Equilibrium dissociation constants (KD) for binding of NNIs to Δ21 and fold-shifts in KD for association to Δ55 and Δ21-Δ8 determined by SPR.

a Sensorgrams for the binding of NNIs to Δ21, Δ55 and Δ21-Δ8 along with a table of equilibrium and kinetic parameters of interaction are shown in Figure S2 and Table S1 in File S1, respectively.b Fold shift in KD for association of NNIs to Δ55 and Δ21-Δ8 was calculated relative to the KD determined for binding towards Δ21.c Where KD values could not be obtained either due to complex binding kinetics (Palm Site II inhibitor binding to Δ55 and Δ21-Δ8) or super-stoichiometric binding (Palm Site I inhibitor binding to Δ21-Δ8), numerical values have been replaced by n/a (not applicable).