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. 2015 Jul 20;112(31):9614–9619. doi: 10.1073/pnas.1512799112

Fig. 2.

Fig. 2.

c-Myb:KIX interactions. (A and B) Primary (A) and secondary (B) c-Myb binding sites on KIX. The weighted average chemical shift differences between the free and bound KIX amide resonances are mapped onto the surface of KIX in the KIX:c-Myb:MLL ternary complex (Protein Data Bank ID 2AGH) (14). Changes in chemical shift greater than 2 × SD from the mean (red), between 1 SD and 2 SD from the mean (orange), and between mean and 1 SD from the mean (yellow) are indicated. c-Myb (residues 290–315) and MLL (residues 2,842–2,860) are shown in blue and green, respectively. (C) 15N-labeled Myb32 titration with KIX in the presence of a twofold excess of MLL28 over the KIX concentration. (D) 15N-labeled KIX titration with Myb32 in the presence of MLL28 in a twofold excess to KIX. The cross-peak color changes gradually from blue (free) to red (bound) in C and from black (free) to magenta (bound) in D according to the concentration ratios shown.