Table 1 Crystallographic data collection and refinement statistics
From: Structural insights into chaperone addiction of toxin-antitoxin systems
Mtb-SecBTA/HigA1(104–116) | |
|---|---|
PDB code 5MTW | |
Data collection | |
Diffraction source | ESRF ID29 |
Space group | P212121 |
Unit cell a, b, c (Å) | 86.86, 89.96, 91.34 |
Unit cell α, β, γ (°) | 90.00, 90.00, 90.00 |
Resolution range (Å) | 64.09–1.835 (1.867–1.835)a |
No. of unique reflections | 63,188 (3135) |
Completeness (%) | 99.9 (99.6) |
Redundancy | 6.5 (6.7) |
〈I/σI〉 | 13.7 (2.3) |
R merge | 0.093 (0.796) |
CC1/2 | 0.999 (0.338) |
Refinement | |
Resolution range (Å) | 64.09–1.835 (1.883–1.835)a |
No. of reflections (work/test) | 59,790/3397 (4325/275) |
No. of molecules/AUb | 1 Mtb-SecBTA tetramer + 3 bound Mtb-HigA1(104–116) peptides |
Rwork/Rfree | 0.212/0.265 (0.330/0.354) |
Chain/no. of residues/missing residues | A/138/1–8, 43–44, 82–96, 164–181 |
B/138/1–5, 43–46, 81–96, 164–181 | |
C/138/1–12, 82–94, 114–116, 167–181 | |
D/136/1–9, 81–95, 114–115, 163–181 | |
E/12/116 | |
F/12/116 | |
G/12/116 | |
No. of nonhydrogen atoms | |
All atoms | 4660 |
Protein atoms | 4282 |
Peptide atoms | 318 |
Other ligands | 8 |
Ions | 3 |
Water molecules | 49 |
Average B-factors (Å 2 ) | |
All atoms | 34.7 |
Protein atoms | 34.3 |
Peptide atoms | 39.7 |
Other ligands | 63.5 |
Ions | 45.7 |
Water molecules | 32.6 |
RMS deviations | |
Bond lengths (Å) | 0.019 |
Bond angles (°) | 1.941 |
Ramachandran plot (%) | |
Most favored regions | 93.9 |
Allowed/disallowed | 6.1/0.0 |
