                         SEQUENCE LISTING

<110>  ECOLE POLYTECHNIQUE FEDERALE DE LAUSANNE (EPFL)
 
<120>  EXTRACELLULAR MATRIX HEPARIN-BINDING DOMAINS

<130>  131664WO

<150>  US 61/667,634
<151>  2012-07-03

<160>  13    

<170>  PatentIn version 3.5

<210>  1
<211>  504
<212>  PRT
<213>  artificial

<220>
<223>  Tenascin III signal sequence with polyhistidine tag

<400>  1

Met Glu Thr Asp Thr Leu Leu Leu Trp Val Leu Leu Leu Trp Val Pro 
1               5                   10                  15      


Gly Ser Thr Gly Asp Ala Ala Gln Pro Ala Ile Glu Gly Arg Asn Gln 
            20                  25                  30          


Glu Gln Val Ser Pro Leu Gly Gly Ser Glu Val Ser Pro Pro Lys Asp 
        35                  40                  45              


Leu Val Val Thr Glu Val Thr Glu Glu Thr Val Asn Leu Ala Trp Asp 
    50                  55                  60                  


Asn Glu Met Arg Val Thr Glu Tyr Leu Val Val Tyr Thr Pro Thr His 
65                  70                  75                  80  


Glu Gly Gly Leu Glu Met Gln Phe Arg Val Pro Gly Asp Gln Thr Ser 
                85                  90                  95      


Thr Ile Ile Gln Glu Leu Glu Pro Gly Val Glu Tyr Phe Ile Arg Val 
            100                 105                 110         


Phe Ala Ile Leu Glu Asn Lys Lys Ser Ile Pro Val Ser Ala Arg Val 
        115                 120                 125             


Ala Thr Tyr Leu Pro Ala Pro Glu Gly Leu Lys Phe Lys Ser Ile Lys 
    130                 135                 140                 


Glu Thr Ser Val Glu Val Glu Trp Asp Pro Leu Asp Ile Ala Phe Glu 
145                 150                 155                 160 


Thr Trp Glu Ile Ile Phe Arg Asn Met Asn Lys Glu Asp Glu Gly Glu 
                165                 170                 175     


Ile Thr Lys Ser Leu Arg Arg Pro Glu Thr Ser Tyr Arg Gln Thr Gly 
            180                 185                 190         


Leu Ala Pro Gly Gln Glu Tyr Glu Ile Ser Leu His Ile Val Lys Asn 
        195                 200                 205             


Asn Thr Arg Gly Pro Gly Leu Lys Arg Val Thr Thr Thr Arg Leu Asp 
    210                 215                 220                 


Ala Pro Ser Gln Ile Glu Val Lys Asp Val Thr Asp Thr Thr Ala Leu 
225                 230                 235                 240 


Ile Thr Trp Phe Lys Pro Leu Ala Glu Ile Asp Gly Ile Glu Leu Thr 
                245                 250                 255     


Tyr Gly Ile Lys Asp Val Pro Gly Asp Arg Thr Thr Ile Asp Leu Thr 
            260                 265                 270         


Glu Asp Glu Asn Gln Tyr Ser Ile Gly Asn Leu Lys Pro Asp Thr Glu 
        275                 280                 285             


Tyr Glu Val Ser Leu Ile Ser Arg Arg Gly Asp Met Ser Ser Asn Pro 
    290                 295                 300                 


Ala Lys Glu Thr Phe Thr Thr Gly Leu Asp Ala Pro Arg Asn Leu Arg 
305                 310                 315                 320 


Arg Val Ser Gln Thr Asp Asn Ser Ile Thr Leu Glu Trp Arg Asn Gly 
                325                 330                 335     


Lys Ala Ala Ile Asp Ser Tyr Arg Ile Lys Tyr Ala Pro Ile Ser Gly 
            340                 345                 350         


Gly Asp His Ala Glu Val Asp Val Pro Lys Ser Gln Gln Ala Thr Thr 
        355                 360                 365             


Lys Thr Thr Leu Thr Gly Leu Arg Pro Gly Thr Glu Tyr Gly Ile Gly 
    370                 375                 380                 


