Table 1.
Crystallographic summary of WT-PI5P4Kβ
| Apo | WT- AMP |
WT- GMP |
WT-AMPPNP | WT-GMPPNP | |
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | C2221 | C2221 | C2221 | C2221 | C2221 |
| Cell dimensions | |||||
| a, b, c (Å) | 107.1, 182.4, 105.4 90.0, |
108.4, 181.8, 107.6 90.0, |
108.8, 183.2, 106.8 90.0, |
108.6, 183.0, 106.0 90.0, |
109.8, 185.2, 106.5 90.0, |
| α, β,γ (°) | 90.0, 90.0 |
90.0, 90.0 |
90.0, 90.0 |
90.0, 90.0 |
90.0, 90.0 |
| Resolution (Å)* | 69.47– 2.60 (2.74– 2.60) |
70.41– 2.15 (2.27– 2.15) |
46.76– 2.45 (2.58– 2.45) |
91.49–2.70 (2.85–2.70) |
94.45–2.60 (2.74–2.60) |
| Rmerge(%) | 3.8 (41.4) | 3.1 (45.0) | 4.2 (59.5) | 2.5 (39.6) | 3.1 (48.5) |
| I /σI | 27.7 (3.7) | 27.9 (3.4) | 21.4 (2.6) | 37.5 (3.8) | 29.3 (3.2) |
| Completeness (%) | 99.6 (100.0) |
97.5 (95.7) |
99.2 (99.9) |
98.6 (99.5) | 97.9 (99.8) |
| Redundancy | 3.8 (3.8) | 3.8 (3.7) | 3.8 (3.8) | 3.8 (3.8) | 3.7 (3.6) |
| Refinement | |||||
| Resolution (Å) | 52.70– 2.60 |
48.40– 2.15 |
46.76– 2.45 |
53.18–2.70 | 94.45–2.60 |
| No. reflections | 32017 | 56883 | 39252 | 29012 | 33027 |
| Rwork / Rfree (%) | 21.1/26.0 | 24.6/27.9 | 22.4/25.5 | 23.4/28.0 | 22.9/27.7 |
| No. atoms | |||||
| Protein | 5162 | 5063 | 5111 | 5284 | 5035 |
| Ligand/ion | 0 | 140 | 120 | 141 | 128 |
| Water | 51 | 106 | 42 | 25 | 17 |
| B-factors | |||||
| Protein | 71.9 | 69.6 | 77 | 97.9 | 83.7 |
| Ligand/ion | - | 74.5 | 74.1 | 125 | 114.8 |
| Water | 45.6 | 47.2 | 50.3 | 50.2 | 54 |
| R.m.s deviations | |||||
| Bond lengths (Å) | 0.009 | 0.012 | 0.009 | 0.019 | 0.01 |
| Bond angles (°) | 1.149 | 1.182 | 1.223 | 2.381 | 1.236 |
| PDB ID | 3WZZ | 3X01 | 3X02 | 3X03 | 3X04 |
Each structure was determined from single-crystal diffraction.
*
Highest resolution shell is shown in parenthesis.