Table 2.

Statistics for the 20 energy-minimized conformers of PHF1_Tudorin complex with H3_31–41K36Me3

Distance constraints
Long [(i–j)>5] (intramolecular)	250
Medium [1<(i–j)≤5]	106
Sequential [(i–j)=1]	234
Intraresidue [i=j]	462
Intermolecular	38

Dihedral angle constraints (φ and ψ)	96

Hydrogen bond constraints	16

Average pairwise R.M.S.D. to the mean structure (Å)^a

Backbone (C^α, C′, N, O)	0.26 ± 0.05
Heavy atoms	0.72 ± 0.10

Deviations from idealized covalent geometry

Bond (Å)	0.008 ± 0.002
Angles (°)	0.744 ± 0.012
Impropers (°)	0.479 ± 0.010

R.M.S.D. from experimental distance restraints (Å)	0.032 ± 0.001

R.M.S.D. from experimental dihedral restraints (°)	0.578 ± 0.027

Ramachandran statistics (% of all residues)^a

Most favored	91.3
Additionally allowed	8.7
Generously allowed	0.0
Disallowed	0.0

Statistics are given for residues 31–81 of PHF1_Tudorand residues 35–40 of the H3_31–41K36Me3 peptide.