Val Ser Ala Val Lys Glu Asp Lys Glu Ser Asn Pro Ala Thr Ile Asn 
385                 390                 395                 400 


Ala Ala Thr Glu Leu Asp Thr Pro Lys Asp Leu Gln Val Ser Glu Thr 
                405                 410                 415     


Ala Glu Thr Ser Leu Thr Leu Leu Trp Lys Thr Pro Leu Ala Lys Phe 
            420                 425                 430         


Asp Arg Tyr Arg Leu Asn Tyr Ser Leu Pro Thr Gly Gln Trp Val Gly 
        435                 440                 445             


Val Gln Leu Pro Arg Asn Thr Thr Ser Tyr Val Leu Arg Gly Leu Glu 
    450                 455                 460                 


Pro Gly Gln Glu Tyr Asn Val Leu Leu Thr Ala Glu Lys Gly Arg His 
465                 470                 475                 480 


Lys Ser Lys Pro Ala Arg Val Lys Ala Ser Thr Glu Gln Ala Gly Gly 
                485                 490                 495     


Gly Ser His His His His His His 
            500                 


<210>  2
<211>  68
<212>  PRT
<213>  artificial

<220>
<223>  GS linker, transglutaminase substrate, the Fg beta15-66, with a 
       Histidine tag

<400>  2

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


Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile 
            20                  25                  30          


Ser Gly Gly Gly Tyr Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr Gln 
        35                  40                  45              


Lys Lys Val Glu Arg Lys Ala Pro Asp Ala Gly Gly Cys Gly His His 
    50                  55                  60                  


His His His His 
65              


<210>  3
<211>  477
<212>  PRT
<213>  artificial

<220>
<223>  TG-FN III9-10/12/TNC III4-5, without C-terminal His tag

<400>  3

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


Gly Ile Asp Phe Ser Asp Ile Thr Ala Asn Ser Phe Thr Val His Trp 
            20                  25                  30          


Ile Ala Pro Arg Ala Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro 
        35                  40                  45              


Glu His Phe Ser Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg 
    50                  55                  60                  


Asn Ser Ile Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val 
65                  70                  75                  80  


Ser Ile Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Pro Leu Ile Gly 
                85                  90                  95      


Gln Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 
            100                 105                 110         


Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val Thr 
        115                 120                 125             


Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn Ser Pro 
    130                 135                 140                 


Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala Thr Ile Ser 
145                 150                 155                 160 


Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val Tyr Ala Val Thr 
                165                 170                 175     


Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro Ile Ser Ile Asn Tyr 
            180                 185                 190         


Arg Thr Glu Ile Asp Ser Ala Thr Ala Ile Pro Ala Pro Thr Asp Leu 
        195                 200                 205             


Lys Phe Thr Gln Val Thr Pro Thr Ser Leu Ser Ala Gln Trp Thr Pro 
    210                 215                 220                 


Pro Asn Val Gln Leu Thr Gly Tyr Arg Val Arg Val Thr Pro Lys Glu 
225                 230                 235                 240 


Lys Thr Gly Pro Met Lys Glu Ile Asn Leu Ala Pro Asp Ser Ser Ser 
                245                 250                 255     


Val Val Val Ser Gly Leu Met Val Ala Thr Lys Tyr Glu Val Ser Val 
            260                 265                 270         


Tyr Ala Leu Lys Asp Thr Leu Thr Ser Arg Pro Ala Gln Gly Val Val 
        275                 280                 285             


Thr Thr Gly Leu Asp Ala Pro Arg Asn Leu Arg Arg Val Ser Gln Thr 
    290                 295                 300                 


Asp Asn Ser Ile Thr Leu Glu Trp Arg Asn Gly Lys Ala Ala Ile Asp 
305                 310                 315                 320 


Ser Tyr Arg Ile Lys Tyr Ala Pro Ile Ser Gly Gly Asp His Ala Glu 
                325                 330                 335     


Val Asp Val Pro Lys Ser Gln Gln Ala Thr Thr Lys Thr Thr Leu Thr 
            340                 345                 350         


