﻿               SEQUENCE LISTING

<110> DSM IP Assets B.V.

<120> ALPHA-AMYLASE VARIANTS

<130> 29253-WO-PCT

<160> 8

<170> BiSSAP 1.2

<210> 1
<211> 2160
<212> DNA
<213> Alicyclobacillus pohliae

<220> 
<221> source
<222> 1..2160
<223> /organism="Alicyclobacillus pohliae"
      /mol_type="unassigned DNA"

<400> 1
atgaaaaaga aaacgctttc attatttgtg ggactgatgc tgctcctcgg tcttctgttc      60

agcggttctc ttccgtacaa tccaaacgcc gctgaagcca gcagttccgc aagcgtcaaa     120

ggggacgtga tttaccagat tatcattgac cggttttacg atggggacac gacgaacaac     180

aatcctgcca aaagttatgg actttacgat cccaccaaat cgaagtggaa aatgtattgg     240

ggcggggatc tggagggggt tcgtcaaaaa cttccttatc ttaaacagct gggcgtaacg     300

acgatctggt tgtccccggt tttggacaat ctggatacac ttgcaggtac cgataacact     360

ggctatcacg gatactggac gcgcgatttt aaacagattg aggaacattt cgggaattgg     420

accacatttg acacgttggt caatgatgct caccaaaacg gaatcaaggt gattgtcgac     480

tttgtgccca atcattcaac tccttttaag gcaaacgatt ccacctttgc ggaaggcggc     540

gccctctacg acaacggaac ctatatgggc aattattttg atgacgcaac aaaagggtac     600

tttcaccata atggggacat cagcaactgg gacgaccggt acgaggcgca atggaaaaac     660

ttcacggatc cagccggttt ctcgcttgcc gatttgtcgc aggaaaatgg cacgattgct     720

caatacctga ccgatgcggc ggttcaatta gtagcacatg gagcggatgg tttgcggatt     780

gatgcggtga agcattttaa ttctgggttc tccaaatcgt tggctgataa actgtaccaa     840

aagaaagaca ttttcctagt gggggaatgg tacggagatg accccggagc agccaatcat     900

ttggaaaagg tccggtacgc caacaacagc ggtgtcaatg tgctggattt tgatctcaac     960

acggtgattc gaaatgtgtt cggtacattt acgcaaacga tgtacgatct taacaatatg    1020

gtgaaccaaa cggggaacga gtacaaatac aaagaaaatc taatcacatt tatcgataac    1080

catgatatgt cgagatttct tacggtaaat tcgaacaagg cgaatttgca ccaggcgctt    1140

gctttcattc tcacttcgcg gggaacgccc tccatctatt acggaaccga acaatacatg    1200

gcaggcggca atgacccgta caacaggggg atgatgccgg cgtttgatac gacaaccacc    1260

gcctttaaag aggtgtcaac tctggcgggg ttgcgcagga acaatgcagc gatccagtac    1320

ggcaccacca cccaacgttg gatcaacaat gatgtttaca tttatgagcg gaaatttttc    1380

aacgatgtcg tattggtggc catcaatcga aacacgcaat cctcctactc gatttccggt    1440

ttgcagactg ccttgccaaa tggcaactat gcggattatc tgtcagggct gttggggggg    1500

aacgggattt ccgtttccaa tggaagtgtc gcttcgttca cgcttgcgcc tggagccgtg    1560

tctgtttggc agtacagcac atccgcttca gcgccgcaaa tcggatcggt tgctccgaat    1620

atgggaattc cgggtaatgt ggtcacgatc gacgggaaag gttttggaac gacgcaggga    1680

accgtgacat ttggcggagt gacagcgact gtaaaatcct ggacatcaaa ccggattgaa    1740

gtgtacgtgc ccaacatggc cgccggtctg accgatgtaa aagtcaccgc gggtggagtt    1800

tccagcaatc tgtattctta caatattttg agtggaacgc agacatcggt tgtgtttact    1860

gtgaaaagtg ctcctccgac caacctgggg gataagattt acctgacggg caacataccg    1920

gaattgggaa attggagcac ggatacgagc ggagccgtta acaatgcgca agggcccctg    1980

ctcgcgccca attatccgga ttggttttat gtattcagcg ttccggcagg aaagacgatt    2040

caattcaagt ttttcatcaa gcgtgcggat ggaacgattc aatgggagaa tggttcgaac    2100

cacgtggcca caactcccac gggtgcaacc ggtaacatca ctgtcacgtg gcaaaactag    2160


<210> 2
<211> 686
<212> PRT
<213> Alicyclobacillus pohliae


<400> 2
Ser Ser Ser Ala Ser Val Lys Gly Asp Val Ile Tyr Gln Ile Ile Ile 
1               5                   10                  15      
Asp Arg Phe Tyr Asp Gly Asp Thr Thr Asn Asn Asn Pro Ala Lys Ser 
            20                  25                  30          
Tyr Gly Leu Tyr Asp Pro Thr Lys Ser Lys Trp Lys Met Tyr Trp Gly 
        35                  40                  45              
Gly Asp Leu Glu Gly Val Arg Gln Lys Leu Pro Tyr Leu Lys Gln Leu 
    50                  55                  60                  
Gly Val Thr Thr Ile Trp Leu Ser Pro Val Leu Asp Asn Leu Asp Thr 
65                  70                  75                  80  
Leu Ala Gly Thr Asp Asn Thr Gly Tyr His Gly Tyr Trp Thr Arg Asp 
                85                  90                  95      
Phe Lys Gln Ile Glu Glu His Phe Gly Asn Trp Thr Thr Phe Asp Thr 
            100                 105                 110         
Leu Val Asn Asp Ala His Gln Asn Gly Ile Lys Val Ile Val Asp Phe 
        115                 120                 125             
Val Pro Asn His Ser Thr Pro Phe Lys Ala Asn Asp Ser Thr Phe Ala 
    130                 135                 140                 
Glu Gly Gly Ala Leu Tyr Asp Asn Gly Thr Tyr Met Gly Asn Tyr Phe 
