ID   NFSB_ECOLI              Reviewed;         217 AA.
AC   P38489; P19575;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Oxygen-insensitive NAD(P)H nitroreductase;
DE            EC=1.-.-.-;
DE   AltName: Full=Dihydropteridine reductase;
DE            EC=1.5.1.34;
DE   AltName: Full=FMN-dependent nitroreductase;
GN   Name=nfsB {ECO:0000303|PubMed:8947835};
GN   Synonyms=dprA, nfnB {ECO:0000303|PubMed:7813889}, nfsI, ntr;
GN   OrderedLocusNames=b0578, JW0567;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB
RC   10222;
RX   PubMed=8947835; DOI=10.1093/oxfordjournals.jbchem.a021473;
RA   Zenno S., Koike H., Tanokura M., Saigo K.;
RT   "Gene cloning, purification, and characterization of NfsB, a minor oxygen-
RT   insensitive nitroreductase from Escherichia coli, similar in biochemical
RT   properties to FRase I, the major flavin reductase in Vibrio fischeri.";
RL   J. Biochem. 120:736-744(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B;
RX   PubMed=7813889; DOI=10.1111/j.1574-6968.1994.tb07284.x;
RA   Michael N.P., Brehm J.K., Anlezark G.M., Minton N.P.;
RT   "Physical characterisation of the Escherichia coli B gene encoding
RT   nitroreductase and its over-expression in Escherichia coli K12.";
RL   FEMS Microbiol. Lett. 124:195-202(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-31 AND 139-180, AND CHARACTERIZATION.
RC   STRAIN=B;
RX   PubMed=1472094; DOI=10.1016/0006-2952(92)90671-5;
RA   Anlezark G.M., Melton R.G., Sherwood R.F., Coles B., Friedlos F.,
RA   Knox R.J.;
RT   "The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954) -- I.
RT   Purification and properties of a nitroreductase enzyme from Escherichia
RT   coli -- a potential enzyme for antibody-directed enzyme prodrug therapy
RT   (ADEPT).";
RL   Biochem. Pharmacol. 44:2289-2295(1992).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [9]
RP   PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION AS A DIHYDROPTERIDINE
RP   REDUCT.
RX   PubMed=3060113;
RA   Vasudevan S.G., Shaw D.C., Armarego W.L.F.;
RT   "Dihydropteridine reductase from Escherichia coli.";
RL   Biochem. J. 255:581-588(1988).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RC   STRAIN=B;
RX   PubMed=11020276; DOI=10.1021/jm000159m;
RA   Parkinson G.N., Skelly J.V., Neidle S.;
RT   "Crystal structure of FMN-dependent nitroreductase from Escherichia coli B:
RT   a prodrug-activating enzyme.";
RL   J. Med. Chem. 43:3624-3631(2000).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NICOTININC ACID AND
RP   FMN, AND SUBUNIT.
RC   STRAIN=K12 / DH5-alpha;
RX   PubMed=11491290; DOI=10.1006/jmbi.2001.4653;
RA   Lovering A.L., Hyde E.I., Searle P.F., White S.A.;
RT   "The structure of Escherichia coli nitroreductase complexed with nicotinic
RT   acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution.";
RL   J. Mol. Biol. 309:203-213(2001).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH FMN; DICOUMAROL AND
RP   DINITROBENZAMIDE PRODRUGS, AND SUBUNIT.
RX   PubMed=12954054; DOI=10.1021/jm030843b;
RA   Johansson E., Parkinson G.N., Denny W.A., Neidle S.;
RT   "Studies on the nitroreductase prodrug-activating system. Crystal
RT   structures of complexes with the inhibitor dicoumarol and dinitrobenzamide
RT   prodrugs and of the enzyme active form.";
RL   J. Med. Chem. 46:4009-4020(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FMN; ACETATE AND THE
RP   ANTIBIOTIC NITROFURAZONE, FUNCTION, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15684426; DOI=10.1074/jbc.m409652200;
RA   Race P.R., Lovering A.L., Green R.M., Ossor A., White S.A., Searle P.F.,
RA   Wrighton C.J., Hyde E.I.;
RT   "Structural and mechanistic studies of Escherichia coli nitroreductase with
RT   the antibiotic nitrofurazone. Reversed binding orientations in different
RT   redox states of the enzyme.";
RL   J. Biol. Chem. 280:13256-13264(2005).
