Figure 3.

ps-ns conformational dynamics in apo Alkbh5. (a) ¹⁵N R₂, R₁, and R₂/R₁ data measured at 800 MHz and 25°C are graphed versus residue index. The secondary structure calculated from the x-ray coordinates using the software MolMol (68) and the secondary structure propensity calculated from the assignment of the NMR backbone resonances using the software Talos+ (69) are shown in the uppermost panel. (b) R₂/R₁ ratios are plotted on the structure of apo Alkbh5 according to the color bar. Residues that are missing from the x-ray structure are indicated by a black curve. The Cys²³⁰–Cys²⁶⁷ disulfide bridge is shown as yellow sticks. αKG is modeled in the protein active site and shown as green spheres. To see this figure in color, go online.