PURR_ECOLI
ID PURR_ECOLI Reviewed; 341 AA.
AC P0ACP7; P15039; Q83RB1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=HTH-type transcriptional repressor PurR;
DE AltName: Full=Pur regulon repressor;
DE AltName: Full=Purine nucleotide synthesis repressor;
GN Name=purR; OrderedLocusNames=b1658, JW1650;
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=3058704; DOI=10.1016/s0021-9258(19)77686-8;
RA Rolfes R.J., Zalkin H.;
RT "Escherichia coli gene purR encoding a repressor protein for purine
RT nucleotide synthesis. Cloning, nucleotide sequence, and interaction with
RT the purF operator.";
RL J. Biol. Chem. 263:19653-19661(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=2404765; DOI=10.1111/j.1432-1033.1990.tb15314.x;
RA Meng L.M., Kilstrup M., Nygaard P.;
RT "Autoregulation of PurR repressor synthesis and involvement of purR in the
RT regulation of purB, purC, purL, purMN and guaBA expression in Escherichia
RT coli.";
RL Eur. J. Biochem. 187:373-379(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-7, FUNCTION, AND IDENTIFICATION OF COREPRESSORS.
RX PubMed=2211500; DOI=10.1128/jb.172.10.5637-5642.1990;
RA Rolfes R.J., Zalkin H.;
RT "Purification of the Escherichia coli purine regulon repressor and
RT identification of corepressors.";
RL J. Bacteriol. 172:5637-5642(1990).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CHARACTERIZATION, AND SUBUNIT.
RX PubMed=1400170; DOI=10.1128/jb.174.19.6207-6214.1992;
RA Choi K.Y., Zalkin H.;
RT "Structural characterization and corepressor binding of the Escherichia
RT coli purine repressor.";
RL J. Bacteriol. 174:6207-6214(1992).
RN [8]
RP REVIEW.
RA Zalkin H., Nygaard P.;
RT "Biosynthesis of purine nucleotides.";
RL (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
RL Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
RL Umbarger H.E. (eds.);
RL Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.),
RL pp.561-579, American Society for Microbiology Press, Washington D.C.
RL (1996).
RN [9]
RP FUNCTION IN CARAB REPRESSION.
RX PubMed=14741201; DOI=10.1016/j.jmb.2003.12.024;
RA Devroede N., Thia-Toong T.-L., Gigot D., Maes D., Charlier D.;
RT "Purine and pyrimidine-specific repression of the Escherichia coli carAB
RT operon are functionally and structurally coupled.";
RL J. Mol. Biol. 336:25-42(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH HYPOXANTHINE
RP COREPRESSOR AND PURF OPERATOR DNA.
RX PubMed=7973627; DOI=10.1126/science.7973627;
RA Schumacher M.A., Choi K.Y., Zalkin H., Brennan R.G.;
RT "Crystal structure of LacI member, PurR, bound to DNA: minor groove binding
RT by alpha helices.";
RL Science 266:763-770(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 53-341.
RX PubMed=7553867; DOI=10.1016/0092-8674(95)90243-0;
RA Schumacher M.A., Choi K.Y., Lu F., Zalkin H., Brennan R.G.;
RT "Mechanism of corepressor-mediated specific DNA binding by the purine
RT repressor.";
RL Cell 83:147-155(1995).
RN [12]
RP STRUCTURE BY NMR OF 1-56.
RX PubMed=8591032; DOI=10.1016/s0969-2126(01)00257-x;
RA Nagadoi A., Morikawa S., Nakamura H., Enari M., Kobayashi K., Yamamoto H.,
RA Sampei G., Mizobuchi K., Schumacher M.A., Brennan R.G., Nishimura Y.;
RT "Structural comparison of the free and DNA-bound forms of the purine
RT repressor DNA-binding domain.";
RL Structure 3:1217-1224(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GUANINE COREPRESSOR
RP AND PURF OPERATOR DNA.
RX PubMed=9278422; DOI=10.1074/jbc.272.36.22648;
RA Schumacher M.A., Glasfeld A., Zalkin H., Brennan R.G.;
RT "The X-ray structure of the PurR-guanine-purF operator complex reveals the
RT contributions of complementary electrostatic surfaces and a water-mediated
RT hydrogen bond to corepressor specificity and binding affinity.";
RL J. Biol. Chem. 272:22648-22653(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS GLN-190 AND ALA-190 IN
RP COMPLEXES WITH VARIOUS PURINES AND OPERATOR DNA, AND MUTAGENESIS OF
RP ARG-190.
