TABLE 1.
Crystallographic X-ray diffraction and refinement statisticsa
| Characteristic (unit) | N7 | N6 | N5-LSTa | N6-laninamivir | N7-oseltamivir |
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | P4212 | P4212 | P4 | P4212 | P4212 |
| Cell dimensions | |||||
| a (Å) | 110.50 | 138.10 | 112.30 | 137.90 | 115.50 |
| b (Å) | 110.50 | 138.10 | 112.30 | 137.90 | 115.50 |
| c (Å) | 121.40 | 150.00 | 66.80 | 148.80 | 121.70 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 50–2.10 (2.18–2.10) | 50–1.80 (1.86–1.80) | 50–1.70 (1.76–1.70) | 50–1.95 (2.02–1.95) | 50–2.30 (2.38–2.30) |
| Rmerge | 0.125 (0.714) | 0.115 (0.540) | 0.146 (0.586) | 0.082 (0.320) | 0.113 (0.365) |
| I/σI | 19.29 (2.85) | 14.9 (3.1) | 16.1 (5.8) | 25.66 (7.12) | 22.59 (8.966) |
| Completeness (%) | 98.5 (91.1) | 98.1 (96.3) | 100.0 (100.0) | 99.9 (100.0) | 100.0 (100.0) |
| Redundancy | 9.4 (8.3) | 5.1 (4.6) | 8.1 (7.9) | 7.7 (7.6) | 12.8 (12.9) |
| Refinement | |||||
| Resolution (Å) | 33.59–2.10 | 47.69–1.80 | 42.96–1.70 | 47.48–1.95 | 41.89–2.30 |
| No. of reflections | 44,404 | 131,314 | 88,296 | 105,174 | 37,039 |
| Rwork/Rfree | 0.1746/0.2108 | 0.1408/0.1562 | 0.1172/0.1759 | 0.1451/0.1611 | 0.1669/0.2066 |
| No. of atoms | |||||
| Protein | 6,092 | 6,268 | 6,172 | 6,144 | 6,112 |
| Ligand/ion | 82 | 30 | 96 | 136 | 102 |
| Water | 520 | 1,056 | 743 | 846 | 463 |
| B-factors | |||||
| Protein | 26.2 | 10.9 | 14.5 | 20.2 | 24.9 |
| Water | 33.8 | 28.5 | 28.0 | 35.7 | 31.3 |
| RMSD | |||||
| Bond lengths (Å) | 0.005 | 0.006 | 0.003 | 0.008 | 0.005 |
| Bond angles (°) | 1.007 | 1.173 | 1.043 | 1.183 | 1.028 |
| Ramachandran plot | |||||
| Most favored (%) | 83.8 | 86.9 | 86.5 | 86.6 | 83.8 |
| Additionally favored (%) | 15.6 | 13.0 | 13.2 | 13.4 | 15.1 |
| Generally allowed (%) | 0.6 | 0.2 | 0.3 | 0 | 1.0 |
| Disallowed (%) | 0 | 0 | 0 | 0 | 0 |
a
Values in parentheses are for the highest-resolution shell. Rmerge = ∑|I(k) − <I(k)>|/∑I(k), where I(k) is the value of the kth measurement of the intensity of reflection and <Ik> is the mean intensity of that reflection; Rwork = ∑|Fo − Fc|/∑Fo for the 95% of the reflection data used in the refinement, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively; Rfree is the equivalent of Rwork, except that it was calculated for a randomly chosen 5% test set excluded from the refinement. I, intensity of a reflection; σI, standard deviation of intensity.