Table 1.
Data Collection and Refinement Statistics
| DYRK1A-Inhibitora | DYRK1A-Inhibitora-Peptide | DYRK2 | |
|---|---|---|---|
| PDB ID code | 2VX3 | 2WO6 | 3K2L |
| Crystallization conditions | 4% (v/v) PEG 300, 0.1 M Li2SO4, 0.1 M Tris, pH 8.5 | 0.2 M sodium formate, 20% (w/v) PEG 3350, 10% ethylene glycol | 1.26 M (NH4)2SO4, 0.2 M Li2SO4, 0.1 M Tris, pH 8.5 |
| Space group | C2 | P65 | P42212 |
| No. of molecules in the asymmetric unit | 4 | 2 | 1 |
| Unit cell dimensions | |||
| a, b, c (Å) | 264.2, 65.1, 140.3 | 168.4, 168.4, 62.4 | 84.3, 84.3, 148.5 |
| α, β, γ (°) | 90.0, 115.44, 90.0 | 90.0, 90.0, 120.0 | 90.0, 90.0, 90.0 |
| Data Collection | |||
| Beamline | SLS X10SA | Diamond I02 | Diamond I03 |
| Resolution range (Å)b | 27.24–2.40 (2.53–2.40) | 55.13–2.50 (2.64–2.50) | 42.19–2.36 (2.49–2.36) |
| Unique observationsb | 85,770 (12,458) | 35,283 (5,093) | 22,801 (3,275) |
| Average multiplicityb | 3.4 (3.2) | 7.5 (6.9) | 6.2 (6.4) |
| Completeness (%)b | 99.9 (99.9) | 100.0 (100.0) | 99.8 (100.0) |
| Rmergeb | 0.10 (0.82) | 0.18 (0.57) | 0.08 (0.90) |
| Mean (I)/σ(I)b | 9.5 (1.9) | 10.8 (3.7) | 12.2 (2.1) |
| Refinement | |||
| Resolution range (Å) | 26.00–2.40 | 40.00–2.50 | 42.19–2.36 |
| R value, Rfree | 0.19, 0.23 | 0.19, 0.23 | 0.23, 0.29 |
| Mean protein B values (Å2) | 53 | 23.1c | 33.8c |
| Mean ligand B values (Å2) | 46 (inhibitor) | 34 (inhibitor) | |
| 71 (peptide) | |||
| Rmsd from ideal bond length (Å) | 0.014 | 0.014 | 0.014 |
| Rmsd from ideal bond angle (°) | 1.52 | 1.53 | 1.60 |
| Ramachandran outliers (%) Most favored (%) |
0.15 | 0.0 | 0.0 |
| 96.1 | 96.3 | 95.0 | |
a
The inhibitor structure is shown in Figure S2.
b
Values within parentheses refer to the highest resolution shell.
c
Residual after TLS parameterization.