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K D = 23 µM

ITC characterization of L3MBTL2 4MBT binding with different histone peptides. H3K4me1. H3K9me1. H3K27me1. H3K9me2. H3K27me2. K D = 23 µM. K D = 43 µM. K D = 56 µM. K D = 9 µM. K D = 38 µM. Supplementary Figure 3a. Monomethylated Lysine interaction with L3MBTL2.

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K D = 23 µM

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  1. ITC characterization of L3MBTL2 4MBT binding with different histone peptides H3K4me1 H3K9me1 H3K27me1 H3K9me2 H3K27me2 KD = 23 µM KD = 43 µM KD = 56 µM KD = 9 µM KD = 38 µM Supplementary Figure 3a

  2. Monomethylated Lysine interaction with L3MBTL2 The binding of monomethylated lysine to L3MBTl2 is very weak (~4000 uM) Supplementary Figure 3b

  3. Thermodynamic parameters of the interaction of L3MBTL2 with histone peptides Supplementary Figure 3c

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