2J7J

Invariance of the zinc finger module: a comparison of the free structure with those in nucleic-acid complexes

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.218 

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This is version 1.1 of the entry. See complete history. 


Literature

Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes.

Lu, D., Klug, A.

(2007) Proteins 67: 508


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTION FACTOR IIIA85Xenopus laevisMutation(s): 0 
UniProt
Find proteins for P03001 (Xenopus laevis)
Explore P03001 
Go to UniProtKB:  P03001
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03001
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.218 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.954α = 90
b = 50.954β = 90
c = 173.431γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
SHARPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-09
    Type: Initial release
  • Version 1.1: 2012-10-10
    Changes: Database references, Derived calculations, Non-polymer description, Other, Version format compliance