K1A_STIHL
ID K1A_STIHL Reviewed; 35 AA.
AC P29187;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Kappa-stichotoxin-She3a {ECO:0000303|PubMed:22683676};
DE Short=Kappa-SHTX-She3a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Potassium channel toxin ShK {ECO:0000303|PubMed:7660365};
OS Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=6123;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Nematoblast;
RX PubMed=7660365; DOI=10.1016/0041-0101(95)00013-c;
RA Castaneda O., Sotolongo V., Amor A.M., Stoecklin R., Anderson A.J.,
RA Harvey A.L., Engstrom A., Wernstedt C., Karlsson E.;
RT "Characterization of a potassium channel toxin from the Caribbean Sea
RT anemone Stichodactyla helianthus.";
RL Toxicon 33:603-613(1995).
RN [2]
RP PROTEIN SEQUENCE.
RA Karlsson E., Harvey A.L., Aneiros A., Castaneda O.;
RL (In) Xeme congres europeen de toxinologie, pp.35-35, Paris (1992).
RN [3]
RP DISULFIDE BONDS, AND SIMILARITY.
RA Stoecklin R., Harvey A.L., Karlsson E.;
RL (In) 11th congress on animal, plant and microbial toxins,
RL International Society on Toxinology, pp.132-132, Tel Aviv University,
RL Tel Aviv (1994).
RN [4]
RP FUNCTION, AND SYNTHESIS.
RX PubMed=8567178; DOI=10.1111/j.1399-3011.1995.tb01068.x;
RA Pennington M.W., Byrnes M.E., Zaydenberg I., Khaytin I., de Chastonay J.,
RA Krafte D.S., Hill R., Mahnir V.M., Volberg W.A., Gorczyca W.;
RT "Chemical synthesis and characterization of ShK toxin: a potent potassium
RT channel inhibitor from a sea anemone.";
RL Int. J. Pept. Protein Res. 46:354-358(1995).
RN [5]
RP DISULFIDE BONDS.
RA Pohl J., Hubalek F., Byrnes M.E., Nielsen K.R., Woods A., Pennington M.W.;
RT "Assignment of the three disulfide bonds in ShK toxin. A potent potassium
RT channel inhibitor from the sea anemone Stichodactyla helianthus.";
RL Lett. Pept. Sci. 1:291-297(1995).
RN [6]
RP FUNCTION, MUTAGENESIS OF LYS-9; ARG-11 AND LYS-22, AND SITES LYS-9; ARG-11
RP AND LYS-22.
RX PubMed=8645244; DOI=10.1006/bbrc.1996.0297;
RA Pennington M.W., Mahnir V.M., Krafte D.S., Zaydenberg I., Byrnes M.E.,
RA Khaytin I., Crowley K., Kem W.R.;
RT "Identification of three separate binding sites on SHK toxin, a potent
RT inhibitor of voltage-dependent potassium channels in human T-lymphocytes
RT and rat brain.";
RL Biochem. Biophys. Res. Commun. 219:696-701(1996).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF SER-20.
RX PubMed=10419508; DOI=10.1074/jbc.274.31.21885;
RA Rauer H., Pennington M., Cahalan M., Chandy K.G.;
RT "Structural conservation of the pores of calcium-activated and voltage-
RT gated potassium channels determined by a sea anemone toxin.";
RL J. Biol. Chem. 274:21885-21892(1999).
RN [8]
RP FUNCTION.
RX PubMed=15665253; DOI=10.1124/mol.104.008193;
RA Beeton C., Pennington M.W., Wulff H., Singh S., Nugent D., Crossley G.,
RA Khaytin I., Calabresi P.A., Chen C.Y., Gutman G.A., Chandy K.G.;
RT "Targeting effector memory T cells with a selective peptide inhibitor of
RT Kv1.3 channels for therapy of autoimmune diseases.";
RL Mol. Pharmacol. 67:1369-1381(2005).
RN [9]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
RN [10]
RP FUNCTION AS ANTIBIOTIC.
RX PubMed=28796463; DOI=10.1111/febs.14194;
RA Kim C.H., Lee Y.J., Go H.J., Oh H.Y., Lee T.K., Park J.B., Park N.G.;
RT "Defensin-neurotoxin dyad in a basally branching metazoan sea anemone.";
RL FEBS J. 284:3320-3338(2017).
