Table 1 X-ray data collection and refinement statistics
From: An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering
53BP1TT-UNC2991 (PDB 6MXX) | 53BP1TT-UNC3351 (PDB 6MXY) | 53BP1TT-UNC3474 (PDB 6MXZ) | 53BP1TT-PN (PDB 6MY0) | 53BP1TT-CC (PDB 8U4U) | |
|---|---|---|---|---|---|
Data collection | |||||
Space group | P21 21 21 | P3121 | P212121 | C2 2 21 | P21 21 21 |
Cell dimensions | |||||
a, b, c (Å) | 68.94, 159.43, 181.19 | 60.57, 60,57, 138.22 | 68.67, 160.71, 182.65 | 73.10,141.27, 47.06 | 72.50, 161.83, 179.95 |
α, β, γ (°) | 90, 90, 90 | 90, 90, 120 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
Resolution (Å) | 50–2.30 (2.38–2.30)a | 50–1.62 (1.68–1.62) | 50–2.50 (2.59-2.50) | 50–2.20 (2.28–2.20) | 50–3.79 (3.93–3.79) |
Rmerge | 0.077 (1.06) | 0.074 (0.741) | 0.045 (0.436) | 0.087 (0.553) | 0.120 (0.614) |
I / σI | 21.3 (1.3) | 30.6 (2.7) | 20.5 (2.4) | 23.4 (5.3) | 15.7 (3.2) |
Completeness (%) | 97.5 (75.3) | 99.7 (98.0) | 97.2 (76.4) | 98.6 (87.4) | 89.4 (76.8) |
Redundancy | 14.0 (6.7) | 11.2 (8.0) | 6.0 (6.1) | 12.2 (11.4) | 5.7 (5.0) |
Refinement | |||||
Resolution (Å) | 2.30 | 1.62 | 2.50 | 2.20 | 3.79 |
No. of unique reflections | 87,459 | 37,781 | 68,884 | 12,596 | 19,457 |
Rwork / Rfree | 0.206 / 0.232 | 0.179 / 0.213 | 0.191 / 0.223 | 0.187 / 0.233 | 0.246 / 0.300 |
No. atoms | |||||
Protein | 10,054 | 2004 | 10,562 | 1887 | 9490 |
Ligand/ion | 302 | 46 | 221 | N/A | N/A |
Water | 411 | 348 | 667 | 129 | N/A |
B-factors | |||||
Protein | 55.90 | 19.77 | 56.25 | 27.71 | 142.67 |
Ligand/ion | 124.93 | 43.04 | 49.13 | N/A | N/A |
Water | 48.00 | 31.33 | 49.02 | 31.13 | N/A |
R.m.s. deviations | |||||
Bond lengths (Å) | 0.004 | 0.019 | 0.003 | 0.004 | 0.002 |
Bond angles (°) | 0.93 | 1.71 | 0.93 | 0.97 | 0.40 |
