                         SEQUENCE LISTING

<110>  AFFIBODY AB
 
<120>  NEW POLYPEPTIDES

<130>  21071642

<150>  EP13182022.7
<151>  2013-08-28

<160>  54    

<170>  PatentIn version 3.5

<210>  1
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  1

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  2
<211>  46
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered albumin binding polypeptide

<400>  2

Leu Ala Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly 
1               5                   10                  15      


Val Ser Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu 
            20                  25                  30          


Gly Val Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
        35                  40                  45      


<210>  3
<211>  1676
<212>  PRT
<213>  HOMO SAPIENS

<400>  3

Met Gly Leu Leu Gly Ile Leu Cys Phe Leu Ile Phe Leu Gly Lys Thr 
1               5                   10                  15      


Trp Gly Gln Glu Gln Thr Tyr Val Ile Ser Ala Pro Lys Ile Phe Arg 
            20                  25                  30          


Val Gly Ala Ser Glu Asn Ile Val Ile Gln Val Tyr Gly Tyr Thr Glu 
        35                  40                  45              


Ala Phe Asp Ala Thr Ile Ser Ile Lys Ser Tyr Pro Asp Lys Lys Phe 
    50                  55                  60                  


Ser Tyr Ser Ser Gly His Val His Leu Ser Ser Glu Asn Lys Phe Gln 
65                  70                  75                  80  


Asn Ser Ala Ile Leu Thr Ile Gln Pro Lys Gln Leu Pro Gly Gly Gln 
                85                  90                  95      


Asn Pro Val Ser Tyr Val Tyr Leu Glu Val Val Ser Lys His Phe Ser 
            100                 105                 110         


Lys Ser Lys Arg Met Pro Ile Thr Tyr Asp Asn Gly Phe Leu Phe Ile 
        115                 120                 125             


His Thr Asp Lys Pro Val Tyr Thr Pro Asp Gln Ser Val Lys Val Arg 
    130                 135                 140                 


Val Tyr Ser Leu Asn Asp Asp Leu Lys Pro Ala Lys Arg Glu Thr Val 
145                 150                 155                 160 


Leu Thr Phe Ile Asp Pro Glu Gly Ser Glu Val Asp Met Val Glu Glu 
                165                 170                 175     


Ile Asp His Ile Gly Ile Ile Ser Phe Pro Asp Phe Lys Ile Pro Ser 
            180                 185                 190         


Asn Pro Arg Tyr Gly Met Trp Thr Ile Lys Ala Lys Tyr Lys Glu Asp 
        195                 200                 205             


Phe Ser Thr Thr Gly Thr Ala Tyr Phe Glu Val Lys Glu Tyr Val Leu 
    210                 215                 220                 


Pro His Phe Ser Val Ser Ile Glu Pro Glu Tyr Asn Phe Ile Gly Tyr 
225                 230                 235                 240 


Lys Asn Phe Lys Asn Phe Glu Ile Thr Ile Lys Ala Arg Tyr Phe Tyr 
                245                 250                 255     


Asn Lys Val Val Thr Glu Ala Asp Val Tyr Ile Thr Phe Gly Ile Arg 
            260                 265                 270         


Glu Asp Leu Lys Asp Asp Gln Lys Glu Met Met Gln Thr Ala Met Gln 
        275                 280                 285             


Asn Thr Met Leu Ile Asn Gly Ile Ala Gln Val Thr Phe Asp Ser Glu 
    290                 295                 300                 


Thr Ala Val Lys Glu Leu Ser Tyr Tyr Ser Leu Glu Asp Leu Asn Asn 
305                 310                 315                 320 


Lys Tyr Leu Tyr Ile Ala Val Thr Val Ile Glu Ser Thr Gly Gly Phe 
                325                 330                 335     


Ser Glu Glu Ala Glu Ile Pro Gly Ile Lys Tyr Val Leu Ser Pro Tyr 
            340                 345                 350         


Lys Leu Asn Leu Val Ala Thr Pro Leu Phe Leu Lys Pro Gly Ile Pro 
        355                 360                 365             


Tyr Pro Ile Lys Val Gln Val Lys Asp Ser Leu Asp Gln Leu Val Gly 
    370                 375                 380                 


Gly Val Pro Val Thr Leu Asn Ala Gln Thr Ile Asp Val Asn Gln Glu 
385                 390                 395                 400 


Thr Ser Asp Leu Asp Pro Ser Lys Ser Val Thr Arg Val Asp Asp Gly 
                405                 410                 415     


Val Ala Ser Phe Val Leu Asn Leu Pro Ser Gly Val Thr Val Leu Glu 
            420                 425                 430         


Phe Asn Val Lys Thr Asp Ala Pro Asp Leu Pro Glu Glu Asn Gln Ala 
        435                 440                 445             


Arg Glu Gly Tyr Arg Ala Ile Ala Tyr Ser Ser Leu Ser Gln Ser Tyr 
    450                 455                 460                 


Leu Tyr Ile Asp Trp Thr Asp Asn His Lys Ala Leu Leu Val Gly Glu 
465                 470                 475                 480 


His Leu Asn Ile Ile Val Thr Pro Lys Ser Pro Tyr Ile Asp Lys Ile 
                485                 490                 495     


Thr His Tyr Asn Tyr Leu Ile Leu Ser Lys Gly Lys Ile Ile His Phe 
            500                 505                 510         


Gly Thr Arg Glu Lys Phe Ser Asp Ala Ser Tyr Gln Ser Ile Asn Ile 
        515                 520                 525             


Pro Val Thr Gln Asn Met Val Pro Ser Ser Arg Leu Leu Val Tyr Tyr 
    530                 535                 540                 


Ile Val Thr Gly Glu Gln Thr Ala Glu Leu Val Ser Asp Ser Val Trp 
545                 550                 555                 560 


Leu Asn Ile Glu Glu Lys Cys Gly Asn Gln Leu Gln Val His Leu Ser 
                565                 570                 575     


Pro Asp Ala Asp Ala Tyr Ser Pro Gly Gln Thr Val Ser Leu Asn Met 
            580                 585                 590         


Ala Thr Gly Met Asp Ser Trp Val Ala Leu Ala Ala Val Asp Ser Ala 
        595                 600                 605             


Val Tyr Gly Val Gln Arg Gly Ala Lys Lys Pro Leu Glu Arg Val Phe 
    610                 615                 620                 


Gln Phe Leu Glu Lys Ser Asp Leu Gly Cys Gly Ala Gly Gly Gly Leu 
625                 630                 635                 640 


Asn Asn Ala Asn Val Phe His Leu Ala Gly Leu Thr Phe Leu Thr Asn 
                645                 650                 655     


Ala Asn Ala Asp Asp Ser Gln Glu Asn Asp Glu Pro Cys Lys Glu Ile 
            660                 665                 670         


Leu Arg Pro Arg Arg Thr Leu Gln Lys Lys Ile Glu Glu Ile Ala Ala 
        675                 680                 685             


Lys Tyr Lys His Ser Val Val Lys Lys Cys Cys Tyr Asp Gly Ala Cys 
    690                 695                 700                 


Val Asn Asn Asp Glu Thr Cys Glu Gln Arg Ala Ala Arg Ile Ser Leu 
705                 710                 715                 720 


Gly Pro Arg Cys Ile Lys Ala Phe Thr Glu Cys Cys Val Val Ala Ser 
                725                 730                 735     


Gln Leu Arg Ala Asn Ile Ser His Lys Asp Met Gln Leu Gly Arg Leu 
            740                 745                 750         


His Met Lys Thr Leu Leu Pro Val Ser Lys Pro Glu Ile Arg Ser Tyr 
        755                 760                 765             


Phe Pro Glu Ser Trp Leu Trp Glu Val His Leu Val Pro Arg Arg Lys 
    770                 775                 780                 


Gln Leu Gln Phe Ala Leu Pro Asp Ser Leu Thr Thr Trp Glu Ile Gln 
785                 790                 795                 800 


Gly Val Gly Ile Ser Asn Thr Gly Ile Cys Val Ala Asp Thr Val Lys 
                805                 810                 815     


Ala Lys Val Phe Lys Asp Val Phe Leu Glu Met Asn Ile Pro Tyr Ser 
            820                 825                 830         


Val Val Arg Gly Glu Gln Ile Gln Leu Lys Gly Thr Val Tyr Asn Tyr 
        835                 840                 845             


Arg Thr Ser Gly Met Gln Phe Cys Val Lys Met Ser Ala Val Glu Gly 
    850                 855                 860                 


Ile Cys Thr Ser Glu Ser Pro Val Ile Asp His Gln Gly Thr Lys Ser 
865                 870                 875                 880 


Ser Lys Cys Val Arg Gln Lys Val Glu Gly Ser Ser Ser His Leu Val 
                885                 890                 895     


Thr Phe Thr Val Leu Pro Leu Glu Ile Gly Leu His Asn Ile Asn Phe 
            900                 905                 910         


Ser Leu Glu Thr Trp Phe Gly Lys Glu Ile Leu Val Lys Thr Leu Arg 
        915                 920                 925             


Val Val Pro Glu Gly Val Lys Arg Glu Ser Tyr Ser Gly Val Thr Leu 
    930                 935                 940                 


Asp Pro Arg Gly Ile Tyr Gly Thr Ile Ser Arg Arg Lys Glu Phe Pro 
945                 950                 955                 960 


Tyr Arg Ile Pro Leu Asp Leu Val Pro Lys Thr Glu Ile Lys Arg Ile 
                965                 970                 975     


Leu Ser Val Lys Gly Leu Leu Val Gly Glu Ile Leu Ser Ala Val Leu 
            980                 985                 990         


Ser Gln Glu Gly Ile Asn Ile Leu  Thr His Leu Pro Lys  Gly Ser Ala 
        995                 1000                 1005             


Glu Ala  Glu Leu Met Ser Val  Val Pro Val Phe Tyr  Val Phe His 
    1010                 1015                 1020             


Tyr Leu  Glu Thr Gly Asn His  Trp Asn Ile Phe His  Ser Asp Pro 
    1025                 1030                 1035             


Leu Ile  Glu Lys Gln Lys Leu  Lys Lys Lys Leu Lys  Glu Gly Met 
    1040                 1045                 1050             


Leu Ser  Ile Met Ser Tyr Arg  Asn Ala Asp Tyr Ser  Tyr Ser Val 
    1055                 1060                 1065             


Trp Lys  Gly Gly Ser Ala Ser  Thr Trp Leu Thr Ala  Phe Ala Leu 
    1070                 1075                 1080             


Arg Val  Leu Gly Gln Val Asn  Lys Tyr Val Glu Gln  Asn Gln Asn 
    1085                 1090                 1095             


Ser Ile  Cys Asn Ser Leu Leu  Trp Leu Val Glu Asn  Tyr Gln Leu 
    1100                 1105                 1110             


Asp Asn  Gly Ser Phe Lys Glu  Asn Ser Gln Tyr Gln  Pro Ile Lys 
    1115                 1120                 1125             


Leu Gln  Gly Thr Leu Pro Val  Glu Ala Arg Glu Asn  Ser Leu Tyr 
    1130                 1135                 1140             


Leu Thr  Ala Phe Thr Val Ile  Gly Ile Arg Lys Ala  Phe Asp Ile 
    1145                 1150                 1155             


Cys Pro  Leu Val Lys Ile Asp  Thr Ala Leu Ile Lys  Ala Asp Asn 
    1160                 1165                 1170             


Phe Leu  Leu Glu Asn Thr Leu  Pro Ala Gln Ser Thr  Phe Thr Leu 
    1175                 1180                 1185             


Ala Ile  Ser Ala Tyr Ala Leu  Ser Leu Gly Asp Lys  Thr His Pro 
    1190                 1195                 1200             


Gln Phe  Arg Ser Ile Val Ser  Ala Leu Lys Arg Glu  Ala Leu Val 
    1205                 1210                 1215             


Lys Gly  Asn Pro Pro Ile Tyr  Arg Phe Trp Lys Asp  Asn Leu Gln 
    1220                 1225                 1230             


His Lys  Asp Ser Ser Val Pro  Asn Thr Gly Thr Ala  Arg Met Val 
    1235                 1240                 1245             


Glu Thr  Thr Ala Tyr Ala Leu  Leu Thr Ser Leu Asn  Leu Lys Asp 
    1250                 1255                 1260             


Ile Asn  Tyr Val Asn Pro Val  Ile Lys Trp Leu Ser  Glu Glu Gln 
    1265                 1270                 1275             


Arg Tyr  Gly Gly Gly Phe Tyr  Ser Thr Gln Asp Thr  Ile Asn Ala 
    1280                 1285                 1290             


Ile Glu  Gly Leu Thr Glu Tyr  Ser Leu Leu Val Lys  Gln Leu Arg 
    1295                 1300                 1305             


Leu Ser  Met Asp Ile Asp Val  Ser Tyr Lys His Lys  Gly Ala Leu 
    1310                 1315                 1320             


His Asn  Tyr Lys Met Thr Asp  Lys Asn Phe Leu Gly  Arg Pro Val 
    1325                 1330                 1335             


Glu Val  Leu Leu Asn Asp Asp  Leu Ile Val Ser Thr  Gly Phe Gly 
    1340                 1345                 1350             


Ser Gly  Leu Ala Thr Val His  Val Thr Thr Val Val  His Lys Thr 
    1355                 1360                 1365             


Ser Thr  Ser Glu Glu Val Cys  Ser Phe Tyr Leu Lys  Ile Asp Thr 
    1370                 1375                 1380             


Gln Asp  Ile Glu Ala Ser His  Tyr Arg Gly Tyr Gly  Asn Ser Asp 
    1385                 1390                 1395             


Tyr Lys  Arg Ile Val Ala Cys  Ala Ser Tyr Lys Pro  Ser Arg Glu 
    1400                 1405                 1410             


Glu Ser  Ser Ser Gly Ser Ser  His Ala Val Met Asp  Ile Ser Leu 
    1415                 1420                 1425             


Pro Thr  Gly Ile Ser Ala Asn  Glu Glu Asp Leu Lys  Ala Leu Val 
    1430                 1435                 1440             


Glu Gly  Val Asp Gln Leu Phe  Thr Asp Tyr Gln Ile  Lys Asp Gly 
    1445                 1450                 1455             


His Val  Ile Leu Gln Leu Asn  Ser Ile Pro Ser Ser  Asp Phe Leu 
    1460                 1465                 1470             


Cys Val  Arg Phe Arg Ile Phe  Glu Leu Phe Glu Val  Gly Phe Leu 
    1475                 1480                 1485             


Ser Pro  Ala Thr Phe Thr Val  Tyr Glu Tyr His Arg  Pro Asp Lys 
    1490                 1495                 1500             


Gln Cys  Thr Met Phe Tyr Ser  Thr Ser Asn Ile Lys  Ile Gln Lys 
    1505                 1510                 1515             


Val Cys  Glu Gly Ala Ala Cys  Lys Cys Val Glu Ala  Asp Cys Gly 
    1520                 1525                 1530             


