Table 1.
Data quality and refinement statistics of the crystal structures determined
| Protein | Wild type | H662A | E631Q | H662A | E631Q |
|---|---|---|---|---|---|
| Ligand | ADP | ADP | ADP | ATP | ATP |
| Crystal parameters | |||||
| Space group | C2 | C2 | C2 | P21 | P21 |
| Cell constants at 100 K | |||||
| a, b, c (Å) | 180.37, 34.84, 37.82 | 180.16, 34.77, 38.1 | 178.57, 34.75, 37.52 | 46.56, 195.17, 63.23 | 47.14, 189.26, 63.48 |
| β (deg) | 98.41 | 98.58 | 97.97 | 110.85 | 111.87 |
| Data collection and processing | |||||
| Wavelength (Å) | 1.05 | 1.05 | 1.05 | 1.05 | 1.05 |
| Resolution (Å) | 20–1.6 | 20–1.7 | 20–1.9 | 20–2.6 | 20–2.7 |
| Mean redundancy | 10.9 | 12.2 | 6.9 | 10.2 | 6.8 |
| Completeness (%) | 90.5 (69.5) | 99.2 (88.5) | 94.1 (88.1) | 96.4 (93.2) | 98.9 (98.3) |
| I/σ | 14.7 (2.1) | 26 (3.2) | 10.8 (2.3) | 12.1 (3.2) | 22.5 (5.2) |
| Rsym (%) | 8.8 (25.4) | 6.2 (16.3) | 4.9 (27.7) | 5.7 (19.3) | 9.4 (25.7) |
| Refinement | |||||
| RF (%) | 19.2 (26.8) | 20.5 (24.0) | 20.2 (29.7) | 21.1 (27.3) | 22.6 (29.3) |
| Rfree (%) | 23.1 (36.6) | 24.0 (32.0) | 25.0 (30.1) | 27.9 (37.1) | 28.0 (36.9) |
| R.m.s.d. | |||||
| Bond length (Å) | 0.013 | 0.015 | 0.013 | 0.007 | 0.012 |
| Bond angle (deg) | 1.434 | 1.498 | 1.414 | 1.085 | 1.214 |
| Average B-factor (Å2) | 30.2 | 25.1 | 37.0 | 51.0 | 51.5 |
| Ramachandran plot | |||||
| Most favored (%) | 93.5 | 93.0 | 92.0 | 90.0 | 88.7 |
| Allowed (%) | 5.6 | 6.0 | 7.1 | 8.7 | 10.2 |
| Generously allowed (%) | 0.9 | 0.9 | 0.9 | 0.9 | 0.8 |
| Disallowed (%) | — | — | — | 0.4 | 0.2 |
| Model content | |||||
| Protein residues | 242 | 243 | 243 | 964 | 964 |
| Ligands | ADP | ADP | ADP | 4 ATP | 4 ATP |
| Water molecules | 176 | 246 | 128 | 197 | 152 |
| Values in parentheses correspond to the highest resolution shell (1.65–1.6 Å for the wild-type ADP, 1.76–1.7 Å for the ADP H662A, 1.95–1.9 Å for the E631Q-ADP, 2.65–2.6 Å for the ATP H662A and 2.75–2.7 Å for the ATP E631Q structure). | |||||