MUTB_PROFR
ID MUTB_PROFR Reviewed; 728 AA.
AC P11653;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Methylmalonyl-CoA mutase large subunit;
DE EC=5.4.99.2 {ECO:0000269|PubMed:9772164};
DE AltName: Full=MCM-alpha;
GN Name=mutB;
OS Propionibacterium freudenreichii subsp. shermanii.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=1752;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21 AND 104-110,
RP SUBUNIT, AND FUNCTION.
RC STRAIN=NCIMB 9885;
RX PubMed=2569861; DOI=10.1042/bj2600345;
RA Marsh E.N., McKie N., Davis N.K., Leadlay P.F.;
RT "Cloning and structural characterization of the genes coding for
RT adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium
RT shermanii.";
RL Biochem. J. 260:345-352(1989).
RN [2]
RP PROTEIN SEQUENCE OF 534-537.
RC STRAIN=NCIMB 9885;
RX PubMed=2569860; DOI=10.1042/bj2600339;
RA Marsh E.N., Leadlay P.F.;
RT "Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for
RT the presence of two masked cysteine residues.";
RL Biochem. J. 260:339-343(1989).
RN [3] {ECO:0007744|PDB:1REQ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COBALAMIN;
RP DESULFO-COENZYME A AND METHYLMALONYL-COA MUTASE SMALL SUBUNIT, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=NCIMB 9885;
RX PubMed=8805541; DOI=10.1016/s0969-2126(96)00037-8;
RA Mancia F., Keep N.H., Nakagawa A., Leadlay P.F., McSweeney S.,
RA Rasmussen B., Bosecke P., Diat O., Evans P.R.;
RT "How coenzyme B12 radicals are generated: the crystal structure of
RT methylmalonyl-coenzyme A mutase at 2-A resolution.";
RL Structure 4:339-350(1996).
RN [4] {ECO:0007744|PDB:5REQ}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT PHE-89 IN COMPLEX WITH
RP COBALAMIN; SUBSTRATE ANALOGS AND METHYLMALONYL-COA MUTASE SMALL SUBUNIT,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-89.
RX PubMed=9772164; DOI=10.1021/bi981375o;
RA Thoma N.H., Meier T.W., Evans P.R., Leadlay P.F.;
RT "Stabilization of radical intermediates by an active-site tyrosine residue
RT in methylmalonyl-CoA mutase.";
RL Biochemistry 37:14386-14393(1998).
RN [5] {ECO:0007744|PDB:2REQ, ECO:0007744|PDB:3REQ}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH COBALAMIN;
RP COENZYME A AND METHYLMALONYL-COA MUTASE SMALL SUBUNIT.
RX PubMed=9655823; DOI=10.1016/s0969-2126(98)00073-2;
RA Mancia F., Evans P.R.;
RT "Conformational changes on substrate binding to methylmalonyl CoA mutase
RT and new insights into the free radical mechanism.";
RL Structure 6:711-720(1998).
RN [6] {ECO:0007744|PDB:4REQ, ECO:0007744|PDB:6REQ, ECO:0007744|PDB:7REQ}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH
RP (R)-METHYLMALONYL-COA; SUCCINYL-COA; COBALAMIN; 5'-DEOXYADENOSINE; 3- AND
RP 2-CARBOXYPROPYL-COA INHIBITORS AND METHYLMALONYL-COA MUTASE SMALL SUBUNIT,
RP AND COFACTOR.
RX PubMed=10387043; DOI=10.1021/bi9903852;
RA Mancia F., Smith G.A., Evans P.R.;
RT "Crystal structure of substrate complexes of methylmalonyl-CoA mutase.";
RL Biochemistry 38:7999-8005(1999).
CC -!- FUNCTION: Catalyzes the reversible conversion of succinyl-CoA to (R)-
CC methylmalonyl-CoA through a radical mechanism (PubMed:9772164). Is
CC involved in the fermentation of pyruvate to propanoate that occurs in
CC Propionibacteria (Probable). {ECO:0000269|PubMed:9772164,
CC ECO:0000305|PubMed:2569861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC Evidence={ECO:0000269|PubMed:9772164};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22890;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541,
CC ECO:0000269|PubMed:9772164};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for succinyl-CoA {ECO:0000269|PubMed:9772164};
CC Note=kcat is 48 sec(-1) with succinyl-CoA as substrate.
CC {ECO:0000269|PubMed:9772164};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000269|PubMed:2569861, ECO:0000269|PubMed:8805541}.
CC -!- INTERACTION:
CC P11653; P11652: mutA; NbExp=4; IntAct=EBI-1027336, EBI-1027328;
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; X14965; CAA33090.1; -; Genomic_DNA.
DR PIR; S04641; S04641.
DR RefSeq; WP_044636063.1; NZ_OVTV01000167.1.
DR PDB; 1E1C; X-ray; 2.62 A; A/C=2-728.
DR PDB; 1REQ; X-ray; 2.00 A; A/C=2-728.
DR PDB; 2REQ; X-ray; 2.50 A; A/C=2-728.
DR PDB; 3REQ; X-ray; 2.70 A; A=2-728.
DR PDB; 4REQ; X-ray; 2.20 A; A/C=2-728.
DR PDB; 5REQ; X-ray; 2.20 A; A/C=2-728.
DR PDB; 6REQ; X-ray; 2.20 A; A/C=2-728.
DR PDB; 7REQ; X-ray; 2.20 A; A/C=2-728.
DR PDBsum; 1E1C; -.
DR PDBsum; 1REQ; -.
DR PDBsum; 2REQ; -.
DR PDBsum; 3REQ; -.
DR PDBsum; 4REQ; -.
DR PDBsum; 5REQ; -.
DR PDBsum; 6REQ; -.
DR PDBsum; 7REQ; -.
DR AlphaFoldDB; P11653; -.
DR SMR; P11653; -.
DR DIP; DIP-6148N; -.
DR IntAct; P11653; 1.
DR MINT; P11653; -.
DR GeneID; 61222542; -.
DR BioCyc; MetaCyc:MON-13077; -.
DR BRENDA; 5.4.99.2; 5032.
DR SABIO-RK; P11653; -.
DR EvolutionaryTrace; P11653; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase;
KW Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2569861"
FT CHAIN 2..728
FT /note="Methylmalonyl-CoA mutase large subunit"
FT /id="PRO_0000194273"
FT DOMAIN 597..728
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 75
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 78
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 82
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 85
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 87
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 89
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 114
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 117
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 139
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 195
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 197
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 206
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 207
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 207
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 244
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 283
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 285
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0007744|PDB:4REQ"
FT BINDING 333
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 370
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 373
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 609
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 610
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 611
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 612
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 655
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 657
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 686
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT BINDING 709
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:10387043,
FT ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ,
FT ECO:0007744|PDB:4REQ"
FT SITE 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:9772164"
FT MUTAGEN 89
FT /note="Y->F: Does not significantly affect affinity for
FT succiny-CoA, but kcat is lowered about 580-fold."
FT /evidence="ECO:0000269|PubMed:9772164"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4REQ"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:3REQ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3REQ"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6REQ"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 252..272
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 368..372
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 407..429
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 441..458
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:4REQ"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 485..502
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 505..520
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 531..540
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 545..556
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:1REQ"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:4REQ"
FT HELIX 578..594
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:3REQ"
FT HELIX 612..623
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:3REQ"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 661..674
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 680..687
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 711..726
FT /evidence="ECO:0007829|PDB:1REQ"
SQ SEQUENCE 728 AA; 80178 MW; F7731C1E3C9874C0 CRC64;
MSTLPRFDSV DLGNAPVPAD AARRFEELAA KAGTGEAWET AEQIPVGTLF NEDVYKDMDW
LDTYAGIPPF VHGPYATMYA FRPWTIRQYA GFSTAKESNA FYRRNLAAGQ KGLSVAFDLP
THRGYDSDNP RVAGDVGMAG VAIDSIYDMR ELFAGIPLDQ MSVSMTMNGA VLPILALYVV
TAEEQGVKPE QLAGTIQNDI LKEFMVRNTY IYPPQPSMRI ISEIFAYTSA NMPKWNSISI
SGYHMQEAGA TADIEMAYTL ADGVDYIRAG ESVGLNVDQF APRLSFFWGI GMNFFMEVAK
LRAARMLWAK LVHQFGPKNP KSMSLRTHSQ TSGWSLTAQD VYNNVVRTCI EAMAATQGHT
QSLHTNSLDE AIALPTDFSA RIARNTQLFL QQESGTTRVI DPWSGSAYVE ELTWDLARKA
WGHIQEVEKV GGMAKAIEKG IPKMRIEEAA ARTQARIDSG RQPLIGVNKY RLEHEPPLDV
LKVDNSTVLA EQKAKLVKLR AERDPEKVKA ALDKITWAAG NPDDKDPDRN LLKLCIDAGR
AMATVGEMSD ALEKVFGRYT AQIRTISGVY SKEVKNTPEV EEARELVEEF EQAEGRRPRI
LLAKMGQDGH DRGQKVIATA YADLGFDVDV GPLFQTPEET ARQAVEADVH VVGVSSLAGG
HLTLVPALRK ELDKLGRPDI LITVGGVIPE QDFDELRKDG AVEIYTPGTV IPESAISLVK
KLRASLDA