RN [11]
RP REVIEW.
RX PubMed=21867724; DOI=10.1016/j.toxicon.2011.07.016;
RA Chi V., Pennington M.W., Norton R.S., Tarcha E.J., Londono L.M.,
RA Sims-Fahey B., Upadhyay S.K., Lakey J.T., Iadonato S., Wulff H., Beeton C.,
RA Chandy K.G.;
RT "Development of a sea anemone toxin as an immunomodulator for therapy of
RT autoimmune diseases.";
RL Toxicon 59:529-546(2012).
RN [12]
RP REVIEW.
RX PubMed=29316700; DOI=10.3390/toxins10010036;
RA Prentis P.J., Pavasovic A., Norton R.S.;
RT "Sea anemones: quiet achievers in the field of peptide toxins.";
RL Toxins 10:0-0(2018).
RN [13]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=8599755; DOI=10.1038/nsb0496-317;
RA Tudor J.E., Pallaghy P.K., Pennington M.W., Norton R.S.;
RT "Solution structure of ShK toxin, a novel potassium channel inhibitor from
RT a sea anemone.";
RL Nat. Struct. Biol. 3:317-320(1996).
RN [14]
RP STRUCTURE BY NMR, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=9830012; DOI=10.1074/jbc.273.49.32697;
RA Kalman K., Pennington M.W., Lanigan M.D., Nguyen A., Rauer H., Mahnir V.,
RA Paschetto K., Kem W.R., Grissmer S., Gutman G.A., Christian E.P.,
RA Cahalan M.D., Norton R.S., Chandy K.G.;
RT "ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide.";
RL J. Biol. Chem. 273:32697-32707(1998).
RN [15]
RP STRUCTURE BY NMR OF SHK WITHOUT DISULFIDE BOND BETWEEN CYS-3 AND CYS-35,
RP AND FUNCTION.
RX PubMed=10545177; DOI=10.1021/bi991282m;
RA Pennington M.W., Lanigan M.D., Kalman K., Mahnir V.M., Rauer H.,
RA McVaugh C.T., Behm D., Donaldson D., Chandy K.G., Kem W.R., Norton R.S.;
RT "Role of disulfide bonds in the structure and potassium channel blocking
RT activity of ShK toxin.";
RL Biochemistry 38:14549-14558(1999).
RN [16]
RP STRUCTURE BY NMR OF THE SYNTHETIC MUTANT SHK-192, AND 3D-STRUCTURE MODELING
RP OF SHK-192 IN COMPLEX WITH KV1.3 POTASSIUM CHANNEL.
RX PubMed=19122005; DOI=10.1124/mol.108.052704;
RA Pennington M.W., Beeton C., Galea C.A., Smith B.J., Chi V., Monaghan K.P.,
RA Garcia A., Rangaraju S., Giuffrida A., Plank D., Crossley G., Nugent D.,
RA Khaytin I., Lefievre Y., Peshenko I., Dixon C., Chauhan S., Orzel A.,
RA Inoue T., Hu X., Moore R.V., Norton R.S., Chandy K.G.;
RT "Engineering a stable and selective peptide blocker of the Kv1.3 channel in
RT T lymphocytes.";
RL Mol. Pharmacol. 75:762-773(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF SYNTHETIC L-SHK AND D-SHK.
RX PubMed=23919482; DOI=10.1021/ja4046795;
RA Dang B., Kubota T., Mandal K., Bezanilla F., Kent S.B.;
RT "Native chemical ligation at Asx-Cys, Glx-Cys: chemical synthesis and high-
RT resolution X-ray structure of ShK toxin by racemic protein
RT crystallography.";
RL J. Am. Chem. Soc. 135:11911-11919(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF MUTANT GLN-16, FUNCTION,
RP MUTAGENESIS OF ILE-7; ARG-11; GLN-16; SER-20; MET-21; LYS-22; TYR-23 AND
RP PHE-27, AND BIOASSAY.
