{"reference": "J Phys Chem B. 2013 Oct 24;117(42):13245-13258.", "alternative_name": "1, 4-beta-N-acetylmuramidase C", "entry": "S-0324", "gene_names": "LYZ, LZM", "remarks": "The structure of the camelid antibody cAbHuL5 in complex with human lysozyme", "secondary_structure": "KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV#CBCCHHHHHHHHHHTTCTTBTTBCHHHHHHHHHHHHSSBTTCEEEETTTTEEEETTTTEETTTTSBCSCCTTCCCTTCCBGGGGGSSCCHHHHHHHHHHTTSTTGGGGSHHHHHHTTTSCCGGGTTTSCC&KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV#CBCCHHHHHHHHHHTTCTTBTTBCHHHHHHHHHHHHTTBTTCEEEETTTTEEEETTTTEETTTTSBCSCSTTCCCTTCSBGGGGGSSCCHHHHHHHHHHHTSTTGGGGSHHHHHHTTTSCCGGGTTTSCC&QVQLQESGGGSVQAGGSLRLSCEASGLSTTVMAWFRQAPGKEREGVAAIYTGDGFPYYADSVKGRFTISQDNAKNRMYLQMNSLEPEDTAMYYCAAKTGAFSYGSLWWMSRAYNHWGQGTQVTVSSHHHHHH#CCEEEEECCEEEETTCCEEEEEEEESSCCSEEEEEEECTTCCCEEEEEEETTTCCEEECGGGTTTEEEEEETTTTEEEEEECSCCGGGCEEEEEEEESSCCCTTCCTTCGGGCCEECCCEEEEEECCCCCCC&QVQLQESGGGSVQAGGSLRLSCEASGLSTTVMAWFRQAPGKEREGVAAIYTGDGFPYYADSVKGRFTISQDNAKNRMYLQMNSLEPEDTAMYYCAAKTGAFSYGSLWWMSRAYNHWGQGTQVTVSSHHHHHH#CEEEEEECCEEEETTCCEEEEEEEEESCCSEEEEEEECTTSCCEEEEEEETTTCCEEECGGGTTTEEEEEEGGGTEEEEEECSCCGGGCEEEEEEEESSCCCTTCCTTCGGGCSEECCCEEEEEECCCCCCC", "chain_id": "A%%A%%B%%B%%C", "inchi": "InChI=1S/ClH/h1H/p-1%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/ClH/h1H/p-1%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/ClH/h1H/p-1", "amyloid_non_amyloid": "Non-amyloid", "pmid": "23919586", "ligand_smiles": "[Cl-]%%C(C(CO)O)O%%[Cl-]%%C(C(CO)O)O%%[Cl-]", "keyword": "", "peptide_protein_sequence": "chain-ID A: KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV; chain-ID B: KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV; chain-ID C: QVQLQESGGGSVQAGGSLRLSCEASGLSTTVMAWFRQAPGKEREGVAAIYTGDGFPYYADSVKGRFTISQDNAKNRMYLQMNSLEPEDTAMYYCAAKTGAFSYGSLWWMSRAYNHWGQGTQVTVSSHHHHHH; chain-ID D: QVQLQESGGGSVQAGGSLRLSCEASGLSTTVMAWFRQAPGKEREGVAAIYTGDGFPYYADSVKGRFTISQDNAKNRMYLQMNSLEPEDTAMYYCAAKTGAFSYGSLWWMSRAYNHWGQGTQVTVSSHHHHHH", "uniprot_ac": "", "protein_name": "Lysozyme", "r_value_free": "0.21899999", "mutation_s_field": "No", "ligand_mw": "35.45%%92.09%%35.45%%92.09%%35.45", "pdb_id": "4I0C", "inchi_key": "VEXZGXHMUGYJMC-UHFFFAOYSA-M%%PEDCQBHIVMGVHV-UHFFFAOYSA-N%%VEXZGXHMUGYJMC-UHFFFAOYSA-M%%PEDCQBHIVMGVHV-UHFFFAOYSA-N%%VEXZGXHMUGYJMC-UHFFFAOYSA-M", "ec_number": "3.2.1.17", "pdb_classification": "IMMUNE SYSTEM/HYDROLASE", "type": "Inhibitor complex", "author": "De Genst, E., Chan, P.H., Pardon, E., Hsu, S.T., Kumita, J.R., Christodoulou, J., Menzer, L., Chirgadze, D.Y., Robinson, C.V., Muyldermans, S., Matagne, A., Wyns, L., Dobson, C.M., Dumoulin, M.", "species": "", "ligand_id": "CL%%GOL%%CL%%GOL%%CL", "method": "X-RAY DIFFRACTION", "ligand_name": "CHLORIDE ION%%GLYCEROL%%CHLORIDE ION%%GLYCEROL%%CHLORIDE ION", "global_stoichiometry": "Hetero 2-mer - AB ", "resolution": "1.95", "ligand_formula": "Cl -1%%C3 H8 O3%%Cl -1%%C3 H8 O3%%Cl -1", "length": "130 ,  132 ,  132", "ligstr": "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;CL:B:Cl -1:35.45:CHLORIDE ION:[Cl-]:InChI=1S/ClH/h1H/p-1:VEXZGXHMUGYJMC-UHFFFAOYSA-M;GOL:B: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;CL:C:Cl -1:35.45:CHLORIDE ION:[Cl-]:InChI=1S/ClH/h1H/p-1:VEXZGXHMUGYJMC-UHFFFAOYSA-M", "description": "They report the effects of the interaction of two camelid antibody fragments, generally called nanobodies, namely cAb-HuL5. cAb-HuL5 binds to the Alpha-domain, one of the two lobes of the native lysozyme structure. The binding of cAb-HuL5/cAb-HuL5G strongly inhibits fibril formation by the amyloidogenic variants; it does not, however, suppress the locally transient cooperative unfolding transitions, characteristic of these variants, in which the Beta-domain and the C-helix unfold and which represents key early intermediate species in the formation of amyloid fibrils."}