DFPA_LOLVU
ID DFPA_LOLVU Reviewed; 314 AA.
AC Q7SIG4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Diisopropyl-fluorophosphatase;
DE Short=DFPase;
DE EC=3.1.8.2;
OS Loligo vulgaris (Common European squid).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Loligo.
OX NCBI_TaxID=6622;
RN [1] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-181; HIS-219;
RP HIS-224; HIS-248; HIS-274 AND HIS-287.
RX PubMed=11295437; DOI=10.1016/s0167-4838(01)00153-4;
RA Hartleib J., Rueterjans H.;
RT "Insights into the reaction mechanism of the diisopropyl fluorophosphatase
RT from Loligo vulgaris by means of kinetic studies, chemical modification and
RT site-directed mutagenesis.";
RL Biochim. Biophys. Acta 1546:312-324(2001).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=11171055; DOI=10.1042/0264-6021:3530579;
RA Hartleib J., Geschwindner S., Scharff E.I., Rueterjans H.;
RT "Role of calcium ions in the structure and function of the di-
RT isopropylfluorophosphatase from Loligo vulgaris.";
RL Biochem. J. 353:579-589(2001).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLN-77; ASN-120; ASP-121; TYR-144; ARG-146;
RP MET-148; PHE-173; ASN-175; HIS-181; THR-195; ASP-229; ASP-232; ASN-237;
RP SER-271; ASN-272; HIS-274; HIS-287; GLN-304 AND PHE-314.
RX PubMed=15966726; DOI=10.1021/bi0500675;
RA Katsemi V., Luecke C., Koepke J., Lohr F., Maurer S., Fritzsch G.,
RA Rueterjans H.;
RT "Mutational and structural studies of the diisopropylfluorophosphatase from
RT Loligo vulgaris shed new light on the catalytic mechanism of the enzyme.";
RL Biochemistry 44:9022-9033(2005).
RN [4] {ECO:0000305, ECO:0000312|PDB:1E1A}
RP CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND BIOTECHNOLOGY.
RX PubMed=11134940; DOI=10.1107/s0907444900014232;
RA Scharff E.I., Lucke C., Fritzsch G., Koepke J., Hartleib J., Dierl S.,
RA Rueterjans H.;
RT "Crystallization and preliminary X-ray crystallographic analysis of DFPase
RT from Loligo vulgaris.";
RL Acta Crystallogr. D 57:148-149(2001).
RN [5] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), COFACTOR, SUBUNIT, AND MUTAGENESIS
RP OF GLU-21; GLU-37; ASP-229; TRP-244 AND SER-271.
RX PubMed=11435114; DOI=10.1016/s0969-2126(01)00610-4;
RA Scharff E.I., Koepke J., Fritzsch G., Lucke C., Rueterjans H.;
RT "Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris.";
RL Structure 9:493-502(2001).
RN [6] {ECO:0000305, ECO:0000312|PDB:1PJX}
RP X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX PubMed=14501113; DOI=10.1107/s0907444903016135;
RA Koepke J., Scharff E.I., Lucke C., Rueterjans H., Fritzsch G.;
RT "Statistical analysis of crystallographic data obtained from squid ganglion
RT DFPase at 0.85 A resolution.";
RL Acta Crystallogr. D 59:1744-1754(2003).
CC -!- FUNCTION: Biological function and substrate unknown. However, it is
CC capable of acting on phosphorus anhydride bonds (such as phosphorus-
CC halide and phosphorus-cyanide) in organophosphorus compounds (including
CC nerve gases). {ECO:0000269|PubMed:15966726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diisopropyl fluorophosphate + H2O = diisopropyl phosphate +
CC fluoride + 2 H(+); Xref=Rhea:RHEA:24100, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17051, ChEBI:CHEBI:17941,
CC ChEBI:CHEBI:57896; EC=3.1.8.2; Evidence={ECO:0000269|PubMed:11171055,
CC ECO:0000269|PubMed:11295437};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11171055, ECO:0000269|PubMed:11435114,
CC ECO:0000269|PubMed:14501113};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:11171055,
CC ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113};
CC -!- ACTIVITY REGULATION: Inhibited by chelating agents.
