{"global_stoichiometry": "Monomer - A ", "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;MAL:A:C12 H22 O11:342.3:MALTOSE: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)CO)O)O)O)O:InChI=1S/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5-,6+,7-,8-,9-,10-,11+,12-/m1/s1:GUBGYTABKSRVRQ-ASMJPISFSA-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;GOL:C: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;MAL:C:C12 H22 O11:342.3:MALTOSE: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)CO)O)O)O)O:InChI=1S/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5-,6+,7-,8-,9-,10-,11+,12-/m1/s1:GUBGYTABKSRVRQ-ASMJPISFSA-N;SO4:C: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/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5-,6+,7-,8-,9-,10-,11+,12-/m1/s1%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5-,6+,7-,8-,9-,10-,11+,12-/m1/s1%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "reference": "Protein Sci. 2011 Jun;20(6):996-1004.", "author": "Zhao, M., Cascio, D., Sawaya, M.R., Eisenberg, D.", "type": "Protein", "ligand_id": "GOL%%MAL%%SO4%%GOL%%MAL%%SO4", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "Maltose-binding periplasmic protein/alpha-synuclein chimeric protein, fiber-like nano-crystals (without visible ThT fluorescence)", "gene_names": "P0AEX9:, malE, b4034, JW3994, P37840:, SNCA, NACP, PARK1", "chain_id": "A%%A%%A%%C%%C%%C", "ligand_mw": "92.09%%342.3%%96.06%%92.09%%342.3%%96.06", "inchi_key": "PEDCQBHIVMGVHV-UHFFFAOYSA-N%%GUBGYTABKSRVRQ-ASMJPISFSA-N%%QAOWNCQODCNURD-UHFFFAOYSA-L%%PEDCQBHIVMGVHV-UHFFFAOYSA-N%%GUBGYTABKSRVRQ-ASMJPISFSA-N%%QAOWNCQODCNURD-UHFFFAOYSA-L", "secondary_structure": "MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSMDVFMKGLSKAKEGVVAAA#CCCCSSSEEEECCTTSCHHHHHHHHHHHHTTTCCCEEEECCTTHHHHHHHHGGGTCSCSEEEEEGGGHHHHHHTTCBCCCCCCHHHHTTBCHHHHHHTEETTEECSEEEEEECCEEEEETTTCSSCCSBGGGHHHHHHHHHTTTCEEECCCCSSGGGTHHHHHHTTCEEEEEETTEEEEEEEESSSHHHHHHHHHHHHHHHTTSSCTTCCHHHHHHHHHTTSEEEEEECGGGHHHHHHHTCCEEEECCCEETTEECCCEEEEEEEEEBTTCTTHHHHHHHHHHTTTSHHHHHHHHHHSCCSEESBGGGHHHHHHCHHHHHHHHHHHHSEECCCCTTHHHHHHHHHHHHHHHHHTSSCHHHHHHHHHHHHSCHHHHHHHHCCCCCCCCCCC&MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSMDVFMKGLSKAKEGVVAAA#CCCCTTSEEEECCTTSCHHHHHHHHHHHHHHHCCCEEEECCTTHHHHHHHHHTTTCSCSEEEEEGGGHHHHHHTTCBCCCCCCHHHHTTBCHHHHHHTEETTEECSEEEEEECCEEEEETTTCSSCCSBSTTHHHHHHHHHTTTCEEECCCCSSHHHHHHHHHHTTCEEEEEETTEEEEEEEESSSHHHHHHHHHHHHHHHTTSSCTTCCHHHHHHHHHTTSEEEEEECGGGHHHHHHHTCCEEEECCCBBTTBCCCCEEEEEEEEEBTTCTTHHHHHHHHHHTTSSHHHHHHHHHHSCCSEESBGGGHHHHTTCHHHHHHHHHHHHSEECCCSTTHHHHHHHHHHHHHHHHHTSSCHHHHHHHHHHTTSSHHHHHHHHHHTTCCCCCCC", "amyloid_non_amyloid": "Non-amyloid", "length": "390", "remarks": "Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP); in space group P212121", "protein_name": "alpha-synuclein", "peptide_protein_sequence": "chain-ID A: MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSMDVFMKGLSKAKEGVVAAA; chain-ID C: MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSMDVFMKGLSKAKEGVVAAA", "ligand_name": "GLYCEROL%%MALTOSE%%SULFATE ION%%GLYCEROL%%MALTOSE%%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)CO)O)O)O)O%%[O-]S(=O)(=O)[O-]%%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)CO)O)O)O)O%%[O-]S(=O)(=O)[O-]", "pdb_id": "3Q29", "ec_number": "", "pdb_classification": "SUGAR BINDING PROTEIN", "mutation_s_field": "No", "ligand_formula": "C3 H8 O3%%C12 H22 O11%%O4 S -2%%C3 H8 O3%%C12 H22 O11%%O4 S -2", "r_value_free": "0.23199999", "alternative_name": "P0AEX9:, MMBP, Maltodextrin-binding protein, Maltose-binding protein, P37840:, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor", "description": "They use maltose-binding protein (MBP) as a carrier to crystallize segments of Alpha-synuclein. From crystal structures of fusions between MBP and four segments of Alpha-synuclein, They have been able to trace a virtual model of the first 72 residues of Alpha-synuclein. Instead of a mostly Alpha-helical conformation observed in the lipid environment, our crystal structures show Alpha-helices only at residues 1-13 and 20-34. The remaining segments are extended loops or coils. All of the predicted fiber-forming segments based on the 3D profile method are in extended conformations. Crystallized constructs showed fiber-like nano-crystals that are much thicker than typical amyloid fibrils without visible ThT fluorescence. space group: P 2(1) 2(1) 2(1)).", "resolution": "2.3", "pmid": "21462277", "entry": "S-0291"}