Solution Structure of Ribosomal Protein L18 of Thermus thermophilus
The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold.
RLRLSVFRSLKHIYAQIIDDEKGVTLVSASSLALKLKGNKTEVARQVGRALAEKALALGIKQVAFDRGPYKYHGRVKALA EGAREGGLEF
structures are based on 1925 NOE-derived distance restraints, 125 backbone dihedral angle restraints, 12 chi-1 angle restraints, 68 distance restraints from hydrogen bonds
simulated annealing, torsion angle dynamics
0.8 mM L18 U-15N,13C; 50 mM phosphate buffer; 200 mM LiCl
1.3 mM L18 U-15N; 50 mM phosphate buffer; 200 mM LiCl