Table 1. Data collection and refinement statistics for FAK/inhibitor structures.
| Compound | TAE226 | AZW592 | TAF089 | TAF672 |
| Data collection | ||||
| Space group | P21 | P21 | P21 | P21 |
| Cell dimensions | ||||
| a, b, c (Å) | 44.1, 45.2, 67.5 | 44.1, 45.6, 66.4 | 45.7, 47.1, 63.0 | 44.5, 44.9, 66.4 |
| α, β, γ (°) | 90, 94.7, 90 | 90, 95.4, 90 | 90, 98.6, 90 | 90, 95.4, 90 |
| Resolution (Å) * | 50−2.0 (2.07−2.0) | 50−2.3 (2.37−2.3) | 50−1.65 (1.70−1.65) | 50−2.6 (2.69−2.6) |
| Rmerge * | 10.7 (30.8) | 11.0 (24.4) | 9.6 (21.1) | 18.0 (29.1) |
| I/σI* | 11.2 (2.58) | 10.8 (3.36) | 13.2 (3.38) | 8.0 (3.08) |
| Completeness (%)* | 93.2 (61.0) | 92.6 (70.1) | 94.4 (59.7) | 92.1 (63.4) |
| Redundancy* | 3.9 (2.1) | 3.4 (2.6) | 4.2 (1.7) | 4.2 (3.0) |
| Refinement | ||||
| Resolution (Å) | 31.51−2.0 | 37.56−2.3 | 27.67−1.65 | 33.08−2.6 |
| No. reflections | 16 070 | 10 336 | 28 834 | 7222 |
| Rwork/Rfree | 17.9/23.6 | 20.8/27.2 | 18.8/21.7 | 21.5/26.2 |
| No. atoms | 2252 | 2194 | 2332 | 2128 |
| Protein | 2075 | 2084 | 2053 | 2064 |
| Ligand | 38 | 37 | 35 | 40 |
| Water | 139 | 73 | 244 | 24 |
| Average B-factor | 28.2 | 36.9 | 26.6 | 33.6 |
| R.m.s deviations | ||||
| Bond lengths (Å) | 0.013 | 0.010 | 0.008 | 0.013 |
| Bond angles (°) | 1.400 | 1.475 | 1.168 | 1.295 |
Each dataset was collected on one single crystal.
*
Highest resolution shell is shown in parentheses.