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Yorodumi- PDB-5h4g: Structure of PIN-domain protein (VapC4 toxin) from Pyrococcus hor... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5h4g | ||||||
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Title | Structure of PIN-domain protein (VapC4 toxin) from Pyrococcus horikoshii determined at 1.77 A resolution | ||||||
Components | Ribonuclease VapC4 | ||||||
Keywords | HYDROLASE / Pyrococcus horikoshii / hypothetical protein / PIN-domain | ||||||
Function / homology | Function and homology information RNA nuclease activity / Hydrolases; Acting on ester bonds / magnesium ion binding Similarity search - Function | ||||||
Biological species | Pyrococcus horikoshii OT3 (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.77 Å | ||||||
Authors | Biswas, A. / Hatti, K. / Srinivasan, N. / Murthy, M.R.N. / Sekar, K. | ||||||
Citation | Journal: J. Struct. Biol. / Year: 2017 Title: Structure determination of contaminant proteins using the MarathonMR procedure Authors: Hatti, K. / Biswas, A. / Chaudhary, S. / Dadireddy, V. / Sekar, K. / Srinivasan, N. / Murthy, M.R.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5h4g.cif.gz | 71.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5h4g.ent.gz | 51.9 KB | Display | PDB format |
PDBx/mmJSON format | 5h4g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5h4g_validation.pdf.gz | 433.7 KB | Display | wwPDB validaton report |
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Full document | 5h4g_full_validation.pdf.gz | 435.2 KB | Display | |
Data in XML | 5h4g_validation.xml.gz | 13.2 KB | Display | |
Data in CIF | 5h4g_validation.cif.gz | 18.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h4/5h4g ftp://data.pdbj.org/pub/pdb/validation_reports/h4/5h4g | HTTPS FTP |
-Related structure data
Related structure data | 5h3lC 5h4fC 5h4hC 1v96S C: citing same article (ref.) S: Starting model for refinement |
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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: 17210.270 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii OT3 (archaea) / Strain: OT3 / Gene: vapC4, PH0500 / Production host: Escherichia coli (E. coli) References: UniProt: O58236, Hydrolases; Acting on ester bonds #2: Chemical | ChemComp-ZN / | #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: 1.68 Å3/Da / Density % sol: 26.68 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.2M Sodium acetate trihydrate, 0.1M Tris-HCl, 30%(w/v) PEG 4000, 0.1M Turine |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.97625 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 14, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97625 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→50.94 Å / Num. obs: 22115 / % possible obs: 99.1 % / Redundancy: 7.2 % / Net I/σ(I): 18.4 |
Reflection shell | Resolution: 1.77→1.81 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.749 / Mean I/σ(I) obs: 2.3 / CC1/2: 0.68 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1V96 Resolution: 1.77→50.94 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.939 / SU B: 3.303 / SU ML: 0.102 / Cross valid method: THROUGHOUT / ESU R: 0.136 / ESU R Free: 0.134 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.634 Å2
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Refinement step | Cycle: 1 / Resolution: 1.77→50.94 Å
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Refine LS restraints |
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