Table 2.

Summary of peptide‐binding data determined by ITC against HumRadA2. Mutated residues are highlighted in bold. All peptides were N‐acetylated and C‐amide terminated

Table entry	Peptide	K D/μm	ΔH/cal·mol−1	TΔS/cal·mol−1	PDB code
First position variation
1	FHTA	280 ± 20	−2388 ± 94	2453	4b3b 15
2	WHTA	93 ± 3	−2768 ± 34	2727	5fow
Second position variation
3	FATA	280 ± 29	−1820 ± 109	3010	5fpk a
4	FNTA	613 ± 44	−4036 ± 177	346	–
5	FPTA	No detectable binding			–
Third position variation
6	FHPA	113 ± 3	−2155 ± 26	3218	5fou
7	FHAA	675 ± 60	−7948 ± 466	−3636	5fox
Fourth position variation
8	FHTG	1590 ± 300	−5518 ± 924	−1702	5fov
9	FHTU	680 ± 51	−14 600 ± 771	−10 281	5fot
Combination
10	WHPA	330 ± 25	−6801 ± 318	−2044	–
Peptide truncations
11	FH	No binding detected No binding detected No binding detected			–
12	FHT				–
13	HTA				–

^aStructure solved with wild‐type RadA.