TABLE 1.

Isothermal titration calorimetric data for the interaction between E6_L151V and the respective PDZ domains

Stoichiometry from stopped flow is also included (see “Results”).

Protein	ΔH	−TΔS	Kda	ΔG	Stoichiometry	Stoichiometry, stopped flow
	kcal mol−1	kcal mol−1	μm	kcal mol−1
PDZ1	−5.6 ± 0.4	−1.8 ± 0.5	1.7 ± 0.4	−7.5 ± 0.1	1.0 ± 0.1	1.5
PDZ2	−9.3 ± 0.3	0.9 ± 0.3	0.34 ± 0.02	−8.3 ± 0.1	1.3 ± 0.1	0.7
PDZ3	−9.9 ± 0.2	0.7 ± 0.3	0.08 ± 0.01	−9.2 ± 0.3	0.8 ± 0.1	0.8
PDZ12	−9.4 ± 0.5	1.4 ± 0.5	0.7 ± 0.01a	−8.0 ± 0.1	1.7 ± 0.1	2.4
PDZ23	−9.7 ± 0.1	0.7 ± 0.1	0.1 ± 0.01a	−9.0 ± 0.1	2.4 ± 0.1	1.7
PDZ123	−9.5 ± 0.6	1.4 ± 0.6	0.5 ± 0.01a	−8.2 ± 0.1	3.6 ± 0.2	2.8

^a Apparent average K_d over all binding sites.