                         SEQUENCE LISTING

<110>  Iconic Therapeutics, Inc.
       Migone, Thi-Sau
       Burian, Gabriela
       Greene, William
       Dornbush, Kirk
 
<120>  METHODS AND COMPOSITIONS FOR TREATING DISORDERS ASSOCIATED WITH PATHOLOGICAL NEOVASCULARIZATION

<130>  ICTH-005/01WO

<150>  62/254,918
<151>  2015-11-13

<150>  62/263,207
<151>  2015-12-04

<150>  62/263,203
<151>  2015-12-04

<160>  24    

<170>  PatentIn version 3.5

<210>  1
<211>  2072
<212>  DNA
<213>  Artificial Sequence

<220>
<223>  Human factor VII active site mutant immunoconjugate mRNA, 
       complete coding sequence

<400>  1
aagctttgca gagatttcat catggtctcc caggccctca ggctcctctg ccttctgctt       60

gggcttcagg gctgcctggc tgcagtcttc gtaacccagg aggaagccca cggcgtcctg      120

caccggcgcc ggcgcgccaa cgcgttcctg gaggagctgc ggccgggctc cctggagagg      180

gagtgcaagg aggagcagtg ctccttcgag gaggcccggg agatcttcaa ggacgcggag      240

aggacgaagc tgttctggat ttcttacagt gatggtgacc agtgtgcctc aagtccatgc      300

cagaatgggg gctcctgcaa ggaccagctc cagtcctata tctgcttctg cctccctgcc      360

ttcgagggcc ggaactgtga gacgcacaag gatgaccagc tgatctgtgt gaacgagaac      420

ggcggctgtg agcagtactg cagtgaccac acgggcacca agcgctcctg tcggtgccac      480

gaggggtact ctctgctggc agacggggtg tcctgcacac ccacagttga atatccatgt      540

ggaaaaatac ctattctaga aaaaagaaat gccagcaagc cccaagggcg aattgtgggg      600

ggcaaggtgt gccccaaagg ggagtgtcca tggcaggtcc tgttgttggt gaatggagct      660

cagttgtgtg gggggaccct gatcaacacc atctgggtgg tctccgcggc ccactgtttc      720

gacaaaatca agaactggag gaacctgatc gcggtgctcg gggagcacga cctcagcgag      780

cacgacgggg atgagcagag ccggcgggtg gcgcaggtca tcatccccag cacgtacgtc      840

ccgggcacca ccaaccacga catcgcgctg ctccgcctgc accagcccgt ggtcctcact      900

gaccatgtgg tgcccctctg cctgcccgaa cggacgttct ctgagaggac gctggccttc      960

gtgcgcttct cattggtcag cggctggggc cagctgctgg accgtggcgc cacggccctg     1020

gagctcatgg tcctcaacgt gccccggctg atgacccagg actgcctgca gcagtcacgg     1080

aaggtgggag actccccaaa tatcacggag tacatgttct gtgccggcta ctcggatggc     1140

agcaaggact cctgcgcggg ggacagtgga ggcccacatg ccacccacta ccggggcacg     1200

tggtacctga cgggcatcgt cagctggggc cagggctgcg caaccgtggg ccactttggg     1260

gtgtacacca gggtctccca gtacatcgag tggctgcaaa agctcatgcg ctcagagcca     1320

cgcccaggag tcctcctgcg agccccattt cccggatccg cagagcccaa atcttgtgac     1380

aaaactcaca catgcccacc gtgcccagca cctgaactcc tggggggacc gtcagtcttc     1440

ctcttccccc caaaacccaa ggacaccctc atgatctccc ggacccctga ggtcacatgc     1500

gtggtggtgg acgtgagcca cgaagaccct gaggtcaagt tcaactggta cgtggacggc     1560

gtggaggtgc ataatgccaa gacaaagccg cgggaggagc agtacaacag cacgtaccgt     1620

gtggtcagcg tcctcaccgt cctgcaccag gactggctga atggcaagga gtacaagtgc     1680

aaggtctcca acaaagccct cccagccccc atcgagaaaa ccatctccaa agccaaaggg     1740

cagccccgag aaccacaggt gtacaccctg cccccatccc gggatgagct gaccaagaac     1800

caggtcagcc tgacctgcct ggtcaaaggc ttctatccca gcgacatcgc cgtggagtgg     1860

gagagcaatg ggcagccgga gaacaactac aagaccacgc ctcccgtgct ggactccgac     1920

ggctccttct tcctctacag caagctcacc gtggacaaga gcaggtggca gcaggggaac     1980

gtcttctcat gctccgtgat gcatgaggct ctgcacaacc actacacgca gaagagcctc     2040

tccctgtctc cgggtaaatg ataagcggcc gc                                   2072


<210>  2
<211>  641
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Human factor VII mutant immunoconjugate AA sequence


<220>
<221>  MOD_RES
<222>  (6)..(6)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (7)..(7)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (14)..(14)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (16)..(16)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (19)..(19)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (20)..(20)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (25)..(25)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (26)..(26)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (29)..(29)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (34)..(34)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  CARBOHYD
<222>  (52)..(52)
<223>  May be site of O-glycosylation

<220>
<221>  CARBOHYD
<222>  (60)..(60)
<223>  May be site of O-glycosylation

<220>
<221>  CARBOHYD
<222>  (145)..(145)
<223>  May be site of N-glycosylation

<220>
<221>  CARBOHYD
<222>  (322)..(322)
<223>  May be site of N-glycosylation

<220>
<221>  CARBOHYD
<222>  (491)..(491)
<223>  May be site of N-glycosylation

<400>  2

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Lys Ser Cys Asp Lys 
                405                 410                 415     