Gln Met  Gln Glu Glu Leu Asp  Leu Thr Ile Ser Ala  Glu Thr Arg 
    1535                 1540                 1545             


Lys Gln  Thr Ala Cys Lys Pro  Glu Ile Ala Tyr Ala  Tyr Lys Val 
    1550                 1555                 1560             


Ser Ile  Thr Ser Ile Thr Val  Glu Asn Val Phe Val  Lys Tyr Lys 
    1565                 1570                 1575             


Ala Thr  Leu Leu Asp Ile Tyr  Lys Thr Gly Glu Ala  Val Ala Glu 
    1580                 1585                 1590             


Lys Asp  Ser Glu Ile Thr Phe  Ile Lys Lys Val Thr  Cys Thr Asn 
    1595                 1600                 1605             


Ala Glu  Leu Val Lys Gly Arg  Gln Tyr Leu Ile Met  Gly Lys Glu 
    1610                 1615                 1620             


Ala Leu  Gln Ile Lys Tyr Asn  Phe Ser Phe Arg Tyr  Ile Tyr Pro 
    1625                 1630                 1635             


Leu Asp  Ser Leu Thr Trp Ile  Glu Tyr Trp Pro Arg  Asp Thr Thr 
    1640                 1645                 1650             


Cys Ser  Ser Cys Gln Ala Phe  Leu Ala Asn Leu Asp  Glu Phe Ala 
    1655                 1660                 1665             


Glu Asp  Ile Phe Leu Asn Gly  Cys 
    1670                 1675     


<210>  4
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  4

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Arg Gln Pro Glu Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  5
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  5

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  6
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  6

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Val Leu Ala Asn Arg Glu Leu Asp Lys Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asn Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Leu His Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  7
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  7

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Ser Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  8
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  8

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Glu Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  9
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  9

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Ala 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  10
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  10

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Glu Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  11
<211>  103
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  11

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Leu Ala Glu Ala Lys Glu Ala 
    50                  55                  60                  


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


Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val Glu Ala Leu Lys Asp 
                85                  90                  95      


Ala Ile Leu Ala Ala Leu Pro 
            100             


<210>  12
<211>  57
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  12

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro 
    50                  55          


<210>  13
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  13

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  14
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  14

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys Val Ala Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  15
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  15

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Glu Ser Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  16
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  16

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Arg Gln Pro Glu Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  17
<211>  57
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  17

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Glu Ser Ser Gln Ala Pro 
    50                  55          


<210>  18
<211>  57
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  18

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Arg Gln Pro Glu Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro 
    50                  55          


<210>  19
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  19

Glu Val Leu Glu Ala Trp Asp Glu Ile Asp Arg Leu Pro Asn Leu Thr 
1               5                   10                  15      


Ile Glu Gln Trp Leu Ala Phe Ile Asn Lys Leu Asp Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  20
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  20

Glu Val Leu Glu Ala Trp Asp Glu Ile Asp Arg Leu Pro Asn Leu Thr 
1               5                   10                  15      


Ile Glu Gln Trp Leu Ala Phe Ile Asn Lys Leu Asp Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Glu Ser Ser Gln 
        35                  40                  45              


<210>  21
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  21

Glu Val Leu Glu Ala Trp Asp Glu Ile Asp Arg Leu Pro Asn Leu Thr 
1               5                   10                  15      


Ile Glu Gln Trp Leu Ala Phe Ile Asn Lys Leu Asp Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  22
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  22

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  23
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  23

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  24
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  24

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Glu Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  25
<211>  108
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  25

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Asp Ser Gln Ala Pro Lys Val Glu Gly Ser Leu Ala 
    50                  55                  60                  


Glu Ala Lys Glu Ala Ala Asn Ala Glu Leu Asp Ser Tyr Gly Val Ser 
65                  70                  75                  80  


Asp Phe Tyr Lys Arg Leu Ile Asp Lys Ala Lys Thr Val Glu Gly Val 
                85                  90                  95      


