2dcp

Solution NMR

Fully automated NMR structure determination of the ENTH-VHS domain AT3G16270 from Arabidopsis thaliana

Released:
Source organism: Arabidopsis thaliana
Primary publication:
Automated protein structure determination from NMR spectra.
J Am Chem Soc 128 13112-22 (2006)
PMID: 17017791

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein MODIFIED TRANSPORT TO THE VACUOLE 1 Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.58 KDa
Source organism: Arabidopsis thaliana
Expression system: Cell free synthesis
UniProt:
  • Canonical: Q9C5H4 (Residues: 9-135; Coverage: 18%)
Gene names: At3g16270, MTV1, T02O04.23
Sequence domains: ENTH domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: Fully automated NMR spectrum analysis and structure calculation without human intervention. Chemical shift assignments and conformational restraints have not been verified manually.
Expression system: Cell free synthesis