Table 5.
Data collection and refinement statistics for determined VCNA-inhibitor complex structures.
| Oseltamivir Carboxylate | Zanamivir | |
|---|---|---|
| Data Collection | ||
| Space group | P212121 | C121 |
| Cell dimension | ||
| a, b, c (Å) | 71.76, 77.86, 163.48 | 190.55, 50.34, 86.09 |
| α, β, γ (˚) | 90, 90, 90 | 90, 107.24, 90 |
| Resolution (Å) | 44.33–1.87 (1.94–1.87) * | 46.00–1.75 (1.81–1.75) |
| Rmerge (%) | 10.1 (49.6) | 4.4 (47.8) |
| <I/σ(I)> | 10.2 (2.4) | 14.7 (1.8) |
| Completeness (%) | 99.2 (97.9) | 97.8 (96.8) |
| Multiplicity | 3.7 (3.5) | 2.3 (2.2) |
| Refinement | ||
| Resolution (Å) | 44.33–1.87 | 46.00–1.75 |
| No. reflections | 282260 | 176727 |
| Rwork/Rfree (%) | 16.31/20.44 | 16.69/20.29 |
| No. atoms | 6632 | 6569 |
| Protein | 5834 | 5852 |
| Ligand/ion | 42 | 57 |
| Water | 756 | 660 |
| Average B-factor (Å2) | ||
| Overall | 24.3 | 32.0 |
| Protein | 23.4 | 31.3 |
| Ligand/ion | 22.7 | 36.0 |
| Water | 31.9 | 38.0 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.010 | 0.007 |
| Bond angles (˚) | 1.18 | 1.05 |
One single-crystal was used to collect a complete dataset for every structure. * Highest resolution shell is shown in parenthesis.