Table 2.
Crystallographic data collection and structural refinement
| JNK1–1aR-IN-8b | JNK1–1aS-IN-8b | JNK1–1a’R-IN-8b | |
|---|---|---|---|
| Data collection | |||
| Space group | P31 | P31 | P31 |
| Cell dimensions | |||
| a, b, c (Å) | 106.26, 106.26, 99.72 | 106.55, 106.55, 99.79 | 107.72, 107.72, 99.08 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution range (Å) | 46.89-2.41 | 47.00-2.70 | 47.32-2.78 |
| CC1/2 | 0.999 (0.48) | 0.999 (0.544) | 0.999 (0.518) |
| Rmergea | 0.073 (2.156) | 0.102 (2.317) | 0.094 (2.189) |
| I/σI | 16.0 (0.9) | 17.0 (1.2) | 18.0 (1.4) |
| Completeness (%) | 99.8 (98.2) | 99.9 (100.0) | 99.9 (99.9) |
| Redundancy | 10.5 (7.3) | 10.7 (10.8) | 10.8 (10.8) |
| No. reflections | 48522 | 34745 | 32333 |
| Refinement | |||
| Rwork/ Rfree | 0.2097 / 0.2262 | 0.2063 / 0.2256 | 0.2032 / 0.2179 |
| No. atoms | 8442 | 8391 | 8361 |
| Protein | 8277 | 8257 | 8215 |
| Ligand/ion | 138 | 132 | 141 |
| Water | 27 | 2 | 5 |
| B-factors (Å2) | 84.37 | 89.09 | 93.04 |
| Protein | 84.50 | 89.10 | 92.93 |
| Ligand/ion | 79.43 | 88.34 | 99.53 |
| Water | 70.25 | 66.86 | 82.87 |
| Ramachandran | |||
| Favored (%) | 97.03 % | 96.92 % | 96.00 % |
| Allowed (%) | 2.88 % | 3.08 % | 4.00 % |
| Outliers (%) | 0.10 % | 0.00 % | 0.00 % |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.007 | 0.007 | 0.006 |
| Bond angles (°) | 1.048 | 1.035 | 1.005 |
| PDB ID | 8PTA | 8PT9 | 8PT8 |
aRmerge = ΣhklΣi | Ii(hkl)-<I(hkl)>|/ΣhklΣi Ii(hkl).
bTwinning was present, -h,-k,l twinning operator was used during refinement.
Values in brackets are for the highest resolution bin.
The final crystallographic models contain three JNK1-small molecule complexes in the asymmetric unit.