Table 2.
Summary of NMR restraints and structure statistics
| Capsid protein (BRMB 30741, PDB 6WAP, PDB 6X63) | |||
|---|---|---|---|
| NMR distance and dihedral constraints | CA FL | CA NTD | CA CTD |
| Distance constraints | |||
| Total 13C-13C distance restraints | 1311 | 994 | 311 |
| Intraresidue | 491 | 374 | 114 |
| Inter-residue | 820 | 620 | 197 |
| Sequential (|i – j| = 1) | 221 | 161 | 58 |
| Medium range (2 ≤ |i – j| ≤ 4) | 204 | 166 | 38 |
| Long range (|i – j| ≥ 5) (sidechain-sidechain) | 210 (101) | 166 (85) | 43 (16) |
| Ambiguous | 185 | 127 | 58 |
| Restraints/residue | 5.7 | 6.9 | 3.7 |
| Percent completeness | 15% | 17% | 10% |
| Total dihedral-angle restraints | |||
| ϕ | 195 | 126 | 68 |
| ψ | 195 | 126 | 68 |
| Structure statisticsa | |||
| Violations (mean ± s.d.) | |||
| Distance constraints (Å) | 0.049 ± 0.002 Å | ||
| Dihedral-angle constraints (°) | 1.076 ± 0.101° | ||
| Max. distance-constraint violation (Å) | 0.773 Å | ||
| Max. dihedral-angle violation (°) | 12.364° | ||
| Deviations from idealized geometry | |||
| Bond lengths (Å) | 0.005 ± 0.000 Å | ||
| Bond angles (°) | 0.680 ± 0.006° | ||
| Impropers (°) | 0.575 ± 0.007° | ||
| Average pairwise r.m.s. deviation (Å) | |||
| Heavy | 1.2 ± 0.1 Å | ||
| Backbone | 0.5 ± 0.1 Å | ||
a
Pairwise r.m.s.d. was calculated among 10 refined structures.