145                 150                 155                 160 
Asp Asp Ala Thr Lys Gly Tyr Phe His His Asn Gly Asp Ile Ser Asn 
                165                 170                 175     
Trp Asp Asp Arg Tyr Glu Ala Gln Trp Lys Asn Phe Thr Asp Pro Ala 
            180                 185                 190         
Gly Phe Ser Leu Ala Asp Leu Ser Gln Glu Asn Gly Thr Ile Ala Gln 
        195                 200                 205             
Tyr Leu Thr Asp Ala Ala Val Gln Leu Val Ala His Gly Ala Asp Gly 
    210                 215                 220                 
Leu Arg Ile Asp Ala Val Lys His Phe Asn Ser Gly Phe Ser Lys Ser 
225                 230                 235                 240 
Leu Ala Asp Lys Leu Tyr Gln Lys Lys Asp Ile Phe Leu Val Gly Glu 
                245                 250                 255     
Trp Tyr Gly Asp Asp Pro Gly Ala Ala Asn His Leu Glu Lys Val Arg 
            260                 265                 270         
Tyr Ala Asn Asn Ser Gly Val Asn Val Leu Asp Phe Asp Leu Asn Thr 
        275                 280                 285             
Val Ile Arg Asn Val Phe Gly Thr Phe Thr Gln Thr Met Tyr Asp Leu 
    290                 295                 300                 
Asn Asn Met Val Asn Gln Thr Gly Asn Glu Tyr Lys Tyr Lys Glu Asn 
305                 310                 315                 320 
Leu Ile Thr Phe Ile Asp Asn His Asp Met Ser Arg Phe Leu Thr Val 
                325                 330                 335     
Asn Ser Asn Lys Ala Asn Leu His Gln Ala Leu Ala Phe Ile Leu Thr 
            340                 345                 350         
Ser Arg Gly Thr Pro Ser Ile Tyr Tyr Gly Thr Glu Gln Tyr Met Ala 
        355                 360                 365             
Gly Gly Asn Asp Pro Tyr Asn Arg Gly Met Met Pro Ala Phe Asp Thr 
    370                 375                 380                 
Thr Thr Thr Ala Phe Lys Glu Val Ser Thr Leu Ala Gly Leu Arg Arg 
385                 390                 395                 400 
Asn Asn Ala Ala Ile Gln Tyr Gly Thr Thr Thr Gln Arg Trp Ile Asn 
                405                 410                 415     
Asn Asp Val Tyr Ile Tyr Glu Arg Lys Phe Phe Asn Asp Val Val Leu 
            420                 425                 430         
Val Ala Ile Asn Arg Asn Thr Gln Ser Ser Tyr Ser Ile Ser Gly Leu 
        435                 440                 445             
Gln Thr Ala Leu Pro Asn Gly Asn Tyr Ala Asp Tyr Leu Ser Gly Leu 
    450                 455                 460                 
Leu Gly Gly Asn Gly Ile Ser Val Ser Asn Gly Ser Val Ala Ser Phe 
465                 470                 475                 480 
Thr Leu Ala Pro Gly Ala Val Ser Val Trp Gln Tyr Ser Thr Ser Ala 
                485                 490                 495     
Ser Ala Pro Gln Ile Gly Ser Val Ala Pro Asn Met Gly Ile Pro Gly 
            500                 505                 510         
Asn Val Val Thr Ile Asp Gly Lys Gly Phe Gly Thr Thr Gln Gly Thr 
        515                 520                 525             
Val Thr Phe Gly Gly Val Thr Ala Thr Val Lys Ser Trp Thr Ser Asn 
    530                 535                 540                 
Arg Ile Glu Val Tyr Val Pro Asn Met Ala Ala Gly Leu Thr Asp Val 
545                 550                 555                 560 
Lys Val Thr Ala Gly Gly Val Ser Ser Asn Leu Tyr Ser Tyr Asn Ile 
                565                 570                 575     
Leu Ser Gly Thr Gln Thr Ser Val Val Phe Thr Val Lys Ser Ala Pro 
            580                 585                 590         
Pro Thr Asn Leu Gly Asp Lys Ile Tyr Leu Thr Gly Asn Ile Pro Glu 
        595                 600                 605             
Leu Gly Asn Trp Ser Thr Asp Thr Ser Gly Ala Val Asn Asn Ala Gln 
    610                 615                 620                 
Gly Pro Leu Leu Ala Pro Asn Tyr Pro Asp Trp Phe Tyr Val Phe Ser 
625                 630                 635                 640 
Val Pro Ala Gly Lys Thr Ile Gln Phe Lys Phe Phe Ile Lys Arg Ala 
                645                 650                 655     
Asp Gly Thr Ile Gln Trp Glu Asn Gly Ser Asn His Val Ala Thr Thr 
            660                 665                 670         
Pro Thr Gly Ala Thr Gly Asn Ile Thr Val Thr Trp Gln Asn 
        675                 680                 685     

