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. Author manuscript; available in PMC: 2008 Nov 2.
Published in final edited form as: J Mol Biol. 2007 Aug 21;373(4):941–953. doi: 10.1016/j.jmb.2007.08.027

Table 1.

Interface characteristics of wild-type and affinity-matured cAb-RN05 and related proteins.

Epitope Paratope


Ligand Kd (nM) ΔG (kcal/mol) # of atoms1 Ligand Efficiency Area (Å2) # of atoms1 Efficiency Area (Å2) SC2 Planarity
cAb-RN05
WT 23 10.3 46 0.22 589 47 0.22 613 0.76 2.13
matured 0.15 13.2 63 0.21 562 51 0.26 592 0.78 2.02
Other VHH
D3-L11 (1ZVY) 0.14 13.3 43 0.31 729 58 0.23 649 0.77 2.43
D2-L29 (1ZV5) 10 10.8 45 0.24 759 60 0.18 634 0.75 2.88
cAb-Lys3 (1JTT) 7.5 10.9 68 0.16 690 54 0.20 793 0.75 3.3
cAb-Lys2 (1RI8) 0.077 13.6 52 0.26 795 67 0.20 771 0.71 3.08
D2-L19 (1RJC) 3 11.5 59 0.19 741 60 0.19 644 0.79 2.88
D2-L24 (1ZVH) 80 9.5 63 0.15 528 51 0.19 593 0.82 1.65
cAb-Hu6 (1OP9) 0.7 12.3 45 0.27 556 43 0.29 577 0.76 1.61
Small molecule
SP4206-IL2R (1PY2) 68.8 9.6 44 0.22 422 30 0.32 572 0.77 2.01
1

Atoms within 4Å of the binding partner.

2

Surface complementarity.21