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Beta-lactamase (EC 3.5.2.6) (Cephalosporinase)

 AMPC_ECOLI              Reviewed;         377 AA.
P00811; Q2M6F2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 163.
RecName: Full=Beta-lactamase;
EC=3.5.2.6;
AltName: Full=Cephalosporinase;
Flags: Precursor;
Name=ampC; Synonyms=ampA; OrderedLocusNames=b4150, JW4111;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-31.
STRAIN=K12;
PubMed=6795623; DOI=10.1073/pnas.78.8.4897;
Jaurin B., Grundstroem T.;
"ampC cephalosporinase of Escherichia coli K-12 has a different
evolutionary origin from that of beta-lactamases of the penicillinase
type.";
Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
PubMed=7041115; DOI=10.1073/pnas.79.4.1111;
Grundstroem T., Jaurin B.;
"Overlap between ampC and frd operons on the Escherichia coli
chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982).
[6]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9819201; DOI=10.1021/bi981210f;
Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K.,
Remington S.J.;
"Three-dimensional structure of AmpC beta-lactamase from Escherichia
coli bound to a transition-state analogue: possible implications for
the oxyanion hypothesis and for inhibitor design.";
Biochemistry 37:16082-16092(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=10595535; DOI=10.1110/ps.8.11.2330;
Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F.,
Shoichet B.K.;
"The complexed structure and antimicrobial activity of a non-beta-
lactam inhibitor of AmpC beta-lactamase.";
Protein Sci. 8:2330-2337(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGUE.
PubMed=11478888; DOI=10.1021/bi0109358;
Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.;
"Structures of ceftazidime and its transition-state analogue in
complex with AmpC beta-lactamase: implications for resistance
mutations and inhibitor design.";
Biochemistry 40:9207-9214(2001).
[10]
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), AND MUTAGENESIS OF SER-80;
LYS-83; TYR-166; ASN-168 AND LYS-331.
PubMed=12144785; DOI=10.1016/S0022-2836(02)00599-5;
Beadle B.M., Shoichet B.K.;
"Structural bases of stability-function tradeoffs in enzymes.";
J. Mol. Biol. 321:285-296(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
PubMed=12526668; DOI=10.1021/ja0288338;
Morandi F., Caselli E., Morandi S., Focia P.J., Blazquez J.,
Shoichet B.K., Prati F.;
"Nanomolar inhibitors of AmpC beta-lactamase.";
J. Am. Chem. Soc. 125:685-695(2003).
-!- FUNCTION: This protein is a serine beta-lactamase with a substrate
specificity for cephalosporins.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000255|PROSITE-ProRule:PRU10102}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11478888}.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the class-C beta-lactamase family.
{ECO:0000305}.
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EMBL; J01611; AAA23441.1; -; Genomic_DNA.
EMBL; U14003; AAA97049.1; -; Genomic_DNA.
EMBL; U00096; AAC77110.1; -; Genomic_DNA.
EMBL; AP009048; BAE78154.1; -; Genomic_DNA.
EMBL; V00277; CAA23537.1; -; Genomic_DNA.
PIR; A01007; QKEC.
RefSeq; NP_418574.1; NC_000913.3.
RefSeq; WP_001336292.1; NZ_LN832404.1.
PDB; 1C3B; X-ray; 2.25 A; A/B=20-377.
PDB; 1FCM; X-ray; 2.46 A; A/B=20-377.
PDB; 1FCN; X-ray; 2.35 A; A/B=20-377.
PDB; 1FCO; X-ray; 2.20 A; A/B=20-377.
PDB; 1FSW; X-ray; 1.90 A; A/B=20-376.
PDB; 1FSY; X-ray; 1.75 A; A/B=20-376.
PDB; 1GA9; X-ray; 2.10 A; A/B=20-377.
PDB; 1I5Q; X-ray; 1.83 A; A/B=20-377.
PDB; 1IEL; X-ray; 2.00 A; A/B=20-377.
PDB; 1IEM; X-ray; 2.30 A; A/B=20-377.
PDB; 1KDS; X-ray; 2.15 A; A/B=20-377.
PDB; 1KDW; X-ray; 2.28 A; A/B=20-377.
PDB; 1KE0; X-ray; 2.30 A; A/B=20-377.
PDB; 1KE3; X-ray; 2.15 A; A/B=20-377.
PDB; 1KE4; X-ray; 1.72 A; A/B=20-377.
PDB; 1KVL; X-ray; 1.53 A; A/B=20-377.
PDB; 1KVM; X-ray; 2.06 A; A/B=20-377.
PDB; 1L0D; X-ray; 1.53 A; A/B=20-377.
