(data stored in SCRATCH zone)

SWISSPROT: GLMS_ECOLI

ID   GLMS_ECOLI              Reviewed;         609 AA.
AC   P17169; P76745; Q2M847;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   11-DEC-2019, entry version 195.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=b3729, JW3707;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6395859; DOI=10.1042/bj2240799;
RA   Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT   "DNA sequence around the Escherichia coli unc operon. Completion of the
RT   sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT   phoS.";
RL   Biochem. J. 224:799-815(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 49-52; 219-231; 489-493; 505-508 AND 601-609.
RX   PubMed=1915361; DOI=10.1111/j.1432-1033.1991.tb16271.x;
RA   Golinelli-Pimpaneau B., Badet B.;
RT   "Possible involvement of Lys603 from Escherichia coli glucosamine-6-
RT   phosphate synthase in the binding of its substrate fructose 6-phosphate.";
RL   Eur. J. Biochem. 201:175-182(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-609.
RX   PubMed=6283361; DOI=10.1038/297601a0;
RA   Lichtenstein C., Brenner S.;
RT   "Unique insertion site of Tn7 in the E. coli chromosome.";
RL   Nature 297:601-603(1982).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 607-609.
RX   PubMed=3010949; DOI=10.1042/bj2340111;
RA   Gay N.J., Tybulewicz V.L.J., Walker J.E.;
RT   "Insertion of transposon Tn7 into the Escherichia coli glmS transcriptional
RT   terminator.";
RL   Biochem. J. 234:111-117(1986).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 597-609.
RX   PubMed=2826397; DOI=10.1128/jb.170.1.352-358.1988;
RA   McKown R.L., Orle K.A., Chen T., Craig N.L.;
RT   "Sequence requirements of Escherichia coli attTn7, a specific site of
RT   transposon Tn7 insertion.";
RL   J. Bacteriol. 170:352-358(1988).
RN   [9]
RP   CHARACTERIZATION.
RX   PubMed=3134953; DOI=10.1016/0300-9084(88)90073-9;
RA   Dutka-Malen S., Mazodier P., Badet B.;
RT   "Molecular cloning and overexpression of the glucosamine synthetase gene
RT   from Escherichia coli.";
RL   Biochimie 70:287-290(1988).
RN   [10]
RP   REGULATION BY THE GLMYZ CASCADE.
RX   PubMed=18334534; DOI=10.1093/nar/gkn091;
RA   Reichenbach B., Maes A., Kalamorz F., Hajnsdorf E., Goerke B.;
RT   "The small RNA GlmY acts upstream of the sRNA GlmZ in the activation of
RT   glmS expression and is subject to regulation by polyadenylation in
RT   Escherichia coli.";
RL   Nucleic Acids Res. 36:2570-2580(2008).
RN   [11]
RP   REGULATION BY THE GLMYZ CASCADE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=18351803; DOI=10.1371/journal.pbio.0060064;
RA   Urban J.H., Vogel J.;
RT   "Two seemingly homologous noncoding RNAs act hierarchically to activate
RT   glmS mRNA translation.";
RL   PLoS Biol. 6:E64-E64(2008).
RN   [12]
RP   REGULATION BY THE GLMYZ CASCADE.
RX   PubMed=23475961; DOI=10.1101/gad.210112.112;
RA   Gopel Y., Papenfort K., Reichenbach B., Vogel J., Gorke B.;
RT   "Targeted decay of a regulatory small RNA by an adaptor protein for RNase E
RT   and counteraction by an anti-adaptor RNA.";
RL   Genes Dev. 27:552-564(2013).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-241.
RX   PubMed=8805567; DOI=10.1016/s0969-2126(96)00087-1;
RA   Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A., Badet B.,
RA   Polikarpov I., Littlechild J.A., Teplyakov A.;
RT   "Substrate binding is required for assembly of the active conformation of
RT   the catalytic site in Ntn amidotransferases: evidence from the 1.8-A
RT   crystal structure of the glutaminase domain of glucosamine 6-phosphate
RT   synthase.";
RL   Structure 4:801-810(1996).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 244-609.
