CP121_MYCTU
ID CP121_MYCTU Reviewed; 396 AA.
AC P9WPP7; L0TAQ4; P0A514; Q59571;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Mycocyclosin synthase;
DE EC=1.14.19.70 {ECO:0000269|PubMed:19416919};
DE AltName: Full=Cytochrome P450 121;
DE AltName: Full=Cytochrome P450 MT2;
GN Name=cyp121; OrderedLocusNames=Rv2276; ORFNames=MTCY339.34c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION.
RA Souter A., McLean K.J., Smith W.E., Munro A.W.;
RT "The genome sequence of Mycobacterium tuberculosis reveals cytochromes P450
RT as novel anti-TB drug targets.";
RL J. Chem. Technol. Biotechnol. 75:933-941(2000).
RN [3]
RP FUNCTION, COFACTOR, CIRCULAR DICHROISM ANALYSIS, EPR SPECTROSCOPY, MAGNETIC
RP CIRCULAR DICHROISM, MASS SPECTROMETRY, AND RESONANCE RAMAN SPECTROSCOPY.
RX PubMed=12237220; DOI=10.1016/s0162-0134(02)00479-8;
RA McLean K.J., Cheesman M.R., Rivers S.L., Richmond A., Leys D.,
RA Chapman S.K., Reid G.A., Price N.C., Kelly S.M., Clarkson J., Smith W.E.,
RA Munro A.W.;
RT "Expression, purification and spectroscopic characterization of the
RT cytochrome P450 CYP121 from Mycobacterium tuberculosis.";
RL J. Inorg. Biochem. 91:527-541(2002).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=11914502; DOI=10.1107/s0907444902002676;
RA Mowat C.G., Leys D., McLean K.J., Rivers S.L., Richmond A., Munro A.W.,
RA Ortiz Lombardia M., Alzari P.M., Reid G.A., Chapman S.K., Walkinshaw M.D.;
RT "Crystallization and preliminary crystallographic analysis of a novel
RT cytochrome P450 from Mycobacterium tuberculosis.";
RL Acta Crystallogr. D 58:704-705(2002).
RN [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS) IN COMPLEX WITH HEME, AND COFACTOR.
RX PubMed=12435731; DOI=10.1074/jbc.m209928200;
RA Leys D., Mowat C.G., McLean K.J., Richmond A., Chapman S.K.,
RA Walkinshaw M.D., Munro A.W.;
RT "Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals
RT novel features of cytochrome P450.";
RL J. Biol. Chem. 278:5141-5147(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE,
RP AND COFACTOR.
RX PubMed=17028183; DOI=10.1074/jbc.m607665200;
RA Seward H.E., Roujeinikova A., McLean K.J., Munro A.W., Leys D.;
RT "Crystal structure of the Mycobacterium tuberculosis P450 CYP121-
RT fluconazole complex reveals new azole drug-P450 binding mode.";
RL J. Biol. Chem. 281:39437-39443(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF MUTANTS IN COMPLEX WITH HEME,
RP MUTAGENESIS OF ALA-233; SER-237; SER-279; PHE-338; PRO-346 AND ARG-386,
RP COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=18818197; DOI=10.1074/jbc.m802115200;
RA McLean K.J., Carroll P., Lewis D.G., Dunford A.J., Seward H.E., Neeli R.,
RA Cheesman M.R., Marsollier L., Douglas P., Smith W.E., Rosenkrands I.,
RA Cole S.T., Leys D., Parish T., Munro A.W.;
RT "Characterization of active site structure in CYP121. A cytochrome P450
RT essential for viability of Mycobacterium tuberculosis H37Rv.";
RL J. Biol. Chem. 283:33406-33416(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION
RP MECHANISM, AND COFACTOR.
RX PubMed=19416919; DOI=10.1073/pnas.0812191106;
RA Belin P., Le Du M.H., Fielding A., Lequin O., Jacquet M., Charbonnier J.B.,
RA Lecoq A., Thai R., Courcon M., Masson C., Dugave C., Genet R.,
RA Pernodet J.L., Gondry M.;
RT "Identification and structural basis of the reaction catalyzed by CYP121,
RT an essential cytochrome P450 in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7426-7431(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS, AND COFACTOR.
