ATP STD values in complex with p38γ inactive with CSH18
| Proton . | 1H, ppm . | STD (%) ± error . | STD (%) ± error . | STD (%) ± error . |
|---|---|---|---|---|
| CSH18 = 4 μM . | CSH18 = 20 μM . | |||
| H8 | 8.51 | 1.07 ± 0.18 | 0.64 ± 0.18 | 2.02 ± 0.2 |
| H2 | 8.26 | 11.05 ± 0.36 | 9.77 ± 0.29 | 11.15 ± 0.25 |
| H1′ | 6.144 | 3.4 ± 0.34 | 1.89 ± 0.33 | 4.48 ± 0.34 |
| H1′ | 6.136 | 3.52 ± 0.33 | 2.28 ± 0.31 | 4.12 ± 0.32 |
| Proton . | 1H, ppm . | STD (%) ± error . | STD (%) ± error . | STD (%) ± error . |
|---|---|---|---|---|
| CSH18 = 4 μM . | CSH18 = 20 μM . | |||
| H8 | 8.51 | 1.07 ± 0.18 | 0.64 ± 0.18 | 2.02 ± 0.2 |
| H2 | 8.26 | 11.05 ± 0.36 | 9.77 ± 0.29 | 11.15 ± 0.25 |
| H1′ | 6.144 | 3.4 ± 0.34 | 1.89 ± 0.33 | 4.48 ± 0.34 |
| H1′ | 6.136 | 3.52 ± 0.33 | 2.28 ± 0.31 | 4.12 ± 0.32 |
STD values in the interaction of p38γ with compound CSH18. The compound competes with ATP at the ATP binding site. A competition STD experiment was conducted, measuring the STD values of 50 μM ATP in the presence of 1 μM inactive p38γ under 3 conditions: with 4 μM of compound 18, with 20 μM of compound 18, and no compound 18 added.