Fig. 2

Inactive ERK2 interacts preferably with the D3-domain and two F-sites of hNHE1cdt. a Position of transient helices (black and dark grey bars, see panel h), TV- and LSD-boxes (light grey bars), predicted D-domains and F-sites (red bars), as well as ERK2 phosphorylation sites (stars) in the hNHE1cdt. b Combined chemical shift perturbations Δδ(¹⁵N,¹H) of WT hNHE1cdt by iaERK2 interaction. c ¹⁵N,¹H-HSQC peak intensity ratios of hNHE1cdt WT in the presence/absence of iaERK2. d Difference in relaxation rates ΔR ₂ between hNHE1cdt and NHE1cdt:iaERK2. e–g ¹⁵N,¹H-HSQC peak intensity ratios of e hNHE1cdt D3-AXA, f hNHE1cdt F1-A, and g hNHE1cdt F2-AA in the presence/absence of iaERK2. h Internally urea referenced secondary C^α chemical shifts (ΔδC^α) of WT hNHE1cdt identify the presence of several transient helices (ΔδC’ in Additional file 2: Figure S2h). ● indicate the position of prolines, □ unassigned residues, and blue box severe peak overlap