                         SEQUENCE LISTING

<110>  Eli Lilly and Company
 
<120>  INCRETIN ANALOGS AND USES THEREOF

<130>  P22622

<160>  16    

<170>  PatentIn version 3.5

<210>  1
<211>  42
<212>  PRT
<213>  Homo sapiens

<400>  1

Tyr Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 
1               5                   10                  15      


Ile His Gln Gln Asp Phe Val Asn Trp Leu Leu Ala Gln Lys Gly Lys 
            20                  25                  30          


Lys Asn Asp Trp Lys His Asn Ile Thr Gln 
        35                  40          


<210>  2
<211>  30
<212>  PRT
<213>  Homo sapiens


<220>
<221>  MOD_RES
<222>  (30)..(30)
<223>  AMIDATION

<400>  2

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


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


<210>  3
<211>  29
<212>  PRT
<213>  Homo sapiens

<400>  3

His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 
1               5                   10                  15      


Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr 
            20                  25                  


<210>  4
<211>  37
<212>  PRT
<213>  Homo sapiens

<400>  4

His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 
1               5                   10                  15      


Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr Lys Arg Asn 
            20                  25                  30          


Arg Asn Asn Ile Ala 
        35          


<210>  5
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (10)..(10)
<223>  Xaa at position 10 is Y or 4Pal

<220>
<221>  MISC_FEATURE
<222>  (13)..(13)
<223>  Xaa at position 13 is L or alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MISC_FEATURE
<222>  (17)..(17)
<223>  Xaa at position 17 is any amino acid with a functional group 
       available for conjugation

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is 4Pal, Iva, or alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (21)..(21)
<223>  Xaa at position 21 is A or Aib

<220>
<221>  MISC_FEATURE
<222>  (24)..(24)
<223>  Xaa at position 24 is E or D-Glu

<220>
<221>  MISC_FEATURE
<222>  (25)..(25)
<223>  Xaa at position 25 is Y or alpha-MeY

<220>
<221>  MISC_FEATURE
<222>  (39)..(39)
<223>  Xaa at position 39 is E or S

<400>  5

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Xaa Ser Ile Xaa Leu Asp Xaa 
1               5                   10                  15      


Xaa Ala Gln Xaa Xaa Phe Ile Xaa Xaa Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Xaa 
        35                  


<210>  6
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is 4Pal

<400>  6

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Tyr Ser Ile Leu Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Ala Phe Ile Glu Tyr Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Glu 
        35                  


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

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (13)..(13)
<223>  Xaa at position 13 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is Iva

<220>
<221>  MISC_FEATURE
<222>  (25)..(25)
<223>  Xaa at position 25 is alpha-MeY

<400>  7

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Tyr Ser Ile Xaa Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Ala Phe Ile Glu Xaa Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Ser 
        35                  


<210>  8
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (10)..(10)
<223>  Xaa at position 10 is 4Pal

<220>
<221>  MISC_FEATURE
<222>  (13)..(13)
<223>  Xaa at position 13 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (21)..(21)
<223>  Xaa at position 21 is Aib

<220>
<221>  MISC_FEATURE
<222>  (24)..(24)
<223>  Xaa at position 24 is D-Glu

<220>
<221>  MISC_FEATURE
<222>  (25)..(25)
<223>  Xaa at position 25 is alpha-MeY

<400>  8

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Xaa Ser Ile Xaa Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Xaa Phe Ile Xaa Xaa Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Ser 
        35                  


<210>  9
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MOD_RES
<222>  (17)..(17)
<223>  K at position 17 is chemically modified by conjugation of the 
       epsilon-amino group of the K side chain with 
       (2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)-(gamma-Glu)-CO-(CH2)18-CO2
       H

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is 4Pal

<220>
<221>  MOD_RES
<222>  (39)..(39)
<223>  Glutamic acid at position 39 is amidated

<400>  9

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Tyr Ser Ile Leu Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Ala Phe Ile Glu Tyr Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Glu 
        35                  


