TABLE 1.
Data collection and refinement statistics for IWR compound/Tnks1 crystal structure
| Statistic | Valuea |
||
|---|---|---|---|
| TNKS1/IWR-1 | TNKS1/IWR-3 | TNKS1/IWR-8 | |
| Data collection | |||
| Space group | P 62 | P 212121 | P 62 |
| Cell dimensions | |||
| a, b, c (Å) | 107.94, 107.94, 121.92 | 48.20, 81.17, 114.16 | 108.38, 108.38, 122.22 |
| a, β, γ (°) | 90, 90, 120 | 90, 90, 90 | 90, 90, 120 |
| Resolution (Å) | 50.0–2.3 (2.34–2.30) | 31.0–1.8 (1.87–1.80) | 37.4–1.5 (1.55–1.50) |
| Rsym | 11.2 (51.3) | 7.3 (>100) | 8.3 (95.1) |
| I/σI | 15.7 (2.4) | 38.8 (1.5) | 26.3 (1.3) |
| Completeness (%) | 99.7 (94.7) | 99.3 (94.5) | 99.1 (92.0) |
| Redundancy | 7.3 (5.2) | 7.0 (6.2) | 6.2 (3.0) |
| CC1/2b at the highest-resolution shell | 0.86 | 0.84 | 0.60 |
| Refinement | |||
| Resolution (Å) | 2.30 | 1.80 | 1.50 |
| No. of reflections | 34,662 | 41,860 | 128,406 |
| Completeness (%) | 97 | 99 | 99 |
| Rwork/Rfreec (%) | 22.6/28.3 | 18.1/21.1 | 17.7/20.7 |
| No. of atoms | 7,048 | 3,522 | 7,804 |
| Protein | 6,568 | 3,262 | 6,820 |
| Ligand/ion | 128 | 44 | 163 |
| Water | 352 | 216 | 821 |
| B-factors | |||
| Protein | 43.7 | 45.7 | 22.0 |
| Ligand/ion | 40.6 | 37.3 | 26.2 |
| Water | 39.5 | 49.9 | 33.7 |
| R.m.s. deviations | |||
| Bond length (Å) | 0.004 | 0.007 | 0.007 |
| Bond angle (°) | 0.77 | 1.01 | 1.08 |
| Ramachandran plot | |||
| Favored (%) | 98.2 | 99.0 | 99.0 |
| Allowed (%) | 1.8 | 1.0 | 1.0 |
| Disallowed (%) | 0 | 0 | 0 |
a
The highest-resolution shell is shown in parentheses.
b
Pearson correlation coefficient between random half data sets.
c
Rwork/Rfree = Σ|Fobs − Fcalc|/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factor amplitudes, respectively. Rwork was calculated from data used for the refinement, whereas Rfree was calculated from the test set.