<210> 3
<211> 100
<212> DNA
<213> Artificial Sequence

<220> 
<221> source
<222> 1..100
<223> /organism="Artificial Sequence"
      /note="Sets out a synthetic DNA fragment containing the PmeI
      restriction site, the amyQ terminator and the SphI and HindIII
      restriction sites"
      /mol_type="unassigned DNA"

<400> 3
gcatgcgttt aaacaaaaac acctccaagc tgagtgcggg tatcagcttg gaggtgcgtt     60

tattttttca gccgtatgac aaggtcggca tcagaagctt                          100


<210> 4
<211> 26
<212> DNA
<213> Artificial Sequence

<220> 
<221> source
<222> 1..26
<223> /organism="Artificial Sequence"
      /note="Sets out the 5’ sequence containing a ribosome binding
      site and PacI restriction site"
      /mol_type="unassigned DNA"

<400> 4
ttaattaaaa aaggagcgat ttacat                                         26


<210> 5
<211> 14
<212> DNA
<213> Artificial Sequence

<220> 
<221> source
<222> 1..14
<223> /organism="Artificial Sequence"
      /note="Sets out the 3’ sequence containing a double stop codon
      and PmeI restriction site"
      /mol_type="unassigned DNA"

<400> 5
taataagttt aaac                                                      14


<210> 6
<211> 2197
<212> DNA
<213> Artificial Sequence

<220> 
<221> source
<222> 1..2197
<223> /organism="Artificial Sequence"
      /note="Sets out the polynucleotide sequence from a synthetic DNA
      construct containing a PacI site, ribosome binding site, wild
      type DSM-AM sequence, double stop codon and PmeI restriction
      site"
      /mol_type="unassigned DNA"

