{"resolution": "1.83", "ligand_mw": "59.04%%175.21%%35.45%%92.09", "secondary_structure": "KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL#CBCCHHHHHHHHHHTTCTTBTTBCHHHHHHHHHHHHTTBTTCEEECTTSCEEETTTTEETTTTCBCSCCTTCCCTTCSBGGGGGSSSTHHHHHHHHHHHHTTTGGGGCHHHHHHTTTSCGGGGGTTCCC", "inchi": "InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1%%InChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1%%InChI=1S/ClH/h1H/p-1%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2", "method": "X-RAY DIFFRACTION", "ec_number": "3.2.1.17", "uniprot_ac": "P00698", "remarks": "Lysozyme in the presence of arginine", "description": "They report results on how heat transforms globular protein, lysozyme into building block of Beta-amyloids. Light scattering experiments showed formation of lower order associated species around 50-70?\u00c2\u00b0C followed by rapid cooperativity to Beta-amyloid fibrils. crystallization drops set at higher temperatures either led to aggregates or spherulites. The latter possess an amorphous Beta-fibril rich core with thin crystalline needles projecting outwards. Diffraction of the crystalline outgrowths revealed novel dimers and trimers of lysozyme where individual chains were similar to monomer with marginal gain in Beta-sheet content. Overall this work concludes that heat induced weakly associated structures of lysozyme are the first step towards its amyloid formation. ", "type": "Inhibitor complex", "ligand_smiles": "CC(=O)[O-]%%C(C[C@@H](C(=O)O)N)CNC(=[NH2+])N%%[Cl-]%%C(C(CO)O)O", "chain_id": "A%%A%%A%%A", "species": "Gallus gallus", "keyword": "Lysozyme", "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;ARG:A:C6 H15 N4 O2 1:175.21:ARGININE:C(C[C@@H](C(=O)O)N)CNC(=[NH2+])N:InChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1:ODKSFYDXXFIFQN-BYPYZUCNSA-O;CL:A:Cl -1:35.45:CHLORIDE ION:[Cl-]:InChI=1S/ClH/h1H/p-1:VEXZGXHMUGYJMC-UHFFFAOYSA-M;GOL:A:C3 H8 O3:92.09:GLYCEROL:C(C(CO)O)O:InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2:PEDCQBHIVMGVHV-UHFFFAOYSA-N", "pmid": "26926993", "mutation_s_field": "No", "author": "Sharma, P., Verma, N., Singh, P.K., Korpole, S., Ashish", "pdb_id": "4EOF", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "QTBSBXVTEAMEQO-UHFFFAOYSA-M%%ODKSFYDXXFIFQN-BYPYZUCNSA-O%%VEXZGXHMUGYJMC-UHFFFAOYSA-M%%PEDCQBHIVMGVHV-UHFFFAOYSA-N", "ligand_name": "ACETATE ION%%ARGININE%%CHLORIDE ION%%GLYCEROL", "ligand_formula": "C2 H3 O2 -1%%C6 H15 N4 O2 1%%Cl -1%%C3 H8 O3", "ligand_id": "ACT%%ARG%%CL%%GOL", "r_value_free": "0.24600000", "protein_name": "Lysozyme C", "gene_names": "LYZ", "global_stoichiometry": "Monomer - A ", "alternative_name": "1, 4-beta-N-acetylmuramidase C, Allergen Gal d IV", "peptide_protein_sequence": "chain-ID A: KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL", "pdb_classification": "HYDROLASE", "reference": "Sci Rep. 2016 Mar 1;6:22475.", "length": "129", "entry": "S-0319"}