Table 2 Crystallographic statistics of ThrRS–BN complex structures.
From: Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase
Human ThrRS-BN | E. coli ThrRS-BN 1* | E. coli ThrRS-BN 2 † | |
|---|---|---|---|
Data collection | |||
Space group | P1 | P2 1 2 1 2 1 | P2 1 2 1 2 1 |
Cell dimensions | |||
a, b, c (Å) | 63.87, 78.00, 118.05 | 94.53, 107.64, 109.62 | 94.45, 107.62, 109.21 |
α, β, γ (°) | 86.99, 83.32, 84.39 | 90, 90, 90 | 90, 90, 90 |
Resolution (Å) | 50.00–2.60 (2.74–2.60)‡ | 50–2.10 (2.18–2.10) | 50–2.50 (2.59–2.50) |
Rsym or Rmerge (%) | 9.6 (33.2) | 11.8 (75.0) | 10.5 (51.5) |
I/sI | 5.8 (2.0) | 15.5 (2.6) | 15.1 (2.8) |
Completeness (%) | 98.1 (97.5) | 99.1 (99.8) | 94.1 (88.9) |
Redundancy | 2.2 (2.2) | 6.6 (6.5) | 5.9 (5.2) |
Refinement | |||
Resolution (Å) | 50.00–2.60 (2.69–2.60) | 50–2.10 (2.16–2.10) | 50–2.50 (2.59–2.50) |
No. of reflections | 67,853 (6794) | 63,912 (4564) | 34,852 (2457) |
Rwork/Rfree (%) | 22.8/25.5 | 20.0/21.9 | 19.8 (22.4) |
No. of atoms | |||
Protein | 12,973 | 6,536 | 6,536 |
Chain A | 3,260 | 3,262 | 3,262 |
Chain B | 3,253 | 3,274 | 3,274 |
Chain C | 3,249 | — | — |
Chain D | 3,211 | — | — |
Zn2+ | 4 | 2 | 2 |
BN | 140 | 70 | 70 |
Solvent | 390 | 656 | 381 |
B-factors (Å2) | |||
Protein | 56.38 | 24.8 | 35.8 |
Chain A | 52.40 | 25.30 | 36.41 |
Chain B | 53.85 | 24.29 | 35.24 |
Chain C | 59.82 | — | — |
Chain D | 59.51 | — | — |
Zn2+ | 51.41 | 19.84 | 28.59 |
BN | 48.78 | 17.36 | 30.03 |
Solvent | 52.10 | 34.75 | 38.96 |
Root mean square deviations | |||
Bond lengths (Å) | 0.008 | 0.012 | 0.007 |
Bond angles (°) | 1.027 | 1.220 | 1.470 |
Ramachandran plot | |||
Most favoured (%) | 98.2 | 98.0 | 98.0 |
Additional allowed (%) | 1.8 | 2.0 | 2.0 |
