOM 527 O O . ASN A 1 62 ? 51.233 30.833 -2.490 1.00 16.78 ? 62 ASN A O 1 ATOM 528 C CB . ASN A 1 62 ? 51.017 27.611 -1.964 1.00 16.16 ? 62 ASN A CB 1 ATOM 529 C CG . ASN A 1 62 ? 51.690 26.574 -2.845 1.00 24.04 ? 62 ASN A CG 1 ATOM 530 O OD1 . ASN A 1 62 ? 52.922 26.479 -2.883 1.00 21.55 ? 62 ASN A OD1 1 ATOM 531 N ND2 . ASN A 1 62 ? 50.889 25.806 -3.574 1.00 20.78 ? 62 ASN A ND2 1 ATOM 532 N N . ILE A 1 63 ? 50.519 30.303 -0.422 1.00 17.70 ? 63 ILE A N 1 ATOM 533 C CA . ILE A 1 63 ? 49.721 31.510 -0.285 1.00 20.25 ? 63 ILE A CA 1 ATOM 534 C C . ILE A 1 63 ? 50.649 32.736 -0.289 1.00 16.25 ? 63 ILE A C 1 ATOM 535 O O . ILE A 1 63 ? 50.309 33.782 -0.841 1.00 20.02 ? 63 ILE A O 1 ATOM 536 C CB . ILE A 1 63 ? 48.826 31.480 0.992 1.00 24.32 ? 63 ILE A CB 1 ATOM 537 C CG1 . ILE A 1 63 ? 47.498 30.736 0.748 1.00 25.19 ? 63 ILE A CG1 1 ATOM 538 C CG2 . ILE A 1 63 ? 48.519 32.900 1.480 1.00 24.33 ? 63 ILE A CG2 1 ATOM 539 C CD1 . ILE A 1 63 ? 47.311 30.129 -0.620 1.00 27.42 ? 63 ILE A CD1 1 ATOM 540 N N . ALA A 1 64 ? 51.825 32.593 0.310 1.00 16.86 ? 64 ALA A N 1 ATOM 541 C CA . ALA A 1 64 ? 52.821 33.662 0.269 1.00 20.14 ? 64 ALA A CA 1 ATOM 542 C C . ALA A 1 64 ? 53.241 33.970 -1.177 1.00 23.91 ? 64 ALA A C 1 ATOM 543 O O . ALA A 1 64 ? 53.396 35.130 -1.546 1.00 25.97 ? 64 ALA A O 1 ATOM 544 C CB . ALA A 1 64 ? 54.036 33.297 1.116 1.00 19.92 ? 64 ALA A CB 1 ATOM 545 N N . VAL A 1 65 ? 53.434 32.934 -1.992 1.00 21.78 ? 65 VAL A N 1 ATOM 546 C CA . VAL A 1 65 ? 53.776 33.144 -3.401 1.00 16.66 ? 65 VAL A CA 1 ATOM 547 C C . VAL A 1 65 ? 52.597 33.843 -4.106 1.00 18.57 ? 65 VAL A C 1 ATOM 548 O O . VAL A 1 65 ? 52.784 34.800 -4.865 1.00 16.51 ? 65 VAL A O 1 ATOM 549 C CB . VAL A 1 65 ? 54.155 31.815 -4.108 1.00 16.85 ? 65 VAL A CB 1 ATOM 550 C CG1 . VAL A 1 65 ? 54.219 32.000 -5.619 1.00 18.26 ? 65 VAL A CG1 1 ATOM 551 C CG2 . VAL A 1 65 ? 55.504 31.271 -3.581 1.00 18.28 ? 65 VAL A CG2 1 ATOM 552 N N . ASP A 1 66 ? 51.380 33.390 -3.812 1.00 17.64 ? 66 ASP A N 1 ATOM 553 C CA . ASP A 1 66 ? 50.181 33.965 -4.422 1.00 18.99 ? 66 ASP A CA 1 ATOM 554 C C . ASP A 1 66 ? 50.053 35.459 -4.113 1.00 18.26 ? 66 ASP A C 1 ATOM 555 O O . ASP A 1 66 ? 49.691 36.249 -4.978 1.00 15.69 ? 66 ASP A O 1 ATOM 556 C CB . ASP A 1 66 ? 48.918 33.232 -3.960 1.00 16.86 ? 66 ASP A CB 1 ATOM 557 C CG . ASP A 1 66 ? 48.889 31.784 -4.399 1.00 16.13 ? 66 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 66 ? 49.622 31.432 -5.349 1.00 18.07 ? 66 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 66 ? 48.119 31.003 -3.793 1.00 17.52 ? 66 ASP A OD2 1 ATOM 560 N N . LYS A 1 67 ? 50.370 35.838 -2.884 1.00 18.00 ? 67 LYS A N 1 ATOM 561 C CA . LYS A 1 67 ? 50.346 37.245 -2.487 1.00 19.17 ? 67 LYS A CA 1 ATOM 562 C C . LYS A 1 67 ? 51.376 38.062 -3.280 1.00 23.91 ? 67 LYS A C 1 ATOM 563 O O . LYS A 1 67 ? 51.064 39.143 -3.792 1.00 19.97 ? 67 LYS A O 1 ATOM 564 C CB . LYS A 1 67 ? 50.584 37.361 -0.976 1.00 23.78 ? 67 LYS A CB 1 ATOM 565 C CG . LYS A 1 67 ? 50.903 38.766 -0.458 1.00 23.37 ? 67 LYS A CG 1 ATOM 566 C CD . LYS A 1 67 ? 51.176 38.718 1.046 1.00 26.85 ? 67 LYS A CD 1 ATOM 567 C CE . LYS A 1 67 ? 51.817 40.003 1.568 1.00 34.00 ? 67 LYS A CE 1 ATOM 568 N NZ . LYS A 1 67 ? 50.806 41.008 1.945 1.00 36.62 ? 67 LYS A NZ 1 ATOM 569 N N . ALA A 1 68 ? 52.599 37.548 -3.397 1.00 20.31 ? 68 ALA A N 1 ATOM 570 C CA . ALA A 1 68 ? 53.615 38.225 -4.203 1.00 21.88 ? 68 ALA A CA 1 ATOM 571 C C . ALA A 1 68 ? 53.177 38.314 -5.666 1.00 20.62 ? 68 ALA A C 1 ATOM 572 O O . ALA A 1 68 ? 53.334 39.359 -6.308 1.00 18.95 ? 68 ALA A O 1 ATOM 573 C CB . ALA A 1 68 ? 54.968 37.515 -4.091 1.00 27.38 ? 68 ALA A CB 1 ATOM 574 N N . ASN A 1 69 ? 52.622 37.225 -6.190 1.00 17.07 ? 69 ASN A N 1 ATOM 575 C CA . ASN A 1 69 ? 52.139 37.228 -7.570 1.00 17.19 ? 69 ASN A CA 1 ATOM 576 C C . ASN A 1 69 ? 50.988 38.204 -7.783 1.00 16.53 ? 69 ASN A C 1 ATOM 577 O O . ASN A 1 69 ? 50.896 38.836 -8.839 1.00 19.13 ? 69 ASN A O 1 ATOM 578 C CB . ASN A 1 69 ? 51.757 35.820 -8.045 1.00 19.65 ? 69 ASN A CB 1 ATOM 579 C CG . ASN A 1 69 ? 52.975 34.941 -8.305 1.00 23.89 ? 69 ASN A CG 1 ATOM 580 O OD1 . ASN A 1 69 ? 54.113 35.419 -8.308 1.00 26.61 ? 69 ASN A OD1 1 ATOM 581 N ND2 . ASN A 1 69 ? 52.739 33.656 -8.535 1.00 16.12 ? 69 ASN A ND2 1 ATOM 582 N N . LEU A 1 70 ? 50.109 38.335 -6.792 1.00 15.10 ? 70 LEU A N 1 ATOM 583 C CA . LEU A 1 70 ? 49.008 39.295 -6.911 1.00 16.95 ? 70 LEU A CA 1 ATOM 584 C C . LEU A 1 70 ? 49.550 40.721 -7.081 1.00 19.81 ? 70 LEU A C 1 ATOM 585 O O . LEU A 1 70 ? 49.031 41.497 -7.881 1.00 20.93 ? 70 LEU A O 1 ATOM 586 C CB . LEU A 1 70 ? 48.082 39.228 -5.695 1.00 15.99 ? 70 LEU A CB 1 ATOM 587 C CG . LEU A 1 70 ? 46.925 40.235 -5.703 1.00 19.93 ? 70 LEU A CG 1 ATOM 588 C CD1 . LEU A 1 70 ? 46.124 40.149 -7.009 1.00 17.33 ? 70 LEU A CD1 1 ATOM 589 C CD2 . LEU A 1 70 ? 46.013 40.032 -4.491 1.00 21.10 ? 70 LEU A CD2 1 ATOM 590 N N A GLU A 1 71 ? 50.591 41.053 -6.318 0.55 15.58 ? 71 GLU A N 1 ATOM 591 N N B GLU A 1 71 ? 50.592 41.055 -6.325 0.45 16.12 ? 71 GLU A N 1 ATOM 592 C CA A GLU A 1 71 ? 51.252 42.353 -6.423 0.55 19.79 ? 71 GLU A CA 1 ATOM 593 C CA B GLU A 1 71 ? 51.212 42.376 -6.420 0.45 19.16 ? 71 GLU A CA 1 ATOM 594 C C A GLU A 1 71 ? 51.713 42.602 -7.846 0.55 19.33 ? 71 GLU A C 1 ATOM 595 C C B GLU A 1 71 ? 51.781 42.634 -7.816 0.45 19.34 ? 71 GLU A C 1 ATOM 596 O O A GLU A 1 71 ? 51.455 43.659 -8.432 0.55 19.71 ? 71 GLU A O 1 ATOM 597 O O B GLU A 1 71 ? 51.642 43.732 -8.367 0.45 19.64 ? 71 GLU A O 1 ATOM 598 C CB A GLU A 1 71 ? 52.478 42.404 -5.517 0.55 25.85 ? 71 GLU A CB 1 ATOM 599 C CB B GLU A 1 71 ? 52.304 42.534 -5.360 0.45 24.76 ? 71 GLU A CB 1 ATOM 600 C CG A GLU A 1 71 ? 52.197 42.362 -4.039 0.55 29.09 ? 71 GLU A CG 1 ATOM 601 C CG B GLU A 1 71 ? 53.178 43.773 -5.533 0.45 28.60 ? 71 GLU A CG 1 ATOM 602 C CD A GLU A 1 71 ? 53.472 42.467 -3.219 0.55 40.00 ? 71 GLU A CD 1 ATOM 603 C CD B GLU A 1 71 ? 52.394 45.070 -5.441 0.45 30.70 ? 71 GLU A CD 1 ATOM 604 O OE1 A GLU A 1 71 ? 54.356 43.278 -3.587 0.55 39.59 ? 71 GLU A OE1 1 ATOM 605 O OE1 B GLU A 1 71 ? 51.328 45.084 -4.784 0.45 30.55 ? 71 GLU A OE1 1 ATOM 606 O OE2 A GLU A 1 71 ? 53.597 41.721 -2.224 0.55 41.57 ? 71 GLU A OE2 1 ATOM 607 O OE2 B GLU A 1 71 ? 52.845 46.078 -6.026 0.45 32.08 ? 71 GLU A OE2 1 ATOM 608 N N . ILE A 1 72 ? 52.415 41.616 -8.387 1.00 17.47 ? 72 ILE A N 1 ATOM 609 C CA . ILE A 1 72 ? 52.935 41.691 -9.738 1.00 24.73 ? 72 ILE A CA 1 ATOM 610 C C . ILE A 1 72 ? 51.809 41.888 -10.753 1.00 21.77 ? 72 ILE A C 1 ATOM 611 O O . ILE A 1 72 ? 51.899 42.776 -11.607 1.00 21.01 ? 72 ILE A O 1 ATOM 612 C CB . ILE A 1 72 ? 53.742 40.422 -10.087 1.00 28.55 ? 72 ILE A CB 1 ATOM 613 C CG1 . ILE A 1 72 ? 55.065 40.413 -9.312 1.00 29.37 ? 72 ILE A CG1 1 ATOM 614 C CG2 . ILE A 1 72 ? 53.995 40.338 -11.584 1.00 29.17 ? 72 ILE A CG2 1 ATOM 615 C CD1 . ILE A 1 72 ? 55.784 39.087 -9.342 1.00 34.80 ? 72 ILE A CD1 1 ATOM 616 N N . MET A 1 73 ? 50.748 41.085 -10.642 1.00 19.83 ? 73 MET A N 1 ATOM 617 C CA . MET A 1 73 ? 49.675 41.101 -11.642 1.00 16.53 ? 73 MET A CA 1 ATOM 618 C C . MET A 1 73 ? 48.845 42.373 -11.532 1.00 18.18 ? 73 MET A C 1 ATOM 619 O O . MET A 1 73 ? 48.387 42.918 -12.537 1.00 22.00 ? 73 MET A O 1 ATOM 620 C CB . MET A 1 73 ? 48.771 39.865 -11.518 1.00 19.96 ? 73 MET A CB 1 ATOM 621 C CG . MET A 1 73 ? 49.501 38.532 -11.727 1.00 17.93 ? 73 MET A CG 1 ATOM 622 S SD . MET A 1 73 ? 50.523 38.459 -13.216 1.00 23.43 ? 73 MET A SD 1 ATOM 623 C CE . MET A 1 73 ? 49.324 38.824 -14.502 1.00 14.48 ? 73 MET A CE 1 ATOM 624 N N . THR A 1 74 ? 48.650 42.834 -10.302 1.00 16.55 ? 74 THR A N 1 ATOM 625 C CA . THR A 1 74 ? 47.961 44.092 -10.055 1.00 20.21 ? 74 THR A CA 1 ATOM 626 C C . THR A 1 74 ? 48.624 45.233 -10.831 1.00 20.66 ? 74 THR A C 1 ATOM 627 O O . THR A 1 74 ? 47.929 46.022 -11.479 1.00 16.66 ? 74 THR A O 1 ATOM 628 C CB . THR A 1 74 ? 47.899 44.406 -8.540 1.00 17.63 ? 74 THR A CB 1 ATOM 629 O OG1 . THR A 1 74 ? 47.102 43.399 -7.886 1.00 19.08 ? 74 THR A OG1 1 ATOM 630 C CG2 . THR A 1 74 ? 47.294 45.788 -8.285 1.00 16.78 ? 74 THR A CG2 1 ATOM 631 N N . LYS A 1 75 ? 49.957 45.296 -10.788 1.00 21.04 ? 75 LYS A N 1 ATOM 632 C CA A LYS A 1 75 ? 50.703 46.330 -11.505 0.39 22.20 ? 75 LYS A CA 1 ATOM 633 C CA B LYS A 1 75 ? 50.721 46.317 -11.513 0.61 22.01 ? 75 LYS A CA 1 ATOM 634 C C . LYS A 1 75 ? 50.636 46.132 -13.017 1.00 20.46 ? 75 LYS A C 1 ATOM 635 O O . LYS A 1 75 ? 50.533 47.104 -13.772 1.00 22.86 ? 75 LYS A O 1 ATOM 636 C CB A LYS A 1 75 ? 52.174 46.362 -11.060 0.39 25.10 ? 75 LYS A CB 1 ATOM 637 C CB B LYS A 1 75 ? 52.204 46.272 -11.125 0.61 25.72 ? 75 LYS A CB 1 ATOM 638 C CG A LYS A 1 75 ? 52.388 46.477 -9.558 0.39 24.22 ? 75 LYS A CG 1 ATOM 639 C CG B LYS A 1 75 ? 52.554 46.912 -9.805 0.61 26.64 ? 75 LYS A CG 1 ATOM 640 C CD A LYS A 1 75 ? 53.882 46.498 -9.201 0.39 25.88 ? 75 LYS A CD 1 ATOM 641 C CD B LYS A 1 75 ? 54.041 46.716 -9.493 0.61 26.58 ? 75 LYS A CD 1 ATOM 642 C CE A LYS A 1 75 ? 54.102 46.464 -7.689 0.39 23.68 ? 75 LYS A CE 1 ATOM 643 C CE B LYS A 1 75 ? 54.916 47.087 -10.684 0.61 25.32 ? 75 LYS A CE 1 ATOM 644 N NZ A LYS A 1 75 ? 55.540 46.594 -7.299 0.39 26.56 ? 75 LYS A NZ 1 ATOM 645 N NZ B LYS A 1 75 ? 56.372 46.937 -10.380 0.61 31.82 ? 75 LYS A NZ 1 ATOM 646 N N . ARG A 1 76 ? 50.715 44.877 -13.459 1.00 19.47 ? 76 ARG A N 1 ATOM 647 C CA . ARG A 1 76 ? 50.655 44.578 -14.884 1.00 21.91 ? 76 ARG A CA 1 ATOM 648 C C . ARG A 1 76 ? 49.331 45.050 -15.453 1.00 17.51 ? 76 ARG A C 1 ATOM 649 O O . ARG A 1 76 ? 49.276 45.545 -16.572 1.00 23.58 ? 76 ARG A O 1 ATOM 650 C CB . ARG A 1 76 ? 50.836 43.070 -15.170 1.00 17.12 ? 76 ARG A CB 1 ATOM 651 C CG . ARG A 1 76 ? 52.270 42.640 -15.411 1.00 27.77 ? 76 ARG A CG 1 ATOM 652 C CD . ARG A 1 76 ? 52.371 41.197 -15.931 1.00 25.52 ? 76 ARG A CD 1 ATOM 653 N NE . ARG A 1 76 ? 53.494 40.493 -15.313 1.00 26.33 ? 76 ARG A NE 1 ATOM 654 C CZ . ARG A 1 76 ? 53.642 39.171 -15.299 1.00 30.39 ? 76 ARG A CZ 1 ATOM 655 N NH1 . ARG A 1 76 ? 52.742 38.377 -15.884 1.00 26.28 ? 76 ARG A NH1 1 ATOM 656 N NH2 . ARG A 1 76 ? 54.701 38.635 -14.702 1.00 33.04 ? 76 ARG A NH2 1 ATOM 657 N N . SER A 1 77 ? 48.270 44.905 -14.662 1.00 16.83 ? 77 SER A N 1 ATOM 658 C CA . SER A 1 77 ? 46.918 45.263 -15.090 1.00 17.08 ? 77 SER A CA 1 ATOM 659 C C . SER A 1 77 ? 46.650 46.764 -15.020 1.00 21.82 ? 77 SER A C 1 ATOM 660 O O . SER A 1 77 ? 45.527 47.209 -15.311 1.00 20.11 ? 77 SER A O 1 ATOM 661 C CB . SER A 1 77 ? 45.884 44.566 -14.198 1.00 19.65 ? 77 SER A CB 1 ATOM 662 O OG . SER A 1 77 ? 45.711 45.274 -12.976 1.00 21.04 ? 77 SER A OG 1 ATOM 663 N N . ASN A 1 78 ? 47.673 47.534 -14.639 1.00 20.02 ? 78 ASN A N 1 ATOM 664 C CA . ASN A 1 78 ? 47.515 48.956 -14.326 1.00 19.47 ? 78 ASN A CA 1 ATOM 665 C C . ASN A 1 78 ? 46.477 49.169 -13.227 1.00 21.13 ? 78 ASN A C 1 ATOM 666 O O . ASN A 1 78 ? 45.635 50.054 -13.319 1.00 22.67 ? 78 ASN A O 1 ATOM 667 C CB . ASN A 1 78 ? 47.149 49.751 -15.579 1.00 20.51 ? 78 ASN A CB 1 ATOM 668 C CG . ASN A 1 78 ? 48.180 49.604 -16.675 1.00 28.23 ? 78 ASN A CG 1 ATOM 669 O OD1 . ASN A 1 78 ? 49.383 49.609 -16.402 1.00 31.84 ? 78 ASN A OD1 1 ATOM 670 N ND2 . ASN A 1 78 ? 47.718 49.455 -17.922 1.00 38.27 ? 78 ASN A ND2 1 ATOM 671 N N . TYR A 1 79 ? 46.544 48.344 -12.184 1.00 21.10 ? 79 TYR A N 1 ATOM 672 C CA . TYR A 1 79 ? 45.628 48.444 -11.046 1.00 20.32 ? 79 TYR A CA 1 ATOM 673 C C . TYR A 1 79 ? 44.140 48.352 -11.430 1.00 26.50 ? 79 TYR A C 1 ATOM 674 O O . TYR A 1 79 ? 43.307 49.079 -10.898 1.00 26.07 ? 79 TYR A O 1 ATOM 675 C CB . TYR A 1 79 ? 45.928 49.705 -10.226 1.00 23.31 ? 79 TYR A CB 1 ATOM 676 C CG . TYR A 1 79 ? 47.327 49.681 -9.656 1.00 23.80 ? 79 TYR A CG 1 ATOM 677 C CD1 . TYR A 1 79 ? 47.557 49.287 -8.340 1.00 20.92 ? 79 TYR A CD1 1 ATOM 678 C CD2 . TYR A 1 79 ? 48.427 50.009 -10.445 1.00 21.11 ? 79 TYR A CD2 1 ATOM 679 C CE1 . TYR A 1 79 ? 48.838 49.239 -7.823 1.00 22.69 ? 79 TYR A CE1 1 ATOM 680 C CE2 . TYR A 1 79 ? 49.715 49.959 -9.934 1.00 25.16 ? 79 TYR A CE2 1 ATOM 681 C CZ . TYR A 1 79 ? 49.910 49.572 -8.620 1.00 25.83 ? 79 TYR A CZ 1 ATOM 682 O OH . TYR A 1 79 ? 51.189 49.522 -8.114 1.00 32.45 ? 79 TYR A OH 1 ATOM 683 N N . THR A 1 80 ? 43.816 47.446 -12.349 1.00 20.84 ? 80 THR A N 1 ATOM 684 C CA . THR A 1 80 ? 42.426 47.182 -12.703 1.00 20.19 ? 80 THR A CA 1 ATOM 685 C C . THR A 1 80 ? 41.812 46.303 -11.617 1.00 20.97 ? 80 THR A C 1 ATOM 686 O O . THR A 1 80 ? 42.277 45.177 -11.400 1.00 19.83 ? 80 THR A O 1 ATOM 687 C CB . THR A 1 80 ? 42.326 46.442 -14.056 1.00 22.79 ? 80 THR A CB 1 ATOM 688 O OG1 . THR A 1 80 ? 42.965 47.219 -15.073 1.00 25.31 ? 80 THR A OG1 1 ATOM 689 C CG2 . THR A 1 80 ? 40.860 46.197 -14.438 1.00 16.94 ? 80 THR A CG2 1 ATOM 690 N N . PRO A 1 81 ? 40.787 46.814 -10.916 1.00 16.75 ? 81 PRO A N 1 ATOM 691 C CA . PRO A 1 81 ? 40.170 46.067 -9.810 1.00 19.14 ? 81 PRO A CA 1 ATOM 692 C C . PRO A 1 81 ? 39.167 45.018 -10.294 1.00 22.20 ? 81 PRO A C 1 ATOM 693 O O . PRO A 1 81 ? 38.770 45.014 -11.459 1.00 18.59 ? 81 PRO A O 1 ATOM 694 C CB . PRO A 1 81 ? 39.437 47.158 -9.020 1.00 19.15 ? 81 PRO A CB 1 ATOM 695 C CG . PRO A 1 81 ? 39.054 48.156 -10.059 1.00 26.15 ? 81 PRO A CG 1 ATOM 696 C CD . PRO A 1 81 ? 40.183 48.150 -11.085 1.00 17.12 ? 81 PRO A CD 1 ATOM 697 N N . ILE A 1 82 ? 38.770 44.125 -9.399 1.00 17.33 ? 82 ILE A N 1 ATOM 698 C CA . ILE A 1 82 ? 37.771 43.120 -9.740 1.00 21.18 ? 82 ILE A CA 1 ATOM 699 C C . ILE A 1 82 ? 36.397 43.785 -9.824 1.00 21.50 ? 82 ILE A C 1 ATOM 700 O O . ILE A 1 82 ? 36.131 44.763 -9.125 1.00 21.26 ? 82 ILE A O 1 ATOM 701 C CB . ILE A 1 82 ? 37.761 41.969 -8.698 1.00 13.38 ? 82 ILE A CB 1 ATOM 702 C CG1 . ILE A 1 82 ? 37.042 40.723 -9.238 1.00 15.44 ? 82 ILE A CG1 1 ATOM 703 C CG2 . ILE A 1 82 ? 37.205 42.454 -7.354 1.00 18.99 ? 82 ILE A CG2 1 ATOM 704 C CD1 . ILE A 1 82 ? 37.370 39.450 -8.439 1.00 18.22 ? 82 ILE A CD1 1 ATOM 705 N N . THR A 1 83 ? 35.541 43.279 -10.709 1.00 17.13 ? 83 THR A N 1 ATOM 706 C CA . THR A 1 83 ? 34.151 43.724 -10.768 1.00 21.65 ? 83 THR A CA 1 ATOM 707 C C . THR A 1 83 ? 33.296 42.821 -9.870 1.00 18.95 ? 83 THR A C 1 ATOM 708 O O . THR A 1 83 ? 33.373 41.592 -9.969 1.00 18.64 ? 83 THR A O 1 ATOM 709 C CB . THR A 1 83 ? 33.618 43.685 -12.214 1.00 26.80 ? 83 THR A CB 1 ATOM 710 O OG1 . THR A 1 83 ? 34.372 44.597 -13.020 1.00 23.88 ? 83 THR A OG1 1 ATOM 711 C CG2 . THR A 1 83 ? 32.125 44.062 -12.270 1.00 26.26 ? 83 THR A CG2 1 ATOM 712 N N . ASN A 1 84 ? 32.507 43.426 -8.980 1.00 17.11 ? 84 ASN A N 1 ATOM 713 C CA . ASN A 1 84 ? 31.678 42.649 -8.049 1.00 21.31 ? 84 ASN A CA 1 ATOM 714 C C . ASN A 1 84 ? 30.608 41.889 -8.815 1.00 24.01 ? 84 ASN A C 1 ATOM 715 O O . ASN A 1 84 ? 29.965 42.457 -9.694 1.00 18.77 ? 84 ASN A O 1 ATOM 716 C CB . ASN A 1 84 ? 31.006 43.563 -7.009 1.00 22.56 ? 84 ASN A CB 1 ATOM 717 C CG . ASN A 1 84 ? 32.009 44.263 -6.112 1.00 22.43 ? 84 ASN A CG 1 ATOM 718 O OD1 . ASN A 1 84 ? 33.005 43.673 -5.706 1.00 20.44 ? 84 ASN A OD1 1 ATOM 719 N ND2 . ASN A 1 84 ? 31.757 45.531 -5.813 1.00 17.50 ? 84 ASN A ND2 1 ATOM 720 N N . VAL A 1 85 ? 30.455 40.600 -8.501 1.00 15.96 ? 85 VAL A N 1 ATOM 721 C CA . VAL A 1 85 ? 29.397 39.775 -9.045 1.00 17.95 ? 85 VAL A CA 1 ATOM 722 C C . VAL A 1 85 ? 28.583 39.295 -7.842 1.00 20.42 ? 85 VAL A C 1 ATOM 723 O O . VAL A 1 85 ? 29.068 38.492 -7.045 1.00 18.11 ? 85 VAL A O 1 ATOM 724 C CB . VAL A 1 85 ? 29.963 38.556 -9.834 1.00 22.54 ? 85 VAL A CB 1 ATOM 725 C CG1 . VAL A 1 85 ? 28.824 37.693 -10.407 1.00 17.17 ? 85 VAL A CG1 1 ATOM 726 C CG2 . VAL A 1 85 ? 30.905 39.020 -10.953 1.00 16.23 ? 85 VAL A CG2 1 ATOM 727 N N . PRO A 1 86 ? 27.355 39.816 -7.683 1.00 20.05 ? 86 PRO A N 1 ATOM 728 C CA . PRO A 1 86 ? 26.508 39.479 -6.535 1.00 18.55 ? 86 PRO A CA 1 ATOM 729 C C . PRO A 1 86 ? 26.063 38.024 -6.574 1.00 17.65 ? 86 PRO A C 1 ATOM 730 O O . PRO A 1 86 ? 25.931 37.472 -7.663 1.00 15.45 ? 86 PRO A O 1 ATOM 731 C CB . PRO A 1 86 ? 25.284 40.394 -6.728 1.00 19.25 ? 86 PRO A CB 1 ATOM 732 C CG . PRO A 1 86 ? 25.221 40.620 -8.203 1.00 23.01 ? 86 PRO A CG 1 ATOM 733 C CD . PRO A 1 86 ? 26.673 40.732 -8.617 1.00 24.34 ? 86 PRO A CD 1 ATOM 734 N N . PRO A 1 87 ? 25.818 37.413 -5.405 1.00 21.22 ? 87 PRO A N 1 ATOM 735 C CA . PRO A 1 87 ? 25.435 35.995 -5.368 1.00 16.42 ? 87 PRO A CA 1 ATOM 736 C C . PRO A 1 87 ? 23.972 35.711 -5.663 1.00 17.77 ? 87 PRO A C 1 ATOM 737 O O . PRO A 1 87 ? 23.106 36.567 -5.486 1.00 17.60 ? 87 PRO A O 1 ATOM 738 C CB . PRO A 1 87 ? 25.692 35.603 -3.919 1.00 15.32 ? 87 PRO A CB 1 ATOM 739 C CG . PRO A 1 87 ? 25.465 36.893 -3.147 1.00 16.92 ? 87 PRO A CG 1 ATOM 740 C CD . PRO A 1 87 ? 25.951 37.996 -4.055 1.00 13.55 ? 87 PRO A CD 1 ATOM 741 N N . GLU A 1 88 ? 23.724 34.481 -6.088 1.00 19.92 ? 88 GLU A N 1 ATOM 742 C CA . GLU A 1 88 ? 22.394 33.895 -6.095 1.00 16.94 ? 88 GLU A CA 1 ATOM 743 C C . GLU A 1 88 ? 22.297 33.171 -4.777 1.00 18.71 ? 88 GLU A C 1 ATOM 744 O O . GLU A 1 88 ? 23.246 32.531 -4.351 1.00 20.35 ? 88 GLU A O 1 ATOM 745 C CB . GLU A 1 88 ? 22.284 32.871 -7.217 1.00 17.60 ? 88 GLU A CB 1 ATOM 746 C CG . GLU A 1 88 ? 22.364 33.451 -8.608 1.00 36.71 ? 88 GLU A CG 1 ATOM 747 C CD . GLU A 1 88 ? 22.092 32.401 -9.684 1.00 48.13 ? 88 GLU A CD 1 ATOM 748 O OE1 . GLU A 1 88 ? 21.854 31.222 -9.331 1.00 48.49 ? 88 GLU A OE1 1 ATOM 749 O OE2 . GLU A 1 88 ? 22.120 32.757 -10.881 1.00 49.50 ? 88 GLU A OE2 1 ATOM 750 N N . VAL A 1 89 ? 21.167 33.279 -4.103 1.00 15.22 ? 89 VAL A N 1 ATOM 751 C CA . VAL A 1 89 ? 21.046 32.616 -2.817 1.00 16.88 ? 89 VAL A CA 1 ATOM 752 C C . VAL A 1 89 ? 19.818 31.719 -2.791 1.00 18.01 ? 89 VAL A C 1 ATOM 753 O O . VAL A 1 89 ? 18.735 32.128 -3.206 1.00 17.39 ? 89 VAL A O 1 ATOM 754 C CB . VAL A 1 89 ? 20.996 33.638 -1.673 1.00 15.11 ? 89 VAL A CB 1 ATOM 755 C CG1 . VAL A 1 89 ? 20.709 32.943 -0.321 1.00 18.33 ? 89 VAL A CG1 1 ATOM 756 C CG2 . VAL A 1 89 ? 22.319 34.418 -1.617 1.00 15.41 ? 89 VAL A CG2 1 ATOM 757 N N . THR A 1 90 ? 19.993 30.486 -2.334 1.00 18.00 ? 90 THR A N 1 ATOM 758 C CA A THR A 1 90 ? 18.880 29.545 -2.194 0.61 18.67 ? 90 THR A CA 1 ATOM 759 C CA B THR A 1 90 ? 18.858 29.588 -2.170 0.39 18.66 ? 90 THR A CA 1 ATOM 760 C C . THR A 1 90 ? 18.861 28.971 -0.785 1.00 17.52 ? 90 THR A C 1 ATOM 761 O O . THR A 1 90 ? 19.914 28.620 -0.250 1.00 19.80 ? 90 THR A O 1 ATOM 762 C CB A THR A 1 90 ? 19.021 28.377 -3.186 0.61 16.38 ? 90 THR A CB 1 ATOM 763 C CB B THR A 1 90 ? 18.851 28.473 -3.223 0.39 17.27 ? 90 THR A CB 1 ATOM 764 O OG1 A THR A 1 90 ? 19.341 28.891 -4.481 0.61 16.25 ? 90 THR A OG1 1 ATOM 765 O OG1 B THR A 1 90 ? 20.170 27.931 -3.348 0.39 19.19 ? 90 THR A OG1 1 ATOM 766 C CG2 A THR A 1 90 ? 17.733 27.558 -3.265 0.61 18.09 ? 90 THR A CG2 1 ATOM 767 C CG2 B THR A 1 90 ? 18.403 29.021 -4.563 0.39 16.81 ? 90 THR A CG2 1 ATOM 768 N N . VAL A 1 91 ? 17.670 28.872 -0.194 1.00 17.10 ? 91 VAL A N 1 ATOM 769 C CA . VAL A 1 91 ? 17.505 28.217 1.098 1.00 17.38 ? 91 VAL A CA 1 ATOM 770 C C . VAL A 1 91 ? 16.694 26.945 0.885 1.00 27.61 ? 91 VAL A C 1 ATOM 771 O O . VAL A 1 91 ? 15.653 26.961 0.233 1.00 24.42 ? 91 VAL A O 1 ATOM 772 C CB . VAL A 1 91 ? 16.813 29.130 2.133 1.00 20.46 ? 91 VAL A CB 1 ATOM 773 C CG1 . VAL A 1 91 ? 16.399 28.329 3.373 1.00 22.37 ? 91 VAL A CG1 1 ATOM 774 C CG2 . VAL A 1 91 ? 17.735 30.257 2.520 1.00 17.52 ? 91 VAL A CG2 1 ATOM 775 N N . LEU A 1 92 ? 17.205 25.831 1.389 1.00 25.48 ? 92 LEU A N 1 ATOM 776 C CA . LEU A 1 92 ? 16.500 24.559 1.291 1.00 27.98 ? 92 LEU A CA 1 ATOM 777 C C . LEU A 1 92 ? 16.785 23.730 2.536 1.00 25.75 ? 92 LEU A C 1 ATOM 778 O O . LEU A 1 92 ? 17.611 24.117 3.363 1.00 23.53 ? 92 LEU A O 1 ATOM 779 C CB . LEU A 1 92 ? 16.868 23.806 -0.001 1.00 25.48 ? 92 LEU A CB 1 ATOM 780 C CG . LEU A 1 92 ? 18.290 23.372 -0.420 1.00 36.88 ? 92 LEU A CG 1 ATOM 781 C CD1 . LEU A 1 92 ? 19.329 24.518 -0.485 1.00 31.70 ? 92 LEU A CD1 1 ATOM 782 C CD2 . LEU A 1 92 ? 18.812 22.233 0.433 1.00 46.24 ? 92 LEU A CD2 1 ATOM 783 N N . THR A 1 93 ? 16.084 22.612 2.692 1.00 26.90 ? 93 THR A N 1 ATOM 784 C CA . THR A 1 93 ? 16.398 21.704 3.793 1.00 27.93 ? 93 THR A CA 1 ATOM 785 C C . THR A 1 93 ? 17.145 20.467 3.317 1.00 29.98 ? 93 THR A C 1 ATOM 786 O O . THR A 1 93 ? 17.069 20.088 2.146 1.00 23.34 ? 93 THR A O 1 ATOM 787 C CB . THR A 1 93 ? 15.150 21.260 4.577 1.00 23.69 ? 93 THR A CB 1 ATOM 788 O OG1 . THR A 1 93 ? 14.249 20.548 3.718 1.00 23.39 ? 93 THR A OG1 1 ATOM 789 C CG2 . THR A 1 93 ? 14.445 22.465 5.179 1.00 29.02 ? 93 THR A CG2 1 ATOM 790 N N . ASN A 1 94 ? 17.863 19.855 4.255 1.00 29.55 ? 94 ASN A N 1 ATOM 791 C CA . ASN A 1 94 ? 18.606 18.624 4.048 1.00 26.11 ? 94 ASN A CA 1 ATOM 792 C C . ASN A 1 94 ? 17.691 17.471 3.642 1.00 27.98 ? 94 ASN A C 1 ATOM 793 O O . ASN A 1 94 ? 18.066 16.618 2.847 1.00 23.68 ? 94 ASN A O 1 ATOM 794 C CB . ASN A 1 94 ? 19.303 18.266 5.358 1.00 33.41 ? 94 ASN A CB 1 ATOM 795 C CG . ASN A 1 94 ? 20.334 17.185 5.195 1.00 46.91 ? 94 ASN A CG 1 ATOM 796 O OD1 . ASN A 1 94 ? 20.632 16.754 4.082 1.00 53.97 ? 94 ASN A OD1 1 ATOM 797 N ND2 . ASN A 1 94 ? 20.906 16.750 6.312 1.00 56.41 ? 94 ASN A ND2 1 ATOM 798 N N . SER A 1 95 ? 16.496 17.429 4.219 1.00 22.48 ? 95 SER A N 1 ATOM 799 C CA . SER A 1 95 ? 15.571 16.347 3.924 1.00 31.09 ? 95 SER A CA 1 ATOM 800 C C . SER A 1 95 ? 14.133 16.843 4.067 1.00 33.05 ? 95 SER A C 1 ATOM 801 O O . SER A 1 95 ? 13.909 17.930 4.608 1.00 28.70 ? 95 SER A O 1 ATOM 802 C CB . SER A 1 95 ? 15.846 15.153 4.851 1.00 37.12 ? 95 SER A CB 1 ATOM 803 O OG . SER A 1 95 ? 15.449 15.429 6.178 1.00 41.93 ? 95 SER A OG 1 ATOM 804 N N . PRO A 1 96 ? 13.156 16.065 3.558 1.00 34.81 ? 96 PRO A N 1 ATOM 805 C CA . PRO A 1 96 ? 11.759 16.488 3.663 1.00 37.06 ? 96 PRO A CA 1 ATOM 806 C C . PRO A 1 96 ? 11.374 16.804 5.106 1.00 34.44 ? 96 PRO A C 1 ATOM 807 O O . PRO A 1 96 ? 11.721 16.071 6.036 1.00 29.61 ? 96 PRO A O 1 ATOM 808 C CB . PRO A 1 96 ? 10.978 15.273 3.140 1.00 38.37 ? 96 PRO A CB 1 ATOM 809 C CG . PRO A 1 96 ? 11.987 14.161 3.006 1.00 39.24 ? 96 PRO A CG 1 ATOM 810 C CD . PRO A 1 96 ? 13.279 14.826 2.770 1.00 36.92 ? 96 PRO A CD 1 ATOM 811 N N . VAL A 1 97 ? 10.671 17.913 5.278 1.00 28.95 ? 97 VAL A N 1 ATOM 812 C CA . VAL A 1 97 ? 10.407 18.445 6.603 1.00 32.29 ? 97 VAL A CA 1 ATOM 813 C C . VAL A 1 97 ? 9.194 17.789 7.241 1.00 31.15 ? 97 VAL A C 1 ATOM 814 O O . VAL A 1 97 ? 8.144 17.655 6.615 1.00 34.80 ? 97 VAL A O 1 ATOM 815 C CB . VAL A 1 97 ? 10.200 19.963 6.541 1.00 35.61 ? 97 VAL A CB 1 ATOM 816 C CG1 . VAL A 1 97 ? 9.844 20.516 7.905 1.00 34.31 ? 97 VAL A CG1 1 ATOM 817 C CG2 . VAL A 1 97 ? 11.451 20.629 5.993 1.00 36.04 ? 97 VAL A CG2 1 ATOM 818 N N . GLU A 1 98 ? 9.364 17.359 8.484 1.00 32.53 ? 98 GLU A N 1 ATOM 819 C CA . GLU A 1 98 ? 8.256 16.875 9.289 1.00 37.89 ? 98 GLU A CA 1 ATOM 820 C C . GLU A 1 98 ? 8.289 17.558 10.647 1.00 38.95 ? 98 GLU A C 1 ATOM 821 O O . GLU A 1 98 ? 9.366 17.788 11.200 1.00 33.97 ? 98 GLU A O 1 ATOM 822 C CB . GLU A 1 98 ? 8.339 15.358 9.441 1.00 47.04 ? 98 GLU A CB 1 ATOM 823 C CG . GLU A 1 98 ? 8.173 14.626 8.125 1.00 56.82 ? 98 GLU A CG 1 ATOM 824 C CD . GLU A 1 98 ? 8.368 13.137 8.260 1.00 70.34 ? 98 GLU A CD 1 ATOM 825 O OE1 . GLU A 1 98 ? 9.344 12.722 8.924 1.00 72.84 ? 98 GLU A OE1 1 ATOM 826 O OE2 . GLU A 1 98 ? 7.541 12.384 7.704 1.00 78.83 ? 98 GLU A OE2 1 ATOM 827 N N . LEU A 1 99 ? 7.107 17.883 11.170 1.00 41.16 ? 99 LEU A N 1 ATOM 828 C CA . LEU A 1 99 ? 6.979 18.591 12.439 1.00 39.29 ? 99 LEU A CA 1 ATOM 829 C C . LEU A 1 99 ? 7.755 17.911 13.548 1.00 39.76 ? 99 LEU A C 1 ATOM 830 O O . LEU A 1 99 ? 7.623 16.701 13.758 1.00 39.99 ? 99 LEU A O 1 ATOM 831 C CB . LEU A 1 99 ? 5.506 18.720 12.850 1.00 38.22 ? 99 LEU A CB 1 ATOM 832 C CG . LEU A 1 99 ? 4.695 19.741 12.049 1.00 43.59 ? 99 LEU A CG 1 ATOM 833 C CD1 . LEU A 1 99 ? 3.269 19.833 12.576 1.00 44.12 ? 99 LEU A CD1 1 ATOM 834 C CD2 . LEU A 1 99 ? 5.383 21.115 12.061 1.00 45.68 ? 99 LEU A CD2 1 ATOM 835 N N . ARG A 1 100 ? 8.578 18.695 14.239 1.00 34.73 ? 100 ARG A N 1 ATOM 836 C CA . ARG A 1 100 ? 9.311 18.212 15.405 1.00 37.81 ? 100 ARG A CA 1 ATOM 837 C C . ARG A 1 100 ? 10.319 17.102 15.100 1.00 37.13 ? 100 ARG A C 1 ATOM 838 O O . ARG A 1 100 ? 10.747 16.387 16.004 1.00 39.84 ? 100 ARG A O 1 ATOM 839 C CB . ARG A 1 100 ? 8.344 17.778 16.513 1.00 41.24 ? 100 ARG A CB 1 ATOM 840 C CG . ARG A 1 100 ? 7.626 18.940 17.181 1.00 48.77 ? 100 ARG A CG 1 ATOM 841 C CD . ARG A 1 100 ? 6.622 18.452 18.216 1.00 58.62 ? 100 ARG A CD 1 ATOM 842 N NE . ARG A 1 100 ? 5.592 17.598 17.627 1.00 66.59 ? 100 ARG A NE 1 ATOM 843 C CZ . ARG A 1 100 ? 4.531 18.051 16.961 1.00 70.95 ? 100 ARG A CZ 1 ATOM 844 N NH1 . ARG A 1 100 ? 4.357 19.354 16.788 1.00 66.43 ? 100 ARG A NH1 1 ATOM 845 N NH2 . ARG A 1 100 ? 3.645 17.199 16.460 1.00 75.96 ? 100 ARG A NH2 1 ATOM 846 N N . GLU A 1 101 ? 10.689 16.957 13.828 1.00 35.18 ? 101 GLU A N 1 ATOM 847 C CA A GLU A 1 101 ? 11.744 16.029 13.455 0.57 33.20 ? 101 GLU A CA 1 ATOM 848 C CA B GLU A 1 101 ? 11.738 16.019 13.426 0.43 33.37 ? 101 GLU A CA 1 ATOM 849 C C . GLU A 1 101 ? 12.976 16.802 13.004 1.00 31.79 ? 101 GLU A C 1 ATOM 850 O O . GLU A 1 101 ? 12.928 17.536 12.013 1.00 28.79 ? 101 GLU A O 1 ATOM 851 C CB A GLU A 1 101 ? 11.276 15.060 12.369 0.57 33.68 ? 101 GLU A CB 1 ATOM 852 C CB B GLU A 1 101 ? 11.261 15.127 12.272 0.43 33.99 ? 101 GLU A CB 1 ATOM 853 C CG A GLU A 1 101 ? 10.288 14.012 12.854 0.57 34.73 ? 101 GLU A CG 1 ATOM 854 C CG B GLU A 1 101 ? 12.202 13.968 11.914 0.43 32.79 ? 101 GLU A CG 1 ATOM 855 C CD A GLU A 1 101 ? 10.944 12.909 13.669 0.57 37.99 ? 101 GLU A CD 1 ATOM 856 C CD B GLU A 1 101 ? 13.082 14.238 10.694 0.43 34.19 ? 101 GLU A CD 1 ATOM 857 O OE1 A GLU A 1 101 ? 12.160 12.986 13.941 0.57 39.08 ? 101 GLU A OE1 1 ATOM 858 O OE1 B GLU A 1 101 ? 12.545 14.547 9.604 0.43 30.71 ? 101 GLU A OE1 1 ATOM 859 O OE2 A GLU A 1 101 ? 10.233 11.956 14.037 0.57 46.92 ? 101 GLU A OE2 1 ATOM 860 O OE2 B GLU A 1 101 ? 14.320 14.120 10.826 0.43 30.62 ? 101 GLU A OE2 1 ATOM 861 N N . PRO A 1 102 ? 14.082 16.651 13.759 1.00 32.75 ? 102 PRO A N 1 ATOM 862 C CA . PRO A 1 102 ? 15.350 17.346 13.528 1.00 30.83 ? 102 PRO A CA 1 ATOM 863 C C . PRO A 1 102 ? 15.723 17.377 12.053 1.00 35.34 ? 102 PRO A C 1 ATOM 864 O O . PRO A 1 102 ? 15.711 16.351 11.371 1.00 28.39 ? 102 PRO A O 1 ATOM 865 C CB . PRO A 1 102 ? 16.351 16.501 14.310 1.00 34.84 ? 102 PRO A CB 1 ATOM 866 C CG . PRO A 1 102 ? 15.547 15.961 15.458 1.00 35.87 ? 102 PRO A CG 1 ATOM 867 C CD . PRO A 1 102 ? 14.159 15.741 14.921 1.00 38.67 ? 102 PRO A CD 1 ATOM 868 N N . ASN A 1 103 ? 16.038 18.569 11.565 1.00 25.64 ? 103 ASN A N 1 ATOM 869 C CA . ASN A 1 103 ? 16.365 18.759 10.166 1.00 24.39 ? 103 ASN A CA 1 ATOM 870 C C . ASN A 1 103 ? 17.445 19.831 10.098 1.00 25.62 ? 103 ASN A C 1 ATOM 871 O O . ASN A 1 103 ? 17.910 20.313 11.136 1.00 25.76 ? 103 ASN A O 1 ATOM 872 C CB . ASN A 1 103 ? 15.102 19.171 9.395 1.00 24.56 ? 103 ASN A CB 1 ATOM 873 C CG . ASN A 1 103 ? 15.134 18.767 7.931 1.00 24.19 ? 103 ASN A CG 1 ATOM 874 O OD1 . ASN A 1 103 ? 16.139 18.949 7.237 1.00 27.40 ? 103 ASN A OD1 1 ATOM 875 N ND2 . ASN A 1 103 ? 14.018 18.230 7.446 1.00 24.91 ? 103 ASN A ND2 1 ATOM 876 N N . VAL A 1 104 ? 17.865 20.188 8.888 1.00 24.48 ? 104 VAL A N 1 ATOM 877 C CA . VAL A 1 104 ? 18.918 21.180 8.706 1.00 23.75 ? 104 VAL A CA 1 ATOM 878 C C . VAL A 1 104 ? 18.564 22.131 7.564 1.00 21.39 ? 104 VAL A C 1 ATOM 879 O O . VAL A 1 104 ? 18.248 21.694 6.451 1.00 19.86 ? 104 VAL A O 1 ATOM 880 C CB . VAL A 1 104 ? 20.291 20.517 8.401 1.00 25.19 ? 104 VAL A CB 1 ATOM 881 C CG1 . VAL A 1 104 ? 21.380 21.583 8.237 1.00 20.65 ? 104 VAL A CG1 1 ATOM 882 C CG2 . VAL A 1 104 ? 20.670 19.512 9.493 1.00 25.39 ? 104 VAL A CG2 1 ATOM 883 N N . LEU A 1 105 ? 18.590 23.426 7.852 1.00 19.73 ? 105 LEU A N 1 ATOM 884 C CA . LEU A 1 105 ? 18.440 24.443 6.813 1.00 20.89 ? 105 LEU A CA 1 ATOM 885 C C . LEU A 1 105 ? 19.780 24.702 6.159 1.00 23.68 ? 105 LEU A C 1 ATOM 886 O O . LEU A 1 105 ? 20.787 24.860 6.850 1.00 17.60 ? 105 LEU A O 1 ATOM 887 C CB . LEU A 1 105 ? 17.915 25.743 7.417 1.00 21.80 ? 105 LEU A CB 1 ATOM 888 C CG . LEU A 1 105 ? 16.401 25.783 7.648 1.00 26.61 ? 105 LEU A CG 1 ATOM 889 C CD1 . LEU A 1 105 ? 16.034 26.922 8.569 1.00 28.39 ? 105 LEU A CD1 1 ATOM 890 C CD2 . LEU A 1 105 ? 15.678 25.932 6.325 1.00 26.97 ? 105 LEU A CD2 1 ATOM 891 N N . ILE A 1 106 ? 19.792 24.738 4.830 1.00 17.28 ? 106 ILE A N 1 ATOM 892 C CA . ILE A 1 106 ? 21.012 24.992 4.082 1.00 18.93 ? 106 ILE A CA 1 ATOM 893 C C . ILE A 1 106 ? 20.843 26.290 3.319 1.00 21.87 ? 106 ILE A C 1 ATOM 894 O O . ILE A 1 106 ? 19.853 26.467 2.587 1.00 21.12 ? 106 ILE A O 1 ATOM 895 C CB . ILE A 1 106 ? 21.314 23.866 3.059 1.00 18.66 ? 106 ILE A CB 1 ATOM 896 C CG1 . ILE A 1 106 ? 21.326 22.503 3.745 1.00 19.31 ? 106 ILE A CG1 1 ATOM 897 C CG2 . ILE A 1 106 ? 22.659 24.131 2.350 1.00 21.10 ? 106 ILE A CG2 1 ATOM 898 C CD1 . ILE A 1 106 ? 21.431 21.316 2.779 1.00 22.56 ? 106 ILE A CD1 1 ATOM 899 N N . CYS A 1 107 ? 21.793 27.202 3.502 1.00 15.23 ? 107 CYS A N 1 ATOM 900 C CA . CYS A 1 107 ? 21.827 28.429 2.718 1.00 16.42 ? 107 CYS A CA 1 ATOM 901 C C . CYS A 1 107 ? 22.946 28.298 1.704 1.00 19.69 ? 107 CYS A C 1 ATOM 902 O O . CYS A 1 107 ? 24.133 28.196 2.061 1.00 21.04 ? 107 CYS A O 1 ATOM 903 C CB . CYS A 1 107 ? 22.016 29.658 3.610 1.00 15.04 ? 107 CYS A CB 1 ATOM 904 S SG . CYS A 1 107 ? 21.938 31.233 2.706 1.00 20.81 ? 107 CYS A SG 1 ATOM 905 N N . PHE A 1 108 ? 22.559 28.240 0.437 1.00 17.65 ? 108 PHE A N 1 ATOM 906 C CA . PHE A 1 108 ? 23.522 28.045 -0.636 1.00 16.12 ? 108 PHE A CA 1 ATOM 907 C C . PHE A 1 108 ? 23.754 29.386 -1.309 1.00 18.71 ? 108 PHE A C 1 ATOM 908 O O . PHE A 1 108 ? 22.820 29.992 -1.833 1.00 20.51 ? 108 PHE A O 1 ATOM 909 C CB . PHE A 1 108 ? 22.999 27.039 -1.662 1.00 15.36 ? 108 PHE A CB 1 ATOM 910 C CG . PHE A 1 108 ? 23.976 26.757 -2.784 1.00 22.98 ? 108 PHE A CG 1 ATOM 911 C CD1 . PHE A 1 108 ? 25.335 26.600 -2.517 1.00 26.13 ? 108 PHE A CD1 1 ATOM 912 C CD2 . PHE A 1 108 ? 23.536 26.630 -4.094 1.00 21.17 ? 108 PHE A CD2 1 ATOM 913 C CE1 . PHE A 1 108 ? 26.232 26.325 -3.535 1.00 25.75 ? 108 PHE A CE1 1 ATOM 914 C CE2 . PHE A 1 108 ? 24.431 26.352 -5.118 1.00 25.84 ? 108 PHE A CE2 1 ATOM 915 C CZ . PHE A 1 108 ? 25.776 26.199 -4.837 1.00 20.85 ? 108 PHE A CZ 1 ATOM 916 N N . ILE A 1 109 ? 24.998 29.843 -1.291 1.00 14.67 ? 109 ILE A N 1 ATOM 917 C CA . ILE A 1 109 ? 25.347 31.151 -1.837 1.00 15.82 ? 109 ILE A CA 1 ATOM 918 C C . ILE A 1 109 ? 26.266 30.918 -3.031 1.00 20.37 ? 109 ILE A C 1 ATOM 919 O O . ILE A 1 109 ? 27.356 30.382 -2.868 1.00 15.75 ? 109 ILE A O 1 ATOM 920 C CB . ILE A 1 109 ? 26.055 31.973 -0.765 1.00 17.08 ? 109 ILE A CB 1 ATOM 921 C CG1 . ILE A 1 109 ? 25.146 32.092 0.453 1.00 18.57 ? 109 ILE A CG1 1 ATOM 922 C CG2 . ILE A 1 109 ? 26.444 33.352 -1.280 1.00 12.05 ? 109 ILE A CG2 1 ATOM 923 C CD1 . ILE A 1 109 ? 25.878 31.990 1.766 1.00 27.51 ? 109 ILE A CD1 1 ATOM 924 N N . ASP A 1 110 ? 25.825 31.308 -4.226 1.00 15.27 ? 110 ASP A N 1 ATOM 925 C CA . ASP A 1 110 ? 26.449 30.807 -5.450 1.00 15.31 ? 110 ASP A CA 1 ATOM 926 C C . ASP A 1 110 ? 26.798 31.934 -6.426 1.00 18.95 ? 110 ASP A C 1 ATOM 927 O O . ASP A 1 110 ? 26.170 32.995 -6.416 1.00 16.04 ? 110 ASP A O 1 ATOM 928 C CB . ASP A 1 110 ? 25.476 29.822 -6.110 1.00 12.41 ? 110 ASP A CB 1 ATOM 929 C CG . ASP A 1 110 ? 26.136 28.903 -7.107 1.00 21.91 ? 110 ASP A CG 1 ATOM 930 O OD1 . ASP A 1 110 ? 27.381 28.774 -7.101 1.00 19.69 ? 110 ASP A OD1 1 ATOM 931 O OD2 . ASP A 1 110 ? 25.388 28.284 -7.890 1.00 21.06 ? 110 ASP A OD2 1 ATOM 932 N N . LYS A 1 111 ? 27.806 31.679 -7.260 1.00 15.78 ? 111 LYS A N 1 ATOM 933 C CA . LYS A 1 111 ? 28.161 32.511 -8.417 1.00 19.05 ? 111 LYS A CA 1 ATOM 934 C C . LYS A 1 111 ? 28.494 33.955 -8.071 1.00 19.80 ? 111 LYS A C 1 ATOM 935 O O . LYS A 1 111 ? 27.945 34.895 -8.664 1.00 13.11 ? 111 LYS A O 1 ATOM 936 C CB . LYS A 1 111 ? 27.052 32.499 -9.485 1.00 26.10 ? 111 LYS A CB 1 ATOM 937 C CG . LYS A 1 111 ? 26.413 31.150 -9.753 1.00 34.40 ? 111 LYS A CG 1 ATOM 938 C CD . LYS A 1 111 ? 25.473 31.237 -10.958 1.00 41.77 ? 111 LYS A CD 1 ATOM 939 C CE . LYS A 1 111 ? 24.419 30.129 -10.957 1.00 44.76 ? 111 LYS A CE 1 ATOM 940 N NZ . LYS A 1 111 ? 25.002 28.769 -11.081 1.00 53.54 ? 111 LYS A NZ 1 ATOM 941 N N . PHE A 1 112 ? 29.416 34.138 -7.138 1.00 13.62 ? 112 PHE A N 1 ATOM 942 C CA . PHE A 1 112 ? 29.755 35.479 -6.718 1.00 13.74 ? 112 PHE A CA 1 ATOM 943 C C . PHE A 1 112 ? 31.262 35.673 -6.617 1.00 18.48 ? 112 PHE A C 1 ATOM 944 O O . PHE A 1 112 ? 32.033 34.700 -6.516 1.00 15.19 ? 112 PHE A O 1 ATOM 945 C CB . PHE A 1 112 ? 29.084 35.795 -5.388 1.00 13.50 ? 112 PHE A CB 1 ATOM 946 C CG . PHE A 1 112 ? 29.593 34.973 -4.246 1.00 18.30 ? 112 PHE A CG 1 ATOM 947 C CD1 . PHE A 1 112 ? 30.609 35.455 -3.419 1.00 16.19 ? 112 PHE A CD1 1 ATOM 948 C CD2 . PHE A 1 112 ? 29.060 33.717 -3.995 1.00 12.91 ? 112 PHE A CD2 1 ATOM 949 C CE1 . PHE A 1 112 ? 31.080 34.687 -2.367 1.00 18.89 ? 112 PHE A CE1 1 ATOM 950 C CE2 . PHE A 1 112 ? 29.528 32.946 -2.948 1.00 18.79 ? 112 PHE A CE2 1 ATOM 951 C CZ . PHE A 1 112 ? 30.542 33.426 -2.136 1.00 15.03 ? 112 PHE A CZ 1 ATOM 952 N N . THR A 1 113 ? 31.671 36.937 -6.663 1.00 17.96 ? 113 THR A N 1 ATOM 953 C CA . THR A 1 113 ? 33.061 37.314 -6.410 1.00 15.05 ? 113 THR A CA 1 ATOM 954 C C . THR A 1 113 ? 33.022 38.807 -6.119 1.00 16.19 ? 113 THR A C 1 ATOM 955 O O . THR A 1 113 ? 32.120 39.498 -6.598 1.00 16.66 ? 113 THR A O 1 ATOM 956 C CB . THR A 1 113 ? 33.982 36.985 -7.610 1.00 15.15 ? 113 THR A CB 1 ATOM 957 O OG1 . THR A 1 113 ? 35.341 36.842 -7.158 1.00 15.98 ? 113 THR A OG1 1 ATOM 958 C CG2 . THR A 1 113 ? 33.880 38.084 -8.716 1.00 14.82 ? 113 THR A CG2 1 ATOM 959 N N . PRO A 1 114 ? 33.963 39.313 -5.298 1.00 18.30 ? 114 PRO A N 1 ATOM 960 C CA . PRO A 1 114 ? 35.069 38.618 -4.621 1.00 12.01 ? 114 PRO A CA 1 ATOM 961 C C . PRO A 1 114 ? 34.600 37.667 -3.515 1.00 13.93 ? 114 PRO A C 1 ATOM 962 O O . PRO A 1 114 ? 33.440 37.766 -3.078 1.00 17.43 ? 114 PRO A O 1 ATOM 963 C CB . PRO A 1 114 ? 35.906 39.776 -4.036 1.00 15.81 ? 114 PRO A CB 1 ATOM 964 C CG . PRO A 1 114 ? 34.956 40.894 -3.897 1.00 16.01 ? 114 PRO A CG 1 ATOM 965 C CD . PRO A 1 114 ? 33.997 40.767 -5.057 1.00 14.90 ? 114 PRO A CD 1 ATOM 966 N N . PRO A 1 115 ? 35.480 36.745 -3.076 1.00 15.67 ? 115 PRO A N 1 ATOM 967 C CA . PRO A 1 115 ? 35.128 35.788 -2.020 1.00 18.06 ? 115 PRO A CA 1 ATOM 968 C C . PRO A 1 115 ? 35.054 36.442 -0.639 1.00 18.93 ? 115 PRO A C 1 ATOM 969 O O . PRO A 1 115 ? 35.901 36.161 0.226 1.00 16.91 ? 115 PRO A O 1 ATOM 970 C CB . PRO A 1 115 ? 36.281 34.771 -2.078 1.00 13.40 ? 115 PRO A CB 1 ATOM 971 C CG . PRO A 1 115 ? 37.462 35.594 -2.611 1.00 13.32 ? 115 PRO A CG 1 ATOM 972 C CD . PRO A 1 115 ? 36.823 36.482 -3.639 1.00 19.18 ? 115 PRO A CD 1 ATOM 973 N N . VAL A 1 116 ? 34.076 37.332 -0.453 1.00 17.95 ? 116 VAL A N 1 ATOM 974 C CA . VAL A 1 116 ? 33.800 37.981 0.838 1.00 15.22 ? 116 VAL A CA 1 ATOM 975 C C . VAL A 1 116 ? 32.290 38.163 0.972 1.00 21.41 ? 116 VAL A C 1 ATOM 976 O O . VAL A 1 116 ? 31.663 38.756 0.091 1.00 17.60 ? 116 VAL A O 1 ATOM 977 C CB . VAL A 1 116 ? 34.459 39.376 0.962 1.00 22.12 ? 116 VAL A CB 1 ATOM 978 C CG1 . VAL A 1 116 ? 34.245 39.955 2.367 1.00 21.09 ? 116 VAL A CG1 1 ATOM 979 C CG2 . VAL A 1 116 ? 35.950 39.316 0.636 1.00 16.64 ? 116 VAL A CG2 1 ATOM 980 N N . VAL A 1 117 ? 31.707 37.633 2.052 1.00 20.69 ? 117 VAL A N 1 ATOM 981 C CA . VAL A 1 117 ? 30.262 37.765 2.327 1.00 16.63 ? 117 VAL A CA 1 ATOM 982 C C . VAL A 1 117 ? 30.023 37.834 3.824 1.00 21.37 ? 117 VAL A C 1 ATOM 983 O O . VAL A 1 117 ? 30.821 37.321 4.621 1.00 26.15 ? 117 VAL A O 1 ATOM 984 C CB . VAL A 1 117 ? 29.417 36.556 1.810 1.00 24.35 ? 117 VAL A CB 1 ATOM 985 C CG1 . VAL A 1 117 ? 29.322 36.540 0.307 1.00 27.53 ? 117 VAL A CG1 1 ATOM 986 C CG2 . VAL A 1 117 ? 29.967 35.225 2.352 1.00 24.54 ? 117 VAL A CG2 1 ATOM 987 N N . ASN A 1 118 ? 28.931 38.482 4.214 1.00 21.53 ? 118 ASN A N 1 ATOM 988 C CA . ASN A 1 118 ? 28.440 38.395 5.591 1.00 21.58 ? 118 ASN A CA 1 ATOM 989 C C . ASN A 1 118 ? 27.128 37.631 5.520 1.00 22.17 ? 118 ASN A C 1 ATOM 990 O O . ASN A 1 118 ? 26.209 38.027 4.792 1.00 21.20 ? 118 ASN A O 1 ATOM 991 C CB . ASN A 1 118 ? 28.186 39.773 6.195 1.00 23.94 ? 118 ASN A CB 1 ATOM 992 C CG . ASN A 1 118 ? 29.463 40.582 6.396 1.00 33.59 ? 118 ASN A CG 1 ATOM 993 O OD1 . ASN A 1 118 ? 30.532 40.024 6.627 1.00 32.94 ? 118 ASN A OD1 1 ATOM 994 N ND2 . ASN A 1 118 ? 29.343 41.910 6.311 1.00 38.91 ? 118 ASN A ND2 1 ATOM 995 N N . VAL A 1 119 ? 27.043 36.531 6.252 1.00 21.71 ? 119 VAL A N 1 ATOM 996 C CA . VAL A 1 119 ? 25.858 35.684 6.204 1.00 23.26 ? 119 VAL A CA 1 ATOM 997 C C . VAL A 1 119 ? 25.303 35.553 7.600 1.00 27.04 ? 119 VAL A C 1 ATOM 998 O O . VAL A 1 119 ? 26.046 35.255 8.537 1.00 23.39 ? 119 VAL A O 1 ATOM 999 C CB . VAL A 1 119 ? 26.176 34.271 5.686 1.00 25.77 ? 119 VAL A CB 1 ATOM 1000 C CG1 . VAL A 1 119 ? 24.919 33.400 5.713 1.00 20.12 ? 119 VAL A CG1 1 ATOM 1001 C CG2 . VAL A 1 119 ? 26.771 34.336 4.285 1.00 21.09 ? 119 VAL A CG2 1 ATOM 1002 N N . THR A 1 120 ? 24.001 35.790 7.741 1.00 22.94 ? 120 THR A N 1 ATOM 1003 C CA . THR A 1 120 ? 23.341 35.641 9.029 1.00 20.36 ? 120 THR A CA 1 ATOM 1004 C C . THR A 1 120 ? 22.065 34.817 8.901 1.00 19.25 ? 120 THR A C 1 ATOM 1005 O O . THR A 1 120 ? 21.257 35.050 8.002 1.00 22.39 ? 120 THR A O 1 ATOM 1006 C CB . THR A 1 120 ? 22.928 37.001 9.618 1.00 21.61 ? 120 THR A CB 1 ATOM 1007 O OG1 . THR A 1 120 ? 24.000 37.936 9.492 1.00 24.35 ? 120 THR A OG1 1 ATOM 1008 C CG2 . THR A 1 120 ? 22.548 36.839 11.097 1.00 19.14 ? 120 THR A CG2 1 ATOM 1009 N N . TRP A 1 121 ? 21.887 33.872 9.816 1.00 22.37 ? 121 TRP A N 1 ATOM 1010 C CA . TRP A 1 121 ? 20.637 33.149 9.944 1.00 21.74 ? 121 TRP A CA 1 ATOM 1011 C C . TRP A 1 121 ? 19.713 33.940 10.853 1.00 25.43 ? 121 TRP A C 1 ATOM 1012 O O . TRP A 1 121 ? 20.131 34.375 11.923 1.00 24.94 ? 121 TRP A O 1 ATOM 1013 C CB . TRP A 1 121 ? 20.886 31.785 10.580 1.00 22.74 ? 121 TRP A CB 1 ATOM 1014 C CG . TRP A 1 121 ? 21.428 30.758 9.652 1.00 20.51 ? 121 TRP A CG 1 ATOM 1015 C CD1 . TRP A 1 121 ? 22.678 30.217 9.668 1.00 20.85 ? 121 TRP A CD1 1 ATOM 1016 C CD2 . TRP A 1 121 ? 20.729 30.132 8.571 1.00 20.02 ? 121 TRP A CD2 1 ATOM 1017 N NE1 . TRP A 1 121 ? 22.803 29.279 8.662 1.00 20.18 ? 121 TRP A NE1 1 ATOM 1018 C CE2 . TRP A 1 121 ? 21.619 29.209 7.976 1.00 23.37 ? 121 TRP A CE2 1 ATOM 1019 C CE3 . TRP A 1 121 ? 19.433 30.252 8.058 1.00 21.25 ? 121 TRP A CE3 1 ATOM 1020 C CZ2 . TRP A 1 121 ? 21.252 28.410 6.892 1.00 20.33 ? 121 TRP A CZ2 1 ATOM 1021 C CZ3 . TRP A 1 121 ? 19.068 29.460 6.976 1.00 20.51 ? 121 TRP A CZ3 1 ATOM 1022 C CH2 . TRP A 1 121 ? 19.970 28.553 6.406 1.00 20.09 ? 121 TRP A CH2 1 ATOM 1023 N N . LEU A 1 122 ? 18.466 34.127 10.431 1.00 21.51 ? 122 LEU A N 1 ATOM 1024 C CA . LEU A 1 122 ? 17.468 34.807 11.249 1.00 25.50 ? 122 LEU A CA 1 ATOM 1025 C C . LEU A 1 122 ? 16.327 33.849 11.530 1.00 26.04 ? 122 LEU A C 1 ATOM 1026 O O . LEU A 1 122 ? 15.838 33.172 10.614 1.00 26.98 ? 122 LEU A O 1 ATOM 1027 C CB . LEU A 1 122 ? 16.917 36.033 10.519 1.00 25.51 ? 122 LEU A CB 1 ATOM 1028 C CG . LEU A 1 122 ? 17.907 37.117 10.104 1.00 23.50 ? 122 LEU A CG 1 ATOM 1029 C CD1 . LEU A 1 122 ? 17.260 38.088 9.117 1.00 23.23 ? 122 LEU A CD1 1 ATOM 1030 C CD2 . LEU A 1 122 ? 18.442 37.867 11.320 1.00 25.15 ? 122 LEU A CD2 1 ATOM 1031 N N . ARG A 1 123 ? 15.928 33.769 12.797 1.00 22.38 ? 123 ARG A N 1 ATOM 1032 C CA . ARG A 1 123 ? 14.734 33.042 13.201 1.00 25.93 ? 123 ARG A CA 1 ATOM 1033 C C . ARG A 1 123 ? 13.754 34.061 13.769 1.00 25.54 ? 123 ARG A C 1 ATOM 1034 O O . ARG A 1 123 ? 14.069 34.751 14.731 1.00 21.14 ? 123 ARG A O 1 ATOM 1035 C CB . ARG A 1 123 ? 15.062 31.969 14.252 1.00 23.10 ? 123 ARG A CB 1 ATOM 1036 C CG . ARG A 1 123 ? 13.826 31.423 14.996 1.00 30.89 ? 123 ARG A CG 1 ATOM 1037 C CD . ARG A 1 123 ? 14.099 30.129 15.787 1.00 32.41 ? 123 ARG A CD 1 ATOM 1038 N NE . ARG A 1 123 ? 15.436 30.085 16.371 1.00 50.72 ? 123 ARG A NE 1 ATOM 1039 C CZ . ARG A 1 123 ? 16.285 29.065 16.239 1.00 62.88 ? 123 ARG A CZ 1 ATOM 1040 N NH1 . ARG A 1 123 ? 17.486 29.122 16.801 1.00 64.55 ? 123 ARG A NH1 1 ATOM 1041 N NH2 . ARG A 1 123 ? 15.938 27.983 15.549 1.00 66.06 ? 123 ARG A NH2 1 ATOM 1042 N N . ASN A 1 124 ? 12.573 34.155 13.169 1.00 23.25 ? 124 ASN A N 1 ATOM 1043 C CA . ASN A 1 124 ? 11.599 35.177 13.551 1.00 24.04 ? 124 ASN A CA 1 ATOM 1044 C C . ASN A 1 124 ? 12.218 36.589 13.546 1.00 25.40 ? 124 ASN A C 1 ATOM 1045 O O . ASN A 1 124 ? 11.911 37.420 14.391 1.00 22.76 ? 124 ASN A O 1 ATOM 1046 C CB . ASN A 1 124 ? 10.960 34.829 14.906 1.00 30.11 ? 124 ASN A CB 1 ATOM 1047 C CG . ASN A 1 124 ? 10.359 33.427 14.916 1.00 29.10 ? 124 ASN A CG 1 ATOM 1048 O OD1 . ASN A 1 124 ? 9.851 32.964 13.894 1.00 28.90 ? 124 ASN A OD1 1 ATOM 1049 N ND2 . ASN A 1 124 ? 10.426 32.742 16.064 1.00 27.63 ? 124 ASN A ND2 1 ATOM 1050 N N . GLY A 1 125 ? 13.096 36.844 12.582 1.00 19.66 ? 125 GLY A N 1 ATOM 1051 C CA . GLY A 1 125 ? 13.706 38.157 12.434 1.00 26.70 ? 125 GLY A CA 1 ATOM 1052 C C . GLY A 1 125 ? 14.864 38.467 13.368 1.00 25.75 ? 125 GLY A C 1 ATOM 1053 O O . GLY A 1 125 ? 15.351 39.597 13.379 1.00 26.78 ? 125 GLY A O 1 ATOM 1054 N N . LYS A 1 126 ? 15.308 37.472 14.139 1.00 25.03 ? 126 LYS A N 1 ATOM 1055 C CA . LYS A 1 126 ? 16.405 37.638 15.104 1.00 21.22 ? 126 LYS A CA 1 ATOM 1056 C C . LYS A 1 126 ? 17.579 36.733 14.740 1.00 21.00 ? 126 LYS A C 1 ATOM 1057 O O . LYS A 1 126 ? 17.380 35.563 14.400 1.00 25.42 ? 126 LYS A O 1 ATOM 1058 C CB . LYS A 1 126 ? 15.937 37.315 16.537 1.00 23.04 ? 126 LYS A CB 1 ATOM 1059 C CG . LYS A 1 126 ? 14.722 38.117 17.043 1.00 23.46 ? 126 LYS A CG 1 ATOM 1060 C CD . LYS A 1 126 ? 14.434 37.810 18.512 1.00 28.32 ? 126 LYS A CD 1 ATOM 1061 C CE . LYS A 1 126 ? 13.366 38.729 19.101 1.00 39.42 ? 126 LYS A CE 1 ATOM 1062 N NZ . LYS A 1 126 ? 13.209 38.527 20.581 1.00 39.73 ? 126 LYS A NZ 1 ATOM 1063 N N . PRO A 1 127 ? 18.814 37.270 14.799 1.00 30.69 ? 127 PRO A N 1 ATOM 1064 C CA . PRO A 1 127 ? 20.001 36.480 14.448 1.00 25.36 ? 127 PRO A CA 1 ATOM 1065 C C . PRO A 1 127 ? 20.121 35.238 15.332 1.00 25.50 ? 127 PRO A C 1 ATOM 1066 O O . PRO A 1 127 ? 19.834 35.299 16.522 1.00 23.96 ? 127 PRO A O 1 ATOM 1067 C CB . PRO A 1 127 ? 21.164 37.438 14.735 1.00 30.82 ? 127 PRO A CB 1 ATOM 1068 C CG . PRO A 1 127 ? 20.568 38.800 14.694 1.00 34.82 ? 127 PRO A CG 1 ATOM 1069 C CD . PRO A 1 127 ? 19.162 38.642 15.208 1.00 37.04 ? 127 PRO A CD 1 ATOM 1070 N N . VAL A 1 128 ? 20.512 34.111 14.750 1.00 26.44 ? 128 VAL A N 1 ATOM 1071 C CA . VAL A 1 128 ? 20.740 32.903 15.537 1.00 33.27 ? 128 VAL A CA 1 ATOM 1072 C C . VAL A 1 128 ? 22.104 32.311 15.209 1.00 35.76 ? 128 VAL A C 1 ATOM 1073 O O . VAL A 1 128 ? 22.545 32.358 14.060 1.00 37.28 ? 128 VAL A O 1 ATOM 1074 C CB . VAL A 1 128 ? 19.622 31.858 15.334 1.00 40.05 ? 128 VAL A CB 1 ATOM 1075 C CG1 . VAL A 1 128 ? 18.321 32.355 15.941 1.00 50.30 ? 128 VAL A CG1 1 ATOM 1076 C CG2 . VAL A 1 128 ? 19.428 31.544 13.871 1.00 32.90 ? 128 VAL A CG2 1 ATOM 1077 N N . THR A 1 129 ? 22.779 31.770 16.220 1.00 39.13 ? 129 THR A N 1 ATOM 1078 C CA . THR A 1 129 ? 24.152 31.292 16.046 1.00 45.59 ? 129 THR A CA 1 ATOM 1079 C C . THR A 1 129 ? 24.397 29.902 16.620 1.00 49.28 ? 129 THR A C 1 ATOM 1080 O O . THR A 1 129 ? 25.386 29.252 16.292 1.00 51.42 ? 129 THR A O 1 ATOM 1081 C CB . THR A 1 129 ? 25.170 32.251 16.692 1.00 44.07 ? 129 THR A CB 1 ATOM 1082 O OG1 . THR A 1 129 ? 24.805 32.483 18.058 1.00 46.89 ? 129 THR A OG1 1 ATOM 1083 C CG2 . THR A 1 129 ? 25.206 33.572 15.945 1.00 42.59 ? 129 THR A CG2 1 ATOM 1084 N N . THR A 1 130 ? 23.506 29.447 17.488 1.00 53.87 ? 130 THR A N 1 ATOM 1085 C CA . THR A 1 130 ? 23.684 28.145 18.110 1.00 53.87 ? 130 THR A CA 1 ATOM 1086 C C . THR A 1 130 ? 23.546 27.030 17.082 1.00 47.74 ? 130 THR A C 1 ATOM 1087 O O . THR A 1 130 ? 22.505 26.885 16.439 1.00 50.07 ? 130 THR A O 1 ATOM 1088 C CB . THR A 1 130 ? 22.674 27.917 19.240 1.00 57.46 ? 130 THR A CB 1 ATOM 1089 O OG1 . THR A 1 130 ? 21.349 27.910 18.692 1.00 63.53 ? 130 THR A OG1 1 ATOM 1090 C CG2 . THR A 1 130 ? 22.790 29.020 20.289 1.00 51.20 ? 130 THR A CG2 1 ATOM 1091 N N . GLY A 1 131 ? 24.610 26.252 16.927 1.00 41.43 ? 131 GLY A N 1 ATOM 1092 C CA . GLY A 1 131 ? 24.582 25.080 16.076 1.00 39.07 ? 131 GLY A CA 1 ATOM 1093 C C . GLY A 1 131 ? 24.985 25.362 14.646 1.00 37.18 ? 131 GLY A C 1 ATOM 1094 O O . GLY A 1 131 ? 25.180 24.431 13.864 1.00 43.14 ? 131 GLY A O 1 ATOM 1095 N N . VAL A 1 132 ? 25.126 26.636 14.296 1.00 26.92 ? 132 VAL A N 1 ATOM 1096 C CA . VAL A 1 132 ? 25.436 26.975 12.910 1.00 23.98 ? 132 VAL A CA 1 ATOM 1097 C C . VAL A 1 132 ? 26.845 26.552 12.492 1.00 30.14 ? 132 VAL A C 1 ATOM 1098 O O . VAL A 1 132 ? 27.733 26.355 13.323 1.00 32.04 ? 132 VAL A O 1 ATOM 1099 C CB . VAL A 1 132 ? 25.170 28.467 12.575 1.00 25.27 ? 132 VAL A CB 1 ATOM 1100 C CG1 . VAL A 1 132 ? 23.757 28.847 12.975 1.00 22.24 ? 132 VAL A CG1 1 ATOM 1101 C CG2 . VAL A 1 132 ? 26.186 29.379 13.245 1.00 32.61 ? 132 VAL A CG2 1 ATOM 1102 N N . SER A 1 133 ? 27.028 26.385 11.189 1.00 23.86 ? 133 SER A N 1 ATOM 1103 C CA . SER A 1 133 ? 28.318 26.027 10.636 1.00 22.05 ? 133 SER A CA 1 ATOM 1104 C C . SER A 1 133 ? 28.331 26.496 9.194 1.00 20.95 ? 133 SER A C 1 ATOM 1105 O O . SER A 1 133 ? 27.293 26.893 8.647 1.00 21.74 ? 133 SER A O 1 ATOM 1106 C CB . SER A 1 133 ? 28.525 24.515 10.687 1.00 25.28 ? 133 SER A CB 1 ATOM 1107 O OG . SER A 1 133 ? 27.520 23.865 9.918 1.00 25.77 ? 133 SER A OG 1 ATOM 1108 N N . GLU A 1 134 ? 29.496 26.445 8.566 1.00 19.88 ? 134 GLU A N 1 ATOM 1109 C CA . GLU A 1 134 ? 29.625 26.969 7.212 1.00 21.69 ? 134 GLU A CA 1 ATOM 1110 C C . GLU A 1 134 ? 30.841 26.352 6.560 1.00 22.90 ? 134 GLU A C 1 ATOM 1111 O O . GLU A 1 134 ? 31.712 25.819 7.248 1.00 23.14 ? 134 GLU A O 1 ATOM 1112 C CB . GLU A 1 134 ? 29.795 28.490 7.257 1.00 21.61 ? 134 GLU A CB 1 ATOM 1113 C CG . GLU A 1 134 ? 31.087 28.947 7.939 1.00 30.76 ? 134 GLU A CG 1 ATOM 1114 C CD . GLU A 1 134 ? 31.123 30.447 8.201 1.00 33.70 ? 134 GLU A CD 1 ATOM 1115 O OE1 . GLU A 1 134 ? 31.834 31.169 7.471 1.00 32.72 ? 134 GLU A OE1 1 ATOM 1116 O OE2 . GLU A 1 134 ? 30.433 30.900 9.137 1.00 41.34 ? 134 GLU A OE2 1 ATOM 1117 N N . THR A 1 135 ? 30.899 26.426 5.239 1.00 22.97 ? 135 THR A N 1 ATOM 1118 C CA . THR A 1 135 ? 32.075 25.986 4.503 1.00 25.84 ? 135 THR A CA 1 ATOM 1119 C C . THR A 1 135 ? 32.930 27.194 4.168 1.00 26.57 ? 135 THR A C 1 ATOM 1120 O O . THR A 1 135 ? 32.486 28.342 4.308 1.00 21.37 ? 135 THR A O 1 ATOM 1121 C CB . THR A 1 135 ? 31.697 25.315 3.176 1.00 19.91 ? 135 THR A CB 1 ATOM 1122 O OG1 . THR A 1 135 ? 31.145 26.294 2.280 1.00 18.13 ? 135 THR A OG1 1 ATOM 1123 C CG2 . THR A 1 135 ? 30.682 24.205 3.408 1.00 19.92 ? 135 THR A CG2 1 ATOM 1124 N N . VAL A 1 136 ? 34.153 26.936 3.711 1.00 22.00 ? 136 VAL A N 1 ATOM 1125 C CA . VAL A 1 136 ? 34.969 27.987 3.128 1.00 21.37 ? 136 VAL A CA 1 ATOM 1126 C C . VAL A 1 136 ? 34.433 28.330 1.737 1.00 21.92 ? 136 VAL A C 1 ATOM 1127 O O . VAL A 1 136 ? 33.423 27.769 1.290 1.00 20.23 ? 136 VAL A O 1 ATOM 1128 C CB . VAL A 1 136 ? 36.474 27.596 3.093 1.00 18.24 ? 136 VAL A CB 1 ATOM 1129 C CG1 . VAL A 1 136 ? 36.961 27.280 4.500 1.00 20.59 ? 136 VAL A CG1 1 ATOM 1130 C CG2 . VAL A 1 136 ? 36.713 26.402 2.177 1.00 18.12 ? 136 VAL A CG2 1 ATOM 1131 N N . PHE A 1 137 ? 35.092 29.255 1.054 1.00 16.43 ? 137 PHE A N 1 ATOM 1132 C CA . PHE A 1 137 ? 34.714 29.597 -0.316 1.00 19.99 ? 137 PHE A CA 1 ATOM 1133 C C . PHE A 1 137 ? 35.155 28.514 -1.277 1.00 23.86 ? 137 PHE A C 1 ATOM 1134 O O . PHE A 1 137 ? 36.327 28.161 -1.337 1.00 22.97 ? 137 PHE A O 1 ATOM 1135 C CB . PHE A 1 137 ? 35.309 30.951 -0.718 1.00 20.21 ? 137 PHE A CB 1 ATOM 1136 C CG . PHE A 1 137 ? 34.823 32.087 0.134 1.00 18.19 ? 137 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 137 ? 33.618 32.718 -0.153 1.00 15.35 ? 137 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 137 ? 35.544 32.501 1.241 1.00 23.89 ? 137 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 137 ? 33.157 33.765 0.645 1.00 19.13 ? 137 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 137 ? 35.089 33.545 2.042 1.00 31.77 ? 137 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 137 ? 33.891 34.171 1.744 1.00 26.24 ? 137 PHE A CZ 1 ATOM 1142 N N . LEU A 1 138 ? 34.205 27.990 -2.033 1.00 18.54 ? 138 LEU A N 1 ATOM 1143 C CA . LEU A 1 138 ? 34.466 26.850 -2.885 1.00 16.19 ? 138 LEU A CA 1 ATOM 1144 C C . LEU A 1 138 ? 34.540 27.337 -4.314 1.00 19.54 ? 138 LEU A C 1 ATOM 1145 O O . LEU A 1 138 ? 33.773 28.205 -4.715 1.00 17.89 ? 138 LEU A O 1 ATOM 1146 C CB . LEU A 1 138 ? 33.344 25.819 -2.725 1.00 16.08 ? 138 LEU A CB 1 ATOM 1147 C CG . LEU A 1 138 ? 33.084 25.429 -1.261 1.00 16.77 ? 138 LEU A CG 1 ATOM 1148 C CD1 . LEU A 1 138 ? 31.765 24.653 -1.125 1.00 16.87 ? 138 LEU A CD1 1 ATOM 1149 C CD2 . LEU A 1 138 ? 34.237 24.592 -0.732 1.00 18.72 ? 138 LEU A CD2 1 ATOM 1150 N N . PRO A 1 139 ? 35.471 26.780 -5.090 1.00 17.90 ? 139 PRO A N 1 ATOM 1151 C CA . PRO A 1 139 ? 35.716 27.292 -6.438 1.00 17.06 ? 139 PRO A CA 1 ATOM 1152 C C . PRO A 1 139 ? 34.666 26.813 -7.431 1.00 21.03 ? 139 PRO A C 1 ATOM 1153 O O . PRO A 1 139 ? 34.157 25.700 -7.311 1.00 18.88 ? 139 PRO A O 1 ATOM 1154 C CB . PRO A 1 139 ? 37.068 26.677 -6.789 1.00 15.61 ? 139 PRO A CB 1 ATOM 1155 C CG . PRO A 1 139 ? 37.093 25.394 -6.024 1.00 18.81 ? 139 PRO A CG 1 ATOM 1156 C CD . PRO A 1 139 ? 36.371 25.668 -4.737 1.00 19.25 ? 139 PRO A CD 1 ATOM 1157 N N . ARG A 1 140 ? 34.354 27.648 -8.414 1.00 13.76 ? 140 ARG A N 1 ATOM 1158 C CA . ARG A 1 140 ? 33.459 27.240 -9.488 1.00 19.30 ? 140 ARG A CA 1 ATOM 1159 C C . ARG A 1 140 ? 34.288 27.161 -10.748 1.00 21.35 ? 140 ARG A C 1 ATOM 1160 O O . ARG A 1 140 ? 35.345 27.792 -10.842 1.00 14.63 ? 140 ARG A O 1 ATOM 1161 C CB . ARG A 1 140 ? 32.325 28.257 -9.677 1.00 17.08 ? 140 ARG A CB 1 ATOM 1162 C CG . ARG A 1 140 ? 31.273 28.258 -8.576 1.00 14.38 ? 140 ARG A CG 1 ATOM 1163 C CD . ARG A 1 140 ? 30.299 29.441 -8.788 1.00 15.96 ? 140 ARG A CD 1 ATOM 1164 N NE . ARG A 1 140 ? 29.876 29.516 -10.185 1.00 14.41 ? 140 ARG A NE 1 ATOM 1165 C CZ . ARG A 1 140 ? 28.829 28.858 -10.681 1.00 21.61 ? 140 ARG A CZ 1 ATOM 1166 N NH1 . ARG A 1 140 ? 28.075 28.106 -9.888 1.00 15.25 ? 140 ARG A NH1 1 ATOM 1167 N NH2 . ARG A 1 140 ? 28.528 28.962 -11.964 1.00 18.75 ? 140 ARG A NH2 1 ATOM 1168 N N . GLU A 1 141 ? 33.808 26.408 -11.726 1.00 15.53 ? 141 GLU A N 1 ATOM 1169 C CA . GLU A 1 141 ? 34.534 26.265 -12.982 1.00 18.10 ? 141 GLU A CA 1 ATOM 1170 C C . GLU A 1 141 ? 34.576 27.561 -13.796 1.00 19.19 ? 141 GLU A C 1 ATOM 1171 O O . GLU A 1 141 ? 35.405 27.695 -14.694 1.00 16.73 ? 141 GLU A O 1 ATOM 1172 C CB . GLU A 1 141 ? 33.974 25.104 -13.801 1.00 23.84 ? 141 GLU A CB 1 ATOM 1173 C CG . GLU A 1 141 ? 34.213 23.754 -13.125 1.00 26.91 ? 141 GLU A CG 1 ATOM 1174 C CD . GLU A 1 141 ? 33.444 22.622 -13.780 1.00 38.43 ? 141 GLU A CD 1 ATOM 1175 O OE1 . GLU A 1 141 ? 33.799 22.244 -14.912 1.00 41.45 ? 141 GLU A OE1 1 ATOM 1176 O OE2 . GLU A 1 141 ? 32.487 22.115 -13.156 1.00 50.05 ? 141 GLU A OE2 1 ATOM 1177 N N . ASP A 1 142 ? 33.709 28.525 -13.468 1.00 17.98 ? 142 ASP A N 1 ATOM 1178 C CA . ASP A 1 142 ? 33.774 29.846 -14.124 1.00 14.51 ? 142 ASP A CA 1 ATOM 1179 C C . ASP A 1 142 ? 34.586 30.851 -13.286 1.00 20.19 ? 142 ASP A C 1 ATOM 1180 O O . ASP A 1 142 ? 34.624 32.051 -13.586 1.00 17.91 ? 142 ASP A O 1 ATOM 1181 C CB . ASP A 1 142 ? 32.380 30.396 -14.468 1.00 13.83 ? 142 ASP A CB 1 ATOM 1182 C CG . ASP A 1 142 ? 31.492 30.568 -13.236 1.00 19.00 ? 142 ASP A CG 1 ATOM 1183 O OD1 . ASP A 1 142 ? 32.009 30.443 -12.110 1.00 15.63 ? 142 ASP A OD1 1 ATOM 1184 O OD2 . ASP A 1 142 ? 30.280 30.815 -13.397 1.00 21.23 ? 142 ASP A OD2 1 ATOM 1185 N N . HIS A 1 143 ? 35.234 30.330 -12.247 1.00 15.07 ? 143 HIS A N 1 ATOM 1186 C CA . HIS A 1 143 ? 36.196 31.074 -11.426 1.00 13.23 ? 143 HIS A CA 1 ATOM 1187 C C . HIS A 1 143 ? 35.578 32.127 -10.510 1.00 14.00 ? 143 HIS A C 1 ATOM 1188 O O . HIS A 1 143 ? 36.276 32.949 -9.911 1.00 16.98 ? 143 HIS A O 1 ATOM 1189 C CB . HIS A 1 143 ? 37.321 31.600 -12.310 1.00 15.67 ? 143 HIS A CB 1 ATOM 1190 C CG . HIS A 1 143 ? 37.761 30.589 -13.318 1.00 13.15 ? 143 HIS A CG 1 ATOM 1191 N ND1 . HIS A 1 143 ? 38.198 29.330 -12.956 1.00 12.63 ? 143 HIS A ND1 1 ATOM 1192 C CD2 . HIS A 1 143 ? 37.779 30.620 -14.672 1.00 12.71 ? 143 HIS A CD2 1 ATOM 1193 C CE1 . HIS A 1 143 ? 38.494 28.642 -14.043 1.00 13.18 ? 143 HIS A CE1 1 ATOM 1194 N NE2 . HIS A 1 143 ? 38.249 29.404 -15.097 1.00 14.79 ? 143 HIS A NE2 1 ATOM 1195 N N . LEU A 1 144 ? 34.254 32.053 -10.390 1.00 16.91 ? 144 LEU A N 1 ATOM 1196 C CA . LEU A 1 144 ? 33.530 32.686 -9.298 1.00 14.84 ? 144 LEU A CA 1 ATOM 1197 C C . LEU A 1 144 ? 33.544 31.709 -8.119 1.00 15.40 ? 144 LEU A C 1 ATOM 1198 O O . LEU A 1 144 ? 34.281 30.717 -8.140 1.00 17.14 ? 144 LEU A O 1 ATOM 1199 C CB . LEU A 1 144 ? 32.093 32.962 -9.736 1.00 13.66 ? 144 LEU A CB 1 ATOM 1200 C CG . LEU A 1 144 ? 31.976 33.866 -10.961 1.00 15.13 ? 144 LEU A CG 1 ATOM 1201 C CD1 . LEU A 1 144 ? 30.527 34.001 -11.326 1.00 19.34 ? 144 LEU A CD1 1 ATOM 1202 C CD2 . LEU A 1 144 ? 32.607 35.243 -10.700 1.00 18.99 ? 144 LEU A CD2 1 ATOM 1203 N N . PHE A 1 145 ? 32.722 31.978 -7.105 1.00 18.74 ? 145 PHE A N 1 ATOM 1204 C CA . PHE A 1 145 ? 32.734 31.185 -5.885 1.00 13.25 ? 145 PHE A CA 1 ATOM 1205 C C . PHE A 1 145 ? 31.348 30.752 -5.448 1.00 15.30 ? 145 PHE A C 1 ATOM 1206 O O . PHE A 1 145 ? 30.329 31.313 -5.869 1.00 15.44 ? 145 PHE A O 1 ATOM 1207 C CB . PHE A 1 145 ? 33.391 31.966 -4.737 1.00 15.82 ? 145 PHE A CB 1 ATOM 1208 C CG . PHE A 1 145 ? 34.826 32.275 -4.984 1.00 12.75 ? 145 PHE A CG 1 ATOM 1209 C CD1 . PHE A 1 145 ? 35.812 31.348 -4.656 1.00 15.12 ? 145 PHE A CD1 1 ATOM 1210 C CD2 . PHE A 1 145 ? 35.193 33.451 -5.616 1.00 12.51 ? 145 PHE A CD2 1 ATOM 1211 C CE1 . PHE A 1 145 ? 37.153 31.611 -4.917 1.00 17.68 ? 145 PHE A CE1 1 ATOM 1212 C CE2 . PHE A 1 145 ? 36.542 33.726 -5.877 1.00 16.22 ? 145 PHE A CE2 1 ATOM 1213 C CZ . PHE A 1 145 ? 37.514 32.808 -5.529 1.00 18.84 ? 145 PHE A CZ 1 ATOM 1214 N N . ARG A 1 146 ? 31.325 29.730 -4.606 1.00 15.48 ? 146 ARG A N 1 ATOM 1215 C CA A ARG A 1 146 ? 30.103 29.353 -3.912 0.48 17.61 ? 146 ARG A CA 1 ATOM 1216 C CA B ARG A 1 146 ? 30.107 29.319 -3.925 0.52 17.34 ? 146 ARG A CA 1 ATOM 1217 C C . ARG A 1 146 ? 30.421 28.996 -2.467 1.00 20.17 ? 146 ARG A C 1 ATOM 1218 O O . ARG A 1 146 ? 31.594 28.840 -2.095 1.00 18.22 ? 146 ARG A O 1 ATOM 1219 C CB A ARG A 1 146 ? 29.373 28.218 -4.627 0.48 16.05 ? 146 ARG A CB 1 ATOM 1220 C CB B ARG A 1 146 ? 29.428 28.144 -4.636 0.52 15.92 ? 146 ARG A CB 1 ATOM 1221 C CG A ARG A 1 146 ? 30.183 26.963 -4.831 0.48 16.10 ? 146 ARG A CG 1 ATOM 1222 C CG B ARG A 1 146 ? 30.335 26.980 -5.015 0.52 17.44 ? 146 ARG A CG 1 ATOM 1223 C CD A ARG A 1 146 ? 29.385 25.962 -5.646 0.48 20.58 ? 146 ARG A CD 1 ATOM 1224 C CD B ARG A 1 146 ? 29.609 26.038 -5.979 0.52 23.95 ? 146 ARG A CD 1 ATOM 1225 N NE A ARG A 1 146 ? 30.192 24.802 -6.005 0.48 26.58 ? 146 ARG A NE 1 ATOM 1226 N NE B ARG A 1 146 ? 30.481 25.004 -6.540 0.52 27.62 ? 146 ARG A NE 1 ATOM 1227 C CZ A ARG A 1 146 ? 30.182 23.653 -5.340 0.48 29.79 ? 146 ARG A CZ 1 ATOM 1228 C CZ B ARG A 1 146 ? 30.330 24.473 -7.754 0.52 33.16 ? 146 ARG A CZ 1 ATOM 1229 N NH1 A ARG A 1 146 ? 29.394 23.498 -4.286 0.48 24.15 ? 146 ARG A NH1 1 ATOM 1230 N NH1 B ARG A 1 146 ? 29.346 24.887 -8.546 0.52 36.20 ? 146 ARG A NH1 1 ATOM 1231 N NH2 A ARG A 1 146 ? 30.955 22.652 -5.737 0.48 31.41 ? 146 ARG A NH2 1 ATOM 1232 N NH2 B ARG A 1 146 ? 31.168 23.535 -8.184 0.52 27.42 ? 146 ARG A NH2 1 ATOM 1233 N N . LYS A 1 147 ? 29.382 28.902 -1.647 1.00 16.42 ? 147 LYS A N 1 ATOM 1234 C CA . LYS A 1 147 ? 29.557 28.759 -0.205 1.00 20.73 ? 147 LYS A CA 1 ATOM 1235 C C . LYS A 1 147 ? 28.277 28.188 0.392 1.00 16.09 ? 147 LYS A C 1 ATOM 1236 O O . LYS A 1 147 ? 27.185 28.430 -0.136 1.00 15.58 ? 147 LYS A O 1 ATOM 1237 C CB . LYS A 1 147 ? 29.841 30.138 0.413 1.00 16.20 ? 147 LYS A CB 1 ATOM 1238 C CG . LYS A 1 147 ? 30.570 30.116 1.751 1.00 20.06 ? 147 LYS A CG 1 ATOM 1239 C CD . LYS A 1 147 ? 30.801 31.542 2.258 1.00 17.98 ? 147 LYS A CD 1 ATOM 1240 C CE . LYS A 1 147 ? 31.864 31.604 3.354 1.00 26.79 ? 147 LYS A CE 1 ATOM 1241 N NZ . LYS A 1 147 ? 31.405 31.014 4.639 1.00 23.41 ? 147 LYS A NZ 1 ATOM 1242 N N . PHE A 1 148 ? 28.414 27.411 1.466 1.00 17.12 ? 148 PHE A N 1 ATOM 1243 C CA . PHE A 1 148 ? 27.258 26.824 2.150 1.00 17.11 ? 148 PHE A CA 1 ATOM 1244 C C . PHE A 1 148 ? 27.262 27.254 3.606 1.00 20.93 ? 148 PHE A C 1 ATOM 1245 O O . PHE A 1 148 ? 28.322 27.271 4.245 1.00 23.68 ? 148 PHE A O 1 ATOM 1246 C CB . PHE A 1 148 ? 27.306 25.298 2.128 1.00 13.31 ? 148 PHE A CB 1 ATOM 1247 C CG . PHE A 1 148 ? 27.158 24.679 0.757 1.00 18.58 ? 148 PHE A CG 1 ATOM 1248 C CD1 . PHE A 1 148 ? 25.933 24.166 0.338 1.00 16.30 ? 148 PHE A CD1 1 ATOM 1249 C CD2 . PHE A 1 148 ? 28.259 24.559 -0.087 1.00 16.29 ? 148 PHE A CD2 1 ATOM 1250 C CE1 . PHE A 1 148 ? 25.806 23.569 -0.918 1.00 18.32 ? 148 PHE A CE1 1 ATOM 1251 C CE2 . PHE A 1 148 ? 28.143 23.974 -1.335 1.00 15.64 ? 148 PHE A CE2 1 ATOM 1252 C CZ . PHE A 1 148 ? 26.912 23.480 -1.755 1.00 23.53 ? 148 PHE A CZ 1 ATOM 1253 N N . HIS A 1 149 ? 26.084 27.593 4.131 1.00 17.41 ? 149 HIS A N 1 ATOM 1254 C CA . HIS A 1 149 ? 25.897 27.804 5.564 1.00 15.24 ? 149 HIS A CA 1 ATOM 1255 C C . HIS A 1 149 ? 24.788 26.863 6.054 1.00 22.29 ? 149 HIS A C 1 ATOM 1256 O O . HIS A 1 149 ? 23.863 26.559 5.306 1.00 20.40 ? 149 HIS A O 1 ATOM 1257 C CB . HIS A 1 149 ? 25.537 29.263 5.855 1.00 16.88 ? 149 HIS A CB 1 ATOM 1258 C CG . HIS A 1 149 ? 26.719 30.181 5.855 1.00 19.63 ? 149 HIS A CG 1 ATOM 1259 N ND1 . HIS A 1 149 ? 27.149 30.833 6.988 1.00 16.88 ? 149 HIS A ND1 1 ATOM 1260 C CD2 . HIS A 1 149 ? 27.581 30.531 4.870 1.00 14.33 ? 149 HIS A CD2 1 ATOM 1261 C CE1 . HIS A 1 149 ? 28.215 31.559 6.702 1.00 24.18 ? 149 HIS A CE1 1 ATOM 1262 N NE2 . HIS A 1 149 ? 28.501 31.393 5.424 1.00 17.90 ? 149 HIS A NE2 1 ATOM 1263 N N . TYR A 1 150 ? 24.879 26.410 7.302 1.00 17.39 ? 150 TYR A N 1 ATOM 1264 C CA . TYR A 1 150 ? 23.983 25.369 7.806 1.00 21.91 ? 150 TYR A CA 1 ATOM 1265 C C . TYR A 1 150 ? 23.371 25.743 9.150 1.00 23.03 ? 150 TYR A C 1 ATOM 1266 O O . TYR A 1 150 ? 24.051 26.297 10.031 1.00 19.22 ? 150 TYR A O 1 ATOM 1267 C CB . TYR A 1 150 ? 24.731 24.027 7.964 1.00 21.18 ? 150 TYR A CB 1 ATOM 1268 C CG . TYR A 1 150 ? 25.401 23.504 6.703 1.00 19.15 ? 150 TYR A CG 1 ATOM 1269 C CD1 . TYR A 1 150 ? 24.677 22.810 5.746 1.00 19.63 ? 150 TYR A CD1 1 ATOM 1270 C CD2 . TYR A 1 150 ? 26.762 23.684 6.489 1.00 22.84 ? 150 TYR A CD2 1 ATOM 1271 C CE1 . TYR A 1 150 ? 25.282 22.325 4.603 1.00 17.20 ? 150 TYR A CE1 1 ATOM 1272 C CE2 . TYR A 1 150 ? 27.385 23.195 5.349 1.00 21.71 ? 150 TYR A CE2 1 ATOM 1273 C CZ . TYR A 1 150 ? 26.637 22.515 4.410 1.00 23.92 ? 150 TYR A CZ 1 ATOM 1274 O OH . TYR A 1 150 ? 27.241 22.028 3.274 1.00 17.87 ? 150 TYR A OH 1 ATOM 1275 N N . LEU A 1 151 ? 22.096 25.408 9.317 1.00 19.99 ? 151 LEU A N 1 ATOM 1276 C CA . LEU A 1 151 ? 21.423 25.611 10.596 1.00 19.29 ? 151 LEU A CA 1 ATOM 1277 C C . LEU A 1 151 ? 20.519 24.433 10.957 1.00 19.21 ? 151 LEU A C 1 ATOM 1278 O O . LEU A 1 151 ? 19.425 24.287 10.406 1.00 19.65 ? 151 LEU A O 1 ATOM 1279 C CB . LEU A 1 151 ? 20.603 26.901 10.568 1.00 18.20 ? 151 LEU A CB 1 ATOM 1280 C CG . LEU A 1 151 ? 19.672 27.154 11.761 1.00 20.82 ? 151 LEU A CG 1 ATOM 1281 C CD1 . LEU A 1 151 ? 20.451 27.243 13.072 1.00 26.41 ? 151 LEU A CD1 1 ATOM 1282 C CD2 . LEU A 1 151 ? 18.825 28.419 11.537 1.00 25.13 ? 151 LEU A CD2 1 ATOM 1283 N N . PRO A 1 152 ? 20.972 23.583 11.884 1.00 22.56 ? 152 PRO A N 1 ATOM 1284 C CA . PRO A 1 152 ? 20.082 22.545 12.409 1.00 27.30 ? 152 PRO A CA 1 ATOM 1285 C C . PRO A 1 152 ? 18.893 23.201 13.102 1.00 30.49 ? 152 PRO A C 1 ATOM 1286 O O . PRO A 1 152 ? 19.066 24.250 13.721 1.00 27.74 ? 152 PRO A O 1 ATOM 1287 C CB . PRO A 1 152 ? 20.961 21.799 13.422 1.00 34.48 ? 152 PRO A CB 1 ATOM 1288 C CG . PRO A 1 152 ? 22.110 22.709 13.700 1.00 35.31 ? 152 PRO A CG 1 ATOM 1289 C CD . PRO A 1 152 ? 22.320 23.518 12.472 1.00 27.17 ? 152 PRO A CD 1 ATOM 1290 N N . PHE A 1 153 ? 17.706 22.621 12.966 1.00 26.35 ? 153 PHE A N 1 ATOM 1291 C CA . PHE A 1 153 ? 16.511 23.198 13.574 1.00 27.05 ? 153 PHE A CA 1 ATOM 1292 C C . PHE A 1 153 ? 15.448 22.139 13.827 1.00 31.01 ? 153 PHE A C 1 ATOM 1293 O O . PHE A 1 153 ? 15.482 21.050 13.249 1.00 30.14 ? 153 PHE A O 1 ATOM 1294 C CB . PHE A 1 153 ? 15.943 24.341 12.712 1.00 26.46 ? 153 PHE A CB 1 ATOM 1295 C CG . PHE A 1 153 ? 15.226 23.880 11.464 1.00 23.71 ? 153 PHE A CG 1 ATOM 1296 C CD1 . PHE A 1 153 ? 13.861 24.086 11.316 1.00 22.98 ? 153 PHE A CD1 1 ATOM 1297 C CD2 . PHE A 1 153 ? 15.921 23.247 10.437 1.00 24.09 ? 153 PHE A CD2 1 ATOM 1298 C CE1 . PHE A 1 153 ? 13.198 23.664 10.171 1.00 27.40 ? 153 PHE A CE1 1 ATOM 1299 C CE2 . PHE A 1 153 ? 15.264 22.827 9.289 1.00 26.65 ? 153 PHE A CE2 1 ATOM 1300 C CZ . PHE A 1 153 ? 13.907 23.037 9.150 1.00 26.44 ? 153 PHE A CZ 1 ATOM 1301 N N . LEU A 1 154 ? 14.520 22.462 14.719 1.00 30.38 ? 154 LEU A N 1 ATOM 1302 C CA . LEU A 1 154 ? 13.371 21.614 14.976 1.00 30.48 ? 154 LEU A CA 1 ATOM 1303 C C . LEU A 1 154 ? 12.163 22.292 14.339 1.00 28.67 ? 154 LEU A C 1 ATOM 1304 O O . LEU A 1 154 ? 11.703 23.328 14.821 1.00 27.72 ? 154 LEU A O 1 ATOM 1305 C CB . LEU A 1 154 ? 13.166 21.449 16.480 1.00 30.54 ? 154 LEU A CB 1 ATOM 1306 C CG . LEU A 1 154 ? 12.391 20.213 16.932 1.00 39.58 ? 154 LEU A CG 1 ATOM 1307 C CD1 . LEU A 1 154 ? 13.031 18.960 16.366 1.00 45.73 ? 154 LEU A CD1 1 ATOM 1308 C CD2 . LEU A 1 154 ? 12.314 20.139 18.463 1.00 36.47 ? 154 LEU A CD2 1 ATOM 1309 N N . PRO A 1 155 ? 11.651 21.715 13.246 1.00 32.29 ? 155 PRO A N 1 ATOM 1310 C CA . PRO A 1 155 ? 10.606 22.356 12.445 1.00 25.42 ? 155 PRO A CA 1 ATOM 1311 C C . PRO A 1 155 ? 9.324 22.529 13.241 1.00 33.68 ? 155 PRO A C 1 ATOM 1312 O O . PRO A 1 155 ? 8.849 21.571 13.851 1.00 29.25 ? 155 PRO A O 1 ATOM 1313 C CB . PRO A 1 155 ? 10.368 21.359 11.309 1.00 29.25 ? 155 PRO A CB 1 ATOM 1314 C CG . PRO A 1 155 ? 11.608 20.494 11.273 1.00 27.42 ? 155 PRO A CG 1 ATOM 1315 C CD . PRO A 1 155 ? 12.049 20.407 12.699 1.00 35.97 ? 155 PRO A CD 1 ATOM 1316 N N . SER A 1 156 ? 8.783 23.744 13.234 1.00 32.72 ? 156 SER A N 1 ATOM 1317 C CA . SER A 1 156 ? 7.505 24.027 13.868 1.00 35.65 ? 156 SER A CA 1 ATOM 1318 C C . SER A 1 156 ? 6.770 25.076 13.055 1.00 34.23 ? 156 SER A C 1 ATOM 1319 O O . SER A 1 156 ? 7.364 25.764 12.236 1.00 41.29 ? 156 SER A O 1 ATOM 1320 C CB . SER A 1 156 ? 7.698 24.520 15.303 1.00 47.32 ? 156 SER A CB 1 ATOM 1321 O OG . SER A 1 156 ? 8.291 25.802 15.322 1.00 55.42 ? 156 SER A OG 1 ATOM 1322 N N . THR A 1 157 ? 5.472 25.204 13.293 1.00 37.85 ? 157 THR A N 1 ATOM 1323 C CA . THR A 1 157 ? 4.676 26.211 12.613 1.00 44.06 ? 157 THR A CA 1 ATOM 1324 C C . THR A 1 157 ? 4.879 27.581 13.253 1.00 46.06 ? 157 THR A C 1 ATOM 1325 O O . THR A 1 157 ? 4.364 28.590 12.764 1.00 49.28 ? 157 THR A O 1 ATOM 1326 C CB . THR A 1 157 ? 3.191 25.856 12.694 1.00 50.65 ? 157 THR A CB 1 ATOM 1327 O OG1 . THR A 1 157 ? 2.795 25.817 14.069 1.00 50.83 ? 157 THR A OG1 1 ATOM 1328 C CG2 . THR A 1 157 ? 2.940 24.494 12.067 1.00 53.65 ? 157 THR A CG2 1 ATOM 1329 N N . GLU A 1 158 ? 5.620 27.608 14.358 1.00 45.38 ? 158 GLU A N 1 ATOM 1330 C CA . GLU A 1 158 ? 5.835 28.837 15.121 1.00 49.53 ? 158 GLU A CA 1 ATOM 1331 C C . GLU A 1 158 ? 6.930 29.704 14.512 1.00 46.16 ? 158 GLU A C 1 ATOM 1332 O O . GLU A 1 158 ? 6.858 30.933 14.557 1.00 49.16 ? 158 GLU A O 1 ATOM 1333 C CB . GLU A 1 158 ? 6.204 28.504 16.569 1.00 55.33 ? 158 GLU A CB 1 ATOM 1334 C CG . GLU A 1 158 ? 5.230 27.566 17.262 1.00 68.77 ? 158 GLU A CG 1 ATOM 1335 C CD . GLU A 1 158 ? 3.844 28.167 17.400 1.00 79.69 ? 158 GLU A CD 1 ATOM 1336 O OE1 . GLU A 1 158 ? 3.542 28.717 18.480 1.00 88.15 ? 158 GLU A OE1 1 ATOM 1337 O OE2 . GLU A 1 158 ? 3.057 28.093 16.431 1.00 81.25 ? 158 GLU A OE2 1 ATOM 1338 N N . ASP A 1 159 ? 7.941 29.055 13.943 1.00 33.18 ? 159 ASP A N 1 ATOM 1339 C CA . ASP A 1 159 ? 9.144 29.746 13.495 1.00 31.78 ? 159 ASP A CA 1 ATOM 1340 C C . ASP A 1 159 ? 9.227 29.931 11.985 1.00 39.33 ? 159 ASP A C 1 ATOM 1341 O O . ASP A 1 159 ? 8.918 29.020 11.220 1.00 43.51 ? 159 ASP A O 1 ATOM 1342 C CB . ASP A 1 159 ? 10.390 28.973 13.931 1.00 32.86 ? 159 ASP A CB 1 ATOM 1343 C CG . ASP A 1 159 ? 10.488 28.817 15.428 1.00 44.10 ? 159 ASP A CG 1 ATOM 1344 O OD1 . ASP A 1 159 ? 10.153 29.776 16.155 1.00 44.34 ? 159 ASP A OD1 1 ATOM 1345 O OD2 . ASP A 1 159 ? 10.906 27.728 15.876 1.00 50.21 ? 159 ASP A OD2 1 ATOM 1346 N N . VAL A 1 160 ? 9.672 31.112 11.568 1.00 32.32 ? 160 VAL A N 1 ATOM 1347 C CA . VAL A 1 160 ? 10.104 31.312 10.195 1.00 25.53 ? 160 VAL A CA 1 ATOM 1348 C C . VAL A 1 160 ? 11.596 31.619 10.184 1.00 23.86 ? 160 VAL A C 1 ATOM 1349 O O . VAL A 1 160 ? 12.157 32.054 11.189 1.00 26.57 ? 160 VAL A O 1 ATOM 1350 C CB . VAL A 1 160 ? 9.318 32.423 9.499 1.00 29.13 ? 160 VAL A CB 1 ATOM 1351 C CG1 . VAL A 1 160 ? 7.823 32.153 9.613 1.00 35.82 ? 160 VAL A CG1 1 ATOM 1352 C CG2 . VAL A 1 160 ? 9.668 33.785 10.082 1.00 35.25 ? 160 VAL A CG2 1 ATOM 1353 N N . TYR A 1 161 ? 12.237 31.380 9.047 1.00 22.10 ? 161 TYR A N 1 ATOM 1354 C CA . TYR A 1 161 ? 13.670 31.569 8.938 1.00 25.91 ? 161 TYR A CA 1 ATOM 1355 C C . TYR A 1 161 ? 14.025 32.388 7.702 1.00 26.20 ? 161 TYR A C 1 ATOM 1356 O O . TYR A 1 161 ? 13.265 32.430 6.723 1.00 23.41 ? 161 TYR A O 1 ATOM 1357 C CB . TYR A 1 161 ? 14.387 30.218 8.885 1.00 22.20 ? 161 TYR A CB 1 ATOM 1358 C CG . TYR A 1 161 ? 14.302 29.410 10.161 1.00 21.09 ? 161 TYR A CG 1 ATOM 1359 C CD1 . TYR A 1 161 ? 15.294 29.501 11.129 1.00 25.24 ? 161 TYR A CD1 1 ATOM 1360 C CD2 . TYR A 1 161 ? 