Table 1.
NMR experimental restraints and structural statistics.
| RRM1+UUAGGUC | RRM2+UCAGUU | |||
|---|---|---|---|---|
| Protein | RNA | Protein | RNA | |
| Distance restraints | ||||
| Total NOE (intramolecular) | 2356 | 87 | 2083 | 59 |
| Intra-residue | 395 | 63 | 369 | 45 |
| Sequential | 609 | 24 | 450 | 14 |
| Medium range (|i-j|<5 residues) | 522 | 0 | 424 | 0 |
| Long range (|i-j|≥5 residues) | 830 | 0 | 840 | 0 |
| Hydrogen bonds (intramolecular) | 22 | 0 | 21 | 0 |
| Protein-RNA intermolecular NOE | 117 | 111 | ||
| Protein-RNA intermolecular hydrogen bonds | 2 | 2 | ||
| Distance restraints violations (mean ± s.d.) | ||||
| Number of NOE violations > 0.2 Å | 1.9 ± 1.2 | 3.1 ± 1.0 | ||
| Maximum NOE violation (Å) | 0.25 ± 0.05 | 0.27 ± 0.04 | ||
| Dihedral angle restraints | ||||
| Sugar pucker | 4 | 4 | ||
| Dihedral violations (mean ± s.d.) | ||||
| Number of dihedral violations > 5° | 0 | 0 | ||
| Maximum dihedral violation (°) | 0.04 ± 0.16 | 0.47 ± 0.86 | ||
| R.m.s.d. from mean structure (Å) | ||||
| Protein* | ||||
| Backbone | 0.40 ± 0.11 | 0.45 ± 0.08 | ||
| Heavy atoms | 0.83 ± 0.10 | 0.78 ± 0.07 | ||
| RNA† | ||||
| Heavy atoms | 0.62 ± 0.13 | 0.78 ± 0.14 | ||
| Deviation from ideal geometry (mean ± s.d.) | ||||
| Bond lengths (Å) | 0.0037 ± 0.0001 | 0.0035 ± 0.0001 | ||
| Bond angles (°) | 0.51 ± 0.02 | 0.49 ± 0.01 | ||
| Impropers (°) | 1.13 ± 0.09 | 1.22 ± 0.06 | ||
| Ramachandran analysis | ||||
| Most favored region | 85.9% | 83.1% | ||
| Allowed region | 13.6% | 16.6% | ||
| Disallowed region | 0.5% | 0.2% | ||
| CING Red/Orange/Green scores | ||||
| R/O/G (%) | 18/28/54 | 21/25/54 | ||
*Protein r.m.s.d. was calculated using residues 11–92 for RRM1 and 103–112, 115–139, 144–187 for RRM2;.
†RNA r.m.s.d. was calculated using residues 2–5 for RNA bound to RRM1 and 2–4 for the RNA bound to RRM2.