<400> 6
ttaattaaaa aaggagcgat ttacatatga aaaagaaaac gctttcatta tttgtgggac      60

tgatgctgct cctcggtctt ctgttcagcg gttctcttcc gtacaatcca aacgccgctg     120

aagccagcag ttccgcaagc gtcaaagggg acgtgattta ccagattatc attgaccggt     180

tttacgatgg ggacacgacg aacaacaatc ctgccaaaag ttatggactt tacgatccca     240

ccaaatcgaa gtggaaaatg tattggggcg gggatctgga gggggttcgt caaaaacttc     300

cttatcttaa acagctgggc gtaacgacga tctggttgtc cccggttttg gacaatctgg     360

atacacttgc aggtaccgat aacactggct atcacggata ctggacgcgc gattttaaac     420

agattgagga acatttcggg aattggacca catttgacac gttggtcaat gatgctcacc     480

aaaacggaat caaggtgatt gtcgactttg tgcccaatca ttcaactcct tttaaggcaa     540

acgattccac ctttgcggaa ggcggcgccc tctacgacaa cggaacctat atgggcaatt     600

attttgatga cgcaacaaaa gggtactttc accataatgg ggacatcagc aactgggacg     660

accggtacga ggcgcaatgg aaaaacttca cggatccagc cggtttctcg cttgccgatt     720

tgtcgcagga aaatggcacg attgctcaat acctgaccga tgcggcggtt caattagtag     780

cacatggagc ggatggtttg cggattgatg cggtgaagca ttttaattct gggttctcca     840

aatcgttggc tgataaactg taccaaaaga aagacatttt cctagtgggg gaatggtacg     900

gagatgaccc cggagcagcc aatcatttgg aaaaggtccg gtacgccaac aacagcggtg     960

tcaatgtgct ggattttgat ctcaacacgg tgattcgaaa tgtgttcggt acatttacgc    1020

aaacgatgta cgatcttaac aatatggtga accaaacggg gaacgagtac aaatacaaag    1080

aaaatctaat cacatttatc gataaccatg atatgtcgag atttcttacg gtaaattcga    1140

acaaggcgaa tttgcaccag gcgcttgctt tcattctcac ttcgcgggga acgccctcca    1200

tctattacgg aaccgaacaa tacatggcag gcggcaatga cccgtacaac agggggatga    1260

tgccggcgtt tgatacgaca accaccgcct ttaaagaggt gtcaactctg gcggggttgc    1320

gcaggaacaa tgcagcgatc cagtacggca ccaccaccca acgttggatc aacaatgatg    1380

tttacattta tgagcggaaa tttttcaacg atgtcgtatt ggtggccatc aatcgaaaca    1440

cgcaatcctc ctactcgatt tccggtttgc agactgcctt gccaaatggc aactatgcgg    1500

attatctgtc agggctgttg ggggggaacg ggatttccgt ttccaatgga agtgtcgctt    1560

cgttcacgct tgcgcctgga gccgtgtctg tttggcagta cagcacatcc gcttcagcgc    1620

cgcaaatcgg atcggttgct ccgaatatgg gaattccggg taatgtggtc acgatcgacg    1680

ggaaaggttt tggaacgacg cagggaaccg tgacatttgg cggagtgaca gcgactgtaa    1740

aatcctggac atcaaaccgg attgaagtgt acgtgcccaa catggccgcc ggtctgaccg    1800

atgtaaaagt caccgcgggt ggagtttcca gcaatctgta ttcttacaat attttgagtg    1860

gaacgcagac atcggttgtg tttactgtga aaagtgctcc tccgaccaac ctgggggata    1920

agatttacct gacgggcaac ataccggaat tgggaaattg gagcacggat acgagcggag    1980

ccgttaacaa tgcgcaaggg cccctgctcg cgcccaatta tccggattgg ttttatgtat    2040

tcagcgttcc ggcaggaaag acgattcaat tcaagttttt catcaagcgt gcggatggaa    2100

cgattcaatg ggagaatggt tcgaaccacg tggccacaac tcccacgggt gcaaccggta    2160

acatcactgt cacgtggcaa aactaataag tttaaac                             2197


<210> 7
<211> 686
<212> PRT
<213> Artificial Sequence

<220> 
<221> source
<222> 1..686
<223> /organism="Artificial Sequence"
      /note="amino acid sequence of a variant of the 
	Alicyclobacillus pohliae NCIMB14276 wild type alpha-amylase 
	polypeptide"


