Skip to main content
. 2012 Jun 7;40(16):8129–8143. doi: 10.1093/nar/gks516

Table 3.

ITC analyses for the interaction of the M.EcoKI MTase with Ocr or its variants

Ocr variant Stoichiometry Ocr dimers per M.EcoKI Enthalpy (kcal mol−1) Dissociation constant (Kd) (nM)
Wild typea 0.87 ± 0.01 −20.5 ± 0.3 Too tight
Mut1 0.98 ± 0.01 −13.8 ± 0.3 Too tight
Mut2 1.04 ± 0.01 −14.5 ± 0.2 Too tight
Mut3 0.93 ± 0.02 −14.7 ± 0.5 79 ± 21
Mut4 0.83 ± 0.01 −19.4 ± 0.2 Too tight
Mut7 0.99 ± 0.01 −12.5 ± 0.3 Too tight
Mut10 ∼0 ∼0 ∼no binding
Mut11 ∼0 ∼0 ∼no binding
Mut12 0.90 ± 0.01 −15.4 ± 0.4 20 ± 9
Mut13 1.18 ± 0.03 −11.0 ± 0.4 41 ± 16
Mut16 0.98 ± 0.03 −8.2 ± 0.4 71 ± 30
Ocr/POcr 0.89 ± 0.01 −15.3 ± 0.2 Too tight
Ocr99a 0.71 ± 0.01 −22.4 ± 0.7 Too tight
Ocr109a 0.74 ± 0.01 −25.0 ± 0.6 Too tight

aData from (17).