                         SEQUENCE LISTING

<110>  BioNTech SE
 
<120>  BINDING AGENTS FOR CORONAVIRUS S PROTEIN

<130>  674-342 PCT2

<150>  PCT/EP2020/072199
<151>  2020-08-06

<160>  212   

<170>  PatentIn version 3.5

<210>  1
<211>  119
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  1

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Lys Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Gly Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Asp Leu Lys Ile 
65                  70                  75                  80  


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ala 
                85                  90                  95      


Gly Tyr Pro Gly Tyr Ser Pro His Tyr Phe Asn Ile Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Leu 
        115                 


<210>  2
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  2

Lys Tyr Ala Met Ser 
1               5   


<210>  3
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  3

Ile Ile Ser Ser Gly Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  4
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  4

Ala Gly Tyr Pro Gly Tyr Ser Pro His Tyr Phe Asn Ile 
1               5                   10              


<210>  5
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  5

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Thr Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  6
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  6

Lys Ala Ser Glu Asp Ile Gly Tyr Glu Leu Asn 
1               5                   10      


<210>  7
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  7

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  8
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  8

Gln Gln Gly Tyr Ser Thr Pro Pro Thr 
1               5                   


<210>  9
<211>  118
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  9

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ala Met 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Thr Gly Val Tyr Asn Ile Trp Gly Pro Gly Thr 
            100                 105                 110         


Leu Val Thr Val Ser Leu 
        115             


<210>  10
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  10

Ser Tyr Ala Met Ser 
1               5   


<210>  11
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  11

Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  12
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  12

Ala Met Tyr Pro Gly Tyr Ser Thr Gly Val Tyr Asn Ile 
1               5                   10              


<210>  13
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  13

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Asn 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  14
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  14

Lys Ala Ser Glu Asp Ile Gly Tyr Glu Leu Asn 
1               5                   10      


<210>  15
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  15

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  16
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  16

Gln Gln Gly Tyr Asn Thr Pro Asn Thr 
1               5                   


<210>  17
<211>  120
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  17

Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser 
        115                 120 


<210>  18
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  18

Ser Tyr Ala Met Ser 
1               5   


<210>  19
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  19

Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  20
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  20

Asp Ala Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro 
1               5                   10                  15  


<210>  21
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  21

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  22
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  22

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  23
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  23

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  24
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  24

Gln Gln Gly Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  25
<211>  120
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  25

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Asn Ser Gly Arg Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Thr Ser Ile Gly Tyr Tyr Arg Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser 
        115                 120 


<210>  26
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  26

Ser Tyr Ala Met Ser 
1               5   


<210>  27
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  27

Ile Ile Asn Ser Gly Arg Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  28
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  28

Asp Ala Thr Ser Ile Gly Tyr Tyr Arg Tyr Tyr Gly Met Asp Pro 
1               5                   10                  15  


<210>  29
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  29

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  30
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  30

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  31
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  31

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  32
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  32

Gln Gln Gly Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  33
<211>  123
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  33

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Val Gly 
                85                  90                  95      


Ala Gly Tyr Ala Gly Tyr Gly Tyr Asp Asn Tyr Tyr Gly Met Asp Pro 
            100                 105                 110         


Trp Gly Pro Gly Thr Leu Val Thr Val Ser Ser 
        115                 120             


<210>  34
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  34

Ser Tyr Ala Met Asn 
1               5   


<210>  35
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  35

Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  36
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  36

Val Gly Ala Gly Tyr Ala Gly Tyr Gly Tyr Asp Asn Tyr Tyr Gly Met 
1               5                   10                  15      


Asp Pro 
        


<210>  37
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  37

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  38
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  38

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  39
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  39

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  40
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  40

Gln Gln Gly Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  41
<211>  120
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  41

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Pro Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly Gly 
                85                  90                  95      


Ala Gly Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser 
        115                 120 


<210>  42
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  42

Ser Tyr Ala Met Ser 
1               5   


<210>  43
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  43

Ile Ile Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  44
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  44

Gly Gly Ala Gly Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro 
1               5                   10                  15  


<210>  45
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  45

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  46
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  46

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  47
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  47

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  48
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  48

Gln Gln Gly Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  49
<211>  119
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  49

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser 
        115                 


<210>  50
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  50

Asn Tyr Ala Met Asn 
1               5   


<210>  51
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  51

Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 
1               5                   10                  15      


<210>  52
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  52

Asp Ser Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro 
1               5                   10                  


<210>  53
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  53

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Ala Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Thr Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr His Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  54
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  54

Lys Ala Ser Glu Asp Ile Ala Tyr Gly Leu Asn 
1               5                   10      


<210>  55
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  55

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  56
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  56

Gln Gln Gly Tyr Asn Thr Pro Pro Thr 
1               5                   


<210>  57
<211>  132
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  57

Gln Glu Glu Leu Lys Glu Thr Gly Gly Gly Leu Val Gln Pro Gly Gly 
1               5                   10                  15      


Ser Leu Thr Leu Ser Cys Lys Ala Ser Gly Phe Asp Phe Ser Ser Tyr 
            20                  25                  30          


Tyr Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 
        35                  40                  45              


Gly Val Ile Tyr Ala Ser Lys Gly Ser Thr Asp Tyr Ala Ser Trp Val 
    50                  55                  60                  


Asn Gly Arg Phe Thr Ile Ser Ser Asp Asn Ala Gln Asn Thr Val Asp 
65                  70                  75                  80  


Leu Gln Met Asn Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Tyr Cys 
                85                  90                  95      


Ala Arg Ser Lys Arg Phe Tyr Thr Tyr Gly Tyr Ala Gly Tyr Ala Tyr 
            100                 105                 110         


Ala His Tyr Tyr Tyr Gly Met Asp Leu Trp Gly Pro Gly Thr Leu Val 
        115                 120                 125             


Thr Val Ser Ser 
    130         


<210>  58
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  58

Ser Tyr Tyr Met Ser 
1               5   


<210>  59
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  59

Val Ile Tyr Ala Ser Lys Gly Ser Thr Asp Tyr Ala Ser Trp Val Asn 
1               5                   10                  15      


Gly 
    


<210>  60
<211>  23
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  60

Ser Lys Arg Phe Tyr Thr Tyr Gly Tyr Ala Gly Tyr Ala Tyr Ala His 
1               5                   10                  15      


Tyr Tyr Tyr Gly Met Asp Leu 
            20              


<210>  61
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  61

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asp Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  62
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  62

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  63
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  63

Gly Ala Asp Thr Leu Glu Ser 
1               5           


<210>  64
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  64

Gln Gln Gly Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  65
<211>  123
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  65

Gln Glu Leu Val Glu Ser Gly Gly Gly Leu Val Gln Ala Gly Glu Ser 
1               5                   10                  15      


Leu Lys Leu Ser Cys Lys Ala Ser Gly Ile Asp Phe Ser Ser Tyr Gly 
            20                  25                  30          


Ile Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Tyr Ile Tyr Pro Gly Phe Gly Ile Thr Asn Tyr Ala Asn Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Ser Asp Asn Ala Gln Asn Thr Val Phe Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ser Asp Thr Ala Thr Tyr Phe Cys Thr 
                85                  90                  95      


Arg Ala Tyr Ala Ser Ser Ser Gly Tyr Tyr Ile His Tyr Phe Asn Leu 
            100                 105                 110         


Trp Gly Pro Gly Thr Leu Val Thr Val Ser Ser 
        115                 120             


<210>  66
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  66

Ser Tyr Gly Ile Ser 
1               5   


<210>  67
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  67

Tyr Ile Tyr Pro Gly Phe Gly Ile Thr Asn Tyr Ala Asn Ser Val Lys 
1               5                   10                  15      


Gly 
    


<210>  68
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  68

Ala Tyr Ala Ser Ser Ser Gly Tyr Tyr Ile His Tyr Phe Asn Leu 
1               5                   10                  15  


<210>  69
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  69

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Ala Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 
            100                 105         


<210>  70
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  70

Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn 
1               5                   10      


<210>  71
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  71

Gly Ala Asn Thr Leu Glu Ser 
1               5           


<210>  72
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  72

Gln Gln Ala Tyr Ser Thr Pro Leu Thr 
1               5                   


<210>  73
<211>  117
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  73

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Ser Tyr 
            20                  25                  30          


Trp Ile Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 
        35                  40                  45              


Gly Cys Ile Tyr Thr Gly Ser Gly Ser Thr Trp Tyr Ala Ser Trp Ala 
    50                  55                  60                  


Lys Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Arg Gly Tyr Gly Ser Tyr Met Tyr Asp Phe Trp Gly Pro Gly Thr Leu 
            100                 105                 110         


Val Thr Val Ser Ser 
        115         


<210>  74
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  74

Ser Ser Tyr Trp Ile Cys 
1               5       


<210>  75
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  75

Cys Ile Tyr Thr Gly Ser Gly Ser Thr Trp Tyr Ala Ser Trp Ala Lys 
1               5                   10                  15      


Gly 
    


<210>  76
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  76

Gly Tyr Gly Ser Tyr Met Tyr Asp Phe 
1               5                   


<210>  77
<211>  107
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  77

Asp Val Val Met Thr Gln Thr Pro Ala Ser Val Glu Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Lys Cys Gln Ala Ser Gln Ser Ile Ser Thr Ala 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Ser Ala Ser Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Ala Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Gly Ala Asp Gly Ser Ser Ser 
                85                  90                  95      


Ser Phe Gly Gly Gly Thr Glu Val Val Val Lys 
            100                 105         


<210>  78
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  78

Gln Ala Ser Gln Ser Ile Ser Thr Ala Leu Ala 
1               5                   10      


<210>  79
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  79

Ser Ala Ser Thr Leu Glu Ser 
1               5           


<210>  80
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  80

Gln Gly Ala Asp Gly Ser Ser Ser Ser 
1               5                   


<210>  81
<211>  121
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  81

Gln Glu Gln Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Glu Gly 
1               5                   10                  15      


Ser Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asn 
            20                  25                  30          


Tyr Trp Ile Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        35                  40                  45              


Ile Gly Cys Ile Tyr Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp 
    50                  55                  60                  


Ala Lys Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr 
65                  70                  75                  80  


Leu Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                85                  90                  95      


Ala Arg Ser Tyr Thr Pro Gly Ser Tyr Tyr Asn Met Asn Leu Trp Gly 
            100                 105                 110         


Pro Gly Thr Leu Val Thr Val Ser Ser 
        115                 120     


<210>  82
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  82

Ser Asn Tyr Trp Ile Cys 
1               5       


<210>  83
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  83

Cys Ile Tyr Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp Ala Lys 
1               5                   10                  15      


Gly 
    


<210>  84
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  84

Ser Tyr Thr Pro Gly Ser Tyr Tyr Asn Met Asn Leu 
1               5                   10          


<210>  85
<211>  110
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  85

Asp Val Val Met Thr Gln Thr Pro Ser Ser Val Ser Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Asn Cys Gln Ala Ser Gln Gln Ile Ser Asn Glu 
            20                  25                  30          


Leu Ser Trp Tyr Gln Gln Lys Ser Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Asp Ala Ser Asp Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Ser Thr Gly Gly Ala Ser Ser 
                85                  90                  95      


Asp Gly Asn Ala Phe Gly Gly Gly Thr Glu Val Val Val Lys 
            100                 105                 110 


<210>  86
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  86

Gln Ala Ser Gln Gln Ile Ser Asn Glu Leu Ser 
1               5                   10      


<210>  87
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  87

Asp Ala Ser Asp Leu Ala Ser 
1               5           


<210>  88
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  88

Gln Ser Thr Gly Gly Ala Ser Ser Asp Gly Asn Ala 
1               5                   10          


<210>  89
<211>  120
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  89

Gln Ser Leu Glu Glu Ser Gly Gly Gly Leu Val Lys Pro Glu Gly Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Lys Ala Ser Gly Phe Asp Leu Asn Thr Tyr Tyr 
            20                  25                  30          


Tyr Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 
        35                  40                  45              


Ala Cys Ile Ala Thr Ser Asp Ser Gly His Thr Ala Tyr Ala Ser Trp 
    50                  55                  60                  


Ala Arg Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr 
65                  70                  75                  80  


Leu Gln Met Thr Gly Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                85                  90                  95      


Ala Arg Gly Gly Arg Ser Val Gly Asp Gly Val Asp Leu Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser 
        115                 120 


<210>  90
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  90

Thr Tyr Tyr Tyr Met Cys 
1               5       


<210>  91
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  91

Cys Ile Ala Thr Ser Asp Ser Gly His Thr Ala Tyr Ala Ser Trp Ala 
1               5                   10                  15      


Arg Gly 
        


<210>  92
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  92

Gly Gly Arg Ser Val Gly Asp Gly Val Asp Leu 
1               5                   10      


<210>  93
<211>  112
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  93

Asp Ile Val Met Thr Gln Thr Pro Ala Ser Val Glu Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Lys Cys Gln Ala Ser Gln Ser Ile Ser Ser Trp 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Asp Ala Ser Asp Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Ser Tyr Leu Tyr Val Glu Ser 
                85                  90                  95      


Gly Ser His Gly Phe Gly Phe Gly Gly Gly Thr Glu Val Val Val Arg 
            100                 105                 110         


<210>  94
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  94

Gln Ala Ser Gln Ser Ile Ser Ser Trp Leu Ala 
1               5                   10      


<210>  95
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  95

Asp Ala Ser Asp Leu Ala Ser 
1               5           


<210>  96
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  96

Gln Ser Tyr Leu Tyr Val Glu Ser Gly Ser His Gly Phe Gly 
1               5                   10                  


<210>  97
<211>  120
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  97

Gln Ser Leu Glu Glu Ser Gly Gly Gly Leu Val Lys Pro Glu Gly Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Lys Ala Ser Gly Phe Asp Leu Asn Thr Tyr Tyr 
            20                  25                  30          


Tyr Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 
        35                  40                  45              


Ala Cys Ile Gly Thr Ser Asp Ser Gly His Thr Ala Tyr Ala Ser Trp 
    50                  55                  60                  


Ala Arg Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr 
65                  70                  75                  80  


Leu Gln Met Thr Gly Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                85                  90                  95      


Ala Arg Gly Gly Arg Ser Val Gly Asp Gly Val Asp Leu Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser 
        115                 120 


<210>  98
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  98

Thr Tyr Tyr Tyr Met Cys 
1               5       


<210>  99
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  99

Cys Ile Gly Thr Ser Asp Ser Gly His Thr Ala Tyr Ala Ser Trp Ala 
1               5                   10                  15      


Arg Gly 
        


<210>  100
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  100

Gly Gly Arg Ser Val Gly Asp Gly Val Asp Leu 
1               5                   10      


<210>  101
<211>  112
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  101

Asp Ile Val Met Thr Gln Thr Pro Ala Ser Val Glu Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Lys Cys Gln Ala Ser Gln Ser Ile Ser Ser Trp 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Asp Ala Phe Asp Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Ser Tyr Leu Tyr Gly Glu Ser 
                85                  90                  95      


Gly Ser His Gly Phe Gly Phe Gly Gly Gly Thr Glu Val Val Val Arg 
            100                 105                 110         


<210>  102
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  102

Gln Ala Ser Gln Ser Ile Ser Ser Trp Leu Ala 
1               5                   10      


<210>  103
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  103

Asp Ala Phe Asp Leu Ala Ser 
1               5           


<210>  104
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  104

Gln Ser Tyr Leu Tyr Gly Glu Ser Gly Ser His Gly Phe Gly 
1               5                   10                  


<210>  105
<211>  119
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  105

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly 
            20                  25                  30          


Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
    50                  55                  60                  


Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser 
        115                 


<210>  106
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  106

Ser Asp Gly Met Cys 
1               5   


<210>  107
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  107

Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
1               5                   10                  15      


Gln Gly 
        


<210>  108
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  108

Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu 
1               5                   10      


<210>  109
<211>  110
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  109

Ala Ile Asp Met Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser 
65                  70                  75                  80  


Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp 
                85                  90                  95      


Ala Asp Asn Thr Phe Gly Gly Gly Thr Glu Val Val Val Lys 
            100                 105                 110 


<210>  110
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  110

Gln Ala Ser Glu Asn Ile Tyr Ser Phe Leu Ala 
1               5                   10      


<210>  111
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  111

Phe Ala Ser Lys Leu Ala Ser 
1               5           


<210>  112
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  112

Gln Gln Thr Gly Thr Tyr Ser Asp Ala Asp Asn Thr 
1               5                   10          


<210>  113
<211>  117
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  113

Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Leu Ser Ser Tyr Trp 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Tyr Val Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Met Thr 
65                  70                  75                  80  


Ser Leu Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Val Asp 
                85                  90                  95      


Tyr Ser Thr Gly Trp Pro Leu Phe Asn Ile Trp Gly Pro Gly Thr Leu 
            100                 105                 110         


Val Thr Val Ser Leu 
        115         


<210>  114
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  114

Ser Tyr Trp Met Ser 
1               5   


<210>  115
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  115

Ile Ile Tyr Val Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
1               5                   10                  15      


<210>  116
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  116

Val Asp Tyr Ser Thr Gly Trp Pro Leu Phe Asn Ile 
1               5                   10          


<210>  117
<211>  110
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  117

Ala Gln Val Leu Thr Gln Thr Ala Ser Pro Val Ser Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Asn Cys Gln Ser Ser Gln Ser Val Tyr Asp Asn 
            20                  25                  30          


Asn Trp Leu Gly Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu 
        35                  40                  45              


Leu Ile Tyr Gly Ala Ser Ile Leu Ala Ser Gly Val Pro Ser Arg Phe 
    50                  55                  60                  


Lys Gly Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Leu 
65                  70                  75                  80  


Glu Ser Asp Asp Ala Ala Thr Tyr Tyr Cys Gln Gly Gly Cys Ser Gly 
                85                  90                  95      


Asn Thr Phe Val Phe Gly Gly Gly Thr Glu Val Val Val Lys 
            100                 105                 110 


<210>  118
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  118

Gln Ser Ser Gln Ser Val Tyr Asp Asn Asn Trp Leu Gly 
1               5                   10              


<210>  119
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  119

Gly Ala Ser Ile Leu Ala Ser 
1               5           


<210>  120
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  120

Gln Gly Gly Cys Ser Gly Asn Thr Phe Val 
1               5                   10  


<210>  121
<211>  117
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  HC VR

<400>  121

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val 
        115         


<210>  122
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H1

<400>  122

Thr Tyr Trp Ile Gly 
1               5   


<210>  123
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H2

<400>  123

Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln 
1               5                   10                  15      


Gly 
    


<210>  124
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-H3

<400>  124

Gly Ser Gly Ile Ser Thr Pro Met Asp Val 
1               5                   10  


<210>  125
<211>  113
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  LC VR

<400>  125

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys 
    


<210>  126
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L1

<400>  126

Lys Ser Ser Gln Ser Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu 
1               5                   10                  15      


Ala 
    


<210>  127
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L2

<400>  127

Trp Ala Ser Thr Arg Glu Ser 
1               5           


<210>  128
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  CDR-L3

<400>  128

Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr 
1               5                   


<210>  129
<211>  598
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  ACE2 ECD Mutant

<400>  129

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp 
        595             


<210>  130
<211>  805
<212>  PRT
<213>  Homo sapiens

<400>  130

Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 
1               5                   10                  15      


Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe 
            20                  25                  30          


Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 
        35                  40                  45              


Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 
    50                  55                  60                  


Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 
65                  70                  75                  80  


Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 
                85                  90                  95      


Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 
            100                 105                 110         


Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 
        115                 120                 125             


Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 
    130                 135                 140                 


Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 
145                 150                 155                 160 


Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 
                165                 170                 175     


Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 
            180                 185                 190         


Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu 
        195                 200                 205             


Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 
    210                 215                 220                 


Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu 
225                 230                 235                 240 


His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 
                245                 250                 255     


Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 
            260                 265                 270         


Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 
        275                 280                 285             


Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 
    290                 295                 300                 


Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 
305                 310                 315                 320 


Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 
                325                 330                 335     


Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 
            340                 345                 350         


Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp 
        355                 360                 365             


Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met Ala 
    370                 375                 380                 


Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe 
385                 390                 395                 400 


His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys 
                405                 410                 415     


His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn 
            420                 425                 430         


Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly 
        435                 440                 445             


Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe 
    450                 455                 460                 


Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met 
465                 470                 475                 480 


Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr 
                485                 490                 495     


Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe 
            500                 505                 510         


Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala 
        515                 520                 525             


Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile 
    530                 535                 540                 


Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu 
545                 550                 555                 560 


Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala 
                565                 570                 575     


Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe 
            580                 585                 590         


Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr 
        595                 600                 605             


Asp Trp Ser Pro Tyr Ala Asp Gln Ser Ile Lys Val Arg Ile Ser Leu 
    610                 615                 620                 


Lys Ser Ala Leu Gly Asp Lys Ala Tyr Glu Trp Asn Asp Asn Glu Met 
625                 630                 635                 640 


Tyr Leu Phe Arg Ser Ser Val Ala Tyr Ala Met Arg Gln Tyr Phe Leu 
                645                 650                 655     


Lys Val Lys Asn Gln Met Ile Leu Phe Gly Glu Glu Asp Val Arg Val 
            660                 665                 670         


Ala Asn Leu Lys Pro Arg Ile Ser Phe Asn Phe Phe Val Thr Ala Pro 
        675                 680                 685             


Lys Asn Val Ser Asp Ile Ile Pro Arg Thr Glu Val Glu Lys Ala Ile 
    690                 695                 700                 


Arg Met Ser Arg Ser Arg Ile Asn Asp Ala Phe Arg Leu Asn Asp Asn 
705                 710                 715                 720 


Ser Leu Glu Phe Leu Gly Ile Gln Pro Thr Leu Gly Pro Pro Asn Gln 
                725                 730                 735     


Pro Pro Val Ser Ile Trp Leu Ile Val Phe Gly Val Val Met Gly Val 
            740                 745                 750         


