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- PDB-4hi5: crystal structure of F37A mutant of borna disease virus matrix protein -
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Open data
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Basic information
Entry | Database: PDB / ID: 4hi5 | ||||||
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Title | crystal structure of F37A mutant of borna disease virus matrix protein | ||||||
![]() | Matrix protein | ||||||
![]() | VIRAL PROTEIN / VIRAL MATRIX PROTEIN / RNA BINDING / MEMBRANE BINDING / VIRUSES / SSRNA NEGATIVE-STRAND VIRUSES / MONONEGAVIRALES / BORNAVIRIDAE / BORNAVIRUS / VIRION | ||||||
Function / homology | ![]() virion component / host cell cytoplasm / structural constituent of virion / host cell plasma membrane / identical protein binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dautel, P. / Kolenko, P. / Stubbs, M.T. | ||||||
![]() | ![]() Title: Matrix protein variants provide support for alternative borna disease virus infection pathway Authors: Dautel, P. / Kolenko, P. / Stubbs, M.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.1 KB | Display | ![]() |
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PDB format | ![]() | 28.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 732.7 KB | Display | ![]() |
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Full document | ![]() | 733.5 KB | Display | |
Data in XML | ![]() | 7.3 KB | Display | |
Data in CIF | ![]() | 8.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4hitC ![]() 4hiuC ![]() 4hiwC ![]() 4hiyC ![]() 3f1jS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 16201.722 Da / Num. of mol.: 1 / Mutation: F37A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-C5P / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.5 Å3/Da / Density % sol: 64.87 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.1 Details: 0.2 M MgCl2, 30% w/v PEG400, 0.1 M HEPES, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 10, 2010 / Details: MIRRORS |
Radiation | Monochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 3.6→70 Å / Num. obs: 2918 / % possible obs: 100 % / Observed criterion σ(I): -3.7 / Redundancy: 11 % / Rmerge(I) obs: 0.134 / Net I/σ(I): 13.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3F1J Resolution: 3.6→70 Å / Cor.coef. Fo:Fc: 0.901 / Cor.coef. Fo:Fc free: 0.87 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / ESU R Free: 0.775 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. STRUCTURE SOLUTION AND REFINEMENT WERE PERFORMED USING FREE R FOR CROSS-VALIDATION THROUGHOUT: WORKING R = 0.2352; FREE R = 0.3125 FROM A ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. STRUCTURE SOLUTION AND REFINEMENT WERE PERFORMED USING FREE R FOR CROSS-VALIDATION THROUGHOUT: WORKING R = 0.2352; FREE R = 0.3125 FROM A RANDOM TEST SET COMPRISING 10% OF ALL REFLECTIONS (273 TOTAL). FINAL REFINEMENT WAS PERFORMED USING ALL REFLECTIONS.
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 105.14 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.6→70 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.601→3.694 Å / Total num. of bins used: 20 /
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