Table 1.
Input and calculation statistics for the NMR structure determination of the protein NP_344798.1 in aqueous solution at pH = 6.0 and T = 298K.
| Quantity | Valuea |
|---|---|
| NOE upper distance limits | 4090 |
| intraresidual | 993 |
| short-range | 1055 |
| medium-range | 904 |
| long-range | 1138 |
| Dihedral angle constraints | 799 |
|
| |
| Residual target function value [Å2] | 3.9 ± 0.43 |
| Residual NOE violations | |
| number ≥ 0.1 A | 41 ± 6 |
| maximum [Å] | 0.2 ± 0.19 |
| Residual dihedral angle violations | |
| number ≥ 2.5o | 1 ± 1 |
| maximum [°] | 4.79 ± 1.5 |
| AMBER energies [kcal/mol] | |
| total | −7843 ± 144 |
| van der Waals | −705 ± 35 |
| electrostatic | −8779 ± 112 |
| RMSD from the mean coordinates b[Å] | |
| backbone (2–191) | 0.66 ± 0.09 |
| all heavy atoms (2–191) | 1.05 ± 0.09 |
| Ramachandran plot statisticsc | |
| most favoured regions [%] | 75.1 |
| additional allowed regions [%] | 23.0 |
| generously allowed regions [%] | 1.6 |
| disallowed regions [%] | 0.3 |
a
Except for the top six entries, which represent the input generated for the final cycle of structure calculation with UNIO-ATNOS/CANDID and CYANA 3.0, average values and standard deviations for the 20 energy-minimized conformers are given.
b
The numbers in parentheses indicate the residues for which the RMSD was calculated.
c
As determined by PROCHECK (Laskowski et al. 1993).