TABLE 2.
Crystallographic data
|
Form 1 - SeMet
|
Form 2 (native)
|
|||
|---|---|---|---|---|
| Peak | Inflection | Remote | ||
| Diffraction data | ||||
| Space group | P21 | P21 | P21 | P212121 |
| Cell dimensions | ||||
| a, b, c (Å) | 39.51, 94.65, 63.17 | 39.51, 94.65, 63.17 | 39.51, 94.65, 63.17 | 38.94, 62.50, 82.47 |
| α, β, γ (°) | 90, 90.55, 90 | 90, 90.55, 90 | 90, 90.55, 90 | 90, 90, 90 |
| Wavelength (Å) | 0.97942 | 0.97959 | 0.95446 | |
| Resolution (Å) | 50.00-1.80 (1.86-1.80) | 50.00-1.90 (1.97-1.90) | 50.00-1.86 (1.94-1.86) | 50.00-1.80 (1.86-1.80) |
| Avg I/σI | 10.5 (1.5) | 19.2 (2.2) | 13.5 (2.6) | 12.5 (2.2) |
| Rsymm | 0.115 (0.540) | 0.112 (0.488) | 0.131 (0.665) | 0.069 (0.376) |
| Completeness (%) | 99.8 (87.5) | 99.0 (97.6) | 98.4 (97.1) | 96.1 (88.3) |
| Average redundancy | 3.6 (2.5) | 3.6 (3.0) | 3.5 (2.9) | 2.9 (2.5) |
| Refinement | ||||
| Resolution (Å) | 50.0-1.80 | 50.0-1.80 | ||
| No. reflections | 39950 | 17702 | ||
| Rwork/Rfree | 0.171/0.200 | 0.195/0.237 | ||
| No. atoms | ||||
| Protein | 3888 | 1926 | ||
| Ligand/ion | 2 | 14 | ||
| Water | 482 | 168 | ||
| B-factors (Å2) | ||||
| Protein | 17.2 | 22.9 | ||
| Ligand-ion | 22.7 | 48.2 | ||
| Water | 29.9 | 33.6 | ||
| R.m.s deviations | ||||
| Bond lengths (Å) | 0.009 | 0.008 | ||
| Bond angles (°) | 1.204 | 1.181 | ||