RX PubMed=9454587; DOI=10.1021/bi971942s;
RA Lu F., Schumacher M.A., Arvidson D.N., Haldimann A., Wanner B.L.,
RA Zalkin H., Brennan R.G.;
RT "Structure-based redesign of corepressor specificity of the Escherichia
RT coli purine repressor by substitution of residue 190.";
RL Biochemistry 37:971-982(1998).
RN [15] {ECO:0007744|PDB:1VPW}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT MET-54 IN COMPLEX WITH
RP HYPOXANTHINE COREPRESSOR AND PURF OPERATOR DNA.
RX PubMed=9628480; DOI=10.1038/nsb0698-436;
RA Arvidson D.N., Lu F., Faber C., Zalkin H., Brennan R.G.;
RT "The structure of PurR mutant L54M shows an alternative route to DNA
RT kinking.";
RL Nat. Struct. Biol. 5:436-441(1998).
RN [16] {ECO:0007744|PDB:1QP0, ECO:0007744|PDB:1QP4, ECO:0007744|PDB:1QP7, ECO:0007744|PDB:1QPZ, ECO:0007744|PDB:1QQA, ECO:0007744|PDB:1QQB}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-55 IN
RP COMPLEXES WITH VARIOUS PURF OPERATOR ANALOGS, AND MUTAGENESIS OF LYS-55.
RX PubMed=10438625; DOI=10.1006/jmbi.1999.2946;
RA Glasfeld A., Koehler A.N., Schumacher M.A., Brennan R.G.;
RT "The role of lysine 55 in determining the specificity of the purine
RT repressor for its operators through minor groove interactions.";
RL J. Mol. Biol. 291:347-361(1999).
RN [17] {ECO:0007744|PDB:1ZAY}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH HYPOXANTHINE
RP COREPRESSOR AND PURF OPERATOR ANALOG.
RA Zheleznova E.E., Brennan R.G.;
RT "The roles of exocyclic groups in the central base-pair step in modulating
RT the affinity of PurR for its operator.";
RL Submitted (DEC-1999) to the PDB data bank.
RN [18] {ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1JFT, ECO:0007744|PDB:1JH9, ECO:0007744|PDB:1JHZ}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS ARG-147; PHE-147 AND
RP ALA-147 UNCOMPLEXED AND IN COMPLEX WITH HYPOXANTHINE COREPRESSOR AND PURF
RP OPERATOR DNA, AND MUTAGENESIS OF TRP-147.
RX PubMed=11781089; DOI=10.1021/bi0156660;
RA Huffman J.L., Lu F., Zalkin H., Brennan R.G.;
RT "Role of residue 147 in the gene regulatory function of the Escherichia
RT coli purine repressor.";
RL Biochemistry 41:511-520(2002).
CC -!- FUNCTION: Is the main repressor of the genes involved in the de novo
CC synthesis of purine nucleotides, regulating purB, purC, purEK, purF,
CC purHD, purL, purMN and guaBA expression. In addition, it participates
CC in the regulation or coregulation of genes involved in de novo
CC pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD,
CC carAB and codBA), and of several genes encoding enzymes necessary for
CC nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB).
CC Binds to a 16-bp palindromic sequence located within the promoter
CC region of pur regulon genes. The consensus binding sequence is 5'-
CC ACGCAAACGTTTTCNT-3'. PurR is allosterically activated to bind its
CC cognate DNA by binding the purine corepressors, hypoxanthine or
CC guanine, thereby effecting transcription repression.
CC {ECO:0000269|PubMed:1400170, ECO:0000269|PubMed:14741201,
CC ECO:0000269|PubMed:2211500, ECO:0000269|PubMed:2404765}.
CC -!- PATHWAY: Purine metabolism; purine nucleotide biosynthesis
CC [regulation].
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11781089,
CC ECO:0000269|PubMed:1400170, ECO:0000269|PubMed:7973627,
CC ECO:0000269|PubMed:9278422, ECO:0000269|PubMed:9628480,
CC ECO:0000269|Ref.17}.
CC -!- INTERACTION:
CC P0ACP7; P64503: yebV; NbExp=4; IntAct=EBI-1115258, EBI-9126792;
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:2404765}.
CC -!- DOMAIN: Consists of two structural and functional domains: an N-
CC terminal DNA-binding domain, approximately the first 60 residues, and a
CC larger C-terminal domain, approximately 280 residues, which imparts the
CC function of corepressor binding and oligomerization.
