Table 2 Quantum-chemical analyses (calculated energies in kcal mol−1, distances in Å) for the TRP2–Kme3 and TRP2–KPme3 complexes in watera.

From: Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

 

TRP2–Kme3[b]

TRP2–KPme3[c]

ΔE(aq)

−10.2

−11.4

ΔE(aq)strain

0.1

0.8

ΔE(aq)int

−10.3

−12.2

ΔE(desolv)int

17.3

15.7

ΔEint

−27.6

−28.0

ΔEPauli

20.8

23.5

ΔVelstat

−15.0

−15.8

ΔEoi

−13.0

−13.6

ΔEdisp

−20.4

−22.0

d(HMe-CTRP-6MR)

2.88

2.90

d(HMe-CTRP-5MR)

2.78

2.68

  1. aComputed using BLYP-D3BJ/TZ2P with COSMO to simulate aqueous solution. Structural rigidity imposed by the protein backbone is simulated through constrained geometry optimizations. See Eqs. ( 1–3) in Supplementary Information.
  2. bTRP2 fixed, Kme3 free.
  3. cTRP2 frozen, α-methyl carbon of KPme3 fixed to position in TRP2-Kme3 optimization.
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