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Table 2 NMR and refinement statistics for ribbon BuIA

From: Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics

NMR distance & dihedral constraints  
Distance constraints  
   Total NOE 96
   Sequential (|i-j| = 1) 50
   Medium-range (|i-j| < 4) 18
   Long-range (|i-j| > 5) 12
   Intra-residual 16
Total dihedral angle restraints  
   Phi 5
   chi1 1
Structure statistics  
Violations (mean and s.d.)  
   Distance constraints (Å) 0.05 ± 0.003
   Dihedral angle constraints (°) 0.61 ± 0.2
   Max. dihedral angle violation (°) 3
   Max. distance constraint violation (Å) 0.3
Deviations from idealized geometry  
   Bond length (Å) 0.004 ± 0.00025
   Bond angles (°) 0.53 ± 0.02
   Impropers (°) 0.35 ± 0.02
Average pairwise r.m.s.d.** (Å)  
   Backbone 0.36 ± 0.12
   Heavy atoms 1.1 ± 0.49
Ramachandran statistics (%)  
   Most favoured 55.6
   Additionally allowed 44.4
   Disallowed 0.0
  1. **Pairwise r.m.s.d. was calculated among 20 refined structures