Table 1. Crystallographic data collection and refinement statistics of ChREBP NLS bound structures of importin α.
| PDB CODE | Imp-α:ChREBP(6MJL) |
|---|---|
| Data Collection | |
| space group | P212121 |
| Cell Constants | |
| a (Å) | 77.434 |
| b | 89.691 |
| c | 96.332 |
| α (°) | 90.00 |
| Β | 90.00 |
| γ | 90.00 |
| Resolution (Å)a | 50.00–2.50 (2.54–2.50) |
| Rmergeb (%) | 0.049 (0.357) |
| <I/σ> | 13.2 (1.8) |
| CC1/2 | 0.750 |
| completeness (%) | 97.6 (88.6) |
| Redundancy | 3.9 (3.5) |
| Refinement | |
| Rworkc/Rfreed (%) | 19.8/24.4 |
| unique reflections | 23 621 |
| Mean B Factor (Å2) | |
| Protein | 34.15 |
| Ligand (peptide) | 41.68 |
| Solvent | 32.08 |
| Ramachandran Plot | |
| most favored (%) | 96.7 |
| add. allowed (%) | 3.1 |
| RMSD | |
| bond lengths (Å) | 0.008 |
| bond angles (degree) | 0.967 |
a
Values in parentheses are for the highest resolution shell;
b
Rmerge = Σ|I–|/ΣI where I is the integrated intensity of a given reflection;
c
Rwork = Σ|F(obs)–F(calc)|/ΣF(obs);
d
Rfree = Σ|F(obs)–F(calc)|/ΣF(obs), calculated using 5% of the data.