TABLE 1.
Crystallographic X-ray diffraction and refinement statistics
| Parameter | Valuea |
||
|---|---|---|---|
| P[19] VP8*-core 2 | P[19] VP8*-LNT | P[6] VP8* | |
| Data collection | |||
| Space group | C121 | P32 | H3 |
| Cell dimensions (Å) | |||
| a | 179.776 | 131.667 | 131.396 |
| b | 129.346 | 131.667 | 131.396 |
| c | 86.365 | 150.530 | 123.592 |
| α, β, γ (°) | 90, 116, 90 | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 50.00–2.10 (2.18–2.10) | 50.00–2.20 (2.28–2.20) | 50.00–1.80 (1.86–1.80) |
| Rmerge (%)b | 0.164 (1.059) | 0.115 (1.029) | 0.115 (1.156) |
| I /σI | 10.575 (1.717) | 15.231 (2.060) | 21.895 (2.750) |
| Completeness (%) | 99.9 (100.0) | 99.9 (99.7) | 100.0 (100.0) |
| Redundancy | 6.3 (6.4) | 6.0 (5.7) | 10.5 (10.6) |
| Refinement | |||
| Resolution (Å) | 49.68–2.10 | 39.91–2.20 | 41.86–1.80 |
| No. of reflections | 98,627 | 132,870 | 73,566 |
| Rwork/Rfree | 0.1812/0.2130 | 0.2261/0.2669 | 0.1663/0.1892 |
| No. of atoms | |||
| Protein | 10,270 | 17,914 | 5,260 |
| Ligand/ion | 164 | 144 | 0 |
| Water | 982 | 664 | 692 |
| B-factors | |||
| Protein | 31.06 | 35.34 | 22.44 |
| Water | 36.76 | 33.92 | 35.81 |
| Ligand | 58.60 | 54.03 | 0 |
| RMSDs | |||
| Bond lengths (Å) | 0.008 | 0.007 | 0.005 |
| Bond angles (°) | 1.056 | 0.905 | 0.921 |
| Ramachandran plot | |||
| Favored (%) | 97.0 | 95.84 | 96.2 |
| Allowed (%) | 3.00 | 4.16 | 3.64 |
| Disallowed (%) | 0.00 | 0.00 | 0.16 |
a
Values in parentheses are for the highest-resolution shell.
b
Rmerge = Σhkl |I − <I>|/ΣhklI, where I is the intensity of unique relfection hkl and <I> is the average over symmetry-related observations of unique reflection hkl; hkl are the reflection indices.