                         SEQUENCE LISTING

<110>  MAVERICK THERAPEUTICS, INC.
 
<120>  CONSTRAINED CONDITIONALLY ACTIVATED BINDING PROTEINS

<130>  118459-5009-US, WO

<160>  335   

<170>  PatentIn version 3.5

<210>  1
<211>  127
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-EGFR1

<400>  1

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


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


Ala Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Met Tyr 
65                  70                  75                  80  


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr 
            100                 105                 110         


Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser 
        115                 120                 125         


<210>  2
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-EGFR1

<400>  2

Gly Arg Thr Phe Ser Ser Tyr Ala Met Gly 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-EGFR1

<400>  3

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


<210>  4
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 - Targeting sdAbs - alpha-EGFR1

<400>  4

Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr Glu Tyr 
1               5                   10                  15      


Asp Tyr 
        


<210>  5
<211>  124
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-EGFR2

<400>  5

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser 
        115                 120                 


<210>  6
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-EGFR2

<400>  6

Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly 
1               5                   10  


<210>  7
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-EGFR2

<400>  7

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


Gly 
    


<210>  8
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-EGFR2

<400>  8

Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr 
1               5                   10                  15  


<210>  9
<211>  127
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - h-alpha-EGFR1

<400>  9

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


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


Ala Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr 
            100                 105                 110         


Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125         


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

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - h-alpha-EGFR1

<400>  10

Gly Arg Thr Phe Ser Ser Tyr Ala Met Gly 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - h-alpha-EGFR1

<400>  11

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


<210>  12
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - h-alpha-EGFR1

<400>  12

Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr Glu Tyr 
1               5                   10                  15      


Asp Tyr 
        


<210>  13
<211>  124
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aEGFR2a sdAb

<400>  13

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 


<210>  14
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - aEGFR2a sdAb

<400>  14

Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly 
1               5                   10  


<210>  15
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - aEGFR2a sdAb

<400>  15

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


Gly 
    


<210>  16
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - aEGFR2a sdAb

<400>  16

Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr 
1               5                   10                  15  


<210>  17
<211>  124
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - h-alpha-EGFR2

<400>  17

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 


<210>  18
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - h-alpha-EGFR2

<400>  18

Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly 
1               5                   10  


<210>  19
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - h-alpha-EGFR2

<400>  19

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


Gly 
    


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

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - h-alpha-EGFR2

<400>  20

Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr 
1               5                   10                  15  


<210>  21
<211>  114
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-FOLR1 
       h77-2

<400>  21

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser 
        


<210>  22
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-FOLR1 h77-2

<400>  22

Gly Phe Thr Val Ser Asn Ser Val Met Ala 
1               5                   10  


<210>  23
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-FOLR1 h77-2

<400>  23

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


<210>  24
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-FOLR1 h77-2

<400>  24

Asn Phe Asp Arg Ile Tyr 
1               5       


<210>  25
<211>  113
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-FOLR1 
       h59.3

<400>  25

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


Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser 
            20                  25                  30          


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


Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys 
                85                  90                  95      


His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
            100                 105                 110         


Ser 
    


<210>  26
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-FOLR1 h59.3

<400>  26

Gly Asn Thr Phe Ser Ile Ser Ala Met Gly 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-FOLR1 h59.3

<400>  27

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


<210>  28
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-FOLR1 h59.3

<400>  28

Tyr Gly Ile Asp Tyr 
1               5   


<210>  29
<211>  117
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-FOLR1 
       h22-4

<400>  29

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


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


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


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Ala Asn Thr Ala Thr Trp Gly Arg Val Phe Trp Gly Gln Gly Thr Leu 
            100                 105                 110         


Val Thr Val Ser Ser 
        115         


<210>  30
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-FOLR1 h22-4

<400>  30

Gly Thr Thr Phe Ser Arg Asp Val Met Gly 
1               5                   10  


<210>  31
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-FOLR1 h22-4

<400>  31

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


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

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-FOLR1 h22-4

<400>  32

Asn Thr Ala Thr Trp Gly Arg Val Phe 
1               5                   


<210>  33
<211>  124
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF7

<400>  33

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 


<210>  34
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-B7H3 hF7

<400>  34

Arg Arg Thr Phe His Thr Tyr His Met Gly 
1               5                   10  


<210>  35
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-B7H3 hF7

<400>  35

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


Gly 
    


<210>  36
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-B7H3 hF7

<400>  36

Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr 
1               5                   10                  15  


<210>  37
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12

<400>  37

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  38
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-B7H3 hF12

<400>  38

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


<210>  39
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-B7H3 hF12

<400>  39

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


Gly 
    


<210>  40
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-B7H3 hF12

<400>  40

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  41
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12 - (N57Q)

<400>  41

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  42
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-B7H3 hF12 - (N57Q)

<400>  42

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


<210>  43
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-B7H3 hF12 - (N57Q)

<400>  43

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


Gly 
    


<210>  44
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-B7H3 hF12 - (N57Q)

<400>  44

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  45
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12 - (N57E)

<400>  45

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  46
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - alpha-B7H3 hF12 - (N57E)

<400>  46

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


<210>  47
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - alpha-B7H3 hF12 - (N57E)

<400>  47

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


Gly 
    


<210>  48
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - alpha-B7H3 hF12 - (N57E)

<400>  48

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  49
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12 - (N57D)

<400>  49

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  50
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - alpha-B7H3 hF12 - (N57D)

<400>  50

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


<210>  51
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - alpha-B7H3 hF12 - (N57D)

<400>  51

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


Gly 
    


<210>  52
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - alpha-B7H3 hF12 - (N57D)

<400>  52

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  53
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12 - (S59A)

<400>  53

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  54
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - alpha-B7H3 hF12 - (S59A)

<400>  54

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


<210>  55
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - alpha-B7H3 hF12 - (S59A)

<400>  55

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


Gly 
    


<210>  56
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - alpha-B7H3 hF12 - (S59A)

<400>  56

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  57
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-B7H3 
       hF12 - (S59Y)

<400>  57

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  58
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - alpha-B7H3 hF12 - (S59Y)

<400>  58

Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - alpha-B7H3 hF12 - (S59Y)

<400>  59

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


Gly 
    


<210>  60
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - alpha-B7H3 hF12 - (S59Y)

<400>  60

Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr 
1               5                   10              


<210>  61
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-EpCAM 
       h13

<400>  61

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


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


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


Leu Val Ala Arg Ile Thr Ser Gly Asp Ser Thr Val Tyr Ala Asp Ser 
    50                  55                  60                  


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


Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr 
                85                  90                  95      


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


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  62
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-EpCAM h13

<400>  62

Gly Thr Gly Ser Ile Phe Ser Ile Asn Leu Met Gly 
1               5                   10          


<210>  63
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-EpCAM h13

<400>  63

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


<210>  64
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-EpCAM h13

<400>  64

Leu Leu Arg Ser Ser Pro Gly Ala Thr Thr Pro Tyr 
1               5                   10          


<210>  65
<211>  122
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-EpCAM 
       h23

<400>  65

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


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


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


Leu Val Ala Arg Ile Thr Ser Gly Asp Ser Thr Val Tyr Ala Asp Ser 
    50                  55                  60                  


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


Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr 
                85                  90                  95      


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


Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120         


<210>  66
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - alpha-EpCAM h23

<400>  66

Gly Ser Phe Ser Ala Leu Trp Ala Met Arg 
1               5                   10  


<210>  67
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - alpha-EpCAM h23

<400>  67

Ser Ser Arg Gly Gly Thr Thr Ser Tyr Ala Asp Ser Val Lys Gly 
1               5                   10                  15  


<210>  68
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - alpha-EpCAM h23

<400>  68

Ile Asp Gly His Leu Ala Tyr 
1               5           


<210>  69
<211>  126
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - acEpCAM 
       hVIB665

<400>  69

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125     


<210>  70
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - acEpCAM hVIB665

<400>  70

Gly Arg Thr Phe Ser Asp Tyr Asp Met Gly 
1               5                   10  


<210>  71
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - acEpCAM hVIB665

<400>  71

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


Gly 
    


<210>  72
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - acEpCAM hVIB665

<400>  72

Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr Tyr Asp 
1               5                   10                  15      


Tyr 
    


<210>  73
<211>  126
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - acEpCAM 
       hVIB666

<400>  73

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Thr Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125     


<210>  74
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - acEpCAM hVIB666

<400>  74

Gly Arg Thr Leu Asp Asn Tyr Asp Met Gly 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - acEpCAM hVIB666

<400>  75

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


Gly 
    


<210>  76
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - acEpCAM hVIB666

<400>  76

Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr Tyr Asp 
1               5                   10                  15      


Tyr 
    


<210>  77
<211>  129
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB557

<400>  77

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Ser Gln 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg Ala Thr Ala 
            100                 105                 110         


Glu Thr Ser Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        115                 120                 125             


Ser 
    


<210>  78
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB557

<400>  78

Gly Arg Thr Phe Ser Ser Gln Ser Met Gly 
1               5                   10  


<210>  79
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB557

<400>  79

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


Gly 
    


<210>  80
<211>  20
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB557

<400>  80

Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg Ala Thr Ala Glu Thr 
1               5                   10                  15      


Ser Tyr Asp Tyr 
            20  


<210>  81
<211>  128
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB565

<400>  81

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


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


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Val Tyr 
65                  70                  75                  80  


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


Ala Thr Ala Gly Asp Gly Gly Asp Tyr His Cys Ser Gly Leu Val Asp 
            100                 105                 110         


Tyr Gly Met Asp Tyr Trp Gly Lys Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125             


<210>  82
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB565

<400>  82

Gly Phe Thr Phe Asp Tyr Tyr Ala Ile Gly 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB565

<400>  83

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


Gly 
    


<210>  84
<211>  19
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB565

<400>  84

Ala Gly Asp Gly Gly Asp Tyr His Cys Ser Gly Leu Val Asp Tyr Gly 
1               5                   10                  15      


Met Asp Tyr 
            


<210>  85
<211>  123
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB575

<400>  85

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


Ser Leu Arg Leu Ser Cys Leu Ala Ser Gly Arg Thr Val Gly Arg Thr 
            20                  25                  30          


Ala Met Gly Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ser Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr 
            100                 105                 110         


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


<210>  86
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB575

<400>  86

Gly Arg Thr Val Gly Arg Thr Ala Met Gly 
1               5                   10  


<210>  87
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB575

<400>  87

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


Gly 
    


<210>  88
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB575

<400>  88

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


<210>  89
<211>  123
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB578

<400>  89

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


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


Ala Met Gly Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Ala 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Val Tyr 
65                  70                  75                  80  


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


Ala Ala Ser Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr 
            100                 105                 110         


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


<210>  90
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB578

<400>  90

Gly Arg Thr Phe Gly Arg Ala Ala Met Gly 
1               5                   10  


<210>  91
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB578

<400>  91

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


Gly 
    


<210>  92
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB578

<400>  92

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


<210>  93
<211>  125
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB609

<400>  93

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


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


Pro Met Ala Trp Phe Arg Gln Pro Pro Gly Gln Glu Arg Glu Phe Val 
        35                  40                  45              


Ala Asp Met Ser Trp Ser Gly Thr Asn Thr Tyr Tyr Ala Asp Ser Val 
    50                  55                  60                  


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Trp Pro Tyr Ser Gly Thr Gly Arg Ser Thr Thr Asp Tyr 
            100                 105                 110         


Thr Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125 


<210>  94
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB609

<400>  94

Gly Leu Thr Phe Asn Thr Tyr Pro Met Ala 
1               5                   10  


<210>  95
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB609

<400>  95

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


Gly 
    


<210>  96
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB609

<400>  96

Gly Trp Pro Tyr Ser Gly Thr Gly Arg Ser Thr Thr Asp Tyr Thr Tyr 
1               5                   10                  15      


<210>  97
<211>  126
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aTrop2 
       hVIB619

<400>  97

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


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


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Glu Ser Leu Pro Tyr Glu Ser Gly Ser Pro Arg Leu Thr Asp 
            100                 105                 110         


Phe Ala Ser Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125     


<210>  98
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aTrop2 hVIB619

<400>  98

Gly Arg Ser Phe Ser Arg Tyr Gly Met Gly 
1               5                   10  


<210>  99
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aTrop2 hVIB619

<400>  99

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


Gly 
    


<210>  100
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aTrop2 hVIB619

<400>  100

Glu Ser Leu Pro Tyr Glu Ser Gly Ser Pro Arg Leu Thr Asp Phe Ala 
1               5                   10                  15      


Ser 
    


<210>  101
<211>  119
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aCA9 hVIB456 
       sdAb

<400>  101

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ser Ala Leu Ile Ile Asn 
            20                  25                  30          


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


Ala Thr Val Thr Arg Ser Gly Arg Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Val Ala Leu Trp Ile Ala Asp Gly Glu Tyr Asp Tyr Trp Gly Gln Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser 
        115                 


<210>  102
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aCA9 hVIB456 sdAb

<400>  102

Gly Ser Ala Leu Ile Ile Asn Ala Met Gly 
1               5                   10  


<210>  103
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aCA9 hVIB456 sdAb

<400>  103

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


<210>  104
<211>  11
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aCA9 hVIB456 sdAb

<400>  104

Ala Leu Trp Ile Ala Asp Gly Glu Tyr Asp Tyr 
1               5                   10      


<210>  105
<211>  116
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aCA9 hVIB476 
       sdAb

<400>  105

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Asn Ile Phe Ile Ile Asn 
            20                  25                  30          


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


Ala Thr Ile Thr Asn Gly Gly Arg Thr His Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Ala Asn His Ile Glu Leu Gly Asp Tyr Trp Gly Gln Gly Thr Leu Val 
            100                 105                 110         


Thr Val Ser Ser 
        115     


<210>  106
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - aCA9 hVIB476 sdAb

<400>  106

Gly Asn Ile Phe Ile Ile Asn Val Met Gly 
1               5                   10  


<210>  107
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - aCA9 hVIB476 sdAb

<400>  107

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


<210>  108
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - aCA9 hVIB476 sdAb

<400>  108

Asn His Ile Glu Leu Gly Asp Tyr 
1               5               


<210>  109
<211>  115
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aCA9 hVIB407 
       sdAb

<400>  109

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


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


Asp Met Gly Trp Tyr Arg Gln Thr Pro Gly Lys Gln Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Gly Val Tyr Tyr Cys Asn 
                85                  90                  95      


Ala Ala Trp Ile Gly Asp Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser 
        115 


<210>  110
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - aCA9 hVIB407 sdAb

<400>  110

Gly Ile Ile Phe Ser Val Tyr Asp Met Gly 
1               5                   10  


<210>  111
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - aCA9 hVIB407 sdAb

<400>  111

Arg Ile Thr Ala Gly Gly Gly Thr Tyr Leu Thr Asp Ser Val Lys Gly 
1               5                   10                  15      


<210>  112
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - aCA9 hVIB407 sdAb

<400>  112

Ala Trp Ile Gly Asp Asp Tyr 
1               5           


<210>  113
<211>  115
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - aCA9 hVIB445 
       sdAb

<400>  113

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ile Thr Phe Asn Leu His 
            20                  25                  30          


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


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu 
65                  70                  75                  80  


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


Thr Asp Leu Val Gly Glu Asp Tyr Trp Gly Arg Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser 
        115 


<210>  114
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 -Targeting sdAbs - aCA9 hVIB445 sdAb

<400>  114

Gly Ile Thr Phe Asn Leu His Ala Met Arg 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2 -Targeting sdAbs - aCA9 hVIB445 sdAb

<400>  115

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


<210>  116
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 -Targeting sdAbs - aCA9 hVIB445 sdAb

<400>  116

Asp Leu Val Gly Glu Asp Tyr 
1               5           


<210>  117
<211>  115
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain -Targeting sdAbs - alpha-HSA 
       half-life extension domain (aHSA (10GE))

<400>  117

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
65                  70                  75                  80  


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
                85                  90                  95      


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser 
        115 


<210>  118
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1-Targeting sdAbs - alpha-HSA half-life extension 
       domain (aHSA (10GE))

<400>  118

Gly Phe Thr Phe Ser Lys Phe Gly Met Ser 
1               5                   10  


<210>  119
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR2-Targeting sdAbs - alpha-HSA half-life extension 
       domain (aHSA (10GE))

<400>  119

Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys 
1               5                   10                  15      


Gly 
    


<210>  120
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3-Targeting sdAbs - alpha-HSA half-life extension 
       domain (aHSA (10GE))

<400>  120

Gly Gly Ser Leu Ser Val 
1               5       


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

<220>
<223>  Synthetic antigen binding domain - alpha-HSA half life extension 
       domain

<400>  121

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
65                  70                  75                  80  


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
                85                  90                  95      


