ID CARB_ECOLI Reviewed; 1073 AA. AC P00968; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 232. DE RecName: Full=Carbamoyl phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210}; DE EC=6.3.4.16 {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:4944634}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:4944634}; DE AltName: Full=Carbamoyl phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210, GN ECO:0000303|PubMed:6308632}; Synonyms=pyrA; GN OrderedLocusNames=b0033, JW0031; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-2. RC STRAIN=K12; RX PubMed=6308632; DOI=10.1073/pnas.80.15.4629; RA Nyunoya H., Lusty C.J.; RT "The carB gene of Escherichia coli: a duplicated gene coding for the large RT subunit of carbamoyl-phosphate synthetase."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6377309; DOI=10.1073/pnas.81.13.4139; RA Bouvier J., Patte J.-C., Stragier P.; RT "Multiple regulatory signals in the control region of the Escherichia coli RT carAB operon."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12; RX PubMed=1630901; DOI=10.1093/nar/20.13.3305; RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., RA Mizobuchi K., Nakata A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the RT 0-2.4 min region."; RL Nucleic Acids Res. 20:3305-3308(1992). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7. RX PubMed=6330744; DOI=10.1073/pnas.81.13.4134; RA Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M., RA Charlier D.R.M., Glansdorff N., Pierard A.; RT "DNA sequence of the carA gene and the control region of carAB: tandem RT promoters, respectively controlled by arginine and the pyrimidines, RT regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia RT coli K-12."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=4944634; DOI=10.1073/pnas.68.10.2599; RA Trotta P.P., Burt M.E., Haschemeyer R.H., Meister A.; RT "Reversible dissociation of carbamyl phosphate synthetase into a regulated RT synthesis subunit and a subunit required for glutamine utilization."; RL Proc. Natl. Acad. Sci. U.S.A. 68:2599-2603(1971). RN [8] RP FUNCTION, AND PATHWAY. RA Pierard A., Grenson M., Glansdorff N., Wiame J.M.; RT "A comparison of the organization of carbamylphosphate synthesis in RT Saccharomyces cerevisiae and Escherichia coli, based on genetical and RT biochemical evidences."; RL (In) Prusiner S.B., Stadtman E.R. (eds.); RL The Enzymes of Glutamine Metabolism, pp.483-503, Academic Press, New York RL (1973). RN [9] RP FUNCTION. RX PubMed=2868386; DOI=10.1016/s0076-6879(85)13044-2; RA Kaseman D.S., Meister A.; RT "Carbamyl phosphate synthetase (glutamine-utilizing) from Escherichia RT coli."; RL Methods Enzymol. 113:305-326(1985). RN [10] RP FUNCTION. RX PubMed=2658488; DOI=10.1002/9780470123089.ch7; RA Meister A.; RT "Mechanism and regulation of the glutamine-dependent carbamyl phosphate RT synthetase of Escherichia coli."; RL Adv. Enzymol. Relat. Areas Mol. Biol. 62:315-374(1989). RN [11] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=9174345; DOI=10.1021/bi970503q; RA Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.; RT "Structure of carbamoyl phosphate synthetase: a journey of 96 A from RT substrate to product."; RL Biochemistry 36:6305-6316(1997). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE. RX PubMed=9636022; DOI=10.1021/bi9807761; RA Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M., RA Holden H.M.; RT "Carbamoyl phosphate synthetase: caught in the act of glutamine RT hydrolysis."; RL Biochemistry 37:8825-8831(1998). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE. RX PubMed=10089390; DOI=10.1107/s0907444998006234; RA Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.; RT "The structure of carbamoyl phosphate synthetase determined to 2.1-A RT resolution."; RL Acta Crystallogr. D 55:8-24(1999). RN [15] {ECO:0007744|PDB:1BXR} RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND RP MANGANESE. RX PubMed=10029528; DOI=10.1021/bi982517h; RA Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.; RT "Carbamoyl phosphate synthetase: closure of the B-domain as a result of RT nucleotide binding."; RL Biochemistry 38:2347-2357(1999). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE. RX PubMed=10587438; DOI=10.1021/bi991741j; RA Thoden J.B., Huang X., Raushel F.M., Holden H.M.; RT "The small subunit of carbamoyl phosphate synthetase: snapshots along the RT reaction pathway."; RL Biochemistry 38:16158-16166(1999). RN [17] {ECO:0007744|PDB:1CE8} RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE. RX PubMed=10428826; DOI=10.1074/jbc.274.32.22502; RA Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.; RT "The binding of inosine monophosphate to Escherichia coli carbamoyl RT phosphate synthetase."; RL J. Biol. Chem. 274:22502-22507(1999). CC -!- FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl CC phosphate from the ammonia moiety of glutamine, carbonate, and CC phosphate donated by ATP, constituting the first step of 2 biosynthetic CC pathways, one leading to arginine and/or urea and the other to CC pyrimidine nucleotides. The large subunit (synthetase) binds the CC substrates ammonia (free or transferred from glutamine from the small CC subunit), hydrogencarbonate and ATP and carries out an ATP-coupled CC ligase reaction, activating hydrogencarbonate by forming carboxy CC phosphate which reacts with ammonia to form carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:2658488, CC ECO:0000269|PubMed:2868386, ECO:0000269|PubMed:4944634, CC ECO:0000269|Ref.8}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl CC phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+); CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01210, ECO:0000269|PubMed:4944634}; CC -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase large chain]: CC Reaction=hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 CC ADP + phosphate + 2 H(+); Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; CC EC=6.3.4.16; Evidence={ECO:0000255|HAMAP-Rule:MF_01210, CC ECO:0000269|PubMed:4944634}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01210}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01210, ECO:0000269|PubMed:10428826}; CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01210, ECO:0000269|PubMed:10428826}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01210, CC ECO:0000305|Ref.8}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP- CC Rule:MF_01210, ECO:0000305|Ref.8}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by the CC large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of CC heterodimers (alpha,beta)4. {ECO:0000255|HAMAP-Rule:MF_01210, CC ECO:0000269|PubMed:4944634}. CC -!- INTERACTION: CC P00968; P0A6F1: carA; NbExp=14; IntAct=EBI-546118, EBI-546107; CC -!- DOMAIN: The large subunit is composed of 2 ATP-grasp domains that are CC involved in binding the 2 ATP molecules needed for carbamoyl phosphate CC synthesis. The N-terminal ATP-grasp domain (referred to as the CC carboxyphosphate synthetic component) catalyzes the ATP-dependent CC phosphorylation of hydrogencarbonate to carboxyphosphate and the CC subsequent nucleophilic attack by ammonia to form a carbamate CC intermediate. The C-terminal ATP-grasp domain (referred to as the CC carbamoyl phosphate synthetic component) then catalyzes the CC phosphorylation of carbamate with the second ATP to form the end CC product carbamoyl phosphate. The reactive and unstable enzyme CC intermediates are sequentially channeled from one active site to the CC next through the interior of the protein over a distance of at least 96 CC A. {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:9174345}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J01597; AAA23539.1; -; Genomic_DNA. DR EMBL; V01500; CAA24744.1; -; Genomic_DNA. DR EMBL; U00096; AAC73144.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96602.1; -; Genomic_DNA. DR PIR; A01198; SYECCP. DR RefSeq; NP_414574.1; NC_000913.3. DR RefSeq; WP_001126348.1; NZ_CP009789.1. DR PDB; 1A9X; X-ray; 1.80 A; A/C/E/G=1-1073. DR PDB; 1BXR; X-ray; 2.10 A; A/C/E/G=1-1073. DR PDB; 1C30; X-ray; 2.00 A; A/C/E/G=1-1073. DR PDB; 1C3O; X-ray; 2.10 A; A/C/E/G=1-1073. DR PDB; 1CE8; X-ray; 2.10 A; A/C/E/G=1-1073. DR PDB; 1CS0; X-ray; 2.00 A; A/C/E/G=1-1073. DR PDB; 1JDB; X-ray; 2.10 A; B/E/H/K=1-1073. DR PDB; 1KEE; X-ray; 2.10 A; A/C/E/G=1-1073. DR PDB; 1M6V; X-ray; 2.10 A; A/C/E/G=1-1073. DR PDB; 1T36; X-ray; 2.10 A; A/C/E/G=1-1073. DR AlphaFoldDB; P00968; -. DR SMR; P00968; -. DR BioGRID; 4259726; 51. DR BioGRID; 849177; 2. DR ComplexPortal; CPX-1937; Carbamoyl phosphate synthetase complex. DR DIP; DIP-1025N; -. DR FunCoup; P00968; 874. DR IntAct; P00968; 14. DR STRING; 511145.b0033; -. DR jPOST; P00968; -. DR PaxDb; 511145-b0033; -. DR EnsemblBacteria; AAC73144; AAC73144; b0033. DR GeneID; 944775; -. DR KEGG; ecj:JW0031; -. DR KEGG; eco:b0033; -. DR KEGG; ecoc:C3026_00170; -. DR PATRIC; fig|1411691.4.peg.2251; -. DR EchoBASE; EB0133; -. DR eggNOG; COG0458; Bacteria. DR HOGENOM; CLU_000513_1_0_6; -. DR InParanoid; P00968; -. DR OMA; FPFNKFP; -. DR OrthoDB; 9804197at2; -. DR PhylomeDB; P00968; -. DR BioCyc; EcoCyc:CARBPSYN-LARGE; -. DR BioCyc; MetaCyc:CARBPSYN-LARGE; -. DR BRENDA; 6.3.5.5; 2026. DR SABIO-RK; P00968; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR EvolutionaryTrace; P00968; -. DR PRO; PR:P00968; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P00968; -. DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:EcoCyc. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016597; F:amino acid binding; IDA:EcoliWiki. DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:EcoliWiki. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; EXP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki. DR GO; GO:0000166; F:nucleotide binding; IDA:EcoliWiki. