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Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase)

 PURA_ECOLI              Reviewed;         432 AA.
P0A7D4; P12283; Q2M6C8;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 126.
RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011};
Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011};
Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011};
EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011};
AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011};
Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; Synonyms=adeK;
OrderedLocusNames=b4177, JW4135;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
STRAIN=K12;
PubMed=3058695;
Wolfe S.A., Smith J.M.;
"Nucleotide sequence and analysis of the purA gene encoding
adenylosuccinate synthetase of Escherichia coli K12.";
J. Biol. Chem. 263:19147-19153(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[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]
PROTEIN SEQUENCE OF 146-148, AND MUTAGENESIS OF ARG-148.
PubMed=2061308;
Dong Q., Liu F., Myers A.M., Fromm H.J.;
"Evidence for an arginine residue at the substrate binding site of
Escherichia coli adenylosuccinate synthetase as studied by chemical
modification and site-directed mutagenesis.";
J. Biol. Chem. 266:12228-12233(1991).
[6]
PROTEIN SEQUENCE OF 2-10.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
ACTIVE SITE LYS-141.
PubMed=2108156;
Dong Q., Fromm H.J.;
"Chemical modification of adenylosuccinate synthetase from Escherichia
coli by pyridoxal 5'-phosphate. Identification of an active site lysyl
residue.";
J. Biol. Chem. 265:6235-6240(1990).
[8]
MUTAGENESIS.
PubMed=1733940;
Liu F., Dong Q., Fromm H.J.;
"Site-directed mutagenesis of the phosphate-binding consensus sequence
in Escherichia coli adenylosuccinate synthetase.";
J. Biol. Chem. 267:2388-2392(1992).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO 417.
PubMed=7490761; DOI=10.1006/jmbi.1995.0629;
Silva M.M., Poland B.W., Hoffman C.R., Fromm H.J., Honzatko R.B.;
"Refined crystal structures of unligated adenylosuccinate synthetase
from Escherichia coli.";
J. Mol. Biol. 254:431-446(1995).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GDP; MAGNESIUM;
SUBSTRATE ANALOG AND INHIBITOR.
PubMed=8961938; DOI=10.1021/bi961758r;
Poland B.W., Lee S.F., Subramanian M.V., Siehl D.L., Anderson R.J.,
Fromm H.J., Honzatko R.B.;
"Refined crystal structure of adenylosuccinate synthetase from
Escherichia coli complexed with hydantocidin 5'-phosphate, GDP,
HPO4(2-), Mg2+, and hadacidin.";
Biochemistry 35:15753-15759(1996).
[11]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-431.
PubMed=8663109; DOI=10.1074/jbc.271.26.15407;
Poland B.W., Hou Z., Bruns C., Fromm H.J., Honzatko R.B.;
"Refined crystal structures of guanine nucleotide complexes of
adenylosuccinate synthetase from Escherichia coli.";
J. Biol. Chem. 271:15407-15413(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP; IMP;
MAGNESIUM AND SUBSTRATE ANALOG.
PubMed=9000627; DOI=10.1006/jmbi.1996.0693;
Poland B.W., Fromm H.J., Honzatko R.B.;
"Crystal structures of adenylosuccinate synthetase from Escherichia
coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+.";
J. Mol. Biol. 264:1013-1027(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-431.
PubMed=8790347; DOI=10.1073/pnas.93.18.9431;
Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E.,
Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G.,
Cowan-Jacob S.W.;
"The mode of action and the structure of a herbicide in complex with
its target: binding of activated hydantocidin to the feedback
regulation site of adenylosuccinate synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996).
[14]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-431.
PubMed=9182542; DOI=10.1074/jbc.272.24.15200;
Poland B.W., Bruns C., Fromm H.J., Honzatko R.B.;
"Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline
adenylosuccinate synthetase from Escherichia coli.";
J. Biol. Chem. 272:15200-15205(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
PubMed=10556888;
DOI=10.1002/(SICI)1521-3773(19991102)38:21<3159::AID-ANIE3159>3.0.CO;2-2;
Hanessian S., Lu P.P., Sanceau J.Y., Chemla P., Gohda K.,
Fonne-Pfister R., Prade L., Cowan-Jacob S.W.;
"An enzyme-bound bisubstrate hybrid inhibitor of adenylosuccinate
synthetase.";
Angew. Chem. Int. Ed. Engl. 38:3159-3162(1999).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-17;
LEU-144 AND LEU-304 IN COMPLEX WITH GTP; IMP; MAGNESIUM AND SUBSTRATE
ANALOG.
