4V5W

Grapevine Fanleaf virus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Exploiting Protein Engineering and Crystal Polymorphism for Successful X-Ray Structure Determination

Bonnefond, L.Schellenberger, P.Basquin, J.Demangeat, G.Ritzenthaler, C.Chenevert, R.Balg, C.Frugier, M.Rudinger-Thirion, J.Giege, R.Lorber, B.Sauter, C.

(2011) Cryst Growth Des 11: 4334


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
COAT PROTEIN504Grapevine fanleaf virusMutation(s): 0 
UniProt
Find proteins for P18474 (Grapevine fanleaf virus)
Explore P18474 
Go to UniProtKB:  P18474
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP18474
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.232 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 283.6α = 90
b = 295.5β = 91.6
c = 394.3γ = 90
Software Package:
Software NamePurpose
AMoREmodel building
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-09
    Type: Initial release
  • Version 1.1: 2014-12-10
    Changes: Other
  • Version 1.2: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2024-01-10
    Changes: Data collection, Database references, Refinement description