ML1_VISAL
ID ML1_VISAL Reviewed; 564 AA.
AC P81446; P81830; Q6H270; Q6H271; Q8RXH6; Q9S7D0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Beta-galactoside-specific lectin 1;
DE AltName: Full=Beta-galactoside-specific lectin I;
DE AltName: Full=Viscumin;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 1 chain A isoform 1;
DE EC=3.2.2.22;
DE AltName: Full=Beta-galactoside-specific lectin I chain A isoform 1;
DE AltName: Full=ML-I A;
DE Short=MLA;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 1 chain B;
DE AltName: Full=Beta-galactoside-specific lectin I chain B;
DE AltName: Full=ML-I B;
DE Short=MLB;
DE Flags: Precursor;
OS Viscum album (European mistletoe).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Viscaceae; Viscum.
OX NCBI_TaxID=3972;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Leaf;
RX PubMed=15182350; DOI=10.1111/j.1432-1033.2004.04153.x;
RA Kourmanova A.G., Soudarkina O.J., Olsnes S., Kozlov J.V.;
RT "Cloning and characterization of the genes encoding toxic lectins in
RT mistletoe (Viscum album L).";
RL Eur. J. Biochem. 271:2350-2360(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-564, PROTEIN SEQUENCE OF 34-53, AND
RP FUNCTION.
RC TISSUE=Leaf;
RX PubMed=15001393; DOI=10.1016/j.abb.2003.12.033;
RA Mishra V., Sharma R.S., Yadav S., Babu C.R., Singh T.P.;
RT "Purification and characterization of four isoforms of Himalayan mistletoe
RT ribosome-inactivating protein from Viscum album having unique sugar
RT affinity.";
RL Arch. Biochem. Biophys. 423:288-301(2004).
RN [3]
RP PROTEIN SEQUENCE OF 34-287 (CHAIN A), AND VARIANTS ASP-48; THR-145;
RP THR-149; 166-GLU-GLU-167; SER-173; TYR-177; ALA-184; ASP-212; GLU-217;
RP MET-223; PHE-251; 256-SER-THR-257; SER-264 AND SER-268.
RX PubMed=8980141; DOI=10.1016/s0014-5793(96)01309-9;
RA Soler M.H., Stoeva S., Schwamborn C., Wilhelm S., Stiefel T., Voelter W.;
RT "Complete amino acid sequence of the A chain of mistletoe lectin I.";
RL FEBS Lett. 399:153-157(1996).
RN [4]
RP PROTEIN SEQUENCE OF 34-62, AND FUNCTION.
RX PubMed=1450445; DOI=10.1097/00001813-199210000-00010;
RA Dietrich J.B., Ribereau-Gayon G., Jung M.L., Franz H., Beck J.P., Anton R.;
RT "Identity of the N-terminal sequences of the three A chains of mistletoe
RT (Viscum album L.) lectins: homology with ricin-like plant toxins and
RT single-chain ribosome-inhibiting proteins.";
RL Anticancer Drugs 3:507-511(1992).
RN [5]
RP PROTEIN SEQUENCE OF 302-564 (CHAIN B), AND VARIANTS SER-319; ASN-357;
RP GLN-458; VAL-495; TYR-524; SER-531; THR-531; 531-LYS--PRO-533 AND
RP 532-SER--VAL-535.
RX PubMed=9618256; DOI=10.1006/bbrc.1998.8670;
RA Soler M.H., Stoeva S., Voelter W.;
RT "Complete amino acid sequence of the B chain of mistletoe lectin I.";
RL Biochem. Biophys. Res. Commun. 246:596-601(1998).
RN [6]
RP 3D-STRUCTURE MODELING OF 34-287 AND 302-564.
RX PubMed=9642133; DOI=10.1006/bbrc.1998.8760;
RA Eschenburg S., Krauspenhaar R., Mikhailov A., Stoeva S., Betzel C.,
RA Voelter W.;
RT "Primary structure and molecular modeling of mistletoe lectin I from Viscum
RT album.";
RL Biochem. Biophys. Res. Commun. 247:367-372(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-287 AND 302-564 IN COMPLEX WITH
RP AMP.
RX PubMed=12351890; DOI=10.1107/s0907444902014270;
RA Krauspenhaar R., Rypniewski W., Kalkura N., Moore K., DeLucas L.,
RA Stoeva S., Mikhailov A., Voelter W., Betzel C.;
RT "Crystallisation under microgravity of mistletoe lectin I from Viscum album
RT with adenine monophosphate and the crystal structure at 1.9 A resolution.";
RL Acta Crystallogr. D 58:1704-1707(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH
RP GALACTOSE, SUBUNIT, GLYCOSYLATION AT ASN-145; ASN-362; ASN-397 AND ASN-437,
RP AND DISULFIDE BONDS.
