ID HV323_HUMAN Reviewed; 117 AA. AC P01764; A0A087WSX3; P01765; P01774; P01775; P01776; P01777; P01778; AC P01779; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2015, sequence version 2. DT 16-JAN-2019, entry version 151. DE RecName: Full=Immunoglobulin heavy variable 3-23 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.8}; DE AltName: Full=Ig heavy chain V-III region LAY {ECO:0000305|PubMed:4139708}; DE AltName: Full=Ig heavy chain V-III region POM {ECO:0000305|PubMed:4139708}; DE AltName: Full=Ig heavy chain V-III region TEI {ECO:0000305|PubMed:4522793}; DE AltName: Full=Ig heavy chain V-III region TIL {ECO:0000305|PubMed:409716}; DE AltName: Full=Ig heavy chain V-III region TUR {ECO:0000305|PubMed:4522793}; DE AltName: Full=Ig heavy chain V-III region VH26 {ECO:0000305|PubMed:6450418}; DE AltName: Full=Ig heavy chain V-III region WAS {ECO:0000305|PubMed:4522793}; DE AltName: Full=Ig heavy chain V-III region ZAP {ECO:0000305|PubMed:4522793}; DE Flags: Precursor; GN Name=IGHV3-23 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.8}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHV3-23*02), AND RP VARIANTS LEU-24 AND GLY-80. RX PubMed=6450418; DOI=10.1073/pnas.77.11.6561; RA Matthyssens G., Rabbitts T.H.; RT "Structure and multiplicity of genes for the human immunoglobulin RT heavy chain variable region."; RL Proc. Natl. Acad. Sci. U.S.A. 77:6561-6565(1980). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP IGHV3-23*04). RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24. RX PubMed=4522793; DOI=10.1073/pnas.71.3.845; RA Capra J.D., Kehoe J.M.; RT "Variable region sequences of five human immunoglobulin heavy chains RT of the VH3 subgroup: definitive identification of four heavy chain RT hypervariable regions."; RL Proc. Natl. Acad. Sci. U.S.A. 71:845-848(1974). RN [4] RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24. RX PubMed=4139708; DOI=10.1073/pnas.71.10.4032; RA Capra J.D., Kehoe J.M.; RT "Structure of antibodies with shared idiotypy: the complete sequence RT of the heavy chain variable regions of two immunoglobulin M anti-gamma RT globulins."; RL Proc. Natl. Acad. Sci. U.S.A. 71:4032-4036(1974). RN [5] RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24. RX PubMed=409716; RA Wang A.-C., Wang I.Y., Fudenberg H.H.; RT "Immunoglobulin structure and genetics. Identity between variable RT regions of a mu and a gamma2 chain."; RL J. Biol. Chem. 252:7192-7199(1977). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-117. RX PubMed=7681398; DOI=10.1002/eji.1830230412; RA Mariette X., Tsapis A., Brouet J.C.; RT "Nucleotidic sequence analysis of the variable domains of four human RT monoclonal IgM with an antibody activity to myelin-associated RT glycoprotein."; RL Eur. J. Immunol. 23:846-851(1993). RN [7] RP NOMENCLATURE. RX PubMed=11340299; RA Lefranc M.P.; RT "Nomenclature of the human immunoglobulin heavy (IGH) genes."; RL Exp. Clin. Immunogenet. 18:100-116(2001). RN [8] RP NOMENCLATURE. RA Lefranc M.P., Lefranc G.; RT "The Immunoglobulin FactsBook."; RL (In) Lefranc M.P., Lefranc G. (eds.); RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. RL (2001). RN [9] RP REVIEW ON SOMATIC HYPERMUTATION. RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340; RA Teng G., Papavasiliou F.N.; RT "Immunoglobulin somatic hypermutation."; RL Annu. Rev. Genet. 41:107-120(2007). RN [10] RP REVIEW ON IMMUNOGLOBULINS. RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046; RA Schroeder H.W. Jr., Cavacini L.; RT "Structure and function of immunoglobulins."; RL J. Allergy Clin. Immunol. 