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IMP:EcoliWiki. DR GO; GO:0006526; P:L-arginine biosynthetic process; IMP:EcoCyc. DR GO; GO:0006541; P:L-glutamine metabolic process; IBA:GO_Central. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:EcoliWiki. DR CDD; cd01424; MGS_CPS_II; 1. DR FunFam; 1.10.1030.10:FF:000002; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.30.1490.20:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.30.470.20:FF:000007; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.30.470.20:FF:000013; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.40.50.1380:FF:000004; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.40.50.20:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.40.50.20:FF:000003; Carbamoyl-phosphate synthase large chain; 1. DR Gene3D; 3.40.50.20; -; 2. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR005479; CPAse_ATP-bd. DR InterPro; IPR005483; CPSase_dom. DR InterPro; IPR006275; CPSase_lsu. DR InterPro; IPR005480; CPSase_lsu_oligo. DR InterPro; IPR058047; CPSase_preATP-grasp. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR033937; MGS_CPS_CarB. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR NCBIfam; NF003671; PRK05294.1; 1. DR NCBIfam; NF009455; PRK12815.1; 1. DR PANTHER; PTHR11405:SF53; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. DR Pfam; PF25596; CPSase_L_D1; 2. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS51855; MGS; 1. DR PDBsum; 1A9X; -. DR PDBsum; 1BXR; -. DR PDBsum; 1C30; -. DR PDBsum; 1C3O; -. DR PDBsum; 1CE8; -. DR PDBsum; 1CS0; -. DR PDBsum; 1JDB; -. DR PDBsum; 1KEE; -. DR PDBsum; 1M6V; -. DR PDBsum; 1T36; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Direct protein sequencing; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6308632" FT CHAIN 2..1073 FT /note="Carbamoyl phosphate synthase large chain" FT /id="PRO_0000145004" FT DOMAIN 133..328 FT /note="ATP-grasp 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT DOMAIN 679..870 FT /note="ATP-grasp 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT DOMAIN 937..1073 FT /note="MGS-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 2..403 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 404..553 FT /note="Oligomerization domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 554..936 FT /note="Carbamoyl phosphate synthetic domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 937..1073 FT /note="Allosteric domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 169 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 243 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 285 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10428826, ECO:0007744|PDB:1CE8" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:10587438, FT ECO:0000269|PubMed:9636022, ECO:0007744|PDB:1CE8" FT BINDING 299 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:10587438, FT ECO:0000269|PubMed:9636022, ECO:0007744|PDB:1CE8" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 301 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:10587438, FT ECO:0000269|PubMed:9636022, ECO:0007744|PDB:1CE8" FT BINDING 715 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 754 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 756 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 761 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 786 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 787 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 788 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 789 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 829 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 829 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 829 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:9636022, FT ECO:0007744|PDB:1CE8" FT BINDING 841 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0007744|PDB:1A9X, FT ECO:0007744|PDB:1C30, ECO:0007744|PDB:1C3O, FT ECO:0007744|PDB:1CE8, ECO:0007744|PDB:1CS0, FT ECO:0007744|PDB:1JDB, ECO:0007744|PDB:1KEE, FT ECO:0007744|PDB:1M6V, ECO:0007744|PDB:1T36" FT BINDING 841 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 841 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 841 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:9636022, FT ECO:0007744|PDB:1CE8" FT BINDING 841 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390, FT ECO:0000269|PubMed:10428826, ECO:0000269|PubMed:9636022, FT ECO:0007744|PDB:1CE8" FT BINDING 843 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 843 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210, FT ECO:0000269|PubMed:10029528, ECO:0000269|PubMed:10089390" FT STRAND 9..13 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 25..40 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 71..81 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 