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. 2012 Sep 10;109(43):17388–17393. doi: 10.1073/pnas.1208642109

Table 1.

NMR structural statistics for the family of 20 structures of Myo10 antiparallel coiled coil

Protein
NMR distance and dihedral constraints
 Total NOE 2,591
 Intraresidue 312
 Interresidue
 Sequential (|ij| = 1) 573
 Medium range (|ij| < 4) 561
 Long range (|ij| > 5) 27
 Intermolecular 659
 Ambiguous NOEs restraints (i.e., either intra- or intermolecular couplings) 382
 Hydrogen bonds 104
NMR total dihedral angle restraints 164
 ϕ 82
 ψ 82
Structure statistics
 Violations (mean and SD)
  Distance constraints (Å) 0.004 ± 0.000
  Dihedral angle constraints (°) 0.099 ± 0.017
 Deviations from idealized geometry
  Bond lengths (Å) 0.001 ± 0.000
  Bond angles (°) 0.331 ± 0.004
  Impropers (°) 0.154 ± 0.010
 Average pairwise rmsd* (Å)
  Well-ordered residues (Myo 10 anti-CC883–925)
   Heavy 1.272
  Backbone 0.67

*Pairwise rmsd was calculated among 20 refined structures.