Table 1. Structural statistics of the YT521-B YTH domain in complex with 5′-UGm6ACAC-3'.
| NMR restraints | |
| Distance restraints | 4760 |
| Protein intramolecular | 4497 |
| intraresidual | 915 |
| sequential (|i − j | =1 ) | 1008 |
| medium range (1 < |i − j | < 5) | 895 |
| long range (|i − j | ≥ 5) | 1644 |
| hydrogen bondsa | 35 |
| RNA intramolecular | 49 |
| intraresidual | 30 |
| sequential (|i − j | =1) | 19 |
| Complex intermolecular | 214 |
| Torsion anglesb | 241 |
| Protein backbone | 234 |
| RNA sugar pucker (DELTA) | 6 |
| RNA base conformation (CHI; syn) | 1 |
| Energy statisticsc | |
| Average distance constraint violations | |
| 0.1–0.2 Å | 65.2 ± 4.7 |
| 0.2–0.3 Å | 6.1 ± 2.3 |
| 0.3–0.4 Å | 0.6 ± 0.7 |
| > 0.4 Å | 0.1 ± 0.3 |
| Maximal (Å) | 0.32 ± 0.06 |
| Average angle constraint violations | |
| < 5° | 29.3 ± 2.7 |
| > 5° | 0.0 ± 0.0 |
| Maximal (°) | 0.51 ± 0.07 |
| Mean AMBER constraint violation energy (kcal mol−1) | 53.2 ± 2.7 |
| Distance (kcal mol−1) | 52.6 ± 2.7 |
| Torsion (kcal mol−1) | 0.6 ± 0.1 |
| Mean AMBER energy (kcal mol−1) | −5040.4 ± 11.4 |
| Mean deviation from ideal covalent geometry | |
| Bond length (Å) | 0.0036 ± 0.0000 |
| Bond angle (°) | 1.706 ± 0.007 |
| Ramachandran plot statisticsc,d,e | |
| Residues in most favored regions (%) | 91.2 ± 0.7 |
| Residues in additionally allowed regions (%) | 8.8 ± 0.7 |
| Residues in generously allowed regions (%) | 0.0 ± 0.0 |
| Residues in disallowed regions (%) | 0.0 ± 0.0 |
| RMSD to mean structure statisticsc,d | |
| Protein | |
| Backbone atoms | 0.21 ± 0.04 |
| Heavy atoms | 0.51 ± 0.05 |
| RNA | |
| Backbone atoms | 0.59 ± 0.31 |
| Heavy atoms | 0.64 ± 0.26 |
| All molecules | |
| Backbone atoms | 0.29 ± 0.08 |
| Heavy atoms | 0.54 ± 0.06 |
aH-bond constraints were identified from slow exchanging amide protons in D2O.
bProtein backbone angles determined by the program TALOS+ and sugar pucker angles based on coupling efficiency in homonuclear TOCSY.
cStatistics computed for the deposited bundle of 20 violation energy best structure selected out of 30 amber energy best.
dBased on structured residue range as defined by user: protein: 351–498, chain ID: A (sequence range: 347–502) RNA : 1–6, chain ID: B (sequence range: 1–6).
eRamachandran plot as defined by the program PROCHECK.