PDB; 1L0E; X-ray; 1.90 A; A/B=20-377.
PDB; 1L0F; X-ray; 1.66 A; A/B=20-377.
PDB; 1L0G; X-ray; 1.50 A; A/B=20-377.
PDB; 1L2S; X-ray; 1.94 A; A/B=20-377.
PDB; 1LL5; X-ray; 1.80 A; A/B=20-377.
PDB; 1LL9; X-ray; 1.87 A; A/B=20-377.
PDB; 1LLB; X-ray; 1.72 A; A/B=20-377.
PDB; 1MXO; X-ray; 1.83 A; A/B=20-377.
PDB; 1MY8; X-ray; 1.72 A; A/B=20-377.
PDB; 1O07; X-ray; 1.71 A; A/B=20-377.
PDB; 1PI4; X-ray; 1.39 A; A/B=20-377.
PDB; 1PI5; X-ray; 1.49 A; A/B=20-377.
PDB; 1XGI; X-ray; 1.96 A; A/B=20-377.
PDB; 1XGJ; X-ray; 1.97 A; A/B=20-377.
PDB; 2BLS; X-ray; 2.00 A; A/B=20-377.
PDB; 2FFY; X-ray; 1.07 A; A/B=20-377.
PDB; 2HDQ; X-ray; 2.10 A; A/B=20-377.
PDB; 2HDR; X-ray; 2.20 A; A/B=20-377.
PDB; 2HDS; X-ray; 1.16 A; A/B=20-377.
PDB; 2HDU; X-ray; 1.49 A; A/B=20-377.
PDB; 2I72; X-ray; 2.20 A; A/B=20-377.
PDB; 2P9V; X-ray; 1.80 A; A/B=20-377.
PDB; 2PU2; X-ray; 1.86 A; A/B=20-377.
PDB; 2PU4; X-ray; 2.00 A; A/B=20-377.
PDB; 2R9W; X-ray; 1.80 A; A/B=20-377.
PDB; 2R9X; X-ray; 1.90 A; A/B=20-377.
PDB; 2RCX; X-ray; 2.00 A; A/B=20-377.
PDB; 3BLS; X-ray; 2.30 A; A/B=20-377.
PDB; 3BM6; X-ray; 2.10 A; A/B=20-377.
PDB; 3FKV; X-ray; 1.85 A; A/B=20-377.
PDB; 3FKW; X-ray; 1.50 A; A/B=20-377.
PDB; 3GQZ; X-ray; 1.80 A; A/B=20-377.
PDB; 3GR2; X-ray; 1.80 A; A/B=20-377.
PDB; 3GRJ; X-ray; 2.49 A; A/B=20-377.
PDB; 3GSG; X-ray; 2.10 A; A/B=20-377.
PDB; 3GTC; X-ray; 1.90 A; A/B=20-377.
PDB; 3GV9; X-ray; 1.80 A; A/B=20-377.
PDB; 3GVB; X-ray; 1.80 A; A/B=20-377.
PDB; 3IWI; X-ray; 1.64 A; A/B=20-377.
PDB; 3IWO; X-ray; 1.90 A; A/B=20-377.
PDB; 3IWQ; X-ray; 1.84 A; A/B=20-377.
PDB; 3IXB; X-ray; 1.63 A; A/B=20-377.
PDB; 3IXD; X-ray; 2.64 A; A/B=20-377.
PDB; 3IXG; X-ray; 2.14 A; A/B=20-377.
PDB; 3IXH; X-ray; 2.30 A; A/B=20-377.
PDB; 3O86; X-ray; 1.60 A; A/B=20-377.
PDB; 3O87; X-ray; 1.78 A; A/B=20-377.
PDB; 3O88; X-ray; 1.64 A; A/B=20-377.
PDB; 4E3I; X-ray; 1.60 A; A/B=20-377.
PDB; 4E3J; X-ray; 1.80 A; A/B=20-377.
PDB; 4E3K; X-ray; 1.43 A; A/B=20-377.
PDB; 4E3L; X-ray; 1.43 A; A/B=20-377.
PDB; 4E3M; X-ray; 1.44 A; A/B=20-377.
PDB; 4E3N; X-ray; 1.49 A; A/B=20-377.
PDB; 4E3O; X-ray; 1.60 A; A/B=20-377.
PDB; 4JXG; X-ray; 1.65 A; A/B=20-377.
PDB; 4JXS; X-ray; 1.90 A; A/B=20-377.
PDB; 4JXV; X-ray; 1.76 A; A/B=20-377.
PDB; 4JXW; X-ray; 2.30 A; A/B=20-377.
