Table 2.
Crystallographic statistics
| Dataset | Ang − Pi | Ang − PPi | Q117G − Pi |
| Data collection statistics | |||
| Space group | P21212 | P21212 | P21212 |
| a (Å) | 86.3 | 86.0 | 85.4 |
| b (Å) | 38.5 | 37.8 | 37.5 |
| c (Å) | 33.6 | 33.0 | 38.5 |
| Resolution (Å) | 40–2.0 | 30–2.0 | 40–2.0 |
| Number of reflections measured | 38523 | 53426 | 45669 |
| Number of unique reflections | 7458 | 6973 | 8677 |
| Rsym (%) | 7.6 | 8.5 | 10.1 |
| Completeness (%) | 92.9 | 91.1 | 97.8 |
| (outermost shell) | (97.1) | (78.4) | (85.6) |
| I/σI | 13.2 | 9.6 | 6.4 |
| Refinement statistics | |||
| Rcryst (%) | 18.5 | 23.5 | 19.8 |
| Rfree (%) | 23.0 | 28.7 | 26.0 |
| Number of protein atoms | 992 | 984 | 971 |
| Number of solvent molecules | 46 | 104 | 47 |
| r.m.s. dev. in bond lengths (Å) | 0.009 | 0.009 | 0.010 |
| r.m.s. dev. in bond angles (°) | 1.4 | 1.5 | 1.6 |
| Average B-factor for protein atoms (Å2) | 24.1 | 24.8 | 24.4 |
| Average B-factor for water molecules (Å2) | 35.0 | 42.7 | 34.8 |
| Average B-factor for ligand atoms (Å2) | 52.5 | 47.2 | 48.8 |
Rsym = ∑ (|Ij − 〈I〉|).∑〈I〉 where Ij is the observed intensity of reflection j and 〈I〉 is the average intensity of multiple observations. Rcryst = ∑ ∥Fo | − | Fc ∥ /∑| Fo |, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively. 5% of the data which were used for the calculation of Rfree were excluded from the refinement.