Table 1.
Structure statistics of free PARN RRM and the RRM:cap analog complex
| Free PARN RRM | RRM: cap complex | |
|---|---|---|
| Restraints for final structure calculations | ||
| Number of NOE distance restraints | 1266 | 1131 |
| Intraresidue | 372 | 348 |
| Sequential (|i−j| = 1) | 367 | 298 |
| Medium–range (1 < |i−j| < 5) | 178 | 154 |
| Long–range (|i−j| ≥ 5) | 349 | 314 |
| Protein–RNA intermolecular | NA | 17 |
| Number of dihedral angle restraintsa | ||
| φ angles | 61 | 42 |
| ψ angles | 58 | 41 |
| χ angles | 24 | 27 |
| Number of hydrogen bond restraintsb | 14 | 18 |
| Structure statistics (20 structures) | ||
| Mean number of NOE violations >0.2 Å | 0 | 0 |
| Mean number of dihedral angle violations >5° | 0 | 1.7 ± 1.5 |
| Average CYANA target function (Å2) | 0.01 | 0.08 |
| Average AMBER energy (kcal mol−1) | NA | −4785 ± 8 |
| RMS deviation to mean coordinatesc | ||
| Backbone heavy atoms (Å) | 0.33 ± 0.07 | 0.52 ± 0.11 |
| All heavy atoms (Å) | 0.74 ± 0.07 | 0.93 ± 0.14 |
| Ramachandran plot analysisd | ||
| Residues in most favored regions (%) | 89.2 | 89.2 |
| Residues in additionally allowed regions (%) | 10.8 | 10.5 |
| Residues in generously allowed regions (%) | 0.0 | 0.3 |
| Residues in disallowed regions (%) | 0.0 | 0.0 |
aφ and ψ angles were derived from the program TALOS. The χ angles contain 18 χ1 and 6 χ2 angle restraints for free PARN RRM and 19 χ1 and 8 χ2 angle restraints for the RRM:cap complex.
bOnly hydrogen bonds supported by NOEs were used.
cResidues 440–509 for free PARN RRM. Residues 440–509 and m7GpppG for the RRM:cap complex.
dFrom PROCHECK-NMR (46) for 20 structures. Residues 440–509 were used.