Table 2. Data collection and refinement statistics.
| Native dataset | |
|---|---|
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 43.619, 73.653, 46.460 |
| α, β, γ (°) | 90, 106.596, 90 |
| Resolution (Å)a | 44.5–2.1 (2.22–2.10) |
| Total reflections | 60 325 |
| Unique reflections | 15 711 |
| Rsym or Rmerge (%)b | 0.060 (0.438) |
| I/σI | 14.6 (3.3) |
| Completeness (%) | 95.6 (93.3) |
| Redundancy | 3.8 (3.9) |
| Refinement | |
| Resolution (Å) | 45.0–2.1 |
| No. reflections | 15 656 |
| Rwork/Rfreec | 20.0, 0.26.0 |
| Number of atoms | |
| Protein | 2117 |
| Water | 130 |
| B-factors | |
| Protein | 34.26 |
| Water | 35.40 |
| RMS deviationsd | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 0.918 |
| PDB code | 5L7A |
a
Highest resolution shell is shown in parenthesis.
b
Rm:ΣhΣi|I/(h, i) – I(h)|/ΣhΣi/I(h, i) where I(h, i) are symmetry-related intensities and I(h) is the mean intensity of the reflection with unique index h.
c
R-factor = Σ(|Fobs| – k|Fcalc|)/Σ|Fobs| and R-free is the R value for a test set of reflections consisting of a random 5% of the diffraction data not used in refinement.
d
RMS deviations from ideal geometry for bond lengths and restraint angles (Engh and Huber).