1IDZ

STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 120 
  • Conformers Submitted: 20 
  • Selection Criteria: 0.1 ANGSTROM MAXIMUM DISTANCE VIOLATION 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy.

Furukawa, K.Oda, M.Nakamura, H.

(1996) Proc Natl Acad Sci U S A 93: 13583-13588

  • DOI: https://doi.org/10.1073/pnas.93.24.13583
  • Primary Citation of Related Structures:  
    1IDY, 1IDZ

  • PubMed Abstract: 

    A small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure.


  • Organizational Affiliation

    Biomolecular Engineering Research Institute, Osaka, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 354Mus musculusMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P06876 (Mus musculus)
Explore P06876 
Go to UniProtKB:  P06876
IMPC:  MGI:97249
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06876
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 120 
  • Conformers Submitted: 20 
  • Selection Criteria: 0.1 ANGSTROM MAXIMUM DISTANCE VIOLATION 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-12-23
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references, Derived calculations, Other, Structure summary