Table 1

NMR structure determination: distance restraints, structural statistics, and atomic root-mean-square (rms) deviations. 〈SA〉 are the 41 simulated annealing structures,SA is the average structure before energy minimization, (SA)r is the restrained energy minimized average structure, and SD is the standard deviation.

Distance restraints
Intraresidue97
Sequential83
Short range (|ij| = 2 to 5 residues)59
Long range (|ij| > 5 residues)35
Hydrogen bond10
Total284
Structural statistics
rms deviationsSA〉 ± SD(SA)r
Distance restraints (Å)0.043  ±  0.0030.038
Idealized geometry
Bonds (Å)0.0041  ±  0.00020.0037
Angles (degrees)0.67  ±  0.020.65
Impropers (degrees)0.53  ±  0.050.51
Atomic rms deviations (Å)*
SA〉 versus SA ± SD 〈SA〉 versus  (SA)r ± SD
Backbone0.54  ±  0.150.69  ±  0.16
Backbone + nonpolar side chains 0.99  ±  0.171.16  ±  0.18
Heavy atoms1.43  ±  0.201.90  ±  0.29
  • * Atomic rms deviations are for residues 3 to 26, inclusive. Residues 1, 2, 27, and 28 were disordered [φ, ψ, angular order parameters (34) < 0.78] and had only sequential and |ij| = 2 NOEs.

  • Nonpolar side chains are from residues Tyr3, Ala5, Ile7, Phe12, Leu18, Phe21, Ile22, and Phe25, which constitute the core of the protein.