1JBC

CONCANAVALIN A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.15 Å
  • R-Value Free: 0.167 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history


Literature

Atomic resolution structure of concanavalin A at 120 K.

Parkin, S.Rupp, B.Hope, H.

(1996) Acta Crystallogr D Biol Crystallogr 52: 1161-1168

  • DOI: https://doi.org/10.1107/S0907444996009237
  • Primary Citation of Related Structures:  
    1JBC

  • PubMed Abstract: 

    The structure of native concanavalin A has been refined to a resolution of 1.2 A against data collected at 120 K. The space group is I222, with a = 61.954 (8), b = 86.053 (11), c = 89.079 (11) A. The structure was refined by restrained weighted least-squares minimization of sum w(F(o)(2) - F(c)(2)(2) with SHELXL92/3/6. The final model contains all of the atoms from 237 amino acids, two metal ions and 271 water molecules spread over 287 sites. Disorder is modelled over two conformations for 30 amino-acid side chains. The final weighted R index on F(2) (wR(2)) on all data was 30.4%. Conventional R indices based on F were 14.2 and 11.8% for all data and for data with F > 4sigma(F), respectively.


  • Organizational Affiliation

    Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, CA 94550, USA. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CONCANAVALIN A237Canavalia ensiformisMutation(s): 0 
UniProt
Find proteins for P02866 (Canavalia ensiformis)
Explore P02866 
Go to UniProtKB:  P02866
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02866
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.15 Å
  • R-Value Free: 0.167 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.954α = 90
b = 86.053β = 90
c = 89.079γ = 90
Software Package:
Software NamePurpose
SHELXL-92model building
SHELXL-92refinement
ADSCdata collection
SHELXL-92phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-02-12
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Database references, Derived calculations, Refinement description
  • Version 1.4: 2024-05-22
    Changes: Data collection