CC {ECO:0000269|PubMed:11171055}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for diisopropyl-fluorophosphate (in the presence of 10 mM
CC NaCl) {ECO:0000269|PubMed:11295437};
CC KM=0.42 mM for diisopropyl-fluorophosphate (in the presence of 100 mM
CC NaCl) {ECO:0000269|PubMed:11295437};
CC KM=0.34 mM for diisopropyl-fluorophosphate (in the presence of 200 mM
CC NaCl) {ECO:0000269|PubMed:11295437};
CC KM=0.25 mM for diisopropyl-fluorophosphate (in the presence of 500 mM
CC NaCl) {ECO:0000269|PubMed:11295437};
CC KM=0.17 mM for diisopropyl-fluorophosphate (in the presence of 1000
CC mM NaCl) {ECO:0000269|PubMed:11295437};
CC Vmax=130 umol/min/mg enzyme (in the presence of 10 mM NaCl)
CC {ECO:0000269|PubMed:11295437};
CC Vmax=170 umol/min/mg enzyme (in the presence of 100 mM NaCl)
CC {ECO:0000269|PubMed:11295437};
CC Vmax=307 umol/min/mg enzyme (in the presence of 200 mM NaCl)
CC {ECO:0000269|PubMed:11295437};
CC Vmax=326 umol/min/mg enzyme (in the presence of 500 mM NaCl)
CC {ECO:0000269|PubMed:11295437};
CC Vmax=214 umol/min/mg enzyme (in the presence of 1000 mM NaCl)
CC {ECO:0000269|PubMed:11295437};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:11295437};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:11295437};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11435114,
CC ECO:0000269|PubMed:14501113}.
CC -!- BIOTECHNOLOGY: Has potential application in bio-remediation by
CC detoxification of organo-phosphates used in insecticides or nerve
CC agents used in chemical warfare such as soman, tabun and sarin.
CC {ECO:0000269|PubMed:11134940}.
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DR PDB; 1E1A; X-ray; 1.80 A; A=1-314.
DR PDB; 1PJX; X-ray; 0.85 A; A=1-314.
DR PDB; 2GVU; X-ray; 2.00 A; A=1-314.
DR PDB; 2GVV; X-ray; 1.73 A; A=1-314.
DR PDB; 2GVW; X-ray; 1.86 A; A=1-314.
DR PDB; 2GVX; X-ray; 2.00 A; A=1-314.
DR PDB; 2IAO; X-ray; 2.00 A; A=3-314.
DR PDB; 2IAP; X-ray; 1.90 A; A=3-314.
DR PDB; 2IAQ; X-ray; 2.10 A; A=3-314.
DR PDB; 2IAR; X-ray; 1.90 A; A=3-314.
DR PDB; 2IAS; X-ray; 2.00 A; A=3-314.
DR PDB; 2IAT; X-ray; 1.90 A; A=3-314.
DR PDB; 2IAU; X-ray; 2.00 A; A=3-314.
DR PDB; 2IAV; X-ray; 1.07 A; A=3-314.
DR PDB; 2IAW; X-ray; 1.74 A; A=3-314.
DR PDB; 2IAX; X-ray; 1.10 A; A=3-314.
DR PDB; 3BYC; X-ray; 2.20 A; A=1-314.
DR PDB; 3HLH; X-ray; 1.80 A; A/B/C/D=1-314.
DR PDB; 3HLI; X-ray; 1.40 A; A/B/C/D=1-314.
DR PDB; 3I1C; X-ray; 2.20 A; A=1-314.
DR PDB; 3KGG; X-ray; 2.10 A; A=1-314.
DR PDB; 3LI3; X-ray; 1.66 A; A=1-314.
DR PDB; 3LI4; X-ray; 1.35 A; A=1-314.
DR PDB; 3LI5; X-ray; 1.36 A; A=1-314.
DR PDB; 3O4P; X-ray; 0.85 A; A=1-314.
DR PDB; 3U0S; X-ray; 2.60 A; A/B=1-314.
DR PDB; 4O5S; X-ray; 1.80 A; A/B=1-314.
DR PDB; 4O5T; X-ray; 2.90 A; A/B=1-314.
DR PDBsum; 1E1A; -.
DR PDBsum; 1PJX; -.
DR PDBsum; 2GVU; -.
DR PDBsum; 2GVV; -.
DR PDBsum; 2GVW; -.
DR PDBsum; 2GVX; -.
DR PDBsum; 2IAO; -.
DR PDBsum; 2IAP; -.
DR PDBsum; 2IAQ; -.
DR PDBsum; 2IAR; -.
DR PDBsum; 2IAS; -.
DR PDBsum; 2IAT; -.
DR PDBsum; 2IAU; -.
DR PDBsum; 2IAV; -.
DR PDBsum; 2IAW; -.
DR PDBsum; 2IAX; -.
DR PDBsum; 3BYC; -.
DR PDBsum; 3HLH; -.
DR PDBsum; 3HLI; -.
DR PDBsum; 3I1C; -.
DR PDBsum; 3KGG; -.
DR PDBsum; 3LI3; -.
DR PDBsum; 3LI4; -.
