Table I.
Crystallographic data and refinement statistics
| Resolution (Å) (highest shell) | 33.0–2.61 (2.67–2.61) |
| Space group | P21 |
| Unit-cell parameters (Å, °) | a= 80.55 b=86.69 c=114.74 β=89.97 |
| Twinning fraction | 0.5 |
| Number of total reflections | 48404 |
| Number of unique reflections | 46744 |
| Rsyma (%) (highest shell) | 12.0 (58.0) |
| Completeness (%) (highest shell) | 96.6 (91.0) |
| Mean I/σ (highest shell) | 13.0 (2.30) |
| Average redundancy | 2.90 (2.60) |
| Rcryst b(%) (highest shell) | 18.2 (35.0) |
| Rfreec (%) (highest shell) | 22.4 (41.2) |
| RMSD | |
| Bond lengths (Å) | 0.007 |
| Bond angles ( ° ) | 1.17 |
| Dihedral angles ( ° ) | 16.2 |
| Number of atoms per AU | |
| Protein | 10751 |
| Ligand | 104 |
| Solvent | 174 |
a
Rsym = Σ|I − 〈I〉|/ΣI where I is the observed intensity and 〈I〉 is the average intensity of multiple symmetry-related observation of the reflection.
b
Rcryst = Σ||Fobs| − |Fcalc||/Σ|Fobs| where Fobs and Fcalc are the observed and calculated structure factors, respectively.
c
Rfree = Σ||Fobs| − |Fcalc||/Σ|Fobs| for 5% of the data not used at any stage of the refinement.