+Open data
-Basic information
Entry | Database: PDB / ID: 4liz | ||||||
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Title | Crystal structure of coactosin from Entamoeba histolytica | ||||||
Components | Actin-binding protein, cofilin/tropomyosin family protein, putative | ||||||
Keywords | STRUCTURAL PROTEIN / Coactosin / actin binding protein / actin | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Entamoeba histolytica (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.499 Å | ||||||
Authors | Gourinath, S. / Kumar, N. | ||||||
Citation | Journal: Plos Pathog. / Year: 2014 Title: EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica. Authors: Kumar, N. / Somlata / Mazumder, M. / Dutta, P. / Maiti, S. / Gourinath, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4liz.cif.gz | 43.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4liz.ent.gz | 32.7 KB | Display | PDB format |
PDBx/mmJSON format | 4liz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/li/4liz ftp://data.pdbj.org/pub/pdb/validation_reports/li/4liz | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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: 15883.747 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Entamoeba histolytica (eukaryote) / Strain: HM1:IMSS Gene: Actin binding protein, Cofilin/tropomyosin family, EHI7A_006660 Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: N9TKD6 |
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#2: Chemical | ChemComp-EPE / |
#3: Chemical | ChemComp-NA / |
#4: 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: 2.92 Å3/Da / Density % sol: 57.91 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop Details: 100 mM HEPES, 33 % PEG 3350, 100mM Sodium acetate, 0.2 mM CaCl2, 10mM MgCl2, pH 7.3 - 7.5, vapor diffusion, hanging drop, temperature 289K PH range: 7.3 - 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.97372 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARmosaic 225 / Detector: CCD / Date: Oct 28, 2009 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97372 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.499→50 Å / Num. obs: 28852 / % possible obs: 98.2 % / Redundancy: 8.6 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 17.6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: SAD |
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-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.499→42.21 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.964 / Occupancy max: 1 / Occupancy min: 0.12 / SU B: 0.985 / SU ML: 0.038 / SU R Cruickshank DPI: 0.0615 / Cross valid method: THROUGHOUT / ESU R: 0.061 / ESU R Free: 0.064 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.25 Å2
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Refinement step | Cycle: LAST / Resolution: 1.499→42.21 Å
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Refine LS restraints |
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