Table S1.
Crystallographic statistics
| Data collection | Native | AMP-PNP | AMP-PNP/selenate |
| Wavelength, Å | 1.075 | 1.075 | 0.9788 |
| Cell dimensions, Å | a = b = 88.9, c = 154.6 | a = b= 87.9, c = 156.5 | a = b = 88.1, c = 155.8 |
| Resolution,* Å | 40–3.1 (3.2–3.1) | 40–3.3 (3.4–3.3) | 40–3.6 (3.7–3.6) |
| Redundancy,* | 9.3 (9.7) | 9.3 (9.6) | 13.6 (14.0) |
| Completeness,* % | 99.6 (100) | 99.5 (99.3) | 100 (100) |
| <I/σ>* | 11.3 (1.2) | 9.9 (2.8) | 5.5 (5.2) |
| Rmerge*,† | 0.073 (0.678) | 0.078 (0.898) | 0.152 (0.584) |
| Refinement | |||
| Unique reflections | 11,844 | 9,831 | 7,655 |
| No. of atoms | |||
| Protein | 2,327 | 2,268 | 2,268 |
| Ligand | — | 36 | 45 |
| Rwork/Rfree‡ | 0.210/0.273 | 0.204/0.272 | 0.202/0.262 |
| B-factor, Å2 | 83 | 103 | 84 |
| rmsd | |||
| Bond lengths, Å | 0.014 | 0.012 | 0.010 |
| Bond angles, ° | 1.863 | 1.746 | 1.568 |
Space group is P43212.
*
Highest resolution shell is shown in parentheses.
†
Rmerge = ∑ | Ii - <I> |/∑ Ii.
‡
Rwork = ∑ | Fo – Fc |/∑ Fo. Rfree is the cross-validation R factor for the test set of reflections (5% of the total) omitted in model refinement.