<210>  10
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alpha-MeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (13)..(13)
<223>  Xaa at position 13 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MOD_RES
<222>  (17)..(17)
<223>  K at position 17 is chemically modified by conjugation of the 
       epsilon-amino group of the K side chain with 
       (2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)-(gamma-Glu)-CO-(CH2)18-CO2
       H

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is Iva

<220>
<221>  MISC_FEATURE
<222>  (25)..(25)
<223>  Xaa at position 25 is alpha-MeY

<220>
<221>  MOD_RES
<222>  (39)..(39)
<223>  Ser at position 39 is amidated

<400>  10

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Tyr Ser Ile Xaa Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Ala Phe Ile Glu Xaa Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Ser 
        35                  


<210>  11
<211>  39
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is Aib

<220>
<221>  MISC_FEATURE
<222>  (6)..(6)
<223>  Xaa at position 6 is alphaMeF(2F)

<220>
<221>  MISC_FEATURE
<222>  (10)..(10)
<223>  Xaa at position 10 is 4Pal

<220>
<221>  MISC_FEATURE
<222>  (13)..(13)
<223>  Xaa at position 13 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (16)..(16)
<223>  Xaa at position 16 is Orn

<220>
<221>  MOD_RES
<222>  (17)..(17)
<223>  K at position 17 is chemically modified by conjugation of the 
       epsilon-amino group of the K side chain with 
       (2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)-(gamma-Glu)-CO-(CH2)18-CO2
       H

<220>
<221>  MISC_FEATURE
<222>  (20)..(20)
<223>  Xaa at position 20 is alpha-MeL

<220>
<221>  MISC_FEATURE
<222>  (21)..(21)
<223>  Xaa at position 21 is Aib

<220>
<221>  MISC_FEATURE
<222>  (24)..(24)
<223>  Xaa at position 24 is D-Glu

<220>
<221>  MISC_FEATURE
<222>  (25)..(25)
<223>  Xaa at position 25 is alpha-MeY

<220>
<221>  MISC_FEATURE
<222>  (39)..(39)
<223>  Ser at position 39 is amidated

<400>  11

Tyr Xaa Gln Gly Thr Xaa Thr Ser Asp Xaa Ser Ile Xaa Leu Asp Xaa 
1               5                   10                  15      


Lys Ala Gln Xaa Xaa Phe Ile Xaa Xaa Leu Leu Glu Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Glu Pro Pro Pro Ser 
        35                  


<210>  12
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct

<400>  12

Gly Pro Ser Ser Gly Glu Pro Pro Pro Glu 
1               5                   10  


<210>  13
<211>  10
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic Construct

<400>  13

Gly Pro Ser Ser Gly Glu Pro Pro Pro Ser 
1               5                   10  


<210>  14
<211>  466
<212>  PRT
<213>  Homo sapiens

<400>  14

Met Thr Thr Ser Pro Ile Leu Gln Leu Leu Leu Arg Leu Ser Leu Cys 
1               5                   10                  15      


Gly Leu Leu Leu Gln Arg Ala Glu Thr Gly Ser Lys Gly Gln Thr Ala 
            20                  25                  30          


Gly Glu Leu Tyr Gln Arg Trp Glu Arg Tyr Arg Arg Glu Cys Gln Glu 
        35                  40                  45              


Thr Leu Ala Ala Ala Glu Pro Pro Ser Gly Leu Ala Cys Asn Gly Ser 
    50                  55                  60                  


Phe Asp Met Tyr Val Cys Trp Asp Tyr Ala Ala Pro Asn Ala Thr Ala 
65                  70                  75                  80  


Arg Ala Ser Cys Pro Trp Tyr Leu Pro Trp His His His Val Ala Ala 
                85                  90                  95      


Gly Phe Val Leu Arg Gln Cys Gly Ser Asp Gly Gln Trp Gly Leu Trp 
            100                 105                 110         


