Y. Cao is supported by National Natural Science Foundation of China (31401130 to Y.C.) . Z. Miao is supported by the French Government grant ANR-10-BINF-02-02 " BACNET ".
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+ shows H96 of 3c7wA (φ= 0.00, ψ= 0.00) in the Ramachandran Plots of two amino acids x shows K96 of 3f8vA (φ= 0.00, ψ= 0.00) in the Ramachandran Plots of two amino acids
Allowed regions (red) for HIS
Allowed regions (red) for LYS
Ramachandran Plots illustrate the backbone dihedral angles (ψ, φ) which are possible for an amino-acid residue in a protein. (ψ,φ) outside the colored regions are of very low possibilities in real proteins.
The deeper the color, the higher the possiblilities (more favorable).
Residue substitution may result in the original (ψ, φ) out of allowed regions. In this case, protein backbone may be alternated to another (ψ, φ). Please note the distance between '+' and 'x' versus the colored regions of their location.
One of our study (in preparation) shows that the changes of Ramachandran probabilities have significant correlation with backbone displacement upon residue substitutions.
Ramachandran Plots obtained the Ramachandran probabilities from Dunbrack Lab.