RX PubMed=22890978; DOI=10.1002/anie.201202544;
RA Hudson S.A., McLean K.J., Surade S., Yang Y.Q., Leys D., Ciulli A.,
RA Munro A.W., Abell C.;
RT "Application of fragment screening and merging to the discovery of
RT inhibitors of the Mycobacterium tuberculosis cytochrome P450 CYP121.";
RL Angew. Chem. Int. Ed. Engl. 51:9311-9316(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 2-396 IN COMPLEX WITH HEME AND
RP SUBSTRATE ANALOGS, SUBSTRATE SPECIFICITY, AND COFACTOR.
RX PubMed=23620594; DOI=10.1074/jbc.m112.443853;
RA Fonvielle M., Le Du M.H., Lequin O., Lecoq A., Jacquet M., Thai R.,
RA Dubois S., Grach G., Gondry M., Belin P.;
RT "Substrate and reaction specificity of Mycobacterium tuberculosis
RT cytochrome P450 CYP121: insights from biochemical studies and crystal
RT structures.";
RL J. Biol. Chem. 288:17347-17359(2013).
CC -!- FUNCTION: Catalyzes C-C bond formation between the carbons ortho to the
CC phenolic hydroxyl of cyclo(L-tyr-L-tyr) (cYY) producing mycocyclosin.
CC Can also use cyclo(L-Tyr-L-Phe) (cYF), cyclo(L-Tyr-L-Trp) (cYW) and
CC cyclo(L-Tyr-L-3,4-dihydroxyphenylalanine) (cY-DOPA) as substrate.
CC {ECO:0000269|PubMed:12237220, ECO:0000269|PubMed:19416919,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclo(L-tyrosyl-L-tyrosyl) + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = 2 H2O + mycoclysin + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:35547, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:65063,
CC ChEBI:CHEBI:71596; EC=1.14.19.70;
CC Evidence={ECO:0000269|PubMed:19416919};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:12237220, ECO:0000269|PubMed:12435731,
CC ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197,
CC ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978,
CC ECO:0000269|PubMed:23620594};
CC -!- ACTIVITY REGULATION: Inhibited by clotrimazole, econazole,
CC ketoconazole, and miconazole. {ECO:0000269|PubMed:18818197}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.3 uM for cYY (at pH7.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19416919};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=43128; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12237220};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45058.1; -; Genomic_DNA.
DR PIR; H70730; H70730.
DR RefSeq; NP_216792.1; NC_000962.3.
DR RefSeq; WP_003411685.1; NZ_NVQJ01000008.1.
DR PDB; 1N40; X-ray; 1.06 A; A=1-396.
DR PDB; 1N4G; X-ray; 1.80 A; A=1-396.
DR PDB; 2IJ5; X-ray; 1.60 A; A/B/C/D/E/F=1-396.
DR PDB; 2IJ7; X-ray; 1.90 A; A/B/C/D/E/F=1-396.
DR PDB; 3CXV; X-ray; 1.70 A; A=1-396.
DR PDB; 3CXX; X-ray; 1.90 A; A=1-396.
DR PDB; 3CXY; X-ray; 1.45 A; A=1-396.
DR PDB; 3CXZ; X-ray; 1.08 A; A=1-396.
DR PDB; 3CY0; X-ray; 1.90 A; A=1-396.
DR PDB; 3CY1; X-ray; 1.75 A; A=1-396.
DR PDB; 3G5F; X-ray; 1.40 A; A=1-396.
DR PDB; 3G5H; X-ray; 1.40 A; A=1-396.
DR PDB; 4G1X; X-ray; 1.30 A; A=2-396.
DR PDB; 4G2G; X-ray; 2.25 A; A=2-396.
DR PDB; 4G44; X-ray; 1.24 A; A=1-396.
DR PDB; 4G45; X-ray; 1.53 A; A=1-396.
DR PDB; 4G46; X-ray; 1.52 A; A=1-396.
DR PDB; 4G47; X-ray; 1.34 A; A=1-396.
DR PDB; 4G48; X-ray; 1.50 A; A=1-396.
DR PDB; 4ICT; X-ray; 1.80 A; A=3-396.
DR PDB; 4IPS; X-ray; 1.20 A; A=2-396.
DR PDB; 4IPW; X-ray; 1.40 A; A=2-396.
DR PDB; 4IQ7; X-ray; 1.90 A; A=2-396.
DR PDB; 4IQ9; X-ray; 1.40 A; A=2-396.