Arg Asp His Thr Gln Cys Glu Asn Pro Glu Lys Asn Glu Ala Phe Leu 
        115                 120                 125             


Asp Gln Arg Leu Ile Leu Glu Arg Leu Gln Val Met Tyr Thr Val Gly 
    130                 135                 140                 


Tyr Ser Leu Ser Leu Ala Thr Leu Leu Leu Ala Leu Leu Ile Leu Ser 
145                 150                 155                 160 


Leu Phe Arg Arg Leu His Cys Thr Arg Asn Tyr Ile His Ile Asn Leu 
                165                 170                 175     


Phe Thr Ser Phe Met Leu Arg Ala Ala Ala Ile Leu Ser Arg Asp Arg 
            180                 185                 190         


Leu Leu Pro Arg Pro Gly Pro Tyr Leu Gly Asp Gln Ala Leu Ala Leu 
        195                 200                 205             


Trp Asn Gln Ala Leu Ala Ala Cys Arg Thr Ala Gln Ile Val Thr Gln 
    210                 215                 220                 


Tyr Cys Val Gly Ala Asn Tyr Thr Trp Leu Leu Val Glu Gly Val Tyr 
225                 230                 235                 240 


Leu His Ser Leu Leu Val Leu Val Gly Gly Ser Glu Glu Gly His Phe 
                245                 250                 255     


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


Pro Trp Val Ile Val Arg Tyr Leu Tyr Glu Asn Thr Gln Cys Trp Glu 
        275                 280                 285             


Arg Asn Glu Val Lys Ala Ile Trp Trp Ile Ile Arg Thr Pro Ile Leu 
    290                 295                 300                 


Met Thr Ile Leu Ile Asn Phe Leu Ile Phe Ile Arg Ile Leu Gly Ile 
305                 310                 315                 320 


Leu Leu Ser Lys Leu Arg Thr Arg Gln Met Arg Cys Arg Asp Tyr Arg 
                325                 330                 335     


Leu Arg Leu Ala Arg Ser Thr Leu Thr Leu Val Pro Leu Leu Gly Val 
            340                 345                 350         


His Glu Val Val Phe Ala Pro Val Thr Glu Glu Gln Ala Arg Gly Ala 
        355                 360                 365             


Leu Arg Phe Ala Lys Leu Gly Phe Glu Ile Phe Leu Ser Ser Phe Gln 
    370                 375                 380                 


Gly Phe Leu Val Ser Val Leu Tyr Cys Phe Ile Asn Lys Glu Val Gln 
385                 390                 395                 400 


Ser Glu Ile Arg Arg Gly Trp His His Cys Arg Leu Arg Arg Ser Leu 
                405                 410                 415     


Gly Glu Glu Gln Arg Gln Leu Pro Glu Arg Ala Phe Arg Ala Leu Pro 
            420                 425                 430         


Ser Gly Ser Gly Pro Gly Glu Val Pro Thr Ser Arg Gly Leu Ser Ser 
        435                 440                 445             


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


Tyr Cys 
465     


<210>  15
<211>  463
<212>  PRT
<213>  Homo sapiens

<400>  15

Met Ala Gly Ala Pro Gly Pro Leu Arg Leu Ala Leu Leu Leu Leu Gly 
1               5                   10                  15      


Met Val Gly Arg Ala Gly Pro Arg Pro Gln Gly Ala Thr Val Ser Leu 
            20                  25                  30          


Trp Glu Thr Val Gln Lys Trp Arg Glu Tyr Arg Arg Gln Cys Gln Arg 
        35                  40                  45              


Ser Leu Thr Glu Asp Pro Pro Pro Ala Thr Asp Leu Phe Cys Asn Arg 
    50                  55                  60                  


Thr Phe Asp Glu Tyr Ala Cys Trp Pro Asp Gly Glu Pro Gly Ser Phe 
65                  70                  75                  80  


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


Gln Gly His Val Tyr Arg Phe Cys Thr Ala Glu Gly Leu Trp Leu Gln 
            100                 105                 110         


Lys Asp Asn Ser Ser Leu Pro Trp Arg Asp Leu Ser Glu Cys Glu Glu 
        115                 120                 125             


Ser Lys Arg Gly Glu Arg Ser Ser Pro Glu Glu Gln Leu Leu Phe Leu 
    130                 135                 140                 


Tyr Ile Ile Tyr Thr Val Gly Tyr Ala Leu Ser Phe Ser Ala Leu Val 
145                 150                 155                 160 


Ile Ala Ser Ala Ile Leu Leu Gly Phe Arg His Leu His Cys Thr Arg 
                165                 170                 175     


Asn Tyr Ile His Leu Asn Leu Phe Ala Ser Phe Ile Leu Arg Ala Leu 
            180                 185                 190         


Ser Val Phe Ile Lys Asp Ala Ala Leu Lys Trp Met Tyr Ser Thr Ala 
        195                 200                 205             


Ala Gln Gln His Gln Trp Asp Gly Leu Leu Ser Tyr Gln Asp Ser Leu 
    210                 215                 220                 


Ser Cys Arg Leu Val Phe Leu Leu Met Gln Tyr Cys Val Ala Ala Asn 
225                 230                 235                 240 


Tyr Tyr Trp Leu Leu Val Glu Gly Val Tyr Leu Tyr Thr Leu Leu Ala 
                245                 250                 255     


Phe Ser Val Leu Ser Glu Gln Trp Ile Phe Arg Leu Tyr Val Ser Ile 
            260                 265                 270         


Gly Trp Gly Val Pro Leu Leu Phe Val Val Pro Trp Gly Ile Val Lys 
        275                 280                 285             


Tyr Leu Tyr Glu Asp Glu Gly Cys Trp Thr Arg Asn Ser Asn Met Asn 
    290                 295                 300                 


Tyr Trp Leu Ile Ile Arg Leu Pro Ile Leu Phe Ala Ile Gly Val Asn 
305                 310                 315                 320 


Phe Leu Ile Phe Val Arg Val Ile Cys Ile Val Val Ser Lys Leu Lys 
                325                 330                 335     


Ala Asn Leu Met Cys Lys Thr Asp Ile Lys Cys Arg Leu Ala Lys Ser 
            340                 345                 350         


Thr Leu Thr Leu Ile Pro Leu Leu Gly Thr His Glu Val Ile Phe Ala 
        355                 360                 365             


Phe Val Met Asp Glu His Ala Arg Gly Thr Leu Arg Phe Ile Lys Leu 
    370                 375                 380                 


Phe Thr Glu Leu Ser Phe Thr Ser Phe Gln Gly Leu Met Val Ala Ile 
385                 390                 395                 400 


Leu Tyr Cys Phe Val Asn Asn Glu Val Gln Leu Glu Phe Arg Lys Ser 
                405                 410                 415     


Trp Glu Arg Trp Arg Leu Glu His Leu His Ile Gln Arg Asp Ser Ser 
            420                 425                 430         


Met Lys Pro Leu Lys Cys Pro Thr Ser Ser Leu Ser Ser Gly Ala Thr 
        435                 440                 445             


Ala Gly Ser Ser Met Tyr Thr Ala Thr Cys Gln Ala Ser Cys Ser 
    450                 455                 460             


<210>  16
<211>  476
<212>  PRT
<213>  Homo sapiens

<400>  16

Met Pro Pro Cys Gln Pro Gln Arg Pro Leu Leu Leu Leu Leu Leu Leu 
1               5                   10                  15      


Leu Ala Cys Gln Pro Gln Val Pro Ser Ala Gln Val Met Asp Phe Leu 
            20                  25                  30          


Phe Glu Lys Trp Lys Leu Tyr Gly Asp Gln Cys His His Asn Leu Ser 
        35                  40                  45              


