{"global_stoichiometry": "Homo 20-mer - A20", "ligstr": "ACT:A:C2 H3 O2 -1:59.04:ACETATE ION:CC(=O)[O-]:InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1:QTBSBXVTEAMEQO-UHFFFAOYSA-M;MPD:A:C6 H14 O2:118.17:(4S)-2-METHYL-2,4-PENTANEDIOL:C[C@@H](CC(C)(C)O)O:InChI=1S/C6H14O2/c1-5(7)4-6(2,3)8/h5,7-8H,4H2,1-3H3/t5-/m0/s1:SVTBMSDMJJWYQN-YFKPBYRVSA-N;MSE:A:C5 H11 N O2 Se:196.11:SELENOMETHIONINE:C[Se]CC[C@@H](C(=O)O)N:InChI=1S/C5H11NO2Se/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1:RJFAYQIBOAGBLC-BYPYZUCNSA-N", "uniprot_ac": "P0C805", "inchi": "InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1%%InChI=1S/C6H14O2/c1-5(7)4-6(2,3)8/h5,7-8H,4H2,1-3H3/t5-/m0/s1%%InChI=1S/C5H11NO2Se/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1", "reference": "Science. 2017 Feb 24;355(6327):831-833.", "author": "Tayeb-Fligelman, E., Tabachnikov, O., Moshe, A., Goldshmidt-Tran, O., Sawaya, M.R., Coquelle, N., Colletier, J.P., Landau, M.", "type": "Fibril", "ligand_id": "ACT%%MPD%%MSE", "species": "Staphylococcus aureus", "method": "X-RAY DIFFRACTION", "keyword": "Psm alpha-3", "gene_names": "psmA3, SAOUHSC_00411.2", "chain_id": "A%%A%%A", "ligand_mw": "59.04%%118.17%%196.11", "inchi_key": "QTBSBXVTEAMEQO-UHFFFAOYSA-M%%SVTBMSDMJJWYQN-YFKPBYRVSA-N%%RJFAYQIBOAGBLC-BYPYZUCNSA-N", "secondary_structure": "MEFVAKLFKFFKDLLGKFLGNN#CCHHHHHHHHHHHHHHHHHTCC", "amyloid_non_amyloid": "Amyloid", "length": "22", "remarks": "Crystal Structure of the Virulent PSM-alpha3 Peptide Forming a Cross-alpha amyloid-like Fibril", "protein_name": "Phenol-soluble modulin alpha 3 peptide", "peptide_protein_sequence": "chain-ID A: MEFVAKLFKFFKDLLGKFLGNN", "ligand_name": "ACETATE ION%%(4S)-2-METHYL-2,4-PENTANEDIOL%%SELENOMETHIONINE", "ligand_smiles": "CC(=O)[O-]%%C[C@@H](CC(C)(C)O)O%%C[Se]CC[C@@H](C(=O)O)N", "pdb_id": "5I55", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "C2 H3 O2 -1%%C6 H14 O2%%C5 H11 N O2 Se", "r_value_free": "0.184", "alternative_name": "", "description": "\"The crystal structure of full-length PSMAlpha3 revealed a distinctive \"\"cross-Alpha\"\" amyloid-like architecture, in which amphipathic Alpha helices stacked perpendicular to the fibril axis into tight self-associating sheets. \"", "resolution": "1.45", "pmid": "28232575", "entry": "S-0429"}