{"global_stoichiometry": "Homo 2-mer - A2 ", "ligstr": "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;MLR:A:C18 H32 O16:504.44:MALTOTRIOSE:C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@H](O[C@@H]([C@@H]([C@H]2O)O)O[C@@H]3[C@H](O[C@@H]([C@@H]([C@H]3O)O)O)CO)CO)O)O)O)O:InChI=1S/C18H32O16/c19-1-4-7(22)8(23)12(27)17(31-4)34-15-6(3-21)32-18(13(28)10(15)25)33-14-5(2-20)30-16(29)11(26)9(14)24/h4-29H,1-3H2/t4-,5-,6-,7-,8+,9-,10-,11-,12-,13-,14-,15-,16+,17-,18-/m1/s1:FYGDTMLNYKFZSV-PXXRMHSHSA-N;SO4:A:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L", "uniprot_ac": "", "inchi": "InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/C18H32O16/c19-1-4-7(22)8(23)12(27)17(31-4)34-15-6(3-21)32-18(13(28)10(15)25)33-14-5(2-20)30-16(29)11(26)9(14)24/h4-29H,1-3H2/t4-,5-,6-,7-,8+,9-,10-,11-,12-,13-,14-,15-,16+,17-,18-/m1/s1%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "reference": "Protein Sci. 2009 Jul;18(7):1521-30.", "author": "Wiltzius, J.J., Sievers, S.A., Sawaya, M.R., Eisenberg, D.", "type": "Inhibitor complex", "ligand_id": "GOL%%MLR%%SO4", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "Maltose-binding periplasmic protein,  Islet amyloid polypeptide fusion protein", "gene_names": "P0AEX9:, malE, b4034, JW3994, P10997:, IAPP", "chain_id": "A%%A%%A", "ligand_mw": "92.09%%504.44%%96.06", "inchi_key": "PEDCQBHIVMGVHV-UHFFFAOYSA-N%%FYGDTMLNYKFZSV-PXXRMHSHSA-N%%QAOWNCQODCNURD-UHFFFAOYSA-L", "secondary_structure": "MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAKCNTATCATQRLANFLVHSSNN#CCCCTTSEEEECCTTSCHHHHHHHHHHHHHHHSCCEEEECCTTHHHHHHHHHHTTCSCSEEEEEGGGHHHHHHTTCBCCBCCCHHHHTTBCHHHHHTTEETTEECSEEEEEECCEEEEETTTCSSCCSBSTTHHHHHHHHHHTTCEEECCCSSSGGGTHHHHHHTTCEEEEEETTEEEEEEEETTSHHHHHHHHHHHHHHHTTSSCTTCCHHHHHHHHHTTSEEEEEECGGGHHHHHHHTCCEEEECCCBBTTBCCCCEEEEEEEEEBTTCSCHHHHHHHHHHTTSSHHHHHHHHHHSCCSEESBHHHHHHHTTCHHHHHHHHHHHHSEECCCSTTHHHHHHHHHHHHHHHHHTSSCHHHHHHHHHHHHHSCCSSTTCTTGGGGGGGCCCCCC", "amyloid_non_amyloid": "Non-amyloid", "length": "393", "remarks": "Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein; The helical dimerization of IAPP accelerates fibril formation and that insulin impedes fibrillation by blocking the IAPP dimerization interface", "protein_name": "Amylin", "peptide_protein_sequence": "chain-ID A: MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAKCNTATCATQRLANFLVHSSNN", "ligand_name": "GLYCEROL%%MALTOTRIOSE%%SULFATE ION", "ligand_smiles": "C(C(CO)O)O%%C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@H](O[C@@H]([C@@H]([C@H]2O)O)O[C@@H]3[C@H](O[C@@H]([C@@H]([C@H]3O)O)O)CO)CO)O)O)O)O%%[O-]S(=O)(=O)[O-]", "pdb_id": "3G7W", "ec_number": "", "pdb_classification": "Sugar binding protein", "mutation_s_field": "No", "ligand_formula": "C3 H8 O3%%C18 H32 O16%%O4 S -2", "r_value_free": "0.19399999", "alternative_name": "P0AEX9:, MMBP, Maltodextrin-binding protein, Maltose-binding protein, P10997:, Amylin, Diabetes-associated peptide, Insulinoma amyloid peptide", "description": "IAPP can adopt a Alpha-helical structure at residues 8-18 and 22-27 and that molecules of IAPP dimerize. Mutational analysis suggests that this dimerization is on the pathway to fibrillation. The structure suggests how IAPP may heterodimerize with insulin. The experiments suggest the helical dimerization of IAPP accelerates fibril formation and that insulin impedes fibrillation by blocking the IAPP dimerization interface. Crystallographic studies of this helical form of IAPP are hindered by its aggressive propensity to aggregate. They have overcome this problem by chaperoning IAPP by fusion with a larger, more soluble protein. To acquire X-ray diffraction data from what is essentially an isolated IAPP molecule, they set out to protect IAPP from the inevitable fibrillation that occurs when it is unchaperoned.", "resolution": "1.75", "pmid": "19475663", "entry": "S-0238"}