1EB6

Deuterolysin from Aspergillus oryzae


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.00 Å
  • R-Value Free: 0.126 
  • R-Value Work: 0.104 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

A Quick Solution: Ab Initio Structure Determination of a 19 kDa Metalloproteinase Using Acorn

Mcauley, K.E.Jia-Xing, Y.Dodson, E.J.Lehmbeck, J.Ostergaard, P.R.Wilson, K.S.

(2001) Acta Crystallogr D Biol Crystallogr 57: 1571

  • DOI: https://doi.org/10.1107/s090744490101335x
  • Primary Citation of Related Structures:  
    1EB6

  • PubMed Abstract: 

    A data set from the metalloproteinase deuterolysin was collected at atomic resolution (1.0 A) with synchrotron radiation. The high resolution allowed the structure to be solved with the new direct-methods program ACORN using the coordinates of the Zn atom as a starting point. The phases obtained from ACORN were of sufficient quality to allow automated building to be carried out in ARP/wARP. Minimal manual rebuilding of the model was required and the structure determination was completed using the maximum-likelihood refinement program REFMAC. The whole process, starting from the processed and merged data and ending with a refined model, required less than 6 h of computational time.


  • Organizational Affiliation

    York Structural Biology Laboratory, Chemistry Department, University of York, Heslington, York YO10 5DD, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NEUTRAL PROTEASE II177Aspergillus oryzaeMutation(s): 0 
EC: 3.4.24.39
UniProt
Find proteins for P46076 (Aspergillus oryzae (strain ATCC 42149 / RIB 40))
Explore P46076 
Go to UniProtKB:  P46076
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46076
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.00 Å
  • R-Value Free: 0.126 
  • R-Value Work: 0.104 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.43α = 90
b = 34.764β = 106.03
c = 60.276γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
ACORNphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-11-23
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance