TABLE 1.
Data collection and refinement statistics
| Type of data | Parametera | Valueb |
|---|---|---|
| Data collection statisticsc | a (Å) | 58.7 |
| b (Å) | 113.8 | |
| c (Å) | 79.5 | |
| β (°) | 94.6 | |
| Matthews no. | 2.4 | |
| No. of unique reflections | 17,489 | |
| Redundancy | 5 (3) | |
| Completeness (%) | 99.5 (97) | |
| Average I/σ(I) | 20.2 (2.6) | |
| Rmerge (%) | 10.0 (41.5) | |
| Wavelength (Å) | 0.91840 | |
| Refinement statisticsd | No. of protein atoms | 6,595 |
| Resolution range (Å) | 50-3.2 | |
| Rwork (%) | 24.1 | |
| Rfree (%) | 28.5 | |
| Rmsd bond distances (Å) | 0.008 | |
| Rmsd bond angles (°) | 1.003 | |
| Average B factor (Å2) | 82 | |
| Main chain (Å2) | 80 | |
| Side chain (Å2) | 84 | |
| Ramachandran plot most favored (%) | 87.2 |
a
Rmerge = Σ|Ihkl − 〈Ihkl〉|/Σ|Ihkl|. Rwork = Σ|Fobs − Fcalc|/Σ|Fobs|. Rfree is the R factor calculated from a subset of reflections excluded from refinement.
b
The values in parentheses are data for the highest-resolution shell.
c
The space group is P21.
d
The Protein Data Bank code is 1SJP.