Table 1.
NMR and refinement statistics for NHR3(a.a. 585-615)/PKA(RIIα) complex protein structure‡.
| NMR Distance and Dihedral Constraints: | ||||||
|---|---|---|---|---|---|---|
| Distance constraints: | ||||||
| NOEs (total): 3094 | ||||||
| NHR3(a.a. 585-615) | PKA(RIIα) | |||||
| Monomer I | Monomer II | |||||
| Intra-residue | 379 | 454 | 454 | |||
| Inter-residue | ||||||
| Sequential (|i − j | = 1) | 173 | 258 | 258 | |||
| Medium-range (1 < |i − j | < 5) | 84 | 140 | 140 | |||
| Intramonomer | Intermonomer | Intramonomer | Intermonomer | |||
| Long-range (|i − j | > 4) | 6 | 20 | 88 | 52 | 79 | |
| Intermolecular | 294 (NHR3 → PKA(RIIα)) | 179 (PKA(RIIα) → NHR3) | ||||
| Ambiguous | N/A | 42 | ||||
| Total dihedral angle restraints: | ||||||
| Φ (total): 83 | ||||||
| Ψ (total): 83 | ||||||
| NHR3(a.a. 585-615) | PKA(RIIα) | |||||
| Φ | 21 | 62 (31 per monomer) | ||||
| Ψ | 21 | 62 (31 per monomer) | ||||
| Residual dipolar couplings: | ||||||
| NHR3(a.a. 585-615) | PKA(RIIα) | |||||
| Monomer I | Monomer II | |||||
| 1DHN (50 + M) | 18 | 22 | 17 | |||
| 1DNC′ (50 + M) | 21 | 21 | 21 | |||
| 1DC′Ca (50 + M) | 22 | 19 | 18 | |||
| 2DHNC′ (50 + M) | 19 | N/A | ||||
| 1DHN (50 ± MA) | 18 | N/A | ||||
| 1DNC′ (50 ± MA) | 21 | N/A | ||||
| 1DC′Ca (50 ± MA) | 18 | N/A | ||||
| 2DHNC′ (50 ± MA) | 19 | N/A | ||||
| Structure statistics: | ||
|---|---|---|
| Structures: | 15 | |
| Violations (mean and s.d.): | ||
| Distance constraints (Å) | 0.0110±0.0007 | |
| Dihedral angle constraints (°) | 0.2709±0.0333 | |
| Residual dipolar couplings (Hz): | ||
| HN (50 + M) | 1.7578±0.0707 | (complex) |
| NC′ (50 + M) | 0.7893±0.0364 | (complex) |
| C′Cα (50 + M) | 0.6587±0.0436 | (complex) |
| HNC′ (50 + M) | 2.4604±0.0865 | (NHR3 only) |
| HN (50 ± MA) | 1.3015±0.1680 | (NHR3 only) |
| NC′ (50 ± MA) | 0.3731±0.0411 | (NHR3 only) |
| C′Cα (50 ± MA) | 0.3997±0.0422 | (NHR3 only) |
| HNC′ (50 ± MA) | 1.3247±0.0700 | (NHR3 only) |
| Deviations from idealized geometry: | ||
| Bond lengths (Å) | 0.0027±0.0001 | |
| Bond angles (°) | 0.4223±0.0085 | |
| Impropers (°) | 0.2764±0.0152 | |
| Ramachandran plot statistics: | ||
| Rigid Regions* (%) | Complete Structure† (%) | |
| Residues in most favored regions | 93.2 | 85.8 |
| Residues in additionally allowed regions | 5.5 | 10.6 |
| Residues in generously allowed regions | 0.5 | 2.3 |
| Residues in disallowed regions | 0.8 | 1.3 |
| Average pairwise r.m.s. deviation: | ||
| Rigid Regions* (Å) | Complete Structure† (Å) | |
| Heavy | 1.45±0.09 | 2.09±0.18 |
| Backbone | 0.58±0.09 | 1.46±0.28 |
‡
All statistics based on complex structure
*
Statistics applied in structure rigid regions (a.a. 11–48, 111–148, 212–236)
†
Statistics applied in total stucture (a.a. 8–50, 108–150, 208–238)