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Figure 5 Comparisons of the glycine-rich loop. (a) Superposition of the glycine-rich loops of apo DAPK (beige), DAPK-ADP-Mg2+ (red) and DAPK-AMP-PNP-Mg2+ (blue) and their position relative to the nucleotide. The DAPK-AMP-PNP-Mg2+ loop has the most closed conformation. Residues 17-28 are shown for simplicity. The calculated r.m.s. deviation over the C atoms of residues 20-25 between the apo DAPK structure and the DAPK-AMP-PNP-Mg2+ structure is 1.03 Å and that between the apo DAPK and DAPK-ADP-Mg2+ structures is 0.62 Å. (b) 2Fo - Fc electron-density map at 1.0 of the glycine-rich loop of DAPK-ADP-Mg2+. One conformation of Gln23 is modeled such that the side chain is within proximity of the -phosphate (conformation B). (c) 2Fo - Fc electron-density map of the glycine-rich loop of DAPK-AMP-PNP-Mg2+. The side chain of Phe24 in the DAPK-AMP-PNP structure can be modeled in the `open' conformation (B) or a conformationally restricted position (A).