TABLE 1.
Statistics for data collection and refinement
| Crystal parameters | ||||
| Complex | 2 | 2-HAA | 1-HAA | UDP-HAA |
| Beamline | MAXII I911-5 | MAXII I911-2 | MAXII I911-2 | ESRF ID-23-1 |
| Symmetry | C2221 | P21212 | ||
| Unit cell dimensions (Å) | ||||
| a | 152.43 | 78.17 | 78.30 | 78.10 |
| b | 48.58 | 153.25 | 153.52 | 153.67 |
| c | 78.80 | 52.72 | 52.83 | 52.50 |
| Data collection | ||||
| Resolution range (Å) | 20.0–1.75 (1.72–1.68) | 30–1.68 (1.95–1.90) | 30.0–1.9 | 20.0–1.80 (1.90–1.80) |
| Rsymb (%) | 9.4 (65.0) | 6.7 (68.8) | 12.1 (65.2) | 11.4 (65.6) |
| Completeness (%) | 99.9 (99.9) | 95.8 (90.3) | 97.5 (95.5) | 99.1 (99.4) |
| Average I/σ (I) | 15.1 (3.3) | 17.5 (2.2) | 12.6 (2.7) | 11.8 (2.5) |
| Redundancy | 7.3 (7.4) | 5.9 (4.8) | 6.0 (5.2) | 5.2 (5.3) |
| Refinement statistics | ||||
| Resolution range (Å) | 19.7–1.75 | 29.05–1.68 | 29.11/1.90 | 19.94/1.80 |
| Reflections | ||||
| Work set/Test set | 30,505/945 | 67,183/2,799 | 47,821/1,987 | 57,223/1,771 |
| No. of atoms | ||||
| Protein | 2,308 | 4,741 | 4,836 | 4,930 |
| Ligand | 43 | 124 | 126 | 112 |
| Waters | 206 | 551 | 568 | 636 |
| Glycerol | 18 | |||
| SO4 | 5 | 5 | 5 | 10 |
| Overall B-factor (Å2) | 21.9 | 21.9 | 18.1 | 17.1 |
| R.m.s. deviationc | ||||
| Bond lengths (Å) | 0.021 | 0.010 | 0.007 | 0.008 |
| Bond angles (°) | 1.884 | 1.300 | 1.049 | 1.208 |
| R-factord (%) | 14.7 | 16.4 | 15.9 | 15.1 |
| Rfree-factore (%) | 17.8 | 19.2 | 19.3 | 19.1 |
| Ramachandran plot (%) | ||||
| Most favored | 92.6 | 92.2 | 91.5 | 92.9 |
| Additionally allowed | 7.4 | 7.8 | 8.5 | 7.1 |
| Protein Data Bank ID | 3V0L | 3V0M | 3V0P | 3V0Q |
a Values in parentheses are for the highest resolution shell.
b Rsym = Σ|(I − <I>)|IΣ(I), where I is the observed intensity.
c R.m.s., root mean square.
d r = Σ‖Fobs| − | Fcalc‖Σ|Fobs|, where |Fobs| and |Fcalc| are observed and calculated structure factor amplitude.
e The Rfree value was calculated with a random 5% subset of all reflections excluded from refinement.