5U5B

Coiled Coil Peptide Metal Coordination Framework: Trimer Fold

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.253 
  • R-Value Observed: 0.256 

wwPDB Validation   3D Report Full Report


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


Literature

Supramolecular Metal-Coordination Polymers, Nets, and Frameworks from Synthetic Coiled-Coil Peptides.

Tavenor, N.A., Murnin, M.J., Horne, W.S.

(2017) J Am Chem Soc 139: 2212-2215

  • DOI: https://doi.org/10.1021/jacs.7b00651
  • Primary Citation of Related Structures:  
    5U59, 5U5A, 5U5B, 5U5C

  • PubMed Abstract: 

    Metal coordination and peptide-directed self-assembly are two proven methods for creating defined supramolecular architectures. Here, we report a new class of crystalline materials based on coiled-coil peptides bearing unnatural metal-chelating terpyridine moieties. High-resolution structural characterization of lattices formed in the presence of Cu 2+ reveals a general assembly mechanism. Subtle sequence variation in the modular synthetic ligand dictates assembly morphology.

    • Organizational Affiliation: 

    Department of Chemistry, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Designed trimeric coiled coil peptide with two terpyridine side chains
A, B, C
30synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.253 
  • R-Value Observed: 0.256 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.749α = 90
b = 77.749β = 90
c = 55.325γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
d*TREKdata reduction
d*TREKdata scaling
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
National Science Foundation (NSF, United States)United StatesDMR1149067

Revision History  (Full details and data files)

  • Version 1.0: 2017-02-22
    Type: Initial release
  • Version 1.1: 2017-09-20
    Changes: Author supporting evidence
  • Version 1.2: 2019-11-27
    Changes: Author supporting evidence
  • Version 1.3: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2023-11-15
    Changes: Data collection, Derived calculations