125:S41-S52(2010). RN [11] RP REVIEW ON FUNCTION. RX PubMed=22158414; DOI=10.1038/nri3128; RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.; RT "Molecular programming of B cell memory."; RL Nat. Rev. Immunol. 12:24-34(2012). RN [12] RP NOMENCLATURE. RX PubMed=24600447; DOI=10.3389/fimmu.2014.00022; RA Lefranc M.P.; RT "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and RT Rise of Immunoinformatics."; RL Front. Immunol. 5:22-22(2014). RN [13] RP 3D-STRUCTURE MODELING OF 20-117. RX PubMed=3866244; DOI=10.1073/pnas.82.24.8624; RA Toyonaga B., Yoshikai Y., Vadasz V., Chin B., Mak T.W.; RT "Organization and sequences of the diversity, joining, and constant RT region genes of the human T-cell receptor beta chain."; RL Proc. Natl. Acad. Sci. U.S.A. 82:8624-8628(1985). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-116, AND DISULFIDE BONDS. RX PubMed=15033359; DOI=10.1016/j.jmb.2004.02.013; RA Jespers L., Schon O., James L.C., Veprintsev D., Winter G.; RT "Crystal structure of HEL4, a soluble, refoldable human V(H) single RT domain with a germ-line scaffold."; RL J. Mol. Biol. 337:893-903(2004). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 20-116, AND DISULFIDE BONDS. RX PubMed=24892548; DOI=10.1371/journal.pone.0098178; RA Kim D.S., Song H.N., Nam H.J., Kim S.G., Park Y.S., Park J.C., RA Woo E.J., Lim H.K.; RT "Directed evolution of human heavy chain variable domain (VH) using in RT vivo protein fitness filter."; RL PLoS ONE 9:E98178-E98192(2014). CC -!- FUNCTION: V region of the variable domain of immunoglobulin heavy CC chains that participates in the antigen recognition CC (PubMed:24600447). Immunoglobulins, also known as antibodies, are CC membrane-bound or secreted glycoproteins produced by B CC lymphocytes. In the recognition phase of humoral immunity, the CC membrane-bound immunoglobulins serve as receptors which, upon CC binding of a specific antigen, trigger the clonal expansion and CC differentiation of B lymphocytes into immunoglobulins-secreting CC plasma cells. Secreted immunoglobulins mediate the effector phase CC of humoral immunity, which results in the elimination of bound CC antigens (PubMed:22158414, PubMed:20176268). The antigen binding CC site is formed by the variable domain of one heavy chain, together CC with that of its associated light chain. Thus, each immunoglobulin CC has two antigen binding sites with remarkable affinity for a CC particular antigen. The variable domains are assembled by a CC process called V-(D)-J rearrangement and can then be subjected to CC somatic hypermutations which, after exposure to antigen and CC selection, allow affinity maturation for a particular antigen CC (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170, CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, CC ECO:0000303|PubMed:24600447}. CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy CC chains and two identical light chains; disulfide-linked. CC {ECO:0000303|PubMed:20176268}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, CC ECO:0000303|PubMed:22158414}. Cell membrane CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. CC -!- POLYMORPHISM: There are several alleles. The sequence shown is CC that of IMGT allele IGHV3-23*04. {ECO:0000305}. CC -!- CAUTION: For examples of full-length immunoglobulin heavy chains CC (of different isotypes) see AC P0DOX2, AC P0DOX3, AC P0DOX4, AC CC P0DOX5 and AC P0DOX6. {ECO:0000305}. 