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. 2017 Jul 29;45(17):10115–10131. doi: 10.1093/nar/gkx674

Table 2. Statistics for the ensemble of 15 lowest energy structures of Pcf11 residues 548–603.

NMR distance and dihedral restraints
Distance restraints
Total 1170
Intraresidue 353
Sequential (|i-j| = 1) 160
Medium range (1<|i-j|<5) 54
Long range (|i-j|>4) 332
Ambiguous 271
Dihedral angle restraints
Φ 51
Ψ 51
χ 32
Zn2+ coordination restraints
Distance 4
Dihedral 13
Structure statistics
Violations (mean and SD)
Distance restraints (Å) 0.010 ± 0.001
Dihedral angle restraints (°) 0.76 ± 0.09
Deviations from idealized geometry
Bond lengths (Å) 0.001 ± 0.000
Bond angles (°) 0.300 ± 0.005
Impropers (°) 0.22 ± 0.01
Ramachandran plot (%)a,b
Most favored regions 91.0 (95.9)c
Additionally favored regions 7.8 (4.1)
Generally allowed regions 0.4 (0.0)
Disallowed regions 0.8 (0.0)
Average pairwise rmsd (Å)a
Backbone 0.6 (0.4)
Heavy 1.0 (0.9)

aUsing the Protein Structure Validation Software suite (71).

bPROCHECK (72).

cNumber in parentheses for ordered regions: 549–555, 561–602.