RX   PubMed=9739095; DOI=10.1016/s0969-2126(98)00105-1;
RA   Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B., Polikarpov I.;
RT   "Involvement of the C-terminus in intramolecular nitrogen channeling in
RT   glucosamine 6-phosphate synthase: evidence from a 1.6-A crystal structure
RT   of the isomerase domain.";
RL   Structure 6:1047-1055(1998).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-609.
RX   PubMed=10091662; DOI=10.1110/ps.8.3.596;
RA   Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B.;
RT   "The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate
RT   synthase.";
RL   Protein Sci. 8:596-602(1999).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P62615:ispE; NbExp=2; IntAct=EBI-551022, EBI-562202;
CC       P76093:ynbD; NbExp=4; IntAct=EBI-551022, EBI-551038;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Post-transcriptionally regulated by the GlmY/GlmZ sRNA
CC       regulatory cascade. The sRNA GlmZ, together with Hfq, directly
CC       activates glmS mRNA translation through base-pairing. A second sRNA,
CC       GlmY, positively regulates glmS indirectly, by sequestering the adapter
CC       protein RapZ and protecting GlmZ from RNA cleavage.
CC       {ECO:0000269|PubMed:18334534, ECO:0000269|PubMed:18351803,
CC       ECO:0000269|PubMed:23475961}.
DR   EMBL; X01631; CAA25785.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62080.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76752.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77559.1; -; Genomic_DNA.
DR   EMBL; V00620; CAA23894.1; -; Genomic_DNA.
DR   EMBL; M18980; AAA23836.1; -; Genomic_DNA.
DR   PIR; B65176; XNECGM.
DR   RefSeq; NP_418185.1; NC_000913.3.
DR   RefSeq; WP_000334099.1; NZ_SSZK01000036.1.
DR   PDB; 1JXA; X-ray; 3.10 A; A/B/C=2-609.
DR   PDB; 1MOQ; X-ray; 1.57 A; A=242-609.
DR   PDB; 1MOR; X-ray; 1.90 A; A=242-609.
DR   PDB; 1MOS; X-ray; 2.00 A; A=242-609.
DR   PDB; 1XFF; X-ray; 1.80 A; A/B=2-241.
DR   PDB; 1XFG; X-ray; 1.85 A; A/B=2-241.
DR   PDB; 2J6H; X-ray; 2.35 A; A/B=2-609.
DR   PDB; 2VF4; X-ray; 2.95 A; X=2-609.
DR   PDB; 2VF5; X-ray; 2.90 A; X=2-609.
DR   PDB; 3OOJ; X-ray; 2.50 A; A/B/C/D/E/F/G/H=3-609.
DR   PDB; 4AMV; X-ray; 2.05 A; A/B/C=1-609.
DR   PDBsum; 1JXA; -.
DR   PDBsum; 1MOQ; -.
DR   PDBsum; 1MOR; -.
DR   PDBsum; 1MOS; -.
DR   PDBsum; 1XFF; -.
DR   PDBsum; 1XFG; -.
DR   PDBsum; 2J6H; -.
DR   PDBsum; 2VF4; -.
DR   PDBsum; 2VF5; -.
DR   PDBsum; 3OOJ; -.
DR   PDBsum; 4AMV; -.
DR   SMR; P17169; -.
DR   BioGrid; 4262136; 528.
DR   BioGrid; 852543; 1.
DR   DIP; DIP-9775N; -.
DR   IntAct; P17169; 8.
DR   STRING; 511145.b3729; -.
DR   BindingDB; P17169; -.
DR   DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DR   DrugBank; DB02445; 2-Deoxy-2-Amino Glucitol-6-Phosphate.
DR   DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR   DrugBank; DB02657; Glucosamine 6-Phosphate.
