Table 1.
Data collection and refinement statistics
| xtTet3 CXXC- GCCAACGTTGGC |
xtTet3 CXXC- GCCACmCGGTGGC |
|
|---|---|---|
| PDB code | 4HP3 | 4HP1 |
| Space Group | C2 | C2 |
| Cell dimensions | ||
| a, b, c (Å) | 69.9, 39.5, 54.1 | 71.0, 39.5, 57.6 |
| α, β, γ (°) | 90.0, 99.9, 90.0 | 90.0, 91.0, 90.0 |
| Resolution range (Å) | 34.42-2.05 (2.16-2.05) | 35.51-2.25 (2.37-2.25) |
| Number of unique HKLs | 9281 (1345) | 7738 (1110) |
| Completeness (%) | 99.8 (99.8) | 99.9 (100.0) |
| Friedel Redundancy | 3.7 (3.7) | 4.1 (4.2) |
| Rsym (%) | 5.3 (66.9) | 4.6 (48.7) |
| <I/σ(I)> | 12.6 (2.1) | 14.7 (2.8) |
| Resolution limits (Å) | 30.00-2.05 | 35.00-2.25 |
| Number of unique HKLs work / free | 8829 / 452 | 7385 / 351 |
| Rwork / Rfree (%) | 21.6 / 24.3 | 22.0 / 25.0 |
| Number of atoms / <B> (Å2) | 898 / 54.8 | 886 / 73.9 |
| DNA | 486 / 58.2 | 487 / 78.8 |
| Protein | 384 / 51.7 | 387 / 68.5 |
| Zn2+ | 2 / 33.2 | 2 / 46.8 |
| RMSD bonds (Å) / angles (°) | 0.013 / 1.4 | 0.012 / 1.4 |
| Ramachandran plot favored residues, no outliers (Lovell et al., 2003) |
47 of 49 | 48 of 49 |
RMSD: Root Mean Squared Deviation.
Average B-factors calculated with MOLEMAN (G.J. Kleywegt, Uppsala Univ.) The highest resolution shell is shown in parentheses.
Lovell, S.C., Davis, I.W., Arendall, W.B., de Bakker, P.I.W., Word, J.M., Prisant, M.G., Richardson, J.S., and Richardson, D.C. (2003). Structure validation by Cα geometry: ϕ,ψ and Cβ deviation. Proteins: Structure, Function, and Bioinformatics 50, 437-450.