CABC2_BACT4
ID CABC2_BACT4 Reviewed; 1014 AA.
AC C5G6D7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Chondroitin sulfate ABC exolyase {ECO:0000303|PubMed:18512954, ECO:0000312|EMBL:ABV21364.1};
DE EC=4.2.2.21 {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
DE AltName: Full=Chondroitin ABC exoeliminase {ECO:0000250|UniProtKB:C7S340};
DE AltName: Full=Chondroitin ABC lyase II {ECO:0000250|UniProtKB:C7S340, ECO:0000303|PubMed:18227125};
DE AltName: Full=Chondroitin sulfate ABC lyase II {ECO:0000250|UniProtKB:C7S340, ECO:0000303|PubMed:18512954};
DE Short=ChS ABC lyase II {ECO:0000250|UniProtKB:C7S340};
DE AltName: Full=Chondroitinase ABC II {ECO:0000250|UniProtKB:C7S340, ECO:0000303|PubMed:18227125};
DE Short=cABC II {ECO:0000250|UniProtKB:C7S340};
DE AltName: Full=Exochondroitinase ABC {ECO:0000250|UniProtKB:C7S340};
DE Flags: Precursor;
GN Name=chonabc;
OS Bacteroides thetaiotaomicron.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=818;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE RESIDUES, AND MUTAGENESIS OF HIS-344; HIS-345; HIS-453;
RP HIS-454; TYR-461 AND GLU-628.
RC STRAIN=ATCC 29741 / DSM 2255 / WAL 2926 {ECO:0000269|PubMed:18512954};
RX PubMed=18512954; DOI=10.1021/bi800353g;
RA Shaya D., Hahn B.S., Park N.Y., Sim J.S., Kim Y.S., Cygler M.;
RT "Characterization of chondroitin sulfate lyase ABC from Bacteroides
RT thetaiotaomicron WAL2926.";
RL Biochemistry 47:6650-6661(2008).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABV21364.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE RESIDUES,
RP MUTAGENESIS OF ARG-172; GLN-173; ARG-267; HIS-344; HIS-345; HIS-453;
RP HIS-454; TYR-461; ARG-514 AND GLU-628, AND X-RAY CRYSTALLOGRAPHY (2.85
RP ANGSTROMS) IN COMPLEX WITH CALCIUM.
RC STRAIN=ATCC 29741 / DSM 2255 / WAL 2926 {ECO:0000312|EMBL:ABV21364.1};
RX PubMed=18227125; DOI=10.1093/glycob/cwn002;
RA Shaya D., Hahn B.S., Bjerkan T.M., Kim W.S., Park N.Y., Sim J.S., Kim Y.S.,
RA Cygler M.;
RT "Composite active site of chondroitin lyase ABC accepting both epimers of
RT uronic acid.";
RL Glycobiology 18:270-277(2008).
CC -!- FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an
CC exolytic fashion degrading chondroitin sulfates and dermatan sulfate to
CC yield only disaccharide products. Has a preference for chondroitin 4-
CC sulfate over chondroitin 6-sulfate. Has extremely low activity against
CC hyaluronic acid. Is not active against acharan sulfate, heparin or
CC heparan sulfate. {ECO:0000269|PubMed:18512954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic removal of Delta(4)-unsaturated disaccharide residues
CC from the non-reducing ends of both polymeric chondroitin/dermatan
CC sulfates and their oligosaccharide fragments.; EC=4.2.2.21;
CC Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC Note=Divalent metal cation. Requires divalent metal cation for binding
CC of dermatan sulfate substrate, whereas it is not necessary for the
CC binding of chondroitin sulfate substrates. Prefers Ca(2+) or Mg(2+),
CC binding 1 ion per subunit. {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC -!- ACTIVITY REGULATION: Specific activity for chondroitin sulfate
CC substrates increases moderately (2-fold) while an increase of 25-fold
CC is observed for dermatan sulfate as substrate upon addition of Ca(2+)
CC or Mg(2+) ions (PubMed:18227125). Increasing the concentration of
CC Na(+), K(+) or Cs(+) chloride from 0 to 0.1 M, increases the activity
CC against all substrates. Further increases in salt concentration reduces
CC the activity dramatically, with 50% inhibition occurring at 0.15 M and
CC nearly complete inhibition at 0.4 M salt. The addition of 10 mM Ca(2+)
CC or Mg(2+) ions increases the activity against chondroitin 4- and 6-
CC sulfates by 2-3-fold, while the activity against dermatan sulfate
CC increases much more significantly by 50-fold (PubMed:18512954).
CC Addition of Mn(2+) and Zn(2+) reduces activity against chondroitin
CC sulfate substrates, but increases the activity against dermatan
CC sulfate. Increasing the concentration of CaCl(2) with both chondroitin
CC 4- and 6-sulfates from 0 to 0.04 M increases the activity. A further
CC increase reduces activity, with 50% inhibition at 0.065-0.085 M and a
CC complete inhibition of the reaction at 0.2 M. In case of dermatan
CC sulfate, the addition of low concentration of CaCl(2) dramatically
CC increases the activity from the basal level. The maximal activity is
CC reached at 0.01 M CaCl(2). {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for chondroitin 4-sulfate from porcine or bovine trachea (at
CC 37 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC KM=33 uM for chondroitin 6-sulfate from shark cartilage (at 37
CC degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC KM=61 uM for dermatan sulfate from porcine intestinal mucosa (at 37
CC degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC Vmax=77.6 umol/min/mg enzyme with chondroitin 4-sulfate from bovine
CC trachea as substrate (at 37 degrees Celsius and in 50 mM phosphate at
CC pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC Vmax=47.4 umol/min/mg enzyme with chondroitin 6-sulfate from shark
CC cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate
CC at pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC Vmax=14.4 umol/min/mg enzyme with chondroitin 2,6-sulfate from skate
CC cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate
CC at pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC Vmax=28.5 umol/min/mg enzyme with chondroitin 4,6-sulfate from squid
CC cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate
CC at pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC Vmax=9.1 umol/min/mg enzyme with dermatan sulfate from porcine
CC intestinal mucosa as substrate (at 37 degrees Celsius and in 50 mM
CC phosphate at pH 7.6) {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC Note=kcat is 15792 min(-1) with chondroitin 4-sulfate from porcine or
CC bovine trachea as substrate. kcat is 10404 min(-1) with chondroitin
CC 6-sulfate from shark cartilage as substrate. kcat is 2307 min(-1)
CC with dermatan sulfate from porcine intestinal mucosa as substrate.
CC {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC pH dependence:
CC Optimum pH is 7.6. Decreased activity at pH values below 7.0 and
CC above 8.0. The activity against chondroitin 6-sulfate remains higher
CC than with other substrates at low pH. At pH 6.5 the enzyme exhibits
CC almost 60% of its maximal activity against chondroitin 6-sulfate,
CC only 20% activity against chondroitin 4-sulfate and no measurable
CC activity against dermatan sulfate. In contrast, at pH of 8.5 about
CC 30% of enzyme's maximal activity against all substrates is displayed.
CC {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. No significant reduction
CC in activity at temperatures in the range of 25-40 degrees Celsius. At
CC 50 degrees Celsius, activity of 45% for dermatan sulfate, 60% for
CC chondroitin 4-sulfate and 75% for chondroitin 6-sulfate is detected.
CC Thermal denaturation curve is bimodal with two consecutive thermal
CC denaturation midpoints (Tm) corresponding to 44 and 50 degrees
CC Celsius, respectively. {ECO:0000269|PubMed:18227125,
CC ECO:0000269|PubMed:18512954};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18227125}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q8A2I1}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV21364.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; EF639172; ABV21364.1; ALT_SEQ; Genomic_DNA.
DR PDB; 2Q1F; X-ray; 2.85 A; A/B=1-1014.
DR PDBsum; 2Q1F; -.
DR AlphaFoldDB; C5G6D7; -.
DR SMR; C5G6D7; -.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR SABIO-RK; C5G6D7; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:InterPro.
DR GO; GO:0034001; F:chondroitin-sulfate-ABC exolyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030209; P:dermatan sulfate catabolic process; IDA:UniProtKB.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR039174; Chondroitin_ABC_lyase.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR024200; Chondroitinase_ABC_I.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR InterPro; IPR015177; Lyase_catalyt.
DR InterPro; IPR015176; Lyase_N.
DR PANTHER; PTHR37322; PTHR37322; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF09093; Lyase_catalyt; 1.
DR Pfam; PF09092; Lyase_N; 1.
DR PIRSF; PIRSF034515; Chondroitinase; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Lyase; Metal-binding;
KW Periplasm; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1014
FT /note="Chondroitin sulfate ABC exolyase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420123"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18227125"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18227125"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18227125"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18227125"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18227125"
FT SITE 172
FT /note="Important for catalytic activity against all
FT substrates"
FT /evidence="ECO:0000269|PubMed:18227125"
FT SITE 344
FT /note="Important for catalytic activity against dermatan
FT sulfate substrate"
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT SITE 514
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:18227125"
FT SITE 628
FT /note="Important for catalytic activity against all
FT substrates"
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 172
FT /note="R->A: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125"
FT MUTAGEN 173
FT /note="Q->A: Reduced activity against all substrates by a
FT factor of about 2-10."
FT /evidence="ECO:0000269|PubMed:18227125"
FT MUTAGEN 267
FT /note="R->A: Reduced activity against all substrates by a
FT factor of about 2-10."