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser His His His His His His 
        115                 120     


<210>  122
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR1 - alpha-HSA half-life extension domain

<400>  122

Gly Phe Thr Phe Ser Lys Phe Gly Met Ser 
1               5                   10  


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

<220>
<223>  Synthetic sdCDR2 - alpha-HSA half-life extension domain

<400>  123

Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys 
1               5                   10                  15      


Gly 
    


<210>  124
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic sdCDR3 - alpha-HSA half-life extension domain

<400>  124

Gly Gly Ser Leu Ser Val 
1               5       


<210>  125
<211>  109
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(L)

<400>  125

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


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


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
        35                  40                  45              


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
    50                  55                  60                  


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
65                  70                  75                  80  


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
                85                  90                  95      


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 
            100                 105                 


<210>  126
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVLCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(L)

<400>  126

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


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

<220>
<223>  Synthetic aVLsdCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(L)

<400>  127

Gly Thr Lys Phe Leu Val Pro 
1               5           


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

<220>
<223>  Synthetic aVLsdCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(L)

<400>  128

Thr Leu Trp Tyr Ser Asn Arg Trp Val 
1               5                   


<210>  129
<211>  110
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(Li)

<400>  129

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


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


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
        35                  40                  45              


Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg 
    50                  55                  60                  


Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly 
65                  70                  75                  80  


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


Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 
            100                 105                 110 


<210>  130
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(Li)

<400>  130

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


<210>  131
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLsdCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(Li)

<400>  131

Asp Tyr Lys Asp Asp Asp Asp Lys 
1               5               


<210>  132
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLsdCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(Li)

<400>  132

Val Leu Trp Tyr Ser Asn Arg Trp Val 
1               5                   


<210>  133
<211>  109
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(Li2)

<400>  133

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


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


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
        35                  40                  45              


Leu Ile Gly Gly Thr Lys Asp Asp Ala Pro Gly Thr Pro Ala Arg Phe 
    50                  55                  60                  


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
65                  70                  75                  80  


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
                85                  90                  95      


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 
            100                 105                 


<210>  134
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(Li2)

<400>  134

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


<210>  135
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(Li2)

<400>  135

Gly Thr Lys Asp Asp Ala Pro 
1               5           


<210>  136
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVLCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(Li2)

<400>  136

Val Leu Trp Tyr Ser Asn Arg Trp Val 
1               5                   


<210>  137
<211>  109
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - alpha-
       CD3 VliGL

<400>  137

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


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


His Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
        35                  40                  45              


Leu Ile Gly Gly Thr Ser Asn Lys His Ser Trp Thr Pro Ala Arg Phe 
    50                  55                  60                  


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
65                  70                  75                  80  


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Gly Ser Arg 
                85                  90                  95      


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 
            100                 105                 


<210>  138
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVLiGLCDR1 - alpha-CD3 scFv Domain - alpha- CD3 VliGL

<400>  138

Gly Ser Ser Thr Gly Ala Val Thr Ser Gly His Tyr Pro Asn 
1               5                   10                  


<210>  139
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVLiGLCDR2 - alpha-CD3 scFv Domain - alpha- CD3 VliGL

<400>  139

Gly Thr Ser Asn Lys His Ser 
1               5           


<210>  140
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVLiGLCDR3 - alpha-CD3 scFv Domain - alpha- CD3 VliGL

<400>  140

Val Leu Trp Gly Ser Arg Arg Trp Val 
1               5                   


<210>  141
<211>  125
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(H)

<400>  141

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


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


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


Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 
    50                  55                  60                  


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


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                85                  90                  95      


Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            100                 105                 110         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125 


<210>  142
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(H)

<400>  142

Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn 
1               5                   10  


<210>  143
<211>  19
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHsdCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(H)

<400>  143

Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln 
1               5                   10                  15      


Val Lys Asp 
            


<210>  144
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHsdCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(H)

<400>  144

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


<210>  145
<211>  126
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(Hi)

<400>  145

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


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


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


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    50                  55                  60                  


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


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                85                  90                  95      


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            100                 105                 110         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125     


<210>  146
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(Hi)

<400>  146

Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
1               5                   10  


<210>  147
<211>  20
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(Hi)

<400>  147

Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
1               5                   10                  15      


Ser Val Lys Asp 
            20  


<210>  148
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(Hi)

<400>  148

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


<210>  149
<211>  125
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - 
       alpha-CD3V(Hi2)

<400>  149

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


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


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


Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp 
    50                  55                  60                  


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


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                85                  90                  95      


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            100                 105                 110         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125 


<210>  150
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR1 - alpha CD3 scFV Domain - alpha-CD3 V(Hi2)

<400>  150

Gly Phe Thr Phe Asn Lys His Ala Met Asn 
1               5                   10  


<210>  151
<211>  19
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR2 - alpha CD3 scFV Domain - alpha-CD3 V(Hi2)

<400>  151

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


Val Lys Asp 
            


<210>  152
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic iVHsdCDR3 - alpha CD3 scFV Domain - alpha-CD3 V(Hi2)

<400>  152

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


<210>  153
<211>  125
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic antigen binding domain - alpha-CD3 scFv Domain - alpha 
       - CD3 VHiGL4

<400>  153

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


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


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


Ala Arg Ile Arg Ser Lys Ala Asn Ser Tyr Ala Thr Glu Tyr Ala Ala 
    50                  55                  60                  


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


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                85                  90                  95      


Tyr Cys Val Arg His Gly Asn Ala Gly Asn Ser Ala Ile Ser Tyr Trp 
            100                 105                 110         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125 


<210>  154
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHiGL4CDR1 - alpha-CD3 scFv Domain - alpha - CD3 
       VHiGL4

<400>  154

Gly Phe Thr Phe Ser Gly Tyr Ala Met Asn 
1               5                   10  


<210>  155
<211>  19
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHiGL4CDR2 - alpha-CD3 scFv Domain - alpha - CD3 
       VHiGL4

<400>  155

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


Val Lys Asp 
            


<210>  156
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic aVHiGL4CDR3 - alpha-CD3 scFv Domain - alpha - CD3 
       VHiGL4

<400>  156

His Gly Asn Ala Gly Asn Ser Ala Ile Ser Tyr Trp Ala Tyr 
1               5                   10                  


<210>  157
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP 2/9

<400>  157

Gly Pro Ala Gly Met Lys Gly Leu 
1               5               


<210>  158
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP 2/9

<400>  158

Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser 
1               5                   10                  15  


<210>  159
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP 2/9

<400>  159

Ser Gly Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Gly 
1               5                   10                  15      


Ser 
    


<210>  160
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin A/B

<400>  160

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


<210>  161
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin A/B

<400>  161

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


<210>  162
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin A/B

<400>  162

Lys Lys Leu Ala Asp Glu Pro Glu 
1               5               


<210>  163
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin A/B (Variant, high 
       efficiency)

<400>  163

Gly Gly Gly Lys Phe Leu Ala Asp Glu Pro Glu Gly Gly 
1               5                   10              


<210>  164
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Cathepsin S,K,L

<400>  164

Ser Gly Gly Gly Ala Arg Leu Gln Ser Ala Ala Pro Gly Gly Gly Ser 
1               5                   10                  15      


<210>  165
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Cathepsin S,K,L

<400>  165

Ser Gly Gly Gly Ala Arg Leu Gln Ser Ala Ala Pro Gly Gly Gly Ser 
1               5                   10                  15      


<210>  166
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Cathepsin S,K,L

<400>  166

Ala Arg Leu Gln Ser Ala Ala Pro 
1               5               


<210>  167
<211>  18
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin/Granzyme B

<400>  167

Ser Gly Gly Gly Gly Val Tyr Ala Asp Ser Leu Glu Asp Gly Gly Gly 
1               5                   10                  15      


Gly Ser 
        


<210>  168
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Meprin/Granzyme B

<400>  168

Gly Val Tyr Ala Asp Ser Leu Glu Asp Gly 
1               5                   10  


<210>  169
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Matriptase/uPA (MS)

<400>  169

Gly Gly Gly Ser Leu Ser Gly Arg Ser Asp Asn His Gly Gly Gly Ser 
1               5                   10                  15      


<210>  170
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Matriptase/uPA (MS)

<400>  170

Gly Leu Ser Gly Arg Ser Asp Asn His Gly 
1               5                   10  


<210>  171
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Matriptase (MV)

<400>  171

Ser Gly Gly Gly Ser Phe Thr Arg Gln Ala Arg Val Val Gly Gly Gly 
1               5                   10                  15      


Ser 
    


<210>  172
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Matriptase (MV)

<400>  172

Ser Phe Thr Arg Gln Ala Arg Val Val 
1               5                   


<210>  173
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - CathepsinS/MMP9/Meprin A

<400>  173

Ala Arg Leu Gln Ser Ala Ala Pro Ala Gly Leu Lys Gly Ala 
1               5                   10                  


<210>  174
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - CathepsinS/MMP9/Meprin A

<400>  174

Gly Ala Arg Leu Gln Ser Ala Ala Pro Ala Gly Leu Lys Gly Ala Gly 
1               5                   10                  15      


<210>  175
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9 (Variant, high efficiency)

<400>  175

Gly Gly Pro Gly Pro Ala Gly Met His Gly Leu Pro Gly 
1               5                   10              


<210>  176
<211>  17
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9 (Variant, high efficiency)

<400>  176

Gly Ser Gly Gly Pro Gly Pro Ala Gly Met His Gly Leu Pro Gly Gly 
1               5                   10                  15      


Ser 
    


<210>  177
<211>  13
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9 (Variant, low efficiency)

<400>  177

Gly Gly Pro Gly Pro Ala Gly Met Glu Gly Leu Pro Gly 
1               5                   10              


<210>  178
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9-15 (K>E)

<400>  178

Ser Gly Gly Pro Gly Pro Ala Gly Met Glu Gly Leu Pro Gly Ser 
1               5                   10                  15  


<210>  179
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9-15 (M>P)

<400>  179

Ser Gly Gly Pro Gly Pro Ala Gly Pro Lys Gly Leu Pro Gly Ser 
1               5                   10                  15  


<210>  180
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Thrombin 1

<400>  180

Gly Gly Gly Gly Leu Val Pro Arg Gly Ser Leu Gly Gly Gly Gly Ser 
1               5                   10                  15      


<210>  181
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Thrombin 2

<400>  181

Ser Ser Gly Gly Gly Met Pro Arg Ser Phe Arg Gly Gly Gly Ser 
1               5                   10                  15  


<210>  182
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - Enterokinase/Flag

<400>  182

Gly Gly Gly Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Gly Gly Ser 
1               5                   10                  15      


<210>  183
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - KLK7-6

<400>  183

Ser Gly Gly Gly Gln Asn Pro Tyr Ser Ala Gly Arg Gly Gly Gly Ser 
1               5                   10                  15      


<210>  184
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - KLK7-13

<400>  184

Ser Gly Gly Gly Gln Asn Pro Tyr Ser Ala Gly Gly Gly Ser Gly Gly 
1               5                   10                  15      


<210>  185
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - KLK7-11

<400>  185

Ser Gly Gly Gly Arg Asn Val Tyr Ser Ala Gly Gly Gly Ser Gly Gly 
1               5                   10                  15      


<210>  186
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - KLK7-10

<400>  186

Ser Gly Gly Gly Gln Asn Thr Trp Ser Ala Gly Lys Gly Gly Gly Ser 
1               5                   10                  15      


<210>  187
<211>  16
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - uPA

<400>  187

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


<210>  188
<211>  15
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic cleavable linker - MMP9-2

<400>  188

Ser Gly Gly Pro Gly Pro Ala Gly Leu Lys Gly Ala Pro Gly Ser 
1               5                   10                  15  


<210>  189
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP7

<400>  189

Lys Arg Ala Leu Gly Leu Pro Gly 
1               5               


<210>  190
<211>  24
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP7


<220>
<221>  MISC_FEATURE
<222>  (1)..(8)
<223>  X can be Asp or Glu

<220>
<221>  MISC_FEATURE
<222>  (17)..(24)
<223>  X can be Asp or Arg

<400>  190

Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Arg Pro Leu Ala Leu Trp Arg Ser 
1               5                   10                  15      


Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 
            20                  


<210>  191
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP9

<400>  191

Pro Arg Ser Thr Leu Ile Ser Thr 
1               5               


<210>  192
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP9

<400>  192

Leu Glu Ala Thr Ala 
1               5   


<210>  193
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP11

<400>  193

Gly Gly Ala Ala Asn Leu Val Arg Gly Gly 
1               5                   10  


<210>  194
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP14

<400>  194

Ser Gly Arg Ile Gly Phe Leu Arg Thr Ala 
1               5                   10  


<210>  195
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP

<400>  195

Pro Leu Gly Leu Ala Gly 
1               5       


<210>  196
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP


<220>
<221>  misc_feature
<222>  (6)..(6)
<223>  Xaa can be any naturally occurring amino acid

<400>  196

Pro Leu Gly Leu Ala Xaa 
1               5       


<210>  197
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP


<220>
<221>  MISC_FEATURE
<222>  (5)..(5)
<223>  X can be Met or Glu

<400>  197

Pro Leu Gly Cys Xaa Ala Gly 
1               5           


<210>  198
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP

<400>  198

Glu Ser Pro Ala Tyr Tyr Thr Ala 
1               5               


<210>  199
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP

<400>  199

Arg Leu Gln Leu Lys Leu 
1               5       


<210>  200
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP

<400>  200

Arg Leu Gln Leu Lys Ala Cys 
1               5           


<210>  201
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - MMP2, MMP9, MMP14


<220>
<221>  MISC_FEATURE
<222>  (3)..(3)
<223>  X can be Cys or Ile or Thr

<220>
<221>  MISC_FEATURE
<222>  (5)..(5)
<223>  X can be His or Orn or Phe

<400>  201

Glu Pro Xaa Gly Xaa Tyr Leu 
1               5           


<210>  202
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Urokinase plasminogen 
       activator (upa)

<400>  202

Ser Gly Arg Ser Ala 
1               5   


<210>  203
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Urokinase plasminogen 
       activator (upa)

<400>  203

Asp Ala Phe Lys 
1               


<210>  204
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Urokinase plasminogen 
       activator (upa)

<400>  204

Gly Gly Gly Arg Arg 
1               5   


<210>  205
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Lysosomal enzyme

<400>  205

Gly Phe Leu Gly 
1               


<210>  206
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Lysosomal enzyme

<400>  206

Ala Leu Ala Leu 
1               


<210>  207
<211>  2
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Lysosomal enzyme

<400>  207

Phe Lys 
1       


<210>  208
<211>  3
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Cathepsin B

<400>  208

Asn Leu Leu 
1           


<210>  209
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Cathepsin D


<220>
<221>  MISC_FEATURE
<222>  (4)..(4)

<400>  209

Pro Ile Cys Xaa Phe Phe 
1               5       


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

<220>
<223>  Synthetic protease cleavage site - Cathepsin K

<400>  210

Gly Gly Pro Arg Gly Leu Pro Gly 
1               5               


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

<220>
<223>  Synthetic protease cleavage site - Prostate specific antigen

<400>  211

His Ser Ser Lys Leu Gln 
1               5       


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

<220>
<223>  Synthetic protease cleavage site - Prostate specific antigen

<400>  212

His Ser Ser Lys Leu Gln Leu 
1               5           


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

<220>
<223>  Synthetic protease cleavage site - Prostate specific antigen

<400>  213

His Ser Ser Lys Leu Gln Glu Asp Ala 
1               5                   


<210>  214
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Herpes simplex virus protease

<400>  214

Leu Val Leu Ala Ser Ser Ser Phe Gly Tyr 
1               5                   10  


<210>  215
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Hiv protease

<400>  215

Gly Val Ser Gln Asn Tyr Pro Ile Val Gly 
1               5                   10  


<210>  216
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Cmv protease

<400>  216

Gly Val Val Gln Ala Ser Cys Arg Leu Ala 
1               5                   10  


<210>  217
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Thrombin


<220>
<221>  misc_feature
<222>  (2)..(2)
<223>  Xaa can be any naturally occurring amino acid

<400>  217

Phe Xaa Arg Ser 
1               


<210>  218
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Thrombin

<400>  218

Asp Pro Arg Ser Phe Leu 
1               5       


<210>  219
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Thrombin

<400>  219

Pro Pro Arg Ser Phe Leu 
1               5       


<210>  220
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Caspase-3

<400>  220

Asp Glu Val Asp 
1               


<210>  221
<211>  5
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Caspase-3

<400>  221

Asp Glu Val Asp Pro 
1               5   


<210>  222
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Caspase-3

<400>  222

Lys Gly Ser Gly Asp Val Glu Gly 
1               5               


<210>  223
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Interleukin 1-beta converting 
       enzyme

<400>  223

Gly Trp Glu His Asp Gly 
1               5       


<210>  224
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Enterokinase

<400>  224

Glu Asp Asp Asp Asp Lys Ala 
1               5           


<210>  225
<211>  9
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Fap

<400>  225

Lys Gln Glu Gln Asn Pro Gly Ser Thr 
1               5                   


<210>  226
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Kallikrein 2

<400>  226

Gly Lys Ala Phe Arg Arg 
1               5       


<210>  227
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Plasmin

<400>  227

Asp Ala Phe Lys 
1               


<210>  228
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Plasmin

<400>  228

Asp Val Leu Lys 
1               


<210>  229
<211>  4
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Plasmin

<400>  229

Asp Ala Phe Lys 
1               


<210>  230
<211>  7
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic protease cleavage site - Top

<400>  230

Ala Leu Leu Leu Ala Leu Leu 
1               5           


<210>  231
<211>  889
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro140 Format 1

<400>  231

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Pro Ala Gly Met Lys Gly Leu Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser 
                885                 


<210>  232
<211>  890
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro140b Format 1

<400>  232

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Lys Lys Leu Ala Asp Glu Pro Glu Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Lys Lys 
            500                 505                 510         


Leu Ala Asp Glu Pro Glu Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser 
                885                 890 


<210>  233
<211>  889
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro186 Format 2

<400>  233

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser 
                885                 


<210>  234
<211>  890
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro187 Format 2

<400>  234

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Lys Lys 
            500                 505                 510         


Leu Ala Asp Glu Pro Glu Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser 
                885                 890 


<210>  235
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro225 (FL aB7H3 hF7 MMP9 linker) Format 2

<400>  235

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  236
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro226 (FL aB7H3 hF12 MMP9 linker) Format 2

<400>  236

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  237
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro233 (humanized Pro186) Format 2

<400>  237

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Val Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Thr Leu Ser Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  238
<211>  875
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro311 (FL aFOLR1 h77.2 MMP9 linker) Format
       2

<400>  238

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
        115                 120                 125             


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
    130                 135                 140                 


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg 
145                 150                 155                 160 


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


Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe 
            180                 185                 190         


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
        195                 200                 205             


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala 
    210                 215                 220                 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
            260                 265                 270         


Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
        275                 280                 285             


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
    290                 295                 300                 


Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser 
305                 310                 315                 320 


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
                325                 330                 335     


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg 
            340                 345                 350         


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    370                 375                 380                 


Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
385                 390                 395                 400 


Val Ser Asn Ser Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu 
                405                 410                 415     


Arg Glu Phe Val Ala Ile Ile Asn Ser Ile Gly Ile Thr Asn Tyr Ala 
            420                 425                 430         


Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn 
        435                 440                 445             


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val 
    450                 455                 460                 


Tyr Val Cys Asn Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr 
465                 470                 475                 480 


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
                485                 490                 495     


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
            500                 505                 510         


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
        515                 520                 525             


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
    530                 535                 540                 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
545                 550                 555                 560 


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
                565                 570                 575     


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
            580                 585                 590         


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
        595                 600                 605             


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
    610                 615                 620                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
625                 630                 635                 640 


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
                645                 650                 655     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 
            660                 665                 670         


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
        675                 680                 685             


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
    690                 695                 700                 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
705                 710                 715                 720 


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
                725                 730                 735     


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
            740                 745                 750         


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
        755                 760                 765             


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
    770                 775                 780                 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
785                 790                 795                 800 


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
                805                 810                 815     


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
            820                 825                 830         


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
        835                 840                 845             


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
    850                 855                 860                 


Val Thr Val Ser Ser His His His His His His 
865                 870                 875 


<210>  239
<211>  873
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro312 (FL aFOLR1 h59.3 MMP9 linker)

<400>  239

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


Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser 
            20                  25                  30          


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


Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys 
                85                  90                  95      


His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
            100                 105                 110         


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
        115                 120                 125             


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
    130                 135                 140                 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
145                 150                 155                 160 


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
                165                 170                 175     


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
        195                 200                 205             


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
    210                 215                 220                 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
225                 230                 235                 240 


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
                245                 250                 255     


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
            260                 265                 270         


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
        275                 280                 285             


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
    290                 295                 300                 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
305                 310                 315                 320 


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
                325                 330                 335     


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
            340                 345                 350         


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
    370                 375                 380                 


Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe 
385                 390                 395                 400 


Ser Ile Ser Ala Met Gly Trp Tyr Arg Gln Ala Pro Gly Lys Gln Arg 
                405                 410                 415     


Glu Trp Val Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp 
            420                 425                 430         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr 
        435                 440                 445             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Lys His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val 
465                 470                 475                 480 


Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu 
                485                 490                 495     


Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 
            500                 505                 510         


Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val 
        515                 520                 525             


Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 
    530                 535                 540                 


Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr 
545                 550                 555                 560 


Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr 
                565                 570                 575     


Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu 
            580                 585                 590         


Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 
        595                 600                 605             


Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
    610                 615                 620                 


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
625                 630                 635                 640 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln 
                645                 650                 655     


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
            660                 665                 670         


Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe 
        675                 680                 685             


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
    690                 695                 700                 


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly 
705                 710                 715                 720 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
                725                 730                 735     


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
            740                 745                 750         


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn 
        755                 760                 765             


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
    770                 775                 780                 


Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
785                 790                 795                 800 


Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val 
                805                 810                 815     


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
            820                 825                 830         


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
        835                 840                 845             


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
    850                 855                 860                 


Val Ser Ser His His His His His His 
865                 870             


<210>  240
<211>  761
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro313 (FL aFOLR1 h22.4 MMP9 linker) Format
       2

<400>  240

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


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
            20                  25                  30          


Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys 
        35                  40                  45              


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


Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
65                  70                  75                  80  


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


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser 
            100                 105                 110         


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
        115                 120                 125             


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
    130                 135                 140                 


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
145                 150                 155                 160 


Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
                165                 170                 175     


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys 
            180                 185                 190         


Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
        195                 200                 205             


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
    210                 215                 220                 


Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
225                 230                 235                 240 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
            260                 265                 270         


Leu Arg Leu Ser Cys Glu Ala Ser Gly Thr Thr Phe Ser Arg Asp Val 
        275                 280                 285             


Met Gly Trp Tyr Arg Gln Ala Pro Gly Lys Gln Arg Glu Leu Val Ala 
    290                 295                 300                 


Ile Ile Ser Arg Gly Gly Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly 
305                 310                 315                 320 


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
                325                 330                 335     


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Asn Ala 
            340                 345                 350         


Asn Thr Ala Thr Trp Gly Arg Val Phe Trp Gly Gln Gly Thr Leu Val 
        355                 360                 365             


Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu 
    370                 375                 380                 


Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 
385                 390                 395                 400 


Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val 
                405                 410                 415     


Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 
            420                 425                 430         


Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr 
        435                 440                 445             


Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr 
    450                 455                 460                 


Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu 
465                 470                 475                 480 


Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 
                485                 490                 495     


Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
            500                 505                 510         


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
        515                 520                 525             


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln 
    530                 535                 540                 


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
545                 550                 555                 560 


Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe 
                565                 570                 575     


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
            580                 585                 590         


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly 
        595                 600                 605             


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
    610                 615                 620                 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn 
                645                 650                 655     


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
            660                 665                 670         


Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val 
    690                 695                 700                 


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser His His His His His His 
        755                 760     


<210>  241
<211>  898
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro246 (FL haEGFR1/haEGFR2 heterologous 
       COBRA with MMP9 linker)

<400>  241

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


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


Ala Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr 
            100                 105                 110         


Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        115                 120                 125             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    130                 135                 140                 


Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser 
145                 150                 155                 160 


Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro 
                165                 170                 175     


Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn 
            180                 185                 190         


Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser 
        195                 200                 205             


Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys 
    210                 215                 220                 


Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly 
225                 230                 235                 240 


Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val 
                245                 250                 255     


Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val 
            260                 265                 270         


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
        275                 280                 285             


Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
    290                 295                 300                 


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly 
305                 310                 315                 320 


Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
                325                 330                 335     


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


Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe 
        355                 360                 365             


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
    370                 375                 380                 


Ser Gln Val Lys Leu Val Glu Ser Gly Gly Gly Val Val Arg Pro Gly 
385                 390                 395                 400 


Gly Ser Leu Thr Leu Ser Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser 
                405                 410                 415     


Tyr Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe 
            420                 425                 430         


Val Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser 
        435                 440                 445             


Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu 
    450                 455                 460                 


Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr 
465                 470                 475                 480 


Cys Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr 
                485                 490                 495     


Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly 
            500                 505                 510         


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val 
        515                 520                 525             


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
    530                 535                 540                 


Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
545                 550                 555                 560 


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp 
                565                 570                 575     


Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser 
            580                 585                 590         


Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu 
        595                 600                 605             


Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val 
    610                 615                 620                 


Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly 
625                 630                 635                 640 


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
                645                 650                 655     


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
            660                 665                 670         


Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
        675                 680                 685             


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp 
    690                 695                 700                 


Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser 
705                 710                 715                 720 


Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr 
                725                 730                 735     


Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile 
            740                 745                 750         


Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        755                 760                 765             


Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
    770                 775                 780                 


Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala 
785                 790                 795                 800 


Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln 
                805                 810                 815     


Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly 
            820                 825                 830         


Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser 
        835                 840                 845             


Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg 
    850                 855                 860                 


Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser 
865                 870                 875                 880 


Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His 
                885                 890                 895     


His His 
        


<210>  242
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro256 (FL haEpCAM VIB13/haEGFR1 
       heterologous COBRA MMP9 linker)

<400>  242

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


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


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


Leu Val Ala Arg Ile Thr Ser Gly Asp Ser Thr Val Tyr Ala Asp Ser 
    50                  55                  60                  


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


Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr 
                85                  90                  95      


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


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Lys Leu 
    370                 375                 380                 


Val Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly Ser Leu Thr Leu 
385                 390                 395                 400 


Ser Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly Ile Ser 
            420                 425                 430         


Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys Ala Ala Ala Ala 
465                 470                 475                 480 


Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  243
<211>  885
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro420 (FL aFOLR1 h77.2/haEGFR1 
       heterologous COBRA MMP9 linker)

<400>  243

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
        115                 120                 125             


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
    130                 135                 140                 


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg 
145                 150                 155                 160 


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


Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe 
            180                 185                 190         


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
        195                 200                 205             


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala 
    210                 215                 220                 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
            260                 265                 270         


Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
        275                 280                 285             


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
    290                 295                 300                 


Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser 
305                 310                 315                 320 


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
                325                 330                 335     


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg 
            340                 345                 350         


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Ser Gln Val Lys Leu Val Glu Ser Gly Gly Gly Val Val 
    370                 375                 380                 


Arg Pro Gly Gly Ser Leu Thr Leu Ser Cys Ala Ala Ser Gly Arg Thr 
385                 390                 395                 400 


Ser Arg Ser Tyr Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu 
                405                 410                 415     


Arg Glu Phe Val Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr 
            420                 425                 430         


Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        435                 440                 445             


Asn Ser Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala 
    450                 455                 460                 


Leu Tyr Tyr Cys Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu 
465                 470                 475                 480 


Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                485                 490                 495     


Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln 
            500                 505                 510         


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
        515                 520                 525             


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
    530                 535                 540                 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
545                 550                 555                 560 


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
                565                 570                 575     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            580                 585                 590         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
        595                 600                 605             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    610                 615                 620                 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
625                 630                 635                 640 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
                645                 650                 655     


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
            660                 665                 670         


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


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
    690                 695                 700                 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
705                 710                 715                 720 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
                725                 730                 735     


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        755                 760                 765             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
    770                 775                 780                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
785                 790                 795                 800 


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
                805                 810                 815     


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
            820                 825                 830         


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
        835                 840                 845             


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
    850                 855                 860                 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
865                 870                 875                 880 


His His His His His 
                885 


<210>  244
<211>  885
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro421 (FL haEGFR1/aFOLR1 h77.2 
       heterologous COBRA MMP9 linker)

<400>  244

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Val Ser Asn Ser Val Met 
                405                 410                 415     


Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val Ala Ile 
            420                 425                 430         


Ile Asn Ser Ile Gly Ile Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg 
        435                 440                 445             


Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met 
    450                 455                 460                 


Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Val Cys Asn Arg Asn 
465                 470                 475                 480 


Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                485                 490                 495     


Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln 
            500                 505                 510         


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
        515                 520                 525             


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
    530                 535                 540                 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
545                 550                 555                 560 


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
                565                 570                 575     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            580                 585                 590         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
        595                 600                 605             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    610                 615                 620                 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
625                 630                 635                 640 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
                645                 650                 655     


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
            660                 665                 670         


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


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
    690                 695                 700                 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
705                 710                 715                 720 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
                725                 730                 735     


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        755                 760                 765             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
    770                 775                 780                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
785                 790                 795                 800 


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
                805                 810                 815     


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
            820                 825                 830         


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
        835                 840                 845             


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
    850                 855                 860                 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
865                 870                 875                 880 


His His His His His 
                885 


<210>  245
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro393 (Pro186 S9 linker)

<400>  245

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Ala Arg Leu Gln Ser 
            500                 505                 510         


Ala Ala Pro Ala Gly Leu Lys Gly Ala Gly Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  246
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro394 (Pro186 ST14(MV) linker)

<400>  246

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Phe Thr 
            500                 505                 510         


Arg Gln Ala Arg Val Val Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  247
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro395 (Pro186 CathS linker)

<400>  247

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Ala Arg 
            500                 505                 510         


Leu Gln Ser Ala Ala Pro Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  248
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro396 (Pro186 MMP9v linker)

<400>  248

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly 
            500                 505                 510         


Pro Ala Gly Met His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  249
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro429 (Pro186 Meprin/GranzymeB linker)

<400>  249

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Val Tyr 
            500                 505                 510         


Ala Asp Ser Leu Glu Asp Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  250
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro430 (Pro186 MMP9-2 linker)

<400>  250

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Leu Lys Gly Ala Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  251
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro431 (Pro186 ST14(MS) linker)

<400>  251

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Leu Ser 
            500                 505                 510         


Gly Arg Ser Asp Asn His Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  252
<211>  763
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro258 (Pro186 with a single aEGFR domain 
       and a central aHSA domain)

<400>  252

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
    370                 375                 380                 


Gly Leu Pro Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
385                 390                 395                 400 


Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe 
                405                 410                 415     


Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys 
            420                 425                 430         


Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu 
        435                 440                 445             


Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala 
    450                 455                 460                 


Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr 
465                 470                 475                 480 


Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly 
            500                 505                 510         


Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly 
        515                 520                 525             


Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser 
    530                 535                 540                 


Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg 
545                 550                 555                 560 


Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala 
                565                 570                 575     


Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser 
            580                 585                 590         


Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr 
        595                 600                 605             


Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 
    610                 615                 620                 


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
625                 630                 635                 640 


Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser 
                645                 650                 655     


Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro 
            660                 665                 670         


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


Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile 
    690                 695                 700                 


Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu 
705                 710                 715                 720 


Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe 
                725                 730                 735     


Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu 
            740                 745                 750         


Val Thr Val Ser Ser His His His His His His 
        755                 760             


<210>  253
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro221 - Cleavable linker variant

<400>  253

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Gln Asn 
            500                 505                 510         


Pro Tyr Ser Ala Gly Arg Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  254
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro222 - Cleavable linker variant

<400>  254

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Gln Asn 
            500                 505                 510         


Pro Tyr Ser Ala Gly Gly Gly Ser Gly Gly Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  255
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro223 - Cleavable linker variant

<400>  255

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Arg Asn 
            500                 505                 510         


Val Tyr Ser Ala Gly Gly Gly Ser Gly Gly Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  256
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro224- Cleavable linker variant

<400>  256

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Gln Asn 
            500                 505                 510         


Thr Trp Ser Ala Gly Lys Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  257
<211>  898
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro254- Heterologous Format 2

<400>  257

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Ser Tyr Ala Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Val Ala 
            420                 425                 430         


Ile Asn Trp Ser Ser Gly Ser Thr Tyr Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr Glu Tyr 
                485                 490                 495     


Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly 
            500                 505                 510         


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val 
        515                 520                 525             


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
    530                 535                 540                 


Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
545                 550                 555                 560 


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp 
                565                 570                 575     


Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser 
            580                 585                 590         


Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu 
        595                 600                 605             


Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val 
    610                 615                 620                 


Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly 
625                 630                 635                 640 


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
                645                 650                 655     


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
            660                 665                 670         


Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
        675                 680                 685             


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp 
    690                 695                 700                 


Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser 
705                 710                 715                 720 


Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr 
                725                 730                 735     


Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile 
            740                 745                 750         


Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
        755                 760                 765             


Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
    770                 775                 780                 


Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala 
785                 790                 795                 800 


Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln 
                805                 810                 815     


Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly 
            820                 825                 830         


Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser 
        835                 840                 845             


Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg 
    850                 855                 860                 


Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser 
865                 870                 875                 880 


Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His 
                885                 890                 895     


His His 
        


<210>  258
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro255- Heterologous Format 2

<400>  258

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Thr Leu Ser Cys Ala Ala Ser Gly Thr Gly Ser Ile Phe Ser Ile Asn 
                405                 410                 415     


Leu Met Gly Trp Tyr Arg Gln Ala Pro Gly Lys Gln Arg Glu Leu Val 
            420                 425                 430         


Ala Arg Ile Thr Ser Gly Asp Ser Thr Val Tyr Ala Asp Ser Val Lys 
        435                 440                 445             


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
    450                 455                 460                 


Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Asn 
465                 470                 475                 480 


Leu Leu Leu Arg Ser Ser Pro Gly Ala Thr Thr Pro Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  259
<211>  902
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro262

<400>  259

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
            260                 265                 270         


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
        275                 280                 285             


Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly 
    290                 295                 300                 


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
305                 310                 315                 320 


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
                325                 330                 335     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            340                 345                 350         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
        355                 360                 365             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    370                 375                 380                 


Ser Gly Gly Gly Ser Gln Val Lys Leu Glu Glu Ser Gly Gly Gly Ser 
385                 390                 395                 400 


Val Gln Thr Gly Gly Ser Leu Arg Leu Thr Cys Ala Ala Ser Gly Arg 
                405                 410                 415     


Thr Ser Arg Ser Tyr Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys 
            420                 425                 430         


Glu Arg Glu Phe Val Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly 
        435                 440                 445             


Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala 
    450                 455                 460                 


Lys Asn Thr Val Asp Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr 
465                 470                 475                 480 


Ala Ile Tyr Tyr Cys Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr 
                485                 490                 495     


Leu Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser 
            500                 505                 510         


Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser 
        515                 520                 525             


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
    530                 535                 540                 


Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly 
545                 550                 555                 560 


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
                565                 570                 575     


Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg 
            580                 585                 590         


Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly 
        595                 600                 605             


Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser 
    610                 615                 620                 


Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly 
625                 630                 635                 640 


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
                645                 650                 655     


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
            660                 665                 670         


Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly 
        675                 680                 685             


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys 
    690                 695                 700                 


Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser 
705                 710                 715                 720 


Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys 
                725                 730                 735     


Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly 
            740                 745                 750         


Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val 
        755                 760                 765             


Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
    770                 775                 780                 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg 
785                 790                 795                 800 


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser 
                805                 810                 815     


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile 
            820                 825                 830         


Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg 
        835                 840                 845             


Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met 
    850                 855                 860                 


Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly 
865                 870                 875                 880 


Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser 
                885                 890                 895     


His His His His His His 
            900         


<210>  260
<211>  766
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro356 - Format 4

<400>  260

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


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


Ala Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Tyr Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr 
            100                 105                 110         


Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        115                 120                 125             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    130                 135                 140                 


Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser 
145                 150                 155                 160 


Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro 
                165                 170                 175     


Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn 
            180                 185                 190         


Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser 
        195                 200                 205             


Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys 
    210                 215                 220                 


Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly 
225                 230                 235                 240 


Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val 
                245                 250                 255     


Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val 
            260                 265                 270         


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
        275                 280                 285             


Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
    290                 295                 300                 


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly 
305                 310                 315                 320 


Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
                325                 330                 335     


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


Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe 
        355                 360                 365             


Gly Gly Gly Thr Lys Leu Thr Val Leu Ser Gly Gly Pro Gly Pro Ala 
    370                 375                 380                 


Gly Met Lys Gly Leu Pro Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
385                 390                 395                 400 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
                405                 410                 415     


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
            420                 425                 430         


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
        435                 440                 445             


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
    450                 455                 460                 


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
465                 470                 475                 480 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
                485                 490                 495     


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
            500                 505                 510         


Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val 
        515                 520                 525             


Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala 
    530                 535                 540                 


Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln 
545                 550                 555                 560 


Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly 
                565                 570                 575     


Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu 
            580                 585                 590         


Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val 
        595                 600                 605             


Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr 
    610                 615                 620                 


Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
625                 630                 635                 640 


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
                645                 650                 655     


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg 
            660                 665                 670         


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


Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg 
    690                 695                 700                 


Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met 
705                 710                 715                 720 


Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 
                725                 730                 735     


Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln 
            740                 745                 750         


Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
        755                 760                 765     


<210>  261
<211>  763
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro359 - Format 4

<400>  261

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
    370                 375                 380                 


Gly Leu Pro Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
385                 390                 395                 400 


Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe 
                405                 410                 415     


Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys 
            420                 425                 430         


Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu 
        435                 440                 445             


Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala 
    450                 455                 460                 


Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr 
465                 470                 475                 480 


Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly 
            500                 505                 510         


Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly 
        515                 520                 525             


Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser 
    530                 535                 540                 


Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg 
545                 550                 555                 560 


Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala 
                565                 570                 575     


Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser 
            580                 585                 590         


Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr 
        595                 600                 605             


Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 
    610                 615                 620                 


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
625                 630                 635                 640 


Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser 
                645                 650                 655     


Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro 
            660                 665                 670         


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


Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile 
    690                 695                 700                 


Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu 
705                 710                 715                 720 


Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe 
                725                 730                 735     


Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu 
            740                 745                 750         


Val Thr Val Ser Ser His His His His His His 
        755                 760             


<210>  262
<211>  752
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro364 - Format 4

<400>  262

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


Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser 
            20                  25                  30          


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


Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys 
                85                  90                  95      


His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
            100                 105                 110         


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
        115                 120                 125             


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
    130                 135                 140                 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
145                 150                 155                 160 


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
                165                 170                 175     


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
        195                 200                 205             


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
    210                 215                 220                 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
225                 230                 235                 240 


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
                245                 250                 255     


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
            260                 265                 270         


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
        275                 280                 285             


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
    290                 295                 300                 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
305                 310                 315                 320 


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
                325                 330                 335     


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
            340                 345                 350         


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Ser Gly Gly Pro Gly 
        355                 360                 365             


Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Glu Val Gln Leu Val Glu 
    370                 375                 380                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
385                 390                 395                 400 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                405                 410                 415     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            420                 425                 430         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        435                 440                 445             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    450                 455                 460                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
465                 470                 475                 480 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
                485                 490                 495     


Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu 
            500                 505                 510         


Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr 
        515                 520                 525             


Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro 
    530                 535                 540                 


Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp 
545                 550                 555                 560 


Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                565                 570                 575     


Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr 
            580                 585                 590         


Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        595                 600                 605             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
    610                 615                 620                 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
625                 630                 635                 640 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp 
                645                 650                 655     


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
            660                 665                 670         


Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys 
        675                 680                 685             


Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu 
    690                 695                 700                 


Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val 
705                 710                 715                 720 


Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp 
                725                 730                 735     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
            740                 745                 750         


<210>  263
<211>  753
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro388 - Format 4

<400>  263

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
        115                 120                 125             


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
    130                 135                 140                 


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg 
145                 150                 155                 160 


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


Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe 
            180                 185                 190         


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
        195                 200                 205             


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala 
    210                 215                 220                 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
            260                 265                 270         


Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
        275                 280                 285             


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
    290                 295                 300                 


Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser 
305                 310                 315                 320 


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
                325                 330                 335     


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg 
            340                 345                 350         


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Ser Gly Gly Pro 
        355                 360                 365             


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Glu Val Gln Leu Val 
    370                 375                 380                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
385                 390                 395                 400 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
                405                 410                 415     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
            420                 425                 430         


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
        435                 440                 445             


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
    450                 455                 460                 


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
465                 470                 475                 480 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
                485                 490                 495     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            500                 505                 510         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
        515                 520                 525             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    530                 535                 540                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
545                 550                 555                 560 


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                565                 570                 575     


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
            580                 585                 590         


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        595                 600                 605             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
    610                 615                 620                 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
625                 630                 635                 640 


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
                645                 650                 655     


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
            660                 665                 670         


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
        675                 680                 685             


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
    690                 695                 700                 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
705                 710                 715                 720 


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
                725                 730                 735     


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
            740                 745                 750         


His 
    


<210>  264
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro429 - Format 4

<400>  264

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Gly Val Tyr 
            500                 505                 510         


Ala Asp Ser Leu Glu Asp Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  265
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro430 - Format 4

<400>  265

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Leu Lys Gly Ala Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  266
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro431 - Format 4

<400>  266

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser Leu Ser 
            500                 505                 510         


Gly Arg Ser Asp Asn His Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  267
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro432- Heterologous - Format 2

<400>  267

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


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


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


Leu Val Ala Arg Ile Thr Ser Gly Asp Ser Thr Val Tyr Ala Asp Ser 
    50                  55                  60                  


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


Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr 
                85                  90                  95      


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


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
    370                 375                 380                 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Ser Tyr Ala Met Gly Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Val Ala Ile Asn 
            420                 425                 430         


Trp Ser Ser Gly Ser Thr Tyr Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Tyr 
465                 470                 475                 480 


Gln Ile Asn Ser Gly Asn Tyr Asn Phe Lys Asp Tyr Glu Tyr Asp Tyr 
                485                 490                 495     


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly 
            500                 505                 510         


Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  268
<211>  636
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro448- Dual Targeting Hemis Format 3

<400>  268

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Lys Leu Val 
        115                 120                 125             


Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly Ser Leu Thr Leu Ser 
    130                 135                 140                 


Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly Trp Phe 
145                 150                 155                 160 


Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly Ile Ser Trp 
                165                 170                 175     


Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gln Met Asn Ser 
        195                 200                 205             


Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys Ala Ala Ala Ala Gly 
    210                 215                 220                 


Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
            260                 265                 270         


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
        275                 280                 285             


Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
    290                 295                 300                 


Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 
305                 310                 315                 320 


Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
                325                 330                 335     


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
            340                 345                 350         


Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
        355                 360                 365             


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly 
    370                 375                 380                 


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val 
385                 390                 395                 400 


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
                405                 410                 415     


Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
            420                 425                 430         


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp 
        435                 440                 445             


Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser 
    450                 455                 460                 


Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu 
465                 470                 475                 480 


Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val 
                485                 490                 495     


Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
        515                 520                 525             


Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
    530                 535                 540                 


Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
545                 550                 555                 560 


Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala 
                565                 570                 575     


Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr 
            580                 585                 590         


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val 
        595                 600                 605             


Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr 
    610                 615                 620                 


Leu Val Thr Val Ser Ser His His His His His His 
625                 630                 635     


<210>  269
<211>  636
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro449 Dual Targeting Hemis Format 3

<400>  269

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly 
        115                 120                 125             


Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
    130                 135                 140                 


Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe 
145                 150                 155                 160 


Thr Val Ser Asn Ser Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn 
                165                 170                 175     


Glu Arg Glu Phe Val Ala Ile Ile Asn Ser Ile Gly Ile Thr Asn Tyr 
            180                 185                 190         


Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys 
        195                 200                 205             


Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Val Cys Asn Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
            260                 265                 270         


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
        275                 280                 285             


Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
    290                 295                 300                 


Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 
305                 310                 315                 320 


Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
                325                 330                 335     


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
            340                 345                 350         


Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
        355                 360                 365             


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly 
    370                 375                 380                 


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val 
385                 390                 395                 400 


Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 
                405                 410                 415     


Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn 
            420                 425                 430         


Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp 
        435                 440                 445             


Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser 
    450                 455                 460                 


Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu 
465                 470                 475                 480 


Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val 
                485                 490                 495     


Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
        515                 520                 525             


Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
    530                 535                 540                 


Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
545                 550                 555                 560 


Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala 
                565                 570                 575     


Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr 
            580                 585                 590         


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val 
        595                 600                 605             


Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr 
    610                 615                 620                 


Leu Val Thr Val Ser Ser His His His His His His 
625                 630                 635     


<210>  270
<211>  636
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro450 Dual Targeting Hemis Format 3

<400>  270

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Lys Leu Val 
        115                 120                 125             


Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly Ser Leu Thr Leu Ser 
    130                 135                 140                 


Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met Gly Trp Phe 
145                 150                 155                 160 


Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly Ile Ser Trp 
                165                 170                 175     


Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gln Met Asn Ser 
        195                 200                 205             


Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys Ala Ala Ala Ala Gly 
    210                 215                 220                 


Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
            260                 265                 270         


Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly 
        275                 280                 285             


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
    290                 295                 300                 


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
305                 310                 315                 320 


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
                325                 330                 335     


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
            340                 345                 350         


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Ser Gly Gly 
        355                 360                 365             


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Glu Val Gln Leu 
    370                 375                 380                 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
385                 390                 395                 400 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp 
                405                 410                 415     


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
            420                 425                 430         


Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys 
        435                 440                 445             


Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu 
    450                 455                 460                 


Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val 
465                 470                 475                 480 


Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
        515                 520                 525             


Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
    530                 535                 540                 


Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
545                 550                 555                 560 


Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala 
                565                 570                 575     


Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr 
            580                 585                 590         


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val 
        595                 600                 605             


Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr 
    610                 615                 620                 


Leu Val Thr Val Ser Ser His His His His His His 
625                 630                 635     


<210>  271
<211>  636
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro451 Dual Targeting Hemis Format 3

<400>  271

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly 
        115                 120                 125             


Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
    130                 135                 140                 


Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe 
145                 150                 155                 160 


Thr Val Ser Asn Ser Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn 
                165                 170                 175     


Glu Arg Glu Phe Val Ala Ile Ile Asn Ser Ile Gly Ile Thr Asn Tyr 
            180                 185                 190         


Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys 
        195                 200                 205             


Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Val Cys Asn Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
            260                 265                 270         


Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly 
        275                 280                 285             


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
    290                 295                 300                 


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
305                 310                 315                 320 


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
                325                 330                 335     


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
            340                 345                 350         


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Ser Gly Gly 
        355                 360                 365             


Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Glu Val Gln Leu 
    370                 375                 380                 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
385                 390                 395                 400 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp 
                405                 410                 415     


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
            420                 425                 430         


Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys 
        435                 440                 445             


Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu 
    450                 455                 460                 


Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val 
465                 470                 475                 480 


Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
        515                 520                 525             


Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
    530                 535                 540                 


Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
545                 550                 555                 560 


Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala 
                565                 570                 575     


Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr 
            580                 585                 590         


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val 
        595                 600                 605             


Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr 
    610                 615                 620                 


Leu Val Thr Val Ser Ser His His His His His His 
625                 630                 635     


<210>  272
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro479- Heterologous - Format 2

<400>  272

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met 
                405                 410                 415     


Ala Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  273
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro480- Heterologous - Format 2

<400>  273

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met Gly Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  274
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro495 - Format 2

<400>  274

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp 
                565                 570                 575     


Asp Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
            580                 585                 590         


Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu 
        595                 600                 605             


Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
    610                 615                 620                 


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
625                 630                 635                 640 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
                645                 650                 655     


Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met 
            660                 665                 670         


Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 
        675                 680                 685             


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


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  275
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro601 aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9-15 - aCD3Vli2 -NCL-8
       - aCD3Vhi2 - aHSA (10GE) - His6

<400>  275

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp 
                565                 570                 575     


Asp Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
            580                 585                 590         


Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu 
        595                 600                 605             


Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
    610                 615                 620                 


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
625                 630                 635                 640 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
                645                 650                 655     


Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met 
            660                 665                 670         


Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 
        675                 680                 685             


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


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  276
<211>  889
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro602 aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - aCD3Vli2 
       -NCL-8 - aCD3Vhi2 - aHSA (10GE) - His6

<400>  276

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp Asp Ala Pro Gly 
                565                 570                 575     


Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu 
            580                 585                 590         


Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val 
        595                 600                 605             


Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr 
    610                 615                 620                 


Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
625                 630                 635                 640 


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
                645                 650                 655     


Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met Asn Trp Val Arg 
            660                 665                 670         


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


Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp Ser Val Lys Asp Arg Phe 
    690                 695                 700                 


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
705                 710                 715                 720 


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly 
                725                 730                 735     


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
            740                 745                 750         


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
        755                 760                 765             


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn 
    770                 775                 780                 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
785                 790                 795                 800 


Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
                805                 810                 815     


Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val 
            820                 825                 830         


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
        835                 840                 845             


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
    850                 855                 860                 


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
865                 870                 875                 880 


Val Ser Ser His His His His His His 
                885                 


<210>  277
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - V3 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - aCD3Vli2 -NCL-8 - 
       aCD3Vhi2 - aHSA (10GE) - His6

<400>  277

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met 
                405                 410                 415     


Ala Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp Asp Ala 
                565                 570                 575     


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
            580                 585                 590         


Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr 
        595                 600                 605             


Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
    610                 615                 620                 