13.229 28.558 10.402 1.00 27.21 ? 161 TYR A CD2 1 ATOM 1361 C CE1 . TYR A 1 161 ? 15.224 28.767 12.297 1.00 21.03 ? 161 TYR A CE1 1 ATOM 1362 C CE2 . TYR A 1 161 ? 13.154 27.813 11.569 1.00 31.59 ? 161 TYR A CE2 1 ATOM 1363 C CZ . TYR A 1 161 ? 14.162 27.924 12.510 1.00 30.88 ? 161 TYR A CZ 1 ATOM 1364 O OH . TYR A 1 161 ? 14.112 27.195 13.672 1.00 32.21 ? 161 TYR A OH 1 ATOM 1365 N N . ASP A 1 162 ? 15.175 33.055 7.772 1.00 22.17 ? 162 ASP A N 1 ATOM 1366 C CA . ASP A 1 162 ? 15.749 33.745 6.632 1.00 21.99 ? 162 ASP A CA 1 ATOM 1367 C C . ASP A 1 162 ? 17.255 33.562 6.644 1.00 24.76 ? 162 ASP A C 1 ATOM 1368 O O . ASP A 1 162 ? 17.881 33.570 7.700 1.00 24.20 ? 162 ASP A O 1 ATOM 1369 C CB . ASP A 1 162 ? 15.442 35.246 6.671 1.00 22.79 ? 162 ASP A CB 1 ATOM 1370 C CG . ASP A 1 162 ? 13.961 35.546 6.560 1.00 29.08 ? 162 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 162 ? 13.441 35.546 5.419 1.00 24.64 ? 162 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 162 ? 13.323 35.788 7.614 1.00 23.87 ? 162 ASP A OD2 1 ATOM 1373 N N . CYS A 1 163 ? 17.835 33.390 5.466 1.00 16.02 ? 163 CYS A N 1 ATOM 1374 C CA . CYS A 1 163 ? 19.270 33.523 5.334 1.00 15.25 ? 163 CYS A CA 1 ATOM 1375 C C . CYS A 1 163 ? 19.514 34.919 4.787 1.00 22.22 ? 163 CYS A C 1 ATOM 1376 O O . CYS A 1 163 ? 18.993 35.277 3.727 1.00 22.17 ? 163 CYS A O 1 ATOM 1377 C CB . CYS A 1 163 ? 19.829 32.470 4.383 1.00 22.07 ? 163 CYS A CB 1 ATOM 1378 S SG . CYS A 1 163 ? 21.616 32.561 4.193 1.00 24.93 ? 163 CYS A SG 1 ATOM 1379 N N . ARG A 1 164 ? 20.267 35.723 5.525 1.00 20.72 ? 164 ARG A N 1 ATOM 1380 C CA . ARG A 1 164 ? 20.575 37.071 5.070 1.00 18.05 ? 164 ARG A CA 1 ATOM 1381 C C . ARG A 1 164 ? 22.003 37.147 4.568 1.00 19.49 ? 164 ARG A C 1 ATOM 1382 O O . ARG A 1 164 ? 22.963 36.878 5.308 1.00 20.31 ? 164 ARG A O 1 ATOM 1383 C CB . ARG A 1 164 ? 20.347 38.099 6.171 1.00 19.57 ? 164 ARG A CB 1 ATOM 1384 C CG . ARG A 1 164 ? 20.643 39.516 5.720 1.00 28.26 ? 164 ARG A CG 1 ATOM 1385 C CD . ARG A 1 164 ? 20.405 40.488 6.858 1.00 33.06 ? 164 ARG A CD 1 ATOM 1386 N NE . ARG A 1 164 ? 21.404 40.335 7.911 1.00 23.41 ? 164 ARG A NE 1 ATOM 1387 C CZ . ARG A 1 164 ? 21.179 40.607 9.189 1.00 28.93 ? 164 ARG A CZ 1 ATOM 1388 N NH1 . ARG A 1 164 ? 19.983 41.023 9.578 1.00 26.22 ? 164 ARG A NH1 1 ATOM 1389 N NH2 . ARG A 1 164 ? 22.143 40.449 10.084 1.00 32.02 ? 164 ARG A NH2 1 ATOM 1390 N N . VAL A 1 165 ? 22.146 37.523 3.304 1.00 16.50 ? 165 VAL A N 1 ATOM 1391 C CA . VAL A 1 165 ? 23.462 37.565 2.689 1.00 19.72 ? 165 VAL A CA 1 ATOM 1392 C C . VAL A 1 165 ? 23.852 38.991 2.290 1.00 23.50 ? 165 VAL A C 1 ATOM 1393 O O . VAL A 1 165 ? 23.112 39.663 1.562 1.00 23.70 ? 165 VAL A O 1 ATOM 1394 C CB . VAL A 1 165 ? 23.512 36.629 1.469 1.00 17.95 ? 165 VAL A CB 1 ATOM 1395 C CG1 . VAL A 1 165 ? 24.871 36.718 0.776 1.00 17.64 ? 165 VAL A CG1 1 ATOM 1396 C CG2 . VAL A 1 165 ? 23.219 35.190 1.912 1.00 16.89 ? 165 VAL A CG2 1 ATOM 1397 N N . GLU A 1 166 ? 24.995 39.459 2.790 1.00 18.18 ? 166 GLU A N 1 ATOM 1398 C CA . GLU A 1 166 ? 25.547 40.743 2.357 1.00 21.42 ? 166 GLU A CA 1 ATOM 1399 C C . GLU A 1 166 ? 26.774 40.522 1.483 1.00 24.05 ? 166 GLU A C 1 ATOM 1400 O O . GLU A 1 166 ? 27.628 39.693 1.805 1.00 22.36 ? 166 GLU A O 1 ATOM 1401 C CB . GLU A 1 166 ? 25.953 41.609 3.553 1.00 26.11 ? 166 GLU A CB 1 ATOM 1402 C CG . GLU A 1 166 ? 24.859 41.932 4.551 1.00 33.79 ? 166 GLU A CG 1 ATOM 1403 C CD . GLU A 1 166 ? 25.446 42.368 5.891 1.00 45.57 ? 166 GLU A CD 1 ATOM 1404 O OE1 . GLU A 1 166 ? 26.370 43.219 5.904 1.00 39.69 ? 166 GLU A OE1 1 ATOM 1405 O OE2 . GLU A 1 166 ? 25.010 41.824 6.928 1.00 49.39 ? 166 GLU A OE2 1 ATOM 1406 N N . HIS A 1 167 ? 26.857 41.272 0.386 1.00 20.42 ? 167 HIS A N 1 ATOM 1407 C CA . HIS A 1 167 ? 27.982 41.195 -0.544 1.00 13.77 ? 167 HIS A CA 1 ATOM 1408 C C . HIS A 1 167 ? 28.136 42.538 -1.256 1.00 23.49 ? 167 HIS A C 1 ATOM 1409 O O . HIS A 1 167 ? 27.138 43.204 -1.537 1.00 19.12 ? 167 HIS A O 1 ATOM 1410 C CB . HIS A 1 167 ? 27.747 40.077 -1.557 1.00 15.18 ? 167 HIS A CB 1 ATOM 1411 C CG . HIS A 1 167 ? 28.901 39.840 -2.487 1.00 19.70 ? 167 HIS A CG 1 ATOM 1412 N ND1 . HIS A 1 167 ? 29.039 40.506 -3.687 1.00 16.70 ? 167 HIS A ND1 1 ATOM 1413 C CD2 . HIS A 1 167 ? 29.958 38.995 -2.402 1.00 17.21 ? 167 HIS A CD2 1 ATOM 1414 C CE1 . HIS A 1 167 ? 30.137 40.092 -4.295 1.00 22.11 ? 167 HIS A CE1 1 ATOM 1415 N NE2 . HIS A 1 167 ? 30.716 39.175 -3.535 1.00 20.01 ? 167 HIS A NE2 1 ATOM 1416 N N . TRP A 1 168 ? 29.371 42.943 -1.555 1.00 17.38 ? 168 TRP A N 1 ATOM 1417 C CA . TRP A 1 168 ? 29.592 44.281 -2.121 1.00 25.87 ? 168 TRP A CA 1 ATOM 1418 C C . TRP A 1 168 ? 28.875 44.475 -3.460 1.00 24.42 ? 168 TRP A C 1 ATOM 1419 O O . TRP A 1 168 ? 28.639 45.601 -3.877 1.00 21.17 ? 168 TRP A O 1 ATOM 1420 C CB . TRP A 1 168 ? 31.087 44.612 -2.237 1.00 24.07 ? 168 TRP A CB 1 ATOM 1421 C CG . TRP A 1 168 ? 31.775 44.648 -0.897 1.00 25.31 ? 168 TRP A CG 1 ATOM 1422 C CD1 . TRP A 1 168 ? 31.309 45.234 0.249 1.00 27.49 ? 168 TRP A CD1 1 ATOM 1423 C CD2 . TRP A 1 168 ? 33.028 44.041 -0.557 1.00 28.03 ? 168 TRP A CD2 1 ATOM 1424 N NE1 . TRP A 1 168 ? 32.204 45.043 1.275 1.00 30.11 ? 168 TRP A NE1 1 ATOM 1425 C CE2 . TRP A 1 168 ? 33.263 44.307 0.810 1.00 33.08 ? 168 TRP A CE2 1 ATOM 1426 C CE3 . TRP A 1 168 ? 33.975 43.296 -1.276 1.00 23.00 ? 168 TRP A CE3 1 ATOM 1427 C CZ2 . TRP A 1 168 ? 34.408 43.858 1.473 1.00 32.75 ? 168 TRP A CZ2 1 ATOM 1428 C CZ3 . TRP A 1 168 ? 35.104 42.849 -0.624 1.00 21.86 ? 168 TRP A CZ3 1 ATOM 1429 C CH2 . TRP A 1 168 ? 35.317 43.134 0.746 1.00 24.97 ? 168 TRP A CH2 1 ATOM 1430 N N . GLY A 1 169 ? 28.522 43.376 -4.123 1.00 16.43 ? 169 GLY A N 1 ATOM 1431 C CA . GLY A 1 169 ? 27.792 43.458 -5.377 1.00 17.02 ? 169 GLY A CA 1 ATOM 1432 C C . GLY A 1 169 ? 26.295 43.706 -5.202 1.00 21.87 ? 169 GLY A C 1 ATOM 1433 O O . GLY A 1 169 ? 25.587 43.939 -6.180 1.00 22.51 ? 169 GLY A O 1 ATOM 1434 N N . LEU A 1 170 ? 25.812 43.649 -3.963 1.00 21.06 ? 170 LEU A N 1 ATOM 1435 C CA . LEU A 1 170 ? 24.391 43.858 -3.669 1.00 24.58 ? 170 LEU A CA 1 ATOM 1436 C C . LEU A 1 170 ? 24.156 45.270 -3.144 1.00 33.15 ? 170 LEU A C 1 ATOM 1437 O O . LEU A 1 170 ? 24.969 45.792 -2.385 1.00 35.35 ? 170 LEU A O 1 ATOM 1438 C CB . LEU A 1 170 ? 23.902 42.838 -2.631 1.00 21.58 ? 170 LEU A CB 1 ATOM 1439 C CG . LEU A 1 170 ? 23.873 41.359 -3.031 1.00 24.67 ? 170 LEU A CG 1 ATOM 1440 C CD1 . LEU A 1 170 ? 23.736 40.457 -1.801 1.00 22.03 ? 170 LEU A CD1 1 ATOM 1441 C CD2 . LEU A 1 170 ? 22.725 41.101 -4.026 1.00 27.72 ? 170 LEU A CD2 1 ATOM 1442 N N . ASP A 1 171 ? 23.041 45.883 -3.540 1.00 32.26 ? 171 ASP A N 1 ATOM 1443 C CA . ASP A 1 171 ? 22.712 47.226 -3.074 1.00 38.77 ? 171 ASP A CA 1 ATOM 1444 C C . ASP A 1 171 ? 22.164 47.168 -1.659 1.00 39.73 ? 171 ASP A C 1 ATOM 1445 O O . ASP A 1 171 ? 22.316 48.112 -0.886 1.00 45.69 ? 171 ASP A O 1 ATOM 1446 C CB . ASP A 1 171 ? 21.711 47.899 -4.009 1.00 43.91 ? 171 ASP A CB 1 ATOM 1447 C CG . ASP A 1 171 ? 22.344 48.329 -5.318 1.00 62.13 ? 171 ASP A CG 1 ATOM 1448 O OD1 . ASP A 1 171 ? 23.493 48.824 -5.288 1.00 65.56 ? 171 ASP A OD1 1 ATOM 1449 O OD2 . ASP A 1 171 ? 21.701 48.163 -6.376 1.00 69.99 ? 171 ASP A OD2 1 ATOM 1450 N N . GLU A 1 172 ? 21.535 46.048 -1.324 1.00 27.14 ? 172 GLU A N 1 ATOM 1451 C CA . GLU A 1 172 ? 21.043 45.830 0.025 1.00 27.74 ? 172 GLU A CA 1 ATOM 1452 C C . GLU A 1 172 ? 21.165 44.344 0.328 1.00 26.10 ? 172 GLU A C 1 ATOM 1453 O O . GLU A 1 172 ? 21.338 43.546 -0.589 1.00 27.87 ? 172 GLU A O 1 ATOM 1454 C CB . GLU A 1 172 ? 19.596 46.312 0.145 1.00 36.66 ? 172 GLU A CB 1 ATOM 1455 C CG . GLU A 1 172 ? 18.642 45.680 -0.847 1.00 50.11 ? 172 GLU A CG 1 ATOM 1456 C CD . GLU A 1 172 ? 17.365 46.475 -0.995 1.00 69.58 ? 172 GLU A CD 1 ATOM 1457 O OE1 . GLU A 1 172 ? 17.437 47.594 -1.547 1.00 77.96 ? 172 GLU A OE1 1 ATOM 1458 O OE2 . GLU A 1 172 ? 16.298 45.991 -0.553 1.00 74.56 ? 172 GLU A OE2 1 ATOM 1459 N N . PRO A 1 173 ? 21.101 43.965 1.617 1.00 27.48 ? 173 PRO A N 1 ATOM 1460 C CA . PRO A 1 173 ? 21.217 42.541 1.951 1.00 28.04 ? 173 PRO A CA 1 ATOM 1461 C C . PRO A 1 173 ? 20.129 41.717 1.257 1.00 24.18 ? 173 PRO A C 1 ATOM 1462 O O . PRO A 1 173 ? 19.003 42.189 1.054 1.00 25.55 ? 173 PRO A O 1 ATOM 1463 C CB . PRO A 1 173 ? 21.010 42.525 3.470 1.00 32.84 ? 173 PRO A CB 1 ATOM 1464 C CG . PRO A 1 173 ? 21.414 43.888 3.920 1.00 39.37 ? 173 PRO A CG 1 ATOM 1465 C CD . PRO A 1 173 ? 21.017 44.816 2.820 1.00 33.01 ? 173 PRO A CD 1 ATOM 1466 N N . LEU A 1 174 ? 20.472 40.500 0.877 1.00 21.56 ? 174 LEU A N 1 ATOM 1467 C CA . LEU A 1 174 ? 19.529 39.615 0.216 1.00 20.47 ? 174 LEU A CA 1 ATOM 1468 C C . LEU A 1 174 ? 18.987 38.653 1.257 1.00 20.84 ? 174 LEU A C 1 ATOM 1469 O O . LEU A 1 174 ? 19.760 37.982 1.940 1.00 24.53 ? 174 LEU A O 1 ATOM 1470 C CB . LEU A 1 174 ? 20.253 38.834 -0.883 1.00 20.93 ? 174 LEU A CB 1 ATOM 1471 C CG . LEU A 1 174 ? 19.458 37.977 -1.859 1.00 30.73 ? 174 LEU A CG 1 ATOM 1472 C CD1 . LEU A 1 174 ? 18.327 38.786 -2.479 1.00 36.00 ? 174 LEU A CD1 1 ATOM 1473 C CD2 . LEU A 1 174 ? 20.402 37.438 -2.937 1.00 31.19 ? 174 LEU A CD2 1 ATOM 1474 N N . LEU A 1 175 ? 17.669 38.589 1.400 1.00 22.35 ? 175 LEU A N 1 ATOM 1475 C CA . LEU A 1 175 ? 17.071 37.653 2.351 1.00 25.82 ? 175 LEU A CA 1 ATOM 1476 C C . LEU A 1 175 ? 16.307 36.576 1.612 1.00 26.14 ? 175 LEU A C 1 ATOM 1477 O O . LEU A 1 175 ? 15.454 36.875 0.784 1.00 26.03 ? 175 LEU A O 1 ATOM 1478 C CB . LEU A 1 175 ? 16.115 38.353 3.317 1.00 27.37 ? 175 LEU A CB 1 ATOM 1479 C CG . LEU A 1 175 ? 16.722 38.992 4.566 1.00 31.10 ? 175 LEU A CG 1 ATOM 1480 C CD1 . LEU A 1 175 ? 17.254 40.370 4.224 1.00 32.17 ? 175 LEU A CD1 1 ATOM 1481 C CD2 . LEU A 1 175 ? 15.692 39.064 5.680 1.00 39.09 ? 175 LEU A CD2 1 ATOM 1482 N N . LYS A 1 176 ? 16.609 35.322 1.923 1.00 19.89 ? 176 LYS A N 1 ATOM 1483 C CA . LYS A 1 176 ? 15.848 34.222 1.358 1.00 19.54 ? 176 LYS A CA 1 ATOM 1484 C C . LYS A 1 176 ? 15.142 33.518 2.498 1.00 20.97 ? 176 LYS A C 1 ATOM 1485 O O . LYS A 1 176 ? 15.764 33.144 3.496 1.00 20.31 ? 176 LYS A O 1 ATOM 1486 C CB . LYS A 1 176 ? 16.738 33.268 0.568 1.00 27.98 ? 176 LYS A CB 1 ATOM 1487 C CG . LYS A 1 176 ? 17.160 33.824 -0.790 1.00 36.37 ? 176 LYS A CG 1 ATOM 1488 C CD . LYS A 1 176 ? 15.965 34.102 -1.687 1.00 38.42 ? 176 LYS A CD 1 ATOM 1489 C CE . LYS A 1 176 ? 16.213 35.306 -2.584 1.00 43.31 ? 176 LYS A CE 1 ATOM 1490 N NZ . LYS A 1 176 ? 16.624 34.939 -3.966 1.00 48.90 ? 176 LYS A NZ 1 ATOM 1491 N N . HIS A 1 177 ? 13.837 33.364 2.334 1.00 25.77 ? 177 HIS A N 1 ATOM 1492 C CA . HIS A 1 177 ? 12.926 32.956 3.395 1.00 24.40 ? 177 HIS A CA 1 ATOM 1493 C C . HIS A 1 177 ? 12.677 31.452 3.360 1.00 28.00 ? 177 HIS A C 1 ATOM 1494 O O . HIS A 1 177 ? 12.758 30.809 2.301 1.00 25.00 ? 177 HIS A O 1 ATOM 1495 C CB . HIS A 1 177 ? 11.607 33.703 3.176 1.00 28.40 ? 177 HIS A CB 1 ATOM 1496 C CG . HIS A 1 177 ? 10.658 33.654 4.334 1.00 37.79 ? 177 HIS A CG 1 ATOM 1497 N ND1 . HIS A 1 177 ? 10.851 34.382 5.487 1.00 37.63 ? 177 HIS A ND1 1 ATOM 1498 C CD2 . HIS A 1 177 ? 9.482 32.999 4.494 1.00 38.19 ? 177 HIS A CD2 1 ATOM 1499 C CE1 . HIS A 1 177 ? 9.840 34.171 6.313 1.00 38.44 ? 177 HIS A CE1 1 ATOM 1500 N NE2 . HIS A 1 177 ? 9.000 33.328 5.738 1.00 37.69 ? 177 HIS A NE2 1 ATOM 1501 N N . TRP A 1 178 ? 12.377 30.888 4.524 1.00 27.62 ? 178 TRP A N 1 ATOM 1502 C CA . TRP A 1 178 ? 11.864 29.528 4.600 1.00 24.31 ? 178 TRP A CA 1 ATOM 1503 C C . TRP A 1 178 ? 10.840 29.441 5.722 1.00 29.30 ? 178 TRP A C 1 ATOM 1504 O O . TRP A 1 178 ? 11.052 29.993 6.803 1.00 23.28 ? 178 TRP A O 1 ATOM 1505 C CB . TRP A 1 178 ? 12.982 28.502 4.835 1.00 24.77 ? 178 TRP A CB 1 ATOM 1506 C CG . TRP A 1 178 ? 12.449 27.087 4.837 1.00 24.81 ? 178 TRP A CG 1 ATOM 1507 C CD1 . TRP A 1 178 ? 12.364 26.239 3.769 1.00 32.90 ? 178 TRP A CD1 1 ATOM 1508 C CD2 . TRP A 1 178 ? 11.876 26.388 5.949 1.00 23.81 ? 178 TRP A CD2 1 ATOM 1509 N NE1 . TRP A 1 178 ? 11.788 25.049 4.152 1.00 29.73 ? 178 TRP A NE1 1 ATOM 1510 C CE2 . TRP A 1 178 ? 11.480 25.114 5.485 1.00 27.35 ? 178 TRP A CE2 1 ATOM 1511 C CE3 . TRP A 1 178 ? 11.670 26.710 7.297 1.00 28.79 ? 178 TRP A CE3 1 ATOM 1512 C CZ2 . TRP A 1 178 ? 10.888 24.165 6.318 1.00 27.22 ? 178 TRP A CZ2 1 ATOM 1513 C CZ3 . TRP A 1 178 ? 11.074 25.764 8.122 1.00 29.14 ? 178 TRP A CZ3 1 ATOM 1514 C CH2 . TRP A 1 178 ? 10.695 24.507 7.628 1.00 26.03 ? 178 TRP A CH2 1 ATOM 1515 N N . GLU A 1 179 ? 9.727 28.765 5.460 1.00 26.43 ? 179 GLU A N 1 ATOM 1516 C CA . GLU A 1 179 ? 8.796 28.412 6.526 1.00 32.29 ? 179 GLU A CA 1 ATOM 1517 C C . GLU A 1 179 ? 8.059 27.108 6.226 1.00 35.91 ? 179 GLU A C 1 ATOM 1518 O O . GLU A 1 179 ? 8.043 26.635 5.086 1.00 36.86 ? 179 GLU A O 1 ATOM 1519 C CB . GLU A 1 179 ? 7.826 29.554 6.839 1.00 31.58 ? 179 GLU A CB 1 ATOM 1520 C CG . GLU A 1 179 ? 6.899 29.951 5.710 1.00 37.54 ? 179 GLU A CG 1 ATOM 1521 C CD . GLU A 1 179 ? 6.040 31.151 6.071 1.00 45.32 ? 179 GLU A CD 1 ATOM 1522 O OE1 . GLU A 1 179 ? 6.523 32.295 5.930 1.00 47.48 ? 179 GLU A OE1 1 ATOM 1523 O OE2 . GLU A 1 179 ? 4.887 30.952 6.506 1.00 48.65 ? 179 GLU A OE2 1 ATOM 1524 N N . PHE A 1 180 ? 7.462 26.532 7.262 1.00 31.94 ? 180 PHE A N 1 ATOM 1525 C CA . PHE A 1 180 ? 6.796 25.238 7.154 1.00 41.41 ? 180 PHE A CA 1 ATOM 1526 C C . PHE A 1 180 ? 5.545 25.329 6.276 1.00 48.44 ? 180 PHE A C 1 ATOM 1527 O O . PHE A 1 180 ? 4.899 26.375 6.238 1.00 47.65 ? 180 PHE A O 1 ATOM 1528 C CB . PHE A 1 180 ? 6.452 24.723 8.551 1.00 42.91 ? 180 PHE A CB 1 ATOM 1529 C CG . PHE A 1 180 ? 5.842 23.353 8.565 1.00 45.96 ? 180 PHE A CG 1 ATOM 1530 C CD1 . PHE A 1 180 ? 6.635 22.224 8.421 1.00 36.98 ? 180 PHE A CD1 1 ATOM 1531 C CD2 . PHE A 1 180 ? 4.476 23.191 8.745 1.00 53.70 ? 180 PHE A CD2 1 ATOM 1532 C CE1 . PHE A 1 180 ? 6.074 20.960 8.444 1.00 37.57 ? 180 PHE A CE1 1 ATOM 1533 C CE2 . PHE A 1 180 ? 3.911 21.927 8.770 1.00 54.49 ? 180 PHE A CE2 1 ATOM 1534 C CZ . PHE A 1 180 ? 4.714 20.813 8.615 1.00 46.96 ? 180 PHE A CZ 1 ATOM 1535 N N . ASP A 1 181 ? 5.249 24.224 5.582 1.00 60.82 ? 181 ASP A N 1 ATOM 1536 C CA . ASP A 1 181 ? 4.121 24.029 4.635 1.00 77.59 ? 181 ASP A CA 1 ATOM 1537 C C . ASP A 1 181 ? 4.570 24.102 3.174 1.00 76.29 ? 181 ASP A C 1 ATOM 1538 O O . ASP A 1 181 ? 3.825 23.716 2.269 1.00 79.29 ? 181 ASP A O 1 ATOM 1539 C CB . ASP A 1 181 ? 2.916 24.962 4.868 1.00 83.87 ? 181 ASP A CB 1 ATOM 1540 C CG . ASP A 1 181 ? 1.736 24.257 5.512 1.00 88.30 ? 181 ASP A CG 1 ATOM 1541 O OD1 . ASP A 1 181 ? 0.976 23.571 4.792 1.00 91.74 ? 181 ASP A OD1 1 ATOM 1542 O OD2 . ASP A 1 181 ? 1.552 24.412 6.738 1.00 88.50 ? 181 ASP A OD2 1 ATOM 1543 N N . ASP B 2 4 ? 32.247 49.397 2.575 1.00 68.04 ? 2 ASP B N 1 ATOM 1544 C CA . ASP B 2 4 ? 33.608 49.351 2.040 1.00 61.16 ? 2 ASP B CA 1 ATOM 1545 C C . ASP B 2 4 ? 33.570 49.410 0.520 1.00 58.73 ? 2 ASP B C 1 ATOM 1546 O O . ASP B 2 4 ? 33.072 48.498 -0.136 1.00 65.76 ? 2 ASP B O 1 ATOM 1547 C CB . ASP B 2 4 ? 34.320 48.087 2.502 1.00 59.57 ? 2 ASP B CB 1 ATOM 1548 C CG . ASP B 2 4 ? 35.842 48.196 2.421 1.00 54.92 ? 2 ASP B CG 1 ATOM 1549 O OD1 . ASP B 2 4 ? 36.357 49.058 1.671 1.00 47.70 ? 2 ASP B OD1 1 ATOM 1550 O OD2 . ASP B 2 4 ? 36.519 47.404 3.122 1.00 54.98 ? 2 ASP B OD2 1 ATOM 1551 N N . THR B 2 5 ? 34.120 50.479 -0.042 1.00 48.69 ? 3 THR B N 1 ATOM 1552 C CA . THR B 2 5 ? 34.192 50.597 -1.493 1.00 44.91 ? 3 THR B CA 1 ATOM 1553 C C . THR B 2 5 ? 35.617 50.567 -2.048 1.00 39.84 ? 3 THR B C 1 ATOM 1554 O O . THR B 2 5 ? 35.824 50.795 -3.242 1.00 45.70 ? 3 THR B O 1 ATOM 1555 C CB . THR B 2 5 ? 33.470 51.844 -2.009 1.00 47.97 ? 3 THR B CB 1 ATOM 1556 O OG1 . THR B 2 5 ? 34.040 53.006 -1.400 1.00 47.54 ? 3 THR B OG1 1 ATOM 1557 C CG2 . THR B 2 5 ? 31.988 51.770 -1.688 1.00 50.99 ? 3 THR B CG2 1 ATOM 1558 N N . ARG B 2 6 ? 36.595 50.285 -1.193 1.00 32.21 ? 4 ARG B N 1 ATOM 1559 C CA . ARG B 2 6 ? 37.957 50.082 -1.682 1.00 32.46 ? 4 ARG B CA 1 ATOM 1560 C C . ARG B 2 6 ? 37.981 49.027 -2.792 1.00 28.68 ? 4 ARG B C 1 ATOM 1561 O O . ARG B 2 6 ? 37.278 48.016 -2.720 1.00 29.49 ? 4 ARG B O 1 ATOM 1562 C CB . ARG B 2 6 ? 38.891 49.668 -0.546 1.00 29.92 ? 4 ARG B CB 1 ATOM 1563 C CG . ARG B 2 6 ? 39.109 50.767 0.495 1.00 40.27 ? 4 ARG B CG 1 ATOM 1564 C CD . ARG B 2 6 ? 40.036 50.274 1.593 1.00 42.57 ? 4 ARG B CD 1 ATOM 1565 N NE . ARG B 2 6 ? 39.456 49.140 2.308 1.00 44.92 ? 4 ARG B NE 1 ATOM 1566 C CZ . ARG B 2 6 ? 40.149 48.309 3.079 1.00 47.04 ? 4 ARG B CZ 1 ATOM 1567 N NH1 . ARG B 2 6 ? 41.457 48.479 3.226 1.00 44.80 ? 4 ARG B NH1 1 ATOM 1568 N NH2 . ARG B 2 6 ? 39.536 47.305 3.694 1.00 46.05 ? 4 ARG B NH2 1 ATOM 1569 N N . PRO B 2 7 ? 38.775 49.275 -3.841 1.00 25.13 ? 5 PRO B N 1 ATOM 1570 C CA . PRO B 2 7 ? 38.894 48.295 -4.921 1.00 25.84 ? 5 PRO B CA 1 ATOM 1571 C C . PRO B 2 7 ? 39.549 47.009 -4.435 1.00 25.30 ? 5 PRO B C 1 ATOM 1572 O O . PRO B 2 7 ? 40.454 47.061 -3.602 1.00 24.20 ? 5 PRO B O 1 ATOM 1573 C CB . PRO B 2 7 ? 39.793 49.003 -5.943 1.00 22.71 ? 5 PRO B CB 1 ATOM 1574 C CG . PRO B 2 7 ? 40.477 50.096 -5.177 1.00 30.88 ? 5 PRO B CG 1 ATOM 1575 C CD . PRO B 2 7 ? 39.505 50.523 -4.133 1.00 25.15 ? 5 PRO B CD 1 ATOM 1576 N N . ARG B 2 8 ? 39.088 45.873 -4.946 1.00 20.29 ? 6 ARG B N 1 ATOM 1577 C CA . ARG B 2 8 ? 39.699 44.592 -4.615 1.00 19.15 ? 6 ARG B CA 1 ATOM 1578 C C . ARG B 2 8 ? 40.466 44.036 -5.803 1.00 24.23 ? 6 ARG B C 1 ATOM 1579 O O . ARG B 2 8 ? 40.158 44.328 -6.959 1.00 21.99 ? 6 ARG B O 1 ATOM 1580 C CB . ARG B 2 8 ? 38.648 43.576 -4.157 1.00 19.01 ? 6 ARG B CB 1 ATOM 1581 C CG . ARG B 2 8 ? 38.529 43.409 -2.641 1.00 24.09 ? 6 ARG B CG 1 ATOM 1582 C CD . ARG B 2 8 ? 37.987 44.659 -1.971 1.00 24.90 ? 6 ARG B CD 1 ATOM 1583 N NE . ARG B 2 8 ? 38.009 44.557 -0.511 1.00 22.43 ? 6 ARG B NE 1 ATOM 1584 C CZ . ARG B 2 8 ? 37.597 45.519 0.303 1.00 24.03 ? 6 ARG B CZ 1 ATOM 1585 N NH1 . ARG B 2 8 ? 37.117 46.650 -0.200 1.00 24.76 ? 6 ARG B NH1 1 ATOM 1586 N NH2 . ARG B 2 8 ? 37.646 45.346 1.618 1.00 31.64 ? 6 ARG B NH2 1 ATOM 1587 N N . PHE B 2 9 ? 41.458 43.209 -5.502 1.00 21.24 ? 7 PHE B N 1 ATOM 1588 C CA . PHE B 2 9 ? 42.285 42.570 -6.514 1.00 16.15 ? 7 PHE B CA 1 ATOM 1589 C C . PHE B 2 9 ? 42.471 41.139 -6.054 1.00 15.33 ? 7 PHE B C 1 ATOM 1590 O O . PHE B 2 9 ? 42.783 40.893 -4.893 1.00 17.36 ? 7 PHE B O 1 ATOM 1591 C CB . PHE B 2 9 ? 43.634 43.294 -6.622 1.00 16.50 ? 7 PHE B CB 1 ATOM 1592 C CG . PHE B 2 9 ? 43.503 44.790 -6.765 1.00 21.72 ? 7 PHE B CG 1 ATOM 1593 C CD1 . PHE B 2 9 ? 43.393 45.377 -8.017 1.00 17.87 ? 7 PHE B CD1 1 ATOM 1594 C CD2 . PHE B 2 9 ? 43.479 45.610 -5.644 1.00 23.82 ? 7 PHE B CD2 1 ATOM 1595 C CE1 . PHE B 2 9 ? 43.285 46.766 -8.151 1.00 19.17 ? 7 PHE B CE1 1 ATOM 1596 C CE2 . PHE B 2 9 ? 43.353 46.992 -5.772 1.00 26.90 ? 7 PHE B CE2 1 ATOM 1597 C CZ . PHE B 2 9 ? 43.253 47.566 -7.032 1.00 20.77 ? 7 PHE B CZ 1 ATOM 1598 N N . LEU B 2 10 ? 42.247 40.190 -6.954 1.00 14.45 ? 8 LEU B N 1 ATOM 1599 C CA . LEU B 2 10 ? 42.240 38.773 -6.590 1.00 16.62 ? 8 LEU B CA 1 ATOM 1600 C C . LEU B 2 10 ? 43.196 37.973 -7.460 1.00 16.64 ? 8 LEU B C 1 ATOM 1601 O O . LEU B 2 10 ? 43.222 38.150 -8.676 1.00 16.71 ? 8 LEU B O 1 ATOM 1602 C CB . LEU B 2 10 ? 40.825 38.205 -6.775 1.00 13.86 ? 8 LEU B CB 1 ATOM 1603 C CG . LEU B 2 10 ? 40.603 36.717 -6.485 1.00 17.82 ? 8 LEU B CG 1 ATOM 1604 C CD1 . LEU B 2 10 ? 40.656 36.472 -4.978 1.00 15.50 ? 8 LEU B CD1 1 ATOM 1605 C CD2 . LEU B 2 10 ? 39.255 36.259 -7.066 1.00 18.83 ? 8 LEU B CD2 1 ATOM 1606 N N . GLU B 2 11 ? 43.957 37.080 -6.835 1.00 12.68 ? 9 GLU B N 1 ATOM 1607 C CA . GLU B 2 11 ? 44.822 36.154 -7.550 1.00 15.64 ? 9 GLU B CA 1 ATOM 1608 C C . GLU B 2 11 ? 44.266 34.767 -7.241 1.00 16.35 ? 9 GLU B C 1 ATOM 1609 O O . GLU B 2 11 ? 43.966 34.475 -6.082 1.00 15.82 ? 9 GLU B O 1 ATOM 1610 C CB . GLU B 2 11 ? 46.262 36.261 -7.007 1.00 14.21 ? 9 GLU B CB 1 ATOM 1611 C CG . GLU B 2 11 ? 47.243 35.206 -7.553 1.00 14.32 ? 9 GLU B CG 1 ATOM 1612 C CD . GLU B 2 11 ? 47.711 35.515 -8.969 1.00 18.49 ? 9 GLU B CD 1 ATOM 1613 O OE1 . GLU B 2 11 ? 47.553 36.679 -9.389 1.00 17.63 ? 9 GLU B OE1 1 ATOM 1614 O OE2 . GLU B 2 11 ? 48.236 34.604 -9.664 1.00 18.22 ? 9 GLU B OE2 1 ATOM 1615 N N . GLN B 2 12 ? 44.105 33.918 -8.254 1.00 14.39 ? 10 GLN B N 1 ATOM 1616 C CA . GLN B 2 12 ? 43.729 32.524 -8.002 1.00 11.87 ? 10 GLN B CA 1 ATOM 1617 C C . GLN B 2 12 ? 44.710 31.585 -8.680 1.00 16.29 ? 10 GLN B C 1 ATOM 1618 O O . GLN B 2 12 ? 45.286 31.926 -9.707 1.00 15.04 ? 10 GLN B O 1 ATOM 1619 C CB . GLN B 2 12 ? 42.328 32.180 -8.533 1.00 12.39 ? 10 GLN B CB 1 ATOM 1620 C CG . GLN B 2 12 ? 41.197 33.113 -8.112 1.00 11.66 ? 10 GLN B CG 1 ATOM 1621 C CD . GLN B 2 12 ? 39.857 32.535 -8.492 1.00 17.94 ? 10 GLN B CD 1 ATOM 1622 O OE1 . GLN B 2 12 ? 39.524 31.408 -8.099 1.00 17.94 ? 10 GLN B OE1 1 ATOM 1623 N NE2 . GLN B 2 12 ? 39.082 33.283 -9.281 1.00 15.10 ? 10 GLN B NE2 1 ATOM 1624 N N . VAL B 2 13 ? 44.879 30.397 -8.099 1.00 14.19 ? 11 VAL B N 1 ATOM 1625 C CA . VAL B 2 13 ? 45.634 29.328 -8.732 1.00 11.89 ? 11 VAL B CA 1 ATOM 1626 C C . VAL B 2 13 ? 44.829 28.044 -8.593 1.00 14.49 ? 11 VAL B C 1 ATOM 1627 O O . VAL B 2 13 ? 44.270 27.760 -7.526 1.00 15.41 ? 11 VAL B O 1 ATOM 1628 C CB . VAL B 2 13 ? 47.026 29.125 -8.090 1.00 14.82 ? 11 VAL B CB 1 ATOM 1629 C CG1 . VAL B 2 13 ? 47.838 28.082 -8.877 1.00 14.56 ? 11 VAL B CG1 1 ATOM 1630 C CG2 . VAL B 2 13 ? 47.798 30.457 -8.007 1.00 10.98 ? 11 VAL B CG2 1 ATOM 1631 N N . LYS B 2 14 ? 44.755 27.286 -9.681 1.00 11.67 ? 12 LYS B N 1 ATOM 1632 C CA . LYS B 2 14 ? 44.094 25.990 -9.674 1.00 13.11 ? 12 LYS B CA 1 ATOM 1633 C C . LYS B 2 14 ? 45.028 24.996 -10.317 1.00 15.42 ? 12 LYS B C 1 ATOM 1634 O O . LYS B 2 14 ? 45.336 25.106 -11.512 1.00 15.98 ? 12 LYS B O 1 ATOM 1635 C CB . LYS B 2 14 ? 42.758 26.046 -10.444 1.00 12.37 ? 12 LYS B CB 1 ATOM 1636 C CG . LYS B 2 14 ? 41.745 26.994 -9.786 1.00 12.14 ? 12 LYS B CG 1 ATOM 1637 C CD . LYS B 2 14 ? 40.399 27.029 -10.510 1.00 14.69 ? 12 LYS B CD 1 ATOM 1638 C CE . LYS B 2 14 ? 39.418 27.917 -9.749 1.00 14.34 ? 12 LYS B CE 1 ATOM 1639 N NZ . LYS B 2 14 ? 38.077 27.996 -10.416 1.00 13.99 ? 12 LYS B NZ 1 ATOM 1640 N N . HIS B 2 15 ? 45.496 24.045 -9.516 1.00 14.24 ? 13 HIS B N 1 ATOM 1641 C CA . HIS B 2 15 ? 46.364 22.993 -10.006 1.00 15.37 ? 13 HIS B CA 1 ATOM 1642 C C . HIS B 2 15 ? 45.437 21.809 -10.213 1.00 17.12 ? 13 HIS B C 1 ATOM 1643 O O . HIS B 2 15 ? 45.004 21.192 -9.236 1.00 15.01 ? 13 HIS B O 1 ATOM 1644 C CB . HIS B 2 15 ? 47.431 22.614 -8.960 1.00 13.53 ? 13 HIS B CB 1 ATOM 1645 C CG . HIS B 2 15 ? 48.075 23.782 -8.266 1.00 18.59 ? 13 HIS B CG 1 ATOM 1646 N ND1 . HIS B 2 15 ? 49.180 24.436 -8.770 1.00 17.88 ? 13 HIS B ND1 1 ATOM 1647 C CD2 . HIS B 2 15 ? 47.797 24.379 -7.081 1.00 17.51 ? 13 HIS B CD2 1 ATOM 1648 C CE1 . HIS B 2 15 ? 49.550 25.386 -7.928 1.00 14.30 ? 13 HIS B CE1 1 ATOM 1649 N NE2 . HIS B 2 15 ? 48.725 25.373 -6.893 1.00 17.85 ? 13 HIS B NE2 1 ATOM 1650 N N . GLU B 2 16 ? 45.109 21.511 -11.470 1.00 16.77 ? 14 GLU B N 1 ATOM 1651 C CA . GLU B 2 16 ? 44.079 20.521 -11.773 1.00 16.58 ? 14 GLU B CA 1 ATOM 1652 C C . GLU B 2 16 ? 44.662 19.185 -12.232 1.00 21.79 ? 14 GLU B C 1 ATOM 1653 O O . GLU B 2 16 ? 45.567 19.146 -13.069 1.00 19.03 ? 14 GLU B O 1 ATOM 1654 C CB . GLU B 2 16 ? 43.115 21.044 -12.845 1.00 11.85 ? 14 GLU B CB 1 ATOM 1655 C CG . GLU B 2 16 ? 42.541 22.421 -12.536 1.00 13.44 ? 14 GLU B CG 1 ATOM 1656 C CD . GLU B 2 16 ? 41.490 22.835 -13.539 1.00 17.48 ? 14 GLU B CD 1 ATOM 1657 O OE1 . GLU B 2 16 ? 41.300 22.120 -14.553 1.00 16.74 ? 14 GLU B OE1 1 ATOM 1658 O OE2 . GLU B 2 16 ? 40.849 23.872 -13.314 1.00 19.52 ? 14 GLU B OE2 1 ATOM 1659 N N . CYS B 2 17 ? 44.123 18.102 -11.676 1.00 13.19 ? 15 CYS B N 1 ATOM 1660 C CA . CYS B 2 17 ? 44.433 16.753 -12.129 1.00 17.94 ? 15 CYS B CA 1 ATOM 1661 C C . CYS B 2 17 ? 43.193 16.111 -12.719 1.00 17.88 ? 15 CYS B C 1 ATOM 1662 O O . CYS B 2 17 ? 42.178 15.975 -12.032 1.00 16.39 ? 15 CYS B O 1 ATOM 1663 C CB . CYS B 2 17 ? 44.950 15.910 -10.968 1.00 16.90 ? 15 CYS B CB 1 ATOM 1664 S SG . CYS B 2 17 ? 46.547 16.487 -10.408 1.00 19.92 ? 15 CYS B SG 1 ATOM 1665 N N . HIS B 2 18 ? 43.277 15.720 -13.988 1.00 19.43 ? 16 HIS B N 1 ATOM 1666 C CA . HIS B 2 18 ? 42.138 15.133 -14.694 1.00 21.48 ? 16 HIS B CA 1 ATOM 1667 C C . HIS B 2 18 ? 42.354 13.643 -14.974 1.00 18.40 ? 16 HIS B C 1 ATOM 1668 O O . HIS B 2 18 ? 43.306 13.271 -15.655 1.00 20.40 ? 16 HIS B O 1 ATOM 1669 C CB . HIS B 2 18 ? 41.881 15.878 -16.007 1.00 21.95 ? 16 HIS B CB 1 ATOM 1670 C CG . HIS B 2 18 ? 41.525 17.322 -15.823 1.00 23.06 ? 16 HIS B CG 1 ATOM 1671 N ND1 . HIS B 2 18 ? 40.271 17.820 -16.098 1.00 22.45 ? 16 HIS B ND1 1 ATOM 1672 C CD2 . HIS B 2 18 ? 42.255 18.371 -15.379 1.00 23.10 ? 16 HIS B CD2 1 ATOM 1673 C CE1 . HIS B 2 18 ? 40.246 19.117 -15.842 1.00 23.75 ? 16 HIS B CE1 1 ATOM 1674 N NE2 . HIS B 2 18 ? 41.438 19.476 -15.400 1.00 18.57 ? 16 HIS B NE2 1 ATOM 1675 N N . PHE B 2 19 ? 41.464 12.804 -14.453 1.00 18.36 ? 17 PHE B N 1 ATOM 1676 C CA . PHE B 2 19 ? 41.630 11.356 -14.550 1.00 21.65 ? 17 PHE B CA 1 ATOM 1677 C C . PHE B 2 19 ? 40.630 10.708 -15.501 1.00 26.14 ? 17 PHE B C 1 ATOM 1678 O O . PHE B 2 19 ? 39.436 11.017 -15.466 1.00 27.66 ? 17 PHE B O 1 ATOM 1679 C CB . PHE B 2 19 ? 41.528 10.726 -13.158 1.00 23.17 ? 17 PHE B CB 1 ATOM 1680 C CG . PHE B 2 19 ? 42.501 11.310 -12.170 1.00 23.78 ? 17 PHE B CG 1 ATOM 1681 C CD1 . PHE B 2 19 ? 43.779 10.771 -12.033 1.00 22.93 ? 17 PHE B CD1 1 ATOM 1682 C CD2 . PHE B 2 19 ? 42.152 12.409 -11.400 1.00 18.57 ? 17 PHE B CD2 1 ATOM 1683 C CE1 . PHE B 2 19 ? 44.684 11.315 -11.135 1.00 19.22 ? 17 PHE B CE1 1 ATOM 1684 C CE2 . PHE B 2 19 ? 43.040 12.956 -10.499 1.00 17.87 ? 17 PHE B CE2 1 ATOM 1685 C CZ . PHE B 2 19 ? 44.325 12.411 -10.368 1.00 18.99 ? 17 PHE B CZ 1 ATOM 1686 N N . PHE B 2 20 ? 41.137 9.813 -16.349 1.00 24.90 ? 18 PHE B N 1 ATOM 1687 C CA . PHE B 2 20 ? 40.321 9.062 -17.299 1.00 29.02 ? 18 PHE B CA 1 ATOM 1688 C C . PHE B 2 20 ? 40.607 7.578 -17.104 1.00 29.38 ? 18 PHE B C 1 ATOM 1689 O O . PHE B 2 20 ? 41.756 7.152 -17.261 1.00 27.51 ? 18 PHE B O 1 ATOM 1690 C CB . PHE B 2 20 ? 40.684 9.445 -18.739 1.00 33.43 ? 18 PHE B CB 1 ATOM 1691 C CG . PHE B 2 20 ? 40.711 10.934 -18.997 1.00 43.83 ? 18 PHE B CG 1 ATOM 1692 C CD1 . PHE B 2 20 ? 39.561 11.607 -19.388 1.00 53.48 ? 18 PHE B CD1 1 ATOM 1693 C CD2 . PHE B 2 20 ? 41.894 11.660 -18.870 1.00 41.58 ? 18 PHE B CD2 1 ATOM 1694 C CE1 . PHE B 2 20 ? 39.587 12.983 -19.629 1.00 54.19 ? 18 PHE B CE1 1 ATOM 1695 C CE2 . PHE B 2 20 ? 41.925 13.027 -19.110 1.00 42.39 ? 18 PHE B CE2 1 ATOM 1696 C CZ . PHE B 2 20 ? 40.769 13.688 -19.487 1.00 46.86 ? 18 PHE B CZ 1 ATOM 1697 N N . ASN B 2 21 ? 39.586 6.792 -16.771 1.00 33.88 ? 19 ASN B N 1 ATOM 1698 C CA . ASN B 2 21 ? 39.771 5.356 -16.546 1.00 41.41 ? 19 ASN B CA 1 ATOM 1699 C C . ASN B 2 21 ? 40.802 5.162 -15.432 1.00 39.94 ? 19 ASN B C 1 ATOM 1700 O O . ASN B 2 21 ? 41.860 4.576 -15.635 1.00 34.47 ? 19 ASN B O 1 ATOM 1701 C CB . ASN B 2 21 ? 40.188 4.668 -17.857 1.00 49.85 ? 19 ASN B CB 1 ATOM 1702 C CG . ASN B 2 21 ? 40.445 3.174 -17.708 1.00 64.85 ? 19 ASN B CG 1 ATOM 1703 O OD1 . ASN B 2 21 ? 39.906 2.515 -16.816 1.00 62.12 ? 19 ASN B OD1 1 ATOM 1704 N ND2 . ASN B 2 21 ? 41.289 2.636 -18.597 1.00 80.81 ? 19 ASN B ND2 1 ATOM 1705 N N . GLY B 2 22 ? 40.492 5.693 -14.254 1.00 48.67 ? 20 GLY B N 1 ATOM 1706 C CA . GLY B 2 22 ? 41.409 5.649 -13.128 1.00 50.74 ? 20 GLY B CA 1 ATOM 1707 C C . GLY B 2 22 ? 42.646 6.486 -13.374 1.00 44.28 ? 20 GLY B C 1 ATOM 1708 O O . GLY B 2 22 ? 42.551 7.662 -13.707 1.00 44.16 ? 20 GLY B O 1 ATOM 1709 N N . THR B 2 23 ? 43.818 5.881 -13.216 1.00 36.44 ? 21 THR B N 1 ATOM 1710 C CA . THR B 2 23 ? 45.062 6.594 -13.474 1.00 34.25 ? 21 THR B CA 1 ATOM 1711 C C . THR B 2 23 ? 45.674 6.136 -14.788 1.00 35.40 ? 21 THR B C 1 ATOM 1712 O O . THR B 2 23 ? 46.860 6.362 -15.051 1.00 31.41 ? 21 THR B O 1 ATOM 1713 C CB . THR B 2 23 ? 46.081 6.410 -12.330 1.00 33.42 ? 21 THR B CB 1 ATOM 1714 O OG1 . THR B 2 23 ? 46.320 5.019 -12.109 1.00 33.34 ? 21 THR B OG1 1 ATOM 1715 C CG2 . THR B 2 23 ? 45.552 7.017 -11.050 1.00 38.26 ? 21 THR B CG2 1 ATOM 1716 N N . GLU B 2 24 ? 44.864 5.488 -15.620 1.00 33.85 ? 22 GLU B N 1 ATOM 1717 C CA . GLU B 2 24 ? 45.368 5.001 -16.897 1.00 31.22 ? 22 GLU B CA 1 ATOM 1718 C C . GLU B 2 24 ? 45.713 6.159 -17.825 1.00 31.45 ? 22 GLU B C 1 ATOM 1719 O O . GLU B 2 24 ? 46.740 6.136 -18.497 1.00 32.87 ? 22 GLU B O 1 ATOM 1720 C CB . GLU B 2 24 ? 44.379 4.045 -17.562 1.00 45.55 ? 22 GLU B CB 1 ATOM 1721 C CG . GLU B 2 24 ? 45.040 3.015 -18.468 1.00 57.74 ? 22 GLU B CG 1 ATOM 1722 C CD . GLU B 2 24 ? 45.805 1.930 -17.707 1.00 68.69 ? 22 GLU B CD 1 ATOM 1723 O OE1 . GLU B 2 24 ? 45.855 1.974 -16.455 1.00 66.32 ? 22 GLU B OE1 1 ATOM 1724 O OE2 . GLU B 2 24 ? 46.353 1.021 -18.372 1.00 75.97 ? 22 GLU B OE2 1 ATOM 1725 N N . ARG B 2 25 ? 44.869 7.183 -17.844 1.00 23.14 ? 23 ARG B N 1 ATOM 1726 C CA . ARG B 2 25 ? 45.164 8.374 -18.627 1.00 27.97 ? 23 ARG B CA 1 ATOM 1727 C C . ARG B 2 25 ? 44.972 9.594 -17.742 1.00 26.96 ? 23 ARG B C 1 ATOM 1728 O O . ARG B 2 25 ? 43.925 9.755 -17.121 1.00 23.28 ? 23 ARG B O 1 ATOM 1729 C CB . ARG B 2 25 ? 44.290 8.438 -19.880 1.00 33.83 ? 23 ARG B CB 1 ATOM 1730 C CG . ARG B 2 25 ? 44.649 9.577 -20.811 1.00 49.16 ? 23 ARG B CG 1 ATOM 1731 C CD . ARG B 2 25 ? 44.225 9.291 -22.248 1.00 66.38 ? 23 ARG B CD 1 ATOM 1732 N NE . ARG B 2 25 ? 43.558 10.449 -22.838 1.00 78.55 ? 23 ARG B NE 1 ATOM 1733 C CZ . ARG B 2 25 ? 42.237 10.595 -22.901 1.00 85.45 ? 23 ARG B CZ 1 ATOM 1734 N NH1 . ARG B 2 25 ? 41.710 11.688 -23.444 1.00 84.99 ? 23 ARG B NH1 1 ATOM 1735 N NH2 . ARG B 2 25 ? 41.441 9.644 -22.425 1.00 88.26 ? 23 ARG B NH2 1 ATOM 1736 N N . VAL B 2 26 ? 46.004 10.428 -17.637 1.00 25.50 ? 24 VAL B N 1 ATOM 1737 C CA . VAL B 2 26 ? 45.974 11.538 -16.687 1.00 22.08 ? 24 VAL B CA 1 ATOM 1738 C C . VAL B 2 26 ? 46.504 12.826 -17.318 1.00 21.89 ? 24 VAL B C 1 ATOM 1739 O O . VAL B 2 26 ? 47.505 12.819 -18.023 1.00 23.14 ? 24 VAL B O 1 ATOM 1740 C CB . VAL B 2 26 ? 46.778 11.217 -15.393 1.00 23.20 ? 24 VAL B CB 1 ATOM 1741 C CG1 . VAL B 2 26 ? 46.731 12.388 -14.419 1.00 21.74 ? 24 VAL B CG1 1 ATOM 1742 C CG2 . VAL B 2 26 ? 46.257 9.938 -14.726 1.00 22.03 ? 24 VAL B CG2 1 ATOM 1743 N N . ARG B 2 27 ? 45.797 13.924 -17.088 1.00 20.34 ? 25 ARG B N 1 ATOM 1744 C CA . ARG B 2 27 ? 46.204 15.227 -17.603 1.00 19.42 ? 25 ARG B CA 1 ATOM 1745 C C . ARG B 2 27 ? 46.295 16.240 -16.473 1.00 20.90 ? 25 ARG B C 1 ATOM 1746 O O . ARG B 2 27 ? 45.382 16.345 -15.650 1.00 18.19 ? 25 ARG B O 1 ATOM 1747 C CB . ARG B 2 27 ? 45.202 15.713 -18.645 1.00 20.64 ? 25 ARG B CB 1 ATOM 1748 C CG . ARG B 2 27 ? 45.418 17.139 -19.106 1.00 24.69 ? 25 ARG B CG 1 ATOM 1749 C CD . ARG B 2 27 ? 44.570 17.414 -20.349 1.00 28.41 ? 25 ARG B CD 1 ATOM 1750 N NE . ARG B 2 27 ? 44.690 18.791 -20.822 1.00 31.51 ? 25 ARG B NE 1 ATOM 1751 C CZ . ARG B 2 27 ? 43.713 19.687 -20.739 1.00 42.82 ? 25 ARG B CZ 1 ATOM 1752 N NH1 . ARG B 2 27 ? 42.541 19.346 -20.209 1.00 41.73 ? 25 ARG B NH1 1 ATOM 1753 N NH2 . ARG B 2 27 ? 43.902 20.920 -21.188 1.00 42.49 ? 25 ARG B NH2 1 ATOM 1754 N N . PHE B 2 28 ? 47.403 16.978 -16.444 1.00 17.05 ? 26 PHE B N 1 ATOM 1755 C CA . PHE B 2 28 ? 47.670 17.968 -15.415 1.00 17.79 ? 26 PHE B CA 1 ATOM 1756 C C . PHE B 2 28 ? 47.581 19.341 -16.065 1.00 18.78 ? 26 PHE B C 1 ATOM 1757 O O . PHE B 2 28 ? 48.198 19.588 -17.105 1.00 20.34 ? 26 PHE B O 1 ATOM 1758 C CB . PHE B 2 28 ? 49.059 17.726 -14.813 1.00 17.91 ? 26 PHE B CB 1 ATOM 1759 C CG . PHE B 2 28 ? 49.579 18.858 -13.948 1.00 20.03 ? 26 PHE B CG 1 ATOM 1760 C CD1 . PHE B 2 28 ? 48.965 19.173 -12.744 1.00 16.84 ? 26 PHE B CD1 1 ATOM 1761 C CD2 . PHE B 2 28 ? 50.727 19.564 -14.316 1.00 22.88 ? 26 PHE B CD2 1 ATOM 1762 C CE1 . PHE B 2 28 ? 49.467 20.198 -11.926 1.00 21.98 ? 26 PHE B CE1 1 ATOM 1763 C CE2 . PHE B 2 28 ? 51.238 20.593 -13.503 1.00 16.41 ? 26 PHE B CE2 1 ATOM 1764 C CZ . PHE B 2 28 ? 50.599 20.904 -12.309 1.00 16.69 ? 26 PHE B CZ 1 ATOM 1765 N N . LEU B 2 29 ? 46.785 20.216 -15.461 1.00 19.05 ? 27 LEU B N 1 ATOM 1766 C CA . LEU B 2 29 ? 46.552 21.559 -15.983 1.00 16.87 ? 27 LEU B CA 1 ATOM 1767 C C . LEU B 2 29 ? 46.765 22.543 -14.838 1.00 17.24 ? 27 LEU B C 1 ATOM 1768 O O . LEU B 2 29 ? 45.967 22.586 -13.900 1.00 17.00 ? 27 LEU B O 1 ATOM 1769 C CB . LEU B 2 29 ? 45.112 21.671 -16.517 1.00 19.46 ? 27 LEU B CB 1 ATOM 1770 C CG . LEU B 2 29 ? 44.727 22.931 -17.296 1.00 27.10 ? 27 LEU B CG 1 ATOM 1771 C CD1 . LEU B 2 29 ? 45.606 23.105 -18.542 1.00 23.25 ? 27 LEU B CD1 1 ATOM 1772 C CD2 . LEU B 2 29 ? 43.239 22.896 -17.682 1.00 25.67 ? 27 LEU B CD2 1 ATOM 1773 N N . ASP B 2 30 ? 47.848 23.312 -14.915 1.00 13.65 ? 28 ASP B N 1 ATOM 1774 C CA . ASP B 2 30 ? 48.249 24.251 -13.873 1.00 18.29 ? 28 ASP B CA 1 ATOM 1775 C C . ASP B 2 30 ? 47.861 25.654 -14.335 1.00 20.34 ? 28 ASP B C 1 ATOM 1776 O O . ASP B 2 30 ? 48.364 26.133 -15.348 1.00 21.09 ? 28 ASP B O 1 ATOM 1777 C CB . ASP B 2 30 ? 49.763 24.169 -13.679 1.00 20.23 ? 28 ASP B CB 1 ATOM 1778 C CG . ASP B 2 30 ? 50.182 24.268 -12.216 1.00 23.82 ? 28 ASP B CG 1 ATOM 1779 O OD1 . ASP B 2 30 ? 49.304 24.281 -11.318 1.00 15.36 ? 28 ASP B OD1 1 ATOM 1780 O OD2 . ASP B 2 30 ? 51.408 24.300 -11.967 1.00 21.96 ? 28 ASP B OD2 1 ATOM 1781 N N . ARG B 2 31 ? 46.975 26.306 -13.591 1.00 15.49 ? 29 ARG B N 1 ATOM 1782 C CA . ARG B 2 31 ? 46.275 27.498 -14.081 1.00 17.68 ? 29 ARG B CA 1 ATOM 1783 C C . ARG B 2 31 ? 46.389 28.682 -13.119 1.00 18.34 ? 29 ARG B C 1 ATOM 1784 O O . ARG B 2 31 ? 46.151 28.545 -11.914 1.00 17.10 ? 29 ARG B O 1 ATOM 1785 C CB . ARG B 2 31 ? 44.784 27.168 -14.301 1.00 15.47 ? 29 ARG B CB 1 ATOM 1786 C CG . ARG B 2 31 ? 44.539 25.841 -15.042 1.00 15.95 ? 29 ARG B CG 1 ATOM 1787 C CD . ARG B 2 31 ? 43.043 25.525 -15.153 1.00 10.77 ? 29 ARG B CD 1 ATOM 1788 N NE . ARG B 2 31 ? 42.351 26.469 -16.032 1.00 14.94 ? 29 ARG B NE 1 ATOM 1789 C CZ . ARG B 2 31 ? 41.033 26.514 -16.183 1.00 15.09 ? 29 ARG B CZ 1 ATOM 1790 N NH1 . ARG B 2 31 ? 40.260 25.655 -15.520 1.00 13.72 ? 29 ARG B NH1 1 ATOM 1791 N NH2 . ARG B 2 31 ? 40.491 27.399 -17.011 1.00 12.45 ? 29 ARG B NH2 1 ATOM 1792 N N . TYR B 2 32 ? 46.735 29.849 -13.664 1.00 15.64 ? 30 TYR B N 1 ATOM 1793 C CA . TYR B 2 32 ? 46.881 31.074 -12.865 1.00 10.66 ? 30 TYR B CA 1 ATOM 1794 C C . TYR B 2 32 ? 45.889 32.133 -13.348 1.00 11.21 ? 30 TYR B C 1 ATOM 1795 O O . TYR B 2 32 ? 45.742 32.340 -14.559 1.00 13.83 ? 30 TYR B O 1 ATOM 1796 C CB . TYR B 2 32 ? 48.316 31.616 -12.971 1.00 13.96 ? 30 TYR B CB 1 ATOM 1797 C CG . TYR B 2 32 ? 49.331 30.785 -12.205 1.00 17.59 ? 30 TYR B CG 1 ATOM 1798 C CD1 . TYR B 2 32 ? 49.881 31.255 -11.022 1.00 10.40 ? 30 TYR B CD1 1 ATOM 1799 C CD2 . TYR B 2 32 ? 49.711 29.521 -12.651 1.00 16.98 ? 30 TYR B CD2 1 ATOM 1800 C CE1 . TYR B 2 32 ? 50.798 30.489 -10.293 1.00 14.30 ? 30 TYR B CE1 1 ATOM 1801 C CE2 . TYR B 2 32 ? 50.636 28.750 -11.945 1.00 19.11 ? 30 TYR B CE2 1 ATOM 1802 C CZ . TYR B 2 32 ? 51.171 29.240 -10.764 1.00 16.16 ? 30 TYR B CZ 1 ATOM 1803 O OH . TYR B 2 32 ? 52.083 28.495 -10.053 1.00 18.06 ? 30 TYR B OH 1 ATOM 1804 N N . PHE B 2 33 ? 45.218 32.794 -12.407 1.00 10.14 ? 31 PHE B N 1 ATOM 1805 C CA . PHE B 2 33 ? 44.124 33.725 -12.730 1.00 15.81 ? 31 PHE B CA 1 ATOM 1806 C C . PHE B 2 33 ? 44.297 35.076 -12.053 1.00 12.25 ? 31 PHE B C 1 ATOM 1807 O O . PHE B 2 33 ? 44.720 35.152 -10.904 1.00 14.46 ? 31 PHE B O 1 ATOM 1808 C CB . PHE B 2 33 ? 42.753 33.165 -12.281 1.00 10.70 ? 31 PHE B CB 1 ATOM 1809 C CG . PHE B 2 33 ? 42.464 31.764 -12.753 1.00 12.97 ? 31 PHE B CG 1 ATOM 1810 C CD1 . PHE B 2 33 ? 41.634 31.544 -13.844 1.00 16.08 ? 31 PHE B CD1 1 ATOM 1811 C CD2 . PHE B 2 33 ? 42.995 30.666 -12.083 1.00 14.40 ? 31 PHE B CD2 1 ATOM 1812 C CE1 . PHE B 2 33 ? 41.349 30.243 -14.284 1.00 20.35 ? 31 PHE B CE1 1 ATOM 1813 C CE2 . PHE B 2 33 ? 42.725 29.367 -12.513 1.00 15.97 ? 31 PHE B CE2 1 ATOM 1814 C CZ . PHE B 2 33 ? 41.903 29.155 -13.617 1.00 12.72 ? 31 PHE B CZ 1 ATOM 1815 N N . TYR B 2 34 ? 43.949 36.145 -12.761 1.00 12.93 ? 32 TYR B N 1 ATOM 1816 C CA . TYR B 2 34 ? 43.864 37.460 -12.140 1.00 17.18 ? 32 TYR B CA 1 ATOM 1817 C C . TYR B 2 34 ? 42.398 37.871 -12.213 1.00 18.60 ? 32 TYR B C 1 ATOM 1818 O O . TYR B 2 34 ? 41.836 38.004 -13.307 1.00 14.99 ? 32 TYR B O 1 ATOM 1819 C CB . TYR B 2 34 ? 44.790 38.464 -12.835 1.00 14.34 ? 32 TYR B CB 1 ATOM 1820 C CG . TYR B 2 34 ? 44.703 39.870 -12.271 1.00 13.30 ? 32 TYR B CG 1 ATOM 1821 C CD1 . TYR B 2 34 ? 45.218 40.167 -11.020 1.00 13.41 ? 32 TYR B CD1 1 ATOM 1822 C CD2 . TYR B 2 34 ? 44.114 40.900 -12.999 1.00 17.27 ? 32 TYR B CD2 1 ATOM 1823 C CE1 . TYR B 2 34 ? 45.148 41.457 -10.498 1.00 16.11 ? 32 TYR B CE1 1 ATOM 1824 C CE2 . TYR B 2 34 ? 44.037 42.200 -12.484 1.00 15.61 ? 32 TYR B CE2 1 ATOM 1825 C CZ . TYR B 2 34 ? 44.556 42.468 -11.236 1.00 17.04 ? 32 TYR B CZ 1 ATOM 1826 O OH . TYR B 2 34 ? 44.482 43.743 -10.717 1.00 18.63 ? 32 TYR B OH 1 ATOM 1827 N N . HIS B 2 35 ? 41.782 38.024 -11.042 1.00 13.97 ? 33 HIS B N 1 ATOM 1828 C CA . HIS B 2 35 ? 40.321 38.055 -10.907 1.00 17.98 ? 33 HIS B CA 1 ATOM 1829 C C . HIS B 2 35 ? 39.742 36.718 -11.437 1.00 24.24 ? 33 HIS B C 1 ATOM 1830 O O . HIS B 2 35 ? 40.006 35.664 -10.846 1.00 17.70 ? 33 HIS B O 1 ATOM 1831 C CB . HIS B 2 35 ? 39.692 39.302 -11.569 1.00 16.11 ? 33 HIS B CB 1 ATOM 1832 C CG . HIS B 2 35 ? 40.368 40.601 -11.210 1.00 16.54 ? 33 HIS B CG 1 ATOM 1833 N ND1 . HIS B 2 35 ? 41.030 40.803 -10.017 1.00 19.85 ? 33 HIS B ND1 1 ATOM 1834 C CD2 . HIS B 2 35 ? 40.488 41.761 -11.902 1.00 17.33 ? 33 HIS B CD2 1 ATOM 1835 C CE1 . HIS B 2 35 ? 41.533 42.027 -9.990 1.00 17.11 ? 33 HIS B CE1 1 ATOM 1836 N NE2 . HIS B 2 35 ? 41.208 42.634 -11.117 1.00 16.14 ? 33 HIS B NE2 1 ATOM 1837 N N . GLN B 2 36 ? 38.977 36.740 -12.533 1.00 13.56 ? 34 GLN B N 1 ATOM 1838 C CA . GLN B 2 36 ? 38.550 35.482 -13.171 1.00 13.47 ? 34 GLN B CA 1 ATOM 1839 C C . GLN B 2 36 ? 39.300 35.160 -14.450 1.00 19.55 ? 34 GLN B C 1 ATOM 1840 O O . GLN B 2 36 ? 38.989 34.171 -15.113 1.00 21.66 ? 34 GLN B O 1 ATOM 1841 C CB . GLN B 2 36 ? 37.062 35.495 -13.542 1.00 23.92 ? 34 GLN B CB 1 ATOM 1842 C CG . GLN B 2 36 ? 36.116 35.494 -12.387 1.00 24.76 ? 34 GLN B CG 1 ATOM 1843 C CD . GLN B 2 36 ? 35.839 36.888 -11.894 1.00 30.77 ? 34 GLN B CD 1 ATOM 1844 O OE1 . GLN B 2 36 ? 35.040 37.626 -12.481 1.00 38.70 ? 34 GLN B OE1 1 ATOM 1845 N NE2 . GLN B 2 36 ? 36.502 37.264 -10.813 1.00 29.56 ? 34 GLN B NE2 1 ATOM 1846 N N . GLU B 2 37 ? 40.257 36.000 -14.821 1.00 19.68 ? 35 GLU B N 1 ATOM 1847 C CA . GLU B 2 37 ? 40.923 35.860 -16.111 1.00 20.79 ? 35 GLU B CA 1 ATOM 1848 C C . GLU B 2 37 ? 42.110 34.931 -15.991 1.00 18.68 ? 35 GLU B C 1 ATOM 1849 O O . GLU B 2 37 ? 43.114 35.278 -15.363 1.00 15.27 ? 35 GLU B O 1 ATOM 1850 C CB . GLU B 2 37 ? 41.376 37.233 -16.630 1.00 21.87 ? 35 GLU B CB 1 ATOM 1851 C CG . GLU B 2 37 ? 42.341 37.194 -17.826 1.00 28.14 ? 35 GLU B CG 1 ATOM 1852 C CD . GLU B 2 37 ? 43.040 38.537 -18.088 1.00 36.53 ? 35 GLU B CD 1 ATOM 1853 O OE1 . GLU B 2 37 ? 42.519 39.587 -17.656 1.00 34.24 ? 35 GLU B OE1 1 ATOM 1854 O OE2 . GLU B 2 37 ? 44.121 38.536 -18.722 1.00 38.33 ? 35 GLU B OE2 1 ATOM 1855 N N . GLU B 2 38 ? 42.005 33.747 -16.585 1.00 16.96 ? 36 GLU B N 1 ATOM 1856 C CA . GLU B 2 38 ? 43.161 32.868 -16.669 1.00 17.05 ? 36 GLU B CA 1 ATOM 1857 C C . GLU B 2 38 ? 44.218 33.556 -17.540 1.00 17.18 ? 36 GLU B C 1 ATOM 1858 O O . GLU B 2 38 ? 43.934 33.938 -18.677 1.00 15.73 ? 36 GLU B O 1 ATOM 1859 C CB . GLU B 2 38 ? 42.793 31.505 -17.282 1.00 13.79 ? 36 GLU B CB 1 ATOM 1860 C CG . GLU B 2 38 ? 43.960 30.490 -17.164 1.00 16.67 ? 36 GLU B CG 1 ATOM 1861 C CD . GLU B 2 38 ? 43.619 29.114 -17.708 1.00 18.83 ? 36 GLU B CD 1 ATOM 1862 O OE1 . GLU B 2 38 ? 42.578 28.973 -18.372 1.00 16.48 ? 36 GLU B OE1 1 ATOM 1863 O OE2 . GLU B 2 38 ? 44.387 28.164 -17.461 1.00 17.20 ? 36 GLU B OE2 1 ATOM 1864 N N . TYR B 2 39 ? 45.432 33.728 -17.026 1.00 14.15 ? 37 TYR B N 1 ATOM 1865 C CA . TYR B 2 39 ? 46.432 34.446 -17.812 1.00 15.47 ? 37 TYR B CA 1 ATOM 1866 C C . TYR B 2 39 ? 47.602 33.593 -18.306 1.00 17.37 ? 37 TYR B C 1 ATOM 1867 O O . TYR B 2 39 ? 48.235 33.923 -19.312 1.00 16.23 ? 37 TYR B O 1 ATOM 1868 C CB . TYR B 2 39 ? 46.908 35.728 -17.092 1.00 12.31 ? 37 TYR B CB 1 ATOM 1869 C CG . TYR B 2 39 ? 47.552 35.521 -15.729 1.00 20.83 ? 37 TYR B CG 1 ATOM 1870 C CD1 . TYR B 2 39 ? 48.911 35.269 -15.622 1.00 16.59 ? 37 TYR B CD1 1 ATOM 1871 C CD2 . TYR B 2 39 ? 46.802 35.620 -14.544 1.00 16.02 ? 37 TYR B CD2 1 ATOM 1872 C CE1 . TYR B 2 39 ? 49.523 35.107 -14.378 1.00 21.01 ? 37 TYR B CE1 1 ATOM 1873 C CE2 . TYR B 2 39 ? 47.411 35.458 -13.286 1.00 12.00 ? 37 TYR B CE2 1 ATOM 1874 C CZ . TYR B 2 39 ? 48.771 35.207 -13.216 1.00 15.94 ? 37 TYR B CZ 1 ATOM 1875 O OH . TYR B 2 39 ? 49.400 35.033 -11.997 1.00 16.00 ? 37 TYR B OH 1 ATOM 1876 N N . VAL B 2 40 ? 47.895 32.504 -17.602 1.00 16.91 ? 38 VAL B N 1 ATOM 1877 C CA . VAL B 2 40 ? 48.951 31.601 -18.029 1.00 13.96 ? 38 VAL B CA 1 ATOM 1878 C C . VAL B 2 40 ? 48.635 30.193 -17.535 1.00 18.99 ? 38 VAL B C 1 ATOM 1879 O O . VAL B 2 40 ? 48.007 30.026 -16.487 1.00 15.10 ? 38 VAL B O 1 ATOM 1880 C CB . VAL B 2 40 ? 50.340 32.062 -17.535 1.00 15.21 ? 38 VAL B CB 1 ATOM 1881 C CG1 . VAL B 2 40 ? 50.407 32.096 -16.004 1.00 16.89 ? 38 VAL B CG1 1 ATOM 1882 C CG2 . VAL B 2 40 ? 51.471 31.181 -18.129 1.00 15.70 ? 38 VAL B CG2 1 ATOM 1883 N N . ARG B 2 41 ? 49.032 29.184 -18.300 1.00 13.30 ? 39 ARG B N 1 ATOM 1884 C CA . ARG B 2 41 ? 48.829 27.804 -17.857 1.00 16.35 ? 39 ARG B CA 1 ATOM 1885 C C . ARG B 2 41 ? 49.932 26.837 -18.303 1.00 13.65 ? 39 ARG B C 1 ATOM 1886 O O . ARG B 2 41 ? 50.572 27.040 -19.331 1.00 16.97 ? 39 ARG B O 1 ATOM 1887 C CB . ARG B 2 41 ? 47.475 27.269 -18.345 1.00 15.53 ? 39 ARG B CB 1 ATOM 1888 C CG . ARG B 2 41 ? 47.291 27.308 -19.877 1.00 19.60 ? 39 ARG B CG 1 ATOM 1889 C CD . ARG B 2 41 ? 46.204 26.323 -20.374 1.00 19.34 ? 39 ARG B CD 1 ATOM 1890 N NE . ARG B 2 41 ? 44.872 26.650 -19.874 1.00 14.61 ? 39 ARG B NE 1 ATOM 1891 C CZ . ARG B 2 41 ? 43.753 26.036 -20.262 1.00 21.28 ? 39 ARG B CZ 1 ATOM 1892 N NH1 . ARG B 2 41 ? 43.803 25.049 -21.152 1.00 16.98 ? 39 ARG B NH1 1 ATOM 1893 N NH2 . ARG B 2 41 ? 42.583 26.407 -19.753 1.00 23.17 ? 39 ARG B NH2 1 ATOM 1894 N N . PHE B 2 42 ? 50.129 25.775 -17.529 1.00 13.69 ? 40 PHE B N 1 ATOM 1895 C CA . PHE B 2 42 ? 50.883 24.620 -18.014 1.00 13.49 ? 40 PHE B CA 1 ATOM 1896 C C . PHE B 2 42 ? 49.899 23.471 -18.265 1.00 17.14 ? 40 PHE B C 1 ATOM 1897 O O . PHE B 2 42 ? 49.163 23.069 -17.372 1.00 14.58 ? 40 PHE B O 1 ATOM 1898 C CB . PHE B 2 42 ? 51.973 24.202 -17.015 1.00 11.97 ? 40 PHE B CB 1 ATOM 1899 C CG . PHE B 2 42 ? 52.744 22.962 -17.426 1.00 19.97 ? 40 PHE B CG 1 ATOM 1900 C CD1 . PHE B 2 42 ? 53.999 23.068 -18.009 1.00 17.72 ? 40 PHE B CD1 1 ATOM 1901 C CD2 . PHE B 2 42 ? 52.220 21.694 -17.207 1.00 17.52 ? 40 PHE B CD2 1 ATOM 1902 C CE1 . PHE B 2 42 ? 54.709 21.931 -18.383 1.00 16.44 ? 40 PHE B CE1 1 ATOM 1903 C CE2 . PHE B 2 42 ? 52.917 20.564 -17.572 1.00 18.90 ? 40 PHE B CE2 1 ATOM 1904 C CZ . PHE B 2 42 ? 54.169 20.681 -18.161 1.00 17.55 ? 40 PHE B CZ 1 ATOM 1905 N N . ASP B 2 43 ? 49.904 22.950 -19.486 1.00 14.34 ? 41 ASP B N 1 ATOM 1906 C CA . ASP B 2 43 ? 49.087 21.812 -19.875 1.00 13.28 ? 41 ASP B CA 1 ATOM 1907 C C . ASP B 2 43 ? 50.045 20.634 -20.131 1.00 13.95 ? 41 ASP B C 1 ATOM 1908 O O . ASP B 2 43 ? 50.939 20.726 -20.970 1.00 19.93 ? 41 ASP B O 1 ATOM 1909 C CB . ASP B 2 43 ? 48.299 22.177 -21.147 1.00 14.87 ? 41 ASP B CB 1 ATOM 1910 C CG . ASP B 2 43 ? 47.256 21.123 -21.555 1.00 21.86 ? 41 ASP B CG 1 ATOM 1911 O OD1 . ASP B 2 43 ? 47.359 19.936 -21.170 1.00 20.40 ? 41 ASP B OD1 1 ATOM 1912 O OD2 . ASP B 2 43 ? 46.328 21.501 -22.302 1.00 19.61 ? 41 ASP B OD2 1 ATOM 1913 N N . SER B 2 44 ? 49.881 19.531 -19.401 1.00 13.08 ? 42 SER B N 1 ATOM 1914 C CA . SER B 2 44 ? 50.744 18.364 -19.625 1.00 13.81 ? 42 SER B CA 1 ATOM 1915 C C . SER B 2 44 ? 50.685 17.843 -21.064 1.00 19.04 ? 42 SER B C 1 ATOM 1916 O O . SER B 2 44 ? 51.614 17.157 -21.522 1.00 21.32 ? 42 SER B O 1 ATOM 1917 C CB . SER B 2 44 ? 50.436 17.237 -18.632 1.00 18.75 ? 42 SER B CB 1 ATOM 1918 O OG . SER B 2 44 ? 49.067 16.886 -18.650 1.00 17.44 ? 42 SER B OG 1 ATOM 1919 N N . ASP B 2 45 ? 49.598 18.154 -21.771 1.00 17.12 ? 43 ASP B N 1 ATOM 1920 C CA . ASP B 2 45 ? 49.466 17.796 -23.185 1.00 21.86 ? 43 ASP B CA 1 ATOM 1921 C C . ASP B 2 45 ? 50.507 18.521 -24.028 1.00 22.06 ? 43 ASP B C 1 ATOM 1922 O O . ASP B 2 45 ? 50.871 18.059 -25.103 1.00 19.76 ? 43 ASP B O 1 ATOM 1923 C CB . ASP B 2 45 ? 48.089 18.180 -23.712 1.00 25.23 ? 43 ASP B CB 1 ATOM 1924 C CG . ASP B 2 45 ? 47.020 17.163 -23.363 1.00 31.37 ? 43 ASP B CG 1 ATOM 1925 O OD1 . ASP B 2 45 ? 47.295 16.238 -22.567 1.00 30.31 ? 43 ASP B OD1 1 ATOM 1926 O OD2 . ASP B 2 45 ? 45.900 17.299 -23.891 1.00 37.62 ? 43 ASP B OD2 1 ATOM 1927 N N . VAL B 2 46 ? 50.969 19.665 -23.536 1.00 17.55 ? 44 VAL B N 1 ATOM 1928 C CA . VAL B 2 46 ? 51.896 20.509 -24.286 1.00 21.43 ? 44 VAL B CA 1 ATOM 1929 C C . VAL B 2 46 ? 53.318 20.376 -23.735 1.00 22.96 ? 44 VAL B C 1 ATOM 1930 O O . VAL B 2 46 ? 54.285 20.264 -24.494 1.00 22.80 ? 44 VAL B O 1 ATOM 1931 C CB . VAL B 2 46 ? 51.465 21.999 -24.227 1.00 15.89 ? 44 VAL B CB 1 ATOM 1932 C CG1 . VAL B 2 46 ? 52.496 22.874 -24.919 1.00 16.62 ? 44 VAL B CG1 1 ATOM 1933 C CG2 . VAL B 2 46 ? 50.066 22.186 -24.875 1.00 19.83 ? 44 VAL B CG2 1 ATOM 1934 N N . GLY B 2 47 ? 53.441 20.409 -22.414 1.00 20.81 ? 45 GLY B N 1 ATOM 1935 C CA . GLY B 2 47 ? 54.732 20.227 -21.767 1.00 19.08 ? 45 GLY B CA 1 ATOM 1936 C C . GLY B 2 47 ? 55.532 21.506 -21.595 1.00 20.21 ? 45 GLY B C 1 ATOM 1937 O O . GLY B 2 47 ? 56.709 21.454 -21.235 1.00 21.47 ? 45 GLY B O 1 ATOM 1938 N N . GLU B 2 48 ? 54.893 22.648 -21.858 1.00 15.28 ? 46 GLU B N 1 ATOM 1939 C CA . GLU B 2 48 ? 55.467 23.971 -21.578 1.00 19.88 ? 46 GLU B CA 1 ATOM 1940 C C . GLU B 2 48 ? 54.335 24.905 -21.188 1.00 19.89 ? 46 GLU B C 1 ATOM 1941 O O . GLU B 2 48 ? 53.174 24.643 -21.506 1.00 15.90 ? 46 GLU B O 1 ATOM 1942 C CB . GLU B 2 48 ? 56.165 24.548 -22.816 1.00 22.57 ? 46 GLU B CB 1 ATOM 1943 C CG . GLU B 2 48 ? 57.564 24.019 -23.074 1.00 38.29 ? 46 GLU B CG 1 ATOM 1944 C CD . GLU B 2 48 ? 58.223 24.671 -24.289 1.00 47.88 ? 46 GLU B CD 1 ATOM 1945 O OE1 . GLU B 2 48 ? 59.458 24.491 -24.460 1.00 52.58 ? 46 GLU B OE1 1 ATOM 1946 O OE2 . GLU B 2 48 ? 57.501 25.352 -25.062 1.00 37.68 ? 46 GLU B OE2 1 ATOM 1947 N N . TYR B 2 49 ? 54.666 25.994 -20.503 1.00 16.92 ? 47 TYR B N 1 ATOM 1948 C CA . TYR B 2 49 ? 53.664 27.006 -20.198 1.00 15.51 ? 47 TYR B CA 1 ATOM 1949 C C . TYR B 2 49 ? 53.258 27.731 -21.462 1.00 20.16 ? 47 TYR B C 1 ATOM 1950 O O . TYR B 2 49 ? 54.088 27.959 -22.347 1.00 18.43 ? 47 TYR B O 1 ATOM 1951 C CB . TYR B 2 49 ? 54.224 28.032 -19.238 1.00 15.73 ? 47 TYR B CB 1 ATOM 1952 C CG . TYR B 2 49 ? 54.480 27.524 -17.848 1.00 18.80 ? 47 TYR B CG 1 ATOM 1953 C CD1 . TYR B 2 49 ? 53.497 27.594 -16.873 1.00 19.20 ? 47 TYR B CD1 1 ATOM 1954 C CD2 . TYR B 2 49 ? 55.715 27.002 -17.500 1.00 20.62 ? 47 TYR B CD2 1 ATOM 1955 C CE1 . TYR B 2 49 ? 53.741 27.138 -15.582 1.00 25.33 ? 47 TYR B CE1 1 ATOM 1956 C CE2 . TYR B 2 49 ? 55.965 26.546 -16.220 1.00 20.54 ? 47 TYR B CE2 1 ATOM 1957 C CZ . TYR B 2 49 ? 54.979 26.632 -15.263 1.00 19.18 ? 47 TYR B CZ 1 ATOM 1958 O OH . TYR B 2 49 ? 55.239 26.193 -13.976 1.00 23.21 ? 47 TYR B OH 1 ATOM 1959 N N . ARG B 2 50 ? 51.985 28.112 -21.534 1.00 18.58 ? 48 ARG B N 1 ATOM 1960 C CA . ARG B 2 50 ? 51.505 29.007 -22.587 1.00 19.11 ? 48 ARG B CA 1 ATOM 1961 C C . ARG B 2 50 ? 50.717 30.158 -21.951 1.00 20.46 ? 48 ARG B C 1 ATOM 1962 O O . ARG B 2 50 ? 49.961 29.949 -21.005 1.00 18.18 ? 48 ARG B O 1 ATOM 1963 C CB . ARG B 2 50 ? 50.622 28.258 -23.598 1.00 18.04 ? 48 ARG B CB 1 ATOM 1964 C CG . ARG B 2 50 ? 51.337 27.189 -24.431 1.00 25.03 ? 48 ARG B CG 1 ATOM 1965 C CD . ARG B 2 50 ? 52.272 27.795 -25.492 1.00 24.88 ? 48 ARG B CD 1 ATOM 1966 N NE . ARG B 2 50 ? 53.042 26.766 -26.202 1.00 33.26 ? 48 ARG B NE 1 ATOM 1967 C CZ . ARG B 2 50 ? 54.273 26.387 -25.854 1.00 45.38 ? 48 ARG B CZ 1 ATOM 1968 N NH1 . ARG B 2 50 ? 54.869 26.946 -24.810 1.00 53.57 ? 48 ARG B NH1 1 ATOM 1969 N NH2 . ARG B 2 50 ? 54.916 25.451 -26.541 1.00 39.25 ? 48 ARG B NH2 1 ATOM 1970 N N . ALA B 2 51 ? 50.918 31.369 -22.462 1.00 20.35 ? 49 ALA B N 1 ATOM 1971 C CA . ALA B 2 51 ? 50.156 32.530 -22.038 1.00 20.07 ? 49 ALA B CA 1 ATOM 1972 C C . ALA B 2 51 ? 48.736 32.387 -22.558 1.00 20.60 ? 49 ALA B C 1 ATOM 1973 O O . ALA B 2 51 ? 48.536 32.127 -23.742 1.00 24.32 ? 49 ALA B O 1 ATOM 1974 C CB . ALA B 2 51 ? 50.785 33.808 -22.602 1.00 22.84 ? 49 ALA B CB 1 ATOM 1975 N N . VAL B 2 52 ? 47.749 32.568 -21.688 1.00 17.54 ? 50 VAL B N 1 ATOM 1976 C CA . VAL B 2 52 ? 46.356 32.577 -22.139 1.00 16.54 ? 50 VAL B CA 1 ATOM 1977 C C . VAL B 2 52 ? 45.937 33.975 -22.616 1.00 21.09 ? 50 VAL B C 1 ATOM 1978 O O . VAL B 2 52 ? 45.169 34.118 -23.572 1.00 23.10 ? 50 VAL B O 1 ATOM 1979 C CB . VAL B 2 52 ? 45.409 32.042 -21.047 1.00 16.94 ? 50 VAL B CB 1 ATOM 1980 C CG1 . VAL B 2 52 ? 43.969 31.984 -21.569 1.00 18.15 ? 50 VAL B CG1 1 ATOM 1981 C CG2 . VAL B 2 52 ? 45.873 30.664 -20.597 1.00 20.19 ? 50 VAL B CG2 1 ATOM 1982 N N . THR B 2 53 ? 46.451 35.006 -21.953 1.00 24.80 ? 51 THR B N 1 ATOM 1983 C CA . THR B 2 53 ? 46.218 36.384 -22.371 1.00 24.61 ? 51 THR B CA 1 ATOM 1984 C C . THR B 2 53 ? 47.551 37.115 -22.341 1.00 25.10 ? 51 THR B C 1 ATOM 1985 O O . THR B 2 53 ? 48.534 36.584 -21.817 1.00 21.27 ? 51 THR B O 1 ATOM 1986 C CB . THR B 2 53 ? 45.279 37.114 -21.401 1.00 27.55 ? 51 THR B CB 1 ATOM 1987 O OG1 . THR B 2 53 ? 45.939 37.250 -20.135 1.00 23.85 ? 51 THR B OG1 1 ATOM 1988 C CG2 . THR B 2 53 ? 43.960 36.341 -21.221 1.00 24.29 ? 51 THR B CG2 1 ATOM 1989 N N . GLU B 2 54 ? 47.580 38.334 -22.876 1.00 21.90 ? 52 GLU B N 1 ATOM 1990 C CA . GLU B 2 54 ? 48.823 39.115 -22.955 1.00 29.33 ? 52 GLU B CA 1 ATOM 1991 C C . GLU B 2 54 ? 49.430 39.326 -21.568 1.00 24.44 ? 52 GLU B C 1 ATOM 1992 O O . GLU B 2 54 ? 50.647 39.339 -21.414 1.00 26.13 ? 52 GLU B O 1 ATOM 1993 C CB . GLU B 2 54 ? 48.598 40.463 -23.659 1.00 39.22 ? 52 GLU B CB 1 ATOM 1994 C CG . GLU B 2 54 ? 47.711 41.454 -22.886 1.00 58.63 ? 52 GLU B CG 1 ATOM 1995 C CD . GLU B 2 54 ? 47.807 42.893 -23.406 1.00 70.20 ? 52 GLU B CD 1 ATOM 1996 O OE1 . GLU B 2 54 ? 47.384 43.829 -22.684 1.00 66.65 ? 52 GLU B OE1 1 ATOM 1997 O OE2 . GLU B 2 54 ? 48.305 43.088 -24.537 1.00 76.98 ? 52 GLU B OE2 1 ATOM 1998 N N . LEU B 2 55 ? 48.563 39.455 -20.568 1.00 21.21 ? 53 LEU B N 1 ATOM 1999 C CA . LEU B 2 55 ? 48.954 39.595 -19.168 1.00 24.23 ? 53 LEU B CA 1 ATOM 2000 C C . LEU B 2 55 ? 49.900 38.492 -18.690 1.00 23.72 ? 53 LEU B C 1 ATOM 2001 O O . LEU B 2 55 ? 50.671 38.698 -17.756 1.00 21.76 ? 53 LEU B O 1 ATOM 2002 C CB . LEU B 2 55 ? 47.699 39.560 -18.296 1.00 29.45 ? 53 LEU B CB 1 ATOM 2003 C CG . LEU B 2 55 ? 47.581 40.510 -17.102 1.00 36.04 ? 53 LEU B CG 1 ATOM 2004 C CD1 . LEU B 2 55 ? 47.646 41.962 -17.537 1.00 30.14 ? 53 LEU B CD1 1 ATOM 2005 C CD2 . LEU B 2 55 ? 46.286 40.235 -16.347 1.00 32.66 ? 53 LEU B CD2 1 ATOM 2006 N N . GLY B 2 56 ? 49.823 37.314 -19.305 1.00 20.37 ? 54 GLY B N 1 ATOM 2007 C CA . GLY B 2 56 ? 50.604 36.189 -18.828 1.00 16.87 ? 54 GLY B CA 1 ATOM 2008 C C . GLY B 2 56 ? 51.838 35.897 -19.647 1.00 18.94 ? 54 GLY B C 1 ATOM 2009 O O . GLY B 2 56 ? 52.599 34.981 -19.330 1.00 21.88 ? 54 GLY B O 1 ATOM 2010 N N . ARG B 2 57 ? 52.039 36.662 -20.713 1.00 17.87 ? 55 ARG B N 1 ATOM 2011 C CA . ARG B 2 57 ? 53.214 36.454 -21.553 1.00 22.79 ? 55 ARG B CA 1 ATOM 2012 C C . ARG B 2 57 ? 54.564 36.497 -20.807 1.00 21.48 ? 55 ARG B C 1 ATOM 2013 O O . ARG B 2 57 ? 55.413 35.639 -21.055 1.00 20.67 ? 55 ARG B O 1 ATOM 2014 C CB . ARG B 2 57 ? 53.208 37.386 -22.767 1.00 23.76 ? 55 ARG B CB 1 ATOM 2015 C CG . ARG B 2 57 ? 52.174 36.982 -23.811 1.00 33.65 ? 55 ARG B CG 1 ATOM 2016 C CD . ARG B 2 57 ? 52.342 37.748 -25.110 1.00 50.08 ? 55 ARG B CD 1 ATOM 2017 N NE . ARG B 2 57 ? 51.146 38.524 -25.425 1.00 55.08 ? 55 ARG B NE 1 ATOM 2018 C CZ . ARG B 2 57 ? 51.110 39.493 -26.330 1.00 64.68 ? 55 ARG B CZ 1 ATOM 2019 N NH1 . ARG B 2 57 ? 52.209 39.802 -27.009 1.00 67.02 ? 55 ARG B NH1 1 ATOM 2020 N NH2 . ARG B 2 57 ? 49.982 40.153 -26.552 1.00 68.59 ? 55 ARG B NH2 1 ATOM 2021 N N . PRO B 2 58 ? 54.764 37.475 -19.894 1.00 18.59 ? 56 PRO B N 1 ATOM 2022 C CA . PRO B 2 58 ? 56.062 37.496 -19.207 1.00 24.02 ? 56 PRO B CA 1 ATOM 2023 C C . PRO B 2 58 ? 56.327 36.224 -18.384 1.00 22.89 ? 56 PRO B C 1 ATOM 2024 O O . PRO B 2 58 ? 57.466 35.762 -18.315 1.00 19.89 ? 56 PRO B O 1 ATOM 2025 C CB . PRO B 2 58 ? 55.951 38.720 -18.284 1.00 30.26 ? 56 PRO B CB 1 ATOM 2026 C CG . PRO B 2 58 ? 54.902 39.595 -18.921 1.00 27.47 ? 56 PRO B CG 1 ATOM 2027 C CD . PRO B 2 58 ? 53.918 38.625 -19.498 1.00 20.78 ? 56 PRO B CD 1 ATOM 2028 N N . ASP B 2 59 ? 55.287 35.655 -17.786 1.00 22.34 ? 57 ASP B N 1 ATOM 2029 C CA . ASP B 2 59 ? 55.472 34.470 -16.954 1.00 18.49 ? 57 ASP B CA 1 ATOM 2030 C C . ASP B 2 59 ? 55.716 33.227 -17.799 1.00 19.94 ? 57 ASP B C 1 ATOM 2031 O O . ASP B 2 59 ? 56.560 32.398 -17.467 1.00 18.92 ? 57 ASP B O 1 ATOM 2032 C CB . ASP B 2 59 ? 54.272 34.270 -16.028 1.00 21.65 ? 57 ASP B CB 1 ATOM 2033 C CG . ASP B 2 59 ? 54.167 35.358 -14.977 1.00 24.25 ? 57 ASP B CG 1 ATOM 2034 O OD1 . ASP B 2 59 ? 55.226 35.851 -14.516 1.00 24.11 ? 57 ASP B OD1 1 ATOM 2035 O OD2 . ASP B 2 59 ? 53.033 35.732 -14.620 1.00 23.71 ? 57 ASP B OD2 1 ATOM 2036 N N . ALA B 2 60 ? 54.978 33.097 -18.895 1.00 20.31 ? 58 ALA B N 1 ATOM 2037 C CA . ALA B 2 60 ? 55.201 31.987 -19.817 1.00 23.38 ? 58 ALA B CA 1 ATOM 2038 C C . ALA B 2 60 ? 56.649 31.971 -20.299 1.00 22.17 ? 58 ALA B C 1 ATOM 2039 O O . ALA B 2 60 ? 57.314 30.938 -20.256 1.00 20.58 ? 58 ALA B O 1 ATOM 2040 C CB . ALA B 2 60 ? 54.223 32.062 -21.010 1.00 19.35 ? 58 ALA B CB 1 ATOM 2041 N N . GLU B 2 61 ? 57.138 33.125 -20.747 1.00 22.55 ? 59 GLU B N 1 ATOM 2042 C CA . GLU B 2 61 ? 58.487 33.224 -21.292 1.00 22.99 ? 59 GLU B CA 1 ATOM 2043 C C . GLU B 2 61 ? 59.556 32.934 -20.241 1.00 23.49 ? 59 GLU B C 1 ATOM 2044 O O . GLU B 2 61 ? 60.518 32.232 -20.514 1.00 24.66 ? 59 GLU B O 1 ATOM 2045 C CB . GLU B 2 61 ? 58.725 34.602 -21.918 1.00 28.14 ? 59 GLU B CB 1 ATOM 2046 C CG . GLU B 2 61 ? 57.941 34.825 -23.204 1.00 43.91 ? 59 GLU B CG 1 ATOM 2047 C CD . GLU B 2 61 ? 57.998 36.268 -23.688 1.00 54.51 ? 59 GLU B CD 1 ATOM 2048 O OE1 . GLU B 2 61 ? 58.733 37.077 -23.076 1.00 58.90 ? 59 GLU B OE1 1 ATOM 2049 O OE2 . GLU B 2 61 ? 57.300 36.589 -24.676 1.00 51.30 ? 59 GLU B OE2 1 ATOM 2050 N N . TYR B 2 62 ? 59.388 33.468 -19.039 1.00 24.94 ? 60 TYR B N 1 ATOM 2051 C CA . TYR B 2 62 ? 60.387 33.237 -18.001 1.00 26.94 ? 60 TYR B CA 1 ATOM 2052 C C . TYR B 2 62 ? 60.379 31.793 -17.499 1.00 24.32 ? 60 TYR B C 1 ATOM 2053 O O . TYR B 2 62 ? 61.421 31.135 -17.468 1.00 29.43 ? 60 TYR B O 1 ATOM 2054 C CB . TYR B 2 62 ? 60.211 34.194 -16.824 1.00 27.18 ? 60 TYR B CB 1 ATOM 2055 C CG . TYR B 2 62 ? 61.240 33.972 -15.738 1.00 36.98 ? 60 TYR B CG 1 ATOM 2056 C CD1 . TYR B 2 62 ? 62.581 34.272 -15.958 1.00 39.58 ? 60 TYR B CD1 1 ATOM 2057 C CD2 . TYR B 2 62 ? 60.879 33.447 -14.504 1.00 39.72 ? 60 TYR B CD2 1 ATOM 2058 C CE1 . TYR B 2 62 ? 63.535 34.060 -14.980 1.00 46.69 ? 60 TYR B CE1 1 ATOM 2059 C CE2 . TYR B 2 62 ? 61.831 33.231 -13.515 1.00 46.84 ? 60 TYR B CE2 1 ATOM 2060 C CZ . TYR B 2 62 ? 63.156 33.543 -13.762 1.00 54.22 ? 60 TYR B CZ 1 ATOM 2061 O OH . TYR B 2 62 ? 64.112 33.335 -12.792 1.00 68.17 ? 60 TYR B OH 1 ATOM 2062 N N . TRP B 2 63 ? 59.207 31.312 -17.099 1.00 20.07 ? 61 TRP B N 1 ATOM 2063 C CA . TRP B 2 63 ? 59.084 29.962 -16.551 1.00 22.29 ? 61 TRP B CA 1 ATOM 2064 C C . TRP B 2 63 ? 59.580 28.906 -17.547 1.00 23.66 ? 61 TRP B C 1 ATOM 2065 O O . TRP B 2 63 ? 60.225 27.931 -17.159 1.00 26.91 ? 61 TRP B O 1 ATOM 2066 C CB . TRP B 2 63 ? 57.641 29.684 -16.117 1.00 17.92 ? 61 TRP B CB 1 ATOM 2067 C CG . TRP B 2 63 ? 57.187 30.496 -14.921 1.00 19.28 ? 61 TRP B CG 1 ATOM 2068 C CD1 . TRP B 2 63 ? 57.975 31.180 -14.033 1.00 25.43 ? 61 TRP B CD1 1 ATOM 2069 C CD2 . TRP B 2 63 ? 55.833 30.712 -14.501 1.00 20.12 ? 61 TRP B CD2 1 ATOM 2070 N NE1 . TRP B 2 63 ? 57.189 31.802 -13.084 1.00 21.11 ? 61 TRP B NE1 1 ATOM 2071 C CE2 . TRP B 2 63 ? 55.874 31.529 -13.350 1.00 20.15 ? 61 TRP B CE2 1 ATOM 2072 C CE3 . TRP B 2 63 ? 54.588 30.295 -14.991 1.00 15.37 ? 61 TRP B CE3 1 ATOM 2073 C CZ2 . TRP B 2 63 ? 54.720 31.928 -12.680 1.00 21.58 ? 61 TRP B CZ2 1 ATOM 2074 C CZ3 . TRP B 2 63 ? 53.451 30.693 -14.335 1.00 14.39 ? 61 TRP B CZ3 1 ATOM 2075 C CH2 . TRP B 2 63 ? 53.520 31.496 -13.183 1.00 22.26 ? 61 TRP B CH2 1 ATOM 2076 N N . ASN B 2 64 ? 59.300 29.123 -18.832 1.00 25.10 ? 62 ASN B N 1 ATOM 2077 C CA . ASN B 2 64 ? 59.827 28.267 -19.894 1.00 23.80 ? 62 ASN B CA 1 ATOM 2078 C C . ASN B 2 64 ? 61.349 28.318 -20.044 1.00 26.00 ? 62 ASN B C 1 ATOM 2079 O O . ASN B 2 64 ? 61.935 27.421 -20.651 1.00 28.37 ? 62 ASN B O 1 ATOM 2080 C CB . ASN B 2 64 ? 59.154 28.582 -21.244 1.00 21.72 ? 62 ASN B CB 1 ATOM 2081 C CG . ASN B 2 64 ? 57.735 27.999 -21.348 1.00 23.01 ? 62 ASN B CG 1 ATOM 2082 O OD1 . ASN B 2 64 ? 57.346 27.116 -20.567 1.00 19.40 ? 62 ASN B OD1 1 ATOM 2083 N ND2 . ASN B 2 64 ? 56.974 28.469 -22.330 1.00 20.54 ? 62 ASN B ND2 1 ATOM 2084 N N . SER B 2 65 ? 61.988 29.356 -19.504 1.00 21.34 ? 63 SER B N 1 ATOM 2085 C CA . SER B 2 65 ? 63.450 29.451 -19.543 1.00 26.49 ? 63 SER B CA 1 ATOM 2086 C C . SER B 2 65 ? 64.096 28.691 -18.376 1.00 28.93 ? 63 SER B C 1 ATOM 2087 O O . SER B 2 65 ? 65.320 28.526 -18.319 1.00 27.97 ? 63 SER B O 1 ATOM 2088 C CB . SER B 2 65 ? 63.912 30.917 -19.525 1.00 23.06 ? 63 SER B CB 1 ATOM 2089 O OG . SER B 2 65 ? 63.627 31.540 -18.283 1.00 28.38 ? 63 SER B OG 1 ATOM 2090 N N . GLN B 2 66 ? 63.265 28.252 -17.439 1.00 23.40 ? 64 GLN B N 1 ATOM 2091 C CA . GLN B 2 66 ? 63.752 27.613 -16.221 1.00 26.42 ? 64 GLN B CA 1 ATOM 2092 C C . GLN B 2 66 ? 63.487 26.116 -16.305 1.00 28.29 ? 64 GLN B C 1 ATOM 2093 O O . GLN B 2 66 ? 62.395 25.629 -15.991 1.00 19.40 ? 64 GLN B O 1 ATOM 2094 C CB . GLN B 2 66 ? 63.090 28.221 -14.973 1.00 28.08 ? 64 GLN B CB 1 ATOM 2095 C CG . GLN B 2 66 ? 63.400 29.716 -14.767 1.00 28.05 ? 64 GLN B CG 1 ATOM 2096 C CD . GLN B 2 66 ? 64.894 30.022 -14.861 1.00 38.50 ? 64 GLN B CD 1 ATOM 2097 O OE1 . GLN B 2 66 ? 65.338 30.764 -15.742 1.00 42.42 ? 64 GLN B OE1 1 ATOM 2098 N NE2 . GLN B 2 66 ? 65.672 29.457 -13.945 1.00 34.38 ? 64 GLN B NE2 1 ATOM 2099 N N . LYS B 2 67 ? 64.504 25.399 -16.759 1.00 27.83 ? 65 LYS B N 1 ATOM 2100 C CA . LYS B 2 67 ? 64.417 23.964 -16.981 1.00 28.26 ? 65 LYS B CA 1 ATOM 2101 C C . LYS B 2 67 ? 63.939 23.202 -15.736 1.00 24.67 ? 65 LYS B C 1 ATOM 2102 O O . LYS B 2 67 ? 63.158 22.261 -15.847 1.00 19.87 ? 65 LYS B O 1 ATOM 2103 C CB . LYS B 2 67 ? 65.774 23.455 -17.473 1.00 33.19 ? 65 LYS B CB 1 ATOM 2104 C CG . LYS B 2 67 ? 65.823 21.981 -17.733 1.00 45.86 ? 65 LYS B CG 1 ATOM 2105 C CD . LYS B 2 67 ? 66.697 21.308 -16.707 1.00 47.25 ? 65 LYS B CD 1 ATOM 2106 C CE . LYS B 2 67 ? 66.592 19.809 -16.825 1.00 41.97 ? 65 LYS B CE 1 ATOM 2107 N NZ . LYS B 2 67 ? 67.401 19.150 -15.782 1.00 40.28 ? 65 LYS B NZ 1 ATOM 2108 N N . ASP B 2 68 ? 64.391 23.614 -14.553 1.00 23.18 ? 66 ASP B N 1 ATOM 2109 C CA . ASP B 2 68 ? 63.949 22.965 -13.318 1.00 20.01 ? 66 ASP B CA 1 ATOM 2110 C C . ASP B 2 68 ? 62.441 23.126 -13.054 1.00 24.64 ? 66 ASP B C 1 ATOM 2111 O O . ASP B 2 68 ? 61.772 22.174 -12.646 1.00 22.24 ? 66 ASP B O 1 ATOM 2112 C CB . ASP B 2 68 ? 64.765 23.438 -12.107 1.00 25.17 ? 66 ASP B CB 1 ATOM 2113 C CG . ASP B 2 68 ? 64.707 24.950 -11.899 1.00 31.08 ? 66 ASP B CG 1 ATOM 2114 O OD1 . ASP B 2 68 ? 64.495 25.701 -12.874 1.00 35.83 ? 66 ASP B OD1 1 ATOM 2115 O OD2 . ASP B 2 68 ? 64.870 25.387 -10.745 1.00 40.70 ? 66 ASP B OD2 1 ATOM 2116 N N . ILE B 2 69 ? 61.914 24.325 -13.274 1.00 21.54 ? 67 ILE B N 1 ATOM 2117 C CA . ILE B 2 69 ? 60.470 24.535 -13.184 1.00 19.81 ? 67 ILE B CA 1 ATOM 2118 C C . ILE B 2 69 ? 59.728 23.665 -14.191 1.00 20.82 ? 67 ILE B C 1 ATOM 2119 O O . ILE B 2 69 ? 58.780 22.975 -13.826 1.00 17.50 ? 67 ILE B O 1 ATOM 2120 C CB . ILE B 2 69 ? 60.092 26.018 -13.418 1.00 24.78 ? 67 ILE B CB 1 ATOM 2121 C CG1 . ILE B 2 69 ? 60.710 26.907 -12.340 1.00 27.13 ? 67 ILE B CG1 1 ATOM 2122 C CG2 . ILE B 2 69 ? 58.567 26.186 -13.488 1.00 23.55 ? 67 ILE B CG2 1 ATOM 2123 C CD1 . ILE B 2 69 ? 60.462 28.407 -12.571 1.00 33.00 ? 67 ILE B CD1 1 ATOM 2124 N N . LEU B 2 70 ? 60.151 23.699 -15.457 1.00 18.52 ? 68 LEU B N 1 ATOM 2125 C CA . LEU B 2 70 ? 59.529 22.853 -16.484 1.00 19.33 ? 68 LEU B CA 1 ATOM 2126 C C . LEU B 2 70 ? 59.502 21.375 -16.098 1.00 24.49 ? 68 LEU B C 1 ATOM 2127 O O . LEU B 2 70 ? 58.479 20.713 -16.245 1.00 22.60 ? 68 LEU B O 1 ATOM 2128 C CB . LEU B 2 70 ? 60.224 23.004 -17.840 1.00 26.27 ? 68 LEU B CB 1 ATOM 2129 C CG . LEU B 2 70 ? 59.956 24.265 -18.661 1.00 28.13 ? 68 LEU B CG 1 ATOM 2130 C CD1 . LEU B 2 70 ? 60.878 24.323 -19.878 1.00 21.33 ? 68 LEU B CD1 1 ATOM 2131 C CD2 . LEU B 2 70 ? 58.485 24.340 -19.090 1.00 27.21 ? 68 LEU B CD2 1 ATOM 2132 N N . GLU B 2 71 ? 60.613 20.846 -15.597 1.00 20.76 ? 69 GLU B N 1 ATOM 2133 C CA . GLU B 2 71 ? 60.623 19.428 -15.269 1.00 20.08 ? 69 GLU B CA 1 ATOM 2134 C C . GLU B 2 71 ? 59.756 19.087 -14.050 1.00 17.30 ? 69 GLU B C 1 ATOM 2135 O O . GLU B 2 71 ? 59.207 17.983 -13.978 1.00 16.63 ? 69 GLU B O 1 ATOM 2136 C CB . GLU B 2 71 ? 62.056 18.883 -15.143 1.00 20.73 ? 69 GLU B CB 1 ATOM 2137 C CG . GLU B 2 71 ? 62.805 18.841 -16.493 1.00 18.86 ? 69 GLU B CG 1 ATOM 2138 C CD . GLU B 2 71 ? 62.095 17.993 -17.550 1.00 23.93 ? 69 GLU B CD 1 ATOM 2139 O OE1 . GLU B 2 71 ? 61.322 17.076 -17.191 1.00 26.86 ? 69 GLU B OE1 1 ATOM 2140 O OE2 . GLU B 2 71 ? 62.312 18.235 -18.757 1.00 21.56 ? 69 GLU B OE2 1 ATOM 2141 N N . ASP B 2 72 ? 59.606 20.028 -13.116 1.00 21.16 ? 70 ASP B N 1 ATOM 2142 C CA . ASP B 2 72 ? 58.669 19.816 -12.002 1.00 22.44 ? 70 ASP B CA 1 ATOM 2143 C C . ASP B 2 72 ? 57.254 19.700 -12.561 1.00 17.77 ? 70 ASP B C 1 ATOM 2144 O O . ASP B 2 72 ? 56.461 18.850 -12.140 1.00 18.65 ? 70 ASP B O 1 ATOM 2145 C CB . ASP B 2 72 ? 58.706 20.978 -11.010 1.00 14.82 ? 70 ASP B CB 1 ATOM 2146 C CG . ASP B 2 72 ? 59.913 20.946 -10.095 1.00 29.61 ? 70 ASP B CG 1 ATOM 2147 O OD1 . ASP B 2 72 ? 60.530 19.871 -9.923 1.00 26.93 ? 70 ASP B OD1 1 ATOM 2148 O OD2 . ASP B 2 72 ? 60.244 22.018 -9.539 1.00 32.39 ? 70 ASP B OD2 1 ATOM 2149 N N . GLU B 2 73 ? 56.940 20.578 -13.504 1.00 19.83 ? 71 GLU B N 1 ATOM 2150 C CA . GLU B 2 73 ? 55.625 20.582 -14.138 1.00 13.85 ? 71 GLU B CA 1 ATOM 2151 C C . GLU B 2 73 ? 55.396 19.292 -14.921 1.00 14.63 ? 71 GLU B C 1 ATOM 2152 O O . GLU B 2 73 ? 54.318 18.702 -14.861 1.00 19.39 ? 71 GLU B O 1 ATOM 2153 C CB . GLU B 2 73 ? 55.491 21.796 -15.055 1.00 16.65 ? 71 GLU B CB 1 ATOM 2154 C CG . GLU B 2 73 ? 55.409 23.131 -14.321 1.00 18.49 ? 71 GLU B CG 1 ATOM 2155 C CD . GLU B 2 73 ? 54.184 23.231 -13.436 1.00 26.65 ? 71 GLU B CD 1 ATOM 2156 O OE1 . GLU B 2 73 ? 53.147 23.783 -13.890 1.00 19.38 ? 71 GLU B OE1 1 ATOM 2157 O OE2 . GLU B 2 73 ? 54.253 22.757 -12.278 1.00 27.57 ? 71 GLU B OE2 1 ATOM 2158 N N . ARG B 2 74 ? 56.419 18.842 -15.645 1.00 15.21 ? 72 ARG B N 1 ATOM 2159 C CA . ARG B 2 74 ? 56.282 17.649 -16.489 1.00 20.03 ? 72 ARG B CA 1 ATOM 2160 C C . ARG B 2 74 ? 56.097 16.362 -15.689 1.00 24.15 ? 72 ARG B C 1 ATOM 2161 O O . ARG B 2 74 ? 55.442 15.423 -16.158 1.00 18.44 ? 72 ARG B O 1 ATOM 2162 C CB . ARG B 2 74 ? 57.489 17.522 -17.426 1.00 20.17 ? 72 ARG B CB 1 ATOM 2163 C CG . ARG B 2 74 ? 57.506 18.611 -18.479 1.00 21.14 ? 72 ARG B CG 1 ATOM 2164 C CD . ARG B 2 74 ? 58.860 18.782 -19.132 1.00 21.17 ? 72 ARG B CD 1 ATOM 2165 N NE . ARG B 2 74 ? 58.773 19.801 -20.169 1.00 22.41 ? 72 ARG B NE 1 ATOM 2166 C CZ . ARG B 2 74 ? 59.815 20.288 -20.833 1.00 26.90 ? 72 ARG B CZ 1 ATOM 2167 N NH1 . ARG B 2 74 ? 61.048 19.852 -20.571 1.00 20.48 ? 72 ARG B NH1 1 ATOM 2168 N NH2 . ARG B 2 74 ? 59.617 21.223 -21.755 1.00 24.51 ? 72 ARG B NH2 1 ATOM 2169 N N . ALA B 2 75 ? 56.660 16.319 -14.481 1.00 17.53 ? 73 ALA B N 1 ATOM 2170 C CA . ALA B 2 75 ? 56.553 15.114 -13.653 1.00 19.34 ? 73 ALA B CA 1 ATOM 2171 C C . ALA B 2 75 ? 55.233 15.055 -12.898 1.00 17.65 ? 73 ALA B C 1 ATOM 2172 O O . ALA B 2 75 ? 54.811 13.988 -12.459 1.00 17.74 ? 73 ALA B O 1 ATOM 2173 C CB . ALA B 2 75 ? 57.718 15.025 -12.668 1.00 19.45 ? 73 ALA B CB 1 ATOM 2174 N N . ALA B 2 76 ? 54.594 16.207 -12.740 1.00 16.93 ? 74 ALA B N 1 ATOM 2175 C CA . ALA B 2 76 ? 53.413 16.327 -11.890 1.00 19.88 ? 74 ALA B CA 1 ATOM 2176 C C . ALA B 2 76 ? 52.301 15.304 -12.157 1.00 19.28 ? 74 ALA B C 1 ATOM 2177 O O . ALA B 2 76 ? 51.664 14.843 -11.200 1.00 17.92 ? 74 ALA B O 1 ATOM 2178 C CB . ALA B 2 76 ? 52.861 17.766 -11.922 1.00 15.89 ? 74 ALA B CB 1 ATOM 2179 N N . VAL B 2 77 ? 52.070 14.929 -13.421 1.00 17.78 ? 75 VAL B N 1 ATOM 2180 C CA . VAL B 2 77 ? 51.058 13.893 -13.705 1.00 20.38 ? 75 VAL B CA 1 ATOM 2181 C C . VAL B 2 77 ? 51.315 12.649 -12.854 1.00 30.33 ? 75 VAL B C 1 ATOM 2182 O O . VAL B 2 77 ? 50.377 11.997 -12.379 1.00 23.41 ? 75 VAL B O 1 ATOM 2183 C CB . VAL B 2 77 ? 50.973 13.462 -15.205 1.00 28.24 ? 75 VAL B CB 1 ATOM 2184 C CG1 . VAL B 2 77 ? 50.235 14.502 -16.025 1.00 31.79 ? 75 VAL B CG1 1 ATOM 2185 C CG2 . VAL B 2 77 ? 52.363 13.134 -15.803 1.00 21.49 ? 75 VAL B CG2 1 ATOM 2186 N N . ASP B 2 78 ? 52.593 12.349 -12.638 1.00 24.84 ? 76 ASP B N 1 ATOM 2187 C CA . ASP B 2 78 ? 52.980 11.188 -11.850 1.00 22.41 ? 76 ASP B CA 1 ATOM 2188 C C . ASP B 2 78 ? 53.113 11.484 -10.358 1.00 26.56 ? 76 ASP B C 1 ATOM 2189 O O . ASP B 2 78 ? 52.446 10.855 -9.535 1.00 20.97 ? 76 ASP B O 1 ATOM 2190 C CB . ASP B 2 78 ? 54.286 10.596 -12.383 1.00 20.14 ? 76 ASP B CB 1 ATOM 2191 C CG . ASP B 2 78 ? 54.096 9.885 -13.702 1.00 22.80 ? 