FT /evidence="ECO:0000269|PubMed:18227125"
FT MUTAGEN 344
FT /note="H->A: No detectable activity against dermatan
FT sulfate in the standard assay, but after overnight
FT incubation shows traces of degradation products, also still
FT degrades chondroitin sulfate albeit with 10- to 30-fold
FT lower catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 344
FT /note="H->D,E: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 344
FT /note="H->N: Retains 5-25% catalytic efficiency against all
FT substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 344
FT /note="H->Q: Retains 5% catalytic efficiency against
FT chondroitin 4-sulfate only."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 345
FT /note="H->A: No activity against dermatan sulfate even
FT after overnight incubation, but still degrades chondroitin
FT sulfate albeit with 10- to 30-fold lower catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 345
FT /note="H->D,E: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 345
FT /note="H->N,Q: Low levels of activity against chondroitin
FT sulfate substrates, but no activity against dermatan
FT sulfate."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 453
FT /note="H->A: Slightly reduced activity against all
FT substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 453
FT /note="H->N: Shows no activity against dermatan sulfate
FT while retaining about 10% of its catalytic efficiency
FT against chondroitin 4- and 6-sulfates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 454
FT /note="H->A,D,N,Q: Loss of activity against all
FT substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 461
FT /note="Y->A: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 514
FT /note="R->A: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125"
FT MUTAGEN 628
FT /note="E->A,D: Loss of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT MUTAGEN 628
FT /note="E->Q: Retains low levels of activity against
FT chondroitin sulfate substrates, but not against dermatan
FT sulfate as substrate."
FT /evidence="ECO:0000269|PubMed:18227125,
FT ECO:0000269|PubMed:18512954"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 34..46
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 156..169
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 313..332
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 418..435
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 459..476
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 485..501
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 524..531
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 601..604
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 642..648
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 658..662
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 683..686
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 719..727
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 737..745
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 748..757
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 761..773
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 777..782
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 790..794
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 808..818
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 820..822
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 825..840
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 842..853
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 856..864
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 869..882
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 883..886
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 887..894
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 903..929
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:2Q1F"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:2Q1F"
FT TURN 959..962
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 968..976
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 986..991
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 993..1002
FT /evidence="ECO:0007829|PDB:2Q1F"
FT STRAND 1007..1013
FT /evidence="ECO:0007829|PDB:2Q1F"
SQ SEQUENCE 1014 AA; 114921 MW; 10C46B91CF02A44A CRC64;
MLILSFLCPA FLNAQIVTDE RMFSFEEPQL PACITGVQSQ LGISGAHYKD GKHSLEWTFE
PNGRLELRKD LKFEKKDPTG KDLYLSAFIV WIYNEQPQDA AIEFEFLKDG RKCASFPFGI
NFKGWRAAWV CYERDMQGTP EEGMNELRIV APDAKGRLFI DHLITATKVD ARQQTADLQV
PFVNAGTTNH WLVLYKHSLL KPDIELTPVS DKQRQEMKLL EKRFRDMIYT KGKVTEKEAE
TIRKKYDLYQ ITYKDGQVSG VPVFMVRASE AYERMIPDWD KDMLTKMGIE MRAYFDLMKR
IAVAYNNSEA GSPIRKEMRR KFLAMYDHIT DQGVAYGSCW GNIHHYGYSV RGLYPAYFLM
KDVLREEGKL LEAERTLRWY AITNEVYPKP EGNGIDMDSF NTQTTGRIAS ILMMEDTPEK
LQYLKSFSRW IDYGCRPAPG LAGSFKVDGG AFHHRNNYPA YAVGGLDGAT NMIYLFSRTS
LAVSELAHRT VKDVLLAMRF YCNKLNFPLS MSGRHPDGKG KLVPMHYAIM AIAGTPDGKG
DFDKEMASAY LRLVSSDSSS AEQAPEYMPK VSNAQERKIA KRLVENGFRA EPDPQGNLSL
GYGCVSVQRR ENWSAVARGH SRYLWAAEHY LGHNLYGRYL AHGSLQILTA PPGQTVTPTT
SGWQQEGFDW NRIPGVTSIH LPLDLLKANV LNVDTFSGME EMLYSDEAFA GGLSQGKMNG
NFGMKLHEHD KYNGTHRARK SFHFIDGMIV CLGSDIENTN MDYPTETTIF QLAVTDKAAH
DYWKNNAGEG KVWMDHLGTG YYVPVAARFE KNFPQYSRMQ DTGKETKGDW VSLIIDHGKA
PKAGSYEYAI LPGTDRKTMT AFAKKPAYSV LQQDRNAHIL ESPSDRITSY VLFETPQSLL
PGGLLQRTDT SCLVMVRKES ADKVLLTVAQ PDLALYRGPS DEAFDKDGKR MERSIYSRPW
IDNESGEIPV TVTLKGRWKV VETPYCKVVS EDKKQTVLRF LCKDGASYEV ELEK