RX PubMed=26288216; DOI=10.1021/acs.jmedchem.5b00495;
RA Murray J.K., Qian Y.X., Liu B., Elliott R., Aral J., Park C., Zhang X.,
RA Stenkilsson M., Salyers K., Rose M., Li H., Yu S., Andrews K.L.,
RA Colombero A., Werner J., Gaida K., Sickmier E.A., Miu P., Itano A.,
RA McGivern J., Gegg C.V., Sullivan J.K., Miranda L.P.;
RT "Pharmaceutical optimization of peptide toxins for ion channel targets:
RT potent, selective, and long-lived antagonists of Kv1.3.";
RL J. Med. Chem. 58:6784-6802(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF SYNTHETIC [ALLO-ILE7]SHK;
RP [ALLO-THR13]SHK; [ALLO-THR31]SHK AND D-SHK.
RX PubMed=28194851; DOI=10.1002/anie.201612398;
RA Dang B., Shen R., Kubota T., Mandal K., Bezanilla F., Roux B., Kent S.B.;
RT "Inversion of the side-chain stereochemistry of indvidual Thr or Ile
RT residues in a protein molecule: impact on the folding, stability, and
RT structure of the ShK toxin.";
RL Angew. Chem. Int. Ed. 56:3324-3328(2017).
CC -!- FUNCTION: Peptide with both antimicrobial and neurotoxin activities.
CC Inhibits voltage-dependent potassium channels. Potently blocks
CC Kv1.1/KCNA1 (IC(50)=6.7-87 pM) and Kv1.3/KCNA3 (IC(50)=10-250 pM)
CC (PubMed:8567178, PubMed:15665253, PubMed:9830012, PubMed:10545177,
CC PubMed:23919482, PubMed:26288216, PubMed:28194851). Less potently
CC blocks Kv1.4/KCNA4 (IC(50)=0.31 nM), and Kv1.6/KCNA6 (IC(50)=0.16 nM)
CC (PubMed:9830012). Shows moderate activity on Kv1.2/KCNA2 (IC(50)=9 nM),
CC Kv1.7/KCNA7 (IC(50)=11.5 nM), and KCa3.1/KCNN4 (Kd=0.03-30 nM)
CC (PubMed:10419508, PubMed:9830012). Blocks Kv channels by binding to a
CC shallow vestibule at the outer entrance to the ion conduction pathway
CC and occluding the entrance to the pore (PubMed:10419508,
CC PubMed:9830012). Shows antibacterial activity against all tested
CC bacteria (the Gram-positive bacteria B.subtilis and S.aureus, and the
CC Gram-negative bacteria S.typhimurium and P.aeruginosa)
CC (PubMed:28796463). {ECO:0000269|PubMed:10419508,
CC ECO:0000269|PubMed:10545177, ECO:0000269|PubMed:15665253,
CC ECO:0000269|PubMed:23919482, ECO:0000269|PubMed:26288216,
CC ECO:0000269|PubMed:28194851, ECO:0000269|PubMed:7660365,
CC ECO:0000269|PubMed:8567178, ECO:0000269|PubMed:9830012}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.2}. Nematocyst
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4054.82; Mass_error=0.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7660365};
CC -!- PHARMACEUTICAL: Synthetic analog ShK-186 is under clinical trial by
CC 'Kv1.3 Therapeutics, Inc.' under the name dalazatide. Dalazatide has
CC been validated in multiple models of autoimmune disease and has
CC demonstrated proof of concept in a Phase 1b study in psoriasis.
CC Dalazatide is ready to begin Phase 2 clinical studies for inclusion
CC body myositis (IBM) a rare disease with no approved treatment options
CC and generally poor prognosis for the patients. The dalazatide
CC development program is focused on providing a breakthrough treatment
CC first for IBM and then followed by other rare and autoimmune diseases.
CC ShK-186 contains an L-phosphotyrosine attached via an aeea (mini-PEG)
CC hydrophilic linker to Arg-1 and is amidated.
CC {ECO:0000305|PubMed:19122005, ECO:0000305|PubMed:29316700}.
CC -!- MISCELLANEOUS: Does not show or very weak activity on Kv1.5/KCNA5,
CC Kv3.1/KCNC1, and Kv3.4/KCNC4 (IC(50)>100 nM).
