3QQT

Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 

Starting Model: experimental
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This is version 1.2 of the entry. See complete history


Literature

Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII.

Kallio, J.M.Rouvinen, J.

(2011) Chem Commun (Camb) 47: 9843-9845

  • DOI: https://doi.org/10.1039/c1cc13139g
  • Primary Citation of Related Structures:  
    3QQT

  • PubMed Abstract: 

    Atomic scale experimental data by X-ray crystallography have been collected on an amphiphilic protein nanotube, consisting of a biosurfactant protein Trichoderma reesei hydrophobin HFBII.


  • Organizational Affiliation

    Department of Chemistry, University of Eastern Finland, Joensuu, Finland. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hydrophobin-2
A, B
71Trichoderma reeseiMutation(s): 0 
UniProt
Find proteins for P79073 (Hypocrea jecorina)
Explore P79073 
Go to UniProtKB:  P79073
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP79073
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.052α = 90
b = 91.359β = 90
c = 94.808γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
CCP4model building
PHASERphasing
PHENIXrefinement
XDSdata reduction
CCP4phasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-23
    Type: Initial release
  • Version 1.1: 2023-09-13
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.2: 2024-11-06
    Changes: Structure summary