ID   GSPB_STRGN              Reviewed;        3072 AA.
AC   Q939N5;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Platelet binding protein GspB;
DE   AltName: Full=Adhesin GspB {ECO:0000305};
DE   AltName: Full=Serine-rich adhesin for platelets;
DE   AltName: Full=Serine-rich repeat protein GspB;
DE   Flags: Precursor;
GN   Name=gspB;
OS   Streptococcus gordonii.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA   Bensing B.A., Sullam P.M.;
RT   "An accessory sec locus of Streptococcus gordonii is required for export of
RT   the surface protein GspB and for normal levels of binding to human
RT   platelets.";
RL   Mol. Microbiol. 44:1081-1094(2002).
RN   [2]
RP   S.GORDONII IN INFECTIVE ENDOCARDITIS.
RX   PubMed=8366515; DOI=10.1099/00222615-39-3-179;
RA   Douglas C.W., Heath J., Hampton K.K., Preston F.E.;
RT   "Identity of viridans streptococci isolated from cases of infective
RT   endocarditis.";
RL   J. Med. Microbiol. 39:179-182(1993).
RN   [3]
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=M99;
RX   PubMed=14729688; DOI=10.1128/jb.186.3.638-645.2004;
RA   Bensing B.A., Gibson B.W., Sullam P.M.;
RT   "The Streptococcus gordonii platelet binding protein GspB undergoes
RT   glycosylation independently of export.";
RL   J. Bacteriol. 186:638-645(2004).
RN   [4]
RP   EXPORT VIA THE ACCESSORY SECA2/SECY2 SYSTEM.
RC   STRAIN=M99;
RX   PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Genes in the accessory sec locus of Streptococcus gordonii have three
RT   functionally distinct effects on the expression of the platelet-binding
RT   protein GspB.";
RL   Mol. Microbiol. 52:189-203(2004).
RN   [5]
RP   GLYCOSYLATION OF SER-RICH REGIONS.
RC   STRAIN=M99;
RX   PubMed=15489421; DOI=10.1128/jb.186.21.7100-7111.2004;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii
RT   mediate the intracellular glycosylation of the platelet-binding protein
RT   GspB.";
RL   J. Bacteriol. 186:7100-7111(2004).
RN   [6]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=19202081; DOI=10.1099/mic.0.025221-0;
RA   Zhou M., Wu H.;
RT   "Glycosylation and biogenesis of a family of serine-rich bacterial
RT   adhesins.";
RL   Microbiology 155:317-327(2009).
RN   [7]
RP   FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=20714350; DOI=10.1371/journal.ppat.1001044;
RA   Sanchez C.J., Shivshankar P., Stol K., Trakhtenbroit S., Sullam P.M.,
RA   Sauer K., Hermans P.W., Orihuela C.J.;
RT   "The pneumococcal serine-rich repeat protein is an intra-species bacterial
RT   adhesin that promotes bacterial aggregation in vivo and in biofilms.";
RL   PLoS Pathog. 6:E1001044-E1001044(2010).
RN   [8]
RP   INTERACTION WITH ASP2 AND ASP3.
RX   PubMed=21531800; DOI=10.1128/jb.00057-11;
RA   Yen Y.T., Seepersaud R., Bensing B.A., Sullam P.M.;
RT   "Asp2 and Asp3 interact directly with GspB, the export substrate of the
RT   Streptococcus gordonii accessory Sec System.";
RL   J. Bacteriol. 193:3165-3174(2011).
RN   [9]
RP   GLYCOSYLATION OF SER-RICH REGIONS.
RC   STRAIN=M99;
RX   PubMed=26884191; DOI=10.1073/pnas.1600494113;
RA   Chen Y., Seepersaud R., Bensing B.A., Sullam P.M., Rapoport T.A.;
RT   "Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis
RT   of a bacterial adhesion protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E1190-E1199(2016).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 245-604, FUNCTION, MUTAGENESIS OF
RP   TYR-443; ARG-484 AND TYR-485, AND INTERACTION WITH HUMAN GP1BA.
RX   PubMed=21765814; DOI=10.1371/journal.ppat.1002112;
RA   Pyburn T.M., Bensing B.A., Xiong Y.Q., Melancon B.J., Tomasiak T.M.,
RA   Ward N.J., Yankovskaya V., Oliver K.M., Cecchini G., Sulikowski G.A.,
RA   Tyska M.J., Sullam P.M., Iverson T.M.;
RT   "A structural model for binding of the serine-rich repeat adhesin GspB to
RT   host carbohydrate receptors.";
RL   PLoS Pathog. 7:E1002112-E1002112(2011).
CC   -!- FUNCTION: Plays a role in virulence and host-pathogen interactions.
