TABLE 1.
Data collection and refinement statistics of unliganded and complexed RHDVb P domain structures
| Parameter | Value(s) fora: |
||
|---|---|---|---|
| RHDVb unliganded (4X1W) | RHDVb Ley-tetra (4X1X) | RHDVb H2-tri (4X1Z) | |
| Data collection statistics | |||
| Space group | P1211 | P1211 | P212121 |
| Cell dimensions | |||
| a, b, c (Å) | 59.19, 83.13, 118.29 | 59.44, 84.15, 62.66 | 76.17, 76.21, 107.68 |
| α, β, γ (°) | 90.00, 93.21, 90.00 | 90.00, 110.11, 90.00 | 90.00, 90.00, 90.00 |
| Resolution range (Å) | 19.80–1.95 (2.02–1.95)* | 48.22–1.55 (1.61–1.55)* | 20.00–1.30 (1.35–1.30)* |
| Rmerge (%) | 16.61 (74.89)* | 6.87 (54.95)* | 6.57 (43.74)* |
| I/σ (I) | 7.82 (1.40)* | 10.85 (1.85)* | 22.20 (1.95)* |
| Completeness (%) | 99.67 (98.50)* | 98.02 (95.50)* | 98.30 (86.57)* |
| Redundancy | 4.6 (2.9)* | 3.0 (3.0)* | 13.5 (3.0)* |
| Refinement statistics | |||
| Resolution range (Å) | 19.80–1.95 | 48.22–1.60 | 20.00–1.36 |
| No. of unique reflections | 83191 | 82109 | 151410 |
| Rwork/Rfree (%) | 17.98/21.24 | 15.45/18.45 | 10.78/13.24 |
| No. of atoms | 10,593 | 5,583 | 5,773 |
| Protein | 9,665 | 4,869 | 4,856 |
| Ligand/ion | 27 | 51 | 86 |
| Water | 901 | 662 | 828 |
| Avg B factors (Å2) | |||
| Protein | 25.40 | 17.10 | 13.50 |
| Ligand/ion | 29.70 | 23.70 | 46.30 |
| Water | 30.50 | 26.60 | 26.00 |
| RMSD | |||
| Bond length (Å) | 0.005 | 0.005 | 0.007 |
| Bond angle (°) | 0.98 | 1.08 | 1.25 |
a
For RHDVb unliganded, two datasets were merged from two crystals. For RHDVb Ley-tetra, the data were collected from a single crystal. For RHDVb H2-tri, two datasets were merged from two different locations on a single crystal. Values in parentheses are for the highest-resolution shell.