FIGURE 7.

Structural effects of activating pro-HIP/PAP mutations. A, chemical shift changes in the ¹⁵N/¹H HSQC spectra of rpro-HIP/PAP and the activated mutant rpro-HIP/PAP-EEE/AAA are plotted as a function of residue number. Chemical shift changes >0.05 ppm are indicated with the red line. The trypsin cleavage site is indicated. B, superimposed ¹⁵N/¹H HSQC spectra of ¹⁵N-labeled rpro-HIP/PAP and activating rpro-HIP/PAP mutations reveal colinear chemical shift perturbations among four residues surrounding the trypsin cleavage site at Arg³⁷/Ser³⁸. Arrows indicate the direction of larger chemical shift changes from wild-type and progression toward enhanced HIP/PAP killing activity.