DR   DrugBank; DB03581; Glucose-6-Phosphate.
DR   DrugBank; DB02446; Glutamine hydroxamate.
DR   EPD; P17169; -.
DR   jPOST; P17169; -.
DR   PaxDb; P17169; -.
DR   PRIDE; P17169; -.
DR   EnsemblBacteria; AAC76752; AAC76752; b3729.
DR   EnsemblBacteria; BAE77559; BAE77559; BAE77559.
DR   GeneID; 948241; -.
DR   KEGG; ecj:JW3707; -.
DR   KEGG; eco:b3729; -.
DR   PATRIC; fig|1411691.4.peg.2971; -.
DR   EchoBASE; EB0377; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258898; -.
DR   InParanoid; P17169; -.
DR   KO; K00820; -.
DR   PhylomeDB; P17169; -.
DR   BioCyc; EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER; -.
DR   BioCyc; ECOL316407:JW3707-MONOMER; -.
DR   BioCyc; MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER; -.
DR   BRENDA; 2.6.1.16; 2026.
DR   EvolutionaryTrace; P17169; -.
DR   PRO; PR:P17169; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   1: Evidence at protein level;
DR   PRODOM; P17169.
DR   SWISS-2DPAGE; P17169.
KW   3D-structure; Aminotransferase; Cytoplasm; Direct protein sequencing;
KW   Glutamine amidotransferase; Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..609
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135328"
FT   DOMAIN          2..218
FT                   /note="Glutamine amidotransferase type-2"
FT   DOMAIN          286..426
FT                   /note="SIS 1"
FT   DOMAIN          458..599
FT                   /note="SIS 2"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        604
FT                   /note="For Fru-6P isomerization activity"
FT   CONFLICT        419..420
FT                   /note="KL -> NV (in Ref. 1; CAA25785)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           14..24
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           25..27
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          30..37
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          43..50
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           52..61
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          67..74
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          77..79
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   TURN            83..85
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          89..91
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          94..102
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           105..114
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           125..137
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           142..149
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           150..152
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          155..163
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          170..177
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          180..183
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          188..193
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   HELIX           194..196
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   TURN            197..200
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          202..206
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          212..215
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          220..223
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   STRAND          225..227
FT                   /evidence="ECO:0000244|PDB:4AMV"
FT   STRAND          234..236
FT                   /evidence="ECO:0000244|PDB:1XFF"
FT   TURN            241..244
FT                   /evidence="ECO:0000244|PDB:4AMV"
FT   HELIX           252..258
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           260..268
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          271..273
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          274..277
FT                   /evidence="ECO:0000244|PDB:1MOR"
FT   HELIX           280..282
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           286..292
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          295..300
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           302..318
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          323..327
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           328..332
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          342..351
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           354..363
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   TURN            364..367
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          369..377
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           381..385
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          386..391
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          399..401
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           404..423
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           428..448
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           449..451
FT                   /evidence="ECO:0000244|PDB:4AMV"
FT   HELIX           454..462
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          466..472
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           474..476
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           477..491
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          494..499
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           500..505
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           507..510
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          517..521
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           524..536
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           537..540
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          544..549
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           550..552
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          560..565
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           570..572
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   HELIX           573..592
FT                   /evidence="ECO:0000244|PDB:1MOQ"
FT   STRAND          596..598
FT                   /evidence="ECO:0000244|PDB:1MOQ"
SQ   SEQUENCE   609 AA;  66894 MW;  A1CB929E839436E0 CRC64;
     MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE
     EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG IIENHEPLRE ELKARGYTFV
     SETDTEVIAH LVNWELKQGG TLREAVLRAI PQLRGAYGTV IMDSRHPDTL LAARSGSPLV
     IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ
     YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA
     CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL
     RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL
     SRLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIEALAE DFSDKHHALF LGRGDQYPIA
     LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR
     GGQLYVFADQ DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR
     NLAKSVTVE
//

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