› 1mnl

Solution NMR

HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES

Released:
DOI: 10.2210/pdb1mnl/pdb
PDB entry 1mnl coloured by chain, ensemble of 21 models, front view.
PDB entry 1mnl coloured by chain, ensemble of 21 models, side view.
PDB entry 1mnl coloured by chain, ensemble of 21 models, top view.
Source organism: Dioscoreophyllum cumminsii
Primary publication:
Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations.
Lee SY, Lee JH, Chang HJ, Cho JM, Jung JW, Lee W
Biochemistry 38 2340-6 (1999)
PMID: 10029527

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monellin chain A Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 11.08 KDa
Source organism: Dioscoreophyllum cumminsii
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P02881 (Residues: 2-45; Coverage: 98%)
Sequence domains: Monellin
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: HYBRID GEOMETRY/DYNAMICAL SIMULATED ANNEALING CALCULATIONS
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

Sweet proteins--potential replacement for artificial low calorie sweeteners.
Kant R. (2005)
3 more

3 mentions without citation

Application of sparse NMR restraints to large-scale protein structure prediction.
Li et al. (2004)
2 more