TABLE 1.
Data collection and structure refinement
r.m.s.d., root mean square deviation.
| ClpP1P2 with Bz-Leu-Leu | ClpP1P2 with Z-Leu-Leu | |
|---|---|---|
| Data collection | ||
| Space group | C2 | C2 |
| Molecules/asymmetric unit | 2 (28 chains) | 2 (28 chains) |
| Unit cell a, b, c (Å); β | 205.94, 183.35, 188.45; 94.44° | 205.18, 183.54, 188.37; 94.53° |
| Resolution (Å) | 100.0-3.07 (3.15-3.07)a | 50.0-2.9 (2.95-2.9) |
| Rmergeb (%) | 10.5 (66.6) | 9.1 (80.4) |
| No. of reflections (measured/unique) | 545,500/129,368 | 560,142/147,557 |
| 〈I /σI〉 | 11.33 (2.29) | 14.1 (1.2) |
| Completeness (%) | 99.5 (100) | 94.6 (84.9) |
| Redundancy | 4.22 (4.29) | 3.8 (2.9) |
| Refinement | ||
| Resolution (Å) | 72.2-3.07 | 49.27-2.9 |
| No. of reflections (refinement/Rfree) | 115,022/6,092 | 143,061/4,469 |
| R / Rfreec | 0.197/0.231 | 0.202/0.234 |
| No. atoms | ||
| Protein | 40,432 | 40,563 |
| Ligands | 490 | 0 |
| Water | 53 | 105 |
| r.m.s.d. from ideal targets | ||
| Bond lengths (Å) | 0.016 | 0.018 |
| Bond angles (°) | 1.94 | 1.99 |
| PDB accession code | 5DZK | 5E0S |
a The highest resolution shell is shown in parentheses.
b Rmerge = ΣhΣi|Ii − 〈I〉|/ΣhΣiIi, where Ii is the observed intensity of the ith measurement of reflection h, and 〈I〉 is the average intensity of that reflection obtained from multiple observations.
c R = Σ‖Fo| − |Fc‖/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively, calculated for all data. Rfree was defined in Ref. 56.