Table 1. Crystallographic statistics.
| C-domain ACE-Ang II peptide complex | C-domain ACE-BPPb peptide complex | |
|---|---|---|
| Resolution (Å) | 1.99 | 2.6 |
| Space group | P212121 | |
| Cell dimensions (Å; a, b, c) angle (°; α = β = γ) | 56.50, 84.66, 133.97 90 | 56.87, 85.28, 133.22 90 |
| Total/Unique reflections | 173,400/37,104 | 97,093/20,038 |
| Completeness (%) | 82.9 (79.1) | 97.7 (97.2) |
| Rsymm a | 10.8 (62.3) | 13.2 (47.9) |
| I/σ(I) | 10.7 (2.6) | 10.4 (3.5) |
| Rcrystb | 19.6 | 21.7 |
| Rfreec | 24.0 | 25.6 |
| Rmsd in bond lengths (Å) | 0.009 | 0.008 |
| Rmsd in bond angles (deg.) | 1.131 | 1.105 |
| B- factor statistics (Å2) | ||
| Protein all atoms | 19.5 | 25.3 |
| Protein main chain atoms | 19.1 | 25.3 |
| Protein side chain atoms | 19.9 | 25.2 |
| Peptide atoms | 24.9/20.7d | 24.6 |
| Solvent atoms | 26.2 | 21.2 |
| Zn2+ ion | 30.8 | n/a |
| Cl− / Acetate ions | 19.9/44.4 | 31.1/42.2 |
| Glycosylatedcarbohydrate atoms | 42.4 | 50.0 |
| PDB code | 4APH | 4APJ |
Values in parentheses are for the last resolution shell. aRsymm = ΣhΣi[|Ii(h) − <I(h)>|/ΣhΣi Ii(h)], where Ii is the ith measurement and <I(h)> is the weighted mean of all the measurements of I(h). bRcryst = Σh|Fo−Fc|/ΣhFo,where Fo and Fc are observed and calculated structure factor amplitudes of reflection h, respectively. CRfree is equal to Rcryst for a randomly selected 5% subset of reflections. dValues for conformation 1 (Asp1-Arg-Val-Tyr-Ile-His6) and 2 (Arg2-Val-Tyr-Ile-His-Pro7) respectively (with 50% occupancy for each observed peptide).