Gly Leu Arg Pro Gly Thr Glu Tyr Gly Ile Gly Val Ser Ala Val Lys 
        355                 360                 365             


Glu Asp Lys Glu Ser Asn Pro Ala Thr Ile Asn Ala Ala Thr Glu Leu 
    370                 375                 380                 


Asp Thr Pro Lys Asp Leu Gln Val Ser Glu Thr Ala Glu Thr Ser Leu 
385                 390                 395                 400 


Thr Leu Leu Trp Lys Thr Pro Leu Ala Lys Phe Asp Arg Tyr Arg Leu 
                405                 410                 415     


Asn Tyr Ser Leu Pro Thr Gly Gln Trp Val Gly Val Gln Leu Pro Arg 
            420                 425                 430         


Asn Thr Thr Ser Tyr Val Leu Arg Gly Leu Glu Pro Gly Gln Glu Tyr 
        435                 440                 445             


Asn Val Leu Leu Thr Ala Glu Lys Gly Arg His Lys Ser Lys Pro Ala 
    450                 455                 460                 


Arg Val Lys Ala Ser Thr Glu Gln Ala Gly Gly Gly Ser 
465                 470                 475         


<210>  4
<211>  474
<212>  PRT
<213>  artificial

<220>
<223>  TG-FN III9-10/TNC III3-5, without His tag

<400>  4

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


Gly Ile Asp Phe Ser Asp Ile Thr Ala Asn Ser Phe Thr Val His Trp 
            20                  25                  30          


Ile Ala Pro Arg Ala Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro 
        35                  40                  45              


Glu His Phe Ser Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg 
    50                  55                  60                  


Asn Ser Ile Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val 
65                  70                  75                  80  


Ser Ile Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Pro Leu Ile Gly 
                85                  90                  95      


Gln Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 
            100                 105                 110         


Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val Thr 
        115                 120                 125             


Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn Ser Pro 
    130                 135                 140                 


Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala Thr Ile Ser 
145                 150                 155                 160 


Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val Tyr Ala Val Thr 
                165                 170                 175     


Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro Ile Ser Ile Asn Tyr 
            180                 185                 190         


Arg Thr Thr Thr Thr Arg Leu Asp Ala Pro Ser Gln Ile Glu Val Lys 
        195                 200                 205             


Asp Val Thr Asp Thr Thr Ala Leu Ile Thr Trp Phe Lys Pro Leu Ala 
    210                 215                 220                 


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


Asp Arg Thr Thr Ile Asp Leu Thr Glu Asp Glu Asn Gln Tyr Ser Ile 
                245                 250                 255     


Gly Asn Leu Lys Pro Asp Thr Glu Tyr Glu Val Ser Leu Ile Ser Arg 
            260                 265                 270         


Arg Gly Asp Met Ser Ser Asn Pro Ala Lys Glu Thr Phe Thr Thr Gly 
        275                 280                 285             


Leu Asp Ala Pro Arg Asn Leu Arg Arg Val Ser Gln Thr Asp Asn Ser 
    290                 295                 300                 


Ile Thr Leu Glu Trp Arg Asn Gly Lys Ala Ala Ile Asp Ser Tyr Arg 
305                 310                 315                 320 


Ile Lys Tyr Ala Pro Ile Ser Gly Gly Asp His Ala Glu Val Asp Val 
                325                 330                 335     


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


Pro Gly Thr Glu Tyr Gly Ile Gly Val Ser Ala Val Lys Glu Asp Lys 
        355                 360                 365             


Glu Ser Asn Pro Ala Thr Ile Asn Ala Ala Thr Glu Leu Asp Thr Pro 
    370                 375                 380                 


Lys Asp Leu Gln Val Ser Glu Thr Ala Glu Thr Ser Leu Thr Leu Leu 
385                 390                 395                 400 


Trp Lys Thr Pro Leu Ala Lys Phe Asp Arg Tyr Arg Leu Asn Tyr Ser 
                405                 410                 415     


