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Yorodumi- PDB-4rjj: Acetolactate synthase from Bacillus subtilis bound to ThDP - crys... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4rjj | ||||||
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Title | Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form II | ||||||
Components | Acetolactate synthase | ||||||
Keywords | LYASE / ThDP | ||||||
Function / homology | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / TPP-binding domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / ACETATE ION / THIAMINE DIPHOSPHATE / : Function and homology information | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.34 Å | ||||||
Authors | Sommer, B. / von Moeller, H. / Haack, M. / Qoura, F. / Langner, C. / Bourenkov, G. / Garbe, D. / Brueck, T. / Loll, B. | ||||||
Citation | Journal: Chembiochem / Year: 2015 Title: Detailed Structure-Function Correlations of Bacillus subtilis Acetolactate Synthase. Authors: Sommer, B. / von Moeller, H. / Haack, M. / Qoura, F. / Langner, C. / Bourenkov, G. / Garbe, D. / Loll, B. / Bruck, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rjj.cif.gz | 889.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rjj.ent.gz | 731.7 KB | Display | PDB format |
PDBx/mmJSON format | 4rjj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4rjj_validation.pdf.gz | 2.6 MB | Display | wwPDB validaton report |
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Full document | 4rjj_full_validation.pdf.gz | 2.6 MB | Display | |
Data in XML | 4rjj_validation.xml.gz | 173.2 KB | Display | |
Data in CIF | 4rjj_validation.cif.gz | 241 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rj/4rjj ftp://data.pdbj.org/pub/pdb/validation_reports/rj/4rjj | HTTPS FTP |
-Related structure data
-Links
-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 on special symmetry positions |
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-Components
-Protein , 1 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 62186.750 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Strain: PY79 / Gene: U712_18080 / Plasmid: pCBR / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21(DE3) / References: UniProt: V5MX36, EC: 4.1.3.18 |
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-Non-polymers , 5 types, 2004 molecules
#2: Chemical | ChemComp-TPP / #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-PG4 / #5: Chemical | ChemComp-ACT / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 62.06 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 45 % (v/v) PEG 200, 100 mM Tris/HCl, pH 7.0, 50 mM Li2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184 Å |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Apr 17, 2012 |
Radiation | Monochromator: SAGITALLY FOCUSED SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 2.34→48.437 Å / Num. obs: 268024 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Biso Wilson estimate: 27.5 Å2 |
Reflection shell | Resolution: 2.34→2.48 Å / Redundancy: 4.1 % / % possible all: 94.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.34→30 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 21.03 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.34→30 Å
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Refine LS restraints |
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LS refinement shell |
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