1BIT

THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN A SECOND CRYSTAL FORM

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 

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


Literature

Structure of anionic salmon trypsin in a second crystal form.

Berglund, G.I., Smalas, A.O., Hordvik, A., Willassen, N.P.

(1995) Acta Crystallogr D Biol Crystallogr 51: 725-730

  • DOI: https://doi.org/10.1107/S0907444995000333
  • Primary Citation of Related Structures:  
    1BIT

  • PubMed Abstract: 

    Anionic salmon trypsin in a second crystal form (ST-IIB) has been refined at 1.83 A, resolution. The crystals are orthorhombic and belong to space group P2(1)2(1)2 with lattice parameters a = 77.09, b = 82.33 and c = 31.16 A. The present structure has been compared to salmon trypsin as it appears in a previously reported crystal form (ST-IIA) with cell dimensions a = 61.95, b = 84.33 and c = 39.11 A [Smalås & Hordvik (1993). Acta Cryst. D49, 318-330]. The presence of a sulfate group involved in several hydrogen bonds to active-site residues, and the location of an additional benzamidine site in the crystal lattice, are the most striking differences between the present and the previous structure. Superposition of main-chain atoms in the two structures give an overall r.m.s. difference of 0.26 A, with the main differences located to areas with different molecular packing. The overall coordinate error is estimated to be between 0.20 and 0.25 A, by the method of Luzzati.

    • Organizational Affiliation: 

    Protein Crystallography Group, Department of Chemistry, Institute of Mathematical and Physical Sciences, University of Tromsø, Norway.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRYPSIN237Salmo salarMutation(s): 0 
UniProt
Find proteins for P35031 (Salmo salar)
Explore P35031 
Go to UniProtKB:  P35031
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP35031
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.09α = 90
b = 82.33β = 90
c = 31.16γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
PROLSQrefinement
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-11-01
    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: 2019-07-17
    Changes: Advisory, Data collection, Other, Refinement description
  • Version 1.4: 2019-08-14
    Changes: Data collection, Refinement description