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CATH classification
1.10.490.10
C: Mainly Alpha
A: Orthogonal Bundle
T: Globin-like
H: Globins

SCOP classification
a.1.1.2
C: All alpha proteins
F: Globin-like
S: Globin-like
F: Globins

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Molecular Function
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 ERROR
PDB ID1uc3
ChainA
N 149
Fmax [ε/Å] 1.47
Fmax [pN] 161.7
ΔFmax [ε/Å] 0.16
Dmax [Å] 29.59
Lmax [Å] 30.75
λ 0.01
nSS 0

For help click on values in the Table.

Latest estimate of force unit, ε/Å is 110+/-30 [pN]. For details see our paper.

Unfolding scenario

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Chain
Opis Chain
 
xN
Number of amino-acids in the structure
 
xFmax
In the force-displacement curve the height of a highest force peak. Final stage of protein stretching resulting in hooke`an linear force growth is excluded. If a curve has no apparent peaks, the Fmax is arbitrarily set to 0.
 
xFmax
Estimated value of Fmax in pN
 
xΔFmax
Standard deviation of Fmax across saveral trajectories
 
xLmax
End-to-end at which the force rises to Fmax.
 
xDmax
Tip displacement at which the force rises to Fmax.
 
xLambda
λ=(Lmax - Ln)/(Lf - Ln) where Ln is the native end-to-end distance in the structure,
Lf denominates end-to-end distance at full extension. lambda varies between 0 and 1. Small values of lambda indicate occurance of the maximum force at the beginning of the pulling process. Note, that the disulphide bridges may not allow for the full extension.
nSS: the number of disulphide bridges in protein structure
 
xnSS
The number of disulphide bridges in protein structure.
 

Institute of Physics, Polish Academy of Sciences 2010
Authors: Mateusz Sikora, Marek Cieplak, Joanna I. Sułkowska    Realization: Bartłomiej S. Witkowski