FIGURE 3.

The majority of pyrin PYD mutant proteins retain structural integrity. A–F, overlay of the two-dimensional ¹H-¹⁵N HSQC spectra of wild-type (black) and mutant (red) pyrin PYD proteins E14A, E22A, R42A, E63A, R75A, and R80A, respectively. All spectra were recorded in 50 mm sodium phosphate, pH 4, and 150 mm NaCl at 25 °C. Residues that show chemical shift changes are indicated with the one-letter amino acid code and sequence number. Horizontal lines connect peaks corresponding to side chain NH₂ groups of Asn and Gln residues that exhibit changes in chemical shifts. G–L, ribbon diagrams of the pyrin PYD structure showing residues with their chemical shifts perturbed by the E14A, E22A, R42A, E63A, R75A, and R80A mutations, respectively. Mutated residues are colored red, and residues with chemical shift changes are colored orange, and their side chains are shown.