Table 1.
Data collection and refinement statistics
| Crystala | Fragment 1 | Fragment 2 | Compound 1 | Valsartan |
|---|---|---|---|---|
| Data collection | ||||
| Space group | P6422 | P6422 | P6422 | P6422 |
| Cells | ||||
| a, b, c (Å) | 111.96, 111.96, 137.18 | 111.40, 111.40 140.55 | 111.27 111.27 140.11 | 111.16 111.16 141.74 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å)b | 96.96–2.05 (2.19–2.05) | 96.50–1.85 (1.98–1.85) | 96.36–1.96 (2.14–1.96) | 96.27–1.92 (2.10–1.92) |
| Rmergec | 0.062 (2.01) | 0.053 (1.28) | 0.060 (1.489) | 0.081 (1.39) |
| I/σI | 26.9 (1.8) | 28.0 (1.5) | 24.8 (2.0) | 18.5 (1.8) |
| Completeness (%) | 85.2 (52.1) | 95.7 (74.0) | 88.6 (54.4) | 87.1 (42.0) |
| Redundancy | 19.1 (20.2) | 18.8 (11.1) | 19.5 (20.3) | 19.2 (16.9) |
| Refinement | ||||
| Resolution (Å) | 23.6–2.05 | 20.49–1.85 | 23.7–1.96 | 96.3–1.92 |
| No. of reflections | 24,779 (1224) | 36,650 (1892) | 27,571 (1441) | 29,906 |
| Rworkd | 0.239 (0.322) | 0.221 (0.213) | 0.226 (0.290) | 0.238 (0.263) |
| Rfreee | 0.256 (0.376) | 0.250 (0.287) | 0.267 (0.353) | 0.269 (0.373) |
| No. of atoms | ||||
| Protein | 2617 | 2599 | 2599 | 2593 |
| Ligand | 83 | 79 | 122 | 96 |
| Water | 48 | 88 | 175 | 160 |
| B-factors (Å2) | ||||
| Protein | 60.3 | 62 | 58.9 | 52.3 |
| Ligand | 71.5 | 64.0 | 72.4 | 64.5 |
| Water | 64.2 | 44.9 | 58.4 | 52.3 |
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.008 | 0.010 | 0.008 | 0.008 |
| Bond angles (°) | 0.86 | 0.97 | 0.88 | 0.88 |
| Ramachandran (favored, outlier [%])f | 96.9, 0.0 | 96.6, 0.0 | 97.5, 0.0 | 97.8, 0.3 |
Data sets were collected on one crystal for each complex. Values in parentheses are for highest resolution shell.
Statistics in the highest resolution bins are shown in parenthesis. Based on anisotropic scaling and merge.
Rmerge = ∑hkl∑i|Ii(hkl)−<I(hkl)>|/∑hkl∑iIi(hkl), where Ii (hkl) is the ith intensity measurement of reflection (hkl), and <I(hkl)> is the mean intensity from multiple observations of that reflection.
Rwork = ∑hkl||Fobs|−|Fcalc||/∑hkl∑|Fobs|, where Fobs and Fcalc are observed and calculated structure–factor amplitudes, respectively.
Rfree is calculated using 5% of reflections randomly excluded from refinement. For all crystals used in this study, the same set of reflections were chosen for exclusion.
Percentages of residues in the most favorable and disallowed regions of the Ramachandran plot.