The NMR structure of the submillisecond folding intermediate of the Thermus thermophilus ribonuclease H
The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H
MNPSPRKRVALFTDGAALGNPGPGTTNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKAFTEGWLEGWRKRGWRTAEGK PVKNRDLWEALLLAMAPHRVRFHFVKHHHHHH
THE RESIDUES 25-45 IN THE DATABASE SEQUENCE (RNH_THET8 P29253) WERE DELETED SINCE THIS IS THE INTERMEDIATE STATE OF THE PROTEIN. IN THIS INTERMEDIATE STATE, IT EXCLUDES THE RESIDUES 25-45, BUT STILL FOLDS WELL. ABOUT RESIDUE 17, 67, THESE CONFLICTS ARE BASED ON FOLDING, THERMAL STABILITY AND EXPRESSION.
DGSA-distance geometry simulated annealing, torsion angle dynamics
Schwieters, Kuszewski, Tjandra and Clore
submillisecond folding intermediate, Thermus thermophilus ribonuclease H, High-resolution structure, Endonuclease, Hydrolase, Magnesium, Metal-binding, Nuclease
TTNNRMELKAAIEGLKALKEPCEVDLYTDSHYLKKAFTEGWLEGWRKRGWRTAEGKPVKNRDLWEALLLAMAPHRVRFHF VK