Ile Val Val Gly Ile Val Ile Leu Ile Phe Thr Gly Ile Arg Asp Arg 
        755                 760                 765             


Lys Lys Lys Asn Lys Ala Arg Ser Gly Glu Asn Pro Tyr Ala Ser Ile 
    770                 775                 780                 


Asp Ile Ser Lys Gly Glu Asn Asn Pro Gly Phe Gln Asn Thr Asp Asp 
785                 790                 795                 800 


Val Gln Thr Ser Phe 
                805 


<210>  131
<211>  830
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent

<400>  131

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Glu Pro Lys Ser Cys Asp Lys Thr His Thr 
        595                 600                 605             


Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe 
    610                 615                 620                 


Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro 
625                 630                 635                 640 


Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val 
                645                 650                 655     


Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr 
            660                 665                 670         


Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val 
        675                 680                 685             


Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys 
    690                 695                 700                 


Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser 
705                 710                 715                 720 


Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro 
                725                 730                 735     


Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val 
            740                 745                 750         


Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly 
        755                 760                 765             


Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp 
    770                 775                 780                 


Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp 
785                 790                 795                 800 


Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His 
                805                 810                 815     


Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
            820                 825                 830 


<210>  132
<211>  830
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent

<400>  132

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Glu Pro Lys Ser Cys Asp Lys Thr His Thr 
        595                 600                 605             


Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe 
    610                 615                 620                 


Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro 
625                 630                 635                 640 


Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val 
                645                 650                 655     


Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr 
            660                 665                 670         


Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val 
        675                 680                 685             


Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys 
    690                 695                 700                 


Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser 
705                 710                 715                 720 


Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro 
                725                 730                 735     


Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val 
            740                 745                 750         


Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly 
        755                 760                 765             


Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp 
    770                 775                 780                 


Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp 
785                 790                 795                 800 


Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu His 
                805                 810                 815     


Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
            820                 825                 830 


<210>  133
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  133

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  134
<211>  838
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  134

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        595                 600                 605             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln 
    610                 615                 620                 


Ser Pro Asp Ser Leu Ala Val Ser Leu Gly Glu Arg Ala Thr Ile Asn 
625                 630                 635                 640 


Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr 
                645                 650                 655     


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
            660                 665                 670         


Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val Pro Asp Arg Phe Ser Gly 
        675                 680                 685             


Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala 
    690                 695                 700                 


Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr 
705                 710                 715                 720 


Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
                725                 730                 735     


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
            740                 745                 750         


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
        755                 760                 765             


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
    770                 775                 780                 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
785                 790                 795                 800 


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
                805                 810                 815     


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
            820                 825                 830         


Phe Asn Arg Gly Glu Cys 
        835             


<210>  135
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  135

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  136
<211>  843
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  136

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        595                 600                 605             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Asp 
    610                 615                 620                 


Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly Glu 
625                 630                 635                 640 


Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser Ser 
                645                 650                 655     


Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro 
            660                 665                 670         


Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val Pro 
        675                 680                 685             


Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile 
    690                 695                 700                 


Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln Tyr 
705                 710                 715                 720 


Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 
                725                 730                 735     


Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu 
            740                 745                 750         


Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe 
        755                 760                 765             


Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln 
    770                 775                 780                 


Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser 
785                 790                 795                 800 


Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu 
                805                 810                 815     


Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser 
            820                 825                 830         


Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys 
        835                 840             


<210>  137
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  137

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  138
<211>  838
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  138

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
225                 230                 235                 240 


Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
                245                 250                 255     


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            260                 265                 270         


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        275                 280                 285             


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    290                 295                 300                 


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
305                 310                 315                 320 


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                325                 330                 335     


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            340                 345                 350         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        355                 360                 365             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    370                 375                 380                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
385                 390                 395                 400 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                405                 410                 415     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            420                 425                 430         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        435                 440                 445             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    450                 455                 460                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
465                 470                 475                 480 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                485                 490                 495     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            500                 505                 510         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        515                 520                 525             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    530                 535                 540                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
545                 550                 555                 560 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                565                 570                 575     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            580                 585                 590         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        595                 600                 605             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    610                 615                 620                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
625                 630                 635                 640 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                645                 650                 655     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            660                 665                 670         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        675                 680                 685             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    690                 695                 700                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
705                 710                 715                 720 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                725                 730                 735     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            740                 745                 750         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        755                 760                 765             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    770                 775                 780                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
785                 790                 795                 800 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                805                 810                 815     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            820                 825                 830         


Trp Ser Pro Tyr Ala Asp 
        835             


<210>  139
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  139

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  140
<211>  842
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  140

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
225                 230                 235                 240 


Gly Gly Gly Ser Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu 
                245                 250                 255     


Asp Lys Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu 
            260                 265                 270         


Ala Ser Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn 
        275                 280                 285             


Met Asn Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser 
    290                 295                 300                 


Thr Leu Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val 
305                 310                 315                 320 


Lys Leu Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser 
                325                 330                 335     


Glu Asp Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr 
            340                 345                 350         


Ile Tyr Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys 
        355                 360                 365             


Leu Leu Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp 
    370                 375                 380                 


Tyr Asn Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly 
385                 390                 395                 400 


Lys Gln Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu 
                405                 410                 415     


Met Ala Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly 
            420                 425                 430         


Asp Tyr Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln 
        435                 440                 445             


Leu Ile Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr 
    450                 455                 460                 


Glu His Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro 
465                 470                 475                 480 


Ser Tyr Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp 
                485                 490                 495     


Met Trp Gly Gln Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe 
            500                 505                 510         


Gly Gln Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala 
        515                 520                 525             


Trp Asp Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser 
    530                 535                 540                 


Val Gly Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu 
545                 550                 555                 560 


Thr Asp Pro Gly Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp 
                565                 570                 575     


Asp Leu Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr 
            580                 585                 590         


Met Asp Asp Phe Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr 
        595                 600                 605             


Asp Met Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn 
    610                 615                 620                 


Glu Gly Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala 
625                 630                 635                 640 


Thr Pro Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln 
                645                 650                 655     


Glu Asp Asn Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr 
            660                 665                 670         


Ile Val Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp 
        675                 680                 685             


Met Val Phe Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp 
    690                 695                 700                 


Trp Glu Met Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His 
705                 710                 715                 720 


Asp Glu Thr Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp 
                725                 730                 735     


Tyr Ser Phe Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe 
            740                 745                 750         


Gln Glu Ala Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys 
        755                 760                 765             


Cys Asp Ile Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met 
    770                 775                 780                 


Leu Arg Leu Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val 
785                 790                 795                 800 


Val Gly Ala Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu 
                805                 810                 815     


Pro Leu Phe Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly 
            820                 825                 830         


Trp Ser Thr Asp Trp Ser Pro Tyr Ala Asp 
        835                 840         


<210>  141
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  141

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  142
<211>  220
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  142

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys 
    210                 215                 220 


<210>  143
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  143

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
            420                 425                 430         


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  144
<211>  838
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  144

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        595                 600                 605             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln 
    610                 615                 620                 


Ser Pro Asp Ser Leu Ala Val Ser Leu Gly Glu Arg Ala Thr Ile Asn 
625                 630                 635                 640 


Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr 
                645                 650                 655     


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
            660                 665                 670         


Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val Pro Asp Arg Phe Ser Gly 
        675                 680                 685             


Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala 
    690                 695                 700                 


Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr 
705                 710                 715                 720 


Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
                725                 730                 735     


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
            740                 745                 750         


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
        755                 760                 765             


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
    770                 775                 780                 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
785                 790                 795                 800 


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
                805                 810                 815     


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
            820                 825                 830         


Phe Asn Arg Gly Glu Cys 
        835             


<210>  145
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  145

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
            420                 425                 430         


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  146
<211>  843
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  146

Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
1               5                   10                  15      


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            20                  25                  30          


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        35                  40                  45              


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    50                  55                  60                  


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
65                  70                  75                  80  


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                85                  90                  95      


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            100                 105                 110         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        115                 120                 125             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    130                 135                 140                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
145                 150                 155                 160 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                165                 170                 175     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            180                 185                 190         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        195                 200                 205             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    210                 215                 220                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
225                 230                 235                 240 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                245                 250                 255     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            260                 265                 270         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        275                 280                 285             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    290                 295                 300                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
305                 310                 315                 320 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                325                 330                 335     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            340                 345                 350         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        355                 360                 365             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    370                 375                 380                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
385                 390                 395                 400 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                405                 410                 415     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            420                 425                 430         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        435                 440                 445             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    450                 455                 460                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
465                 470                 475                 480 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                485                 490                 495     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            500                 505                 510         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        515                 520                 525             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    530                 535                 540                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
545                 550                 555                 560 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                565                 570                 575     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            580                 585                 590         


Trp Ser Pro Tyr Ala Asp Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        595                 600                 605             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Asp 
    610                 615                 620                 


Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly Glu 
625                 630                 635                 640 


Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser Ser 
                645                 650                 655     


Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro 
            660                 665                 670         


Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val Pro 
        675                 680                 685             


Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile 
    690                 695                 700                 


Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln Tyr 
705                 710                 715                 720 


Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 
                725                 730                 735     


Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu 
            740                 745                 750         


Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe 
        755                 760                 765             


Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln 
    770                 775                 780                 


Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser 
785                 790                 795                 800 


Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu 
                805                 810                 815     


Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser 
            820                 825                 830         


Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys 
        835                 840             


<210>  147
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  147

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
            420                 425                 430         


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  148
<211>  838
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  148

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
225                 230                 235                 240 


Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn 
                245                 250                 255     


His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn 
            260                 265                 270         


Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala 
        275                 280                 285             


Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln 
    290                 295                 300                 


Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln Leu 
305                 310                 315                 320 


Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys Ser 
                325                 330                 335     


Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser Thr 
            340                 345                 350         


Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu Glu 
        355                 360                 365             


Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu Arg 
    370                 375                 380                 


Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu Arg 
385                 390                 395                 400 


Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg Ala 
                405                 410                 415     


Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu Val 
            420                 425                 430         


Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu Asp 
        435                 440                 445             


Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu His 
    450                 455                 460                 


Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile Ser 
465                 470                 475                 480 


Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly Gln 
                485                 490                 495     


Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys Pro 
            500                 505                 510         


Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala Gln 
        515                 520                 525             


Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu Pro 
    530                 535                 540                 


Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro Gly 
545                 550                 555                 560 


Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp Asp Leu Gly Lys 
                565                 570                 575     


Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp Phe 
            580                 585                 590         


Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr Asp Met Ala Tyr 
        595                 600                 605             


Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe His 
    610                 615                 620                 


Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys His 
625                 630                 635                 640 


Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn Glu 
                645                 650                 655     


Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly Thr 
            660                 665                 670         


Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe Lys 
        675                 680                 685             


Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met Lys 
    690                 695                 700                 


Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr Tyr 
705                 710                 715                 720 


Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe Ile 
                725                 730                 735     


Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala Leu 
            740                 745                 750         


Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile Ser 
        755                 760                 765             


Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu Gly 
    770                 775                 780                 


Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala Lys 
785                 790                 795                 800 


Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe Thr 
                805                 810                 815     


Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr Asp 
            820                 825                 830         


Trp Ser Pro Tyr Ala Asp 
        835             


<210>  149
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  149

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
            420                 425                 430         


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  150
<211>  842
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  150

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
225                 230                 235                 240 


Gly Gly Gly Ser Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu 
                245                 250                 255     


Asp Lys Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu 
            260                 265                 270         


Ala Ser Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn 
        275                 280                 285             


Met Asn Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser 
    290                 295                 300                 


Thr Leu Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val 
305                 310                 315                 320 


Lys Leu Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser 
                325                 330                 335     


Glu Asp Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr 
            340                 345                 350         


Ile Tyr Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys 
        355                 360                 365             


Leu Leu Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp 
    370                 375                 380                 


Tyr Asn Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly 
385                 390                 395                 400 


Lys Gln Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu 
                405                 410                 415     


Met Ala Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly 
            420                 425                 430         


Asp Tyr Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln 
        435                 440                 445             


Leu Ile Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr 
    450                 455                 460                 


Glu His Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro 
465                 470                 475                 480 


Ser Tyr Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp 
                485                 490                 495     


Met Trp Gly Gln Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe 
            500                 505                 510         


Gly Gln Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala 
        515                 520                 525             


Trp Asp Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser 
    530                 535                 540                 


Val Gly Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu 
545                 550                 555                 560 


Thr Asp Pro Gly Asn Val Gln Lys Ala Val Cys Leu Pro Thr Ala Trp 
                565                 570                 575     


Asp Leu Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr 
            580                 585                 590         


Met Asp Asp Phe Leu Thr Ala His Asn Glu Met Gly Asn Ile Gln Tyr 
        595                 600                 605             


Asp Met Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn 
    610                 615                 620                 


Glu Gly Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala 
625                 630                 635                 640 


Thr Pro Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln 
                645                 650                 655     


Glu Asp Asn Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr 
            660                 665                 670         


Ile Val Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp 
        675                 680                 685             


Met Val Phe Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp 
    690                 695                 700                 


Trp Glu Met Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His 
705                 710                 715                 720 


Asp Glu Thr Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp 
                725                 730                 735     


Tyr Ser Phe Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe 
            740                 745                 750         


Gln Glu Ala Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys 
        755                 760                 765             


Cys Asp Ile Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met 
    770                 775                 780                 


Leu Arg Leu Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val 
785                 790                 795                 800 


Val Gly Ala Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu 
                805                 810                 815     


Pro Leu Phe Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly 
            820                 825                 830         


Trp Ser Thr Asp Trp Ser Pro Tyr Ala Asp 
        835                 840         


<210>  151
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  151

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
            420                 425                 430         


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  152
<211>  220
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  152

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys 
    210                 215                 220 


<210>  153
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  153

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  154
<211>  491
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  154

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr 
            260                 265                 270         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Val 
                325                 330                 335     


Gly Ala Gly Tyr Ala Gly Tyr Gly Tyr Asp Asn Tyr Tyr Gly Met Asp 
            340                 345                 350         


Pro Trp Gly Pro Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
    370                 375                 380                 


Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
385                 390                 395                 400 


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
                405                 410                 415     


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
            420                 425                 430         


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
        435                 440                 445             


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
    450                 455                 460                 


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
465                 470                 475                 480 


Thr Phe Gly Cys Gly Thr Lys Val Glu Ile Lys 
                485                 490     


<210>  155
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  155

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  156
<211>  487
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  156

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Lys Tyr 
            260                 265                 270         


Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Gly Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Asp Leu Lys 
305                 310                 315                 320 


Ile Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg 
                325                 330                 335     


Ala Gly Tyr Pro Gly Tyr Ser Pro His Tyr Phe Asn Ile Trp Gly Pro 
            340                 345                 350         


Gly Thr Leu Val Thr Val Ser Leu Gly Gly Gly Gly Ser Gly Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met 
    370                 375                 380                 


Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr 
385                 390                 395                 400 


Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu Leu Asn Trp Tyr 
                405                 410                 415     


Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala Asn 
            420                 425                 430         


Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Thr Gly Ser Gly Ser Glu 
        435                 440                 445             


Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly 
    450                 455                 460                 


Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Pro Thr Phe Gly Cys 
465                 470                 475                 480 


Gly Thr Lys Val Glu Ile Lys 
                485         


<210>  157
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  157

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  158
<211>  486
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  158

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr 
            260                 265                 270         


Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ala 
                325                 330                 335     


Met Tyr Pro Gly Tyr Ser Thr Gly Val Tyr Asn Ile Trp Gly Pro Gly 
            340                 345                 350         


Thr Leu Val Thr Val Ser Leu Gly Gly Gly Gly Ser Gly Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr 
    370                 375                 380                 


Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile 
385                 390                 395                 400 


Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu Leu Asn Trp Tyr Gln 
                405                 410                 415     


Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr 
            420                 425                 430         


Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr 
        435                 440                 445             


Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile 
    450                 455                 460                 


Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Asn Thr Phe Gly Cys Gly 
465                 470                 475                 480 


Thr Lys Val Glu Ile Lys 
                485     


<210>  159
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  159

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  160
<211>  488
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  160

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr 
            260                 265                 270         


Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Asn Ser Gly Arg Ser Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp 
                325                 330                 335     


Ala Thr Ser Ile Gly Tyr Tyr Arg Tyr Tyr Gly Met Asp Pro Trp Gly 
            340                 345                 350         


Pro Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        355                 360                 365             


Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln 
    370                 375                 380                 


Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val 
385                 390                 395                 400 


Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp 
                405                 410                 415     


Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala 
            420                 425                 430         


Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser 
        435                 440                 445             


Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala 
    450                 455                 460                 


Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly 
465                 470                 475                 480 


Cys Gly Thr Lys Val Glu Ile Lys 
                485             


<210>  161
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  161

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  162
<211>  488
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  162

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr 
            260                 265                 270         


Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Pro Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly 
                325                 330                 335     


Gly Ala Gly Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro Trp Gly 
            340                 345                 350         


Pro Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        355                 360                 365             


Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln 
    370                 375                 380                 


Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val 
385                 390                 395                 400 


Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp 
                405                 410                 415     


Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala 
            420                 425                 430         


Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser 
        435                 440                 445             


Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala 
    450                 455                 460                 


Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly 
465                 470                 475                 480 


Cys Gly Thr Lys Val Glu Ile Lys 
                485             


<210>  163
<211>  453
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  163

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Val Gly 
                85                  90                  95      


Ala Gly Tyr Ala Gly Tyr Gly Tyr Asp Asn Tyr Tyr Gly Met Asp Pro 
            100                 105                 110         


Trp Gly Pro Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly 
        115                 120                 125             


Pro Ser Val Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly 
    130                 135                 140                 


Thr Ala Ala Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val 
145                 150                 155                 160 


Thr Val Ser Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe 
                165                 170                 175     


Pro Ala Val Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val 
            180                 185                 190         


Thr Val Pro Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val 
        195                 200                 205             


Asn His Lys Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys 
    210                 215                 220                 


Ser Cys Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala 
225                 230                 235                 240 


Ala Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr 
                245                 250                 255     


Leu Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val 
            260                 265                 270         


Ser His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val 
        275                 280                 285             


Glu Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser 
    290                 295                 300                 


Thr Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu 
305                 310                 315                 320 


Asn Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala 
                325                 330                 335     


Pro Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro 
            340                 345                 350         


Gln Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln 
        355                 360                 365             


Val Ser Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala 
    370                 375                 380                 


Val Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr 
385                 390                 395                 400 


Pro Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu 
                405                 410                 415     


Thr Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser 
            420                 425                 430         


Val Leu His Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser 
        435                 440                 445             


Leu Ser Pro Gly Lys 
    450             


<210>  164
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  164

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  165
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  165

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Asn Ser Gly Arg Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Thr Ser Ile Gly Tyr Tyr Arg Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  166
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  166

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  167
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  167

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Pro Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly Gly 
                85                  90                  95      


Ala Gly Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  168
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  168

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  169
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  169

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Lys Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Gly Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Asp Leu Lys Ile 
65                  70                  75                  80  


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ala 
                85                  90                  95      


Gly Tyr Pro Gly Tyr Ser Pro His Tyr Phe Asn Ile Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Leu Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  170
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  170

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Thr Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  171
<211>  448
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  171

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ala Met 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Thr Gly Val Tyr Asn Ile Trp Gly Pro Gly Thr 
            100                 105                 110         


Leu Val Thr Val Ser Leu Ala Ser Thr Lys Gly Pro Ser Val Phe Pro 
        115                 120                 125             


Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly 
    130                 135                 140                 


Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn 
145                 150                 155                 160 


Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln 
                165                 170                 175     


Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser 
            180                 185                 190         


Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser 
        195                 200                 205             


Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr 
    210                 215                 220                 


His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser 
225                 230                 235                 240 


Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg 
                245                 250                 255     


Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro 
            260                 265                 270         


Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala 
        275                 280                 285             


Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val 
    290                 295                 300                 


Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr 
305                 310                 315                 320 


Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr 
                325                 330                 335     


Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu 
            340                 345                 350         


Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys 
        355                 360                 365             


Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser 
    370                 375                 380                 


Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp 
385                 390                 395                 400 


Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser 
                405                 410                 415     


Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala 
            420                 425                 430         


Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445             


<210>  172
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  172

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Glu 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Asn 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  173
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  173

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  174
<211>  488
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  174

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr 
            260                 265                 270         


Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp 
                325                 330                 335     


Ala Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly 
            340                 345                 350         


Pro Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        355                 360                 365             


Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln 
    370                 375                 380                 


Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val 
385                 390                 395                 400 


Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp 
                405                 410                 415     


Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala 
            420                 425                 430         


Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser 
        435                 440                 445             


Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala 
    450                 455                 460                 


Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly 
465                 470                 475                 480 


Cys Gly Thr Lys Val Glu Ile Lys 
                485             


<210>  175
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  175

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  176
<211>  487
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  176

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr 
                245                 250                 255     


Pro Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr 
            260                 265                 270         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Gly Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys 
    290                 295                 300                 


Gly Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile 
305                 310                 315                 320 


Thr Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp 
                325                 330                 335     


Ser Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            340                 345                 350         


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met 
    370                 375                 380                 


Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr 
385                 390                 395                 400 


Ile Thr Cys Lys Ala Ser Glu Asp Ile Ala Tyr Gly Leu Asn Trp Tyr 
                405                 410                 415     


Gln Gln Lys Leu Gly Ile Thr Pro Lys Leu Leu Ile Tyr Gly Ala Asn 
            420                 425                 430         


Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu 
        435                 440                 445             


Thr His Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly 
    450                 455                 460                 


Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Pro Thr Phe Gly Cys 
465                 470                 475                 480 


Gly Thr Lys Val Glu Ile Lys 
                485         


<210>  177
<211>  447
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  177

Gln Met Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu 
1               5                   10                  15      


Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr 
            20                  25                  30          


Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 
        35                  40                  45              


Gly Ile Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe 
    50                  55                  60                  


Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 
65                  70                  75                  80  


Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Gly Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly 
            100                 105                 110         


Thr Thr Val Thr Val Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu 
        115                 120                 125             


Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys 
    130                 135                 140                 


Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser 
145                 150                 155                 160 


Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser 
                165                 170                 175     


Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser 
            180                 185                 190         


Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn 
        195                 200                 205             


Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys Thr His 
    210                 215                 220                 


Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro Ser Val 
225                 230                 235                 240 


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
                245                 250                 255     


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
            260                 265                 270         


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
        275                 280                 285             


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
    290                 295                 300                 


Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys 
305                 310                 315                 320 


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
                325                 330                 335     


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
            340                 345                 350         


Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
        355                 360                 365             


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
    370                 375                 380                 


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
385                 390                 395                 400 


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
                405                 410                 415     


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu Ala Leu 
            420                 425                 430         


His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
        435                 440                 445         


<210>  178
<211>  490
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  178

Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 
1               5                   10                  15      


Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 
            20                  25                  30          


Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
        35                  40                  45              


Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 
    50                  55                  60                  


Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 
65                  70                  75                  80  


Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 
                85                  90                  95      


Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 
            100                 105                 110         


Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp 
        115                 120                 125             


Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn 
    130                 135                 140                 


Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu 
145                 150                 155                 160 


Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp 
                165                 170                 175     


Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr 
            180                 185                 190         


Glu Lys His Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser 
        195                 200                 205             


Ser Pro Val Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly 
    210                 215                 220                 


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
225                 230                 235                 240 


Ser Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala 
                245                 250                 255     


Ser Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp 
            260                 265                 270         


Gly Met Cys Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile 
        275                 280                 285             


Ala Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp 
    290                 295                 300                 


Ala Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr 
305                 310                 315                 320 


Leu Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                325                 330                 335     


Ala Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro 
            340                 345                 350         


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Asp Met 
    370                 375                 380                 


Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly Asp Thr Val Thr 
385                 390                 395                 400 


Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe Leu Ala Trp Tyr 
                405                 410                 415     


Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Phe Ala Ser 
            420                 425                 430         


Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly 
        435                 440                 445             


Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser Asp Asp Ala Ala 
    450                 455                 460                 


Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp Ala Asp Asn Thr 
465                 470                 475                 480 


Phe Gly Cys Gly Thr Glu Val Val Val Lys 
                485                 490 


<210>  179
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  179

Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  180
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  180

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  181
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  181

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  182
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  182

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Ala Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Thr Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr His Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met Gln Leu Val 
225                 230                 235                 240 


Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu Lys Ile Ser 
                245                 250                 255     


Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile Gly Trp Val 
            260                 265                 270         


Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile Ile Tyr Pro 
        275                 280                 285             


Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly Gln Val Thr 
    290                 295                 300                 


Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln Trp Ser Ser 
305                 310                 315                 320 


Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly Gly Ser Gly 
                325                 330                 335     


Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val 
            340                 345                 350         


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp Ser Leu Ala 
    370                 375                 380                 


Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser 
385                 390                 395                 400 


Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln 
                405                 410                 415     


Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg 
            420                 425                 430         


Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 
        435                 440                 445             


Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  183
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  183

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly 
            20                  25                  30          


Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
    50                  55                  60                  


Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  184
<211>  488
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  184

Ala Ile Asp Met Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser 
65                  70                  75                  80  


Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp 
                85                  90                  95      


Ala Asp Asn Thr Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Met 
225                 230                 235                 240 


Gln Leu Val Gln Ser Gly Thr Glu Val Lys Lys Pro Gly Glu Ser Leu 
                245                 250                 255     


Lys Ile Ser Cys Lys Gly Ser Gly Tyr Gly Phe Ile Thr Tyr Trp Ile 
            260                 265                 270         


Gly Trp Val Arg Gln Met Pro Gly Lys Cys Leu Glu Trp Met Gly Ile 
        275                 280                 285             


Ile Tyr Pro Gly Asp Ser Glu Thr Arg Tyr Ser Pro Ser Phe Gln Gly 
    290                 295                 300                 


Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr Leu Gln 
305                 310                 315                 320 


Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys Ala Gly 
                325                 330                 335     


Gly Ser Gly Ile Ser Thr Pro Met Asp Val Trp Gly Gln Gly Thr Thr 
            340                 345                 350         


Val Thr Val Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Gly Ser Asp Ile Gln Leu Thr Gln Ser Pro Asp 
    370                 375                 380                 


Ser Leu Ala Val Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys Lys Ser 
385                 390                 395                 400 


Ser Gln Ser Val Leu Tyr Ser Ser Ile Asn Lys Asn Tyr Leu Ala Trp 
                405                 410                 415     


Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile Tyr Trp Ala 
            420                 425                 430         


Ser Thr Arg Glu Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser 
        435                 440                 445             


Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala Glu Asp Val 
    450                 455                 460                 


Ala Val Tyr Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Tyr Thr Phe Gly 
465                 470                 475                 480 


Cys Gly Thr Lys Val Glu Ile Lys 
                485             


<210>  185
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  185

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly 
            20                  25                  30          


Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
    50                  55                  60                  


Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  186
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  186

Ala Ile Asp Met Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser 
65                  70                  75                  80  


Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp 
                85                  90                  95      


Ala Asp Asn Thr Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser 
225                 230                 235                 240 


Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro Leu Thr 
                245                 250                 255     


Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala Met Ser 
            260                 265                 270         


Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Gly Ile Ile 
        275                 280                 285             


Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr Ser Pro 
305                 310                 315                 320 


Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala Ser Ser 
                325                 330                 335     


Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly Thr 
            340                 345                 350         


Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr Gln 
    370                 375                 380                 


Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile Thr 
385                 390                 395                 400 


Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp Tyr Gln Gln 
                405                 410                 415     


Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr Leu 
            420                 425                 430         


Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr Asp 
        435                 440                 445             


Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  187
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  187

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly 
            20                  25                  30          


Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
    50                  55                  60                  


Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  188
<211>  484
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  188

Ala Ile Asp Met Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser 
65                  70                  75                  80  


Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp 
                85                  90                  95      


Ala Asp Asn Thr Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser 
225                 230                 235                 240 


Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro Leu Thr 
                245                 250                 255     


Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala Met Asn 
            260                 265                 270         


Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Gly Ile Ile 
        275                 280                 285             


Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr Ser Pro 
305                 310                 315                 320 


Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser Tyr Pro 
                325                 330                 335     


Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly Thr Leu 
            340                 345                 350         


Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr Gln Ser 
    370                 375                 380                 


Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile Thr Cys 
385                 390                 395                 400 


Lys Ala Ser Glu Asp Ile Ala Tyr Gly Leu Asn Trp Tyr Gln Gln Lys 
                405                 410                 415     


Leu Gly Ile Thr Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr Leu Glu 
            420                 425                 430         


Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr His Tyr 
        435                 440                 445             


Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile Tyr Tyr 
    450                 455                 460                 


Cys Gln Gln Gly Tyr Asn Thr Pro Pro Thr Phe Gly Cys Gly Thr Lys 
465                 470                 475                 480 


Val Glu Ile Lys 
                


<210>  189
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  189

Gln Ser Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly 
            20                  25                  30          


Met Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Ala 
        35                  40                  45              


Cys Ile Ala Ala Gly Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala 
    50                  55                  60                  


Gln Gly Arg Phe Thr Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu 
65                  70                  75                  80  


Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala 
                85                  90                  95      


Gly Glu Asp Tyr Thr Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  190
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  190

Ala Ile Asp Met Thr Gln Thr Pro Ser Pro Val Ser Ala Val Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Asn Cys Gln Ala Ser Glu Asn Ile Tyr Ser Phe 
            20                  25                  30          


Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr Ile Ser Asp Val His Ser 
65                  70                  75                  80  


Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln Thr Gly Thr Tyr Ser Asp 
                85                  90                  95      


Ala Asp Asn Thr Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser 
225                 230                 235                 240 


Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro Leu Thr 
                245                 250                 255     


Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala Met Ser 
            260                 265                 270         


Trp Val Arg Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Gly Ile Ile 
        275                 280                 285             


Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys Gly Pro Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr Ser Pro 
305                 310                 315                 320 


Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly Gly Ala Gly 
                325                 330                 335     


Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly Thr 
            340                 345                 350         


Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr Gln 
    370                 375                 380                 


Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile Thr 
385                 390                 395                 400 


Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp Tyr Gln Gln 
                405                 410                 415     


Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr Leu 
            420                 425                 430         


Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr Asp 
        435                 440                 445             


Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly Cys Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  191
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  191

Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  192
<211>  484
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  192

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser Leu Glu Glu 
225                 230                 235                 240 


Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser Leu Thr Leu Thr Cys 
                245                 250                 255     


Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly Met Cys Trp Val Arg 
            260                 265                 270         


Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Ala Cys Ile Ala Ala Gly 
        275                 280                 285             


Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala Gln Gly Arg Phe Thr 
    290                 295                 300                 


Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu Gln Met Thr Ser Leu 
305                 310                 315                 320 


Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala Gly Glu Asp Tyr Thr 
                325                 330                 335     


Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly Thr Leu Val Thr Val 
            340                 345                 350         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Gly Ser Ala Ile Asp Met Thr Gln Thr Pro Ser Pro 
    370                 375                 380                 


Val Ser Ala Val Val Gly Asp Thr Val Thr Ile Asn Cys Gln Ala Ser 
385                 390                 395                 400 


Glu Asn Ile Tyr Ser Phe Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
                405                 410                 415     


Pro Pro Lys Leu Leu Ile Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val 
            420                 425                 430         


Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr 
        435                 440                 445             


Ile Ser Asp Val His Ser Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln 
    450                 455                 460                 


Thr Gly Thr Tyr Ser Asp Ala Asp Asn Thr Phe Gly Cys Gly Thr Glu 
465                 470                 475                 480 


Val Val Val Lys 
                


<210>  193
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  193

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  194
<211>  484
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  194

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Ala Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Thr Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr His Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser Leu Glu Glu 
225                 230                 235                 240 


Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser Leu Thr Leu Thr Cys 
                245                 250                 255     


Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly Met Cys Trp Val Arg 
            260                 265                 270         


Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Ala Cys Ile Ala Ala Gly 
        275                 280                 285             


Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala Gln Gly Arg Phe Thr 
    290                 295                 300                 


Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu Gln Met Thr Ser Leu 
305                 310                 315                 320 


Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala Gly Glu Asp Tyr Thr 
                325                 330                 335     


Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly Thr Leu Val Thr Val 
            340                 345                 350         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Gly Ser Ala Ile Asp Met Thr Gln Thr Pro Ser Pro 
    370                 375                 380                 


Val Ser Ala Val Val Gly Asp Thr Val Thr Ile Asn Cys Gln Ala Ser 
385                 390                 395                 400 


Glu Asn Ile Tyr Ser Phe Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
                405                 410                 415     


Pro Pro Lys Leu Leu Ile Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val 
            420                 425                 430         


Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr 
        435                 440                 445             


Ile Ser Asp Val His Ser Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln 
    450                 455                 460                 


Thr Gly Thr Tyr Ser Asp Ala Asp Asn Thr Phe Gly Cys Gly Thr Glu 
465                 470                 475                 480 


