FIGURE 3.

Combined chemical shift variations of signals between ATP-free N-MNK and ATP-free N-MNK in the presence of 3.0 equivalents of ATP. Empty columns correspond to residues whose backbone experienced significant structural changes upon ATP binding; these residues are shown in red/pink in Fig. 5B. Combined chemical shift variations are calculated from the experimental ¹H and ¹⁵N chemical shift changes (Δδ(¹H) and Δδ(¹⁵N), respectively) between corresponding peaks in the two forms, through the following equation (43), $\Delta {\delta }^{\text{combined}}=\sqrt{\frac{{\left(\Delta \delta \left({}^1\text{H}\right)\right)}^2+\frac{1}{25}{\left(\Delta \delta \left({}^{15}\text{N}\right)\right)}^2}{2}}$. The missing assignment for residue Ile¹¹¹⁹ of the ATP-free N-MNK prevented the determination of its chemical shifts perturbations. The position of secondary structure elements is shown.