Table 1.

Thermodynamic and dissociation constants for p38α:KIM-PTP domains derived from ITC experiments at 25 °C. See also Figure S2.

Interaction	Kd (nM)	ΔH (kcal·mol−1)	TΔS (kcal·mol−1)	ΔG (kcal·mol−1)
p38α : STEPKIM	3567 ± 208	−37.7 ± 2.5	−30.2 ± 2.5	−7.4 ± 0.1
p38α : STEPKIMKIS	1340 ± 135	−34.7 ± 1.4	−26.6 ± 1.5	−8.0 ± 0.1
p38α : STEP	577 ± 71	−28.8 ± 2.0	−20.3 ± 2.0	−8.5 ± 0.1
p38α : STEPF274A/F281A	1074 ± 105	−24.2± 0.4	−16.0 ± 0.4	−8.2 ± 0.1
p38α : STEPF281A/I307A	1062 ± 36	−34.3± 1.1	−26.2 ± 1.0	−8.2 ± 0.1
p38α : STEPM285A/I307A	592 ± 106	−27.6± 0.5	−19 ± 0.3	−8.5 ± 0.1
p38α : PTPSLKIM	2840 ± 135	−33.0 ± 1.7	−25.4 ± 1.7	−7.6 ± 0.1
p38α : PTPSLKIMKIS	1527 ± 23	−38.8 ± 6.1	−30.8 ± 6.1	−7.9 ± 0.1
p38α : PTPSL	382 ± 65	−30.2 ± 1.5	−21.4 ± 1.4	−8.8 ± 0.1
p38α : PSChimera	309 ± 4	−27.2 ± 0.7	−18.3 ± 0.7	−8.9 ± 0.0