2OVO

THE CRYSTAL AND MOLECULAR STRUCTURE OF THE THIRD DOMAIN OF SILVER PHEASANT OVOMUCOID (OMSVP3)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Work: 0.199 

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This is version 2.0 of the entry. See complete history


Literature

The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).

Bode, W.Epp, O.Huber, R.Laskowski Jr., M.Ardelt, W.

(1985) Eur J Biochem 147: 387-395

  • DOI: https://doi.org/10.1111/j.1432-1033.1985.tb08762.x
  • Primary Citation of Related Structures:  
    2OVO

  • PubMed Abstract: 

    OMSVP3 and OMTKY3 (third domains of silver pheasant and turkey ovomucoid inhibitor) are Kazal-type serine proteinase inhibitors. They have been isomorphously crystallized in the monoclinic space group C2 with cell dimensions of a = 4.429 nm, b = 2.115 nm, c = 4.405 nm, beta = 107 degrees. The asymmetric unit contains one molecule corresponding to an extremely low volume per unit molecular mass of 0.0017 nm3/Da. Data collection was only possible for the OMSVP3 crystals. Orientation and position of the OMSVP3 molecules in the monoclinic unit cells were determined using Patterson search methods and the known structure of the third domain of Japanese quail ovomucoid (OMJPQ3) [Papamokos, E., Weber, E., Bode, W., Huber, R., Empie, M. W., Kato, I. and Laskowski, M., Jr (1982) J. Mol. Biol. 158, 515-537]. The OMSVP3 structure has been refined by restrained crystallographic refinement yielding a final R value of 0.199 for data to 0.15 nm resolution. Conformation and hydrogen-bonding pattern of OMSVP3 and OMJPQ3 are very similar. Large deviations occur at the NH2 terminus owing to different crystal packing, and at the C terminus of the central helix, representing an intrinsic property and resulting from amino acid substitutions far away from this site. The deviation of OMSVP3 from OMTKY3 complexed with the Streptomyces griseus protease B is very small [Fujinaga, M., Read, R. J., Sielecki, A., Ardelt, W., Laskowski, M., Jr and James, M. N. G. (1982) Proc. Natl Acad. Sci. USA, 79, 4868-4872].


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
OVOMUCOID THIRD DOMAIN56Lophura nycthemeraMutation(s): 0 
UniProt
Find proteins for P67954 (Lophura nycthemera)
Explore P67954 
Go to UniProtKB:  P67954
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP67954
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Work: 0.199 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.29α = 90
b = 21.15β = 107
c = 44.05γ = 90
Software Package:
Software NamePurpose
EREFrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1985-11-08
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other
  • Version 2.0: 2023-07-26
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Other