Table 2 Summary of thermodynamic-binding parameters for complex formation between different H3 peptides and WT and mutant BAZ2A/B PHD fingers

Error values reported on dissociation constant (KD), stoichiometry of binding (N) and binding enthalpy (ΔH) are generated by the Origin program and reflect the quality of the fit between the nonlinear least-squares curve and the experimental data. Errors reported on TΔS and ΔG were propagated from the errors of KD and ΔH. Raw ITC data are shown for each titration in Supplementary Data (Supplementary Figure S1).

PeptideProteinKD (µM)NΔH (kcal/mol)TΔS (kcal/mol)ΔG (kcal/mol)
ARTKBAZ2A PHD100 ± 41.57 ± 0.03−6.1 ± 0.2−0.6 ± 0.2−5.46 ± 0.02
ARTABAZ2A PHD56 ± 21.44 ± 0.01−4.7 ± 0.11.1 ± 0.1−5.81 ± 0.02
ARTKQBAZ2A PHD210 ± 301.6 ± 0.1−3.7 ± 0.41.3 ± 0.4−5.0 ± 0.1
ARTKQTARKSBAZ2A PHD51 ± 21.35 ± 0.01−5.8 ± 0.10.1 ± 0.1−5.86 ± 0.02
AATKQTARKSBAZ2A PHD>1000N.D.N.D.N.D.N.D.
ARAKQTARKSBAZ2A PHDNo binding
ARTAQTARKSBAZ2A PHD42 ± 21.03 ± 0.02−6.1 ± 0.2−0.1 ± 0.2−6.00 ± 0.03
ARTKATARKSBAZ2A PHD9.3 ± 0.21.21 ± 0.01−6.13 ± 0.020.74 ± 0.02−6.87 ± 0.01
ARTKQAARKSBAZ2A PHD55 ± 20.90 ± 0.01−5.6 ± 0.10.2 ± 0.1−5.82 ± 0.02
ARTAATARKSBAZ2A PHD12.1 ± 0.31.32 ± 0.01−7.01 ± 0.04−0.30 ± 0.04−6.71 ± 0.02
ARTGGTARKSBAZ2A PHD143 ± 71.28 ± 0.04−7.4 ± 0.3−2.2 ± 0.3−5.25 ± 0.03
ARTKQBAZ2B PHD190 ± 251.0 ± 0.1−4.7 ± 0.80.4 ± 0.8−5.1 ± 0.1
ARTKQTARKSBAZ2B PHD40.0 ± 0.51.45 ± 0.04−5.43 ± 0.020.58 ± 0.02−6.01 ± 0.01
AATKQTARKSBAZ2B PHD>1000N.D.N.D.N.D.N.D.
ARAKQTARKSBAZ2B PHD>5000N.D.N.D.N.D.N.D.
ARTAQTARKSBAZ2B PHD8.5 ± 0.20.88 ± 0.01−6.62 ± 0.040.30 ± 0.05−6.92 ± 0.01
ARTKATARKSBAZ2B PHD7.0 ± 0.21.20 ± 0.03−6.18 ± 0.020.86 ± 0.03−7.04 ± 0.02
ARTKQAARKSBAZ2B PHD44.6 ± 0.81.01 ± 0.01−5.3 ± 0.10.68 ± 0.06−5.94 ± 0.01
ARTAATARKSBAZ2B PHD2.6 ± 0.11.13 ± 0.01−7.12 ± 0.020.50 ± 0.03−7.63 ± 0.02
ARTGGTARKSBAZ2B PHD166 ± 81.3 ± 0.1−8.4 ± 0.5−3.3 ± 0.5−5.16 ± 0.03

Abbreviations: N.D.: not determined.