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. 2013 Jul 12;453(Pt 3):371–380. doi: 10.1042/BJ20130276

Figure 3. Structural distribution of residues exhibiting amide resonance doubling due to slow conformational exchange in FKBP12.

Figure 3

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.