Table 2.
Crystallographic data.
| Dataset | Kly18 with Mg2+ | Kly18 without Mg2+ |
|---|---|---|
| Space group / cell constants (a, b, c, in Å; β in ° if ≠90) | I4 / 82.79, 85.79, 53.48 | C2 / 121.4, 53.1, 86.3, 134.6 |
| Wavelength (Å) | 0.9790 | 0.8726 |
| No. of measurements / unique reflections | 153,136 / 21,225 | 62,645 / 15,411 |
| Resolution range (Å) (outermost shell) a | 30.3 – 1.70 (1.79 – 1.70) | 45.3 – 2.40 (2.53 – 2.40) |
| Completeness (%) | 99.0 (95.9) | 99.3 (95.9) |
| Rmerge b | 0.034 (0.121) | 0.088 (0.511) |
| Rr.i.m. (= Rmeas) b / Rp.i.m. b | 0.036 (0.139) / 0.013 (0.065) | 0.101 (0.608) / 0.050 (0.322) |
| Average intensity (<[<I> / σ(<I>)]>) | 37.1 (10.8) | 14.8 (2.5) |
| B-Factor (Wilson) (Å2) / Average multiplicity | 18.9 / 7.2 (4.4) | 38.4 / 4.1 (3.4) |
| Resolution range used for refinement (Å) | ∞ – 1.70 | ∞ – 2.40 |
| No. of reflections used (test set) | 20,403 (820) | 14,703 (708) |
| Crystallographic Rfactor (free Rfactor) b | 0.158 (0.186) | 0.189 (0.259) |
| No. of protein atoms / solvent molecules / | 1,328 / 196 / | 2,644 / 115 / |
| ligands / ions | 1 tripeptide (AFT)/ 2 Zn2+, 1 Mg2+, 1 Cl− | 1 tris, 1 tetrapeptide (AFTS) / 2 Zn2+ |
| Rmsd from target values | ||
| bonds (Å) / angles (°) | 0.006 / 1.03 | 0.013 / 1.32 |
| bonded B-factors (main chain / side chain) (Å2) | 0.46 / 1.23 | 0.60 / 1.46 |
| Average B-factors for protein / peptide ligand atoms (Å2) | 16.6 / 19.6 | 33.3 / 50.2 |
| Main-chain conformational angle analysis c | ||
| Residues in favored regions / outliers / all residues | 160 / 0 / 166 | 315 / 0 / 332 |
a
Values in parentheses refer to the outermost resolution shell.
b
For definitions, see Table 1 in (Mallorquí-Fernández et al., 2008).
c
According to MOLPROBITY (Davis et al., 2007).