Distance restraints | ||
---|---|---|
Intraresidue | 97 | |
Sequential | 83 | |
Short range (|i – j| = 2 to 5 residues) | 59 | |
Long range (|i – j| > 5 residues) | 35 | |
Hydrogen bond | 10 | |
Total | 284 | |
Structural statistics | ||
rms deviations | 〈SA〉 ± SD | (SA)_{r} |
Distance restraints (Å) | 0.043 ± 0.003 | 0.038 |
Idealized geometry | ||
Bonds (Å) | 0.0041 ± 0.0002 | 0.0037 |
Angles (degrees) | 0.67 ± 0.02 | 0.65 |
Impropers (degrees) | 0.53 ± 0.05 | 0.51 |
Atomic rms deviations (Å)^{*} | ||
〈SA〉 versus SA ± SD 〈SA〉 versus (SA)_{r} ± SD | ||
Backbone | 0.54 ± 0.15 | 0.69 ± 0.16 |
Backbone + nonpolar side chains^{†} | 0.99 ± 0.17 | 1.16 ± 0.18 |
Heavy atoms | 1.43 ± 0.20 | 1.90 ± 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 |i – j| = 2 NOEs.
↵† Nonpolar side chains are from residues Tyr^{3}, Ala^{5}, Ile^{7}, Phe^{12}, Leu^{18}, Phe^{21}, Ile^{22}, and Phe^{25}, which constitute the core of the protein.