92..104 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 107..111 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 120..127 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 152..162 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 175..178 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 185..198 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 204..208 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 213..222 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 228..238 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 258..275 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 279..288 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 295..303 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 306..315 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 319..327 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 338..342 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 353..361 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 382..390 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 391..401 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 402..405 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 420..429 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 435..444 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 449..456 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 460..479 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 486..494 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 499..505 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 510..519 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 561..565 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 576..591 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 595..599 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 606..608 FT /evidence="ECO:0007829|PDB:1CS0" FT STRAND 612..617 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 623..633 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 636..639 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 641..643 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 645..648 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 651..656 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 661..664 FT /evidence="ECO:0007829|PDB:1CS0" FT HELIX 666..673 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 675..685 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 698..708 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 710..715 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 721..724 FT /evidence="ECO:0007829|PDB:1BXR" FT STRAND 725..728 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 731..740 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 751..754 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 760..768 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 773..783 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 789..791 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 794..797 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 799..801 FT /evidence="ECO:0007829|PDB:1JDB" FT HELIX 803..819 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 824..832 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 837..843 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 850..857 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 861..869 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 874..877 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 886..894 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 896..899 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 915..923 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 924..934 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 941..948 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 951..954 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 957..966 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 970..973 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 975..982 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 983..985 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 989..992 FT /evidence="ECO:0007829|PDB:1CS0" FT TURN 994..996 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 998..1000 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 1001..1007 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 1011..1015 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 1020..1025 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 1027..1035 FT /evidence="ECO:0007829|PDB:1A9X" FT STRAND 1039..1043 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 1044..1054 FT /evidence="ECO:0007829|PDB:1A9X" FT TURN 1058..1060 FT /evidence="ECO:0007829|PDB:1A9X" FT HELIX 1065..1070 FT /evidence="ECO:0007829|PDB:1A9X" SQ SEQUENCE 1073 AA; 117842 MW; A09D019CBDFF8D2B CRC64; MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK //