› 2mck

Solution NMR

Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus CR6 NS1/2 protein

Released:
DOI: 10.2210/pdb2mck/pdb
PDB entry 2mck coloured by chain, ensemble of 20 models, front view.
PDB entry 2mck coloured by chain, ensemble of 20 models, side view.
PDB entry 2mck coloured by chain, ensemble of 20 models, top view.
Source organism: Murine norovirus GV/CR6/2005/USA
Primary publication:
Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.
Borin BN, Tang W, Nice TJ, McCune BT, Virgin HW, Krezel AM
Proteins 82 1200-9 (2014)
PMID: 24273131

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124852 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyprotein Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 8.03 KDa
Source organism: Murine norovirus GV/CR6/2005/USA
Expression system: Escherichia coli
UniProt:
  • Canonical: H6WEV7 (Residues: 58-114; Coverage: 3%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 66%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Advances in norovirus biology.
Karst et al. (2014)
7 more

1 mention without citation

Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.
Borin et al. (2014)