PubMed=10346917; DOI=10.1021/bi990159s;
Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B.;
"Mechanistic implications from crystalline complexes of wild-type and
mutant adenylosuccinate synthetases from Escherichia coli.";
Biochemistry 38:6953-6961(1999).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=10364182; DOI=10.1074/jbc.274.25.17505;
Hou Z., Cashel M., Fromm H.J., Honzatko R.B.;
"Effectors of the stringent response target the active site of
Escherichia coli adenylosuccinate synthetase.";
J. Biol. Chem. 274:17505-17510(1999).
[18]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-432.
PubMed=11741996; DOI=10.1074/jbc.M109561200;
Hou Z., Wang W., Fromm H.J., Honzatko R.B.;
"IMP alone organizes the active site of adenylosuccinate synthetase
from Escherichia coli.";
J. Biol. Chem. 277:5970-5976(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-431.
PubMed=16981730; DOI=10.1021/bi0607498;
Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.;
"Cavitation as a mechanism of substrate discrimination by
adenylosuccinate synthetases.";
Biochemistry 45:11703-11711(2006).
-!- FUNCTION: Plays an important role in the de novo pathway of purine
nucleotide biosynthesis. Catalyzes the first committed step in the
biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
-!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938,
ECO:0000269|PubMed:9000627}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
{ECO:0000255|HAMAP-Rule:MF_00011}.
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EMBL; J04199; AAA24446.1; -; Genomic_DNA.
EMBL; U14003; AAA97073.1; -; Genomic_DNA.
EMBL; U00096; AAC77134.1; -; Genomic_DNA.
EMBL; AP009048; BAE78178.1; -; Genomic_DNA.
PIR; S56402; AJECDS.
RefSeq; NP_418598.1; NC_000913.3.
RefSeq; WP_000527955.1; NZ_LN832404.1.
PDB; 1ADE; X-ray; 2.00 A; A/B=2-432.
PDB; 1ADI; X-ray; 2.50 A; A/B=2-432.
PDB; 1CG0; X-ray; 2.50 A; A=2-432.
PDB; 1CG1; X-ray; 2.50 A; A=2-432.
PDB; 1CG3; X-ray; 2.50 A; A=2-432.
PDB; 1CG4; X-ray; 2.50 A; A=2-432.
PDB; 1CH8; X-ray; 2.50 A; A=2-432.
PDB; 1CIB; X-ray; 2.30 A; A=2-432.
PDB; 1GIM; X-ray; 2.50 A; A=2-432.
PDB; 1GIN; X-ray; 2.80 A; A=2-432.
PDB; 1HON; X-ray; 2.30 A; A/B=2-432.
PDB; 1HOO; X-ray; 2.30 A; A/B=2-432.
PDB; 1HOP; X-ray; 2.30 A; A/B=2-432.
PDB; 1JUY; X-ray; 2.50 A; A=2-432.
PDB; 1KJX; X-ray; 2.60 A; A=1-432.
PDB; 1KKB; X-ray; 2.60 A; A=1-432.
PDB; 1KKF; X-ray; 2.60 A; A=1-432.
PDB; 1KSZ; X-ray; 2.80 A; A=2-432.
PDB; 1NHT; X-ray; 2.50 A; A=2-432.
PDB; 1QF4; X-ray; 2.20 A; A=2-432.
PDB; 1QF5; X-ray; 2.00 A; A=2-432.
PDB; 1SON; X-ray; 2.55 A; A=2-432.
PDB; 1SOO; X-ray; 2.60 A; A=2-432.
PDB; 2GCQ; X-ray; 2.00 A; A=2-432.
PDBsum; 1ADE; -.
PDBsum; 1ADI; -.
PDBsum; 1CG0; -.
PDBsum; 1CG1; -.
PDBsum; 1CG3; -.
PDBsum; 1CG4; -.
PDBsum; 1CH8; -.
PDBsum; 1CIB; -.
PDBsum; 1GIM; -.
PDBsum; 1GIN; -.
PDBsum; 1HON; -.
PDBsum; 1HOO; -.
PDBsum; 1HOP; -.
PDBsum; 1JUY; -.
PDBsum; 1KJX; -.
PDBsum; 1KKB; -.
PDBsum; 1KKF; -.
PDBsum; 1KSZ; -.
PDBsum; 1NHT; -.
PDBsum; 1QF4; -.
PDBsum; 1QF5; -.
PDBsum; 1SON; -.
PDBsum; 1SOO; -.
PDBsum; 2GCQ; -.
ProteinModelPortal; P0A7D4; -.
SMR; P0A7D4; -.
BioGrid; 4262696; 52.
BioGrid; 852987; 1.
DIP; DIP-36219N; -.
IntAct; P0A7D4; 3.
STRING; 316385.ECDH10B_4372; -.
DrugBank; DB02666; (C8-R)-Hydantocidin 5'-Phosphate.
DrugBank; DB04460; (C8-S)-Hydantocidin 5'-Phosphate.
DrugBank; DB02954; (Carboxyhydroxyamino)Ethanoic Acid.
DrugBank; DB02682; 2-Deamino-6-Deoxy-6thiophosphite-5'-Phosphate Guanosine.
DrugBank; DB03146; 2-Deazo-6-Thiophosphate Guanosine-5'-Monophosphate.
DrugBank; DB02836; Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB02109; Hadacidin.
DrugBank; DB02493; Hydantocidin-5'-Phosphate.
DrugBank; DB04566; Inosinic Acid.
CarbonylDB; P0A7D4; -.
SWISS-2DPAGE; P0A7D4; -.
EPD; P0A7D4; -.
PaxDb; P0A7D4; -.
PRIDE; P0A7D4; -.
EnsemblBacteria; AAC77134; AAC77134; b4177.
EnsemblBacteria; BAE78178; BAE78178; BAE78178.
GeneID; 948695; -.
KEGG; ecj:JW4135; -.
KEGG; eco:b4177; -.
PATRIC; fig|1411691.4.peg.2524; -.
EchoBASE; EB0783; -.
EcoGene; EG10790; purA.
eggNOG; ENOG4105C91; Bacteria.
eggNOG; COG0104; LUCA.
HOGENOM; HOG000260959; -.
InParanoid; P0A7D4; -.
KO; K01939; -.
OMA; SNAGHTV; -.
PhylomeDB; P0A7D4; -.
BioCyc; EcoCyc:ADENYLOSUCCINATE-SYN-MONOMER; -.
BioCyc; MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER; -.
BRENDA; 6.3.4.4; 2026.
SABIO-RK; P0A7D4; -.
UniPathway; UPA00075; UER00335.
EvolutionaryTrace; P0A7D4; -.
PRO; PR:P0A7D4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:EcoCyc.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
GO; GO:0046086; P:adenosine biosynthetic process; IMP:EcoliWiki.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki.
GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:EcoCyc.
CDD; cd03108; AdSS; 1.
HAMAP; MF_00011; Adenylosucc_synth; 1.
InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
InterPro; IPR001114; Adenylosuccinate_synthetase.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11846; PTHR11846; 1.
Pfam; PF00709; Adenylsucc_synt; 1.
SMART; SM00788; Adenylsucc_synt; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00184; purA; 1.
PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
Purine biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3058695,
ECO:0000269|PubMed:9298646}.
CHAIN 2 432 Adenylosuccinate synthetase.
/FTId=PRO_0000095174.
NP_BIND 13 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917}.
NP_BIND 41 43 GTP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917}.
NP_BIND 332 334 GTP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917}.
NP_BIND 415 417 GTP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917}.
REGION 14 17 IMP binding.
REGION 39 42 IMP binding.
REGION 300 306 Substrate binding.
ACT_SITE 14 14 Proton acceptor.
ACT_SITE 42 42 Proton donor.
METAL 14 14 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:8961938,
ECO:0000269|PubMed:9000627}.
METAL 41 41 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:8961938,
ECO:0000269|PubMed:9000627}.
BINDING 130 130 IMP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:9000627}.
BINDING 144 144 IMP; shared with dimeric partner.
{ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:9000627}.
BINDING 225 225 IMP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:9000627}.
BINDING 240 240 IMP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:9000627}.
BINDING 304 304 IMP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917,
ECO:0000269|PubMed:9000627}.
BINDING 306 306 GTP. {ECO:0000255|HAMAP-Rule:MF_00011,
ECO:0000269|PubMed:10346917}.
MUTAGEN 13 13 G->V: Significant reduction in activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 16 16 G->V: Significant reduction in activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 17 17 K->Q: Reduces catalytic efficiency by
50%. {ECO:0000269|PubMed:1733940}.
MUTAGEN 18 18 G->V: Significant reduction in activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 19 19 K->R: Significant reduction in activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 20 20 I->T: Significant reduction in activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 141 141 K->I: Total loss of activity.
{ECO:0000269|PubMed:1733940}.
MUTAGEN 144 144 R->L: Does not reduce catalytic
efficiency. {ECO:0000269|PubMed:1733940}.
MUTAGEN 148 148 R->L: Reduced activity.
{ECO:0000269|PubMed:2061308}.
