| | GvpF |
|---|
| Data collection |
| Space group | C2221 |
| Unit cell parameters |
| a, b, c (Å) | 96.40, 147.09, 106.58 |
| α, β, γ (°) | 90.00, 90.00, 90.00 |
| Resolution range (Å) | 50.00–2.55 (2.62–2.55)a |
| Unique reflections | 24, 900 (2, 440) |
| Completeness (%) | 99.9 (100) |
| <I/σ(I)> | 16.3 (2.9) |
| Rmergeb (%) | 10.6 (69.1) |
| Average redundancy | 10.9 (10.9) |
| Structure refinement |
| Resolution range (Å) | 44.46–2.55 |
| Rfactorc/Rfreed (%) | 19.57/25.61 |
| Number of protein atoms | 3, 962 |
| Number of water atoms | 28 |
| RMSDe bond lengths (Å) | 0.015 |
| RMSD bond angles (°) | 1.709 |
| Mean B factors (Å2) | 53.189 |
| Ramachandran plot (residues, %)f |
| Most favored | 95.80 |
| Allowed | 4.00 |
| Outliers | 0.20 |
| Protein Data Bank entry | 6L5D |
- a Highest resolution shell is shown in parenthesis. Rsym = ΣhΣi|Ih,i − Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry related reflections of h. R = Σ|Fobs − Fcalc|/ΣFobs, where Fobs = Fp, and Fcalc is the calculated protein structure factor from the atomic model. RMSD in bond lengths and angles are the deviations from ideal values