CC       Mediates binding to human platelets via interaction with the human cell
CC       surface glycoprotein GP1BA (PubMed:21765814). Plays a positive role in
CC       biofilm formation, possibly by self-association via the basic region
CC       (BR) (PubMed:20714350). {ECO:0000269|PubMed:20714350,
CC       ECO:0000269|PubMed:21765814}.
CC   -!- SUBUNIT: Both SSR domains in the unglycosylated protein bind to Asp2
CC       and Asp3; glycosylated protein binds less well. Interacts with the
CC       human cell surface glycoprotein GP1BA. {ECO:0000269|PubMed:21531800,
CC       ECO:0000269|PubMed:21765814}.
CC   -!- INTERACTION:
CC       Q939N5; Q9AET8: asp2; NbExp=4; IntAct=EBI-6414561, EBI-6414583;
CC       Q939N5; Q9AET7: asp3; NbExp=4; IntAct=EBI-6414561, EBI-6414568;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12010500,
CC       ECO:0000269|PubMed:14729688}; Peptidoglycan-anchor
CC       {ECO:0000269|PubMed:12010500, ECO:0000269|PubMed:14729688}.
CC       Note=Exported by the accessory SecA2/SecY2 protein translocation
CC       apparatus. {ECO:0000269|PubMed:12010500}.
CC   -!- DOMAIN: Has a short and long Ser-rich region with a basic region
CC       between them. The SRR domains themselves are comprised of inexact
CC       repeats of SASESASTSASV. SSR1 has 6 repeats, SSR2 has 200. The Ser-rich
CC       regions are both glycosylated. The basic region (BR) binds to whole
CC       cell lysates of wild-type but not bacteria deleted of this gene; it
CC       also recognizes whole cell lysates of S.aureus strain ISP479C probably
CC       via SraP, but not lysates of S.pneumoniae TIGR4 (PubMed:20714350). The
CC       predicted pI of the basic region is 9.51 (PubMed:19202081).
CC       {ECO:0000269|PubMed:20714350, ECO:0000303|PubMed:19202081}.
CC   -!- PTM: Proteolytically cleaved by a metalloprotease. {ECO:0000250}.
CC   -!- PTM: Both SSR1 and SSR2 domains are glycosylated (Probable). A
CC       truncated derivative (residues 1-2062) contains 105 nmol per nmol of
CC       protein, suggesting at least 10% of the apparent molecular weight is
CC       due to carbohydrates (PubMed:14729688). Glucose and N-acetylglucosamine
CC       are present in a ratio of 30:73 residues per truncated polypeptide, as
CC       well as minor amounts of galactose and N-acetylgalactosamine
CC       (PubMed:14729688). Glycosylation occurs intracellularly in the Ser-rich
CC       regions SSR1 and SSR2 (PubMed:14729688, PubMed:15489421). Glycosylation
CC       of SSR2 domain may be required to prevent aggregation of GspB
CC       (Probable). It is probable that most of the Ser residues in SSR1 and
CC       SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases
CC       are able to generate complex sugar polymorphisms (By similarity).
CC       {ECO:0000250|UniProtKB:A0A0H2URK1, ECO:0000269|PubMed:14729688,
CC       ECO:0000269|PubMed:15489421, ECO:0000305|PubMed:14729688,
CC       ECO:0000305|PubMed:15489421, ECO:0000305|PubMed:26884191}.
CC   -!- DISRUPTION PHENOTYPE: Loss of adherence to human platelet cells
CC       (PubMed:12010500). Decrease in early biofilm formation
CC       (PubMed:20714350). {ECO:0000269|PubMed:12010500,
CC       ECO:0000269|PubMed:20714350}.
CC   -!- MISCELLANEOUS: S.gordonii, a commensal oral cavity bacteria, is among
CC       the bacteria most frequently identified as being the primary
CC       etiological agents of subacute infective endocarditis (found in 13% of
CC       cases). {ECO:0000269|PubMed:8366515}.
CC   -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC       {ECO:0000305}.
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DR   EMBL; AY028381; AAL13053.1; -; Genomic_DNA.
DR   PDB; 3QC5; X-ray; 1.40 A; X=245-604.
DR   PDB; 3QC6; X-ray; 1.90 A; X=245-604.
DR   PDB; 5IUC; X-ray; 1.25 A; A/B=399-521.
DR   PDB; 6EF7; X-ray; 1.03 A; A=399-521.
DR   PDB; 6EF9; X-ray; 1.30 A; A=398-521.
DR   PDB; 6EFA; X-ray; 1.60 A; A=399-601.
DR   PDBsum; 3QC5; -.
DR   PDBsum; 3QC6; -.
DR   PDBsum; 5IUC; -.
DR   PDBsum; 6EF7; -.
DR   PDBsum; 6EF9; -.
DR   PDBsum; 6EFA; -.
