Biology Reference
In-Depth Information
155
ones, this sum of squares can usually be reduced to less than 1.5 A
2
.
However, it is important to avoid steric hindrance. Since Newm has no
CDRL2, a longer segment from MOPC-315 is used.
For the six CDR's, the structures of the middle ones, i.e. CDRH3 and
CDRL3, are predicted first, followed by those of CDRH1 and CDRL1.
CDRH2 and CDRL2 are on the periphery and their structures are usually
predicted last. The six CDR's form a very compact structure with little
flexibility. In the case of MOPC-315, the final sets of angles for the
six CDR's are illustrated in Tables 6-5. Angles are rounded off to the
nearest degree. Table 6-6 gives the predicted atomic coordinates of the non-
hydrogen backbone atoms. These results were from Stanford (1979).
Table 6-5. Amino acid residue
angles of MOPC-315 CDR's. Adjacent residues are in
parenthesis.
Position (Kabat numbering)
Amino acid residue
angle
-130
0
,+133
0
-155
0
,+131
0
-72
0
,-41
0
-75
0
,+151
0
-112
0
,-16
0
-79
0
,-41
0
-107
0
,+154
0
-63
0
,-47
0
-138
0
,+139
0
(23)
24
25
26
27
27A
27B
27C
28
29
30
31
32
33
34
(35)
(36)
(37)
Cys
Arg
Ser
Ser
Thr-
Gly
Ala
Val
Thr
Thr
Ser
Asn
Tyr
Ala
Asn
Trp
Ile
Gln
CDRL1
-
118
0
,+137
0
+53
0
,+82
0
-66
0
,+108
0
-157
0
,+151
0
-69
0
,+99
0
-124
0
,+91
0
-142
0
,+140
0
-147
0
,+123
0
-130
0
,+123
0
-86
0
,+106
0
-72
0
,-37
0
-152
0
,+133
0
-125
0
,+149
0
-67
0
,-33
0
-79
0
,-38
0
-144
0
,+111
0
CDRL2
(46)
(47)
(48)
(49)
50
51
52
Gly
Leu
Ile
Gly
Gly
Thr
Ser
