HYSA_STRPN
ID HYSA_STRPN Reviewed; 1066 AA.
AC Q54873; Q54874;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:10716923};
DE EC=4.2.2.1 {ECO:0000269|PubMed:10716923, ECO:0000269|PubMed:8112843};
DE AltName: Full=Hyaluronidase {ECO:0000303|PubMed:8112843};
DE Short=HYase;
DE Flags: Precursor;
GN OrderedLocusNames=SP_0314;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-1066, AND CATALYTIC ACTIVITY.
RC STRAIN=Type 23;
RX PubMed=8112843; DOI=10.1128/iai.62.3.1101-1108.1994;
RA Berry A.M., Lock R.A., Thomas S.M., Rajan D.P., Hansman D., Paton J.C.;
RT "Cloning and nucleotide sequence of the Streptococcus pneumoniae
RT hyaluronidase gene and purification of the enzyme from recombinant
RT Escherichia coli.";
RL Infect. Immun. 62:1101-1108(1994).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=9573623; DOI=10.1006/jsbi.1998.3963;
RA Jedrzejas M.J., Chantalat L., Mewbourne R.B.;
RT "Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae
RT hyaluronate lyase.";
RL J. Struct. Biol. 121:73-75(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 285-1015, CATALYTIC ACTIVITY,
RP ACTIVE SITE, AND MUTAGENESIS OF ARG-360; ASN-466; HIS-516; TYR-525 AND
RP ASN-697.
RX PubMed=10716923; DOI=10.1093/emboj/19.6.1228;
RA Li S., Kelly S.J., Lamani E., Ferraroni M., Jedrzejas M.J.;
RT "Structural basis of hyaluronan degradation by Streptococcus pneumoniae
RT hyaluronate lyase.";
RL EMBO J. 19:1228-1240(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-
CC acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA-
CC COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151,
CC ChEBI:CHEBI:132153; EC=4.2.2.1;
CC Evidence={ECO:0000269|PubMed:10716923, ECO:0000269|PubMed:8112843};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA53685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA53686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005672; AAK74491.1; -; Genomic_DNA.
DR EMBL; L20670; AAA53685.1; ALT_INIT; Genomic_DNA.
DR EMBL; L20670; AAA53686.1; ALT_INIT; Genomic_DNA.
DR PIR; B95037; B95037.
DR RefSeq; WP_001193686.1; NZ_AKBW01000001.1.
DR PDB; 1C82; X-ray; 1.70 A; A=285-1009.
DR PDB; 1EGU; X-ray; 1.56 A; A=285-1009.
DR PDB; 1F9G; X-ray; 2.00 A; A=285-1009.
DR PDB; 1LOH; X-ray; 2.00 A; A=287-1007.
DR PDB; 1LXK; X-ray; 1.53 A; A=287-1007.
DR PDB; 1N7N; X-ray; 1.55 A; A=287-1007.
DR PDB; 1N7O; X-ray; 1.50 A; A=287-1007.
DR PDB; 1N7P; X-ray; 1.55 A; A=287-1007.
DR PDB; 1N7Q; X-ray; 2.30 A; A=287-1007.
DR PDB; 1N7R; X-ray; 2.20 A; A=287-1007.
DR PDB; 1OJM; X-ray; 1.78 A; A=291-1009.
DR PDB; 1OJN; X-ray; 1.60 A; A=285-1009.
DR PDB; 1OJO; X-ray; 1.75 A; A=285-1009.
DR PDB; 1OJP; X-ray; 1.90 A; A=285-1009.
DR PDB; 1W3Y; X-ray; 1.65 A; A=285-1009.
DR PDB; 2BRP; X-ray; 2.00 A; A=285-1009.
DR PDB; 2BRV; X-ray; 3.30 A; X=285-1009.
DR PDB; 2BRW; X-ray; 2.80 A; A/B=285-1009.
DR PDB; 4D0Q; X-ray; 1.20 A; A=54-212.
DR PDBsum; 1C82; -.
DR PDBsum; 1EGU; -.
DR PDBsum; 1F9G; -.
DR PDBsum; 1LOH; -.
DR PDBsum; 1LXK; -.
DR PDBsum; 1N7N; -.
DR PDBsum; 1N7O; -.
DR PDBsum; 1N7P; -.
DR PDBsum; 1N7Q; -.
DR PDBsum; 1N7R; -.
DR PDBsum; 1OJM; -.
DR PDBsum; 1OJN; -.
DR PDBsum; 1OJO; -.
DR PDBsum; 1OJP; -.
DR PDBsum; 1W3Y; -.
DR PDBsum; 2BRP; -.
DR PDBsum; 2BRV; -.
DR PDBsum; 2BRW; -.
DR PDBsum; 4D0Q; -.
DR AlphaFoldDB; Q54873; -.
DR SMR; Q54873; -.
DR STRING; 170187.SP_0314; -.
DR BindingDB; Q54873; -.
DR ChEMBL; CHEMBL1795158; -.
DR DrugBank; DB08438; (2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACID.
