Table 2 Comparison between experimental (Exp) and theoretical (Theo) FRET values.

From: Structure of prothrombin in the closed form reveals new details on the mechanism of activation

FRET mutant

Domains

Exp

Theo

ΔFRET (Exp-Theo)

34–101

Gla-K1

0.94

0.92

0.02

34–210

Gla-K2

0

0.02

0.02

34–478

Gla-Bc

0.77

0.74

0.03

101–160

K1-Lnk2

0.62

0.23

0.39

101–210

K1-K2

0.15

0.11

0.04

101–478

K1-Bc

0.89

0.94

0.05

120–478

K1-Bc

0.58

0.55

0.03

210–478

K2-Bc

0.19

0.12

0.07

  1. Standard deviations for experimental FRET values are typically 10%. Significant changes between experimental and theoretical values (>0.1) were observed only for the couple 101/160, indicating that the position of residue 160 in Lnk2 varies in solution and, on average, is closer to residue 101.