4W9B

Crystal structure of Gamma-B Crystallin expressed in E. coli based on mRNA variant 1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.28 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.171 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Two synonymous gene variants encode proteins with identical sequence, but different folding conformations.

Buhr, F.Jha, S.Thommen, M.Rodnina, M.Kutz, F.Kudlinzki, D.Linhard, V.L.Komar, A.A.Schwalbe, H.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Gamma-crystallin B181Bos taurusMutation(s): 0 
Gene Names: CRYGB
UniProt
Find proteins for P02526 (Bos taurus)
Explore P02526 
Go to UniProtKB:  P02526
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02526
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.28 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.171 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 123.641α = 90
b = 123.641β = 90
c = 56.548γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Cootmodel building
PHASERphasing
XSCALEdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-09-09
    Type: Initial release
  • Version 2.0: 2024-01-10
    Changes: Atomic model, Data collection, Database references, Refinement description