{"global_stoichiometry": "Monomer - A ", "ligstr": "", "uniprot_ac": "P52750", "inchi": "", "reference": "J Mol Biol. 2013 Jan 23;425(2):244-56.", "author": "Morris, V.K., Kwan, A.H., Sunde, M.", "type": "Protein", "ligand_id": "", "species": "Aspergillus nidulans", "method": "SOLUTION NMR", "keyword": "Spore-wall fungal hydrophobin dewA", "gene_names": "dewA, AN8006", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "SLPASAAKNAKLATSAAFAKQAEGTTCNVGSIACCNSPAETNNDSLLSGLLGAGLLNGLSGNTGSACAKASLIDQLGLLALVDHTEEGPVCKNIVACCPEGTTNCVAVDNAGAGTKAE#CCTTSSCCCCSSTTCTHHHHHHHHSCCCGGGEEEECCHHHHTSSTTHHHHSCTTSCCEETTEEEEEEEEHHHHTTTCCTTTEEEETTEEEESSEEEECCSSSSCBEESCSSSCSCCCC", "amyloid_non_amyloid": "Amyloid", "length": "118", "remarks": "Solution structure of the class I hydrophobin DewA", "protein_name": "Spore-wall fungal hydrophobin dewA", "peptide_protein_sequence": "chain-ID A: SLPASAAKNAKLATSAAFAKQAEGTTCNVGSIACCNSPAETNNDSLLSGLLGAGLLNGLSGNTGSACAKASLIDQLGLLALVDHTEEGPVCKNIVACCPEGTTNCVAVDNAGAGTKAE", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2LSH", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "The hydrophobin DewA from the fungus Aspergillus nidulans is a highly surface-active protein that spontaneously self-assembles into amphipathic monolayers at hydrophobic:hydrophilic interfaces. These monolayers are composed of fibrils that are a form of functional amyloid. In the solution NMR structure of DewA, the pattern of four disulfide bonds that is a defining feature of hydrophobins is conserved, the arrangement and composition of secondary-structure elements in DewA are quite different to what has been observed in other hydrophobin structures. In addition, DewA populates two conformations in solution, both of which are assembly competent. One conformer forms a dimer at high concentrations, but this dimer is off-pathway to fibril formation and may represent an assembly control mechanism. These data highlight the structural differences between fibril-forming hydrophobins and those that form amorphous monolayers.", "resolution": "", "pmid": "23137797", "entry": "S-0129"}