Extended Data Table 1.
Data collection and refinement statistics.
| σ1 bound to PD144418 (native) | σ1 bound to 4-IBP | σ1 bound to PD144418 Ta6Br12 soak | |
|---|---|---|---|
| Data collectiona | |||
| Wavelength (Å) | 1.033 | 1.033 | 1.2548 |
| Space group | P21 21 2 | P21 21 2 | P 21 21 2 |
| Number of crystals | 1 | 3 | 1 |
| Unit cell dimensions | |||
| a, b, c (Å) | 85.6, 126.1, 109.7 | 85.7, 126.8, 110.8 | 85.0, 127.4, 109.4 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 40 – 2.5 (2.65 – 2.50) | 50 – 3.2 (3.30 – 3.20) | 46.2–3.50 (3.63–3.50) |
| Completeness (%) | 98.8 (97.7) | 97.1 (97.8) | 99.0 (99.2) |
| <I/σ(I)> | 10.1 (0.9) | 5.8 (1.9) | 12.4 (3.1) |
| CC1/2 (%)f | 99.8 (40.1) | 98.0 (35.6) | 98.2 (12.9) |
| Multiplicity | 3.5 (3.4) | 3.2 (3.2) | 3.1 (3.1) |
| Refinement | |||
| Resolution (Å) | 40 – 2.51 (2.57 – 2.51) | 33.6 – 3.2 (3.28 – 3.20) | |
| No. reflections | 41026 (2000 in test set) | 19968 (1998 in test set) | |
| Rwork/Rfree (%) | 19.5/23.3 | 21.8/26.1 | |
| No. atoms | |||
| Protein | 5097 | 5027 | |
| Ligand | 63 | 69 | |
| Solvent ions/lipid | 160 | 130 | |
| Water | 136 | 0 | |
| B factors (Å2) | |||
| Protein | 79.5 | 66.5 | |
| Ligands | 84.6 | 90.2 | |
| Water | 76.8 | N/A | |
| Solvent ions/lipids | 116.8 | 96.6 | |
| RMS deviation | |||
| Bond length (Å) | 0.003 | 0.003 | |
| Bond angles (°) | 0.586 | 0.613 | |
| Ramachandran statisticsb | |||
| Favored | 98.8% | 98.4% | |
| Allowed | 1.2% | 1.6% | |
| Outliers | 0% | 0% |