1EZJ | pdb_00001ezj

CRYSTAL STRUCTURE OF THE MULTIMERIZATION DOMAIN OF THE PHOSPHOPROTEIN FROM SENDAI VIRUS

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 
    0.293 (Depositor), 0.300 (DCC) 
  • R-Value Work: 
    0.249 (Depositor), 0.250 (DCC) 
  • R-Value Observed: 
    0.255 (Depositor) 

wwPDB Validation   3D Report Full Report


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


Literature

Tetrameric coiled coil domain of Sendai virus phosphoprotein.

Tarbouriech, N., Curran, J., Ruigrok, R.W., Burmeister, W.P.

(2000) Nat Struct Biol 7: 777-781

  • DOI: https://doi.org/10.1038/79013
  • Primary Citation of Related Structures:  
    1EZJ

  • PubMed Abstract: 

    The high resolution X-ray structure of the Sendai virus oligomerization domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with canonical hydrophobic heptad repeats. Alternatives to the classic knobs-into-holes packing lead to differences in supercoil pitch and diameter that allow water molecules inside the core. This open and more hydrophilic structure does not seem to be destabilized by mutations that would be expected to disrupt classic coiled coils.

    • Organizational Affiliation: 

    European Synchrotron Radiation Facility, Grenoble cedex, France.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEOCAPSID PHOSPHOPROTEIN115Sendai virus (strain Harris)Mutation(s): 0 
EC: 2.7.7.48
UniProt
Find proteins for P04859 (Sendai virus (strain Harris))
Explore P04859 
Go to UniProtKB:  P04859
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04859
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free:  0.293 (Depositor), 0.300 (DCC) 
  • R-Value Work:  0.249 (Depositor), 0.250 (DCC) 
  • R-Value Observed: 0.255 (Depositor) 
Space Group: P 4 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.584α = 90
b = 48.584β = 90
c = 100.847γ = 90
Software Package:
Software NamePurpose
SHARPphasing
CNSrefinement
DENZOdata reduction
CCP4data scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-09-20
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2011-11-16
    Changes: Atomic model
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations