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Open data
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Basic information
Entry | Database: PDB / ID: 1jmu | ||||||
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Title | Crystal Structure of the Reovirus mu1/sigma3 Complex | ||||||
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![]() | VIRAL PROTEIN / Protein-protein complex / jelly roll / zinc finger | ||||||
Function / homology | ![]() host cell surface binding / symbiont-mediated suppression of host PKR/eIFalpha signaling / viral outer capsid / permeabilization of host organelle membrane involved in viral entry into host cell / symbiont entry into host cell via permeabilization of inner membrane / protein serine/threonine kinase inhibitor activity / host cell endoplasmic reticulum / host cell mitochondrion / viral life cycle / viral capsid ...host cell surface binding / symbiont-mediated suppression of host PKR/eIFalpha signaling / viral outer capsid / permeabilization of host organelle membrane involved in viral entry into host cell / symbiont entry into host cell via permeabilization of inner membrane / protein serine/threonine kinase inhibitor activity / host cell endoplasmic reticulum / host cell mitochondrion / viral life cycle / viral capsid / regulation of translation / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / virus-mediated perturbation of host defense response / host cell plasma membrane / structural molecule activity / RNA binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liemann, S. / Nibert, M.L. / Harrison, S.C. | ||||||
![]() | ![]() Title: Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3. Authors: Liemann, S. / Chandran, K. / Baker, T.S. / Nibert, M.L. / Harrison, S.C. | ||||||
History |
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Remark 999 | Sequence The authors maintain that their sequence is correct. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 576.2 KB | Display | ![]() |
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PDB format | ![]() | 484 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 884 KB | Display | ![]() |
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Full document | ![]() | 945.8 KB | Display | |
Data in XML | ![]() | 108.4 KB | Display | |
Data in CIF | ![]() | 147.3 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
-Protein , 2 types, 6 molecules BDFGHI
#2: Protein | Mass: 72182.703 Da / Num. of mol.: 3 / Fragment: C-terminus (residues 43-708) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Protein | Mass: 41263.156 Da / Num. of mol.: 3 / Mutation: A104C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Protein/peptide / Sugars , 2 types, 6 molecules ACE![](data/chem/img/BOG.gif)
![](data/chem/img/BOG.gif)
#1: Protein/peptide | Mass: 4050.441 Da / Num. of mol.: 3 / Fragment: N-terminus (residues 2-42) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #5: Sugar | |
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-Non-polymers , 4 types, 284 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-CL / | ||||
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#6: Chemical | ChemComp-SO4 / #7: Chemical | #8: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.36 Å3/Da / Density % sol: 63.39 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Ammonium sulfate, n-octyl-b-D-glucopyranoside, DTT, Pipes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
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: BRANDEIS - B4 / Detector: CCD / Date: Jun 25, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→35 Å / Num. all: 107661 / Num. obs: 107661 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5 % / Biso Wilson estimate: -1 Å2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 0.346 / Num. unique all: 6443 / % possible all: 57.3 |
Reflection | *PLUS |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 24.95 Å2 / ksol: 0.3179 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→35 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 55.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.372 / % reflection Rfree: 5.2 % / Rfactor Rwork: 0.352 |