+Open data
-Basic information
Entry | Database: PDB / ID: 1esj | ||||||
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Title | CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S) | ||||||
Components | HYDROXYETHYLTHIAZOLE KINASE | ||||||
Keywords | TRANSFERASE / trimer / alpha-beta protein | ||||||
Function / homology | Function and homology information hydroxyethylthiazole kinase / hydroxyethylthiazole kinase activity / thiamine diphosphate biosynthetic process / thiamine biosynthetic process / phosphorylation / magnesium ion binding / ATP binding Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Campobasso, N. / Mathews, I.I. / Begley, T.P. / Ealick, S.E. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution. Authors: Campobasso, N. / Mathews, I.I. / Begley, T.P. / Ealick, S.E. #1: Journal: Arch.Microbiol. / Year: 1999 Title: Thiamin Biosynthesis in Prokaryotes Authors: Begley, T.P. / Downs, D. / Ealick, S. / McLafferty, F. / Van Loon, D. / Taylor, S. / Campobasso, N. / Chiu, H.J. / Kinsland, C. / Reddick, J.J. / Xi, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1esj.cif.gz | 167.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1esj.ent.gz | 133.9 KB | Display | PDB format |
PDBx/mmJSON format | 1esj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/es/1esj ftp://data.pdbj.org/pub/pdb/validation_reports/es/1esj | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 29629.633 Da / Num. of mol.: 3 / Mutation: C198S Source method: isolated from a genetically manipulated source Details: N-TERMINAL HIS TAG / Source: (gene. exp.) Bacillus subtilis (bacteria) / Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / References: UniProt: P39593, hydroxyethylthiazole kinase #2: Chemical | #3: 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: 2.19 Å3/Da / Density % sol: 43.77 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.6 Details: 21% peg4k, 0.1M ammonium sulfate, 0.1 tris.HCl, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 18K | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.6 / Method: vapor diffusion, sitting dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1.0332 |
Detector | Detector: CCD / Date: Jun 17, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. all: 83184 / Num. obs: 83184 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 21.6 Å2 / Rmerge(I) obs: 0.042 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.375 / Num. unique all: 7921 / % possible all: 93.6 |
Reflection | *PLUS Num. measured all: 340088 |
Reflection shell | *PLUS % possible obs: 93.6 % / Mean I/σ(I) obs: 2.1 |
-Processing
Software |
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Refinement | Resolution: 1.8→20 Å / σ(F): 2 / σ(I): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.229 / Rfactor Rwork: 0.231 |