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Yorodumi- PDB-2fsj: Crystal structure of Ta0583, an archaeal actin homolog, native data -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fsj | ||||||
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Title | Crystal structure of Ta0583, an archaeal actin homolog, native data | ||||||
Components | hypothetical protein Ta0583 | ||||||
Keywords | STRUCTURAL PROTEIN / Actin homologs / archaea / ATPase / MreB / ParM | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermoplasma acidophilum (acidophilic) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Roeben, A. / Kofler, C. / Nagy, I. / Nickell, S. / Ulrich Hartl, F. / Bracher, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Crystal structure of an archaeal actin homolog Authors: Roeben, A. / Kofler, C. / Nagy, I. / Nickell, S. / Ulrich Hartl, F. / Bracher, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fsj.cif.gz | 78.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fsj.ent.gz | 57.4 KB | Display | PDB format |
PDBx/mmJSON format | 2fsj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2fsj_validation.pdf.gz | 435.5 KB | Display | wwPDB validaton report |
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Full document | 2fsj_full_validation.pdf.gz | 435.9 KB | Display | |
Data in XML | 2fsj_validation.xml.gz | 15.7 KB | Display | |
Data in CIF | 2fsj_validation.cif.gz | 23.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/2fsj ftp://data.pdbj.org/pub/pdb/validation_reports/fs/2fsj | HTTPS FTP |
-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: 37084.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermoplasma acidophilum (acidophilic) / Strain: DSM 1728 / Gene: Ta0583 / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): Bl21 / References: UniProt: Q9HKL4 |
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#2: Chemical | ChemComp-GOL / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.15 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM Bis-Tris pH 6.5, 15-17% PEG-2000MME, 21-22% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.95436 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 4, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95436 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→61.695 Å / Num. obs: 26096 / % possible obs: 99.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 21.2 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 6.4 |
Reflection shell | Resolution: 1.9→2 Å / % possible obs: 98.6 % / Redundancy: 2.6 % / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 2.2 / Num. measured all: 9580 / Num. unique obs: 3666 / Rsym value: 0.292 / % possible all: 98.6 |
-Phasing
Phasing MR | Rfactor: 0.488 / Cor.coef. Fo:Fc: 0.427
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→61.695 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.911 / SU B: 3.188 / SU ML: 0.095 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.161 / ESU R Free: 0.151 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.951 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→61.695 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.949 Å / Total num. of bins used: 20
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