Table 1. Data Collection and Structure Refinement Statistics.
| Data Collection | At-PPH1-SD | D180E-Phosphopeptide |
|---|---|---|
| Wavelength (Å) | 1.0000 | 1.0000 |
| Space group | P21 | P21221 |
| Cell dimensions | ||
| a, b, c (Å) | 55.40, 73.88, 82.00 | 60.29, 64.08, 100.08 |
| α, β, γ (°) | 90.00, 109.14, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 50–1.60 (1.66–1.60)a | 50–2.0 (2.07–2.0)* |
| Completeness (%) | 98.4 (97.2)a | 99.8 (100)a |
| Redundancy | 3.8 (3.7)a | 5.4 (5.5)a |
| I/σ(I) | 22.0 (2.6)a | 14.3 (4.6)a |
| Rmerge | 0.053 (0.493)a | 0.123 (0.482)a |
| Refinement | ||
| Resolution (Å) | 30–1.60 | 40–2.0 |
| Rwork/Rfree | 0.180/0.203 | 0.193/0.217 |
| No. of Atoms | ||
| All | 5177 | 2603 |
| Protein | 4589 | 2371 |
| Ligand/ion | 14 | 2 |
| Water | 574 | 230 |
| B-factor (Å2) | ||
| All | 32.4 | 24.8 |
| Protein | 31.4 | 24.3 |
| Ligand/ion | 38.8 | 11.0 |
| Water | 40.2 | 30.0 |
| Root mean square deviations | ||
| Bond lengths (Å) | 0.017 | 0.012 |
| Bond angles (°) | 1.690 | 1.835 |
| Ramachandran plot (%)b | 97.8, 2.2, 0 | 97.0, 3.0, 0 |
a
Numbers in parentheses represent the values for the highest resolution shell.
b
Percentage of amino acid residues in most favored, allowed, and outlier regions in the Ramachandran plot (showing the relationship between the two backbone dihedral angles of each amino acid residue in the protein structure).