76 ASP B CG 1 ATOM 2192 O OD1 . ASP B 2 78 ? 52.956 9.437 -13.979 1.00 27.47 ? 76 ASP B OD1 1 ATOM 2193 O OD2 . ASP B 2 78 ? 55.078 9.777 -14.460 1.00 29.77 ? 76 ASP B OD2 1 ATOM 2194 N N . THR B 2 79 ? 53.981 12.438 -10.019 1.00 22.40 ? 77 THR B N 1 ATOM 2195 C CA . THR B 2 79 ? 54.340 12.698 -8.626 1.00 21.86 ? 77 THR B CA 1 ATOM 2196 C C . THR B 2 79 ? 53.255 13.432 -7.849 1.00 21.73 ? 77 THR B C 1 ATOM 2197 O O . THR B 2 79 ? 53.280 13.470 -6.623 1.00 22.58 ? 77 THR B O 1 ATOM 2198 C CB . THR B 2 79 ? 55.616 13.552 -8.549 1.00 18.06 ? 77 THR B CB 1 ATOM 2199 O OG1 . THR B 2 79 ? 55.349 14.819 -9.150 1.00 18.16 ? 77 THR B OG1 1 ATOM 2200 C CG2 . THR B 2 79 ? 56.768 12.848 -9.295 1.00 22.92 ? 77 THR B CG2 1 ATOM 2201 N N . TYR B 2 80 ? 52.314 14.033 -8.569 1.00 18.50 ? 78 TYR B N 1 ATOM 2202 C CA . TYR B 2 80 ? 51.277 14.841 -7.945 1.00 17.89 ? 78 TYR B CA 1 ATOM 2203 C C . TYR B 2 80 ? 49.890 14.234 -8.205 1.00 20.57 ? 78 TYR B C 1 ATOM 2204 O O . TYR B 2 80 ? 49.235 13.746 -7.287 1.00 16.33 ? 78 TYR B O 1 ATOM 2205 C CB . TYR B 2 80 ? 51.357 16.277 -8.477 1.00 17.78 ? 78 TYR B CB 1 ATOM 2206 C CG . TYR B 2 80 ? 50.261 17.214 -7.996 1.00 15.00 ? 78 TYR B CG 1 ATOM 2207 C CD1 . TYR B 2 80 ? 50.109 17.505 -6.645 1.00 14.66 ? 78 TYR B CD1 1 ATOM 2208 C CD2 . TYR B 2 80 ? 49.422 17.846 -8.902 1.00 17.64 ? 78 TYR B CD2 1 ATOM 2209 C CE1 . TYR B 2 80 ? 49.116 18.390 -6.204 1.00 14.70 ? 78 TYR B CE1 1 ATOM 2210 C CE2 . TYR B 2 80 ? 48.426 18.733 -8.478 1.00 12.30 ? 78 TYR B CE2 1 ATOM 2211 C CZ . TYR B 2 80 ? 48.286 18.999 -7.133 1.00 20.10 ? 78 TYR B CZ 1 ATOM 2212 O OH . TYR B 2 80 ? 47.308 19.863 -6.712 1.00 24.25 ? 78 TYR B OH 1 ATOM 2213 N N . CYS B 2 81 ? 49.464 14.237 -9.463 1.00 16.45 ? 79 CYS B N 1 ATOM 2214 C CA . CYS B 2 81 ? 48.160 13.675 -9.822 1.00 18.75 ? 79 CYS B CA 1 ATOM 2215 C C . CYS B 2 81 ? 48.000 12.189 -9.487 1.00 22.42 ? 79 CYS B C 1 ATOM 2216 O O . CYS B 2 81 ? 47.128 11.816 -8.691 1.00 21.59 ? 79 CYS B O 1 ATOM 2217 C CB . CYS B 2 81 ? 47.883 13.903 -11.311 1.00 18.49 ? 79 CYS B CB 1 ATOM 2218 S SG . CYS B 2 81 ? 47.860 15.648 -11.747 1.00 18.61 ? 79 CYS B SG 1 ATOM 2219 N N . ARG B 2 82 ? 48.815 11.330 -10.094 1.00 20.33 ? 80 ARG B N 1 ATOM 2220 C CA . ARG B 2 82 ? 48.668 9.895 -9.839 1.00 18.22 ? 80 ARG B CA 1 ATOM 2221 C C . ARG B 2 82 ? 48.869 9.575 -8.358 1.00 24.26 ? 80 ARG B C 1 ATOM 2222 O O . ARG B 2 82 ? 48.138 8.753 -7.803 1.00 23.67 ? 80 ARG B O 1 ATOM 2223 C CB . ARG B 2 82 ? 49.588 9.037 -10.721 1.00 24.39 ? 80 ARG B CB 1 ATOM 2224 C CG . ARG B 2 82 ? 49.107 8.908 -12.169 1.00 24.94 ? 80 ARG B CG 1 ATOM 2225 C CD . ARG B 2 82 ? 49.953 7.943 -12.995 1.00 25.43 ? 80 ARG B CD 1 ATOM 2226 N NE . ARG B 2 82 ? 49.307 7.664 -14.277 1.00 26.28 ? 80 ARG B NE 1 ATOM 2227 C CZ . ARG B 2 82 ? 49.436 8.425 -15.360 1.00 28.25 ? 80 ARG B CZ 1 ATOM 2228 N NH1 . ARG B 2 82 ? 50.208 9.505 -15.328 1.00 28.35 ? 80 ARG B NH1 1 ATOM 2229 N NH2 . ARG B 2 82 ? 48.802 8.104 -16.478 1.00 28.51 ? 80 ARG B NH2 1 ATOM 2230 N N . HIS B 2 83 ? 49.830 10.247 -7.719 1.00 20.90 ? 81 HIS B N 1 ATOM 2231 C CA . HIS B 2 83 ? 50.081 10.049 -6.287 1.00 22.09 ? 81 HIS B CA 1 ATOM 2232 C C . HIS B 2 83 ? 48.864 10.369 -5.424 1.00 22.57 ? 81 HIS B C 1 ATOM 2233 O O . HIS B 2 83 ? 48.428 9.558 -4.593 1.00 21.86 ? 81 HIS B O 1 ATOM 2234 C CB . HIS B 2 83 ? 51.271 10.891 -5.795 1.00 20.58 ? 81 HIS B CB 1 ATOM 2235 C CG . HIS B 2 83 ? 51.481 10.803 -4.312 1.00 26.66 ? 81 HIS B CG 1 ATOM 2236 N ND1 . HIS B 2 83 ? 52.272 9.835 -3.726 1.00 29.01 ? 81 HIS B ND1 1 ATOM 2237 C CD2 . HIS B 2 83 ? 50.953 11.524 -3.293 1.00 21.54 ? 81 HIS B CD2 1 ATOM 2238 C CE1 . HIS B 2 83 ? 52.246 9.984 -2.412 1.00 28.82 ? 81 HIS B CE1 1 ATOM 2239 N NE2 . HIS B 2 83 ? 51.456 11.006 -2.123 1.00 28.24 ? 81 HIS B NE2 1 ATOM 2240 N N . ASN B 2 84 ? 48.310 11.558 -5.618 1.00 20.31 ? 82 ASN B N 1 ATOM 2241 C CA . ASN B 2 84 ? 47.189 11.983 -4.800 1.00 17.10 ? 82 ASN B CA 1 ATOM 2242 C C . ASN B 2 84 ? 45.940 11.152 -5.061 1.00 17.23 ? 82 ASN B C 1 ATOM 2243 O O . ASN B 2 84 ? 45.140 10.916 -4.153 1.00 24.29 ? 82 ASN B O 1 ATOM 2244 C CB . ASN B 2 84 ? 46.937 13.484 -4.980 1.00 15.77 ? 82 ASN B CB 1 ATOM 2245 C CG . ASN B 2 84 ? 47.956 14.328 -4.229 1.00 19.52 ? 82 ASN B CG 1 ATOM 2246 O OD1 . ASN B 2 84 ? 48.622 13.840 -3.312 1.00 22.31 ? 82 ASN B OD1 1 ATOM 2247 N ND2 . ASN B 2 84 ? 48.075 15.593 -4.602 1.00 15.20 ? 82 ASN B ND2 1 ATOM 2248 N N . TYR B 2 85 ? 45.781 10.682 -6.294 1.00 23.27 ? 83 TYR B N 1 ATOM 2249 C CA . TYR B 2 85 ? 44.640 9.834 -6.618 1.00 21.87 ? 83 TYR B CA 1 ATOM 2250 C C . TYR B 2 85 ? 44.751 8.588 -5.753 1.00 27.62 ? 83 TYR B C 1 ATOM 2251 O O . TYR B 2 85 ? 43.775 8.140 -5.149 1.00 25.98 ? 83 TYR B O 1 ATOM 2252 C CB . TYR B 2 85 ? 44.637 9.475 -8.110 1.00 22.87 ? 83 TYR B CB 1 ATOM 2253 C CG . TYR B 2 85 ? 43.429 8.670 -8.583 1.00 22.94 ? 83 TYR B CG 1 ATOM 2254 C CD1 . TYR B 2 85 ? 42.330 9.302 -9.162 1.00 27.17 ? 83 TYR B CD1 1 ATOM 2255 C CD2 . TYR B 2 85 ? 43.396 7.277 -8.461 1.00 25.95 ? 83 TYR B CD2 1 ATOM 2256 C CE1 . TYR B 2 85 ? 41.234 8.572 -9.605 1.00 25.70 ? 83 TYR B CE1 1 ATOM 2257 C CE2 . TYR B 2 85 ? 42.308 6.543 -8.904 1.00 28.43 ? 83 TYR B CE2 1 ATOM 2258 C CZ . TYR B 2 85 ? 41.229 7.198 -9.471 1.00 29.61 ? 83 TYR B CZ 1 ATOM 2259 O OH . TYR B 2 85 ? 40.153 6.467 -9.912 1.00 33.63 ? 83 TYR B OH 1 ATOM 2260 N N . GLY B 2 86 ? 45.959 8.040 -5.686 1.00 29.82 ? 84 GLY B N 1 ATOM 2261 C CA . GLY B 2 86 ? 46.225 6.906 -4.835 1.00 22.47 ? 84 GLY B CA 1 ATOM 2262 C C . GLY B 2 86 ? 45.847 7.184 -3.398 1.00 22.34 ? 84 GLY B C 1 ATOM 2263 O O . GLY B 2 86 ? 45.258 6.340 -2.735 1.00 25.07 ? 84 GLY B O 1 ATOM 2264 N N . VAL B 2 87 ? 46.164 8.378 -2.914 1.00 22.34 ? 85 VAL B N 1 ATOM 2265 C CA . VAL B 2 87 ? 45.961 8.677 -1.500 1.00 25.86 ? 85 VAL B CA 1 ATOM 2266 C C . VAL B 2 87 ? 44.482 8.777 -1.128 1.00 25.00 ? 85 VAL B C 1 ATOM 2267 O O . VAL B 2 87 ? 44.057 8.275 -0.084 1.00 24.08 ? 85 VAL B O 1 ATOM 2268 C CB . VAL B 2 87 ? 46.694 9.971 -1.088 1.00 30.35 ? 85 VAL B CB 1 ATOM 2269 C CG1 . VAL B 2 87 ? 46.326 10.369 0.341 1.00 29.79 ? 85 VAL B CG1 1 ATOM 2270 C CG2 . VAL B 2 87 ? 48.196 9.778 -1.215 1.00 31.91 ? 85 VAL B CG2 1 ATOM 2271 N N . VAL B 2 88 ? 43.687 9.403 -1.992 1.00 29.49 ? 86 VAL B N 1 ATOM 2272 C CA . VAL B 2 88 ? 42.311 9.724 -1.629 1.00 27.88 ? 86 VAL B CA 1 ATOM 2273 C C . VAL B 2 88 ? 41.235 8.848 -2.276 1.00 25.80 ? 86 VAL B C 1 ATOM 2274 O O . VAL B 2 88 ? 40.066 8.953 -1.916 1.00 27.30 ? 86 VAL B O 1 ATOM 2275 C CB . VAL B 2 88 ? 41.991 11.215 -1.909 1.00 25.26 ? 86 VAL B CB 1 ATOM 2276 C CG1 . VAL B 2 88 ? 43.069 12.100 -1.296 1.00 22.77 ? 86 VAL B CG1 1 ATOM 2277 C CG2 . VAL B 2 88 ? 41.849 11.472 -3.412 1.00 17.56 ? 86 VAL B CG2 1 ATOM 2278 N N . GLU B 2 89 ? 41.615 7.989 -3.219 1.00 21.32 ? 87 GLU B N 1 ATOM 2279 C CA . GLU B 2 89 ? 40.607 7.276 -4.014 1.00 25.06 ? 87 GLU B CA 1 ATOM 2280 C C . GLU B 2 89 ? 39.642 6.417 -3.195 1.00 25.01 ? 87 GLU B C 1 ATOM 2281 O O . GLU B 2 89 ? 38.469 6.261 -3.570 1.00 23.24 ? 87 GLU B O 1 ATOM 2282 C CB . GLU B 2 89 ? 41.240 6.479 -5.167 1.00 30.98 ? 87 GLU B CB 1 ATOM 2283 C CG . GLU B 2 89 ? 42.019 5.256 -4.772 1.00 40.98 ? 87 GLU B CG 1 ATOM 2284 C CD . GLU B 2 89 ? 41.161 4.008 -4.819 1.00 59.94 ? 87 GLU B CD 1 ATOM 2285 O OE1 . GLU B 2 89 ? 41.039 3.340 -3.771 1.00 68.40 ? 87 GLU B OE1 1 ATOM 2286 O OE2 . GLU B 2 89 ? 40.599 3.704 -5.898 1.00 60.53 ? 87 GLU B OE2 1 ATOM 2287 N N . SER B 2 90 ? 40.112 5.882 -2.069 1.00 27.99 ? 88 SER B N 1 ATOM 2288 C CA . SER B 2 90 ? 39.277 4.958 -1.292 1.00 34.93 ? 88 SER B CA 1 ATOM 2289 C C . SER B 2 90 ? 38.058 5.638 -0.658 1.00 33.97 ? 88 SER B C 1 ATOM 2290 O O . SER B 2 90 ? 37.023 4.991 -0.448 1.00 30.79 ? 88 SER B O 1 ATOM 2291 C CB . SER B 2 90 ? 40.091 4.210 -0.231 1.00 32.97 ? 88 SER B CB 1 ATOM 2292 O OG . SER B 2 90 ? 40.425 5.050 0.856 1.00 34.20 ? 88 SER B OG 1 ATOM 2293 N N . PHE B 2 91 ? 38.167 6.938 -0.369 1.00 23.93 ? 89 PHE B N 1 ATOM 2294 C CA . PHE B 2 91 ? 37.051 7.648 0.253 1.00 27.24 ? 89 PHE B CA 1 ATOM 2295 C C . PHE B 2 91 ? 36.422 8.690 -0.651 1.00 26.02 ? 89 PHE B C 1 ATOM 2296 O O . PHE B 2 91 ? 35.527 9.416 -0.224 1.00 28.56 ? 89 PHE B O 1 ATOM 2297 C CB . PHE B 2 91 ? 37.446 8.266 1.598 1.00 28.41 ? 89 PHE B CB 1 ATOM 2298 C CG . PHE B 2 91 ? 38.652 9.168 1.535 1.00 29.74 ? 89 PHE B CG 1 ATOM 2299 C CD1 . PHE B 2 91 ? 38.512 10.526 1.272 1.00 28.30 ? 89 PHE B CD1 1 ATOM 2300 C CD2 . PHE B 2 91 ? 39.924 8.659 1.763 1.00 32.39 ? 89 PHE B CD2 1 ATOM 2301 C CE1 . PHE B 2 91 ? 39.623 11.361 1.229 1.00 33.34 ? 89 PHE B CE1 1 ATOM 2302 C CE2 . PHE B 2 91 ? 41.045 9.487 1.718 1.00 33.00 ? 89 PHE B CE2 1 ATOM 2303 C CZ . PHE B 2 91 ? 40.893 10.840 1.452 1.00 32.31 ? 89 PHE B CZ 1 ATOM 2304 N N . THR B 2 92 ? 36.886 8.765 -1.896 1.00 22.27 ? 90 THR B N 1 ATOM 2305 C CA . THR B 2 92 ? 36.339 9.716 -2.855 1.00 23.76 ? 90 THR B CA 1 ATOM 2306 C C . THR B 2 92 ? 35.804 8.995 -4.087 1.00 25.34 ? 90 THR B C 1 ATOM 2307 O O . THR B 2 92 ? 34.589 8.909 -4.291 1.00 25.05 ? 90 THR B O 1 ATOM 2308 C CB . THR B 2 92 ? 37.391 10.760 -3.277 1.00 25.15 ? 90 THR B CB 1 ATOM 2309 O OG1 . THR B 2 92 ? 38.554 10.088 -3.777 1.00 21.21 ? 90 THR B OG1 1 ATOM 2310 C CG2 . THR B 2 92 ? 37.783 11.623 -2.090 1.00 22.69 ? 90 THR B CG2 1 ATOM 2311 N N . VAL B 2 93 ? 36.721 8.472 -4.896 1.00 23.30 ? 91 VAL B N 1 ATOM 2312 C CA . VAL B 2 93 ? 36.383 7.663 -6.064 1.00 24.33 ? 91 VAL B CA 1 ATOM 2313 C C . VAL B 2 93 ? 35.429 6.509 -5.737 1.00 25.17 ? 91 VAL B C 1 ATOM 2314 O O . VAL B 2 93 ? 34.476 6.256 -6.482 1.00 27.32 ? 91 VAL B O 1 ATOM 2315 C CB . VAL B 2 93 ? 37.668 7.086 -6.715 1.00 22.14 ? 91 VAL B CB 1 ATOM 2316 C CG1 . VAL B 2 93 ? 37.332 6.117 -7.850 1.00 26.16 ? 91 VAL B CG1 1 ATOM 2317 C CG2 . VAL B 2 93 ? 38.553 8.228 -7.205 1.00 17.85 ? 91 VAL B CG2 1 ATOM 2318 N N . GLN B 2 94 ? 35.687 5.822 -4.623 1.00 23.60 ? 92 GLN B N 1 ATOM 2319 C CA . GLN B 2 94 ? 34.931 4.621 -4.254 1.00 26.12 ? 92 GLN B CA 1 ATOM 2320 C C . GLN B 2 94 ? 33.740 4.927 -3.353 1.00 27.76 ? 92 GLN B C 1 ATOM 2321 O O . GLN B 2 94 ? 33.000 4.017 -2.974 1.00 32.03 ? 92 GLN B O 1 ATOM 2322 C CB . GLN B 2 94 ? 35.826 3.604 -3.534 1.00 26.54 ? 92 GLN B CB 1 ATOM 2323 C CG . GLN B 2 94 ? 37.079 3.195 -4.291 1.00 32.63 ? 92 GLN B CG 1 ATOM 2324 C CD . GLN B 2 94 ? 37.767 2.011 -3.629 1.00 45.98 ? 92 GLN B CD 1 ATOM 2325 O OE1 . GLN B 2 94 ? 37.159 1.295 -2.833 1.00 53.04 ? 92 GLN B OE1 1 ATOM 2326 N NE2 . GLN B 2 94 ? 39.034 1.803 -3.952 1.00 51.21 ? 92 GLN B NE2 1 ATOM 2327 N N . ARG B 2 95 ? 33.563 6.195 -2.996 1.00 22.13 ? 93 ARG B N 1 ATOM 2328 C CA . ARG B 2 95 ? 32.460 6.585 -2.119 1.00 27.17 ? 93 ARG B CA 1 ATOM 2329 C C . ARG B 2 95 ? 31.107 6.273 -2.751 1.00 26.26 ? 93 ARG B C 1 ATOM 2330 O O . ARG B 2 95 ? 30.830 6.680 -3.882 1.00 21.71 ? 93 ARG B O 1 ATOM 2331 C CB . ARG B 2 95 ? 32.542 8.079 -1.777 1.00 28.27 ? 93 ARG B CB 1 ATOM 2332 C CG . ARG B 2 95 ? 31.403 8.595 -0.911 1.00 24.57 ? 93 ARG B CG 1 ATOM 2333 C CD . ARG B 2 95 ? 31.664 10.053 -0.528 1.00 23.22 ? 93 ARG B CD 1 ATOM 2334 N NE . ARG B 2 95 ? 30.532 10.677 0.152 1.00 19.37 ? 93 ARG B NE 1 ATOM 2335 C CZ . ARG B 2 95 ? 30.258 10.521 1.437 1.00 23.33 ? 93 ARG B CZ 1 ATOM 2336 N NH1 . ARG B 2 95 ? 31.026 9.736 2.183 1.00 22.01 ? 93 ARG B NH1 1 ATOM 2337 N NH2 . ARG B 2 95 ? 29.212 11.145 1.976 1.00 21.04 ? 93 ARG B NH2 1 ATOM 2338 N N . ARG B 2 96 ? 30.275 5.549 -2.009 1.00 24.05 ? 94 ARG B N 1 ATOM 2339 C CA . ARG B 2 96 ? 28.907 5.238 -2.422 1.00 30.25 ? 94 ARG B CA 1 ATOM 2340 C C . ARG B 2 96 ? 27.941 5.425 -1.256 1.00 30.48 ? 94 ARG B C 1 ATOM 2341 O O . ARG B 2 96 ? 28.052 4.748 -0.230 1.00 30.85 ? 94 ARG B O 1 ATOM 2342 C CB . ARG B 2 96 ? 28.790 3.787 -2.886 1.00 33.76 ? 94 ARG B CB 1 ATOM 2343 C CG . ARG B 2 96 ? 29.673 3.414 -4.046 1.00 34.43 ? 94 ARG B CG 1 ATOM 2344 C CD . ARG B 2 96 ? 29.152 3.984 -5.340 1.00 28.78 ? 94 ARG B CD 1 ATOM 2345 N NE . ARG B 2 96 ? 29.972 3.526 -6.455 1.00 42.07 ? 94 ARG B NE 1 ATOM 2346 C CZ . ARG B 2 96 ? 31.049 4.164 -6.905 1.00 46.53 ? 94 ARG B CZ 1 ATOM 2347 N NH1 . ARG B 2 96 ? 31.439 5.301 -6.344 1.00 48.92 ? 94 ARG B NH1 1 ATOM 2348 N NH2 . ARG B 2 96 ? 31.735 3.664 -7.921 1.00 44.62 ? 94 ARG B NH2 1 ATOM 2349 N N . VAL B 2 97 ? 26.992 6.339 -1.421 1.00 23.69 ? 95 VAL B N 1 ATOM 2350 C CA . VAL B 2 97 ? 25.942 6.530 -0.437 1.00 24.58 ? 95 VAL B CA 1 ATOM 2351 C C . VAL B 2 97 ? 24.574 6.416 -1.112 1.00 23.04 ? 95 VAL B C 1 ATOM 2352 O O . VAL B 2 97 ? 24.238 7.190 -2.010 1.00 20.08 ? 95 VAL B O 1 ATOM 2353 C CB . VAL B 2 97 ? 26.065 7.888 0.269 1.00 27.60 ? 95 VAL B CB 1 ATOM 2354 C CG1 . VAL B 2 97 ? 25.058 7.975 1.421 1.00 30.44 ? 95 VAL B CG1 1 ATOM 2355 C CG2 . VAL B 2 97 ? 27.491 8.089 0.773 1.00 24.62 ? 95 VAL B CG2 1 ATOM 2356 N N . TYR B 2 98 ? 23.782 5.443 -0.687 1.00 21.34 ? 96 TYR B N 1 ATOM 2357 C CA . TYR B 2 98 ? 22.501 5.232 -1.341 1.00 25.20 ? 96 TYR B CA 1 ATOM 2358 C C . TYR B 2 98 ? 21.475 6.271 -0.894 1.00 21.57 ? 96 TYR B C 1 ATOM 2359 O O . TYR B 2 98 ? 21.589 6.832 0.188 1.00 24.05 ? 96 TYR B O 1 ATOM 2360 C CB . TYR B 2 98 ? 22.018 3.777 -1.211 1.00 30.77 ? 96 TYR B CB 1 ATOM 2361 C CG . TYR B 2 98 ? 21.687 3.266 0.179 1.00 34.22 ? 96 TYR B CG 1 ATOM 2362 C CD1 . TYR B 2 98 ? 20.452 3.544 0.766 1.00 36.25 ? 96 TYR B CD1 1 ATOM 2363 C CD2 . TYR B 2 98 ? 22.579 2.455 0.876 1.00 26.73 ? 96 TYR B CD2 1 ATOM 2364 C CE1 . TYR B 2 98 ? 20.124 3.063 2.021 1.00 38.63 ? 96 TYR B CE1 1 ATOM 2365 C CE2 . TYR B 2 98 ? 22.262 1.962 2.142 1.00 33.38 ? 96 TYR B CE2 1 ATOM 2366 C CZ . TYR B 2 98 ? 21.028 2.269 2.709 1.00 40.62 ? 96 TYR B CZ 1 ATOM 2367 O OH . TYR B 2 98 ? 20.682 1.794 3.962 1.00 37.37 ? 96 TYR B OH 1 ATOM 2368 N N . PRO B 2 99 ? 20.499 6.568 -1.755 1.00 22.66 ? 97 PRO B N 1 ATOM 2369 C CA . PRO B 2 99 ? 19.534 7.617 -1.426 1.00 23.88 ? 97 PRO B CA 1 ATOM 2370 C C . PRO B 2 99 ? 18.384 7.130 -0.548 1.00 24.56 ? 97 PRO B C 1 ATOM 2371 O O . PRO B 2 99 ? 18.034 5.949 -0.616 1.00 25.74 ? 97 PRO B O 1 ATOM 2372 C CB . PRO B 2 99 ? 18.975 7.986 -2.798 1.00 24.38 ? 97 PRO B CB 1 ATOM 2373 C CG . PRO B 2 99 ? 19.072 6.739 -3.585 1.00 27.94 ? 97 PRO B CG 1 ATOM 2374 C CD . PRO B 2 99 ? 20.359 6.099 -3.148 1.00 25.58 ? 97 PRO B CD 1 ATOM 2375 N N A GLU B 2 100 ? 17.844 8.012 0.295 0.46 20.60 ? 98 GLU B N 1 ATOM 2376 N N B GLU B 2 100 ? 17.805 8.022 0.249 0.54 20.56 ? 98 GLU B N 1 ATOM 2377 C CA A GLU B 2 100 ? 16.521 7.787 0.866 0.46 23.27 ? 98 GLU B CA 1 ATOM 2378 C CA B GLU B 2 100 ? 16.538 7.747 0.913 0.54 21.98 ? 98 GLU B CA 1 ATOM 2379 C C A GLU B 2 100 ? 15.571 8.217 -0.226 0.46 24.93 ? 98 GLU B C 1 ATOM 2380 C C B GLU B 2 100 ? 15.445 8.329 0.018 0.54 23.44 ? 98 GLU B C 1 ATOM 2381 O O A GLU B 2 100 ? 15.849 9.164 -0.974 0.46 19.49 ? 98 GLU B O 1 ATOM 2382 O O B GLU B 2 100 ? 15.508 9.504 -0.356 0.54 19.84 ? 98 GLU B O 1 ATOM 2383 C CB A GLU B 2 100 ? 16.248 8.629 2.126 0.46 27.66 ? 98 GLU B CB 1 ATOM 2384 C CB B GLU B 2 100 ? 16.496 8.410 2.289 0.54 24.07 ? 98 GLU B CB 1 ATOM 2385 C CG A GLU B 2 100 ? 16.138 10.144 1.866 0.46 35.33 ? 98 GLU B CG 1 ATOM 2386 C CG B GLU B 2 100 ? 17.733 8.177 3.138 0.54 25.31 ? 98 GLU B CG 1 ATOM 2387 C CD A GLU B 2 100 ? 14.769 10.787 2.184 0.46 35.34 ? 98 GLU B CD 1 ATOM 2388 C CD B GLU B 2 100 ? 17.720 6.827 3.822 0.54 34.84 ? 98 GLU B CD 1 ATOM 2389 O OE1 A GLU B 2 100 ? 13.934 10.970 1.253 0.46 21.05 ? 98 GLU B OE1 1 ATOM 2390 O OE1 B GLU B 2 100 ? 16.618 6.281 4.046 0.54 38.59 ? 98 GLU B OE1 1 ATOM 2391 O OE2 A GLU B 2 100 ? 14.554 11.163 3.361 0.46 27.14 ? 98 GLU B OE2 1 ATOM 2392 O OE2 B GLU B 2 100 ? 18.813 6.312 4.135 0.54 39.81 ? 98 GLU B OE2 1 ATOM 2393 N N . VAL B 2 101 ? 14.460 7.509 -0.340 1.00 21.21 ? 99 VAL B N 1 ATOM 2394 C CA . VAL B 2 101 ? 13.434 7.908 -1.287 1.00 21.87 ? 99 VAL B CA 1 ATOM 2395 C C . VAL B 2 101 ? 12.110 8.012 -0.559 1.00 30.14 ? 99 VAL B C 1 ATOM 2396 O O . VAL B 2 101 ? 11.711 7.087 0.154 1.00 30.52 ? 99 VAL B O 1 ATOM 2397 C CB . VAL B 2 101 ? 13.329 6.919 -2.463 1.00 22.72 ? 99 VAL B CB 1 ATOM 2398 C CG1 . VAL B 2 101 ? 12.351 7.439 -3.506 1.00 25.68 ? 99 VAL B CG1 1 ATOM 2399 C CG2 . VAL B 2 101 ? 14.698 6.690 -3.084 1.00 24.44 ? 99 VAL B CG2 1 ATOM 2400 N N . THR B 2 102 ? 11.453 9.157 -0.720 1.00 21.23 ? 100 THR B N 1 ATOM 2401 C CA . THR B 2 102 ? 10.135 9.404 -0.143 1.00 27.80 ? 100 THR B CA 1 ATOM 2402 C C . THR B 2 102 ? 9.205 9.880 -1.261 1.00 31.39 ? 100 THR B C 1 ATOM 2403 O O . THR B 2 102 ? 9.631 10.610 -2.154 1.00 28.23 ? 100 THR B O 1 ATOM 2404 C CB . THR B 2 102 ? 10.208 10.519 0.923 1.00 27.76 ? 100 THR B CB 1 ATOM 2405 O OG1 . THR B 2 102 ? 11.132 10.146 1.946 1.00 40.30 ? 100 THR B OG1 1 ATOM 2406 C CG2 . THR B 2 102 ? 8.850 10.764 1.557 1.00 41.67 ? 100 THR B CG2 1 ATOM 2407 N N . VAL B 2 103 ? 7.948 9.454 -1.221 1.00 26.01 ? 101 VAL B N 1 ATOM 2408 C CA . VAL B 2 103 ? 6.941 9.963 -2.142 1.00 26.53 ? 101 VAL B CA 1 ATOM 2409 C C . VAL B 2 103 ? 5.797 10.574 -1.343 1.00 32.04 ? 101 VAL B C 1 ATOM 2410 O O . VAL B 2 103 ? 5.304 9.964 -0.399 1.00 27.97 ? 101 VAL B O 1 ATOM 2411 C CB . VAL B 2 103 ? 6.372 8.872 -3.072 1.00 31.32 ? 101 VAL B CB 1 ATOM 2412 C CG1 . VAL B 2 103 ? 5.204 9.434 -3.885 1.00 27.50 ? 101 VAL B CG1 1 ATOM 2413 C CG2 . VAL B 2 103 ? 7.464 8.318 -3.993 1.00 21.41 ? 101 VAL B CG2 1 ATOM 2414 N N . TYR B 2 104 ? 5.384 11.782 -1.713 1.00 34.53 ? 102 TYR B N 1 ATOM 2415 C CA . TYR B 2 104 ? 4.273 12.442 -1.038 1.00 28.57 ? 102 TYR B CA 1 ATOM 2416 C C . TYR B 2 104 ? 3.521 13.404 -1.974 1.00 26.60 ? 102 TYR B C 1 ATOM 2417 O O . TYR B 2 104 ? 4.115 13.990 -2.881 1.00 28.22 ? 102 TYR B O 1 ATOM 2418 C CB . TYR B 2 104 ? 4.779 13.168 0.213 1.00 25.36 ? 102 TYR B CB 1 ATOM 2419 C CG . TYR B 2 104 ? 5.846 14.220 -0.038 1.00 30.00 ? 102 TYR B CG 1 ATOM 2420 C CD1 . TYR B 2 104 ? 5.497 15.519 -0.388 1.00 36.24 ? 102 TYR B CD1 1 ATOM 2421 C CD2 . TYR B 2 104 ? 7.198 13.920 0.100 1.00 34.69 ? 102 TYR B CD2 1 ATOM 2422 C CE1 . TYR B 2 104 ? 6.460 16.492 -0.601 1.00 38.77 ? 102 TYR B CE1 1 ATOM 2423 C CE2 . TYR B 2 104 ? 8.177 14.893 -0.110 1.00 40.30 ? 102 TYR B CE2 1 ATOM 2424 C CZ . TYR B 2 104 ? 7.797 16.177 -0.464 1.00 43.03 ? 102 TYR B CZ 1 ATOM 2425 O OH . TYR B 2 104 ? 8.744 17.157 -0.682 1.00 42.64 ? 102 TYR B OH 1 ATOM 2426 N N . PRO B 2 105 ? 2.206 13.549 -1.764 1.00 27.01 ? 103 PRO B N 1 ATOM 2427 C CA . PRO B 2 105 ? 1.404 14.493 -2.554 1.00 28.26 ? 103 PRO B CA 1 ATOM 2428 C C . PRO B 2 105 ? 1.676 15.953 -2.176 1.00 33.52 ? 103 PRO B C 1 ATOM 2429 O O . PRO B 2 105 ? 2.114 16.235 -1.062 1.00 39.28 ? 103 PRO B O 1 ATOM 2430 C CB . PRO B 2 105 ? -0.033 14.111 -2.194 1.00 31.38 ? 103 PRO B CB 1 ATOM 2431 C CG . PRO B 2 105 ? 0.075 13.484 -0.821 1.00 31.16 ? 103 PRO B CG 1 ATOM 2432 C CD . PRO B 2 105 ? 1.377 12.745 -0.844 1.00 25.48 ? 103 PRO B CD 1 ATOM 2433 N N . ALA B 2 106 ? 1.414 16.865 -3.107 1.00 33.06 ? 104 ALA B N 1 ATOM 2434 C CA . ALA B 2 106 ? 1.587 18.297 -2.875 1.00 32.65 ? 104 ALA B CA 1 ATOM 2435 C C . ALA B 2 106 ? 0.570 19.089 -3.701 1.00 39.52 ? 104 ALA B C 1 ATOM 2436 O O . ALA B 2 106 ? -0.257 18.507 -4.417 1.00 29.98 ? 104 ALA B O 1 ATOM 2437 C CB . ALA B 2 106 ? 3.013 18.722 -3.213 1.00 30.00 ? 104 ALA B CB 1 ATOM 2438 N N . LYS B 2 107 ? 0.627 20.414 -3.598 1.00 50.14 ? 105 LYS B N 1 ATOM 2439 C CA . LYS B 2 107 ? -0.330 21.280 -4.284 1.00 54.35 ? 105 LYS B CA 1 ATOM 2440 C C . LYS B 2 107 ? 0.382 22.332 -5.128 1.00 58.16 ? 105 LYS B C 1 ATOM 2441 O O . LYS B 2 107 ? 1.373 22.917 -4.691 1.00 60.45 ? 105 LYS B O 1 ATOM 2442 C CB . LYS B 2 107 ? -1.241 21.981 -3.275 1.00 56.52 ? 105 LYS B CB 1 ATOM 2443 C CG . LYS B 2 107 ? -2.054 21.058 -2.381 1.00 58.81 ? 105 LYS B CG 1 ATOM 2444 C CD . LYS B 2 107 ? -2.792 21.868 -1.322 1.00 63.64 ? 105 LYS B CD 1 ATOM 2445 C CE . LYS B 2 107 ? -3.485 20.983 -0.293 1.00 69.34 ? 105 LYS B CE 1 ATOM 2446 N NZ . LYS B 2 107 ? -4.753 20.388 -0.798 1.00 73.40 ? 105 LYS B NZ 1 ATOM 2447 N N . THR B 2 108 ? -0.122 22.569 -6.337 1.00 57.68 ? 106 THR B N 1 ATOM 2448 C CA . THR B 2 108 ? 0.400 23.643 -7.177 1.00 64.36 ? 106 THR B CA 1 ATOM 2449 C C . THR B 2 108 ? -0.091 24.985 -6.631 1.00 72.26 ? 106 THR B C 1 ATOM 2450 O O . THR B 2 108 ? 0.548 26.023 -6.812 1.00 78.05 ? 106 THR B O 1 ATOM 2451 C CB . THR B 2 108 ? -0.014 23.478 -8.660 1.00 59.93 ? 106 THR B CB 1 ATOM 2452 O OG1 . THR B 2 108 ? -1.443 23.420 -8.762 1.00 59.31 ? 106 THR B OG1 1 ATOM 2453 C CG2 . THR B 2 108 ? 0.593 22.208 -9.254 1.00 52.87 ? 106 THR B CG2 1 ATOM 2454 N N . GLN B 2 109 ? -1.236 24.947 -5.960 1.00 71.67 ? 107 GLN B N 1 ATOM 2455 C CA . GLN B 2 109 ? -1.748 26.096 -5.225 1.00 78.89 ? 107 GLN B CA 1 ATOM 2456 C C . GLN B 2 109 ? -2.255 25.621 -3.868 1.00 79.85 ? 107 GLN B C 1 ATOM 2457 O O . GLN B 2 109 ? -2.995 24.637 -3.790 1.00 75.16 ? 107 GLN B O 1 ATOM 2458 C CB . GLN B 2 109 ? -2.868 26.789 -6.000 1.00 82.02 ? 107 GLN B CB 1 ATOM 2459 C CG . GLN B 2 109 ? -2.430 27.393 -7.323 1.00 80.48 ? 107 GLN B CG 1 ATOM 2460 C CD . GLN B 2 109 ? -3.581 28.030 -8.071 1.00 83.22 ? 107 GLN B CD 1 ATOM 2461 O OE1 . GLN B 2 109 ? -3.774 27.778 -9.259 1.00 83.88 ? 107 GLN B OE1 1 ATOM 2462 N NE2 . GLN B 2 109 ? -4.354 28.863 -7.379 1.00 86.73 ? 107 GLN B NE2 1 ATOM 2463 N N . PRO B 2 110 ? -1.852 26.320 -2.793 1.00 84.27 ? 108 PRO B N 1 ATOM 2464 C CA . PRO B 2 110 ? -2.132 25.916 -1.407 1.00 86.89 ? 108 PRO B CA 1 ATOM 2465 C C . PRO B 2 110 ? -3.617 25.670 -1.089 1.00 87.65 ? 108 PRO B C 1 ATOM 2466 O O . PRO B 2 110 ? -3.920 24.961 -0.125 1.00 85.88 ? 108 PRO B O 1 ATOM 2467 C CB . PRO B 2 110 ? -1.590 27.096 -0.588 1.00 87.16 ? 108 PRO B CB 1 ATOM 2468 C CG . PRO B 2 110 ? -0.514 27.678 -1.447 1.00 83.46 ? 108 PRO B CG 1 ATOM 2469 C CD . PRO B 2 110 ? -1.017 27.534 -2.856 1.00 82.84 ? 108 PRO B CD 1 ATOM 2470 N N . LEU B 2 111 ? -4.520 26.230 -1.891 1.00 87.51 ? 109 LEU B N 1 ATOM 2471 C CA . LEU B 2 111 ? -5.956 26.102 -1.640 1.00 87.20 ? 109 LEU B CA 1 ATOM 2472 C C . LEU B 2 111 ? -6.593 24.868 -2.298 1.00 84.41 ? 109 LEU B C 1 ATOM 2473 O O . LEU B 2 111 ? -7.586 24.336 -1.800 1.00 79.54 ? 109 LEU B O 1 ATOM 2474 C CB . LEU B 2 111 ? -6.688 27.373 -2.080 1.00 87.52 ? 109 LEU B CB 1 ATOM 2475 N N . GLN B 2 112 ? -6.015 24.416 -3.407 1.00 86.27 ? 110 GLN B N 1 ATOM 2476 C CA . GLN B 2 112 ? -6.561 23.290 -4.168 1.00 87.42 ? 110 GLN B CA 1 ATOM 2477 C C . GLN B 2 112 ? -6.509 21.956 -3.413 1.00 82.05 ? 110 GLN B C 1 ATOM 2478 O O . GLN B 2 112 ? -6.120 21.895 -2.242 1.00 80.67 ? 110 GLN B O 1 ATOM 2479 C CB . GLN B 2 112 ? -5.790 23.124 -5.483 1.00 88.91 ? 110 GLN B CB 1 ATOM 2480 C CG . GLN B 2 112 ? -5.706 24.365 -6.356 1.00 91.16 ? 110 GLN B CG 1 ATOM 2481 C CD . GLN B 2 112 ? -4.687 24.206 -7.474 1.00 89.86 ? 110 GLN B CD 1 ATOM 2482 O OE1 . GLN B 2 112 ? -3.607 23.648 -7.267 1.00 86.46 ? 110 GLN B OE1 1 ATOM 2483 N NE2 . GLN B 2 112 ? -5.029 24.687 -8.666 1.00 90.11 ? 110 GLN B NE2 1 ATOM 2484 N N . HIS B 2 113 ? -6.912 20.891 -4.105 1.00 73.74 ? 111 HIS B N 1 ATOM 2485 C CA . HIS B 2 113 ? -6.652 19.525 -3.662 1.00 59.92 ? 111 HIS B CA 1 ATOM 2486 C C . HIS B 2 113 ? -5.248 19.150 -4.141 1.00 51.60 ? 111 HIS B C 1 ATOM 2487 O O . HIS B 2 113 ? -4.536 19.983 -4.701 1.00 44.69 ? 111 HIS B O 1 ATOM 2488 C CB . HIS B 2 113 ? -7.679 18.551 -4.253 1.00 61.57 ? 111 HIS B CB 1 ATOM 2489 C CG . HIS B 2 113 ? -9.102 18.860 -3.887 1.00 67.01 ? 111 HIS B CG 1 ATOM 2490 N ND1 . HIS B 2 113 ? -9.795 19.929 -4.415 1.00 69.46 ? 111 HIS B ND1 1 ATOM 2491 C CD2 . HIS B 2 113 ? -9.966 18.227 -3.055 1.00 71.28 ? 111 HIS B CD2 1 ATOM 2492 C CE1 . HIS B 2 113 ? -11.021 19.947 -3.920 1.00 70.05 ? 111 HIS B CE1 1 ATOM 2493 N NE2 . HIS B 2 113 ? -11.152 18.925 -3.093 1.00 71.94 ? 111 HIS B NE2 1 ATOM 2494 N N . HIS B 2 114 ? -4.850 17.901 -3.936 1.00 50.03 ? 112 HIS B N 1 ATOM 2495 C CA . HIS B 2 114 ? -3.532 17.453 -4.384 1.00 48.59 ? 112 HIS B CA 1 ATOM 2496 C C . HIS B 2 114 ? -3.494 17.247 -5.900 1.00 42.83 ? 112 HIS B C 1 ATOM 2497 O O . HIS B 2 114 ? -4.368 16.593 -6.477 1.00 41.83 ? 112 HIS B O 1 ATOM 2498 C CB . HIS B 2 114 ? -3.113 16.184 -3.634 1.00 49.20 ? 112 HIS B CB 1 ATOM 2499 C CG . HIS B 2 114 ? -2.813 16.416 -2.185 1.00 55.77 ? 112 HIS B CG 1 ATOM 2500 N ND1 . HIS B 2 114 ? -3.247 15.570 -1.187 1.00 57.33 ? 112 HIS B ND1 1 ATOM 2501 C CD2 . HIS B 2 114 ? -2.125 17.407 -1.566 1.00 57.86 ? 112 HIS B CD2 1 ATOM 2502 C CE1 . HIS B 2 114 ? -2.840 16.028 -0.016 1.00 58.54 ? 112 HIS B CE1 1 ATOM 2503 N NE2 . HIS B 2 114 ? -2.158 17.142 -0.218 1.00 59.18 ? 112 HIS B NE2 1 ATOM 2504 N N . ASN B 2 115 ? -2.496 17.840 -6.545 1.00 35.80 ? 113 ASN B N 1 ATOM 2505 C CA . ASN B 2 115 ? -2.361 17.738 -7.997 1.00 32.50 ? 113 ASN B CA 1 ATOM 2506 C C . ASN B 2 115 ? -0.899 17.638 -8.407 1.00 28.61 ? 113 ASN B C 1 ATOM 2507 O O . ASN B 2 115 ? -0.509 17.961 -9.531 1.00 27.29 ? 113 ASN B O 1 ATOM 2508 C CB . ASN B 2 115 ? -3.093 18.881 -8.723 1.00 33.87 ? 113 ASN B CB 1 ATOM 2509 C CG . ASN B 2 115 ? -2.589 20.265 -8.328 1.00 37.75 ? 113 ASN B CG 1 ATOM 2510 O OD1 . ASN B 2 115 ? -1.607 20.403 -7.611 1.00 29.73 ? 113 ASN B OD1 1 ATOM 2511 N ND2 . ASN B 2 115 ? -3.274 21.298 -8.804 1.00 45.77 ? 113 ASN B ND2 1 ATOM 2512 N N . LEU B 2 116 ? -0.095 17.158 -7.469 1.00 27.82 ? 114 LEU B N 1 ATOM 2513 C CA . LEU B 2 116 ? 1.331 17.062 -7.657 1.00 31.85 ? 114 LEU B CA 1 ATOM 2514 C C . LEU B 2 116 ? 1.849 15.916 -6.796 1.00 34.21 ? 114 LEU B C 1 ATOM 2515 O O . LEU B 2 116 ? 1.495 15.816 -5.622 1.00 33.76 ? 114 LEU B O 1 ATOM 2516 C CB . LEU B 2 116 ? 1.968 18.381 -7.227 1.00 37.90 ? 114 LEU B CB 1 ATOM 2517 C CG . LEU B 2 116 ? 3.391 18.671 -7.669 1.00 46.48 ? 114 LEU B CG 1 ATOM 2518 C CD1 . LEU B 2 116 ? 3.442 18.777 -9.185 1.00 44.67 ? 114 LEU B CD1 1 ATOM 2519 C CD2 . LEU B 2 116 ? 3.860 19.959 -7.013 1.00 47.31 ? 114 LEU B CD2 1 ATOM 2520 N N . LEU B 2 117 ? 2.664 15.039 -7.377 1.00 22.81 ? 115 LEU B N 1 ATOM 2521 C CA . LEU B 2 117 ? 3.343 14.003 -6.595 1.00 25.71 ? 115 LEU B CA 1 ATOM 2522 C C . LEU B 2 117 ? 4.836 14.267 -6.527 1.00 24.88 ? 115 LEU B C 1 ATOM 2523 O O . LEU B 2 117 ? 5.490 14.432 -7.554 1.00 23.69 ? 115 LEU B O 1 ATOM 2524 C CB . LEU B 2 117 ? 3.107 12.613 -7.187 1.00 23.26 ? 115 LEU B CB 1 ATOM 2525 C CG . LEU B 2 117 ? 1.684 12.073 -7.088 1.00 24.98 ? 115 LEU B CG 1 ATOM 2526 C CD1 . LEU B 2 117 ? 1.632 10.660 -7.626 1.00 30.22 ? 115 LEU B CD1 1 ATOM 2527 C CD2 . LEU B 2 117 ? 1.194 12.119 -5.647 1.00 29.44 ? 115 LEU B CD2 1 ATOM 2528 N N . VAL B 2 118 ? 5.383 14.290 -5.317 1.00 21.17 ? 116 VAL B N 1 ATOM 2529 C CA . VAL B 2 118 ? 6.808 14.536 -5.158 1.00 20.38 ? 116 VAL B CA 1 ATOM 2530 C C . VAL B 2 118 ? 7.567 13.244 -4.843 1.00 24.81 ? 116 VAL B C 1 ATOM 2531 O O . VAL B 2 118 ? 7.224 12.510 -3.909 1.00 20.49 ? 116 VAL B O 1 ATOM 2532 C CB . VAL B 2 118 ? 7.095 15.587 -4.060 1.00 22.94 ? 116 VAL B CB 1 ATOM 2533 C CG1 . VAL B 2 118 ? 8.580 16.008 -4.088 1.00 24.72 ? 116 VAL B CG1 1 ATOM 2534 C CG2 . VAL B 2 118 ? 6.197 16.811 -4.238 1.00 23.56 ? 116 VAL B CG2 1 ATOM 2535 N N . CYS B 2 119 ? 8.596 12.970 -5.637 1.00 20.51 ? 117 CYS B N 1 ATOM 2536 C CA . CYS B 2 119 ? 9.554 11.941 -5.279 1.00 25.19 ? 117 CYS B CA 1 ATOM 2537 C C . CYS B 2 119 ? 10.827 12.591 -4.763 1.00 24.82 ? 117 CYS B C 1 ATOM 2538 O O . CYS B 2 119 ? 11.618 13.126 -5.543 1.00 22.69 ? 117 CYS B O 1 ATOM 2539 C CB . CYS B 2 119 ? 9.882 11.040 -6.462 1.00 18.74 ? 117 CYS B CB 1 ATOM 2540 S SG . CYS B 2 119 ? 10.989 9.689 -5.962 1.00 23.38 ? 117 CYS B SG 1 ATOM 2541 N N . SER B 2 120 ? 11.019 12.556 -3.445 1.00 21.21 ? 118 SER B N 1 ATOM 2542 C CA . SER B 2 120 ? 12.188 13.179 -2.839 1.00 19.58 ? 118 SER B CA 1 ATOM 2543 C C . SER B 2 120 ? 13.305 12.150 -2.726 1.00 22.86 ? 118 SER B C 1 ATOM 2544 O O . SER B 2 120 ? 13.133 11.113 -2.090 1.00 26.14 ? 118 SER B O 1 ATOM 2545 C CB . SER B 2 120 ? 11.842 13.743 -1.459 1.00 24.28 ? 118 SER B CB 1 ATOM 2546 O OG . SER B 2 120 ? 12.917 14.502 -0.941 1.00 25.73 ? 118 SER B OG 1 ATOM 2547 N N . VAL B 2 121 ? 14.441 12.438 -3.354 1.00 21.56 ? 119 VAL B N 1 ATOM 2548 C CA . VAL B 2 121 ? 15.587 11.536 -3.337 1.00 17.68 ? 119 VAL B CA 1 ATOM 2549 C C . VAL B 2 121 ? 16.736 12.232 -2.610 1.00 20.62 ? 119 VAL B C 1 ATOM 2550 O O . VAL B 2 121 ? 17.286 13.220 -3.110 1.00 16.46 ? 119 VAL B O 1 ATOM 2551 C CB . VAL B 2 121 ? 15.990 11.159 -4.772 1.00 18.34 ? 119 VAL B CB 1 ATOM 2552 C CG1 . VAL B 2 121 ? 17.103 10.122 -4.768 1.00 18.10 ? 119 VAL B CG1 1 ATOM 2553 C CG2 . VAL B 2 121 ? 14.775 10.620 -5.521 1.00 17.09 ? 119 VAL B CG2 1 ATOM 2554 N N . ASN B 2 122 ? 17.070 11.750 -1.414 1.00 19.81 ? 120 ASN B N 1 ATOM 2555 C CA . ASN B 2 122 ? 17.996 12.479 -0.532 1.00 18.23 ? 120 ASN B CA 1 ATOM 2556 C C . ASN B 2 122 ? 19.199 11.705 -0.065 1.00 18.63 ? 120 ASN B C 1 ATOM 2557 O O . ASN B 2 122 ? 19.102 10.526 0.293 1.00 19.47 ? 120 ASN B O 1 ATOM 2558 C CB . ASN B 2 122 ? 17.294 12.978 0.741 1.00 20.33 ? 120 ASN B CB 1 ATOM 2559 C CG . ASN B 2 122 ? 16.151 13.886 0.453 1.00 30.78 ? 120 ASN B CG 1 ATOM 2560 O OD1 . ASN B 2 122 ? 15.034 13.431 0.192 1.00 28.65 ? 120 ASN B OD1 1 ATOM 2561 N ND2 . ASN B 2 122 ? 16.409 15.192 0.507 1.00 24.40 ? 120 ASN B ND2 1 ATOM 2562 N N . GLY B 2 123 ? 20.326 12.401 -0.014 1.00 17.87 ? 121 GLY B N 1 ATOM 2563 C CA . GLY B 2 123 ? 21.470 11.945 0.746 1.00 20.76 ? 121 GLY B CA 1 ATOM 2564 C C . GLY B 2 123 ? 22.436 11.081 -0.023 1.00 22.54 ? 121 GLY B C 1 ATOM 2565 O O . GLY B 2 123 ? 23.283 10.439 0.584 1.00 23.19 ? 121 GLY B O 1 ATOM 2566 N N . PHE B 2 124 ? 22.332 11.082 -1.348 1.00 19.33 ? 122 PHE B N 1 ATOM 2567 C CA . PHE B 2 124 ? 23.111 10.155 -2.170 1.00 19.97 ? 122 PHE B CA 1 ATOM 2568 C C . PHE B 2 124 ? 24.463 10.682 -2.649 1.00 23.84 ? 122 PHE B C 1 ATOM 2569 O O . PHE B 2 124 ? 24.698 11.897 -2.694 1.00 19.38 ? 122 PHE B O 1 ATOM 2570 C CB . PHE B 2 124 ? 22.288 9.646 -3.365 1.00 20.30 ? 122 PHE B CB 1 ATOM 2571 C CG . PHE B 2 124 ? 21.804 10.728 -4.297 1.00 20.62 ? 122 PHE B CG 1 ATOM 2572 C CD1 . PHE B 2 124 ? 22.596 11.162 -5.352 1.00 23.04 ? 122 PHE B CD1 1 ATOM 2573 C CD2 . PHE B 2 124 ? 20.546 11.290 -4.133 1.00 24.55 ? 122 PHE B CD2 1 ATOM 2574 C CE1 . PHE B 2 124 ? 22.149 12.142 -6.220 1.00 24.04 ? 122 PHE B CE1 1 ATOM 2575 C CE2 . PHE B 2 124 ? 20.085 12.276 -4.998 1.00 23.78 ? 122 PHE B CE2 1 ATOM 2576 C CZ . PHE B 2 124 ? 20.897 12.708 -6.048 1.00 20.69 ? 122 PHE B CZ 1 ATOM 2577 N N . TYR B 2 125 ? 25.355 9.747 -2.969 1.00 20.59 ? 123 TYR B N 1 ATOM 2578 C CA . TYR B 2 125 ? 26.658 10.059 -3.573 1.00 18.24 ? 123 TYR B CA 1 ATOM 2579 C C . TYR B 2 125 ? 27.127 8.853 -4.376 1.00 19.03 ? 123 TYR B C 1 ATOM 2580 O O . TYR B 2 125 ? 27.021 7.726 -3.897 1.00 26.13 ? 123 TYR B O 1 ATOM 2581 C CB . TYR B 2 125 ? 27.721 10.386 -2.514 1.00 19.15 ? 123 TYR B CB 1 ATOM 2582 C CG . TYR B 2 125 ? 28.956 10.976 -3.155 1.00 24.61 ? 123 TYR B CG 1 ATOM 2583 C CD1 . TYR B 2 125 ? 29.074 12.350 -3.323 1.00 25.15 ? 123 TYR B CD1 1 ATOM 2584 C CD2 . TYR B 2 125 ? 29.973 10.163 -3.643 1.00 19.03 ? 123 TYR B CD2 1 ATOM 2585 C CE1 . TYR B 2 125 ? 30.176 12.903 -3.935 1.00 21.51 ? 123 TYR B CE1 1 ATOM 2586 C CE2 . TYR B 2 125 ? 31.093 10.709 -4.268 1.00 21.41 ? 123 TYR B CE2 1 ATOM 2587 C CZ . TYR B 2 125 ? 31.183 12.081 -4.405 1.00 19.97 ? 123 TYR B CZ 1 ATOM 2588 O OH . TYR B 2 125 ? 32.270 12.648 -5.023 1.00 18.28 ? 123 TYR B OH 1 ATOM 2589 N N . PRO B 2 126 ? 27.665 9.075 -5.594 1.00 22.80 ? 124 PRO B N 1 ATOM 2590 C CA . PRO B 2 126 ? 27.891 10.359 -6.276 1.00 21.82 ? 124 PRO B CA 1 ATOM 2591 C C . PRO B 2 126 ? 26.626 10.949 -6.870 1.00 25.08 ? 124 PRO B C 1 ATOM 2592 O O . PRO B 2 126 ? 25.516 10.506 -6.553 1.00 19.34 ? 124 PRO B O 1 ATOM 2593 C CB . PRO B 2 126 ? 28.893 10.002 -7.385 1.00 26.21 ? 124 PRO B CB 1 ATOM 2594 C CG . PRO B 2 126 ? 28.644 8.561 -7.660 1.00 28.08 ? 124 PRO B CG 1 ATOM 2595 C CD . PRO B 2 126 ? 28.249 7.945 -6.339 1.00 23.25 ? 124 PRO B CD 1 ATOM 2596 N N . GLY B 2 127 ? 26.792 11.944 -7.732 1.00 23.49 ? 125 GLY B N 1 ATOM 2597 C CA . GLY B 2 127 ? 25.663 12.740 -8.184 1.00 25.80 ? 125 GLY B CA 1 ATOM 2598 C C . GLY B 2 127 ? 24.828 12.165 -9.310 1.00 25.54 ? 125 GLY B C 1 ATOM 2599 O O . GLY B 2 127 ? 23.655 12.502 -9.435 1.00 31.37 ? 125 GLY B O 1 ATOM 2600 N N . SER B 2 128 ? 25.423 11.307 -10.132 1.00 23.13 ? 126 SER B N 1 ATOM 2601 C CA . SER B 2 128 ? 24.719 10.733 -11.278 1.00 23.29 ? 126 SER B CA 1 ATOM 2602 C C . SER B 2 128 ? 23.564 9.840 -10.826 1.00 19.97 ? 126 SER B C 1 ATOM 2603 O O . SER B 2 128 ? 23.770 8.848 -10.141 1.00 24.52 ? 126 SER B O 1 ATOM 2604 C CB . SER B 2 128 ? 25.677 9.898 -12.111 1.00 30.29 ? 126 SER B CB 1 ATOM 2605 O OG . SER B 2 128 ? 26.076 8.766 -11.362 1.00 44.01 ? 126 SER B OG 1 ATOM 2606 N N . ILE B 2 129 ? 22.350 10.187 -11.223 1.00 23.74 ? 127 ILE B N 1 ATOM 2607 C CA . ILE B 2 129 ? 21.182 9.445 -10.765 1.00 25.67 ? 127 ILE B CA 1 ATOM 2608 C C . ILE B 2 129 ? 20.094 9.496 -11.832 1.00 23.09 ? 127 ILE B C 1 ATOM 2609 O O . ILE B 2 129 ? 20.037 10.432 -12.629 1.00 29.11 ? 127 ILE B O 1 ATOM 2610 C CB . ILE B 2 129 ? 20.673 10.022 -9.423 1.00 20.15 ? 127 ILE B CB 1 ATOM 2611 C CG1 . ILE B 2 129 ? 19.705 9.053 -8.734 1.00 23.33 ? 127 ILE B CG1 1 ATOM 2612 C CG2 . ILE B 2 129 ? 20.068 11.415 -9.629 1.00 19.79 ? 127 ILE B CG2 1 ATOM 2613 C CD1 . ILE B 2 129 ? 19.567 9.298 -7.269 1.00 22.49 ? 127 ILE B CD1 1 ATOM 2614 N N . GLU B 2 130 ? 19.249 8.478 -11.876 1.00 24.22 ? 128 GLU B N 1 ATOM 2615 C CA . GLU B 2 130 ? 18.147 8.473 -12.828 1.00 27.50 ? 128 GLU B CA 1 ATOM 2616 C C . GLU B 2 130 ? 16.858 8.249 -12.064 1.00 27.70 ? 128 GLU B C 1 ATOM 2617 O O . GLU B 2 130 ? 16.697 7.235 -11.383 1.00 24.09 ? 128 GLU B O 1 ATOM 2618 C CB . GLU B 2 130 ? 18.350 7.393 -13.901 1.00 35.84 ? 128 GLU B CB 1 ATOM 2619 C CG . GLU B 2 130 ? 17.256 7.320 -14.978 1.00 40.43 ? 128 GLU B CG 1 ATOM 2620 C CD . GLU B 2 130 ? 17.410 8.357 -16.094 1.00 48.97 ? 128 GLU B CD 1 ATOM 2621 O OE1 . GLU B 2 130 ? 18.523 8.502 -16.650 1.00 49.72 ? 128 GLU B OE1 1 ATOM 2622 O OE2 . GLU B 2 130 ? 16.404 9.023 -16.425 1.00 52.68 ? 128 GLU B OE2 1 ATOM 2623 N N . VAL B 2 131 ? 15.939 9.204 -12.163 1.00 19.05 ? 129 VAL B N 1 ATOM 2624 C CA . VAL B 2 131 ? 14.675 9.100 -11.439 1.00 20.56 ? 129 VAL B CA 1 ATOM 2625 C C . VAL B 2 131 ? 13.505 9.197 -12.413 1.00 23.84 ? 129 VAL B C 1 ATOM 2626 O O . VAL B 2 131 ? 13.393 10.173 -13.169 1.00 22.74 ? 129 VAL B O 1 ATOM 2627 C CB . VAL B 2 131 ? 14.551 10.221 -10.389 1.00 19.54 ? 129 VAL B CB 1 ATOM 2628 C CG1 . VAL B 2 131 ? 13.266 10.052 -9.553 1.00 16.88 ? 129 VAL B CG1 1 ATOM 2629 C CG2 . VAL B 2 131 ? 15.806 10.269 -9.509 1.00 20.43 ? 129 VAL B CG2 1 ATOM 2630 N N . ARG B 2 132 ? 12.643 8.186 -12.387 1.00 20.63 ? 130 ARG B N 1 ATOM 2631 C CA . ARG B 2 132 ? 11.531 8.081 -13.331 1.00 21.75 ? 130 ARG B CA 1 ATOM 2632 C C . ARG B 2 132 ? 10.211 7.816 -12.609 1.00 23.04 ? 130 ARG B C 1 ATOM 2633 O O . ARG B 2 132 ? 10.187 7.154 -11.571 1.00 20.11 ? 130 ARG B O 1 ATOM 2634 C CB . ARG B 2 132 ? 11.813 6.990 -14.377 1.00 23.95 ? 130 ARG B CB 1 ATOM 2635 C CG . ARG B 2 132 ? 13.060 7.295 -15.225 1.00 30.77 ? 130 ARG B CG 1 ATOM 2636 C CD . ARG B 2 132 ? 13.293 6.343 -16.402 1.00 40.13 ? 130 ARG B CD 1 ATOM 2637 N NE . ARG B 2 132 ? 14.231 6.951 -17.349 1.00 45.43 ? 130 ARG B NE 1 ATOM 2638 C CZ . ARG B 2 132 ? 14.129 6.891 -18.676 1.00 50.71 ? 130 ARG B CZ 1 ATOM 2639 N NH1 . ARG B 2 132 ? 13.129 6.231 -19.247 1.00 56.75 ? 130 ARG B NH1 1 ATOM 2640 N NH2 . ARG B 2 132 ? 15.038 7.491 -19.439 1.00 47.34 ? 130 ARG B NH2 1 ATOM 2641 N N . TRP B 2 133 ? 9.123 8.345 -13.167 1.00 21.54 ? 131 TRP B N 1 ATOM 2642 C CA . TRP B 2 133 ? 7.779 8.131 -12.640 1.00 22.26 ? 131 TRP B CA 1 ATOM 2643 C C . TRP B 2 133 ? 7.004 7.128 -13.480 1.00 27.04 ? 131 TRP B C 1 ATOM 2644 O O . TRP B 2 133 ? 7.057 7.154 -14.713 1.00 25.18 ? 131 TRP B O 1 ATOM 2645 C CB . TRP B 2 133 ? 6.993 9.442 -12.609 1.00 21.95 ? 131 TRP B CB 1 ATOM 2646 C CG . TRP B 2 133 ? 7.194 10.260 -11.375 1.00 19.15 ? 131 TRP B CG 1 ATOM 2647 C CD1 . TRP B 2 133 ? 7.923 11.416 -11.261 1.00 22.56 ? 131 TRP B CD1 1 ATOM 2648 C CD2 . TRP B 2 133 ? 6.648 10.001 -10.074 1.00 25.01 ? 131 TRP B CD2 1 ATOM 2649 N NE1 . TRP B 2 133 ? 7.868 11.882 -9.968 1.00 17.33 ? 131 TRP B NE1 1 ATOM 2650 C CE2 . TRP B 2 133 ? 7.090 11.035 -9.221 1.00 18.72 ? 131 TRP B CE2 1 ATOM 2651 C CE3 . TRP B 2 133 ? 5.834 8.991 -9.546 1.00 26.55 ? 131 TRP B CE3 1 ATOM 2652 C CZ2 . TRP B 2 133 ? 6.735 11.096 -7.876 1.00 19.81 ? 131 TRP B CZ2 1 ATOM 2653 C CZ3 . TRP B 2 133 ? 5.482 9.052 -8.205 1.00 26.89 ? 131 TRP B CZ3 1 ATOM 2654 C CH2 . TRP B 2 133 ? 5.938 10.093 -7.385 1.00 26.14 ? 131 TRP B CH2 1 ATOM 2655 N N . PHE B 2 134 ? 6.265 6.263 -12.795 1.00 23.58 ? 132 PHE B N 1 ATOM 2656 C CA . PHE B 2 134 ? 5.413 5.274 -13.437 1.00 27.71 ? 132 PHE B CA 1 ATOM 2657 C C . PHE B 2 134 ? 3.991 5.376 -12.884 1.00 35.01 ? 132 PHE B C 1 ATOM 2658 O O . PHE B 2 134 ? 3.794 5.623 -11.688 1.00 29.25 ? 132 PHE B O 1 ATOM 2659 C CB . PHE B 2 134 ? 5.969 3.865 -13.215 1.00 27.86 ? 132 PHE B CB 1 ATOM 2660 C CG . PHE B 2 134 ? 7.299 3.621 -13.887 1.00 25.63 ? 132 PHE B CG 1 ATOM 2661 C CD1 . PHE B 2 134 ? 7.363 2.945 -15.095 1.00 29.90 ? 132 PHE B CD1 1 ATOM 2662 C CD2 . PHE B 2 134 ? 8.482 4.062 -13.309 1.00 24.44 ? 132 PHE B CD2 1 ATOM 2663 C CE1 . PHE B 2 134 ? 8.574 2.709 -15.721 1.00 26.37 ? 132 PHE B CE1 1 ATOM 2664 C CE2 . PHE B 2 134 ? 9.700 3.834 -13.927 1.00 27.02 ? 132 PHE B CE2 1 ATOM 2665 C CZ . PHE B 2 134 ? 9.750 3.150 -15.136 1.00 28.88 ? 132 PHE B CZ 1 ATOM 2666 N N . ARG B 2 135 ? 3.009 5.223 -13.770 1.00 38.02 ? 133 ARG B N 1 ATOM 2667 C CA . ARG B 2 135 ? 1.610 5.133 -13.372 1.00 42.23 ? 133 ARG B CA 1 ATOM 2668 C C . ARG B 2 135 ? 1.053 3.814 -13.894 1.00 39.97 ? 133 ARG B C 1 ATOM 2669 O O . ARG B 2 135 ? 1.054 3.560 -15.102 1.00 42.18 ? 133 ARG B O 1 ATOM 2670 C CB . ARG B 2 135 ? 0.790 6.314 -13.910 1.00 38.43 ? 133 ARG B CB 1 ATOM 2671 C CG . ARG B 2 135 ? -0.656 6.316 -13.413 1.00 42.86 ? 133 ARG B CG 1 ATOM 2672 C CD . ARG B 2 135 ? -1.567 7.212 -14.243 1.00 42.10 ? 133 ARG B CD 1 ATOM 2673 N NE . ARG B 2 135 ? -1.252 8.625 -14.079 1.00 52.01 ? 133 ARG B NE 1 ATOM 2674 C CZ . ARG B 2 135 ? -0.818 9.414 -15.058 1.00 58.21 ? 133 ARG B CZ 1 ATOM 2675 N NH1 . ARG B 2 135 ? -0.660 8.925 -16.282 1.00 66.81 ? 133 ARG B NH1 1 ATOM 2676 N NH2 . ARG B 2 135 ? -0.553 10.694 -14.816 1.00 51.59 ? 133 ARG B NH2 1 ATOM 2677 N N . ASN B 2 136 ? 0.592 2.971 -12.977 1.00 38.28 ? 134 ASN B N 1 ATOM 2678 C CA . ASN B 2 136 ? 0.119 1.634 -13.319 1.00 42.58 ? 134 ASN B CA 1 ATOM 2679 C C . ASN B 2 136 ? 1.108 0.876 -14.203 1.00 44.81 ? 134 ASN B C 1 ATOM 2680 O O . ASN B 2 136 ? 0.714 0.240 -15.180 1.00 45.67 ? 134 ASN B O 1 ATOM 2681 C CB . ASN B 2 136 ? -1.262 1.693 -13.988 1.00 48.14 ? 134 ASN B CB 1 ATOM 2682 C CG . ASN B 2 136 ? -2.339 2.221 -13.060 1.00 46.30 ? 134 ASN B CG 1 ATOM 2683 O OD1 . ASN B 2 136 ? -2.269 2.044 -11.842 1.00 46.69 ? 134 ASN B OD1 1 ATOM 2684 N ND2 . ASN B 2 136 ? -3.345 2.873 -13.631 1.00 43.36 ? 134 ASN B ND2 1 ATOM 2685 N N . GLY B 2 137 ? 2.394 0.972 -13.874 1.00 42.36 ? 135 GLY B N 1 ATOM 2686 C CA . GLY B 2 137 ? 3.408 0.194 -14.561 1.00 45.70 ? 135 GLY B CA 1 ATOM 2687 C C . GLY B 2 137 ? 3.918 0.793 -15.858 1.00 45.68 ? 135 GLY B C 1 ATOM 2688 O O . GLY B 2 137 ? 4.852 0.262 -16.460 1.00 49.72 ? 135 GLY B O 1 ATOM 2689 N N . GLN B 2 138 ? 3.312 1.896 -16.289 1.00 41.98 ? 136 GLN B N 1 ATOM 2690 C CA . GLN B 2 138 ? 3.715 2.570 -17.519 1.00 40.02 ? 136 GLN B CA 1 ATOM 2691 C C . GLN B 2 138 ? 4.438 3.872 -17.174 1.00 36.04 ? 136 GLN B C 1 ATOM 2692 O O . GLN B 2 138 ? 3.969 4.648 -16.336 1.00 32.71 ? 136 GLN B O 1 ATOM 2693 C CB . GLN B 2 138 ? 2.491 2.842 -18.408 1.00 53.67 ? 136 GLN B CB 1 ATOM 2694 C CG . GLN B 2 138 ? 2.810 3.551 -19.729 1.00 62.30 ? 136 GLN B CG 1 ATOM 2695 C CD . GLN B 2 138 ? 1.615 3.628 -20.678 1.00 70.21 ? 136 GLN B CD 1 ATOM 2696 O OE1 . GLN B 2 138 ? 1.382 2.715 -21.473 1.00 78.02 ? 136 GLN B OE1 1 ATOM 2697 N NE2 . GLN B 2 138 ? 0.861 4.725 -20.604 1.00 64.63 ? 136 GLN B NE2 1 ATOM 2698 N N . GLU B 2 139 ? 5.590 4.113 -17.793 1.00 30.27 ? 137 GLU B N 1 ATOM 2699 C CA . GLU B 2 139 ? 6.332 5.319 -17.455 1.00 29.29 ? 137 GLU B CA 1 ATOM 2700 C C . GLU B 2 139 ? 5.595 6.583 -17.901 1.00 31.53 ? 137 GLU B C 1 ATOM 2701 O O . GLU B 2 139 ? 5.134 6.684 -19.040 1.00 27.99 ? 137 GLU B O 1 ATOM 2702 C CB . GLU B 2 139 ? 7.764 5.314 -18.002 1.00 27.56 ? 137 GLU B CB 1 ATOM 2703 C CG . GLU B 2 139 ? 8.560 6.498 -17.453 1.00 23.14 ? 137 GLU B CG 1 ATOM 2704 C CD . GLU B 2 139 ? 9.949 6.638 -18.047 1.00 34.50 ? 137 GLU B CD 1 ATOM 2705 O OE1 . GLU B 2 139 ? 10.412 5.702 -18.731 1.00 32.66 ? 137 GLU B OE1 1 ATOM 2706 O OE2 . GLU B 2 139 ? 10.579 7.692 -17.812 1.00 34.81 ? 137 GLU B OE2 1 ATOM 2707 N N . GLU B 2 140 ? 5.475 7.527 -16.976 1.00 30.65 ? 138 GLU B N 1 ATOM 2708 C CA . GLU B 2 140 ? 4.907 8.832 -17.261 1.00 32.14 ? 138 GLU B CA 1 ATOM 2709 C C . GLU B 2 140 ? 6.047 9.796 -17.570 1.00 27.84 ? 138 GLU B C 1 ATOM 2710 O O . GLU B 2 140 ? 6.921 10.019 -16.730 1.00 28.64 ? 138 GLU B O 1 ATOM 2711 C CB . GLU B 2 140 ? 4.108 9.332 -16.054 1.00 41.01 ? 138 GLU B CB 1 ATOM 2712 C CG . GLU B 2 140 ? 2.600 9.260 -16.229 1.00 55.25 ? 138 GLU B CG 1 ATOM 2713 C CD . GLU B 2 140 ? 2.089 10.249 -17.268 1.00 58.50 ? 138 GLU B CD 1 ATOM 2714 O OE1 . GLU B 2 140 ? 2.809 11.231 -17.569 1.00 50.11 ? 138 GLU B OE1 1 ATOM 2715 O OE2 . GLU B 2 140 ? 0.972 10.042 -17.792 1.00 60.63 ? 138 GLU B OE2 1 ATOM 2716 N N . LYS B 2 141 ? 6.043 10.350 -18.779 1.00 31.90 ? 139 LYS B N 1 ATOM 2717 C CA . LYS B 2 141 ? 7.102 11.263 -19.213 1.00 29.26 ? 139 LYS B CA 1 ATOM 2718 C C . LYS B 2 141 ? 6.619 12.710 -19.384 1.00 29.61 ? 139 LYS B C 1 ATOM 2719 O O . LYS B 2 141 ? 7.434 13.630 -19.493 1.00 34.24 ? 139 LYS B O 1 ATOM 2720 C CB . LYS B 2 141 ? 7.755 10.754 -20.502 1.00 33.80 ? 139 LYS B CB 1 ATOM 2721 C CG . LYS B 2 141 ? 8.588 9.475 -20.333 1.00 34.31 ? 139 LYS B CG 1 ATOM 2722 C CD . LYS B 2 141 ? 9.342 9.122 -21.621 1.00 36.05 ? 139 LYS B CD 1 ATOM 2723 C CE . LYS B 2 141 ? 10.322 7.967 -21.408 1.00 35.53 ? 139 LYS B CE 1 ATOM 2724 N NZ . LYS B 2 141 ? 10.960 7.516 -22.681 1.00 30.30 ? 139 LYS B NZ 1 ATOM 2725 N N . THR B 2 142 ? 5.304 12.922 -19.390 1.00 26.25 ? 140 THR B N 1 ATOM 2726 C CA . THR B 2 142 ? 4.774 14.291 -19.459 1.00 24.13 ? 140 THR B CA 1 ATOM 2727 C C . THR B 2 142 ? 4.541 14.867 -18.068 1.00 25.06 ? 140 THR B C 1 ATOM 2728 O O . THR B 2 142 ? 4.302 14.129 -17.114 1.00 26.59 ? 140 THR B O 1 ATOM 2729 C CB . THR B 2 142 ? 3.446 14.364 -20.247 1.00 32.34 ? 140 THR B CB 1 ATOM 2730 O OG1 . THR B 2 142 ? 2.387 13.835 -19.441 1.00 41.55 ? 140 THR B OG1 1 ATOM 2731 C CG2 . THR B 2 142 ? 3.542 13.577 -21.556 1.00 24.03 ? 140 THR B CG2 1 ATOM 2732 N N . GLY B 2 143 ? 4.600 16.191 -17.960 1.00 20.92 ? 141 GLY B N 1 ATOM 2733 C CA . GLY B 2 143 ? 4.331 16.870 -16.708 1.00 23.05 ? 141 GLY B CA 1 ATOM 2734 C C . GLY B 2 143 ? 5.311 16.503 -15.601 1.00 25.26 ? 141 GLY B C 1 ATOM 2735 O O . GLY B 2 143 ? 4.948 16.488 -14.426 1.00 26.50 ? 141 GLY B O 1 ATOM 2736 N N . VAL B 2 144 ? 6.547 16.188 -15.971 1.00 21.36 ? 142 VAL B N 1 ATOM 2737 C CA . VAL B 2 144 ? 7.574 15.905 -14.965 1.00 22.68 ? 142 VAL B CA 1 ATOM 2738 C C . VAL B 2 144 ? 8.564 17.068 -14.858 1.00 23.77 ? 142 VAL B C 1 ATOM 2739 O O . VAL B 2 144 ? 9.098 17.536 -15.864 1.00 23.23 ? 142 VAL B O 1 ATOM 2740 C CB . VAL B 2 144 ? 8.343 14.613 -15.277 1.00 26.21 ? 142 VAL B CB 1 ATOM 2741 C CG1 . VAL B 2 144 ? 9.507 14.436 -14.300 1.00 19.67 ? 142 VAL B CG1 1 ATOM 2742 C CG2 . VAL B 2 144 ? 7.404 13.421 -15.214 1.00 17.59 ? 142 VAL B CG2 1 ATOM 2743 N N . VAL B 2 145 ? 8.793 17.525 -13.633 1.00 20.68 ? 143 VAL B N 1 ATOM 2744 C CA . VAL B 2 145 ? 9.648 18.676 -13.371 1.00 21.12 ? 143 VAL B CA 1 ATOM 2745 C C . VAL B 2 145 ? 10.454 18.379 -12.100 1.00 19.89 ? 143 VAL B C 1 ATOM 2746 O O . VAL B 2 145 ? 10.028 17.596 -11.260 1.00 24.74 ? 143 VAL B O 1 ATOM 2747 C CB . VAL B 2 145 ? 8.797 19.971 -13.204 1.00 28.57 ? 143 VAL B CB 1 ATOM 2748 C CG1 . VAL B 2 145 ? 7.947 19.897 -11.957 1.00 27.15 ? 143 VAL B CG1 1 ATOM 2749 C CG2 . VAL B 2 145 ? 9.673 21.220 -13.193 1.00 29.23 ? 143 VAL B CG2 1 ATOM 2750 N N . SER B 2 146 ? 11.618 18.998 -11.971 1.00 15.77 ? 144 SER B N 1 ATOM 2751 C CA . SER B 2 146 ? 12.567 18.651 -10.915 1.00 17.67 ? 144 SER B CA 1 ATOM 2752 C C . SER B 2 146 ? 13.362 19.872 -10.466 1.00 26.83 ? 144 SER B C 1 ATOM 2753 O O . SER B 2 146 ? 13.506 20.845 -11.208 1.00 25.89 ? 144 SER B O 1 ATOM 2754 C CB . SER B 2 146 ? 13.549 17.590 -11.439 1.00 21.59 ? 144 SER B CB 1 ATOM 2755 O OG . SER B 2 146 ? 14.592 17.332 -10.513 1.00 21.91 ? 144 SER B OG 1 ATOM 2756 N N . THR B 2 147 ? 13.895 19.795 -9.252 1.00 28.52 ? 145 THR B N 1 ATOM 2757 C CA . THR B 2 147 ? 14.872 20.754 -8.755 1.00 23.23 ? 145 THR B CA 1 ATOM 2758 C C . THR B 2 147 ? 16.162 20.712 -9.564 1.00 23.82 ? 145 THR B C 1 ATOM 2759 O O . THR B 2 147 ? 16.945 21.662 -9.569 1.00 24.63 ? 145 THR B O 1 ATOM 2760 C CB . THR B 2 147 ? 15.250 20.415 -7.306 1.00 21.29 ? 145 THR B CB 1 ATOM 2761 O OG1 . THR B 2 147 ? 15.654 19.037 -7.227 1.00 20.32 ? 145 THR B OG1 1 ATOM 2762 C CG2 . THR B 2 147 ? 14.067 20.638 -6.394 1.00 18.15 ? 145 THR B CG2 1 ATOM 2763 N N . GLY B 2 148 ? 16.382 19.600 -10.249 1.00 20.70 ? 146 GLY B N 1 ATOM 2764 C CA . GLY B 2 148 ? 17.689 19.302 -10.792 1.00 21.15 ? 146 GLY B CA 1 ATOM 2765 C C . GLY B 2 148 ? 18.534 18.655 -9.702 1.00 19.67 ? 146 GLY B C 1 ATOM 2766 O O . GLY B 2 148 ? 18.043 18.359 -8.609 1.00 16.55 ? 146 GLY B O 1 ATOM 2767 N N . LEU B 2 149 ? 19.809 18.441 -9.991 1.00 19.45 ? 147 LEU B N 1 ATOM 2768 C CA . LEU B 2 149 ? 20.717 17.830 -9.028 1.00 18.61 ? 147 LEU B CA 1 ATOM 2769 C C . LEU B 2 149 ? 21.226 18.891 -8.058 1.00 21.78 ? 147 LEU B C 1 ATOM 2770 O O . LEU B 2 149 ? 21.828 19.877 -8.474 1.00 17.31 ? 147 LEU B O 1 ATOM 2771 C CB . LEU B 2 149 ? 21.899 17.182 -9.752 1.00 19.75 ? 147 LEU B CB 1 ATOM 2772 C CG . LEU B 2 149 ? 22.940 16.567 -8.821 1.00 26.80 ? 147 LEU B CG 1 ATOM 2773 C CD1 . LEU B 2 149 ? 22.274 15.522 -7.945 1.00 29.13 ? 147 LEU B CD1 1 ATOM 2774 C CD2 . LEU B 2 149 ? 24.106 15.959 -9.604 1.00 33.17 ? 147 LEU B CD2 1 ATOM 2775 N N . ILE B 2 150 ? 20.986 18.689 -6.767 1.00 19.31 ? 148 ILE B N 1 ATOM 2776 C CA . ILE B 2 150 ? 21.369 19.677 -5.767 1.00 18.65 ? 148 ILE B CA 1 ATOM 2777 C C . ILE B 2 150 ? 22.510 19.175 -4.890 1.00 19.96 ? 148 ILE B C 1 ATOM 2778 O O . ILE B 2 150 ? 22.393 18.132 -4.250 1.00 17.13 ? 148 ILE B O 1 ATOM 2779 C CB . ILE B 2 150 ? 20.177 20.018 -4.871 1.00 20.14 ? 148 ILE B CB 1 ATOM 2780 C CG1 . ILE B 2 150 ? 19.074 20.707 -5.679 1.00 21.36 ? 148 ILE B CG1 1 ATOM 2781 C CG2 . ILE B 2 150 ? 20.618 20.898 -3.702 1.00 28.28 ? 148 ILE B CG2 1 ATOM 2782 C CD1 . ILE B 2 150 ? 17.825 20.951 -4.861 1.00 27.23 ? 148 ILE B CD1 1 ATOM 2783 N N . GLN B 2 151 ? 23.622 19.903 -4.879 1.00 19.24 ? 149 GLN B N 1 ATOM 2784 C CA . GLN B 2 151 ? 24.705 19.627 -3.928 1.00 21.05 ? 149 GLN B CA 1 ATOM 2785 C C . GLN B 2 151 ? 24.323 20.120 -2.547 1.00 25.59 ? 149 GLN B C 1 ATOM 2786 O O . GLN B 2 151 ? 23.827 21.243 -2.408 1.00 27.33 ? 149 GLN B O 1 ATOM 2787 C CB . GLN B 2 151 ? 25.964 20.370 -4.339 1.00 28.16 ? 149 GLN B CB 1 ATOM 2788 C CG . GLN B 2 151 ? 26.927 19.570 -5.157 1.00 35.88 ? 149 GLN B CG 1 ATOM 2789 C CD . GLN B 2 151 ? 28.163 20.369 -5.491 1.00 48.12 ? 149 GLN B CD 1 ATOM 2790 O OE1 . GLN B 2 151 ? 28.119 21.601 -5.564 1.00 52.73 ? 149 GLN B OE1 1 ATOM 2791 N NE2 . GLN B 2 151 ? 29.277 19.680 -5.682 1.00 50.40 ? 149 GLN B NE2 1 ATOM 2792 N N . ASN B 2 152 ? 24.557 19.308 -1.519 1.00 20.52 ? 150 ASN B N 1 ATOM 2793 C CA . ASN B 2 152 ? 24.338 19.778 -0.144 1.00 19.45 ? 150 ASN B CA 1 ATOM 2794 C C . ASN B 2 152 ? 25.601 20.380 0.498 1.00 23.55 ? 150 ASN B C 1 ATOM 2795 O O . ASN B 2 152 ? 25.536 20.991 1.571 1.00 19.79 ? 150 ASN B O 1 ATOM 2796 C CB . ASN B 2 152 ? 23.771 18.663 0.735 1.00 20.66 ? 150 ASN B CB 1 ATOM 2797 C CG . ASN B 2 152 ? 22.378 18.237 0.302 1.00 27.76 ? 150 ASN B CG 1 ATOM 2798 O OD1 . ASN B 2 152 ? 21.551 19.075 -0.068 1.00 21.23 ? 150 ASN B OD1 1 ATOM 2799 N ND2 . ASN B 2 152 ? 22.115 16.929 0.334 1.00 15.06 ? 150 ASN B ND2 1 ATOM 2800 N N . GLY B 2 153 ? 26.740 20.201 -0.166 1.00 23.93 ? 151 GLY B N 1 ATOM 2801 C CA . GLY B 2 153 ? 28.002 20.758 0.289 1.00 22.02 ? 151 GLY B CA 1 ATOM 2802 C C . GLY B 2 153 ? 28.733 19.874 1.290 1.00 22.06 ? 151 GLY B C 1 ATOM 2803 O O . GLY B 2 153 ? 29.821 20.216 1.739 1.00 23.19 ? 151 GLY B O 1 ATOM 2804 N N . ASP B 2 154 ? 28.139 18.730 1.622 1.00 20.20 ? 152 ASP B N 1 ATOM 2805 C CA . ASP B 2 154 ? 28.684 17.823 2.620 1.00 20.36 ? 152 ASP B CA 1 ATOM 2806 C C . ASP B 2 154 ? 28.911 16.425 2.063 1.00 22.38 ? 152 ASP B C 1 ATOM 2807 O O . ASP B 2 154 ? 28.822 15.442 2.794 1.00 18.09 ? 152 ASP B O 1 ATOM 2808 C CB . ASP B 2 154 ? 27.745 17.754 3.840 1.00 28.56 ? 152 ASP B CB 1 ATOM 2809 C CG . ASP B 2 154 ? 26.363 17.198 3.490 1.00 29.02 ? 152 ASP B CG 1 ATOM 2810 O OD1 . ASP B 2 154 ? 26.055 17.063 2.284 1.00 22.41 ? 152 ASP B OD1 1 ATOM 2811 O OD2 . ASP B 2 154 ? 25.582 16.901 4.420 1.00 28.29 ? 152 ASP B OD2 1 ATOM 2812 N N . TRP B 2 155 ? 29.228 16.346 0.777 1.00 20.94 ? 153 TRP B N 1 ATOM 2813 C CA . TRP B 2 155 ? 29.432 15.068 0.092 1.00 20.88 ? 153 TRP B CA 1 ATOM 2814 C C . TRP B 2 155 ? 28.149 14.237 0.006 1.00 24.39 ? 153 TRP B C 1 ATOM 2815 O O . TRP B 2 155 ? 28.191 13.005 0.004 1.00 24.65 ? 153 TRP B O 1 ATOM 2816 C CB . TRP B 2 155 ? 30.586 14.253 0.695 1.00 19.27 ? 153 TRP B CB 1 ATOM 2817 C CG . TRP B 2 155 ? 31.958 14.864 0.461 1.00 21.11 ? 153 TRP B CG 1 ATOM 2818 C CD1 . TRP B 2 155 ? 32.506 15.932 1.116 1.00 21.63 ? 153 TRP B CD1 1 ATOM 2819 C CD2 . TRP B 2 155 ? 32.943 14.428 -0.487 1.00 21.03 ? 153 TRP B CD2 1 ATOM 2820 N NE1 . TRP B 2 155 ? 33.774 16.190 0.631 1.00 19.19 ? 153 TRP B NE1 1 ATOM 2821 C CE2 . TRP B 2 155 ? 34.065 15.275 -0.349 1.00 18.03 ? 153 TRP B CE2 1 ATOM 2822 C CE3 . TRP B 2 155 ? 32.990 13.397 -1.430 1.00 23.93 ? 153 TRP B CE3 1 ATOM 2823 C CZ2 . TRP B 2 155 ? 35.209 15.130 -1.124 1.00 22.48 ? 153 TRP B CZ2 1 ATOM 2824 C CZ3 . TRP B 2 155 ? 34.135 13.250 -2.198 1.00 22.98 ? 153 TRP B CZ3 1 ATOM 2825 C CH2 . TRP B 2 155 ? 35.229 14.113 -2.040 1.00 20.47 ? 153 TRP B CH2 1 ATOM 2826 N N . THR B 2 156 ? 27.016 14.925 -0.078 1.00 18.57 ? 154 THR B N 1 ATOM 2827 C CA . THR B 2 156 ? 25.770 14.282 -0.449 1.00 16.70 ? 154 THR B CA 1 ATOM 2828 C C . THR B 2 156 ? 25.014 15.160 -1.430 1.00 16.65 ? 154 THR B C 1 ATOM 2829 O O . THR B 2 156 ? 25.232 16.363 -1.494 1.00 19.92 ? 154 THR B O 1 ATOM 2830 C CB . THR B 2 156 ? 24.864 14.000 0.776 1.00 16.44 ? 154 THR B CB 1 ATOM 2831 O OG1 . THR B 2 156 ? 24.412 15.233 1.343 1.00 23.00 ? 154 THR B OG1 1 ATOM 2832 C CG2 . THR B 2 156 ? 25.597 13.190 1.840 1.00 25.80 ? 154 THR B CG2 1 ATOM 2833 N N . PHE B 2 157 ? 24.114 14.545 -2.189 1.00 18.13 ? 155 PHE B N 1 ATOM 2834 C CA . PHE B 2 157 ? 23.242 15.271 -3.092 1.00 20.19 ? 155 PHE B CA 1 ATOM 2835 C C . PHE B 2 157 ? 21.797 15.026 -2.697 1.00 21.64 ? 155 PHE B C 1 ATOM 2836 O O . PHE B 2 157 ? 21.493 14.128 -1.907 1.00 17.95 ? 155 PHE B O 1 ATOM 2837 C CB . PHE B 2 157 ? 23.426 14.791 -4.533 1.00 16.93 ? 155 PHE B CB 1 ATOM 2838 C CG . PHE B 2 157 ? 24.769 15.111 -5.129 1.00 16.24 ? 155 PHE B CG 1 ATOM 2839 C CD1 . PHE B 2 157 ? 24.965 16.277 -5.852 1.00 17.98 ? 155 PHE B CD1 1 ATOM 2840 C CD2 . PHE B 2 157 ? 25.824 14.222 -5.004 1.00 22.26 ? 155 PHE B CD2 1 ATOM 2841 C CE1 . PHE B 2 157 ? 26.205 16.561 -6.435 1.00 23.33 ? 155 PHE B CE1 1 ATOM 2842 C CE2 . PHE B 2 157 ? 27.076 14.504 -5.580 1.00 29.62 ? 155 PHE B CE2 1 ATOM 2843 C CZ . PHE B 2 157 ? 27.264 15.677 -6.289 1.00 24.47 ? 155 PHE B CZ 1 ATOM 2844 N N . GLN B 2 158 ? 20.897 15.823 -3.258 1.00 16.21 ? 156 GLN B N 1 ATOM 2845 C CA . GLN B 2 158 ? 19.497 15.457 -3.235 1.00 16.76 ? 156 GLN B CA 1 ATOM 2846 C C . GLN B 2 158 ? 18.865 15.935 -4.533 1.00 20.18 ? 156 GLN B C 1 ATOM 2847 O O . GLN B 2 158 ? 19.459 16.718 -5.267 1.00 20.29 ? 156 GLN B O 1 ATOM 2848 C CB . GLN B 2 158 ? 18.785 16.089 -2.036 1.00 16.76 ? 156 GLN B CB 1 ATOM 2849 C CG . GLN B 2 158 ? 18.982 17.607 -1.942 1.00 18.05 ? 156 GLN B CG 1 ATOM 2850 C CD . GLN B 2 158 ? 18.109 18.241 -0.876 1.00 27.11 ? 156 GLN B CD 1 ATOM 2851 O OE1 . GLN B 2 158 ? 16.889 18.115 -0.915 1.00 25.99 ? 156 GLN B OE1 1 ATOM 2852 N NE2 . GLN B 2 158 ? 18.732 18.910 0.092 1.00 20.03 ? 156 GLN B NE2 1 ATOM 2853 N N . THR B 2 159 ? 17.660 15.455 -4.810 1.00 21.24 ? 157 THR B N 1 ATOM 2854 C CA . THR B 2 159 ? 16.880 15.964 -5.925 1.00 19.37 ? 157 THR B CA 1 ATOM 2855 C C . THR B 2 159 ? 15.403 15.679 -5.649 1.00 21.01 ? 157 THR B C 1 ATOM 2856 O O . THR B 2 159 ? 15.056 14.647 -5.071 1.00 21.34 ? 157 THR B O 1 ATOM 2857 C CB . THR B 2 159 ? 17.311 15.322 -7.273 1.00 21.77 ? 157 THR B CB 1 ATOM 2858 O OG1 . THR B 2 159 ? 16.604 15.951 -8.348 1.00 24.00 ? 157 THR B OG1 1 ATOM 2859 C CG2 . THR B 2 159 ? 17.005 13.808 -7.296 1.00 22.87 ? 157 THR B CG2 1 ATOM 2860 N N . LEU B 2 160 ? 14.531 16.595 -6.043 1.00 19.23 ? 158 LEU B N 1 ATOM 2861 C CA . LEU B 2 160 ? 13.100 16.335 -5.979 1.00 18.49 ? 158 LEU B CA 1 ATOM 2862 C C . LEU B 2 160 ? 12.580 16.212 -7.405 1.00 20.14 ? 158 LEU B C 1 ATOM 2863 O O . LEU B 2 160 ? 12.848 17.082 -8.235 1.00 19.93 ? 158 LEU B O 1 ATOM 2864 C CB . LEU B 2 160 ? 12.370 17.464 -5.245 1.00 21.60 ? 158 LEU B CB 1 ATOM 2865 C CG . LEU B 2 160 ? 12.222 17.455 -3.721 1.00 32.86 ? 158 LEU B CG 1 ATOM 2866 C CD1 . LEU B 2 160 ? 13.553 17.329 -2.999 1.00 31.55 ? 158 LEU B CD1 1 ATOM 2867 C CD2 . LEU B 2 160 ? 11.529 18.745 -3.318 1.00 37.79 ? 158 LEU B CD2 1 ATOM 2868 N N . VAL B 2 161 ? 11.862 15.130 -7.699 1.00 18.81 ? 159 VAL B N 1 ATOM 2869 C CA . VAL B 2 161 ? 11.260 14.948 -9.019 1.00 20.46 ? 159 VAL B CA 1 ATOM 2870 C C . VAL B 2 161 ? 9.734 14.878 -8.897 1.00 24.88 ? 159 VAL B C 1 ATOM 2871 O O . VAL B 2 161 ? 9.188 13.946 -8.293 1.00 21.27 ? 159 VAL B O 1 ATOM 2872 C CB . VAL B 2 161 ? 11.801 13.680 -9.718 1.00 17.97 ? 159 VAL B CB 1 ATOM 2873 C CG1 . VAL B 2 161 ? 11.240 13.567 -11.133 1.00 19.08 ? 159 VAL B CG1 1 ATOM 2874 C CG2 . VAL B 2 161 ? 13.332 13.707 -9.727 1.00 15.80 ? 159 VAL B CG2 1 ATOM 2875 N N . MET B 2 162 ? 9.062 15.862 -9.485 1.00 21.26 ? 160 MET B N 1 ATOM 2876 C CA . MET B 2 162 ? 7.615 16.033 -9.348 1.00 23.11 ? 160 MET B CA 1 ATOM 2877 C C . MET B 2 162 ? 6.865 15.484 -10.542 1.00 27.77 ? 160 MET B C 1 ATOM 2878 O O . MET B 2 162 ? 7.295 15.651 -11.689 1.00 24.32 ? 160 MET B O 1 ATOM 2879 C CB . MET B 2 162 ? 7.265 17.518 -9.260 1.00 27.62 ? 160 MET B CB 1 ATOM 2880 C CG . MET B 2 162 ? 7.230 18.084 -7.879 1.00 40.32 ? 160 MET B CG 1 ATOM 2881 S SD . MET B 2 162 ? 8.860 18.185 -7.167 1.00 46.59 ? 160 MET B SD 1 ATOM 2882 C CE . MET B 2 162 ? 9.551 19.590 -8.032 1.00 32.07 ? 160 MET B CE 1 ATOM 2883 N N . LEU B 2 163 ? 5.729 14.854 -10.274 1.00 16.70 ? 161 LEU B N 1 ATOM 2884 C CA . LEU B 2 163 ? 4.797 14.502 -11.333 1.00 20.42 ? 161 LEU B CA 1 ATOM 2885 C C . LEU B 2 163 ? 3.515 15.309 -11.166 1.00 21.85 ? 161 LEU B C 1 ATOM 2886 O O . LEU B 2 163 ? 2.827 15.203 -10.147 1.00 20.57 ? 161 LEU B O 1 ATOM 2887 C CB . LEU B 2 163 ? 4.480 12.996 -11.327 1.00 18.10 ? 161 LEU B CB 1 ATOM 2888 C CG . LEU B 2 163 ? 3.433 12.506 -12.339 1.00 21.39 ? 161 LEU B CG 1 ATOM 2889 C CD1 . LEU B 2 163 ? 3.877 12.738 -13.790 1.00 20.02 ? 161 LEU B CD1 1 ATOM 2890 C CD2 . LEU B 2 163 ? 3.067 11.025 -12.111 1.00 20.01 ? 161 LEU B CD2 1 ATOM 2891 N N . GLU B 2 164 ? 3.203 16.119 -12.171 1.00 23.75 ? 162 GLU B N 1 ATOM 2892 C CA . GLU B 2 164 ? 1.943 16.852 -12.210 1.00 23.85 ? 162 GLU B CA 1 ATOM 2893 C C . GLU B 2 164 ? 0.823 15.910 -12.617 1.00 22.10 ? 162 GLU B C 1 ATOM 2894 O O . GLU B 2 164 ? 0.739 15.484 -13.766 1.00 22.73 ? 162 GLU B O 1 ATOM 2895 C CB . GLU B 2 164 ? 2.036 18.004 -13.202 1.00 21.27 ? 162 GLU B CB 1 ATOM 2896 C CG . GLU B 2 164 ? 3.046 19.059 -12.802 1.00 22.86 ? 162 GLU B CG 1 ATOM 2897 C CD . GLU B 2 164 ? 3.429 19.968 -13.958 1.00 29.70 ? 162 GLU B CD 1 ATOM 2898 O OE1 . GLU B 2 164 ? 3.013 19.702 -15.107 1.00 30.39 ? 162 GLU B OE1 1 ATOM 2899 O OE2 . GLU B 2 164 ? 4.155 20.946 -13.715 1.00 28.57 ? 162 GLU B OE2 1 ATOM 2900 N N . THR B 2 165 ? -0.037 15.577 -11.669 1.00 19.67 ? 163 THR B N 1 ATOM 2901 C CA . THR B 2 165 ? -1.110 14.645 -11.941 1.00 23.26 ? 163 THR B CA 1 ATOM 2902 C C . THR B 2 165 ? -2.189 14.836 -10.900 1.00 23.22 ? 163 THR B C 1 ATOM 2903 O O . THR B 2 165 ? -1.895 15.184 -9.762 1.00 20.57 ? 163 THR B O 1 ATOM 2904 C CB . THR B 2 165 ? -0.600 13.171 -11.905 1.00 26.53 ? 163 THR B CB 1 ATOM 2905 O OG1 . THR B 2 165 ? -1.672 12.277 -12.225 1.00 35.50 ? 163 THR B OG1 1 ATOM 2906 C CG2 . THR B 2 165 ? -0.045 12.812 -10.532 1.00 24.73 ? 163 THR B CG2 1 ATOM 2907 N N . VAL B 2 166 ? -3.439 14.620 -11.295 1.00 21.67 ? 164 VAL B N 1 ATOM 2908 C CA . VAL B 2 166 ? -4.531 14.527 -10.340 1.00 23.30 ? 164 VAL B CA 1 ATOM 2909 C C . VAL B 2 166 ? -4.800 13.043 -10.058 1.00 31.65 ? 164 VAL B C 1 ATOM 2910 O O . VAL B 2 166 ? -5.340 12.336 -10.907 1.00 31.64 ? 164 VAL B O 1 ATOM 2911 C CB . VAL B 2 166 ? -5.824 15.171 -10.876 1.00 23.17 ? 164 VAL B CB 1 ATOM 2912 C CG1 . VAL B 2 166 ? -6.950 15.030 -9.848 1.00 24.36 ? 164 VAL B CG1 1 ATOM 2913 C CG2 . VAL B 2 166 ? -5.596 16.631 -11.236 1.00 22.27 ? 164 VAL B CG2 1 ATOM 2914 N N . PRO B 2 167 ? -4.421 12.567 -8.865 1.00 30.43 ? 165 PRO B N 1 ATOM 2915 C CA . PRO B 2 167 ? -4.601 11.148 -8.530 1.00 28.46 ? 165 PRO B CA 1 ATOM 2916 C C . PRO B 2 167 ? -6.055 10.695 -8.487 1.00 33.69 ? 165 PRO B C 1 ATOM 2917 O O . PRO B 2 167 ? -6.925 11.399 -7.964 1.00 32.57 ? 165 PRO B O 1 ATOM 2918 C CB . PRO B 2 167 ? -3.974 11.039 -7.136 1.00 30.05 ? 165 PRO B CB 1 ATOM 2919 C CG . PRO B 2 167 ? -2.969 12.159 -7.087 1.00 29.85 ? 165 PRO B CG 1 ATOM 2920 C CD . PRO B 2 167 ? -3.640 13.281 -7.838 1.00 31.67 ? 165 PRO B CD 1 ATOM 2921 N N . ARG B 2 168 ? -6.309 9.517 -9.049 1.00 32.18 ? 166 ARG B N 1 ATOM 2922 C CA . ARG B 2 168 ? -7.620 8.892 -8.968 1.00 39.87 ? 166 ARG B CA 1 ATOM 2923 C C . ARG B 2 168 ? -7.490 7.641 -8.111 1.00 41.94 ? 166 ARG B C 1 ATOM 2924 O O . ARG B 2 168 ? -6.433 7.011 -8.093 1.00 42.34 ? 166 ARG B O 1 ATOM 2925 C CB . ARG B 2 168 ? -8.126 8.519 -10.363 1.00 42.92 ? 166 ARG B CB 1 ATOM 2926 C CG . ARG B 2 168 ? -8.569 9.695 -11.221 1.00 46.08 ? 166 ARG B CG 1 ATOM 2927 C CD . ARG B 2 168 ? -8.665 9.268 -12.675 1.00 49.15 ? 166 ARG B CD 1 ATOM 2928 N NE . ARG B 2 168 ? -9.406 10.207 -13.518 1.00 39.92 ? 166 ARG B NE 1 ATOM 2929 C CZ . ARG B 2 168 ? -8.878 11.299 -14.065 1.00 38.62 ? 166 ARG B CZ 1 ATOM 2930 N NH1 . ARG B 2 168 ? -7.607 11.610 -13.839 1.00 35.34 ? 166 ARG B NH1 1 ATOM 2931 N NH2 . ARG B 2 168 ? -9.622 12.085 -14.832 1.00 39.47 ? 166 ARG B NH2 1 ATOM 2932 N N . SER B 2 169 ? -8.553 7.289 -7.394 1.00 42.62 ? 167 SER B N 1 ATOM 2933 C CA . SER B 2 169 ? -8.570 6.036 -6.650 1.00 47.58 ? 167 SER B CA 1 ATOM 2934 C C . SER B 2 169 ? -8.303 4.890 -7.612 1.00 43.62 ? 167 SER B C 1 ATOM 2935 O O . SER B 2 169 ? -8.684 4.947 -8.783 1.00 43.48 ? 167 SER B O 1 ATOM 2936 C CB . SER B 2 169 ? -9.912 5.838 -5.951 1.00 52.75 ? 167 SER B CB 1 ATOM 2937 O OG . SER B 2 169 ? -10.149 6.880 -5.022 1.00 59.33 ? 167 SER B OG 1 ATOM 2938 N N . GLY B 2 170 ? -7.623 3.863 -7.127 1.00 42.79 ? 168 GLY B N 1 ATOM 2939 C CA . GLY B 2 170 ? -7.282 2.735 -7.970 1.00 46.96 ? 168 GLY B CA 1 ATOM 2940 C C . GLY B 2 170 ? -5.883 2.832 -8.541 1.00 47.78 ? 168 GLY B C 1 ATOM 2941 O O . GLY B 2 170 ? -5.204 1.816 -8.684 1.00 50.94 ? 168 GLY B O 1 ATOM 2942 N N . GLU B 2 171 ? -5.450 4.054 -8.857 1.00 40.19 ? 169 GLU B N 1 ATOM 2943 C CA . GLU B 2 171 ? -4.134 4.280 -9.442 1.00 42.75 ? 169 GLU B CA 1 ATOM 2944 C C . GLU B 2 171 ? -2.993 4.000 -8.463 1.00 43.71 ? 169 GLU B C 1 ATOM 2945 O O . GLU B 2 171 ? -3.028 4.416 -7.303 1.00 40.08 ? 169 GLU B O 1 ATOM 2946 C CB . GLU B 2 171 ? -4.014 5.713 -9.985 1.00 33.51 ? 169 GLU B CB 1 ATOM 2947 C CG . GLU B 2 171 ? -4.885 5.983 -11.200 1.00 38.79 ? 169 GLU B CG 1 ATOM 2948 C CD . GLU B 2 171 ? -4.741 7.397 -11.743 1.00 44.88 ? 169 GLU B CD 1 ATOM 2949 O OE1 . GLU B 2 171 ? -4.285 8.297 -10.996 1.00 33.18 ? 169 GLU B OE1 1 ATOM 2950 O OE2 . GLU B 2 171 ? -5.088 7.609 -12.927 1.00 54.62 ? 169 GLU B OE2 1 ATOM 2951 N N . VAL B 2 172 ? -1.978 3.295 -8.949 1.00 45.53 ? 170 VAL B N 1 ATOM 2952 C CA . VAL B 2 172 ? -0.744 3.107 -8.197 1.00 40.82 ? 170 VAL B CA 1 ATOM 2953 C C . VAL B 2 172 ? 0.425 3.802 -8.906 1.00 33.81 ? 170 VAL B C 1 ATOM 2954 O O . VAL B 2 172 ? 0.749 3.485 -10.053 1.00 36.23 ? 170 VAL B O 1 ATOM 2955 C CB . VAL B 2 172 ? -0.448 1.605 -7.959 1.00 43.90 ? 170 VAL B CB 1 ATOM 2956 C CG1 . VAL B 2 172 ? -0.879 0.781 -9.167 1.00 55.44 ? 170 VAL B CG1 1 ATOM 2957 C CG2 . VAL B 2 172 ? 1.025 1.373 -7.615 1.00 36.70 ? 170 VAL B CG2 1 ATOM 2958 N N . TYR B 2 173 ? 1.035 4.766 -8.222 1.00 27.62 ? 171 TYR B N 1 ATOM 2959 C CA . TYR B 2 173 ? 2.175 5.492 -8.762 1.00 26.79 ? 171 TYR B CA 1 ATOM 2960 C C . TYR B 2 173 ? 3.461 4.926 -8.190 1.00 29.79 ? 171 TYR B C 1 ATOM 2961 O O . TYR B 2 173 ? 3.504 4.495 -7.039 1.00 33.91 ? 171 TYR B O 1 ATOM 2962 C CB . TYR B 2 173 ? 2.082 6.984 -8.438 1.00 24.01 ? 171 TYR B CB 1 ATOM 2963 C CG . TYR B 2 173 ? 0.934 7.698 -9.133 1.00 26.44 ? 171 TYR B CG 1 ATOM 2964 C CD1 . TYR B 2 173 ? 1.145 8.389 -10.317 1.00 24.77 ? 171 TYR B CD1 1 ATOM 2965 C CD2 . TYR B 2 173 ? -0.351 7.696 -8.595 1.00 26.51 ? 171 TYR B CD2 1 ATOM 2966 C CE1 . TYR B 2 173 ? 0.113 9.045 -10.964 1.00 26.67 ? 171 TYR B CE1 1 ATOM 2967 C CE2 . TYR B 2 173 ? -1.400 8.357 -9.242 1.00 25.21 ? 171 TYR B CE2 1 ATOM 2968 C CZ . TYR B 2 173 ? -1.154 9.032 -10.422 1.00 27.40 ? 171 TYR B CZ 1 ATOM 2969 O OH . TYR B 2 173 ? -2.157 9.702 -11.086 1.00 32.74 ? 171 TYR B OH 1 ATOM 2970 N N . THR B 2 174 ? 4.514 4.937 -8.993 1.00 25.97 ? 172 THR B N 1 ATOM 2971 C CA . THR B 2 174 ? 5.790 4.414 -8.547 1.00 26.80 ? 172 THR B CA 1 ATOM 2972 C C . THR B 2 174 ? 6.909 5.353 -8.953 1.00 23.90 ? 172 THR B C 1 ATOM 2973 O O . THR B 2 174 ? 7.014 5.731 -10.120 1.00 26.62 ? 172 THR B O 1 ATOM 2974 C CB . THR B 2 174 ? 6.078 3.029 -9.154 1.00 26.97 ? 172 THR B CB 1 ATOM 2975 O OG1 . THR B 2 174 ? 5.004 2.134 -8.847 1.00 29.65 ? 172 THR B OG1 1 ATOM 2976 C CG2 . THR B 2 174 ? 7.382 2.463 -8.600 1.00 33.11 ? 172 THR B CG2 1 ATOM 2977 N N . CYS B 2 175 ? 7.728 5.745 -7.987 1.00 22.14 ? 173 CYS B N 1 ATOM 2978 C CA . CYS B 2 175 ? 8.947 6.483 -8.296 1.00 29.27 ? 173 CYS B CA 1 ATOM 2979 C C . CYS B 2 175 ? 10.075 5.465 -8.326 1.00 25.75 ? 173 CYS B C 1 ATOM 2980 O O . CYS B 2 175 ? 10.234 4.699 -7.376 1.00 26.94 ? 173 CYS B O 1 ATOM 2981 C CB . CYS B 2 175 ? 9.251 7.539 -7.232 1.00 19.92 ? 173 CYS B CB 1 ATOM 2982 S SG . CYS B 2 175 ? 10.770 8.476 -7.579 1.00 22.98 ? 173 CYS B SG 1 ATOM 2983 N N . GLN B 2 176 ? 10.846 5.458 -9.410 1.00 28.04 ? 174 GLN B N 1 ATOM 2984 C CA . GLN B 2 176 ? 11.961 4.523 -9.567 1.00 26.51 ? 174 GLN B CA 1 ATOM 2985 C C . GLN B 2 176 ? 13.295 5.261 -9.633 1.00 26.49 ? 174 GLN B C 1 ATOM 2986 O O . GLN B 2 176 ? 13.449 6.222 -10.396 1.00 21.28 ? 174 GLN B O 1 ATOM 2987 C CB . GLN B 2 176 ? 11.765 3.674 -10.823 1.00 23.89 ? 174 GLN B CB 1 ATOM 2988 C CG . GLN B 2 176 ? 12.865 2.646 -11.103 1.00 29.11 ? 174 GLN B CG 1 ATOM 2989 C CD . GLN B 2 176 ? 12.746 2.078 -12.507 1.00 36.78 ? 174 GLN B CD 1 ATOM 2990 O OE1 . GLN B 2 176 ? 12.220 0.984 -12.701 1.00 38.22 ? 174 GLN B OE1 1 ATOM 2991 N NE2 . GLN B 2 176 ? 13.208 2.840 -13.500 1.00 35.93 ? 174 GLN B NE2 1 ATOM 2992 N N . VAL B 2 177 ? 14.253 4.794 -8.835 1.00 22.01 ? 175 VAL B N 1 ATOM 2993 C CA . VAL B 2 177 ? 15.571 5.417 -8.731 1.00 19.89 ? 175 VAL B CA 1 ATOM 2994 C C . VAL B 2 177 ? 16.697 4.434 -9.068 1.00 23.32 ? 175 VAL B C 1 ATOM 2995 O O . VAL B 2 177 ? 16.752 3.321 -8.527 1.00 25.05 ? 175 VAL B O 1 ATOM 2996 C CB . VAL B 2 177 ? 15.818 5.968 -7.312 1.00 19.74 ? 175 VAL B CB 1 ATOM 2997 C CG1 . VAL B 2 177 ? 17.180 6.663 -7.230 1.00 20.86 ? 175 VAL B CG1 1 ATOM 2998 C CG2 . VAL B 2 177 ? 14.708 6.920 -6.909 1.00 18.69 ? 175 VAL B CG2 1 ATOM 2999 N N . GLU B 2 178 ? 17.578 4.847 -9.979 1.00 21.83 ? 176 GLU B N 1 ATOM 3000 C CA . GLU B 2 178 ? 18.766 4.069 -10.347 1.00 21.47 ? 176 GLU B CA 1 ATOM 3001 C C . GLU B 2 178 ? 20.007 4.910 -10.020 1.00 27.24 ? 176 GLU B C 1 ATOM 3002 O O . GLU B 2 178 ? 20.055 6.108 -10.319 1.00 22.94 ? 176 GLU B O 1 ATOM 3003 C CB . GLU B 2 178 ? 18.748 3.737 -11.843 1.00 28.12 ? 176 GLU B CB 1 ATOM 3004 C CG . GLU B 2 178 ? 17.626 2.811 -12.301 1.00 33.15 ? 176 GLU B CG 1 ATOM 3005 C CD . GLU B 2 178 ? 17.341 2.937 -13.796 1.00 43.81 ? 176 GLU B CD 1 ATOM 3006 O OE1 . GLU B 2 178 ? 16.765 3.972 -14.218 1.00 43.06 ? 176 GLU B OE1 1 ATOM 3007 O OE2 . GLU B 2 178 ? 17.706 2.012 -14.551 1.00 44.50 ? 176 GLU B OE2 1 ATOM 3008 N N . HIS B 2 179 ? 21.005 4.285 -9.408 1.00 22.05 ? 177 HIS B N 1 ATOM 3009 C CA . HIS B 2 179 ? 22.147 5.004 -8.860 1.00 22.10 ? 177 HIS B CA 1 ATOM 3010 C C . HIS B 2 179 ? 23.267 3.986 -8.690 1.00 23.26 ? 177 HIS B C 1 ATOM 3011 O O . HIS B 2 179 ? 22.988 2.801 -8.509 1.00 22.28 ? 177 HIS B O 1 ATOM 3012 C CB . HIS B 2 179 ? 21.775 5.625 -7.509 1.00 20.71 ? 177 HIS B CB 1 ATOM 3013 C CG . HIS B 2 179 ? 22.853 6.478 -6.909 1.00 22.15 ? 177 HIS B CG 1 ATOM 3014 N ND1 . HIS B 2 179 ? 23.694 6.027 -5.914 1.00 23.19 ? 177 HIS B ND1 1 ATOM 3015 C CD2 . HIS B 2 179 ? 23.233 7.751 -7.174 1.00 22.74 ? 177 HIS B CD2 1 ATOM 3016 C CE1 . HIS B 2 179 ? 24.540 6.989 -5.586 1.00 25.38 ? 177 HIS B CE1 1 ATOM 3017 N NE2 . HIS B 2 179 ? 24.289 8.040 -6.342 1.00 20.91 ? 177 HIS B NE2 1 ATOM 3018 N N . PRO B 2 180 ? 24.538 4.430 -8.766 1.00 25.28 ? 178 PRO B N 1 ATOM 3019 C CA . PRO B 2 180 ? 25.648 3.467 -8.662 1.00 23.56 ? 178 PRO B CA 1 ATOM 3020 C C . PRO B 2 180 ? 25.741 2.731 -7.315 1.00 26.30 ? 