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- PDB-5fbz: Structure of subtilase SubHal from Bacillus halmapalus - complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5fbz | |||||||||
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Title | Structure of subtilase SubHal from Bacillus halmapalus - complex with chymotrypsin inhibitor CI2A | |||||||||
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![]() | HYDROLASE / Protease / Subtilase / Calcium binding / CI2A inhibitor | |||||||||
Function / homology | ![]() 3.4.21.14 / serine-type endopeptidase inhibitor activity / response to wounding / serine-type endopeptidase activity / proteolysis / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Dohnalek, J. / Brzozowski, A.M. / Svendsen, A. / Wilson, K.S. | |||||||||
![]() | ![]() Journal: Book / Year: 2016 Title: Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family Authors: Dohnalek, J. / McAuley, K.E. / Brzozowski, A.M. / Oestergaard, P.R. / Svendsen, A. / Wilson, K.S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 225.5 KB | Display | ![]() |
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PDB format | ![]() | 176.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.9 KB | Display | ![]() |
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Full document | ![]() | 454.4 KB | Display | |
Data in XML | ![]() | 46.8 KB | Display | |
Data in CIF | ![]() | 72.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 45356.980 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The N-terminal asparagine is carbamoylated to N-carboxyasparagine, The sequence is available in patent WO 2004083362 Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 8107.385 Da / Num. of mol.: 2 / Fragment: UNP residues 13-84 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein/peptide | | Mass: 557.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The fragment was produced probably during crystallization. The fragment length is not known. Source: (gene. exp.) ![]() ![]() ![]() #4: Chemical | ChemComp-CA / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.4 % / Description: Plate-like crystal |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Plate-like crystals were grown by hanging drop vapour diffusion with the drop consisting of 2 microliters of 15-20 mg/mL concentration protein, 10 mM sodium cacodylate in HCl buffer, pH 6.5 ...Details: Plate-like crystals were grown by hanging drop vapour diffusion with the drop consisting of 2 microliters of 15-20 mg/mL concentration protein, 10 mM sodium cacodylate in HCl buffer, pH 6.5 and 1 microliter of reservoir solution: 20% w/v PEG 4000, 0.1 M HEPES buffer, pH 7.5, 10% v/v isopropanol. |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 9, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. all: 59477 / Num. obs: 59477 / % possible obs: 76.6 % / Observed criterion σ(I): -3 / Redundancy: 9.2 % / Biso Wilson estimate: 25.5 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 22 |
Reflection shell | Resolution: 1.9→1.93 Å / Rmerge(I) obs: 0.128 / Mean I/σ(I) obs: 5.4 / % possible all: 14.5 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 14.619 Å2
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Refinement step | Cycle: 1 / Resolution: 1.9→19.97 Å
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Refine LS restraints |
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