Table I.
Data collection and refinement statistics
| Data collection and refinement statistics | Sec13–Sec16 | Sec13–Sec16 | Sec13–Sec31ΔL |
| Data collection | |||
| Data set | Native | Selenomethionine | Native |
| Space group | P212121 | P21 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 56.7, 139.0, 205.4 | 56.0, 144.1, 204.3 | 156.2, 46.6, 192.0 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 93.5, 90 |
| Wavelength (Å) | 0.9792 | 0.9792 | 0.9792 |
| Resolution range (Å) | 30.0–2.65 (2.74–2.65) | 30.0–2.70 (2.80–2.70) | 30.0–2.80 (2.87–2.80) |
| Total reflections | 168736 | 430502 | 396307 |
| Unique reflections | 45333 | 88825 | 69366 |
| Completeness (%) | 99.8 (99.4) | 99.9 (100) | 99.6 (99.4) |
| Redundancy | 3.7 (3.5) | 3.6 (3.7) | 5.7 (5.5) |
| Rmerge (%) | 7.4 (65.3) | 8.1 (56.0) | 16.4 (47.7) |
| Rr.i.m. (%) | 8.6 (80.1) | 9.9 (78.7) | 18.1 (50.0) |
| Rp.i.m. (%) | 4.4 (42.0) | 4.5 (35.8) | 7.3 (20.8) |
| I/σ | 20.7 (1.9) | 25.5 (2.7) | 9.6 (3.3) |
| Wilson B factor (Å2) | 51.6 | 49.6 | 55.7 |
| Refinement | |||
| Resolution range (Å) | 30.0–2.69 | 30.0–2.80 | |
| Rwork | 19.8 | 26.7 | |
| Rfree | 24.3 | 30.0 | |
| Twin law | −h, −k, l | ||
| Twin fraction | 0.23 | ||
| Number of reflections | |||
| Total | 44,752 | 69,353 | |
| Rfree | 2,158 | 1,792 | |
| Number of atoms | |||
| Protein | 10,476 | 19,197 | |
| Water | 184 | 0 | |
| B factors (Å2) | |||
| Protein | 103.0 | 51.8 | |
| Sec13 (chain A) | 45.8 | ||
| Sec16 (chain B) | 74.3 | ||
| Sec16 (chain C) | 111.0 | ||
| Sec13 (chain D) | 191.0 | ||
| Water | 52.0 | ||
| R.m.s deviations | |||
| Bond lengths (Å) | 0.005 | 0.006 | |
| Bond angles (°) | 0.836 | 0.936 | |
| Ramachandran plot | |||
| Favored (%) | 95.5 | 94.4 | |
| Allowed (%) | 4.3 | 5.1 | |
| Outliers (%) | 0.2 | 0.5 |
The highest resolution shell is shown in parentheses. Rmerge is the merging R factor. Rr.i.m. is the redundancy independent merging R factor. Rp.i.m. is the precision-indicating merging R factor. For definitions, see Weiss (2001).