4RHZ

Crystal structure of Cry23Aa1 and Cry37Aa1 binary protein complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.195 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history. 


Literature

The Associated Bacillus thuringiensis Binary Protein Complex of Cry23Aa1 and Cry37Aa1: Crystal Structure, Insecticidal Data, and Pore Formation Modeling.

Rydel, T.J., Sivasupramanian, S., Williams, J.M., Brown, G.R., Fu, X., Sturman, E.J., Roberts, J.K., Guzov, V.M., Seale, J.W., Moshiri, F.M., Zheng, M., Halls, C., Evdokimov, A.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cry23AA1267Bacillus thuringiensisMutation(s): 0 
Gene Names: cryET33, cry23
UniProt
Find proteins for Q9KKG8 (Bacillus thuringiensis)
Explore Q9KKG8 
Go to UniProtKB:  Q9KKG8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KKG8
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Cry37AA1126Bacillus thuringiensisMutation(s): 0 
Gene Names: cryET34
UniProt
Find proteins for Q9KKG7 (Bacillus thuringiensis)
Explore Q9KKG7 
Go to UniProtKB:  Q9KKG7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KKG7
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.195 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 126.39α = 90
b = 126.39β = 90
c = 79.234γ = 120
Software Package:
Software NamePurpose
SOLVEphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

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: 2015-10-28
    Type: Initial release