Table 1.
Statistics of data collection and refinement
| Structure | AimR (PDB: 6JG5) | AimR–peptide (PDB: 6JG9) | AimR–DNA (PDB: 6JG8) |
|---|---|---|---|
| Data collection | |||
| Space group | P2 1 2 1 2 | P2 1 2 1 2 | P4 1 |
| Unit cell dimensions | |||
| a, b, c (Å) | 33.49, 115.30, 219.43 | 33.59,120.93, 214.0 | 98.01, 98.01, 159.99 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Wavelength (Å) | 0.9792 | 0.9778 | 0.9792 |
| Resolution (Å) | 45–2.22 (2.29–2.22) | 45–2.0 (2.05–2.0) | 45–2.1 (2.13–2.10) |
| Rmerge (%) | 10.9 (34.1) | 7.1 (38.9) | 4.1 (68.9) |
| I/σ(I) | 10.9 (4.9) | 17.8 (4.2) | 23.4 (3.1) |
| Completeness (%) | 99.1 (96.0) | 99.8 (96.2) | 99.7 (98.5) |
| Number of measured reflections | 276,186 | 396,286 | 600,917 |
| Number of unique reflections | 42,901 | 60,685 | 87,895 |
| Redundancy | 6.4 (6.2) | 6.5 (6.2) | 6.8 (7.0) |
| Wilson B factor (Å2) | 24.9 | 23.8 | 44.4 |
| Refinement | |||
| Rwork/Rfree (%) | 19.62/23.94 | 21.35/24.88 | 21.06/22.30 |
| Number of atoms | |||
| Protein main chain | 3120 | 3116 | 3116 |
| Protein side chain | 3304 | 3279 | 3313 |
| Protein all atoms | 6424 | 6395 | 6429 |
| Water molecules | 329 | 406 | 257 |
| Other entities | 0 | 80 | 1227 |
| All atoms | 6753 | 6872 | 7913 |
| Average B value (Å2) | |||
| Protein main chain | 36.8 | 42.1 | 54.8 |
| Protein side chain | 41.6 | 46.0 | 62.4 |
| Protein all atoms | 39.2 | 44.1 | 58.7 |
| Water molecules | 39.8 | 25.4 | 57.3 |
| Other entities | 0 | 42.9 | 79.4 |
| All atoms | 39.3 | 43.8 | 61.9 |
| R.M.S. deviations from ideal values | |||
| Bonds (Å) | 0.009 | 0.010 | 0.009 |
| Angle (°) | 0.956 | 1.094 | 1.067 |
| Ramachandran plot statistics (%) | |||
| Most favorable | 93.2 | 94.4 | 92.1 |
| Additionally allowed | 6.8 | 5.6 | 7.8 |
| Generously allowed | 0 | 0 | 0.1 |
| Disallowed | 0 | 0 | 0 |
Values in parentheses are for the highest resolution shell. Rmerge = ΣhΣi|Ih,i − Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry-related reflections of h. R = Σ|Fobs − Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections selected)