Leu Pro Thr Gly Gln Trp Val Gly Val Gln Leu Pro Arg Asn Thr Thr 
            420                 425                 430         


Ser Tyr Val Leu Arg Gly Leu Glu Pro Gly Gln Glu Tyr Asn Val Leu 
        435                 440                 445             


Leu Thr Ala Glu Lys Gly Arg His Lys Ser Lys Pro Ala Arg Val Lys 
    450                 455                 460                 


Ala Ser Thr Glu Gln Ala Gly Gly Gly Ser 
465                 470                 


<210>  5
<211>  654
<212>  PRT
<213>  artificial

<220>
<223>  FN III9-10/TNC III1-5, without His tag

<400>  5

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


Gly Ile Asp Phe Ser Asp Ile Thr Ala Asn Ser Phe Thr Val His Trp 
            20                  25                  30          


Ile Ala Pro Arg Ala Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro 
        35                  40                  45              


Glu His Phe Ser Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg 
    50                  55                  60                  


Asn Ser Ile Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val 
65                  70                  75                  80  


Ser Ile Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Pro Leu Ile Gly 
                85                  90                  95      


Gln Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 
            100                 105                 110         


Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val Thr 
        115                 120                 125             


Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn Ser Pro 
    130                 135                 140                 


Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala Thr Ile Ser 
145                 150                 155                 160 


Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val Tyr Ala Val Thr 
                165                 170                 175     


Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro Ile Ser Ile Asn Tyr 
            180                 185                 190         


Arg Thr Gly Gly Ser Glu Val Ser Pro Pro Lys Asp Leu Val Val Thr 
        195                 200                 205             


Glu Val Thr Glu Glu Thr Val Asn Leu Ala Trp Asp Asn Glu Met Arg 
    210                 215                 220                 


Val Thr Glu Tyr Leu Val Val Tyr Thr Pro Thr His Glu Gly Gly Leu 
225                 230                 235                 240 


Glu Met Gln Phe Arg Val Pro Gly Asp Gln Thr Ser Thr Ile Ile Gln 
                245                 250                 255     


Glu Leu Glu Pro Gly Val Glu Tyr Phe Ile Arg Val Phe Ala Ile Leu 
            260                 265                 270         


Glu Asn Lys Lys Ser Ile Pro Val Ser Ala Arg Val Ala Thr Tyr Leu 
        275                 280                 285             


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


Glu Val Glu Trp Asp Pro Leu Asp Ile Ala Phe Glu Thr Trp Glu Ile 
305                 310                 315                 320 


Ile Phe Arg Asn Met Asn Lys Glu Asp Glu Gly Glu Ile Thr Lys Ser 
                325                 330                 335     


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


Gln Glu Tyr Glu Ile Ser Leu His Ile Val Lys Asn Asn Thr Arg Gly 
        355                 360                 365             


Pro Gly Leu Lys Arg Val Thr Thr Thr Arg Leu Asp Ala Pro Ser Gln 
    370                 375                 380                 


Ile Glu Val Lys Asp Val Thr Asp Thr Thr Ala Leu Ile Thr Trp Phe 
385                 390                 395                 400 


Lys Pro Leu Ala Glu Ile Asp Gly Ile Glu Leu Thr Tyr Gly Ile Lys 
                405                 410                 415     


Asp Val Pro Gly Asp Arg Thr Thr Ile Asp Leu Thr Glu Asp Glu Asn 
            420                 425                 430         


Gln Tyr Ser Ile Gly Asn Leu Lys Pro Asp Thr Glu Tyr Glu Val Ser 
        435                 440                 445             


Leu Ile Ser Arg Arg Gly Asp Met Ser Ser Asn Pro Ala Lys Glu Thr 
    450                 455                 460                 


Phe Thr Thr Gly Leu Asp Ala Pro Arg Asn Leu Arg Arg Val Ser Gln 
465                 470                 475                 480 


Thr Asp Asn Ser Ile Thr Leu Glu Trp Arg Asn Gly Lys Ala Ala Ile 
                485                 490                 495     


Asp Ser Tyr Arg Ile Lys Tyr Ala Pro Ile Ser Gly Gly Asp His Ala 
            500                 505                 510         


