Table 2.
Statistics of structure refinement
| Ligand complex | BMS270394 | BMS270395 |
|---|---|---|
| Refinement resolution, Å | 15–1.59 | 6–1.67 |
| Observations | 37,646 | 32,478 |
| Residuals | ||
| Rfree, % (5% of reflections) | 25.0 | 24.3 |
| Rcryst, % | 20.9 | 17.9 |
| Model | ||
| Protein atoms | 2,167 | 2,151 |
| Water molecules | 327 | 276 |
| Ligand atoms | 29 | 29 |
| Detergent atoms | 35 | 35 |
| Double conformations | 12 | 11 |
| Bavg, Å2 protein atoms | 25.0 | 23.5 |
| Bavg, Å2 water molecules | 43.4 | 37.8 |
| Bavg, Å2 ligand atoms | 17.8 | 16.7 |
| Bavg, Å2 detergent atoms | 47.0 | 53.5 |
| Stereochemistry | ||
| rmsd bond length, Å | 0.012 | 0.009 |
| rmsd bond angles, ° | 1.635 | 2.160 |
| rmsd improper angles, ° | 0.078 | 1.451 |
| rmsd dihedral angles, ° | 25.83 | 27.27 |
| Ramachandran plot, regions | ||
| Most favored, % | 95.1 | 93.7 |
| Additionally allowed, % | 4.9 | 6.3 |
Overview of data collection statistics for the ligand complexes of the hRARγ LBD, bound to BMS270394 and BMS270395, respectively. Values in parentheses correspond to the highest-resolution shell. Because of the limited crystal size obtained for the BMS270395 complex, a preliminary data set was collected at the microfocus beamline ID13, ESRF. One further data set was collected on BM14 with the only available bigger crystal. Rsym(I) = Σhkl Σi | Ihkl, i − 〈Ihkl〉 |/Σhkl Σi | Ihkl, i |, with 〈Ihkl〉 mean intensity of the multiple Ihkl, i observations for symmetry-related reflections. rmsd, rms deviation.