4PW0

Alpha/beta hydrolase fold protein from Chitinophaga pinensis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.48 Å
  • R-Value Free: 0.133 
  • R-Value Work: 0.103 
  • R-Value Observed: 0.105 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Alpha/beta hydrolase fold protein from Chitinophaga pinensis.

Osipiuk, J.Tesar, C.Clancy, S.Joachimiak, A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha/beta hydrolase fold protein283Chitinophaga pinensis DSM 2588Mutation(s): 0 
Gene Names: Cpin_2213
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.48 Å
  • R-Value Free: 0.133 
  • R-Value Work: 0.103 
  • R-Value Observed: 0.105 
  • Space Group: P 62
  • Diffraction Data: https://doi.org/10.18430/M34PW0
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 110.38α = 90
b = 110.38β = 90
c = 59.184γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
SBC-Collectdata collection
HKL-3000data reduction
HKL-3000data scaling
SHELXDphasing
MLPHAREphasing
DMphasing
SOLVEphasing
RESOLVEphasing
HKL-3000phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-04-02
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Refinement description