{"resolution": "", "ligand_mw": "", "secondary_structure": "GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYGGHHHHHH#CCCSCCCCCSSSCCCCCCCCCCCCSCCCCSCCCTTCCSCEECCCSCCCCCCSSSHHHHHHHHHGGGTSCSCCEECSSCCSSSSTTSSTTHHHHHHHHHHHHHHHTCCCCCHHHHHHHHHHHHHHHHHHHTTHHHHHTTSCCCCCC", "inchi": "", "method": "SOLUTION NMR", "ec_number": "", "uniprot_ac": "P04156", "remarks": "PrP226* - Solution-state NMR structure of truncated human prion protein", "description": "They have determined the NMR structure of recombinant PrP226. The structure of the protein consists of a disordered N-terminal part (residues 90-125) and a structured C-terminal part (residues 126-226). The C-terminal segment consists of four Alpha-helices and a short antiparallel Beta-sheet. Our model predicts a break in the C-terminal helix and reorganized hydrophobic interactions between helix Alpha 3 and Beta 2 -Alpha 2 loop due to the shorter C-terminus. ", "type": "Protein", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "Major prion protein", "ligstr": "", "pmid": "28109886", "mutation_s_field": "No", "author": "Kovac, V., Zupancic, B., Ilc, G., Plavec, J., Curin Serbec, V.", "pdb_id": "5L6R", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "", "protein_name": "Major prion protein", "gene_names": "PRNP, ALTPRP, PRIP, PRP", "global_stoichiometry": "Monomer - A", "alternative_name": "ASCR, PrP27-30, PrP33-35C", "peptide_protein_sequence": "chain-ID A: GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYGGHHHHHH", "pdb_classification": "TRANSPORT PROTEIN", "reference": "Biochem Biophys Res Commun. 2017 Feb 26;484(1):45-50.", "length": "145", "entry": "S-0442"}