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro 
            420                 425                 430         


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
        435                 440                 445             


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
    450                 455                 460                 


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
465                 470                 475                 480 


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


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
            500                 505                 510         


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
        515                 520                 525             


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


Leu Pro Pro Ser Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr 
545                 550                 555                 560 


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
                565                 570                 575     


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
            580                 585                 590         


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
        595                 600                 605             


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu 
    610                 615                 620                 


Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
625                 630                 635                 640 


Lys 
    


<210>  3
<211>  641
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Human factor VII mutant immunoconjugate AA sequence


<220>
<221>  MOD_RES
<222>  (6)..(6)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (7)..(7)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (14)..(14)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (16)..(16)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (19)..(19)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (20)..(20)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (25)..(25)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (26)..(26)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (29)..(29)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  MOD_RES
<222>  (34)..(34)
<223>  May be glutamic acid or a post translationally modified gamma 
       carboxy-glutamic acid (GLA)

<220>
<221>  CARBOHYD
<222>  (52)..(52)
<223>  May be site of O-glycosylation

<220>
<221>  CARBOHYD
<222>  (60)..(60)
<223>  May be site of O-glycosylation

<220>
<221>  CARBOHYD
<222>  (145)..(145)
<223>  May be site of N-glycosylation

<220>
<221>  CARBOHYD
<222>  (322)..(322)
<223>  May be site of N-glycosylation

<220>
<221>  CARBOHYD
<222>  (491)..(491)
<223>  May be site of N-glycosylation

<400>  3

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Lys Gly Asp Ala Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Lys Ser Cys Asp Lys 
                405                 410                 415     


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro 
            420                 425                 430         


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
        435                 440                 445             


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
    450                 455                 460                 


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
465                 470                 475                 480 


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


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
            500                 505                 510         


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
        515                 520                 525             


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


Leu Pro Pro Ser Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr 
545                 550                 555                 560 


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
                565                 570                 575     


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
            580                 585                 590         


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
        595                 600                 605             


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu 
    610                 615                 620                 


Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
625                 630                 635                 640 