Glu Val Asp Val Pro Lys Ser Gln Gln Ala Thr Thr Lys Thr Thr Leu 
        515                 520                 525             


Thr Gly Leu Arg Pro Gly Thr Glu Tyr Gly Ile Gly Val Ser Ala Val 
    530                 535                 540                 


Lys Glu Asp Lys Glu Ser Asn Pro Ala Thr Ile Asn Ala Ala Thr Glu 
545                 550                 555                 560 


Leu Asp Thr Pro Lys Asp Leu Gln Val Ser Glu Thr Ala Glu Thr Ser 
                565                 570                 575     


Leu Thr Leu Leu Trp Lys Thr Pro Leu Ala Lys Phe Asp Arg Tyr Arg 
            580                 585                 590         


Leu Asn Tyr Ser Leu Pro Thr Gly Gln Trp Val Gly Val Gln Leu Pro 
        595                 600                 605             


Arg Asn Thr Thr Ser Tyr Val Leu Arg Gly Leu Glu Pro Gly Gln Glu 
    610                 615                 620                 


Tyr Asn Val Leu Leu Thr Ala Glu Lys Gly Arg His Lys Ser Lys Pro 
625                 630                 635                 640 


Ala Arg Val Lys Ala Ser Thr Glu Gln Ala Gly Gly Gly Ser 
                645                 650                 


<210>  6
<211>  246
<212>  PRT
<213>  artificial

<220>
<223>  FN III9-10/Fg  beta 15-66, without His tag

<400>  6

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


Gly Ile Asp Phe Ser Asp Ile Thr Ala Asn Ser Phe Thr Val His Trp 
            20                  25                  30          


Ile Ala Pro Arg Ala Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro 
        35                  40                  45              


Glu His Phe Ser Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg 
    50                  55                  60                  


Asn Ser Ile Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val 
65                  70                  75                  80  


Ser Ile Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Pro Leu Ile Gly 
                85                  90                  95      


Gln Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 
            100                 105                 110         


Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val Thr 
        115                 120                 125             


Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn Ser Pro 
    130                 135                 140                 


Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala Thr Ile Ser 
145                 150                 155                 160 


Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val Tyr Ala Val Thr 
                165                 170                 175     


Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro Ile Ser Ile Asn Tyr 
            180                 185                 190         


Arg Thr Gly His Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser 
        195                 200                 205             


Leu Arg Pro Ala Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg 
    210                 215                 220                 


Pro Ala Lys Ala Ala Ala Thr Gln Lys Lys Val Glu Arg Lys Ala Pro 
225                 230                 235                 240 


Asp Ala Gly Gly Cys Gly 
                245     


<210>  7
<211>  525
<212>  PRT
<213>  artificial

<220>
<223>  FN III9-10/12-14/Fg  15-66, without His tag

<400>  7

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


Gly Ile Asp Phe Ser Asp Ile Thr Ala Asn Ser Phe Thr Val His Trp 
            20                  25                  30          


Ile Ala Pro Arg Ala Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro 
        35                  40                  45              


Glu His Phe Ser Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg 
    50                  55                  60                  


Asn Ser Ile Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val 
65                  70                  75                  80  


Ser Ile Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Pro Leu Ile Gly 
                85                  90                  95      


Gln Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 
            100                 105                 110         


Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val Thr 
        115                 120                 125             


Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn Ser Pro 
    130                 135                 140                 


Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala Thr Ile Ser 
145                 150                 155                 160 


Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val Tyr Ala Val Thr 
                165                 170                 175     


Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro Ile Ser Ile Asn Tyr 
            180                 185                 190         


Arg Thr Glu Ile Asp Ser Ala Thr Ala Ile Pro Ala Pro Thr Asp Leu 
        195                 200                 205             


Lys Phe Thr Gln Val Thr Pro Thr Ser Leu Ser Ala Gln Trp Thr Pro 
    210                 215                 220                 


Pro Asn Val Gln Leu Thr Gly Tyr Arg Val Arg Val Thr Pro Lys Glu 
225                 230                 235                 240 