Val Val Val Lys 
                


<210>  195
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  195

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Thr Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Pro Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly Gly 
                85                  90                  95      


Ala Gly Tyr Gly Tyr Ala His Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  196
<211>  484
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  196

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser Leu Glu Glu 
225                 230                 235                 240 


Ser Gly Gly Asp Leu Val Lys Pro Gly Ala Ser Leu Thr Leu Thr Cys 
                245                 250                 255     


Thr Ala Ser Gly Phe Ser Phe Ser Ser Asp Gly Met Cys Trp Val Arg 
            260                 265                 270         


Gln Ala Pro Gly Lys Cys Leu Glu Trp Ile Ala Cys Ile Ala Ala Gly 
        275                 280                 285             


Ser Ser Gly Ser Thr Tyr Tyr Ala Thr Trp Ala Gln Gly Arg Phe Thr 
    290                 295                 300                 


Ile Ser Lys Ser Ser Ser Thr Thr Val Thr Leu Gln Met Thr Ser Leu 
305                 310                 315                 320 


Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala Gly Glu Asp Tyr Thr 
                325                 330                 335     


Gly Asn Asn Tyr Tyr Ala Leu Trp Gly Pro Gly Thr Leu Val Thr Val 
            340                 345                 350         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Gly Ser Ala Ile Asp Met Thr Gln Thr Pro Ser Pro 
    370                 375                 380                 


Val Ser Ala Val Val Gly Asp Thr Val Thr Ile Asn Cys Gln Ala Ser 
385                 390                 395                 400 


Glu Asn Ile Tyr Ser Phe Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 
                405                 410                 415     


Pro Pro Lys Leu Leu Ile Tyr Phe Ala Ser Lys Leu Ala Ser Gly Val 
            420                 425                 430         


Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly Thr Gln Phe Thr Leu Thr 
        435                 440                 445             


Ile Ser Asp Val His Ser Asp Asp Ala Ala Ile Tyr Tyr Cys Gln Gln 
    450                 455                 460                 


Thr Gly Thr Tyr Ser Asp Ala Asp Asn Thr Phe Gly Cys Gly Thr Glu 
465                 470                 475                 480 


Val Val Val Lys 
                


<210>  197
<211>  1273
<212>  PRT
<213>  Coronavirus

<400>  197

Met Phe Val Phe Leu Val Leu Leu Pro Leu Val Ser Ser Gln Cys Val 
1               5                   10                  15      


Asn Leu Thr Thr Arg Thr Gln Leu Pro Pro Ala Tyr Thr Asn Ser Phe 
            20                  25                  30          


Thr Arg Gly Val Tyr Tyr Pro Asp Lys Val Phe Arg Ser Ser Val Leu 
        35                  40                  45              


His Ser Thr Gln Asp Leu Phe Leu Pro Phe Phe Ser Asn Val Thr Trp 
    50                  55                  60                  


Phe His Ala Ile His Val Ser Gly Thr Asn Gly Thr Lys Arg Phe Asp 
65                  70                  75                  80  


Asn Pro Val Leu Pro Phe Asn Asp Gly Val Tyr Phe Ala Ser Thr Glu 
                85                  90                  95      


Lys Ser Asn Ile Ile Arg Gly Trp Ile Phe Gly Thr Thr Leu Asp Ser 
            100                 105                 110         


Lys Thr Gln Ser Leu Leu Ile Val Asn Asn Ala Thr Asn Val Val Ile 
        115                 120                 125             


Lys Val Cys Glu Phe Gln Phe Cys Asn Asp Pro Phe Leu Gly Val Tyr 
    130                 135                 140                 


Tyr His Lys Asn Asn Lys Ser Trp Met Glu Ser Glu Phe Arg Val Tyr 
145                 150                 155                 160 


Ser Ser Ala Asn Asn Cys Thr Phe Glu Tyr Val Ser Gln Pro Phe Leu 
                165                 170                 175     


Met Asp Leu Glu Gly Lys Gln Gly Asn Phe Lys Asn Leu Arg Glu Phe 
            180                 185                 190         


Val Phe Lys Asn Ile Asp Gly Tyr Phe Lys Ile Tyr Ser Lys His Thr 
        195                 200                 205             


Pro Ile Asn Leu Val Arg Asp Leu Pro Gln Gly Phe Ser Ala Leu Glu 
    210                 215                 220                 


Pro Leu Val Asp Leu Pro Ile Gly Ile Asn Ile Thr Arg Phe Gln Thr 
225                 230                 235                 240 


Leu Leu Ala Leu His Arg Ser Tyr Leu Thr Pro Gly Asp Ser Ser Ser 
                245                 250                 255     


Gly Trp Thr Ala Gly Ala Ala Ala Tyr Tyr Val Gly Tyr Leu Gln Pro 
            260                 265                 270         


Arg Thr Phe Leu Leu Lys Tyr Asn Glu Asn Gly Thr Ile Thr Asp Ala 
        275                 280                 285             


Val Asp Cys Ala Leu Asp Pro Leu Ser Glu Thr Lys Cys Thr Leu Lys 
    290                 295                 300                 


Ser Phe Thr Val Glu Lys Gly Ile Tyr Gln Thr Ser Asn Phe Arg Val 
305                 310                 315                 320 


Gln Pro Thr Glu Ser Ile Val Arg Phe Pro Asn Ile Thr Asn Leu Cys 
                325                 330                 335     


Pro Phe Gly Glu Val Phe Asn Ala Thr Arg Phe Ala Ser Val Tyr Ala 
            340                 345                 350         


Trp Asn Arg Lys Arg Ile Ser Asn Cys Val Ala Asp Tyr Ser Val Leu 
        355                 360                 365             


Tyr Asn Ser Ala Ser Phe Ser Thr Phe Lys Cys Tyr Gly Val Ser Pro 
    370                 375                 380                 


Thr Lys Leu Asn Asp Leu Cys Phe Thr Asn Val Tyr Ala Asp Ser Phe 
385                 390                 395                 400 


Val Ile Arg Gly Asp Glu Val Arg Gln Ile Ala Pro Gly Gln Thr Gly 
                405                 410                 415     


Lys Ile Ala Asp Tyr Asn Tyr Lys Leu Pro Asp Asp Phe Thr Gly Cys 
            420                 425                 430         


Val Ile Ala Trp Asn Ser Asn Asn Leu Asp Ser Lys Val Gly Gly Asn 
        435                 440                 445             


Tyr Asn Tyr Leu Tyr Arg Leu Phe Arg Lys Ser Asn Leu Lys Pro Phe 
    450                 455                 460                 


Glu Arg Asp Ile Ser Thr Glu Ile Tyr Gln Ala Gly Ser Thr Pro Cys 
465                 470                 475                 480 


Asn Gly Val Glu Gly Phe Asn Cys Tyr Phe Pro Leu Gln Ser Tyr Gly 
                485                 490                 495     


Phe Gln Pro Thr Asn Gly Val Gly Tyr Gln Pro Tyr Arg Val Val Val 
            500                 505                 510         


Leu Ser Phe Glu Leu Leu His Ala Pro Ala Thr Val Cys Gly Pro Lys 
        515                 520                 525             


Lys Ser Thr Asn Leu Val Lys Asn Lys Cys Val Asn Phe Asn Phe Asn 
    530                 535                 540                 


Gly Leu Thr Gly Thr Gly Val Leu Thr Glu Ser Asn Lys Lys Phe Leu 
545                 550                 555                 560 


Pro Phe Gln Gln Phe Gly Arg Asp Ile Ala Asp Thr Thr Asp Ala Val 
                565                 570                 575     


Arg Asp Pro Gln Thr Leu Glu Ile Leu Asp Ile Thr Pro Cys Ser Phe 
            580                 585                 590         


Gly Gly Val Ser Val Ile Thr Pro Gly Thr Asn Thr Ser Asn Gln Val 
        595                 600                 605             


Ala Val Leu Tyr Gln Asp Val Asn Cys Thr Glu Val Pro Val Ala Ile 
    610                 615                 620                 


His Ala Asp Gln Leu Thr Pro Thr Trp Arg Val Tyr Ser Thr Gly Ser 
625                 630                 635                 640 


Asn Val Phe Gln Thr Arg Ala Gly Cys Leu Ile Gly Ala Glu His Val 
                645                 650                 655     


Asn Asn Ser Tyr Glu Cys Asp Ile Pro Ile Gly Ala Gly Ile Cys Ala 
            660                 665                 670         


Ser Tyr Gln Thr Gln Thr Asn Ser Pro Arg Arg Ala Arg Ser Val Ala 
        675                 680                 685             


Ser Gln Ser Ile Ile Ala Tyr Thr Met Ser Leu Gly Ala Glu Asn Ser 
    690                 695                 700                 


Val Ala Tyr Ser Asn Asn Ser Ile Ala Ile Pro Thr Asn Phe Thr Ile 
705                 710                 715                 720 


Ser Val Thr Thr Glu Ile Leu Pro Val Ser Met Thr Lys Thr Ser Val 
                725                 730                 735     


Asp Cys Thr Met Tyr Ile Cys Gly Asp Ser Thr Glu Cys Ser Asn Leu 
            740                 745                 750         


Leu Leu Gln Tyr Gly Ser Phe Cys Thr Gln Leu Asn Arg Ala Leu Thr 
        755                 760                 765             


Gly Ile Ala Val Glu Gln Asp Lys Asn Thr Gln Glu Val Phe Ala Gln 
    770                 775                 780                 


Val Lys Gln Ile Tyr Lys Thr Pro Pro Ile Lys Asp Phe Gly Gly Phe 
785                 790                 795                 800 


Asn Phe Ser Gln Ile Leu Pro Asp Pro Ser Lys Pro Ser Lys Arg Ser 
                805                 810                 815     


Phe Ile Glu Asp Leu Leu Phe Asn Lys Val Thr Leu Ala Asp Ala Gly 
            820                 825                 830         


Phe Ile Lys Gln Tyr Gly Asp Cys Leu Gly Asp Ile Ala Ala Arg Asp 
        835                 840                 845             


Leu Ile Cys Ala Gln Lys Phe Asn Gly Leu Thr Val Leu Pro Pro Leu 
    850                 855                 860                 


Leu Thr Asp Glu Met Ile Ala Gln Tyr Thr Ser Ala Leu Leu Ala Gly 
865                 870                 875                 880 


Thr Ile Thr Ser Gly Trp Thr Phe Gly Ala Gly Ala Ala Leu Gln Ile 
                885                 890                 895     


Pro Phe Ala Met Gln Met Ala Tyr Arg Phe Asn Gly Ile Gly Val Thr 
            900                 905                 910         


Gln Asn Val Leu Tyr Glu Asn Gln Lys Leu Ile Ala Asn Gln Phe Asn 
        915                 920                 925             


Ser Ala Ile Gly Lys Ile Gln Asp Ser Leu Ser Ser Thr Ala Ser Ala 
    930                 935                 940                 


Leu Gly Lys Leu Gln Asp Val Val Asn Gln Asn Ala Gln Ala Leu Asn 
945                 950                 955                 960 


