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- PDB-6w0l: Henipavirus W protein interacts with 14-3-3 to modulate host gene... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6w0l | ||||||
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Title | Henipavirus W protein interacts with 14-3-3 to modulate host gene expression | ||||||
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Function / homology | ![]() regulation of epidermal cell division / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Edwards, M. / Hoad, M. / Tsimbalyuk, S. / Menicucci, A. / Messaoudi, I. / Forwood, J. / Basler, C. | ||||||
![]() | ![]() Title: Henipavirus W Proteins Interact with 14-3-3 To Modulate Host Gene Expression. Authors: Edwards, M.R. / Hoad, M. / Tsimbalyuk, S. / Menicucci, A.R. / Messaoudi, I. / Forwood, J.K. / Basler, C.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.6 KB | Display | ![]() |
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PDB format | ![]() | 44.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4datS S: Starting model for refinement |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 26542.914 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1290.434 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / ![]() |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.88 % |
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Crystal grow![]() | Temperature: 277.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 31% PEG 400, 0.1 M HEPES pH 7.5, 0.2 M CaCl2 and 2 mM DTT |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 5, 2019 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength![]() | ||||||||||||||||||||||||||||||
Reflection | Resolution: 2.3→24.97 Å / Num. obs: 13246 / % possible obs: 99.7 % / Redundancy: 4.8 % / CC1/2: 0.978 / Rmerge(I) obs: 0.188 / Rpim(I) all: 0.096 / Rrim(I) all: 0.212 / Net I/σ(I): 5.2 / Num. measured all: 63050 / Scaling rejects: 46 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing![]() | Method: ![]() |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 4DAT Resolution: 2.3→24.968 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 26.03
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 91.02 Å2 / Biso mean: 36.2406 Å2 / Biso min: 16.36 Å2 | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.3→24.968 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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