PDB; 4KEN; X-ray; 1.89 A; B=20-377.
PDB; 4KG2; X-ray; 1.89 A; A/B=20-377.
PDB; 4KG5; X-ray; 2.11 A; A/B/C/D=20-377.
PDB; 4KG6; X-ray; 1.75 A; A/B/C/D=20-377.
PDB; 4KZ3; X-ray; 1.67 A; A/B=20-377.
PDB; 4KZ4; X-ray; 1.42 A; A/B=20-377.
PDB; 4KZ5; X-ray; 1.35 A; A/B=20-377.
PDB; 4KZ6; X-ray; 1.68 A; A/B=20-377.
PDB; 4KZ7; X-ray; 1.43 A; A/B=20-377.
PDB; 4KZ8; X-ray; 2.28 A; A/B=20-377.
PDB; 4KZ9; X-ray; 1.72 A; A/B=20-377.
PDB; 4KZA; X-ray; 1.60 A; A/B=20-377.
PDB; 4KZB; X-ray; 1.37 A; A/B=20-377.
PDB; 4LV0; X-ray; 1.65 A; A/B=20-377.
PDB; 4LV1; X-ray; 1.74 A; A/B=20-377.
PDB; 4LV2; X-ray; 1.65 A; A/B=20-377.
PDB; 4LV3; X-ray; 1.42 A; A/B=20-377.
PDB; 4OKP; X-ray; 1.37 A; A/B=20-377.
PDB; 4OLD; X-ray; 1.48 A; A/B=20-377.
PDB; 4OLG; X-ray; 1.71 A; A/B=20-377.
PDBsum; 1C3B; -.
PDBsum; 1FCM; -.
PDBsum; 1FCN; -.
PDBsum; 1FCO; -.
PDBsum; 1FSW; -.
PDBsum; 1FSY; -.
PDBsum; 1GA9; -.
PDBsum; 1I5Q; -.
PDBsum; 1IEL; -.
PDBsum; 1IEM; -.
PDBsum; 1KDS; -.
PDBsum; 1KDW; -.
PDBsum; 1KE0; -.
PDBsum; 1KE3; -.
PDBsum; 1KE4; -.
PDBsum; 1KVL; -.
PDBsum; 1KVM; -.
PDBsum; 1L0D; -.
PDBsum; 1L0E; -.
PDBsum; 1L0F; -.
PDBsum; 1L0G; -.
PDBsum; 1L2S; -.
PDBsum; 1LL5; -.
PDBsum; 1LL9; -.
PDBsum; 1LLB; -.
PDBsum; 1MXO; -.
PDBsum; 1MY8; -.
PDBsum; 1O07; -.
PDBsum; 1PI4; -.
PDBsum; 1PI5; -.
PDBsum; 1XGI; -.
PDBsum; 1XGJ; -.
PDBsum; 2BLS; -.
PDBsum; 2FFY; -.
PDBsum; 2HDQ; -.
PDBsum; 2HDR; -.
PDBsum; 2HDS; -.
PDBsum; 2HDU; -.
PDBsum; 2I72; -.
PDBsum; 2P9V; -.
PDBsum; 2PU2; -.
PDBsum; 2PU4; -.
PDBsum; 2R9W; -.
PDBsum; 2R9X; -.
PDBsum; 2RCX; -.
PDBsum; 3BLS; -.
PDBsum; 3BM6; -.
PDBsum; 3FKV; -.
PDBsum; 3FKW; -.
PDBsum; 3GQZ; -.
PDBsum; 3GR2; -.
PDBsum; 3GRJ; -.
PDBsum; 3GSG; -.
PDBsum; 3GTC; -.
PDBsum; 3GV9; -.
PDBsum; 3GVB; -.
PDBsum; 3IWI; -.
PDBsum; 3IWO; -.
PDBsum; 3IWQ; -.
PDBsum; 3IXB; -.
PDBsum; 3IXD; -.
PDBsum; 3IXG; -.
PDBsum; 3IXH; -.
PDBsum; 3O86; -.
PDBsum; 3O87; -.
PDBsum; 3O88; -.
PDBsum; 4E3I; -.
PDBsum; 4E3J; -.
PDBsum; 4E3K; -.
PDBsum; 4E3L; -.
PDBsum; 4E3M; -.
PDBsum; 4E3N; -.
PDBsum; 4E3O; -.
PDBsum; 4JXG; -.
PDBsum; 4JXS; -.
PDBsum; 4JXV; -.
PDBsum; 4JXW; -.
PDBsum; 4KEN; -.
PDBsum; 4KG2; -.
PDBsum; 4KG5; -.
