1EJ6

Reovirus core


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.60 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 

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This is version 1.4 of the entry. See complete history


Literature

Structure of the reovirus core at 3.6 A resolution.

Reinisch, K.M.Nibert, M.L.Harrison, S.C.

(2000) Nature 404: 960-967

  • DOI: https://doi.org/10.1038/35010041
  • Primary Citation of Related Structures:  
    1EJ6

  • PubMed Abstract: 

    The reovirus core is an assembly with a relative molecular mass of 52 million that synthesizes, modifies and exports viral messenger RNA. Analysis of its structure by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions; that the genomic double-stranded RNA is coiled into concentric layers within the particle; and that there is a protein shell that appears to be common to all groups of double-stranded RNA viruses.


  • Organizational Affiliation

    Harvard University, Cambridge, Massachusetts 02138, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LAMBDA21,289Reovirus sp.Mutation(s): 0 
UniProt
Find proteins for P11079 (Reovirus type 3 (strain Dearing))
Explore P11079 
Go to UniProtKB:  P11079
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11079
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
LAMBDA1
B, C
1,275Reovirus sp.Mutation(s): 0 
UniProt
Find proteins for P15024 (Reovirus type 3 (strain Dearing))
Explore P15024 
Go to UniProtKB:  P15024
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15024
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
SIGMA2
D, E
418Reovirus sp.Mutation(s): 0 
UniProt
Find proteins for P11314 (Reovirus type 1 (strain Lang))
Explore P11314 
Go to UniProtKB:  P11314
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11314
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
F [auth C]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.60 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 
  • Space Group: F 4 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 1255α = 90
b = 1255β = 90
c = 1255γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALAdata scaling
CCP4model building
RAVEmodel building
CNSrefinement
CCP4data scaling
CCP4phasing
RAVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-07-12
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations