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Botulinum neurotoxin type G (BoNT/G) (EC 3.4.24.69) (Bontoxilysin-G) [Cleaved into: Botulinum neurotoxin G light chain; Botulinum neurotoxin G heavy chain]

 BXG_CLOBO               Reviewed;        1297 AA.
Q60393;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 126.
RecName: Full=Botulinum neurotoxin type G;
Short=BoNT/G {ECO:0000303|PubMed:8268233};
AltName: Full=Bontoxilysin-G;
Contains:
RecName: Full=Botulinum neurotoxin G light chain;
Short=LC;
EC=3.4.24.69 {ECO:0000269|PubMed:7910017};
Contains:
RecName: Full=Botulinum neurotoxin G heavy chain;
Short=HC;
Flags: Precursor;
Name=botG;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=113 / 30 / NCFB 3012 / Type G;
PubMed=8268233; DOI=10.1016/0167-4781(93)90020-E;
Campbell K., Collins M.D., East A.K.;
"Nucleotide sequence of the gene coding for Clostridium botulinum
(Clostridium argentinense) type G neurotoxin: genealogical comparison
with other clostridial neurotoxins.";
Biochim. Biophys. Acta 1216:487-491(1993).
[2]
IDENTIFICATION OF TOXIN, SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN
TYPE G), HOST RANGE, EPIDEMIOLOGY, AND POSSIBLE RELEASE AS SINGLE
CHAIN.
STRAIN=89 / BL 1353 /Type G;
PubMed=4922309;
Gimenez D.F., Ciccarelli A.S.;
"Another type of Clostridium botulinum.";
Zentralbl. Bakteriol. 215:221-224(1970).
[3]
SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN TYPE G), HOST RANGE,
EPIDEMIOLOGY, AND POSSIBLE RELEASE AS SINGLE CHAIN.
STRAIN=89 / BL 1353 /Type G;
PubMed=74236;
Ciccarelli A.S., Whaley D.N., McCroskey L.M., Gimenez D.F.,
Dowell V.R. Jr., Hatheway C.L.;
"Cultural and physiological characteristics of Clostridium botulinum
type G and the susceptibility of certain animals to its toxin.";
Appl. Environ. Microbiol. 34:843-848(1977).
[4]
HOST RANGE, AND EPIDEMIOLOGY.
DOI=10.1099/00207713-38-4-375;
Sue J.C., Hatheway C.L., Steigerwalt A.G., Brenner D.J.;
"Clostridium argentinense sp. nov.: a genetically homogeneous group
composed of all Strains of Clostridium botulinum toxin type G and some
nontoxigenic strains previously identified as Clostridium subterminale
or Clostridium hastiforme.";
Int. J. Syst. Bacteriol. 38:375-381(1988).
[5]
FUNCTION (BOTULINUM NEUROTOXIN G LIGHT CHAIN), IDENTIFICATION OF
SUBSTRATE, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION (BOTULINUM
NEUROTOXIN G LIGHT CHAIN).
PubMed=7910017; DOI=10.1006/bbrc.1994.1526;
Yamasaki S., Binz T., Hayashi T., Szabo E., Yamasaki N., Eklund M.,
Jahn R., Niemann H.;
"Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat
synaptobrevin 2.";
Biochem. Biophys. Res. Commun. 200:829-835(1994).
[6]
FUNCTION (BOTULINUM NEUROTOXIN TYPE G AND BOTULINUM NEUROTOXIN G HEAVY
CHAIN), IDENTIFICATION OF HOST RECEPTOR (BOTULINUM NEUROTOXIN TYPE G),
AND INTERACTION WITH HOST SYT1 AND SYT2.
STRAIN=Type G;
PubMed=15123599; DOI=10.1074/jbc.M403945200;
Rummel A., Karnath T., Henke T., Bigalke H., Binz T.;
"Synaptotagmins I and II act as nerve cell receptors for botulinum
neurotoxin G.";
J. Biol. Chem. 279:30865-30870(2004).
[7]
FUNCTION (BOTULINUM NEUROTOXIN B HEAVY CHAIN), INTERACTION WITH HOST
SYT1 AND SYT2, AND MUTAGENESIS OF MET-1126; LEU-1191; GLN-1200;
TYR-1262 AND TRP-1268.
STRAIN=Type G;
PubMed=17185412; DOI=10.1073/pnas.0609713104;
Rummel A., Eichner T., Weil T., Karnath T., Gutcaits A., Mahrhold S.,
Sandhoff K., Proia R.L., Acharya K.R., Bigalke H., Binz T.;
"Identification of the protein receptor binding site of botulinum
neurotoxins B and G proves the double-receptor concept.";
Proc. Natl. Acad. Sci. U.S.A. 104:359-364(2007).
[8]
FUNCTION (BOTULINUM NEUROTOXIN TYPE G), FUNCTION (BOTULINUM NEUROTOXIN
G HEAVY CHAIN), AND MUTAGENESIS OF GLN-1200 AND TRP-1268.
PubMed=19650874; DOI=10.1111/j.1471-4159.2009.06298.x;
Rummel A., Haefner K., Mahrhold S., Darashchonak N., Holt M., Jahn R.,
Beermann S., Karnath T., Bigalke H., Binz T.;
"Botulinum neurotoxins C, E and F bind gangliosides via a conserved
binding site prior to stimulation-dependent uptake with botulinum
neurotoxin F utilising the three isoforms of SV2 as second receptor.";
J. Neurochem. 110:1942-1954(2009).
[9] {ECO:0000244|PDB:1ZB7}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-443 IN COMPLEX WITH ZINC,
AND COFACTOR.
PubMed=16008342; DOI=10.1021/bi0505924;
Arndt J.W., Yu W., Bi F., Stevens R.C.;
"Crystal structure of botulinum neurotoxin type G light chain:
serotype divergence in substrate recognition.";
Biochemistry 44:9574-9580(2005).
[10] {ECO:0000244|PDB:3MPP}
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 867-1297, FUNCTION
(BOTULINUM NEUROTOXIN B HEAVY CHAIN), DOMAIN, GANGLIOSIDE-BINDING, AND
MUTAGENESIS OF 1080-SER--TRP-1084.
STRAIN=Type G;
PubMed=20507178; DOI=10.1021/bi100412v;
Schmitt J., Karalewitz A., Benefield D.A., Mushrush D.J., Pruitt R.N.,
Spiller B.W., Barbieri J.T., Lacy D.B.;
"Structural analysis of botulinum neurotoxin type G receptor
binding.";
Biochemistry 49:5200-5205(2010).
[11] {ECO:0000244|PDB:2VXR}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 863-1297, FUNCTION
(BOTULINUM NEUROTOXIN B HEAVY CHAIN), SUBUNIT, AND DOMAIN.
STRAIN=Type G;
PubMed=20219474; DOI=10.1016/J.JMB.2010.02.041;
Stenmark P., Dong M., Dupuy J., Chapman E.R., Stevens R.C.;
"Crystal structure of the botulinum neurotoxin type G binding domain:
insight into cell surface binding.";
J. Mol. Biol. 397:1287-1297(2010).
-!- FUNCTION: Botulinum neurotoxin type G: Botulinum toxin causes
flaccid paralysis by inhibiting neurotransmitter (acetylcholine)
release from the presynaptic membranes of nerve terminals of the
eukaryotic host skeletal and autonomic nervous system, with
frequent heart or respiratory failure (PubMed:15123599). Precursor
of botulinum neurotoxin G which has 2 coreceptors; complex
polysialylated gangliosides found on neural tissue and specific
membrane-anchored proteins found in synaptic vesicles
(PubMed:15123599). Receptor proteins are exposed on host
presynaptic cell membrane during neurotransmitter release, when
the toxin heavy chain (HC) binds to them. Upon synaptic vesicle
recycling the toxin is taken up via the endocytic pathway. When
the pH of the toxin-containing endosome drops a structural
rearrangement occurs so that the N-terminus of the HC forms pores
that allows the light chain (LC) to translocate into the cytosol.
Once in the cytosol the disulfide bond linking the 2 subunits is
reduced and LC cleaves its target protein on synaptic vesicles,
preventing their fusion with the cytoplasmic membrane and thus
neurotransmitter release (By similarity). Binds to host peripheral
neuronal presynaptic membranes via synaptotagmins 1 and 2 (SYT1
and SYT2) (PubMed:15123599). Toxin binds to the membrane proximal
extra-cytoplasmic region of SYT1 and SYT2 that is transiently
exposed outside of cells during exocytosis; exogenous gangliosides
do not enhance binding and subsequent uptake of toxin into host
cells (PubMed:15123599). Toxin activity can be blocked by the
appropriate synaptotagmin protein fragments in cell culture
(PubMed:15123599). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000269|PubMed:15123599}.
-!- FUNCTION: Botulinum neurotoxin G light chain: Has proteolytic
activity. After translocation into the eukaryotic host cytosol
acts as a zinc endopeptidase that cleaves synaptobrevins-1, -2 and
-3 (also called VAMP1, VAMP2 and VAMP3) (PubMed:7910017).
Hydrolyzes the '81-Ala-|-Ala-82' bond of VAMP2, and probably also
the equivalent 'Ala-|-Ala' sites in VAMP1 and VAMP3
(PubMed:7910017). Has low activity on A.californica synaptobrevin
and none on D.melanogaster synaptobrevin or cellubrevin, have a
slightly different sequence (PubMed:7910017).
{ECO:0000269|PubMed:7910017}.
-!- FUNCTION: Botulinum neurotoxin G heavy chain: Responsible for host
cell targeting and translocation of light chain (LC) into host
cytosol. Composed of 3 subdomains; the translocation domain (TD),
and N-terminus and C-terminus of the receptor-binding domain (N-
RBD, C-RBD). The RBD is responsible for the adherence of the toxin
to the cell surface. It simultaneously recognizes 2 coreceptors;
polysialated gangliosides and the receptor proteins SYT1 and SYT2
in close proximity on host synaptic vesicles (PubMed:17185412).
The N-terminus of the TD wraps an extended belt around the
perimeter of the LC, protecting Zn(2+) in the active site; it may
also prevent premature LC dissociation from the translocation
channel and protect toxin prior to translocation (By similarity).
The TD inserts into synaptic vesicle membrane to allow
translocation into the host cytosol (By similarity). Has 2
coreceptors; complex gangliosides found primarily on neural tissue
and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind to
separate sites at the tip of the HC (PubMed:17185412). HC alone
binds to host receptors SYT1 and SYT2; C-RBD interacts with host
SYT2 (PubMed:15123599). Has equal affinity for SYT1 and SYT2;
gangliosides are not required for (or only very slightly improve)
binding to a membrane-anchored receptor fragment (PubMed:17185412,
PubMed:20219474). Has also been shown to only bind SYT1; the assay
methods were different (PubMed:20507178). Binds ganglioside GT1b
(PubMed:20507178). Significantly decreases uptake and toxicity of
whole BoNT/B and BoNT/G (PubMed:19650874).
{ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:15123599,
ECO:0000269|PubMed:17185412, ECO:0000269|PubMed:19650874,
ECO:0000269|PubMed:20219474, ECO:0000269|PubMed:20507178}.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
{ECO:0000269|PubMed:7910017}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16008342};
Note=Binds 1 zinc ion per subunit (PubMed:16008342).
{ECO:0000269|PubMed:16008342};
-!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light
chain (LC) and a heavy chain (HC). The LC has the
proteolytic/pharmacological activity, while the N- and C-termini
of the HC mediate channel formation and toxin binding,
respectively. Interacts with host receptors synaptotagmin-1 and -2
(SYT1 and SYT2) (PubMed:15123599, PubMed:17185412,
PubMed:20219474). {ECO:0000269|PubMed:15123599,
ECO:0000269|PubMed:17185412, ECO:0000269|PubMed:20219474}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin type G: Secreted
{ECO:0000269|PubMed:74236, ECO:0000305|PubMed:4922309}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin G light chain: Secreted
{ECO:0000305|PubMed:74236}. Host cytoplasm, host cytosol
{ECO:0000305|PubMed:7910017}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin G heavy chain: Secreted
{ECO:0000305|PubMed:74236}. Host cell junction, host synapse, host
presynaptic cell membrane {ECO:0000250|UniProtKB:P0DPI0}. Host
cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle
membrane {ECO:0000250|UniProtKB:P0DPI0}; Multi-pass membrane
protein {ECO:0000305}.
-!- DOMAIN: Botulinum neurotoxin G light chain: Has protease activity
(PubMed:7910017). {ECO:0000269|PubMed:7910017}.
-!- DOMAIN: Botulinum neurotoxin G heavy chain: Has 3 functional
domains. The translocation domain (TD) which probably forms
membrane channels to allow light chain (LC) into the host cytosol
(Probable). The C-terminal receptor-binding domain (RBD) has 2
further subdomains, N-RBD (Hcn) and C-RBD (Hcc) (PubMed:20507178,
PubMed:20219474). The N-terminus of the TD wraps an extended belt
around the perimeter of the LC, protecting Zn(2+) in the active
site and may be a pseudosubstrate inhibitor which serves as an
intramolecular chaperone for the LC prior to its translocation
into the host cytosol (By similarity). The RBD binds transiently
exposed coreceptors on the host presynaptic cell membrane
(Probable). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000269|PubMed:20219474, ECO:0000269|PubMed:20507178,
ECO:0000269|PubMed:7910017, ECO:0000305|PubMed:15123599}.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes
are quite frequent.
-!- MISCELLANEOUS: Botulism poisoning is usually food-borne, either by
ingesting toxin or bacterial-contaminated food, or less frequently
by inhalation poisoning. In both cases the neurotoxin binds to the
apical surface of epithelial cells in the gut or airway. Toxin
undergoes receptor-mediated endocytosis (using a different
receptor than on target nerve cells), transcytosis across the
epithelial cells and release into the general circulation. Once in
the general circulation it binds to its target cells.
{ECO:0000250|UniProtKB:P0DPI0}.
-!- MISCELLANEOUS: Type G toxin has been isolated from soil samples
and human autopsy specimens but has not been clearly implicated as
the cause of human paralytic illness or death (Ref.4). Strain 89
was isolated from soil in Mendoza province, Argentiana
(PubMed:4922309). Administration of strain 89 toxin to mouse,
chicken, guinea pig and rhesus monkeys causes botulism symptoms
and in most cases death, while dog and sheep show no signs of
botulism (PubMed:74236). In the original report 5-fold higher
levels of toxin caused botulism and death in sheep
(PubMed:4922309). {ECO:0000269|PubMed:4922309,
ECO:0000269|PubMed:74236, ECO:0000305|Ref.4}.
-!- MISCELLANEOUS: Trypsinization of purified toxin increases its
toxicity, suggesting it is released as a single chain
(PubMed:4922309, PubMed:74236). {ECO:0000305|PubMed:4922309,
ECO:0000305|PubMed:74236}.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
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EMBL; X74162; CAA52275.1; -; Genomic_DNA.
PIR; S39791; S39791.
PDB; 1ZB7; X-ray; 2.35 A; A=1-443.
PDB; 2VXR; X-ray; 1.90 A; A=863-1297.
PDB; 3MPP; X-ray; 1.98 A; G=867-1297.
PDBsum; 1ZB7; -.
PDBsum; 2VXR; -.
PDBsum; 3MPP; -.
SMR; Q60393; -.
DIP; DIP-60790N; -.
IntAct; Q60393; 3.
MINT; Q60393; -.
MEROPS; M27.002; -.
UniLectin; Q60393; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250989; Toxicity of botulinum toxin type G (BoNT/G).
EvolutionaryTrace; Q60393; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 2.