Glu Ala Leu Lys Asp Ala Ile Leu Ala Ala Leu Pro 
            100                 105             


<210>  26
<211>  62
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered C5 binding Z variant

<400>  26

Ala Glu Ala Lys Tyr Ala Lys Glu Val Leu Glu Ala Trp Asp Glu Ile 
1               5                   10                  15      


Asp Arg Leu Pro Asn Leu Thr Ile Glu Gln Trp Leu Ala Phe Ile Asn 
            20                  25                  30          


Lys Leu Asp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys Val Asp Gly Ser 
    50                  55                  60          


<210>  27
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered HER2 binding Z variant

<400>  27

Ala Glu Ala Lys Tyr Ala Lys Glu Met Arg Asn Ala Tyr Trp Glu Ile 
1               5                   10                  15      


Ala Leu Leu Pro Asn Leu Thr Asn Gln Gln Lys Arg Ala Phe Ile Arg 
            20                  25                  30          


Lys Leu Tyr Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  28
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered HER2 binding Z variant

<400>  28

Ala Glu Ala Lys Tyr Ala Lys Glu Met Arg Asn Ala Tyr Trp Glu Ile 
1               5                   10                  15      


Ala Leu Leu Pro Asn Leu Thr Asn Gln Gln Lys Arg Ala Phe Ile Arg 
            20                  25                  30          


Lys Leu Tyr Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  29
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered HER2 binding Z variant

<400>  29

Ala Glu Ala Lys Tyr Ala Lys Glu Met Arg Asn Ala Tyr Trp Glu Ile 
1               5                   10                  15      


Ala Leu Leu Pro Asn Leu Thr Asn Gln Gln Lys Arg Ala Phe Ile Arg 
            20                  25                  30          


Lys Leu Tyr Arg Gln Pro Glu Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  30
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered PDGFRbeta binding Z variant

<400>  30

Ala Glu Ala Lys Tyr Ala Lys Glu Leu Ile Glu Ala Ala Ala Glu Ile 
1               5                   10                  15      


Asp Ala Leu Pro Asn Leu Thr Arg Arg Gln Trp Asn Ala Phe Ile Lys 
            20                  25                  30          


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


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  31
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered PDGFRbeta binding Z variant

<400>  31

Ala Glu Ala Lys Tyr Ala Lys Glu Leu Ile Glu Ala Ala Ala Glu Ile 
1               5                   10                  15      


Asp Ala Leu Pro Asn Leu Thr Arg Arg Gln Trp Asn Ala Phe Ile Lys 
            20                  25                  30          


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


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  32
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered PDGFRbeta binding Z variant

<400>  32

Ala Glu Ala Lys Tyr Ala Lys Glu Leu Ile Glu Ala Ala Ala Glu Ile 
1               5                   10                  15      


Asp Ala Leu Pro Asn Leu Thr Arg Arg Gln Trp Asn Ala Phe Ile Lys 
            20                  25                  30          


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


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  33
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered FcRn binding Z variant

<400>  33

Ala Glu Ala Lys Tyr Ala Lys Glu Gln Asp Ala Ala Ala His Glu Ile 
1               5                   10                  15      


Arg Trp Leu Pro Asn Leu Thr Phe Asp Gln Arg Val Ala Phe Ile His 
            20                  25                  30          


Lys Leu Ala Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  34
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered FcRn binding Z variant

<400>  34

Ala Glu Ala Lys Tyr Ala Lys Glu Gln Asp Ala Ala Ala His Glu Ile 
1               5                   10                  15      


Arg Trp Leu Pro Asn Leu Thr Phe Asp Gln Arg Val Ala Phe Ile His 
            20                  25                  30          


Lys Leu Ala Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  35
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered FcRn binding Z variant

