2O18

Crystal structure of a Thiamine biosynthesis lipoprotein apbE, NorthEast Strcutural Genomics target ER559


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of a Thiamine biosynthesis lipoprotein apbE

Seetharaman, J.Su, M.Wang, D.Fang, Y.Cunningham, K.Ma, L.Xiao, R.Liu, J.Baran, M.C.Acton, T.B.Rost, B.Montelione, G.T.Hunt, J.F.Tong, L.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thiamine biosynthesis lipoprotein apbE
A, B, C, D
340Escherichia coliMutation(s): 10 
Gene Names: apbE
UniProt
Find proteins for P0AB85 (Escherichia coli (strain K12))
Explore P0AB85 
Go to UniProtKB:  P0AB85
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AB85
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 57.32α = 75.76
b = 70.653β = 71.67
c = 86.637γ = 69.46
Software Package:
Software NamePurpose
CNSrefinement
CBASSdata collection
HKL-2000data reduction
HKL-2000data scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-12-05
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations