1KTH

The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.95 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.135 
  • R-Value Observed: 0.136 

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This is version 1.4 of the entry. See complete history


Literature

Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A).

Arnoux, B.Ducruix, A.Prange, T.

(2002) Acta Crystallogr D Biol Crystallogr 58: 1252-1254

  • DOI: https://doi.org/10.1107/s0907444902007333
  • Primary Citation of Related Structures:  
    1KTH

  • PubMed Abstract: 

    The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.


  • Organizational Affiliation

    Laboratoire de Cristallographie et RMN Biologiques (UMR 8015 CNRS), Faculté de Pharmacie 4, Avenue de l'Observatoire, 75006 Paris, France. arnoux@pharmacie.univ-paris5.fr


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Collagen alpha 3(VI) chain58Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P12111 (Homo sapiens)
Explore P12111 
Go to UniProtKB:  P12111
PHAROS:  P12111
GTEx:  ENSG00000163359 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP12111
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.95 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.135 
  • R-Value Observed: 0.136 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 25.27α = 90
b = 37.8β = 109.42
c = 28.51γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
SHELXL-97refinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-02-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Database references
  • Version 1.4: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description