178 PRO B C 1 ATOM 3021 O O . PRO B 2 180 ? 26.346 1.654 -7.253 1.00 25.98 ? 178 PRO B O 1 ATOM 3022 C CB . PRO B 2 180 ? 26.895 4.337 -8.886 1.00 28.58 ? 178 PRO B CB 1 ATOM 3023 C CG . PRO B 2 180 ? 26.412 5.499 -9.672 1.00 27.81 ? 178 PRO B CG 1 ATOM 3024 C CD . PRO B 2 180 ? 25.001 5.758 -9.208 1.00 25.76 ? 178 PRO B CD 1 ATOM 3025 N N . SER B 2 181 ? 25.172 3.300 -6.253 1.00 22.05 ? 179 SER B N 1 ATOM 3026 C CA . SER B 2 181 ? 25.163 2.624 -4.956 1.00 25.80 ? 179 SER B CA 1 ATOM 3027 C C . SER B 2 181 ? 24.147 1.481 -4.910 1.00 29.65 ? 179 SER B C 1 ATOM 3028 O O . SER B 2 181 ? 24.106 0.726 -3.942 1.00 27.47 ? 179 SER B O 1 ATOM 3029 C CB . SER B 2 181 ? 24.810 3.600 -3.841 1.00 21.46 ? 179 SER B CB 1 ATOM 3030 O OG . SER B 2 181 ? 23.490 4.080 -4.037 1.00 25.64 ? 179 SER B OG 1 ATOM 3031 N N . LEU B 2 182 ? 23.314 1.380 -5.940 1.00 27.67 ? 180 LEU B N 1 ATOM 3032 C CA . LEU B 2 182 ? 22.232 0.400 -5.963 1.00 27.98 ? 180 LEU B CA 1 ATOM 3033 C C . LEU B 2 182 ? 22.534 -0.737 -6.937 1.00 31.77 ? 180 LEU B C 1 ATOM 3034 O O . LEU B 2 182 ? 23.021 -0.504 -8.044 1.00 34.13 ? 180 LEU B O 1 ATOM 3035 C CB . LEU B 2 182 ? 20.914 1.083 -6.342 1.00 28.04 ? 180 LEU B CB 1 ATOM 3036 C CG . LEU B 2 182 ? 20.484 2.229 -5.419 1.00 27.08 ? 180 LEU B CG 1 ATOM 3037 C CD1 . LEU B 2 182 ? 19.336 3.011 -6.026 1.00 27.38 ? 180 LEU B CD1 1 ATOM 3038 C CD2 . LEU B 2 182 ? 20.096 1.675 -4.044 1.00 27.34 ? 180 LEU B CD2 1 ATOM 3039 N N . THR B 2 183 ? 22.249 -1.967 -6.522 1.00 30.47 ? 181 THR B N 1 ATOM 3040 C CA . THR B 2 183 ? 22.470 -3.121 -7.388 1.00 31.36 ? 181 THR B CA 1 ATOM 3041 C C . THR B 2 183 ? 21.218 -3.463 -8.202 1.00 34.07 ? 181 THR B C 1 ATOM 3042 O O . THR B 2 183 ? 21.264 -4.275 -9.119 1.00 37.80 ? 181 THR B O 1 ATOM 3043 C CB . THR B 2 183 ? 22.951 -4.350 -6.591 1.00 36.13 ? 181 THR B CB 1 ATOM 3044 O OG1 . THR B 2 183 ? 21.996 -4.658 -5.570 1.00 31.27 ? 181 THR B OG1 1 ATOM 3045 C CG2 . THR B 2 183 ? 24.300 -4.057 -5.944 1.00 29.50 ? 181 THR B CG2 1 ATOM 3046 N N . SER B 2 184 ? 20.102 -2.828 -7.865 1.00 31.08 ? 182 SER B N 1 ATOM 3047 C CA . SER B 2 184 ? 18.889 -2.948 -8.664 1.00 28.99 ? 182 SER B CA 1 ATOM 3048 C C . SER B 2 184 ? 18.066 -1.684 -8.413 1.00 31.35 ? 182 SER B C 1 ATOM 3049 O O . SER B 2 184 ? 18.324 -0.964 -7.444 1.00 31.33 ? 182 SER B O 1 ATOM 3050 C CB . SER B 2 184 ? 18.117 -4.231 -8.313 1.00 33.33 ? 182 SER B CB 1 ATOM 3051 O OG . SER B 2 184 ? 17.458 -4.129 -7.066 1.00 33.66 ? 182 SER B OG 1 ATOM 3052 N N . PRO B 2 185 ? 17.096 -1.386 -9.295 1.00 29.04 ? 183 PRO B N 1 ATOM 3053 C CA . PRO B 2 185 ? 16.342 -0.143 -9.104 1.00 31.00 ? 183 PRO B CA 1 ATOM 3054 C C . PRO B 2 185 ? 15.594 -0.092 -7.777 1.00 27.47 ? 183 PRO B C 1 ATOM 3055 O O . PRO B 2 185 ? 15.013 -1.083 -7.347 1.00 28.65 ? 183 PRO B O 1 ATOM 3056 C CB . PRO B 2 185 ? 15.348 -0.146 -10.275 1.00 33.82 ? 183 PRO B CB 1 ATOM 3057 C CG . PRO B 2 185 ? 15.988 -1.014 -11.316 1.00 32.95 ? 183 PRO B CG 1 ATOM 3058 C CD . PRO B 2 185 ? 16.748 -2.065 -10.558 1.00 32.25 ? 183 PRO B CD 1 ATOM 3059 N N . LEU B 2 186 ? 15.633 1.069 -7.136 1.00 29.00 ? 184 LEU B N 1 ATOM 3060 C CA . LEU B 2 186 ? 14.877 1.306 -5.922 1.00 30.45 ? 184 LEU B CA 1 ATOM 3061 C C . LEU B 2 186 ? 13.538 1.909 -6.335 1.00 28.99 ? 184 LEU B C 1 ATOM 3062 O O . LEU B 2 186 ? 13.500 2.914 -7.032 1.00 25.22 ? 184 LEU B O 1 ATOM 3063 C CB . LEU B 2 186 ? 15.645 2.280 -5.031 1.00 33.36 ? 184 LEU B CB 1 ATOM 3064 C CG . LEU B 2 186 ? 15.262 2.426 -3.561 1.00 42.65 ? 184 LEU B CG 1 ATOM 3065 C CD1 . LEU B 2 186 ? 15.323 1.078 -2.864 1.00 51.79 ? 184 LEU B CD1 1 ATOM 3066 C CD2 . LEU B 2 186 ? 16.214 3.405 -2.898 1.00 44.98 ? 184 LEU B CD2 1 ATOM 3067 N N . THR B 2 187 ? 12.442 1.275 -5.931 1.00 28.87 ? 185 THR B N 1 ATOM 3068 C CA . THR B 2 187 ? 11.116 1.747 -6.298 1.00 29.82 ? 185 THR B CA 1 ATOM 3069 C C . THR B 2 187 ? 10.291 2.031 -5.044 1.00 35.46 ? 185 THR B C 1 ATOM 3070 O O . THR B 2 187 ? 10.352 1.273 -4.073 1.00 28.82 ? 185 THR B O 1 ATOM 3071 C CB . THR B 2 187 ? 10.378 0.702 -7.168 1.00 27.82 ? 185 THR B CB 1 ATOM 3072 O OG1 . THR B 2 187 ? 10.269 -0.533 -6.446 1.00 29.97 ? 185 THR B OG1 1 ATOM 3073 C CG2 . THR B 2 187 ? 11.149 0.446 -8.450 1.00 28.69 ? 185 THR B CG2 1 ATOM 3074 N N . VAL B 2 188 ? 9.531 3.125 -5.067 1.00 28.53 ? 186 VAL B N 1 ATOM 3075 C CA . VAL B 2 188 ? 8.614 3.460 -3.983 1.00 30.17 ? 186 VAL B CA 1 ATOM 3076 C C . VAL B 2 188 ? 7.213 3.695 -4.556 1.00 26.56 ? 186 VAL B C 1 ATOM 3077 O O . VAL B 2 188 ? 7.043 4.476 -5.486 1.00 26.12 ? 186 VAL B O 1 ATOM 3078 C CB . VAL B 2 188 ? 9.086 4.723 -3.206 1.00 33.68 ? 186 VAL B CB 1 ATOM 3079 C CG1 . VAL B 2 188 ? 8.064 5.117 -2.136 1.00 35.24 ? 186 VAL B CG1 1 ATOM 3080 C CG2 . VAL B 2 188 ? 10.452 4.489 -2.585 1.00 29.83 ? 186 VAL B CG2 1 ATOM 3081 N N . GLU B 2 189 ? 6.221 3.008 -4.002 1.00 26.65 ? 187 GLU B N 1 ATOM 3082 C CA . GLU B 2 189 ? 4.842 3.127 -4.459 1.00 35.77 ? 187 GLU B CA 1 ATOM 3083 C C . GLU B 2 189 ? 4.061 4.132 -3.622 1.00 34.40 ? 187 GLU B C 1 ATOM 3084 O O . GLU B 2 189 ? 4.337 4.317 -2.435 1.00 35.36 ? 187 GLU B O 1 ATOM 3085 C CB . GLU B 2 189 ? 4.129 1.768 -4.401 1.00 37.32 ? 187 GLU B CB 1 ATOM 3086 C CG . GLU B 2 189 ? 4.725 0.695 -5.297 1.00 45.03 ? 187 GLU B CG 1 ATOM 3087 C CD . GLU B 2 189 ? 3.819 -0.523 -5.427 1.00 53.48 ? 187 GLU B CD 1 ATOM 3088 O OE1 . GLU B 2 189 ? 2.912 -0.693 -4.580 1.00 53.96 ? 187 GLU B OE1 1 ATOM 3089 O OE2 . GLU B 2 189 ? 4.006 -1.303 -6.386 1.00 52.84 ? 187 GLU B OE2 1 ATOM 3090 N N . TRP B 2 190 ? 3.085 4.774 -4.257 1.00 31.09 ? 188 TRP B N 1 ATOM 3091 C CA . TRP B 2 190 ? 2.123 5.628 -3.568 1.00 28.57 ? 188 TRP B CA 1 ATOM 3092 C C . TRP B 2 190 ? 0.751 5.419 -4.199 1.00 34.78 ? 188 TRP B C 1 ATOM 3093 O O . TRP B 2 190 ? 0.629 5.376 -5.429 1.00 32.36 ? 188 TRP B O 1 ATOM 3094 C CB . TRP B 2 190 ? 2.542 7.095 -3.690 1.00 31.56 ? 188 TRP B CB 1 ATOM 3095 C CG . TRP B 2 190 ? 1.627 8.074 -3.008 1.00 35.61 ? 188 TRP B CG 1 ATOM 3096 C CD1 . TRP B 2 190 ? 1.757 8.574 -1.742 1.00 37.01 ? 188 TRP B CD1 1 ATOM 3097 C CD2 . TRP B 2 190 ? 0.448 8.682 -3.560 1.00 34.73 ? 188 TRP B CD2 1 ATOM 3098 N NE1 . TRP B 2 190 ? 0.734 9.454 -1.475 1.00 35.67 ? 188 TRP B NE1 1 ATOM 3099 C CE2 . TRP B 2 190 ? -0.082 9.538 -2.571 1.00 31.66 ? 188 TRP B CE2 1 ATOM 3100 C CE3 . TRP B 2 190 ? -0.210 8.586 -4.792 1.00 31.27 ? 188 TRP B CE3 1 ATOM 3101 C CZ2 . TRP B 2 190 ? -1.237 10.288 -2.775 1.00 30.95 ? 188 TRP B CZ2 1 ATOM 3102 C CZ3 . TRP B 2 190 ? -1.356 9.336 -4.991 1.00 30.26 ? 188 TRP B CZ3 1 ATOM 3103 C CH2 . TRP B 2 190 ? -1.859 10.173 -3.988 1.00 28.98 ? 188 TRP B CH2 1 ATOM 3104 N N . ARG B 2 191 ? -0.274 5.280 -3.360 1.00 37.11 ? 189 ARG B N 1 ATOM 3105 C CA . ARG B 2 191 ? -1.647 5.119 -3.828 1.00 37.84 ? 189 ARG B CA 1 ATOM 3106 C C . ARG B 2 191 ? -2.533 6.234 -3.263 1.00 40.21 ? 189 ARG B C 1 ATOM 3107 O O . ARG B 2 191 ? -2.356 6.658 -2.122 1.00 39.12 ? 189 ARG B O 1 ATOM 3108 C CB . ARG B 2 191 ? -2.198 3.751 -3.408 1.00 46.57 ? 189 ARG B CB 1 ATOM 3109 C CG . ARG B 2 191 ? -1.650 2.561 -4.196 1.00 46.09 ? 189 ARG B CG 1 ATOM 3110 C CD . ARG B 2 191 ? -1.995 1.240 -3.512 1.00 56.88 ? 189 ARG B CD 1 ATOM 3111 N NE . ARG B 2 191 ? -1.619 0.062 -4.299 1.00 65.48 ? 189 ARG B NE 1 ATOM 3112 C CZ . ARG B 2 191 ? -0.390 -0.452 -4.357 1.00 70.11 ? 189 ARG B CZ 1 ATOM 3113 N NH1 . ARG B 2 191 ? 0.610 0.115 -3.687 1.00 68.25 ? 189 ARG B NH1 1 ATOM 3114 N NH2 . ARG B 2 191 ? -0.154 -1.532 -5.095 1.00 70.89 ? 189 ARG B NH2 1 ATOM 3115 N N . ALA B 2 192 ? -3.479 6.710 -4.066 1.00 42.70 ? 190 ALA B N 1 ATOM 3116 C CA . ALA B 2 192 ? -4.408 7.748 -3.623 1.00 42.11 ? 190 ALA B CA 1 ATOM 3117 C C . ALA B 2 192 ? -5.241 7.282 -2.428 1.00 35.14 ? 190 ALA B C 1 ATOM 3118 O O . ALA B 2 192 ? -5.734 6.157 -2.414 1.00 39.43 ? 190 ALA B O 1 ATOM 3119 C CB . ALA B 2 192 ? -5.319 8.182 -4.774 1.00 36.76 ? 190 ALA B CB 1 ATOM 3120 N N . SER C 3 1 ? 48.339 7.965 4.411 1.00 45.35 ? 1 SER C N 1 ATOM 3121 C CA . SER C 3 1 ? 49.418 8.513 3.602 1.00 44.26 ? 1 SER C CA 1 ATOM 3122 C C . SER C 3 1 ? 49.189 9.995 3.287 1.00 40.87 ? 1 SER C C 1 ATOM 3123 O O . SER C 3 1 ? 48.097 10.524 3.503 1.00 37.35 ? 1 SER C O 1 ATOM 3124 C CB . SER C 3 1 ? 49.588 7.699 2.324 1.00 45.41 ? 1 SER C CB 1 ATOM 3125 O OG . SER C 3 1 ? 48.334 7.481 1.712 1.00 56.23 ? 1 SER C OG 1 ATOM 3126 N N . ALA C 3 2 ? 50.222 10.655 2.769 1.00 36.88 ? 2 ALA C N 1 ATOM 3127 C CA . ALA C 3 2 ? 50.240 12.113 2.663 1.00 29.63 ? 2 ALA C CA 1 ATOM 3128 C C . ALA C 3 2 ? 49.871 12.655 1.288 1.00 26.20 ? 2 ALA C C 1 ATOM 3129 O O . ALA C 3 2 ? 50.445 12.266 0.270 1.00 31.82 ? 2 ALA C O 1 ATOM 3130 C CB . ALA C 3 2 ? 51.605 12.648 3.089 1.00 32.19 ? 2 ALA C CB 1 ATOM 3131 N N . VAL C 3 3 ? 48.907 13.568 1.276 1.00 25.68 ? 3 VAL C N 1 ATOM 3132 C CA . VAL C 3 3 ? 48.566 14.329 0.092 1.00 24.42 ? 3 VAL C CA 1 ATOM 3133 C C . VAL C 3 3 ? 49.733 15.259 -0.217 1.00 24.74 ? 3 VAL C C 1 ATOM 3134 O O . VAL C 3 3 ? 50.270 15.886 0.686 1.00 24.76 ? 3 VAL C O 1 ATOM 3135 C CB . VAL C 3 3 ? 47.300 15.170 0.339 1.00 19.80 ? 3 VAL C CB 1 ATOM 3136 C CG1 . VAL C 3 3 ? 47.082 16.171 -0.789 1.00 21.53 ? 3 VAL C CG1 1 ATOM 3137 C CG2 . VAL C 3 3 ? 46.078 14.255 0.522 1.00 20.67 ? 3 VAL C CG2 1 ATOM 3138 N N . ARG C 3 4 ? 50.129 15.330 -1.485 1.00 19.22 ? 4 ARG C N 1 ATOM 3139 C CA . ARG C 3 4 ? 51.245 16.178 -1.892 1.00 21.64 ? 4 ARG C CA 1 ATOM 3140 C C . ARG C 3 4 ? 50.712 17.457 -2.486 1.00 19.75 ? 4 ARG C C 1 ATOM 3141 O O . ARG C 3 4 ? 49.696 17.448 -3.187 1.00 22.79 ? 4 ARG C O 1 ATOM 3142 C CB . ARG C 3 4 ? 52.116 15.477 -2.930 1.00 19.58 ? 4 ARG C CB 1 ATOM 3143 C CG . ARG C 3 4 ? 52.920 14.326 -2.366 1.00 32.88 ? 4 ARG C CG 1 ATOM 3144 C CD . ARG C 3 4 ? 53.755 13.666 -3.444 1.00 34.24 ? 4 ARG C CD 1 ATOM 3145 N NE . ARG C 3 4 ? 54.545 12.551 -2.928 1.00 33.99 ? 4 ARG C NE 1 ATOM 3146 C CZ . ARG C 3 4 ? 55.114 11.642 -3.708 1.00 39.23 ? 4 ARG C CZ 1 ATOM 3147 N NH1 . ARG C 3 4 ? 54.962 11.728 -5.027 1.00 27.45 ? 4 ARG C NH1 1 ATOM 3148 N NH2 . ARG C 3 4 ? 55.824 10.652 -3.176 1.00 40.05 ? 4 ARG C NH2 1 ATOM 3149 N N . LEU C 3 5 ? 51.388 18.562 -2.212 1.00 23.26 ? 5 LEU C N 1 ATOM 3150 C CA . LEU C 3 5 ? 50.949 19.823 -2.786 1.00 26.31 ? 5 LEU C CA 1 ATOM 3151 C C . LEU C 3 5 ? 51.775 20.145 -4.022 1.00 24.50 ? 5 LEU C C 1 ATOM 3152 O O . LEU C 3 5 ? 52.931 19.734 -4.117 1.00 21.87 ? 5 LEU C O 1 ATOM 3153 C CB . LEU C 3 5 ? 51.067 20.960 -1.766 1.00 32.35 ? 5 LEU C CB 1 ATOM 3154 C CG . LEU C 3 5 ? 52.449 21.601 -1.661 1.00 39.70 ? 5 LEU C CG 1 ATOM 3155 C CD1 . LEU C 3 5 ? 52.412 23.048 -2.092 1.00 41.49 ? 5 LEU C CD1 1 ATOM 3156 C CD2 . LEU C 3 5 ? 52.982 21.487 -0.260 1.00 48.94 ? 5 LEU C CD2 1 HETATM 3157 C C1 . CIR C 3 6 ? 52.157 22.712 -5.765 1.00 16.80 ? 6 CIR C C1 1 HETATM 3158 O O1 . CIR C 3 6 ? 51.340 23.517 -5.241 1.00 15.72 ? 6 CIR C O1 1 HETATM 3159 C C2 . CIR C 3 6 ? 51.710 21.334 -6.122 1.00 15.71 ? 6 CIR C C2 1 HETATM 3160 N N2 . CIR C 3 6 ? 51.104 20.862 -4.900 1.00 19.29 ? 6 CIR C N2 1 HETATM 3161 C C3 . CIR C 3 6 ? 50.751 21.388 -7.274 1.00 16.47 ? 6 CIR C C3 1 HETATM 3162 C C4 . CIR C 3 6 ? 51.489 21.888 -8.512 1.00 16.28 ? 6 CIR C C4 1 HETATM 3163 C C5 . CIR C 3 6 ? 52.386 20.806 -9.083 1.00 24.59 ? 6 CIR C C5 1 HETATM 3164 N N6 . CIR C 3 6 ? 53.478 21.428 -9.820 1.00 20.46 ? 6 CIR C N6 1 HETATM 3165 C C7 . CIR C 3 6 ? 54.709 21.730 -9.134 1.00 26.05 ? 6 CIR C C7 1 HETATM 3166 O O7 . CIR C 3 6 ? 55.638 22.268 -9.713 1.00 29.55 ? 6 CIR C O7 1 HETATM 3167 N N8 . CIR C 3 6 ? 54.845 21.389 -7.744 1.00 23.60 ? 6 CIR C N8 1 ATOM 3168 N N . SER C 3 7 ? 53.434 23.064 -5.963 1.00 17.36 ? 7 SER C N 1 ATOM 3169 C CA . SER C 3 7 ? 53.942 24.389 -5.614 1.00 18.79 ? 7 SER C CA 1 ATOM 3170 C C . SER C 3 7 ? 53.383 25.431 -6.562 1.00 22.37 ? 7 SER C C 1 ATOM 3171 O O . SER C 3 7 ? 53.198 25.158 -7.746 1.00 18.74 ? 7 SER C O 1 ATOM 3172 C CB . SER C 3 7 ? 55.468 24.407 -5.718 1.00 21.05 ? 7 SER C CB 1 ATOM 3173 O OG . SER C 3 7 ? 56.050 23.552 -4.750 1.00 30.56 ? 7 SER C OG 1 ATOM 3174 N N . SER C 3 8 ? 53.094 26.614 -6.029 1.00 21.09 ? 8 SER C N 1 ATOM 3175 C CA . SER C 3 8 ? 52.768 27.762 -6.854 1.00 18.84 ? 8 SER C CA 1 ATOM 3176 C C . SER C 3 8 ? 54.073 28.511 -7.090 1.00 22.52 ? 8 SER C C 1 ATOM 3177 O O . SER C 3 8 ? 54.898 28.607 -6.191 1.00 18.15 ? 8 SER C O 1 ATOM 3178 C CB . SER C 3 8 ? 51.739 28.654 -6.156 1.00 19.01 ? 8 SER C CB 1 ATOM 3179 O OG . SER C 3 8 ? 50.473 27.997 -6.049 1.00 15.42 ? 8 SER C OG 1 ATOM 3180 N N . VAL C 3 9 ? 54.259 29.024 -8.300 1.00 16.64 ? 9 VAL C N 1 ATOM 3181 C CA . VAL C 3 9 ? 55.549 29.553 -8.738 1.00 20.54 ? 9 VAL C CA 1 ATOM 3182 C C . VAL C 3 9 ? 55.554 31.089 -8.792 1.00 20.85 ? 9 VAL C C 1 ATOM 3183 O O . VAL C 3 9 ? 54.598 31.699 -9.295 1.00 22.70 ? 9 VAL C O 1 ATOM 3184 C CB . VAL C 3 9 ? 55.881 29.007 -10.156 1.00 24.95 ? 9 VAL C CB 1 ATOM 3185 C CG1 . VAL C 3 9 ? 57.287 29.407 -10.581 1.00 29.02 ? 9 VAL C CG1 1 ATOM 3186 C CG2 . VAL C 3 9 ? 55.730 27.506 -10.179 1.00 22.45 ? 9 VAL C CG2 1 ATOM 3187 N N . PRO C 3 10 ? 56.627 31.716 -8.269 1.00 20.72 ? 10 PRO C N 1 ATOM 3188 C CA . PRO C 3 10 ? 56.800 33.172 -8.336 1.00 22.12 ? 10 PRO C CA 1 ATOM 3189 C C . PRO C 3 10 ? 56.872 33.651 -9.779 1.00 23.99 ? 10 PRO C C 1 ATOM 3190 O O . PRO C 3 10 ? 57.638 33.096 -10.563 1.00 20.57 ? 10 PRO C O 1 ATOM 3191 C CB . PRO C 3 10 ? 58.163 33.399 -7.666 1.00 24.22 ? 10 PRO C CB 1 ATOM 3192 C CG . PRO C 3 10 ? 58.313 32.263 -6.722 1.00 29.72 ? 10 PRO C CG 1 ATOM 3193 C CD . PRO C 3 10 ? 57.643 31.078 -7.413 1.00 21.21 ? 10 PRO C CD 1 ATOM 3194 N N . GLY C 3 11 ? 56.093 34.671 -10.121 1.00 26.01 ? 11 GLY C N 1 ATOM 3195 C CA . GLY C 3 11 ? 56.144 35.241 -11.458 1.00 24.15 ? 11 GLY C CA 1 ATOM 3196 C C . GLY C 3 11 ? 57.279 36.228 -11.602 1.00 25.63 ? 11 GLY C C 1 ATOM 3197 O O . GLY C 3 11 ? 58.063 36.411 -10.669 1.00 26.46 ? 11 GLY C O 1 ATOM 3198 N N . VAL C 3 12 ? 57.357 36.883 -12.761 1.00 23.57 ? 12 VAL C N 1 ATOM 3199 C CA . VAL C 3 12 ? 58.391 37.872 -13.031 1.00 26.54 ? 12 VAL C CA 1 ATOM 3200 C C . VAL C 3 12 ? 58.005 39.236 -12.482 1.00 31.47 ? 12 VAL C C 1 ATOM 3201 O O . VAL C 3 12 ? 56.904 39.720 -12.748 1.00 34.81 ? 12 VAL C O 1 ATOM 3202 C CB . VAL C 3 12 ? 58.593 38.061 -14.537 1.00 32.12 ? 12 VAL C CB 1 ATOM 3203 C CG1 . VAL C 3 12 ? 59.883 38.841 -14.805 1.00 32.85 ? 12 VAL C CG1 1 ATOM 3204 C CG2 . VAL C 3 12 ? 58.620 36.741 -15.226 1.00 30.87 ? 12 VAL C CG2 1 ATOM 3205 N N . ARG C 3 13 ? 58.917 39.865 -11.742 1.00 31.61 ? 13 ARG C N 1 ATOM 3206 C CA . ARG C 3 13 ? 58.676 41.193 -11.186 1.00 37.24 ? 13 ARG C CA 1 ATOM 3207 C C . ARG C 3 13 ? 58.567 42.252 -12.279 1.00 38.99 ? 13 ARG C C 1 ATOM 3208 O O . ARG C 3 13 ? 59.389 42.293 -13.191 1.00 41.85 ? 13 ARG C O 1 ATOM 3209 C CB . ARG C 3 13 ? 59.792 41.585 -10.214 1.00 50.42 ? 13 ARG C CB 1 ATOM 3210 C CG . ARG C 3 13 ? 59.612 41.075 -8.797 1.00 58.77 ? 13 ARG C CG 1 ATOM 3211 C CD . ARG C 3 13 ? 60.331 41.991 -7.807 1.00 70.98 ? 13 ARG C CD 1 ATOM 3212 N NE . ARG C 3 13 ? 60.078 41.621 -6.418 1.00 78.11 ? 13 ARG C NE 1 ATOM 3213 C CZ . ARG C 3 13 ? 60.495 42.328 -5.371 1.00 90.00 ? 13 ARG C CZ 1 ATOM 3214 N NH1 . ARG C 3 13 ? 61.186 43.448 -5.557 1.00 93.94 ? 13 ARG C NH1 1 ATOM 3215 N NH2 . ARG C 3 13 ? 60.221 41.917 -4.139 1.00 94.01 ? 13 ARG C NH2 1 HETATM 3216 C C1 . NAG D 4 . ? 48.799 49.232 -18.865 1.00 35.48 ? 500 NAG A C1 1 HETATM 3217 C C2 . NAG D 4 . ? 48.272 48.387 -20.027 1.00 51.99 ? 500 NAG A C2 1 HETATM 3218 C C3 . NAG D 4 . ? 49.342 48.132 -21.083 1.00 59.56 ? 500 NAG A C3 1 HETATM 3219 C C4 . NAG D 4 . ? 50.022 49.434 -21.496 1.00 60.17 ? 500 NAG A C4 1 HETATM 3220 C C5 . NAG D 4 . ? 50.450 50.243 -20.267 1.00 58.51 ? 500 NAG A C5 1 HETATM 3221 C C6 . NAG D 4 . ? 50.996 51.608 -20.673 1.00 62.21 ? 500 NAG A C6 1 HETATM 3222 C C7 . NAG D 4 . ? 46.441 46.835 -19.643 1.00 57.49 ? 500 NAG A C7 1 HETATM 3223 C C8 . NAG D 4 . ? 45.598 47.737 -20.493 1.00 55.28 ? 500 NAG A C8 1 HETATM 3224 N N2 . NAG D 4 . ? 47.737 47.121 -19.557 1.00 54.54 ? 500 NAG A N2 1 HETATM 3225 O O3 . NAG D 4 . ? 48.731 47.530 -22.203 1.00 61.93 ? 500 NAG A O3 1 HETATM 3226 O O4 . NAG D 4 . ? 51.140 49.150 -22.314 1.00 54.81 ? 500 NAG A O4 1 HETATM 3227 O O5 . NAG D 4 . ? 49.367 50.431 -19.369 1.00 46.39 ? 500 NAG A O5 1 HETATM 3228 O O6 . NAG D 4 . ? 49.989 52.325 -21.355 1.00 65.14 ? 500 NAG A O6 1 HETATM 3229 O O7 . NAG D 4 . ? 45.935 45.879 -19.059 1.00 62.35 ? 500 NAG A O7 1 HETATM 3230 C C1 . NAG E 4 . ? 30.549 42.603 6.700 1.00 38.47 ? 501 NAG A C1 1 HETATM 3231 C C2 . NAG E 4 . ? 30.778 43.517 5.498 1.00 40.18 ? 501 NAG A C2 1 HETATM 3232 C C3 . NAG E 4 . ? 31.939 44.479 5.744 1.00 46.35 ? 501 NAG A C3 1 HETATM 3233 C C4 . NAG E 4 . ? 31.958 45.126 7.125 1.00 60.22 ? 501 NAG A C4 1 HETATM 3234 C C5 . NAG E 4 . ? 31.382 44.248 8.244 1.00 56.22 ? 501 NAG A C5 1 HETATM 3235 C C6 . NAG E 4 . ? 30.863 45.099 9.402 1.00 60.87 ? 501 NAG A C6 1 HETATM 3236 C C7 . NAG E 4 . ? 30.338 42.693 3.246 1.00 33.13 ? 501 NAG A C7 1 HETATM 3237 C C8 . NAG E 4 . ? 30.885 41.880 2.107 1.00 24.58 ? 501 NAG A C8 1 HETATM 3238 N N2 . NAG E 4 . ? 31.104 42.723 4.330 1.00 35.31 ? 501 NAG A N2 1 HETATM 3239 O O3 . NAG E 4 . ? 31.990 45.483 4.747 1.00 40.82 ? 501 NAG A O3 1 HETATM 3240 O O4 . NAG E 4 . ? 33.346 45.236 7.338 1.00 75.94 ? 501 NAG A O4 1 HETATM 3241 O O5 . NAG E 4 . ? 30.316 43.408 7.837 1.00 48.36 ? 501 NAG A O5 1 HETATM 3242 O O6 . NAG E 4 . ? 29.886 46.010 8.946 1.00 63.67 ? 501 NAG A O6 1 HETATM 3243 O O7 . NAG E 4 . ? 29.250 43.277 3.162 1.00 30.96 ? 501 NAG A O7 1 HETATM 3244 C C1 . NAG F 4 . ? 33.887 46.384 8.034 1.00 81.05 ? 502 NAG A C1 1 HETATM 3245 C C2 . NAG F 4 . ? 33.239 47.756 7.888 1.00 80.62 ? 502 NAG A C2 1 HETATM 3246 C C3 . NAG F 4 . ? 34.224 48.776 8.477 1.00 83.28 ? 502 NAG A C3 1 HETATM 3247 C C4 . NAG F 4 . ? 35.291 48.220 9.439 1.00 86.90 ? 502 NAG A C4 1 HETATM 3248 C C5 . NAG F 4 . ? 35.093 46.784 9.956 1.00 85.63 ? 502 NAG A C5 1 HETATM 3249 C C6 . NAG F 4 . ? 34.982 46.710 11.474 1.00 84.54 ? 502 NAG A C6 1 HETATM 3250 C C7 . NAG F 4 . ? 32.421 49.262 6.145 1.00 79.00 ? 502 NAG A C7 1 HETATM 3251 C C8 . NAG F 4 . ? 30.943 49.257 5.879 1.00 77.33 ? 502 NAG A C8 1 HETATM 3252 N N2 . NAG F 4 . ? 32.963 48.097 6.504 1.00 79.08 ? 502 NAG A N2 1 HETATM 3253 O O3 . NAG F 4 . ? 33.531 49.818 9.129 1.00 82.22 ? 502 NAG A O3 1 HETATM 3254 O O4 . NAG F 4 . ? 36.544 48.298 8.788 1.00 89.89 ? 502 NAG A O4 1 HETATM 3255 O O5 . NAG F 4 . ? 33.960 46.148 9.415 1.00 83.54 ? 502 NAG A O5 1 HETATM 3256 O O6 . NAG F 4 . ? 34.752 45.363 11.832 1.00 82.17 ? 502 NAG A O6 1 HETATM 3257 O O7 . NAG F 4 . ? 33.068 50.302 6.018 1.00 80.30 ? 502 NAG A O7 1 HETATM 3258 C C1 . NAG G 4 . ? 41.078 1.211 -18.777 1.00 65.35 ? 201 NAG B C1 1 HETATM 3259 C C2 . NAG G 4 . ? 41.007 0.907 -20.280 1.00 75.40 ? 201 NAG B C2 1 HETATM 3260 C C3 . NAG G 4 . ? 41.314 -0.534 -20.686 1.00 77.73 ? 201 NAG B C3 1 HETATM 3261 C C4 . NAG G 4 . ? 42.362 -1.215 -19.823 1.00 74.93 ? 201 NAG B C4 1 HETATM 3262 C C5 . NAG G 4 . ? 42.067 -0.905 -18.369 1.00 71.91 ? 201 NAG B C5 1 HETATM 3263 C C6 . NAG G 4 . ? 43.061 -1.579 -17.441 1.00 66.70 ? 201 NAG B C6 1 HETATM 3264 C C7 . NAG G 4 . ? 39.476 1.814 -21.961 1.00 83.82 ? 201 NAG B C7 1 HETATM 3265 C C8 . NAG G 4 . ? 40.575 2.579 -22.650 1.00 82.01 ? 201 NAG B C8 1 HETATM 3266 N N2 . NAG G 4 . ? 39.709 1.302 -20.756 1.00 80.89 ? 201 NAG B N2 1 HETATM 3267 O O3 . NAG G 4 . ? 41.786 -0.592 -22.016 1.00 76.39 ? 201 NAG B O3 1 HETATM 3268 O O4 . NAG G 4 . ? 42.324 -2.619 -20.026 1.00 75.21 ? 201 NAG B O4 1 HETATM 3269 O O5 . NAG G 4 . ? 42.131 0.488 -18.163 1.00 70.06 ? 201 NAG B O5 1 HETATM 3270 O O6 . NAG G 4 . ? 43.710 -0.622 -16.630 1.00 64.59 ? 201 NAG B O6 1 HETATM 3271 O O7 . NAG G 4 . ? 38.384 1.671 -22.532 1.00 84.51 ? 201 NAG B O7 1 HETATM 3272 C C1 . EDO H 5 . ? 54.264 16.599 -5.973 1.00 52.18 ? 202 EDO B C1 1 HETATM 3273 O O1 . EDO H 5 . ? 55.443 16.167 -5.281 1.00 47.85 ? 202 EDO B O1 1 HETATM 3274 C C2 . EDO H 5 . ? 54.474 17.985 -6.580 1.00 55.09 ? 202 EDO B C2 1 HETATM 3275 O O2 . EDO H 5 . ? 54.824 17.875 -7.968 1.00 53.71 ? 202 EDO B O2 1 HETATM 3276 O O . HOH I 6 . ? 50.063 32.884 -7.763 1.00 16.66 ? 601 HOH A O 1 HETATM 3277 O O . HOH I 6 . ? 44.882 18.537 -7.633 1.00 15.81 ? 602 HOH A O 1 HETATM 3278 O O . HOH I 6 . ? 37.758 19.080 -9.043 1.00 16.86 ? 603 HOH A O 1 HETATM 3279 O O . HOH I 6 . ? 34.736 24.131 4.606 1.00 19.63 ? 604 HOH A O 1 HETATM 3280 O O . HOH I 6 . ? 13.475 35.098 10.305 1.00 16.69 ? 605 HOH A O 1 HETATM 3281 O O . HOH I 6 . ? 37.026 29.929 -8.388 1.00 14.73 ? 606 HOH A O 1 HETATM 3282 O O . HOH I 6 . ? 46.776 43.886 -5.068 1.00 20.30 ? 607 HOH A O 1 HETATM 3283 O O . HOH I 6 . ? 19.857 15.247 1.339 1.00 24.52 ? 608 HOH A O 1 HETATM 3284 O O . HOH I 6 . ? 33.846 36.657 4.156 1.00 19.93 ? 609 HOH A O 1 HETATM 3285 O O . HOH I 6 . ? 36.835 45.979 -6.727 1.00 17.42 ? 610 HOH A O 1 HETATM 3286 O O . HOH I 6 . ? 27.770 18.091 -1.697 1.00 22.46 ? 611 HOH A O 1 HETATM 3287 O O . HOH I 6 . ? 32.499 22.222 1.809 1.00 17.95 ? 612 HOH A O 1 HETATM 3288 O O . HOH I 6 . ? 36.882 20.991 5.494 1.00 28.46 ? 613 HOH A O 1 HETATM 3289 O O . HOH I 6 . ? 19.128 34.847 -5.317 1.00 24.55 ? 614 HOH A O 1 HETATM 3290 O O . HOH I 6 . ? 32.114 11.871 -7.887 1.00 23.84 ? 615 HOH A O 1 HETATM 3291 O O . HOH I 6 . ? 46.870 46.953 -4.321 1.00 28.28 ? 616 HOH A O 1 HETATM 3292 O O . HOH I 6 . ? 32.188 46.362 -9.040 1.00 30.93 ? 617 HOH A O 1 HETATM 3293 O O . HOH I 6 . ? 31.670 26.058 10.601 1.00 24.30 ? 618 HOH A O 1 HETATM 3294 O O . HOH I 6 . ? 11.893 17.207 9.415 1.00 27.26 ? 619 HOH A O 1 HETATM 3295 O O . HOH I 6 . ? 52.283 20.352 2.485 1.00 29.01 ? 620 HOH A O 1 HETATM 3296 O O . HOH I 6 . ? 21.798 29.882 -4.806 1.00 18.83 ? 621 HOH A O 1 HETATM 3297 O O . HOH I 6 . ? 35.130 24.100 -9.534 1.00 23.68 ? 622 HOH A O 1 HETATM 3298 O O . HOH I 6 . ? 32.157 15.302 -5.269 1.00 27.52 ? 623 HOH A O 1 HETATM 3299 O O . HOH I 6 . ? 24.013 39.033 7.064 1.00 25.70 ? 624 HOH A O 1 HETATM 3300 O O . HOH I 6 . ? 11.773 25.873 14.048 1.00 26.65 ? 625 HOH A O 1 HETATM 3301 O O . HOH I 6 . ? 36.689 41.376 -12.784 1.00 25.87 ? 626 HOH A O 1 HETATM 3302 O O . HOH I 6 . ? 30.991 27.134 -13.030 1.00 31.89 ? 627 HOH A O 1 HETATM 3303 O O . HOH I 6 . ? 54.249 43.844 -12.381 1.00 20.43 ? 628 HOH A O 1 HETATM 3304 O O . HOH I 6 . ? 31.571 41.223 -1.078 1.00 22.66 ? 629 HOH A O 1 HETATM 3305 O O . HOH I 6 . ? 48.545 42.375 0.818 1.00 36.95 ? 630 HOH A O 1 HETATM 3306 O O . HOH I 6 . ? 56.498 30.980 -0.146 1.00 24.72 ? 631 HOH A O 1 HETATM 3307 O O . HOH I 6 . ? 51.325 32.449 3.804 1.00 23.42 ? 632 HOH A O 1 HETATM 3308 O O . HOH I 6 . ? 20.010 41.396 12.482 1.00 26.05 ? 633 HOH A O 1 HETATM 3309 O O . HOH I 6 . ? 31.887 20.186 -0.439 1.00 23.12 ? 634 HOH A O 1 HETATM 3310 O O . HOH I 6 . ? 55.593 41.884 -14.245 1.00 34.22 ? 635 HOH A O 1 HETATM 3311 O O . HOH I 6 . ? 25.745 22.927 11.458 1.00 29.11 ? 636 HOH A O 1 HETATM 3312 O O . HOH I 6 . ? 39.836 17.706 10.188 1.00 30.07 ? 637 HOH A O 1 HETATM 3313 O O . HOH I 6 . ? 15.368 29.580 -1.630 1.00 26.49 ? 638 HOH A O 1 HETATM 3314 O O . HOH I 6 . ? 17.538 41.452 13.341 1.00 24.48 ? 639 HOH A O 1 HETATM 3315 O O . HOH I 6 . ? 35.274 44.967 -4.931 1.00 24.99 ? 640 HOH A O 1 HETATM 3316 O O . HOH I 6 . ? 28.416 19.679 6.849 1.00 26.63 ? 641 HOH A O 1 HETATM 3317 O O . HOH I 6 . ? 31.379 24.958 -11.314 1.00 28.82 ? 642 HOH A O 1 HETATM 3318 O O . HOH I 6 . ? 29.393 35.595 7.518 1.00 27.27 ? 643 HOH A O 1 HETATM 3319 O O . HOH I 6 . ? 10.909 36.889 7.916 1.00 32.28 ? 644 HOH A O 1 HETATM 3320 O O . HOH I 6 . ? 28.709 42.448 -12.127 1.00 36.51 ? 645 HOH A O 1 HETATM 3321 O O . HOH I 6 . ? 12.618 34.279 0.015 1.00 31.81 ? 646 HOH A O 1 HETATM 3322 O O . HOH I 6 . ? 21.811 38.336 -7.238 1.00 39.95 ? 647 HOH A O 1 HETATM 3323 O O . HOH I 6 . ? 54.511 36.970 -0.159 1.00 27.63 ? 648 HOH A O 1 HETATM 3324 O O . HOH I 6 . ? 13.230 13.857 7.008 1.00 44.36 ? 649 HOH A O 1 HETATM 3325 O O . HOH I 6 . ? 14.971 24.596 16.256 1.00 30.70 ? 650 HOH A O 1 HETATM 3326 O O . HOH I 6 . ? 10.275 25.656 11.756 1.00 30.25 ? 651 HOH A O 1 HETATM 3327 O O . HOH I 6 . ? 46.199 33.902 4.558 1.00 41.84 ? 652 HOH A O 1 HETATM 3328 O O . HOH I 6 . ? 28.805 29.588 10.677 1.00 28.81 ? 653 HOH A O 1 HETATM 3329 O O . HOH I 6 . ? 22.965 40.862 12.987 1.00 51.42 ? 654 HOH A O 1 HETATM 3330 O O . HOH I 6 . ? 33.720 8.767 1.823 1.00 29.15 ? 655 HOH A O 1 HETATM 3331 O O . HOH I 6 . ? 14.429 33.924 17.518 1.00 32.61 ? 656 HOH A O 1 HETATM 3332 O O . HOH I 6 . ? 37.368 20.792 -15.627 1.00 41.80 ? 657 HOH A O 1 HETATM 3333 O O . HOH I 6 . ? 55.698 40.823 -5.728 1.00 28.64 ? 658 HOH A O 1 HETATM 3334 O O . HOH I 6 . ? 51.121 14.635 5.713 1.00 35.89 ? 659 HOH A O 1 HETATM 3335 O O . HOH I 6 . ? 49.846 19.935 9.069 1.00 36.66 ? 660 HOH A O 1 HETATM 3336 O O . HOH I 6 . ? 25.967 35.761 -10.264 1.00 26.14 ? 661 HOH A O 1 HETATM 3337 O O . HOH I 6 . ? 37.126 4.699 -11.590 1.00 44.08 ? 662 HOH A O 1 HETATM 3338 O O . HOH I 6 . ? 26.437 44.500 -9.157 1.00 36.38 ? 663 HOH A O 1 HETATM 3339 O O . HOH I 6 . ? 36.203 48.538 -7.281 1.00 22.38 ? 664 HOH A O 1 HETATM 3340 O O . HOH I 6 . ? 51.703 48.112 -5.833 1.00 32.60 ? 665 HOH A O 1 HETATM 3341 O O . HOH I 6 . ? 36.984 21.496 -13.253 1.00 32.45 ? 666 HOH A O 1 HETATM 3342 O O . HOH I 6 . ? 35.940 19.933 -11.013 1.00 25.98 ? 667 HOH A O 1 HETATM 3343 O O . HOH I 6 . ? 26.242 30.196 9.429 1.00 40.40 ? 668 HOH A O 1 HETATM 3344 O O . HOH I 6 . ? 56.381 44.049 -10.571 1.00 29.92 ? 669 HOH A O 1 HETATM 3345 O O . HOH I 6 . ? 47.199 20.035 10.421 1.00 40.60 ? 670 HOH A O 1 HETATM 3346 O O . HOH I 6 . ? 23.752 33.468 11.833 1.00 34.83 ? 671 HOH A O 1 HETATM 3347 O O . HOH I 6 . ? 34.960 22.099 6.970 1.00 43.33 ? 672 HOH A O 1 HETATM 3348 O O . HOH I 6 . ? 27.260 35.172 -12.615 1.00 35.78 ? 673 HOH A O 1 HETATM 3349 O O . HOH I 6 . ? 7.193 33.588 13.323 1.00 40.94 ? 674 HOH A O 1 HETATM 3350 O O . HOH I 6 . ? 4.753 23.493 15.576 1.00 45.57 ? 675 HOH A O 1 HETATM 3351 O O . HOH I 6 . ? 39.475 28.667 7.615 1.00 46.23 ? 676 HOH A O 1 HETATM 3352 O O . HOH I 6 . ? 22.598 28.601 -7.281 1.00 38.88 ? 677 HOH A O 1 HETATM 3353 O O . HOH I 6 . ? 54.448 45.754 -14.515 1.00 36.04 ? 678 HOH A O 1 HETATM 3354 O O . HOH I 6 . ? 48.821 32.737 5.134 1.00 44.58 ? 679 HOH A O 1 HETATM 3355 O O . HOH I 6 . ? 29.451 30.749 -16.088 1.00 38.98 ? 680 HOH A O 1 HETATM 3356 O O . HOH I 6 . ? 14.717 26.611 -2.621 1.00 48.69 ? 681 HOH A O 1 HETATM 3357 O O . HOH I 6 . ? 15.876 40.222 0.011 1.00 40.11 ? 682 HOH A O 1 HETATM 3358 O O . HOH I 6 . ? 45.415 12.704 9.279 1.00 39.94 ? 683 HOH A O 1 HETATM 3359 O O . HOH I 6 . ? 12.847 35.847 21.373 1.00 53.36 ? 684 HOH A O 1 HETATM 3360 O O . HOH I 6 . ? 31.134 31.320 -18.203 1.00 41.28 ? 685 HOH A O 1 HETATM 3361 O O . HOH I 6 . ? 29.536 46.944 -7.465 1.00 41.59 ? 686 HOH A O 1 HETATM 3362 O O . HOH I 6 . ? 34.386 22.075 -3.362 1.00 32.13 ? 687 HOH A O 1 HETATM 3363 O O . HOH I 6 . ? 38.713 33.825 3.450 1.00 30.99 ? 688 HOH A O 1 HETATM 3364 O O . HOH I 6 . ? 15.775 31.736 -3.809 1.00 42.10 ? 689 HOH A O 1 HETATM 3365 O O . HOH I 6 . ? 26.157 26.418 -11.626 1.00 46.25 ? 690 HOH A O 1 HETATM 3366 O O . HOH I 6 . ? 33.408 34.051 -15.003 1.00 40.27 ? 691 HOH A O 1 HETATM 3367 O O . HOH I 6 . ? 37.709 35.999 2.171 1.00 32.35 ? 692 HOH A O 1 HETATM 3368 O O . HOH I 6 . ? 26.120 32.738 10.601 1.00 38.82 ? 693 HOH A O 1 HETATM 3369 O O . HOH I 6 . ? 29.832 33.328 9.504 1.00 46.26 ? 694 HOH A O 1 HETATM 3370 O O . HOH I 6 . ? 12.517 37.346 3.612 1.00 33.48 ? 695 HOH A O 1 HETATM 3371 O O . HOH I 6 . ? 42.003 29.915 6.864 1.00 36.18 ? 696 HOH A O 1 HETATM 3372 O O . HOH I 6 . ? 35.761 31.049 4.634 1.00 41.56 ? 697 HOH A O 1 HETATM 3373 O O . HOH I 6 . ? 20.188 40.529 -6.792 1.00 44.42 ? 698 HOH A O 1 HETATM 3374 O O . HOH I 6 . ? 33.291 30.457 -17.813 1.00 44.69 ? 699 HOH A O 1 HETATM 3375 O O . HOH I 6 . ? 9.617 19.030 3.052 1.00 47.35 ? 700 HOH A O 1 HETATM 3376 O O . HOH I 6 . ? 33.663 6.058 1.189 1.00 40.56 ? 701 HOH A O 1 HETATM 3377 O O . HOH I 6 . ? 33.204 33.035 8.518 1.00 45.25 ? 702 HOH A O 1 HETATM 3378 O O . HOH I 6 . ? 42.381 50.472 -8.743 1.00 33.73 ? 703 HOH A O 1 HETATM 3379 O O . HOH I 6 . ? 19.522 42.214 -2.458 1.00 37.44 ? 704 HOH A O 1 HETATM 3380 O O . HOH I 6 . ? 26.998 26.868 18.807 1.00 46.45 ? 705 HOH A O 1 HETATM 3381 O O . HOH I 6 . ? 16.856 34.124 18.193 1.00 48.89 ? 706 HOH A O 1 HETATM 3382 O O . HOH I 6 . ? 36.499 36.932 3.957 1.00 41.75 ? 707 HOH A O 1 HETATM 3383 O O . HOH I 6 . ? 22.289 14.725 3.173 1.00 31.13 ? 708 HOH A O 1 HETATM 3384 O O . HOH I 6 . ? 30.158 21.124 -2.352 1.00 31.66 ? 709 HOH A O 1 HETATM 3385 O O . HOH I 6 . ? 34.672 27.070 7.944 1.00 45.42 ? 710 HOH A O 1 HETATM 3386 O O . HOH I 6 . ? 53.510 32.764 5.440 1.00 41.02 ? 711 HOH A O 1 HETATM 3387 O O . HOH I 6 . ? 28.750 21.626 8.556 1.00 41.81 ? 712 HOH A O 1 HETATM 3388 O O . HOH I 6 . ? 28.825 45.121 -9.791 1.00 49.19 ? 713 HOH A O 1 HETATM 3389 O O . HOH I 6 . ? 54.477 39.803 -0.775 1.00 34.11 ? 714 HOH A O 1 HETATM 3390 O O . HOH I 6 . ? 27.497 32.447 -13.163 1.00 40.44 ? 715 HOH A O 1 HETATM 3391 O O . HOH I 6 . ? 34.413 6.109 -10.413 1.00 48.21 ? 716 HOH A O 1 HETATM 3392 O O . HOH I 6 . ? 16.822 42.418 -1.630 1.00 46.08 ? 717 HOH A O 1 HETATM 3393 O O . HOH I 6 . ? 30.629 9.517 5.169 1.00 38.28 ? 718 HOH A O 1 HETATM 3394 O O . HOH I 6 . ? 56.400 43.245 -7.687 1.00 43.03 ? 719 HOH A O 1 HETATM 3395 O O . HOH I 6 . ? 57.541 31.097 2.428 1.00 46.49 ? 720 HOH A O 1 HETATM 3396 O O . HOH I 6 . ? 4.836 17.041 9.603 1.00 42.12 ? 721 HOH A O 1 HETATM 3397 O O . HOH I 6 . ? 19.422 18.680 13.023 1.00 42.09 ? 722 HOH A O 1 HETATM 3398 O O . HOH I 6 . ? 51.083 35.173 3.046 1.00 31.66 ? 723 HOH A O 1 HETATM 3399 O O . HOH I 6 . ? 25.636 41.065 8.992 1.00 44.93 ? 724 HOH A O 1 HETATM 3400 O O . HOH I 6 . ? 12.512 37.485 1.371 1.00 39.08 ? 725 HOH A O 1 HETATM 3401 O O . HOH I 6 . ? 22.215 38.090 -9.467 1.00 48.30 ? 726 HOH A O 1 HETATM 3402 O O . HOH I 6 . ? 39.877 51.585 -9.246 1.00 45.64 ? 727 HOH A O 1 HETATM 3403 O O . HOH I 6 . ? 53.418 36.563 2.930 1.00 35.00 ? 728 HOH A O 1 HETATM 3404 O O . HOH I 6 . ? 31.584 36.954 -14.648 1.00 41.57 ? 729 HOH A O 1 HETATM 3405 O O . HOH I 6 . ? 9.544 26.506 18.062 1.00 55.78 ? 730 HOH A O 1 HETATM 3406 O O . HOH I 6 . ? 33.578 27.696 10.362 1.00 49.08 ? 731 HOH A O 1 HETATM 3407 O O . HOH I 6 . ? 11.161 35.871 22.817 1.00 57.46 ? 732 HOH A O 1 HETATM 3408 O O . HOH I 6 . ? 33.222 44.109 -15.691 1.00 50.26 ? 733 HOH A O 1 HETATM 3409 O O . HOH I 6 . ? 37.324 25.746 -15.356 1.00 20.11 ? 734 HOH A O 1 HETATM 3410 O O . HOH I 6 . ? 20.382 24.842 -4.400 1.00 31.19 ? 735 HOH A O 1 HETATM 3411 O O . HOH I 6 . ? 57.368 34.843 -3.932 1.00 29.68 ? 736 HOH A O 1 HETATM 3412 O O . HOH I 6 . ? 34.878 32.948 -16.264 1.00 38.68 ? 737 HOH A O 1 HETATM 3413 O O . HOH I 6 . ? 52.334 49.371 -16.480 1.00 43.31 ? 738 HOH A O 1 HETATM 3414 O O . HOH I 6 . ? 51.190 15.822 7.803 1.00 39.89 ? 739 HOH A O 1 HETATM 3415 O O . HOH I 6 . ? 13.379 31.149 -0.320 1.00 37.64 ? 740 HOH A O 1 HETATM 3416 O O . HOH I 6 . ? 55.741 25.497 -2.017 1.00 45.46 ? 741 HOH A O 1 HETATM 3417 O O . HOH I 6 . ? 56.483 35.913 -6.580 1.00 47.76 ? 742 HOH A O 1 HETATM 3418 O O . HOH I 6 . ? 56.075 24.393 0.084 1.00 49.54 ? 743 HOH A O 1 HETATM 3419 O O . HOH I 6 . ? 5.934 15.028 12.805 1.00 47.88 ? 744 HOH A O 1 HETATM 3420 O O . HOH I 6 . ? 33.862 41.498 5.235 1.00 32.54 ? 745 HOH A O 1 HETATM 3421 O O . HOH I 6 . ? 25.024 43.754 1.050 1.00 31.31 ? 746 HOH A O 1 HETATM 3422 O O . HOH I 6 . ? 44.749 49.963 -18.335 1.00 50.44 ? 747 HOH A O 1 HETATM 3423 O O . HOH I 6 . ? 16.108 13.090 12.126 1.00 55.21 ? 748 HOH A O 1 HETATM 3424 O O . HOH I 6 . ? 10.405 29.712 18.621 1.00 55.03 ? 749 HOH A O 1 HETATM 3425 O O . HOH I 6 . ? 13.437 27.000 17.073 1.00 55.93 ? 750 HOH A O 1 HETATM 3426 O O . HOH I 6 . ? 27.412 37.485 10.004 1.00 50.10 ? 751 HOH A O 1 HETATM 3427 O O . HOH I 6 . ? 26.555 25.657 -8.334 1.00 39.77 ? 752 HOH A O 1 HETATM 3428 O O . HOH I 6 . ? 41.659 20.357 12.027 1.00 50.11 ? 753 HOH A O 1 HETATM 3429 O O . HOH I 6 . ? 20.941 42.925 14.270 1.00 50.00 ? 754 HOH A O 1 HETATM 3430 O O . HOH I 6 . ? 38.488 26.933 9.120 1.00 36.09 ? 755 HOH A O 1 HETATM 3431 O O . HOH I 6 . ? 51.256 42.123 -1.091 1.00 48.65 ? 756 HOH A O 1 HETATM 3432 O O . HOH I 6 . ? 31.680 37.304 7.766 1.00 49.60 ? 757 HOH A O 1 HETATM 3433 O O . HOH I 6 . ? 40.938 29.595 12.817 1.00 43.95 ? 758 HOH A O 1 HETATM 3434 O O . HOH I 6 . ? 38.793 43.968 5.041 1.00 43.36 ? 759 HOH A O 1 HETATM 3435 O O . HOH I 6 . ? 44.056 17.595 11.051 1.00 51.78 ? 760 HOH A O 1 HETATM 3436 O O . HOH I 6 . ? 33.029 47.665 -4.117 1.00 32.77 ? 761 HOH A O 1 HETATM 3437 O O . HOH I 6 . ? 24.962 38.059 -10.392 1.00 38.33 ? 762 HOH A O 1 HETATM 3438 O O . HOH I 6 . ? 22.823 12.575 4.383 1.00 42.28 ? 763 HOH A O 1 HETATM 3439 O O . HOH I 6 . ? 11.799 33.906 18.534 1.00 48.15 ? 764 HOH A O 1 HETATM 3440 O O . HOH I 6 . ? 30.398 28.985 13.040 1.00 51.39 ? 765 HOH A O 1 HETATM 3441 O O . HOH I 6 . ? 33.250 38.965 5.902 1.00 34.46 ? 766 HOH A O 1 HETATM 3442 O O . HOH I 6 . ? 25.733 39.413 -12.051 1.00 50.74 ? 767 HOH A O 1 HETATM 3443 O O . HOH I 6 . ? 38.674 51.368 -11.467 1.00 46.67 ? 768 HOH A O 1 HETATM 3444 O O . HOH I 6 . ? 19.454 37.090 18.881 1.00 61.19 ? 769 HOH A O 1 HETATM 3445 O O . HOH I 6 . ? 51.329 54.818 -20.899 1.00 58.40 ? 770 HOH A O 1 HETATM 3446 O O . HOH I 6 . ? 41.901 27.748 3.340 1.00 18.96 ? 771 HOH A O 1 HETATM 3447 O O . HOH I 6 . ? 23.674 34.719 -11.190 1.00 32.29 ? 772 HOH A O 1 HETATM 3448 O O . HOH I 6 . ? 56.868 34.439 -1.659 1.00 47.57 ? 773 HOH A O 1 HETATM 3449 O O . HOH I 6 . ? 37.920 43.909 -13.582 1.00 44.63 ? 774 HOH A O 1 HETATM 3450 O O . HOH I 6 . ? 35.329 4.903 3.015 1.00 42.09 ? 775 HOH A O 1 HETATM 3451 O O . HOH I 6 . ? 36.698 17.418 10.429 1.00 55.36 ? 776 HOH A O 1 HETATM 3452 O O . HOH I 6 . ? 29.438 17.129 7.766 1.00 51.77 ? 777 HOH A O 1 HETATM 3453 O O . HOH I 6 . ? 9.255 28.151 2.402 1.00 33.19 ? 778 HOH A O 1 HETATM 3454 O O . HOH I 6 . ? 46.463 16.051 8.292 1.00 31.84 ? 779 HOH A O 1 HETATM 3455 O O . HOH I 6 . ? 28.100 44.882 1.381 1.00 43.82 ? 780 HOH A O 1 HETATM 3456 O O . HOH I 6 . ? 25.309 35.795 13.237 1.00 45.45 ? 781 HOH A O 1 HETATM 3457 O O . HOH I 6 . ? 43.638 34.375 5.328 1.00 50.77 ? 782 HOH A O 1 HETATM 3458 O O . HOH I 6 . ? 44.234 51.566 -6.931 1.00 43.44 ? 783 HOH A O 1 HETATM 3459 O O . HOH I 6 . ? 27.892 26.315 16.181 1.00 48.28 ? 784 HOH A O 1 HETATM 3460 O O . HOH I 6 . ? 37.439 3.199 -14.686 1.00 54.66 ? 785 HOH A O 1 HETATM 3461 O O . HOH I 6 . ? 57.426 36.138 0.044 1.00 51.76 ? 786 HOH A O 1 HETATM 3462 O O . HOH I 6 . ? 31.435 9.618 -9.485 1.00 53.22 ? 787 HOH A O 1 HETATM 3463 O O . HOH I 6 . ? 37.240 47.229 -13.044 1.00 47.63 ? 788 HOH A O 1 HETATM 3464 O O . HOH I 6 . ? 37.945 38.822 3.780 1.00 44.09 ? 789 HOH A O 1 HETATM 3465 O O . HOH I 6 . ? 32.069 40.528 -14.135 1.00 34.48 ? 790 HOH A O 1 HETATM 3466 O O . HOH I 6 . ? 21.720 44.482 -6.452 1.00 45.20 ? 791 HOH A O 1 HETATM 3467 O O . HOH I 6 . ? 35.939 18.506 -16.846 1.00 43.76 ? 792 HOH A O 1 HETATM 3468 O O . HOH I 6 . ? 51.292 21.963 10.605 1.00 50.73 ? 793 HOH A O 1 HETATM 3469 O O . HOH I 6 . ? 48.613 20.973 13.058 1.00 52.05 ? 794 HOH A O 1 HETATM 3470 O O . HOH I 6 . ? 11.426 24.645 17.763 1.00 51.67 ? 795 HOH A O 1 HETATM 3471 O O . HOH I 6 . ? 37.236 40.890 4.275 1.00 47.57 ? 796 HOH A O 1 HETATM 3472 O O . HOH I 6 . ? 34.240 41.497 -15.716 1.00 51.90 ? 797 HOH A O 1 HETATM 3473 O O . HOH I 6 . ? 10.798 36.135 18.795 1.00 60.39 ? 798 HOH A O 1 HETATM 3474 O O . HOH I 6 . ? 20.161 44.394 -4.106 1.00 51.20 ? 799 HOH A O 1 HETATM 3475 O O . HOH J 6 . ? 52.471 16.734 -15.662 1.00 17.00 ? 301 HOH B O 1 HETATM 3476 O O . HOH J 6 . ? 53.899 17.401 -20.075 1.00 19.01 ? 302 HOH B O 1 HETATM 3477 O O . HOH J 6 . ? 50.515 24.686 -21.779 1.00 17.22 ? 303 HOH B O 1 HETATM 3478 O O . HOH J 6 . ? 36.595 35.521 -8.957 1.00 15.23 ? 304 HOH B O 1 HETATM 3479 O O . HOH J 6 . ? 62.796 19.932 -11.597 1.00 22.44 ? 305 HOH B O 1 HETATM 3480 O O . HOH J 6 . ? 49.020 15.127 -20.993 1.00 32.11 ? 306 HOH B O 1 HETATM 3481 O O . HOH J 6 . ? 46.223 16.208 -6.992 1.00 16.82 ? 307 HOH B O 1 HETATM 3482 O O . HOH J 6 . ? 9.355 9.595 -15.866 1.00 24.30 ? 308 HOH B O 1 HETATM 3483 O O . HOH J 6 . ? 52.292 25.863 -10.176 1.00 21.93 ? 309 HOH B O 1 HETATM 3484 O O . HOH J 6 . ? 53.662 15.694 -18.051 1.00 19.83 ? 310 HOH B O 1 HETATM 3485 O O . HOH J 6 . ? 34.282 40.102 -12.012 1.00 25.53 ? 311 HOH B O 1 HETATM 3486 O O . HOH J 6 . ? 52.129 35.036 -12.096 1.00 22.87 ? 312 HOH B O 1 HETATM 3487 O O . HOH J 6 . ? 14.859 5.124 -12.992 1.00 26.74 ? 313 HOH B O 1 HETATM 3488 O O . HOH J 6 . ? 45.962 23.968 -22.982 1.00 17.56 ? 314 HOH B O 1 HETATM 3489 O O . HOH J 6 . ? 5.540 22.796 -15.204 1.00 26.99 ? 315 HOH B O 1 HETATM 3490 O O . HOH J 6 . ? 38.214 24.134 -12.921 1.00 18.06 ? 316 HOH B O 1 HETATM 3491 O O . HOH J 6 . ? 37.363 25.355 -10.629 1.00 18.08 ? 317 HOH B O 1 HETATM 3492 O O . HOH J 6 . ? 60.224 15.744 -15.231 1.00 21.38 ? 318 HOH B O 1 HETATM 3493 O O . HOH J 6 . ? 52.425 13.541 -19.546 1.00 27.65 ? 319 HOH B O 1 HETATM 3494 O O . HOH J 6 . ? 10.667 16.335 -17.517 1.00 18.30 ? 320 HOH B O 1 HETATM 3495 O O . HOH J 6 . ? 41.359 40.159 -14.887 1.00 26.76 ? 321 HOH B O 1 HETATM 3496 O O . HOH J 6 . ? 42.632 48.385 -2.485 1.00 22.09 ? 322 HOH B O 1 HETATM 3497 O O . HOH J 6 . ? 54.361 10.614 -17.328 1.00 23.14 ? 323 HOH B O 1 HETATM 3498 O O . HOH J 6 . ? 56.608 17.250 -9.812 1.00 25.11 ? 324 HOH B O 1 HETATM 3499 O O . HOH J 6 . ? 29.328 13.150 -8.210 1.00 33.15 ? 325 HOH B O 1 HETATM 3500 O O . HOH J 6 . ? 40.718 29.569 -6.380 1.00 22.53 ? 326 HOH B O 1 HETATM 3501 O O . HOH J 6 . ? 41.614 34.221 -19.878 1.00 20.55 ? 327 HOH B O 1 HETATM 3502 O O . HOH J 6 . ? 48.557 9.857 -19.053 1.00 29.50 ? 328 HOH B O 1 HETATM 3503 O O . HOH J 6 . ? 39.501 32.824 -17.923 1.00 25.72 ? 329 HOH B O 1 HETATM 3504 O O . HOH J 6 . ? 28.022 14.140 5.028 1.00 28.81 ? 330 HOH B O 1 HETATM 3505 O O . HOH J 6 . ? -8.400 13.735 -16.054 1.00 28.03 ? 331 HOH B O 1 HETATM 3506 O O . HOH J 6 . ? 52.790 31.550 -24.547 1.00 31.64 ? 332 HOH B O 1 HETATM 3507 O O . HOH J 6 . ? 51.236 14.746 -25.051 1.00 32.24 ? 333 HOH B O 1 HETATM 3508 O O . HOH J 6 . ? 14.090 5.012 0.915 1.00 34.00 ? 334 HOH B O 1 HETATM 3509 O O . HOH J 6 . ? 48.409 25.520 -23.422 1.00 19.66 ? 335 HOH B O 1 HETATM 3510 O O . HOH J 6 . ? 53.406 15.319 -23.709 1.00 34.47 ? 336 HOH B O 1 HETATM 3511 O O . HOH J 6 . ? 44.890 46.507 -2.473 1.00 31.90 ? 337 HOH B O 1 HETATM 3512 O O . HOH J 6 . ? 16.911 3.755 0.580 1.00 34.14 ? 338 HOH B O 1 HETATM 3513 O O . HOH J 6 . ? 48.400 25.232 -26.342 1.00 32.04 ? 339 HOH B O 1 HETATM 3514 O O . HOH J 6 . ? 16.356 11.958 -17.378 1.00 35.91 ? 340 HOH B O 1 HETATM 3515 O O . HOH J 6 . ? 10.077 13.679 -18.659 1.00 30.09 ? 341 HOH B O 1 HETATM 3516 O O . HOH J 6 . ? 18.979 13.352 -13.252 1.00 39.77 ? 342 HOH B O 1 HETATM 3517 O O . HOH J 6 . ? 64.623 19.139 -19.738 1.00 26.73 ? 343 HOH B O 1 HETATM 3518 O O . HOH J 6 . ? 59.571 37.394 -19.109 1.00 27.05 ? 344 HOH B O 1 HETATM 3519 O O . HOH J 6 . ? 20.926 19.434 -12.413 1.00 35.96 ? 345 HOH B O 1 HETATM 3520 O O . HOH J 6 . ? 38.181 38.868 -14.326 1.00 29.89 ? 346 HOH B O 1 HETATM 3521 O O . HOH J 6 . ? 40.380 31.958 -21.830 1.00 28.49 ? 347 HOH B O 1 HETATM 3522 O O . HOH J 6 . ? 41.608 42.971 -14.882 1.00 25.83 ? 348 HOH B O 1 HETATM 3523 O O . HOH J 6 . ? 43.708 41.973 -18.760 1.00 38.90 ? 349 HOH B O 1 HETATM 3524 O O . HOH J 6 . ? 22.363 23.984 -8.082 1.00 40.42 ? 350 HOH B O 1 HETATM 3525 O O . HOH J 6 . ? 37.801 28.101 -17.814 1.00 31.15 ? 351 HOH B O 1 HETATM 3526 O O . HOH J 6 . ? 39.554 22.524 -16.627 1.00 26.60 ? 352 HOH B O 1 HETATM 3527 O O . HOH J 6 . ? 48.891 4.724 -17.682 1.00 35.37 ? 353 HOH B O 1 HETATM 3528 O O . HOH J 6 . ? 23.651 22.574 -5.914 1.00 28.91 ? 354 HOH B O 1 HETATM 3529 O O . HOH J 6 . ? 45.162 6.896 1.786 1.00 42.04 ? 355 HOH B O 1 HETATM 3530 O O . HOH J 6 . ? 31.241 4.527 0.413 1.00 36.37 ? 356 HOH B O 1 HETATM 3531 O O . HOH J 6 . ? 49.823 14.802 -27.092 1.00 39.30 ? 357 HOH B O 1 HETATM 3532 O O . HOH J 6 . ? 40.054 25.621 -20.531 1.00 34.50 ? 358 HOH B O 1 HETATM 3533 O O . HOH J 6 . ? 24.910 4.342 2.048 1.00 24.04 ? 359 HOH B O 1 HETATM 3534 O O . HOH J 6 . ? 14.220 11.767 -15.712 1.00 31.86 ? 360 HOH B O 1 HETATM 3535 O O . HOH J 6 . ? 41.469 22.725 -21.518 1.00 40.31 ? 361 HOH B O 1 HETATM 3536 O O . HOH J 6 . ? 9.491 5.582 1.287 1.00 25.15 ? 362 HOH B O 1 HETATM 3537 O O . HOH J 6 . ? 61.374 31.326 -22.780 1.00 28.89 ? 363 HOH B O 1 HETATM 3538 O O . HOH J 6 . ? 23.542 10.373 3.346 1.00 27.00 ? 364 HOH B O 1 HETATM 3539 O O . HOH J 6 . ? 43.988 32.561 -25.245 1.00 32.27 ? 365 HOH B O 1 HETATM 3540 O O . HOH J 6 . ? 1.483 14.269 -16.039 1.00 37.03 ? 366 HOH B O 1 HETATM 3541 O O . HOH J 6 . ? 42.690 5.727 -0.790 1.00 36.87 ? 367 HOH B O 1 HETATM 3542 O O . HOH J 6 . ? 19.642 22.824 -11.127 1.00 44.57 ? 368 HOH B O 1 HETATM 3543 O O . HOH J 6 . ? 7.276 7.257 0.721 1.00 28.02 ? 369 HOH B O 1 HETATM 3544 O O . HOH J 6 . ? 45.357 14.148 -22.406 1.00 33.80 ? 370 HOH B O 1 HETATM 3545 O O . HOH J 6 . ? 51.067 25.646 -27.451 1.00 41.45 ? 371 HOH B O 1 HETATM 3546 O O . HOH J 6 . ? 25.155 14.329 5.578 1.00 36.93 ? 372 HOH B O 1 HETATM 3547 O O . HOH J 6 . ? 40.681 30.197 -19.689 1.00 44.65 ? 373 HOH B O 1 HETATM 3548 O O . HOH J 6 . ? -2.490 16.823 -14.595 1.00 37.00 ? 374 HOH B O 1 HETATM 3549 O O . HOH J 6 . ? 20.683 1.265 -10.152 1.00 33.32 ? 375 HOH B O 1 HETATM 3550 O O . HOH J 6 . ? 47.250 30.038 -25.294 1.00 48.10 ? 376 HOH B O 1 HETATM 3551 O O . HOH J 6 . ? 36.403 2.265 0.567 1.00 47.56 ? 377 HOH B O 1 HETATM 3552 O O . HOH J 6 . ? 58.060 30.451 -24.053 1.00 37.14 ? 378 HOH B O 1 HETATM 3553 O O . HOH J 6 . ? 66.972 26.557 -17.523 1.00 38.50 ? 379 HOH B O 1 HETATM 3554 O O . HOH J 6 . ? 19.652 -5.429 -5.965 1.00 38.24 ? 380 HOH B O 1 HETATM 3555 O O . HOH J 6 . ? 49.568 7.158 -3.869 1.00 33.85 ? 381 HOH B O 1 HETATM 3556 O O . HOH J 6 . ? -4.250 14.431 -14.058 1.00 30.76 ? 382 HOH B O 1 HETATM 3557 O O . HOH J 6 . ? -1.982 18.609 -12.398 1.00 34.12 ? 383 HOH B O 1 HETATM 3558 O O . HOH J 6 . ? 47.259 12.717 -21.070 1.00 32.39 ? 384 HOH B O 1 HETATM 3559 O O . HOH J 6 . ? 6.849 2.134 -19.584 1.00 39.92 ? 385 HOH B O 1 HETATM 3560 O O . HOH J 6 . ? 37.109 33.615 -17.074 1.00 44.26 ? 386 HOH B O 1 HETATM 3561 O O . HOH J 6 . ? 50.204 5.456 -5.927 1.00 46.48 ? 387 HOH B O 1 HETATM 3562 O O . HOH J 6 . ? -5.137 10.459 -12.796 1.00 31.31 ? 388 HOH B O 1 HETATM 3563 O O . HOH J 6 . ? 53.679 27.769 -12.701 1.00 51.64 ? 389 HOH B O 1 HETATM 3564 O O . HOH J 6 . ? 46.988 28.060 -23.807 1.00 36.09 ? 390 HOH B O 1 HETATM 3565 O O . HOH J 6 . ? 40.885 17.173 -19.338 1.00 33.11 ? 391 HOH B O 1 HETATM 3566 O O . HOH J 6 . ? 44.480 24.538 -25.204 1.00 37.37 ? 392 HOH B O 1 HETATM 3567 O O . HOH J 6 . ? 59.751 40.270 -18.307 1.00 49.84 ? 393 HOH B O 1 HETATM 3568 O O . HOH J 6 . ? 12.691 -1.079 -4.012 1.00 31.78 ? 394 HOH B O 1 HETATM 3569 O O . HOH J 6 . ? 34.855 47.112 -2.932 1.00 38.91 ? 395 HOH B O 1 HETATM 3570 O O . HOH J 6 . ? 43.214 43.742 -16.777 1.00 33.53 ? 396 HOH B O 1 HETATM 3571 O O . HOH J 6 . ? 27.325 4.838 3.430 1.00 35.42 ? 397 HOH B O 1 HETATM 3572 O O . HOH J 6 . ? 42.727 3.465 -20.439 1.00 42.00 ? 398 HOH B O 1 HETATM 3573 O O . HOH J 6 . ? 52.724 8.198 -8.725 1.00 43.89 ? 399 HOH B O 1 HETATM 3574 O O . HOH J 6 . ? 34.263 3.751 -9.031 1.00 44.58 ? 400 HOH B O 1 HETATM 3575 O O . HOH J 6 . ? -0.225 16.753 -16.208 1.00 35.21 ? 401 HOH B O 1 HETATM 3576 O O . HOH J 6 . ? 5.364 -0.662 -8.892 1.00 44.41 ? 402 HOH B O 1 HETATM 3577 O O . HOH J 6 . ? 42.671 35.370 -24.564 1.00 50.88 ? 403 HOH B O 1 HETATM 3578 O O . HOH J 6 . ? 40.659 20.861 -23.406 1.00 42.76 ? 404 HOH B O 1 HETATM 3579 O O . HOH J 6 . ? 48.076 6.049 -8.023 1.00 43.05 ? 405 HOH B O 1 HETATM 3580 O O . HOH J 6 . ? 69.801 25.496 -18.490 1.00 29.40 ? 406 HOH B O 1 HETATM 3581 O O . HOH J 6 . ? 10.770 11.647 -16.898 1.00 31.81 ? 407 HOH B O 1 HETATM 3582 O O . HOH J 6 . ? 14.923 18.511 0.972 1.00 38.51 ? 408 HOH B O 1 HETATM 3583 O O . HOH J 6 . ? 55.057 30.095 -24.789 1.00 38.25 ? 409 HOH B O 1 HETATM 3584 O O . HOH J 6 . ? 22.961 23.768 -3.269 1.00 38.03 ? 410 HOH B O 1 HETATM 3585 O O . HOH J 6 . ? 11.147 12.974 -21.240 1.00 35.51 ? 411 HOH B O 1 HETATM 3586 O O . HOH J 6 . ? 4.818 21.864 -11.471 1.00 34.70 ? 412 HOH B O 1 HETATM 3587 O O . HOH J 6 . ? 3.019 2.164 -11.127 1.00 35.54 ? 413 HOH B O 1 HETATM 3588 O O . HOH J 6 . ? 29.807 17.542 -6.178 1.00 49.53 ? 414 HOH B O 1 HETATM 3589 O O . HOH J 6 . ? 13.879 7.576 -22.375 1.00 37.68 ? 415 HOH B O 1 HETATM 3590 O O . HOH J 6 . ? 25.915 18.423 6.563 1.00 36.94 ? 416 HOH B O 1 HETATM 3591 O O . HOH J 6 . ? 3.051 10.841 -19.952 1.00 43.95 ? 417 HOH B O 1 HETATM 3592 O O . HOH J 6 . ? 20.040 -0.819 -11.072 1.00 41.36 ? 418 HOH B O 1 HETATM 3593 O O . HOH J 6 . ? 47.302 10.744 -22.782 1.00 52.40 ? 419 HOH B O 1 HETATM 3594 O O . HOH J 6 . ? -6.291 4.326 -4.908 1.00 54.16 ? 420 HOH B O 1 HETATM 3595 O O . HOH J 6 . ? 41.444 31.679 -24.319 1.00 35.57 ? 421 HOH B O 1 HETATM 3596 O O . HOH J 6 . ? 53.575 8.204 -5.641 1.00 39.80 ? 422 HOH B O 1 HETATM 3597 O O . HOH J 6 . ? 64.970 33.939 -18.569 1.00 45.29 ? 423 HOH B O 1 HETATM 3598 O O . HOH J 6 . ? 1.984 15.752 1.709 1.00 46.91 ? 424 HOH B O 1 HETATM 3599 O O . HOH J 6 . ? 9.450 2.863 1.000 1.00 45.86 ? 425 HOH B O 1 HETATM 3600 O O . HOH J 6 . ? 41.084 39.215 -20.704 1.00 47.78 ? 426 HOH B O 1 HETATM 3601 O O . HOH J 6 . ? 6.906 1.114 -1.748 1.00 33.32 ? 427 HOH B O 1 HETATM 3602 O O . HOH J 6 . ? 28.498 11.011 -10.666 1.00 34.04 ? 428 HOH B O 1 HETATM 3603 O O . HOH J 6 . ? 30.184 5.705 2.893 1.00 50.86 ? 429 HOH B O 1 HETATM 3604 O O . HOH J 6 . ? 28.335 11.409 4.851 1.00 48.26 ? 430 HOH B O 1 HETATM 3605 O O . HOH J 6 . ? 26.048 10.208 4.675 1.00 48.41 ? 431 HOH B O 1 HETATM 3606 O O . HOH J 6 . ? 26.555 7.146 4.861 1.00 39.96 ? 432 HOH B O 1 HETATM 3607 O O . HOH J 6 . ? 45.448 39.093 -24.676 1.00 41.18 ? 433 HOH B O 1 HETATM 3608 O O . HOH J 6 . ? 46.167 48.026 -0.085 1.00 44.07 ? 434 HOH B O 1 HETATM 3609 O O . HOH J 6 . ? 67.021 30.093 -19.344 0.50 40.12 ? 435 HOH B O 1 HETATM 3610 O O . HOH J 6 . ? 63.750 21.078 -21.258 1.00 29.09 ? 436 HOH B O 1 HETATM 3611 O O . HOH J 6 . ? 69.928 23.401 -16.781 1.00 26.60 ? 437 HOH B O 1 HETATM 3612 O O . HOH J 6 . ? 45.360 40.575 -20.917 1.00 46.68 ? 438 HOH B O 1 HETATM 3613 O O . HOH J 6 . ? 25.088 19.633 8.480 1.00 40.97 ? 439 HOH B O 1 HETATM 3614 O O . HOH J 6 . ? 47.742 49.813 -0.819 1.00 54.96 ? 440 HOH B O 1 HETATM 3615 O O . HOH J 6 . ? 42.846 38.248 -24.567 1.00 43.23 ? 441 HOH B O 1 HETATM 3616 O O . HOH J 6 . ? 16.254 24.153 -8.547 1.00 44.57 ? 442 HOH B O 1 HETATM 3617 O O . HOH J 6 . ? 25.602 11.149 7.114 1.00 49.03 ? 443 HOH B O 1 HETATM 3618 O O . HOH J 6 . ? -0.000 11.759 -19.344 0.50 45.11 ? 444 HOH B O 1 HETATM 3619 O O . HOH J 6 . ? 23.205 18.288 4.299 1.00 42.61 ? 445 HOH B O 1 HETATM 3620 O O . HOH J 6 . ? 60.986 24.763 -26.568 1.00 55.67 ? 446 HOH B O 1 HETATM 3621 O O . HOH J 6 . ? 55.914 38.634 -25.320 1.00 53.33 ? 447 HOH B O 1 HETATM 3622 O O . HOH J 6 . ? 42.722 39.986 -22.215 1.00 41.55 ? 448 HOH B O 1 HETATM 3623 O O . HOH J 6 . ? 68.266 31.489 -16.031 1.00 46.08 ? 449 HOH B O 1 HETATM 3624 O O . HOH J 6 . ? 27.624 2.332 4.844 1.00 39.64 ? 450 HOH B O 1 HETATM 3625 O O . HOH J 6 . ? 52.081 14.071 -22.163 1.00 33.66 ? 451 HOH B O 1 HETATM 3626 O O . HOH J 6 . ? 35.721 38.080 -16.372 1.00 37.08 ? 452 HOH B O 1 HETATM 3627 O O . HOH J 6 . ? 40.319 3.753 -8.839 1.00 51.13 ? 453 HOH B O 1 HETATM 3628 O O . HOH J 6 . ? 38.175 37.184 -17.278 1.00 39.28 ? 454 HOH B O 1 HETATM 3629 O O . HOH J 6 . ? 32.851 1.689 -5.072 1.00 42.55 ? 455 HOH B O 1 HETATM 3630 O O . HOH J 6 . ? 27.924 -0.284 4.033 1.00 44.43 ? 456 HOH B O 1 HETATM 3631 O O . HOH J 6 . ? 55.895 9.391 -7.654 1.00 26.76 ? 457 HOH B O 1 HETATM 3632 O O . HOH J 6 . ? 13.174 2.287 -16.637 1.00 37.14 ? 458 HOH B O 1 HETATM 3633 O O . HOH J 6 . ? 54.719 23.322 -27.838 1.00 43.64 ? 459 HOH B O 1 HETATM 3634 O O . HOH J 6 . ? 66.611 20.832 -13.317 1.00 44.66 ? 460 HOH B O 1 HETATM 3635 O O . HOH J 6 . ? 63.362 34.737 -20.887 1.00 44.60 ? 461 HOH B O 1 HETATM 3636 O O . HOH J 6 . ? 35.226 45.785 5.024 1.00 50.24 ? 462 HOH B O 1 HETATM 3637 O O . HOH J 6 . ? 55.264 7.695 -10.109 1.00 47.41 ? 463 HOH B O 1 HETATM 3638 O O . HOH J 6 . ? 16.718 11.931 -13.226 1.00 26.90 ? 464 HOH B O 1 HETATM 3639 O O . HOH J 6 . ? 43.613 2.834 -12.376 1.00 45.50 ? 465 HOH B O 1 HETATM 3640 O O . HOH J 6 . ? 51.376 10.417 -17.973 1.00 34.90 ? 466 HOH B O 1 HETATM 3641 O O . HOH J 6 . ? 39.748 39.933 -18.516 1.00 52.58 ? 467 HOH B O 1 HETATM 3642 O O . HOH J 6 . ? 53.916 24.054 -30.603 1.00 47.46 ? 468 HOH B O 1 HETATM 3643 O O . HOH J 6 . ? 44.910 3.634 -3.590 1.00 34.86 ? 469 HOH B O 1 HETATM 3644 O O . HOH J 6 . ? -9.428 20.679 -6.920 1.00 53.37 ? 470 HOH B O 1 HETATM 3645 O O . HOH J 6 . ? 68.514 23.469 -13.996 1.00 53.50 ? 471 HOH B O 1 HETATM 3646 O O . HOH J 6 . ? 0.438 4.835 -0.463 1.00 38.06 ? 472 HOH B O 1 HETATM 3647 O O . HOH J 6 . ? 61.992 36.578 -18.731 1.00 52.71 ? 473 HOH B O 1 HETATM 3648 O O . HOH J 6 . ? 43.384 50.208 1.745 1.00 52.86 ? 474 HOH B O 1 HETATM 3649 O O . HOH J 6 . ? 16.696 11.926 4.291 1.00 47.86 ? 475 HOH B O 1 HETATM 3650 O O . HOH J 6 . ? 40.161 36.472 -20.995 1.00 47.78 ? 476 HOH B O 1 HETATM 3651 O O . HOH J 6 . ? 49.654 4.281 -14.978 1.00 50.56 ? 477 HOH B O 1 HETATM 3652 O O . HOH J 6 . ? 52.532 41.627 -25.006 1.00 58.42 ? 478 HOH B O 1 HETATM 3653 O O . HOH J 6 . ? 4.730 5.840 -0.822 1.00 48.92 ? 479 HOH B O 1 HETATM 3654 O O . HOH J 6 . ? 41.682 6.186 -20.504 1.00 54.01 ? 480 HOH B O 1 HETATM 3655 O O . HOH J 6 . ? 17.754 -1.712 -4.601 1.00 39.84 ? 481 HOH B O 1 HETATM 3656 O O . HOH J 6 . ? 23.237 -6.077 -3.821 1.00 41.19 ? 482 HOH B O 1 HETATM 3657 O O . HOH J 6 . ? 58.335 23.848 -8.922 1.00 40.53 ? 483 HOH B O 1 HETATM 3658 O O . HOH J 6 . ? -4.878 3.982 -0.385 1.00 45.24 ? 484 HOH B O 1 HETATM 3659 O O . HOH J 6 . ? 22.381 13.095 -12.357 1.00 39.61 ? 485 HOH B O 1 HETATM 3660 O O . HOH J 6 . ? 50.222 3.814 -12.101 1.00 50.49 ? 486 HOH B O 1 HETATM 3661 O O . HOH J 6 . ? -8.512 6.974 -1.927 1.00 64.87 ? 487 HOH B O 1 HETATM 3662 O O . HOH J 6 . ? 1.489 21.454 -0.986 1.00 52.44 ? 488 HOH B O 1 HETATM 3663 O O . HOH J 6 . ? 9.753 -1.552 -3.566 1.00 58.59 ? 489 HOH B O 1 HETATM 3664 O O . HOH K 6 . ? 60.073 31.660 -10.552 1.00 30.97 ? 101 HOH C O 1 HETATM 3665 O O . HOH K 6 . ? 58.190 38.973 -6.197 1.00 34.78 ? 102 HOH C O 1 HETATM 3666 O O . HOH K 6 . ? 61.529 38.272 -11.204 1.00 36.17 ? 103 HOH C O 1 HETATM 3667 O O . HOH K 6 . ? 51.432 16.567 2.954 1.00 34.71 ? 104 HOH C O 1 HETATM 3668 O O . HOH K 6 . ? 58.282 37.044 -7.766 1.00 46.37 ? 105 HOH C O 1 HETATM 3669 O O . HOH K 6 . ? 60.482 35.860 -7.073 1.00 43.72 ? 106 HOH C O 1 HETATM 3670 O O . HOH K 6 . ? 61.580 33.705 -5.848 1.00 47.35 ? 107 HOH C O 1 HETATM 3671 O O . HOH K 6 . ? 57.156 27.890 -4.810 1.00 38.54 ? 108 HOH C O 1 HETATM 3672 O O . HOH K 6 . ? 47.343 5.177 0.576 1.00 55.55 ? 109 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 ? 0.9374 0.7976 0.8644 -0.0891 -0.0348 -0.2017 3 GLU A N 2 C CA . GLU A 3 ? 0.9432 0.8170 0.8990 -0.0801 -0.0131 -0.1857 3 GLU A CA 3 C C . GLU A 3 ? 0.8605 0.7546 0.8901 -0.0765 -0.0098 -0.1747 3 GLU A C 4 O O . GLU A 3 ? 0.9080 0.8192 0.9595 -0.0771 -0.0317 -0.1683 3 GLU A O 5 C CB . GLU A 3 ? 0.9417 0.8265 0.8600 -0.0741 -0.0251 -0.1701 3 GLU A CB 6 C CG . GLU A 3 ? 0.8284 0.7269 0.7682 -0.0606 -0.0064 -0.1443 3 GLU A CG 7 C CD . GLU A 3 ? 0.8663 0.7749 0.7716 -0.0542 -0.0183 -0.1280 3 GLU A CD 8 O OE1 . GLU A 3 ? 0.9471 0.8672 0.8471 -0.0559 -0.0436 -0.1245 3 GLU A OE1 9 O OE2 . GLU A 3 ? 0.8173 0.7221 0.7059 -0.0477 -0.0021 -0.1187 3 GLU A OE2 10 N N . GLU A 4 ? 0.7694 0.6621 0.8383 -0.0705 0.0184 -0.1668 4 GLU A N 11 C CA . GLU A 4 ? 0.7000 0.6085 0.8361 -0.0648 0.0254 -0.1520 4 GLU A CA 12 C C . GLU A 4 ? 0.5126 0.4433 0.6575 -0.0513 0.0240 -0.1207 4 GLU A C 13 O O . GLU A 4 ? 0.4140 0.3594 0.5869 -0.0490 0.0132 -0.1105 4 GLU A O 14 C CB . GLU A 4 ? 0.7740 0.6709 0.9529 -0.0640 0.0555 -0.1552 4 GLU A CB 15 C CG . GLU A 4 ? 0.8615 0.7464 1.0389 -0.0737 0.0560 -0.1773 4 GLU A CG 16 C CD . GLU A 4 ? 0.9038 0.7910 1.1402 -0.0699 0.0823 -0.1721 4 GLU A CD 17 O OE1 . GLU A 4 ? 0.8857 0.7842 1.1606 -0.0588 0.0988 -0.1484 4 GLU A OE1 18 O OE2 . GLU A 4 ? 0.9257 0.8036 1.1690 -0.0778 0.0859 -0.1906 4 GLU A OE2 19 N N . HIS A 5 ? 0.3401 0.2722 0.4633 -0.0428 0.0357 -0.1063 5 HIS A N 20 C CA . HIS A 5 ? 0.2368 0.1877 0.3644 -0.0311 0.0339 -0.0796 5 HIS A CA 21 C C . HIS A 5 ? 0.2324 0.1847 0.3167 -0.0264 0.0322 -0.0718 5 HIS A C 22 O O . HIS A 5 ? 0.2536 0.1920 0.3149 -0.0291 0.0416 -0.0815 5 HIS A O 23 C CB . HIS A 5 ? 0.2167 0.1737 0.3910 -0.0221 0.0534 -0.0612 5 HIS A CB 24 C CG . HIS A 5 ? 0.3155 0.2721 0.5402 -0.0248 0.0586 -0.0646 5 HIS A CG 25 N ND1 . HIS A 5 ? 0.2646 0.2321 0.5100 -0.0231 0.0492 -0.0564 5 HIS A ND1 26 C CD2 . HIS A 5 ? 0.3672 0.3124 0.6308 -0.0294 0.0743 -0.0757 5 HIS A CD2 27 C CE1 . HIS A 5 ? 0.2780 0.2417 0.5746 -0.0262 0.0586 -0.0615 5 HIS A CE1 28 N NE2 . HIS A 5 ? 0.2709 0.2213 0.5792 -0.0304 0.0732 -0.0738 5 HIS A NE2 29 N N . VAL A 6 ? 0.2167 0.1842 0.2930 -0.0195 0.0227 -0.0548 6 VAL A N 30 C CA . VAL A 6 ? 0.2397 0.2101 0.2829 -0.0149 0.0210 -0.0467 6 VAL A CA 31 C C . VAL A 6 ? 0.2616 0.2463 0.3190 -0.0048 0.0244 -0.0250 6 VAL A C 32 O O . VAL A 6 ? 0.2561 0.2502 0.3271 -0.0012 0.0200 -0.0152 6 VAL A O 33 C CB . VAL A 6 ? 0.2996 0.2714 0.3069 -0.0183 0.0023 -0.0512 6 VAL A CB 34 C CG1 . VAL A 6 ? 0.3237 0.2969 0.3025 -0.0137 0.0038 -0.0433 6 VAL A CG1 35 C CG2 . VAL A 6 ? 0.3012 0.2582 0.2866 -0.0288 -0.0059 -0.0725 6 VAL A CG2 36 N N . ILE A 7 ? 0.1730 0.1583 0.2274 -0.0003 0.0327 -0.0175 7 ILE A N 37 C CA . ILE A 7 ? 0.1858 0.1839 0.2447 0.0082 0.0312 0.0012 7 ILE A CA 38 C C . ILE A 7 ? 0.1958 0.1962 0.2262 0.0087 0.0241 0.0014 7 ILE A C 39 O O . ILE A 7 ? 0.1976 0.1900 0.2201 0.0061 0.0299 -0.0056 7 ILE A O 40 C CB . ILE A 7 ? 0.2071 0.2072 0.2968 0.0137 0.0434 0.0132 7 ILE A CB 41 C CG1 . ILE A 7 ? 0.1820 0.1787 0.3053 0.0137 0.0534 0.0141 7 ILE A CG1 42 C CG2 . ILE A 7 ? 0.1769 0.1898 0.2628 0.0217 0.0368 0.0320 7 ILE A CG2 43 C CD1 . ILE A 7 ? 0.2354 0.2325 0.3955 0.0193 0.0680 0.0271 7 ILE A CD1 44 N N . ILE A 8 ? 0.2161 0.2255 0.2333 0.0118 0.0145 0.0090 8 ILE A N 45 C CA . ILE A 8 ? 0.2152 0.2269 0.2101 0.0120 0.0082 0.0087 8 ILE A CA 46 C C . ILE A 8 ? 0.2199 0.2417 0.2151 0.0175 0.0037 0.0207 8 ILE A C 47 O O . ILE A 8 ? 0.2465 0.2723 0.2405 0.0208 0.0016 0.0278 8 ILE A O 48 C CB . ILE A 8 ? 0.1850 0.1955 0.1598 0.0088 -0.0005 0.0030 8 ILE A CB 49 C CG1 . ILE A 8 ? 0.1718 0.1722 0.1396 0.0025 -0.0012 -0.0094 8 ILE A CG1 50 C CG2 . ILE A 8 ? 0.1579 0.1701 0.1146 0.0096 -0.0043 0.0040 8 ILE A CG2 51 C CD1 . ILE A 8 ? 0.2022 0.2028 0.1526 -0.0004 -0.0136 -0.0124 8 ILE A CD1 52 N N . GLN A 9 ? 0.2345 0.2589 0.2314 0.0183 0.0027 0.0224 9 GLN A N 53 C CA . GLN A 9 ? 0.1614 0.1947 0.1539 0.0216 -0.0063 0.0299 9 GLN A CA 54 C C . GLN A 9 ? 0.1997 0.2315 0.1730 0.0187 -0.0107 0.0224 9 GLN A C 55 O O . GLN A 9 ? 0.1801 0.2082 0.1551 0.0163 -0.0076 0.0171 9 GLN A O 56 C CB . GLN A 9 ? 0.1830 0.2213 0.1984 0.0231 -0.0068 0.0355 9 GLN A CB 57 C CG . GLN A 9 ? 0.1821 0.2302 0.1946 0.0247 -0.0207 0.0407 9 GLN A CG 58 C CD . GLN A 9 ? 0.2412 0.2953 0.2860 0.0252 -0.0227 0.0457 9 GLN A CD 59 O OE1 . GLN A 9 ? 0.2016 0.2558 0.2733 0.0275 -0.0151 0.0528 9 GLN A OE1 60 N NE2 . GLN A 9 ? 0.1416 0.2005 0.1904 0.0230 -0.0316 0.0420 9 GLN A NE2 61 N N . ALA A 10 ? 0.1927 0.2254 0.1501 0.0194 -0.0147 0.0228 10 ALA A N 62 C CA . ALA A 10 ? 0.2044 0.2348 0.1485 0.0172 -0.0166 0.0170 10 ALA A CA 63 C C . ALA A 10 ? 0.2432 0.2772 0.1789 0.0178 -0.0226 0.0169 10 ALA A C 64 O O . ALA A 10 ? 0.2069 0.2422 0.1335 0.0204 -0.0253 0.0214 10 ALA A O 65 C CB . ALA A 10 ? 0.2092 0.2364 0.1482 0.0168 -0.0149 0.0165 10 ALA A CB 66 N N . GLU A 11 ? 0.2386 0.2721 0.1758 0.0153 -0.0238 0.0114 11 GLU A N 67 C CA . GLU A 11 ? 0.2411 0.2770 0.1740 0.0140 -0.0304 0.0074 11 GLU A CA 68 C C . GLU A 11 ? 0.2483 0.2791 0.1780 0.0120 -0.0256 0.0015 11 GLU A C 69 O O . GLU A 11 ? 0.2113 0.2389 0.1459 0.0117 -0.0195 0.0023 11 GLU A O 70 C CB . GLU A 11 ? 0.1421 0.1838 0.0951 0.0126 -0.0363 0.0067 11 GLU A CB 71 C CG . GLU A 11 ? 0.2050 0.2525 0.1712 0.0152 -0.0398 0.0151 11 GLU A CG 72 C CD . GLU A 11 ? 0.2207 0.2729 0.2187 0.0142 -0.0411 0.0162 11 GLU A CD 73 O OE1 . GLU A 11 ? 0.2356 0.2881 0.2459 0.0112 -0.0420 0.0101 11 GLU A OE1 74 O OE2 . GLU A 11 ? 0.1848 0.2400 0.2011 0.0165 -0.0392 0.0237 11 GLU A OE2 75 N N . PHE A 12 ? 0.2337 0.2624 0.1537 0.0106 -0.0277 -0.0041 12 PHE A N 76 C CA . PHE A 12 ? 0.2052 0.2296 0.1317 0.0083 -0.0223 -0.0103 12 PHE A CA 77 C C . PHE A 12 ? 0.2310 0.2541 0.1552 0.0045 -0.0281 -0.0209 12 PHE A C 78 O O . PHE A 12 ? 0.2262 0.2505 0.1340 0.0039 -0.0375 -0.0235 12 PHE A O 79 C CB . PHE A 12 ? 0.1798 0.1984 0.1022 0.0099 -0.0130 -0.0073 12 PHE A CB 80 C CG . PHE A 12 ? 0.2376 0.2504 0.1441 0.0108 -0.0092 -0.0095 12 PHE A CG 81 C CD1 . PHE A 12 ? 0.2300 0.2357 0.1285 0.0081 -0.0061 -0.0196 12 PHE A CD1 82 C CD2 . PHE A 12 ? 0.2249 0.2368 0.1260 0.0141 -0.0058 -0.0022 12 PHE A CD2 83 C CE1 . PHE A 12 ? 0.2137 0.2094 0.0925 0.0091 0.0018 -0.0224 12 PHE A CE1 84 C CE2 . PHE A 12 ? 0.2844 0.2877 0.1718 0.0158 0.0028 -0.0028 12 PHE A CE2 85 C CZ . PHE A 12 ? 0.2888 0.2830 0.1618 0.0134 0.0075 -0.0128 12 PHE A CZ 86 N N . TYR A 13 ? 0.1822 0.2023 0.1224 0.0018 -0.0227 -0.0270 13 TYR A N 87 C CA . TYR A 13 ? 0.2225 0.2391 0.1634 -0.0032 -0.0266 -0.0407 13 TYR A CA 88 C C . TYR A 13 ? 0.2063 0.2146 0.1593 -0.0038 -0.0117 -0.0437 13 TYR A C 89 O O . TYR A 13 ? 0.2147 0.2238 0.1873 -0.0016 -0.0034 -0.0358 13 TYR A O 90 C CB . TYR A 13 ? 0.2308 0.2549 0.1955 -0.0071 -0.0382 -0.0460 13 TYR A CB 91 C CG . TYR A 13 ? 0.2201 0.2412 0.1830 -0.0139 -0.0477 -0.0630 13 TYR A CG 92 C CD1 . TYR A 13 ? 0.2351 0.2575 0.1705 -0.0162 -0.0653 -0.0688 13 TYR A CD1 93 C CD2 . TYR A 13 ? 0.2237 0.2388 0.2097 -0.0181 -0.0389 -0.0735 13 TYR A CD2 94 C CE1 . TYR A 13 ? 0.3171 0.3344 0.2435 -0.0237 -0.0764 -0.0871 13 TYR A CE1 95 C CE2 . TYR A 13 ? 0.2759 0.2862 0.2603 -0.0257 -0.0477 -0.0925 13 TYR A CE2 96 C CZ . TYR A 13 ? 0.3243 0.3354 0.2763 -0.0290 -0.0676 -0.1005 13 TYR A CZ 97 O OH . TYR A 13 ? 0.4400 0.4445 0.3845 -0.0378 -0.0785 -0.1219 13 TYR A OH 98 N N . LEU A 14 ? 0.2236 0.2223 0.1636 -0.0064 -0.0068 -0.0542 14 LEU A N 99 C CA . LEU A 14 ? 0.2178 0.2075 0.1732 -0.0063 0.0101 -0.0557 14 LEU A CA 100 C C . LEU A 14 ? 0.2664 0.2480 0.2317 -0.0132 0.0123 -0.0744 14 LEU A C 101 O O . LEU A 14 ? 0.2683 0.2441 0.2086 -0.0180 0.0045 -0.0890 14 LEU A O 102 C CB . LEU A 14 ? 0.2117 0.1934 0.1494 -0.0029 0.0206 -0.0513 14 LEU A CB 103 C CG . LEU A 14 ? 0.2788 0.2510 0.2372 -0.0021 0.0396 -0.0508 14 LEU A CG 104 C CD1 . LEU A 14 ? 0.1916 0.1712 0.1790 0.0021 0.0426 -0.0346 14 LEU A CD1 105 C CD2 . LEU A 14 ? 0.2913 0.2543 0.2356 0.0008 0.0511 -0.0478 14 LEU A CD2 106 N N . ASN A 15 ? 0.2656 0.2457 0.2659 -0.0139 0.0230 -0.0740 15 ASN A N 107 C CA . ASN A 15 ? 0.2718 0.2422 0.2899 -0.0207 0.0294 -0.0926 15 ASN A CA 108 C C . ASN A 15 ? 0.3376 0.2959 0.3685 -0.0186 0.0521 -0.0905 15 ASN A C 109 O O . ASN A 15 ? 0.2954 0.2573 0.3382 -0.0114 0.0607 -0.0708 15 ASN A O 110 C CB . ASN A 15 ? 0.2857 0.2621 0.3451 -0.0228 0.0286 -0.0929 15 ASN A CB 111 C CG . ASN A 15 ? 0.3605 0.3448 0.4211 -0.0291 0.0071 -0.1052 15 ASN A CG 112 O OD1 . ASN A 15 ? 0.3034 0.2856 0.3339 -0.0342 -0.0078 -0.1195 15 ASN A OD1 113 N ND2 . ASN A 15 ? 0.2450 0.2378 0.3413 -0.0284 0.0056 -0.0986 15 ASN A ND2 114 N N . PRO A 16 ? 0.2891 0.2323 0.3201 -0.0250 0.0616 -0.1109 16 PRO A N 115 C CA . PRO A 16 ? 0.2998 0.2367 0.3166 -0.0351 0.0496 -0.1375 16 PRO A CA 116 C C . PRO A 16 ? 0.3295 0.2592 0.2887 -0.0370 0.0395 -0.1469 16 PRO A C 117 O O . PRO A 16 ? 0.3823 0.3045 0.3174 -0.0454 0.0270 -0.1690 16 PRO A O 118 C CB . PRO A 16 ? 0.3199 0.2397 0.3636 -0.0403 0.0710 -0.1536 16 PRO A CB 119 C CG . PRO A 16 ? 0.3129 0.2251 0.3595 -0.0327 0.0939 -0.1384 16 PRO A CG 120 C CD . PRO A 16 ? 0.2746 0.2049 0.3270 -0.0229 0.0870 -0.1087 16 PRO A CD 121 N N . ASP A 17 ? 0.3187 0.2499 0.2563 -0.0292 0.0445 -0.1297 17 ASP A N 122 C CA . ASP A 17 ? 0.4655 0.3871 0.3499 -0.0288 0.0414 -0.1342 17 ASP A CA 123 C C . ASP A 17 ? 0.4323 0.3631 0.2861 -0.0321 0.0127 -0.1392 17 ASP A C 124 O O . ASP A 17 ? 0.4325 0.3529 0.2421 -0.0319 0.0056 -0.1447 17 ASP A O 125 C CB . ASP A 17 ? 0.4094 0.3341 0.2902 -0.0193 0.0521 -0.1117 17 ASP A CB 126 C CG . ASP A 17 ? 0.4602 0.3784 0.3772 -0.0155 0.0771 -0.1035 17 ASP A CG 127 O OD1 . ASP A 17 ? 0.4482 0.3484 0.3535 -0.0148 0.0976 -0.1083 17 ASP A OD1 128 O OD2 . ASP A 17 ? 0.3751 0.3049 0.3328 -0.0132 0.0773 -0.0918 17 ASP A OD2 129 N N . GLN A 18 ? 0.3802 0.3305 0.2638 -0.0317 -0.0040 -0.1307 18 GLN A N 130 C CA . GLN A 18 ? 0.3708 0.3341 0.2391 -0.0332 -0.0316 -0.1295 18 GLN A CA 131 C C . GLN A 18 ? 0.4184 0.3829 0.2468 -0.0262 -0.0350 -0.1148 18 GLN A C 132 O O . GLN A 18 ? 0.3953 0.3554 0.1899 -0.0268 -0.0518 -0.1136 18 GLN A O 133 C CB . GLN A 18 ? 0.4288 0.3850 0.2835 -0.0427 -0.0500 -0.1502 18 GLN A CB 134 C CG . GLN A 18 ? 0.4514 0.4103 0.3567 -0.0501 -0.0483 -0.1649 18 GLN A CG 135 C CD . GLN A 18 ? 0.5568 0.5112 0.4574 -0.0595 -0.0704 -0.1775 18 GLN A CD 136 O OE1 . GLN A 18 ? 0.5577 0.4912 0.4146 -0.0632 -0.0730 -0.1875 18 GLN A OE1 137 N NE2 . GLN A 18 ? 0.6083 0.5808 0.5550 -0.0632 -0.0859 -0.1768 18 GLN A NE2 138 N N . SER A 19 ? 0.3533 0.3195 0.1910 -0.0185 -0.0188 -0.0974 19 SER A N 139 C CA A SER A 19 ? 0.4228 0.3911 0.2346 -0.0117 -0.0197 -0.0820 19 SER A CA 140 C CA B SER A 19 ? 0.4162 0.3847 0.2274 -0.0118 -0.0203 -0.0823 19 SER A CA 141 C C . SER A 19 ? 0.3253 0.3126 0.1631 -0.0076 -0.0301 -0.0656 19 SER A C 142 O O . SER A 19 ? 0.3485 0.3423 0.2206 -0.0065 -0.0237 -0.0598 19 SER A O 143 C CB A SER A 19 ? 0.4418 0.3982 0.2499 -0.0066 0.0051 -0.0749 19 SER A CB 144 C CB B SER A 19 ? 0.4435 0.3988 0.2457 -0.0068 0.0041 -0.0759 19 SER A CB 145 O OG A SER A 19 ? 0.4191 0.3549 0.2075 -0.0103 0.0203 -0.0907 19 SER A OG 146 O OG B SER A 19 ? 0.4112 0.3699 0.2537 -0.0049 0.0175 -0.0692 19 SER A OG 147 N N . GLY A 20 ? 0.3558 0.3503 0.1761 -0.0052 -0.0447 -0.0577 20 GLY A N 148 C CA . GLY A 20 ? 0.3826 0.3918 0.2269 -0.0011 -0.0504 -0.0427 20 GLY A CA 149 C C . GLY A 20 ? 0.4454 0.4534 0.2741 0.0035 -0.0455 -0.0275 20 GLY A C 150 O O . GLY A 20 ? 0.5220 0.5240 0.3255 0.0015 -0.0439 -0.0265 20 GLY A O 151 N N A GLU A 21 ? 0.3124 0.3273 0.1596 0.0085 -0.0412 -0.0162 21 GLU A N 152 N N C GLU A 21 ? 0.3104 0.3256 0.1581 0.0085 -0.0415 -0.0163 21 GLU A N 153 C CA A GLU A 21 ? 0.2839 0.2972 0.1265 0.0120 -0.0360 -0.0028 21 GLU A CA 154 C CA C GLU A 21 ? 0.2811 0.2948 0.1253 0.0122 -0.0358 -0.0028 21 GLU A CA 155 C C A GLU A 21 ? 0.2435 0.2677 0.1101 0.0151 -0.0409 0.0066 21 GLU A C 156 C C C GLU A 21 ? 0.2403 0.2653 0.1070 0.0147 -0.0429 0.0062 21 GLU A C 157 O O A GLU A 21 ? 0.2425 0.2739 0.1283 0.0153 -0.0412 0.0042 21 GLU A O 158 O O C GLU A 21 ? 0.2471 0.2809 0.1337 0.0145 -0.0465 0.0033 21 GLU A O 159 C CB A GLU A 21 ? 0.3130 0.3177 0.1502 0.0159 -0.0183 -0.0005 21 GLU A CB 160 C CB C GLU A 21 ? 0.2671 0.2752 0.1131 0.0163 -0.0192 0.0001 21 GLU A CB 161 C CG A GLU A 21 ? 0.3692 0.3603 0.1791 0.0147 -0.0083 -0.0069 21 GLU A CG 162 C CG C GLU A 21 ? 0.2974 0.3029 0.1410 0.0209 -0.0118 0.0119 21 GLU A CG 163 C CD A GLU A 21 ? 0.3608 0.3417 0.1694 0.0206 0.0115 -0.0005 21 GLU A CD 164 C CD C GLU A 21 ? 0.2601 0.2625 0.1149 0.0251 0.0023 0.0159 21 GLU A CD 165 O OE1 A GLU A 21 ? 0.3139 0.3002 0.1438 0.0249 0.0152 0.0086 21 GLU A OE1 166 O OE1 C GLU A 21 ? 0.2941 0.2858 0.1421 0.0254 0.0148 0.0127 21 GLU A OE1 167 O OE2 A GLU A 21 ? 0.2888 0.2562 0.0781 0.0205 0.0242 -0.0048 21 GLU A OE2 168 O OE2 C GLU A 21 ? 0.2306 0.2401 0.1088 0.0256 0.0009 0.0212 21 GLU A OE2 169 N N . PHE A 22 ? 0.2258 0.2505 0.0897 0.0179 -0.0429 0.0173 22 PHE A N 170 C CA . PHE A 22 ? 0.2222 0.2572 0.1086 0.0217 -0.0466 0.0263 22 PHE A CA 171 C C . PHE A 22 ? 0.2166 0.2480 0.1010 0.0268 -0.0364 0.0370 22 PHE A C 172 O O . PHE A 22 ? 0.2845 0.3088 0.1502 0.0282 -0.0355 0.0424 22 PHE A O 173 C CB . PHE A 22 ? 0.2327 0.2747 0.1238 0.0212 -0.0637 0.0301 22 PHE A CB 174 C CG . PHE A 22 ? 0.2494 0.3049 0.1707 0.0257 -0.0665 0.0412 22 PHE A CG 175 C CD1 . PHE A 22 ? 0.2185 0.2825 0.1714 0.0229 -0.0706 0.0379 22 PHE A CD1 176 C CD2 . PHE A 22 ? 0.3578 0.4126 0.2831 0.0311 -0.0607 0.0546 22 PHE A CD2 177 C CE1 . PHE A 22 ? 0.2705 0.3403 0.2581 0.0252 -0.0678 0.0472 22 PHE A CE1 178 C CE2 . PHE A 22 ? 0.3310 0.3956 0.2914 0.0341 -0.0599 0.0652 22 PHE A CE2 179 C CZ . PHE A 22 ? 0.2351 0.3051 0.2266 0.0306 -0.0626 0.0602 22 PHE A CZ 180 N N . MET A 23 ? 0.2252 0.2609 0.1276 0.0295 -0.0284 0.0401 23 MET A N 181 C CA . MET A 23 ? 0.3009 0.3335 0.2110 0.0339 -0.0178 0.0498 23 MET A CA 182 C C . MET A 23 ? 0.2406 0.2764 0.1817 0.0326 -0.0138 0.0500 23 MET A C 183 O O . MET A 23 ? 0.2300 0.2673 0.1810 0.0283 -0.0161 0.0414 23 MET A O 184 C CB . MET A 23 ? 0.2200 0.2441 0.1232 0.0341 -0.0063 0.0471 23 MET A CB 185 C CG . MET A 23 ? 0.3025 0.3268 0.2195 0.0290 -0.0056 0.0369 23 MET A CG 186 S SD . MET A 23 ? 0.2577 0.2830 0.2046 0.0271 -0.0017 0.0364 23 MET A SD 187 C CE . MET A 23 ? 0.2238 0.2437 0.1819 0.0312 0.0110 0.0444 23 MET A CE 188 N N . PHE A 24 ? 0.2160 0.2505 0.1716 0.0365 -0.0056 0.0595 24 PHE A N 189 C CA . PHE A 24 ? 