6OLO

Controlling the Self-Assembly of Synthetic Metal-Coordinating Coiled-Coil Peptides: Hexagonal Lattice from a Trimeric Coiled Coil

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.273 
  • R-Value Work: 0.257 
  • R-Value Observed: 0.259 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides.

Scheib, K.A., Tavenor, N.A., Lawless, M.J., Saxena, S., Horne, W.S.

(2019) Chem Commun (Camb) 55: 7752-7755

  • DOI: https://doi.org/10.1039/c9cc03496j
  • Primary Citation of Related Structures:  
    6OLN, 6OLO

  • PubMed Abstract: 

    Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that drives the assembly and apply these insights to exert rational control over structure and morphology in the materials.

    • Organizational Affiliation: 

    Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Designed trimeric coiled coil peptide30synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CU
Query on CU
Download Ideal Coordinates CCD File 
B [auth A]COPPER (II) ION
Cu
JPVYNHNXODAKFH-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.273 
  • R-Value Work: 0.257 
  • R-Value Observed: 0.259 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 39.739α = 90
b = 39.739β = 90
c = 41.945γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
d*TREKdata reduction
d*TREKdata scaling
PHASERphasing

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: 2020-03-25
    Type: Initial release
  • Version 1.1: 2023-10-11
    Changes: Data collection, Database references, Refinement description
  • Version 1.2: 2023-11-15
    Changes: Data collection, Derived calculations