Lys 
    


<210>  4
<211>  2057
<212>  DNA
<213>  Artificial Sequence

<220>
<223>  Coding sequence for human factor VII mutant immunoconjugate AA 
       sequence

<400>  4
ggatccacca tggtgtcaca agccctccgc ctgctctgcc tccttctcgg acttcaagga       60

tgtctggccg cagtgttcgt gactcaagaa gaggcccacg gggtgctgca ccggaggcgc      120

cgcgcgaacg cctttctgga ggagctgcgg ccaggctcgc tggaaagaga gtgcaaagag      180

gagcaatgct ccttcgagga ggccagagaa attttcaagg acgccgaacg gactaagctg      240

ttttggatct catacagcga cggcgaccag tgtgccagca gcccgtgcca gaacggcggt      300

tcgtgcaagg accagctgca gtcctacatt tgtttctgcc tgccggcgtt cgaaggaaga      360

aactgtgaaa cccacaagga tgaccagctg atctgcgtga acgagaacgg aggctgcgaa      420

cagtactgct ccgaccacac ggggactaag aggagctgca gatgccatga gggctatagc      480

ctgctggccg acggggtgtc ctgcactccg actgtggaat acccgtgcgg aaagatcccc      540

atcctggaga agcggaacgc atccaagccc caaggacgaa ttgtcggcgg aaaggtctgc      600

cctaagggag agtgtccttg gcaagtgctc ctcttggtga acggagcgca gctttgcggc      660

ggaactctga tcaacaccat ctgggtggtg tcggcagctc actgctttga taagattaag      720

aactggcgga acctgatcgc ggtgcttggc gaacatgacc tgtccgaaca cgacggggac      780

gagcagtccc ggagagtggc ccaggtcatc attccatcca cctacgtgcc ggggaccaca      840

aaccacgaca tcgccttgct gcggctgcac cagccggtgg tccttaccga tcacgtcgtg      900

ccgctctgcc tgcccgagcg cacctttagc gagcgcaccc tggccttcgt gcgcttctcc      960

ctggtgtccg gctggggaca gctgctggac agaggcgcca ccgccctgga actgatggtg     1020

ctgaacgtgc cacggctcat gacccaagat tgtctgcagc agtcgcgcaa agtcggggat     1080

tcaccgaaca tcaccgagta catgttctgc gccggttact ccgatggatc gaaggactcg     1140

tgcgctggag actccggtgg accccatgct acccattatc gcggtacttg gtacctgact     1200

ggtattgtgt cctggggaca gggctgcgcc accgtgggac atttcggcgt gtacacaagg     1260

gtgtcacagt acatcgaatg gttgcagaag ctcatgcgca gcgaacctcg cccgggagtg     1320

ctcctgaggg cccctttccc cggaagcgct gagcctaaga gctgcgacaa gacccacact     1380

tgtccgccat gccccgcgcc cgaactgctg ggtggcccat ccgtgttcct gttcccgcct     1440

aagcccaagg acaccctgat gatttcgcgg acccccgaag tgacttgcgt ggtggtggac     1500

gtcagccacg aagatccgga agtcaagttc aattggtacg tggatggcgt cgaagtccat     1560

aacgccaaga ccaagccccg cgaggagcag tacaattcca cttaccgggt ggtgtccgtg     1620

ttgaccgtgt tgcaccagga ctggctgaac ggaaaggaat acaagtgcaa agtgtcgaat     1680

aaggccctcc cggccccgat cgagaaaacg atctccaagg ccaagggcca gcctcgggag     1740

ccccaggtct acaccttgcc gccgtcccgg gatgagctga ccaagaacca ggtgtcactc     1800

acctgtctcg tcaaggggtt ctacccttcc gacatcgccg tggaatggga gtcgaacggg     1860

cagccggaaa acaattacaa gaccactcct cctgtcctgg attccgacgg gtcattcttc     1920

ctgtactcaa agctgaccgt ggacaagagc agatggcaac agggcaacgt gttcagctgc     1980

tccgtgatgc acgaggccct gcacaaccac tacacccaga agtccctgtc cctctctccc     2040

ggaaaatgag cggccgc                                                    2057


<210>  5
<211>  2057
<212>  DNA
<213>  Artificial Sequence

<220>
<223>  Coding sequence for human factor VII mutant immunoconjugate AA 
       sequence

