Table 1 Crystallographic statistics of TARS–BC194 complex structures.
From: Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor
Human ThrRS-BC194 | |
|---|---|
Data collection | |
Space group | P2 1 |
Cell dimensions | |
a, b, c (Å) | 92.02, 134.61, 128.67 |
α, β, γ (°) | 90.00, 90.10, 90.00 |
Resolution (Å) | 50.00 – 2.80 (2.95 – 2.80)* |
Rsym or Rmerge (%) | 14.7 (88.9) |
I/sI | 5.2 (1.3) |
Completeness (%) | 100.0 (100.0) |
Redundancy | 3.2 (3.2) |
Refinement | |
Resolution (Å) | 50.00 – 2.80 (2.90 – 2.80) |
No. reflections | 76770 (7616) |
Rwork/Rfree (%) | 25.1/28.7 |
No. atoms | |
Protein | 13045 |
Ligand | 140 |
Solvent | 62 |
B-factors (Å2) | |
Protein | 56.41 |
Ligand | 49.18 |
Solvent | 46.82 |
R.m.s. deviations | |
Bond lengths (Å) | 0.007 |
Bond angles (°) | 1.149 |
Ramachandran plot | |
Most favored [%] | 96.4 |
Additional allowed [%] | 3.6 |
