Table 1.
Statistics of reflection data and structure refinements. Liganding denotes the states in the 2-Kinase/2-Phosphatase. His-P is phosphorylated at His258. Rsym = Σh(Σj|Ih,j - <Ih>|/ΣIh,j), where h=set of Miller indices, j=set of observations of reflection h, and <Ih>=the mean intensity. RMSD values are deviations from ideal values. Rcrys = Σh || Fo,h | - |Fc,h || / Σh |Fo,h|. Rfree was calculated using 5% of the complete data set randomly excluded from refinement. The numbers in parentheses represent values from the highest resolution shell.
| Orthologue | Human | Bovine |
|---|---|---|
| Liganding | ATP•Citrate/His-P•F6P | ADP•Citrate/His-P•Citrate |
|
| ||
| Space Group | P212121 | C2221 |
|
| ||
| Unit Cell Dimensions (Å) | 106.5 × 113.9 × 133.2 | 82.1 × 169.5 × 85.3 |
|
| ||
| Resolution Range (Å) | 38.55-2.01 | 46.54 – 1.82 |
|
| ||
| Reflections [F ≥ σ(F)] | 106633 | 52149 |
|
| ||
| Completeness (%) | 0.98 (87.3) | 97.0 (81.5) |
|
| ||
| Redundancy | 4.2 (3.4) | 10.9 (10.9) |
|
| ||
| I/σ (I) | 16.2 (2.3) | 2.62 (1.82) |
|
| ||
| Rsym | 0.059 (0.420) | 0.050 (0.284) |
|
| ||
| Rcrys | 0.1490 | 0.1392 |
|
| ||
| Rfree | 0.1751 | 0.1623 |
|
| ||
| No. of Amino Acids | 840 | 423 |
|
| ||
| No. of Protein Atoms | 6925 | 3461 |
|
| ||
| No. of Hetero Atoms | 194 | 62 |
|
| ||
| RMSD | ||
| Bond Lengths (Å) | 0.016 | 0.009 |
| Angles (°) | 1.40 | 1.319 |
| Dihedral Angles (°) | 16.747 | 13.806 |
|
| ||
| Mean B factor | 39.70 | 25.82 |
| Protein Atoms (Å2) | 39.00 | 24.60 |
| Hetero Atoms (Å2) | 42.97 | 22.84 |
| Water Atoms (Å2) | 45.53 | 34.59 |