Leu Leu Pro Pro Pro Thr Leu Val Cys Asn Arg Thr Phe Asp Lys Tyr 
    50                  55                  60                  


Ser Cys Trp Pro Asp Thr Pro Ala Asn Thr Thr Ala Asn Ile Ser Cys 
65                  70                  75                  80  


Pro Trp Tyr Leu Pro Trp His His Lys Val Gln His Arg Phe Val Phe 
                85                  90                  95      


Lys Arg Cys Gly Pro Asp Gly Gln Trp Val Arg Gly Pro Arg Gly Gln 
            100                 105                 110         


Pro Trp Arg Asp Ala Ser Gln Cys Gln Met Asp Gly Glu Glu Ile Glu 
        115                 120                 125             


Val Gln Lys Glu Val Ala Lys Met Tyr Ser Ser Phe Gln Val Met Tyr 
    130                 135                 140                 


Thr Val Gly Tyr Ser Leu Ser Leu Gly Ala Leu Leu Leu Ala Leu Ala 
145                 150                 155                 160 


Ile Leu Gly Gly Leu Ser Lys Leu His Cys Thr Arg Asn Ala Ile His 
                165                 170                 175     


Ala Asn Leu Phe Ala Ser Phe Val Leu Lys Ala Ser Ser Val Leu Val 
            180                 185                 190         


Ile Asp Gly Leu Leu Arg Thr Arg Tyr Ser Gln Lys Ile Gly Asp Asp 
        195                 200                 205             


Leu Ser Val Ser Thr Trp Leu Ser Asp Gly Ala Val Ala Gly Cys Arg 
    210                 215                 220                 


Val Ala Ala Val Phe Met Gln Tyr Gly Ile Val Ala Asn Tyr Cys Trp 
225                 230                 235                 240 


Leu Leu Val Glu Gly Leu Tyr Leu His Asn Leu Leu Gly Leu Ala Thr 
                245                 250                 255     


Leu Pro Glu Arg Ser Phe Phe Ser Leu Tyr Leu Gly Ile Gly Trp Gly 
            260                 265                 270         


Ala Pro Met Leu Phe Val Val Pro Trp Ala Val Val Lys Cys Leu Phe 
        275                 280                 285             


Glu Asn Val Gln Cys Trp Thr Ser Asn Asp Asn Met Gly Phe Trp Trp 
    290                 295                 300                 


Ile Leu Arg Phe Pro Val Phe Leu Ala Ile Leu Ile Asn Phe Phe Ile 
305                 310                 315                 320 


Phe Val Arg Ile Val Gln Leu Leu Val Ala Lys Leu Arg Ala Arg Gln 
                325                 330                 335     


Met His His Thr Asp Tyr Lys Phe Arg Leu Ala Lys Ser Thr Leu Thr 
            340                 345                 350         


Leu Ile Pro Leu Leu Gly Val His Glu Val Val Phe Ala Phe Val Thr 
        355                 360                 365             


Asp Glu His Ala Gln Gly Thr Leu Arg Ser Ala Lys Leu Phe Phe Asp 
    370                 375                 380                 


Leu Phe Leu Ser Ser Phe Gln Gly Leu Leu Val Ala Val Leu Tyr Cys 
385                 390                 395                 400 


Phe Leu Asn Lys Glu Val Gln Ser Glu Leu Arg Arg Arg Trp His Arg 
                405                 410                 415     


Trp Arg Leu Gly Lys Val Leu Trp Glu Glu Arg Asn Thr Ser Asn His 
            420                 425                 430         


Arg Ala Ser Ser Ser Pro Gly His Gly Pro Pro Ser Lys Glu Leu Gln 
        435                 440                 445             


Phe Gly Arg Gly Gly Gly Ser Gln Asp Ser Ser Ala Glu Thr Pro Leu 
    450                 455                 460                 


Ala Gly Gly Leu Pro Arg Leu Ala Glu Ser Pro Phe 
465                 470                 475     