<400> 7
Ser Ser Ser Ala Ser Val Lys Gly Asp Val Ile Tyr Gln Ile Ile Ile 
1               5                   10                  15      
Asp Arg Phe Tyr Asp Gly Asp Thr Thr Asn Asn Asn Pro Ala Lys Ser 
            20                  25                  30          
Tyr Gly Leu Tyr Asp Pro Thr Lys Ser Lys Trp Lys Met Tyr Trp Gly 
        35                  40                  45              
Gly Asp Leu Glu Gly Val Arg Gln Lys Leu Pro Tyr Leu Lys Gln Leu 
    50                  55                  60                  
Gly Val Thr Thr Ile Trp Leu Ser Pro Val Leu Asp Asn Leu Asp Thr 
65                  70                  75                  80  
Leu Ala Gly Thr Asp Asn Thr Gly Tyr His Gly Tyr Trp Thr Arg Asp 
                85                  90                  95      
Phe Lys Gln Ile Glu Glu His Phe Gly Asn Trp Thr Thr Phe Asp Thr 
            100                 105                 110         
Leu Val Asn Asp Ala His Gln Asn Gly Ile Lys Val Ile Val Asp Phe 
        115                 120                 125             
Val Pro Asn His Leu Thr Pro Phe Lys Ala Asn Asp Ser Thr Phe Ala 
    130                 135                 140                 
Glu Gly Gly Ala Leu Tyr Asp Asn Gly Thr Tyr Met Gly Asn Tyr Phe 
145                 150                 155                 160 
Asp Asp Ala Thr Lys Gly Tyr Phe His His Asn Gly Asp Ile Ser Asn 
                165                 170                 175     
Trp Asp Asp Arg Tyr Glu Ala Gln Trp Lys Asn Phe Thr Asp Pro Ala 
            180                 185                 190         
Gly Phe Ser Leu Ala Asp Leu Ser Gln Glu Asn Gly Thr Ile Ala Gln 
        195                 200                 205             
Tyr Leu Thr Asp Ala Ala Val Gln Leu Val Ala His Gly Ala Asp Gly 
    210                 215                 220                 
Leu Arg Ile Asp Ala Val Lys His Phe Asn Ser Gly Phe Ser Lys Ser 
225                 230                 235                 240 
Leu Ala Asp Lys Leu Tyr Gln Lys Lys Asp Ile Phe Leu Val Gly Glu 
                245                 250                 255     
Trp Tyr Gly Asp Asp Pro Gly Ala Ala Asn His Leu Glu Lys Val Arg 
            260                 265                 270         
Tyr Ala Asn Asn Ser Gly Val Asn Val Leu Asp Phe Asp Leu Asn Thr 
        275                 280                 285             
Val Ile Arg Asn Val Phe Gly Thr Phe Thr Gln Thr Met Tyr Asp Leu 
    290                 295                 300                 
Asn Asn Met Val Asn Gln Thr Gly Asn Glu Tyr Lys Tyr Lys Glu Asn 
305                 310                 315                 320 
Leu Ile Thr Phe Ile Asp Asn His Asp Met Ser Arg Phe Leu Thr Val 
                325                 330                 335     
Asn Ser Asn Lys Ala Asn Leu His Gln Ala Leu Ala Phe Ile Leu Thr 
            340                 345                 350         
Ser Arg Gly Thr Pro Ser Ile Tyr Tyr Gly Thr Glu Gln Tyr Met Ala 
        355                 360                 365             
Gly Gly Asn Asp Pro Tyr Asn Arg Gly Met Met Pro Ala Phe Asp Thr 
    370                 375                 380                 
Thr Thr Thr Ala Phe Lys Glu Val Ser Thr Leu Ala Gly Leu Arg Arg 
385                 390                 395                 400 
Asn Asn Ala Ala Ile Gln Tyr Gly Thr Thr Thr Gln Arg Trp Ile Asn 
                405                 410                 415     
Asn Asp Val Tyr Ile Tyr Glu Arg Lys Phe Phe Asn Asp Val Val Leu 
            420                 425                 430         
Val Ala Ile Asn Arg Asn Thr Gln Ser Ser Tyr Ser Ile Ser Gly Leu 
        435                 440                 445             
Gln Thr Ala Leu Pro Asn Gly Asn Tyr Ala Asp Tyr Leu Ser Gly Leu 
    450                 455                 460                 
Leu Gly Gly Asn Gly Ile Ser Val Ser Asn Gly Ser Val Ala Ser Phe 
465                 470                 475                 480 
Thr Leu Ala Pro Gly Ala Val Ser Val Trp Gln Tyr Ser Thr Ser Ala 
                485                 490                 495     
Ser Ala Pro Gln Ile Gly Ser Val Ala Pro Asn Met Gly Ile Pro Gly 
            500                 505                 510         
Asn Val Val Thr Ile Asp Gly Lys Gly Phe Gly Thr Thr Gln Gly Thr 
        515                 520                 525             
Val Thr Phe Gly Gly Val Thr Ala Thr Val Lys Ser Trp Thr Ser Asn 
    530                 535                 540                 
Arg Ile Glu Val Tyr Val Pro Asn Met Ala Ala Gly Leu Thr Asp Val 
545                 550                 555                 560 
Lys Val Thr Ala Gly Gly Val Ser Ser Asn Leu Tyr Ser Tyr Asn Ile 
                565                 570                 575     
Leu Ser Gly Thr Gln Thr Ser Val Val Phe Thr Val Lys Ser Ala Pro 
            580                 585                 590         
Pro Thr Asn Leu Gly Asp Lys Ile Tyr Leu Thr Gly Asn Ile Pro Glu 
        595                 600                 605             
Leu Gly Asn Trp Ser Thr Asp Thr Ser Gly Ala Val Asn Asn Ala Gln 
    610                 615                 620                 
Gly Pro Leu Leu Ala Pro Asn Tyr Pro Asp Trp Phe Tyr Val Phe Ser 
625                 630                 635                 640 
Val Pro Ala Gly Lys Thr Ile Gln Phe Lys Phe Phe Ile Lys Arg Ala 
                645                 650                 655     
Asp Gly Thr Ile Gln Trp Glu Asn Gly Ser Asn His Val Ala Thr Thr 
            660                 665                 670         
Pro Thr Gly Ala Thr Gly Asn Ile Thr Val Thr Trp Gln Asn 
        675                 680                 685     


