1NI0

Structure of the Y94F mutant of the restriction endonuclease PvuII

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.228 

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This is version 1.4 of the entry. See complete history. 


Literature

Structure of the Y94F mutant of the restriction endonuclease PvuII

Tucker, P.A., Kokkinidis, M., Nicolaki, S., Kotsifaki, D.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Type II restriction enzyme PvuII
A, B, C
159Proteus vulgarisMutation(s): 1 
Gene Names: PVUIIR
EC: 3.1.21.4
UniProt
Find proteins for P23657 (Proteus hauseri)
Explore P23657 
Go to UniProtKB:  P23657
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23657
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.228 
  • Space Group: P 4 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 176.86α = 90
b = 176.86β = 90
c = 46.34γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-02-04
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Data collection, Database references
  • Version 1.4: 2023-08-16
    Changes: Data collection, Refinement description