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Open data
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Basic information
Entry | Database: PDB / ID: 1es6 | ||||||
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Title | CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS | ||||||
![]() | MATRIX PROTEIN VP40 | ||||||
![]() | VIRAL PROTEIN / beta sandwich / anti-parallel strands / beta sheet / helix | ||||||
Function / homology | ![]() host cell endomembrane system / host cell late endosome membrane / viral budding via host ESCRT complex / structural constituent of virion / ribonucleoprotein complex / virus-mediated perturbation of host defense response / host cell plasma membrane / virion membrane / RNA binding / extracellular region / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dessen, A. / Volchkov, V. / Dolnik, O. / Klenk, H.-D. / Weissenhorn, W. | ||||||
![]() | ![]() Title: Crystal structure of the matrix protein VP40 from Ebola virus. Authors: Dessen, A. / Volchkov, V. / Dolnik, O. / Klenk, H.D. / Weissenhorn, W. #1: ![]() Title: Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus Authors: Dessen, A. / Forest, E. / Volchkov, V. / Dolnik, O. / Klenk, H.-D. / Weissenhorn, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.3 KB | Display | ![]() |
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PDB format | ![]() | 46 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.3 KB | Display | ![]() |
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Full document | ![]() | 429.7 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 17.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 31860.824 Da / Num. of mol.: 1 / Mutation: H269L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.41 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: Tris, PEG 750 monomethylether, magnesium chloride, beta-octylglucoside , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Details: Dessen, A., (2000) Acta Crystallogr., Sect.D, 56, 758. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 8, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8855 Å / Relative weight: 1 |
Reflection | Resolution: 2→25 Å / Num. all: 19062 / Num. obs: 17806 / % possible obs: 93.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.7 % / Biso Wilson estimate: 24.59 Å2 / Rmerge(I) obs: 0.039 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.224 / Num. unique all: 1170 / % possible all: 86.6 |
Reflection | *PLUS Num. measured all: 166358 |
Reflection shell | *PLUS % possible obs: 86.8 % / Mean I/σ(I) obs: 3.8 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 25 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.22 / Rfactor Rfree: 0.25 / Rfactor Rwork: 0.22 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 28.3 Å2 | |||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.337 / Rfactor obs: 0.278 |