<210> 8
<211> 686
<212> PRT
<213> Artificial Sequence

<220> 
<221> source
<222> 1..686
<223> /organism="Artificial Sequence"
      /note="amino acid sequence of a variant of the 
	Alicyclobacillus pohliae NCIMB14276 wild type alpha-amylase 
	polypeptide"


<400> 8
Ser Ser Ser Ala Ser Val Lys Gly Asp Val Ile Tyr Gln Ile Ile Ile 
1               5                   10                  15      
Asp Arg Phe Tyr Asp Gly Asp Thr Thr Asn Asn Asn Pro Ala Lys Ser 
            20                  25                  30          
Tyr Gly Leu Tyr Asp Pro Thr Lys Ser Lys Trp Lys Met Tyr Trp Gly 
        35                  40                  45              
Gly Asp Leu Glu Gly Val Arg Gln Lys Leu Pro Tyr Leu Lys Gln Leu 
    50                  55                  60                  
Gly Val Thr Thr Ile Trp Leu Ser Pro Val Leu Asp Asn Leu Asp Thr 
65                  70                  75                  80  
Leu Ala Gly Thr Asp Asn Thr Gly Tyr His Gly Tyr Trp Thr Arg Asp 
                85                  90                  95      
Phe Lys Gln Ile Glu Glu His Phe Gly Asn Trp Thr Thr Phe Asp Thr 
            100                 105                 110         
Leu Val Asn Asp Ala His Gln Asn Gly Ile Lys Val Ile Val Asp Phe 
        115                 120                 125             
Val Pro Asn His Ser Thr Pro Phe Lys Ala Asn Asp Ser Thr Phe Ala 
    130                 135                 140                 
Glu Gly Gly Ala Leu Tyr Asp Asn Gly Thr Tyr Met Gly Asn Tyr Phe 
145                 150                 155                 160 
Asp Asp Ala Thr Lys Gly Tyr Phe His His Asn Gly Asp Ile Ser Asn 
                165                 170                 175     
Trp Asp Asp Arg Tyr Glu Ala Gln Trp Lys Asn Phe Thr Asp Pro Ala 
            180                 185                 190         
Gly Phe Ser Leu Ala Asp Leu Ser Gln Glu Asn Gly Thr Ile Ala Gln 
        195                 200                 205             
Tyr Leu Thr Asp Ala Ala Val Gln Leu Val Ala His Gly Ala Asp Gly 
    210                 215                 220                 
Leu Arg Ile Asp Ala Val Lys His Phe Asn Ser Gly Phe Ser Lys Ser 
225                 230                 235                 240 
Leu Ala Asp Lys Leu Tyr Gln Lys Lys Asp Ile Phe Leu Val Gly Glu 
                245                 250                 255     
Trp Tyr Gly Asp Asp Pro Gly Ala Ala Asn His Leu Glu Lys Val Arg 
            260                 265                 270         
Tyr Ala Asn Asn Ser Gly Val Asn Val Leu Asp Phe Asp Leu Asn Thr 
        275                 280                 285             
Val Ile Arg Asn Val Phe Gly Thr Phe Thr Gln Thr Met Tyr Asp Leu 
    290                 295                 300                 
Asn Asn Met Val Asn Gln Thr Gly Asn Glu Tyr Lys Tyr Lys Glu Asn 
305                 310                 315                 320 
Leu Ile Thr Phe Ile Asp Asn His Asp Met Ser Arg Phe Leu Thr Val 
