2BTV

ATOMIC MODEL FOR BLUETONGUE VIRUS (BTV) CORE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Work: 0.266 
  • R-Value Observed: 0.266 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The atomic structure of the bluetongue virus core.

Grimes, J.M.Burroughs, J.N.Gouet, P.Diprose, J.M.Malby, R.Zientara, S.Mertens, P.P.Stuart, D.I.

(1998) Nature 395: 470-478

  • DOI: https://doi.org/10.1038/26694
  • Primary Citation of Related Structures:  
    2BTV

  • PubMed Abstract: 

    The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 A. This transcriptionally active compartment, 700 A in diameter, represents the largest molecular structure determined in such detail. The atomic structure indicates how approximately 1,000 protein components self-assemble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through triangulation, and a different method, which we term geometrical quasi-equivalence.


  • Organizational Affiliation

    Department of Biochemistry, University of Oxford, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (VP3 CORE PROTEIN)
A, B
901Bluetongue virus (serotype 1 / isolate South Africa)Mutation(s): 0 
UniProt
Find proteins for P56582 (Bluetongue virus 1 (isolate South Africa))
Explore P56582 
Go to UniProtKB:  P56582
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56582
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (VP7 CORE PROTEIN)349Bluetongue virus (serotype 1 / isolate South Africa)Mutation(s): 0 
UniProt
Find proteins for P18259 (Bluetongue virus 1 (isolate South Africa))
Explore P18259 
Go to UniProtKB:  P18259
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP18259
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Work: 0.266 
  • R-Value Observed: 0.266 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 795.6α = 90
b = 821.8β = 90
c = 753.3γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-09-30
    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: 2024-02-14
    Changes: Data collection, Database references, Derived calculations