Table 1. Data Collection and Refinement Statistics of PilB Structures.
| PilB:ADP | PilB:AMP-PNP | |
|---|---|---|
| Data collection | ||
| Beamline | 08ID-1 | 08ID-1 |
| Wavelength (Å) | 0.97920 | 0.97920 |
| Space group | P3221 | P1 |
| a, b, c (Å) | 112.1, 112.1, 299.2 | 74.3, 100.0, 109.8 |
| α, β, γ (°) | 90.0, 90.0, 120.0 | 113.0, 107.7, 88.9 |
| Resolution (Å) | 46–3.40 (3.52–3.40) | 48–2.30 (2.38–2.30) |
| Total reflections | 208,303 | 253,982 |
| Unique reflections | 23,642 (375) | 120,979 (1,531) |
| Redundancy | 8.8 (10.3) | 2.1 (2.1) |
| Completeness (%) | 77 (12)* | 96 (95) |
| Mean I/σI | 12.7 (2.78) | 5.8 (2.0) |
| RSym (%)† | 21 (94) | 5.6 (43) |
| CC* (%)† | 100 (96) | 100 (88) |
| Refinement | ||
| Rwork/Rfree (%)‡ | 27.2/28.9 | 18.1/22.0 |
| R.m.s.d. | ||
| Bond lengths (Å) | 0.007 | 0.011 |
| Bond angles (deg) | 1.42 | 0.91 |
| Ramachandran plot§ | ||
| Total favoured (%) | 98 | 99 |
| Total allowed (%) | 100 | 100 |
| Coordinate error (Å)‖ | 0.38 | 0.27 |
| Atoms | 8,477 | 18,174 |
| Protein | 8,406 | 17,443 |
| Water | 12 | 533 |
| Magnesium | 2 | 6 |
| AMP-PNP | 0 | 132 |
| ADP | 54 | 54 |
| Zinc | 3 | 6 |
| Av. B-factors (Å2)§ | 87.7 | 49.3 |
| Protein | 87.9 | 49.2 |
| Water | 36.7 | 48.2 |
| Ligands | 65.6 | 63.2 |
| PDB | 5TSG | 5TSH |
Values in parentheses correspond to the highest resolution shell.
*atypical completeness of the PilB:ADP structure reflects anisotropic truncation.
†RSym=∑∑|I−(I)|/∑∑I, RPim=∑✓(1/(n−1)∑|I−(I)|/∑∑I, and CC*=✓(2CC1/2/(1+CC1/2)) where CC1/2 is the Pearson correlation coefficient of two half data sets as described elsewhere52.
‡Rwork=∑||Fobs|−k|Fcalc||/|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively. Rfree is the sum extended over a subset of reflections (5%) excluded from all stages of the refinement
§As calculated using MolProbity53.
‖Maximum-likelihood based Coordinate Error, as determined by PHENIX41.