. Author manuscript; available in PMC: 2017 Mar 1.

Published in final edited form as: Structure. 2016 Jan 28;24(3):353–363. doi: 10.1016/j.str.2015.11.016

Table 2.

The affinity, degree of cooperativity (σ), and thermodynamics of PKI_5-24 binding with respect to the kinase saturated with the ATP-competitive inhibitor determined from ITC.

	K_d (μM)	σ	ΔG (kcal/mol)	ΔH (kcal/mol)	TΔS (kcal/mol)
Balanol	0.92 ± 0.13	7.0	−8.30 ± 0.09	−16.14 ± 0.56	−7.83 ± 0.65
H89	11.2 ± 0.75	0.57	−6.81 ± 0.04	−18.46 ± 0.62	−11.65 ± 0.60