InterPro; IPR000395; Bot/tetX_LC.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 1.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; Host cell junction; Host cell membrane;
Host cytoplasm; Host cytoplasmic vesicle; Host membrane; Host synapse;
Hydrolase; Lipid-binding; Membrane; Metal-binding; Metalloprotease;
Neurotoxin; Protease; Secreted; Toxin; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DPI0}.
CHAIN 2 1297 Botulinum neurotoxin type G.
/FTId=PRO_0000444922.
CHAIN 2 442 Botulinum neurotoxin G light chain.
/FTId=PRO_0000029227.
CHAIN 443 1297 Botulinum neurotoxin G heavy chain.
/FTId=PRO_0000029228.
REGION 446 862 Translocation domain (TD).
{ECO:0000250|UniProtKB:P0DPI0}.
REGION 488 537 Belt. {ECO:0000250|UniProtKB:P0DPI0}.
REGION 868 1073 N-terminus of receptor binding domain (N-
RBD). {ECO:0000269|PubMed:20219474,
ECO:0000269|PubMed:20507178}.
REGION 1089 1297 C-terminus of receptor binding domain (C-
RBD). {ECO:0000269|PubMed:20219474,
ECO:0000269|PubMed:20507178}.
MOTIF 1266 1269 Host ganglioside-binding motif.
{ECO:0000305|PubMed:17185412}.
ACT_SITE 231 231 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 230 230 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1ZB7,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:16008342}.
METAL 234 234 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1ZB7,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:16008342}.
METAL 268 268 Zinc; catalytic. {ECO:0000244|PDB:1ZB7,
ECO:0000269|PubMed:16008342}.
SITE 1268 1268 Ganglioside-binding site.
{ECO:0000305|PubMed:17185412}.
DISULFID 436 450 Interchain (between light and heavy
chains). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000305}.
MUTAGEN 1080 1084 SSLYW->EERYK: Improves solubility of
isolated heavy chain (HC), used for
crystallization.
{ECO:0000269|PubMed:20507178}.
MUTAGEN 1126 1126 M->D: Significantly decreased binding of
HC to host SYT1 and SYT2 independent of
gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1191 1191 L->R: Significantly decreased binding of
HC to host SYT1 and SYT2 independent of
gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1200 1200 Q->E: Significantly decreased binding of
HC to host SYT1 and SYT2 independent of
gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1200 1200 Q->K: Decreased binding of HC to host
SYT1 and SYT2 independent of
gangliosides; whole toxin is less toxic.
Dramatically decreased toxicity; when
associated with L-1268. HC no longer
inhibits whole-toxin uptake and toxicity.
{ECO:0000269|PubMed:17185412,
ECO:0000269|PubMed:19650874}.
MUTAGEN 1262 1262 Y->F: Slightly increased binding of HC to
host SYT1 and SYT2 in presence of
gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1268 1268 W->L: Gangliosides no longer increase HC
affinity for SYT1 or SYT2; whole toxin
about significantly less toxic.
Dramatically decreased toxicity; when
associated with K-1200. In mice without
complex gangliosides no change compared
to wild-type protein. HC no longer
inhibits whole-toxin uptake and toxicity.
{ECO:0000269|PubMed:17185412,
ECO:0000269|PubMed:19650874}.
STRAND 16 23 {ECO:0000244|PDB:1ZB7}.
STRAND 28 30 {ECO:0000244|PDB:1ZB7}.
STRAND 34 40 {ECO:0000244|PDB:1ZB7}.
STRAND 43 46 {ECO:0000244|PDB:1ZB7}.
STRAND 69 74 {ECO:0000244|PDB:1ZB7}.
TURN 76 79 {ECO:0000244|PDB:1ZB7}.
HELIX 82 99 {ECO:0000244|PDB:1ZB7}.
HELIX 103 114 {ECO:0000244|PDB:1ZB7}.
TURN 134 136 {ECO:0000244|PDB:1ZB7}.
STRAND 137 142 {ECO:0000244|PDB:1ZB7}.
STRAND 150 155 {ECO:0000244|PDB:1ZB7}.
STRAND 157 161 {ECO:0000244|PDB:1ZB7}.
