1 H, 13 C and 15 N resonance assignment for barnase

The nearly complete assignment of1H,13C and15N resonances for bacterial ribonuclease barnase produced byBacillus amyloliquefaciens was obtained by standard methods of heteronuclear triple-resonance nuclear magnetic resonance spectroscopy. Analysis of the secondary chemical shifts of the backbone1Hα,13Cα and13CO nuclei reveal their strong correlation with the protein secondary structure.