CC -!- MISCELLANEOUS: The corepressors hypoxanthine and guanine bind
CC cooperatively to single PurR sites in each subunit of the dimer,
CC inducing a conformational change which increases the affinity of PurR
CC for its DNA operator sites.
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DR EMBL; J04212; AAA24457.1; -; Genomic_DNA.
DR EMBL; X51368; CAA35753.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74730.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15424.1; -; Genomic_DNA.
DR PIR; A32027; RPECDU.
DR RefSeq; NP_416175.1; NC_000913.3.
DR RefSeq; WP_000190982.1; NZ_STEB01000003.1.
DR PDB; 1BDH; X-ray; 2.70 A; A=2-341.
DR PDB; 1BDI; X-ray; 3.00 A; A=2-341.
DR PDB; 1DBQ; X-ray; 2.20 A; A/B=53-341.
DR PDB; 1JFS; X-ray; 2.90 A; A=2-341.
DR PDB; 1JFT; X-ray; 2.50 A; A=2-341.
DR PDB; 1JH9; X-ray; 2.55 A; A=2-341.
DR PDB; 1JHZ; X-ray; 2.40 A; A/B=53-341.
DR PDB; 1PNR; X-ray; 2.70 A; A=2-341.
DR PDB; 1PRU; NMR; -; A=1-56.
DR PDB; 1PRV; NMR; -; A=1-56.
DR PDB; 1QP0; X-ray; 2.90 A; A=2-341.
DR PDB; 1QP4; X-ray; 3.00 A; A=2-341.
DR PDB; 1QP7; X-ray; 2.90 A; A=2-341.
DR PDB; 1QPZ; X-ray; 2.50 A; A=2-341.
DR PDB; 1QQA; X-ray; 3.00 A; A=2-341.
DR PDB; 1QQB; X-ray; 2.70 A; A=2-341.
DR PDB; 1VPW; X-ray; 2.70 A; A=2-341.
DR PDB; 1WET; X-ray; 2.60 A; A=2-341.
DR PDB; 1ZAY; X-ray; 2.70 A; A=2-341.
DR PDB; 2PUA; X-ray; 2.90 A; A=2-341.
DR PDB; 2PUB; X-ray; 2.70 A; A=2-341.
DR PDB; 2PUC; X-ray; 2.60 A; A=2-341.
DR PDB; 2PUD; X-ray; 2.60 A; A=2-341.
DR PDB; 2PUE; X-ray; 2.70 A; A=2-341.
DR PDB; 2PUF; X-ray; 3.00 A; A=2-341.
DR PDB; 2PUG; X-ray; 2.70 A; A=2-341.
DR PDBsum; 1BDH; -.
DR PDBsum; 1BDI; -.
DR PDBsum; 1DBQ; -.
DR PDBsum; 1JFS; -.
DR PDBsum; 1JFT; -.
DR PDBsum; 1JH9; -.
DR PDBsum; 1JHZ; -.
DR PDBsum; 1PNR; -.
DR PDBsum; 1PRU; -.
DR PDBsum; 1PRV; -.
DR PDBsum; 1QP0; -.
DR PDBsum; 1QP4; -.
DR PDBsum; 1QP7; -.
DR PDBsum; 1QPZ; -.
DR PDBsum; 1QQA; -.
DR PDBsum; 1QQB; -.
DR PDBsum; 1VPW; -.
DR PDBsum; 1WET; -.
DR PDBsum; 1ZAY; -.
DR PDBsum; 2PUA; -.
DR PDBsum; 2PUB; -.
DR PDBsum; 2PUC; -.
DR PDBsum; 2PUD; -.
DR PDBsum; 2PUE; -.
DR PDBsum; 2PUF; -.
DR PDBsum; 2PUG; -.
DR AlphaFoldDB; P0ACP7; -.
DR SMR; P0ACP7; -.
DR BioGRID; 4260271; 7.
DR BioGRID; 849611; 1.
DR DIP; DIP-35931N; -.
DR IntAct; P0ACP7; 8.
DR STRING; 511145.b1658; -.
DR jPOST; P0ACP7; -.
DR PaxDb; P0ACP7; -.
DR PRIDE; P0ACP7; -.
DR EnsemblBacteria; AAC74730; AAC74730; b1658.
DR EnsemblBacteria; BAA15424; BAA15424; BAA15424.
DR GeneID; 66674449; -.
DR GeneID; 945226; -.