STRAND 171 173 {ECO:0000244|PDB:1ZB7}.
HELIX 182 184 {ECO:0000244|PDB:1ZB7}.
STRAND 185 187 {ECO:0000244|PDB:1ZB7}.
STRAND 191 194 {ECO:0000244|PDB:1ZB7}.
STRAND 199 208 {ECO:0000244|PDB:1ZB7}.
STRAND 215 221 {ECO:0000244|PDB:1ZB7}.
HELIX 224 239 {ECO:0000244|PDB:1ZB7}.
HELIX 266 273 {ECO:0000244|PDB:1ZB7}.
TURN 277 279 {ECO:0000244|PDB:1ZB7}.
HELIX 282 303 {ECO:0000244|PDB:1ZB7}.
STRAND 308 313 {ECO:0000244|PDB:1ZB7}.
HELIX 316 327 {ECO:0000244|PDB:1ZB7}.
HELIX 341 353 {ECO:0000244|PDB:1ZB7}.
HELIX 357 364 {ECO:0000244|PDB:1ZB7}.
STRAND 377 381 {ECO:0000244|PDB:1ZB7}.
TURN 388 390 {ECO:0000244|PDB:1ZB7}.
TURN 393 395 {ECO:0000244|PDB:1ZB7}.
HELIX 400 402 {ECO:0000244|PDB:1ZB7}.
HELIX 406 411 {ECO:0000244|PDB:1ZB7}.
TURN 413 415 {ECO:0000244|PDB:1ZB7}.
HELIX 417 419 {ECO:0000244|PDB:1ZB7}.
TURN 425 427 {ECO:0000244|PDB:1ZB7}.
STRAND 428 432 {ECO:0000244|PDB:1ZB7}.
STRAND 870 876 {ECO:0000244|PDB:2VXR}.
STRAND 879 882 {ECO:0000244|PDB:2VXR}.
STRAND 889 892 {ECO:0000244|PDB:2VXR}.
STRAND 897 899 {ECO:0000244|PDB:2VXR}.
STRAND 905 911 {ECO:0000244|PDB:2VXR}.
STRAND 916 919 {ECO:0000244|PDB:2VXR}.
TURN 922 924 {ECO:0000244|PDB:2VXR}.
STRAND 927 930 {ECO:0000244|PDB:2VXR}.
STRAND 933 940 {ECO:0000244|PDB:2VXR}.
HELIX 946 948 {ECO:0000244|PDB:2VXR}.
HELIX 949 954 {ECO:0000244|PDB:2VXR}.
STRAND 956 964 {ECO:0000244|PDB:2VXR}.
STRAND 967 974 {ECO:0000244|PDB:2VXR}.
STRAND 977 983 {ECO:0000244|PDB:2VXR}.
STRAND 989 995 {ECO:0000244|PDB:2VXR}.
STRAND 998 1002 {ECO:0000244|PDB:3MPP}.
STRAND 1010 1016 {ECO:0000244|PDB:2VXR}.
STRAND 1020 1026 {ECO:0000244|PDB:2VXR}.
STRAND 1029 1035 {ECO:0000244|PDB:2VXR}.
STRAND 1046 1054 {ECO:0000244|PDB:2VXR}.
STRAND 1061 1072 {ECO:0000244|PDB:2VXR}.
HELIX 1076 1086 {ECO:0000244|PDB:2VXR}.
STRAND 1097 1099 {ECO:0000244|PDB:2VXR}.
STRAND 1105 1113 {ECO:0000244|PDB:2VXR}.
STRAND 1116 1121 {ECO:0000244|PDB:2VXR}.
HELIX 1122 1124 {ECO:0000244|PDB:2VXR}.
STRAND 1126 1131 {ECO:0000244|PDB:2VXR}.
STRAND 1134 1136 {ECO:0000244|PDB:2VXR}.
STRAND 1141 1143 {ECO:0000244|PDB:2VXR}.
STRAND 1150 1155 {ECO:0000244|PDB:2VXR}.
STRAND 1174 1184 {ECO:0000244|PDB:2VXR}.
