Table 1.
Details of data collection and structure refinement
| ChiB–argifin | ChiB–argadin | |
|---|---|---|
| Cell dimensions, Å | a = 55.77 | a = 55.06 |
| b = 103.91 | b = 102.93 | |
| c = 186.61 | c = 185.78 | |
| Resolution range, Å | 35–2.0 (2.07–2.0) | 30–2.0 (2.07–2.0) |
| No. observed reflections | 234,279 (17,389) | 224,646 (18,204) |
| No. unique reflections | 72,253 (6,453) | 69,979 (6,563) |
| Redundancy | 3.2 (2.7) | 3.2 (2.8) |
| I/σI | 6.3 (3.1) | 9.7 (2.6) |
| Completeness, % | 96.9 (88.0) | 97.8 (93.3) |
| Rsym, % | 9.4 (34.1) | 7.6 (43.2) |
| Rcryst, % | 19.2 | 20.4 |
| Rfree, % | 23.1 | 23.1 |
| No. Rfree reflections | 722 | 1,030 |
| No. protein atoms | 7,793 | 7,794 |
| No. water molecules | 1,065 | 590 |
| No. inhibitor atoms | 96 | 96 |
| RMSD from ideal geometry | ||
| Bonds, Å | 0.008 | 0.008 |
| Angles, ° | 1.4 | 1.4 |
| B-factor rmsd, Å2 (bonded, main chain) | 1.4 | 1.5 |
| 〈Bprotein〉, Å2 | 30.2 | 35.3 |
| 〈Binhibitor〉, Å2 | 34.1 | 37.3 |
Values between brackets are for the highest resolution shell. Crystals were of space group P212121 and were cryocooled to 100 K. All measured data were included in structure refinement. rmsd, rms deviation.