Table 1. Thermodynamic parameters deduced from analysis of ITC data.

Interactions between MAN1Luhm and different Smad fragment complexes were tested. The stoichiometry was always equal to 1. Standard errors were calculated from two independent ITC measurements. In the case of MAN1Luhm binding to a complex between Smad2 and a FAST1 peptide, only an apparent Kd value is provided because the ITC signal results from a competition. The error is evaluated from the deviation between the experimental ITC values and the calculated fitting curve.

MAN1Luhm against:	Kd (μM) with their fitting errors	ΔH (kCal/Mol)	TΔS (kCal/Mol)
S2LMH2EEE	1.27±0.04; 1.40±0.03	−8.4; −8.4	−0.5; −0.5
S3LMH2EEE	1.17±0.02; 1.35±0.04	−8.4; −8.4	−0.5; −0.5
S2LMH2EEE/S4LMH2	1.25±0.04; 1.30±0.03	−8.4; −8.4	−0.5; −0.5
S3LMH2EEE/S4LMH2	1.50±0.04; 1.37±0.03	−8.7; −8.8	−0.9; −0.9
S2LMH2EEE Y366A-W368A	37.9±6.3; 33.9±8.4	−1.6; −1.4	4.3; 4.5
S2LMH2EEE/SIM	12.2±0.1; 5.92±0.09