Thr Leu Val Lys Gln Leu Ser Ser Asn Phe Gly Ala Ile Ser Ser Val 
                965                 970                 975     


Leu Asn Asp Ile Leu Ser Arg Leu Asp Lys Val Glu Ala Glu Val Gln 
            980                 985                 990         


Ile Asp Arg Leu Ile Thr Gly Arg  Leu Gln Ser Leu Gln  Thr Tyr Val 
        995                 1000                 1005             


Thr Gln  Gln Leu Ile Arg Ala  Ala Glu Ile Arg Ala  Ser Ala Asn 
    1010                 1015                 1020             


Leu Ala  Ala Thr Lys Met Ser  Glu Cys Val Leu Gly  Gln Ser Lys 
    1025                 1030                 1035             


Arg Val  Asp Phe Cys Gly Lys  Gly Tyr His Leu Met  Ser Phe Pro 
    1040                 1045                 1050             


Gln Ser  Ala Pro His Gly Val  Val Phe Leu His Val  Thr Tyr Val 
    1055                 1060                 1065             


Pro Ala  Gln Glu Lys Asn Phe  Thr Thr Ala Pro Ala  Ile Cys His 
    1070                 1075                 1080             


Asp Gly  Lys Ala His Phe Pro  Arg Glu Gly Val Phe  Val Ser Asn 
    1085                 1090                 1095             


Gly Thr  His Trp Phe Val Thr  Gln Arg Asn Phe Tyr  Glu Pro Gln 
    1100                 1105                 1110             


Ile Ile  Thr Thr Asp Asn Thr  Phe Val Ser Gly Asn  Cys Asp Val 
    1115                 1120                 1125             


Val Ile  Gly Ile Val Asn Asn  Thr Val Tyr Asp Pro  Leu Gln Pro 
    1130                 1135                 1140             


Glu Leu  Asp Ser Phe Lys Glu  Glu Leu Asp Lys Tyr  Phe Lys Asn 
    1145                 1150                 1155             


His Thr  Ser Pro Asp Val Asp  Leu Gly Asp Ile Ser  Gly Ile Asn 
    1160                 1165                 1170             


Ala Ser  Val Val Asn Ile Gln  Lys Glu Ile Asp Arg  Leu Asn Glu 
    1175                 1180                 1185             


Val Ala  Lys Asn Leu Asn Glu  Ser Leu Ile Asp Leu  Gln Glu Leu 
    1190                 1195                 1200             


Gly Lys  Tyr Glu Gln Tyr Ile  Lys Trp Pro Trp Tyr  Ile Trp Leu 
    1205                 1210                 1215             


Gly Phe  Ile Ala Gly Leu Ile  Ala Ile Val Met Val  Thr Ile Met 
    1220                 1225                 1230             


Leu Cys  Cys Met Thr Ser Cys  Cys Ser Cys Leu Lys  Gly Cys Cys 
    1235                 1240                 1245             


Ser Cys  Gly Ser Cys Cys Lys  Phe Asp Glu Asp Asp  Ser Glu Pro 
    1250                 1255                 1260             


Val Leu  Lys Gly Val Lys Leu  His Tyr Thr 
    1265                 1270             


<210>  198
<211>  202
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  S Protein RBD

<400>  198

Val Arg Phe Pro Asn Ile Thr Asn Leu Cys Pro Phe Gly Glu Val Phe 
1               5                   10                  15      


Asn Ala Thr Arg Phe Ala Ser Val Tyr Ala Trp Asn Arg Lys Arg Ile 
            20                  25                  30          


Ser Asn Cys Val Ala Asp Tyr Ser Val Leu Tyr Asn Ser Ala Ser Phe 
        35                  40                  45              


Ser Thr Phe Lys Cys Tyr Gly Val Ser Pro Thr Lys Leu Asn Asp Leu 
    50                  55                  60                  


Cys Phe Thr Asn Val Tyr Ala Asp Ser Phe Val Ile Arg Gly Asp Glu 
65                  70                  75                  80  


Val Arg Gln Ile Ala Pro Gly Gln Thr Gly Lys Ile Ala Asp Tyr Asn 
                85                  90                  95      


Tyr Lys Leu Pro Asp Asp Phe Thr Gly Cys Val Ile Ala Trp Asn Ser 
            100                 105                 110         


Asn Asn Leu Asp Ser Lys Val Gly Gly Asn Tyr Asn Tyr Leu Tyr Arg 
        115                 120                 125             


Leu Phe Arg Lys Ser Asn Leu Lys Pro Phe Glu Arg Asp Ile Ser Thr 
    130                 135                 140                 


Glu Ile Tyr Gln Ala Gly Ser Thr Pro Cys Asn Gly Val Glu Gly Phe 
145                 150                 155                 160 


Asn Cys Tyr Phe Pro Leu Gln Ser Tyr Gly Phe Gln Pro Thr Asn Gly 
                165                 170                 175     


Val Gly Tyr Gln Pro Tyr Arg Val Val Val Leu Ser Phe Glu Leu Leu 
            180                 185                 190         


His Ala Pro Ala Thr Val Cys Gly Pro Lys 
        195                 200         


<210>  199
<211>  47
<212>  RNA
<213>  Artificial Sequence

<220>
<223>  5'-UTR (hAg-Kozak)

<400>  199
aacuaguauu cuucuggucc ccacagacuc agagagaacc cgccacc                     47


<210>  200
<211>  311
<212>  RNA
<213>  Artificial Sequence

<220>
<223>  3'-UTR (2hBg)

<400>  200
cucgagagcu cgcuuucuug cuguccaauu ucuauuaaag guuccuuugu ucccuaaguc       60

caacuacuaa acugggggau auuaugaagg gccuugagca ucuggauucu gccuaauaaa      120

aaacauuuau uuucauugcu gcgucgagag cucgcuuucu ugcuguccaa uuucuauuaa      180

agguuccuuu guucccuaag uccaacuacu aaacuggggg auauuaugaa gggccuugag      240

caucuggauu cugccuaaua aaaaacauuu auuuucauug cugcgucgag accuggucca      300

gagucgcuag c                                                           311


<210>  201
<211>  278
<212>  RNA
<213>  Artificial Sequence

<220>
<223>  3'-UTR (FI element)

<400>  201
cugguacugc augcacgcaa ugcuagcugc cccuuucccg uccuggguac cccgagucuc       60

ccccgaccuc gggucccagg uaugcuccca ccuccaccug ccccacucac caccucugcu      120

aguuccagac accucccaag cacgcagcaa ugcagcucaa aacgcuuagc cuagccacac      180

ccccacggga aacagcagug auuaaccuuu agcaauaaac gaaaguuuaa cuaagcuaua      240

cuaaccccag gguuggucaa uuucgugcca gccacacc                              278


<210>  202
<211>  110
<212>  RNA
<213>  Artificial Sequence

<220>
<223>  A30L70

<400>  202
aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa gcauaugacu aaaaaaaaaa aaaaaaaaaa       60

aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa                 110


<210>  203
<211>  20
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Linker

<400>  203

Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
1               5                   10                  15      


Gly Gly Gly Ser 
            20  


<210>  204
<211>  25
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Linker

<400>  204

Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
1               5                   10                  15      


Gly Gly Gly Ser Gly Gly Gly Gly Ser 
            20                  25  


<210>  205
<211>  450
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  205

Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala 
            20                  25                  30          


Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala 
                85                  90                  95      


Ser Ser Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro 
            100                 105                 110         


Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val 
        115                 120                 125             


Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala 
    130                 135                 140                 


Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser 
145                 150                 155                 160 


Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val 
                165                 170                 175     


Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro 
            180                 185                 190         


Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys 
        195                 200                 205             


Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp 
    210                 215                 220                 


Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly 
225                 230                 235                 240 


Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile 
                245                 250                 255     


Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu 
            260                 265                 270         


Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His 
        275                 280                 285             


Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg 
    290                 295                 300                 


Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys 
305                 310                 315                 320 


Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu 
                325                 330                 335     


Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr 
            340                 345                 350         


Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu 
        355                 360                 365             


Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp 
    370                 375                 380                 


Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val 
385                 390                 395                 400 


Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp 
                405                 410                 415     


Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His 
            420                 425                 430         


Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro 
        435                 440                 445             


Gly Lys 
    450 


<210>  206
<211>  486
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  206

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr Asp Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Glu Gln Leu Glu 
225                 230                 235                 240 


Glu Ser Gly Gly Asp Leu Val Lys Pro Glu Gly Ser Leu Thr Leu Thr 
                245                 250                 255     


Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asn Tyr Trp Ile Cys Trp 
            260                 265                 270         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly Cys Ile Tyr 
        275                 280                 285             


Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr Leu Gln Met Thr Ser 
305                 310                 315                 320 


Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ser Tyr Thr 
                325                 330                 335     


Pro Gly Ser Tyr Tyr Asn Met Asn Leu Trp Gly Pro Gly Thr Leu Val 
            340                 345                 350         


Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly 
        355                 360                 365             


Gly Gly Ser Gly Gly Gly Gly Ser Asp Val Val Met Thr Gln Thr Pro 
    370                 375                 380                 


Ser Ser Val Ser Ala Ala Val Gly Gly Thr Val Thr Ile Asn Cys Gln 
385                 390                 395                 400 


Ala Ser Gln Gln Ile Ser Asn Glu Leu Ser Trp Tyr Gln Gln Lys Ser 
                405                 410                 415     


Gly Gln Pro Pro Lys Leu Leu Ile Tyr Asp Ala Ser Asp Leu Ala Ser 
            420                 425                 430         


Gly Val Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly Thr Glu Phe Thr 
        435                 440                 445             


Leu Thr Ile Ser Asp Leu Glu Ser Ala Asp Ala Ala Thr Tyr Tyr Cys 
    450                 455                 460                 


Gln Ser Thr Gly Gly Ala Ser Ser Asp Gly Asn Ala Phe Gly Gly Gly 
465                 470                 475                 480 


Thr Glu Val Val Val Lys 
                485     


<210>  207
<211>  451
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  207

Gln Glu Gln Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Glu Gly 
1               5                   10                  15      


Ser Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asn 
            20                  25                  30          


Tyr Trp Ile Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        35                  40                  45              


Ile Gly Cys Ile Tyr Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp 
    50                  55                  60                  


Ala Lys Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr 
65                  70                  75                  80  


Leu Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                85                  90                  95      


Ala Arg Ser Tyr Thr Pro Gly Ser Tyr Tyr Asn Met Asn Leu Trp Gly 
            100                 105                 110         


Pro Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser 
        115                 120                 125             


Val Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala 
    130                 135                 140                 


Ala Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val 
145                 150                 155                 160 


Ser Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala 
                165                 170                 175     


Val Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val 
            180                 185                 190         


Pro Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His 
        195                 200                 205             


Lys Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys 
    210                 215                 220                 


Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly 
225                 230                 235                 240 


Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met 
                245                 250                 255     


Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His 
            260                 265                 270         


Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val 
        275                 280                 285             


His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr 
    290                 295                 300                 


Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly 
305                 310                 315                 320 


Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile 
                325                 330                 335     


Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val 
            340                 345                 350         


Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser 
        355                 360                 365             


Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu 
    370                 375                 380                 


Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro 
385                 390                 395                 400 


Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val 
                405                 410                 415     


Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu 
            420                 425                 430         


His Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser 
        435                 440                 445             


Pro Gly Lys 
    450     


<210>  208
<211>  485
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  208

Asp Val Val Met Thr Gln Thr Pro Ser Ser Val Ser Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Asn Cys Gln Ala Ser Gln Gln Ile Ser Asn Glu 
            20                  25                  30          


Leu Ser Trp Tyr Gln Gln Lys Ser Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Asp Ala Ser Asp Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Ser Thr Gly Gly Ala Ser Ser 
                85                  90                  95      


Asp Gly Asn Ala Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser 
225                 230                 235                 240 


Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro Leu Thr 
                245                 250                 255     


Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Ser Ser Tyr Ala Met Ser 
            260                 265                 270         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly Ile Ile 
        275                 280                 285             


Ser Ser Ser Gly Ser Thr Tyr Tyr Ala Ser Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr Ser Pro 
305                 310                 315                 320 


Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ala Ser Ser 
                325                 330                 335     


Arg Gly Tyr Tyr Tyr Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly Thr 
            340                 345                 350         


Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr Gln 
    370                 375                 380                 


Ser Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile Thr 
385                 390                 395                 400 


Cys Lys Ala Ser Glu Asp Ile Gly Tyr Gly Leu Asn Trp Tyr Gln Gln 
                405                 410                 415     


Lys Leu Gly Ile Ala Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr Leu 
            420                 425                 430         


Glu Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr Asp 
        435                 440                 445             


Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile Tyr 
    450                 455                 460                 


Tyr Cys Gln Gln Gly Tyr Ser Thr Pro Leu Thr Phe Gly Ala Gly Thr 
465                 470                 475                 480 


Lys Val Glu Ile Lys 
                485 


<210>  209
<211>  451
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  209

Gln Glu Gln Leu Glu Glu Ser Gly Gly Asp Leu Val Lys Pro Glu Gly 
1               5                   10                  15      


Ser Leu Thr Leu Thr Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asn 
            20                  25                  30          


Tyr Trp Ile Cys Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        35                  40                  45              


Ile Gly Cys Ile Tyr Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp 
    50                  55                  60                  


Ala Lys Gly Arg Phe Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr 
65                  70                  75                  80  


Leu Gln Met Thr Ser Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys 
                85                  90                  95      


Ala Arg Ser Tyr Thr Pro Gly Ser Tyr Tyr Asn Met Asn Leu Trp Gly 
            100                 105                 110         


Pro Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser 
        115                 120                 125             


Val Phe Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala 
    130                 135                 140                 


Ala Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val 
145                 150                 155                 160 


Ser Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala 
                165                 170                 175     


Val Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val 
            180                 185                 190         


Pro Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His 
        195                 200                 205             


Lys Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys 
    210                 215                 220                 


Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly 
225                 230                 235                 240 


Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met 
                245                 250                 255     


Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His 
            260                 265                 270         


Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val 
        275                 280                 285             


His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr 
    290                 295                 300                 


Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly 
305                 310                 315                 320 


Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile 
                325                 330                 335     


Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val 
            340                 345                 350         


Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser 
        355                 360                 365             


Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu 
    370                 375                 380                 


Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro 
385                 390                 395                 400 


Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val 
                405                 410                 415     


Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu 
            420                 425                 430         


His Glu Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser 
        435                 440                 445             


Pro Gly Lys 
    450     


<210>  210
<211>  484
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  210

Asp Val Val Met Thr Gln Thr Pro Ser Ser Val Ser Ala Ala Val Gly 
1               5                   10                  15      


Gly Thr Val Thr Ile Asn Cys Gln Ala Ser Gln Gln Ile Ser Asn Glu 
            20                  25                  30          


Leu Ser Trp Tyr Gln Gln Lys Ser Gly Gln Pro Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Asp Ala Ser Asp Leu Ala Ser Gly Val Pro Ser Arg Phe Lys Gly 
    50                  55                  60                  


Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Asp Leu Glu Ser 
65                  70                  75                  80  


Ala Asp Ala Ala Thr Tyr Tyr Cys Gln Ser Thr Gly Gly Ala Ser Ser 
                85                  90                  95      


Asp Gly Asn Ala Phe Gly Gly Gly Thr Glu Val Val Val Lys Arg Thr 
            100                 105                 110         


Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu 
        115                 120                 125             


Lys Ser Gly Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro 
    130                 135                 140                 


Arg Glu Ala Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly 
145                 150                 155                 160 


Asn Ser Gln Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr 
                165                 170                 175     


Ser Leu Ser Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His 
            180                 185                 190         


Lys Val Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val 
        195                 200                 205             


Thr Lys Ser Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly 
    210                 215                 220                 


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Ser 
225                 230                 235                 240 


Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro Leu Thr 
                245                 250                 255     


Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala Met Asn 
            260                 265                 270         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly Ile Ile 
        275                 280                 285             


Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr Ser Pro 
305                 310                 315                 320 


Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser Tyr Pro 
                325                 330                 335     


Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly Thr Leu 
            340                 345                 350         


Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Gly Ser Gly Gly Gly Gly Ser Ala Ile Gln Met Thr Gln Ser 
    370                 375                 380                 


Pro Ser Ser Leu Ala Ala Ser Val Gly Asp Thr Val Thr Ile Thr Cys 
385                 390                 395                 400 


Lys Ala Ser Glu Asp Ile Ala Tyr Gly Leu Asn Trp Tyr Gln Gln Lys 
                405                 410                 415     


Leu Gly Ile Thr Pro Lys Leu Leu Ile Tyr Gly Ala Asn Thr Leu Glu 
            420                 425                 430         


Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Glu Thr His Tyr 
        435                 440                 445             


Thr Leu Thr Ile Ser Ser Val Gln Ala Glu Asp Ala Gly Ile Tyr Tyr 
    450                 455                 460                 


Cys Gln Gln Gly Tyr Asn Thr Pro Pro Thr Phe Gly Ala Gly Thr Lys 
465                 470                 475                 480 


Val Glu Ile Lys 
                


<210>  211
<211>  449
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (HC)

<400>  211

Gln Ser Val Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 
1               5                   10                  15      


Leu Thr Leu Thr Cys Thr Val Ser Gly Phe Ser Leu Asn Asn Tyr Ala 
            20                  25                  30          


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 
        35                  40                  45              


Ile Ile Ser Ser Ser Gly Asn Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 
    50                  55                  60                  


Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Lys Ile Thr 
65                  70                  75                  80  


Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Ser 
                85                  90                  95      


Tyr Pro Gly Tyr Ser Pro Tyr Tyr Gly Met Asp Pro Trp Gly Pro Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe 
        115                 120                 125             


Pro Leu Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu 
    130                 135                 140                 


Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp 
145                 150                 155                 160 


Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu 
                165                 170                 175     


Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser 
            180                 185                 190         


Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro 
        195                 200                 205             


Ser Asn Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Cys Asp Lys 
    210                 215                 220                 


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Ala Ala Gly Gly Pro 
225                 230                 235                 240 


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
                245                 250                 255     


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
            260                 265                 270         


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
        275                 280                 285             


Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val 
    290                 295                 300                 


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
305                 310                 315                 320 


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
                325                 330                 335     


Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr 
            340                 345                 350         


Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr 
        355                 360                 365             


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
    370                 375                 380                 


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
385                 390                 395                 400 


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
                405                 410                 415     


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Leu His Glu 
            420                 425                 430         


Ala Leu His Ser His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
        435                 440                 445             


Lys 
    


<210>  212
<211>  486
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Binding agent (LC)

<400>  212

Ala Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ala Ala Ser Val Gly 
1               5                   10                  15      


Asp Thr Val Thr Ile Thr Cys Lys Ala Ser Glu Asp Ile Ala Tyr Gly 
            20                  25                  30          


Leu Asn Trp Tyr Gln Gln Lys Leu Gly Ile Thr Pro Lys Leu Leu Ile 
        35                  40                  45              


Tyr Gly Ala Asn Thr Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 
    50                  55                  60                  


Ser Gly Ser Glu Thr His Tyr Thr Leu Thr Ile Ser Ser Val Gln Ala 
65                  70                  75                  80  


Glu Asp Ala Gly Ile Tyr Tyr Cys Gln Gln Gly Tyr Asn Thr Pro Pro 
                85                  90                  95      


Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala 
            100                 105                 110         


Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly 
        115                 120                 125             


Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala 
    130                 135                 140                 


Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln 
145                 150                 155                 160 


Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser 
                165                 170                 175     


Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr 
            180                 185                 190         


Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser 
        195                 200                 205             


Phe Asn Arg Gly Glu Cys Asp Val Pro Gly Gly Ser Gly Gly Gly Gly 
    210                 215                 220                 


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Glu Gln Leu Glu 
225                 230                 235                 240 


Glu Ser Gly Gly Asp Leu Val Lys Pro Glu Gly Ser Leu Thr Leu Thr 
                245                 250                 255     


Cys Thr Ala Ser Gly Phe Ser Phe Ser Ser Asn Tyr Trp Ile Cys Trp 
            260                 265                 270         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly Cys Ile Tyr 
        275                 280                 285             


Ile Gly Ser Gly Asp Thr Tyr Tyr Ala Ser Trp Ala Lys Gly Arg Phe 
    290                 295                 300                 


Thr Ile Ser Lys Thr Ser Ser Thr Thr Val Thr Leu Gln Met Thr Ser 
305                 310                 315                 320 


Leu Thr Ala Ala Asp Thr Ala Thr Tyr Phe Cys Ala Arg Ser Tyr Thr 
                325                 330                 335     


Pro Gly Ser Tyr Tyr Asn Met Asn Leu Trp Gly Pro Gly Thr Leu Val 
            340                 345                 350         


Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly 
        355                 360                 365             


Gly Gly Ser Gly Gly Gly Gly Ser Asp Val Val Met Thr Gln Thr Pro 
    370                 375                 380                 


Ser Ser Val Ser Ala Ala Val Gly Gly Thr Val Thr Ile Asn Cys Gln 
385                 390                 395                 400 


Ala Ser Gln Gln Ile Ser Asn Glu Leu Ser Trp Tyr Gln Gln Lys Ser 
                405                 410                 415     


Gly Gln Pro Pro Lys Leu Leu Ile Tyr Asp Ala Ser Asp Leu Ala Ser 
            420                 425                 430         


Gly Val Pro Ser Arg Phe Lys Gly Ser Gly Ser Gly Thr Glu Phe Thr 
        435                 440                 445             


Leu Thr Ile Ser Asp Leu Glu Ser Ala Asp Ala Ala Thr Tyr Tyr Cys 
    450                 455                 460                 


Gln Ser Thr Gly Gly Ala Ser Ser Asp Gly Asn Ala Phe Gly Gly Gly 
465                 470                 475                 480 


Thr Glu Val Val Val Lys 
                485     