DR DrugBank; DB01872; 2-deoxy-2-acetamido-beta-D-galactose-4-sulfate.
DR DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB03156; beta-D-glucuronic acid.
DR DrugBank; DB02186; N-acetyl-beta-D-galactosamine 6-sulfate.
DR DrugBank; DB11195; Xylitol.
DR CAZy; CBM70; Carbohydrate-Binding Module Family 70.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR EnsemblBacteria; AAK74491; AAK74491; SP_0314.
DR KEGG; spn:SP_0314; -.
DR eggNOG; COG5492; Bacteria.
DR OMA; RYYQDET; -.
DR PhylomeDB; Q54873; -.
DR BioCyc; MetaCyc:MON-19222; -.
DR BRENDA; 4.2.2.1; 1960.
DR SABIO-RK; Q54873; -.
DR EvolutionaryTrace; Q54873; -.
DR PRO; PR:Q54873; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0030340; F:hyaluronate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.60.40.1380; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR023295; Hyaluronate_lyase_beta_dom_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR038970; Lyase_8.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR012970; Lyase_8_alpha_N.
DR InterPro; IPR004103; Lyase_8_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR PANTHER; PTHR38481; PTHR38481; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Lyase; Peptidoglycan-anchor; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1039
FT /note="Hyaluronate lyase"
FT /id="PRO_0000024933"
FT PROPEP 1040..1066
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000024934"
FT REGION 1010..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1036..1040
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1018..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /evidence="ECO:0000305|PubMed:10716923"
FT ACT_SITE 516
FT /evidence="ECO:0000305|PubMed:10716923"
FT ACT_SITE 525
FT /evidence="ECO:0000305|PubMed:10716923"
FT MOD_RES 1039
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 360
FT /note="R->V: Retains 67% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10716923"
FT MUTAGEN 466
FT /note="N->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10716923"
FT MUTAGEN 516
FT /note="H->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10716923"
FT MUTAGEN 525
FT /note="Y->F: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10716923"
FT MUTAGEN 697
FT /note="N->G: Slightly increased activity."
FT /evidence="ECO:0000269|PubMed:10716923"
FT CONFLICT 108
FT /note="H -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="L -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="I -> V (in Ref. 2; AAA53685)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> P (in Ref. 2; AAA53685)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> P (in Ref. 2; AAA53685)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> T (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="E -> D (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> I (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="C -> R (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="P -> T (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="G -> S (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="V -> G (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="F -> S (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="R -> G (in Ref. 2; AAA53685/AAA53686)"
FT /evidence="ECO:0000305"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4D0Q"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 102..120
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 127..150
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 162..175
FT /evidence="ECO:0007829|PDB:4D0Q"
FT STRAND 182..206
FT /evidence="ECO:0007829|PDB:4D0Q"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2BRW"
FT HELIX 313..332
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2BRV"
FT HELIX 353..369
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:2BRV"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 432..445
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1EGU"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 464..480
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 484..494
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 525..540
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 554..561
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:1N7P"
FT HELIX 588..605
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 608..624
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 637..648
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 675..678
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 679..684
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:1LXK"
FT TURN 704..707
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 718..721
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 725..728
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:1LXK"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 767..775
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 779..789
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 794..803
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 809..817
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:1EGU"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 840..851
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 855..857
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 859..878
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 892..902
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 908..917
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 920..929
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 934..946
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 947..950
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 951..958
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 965..967
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 968..970
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 972..981
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 984..991
FT /evidence="ECO:0007829|PDB:1N7O"
FT TURN 992..995
FT /evidence="ECO:0007829|PDB:1N7O"
FT HELIX 1000..1003
FT /evidence="ECO:0007829|PDB:1N7O"
FT STRAND 1004..1006
FT /evidence="ECO:0007829|PDB:1OJN"
SQ SEQUENCE 1066 AA; 120771 MW; 81DB22A837BE61F9 CRC64;
MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR DTKNLVENGD
FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD GAITISSHEK LRAALHRMVP
IEAKKKYKLR FKIKTDNKIG IAKVRIIEES GKDKRLWNSA TTSGTKDWQT IEADYSPTLD
VDKIKLELFY ETGTGTVSFK DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY
TYKVENPDVA SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG
IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK TSANLTATYR
KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS EKSIVGNWWD YEIGTPRAIN
NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE HFRKTTDNPF KALGGNLVDM GRVKVIAGLL
RKDDQEISST IRSIEQVFKL VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI
QKTKNPIDKD KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH
RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA GVASVPRPSY
LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN KRGWYTSDGM FYLYNGDLSH
YSDGYWPTVN PYKMPGTTET DAKRADSDTG KVLPSAFVGT SKLDDANATA TMDFTNWNQT
LTAHKSWFML KDKIAFLGSN IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK
DYPETQSVFL ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS
QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG VWGIVKYDDS
VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD QEVFKKLEQA AQPQVQNSKE
KEKSEEEKNH SDQKNLPQTG EGQSILASLG FLLLGAFYLF RRGKNN