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
625                 630                 635                 640 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
                645                 650                 655     


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met Asn Trp 
            660                 665                 670         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
        675                 680                 685             


Ser Lys Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  278
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - V4 - aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9-15 - aCD3Vli2 -NCL-8
       - aCD3Vhi2 - aHSA (10GE) - His6

<400>  278

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met Gly Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp Gly Gln 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp Asp Ala 
                565                 570                 575     


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
            580                 585                 590         


Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr 
        595                 600                 605             


Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
    610                 615                 620                 


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
625                 630                 635                 640 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
                645                 650                 655     


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met Asn Trp 
            660                 665                 670         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
        675                 680                 685             


Ser Lys Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  279
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro664 - aB7H3 hF12 (S59Y) sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  279

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Tyr Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  280
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro665 - aB7H3 hF12 (N57Q) sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  280

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Gln Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  281
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro667 - aB7H3 hF12 (N57E) sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  281

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Glu Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  282
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro694 - aB7H3 hF12 (S59A) sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  282

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ala Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  283
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro695 - aB7H3 hF12 (N57D) sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  283

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asp Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys 
            500                 505                 510         


Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  284
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro766 - aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - NCL-15 - aCD3Vli -NCL-8 
       - aCD3Vhi - aHSA (10GE) - His6

<400>  284

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Tyr Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 
            500                 505                 510         


Gly Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
        515                 520                 525             


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
    530                 535                 540                 


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
545                 550                 555                 560 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
                565                 570                 575     


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
            580                 585                 590         


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
        595                 600                 605             


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
    610                 615                 620                 


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
625                 630                 635                 640 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
                645                 650                 655     


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
            660                 665                 670         


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


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  285
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro565 acEpCAM hVIB664 sdAb - aCD3 Vh (2B2)
       - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  285

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly 
            500                 505                 510         


Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  286
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro566 - acEpCAM hVIB665 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB665 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  286

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Asp Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly His Thr Asn Tyr Ala Asp Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly 
            500                 505                 510         


Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  287
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro567- acEpCAM hVIB666 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB666 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  287

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Thr Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Arg 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Thr Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly 
            500                 505                 510         


Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  288
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro568 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - NCL-16 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  288

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
            500                 505                 510         


Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  289
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro727 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - Meprin-15 -
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  289

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly 
            500                 505                 510         


Gly Gly Lys Lys Leu Ala Asp Glu Pro Glu Gly Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  290
<211>  901
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro728 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - MMP9v - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  290

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Ser 
            500                 505                 510         


Gly Gly Pro Gly Pro Ala Gly Met His Gly Leu Pro Gly Gly Ser Gln 
        515                 520                 525             


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
    530                 535                 540                 


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
545                 550                 555                 560 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
                565                 570                 575     


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
            580                 585                 590         


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
        595                 600                 605             


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
    610                 615                 620                 


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
625                 630                 635                 640 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
                645                 650                 655     


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
            660                 665                 670         


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
        675                 680                 685             


Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp 
    690                 695                 700                 


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
705                 710                 715                 720 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
                725                 730                 735     


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
            740                 745                 750         


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
        755                 760                 765             


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
    770                 775                 780                 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
785                 790                 795                 800 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
                805                 810                 815     


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
            820                 825                 830         


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
        835                 840                 845             


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
    850                 855                 860                 


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
865                 870                 875                 880 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
                885                 890                 895     


His His His His His 
            900     


<210>  291
<211>  900
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro729  - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - CathS - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  291

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
            500                 505                 510         


Gly Ser Ala Arg Leu Gln Ser Ala Ala Pro Gly Gly Gly Ser Gln Thr 
        515                 520                 525             


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
    530                 535                 540                 


Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
545                 550                 555                 560 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
                565                 570                 575     


Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser 
            580                 585                 590         


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
        595                 600                 605             


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg 
    610                 615                 620                 


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
625                 630                 635                 640 


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
                645                 650                 655     


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
            660                 665                 670         


Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
        675                 680                 685             


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp 
    690                 695                 700                 


Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
705                 710                 715                 720 


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
                725                 730                 735     


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser 
            740                 745                 750         


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
        755                 760                 765             


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
    770                 775                 780                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
785                 790                 795                 800 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
                805                 810                 815     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
            820                 825                 830         


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
        835                 840                 845             


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
    850                 855                 860                 


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
865                 870                 875                 880 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His 
                885                 890                 895     


His His His His 
            900 


<210>  292
<211>  900
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro730 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - S9 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  292

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Ala 
            500                 505                 510         


Arg Leu Gln Ser Ala Ala Pro Ala Gly Leu Lys Gly Ala Gly Gln Thr 
        515                 520                 525             


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
    530                 535                 540                 


Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
545                 550                 555                 560 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
                565                 570                 575     


Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser 
            580                 585                 590         


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
        595                 600                 605             


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg 
    610                 615                 620                 


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
625                 630                 635                 640 


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
                645                 650                 655     


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
            660                 665                 670         


Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
        675                 680                 685             


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp 
    690                 695                 700                 


Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
705                 710                 715                 720 


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
                725                 730                 735     


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser 
            740                 745                 750         


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
        755                 760                 765             


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
    770                 775                 780                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
785                 790                 795                 800 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
                805                 810                 815     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
            820                 825                 830         


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
        835                 840                 845             


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
    850                 855                 860                 


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
865                 870                 875                 880 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His 
                885                 890                 895     


His His His His 
            900 


<210>  293
<211>  900
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro731 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - ST14-MS - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  293

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr 
                405                 410                 415     


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Ala Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
                485                 490                 495     


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
            500                 505                 510         


Gly Ser Leu Ser Gly Arg Ser Asp Asn His Gly Gly Gly Ser Gln Thr 
        515                 520                 525             


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
    530                 535                 540                 


Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
545                 550                 555                 560 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
                565                 570                 575     


Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser 
            580                 585                 590         


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
        595                 600                 605             


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg 
    610                 615                 620                 


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
625                 630                 635                 640 


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
                645                 650                 655     


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
            660                 665                 670         


Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
        675                 680                 685             


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp 
    690                 695                 700                 


Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
705                 710                 715                 720 


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
                725                 730                 735     


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser 
            740                 745                 750         


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
        755                 760                 765             


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
    770                 775                 780                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
785                 790                 795                 800 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
                805                 810                 815     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
            820                 825                 830         


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
        835                 840                 845             


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
    850                 855                 860                 


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
865                 870                 875                 880 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His 
                885                 890                 895     


His His His His 
            900 


<210>  294
<211>  903
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro676 - aTrop2 hVIB565 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTrop2 hVIB565 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  294

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


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


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Val Tyr 
65                  70                  75                  80  


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


Ala Thr Ala Gly Asp Gly Gly Asp Tyr His Cys Ser Gly Leu Val Asp 
            100                 105                 110         


Tyr Gly Met Asp Tyr Trp Gly Lys Gly Thr Leu Val Thr Val Ser Ser 
        115                 120                 125             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    130                 135                 140                 


Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala 
145                 150                 155                 160 


Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala 
                165                 170                 175     


Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn 
            180                 185                 190         


Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile 
        195                 200                 205             


Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu 
    210                 215                 220                 


Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe 
225                 230                 235                 240 


Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu 
                245                 250                 255     


Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val 
            260                 265                 270         


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
        275                 280                 285             


Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
    290                 295                 300                 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
305                 310                 315                 320 


Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser 
                325                 330                 335     


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


Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val 
        355                 360                 365             


Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly 
    370                 375                 380                 


Gly Ser Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro 
385                 390                 395                 400 


Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asp 
                405                 410                 415     


Tyr Tyr Ala Ile Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu 
            420                 425                 430         


Gly Val Ser Cys Ile Ser Ser Ser His Gly Ser Thr Tyr Tyr Ala Asp 
        435                 440                 445             


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr 
    450                 455                 460                 


Val Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr 
465                 470                 475                 480 


Tyr Cys Ala Thr Ala Gly Asp Gly Gly Asp Tyr His Cys Ser Gly Leu 
                485                 490                 495     


Val Asp Tyr Gly Met Asp Tyr Trp Gly Lys Gly Thr Leu Val Thr Val 
            500                 505                 510         


Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly 
        515                 520                 525             


Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly 
    530                 535                 540                 


Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser 
545                 550                 555                 560 


Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg 
                565                 570                 575     


Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala 
            580                 585                 590         


Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser 
        595                 600                 605             


Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr 
    610                 615                 620                 


Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 
625                 630                 635                 640 


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
                645                 650                 655     


Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser 
            660                 665                 670         


Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro 
        675                 680                 685             


Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr 
    690                 695                 700                 


Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile 
705                 710                 715                 720 


Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu 
                725                 730                 735     


Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe 
            740                 745                 750         


Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu 
        755                 760                 765             


Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
    770                 775                 780                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu 
785                 790                 795                 800 


Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met 
                805                 810                 815     


Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser 
            820                 825                 830         


Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly 
        835                 840                 845             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln 
    850                 855                 860                 


Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile 
865                 870                 875                 880 


Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser 
                885                 890                 895     


Ser His His His His His His 
            900             


<210>  295
<211>  905
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro677 - aTrop2 hVIB557 sdAb sdAb - aCD3 Vh
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTrop2 hVIB557 sdAb sdAb - MMP9-15
       - aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  295

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Ser Gln 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg Ala Thr Ala 
            100                 105                 110         


Glu Thr Ser Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        115                 120                 125             


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
    130                 135                 140                 


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
145                 150                 155                 160 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
                165                 170                 175     


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
            180                 185                 190         


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
        195                 200                 205             


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
    210                 215                 220                 


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
225                 230                 235                 240 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
                245                 250                 255     


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
            260                 265                 270         


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
        275                 280                 285             


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
    290                 295                 300                 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
305                 310                 315                 320 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
                325                 330                 335     


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


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
        355                 360                 365             


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
    370                 375                 380                 


Gly Gly Ser Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln 
385                 390                 395                 400 


Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe 
                405                 410                 415     


Ser Ser Gln Ser Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg 
            420                 425                 430         


Glu Phe Val Ser Ala Ile Ser Trp Thr Gly Ala Asn Pro Thr Tyr Ala 
        435                 440                 445             


Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn 
    450                 455                 460                 


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val 
465                 470                 475                 480 


Tyr Tyr Cys Ala Ala Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg 
                485                 490                 495     


Ala Thr Ala Glu Thr Ser Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val 
            500                 505                 510         


Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu 
        515                 520                 525             


Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 
    530                 535                 540                 


Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val 
545                 550                 555                 560 


Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 
                565                 570                 575     


Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr 
            580                 585                 590         


Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr 
        595                 600                 605             


Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu 
    610                 615                 620                 


Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 
625                 630                 635                 640 


Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
                645                 650                 655     


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
            660                 665                 670         


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln 
        675                 680                 685             


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
    690                 695                 700                 


Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe 
705                 710                 715                 720 


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
                725                 730                 735     


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly 
            740                 745                 750         


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
        755                 760                 765             


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
    770                 775                 780                 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn 
785                 790                 795                 800 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
                805                 810                 815     


Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
            820                 825                 830         


Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val 
        835                 840                 845             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
    850                 855                 860                 


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
865                 870                 875                 880 


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
                885                 890                 895     


Val Ser Ser His His His His His His 
            900                 905 


<210>  296
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro678 - aTrop2 hVIB575 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTrop2 hVIB575 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  296

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


Ser Leu Arg Leu Ser Cys Leu Ala Ser Gly Arg Thr Val Gly Arg Thr 
            20                  25                  30          


Ala Met Gly Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ser Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr 
            100                 105                 110         


Trp Gly Lys Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly 
        115                 120                 125             


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
    130                 135                 140                 


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
145                 150                 155                 160 


Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
                165                 170                 175     


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr 
            180                 185                 190         


Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser 
        195                 200                 205             


Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr 
    210                 215                 220                 


Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile 
225                 230                 235                 240 


Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                245                 250                 255     


Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro 
            260                 265                 270         


Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser 
        275                 280                 285             


Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln 
    290                 295                 300                 


Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu 
305                 310                 315                 320 


Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                325                 330                 335     


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


Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        355                 360                 365             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln 
    370                 375                 380                 


Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg 
385                 390                 395                 400 


Leu Ser Cys Leu Ala Ser Gly Arg Thr Val Gly Arg Thr Ala Met Gly 
                405                 410                 415     


Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Val Ala Thr Ile 
            420                 425                 430         


Ser Trp Ala Gly Gly Thr Thr Tyr Tyr Ala Asp Phe Val Lys Gly Arg 
        435                 440                 445             


Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met 
    450                 455                 460                 


Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Ser 
465                 470                 475                 480 


Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr Trp Gly Lys 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  297
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro679 - aTrop2 hVIB578 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTrop2 hVIB578 sdAb - MMP9-15 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  297

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


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


Ala Met Gly Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Ala 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Val Tyr 
65                  70                  75                  80  


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


Ala Ala Ser Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr 
            100                 105                 110         


Trp Gly Lys Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly 
        115                 120                 125             


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
    130                 135                 140                 


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
145                 150                 155                 160 


Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
                165                 170                 175     


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr 
            180                 185                 190         


Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser 
        195                 200                 205             


Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr 
    210                 215                 220                 


Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile 
225                 230                 235                 240 


Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                245                 250                 255     


Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro 
            260                 265                 270         


Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser 
        275                 280                 285             


Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln 
    290                 295                 300                 


Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu 
305                 310                 315                 320 


Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                325                 330                 335     


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


Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        355                 360                 365             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln 
    370                 375                 380                 


Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg 
385                 390                 395                 400 


Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Gly Arg Ala Ala Met Gly 
                405                 410                 415     


Trp Phe Arg Gln Pro Pro Gly Lys Glu Arg Glu Phe Ala Ala Thr Ile 
            420                 425                 430         


Ser Trp Ser Gly Ser Asn Thr Tyr Tyr Ala Asp Phe Val Lys Gly Arg 
        435                 440                 445             


Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Val Tyr Leu Gln Met 
    450                 455                 460                 


Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Ser 
465                 470                 475                 480 


Glu Pro Tyr Ser Asp Tyr Asp Pro Ser Gly Met Val Tyr Trp Gly Lys 
                485                 490                 495     


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
            500                 505                 510         


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  298
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro808 - aTROP2 hVIB609 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTROP2 hVIB609 sdAb - MMP9-15 - 
       aCD3Vli -NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  298

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


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


Pro Met Ala Trp Phe Arg Gln Pro Pro Gly Gln Glu Arg Glu Phe Val 
        35                  40                  45              


Ala Asp Met Ser Trp Ser Gly Thr Asn Thr Tyr Tyr Ala Asp Ser Val 
    50                  55                  60                  


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Trp Pro Tyr Ser Gly Thr Gly Arg Ser Thr Thr Asp Tyr 
            100                 105                 110         


Thr Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        115                 120                 125             


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
    130                 135                 140                 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
145                 150                 155                 160 


Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys 
                165                 170                 175     


Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala 
            180                 185                 190         


Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
        195                 200                 205             


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
    210                 215                 220                 


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser 
225                 230                 235                 240 


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
                245                 250                 255     


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
            260                 265                 270         


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
        275                 280                 285             


Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
    290                 295                 300                 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys 
305                 310                 315                 320 


Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
                325                 330                 335     


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


Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
        355                 360                 365             


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln 
    370                 375                 380                 


Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
385                 390                 395                 400 


Leu Arg Leu Ser Cys Ala Leu Ser Gly Leu Thr Phe Asn Thr Tyr Pro 
                405                 410                 415     


Met Ala Trp Phe Arg Gln Pro Pro Gly Gln Glu Arg Glu Phe Val Ala 
            420                 425                 430         


Asp Met Ser Trp Ser Gly Thr Asn Thr Tyr Tyr Ala Asp Ser Val Lys 
        435                 440                 445             


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
    450                 455                 460                 


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala 
465                 470                 475                 480 


Ala Gly Trp Pro Tyr Ser Gly Thr Gly Arg Ser Thr Thr Asp Tyr Thr 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  299
<211>  899
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro819 - aTROP2 hVIB619 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTROP2 hVIB619 sdAb - MMP9-15 - 
       aCD3Vli -NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  299

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


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


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Glu Ser Leu Pro Tyr Glu Ser Gly Ser Pro Arg Leu Thr Asp 
            100                 105                 110         


Phe Ala Ser Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Ser Phe Ser Arg Tyr 
                405                 410                 415     


Gly Met Gly Trp Leu Arg Gln Ala Pro Gly Lys Glu Arg Glu Leu Val 
            420                 425                 430         


Ala Ser Ile Ser Trp Ser Gly His Ser Thr Tyr Tyr Ala Asp Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Glu Ser Leu Pro Tyr Glu Ser Gly Ser Pro Arg Leu Thr Asp 
                485                 490                 495     


Phe Ala Ser Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly 
            500                 505                 510         


Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val 
        515                 520                 525             


Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr 
    530                 535                 540                 


Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro 
545                 550                 555                 560 


Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 
                565                 570                 575     


Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly 
            580                 585                 590         


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
        595                 600                 605             


Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp 
    610                 615                 620                 


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
625                 630                 635                 640 


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
                645                 650                 655     


Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
            660                 665                 670         


Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
        675                 680                 685             


Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp 
    690                 695                 700                 


Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
705                 710                 715                 720 


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
                725                 730                 735     


Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr 
            740                 745                 750         


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        755                 760                 765             


Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
    770                 775                 780                 


Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys 
785                 790                 795                 800 


Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg 
                805                 810                 815     


Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser 
            820                 825                 830         


Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile 
        835                 840                 845             


Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu 
    850                 855                 860                 


Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu 
865                 870                 875                 880 


Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His 
                885                 890                 895     


His His His 
            


<210>  300
<211>  905
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro681 - aTrop2 hVIB557 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aTrop2 hVIB557 sdAb - NCL-16 - 
       aCD3Vli - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  300

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Ser Gln 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg Ala Thr Ala 
            100                 105                 110         


Glu Thr Ser Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
        115                 120                 125             


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
    130                 135                 140                 


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
145                 150                 155                 160 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
                165                 170                 175     


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
            180                 185                 190         


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
        195                 200                 205             


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
    210                 215                 220                 


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
225                 230                 235                 240 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
                245                 250                 255     


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
            260                 265                 270         


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
        275                 280                 285             


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
    290                 295                 300                 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
305                 310                 315                 320 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
                325                 330                 335     


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


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
        355                 360                 365             


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
    370                 375                 380                 


Gly Gly Ser Gln Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln 
385                 390                 395                 400 


Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe 
                405                 410                 415     


Ser Ser Gln Ser Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg 
            420                 425                 430         


Glu Phe Val Ser Ala Ile Ser Trp Thr Gly Ala Asn Pro Thr Tyr Ala 
        435                 440                 445             


Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn 
    450                 455                 460                 


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val 
465                 470                 475                 480 


Tyr Tyr Cys Ala Ala Asp Thr Ser Gly Gly Ser Tyr Tyr Tyr Glu Arg 
                485                 490                 495     


Ala Thr Ala Glu Thr Ser Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val 
            500                 505                 510         


Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly 
        515                 520                 525             


Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 
    530                 535                 540                 


Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val 
545                 550                 555                 560 


Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 
                565                 570                 575     


Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr 
            580                 585                 590         


Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr 
        595                 600                 605             


Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu 
    610                 615                 620                 


Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 
625                 630                 635                 640 


Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
                645                 650                 655     


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
            660                 665                 670         


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln 
        675                 680                 685             


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
    690                 695                 700                 


Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe 
705                 710                 715                 720 


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
                725                 730                 735     


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly 
            740                 745                 750         


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
        755                 760                 765             


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser 
    770                 775                 780                 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn 
785                 790                 795                 800 


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe 
                805                 810                 815     


Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
            820                 825                 830         


Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val 
        835                 840                 845             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr 
    850                 855                 860                 


Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 
865                 870                 875                 880 


Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr 
                885                 890                 895     


Val Ser Ser His His His His His His 
            900                 905 


<210>  301
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro621 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - CathS-16 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  301

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Ala Arg 
            500                 505                 510         


Leu Gln Ser Ala Ala Pro Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  302
<211>  892
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro622 - aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - CathS-16 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  302

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Ala Arg Leu Gln Ser Ala 
            500                 505                 510         


Ala Pro Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu 
        515                 520                 525             


Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr 
    530                 535                 540                 


Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro 
545                 550                 555                 560 


Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp 
                565                 570                 575     


Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
            580                 585                 590         


Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr 
        595                 600                 605             


Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
    610                 615                 620                 


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
625                 630                 635                 640 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
                645                 650                 655     


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp 
            660                 665                 670         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
        675                 680                 685             


Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys 
    690                 695                 700                 


Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu 
705                 710                 715                 720 


Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val 
                725                 730                 735     


Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp 
            740                 745                 750         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly 
        755                 760                 765             


Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
    770                 775                 780                 


Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 
785                 790                 795                 800 


Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 
                805                 810                 815     


Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala 
            820                 825                 830         


Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr 
        835                 840                 845             


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val 
    850                 855                 860                 


Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr 
865                 870                 875                 880 


Leu Val Thr Val Ser Ser His His His His His His 
                885                 890         


<210>  303
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro640 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9v - aCD3Vli - NCL-8 -
       aCD3Vhi - aHSA (10GE) - His6

<400>  303

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly 
            500                 505                 510         


Pro Ala Gly Met His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  304
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro641 - aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9v - aCD3Vli - NCL-8 
       - aCD3Vhi - aHSA (10GE) - His6

<400>  304

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly Pro Ala Gly Met 
            500                 505                 510         


His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
                565                 570                 575     


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
            580                 585                 590         


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
        595                 600                 605             


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
    610                 615                 620                 


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
625                 630                 635                 640 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
                645                 650                 655     


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
            660                 665                 670         


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
        675                 680                 685             


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
    690                 695                 700                 


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  305
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro642 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9v - aCD3Vli2 - NCL-8 
       - aCD3Vhi2 - aHSA (10GE) - His6

<400>  305

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly 
            500                 505                 510         


Pro Ala Gly Met His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
                565                 570                 575     


Lys Asp Asp Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  306
<211>  891
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro643 - aB7H3 hF12 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF12 sdAb - MMP9v - aCD3Vli2 - NCL-8
       - aCD3Vhi2 - aHSA (10GE) - His6

<400>  306

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


Ser Leu Arg Leu Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr 
            20                  25                  30          


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


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp 
            100                 105                 110         


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
        115                 120                 125             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    130                 135                 140                 


Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 
145                 150                 155                 160 


Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                165                 170                 175     


Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 
            180                 185                 190         


Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
        195                 200                 205             


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
    210                 215                 220                 


Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser 
225                 230                 235                 240 


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
                245                 250                 255     


Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            260                 265                 270         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser 
        275                 280                 285             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    290                 295                 300                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val 
305                 310                 315                 320 


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
                325                 330                 335     


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


Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
        355                 360                 365             


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu 
    370                 375                 380                 


Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 
385                 390                 395                 400 


Ser Cys Glu Ala Ser Pro Arg Thr Phe Ser Thr Tyr Ser Met Ala Trp 
                405                 410                 415     


Phe Arg Gln Ala Pro Gly Lys Glu Arg Ser Phe Val Ala Ala Ile Asn 
            420                 425                 430         


Trp Ser Gly Gly Asn Thr Ser Tyr Ala Asp Ser Val Lys Gly Arg Phe 
        435                 440                 445             


Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn 
    450                 455                 460                 


Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala Gly Gly 
465                 470                 475                 480 


Val Leu Ala His His Asn Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr 
                485                 490                 495     


Leu Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly Pro Ala Gly Met 
            500                 505                 510         


His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
        515                 520                 525             


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
    530                 535                 540                 


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
545                 550                 555                 560 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp Asp Ala 
                565                 570                 575     


Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 
            580                 585                 590         


Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr 
        595                 600                 605             


Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys 
    610                 615                 620                 


Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
625                 630                 635                 640 


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
                645                 650                 655     


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met Asn Trp 
            660                 665                 670         


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg 
        675                 680                 685             


Ser Lys Tyr Asn Asn Tyr Ala Thr Ala Tyr Ala Asp Ser Val Lys Asp 
    690                 695                 700                 


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
705                 710                 715                 720 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
                725                 730                 735     


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
            740                 745                 750         


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
        755                 760                 765             


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
    770                 775                 780                 


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
785                 790                 795                 800 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
                805                 810                 815     


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
            820                 825                 830         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
        835                 840                 845             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
    850                 855                 860                 


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
865                 870                 875                 880 


Val Thr Val Ser Ser His His His His His His 
                885                 890     


<210>  307
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro744  - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9-15 (K->E) - aCD3Vli 
       -NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  307

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Glu Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  308
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro746  - haB7H3 F7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - haB7H3 F7 sdAb - MMP9-15 (M->P) - aCD3Vli 
       -NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  308

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Pro Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  309
<211>  877
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro638 - aFOLR1 h77-2 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aFOLR1 h77-2 sdAb - MMP9v - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  309

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
        115                 120                 125             


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
    130                 135                 140                 


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg 
145                 150                 155                 160 


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


Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe 
            180                 185                 190         


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
        195                 200                 205             


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala 
    210                 215                 220                 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
            260                 265                 270         


Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
        275                 280                 285             


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
    290                 295                 300                 


Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser 
305                 310                 315                 320 


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
                325                 330                 335     


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg 
            340                 345                 350         


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    370                 375                 380                 


Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
385                 390                 395                 400 


Val Ser Asn Ser Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu 
                405                 410                 415     


Arg Glu Phe Val Ala Ile Ile Asn Ser Ile Gly Ile Thr Asn Tyr Ala 
            420                 425                 430         


Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn 
        435                 440                 445             


Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val 
    450                 455                 460                 


Tyr Val Cys Asn Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr 
465                 470                 475                 480 


Leu Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly Pro Ala Gly Met 
                485                 490                 495     


His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            500                 505                 510         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
        515                 520                 525             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    530                 535                 540                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
545                 550                 555                 560 


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                565                 570                 575     


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
            580                 585                 590         


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        595                 600                 605             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
    610                 615                 620                 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
625                 630                 635                 640 


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
                645                 650                 655     


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
            660                 665                 670         


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
        675                 680                 685             


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
    690                 695                 700                 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
705                 710                 715                 720 


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
                725                 730                 735     


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
            740                 745                 750         


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
        755                 760                 765             


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
    770                 775                 780                 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
785                 790                 795                 800 


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
                805                 810                 815     


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
            820                 825                 830         


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
        835                 840                 845             


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
    850                 855                 860                 


Thr Leu Val Thr Val Ser Ser His His His His His His 
865                 870                 875         


<210>  310
<211>  875
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro639  - aFOLR1 h59.3 sdAb - aCD3 Vh (2B2)
       - NCL-8 - aCD3Vl (2B2) - aFOLR1 h59.3 sdAb - MMP9v - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  310

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


Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser 
            20                  25                  30          


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


Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys 
                85                  90                  95      


His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
            100                 105                 110         


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
        115                 120                 125             


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
    130                 135                 140                 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
145                 150                 155                 160 


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
                165                 170                 175     


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
        195                 200                 205             


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
    210                 215                 220                 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
225                 230                 235                 240 


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
                245                 250                 255     


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
            260                 265                 270         


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
        275                 280                 285             


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
    290                 295                 300                 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
305                 310                 315                 320 


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
                325                 330                 335     


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
            340                 345                 350         


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln 
    370                 375                 380                 


Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe 
385                 390                 395                 400 


Ser Ile Ser Ala Met Gly Trp Tyr Arg Gln Ala Pro Gly Lys Gln Arg 
                405                 410                 415     


Glu Trp Val Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp 
            420                 425                 430         


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr 
        435                 440                 445             


Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr 
    450                 455                 460                 


Tyr Cys Lys His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val 
465                 470                 475                 480 


Thr Val Ser Ser Gly Ser Gly Gly Pro Gly Pro Ala Gly Met His Gly 
                485                 490                 495     


Leu Pro Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr 
            500                 505                 510         


Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly 
        515                 520                 525             


Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly 
    530                 535                 540                 


Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys 
545                 550                 555                 560 


Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 
                565                 570                 575     


Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 
            580                 585                 590         


Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu 
        595                 600                 605             


Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
    610                 615                 620                 


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
625                 630                 635                 640 


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn Trp Val 
                645                 650                 655     


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 
            660                 665                 670         


Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val Lys Asp 
        675                 680                 685             


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
    690                 695                 700                 


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
705                 710                 715                 720 


His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
                725                 730                 735     


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly Gly 
            740                 745                 750         


Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro 
        755                 760                 765             


Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser 
    770                 775                 780                 


Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 
785                 790                 795                 800 


Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu 
                805                 810                 815     


Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr 
            820                 825                 830         


Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr 
        835                 840                 845             


Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly Thr Leu 
    850                 855                 860                 


Val Thr Val Ser Ser His His His His His His 
865                 870                 875 


<210>  311
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro396 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - MMP9v-16 - aCD3Vli - NCL-8 - 
       aCD3Vhi - aHSA (10GE) - His6

<400>  311

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Ser Gly Gly Pro Gly 
            500                 505                 510         


Pro Ala Gly Met His Gly Leu Pro Gly Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  312
<211>  893
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro476 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli2 - NCL-8 - 
       aCD3Vhi2 - aHSA (10GE) - His6

<400>  312

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Asp 
                565                 570                 575     


Asp Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
            580                 585                 590         


Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu 
        595                 600                 605             


Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
    610                 615                 620                 


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
625                 630                 635                 640 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
                645                 650                 655     


Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys His Ala Met 
            660                 665                 670         


Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 
        675                 680                 685             


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


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
705                 710                 715                 720 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
                725                 730                 735     


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
            740                 745                 750         


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
        755                 760                 765             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    770                 775                 780                 


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
785                 790                 795                 800 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
                805                 810                 815     


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
            820                 825                 830         


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        835                 840                 845             


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
    850                 855                 860                 


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
865                 870                 875                 880 


Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890             


<210>  313
<211>  896
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro706 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - uPA - aCD3Vli - NCL-8 - aCD3Vhi - 
       aHSA (10GE) - His6

<400>  313

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser His Thr 
            500                 505                 510         


Gly Arg Ser Ala Tyr Phe Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
        515                 520                 525             


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
    530                 535                 540                 


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
545                 550                 555                 560 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
                565                 570                 575     


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
            580                 585                 590         


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
        595                 600                 605             


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
    610                 615                 620                 


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
625                 630                 635                 640 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
                645                 650                 655     


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
            660                 665                 670         


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
        675                 680                 685             


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
    690                 695                 700                 


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
705                 710                 715                 720 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
                725                 730                 735     


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
            740                 745                 750         


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        755                 760                 765             


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
    770                 775                 780                 


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
785                 790                 795                 800 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
                805                 810                 815     


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
            820                 825                 830         


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
        835                 840                 845             


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
    850                 855                 860                 


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
865                 870                 875                 880 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895     


<210>  314
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro709 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli - NCL-8 - aCD3Vhi
       - aHSA (10GE) - His6

<400>  314

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  315
<211>  885
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro470 - aFOLR1 h77.2 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli - NCL-8 -
       aCD3Vhi - aHSA (10GE) - His6

<400>  315

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


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


Val Met Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Arg Asn Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            100                 105                 110         


Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu 
        115                 120                 125             


Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys 
    130                 135                 140                 


Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg 
145                 150                 155                 160 


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


Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe 
            180                 185                 190         


Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 
        195                 200                 205             


Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala 
    210                 215                 220                 


Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly 
225                 230                 235                 240 


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln 
                245                 250                 255     


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
            260                 265                 270         


Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
        275                 280                 285             


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
    290                 295                 300                 


Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser 
305                 310                 315                 320 


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
                325                 330                 335     


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg 
            340                 345                 350         


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
        355                 360                 365             


Gly Gly Gly Ser Gln Val Lys Leu Val Glu Ser Gly Gly Gly Val Val 
    370                 375                 380                 


Arg Pro Gly Gly Ser Leu Thr Leu Ser Cys Ala Ala Ser Gly Arg Thr 
385                 390                 395                 400 


Ser Arg Ser Tyr Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu 
                405                 410                 415     


Arg Glu Phe Val Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr 
            420                 425                 430         


Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        435                 440                 445             


Asn Ser Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala 
    450                 455                 460                 


Leu Tyr Tyr Cys Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu 
465                 470                 475                 480 


Tyr Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                485                 490                 495     


Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln 
            500                 505                 510         


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
        515                 520                 525             


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
    530                 535                 540                 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
545                 550                 555                 560 


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
                565                 570                 575     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            580                 585                 590         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
        595                 600                 605             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    610                 615                 620                 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
625                 630                 635                 640 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
                645                 650                 655     


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
            660                 665                 670         


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


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
    690                 695                 700                 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
705                 710                 715                 720 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
                725                 730                 735     


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        755                 760                 765             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
    770                 775                 780                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
785                 790                 795                 800 


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
                805                 810                 815     


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
            820                 825                 830         


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
        835                 840                 845             


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
    850                 855                 860                 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
865                 870                 875                 880 


His His His His His 
                885 


<210>  316
<211>  885
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro471  - aEGFR sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aFOLR1 h77.2 sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  316

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Val Ser Asn Ser Val Met 
                405                 410                 415     


Ala Trp Tyr Arg Gln Thr Pro Gly Asn Glu Arg Glu Phe Val Ala Ile 
            420                 425                 430         


Ile Asn Ser Ile Gly Ile Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg 
        435                 440                 445             


Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met 
    450                 455                 460                 


Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Val Cys Asn Arg Asn 
465                 470                 475                 480 


Phe Asp Arg Ile Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                485                 490                 495     


Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln 
            500                 505                 510         


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
        515                 520                 525             


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
    530                 535                 540                 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
545                 550                 555                 560 


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
                565                 570                 575     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            580                 585                 590         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
        595                 600                 605             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    610                 615                 620                 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
625                 630                 635                 640 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
                645                 650                 655     


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
            660                 665                 670         


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


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
    690                 695                 700                 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
705                 710                 715                 720 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
                725                 730                 735     


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        755                 760                 765             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
    770                 775                 780                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
785                 790                 795                 800 


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
                805                 810                 815     


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
            820                 825                 830         


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
        835                 840                 845             


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
    850                 855                 860                 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
865                 870                 875                 880 


His His His His His 
                885 


<210>  317
<211>  884
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro551 - EGFR sdAb - aCD3 Vh (2B2) - NCL-8 
       - aCD3Vl (2B2) - aFOLR1 h59.3 sdAb - MMP9-16 - aCD3Vli - NCL-8 - 
       aCD3Vhi - aHSA (10GE) - His6

<400>  317

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser Ala Met 
                405                 410                 415     


Gly Trp Tyr Arg Gln Ala Pro Gly Lys Gln Arg Glu Trp Val Ala Val 
            420                 425                 430         


Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg 
        435                 440                 445             


Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met 
    450                 455                 460                 


Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys His Tyr 
465                 470                 475                 480 


Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser 
                485                 490                 495     


Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr 
            500                 505                 510         


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
        515                 520                 525             


Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
    530                 535                 540                 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
545                 550                 555                 560 


Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser 
                565                 570                 575     


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
            580                 585                 590         


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg 
        595                 600                 605             


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
    610                 615                 620                 


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
625                 630                 635                 640 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
                645                 650                 655     


Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
            660                 665                 670         


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp 
        675                 680                 685             


Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
    690                 695                 700                 


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
705                 710                 715                 720 


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser 
                725                 730                 735     


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            740                 745                 750         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
        755                 760                 765             


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
    770                 775                 780                 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
785                 790                 795                 800 


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
                805                 810                 815     


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
            820                 825                 830         


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
        835                 840                 845             


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
    850                 855                 860                 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His 
865                 870                 875                 880 


His His His His 
                


<210>  318
<211>  884
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro552 - aFOLR1 h59.3 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - EGFR sdAb - MMP9-15 - aCD3Vli - NCL-8 - 
       aCD3Vhi - aHSA (10GE) - His6

<400>  318

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


Ser Leu Arg Leu Ser Cys Ala Ala Pro Gly Asn Thr Phe Ser Ile Ser 
            20                  25                  30          


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


Ala Val Thr His Ser Asp Tyr Ser Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Lys 
                85                  90                  95      


His Tyr Gly Ile Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
            100                 105                 110         


Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser 
        115                 120                 125             


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala 
    130                 135                 140                 


Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln 
145                 150                 155                 160 


Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr 
                165                 170                 175     


Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr 
            180                 185                 190         


Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn 
        195                 200                 205             


Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn 
    210                 215                 220                 


Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr 
225                 230                 235                 240 


Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr 
                245                 250                 255     


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
            260                 265                 270         


Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
        275                 280                 285             


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
    290                 295                 300                 


Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly 
305                 310                 315                 320 


Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro 
                325                 330                 335     


Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp 
            340                 345                 350         


Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly 
        355                 360                 365             


Gly Gly Ser Gln Val Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln 
    370                 375                 380                 


Thr Gly Gly Ser Leu Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser 
385                 390                 395                 400 


Arg Ser Tyr Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg 
                405                 410                 415     


Glu Phe Val Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala 
            420                 425                 430         


Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn 
        435                 440                 445             


Thr Val Asp Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile 
    450                 455                 460                 


Tyr Tyr Cys Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr 
465                 470                 475                 480 


Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser 
                485                 490                 495     


Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr 
            500                 505                 510         


Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val 
        515                 520                 525             


Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr 
    530                 535                 540                 


Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 
545                 550                 555                 560 


Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser 
                565                 570                 575     


Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln 
            580                 585                 590         


Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg 
        595                 600                 605             


Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser 
    610                 615                 620                 


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
625                 630                 635                 640 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
                645                 650                 655     


Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
            660                 665                 670         


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp 
        675                 680                 685             


Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp 
    690                 695                 700                 


Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 
705                 710                 715                 720 


Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser 
                725                 730                 735     


Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 
            740                 745                 750         


Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
        755                 760                 765             


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser 
    770                 775                 780                 


Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val 
785                 790                 795                 800 


Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly 
                805                 810                 815     


Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr 
            820                 825                 830         


Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser 
        835                 840                 845             


Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser 
    850                 855                 860                 


Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His 
865                 870                 875                 880 


His His His His 
                


<210>  319
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro623 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - MMP9-15 - aCD3Vli - NCL-8
       - aCD3Vhi - aHSA (10GE) - His6

<400>  319

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr Asp Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val Ala Ala 
            420                 425                 430         


Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  320
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro624 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - acEpCAM hVIB665 sdAb - MMP9-15 - aCD3Vli - NCL-8
       - aCD3Vhi - aHSA (10GE) - His6

<400>  320

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Asp Tyr Asp Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val Ala Ala 
            420                 425                 430         


Ile Ser Trp Ser Gly Gly His Thr Asn Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  321
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro698 - acEpCAM hVIB665 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  321

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Lys Leu Val Glu Ser Gly Gly Gly Val Val Arg Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Thr Leu Ser Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr 
                405                 410                 415     


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ser Gly Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  322
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro655 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB664 sdAb - MMP9-15 - aCD3Vli -
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  322

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Leu Asp Asn Tyr Asp Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val Ala Ala 
            420                 425                 430         


Ile Ser Trp Ser Gly Gly Ser Thr Asp Tyr Ala Tyr Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  323
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro656 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - acEpCAM hVIB665 sdAb - MMP9-15 - aCD3Vli -
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  323

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Ala Ser Gly Arg Thr Phe Ser Asp Tyr Asp Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val Ala Ala 
            420                 425                 430         


Ile Ser Trp Ser Gly Gly His Thr Asn Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  324
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro657 - acEpCAM hVIB664 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - haB7H3 F7 sdAb - MMP9-15 - aCD3Vli
       - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  324

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Met Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
                405                 410                 415     


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Val Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  325
<211>  897
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro658 - acEpCAM hVIB665 sdAb - aCD3 Vh 
       (2B2) - NCL-8 - aCD3Vl (2B2) - haB7H3 F7 sdAb - MMP9-15 - aCD3Vli
       - NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  325

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


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


Asp Met Gly Trp Phe Arg Gln Gly Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Asp Leu Arg Phe Thr Gly Gly Asp Thr Thr Thr Pro Glu Thr 
            100                 105                 110         


Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
        115                 120                 125             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    130                 135                 140                 


Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 
145                 150                 155                 160 


Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly 
                165                 170                 175     


Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 
            180                 185                 190         


Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg 
        195                 200                 205             


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
    210                 215                 220                 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn 
225                 230                 235                 240 


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
                245                 250                 255     


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr 
            260                 265                 270         


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
        275                 280                 285             


Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
    290                 295                 300                 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 
305                 310                 315                 320 


Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                325                 330                 335     


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


Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        355                 360                 365             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    370                 375                 380                 


Gln Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
385                 390                 395                 400 


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
                405                 410                 415     


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
            420                 425                 430         


Ala Val Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val 
        435                 440                 445             


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
    450                 455                 460                 


Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 
465                 470                 475                 480 


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
                485                 490                 495     


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro 
            500                 505                 510         


Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr 
        515                 520                 525             


Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 
    530                 535                 540                 


Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp 
545                 550                 555                 560 


Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr 
                565                 570                 575     


Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu 
            580                 585                 590         


Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp 
        595                 600                 605             


Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe 
    610                 615                 620                 


Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly 
625                 630                 635                 640 


Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly 
                645                 650                 655     


Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys 
            660                 665                 670         


Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp 
        675                 680                 685             


Val Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys 
    690                 695                 700                 


Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 
705                 710                 715                 720 


Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 
                725                 730                 735     


Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser 
            740                 745                 750         


Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 
        755                 760                 765             


Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly 
    770                 775                 780                 


Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala 
785                 790                 795                 800 


Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala 
                805                 810                 815     


Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg 
            820                 825                 830         


Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        835                 840                 845             


Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro 
    850                 855                 860                 


Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val 
865                 870                 875                 880 


Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His 
                885                 890                 895     


His 
    


<210>  326
<211>  885
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro516 - aCA9 hVIB456 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aCA9 hVIB456 sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  326

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ser Ala Leu Ile Ile Asn 
            20                  25                  30          


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


Ala Thr Val Thr Arg Ser Gly Arg Thr Asn Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Val Ala Leu Trp Ile Ala Asp Gly Glu Tyr Asp Tyr Trp Gly Gln Gly 
            100                 105                 110         


Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu 
        115                 120                 125             


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
    130                 135                 140                 


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
145                 150                 155                 160 


Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
                165                 170                 175     


Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln 
            180                 185                 190         


Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala 
        195                 200                 205             


Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr 
    210                 215                 220                 


Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala 
225                 230                 235                 240 


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
                245                 250                 255     


Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val 
            260                 265                 270         


Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala 
        275                 280                 285             


Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln 
    290                 295                 300                 


Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr 
305                 310                 315                 320 


Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr 
                325                 330                 335     


Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu 
            340                 345                 350         


Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 
        355                 360                 365             


Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser 
    370                 375                 380                 


Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala 
385                 390                 395                 400 


Ala Ser Gly Ser Ala Leu Ile Ile Asn Ala Met Gly Trp Tyr Arg Gln 
                405                 410                 415     


Ala Pro Gly Lys Gln Arg Glu Leu Val Ala Thr Val Thr Arg Ser Gly 
            420                 425                 430         


Arg Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg 
        435                 440                 445             


Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala 
    450                 455                 460                 


Glu Asp Thr Ala Val Tyr Tyr Cys Asn Val Ala Leu Trp Ile Ala Asp 
465                 470                 475                 480 


Gly Glu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 
                485                 490                 495     


Ser Gly Gly Pro Gly Pro Ala Gly Met Lys Gly Leu Pro Gly Ser Gln 
            500                 505                 510         


Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr 
        515                 520                 525             


Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn 
    530                 535                 540                 


Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu 
545                 550                 555                 560 


Ile Gly Asp Tyr Lys Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe 
                565                 570                 575     


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
            580                 585                 590         


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn 
        595                 600                 605             


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
    610                 615                 620                 


Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
625                 630                 635                 640 


Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe 
                645                 650                 655     


Thr Phe Asn Lys Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys 
            660                 665                 670         


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


Asp Asp Asp Lys Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 
    690                 695                 700                 


Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr 
705                 710                 715                 720 


Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn 
                725                 730                 735     


Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            740                 745                 750         


Val Ser Ser Gly Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        755                 760                 765             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu 
    770                 775                 780                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp 
785                 790                 795                 800 


Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser 
                805                 810                 815     


Gly Ser Gly Arg Asp Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe 
            820                 825                 830         


Thr Ile Ser Arg Asp Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn 
        835                 840                 845             


Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly 
    850                 855                 860                 


Ser Leu Ser Val Ser Ser Gln Gly Thr Leu Val Thr Val Ser Ser His 
865                 870                 875                 880 


His His His His His 
                885 


<210>  327
<211>  879
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro517 - aCA9 hVIB476 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aCA9 hVIB476 sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  327

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Asn Ile Phe Ile Ile Asn 
            20                  25                  30          


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


Ala Thr Ile Thr Asn Gly Gly Arg Thr His Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Ala Asn His Ile Glu Leu Gly Asp Tyr Trp Gly Gln Gly Thr Leu Val 
            100                 105                 110         


Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        115                 120                 125             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
    130                 135                 140                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp 
145                 150                 155                 160 


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


Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp 
            180                 185                 190         


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
        195                 200                 205             


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
    210                 215                 220                 


His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
225                 230                 235                 240 


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly 
                245                 250                 255     


Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly 
            260                 265                 270         


Gly Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser 
        275                 280                 285             


Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg 
    290                 295                 300                 


Gly Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg 
305                 310                 315                 320 


Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly 
                325                 330                 335     


Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser 
            340                 345                 350         


Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly 
    370                 375                 380                 


Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
385                 390                 395                 400 


Asn Ile Phe Ile Ile Asn Val Met Gly Trp Tyr Arg Gln Ala Pro Gly 
                405                 410                 415     


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


Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser 
        435                 440                 445             


Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr 
    450                 455                 460                 


Ala Val Tyr Tyr Cys Asn Ala Asn His Ile Glu Leu Gly Asp Tyr Trp 
465                 470                 475                 480 


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
                485                 490                 495     


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
            500                 505                 510         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
        515                 520                 525             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    530                 535                 540                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
545                 550                 555                 560 


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
                565                 570                 575     


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
            580                 585                 590         


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
        595                 600                 605             


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
    610                 615                 620                 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
625                 630                 635                 640 


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
                645                 650                 655     


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
            660                 665                 670         


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
        675                 680                 685             


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
    690                 695                 700                 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
705                 710                 715                 720 


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
                725                 730                 735     


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
            740                 745                 750         


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
        755                 760                 765             


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
    770                 775                 780                 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
785                 790                 795                 800 


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
                805                 810                 815     


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
            820                 825                 830         


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
        835                 840                 845             


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
    850                 855                 860                 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
865                 870                 875                 


<210>  328
<211>  877
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro518 - aCA9 hVIB407 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aCA9 hVIB407 sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  328

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


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


Asp Met Gly Trp Tyr Arg Gln Thr Pro Gly Lys Gln Arg Glu Phe Val 
        35                  40                  45              


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Gly Val Tyr Tyr Cys Asn 
                85                  90                  95      


Ala Ala Trp Ile Gly Asp Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
        115                 120                 125             


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
    130                 135                 140                 


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val 
145                 150                 155                 160 


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


Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg 
            180                 185                 190         


Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met 
        195                 200                 205             


Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 
    210                 215                 220                 


Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln 
225                 230                 235                 240 


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
            260                 265                 270         


Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly 
        275                 280                 285             


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
    290                 295                 300                 


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
305                 310                 315                 320 


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
                325                 330                 335     


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
            340                 345                 350         


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
    370                 375                 380                 


Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Thr Ala Ser Gly Ile 
385                 390                 395                 400 


Ile Phe Ser Val Tyr Asp Met Gly Trp Tyr Arg Gln Thr Pro Gly Lys 
                405                 410                 415     


Gln Arg Glu Phe Val Ala Arg Ile Thr Ala Gly Gly Gly Thr Tyr Leu 
            420                 425                 430         


Thr Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys 
        435                 440                 445             


Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Gly 
    450                 455                 460                 


Val Tyr Tyr Cys Asn Ala Ala Trp Ile Gly Asp Asp Tyr Trp Gly Gln 
465                 470                 475                 480 


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
                485                 490                 495     


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            500                 505                 510         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
        515                 520                 525             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    530                 535                 540                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
545                 550                 555                 560 


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                565                 570                 575     


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
            580                 585                 590         


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        595                 600                 605             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
    610                 615                 620                 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
625                 630                 635                 640 


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
                645                 650                 655     


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
            660                 665                 670         


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
        675                 680                 685             


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
    690                 695                 700                 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
705                 710                 715                 720 


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
                725                 730                 735     


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
            740                 745                 750         


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
        755                 760                 765             


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
    770                 775                 780                 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
785                 790                 795                 800 


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
                805                 810                 815     


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
            820                 825                 830         


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
        835                 840                 845             


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
    850                 855                 860                 


Thr Leu Val Thr Val Ser Ser His His His His His His 
865                 870                 875         


<210>  329
<211>  877
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro519 - aCA9 hVIB445 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aCA9 hVIB445 sdAb - MMP9-15 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  329

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ile Thr Phe Asn Leu His 
            20                  25                  30          


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


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


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr Leu 
65                  70                  75                  80  


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


Thr Asp Leu Val Gly Glu Asp Tyr Trp Gly Arg Gly Thr Leu Val Thr 
            100                 105                 110         


Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val 
        115                 120                 125             


Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 
    130                 135                 140                 


Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp Val 
145                 150                 155                 160 


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


Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp Arg 
            180                 185                 190         


Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met 
        195                 200                 205             


Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 
    210                 215                 220                 


Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly Gln 
225                 230                 235                 240 


Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser 
                245                 250                 255     


Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 
            260                 265                 270         


Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser Gly 
        275                 280                 285             


Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 
    290                 295                 300                 


Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg Phe 
305                 310                 315                 320 


Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 
                325                 330                 335     


Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn 
            340                 345                 350         


Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly 
        355                 360                 365             


Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu 
    370                 375                 380                 