Lys Thr Gly Pro Met Lys Glu Ile Asn Leu Ala Pro Asp Ser Ser Ser 
                245                 250                 255     


Val Val Val Ser Gly Leu Met Val Ala Thr Lys Tyr Glu Val Ser Val 
            260                 265                 270         


Tyr Ala Leu Lys Asp Thr Leu Thr Ser Arg Pro Ala Gln Gly Val Val 
        275                 280                 285             


Thr Thr Leu Glu Asn Val Ser Pro Pro Arg Arg Ala Arg Val Thr Asp 
    290                 295                 300                 


Ala Thr Glu Thr Thr Ile Thr Ile Ser Trp Arg Thr Lys Thr Glu Thr 
305                 310                 315                 320 


Ile Thr Gly Phe Gln Val Asp Ala Val Pro Ala Asn Gly Gln Thr Pro 
                325                 330                 335     


Ile Gln Arg Thr Ile Lys Pro Asp Val Arg Ser Tyr Thr Ile Thr Gly 
            340                 345                 350         


Leu Gln Pro Gly Thr Asp Tyr Lys Ile Tyr Leu Tyr Thr Leu Asn Asp 
        355                 360                 365             


Asn Ala Arg Ser Ser Pro Val Val Ile Asp Ala Ser Thr Ala Ile Asp 
    370                 375                 380                 


Ala Pro Ser Asn Leu Arg Phe Leu Ala Thr Thr Pro Asn Ser Leu Leu 
385                 390                 395                 400 


Val Ser Trp Gln Pro Pro Arg Ala Arg Ile Thr Gly Tyr Ile Ile Lys 
                405                 410                 415     


Tyr Glu Lys Pro Gly Ser Pro Pro Arg Glu Val Val Pro Arg Pro Arg 
            420                 425                 430         


Pro Gly Val Thr Glu Ala Thr Ile Thr Gly Leu Glu Pro Gly Thr Glu 
        435                 440                 445             


Tyr Thr Ile Tyr Val Ile Ala Leu Lys Asn Asn Gln Lys Ser Glu Pro 
    450                 455                 460                 


Leu Ile Gly Arg Lys Lys Thr Phe Lys Gly His Arg Pro Leu Asp Lys 
465                 470                 475                 480 


Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser 
                485                 490                 495     


Gly Gly Gly Tyr Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr Gln Lys 
            500                 505                 510         


Lys Val Glu Arg Lys Ala Pro Asp Ala Gly Gly Cys Gly 
        515                 520                 525 


<210>  8
<211>  52
<212>  PRT
<213>  artificial

<220>
<223>  frgament of fibrinogen beta 15-66

<400>  8

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


Pro Ala Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg Pro Ala 
            20                  25                  30          


Lys Ala Ala Ala Thr Gln Lys Lys Val Glu Arg Lys Ala Pro Asp Ala 
        35                  40                  45              


Gly Gly Cys Gly 
    50          


<210>  9
<211>  452
<212>  PRT
<213>  artificial

<220>
<223>  Tenascin III1-5

<400>  9

Glu Val Ser Pro Pro Lys Asp Leu Val Val Thr Glu Val Thr Glu Glu 
1               5                   10                  15      


Thr Val Asn Leu Ala Trp Asp Asn Glu Met Arg Val Thr Glu Tyr Leu 
            20                  25                  30          


Val Val Tyr Thr Pro Thr His Glu Gly Gly Leu Glu Met Gln Phe Arg 
        35                  40                  45              


Val Pro Gly Asp Gln Thr Ser Thr Ile Ile Gln Glu Leu Glu Pro Gly 
    50                  55                  60                  


Val Glu Tyr Phe Ile Arg Val Phe Ala Ile Leu Glu Asn Lys Lys Ser 
65                  70                  75                  80  


Ile Pro Val Ser Ala Arg Val Ala Thr Tyr Leu Pro Ala Pro Glu Gly 
                85                  90                  95      


Leu Lys Phe Lys Ser Ile Lys Glu Thr Ser Val Glu Val Glu Trp Asp 
            100                 105                 110         