<400>  35

Ala Glu Ala Lys Tyr Ala Lys Glu Gln Asp Ala Ala Ala His Glu Ile 
1               5                   10                  15      


Arg Trp Leu Pro Asn Leu Thr Phe Asp Gln Arg Val Ala Phe Ile His 
            20                  25                  30          


Lys Leu Ala Arg Gln Pro Glu Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  36
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  36

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


Lys Leu Trp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  37
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  37

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


Lys Leu Trp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  38
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  38

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


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


Lys Lys Leu Ser Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  39
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  39

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


Lys Leu Trp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Asn Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  40
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  40

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


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


Lys Lys Leu Asn Glu Ser Gln Ala Pro Lys 
    50                  55              


<210>  41
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  41

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


Lys Leu Trp Asp Asp Pro Ser Gln Ser Ser Glu Leu Leu Ser Glu Ala 
        35                  40                  45              


Lys Lys Leu Ser Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  42
<211>  58
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  42

Ala Glu Ala Lys Tyr Ala Lys Glu Asn Leu Phe Ala Gly Trp Glu Ile 
1               5                   10                  15      


Ser Asp Leu Pro Asn Leu Thr Asp Tyr Gln Arg Asn Ala Phe Ile Tyr 
            20                  25                  30          


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


Lys Lys Leu Ser Asp Ser Gln Ala Pro Lys 
    50                  55              


<210>  43
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered HER2 binding Z variant

<400>  43

Glu Met Arg Asn Ala Tyr Trp Glu Ile Ala Leu Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asn Gln Gln Lys Arg Ala Phe Ile Arg Lys Leu Tyr Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  44
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered HER2 binding Z variant

<400>  44

Glu Met Arg Asn Ala Tyr Trp Glu Ile Ala Leu Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asn Gln Gln Lys Arg Ala Phe Ile Arg Lys Leu Tyr Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  45
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered PDGFRbeta binding Z variant

<400>  45

Glu Leu Ile Glu Ala Ala Ala Glu Ile Asp Ala Leu Pro Asn Leu Thr 
1               5                   10                  15      


Arg Arg Gln Trp Asn Ala Phe Ile Lys Lys Leu Val Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  46
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered PDGFRbeta binding Z variant

<400>  46

Glu Leu Ile Glu Ala Ala Ala Glu Ile Asp Ala Leu Pro Asn Leu Thr 
1               5                   10                  15      


Arg Arg Gln Trp Asn Ala Phe Ile Lys Lys Leu Val Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  47
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered FcRn binding Z variant

<400>  47

Glu Gln Asp Ala Ala Ala His Glu Ile Arg Trp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Phe Asp Gln Arg Val Ala Phe Ile His Lys Leu Ala Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  48
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered FcRn binding Z variant

<400>  48

Glu Gln Asp Ala Ala Ala His Glu Ile Arg Trp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Phe Asp Gln Arg Val Ala Phe Ile His Lys Leu Ala Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  49
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  49

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  50
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  50

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Glu Ser Gln 
        35                  40                  45              


<210>  51
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  51

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Asn Glu Ser Gln 
        35                  40                  45              


<210>  52
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  52

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Asn Glu Ser Gln 
        35                  40                  45              


<210>  53
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  53

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Asp Asp Pro Ser 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Asp Ser Gln 
        35                  40                  45              


<210>  54
<211>  48
<212>  PRT
<213>  ARTIFICIAL SEQUENCE

<220>
<223>  Engineered CAIX binding Z variant

<400>  54

Glu Asn Leu Phe Ala Gly Trp Glu Ile Ser Asp Leu Pro Asn Leu Thr 
1               5                   10                  15      


Asp Tyr Gln Arg Asn Ala Phe Ile Tyr Lys Leu Trp Arg Gln Pro Glu 
            20                  25                  30          


Gln Ser Ser Glu Leu Leu Ser Glu Ala Lys Lys Leu Ser Asp Ser Gln 
        35                  40                  45              