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; M35415; AAA58735.1; -; Genomic_DNA. DR EMBL; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A02047; H3HU26. DR PIR; A02048; H3HUTL. DR PIR; A02057; M3HUPM. DR PIR; A02058; M3HULY. DR PIR; A02059; G1HUWS. DR PIR; A02060; G1HUTE. DR PIR; A02061; A1HUZP. DR PIR; A02062; A1HUTU. DR UniGene; Hs.719895; -. DR PDB; 1HOU; Model; -; H=20-117. DR PDB; 1OHQ; X-ray; 2.00 A; A/B=20-116. DR PDB; 3BN9; X-ray; 2.17 A; D/F=21-116. DR PDB; 3UPC; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=22-117. DR PDB; 3ZHD; X-ray; 1.96 A; A/B=20-116. DR PDB; 3ZHK; X-ray; 1.96 A; A/B=20-116. DR PDB; 3ZHL; X-ray; 2.47 A; A=20-116. DR PDB; 4KFZ; X-ray; 2.80 A; C/D=20-116. DR PDBsum; 1HOU; -. DR PDBsum; 1OHQ; -. DR PDBsum; 3BN9; -. DR PDBsum; 3UPC; -. DR PDBsum; 3ZHD; -. DR PDBsum; 3ZHK; -. DR PDBsum; 3ZHL; -. DR PDBsum; 4KFZ; -. DR ProteinModelPortal; P01764; -. DR SMR; P01764; -. DR IntAct; P01764; 1. DR DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide. DR IMGT_GENE-DB; IGHV3-23; -. DR BioMuta; IGHV3-23; -. DR DMDM; 123854; -. DR jPOST; P01764; -. DR PeptideAtlas; P01764; -. DR PRIDE; P01764; -. DR ProteomicsDB; 51463; -. DR ProteomicsDB; 51464; -. DR ProteomicsDB; 51473; -. DR ProteomicsDB; 51474; -. DR ProteomicsDB; 51475; -. DR ProteomicsDB; 51476; -. DR ProteomicsDB; 51477; -. DR ProteomicsDB; 51478; -. DR Ensembl; ENST00000390609; ENSP00000375018; ENSG00000211949. DR Ensembl; ENST00000632630; ENSP00000487761; ENSG00000281962. DR UCSC; uc059gga.1; human. DR DisGeNET; 28442; -. DR EuPathDB; HostDB:ENSG00000211949.3; -. DR GeneCards; IGHV3-23; -. DR HGNC; HGNC:5588; IGHV3-23. DR neXtProt; NX_P01764; -. DR OpenTargets; ENSG00000211949; -. DR GeneTree; ENSGT00940000154310; -. DR HOVERGEN; HBG018013; -. DR InParanoid; P01764; -. DR OMA; EWINSAV; -. DR Reactome; R-HSA-166663; Initial triggering of complement. DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-2029481; FCGR activation. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis. DR Reactome; R-HSA-2168880; Scavenging of heme from plasma. DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling. DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization. DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR EvolutionaryTrace; P01764; -. DR PRO; PR:P01764; -. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000211949; Expressed in 118 organ(s), highest expression level in lymph node. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0003823; F:antigen binding; IBA:GO_Central. DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006956; P:complement activation; TAS:Reactome. DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central. DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central. DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central. DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR GO; GO:0030449; P:regulation of complement activation; TAS:Reactome. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07686; V-set; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Immunity; KW Immunoglobulin domain; Immunoglobulin V region; Membrane; KW Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:409716, FT ECO:0000269|PubMed:4139708, FT ECO:0000269|PubMed:4522793}. FT CHAIN 20 117 Immunoglobulin heavy variable 3-23. FT {ECO:0000269|PubMed:409716, FT ECO:0000269|PubMed:4139708, FT ECO:0000269|PubMed:4522793}. FT /FTId=PRO_0000015249. FT DOMAIN 20 >117 Ig-like. FT DISULFID 41 115 {ECO:0000244|PDB:1OHQ, FT ECO:0000244|PDB:3BN9, FT ECO:0000244|PDB:3UPC, FT ECO:0000244|PDB:3ZHD, FT ECO:0000244|PDB:3ZHK, FT ECO:0000244|PDB:3ZHL, FT ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:15033359, FT