Table 2. NMR and refinement statistics.
| Protein | Nucleic acid | |
|---|---|---|
| NMR distance and dihedral constraints | ||
| Distance restraints | ||
| Total NOE | 487 | 115 |
| Intraresidue | 105 | 68 |
| Inter-residue | 382 | 47 |
| Sequential (|i − j| = 1) | 149 | 30 |
| Non-sequential (|i − j| > 1) | 233 | 17 |
| Hydrogen bonds | 18 | 37 |
| Hydrogen bonds protein–nucleic acid | 4 | |
| Protein–nucleic acid intermolecular | 12 | |
| Total dihedral angle restraints | ||
| Protein | ||
| ψ | 48 | |
| φ | 47 | |
| χ1 | 15 | |
| Nucleic acid | ||
| Backbone | 120 | |
| Sugar pucker | 20 | |
| RDC Q% (number of constraints) | ||
| NH | 1.0 ± 0.4 (37) | |
| Structure statistics | ||
| Violations (mean and s.d. for the complex) | ||
| Distance constraints (Å) | 0.035 ± 0.004 | |
| Dihedral angle constraints (º) | 0.34 ± 0.04 | |
| Maximum dihedral angle violation (º) | 2.2 | |
| Maximum distance constraint violation (Å) | 0.39 | |
| Deviations from idealized geometry | ||
| Bond lengths (Å) | 0.0027 ± 0.0002 | |
| Bond angles (º) | 0.546 ± 0.008 | |
| Impropers (º) | 0.32 ± 0.01 | |
| Average pairwise RMS deviationa (Å) | ||
| Protein | ||
| Heavy | 1.3 ± 0.2 | |
| Backbone | 0.7 ± 0.1 | |
| DNA | ||
| Heavy | 0.3 ± 0.1 | |
| Backbone | 0.5 ± 0.1 | |
| Complex | ||
| Heavy | 1.4 ± 0.3 | |
| Backbone | 1.2 ± 0.3 | |
| Ramachandran plot summarya | ||
| Most favored regions | 94.0% | |
| Additionally allowed regions | 5.9% | |
| Generously allowed regions | 0.1% | |
| Disallowed regions | 0.0% | |
aPairwise RMS deviation and Ramachandran plot summary was calculated among 20 refined structures for structured residues (amino acids 86–140 of MBD4MBD and base pairs 202–212 of DNA).