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. Author manuscript; available in PMC: 2018 Jan 1.
Published in final edited form as: Proteins. 2016 Nov 13;85(1):93–102. doi: 10.1002/prot.25201

Figure 4.

Figure 4

ConSurf Analysis. (A) ConSurf per residue scores for the structure RPA3313. Conserved residues are magenta and non-conserved residues are cyan. (B) ConSurf scores mapped onto the molecular surface representation of RPA3313. A conserved pocket is formed between the N-terminus of the α-helix and the first β-strand. Residues found to be less conserved are mostly found in the loop regions and the disordered tail (C-terminus, not shown).