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1BLI
BACILLUS LICHENIFORMIS ALPHA-AMYLASE
Deposited 1998-01-07
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Different mutation/modification
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Protein monomer
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
30–512（483 aa）
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Mutation：N190F, Q264S, N265Y
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CA CALCIUM ION × 3
NA SODIUM ION × 1
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X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
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Resolution 1.90 Å
R-free 0.185
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1BPL
GLYCOSYLTRANSFERASE
Deposited 1995-07-13
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Different construct
Different mutation/modification
Different oligomeric state
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Protein homooligomer
Homooligomer；Protein × 2
PDB declaration: dimeric
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Chain A
30–218（189 aa）
Chain B
219–512（294 aa）
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Not recorded
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No recorded non-water small molecule
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 8.2；MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE FROM BACILLUS LICHENIFORMIS. VAPOR DIFFUSION, ROOM TEMPERATURE PROTEIN SOLUTION: 15 MG/ML BLA IN 0.4 M SODIUM CITRATE 2.5 MM EDTA, PH 8.2 RESERVOIR: 0.66 M SODIUM CITRATE, 2.5 MM EDTA, PH 8.2 CALCIUM REMOVAL BY EDTA LEADS TO A CLEAVAGE OF BLA AFTER GLU 189 DUE TO TRACE AMOUNTS OF A GLU-C-ENDOPEPTIDASE PRESENT IN THE PREPARATION (SEE PAPER)., vapor diffusion
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Resolution 2.20 Å
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1E3X
Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A
Deposited 2000-06-26
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Different construct
Different oligomeric state
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Insufficient information
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
330–512（183 aa）
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Not recorded
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CA CALCIUM ION × 4
NA SODIUM ION × 1
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML.
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Resolution 1.90 Å
R-free 0.200
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1E3Z
Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A
Deposited 2000-06-27
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Different construct
Different oligomeric state
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Insufficient information
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
330–512（183 aa）
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Not recorded
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CA CALCIUM ION × 4
NA SODIUM ION × 1
ACI 6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL × 3
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM ACARBOSE SOLUTION TO OBTAIN THE COMPLEX.
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Resolution 1.93 Å
R-free 0.200
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1E40
Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A
Deposited 2000-06-27
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Different construct
Different oligomeric state
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Insufficient information
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
330–512（183 aa）
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Not recorded
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CA CALCIUM ION × 4
NA SODIUM ION × 1
TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM MALTOTRIOSE SOLUTION TO OBTAIN THE COMPLEX.
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Resolution 2.20 Å
R-free 0.210
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1E43
Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A
Deposited 2000-06-27
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Different construct
Different oligomeric state
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Insufficient information
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
330–512（183 aa）
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Not recorded
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CA CALCIUM ION × 4
NA SODIUM ION × 1
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 10；291 K；CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML.
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Resolution 1.70 Å
R-free 0.185
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1OB0
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
Deposited 2003-01-21
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Different mutation/modification
Different ligand/ion
Different experimental conditions
Different structure-quality metrics
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Assembly 1
Protein monomer
Monomer；Protein × 1
PDB declaration: monomeric
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Chain A
30–512（483 aa）
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Mutation：YES
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CA CALCIUM ION × 3
NA SODIUM ION × 1
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X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 7；PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION FROM DROPS CONTAINING 4 UL OF PROTEIN SOLUTION (10 MG/ML IN 50 MM TRIS/HCL, PH 8.0) PLUS 4 UL OF RESERVOIR SOLUTION (50 MM HEPES, 1 M AMMONIUM SULFATE, 1% (V/V) PEG 500, PH 7.0) EQUILIBRATED AGAINST 1 ML OF RESERVOIR SOLUTION.
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Resolution 1.83 Å
R-free 0.154
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