STRAND 1186 1191 {ECO:0000244|PDB:2VXR}.
STRAND 1196 1200 {ECO:0000244|PDB:2VXR}.
STRAND 1202 1206 {ECO:0000244|PDB:2VXR}.
STRAND 1216 1219 {ECO:0000244|PDB:2VXR}.
STRAND 1229 1236 {ECO:0000244|PDB:2VXR}.
STRAND 1239 1248 {ECO:0000244|PDB:2VXR}.
STRAND 1260 1267 {ECO:0000244|PDB:2VXR}.
HELIX 1268 1272 {ECO:0000244|PDB:2VXR}.
STRAND 1275 1277 {ECO:0000244|PDB:2VXR}.
STRAND 1286 1289 {ECO:0000244|PDB:2VXR}.
SEQUENCE 1297 AA; 149146 MW; 306CF54CF3973C3B CRC64;
MPVNIKXFNY NDPINNDDII MMEPFNDPGP GTYYKAFRII DRIWIVPERF TYGFQPDQFN
ASTGVFSKDV YEYYDPTYLK TDAEKDKFLK TMIKLFNRIN SKPSGQRLLD MIVDAIPYLG
NASTPPDKFA ANVANVSINK KIIQPGAEDQ IKGLMTNLII FGPGPVLSDN FTDSMIMNGH
SPISEGFGAR MMIRFCPSCL NVFNNVQENK DTSIFSRRAY FADPALTLMH ELIHVLHGLY
GIKISNLPIT PNTKEFFMQH SDPVQAEELY TFGGHDPSVI SPSTDMNIYN KALQNFQDIA
NRLNIVSSAQ GSGIDISLYK QIYKNKYDFV EDPNGKYSVD KDKFDKLYKA LMFGFTETNL
AGEYGIKTRY SYFSEYLPPI KTEKLLDNTI YTQNEGFNIA SKNLKTEFNG QNKAVNKEAY
EEISLEHLVI YRIAMCKPVM YKNTGKSEQC IIVNNEDLFF IANKDSFSKD LAKAETIAYN
TQNNTIENNF SIDQLILDND LSSGIDLPNE NTEPFTNFDD IDIPVYIKQS ALKKIFVDGD
SLFEYLHAQT FPSNIENLQL TNSLNDALRN NNKVYTFFST NLVEKANTVV GASLFVNWVK
GVIDDFTSES TQKSTIDKVS DVSIIIPYIG PALNVGNETA KENFKNAFEI GGAAILMEFI
PELIVPIVGF FTLESYVGNK GHIIMTISNA LKKRDQKWTD MYGLIVSQWL STVNTQFYTI
KERMYNALNN QSQAIEKIIE DQYNRYSEED KMNINIDFND IDFKLNQSIN LAINNIDDFI
NQCSISYLMN RMIPLAVKKL KDFDDNLKRD LLEYIDTNEL YLLDEVNILK SKVNRHLKDS
IPFDLSLYTK DTILIQVFNN YISNISSNAI LSLSYRGGRL IDSSGYGATM NVGSDVIFND
IGNGQFKLNN SENSNITAHQ SKFVVYDSMF DNFSINFWVR TPKYNNNDIQ TYLQNEYTII
SCIKNDSGWK VSIKGNRIIW TLIDVNAKSK SIFFEYSIKD NISDYINKWF SITITNDRLG
NANIYINGSL KKSEKILNLD RINSSNDIDF KLINCTDTTK FVWIKDFNIF GRELNATEVS
SLYWIQSSTN TLKDFWGNPL RYDTQYYLFN QGMQNIYIKY FSKASMGETA PRTNFNNAAI
NYQNLYLGLR FIIKKASNSR NINNDNIVRE GDYIYLNIDN ISDESYRVYV LVNSKEIQTQ
LFLAPINDDP TFYDVLQIKK YYEKTTYNCQ ILCEKDTKTF GLFGIGKFVK DYGYVWDTYD
NYFCISQWYL RRISENINKL RLGCNWQFIP VDEGWTE


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