Table 1.
X‐ray Data Collection and Model Refinement Statistics
| RbmB from S. ribosidificus | BtrR from B. circulans | |
|---|---|---|
| Resolution limits (Å) | 50.0–2.1 (2.2–2.1)a | 50.0–2.1 (2.2–2.1)a |
| Number of independent reflections | 48736 (6185) | 54841 (6774) |
| Completeness (%) | 99.2 (98.2) | 98.7 (95.0) |
| Redundancy | 8.3 (4.1) | 6.3 (3.1) |
| avg I/avg σ(I) | 10.3 (2.8) | 7.4 (2.1) |
| R sym (%)b | 9.2 (37.5) | 9.6 (38.2) |
| c R‐factor (overall)%/no. reflections | 18.5/45736 | 19.2/54841 |
| R‐factor (working)%/no. reflections | 18.2/46279 | 19.0/52130 |
| R‐factor (free)%/no. reflections | 23.3/2457 | 23.9/2711 |
| Number of protein atoms | 6174 | 6504 |
| Number of heteroatoms | 398 | 427 |
| Average B values | ||
| Protein atoms (Å2) | 20.7 | 23.2 |
| Ligand (Å2) | 15.2 | 18.6 |
| Solvent (Å2) | 20.3 | 23.7 |
| Weighted RMS deviations from ideality | ||
| Bond lengths (Å) | 0.012 | 0.014 |
| Bond angles (°) | 2.1 | 1.7 |
| Planar groups (Å) | 0.006 | 0.008 |
| Ramachandran regions (%)d | ||
| Most favored | 97.3 | 96.9 |
| Additionally allowed | 2.5 | 2.8 |
| Generously allowed | 0.1 | 0.2 |
a
Statistics for the highest resolution bin.
b
R sym = (∑|I – |/∑I)⋅× 100.
c
R‐factor = (Σ|F o – F c|/Σ|F o|) × 100 where F o is the observed structure‐factor amplitude and F c is the calculated structure‐factor amplitude.
d
Distribution of Ramachandran angles according to PROCHECK.17