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Open data
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Basic information
Entry | Database: PDB / ID: 2wan | ||||||
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Title | Pullulanase from Bacillus acidopullulyticus | ||||||
![]() | PULLULANASE | ||||||
![]() | HYDROLASE / GLYCOSIDE HYDROLASE / POLYSACCHARIDE / AMYLASE / STARCH / CARBOHYDRATE | ||||||
Function / homology | ![]() Rab geranylgeranyltransferase alpha-subunit, insert domain / Golgi alpha-mannosidase II / Glycosidases / Immunoglobulins / TIM Barrel / Alpha-Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Turkenburg, J.P. / Brzozowski, A.M. / Svendsen, A. / Borchert, T.V. / Davies, G.J. / Wilson, K.S. | ||||||
![]() | ![]() Title: Structure of a Pullulanase from Bacillus Acidopullulyticus. Authors: Turkenburg, J.P. / Brzozowski, A.M. / Svendsen, A. / Borchert, T.V. / Davies, G.J. / Wilson, K.S. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.8 KB | Display | ![]() |
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PDB format | ![]() | 157.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.3 KB | Display | ![]() |
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Full document | ![]() | 479.6 KB | Display | |
Data in XML | ![]() | 40.1 KB | Display | |
Data in CIF | ![]() | 63.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 101633.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: A588 CYS MODELLED AS OXIDISED CYSTEINE (CSX) / Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-GOL / #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-ACT / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.95 Å3/Da / Density % sol: 58 % / Description: NONE |
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Crystal grow | Details: 25-35% AS (V/V OF SATURATED SOLUTION), 0.1 M ACETATE BUFFER PH 4.5, 5-10 MM NDSB 195, OR 256, OR DETERGENT SB12 |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→104 Å / Num. obs: 124792 / % possible obs: 95.8 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 1.65→1.68 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 1.5 / % possible all: 89.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.65→105.41 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.946 / SU B: 1.692 / SU ML: 0.058 / Cross valid method: THROUGHOUT / ESU R: 0.09 / ESU R Free: 0.093 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. THE N-TERMINAL 111 RESIDUES IN THE SEQUENCE HAVE NOT BEEN MODELLED. THE ELECTRON DENSITY IS UNINTERPRETABLE, ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. THE N-TERMINAL 111 RESIDUES IN THE SEQUENCE HAVE NOT BEEN MODELLED. THE ELECTRON DENSITY IS UNINTERPRETABLE, ALTHOUGH IT HAS SOME FEATURES INDICATING THIS DOMAIN IS DISORDERED BUT PRESENT.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.218 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→105.41 Å
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Refine LS restraints |
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