CC {ECO:0000269|PubMed:9830012}.
CC -!- MISCELLANEOUS: The synthetic analog ShK-192 has a paraphosphono-Phe
CC (Ppa) at position 0, a Norleucine at position 21, and is amidated. It
CC is stable at acidic pH values and high temperatures. The circulating
CC half-life of the synthetic mutant is estimated to be about 30 minutes
CC in rats. However, low concentrations of functionally active peptide are
CC detected in the blood 72 hours after the injection. The synthetic
CC mutant effectively inhibits the proliferation of T lymphocytes (T(EM))
CC cells in rats and suppresses delayed type hypersensitivity when
CC administered at 10 or 100 ug/kg by subcutaneous injection once daily.
CC {ECO:0000269|PubMed:19122005}.
CC -!- MISCELLANEOUS: The synthetic analog ShK-145 has a 20 kDa polyethylene
CC glycol (PEG), and a Lys at position 16. In vivo, its injection into rat
CC model of multiple sclerosis inhibits the progression of the disease. In
CC addition, weekly administration of ShK-145 suppress interleukin-17 (IL-
CC 17) cytokine secretion from T cells in cynomolgus monkeys and does not
CC show adverse side effects. {ECO:0000269|PubMed:26288216}.
CC -!- MISCELLANEOUS: The synthetic analog ShK-L5 contains a L-phosphotyrosine
CC linked via a hydrophilic linker to the N-terminus of the ShK peptide.
CC It is a highly specific Kv1.3/KCNA3 blocker that exhibits 100-fold
CC selectivity for Kv1.3/KCNA3 over Kv1.1/KCNA1 and greater than 250-fold
CC selectivity over all other channels tested. In vivo, it does not cause
CC cardiac toxicity and does not alter clinical chemistry and
CC hematological parameters after 2-week therapy. It also prevents and
CC treats experimental autoimmune encephalomyelitis and suppresses delayed
CC type hypersensitivity in rats. {ECO:0000269|PubMed:15665253}.
CC -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC family. Type 1a subfamily. {ECO:0000305}.
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DR PDB; 1BEI; NMR; -; A=1-35.
DR PDB; 1C2U; NMR; -; A=1-35.
DR PDB; 1ROO; NMR; -; A=1-35.
DR PDB; 2K9E; NMR; -; A=1-35.
DR PDB; 4LFQ; X-ray; 1.06 A; A=1-35.
DR PDB; 4LFS; X-ray; 0.97 A; A=1-35.
DR PDB; 4Z7P; X-ray; 1.20 A; A=1-35.
DR PDB; 5I5A; X-ray; 1.20 A; A=1-35.
DR PDB; 5I5B; X-ray; 0.90 A; A=1-35.
DR PDB; 5I5C; X-ray; 1.30 A; A/B/C=1-35.
DR PDBsum; 1BEI; -.
DR PDBsum; 1C2U; -.
DR PDBsum; 1ROO; -.
DR PDBsum; 2K9E; -.
DR PDBsum; 4LFQ; -.
DR PDBsum; 4LFS; -.
DR PDBsum; 4Z7P; -.
DR PDBsum; 5I5A; -.
DR PDBsum; 5I5B; -.
DR PDBsum; 5I5C; -.
DR AlphaFoldDB; P29187; -.
DR BMRB; P29187; -.
DR SMR; P29187; -.
DR TCDB; 8.B.14.1.2; the sea anemone peptide toxin, class 1 (bgk) family.