Val Lys Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ile 
385                 390                 395                 400 


Thr Phe Asn Leu His Ala Met Arg Trp Tyr Arg Arg Ala Pro Gly Lys 
                405                 410                 415     


Gln Arg Glu Leu Val Ala Tyr Ile Ser Ala Arg Asp Trp Thr Asn Tyr 
            420                 425                 430         


Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
        435                 440                 445             


Asn Ser Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala 
    450                 455                 460                 


Val Tyr Tyr Cys Asn Thr Asp Leu Val Gly Glu Asp Tyr Trp Gly Arg 
465                 470                 475                 480 


Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro Ala Gly 
                485                 490                 495     


Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu Pro Ser 
            500                 505                 510         


Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly Ser Ser 
        515                 520                 525             


Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys 
    530                 535                 540                 


Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp Asp Asp 
545                 550                 555                 560 


Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys 
                565                 570                 575     


Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr 
            580                 585                 590         


Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly Thr 
        595                 600                 605             


Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln 
    610                 615                 620                 


Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys 
625                 630                 635                 640 


Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Met Asn 
                645                 650                 655     


Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile 
            660                 665                 670         


Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp Ser Val 
        675                 680                 685             


Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 
    690                 695                 700                 


Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 
705                 710                 715                 720 


Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr 
                725                 730                 735     


Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser 
            740                 745                 750         


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
        755                 760                 765             


Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr 
    770                 775                 780                 


Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly 
785                 790                 795                 800 


Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr Leu Tyr 
                805                 810                 815     


Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys 
            820                 825                 830         


Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp Thr Ala 
        835                 840                 845             


Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser Gln Gly 
    850                 855                 860                 


Thr Leu Val Thr Val Ser Ser His His His His His His 
865                 870                 875         


<210>  330
<211>  880
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro513 - aCA9 hVIB476 sdAb - aCD3 Vh (2B2) 
       - NCL-8 - aCD3Vl (2B2) - aCA9 hVIB476 sdAb - NCL-16 - aCD3Vli - 
       NCL-8 - aCD3Vhi - aHSA (10GE) - His6

<400>  330

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


Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Asn Ile Phe Ile Ile Asn 
            20                  25                  30          


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


Ala Thr Ile Thr Asn Gly Gly Arg Thr His Tyr Ala Asp Ser Val Lys 
    50                  55                  60                  


Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu 
65                  70                  75                  80  


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


Ala Asn His Ile Glu Leu Gly Asp Tyr Trp Gly Gln Gly Thr Leu Val 
            100                 105                 110         


Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu 
        115                 120                 125             


Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu 
    130                 135                 140                 


Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala Ile Asn Trp 
145                 150                 155                 160 


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


Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Gln Val Lys Asp 
            180                 185                 190         


Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 
        195                 200                 205             


Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 
    210                 215                 220                 


His Ala Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp Ala Tyr Trp Gly 
225                 230                 235                 240 


Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly Gly 
                245                 250                 255     


Ser Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly 
            260                 265                 270         


Gly Thr Val Thr Leu Thr Cys Ala Ser Ser Thr Gly Ala Val Thr Ser 
        275                 280                 285             


Gly Asn Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg 
    290                 295                 300                 


Gly Leu Ile Gly Gly Thr Lys Phe Leu Val Pro Gly Thr Pro Ala Arg 
305                 310                 315                 320 


Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly 
                325                 330                 335     


Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Thr Leu Trp Tyr Ser 
            340                 345                 350         


Asn Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gly 
        355                 360                 365             


Gly Ser Gly Gly Gly Ser Gln Val Gln Leu Val Glu Ser Gly Gly Gly 
    370                 375                 380                 


Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
385                 390                 395                 400 


Asn Ile Phe Ile Ile Asn Val Met Gly Trp Tyr Arg Gln Ala Pro Gly 
                405                 410                 415     


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


Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser 
        435                 440                 445             


Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr 
    450                 455                 460                 


Ala Val Tyr Tyr Cys Asn Ala Asn His Ile Glu Leu Gly Asp Tyr Trp 
465                 470                 475                 480 


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser Gly Gly 
                485                 490                 495     


Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln 
            500                 505                 510         


Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys 
        515                 520                 525             


Gly Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val 
    530                 535                 540                 


Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys 
545                 550                 555                 560 


Asp Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 
                565                 570                 575     


Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 
            580                 585                 590         


Ala Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly 
        595                 600                 605             


Gly Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser 
    610                 615                 620                 


Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 
625                 630                 635                 640 


Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 
                645                 650                 655     


Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 
            660                 665                 670         


Ala Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala 
        675                 680                 685             


Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn 
    690                 695                 700                 


Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val 
705                 710                 715                 720 


Tyr Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr 
                725                 730                 735     


Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 
            740                 745                 750         


Gly Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly 
        755                 760                 765             


Gly Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser 
    770                 775                 780                 


Gly Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro 
785                 790                 795                 800 


Gly Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp 
                805                 810                 815     


Thr Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp 
            820                 825                 830         


Asn Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu 
        835                 840                 845             


Asp Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser 
    850                 855                 860                 


Ser Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
865                 870                 875                 880 


<210>  331
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro186 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli -NCL-8 - aCD3Vhi 
       - aHSA (10GE) - His6

<400>  331

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  332
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro214 - aEGFR sdAb - aCD3 Vh (2B2) - NCL-8
       - aCD3Vl (2B2) - aEGFR sdAb - NCL-15 - aCD3Vli - NCL-8 - aCD3Vhi 
       - aHSA (10GE) - His6

<400>  332

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  333
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro225 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - MMP9-15 - aCD3Vli -NCL-8 
       - aCD3Vhi - aHSA (10GE) - His6

<400>  333

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  334
<211>  895
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro295 - aB7H3 hF7 sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aB7H3 hF7 sdAb - NCL-15 - aCD3Vli - NCL-8 
       - aCD3Vhi - aHSA (10GE) - His6

<400>  334

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


Ser Leu Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr 
            20                  25                  30          


His Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 
65                  70                  75                  80  


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


Ala Ala Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Ser Cys Ala Pro Ser Arg Arg Thr Phe His Thr Tyr His Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ala Val 
            420                 425                 430         


Ile Asn Trp Ser Gly Gly Ser Thr Val Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Gly Gly Ala Thr Thr Gln Arg Ala Thr Glu Ala Ser Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Gly 
            500                 505                 510         


Gly Gly Gly Ser Gly Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly 
    770                 775                 780                 


Leu Val Gln Pro Gly Asn Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly 
785                 790                 795                 800 


Phe Thr Phe Ser Lys Phe Gly Met Ser Trp Val Arg Gln Ala Pro Gly 
                805                 810                 815     


Lys Gly Leu Glu Trp Val Ser Ser Ile Ser Gly Ser Gly Arg Asp Thr 
            820                 825                 830         


Leu Tyr Ala Glu Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn 
        835                 840                 845             


Ala Lys Thr Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Pro Glu Asp 
    850                 855                 860                 


Thr Ala Val Tyr Tyr Cys Thr Ile Gly Gly Ser Leu Ser Val Ser Ser 
865                 870                 875                 880 


Gln Gly Thr Leu Val Thr Val Ser Ser His His His His His His 
                885                 890                 895 


<210>  335
<211>  1359
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic construct - Pro 817 - aEGFR sdAb - aCD3 Vh (2B2) - 
       NCL-8 - aCD3Vl (2B2) - aEGFR sdAb - MMP9-15 - aCD3Vli -NCL-8 - 
       aCD3Vhi - HAS

<400>  335

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


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


Gly Met Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val 
        35                  40                  45              


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


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


Leu Gln Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys 
                85                  90                  95      


Ala Ala Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp 
            100                 105                 110         


Tyr Trp Gly Gln Gly Thr Gln Val Thr Val Ser Ser Gly Gly Gly Ser 
        115                 120                 125             


Gly Gly Gly Ser Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val 
    130                 135                 140                 


Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr 
145                 150                 155                 160 


Phe Asn Lys Tyr Ala Ile Asn Trp Val Arg Gln Ala Pro Gly Lys Gly 
                165                 170                 175     


Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr 
            180                 185                 190         


Tyr Tyr Ala Asp Gln Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 
        195                 200                 205             


Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp 
    210                 215                 220                 


Thr Ala Val Tyr Tyr Cys Val Arg His Ala Asn Phe Gly Asn Ser Tyr 
225                 230                 235                 240 


Ile Ser Tyr Trp Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 
                245                 250                 255     


Ser Gly Gly Gly Ser Gly Gly Gly Ser Gln Thr Val Val Thr Gln Glu 
            260                 265                 270         


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Ala 
        275                 280                 285             


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
    290                 295                 300                 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Lys Phe 
305                 310                 315                 320 


Leu Val Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly 
                325                 330                 335     


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


Tyr Tyr Cys Thr Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly Gly 
        355                 360                 365             


Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Gln Val 
    370                 375                 380                 


Lys Leu Glu Glu Ser Gly Gly Gly Ser Val Gln Thr Gly Gly Ser Leu 
385                 390                 395                 400 


Arg Leu Thr Cys Ala Ala Ser Gly Arg Thr Ser Arg Ser Tyr Gly Met 
                405                 410                 415     


Gly Trp Phe Arg Gln Ala Pro Gly Lys Glu Arg Glu Phe Val Ser Gly 
            420                 425                 430         


Ile Ser Trp Arg Gly Asp Ser Thr Gly Tyr Ala Asp Ser Val Lys Gly 
        435                 440                 445             


Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Val Asp Leu Gln 
    450                 455                 460                 


Met Asn Ser Leu Lys Pro Glu Asp Thr Ala Ile Tyr Tyr Cys Ala Ala 
465                 470                 475                 480 


Ala Ala Gly Ser Ala Trp Tyr Gly Thr Leu Tyr Glu Tyr Asp Tyr Trp 
                485                 490                 495     


Gly Gln Gly Thr Gln Val Thr Val Ser Ser Ser Gly Gly Pro Gly Pro 
            500                 505                 510         


Ala Gly Met Lys Gly Leu Pro Gly Ser Gln Thr Val Val Thr Gln Glu 
        515                 520                 525             


Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Gly 
    530                 535                 540                 


Ser Ser Thr Gly Ala Val Thr Ser Gly Asn Tyr Pro Asn Trp Val Gln 
545                 550                 555                 560 


Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Asp Tyr Lys Asp 
                565                 570                 575     


Asp Asp Asp Lys Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly 
            580                 585                 590         


Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala 
        595                 600                 605             


Glu Tyr Tyr Cys Val Leu Trp Tyr Ser Asn Arg Trp Val Phe Gly Gly 
    610                 615                 620                 


Gly Thr Lys Leu Thr Val Leu Gly Gly Gly Ser Gly Gly Gly Ser Glu 
625                 630                 635                 640 


Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 
                645                 650                 655     


Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr Ala 
            660                 665                 670         


Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 
        675                 680                 685             


Arg Ile Arg Ser Lys Tyr Asp Tyr Lys Asp Asp Asp Asp Lys Ala Asp 
    690                 695                 700                 


Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 
705                 710                 715                 720 


Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 
                725                 730                 735     


Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 
            740                 745                 750         


Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly Gly 
        755                 760                 765             


Gly Ser Gly Gly Gly Ser Asp Ala His Lys Ser Glu Val Ala His Arg 
    770                 775                 780                 


Phe Lys Asp Leu Gly Glu Glu Asn Phe Lys Ala Leu Val Leu Ile Ala 
785                 790                 795                 800 


Phe Ala Gln Tyr Leu Gln Gln Cys Pro Phe Glu Asp His Val Lys Leu 
                805                 810                 815     


Val Asn Glu Val Thr Glu Phe Ala Lys Thr Cys Val Ala Asp Glu Ser 
            820                 825                 830         


Ala Glu Asn Cys Asp Lys Ser Leu His Thr Leu Phe Gly Asp Lys Leu 
        835                 840                 845             


Cys Thr Val Ala Thr Leu Arg Glu Thr Tyr Gly Glu Met Ala Asp Cys 
    850                 855                 860                 


Cys Ala Lys Gln Glu Pro Glu Arg Asn Glu Cys Phe Leu Gln His Lys 
865                 870                 875                 880 


Asp Asp Asn Pro Asn Leu Pro Arg Leu Val Arg Pro Glu Val Asp Val 
                885                 890                 895     


Met Cys Thr Ala Phe His Asp Asn Glu Glu Thr Phe Leu Lys Lys Tyr 
            900                 905                 910         


Leu Tyr Glu Ile Ala Arg Arg His Pro Tyr Phe Tyr Ala Pro Glu Leu 
        915                 920                 925             


Leu Phe Phe Ala Lys Arg Tyr Lys Ala Ala Phe Thr Glu Cys Cys Gln 
    930                 935                 940                 


Ala Ala Asp Lys Ala Ala Cys Leu Leu Pro Lys Leu Asp Glu Leu Arg 
945                 950                 955                 960 


Asp Glu Gly Lys Ala Ser Ser Ala Lys Gln Arg Leu Lys Cys Ala Ser 
                965                 970                 975     


Leu Gln Lys Phe Gly Glu Arg Ala Phe Lys Ala Trp Ala Val Ala Arg 
            980                 985                 990         


Leu Ser Gln Arg Phe Pro Lys Ala  Glu Phe Ala Glu Val  Ser Lys Leu 
        995                 1000                 1005             


Val Thr  Asp Leu Thr Lys Val  His Thr Glu Cys Cys  His Gly Asp 
    1010                 1015                 1020             


Leu Leu  Glu Cys Ala Asp Asp  Arg Ala Asp Leu Ala  Lys Tyr Ile 
    1025                 1030                 1035             


Cys Glu  Asn Gln Asp Ser Ile  Ser Ser Lys Leu Lys  Glu Cys Cys 
    1040                 1045                 1050             


Glu Lys  Pro Leu Leu Glu Lys  Ser His Cys Ile Ala  Glu Val Glu 
    1055                 1060                 1065             


Asn Asp  Glu Met Pro Ala Asp  Leu Pro Ser Leu Ala  Ala Asp Phe 
    1070                 1075                 1080             


Val Glu  Ser Lys Asp Val Cys  Lys Asn Tyr Ala Glu  Ala Lys Asp 
    1085                 1090                 1095             


Val Phe  Leu Gly Met Phe Leu  Tyr Glu Tyr Ala Arg  Arg His Pro 
    1100                 1105                 1110             


Asp Tyr  Ser Val Val Leu Leu  Leu Arg Leu Ala Lys  Thr Tyr Lys 
    1115                 1120                 1125             


Thr Thr  Leu Glu Lys Cys Cys  Ala Ala Ala Asp Pro  His Glu Cys 
    1130                 1135                 1140             


Tyr Ala  Lys Val Phe Asp Glu  Phe Lys Pro Leu Val  Glu Glu Pro 
    1145                 1150                 1155             


Gln Asn  Leu Ile Lys Gln Asn  Cys Glu Leu Phe Glu  Gln Leu Gly 
    1160                 1165                 1170             


Glu Tyr  Lys Phe Gln Asn Ala  Leu Leu Val Arg Tyr  Thr Lys Lys 
    1175                 1180                 1185             


Val Pro  Gln Val Ser Thr Pro  Thr Leu Val Glu Val  Ser Arg Asn 
    1190                 1195                 1200             


Leu Gly  Lys Val Gly Ser Lys  Cys Cys Lys His Pro  Glu Ala Lys 
    1205                 1210                 1215             


Arg Met  Pro Cys Ala Glu Asp  Tyr Leu Ser Val Val  Leu Asn Gln 
    1220                 1225                 1230             


Leu Cys  Val Leu His Glu Lys  Thr Pro Val Ser Asp  Arg Val Thr 
    1235                 1240                 1245             


Lys Cys  Cys Thr Glu Ser Leu  Val Asn Arg Arg Pro  Cys Phe Ser 
    1250                 1255                 1260             


Ala Leu  Glu Val Asp Glu Thr  Tyr Val Pro Lys Glu  Phe Asn Ala 
    1265                 1270                 1275             


Glu Thr  Phe Thr Phe His Ala  Asp Ile Cys Thr Leu  Ser Glu Lys 
    1280                 1285                 1290             


Glu Arg  Gln Ile Lys Lys Gln  Thr Ala Leu Val Glu  Leu Val Lys 
    1295                 1300                 1305             


His Lys  Pro Lys Ala Thr Lys  Glu Gln Leu Lys Ala  Val Met Asp 
    1310                 1315                 1320             


Asp Phe  Ala Ala Phe Val Glu  Lys Cys Cys Lys Ala  Asp Asp Lys 
    1325                 1330                 1335             


Glu Thr  Cys Phe Ala Glu Glu  Gly Lys Lys Leu Val  Ala Ala Ser 
    1340                 1345                 1350             


Arg Ala  Ala Leu Gly Leu 
    1355                 