<400>  5
tctagaccac catggtgtca caagccctcc gcctgctctg cctccttctc ggacttcaag       60

gatgtctggc cgcagtgttc gtgactcaag aagaggccca cggggtgctg caccggaggc      120

gccgcgcgaa cgcctttctg gaggagctgc ggccaggctc gctggaaaga gagtgcaaag      180

aggagcaatg ctccttcgag gaggccagag aaattttcaa ggacgccgaa cggactaagc      240

tgttttggat ctcatacagc gacggcgacc agtgtgccag cagcccgtgc cagaacggcg      300

gttcgtgcaa ggaccagctg cagtcctaca tttgtttctg cctgccggcg ttcgaaggaa      360

gaaactgtga aacccacaag gatgaccagc tgatctgcgt gaacgagaac ggaggctgcg      420

aacagtactg ctccgaccac acggggacta agaggagctg cagatgccat gagggctata      480

gcctgctggc cgacggggtg tcctgcactc cgactgtgga atacccgtgc ggaaagatcc      540

ccatcctgga gaagcggaac gcatccaagc cccaaggacg aattgtcggc ggaaaggtct      600

gccctaaggg agagtgtcct tggcaagtgc tcctcttggt gaacggagcg cagctttgcg      660

gcggaactct gatcaacacc atctgggtgg tgtcggcagc tcactgcttt gataagatta      720

agaactggcg gaacctgatc gcggtgcttg gcgaacatga cctgtccgaa cacgacgggg      780

acgagcagtc ccggagagtg gcccaggtca tcattccatc cacctacgtg ccggggacca      840

caaaccacga catcgccttg ctgcggctgc accagccggt ggtccttacc gatcacgtcg      900

tgccgctctg cctgcccgag cgcaccttta gcgagcgcac cctggccttc gtgcgcttct      960

ccctggtgtc cggctgggga cagctgctgg acagaggcgc caccgccctg gaactgatgg     1020

tgctgaacgt gccacggctc atgacccaag attgtctgca gcagtcgcgc aaagtcgggg     1080

attcaccgaa catcaccgag tacatgttct gcgccggtta ctccgatgga tcgaaggact     1140

cgtgcgctgg agactccggt ggaccccatg ctacccatta tcgcggtact tggtacctga     1200

ctggtattgt gtcctgggga cagggctgcg ccaccgtggg acatttcggc gtgtacacaa     1260

gggtgtcaca gtacatcgaa tggttgcaga agctcatgcg cagcgaacct cgcccgggag     1320

tgctcctgag ggcccctttc cccggaagcg ctgagcctaa gagctgcgac aagacccaca     1380

cttgtccgcc atgccccgcg cccgaactgc tgggtggccc atccgtgttc ctgttcccgc     1440

ctaagcccaa ggacaccctg atgatttcgc ggacccccga agtgacttgc gtggtggtgg     1500

acgtcagcca cgaagatccg gaagtcaagt tcaattggta cgtggatggc gtcgaagtcc     1560

ataacgccaa gaccaagccc cgcgaggagc agtacaattc cacttaccgg gtggtgtccg     1620

tgttgaccgt gttgcaccag gactggctga acggaaagga atacaagtgc aaagtgtcga     1680

ataaggccct cccggccccg atcgagaaaa cgatctccaa ggccaagggc cagcctcggg     1740

agccccaggt ctacaccttg ccgccgtccc gggatgagct gaccaagaac caggtgtcac     1800

tcacctgtct cgtcaagggg ttctaccctt ccgacatcgc cgtggaatgg gagtcgaacg     1860

ggcagccgga aaacaattac aagaccactc ctcctgtcct ggattccgac gggtcattct     1920

tcctgtactc aaagctgacc gtggacaaga gcagatggca acagggcaac gtgttcagct     1980

gctccgtgat gcacgaggcc ctgcacaacc actacaccca gaagtccctg tccctctctc     2040

ccggaaaatg aaccggt                                                    2057


<210>  6
<211>  29
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Hinge Region

