Table 1. Data collection and refinement statistics for NS1 effector domains.
| PDB ID | 3O9S | 3O9T | 3O9U | 3OA9 | 3O9Q | 3O9R |
| Protein | PR8 ED | PR8 ED | PR8 ED | Alb/76 ED | PR8 ED (W187A) | PR8 ED (W187A) |
| Space group | P212121 | C2221 | P64 | P61 | P3221 | P212121 |
| Cell dimensions (Å) | a = 48.71 b = 57.02 c = 101.43 | a = 72.40 b = 114.87 c = 106.42 | a = 114.12 b = 114.12 c = 199.29 | a = 47.95, b = 47.95, c = 231.54 | a = 67.52, b = 67.52, c = 158.98 | a = 33.60, b = 70.11, c = 104.26 |
| Resolution (Å)* | 2.50 (2.54–2.50) | 2.20 (2.24–2.20) | 3.20 (3.31–3.20) | 2.90 (2.95–2.90) | 2.50 (2.54–2.50) | 2.00 (2.03–2.00) |
| Rsym (%)* | 8.5 (41.6) | 4.2 (48.4) | 10.2 (59.3) | 12.4 (55.3) | 4.9 (47.2) | 6.2 (32.1) |
| I/σI * | 28.5 (4.3) | 30.0 (2.9) | 14.8 (2.8) | 19.3 (2.8) | 43.7 (3.4) | 28.7 (2.7) |
| Completeness (%)* | 92.4 (77.0) | 96.4 (80.9) | 97.2 (80.4) | 99.2 (90.6) | 99.4 (99.0) | 95.5 (63.5) |
| Unique reflections | 9692 | 22031 | 23562 | 6694 | 15144 | 16609 |
| Redundancy | 6.3 | 3.3 | 4.2 | 4.9 | 6.0 | 3.5 |
| Rwork (%) | 19.6 | 24.2 | 17.5 | 22.0 | 24.7 | 19.6 |
| Rfree (%) | 25.7 | 27.0 | 22.2 | 22.8 | 30.2 | 25.3 |
| Protein atoms | 1895 | 1869 | 7247 | 1791 | 1885 | 1836 |
| Water atoms | 102 | 28 | 0 | 16 | 30 | 206 |
| Rmsd bonds (Å) | 0.008 | 0.026 | 0.008 | 0.01 | 0.008 | 0.008 |
| Rmsd angles (°) | 1.126 | 2.004 | 1.165 | 1.344 | 1.082 | 1.048 |
| Average Bfactor | 36.0 | 42.6 | 85.8 | 41.2 | 66.0 | 30.6 |
Structures of PR8 ED-WT, PR8 ED-W187A, and Alb/76 ED-WT were solved by molecular replacement using existing PR8 and Alb/76 structures (PDB IDs 2GX9 and 3D6R).
*Values in parentheses are for highest resolution shell.