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. Author manuscript; available in PMC: 2007 May 5.
Published in final edited form as: J Mol Biol. 2006 Nov 11;366(1):155–164. doi: 10.1016/j.jmb.2006.11.024

Table 1.

Statistics for the 20 NMR-derived conformers that represent the solution structure of HsSen15(36–157)

Experimental constraints (per monomer)
 Distance constraints
  Long (intramolecuar) 431
  Long (intermolecular) 55
  Medium [1<(i–j)≤5] 401
  Sequential [2 (i–j)=1] 519
  Intraresidue [i=j] 852
 Dihedral angle constraints (ϕ and Ψ) 163
 Hydrogen bonds 46
 DNH residual dipolar couplings 94

Target function ( Å2) 2.68 ± 0.49

Average atomic R.M.S.D. to the mean structure (Å)

 Dimer (residues 10–122 of the construct)
  Backbone ( Cα, C′, N, O) 1.09 ± 0.19
  Heavy atoms 1.45 ± 0.15
 Monomer I (residues 10–122 of the construct)
  Backbone ( Cα, C′, N, O) 0.78 ± 0.12
  Heavy atoms 1.21 ± 0.10
 Monomer II (residues 10–122 of the construct)
  Backbone ( Cα, C′, N, O) 0.82 ± 0.12
  Heavy atoms 1.25 ± 0.10
 Deviations from idealized covalent geometry
  Bond (Å) 0.018 ± 0.001
  Angles (°) 1.901 ± 0.089
  Impropers (°) 1.744 ± 0.091

R.M.S.D. from experimental distance constraints (Å) 0.019 ± 0.003

R.M.S.D. from experimental dihedral constraints (Å) 0.468 ± 0.064

Ramachandran statistics (% of all residues)

 Most favored 84.23 ± 1.63
 Additionally allowed 12.72 ± 1.61
 Generously allowed 2.47 ± 0.90
 Disallowed 0.58 ± 0.47