<400>  6

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


Cys Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro 
            20                  25                  


<210>  7
<211>  29
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Mutated Hinge/Linker Region

<400>  7

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


Ser Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro 
            20                  25                  


<210>  8
<211>  29
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Mutated Hinge/Linker Region

<400>  8

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Ala Ser 
1               5                   10                  15      


Ser Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro 
            20                  25                  


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

<220>
<223>  Mutated Hinge Region

<400>  9

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Ser Ala Asp Lys Thr His 
1               5                   10                  15      


Thr Cys Pro Pro Cys Pro Ala Pro 
            20                  


<210>  10
<211>  25
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Mutated Hinge Region

<400>  10

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Gly Ser Ser Asp Lys Thr 
1               5                   10                  15      


His Thr Cys Pro Pro Cys Pro Ala Pro 
            20                  25  


<210>  11
<211>  641
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Immunocongugate comprising mutated hinge region

<400>  11

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Lys Ser Ser Asp Lys 
                405                 410                 415     


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro 
            420                 425                 430         


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
        435                 440                 445             


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
    450                 455                 460                 


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
465                 470                 475                 480 


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


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
            500                 505                 510         


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
        515                 520                 525             


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


Leu Pro Pro Ser Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr 
545                 550                 555                 560 


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
                565                 570                 575     


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
            580                 585                 590         


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
        595                 600                 605             


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu 
    610                 615                 620                 


Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
625                 630                 635                 640 


Lys 
    


<210>  12
<211>  641
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Immunoconjugate comprising mutated hinge region

<400>  12

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Ala Ser Ser Asp Lys 
                405                 410                 415     


Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro 
            420                 425                 430         


Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser 
        435                 440                 445             


Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp 
    450                 455                 460                 


Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn 
465                 470                 475                 480 


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


Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu 
            500                 505                 510         


Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys 
        515                 520                 525             


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


Leu Pro Pro Ser Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr 
545                 550                 555                 560 


Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu 
                565                 570                 575     


Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu 
            580                 585                 590         


Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys 
        595                 600                 605             


Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu 
    610                 615                 620                 


Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly 
625                 630                 635                 640 


Lys 
    


<210>  13
<211>  636
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Immunocongugate comprising mutated hinge region

<400>  13

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Ser Ala Asp Lys Thr His Thr Cys Pro 
                405                 410                 415     


Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu Phe 
            420                 425                 430         


Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val 
        435                 440                 445             


Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val Lys Phe 
    450                 455                 460                 


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


Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr 
                485                 490                 495     


Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val 
            500                 505                 510         


Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys Ala 
        515                 520                 525             


Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Arg 
    530                 535                 540                 


Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly 
545                 550                 555                 560 


Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro 
                565                 570                 575     


Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly Ser 
            580                 585                 590         


Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln Gln 
        595                 600                 605             


Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His 
    610                 615                 620                 


Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
625                 630                 635     


<210>  14
<211>  637
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Immunocongjugate comprising mutated hinge region

<400>  14

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro Gly Gly Ser Ser Asp Lys Thr His Thr Cys 
                405                 410                 415     


Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu 
            420                 425                 430         


Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu 
        435                 440                 445             


Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val Lys 
    450                 455                 460                 


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


Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val Leu 
                485                 490                 495     


Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys 
            500                 505                 510         


Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys 
        515                 520                 525             


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


Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys 
545                 550                 555                 560 


Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln 
                565                 570                 575     


Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly 
            580                 585                 590         


Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln 
        595                 600                 605             


Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn 
    610                 615                 620                 


His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
625                 630                 635         


<210>  15
<211>  228
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  IgG Fc Region

<400>  15

Met Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu 
1               5                   10                  15      


Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu 
            20                  25                  30          


Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser 
        35                  40                  45              


His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu 
    50                  55                  60                  


Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr 
65                  70                  75                  80  


Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn 
                85                  90                  95      


Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro 
            100                 105                 110         


Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln 
        115                 120                 125             


Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val 
    130                 135                 140                 


Ser Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val 
145                 150                 155                 160 


Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro 
                165                 170                 175     


Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr 
            180                 185                 190         


Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val 
        195                 200                 205             


Met His Glu Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu 
    210                 215                 220                 


Ser Pro Gly Lys 
225             


<210>  16
<211>  406
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Human factor VII active site mutant

<400>  16

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu 
385                 390                 395                 400 


Leu Arg Ala Pro Phe Pro 
                405     


<210>  17
<211>  397
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens factor VII active site mutant amino acid sequence 
       (no hinge region)

<400>  17

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Ala Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro 
385                 390                 395         


<210>  18
<211>  397
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens factor VII active site mutant amino acid sequence 
       (no hinge region), with mutations S344A and A341K relative to 
       SEQ ID NO:17

<400>  18

Ala Asn Ala Phe Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu 
1               5                   10                  15      


Cys Lys Glu Glu Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys 
            20                  25                  30          


Asp Ala Glu Arg Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp 
        35                  40                  45              


Gln Cys Ala Ser Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln 
    50                  55                  60                  


Leu Gln Ser Tyr Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn 
65                  70                  75                  80  


Cys Glu Thr His Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly 
                85                  90                  95      


Gly Cys Glu Gln Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys 
            100                 105                 110         


Arg Cys His Glu Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr 
        115                 120                 125             


Pro Thr Val Glu Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg 
    130                 135                 140                 


Asn Ala Ser Lys Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro 
145                 150                 155                 160 


Lys Gly Glu Cys Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln 
                165                 170                 175     


Leu Cys Gly Gly Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala 
            180                 185                 190         


His Cys Phe Asp Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu 
        195                 200                 205             


Gly Glu His Asp Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg 
    210                 215                 220                 


Val Ala Gln Val Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn 
225                 230                 235                 240 


His Asp Ile Ala Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp 
                245                 250                 255     


His Val Val Pro Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr 
            260                 265                 270         


Leu Ala Phe Val Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu 
        275                 280                 285             


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


Leu Met Thr Gln Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser 
305                 310                 315                 320 


Pro Asn Ile Thr Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser 
                325                 330                 335     


Lys Asp Ser Cys Lys Gly Asp Ala Gly Gly Pro His Ala Thr His Tyr 
            340                 345                 350         


Arg Gly Thr Trp Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys 
        355                 360                 365             


Ala Thr Val Gly His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile 
    370                 375                 380                 


Glu Trp Leu Gln Lys Leu Met Arg Ser Glu Pro Arg Pro 
385                 390                 395         


<210>  19
<211>  244
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IgG Fc (with hinge region)

<400>  19

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


Cys Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu 
            20                  25                  30          


Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu 
        35                  40                  45              


Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser 
    50                  55                  60                  


His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu 
65                  70                  75                  80  


Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr 
                85                  90                  95      


Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn 
            100                 105                 110         


Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro 
        115                 120                 125             


Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln 
    130                 135                 140                 


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


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


Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro 
            180                 185                 190         


Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr 
        195                 200                 205             


Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val 
    210                 215                 220                 


Met His Glu Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu 
225                 230                 235                 240 


Ser Pro Gly Lys 
                


<210>  20
<211>  244
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IGG Fc (with hinge region), with ProtA 
       mutation

<400>  20

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


Cys Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu 
            20                  25                  30          


Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu 
        35                  40                  45              


Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser 
    50                  55                  60                  