RX PubMed=12823544; DOI=10.1046/j.1432-1033.2003.03646.x;
RA Niwa H., Tonevitsky A.G., Agapov I.I., Saward S., Pfueller U., Palmer R.A.;
RT "Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II
RT ribosome-inactivating protein, complexed with galactose.";
RL Eur. J. Biochem. 270:2739-2749(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH
RP LACTOSE AND GALACTOSE.
RX PubMed=16508080; DOI=10.1107/s1744309104031501;
RA Mikeska R., Wacker R., Arni R., Singh T.P., Mikhailov A., Gabdoulkhakov A.,
RA Voelter W., Betzel C.;
RT "Mistletoe lectin I in complex with galactose and lactose reveals distinct
RT sugar-binding properties.";
RL Acta Crystallogr. F 61:17-25(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-287 AND 302-563.
RA Gabdoulkhakov A.G., Savoshkina Y., Krauspenhaar R., Stoeva S., Konareva N.,
RA Kornilov V., Kornev A.N., Voelter W., Nikonov S.V., Betzel C.,
RA Mikhailov A.M.;
RT "Mistletoe lectin I From Viscum album.";
RL Submitted (FEB-2003) to the PDB data bank.
CC -!- FUNCTION: The A chain is responsible for inhibiting protein synthesis
CC through the catalytic inactivation of 60S ribosomal subunits by
CC removing adenine from position 4,324 of 28S rRNA. The B chain binds to
CC cell receptors and probably facilitates the entry into the cell of the
CC A chain; B chains are also responsible for cell agglutination (lectin
CC activity). Inhibits growth of the human tumor cell line Molt4.
CC {ECO:0000269|PubMed:1450445, ECO:0000269|PubMed:15001393,
CC ECO:0000269|PubMed:15182350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC {ECO:0000269|PubMed:12351890, ECO:0000269|PubMed:12823544,
CC ECO:0000269|PubMed:16508080}.
CC -!- PTM: The A chain of variant MLA' is not glycosylated.
CC {ECO:0000269|PubMed:12823544}.
CC -!- PHARMACEUTICAL: Due to its immunomodulative effects it is being studied
CC in clinical trials in cancer patients as it may slow the growth of
CC cancer cells and be an effective treatment for solid tumors.
CC -!- MISCELLANEOUS: Several isoforms exist.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; AY377890; AAR25545.1; -; Genomic_DNA.
DR EMBL; AY377891; AAR25546.1; -; mRNA.
DR EMBL; AY081149; AAL87006.1; -; mRNA.
DR PIR; JW0090; JW0090.
DR PIR; PD0018; PD0018.
DR PIR; PD0019; PD0019.
DR PDB; 1M2T; X-ray; 1.89 A; A=34-287, B=313-564.
DR PDB; 1ONK; X-ray; 2.10 A; A=34-287, B=302-563.
DR PDB; 1OQL; X-ray; 3.00 A; A=34-282, B=302-564.
DR PDB; 1PUM; X-ray; 2.30 A; A=34-282, B=302-564.
DR PDB; 1PUU; X-ray; 2.30 A; A=34-282, B=302-564.
DR PDB; 1SZ6; X-ray; 2.05 A; A=34-282, B=302-564.
DR PDB; 2R9K; X-ray; 2.70 A; A=34-287, B=302-564.
DR PDB; 2RG9; X-ray; 1.95 A; A=34-282, B=302-564.
DR PDB; 3D7W; X-ray; 2.49 A; A=34-287, B=302-564.
DR PDB; 3O5W; X-ray; 2.70 A; A=34-287, B=302-564.
DR PDB; 4EB2; X-ray; 1.94 A; A=34-282, B=302-564.
DR PDB; 4JKX; X-ray; 2.35 A; A=34-282, B=302-564.
DR PDB; 6ELY; X-ray; 2.84 A; A=34-282, B=302-564.
DR PDBsum; 1M2T; -.
DR PDBsum; 1ONK; -.
DR PDBsum; 1OQL; -.
DR PDBsum; 1PUM; -.
DR PDBsum; 1PUU; -.
DR PDBsum; 1SZ6; -.
DR PDBsum; 2R9K; -.
DR PDBsum; 2RG9; -.
DR PDBsum; 3D7W; -.
DR PDBsum; 3O5W; -.