DR PDBsum; 3LI5; -.
DR PDBsum; 3O4P; -.
DR PDBsum; 3U0S; -.
DR PDBsum; 4O5S; -.
DR PDBsum; 4O5T; -.
DR AlphaFoldDB; Q7SIG4; -.
DR BMRB; Q7SIG4; -.
DR SMR; Q7SIG4; -.
DR BRENDA; 3.1.8.2; 3066.
DR SABIO-RK; Q7SIG4; -.
DR EvolutionaryTrace; Q7SIG4; -.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047862; F:diisopropyl-fluorophosphatase activity; IDA:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR013658; SGL.
DR Pfam; PF08450; SGL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Metal-binding.
FT CHAIN 1..314
FT /note="Diisopropyl-fluorophosphatase"
FT /id="PRO_0000248834"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15966726"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11435114,
FT ECO:0000269|PubMed:14501113"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11435114,
FT ECO:0000269|PubMed:14501113"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11435114,
FT ECO:0000269|PubMed:14501113"
FT MUTAGEN 21
FT /note="E->Q: 100% decrease in activity. Loss of calcium 1
FT binding."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 37
FT /note="E->Q: 50% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 77
FT /note="Q->F: 100% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 77
FT /note="Q->W: No effect on activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 77
FT /note="Q->Y: 6% increase in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 120
FT /note="N->D: 96% decrease in activity. 100% decrease in
FT activity; when associated with N-229."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 121
FT /note="D->F: 100% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 144
FT /note="Y->S: 8% increase in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 146
FT /note="R->S: 45% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 148
FT /note="M->A: 26% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->A: 84% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->L: 28% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->S: 68% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->V: 46% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->W: 19% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 173
FT /note="F->Y: 53% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 175
FT /note="N->D: 98% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 181
FT /note="H->N: 20% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 195
FT /note="T->A: 60% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 195
FT /note="T->L: 11% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 195
FT /note="T->V: 3% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 219
FT /note="H->N: 3% increase in activity."
FT /evidence="ECO:0000269|PubMed:11295437"
FT MUTAGEN 224
FT /note="H->N: 14% increase in activity."
FT /evidence="ECO:0000269|PubMed:11295437"
FT MUTAGEN 229
FT /note="D->N: 100% decrease in activity. Loss of calcium 1
FT binding. 100% decrease in activity; when associated with D-
FT 120."
FT /evidence="ECO:0000269|PubMed:11435114,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 232
FT /note="D->S: 3% increase in activity. 19% decrease in
FT activity; when associated with A-271."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 237
FT /note="N->S: 4% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 244
FT /note="W->F: 44% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 244
FT /note="W->H: 27% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 244
FT /note="W->L: 62% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 244
FT /note="W->Y: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11435114"
FT MUTAGEN 248
FT /note="H->N: 4% increase in activity."
FT /evidence="ECO:0000269|PubMed:11295437"
FT MUTAGEN 271
FT /note="S->A: 30% increase in activity. 19% decrease in
FT activity; when associated with S-232."
FT /evidence="ECO:0000269|PubMed:11435114,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 272
FT /note="N->F: 100% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 274
FT /note="H->N: 85% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->A: 90% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->F: 36% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->L: 21% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->N: 97% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->Q: 54% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->W: 44% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 287
FT /note="H->Y: 57% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11295437,
FT ECO:0000269|PubMed:15966726"
FT MUTAGEN 304
FT /note="Q->F: 50% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 304
FT /note="Q->W: 3% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT MUTAGEN 314
FT /note="F->A: 3% increase in activity."
FT /evidence="ECO:0000269|PubMed:15966726"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1PJX"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:4O5S"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3HLH"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4O5S"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 164..181
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3LI3"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:1PJX"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:1PJX"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1PJX"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:3LI4"
SQ SEQUENCE 314 AA; 35080 MW; 8A3F3D84002A6EA8 CRC64;
MEIPVIEPLF TKVTEDIPGA EGPVFDKNGD FYIVAPEVEV NGKPAGEILR IDLKTGKKTV
ICKPEVNGYG GIPAGCQCDR DANQLFVADM RLGLLVVQTD GTFEEIAKKD SEGRRMQGCN
DCAFDYEGNL WITAPAGEVA PADYTRSMQE KFGSIYCFTT DGQMIQVDTA FQFPNGIAVR
HMNDGRPYQL IVAETPTKKL WSYDIKGPAK IENKKVWGHI PGTHEGGADG MDFDEDNNLL
VANWGSSHIE VFGPDGGQPK MRIRCPFEKP SNLHFKPQTK TIFVTEHENN AVWKFEWQRN
GKKQYCETLK FGIF