0.2379 0.2718 0.2228 0.0345 0.0011 0.0569 24 PHE A CA 190 C C . PHE A 24 ? 0.2864 0.3146 0.2803 0.0335 0.0099 0.0542 24 PHE A C 191 O O . PHE A 24 ? 0.2030 0.2280 0.1931 0.0381 0.0167 0.0630 24 PHE A O 192 C CB . PHE A 24 ? 0.1831 0.2201 0.1892 0.0394 0.0046 0.0702 24 PHE A CB 193 C CG . PHE A 24 ? 0.2220 0.2644 0.2440 0.0380 -0.0005 0.0698 24 PHE A CG 194 C CD1 . PHE A 24 ? 0.2353 0.2742 0.2863 0.0355 0.0093 0.0651 24 PHE A CD1 195 C CD2 . PHE A 24 ? 0.2335 0.2833 0.2448 0.0390 -0.0141 0.0736 24 PHE A CD2 196 C CE1 . PHE A 24 ? 0.2095 0.2513 0.2809 0.0349 0.0091 0.0660 24 PHE A CE1 197 C CE2 . PHE A 24 ? 0.1961 0.2516 0.2322 0.0380 -0.0179 0.0749 24 PHE A CE2 198 C CZ . PHE A 24 ? 0.2038 0.2550 0.2712 0.0365 -0.0045 0.0720 24 PHE A CZ 199 N N . ASP A 25 ? 0.2207 0.2465 0.2261 0.0275 0.0096 0.0422 25 ASP A N 200 C CA . ASP A 25 ? 0.1936 0.2159 0.2143 0.0248 0.0129 0.0375 25 ASP A CA 201 C C . ASP A 25 ? 0.2553 0.2742 0.3025 0.0215 0.0180 0.0320 25 ASP A C 202 O O . ASP A 25 ? 0.1934 0.2099 0.2391 0.0183 0.0175 0.0249 25 ASP A O 203 C CB . ASP A 25 ? 0.1934 0.2155 0.2009 0.0195 0.0036 0.0270 25 ASP A CB 204 C CG . ASP A 25 ? 0.2922 0.3130 0.3195 0.0157 0.0014 0.0221 25 ASP A CG 205 O OD1 . ASP A 25 ? 0.3013 0.3235 0.3317 0.0170 0.0012 0.0259 25 ASP A OD1 206 O OD2 . ASP A 25 ? 0.2875 0.3055 0.3297 0.0108 -0.0002 0.0137 25 ASP A OD2 207 N N . PHE A 26 ? 0.2123 0.2291 0.2866 0.0222 0.0255 0.0348 26 PHE A N 208 C CA . PHE A 26 ? 0.2152 0.2272 0.3192 0.0175 0.0306 0.0262 26 PHE A CA 209 C C . PHE A 26 ? 0.1809 0.1919 0.3016 0.0115 0.0244 0.0164 26 PHE A C 210 O O . PHE A 26 ? 0.2187 0.2314 0.3591 0.0151 0.0299 0.0252 26 PHE A O 211 C CB . PHE A 26 ? 0.1750 0.1860 0.3085 0.0241 0.0462 0.0404 26 PHE A CB 212 C CG . PHE A 26 ? 0.1657 0.1704 0.3378 0.0191 0.0547 0.0308 26 PHE A CG 213 C CD1 . PHE A 26 ? 0.2237 0.2230 0.4023 0.0158 0.0595 0.0226 26 PHE A CD1 214 C CD2 . PHE A 26 ? 0.2376 0.2403 0.4435 0.0171 0.0593 0.0287 26 PHE A CD2 215 C CE1 . PHE A 26 ? 0.2383 0.2289 0.4520 0.0100 0.0691 0.0106 26 PHE A CE1 216 C CE2 . PHE A 26 ? 0.2444 0.2404 0.4887 0.0112 0.0664 0.0171 26 PHE A CE2 217 C CZ . PHE A 26 ? 0.2441 0.2334 0.4902 0.0074 0.0715 0.0071 26 PHE A CZ 218 N N . ASP A 27 ? 0.2376 0.1949 0.2311 0.0061 0.0193 -0.0005 27 ASP A N 219 C CA . ASP A 27 ? 0.2205 0.1872 0.2103 -0.0009 0.0055 -0.0048 27 ASP A CA 220 C C . ASP A 27 ? 0.2800 0.2706 0.2820 0.0070 -0.0046 0.0045 27 ASP A C 221 O O . ASP A 27 ? 0.2464 0.2600 0.2682 0.0026 -0.0142 0.0019 27 ASP A O 222 C CB . ASP A 27 ? 0.2386 0.2017 0.2451 -0.0142 0.0044 -0.0133 27 ASP A CB 223 C CG . ASP A 27 ? 0.2644 0.1990 0.2551 -0.0192 0.0113 -0.0296 27 ASP A CG 224 O OD1 . ASP A 27 ? 0.3080 0.2356 0.2755 -0.0141 0.0181 -0.0354 27 ASP A OD1 225 O OD2 . ASP A 27 ? 0.3142 0.2324 0.3151 -0.0298 0.0113 -0.0382 27 ASP A OD2 226 N N . GLY A 28 ? 0.2430 0.2299 0.2364 0.0185 -0.0022 0.0125 28 GLY A N 227 C CA . GLY A 28 ? 0.2475 0.2512 0.2516 0.0311 -0.0109 0.0172 28 GLY A CA 228 C C . GLY A 28 ? 0.2896 0.3134 0.3199 0.0352 -0.0003 0.0202 28 GLY A C 229 O O . GLY A 28 ? 0.2552 0.2971 0.2981 0.0476 -0.0037 0.0194 28 GLY A O 230 N N . ASP A 29 ? 0.1977 0.2172 0.2338 0.0261 0.0121 0.0230 29 ASP A N 231 C CA . ASP A 29 ? 0.1900 0.2232 0.2375 0.0270 0.0224 0.0286 29 ASP A CA 232 C C . ASP A 29 ? 0.2706 0.2844 0.3015 0.0304 0.0281 0.0339 29 ASP A C 233 O O . ASP A 29 ? 0.2386 0.2342 0.2615 0.0283 0.0280 0.0333 29 ASP A O 234 C CB . ASP A 29 ? 0.1780 0.2213 0.2424 0.0111 0.0289 0.0321 29 ASP A CB 235 C CG . ASP A 29 ? 0.2312 0.3120 0.3223 0.0048 0.0263 0.0259 29 ASP A CG 236 O OD1 . ASP A 29 ? 0.3025 0.4154 0.4079 0.0136 0.0304 0.0229 29 ASP A OD1 237 O OD2 . ASP A 29 ? 0.2303 0.3116 0.3307 -0.0087 0.0203 0.0213 29 ASP A OD2 238 N N . GLU A 30 ? 0.2417 0.2643 0.2692 0.0354 0.0330 0.0362 30 GLU A N 239 C CA . GLU A 30 ? 0.2223 0.2325 0.2349 0.0370 0.0346 0.0397 30 GLU A CA 240 C C . GLU A 30 ? 0.2289 0.2357 0.2431 0.0307 0.0367 0.0501 30 GLU A C 241 O O . GLU A 30 ? 0.2288 0.2438 0.2440 0.0241 0.0417 0.0573 30 GLU A O 242 C CB . GLU A 30 ? 0.2041 0.2210 0.2061 0.0437 0.0371 0.0353 30 GLU A CB 243 C CG . GLU A 30 ? 0.2569 0.2674 0.2431 0.0412 0.0366 0.0381 30 GLU A CG 244 C CD . GLU A 30 ? 0.3053 0.3214 0.2756 0.0448 0.0406 0.0307 30 GLU A CD 245 O OE1 . GLU A 30 ? 0.2867 0.3143 0.2626 0.0524 0.0464 0.0222 30 GLU A OE1 246 O OE2 . GLU A 30 ? 0.3118 0.3240 0.2656 0.0408 0.0373 0.0311 30 GLU A OE2 247 N N . ILE A 31 ? 0.2048 0.1996 0.2197 0.0328 0.0329 0.0513 31 ILE A N 248 C CA . ILE A 31 ? 0.2031 0.1903 0.2199 0.0332 0.0296 0.0625 31 ILE A CA 249 C C . ILE A 31 ? 0.2333 0.2296 0.2342 0.0344 0.0260 0.0688 31 ILE A C 250 O O . ILE A 31 ? 0.2533 0.2468 0.2408 0.0302 0.0251 0.0820 31 ILE A O 251 C CB . ILE A 31 ? 0.2562 0.2347 0.2878 0.0404 0.0257 0.0579 31 ILE A CB 252 C CG1 . ILE A 31 ? 0.2194 0.1878 0.2585 0.0377 0.0304 0.0468 31 ILE A CG1 253 C CG2 . ILE A 31 ? 0.2806 0.2456 0.3167 0.0467 0.0174 0.0709 31 ILE A CG2 254 C CD1 . ILE A 31 ? 0.2492 0.2133 0.3031 0.0458 0.0317 0.0362 31 ILE A CD1 255 N N . PHE A 32 ? 0.2262 0.2305 0.2234 0.0367 0.0238 0.0595 32 PHE A N 256 C CA . PHE A 32 ? 0.2124 0.2251 0.1916 0.0354 0.0188 0.0603 32 PHE A CA 257 C C . PHE A 32 ? 0.2466 0.2596 0.2210 0.0332 0.0191 0.0461 32 PHE A C 258 O O . PHE A 32 ? 0.2506 0.2570 0.2345 0.0323 0.0221 0.0398 32 PHE A O 259 C CB . PHE A 32 ? 0.2280 0.2453 0.2114 0.0391 0.0052 0.0704 32 PHE A CB 260 C CG . PHE A 32 ? 0.2040 0.2329 0.2144 0.0434 -0.0001 0.0618 32 PHE A CG 261 C CD1 . PHE A 32 ? 0.2526 0.2983 0.2631 0.0374 -0.0048 0.0519 32 PHE A CD1 262 C CD2 . PHE A 32 ? 0.2679 0.2927 0.3042 0.0513 0.0016 0.0610 32 PHE A CD2 263 C CE1 . PHE A 32 ? 0.3391 0.4052 0.3792 0.0369 -0.0061 0.0426 32 PHE A CE1 264 C CE2 . PHE A 32 ? 0.2645 0.3089 0.3288 0.0549 0.0015 0.0494 32 PHE A CE2 265 C CZ . PHE A 32 ? 0.3247 0.3937 0.3931 0.0467 -0.0014 0.0410 32 PHE A CZ 266 N N . HIS A 33 ? 0.2617 0.2775 0.2156 0.0298 0.0161 0.0411 33 HIS A N 267 C CA . HIS A 33 ? 0.2505 0.2594 0.1978 0.0234 0.0134 0.0282 33 HIS A CA 268 C C . HIS A 33 ? 0.2700 0.2927 0.2069 0.0163 0.0016 0.0261 33 HIS A C 269 O O . HIS A 33 ? 0.2625 0.2967 0.1896 0.0188 -0.0051 0.0358 33 HIS A O 270 C CB . HIS A 33 ? 0.2397 0.2281 0.1691 0.0265 0.0201 0.0168 33 HIS A CB 271 C CG . HIS A 33 ? 0.2610 0.2539 0.1678 0.0294 0.0236 0.0105 33 HIS A CG 272 N ND1 . HIS A 33 ? 0.2888 0.2944 0.1964 0.0363 0.0338 0.0136 33 HIS A ND1 273 C CD2 . HIS A 33 ? 0.3127 0.3010 0.1936 0.0239 0.0201 -0.0016 33 HIS A CD2 274 C CE1 . HIS A 33 ? 0.3245 0.3357 0.2067 0.0357 0.0392 0.0039 33 HIS A CE1 275 N NE2 . HIS A 33 ? 0.3352 0.3333 0.1984 0.0292 0.0301 -0.0062 33 HIS A NE2 276 N N . VAL A 34 ? 0.2632 0.2832 0.1989 0.0048 -0.0026 0.0145 34 VAL A N 277 C CA . VAL A 34 ? 0.2885 0.3243 0.2139 -0.0052 -0.0165 0.0087 34 VAL A CA 278 C C . VAL A 34 ? 0.3341 0.3455 0.2225 -0.0122 -0.0146 -0.0076 34 VAL A C 279 O O . VAL A 34 ? 0.4044 0.3852 0.2860 -0.0169 -0.0077 -0.0184 34 VAL A O 280 C CB . VAL A 34 ? 0.2680 0.3265 0.2228 -0.0184 -0.0236 0.0035 34 VAL A CB 281 C CG1 . VAL A 34 ? 0.3130 0.3889 0.2567 -0.0330 -0.0405 -0.0067 34 VAL A CG1 282 C CG2 . VAL A 34 ? 0.2830 0.3711 0.2769 -0.0065 -0.0266 0.0148 34 VAL A CG2 283 N N . ASP A 35 ? 0.3085 0.3285 0.1687 -0.0121 -0.0209 -0.0093 35 ASP A N 284 C CA . ASP A 35 ? 0.4364 0.4362 0.2582 -0.0194 -0.0200 -0.0302 35 ASP A CA 285 C C . ASP A 35 ? 0.4592 0.4621 0.2835 -0.0405 -0.0354 -0.0425 35 ASP A C 286 O O . ASP A 35 ? 0.4279 0.4639 0.2553 -0.0485 -0.0536 -0.0384 35 ASP A O 287 C CB . ASP A 35 ? 0.4821 0.4963 0.2676 -0.0167 -0.0214 -0.0277 35 ASP A CB 288 C CG . ASP A 35 ? 0.5863 0.5806 0.3271 -0.0222 -0.0164 -0.0544 35 ASP A CG 289 O OD1 . ASP A 35 ? 0.5093 0.4810 0.2438 -0.0337 -0.0225 -0.0743 35 ASP A OD1 290 O OD2 . ASP A 35 ? 0.6500 0.6502 0.3597 -0.0166 -0.0046 -0.0570 35 ASP A OD2 291 N N . MET A 36 ? 0.4757 0.4438 0.2987 -0.0509 -0.0300 -0.0565 36 MET A N 292 C CA . MET A 36 ? 0.4362 0.4092 0.2688 -0.0777 -0.0417 -0.0663 36 MET A CA 293 C C . MET A 36 ? 0.5923 0.5693 0.3923 -0.0933 -0.0571 -0.0853 36 MET A C 294 O O . MET A 36 ? 0.5566 0.5703 0.3725 -0.1123 -0.0750 -0.0879 36 MET A O 295 C CB . MET A 36 ? 0.4704 0.3949 0.3014 -0.0902 -0.0318 -0.0730 36 MET A CB 296 C CG . MET A 36 ? 0.5161 0.4329 0.3696 -0.0776 -0.0183 -0.0553 36 MET A CG 297 S SD . MET A 36 ? 0.5686 0.5463 0.4741 -0.0797 -0.0177 -0.0381 36 MET A SD 298 C CE . MET A 36 ? 0.5630 0.5599 0.4849 -0.1189 -0.0236 -0.0501 36 MET A CE 299 N N . ALA A 37 ? 0.6324 0.5764 0.3883 -0.0848 -0.0504 -0.1007 37 ALA A N 300 C CA . ALA A 37 ? 0.6118 0.5550 0.3258 -0.0996 -0.0634 -0.1227 37 ALA A CA 301 C C . ALA A 37 ? 0.6244 0.6226 0.3325 -0.0993 -0.0818 -0.1093 37 ALA A C 302 O O . ALA A 37 ? 0.6731 0.6940 0.3705 -0.1198 -0.1048 -0.1192 37 ALA A O 303 C CB . ALA A 37 ? 0.6210 0.5195 0.2898 -0.0864 -0.0474 -0.1453 37 ALA A CB 304 N N . LYS A 38 ? 0.6133 0.6302 0.3267 -0.0774 -0.0743 -0.0858 38 LYS A N 305 C CA . LYS A 38 ? 0.6212 0.6776 0.3209 -0.0750 -0.0933 -0.0676 38 LYS A CA 306 C C . LYS A 38 ? 0.6036 0.7007 0.3585 -0.0723 -0.1122 -0.0459 38 LYS A C 307 O O . LYS A 38 ? 0.4861 0.6157 0.2363 -0.0695 -0.1366 -0.0307 38 LYS A O 308 C CB . LYS A 38 ? 0.5999 0.6516 0.2731 -0.0572 -0.0760 -0.0516 38 LYS A CB 309 C CG . LYS A 38 ? 0.7251 0.7521 0.3470 -0.0565 -0.0570 -0.0744 38 LYS A CG 310 C CD . LYS A 38 ? 0.8102 0.8420 0.4167 -0.0424 -0.0370 -0.0569 38 LYS A CD 311 C CE . LYS A 38 ? 0.9068 0.9224 0.4763 -0.0377 -0.0157 -0.0811 38 LYS A CE 312 N NZ . LYS A 38 ? 0.9690 0.9945 0.5246 -0.0302 0.0053 -0.0651 38 LYS A NZ 313 N N . LYS A 39 ? 0.4786 0.5733 0.2834 -0.0718 -0.1014 -0.0452 39 LYS A N 314 C CA . LYS A 39 ? 0.4647 0.6000 0.3282 -0.0655 -0.1119 -0.0292 39 LYS A CA 315 C C . LYS A 39 ? 0.4602 0.6056 0.3263 -0.0410 -0.1164 -0.0018 39 LYS A C 316 O O . LYS A 39 ? 0.4346 0.6151 0.3198 -0.0335 -0.1413 0.0110 39 LYS A O 317 C CB . LYS A 39 ? 0.4648 0.6479 0.3515 -0.0828 -0.1408 -0.0382 39 LYS A CB 318 C CG . LYS A 39 ? 0.5435 0.7152 0.4194 -0.1150 -0.1414 -0.0663 39 LYS A CG 319 C CD . LYS A 39 ? 0.7275 0.9578 0.6286 -0.1337 -0.1739 -0.0753 39 LYS A CD 320 C CE . LYS A 39 ? 0.8614 1.0698 0.7546 -0.1664 -0.1711 -0.1023 39 LYS A CE 321 N NZ . LYS A 39 ? 0.9778 1.1244 0.8005 -0.1696 -0.1636 -0.1177 39 LYS A NZ 322 N N . GLU A 40 ? 0.4735 0.5869 0.3207 -0.0288 -0.0942 0.0070 40 GLU A N 323 C CA A GLU A 40 ? 0.4542 0.5669 0.2989 -0.0112 -0.0954 0.0334 40 GLU A CA 324 C CA B GLU A 40 ? 0.4570 0.5703 0.3030 -0.0111 -0.0957 0.0335 40 GLU A CA 325 C C . GLU A 40 ? 0.3835 0.4769 0.2549 0.0001 -0.0714 0.0399 40 GLU A C 326 O O . GLU A 40 ? 0.3812 0.4541 0.2493 -0.0035 -0.0512 0.0262 40 GLU A O 327 C CB A GLU A 40 ? 0.4776 0.5762 0.2584 -0.0143 -0.0944 0.0396 40 GLU A CB 328 C CB B GLU A 40 ? 0.4865 0.5872 0.2691 -0.0138 -0.0969 0.0412 40 GLU A CB 329 C CG A GLU A 40 ? 0.5367 0.6549 0.2817 -0.0233 -0.1244 0.0409 40 GLU A CG 330 C CG B GLU A 40 ? 0.5119 0.5866 0.2640 -0.0166 -0.0668 0.0283 40 GLU A CG 331 C CD A GLU A 40 ? 0.6217 0.7163 0.3027 -0.0273 -0.1138 0.0406 40 GLU A CD 332 C CD B GLU A 40 ? 0.5767 0.6469 0.2689 -0.0208 -0.0617 0.0373 40 GLU A CD 333 O OE1 A GLU A 40 ? 0.6630 0.7390 0.3277 -0.0261 -0.0848 0.0393 40 GLU A OE1 334 O OE1 B GLU A 40 ? 0.4555 0.5160 0.1416 -0.0171 -0.0377 0.0440 40 GLU A OE1 335 O OE2 A GLU A 40 ? 0.7095 0.8075 0.3605 -0.0308 -0.1331 0.0398 40 GLU A OE2 336 O OE2 B GLU A 40 ? 0.6550 0.7282 0.3144 -0.0271 -0.0792 0.0355 40 GLU A OE2 337 N N . THR A 41 ? 0.3424 0.4396 0.2386 0.0145 -0.0765 0.0599 41 THR A N 338 C CA . THR A 41 ? 0.3137 0.3929 0.2317 0.0234 -0.0572 0.0658 41 THR A CA 339 C C . THR A 41 ? 0.4051 0.4622 0.2860 0.0219 -0.0426 0.0756 41 THR A C 340 O O . THR A 41 ? 0.4653 0.5182 0.3144 0.0210 -0.0515 0.0930 41 THR A O 341 C CB . THR A 41 ? 0.3681 0.4542 0.3246 0.0393 -0.0683 0.0801 41 THR A CB 342 O OG1 . THR A 41 ? 0.3655 0.4850 0.3647 0.0408 -0.0786 0.0676 41 THR A OG1 343 C CG2 . THR A 41 ? 0.3373 0.4011 0.3108 0.0454 -0.0489 0.0829 41 THR A CG2 344 N N . VAL A 42 ? 0.3646 0.4101 0.2494 0.0205 -0.0208 0.0651 42 VAL A N 345 C CA . VAL A 42 ? 0.3497 0.3871 0.2110 0.0178 -0.0034 0.0693 42 VAL A CA 346 C C . VAL A 42 ? 0.3224 0.3511 0.2120 0.0222 0.0071 0.0780 42 VAL A C 347 O O . VAL A 42 ? 0.2644 0.2911 0.1776 0.0259 0.0156 0.0660 42 VAL A O 348 C CB . VAL A 42 ? 0.3601 0.3967 0.2070 0.0157 0.0117 0.0459 42 VAL A CB 349 C CG1 . VAL A 42 ? 0.4174 0.4599 0.2503 0.0142 0.0322 0.0465 42 VAL A CG1 350 C CG2 . VAL A 42 ? 0.3166 0.3556 0.1315 0.0086 0.0014 0.0321 42 VAL A CG2 351 N N . TRP A 43 ? 0.3055 0.3245 0.1880 0.0201 0.0047 0.0993 43 TRP A N 352 C CA . TRP A 43 ? 0.3249 0.3313 0.2320 0.0204 0.0129 0.1061 43 TRP A CA 353 C C . TRP A 43 ? 0.3436 0.3606 0.2485 0.0113 0.0344 0.0990 43 TRP A C 354 O O . TRP A 43 ? 0.3411 0.3700 0.2176 0.0024 0.0448 0.0994 43 TRP A O 355 C CB . TRP A 43 ? 0.2962 0.2783 0.1949 0.0199 0.0014 0.1315 43 TRP A CB 356 C CG . TRP A 43 ? 0.3737 0.3524 0.2879 0.0356 -0.0219 0.1359 43 TRP A CG 357 C CD1 . TRP A 43 ? 0.4125 0.3965 0.3064 0.0392 -0.0420 0.1438 43 TRP A CD1 358 C CD2 . TRP A 43 ? 0.3165 0.2929 0.2737 0.0499 -0.0270 0.1274 43 TRP A CD2 359 N NE1 . TRP A 43 ? 0.3934 0.3839 0.3224 0.0568 -0.0606 0.1418 43 TRP A NE1 360 C CE2 . TRP A 43 ? 0.3849 0.3719 0.3534 0.0640 -0.0495 0.1315 43 TRP A CE2 361 C CE3 . TRP A 43 ? 0.3142 0.2844 0.3003 0.0517 -0.0148 0.1147 43 TRP A CE3 362 C CZ2 . TRP A 43 ? 0.4163 0.4123 0.4301 0.0811 -0.0562 0.1215 43 TRP A CZ2 363 C CZ3 . TRP A 43 ? 0.2932 0.2657 0.3142 0.0666 -0.0207 0.1053 43 TRP A CZ3 364 C CH2 . TRP A 43 ? 0.2857 0.2734 0.3234 0.0816 -0.0393 0.1076 43 TRP A CH2 365 N N . ARG A 44 ? 0.2864 0.3043 0.2223 0.0136 0.0409 0.0905 44 ARG A N 366 C CA . ARG A 44 ? 0.2746 0.3133 0.2201 0.0084 0.0576 0.0805 44 ARG A CA 367 C C . ARG A 44 ? 0.3229 0.3666 0.2568 -0.0102 0.0697 0.0951 44 ARG A C 368 O O . ARG A 44 ? 0.4028 0.4749 0.3303 -0.0177 0.0867 0.0882 44 ARG A O 369 C CB . ARG A 44 ? 0.2421 0.2810 0.2205 0.0140 0.0562 0.0703 44 ARG A CB 370 C CG . ARG A 44 ? 0.2321 0.3005 0.2294 0.0133 0.0676 0.0580 44 ARG A CG 371 C CD . ARG A 44 ? 0.2546 0.3398 0.2432 0.0248 0.0738 0.0423 44 ARG A CD 372 N NE . ARG A 44 ? 0.2147 0.3350 0.2301 0.0297 0.0839 0.0284 44 ARG A NE 373 C CZ . ARG A 44 ? 0.2395 0.3956 0.2600 0.0193 0.1022 0.0259 44 ARG A CZ 374 N NH1 . ARG A 44 ? 0.2743 0.4269 0.2639 0.0012 0.1121 0.0397 44 ARG A NH1 375 N NH2 . ARG A 44 ? 0.2296 0.4277 0.2857 0.0268 0.1103 0.0098 44 ARG A NH2 376 N N . LEU A 45 ? 0.2786 0.2932 0.2106 -0.0180 0.0620 0.1142 45 LEU A N 377 C CA . LEU A 45 ? 0.3164 0.3181 0.2262 -0.0399 0.0691 0.1316 45 LEU A CA 378 C C . LEU A 45 ? 0.4436 0.4097 0.3170 -0.0367 0.0518 0.1476 45 LEU A C 379 O O . LEU A 45 ? 0.4520 0.3998 0.3348 -0.0198 0.0326 0.1510 45 LEU A O 380 C CB . LEU A 45 ? 0.3738 0.3569 0.3066 -0.0526 0.0705 0.1368 45 LEU A CB 381 C CG . LEU A 45 ? 0.4168 0.4379 0.3892 -0.0575 0.0828 0.1191 45 LEU A CG 382 C CD1 . LEU A 45 ? 0.4298 0.4320 0.4171 -0.0796 0.0844 0.1257 45 LEU A CD1 383 C CD2 . LEU A 45 ? 0.4176 0.4896 0.3905 -0.0638 0.1024 0.1077 45 LEU A CD2 384 N N A GLU A 46 ? 0.4743 0.6674 0.5029 0.0515 0.1461 0.2044 46 GLU A N 385 N N B GLU A 46 ? 0.4722 0.6677 0.5021 0.0522 0.1472 0.2040 46 GLU A N 386 C CA A GLU A 46 ? 0.5184 0.6791 0.4890 0.0540 0.1410 0.2161 46 GLU A CA 387 C CA B GLU A 46 ? 0.5280 0.6960 0.5000 0.0550 0.1473 0.2193 46 GLU A CA 388 C C A GLU A 46 ? 0.5077 0.6365 0.5064 0.0337 0.1182 0.2298 46 GLU A C 389 C C B GLU A 46 ? 0.5097 0.6421 0.5027 0.0364 0.1208 0.2284 46 GLU A C 390 O O A GLU A 46 ? 0.5358 0.6330 0.5001 0.0392 0.0998 0.2285 46 GLU A O 391 O O B GLU A 46 ? 0.5198 0.6210 0.4762 0.0434 0.1005 0.2209 46 GLU A O 392 C CB A GLU A 46 ? 0.5856 0.7610 0.5218 0.0610 0.1702 0.2400 46 GLU A CB 393 C CB B GLU A 46 ? 0.5908 0.7813 0.5562 0.0555 0.1775 0.2478 46 GLU A CB 394 C CG A GLU A 46 ? 0.6249 0.8230 0.6196 0.0408 0.1849 0.2724 46 GLU A CG 395 C CG B GLU A 46 ? 0.6319 0.8496 0.5885 0.0759 0.2049 0.2355 46 GLU A CG 396 C CD A GLU A 46 ? 0.6789 0.8431 0.6662 0.0251 0.1719 0.2957 46 GLU A CD 397 C CD B GLU A 46 ? 0.5341 0.7964 0.5703 0.0734 0.2099 0.2334 46 GLU A CD 398 O OE1 A GLU A 46 ? 0.7156 0.8845 0.7538 0.0028 0.1766 0.3180 46 GLU A OE1 399 O OE1 B GLU A 46 ? 0.4957 0.7822 0.6050 0.0476 0.2024 0.2538 46 GLU A OE1 400 O OE2 A GLU A 46 ? 0.7056 0.8367 0.6372 0.0348 0.1544 0.2910 46 GLU A OE2 401 O OE2 B GLU A 46 ? 0.4871 0.7544 0.5113 0.0953 0.2167 0.2101 46 GLU A OE2 402 N N A GLU A 47 ? 0.4906 0.6260 0.5525 0.0102 0.1188 0.2435 47 GLU A N 403 N N B GLU A 47 ? 0.4954 0.6316 0.5499 0.0126 0.1208 0.2450 47 GLU A N 404 C CA A GLU A 47 ? 0.5097 0.6011 0.5933 -0.0093 0.1025 0.2558 47 GLU A CA 405 C CA B GLU A 47 ? 0.5140 0.6049 0.5855 -0.0045 0.1034 0.2566 47 GLU A CA 406 C C A GLU A 47 ? 0.4724 0.5201 0.5443 -0.0012 0.0758 0.2253 47 GLU A C 407 C C B GLU A 47 ? 0.4690 0.5173 0.5357 0.0013 0.0760 0.2253 47 GLU A C 408 O O A GLU A 47 ? 0.4626 0.4678 0.5298 -0.0017 0.0665 0.2357 47 GLU A O 409 O O B GLU A 47 ? 0.4591 0.4655 0.5214 0.0010 0.0661 0.2353 47 GLU A O 410 C CB A GLU A 47 ? 0.5155 0.6143 0.6636 -0.0415 0.1031 0.2678 47 GLU A CB 411 C CB B GLU A 47 ? 0.5204 0.6157 0.6532 -0.0367 0.1081 0.2768 47 GLU A CB 412 C CG A GLU A 47 ? 0.4823 0.5841 0.6607 -0.0494 0.0830 0.2347 47 GLU A CG 413 C CG B GLU A 47 ? 0.5032 0.6277 0.6836 -0.0491 0.0994 0.2557 47 GLU A CG 414 C CD A GLU A 47 ? 0.4960 0.5967 0.7316 -0.0881 0.0727 0.2457 47 GLU A CD 415 C CD B GLU A 47 ? 0.5014 0.6988 0.7217 -0.0522 0.1252 0.2775 47 GLU A CD 416 O OE1 A GLU A 47 ? 0.3944 0.4385 0.6276 -0.1037 0.0489 0.2263 47 GLU A OE1 417 O OE1 B GLU A 47 ? 0.4018 0.6271 0.5865 -0.0254 0.1501 0.2820 47 GLU A OE1 418 O OE2 A GLU A 47 ? 0.4599 0.6151 0.7415 -0.1040 0.0887 0.2738 47 GLU A OE2 419 O OE2 B GLU A 47 ? 0.4479 0.6691 0.7297 -0.0795 0.1172 0.2847 47 GLU A OE2 420 N N . PHE A 48 ? 0.3929 0.4507 0.4617 0.0089 0.0675 0.1910 48 PHE A N 421 C CA . PHE A 48 ? 0.4007 0.4206 0.4639 0.0155 0.0476 0.1626 48 PHE A CA 422 C C . PHE A 48 ? 0.3825 0.3863 0.4138 0.0323 0.0394 0.1668 48 PHE A C 423 O O . PHE A 48 ? 0.3574 0.3252 0.3984 0.0353 0.0292 0.1647 48 PHE A O 424 C CB . PHE A 48 ? 0.3007 0.3354 0.3599 0.0249 0.0431 0.1289 48 PHE A CB 425 C CG . PHE A 48 ? 0.3355 0.3864 0.4322 0.0098 0.0416 0.1234 48 PHE A CG 426 C CD1 . PHE A 48 ? 0.2963 0.3450 0.4300 -0.0169 0.0402 0.1439 48 PHE A CD1 427 C CD2 . PHE A 48 ? 0.2635 0.3307 0.3590 0.0205 0.0383 0.0994 48 PHE A CD2 428 C CE1 . PHE A 48 ? 0.3210 0.3910 0.4932 -0.0355 0.0309 0.1408 48 PHE A CE1 429 C CE2 . PHE A 48 ? 0.2515 0.3403 0.3843 0.0076 0.0310 0.0982 48 PHE A CE2 430 C CZ . PHE A 48 ? 0.2617 0.3555 0.4346 -0.0220 0.0248 0.1189 48 PHE A CZ 431 N N . GLY A 49 ? 0.4119 0.4420 0.4040 0.0437 0.0438 0.1739 49 GLY A N 432 C CA . GLY A 49 ? 0.4138 0.4378 0.3740 0.0558 0.0279 0.1780 49 GLY A CA 433 C C . GLY A 49 ? 0.4539 0.4629 0.4178 0.0562 0.0234 0.2152 49 GLY A C 434 O O . GLY A 49 ? 0.4449 0.4527 0.3972 0.0664 0.0048 0.2243 49 GLY A O 435 N N . ARG A 50 ? 0.4493 0.4485 0.4327 0.0444 0.0392 0.2402 50 ARG A N 436 C CA . ARG A 50 ? 0.5117 0.4860 0.5004 0.0441 0.0366 0.2686 50 ARG A CA 437 C C . ARG A 50 ? 0.5065 0.4386 0.5316 0.0455 0.0290 0.2568 50 ARG A C 438 O O . ARG A 50 ? 0.5813 0.4938 0.6093 0.0537 0.0230 0.2676 50 ARG A O 439 C CB . ARG A 50 ? 0.6375 0.6118 0.6300 0.0278 0.0568 0.2918 50 ARG A CB 440 C CG . ARG A 50 ? 0.7248 0.7330 0.6714 0.0318 0.0694 0.3048 50 ARG A CG 441 C CD . ARG A 50 ? 0.8866 0.8889 0.8385 0.0183 0.0882 0.3324 50 ARG A CD 442 N NE . ARG A 50 ? 0.9305 0.9376 0.9347 -0.0040 0.1031 0.3325 50 ARG A NE 443 C CZ . ARG A 50 ? 0.9304 0.9794 0.9478 -0.0113 0.1243 0.3342 50 ARG A CZ 444 N NH1 . ARG A 50 ? 0.9455 1.0248 0.9179 0.0055 0.1382 0.3327 50 ARG A NH1 445 N NH2 . ARG A 50 ? 0.8992 0.9578 0.9738 -0.0353 0.1302 0.3354 50 ARG A NH2 446 N N . PHE A 51 ? 0.5466 0.4632 0.5936 0.0395 0.0308 0.2331 51 PHE A N 447 C CA . PHE A 51 ? 0.5855 0.4532 0.6515 0.0395 0.0290 0.2138 51 PHE A CA 448 C C . PHE A 51 ? 0.4894 0.3601 0.5591 0.0574 0.0200 0.1901 51 PHE A C 449 O O . PHE A 51 ? 0.5351 0.3737 0.6121 0.0640 0.0217 0.1767 51 PHE A O 450 C CB . PHE A 51 ? 0.5977 0.4378 0.6764 0.0164 0.0345 0.1989 51 PHE A CB 451 C CG . PHE A 51 ? 0.7724 0.6173 0.8597 -0.0080 0.0430 0.2219 51 PHE A CG 452 C CD1 . PHE A 51 ? 0.8304 0.6552 0.9098 -0.0098 0.0482 0.2443 51 PHE A CD1 453 C CD2 . PHE A 51 ? 0.7876 0.6628 0.8956 -0.0295 0.0463 0.2224 51 PHE A CD2 454 C CE1 . PHE A 51 ? 0.8818 0.7112 0.9704 -0.0337 0.0580 0.2651 51 PHE A CE1 455 C CE2 . PHE A 51 ? 0.8499 0.7412 0.9759 -0.0539 0.0554 0.2441 51 PHE A CE2 456 C CZ . PHE A 51 ? 0.8862 0.7520 1.0006 -0.0564 0.0619 0.2644 51 PHE A CZ 457 N N . ALA A 52 ? 0.4005 0.3102 0.4609 0.0649 0.0124 0.1850 52 ALA A N 458 C CA . ALA A 52 ? 0.3863 0.3002 0.4543 0.0760 0.0051 0.1597 52 ALA A CA 459 C C . ALA A 52 ? 0.3994 0.3591 0.4479 0.0815 -0.0106 0.1587 52 ALA A C 460 O O . ALA A 52 ? 0.3530 0.3372 0.3683 0.0761 -0.0130 0.1665 52 ALA A O 461 C CB . ALA A 52 ? 0.3382 0.2317 0.4059 0.0681 0.0118 0.1272 52 ALA A CB 462 N N . SER A 53 ? 0.3857 0.3535 0.4508 0.0900 -0.0200 0.1471 53 SER A N 463 C CA . SER A 53 ? 0.3350 0.3392 0.3798 0.0879 -0.0401 0.1411 53 SER A CA 464 C C . SER A 53 ? 0.2998 0.3008 0.3550 0.0866 -0.0393 0.1091 53 SER A C 465 O O . SER A 53 ? 0.3138 0.2885 0.3971 0.0925 -0.0245 0.0995 53 SER A O 466 C CB . SER A 53 ? 0.3582 0.3863 0.4216 0.0945 -0.0603 0.1707 53 SER A CB 467 O OG . SER A 53 ? 0.4146 0.4343 0.5261 0.1016 -0.0524 0.1661 53 SER A OG 468 N N . PHE A 54 ? 0.3230 0.3419 0.3466 0.0782 -0.0533 0.0921 54 PHE A N 469 C CA . PHE A 54 ? 0.3368 0.3524 0.3706 0.0746 -0.0551 0.0669 54 PHE A CA 470 C C . PHE A 54 ? 0.3687 0.4080 0.3813 0.0621 -0.0830 0.0647 54 PHE A C 471 O O . PHE A 54 ? 0.3692 0.4081 0.3230 0.0549 -0.0924 0.0591 54 PHE A O 472 C CB . PHE A 54 ? 0.2973 0.2872 0.3044 0.0735 -0.0371 0.0357 54 PHE A CB 473 C CG . PHE A 54 ? 0.2605 0.2392 0.2722 0.0703 -0.0363 0.0121 54 PHE A CG 474 C CD1 . PHE A 54 ? 0.3046 0.2702 0.3575 0.0764 -0.0246 0.0118 54 PHE A CD1 475 C CD2 . PHE A 54 ? 0.2993 0.2736 0.2690 0.0618 -0.0438 -0.0086 54 PHE A CD2 476 C CE1 . PHE A 54 ? 0.3395 0.2939 0.3964 0.0726 -0.0201 -0.0062 54 PHE A CE1 477 C CE2 . PHE A 54 ? 0.3505 0.3084 0.3237 0.0565 -0.0419 -0.0280 54 PHE A CE2 478 C CZ . PHE A 54 ? 0.2789 0.2302 0.2983 0.0612 -0.0301 -0.0253 54 PHE A CZ 479 N N . GLU A 55 ? 0.3498 0.4082 0.4094 0.0584 -0.0956 0.0704 55 GLU A N 480 C CA . GLU A 55 ? 0.3509 0.4308 0.3972 0.0387 -0.1277 0.0669 55 GLU A CA 481 C C . GLU A 55 ? 0.3526 0.3995 0.3510 0.0263 -0.1215 0.0283 55 GLU A C 482 O O . GLU A 55 ? 0.3610 0.3948 0.3888 0.0263 -0.1063 0.0139 55 GLU A O 483 C CB . GLU A 55 ? 0.3705 0.4896 0.4993 0.0370 -0.1408 0.0891 55 GLU A CB 484 C CG . GLU A 55 ? 0.4790 0.6259 0.6068 0.0090 -0.1801 0.0876 55 GLU A CG 485 C CD . GLU A 55 ? 0.6136 0.7641 0.6695 -0.0050 -0.2153 0.0921 55 GLU A CD 486 O OE1 . GLU A 55 ? 0.6644 0.8346 0.7241 0.0080 -0.2220 0.1219 55 GLU A OE1 487 O OE2 . GLU A 55 ? 0.6998 0.8233 0.6864 -0.0275 -0.2313 0.0641 55 GLU A OE2 488 N N . ALA A 56 ? 0.3062 0.3483 0.2973 0.0982 -0.0745 0.0898 56 ALA A N 489 C CA . ALA A 56 ? 0.3003 0.3385 0.2682 0.0861 -0.0778 0.0700 56 ALA A CA 490 C C . ALA A 56 ? 0.3737 0.4297 0.3490 0.0799 -0.0871 0.0614 56 ALA A C 491 O O . ALA A 56 ? 0.3574 0.4056 0.3244 0.0717 -0.0850 0.0446 56 ALA A O 492 C CB . ALA A 56 ? 0.3713 0.4105 0.3073 0.0809 -0.0843 0.0706 56 ALA A CB 493 N N . GLN A 57 ? 0.3875 0.4681 0.3798 0.0839 -0.0972 0.0740 57 GLN A N 494 C CA . GLN A 57 ? 0.4284 0.5291 0.4303 0.0774 -0.1070 0.0674 57 GLN A CA 495 C C . GLN A 57 ? 0.3871 0.4773 0.4056 0.0756 -0.0965 0.0543 57 GLN A C 496 O O . GLN A 57 ? 0.4352 0.5296 0.4494 0.0661 -0.1004 0.0413 57 GLN A O 497 C CB . GLN A 57 ? 0.5513 0.6822 0.5752 0.0837 -0.1184 0.0861 57 GLN A CB 498 C CG . GLN A 57 ? 0.6869 0.8434 0.7189 0.0750 -0.1313 0.0803 57 GLN A CG 499 C CD . GLN A 57 ? 0.7823 0.9409 0.7815 0.0606 -0.1414 0.0662 57 GLN A CD 500 O OE1 . GLN A 57 ? 0.8035 0.9554 0.7766 0.0574 -0.1446 0.0677 57 GLN A OE1 501 N NE2 . GLN A 57 ? 0.7771 0.9366 0.7779 0.0503 -0.1428 0.0501 57 GLN A NE2 502 N N . GLY A 58 ? 0.3616 0.4370 0.3978 0.0841 -0.0822 0.0572 58 GLY A N 503 C CA . GLY A 58 ? 0.3266 0.3919 0.3759 0.0822 -0.0709 0.0448 58 GLY A CA 504 C C . GLY A 58 ? 0.3441 0.3926 0.3702 0.0719 -0.0672 0.0268 58 GLY A C 505 O O . GLY A 58 ? 0.3363 0.3849 0.3679 0.0665 -0.0641 0.0163 58 GLY A O 506 N N . ALA A 59 ? 0.3295 0.3645 0.3309 0.0695 -0.0670 0.0244 59 ALA A N 507 C CA . ALA A 59 ? 0.3575 0.3786 0.3380 0.0606 -0.0643 0.0094 59 ALA A CA 508 C C . ALA A 59 ? 0.2975 0.3304 0.2702 0.0514 -0.0747 0.0015 59 ALA A C 509 O O . ALA A 59 ? 0.2450 0.2714 0.2153 0.0451 -0.0712 -0.0098 59 ALA A O 510 C CB . ALA A 59 ? 0.3155 0.3228 0.2735 0.0604 -0.0624 0.0100 59 ALA A CB 511 N N . LEU A 60 ? 0.4029 0.4529 0.3712 0.0502 -0.0872 0.0078 60 LEU A N 512 C CA . LEU A 60 ? 0.3959 0.4571 0.3565 0.0401 -0.0973 -0.0006 60 LEU A CA 513 C C . LEU A 60 ? 0.3467 0.4172 0.3298 0.0371 -0.0967 -0.0046 60 LEU A C 514 O O . LEU A 60 ? 0.3415 0.4084 0.3198 0.0283 -0.0969 -0.0161 60 LEU A O 515 C CB . LEU A 60 ? 0.4459 0.5276 0.3988 0.0386 -0.1116 0.0075 60 LEU A CB 516 C CG . LEU A 60 ? 0.5314 0.6062 0.4542 0.0365 -0.1143 0.0070 60 LEU A CG 517 C CD1 . LEU A 60 ? 0.5624 0.6228 0.4818 0.0461 -0.1050 0.0165 60 LEU A CD1 518 C CD2 . LEU A 60 ? 0.5761 0.6751 0.4902 0.0327 -0.1296 0.0134 60 LEU A CD2 519 N N . ALA A 61 ? 0.2334 0.3148 0.2422 0.0449 -0.0945 0.0054 61 ALA A N 520 C CA . ALA A 61 ? 0.2726 0.3638 0.3055 0.0432 -0.0917 0.0028 61 ALA A CA 521 C C . ALA A 61 ? 0.3088 0.3805 0.3380 0.0399 -0.0790 -0.0089 61 ALA A C 522 O O . ALA A 61 ? 0.2710 0.3456 0.3040 0.0322 -0.0792 -0.0167 61 ALA A O 523 C CB . ALA A 61 ? 0.2578 0.3618 0.3199 0.0540 -0.0886 0.0160 61 ALA A CB 524 N N . ASN A 62 ? 0.2468 0.2997 0.2691 0.0451 -0.0682 -0.0095 62 ASN A N 525 C CA . ASN A 62 ? 0.2787 0.3151 0.2946 0.0414 -0.0574 -0.0198 62 ASN A CA 526 C C . ASN A 62 ? 0.2260 0.2548 0.2217 0.0322 -0.0609 -0.0292 62 ASN A C 527 O O . ASN A 62 ? 0.2051 0.2304 0.2021 0.0268 -0.0565 -0.0359 62 ASN A O 528 C CB . ASN A 62 ? 0.1949 0.2139 0.2051 0.0470 -0.0467 -0.0193 62 ASN A CB 529 C CG . ASN A 62 ? 0.2874 0.3064 0.3195 0.0535 -0.0355 -0.0167 62 ASN A CG 530 O OD1 . ASN A 62 ? 0.2434 0.2779 0.2975 0.0567 -0.0368 -0.0115 62 ASN A OD1 531 N ND2 . ASN A 62 ? 0.2534 0.2556 0.2806 0.0549 -0.0239 -0.0211 62 ASN A ND2 532 N N . ILE A 63 ? 0.2233 0.2488 0.2006 0.0307 -0.0678 -0.0292 63 ILE A N 533 C CA . ILE A 63 ? 0.2646 0.2809 0.2239 0.0231 -0.0695 -0.0382 63 ILE A CA 534 C C . ILE A 63 ? 0.2081 0.2349 0.1746 0.0150 -0.0757 -0.0430 63 ILE A C 535 O O . ILE A 63 ? 0.2601 0.2783 0.2222 0.0090 -0.0726 -0.0503 63 ILE A O 536 C CB . ILE A 63 ? 0.3250 0.3362 0.2630 0.0234 -0.0742 -0.0378 63 ILE A CB 537 C CG1 . ILE A 63 ? 0.3448 0.3400 0.2723 0.0279 -0.0656 -0.0370 63 ILE A CG1 538 C CG2 . ILE A 63 ? 0.3309 0.3386 0.2549 0.0148 -0.0785 -0.0472 63 ILE A CG2 539 C CD1 . ILE A 63 ? 0.3719 0.3599 0.3099 0.0306 -0.0554 -0.0375 63 ILE A CD1 540 N N . ALA A 64 ? 0.2050 0.2510 0.1846 0.0147 -0.0842 -0.0380 64 ALA A N 541 C CA . ALA A 64 ? 0.2389 0.2971 0.2292 0.0060 -0.0900 -0.0424 64 ALA A CA 542 C C . ALA A 64 ? 0.2820 0.3379 0.2885 0.0046 -0.0808 -0.0445 64 ALA A C 543 O O . ALA A 64 ? 0.3087 0.3620 0.3162 -0.0037 -0.0803 -0.0511 64 ALA A O 544 C CB . ALA A 64 ? 0.2229 0.3064 0.2274 0.0064 -0.1013 -0.0349 64 ALA A CB 545 N N . VAL A 65 ? 0.2507 0.3071 0.2697 0.0125 -0.0725 -0.0390 65 VAL A N 546 C CA . VAL A 65 ? 0.1825 0.2368 0.2137 0.0111 -0.0623 -0.0412 65 VAL A CA 547 C C . VAL A 65 ? 0.2193 0.2542 0.2322 0.0072 -0.0559 -0.0478 65 VAL A C 548 O O . VAL A 65 ? 0.1926 0.2258 0.2088 0.0009 -0.0525 -0.0511 65 VAL A O 549 C CB . VAL A 65 ? 0.1790 0.2360 0.2254 0.0202 -0.0530 -0.0358 65 VAL A CB 550 C CG1 . VAL A 65 ? 0.1971 0.2486 0.2482 0.0180 -0.0406 -0.0399 65 VAL A CG1 551 C CG2 . VAL A 65 ? 0.1812 0.2604 0.2528 0.0246 -0.0583 -0.0274 65 VAL A CG2 552 N N . ASP A 66 ? 0.2179 0.2395 0.2130 0.0108 -0.0544 -0.0484 66 ASP A N 553 C CA . ASP A 66 ? 0.2454 0.2512 0.2250 0.0081 -0.0491 -0.0529 66 ASP A CA 554 C C . ASP A 66 ? 0.2393 0.2412 0.2134 0.0005 -0.0532 -0.0576 66 ASP A C 555 O O . ASP A 66 ? 0.2096 0.2043 0.1821 -0.0031 -0.0479 -0.0592 66 ASP A O 556 C CB . ASP A 66 ? 0.2274 0.2223 0.1910 0.0129 -0.0480 -0.0524 66 ASP A CB 557 C CG . ASP A 66 ? 0.2165 0.2108 0.1855 0.0195 -0.0416 -0.0489 66 ASP A CG 558 O OD1 . ASP A 66 ? 0.2350 0.2343 0.2172 0.0201 -0.0354 -0.0486 66 ASP A OD1 559 O OD2 . ASP A 66 ? 0.2392 0.2271 0.1992 0.0236 -0.0415 -0.0470 66 ASP A OD2 560 N N . LYS A 67 ? 0.2353 0.2421 0.2066 -0.0024 -0.0621 -0.0596 67 LYS A N 561 C CA . LYS A 67 ? 0.2532 0.2550 0.2202 -0.0107 -0.0652 -0.0661 67 LYS A CA 562 C C . LYS A 67 ? 0.3052 0.3134 0.2897 -0.0173 -0.0634 -0.0668 67 LYS A C 563 O O . LYS A 67 ? 0.2592 0.2569 0.2428 -0.0223 -0.0589 -0.0697 67 LYS A O 564 C CB . LYS A 67 ? 0.3121 0.3202 0.2711 -0.0138 -0.0754 -0.0694 67 LYS A CB 565 C CG . LYS A 67 ? 0.3081 0.3139 0.2658 -0.0245 -0.0793 -0.0784 67 LYS A CG 566 C CD . LYS A 67 ? 0.3527 0.3675 0.3001 -0.0286 -0.0877 -0.0799 67 LYS A CD 567 C CE . LYS A 67 ? 0.4424 0.4581 0.3912 -0.0415 -0.0901 -0.0870 67 LYS A CE 568 N NZ . LYS A 67 ? 0.4882 0.4822 0.4210 -0.0458 -0.0817 -0.0927 67 LYS A NZ 569 N N . ALA A 68 ? 0.2479 0.2738 0.2501 -0.0170 -0.0661 -0.0630 68 ALA A N 570 C CA . ALA A 68 ? 0.2589 0.2926 0.2797 -0.0231 -0.0631 -0.0627 68 ALA A CA 571 C C . ALA A 68 ? 0.2461 0.2704 0.2669 -0.0214 -0.0513 -0.0602 68 ALA A C 572 O O . ALA A 68 ? 0.2248 0.2447 0.2504 -0.0277 -0.0471 -0.0610 68 ALA A O 573 C CB . ALA A 68 ? 0.3138 0.3703 0.3562 -0.0214 -0.0670 -0.0578 68 ALA A CB 574 N N . ASN A 69 ? 0.2042 0.2255 0.2190 -0.0134 -0.0459 -0.0570 69 ASN A N 575 C CA . ASN A 69 ? 0.2092 0.2237 0.2204 -0.0127 -0.0355 -0.0552 69 ASN A CA 576 C C . ASN A 69 ? 0.2107 0.2099 0.2074 -0.0155 -0.0339 -0.0562 69 ASN A C 577 O O . ASN A 69 ? 0.2442 0.2405 0.2420 -0.0186 -0.0275 -0.0535 69 ASN A O 578 C CB . ASN A 69 ? 0.2418 0.2560 0.2488 -0.0052 -0.0300 -0.0536 69 ASN A CB 579 C CG . ASN A 69 ? 0.2846 0.3128 0.3105 -0.0019 -0.0266 -0.0514 69 ASN A CG 580 O OD1 . ASN A 69 ? 0.3091 0.3496 0.3523 -0.0055 -0.0280 -0.0502 69 ASN A OD1 581 N ND2 . ASN A 69 ? 0.1872 0.2136 0.2118 0.0048 -0.0213 -0.0510 69 ASN A ND2 582 N N . LEU A 70 ? 0.1999 0.1899 0.1838 -0.0141 -0.0390 -0.0591 70 LEU A N 583 C CA . LEU A 70 ? 0.2316 0.2073 0.2051 -0.0156 -0.0367 -0.0595 70 LEU A CA 584 C C . LEU A 70 ? 0.2658 0.2381 0.2489 -0.0232 -0.0356 -0.0603 70 LEU A C 585 O O . LEU A 70 ? 0.2830 0.2471 0.2653 -0.0245 -0.0298 -0.0564 70 LEU A O 586 C CB . LEU A 70 ? 0.2267 0.1939 0.1868 -0.0130 -0.0413 -0.0635 70 LEU A CB 587 C CG . LEU A 70 ? 0.2843 0.2366 0.2364 -0.0134 -0.0379 -0.0640 70 LEU A CG 588 C CD1 . LEU A 70 ? 0.2525 0.2031 0.2027 -0.0106 -0.0314 -0.0570 70 LEU A CD1 589 C CD2 . LEU A 70 ? 0.3060 0.2511 0.2447 -0.0103 -0.0408 -0.0683 70 LEU A CD2 590 N N A GLU A 71 ? 0.2067 0.1858 0.1995 -0.0287 -0.0411 -0.0648 71 GLU A N 591 N N B GLU A 71 ? 0.2135 0.1926 0.2063 -0.0287 -0.0411 -0.0648 71 GLU A N 592 C CA A GLU A 71 ? 0.2571 0.2334 0.2615 -0.0376 -0.0399 -0.0668 71 GLU A CA 593 C CA B GLU A 71 ? 0.2494 0.2251 0.2534 -0.0376 -0.0398 -0.0669 71 GLU A CA 594 C C A GLU A 71 ? 0.2463 0.2265 0.2618 -0.0393 -0.0319 -0.0596 71 GLU A C 595 C C B GLU A 71 ? 0.2460 0.2266 0.2623 -0.0397 -0.0321 -0.0598 71 GLU A C 596 O O A GLU A 71 ? 0.2537 0.2235 0.2717 -0.0429 -0.0262 -0.0564 71 GLU A O 597 O O B GLU A 71 ? 0.2516 0.2225 0.2720 -0.0441 -0.0266 -0.0571 71 GLU A O 598 C CB A GLU A 71 ? 0.3257 0.3153 0.3412 -0.0441 -0.0481 -0.0723 71 GLU A CB 599 C CB B GLU A 71 ? 0.3138 0.3004 0.3267 -0.0444 -0.0484 -0.0735 71 GLU A CB 600 C CG A GLU A 71 ? 0.3712 0.3590 0.3749 -0.0453 -0.0568 -0.0800 71 GLU A CG 601 C CG B GLU A 71 ? 0.3573 0.3435 0.3859 -0.0554 -0.0470 -0.0762 71 GLU A CG 602 C CD A GLU A 71 ? 0.4998 0.5048 0.5151 -0.0532 -0.0662 -0.0846 71 GLU A CD 603 C CD B GLU A 71 ? 0.3931 0.3570 0.4162 -0.0596 -0.0420 -0.0800 71 GLU A CD 604 O OE1 A GLU A 71 ? 0.4878 0.4971 0.5195 -0.0620 -0.0650 -0.0859 71 GLU A OE1 605 O OE1 B GLU A 71 ? 0.4007 0.3521 0.4078 -0.0557 -0.0425 -0.0839 71 GLU A OE1 606 O OE2 A GLU A 71 ? 0.5184 0.5341 0.5270 -0.0509 -0.0749 -0.0858 71 GLU A OE2 607 O OE2 B GLU A 71 ? 0.4080 0.3667 0.4442 -0.0667 -0.0364 -0.0785 71 GLU A OE2 608 N N . ILE A 72 ? 0.2154 0.2104 0.2378 -0.0364 -0.0306 -0.0564 72 ILE A N 609 C CA . ILE A 72 ? 0.3023 0.3035 0.3337 -0.0379 -0.0220 -0.0502 72 ILE A CA 610 C C . ILE A 72 ? 0.2728 0.2637 0.2906 -0.0351 -0.0151 -0.0442 72 ILE A C 611 O O . ILE A 72 ? 0.2627 0.2507 0.2849 -0.0393 -0.0090 -0.0384 72 ILE A O 612 C CB . ILE A 72 ? 0.3426 0.3601 0.3822 -0.0337 -0.0201 -0.0492 72 ILE A CB 613 C CG1 . ILE A 72 ? 0.3414 0.3740 0.4007 -0.0374 -0.0263 -0.0517 72 ILE A CG1 614 C CG2 . ILE A 72 ? 0.3480 0.3700 0.3903 -0.0343 -0.0091 -0.0437 72 ILE A CG2 615 C CD1 . ILE A 72 ? 0.4015 0.4496 0.4711 -0.0310 -0.0257 -0.0502 72 ILE A CD1 616 N N . MET A 73 ? 0.2547 0.2416 0.2571 -0.0285 -0.0164 -0.0448 73 MET A N 617 C CA . MET A 73 ? 0.2188 0.2008 0.2086 -0.0261 -0.0112 -0.0388 73 MET A CA 618 C C . MET A 73 ? 0.2449 0.2135 0.2324 -0.0274 -0.0110 -0.0349 73 MET A C 619 O O . MET A 73 ? 0.2946 0.2617 0.2796 -0.0281 -0.0059 -0.0263 73 MET A O 620 C CB . MET A 73 ? 0.2667 0.2489 0.2427 -0.0198 -0.0128 -0.0412 73 MET A CB 621 C CG . MET A 73 ? 0.2364 0.2292 0.2158 -0.0175 -0.0107 -0.0445 73 MET A CG 622 S SD . MET A 73 ? 0.2995 0.3039 0.2868 -0.0214 -0.0007 -0.0412 73 MET A SD 623 C CE . MET A 73 ? 0.1929 0.1945 0.1626 -0.0232 0.0040 -0.0346 73 MET A CE 624 N N . THR A 74 ? 0.2272 0.1864 0.2153 -0.0277 -0.0160 -0.0410 74 THR A N 625 C CA . THR A 74 ? 0.2783 0.2223 0.2672 -0.0289 -0.0142 -0.0392 74 THR A CA 626 C C . THR A 74 ? 0.2804 0.2218 0.2826 -0.0351 -0.0082 -0.0328 74 THR A C 627 O O . THR A 74 ? 0.2324 0.1657 0.2348 -0.0339 -0.0031 -0.0237 74 THR A O 628 C CB . THR A 74 ? 0.2492 0.1839 0.2367 -0.0302 -0.0194 -0.0498 74 THR A CB 629 O OG1 . THR A 74 ? 0.2717 0.2077 0.2457 -0.0239 -0.0235 -0.0532 74 THR A OG1 630 C CG2 . THR A 74 ? 0.2434 0.1599 0.2344 -0.0320 -0.0150 -0.0495 74 THR A CG2 631 N N . LYS A 75 ? 0.2785 0.2280 0.2931 -0.0414 -0.0087 -0.0362 75 LYS A N 632 C CA A LYS A 75 ? 0.2888 0.2368 0.3178 -0.0484 -0.0023 -0.0302 75 LYS A CA 633 C CA B LYS A 75 ? 0.2862 0.2346 0.3154 -0.0485 -0.0023 -0.0302 75 LYS A CA 634 C C . LYS A 75 ? 0.2649 0.2214 0.2911 -0.0468 0.0046 -0.0179 75 LYS A C 635 O O . LYS A 75 ? 0.2955 0.2459 0.3270 -0.0493 0.0111 -0.0078 75 LYS A O 636 C CB A LYS A 75 ? 0.3170 0.2750 0.3618 -0.0563 -0.0050 -0.0370 75 LYS A CB 637 C CB B LYS A 75 ? 0.3244 0.2839 0.3690 -0.0559 -0.0048 -0.0367 75 LYS A CB 638 C CG A LYS A 75 ? 0.3066 0.2612 0.3526 -0.0597 -0.0134 -0.0497 75 LYS A CG 639 C CG B LYS A 75 ? 0.3363 0.2885 0.3873 -0.0623 -0.0107 -0.0478 75 LYS A CG 640 C CD A LYS A 75 ? 0.3168 0.2861 0.3804 -0.0682 -0.0172 -0.0550 75 LYS A CD 641 C CD B LYS A 75 ? 0.3244 0.2936 0.3919 -0.0698 -0.0148 -0.0529 75 LYS A CD 642 C CE A LYS A 75 ? 0.2892 0.2597 0.3507 -0.0722 -0.0275 -0.0674 75 LYS A CE 643 C CE B LYS A 75 ? 0.3005 0.2778 0.3839 -0.0747 -0.0064 -0.0442 75 LYS A CE 644 N NZ A LYS A 75 ? 0.3138 0.3012 0.3943 -0.0818 -0.0326 -0.0720 75 LYS A NZ 645 N NZ B LYS A 75 ? 0.3700 0.3659 0.4732 -0.0821 -0.0100 -0.0485 75 LYS A NZ 646 N N . ARG A 76 ? 0.2506 0.2209 0.2684 -0.0430 0.0040 -0.0187 76 ARG A N 647 C CA . ARG A 76 ? 0.2804 0.2601 0.2918 -0.0426 0.0108 -0.0094 76 ARG A CA 648 C C . ARG A 76 ? 0.2309 0.2037 0.2307 -0.0392 0.0121 0.0007 76 ARG A C 649 O O . ARG A 76 ? 0.3071 0.2835 0.3055 -0.0411 0.0181 0.0124 76 ARG A O 650 C CB . ARG A 76 ? 0.2182 0.2111 0.2211 -0.0392 0.0107 -0.0147 76 ARG A CB 651 C CG . ARG A 76 ? 0.3442 0.3501 0.3608 -0.0425 0.0148 -0.0180 76 ARG A CG 652 C CD . ARG A 76 ? 0.3148 0.3313 0.3234 -0.0387 0.0183 -0.0222 76 ARG A CD 653 N NE . ARG A 76 ? 0.3170 0.3424 0.3412 -0.0376 0.0172 -0.0291 76 ARG A NE 654 C CZ . ARG A 76 ? 0.3669 0.3983 0.3893 -0.0326 0.0189 -0.0345 76 ARG A CZ 655 N NH1 . ARG A 76 ? 0.3219 0.3506 0.3261 -0.0296 0.0219 -0.0360 76 ARG A NH1 656 N NH2 . ARG A 76 ? 0.3914 0.4320 0.4318 -0.0308 0.0177 -0.0383 76 ARG A NH2 657 N N . SER A 77 ? 0.2277 0.1920 0.2199 -0.0339 0.0066 -0.0029 77 SER A N 658 C CA . SER A 77 ? 0.2352 0.1952 0.2187 -0.0294 0.0068 0.0068 77 SER A CA 659 C C . SER A 77 ? 0.2962 0.2418 0.2912 -0.0301 0.0104 0.0155 77 SER A C 660 O O . SER A 77 ? 0.2768 0.2184 0.2689 -0.0253 0.0111 0.0255 77 SER A O 661 C CB . SER A 77 ? 0.2721 0.2285 0.2461 -0.0234 0.0007 -0.0004 77 SER A CB 662 O OG . SER A 77 ? 0.2924 0.2334 0.2735 -0.0225 -0.0012 -0.0063 77 SER A OG 663 N N . ASN A 78 ? 0.2710 0.2090 0.2808 -0.0360 0.0132 0.0119 78 ASN A N 664 C CA . ASN A 78 ? 0.2656 0.1853 0.2887 -0.0376 0.0176 0.0164 78 ASN A CA 665 C C . ASN A 78 ? 0.2923 0.1975 0.3129 -0.0321 0.0147 0.0098 78 ASN A C 666 O O . ASN A 78 ? 0.3142 0.2069 0.3401 -0.0282 0.0190 0.0186 78 ASN A O 667 C CB . ASN A 78 ? 0.2776 0.1975 0.3040 -0.0367 0.0244 0.0361 78 ASN A CB 668 C CG . ASN A 78 ? 0.3704 0.3044 0.3980 -0.0427 0.0289 0.0427 78 ASN A CG 669 O OD1 . ASN A 78 ? 0.4121 0.3479 0.4496 -0.0495 0.0301 0.0345 78 ASN A OD1 670 N ND2 . ASN A 78 ? 0.4968 0.4430 0.5143 -0.0406 0.0314 0.0577 78 ASN A ND2 671 N N . TYR A 79 ? 0.2938 0.2009 0.3069 -0.0315 0.0081 -0.0049 79 TYR A N 672 C CA . TYR A 79 ? 0.2896 0.1842 0.2983 -0.0270 0.0059 -0.0129 79 TYR A CA 673 C C . TYR A 79 ? 0.3701 0.2644 0.3723 -0.0180 0.0070 -0.0027 79 TYR A C 674 O O . TYR A 79 ? 0.3681 0.2478 0.3748 -0.0139 0.0104 -0.0023 79 TYR A O 675 C CB . TYR A 79 ? 0.3301 0.2045 0.3511 -0.0321 0.0102 -0.0199 79 TYR A CB 676 C CG . TYR A 79 ? 0.3332 0.2112 0.3599 -0.0420 0.0068 -0.0320 79 TYR A CG 677 C CD1 . TYR A 79 ? 0.2991 0.1766 0.3193 -0.0446 0.0003 -0.0479 79 TYR A CD1 678 C CD2 . TYR A 79 ? 0.2929 0.1776 0.3317 -0.0489 0.0097 -0.0266 79 TYR A CD2 679 C CE1 . TYR A 79 ? 0.3169 0.2019 0.3434 -0.0539 -0.0043 -0.0577 79 TYR A CE1 680 C CE2 . TYR A 79 ? 0.3393 0.2307 0.3861 -0.0582 0.0061 -0.0370 79 TYR A CE2 681 C CZ . TYR A 79 ? 0.3494 0.2416 0.3903 -0.0606 -0.0016 -0.0523 79 TYR A CZ 682 O OH . TYR A 79 ? 0.4268 0.3293 0.4768 -0.0700 -0.0067 -0.0613 79 TYR A OH 683 N N . THR A 80 ? 0.2960 0.2073 0.2884 -0.0153 0.0044 0.0048 80 THR A N 684 C CA . THR A 80 ? 0.2884 0.2045 0.2743 -0.0080 0.0034 0.0135 80 THR A CA 685 C C . THR A 80 ? 0.3017 0.2170 0.2782 -0.0043 -0.0014 0.0016 80 THR A C 686 O O . THR A 80 ? 0.2872 0.2115 0.2546 -0.0062 -0.0059 -0.0071 80 THR A O 687 C CB . THR A 80 ? 0.3179 0.2540 0.2942 -0.0087 0.0018 0.0235 80 THR A CB 688 O OG1 . THR A 80 ? 0.3467 0.2851 0.3300 -0.0126 0.0068 0.0352 80 THR A OG1 689 C CG2 . THR A 80 ? 0.2428 0.1871 0.2136 -0.0025 -0.0005 0.0329 80 THR A CG2 690 N N . PRO A 81 ? 0.2509 0.1549 0.2307 0.0012 0.0007 0.0015 81 PRO A N 691 C CA . PRO A 81 ? 0.2847 0.1869 0.2556 0.0045 -0.0025 -0.0093 81 PRO A CA 692 C C . PRO A 81 ? 0.3214 0.2388 0.2833 0.0086 -0.0062 -0.0040 81 PRO A C 693 O O . PRO A 81 ? 0.2715 0.2007 0.2342 0.0094 -0.0064 0.0086 81 PRO A O 694 C CB . PRO A 81 ? 0.2879 0.1720 0.2678 0.0087 0.0036 -0.0103 81 PRO A CB 695 C CG . PRO A 81 ? 0.3727 0.2552 0.3658 0.0115 0.0088 0.0065 81 PRO A CG 696 C CD . PRO A 81 ? 0.2552 0.1465 0.2489 0.0049 0.0075 0.0120 81 PRO A CD 697 N N . ILE A 82 ? 0.2624 0.1805 0.2155 0.0105 -0.0092 -0.0134 82 ILE A N 698 C CA . ILE A 82 ? 0.3092 0.2403 0.2552 0.0133 -0.0121 -0.0099 82 ILE A CA 699 C C . ILE A 82 ? 0.3107 0.2411 0.2650 0.0197 -0.0091 0.0001 82 ILE A C 700 O O . ILE A 82 ? 0.3096 0.2255 0.2726 0.0232 -0.0039 -0.0008 82 ILE A O 701 C CB . ILE A 82 ? 0.2141 0.1447 0.1497 0.0135 -0.0151 -0.0218 82 ILE A CB 702 C CG1 . ILE A 82 ? 0.2379 0.1826 0.1662 0.0136 -0.0180 -0.0196 82 ILE A CG1 703 C CG2 . ILE A 82 ? 0.2893 0.2065 0.2258 0.0172 -0.0122 -0.0280 82 ILE A CG2 704 C CD1 . ILE A 82 ? 0.2762 0.2207 0.1954 0.0127 -0.0204 -0.0299 82 ILE A CD1 705 N N . THR A 83 ? 0.2504 0.1973 0.2032 0.0207 -0.0119 0.0095 83 THR A N 706 C CA . THR A 83 ? 0.3029 0.2542 0.2655 0.0272 -0.0102 0.0199 83 THR A CA 707 C C . THR A 83 ? 0.2698 0.2229 0.2274 0.0295 -0.0111 0.0121 83 THR A C 708 O O . THR A 83 ? 0.2666 0.2288 0.2129 0.0253 -0.0154 0.0061 83 THR A O 709 C CB . THR A 83 ? 0.3606 0.3328 0.3248 0.0262 -0.0140 0.0357 83 THR A CB 710 O OG1 . THR A 83 ? 0.3228 0.2928 0.2919 0.0246 -0.0120 0.0449 83 THR A OG1 711 C CG2 . THR A 83 ? 0.3466 0.3278 0.3235 0.0333 -0.0135 0.0480 83 THR A CG2 712 N N . ASN A 84 ? 0.2468 0.1900 0.2133 0.0359 -0.0057 0.0118 84 ASN A N 713 C CA . ASN A 84 ? 0.3009 0.2452 0.2634 0.0382 -0.0050 0.0049 84 ASN A CA 714 C C . ASN A 84 ? 0.3272 0.2934 0.2918 0.0380 -0.0094 0.0137 84 ASN A C 715 O O . ASN A 84 ? 0.2529 0.2310 0.2291 0.0407 -0.0103 0.0280 84 ASN A O 716 C CB . ASN A 84 ? 0.3183 0.2479 0.2908 0.0453 0.0037 0.0031 84 ASN A CB 717 C CG . ASN A 84 ? 0.3254 0.2332 0.2937 0.0436 0.0082 -0.0088 84 ASN A CG 718 O OD1 . ASN A 84 ? 0.3058 0.2105 0.2605 0.0378 0.0042 -0.0195 84 ASN A OD1 719 N ND2 . ASN A 84 ? 0.2635 0.1567 0.2448 0.0483 0.0167 -0.0070 84 ASN A ND2 720 N N . VAL A 85 ? 0.2269 0.1989 0.1807 0.0343 -0.0125 0.0058 85 VAL A N 721 C CA . VAL A 85 ? 0.2450 0.2366 0.2005 0.0324 -0.0162 0.0111 85 VAL A CA 722 C C . VAL A 85 ? 0.2773 0.2644 0.2340 0.0357 -0.0120 0.0052 85 VAL A C 723 O O . VAL A 85 ? 0.2551 0.2330 0.1999 0.0333 -0.0113 -0.0059 85 VAL A O 724 C CB . VAL A 85 ? 0.3043 0.3059 0.2463 0.0234 -0.0221 0.0061 85 VAL A CB 725 C CG1 . VAL A 85 ? 0.2289 0.2510 0.1725 0.0193 -0.0261 0.0099 85 VAL A CG1 726 C CG2 . VAL A 85 ? 0.2244 0.2293 0.1630 0.0197 -0.0247 0.0106 85 VAL A CG2 727 N N . PRO A 86 ? 0.2653 0.2592 0.2373 0.0418 -0.0084 0.0136 86 PRO A N 728 C CA . PRO A 86 ? 0.2467 0.2369 0.2213 0.0455 -0.0025 0.0089 86 PRO A CA 729 C C . PRO A 86 ? 0.2335 0.2358 0.2013 0.0391 -0.0063 0.0052 86 PRO A C 730 O O . PRO A 86 ? 0.2001 0.2192 0.1676 0.0329 -0.0132 0.0094 86 PRO A O 731 C CB . PRO A 86 ? 0.2448 0.2448 0.2420 0.0534 0.0016 0.0220 86 PRO A CB 732 C CG . PRO A 86 ? 0.2838 0.3029 0.2877 0.0509 -0.0063 0.0352 86 PRO A CG 733 C CD . PRO A 86 ? 0.3093 0.3169 0.2985 0.0459 -0.0095 0.0297 86 PRO A CD 734 N N . PRO A 87 ? 0.2835 0.2772 0.2456 0.0399 -0.0013 -0.0028 87 PRO A N 735 C CA . PRO A 87 ? 0.2217 0.2238 0.1782 0.0335 -0.0035 -0.0064 87 PRO A CA 736 C C . PRO A 87 ? 0.2269 0.2492 0.1990 0.0330 -0.0032 0.0014 87 PRO A C 737 O O . PRO A 87 ? 0.2176 0.2455 0.2058 0.0400 0.0011 0.0092 87 PRO A O 738 C CB . PRO A 87 ? 0.2171 0.2024 0.1627 0.0356 0.0028 -0.0154 87 PRO A CB 739 C CG . PRO A 87 ? 0.2387 0.2136 0.1904 0.0440 0.0103 -0.0148 87 PRO A CG 740 C CD . PRO A 87 ? 0.1937 0.1687 0.1524 0.0458 0.0072 -0.0094 87 PRO A CD 741 N N . GLU A 88 ? 0.2519 0.2848 0.2203 0.0244 -0.0073 -0.0012 88 GLU A N 742 C CA . GLU A 88 ? 0.2041 0.2544 0.1853 0.0215 -0.0064 0.0030 88 GLU A CA 743 C C . GLU A 88 ? 0.2333 0.2696 0.2080 0.0225 0.0014 -0.0042 88 GLU A C 744 O O . GLU A 88 ? 0.2648 0.2851 0.2233 0.0201 0.0019 -0.0124 88 GLU A O 745 C CB . GLU A 88 ? 0.2079 0.2745 0.1864 0.0096 -0.0142 0.0015 88 GLU A CB 746 C CG . GLU A 88 ? 0.4431 0.5270 0.4246 0.0067 -0.0228 0.0089 88 GLU A CG 747 C CD . GLU A 88 ? 0.5829 0.6852 0.5605 -0.0069 -0.0299 0.0058 88 GLU A CD 748 O OE1 . GLU A 88 ? 0.5896 0.6888 0.5639 -0.0140 -0.0274 -0.0026 88 GLU A OE1 749 O OE2 . GLU A 88 ? 0.5947 0.7142 0.5718 -0.0112 -0.0375 0.0117 88 GLU A OE2 750 N N . VAL A 89 ? 0.1826 0.2253 0.1704 0.0264 0.0080 -0.0001 89 VAL A N 751 C CA . VAL A 89 ? 0.2104 0.2403 0.1905 0.0273 0.0164 -0.0058 89 VAL A CA 752 C C . VAL A 89 ? 0.2150 0.2611 0.2082 0.0217 0.0188 -0.0027 89 VAL A C 753 O O . VAL A 89 ? 0.1936 0.2599 0.2071 0.0229 0.0185 0.0055 89 VAL A O 754 C CB . VAL A 89 ? 0.1927 0.2092 0.1722 0.0377 0.0259 -0.0064 89 VAL A CB 755 C CG1 . VAL A 89 ? 0.2396 0.2465 0.2105 0.0381 0.0352 -0.0108 89 VAL A CG1 756 C CG2 . VAL A 89 ? 0.2070 0.2060 0.1724 0.0409 0.0235 -0.0115 89 VAL A CG2 757 N N . THR A 90 ? 0.2209 0.2589 0.2042 0.0155 0.0210 -0.0083 90 THR A N 758 C CA A THR A 90 ? 0.2212 0.2717 0.2164 0.0090 0.0247 -0.0063 90 THR A CA 759 C CA B THR A 90 ? 0.2209 0.2715 0.2166 0.0094 0.0249 -0.0061 90 THR A CA 760 C C . THR A 90 ? 0.2150 0.2495 0.2011 0.0114 0.0352 -0.0088 90 THR A C 761 O O . THR A 90 ? 0.2568 0.2718 0.2238 0.0125 0.0358 -0.0138 90 THR A O 762 C CB A THR A 90 ? 0.1905 0.2476 0.1842 -0.0041 0.0177 -0.0106 90 THR A CB 763 C CB B THR A 90 ? 0.1998 0.2600 0.1964 -0.0038 0.0176 -0.0094 90 THR A CB 764 O OG1 A THR A 90 ? 0.1846 0.2536 0.1794 -0.0068 0.0075 -0.0095 90 THR A OG1 765 O OG1 B THR A 90 ? 0.2368 0.2782 0.2140 -0.0063 0.0150 -0.0171 90 THR A OG1 766 C CG2 A THR A 90 ? 0.2007 0.2754 0.2114 -0.0127 0.0201 -0.0081 90 THR A CG2 767 C CG2 B THR A 90 ? 0.1816 0.2662 0.1908 -0.0075 0.0080 -0.0044 90 THR A CG2 768 N N . VAL A 91 ? 0.2017 0.2462 0.2020 0.0124 0.0435 -0.0041 91 VAL A N 769 C CA . VAL A 91 ? 0.2121 0.2443 0.2041 0.0133 0.0543 -0.0050 91 VAL A CA 770 C C . VAL A 91 ? 0.3342 0.3768 0.3382 0.0025 0.0561 -0.0034 91 VAL A C 771 O O . VAL A 91 ? 0.2790 0.3441 0.3047 -0.0022 0.0542 0.0006 91 VAL A O 772 C CB . VAL A 91 ? 0.2493 0.2819 0.2463 0.0232 0.0657 -0.0018 91 VAL A CB 773 C CG1 . VAL A 91 ? 0.2780 0.3034 0.2685 0.0222 0.0776 -0.0010 91 VAL A CG1 774 C CG2 . VAL A 91 ? 0.2223 0.2395 0.2040 0.0321 0.0656 -0.0059 91 VAL A CG2 775 N N . LEU A 92 ? 0.3169 0.3436 0.3078 -0.0021 0.0592 -0.0063 92 LEU A N 776 C CA . LEU A 92 ? 0.3431 0.3751 0.3450 -0.0130 0.0629 -0.0055 92 LEU A CA 777 C C . LEU A 92 ? 0.3258 0.3385 0.3142 -0.0117 0.0730 -0.0038 92 LEU A C 778 O O . LEU A 92 ? 0.3093 0.3065 0.2783 -0.0031 0.0749 -0.0038 92 LEU A O 779 C CB . LEU A 92 ? 0.3097 0.3448 0.3138 -0.0245 0.0534 -0.0114 92 LEU A CB 780 C CG . LEU A 92 ? 0.4663 0.4826 0.4523 -0.0257 0.0477 -0.0181 92 LEU A CG 781 C CD1 . LEU A 92 ? 0.4075 0.4173 0.3796 -0.0155 0.0416 -0.0191 92 LEU A CD1 782 C CD2 . LEU A 92 ? 0.5955 0.5900 0.5714 -0.0266 0.0555 -0.0181 92 LEU A CD2 783 N N . THR A 93 ? 0.3362 0.3508 0.3352 -0.0205 0.0794 -0.0016 93 THR A N 784 C CA . THR A 93 ? 0.3596 0.3553 0.3463 -0.0199 0.0889 0.0020 93 THR A CA 785 C C . THR A 93 ? 0.3918 0.3725 0.3747 -0.0278 0.0864 -0.0014 93 THR A C 786 O O . THR A 93 ? 0.3020 0.2893 0.2955 -0.0373 0.0799 -0.0077 93 THR A O 787 C CB . THR A 93 ? 0.2989 0.3025 0.2989 -0.0229 0.1017 0.0088 93 THR A CB 788 O OG1 . THR A 93 ? 0.2822 0.3005 0.3059 -0.0360 0.1008 0.0073 93 THR A OG1 789 C CG2 . THR A 93 ? 0.3610 0.3771 0.3646 -0.0137 0.1072 0.0120 93 THR A CG2 790 N N . ASN A 94 ? 0.3981 0.3589 0.3657 -0.0236 0.0920 0.0030 94 ASN A N 791 C CA . ASN A 94 ? 0.3613 0.3043 0.3265 -0.0286 0.0928 0.0022 94 ASN A CA 792 C C . ASN A 94 ? 0.3777 0.3227 0.3628 -0.0421 0.0994 0.0014 94 ASN A C 793 O O . ASN A 94 ? 0.3244 0.2605 0.3148 -0.0503 0.0978 -0.0049 94 ASN A O 794 C CB . ASN A 94 ? 0.4654 0.3911 0.4130 -0.0202 0.0990 0.0115 94 ASN A CB 795 C CG . ASN A 94 ? 0.6439 0.5501 0.5883 -0.0214 0.0989 0.0124 94 ASN A CG 796 O OD1 . ASN A 94 ? 0.7313 0.6347 0.6846 -0.0281 0.0946 0.0040 94 ASN A OD1 797 N ND2 . ASN A 94 ? 0.7730 0.6660 0.7044 -0.0145 0.1040 0.0230 94 ASN A ND2 798 N N . SER A 95 ? 0.3006 0.2565 0.2971 -0.0448 0.1079 0.0071 95 SER A N 799 C CA . SER A 95 ? 0.4018 0.3607 0.4188 -0.0588 0.1149 0.0066 95 SER A CA 800 C C . SER A 95 ? 0.4123 0.3961 0.4473 -0.0620 0.1189 0.0098 95 SER A C 801 O O . SER A 95 ? 0.3556 0.3495 0.3853 -0.0516 0.1191 0.0137 95 SER A O 802 C CB . SER A 95 ? 0.4873 0.4231 0.5001 -0.0591 0.1270 0.0151 95 SER A CB 803 O OG . SER A 95 ? 0.5504 0.4872 0.5556 -0.0511 0.1363 0.0267 95 SER A OG 804 N N . PRO A 96 ? 0.4236 0.4178 0.4814 -0.0768 0.1223 0.0074 96 PRO A N 805 C CA . PRO A 96 ? 0.4360 0.4571 0.5152 -0.0803 0.1260 0.0113 96 PRO A CA 806 C C . PRO A 96 ? 0.4055 0.4241 0.4789 -0.0698 0.1390 0.0228 96 PRO A C 807 O O . PRO A 96 ? 0.3550 0.3531 0.4170 -0.0678 0.1492 0.0294 96 PRO A O 808 C CB . PRO A 96 ? 0.4436 0.4689 0.5453 -0.0993 0.1302 0.0078 96 PRO A CB 809 C CG . PRO A 96 ? 0.4687 0.4636 0.5588 -0.1037 0.1323 0.0032 96 PRO A CG 810 C CD . PRO A 96 ? 0.4507 0.4345 0.5176 -0.0918 0.1225 -0.0003 96 PRO A CD 811 N N . VAL A 97 ? 0.3263 0.3662 0.4074 -0.0628 0.1392 0.0255 97 VAL A N 812 C CA . VAL A 97 ? 0.3724 0.4103 0.4441 -0.0513 0.1515 0.0338 97 VAL A CA 813 C C . VAL A 97 ? 0.3483 0.3957 0.4396 -0.0584 0.1665 0.0416 97 VAL A C 814 O O . VAL A 97 ? 0.3771 0.4476 0.4975 -0.0683 0.1659 0.0409 97 VAL A O 815 C CB . VAL A 97 ? 0.4088 0.4628 0.4815 -0.0398 0.1475 0.0326 97 VAL A CB 816 C CG1 . VAL A 97 ? 0.3961 0.4481 0.4594 -0.0291 0.1622 0.0391 97 VAL A CG1 817 C CG2 . VAL A 97 ? 0.4247 0.4676 0.4771 -0.0328 0.1339 0.0257 97 VAL A CG2 818 N N . GLU A 98 ? 0.3767 0.4073 0.4520 -0.0539 0.1796 0.0497 98 GLU A N 819 C CA . GLU A 98 ? 0.4369 0.4756 0.5273 -0.0584 0.1964 0.0587 98 GLU A CA 820 C C . GLU A 98 ? 0.4590 0.4931 0.5280 -0.0450 0.2084 0.0653 98 GLU A C 821 O O . GLU A 98 ? 0.4126 0.4278 0.4504 -0.0360 0.2059 0.0655 98 GLU A O 822 C CB . GLU A 98 ? 0.5575 0.5787 0.6511 -0.0700 0.2032 0.0633 98 GLU A CB 823 C CG . GLU A 98 ? 0.6723 0.6983 0.7883 -0.0857 0.1938 0.0547 98 GLU A CG 824 C CD . GLU A 98 ? 0.8500 0.8537 0.9689 -0.0968 0.2017 0.0579 98 GLU A CD 825 O OE1 . GLU A 98 ? 0.8983 0.8756 0.9936 -0.0896 0.2051 0.0638 98 GLU A OE1 826 O OE2 . GLU A 98 ? 0.9453 0.9584 1.0913 -0.1129 0.2045 0.0550 98 GLU A OE2 827 N N . LEU A 99 ? 0.4750 0.5278 0.5612 -0.0444 0.2217 0.0702 99 LEU A N 828 C CA . LEU A 99 ? 0.4584 0.5092 0.5253 -0.0325 0.2339 0.0743 99 LEU A CA 829 C C . LEU A 99 ? 0.4836 0.5098 0.5174 -0.0299 0.2375 0.0805 99 LEU A C 830 O O . LEU A 99 ? 0.4878 0.5056 0.5260 -0.0383 0.2413 0.0876 99 LEU A O 831 C CB . LEU A 99 ? 0.4293 0.5020 0.5210 -0.0341 0.2434 0.0778 99 LEU A CB 832 C CG . LEU A 99 ? 0.4780 0.5784 0.5999 -0.0315 0.2402 0.0735 99 LEU A CG 833 C CD1 . LEU A 99 ? 0.4701 0.5911 0.6151 -0.0321 0.2505 0.0779 99 LEU A CD1 834 C CD2 . LEU A 99 ? 0.5120 0.6080 0.6157 -0.0172 0.2362 0.0669 99 LEU A CD2 835 N N . ARG A 100 ? 0.4341 0.4497 0.4356 -0.0184 0.2354 0.0780 100 ARG A N 836 C CA . ARG A 100 ? 0.4902 0.4876 0.4589 -0.0149 0.2373 0.0845 100 ARG A CA 837 C C . ARG A 100 ? 0.4910 0.4688 0.4511 -0.0195 0.2312 0.0901 100 ARG A C 838 O O . ARG A 100 ? 0.5357 0.5009 0.4773 -0.0186 0.2335 0.0993 100 ARG A O 839 C CB . ARG A 100 ? 0.5309 0.5342 0.5017 -0.0169 0.2499 0.0924 100 ARG A CB 840 C CG . ARG A 100 ? 0.6226 0.6396 0.5909 -0.0097 0.2569 0.0870 100 ARG A CG 841 C CD . ARG A 100 ? 0.7438 0.7675 0.7159 -0.0128 0.2706 0.0947 100 ARG A CD 842 N NE . ARG A 100 ? 0.8291 0.8639 0.8370 -0.0230 0.2753 0.1000 100 ARG A NE 843 C CZ . ARG A 100 ? 0.8663 0.9222 0.9074 -0.0251 0.2776 0.0960 100 ARG A CZ 844 N NH1 . ARG A 100 ? 0.8045 0.8710 0.8486 -0.0165 0.2765 0.0876 100 ARG A NH1 845 N NH2 . ARG A 100 ? 0.9155 0.9826 0.9882 -0.0362 0.2804 0.1005 100 ARG A NH2 846 N N . GLU A 101 ? 0.4620 0.4379 0.4368 -0.0245 0.2237 0.0848 101 GLU A N 847 C CA A GLU A 101 ? 0.4460 0.4022 0.4134 -0.0275 0.2148 0.0868 101 GLU A CA 848 C CA B GLU A 101 ? 0.4479 0.4042 0.4159 -0.0277 0.2146 0.0867 101 GLU A CA 849 C C . GLU A 101 ? 0.4364 0.3864 0.3849 -0.0195 0.1982 0.0777 101 GLU A C 850 O O . GLU A 101 ? 0.3911 0.3514 0.3515 -0.0196 0.1878 0.0664 101 GLU A O 851 C CB A GLU A 101 ? 0.4412 0.3984 0.4402 -0.0409 0.2126 0.0841 101 GLU A CB 852 C CB B GLU A 101 ? 0.4442 0.4027 0.4445 -0.0411 0.2116 0.0829 101 GLU A CB 853 C CG A GLU A 101 ? 0.4483 0.4061 0.4652 -0.0504 0.2281 0.0943 101 GLU A CG 854 C CG B GLU A 101 ? 0.4376 0.3732 0.4351 -0.0454 0.2069 0.0853 101 GLU A CG 855 C CD A GLU A 101 ? 0.5023 0.4376 0.5034 -0.0489 0.2310 0.1060 101 GLU A CD 856 C CD B GLU A 101 ? 0.4563 0.3886 0.4542 -0.0455 0.1896 0.0724 101 GLU A CD 857 O OE1 A GLU A 101 ? 0.5295 0.4498 0.5054 -0.0405 0.2251 0.1088 101 GLU A OE1 858 O OE1 B GLU A 101 ? 0.4003 0.3478 0.4186 -0.0526 0.1826 0.0615 101 GLU A OE1 859 O OE2 A GLU A 101 ? 0.6112 0.5451 0.6264 -0.0559 0.2390 0.1129 101 GLU A OE2 860 O OE2 B GLU A 101 ? 0.4232 0.3389 0.4013 -0.0386 0.1831 0.0739 101 GLU A OE2 861 N N . PRO A 102 ? 0.4635 0.3980 0.3828 -0.0126 0.1958 0.0838 102 PRO A N 862 C CA . PRO A 102 ? 0.4480 0.3764 0.3471 -0.0050 0.1811 0.0768 102 PRO A CA 863 C C . PRO A 102 ? 0.4990 0.4278 0.4160 -0.0090 0.1674 0.0657 102 PRO A C 864 O O . PRO A 102 ? 0.4075 0.3294 0.3417 -0.0169 0.1667 0.0666 102 PRO A O 865 C CB . PRO A 102 ? 0.5113 0.4229 0.3894 -0.0018 0.1813 0.0893 102 PRO A CB 866 C CG . PRO A 102 ? 0.5256 0.4383 0.3991 -0.0034 0.1979 0.1026 102 PRO A CG 867 C CD . PRO A 102 ? 0.5469 0.4704 0.4519 -0.0123 0.2076 0.0998 102 PRO A CD 868 N N . ASN A 103 ? 0.3751 0.3114 0.2876 -0.0039 0.1574 0.0549 103 ASN A N 869 C CA . ASN A 103 ? 0.3535 0.2928 0.2805 -0.0073 0.1444 0.0446 103 ASN A CA 870 C C . ASN A 103 ? 0.3765 0.3132 0.2839 0.0014 0.1331 0.0378 103 ASN A C 871 O O . ASN A 103 ? 0.3875 0.3200 0.2712 0.0086 0.1353 0.0406 103 ASN A O 872 C CB . ASN A 103 ? 0.3400 0.2993 0.2940 -0.0131 0.1459 0.0392 103 ASN A CB 873 C CG . ASN A 103 ? 0.3274 0.2907 0.3009 -0.0221 0.1358 0.0317 103 ASN A CG 874 O OD1 . ASN A 103 ? 0.3729 0.3294 0.3386 -0.0204 0.1243 0.0254 103 ASN A OD1 875 N ND2 . ASN A 103 ? 0.3239 0.2997 0.3228 -0.0327 0.1403 0.0318 103 ASN A ND2 876 N N . VAL A 104 ? 0.3580 0.2977 0.2744 -0.0002 0.1212 0.0287 104 VAL A N 877 C CA . VAL A 104 ? 0.3548 0.2919 0.2557 0.0068 0.1104 0.0222 104 VAL A CA 878 C C . VAL A 104 ? 0.3153 0.2658 0.2315 0.0060 0.1030 0.0133 104 VAL A C 879 O O . VAL A 104 ? 0.2877 0.2444 0.2223 -0.0016 0.0986 0.0102 104 VAL A O 880 C CB . VAL A 104 ? 0.3808 0.3036 0.2726 0.0072 0.1018 0.0227 104 VAL A CB 881 C CG1 . VAL A 104 ? 0.3285 0.2503 0.2057 0.0138 0.0908 0.0161 104 VAL A CG1 882 C CG2 . VAL A 104 ? 0.3917 0.3021 0.2709 0.0089 0.1085 0.0344 104 VAL A CG2 883 N N . LEU A 105 ? 0.2955 0.2505 0.2038 0.0131 0.1021 0.0094 105 LEU A N 884 C CA . LEU A 105 ? 0.3022 0.2682 0.2233 0.0142 0.0945 0.0030 105 LEU A CA 885 C C . LEU A 105 ? 0.3438 0.3015 0.2544 0.0157 0.0820 -0.0023 105 LEU A C 886 O O . LEU A 105 ? 0.2776 0.2237 0.1675 0.0203 0.0800 -0.0029 105 LEU A O 887 C CB . LEU A 105 ? 0.3124 0.2841 0.2317 0.0219 0.1010 0.0012 105 LEU A CB 888 C CG . LEU A 105 ? 0.3616 0.3481 0.3012 0.0210 0.1126 0.0055 105 LEU A CG 889 C CD1 . LEU A 105 ? 0.3865 0.3730 0.3193 0.0297 0.1228 0.0035 105 LEU A CD1 890 C CD2 . LEU A 105 ? 0.3506 0.3555 0.3186 0.0167 0.1062 0.0056 105 LEU A CD2 891 N N . ILE A 106 ? 0.2554 0.2209 0.1803 0.0111 0.0735 -0.0060 106 ILE A N 892 C CA . ILE A 106 ? 0.2810 0.2403 0.1981 0.0119 0.0625 -0.0111 106 ILE A CA 893 C C . ILE A 106 ? 0.3119 0.2821 0.2370 0.0149 0.0569 -0.0143 106 ILE A C 894 O O . ILE A 106 ? 0.2907 0.2769 0.2348 0.0115 0.0565 -0.0129 106 ILE A O 895 C CB . ILE A 106 ? 0.2755 0.2332 0.2004 0.0032 0.0577 -0.0131 106 ILE A CB 896 C CG1 . ILE A 106 ? 0.2884 0.2345 0.2107 -0.0002 0.0650 -0.0085 106 ILE A CG1 897 C CG2 . ILE A 106 ? 0.3116 0.2625 0.2277 0.0047 0.0479 -0.0183 106 ILE A CG2 898 C CD1 . ILE A 106 ? 0.3272 0.2699 0.2601 -0.0099 0.0636 -0.0118 106 ILE A CD1 899 N N . CYS A 107 ? 0.2348 0.1973 0.1467 0.0210 0.0526 -0.0177 107 CYS A N 900 C CA . CYS A 107 ? 0.2450 0.2146 0.1642 0.0240 0.0473 -0.0200 107 CYS A CA 901 C C . CYS A 107 ? 0.2888 0.2552 0.2042 0.0209 0.0368 -0.0235 107 CYS A C 902 O O . CYS A 107 ? 0.3150 0.2691 0.2153 0.0227 0.0337 -0.0262 107 CYS A O 903 C CB . CYS A 107 ? 0.2331 0.1957 0.1426 0.0322 0.0517 -0.0224 107 CYS A CB 904 S SG . CYS A 107 ? 0.2996 0.2688 0.2221 0.0369 0.0477 -0.0234 107 CYS A SG 905 N N . PHE A 108 ? 0.2541 0.2333 0.1832 0.0158 0.0314 -0.0231 108 PHE A N 906 C CA . PHE A 108 ? 0.2362 0.2142 0.1619 0.0117 0.0228 -0.0268 108 PHE A CA 907 C C . PHE A 108 ? 0.2660 0.2498 0.1950 0.0157 0.0175 -0.0262 108 PHE A C 908 O O . PHE A 108 ? 0.2791 0.2778 0.2223 0.0160 0.0169 -0.0217 108 PHE A O 909 C CB . PHE A 108 ? 0.2197 0.2082 0.1556 0.0014 0.0204 -0.0278 108 PHE A CB 910 C CG . PHE A 108 ? 0.3186 0.3053 0.2494 -0.0035 0.0134 -0.0330 108 PHE A CG 911 C CD1 . PHE A 108 ? 0.3680 0.3389 0.2860 -0.0002 0.0124 -0.0363 108 PHE A CD1 912 C CD2 . PHE A 108 ? 0.2877 0.2900 0.2265 -0.0119 0.0082 -0.0345 108 PHE A CD2 913 C CE1 . PHE A 108 ? 0.3647 0.3342 0.2795 -0.0044 0.0078 -0.0412 108 PHE A CE1 914 C CE2 . PHE A 108 ? 0.3496 0.3502 0.2820 -0.0169 0.0033 -0.0402 108 PHE A CE2 915 C CZ . PHE A 108 ? 0.2960 0.2794 0.2169 -0.0128 0.0039 -0.0437 108 PHE A CZ 916 N N . ILE A 109 ? 0.2223 0.1953 0.1398 0.0186 0.0138 -0.0296 109 ILE A N 917 C CA . ILE A 109 ? 0.2352 0.2105 0.1554 0.0225 0.0099 -0.0288 109 ILE A CA 918 C C . ILE A 109 ? 0.2930 0.2703 0.2105 0.0174 0.0024 -0.0310 109 ILE A C 919 O O . ILE A 109 ? 0.2415 0.2083 0.1487 0.0164 0.0009 -0.0354 109 ILE A O 920 C CB . ILE A 109 ? 0.2597 0.2205 0.1689 0.0290 0.0127 -0.0319 109 ILE A CB 921 C CG1 . ILE A 109 ? 0.2794 0.2379 0.1884 0.0331 0.0218 -0.0310 109 ILE A CG1 922 C CG2 . ILE A 109 ? 0.1947 0.1550 0.1080 0.0325 0.0101 -0.0314 109 ILE A CG2 923 C CD1 . ILE A 109 ? 0.4034 0.3478 0.2941 0.0354 0.0247 -0.0355 109 ILE A CD1 924 N N . ASP A 110 ? 0.2204 0.2124 0.1474 0.0144 -0.0021 -0.0273 110 ASP A N 925 C CA . ASP A 110 ? 0.2203 0.2174 0.1439 0.0073 -0.0079 -0.0300 110 ASP A CA 926 C C . ASP A 110 ? 0.2631 0.2675 0.1893 0.0086 -0.0129 -0.0257 110 ASP A C 927 O O . ASP A 110 ? 0.2209 0.2316 0.1568 0.0138 -0.0125 -0.0186 110 ASP A O 928 C CB . ASP A 110 ? 0.1766 0.1880 0.1069 -0.0016 -0.0088 -0.0302 110 ASP A CB 929 C CG . ASP A 110 ? 0.2992 0.3110 0.2224 -0.0107 -0.0116 -0.0369 110 ASP A CG 930 O OD1 . ASP A 110 ? 0.2784 0.2773 0.1923 -0.0092 -0.0114 -0.0415 110 ASP A OD1 931 O OD2 . ASP A 110 ? 0.2822 0.3080 0.2099 -0.0198 -0.0136 -0.0382 110 ASP A OD2 932 N N . LYS A 111 ? 0.2260 0.2289 0.1445 0.0041 -0.0165 -0.0296 111 LYS A N 933 C CA . LYS A 111 ? 0.2641 0.2762 0.1835 0.0029 -0.0212 -0.0251 111 LYS A CA 934 C C . LYS A 111 ? 0.2745 0.2799 0.1979 0.0111 -0.0204 -0.0197 111 LYS A C 935 O O . LYS A 111 ? 0.1831 0.1993 0.1157 0.0134 -0.0222 -0.0105 111 LYS A O 936 C CB . LYS A 111 ? 0.3431 0.3784 0.2700 -0.0028 -0.0256 -0.0186 111 LYS A CB 937 C CG . LYS A 111 ? 0.4459 0.4894 0.3717 -0.0123 -0.0259 -0.0243 111 LYS A CG 938 C CD . LYS A 111 ? 0.5285 0.5985 0.4601 -0.0197 -0.0324 -0.0182 111 LYS A CD 939 C CE . LYS A 111 ? 0.5610 0.6420 0.4976 -0.0286 -0.0323 -0.0221 111 LYS A CE 940 N NZ . LYS A 111 ? 0.6798 0.7493 0.6053 -0.0375 -0.0291 -0.0356 111 LYS A NZ 941 N N . PHE A 112 ? 0.2041 0.1922 0.1213 0.0151 -0.0176 -0.0251 112 PHE A N 942 C CA . PHE A 112 ? 0.2073 0.1867 0.1279 0.0214 -0.0159 -0.0225 112 PHE A CA 943 C C . PHE A 112 ? 0.2738 0.2417 0.1866 0.0207 -0.0170 -0.0281 112 PHE A C 944 O O . PHE A 112 ? 0.2359 0.2005 0.1408 0.0174 -0.0181 -0.0342 112 PHE A O 945 C CB . PHE A 112 ? 0.2062 0.1772 0.1294 0.0274 -0.0101 -0.0237 112 PHE A CB 946 C CG . PHE A 112 ? 0.2748 0.2343 0.1863 0.0271 -0.0082 -0.0319 112 PHE A CG 947 C CD1 . PHE A 112 ? 0.2551 0.2012 0.1587 0.0291 -0.0075 -0.0375 112 PHE A CD1 948 C CD2 . PHE A 112 ? 0.2060 0.1693 0.1151 0.0242 -0.0072 -0.0332 112 PHE A CD2 949 C CE1 . PHE A 112 ? 0.2956 0.2342 0.1881 0.0289 -0.0069 -0.0429 112 PHE A CE1 950 C CE2 . PHE A 112 ? 0.2872 0.2405 0.1861 0.0246 -0.0052 -0.0382 112 PHE A CE2 951 C CZ . PHE A 112 ? 0.2463 0.1883 0.1365 0.0272 -0.0056 -0.0423 112 PHE A CZ 952 N N . THR A 113 ? 0.2205 0.2321 0.2299 0.0634 0.0003 0.0142 113 THR A N 953 C CA . THR A 113 ? 0.1826 0.1928 0.1965 0.0522 0.0005 0.0167 113 THR A CA 954 C C . THR A 113 ? 0.2033 0.1944 0.2175 0.0468 0.0125 0.0162 113 THR A C 955 O O . THR A 113 ? 0.2133 0.1952 0.2245 0.0562 0.0214 0.0192 113 THR A O 956 C CB . THR A 113 ? 0.1763 0.2007 0.1986 0.0597 -0.0006 0.0246 113 THR A CB 957 O OG1 . THR A 113 ? 0.1835 0.2117 0.2121 0.0473 -0.0050 0.0239 113 THR A OG1 958 C CG2 . THR A 113 ? 0.1737 0.1920 0.1974 0.0715 0.0128 0.0341 113 THR A CG2 959 N N . PRO A 114 ? 0.2298 0.2161 0.2496 0.0321 0.0130 0.0109 114 PRO A N 960 C CA . PRO A 114 ? 0.1450 0.1436 0.1676 0.0216 0.0024 0.0060 114 PRO A CA 961 C C . PRO A 114 ? 0.1712 0.1761 0.1820 0.0184 -0.0080 0.0000 114 PRO A C 962 O O . PRO A 114 ? 0.2212 0.2179 0.2233 0.0209 -0.0056 -0.0028 114 PRO A O 963 C CB . PRO A 114 ? 0.1921 0.1824 0.2262 0.0089 0.0089 -0.0018 114 PRO A CB 964 C CG . PRO A 114 ? 0.2009 0.1728 0.2345 0.0097 0.0206 -0.0041 114 PRO A CG 965 C CD . PRO A 114 ? 0.1901 0.1587 0.2174 0.0262 0.0259 0.0082 114 PRO A CD 966 N N . PRO A 115 ? 0.1881 0.2077 0.1994 0.0141 -0.0184 -0.0009 115 PRO A N 967 C CA . PRO A 115 ? 0.2197 0.2461 0.2204 0.0132 -0.0261 -0.0032 115 PRO A CA 968 C C . PRO A 115 ? 0.2350 0.2577 0.2265 0.0049 -0.0258 -0.0134 115 PRO A C 969 O O . PRO A 115 ? 0.2062 0.2416 0.1946 -0.0002 -0.0331 -0.0182 115 PRO A O 970 C CB . PRO A 115 ? 0.1533 0.1969 0.1591 0.0124 -0.0357 0.0003 115 PRO A CB 971 C CG . PRO A 115 ? 0.1478 0.1928 0.1654 0.0066 -0.0337 -0.0019 115 PRO A CG 972 C CD . PRO A 115 ? 0.2251 0.2563 0.2475 0.0120 -0.0223 0.0022 115 PRO A CD 973 N N . VAL A 116 ? 0.2289 0.2368 0.2165 0.0046 -0.0176 -0.0177 116 VAL A N 974 C CA . VAL A 116 ? 0.1980 0.2032 0.1770 -0.0019 -0.0167 -0.0291 116 VAL A CA 975 C C . VAL A 116 ? 0.2839 0.2755 0.2542 0.0029 -0.0101 -0.0284 116 VAL A C 976 O O . VAL A 116 ? 0.2380 0.2168 0.2141 0.0071 -0.0023 -0.0255 116 VAL A O 977 C CB . VAL A 116 ? 0.2829 0.2831 0.2745 -0.0112 -0.0113 -0.0407 116 VAL A CB 978 C CG1 . VAL A 116 ? 0.2713 0.2745 0.2555 -0.0175 -0.0123 -0.0561 116 VAL A CG1 979 C CG2 . VAL A 116 ? 0.2047 0.2170 0.2104 -0.0162 -0.0157 -0.0422 116 VAL A CG2 980 N N . VAL A 117 ? 0.2780 0.2734 0.2346 0.0039 -0.0126 -0.0303 117 VAL A N 981 C CA . VAL A 117 ? 0.2331 0.2166 0.1821 0.0078 -0.0061 -0.0310 117 VAL A CA 982 C C . VAL A 117 ? 0.2964 0.2850 0.2306 0.0049 -0.0072 -0.0383 117 VAL A C 983 O O . VAL A 117 ? 0.3540 0.3587 0.2808 0.0040 -0.0142 -0.0390 117 VAL A O 984 C CB . VAL A 117 ? 0.3303 0.3140 0.2810 0.0172 -0.0057 -0.0212 117 VAL A CB 985 C CG1 . VAL A 117 ? 0.3670 0.3481 0.3308 0.0234 -0.0041 -0.0164 117 VAL A CG1 986 C CG2 . VAL A 117 ? 0.3288 0.3270 0.2767 0.0192 -0.0120 -0.0142 117 VAL A CG2 987 N N . ASN A 118 ? 0.3042 0.2810 0.2330 0.0048 -0.0004 -0.0439 118 ASN A N 988 C CA . ASN A 118 ? 0.3084 0.2904 0.2210 0.0050 0.0000 -0.0489 118 ASN A CA 989 C C . ASN A 118 ? 0.3199 0.2933 0.2293 0.0124 0.0060 -0.0403 118 ASN A C 990 O O . ASN A 118 ? 0.3099 0.2690 0.2267 0.0143 0.0120 -0.0410 118 ASN A O 991 C CB . ASN A 118 ? 0.3407 0.3170 0.2521 -0.0015 0.0039 -0.0647 118 ASN A CB 992 C CG . ASN A 118 ? 0.4563 0.4429 0.3769 -0.0097 -0.0007 -0.0776 118 ASN A CG 993 O OD1 . ASN A 118 ? 0.4427 0.4469 0.3621 -0.0099 -0.0090 -0.0770 118 ASN A OD1 994 N ND2 . ASN A 118 ? 0.5232 0.4990 0.4561 -0.0163 0.0055 -0.0903 118 ASN A ND2 995 N N . VAL A 119 ? 0.3138 0.2967 0.2144 0.0176 0.0053 -0.0322 119 VAL A N 996 C CA . VAL A 119 ? 0.3349 0.3103 0.2386 0.0243 0.0128 -0.0242 119 VAL A CA 997 C C . VAL A 119 ? 0.3874 0.3662 0.2738 0.0271 0.0179 -0.0237 119 VAL A C 998 O O . VAL A 119 ? 0.3406 0.3351 0.2131 0.0291 0.0140 -0.0210 119 VAL A O 999 C CB . VAL A 119 ? 0.3605 0.3424 0.2761 0.0300 0.0114 -0.0115 119 VAL A CB 1000 C CG1 . VAL A 119 ? 0.2882 0.2627 0.2135 0.0363 0.0212 -0.0059 119 VAL A CG1 1001 C CG2 . VAL A 119 ? 0.2959 0.2780 0.2275 0.0288 0.0059 -0.0120 119 VAL A CG2 1002 N N . THR A 120 ? 0.3395 0.3057 0.2264 0.0285 0.0267 -0.0265 120 THR A N 1003 C CA . THR A 120 ? 0.3112 0.2799 0.1823 0.0323 0.0337 -0.0250 120 THR A CA 1004 C C . THR A 120 ? 0.2971 0.2547 0.1797 0.0379 0.0453 -0.0174 120 THR A C 1005 O O . THR A 120 ? 0.3357 0.2809 0.2342 0.0369 0.0482 -0.0228 120 THR A O 1006 C CB . THR A 120 ? 0.3322 0.2970 0.1919 0.0272 0.0346 -0.0403 120 THR A CB 1007 O OG1 . THR A 120 ? 0.3647 0.3366 0.2239 0.0202 0.0256 -0.0515 120 THR A OG1 1008 C CG2 . THR A 120 ? 0.3046 0.2794 0.1434 0.0326 0.0398 -0.0390 120 THR A CG2 1009 N N . TRP A 121 ? 0.3368 0.3004 0.2128 0.0450 0.0528 -0.0052 121 TRP A N 1010 C CA . TRP A 121 ? 0.3280 0.2813 0.2166 0.0501 0.0670 0.0011 121 TRP A CA 1011 C C . TRP A 121 ? 0.3818 0.3301 0.2545 0.0498 0.0739 -0.0061 121 TRP A C 1012 O O . TRP A 121 ? 0.3800 0.3398 0.2278 0.0514 0.0718 -0.0070 121 TRP A O 1013 C CB . TRP A 121 ? 0.3376 0.2984 0.2280 0.0590 0.0752 0.0202 121 TRP A CB 1014 C CG . TRP A 121 ? 0.3007 0.2631 0.2155 0.0603 0.0729 0.0278 121 TRP A CG 1015 C CD1 . TRP A 121 ? 0.3021 0.2775 0.2126 0.0626 0.0653 0.0370 121 TRP A CD1 1016 C CD2 . TRP A 121 ? 0.2861 0.2392 0.2355 0.0600 0.0779 0.0248 121 TRP A CD2 1017 N NE1 . TRP A 121 ? 0.2843 0.2577 0.2247 0.0633 0.0658 0.0409 121 TRP A NE1 1018 C CE2 . TRP A 121 ? 0.3205 0.2815 0.2858 0.0619 0.0733 0.0325 121 TRP A CE2 1019 C CE3 . TRP A 121 ? 0.2987 0.2401 0.2686 0.0591 0.0855 0.0145 121 TRP A CE3 1020 C CZ2 . TRP A 121 ? 0.2708 0.2292 0.2725 0.0628 0.0759 0.0291 121 TRP A CZ2 1021 C CZ3 . TRP A 121 ? 0.2776 0.2180 0.2837 0.0606 0.0876 0.0103 121 TRP A CZ3 1022 C CH2 . TRP A 121 ? 0.2640 0.2133 0.2862 0.0624 0.0829 0.0170 121 TRP A CH2 1023 N N . LEU A 122 ? 0.3320 0.2657 0.2197 0.0486 0.0817 -0.0128 122 LEU A N 1024 C CA . LEU A 122 ? 0.3885 0.3163 0.2640 0.0485 0.0896 -0.0196 122 LEU A CA 1025 C C . LEU A 122 ? 0.3928 0.3127 0.2840 0.0545 0.1064 -0.0111 122 LEU A C 1026 O O . LEU A 122 ? 0.3972 0.3101 0.3180 0.0552 0.1104 -0.0112 122 LEU A O 1027 C CB . LEU A 122 ? 0.3907 0.3071 0.2714 0.0418 0.0851 -0.0369 122 LEU A CB 1028 C CG . LEU A 122 ? 0.3668 0.2867 0.2395 0.0352 0.0720 -0.0465 122 LEU A CG 1029 C CD1 . LEU A 122 ? 0.3603 0.2717 0.2507 0.0306 0.0676 -0.0564 122 LEU A CD1 1030 C CD2 . LEU A 122 ? 0.3921 0.3232 0.2402 0.0330 0.0687 -0.0526 122 LEU A CD2 1031 N N . ARG A 123 ? 