Table 1.

Sequence of the Peptides Used in This Study with Their Determined K_d and ΔG Values

	(Putative) β-strand						α-Helix
	1	2	3	4	5	6	7	8	9	10	11	12	13	14	15	16	17	18	19	20	21		Kd (μM)	−ΔG (kcal/mol)
NCoR	T	H	R	L	I	T	L	A	D	H	I	C	Q	I	I	T	Q	D	F	A	R		0.4 ± 0.02	8.6 ± 0.03
ID1C
NM
NCoR	T	H	R	L	I	T	L	A	D	H	I	A	Q	I	I	T	Q	D	F	A	R		0.36 ± 0.02	8.8 ± 0.1
ID1C
ITC
NCoR			R	L	I	T	L	A	D	H	I	C	Q	I	I	T	Q	D	F	A	R		5.1 ± 0.82	7.2 ± 0.1
ID1B-2
NM
NCoR			R	L	I	T	L	A	D	H	I	C	Q	I	I	T	Q	D	F	A	R		0.6 ± 0.2	8.5 ± 0.2
ID1B-2
FITC
NCoR	S	F	A	D	P	A	S	N	L	G	L	E	D	I	I	R	K	A	L	M	G		3.5 ± 2.4	7.4 ± 0.4
ID2C
NM
NCoR				D	P	A	S	N	L	G	L	E	D	I	I	R	K	A	L	M	G	SFD	10.7 ± 6.3	6.8 ± 0.4
ID2B-3
NM
NCoR				D	P	A	S	N	L	G	L	E	D	I	I	R	K	A	L	M	G	SFD	3.8 ± 0.04	7.31 ± 0.01
ID2B-3
FITC
NCoR		K	T	T	I	T	A	A	N	F	I	D	V	I	I	T	R	Q	I	A	S	DKDAR	14.8 ± 3.7	6.5 ± 0.15
ID3B-1
FITC
NCoR		K	T	T	I	T	A	A	N	F	I	D	V	I	I	T	R	Q	I	A	S	DKDAR	91 ± 43	5.5 ± 0.35
ID3B-1
NM
NCoR5	T	H	R	L	I	T	L	A	D	H	I	C	Q	I	I	T	Q	D	F	A	R	…………….	0.5 ± 0	8.4 ± 0
	S	F	A	D	P	A	S	N	L	G	L	E	D	I	I	R	K	A	L	M	G
Smrt	H	Q	R	V	V	T	L	A	Q	H	I	S	E	V	I	T	Q	D	Y	T	R		1.4 ± 0.5	7.9 ± 0.2
ID1C
NM
Smrt			R	V	V	T	L	A	Q	H	I	S	E	V	I	T	Q	D	Y	T	R		1.7 ± 0.6	7.8 ± 0.2
ID1B-2
NM
Smrt			R	V	V	T	L	A	Q	H	I	S	E	V	I	T	Q	D	Y	T	R		2.4 ± 0.5	7.7 ± 0.1
ID1B-2
ITC
Smrt			R	V	V	T	L	A	Q	H	I	S	E	V	I	T	Q	D	Y	T	R		0.2 ± 0.06	9.1 ± 0.2
ID1B-2
Rho
Smrt	V	Q	E	H	A	S	T	N	M	G	L	E	A	I	I	R	K	A	L	M	G		2.3 ± 1.4	7.7 ± 0.4
ID2C
NM
Smrt			E	H	A	S	T	N	M	G	L	E	A	I	I	R	K	A	L	M	G		1.2 ± 0.45	8.0 ± 0.1
ID2C
NM
Smrt							T	N	M	G	L	E	A	I	I	R	K	A	L	M	G	KYDQ WEE	7.1 ± 2.2	6.9 ± 0.2
ID2B-6
NM
Smrt							T	N	M	G	L	E	A	I	I	R	K	A	L	M	G	KYDQ WEE	1.15 ± 0.4	8.0 ± 0.2
ID2B-6
FITC

Estimated errors are standard deviations from 3 or more experiments. Labeled peptides were used at a concentration of 4 nM. The sequences ID1 and ID2 motifs of the NCoR5 construct are given here. The complete 266 residue sequence can be found in the Materials and Methods. The secondary structures of the corresponding residues in the crystal structures are indicated in yellow for the putative β-strand in yellow and the α-helix in green in the top line of the table. Red indicates that the residues at these positions have been deleted for the corresponding peptide. FITC and Rho refer to N-terminal labeling of the peptides with either fluorescein or rhodamine. The peptides are ordered beginning with the NCoR variants and then the Smrt variants, and in order of ID1, ID2, and ID3, with N-terminal deletions appearing in order of increasing deletions. ITC refers to results from the titrations by isothermal titration calorimetry. The letter C following the peptide identification indicates that the peptide is complete, or full-length, with respect to the crystal structure interactions. NM refers to not marked or not labeled.