DR PDBsum; 4EB2; -.
DR PDBsum; 4JKX; -.
DR PDBsum; 6ELY; -.
DR AlphaFoldDB; P81446; -.
DR SMR; P81446; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; P81446; -.
DR iPTMnet; P81446; -.
DR BRENDA; 3.2.2.22; 6669.
DR EvolutionaryTrace; P81446; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; PTHR33453; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lectin; Pharmaceutical; Plant defense;
KW Protein synthesis inhibitor; Repeat; Signal; Toxin.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1450445,
FT ECO:0000269|PubMed:15001393, ECO:0000269|PubMed:8980141"
FT CHAIN 34..287
FT /note="Beta-galactoside-specific lectin 1 chain A isoform
FT 1"
FT /id="PRO_0000030749"
FT PROPEP 288..301
FT /note="Connecting peptide"
FT /evidence="ECO:0000269|PubMed:9618256"
FT /id="PRO_0000030750"
FT CHAIN 302..564
FT /note="Beta-galactoside-specific lectin 1 chain B"
FT /id="PRO_0000030751"
FT DOMAIN 309..436
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 440..564
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT BINDING 324..326
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT BINDING 536..538
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12823544"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12823544"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12823544"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12823544"
FT DISULFID 280..306
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:12823544"
FT DISULFID 365..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:12823544"
FT DISULFID 453..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:12823544"
FT DISULFID 492..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:12823544"
FT VARIANT 48
FT /note="E -> D (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 145
FT /note="N -> T (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 149
FT /note="P -> T (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 166..167
FT /note="DQ -> EE (in MLA')"
FT VARIANT 173
FT /note="T -> S (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 177
FT /note="F -> Y (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 184
FT /note="T -> A (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 212
FT /note="Y -> D (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 217
FT /note="A -> E (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 223
FT /note="V -> M (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 251
FT /note="I -> F (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 256..257
FT /note="PP -> ST (in MLA')"
FT VARIANT 264
FT /note="T -> S (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 268
FT /note="D -> S (in MLA')"
FT /evidence="ECO:0000269|PubMed:8980141"
FT VARIANT 319
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 357
FT /note="G -> N"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 458
FT /note="G -> Q"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 495
FT /note="C -> V"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 524
FT /note="G -> Y"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 531..533
FT /note="NGL -> KGP"
FT VARIANT 531
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 531
FT /note="N -> T"
FT /evidence="ECO:0000269|PubMed:9618256"
FT VARIANT 532..535
FT /note="GLAM -> SLMV"
FT CONFLICT 3
FT /note="G -> A (in Ref. 1; AAR25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 19..20
FT /note="GQ -> CL (in Ref. 1; AAR25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="L -> I (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> T (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="T -> S (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="E -> Q (in Ref. 1; AAR25545, 3; AA sequence and 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="G -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="D -> N (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="S -> P (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> N (in Ref. 2; AAL87006)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> I (in Ref. 1; AAR25545/AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> V (in Ref. 1; AAR25545/AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> L (in Ref. 1; AAR25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Q -> H (in Ref. 3; AA sequence and 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> E (in Ref. 2; AAL87006)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="C -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..393
FT /note="LWE -> IWQ (in Ref. 1; AAR25545, 2; AAL87006 and 5;
FT AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="G -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="V -> A (in Ref. 2; AAL87006)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="V -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="I -> S (in Ref. 1; AAR25545, 2; AAL87006 and 5; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..474
FT /note="QNQR -> KNQGK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="C -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 511..515
FT /note="AGSSG -> GASGS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 538..540
FT /note="AQA -> KGS (in Ref. 2; AAL87006)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="R -> Q (in Ref. 2; AAL87006)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="P -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3O5W"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6ELY"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6ELY"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2R9K"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:1M2T"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:1M2T"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1M2T"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1M2T"
SQ SEQUENCE 564 AA; 62628 MW; 8BC06110DD458A6E CRC64;
MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY FRFITLLRDY
VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT AAIDVTNLYV VAYQAGDQSY
FLRDAPRGAE THLFTGTTRS SLPFNGSYPD LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG
STRTQARSIL ILIQMISEAA RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ
QSTDGVFNNP IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL WTIKRDGTIR
SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI INPRSNLVLA ASSGIKGTTL
TVQTLDYTLG QGWLAGNDTA PREVTIYGFR DLCMESNGGS VWVETCVISQ QNQRWALYGD
GSIRPKQNQD QCLTCGRDSV STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA
NPKLRRIIIY PATGKPNQMW LPVP
