Table 1.
Statistics of Q8ZP25_SALTY and HYAE_ECOLI NMR structures.
| Protein | Q8ZP25_SALTY | HYAE_ECOLI |
|---|---|---|
| Conformationally-restricting distance constraints | ||
| Intraresidue [i = j] | 397 | 533 |
| Sequential [(i − j) = 1] | 428 | 542 |
| Medium Range [1 < (i − j) ≤ 5] | 206 | 200 |
| Long Range [(i − j) > 5] | 510 | 339 |
| Total | 1541 | 1524 |
| Dihedral angle constraints | ||
| Φ | 41 | 56 |
| ψ | 41 | 56 |
| Number of constraints per residue | 15.7 | 12.4 |
| Number of long-range constraints per residue | 5.2 | 2.5 |
| Completeness of stereo-specific assignments a[%] | ||
| βCH2 | 28 (16/58) | 25 (19/77) |
| Val and Leu isopropyl groups | 67 (16/24) | 20 (5/25) |
| CYANA target function [Å2] | 1.1 ± 0.17 | 1.88 ± 0.3 |
| Hydrogen bond constraints | 10 | 0 |
| NH RDC-derived orientational constraints | 69 | 0 |
| Average r.m.s.d. to the mean CYANA coordinates [Å] | ||
| regular secondary structure elements, backbone heavy atoms N, Cα, C′ | 0.72 ± 0.15b | 0.82 ± 0.09c |
| regular secondary structure elements, all heavy atoms | 1.14 ± 0.12 | 1.22 ± 0.09 |
| residues 11–41, 56–127, backbone heavy atoms | 0.95 ± 0.12 | 0.94 ± 0.13 |
| residues 11–41, 56–127, all heavy atoms | 1.49 ± 0.13 | 1.52 ± 0.12 |
| heavy atoms of best-defined side-chains | 0.5 ± 0.07d | 0.58 ± 0.1e |
| PROCHECK G-factorsf (ϕ and Ψ/all dihedral angles) | 0.04/−1.6 | 0.04/−1.48 |
| MOLPROBITY clash scoreg | −1.74 | −2.43 |
| AutoQF R/P/DP scores (%)h | 0.94/0.93/0.76 | 0.97/0.93/0.66 |
| Ramachandran plot summary ordered residues: [%] | ||
| most favored regions | 93.5 | 92.3 |
| additionally allowed regions | 6.4 | 7.2 |
| generously allowed regions | 0.1 | 0.5 |
| disallowed regions | 0 | 0 |
| Average number of distance constraints violations per CYANA conformer [Å] | ||
| 0.2–0.5 | 0.1 | 0.1 |
| > 0.5 | 0 | 0 |
| Average number of dihedral-angle constraint violations per CYANA conformer [degrees] | ||
| > 5 | 0 | 0 |
a
Relative to pairs with non-degenerate chemical shifts.
b
Residues: 20–22, 37–40, 71–74, 95–99, 102–107 (β-strands), and 8–16, 26–34, 58–62, 79–86, 115–123 (α-helices).
c
Residues: 19–22, 35–42, 69–75, 94–99, 102–108 (β-strands), and 5–16, 24–33, 56–63, 77–87, 112–124 (α-helices).
d
34 residues: 15, 19, 21, 22, 24, 27, 30, 31, 34, 38–41, 58, 59, 68, 70, 72–75, 82, 83, 94–99, 103, 106, 118, 122, 123.
e
30 residues: 10, 11, 14–16, 19, 21, 38–40, 61, 62, 70, 72–75, 80, 82, 83, 94, 97, 107, 113, 114, 117–120, 123
f
Defined in Reference [42],
g
Defined in Reference [43],
h
Defined in Reference [44]