SOLUTION STRUCTURE OF MNEI, A SWEET PROTEIN
Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin.
GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENEGFREIKGYEYQLYVYASDKLFRADISEDYK TRGRKLLRFNGPVPPP
structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy
the structures are based on a total of 1169 distance constraints, 184 dihedral angle restraints and 60 distance restraints from hydrogen bonds.
torsion angle dynamics energy restrained minimization
2mM MNEI U-15N; 18.5mM phosphate buffer K; 90% H2O, 10% D2O
2mM MNEI; 18.5mM phosphate buffer K; 90% H2O, 10% D2O
2mM MNEI; 18.5mM phosphate buffer; 100% D2O
5 stranded beta sheet 1 helix, STRUCTURAL PROTEIN