{"resolution": "", "ligand_mw": "696.66", "secondary_structure": "MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH#CCCCCCCCCEEEEEEEEESSCEEEESCEECGGGCSCCCCSCCCSCEEEEEEEEESSCEEEESCEEESSSSSSCCCCCCC&MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH#CCCCCCCCCEEEEEEEEESSCEEEESCEEEGGGTTSCCCSCCCCCEEEEEEEEESSCEEEESCEECSSCSSSCCCCCCC&MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH#CCCCCCCCCEEEEEEEEESSCEEEESCEECTTCCCCCCCCCCCCCEEEEEEEEESSCEEEESCEEESSCSSCCSSCCCC&MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH#CCCCCCCCCCEEEEEEEESSCEEEESCEEETTCCSSSCCCCSCSCEEEEEEEEESSCEEEESCEESSSSCSSCSCSCCC&MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH#CCCCCCCCCEEEEEEEEESSCEEEESCEECTTCCSSCSCCCCCCCEEEEEEEEESSCEEEESCCCCSSSSSCCCCCCCC", "inchi": "InChI=1S/C32H24N6O6S2.2Na/c33-31-25-7-3-1-5-23(25)29(45(39,40)41)17-27(31)37-35-21-13-9-19(10-14-21)20-11-15-22(16-12-20)36-38-28-18-30(46(42,43)44)24-6-2-4-8-26(24)32(28)34;;/h1-18H,33-34H2,(H,39,40,41)(H,42,43,44);;/q;2*+1/p-2/b37-35+,38-36+;;", "method": "SOLID-STATE NMR", "ec_number": "", "uniprot_ac": "Q03689", "remarks": "HADDOCK calculated model of Congo red bound to the HET-s amyloid", "description": "Congo red, was studied in complex with an amyloid. The binding interface between Congo red and amyloid fibrils formed by the prion domain of the fungal HET?s protein was characterized at atomic resolution. The dye binds highly site?specifically by interacting with residues flanking a groove in the vicinity of a Beta?arc. The three?dimensional (3D) structure of the fibril is strongly conserved upon the binding of Congo red.", "type": "Fibril", "ligand_smiles": "c1cc2c(cc(c(c2cc1)N)/N=N/c3ccc(cc3)c4ccc(cc4)/N=N/c5c(c6c(c(c5)S(=O)(=O)[O-][Na+])cccc6)N)S(=O)(=O)[O-][Na+]", "chain_id": "B", "species": "Podospora anserina", "keyword": "Small s protein", "ligstr": "CGO:B:C32 H22 N6 Na2 O6 S2:696.66:sodium 3,3'-(1E,1'E)-biphenyl-4,4'-diylbis(diazene-2,1-diyl)bis(4-aminonaphthalene-1-sulfonate):c1cc2c(cc(c(c2cc1)N)/N=N/c3ccc(cc3)c4ccc(cc4)/N=N/c5c(c6c(c(c5)S(=O)(=O)[O-][Na+])cccc6)N)S(=O)(=O)[O-][Na+]:InChI=1S/C32H24N6O6S2.2Na/c33-31-25-7-3-1-5-23(25)29(45(39,40)41)17-27(31)37-35-21-13-9-19(10-14-21)20-11-15-22(16-12-20)36-38-28-18-30(46(42,43)44)24-6-2-4-8-26(24)32(28)34;;/h1-18H,33-34H2,(H,39,40,41)(H,42,43,44);;/q;2*+1/p-2/b37-35+,38-36+;;:IQFVPQOLBLOTPF-HKXUKFGYSA-L", "pmid": "21591034", "mutation_s_field": "No", "author": "Schutz, A.K., Soragni, A., Hornemann, S., Aguzzi, A., Ernst, M., Bockmann, A., Meier, B.H.", "pdb_id": "2LBU", "amyloid_non_amyloid": "Amyloid", "inchi_key": "IQFVPQOLBLOTPF-HKXUKFGYSA-L", "ligand_name": "sodium 3,3'-(1E,1'E)-biphenyl-4,4'-diylbis(diazene-2,1-diyl)bis(4-aminonaphthalene-1-sulfonate)", "ligand_formula": "C32 H22 N6 Na2 O6 S2", "ligand_id": "CGO", "r_value_free": "", "protein_name": "Heterokaryon incompatibility protein s", "gene_names": "het-s, small s", "global_stoichiometry": "Homo 5-mer - A5 ", "alternative_name": "Small s protein, Vegetative incompatibility protein s", "peptide_protein_sequence": "chain-ID A: MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH; chain-ID B: MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH; chain-ID C: MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH; chain-ID D: MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH; chain-ID E: MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDNHHHHHH", "pdb_classification": "PROTEIN FIBRIL", "reference": "Angew Chem Int Ed Engl. 2011 Jun 20;50(26):5956-60.", "length": "79", "entry": "S-0119"}