DR EvolutionaryTrace; P29187; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR003582; ShKT_dom.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Nematocyst; Neurotoxin;
KW Pharmaceutical; Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT PEPTIDE 1..35
FT /note="Kappa-stichotoxin-She3a"
FT /evidence="ECO:0000269|PubMed:7660365, ECO:0000269|Ref.2"
FT /id="PRO_0000044866"
FT DOMAIN 3..35
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT SITE 7
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216"
FT SITE 9
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:8645244"
FT SITE 11
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216,
FT ECO:0000269|PubMed:8645244"
FT SITE 20
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216"
FT SITE 21
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216"
FT SITE 22
FT /note="Key residue for binding both Kv1.2/KCNA2 and
FT Kv1.3/KCNA3 (occludes the channel pore like a cork in a
FT bottle)"
FT /evidence="ECO:0000269|PubMed:26288216,
FT ECO:0000269|PubMed:8645244"
FT SITE 23
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216"
FT SITE 27
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000269|PubMed:26288216"
FT DISULFID 3..35
FT /evidence="ECO:0000269|PubMed:8599755,
FT ECO:0000269|PubMed:9830012, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5, ECO:0000312|PDB:1BEI,
FT ECO:0000312|PDB:1ROO, ECO:0000312|PDB:2K9E,
FT ECO:0000312|PDB:4LFQ, ECO:0000312|PDB:4LFS,
FT ECO:0000312|PDB:4Z7P, ECO:0000312|PDB:5I5A,
FT ECO:0000312|PDB:5I5B, ECO:0000312|PDB:5I5C"
FT DISULFID 12..28
FT /evidence="ECO:0000269|PubMed:10545177,
FT ECO:0000269|PubMed:8599755, ECO:0000269|PubMed:9830012,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000312|PDB:1BEI,
FT ECO:0000312|PDB:1C2U, ECO:0000312|PDB:1ROO,
FT ECO:0000312|PDB:2K9E, ECO:0000312|PDB:4LFQ,
FT ECO:0000312|PDB:4LFS, ECO:0000312|PDB:4Z7P,
FT ECO:0000312|PDB:5I5A, ECO:0000312|PDB:5I5B,
FT ECO:0000312|PDB:5I5C"
FT DISULFID 17..32
FT /evidence="ECO:0000269|PubMed:10545177,
FT ECO:0000269|PubMed:8599755, ECO:0000269|PubMed:9830012,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000312|PDB:1BEI,
FT ECO:0000312|PDB:1C2U, ECO:0000312|PDB:1ROO,
FT ECO:0000312|PDB:2K9E, ECO:0000312|PDB:4LFQ,
FT ECO:0000312|PDB:4LFS, ECO:0000312|PDB:4Z7P,
FT ECO:0000312|PDB:5I5A, ECO:0000312|PDB:5I5B,
FT ECO:0000312|PDB:5I5C"
FT MUTAGEN 7
FT /note="I->Q: 10-fold decrease in potency of inhibition of
FT Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216"
FT MUTAGEN 9
FT /note="K->Q: 10-fold decrease in potency of inhibition of
FT Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:8645244"
FT MUTAGEN 11
FT /note="R->Q: 7.5- to 42-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216,
FT ECO:0000269|PubMed:8645244"
FT MUTAGEN 16
FT /note="Q->K: 6.6-fold increase in selectivity for
FT Kv1.3/KCNA3 over Kv1.1/KCNA1, which is marked by a 2.6-fold
FT and 117-fold decrease in potency of inhibition of
FT Kv1.3/KCNA3 and Kv1.1/KCNA1, respectively."
FT /evidence="ECO:0000269|PubMed:26288216"
FT MUTAGEN 20
FT /note="S->A: 20-fold decrease in potency of inhibition of
FT Kv1.3/KCNA3, and 80-fold decrease in potency of inhibition
FT of KCa3.1/KCNN4."
FT /evidence="ECO:0000269|PubMed:10419508"
FT MUTAGEN 20
FT /note="S->Q,R: More than 25-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216"
FT MUTAGEN 21
FT /note="M->Q: More than 25-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216"
FT MUTAGEN 22
FT /note="K->Q,R: More than 25-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216,
FT ECO:0000269|PubMed:8645244"
FT MUTAGEN 23
FT /note="Y->Q,R: More than 25-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216"
FT MUTAGEN 27
FT /note="F->Q,R: More than 25-fold decrease in potency of
FT inhibition of Kv1.3/KCNA3."
FT /evidence="ECO:0000269|PubMed:26288216"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4LFS"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:5I5B"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:5I5B"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:5I5B"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:5I5B"
SQ SEQUENCE 35 AA; 4061 MW; F53EF5D576734B6E CRC64;
RSCIDTIPKS RCTAFQCKHS MKYRLSFCRK TCGTC