DR KEGG; ecj:JW1650; -.
DR KEGG; eco:b1658; -.
DR PATRIC; fig|1411691.4.peg.599; -.
DR EchoBASE; EB0793; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR InParanoid; P0ACP7; -.
DR OMA; ARWVGPP; -.
DR PhylomeDB; P0ACP7; -.
DR BioCyc; EcoCyc:PD00219; -.
DR BioCyc; MetaCyc:PD00219; -.
DR UniPathway; UPA00488; -.
DR EvolutionaryTrace; P0ACP7; -.
DR PRO; PR:P0ACP7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:EcoCyc.
DR GO; GO:0002057; F:guanine binding; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:1900372; P:negative regulation of purine nucleotide biosynthetic process; IMP:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR HAMAP; MF_01277; HTH_type_PurR; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR023588; Tscrpt_reg_HTH_PurR.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Purine biosynthesis;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211500"
FT CHAIN 2..341
FT /note="HTH-type transcriptional repressor PurR"
FT /id="PRO_0000107976"
FT DOMAIN 2..56
FT /note="HTH lacI-type"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT DNA_BIND 48..56
FT BINDING 73
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000269|PubMed:11781089,
FT ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17,
FT ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1VPW,
FT ECO:0007744|PDB:1ZAY"
FT BINDING 190
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000269|PubMed:11781089,
FT ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17,
FT ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1VPW,
FT ECO:0007744|PDB:1ZAY"
FT BINDING 192
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000269|PubMed:11781089,
FT ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17,
FT ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1VPW,
FT ECO:0007744|PDB:1ZAY"
FT BINDING 221
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000269|PubMed:11781089,
FT ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17,
FT ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1VPW,
FT ECO:0007744|PDB:1ZAY"
FT BINDING 275
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000269|PubMed:11781089,
FT ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17,
FT ECO:0007744|PDB:1JFS, ECO:0007744|PDB:1VPW,
FT ECO:0007744|PDB:1ZAY"
FT SITE 190
FT /note="Is the key determinant of 6-oxopurine corepressor
FT specificity"
FT MUTAGEN 54
FT /note="L->M: Slight decrease in operator DNA affinity."
FT MUTAGEN 55
FT /note="K->A: Decrease in operator DNA affinity."
FT /evidence="ECO:0000269|PubMed:10438625"
FT MUTAGEN 147
FT /note="W->A: 14-fold increase in corepressor affinity.
FT Large increase in repressor activity."
FT /evidence="ECO:0000269|PubMed:11781089"
FT MUTAGEN 147
FT /note="W->F: Large decrease in corepressor affinity and in
FT repressor activity."
FT /evidence="ECO:0000269|PubMed:11781089"
FT MUTAGEN 147
FT /note="W->R: 8-fold increase in corepressor affinity. Large
FT increase in repressor activity."
FT /evidence="ECO:0000269|PubMed:11781089"
FT MUTAGEN 190
FT /note="R->A: Functional repressor. Corepressor specificity
FT is expanded since it allows binding of adenine and 6-
FT methylpurine."
FT /evidence="ECO:0000269|PubMed:9454587"
FT MUTAGEN 190
FT /note="R->Q: Functional repressor. Corepressor specificity
FT is expanded since it allows binding of adenine."
FT /evidence="ECO:0000269|PubMed:9454587"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1JFT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1PRU"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:1JFT"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:1JFT"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:1JFT"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1JH9"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1DBQ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:1DBQ"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1DBQ"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1DBQ"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1QPZ"
SQ SEQUENCE 341 AA; 38175 MW; 5D1DA7CA6C72FBBC CRC64;
MATIKDVAKR ANVSTTTVSH VINKTRFVAE ETRNAVWAAI KELHYSPSAV ARSLKVNHTK
SIGLLATSSE AAYFAEIIEA VEKNCFQKGY TLILGNAWNN LEKQRAYLSM MAQKRVDGLL
VMCSEYPEPL LAMLEEYRHI PMVVMDWGEA KADFTDAVID NAFEGGYMAG RYLIERGHRE
IGVIPGPLER NTGAGRLAGF MKAMEEAMIK VPESWIVQGD FEPESGYRAM QQILSQPHRP
TAVFCGGDIM AMGALCAADE MGLRVPQDVS LIGYDNVRNA RYFTPALTTI HQPKDSLGET
AFNMLLDRIV NKREEPQSIE VHPRLIERRS VADGPFRDYR R
