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. 2012 May 1;4(3):341–348. doi: 10.4161/mabs.19981

Table 2.

 
 H1
 H2
 H3
 L1
 L2
 L3
 F
C
 K
 K
 K
 K
 C
 K
 K
  
Variant
 koff (x 10−5s−1)
 kon (x 105M−1s−1)
 KD [pM]
 Sub.
 30
 31
 32
 58
 96
 99
 100c
 24
 25
 27
 28
 29
 49
 53
 54
 55
 56
 92
 93
 94
 104
D2E7
 13(3)
 7.2(9)
 186(64)
 -
 D
 D
 V
 I
 S
 S
 S
 R
 A
 Q
 G
 I
 Y
 T
 L
 Q
 S
 N
 R
 A
 V
cb1–3
 1.1(4)
 13.43(3)
 8(3)
 10
  
 Q
  
  
  
  
  
 H
  
 R
 K
  
  
 S
  
 L
 R
 D
 K
 P
  
2.1b_9.0_1
 0.8(3)
 6.9(3)
 10(4)
 6
  
 Q
 F
  
  
  
  
  
  
  
  
  
  
 W
  
  
  
 I
 Q
 P
  
3.1d_6.1_2
 0.1*
 7.9(5)
 1.3*
 10
  
 Q
 F
  
  
  
  
  
  
  
 R
 L
  
 S
 T
 I
  
 I
 Q
 P
  
3.1f_12.1_1
 0.4(1)
 18(2)
 2.2(8)
 13
  
 Q
 F
  
 K
  
  
 T
  
  
 R
 L
  
 S
 T
  
 R
 I
 Q
 P
 I
4.2a_6
 0.052(2)
 11(2)
 0.5(7)
 12
 G
 Q
 F
  
  
  
  
  
  
  
 R
 L
 G
 S
 T
 I
  
 I
 Q
 P
  
4.2a_54
 0.011(4)
 12.83(2)
 0.8(3)
 15
 G
 Q
 F
  
 K
  
  
 T
  
  
 R
 L
 W
 S
 T
  
 R
 I
 Q
 P
 I
4.2a_52
 0.06(5)
 13.64(4)
 0.4(4)
 15
 G
 Q
 F
  
 K
  
  
 T
  
  
 R
 L
 G
 S
 T
  
 R
 I
 Q
 P
 I
2.4a_13.3_1
 0.30(4)
 25.79(3)
 1.2(2)
 10
 G
  
  
 V
 K
  
 Q
  
  
  
 R
 V
  
 W
  
 K
  
 D
  
 P
  
2.8a_10.1_1 0.28(3) 14.53(2) 1.9(2) 10   H F V         T M S         K K D   P  

Amino acid substitutions, on- and off-rates and KD of the highest affinity variants from each recombination library. Compared are the D2E7 Fab and cb1–3, the best variant previously generated by yeast display FACS screening.1 C – Contact CDR definition; K – Kabat CDR definition; H1 – CDR H1; F – Framework; Sub – number of amino acid substitutions compared with D2E7. Number in parentheses represents the standard error in the last significant digit. *The intrinsic dissociation rate may be slower than the value shown since slower rates were not resolvable in the assay set-up used to measure this variant.