Pro Leu Asp Ile Ala Phe Glu Thr Trp Glu Ile Ile Phe Arg Asn Met 
        115                 120                 125             


Asn Lys Glu Asp Glu Gly Glu Ile Thr Lys Ser Leu Arg Arg Pro Glu 
    130                 135                 140                 


Thr Ser Tyr Arg Gln Thr Gly Leu Ala Pro Gly Gln Glu Tyr Glu Ile 
145                 150                 155                 160 


Ser Leu His Ile Val Lys Asn Asn Thr Arg Gly Pro Gly Leu Lys Arg 
                165                 170                 175     


Val Thr Thr Thr Arg Leu Asp Ala Pro Ser Gln Ile Glu Val Lys Asp 
            180                 185                 190         


Val Thr Asp Thr Thr Ala Leu Ile Thr Trp Phe Lys Pro Leu Ala Glu 
        195                 200                 205             


Ile Asp Gly Ile Glu Leu Thr Tyr Gly Ile Lys Asp Val Pro Gly Asp 
    210                 215                 220                 


Arg Thr Thr Ile Asp Leu Thr Glu Asp Glu Asn Gln Tyr Ser Ile Gly 
225                 230                 235                 240 


Asn Leu Lys Pro Asp Thr Glu Tyr Glu Val Ser Leu Ile Ser Arg Arg 
                245                 250                 255     


Gly Asp Met Ser Ser Asn Pro Ala Lys Glu Thr Phe Thr Thr Gly Leu 
            260                 265                 270         


Asp Ala Pro Arg Asn Leu Arg Arg Val Ser Gln Thr Asp Asn Ser Ile 
        275                 280                 285             


Thr Leu Glu Trp Arg Asn Gly Lys Ala Ala Ile Asp Ser Tyr Arg Ile 
    290                 295                 300                 


Lys Tyr Ala Pro Ile Ser Gly Gly Asp His Ala Glu Val Asp Val Pro 
305                 310                 315                 320 


Lys Ser Gln Gln Ala Thr Thr Lys Thr Thr Leu Thr Gly Leu Arg Pro 
                325                 330                 335     


Gly Thr Glu Tyr Gly Ile Gly Val Ser Ala Val Lys Glu Asp Lys Glu 
            340                 345                 350         


Ser Asn Pro Ala Thr Ile Asn Ala Ala Thr Glu Leu Asp Thr Pro Lys 
        355                 360                 365             


Asp Leu Gln Val Ser Glu Thr Ala Glu Thr Ser Leu Thr Leu Leu Trp 
    370                 375                 380                 


Lys Thr Pro Leu Ala Lys Phe Asp Arg Tyr Arg Leu Asn Tyr Ser Leu 
385                 390                 395                 400 


Pro Thr Gly Gln Trp Val Gly Val Gln Leu Pro Arg Asn Thr Thr Ser 
                405                 410                 415     


Tyr Val Leu Arg Gly Leu Glu Pro Gly Gln Glu Tyr Asn Val Leu Leu 
            420                 425                 430         


Thr Ala Glu Lys Gly Arg His Lys Ser Lys Pro Ala Arg Val Lys Ala 
        435                 440                 445             


Ser Thr Glu Gln 
    450         


<210>  10
<211>  7
<212>  PRT
<213>  artificial

<220>
<223>  residues 1-8 of alpha2-plasmin inhibitor

<400>  10

Asn Gln Glu Gln Val Ser Pro 
1               5           


<210>  11
<211>  5
<212>  PRT
<213>  artificial

<220>
<223>  FN III9 synergy site

<400>  11

Pro His Ser Arg Asn 
1               5   


<210>  12
<211>  7
<212>  PRT
<213>  artificial

<220>
<223>  domain of TNCIII3

<400>  12

Val Thr Asp Thr Thr Ala Leu 
1               5           


<210>  13
<211>  8
<212>  PRT
<213>  artificial

<220>
<223>  fibronection type III domain fragment

<400>  13

Ala Glu Ile Asp Gly Ile Glu Leu 
1               5               


