TABLE 1.
X-ray crystal diffraction data collection and refinement statistics
| GH84C-CBM | GH84C catalytic | Coh-FN3 | |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | I212121 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 46.85, 69.54, 136.78 | 130.39, 150.05, 155.43 | 148.25, 48.64, 36.90 |
| α, β, γ (°) | 90.00, 95.78, 90.00 | 90.00, 90.00, 90.00 | 90.00, 96.19, 90.00 |
| Resolution (Å) | 20.00-3.30 (3.39-3.30)a | 20.00-2.10 (2.15-2.10) | 20.00-1.80 (1.86-1.80) |
| Rmerge | 0.114 (0.287) | 0.103 (0.397) | 0.030 (0.170) |
| I/σI | 4.4 (2.2) | 12.4 (4.8) | 30.0 (8.0) |
| Completeness (%) | 92.8 (94.7) | 99.9 (100.0) | 95.7 (77.9) |
| Redundancy | 2.5 (2.5) | 16.1 (15.7) | 7.1 (6.1) |
| Refinement | |||
| No. reflections | 31,497 | 1,384,042 | 166,316 |
| Unique reflectionsb | 12,420 | 85,965 | 23,338 |
| Rwork/Rfree | 0.325/0.370 | 0.198/0.255 | 0.224/0.294 |
| No. atoms | |||
| Protein | 5,677 | 4,644 (A); 4,632 (B) | 1750 |
| Ligands | 3 (Ca) | 4 (Ca); 3 (Na); 25 (CAC) | 4 (ACT) |
| Water | 28 | 1,195 | 318 |
| B-factors (Å2) | |||
| Protein | 52.8 | 29.3 (A); 32.1 (B) | 28.3 |
| Ligands | 71.8 (Ca) | 44.3 (Ca); 22.0 (Na); 71.7 (CAC) | 30.2 (ACT) |
| Water | 27.5 | 34.3 | 38.7 |
| r.m.s.d. | |||
| Bond lengths (Å) | 0.006 | 0.010 | 0.018 |
| Bond angles (°) | 0.934 | 1.389 | 1.732 |
| Ramachandran statistics (%) | |||
| Favored | 84.1 | 90.4 | 91.6 |
| Allowed | 15.5 | 9.7 | 8.4 |
| Disallowed | 0.5 | 0.0 | 0.0 |
a
Values in parentheses are for the highest resolution shells.
b
All F > 2σF.