Table IV.

Differential Analysis of Charged Surface Residues

	H6UctB	YfdW	FRC
	3ubm	1q6y	1p5r
Total residues in dimer	872	832	856
Surface residues in dimera	526	498	503
No. acidic residues  (Asp & Glu)	93	94	103
No. basic residues  (Arg, His & Lys)	85	76	90
No. bases–no. acids	−8	−18	−13
No. of altered side chain  chargesb	32	32	32
No. making polar protein  contactsc	8	12	16
No. of charged residues	14	18	18
No. bases–no. acids	+6	−14	−10
Computed isoelectric point
Compositiond	5.81	5.36	5.26
Folded proteine	6.60	5.46	5.43

^aResidues with relative side chain accessible surface area of ≥5% in chains A and B, computed using NACCESS.

^bSurface residues that have different charges in 3ubm than in 1q6y/1p5r. A complete residue list is given in Supporting Information Table SII.

^cResidues with side chains that make polar contacts to other side chains, backbone, or ligand. The other residues appear to make polar contacts only to solvent water.

^dComputed using a tool at the EXPASY server.

^eComputed using PROPKA.