ECO:0000269|PubMed:24892548}. FT VARIANT 24 24 V -> L (in IMGT allele IGHV3-23*02). FT {ECO:0000269|PubMed:6450418}. FT /FTId=VAR_073326. FT VARIANT 80 80 A -> G (in IMGT allele IGHV3-23*02). FT {ECO:0000269|PubMed:6450418}. FT /FTId=VAR_073327. FT CONFLICT 20 20 E -> A (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 29 29 G -> A (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 37 37 L -> G (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 47 54 TFSSYAMS -> SFSTDAMY (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 50 53 SYAM -> RVLS (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 SYA -> TYV (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 50 S -> A (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 50 S -> T (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 54 YAMS -> TSAVY (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 54 YAMS -> TTSRF (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 51 Y -> S (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 84 SAISGSGGSTYYADSVK -> AWKYQEASNSHFADTVN FT (in Ref. 3; AA sequence). {ECO:0000305}. FT CONFLICT 68 84 SAISGSGGSTYYADSVK -> GWRYEGSSLTHYAVSVQ FT (in Ref. 3; AA sequence). {ECO:0000305}. FT CONFLICT 68 78 SAISGSGGSTY -> AWKYENGNDKH (in Ref. 4; AA FT sequence). {ECO:0000305}. FT CONFLICT 68 78 SAISGSGGSTY -> EFRVQGSAISH (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 68 68 S -> G (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 69 84 AISGSGGSTYYADSVK -> GRLNASSNLHFAVSAQ (in FT Ref. 3; AA sequence). {ECO:0000305}. FT CONFLICT 71 78 SGSGGSTY -> ZGLSVSZS (in Ref. 5; AA FT sequence). {ECO:0000305}. FT CONFLICT 84 85 KG -> QA (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 84 84 K -> N (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 92 93 DN -> ND (in Ref. 4; AA sequence and 3; FT AA sequence). {ECO:0000305}. FT CONFLICT 93 101 NSKNTLYLQ -> DSKNT (in Ref. 5; AA FT sequence). {ECO:0000305}. FT CONFLICT 101 101 Q -> L (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 103 107 NSLRA -> LSLEP (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 103 106 NSLR -> LSLQ (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 104 105 SL -> TG (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 104 104 S -> G (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 104 104 S -> R (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 106 106 R -> E (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 106 106 R -> Q (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 109 112 DTAV -> VSAI (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 112 V -> L (in Ref. 3; AA sequence and 4; AA FT sequence). {ECO:0000305}. FT CONFLICT 117 117 K -> R (in Ref. 4; AA sequence and 3; AA FT sequence). {ECO:0000305}. FT NON_TER 117 117 FT STRAND 22 26 {ECO:0000244|PDB:3ZHD}. FT STRAND 29 31 {ECO:0000244|PDB:3ZHD}. FT STRAND 37 46 {ECO:0000244|PDB:3ZHD}. FT HELIX 48 50 {ECO:0000244|PDB:3ZHD}. FT STRAND 53 58 {ECO:0000244|PDB:3ZHD}. FT TURN 60 62 {ECO:0000244|PDB:1OHQ}. FT STRAND 65 70 {ECO:0000244|PDB:3ZHD}. FT STRAND 74 79 {ECO:0000244|PDB:3ZHD}. FT TURN 81 86 {ECO:0000244|PDB:3ZHD}. FT STRAND 87 92 {ECO:0000244|PDB:3ZHD}. FT TURN 93 96 {ECO:0000244|PDB:3ZHD}. FT STRAND 97 102 {ECO:0000244|PDB:3ZHD}. FT HELIX 107 109 {ECO:0000244|PDB:3ZHD}. FT STRAND 111 117 {ECO:0000244|PDB:3ZHD}. SQ SEQUENCE 117 AA; 12582 MW; E96D8794FA22F0B5 CRC64; MEFGLSWLFL VAILKGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS YAMSWVRQAP GKGLEWVSAI SGSGGSTYYA DSVKGRFTIS RDNSKNTLYL QMNSLRAEDT AVYYCAK //