MUTAGEN 304 304 R->L: Reduces catalytic efficiency by
87%. {ECO:0000269|PubMed:1733940}.
CONFLICT 417 417 G -> D (in Ref. 1; AAA24446).
{ECO:0000305}.
STRAND 4 13 {ECO:0000244|PDB:1ADE}.
HELIX 17 24 {ECO:0000244|PDB:1ADE}.
TURN 25 27 {ECO:0000244|PDB:1ADE}.
STRAND 29 33 {ECO:0000244|PDB:1ADE}.
STRAND 42 46 {ECO:0000244|PDB:1ADE}.
STRAND 49 56 {ECO:0000244|PDB:1ADE}.
HELIX 58 61 {ECO:0000244|PDB:1ADE}.
STRAND 62 64 {ECO:0000244|PDB:1HOO}.
STRAND 66 69 {ECO:0000244|PDB:1ADE}.
HELIX 77 89 {ECO:0000244|PDB:1ADE}.
HELIX 94 97 {ECO:0000244|PDB:1ADE}.
STRAND 98 100 {ECO:0000244|PDB:1ADE}.
STRAND 104 106 {ECO:0000244|PDB:1GIM}.
HELIX 109 120 {ECO:0000244|PDB:1ADE}.
HELIX 123 125 {ECO:0000244|PDB:1ADE}.
STRAND 126 128 {ECO:0000244|PDB:1HOP}.
STRAND 131 133 {ECO:0000244|PDB:1QF5}.
HELIX 134 142 {ECO:0000244|PDB:1ADE}.
HELIX 149 153 {ECO:0000244|PDB:1ADE}.
HELIX 155 175 {ECO:0000244|PDB:1ADE}.
HELIX 184 199 {ECO:0000244|PDB:1ADE}.
HELIX 205 215 {ECO:0000244|PDB:1ADE}.
STRAND 219 222 {ECO:0000244|PDB:1ADE}.
HELIX 227 229 {ECO:0000244|PDB:1ADE}.
TURN 231 233 {ECO:0000244|PDB:1ADE}.
STRAND 234 238 {ECO:0000244|PDB:1ADI}.
HELIX 246 248 {ECO:0000244|PDB:1ADE}.
HELIX 249 253 {ECO:0000244|PDB:1ADE}.
HELIX 257 259 {ECO:0000244|PDB:1ADE}.
STRAND 262 273 {ECO:0000244|PDB:1ADE}.
STRAND 275 277 {ECO:0000244|PDB:1ADE}.
HELIX 286 295 {ECO:0000244|PDB:1ADE}.
TURN 300 302 {ECO:0000244|PDB:1ADE}.
STRAND 307 309 {ECO:0000244|PDB:1ADE}.
HELIX 313 323 {ECO:0000244|PDB:1ADE}.
STRAND 327 331 {ECO:0000244|PDB:1ADE}.
HELIX 333 336 {ECO:0000244|PDB:1ADE}.
STRAND 340 349 {ECO:0000244|PDB:1ADE}.
STRAND 355 358 {ECO:0000244|PDB:1ADE}.
HELIX 363 365 {ECO:0000244|PDB:1QF5}.
HELIX 366 368 {ECO:0000244|PDB:1ADE}.
STRAND 370 377 {ECO:0000244|PDB:1ADE}.
HELIX 389 391 {ECO:0000244|PDB:1ADE}.
HELIX 394 407 {ECO:0000244|PDB:1ADE}.
STRAND 411 415 {ECO:0000244|PDB:1ADE}.
STRAND 417 419 {ECO:0000244|PDB:1ADE}.
STRAND 422 427 {ECO:0000244|PDB:1ADE}.
TURN 429 431 {ECO:0000244|PDB:1ADE}.
SEQUENCE 432 AA; 47345 MW; AAA862CA0F80DA70 CRC64;
MGNNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
LRENVTSIIG NGVVLSPAAL MKEMKELEDR GIPVRERLLL SEACPLILDY HVALDNAREK
ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKETFAE KLKEVMEYHN FQLVNYYKAE
AVDYQKVLDD TMAVADILTS MVVDVSDLLD QARQRGDFVM FEGAQGTLLD IDHGTYPYVT
SSNTTAGGVA TGSGLGPRYV DYVLGILKAY STRVGAGPFP TELFDETGEF LCKQGNEFGA
TTGRRRRTGW LDTVAVRRAV QLNSLSGFCL TKLDVLDGLK EVKLCVAYRM PDGREVTTTP
LAADDWKGVE PIYETMPGWS ESTFGVKDRS GLPQAALNYI KRIEELTGVP IDIISTGPDR
TETMILRDPF DA


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