Table 1 NMR and refinement statistics of the (DMA-135)-SLII complex.

From: IRES-targeting small molecule inhibits enterovirus 71 replication via allosteric stabilization of a ternary complex

 

SLII2231-DMA-135

NMR distance and dihedral constraints

 

Distance restraints

 

Total NOE

506

Intra-residue

162

Inter-residue

344

 Sequential (|i – j | = 1)

245

 Nonsequential (|i – j | > 1)

6

 Hydrogen bonds

75

 CH RDCs (base pair only)

23

Qfree (%)

 

 Intermolecular (SLII to DMA-135)

29

 Total dihedral angle restraints

 

Nucleic acid

 

 Base pair

N/A

 Sugar pucker

155

 Backbone

N/A

 Based on A-form geometry

 

Structure statistics

 

Violations (mean and s.d.)

 

 Distance constraints (>0.4 Å)

1.30 ± 1.41

 Dihedral angle constraints (>5°)

N/A

 Max. dihedral angle violation (>5°)

N/A

 Max. distance constraint violation (Å)

0.40 ± 0.38

Deviations from idealized geometry

 

 Bond lengths (Å)

0.01112 ± 0.0007

 Bond angles (°)

2.495 ± 0.018

 Impropers (°)

N/A

Average pairwise r.m.s. deviationa (Ã…)

 

RNA

 

 Heavy

3.26 ± 1.92

 Backboneb

3.25 ± 2.08

 Upper helix (12–20 & 27–35)

 

 Lower helix (1–5 & 35–41)

 

 Complex

0.56 ± 0.11

 All complex heavy (C, N, O, P)c

3.54 ± 1.86

  1. aStatistics were calculated and averaged over an ensemble of the 10 lowest energy structures.
  2. bPairwise r.m.s deviation for backbone was calculated with alignment of C3’, C4’, C5’, O3’, O5’, and P atoms.
  3. cPairwise r.m.s deviation for complex was aligned with base pair region.