CC   -!- FUNCTION: Reduction of a variety of nitroaromatic compounds using NADH
CC       (and to lesser extent NADPH) as source of reducing equivalents; two
CC       electrons are transferred. Capable of reducing nitrofurazone, quinones
CC       and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-
CC       dinitrobenzamide). The reduction of CB1954 results in the generation of
CC       cytotoxic species. {ECO:0000269|PubMed:15684426}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine +
CC         H(+) + NADH; Xref=Rhea:RHEA:17869, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.5.1.34;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydropteridine + NADP(+) = 6,7-dihydropteridine +
CC         H(+) + NADPH; Xref=Rhea:RHEA:17865, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.34;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- ACTIVITY REGULATION: Subject to competitive inhibition by dicoumarol,
CC       nicotinic acid and acetate with respect to NADH. Subject to
CC       uncompetitive inhibition by dicoumarol, nicotinic acid and acetate with
CC       respect to nitrofurazone and nitrofurantoin.
CC       {ECO:0000269|PubMed:15684426}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=350 uM for NADH {ECO:0000269|PubMed:15684426};
CC         KM=1850 uM for nitrofurazone {ECO:0000269|PubMed:15684426};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11020276,
CC       ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:12954054,
CC       ECO:0000269|PubMed:15684426}.
CC   -!- INTERACTION:
CC       P38489; P38489: nfsB; NbExp=2; IntAct=EBI-909296, EBI-909296;
CC   -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR   EMBL; D25414; BAA05004.1; -; Genomic_DNA.
DR   EMBL; U07860; AAC43263.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40776.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73679.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35218.1; -; Genomic_DNA.
DR   PIR; I67685; I67685.
DR   PIR; S01818; S01818.
DR   RefSeq; NP_415110.1; NC_000913.3.
DR   RefSeq; WP_000351487.1; NZ_SSZK01000024.1.
DR   PDB; 1DS7; X-ray; 2.06 A; A/B=1-217.
DR   PDB; 1ICR; X-ray; 1.70 A; A/B=1-217.
DR   PDB; 1ICU; X-ray; 1.80 A; A/B/C/D=1-217.
DR   PDB; 1ICV; X-ray; 2.40 A; A/B/C/D=1-217.
DR   PDB; 1IDT; X-ray; 2.00 A; A/B=1-217.
DR   PDB; 1OO5; X-ray; 2.50 A; A/B=1-217.
DR   PDB; 1OO6; X-ray; 2.00 A; A/B=1-217.
DR   PDB; 1OON; X-ray; 2.49 A; A/B=1-217.
DR   PDB; 1OOQ; X-ray; 2.00 A; A/B=1-217.
DR   PDB; 1YKI; X-ray; 1.70 A; A/B/C/D=1-217.
DR   PDB; 1YLR; X-ray; 1.70 A; A/B=1-217.
DR   PDB; 1YLU; X-ray; 2.00 A; A/B=1-217.
DR   PDB; 3X21; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=1-217.
DR   PDB; 3X22; X-ray; 2.00 A; A/B=1-217.
DR   PDB; 7X32; X-ray; 1.83 A; A/B/C/D/E/F/G/H=1-217.
DR   PDB; 8C5E; X-ray; 1.65 A; A/B=2-217.
DR   PDB; 8C5F; X-ray; 1.60 A; A/B=2-217.
DR   PDB; 8C5P; X-ray; 1.69 A; A/B=1-217.
DR   PDB; 8CCV; X-ray; 2.20 A; A/B=1-217.
DR   PDB; 8CJ0; X-ray; 1.99 A; A/B=1-217.
DR   PDB; 8OG3; X-ray; 2.09 A; A/B=2-217.
DR   PDBsum; 1DS7; -.
DR   PDBsum; 1ICR; -.
DR   PDBsum; 1ICU; -.
DR   PDBsum; 1ICV; -.
DR   PDBsum; 1IDT; -.
DR   PDBsum; 1OO5; -.
DR   PDBsum; 1OO6; -.
DR   PDBsum; 1OON; -.
DR   PDBsum; 1OOQ; -.
DR   PDBsum; 1YKI; -.