0.3512 0.2744 0.2247 0.0596 0.1169 -0.0044 123 ARG A N 1032 C CA . ARG A 123 ? 0.3941 0.3084 0.2829 0.0646 0.1351 0.0031 123 ARG A CA 1033 C C . ARG A 123 ? 0.3931 0.3040 0.2734 0.0600 0.1342 -0.0086 123 ARG A C 1034 O O . ARG A 123 ? 0.3431 0.2646 0.1954 0.0609 0.1307 -0.0110 123 ARG A O 1035 C CB . ARG A 123 ? 0.3580 0.2814 0.2382 0.0753 0.1469 0.0257 123 ARG A CB 1036 C CG . ARG A 123 ? 0.4550 0.3705 0.3483 0.0791 0.1629 0.0343 123 ARG A CG 1037 C CD . ARG A 123 ? 0.4716 0.3919 0.3681 0.0907 0.1754 0.0594 123 ARG A CD 1038 N NE . ARG A 123 ? 0.7066 0.6467 0.5740 0.0975 0.1661 0.0694 123 ARG A NE 1039 C CZ . ARG A 123 ? 0.8560 0.8015 0.7316 0.1040 0.1671 0.0855 123 ARG A CZ 1040 N NH1 . ARG A 123 ? 0.8792 0.8452 0.7283 0.1098 0.1554 0.0915 123 ARG A NH1 1041 N NH2 . ARG A 123 ? 0.8881 0.8201 0.8019 0.1044 0.1786 0.0935 123 ARG A NH2 1042 N N . ASN A 124 ? 0.3586 0.2591 0.2656 0.0547 0.1348 -0.0167 124 ASN A N 1043 C CA . ASN A 124 ? 0.3708 0.2692 0.2736 0.0497 0.1321 -0.0281 124 ASN A CA 1044 C C . ASN A 124 ? 0.3924 0.2971 0.2756 0.0443 0.1178 -0.0414 124 ASN A C 1045 O O . ASN A 124 ? 0.3623 0.2719 0.2306 0.0431 0.1171 -0.0481 124 ASN A O 1046 C CB . ASN A 124 ? 0.4512 0.3504 0.3426 0.0559 0.1471 -0.0188 124 ASN A CB 1047 C CG . ASN A 124 ? 0.4326 0.3238 0.3493 0.0607 0.1627 -0.0042 124 ASN A CG 1048 O OD1 . ASN A 124 ? 0.4215 0.3064 0.3703 0.0556 0.1603 -0.0082 124 ASN A OD1 1049 N ND2 . ASN A 124 ? 0.4168 0.3117 0.3214 0.0703 0.1766 0.0130 124 ASN A ND2 1050 N N . GLY A 125 ? 0.3182 0.2238 0.2050 0.0411 0.1067 -0.0454 125 GLY A N 1051 C CA . GLY A 125 ? 0.4090 0.3194 0.2860 0.0353 0.0940 -0.0572 125 GLY A CA 1052 C C . GLY A 125 ? 0.4025 0.3250 0.2509 0.0363 0.0917 -0.0591 125 GLY A C 1053 O O . GLY A 125 ? 0.4150 0.3429 0.2596 0.0308 0.0821 -0.0711 125 GLY A O 1054 N N . LYS A 126 ? 0.3963 0.3265 0.2281 0.0442 0.0993 -0.0463 126 LYS A N 1055 C CA . LYS A 126 ? 0.3501 0.3007 0.1553 0.0474 0.0937 -0.0463 126 LYS A CA 1056 C C . LYS A 126 ? 0.3469 0.3037 0.1473 0.0526 0.0905 -0.0341 126 LYS A C 1057 O O . LYS A 126 ? 0.4000 0.3513 0.2146 0.0576 0.0983 -0.0181 126 LYS A O 1058 C CB . LYS A 126 ? 0.3740 0.3381 0.1633 0.0551 0.1020 -0.0386 126 LYS A CB 1059 C CG . LYS A 126 ? 0.3794 0.3400 0.1721 0.0514 0.1062 -0.0496 126 LYS A CG 1060 C CD . LYS A 126 ? 0.4419 0.4186 0.2157 0.0598 0.1138 -0.0418 126 LYS A CD 1061 C CE . LYS A 126 ? 0.5820 0.5594 0.3565 0.0557 0.1164 -0.0552 126 LYS A CE 1062 N NZ . LYS A 126 ? 0.5871 0.5822 0.3403 0.0639 0.1227 -0.0490 126 LYS A NZ 1063 N N . PRO A 127 ? 0.4679 0.4399 0.2584 0.0494 0.0766 -0.0421 127 PRO A N 1064 C CA . PRO A 127 ? 0.3960 0.3787 0.1889 0.0519 0.0691 -0.0310 127 PRO A CA 1065 C C . PRO A 127 ? 0.3976 0.3932 0.1779 0.0655 0.0776 -0.0100 127 PRO A C 1066 O O . PRO A 127 ? 0.3790 0.3871 0.1443 0.0711 0.0812 -0.0080 127 PRO A O 1067 C CB . PRO A 127 ? 0.4629 0.4637 0.2446 0.0471 0.0547 -0.0472 127 PRO A CB 1068 C CG . PRO A 127 ? 0.5157 0.5067 0.3007 0.0384 0.0544 -0.0677 127 PRO A CG 1069 C CD . PRO A 127 ? 0.5476 0.5290 0.3308 0.0418 0.0672 -0.0631 127 PRO A CD 1070 N N . VAL A 128 ? 0.4056 0.3985 0.2005 0.0688 0.0793 0.0061 128 VAL A N 1071 C CA . VAL A 128 ? 0.4914 0.4958 0.2770 0.0829 0.0887 0.0286 128 VAL A CA 1072 C C . VAL A 128 ? 0.5180 0.5360 0.3046 0.0851 0.0780 0.0363 128 VAL A C 1073 O O . VAL A 128 ? 0.5333 0.5434 0.3399 0.0759 0.0691 0.0305 128 VAL A O 1074 C CB . VAL A 128 ? 0.5759 0.5616 0.3844 0.0873 0.1082 0.0444 128 VAL A CB 1075 C CG1 . VAL A 128 ? 0.7093 0.6861 0.5159 0.0864 0.1182 0.0383 128 VAL A CG1 1076 C CG2 . VAL A 128 ? 0.4792 0.4476 0.3231 0.0782 0.1059 0.0400 128 VAL A CG2 1077 N N . THR A 129 ? 0.5577 0.5962 0.3327 0.0947 0.0753 0.0474 129 THR A N 1078 C CA . THR A 129 ? 0.6343 0.6886 0.4094 0.0972 0.0636 0.0524 129 THR A CA 1079 C C . THR A 129 ? 0.6770 0.7378 0.4577 0.1109 0.0720 0.0766 129 THR A C 1080 O O . THR A 129 ? 0.6992 0.7680 0.4867 0.1134 0.0658 0.0839 129 THR A O 1081 C CB . THR A 129 ? 0.6126 0.6911 0.3709 0.0946 0.0463 0.0345 129 THR A CB 1082 O OG1 . THR A 129 ? 0.6490 0.7410 0.3915 0.1025 0.0495 0.0337 129 THR A OG1 1083 C CG2 . THR A 129 ? 0.5954 0.6671 0.3559 0.0802 0.0371 0.0101 129 THR A CG2 1084 N N . THR A 130 ? 0.7367 0.7940 0.5161 0.1201 0.0866 0.0886 130 THR A N 1085 C CA . THR A 130 ? 0.7325 0.7953 0.5192 0.1350 0.0968 0.1118 130 THR A CA 1086 C C . THR A 130 ? 0.6504 0.6948 0.4687 0.1340 0.1072 0.1255 130 THR A C 1087 O O . THR A 130 ? 0.6805 0.7025 0.5193 0.1286 0.1196 0.1259 130 THR A O 1088 C CB . THR A 130 ? 0.7803 0.8416 0.5613 0.1458 0.1121 0.1221 130 THR A CB 1089 O OG1 . THR A 130 ? 0.8598 0.8948 0.6591 0.1390 0.1264 0.1219 130 THR A OG1 1090 C CG2 . THR A 130 ? 0.7039 0.7859 0.4555 0.1474 0.1019 0.1072 130 THR A CG2 1091 N N . GLY A 131 ? 0.5647 0.6197 0.3898 0.1391 0.1021 0.1347 131 GLY A N 1092 C CA . GLY A 131 ? 0.5282 0.5696 0.3866 0.1397 0.1121 0.1477 131 GLY A CA 1093 C C . GLY A 131 ? 0.5027 0.5364 0.3737 0.1264 0.1018 0.1370 131 GLY A C 1094 O O . GLY A 131 ? 0.5709 0.5976 0.4705 0.1260 0.1065 0.1451 131 GLY A O 1095 N N . VAL A 132 ? 0.3783 0.4143 0.2301 0.1161 0.0880 0.1182 132 VAL A N 1096 C CA . VAL A 132 ? 0.3395 0.3678 0.2037 0.1046 0.0786 0.1076 132 VAL A CA 1097 C C . VAL A 132 ? 0.4120 0.4545 0.2786 0.1050 0.0650 0.1107 132 VAL A C 1098 O O . VAL A 132 ? 0.4340 0.4956 0.2879 0.1113 0.0581 0.1135 132 VAL A O 1099 C CB . VAL A 132 ? 0.3605 0.3850 0.2148 0.0915 0.0667 0.0821 132 VAL A CB 1100 C CG1 . VAL A 132 ? 0.3269 0.3372 0.1808 0.0911 0.0800 0.0786 132 VAL A CG1 1101 C CG2 . VAL A 132 ? 0.4565 0.5032 0.2793 0.0917 0.0513 0.0717 132 VAL A CG2 1102 N N . SER A 133 ? 0.3262 0.3598 0.2206 0.0954 0.0588 0.1033 133 SER A N 1103 C CA . SER A 133 ? 0.2976 0.3431 0.1972 0.0943 0.0459 0.1046 133 SER A CA 1104 C C . SER A 133 ? 0.2792 0.3155 0.2012 0.0809 0.0360 0.0874 133 SER A C 1105 O O . SER A 133 ? 0.2898 0.3110 0.2253 0.0751 0.0409 0.0773 133 SER A O 1106 C CB . SER A 133 ? 0.3314 0.3774 0.2518 0.1045 0.0570 0.1260 133 SER A CB 1107 O OG . SER A 133 ? 0.3313 0.3584 0.2893 0.1017 0.0701 0.1270 133 SER A OG 1108 N N . GLU A 134 ? 0.2760 0.3509 0.1286 -0.0123 -0.0117 0.0164 134 GLU A N 1109 C CA . GLU A 134 ? 0.3037 0.3506 0.1700 -0.0118 -0.0127 0.0039 134 GLU A CA 1110 C C . GLU A 134 ? 0.3040 0.3769 0.1891 -0.0034 -0.0206 0.0211 134 GLU A C 1111 O O . GLU A 134 ? 0.2911 0.4115 0.1766 -0.0010 -0.0254 0.0428 134 GLU A O 1112 C CB . GLU A 134 ? 0.3144 0.3488 0.1577 -0.0340 -0.0100 -0.0211 134 GLU A CB 1113 C CG . GLU A 134 ? 0.4217 0.4999 0.2471 -0.0570 -0.0193 -0.0230 134 GLU A CG 1114 C CD . GLU A 134 ? 0.4738 0.5237 0.2829 -0.0802 -0.0075 -0.0490 134 GLU A CD 1115 O OE1 . GLU A 134 ? 0.4610 0.5051 0.2773 -0.0889 -0.0079 -0.0566 134 GLU A OE1 1116 O OE2 . GLU A 134 ? 0.5832 0.6148 0.3726 -0.0889 0.0053 -0.0598 134 GLU A OE2 1117 N N . THR A 135 ? 0.3081 0.3554 0.2094 0.0025 -0.0200 0.0150 135 THR A N 1118 C CA . THR A 135 ? 0.3330 0.3982 0.2505 0.0108 -0.0238 0.0293 135 THR A CA 1119 C C . THR A 135 ? 0.3395 0.4198 0.2503 -0.0062 -0.0333 0.0164 135 THR A C 1120 O O . THR A 135 ? 0.2854 0.3473 0.1794 -0.0231 -0.0319 -0.0062 135 THR A O 1121 C CB . THR A 135 ? 0.2651 0.2918 0.1995 0.0234 -0.0150 0.0279 135 THR A CB 1122 O OG1 . THR A 135 ? 0.2506 0.2544 0.1838 0.0142 -0.0179 0.0065 135 THR A OG1 1123 C CG2 . THR A 135 ? 0.2726 0.2747 0.2095 0.0318 -0.0018 0.0337 135 THR A CG2 1124 N N . VAL A 136 ? 0.2669 0.3774 0.1915 -0.0011 -0.0384 0.0324 136 VAL A N 1125 C CA . VAL A 136 ? 0.2562 0.3765 0.1793 -0.0165 -0.0459 0.0208 136 VAL A CA 1126 C C . VAL A 136 ? 0.2763 0.3472 0.2095 -0.0093 -0.0402 0.0054 136 VAL A C 1127 O O . VAL A 136 ? 0.2642 0.3018 0.2028 0.0027 -0.0326 0.0029 136 VAL A O 1128 C CB . VAL A 136 ? 0.1928 0.3673 0.1331 -0.0121 -0.0513 0.0469 136 VAL A CB 1129 C CG1 . VAL A 136 ? 0.2059 0.4291 0.1472 -0.0195 -0.0506 0.0623 136 VAL A CG1 1130 C CG2 . VAL A 136 ? 0.1873 0.3503 0.1509 0.0193 -0.0417 0.0707 136 VAL A CG2 1131 N N . PHE A 137 ? 0.2056 0.2779 0.1407 -0.0193 -0.0436 -0.0037 137 PHE A N 1132 C CA . PHE A 137 ? 0.2584 0.2962 0.2048 -0.0112 -0.0387 -0.0128 137 PHE A CA 1133 C C . PHE A 137 ? 0.3015 0.3394 0.2655 0.0076 -0.0371 0.0023 137 PHE A C 1134 O O . PHE A 137 ? 0.2776 0.3442 0.2509 0.0129 -0.0398 0.0189 137 PHE A O 1135 C CB . PHE A 137 ? 0.2628 0.2991 0.2059 -0.0270 -0.0385 -0.0255 137 PHE A CB 1136 C CG . PHE A 137 ? 0.2511 0.2693 0.1709 -0.0479 -0.0292 -0.0446 137 PHE A CG 1137 C CD1 . PHE A 137 ? 0.2295 0.2061 0.1476 -0.0414 -0.0135 -0.0541 137 PHE A CD1 1138 C CD2 . PHE A 137 ? 0.3209 0.3653 0.2214 -0.0732 -0.0319 -0.0500 137 PHE A CD2 1139 C CE1 . PHE A 137 ? 0.2946 0.2432 0.1892 -0.0576 0.0045 -0.0705 137 PHE A CE1 1140 C CE2 . PHE A 137 ? 0.4365 0.4532 0.3174 -0.0902 -0.0150 -0.0666 137 PHE A CE2 1141 C CZ . PHE A 137 ? 0.3849 0.3504 0.2617 -0.0816 0.0042 -0.0771 137 PHE A CZ 1142 N N . LEU A 138 ? 0.2433 0.2509 0.2101 0.0158 -0.0299 -0.0026 138 LEU A N 1143 C CA . LEU A 138 ? 0.2156 0.2102 0.1894 0.0282 -0.0210 0.0059 138 LEU A CA 1144 C C . LEU A 138 ? 0.2599 0.2445 0.2382 0.0268 -0.0211 -0.0031 138 LEU A C 1145 O O . LEU A 138 ? 0.2403 0.2218 0.2178 0.0197 -0.0245 -0.0141 138 LEU A O 1146 C CB . LEU A 138 ? 0.2248 0.1943 0.1920 0.0292 -0.0103 0.0033 138 LEU A CB 1147 C CG . LEU A 138 ? 0.2313 0.2114 0.1943 0.0314 -0.0097 0.0128 138 LEU A CG 1148 C CD1 . LEU A 138 ? 0.2433 0.1977 0.1999 0.0279 0.0000 0.0067 138 LEU A CD1 1149 C CD2 . LEU A 138 ? 0.2470 0.2464 0.2177 0.0467 -0.0023 0.0387 138 LEU A CD2 1150 N N . PRO A 139 ? 0.2381 0.2201 0.2220 0.0361 -0.0142 0.0055 139 PRO A N 1151 C CA . PRO A 139 ? 0.2276 0.2059 0.2147 0.0348 -0.0147 -0.0013 139 PRO A CA 1152 C C . PRO A 139 ? 0.2884 0.2460 0.2646 0.0271 -0.0074 -0.0145 139 PRO A C 1153 O O . PRO A 139 ? 0.2723 0.2078 0.2373 0.0239 0.0049 -0.0175 139 PRO A O 1154 C CB . PRO A 139 ? 0.2055 0.1874 0.2003 0.0488 -0.0055 0.0150 139 PRO A CB 1155 C CG . PRO A 139 ? 0.2509 0.2209 0.2430 0.0595 0.0097 0.0288 139 PRO A CG 1156 C CD . PRO A 139 ? 0.2529 0.2370 0.2417 0.0515 -0.0015 0.0265 139 PRO A CD 1157 N N . ARG A 140 ? 0.1917 0.1607 0.1706 0.0217 -0.0131 -0.0208 140 ARG A N 1158 C CA . ARG A 140 ? 0.2660 0.2340 0.2333 0.0092 -0.0085 -0.0306 140 ARG A CA 1159 C C . ARG A 140 ? 0.2941 0.2592 0.2580 0.0110 -0.0027 -0.0317 140 ARG A C 1160 O O . ARG A 140 ? 0.2024 0.1741 0.1795 0.0233 -0.0062 -0.0230 140 ARG A O 1161 C CB . ARG A 140 ? 0.2251 0.2234 0.2004 0.0037 -0.0177 -0.0290 140 ARG A CB 1162 C CG . ARG A 140 ? 0.1898 0.1906 0.1660 0.0008 -0.0195 -0.0279 140 ARG A CG 1163 C CD . ARG A 140 ? 0.1947 0.2270 0.1848 0.0036 -0.0220 -0.0178 140 ARG A CD 1164 N NE . ARG A 140 ? 0.1631 0.2301 0.1545 -0.0038 -0.0234 -0.0134 140 ARG A NE 1165 C CZ . ARG A 140 ? 0.2472 0.3439 0.2301 -0.0225 -0.0248 -0.0145 140 ARG A CZ 1166 N NH1 . ARG A 140 ? 0.1717 0.2608 0.1469 -0.0331 -0.0234 -0.0198 140 ARG A NH1 1167 N NH2 . ARG A 140 ? 0.1972 0.3370 0.1784 -0.0335 -0.0274 -0.0096 140 ARG A NH2 1168 N N . GLU A 141 ? 0.2297 0.1869 0.1733 -0.0050 0.0072 -0.0437 141 GLU A N 1169 C CA . GLU A 141 ? 0.2675 0.2189 0.2013 -0.0059 0.0162 -0.0474 141 GLU A CA 1170 C C . GLU A 141 ? 0.2625 0.2551 0.2116 -0.0020 0.0018 -0.0397 141 GLU A C 1171 O O . GLU A 141 ? 0.2320 0.2239 0.1799 0.0035 0.0066 -0.0380 141 GLU A O 1172 C CB . GLU A 141 ? 0.3592 0.2884 0.2583 -0.0322 0.0346 -0.0673 141 GLU A CB 1173 C CG . GLU A 141 ? 0.4222 0.2942 0.3060 -0.0312 0.0606 -0.0724 141 GLU A CG 1174 C CD . GLU A 141 ? 0.5792 0.4391 0.4418 -0.0608 0.0758 -0.0844 141 GLU A CD 1175 O OE1 . GLU A 141 ? 0.6263 0.4757 0.4731 -0.0719 0.0890 -0.0911 141 GLU A OE1 1176 O OE2 . GLU A 141 ? 0.7272 0.5870 0.5873 -0.0746 0.0765 -0.0873 141 GLU A OE2 1177 N N . ASP A 142 ? 0.2308 0.2568 0.1957 -0.0015 -0.0113 -0.0317 142 ASP A N 1178 C CA . ASP A 142 ? 0.1691 0.2290 0.1533 0.0083 -0.0178 -0.0181 142 ASP A CA 1179 C C . ASP A 142 ? 0.2383 0.2852 0.2437 0.0255 -0.0198 -0.0093 142 ASP A C 1180 O O . ASP A 142 ? 0.1984 0.2611 0.2209 0.0343 -0.0191 0.0019 142 ASP A O 1181 C CB . ASP A 142 ? 0.1420 0.2503 0.1330 0.0016 -0.0225 -0.0075 142 ASP A CB 1182 C CG . ASP A 142 ? 0.2057 0.3114 0.2049 0.0040 -0.0240 -0.0036 142 ASP A CG 1183 O OD1 . ASP A 142 ? 0.1755 0.2435 0.1750 0.0103 -0.0229 -0.0099 142 ASP A OD1 1184 O OD2 . ASP A 142 ? 0.2177 0.3657 0.2234 -0.0008 -0.0255 0.0084 142 ASP A OD2 1185 N N . HIS A 143 ? 0.1831 0.2036 0.1858 0.0277 -0.0195 -0.0137 143 HIS A N 1186 C CA . HIS A 143 ? 0.1572 0.1726 0.1727 0.0343 -0.0221 -0.0086 143 HIS A CA 1187 C C . HIS A 143 ? 0.1651 0.1801 0.1867 0.0319 -0.0222 -0.0085 143 HIS A C 1188 O O . HIS A 143 ? 0.2027 0.2130 0.2293 0.0291 -0.0212 -0.0087 143 HIS A O 1189 C CB . HIS A 143 ? 0.1822 0.2049 0.2081 0.0407 -0.0207 -0.0021 143 HIS A CB 1190 C CG . HIS A 143 ? 0.1555 0.1729 0.1711 0.0437 -0.0146 -0.0030 143 HIS A CG 1191 N ND1 . HIS A 143 ? 0.1591 0.1565 0.1641 0.0464 -0.0064 -0.0037 143 HIS A ND1 1192 C CD2 . HIS A 143 ? 0.1486 0.1749 0.1596 0.0439 -0.0104 -0.0032 143 HIS A CD2 1193 C CE1 . HIS A 143 ? 0.1746 0.1594 0.1667 0.0475 0.0061 -0.0069 143 HIS A CE1 1194 N NE2 . HIS A 143 ? 0.1879 0.1926 0.1816 0.0439 0.0016 -0.0083 143 HIS A NE2 1195 N N . LEU A 144 ? 0.2014 0.2214 0.2198 0.0301 -0.0206 -0.0085 144 LEU A N 1196 C CA . LEU A 144 ? 0.1778 0.1891 0.1968 0.0292 -0.0157 -0.0088 144 LEU A CA 1197 C C . LEU A 144 ? 0.1931 0.1928 0.1992 0.0227 -0.0212 -0.0165 144 LEU A C 1198 O O . LEU A 144 ? 0.2177 0.2149 0.2187 0.0224 -0.0253 -0.0177 144 LEU A O 1199 C CB . LEU A 144 ? 0.1536 0.1858 0.1795 0.0337 -0.0100 0.0018 144 LEU A CB 1200 C CG . LEU A 144 ? 0.1588 0.2153 0.2009 0.0439 -0.0027 0.0179 144 LEU A CG 1201 C CD1 . LEU A 144 ? 0.1957 0.2915 0.2477 0.0490 0.0020 0.0365 144 LEU A CD1 1202 C CD2 . LEU A 144 ? 0.2131 0.2438 0.2647 0.0518 0.0131 0.0213 144 LEU A CD2 1203 N N . PHE A 145 ? 0.2394 0.2317 0.2410 0.0205 -0.0171 -0.0183 145 PHE A N 1204 C CA . PHE A 145 ? 0.1761 0.1611 0.1661 0.0154 -0.0211 -0.0230 145 PHE A CA 1205 C C . PHE A 145 ? 0.2032 0.1883 0.1898 0.0151 -0.0181 -0.0219 145 PHE A C 1206 O O . PHE A 145 ? 0.1990 0.1941 0.1936 0.0189 -0.0118 -0.0155 145 PHE A O 1207 C CB . PHE A 145 ? 0.2138 0.1918 0.1954 0.0067 -0.0193 -0.0287 145 PHE A CB 1208 C CG . PHE A 145 ? 0.1704 0.1587 0.1552 0.0015 -0.0243 -0.0283 145 PHE A CG 1209 C CD1 . PHE A 145 ? 0.1935 0.2023 0.1787 0.0018 -0.0335 -0.0205 145 PHE A CD1 1210 C CD2 . PHE A 145 ? 0.1678 0.1489 0.1586 -0.0013 -0.0167 -0.0307 145 PHE A CD2 1211 C CE1 . PHE A 145 ? 0.2165 0.2463 0.2090 -0.0021 -0.0382 -0.0145 145 PHE A CE1 1212 C CE2 . PHE A 145 ? 0.2086 0.2039 0.2039 -0.0086 -0.0217 -0.0294 145 PHE A CE2 1213 C CZ . PHE A 145 ? 0.2319 0.2554 0.2285 -0.0095 -0.0340 -0.0209 145 PHE A CZ 1214 N N . ARG A 146 ? 0.2102 0.1901 0.1878 0.0123 -0.0210 -0.0238 146 ARG A N 1215 C CA A ARG A 146 ? 0.2389 0.2177 0.2125 0.0105 -0.0177 -0.0230 146 ARG A CA 1216 C CA B ARG A 146 ? 0.2356 0.2143 0.2091 0.0104 -0.0178 -0.0230 146 ARG A CA 1217 C C . ARG A 146 ? 0.2773 0.2490 0.2399 0.0090 -0.0184 -0.0240 146 ARG A C 1218 O O . ARG A 146 ? 0.2521 0.2287 0.2116 0.0087 -0.0228 -0.0221 146 ARG A O 1219 C CB A ARG A 146 ? 0.2175 0.2018 0.1905 0.0045 -0.0174 -0.0230 146 ARG A CB 1220 C CB B ARG A 146 ? 0.2163 0.1997 0.1887 0.0043 -0.0174 -0.0232 146 ARG A CB 1221 C CG A ARG A 146 ? 0.2264 0.1938 0.1914 0.0028 -0.0145 -0.0260 146 ARG A CG 1222 C CG B ARG A 146 ? 0.2434 0.2107 0.2087 0.0031 -0.0146 -0.0263 146 ARG A CG 1223 C CD A ARG A 146 ? 0.2871 0.2514 0.2435 -0.0121 -0.0079 -0.0326 146 ARG A CD 1224 C CD B ARG A 146 ? 0.3294 0.2946 0.2860 -0.0119 -0.0082 -0.0334 146 ARG A CD 1225 N NE A ARG A 146 ? 0.3769 0.3109 0.3222 -0.0131 0.0053 -0.0367 146 ARG A NE 1226 N NE B ARG A 146 ? 0.3888 0.3260 0.3345 -0.0131 0.0041 -0.0381 146 ARG A NE 1227 C CZ A ARG A 146 ? 0.4297 0.3353 0.3668 -0.0126 0.0202 -0.0354 146 ARG A CZ 1228 C CZ B ARG A 146 ? 0.4656 0.3967 0.3976 -0.0293 0.0122 -0.0492 146 ARG A CZ 1229 N NH1 A ARG A 146 ? 0.3568 0.2654 0.2954 -0.0134 0.0190 -0.0318 146 ARG A NH1 1230 N NH1 B ARG A 146 ? 0.4931 0.4588 0.4234 -0.0470 0.0041 -0.0538 146 ARG A NH1 1231 N NH2 A ARG A 146 ? 0.4649 0.3360 0.3927 -0.0092 0.0408 -0.0354 146 ARG A NH2 1232 N NH2 B ARG A 146 ? 0.4096 0.3036 0.3287 -0.0280 0.0314 -0.0534 146 ARG A NH2 1233 N N . LYS A 147 ? 0.2324 0.2011 0.1904 0.0083 -0.0139 -0.0233 147 LYS A N 1234 C CA . LYS A 147 ? 0.2919 0.2589 0.2369 0.0058 -0.0135 -0.0237 147 LYS A CA 1235 C C . LYS A 147 ? 0.2346 0.1985 0.1781 0.0073 -0.0081 -0.0202 147 LYS A C 1236 O O . LYS A 147 ? 0.2243 0.1912 0.1765 0.0086 -0.0033 -0.0177 147 LYS A O 1237 C CB . LYS A 147 ? 0.2409 0.2011 0.1737 -0.0016 -0.0080 -0.0326 147 LYS A CB 1238 C CG . LYS A 147 ? 0.2925 0.2641 0.2056 -0.0134 -0.0115 -0.0359 147 LYS A CG 1239 C CD . LYS A 147 ? 0.2781 0.2345 0.1706 -0.0305 -0.0003 -0.0520 147 LYS A CD 1240 C CE . LYS A 147 ? 0.3880 0.3723 0.2576 -0.0530 -0.0080 -0.0574 147 LYS A CE 1241 N NZ . LYS A 147 ? 0.3460 0.3438 0.1995 -0.0558 -0.0086 -0.0539 147 LYS A NZ 1242 N N . PHE A 148 ? 0.2499 0.2157 0.1850 0.0077 -0.0084 -0.0158 148 PHE A N 1243 C CA . PHE A 148 ? 0.2514 0.2138 0.1849 0.0088 -0.0023 -0.0115 148 PHE A CA 1244 C C . PHE A 148 ? 0.3045 0.2698 0.2210 0.0070 0.0004 -0.0123 148 PHE A C 1245 O O . PHE A 148 ? 0.3380 0.3178 0.2439 0.0033 -0.0051 -0.0109 148 PHE A O 1246 C CB . PHE A 148 ? 0.2038 0.1609 0.1410 0.0110 0.0011 -0.0035 148 PHE A CB 1247 C CG . PHE A 148 ? 0.2714 0.2187 0.2160 0.0053 0.0042 -0.0077 148 PHE A CG 1248 C CD1 . PHE A 148 ? 0.2420 0.1885 0.1890 -0.0062 0.0094 -0.0105 148 PHE A CD1 1249 C CD2 . PHE A 148 ? 0.2432 0.1858 0.1898 0.0078 0.0032 -0.0088 148 PHE A CD2 1250 C CE1 . PHE A 148 ? 0.2697 0.2109 0.2156 -0.0205 0.0134 -0.0184 148 PHE A CE1 1251 C CE2 . PHE A 148 ? 0.2393 0.1695 0.1856 -0.0012 0.0092 -0.0158 148 PHE A CE2 1252 C CZ . PHE A 148 ? 0.3404 0.2698 0.2837 -0.0180 0.0143 -0.0225 148 PHE A CZ 1253 N N . HIS A 149 ? 0.2634 0.2216 0.1766 0.0082 0.0096 -0.0127 149 HIS A N 1254 C CA . HIS A 149 ? 0.2429 0.2004 0.1356 0.0053 0.0157 -0.0141 149 HIS A CA 1255 C C . HIS A 149 ? 0.3295 0.2886 0.2290 0.0117 0.0207 -0.0031 149 HIS A C 1256 O O . HIS A 149 ? 0.2997 0.2586 0.2169 0.0143 0.0233 0.0019 149 HIS A O 1257 C CB . HIS A 149 ? 0.2757 0.2129 0.1529 0.0010 0.0311 -0.0258 149 HIS A CB 1258 C CG . HIS A 149 ? 0.3179 0.2505 0.1775 -0.0135 0.0303 -0.0405 149 HIS A CG 1259 N ND1 . HIS A 149 ? 0.2961 0.2240 0.1213 -0.0323 0.0380 -0.0549 149 HIS A ND1 1260 C CD2 . HIS A 149 ? 0.2467 0.1817 0.1160 -0.0163 0.0231 -0.0439 149 HIS A CD2 1261 C CE1 . HIS A 149 ? 0.3921 0.3204 0.2064 -0.0491 0.0358 -0.0675 149 HIS A CE1 1262 N NE2 . HIS A 149 ? 0.3017 0.2338 0.1447 -0.0372 0.0266 -0.0596 149 HIS A NE2 1263 N N . TYR A 150 ? 0.2695 0.2366 0.1546 0.0115 0.0221 0.0019 150 TYR A N 1264 C CA . TYR A 150 ? 0.3239 0.2922 0.2165 0.0178 0.0277 0.0143 150 TYR A CA 1265 C C . TYR A 150 ? 0.3443 0.3134 0.2175 0.0179 0.0371 0.0147 150 TYR A C 1266 O O . TYR A 150 ? 0.3017 0.2795 0.1490 0.0101 0.0365 0.0079 150 TYR A O 1267 C CB . TYR A 150 ? 0.3093 0.2869 0.2085 0.0233 0.0253 0.0287 150 TYR A CB 1268 C CG . TYR A 150 ? 0.2816 0.2506 0.1956 0.0239 0.0227 0.0288 150 TYR A CG 1269 C CD1 . TYR A 150 ? 0.2896 0.2398 0.2165 0.0193 0.0294 0.0262 150 TYR A CD1 1270 C CD2 . TYR A 150 ? 0.3242 0.3071 0.2366 0.0260 0.0153 0.0314 150 TYR A CD2 1271 C CE1 . TYR A 150 ? 0.2610 0.1981 0.1945 0.0166 0.0312 0.0228 150 TYR A CE1 1272 C CE2 . TYR A 150 ? 0.3096 0.2811 0.2342 0.0288 0.0169 0.0324 150 TYR A CE2 1273 C CZ . TYR A 150 ? 0.3439 0.2882 0.2768 0.0241 0.0261 0.0265 150 TYR A CZ 1274 O OH . TYR A 150 ? 0.2711 0.1986 0.2093 0.0234 0.0316 0.0241 150 TYR A OH 1275 N N . LEU A 151 ? 0.3040 0.2681 0.1874 0.0234 0.0465 0.0225 151 LEU A N 1276 C CA . LEU A 151 ? 0.3012 0.2644 0.1674 0.0261 0.0582 0.0254 151 LEU A CA 1277 C C . LEU A 151 ? 0.2929 0.2625 0.1744 0.0322 0.0628 0.0419 151 LEU A C 1278 O O . LEU A 151 ? 0.2917 0.2614 0.1934 0.0331 0.0680 0.0478 151 LEU A O 1279 C CB . LEU A 151 ? 0.2956 0.2404 0.1554 0.0286 0.0750 0.0186 151 LEU A CB 1280 C CG . LEU A 151 ? 0.3371 0.2737 0.1804 0.0339 0.0942 0.0226 151 LEU A CG 1281 C CD1 . LEU A 151 ? 0.4203 0.3592 0.2239 0.0226 0.0945 0.0120 151 LEU A CD1 1282 C CD2 . LEU A 151 ? 0.3996 0.3124 0.2428 0.0429 0.1197 0.0223 151 LEU A CD2 1283 N N . PRO A 152 ? 0.3344 0.3153 0.2076 0.0353 0.0621 0.0523 152 PRO A N 1284 C CA . PRO A 152 ? 0.3903 0.3720 0.2750 0.0412 0.0717 0.0684 152 PRO A CA 1285 C C . PRO A 152 ? 0.4339 0.4135 0.3109 0.0440 0.0834 0.0685 152 PRO A C 1286 O O . PRO A 152 ? 0.4091 0.3849 0.2599 0.0427 0.0881 0.0580 152 PRO A O 1287 C CB . PRO A 152 ? 0.4786 0.4791 0.3522 0.0482 0.0715 0.0836 152 PRO A CB 1288 C CG . PRO A 152 ? 0.4908 0.5107 0.3403 0.0413 0.0604 0.0734 152 PRO A CG 1289 C CD . PRO A 152 ? 0.3916 0.3934 0.2472 0.0336 0.0537 0.0546 152 PRO A CD 1290 N N . PHE A 153 ? 0.3743 0.3548 0.2722 0.0454 0.0914 0.0798 153 PHE A N 1291 C CA . PHE A 153 ? 0.3829 0.3658 0.2792 0.0518 0.1055 0.0860 153 PHE A CA 1292 C C . PHE A 153 ? 0.4227 0.4160 0.3396 0.0517 0.1130 0.1036 153 PHE A C 1293 O O . PHE A 153 ? 0.4062 0.3990 0.3401 0.0418 0.1095 0.1070 153 PHE A O 1294 C CB . PHE A 153 ? 0.3718 0.3547 0.2788 0.0537 0.1105 0.0829 153 PHE A CB 1295 C CG . PHE A 153 ? 0.3178 0.3237 0.2595 0.0455 0.1043 0.0923 153 PHE A CG 1296 C CD1 . PHE A 153 ? 0.2920 0.3250 0.2563 0.0495 0.1149 0.1113 153 PHE A CD1 1297 C CD2 . PHE A 153 ? 0.3198 0.3259 0.2697 0.0317 0.0894 0.0834 153 PHE A CD2 1298 C CE1 . PHE A 153 ? 0.3257 0.3960 0.3193 0.0346 0.1071 0.1209 153 PHE A CE1 1299 C CE2 . PHE A 153 ? 0.3358 0.3669 0.3097 0.0161 0.0845 0.0881 153 PHE A CE2 1300 C CZ . PHE A 153 ? 0.3137 0.3820 0.3089 0.0150 0.0914 0.1065 153 PHE A CZ 1301 N N . LEU A 154 ? 0.4901 0.3899 0.2744 0.0444 0.1346 0.0002 154 LEU A N 1302 C CA . LEU A 154 ? 0.4924 0.3823 0.2833 0.0392 0.1565 0.0134 154 LEU A CA 1303 C C . LEU A 154 ? 0.4402 0.3548 0.2942 0.0340 0.1659 0.0188 154 LEU A C 1304 O O . LEU A 154 ? 0.4210 0.3423 0.2900 0.0387 0.1846 0.0150 154 LEU A O 1305 C CB . LEU A 154 ? 0.5032 0.3813 0.2760 0.0397 0.1684 0.0128 154 LEU A CB 1306 C CG . LEU A 154 ? 0.6258 0.4875 0.3907 0.0335 0.1839 0.0262 154 LEU A CG 1307 C CD1 . LEU A 154 ? 0.7182 0.5634 0.4558 0.0316 0.1659 0.0311 154 LEU A CD1 1308 C CD2 . LEU A 154 ? 0.5975 0.4475 0.3406 0.0370 0.1943 0.0245 154 LEU A CD2 1309 N N . PRO A 155 ? 0.4693 0.3975 0.3599 0.0251 0.1517 0.0277 155 PRO A N 1310 C CA . PRO A 155 ? 0.3511 0.3097 0.3050 0.0213 0.1536 0.0331 155 PRO A CA 1311 C C . PRO A 155 ? 0.4429 0.4115 0.4252 0.0186 0.1839 0.0412 155 PRO A C 1312 O O . PRO A 155 ? 0.3936 0.3514 0.3662 0.0102 0.1962 0.0495 155 PRO A O 1313 C CB . PRO A 155 ? 0.3905 0.3559 0.3648 0.0100 0.1316 0.0410 155 PRO A CB 1314 C CG . PRO A 155 ? 0.3951 0.3327 0.3141 0.0125 0.1136 0.0365 155 PRO A CG 1315 C CD . PRO A 155 ? 0.5272 0.4415 0.3981 0.0190 0.1323 0.0328 155 PRO A CD 1316 N N . SER A 156 ? 0.4134 0.4010 0.4289 0.0266 0.1970 0.0394 156 SER A N 1317 C CA . SER A 156 ? 0.4338 0.4375 0.4834 0.0271 0.2265 0.0482 156 SER A CA 1318 C C . SER A 156 ? 0.3855 0.4225 0.4927 0.0337 0.2268 0.0513 156 SER A C 1319 O O . SER A 156 ? 0.4731 0.5126 0.5832 0.0399 0.2086 0.0444 156 SER A O 1320 C CB . SER A 156 ? 0.6036 0.5828 0.6117 0.0362 0.2455 0.0401 156 SER A CB 1321 O OG . SER A 156 ? 0.7126 0.6847 0.7083 0.0473 0.2389 0.0270 156 SER A OG 1322 N N . THR A 157 ? 0.4092 0.4704 0.5584 0.0327 0.2425 0.0613 157 THR A N 1323 C CA . THR A 157 ? 0.4619 0.5528 0.6594 0.0411 0.2387 0.0644 157 THR A CA 1324 C C . THR A 157 ? 0.5023 0.5727 0.6750 0.0574 0.2474 0.0538 157 THR A C 1325 O O . THR A 157 ? 0.5290 0.6139 0.7294 0.0671 0.2455 0.0552 157 THR A O 1326 C CB . THR A 157 ? 0.5186 0.6425 0.7633 0.0344 0.2478 0.0779 157 THR A CB 1327 O OG1 . THR A 157 ? 0.5342 0.6421 0.7550 0.0368 0.2707 0.0777 157 THR A OG1 1328 C CG2 . THR A 157 ? 0.5424 0.6842 0.8117 0.0135 0.2370 0.0881 157 THR A CG2 1329 N N . GLU A 158 ? 0.5236 0.5588 0.6418 0.0593 0.2556 0.0437 158 GLU A N 1330 C CA . GLU A 158 ? 0.5931 0.6052 0.6837 0.0709 0.2635 0.0332 158 GLU A CA 1331 C C . GLU A 158 ? 0.5616 0.5590 0.6333 0.0751 0.2474 0.0213 158 GLU A C 1332 O O . GLU A 158 ? 0.6027 0.5914 0.6738 0.0839 0.2506 0.0163 158 GLU A O 1333 C CB . GLU A 158 ? 0.6932 0.6759 0.7333 0.0696 0.2746 0.0270 158 GLU A CB 1334 C CG . GLU A 158 ? 0.8561 0.8487 0.9080 0.0644 0.2914 0.0387 158 GLU A CG 1335 C CD . GLU A 158 ? 0.9728 0.9885 1.0666 0.0716 0.3080 0.0479 158 GLU A CD 1336 O OE1 . GLU A 158 ? 1.0919 1.0919 1.1655 0.0798 0.3243 0.0450 158 GLU A OE1 1337 O OE2 . GLU A 158 ? 0.9634 1.0140 1.1096 0.0693 0.3037 0.0581 158 GLU A OE2 1338 N N . ASP A 159 ? 0.4040 0.3976 0.4591 0.0686 0.2310 0.0171 159 ASP A N 1339 C CA . ASP A 159 ? 0.3996 0.3780 0.4298 0.0706 0.2153 0.0047 159 ASP A CA 1340 C C . ASP A 159 ? 0.4762 0.4757 0.5425 0.0725 0.2000 0.0091 159 ASP A C 1341 O O . ASP A 159 ? 0.5116 0.5341 0.6076 0.0683 0.1935 0.0190 159 ASP A O 1342 C CB . ASP A 159 ? 0.4365 0.3958 0.4162 0.0640 0.2043 -0.0041 159 ASP A CB 1343 C CG . ASP A 159 ? 0.5989 0.5374 0.5392 0.0627 0.2138 -0.0091 159 ASP A CG 1344 O OD1 . ASP A 159 ? 0.6069 0.5353 0.5426 0.0676 0.2249 -0.0134 159 ASP A OD1 1345 O OD2 . ASP A 159 ? 0.6881 0.6192 0.6005 0.0576 0.2098 -0.0080 159 ASP A OD2 1346 N N . VAL A 160 ? 0.3915 0.3820 0.4545 0.0779 0.1935 0.0020 160 VAL A N 1347 C CA . VAL A 160 ? 0.2943 0.2977 0.3782 0.0798 0.1755 0.0036 160 VAL A CA 1348 C C . VAL A 160 ? 0.2947 0.2760 0.3358 0.0767 0.1636 -0.0106 160 VAL A C 1349 O O . VAL A 160 ? 0.3499 0.3077 0.3519 0.0735 0.1685 -0.0218 160 VAL A O 1350 C CB . VAL A 160 ? 0.3245 0.3388 0.4436 0.0883 0.1759 0.0100 160 VAL A CB 1351 C CG1 . VAL A 160 ? 0.3876 0.4269 0.5465 0.0910 0.1867 0.0234 160 VAL A CG1 1352 C CG2 . VAL A 160 ? 0.4213 0.4059 0.5123 0.0925 0.1849 -0.0003 160 VAL A CG2 1353 N N . TYR A 161 ? 0.2664 0.2580 0.3152 0.0755 0.1428 -0.0093 161 TYR A N 1354 C CA . TYR A 161 ? 0.3321 0.3093 0.3430 0.0704 0.1272 -0.0210 161 TYR A CA 1355 C C . TYR A 161 ? 0.3277 0.3105 0.3573 0.0736 0.1139 -0.0196 161 TYR A C 1356 O O . TYR A 161 ? 0.2725 0.2745 0.3425 0.0792 0.1086 -0.0079 161 TYR A O 1357 C CB . TYR A 161 ? 0.2914 0.2736 0.2785 0.0626 0.1074 -0.0204 161 TYR A CB 1358 C CG . TYR A 161 ? 0.2913 0.2618 0.2483 0.0595 0.1195 -0.0226 161 TYR A CG 1359 C CD1 . TYR A 161 ? 0.3663 0.3184 0.2744 0.0574 0.1216 -0.0354 161 TYR A CD1 1360 C CD2 . TYR A 161 ? 0.3594 0.3382 0.3363 0.0582 0.1288 -0.0116 161 TYR A CD2 1361 C CE1 . TYR A 161 ? 0.3247 0.2680 0.2064 0.0545 0.1279 -0.0356 161 TYR A CE1 1362 C CE2 . TYR A 161 ? 0.4294 0.3947 0.3763 0.0557 0.1415 -0.0123 161 TYR A CE2 1363 C CZ . TYR A 161 ? 0.4441 0.3894 0.3399 0.0559 0.1428 -0.0246 161 TYR A CZ 1364 O OH . TYR A 161 ? 0.4735 0.4080 0.3423 0.0527 0.1479 -0.0237 161 TYR A OH 1365 N N . ASP A 162 ? 0.2921 0.2587 0.2916 0.0695 0.1091 -0.0314 162 ASP A N 1366 C CA . ASP A 162 ? 0.2856 0.2550 0.2951 0.0702 0.0956 -0.0304 162 ASP A CA 1367 C C . ASP A 162 ? 0.3334 0.3001 0.3072 0.0604 0.0792 -0.0404 162 ASP A C 1368 O O . ASP A 162 ? 0.3424 0.2961 0.2810 0.0538 0.0846 -0.0524 162 ASP A O 1369 C CB . ASP A 162 ? 0.3001 0.2490 0.3168 0.0762 0.1141 -0.0339 162 ASP A CB 1370 C CG . ASP A 162 ? 0.3645 0.3225 0.4179 0.0861 0.1254 -0.0216 162 ASP A CG 1371 O OD1 . ASP A 162 ? 0.2905 0.2682 0.3776 0.0924 0.1150 -0.0094 162 ASP A OD1 1372 O OD2 . ASP A 162 ? 0.3045 0.2520 0.3504 0.0863 0.1417 -0.0238 162 ASP A OD2 1373 N N . CYS A 163 ? 0.2147 0.1962 0.1976 0.0601 0.0591 -0.0349 163 CYS A N 1374 C CA . CYS A 163 ? 0.2139 0.1962 0.1695 0.0520 0.0460 -0.0432 163 CYS A CA 1375 C C . CYS A 163 ? 0.3034 0.2733 0.2675 0.0506 0.0518 -0.0456 163 CYS A C 1376 O O . CYS A 163 ? 0.2915 0.2662 0.2846 0.0585 0.0495 -0.0348 163 CYS A O 1377 C CB . CYS A 163 ? 0.2925 0.2969 0.2490 0.0536 0.0221 -0.0355 163 CYS A CB 1378 S SG . CYS A 163 ? 0.3354 0.3495 0.2624 0.0457 0.0065 -0.0435 163 CYS A SG 1379 N N . ARG A 164 ? 0.2992 0.2512 0.2368 0.0405 0.0597 -0.0595 164 ARG A N 1380 C CA . ARG A 164 ? 0.2704 0.2043 0.2110 0.0364 0.0665 -0.0627 164 ARG A CA 1381 C C . ARG A 164 ? 0.2890 0.2357 0.2157 0.0245 0.0501 -0.0667 164 ARG A C 1382 O O . ARG A 164 ? 0.3066 0.2598 0.2053 0.0130 0.0439 -0.0781 164 ARG A O 1383 C CB . ARG A 164 ? 0.3078 0.2068 0.2290 0.0316 0.0891 -0.0760 164 ARG A CB 1384 C CG . ARG A 164 ? 0.4269 0.2994 0.3475 0.0265 0.0979 -0.0796 164 ARG A CG 1385 C CD . ARG A 164 ? 0.5081 0.3428 0.4054 0.0216 0.1187 -0.0927 164 ARG A CD 1386 N NE . ARG A 164 ? 0.3955 0.2340 0.2601 0.0044 0.1097 -0.1063 164 ARG A NE 1387 C CZ . ARG A 164 ? 0.4758 0.3009 0.3225 0.0018 0.1168 -0.1125 164 ARG A CZ 1388 N NH1 . ARG A 164 ? 0.4446 0.2513 0.3002 0.0139 0.1343 -0.1073 164 ARG A NH1 1389 N NH2 . ARG A 164 ? 0.5207 0.3539 0.3421 -0.0114 0.1056 -0.1225 164 ARG A NH2 1390 N N . VAL A 165 ? 0.2425 0.1954 0.1889 0.0279 0.0432 -0.0567 165 VAL A N 1391 C CA . VAL A 165 ? 0.2807 0.2502 0.2184 0.0179 0.0285 -0.0576 165 VAL A CA 1392 C C . VAL A 165 ? 0.3360 0.2828 0.2742 0.0086 0.0384 -0.0604 165 VAL A C 1393 O O . VAL A 165 ? 0.3374 0.2678 0.2952 0.0184 0.0473 -0.0508 165 VAL A O 1394 C CB . VAL A 165 ? 0.2432 0.2412 0.1977 0.0292 0.0100 -0.0428 165 VAL A CB 1395 C CG1 . VAL A 165 ? 0.2354 0.2525 0.1822 0.0211 -0.0029 -0.0422 165 VAL A CG1 1396 C CG2 . VAL A 165 ? 0.2262 0.2408 0.1746 0.0360 0.0005 -0.0412 165 VAL A CG2 1397 N N . GLU A 166 ? 0.2764 0.2218 0.1925 -0.0108 0.0373 -0.0733 166 GLU A N 1398 C CA . GLU A 166 ? 0.3250 0.2495 0.2394 -0.0240 0.0451 -0.0760 166 GLU A CA 1399 C C . GLU A 166 ? 0.3463 0.3034 0.2642 -0.0323 0.0288 -0.0706 166 GLU A C 1400 O O . GLU A 166 ? 0.3172 0.3078 0.2246 -0.0379 0.0142 -0.0748 166 GLU A O 1401 C CB . GLU A 166 ? 0.4033 0.2989 0.2898 -0.0441 0.0573 -0.0959 166 GLU A CB 1402 C CG . GLU A 166 ? 0.5158 0.3757 0.3924 -0.0368 0.0762 -0.1035 166 GLU A CG 1403 C CD . GLU A 166 ? 0.6832 0.5242 0.5240 -0.0569 0.0818 -0.1255 166 GLU A CD 1404 O OE1 . GLU A 166 ? 0.6174 0.4465 0.4443 -0.0789 0.0820 -0.1356 166 GLU A OE1 1405 O OE2 . GLU A 166 ? 0.7338 0.5781 0.5646 -0.0502 0.0829 -0.1288 166 GLU A OE2 1406 N N . HIS A 167 ? 0.3172 0.2359 0.2228 0.0138 -0.0026 -0.0866 167 HIS A N 1407 C CA . HIS A 167 ? 0.2333 0.1603 0.1297 0.0147 -0.0125 -0.0811 167 HIS A CA 1408 C C . HIS A 167 ? 0.3647 0.2569 0.2710 0.0197 -0.0123 -0.0910 167 HIS A C 1409 O O . HIS A 167 ? 0.3081 0.1785 0.2399 0.0269 -0.0051 -0.0821 167 HIS A O 1410 C CB . HIS A 167 ? 0.2538 0.1878 0.1351 0.0229 -0.0215 -0.0599 167 HIS A CB 1411 C CG . HIS A 167 ? 0.3168 0.2502 0.1816 0.0250 -0.0224 -0.0507 167 HIS A CG 1412 N ND1 . HIS A 167 ? 0.2989 0.1983 0.1375 0.0318 -0.0283 -0.0447 167 HIS A ND1 1413 C CD2 . HIS A 167 ? 0.2798 0.2315 0.1426 0.0235 -0.0161 -0.0444 167 HIS A CD2 1414 C CE1 . HIS A 167 ? 0.3729 0.2725 0.1945 0.0342 -0.0210 -0.0342 167 HIS A CE1 1415 N NE2 . HIS A 167 ? 0.3297 0.2622 0.1682 0.0318 -0.0144 -0.0350 167 HIS A NE2 1416 N N . TRP A 168 ? 0.2850 0.1820 0.1934 0.0119 -0.0133 -0.0944 168 TRP A N 1417 C CA . TRP A 168 ? 0.3870 0.2645 0.3313 0.0050 -0.0002 -0.0883 168 TRP A CA 1418 C C . TRP A 168 ? 0.3689 0.2334 0.3254 0.0187 0.0000 -0.0559 168 TRP A C 1419 O O . TRP A 168 ? 0.3228 0.1675 0.3140 0.0194 0.0146 -0.0454 168 TRP A O 1420 C CB . TRP A 168 ? 0.3556 0.2505 0.3086 -0.0099 -0.0006 -0.0911 168 TRP A CB 1421 C CG . TRP A 168 ? 0.3675 0.2815 0.3127 -0.0324 -0.0063 -0.1185 168 TRP A CG 1422 C CD1 . TRP A 168 ? 0.4054 0.2969 0.3422 -0.0465 0.0004 -0.1411 168 TRP A CD1 1423 C CD2 . TRP A 168 ? 0.3870 0.3492 0.3288 -0.0422 -0.0208 -0.1151 168 TRP A CD2 1424 N NE1 . TRP A 168 ? 0.4337 0.3546 0.3557 -0.0656 -0.0145 -0.1485 168 TRP A NE1 1425 C CE2 . TRP A 168 ? 0.4523 0.4238 0.3808 -0.0694 -0.0288 -0.1424 168 TRP A CE2 1426 C CE3 . TRP A 168 ? 0.3095 0.3063 0.2581 -0.0300 -0.0242 -0.0875 168 TRP A CE3 1427 C CZ2 . TRP A 168 ? 0.4293 0.4571 0.3581 -0.0865 -0.0483 -0.1381 168 TRP A CZ2 1428 C CZ3 . TRP A 168 ? 0.2737 0.3251 0.2319 -0.0410 -0.0362 -0.0813 168 TRP A CZ3 1429 C CH2 . TRP A 168 ? 0.3078 0.3817 0.2594 -0.0705 -0.0523 -0.1049 168 TRP A CH2 1430 N N . GLY A 169 ? 0.2762 0.1490 0.1992 0.0270 -0.0152 -0.0387 169 GLY A N 1431 C CA . GLY A 169 ? 0.2873 0.1507 0.2087 0.0320 -0.0225 -0.0060 169 GLY A CA 1432 C C . GLY A 169 ? 0.3370 0.2047 0.2893 0.0374 -0.0261 0.0087 169 GLY A C 1433 O O . GLY A 169 ? 0.3403 0.2112 0.3036 0.0391 -0.0358 0.0430 169 GLY A O 1434 N N . LEU A 170 ? 0.3209 0.1911 0.2882 0.0398 -0.0176 -0.0125 170 LEU A N 1435 C CA . LEU A 170 ? 0.3505 0.2261 0.3573 0.0486 -0.0135 0.0049 170 LEU A CA 1436 C C . LEU A 170 ? 0.4492 0.3004 0.5099 0.0563 0.0205 0.0032 170 LEU A C 1437 O O . LEU A 170 ? 0.4887 0.3149 0.5396 0.0481 0.0393 -0.0300 170 LEU A O 1438 C CB . LEU A 170 ? 0.3171 0.2005 0.3023 0.0490 -0.0173 -0.0151 170 LEU A CB 1439 C CG . LEU A 170 ? 0.3696 0.2672 0.3006 0.0418 -0.0427 -0.0125 170 LEU A CG 1440 C CD1 . LEU A 170 ? 0.3436 0.2424 0.2509 0.0443 -0.0380 -0.0398 170 LEU A CD1 1441 C CD2 . LEU A 170 ? 0.3983 0.3138 0.3412 0.0361 -0.0642 0.0278 170 LEU A CD2 1442 N N . ASP A 171 ? 0.4174 0.2746 0.5338 0.0700 0.0303 0.0418 171 ASP A N 1443 C CA . ASP A 171 ? 0.4937 0.3202 0.6593 0.0804 0.0731 0.0452 171 ASP A CA 1444 C C . ASP A 171 ? 0.5126 0.3266 0.6703 0.0793 0.0950 0.0190 171 ASP A C 1445 O O . ASP A 171 ? 0.5995 0.3846 0.7518 0.0720 0.1263 -0.0002 171 ASP A O 1446 C CB . ASP A 171 ? 0.5300 0.3882 0.7503 0.0915 0.0751 0.0988 171 ASP A CB 1447 C CG . ASP A 171 ? 0.7599 0.6235 0.9772 0.0888 0.0618 0.1205 171 ASP A CG 1448 O OD1 . ASP A 171 ? 0.8216 0.6511 1.0182 0.0818 0.0753 0.0940 171 ASP A OD1 1449 O OD2 . ASP A 171 ? 0.8417 0.7457 1.0719 0.0891 0.0368 0.1623 171 ASP A OD2 1450 N N . GLU A 172 ? 0.3487 0.1826 0.4999 0.0843 0.0781 0.0209 172 GLU A N 1451 C CA . GLU A 172 ? 0.3656 0.1888 0.4995 0.0825 0.0954 -0.0027 172 GLU A CA 1452 C C . GLU A 172 ? 0.3533 0.1906 0.4478 0.0805 0.0689 -0.0211 172 GLU A C 1453 O O . GLU A 172 ? 0.3701 0.2377 0.4510 0.0761 0.0348 -0.0065 172 GLU A O 1454 C CB . GLU A 172 ? 0.4541 0.2914 0.6473 0.0958 0.1196 0.0350 172 GLU A CB 1455 C CG . GLU A 172 ? 0.5904 0.4812 0.8324 0.1047 0.0921 0.0845 172 GLU A CG 1456 C CD . GLU A 172 ? 0.8046 0.7212 1.1181 0.1140 0.1177 0.1302 172 GLU A CD 1457 O OE1 . GLU A 172 ? 0.9019 0.8155 1.2449 0.1177 0.1370 0.1498 172 GLU A OE1 1458 O OE2 . GLU A 172 ? 0.8499 0.7902 1.1929 0.1177 0.1222 0.1484 172 GLU A OE2 1459 N N . PRO A 173 ? 0.3854 0.2162 0.4424 0.0741 0.0748 -0.0491 173 PRO A N 1460 C CA . PRO A 173 ? 0.3999 0.2490 0.4165 0.0720 0.0514 -0.0649 173 PRO A CA 1461 C C . PRO A 173 ? 0.3312 0.2049 0.3826 0.0830 0.0399 -0.0316 173 PRO A C 1462 O O . PRO A 173 ? 0.3226 0.2075 0.4405 0.0953 0.0531 0.0054 173 PRO A O 1463 C CB . PRO A 173 ? 0.4693 0.3153 0.4631 0.0671 0.0598 -0.0822 173 PRO A CB 1464 C CG . PRO A 173 ? 0.5620 0.3785 0.5554 0.0584 0.0817 -0.0897 173 PRO A CG 1465 C CD . PRO A 173 ? 0.4679 0.2736 0.5129 0.0665 0.1011 -0.0640 173 PRO A CD 1466 N N . LEU A 174 ? 0.3064 0.2025 0.3104 0.0721 0.0084 -0.0368 174 LEU A N 1467 C CA . LEU A 174 ? 0.2780 0.2066 0.2931 0.0662 -0.0158 -0.0059 174 LEU A CA 1468 C C . LEU A 174 ? 0.2890 0.2147 0.2882 0.0704 -0.0066 -0.0218 174 LEU A C 1469 O O . LEU A 174 ? 0.3608 0.2698 0.3016 0.0699 -0.0034 -0.0562 174 LEU A O 1470 C CB . LEU A 174 ? 0.3008 0.2367 0.2576 0.0480 -0.0477 -0.0043 174 LEU A CB 1471 C CG . LEU A 174 ? 0.4213 0.3800 0.3664 0.0284 -0.0783 0.0263 174 LEU A CG 1472 C CD1 . LEU A 174 ? 0.4502 0.4444 0.4734 0.0276 -0.0884 0.0759 174 LEU A CD1 1473 C CD2 . LEU A 174 ? 0.4566 0.3989 0.3295 0.0108 -0.0952 0.0217 174 LEU A CD2 1474 N N . LEU A 175 ? 0.2825 0.2280 0.3387 0.0760 -0.0008 0.0077 175 LEU A N 1475 C CA . LEU A 175 ? 0.3311 0.2733 0.3768 0.0803 0.0105 -0.0041 175 LEU A CA 1476 C C . LEU A 175 ? 0.3230 0.3005 0.3697 0.0603 -0.0211 0.0228 175 LEU A C 1477 O O . LEU A 175 ? 0.2893 0.3056 0.3943 0.0507 -0.0397 0.0680 175 LEU A O 1478 C CB . LEU A 175 ? 0.3336 0.2629 0.4436 0.1026 0.0520 0.0071 175 LEU A CB 1479 C CG . LEU A 175 ? 0.4077 0.3033 0.4705 0.0985 0.0723 -0.0316 175 LEU A CG 1480 C CD1 . LEU A 175 ? 0.4226 0.3029 0.4969 0.0972 0.0817 -0.0296 175 LEU A CD1 1481 C CD2 . LEU A 175 ? 0.5055 0.3941 0.5858 0.1019 0.0975 -0.0243 175 LEU A CD2 1482 N N . LYS A 176 ? 0.2704 0.2342 0.2513 0.0515 -0.0265 -0.0026 176 LYS A N 1483 C CA . LYS A 176 ? 0.2625 0.2468 0.2331 0.0266 -0.0506 0.0168 176 LYS A CA 1484 C C . LYS A 176 ? 0.2786 0.2574 0.2607 0.0372 -0.0270 0.0078 176 LYS A C 1485 O O . LYS A 176 ? 0.2967 0.2424 0.2324 0.0541 -0.0028 -0.0284 176 LYS A O 1486 C CB . LYS A 176 ? 0.4087 0.3693 0.2850 0.0040 -0.0703 -0.0008 176 LYS A CB 1487 C CG . LYS A 176 ? 0.5170 0.4837 0.3811 -0.0135 -0.0969 0.0180 176 LYS A CG 1488 C CD . LYS A 176 ? 0.5091 0.5206 0.4299 -0.0375 -0.1257 0.0658 176 LYS A CD 1489 C CE . LYS A 176 ? 0.5544 0.5813 0.5097 -0.0342 -0.1326 0.0874 176 LYS A CE 1490 N NZ . LYS A 176 ? 0.6471 0.6569 0.5541 -0.0571 -0.1343 0.0803 176 LYS A NZ 1491 N N . HIS A 177 ? 0.3049 0.3211 0.3532 0.0264 -0.0352 0.0456 177 HIS A N 1492 C CA . HIS A 177 ? 0.2736 0.2916 0.3618 0.0403 -0.0073 0.0490 177 HIS A CA 1493 C C . HIS A 177 ? 0.3388 0.3505 0.3747 0.0151 -0.0190 0.0393 177 HIS A C 1494 O O . HIS A 177 ? 0.3135 0.3313 0.3052 -0.0219 -0.0537 0.0462 177 HIS A O 1495 C CB . HIS A 177 ? 0.2665 0.3379 0.4748 0.0435 -0.0070 0.1066 177 HIS A CB 1496 C CG . HIS A 177 ? 0.3651 0.4353 0.6356 0.0680 0.0349 0.1172 177 HIS A CG 1497 N ND1 . HIS A 177 ? 0.3767 0.4002 0.6529 0.1060 0.0872 0.0955 177 HIS A ND1 1498 C CD2 . HIS A 177 ? 0.3382 0.4451 0.6679 0.0579 0.0346 0.1498 177 HIS A CD2 1499 C CE1 . HIS A 177 ? 0.3750 0.3981 0.6875 0.1119 0.1160 0.1092 177 HIS A CE1 1500 N NE2 . HIS A 177 ? 0.3262 0.4070 0.6990 0.0950 0.0903 0.1482 177 HIS A NE2 1501 N N . TRP A 178 ? 0.3420 0.3326 0.3748 0.0335 0.0141 0.0221 178 TRP A N 1502 C CA . TRP A 178 ? 0.3113 0.2974 0.3151 0.0115 0.0112 0.0201 178 TRP A CA 1503 C C . TRP A 178 ? 0.3504 0.3431 0.4198 0.0330 0.0465 0.0321 178 TRP A C 1504 O O . TRP A 178 ? 0.2814 0.2462 0.3568 0.0704 0.0853 0.0145 178 TRP A O 1505 C CB . TRP A 178 ? 0.3728 0.3054 0.2631 0.0127 0.0214 -0.0243 178 TRP A CB 1506 C CG . TRP A 178 ? 0.3903 0.3075 0.2448 -0.0122 0.0241 -0.0263 178 TRP A CG 1507 C CD1 . TRP A 178 ? 0.5134 0.4208 0.3159 -0.0581 -0.0021 -0.0212 178 TRP A CD1 1508 C CD2 . TRP A 178 ? 0.3791 0.2820 0.2437 0.0037 0.0580 -0.0334 178 TRP A CD2 1509 N NE1 . TRP A 178 ? 0.4879 0.3742 0.2676 -0.0736 0.0141 -0.0264 178 TRP A NE1 1510 C CE2 . TRP A 178 ? 0.4434 0.3302 0.2654 -0.0339 0.0507 -0.0325 178 TRP A CE2 1511 C CE3 . TRP A 178 ? 0.4346 0.3282 0.3312 0.0441 0.0969 -0.0416 178 TRP A CE3 1512 C CZ2 . TRP A 178 ? 0.4486 0.3165 0.2691 -0.0297 0.0809 -0.0379 178 TRP A CZ2 1513 C CZ3 . TRP A 178 ? 0.4464 0.3217 0.3390 0.0501 0.1263 -0.0457 178 TRP A CZ3 1514 C CH2 . TRP A 178 ? 0.4214 0.2869 0.2807 0.0147 0.1180 -0.0432 178 TRP A CH2 1515 N N . GLU A 179 ? 0.2873 0.3141 0.4029 0.0060 0.0342 0.0631 179 GLU A N 1516 C CA . GLU A 179 ? 0.3437 0.3710 0.5123 0.0243 0.0716 0.0729 179 GLU A CA 1517 C C . GLU A 179 ? 0.3871 0.4283 0.5492 -0.0164 0.0557 0.0844 179 GLU A C 1518 O O . GLU A 179 ? 0.4036 0.4624 0.5347 -0.0652 0.0114 0.0943 179 GLU A O 1519 C CB . GLU A 179 ? 0.2787 0.3468 0.5743 0.0494 0.0927 0.1190 179 GLU A CB 1520 C CG . GLU A 179 ? 0.2937 0.4443 0.6885 0.0183 0.0510 0.1828 179 GLU A CG 1521 C CD . GLU A 179 ? 0.3362 0.5233 0.8625 0.0536 0.0834 0.2340 179 GLU A CD 1522 O OE1 . GLU A 179 ? 0.3680 0.5393 0.8969 0.0753 0.0925 0.2331 179 GLU A OE1 1523 O OE2 . GLU A 179 ? 0.3457 0.5558 0.9468 0.0569 0.1016 0.2710 179 GLU A OE2 1524 N N . PHE A 180 ? 0.3348 0.3606 0.5181 0.0009 0.0944 0.0817 180 PHE A N 1525 C CA . PHE A 180 ? 0.4578 0.4858 0.6298 -0.0363 0.0885 0.0872 180 PHE A CA 1526 C C . PHE A 180 ? 0.4850 0.5954 0.7602 -0.0826 0.0478 0.1477 180 PHE A C 1527 O O . PHE A 180 ? 0.4177 0.5864 0.8062 -0.0659 0.0463 0.1939 180 PHE A O 1528 C CB . PHE A 180 ? 0.4868 0.4788 0.6648 -0.0006 0.1451 0.0730 180 PHE A CB 1529 C CG . PHE A 180 ? 0.5342 0.5174 0.6945 -0.0353 0.1481 0.0737 180 PHE A CG 1530 C CD1 . PHE A 180 ? 0.4816 0.4037 0.5198 -0.0522 0.1507 0.0325 180 PHE A CD1 1531 C CD2 . PHE A 180 ? 0.5791 0.6127 0.8485 -0.0499 0.1537 0.1186 180 PHE A CD2 1532 C CE1 . PHE A 180 ? 0.5031 0.4056 0.5188 -0.0860 0.1601 0.0312 180 PHE A CE1 1533 C CE2 . PHE A 180 ? 0.5983 0.6212 0.8510 -0.0867 0.1575 0.1181 180 PHE A CE2 1534 C CZ . PHE A 180 ? 0.5703 0.5228 0.6910 -0.1059 0.1613 0.0718 180 PHE A CZ 1535 N N . ASP A 181 ? 0.6563 0.7676 0.8869 -0.1421 0.0171 0.1483 181 ASP A N 1536 C CA . ASP A 181 ? 0.8187 1.0077 1.1215 -0.2065 -0.0339 0.2030 181 ASP A CA 1537 C C . ASP A 181 ? 0.8221 1.0197 1.0570 -0.2611 -0.0947 0.2056 181 ASP A C 1538 O O . ASP A 181 ? 0.8496 1.0813 1.0819 -0.3101 -0.1392 0.2305 181 ASP A O 1539 C CB . ASP A 181 ? 0.8085 1.0928 1.2855 -0.1878 -0.0330 0.2736 181 ASP A CB 1540 C CG . ASP A 181 ? 0.8389 1.1407 1.3754 -0.1892 -0.0127 0.2923 181 ASP A CG 1541 O OD1 . ASP A 181 ? 0.8750 1.2071 1.4035 -0.2414 -0.0550 0.3090 181 ASP A OD1 1542 O OD2 . ASP A 181 ? 0.8326 1.1126 1.4175 -0.1359 0.0476 0.2892 181 ASP A OD2 1543 N N . ASP B 4 ? 0.9382 0.7172 0.9298 0.0527 0.1476 -0.1385 2 ASP B N 1544 C CA . ASP B 4 ? 0.8588 0.6343 0.8308 0.0457 0.1297 -0.1377 2 ASP B CA 1545 C C . ASP B 4 ? 0.8142 0.5995 0.8176 0.0519 0.1173 -0.1276 2 ASP B C 1546 O O . ASP B 4 ? 0.8897 0.6938 0.9151 0.0566 0.1140 -0.1202 2 ASP B O 1547 C CB . ASP B 4 ? 0.8461 0.6287 0.7887 0.0382 0.1249 -0.1377 2 ASP B CB 1548 C CG . ASP B 4 ? 0.7985 0.5750 0.7133 0.0287 0.1081 -0.1411 2 ASP B CG 1549 O OD1 . ASP B 4 ? 0.7057 0.4758 0.6310 0.0274 0.0994 -0.1408 2 ASP B OD1 1550 O OD2 . ASP B 4 ? 0.8090 0.5876 0.6923 0.0226 0.1036 -0.1434 2 ASP B OD2 1551 N N . THR B 5 ? 0.6914 0.4628 0.6958 0.0517 0.1102 -0.1272 3 THR B N 1552 C CA . THR B 5 ? 0.6345 0.4103 0.6616 0.0580 0.0981 -0.1161 3 THR B CA 1553 C C . THR B 5 ? 0.5789 0.3477 0.5871 0.0484 0.0852 -0.1145 3 THR B C 1554 O O . THR B 5 ? 0.6495 0.4164 0.6706 0.0528 0.0763 -0.1047 3 THR B O 1555 C CB . THR B 5 ? 0.6689 0.4343 0.7194 0.0690 0.1010 -0.1119 3 THR B CB 1556 O OG1 . THR B 5 ? 0.6773 0.4194 0.7097 0.0626 0.1066 -0.1201 3 THR B OG1 1557 C CG2 . THR B 5 ? 0.6939 0.4717 0.7718 0.0795 0.1116 -0.1120 3 THR B CG2 1558 N N . ARG B 6 ? 0.4936 0.2591 0.4712 0.0357 0.0835 -0.1235 4 ARG B N 1559 C CA . ARG B 6 ? 0.5017 0.2663 0.4654 0.0253 0.0706 -0.1225 4 ARG B CA 1560 C C . ARG B 6 ? 0.4425 0.2287 0.4185 0.0285 0.0588 -0.1085 4 ARG B C 1561 O O . ARG B 6 ? 0.4441 0.2490 0.4273 0.0333 0.0592 -0.1044 4 ARG B O 1562 C CB . ARG B 6 ? 0.4794 0.2461 0.4113 0.0133 0.0666 -0.1333 4 ARG B CB 1563 C CG . ARG B 6 ? 0.6203 0.3714 0.5385 0.0089 0.0715 -0.1455 4 ARG B CG 1564 C CD . ARG B 6 ? 0.6584 0.4141 0.5451 -0.0004 0.0634 -0.1554 4 ARG B CD 1565 N NE . ARG B 6 ? 0.6901 0.4556 0.5610 0.0036 0.0683 -0.1541 4 ARG B NE 1566 C CZ . ARG B 6 ? 0.7235 0.4971 0.5666 -0.0011 0.0598 -0.1574 4 ARG B CZ 1567 N NH1 . ARG B 6 ? 0.6977 0.4745 0.5300 -0.0097 0.0437 -0.1634 4 ARG B NH1 1568 N NH2 . ARG B 6 ? 0.7141 0.4930 0.5426 0.0035 0.0674 -0.1540 4 ARG B NH2 1569 N N . PRO B 7 ? 0.3968 0.1824 0.3757 0.0256 0.0481 -0.0997 5 PRO B N 1570 C CA . PRO B 7 ? 0.3961 0.2036 0.3822 0.0281 0.0350 -0.0855 5 PRO B CA 1571 C C . PRO B 7 ? 0.3880 0.2148 0.3584 0.0195 0.0280 -0.0872 5 PRO B C 1572 O O . PRO B 7 ? 0.3822 0.2041 0.3333 0.0093 0.0274 -0.0968 5 PRO B O 1573 C CB . PRO B 7 ? 0.3607 0.1560 0.3460 0.0248 0.0297 -0.0782 5 PRO B CB 1574 C CG . PRO B 7 ? 0.4751 0.2470 0.4511 0.0154 0.0380 -0.0912 5 PRO B CG 1575 C CD . PRO B 7 ? 0.4055 0.1672 0.3828 0.0207 0.0503 -0.1023 5 PRO B CD 1576 N N . ARG B 8 ? 0.3146 0.1626 0.2939 0.0241 0.0221 -0.0786 6 ARG B N 1577 C CA . ARG B 8 ? 0.2989 0.1638 0.2649 0.0175 0.0158 -0.0778 6 ARG B CA 1578 C C . ARG B 8 ? 0.3584 0.2353 0.3269 0.0153 0.0030 -0.0674 6 ARG B C 1579 O O . ARG B 8 ? 0.3260 0.2025 0.3070 0.0215 -0.0010 -0.0589 6 ARG B O 1580 C CB . ARG B 8 ? 0.2904 0.1683 0.2637 0.0227 0.0218 -0.0775 6 ARG B CB 1581 C CG . ARG B 8 ? 0.3643 0.2338 0.3171 0.0196 0.0336 -0.0876 6 ARG B CG 1582 C CD . ARG B 8 ? 0.3817 0.2304 0.3341 0.0224 0.0468 -0.0977 6 ARG B CD 1583 N NE . ARG B 8 ? 0.3637 0.2004 0.2880 0.0190 0.0579 -0.1085 6 ARG B NE 1584 C CZ . ARG B 8 ? 0.3935 0.2097 0.3100 0.0203 0.0716 -0.1199 6 ARG B CZ 1585 N NH1 . ARG B 8 ? 0.3987 0.2046 0.3373 0.0254 0.0761 -0.1213 6 ARG B NH1 1586 N NH2 . ARG B 8 ? 0.5040 0.3091 0.3891 0.0177 0.0806 -0.1288 6 ARG B NH2 1587 N N . PHE B 9 ? 0.3218 0.2086 0.2768 0.0074 -0.0031 -0.0681 7 PHE B N 1588 C CA . PHE B 9 ? 0.2529 0.1513 0.2096 0.0045 -0.0130 -0.0596 7 PHE B CA 1589 C C . PHE B 9 ? 0.2392 0.1541 0.1890 0.0028 -0.0165 -0.0586 7 PHE B C 1590 O O . PHE B 9 ? 0.2704 0.1840 0.2052 -0.0008 -0.0149 -0.0653 7 PHE B O 1591 C CB . PHE B 9 ? 0.2618 0.1520 0.2131 -0.0046 -0.0157 -0.0626 7 PHE B CB 1592 C CG . PHE B 9 ? 0.3338 0.2021 0.2893 -0.0044 -0.0088 -0.0657 7 PHE B CG 1593 C CD1 . PHE B 9 ? 0.2857 0.1444 0.2490 0.0001 -0.0078 -0.0559 7 PHE B CD1 1594 C CD2 . PHE B 9 ? 0.3673 0.2216 0.3163 -0.0081 -0.0027 -0.0784 7 PHE B CD2 1595 C CE1 . PHE B 9 ? 0.3091 0.1438 0.2756 0.0012 0.0000 -0.0574 7 PHE B CE1 1596 C CE2 . PHE B 9 ? 0.4120 0.2436 0.3664 -0.0080 0.0052 -0.0818 7 PHE B CE2 1597 C CZ . PHE B 9 ? 0.3344 0.1559 0.2987 -0.0031 0.0069 -0.0705 7 PHE B CZ 1598 N N . LEU B 10 ? 0.2208 0.1490 0.1794 0.0060 -0.0212 -0.0505 8 LEU B N 1599 C CA . LEU B 10 ? 0.2449 0.1864 0.2001 0.0056 -0.0223 -0.0487 8 LEU B CA 1600 C C . LEU B 10 ? 0.2416 0.1937 0.1970 0.0026 -0.0306 -0.0425 8 LEU B C 1601 O O . LEU B 10 ? 0.2397 0.1927 0.2024 0.0044 -0.0343 -0.0373 8 LEU B O 1602 C CB . LEU B 10 ? 0.2025 0.1506 0.1736 0.0123 -0.0174 -0.0471 8 LEU B CB 1603 C CG . LEU B 10 ? 0.2486 0.2077 0.2206 0.0118 -0.0153 -0.0450 8 LEU B CG 1604 C CD1 . LEU B 10 ? 0.2281 0.1794 0.1816 0.0100 -0.0060 -0.0491 8 LEU B CD1 1605 C CD2 . LEU B 10 ? 0.2499 0.2184 0.2473 0.0171 -0.0128 -0.0445 8 LEU B CD2 1606 N N . GLU B 11 ? 0.1924 0.1513 0.1381 -0.0007 -0.0330 -0.0427 9 GLU B N 1607 C CA . GLU B 11 ? 0.2255 0.1952 0.1737 -0.0025 -0.0390 -0.0373 9 GLU B CA 1608 C C . GLU B 11 ? 0.2321 0.2088 0.1804 0.0006 -0.0363 -0.0345 9 GLU B C 1609 O O . GLU B 11 ? 0.2303 0.2030 0.1679 0.0016 -0.0314 -0.0367 9 GLU B O 1610 C CB . GLU B 11 ? 0.2089 0.1811 0.1498 -0.0081 -0.0447 -0.0403 9 GLU B CB 1611 C CG . GLU B 11 ? 0.2046 0.1891 0.1504 -0.0092 -0.0496 -0.0353 9 GLU B CG 1612 C CD . GLU B 11 ? 0.2535 0.2389 0.2102 -0.0112 -0.0494 -0.0316 9 GLU B CD 1613 O OE1 . GLU B 11 ? 0.2454 0.2207 0.2037 -0.0128 -0.0467 -0.0327 9 GLU B OE1 1614 O OE2 . GLU B 11 ? 0.2457 0.2393 0.2072 -0.0108 -0.0504 -0.0272 9 GLU B OE2 1615 N N . GLN B 12 ? 0.2013 0.1858 0.1595 0.0021 -0.0381 -0.0300 10 GLN B N 1616 C CA . GLN B 12 ? 0.1669 0.1567 0.1273 0.0037 -0.0345 -0.0278 10 GLN B CA 1617 C C . GLN B 12 ? 0.2203 0.2171 0.1816 0.0024 -0.0390 -0.0237 10 GLN B C 1618 O O . GLN B 12 ? 0.2027 0.2016 0.1671 0.0011 -0.0435 -0.0226 10 GLN B O 1619 C CB . GLN B 12 ? 0.1668 0.1598 0.1441 0.0065 -0.0307 -0.0290 10 GLN B CB 1620 C CG . GLN B 12 ? 0.1566 0.1451 0.1415 0.0092 -0.0255 -0.0333 10 GLN B CG 1621 C CD . GLN B 12 ? 0.2259 0.2219 0.2340 0.0117 -0.0220 -0.0358 10 GLN B CD 1622 O OE1 . GLN B 12 ? 0.2231 0.2217 0.2368 0.0103 -0.0148 -0.0358 10 GLN B OE1 1623 N NE2 . GLN B 12 ? 0.1836 0.1830 0.2070 0.0159 -0.0273 -0.0380 10 GLN B NE2 1624 N N . VAL B 13 ? 0.1944 0.1925 0.1521 0.0035 -0.0360 -0.0210 11 VAL B N 1625 C CA . VAL B 13 ? 0.1620 0.1659 0.1238 0.0036 -0.0381 -0.0173 11 VAL B CA 1626 C C . VAL B 13 ? 0.1936 0.1958 0.1610 0.0053 -0.0305 -0.0159 11 VAL B C 1627 O O . VAL B 13 ? 0.2097 0.2052 0.1707 0.0068 -0.0231 -0.0149 11 VAL B O 1628 C CB . VAL B 13 ? 0.2011 0.2075 0.1544 0.0041 -0.0430 -0.0147 11 VAL B CB 1629 C CG1 . VAL B 13 ? 0.1930 0.2056 0.1548 0.0050 -0.0439 -0.0112 11 VAL B CG1 1630 C CG2 . VAL B 13 ? 0.1526 0.1605 0.1040 0.0007 -0.0494 -0.0184 11 VAL B CG2 1631 N N . LYS B 14 ? 0.1528 0.1592 0.1313 0.0047 -0.0309 -0.0164 12 LYS B N 1632 C CA . LYS B 14 ? 0.1687 0.1731 0.1564 0.0048 -0.0233 -0.0165 12 LYS B CA 1633 C C . LYS B 14 ? 0.1971 0.2028 0.1860 0.0053 -0.0243 -0.0141 12 LYS B C 1634 O O . LYS B 14 ? 0.2015 0.2116 0.1939 0.0041 -0.0292 -0.0169 12 LYS B O 1635 C CB . LYS B 14 ? 0.1520 0.1605 0.1574 0.0031 -0.0230 -0.0234 12 LYS B CB 1636 C CG . LYS B 14 ? 0.1479 0.1558 0.1576 0.0036 -0.0202 -0.0261 12 LYS B CG 1637 C CD . LYS B 14 ? 0.1697 0.1851 0.2032 0.0032 -0.0217 -0.0337 12 LYS B CD 1638 C CE . LYS B 14 ? 0.1628 0.1776 0.2044 0.0047 -0.0164 -0.0362 12 LYS B CE 1639 N NZ . LYS B 14 ? 0.1449 0.1705 0.2161 0.0054 -0.0195 -0.0442 12 LYS B NZ 1640 N N . HIS B 15 ? 0.1857 0.1858 0.1695 0.0081 -0.0188 -0.0084 13 HIS B N 1641 C CA . HIS B 15 ? 0.1989 0.1988 0.1863 0.0100 -0.0178 -0.0057 13 HIS B CA 1642 C C . HIS B 15 ? 0.2195 0.2126 0.2184 0.0083 -0.0078 -0.0082 13 HIS B C 1643 O O . HIS B 15 ? 0.1970 0.1801 0.1931 0.0100 0.0017 -0.0038 13 HIS B O 1644 C CB . HIS B 15 ? 0.1804 0.1771 0.1565 0.0160 -0.0189 0.0027 13 HIS B CB 1645 C CG . HIS B 15 ? 0.2465 0.2485 0.2113 0.0170 -0.0283 0.0034 13 HIS B CG 1646 N ND1 . HIS B 15 ? 0.2322 0.2449 0.2022 0.0159 -0.0369 0.0017 13 HIS B ND1 1647 C CD2 . HIS B 15 ? 0.2399 0.2367 0.1888 0.0185 -0.0294 0.0046 13 HIS B CD2 1648 C CE1 . HIS B 15 ? 0.1893 0.2044 0.1498 0.0160 -0.0442 0.0010 13 HIS B CE1 1649 N NE2 . HIS B 15 ? 0.2426 0.2477 0.1878 0.0179 -0.0404 0.0025 13 HIS B NE2 1650 N N . GLU B 16 ? 0.2099 0.2066 0.2205 0.0048 -0.0093 -0.0157 14 GLU B N 1651 C CA . GLU B 16 ? 0.2037 0.1961 0.2303 0.0011 -0.0015 -0.0220 14 GLU B CA 1652 C C . GLU B 16 ? 0.2706 0.2557 0.3018 0.0018 0.0047 -0.0220 14 GLU B C 1653 O O . GLU B 16 ? 0.2362 0.2240 0.2629 0.0032 0.0001 -0.0230 14 GLU B O 1654 C CB . GLU B 16 ? 0.1371 0.1384 0.1748 -0.0030 -0.0094 -0.0332 14 GLU B CB 1655 C CG . GLU B 16 ? 0.1558 0.1637 0.1912 -0.0024 -0.0157 -0.0334 14 GLU B CG 1656 C CD . GLU B 16 ? 0.1997 0.2163 0.2481 -0.0043 -0.0247 -0.0437 14 GLU B CD 1657 O OE1 . GLU B 16 ? 0.1876 0.2056 0.2429 -0.0065 -0.0282 -0.0516 14 GLU B OE1 1658 O OE2 . GLU B 16 ? 0.2229 0.2444 0.2744 -0.0029 -0.0290 -0.0444 14 GLU B OE2 1659 N N . CYS B 17 ? 0.1622 0.1362 0.2028 0.0008 0.0174 -0.0209 15 CYS B N 1660 C CA . CYS B 17 ? 0.2230 0.1869 0.2718 0.0006 0.0257 -0.0227 15 CYS B CA 1661 C C . CYS B 17 ? 0.2153 0.1778 0.2863 -0.0076 0.0310 -0.0359 15 CYS B C 1662 O O . CYS B 17 ? 0.1934 0.1524 0.2768 -0.0112 0.0399 -0.0367 15 CYS B O 1663 C CB . CYS B 17 ? 0.2176 0.1657 0.2589 0.0071 0.0374 -0.0095 15 CYS B CB 1664 S SG . CYS B 17 ? 0.2610 0.2141 0.2816 0.0174 0.0273 0.0031 15 CYS B SG 1665 N N . HIS B 18 ? 0.2321 0.1971 0.3089 -0.0109 0.0260 -0.0471 16 HIS B N 1666 C CA . HIS B 18 ? 0.2503 0.2165 0.3495 -0.0193 0.0270 -0.0632 16 HIS B CA 1667 C C . HIS B 18 ? 0.2131 0.1634 0.3226 -0.0217 0.0398 -0.0678 16 HIS B C 1668 O O . HIS B 18 ? 0.2437 0.1892 0.3422 -0.0185 0.0387 -0.0683 16 HIS B O 1669 C CB . HIS B 18 ? 0.2531 0.2330 0.3479 -0.0211 0.0091 -0.0756 16 HIS B CB 1670 C CG . HIS B 18 ? 0.2650 0.2583 0.3530 -0.0187 -0.0027 -0.0721 16 HIS B CG 1671 N ND1 . HIS B 18 ? 0.2475 0.2529 0.3525 -0.0221 -0.0116 -0.0824 16 HIS B ND1 1672 C CD2 . HIS B 18 ? 0.2710 0.2672 0.3395 -0.0130 -0.0068 -0.0603 16 HIS B CD2 1673 C CE1 . HIS B 18 ? 0.2648 0.2781 0.3594 -0.0178 -0.0198 -0.0760 16 HIS B CE1 1674 N NE2 . HIS B 18 ? 0.2089 0.2160 0.2807 -0.0130 -0.0166 -0.0631 16 HIS B NE2 1675 N N . PHE B 19 ? 0.2080 0.1491 0.3404 -0.0276 0.0537 -0.0714 17 PHE B N 1676 C CA . PHE B 19 ? 0.2524 0.1740 0.3961 -0.0301 0.0694 -0.0744 17 PHE B CA 1677 C C . PHE B 19 ? 0.2994 0.2233 0.4706 -0.0416 0.0684 -0.0970 17 PHE B C 1678 O O . PHE B 19 ? 0.3069 0.2428 0.5011 -0.0489 0.0651 -0.1072 17 PHE B O 1679 C CB . PHE B 19 ? 0.2770 0.1794 0.4238 -0.0275 0.0901 -0.0595 17 PHE B CB 1680 C CG . PHE B 19 ? 0.2953 0.1950 0.4131 -0.0155 0.0886 -0.0386 17 PHE B CG 1681 C CD1 . PHE B 19 ? 0.2936 0.1817 0.3958 -0.0056 0.0913 -0.0270 17 PHE B CD1 1682 C CD2 . PHE B 19 ? 0.2292 0.1390 0.3372 -0.0137 0.0833 -0.0320 17 PHE B CD2 1683 C CE1 . PHE B 19 ? 0.2545 0.1431 0.3328 0.0056 0.0865 -0.0098 17 PHE B CE1 1684 C CE2 . PHE B 19 ? 0.2301 0.1378 0.3110 -0.0033 0.0799 -0.0154 17 PHE B CE2 1685 C CZ . PHE B 19 ? 0.2522 0.1505 0.3187 0.0064 0.0801 -0.0045 17 PHE B CZ 1686 N N . PHE B 20 ? 0.2875 0.2006 0.4578 -0.0429 0.0710 -0.1060 18 PHE B N 1687 C CA . PHE B 20 ? 0.3314 0.2529 0.5183 -0.0507 0.0673 -0.1228 18 PHE B CA 1688 C C . PHE B 20 ? 0.3397 0.2414 0.5352 -0.0515 0.0871 -0.1199 18 PHE B C 1689 O O . PHE B 20 ? 0.3266 0.2133 0.5055 -0.0452 0.0927 -0.1137 18 PHE B O 1690 C CB . PHE B 20 ? 0.3908 0.3212 0.5581 -0.0497 0.0483 -0.1351 18 PHE B CB 1691 C CG . PHE B 20 ? 0.5230 0.4691 0.6733 -0.0460 0.0292 -0.1346 18 PHE B CG 1692 C CD1 . PHE B 20 ? 0.6351 0.6019 0.7949 -0.0487 0.0130 -0.1428 18 PHE B CD1 1693 C CD2 . PHE B 20 ? 0.5044 0.4474 0.6280 -0.0377 0.0273 -0.1224 18 PHE B CD2 1694 C CE1 . PHE B 20 ? 0.6454 0.6254 0.7880 -0.0439 -0.0041 -0.1400 18 PHE B CE1 1695 C CE2 . PHE B 20 ? 0.5155 0.4742 0.6210 -0.0333 0.0108 -0.1181 18 PHE B CE2 1696 C CZ . PHE B 20 ? 0.5635 0.5379 0.6792 -0.0372 -0.0047 -0.1293 18 PHE B CZ 1697 N N . ASN B 21 ? 0.3876 0.2897 0.6101 -0.0584 0.0986 -0.1246 19 ASN B N 1698 C CA . ASN B 21 ? 0.4862 0.3690 0.7183 -0.0596 0.1189 -0.1218 19 ASN B CA 1699 C C . ASN B 21 ? 0.4809 0.3415 0.6953 -0.0494 0.1343 -0.0987 19 ASN B C 1700 O O . ASN B 21 ? 0.4209 0.2669 0.6218 -0.0430 0.1392 -0.0928 19 ASN B O 1701 C CB . ASN B 21 ? 0.5957 0.4760 0.8225 -0.0616 0.1127 -0.1360 19 ASN B CB 1702 C CG . ASN B 21 ? 0.7892 0.6489 1.0260 -0.0626 0.1335 -0.1341 19 ASN B CG 1703 O OD1 . ASN B 21 ? 0.7512 0.6024 1.0065 -0.0649 0.1518 -0.1277 19 ASN B OD1 1704 N ND2 . ASN B 21 ? 0.9989 0.8492 1.2223 -0.0604 0.1320 -0.1396 19 ASN B ND2 1705 N N . GLY B 22 ? 0.5927 0.4510 0.8057 -0.0467 0.1412 -0.0854 20 GLY B N 1706 C CA . GLY B 22 ? 0.6330 0.4710 0.8238 -0.0350 0.1522 -0.0620 20 GLY B CA 1707 C C . GLY B 22 ? 0.5592 0.3984 0.7250 -0.0251 0.1377 -0.0554 20 GLY B C 1708 O O . GLY B 22 ? 0.5540 0.4088 0.7150 -0.0264 0.1218 -0.0615 20 GLY B O 1709 N N . THR B 23 ? 0.4696 0.2935 0.6216 -0.0142 0.1434 -0.0431 21 THR B N 1710 C CA . THR B 23 ? 0.4469 0.2742 0.5804 -0.0033 0.1313 -0.0374 21 THR B CA 1711 C C . THR B 23 ? 0.4593 0.2901 0.5955 -0.0047 0.1272 -0.0508 21 THR B C 1712 O O . THR B 23 ? 0.4122 0.2442 0.5370 0.0054 0.1226 -0.0454 21 THR B O 1713 C CB . THR B 23 ? 0.4469 0.2606 0.5624 0.0130 0.1368 -0.0127 21 THR B CB 1714 O OG1 . THR B 23 ? 0.4502 0.2462 0.5703 0.0162 0.1520 -0.0063 21 THR B OG1 1715 C CG2 . THR B 23 ? 0.5126 0.3259 0.6153 0.0152 0.1378 0.0009 21 THR B CG2 1716 N N . GLU B 24 ? 0.4337 0.2675 0.5849 -0.0167 0.1290 -0.0683 22 GLU B N 1717 C CA . GLU B 24 ? 0.4009 0.2352 0.5503 -0.0184 0.1260 -0.0818 22 GLU B CA 1718 C C . GLU B 24 ? 0.4037 0.2534 0.5377 -0.0180 0.1085 -0.0917 22 GLU B C 1719 O O . GLU B 24 ? 0.4264 0.2739 0.5486 -0.0120 0.1079 -0.0928 22 GLU B O 1720 C CB . GLU B 24 ? 0.5765 0.4104 0.7439 -0.0306 0.1304 -0.0988 22 GLU B CB 1721 C CG . GLU B 24 ? 0.7351 0.5580 0.9009 -0.0299 0.1368 -0.1064 22 GLU B CG 1722 C CD . GLU B 24 ? 0.8794 0.6816 1.0489 -0.0212 0.1557 -0.0900 22 GLU B CD 1723 O OE1 . GLU B 24 ? 0.8518 0.6472 1.0210 -0.0147 0.1631 -0.0715 22 GLU B OE1 1724 O OE2 . GLU B 24 ? 0.9747 0.7666 1.1454 -0.0202 0.1629 -0.0955 22 GLU B OE2 1725 N N . ARG B 25 ? 0.2934 0.1586 0.4274 -0.0239 0.0954 -0.0982 23 ARG B N 1726 C CA . ARG B 25 ? 0.3553 0.2369 0.4704 -0.0227 0.0780 -0.1040 23 ARG B CA 1727 C C . ARG B 25 ? 0.3391 0.2376 0.4475 -0.0194 0.0681 -0.0898 23 ARG B C 1728 O O . ARG B 25 ? 0.2866 0.1890 0.4088 -0.0248 0.0682 -0.0904 23 ARG B O 1729 C CB . ARG B 25 ? 0.4267 0.3177 0.5410 -0.0322 0.0651 -0.1256 23 ARG B CB 1730 C CG . ARG B 25 ? 0.6256 0.5280 0.7142 -0.0297 0.0488 -0.1314 23 ARG B CG 1731 C CD . ARG B 25 ? 0.8473 0.7515 0.9234 -0.0345 0.0385 -0.1485 23 ARG B CD 1732 N NE . ARG B 25 ? 1.0008 0.9215 1.0624 -0.0354 0.0175 -0.1540 23 ARG B NE 1733 C CZ . ARG B 25 ? 1.0787 1.0131 1.1551 -0.0408 0.0053 -0.1607 23 ARG B CZ 1734 N NH1 . ARG B 25 ? 1.0731 1.0213 1.1347 -0.0391 -0.0139 -0.1624 23 ARG B NH1 1735 N NH2 . ARG B 25 ? 1.1041 1.0381 1.2113 -0.0473 0.0135 -0.1647 23 ARG B NH2 1736 N N . VAL B 26 ? 0.3239 0.2315 0.4136 -0.0108 0.0615 -0.0774 24 VAL B N 1737 C CA . VAL B 26 ? 0.2786 0.1993 0.3611 -0.0071 0.0536 -0.0636 24 VAL B CA 1738 C C . VAL B 26 ? 0.2770 0.2137 0.3410 -0.0048 0.0390 -0.0632 24 VAL B C 1739 O O . VAL B 26 ? 0.2964 0.2322 0.3507 -0.0010 0.0397 -0.0637 24 VAL B O 1740 C CB . VAL B 26 ? 0.2961 0.2084 0.3769 0.0027 0.0626 -0.0438 24 VAL B CB 1741 C CG1 . VAL B 26 ? 0.2771 0.2018 0.3472 0.0060 0.0536 -0.0321 24 VAL B CG1 1742 C CG2 . VAL B 26 ? 0.2835 0.1746 0.3789 0.0016 0.0799 -0.0414 24 VAL B CG2 1743 N N . ARG B 27 ? 0.2543 0.2040 0.3147 -0.0073 0.0279 -0.0628 25 ARG B N 1744 C CA . ARG B 27 ? 0.2443 0.2062 0.2872 -0.0053 0.0154 -0.0612 25 ARG B CA 1745 C C . ARG B 27 ? 0.2613 0.2320 0.3009 -0.0019 0.0111 -0.0482 25 ARG B C 1746 O O . ARG B 27 ? 0.2237 0.1956 0.2719 -0.0041 0.0118 -0.0467 25 ARG B O 1747 C CB . ARG B 27 ? 0.2592 0.2271 0.2979 -0.0107 0.0034 -0.0755 25 ARG B CB 1748 C CG . ARG B 27 ? 0.3139 0.2910 0.3332 -0.0081 -0.0086 -0.0723 25 ARG B CG 1749 C CD . ARG B 27 ? 0.3635 0.3425 0.3733 -0.0108 -0.0212 -0.0866 25 ARG B CD 1750 N NE . ARG B 27 ? 0.4083 0.3921 0.3969 -0.0072 -0.0320 -0.0821 25 ARG B NE 1751 C CZ . ARG B 27 ? 0.5476 0.5405 0.5387 -0.0068 -0.0444 -0.0832 25 ARG B CZ 1752 N NH1 . ARG B 27 ? 0.5228 0.5234 0.5395 -0.0105 -0.0473 -0.0898 25 ARG B NH1 1753 N NH2 . ARG B 27 ? 0.5503 0.5437 0.5206 -0.0026 -0.0524 -0.0778 25 ARG B NH2 1754 N N . PHE B 28 ? 0.2144 0.1906 0.2427 0.0028 0.0077 -0.0401 26 PHE B N 1755 C CA . PHE B 28 ? 0.2227 0.2068 0.2465 0.0058 0.0027 -0.0296 26 PHE B CA 1756 C C . PHE B 28 ? 0.2361 0.2288 0.2487 0.0038 -0.0075 -0.0323 26 PHE B C 1757 O O . PHE B 28 ? 0.2589 0.2513 0.2628 0.0039 -0.0083 -0.0354 26 PHE B O 1758 C CB . PHE B 28 ? 0.2238 0.2085 0.2483 0.0127 0.0060 -0.0192 26 PHE B CB 1759 C CG . PHE B 28 ? 0.2493 0.2438 0.2679 0.0153 -0.0020 -0.0112 26 PHE B CG 1760 C CD1 . PHE B 28 ? 0.2107 0.2041 0.2249 0.0160 -0.0042 -0.0062 26 PHE B CD1 1761 C CD2 . PHE B 28 ? 0.2824 0.2859 0.3009 0.0166 -0.0058 -0.0096 26 PHE B CD2 1762 C CE1 . PHE B 28 ? 0.2758 0.2768 0.2827 0.0182 -0.0121 -0.0009 26 PHE B CE1 1763 C CE2 . PHE B 28 ? 0.1981 0.2110 0.2144 0.0179 -0.0136 -0.0045 26 PHE B CE2 1764 C CZ . PHE B 28 ? 0.2045 0.2159 0.2136 0.0187 -0.0178 -0.0007 26 PHE B CZ 1765 N N . LEU B 29 ? 0.2382 0.2358 0.2500 0.0025 -0.0135 -0.0310 27 LEU B N 1766 C CA . LEU B 29 ? 0.2120 0.2150 0.2138 0.0015 -0.0227 -0.0326 27 LEU B CA 1767 C C . LEU B 29 ? 0.2160 0.2234 0.2156 0.0030 -0.0251 -0.0249 27 LEU B C 1768 O O . LEU B 29 ? 0.2114 0.2188 0.2159 0.0027 -0.0241 -0.0239 27 LEU B O 1769 C CB . LEU B 29 ? 0.2428 0.2475 0.2492 -0.0012 -0.0289 -0.0420 27 LEU B CB 1770 C CG . LEU B 29 ? 0.3426 0.3501 0.3371 -0.0001 -0.0397 -0.0440 27 LEU B CG 1771 C CD1 . LEU B 29 ? 0.3023 0.3038 0.2772 0.0012 -0.0404 -0.0446 27 LEU B CD1 1772 C CD2 . LEU B 29 ? 0.3191 0.3315 0.3246 -0.0013 -0.0480 -0.0539 27 LEU B CD2 1773 N N . ASP B 30 ? 0.1718 0.1821 0.1647 0.0040 -0.0271 -0.0205 28 ASP B N 1774 C CA . ASP B 30 ? 0.2300 0.2443 0.2208 0.0047 -0.0304 -0.0152 28 ASP B CA 1775 C C . ASP B 30 ? 0.2583 0.2726 0.2418 0.0027 -0.0357 -0.0170 28 ASP B C 1776 O O . ASP B 30 ? 0.2705 0.2829 0.2480 0.0019 -0.0357 -0.0175 28 ASP B O 1777 C CB . ASP B 30 ? 0.2517 0.2708 0.2462 0.0065 -0.0294 -0.0109 28 ASP B CB 1778 C CG . ASP B 30 ? 0.2958 0.3186 0.2908 0.0094 -0.0330 -0.0060 28 ASP B CG 1779 O OD1 . ASP B 30 ? 0.1922 0.2105 0.1809 0.0101 -0.0333 -0.0050 28 ASP B OD1 1780 O OD2 . ASP B 30 ? 0.2676 0.2975 0.2693 0.0113 -0.0354 -0.0035 28 ASP B OD2 1781 N N . ARG B 31 ? 0.1970 0.2112 0.1802 0.0026 -0.0384 -0.0175 29 ARG B N 1782 C CA . ARG B 31 ? 0.2269 0.2391 0.2056 0.0024 -0.0432 -0.0195 29 ARG B CA 1783 C C . ARG B 31 ? 0.2366 0.2479 0.2124 0.0018 -0.0445 -0.0177 29 ARG B C 1784 O O . ARG B 31 ? 0.2203 0.2321 0.1973 0.0022 -0.0427 -0.0172 29 ARG B O 1785 C CB . ARG B 31 ? 0.1961 0.2092 0.1824 0.0033 -0.0453 -0.0248 29 ARG B CB 1786 C CG . ARG B 31 ? 0.2001 0.2139 0.1921 0.0026 -0.0439 -0.0295 29 ARG B CG 1787 C CD . ARG B 31 ? 0.1282 0.1460 0.1351 0.0023 -0.0467 -0.0369 29 ARG B CD 1788 N NE . ARG B 31 ? 0.1816 0.2011 0.1851 0.0052 -0.0573 -0.0402 29 ARG B NE 1789 C CZ . ARG B 31 ? 0.1757 0.2020 0.1955 0.0064 -0.0633 -0.0472 29 ARG B CZ 1790 N NH1 . ARG B 31 ? 0.1491 0.1806 0.1917 0.0031 -0.0570 -0.0522 29 ARG B NH1 1791 N NH2 . ARG B 31 ? 0.1437 0.1710 0.1585 0.0113 -0.0751 -0.0489 29 ARG B NH2 1792 N N . TYR B 32 ? 0.2056 0.2131 0.1755 0.0010 -0.0465 -0.0168 30 TYR B N 1793 C CA . TYR B 32 ? 0.1442 0.1487 0.1122 -0.0005 -0.0473 -0.0167 30 TYR B CA 1794 C C . TYR B 32 ? 0.1545 0.1517 0.1196 0.0020 -0.0494 -0.0174 30 TYR B C 1795 O O . TYR B 32 ? 0.1913 0.1836 0.1504 0.0042 -0.0513 -0.0158 30 TYR B O 1796 C CB . TYR B 32 ? 0.1859 0.1906 0.1541 -0.0044 -0.0460 -0.0153 30 TYR B CB 1797 C CG . TYR B 32 ? 0.2265 0.2406 0.2013 -0.0053 -0.0466 -0.0151 30 TYR B CG 1798 C CD1 . TYR B 32 ? 0.1339 0.1513 0.1099 -0.0071 -0.0504 -0.0173 30 TYR B CD1 1799 C CD2 . TYR B 32 ? 0.2158 0.2345 0.1947 -0.0034 -0.0444 -0.0132 30 TYR B CD2 1800 C CE1 . TYR B 32 ? 0.1786 0.2052 0.1595 -0.0058 -0.0541 -0.0166 30 TYR B CE1 1801 C CE2 . TYR B 32 ? 0.2377 0.2646 0.2238 -0.0021 -0.0458 -0.0119 30 TYR B CE2 1802 C CZ . TYR B 32 ? 0.1986 0.2300 0.1854 -0.0026 -0.0516 -0.0131 30 TYR B CZ 1803 O OH . TYR B 32 ? 0.2178 0.2578 0.2107 0.0007 -0.0560 -0.0115 30 TYR B OH 1804 N N . PHE B 33 ? 0.1409 0.1359 0.1083 0.0027 -0.0490 -0.0197 31 PHE B N 1805 C CA . PHE B 33 ? 0.2141 0.2032 0.1834 0.0069 -0.0509 -0.0205 31 PHE B CA 1806 C C . PHE B 33 ? 0.1731 0.1530 0.1394 0.0056 -0.0483 -0.0215 31 PHE B C 1807 O O . PHE B 33 ? 0.2015 0.1818 0.1661 0.0021 -0.0457 -0.0245 31 PHE B O 1808 C CB . PHE B 33 ? 0.1430 0.1384 0.1250 0.0102 -0.0504 -0.0243 31 PHE B CB 1809 C CG . PHE B 33 ? 0.1665 0.1706 0.1556 0.0100 -0.0517 -0.0257 31 PHE B CG 1810 C CD1 . PHE B 33 ? 0.2024 0.2102 0.1983 0.0138 -0.0586 -0.0281 31 PHE B CD1 1811 C CD2 . PHE B 33 ? 0.1837 0.1910 0.1725 0.0068 -0.0465 -0.0252 31 PHE B CD2 1812 C CE1 . PHE B 33 ? 0.2514 0.2665 0.2554 0.0125 -0.0598 -0.0319 31 PHE B CE1 1813 C CE2 . PHE B 33 ? 0.1992 0.2117 0.1959 0.0062 -0.0458 -0.0270 31 PHE B CE2 1814 C CZ . PHE B 33 ? 0.1539 0.1704 0.1590 0.0082 -0.0521 -0.0313 31 PHE B CZ 1815 N N . TYR B 34 ? 0.1859 0.1555 0.1497 0.0092 -0.0495 -0.0193 32 TYR B N 1816 C CA . TYR B 34 ? 0.2437 0.2020 0.2072 0.0088 -0.0458 -0.0212 32 TYR B CA 1817 C C . TYR B 34 ? 0.2593 0.2157 0.2316 0.0171 -0.0474 -0.0221 32 TYR B C 1818 O O . TYR B 34 ? 0.2143 0.1687 0.1867 0.0240 -0.0531 -0.0180 32 TYR B O 1819 C CB . TYR B 34 ? 0.2149 0.1594 0.1706 0.0061 -0.0432 -0.0173 32 TYR B CB 1820 C CG . TYR B 34 ? 0.2064 0.1359 0.1629 0.0052 -0.0383 -0.0200 32 TYR B CG 1821 C CD1 . TYR B 34 ? 0.2070 0.1369 0.1655 -0.0018 -0.0355 -0.0278 32 TYR B CD1 1822 C CD2 . TYR B 34 ? 0.2631 0.1764 0.2167 0.0120 -0.0371 -0.0150 32 TYR B CD2 1823 C CE1 . TYR B 34 ? 0.2462 0.1606 0.2052 -0.0034 -0.0304 -0.0324 32 TYR B CE1 1824 C CE2 . TYR B 34 ? 0.2470 0.1437 0.2025 0.0114 -0.0310 -0.0177 32 TYR B CE2 1825 C CZ . TYR B 34 ? 0.2637 0.1612 0.2227 0.0029 -0.0271 -0.0273 32 TYR B CZ 1826 O OH . TYR B 34 ? 0.2891 0.1689 0.2498 0.0015 -0.0205 -0.0320 32 TYR B OH 1827 N N . HIS B 35 ? 0.1980 0.1554 0.1775 0.0171 -0.0424 -0.0278 33 HIS B N 1828 C CA . HIS B 35 ? 0.2419 0.2036 0.2378 0.0244 -0.0418 -0.0304 33 HIS B CA 1829 C C . HIS B 35 ? 0.3120 0.2898 0.3191 0.0260 -0.0469 -0.0306 33 HIS B C 1830 O O . HIS B 35 ? 0.2271 0.2120 0.2335 0.0209 -0.0430 -0.0324 33 HIS B O 1831 C CB . HIS B 35 ? 0.2203 0.1709 0.2208 0.0329 -0.0444 -0.0277 33 HIS B CB 1832 C CG . HIS B 35 ? 0.2356 0.1673 0.2254 0.0301 -0.0384 -0.0276 33 HIS B CG 1833 N ND1 . HIS B 35 ? 0.2815 0.2086 0.2642 0.0219 -0.0310 -0.0339 33 HIS B ND1 1834 C CD2 . HIS B 35 ? 0.2532 0.1677 0.2377 0.0345 -0.0386 -0.0224 33 HIS B CD2 1835 C CE1 . HIS B 35 ? 0.2546 0.1641 0.2315 0.0200 -0.0271 -0.0344 33 HIS B CE1 1836 N NE2 . HIS B 35 ? 0.2449 0.1453 0.2232 0.0275 -0.0302 -0.0267 33 HIS B NE2 1837 N N . GLN B 36 ? 0.1721 0.1545 0.1887 0.0333 -0.0561 -0.0292 34 GLN B N 1838 C CA . GLN B 36 ? 0.1628 0.1598 0.1893 0.0335 -0.0627 -0.0314 34 GLN B CA 1839 C C . GLN B 36 ? 0.2468 0.2411 0.2551 0.0336 -0.0714 -0.0268 34 GLN B C 1840 O O . GLN B 36 ? 0.2685 0.2727 0.2819 0.0339 -0.0780 -0.0298 34 GLN B O 1841 C CB . GLN B 36 ? 0.2824 0.2908 0.3358 0.0415 -0.0697 -0.0361 34 GLN B CB 1842 C CG . GLN B 36 ? 0.2825 0.2971 0.3610 0.0413 -0.0588 -0.0423 34 GLN B CG 1843 C CD . GLN B 36 ? 0.3622 0.3653 0.4416 0.0467 -0.0537 -0.0413 34 GLN B CD 1844 O OE1 . GLN B 36 ? 0.4575 0.4619 0.5511 0.0567 -0.0617 -0.0410 34 GLN B OE1 1845 N NE2 . GLN B 36 ? 0.3561 0.3471 0.4199 0.0410 -0.0413 -0.0412 34 GLN B NE2 1846 N N . GLU B 37 ? 0.2602 0.2398 0.2477 0.0331 -0.0701 -0.0205 35 GLU B N 1847 C CA . GLU B 37 ? 0.2833 0.2562 0.2506 0.0344 -0.0754 -0.0154 35 GLU B CA 1848 C C . GLU B 37 ? 0.2580 0.2341 0.2178 0.0256 -0.0694 -0.0154 35 GLU B C 1849 O O . GLU B 37 ? 0.2178 0.1891 0.1734 0.0194 -0.0615 -0.0138 35 GLU B O 1850 C CB . GLU B 37 ? 0.3094 0.2621 0.2593 0.0381 -0.0736 -0.0076 35 GLU B CB 1851 C CG . GLU B 37 ? 0.4016 0.3419 0.3257 0.0377 -0.0727 -0.0010 35 GLU B CG 1852 C CD . GLU B 37 ? 0.5206 0.4378 0.4294 0.0379 -0.0644 0.0071 35 GLU B CD 1853 O OE1 . GLU B 37 ? 0.4923 0.4009 0.4076 0.0421 -0.0634 0.0083 35 GLU B OE1 1854 O OE2 . GLU B 37 ? 