DR PDB; 5IBD; X-ray; 1.77 A; A=1-396.
DR PDB; 5IBE; X-ray; 1.62 A; A=1-396.
DR PDB; 5IBF; X-ray; 1.70 A; A=1-396.
DR PDB; 5IBG; X-ray; 2.10 A; A=1-396.
DR PDB; 5IBH; X-ray; 2.02 A; A=1-396.
DR PDB; 5IBI; X-ray; 2.20 A; A=1-396.
DR PDB; 5IBJ; X-ray; 2.50 A; A=1-396.
DR PDB; 5OP9; X-ray; 1.46 A; A=1-396.
DR PDB; 6RQ0; X-ray; 1.60 A; A=1-396.
DR PDB; 6RQ1; X-ray; 1.49 A; A=1-396.
DR PDB; 6RQ3; X-ray; 1.50 A; A=1-396.
DR PDB; 6RQ5; X-ray; 1.55 A; A=1-396.
DR PDB; 6RQ6; X-ray; 1.42 A; A=1-396.
DR PDB; 6RQ8; X-ray; 1.41 A; A=1-396.
DR PDB; 6RQ9; X-ray; 1.40 A; A=1-396.
DR PDB; 6RQB; X-ray; 1.46 A; A=1-396.
DR PDB; 6RQD; X-ray; 1.50 A; A=1-396.
DR PDB; 6RQE; X-ray; 1.37 A; A=1-396.
DR PDB; 6TE7; X-ray; 1.50 A; A=1-396.
DR PDB; 6TET; X-ray; 1.50 A; A=1-396.
DR PDB; 6TEV; X-ray; 1.70 A; A=1-396.
DR PDB; 6UPG; X-ray; 1.39 A; A=2-396.
DR PDB; 6UPI; X-ray; 1.81 A; A=2-396.
DR PDB; 7NQM; X-ray; 1.60 A; A=1-396.
DR PDB; 7NQN; X-ray; 1.60 A; A=1-396.
DR PDB; 7NQO; X-ray; 1.60 A; A=1-396.
DR PDBsum; 1N40; -.
DR PDBsum; 1N4G; -.
DR PDBsum; 2IJ5; -.
DR PDBsum; 2IJ7; -.
DR PDBsum; 3CXV; -.
DR PDBsum; 3CXX; -.
DR PDBsum; 3CXY; -.
DR PDBsum; 3CXZ; -.
DR PDBsum; 3CY0; -.
DR PDBsum; 3CY1; -.
DR PDBsum; 3G5F; -.
DR PDBsum; 3G5H; -.
DR PDBsum; 4G1X; -.
DR PDBsum; 4G2G; -.
DR PDBsum; 4G44; -.
DR PDBsum; 4G45; -.
DR PDBsum; 4G46; -.
DR PDBsum; 4G47; -.
DR PDBsum; 4G48; -.
DR PDBsum; 4ICT; -.
DR PDBsum; 4IPS; -.
DR PDBsum; 4IPW; -.
DR PDBsum; 4IQ7; -.
DR PDBsum; 4IQ9; -.
DR PDBsum; 5IBD; -.
DR PDBsum; 5IBE; -.
DR PDBsum; 5IBF; -.
DR PDBsum; 5IBG; -.
DR PDBsum; 5IBH; -.
DR PDBsum; 5IBI; -.
DR PDBsum; 5IBJ; -.
DR PDBsum; 5OP9; -.
DR PDBsum; 6RQ0; -.
DR PDBsum; 6RQ1; -.
DR PDBsum; 6RQ3; -.
DR PDBsum; 6RQ5; -.
DR PDBsum; 6RQ6; -.
DR PDBsum; 6RQ8; -.
DR PDBsum; 6RQ9; -.
DR PDBsum; 6RQB; -.
DR PDBsum; 6RQD; -.
DR PDBsum; 6RQE; -.
DR PDBsum; 6TE7; -.
DR PDBsum; 6TET; -.
DR PDBsum; 6TEV; -.
DR PDBsum; 6UPG; -.
DR PDBsum; 6UPI; -.
DR PDBsum; 7NQM; -.
DR PDBsum; 7NQN; -.
DR PDBsum; 7NQO; -.
DR AlphaFoldDB; P9WPP7; -.
DR SMR; P9WPP7; -.
DR STRING; 83332.Rv2276; -.
DR BindingDB; P9WPP7; -.
DR ChEMBL; CHEMBL1681615; -.
DR DrugBank; DB08761; (3S,6S)-3,6-bis(4-hydroxybenzyl)piperazine-2,5-dione.
DR DrugBank; DB02721; 4-Iodopyrazole.
DR DrugCentral; P9WPP7; -.
DR PaxDb; P9WPP7; -.
DR PRIDE; P9WPP7; -.
DR DNASU; 888373; -.
DR GeneID; 888373; -.
DR KEGG; mtu:Rv2276; -.
DR TubercuList; Rv2276; -.
DR eggNOG; COG2124; Bacteria.
DR OMA; FAHKYEP; -.
DR PhylomeDB; P9WPP7; -.
DR BioCyc; MetaCyc:G185E-6494-MON; -.
DR BRENDA; 1.14.19.70; 3445.
DR BRENDA; 1.14.21.9; 3445.
DR PRO; PR:P9WPP7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070025; F:carbon monoxide binding; IDA:MTBBASE.
DR GO; GO:0009975; F:cyclase activity; IDA:MTBBASE.
DR GO; GO:0020037; F:heme binding; IDA:MTBBASE.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MTBBASE.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IDA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..396
FT /note="Mycocyclosin synthase"
FT /id="PRO_0000052274"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17028183,
FT ECO:0000269|PubMed:19416919"
FT BINDING 85..86
FT /ligand="substrate"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17028183,
FT ECO:0000269|PubMed:19416919"
FT BINDING 286
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:12435731,
FT ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197,
FT ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978,
FT ECO:0000269|PubMed:23620594"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17028183,
FT ECO:0000269|PubMed:19416919"
FT BINDING 343
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:12435731,
FT ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197,
FT ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978,
FT ECO:0000269|PubMed:23620594"
FT BINDING 345
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17028183,
FT ECO:0000269|PubMed:19416919"
FT SITE 168
FT /note="Participates in a stacking interactions with the
FT tyrosyl of cYY"
FT SITE 182
FT /note="Participates in a stacking interactions with the
FT tyrosyl of cYY"
FT SITE 346
FT /note="Important for the position of heme"
FT MUTAGEN 233
FT /note="A->G: Has little effect on the heme conformation but
FT significantly alters the environment of the heme and the
FT affinity for azoles."
FT /evidence="ECO:0000269|PubMed:18818197"
FT MUTAGEN 237
FT /note="S->A: Has little effect on the heme conformation but
FT significantly alters the environment of the heme and the
FT affinity for azoles."
FT /evidence="ECO:0000269|PubMed:18818197"
FT MUTAGEN 279
FT /note="S->A: Has little effect."
FT /evidence="ECO:0000269|PubMed:18818197"
FT MUTAGEN 338
FT /note="F->H: No significant change."
FT /evidence="ECO:0000269|PubMed:18818197"
FT MUTAGEN 346
FT /note="P->I: Considerable effects on the heme macrocycle
FT conformation. Mutant leads to a more planar heme
FT conformation."
FT /evidence="ECO:0000269|PubMed:18818197"
FT MUTAGEN 386
FT /note="R->I: No significant change."
FT /evidence="ECO:0000269|PubMed:18818197"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2IJ5"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5IBH"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 176..194
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 220..250
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2IJ7"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1N40"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:1N40"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1N40"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1N40"
SQ SEQUENCE 396 AA; 43256 MW; 510C3B638419DCCB CRC64;
MTATVLLEVP FSARGDRIPD AVAELRTREP IRKVRTITGA EAWLVSSYAL CTQVLEDRRF
SMKETAAAGA PRLNALTVPP EVVNNMGNIA DAGLRKAVMK AITPKAPGLE QFLRDTANSL
LDNLITEGAP ADLRNDFADP LATALHCKVL GIPQEDGPKL FRSLSIAFMS SADPIPAAKI
NWDRDIEYMA GILENPNITT GLMGELSRLR KDPAYSHVSD ELFATIGVTF FGAGVISTGS
FLTTALISLI QRPQLRNLLH EKPELIPAGV EELLRINLSF ADGLPRLATA DIQVGDVLVR
KGELVLVLLE GANFDPEHFP NPGSIELDRP NPTSHLAFGR GQHFCPGSAL GRRHAQIGIE
ALLKKMPGVD LAVPIDQLVW RTRFQRRIPE RLPVLW