PDBsum; 4KG6; -.
PDBsum; 4KZ3; -.
PDBsum; 4KZ4; -.
PDBsum; 4KZ5; -.
PDBsum; 4KZ6; -.
PDBsum; 4KZ7; -.
PDBsum; 4KZ8; -.
PDBsum; 4KZ9; -.
PDBsum; 4KZA; -.
PDBsum; 4KZB; -.
PDBsum; 4LV0; -.
PDBsum; 4LV1; -.
PDBsum; 4LV2; -.
PDBsum; 4LV3; -.
PDBsum; 4OKP; -.
PDBsum; 4OLD; -.
PDBsum; 4OLG; -.
ProteinModelPortal; P00811; -.
SMR; P00811; -.
BioGrid; 4261277; 161.
IntAct; P00811; 1.
STRING; 316385.ECDH10B_4345; -.
BindingDB; P00811; -.
ChEMBL; CHEMBL2026; -.
DrugBank; DB08551; (1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACID.
DrugBank; DB08552; (1R)-1-(2-thienylacetylamino)-1-phenylmethylboronic acid.
DrugBank; DB07057; (3S)-1-(2-hydroxyphenyl)-5-oxopyrrolidine-3-carboxylic acid.
DrugBank; DB07825; (3S)-1-(4-acetylphenyl)-5-oxopyrrolidine-3-carboxylic acid.
DrugBank; DB07803; 2-phenyl-1H-imidazole-4-carboxylic acid.
DrugBank; DB02858; 3-(4-Benzenesulfonyl-Thiophene-2-Sulfonylamino)-Phenylboronic Acid.
DrugBank; DB08573; 3-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACID.
DrugBank; DB02797; 3-Nitrophenylboronic Acid.
DrugBank; DB08306; 3-{[(3-NITROANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID.
DrugBank; DB07927; 3-{[(4-CARBOXY-2-HYDROXYANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID.
DrugBank; DB02503; 4-(Carboxyvin-2-Yl)Phenylboronic Acid.
DrugBank; DB07541; 4-(dihydroxyboranyl)-2-({[4-(phenylsulfonyl)thiophen-2-yl]sulfonyl}amino)benzoic acid.
DrugBank; DB07114; 4-[(METHYLSULFONYL)AMINO]BENZOIC ACID.
DrugBank; DB03140; 4-Carboxyphenylboronic Acid.
DrugBank; DB04293; 7-(2-Amino-2-Phenyl-Acetylamino)-3-Chloro-8-Oxo-1-Aza-Bicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid.
DrugBank; DB03530; Acylated Ceftazidime.
DrugBank; DB09323; Benzathine benzylpenicillin.
DrugBank; DB04360; Benzo[B]Thiophene-2-Boronic Acid.
DrugBank; DB00456; Cefalotin.
DrugBank; DB01147; Cloxacillin.
DrugBank; DB02247; Hydrolyzed Cephalothin.
DrugBank; DB01896; M-Aminophenylboronic Acid.
DrugBank; DB02588; Moxalactam Derivative.
DrugBank; DB02094; N-2-Thiophen-2-Yl-Acetamide Boronic Acid.
DrugBank; DB08375; PCNOTAXIME GROUP.
DrugBank; DB04035; Pinacol[[2-Amino-Alpha-(1-Carboxy-1-Methylethoxyimino)-4-Thiazoleacetyl]Amino]Methaneboronate.
DrugBank; DB02772; Sucrose.
MEROPS; S12.006; -.
SWISS-2DPAGE; P00811; -.
PaxDb; P00811; -.
PRIDE; P00811; -.
EnsemblBacteria; AAC77110; AAC77110; b4150.
EnsemblBacteria; BAE78154; BAE78154; BAE78154.
GeneID; 948669; -.
KEGG; ecj:JW4111; -.
KEGG; eco:b4150; -.
PATRIC; fig|1411691.4.peg.2548; -.
EchoBASE; EB0038; -.
EcoGene; EG10040; ampC.
eggNOG; ENOG41066YJ; Bacteria.
eggNOG; COG1680; LUCA.
HOGENOM; HOG000267102; -.
InParanoid; P00811; -.
KO; K01467; -.
PhylomeDB; P00811; -.
BioCyc; EcoCyc:EG10040-MONOMER; -.
BioCyc; MetaCyc:EG10040-MONOMER; -.
BRENDA; 3.5.2.6; 2026.
SABIO-RK; P00811; -.
EvolutionaryTrace; P00811; -.
PRO; PR:P00811; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
GO; GO:0008800; F:beta-lactamase activity; IDA:EcoliWiki.
GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR001466; Beta-lactam-related.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001586; Beta-lactam_class-C_AS.
Pfam; PF00144; Beta-lactamase; 1.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00336; BETA_LACTAMASE_C; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Hydrolase; Periplasm; Reference proteome;
Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:6795623}.
CHAIN 20 377 Beta-lactamase.
/FTId=PRO_0000016958.
REGION 331 333 Substrate binding. {ECO:0000250}.
ACT_SITE 80 80 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10102,
ECO:0000269|PubMed:6795623}.
ACT_SITE 166 166 Proton acceptor.
MUTAGEN 80 80 S->D,E,G: Loss of activity.
{ECO:0000269|PubMed:12144785}.
MUTAGEN 83 83 K->Q,T: Lowers activity more than 1000-
fold and increases protein stability.
{ECO:0000269|PubMed:12144785}.
MUTAGEN 166 166 Y->E: Lowers activity more than 1000-
fold. {ECO:0000269|PubMed:12144785}.
MUTAGEN 168 168 N->D,H: Lowers activity more than 1000-
fold. {ECO:0000269|PubMed:12144785}.
MUTAGEN 331 331 K->A: Lowers activity more than 1000-
fold. {ECO:0000269|PubMed:12144785}.
HELIX 22 39 {ECO:0000244|PDB:2FFY}.
STRAND 42 50 {ECO:0000244|PDB:2FFY}.
STRAND 53 63 {ECO:0000244|PDB:2FFY}.
TURN 64 67 {ECO:0000244|PDB:2FFY}.
STRAND 75 77 {ECO:0000244|PDB:2FFY}.
HELIX 79 81 {ECO:0000244|PDB:2FFY}.
HELIX 82 95 {ECO:0000244|PDB:2FFY}.
HELIX 105 108 {ECO:0000244|PDB:2FFY}.
HELIX 115 117 {ECO:0000244|PDB:2FFY}.
HELIX 122 126 {ECO:0000244|PDB:2FFY}.
HELIX 144 153 {ECO:0000244|PDB:2FFY}.
STRAND 162 164 {ECO:0000244|PDB:2FFY}.
HELIX 168 178 {ECO:0000244|PDB:2FFY}.
TURN 179 183 {ECO:0000244|PDB:2FFY}.
HELIX 186 193 {ECO:0000244|PDB:2FFY}.
TURN 194 199 {ECO:0000244|PDB:2FFY}.
STRAND 204 206 {ECO:0000244|PDB:2FFY}.
HELIX 209 214 {ECO:0000244|PDB:2FFY}.
STRAND 218 220 {ECO:0000244|PDB:2FFY}.
STRAND 223 225 {ECO:0000244|PDB:2FFY}.
TURN 229 231 {ECO:0000244|PDB:3IWI}.
HELIX 233 236 {ECO:0000244|PDB:2FFY}.
STRAND 240 242 {ECO:0000244|PDB:4OLD}.
HELIX 243 254 {ECO:0000244|PDB:2FFY}.
HELIX 256 258 {ECO:0000244|PDB:2FFY}.
HELIX 262 271 {ECO:0000244|PDB:2FFY}.
STRAND 273 278 {ECO:0000244|PDB:2FFY}.
STRAND 281 283 {ECO:0000244|PDB:2FFY}.
STRAND 288 293 {ECO:0000244|PDB:2FFY}.
HELIX 296 301 {ECO:0000244|PDB:2FFY}.
STRAND 303 305 {ECO:0000244|PDB:3GR2}.
STRAND 306 308 {ECO:0000244|PDB:2FFY}.
STRAND 310 313 {ECO:0000244|PDB:2BLS}.
STRAND 315 321 {ECO:0000244|PDB:2FFY}.
STRAND 325 335 {ECO:0000244|PDB:2FFY}.
STRAND 338 345 {ECO:0000244|PDB:2FFY}.
HELIX 346 348 {ECO:0000244|PDB:2FFY}.
STRAND 350 358 {ECO:0000244|PDB:2FFY}.
HELIX 362 376 {ECO:0000244|PDB:2FFY}.
SEQUENCE 377 AA; 41556 MW; 3C6FB4FE4EF96C9F CRC64;
MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY QGKPYYFTWG
YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK LSDPTTKYWP ELTAKQWNGI
TLLHLATYTA GGLPLQVPDE VKSSSDLLRF YQNWQPAWAP GTQRLYANSS IGLFGALAVK
PSGLSFEQAM QTRVFQPLKL NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK
STIEDMARWV QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL GIVMLANKNY
PNPARVDAAW QILNALQ


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