Table 2.

AMBER refinement statistics for complexes

	mPHD-mDPPA3
Structure statistics
Energy (mean and s.d.)
E-AMBER (kcal/mol)	−5314.54 ± 19.75
NMR NOE	36.31 ± 2.59
NMR Dihedral	6.92 ± 0.87
Violations
Number of distance constraints >0.1 Å, >0.5 Å	24.6 ± 3.3, 0 ± 0
Number of dihedral angle constraints >2.5°, >5°	15.9 ± 2.1, 12.1 ± 1.5
Max. dihedral angle violation (°)	31.5
Max. distance constraint violation (Å)	0.45
Ramachandran plot statistics (%)
Residues in favored regions	88 ± 1
Residues in allowed regions	11 ± 2
Residues in outlier regions	1 ± 0
Average pairwise r.m.s. deviation** (Å)
Heavy	0.850
Backbone (Ca, N, CO)	0.396

¹H–¹H distance (exclusively derived from the NOE peaks) and dihedral (predicted by TALOS+) constraints for the AMBER refinements were identical to those applied to the CYANA calculations.

Ordered residues were automatically identified by Fit_Robot, residues on PHD domain: 9–15, 18–60, 62–68, and peptide: 86–112, 127–129.