Table 1.
X-ray Crystallography Data Collection and Refinement Statistics
| Data Collection | |
| Space Group | P 32 2 1 |
| Cell Dimensions | |
| a, b, c (Å) | 88.0, 88.0, 141.6 |
| α, β, γ (°) | 90.0, 90.0, 120.0 |
| Resolution (Å) | 2.10 (2.15-2.10)* |
| Rsym/Rpim | 0.129 (0.854)/0.042 (0.269)* |
| CC ½ ϒ | 0.886 |
| I / σ | 20.6 (2.3)* |
| Completeness (%) | 100 (100)* |
| Redundancy | 10.8 (11.0)* |
| Refinement | |
| Resolution (Å) | 44.0-2.10 (2.18-2.10)* |
| Unique reflections | 37400 (3661)* |
| Rwork | 0.2022 (0.2373)* |
| Rfree± | 0.2608 (0.3270)* |
| No. atoms | |
| Protein | 5058 |
| Water | 180 |
| B-factors (Å2) | |
| Protein | 29.9 |
| Water | 28.5 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.007 |
| Bond angles (°) | 0.883 |
| Ramachandran plot | |
| Favored | 97.80% |
| Allowed | 2.20% |
| Outliers | 0.00% |
| Molprobity score ^ | 4.51 (98th percentile) |
*
Values for the corresponding parameters in the outermost shell in parenthesis.
ϒ
CC1/2 is the Pearson correlation coefficient for a random half of the data, the two numbers represent the lowest and highest resolution shell, respectively.
±
Rfree is the Rwork calculated for about 10% of the reflections randomly selected and omitted from refinement.
^
MolProbity score is calculated by combining clashscore with rotamer and Ramachandran percentage and scaled based on X-ray resolution. The percentage is calculated with 100th percentile as the best and 0th percentile as the worst among structures of comparable resolution.