Table 1.
Structure Calculation Statistics of the 20 NMR Conformers of the S. gordonii Amylase-Binding Protein A (AbpA)
| Quantity | Valuea |
|---|---|
| NOE upper distance limits | 1774 |
| Intraresidual | 402 |
| Short range | 642 |
| Medium range | 536 |
| Long range | 194 |
| Talos dihedral angle constraints (φ, ψ) | 126 |
| Residual target function value (Å2) | 2.04 ± 0.36 |
| Residual NOE violations | |
| Number ≥0.1 Å | 16 ± 4 |
| Maximum (Å) | 0.17 ± 0.11 |
| Residual dihedral angle violations | |
| Number ≥2.5° | 1 ± 1 |
| Maximum (°) | 3.3 ± 1.3 |
| AMBER energies (kcal/mol) | |
| Total | −6859 ± 131 |
| Van der Waals | −234 ± 32 |
| Electrostatic | −8056 ± 138 |
| RMSD from mean coordinatesb (Å) | |
| Backbone (47–117,134–142) | 0.74 ± 0.23 |
| All heavy atoms (47–117,134–142) | 1.25 ± 0.32 |
| Ramachandran plot statisticsc (24–195) | |
| Most favoured and additional allowed regions (%) | 93.9 |
| Generously allowed regions (%) | 3.8 |
| Disallowed regions (%) | 2.4 |
a
Except for the top six entries, average values, and standard deviations for the 20 energy-minimized conformers are given. The top five entries represent the output from the seventh cycle of UNIO-ATNOS/CANDID and CYANA 3.0.
b
The numbers in parentheses indicate the residues for which the RMSD was calculated.
c
As determined by PROCHECK.27 Residues in the disallowed regions were observed either in the loop or unstructured regions of the structure.