Table 1.
Summary of NMR data and structural statistics for S28E
| Completeness of resonance assignmentsa | |||
| Assignable backbone (%) | 98 | ||
| Assignable side chain (%) | 92 | ||
| 3D 15N | 3D 13C | 4D 13C/13C | |
| NOESY spectral datab | |||
| Total number of peaks | 747 | 1462 | 920 |
| Number of “assignable” peaks | 744 | 1352 | 910 |
| Number of peak assignments | 618 | 1198 | 771 |
| Percent assignment (%) | 83 | 89 | 85 |
| Conformationally restricting constraints | |||
| Distance constraints | |||
| Total | 828 | ||
| Intraresidue (i = j) | 121 | ||
| Sequential (|i − j| = 1) | 268 | ||
| Medium range (1 < |i − j| ≤ 5) | 97 | ||
| Long range (|i − j| > 5) | 342 | ||
| Distance constraints per residue | 11.7 | ||
| Dihedral angle constraints | 69 | ||
| Hydrogen bond constraints | |||
| Total | 30 | ||
| Long range (|i − j| > 5) | 28 | ||
| Number of constraints per residue | 13.1 | ||
| Number of long range constraints per residue | 5.2 | ||
| Residual constraint violationsc | |||
| DYANA target function (Å2) | 0.48 ± 0.067 | ||
| Average number of distance violations per structure | |||
| 0.1–0.2 Å | 6.5 | ||
| 0.2–0.5 Å | 2.4 | ||
| >0.5 Å | 0 | ||
| Average r.m.s. distance violation per constraint (Å) | 0.02 | ||
| Maximum distance violation (Å) | 0.28 | ||
| Average number of dihedral angle violations per structure | |||
| 0–10° | 0.7 | ||
| >10° | 0 | ||
| Average r.m.s. dihedral angle violation per constraint (°) | 0.13 | ||
| Maximum dihedral angle violation (°) | 1.30 | ||
| van der Waals violations per structure | |||
| Average van der Waals violation (Å) | 0.10 | ||
| Maximum van der Waals violation (Å) | 0.12 | ||
| r.m.s.d. from average coordinates; ordered residuesd | |||
| Backbone atoms | 0.3 | ||
| Heavy atoms | 1.1 | ||
| Ramachandran plot statistics; ordered residuesd | |||
| Most favored regions (%) | 82.0 | ||
| Additional allowed regions (%) | 18.0 | ||
| Generously allowed (%) | 0.0 | ||
| Disallowed regions (%) | 0.0 | ||
| r.m.s. deviations from ideal geometry | |||
| Bond length (Å) | 0.011 | ||
| Bond angle (°) | 1.7 | ||
Structural statistics were compared for the 10 structures with lowest DYANA target function out of 56 calculated in the final cycle of AutoStructure analysis.
a Computed using AVS software (H.N.B. Moseley, G. Sahota, and G.T. Montelione, in prep.) from the expected number of peaks, excluding highly exchangeable protons (N-terminal, Lys, and Arg amino groups, hydroxyls of Ser, Thr, Tyr), carboxyls of Asp and Glu, and nonprotonated aromatic carbons.
b Peak assignment statistics for the 3D 15N, combined aliphatic and aromatic 3D 13C, and 4D 13C/13C NOESY spectra from the final cycle of AutoStructure. The total number of peaks refer to the raw input to AutoStructure; the number of “assignable” peaks refer to peaks that can be matched to the chemical shift list within the tolerances used; the number of peak assignments represents the total (unambiguous + ambiguous) number of peaks assigned by AutoStructure.
c Average distance violations were calculated using the sum over r−6.
d Ordered residue ranges: 7–17, 24–33, 36–47, 50–56.