Table 1.
NMR and refinement statistics
| 53BP1-Tudor – H4K20me2 | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOEa | 2,766 |
| Intra-residue | 673 |
| Inter-residue | 2,093 |
| Sequential (|i − j| = 1) | 574 |
| Medium-range (|i − j| < 4) | 400 |
| Long-range (|i − j| > 5) | 1,019 |
| Intermolecular | 100 |
| Hydrogen bonds | 65 |
| Total dihedral angle restraints | 215 |
| φ | 75 |
| ψ | 76 |
| χ1 | 64 |
| Additional distance constraints | |
| Crystallography-based restraints b | 26 |
| Structure statistics | |
| Violations (mean ± s.d.) | |
| Distance constraints (Å) | 0.05 ± 0.04 |
| Dihedral angle constraints (°) | 1.9 ± 1.2 |
| Max. dihedral angle violation (°) | 4.26 ± 0.58 |
| Max. distance constraint violation (Å) | 0.22 ± 0.14 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.0079 ± 0.0001 |
| Bond angles (°) | 2.11 ± 0.03 |
| Impropers (°) | 1.78 ± 0.32 |
| Average pairwise r.m.s. deviationc (Å) | |
| Heavy | 1.01 ± 0.10 |
| Backbone | 0.55 ± 0.11 |
a
The number of unique non-redundant NOEs is indicated.
b
Distance restraints involving K20me2 derived from the crystal structure of 53BP1-Tudor–H4K20me2.
c
Pairwise r.m.s. deviation was calculated for residues1484–1603 of 53BP1-Tudor and residues 15–23 of the H4K20me2 peptide from an ensemble of 20 structures.