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. 2008 Feb 7;36(5):1681–1689. doi: 10.1093/nar/gkn006

Table 1.

NMR and refinement statistics for the HBV HPRE stem-loop α structure (HSLAap)

NMR distance and dihedral constraints
Distance constraints 529
Hydrogen bond constraints 48
Total dihedral angle restraints 207
Structure statistics
Violations
    Target function (Å2) 0.260 (0.00378)
    Distance constraints > 0.1 Å 3.87 (0.96)
    Max. distance constraint violation (Å) 0.18 (0.02)
    Dihedral angle constraints 0 (0)
    Max. dihedral angle violation (°) 1.71 (0.07)
    AMBER physical energies (kcal/mol) −161.68 (8.76)
Deviations from idealized geometry
    Bond lengths (Å) 0.0047 (0.00006)
    Bond angles (°) 1.4115 (0.01533)
Mean global r.m.s.d. (Å)
    Heavy atoms 1.22 (0.40)
    Pentaloop (residues 9–15) 0.74 (0.25)