Binding mode is retained in the covalent eTAFH-HEB fusion protein. (A) Overlay of ¹⁵N-¹H HSQC spectra of apo-eTAFH (red), eTAFH/HEB peptide complex (blue), and eTAFH-HEB fusion protein (green). The amides observed only when eTAFH is bound to HEB (), and the amides undergoing large chemical shift changes on HEB binding (→) are labeled with the residue number. *The peak for T321 is folded in the spectrum of eTAFH-HEB (green). (B) Backbone dynamics of eTAFH-HEB represented by plots of {¹H}¹⁵N heteronuclear NOE and R₂ relaxation rate versus residue number.