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Figure 5 | BMC Structural Biology

Figure 5

From: Solution structure of the Legionella pneumophila Mip-rapamycin complex

Figure 5

Relaxation data of free and bound Mip77–213 measured at 14.1 T. 15N-relaxation as measured in a) free Mip77–213 and b) rapamycin-bound Mip77–213. HetNOEs are shown in c) for free Mip77–213 and in d) for rapamycin-bound Mip77–213. The overall R1/R2 ratio decreased upon binding of rapamycin, reflecting slower motional tumbling of the complex. Residues with HetNOE values < 0.65 (bold black lines) were not considered for calculation of the correlation time τc. For residues R-188 to G-192 HetNOE values increased and R1/R2 decreased, suggesting stabilization of these residues in the complex.

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