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Cytochrome bo(3) ubiquinol oxidase subunit 1 (EC 1.10.3.10) (Cytochrome b562-o complex subunit I) (Cytochrome o ubiquinol oxidase subunit 1) (Cytochrome o subunit 1) (Oxidase bo(3) subunit 1) (Ubiquinol oxidase chain A) (Ubiquinol oxidase polypeptide I) (Ubiquinol oxidase subunit 1)

 CYOB_ECOLI              Reviewed;         663 AA.
P0ABI8; P18401; Q2MBZ5;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
05-JUL-2017, entry version 105.
RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1;
EC=1.10.3.10;
AltName: Full=Cytochrome b562-o complex subunit I;
AltName: Full=Cytochrome o ubiquinol oxidase subunit 1;
Short=Cytochrome o subunit 1;
AltName: Full=Oxidase bo(3) subunit 1;
AltName: Full=Ubiquinol oxidase chain A;
AltName: Full=Ubiquinol oxidase polypeptide I;
AltName: Full=Ubiquinol oxidase subunit 1;
Name=cyoB; OrderedLocusNames=b0431, JW0421;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2162835;
Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.;
"The sequence of the cyo operon indicates substantial structural
similarities between the cytochrome o ubiquinol oxidase of Escherichia
coli and the aa3-type family of cytochrome c oxidases.";
J. Biol. Chem. 265:11185-11192(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
FUNCTION IN UBIQUINOL OXIDATION, FUNCTION IN PROTON ELECTROCHEMICAL
GRADIENT GENERATION, COFACTOR, AND SUBUNIT.
PubMed=6308657; DOI=10.1073/pnas.80.16.4889;
Matsushita K., Patel L., Gennis R.B., Kaback H.R.;
"Reconstitution of active transport in proteoliposomes containing
cytochrome o oxidase and lac carrier protein purified from Escherichia
coli.";
Proc. Natl. Acad. Sci. U.S.A. 80:4889-4893(1983).
[6]
CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBCELLULAR LOCATION.
STRAIN=K12 / KL251/ORF4;
PubMed=6365921;
Kita K., Konishi K., Anraku Y.;
"Terminal oxidases of Escherichia coli aerobic respiratory chain. I.
Purification and properties of cytochrome b562-o complex from cells in
the early exponential phase of aerobic growth.";
J. Biol. Chem. 259:3368-3374(1984).
[7]
TOPOLOGY.
PubMed=2165491;
Chepuri V., Gennis R.B.;
"The use of gene fusions to determine the topology of all of the
subunits of the cytochrome o terminal oxidase complex of Escherichia
coli.";
J. Biol. Chem. 265:12978-12986(1990).
[8]
TOPOLOGY.
PubMed=2168206; DOI=10.1016/0005-2728(90)90231-R;
Chepuri V., Lemieux L., Hill J., Alben J.O., Gennis R.B.;
"Recent studies of the cytochrome o terminal oxidase complex of
Escherichia coli.";
Biochim. Biophys. Acta 1018:124-127(1990).
[9]
COPPER-BINDING, HEME-BINDING, COFACTOR, AND MUTAGENESIS OF HIS-54;
HIS-106; HIS-284; HIS-333; HIS-334; HIS-411; HIS-419 AND HIS-421.
PubMed=1309808;
Minagawa J., Mogi T., Gennis R.B., Anraku Y.;
"Identification of heme and copper ligands in subunit I of the
cytochrome bo complex in Escherichia coli.";
J. Biol. Chem. 267:2096-2104(1992).
[10]
MUTAGENESIS OF LYS-55; ARG-80; ASP-135; TYR-173; ASP-188;
256-ASP-ARG-257; GLU-286; TYR-288; LYS-362; ASP-407; 481-ARG-ARG-482
AND GLU-540.
PubMed=9378723; DOI=10.1093/oxfordjournals.jbchem.a021770;
Kawasaki M., Mogi T., Anraku Y.;
"Substitutions of charged amino acid residues conserved in subunit I
perturb the redox metal centers of the Escherichia coli bo-type
ubiquinol oxidase.";
J. Biochem. 122:422-429(1997).
[11]
PROBABLE HIGH AFFINITY-QUINONE BINDING (QH), COFACTOR, AND MUTAGENESIS
OF ARG-71; ASP-75; HIS-98 AND ILE-102.
PubMed=12186553; DOI=10.1021/bi012146w;
Hellwig P., Yano T., Ohnishi T., Gennis R.B.;
"Identification of the residues involved in stabilization of the
semiquinone radical in the high-affinity ubiquinone binding site in
cytochrome bo(3) from Escherichia coli by site-directed mutagenesis
and EPR spectroscopy.";
Biochemistry 41:10675-10679(2002).
[12]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[13]
MUTAGENESIS OF ASP-75.
PubMed=17267395; DOI=10.1074/jbc.M611595200;
Yap L.L., Samoilova R.I., Gennis R.B., Dikanov S.A.;
"Characterization of mutants that change the hydrogen bonding of the
semiquinone radical at the QH site of the cytochrome bo3 from
Escherichia coli.";
J. Biol. Chem. 282:8777-8785(2007).
[14]
FUNCTION AS AN OXIDASE, FUNCTION AS A PROTON PUMP, AND DISRUPTION
PHENOTYPE.
STRAIN=K12;
PubMed=19542282; DOI=10.1128/JB.00562-09;
Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
"Respiration of Escherichia coli can be fully uncoupled via the
nonelectrogenic terminal cytochrome bd-II oxidase.";
J. Bacteriol. 191:5510-5517(2009).
[15]
FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, AND
DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=22843529; DOI=10.1128/AEM.01507-12;
Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.;
"Uncoupling of substrate-level phosphorylation in Escherichia coli
during glucose-limited growth.";
Appl. Environ. Microbiol. 78:6908-6913(2012).
[16]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), HEME-BINDING, COPPER-BINDING,
PROBABLE UBIQUINE-BINDING, PROBABLE PROTON CHANNELS, COFACTOR,
SUBUNIT, AND MUTAGENESIS OF ARG-71; ASP-75; HIS-98 AND GLN-101.
PubMed=11017202; DOI=10.1038/82824;
Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M.,
Puustinen A., Iwata S., Wikstrom M.;
"The structure of the ubiquinol oxidase from Escherichia coli and its
ubiquinone binding site.";
Nat. Struct. Biol. 7:910-917(2000).
-!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the
component of the aerobic respiratory chain of E.coli that
predominates when cells are grown at high aeration. Has proton
pump activity across the membrane in addition to electron
transfer, pumping 2 protons/electron. Protons are probably pumped
via D- and K- channels found in this subunit (PubMed:11017202).
{ECO:0000269|PubMed:11017202, ECO:0000269|PubMed:19542282,
ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:6308657}.
-!- CATALYTIC ACTIVITY: 2 ubiquinol + O(2) + n H(+)(Side 1) = 2
ubiquinone + 2 H(2)O + n H(+)(Side 2).
{ECO:0000269|PubMed:6365921}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Note=Binds 1 copper B ion per subunit.;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 low-spin heme b per subunit.;
-!- COFACTOR:
Name=heme o; Xref=ChEBI:CHEBI:24480;
Note=Binds 1 high-spin heme o per subunit.;
-!- COFACTOR:
Name=a quinone; Xref=ChEBI:CHEBI:36141;
Note=Binds 1 high-affinity quinone that appears to function as a
tightly bound cofactor (QH), forming a semiquinone intermediate in
the reaction.;
-!- ENZYME REGULATION: Competitively inhibited by piericidin A, non-
competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide,
NaN(3) and KCN; 50% inhibition occurs at 2 uM, 2 uM, 15 mM and 10
uM, respectively. Inhibited by Zn(2+) and Cd(2+).
{ECO:0000269|PubMed:6365921}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for ubiquinol-1 {ECO:0000269|PubMed:6365921};
KM=50 uM for ubiquinol-6 {ECO:0000269|PubMed:6365921};
Vmax=15.5 umol/min/nmol enzyme with ubiquinol-1
{ECO:0000269|PubMed:6365921};
Vmax=12.6 umol/min/nmol enzyme with ubiquinol-6
{ECO:0000269|PubMed:6365921};
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:6365921};
-!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains
and two D chains. {ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:6308657}.
-!- INTERACTION:
P77806:ybdL; NbExp=3; IntAct=EBI-2932021, EBI-543661;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:6365921}; Multi-pass membrane protein
{ECO:0000269|PubMed:6365921}.
-!- DISRUPTION PHENOTYPE: Increased reduction of the ubiquinone pool
(in aerobically grown minimal medium with glucose).
{ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529}.
-!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in
the electron transport chain.
-!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
{ECO:0000305}.
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EMBL; J05492; AAA23632.1; -; Genomic_DNA.
EMBL; U82664; AAB40187.1; -; Genomic_DNA.
EMBL; U00096; AAC73534.1; -; Genomic_DNA.
EMBL; AP009048; BAE76211.1; -; Genomic_DNA.
PIR; B42226; B42226.
RefSeq; NP_414965.1; NC_000913.3.
RefSeq; WP_000467180.1; NZ_LN832404.1.
PDB; 1FFT; X-ray; 3.50 A; A/F=1-663.
PDBsum; 1FFT; -.
DisProt; DP00088; -.
ProteinModelPortal; P0ABI8; -.
SMR; P0ABI8; -.
BioGrid; 4259710; 224.
DIP; DIP-47943N; -.
IntAct; P0ABI8; 3.
STRING; 316385.ECDH10B_0387; -.
TCDB; 3.D.4.5.1; the proton-translocating cytochrome oxidase (cox) superfamily.
PaxDb; P0ABI8; -.
PRIDE; P0ABI8; -.
EnsemblBacteria; AAC73534; AAC73534; b0431.
EnsemblBacteria; BAE76211; BAE76211; BAE76211.
GeneID; 945615; -.
KEGG; ecj:JW0421; -.
KEGG; eco:b0431; -.
PATRIC; fig|1411691.4.peg.1846; -.
EchoBASE; EB0176; -.
EcoGene; EG10179; cyoB.
eggNOG; ENOG4105BZ9; Bacteria.
eggNOG; COG0843; LUCA.
HOGENOM; HOG000085275; -.
InParanoid; P0ABI8; -.
KO; K02298; -.
PhylomeDB; P0ABI8; -.
BioCyc; EcoCyc:CYOB-MONOMER; -.
BioCyc; MetaCyc:CYOB-MONOMER; -.
EvolutionaryTrace; P0ABI8; -.
PRO; PR:P0ABI8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IDA:EcoCyc.
GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IDA:EcoCyc.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IDA:EcoCyc.
GO; GO:0048039; F:ubiquinone binding; IDA:EcoCyc.
GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
GO; GO:0015990; P:electron transport coupled proton transport; IDA:EcoCyc.
Gene3D; 1.20.210.10; -; 1.
InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
InterPro; IPR000883; Cyt_C_Oxase_1.
InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
InterPro; IPR014207; Cyt_c_ubiqinol_oxidase_su1.
PANTHER; PTHR10422; PTHR10422; 1.
Pfam; PF00115; COX1; 1.
PRINTS; PR01165; CYCOXIDASEI.
SUPFAM; SSF81442; SSF81442; 1.
TIGRFAMs; TIGR02843; CyoB; 1.
PROSITE; PS50855; COX1; 1.
PROSITE; PS00077; COX1_CUB; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Copper; Electron transport; Heme; Hydrogen ion transport;
Ion transport; Iron; Membrane; Metal-binding; Oxidoreductase;
Reference proteome; Respiratory chain; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 663 Cytochrome bo(3) ubiquinol oxidase
subunit 1.
/FTId=PRO_0000183476.
TOPO_DOM 1 16 Periplasmic.
TRANSMEM 17 35 Helical; Name=I.
TOPO_DOM 36 52 Cytoplasmic.
TRANSMEM 53 80 Helical; Name=II.
TOPO_DOM 81 95 Periplasmic.
TRANSMEM 96 132 Helical; Name=III.
TOPO_DOM 133 137 Cytoplasmic.
TRANSMEM 138 161 Helical; Name=IV.
TOPO_DOM 162 184 Periplasmic.
TRANSMEM 185 215 Helical; Name=V.
TOPO_DOM 216 224 Cytoplasmic.
TRANSMEM 225 260 Helical; Name=VI.
TOPO_DOM 261 270 Periplasmic.
TRANSMEM 271 307 Helical; Name=VII.
TOPO_DOM 308 311 Cytoplasmic.
TRANSMEM 312 326 Helical; Name=VIII.
TOPO_DOM 327 340 Periplasmic.
TRANSMEM 341 369 Helical; Name=IX.
TOPO_DOM 370 377 Cytoplasmic.
TRANSMEM 378 409 Helical; Name=X.
TOPO_DOM 410 412 Periplasmic.
TRANSMEM 413 445 Helical; Name=XI.
TOPO_DOM 446 448 Cytoplasmic.
TRANSMEM 449 477 Helical; Name=XII.
TOPO_DOM 478 489 Periplasmic.
TRANSMEM 490 521 Helical; Name=XIII.
TOPO_DOM 522 587 Cytoplasmic.
TRANSMEM 588 606 Helical; Name=XIV.
TOPO_DOM 607 613 Periplasmic.
TRANSMEM 614 632 Helical; Name=XV.
TOPO_DOM 633 663 Cytoplasmic.
METAL 106 106 Iron (heme b axial ligand).
METAL 284 284 Copper.
METAL 288 288 Copper. {ECO:0000305}.
METAL 333 333 Copper.
METAL 334 334 Copper.
METAL 419 419 Iron (heme o axial ligand).
METAL 421 421 Iron (heme b axial ligand).
BINDING 71 71 Quinone (QH). {ECO:0000305}.
BINDING 75 75 Quinone (QH). {ECO:0000305}.
BINDING 98 98 Quinone (QH). {ECO:0000305}.
BINDING 101 101 Quinone (QH). {ECO:0000305}.
CROSSLNK 284 288 1'-histidyl-3'-tyrosine (His-Tyr).
{ECO:0000250}.
MUTAGEN 54 54 H->A: 50% quinol oxidase activity.
{ECO:0000269|PubMed:1309808}.
MUTAGEN 55 55 K->Q: No effect.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 71 71 R->H: No quinol oxidase activity.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553}.
MUTAGEN 71 71 R->Q,L: Abolishes quinol oxidase
activity. {ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553}.
MUTAGEN 75 75 D->E: Very similar to wild-type.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553,
ECO:0000269|PubMed:17267395}.
MUTAGEN 75 75 D->H: No quinol oxidase activity, altered
binding of a semiquinone intermediate at
the QH site.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553,
ECO:0000269|PubMed:17267395}.
MUTAGEN 75 75 D->N: Abolishes quinol oxidase activity.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553,
ECO:0000269|PubMed:17267395}.
MUTAGEN 80 80 R->Q: Abolishes quinol oxidase activity.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 98 98 H->F: About 1% quinol oxidase activity.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553}.
MUTAGEN 98 98 H->N: Abolishes enzyme activity.
{ECO:0000269|PubMed:11017202,
ECO:0000269|PubMed:12186553}.
MUTAGEN 101 101 Q->N: Reduces quinol oxidase activity by
75%, decreased affinity for ubiquinol-1.
{ECO:0000269|PubMed:11017202}.
MUTAGEN 102 102 I->W: No quinol oxidase activity.
{ECO:0000269|PubMed:12186553}.
MUTAGEN 106 106 H->A: 2% quinol oxidase activity, loss of
heme b, loss of heme o, loss of Cu(B).
{ECO:0000269|PubMed:1309808}.
MUTAGEN 135 135 D->N: Abolishes quinol oxidase activity.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 173 173 Y->F: No effect.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 188 188 D->N: No effect.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 256 256 D->N: No effect.
MUTAGEN 257 257 R->Q: Abolishes quinol oxidase activity.
MUTAGEN 284 284 H->A: 1% quinol oxidase activity, loss of
heme o. {ECO:0000269|PubMed:1309808}.
MUTAGEN 286 286 E->Q,D: Great decrease in quinol oxidase
activity. {ECO:0000269|PubMed:9378723}.
MUTAGEN 288 288 Y->F: Great decrease in activity, 100-
fold decrease in heme b-to-heme o
electron transfer.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 333 333 H->A: 2% quinol oxidase activity, loss of
Cu(B). {ECO:0000269|PubMed:1309808}.
MUTAGEN 334 334 H->A: 1% quinol oxidase activity, loss of
Cu(B). {ECO:0000269|PubMed:1309808}.
MUTAGEN 362 362 K->Q: Abolishes quinol oxidase activity,
100-fold decrease in heme b-to-heme o
electron transfer.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 407 407 D->N: Abolishes quinol oxidase activity.
{ECO:0000269|PubMed:9378723}.
MUTAGEN 411 411 H->A: 50% quinol oxidase activity.
{ECO:0000269|PubMed:1309808}.
MUTAGEN 419 419 H->A: 3% quinol oxidase activity, loss of
heme o, loss of Cu(B).
{ECO:0000269|PubMed:1309808}.
MUTAGEN 421 421 H->A: 1% quinol oxidase activity, loss of
heme b, some loss of Cu(B).
{ECO:0000269|PubMed:1309808}.
MUTAGEN 481 481 R->Q: No effect.
MUTAGEN 482 482 R->Q: No effect.
MUTAGEN 540 540 E->Q: Abolishes quinol oxidase activity.
{ECO:0000269|PubMed:9378723}.
HELIX 54 79 {ECO:0000244|PDB:1FFT}.
TURN 80 84 {ECO:0000244|PDB:1FFT}.
STRAND 85 88 {ECO:0000244|PDB:1FFT}.
HELIX 97 112 {ECO:0000244|PDB:1FFT}.
HELIX 117 131 {ECO:0000244|PDB:1FFT}.
HELIX 139 160 {ECO:0000244|PDB:1FFT}.
TURN 161 163 {ECO:0000244|PDB:1FFT}.
TURN 169 172 {ECO:0000244|PDB:1FFT}.
TURN 174 176 {ECO:0000244|PDB:1FFT}.
HELIX 186 214 {ECO:0000244|PDB:1FFT}.
HELIX 222 224 {ECO:0000244|PDB:1FFT}.
HELIX 227 241 {ECO:0000244|PDB:1FFT}.
HELIX 244 259 {ECO:0000244|PDB:1FFT}.
TURN 266 269 {ECO:0000244|PDB:1FFT}.
HELIX 272 289 {ECO:0000244|PDB:1FFT}.
HELIX 292 306 {ECO:0000244|PDB:1FFT}.
HELIX 313 325 {ECO:0000244|PDB:1FFT}.
HELIX 331 334 {ECO:0000244|PDB:1FFT}.
TURN 335 339 {ECO:0000244|PDB:1FFT}.
HELIX 342 354 {ECO:0000244|PDB:1FFT}.
HELIX 357 368 {ECO:0000244|PDB:1FFT}.
TURN 369 372 {ECO:0000244|PDB:1FFT}.
HELIX 379 401 {ECO:0000244|PDB:1FFT}.
HELIX 404 408 {ECO:0000244|PDB:1FFT}.
TURN 409 412 {ECO:0000244|PDB:1FFT}.
HELIX 414 425 {ECO:0000244|PDB:1FFT}.
TURN 426 428 {ECO:0000244|PDB:1FFT}.
HELIX 429 444 {ECO:0000244|PDB:1FFT}.
HELIX 450 476 {ECO:0000244|PDB:1FFT}.
HELIX 491 520 {ECO:0000244|PDB:1FFT}.
TURN 539 542 {ECO:0000244|PDB:1FFT}.
SEQUENCE 663 AA; 74368 MW; 17357B8D44C7CF84 CRC64;
MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT SVDHKRLGIM
YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI
GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNVSL GVGEFAQTGW LAYPPLSGIE
YSPGVGVDYW IWSLQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII
ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG
VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF
HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYALGFMGMT
RRLSQQIDPQ FHTMLMIAAS GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE
WATSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST
IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH FDEITKAGLK
NGN


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