Table 1.
The affinity, degree of cooperativity (σ), and thermodynamics of PKI5-24 binding with respect to the kinase saturated with the nucleotide determined from ITC. Note that some of the binding isotherms (See also Figure S1,2) do not have a sharp inflection point and the ΔH and ΔS terms are less reliable.
| Kd (μM) | σ | ΔG (kcal/mol) | ΔH (kcal/mol) | TΔS (kcal/mol) | |
|---|---|---|---|---|---|
| Apo | 6.4 ± 0.56 | 1 | −7.14 ± 0.05 | −22.03 ± 0.63 | −14.90 ± 0.68 |
| ATPγC | 6.1 ± 0.27 | 1.0 | −7.17 ± 0.02 | −13.61 ± 0.36 | −6.43 ± 0.38 |
| AMP | 5.7 ± 0.18 | 1.1 | −7.20 ± 0.02 | −20.17 ± 0.07 | −12.97 ± 0.08 |
| Adenine | 1.5 ± 0.03 | 4.3 | −8.00 ± 0.01 | −19.43 ± 0.16 | −11.43 ± 0.18 |
| Adenosine | 0.53 ± 0.02 | 12 | −8.63 ± 0.02 | −21.32 ± 0.18 | −12.69 ± 0.20 |
| ADP | 0.23 ± 0.0097 | 29 | −9.13 ± 0.03 | −17.67 ± 0.35 | −8.54 ± 0.37 |
| ATPγN | 0.12 ± 0.0050 | 53 | −9.49 ± 0.02 | −18.12 ± 0.27 | −8.64 ± 0.30 |
| ATP | 0.016 ± 0.0019 | 400 | −10.72 ± 0.07 | −11.90 ± 0.34 | −1.17 ± 0.38 |