TABLE 1.
X-ray data collection and refinement statistics
| Enzyme | Racemate |
Pure enantiomer |
|||
|---|---|---|---|---|---|
| VX in cristallo | VR in solution | CVX in solution | VXS-(−) | VXR-(+) | |
| PDB entry code | 2XQF | 2XQG | 2XQI | 2XQK | 2XQJ |
| Data collection | |||||
| Space group | I422 | I422 | I422 | I422 | I422 |
| Unit cell axes, a = b, c (Å) | 155.1 128.1 | 154.6 127.6 | 155.2 127.0 | 154.9 127.4 | 155.8 128.3 |
| X-ray source | ID14-eh4 (λ = 0.981) | ID14-eh1 (λ = 0.933) | ID14-eh2 (λ = 0.933) | ID23-eh1 (λ = 0.954) | |
| No. of reflections | 409,037 | 249,879 | 223,406 | 214,798 | 284,598 |
| Unique reflections | 45,286 | 34,420 | 23,438 | 30,395 | 31,042 |
| Resolution (Å) | 48.0-2.1 (2.5-2.1) | 41.5-2.3 (2.5-2.3) | 49.1-2.6 (2.9-2.6) | 41.5-2.4 (2.5-2.4) | 49.3-2.4 (2.5-2.4) |
| Completeness (%) | 99.2 (98.5) | 99.7 (99.6) | 96.0 (97.7) | 99.5 (99.6) | 99.9 (99.9) |
| Rmeasa (%) | 6.8 (30.8) | 7.2 (48.8) | 15.5 (50.4) | 7.9 (48.9) | 8.1 (41.5) |
| I/ó(I) | 22.3 (7.9) | 27.3 (4.8) | 9.9 (4.1) | 20.5 (5.3) | 19.9 (6.2) |
| Redundancy | 9.0 (8.7) | 7.3 (7.4) | 9.5 (9.0) | 7.1 (6.9) | 9.2 (9.7) |
| Refinement statistics | |||||
| R-factorb (Rfree)c | 15.0 (18.9) | 16.2 (21.4) | 18.4 (24.7) | 15.7 (21.7) | 16.7 (22.3) |
| No. of atoms | |||||
| Protein | 4269 | 4258 | 4258 | 4265 | 4246 |
| Solvent | 432 | 419 | 247 | 323 | 346 |
| Others | 193 | 185 | 186 | 183 | 161 |
| Mean B-factor (Å2) | 37.1 | 38.1 | 54.0 | 41.2 | 39.7 |
| Root mean square deviation from ideality | |||||
| Bond length (Å) | 0.030 | 0.023 | 0.020 | 0.022 | 0.022 |
| Angles (deg) | 2.291 | 2.051 | 1.877 | 1.954 | 1.976 |
| Chiral (Å3) | 0.207 | 0.144 | 0.127 | 0.136 | 0.139 |
a Rmeas as defined in Ref. 31.
b R-factor = Σ |Fo − |Fc‖ / Σ |Fo|, Fo, and Fc are observed and calculated structure factors.
c Rfree set uses about 1000 of randomly chosen reflections.