Table 1 Binding parameters from the mathematical model of the binding of the Gads SH2 domain to 2pY-LAT.

The indicated parameters were calculated from a mathematical model, based on standard equilibrium binding equations, as described in the Supplementary Materials.

Binding constant
at pTyr171 (Kd3) (nM)		First sequential constant
for binding of a single
Gads at either site
(Kd1 = 0.5 × Kd3) (nM)		Second sequential binding
constant (Kd2) (nM)		Fold increase in
site-specific binding
affinity at second
binding event due to
cooperativity (Kd3/Kd2)
WT SH217788.50.95186.5
F92D SH24722365.486.7
SourceSet equal to
pTyr171 dissociation
constant from Fig. 2E		On the basis of an
assumption of equivalence
of the two binding sites		Calculated from mathematical model of competitive
binding data from Fig. 4C