0.5525 0.4592 0.4447 0.0336 -0.0570 0.0118 35 GLU B OE2 1855 N N . GLU B 38 ? 0.2332 0.2179 0.1933 0.0251 -0.0737 -0.0184 36 GLU B N 1856 C CA . GLU B 38 ? 0.2363 0.2223 0.1891 0.0187 -0.0679 -0.0177 36 GLU B CA 1857 C C . GLU B 38 ? 0.2498 0.2214 0.1815 0.0184 -0.0642 -0.0111 36 GLU B C 1858 O O . GLU B 38 ? 0.2404 0.2020 0.1554 0.0245 -0.0692 -0.0081 36 GLU B O 1859 C CB . GLU B 38 ? 0.1910 0.1855 0.1473 0.0188 -0.0724 -0.0230 36 GLU B CB 1860 C CG . GLU B 38 ? 0.2278 0.2241 0.1814 0.0128 -0.0644 -0.0226 36 GLU B CG 1861 C CD . GLU B 38 ? 0.2518 0.2538 0.2099 0.0122 -0.0667 -0.0288 36 GLU B CD 1862 O OE1 . GLU B 38 ? 0.2203 0.2251 0.1809 0.0158 -0.0761 -0.0344 36 GLU B OE1 1863 O OE2 . GLU B 38 ? 0.2297 0.2335 0.1904 0.0084 -0.0597 -0.0290 36 GLU B OE2 1864 N N . TYR B 39 ? 0.2117 0.1817 0.1441 0.0119 -0.0553 -0.0091 37 TYR B N 1865 C CA . TYR B 39 ? 0.2380 0.1940 0.1556 0.0104 -0.0484 -0.0033 37 TYR B CA 1866 C C . TYR B 39 ? 0.2623 0.2207 0.1770 0.0059 -0.0412 -0.0031 37 TYR B C 1867 O O . TYR B 39 ? 0.2575 0.2027 0.1564 0.0061 -0.0341 0.0014 37 TYR B O 1868 C CB . TYR B 39 ? 0.1989 0.1471 0.1218 0.0064 -0.0427 -0.0017 37 TYR B CB 1869 C CG . TYR B 39 ? 0.2968 0.2574 0.2371 -0.0007 -0.0407 -0.0067 37 TYR B CG 1870 C CD1 . TYR B 39 ? 0.2393 0.2048 0.1864 -0.0074 -0.0348 -0.0073 37 TYR B CD1 1871 C CD2 . TYR B 39 ? 0.2311 0.1976 0.1800 0.0000 -0.0447 -0.0112 37 TYR B CD2 1872 C CE1 . TYR B 39 ? 0.2866 0.2639 0.2479 -0.0124 -0.0365 -0.0122 37 TYR B CE1 1873 C CE2 . TYR B 39 ? 0.1745 0.1494 0.1320 -0.0053 -0.0441 -0.0157 37 TYR B CE2 1874 C CZ . TYR B 39 ? 0.2206 0.2013 0.1837 -0.0110 -0.0417 -0.0161 37 TYR B CZ 1875 O OH . TYR B 39 ? 0.2159 0.2058 0.1861 -0.0147 -0.0447 -0.0208 37 TYR B OH 1876 N N . VAL B 40 ? 0.2466 0.2198 0.1760 0.0027 -0.0413 -0.0072 38 VAL B N 1877 C CA . VAL B 40 ? 0.2077 0.1843 0.1384 0.0000 -0.0344 -0.0075 38 VAL B CA 1878 C C . VAL B 40 ? 0.2637 0.2527 0.2053 0.0006 -0.0377 -0.0118 38 VAL B C 1879 O O . VAL B 40 ? 0.2086 0.2048 0.1605 0.0008 -0.0423 -0.0137 38 VAL B O 1880 C CB . VAL B 40 ? 0.2181 0.1980 0.1619 -0.0062 -0.0263 -0.0061 38 VAL B CB 1881 C CG1 . VAL B 40 ? 0.2296 0.2218 0.1904 -0.0087 -0.0318 -0.0091 38 VAL B CG1 1882 C CG2 . VAL B 40 ? 0.2214 0.2049 0.1701 -0.0080 -0.0174 -0.0062 38 VAL B CG2 1883 N N . ARG B 41 ? 0.1930 0.1815 0.1308 0.0011 -0.0337 -0.0133 39 ARG B N 1884 C CA . ARG B 41 ? 0.2250 0.2220 0.1742 0.0014 -0.0344 -0.0171 39 ARG B CA 1885 C C . ARG B 41 ? 0.1892 0.1871 0.1422 0.0008 -0.0256 -0.0175 39 ARG B C 1886 O O . ARG B 41 ? 0.2377 0.2276 0.1795 0.0005 -0.0186 -0.0168 39 ARG B O 1887 C CB . ARG B 41 ? 0.2167 0.2122 0.1612 0.0040 -0.0415 -0.0226 39 ARG B CB 1888 C CG . ARG B 41 ? 0.2791 0.2639 0.2016 0.0066 -0.0433 -0.0252 39 ARG B CG 1889 C CD . ARG B 41 ? 0.2749 0.2617 0.1982 0.0079 -0.0508 -0.0343 39 ARG B CD 1890 N NE . ARG B 41 ? 0.2085 0.2026 0.1440 0.0094 -0.0611 -0.0373 39 ARG B NE 1891 C CZ . ARG B 41 ? 0.2891 0.2878 0.2316 0.0102 -0.0700 -0.0466 39 ARG B CZ 1892 N NH1 . ARG B 41 ? 0.2384 0.2334 0.1732 0.0094 -0.0706 -0.0545 39 ARG B NH1 1893 N NH2 . ARG B 41 ? 0.3045 0.3119 0.2641 0.0116 -0.0777 -0.0493 39 ARG B NH2 1894 N N . PHE B 42 ? 0.1823 0.1877 0.1501 0.0014 -0.0245 -0.0181 40 PHE B N 1895 C CA . PHE B 42 ? 0.1783 0.1831 0.1512 0.0025 -0.0165 -0.0197 40 PHE B CA 1896 C C . PHE B 42 ? 0.2264 0.2270 0.1977 0.0034 -0.0178 -0.0256 40 PHE B C 1897 O O . PHE B 42 ? 0.1899 0.1938 0.1701 0.0036 -0.0213 -0.0256 40 PHE B O 1898 C CB . PHE B 42 ? 0.1491 0.1640 0.1417 0.0039 -0.0139 -0.0156 40 PHE B CB 1899 C CG . PHE B 42 ? 0.2475 0.2618 0.2495 0.0067 -0.0050 -0.0167 40 PHE B CG 1900 C CD1 . PHE B 42 ? 0.2154 0.2322 0.2257 0.0066 0.0039 -0.0162 40 PHE B CD1 1901 C CD2 . PHE B 42 ? 0.2168 0.2270 0.2219 0.0092 -0.0037 -0.0185 40 PHE B CD2 1902 C CE1 . PHE B 42 ? 0.1959 0.2118 0.2171 0.0101 0.0135 -0.0176 40 PHE B CE1 1903 C CE2 . PHE B 42 ? 0.2321 0.2396 0.2466 0.0124 0.0054 -0.0196 40 PHE B CE2 1904 C CZ . PHE B 42 ? 0.2113 0.2220 0.2337 0.0134 0.0138 -0.0192 40 PHE B CZ 1905 N N . ASP B 43 ? 0.1977 0.1898 0.1574 0.0036 -0.0137 -0.0312 41 ASP B N 1906 C CA . ASP B 43 ? 0.1856 0.1732 0.1456 0.0032 -0.0145 -0.0397 41 ASP B CA 1907 C C . ASP B 43 ? 0.1932 0.1766 0.1603 0.0045 -0.0025 -0.0412 41 ASP B C 1908 O O . ASP B 43 ? 0.2738 0.2518 0.2316 0.0053 0.0055 -0.0415 41 ASP B O 1909 C CB . ASP B 43 ? 0.2160 0.1957 0.1533 0.0032 -0.0215 -0.0471 41 ASP B CB 1910 C CG . ASP B 43 ? 0.3043 0.2816 0.2446 0.0016 -0.0263 -0.0592 41 ASP B CG 1911 O OD1 . ASP B 43 ? 0.2806 0.2572 0.2372 0.0000 -0.0191 -0.0624 41 ASP B OD1 1912 O OD2 . ASP B 43 ? 0.2809 0.2565 0.2078 0.0022 -0.0378 -0.0660 41 ASP B OD2 1913 N N . SER B 44 ? 0.1764 0.1603 0.1604 0.0052 0.0007 -0.0416 42 SER B N 1914 C CA . SER B 44 ? 0.1846 0.1628 0.1773 0.0077 0.0125 -0.0428 42 SER B CA 1915 C C . SER B 44 ? 0.2601 0.2260 0.2372 0.0062 0.0179 -0.0542 42 SER B C 1916 O O . SER B 44 ? 0.2900 0.2499 0.2701 0.0086 0.0300 -0.0557 42 SER B O 1917 C CB . SER B 44 ? 0.2420 0.2180 0.2525 0.0094 0.0159 -0.0406 42 SER B CB 1918 O OG . SER B 44 ? 0.2267 0.1984 0.2376 0.0048 0.0119 -0.0483 42 SER B OG 1919 N N . ASP B 45 ? 0.2426 0.2048 0.2031 0.0029 0.0085 -0.0629 43 ASP B N 1920 C CA . ASP B 45 ? 0.3144 0.2638 0.2523 0.0020 0.0102 -0.0749 43 ASP B CA 1921 C C . ASP B 45 ? 0.3263 0.2694 0.2426 0.0045 0.0182 -0.0709 43 ASP B C 1922 O O . ASP B 45 ? 0.3080 0.2375 0.2054 0.0051 0.0268 -0.0787 43 ASP B O 1923 C CB . ASP B 45 ? 0.3616 0.3112 0.2857 -0.0004 -0.0060 -0.0841 43 ASP B CB 1924 C CG . ASP B 45 ? 0.4319 0.3834 0.3767 -0.0046 -0.0102 -0.0947 43 ASP B CG 1925 O OD1 . ASP B 45 ? 0.4109 0.3617 0.3789 -0.0055 0.0002 -0.0921 43 ASP B OD1 1926 O OD2 . ASP B 45 ? 0.5122 0.4658 0.4513 -0.0068 -0.0241 -0.1055 43 ASP B OD2 1927 N N . VAL B 46 ? 0.2656 0.2170 0.1844 0.0054 0.0169 -0.0595 44 VAL B N 1928 C CA . VAL B 46 ? 0.3229 0.2675 0.2238 0.0065 0.0262 -0.0548 44 VAL B CA 1929 C C . VAL B 46 ? 0.3309 0.2836 0.2579 0.0076 0.0402 -0.0477 44 VAL B C 1930 O O . VAL B 46 ? 0.3332 0.2782 0.2550 0.0085 0.0559 -0.0486 44 VAL B O 1931 C CB . VAL B 46 ? 0.2568 0.2031 0.1439 0.0062 0.0162 -0.0479 44 VAL B CB 1932 C CG1 . VAL B 46 ? 0.2742 0.2112 0.1459 0.0066 0.0295 -0.0418 44 VAL B CG1 1933 C CG2 . VAL B 46 ? 0.3171 0.2567 0.1795 0.0073 0.0004 -0.0551 44 VAL B CG2 1934 N N . GLY B 47 ? 0.2891 0.2575 0.2442 0.0080 0.0343 -0.0410 45 GLY B N 1935 C CA . GLY B 47 ? 0.2539 0.2335 0.2376 0.0103 0.0427 -0.0350 45 GLY B CA 1936 C C . GLY B 47 ? 0.2631 0.2511 0.2537 0.0082 0.0445 -0.0285 45 GLY B C 1937 O O . GLY B 47 ? 0.2665 0.2656 0.2836 0.0097 0.0516 -0.0254 45 GLY B O 1938 N N . GLU B 48 ? 0.2094 0.1922 0.1789 0.0050 0.0379 -0.0271 46 GLU B N 1939 C CA . GLU B 48 ? 0.2634 0.2520 0.2398 0.0018 0.0386 -0.0213 46 GLU B CA 1940 C C . GLU B 48 ? 0.2692 0.2560 0.2306 0.0003 0.0241 -0.0193 46 GLU B C 1941 O O . GLU B 48 ? 0.2277 0.2069 0.1697 0.0018 0.0159 -0.0227 46 GLU B O 1942 C CB . GLU B 48 ? 0.3073 0.2821 0.2680 -0.0002 0.0556 -0.0210 46 GLU B CB 1943 C CG . GLU B 48 ? 0.4965 0.4765 0.4818 0.0002 0.0737 -0.0220 46 GLU B CG 1944 C CD . GLU B 48 ? 0.6292 0.5926 0.5974 -0.0025 0.0944 -0.0212 46 GLU B CD 1945 O OE1 . GLU B 48 ? 0.6779 0.6475 0.6725 -0.0034 0.1118 -0.0217 46 GLU B OE1 1946 O OE2 . GLU B 48 ? 0.5198 0.4635 0.4485 -0.0029 0.0937 -0.0196 46 GLU B OE2 1947 N N . TYR B 49 ? 0.2253 0.2195 0.1982 -0.0027 0.0209 -0.0149 47 TYR B N 1948 C CA . TYR B 49 ? 0.2134 0.2036 0.1724 -0.0037 0.0098 -0.0130 47 TYR B CA 1949 C C . TYR B 49 ? 0.2892 0.2599 0.2168 -0.0031 0.0142 -0.0117 47 TYR B C 1950 O O . TYR B 49 ? 0.2734 0.2339 0.1929 -0.0043 0.0289 -0.0101 47 TYR B O 1951 C CB . TYR B 49 ? 0.2066 0.2066 0.1845 -0.0076 0.0072 -0.0102 47 TYR B CB 1952 C CG . TYR B 49 ? 0.2316 0.2492 0.2334 -0.0067 -0.0015 -0.0109 47 TYR B CG 1953 C CD1 . TYR B 49 ? 0.2372 0.2574 0.2350 -0.0053 -0.0136 -0.0109 47 TYR B CD1 1954 C CD2 . TYR B 49 ? 0.2416 0.2724 0.2693 -0.0063 0.0026 -0.0112 47 TYR B CD2 1955 C CE1 . TYR B 49 ? 0.3059 0.3382 0.3183 -0.0033 -0.0209 -0.0104 47 TYR B CE1 1956 C CE2 . TYR B 49 ? 0.2301 0.2754 0.2750 -0.0034 -0.0076 -0.0108 47 TYR B CE2 1957 C CZ . TYR B 49 ? 0.2168 0.2611 0.2507 -0.0019 -0.0191 -0.0100 47 TYR B CZ 1958 O OH . TYR B 49 ? 0.2609 0.3159 0.3050 0.0020 -0.0285 -0.0087 47 TYR B OH 1959 N N . ARG B 50 ? 0.2771 0.2419 0.1869 -0.0005 0.0021 -0.0120 48 ARG B N 1960 C CA . ARG B 50 ? 0.3008 0.2465 0.1788 0.0022 0.0023 -0.0089 48 ARG B CA 1961 C C . ARG B 50 ? 0.3174 0.2633 0.1965 0.0030 -0.0082 -0.0054 48 ARG B C 1962 O O . ARG B 50 ? 0.2792 0.2378 0.1736 0.0033 -0.0194 -0.0082 48 ARG B O 1963 C CB . ARG B 50 ? 0.2992 0.2356 0.1507 0.0073 -0.0043 -0.0144 48 ARG B CB 1964 C CG . ARG B 50 ? 0.3927 0.3230 0.2355 0.0072 0.0078 -0.0192 48 ARG B CG 1965 C CD . ARG B 50 ? 0.4055 0.3159 0.2240 0.0073 0.0257 -0.0140 48 ARG B CD 1966 N NE . ARG B 50 ? 0.5151 0.4199 0.3286 0.0071 0.0405 -0.0193 48 ARG B NE 1967 C CZ . ARG B 50 ? 0.6559 0.5699 0.4984 0.0033 0.0561 -0.0188 48 ARG B CZ 1968 N NH1 . ARG B 50 ? 0.7427 0.6729 0.6199 -0.0008 0.0567 -0.0142 48 ARG B NH1 1969 N NH2 . ARG B 50 ? 0.5818 0.4894 0.4201 0.0041 0.0706 -0.0240 48 ARG B NH2 1970 N N . ALA B 51 ? 0.3267 0.2566 0.1898 0.0034 -0.0022 0.0011 49 ALA B N 1971 C CA . ALA B 51 ? 0.3255 0.2508 0.1864 0.0054 -0.0105 0.0048 49 ALA B CA 1972 C C . ALA B 51 ? 0.3400 0.2612 0.1815 0.0138 -0.0258 0.0031 49 ALA B C 1973 O O . ALA B 51 ? 0.4012 0.3090 0.2137 0.0190 -0.0266 0.0034 49 ALA B O 1974 C CB . ALA B 51 ? 0.3723 0.2767 0.2190 0.0042 0.0025 0.0129 49 ALA B CB 1975 N N . VAL B 52 ? 0.2922 0.2246 0.1497 0.0154 -0.0382 0.0005 50 VAL B N 1976 C CA . VAL B 52 ? 0.2834 0.2148 0.1301 0.0237 -0.0537 -0.0019 50 VAL B CA 1977 C C . VAL B 52 ? 0.3536 0.2667 0.1810 0.0309 -0.0565 0.0063 50 VAL B C 1978 O O . VAL B 52 ? 0.3902 0.2935 0.1940 0.0402 -0.0673 0.0075 50 VAL B O 1979 C CB . VAL B 52 ? 0.2721 0.2238 0.1479 0.0226 -0.0633 -0.0090 50 VAL B CB 1980 C CG1 . VAL B 52 ? 0.2875 0.2420 0.1600 0.0307 -0.0798 -0.0135 50 VAL B CG1 1981 C CG2 . VAL B 52 ? 0.3035 0.2684 0.1951 0.0166 -0.0587 -0.0150 50 VAL B CG2 1982 N N . THR B 53 ? 0.3992 0.3067 0.2362 0.0270 -0.0476 0.0115 51 THR B N 1983 C CA . THR B 53 ? 0.4098 0.2957 0.2294 0.0332 -0.0462 0.0205 51 THR B CA 1984 C C . THR B 53 ? 0.4211 0.2928 0.2397 0.0253 -0.0268 0.0263 51 THR B C 1985 O O . THR B 53 ? 0.3622 0.2462 0.1998 0.0155 -0.0179 0.0219 51 THR B O 1986 C CB . THR B 53 ? 0.4380 0.3305 0.2783 0.0361 -0.0544 0.0190 51 THR B CB 1987 O OG1 . THR B 53 ? 0.3791 0.2819 0.2453 0.0257 -0.0459 0.0151 51 THR B OG1 1988 C CG2 . THR B 53 ? 0.3860 0.2975 0.2393 0.0418 -0.0715 0.0112 51 THR B CG2 1989 N N . GLU B 54 ? 0.3957 0.2416 0.1947 0.0298 -0.0201 0.0359 52 GLU B N 1990 C CA . GLU B 54 ? 0.4951 0.3244 0.2948 0.0214 0.0009 0.0413 52 GLU B CA 1991 C C . GLU B 54 ? 0.4142 0.2611 0.2533 0.0094 0.0050 0.0337 52 GLU B C 1992 O O . GLU B 54 ? 0.4299 0.2790 0.2839 -0.0009 0.0191 0.0319 52 GLU B O 1993 C CB . GLU B 54 ? 0.6407 0.4358 0.4136 0.0290 0.0079 0.0536 52 GLU B CB 1994 C CG . GLU B 54 ? 0.8828 0.6756 0.6692 0.0335 -0.0007 0.0541 52 GLU B CG 1995 C CD . GLU B 54 ? 1.0482 0.8043 0.8148 0.0382 0.0119 0.0667 52 GLU B CD 1996 O OE1 . GLU B 54 ? 0.9996 0.7507 0.7821 0.0390 0.0109 0.0663 52 GLU B OE1 1997 O OE2 . GLU B 54 ? 1.1538 0.8835 0.8875 0.0414 0.0245 0.0771 52 GLU B OE2 1998 N N . LEU B 55 ? 0.3633 0.2234 0.2192 0.0113 -0.0078 0.0283 53 LEU B N 1999 C CA . LEU B 55 ? 0.3857 0.2622 0.2727 0.0017 -0.0076 0.0198 53 LEU B CA 2000 C C . LEU B 55 ? 0.3655 0.2646 0.2710 -0.0067 -0.0061 0.0129 53 LEU B C 2001 O O . LEU B 55 ? 0.3299 0.2390 0.2579 -0.0156 -0.0032 0.0069 53 LEU B O 2002 C CB . LEU B 55 ? 0.4450 0.3327 0.3411 0.0072 -0.0215 0.0149 53 LEU B CB 2003 C CG . LEU B 55 ? 0.5234 0.4098 0.4361 0.0031 -0.0202 0.0098 53 LEU B CG 2004 C CD1 . LEU B 55 ? 0.4610 0.3195 0.3648 0.0047 -0.0108 0.0164 53 LEU B CD1 2005 C CD2 . LEU B 55 ? 0.4741 0.3724 0.3945 0.0095 -0.0316 0.0049 53 LEU B CD2 2006 N N . GLY B 56 ? 0.3233 0.2305 0.2200 -0.0032 -0.0095 0.0130 54 GLY B N 2007 C CA . GLY B 56 ? 0.2660 0.1940 0.1810 -0.0088 -0.0090 0.0071 54 GLY B CA 2008 C C . GLY B 56 ? 0.2938 0.2177 0.2082 -0.0132 0.0054 0.0093 54 GLY B C 2009 O O . GLY B 56 ? 0.3194 0.2602 0.2516 -0.0169 0.0070 0.0050 54 GLY B O 2010 N N . ARG B 57 ? 0.2952 0.1953 0.1886 -0.0118 0.0172 0.0166 55 ARG B N 2011 C CA . ARG B 57 ? 0.3604 0.2534 0.2522 -0.0162 0.0353 0.0190 55 ARG B CA 2012 C C . ARG B 57 ? 0.3250 0.2348 0.2562 -0.0274 0.0443 0.0132 55 ARG B C 2013 O O . ARG B 57 ? 0.3070 0.2277 0.2508 -0.0297 0.0518 0.0106 55 ARG B O 2014 C CB . ARG B 57 ? 0.3946 0.2543 0.2537 -0.0127 0.0493 0.0292 55 ARG B CB 2015 C CG . ARG B 57 ? 0.5388 0.3840 0.3558 -0.0004 0.0406 0.0339 55 ARG B CG 2016 C CD . ARG B 57 ? 0.7721 0.5814 0.5494 0.0045 0.0560 0.0453 55 ARG B CD 2017 N NE . ARG B 57 ? 0.8510 0.6420 0.5998 0.0160 0.0434 0.0525 55 ARG B NE 2018 C CZ . ARG B 57 ? 0.9961 0.7520 0.7096 0.0223 0.0541 0.0647 55 ARG B CZ 2019 N NH1 . ARG B 57 ? 1.0367 0.7711 0.7387 0.0168 0.0803 0.0709 55 ARG B NH1 2020 N NH2 . ARG B 57 ? 1.0579 0.7996 0.7487 0.0347 0.0397 0.0713 55 ARG B NH2 2021 N N . PRO B 58 ? 0.2806 0.1931 0.2328 -0.0339 0.0428 0.0100 56 PRO B N 2022 C CA . PRO B 58 ? 0.3298 0.2609 0.3218 -0.0445 0.0483 0.0025 56 PRO B CA 2023 C C . PRO B 58 ? 0.2986 0.2597 0.3114 -0.0432 0.0350 -0.0045 56 PRO B C 2024 O O . PRO B 58 ? 0.2460 0.2228 0.2868 -0.0478 0.0411 -0.0085 56 PRO B O 2025 C CB . PRO B 58 ? 0.4055 0.3335 0.4109 -0.0505 0.0440 -0.0019 56 PRO B CB 2026 C CG . PRO B 58 ? 0.3912 0.2897 0.3630 -0.0440 0.0468 0.0069 56 PRO B CG 2027 C CD . PRO B 58 ? 0.3160 0.2144 0.2590 -0.0323 0.0371 0.0118 56 PRO B CD 2028 N N . ASP B 59 ? 0.2934 0.2615 0.2940 -0.0364 0.0183 -0.0053 57 ASP B N 2029 C CA . ASP B 59 ? 0.2316 0.2233 0.2478 -0.0342 0.0070 -0.0101 57 ASP B CA 2030 C C . ASP B 59 ? 0.2507 0.2450 0.2621 -0.0297 0.0130 -0.0077 57 ASP B C 2031 O O . ASP B 59 ? 0.2243 0.2359 0.2585 -0.0300 0.0128 -0.0108 57 ASP B O 2032 C CB . ASP B 59 ? 0.2743 0.2694 0.2790 -0.0290 -0.0089 -0.0114 57 ASP B CB 2033 C CG . ASP B 59 ? 0.3048 0.2998 0.3168 -0.0335 -0.0150 -0.0162 57 ASP B CG 2034 O OD1 . ASP B 59 ? 0.2926 0.2959 0.3276 -0.0409 -0.0134 -0.0217 57 ASP B OD1 2035 O OD2 . ASP B 59 ? 0.3058 0.2926 0.3024 -0.0298 -0.0210 -0.0157 57 ASP B OD2 2036 N N . ALA B 60 ? 0.2713 0.2477 0.2527 -0.0247 0.0176 -0.0029 58 ALA B N 2037 C CA . ALA B 60 ? 0.3138 0.2884 0.2863 -0.0209 0.0250 -0.0022 58 ALA B CA 2038 C C . ALA B 60 ? 0.2909 0.2680 0.2836 -0.0261 0.0429 -0.0027 58 ALA B C 2039 O O . ALA B 60 ? 0.2602 0.2508 0.2708 -0.0249 0.0459 -0.0056 58 ALA B O 2040 C CB . ALA B 60 ? 0.2834 0.2357 0.2162 -0.0150 0.0262 0.0019 58 ALA B CB 2041 N N . GLU B 61 ? 0.3002 0.2638 0.2927 -0.0317 0.0563 0.0002 59 GLU B N 2042 C CA . GLU B 61 ? 0.2985 0.2625 0.3126 -0.0377 0.0773 -0.0004 59 GLU B CA 2043 C C . GLU B 61 ? 0.2778 0.2721 0.3425 -0.0427 0.0727 -0.0078 59 GLU B C 2044 O O . GLU B 61 ? 0.2809 0.2867 0.3693 -0.0431 0.0832 -0.0103 59 GLU B O 2045 C CB . GLU B 61 ? 0.3751 0.3151 0.3791 -0.0434 0.0944 0.0047 59 GLU B CB 2046 C CG . GLU B 61 ? 0.6033 0.5103 0.5546 -0.0366 0.1026 0.0136 59 GLU B CG 2047 C CD . GLU B 61 ? 0.7519 0.6309 0.6883 -0.0403 0.1174 0.0210 59 GLU B CD 2048 O OE1 . GLU B 61 ? 0.7935 0.6792 0.7651 -0.0502 0.1242 0.0178 59 GLU B OE1 2049 O OE2 . GLU B 61 ? 0.7367 0.5862 0.6261 -0.0329 0.1216 0.0297 59 GLU B OE2 2050 N N . TYR B 62 ? 0.2865 0.2938 0.3672 -0.0457 0.0563 -0.0119 60 TYR B N 2051 C CA . TYR B 62 ? 0.2871 0.3235 0.4129 -0.0493 0.0479 -0.0197 60 TYR B CA 2052 C C . TYR B 62 ? 0.2457 0.3005 0.3779 -0.0406 0.0354 -0.0207 60 TYR B C 2053 O O . TYR B 62 ? 0.2936 0.3663 0.4583 -0.0399 0.0394 -0.0237 60 TYR B O 2054 C CB . TYR B 62 ? 0.2844 0.3276 0.4206 -0.0545 0.0327 -0.0253 60 TYR B CB 2055 C CG . TYR B 62 ? 0.3839 0.4576 0.5634 -0.0573 0.0203 -0.0346 60 TYR B CG 2056 C CD1 . TYR B 62 ? 0.3976 0.4851 0.6211 -0.0653 0.0317 -0.0406 60 TYR B CD1 2057 C CD2 . TYR B 62 ? 0.4146 0.5031 0.5915 -0.0513 -0.0028 -0.0375 60 TYR B CD2 2058 C CE1 . TYR B 62 ? 0.4631 0.5814 0.7296 -0.0668 0.0171 -0.0502 60 TYR B CE1 2059 C CE2 . TYR B 62 ? 0.4838 0.5995 0.6963 -0.0518 -0.0171 -0.0457 60 TYR B CE2 2060 C CZ . TYR B 62 ? 0.5565 0.6886 0.8151 -0.0593 -0.0087 -0.0526 60 TYR B CZ 2061 O OH . TYR B 62 ? 0.7103 0.8723 1.0077 -0.0590 -0.0260 -0.0619 60 TYR B OH 2062 N N . TRP B 63 ? 0.2031 0.2528 0.3068 -0.0338 0.0215 -0.0180 61 TRP B N 2063 C CA . TRP B 63 ? 0.2259 0.2884 0.3328 -0.0255 0.0108 -0.0178 61 TRP B CA 2064 C C . TRP B 63 ? 0.2426 0.3033 0.3531 -0.0215 0.0251 -0.0163 61 TRP B C 2065 O O . TRP B 63 ? 0.2708 0.3474 0.4043 -0.0165 0.0222 -0.0175 61 TRP B O 2066 C CB . TRP B 63 ? 0.1842 0.2372 0.2595 -0.0204 -0.0015 -0.0151 61 TRP B CB 2067 C CG . TRP B 63 ? 0.2009 0.2574 0.2741 -0.0225 -0.0157 -0.0175 61 TRP B CG 2068 C CD1 . TRP B 63 ? 0.2666 0.3366 0.3629 -0.0272 -0.0230 -0.0229 61 TRP B CD1 2069 C CD2 . TRP B 63 ? 0.2238 0.2696 0.2711 -0.0200 -0.0237 -0.0160 61 TRP B CD2 2070 N NE1 . TRP B 63 ? 0.2183 0.2841 0.2997 -0.0277 -0.0345 -0.0249 61 TRP B NE1 2071 C CE2 . TRP B 63 ? 0.2205 0.2718 0.2733 -0.0232 -0.0339 -0.0202 61 TRP B CE2 2072 C CE3 . TRP B 63 ? 0.1761 0.2092 0.1987 -0.0157 -0.0233 -0.0129 61 TRP B CE3 2073 C CZ2 . TRP B 63 ? 0.2480 0.2908 0.2810 -0.0216 -0.0410 -0.0205 61 TRP B CZ2 2074 C CZ3 . TRP B 63 ? 0.1702 0.1979 0.1786 -0.0143 -0.0312 -0.0132 61 TRP B CZ3 2075 C CH2 . TRP B 63 ? 0.2670 0.2987 0.2800 -0.0170 -0.0387 -0.0165 61 TRP B CH2 2076 N N . ASN B 64 ? 0.2759 0.3157 0.3621 -0.0230 0.0409 -0.0137 62 ASN B N 2077 C CA . ASN B 64 ? 0.2615 0.2955 0.3472 -0.0202 0.0580 -0.0137 62 ASN B CA 2078 C C . ASN B 64 ? 0.2707 0.3189 0.3982 -0.0240 0.0728 -0.0166 62 ASN B C 2079 O O . ASN B 64 ? 0.2972 0.3464 0.4342 -0.0203 0.0860 -0.0178 62 ASN B O 2080 C CB . ASN B 64 ? 0.2591 0.2644 0.3019 -0.0202 0.0705 -0.0105 62 ASN B CB 2081 C CG . ASN B 64 ? 0.2905 0.2854 0.2984 -0.0142 0.0572 -0.0101 62 ASN B CG 2082 O OD1 . ASN B 64 ? 0.2379 0.2448 0.2546 -0.0103 0.0443 -0.0119 62 ASN B OD1 2083 N ND2 . ASN B 64 ? 0.2798 0.2518 0.2490 -0.0133 0.0606 -0.0077 62 ASN B ND2 2084 N N . SER B 65 ? 0.1987 0.2582 0.3540 -0.0315 0.0716 -0.0191 63 SER B N 2085 C CA . SER B 65 ? 0.2413 0.3191 0.4460 -0.0361 0.0842 -0.0238 63 SER B CA 2086 C C . SER B 65 ? 0.2479 0.3578 0.4934 -0.0306 0.0657 -0.0282 63 SER B C 2087 O O . SER B 65 ? 0.2130 0.3438 0.5061 -0.0317 0.0722 -0.0330 63 SER B O 2088 C CB . SER B 65 ? 0.1930 0.2687 0.4145 -0.0479 0.0921 -0.0263 63 SER B CB 2089 O OG . SER B 65 ? 0.2533 0.3417 0.4835 -0.0506 0.0691 -0.0301 63 SER B OG 2090 N N . GLN B 66 ? 0.1831 0.2961 0.4098 -0.0241 0.0430 -0.0264 64 GLN B N 2091 C CA . GLN B 66 ? 0.2032 0.3421 0.4585 -0.0172 0.0227 -0.0287 64 GLN B CA 2092 C C . GLN B 66 ? 0.2312 0.3673 0.4763 -0.0053 0.0220 -0.0240 64 GLN B C 2093 O O . GLN B 66 ? 0.1344 0.2578 0.3450 -0.0003 0.0127 -0.0197 64 GLN B O 2094 C CB . GLN B 66 ? 0.2280 0.3701 0.4687 -0.0181 -0.0008 -0.0298 64 GLN B CB 2095 C CG . GLN B 66 ? 0.2222 0.3670 0.4766 -0.0302 -0.0012 -0.0363 64 GLN B CG 2096 C CD . GLN B 66 ? 0.3280 0.4961 0.6386 -0.0361 0.0055 -0.0441 64 GLN B CD 2097 O OE1 . GLN B 66 ? 0.3759 0.5363 0.6995 -0.0458 0.0267 -0.0460 64 GLN B OE1 2098 N NE2 . GLN B 66 ? 0.2551 0.4513 0.5999 -0.0297 -0.0123 -0.0486 64 GLN B NE2 2099 N N . LYS B 67 ? 0.3059 0.3973 0.3543 -0.0526 -0.0458 0.0577 65 LYS B N 2100 C CA . LYS B 67 ? 0.3067 0.4031 0.3641 -0.0464 -0.0306 0.0460 65 LYS B CA 2101 C C . LYS B 67 ? 0.2677 0.3425 0.3270 -0.0378 -0.0281 0.0429 65 LYS B C 2102 O O . LYS B 67 ? 0.2074 0.2771 0.2706 -0.0332 -0.0179 0.0317 65 LYS B O 2103 C CB . LYS B 67 ? 0.3559 0.4745 0.4306 -0.0466 -0.0236 0.0485 65 LYS B CB 2104 C CG . LYS B 67 ? 0.5083 0.6326 0.6017 -0.0403 -0.0062 0.0349 65 LYS B CG 2105 C CD . LYS B 67 ? 0.5215 0.6391 0.6348 -0.0325 -0.0043 0.0436 65 LYS B CD 2106 C CE . LYS B 67 ? 0.4454 0.5634 0.5857 -0.0250 0.0132 0.0312 65 LYS B CE 2107 N NZ . LYS B 67 ? 0.4171 0.5309 0.5825 -0.0173 0.0142 0.0450 65 LYS B NZ 2108 N N . ASP B 68 ? 0.2526 0.3181 0.3099 -0.0369 -0.0375 0.0531 66 ASP B N 2109 C CA . ASP B 68 ? 0.2167 0.2689 0.2747 -0.0305 -0.0365 0.0535 66 ASP B CA 2110 C C . ASP B 68 ? 0.2861 0.3212 0.3290 -0.0294 -0.0374 0.0442 66 ASP B C 2111 O O . ASP B 68 ? 0.2565 0.2848 0.3039 -0.0234 -0.0300 0.0399 66 ASP B O 2112 C CB . ASP B 68 ? 0.2818 0.3360 0.3387 -0.0326 -0.0471 0.0660 66 ASP B CB 2113 C CG . ASP B 68 ? 0.3637 0.4122 0.4050 -0.0407 -0.0606 0.0662 66 ASP B CG 2114 O OD1 . ASP B 68 ? 0.4251 0.4732 0.4632 -0.0451 -0.0628 0.0636 66 ASP B OD1 2115 O OD2 . ASP B 68 ? 0.4881 0.5350 0.5232 -0.0435 -0.0689 0.0693 66 ASP B OD2 2116 N N . ILE B 69 ? 0.2536 0.2823 0.2827 -0.0349 -0.0462 0.0424 67 ILE B N 2117 C CA . ILE B 69 ? 0.2402 0.2544 0.2581 -0.0338 -0.0463 0.0338 67 ILE B CA 2118 C C . ILE B 69 ? 0.2507 0.2690 0.2713 -0.0316 -0.0350 0.0248 67 ILE B C 2119 O O . ILE B 69 ? 0.2125 0.2210 0.2313 -0.0268 -0.0294 0.0179 67 ILE B O 2120 C CB . ILE B 69 ? 0.3073 0.3155 0.3188 -0.0402 -0.0569 0.0352 67 ILE B CB 2121 C CG1 . ILE B 69 ? 0.3392 0.3421 0.3497 -0.0437 -0.0674 0.0389 67 ILE B CG1 2122 C CG2 . ILE B 69 ? 0.2983 0.2938 0.3026 -0.0386 -0.0558 0.0273 67 ILE B CG2 2123 C CD1 . ILE B 69 ? 0.4147 0.4104 0.4287 -0.0503 -0.0771 0.0399 67 ILE B CD1 2124 N N . LEU B 70 ? 0.2140 0.2502 0.2394 -0.0363 -0.0314 0.0242 68 LEU B N 2125 C CA . LEU B 70 ? 0.2196 0.2667 0.2481 -0.0367 -0.0197 0.0123 68 LEU B CA 2126 C C . LEU B 70 ? 0.2818 0.3240 0.3247 -0.0292 -0.0069 0.0034 68 LEU B C 2127 O O . LEU B 70 ? 0.2597 0.2964 0.3027 -0.0272 0.0002 -0.0074 68 LEU B O 2128 C CB . LEU B 70 ? 0.2965 0.3722 0.3293 -0.0443 -0.0165 0.0120 68 LEU B CB 2129 C CG . LEU B 70 ? 0.3186 0.4080 0.3423 -0.0535 -0.0263 0.0214 68 LEU B CG 2130 C CD1 . LEU B 70 ? 0.2189 0.3432 0.2482 -0.0616 -0.0229 0.0238 68 LEU B CD1 2131 C CD2 . LEU B 70 ? 0.3101 0.3987 0.3249 -0.0558 -0.0257 0.0160 68 LEU B CD2 2132 N N . GLU B 71 ? 0.2283 0.2730 0.2874 -0.0251 -0.0042 0.0093 69 GLU B N 2133 C CA . GLU B 71 ? 0.2133 0.2544 0.2954 -0.0178 0.0084 0.0040 69 GLU B CA 2134 C C . GLU B 71 ? 0.1853 0.2075 0.2647 -0.0120 0.0059 0.0083 69 GLU B C 2135 O O . GLU B 71 ? 0.1730 0.1899 0.2691 -0.0072 0.0164 0.0015 69 GLU B O 2136 C CB . GLU B 71 ? 0.2094 0.2616 0.3168 -0.0148 0.0132 0.0114 69 GLU B CB 2137 C CG . GLU B 71 ? 0.1751 0.2502 0.2913 -0.0199 0.0212 0.0018 69 GLU B CG 2138 C CD . GLU B 71 ? 0.2333 0.3170 0.3588 -0.0218 0.0364 -0.0213 69 GLU B CD 2139 O OE1 . GLU B 71 ? 0.2709 0.3408 0.4090 -0.0166 0.0442 -0.0292 69 GLU B OE1 2140 O OE2 . GLU B 71 ? 0.1970 0.3044 0.3179 -0.0297 0.0406 -0.0318 69 GLU B OE2 2141 N N . ASP B 72 ? 0.2432 0.2571 0.3036 -0.0132 -0.0071 0.0182 70 ASP B N 2142 C CA . ASP B 72 ? 0.2658 0.2669 0.3198 -0.0094 -0.0095 0.0206 70 ASP B CA 2143 C C . ASP B 72 ? 0.2128 0.2049 0.2575 -0.0095 -0.0050 0.0073 70 ASP B C 2144 O O . ASP B 72 ? 0.2240 0.2089 0.2759 -0.0050 0.0010 0.0047 70 ASP B O 2145 C CB . ASP B 72 ? 0.1770 0.1748 0.2113 -0.0128 -0.0233 0.0278 70 ASP B CB 2146 C CG . ASP B 72 ? 0.3579 0.3670 0.4002 -0.0132 -0.0284 0.0422 70 ASP B CG 2147 O OD1 . ASP B 72 ? 0.3134 0.3308 0.3790 -0.0086 -0.0215 0.0509 70 ASP B OD1 2148 O OD2 . ASP B 72 ? 0.3971 0.4081 0.4253 -0.0186 -0.0394 0.0450 70 ASP B OD2 2149 N N . GLU B 73 ? 0.2425 0.2375 0.2733 -0.0154 -0.0086 0.0012 71 GLU B N 2150 C CA . GLU B 73 ? 0.1710 0.1624 0.1930 -0.0171 -0.0056 -0.0093 71 GLU B CA 2151 C C . GLU B 73 ? 0.1730 0.1715 0.2113 -0.0162 0.0088 -0.0219 71 GLU B C 2152 O O . GLU B 73 ? 0.2356 0.2267 0.2746 -0.0143 0.0140 -0.0296 71 GLU B O 2153 C CB . GLU B 73 ? 0.2078 0.2074 0.2173 -0.0247 -0.0131 -0.0081 71 GLU B CB 2154 C CG . GLU B 73 ? 0.2383 0.2271 0.2372 -0.0260 -0.0262 0.0005 71 GLU B CG 2155 C CD . GLU B 73 ? 0.3499 0.3219 0.3407 -0.0221 -0.0279 -0.0032 71 GLU B CD 2156 O OE1 . GLU B 73 ? 0.2605 0.2297 0.2462 -0.0242 -0.0300 -0.0055 71 GLU B OE1 2157 O OE2 . GLU B 73 ? 0.3640 0.3288 0.3549 -0.0173 -0.0272 -0.0023 71 GLU B OE2 2158 N N . ARG B 74 ? 0.1702 0.1840 0.2239 -0.0180 0.0159 -0.0257 72 ARG B N 2159 C CA . ARG B 74 ? 0.2213 0.2447 0.2949 -0.0187 0.0315 -0.0429 72 ARG B CA 2160 C C . ARG B 74 ? 0.2694 0.2790 0.3692 -0.0104 0.0407 -0.0440 72 ARG B C 2161 O O . ARG B 74 ? 0.1921 0.2018 0.3069 -0.0107 0.0524 -0.0597 72 ARG B O 2162 C CB . ARG B 74 ? 0.2113 0.2571 0.2978 -0.0229 0.0379 -0.0484 72 ARG B CB 2163 C CG . ARG B 74 ? 0.2238 0.2908 0.2887 -0.0332 0.0312 -0.0482 72 ARG B CG 2164 C CD . ARG B 74 ? 0.2137 0.3034 0.2872 -0.0372 0.0334 -0.0468 72 ARG B CD 2165 N NE . ARG B 74 ? 0.2274 0.3419 0.2821 -0.0482 0.0266 -0.0436 72 ARG B NE 2166 C CZ . ARG B 74 ? 0.2757 0.4146 0.3316 -0.0541 0.0249 -0.0382 72 ARG B CZ 2167 N NH1 . ARG B 74 ? 0.1879 0.3282 0.2622 -0.0496 0.0300 -0.0370 72 ARG B NH1 2168 N NH2 . ARG B 74 ? 0.2421 0.4062 0.2830 -0.0649 0.0177 -0.0314 72 ARG B NH2 2169 N N . ALA B 75 ? 0.1861 0.1865 0.2934 -0.0040 0.0352 -0.0264 73 ALA B N 2170 C CA . ALA B 75 ? 0.2021 0.1936 0.3392 0.0037 0.0426 -0.0208 73 ALA B CA 2171 C C . ALA B 75 ? 0.1893 0.1673 0.3139 0.0058 0.0389 -0.0180 73 ALA B C 2172 O O . ALA B 75 ? 0.1840 0.1559 0.3340 0.0107 0.0466 -0.0164 73 ALA B O 2173 C CB . ALA B 75 ? 0.1970 0.1921 0.3501 0.0083 0.0381 0.0006 73 ALA B CB 2174 N N . ALA B 76 ? 0.1931 0.1673 0.2827 0.0023 0.0275 -0.0168 74 ALA B N 2175 C CA . ALA B 76 ? 0.2388 0.2023 0.3144 0.0043 0.0229 -0.0131 74 ALA B CA 2176 C C . ALA B 76 ? 0.2286 0.1858 0.3181 0.0061 0.0331 -0.0236 74 ALA B C 2177 O O . ALA B 76 ? 0.2118 0.1626 0.3065 0.0102 0.0328 -0.0151 74 ALA B O 2178 C CB . ALA B 76 ? 0.2004 0.1609 0.2424 -0.0001 0.0113 -0.0145 74 ALA B CB 2179 N N . VAL B 77 ? 0.2057 0.1677 0.3020 0.0018 0.0422 -0.0419 75 VAL B N 2180 C CA . VAL B 77 ? 0.2347 0.1919 0.3478 0.0021 0.0528 -0.0543 75 VAL B CA 2181 C C . VAL B 77 ? 0.3501 0.3005 0.5017 0.0095 0.0603 -0.0446 75 VAL B C 2182 O O . VAL B 77 ? 0.2617 0.2040 0.4239 0.0120 0.0635 -0.0429 75 VAL B O 2183 C CB . VAL B 77 ? 0.3270 0.2970 0.4490 -0.0054 0.0642 -0.0789 75 VAL B CB 2184 C CG1 . VAL B 77 ? 0.3801 0.3602 0.4675 -0.0137 0.0571 -0.0855 75 VAL B CG1 2185 C CG2 . VAL B 77 ? 0.2300 0.2124 0.3741 -0.0063 0.0718 -0.0848 75 VAL B CG2 2186 N N . ASP B 78 ? 0.2711 0.2267 0.4461 0.0127 0.0625 -0.0353 76 ASP B N 2187 C CA . ASP B 78 ? 0.2265 0.1792 0.4458 0.0197 0.0692 -0.0209 76 ASP B CA 2188 C C . ASP B 78 ? 0.2810 0.2360 0.4923 0.0238 0.0574 0.0080 76 ASP B C 2189 O O . ASP B 78 ? 0.2062 0.1585 0.4320 0.0271 0.0580 0.0204 76 ASP B O 2190 C CB . ASP B 78 ? 0.1828 0.1429 0.4397 0.0214 0.0792 -0.0245 76 ASP B CB 2191 C CG . ASP B 78 ? 0.2101 0.1742 0.4820 0.0145 0.0924 -0.0528 76 ASP B CG 2192 O OD1 . ASP B 78 ? 0.2722 0.2336 0.5379 0.0093 0.0942 -0.0632 76 ASP B OD1 2193 O OD2 . ASP B 78 ? 0.2905 0.2645 0.5760 0.0120 0.0987 -0.0630 76 ASP B OD2 2194 N N . THR B 79 ? 0.2329 0.1963 0.4218 0.0222 0.0468 0.0184 77 THR B N 2195 C CA . THR B 79 ? 0.2246 0.1978 0.4082 0.0239 0.0363 0.0443 77 THR B CA 2196 C C . THR B 79 ? 0.2357 0.2076 0.3825 0.0216 0.0266 0.0461 77 THR B C 2197 O O . THR B 79 ? 0.2434 0.2277 0.3870 0.0218 0.0197 0.0653 77 THR B O 2198 C CB . THR B 79 ? 0.1771 0.1613 0.3477 0.0213 0.0280 0.0516 77 THR B CB 2199 O OG1 . THR B 79 ? 0.1936 0.1727 0.3237 0.0157 0.0210 0.0358 77 THR B OG1 2200 C CG2 . THR B 79 ? 0.2246 0.2127 0.4334 0.0239 0.0380 0.0502 77 THR B CG2 2201 N N . TYR B 80 ? 0.2074 0.1681 0.3276 0.0186 0.0264 0.0263 78 TYR B N 2202 C CA . TYR B 80 ? 0.2114 0.1698 0.2987 0.0167 0.0183 0.0249 78 TYR B CA 2203 C C . TYR B 80 ? 0.2473 0.1958 0.3386 0.0181 0.0250 0.0157 78 TYR B C 2204 O O . TYR B 80 ? 0.1905 0.1423 0.2876 0.0205 0.0249 0.0266 78 TYR B O 2205 C CB . TYR B 80 ? 0.2220 0.1770 0.2766 0.0118 0.0102 0.0131 78 TYR B CB 2206 C CG . TYR B 80 ? 0.1979 0.1484 0.2238 0.0099 0.0034 0.0077 78 TYR B CG 2207 C CD1 . TYR B 80 ? 0.1940 0.1537 0.2094 0.0097 -0.0028 0.0170 78 TYR B CD1 2208 C CD2 . TYR B 80 ? 0.2392 0.1802 0.2508 0.0076 0.0033 -0.0066 78 TYR B CD2 2209 C CE1 . TYR B 80 ? 0.2031 0.1597 0.1957 0.0080 -0.0074 0.0086 78 TYR B CE1 2210 C CE2 . TYR B 80 ? 0.1799 0.1163 0.1713 0.0067 -0.0021 -0.0114 78 TYR B CE2 2211 C CZ . TYR B 80 ? 0.2794 0.2222 0.2622 0.0073 -0.0068 -0.0054 78 TYR B CZ 2212 O OH . TYR B 80 ? 0.3385 0.2777 0.3052 0.0065 -0.0103 -0.0132 78 TYR B OH 2213 N N . CYS B 81 ? 0.1985 0.1388 0.2876 0.0157 0.0307 -0.0034 79 CYS B N 2214 C CA . CYS B 81 ? 0.2288 0.1617 0.3218 0.0156 0.0371 -0.0138 79 CYS B CA 2215 C C . CYS B 81 ? 0.2625 0.1937 0.3957 0.0197 0.0471 -0.0073 79 CYS B C 2216 O O . CYS B 81 ? 0.2514 0.1817 0.3874 0.0219 0.0465 0.0019 79 CYS B O 2217 C CB . CYS B 81 ? 0.2283 0.1604 0.3138 0.0100 0.0416 -0.0350 79 CYS B CB 2218 S SG . CYS B 81 ? 0.2420 0.1770 0.2880 0.0049 0.0295 -0.0380 79 CYS B SG 2219 N N . ARG B 82 ? 0.2241 0.1558 0.3924 0.0205 0.0570 -0.0119 80 ARG B N 2220 C CA . ARG B 82 ? 0.1827 0.1136 0.3961 0.0234 0.0668 -0.0060 80 ARG B CA 2221 C C . ARG B 82 ? 0.2516 0.1880 0.4821 0.0293 0.0619 0.0249 80 ARG B C 2222 O O . ARG B 82 ? 0.2372 0.1774 0.4849 0.0294 0.0640 0.0343 80 ARG B O 2223 C CB . ARG B 82 ? 0.2477 0.1858 0.4932 0.0200 0.0766 -0.0164 80 ARG B CB 2224 C CG . ARG B 82 ? 0.2566 0.1979 0.4932 0.0113 0.0829 -0.0450 80 ARG B CG 2225 C CD . ARG B 82 ? 0.2481 0.1976 0.5207 0.0066 0.0938 -0.0565 80 ARG B CD 2226 N NE . ARG B 82 ? 0.2579 0.2154 0.5252 -0.0032 0.0995 -0.0819 80 ARG B NE 2227 C CZ . ARG B 82 ? 0.2883 0.2553 0.5297 -0.0092 0.0988 -0.0991 80 ARG B CZ 2228 N NH1 . ARG B 82 ? 0.2967 0.2637 0.5168 -0.0060 0.0934 -0.0953 80 ARG B NH1 2229 N NH2 . ARG B 82 ? 0.2881 0.2678 0.5272 -0.0193 0.1034 -0.1193 80 ARG B NH2 2230 N N . HIS B 83 ? 0.2099 0.1577 0.4264 0.0298 0.0527 0.0407 81 HIS B N 2231 C CA . HIS B 83 ? 0.2164 0.1808 0.4420 0.0321 0.0458 0.0716 81 HIS B CA 2232 C C . HIS B 83 ? 0.2299 0.1993 0.4285 0.0306 0.0394 0.0774 81 HIS B C 2233 O O . HIS B 83 ? 0.2095 0.1887 0.4325 0.0326 0.0407 0.0975 81 HIS B O 2234 C CB . HIS B 83 ? 0.1984 0.1779 0.4057 0.0302 0.0358 0.0835 81 HIS B CB 2235 C CG . HIS B 83 ? 0.2660 0.2706 0.4763 0.0297 0.0275 0.1140 81 HIS B CG 2236 N ND1 . HIS B 83 ? 0.2749 0.2958 0.5317 0.0327 0.0298 0.1426 81 HIS B ND1 2237 C CD2 . HIS B 83 ? 0.2076 0.2281 0.3827 0.0256 0.0176 0.1208 81 HIS B CD2 2238 C CE1 . HIS B 83 ? 0.2662 0.3155 0.5133 0.0295 0.0204 0.1678 81 HIS B CE1 2239 N NE2 . HIS B 83 ? 0.2755 0.3255 0.4719 0.0248 0.0134 0.1529 81 HIS B NE2 2240 N N . ASN B 84 ? 0.2184 0.1830 0.3701 0.0271 0.0328 0.0608 82 ASN B N 2241 C CA . ASN B 84 ? 0.1846 0.1553 0.3100 0.0257 0.0274 0.0634 82 ASN B CA 2242 C C . ASN B 84 ? 0.1843 0.1448 0.3255 0.0275 0.0351 0.0585 82 ASN B C 2243 O O . ASN B 84 ? 0.2707 0.2418 0.4104 0.0278 0.0332 0.0709 82 ASN B O 2244 C CB . ASN B 84 ? 0.1843 0.1509 0.2638 0.0220 0.0195 0.0461 82 ASN B CB 2245 C CG . ASN B 84 ? 0.2321 0.2149 0.2948 0.0189 0.0102 0.0546 82 ASN B CG 2246 O OD1 . ASN B 84 ? 0.2553 0.2586 0.3336 0.0187 0.0079 0.0762 82 ASN B OD1 2247 N ND2 . ASN B 84 ? 0.1892 0.1653 0.2232 0.0157 0.0045 0.0389 82 ASN B ND2 2248 N N . TYR B 85 ? 0.2612 0.2045 0.4186 0.0276 0.0440 0.0401 83 TYR B N 2249 C CA . TYR B 85 ? 0.2403 0.1744 0.4161 0.0280 0.0520 0.0333 83 TYR B CA 2250 C C . TYR B 85 ? 0.2950 0.2376 0.5167 0.0316 0.0562 0.0586 83 TYR B C 2251 O O . TYR B 85 ? 0.2707 0.2174 0.4990 0.0322 0.0565 0.0686 83 TYR B O 2252 C CB . TYR B 85 ? 0.2532 0.1750 0.4409 0.0249 0.0613 0.0073 83 TYR B CB 2253 C CG . TYR B 85 ? 0.2513 0.1731 0.4474 0.0205 0.0667 -0.0039 83 TYR B CG 2254 C CD1 . TYR B 85 ? 0.3166 0.2339 0.4819 0.0170 0.0646 -0.0197 83 TYR B CD1 2255 C CD2 . TYR B 85 ? 0.2732 0.2015 0.5113 0.0193 0.0739 0.0024 83 TYR B CD2 2256 C CE1 . TYR B 85 ? 0.2944 0.2138 0.4682 0.0126 0.0690 -0.0284 83 TYR B CE1 2257 C CE2 . TYR B 85 ? 0.3010 0.2297 0.5496 0.0149 0.0790 -0.0081 83 TYR B CE2 2258 C CZ . TYR B 85 ? 0.3286 0.2528 0.5436 0.0117 0.0763 -0.0233 83 TYR B CZ 2259 O OH . TYR B 85 ? 0.3751 0.3014 0.6013 0.0070 0.0810 -0.0326 83 TYR B OH 2260 N N . GLY B 86 ? 0.3099 0.2610 0.5620 0.0324 0.0583 0.0695 84 GLY B N 2261 C CA . GLY B 86 ? 0.1967 0.1667 0.4903 0.0326 0.0603 0.0945 84 GLY B CA 2262 C C . GLY B 86 ? 0.1924 0.1820 0.4744 0.0340 0.0511 0.1238 84 GLY B C 2263 O O . GLY B 86 ? 0.2142 0.2182 0.5202 0.0331 0.0526 0.1396 84 GLY B O 2264 N N . VAL B 87 ? 0.2034 0.2009 0.4445 0.0334 0.0411 0.1280 85 VAL B N 2265 C CA . VAL B 87 ? 0.2434 0.2724 0.4667 0.0305 0.0317 0.1520 85 VAL B CA 2266 C C . VAL B 87 ? 0.2388 0.2697 0.4414 0.0291 0.0314 0.1471 85 VAL B C 2267 O O . VAL B 87 ? 0.2145 0.2710 0.4295 0.0279 0.0292 0.1725 85 VAL B O 2268 C CB . VAL B 87 ? 0.3099 0.3537 0.4894 0.0261 0.0214 0.1474 85 VAL B CB 2269 C CG1 . VAL B 87 ? 0.2986 0.3790 0.4542 0.0207 0.0129 0.1646 85 VAL B CG1 2270 C CG2 . VAL B 87 ? 0.3198 0.3694 0.5231 0.0269 0.0207 0.1597 85 VAL B CG2 2271 N N . VAL B 88 ? 0.3133 0.3202 0.4869 0.0290 0.0335 0.1167 86 VAL B N 2272 C CA . VAL B 88 ? 0.3004 0.3102 0.4489 0.0277 0.0322 0.1103 86 VAL B CA 2273 C C . VAL B 88 ? 0.2723 0.2635 0.4445 0.0296 0.0409 0.1031 86 VAL B C 2274 O O . VAL B 88 ? 0.2946 0.2904 0.4522 0.0288 0.0404 0.1018 86 VAL B O 2275 C CB . VAL B 88 ? 0.2867 0.2888 0.3844 0.0254 0.0269 0.0846 86 VAL B CB 2276 C CG1 . VAL B 88 ? 0.2563 0.2758 0.3331 0.0223 0.0188 0.0886 86 VAL B CG1 2277 C CG2 . VAL B 88 ? 0.2006 0.1723 0.2942 0.0262 0.0315 0.0583 86 VAL B CG2 2278 N N . GLU B 89 ? 0.2093 0.1816 0.4193 0.0315 0.0494 0.0968 87 GLU B N 2279 C CA . GLU B 89 ? 0.2563 0.2101 0.4857 0.0313 0.0581 0.0823 87 GLU B CA 2280 C C . GLU B 89 ? 0.2439 0.2092 0.4972 0.0317 0.0597 0.1027 87 GLU B C 2281 O O . GLU B 89 ? 0.2262 0.1817 0.4751 0.0304 0.0632 0.0904 87 GLU B O 2282 C CB . GLU B 89 ? 0.3244 0.2693 0.5834 0.0284 0.0664 0.0639 87 GLU B CB 2283 C CG . GLU B 89 ? 0.4293 0.3896 0.7382 0.0281 0.0706 0.0817 87 GLU B CG 2284 C CD . GLU B 89 ? 0.6556 0.6200 1.0017 0.0255 0.0776 0.0824 87 GLU B CD 2285 O OE1 . GLU B 89 ? 0.7471 0.7301 1.1218 0.0271 0.0763 0.1097 87 GLU B OE1 2286 O OE2 . GLU B 89 ? 0.6666 0.6196 1.0136 0.0213 0.0839 0.0567 87 GLU B OE2 2287 N N . SER B 90 ? 0.2652 0.2574 0.5410 0.0319 0.0563 0.1334 88 SER B N 2288 C CA . SER B 90 ? 0.3378 0.3493 0.6401 0.0308 0.0572 0.1531 88 SER B CA 2289 C C . SER B 90 ? 0.3355 0.3531 0.6022 0.0306 0.0530 0.1597 88 SER B C 2290 O O . SER B 90 ? 0.2884 0.3108 0.5707 0.0297 0.0557 0.1648 88 SER B O 2291 C CB . SER B 90 ? 0.2894 0.3362 0.6272 0.0302 0.0539 0.1848 88 SER B CB 2292 O OG . SER B 90 ? 0.3063 0.3808 0.6122 0.0288 0.0440 0.2047 88 SER B OG 2293 N N . PHE B 91 ? 0.2231 0.2501 0.4362 0.0289 0.0456 0.1479 89 PHE B N 2294 C CA . PHE B 91 ? 0.2728 0.3147 0.4475 0.0269 0.0418 0.1433 89 PHE B CA 2295 C C . PHE B 91 ? 0.2783 0.2961 0.4141 0.0271 0.0421 0.1085 89 PHE B C 2296 O O . PHE B 91 ? 0.3176 0.3450 0.4224 0.0261 0.0396 0.1009 89 PHE B O 2297 C CB . PHE B 91 ? 0.2825 0.3646 0.4325 0.0233 0.0337 0.1604 89 PHE B CB 2298 C CG . PHE B 91 ? 0.3066 0.3896 0.4337 0.0221 0.0285 0.1509 89 PHE B CG 2299 C CD1 . PHE B 91 ? 0.3065 0.3800 0.3888 0.0210 0.0254 0.1224 89 PHE B CD1 2300 C CD2 . PHE B 91 ? 0.3273 0.4216 0.4818 0.0218 0.0266 0.1723 89 PHE B CD2 2301 C CE1 . PHE B 91 ? 0.3761 0.4505 0.4402 0.0191 0.0204 0.1143 89 PHE B CE1 2302 C CE2 . PHE B 91 ? 0.3412 0.4378 0.4749 0.0201 0.0215 0.1643 89 PHE B CE2 2303 C CZ . PHE B 91 ? 0.3512 0.4375 0.4390 0.0185 0.0182 0.1348 89 PHE B CZ 2304 N N . THR B 92 ? 0.2389 0.2286 0.3788 0.0280 0.0454 0.0883 90 THR B N 2305 C CA . THR B 92 ? 0.2747 0.2452 0.3830 0.0273 0.0451 0.0595 90 THR B CA 2306 C C . THR B 92 ? 0.2947 0.2433 0.4248 0.0263 0.0528 0.0447 90 THR B C 2307 O O . THR B 92 ? 0.2936 0.2389 0.4193 0.0252 0.0549 0.0382 90 THR B O 2308 C CB . THR B 92 ? 0.3021 0.2665 0.3869 0.0268 0.0405 0.0467 90 THR B CB 2309 O OG1 . THR B 92 ? 0.2451 0.2024 0.3584 0.0273 0.0437 0.0506 90 THR B OG1 2310 C CG2 . THR B 92 ? 0.2718 0.2590 0.3313 0.0260 0.0330 0.0553 90 THR B CG2 2311 N N . VAL B 93 ? 0.2648 0.2013 0.4193 0.0258 0.0575 0.0384 91 VAL B N 2312 C CA . VAL B 93 ? 0.2744 0.1948 0.4552 0.0229 0.0665 0.0214 91 VAL B CA 2313 C C . VAL B 93 ? 0.2733 0.1961 0.4868 0.0221 0.0717 0.0312 91 VAL B C 2314 O O . VAL B 93 ? 0.3024 0.2213 0.5144 0.0173 0.0749 0.0149 91 VAL B O 2315 C CB . VAL B 93 ? 0.2387 0.1588 0.4438 0.0208 0.0702 0.0155 91 VAL B CB 2316 C CG1 . VAL B 93 ? 0.2820 0.2036 0.5084 0.0135 0.0773 -0.0033 91 VAL B CG1 2317 C CG2 . VAL B 93 ? 0.1959 0.1111 0.3713 0.0211 0.0659 0.0044 91 VAL B CG2 2318 N N . GLN B 94 ? 0.2397 0.1760 0.4810 0.0251 0.0711 0.0595 92 GLN B N 2319 C CA . GLN B 94 ? 0.2565 0.2024 0.5337 0.0234 0.0750 0.0715 92 GLN B CA 2320 C C . GLN B 94 ? 0.2799 0.2328 0.5422 0.0252 0.0719 0.0883 92 GLN B C 2321 O O . GLN B 94 ? 0.3215 0.2841 0.6114 0.0239 0.0742 0.1003 92 GLN B O 2322 C CB . GLN B 94 ? 0.2406 0.2056 0.5622 0.0246 0.0757 0.0955 92 GLN B CB 2323 C CG . GLN B 94 ? 0.3117 0.2733 0.6549 0.0230 0.0801 0.0832 92 GLN B CG 2324 C CD . GLN B 94 ? 0.4558 0.4375 0.8538 0.0241 0.0827 0.1067 92 GLN B CD 2325 O OE1 . GLN B 94 ? 0.5307 0.5285 0.9561 0.0251 0.0822 0.1277 92 GLN B OE1 2326 N NE2 . GLN B 94 ? 0.5152 0.4985 0.9319 0.0238 0.0853 0.1045 92 GLN B NE2 2327 N N . ARG B 95 ? 0.2226 0.1852 0.4331 0.0258 0.0643 0.0828 93 ARG B N 2328 C CA . ARG B 95 ? 0.2881 0.2692 0.4751 0.0258 0.0604 0.0920 93 ARG B CA 2329 C C . ARG B 95 ? 0.2792 0.2487 0.4699 0.0236 0.0649 0.0791 93 ARG B C 2330 O O . ARG B 95 ? 0.2323 0.1838 0.4086 0.0216 0.0666 0.0536 93 ARG B O 2331 C CB . ARG B 95 ? 0.3163 0.3063 0.4515 0.0265 0.0533 0.0812 93 ARG B CB 2332 C CG . ARG B 95 ? 0.2709 0.2810 0.3816 0.0264 0.0509 0.0851 93 ARG B CG 2333 C CD . ARG B 95 ? 0.2651 0.2839 0.3334 0.0268 0.0454 0.0722 93 ARG B CD 2334 N NE . ARG B 95 ? 0.2182 0.2539 0.2638 0.0269 0.0449 0.0686 93 ARG B NE 2335 C CZ . ARG B 95 ? 0.2578 0.3278 0.3009 0.0252 0.0439 0.0858 93 ARG B CZ 2336 N NH1 . ARG B 95 ? 0.2269 0.3192 0.2903 0.0231 0.0423 0.1116 93 ARG B NH1 2337 N NH2 . ARG B 95 ? 0.2304 0.3159 0.2530 0.0252 0.0449 0.0781 93 ARG B NH2 2338 N N . ARG B 96 ? 0.2397 0.2235 0.4507 0.0233 0.0662 0.0988 94 ARG B N 2339 C CA . ARG B 96 ? 0.3190 0.2965 0.5339 0.0208 0.0697 0.0904 94 ARG B CA 2340 C C . ARG B 96 ? 0.3178 0.3220 0.5184 0.0216 0.0665 0.1087 94 ARG B C 2341 O O . ARG B 96 ? 0.3069 0.3338 0.5316 0.0217 0.0658 0.1379 94 ARG B O 2342 C CB . ARG B 96 ? 0.3489 0.3139 0.6201 0.0181 0.0776 0.0948 94 ARG B CB 2343 C CG . ARG B 96 ? 0.3575 0.3028 0.6480 0.0160 0.0825 0.0728 94 ARG B CG 2344 C CD . ARG B 96 ? 0.3000 0.2286 0.5650 0.0114 0.0846 0.0400 94 ARG B CD 2345 N NE . ARG B 96 ? 0.4648 0.3909 0.7426 0.0070 0.0881 0.0178 94 ARG B NE 2346 C CZ . ARG B 96 ? 0.5287 0.4515 0.7877 0.0074 0.0860 0.0077 94 ARG B CZ 2347 N NH1 . ARG B 96 ? 0.5707 0.4900 0.7982 0.0128 0.0804 0.0157 94 ARG B NH1 2348 N NH2 . ARG B 96 ? 0.4991 0.4239 0.7722 0.0025 0.0901 -0.0102 94 ARG B NH2 2349 N N . VAL B 97 ? 0.2437 0.2485 0.4080 0.0218 0.0648 0.0928 95 VAL B N 2350 C CA . VAL B 97 ? 0.2507 0.2808 0.4023 0.0223 0.0635 0.1053 95 VAL B CA 2351 C C . VAL B 97 ? 0.2346 0.2542 0.3866 0.0206 0.0666 0.0932 95 VAL B C 2352 O O . VAL B 97 ? 0.2099 0.2139 0.3393 0.0204 0.0662 0.0699 95 VAL B O 2353 C CB . VAL B 97 ? 0.2976 0.3454 0.4055 0.0246 0.0589 0.0983 95 VAL B CB 2354 C CG1 . VAL B 97 ? 0.3256 0.4066 0.4242 0.0243 0.0591 0.1117 95 VAL B CG1 2355 C CG2 . VAL B 97 ? 0.2579 0.3151 0.3626 0.0249 0.0553 0.1063 95 VAL B CG2 2356 N N . TYR B 98 ? 0.2000 0.2305 0.3802 0.0186 0.0694 0.1111 96 TYR B N 2357 C CA . TYR B 98 ? 0.2505 0.2722 0.4347 0.0158 0.0723 0.1007 96 TYR B CA 2358 C C . TYR B 98 ? 0.2113 0.2493 0.3591 0.0184 0.0702 0.0956 96 TYR B C 2359 O O . TYR B 98 ? 0.2409 0.3033 0.3696 0.0212 0.0680 0.1052 96 TYR B O 2360 C CB . TYR B 98 ? 0.3042 0.3277 0.5374 0.0120 0.0766 0.1192 96 TYR B CB 2361 C CG . TYR B 98 ? 0.3318 0.3878 0.5806 0.0127 0.0754 0.1530 96 TYR B CG 2362 C CD1 . TYR B 98 ? 0.3558 0.4335 0.5882 0.0127 0.0749 0.1594 96 TYR B CD1 2363 C CD2 . TYR B 98 ? 0.2213 0.2894 0.5051 0.0127 0.0750 0.1804 96 TYR B CD2 2364 C CE1 . TYR B 98 ? 0.3693 0.4827 0.6157 0.0120 0.0739 0.1911 96 TYR B CE1 2365 C CE2 . TYR B 98 ? 0.2892 0.3935 0.5857 0.0132 0.0712 0.2116 96 TYR B CE2 2366 C CZ . TYR B 98 ? 0.3795 0.5071 0.6567 0.0120 0.0711 0.2173 96 TYR B CZ 2367 O OH . TYR B 98 ? 0.3232 0.4889 0.6079 0.0131 0.0646 0.2432 96 TYR B OH 2368 N N . PRO B 99 ? 0.2317 0.2582 0.3711 0.0167 0.0714 0.0790 97 PRO B N 2369 C CA . PRO B 99 ? 0.2525 0.2923 0.3624 0.0199 0.0702 0.0729 97 PRO B CA 2370 C C . PRO B 99 ? 0.2498 0.3139 0.3695 0.0196 0.0724 0.0905 97 PRO B C 2371 O O . PRO B 99 ? 0.2542 0.3177 0.4060 0.0154 0.0746 0.1037 97 PRO B O 2372 C CB . PRO B 99 ? 0.2673 0.2876 0.3714 0.0171 0.0702 0.0525 97 PRO B CB 2373 C CG . PRO B 99 ? 0.3063 0.3126 0.4426 0.0102 0.0731 0.0519 97 PRO B CG 2374 C CD . PRO B 99 ? 0.2714 0.2743 0.4262 0.0111 0.0737 0.0622 97 PRO B CD 2375 N N A GLU B 100 ? 0.2001 0.2868 0.2958 0.0236 0.0724 0.0903 98 GLU B N 2376 N N B GLU B 100 ? 0.1999 0.2858 0.2956 0.0235 0.0725 0.0896 98 GLU B N 2377 C CA A GLU B 100 ? 0.2249 0.3339 0.3252 0.0233 0.0751 0.1008 98 GLU B CA 2378 C CA B GLU B 100 ? 0.2081 0.3180 0.3091 0.0232 0.0751 0.1019 98 GLU B CA 2379 C C A GLU B 100 ? 0.2534 0.3446 0.3492 0.0231 0.0757 0.0839 98 GLU B C 2380 C C B GLU B 100 ? 0.2334 0.3308 0.3263 0.0239 0.0760 0.0853 98 GLU B C 2381 O O A GLU B 100 ? 0.1957 0.2702 0.2745 0.0251 0.0739 0.0650 98 GLU B O 2382 O O B GLU B 100 ? 0.1977 0.2869 0.2692 0.0277 0.0751 0.0673 98 GLU B O 2383 C CB A GLU B 100 ? 0.2770 0.4200 0.3540 0.0270 0.0765 0.1023 98 GLU B CB 2384 C CB B GLU B 100 ? 0.2293 0.3753 0.3100 0.0262 0.0761 0.1074 98 GLU B CB 2385 C CG A GLU B 100 ? 0.3857 0.5213 0.4352 0.0321 0.0770 0.0765 98 GLU B CG 2386 C CG B GLU B 100 ? 0.2393 0.4024 0.3199 0.0249 0.0738 0.1209 98 GLU B CG 2387 C CD A GLU B 100 ? 0.3825 0.5352 0.4249 0.0353 0.0814 0.0700 98 GLU B CD 2388 C CD B GLU B 100 ? 0.3422 0.5274 0.4542 0.0204 0.0737 0.1538 98 GLU B CD 2389 O OE1 A GLU B 100 ? 0.2054 0.3410 0.2533 0.0361 0.0816 0.0626 98 GLU B OE1 2390 O OE1 B GLU B 100 ? 0.3804 0.5794 0.5065 0.0187 0.0760 0.1662 98 GLU B OE1 2391 O OE2 A GLU B 100 ? 0.2711 0.4574 0.3028 0.0365 0.0848 0.0714 98 GLU B OE2 2392 O OE2 B GLU B 100 ? 0.3990 0.5888 0.5248 0.0185 0.0711 0.1691 98 GLU B OE2 2393 N N . VAL B 101 ? 0.1984 0.2955 0.3119 0.0198 0.0777 0.0928 99 VAL B N 2394 C CA . VAL B 101 ? 0.2111 0.2989 0.3211 0.0186 0.0778 0.0801 99 VAL B CA 2395 C C . VAL B 101 ? 0.3074 0.4206 0.4172 0.0206 0.0807 0.0896 99 VAL B C 2396 O O . VAL B 101 ? 0.3004 0.4312 0.4280 0.0181 0.0825 0.1088 99 VAL B O 2397 C CB . VAL B 101 ? 0.2204 0.2886 0.3542 0.0100 0.0776 0.0764 99 VAL B CB 2398 C CG1 . VAL B 101 ? 0.2615 0.3257 0.3884 0.0071 0.0765 0.0636 99 VAL B CG1 2399 C CG2 . VAL B 101 ? 0.2480 0.2948 0.3859 0.0077 0.0763 0.0671 99 VAL B CG2 2400 N N . THR B 102 ? 0.1991 0.3158 0.2919 0.0254 0.0814 0.0773 100 THR B N 2401 C CA . THR B 102 ? 0.2742 0.4146 0.3674 0.0282 0.0850 0.0829 100 THR B CA 2402 C C . THR B 102 ? 0.3224 0.4522 0.4182 0.0273 0.0839 0.0737 100 THR B C 2403 O O . THR B 102 ? 0.2909 0.4027 0.3789 0.0279 0.0808 0.0604 100 THR B O 2404 C CB . THR B 102 ? 0.2732 0.4344 0.3473 0.0358 0.0888 0.0755 100 THR B CB 2405 O OG1 . THR B 102 ? 0.4283 0.6054 0.4974 0.0350 0.0889 0.0843 100 THR B OG1 2406 C CG2 . THR B 102 ? 0.4393 0.6279 0.5160 0.0388 0.0942 0.0794 100 THR B CG2 2407 N N . VAL B 103 ? 0.2454 0.3894 0.3536 0.0251 0.0858 0.0832 101 VAL B N 2408 C CA . VAL B 103 ? 0.2514 0.3933 0.3632 0.0242 0.0846 0.0780 101 VAL B CA 2409 C C . VAL B 103 ? 0.3128 0.4797 0.4248 0.0312 0.0899 0.0820 101 VAL B C 2410 O O . VAL B 103 ? 0.2522 0.4407 0.3699 0.0311 0.0935 0.0944 101 VAL B O 2411 C CB . VAL B 103 ? 0.3078 0.4444 0.4378 0.0131 0.0820 0.0836 101 VAL B CB 2412 C CG1 . VAL B 103 ? 0.2560 0.3997 0.3893 0.0115 0.0805 0.0819 101 VAL B CG1 2413 C CG2 . VAL B 103 ? 0.1892 0.3025 0.3218 0.0053 0.0785 0.0746 101 VAL B CG2 2414 N N . TYR B 104 ? 0.3456 0.5115 0.4549 0.0372 0.0906 0.0723 102 TYR B N 2415 C CA . TYR B 104 ? 0.2607 0.4495 0.3754 0.0445 0.0969 0.0732 102 TYR B CA 2416 C C . TYR B 104 ? 0.2334 0.4181 0.3591 0.0473 0.0955 0.0696 102 TYR B C 2417 O O . TYR B 104 ? 0.2606 0.4269 0.3846 0.0466 0.0906 0.0629 102 TYR B O 2418 C CB . TYR B 104 ? 0.2195 0.4216 0.3225 0.0526 0.1034 0.0628 102 TYR B CB 2419 C CG . TYR B 104 ? 0.2879 0.4706 0.3815 0.0571 0.1020 0.0457 102 TYR B CG 2420 C CD1 . TYR B 104 ? 0.3654 0.5431 0.4685 0.0643 0.1043 0.0342 102 TYR B CD1 2421 C CD2 . TYR B 104 ? 0.3560 0.5264 0.4356 0.0542 0.0985 0.0425 102 TYR B CD2 2422 C CE1 . TYR B 104 ? 0.4046 0.5648 0.5036 0.0680 0.1031 0.0198 102 TYR B CE1 2423 C CE2 . TYR B 104 ? 0.4352 0.5889 0.5070 0.0579 0.0971 0.0272 102 TYR B CE2 2424 C CZ . TYR B 104 ? 0.4683 0.6166 0.5499 0.0645 0.0993 0.0158 102 TYR B CZ 2425 O OH . TYR B 104 ? 0.4701 0.6016 0.5486 0.0678 0.0978 0.0018 102 TYR B OH 2426 N N . PRO B 105 ? 0.2273 0.4320 0.3668 0.0502 0.0997 0.0766 103 PRO B N 2427 C CA . PRO B 105 ? 0.2373 0.4431 0.3932 0.0537 0.0988 0.0772 103 PRO B CA 2428 C C . PRO B 105 ? 0.3030 0.5058 0.4647 0.0655 0.1043 0.0630 103 PRO B C 2429 O O . PRO B 105 ? 0.3768 0.5859 0.5297 0.0714 0.1113 0.0510 103 PRO B O 2430 C CB . PRO B 105 ? 0.2637 0.4946 0.4339 0.0538 0.1031 0.0893 103 PRO B CB 2431 C CG . PRO B 105 ? 0.2589 0.5062 0.4190 0.0554 0.1097 0.0895 103 PRO B CG 2432 C CD . PRO B 105 ? 0.1983 0.4280 0.3419 0.0491 0.1047 0.0878 103 PRO B CD 2433 N N . ALA B 106 ? 0.2937 0.4897 0.4729 0.0678 0.1011 0.0648 104 ALA B N 2434 C CA . ALA B 106 ? 0.2846 0.4759 0.4800 0.0790 0.1064 0.0526 104 ALA B CA 2435 C C . ALA B 106 ? 0.3582 0.5564 0.5868 0.0822 0.1051 0.0646 104 ALA B C 2436 O O . ALA B 106 ? 0.2317 0.4412 0.4662 0.0750 0.0997 0.0820 104 ALA B O 2437 C CB . ALA B 106 ? 0.2632 0.4307 0.4461 0.0780 0.1015 0.0422 104 ALA B CB 2438 N N . LYS B 107 ? 0.4860 0.6791 0.7399 0.0925 0.1102 0.0561 105 LYS B N 2439 C CA . LYS B 107 ? 0.5233 0.7246 0.8173 0.0971 0.1098 0.0699 105 LYS B CA 2440 C C . LYS B 107 ? 0.5713 0.7552 0.8835 0.0983 0.1035 0.0721 105 LYS B C 2441 O O . LYS B 107 ? 0.6079 0.7742 0.9148 0.1026 0.1062 0.0539 105 LYS B O 2442 C CB . LYS B 107 ? 0.5430 0.7512 0.8534 0.1056 0.1193 0.0568 105 LYS B CB 2443 C CG . LYS B 107 ? 0.5697 0.7992 0.8656 0.1043 0.1254 0.0557 105 LYS B CG 2444 C CD . LYS B 107 ? 0.6219 0.8615 0.9345 0.1128 0.1359 0.0376 105 LYS B CD 2445 C CE . LYS B 107 ? 0.6913 0.9556 0.9877 0.1108 0.1426 0.0347 105 LYS B CE 2446 N NZ . LYS B 107 ? 0.7349 1.0127 1.0411 0.1070 0.1388 0.0579 105 LYS B NZ 2447 N N . THR B 108 ? 0.5559 0.7471 0.8885 0.0930 0.0942 0.0957 106 THR B N 2448 C CA . THR B 108 ? 0.6373 0.8165 0.9915 0.0930 0.0873 0.1032 106 THR B CA 2449 C C . THR B 108 ? 0.7307 0.8990 1.1158 0.1024 0.0938 0.0940 106 THR B C 2450 O O . THR B 108 ? 0.8042 0.9555 1.2058 0.1048 0.0923 0.0896 106 THR B O 2451 C CB . THR B 108 ? 0.5715 0.7692 0.9364 0.0815 0.0744 0.1339 106 THR B CB 2452 O OG1 . THR B 108 ? 0.5528 0.7677 0.9330 0.0804 0.0747 0.1485 106 THR B OG1 2453 C CG2 . THR B 108 ? 0.4936 0.6964 0.8190 0.0671 0.0662 0.1354 106 THR B CG2 2454 N N . GLN B 109 ? 0.7164 0.8961 1.1108 0.1069 0.1011 0.0908 107 GLN B N 2455 C CA . GLN B 109 ? 0.8007 0.9735 1.2232 0.1161 0.1098 0.0764 107 GLN B CA 2456 C C . GLN B 109 ? 0.8140 0.9989 1.2212 0.1213 0.1212 0.0545 107 GLN B C 2457 O O . GLN B 109 ? 0.7526 0.9562 1.1471 0.1182 0.1215 0.0643 107 GLN B O 2458 C CB . GLN B 109 ? 0.8249 1.0049 1.2867 0.1156 0.1065 0.1010 107 GLN B CB 2459 C CG . GLN B 109 ? 0.8012 0.9750 1.2816 0.1090 0.0953 0.1255 107 GLN B CG 2460 C CD . GLN B 109 ? 0.8195 1.0041 1.3383 0.1071 0.0922 0.1535 107 GLN B CD 2461 O OE1 . GLN B 109 ? 0.8227 1.0217 1.3427 0.0971 0.0812 0.1834 107 GLN B OE1 2462 N NE2 . GLN B 109 ? 0.8548 1.0352 1.4052 0.1156 0.1022 0.1440 107 GLN B NE2 2463 N N . PRO B 110 ? 0.8722 1.0498 1.2799 0.1280 0.1303 0.0252 108 PRO B N 2464 C CA . PRO B 110 ? 0.9059 1.1007 1.2947 0.1318 0.1411 0.0018 108 PRO B CA 2465 C C . PRO B 110 ? 0.9031 1.1211 1.3062 0.1344 0.1466 0.0087 108 PRO B C 2466 O O . PRO B 110 ? 0.8804 1.1197 1.2628 0.1344 0.1534 -0.0025 108 PRO B O 2467 C CB . PRO B 110 ? 0.9098 1.0935 1.3082 0.1378 0.1484 -0.0266 108 PRO B CB 2468 C CG . PRO B 110 ? 0.8698 1.0266 1.2746 0.1347 0.1400 -0.0210 108 PRO B CG 2469 C CD . PRO B 110 ? 0.8559 1.0108 1.2807 0.1305 0.1300 0.0132 108 PRO B CD 2470 N N . LEU B 111 ? 0.8901 1.1063 1.3284 0.1355 0.1434 0.0288 109 LEU B N 2471 C CA . LEU B 111 ? 0.8736 1.1105 1.3291 0.1383 0.1483 0.0364 109 LEU B CA 2472 C C . LEU B 111 ? 0.8383 1.0899 1.2789 0.1301 0.1409 0.0638 109 LEU B C 2473 O O . LEU B 111 ? 0.7703 1.0425 1.2092 0.1304 0.1455 0.0658 109 LEU B O 2474 C CB . LEU B 111 ? 0.8642 1.0930 1.3682 0.1435 0.1498 0.0447 109 LEU B CB 2475 N N . GLN B 112 ? 0.8684 1.1114 1.2979 0.1220 0.1293 0.0842 110 GLN B N 2476 C CA . GLN B 112 ? 0.8828 1.1404 1.2985 0.1122 0.1208 0.1101 110 GLN B CA 2477 C C . GLN B 112 ? 0.8223 1.0926 1.2026 0.1080 0.1240 0.1030 110 GLN B C 2478 O O . GLN B 112 ? 0.8091 1.0810 1.1750 0.1126 0.1331 0.0795 110 GLN B O 2479 C CB . GLN B 112 ? 0.9064 1.1560 1.3159 0.1031 0.1079 0.1287 110 GLN B CB 2480 C CG . GLN B 112 ? 0.9275 1.1663 1.3700 0.1044 0.1027 0.1413 110 GLN B CG 2481 C CD . GLN B 112 ? 0.9166 1.1502 1.3476 0.0952 0.0910 0.1541 110 GLN B CD 2482 O OE1 . GLN B 112 ? 0.8853 1.1109 1.2889 0.0933 0.0906 0.1407 110 GLN B OE1 2483 N NE2 . GLN B 112 ? 0.9103 1.1512 1.3621 0.0886 0.0813 0.1810 110 GLN B NE2 2484 N N . HIS B 113 ? 0.7176 0.9993 1.0848 0.0976 0.1157 0.1241 111 HIS B N 2485 C CA . HIS B 113 ? 0.5511 0.8403 0.8854 0.0905 0.1157 0.1222 111 HIS B CA 2486 C C . HIS B 113 ? 0.4574 0.7321 0.7711 0.0849 0.1101 0.1191 111 HIS B C 2487 O O . HIS B 113 ? 0.3712 0.6317 0.6952 0.0875 0.1071 0.1170 111 HIS B O 2488 C CB . HIS B 113 ? 0.5671 0.8732 0.8991 0.0801 0.1086 0.1440 111 HIS B CB 2489 C CG . HIS B 113 ? 0.6241 0.9453 0.9766 0.0849 0.1132 0.1502 111 HIS B CG 2490 N ND1 . HIS B 113 ? 0.6442 0.9661 1.0290 0.0899 0.1124 0.1596 111 HIS B ND1 2491 C CD2 . HIS B 113 ? 0.6748 1.0118 1.0216 0.0850 0.1185 0.1498 111 HIS B CD2 2492 C CE1 . HIS B 113 ? 0.6421 0.9791 1.0403 0.0935 0.1177 0.1632 111 HIS B CE1 2493 N NE2 . HIS B 113 ? 0.6705 1.0176 1.0454 0.0905 0.1214 0.1570 111 HIS B NE2 2494 N N . HIS B 114 ? 0.4455 0.7233 0.7323 0.0768 0.1086 0.1195 112 HIS B N 2495 C CA . HIS B 114 ? 0.4376 0.7026 0.7060 0.0709 0.1041 0.1162 112 HIS B CA 2496 C C . HIS B 114 ? 0.3646 0.6281 0.6348 0.0583 0.0910 0.1309 112 HIS B C 2497 O O . HIS B 114 ? 0.3445 0.6252 0.6198 0.0486 0.0862 0.1459 112 HIS B O 2498 C CB . HIS B 114 ? 0.4554 0.7194 0.6945 0.0647 0.1052 0.1109 112 HIS B CB 2499 C CG . HIS B 114 ? 0.5401 0.8084 0.7706 0.0743 0.1162 0.0952 112 HIS B CG 2500 N ND1 . HIS B 114 ? 0.5591 0.8420 0.7771 0.0718 0.1197 0.0964 112 HIS B ND1 2501 C CD2 . HIS B 114 ? 0.5696 0.8293 0.7996 0.0838 0.1224 0.0763 112 HIS B CD2 2502 C CE1 . HIS B 114 ? 0.5760 0.8634 0.7847 0.0785 0.1276 0.0795 112 HIS B CE1 2503 N NE2 . HIS B 114 ? 0.5866 0.8597 0.8021 0.0856 0.1297 0.0652 112 HIS B NE2 2504 N N . ASN B 115 ? 0.2823 0.5289 0.5490 0.0573 0.0855 0.1265 113 ASN B N 2505 C CA . ASN B 115 ? 0.2389 0.4899 0.5061 0.0441 0.0733 0.1395 113 ASN B CA 2506 C C . ASN B 115 ? 0.2048 0.4340 0.4483 0.0387 0.0680 0.1279 113 ASN B C 2507 O O . ASN B 115 ? 0.1864 0.4183 0.4322 0.0307 0.0592 0.1353 113 ASN B O 2508 C CB . ASN B 115 ? 0.2383 0.5058 0.5429 0.0480 0.0704 0.1582 113 ASN B CB 2509 C CG . ASN B 115 ? 0.2849 0.5375 0.6120 0.0632 0.0760 0.1511 113 ASN B CG 2510 O OD1 . ASN B 115 ? 0.1962 0.4267 0.5067 0.0693 0.0809 0.1308 113 ASN B OD1 2511 N ND2 . ASN B 115 ? 0.3759 0.6314 0.7318 0.0664 0.0729 0.1649 113 ASN B ND2 2512 N N . LEU B 116 ? 0.2082 0.4195 0.4292 0.0424 0.0733 0.1109 114 LEU B N 2513 C CA . LEU B 116 ? 0.2735 0.4633 0.4732 0.0392 0.0698 0.0987 114 LEU B CA 2514 C C . LEU B 116 ? 0.3144 0.4949 0.4907 0.0370 0.0736 0.0881 114 LEU B C 2515 O O . LEU B 116 ? 0.3068 0.4925 0.4833 0.0450 0.0817 0.0847 114 LEU B O 2516 C CB . LEU B 116 ? 0.3514 0.5278 0.5609 0.0522 0.0737 0.0898 114 LEU B CB 2517 C CG . LEU B 116 ? 0.4714 0.6279 0.6666 0.0496 0.0686 0.0812 114 LEU B CG 2518 C CD1 . LEU B 116 ? 0.4437 0.6090 0.6444 0.0380 0.0578 0.0951 114 LEU B CD1 2519 C CD2 . LEU B 116 ? 0.4812 0.6256 0.6907 0.0632 0.0744 0.0705 114 LEU B CD2 2520 N N . LEU B 117 ? 0.1790 0.3492 0.3386 0.0257 0.0682 0.0840 115 LEU B N 2521 C CA . LEU B 117 ? 0.2245 0.3840 0.3683 0.0241 0.0715 0.0763 115 LEU B CA 2522 C C . LEU B 117 ? 0.2261 0.3646 0.3546 0.0263 0.0702 0.0642 115 LEU B C 2523 O O . LEU B 117 ? 0.2150 0.3456 0.3395 0.0196 0.0641 0.0613 115 LEU B O 2524 C CB . LEU B 117 ? 0.1924 0.3554 0.3360 0.0094 0.0682 0.0797 115 LEU B CB 2525 C CG . LEU B 117 ? 0.2025 0.3862 0.3604 0.0057 0.0697 0.0915 115 LEU B CG 2526 C CD1 . LEU B 117 ? 0.2680 0.4518 0.4286 -0.0098 0.0672 0.0908 115 LEU B CD1 2527 C CD2 . LEU B 117 ? 0.2553 0.4472 0.4159 0.0172 0.0778 0.0955 115 LEU B CD2 2528 N N . VAL B 118 ? 0.1838 0.3172 0.3035 0.0344 0.0759 0.0577 116 VAL B N 2529 C CA . VAL B 118 ? 0.1845 0.3000 0.2899 0.0364 0.0748 0.0470 116 VAL B CA 2530 C C . VAL B 118 ? 0.2459 0.3544 0.3422 0.0301 0.0746 0.0470 116 VAL B C 2531 O O . VAL B 118 ? 0.1870 0.3063 0.2851 0.0308 0.0788 0.0534 116 VAL B O 2532 C CB . VAL B 118 ? 0.2173 0.3340 0.3202 0.0487 0.0808 0.0376 116 VAL B CB 2533 C CG1 . VAL B 118 ? 0.2504 0.3486 0.3402 0.0498 0.0782 0.0266 116 VAL B CG1 2534 C CG2 . VAL B 118 ? 0.2162 0.3405 0.3384 0.0562 0.0832 0.0379 116 VAL B CG2 2535 N N . CYS B 119 ? 0.1989 0.2914 0.2890 0.0236 0.0699 0.0413 117 CYS B N 2536 C CA . CYS B 119 ? 0.2627 0.3456 0.3489 0.0199 0.0706 0.0401 117 CYS B CA 2537 C C . CYS B 119 ? 0.2661 0.3382 0.3387 0.0264 0.0706 0.0322 117 CYS B C 2538 O O . CYS B 119 ? 0.2454 0.3046 0.3121 0.0249 0.0666 0.0244 117 CYS B O 2539 C CB . CYS B 119 ? 0.1820 0.2559 0.2742 0.0074 0.0671 0.0364 117 CYS B CB 2540 S SG . CYS B 119 ? 0.2425 0.3041 0.3416 0.0039 0.0696 0.0367 117 CYS B SG 2541 N N . SER B 120 ? 0.2190 0.3002 0.2867 0.0325 0.0748 0.0348 118 SER B N 2542 C CA . SER B 120 ? 0.2046 0.2804 0.2590 0.0376 0.0750 0.0269 118 SER B CA 2543 C C . SER B 120 ? 0.2490 0.3165 0.3031 0.0327 0.0733 0.0313 118 SER B C 2544 O O . SER B 120 ? 0.2839 0.3622 0.3471 0.0302 0.0754 0.0437 118 SER B O 2545 C CB . SER B 120 ? 0.2589 0.3560 0.3077 0.0449 0.0808 0.0254 118 SER B CB 2546 O OG . SER B 120 ? 0.2825 0.3765 0.3187 0.0486 0.0810 0.0143 118 SER B OG 2547 N N . VAL B 121 ? 0.2406 0.2903 0.2883 0.0314 0.0697 0.0228 119 VAL B N 2548 C CA . VAL B 121 ? 0.1934 0.2338 0.2446 0.0275 0.0686 0.0260 119 VAL B CA 2549 C C . VAL B 121 ? 0.2355 0.2759 0.2720 0.0324 0.0678 0.0214 119 VAL B C 2550 O O . VAL B 121 ? 0.1900 0.2190 0.2164 0.0345 0.0652 0.0098 119 VAL B O 2551 C CB . VAL B 121 ? 0.2056 0.2280 0.2632 0.0200 0.0658 0.0185 119 VAL B CB 2552 C CG1 . VAL B 121 ? 0.2022 0.2148 0.2709 0.0162 0.0664 0.0208 119 VAL B CG1 2553 C CG2 . VAL B 121 ? 0.1839 0.2111 0.2543 0.0134 0.0664 0.0202 119 VAL B CG2 2554 N N . ASN B 122 ? 0.2198 0.2766 0.2563 0.0335 0.0698 0.0319 120 ASN B N 2555 C CA . ASN B 122 ? 0.2020 0.2678 0.2227 0.0370 0.0694 0.0272 120 ASN B CA 2556 C C . ASN B 122 ? 0.2047 0.2734 0.2296 0.0343 0.0676 0.0384 120 ASN B C 2557 O O . ASN B 122 ? 0.2063 0.2846 0.2488 0.0312 0.0686 0.0565 120 ASN B O 2558 C CB . ASN B 122 ? 0.2214 0.3176 0.2335 0.0403 0.0737 0.0274 120 ASN B CB 2559 C CG . ASN B 122 ? 0.3541 0.4499 0.3655 0.0445 0.0767 0.0158 120 ASN B CG 2560 O OD1 . ASN B 122 ? 0.3223 0.4219 0.3445 0.0438 0.0784 0.0230 120 ASN B OD1 2561 N ND2 . ASN B 122 ? 0.2775 0.3693 0.2802 0.0488 0.0775 -0.0019 120 ASN B ND2 2562 N N . GLY B 123 ? 0.2015 0.2640 0.2134 0.0356 0.0650 0.0292 121 GLY B N 2563 C CA . GLY B 123 ? 0.2340 0.3085 0.2464 0.0337 0.0633 0.0405 121 GLY B CA 2564 C C . GLY B 123 ? 0.2580 0.3114 0.2872 0.0310 0.0611 0.0467 121 GLY B C 2565 O O . GLY B 123 ? 0.2592 0.3237 0.2981 0.0293 0.0601 0.0618 121 GLY B O 2566 N N . PHE B 124 ? 0.2244 0.2511 0.2588 0.0299 0.0607 0.0351 122 PHE B N 2567 C CA . PHE B 124 ? 0.2319 0.2404 0.2866 0.0263 0.0608 0.0371 122 PHE B CA 2568 C C . PHE B 124 ? 0.2886 0.2831 0.3342 0.0266 0.0578 0.0273 122 PHE B C 2569 O O . PHE B 124 ? 0.2402 0.2327 0.2634 0.0291 0.0549 0.0155 122 PHE B O 2570 C CB . PHE B 124 ? 0.2364 0.2302 0.3047 0.0220 0.0630 0.0292 122 PHE B CB 2571 C CG . PHE B 124 ? 0.2494 0.2350 0.2992 0.0219 0.0608 0.0124 122 PHE B CG 2572 C CD1 . PHE B 124 ? 0.2869 0.2579 0.3307 0.0195 0.0584 -0.0005 122 PHE B CD1 2573 C CD2 . PHE B 124 ? 0.2986 0.2938 0.3405 0.0239 0.0612 0.0116 122 PHE B CD2 2574 C CE1 . PHE B 124 ? 0.3047 0.2728 0.3360 0.0185 0.0556 -0.0110 122 PHE B CE1 2575 C CE2 . PHE B 124 ? 0.2940 0.2839 0.3255 0.0239 0.0589 0.0005 122 PHE B CE2 2576 C CZ . PHE B 124 ? 0.2608 0.2380 0.2874 0.0208 0.0556 -0.0095 122 PHE B CZ 2577 N N . TYR B 125 ? 0.2354 0.2192 0.3279 0.0272 0.0759 0.0631 123 TYR B N 2578 C CA . TYR B 125 ? 0.2047 0.1925 0.2957 0.0263 0.0761 0.0546 123 TYR B CA 2579 C C . TYR B 125 ? 0.2096 0.1964 0.3171 0.0270 0.0771 0.0464 123 TYR B C 2580 O O . TYR B 125 ? 0.2961 0.2776 0.4193 0.0303 0.0760 0.0502 123 TYR B O 2581 C CB . TYR B 125 ? 0.2154 0.2077 0.3046 0.0307 0.0743 0.0593 123 TYR B CB 2582 C CG . TYR B 125 ? 0.2831 0.2820 0.3699 0.0281 0.0742 0.0521 123 TYR B CG 2583 C CD1 . TYR B 125 ? 0.2937 0.2948 0.3672 0.0240 0.0718 0.0517 123 TYR B CD1 2584 C CD2 . TYR B 125 ? 0.2065 0.2104 0.3061 0.0297 0.0759 0.0461 123 TYR B CD2 2585 C CE1 . TYR B 125 ? 0.2447 0.2539 0.3187 0.0201 0.0717 0.0479 123 TYR B CE1 2586 C CE2 . TYR B 125 ? 0.2335 0.2481 0.3320 0.0271 0.0767 0.0408 123 TYR B CE2 2587 C CZ . TYR B 125 ? 0.2183 0.2360 0.3045 0.0215 0.0748 0.0430 123 TYR B CZ 2588 O OH . TYR B 125 ? 0.1921 0.2225 0.2798 0.0175 0.0754 0.0407 123 TYR B OH 2589 N N . PRO B 126 ? 0.2562 0.2491 0.3609 0.0246 0.0786 0.0353 124 PRO B N 2590 C CA . PRO B 126 ? 0.2465 0.2470 0.3355 0.0197 0.0797 0.0328 124 PRO B CA 2591 C C . PRO B 126 ? 0.2927 0.2895 0.3708 0.0153 0.0794 0.0326 124 PRO B C 2592 O O . PRO B 126 ? 0.2215 0.2106 0.3029 0.0159 0.0785 0.0357 124 PRO B O 2593 C CB . PRO B 126 ? 0.2962 0.3088 0.3907 0.0203 0.0821 0.0222 124 PRO B CB 2594 C CG . PRO B 126 ? 0.3163 0.3238 0.4267 0.0251 0.0814 0.0146 124 PRO B CG 2595 C CD . PRO B 126 ? 0.2561 0.2511 0.3761 0.0279 0.0788 0.0246 124 PRO B CD 2596 N N . GLY B 127 ? 0.2742 0.2779 0.3405 0.0106 0.0799 0.0302 125 GLY B N 2597 C CA . GLY B 127 ? 0.3086 0.3088 0.3628 0.0067 0.0786 0.0317 125 GLY B CA 2598 C C . GLY B 127 ? 0.3045 0.3059 0.3601 0.0058 0.0797 0.0237 125 GLY B C 2599 O O . GLY B 127 ? 0.3821 0.3782 0.4315 0.0040 0.0781 0.0254 125 GLY B O 2600 N N . SER B 128 ? 0.2684 0.2778 0.3325 0.0080 0.0817 0.0138 126 SER B N 2601 C CA . SER B 128 ? 0.2690 0.2813 0.3347 0.0085 0.0814 0.0033 126 SER B CA 2602 C C . SER B 128 ? 0.2275 0.2262 0.3050 0.0098 0.0783 0.0032 126 SER B C 2603 O O . SER B 128 ? 0.2821 0.2739 0.3757 0.0131 0.0770 0.0039 126 SER B O 2604 C CB . SER B 128 ? 0.3506 0.3755 0.4248 0.0133 0.0830 -0.0094 126 SER B CB 2605 O OG . SER B 128 ? 0.5212 0.5379 0.6132 0.0184 0.0814 -0.0113 126 SER B OG 2606 N N . ILE B 129 ? 0.2783 0.2742 0.3494 0.0068 0.0766 0.0034 127 ILE B N 2607 C CA . ILE B 129 ? 0.3022 0.2875 0.3858 0.0066 0.0736 0.0058 127 ILE B CA 2608 C C . ILE B 129 ? 0.2700 0.2572 0.3500 0.0045 0.0711 -0.0019 127 ILE B C 2609 O O . ILE B 129 ? 0.3493 0.3445 0.4124 0.0027 0.0721 -0.0040 127 ILE B O 2610 C CB . ILE B 129 ? 0.2354 0.2152 0.3151 0.0057 0.0741 0.0210 127 ILE B CB 2611 C CG1 . ILE B 129 ? 0.2720 0.2449 0.3695 0.0058 0.0720 0.0271 127 ILE B CG1 2612 C CG2 . ILE B 129 ? 0.2366 0.2190 0.2965 0.0030 0.0740 0.0246 127 ILE B CG2 2613 C CD1 . ILE B 129 ? 0.2617 0.2342 0.3587 0.0076 0.0734 0.0422 127 ILE B CD1 2614 N N . GLU B 130 ? 0.2809 0.2613 0.3782 0.0045 0.0670 -0.0056 128 GLU B N 2615 C CA . GLU B 130 ? 0.3223 0.3045 0.4182 0.0026 0.0634 -0.0133 128 GLU B CA 2616 C C . GLU B 130 ? 0.3235 0.2984 0.4306 -0.0006 0.0611 -0.0030 128 GLU B C 2617 O O . GLU B 130 ? 0.2731 0.2403 0.4019 -0.0008 0.0587 0.0016 128 GLU B O 2618 C CB . GLU B 130 ? 0.4231 0.4072 0.5316 0.0063 0.0587 -0.0317 128 GLU B CB 2619 C CG . GLU B 130 ? 0.4803 0.4678 0.5879 0.0054 0.0536 -0.0425 128 GLU B CG 2620 C CD . GLU B 130 ? 0.5917 0.5948 0.6741 0.0061 0.0563 -0.0480 128 GLU B CD 2621 O OE1 . GLU B 130 ? 0.6003 0.6154 0.6736 0.0099 0.0595 -0.0543 128 GLU B OE1 2622 O OE2 . GLU B 130 ? 0.6414 0.6465 0.7138 0.0030 0.0550 -0.0451 128 GLU B OE2 2623 N N . VAL B 131 ? 0.2174 0.1958 0.3107 -0.0031 0.0615 0.0018 129 VAL B N 2624 C CA . VAL B 131 ? 0.2340 0.2103 0.3368 -0.0056 0.0601 0.0122 129 VAL B CA 2625 C C . VAL B 131 ? 0.2747 0.2543 0.3770 -0.0079 0.0558 0.0047 129 VAL B C 2626 O O . VAL B 131 ? 0.2655 0.2507 0.3477 -0.0075 0.0562 0.0004 129 VAL B O 2627 C CB . VAL B 131 ? 0.2252 0.2044 0.3127 -0.0044 0.0641 0.0260 129 VAL B CB 2628 C CG1 . VAL B 131 ? 0.1870 0.1693 0.2852 -0.0055 0.0636 0.0377 129 VAL B CG1 2629 C CG2 . VAL B 131 ? 0.2380 0.2153 0.3231 -0.0016 0.0675 0.0317 129 VAL B CG2 2630 N N . ARG B 132 ? 0.2273 0.2036 0.3531 -0.0105 0.0510 0.0043 130 ARG B N 2631 C CA . ARG B 132 ? 0.2390 0.2185 0.3690 -0.0127 0.0453 -0.0045 130 ARG B CA 2632 C C . ARG B 132 ? 0.2490 0.2302 0.3964 -0.0169 0.0436 0.0080 130 ARG B C 2633 O O . ARG B 132 ? 0.2064 0.1850 0.3725 -0.0187 0.0446 0.0207 130 ARG B O 2634 C CB . ARG B 132 ? 0.2631 0.2387 0.4081 -0.0115 0.0383 -0.0229 130 ARG B CB 2635 C CG . ARG B 132 ? 0.3542 0.3346 0.4805 -0.0063 0.0406 -0.0360 130 ARG B CG 2636 C CD . ARG B 132 ? 0.4688 0.4503 0.6056 -0.0022 0.0332 -0.0578 130 ARG B CD 2637 N NE . ARG B 132 ? 0.5396 0.5341 0.6525 0.0030 0.0369 -0.0681 130 ARG B NE 2638 C CZ . ARG B 132 ? 0.6053 0.6112 0.7102 0.0073 0.0326 -0.0855 130 ARG B CZ 2639 N NH1 . ARG B 132 ? 0.6778 0.6815 0.7971 0.0072 0.0233 -0.0971 130 ARG B NH1 2640 N NH2 . ARG B 132 ? 0.5646 0.5865 0.6477 0.0118 0.0375 -0.0910 130 ARG B NH2 2641 N N . TRP B 133 ? 0.2296 0.2176 0.3711 -0.0183 0.0410 0.0054 131 TRP B N 2642 C CA . TRP B 133 ? 0.2311 0.2249 0.3897 -0.0223 0.0391 0.0162 131 TRP B CA 2643 C C . TRP B 133 ? 0.2841 0.2757 0.4675 -0.0266 0.0296 0.0057 131 TRP B C 2644 O O . TRP B 133 ? 0.2634 0.2543 0.4391 -0.0249 0.0244 -0.0120 131 TRP B O 2645 C CB . TRP B 133 ? 0.2309 0.2351 0.3681 -0.0201 0.0417 0.0209 131 TRP B CB 2646 C CG . TRP B 133 ? 0.1982 0.2072 0.3222 -0.0164 0.0488 0.0355 131 TRP B CG 2647 C CD1 . TRP B 133 ? 0.2509 0.2585 0.3479 -0.0115 0.0523 0.0350 131 TRP B CD1 2648 C CD2 . TRP B 133 ? 0.2648 0.2828 0.4025 -0.0165 0.0522 0.0526 131 TRP B CD2 2649 N NE1 . TRP B 133 ? 0.1840 0.1975 0.2768 -0.0077 0.0567 0.0482 131 TRP B NE1 2650 C CE2 . TRP B 133 ? 0.1911 0.2130 0.3072 -0.0101 0.0575 0.0593 131 TRP B CE2 2651 C CE3 . TRP B 133 ? 0.2722 0.2969 0.4396 -0.0215 0.0509 0.0637 131 TRP B CE3 2652 C CZ2 . TRP B 133 ? 0.1992 0.2338 0.3195 -0.0067 0.0619 0.0751 131 TRP B CZ2 2653 C CZ3 . TRP B 133 ? 0.2702 0.3088 0.4428 -0.0195 0.0563 0.0824 131 TRP B CZ3 2654 C CH2 . TRP B 133 ? 0.2670 0.3114 0.4149 -0.0113 0.0620 0.0871 131 TRP B CH2 2655 N N . PHE B 134 ? 0.2300 0.2222 0.4437 -0.0321 0.0267 0.0174 132 PHE B N 2656 C CA . PHE B 134 ? 0.2733 0.2628 0.5166 -0.0376 0.0160 0.0098 132 PHE B CA 2657 C C . PHE B 134 ? 0.3562 0.3591 0.6149 -0.0430 0.0159 0.0254 132 PHE B C 2658 O O . PHE B 134 ? 0.2796 0.2919 0.5397 -0.0435 0.0234 0.0458 132 PHE B O 2659 C CB . PHE B 134 ? 0.2694 0.2448 0.5443 -0.0405 0.0096 0.0090 132 PHE B CB 2660 C CG . PHE B 134 ? 0.2486 0.2130 0.5123 -0.0342 0.0081 -0.0094 132 PHE B CG 2661 C CD1 . PHE B 134 ? 0.3016 0.2594 0.5750 -0.0322 -0.0029 -0.0329 132 PHE B CD1 2662 C CD2 . PHE B 134 ? 0.2405 0.2034 0.4846 -0.0294 0.0172 -0.0041 132 PHE B CD2 2663 C CE1 . PHE B 134 ? 0.2622 0.2144 0.5255 -0.0248 -0.0040 -0.0504 132 PHE B CE1 2664 C CE2 . PHE B 134 ? 0.2783 0.2347 0.5135 -0.0234 0.0162 -0.0204 132 PHE B CE2 2665 C CZ . PHE B 134 ? 0.3003 0.2523 0.5448 -0.0207 0.0060 -0.0435 132 PHE B CZ 2666 N N . ARG B 135 ? 0.3896 0.3962 0.6588 -0.0460 0.0074 0.0151 133 ARG B N 2667 C CA . ARG B 135 ? 0.4311 0.4518 0.7215 -0.0521 0.0055 0.0285 133 ARG B CA 2668 C C . ARG B 135 ? 0.3914 0.4045 0.7226 -0.0601 -0.0082 0.0219 133 ARG B C 2669 O O . ARG B 135 ? 0.4220 0.4276 0.7532 -0.0586 -0.0181 -0.0007 133 ARG B O 2670 C CB . ARG B 135 ? 0.3865 0.4209 0.6526 -0.0483 0.0070 0.0235 133 ARG B CB 2671 C CG . ARG B 135 ? 0.4295 0.4827 0.7163 -0.0534 0.0063 0.0384 133 ARG B CG 2672 C CD . ARG B 135 ? 0.4217 0.4858 0.6920 -0.0503 0.0034 0.0285 133 ARG B CD 2673 N NE . ARG B 135 ? 0.5588 0.6275 0.7897 -0.0412 0.0118 0.0292 133 ARG B NE 2674 C CZ . ARG B 135 ? 0.6494 0.7116 0.8506 -0.0355 0.0103 0.0137 133 ARG B CZ 2675 N NH1 . ARG B 135 ? 0.7601 0.8143 0.9640 -0.0367 0.0016 -0.0048 133 ARG B NH1 2676 N NH2 . ARG B 135 ? 0.5751 0.6401 0.7448 -0.0282 0.0167 0.0168 133 ARG B NH2 2677 N N . ASN B 136 ? 0.3572 0.3733 0.7240 -0.0682 -0.0096 0.0420 134 ASN B N 2678 C CA . ASN B 136 ? 0.3999 0.4060 0.8119 -0.0772 -0.0242 0.0389 134 ASN B CA 2679 C C . ASN B 136 ? 0.4346 0.4172 0.8506 -0.0736 -0.0345 0.0144 134 ASN B C 2680 O O . ASN B 136 ? 0.4416 0.4165 0.8772 -0.0755 -0.0490 -0.0045 134 ASN B O 2681 C CB . ASN B 136 ? 0.4614 0.4795 0.8883 -0.0822 -0.0326 0.0337 134 ASN B CB 2682 C CG . ASN B 136 ? 0.4277 0.4718 0.8598 -0.0863 -0.0240 0.0592 134 ASN B CG 2683 O OD1 . ASN B 136 ? 0.4264 0.4791 0.8686 -0.0890 -0.0158 0.0841 134 ASN B OD1 2684 N ND2 . ASN B 136 ? 0.3881 0.4470 0.8122 -0.0855 -0.0259 0.0529 134 ASN B ND2 2685 N N . GLY B 137 ? 0.4131 0.3863 0.8101 -0.0672 -0.0274 0.0133 135 GLY B N 2686 C CA . GLY B 137 ? 0.4601 0.4136 0.8628 -0.0626 -0.0363 -0.0081 135 GLY B CA 2687 C C . GLY B 137 ? 0.4708 0.4247 0.8400 -0.0527 -0.0374 -0.0366 135 GLY B C 2688 O O . GLY B 137 ? 