Table 1.
Statistics of Data Collection and Structural Refinement
| Data Collection Statistics | |
|---|---|
| Ligand | AMPPNP |
| Space group | P1 |
| Unit cell | |
| a, b, c (Å) | 53.45, 99.80, 118.27 |
| α, β, γ (°) | 65.41, 90.03, 77.77 |
| Resolution (Å)a | 45.02–2.91 (3.07–2.91) |
| Number of unique reflectionsa | 46,313 (6,735) |
| Multiplicitya | 2.7 (2.7) |
| Completeness (%)a | 97.7 (97.3) |
| Rmerge (%)a | 9.0 (49.1) |
| I/σ(I)a | 9.2 (2.2) |
| Structural Refinement Statistics | |
| Resolution (Å) | 45.02–2.91 |
| Number of atoms | 13,002 |
| Rwork / Rfree (%)b | 20.04/25.51 |
| Rmsd bond length (Å)c | 0.008 |
| Rmsd bond angle (°)c | 1.132 |
| Mean B-value (Å2)d | 66.7 |
a
Values in parentheses are for the highest resolution shell.
b
The Rfree was calculated by using 5.1% data that were omitted from structural refinement.
c
The rmsd of bond lengths and angles from ideal geometry for the final model.
d
The mean temperature factor for all the atoms of the polypeptide chains in the asymmetric unit.