DR   SMR; Q939N5; -.
DR   IntAct; Q939N5; 2.
DR   UniLectin; Q939N5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.3260; -; 1.
DR   Gene3D; 2.60.40.4140; -; 1.
DR   Gene3D; 3.10.20.890; -; 1.
DR   InterPro; IPR044024; aRib.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR026465; Ser_adhes_glycop_N.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; TIGR04224; ser_adhes_Nterm; 1.
DR   PANTHER; PTHR12239; PROTEIN CBG20215-RELATED; 1.
DR   PANTHER; PTHR12239:SF41; TOLA PROTEIN; 1.
DR   Pfam; PF18938; aRib; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell wall; Glycoprotein; Peptidoglycan-anchor;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..85
FT                   /evidence="ECO:0000255"
FT   CHAIN           86..3041
FT                   /note="Platelet binding protein GspB"
FT                   /id="PRO_0000414192"
FT   PROPEP          3042..3072
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000414193"
FT   REGION          117..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..236
FT                   /note="Ser-rich region 1 (SSR1)"
FT   REGION          182..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..603
FT                   /note="Basic region (BR)"
FT   REGION          604..3028
FT                   /note="Ser-rich region 2 (SSR2)"
FT   REGION          876..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..2085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2106..2139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2173..2223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2250..2595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2625..2967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3014..3045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           3038..3042
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        182..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3014..3044
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            443
FT                   /note="Important for interaction with host glycoprotein and
FT                   virulence"
FT   SITE            484
FT                   /note="Important for interaction with host glycoprotein and
FT                   virulence"
FT   SITE            485
FT                   /note="Important for interaction with host glycoprotein and
FT                   virulence"
FT   MOD_RES         3041
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   MUTAGEN         443
FT                   /note="Y->F: Strongly reduced interaction with GP1BA
FT                   carbohydrate chains."
FT                   /evidence="ECO:0000269|PubMed:21765814"
FT   MUTAGEN         484
FT                   /note="R->E: Strongly reduced interaction with GP1BA
FT                   carbohydrate chains. Strongly reduced platelet binding."
FT                   /evidence="ECO:0000269|PubMed:21765814"
FT   MUTAGEN         485
FT                   /note="Y->F: Strongly reduced interaction with GP1BA
FT                   carbohydrate chains."
FT                   /evidence="ECO:0000269|PubMed:21765814"
FT   STRAND          247..250
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          253..257
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          263..272
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   TURN            273..275
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          277..284
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          291..299
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          303..310
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          316..319
FT                   /evidence="ECO:0007829|PDB:3QC6"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          338..346
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          351..364
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   TURN            368..370
FT                   /evidence="ECO:0007829|PDB:3QC6"
FT   HELIX           375..377
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   TURN            379..382
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          386..395
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          409..414
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          418..426
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   HELIX           434..436
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          438..440
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          442..446
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          455..461
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          464..472
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          480..487
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          495..497
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   HELIX           499..508
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          515..521
FT                   /evidence="ECO:0007829|PDB:6EF7"
FT   STRAND          531..534
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   HELIX           541..554
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   HELIX           560..562
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   HELIX           564..566
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   HELIX           568..571
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          572..574
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          580..584
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          589..592
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   TURN            595..597
FT                   /evidence="ECO:0007829|PDB:3QC5"
FT   STRAND          598..601
FT                   /evidence="ECO:0007829|PDB:3QC5"
SQ   SEQUENCE   3072 AA;  285769 MW;  0B148372697CF7F2 CRC64;
     MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST EVKVVEEQSV
     EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI DTRDVLATRG EAVLSEEAAT
     TLSSTEANPV ESLSDTLSAS ESTSASSSVS TSISVSESFS VSGSLSYSTS LSQSVSASAS
     ASESLSVSSS ASDSVSASTS TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR
     RRTRRAVTES APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS
     GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG GEVKLGLRLV
     TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT ERPVVNVPSE ITVYRGESFE
     YFATVTDNSN AFDLAKTVVR WLYNNQPGRG TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG
     DYTRYVVATD AAGNVNATQT EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT
     EVEKNLVREA VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT
     RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS TSGSVSASES
     ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASTSASKS
     ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASVSASES
     ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS
     ASTSASVSAS ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS ASVSASTSAS TSASVSASTS
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASESAS TSASVSASES
     ASTSASESAS ESASTSASVS ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES
     ASTSASVSAS ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS
     ASTSASVSAS ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
     ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS
     ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS ASDSASISAS
     VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSSSVS ASESASTSAS
     VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
     VSASESASTS ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
     VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASESAS TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS
     VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
     VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASTSASTS ASVSANESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASTSAS TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS
     VSASESASTS ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS
     LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI LALGLGALGL
     AFKKRKKNES ED
//