DR   PDBsum; 1YLR; -.
DR   PDBsum; 1YLU; -.
DR   PDBsum; 3X21; -.
DR   PDBsum; 3X22; -.
DR   PDBsum; 7X32; -.
DR   PDBsum; 8C5E; -.
DR   PDBsum; 8C5F; -.
DR   PDBsum; 8C5P; -.
DR   PDBsum; 8CCV; -.
DR   PDBsum; 8CJ0; -.
DR   PDBsum; 8OG3; -.
DR   AlphaFoldDB; P38489; -.
DR   SMR; P38489; -.
DR   BioGRID; 4262913; 20.
DR   BioGRID; 850145; 1.
DR   DIP; DIP-10330N; -.
DR   IntAct; P38489; 12.
DR   STRING; 511145.b0578; -.
DR   BindingDB; P38489; -.
DR   ChEMBL; CHEMBL1075080; -.
DR   DrugBank; DB04138; 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide.
DR   DrugBank; DB03228; 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide.
DR   DrugBank; DB04392; Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone].
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   DrugBank; DB04253; Tretazicar.
DR   jPOST; P38489; -.
DR   PaxDb; 511145-b0578; -.
DR   EnsemblBacteria; AAC73679; AAC73679; b0578.
DR   GeneID; 945778; -.
DR   KEGG; ecj:JW0567; -.
DR   KEGG; eco:b0578; -.
DR   PATRIC; fig|1411691.4.peg.1696; -.
DR   EchoBASE; EB4146; -.
DR   eggNOG; COG0778; Bacteria.
DR   HOGENOM; CLU_070764_4_1_6; -.
DR   InParanoid; P38489; -.
DR   OMA; DQWMAKQ; -.
DR   OrthoDB; 9809288at2; -.
DR   PhylomeDB; P38489; -.
DR   BioCyc; EcoCyc:DIHYDROPTERIREDUCT-MONOMER; -.
DR   BioCyc; MetaCyc:DIHYDROPTERIREDUCT-MONOMER; -.
DR   BRENDA; 1.7.1.B2; 2026.
DR   SABIO-RK; P38489; -.
DR   EvolutionaryTrace; P38489; -.
DR   PRO; PR:P38489; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004155; F:6,7-dihydropteridine reductase activity; IDA:EcoCyc.
DR   GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:EcoCyc.
DR   GO; GO:0018545; F:NAD(P)H nitroreductase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0046256; P:2,4,6-trinitrotoluene catabolic process; IMP:EcoCyc.
DR   CDD; cd02149; NfsB-like; 1.
DR   Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR   InterPro; IPR033878; NfsB-like.
DR   InterPro; IPR029479; Nitroreductase.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   PANTHER; PTHR23026; NADPH NITROREDUCTASE; 1.
DR   PANTHER; PTHR23026:SF125; OXYGEN-INSENSITIVE NAD(P)H NITROREDUCTASE; 1.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
DR   SWISS-2DPAGE; P38489; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Flavoprotein; FMN; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Oxygen-insensitive NAD(P)H nitroreductase"
FT                   /id="PRO_0000072711"
FT   BINDING         10..14
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11020276,
FT                   ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426"
FT   BINDING         14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q01234"
FT   BINDING         41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q01234"
FT   BINDING         71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11020276,
FT                   ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426"
FT   BINDING         71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q01234"
FT   BINDING         74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q01234"
FT   BINDING         107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q01234"
FT   BINDING         165..166
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11020276,
FT                   ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426"
FT   BINDING         205..207
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11020276,
FT                   ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426"
FT   CONFLICT        5
FT                   /note="S -> C (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10..12
FT                   /note="RHS -> CIV (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="S -> M (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="Missing (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="E -> D (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="E -> I (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:1OO6"
FT   HELIX           24..36
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           54..61
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:8C5E"
FT   HELIX           66..71
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           72..77
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   STRAND          78..89
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           92..104
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           111..130
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           135..156
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           169..175
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   STRAND          183..192
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:8C5F"
FT   STRAND          214..217
FT                   /evidence="ECO:0007829|PDB:8C5F"
SQ   SEQUENCE   217 AA;  23905 MW;  A516CEFC3D46AEAC CRC64;
     MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV
     AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG
     RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE
     KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV
//