Table 1. Data collection and refinement statistics for native SaThiM, SaThiM in complex with THZ and in complex with two substrate analogues, cpd 1 and cpd 2.
| ThiM native | ThiM-THZ | ThiM-cpd 1 | ThiM-cpd 2 | |
|---|---|---|---|---|
| Data collection | ||||
| Space group | P21 | P1 | P1 | P1 |
| Cell dimensions | ||||
| a, b, c (Å) | 62.6, 103.5, 126.2 | 62.6, 62.7, 108.5 | 62.0, 62.4, 108.3 | 62.4, 62.5, 109.2 |
| α, β, γ (°) | 90.0, 99.5, 90.0 | 92.2, 91.4, 101.3 | 92.6, 91.4, 101.3 | 92.6, 92.1, 101.5 |
| Resolution (Å) | 20.0–2.09 | 20.0–1.90 | 30.0–1.87 | 30.0–1.62 |
| Rmerge | 7.8 (49.2) | 2.7 (21.1) | 6.9 (54.9) | 6.9 (51.3) |
| I/σ | 17.3 (4.2) | 21.8 (4) | 12.7 (2.5) | 10.7 (2.5) |
| Completeness (%) | 99.9 (100) | 94.7 (92.9) | 95.8 (94.7) | 93.4 (90.5) |
| Redundancy | 7.8 (7.7) | 2 (1.9) | 3.6 (3.5) | 3.6 (3.6) |
| Refinement | ||||
| Resolution (Å) | 20.0–2.09 | 20.0–1.90 | 30.0–1.87 | 30.0–1.62 |
| No. reflections | 88976 | 117078 | 119598 | 181567 |
| Rwork/Rfree | 20.34/23.04 | 18.61/20.95 | 16.86/19.90 | 18.24/20.28 |
| No. atoms | ||||
| Protein | 11474 | 11149 | 11228 | 11453 |
| Ligand | – | 54 | 66 | 54 |
| Ions | – | 4 Mg2+ | 4 Mg2+ | 5 Mg2+ |
| Water | 552 | 371 | 486 | 511 |
| B-factors | ||||
| Protein | 39.1 | 41.1 | 37.5 | 30.5 |
| Ligand | – | 43.2 | 38.1 | 24.9 |
| Ion | – | 41.2 | 44.8 | 43.6 |
| Water | 33.4 | 26.0 | 33.8 | 26.1 |
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.016 | 0.017 | 0.019 | 0.017 |
| Bond angles (°) | 1.615 | 1.598 | 1.738 | 1.699 |
*Values in parentheses are for highest-resolution shell.