Figure 3. Structural distribution of residues exhibiting amide resonance doubling due to slow conformational exchange in FKBP12.
Residues that yield doublings of their amide resonances separated by more than 0.15 p.p.m. (averaged as Δ1H and 0.2×Δ15N [63]) are indicated in red. Residues exhibiting smaller chemical shift differences between the two conformational states are indicated in magenta. Proline residues are marked in black.