                325                 330                 335     
Asn Ser Asn Lys Ala Asn Leu His Gln Ala Leu Ala Phe Ile Leu Thr 
            340                 345                 350         
Ser Arg Gly Thr Pro Ser Ile Tyr Tyr Gly Thr Glu Gln Tyr Met Ala 
        355                 360                 365             
Gly Gly Asn Asp Pro Tyr Asn Arg Gly Met Met Pro Ala Phe Asp Thr 
    370                 375                 380                 
Thr Thr Thr Ala Phe Lys Glu Val Ser Thr Leu Ala Gly Leu Arg Arg 
385                 390                 395                 400 
Asn Asn Ala Ala Ile Gln Tyr Gly Thr Thr Thr Gln Arg Trp Ile Asn 
                405                 410                 415     
Asn Asp Val Tyr Ile Tyr Glu Arg Lys Phe Phe Asn Asp Val Val Leu 
            420                 425                 430         
Val Ala Ile Asn Arg Asn Thr Gln Ser Ser Tyr Ser Ile Ser Gly Leu 
        435                 440                 445             
Gln Thr Ala Leu Pro Asn Gly Asn Tyr Ala Asp Tyr Leu Ser Gly Leu 
    450                 455                 460                 
Leu Gly Gly Asn Gly Ile Ser Val Ser Asn Gly Ser Val Ala Ser Phe 
465                 470                 475                 480 
Thr Leu Ala Pro Gly Ala Val Ser Val Trp Gln Tyr Ser Thr Ser Ala 
                485                 490                 495     
Ser Ala Pro Gln Ile Gly Ser Val Ala Pro Asn Met Gly Ile Pro Gly 
            500                 505                 510         
Asn Val Val Thr Ile Asp Gly Lys Gly Phe Gly Thr Thr Gln Gly Thr 
        515                 520                 525             
Val Thr Phe Gly Gly Val Thr Ala Thr Val Lys Ser Trp Thr Ser Asn 
    530                 535                 540                 
Arg Ile Glu Val Tyr Val Pro Asn Met Gly Ala Gly Leu Thr Asp Val 
545                 550                 555                 560 
Lys Val Thr Ala Gly Gly Val Ser Ser Asn Leu Tyr Ser Tyr Asn Ile 
                565                 570                 575     
Leu Ser Gly Thr Gln Thr Ser Val Val Phe Thr Val Lys Ser Ala Pro 
            580                 585                 590         
Pro Thr Asn Leu Gly Asp Lys Ile Tyr Leu Thr Gly Asn Ile Pro Glu 
        595                 600                 605             
Leu Gly Asn Trp Ser Thr Asp Thr Ser Gly Ala Val Asn Asn Ala Gln 
    610                 615                 620                 
Gly Pro Leu Leu Ala Pro Asn Tyr Pro Asp Trp Phe Tyr Val Phe Ser 
625                 630                 635                 640 
Val Pro Ala Gly Lys Thr Ile Gln Phe Lys Phe Phe Ile Lys Arg Ala 
                645                 650                 655     
Asp Gly Thr Ile Gln Trp Glu Asn Gly Ser Asn His Val Ala Thr Thr 
            660                 665                 670         
Pro Thr Gly Ala Thr Gly Asn Ile Thr Val Thr Trp Gln Asn 
        675                 680                 685     