His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu 
65                  70                  75                  80  


Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr 
                85                  90                  95      


Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn 
            100                 105                 110         


Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro 
        115                 120                 125             


Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln 
    130                 135                 140                 


Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val 
145                 150                 155                 160 


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


Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro 
            180                 185                 190         


Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr 
        195                 200                 205             


Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val 
    210                 215                 220                 


Met His Glu Ala Leu His Asn Arg Phe Thr Gln Lys Ser Leu Ser Leu 
225                 230                 235                 240 


Ser Pro Gly Lys 
                


<210>  21
<211>  244
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IGG Fc (with hinge region) comprising mutated
       hinge region of SEQ ID NO:7

<400>  21

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


Ser Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu 
            20                  25                  30          


Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu 
        35                  40                  45              


Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser 
    50                  55                  60                  


His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu 
65                  70                  75                  80  


Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr 
                85                  90                  95      


Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn 
            100                 105                 110         


Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro 
        115                 120                 125             


Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln 
    130                 135                 140                 


Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val 
145                 150                 155                 160 


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


Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro 
            180                 185                 190         


Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr 
        195                 200                 205             


Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val 
    210                 215                 220                 


Met His Glu Ala Leu His Asn Arg Phe Thr Gln Lys Ser Leu Ser Leu 
225                 230                 235                 240 


Ser Pro Gly Lys 
                


<210>  22
<211>  244
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IgG Fc (with hinge region) comprising mutated
       hinge region of SEQ ID NO:8

<400>  22

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Ser Ala Glu Pro Ala Ser 
1               5                   10                  15      


Ser Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu 
            20                  25                  30          


Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu 
        35                  40                  45              


Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser 
    50                  55                  60                  


His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu 
65                  70                  75                  80  


Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr 
                85                  90                  95      


Tyr Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn 
            100                 105                 110         


Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro 
        115                 120                 125             


Ile Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln 
    130                 135                 140                 


Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val 
145                 150                 155                 160 


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


Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro 
            180                 185                 190         


Pro Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr 
        195                 200                 205             


Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val 
    210                 215                 220                 


Met His Glu Ala Leu His Asn Arg Phe Thr Gln Lys Ser Leu Ser Leu 
225                 230                 235                 240 


Ser Pro Gly Lys 
                


<210>  23
<211>  239
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IgG Fc (with hinge region) comprising mutated
       hinge region of SEQ ID NO:9

<400>  23

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Ser Ala Asp Lys Thr His 
1               5                   10                  15      


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


Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr 
        35                  40                  45              


Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu 
    50                  55                  60                  


Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys 
65                  70                  75                  80  


Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser 
                85                  90                  95      


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


Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile 
        115                 120                 125             


Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro 
    130                 135                 140                 


Pro Ser Arg Asp Glu Leu Thr Lys Asn Gln Val Ser Leu Thr Cys Leu 
145                 150                 155                 160 


Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn 
                165                 170                 175     


Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser 
            180                 185                 190         


Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg 
        195                 200                 205             


Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu 
    210                 215                 220                 


His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
225                 230                 235                 


<210>  24
<211>  240
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Homo sapiens IgG Fc (with hinge region) comprising mutated
       hinge region of SEQ ID NO:10

<400>  24

Gly Val Leu Leu Arg Ala Pro Phe Pro Gly Gly Ser Ser Asp Lys Thr 
1               5                   10                  15      


His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser 
            20                  25                  30          


Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg 
        35                  40                  45              


Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro 
    50                  55                  60                  


Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala 
65                  70                  75                  80  


Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val 
                85                  90                  95      


Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr 
            100                 105                 110         


Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr 
        115                 120                 125             


Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu 
    130                 135                 140                 


Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys 
145                 150                 155                 160 


Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser 
                165                 170                 175     


Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp 
            180                 185                 190         


Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser 
        195                 200                 205             


Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala 
    210                 215                 220                 


Leu His Asn Arg Phe Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
225                 230                 235                 240 


