{"global_stoichiometry": "Homo 2-mer - A2 ", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):E1562-70.", "author": "Hochberg, G.K., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M.R., Collier, M.P., Stroud, J., Carver, J.A., Baldwin, A.J., Robinson, C.V., Eisenberg, D.S., Benesch, J.L., Laganowsky, A.", "type": "Inhibitor complex", "ligand_id": "", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "", "gene_names": "HSPB1, HSP27, HSP28", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "GVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQS#CCEEECCBTTEEEEEEECTTSCGGGEEEEEETTEEEEEEEEEEEECSSSEEEEEEEEEEECCTTCCTTSCEEEECTTSEEEEEEECCCCCCCC&ITIPVTFE#CCCCCBCC&GVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQS#CCCCBCCCCCCEEEEEECTTCCGGGEEEEEETTEEEEEEEEEEEECSSSEEEEEEEEEEECCTTCCTTSCEEEECTTSEEEEEECCCCCCCCC&ITIPVTFE#CCCCCBCC", "amyloid_non_amyloid": "Non-amyloid", "length": "93 ,  8 ,  93 ,  8", "remarks": "Human Hsp27 core domain in complex with C-terminal peptide", "protein_name": "Human Hsp27", "peptide_protein_sequence": "chain-ID A: GVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQS; chain-ID B: ITIPVTFE; chain-ID C: GVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQS; chain-ID D: ITIPVTFE", "ligand_name": "", "ligand_smiles": "", "pdb_id": "4MJH", "ec_number": "", "pdb_classification": "CHAPERONE", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.266", "alternative_name": "28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, Stress-responsive protein 27", "description": "The structures of  small heat-shock protein's core domains (cABC, cHSP27), each in complex with a segment of their respective C-terminal regions. Both truncated proteins dimerize, and although this interface is labile in the case of cABC, in cHSP27 the dimer can be cross-linked by an intermonomer disulfide linkage.", "resolution": "2.6", "pmid": "24711386", "entry": "S-0340"}