. 2017 Aug 31;39(2):302–310. doi: 10.1038/aps.2017.59

Table 1. The binding affinities of various peptide truncations of EED-binding domain (EBD) determined by FP competitive assay. K_i is the inhibition constant.

No	Peptide sequence	K_i (μmol/L)
1	Ac-KTMFSSNRQKILERTETLNQEWKQRRIQPV-NH₂	0.050
2	Ac-TMFSSNRQKILERTETLNQEWKQR-NH₂	0.079
3	Ac-FSSNRQKILERTETLNQEWKQR-NH₂	0.113
4	Ac-SNRQKILERTETLNQEWKQR-NH₂	>200
5	Ac-RQKILERTETLNQEWKQR-NH₂	>200
6	Ac-KILERTETLNQEWKQR-NH₂	>200
7	Ac-LERTETLNQEWKQR-NH₂	>200
8	Ac-TMFSSNRQKILERTETLNQEWK-NH₂	2.862
9	Ac-TMFSSNRQKILERTETLNQE-NH₂	>200
10	Ac-TMFSSNRQKILERTETLN-NH₂	>200
11	Ac-TMFSSNRQKILERTET-NH₂	>200
12	Ac-TMFSSNRQKILERT-NH₂	>200
13	Ac-TMFSSNRQKILER-NH₂	>200
14	Ac-FSSNRQKILERTETLNQEWK-NH₂	15.501

Table 1. The binding affinities of various peptide truncations of EED-binding domain (EBD) determined by FP competitive assay. Ki is the inhibition constant.