2L9I

NMR structure of thymosin alpha-1


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 1000 
  • Conformers Submitted: 21 
  • Selection Criteria: 1 average structure + 20 structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

NMR structure of human thymosin alpha-1.

Elizondo-Riojas, M.A.Chamow, S.M.Tuthill, C.W.Gorenstein, D.G.Volk, D.E.

(2011) Biochem Biophys Res Commun 416: 356-361

  • DOI: https://doi.org/10.1016/j.bbrc.2011.11.041
  • Primary Citation of Related Structures:  
    2L9I

  • PubMed Abstract: 

    800 MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double β-turns in the N-terminal twelve residues which form a distorted helical structure.


  • Organizational Affiliation

    Center for Proteomics and Systems Biology, Institute of Molecular Medicine for Prevention of Human Diseases, Department of NanoMedicine and Biomedical Engineering, University of Texas Health Science Center-Houston, 1825 Pressler, Houston, TX 77030, United States.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thymosin alpha-129Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P06454 (Homo sapiens)
Explore P06454 
Go to UniProtKB:  P06454
PHAROS:  P06454
GTEx:  ENSG00000187514 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06454
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 1000 
  • Conformers Submitted: 21 
  • Selection Criteria: 1 average structure + 20 structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-12-28
    Type: Initial release