0.5261 0.4683 0.8947 -0.0464 -0.0432 -0.0560 135 GLY B O 2689 N N . GLN B 138 ? 0.4281 0.3973 0.7697 -0.0507 -0.0321 -0.0387 136 GLN B N 2690 C CA . GLN B 138 ? 0.4128 0.3865 0.7212 -0.0418 -0.0325 -0.0619 136 GLN B CA 2691 C C . GLN B 138 ? 0.3736 0.3552 0.6405 -0.0363 -0.0170 -0.0532 136 GLN B C 2692 O O . GLN B 138 ? 0.3317 0.3219 0.5893 -0.0388 -0.0082 -0.0338 136 GLN B O 2693 C CB . GLN B 138 ? 0.5819 0.5662 0.8912 -0.0433 -0.0404 -0.0719 136 GLN B CB 2694 C CG . GLN B 138 ? 0.7000 0.6923 0.9747 -0.0340 -0.0413 -0.0941 136 GLN B CG 2695 C CD . GLN B 138 ? 0.7953 0.7974 1.0748 -0.0348 -0.0519 -0.1064 136 GLN B CD 2696 O OE1 . GLN B 138 ? 0.8887 0.8862 1.1896 -0.0339 -0.0666 -0.1266 136 GLN B OE1 2697 N NE2 . GLN B 138 ? 0.7267 0.7424 0.9867 -0.0356 -0.0455 -0.0956 136 GLN B NE2 2698 N N . GLU B 139 ? 0.3091 0.2889 0.5523 -0.0285 -0.0144 -0.0675 137 GLU B N 2699 C CA . GLU B 139 ? 0.3064 0.2924 0.5142 -0.0245 -0.0012 -0.0584 137 GLU B CA 2700 C C . GLU B 139 ? 0.3391 0.3382 0.5208 -0.0235 0.0019 -0.0564 137 GLU B C 2701 O O . GLU B 139 ? 0.2943 0.2999 0.4694 -0.0212 -0.0048 -0.0717 137 GLU B O 2702 C CB . GLU B 139 ? 0.2908 0.2751 0.4811 -0.0171 0.0014 -0.0719 137 GLU B CB 2703 C CG . GLU B 139 ? 0.2434 0.2322 0.4035 -0.0150 0.0141 -0.0589 137 GLU B CG 2704 C CD . GLU B 139 ? 0.3925 0.3843 0.5342 -0.0085 0.0176 -0.0701 137 GLU B CD 2705 O OE1 . GLU B 139 ? 0.3658 0.3558 0.5192 -0.0042 0.0110 -0.0879 137 GLU B OE1 2706 O OE2 . GLU B 139 ? 0.4029 0.3997 0.5199 -0.0073 0.0263 -0.0612 137 GLU B OE2 2707 N N . GLU B 140 ? 0.3314 0.3344 0.4989 -0.0244 0.0112 -0.0380 138 GLU B N 2708 C CA . GLU B 140 ? 0.3554 0.3685 0.4971 -0.0223 0.0142 -0.0346 138 GLU B CA 2709 C C . GLU B 140 ? 0.3115 0.3251 0.4212 -0.0172 0.0206 -0.0364 138 GLU B C 2710 O O . GLU B 140 ? 0.3252 0.3339 0.4291 -0.0165 0.0275 -0.0269 138 GLU B O 2711 C CB . GLU B 140 ? 0.4647 0.4829 0.6106 -0.0247 0.0192 -0.0148 138 GLU B CB 2712 C CG . GLU B 140 ? 0.6367 0.6647 0.7977 -0.0280 0.0134 -0.0132 138 GLU B CG 2713 C CD . GLU B 140 ? 0.6832 0.7188 0.8209 -0.0242 0.0104 -0.0223 138 GLU B CD 2714 O OE1 . GLU B 140 ? 0.5871 0.6215 0.6953 -0.0194 0.0145 -0.0238 138 GLU B OE1 2715 O OE2 . GLU B 140 ? 0.7036 0.7465 0.8535 -0.0263 0.0032 -0.0272 138 GLU B OE2 2716 N N . LYS B 141 ? 0.3670 0.3880 0.4572 -0.0140 0.0178 -0.0477 139 LYS B N 2717 C CA . LYS B 141 ? 0.3419 0.3661 0.4038 -0.0103 0.0231 -0.0479 139 LYS B CA 2718 C C . LYS B 141 ? 0.3523 0.3821 0.3905 -0.0093 0.0245 -0.0393 139 LYS B C 2719 O O . LYS B 141 ? 0.4177 0.4484 0.4349 -0.0078 0.0288 -0.0341 139 LYS B O 2720 C CB . LYS B 141 ? 0.3987 0.4301 0.4554 -0.0063 0.0196 -0.0663 139 LYS B CB 2721 C CG . LYS B 141 ? 0.4009 0.4256 0.4772 -0.0050 0.0184 -0.0758 139 LYS B CG 2722 C CD . LYS B 141 ? 0.4222 0.4584 0.4891 0.0017 0.0156 -0.0952 139 LYS B CD 2723 C CE . LYS B 141 ? 0.4119 0.4415 0.4964 0.0047 0.0146 -0.1049 139 LYS B CE 2724 N NZ . LYS B 141 ? 0.3434 0.3872 0.4208 0.0134 0.0106 -0.1269 139 LYS B NZ 2725 N N . THR B 142 ? 0.3068 0.3402 0.3502 -0.0103 0.0201 -0.0373 140 THR B N 2726 C CA . THR B 142 ? 0.2855 0.3227 0.3088 -0.0084 0.0202 -0.0290 140 THR B CA 2727 C C . THR B 142 ? 0.2985 0.3304 0.3234 -0.0082 0.0245 -0.0140 140 THR B C 2728 O O . THR B 142 ? 0.3118 0.3419 0.3566 -0.0101 0.0265 -0.0092 140 THR B O 2729 C CB . THR B 142 ? 0.3856 0.4318 0.4112 -0.0079 0.0126 -0.0352 140 THR B CB 2730 O OG1 . THR B 142 ? 0.4943 0.5411 0.5433 -0.0105 0.0110 -0.0307 140 THR B OG1 2731 C CG2 . THR B 142 ? 0.2772 0.3305 0.3052 -0.0069 0.0066 -0.0528 140 THR B CG2 2732 N N . GLY B 143 ? 0.2532 0.2840 0.2578 -0.0053 0.0250 -0.0066 141 GLY B N 2733 C CA . GLY B 143 ? 0.2815 0.3091 0.2851 -0.0025 0.0274 0.0048 141 GLY B CA 2734 C C . GLY B 143 ? 0.3098 0.3308 0.3191 -0.0030 0.0335 0.0106 141 GLY B C 2735 O O . GLY B 143 ? 0.3223 0.3450 0.3395 -0.0008 0.0360 0.0185 141 GLY B O 2736 N N . VAL B 144 ? 0.2633 0.2794 0.2687 -0.0050 0.0361 0.0069 142 VAL B N 2737 C CA . VAL B 144 ? 0.2808 0.2907 0.2904 -0.0050 0.0414 0.0124 142 VAL B CA 2738 C C . VAL B 144 ? 0.3029 0.3070 0.2932 -0.0034 0.0423 0.0170 142 VAL B C 2739 O O . VAL B 144 ? 0.3000 0.3050 0.2777 -0.0049 0.0409 0.0141 142 VAL B O 2740 C CB . VAL B 144 ? 0.3214 0.3298 0.3447 -0.0079 0.0434 0.0051 142 VAL B CB 2741 C CG1 . VAL B 144 ? 0.2399 0.2423 0.2653 -0.0073 0.0485 0.0110 142 VAL B CG1 2742 C CG2 . VAL B 144 ? 0.2032 0.2144 0.2507 -0.0103 0.0408 0.0019 142 VAL B CG2 2743 N N . VAL B 145 ? 0.2656 0.2655 0.2546 -0.0003 0.0439 0.0248 143 VAL B N 2744 C CA . VAL B 145 ? 0.2785 0.2713 0.2527 0.0013 0.0425 0.0293 143 VAL B CA 2745 C C . VAL B 145 ? 0.2621 0.2515 0.2421 0.0033 0.0464 0.0338 143 VAL B C 2746 O O . VAL B 145 ? 0.3180 0.3116 0.3105 0.0051 0.0494 0.0362 143 VAL B O 2747 C CB . VAL B 145 ? 0.3773 0.3680 0.3404 0.0061 0.0362 0.0325 143 VAL B CB 2748 C CG1 . VAL B 145 ? 0.3554 0.3507 0.3254 0.0124 0.0367 0.0355 143 VAL B CG1 2749 C CG2 . VAL B 145 ? 0.3933 0.3742 0.3431 0.0064 0.0318 0.0365 143 VAL B CG2 2750 N N . SER B 146 ? 0.2147 0.1979 0.1866 0.0026 0.0459 0.0359 144 SER B N 2751 C CA . SER B 146 ? 0.2378 0.2185 0.2149 0.0041 0.0493 0.0390 144 SER B CA 2752 C C . SER B 146 ? 0.3600 0.3331 0.3265 0.0059 0.0447 0.0424 144 SER B C 2753 O O . SER B 146 ? 0.3527 0.3214 0.3096 0.0034 0.0398 0.0432 144 SER B O 2754 C CB . SER B 146 ? 0.2841 0.2667 0.2697 -0.0005 0.0543 0.0353 144 SER B CB 2755 O OG . SER B 146 ? 0.2875 0.2676 0.2774 0.0009 0.0569 0.0384 144 SER B OG 2756 N N . THR B 147 ? 0.3809 0.3526 0.3503 0.0101 0.0456 0.0449 145 THR B N 2757 C CA . THR B 147 ? 0.3184 0.2827 0.2816 0.0113 0.0407 0.0467 145 THR B CA 2758 C C . THR B 147 ? 0.3260 0.2889 0.2900 0.0036 0.0424 0.0474 145 THR B C 2759 O O . THR B 147 ? 0.3397 0.2965 0.2996 0.0015 0.0371 0.0501 145 THR B O 2760 C CB . THR B 147 ? 0.2916 0.2582 0.2590 0.0178 0.0422 0.0483 145 THR B CB 2761 O OG1 . THR B 147 ? 0.2735 0.2459 0.2525 0.0152 0.0502 0.0493 145 THR B OG1 2762 C CG2 . THR B 147 ? 0.2508 0.2232 0.2157 0.0271 0.0402 0.0486 145 THR B CG2 2763 N N . GLY B 148 ? 0.2819 0.2517 0.2528 -0.0004 0.0493 0.0447 146 GLY B N 2764 C CA . GLY B 148 ? 0.2854 0.2588 0.2593 -0.0053 0.0527 0.0444 146 GLY B CA 2765 C C . GLY B 148 ? 0.2639 0.2370 0.2465 -0.0025 0.0557 0.0451 146 GLY B C 2766 O O . GLY B 148 ? 0.2238 0.1952 0.2097 0.0031 0.0557 0.0464 146 GLY B O 2767 N N . LEU B 149 ? 0.2586 0.2357 0.2449 -0.0058 0.0582 0.0449 147 LEU B N 2768 C CA . LEU B 149 ? 0.2449 0.2223 0.2398 -0.0030 0.0606 0.0456 147 LEU B CA 2769 C C . LEU B 149 ? 0.2886 0.2599 0.2792 -0.0011 0.0544 0.0499 147 LEU B C 2770 O O . LEU B 149 ? 0.2337 0.2035 0.2205 -0.0056 0.0499 0.0526 147 LEU B O 2771 C CB . LEU B 149 ? 0.2542 0.2405 0.2558 -0.0064 0.0654 0.0425 147 LEU B CB 2772 C CG . LEU B 149 ? 0.3400 0.3271 0.3512 -0.0034 0.0674 0.0432 147 LEU B CG 2773 C CD1 . LEU B 149 ? 0.3681 0.3514 0.3874 0.0021 0.0692 0.0430 147 LEU B CD1 2774 C CD2 . LEU B 149 ? 0.4146 0.4130 0.4327 -0.0055 0.0719 0.0391 147 LEU B CD2 2775 N N . ILE B 150 ? 0.2575 0.2266 0.2497 0.0059 0.0533 0.0509 148 ILE B N 2776 C CA . ILE B 150 ? 0.2524 0.2165 0.2399 0.0101 0.0457 0.0524 148 ILE B CA 2777 C C . ILE B 150 ? 0.2654 0.2328 0.2601 0.0127 0.0470 0.0532 148 ILE B C 2778 O O . ILE B 150 ? 0.2260 0.1982 0.2265 0.0172 0.0521 0.0544 148 ILE B O 2779 C CB . ILE B 150 ? 0.2739 0.2367 0.2548 0.0188 0.0421 0.0520 148 ILE B CB 2780 C CG1 . ILE B 150 ? 0.2929 0.2519 0.2666 0.0171 0.0389 0.0508 148 ILE B CG1 2781 C CG2 . ILE B 150 ? 0.3794 0.3390 0.3560 0.0260 0.0334 0.0507 148 ILE B CG2 2782 C CD1 . ILE B 150 ? 0.3682 0.3300 0.3365 0.0266 0.0363 0.0499 148 ILE B CD1 2783 N N . GLN B 151 ? 0.2566 0.2219 0.2525 0.0094 0.0419 0.0537 149 GLN B N 2784 C CA . GLN B 151 ? 0.2765 0.2448 0.2785 0.0128 0.0409 0.0540 149 GLN B CA 2785 C C . GLN B 151 ? 0.3368 0.3027 0.3327 0.0230 0.0339 0.0526 149 GLN B C 2786 O O . GLN B 151 ? 0.3637 0.3225 0.3521 0.0253 0.0250 0.0502 149 GLN B O 2787 C CB . GLN B 151 ? 0.3650 0.3331 0.3719 0.0056 0.0362 0.0552 149 GLN B CB 2788 C CG . GLN B 151 ? 0.4562 0.4347 0.4724 -0.0004 0.0442 0.0562 149 GLN B CG 2789 C CD . GLN B 151 ? 0.6079 0.5900 0.6305 -0.0078 0.0395 0.0596 149 GLN B CD 2790 O OE1 . GLN B 151 ? 0.6695 0.6440 0.6899 -0.0117 0.0303 0.0624 149 GLN B OE1 2791 N NE2 . GLN B 151 ? 0.6295 0.6235 0.6621 -0.0097 0.0450 0.0598 149 GLN B NE2 2792 N N . ASN B 152 ? 0.2693 0.2421 0.2683 0.0302 0.0369 0.0539 150 ASN B N 2793 C CA . ASN B 152 ? 0.2572 0.2325 0.2493 0.0416 0.0301 0.0521 150 ASN B CA 2794 C C . ASN B 152 ? 0.3088 0.2827 0.3034 0.0433 0.0214 0.0490 150 ASN B C 2795 O O . ASN B 152 ? 0.2629 0.2382 0.2510 0.0533 0.0128 0.0448 150 ASN B O 2796 C CB . ASN B 152 ? 0.2684 0.2551 0.2613 0.0497 0.0372 0.0573 150 ASN B CB 2797 C CG . ASN B 152 ? 0.3581 0.3472 0.3496 0.0490 0.0432 0.0604 150 ASN B CG 2798 O OD1 . ASN B 152 ? 0.2794 0.2643 0.2631 0.0493 0.0392 0.0569 150 ASN B OD1 2799 N ND2 . ASN B 152 ? 0.1919 0.1873 0.1929 0.0480 0.0519 0.0671 150 ASN B ND2 2800 N N . GLY B 153 ? 0.3105 0.2837 0.3151 0.0342 0.0233 0.0504 151 GLY B N 2801 C CA . GLY B 153 ? 0.2845 0.2573 0.2950 0.0335 0.0150 0.0483 151 GLY B CA 2802 C C . GLY B 153 ? 0.2802 0.2629 0.2952 0.0406 0.0177 0.0493 151 GLY B C 2803 O O . GLY B 153 ? 0.2920 0.2763 0.3129 0.0408 0.0109 0.0473 151 GLY B O 2804 N N . ASP B 154 ? 0.2547 0.2442 0.2687 0.0459 0.0268 0.0535 152 ASP B N 2805 C CA . ASP B 154 ? 0.2521 0.2513 0.2702 0.0535 0.0294 0.0569 152 ASP B CA 2806 C C . ASP B 154 ? 0.2728 0.2751 0.3025 0.0493 0.0403 0.0622 152 ASP B C 2807 O O . ASP B 154 ? 0.2151 0.2240 0.2483 0.0557 0.0443 0.0680 152 ASP B O 2808 C CB . ASP B 154 ? 0.3568 0.3640 0.3642 0.0664 0.0281 0.0590 152 ASP B CB 2809 C CG . ASP B 154 ? 0.3632 0.3717 0.3679 0.0660 0.0362 0.0644 152 ASP B CG 2810 O OD1 . ASP B 154 ? 0.2806 0.2813 0.2896 0.0562 0.0408 0.0639 152 ASP B OD1 2811 O OD2 . ASP B 154 ? 0.3521 0.3718 0.3509 0.0756 0.0378 0.0694 152 ASP B OD2 2812 N N . TRP B 155 ? 0.2537 0.2521 0.2900 0.0392 0.0442 0.0601 153 TRP B N 2813 C CA . TRP B 155 ? 0.2482 0.2490 0.2960 0.0361 0.0529 0.0617 153 TRP B CA 2814 C C . TRP B 155 ? 0.2934 0.2920 0.3412 0.0378 0.0586 0.0656 153 TRP B C 2815 O O . TRP B 155 ? 0.2926 0.2923 0.3517 0.0391 0.0634 0.0686 153 TRP B O 2816 C CB . TRP B 155 ? 0.2220 0.2293 0.2808 0.0403 0.0537 0.0634 153 TRP B CB 2817 C CG . TRP B 155 ? 0.2420 0.2539 0.3061 0.0363 0.0496 0.0595 153 TRP B CG 2818 C CD1 . TRP B 155 ? 0.2497 0.2622 0.3098 0.0374 0.0406 0.0580 153 TRP B CD1 2819 C CD2 . TRP B 155 ? 0.2349 0.2533 0.3108 0.0310 0.0539 0.0567 153 TRP B CD2 2820 N NE1 . TRP B 155 ? 0.2134 0.2321 0.2838 0.0315 0.0391 0.0560 153 TRP B NE1 2821 C CE2 . TRP B 155 ? 0.1938 0.2180 0.2733 0.0279 0.0479 0.0555 153 TRP B CE2 2822 C CE3 . TRP B 155 ? 0.2678 0.2890 0.3524 0.0293 0.0614 0.0541 153 TRP B CE3 2823 C CZ2 . TRP B 155 ? 0.2425 0.2780 0.3337 0.0227 0.0507 0.0538 153 TRP B CZ2 2824 C CZ3 . TRP B 155 ? 0.2487 0.2812 0.3433 0.0259 0.0639 0.0503 153 TRP B CZ3 2825 C CH2 . TRP B 155 ? 0.2130 0.2539 0.3108 0.0224 0.0592 0.0511 153 TRP B CH2 2826 N N . THR B 156 ? 0.2245 0.2196 0.2615 0.0376 0.0570 0.0654 154 THR B N 2827 C CA . THR B 156 ? 0.2007 0.1944 0.2393 0.0366 0.0620 0.0683 154 THR B CA 2828 C C . THR B 156 ? 0.2049 0.1932 0.2347 0.0310 0.0607 0.0636 154 THR B C 2829 O O . THR B 156 ? 0.2502 0.2355 0.2710 0.0299 0.0547 0.0604 154 THR B O 2830 C CB . THR B 156 ? 0.1963 0.1965 0.2317 0.0450 0.0622 0.0765 154 THR B CB 2831 O OG1 . THR B 156 ? 0.2838 0.2860 0.3041 0.0502 0.0563 0.0741 154 THR B OG1 2832 C CG2 . THR B 156 ? 0.3101 0.3172 0.3531 0.0514 0.0629 0.0833 154 THR B CG2 2833 N N . PHE B 157 ? 0.2228 0.2095 0.2565 0.0275 0.0651 0.0636 155 PHE B N 2834 C CA . PHE B 157 ? 0.2530 0.2359 0.2784 0.0231 0.0640 0.0601 155 PHE B CA 2835 C C . PHE B 157 ? 0.2711 0.2560 0.2950 0.0266 0.0652 0.0643 155 PHE B C 2836 O O . PHE B 157 ? 0.2199 0.2100 0.2520 0.0306 0.0681 0.0711 155 PHE B O 2837 C CB . PHE B 157 ? 0.2100 0.1920 0.2411 0.0159 0.0677 0.0547 155 PHE B CB 2838 C CG . PHE B 157 ? 0.2000 0.1848 0.2323 0.0119 0.0674 0.0512 155 PHE B CG 2839 C CD1 . PHE B 157 ? 0.2250 0.2096 0.2487 0.0066 0.0642 0.0502 155 PHE B CD1 2840 C CD2 . PHE B 157 ? 0.2709 0.2602 0.3147 0.0133 0.0703 0.0499 155 PHE B CD2 2841 C CE1 . PHE B 157 ? 0.2894 0.2806 0.3164 0.0019 0.0645 0.0494 155 PHE B CE1 2842 C CE2 . PHE B 157 ? 0.3611 0.3571 0.4073 0.0098 0.0707 0.0471 155 PHE B CE2 2843 C CZ . PHE B 157 ? 0.2979 0.2961 0.3359 0.0037 0.0682 0.0476 155 PHE B CZ 2844 N N . GLN B 158 ? 0.2062 0.1886 0.2210 0.0248 0.0629 0.0617 156 GLN B N 2845 C CA . GLN B 158 ? 0.2114 0.1974 0.2280 0.0261 0.0650 0.0648 156 GLN B CA 2846 C C . GLN B 158 ? 0.2579 0.2394 0.2696 0.0202 0.0639 0.0592 156 GLN B C 2847 O O . GLN B 158 ? 0.2632 0.2398 0.2680 0.0163 0.0611 0.0548 156 GLN B O 2848 C CB . GLN B 158 ? 0.2119 0.2053 0.2196 0.0352 0.0622 0.0689 156 GLN B CB 2849 C CG . GLN B 158 ? 0.2349 0.2232 0.2277 0.0384 0.0541 0.0629 156 GLN B CG 2850 C CD . GLN B 158 ? 0.3498 0.3470 0.3333 0.0495 0.0503 0.0638 156 GLN B CD 2851 O OE1 . GLN B 158 ? 0.3333 0.3377 0.3166 0.0516 0.0526 0.0662 156 GLN B OE1 2852 N NE2 . GLN B 158 ? 0.2620 0.2608 0.2384 0.0576 0.0442 0.0611 156 GLN B NE2 2853 N N . THR B 159 ? 0.2687 0.2532 0.2850 0.0194 0.0659 0.0606 157 THR B N 2854 C CA . THR B 159 ? 0.2478 0.2298 0.2582 0.0154 0.0641 0.0557 157 THR B CA 2855 C C . THR B 159 ? 0.2650 0.2537 0.2796 0.0177 0.0649 0.0594 157 THR B C 2856 O O . THR B 159 ? 0.2627 0.2573 0.2909 0.0185 0.0684 0.0657 157 THR B O 2857 C CB . THR B 159 ? 0.2770 0.2566 0.2936 0.0084 0.0663 0.0492 157 THR B CB 2858 O OG1 . THR B 159 ? 0.3082 0.2872 0.3165 0.0053 0.0638 0.0449 157 THR B OG1 2859 C CG2 . THR B 159 ? 0.2842 0.2655 0.3193 0.0072 0.0696 0.0494 157 THR B CG2 2860 N N . LEU B 160 ? 0.2459 0.2346 0.2503 0.0188 0.0612 0.0570 158 LEU B N 2861 C CA . LEU B 160 ? 0.2320 0.2291 0.2415 0.0202 0.0620 0.0598 158 LEU B CA 2862 C C . LEU B 160 ? 0.2535 0.2472 0.2645 0.0136 0.0609 0.0534 158 LEU B C 2863 O O . LEU B 160 ? 0.2569 0.2444 0.2559 0.0117 0.0573 0.0483 158 LEU B O 2864 C CB . LEU B 160 ? 0.2736 0.2764 0.2708 0.0289 0.0580 0.0609 158 LEU B CB 2865 C CG . LEU B 160 ? 0.4121 0.4277 0.4089 0.0385 0.0593 0.0676 158 LEU B CG 2866 C CD1 . LEU B 160 ? 0.3970 0.4090 0.3927 0.0405 0.0597 0.0689 158 LEU B CD1 2867 C CD2 . LEU B 160 ? 0.4779 0.4977 0.4604 0.0481 0.0531 0.0637 158 LEU B CD2 2868 N N . VAL B 161 ? 0.2299 0.2281 0.2567 0.0101 0.0631 0.0543 159 VAL B N 2869 C CA . VAL B 161 ? 0.2505 0.2474 0.2795 0.0050 0.0609 0.0469 159 VAL B CA 2870 C C . VAL B 161 ? 0.3011 0.3074 0.3369 0.0060 0.0598 0.0503 159 VAL B C 2871 O O . VAL B 161 ? 0.2469 0.2604 0.3007 0.0050 0.0620 0.0572 159 VAL B O 2872 C CB . VAL B 161 ? 0.2152 0.2083 0.2592 -0.0002 0.0622 0.0412 159 VAL B CB 2873 C CG1 . VAL B 161 ? 0.2292 0.2228 0.2730 -0.0038 0.0588 0.0312 159 VAL B CG1 2874 C CG2 . VAL B 161 ? 0.1914 0.1789 0.2302 -0.0001 0.0640 0.0387 159 VAL B CG2 2875 N N . MET B 162 ? 0.2593 0.2663 0.2822 0.0075 0.0559 0.0464 160 MET B N 2876 C CA . MET B 162 ? 0.2777 0.2956 0.3046 0.0099 0.0542 0.0491 160 MET B CA 2877 C C . MET B 162 ? 0.3333 0.3525 0.3693 0.0042 0.0516 0.0427 160 MET B C 2878 O O . MET B 162 ? 0.2946 0.3069 0.3225 0.0011 0.0490 0.0341 160 MET B O 2879 C CB . MET B 162 ? 0.3415 0.3590 0.3491 0.0167 0.0498 0.0478 160 MET B CB 2880 C CG . MET B 162 ? 0.5018 0.5260 0.5040 0.0258 0.0504 0.0535 160 MET B CG 2881 S SD . MET B 162 ? 0.5866 0.6009 0.5826 0.0270 0.0520 0.0546 160 MET B SD 2882 C CE . MET B 162 ? 0.4144 0.4124 0.3916 0.0263 0.0444 0.0476 160 MET B CE 2883 N N . LEU B 163 ? 0.1836 0.2140 0.2368 0.0030 0.0517 0.0472 161 LEU B N 2884 C CA . LEU B 163 ? 0.2268 0.2604 0.2887 -0.0013 0.0474 0.0406 161 LEU B CA 2885 C C . LEU B 163 ? 0.2424 0.2882 0.2996 0.0034 0.0451 0.0435 161 LEU B C 2886 O O . LEU B 163 ? 0.2184 0.2781 0.2852 0.0065 0.0479 0.0533 161 LEU B O 2887 C CB . LEU B 163 ? 0.1869 0.2229 0.2780 -0.0081 0.0472 0.0425 161 LEU B CB 2888 C CG . LEU B 163 ? 0.2225 0.2628 0.3275 -0.0127 0.0411 0.0350 161 LEU B CG 2889 C CD1 . LEU B 163 ? 0.2126 0.2445 0.3034 -0.0133 0.0365 0.0192 161 LEU B CD1 2890 C CD2 . LEU B 163 ? 0.1930 0.2350 0.3321 -0.0197 0.0393 0.0392 161 LEU B CD2 2891 N N . GLU B 164 ? 0.2723 0.3151 0.3150 0.0045 0.0401 0.0356 162 GLU B N 2892 C CA . GLU B 164 ? 0.2710 0.3248 0.3103 0.0092 0.0365 0.0363 162 GLU B CA 2893 C C . GLU B 164 ? 0.2375 0.3028 0.2995 0.0039 0.0345 0.0356 162 GLU B C 2894 O O . GLU B 164 ? 0.2456 0.3068 0.3113 -0.0011 0.0301 0.0265 162 GLU B O 2895 C CB . GLU B 164 ? 0.2485 0.2940 0.2657 0.0118 0.0307 0.0293 162 GLU B CB 2896 C CG . GLU B 164 ? 0.2790 0.3129 0.2766 0.0164 0.0305 0.0311 162 GLU B CG 2897 C CD . GLU B 164 ? 0.3750 0.3988 0.3546 0.0155 0.0249 0.0265 162 GLU B CD 2898 O OE1 . GLU B 164 ? 0.3825 0.4095 0.3628 0.0118 0.0221 0.0211 162 GLU B OE1 2899 O OE2 . GLU B 164 ? 0.3687 0.3824 0.3344 0.0185 0.0227 0.0289 162 GLU B OE2 2900 N N . THR B 165 ? 0.1957 0.2776 0.2740 0.0053 0.0373 0.0455 163 THR B N 2901 C CA . THR B 165 ? 0.2283 0.3226 0.3329 -0.0010 0.0350 0.0473 163 THR B CA 2902 C C . THR B 165 ? 0.2164 0.3347 0.3311 0.0037 0.0382 0.0594 163 THR B C 2903 O O . THR B 165 ? 0.1827 0.3081 0.2906 0.0103 0.0438 0.0680 163 THR B O 2904 C CB . THR B 165 ? 0.2635 0.3513 0.3931 -0.0104 0.0359 0.0494 163 THR B CB 2905 O OG1 . THR B 165 ? 0.3641 0.4622 0.5226 -0.0175 0.0314 0.0508 163 THR B OG1 2906 C CG2 . THR B 165 ? 0.2372 0.3290 0.3734 -0.0092 0.0434 0.0635 163 THR B CG2 2907 N N . VAL B 166 ? 0.1865 0.3197 0.3172 0.0012 0.0344 0.0596 164 VAL B N 2908 C CA . VAL B 166 ? 0.1921 0.3537 0.3394 0.0039 0.0380 0.0729 164 VAL B CA 2909 C C . VAL B 166 ? 0.2829 0.4525 0.4670 -0.0079 0.0393 0.0842 164 VAL B C 2910 O O . VAL B 166 ? 0.2767 0.4443 0.4813 -0.0167 0.0327 0.0793 164 VAL B O 2911 C CB . VAL B 166 ? 0.1856 0.3625 0.3324 0.0080 0.0328 0.0683 164 VAL B CB 2912 C CG1 . VAL B 166 ? 0.1827 0.3940 0.3487 0.0112 0.0375 0.0831 164 VAL B CG1 2913 C CG2 . VAL B 166 ? 0.1888 0.3553 0.3021 0.0191 0.0293 0.0577 164 VAL B CG2 2914 N N . PRO B 167 ? 0.2614 0.4399 0.4548 -0.0079 0.0466 0.0996 165 PRO B N 2915 C CA . PRO B 167 ? 0.2221 0.4066 0.4525 -0.0196 0.0471 0.1133 165 PRO B CA 2916 C C . PRO B 167 ? 0.2691 0.4806 0.5302 -0.0253 0.0451 0.1238 165 PRO B C 2917 O O . PRO B 167 ? 0.2475 0.4864 0.5035 -0.0174 0.0488 0.1303 165 PRO B O 2918 C CB . PRO B 167 ? 0.2399 0.4341 0.4677 -0.0152 0.0563 0.1296 165 PRO B CB 2919 C CG . PRO B 167 ? 0.2556 0.4340 0.4447 -0.0040 0.0582 0.1175 165 PRO B CG 2920 C CD . PRO B 167 ? 0.2845 0.4643 0.4545 0.0027 0.0535 0.1040 165 PRO B CD 2921 N N . ARG B 168 ? 0.2414 0.4457 0.5357 -0.0387 0.0382 0.1247 166 ARG B N 2922 C CA . ARG B 168 ? 0.3183 0.5474 0.6492 -0.0470 0.0352 0.1372 166 ARG B CA 2923 C C . ARG B 168 ? 0.3329 0.5655 0.6953 -0.0566 0.0369 0.1581 166 ARG B C 2924 O O . ARG B 168 ? 0.3455 0.5537 0.7096 -0.0601 0.0357 0.1563 166 ARG B O 2925 C CB . ARG B 168 ? 0.3567 0.5724 0.7018 -0.0547 0.0224 0.1199 166 ARG B CB 2926 C CG . ARG B 168 ? 0.4062 0.6225 0.7222 -0.0455 0.0191 0.1019 166 ARG B CG 2927 C CD . ARG B 168 ? 0.4490 0.6460 0.7723 -0.0517 0.0062 0.0816 166 ARG B CD 2928 N NE . ARG B 168 ? 0.3359 0.5398 0.6411 -0.0451 0.0014 0.0683 166 ARG B NE 2929 C CZ . ARG B 168 ? 0.3368 0.5280 0.6024 -0.0350 0.0019 0.0545 166 ARG B CZ 2930 N NH1 . ARG B 168 ? 0.3100 0.4822 0.5506 -0.0305 0.0074 0.0520 166 ARG B NH1 2931 N NH2 . ARG B 168 ? 0.3496 0.5477 0.6022 -0.0296 -0.0036 0.0445 166 ARG B NH2 2932 N N . SER B 169 ? 0.3304 0.5843 0.7046 -0.0576 0.0377 0.1736 167 SER B N 2933 C CA . SER B 169 ? 0.3882 0.6371 0.7824 -0.0644 0.0356 0.1903 167 SER B CA 2934 C C . SER B 169 ? 0.3380 0.5583 0.7610 -0.0771 0.0233 0.1812 167 SER B C 2935 O O . SER B 169 ? 0.3343 0.5486 0.7690 -0.0823 0.0150 0.1653 167 SER B O 2936 C CB . SER B 169 ? 0.4394 0.7181 0.8467 -0.0649 0.0368 0.2079 167 SER B CB 2937 O OG . SER B 169 ? 0.5231 0.8284 0.9027 -0.0512 0.0470 0.2142 167 SER B OG 2938 N N . GLY B 170 ? 0.3296 0.5327 0.7636 -0.0807 0.0208 0.1897 168 GLY B N 2939 C CA . GLY B 170 ? 0.3833 0.5575 0.8436 -0.0903 0.0080 0.1796 168 GLY B CA 2940 C C . GLY B 170 ? 0.4073 0.5540 0.8540 -0.0880 0.0071 0.1618 168 GLY B C 2941 O O . GLY B 170 ? 0.4502 0.5732 0.9120 -0.0917 -0.0003 0.1588 168 GLY B O 2942 N N . GLU B 171 ? 0.3190 0.4699 0.7380 -0.0812 0.0144 0.1505 169 GLU B N 2943 C CA . GLU B 171 ? 0.3639 0.4915 0.7689 -0.0790 0.0146 0.1337 169 GLU B CA 2944 C C . GLU B 171 ? 0.3837 0.5011 0.7758 -0.0741 0.0212 0.1437 169 GLU B C 2945 O O . GLU B 171 ? 0.3374 0.4722 0.7131 -0.0673 0.0307 0.1599 169 GLU B O 2946 C CB . GLU B 171 ? 0.2591 0.3900 0.6241 -0.0687 0.0195 0.1175 169 GLU B CB 2947 C CG . GLU B 171 ? 0.3255 0.4572 0.6910 -0.0699 0.0102 0.0998 169 GLU B CG 2948 C CD . GLU B 171 ? 0.4177 0.5490 0.7384 -0.0581 0.0137 0.0842 169 GLU B CD 2949 O OE1 . GLU B 171 ? 0.2771 0.4141 0.5696 -0.0490 0.0237 0.0906 169 GLU B OE1 2950 O OE2 . GLU B 171 ? 0.5451 0.6704 0.8597 -0.0577 0.0054 0.0657 169 GLU B OE2 2951 N N . VAL B 172 ? 0.4135 0.5037 0.8127 -0.0766 0.0150 0.1321 170 VAL B N 2952 C CA . VAL B 172 ? 0.3620 0.4410 0.7480 -0.0714 0.0205 0.1377 170 VAL B CA 2953 C C . VAL B 172 ? 0.2868 0.3493 0.6487 -0.0668 0.0235 0.1180 170 VAL B C 2954 O O . VAL B 172 ? 0.3236 0.3667 0.6864 -0.0675 0.0143 0.0957 170 VAL B O 2955 C CB . VAL B 172 ? 0.3973 0.4601 0.8106 -0.0756 0.0110 0.1431 170 VAL B CB 2956 C CG1 . VAL B 172 ? 0.5395 0.5860 0.9808 -0.0830 -0.0040 0.1266 170 VAL B CG1 2957 C CG2 . VAL B 172 ? 0.3155 0.3612 0.7176 -0.0705 0.0138 0.1404 170 VAL B CG2 2958 N N . TYR B 173 ? 0.2173 0.2867 0.5456 -0.0574 0.0344 0.1222 171 TYR B N 2959 C CA . TYR B 173 ? 0.2240 0.2771 0.5167 -0.0492 0.0365 0.1030 171 TYR B CA 2960 C C . TYR B 173 ? 0.2659 0.3054 0.5605 -0.0478 0.0388 0.1073 171 TYR B C 2961 O O . TYR B 173 ? 0.3104 0.3591 0.6191 -0.0492 0.0433 0.1287 171 TYR B O 2962 C CB . TYR B 173 ? 0.1968 0.2634 0.4522 -0.0395 0.0448 0.1029 171 TYR B CB 2963 C CG . TYR B 173 ? 0.2261 0.3039 0.4745 -0.0388 0.0419 0.0954 171 TYR B CG 2964 C CD1 . TYR B 173 ? 0.2165 0.2832 0.4415 -0.0354 0.0379 0.0745 171 TYR B CD1 2965 C CD2 . TYR B 173 ? 0.2134 0.3154 0.4785 -0.0410 0.0433 0.1103 171 TYR B CD2 2966 C CE1 . TYR B 173 ? 0.2395 0.3162 0.4578 -0.0342 0.0346 0.0681 171 TYR B CE1 2967 C CE2 . TYR B 173 ? 0.1954 0.3082 0.4544 -0.0396 0.0402 0.1028 171 TYR B CE2 2968 C CZ . TYR B 173 ? 0.2357 0.3345 0.4709 -0.0361 0.0355 0.0815 171 TYR B CZ 2969 O OH . TYR B 173 ? 0.3022 0.4111 0.5306 -0.0341 0.0317 0.0742 171 TYR B OH 2970 N N . THR B 174 ? 0.2288 0.2488 0.5090 -0.0446 0.0359 0.0877 172 THR B N 2971 C CA . THR B 174 ? 0.2432 0.2502 0.5248 -0.0425 0.0374 0.0894 172 THR B CA 2972 C C . THR B 174 ? 0.2210 0.2211 0.4660 -0.0344 0.0419 0.0743 172 THR B C 2973 O O . THR B 174 ? 0.2622 0.2565 0.4929 -0.0327 0.0383 0.0550 172 THR B O 2974 C CB . THR B 174 ? 0.2409 0.2292 0.5547 -0.0480 0.0264 0.0805 172 THR B CB 2975 O OG1 . THR B 174 ? 0.2603 0.2537 0.6127 -0.0572 0.0203 0.0951 172 THR B OG1 2976 C CG2 . THR B 174 ? 0.3217 0.2977 0.6388 -0.0450 0.0278 0.0837 172 THR B CG2 2977 N N . CYS B 175 ? 0.2028 0.2054 0.4331 -0.0293 0.0493 0.0842 173 CYS B N 2978 C CA . CYS B 175 ? 0.3052 0.3002 0.5069 -0.0230 0.0525 0.0719 173 CYS B CA 2979 C C . CYS B 175 ? 0.2605 0.2411 0.4768 -0.0232 0.0497 0.0677 173 CYS B C 2980 O O . CYS B 175 ? 0.2692 0.2495 0.5049 -0.0246 0.0503 0.0829 173 CYS B O 2981 C CB . CYS B 175 ? 0.1912 0.1966 0.3690 -0.0166 0.0604 0.0828 173 CYS B CB 2982 S SG . CYS B 175 ? 0.2434 0.2396 0.3901 -0.0105 0.0631 0.0696 173 CYS B SG 2983 N N . GLN B 176 ? 0.2958 0.2666 0.5029 -0.0210 0.0466 0.0477 174 GLN B N 2984 C CA . GLN B 176 ? 0.2763 0.2347 0.4962 -0.0193 0.0433 0.0401 174 GLN B CA 2985 C C . GLN B 176 ? 0.2848 0.2433 0.4783 -0.0131 0.0489 0.0333 174 GLN B C 2986 O O . GLN B 176 ? 0.2254 0.1887 0.3944 -0.0111 0.0511 0.0230 174 GLN B O 2987 C CB . GLN B 176 ? 0.2404 0.1900 0.4773 -0.0207 0.0333 0.0206 174 GLN B CB 2988 C CG . GLN B 176 ? 0.3056 0.2426 0.5577 -0.0171 0.0279 0.0089 174 GLN B CG 2989 C CD . GLN B 176 ? 0.4017 0.3337 0.6622 -0.0152 0.0179 -0.0159 174 GLN B CD 2990 O OE1 . GLN B 176 ? 0.4127 0.3347 0.7048 -0.0183 0.0071 -0.0200 174 GLN B OE1 2991 N NE2 . GLN B 176 ? 0.3973 0.3377 0.6301 -0.0100 0.0208 -0.0322 174 GLN B NE2 2992 N N . VAL B 177 ? 0.2272 0.1813 0.4276 -0.0107 0.0508 0.0404 175 VAL B N 2993 C CA . VAL B 177 ? 0.2069 0.1623 0.3865 -0.0054 0.0559 0.0363 175 VAL B CA 2994 C C . VAL B 177 ? 0.2486 0.1952 0.4422 -0.0020 0.0523 0.0256 175 VAL B C 2995 O O . VAL B 177 ? 0.2647 0.2029 0.4842 -0.0027 0.0480 0.0321 175 VAL B O 2996 C CB . VAL B 177 ? 0.2061 0.1675 0.3765 -0.0033 0.0620 0.0546 175 VAL B CB 2997 C CG1 . VAL B 177 ? 0.2265 0.1891 0.3770 0.0014 0.0659 0.0498 175 VAL B CG1 2998 C CG2 . VAL B 177 ? 0.1937 0.1655 0.3509 -0.0044 0.0649 0.0640 175 VAL B CG2 2999 N N . GLU B 178 ? 0.2340 0.1839 0.4115 0.0018 0.0535 0.0097 176 GLU B N 3000 C CA . GLU B 178 ? 0.2276 0.1737 0.4145 0.0070 0.0510 -0.0025 176 GLU B CA 3001 C C . GLU B 178 ? 0.3048 0.2589 0.4712 0.0105 0.0581 0.0000 176 GLU B C 3002 O O . GLU B 178 ? 0.2553 0.2185 0.3978 0.0093 0.0628 0.0001 176 GLU B O 3003 C CB . GLU B 178 ? 0.3108 0.2593 0.4984 0.0098 0.0458 -0.0253 176 GLU B CB 3004 C CG . GLU B 178 ? 0.3697 0.3093 0.5807 0.0071 0.0362 -0.0319 176 GLU B CG 3005 C CD . GLU B 178 ? 0.5052 0.4525 0.7070 0.0098 0.0321 -0.0536 176 GLU B CD 3006 O OE1 . GLU B 178 ? 0.4996 0.4568 0.6796 0.0071 0.0362 -0.0519 176 GLU B OE1 3007 O OE2 . GLU B 178 ? 0.5102 0.4545 0.7262 0.0156 0.0243 -0.0726 176 GLU B OE2 3008 N N . HIS B 179 ? 0.2366 0.1869 0.4142 0.0144 0.0579 0.0024 177 HIS B N 3009 C CA . HIS B 179 ? 0.2400 0.1974 0.4024 0.0171 0.0637 0.0075 177 HIS B CA 3010 C C . HIS B 179 ? 0.2502 0.2038 0.4298 0.0230 0.0611 0.0023 177 HIS B C 3011 O O . HIS B 179 ? 0.2334 0.1756 0.4376 0.0241 0.0548 0.0022 177 HIS B O 3012 C CB . HIS B 179 ? 0.2247 0.1823 0.3800 0.0149 0.0671 0.0274 177 HIS B CB 3013 C CG . HIS B 179 ? 0.2459 0.2104 0.3854 0.0174 0.0714 0.0320 177 HIS B CG 3014 N ND1 . HIS B 179 ? 0.2566 0.2198 0.4046 0.0213 0.0715 0.0397 177 HIS B ND1 3015 C CD2 . HIS B 179 ? 0.2579 0.2304 0.3756 0.0163 0.0746 0.0302 177 HIS B CD2 3016 C CE1 . HIS B 179 ? 0.2872 0.2579 0.4191 0.0226 0.0744 0.0413 177 HIS B CE1 3017 N NE2 . HIS B 179 ? 0.2348 0.2104 0.3492 0.0192 0.0760 0.0358 177 HIS B NE2 3018 N N . PRO B 180 ? 0.2761 0.2395 0.4450 0.0268 0.0650 -0.0020 178 PRO B N 3019 C CA . PRO B 180 ? 0.2494 0.2110 0.4348 0.0338 0.0623 -0.0086 178 PRO B CA 3020 C C . PRO B 180 ? 0.2820 0.2323 0.4850 0.0350 0.0596 0.0069 178 PRO B C 3021 O O . PRO B 180 ? 0.2733 0.2170 0.4967 0.0406 0.0545 0.0018 178 PRO B O 3022 C CB . PRO B 180 ? 0.3132 0.2911 0.4815 0.0360 0.0682 -0.0122 178 PRO B CB 3023 C CG . PRO B 180 ? 0.3074 0.2953 0.4538 0.0308 0.0721 -0.0142 178 PRO B CG 3024 C CD . PRO B 180 ? 0.2858 0.2631 0.4298 0.0250 0.0708 -0.0035 178 PRO B CD 3025 N N . SER B 181 ? 0.2309 0.1806 0.4262 0.0308 0.0625 0.0254 179 SER B N 3026 C CA . SER B 181 ? 0.2755 0.2185 0.4862 0.0321 0.0605 0.0426 179 SER B CA 3027 C C . SER B 181 ? 0.3198 0.2499 0.5567 0.0292 0.0539 0.0480 179 SER B C 3028 O O . SER B 181 ? 0.2883 0.2125 0.5430 0.0298 0.0510 0.0636 179 SER B O 3029 C CB . SER B 181 ? 0.2237 0.1744 0.4171 0.0302 0.0655 0.0599 179 SER B CB 3030 O OG . SER B 181 ? 0.2788 0.2304 0.4651 0.0247 0.0666 0.0636 179 SER B OG 3031 N N . LEU B 182 ? 0.2949 0.2216 0.5347 0.0257 0.0510 0.0365 180 LEU B N 3032 C CA . LEU B 182 ? 0.2941 0.2090 0.5600 0.0213 0.0437 0.0415 180 LEU B CA 3033 C C . LEU B 182 ? 0.3384 0.2413 0.6274 0.0252 0.0338 0.0218 180 LEU B C 3034 O O . LEU B 182 ? 0.3702 0.2785 0.6482 0.0296 0.0338 0.0001 180 LEU B O 3035 C CB . LEU B 182 ? 0.2968 0.2166 0.5519 0.0145 0.0458 0.0432 180 LEU B CB 3036 C CG . LEU B 182 ? 0.2880 0.2203 0.5208 0.0122 0.0542 0.0604 180 LEU B CG 3037 C CD1 . LEU B 182 ? 0.2944 0.2323 0.5138 0.0074 0.0559 0.0570 180 LEU B CD1 3038 C CD2 . LEU B 182 ? 0.2857 0.2183 0.5347 0.0108 0.0540 0.0851 180 LEU B CD2 3039 N N . THR B 183 ? 0.3160 0.2038 0.6378 0.0241 0.0246 0.0295 181 THR B N 3040 C CA . THR B 183 ? 0.3235 0.2001 0.6679 0.0281 0.0122 0.0096 181 THR B CA 3041 C C . THR B 183 ? 0.3556 0.2270 0.7119 0.0222 0.0044 0.0012 181 THR B C 3042 O O . THR B 183 ? 0.4003 0.2656 0.7702 0.0257 -0.0066 -0.0195 181 THR B O 3043 C CB . THR B 183 ? 0.3788 0.2500 0.7439 0.0286 0.0035 0.0193 181 THR B CB 3044 O OG1 . THR B 183 ? 0.3130 0.1866 0.6886 0.0194 0.0024 0.0449 181 THR B OG1 3045 C CG2 . THR B 183 ? 0.2969 0.1735 0.6505 0.0358 0.0098 0.0232 181 THR B CG2 3046 N N . SER B 184 ? 0.3183 0.1941 0.6686 0.0138 0.0096 0.0165 182 SER B N 3047 C CA . SER B 184 ? 0.2898 0.1629 0.6489 0.0082 0.0035 0.0085 182 SER B CA 3048 C C . SER B 184 ? 0.3234 0.2096 0.6581 0.0023 0.0146 0.0210 182 SER B C 3049 O O . SER B 184 ? 0.3257 0.2218 0.6429 0.0020 0.0245 0.0385 182 SER B O 3050 C CB . SER B 184 ? 0.3361 0.2048 0.7256 0.0019 -0.0092 0.0184 182 SER B CB 3051 O OG . SER B 184 ? 0.3363 0.2146 0.7279 -0.0052 -0.0042 0.0477 182 SER B OG 3052 N N . PRO B 185 ? 0.2945 0.1839 0.6251 -0.0014 0.0122 0.0105 183 PRO B N 3053 C CA . PRO B 185 ? 0.3230 0.2275 0.6273 -0.0058 0.0219 0.0207 183 PRO B CA 3054 C C . PRO B 185 ? 0.2738 0.1831 0.5869 -0.0121 0.0261 0.0500 183 PRO B C 3055 O O . PRO B 185 ? 0.2805 0.1841 0.6240 -0.0171 0.0188 0.0618 183 PRO B O 3056 C CB . PRO B 185 ? 0.3577 0.2624 0.6650 -0.0087 0.0155 0.0048 183 PRO B CB 3057 C CG . PRO B 185 ? 0.3456 0.2404 0.6660 -0.0022 0.0052 -0.0210 183 PRO B CG 3058 C CD . PRO B 185 ? 0.3327 0.2138 0.6789 0.0001 0.0002 -0.0137 183 PRO B CD 3059 N N . LEU B 186 ? 0.2979 0.2215 0.5826 -0.0110 0.0370 0.0609 184 LEU B N 3060 C CA . LEU B 186 ? 0.3117 0.2464 0.5987 -0.0146 0.0421 0.0867 184 LEU B CA 3061 C C . LEU B 186 ? 0.2921 0.2364 0.5731 -0.0195 0.0430 0.0867 184 LEU B C 3062 O O . LEU B 186 ? 0.2515 0.2007 0.5060 -0.0172 0.0462 0.0734 184 LEU B O 3063 C CB . LEU B 186 ? 0.3544 0.3000 0.6132 -0.0087 0.0518 0.0949 184 LEU B CB 3064 C CG . LEU B 186 ? 0.4674 0.4294 0.7238 -0.0078 0.0563 0.1190 184 LEU B CG 3065 C CD1 . LEU B 186 ? 0.5744 0.5367 0.8566 -0.0086 0.0493 0.1298 184 LEU B CD1 3066 C CD2 . LEU B 186 ? 0.5037 0.4722 0.7330 -0.0007 0.0639 0.1211 184 LEU B CD2 3067 N N . THR B 187 ? 0.2810 0.2298 0.5861 -0.0257 0.0390 0.1014 185 THR B N 3068 C CA . THR B 187 ? 0.2900 0.2483 0.5949 -0.0308 0.0393 0.1029 185 THR B CA 3069 C C . THR B 187 ? 0.3557 0.3374 0.6544 -0.0298 0.0441 0.1250 185 THR B C 3070 O O . THR B 187 ? 0.2653 0.2536 0.5762 -0.0287 0.0419 0.1395 185 THR B O 3071 C CB . THR B 187 ? 0.2577 0.2059 0.5934 -0.0371 0.0268 0.0935 185 THR B CB 3072 O OG1 . THR B 187 ? 0.2764 0.2253 0.6371 -0.0382 0.0195 0.1063 185 THR B OG1 3073 C CG2 . THR B 187 ? 0.2748 0.2053 0.6098 -0.0339 0.0202 0.0656 185 THR B CG2 3074 N N . VAL B 188 ? 0.2694 0.2649 0.5497 -0.0294 0.0502 0.1269 186 VAL B N 3075 C CA . VAL B 188 ? 0.2842 0.3038 0.5583 -0.0269 0.0540 0.1445 186 VAL B CA 3076 C C . VAL B 188 ? 0.2328 0.2614 0.5148 -0.0323 0.0522 0.1441 186 VAL B C 3077 O O . VAL B 188 ? 0.2321 0.2569 0.5036 -0.0338 0.0541 0.1315 186 VAL B O 3078 C CB . VAL B 188 ? 0.3358 0.3679 0.5760 -0.0177 0.0630 0.1471 186 VAL B CB 3079 C CG1 . VAL B 188 ? 0.3488 0.4074 0.5826 -0.0133 0.0659 0.1621 186 VAL B CG1 3080 C CG2 . VAL B 188 ? 0.2915 0.3166 0.5253 -0.0125 0.0642 0.1481 186 VAL B CG2 3081 N N . GLU B 189 ? 0.2230 0.2647 0.5248 -0.0353 0.0484 0.1585 187 GLU B N 3082 C CA . GLU B 189 ? 0.3314 0.3837 0.6439 -0.0406 0.0460 0.1599 187 GLU B CA 3083 C C . GLU B 189 ? 0.3117 0.3912 0.6042 -0.0344 0.0538 0.1709 187 GLU B C 3084 O O . GLU B 189 ? 0.3234 0.4167 0.6035 -0.0270 0.0583 0.1825 187 GLU B O 3085 C CB . GLU B 189 ? 0.3393 0.3907 0.6878 -0.0479 0.0364 0.1695 187 GLU B CB 3086 C CG . GLU B 189 ? 0.4380 0.4629 0.8102 -0.0531 0.0257 0.1561 187 GLU B CG 3087 C CD . GLU B 189 ? 0.5331 0.5569 0.9420 -0.0605 0.0143 0.1631 187 GLU B CD 3088 O OE1 . GLU B 189 ? 0.5295 0.5737 0.9469 -0.0617 0.0157 0.1832 187 GLU B OE1 3089 O OE2 . GLU B 189 ? 0.5251 0.5283 0.9544 -0.0645 0.0033 0.1479 187 GLU B OE2 3090 N N . TRP B 190 ? 0.2675 0.3558 0.5579 -0.0367 0.0544 0.1659 188 TRP B N 3091 C CA . TRP B 190 ? 0.2312 0.3470 0.5075 -0.0307 0.0599 0.1752 188 TRP B CA 3092 C C . TRP B 190 ? 0.2999 0.4251 0.5966 -0.0381 0.0555 0.1763 188 TRP B C 3093 O O . TRP B 190 ? 0.2702 0.3821 0.5771 -0.0449 0.0508 0.1623 188 TRP B O 3094 C CB . TRP B 190 ? 0.2794 0.3979 0.5220 -0.0220 0.0669 0.1646 188 TRP B CB 3095 C CG . TRP B 190 ? 0.3270 0.4730 0.5530 -0.0132 0.0714 0.1706 188 TRP B CG 3096 C CD1 . TRP B 190 ? 0.3453 0.5084 0.5527 -0.0019 0.0754 0.1786 188 TRP B CD1 3097 C CD2 . TRP B 190 ? 0.3104 0.4712 0.5378 -0.0137 0.0715 0.1676 188 TRP B CD2 3098 N NE1 . TRP B 190 ? 0.3240 0.5109 0.5205 0.0052 0.0777 0.1799 188 TRP B NE1 3099 C CE2 . TRP B 190 ? 0.2695 0.4556 0.4779 -0.0018 0.0757 0.1736 188 TRP B CE2 3100 C CE3 . TRP B 190 ? 0.2625 0.4190 0.5065 -0.0224 0.0675 0.1593 188 TRP B CE3 3101 C CZ2 . TRP B 190 ? 0.2549 0.4614 0.4596 0.0020 0.0765 0.1719 188 TRP B CZ2 3102 C CZ3 . TRP B 190 ? 0.2437 0.4214 0.4847 -0.0192 0.0684 0.1585 188 TRP B CZ3 3103 C CH2 . TRP B 190 ? 0.2258 0.4281 0.4471 -0.0069 0.0732 0.1650 188 TRP B CH2 3104 N N . ARG B 191 ? 0.3188 0.4685 0.6226 -0.0366 0.0564 0.1924 189 ARG B N 3105 C CA . ARG B 191 ? 0.3174 0.4800 0.6404 -0.0429 0.0526 0.1953 189 ARG B CA 3106 C C . ARG B 191 ? 0.3439 0.5366 0.6473 -0.0340 0.0594 0.2003 189 ARG B C 3107 O O . ARG B 191 ? 0.3309 0.5395 0.6160 -0.0238 0.0650 0.2093 189 ARG B O 3108 C CB . ARG B 191 ? 0.4161 0.5814 0.7719 -0.0505 0.0459 0.2117 189 ARG B CB 3109 C CG . ARG B 191 ? 0.4110 0.5469 0.7932 -0.0599 0.0357 0.2041 189 ARG B CG 3110 C CD . ARG B 191 ? 0.5365 0.6757 0.9489 -0.0649 0.0294 0.2233 189 ARG B CD 3111 N NE . ARG B 191 ? 0.6451 0.7569 1.0861 -0.0730 0.0173 0.2149 189 ARG B NE 3112 C CZ . ARG B 191 ? 0.7107 0.8007 1.1524 -0.0714 0.0145 0.2081 189 ARG B CZ 3113 N NH1 . ARG B 191 ? 0.6954 0.7871 1.1106 -0.0630 0.0233 0.2091 189 ARG B NH1 3114 N NH2 . ARG B 191 ? 0.7192 0.7860 1.1882 -0.0774 0.0021 0.1989 189 ARG B NH2 3115 N N . ALA B 192 ? 0.3710 0.5723 0.6790 -0.0367 0.0579 0.1931 190 ALA B N 3116 C CA . ALA B 192 ? 0.3592 0.5898 0.6510 -0.0275 0.0630 0.1961 190 ALA B CA 3117 C C . ALA B 192 ? 0.2593 0.5159 0.5600 -0.0252 0.0645 0.2169 190 ALA B C 3118 O O . ALA B 192 ? 0.3040 0.5603 0.6339 -0.0351 0.0593 0.2285 190 ALA B O 3119 C CB . ALA B 192 ? 0.2868 0.5225 0.5875 -0.0318 0.0596 0.1850 190 ALA B CB 3120 N N . SER C 1 ? 0.5397 0.5377 0.6456 0.0738 0.0095 0.2642 1 SER C N 3121 C CA . SER C 1 ? 0.5163 0.5244 0.6409 0.0760 -0.0021 0.2511 1 SER C CA 3122 C C . SER C 1 ? 0.4831 0.5047 0.5651 0.0677 -0.0159 0.2289 1 SER C C 3123 O O . SER C 1 ? 0.4523 0.4713 0.4954 0.0609 -0.0107 0.2219 1 SER C O 3124 C CB . SER C 1 ? 0.5215 0.5020 0.7017 0.0767 0.0195 0.2426 1 SER C CB 3125 O OG . SER C 1 ? 0.6683 0.6215 0.8466 0.0628 0.0371 0.2315 1 SER C OG 3126 N N . ALA C 2 ? 0.4235 0.4610 0.5169 0.0686 -0.0308 0.2182 2 ALA C N 3127 C CA . ALA C 2 ? 0.3413 0.3928 0.3916 0.0603 -0.0473 0.1977 2 ALA C CA 3128 C C . ALA C 2 ? 0.2969 0.3430 0.3556 0.0507 -0.0352 0.1632 2 ALA C C 3129 O O . ALA C 2 ? 0.3551 0.3970 0.4569 0.0515 -0.0259 0.1514 2 ALA C O 3130 C CB . ALA C 2 ? 0.3665 0.4397 0.4167 0.0593 -0.0725 0.1980 2 ALA C CB 3131 N N . VAL C 3 ? 0.3055 0.3503 0.3198 0.0427 -0.0326 0.1468 3 VAL C N 3132 C CA . VAL C 3 ? 0.2896 0.3355 0.3027 0.0331 -0.0256 0.1158 3 VAL C CA 3133 C C . VAL C 3 ? 0.2891 0.3483 0.3026 0.0321 -0.0420 0.1039 3 VAL C C 3134 O O . VAL C 3 ? 0.2963 0.3630 0.2813 0.0327 -0.0616 0.1130 3 VAL C O 3135 C CB . VAL C 3 ? 0.2459 0.2917 0.2148 0.0293 -0.0185 0.1101 3 VAL C CB 3136 C CG1 . VAL C 3 ? 0.2669 0.3192 0.2318 0.0218 -0.0152 0.0834 3 VAL C CG1 3137 C CG2 . VAL C 3 ? 0.2549 0.2949 0.2356 0.0275 -0.0010 0.1247 3 VAL C CG2 3138 N N . ARG C 4 ? 0.2087 0.2694 0.2521 0.0287 -0.0340 0.0842 4 ARG C N 3139 C CA . ARG C 4 ? 0.2310 0.3067 0.2847 0.0272 -0.0456 0.0754 4 ARG C CA 3140 C C . ARG C 4 ? 0.2180 0.2936 0.2389 0.0186 -0.0435 0.0524 4 ARG C C 3141 O O . ARG C 4 ? 0.2617 0.3305 0.2739 0.0148 -0.0283 0.0398 4 ARG C O 3142 C CB . ARG C 4 ? 0.1868 0.2627 0.2944 0.0326 -0.0323 0.0718 4 ARG C CB 3143 C CG . ARG C 4 ? 0.3400 0.4182 0.4911 0.0457 -0.0327 0.0996 4 ARG C CG 3144 C CD . ARG C 4 ? 0.3424 0.4136 0.5451 0.0551 -0.0108 0.0954 4 ARG C CD 3145 N NE . ARG C 4 ? 0.3220 0.3948 0.5745 0.0721 -0.0063 0.1268 4 ARG C NE 3146 C CZ . ARG C 4 ? 0.3800 0.4333 0.6774 0.0857 0.0222 0.1278 4 ARG C CZ 3147 N NH1 . ARG C 4 ? 0.2418 0.2707 0.5303 0.0813 0.0464 0.0961 4 ARG C NH1 3148 N NH2 . ARG C 4 ? 0.3749 0.4296 0.7174 0.1025 0.0287 0.1595 4 ARG C NH2 3149 N N . LEU C 5 ? 0.2652 0.3489 0.2698 0.0141 -0.0595 0.0491 5 LEU C N 3150 C CA . LEU C 5 ? 0.3148 0.3939 0.2910 0.0079 -0.0545 0.0296 5 LEU C CA 3151 C C . LEU C 5 ? 0.2763 0.3667 0.2880 0.0053 -0.0493 0.0179 5 LEU C C 3152 O O . LEU C 5 ? 0.2246 0.3287 0.2777 0.0075 -0.0553 0.0268 5 LEU C O 3153 C CB . LEU C 5 ? 0.4113 0.4798 0.3380 0.0021 -0.0708 0.0295 5 LEU C CB 3154 C CG . LEU C 5 ? 0.4962 0.5753 0.4370 -0.0081 -0.0931 0.0298 5 LEU C CG 3155 C CD1 . LEU C 5 ? 0.5320 0.5973 0.4472 -0.0168 -0.0902 0.0113 5 LEU C CD1 3156 C CD2 . LEU C 5 ? 0.6219 0.6957 0.5419 -0.0107 -0.1131 0.0418 5 LEU C CD2 3157 C C1 . CIR C 6 ? 0.1819 0.2753 0.1810 -0.0061 -0.0394 -0.0108 6 CIR C C1 3158 O O1 . CIR C 6 ? 0.1881 0.2658 0.1435 -0.0075 -0.0398 -0.0141 6 CIR C O1 3159 C C2 . CIR C 6 ? 0.1616 0.2564 0.1789 0.0004 -0.0279 -0.0087 6 CIR C C2 3160 N N2 . CIR C 6 ? 0.2169 0.3035 0.2124 0.0026 -0.0364 0.0024 6 CIR C N2 3161 C C3 . CIR C 6 ? 0.1755 0.2686 0.1817 -0.0006 -0.0105 -0.0210 6 CIR C C3 3162 C C4 . CIR C 6 ? 0.1652 0.2654 0.1880 -0.0018 -0.0005 -0.0302 6 CIR C C4 3163 C C5 . CIR C 6 ? 0.2584 0.3580 0.3178 0.0030 0.0102 -0.0307 6 CIR C C5 3164 N N6 . CIR C 6 ? 0.1946 0.3049 0.2780 0.0047 0.0179 -0.0314 6 CIR C N6 3165 C C7 . CIR C 6 ? 0.2477 0.3742 0.3679 0.0054 0.0048 -0.0165 6 CIR C C7 3166 O O7 . CIR C 6 ? 0.2781 0.4179 0.4266 0.0054 0.0113 -0.0133 6 CIR C O7 3167 N N8 . CIR C 6 ? 0.2140 0.3441 0.3385 0.0043 -0.0178 -0.0023 6 CIR C N8 3168 N N . SER C 7 ? 0.1741 0.2804 0.2052 -0.0110 -0.0477 -0.0077 7 SER C N 3169 C CA . SER C 7 ? 0.1991 0.3000 0.2148 -0.0230 -0.0613 -0.0104 7 SER C CA 3170 C C . SER C 7 ? 0.2541 0.3443 0.2515 -0.0230 -0.0432 -0.0230 7 SER C C 3171 O O . SER C 7 ? 0.1988 0.2991 0.2140 -0.0165 -0.0244 -0.0268 7 SER C O 3172 C CB . SER C 7 ? 0.2014 0.3276 0.2709 -0.0301 -0.0743 0.0010 7 SER C CB 3173 O OG . SER C 7 ? 0.3100 0.4514 0.3998 -0.0300 -0.0948 0.0189 7 SER C OG 3174 N N . SER C 8 ? 0.2595 0.3253 0.2166 -0.0302 -0.0478 -0.0287 8 SER C N 3175 C CA . SER C 8 ? 0.2385 0.2929 0.1845 -0.0299 -0.0311 -0.0356 8 SER C CA 3176 C C . SER C 8 ? 0.2737 0.3328 0.2493 -0.0445 -0.0406 -0.0345 8 SER C C 3177 O O . SER C 8 ? 0.2178 0.2749 0.1968 -0.0593 -0.0649 -0.0315 8 SER C O 3178 C CB . SER C 8 ? 0.2720 0.2899 0.1605 -0.0270 -0.0243 -0.0406 8 SER C CB 3179 O OG . SER C 8 ? 0.2302 0.2492 0.1063 -0.0117 -0.0122 -0.0348 8 SER C OG 3180 N N . VAL C 9 ? 0.1885 0.2570 0.1867 -0.0420 -0.0227 -0.0343 9 VAL C N 3181 C CA . VAL C 9 ? 0.2187 0.3010 0.2606 -0.0542 -0.0264 -0.0284 9 VAL C CA 3182 C C . VAL C 9 ? 0.2398 0.2917 0.2608 -0.0656 -0.0222 -0.0327 9 VAL C C 3183 O O . VAL C 9 ? 0.2795 0.3126 0.2703 -0.0548 -0.0015 -0.0361 9 VAL C O 3184 C CB . VAL C 9 ? 0.2512 0.3628 0.3340 -0.0422 -0.0035 -0.0228 9 VAL C CB 3185 C CG1 . VAL C 9 ? 0.2769 0.4099 0.4160 -0.0519 -0.0034 -0.0111 9 VAL C CG1 3186 C CG2 . VAL C 9 ? 0.2103 0.3377 0.3050 -0.0302 -0.0014 -0.0221 9 VAL C CG2 3187 N N . PRO C 10 ? 0.2335 0.2806 0.2731 -0.0886 -0.0425 -0.0303 10 PRO C N 3188 C CA . PRO C 10 ? 0.2679 0.2799 0.2927 -0.1041 -0.0384 -0.0348 10 PRO C CA 3189 C C . PRO C 10 ? 0.2764 0.3025 0.3328 -0.0938 -0.0088 -0.0260 10 PRO C C 3190 O O . PRO C 10 ? 0.2009 0.2687 0.3119 -0.0901 -0.0027 -0.0139 10 PRO C O 3191 C CB . PRO C 10 ? 0.2796 0.3019 0.3386 -0.1350 -0.0710 -0.0292 10 PRO C CB 3192 C CG . PRO C 10 ? 0.3423 0.3864 0.4005 -0.1351 -0.0972 -0.0259 10 PRO C CG 3193 C CD . PRO C 10 ? 0.2214 0.2927 0.2919 -0.1037 -0.0741 -0.0220 10 PRO C CD 3194 N N . GLY C 11 ? 0.3255 0.3158 0.3469 -0.0875 0.0120 -0.0295 11 GLY C N 3195 C CA . GLY C 11 ? 0.2900 0.2917 0.3357 -0.0783 0.0394 -0.0176 11 GLY C CA 3196 C C . GLY C 11 ? 0.2997 0.2923 0.3819 -0.1014 0.0371 -0.0105 11 GLY C C 3197 O O . GLY C 11 ? 0.3108 0.2925 0.4022 -0.1277 0.0097 -0.0155 11 GLY C O 3198 N N . VAL C 12 ? 0.2653 0.2630 0.3674 -0.0938 0.0641 0.0030 12 VAL C N 3199 C CA . VAL C 12 ? 0.2919 0.2817 0.4347 -0.1154 0.0670 0.0138 12 VAL C CA 3200 C C . VAL C 12 ? 0.3906 0.3120 0.4933 -0.1288 0.0702 0.0052 12 VAL C C 3201 O O . VAL C 12 ? 0.4568 0.3483 0.5174 -0.1080 0.0933 0.0052 12 VAL C O 3202 C CB . VAL C 12 ? 0.3421 0.3609 0.5176 -0.0997 0.1000 0.0346 12 VAL C CB 3203 C CG1 . VAL C 12 ? 0.3294 0.3537 0.5651 -0.1237 0.1021 0.0506 12 VAL C CG1 3204 C CG2 . VAL C 12 ? 0.3045 0.3736 0.4948 -0.0796 0.1073 0.0384 12 VAL C CG2 3205 N N . ARG C 13 ? 0.3961 0.2918 0.5133 -0.1642 0.0479 -0.0001 13 ARG C N 3206 C CA . ARG C 13 ? 0.5078 0.3249 0.5821 -0.1822 0.0519 -0.0121 13 ARG C CA 3207 C C . ARG C 13 ? 0.5303 0.3288 0.6224 -0.1726 0.0893 0.0059 13 ARG C C 3208 O O . ARG C 13 ? 0.5316 0.3722 0.6864 -0.1766 0.0983 0.0272 13 ARG C O 3209 C CB . ARG C 13 ? 0.6774 0.4739 0.7645 -0.2292 0.0141 -0.0218 13 ARG C CB 3210 C CG . ARG C 13 ? 0.8050 0.5871 0.8409 -0.2349 -0.0209 -0.0440 13 ARG C CG 3211 C CD . ARG C 13 ? 0.9754 0.7221 0.9994 -0.2616 -0.0464 -0.0579 13 ARG C CD 3212 N NE . ARG C 13 ? 1.0924 0.8212 1.0542 -0.2640 -0.0720 -0.0780 13 ARG C NE 3213 C CZ . ARG C 13 ? 1.2670 0.9581 1.1943 -0.2868 -0.0925 -0.0940 13 ARG C CZ 3214 N NH1 . ARG C 13 ? 1.3171 0.9829 1.2692 -0.3106 -0.0923 -0.0950 13 ARG C NH1 3215 N NH2 . ARG C 13 ? 1.3425 1.0202 1.2094 -0.2868 -0.1119 -0.1078 13 ARG C NH2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ILE 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 GLU 3 3 3 GLU GLU A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 HIS 5 5 5 HIS HIS A . n A 1 6 VAL 6 6 6 VAL VAL A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 ILE 8 8 8 ILE ILE A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 GLU 11 11 11 GLU GLU A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 TYR 13 13 13 TYR TYR A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 ASN 15 15 15 ASN ASN A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 PHE 22 22 22 PHE PHE A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 PHE 24 24 24 PHE PHE A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 GLU 30 30 30 GLU GLU A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 HIS 33 33 33 HIS HIS A . n A 1 34 VAL 34 34 34 VAL VAL A . n A 1 35 ASP 35 35 35 ASP ASP A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 LYS 38 38 38 LYS LYS A . n A 1 39 LYS 39 39 39 LYS LYS A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 TRP 43 43 43 TRP TRP A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 PHE 48 48 48 PHE PHE A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 GLU 55 55 55 GLU GLU A . n A 1 56 ALA 56 56 56 ALA ALA A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 ASP 66 66 66 ASP ASP A . n A 1 67 LYS 67 67 67 LYS LYS A . n A 1 68 ALA 68 68 68 ALA ALA A . n A 1 69 ASN 69 69 69 ASN ASN A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 ASN 78 78 78 ASN ASN A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 PRO 87 87 87 PRO PRO A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 THR 93 93 93 THR THR A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 GLU 101 101 101 GLU GLU A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 CYS 107 107 107 CYS CYS A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ILE 109 109 109 ILE ILE A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LYS 111 111 111 LYS LYS A . n A 1 112 PHE 112 112 112 PHE PHE A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 TRP 121 121 121 TRP TRP A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 ASN 124 124 124 ASN ASN A . n A 1 125 GLY 125 125 125 GLY GLY A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 PRO 127 127 127 PRO PRO A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 THR 129 129 129 THR THR A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 LEU 138 138 138 LEU LEU A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 ARG 140 140 140 ARG ARG A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 HIS 143 143 143 HIS HIS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 LYS 147 147 147 LYS LYS A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 HIS 149 149 149 HIS HIS A . n A 1 150 TYR 150 150 150 TYR TYR A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 CYS 163 163 163 CYS CYS A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 HIS 167 167 167 HIS HIS A . n A 1 168 TRP 168 168 168 TRP TRP A . n A 1 169 GLY 169 169 169 GLY GLY A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 PRO 173 173 173 PRO PRO A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 HIS 177 177 177 HIS HIS A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 PHE 180 180 180 PHE PHE A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 THR 182 182 ? ? ? A . n A 1 183 SER 183 183 ? ? ? A . n A 1 184 GLY 184 184 ? ? ? A . n A 1 185 ASP 185 185 ? ? ? A . n A 1 186 ASP 186 186 ? ? ? A . n A 1 187 ASP 187 187 ? ? ? A . n A 1 188 ASP 188 188 ? ? ? A . n A 1 189 LYS 189 189 ? ? ? A . n B 2 1 GLY 1 -1 ? ? ? B . n B 2 2 SER 2 0 ? ? ? B . n B 2 3 GLY 3 1 ? ? ? B . n B 2 4 ASP 4 2 2 ASP ASP B . n B 2 5 THR 5 3 3 THR THR B . n B 2 6 ARG 6 4 4 ARG ARG B . n B 2 7 PRO 7 5 5 PRO PRO B . n B 2 8 ARG 8 6 6 ARG ARG B . n B 2 9 PHE 9 7 7 PHE PHE B . n B 2 10 LEU 10 8 8 LEU LEU B . n B 2 11 GLU 11 9 9 GLU GLU B . n B 2 12 GLN 12 10 10 GLN GLN B . n B 2 13 VAL 13 11 11 VAL VAL B . n B 2 14 LYS 14 12 12 LYS LYS B . n B 2 15 HIS 15 13 13 HIS HIS B . n B 2 16 GLU 16 14 14 GLU GLU B . n B 2 17 CYS 17 15 15 CYS CYS B . n B 2 18 HIS 18 16 16 HIS HIS B . n B 2 19 PHE 19 17 17 PHE PHE B . n B 2 20 PHE 20 18 18 PHE PHE B . n B 2 21 ASN 21 19 19 ASN ASN B . n B 2 22 GLY 22 20 20 GLY GLY B . n B 2 23 THR 23 21 21 THR THR B . n B 2 24 GLU 24 22 22 GLU GLU B . n B 2 25 ARG 25 23 23 ARG ARG B . n B 2 26 VAL 26 24 24 VAL VAL B . n B 2 27 ARG 27 25 25 ARG ARG B . n B 2 28 PHE 28 26 26 PHE PHE B . n B 2 29 LEU 29 27 27 LEU LEU B . n B 2 30 ASP 30 28 28 ASP ASP B . n B 2 31 ARG 31 29 29 ARG ARG B . n B 2 32 TYR 32 30 30 TYR TYR B . n B 2 33 PHE 33 31 31 PHE PHE B . n B 2 34 TYR 34 32 32 TYR TYR B . n B 2 35 HIS 35 33 33 HIS HIS B . n B 2 36 GLN 36 34 34 GLN GLN B . n B 2 37 GLU 37 35 35 GLU GLU B . n B 2 38 GLU 38 36 36 GLU GLU B . n B 2 39 TYR 39 37 37 TYR TYR B . n B 2 40 VAL 40 38 38 VAL VAL B . n B 2 41 ARG 41 39 39 ARG ARG B . n B 2 42 PHE 42 40 40 PHE PHE B . n B 2 43 ASP 43 41 41 ASP ASP B . n B 2 44 SER 44 42 42 SER SER B . n B 2 45 ASP 45 43 43 ASP ASP B . n B 2 46 VAL 46 44 44 VAL VAL B . n B 2 47 GLY 47 45 45 GLY GLY B . n B 2 48 GLU 48 46 46 GLU GLU B . n B 2 49 TYR 49 47 47 TYR TYR B . n B 2 50 ARG 50 48 48 ARG ARG B . n B 2 51 ALA 51 49 49 ALA ALA B . n B 2 52 VAL 52 50 50 VAL VAL B . n B 2 53 THR 53 51 51 THR THR B . n B 2 54 GLU 54 52 52 GLU GLU B . n B 2 55 LEU 55 53 53 LEU LEU B . n B 2 56 GLY 56 54 54 GLY GLY B . n B 2 57 ARG 57 55 55 ARG ARG B . n B 2 58 PRO 58 56 56 PRO PRO B . n B 2 59 ASP 59 57 57 ASP ASP B . n B 2 60 ALA 60 58 58 ALA ALA B . n B 2 61 GLU 61 59 59 GLU GLU B . n B 2 62 TYR 62 60 60 TYR TYR B . n B 2 63 TRP 63 61 61 TRP TRP B . n B 2 64 ASN 64 62 62 ASN ASN B . n B 2 65 SER 65 63 63 SER SER B . n B 2 66 GLN 66 64 64 GLN GLN B . n B 2 67 LYS 67 65 65 LYS LYS B . n B 2 68 ASP 68 66 66 ASP ASP B . n B 2 69 ILE 69 67 67 ILE ILE 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 ASP 72 70 70 ASP ASP B . n B 2 73 GLU 73 71 71 GLU GLU 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 ? ? ? 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 A ASN 78 A ASN 78 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 21 B ASN 19 ? 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 # 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)' 7190 ? 1 MORE -28 ? 1 'SSA (A^2)' 18040 ? # _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 435 ? J HOH . 2 1 B HOH 444 ? J 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 41.5777 26.7896 -3.8059 0.1406 0.1710 0.0645 0.0194 -0.0193 0.0185 3.3746 5.0438 0.5149 -0.0488 -1.2281 -0.5853 -0.0559 -0.2423 -0.1412 0.2283 0.0501 -0.0759 -0.0339 0.0855 0.0361 'X-RAY DIFFRACTION' 2 ? refined 40.5605 21.6874 5.3987 0.2096 0.2354 0.1354 0.0266 0.0095 0.0470 4.7103 5.1410 6.4330 1.2582 0.7347 1.3668 0.0877 -0.7142 -0.1404 0.5792 -0.0602 -0.1777 -0.0881 0.1311 0.0316 'X-RAY DIFFRACTION' 3 ? refined 40.9521 12.2789 7.0733 0.3434 0.3608 0.3380 0.0469 0.0345 0.1650 3.7501 7.7783 6.4391 -0.1126 -1.0258 -2.8772 -0.0998 -1.1289 -0.9335 0.7181 0.1234 0.2195 0.4131 -0.3934 0.0270 'X-RAY DIFFRACTION' 4 ? refined 33.7490 32.0489 -1.9237 0.1893 0.1217 0.0652 0.0239 -0.0144 -0.0492 2.3489 1.5285 1.3470 0.4660 -0.8078 -0.3942 -0.0536 -0.0380 0.0344 0.1637 0.0723 0.0489 -0.0147 -0.0494 -0.0021 'X-RAY DIFFRACTION' 5 ? refined 23.6494 34.0700 9.2845 0.2508 0.2286 0.1246 0.0406 0.0366 -0.0070 3.2636 1.1328 0.6255 -1.4814 -1.0916 0.8379 -0.1227 -0.6497 -0.1096 0.4511 0.0433 0.1306 -0.0646 0.2983 0.0602 'X-RAY DIFFRACTION' 6 ? refined 29.8932 27.5921 -1.0285 0.1488 0.1165 0.1015 0.0093 -0.0160 -0.0188 5.2594 1.9784 6.3705 1.4442 -4.8670 -2.8478 -0.0263 -0.2329 -0.0943 0.1892 -0.0341 0.0138 0.0868 0.1043 0.0940 'X-RAY DIFFRACTION' 7 ? refined 14.1695 31.1769 9.9421 0.2849 0.2480 0.2583 0.0661 0.1320 -0.0290 1.3791 2.0256 3.5417 -0.5736 -0.6363 -0.4862 0.1681 -0.2730 0.3293 0.6597 0.1393 0.7766 -0.2361 -0.2009 -0.2429 'X-RAY DIFFRACTION' 8 ? refined 17.4611 36.5041 1.5835 0.2303 0.1840 0.2171 0.0588 -0.0232 -0.0073 3.5259 7.1221 5.6726 1.8404 -4.1625 -4.3535 -0.0653 0.4559 1.1254 0.0236 0.7339 1.3437 -0.0101 -0.5495 -0.6447 'X-RAY DIFFRACTION' 9 ? refined 47.3529 28.5769 -15.0912 0.1321 0.1400 0.1000 0.0013 -0.0438 -0.0169 2.0054 3.6516 1.5896 -0.5205 -0.8640 0.6330 -0.0202 0.0645 -0.0350 -0.1658 -0.0518 0.0056 -0.0820 0.0218 0.0678 'X-RAY DIFFRACTION' 10 ? refined 28.9338 13.8255 -5.8415 0.1822 0.1220 0.1839 0.0241 0.0435 -0.0215 4.9802 0.7073 0.7124 1.1242 -0.3839 -0.5074 -0.1201 -0.2944 -0.3891 0.0718 0.0547 -0.0017 -0.0093 -0.0875 0.0852 'X-RAY DIFFRACTION' 11 ? refined 11.6273 9.5437 -8.8909 0.1869 0.1759 0.3043 -0.0082 0.0623 0.0498 2.8300 0.8044 1.3105 -0.7188 1.1108 -0.1812 0.0012 -0.0274 -0.6407 -0.0731 0.0941 0.1560 0.0953 -0.1426 -0.0909 'X-RAY DIFFRACTION' 12 ? refined 54.0037 24.9355 -5.6114 0.1513 0.2471 0.1583 -0.0272 -0.0630 -0.0134 4.3533 5.9618 4.5975 0.4517 -1.7859 -3.2269 0.0516 -0.3605 -0.2286 0.5916 -0.2043 -0.9036 -0.3281 0.4135 0.1918 # 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 45 ) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 46 through 55 ) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 56 through 112 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 113 through 133 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 134 through 153 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 154 through 166 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 167 through 181 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 2 through 64 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 65 through 122 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 123 through 190 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1 through 13 ) ; # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal Blu-Ice 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.8.1_1168)' ? 3 MOSFLM 'data reduction' . ? 4 SCALA 'data scaling' . ? 5 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS B 33 ? ? 59.60 -114.17 2 1 THR B 90 ? ? -121.94 -71.30 3 1 GLN B 110 ? ? -66.17 -175.61 4 1 ASN B 113 ? ? -142.97 24.49 5 1 PRO B 124 ? ? -77.17 -166.20 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 B LEU 109 ? CG ? B LEU 111 CG 2 1 Y 1 B LEU 109 ? CD1 ? B LEU 111 CD1 3 1 Y 1 B LEU 109 ? CD2 ? B LEU 111 CD2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ILE 1 ? A ILE 1 2 1 Y 1 A LYS 2 ? A LYS 2 3 1 Y 1 A THR 182 ? A THR 182 4 1 Y 1 A SER 183 ? A SER 183 5 1 Y 1 A GLY 184 ? A GLY 184 6 1 Y 1 A ASP 185 ? A ASP 185 7 1 Y 1 A ASP 186 ? A ASP 186 8 1 Y 1 A ASP 187 ? A ASP 187 9 1 Y 1 A ASP 188 ? A ASP 188 10 1 Y 1 A LYS 189 ? A LYS 189 11 1 Y 1 B GLY -1 ? B GLY 1 12 1 Y 1 B SER 0 ? B SER 2 13 1 Y 1 B GLY 1 ? B GLY 3 14 1 Y 1 B THR 191 ? B THR 193 15 1 Y 1 B GLY 192 ? B GLY 194 16 1 Y 1 B GLY 193 ? B GLY 195 17 1 Y 1 B ASP 194 ? B ASP 196 18 1 Y 1 B ASP 195 ? B ASP 197 19 1 Y 1 B ASP 196 ? B ASP 198 20 1 Y 1 B ASP 197 ? B ASP 199 21 1 Y 1 B LYS 198 ? B LYS 200 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 1,2-ETHANEDIOL EDO 6 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 4 NAG 1 500 500 NAG NAG A . E 4 NAG 1 501 501 NAG NAG A . F 4 NAG 2 502 502 NAG NAG A . G 4 NAG 1 201 500 NAG NAG B . H 5 EDO 1 202 1 EDO EDO B . I 6 HOH 1 601 1 HOH HOH A . I 6 HOH 2 602 2 HOH HOH A . I 6 HOH 3 603 3 HOH HOH A . I 6 HOH 4 604 5 HOH HOH A . I 6 HOH 5 605 6 HOH HOH A . I 6 HOH 6 606 7 HOH HOH A . I 6 HOH 7 607 10 HOH HOH A . I 6 HOH 8 608 11 HOH HOH A . I 6 HOH 9 609 16 HOH HOH A . I 6 HOH 10 610 19 HOH HOH A . I 6 HOH 11 611 20 HOH HOH A . I 6 HOH 12 612 24 HOH HOH A . I 6 HOH 13 613 29 HOH HOH A . I 6 HOH 14 614 31 HOH HOH A . I 6 HOH 15 615 32 HOH HOH A . I 6 HOH 16 616 34 HOH HOH A . I 6 HOH 17 617 35 HOH HOH A . I 6 HOH 18 618 36 HOH HOH A . I 6 HOH 19 619 37 HOH HOH A . I 6 HOH 20 620 38 HOH HOH A . I 6 HOH 21 621 39 HOH HOH A . I 6 HOH 22 622 42 HOH HOH A . I 6 HOH 23 623 44 HOH HOH A . I 6 HOH 24 624 46 HOH HOH A . I 6 HOH 25 625 49 HOH HOH A . I 6 HOH 26 626 50 HOH HOH A . I 6 HOH 27 627 52 HOH HOH A . I 6 HOH 28 628 54 HOH HOH A . I 6 HOH 29 629 56 HOH HOH A . I 6 HOH 30 630 61 HOH HOH A . I 6 HOH 31 631 64 HOH HOH A . I 6 HOH 32 632 65 HOH HOH A . I 6 HOH 33 633 66 HOH HOH A . I 6 HOH 34 634 67 HOH HOH A . I 6 HOH 35 635 68 HOH HOH A . I 6 HOH 36 636 70 HOH HOH A . I 6 HOH 37 637 71 HOH HOH A . I 6 HOH 38 638 72 HOH HOH A . I 6 HOH 39 639 73 HOH HOH A . I 6 HOH 40 640 74 HOH HOH A . I 6 HOH 41 641 75 HOH HOH A . I 6 HOH 42 642 78 HOH HOH A . I 6 HOH 43 643 81 HOH HOH A . I 6 HOH 44 644 82 HOH HOH A . I 6 HOH 45 645 88 HOH HOH A . I 6 HOH 46 646 92 HOH HOH A . I 6 HOH 47 647 93 HOH HOH A . I 6 HOH 48 648 96 HOH HOH A . I 6 HOH 49 649 105 HOH HOH A . I 6 HOH 50 650 109 HOH HOH A . I 6 HOH 51 651 112 HOH HOH A . I 6 HOH 52 652 113 HOH HOH A . I 6 HOH 53 653 116 HOH HOH A . I 6 HOH 54 654 117 HOH HOH A . I 6 HOH 55 655 118 HOH HOH A . I 6 HOH 56 656 120 HOH HOH A . I 6 HOH 57 657 122 HOH HOH A . I 6 HOH 58 658 124 HOH HOH A . I 6 HOH 59 659 127 HOH HOH A . I 6 HOH 60 660 130 HOH HOH A . I 6 HOH 61 661 131 HOH HOH A . I 6 HOH 62 662 132 HOH HOH A . I 6 HOH 63 663 135 HOH HOH A . I 6 HOH 64 664 139 HOH HOH A . I 6 HOH 65 665 140 HOH HOH A . I 6 HOH 66 666 142 HOH HOH A . I 6 HOH 67 667 146 HOH HOH A . I 6 HOH 68 668 148 HOH HOH A . I 6 HOH 69 669 150 HOH HOH A . I 6 HOH 70 670 151 HOH HOH A . I 6 HOH 71 671 152 HOH HOH A . I 6 HOH 72 672 155 HOH HOH A . I 6 HOH 73 673 156 HOH HOH A . I 6 HOH 74 674 159 HOH HOH A . I 6 HOH 75 675 160 HOH HOH A . I 6 HOH 76 676 162 HOH HOH A . I 6 HOH 77 677 163 HOH HOH A . I 6 HOH 78 678 164 HOH HOH A . I 6 HOH 79 679 165 HOH HOH A . I 6 HOH 80 680 169 HOH HOH A . I 6 HOH 81 681 171 HOH HOH A . I 6 HOH 82 682 172 HOH HOH A . I 6 HOH 83 683 175 HOH HOH A . I 6 HOH 84 684 176 HOH HOH A . I 6 HOH 85 685 177 HOH HOH A . I 6 HOH 86 686 181 HOH HOH A . I 6 HOH 87 687 182 HOH HOH A . I 6 HOH 88 688 185 HOH HOH A . I 6 HOH 89 689 186 HOH HOH A . I 6 HOH 90 690 187 HOH HOH A . I 6 HOH 91 691 188 HOH HOH A . I 6 HOH 92 692 189 HOH HOH A . I 6 HOH 93 693 190 HOH HOH A . I 6 HOH 94 694 194 HOH HOH A . I 6 HOH 95 695 195 HOH HOH A . I 6 HOH 96 696 197 HOH HOH A . I 6 HOH 97 697 200 HOH HOH A . I 6 HOH 98 698 202 HOH HOH A . I 6 HOH 99 699 203 HOH HOH A . I 6 HOH 100 700 204 HOH HOH A . I 6 HOH 101 701 208 HOH HOH A . I 6 HOH 102 702 210 HOH HOH A . I 6 HOH 103 703 211 HOH HOH A . I 6 HOH 104 704 212 HOH HOH A . I 6 HOH 105 705 214 HOH HOH A . I 6 HOH 106 706 218 HOH HOH A . I 6 HOH 107 707 221 HOH HOH A . I 6 HOH 108 708 224 HOH HOH A . I 6 HOH 109 709 226 HOH HOH A . I 6 HOH 110 710 230 HOH HOH A . I 6 HOH 111 711 232 HOH HOH A . I 6 HOH 112 712 234 HOH HOH A . I 6 HOH 113 713 237 HOH HOH A . I 6 HOH 114 714 239 HOH HOH A . I 6 HOH 115 715 242 HOH HOH A . I 6 HOH 116 716 243 HOH HOH A . I 6 HOH 117 717 244 HOH HOH A . I 6 HOH 118 718 247 HOH HOH A . I 6 HOH 119 719 249 HOH HOH A . I 6 HOH 120 720 250 HOH HOH A . I 6 HOH 121 721 251 HOH HOH A . I 6 HOH 122 722 254 HOH HOH A . I 6 HOH 123 723 255 HOH HOH A . I 6 HOH 124 724 256 HOH HOH A . I 6 HOH 125 725 259 HOH HOH A . I 6 HOH 126 726 260 HOH HOH A . I 6 HOH 127 727 261 HOH HOH A . I 6 HOH 128 728 265 HOH HOH A . I 6 HOH 129 729 266 HOH HOH A . I 6 HOH 130 730 270 HOH HOH A . I 6 HOH 131 731 274 HOH HOH A . I 6 HOH 132 732 275 HOH HOH A . I 6 HOH 133 733 276 HOH HOH A . I 6 HOH 134 734 278 HOH HOH A . I 6 HOH 135 735 280 HOH HOH A . I 6 HOH 136 736 282 HOH HOH A . I 6 HOH 137 737 283 HOH HOH A . I 6 HOH 138 738 285 HOH HOH A . I 6 HOH 139 739 286 HOH HOH A . I 6 HOH 140 740 288 HOH HOH A . I 6 HOH 141 741 289 HOH HOH A . I 6 HOH 142 742 299 HOH HOH A . I 6 HOH 143 743 305 HOH HOH A . I 6 HOH 144 744 306 HOH HOH A . I 6 HOH 145 745 311 HOH HOH A . I 6 HOH 146 746 312 HOH HOH A . I 6 HOH 147 747 313 HOH HOH A . I 6 HOH 148 748 317 HOH HOH A . I 6 HOH 149 749 319 HOH HOH A . I 6 HOH 150 750 321 HOH HOH A . I 6 HOH 151 751 322 HOH HOH A . I 6 HOH 152 752 327 HOH HOH A . I 6 HOH 153 753 333 HOH HOH A . I 6 HOH 154 754 335 HOH HOH A . I 6 HOH 155 755 337 HOH HOH A . I 6 HOH 156 756 338 HOH HOH A . I 6 HOH 157 757 339 HOH HOH A . I 6 HOH 158 758 341 HOH HOH A . I 6 HOH 159 759 343 HOH HOH A . I 6 HOH 160 760 344 HOH HOH A . I 6 HOH 161 761 345 HOH HOH A . I 6 HOH 162 762 346 HOH HOH A . I 6 HOH 163 763 348 HOH HOH A . I 6 HOH 164 764 350 HOH HOH A . I 6 HOH 165 765 352 HOH HOH A . I 6 HOH 166 766 355 HOH HOH A . I 6 HOH 167 767 358 HOH HOH A . I 6 HOH 168 768 359 HOH HOH A . I 6 HOH 169 769 361 HOH HOH A . I 6 HOH 170 770 363 HOH HOH A . I 6 HOH 171 771 364 HOH HOH A . I 6 HOH 172 772 366 HOH HOH A . I 6 HOH 173 773 368 HOH HOH A . I 6 HOH 174 774 369 HOH HOH A . I 6 HOH 175 775 372 HOH HOH A . I 6 HOH 176 776 375 HOH HOH A . I 6 HOH 177 777 376 HOH HOH A . I 6 HOH 178 778 377 HOH HOH A . I 6 HOH 179 779 378 HOH HOH A . I 6 HOH 180 780 381 HOH HOH A . I 6 HOH 181 781 382 HOH HOH A . I 6 HOH 182 782 383 HOH HOH A . I 6 HOH 183 783 384 HOH HOH A . I 6 HOH 184 784 387 HOH HOH A . I 6 HOH 185 785 389 HOH HOH A . I 6 HOH 186 786 390 HOH HOH A . I 6 HOH 187 787 391 HOH HOH A . I 6 HOH 188 788 394 HOH HOH A . I 6 HOH 189 789 400 HOH HOH A . I 6 HOH 190 790 405 HOH HOH A . I 6 HOH 191 791 406 HOH HOH A . I 6 HOH 192 792 407 HOH HOH A . I 6 HOH 193 793 408 HOH HOH A . I 6 HOH 194 794 409 HOH HOH A . I 6 HOH 195 795 410 HOH HOH A . I 6 HOH 196 796 411 HOH HOH A . I 6 HOH 197 797 415 HOH HOH A . I 6 HOH 198 798 416 HOH HOH A . I 6 HOH 199 799 419 HOH HOH A . J 6 HOH 1 301 4 HOH HOH B . J 6 HOH 2 302 8 HOH HOH B . J 6 HOH 3 303 9 HOH HOH B . J 6 HOH 4 304 12 HOH HOH B . J 6 HOH 5 305 13 HOH HOH B . J 6 HOH 6 306 14 HOH HOH B . J 6 HOH 7 307 15 HOH HOH B . J 6 HOH 8 308 17 HOH HOH B . J 6 HOH 9 309 18 HOH HOH B . J 6 HOH 10 310 21 HOH HOH B . J 6 HOH 11 311 22 HOH HOH B . J 6 HOH 12 312 23 HOH HOH B . J 6 HOH 13 313 25 HOH HOH B . J 6 HOH 14 314 26 HOH HOH B . J 6 HOH 15 315 27 HOH HOH B . J 6 HOH 16 316 28 HOH HOH B . J 6 HOH 17 317 30 HOH HOH B . J 6 HOH 18 318 33 HOH HOH B . J 6 HOH 19 319 40 HOH HOH B . J 6 HOH 20 320 41 HOH HOH B . J 6 HOH 21 321 43 HOH HOH B . J 6 HOH 22 322 45 HOH HOH B . J 6 HOH 23 323 47 HOH HOH B . J 6 HOH 24 324 48 HOH HOH B . J 6 HOH 25 325 51 HOH HOH B . J 6 HOH 26 326 53 HOH HOH B . J 6 HOH 27 327 55 HOH HOH B . J 6 HOH 28 328 57 HOH HOH B . J 6 HOH 29 329 58 HOH HOH B . J 6 HOH 30 330 59 HOH HOH B . J 6 HOH 31 331 60 HOH HOH B . J 6 HOH 32 332 62 HOH HOH B . J 6 HOH 33 333 63 HOH HOH B . J 6 HOH 34 334 69 HOH HOH B . J 6 HOH 35 335 76 HOH HOH B . J 6 HOH 36 336 77 HOH HOH B . J 6 HOH 37 337 79 HOH HOH B . J 6 HOH 38 338 83 HOH HOH B . J 6 HOH 39 339 84 HOH HOH B . J 6 HOH 40 340 85 HOH HOH B . J 6 HOH 41 341 86 HOH HOH B . J 6 HOH 42 342 87 HOH HOH B . J 6 HOH 43 343 89 HOH HOH B . J 6 HOH 44 344 90 HOH HOH B . J 6 HOH 45 345 91 HOH HOH B . J 6 HOH 46 346 94 HOH HOH B . J 6 HOH 47 347 95 HOH HOH B . J 6 HOH 48 348 97 HOH HOH B . J 6 HOH 49 349 98 HOH HOH B . J 6 HOH 50 350 99 HOH HOH B . J 6 HOH 51 351 100 HOH HOH B . J 6 HOH 52 352 101 HOH HOH B . J 6 HOH 53 353 102 HOH HOH B . J 6 HOH 54 354 103 HOH HOH B . J 6 HOH 55 355 104 HOH HOH B . J 6 HOH 56 356 106 HOH HOH B . J 6 HOH 57 357 108 HOH HOH B . J 6 HOH 58 358 110 HOH HOH B . J 6 HOH 59 359 111 HOH HOH B . J 6 HOH 60 360 114 HOH HOH B . J 6 HOH 61 361 115 HOH HOH B . J 6 HOH 62 362 119 HOH HOH B . J 6 HOH 63 363 121 HOH HOH B . J 6 HOH 64 364 123 HOH HOH B . J 6 HOH 65 365 125 HOH HOH B . J 6 HOH 66 366 126 HOH HOH B . J 6 HOH 67 367 128 HOH HOH B . J 6 HOH 68 368 129 HOH HOH B . J 6 HOH 69 369 134 HOH HOH B . J 6 HOH 70 370 136 HOH HOH B . J 6 HOH 71 371 137 HOH HOH B . J 6 HOH 72 372 138 HOH HOH B . J 6 HOH 73 373 141 HOH HOH B . J 6 HOH 74 374 143 HOH HOH B . J 6 HOH 75 375 144 HOH HOH B . J 6 HOH 76 376 145 HOH HOH B . J 6 HOH 77 377 147 HOH HOH B . J 6 HOH 78 378 149 HOH HOH B . J 6 HOH 79 379 153 HOH HOH B . J 6 HOH 80 380 154 HOH HOH B . J 6 HOH 81 381 158 HOH HOH B . J 6 HOH 82 382 161 HOH HOH B . J 6 HOH 83 383 166 HOH HOH B . J 6 HOH 84 384 167 HOH HOH B . J 6 HOH 85 385 168 HOH HOH B . J 6 HOH 86 386 170 HOH HOH B . J 6 HOH 87 387 173 HOH HOH B . J 6 HOH 88 388 174 HOH HOH B . J 6 HOH 89 389 178 HOH HOH B . J 6 HOH 90 390 179 HOH HOH B . J 6 HOH 91 391 180 HOH HOH B . J 6 HOH 92 392 183 HOH HOH B . J 6 HOH 93 393 184 HOH HOH B . J 6 HOH 94 394 191 HOH HOH B . J 6 HOH 95 395 192 HOH HOH B . J 6 HOH 96 396 193 HOH HOH B . J 6 HOH 97 397 196 HOH HOH B . J 6 HOH 98 398 198 HOH HOH B . J 6 HOH 99 399 199 HOH HOH B . J 6 HOH 100 400 201 HOH HOH B . J 6 HOH 101 401 205 HOH HOH B . J 6 HOH 102 402 206 HOH HOH B . J 6 HOH 103 403 207 HOH HOH B . J 6 HOH 104 404 209 HOH HOH B . J 6 HOH 105 405 213 HOH HOH B . J 6 HOH 106 406 215 HOH HOH B . J 6 HOH 107 407 216 HOH HOH B . J 6 HOH 108 408 217 HOH HOH B . J 6 HOH 109 409 220 HOH HOH B . J 6 HOH 110 410 222 HOH HOH B . J 6 HOH 111 411 225 HOH HOH B . J 6 HOH 112 412 227 HOH HOH B . J 6 HOH 113 413 228 HOH HOH B . J 6 HOH 114 414 229 HOH HOH B . J 6 HOH 115 415 231 HOH HOH B . J 6 HOH 116 416 233 HOH HOH B . J 6 HOH 117 417 235 HOH HOH B . J 6 HOH 118 418 236 HOH HOH B . J 6 HOH 119 419 238 HOH HOH B . J 6 HOH 120 420 240 HOH HOH B . J 6 HOH 121 421 241 HOH HOH B . J 6 HOH 122 422 246 HOH HOH B . J 6 HOH 123 423 248 HOH HOH B . J 6 HOH 124 424 252 HOH HOH B . J 6 HOH 125 425 253 HOH HOH B . J 6 HOH 126 426 258 HOH HOH B . J 6 HOH 127 427 262 HOH HOH B . J 6 HOH 128 428 263 HOH HOH B . J 6 HOH 129 429 264 HOH HOH B . J 6 HOH 130 430 267 HOH HOH B . J 6 HOH 131 431 268 HOH HOH B . J 6 HOH 132 432 269 HOH HOH B . J 6 HOH 133 433 271 HOH HOH B . J 6 HOH 134 434 272 HOH HOH B . J 6 HOH 135 435 273 HOH HOH B . J 6 HOH 136 436 277 HOH HOH B . J 6 HOH 137 437 279 HOH HOH B . J 6 HOH 138 438 284 HOH HOH B . J 6 HOH 139 439 287 HOH HOH B . J 6 HOH 140 440 290 HOH HOH B . J 6 HOH 141 441 291 HOH HOH B . J 6 HOH 142 442 292 HOH HOH B . J 6 HOH 143 443 294 HOH HOH B . J 6 HOH 144 444 295 HOH HOH B . J 6 HOH 145 445 296 HOH HOH B . J 6 HOH 146 446 298 HOH HOH B . J 6 HOH 147 447 301 HOH HOH B . J 6 HOH 148 448 302 HOH HOH B . J 6 HOH 149 449 307 HOH HOH B . J 6 HOH 150 450 309 HOH HOH B . J 6 HOH 151 451 310 HOH HOH B . J 6 HOH 152 452 314 HOH HOH B . J 6 HOH 153 453 316 HOH HOH B . J 6 HOH 154 454 320 HOH HOH B . J 6 HOH 155 455 323 HOH HOH B . J 6 HOH 156 456 324 HOH HOH B . J 6 HOH 157 457 325 HOH HOH B . J 6 HOH 158 458 328 HOH HOH B . J 6 HOH 159 459 329 HOH HOH B . J 6 HOH 160 460 330 HOH HOH B . J 6 HOH 161 461 331 HOH HOH B . J 6 HOH 162 462 332 HOH HOH B . J 6 HOH 163 463 334 HOH HOH B . J 6 HOH 164 464 336 HOH HOH B . J 6 HOH 165 465 340 HOH HOH B . J 6 HOH 166 466 347 HOH HOH B . J 6 HOH 167 467 351 HOH HOH B . J 6 HOH 168 468 353 HOH HOH B . J 6 HOH 169 469 357 HOH HOH B . J 6 HOH 170 470 360 HOH HOH B . J 6 HOH 171 471 362 HOH HOH B . J 6 HOH 172 472 367 HOH HOH B . J 6 HOH 173 473 371 HOH HOH B . J 6 HOH 174 474 373 HOH HOH B . J 6 HOH 175 475 379 HOH HOH B . J 6 HOH 176 476 385 HOH HOH B . J 6 HOH 177 477 386 HOH HOH B . J 6 HOH 178 478 393 HOH HOH B . J 6 HOH 179 479 395 HOH HOH B . J 6 HOH 180 480 396 HOH HOH B . J 6 HOH 181 481 398 HOH HOH B . J 6 HOH 182 482 399 HOH HOH B . J 6 HOH 183 483 401 HOH HOH B . J 6 HOH 184 484 402 HOH HOH B . J 6 HOH 185 485 403 HOH HOH B . J 6 HOH 186 486 413 HOH HOH B . J 6 HOH 187 487 414 HOH HOH B . J 6 HOH 188 488 417 HOH HOH B . J 6 HOH 189 489 418 HOH HOH B . K 6 HOH 1 101 133 HOH HOH C . K 6 HOH 2 102 157 HOH HOH C . K 6 HOH 3 103 245 HOH HOH C . K 6 HOH 4 104 281 HOH HOH C . K 6 HOH 5 105 297 HOH HOH C . K 6 HOH 6 106 308 HOH HOH C . K 6 HOH 7 107 318 HOH HOH C . K 6 HOH 8 108 349 HOH HOH C . K 6 HOH 9 109 354 HOH HOH C . #