1K51

A G55A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.210 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.186 

wwPDB Validation   3D Report Full Report


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


Literature

Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.

O'Neill, J.W., Kim, D.E., Johnsen, K., Baker, D., Zhang, K.Y.

(2001) Structure 9: 1017-1027

  • DOI: https://doi.org/10.1016/s0969-2126(01)00667-0
  • Primary Citation of Related Structures:  
    1K50, 1K51, 1K52, 1K53

  • PubMed Abstract: 

    Thermodynamic and kinetic studies of the Protein L B1 domain (Ppl) suggest a folding pathway in which, during the folding transition, the first beta hairpin is formed while the second beta hairpin and the alpha helix are largely unstructured. The same mutations in the two beta turns have opposite effects on the folding and unfolding rates. Three of the four residues composing the second beta turn in Ppl have consecutive positive phi angles, indicating strain in the second beta turn.

    • Organizational Affiliation: 

    Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein L72Finegoldia magna ATCC 29328Mutation(s): 2 
Gene Names: Protein L, B1 domain
UniProt
Find proteins for Q51912 (Finegoldia magna)
Explore Q51912 
Go to UniProtKB:  Q51912
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ51912
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.210 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.186 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.008α = 90
b = 75.125β = 90
c = 60.091γ = 90
Software Package:
Software NamePurpose
EPMRphasing
CNSrefinement
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-12-05
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Database references, Derived calculations, Refinement description
  • Version 1.4: 2023-08-16
    Changes: Data collection, Refinement description