2ERL

PHEROMONE ER-1 FROM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.00 Å
  • R-Value Free: 0.165 
  • R-Value Observed: 0.129 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A challenging case for protein crystal structure determination: the mating pheromone Er-1 from Euplotes raikovi.

Anderson, D.H.Weiss, M.S.Eisenberg, D.

(1996) Acta Crystallogr D Biol Crystallogr 52: 469-480

  • DOI: https://doi.org/10.1107/S0907444995014235
  • Primary Citation of Related Structures:  
    2ERL

  • PubMed Abstract: 

    Four different phasing methods have been applied to the determination of the crystal structure of the 40 amino-acid mating pheromone of the unicellular ciliated protozoan Euplotes raikovi. The difficulties, failures and successes in attempts to solve the structure by: (1) molecular replacement, (2) direct phasing using the 'Shake and Bake' algorithm, (3) isomorphous replacement, and (4) multiple-wavelength anomalous dispersion are described. The structure was first solved by molecular replacement, and then was the first successful structure determination by 'Shake and Bake' without the direct involvement of its authors. A description of the current status of the high-resolution refinement of the structure is also given. The model is refined against 1 A resolution data to an R factor of 12.9%, and includes H atoms and discretely disordered side chains.


  • Organizational Affiliation

    UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Molecular Biology Institute, University of California, Los Angeles 90095-1570, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MATING PHEROMONE ER-140Euplotes raikoviMutation(s): 0 
UniProt
Find proteins for P10774 (Euplotes raikovi)
Explore P10774 
Go to UniProtKB:  P10774
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10774
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EOH
Query on EOH

Download Ideal Coordinates CCD File 
B [auth A]ETHANOL
C2 H6 O
LFQSCWFLJHTTHZ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.00 Å
  • R-Value Free: 0.165 
  • R-Value Observed: 0.129 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.91α = 90
b = 23.1β = 110.4
c = 23.1γ = 90
Software Package:
Software NamePurpose
MARRESEARCHdata collection
SHELXL-93model building
SHELXL-93refinement
MARdata reduction
SHELXL-93phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-07-11
    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: 2017-11-29
    Changes: Derived calculations, Other