ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P27487


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DPP4_HUMAN
Primary accession number P27487
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on February 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 104)
Name and origin of the protein
Protein name Dipeptidyl peptidase 4
Synonyms EC 3.4.14.5
Dipeptidyl peptidase IV
DPP IV
T-cell activation antigen CD26
TP103
Adenosine deaminase complexing protein 2
ADABP
CD26 antigen
Contains Dipeptidyl peptidase 4 membrane form
     (Dipeptidyl peptidase IV membrane form)
Dipeptidyl peptidase 4 soluble form
     (Dipeptidyl peptidase IV soluble form)
Gene name
Name: DPP4
Synonyms: ADCP2, CD26
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/0167-4781(92)90036-Y; PubMed=1352704 [NCBI, ExPASy, EBI, Israel, Japan]
Misumi Y., Hayashi Y., Arakawa F., Ikehara Y.;
"Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface.";
Biochim. Biophys. Acta 1131:333-336(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1007/BF01246674; PubMed=7927537 [NCBI, ExPASy, EBI, Israel, Japan]
Abbott C.A., Baker E., Sutherland G.R., McCaughan G.W.;
"Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene.";
Immunogenetics 40:331-338(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood;
PubMed=1352530 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T., Camerini D., Seed B., Torimoto Y., Dang N.H., Kameoka J., Dahlberg H.N., Schlossman S.F., Morimoto C.;
"Cloning and functional expression of the T cell activation antigen CD26.";
J. Immunol. 149:481-486(1992).
[4]
ERRATUM.
PubMed=8094732 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T.;
J. Immunol. 150:2090-2090(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-551.
TISSUE=Colon;
PubMed=1347043 [NCBI, ExPASy, EBI, Israel, Japan]
Darmoul D., Lacasa M., Baricault L., Marguet D., Sapin C., Trotot P., Barbat A.;
"Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like colon cancer cell lines HT-29 and Caco-2. Cloning of the complete human coding sequence and changes of dipeptidyl peptidase IV mRNA levels during cell differentiation.";
J. Biol. Chem. 267:4824-4833(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 545-766.
TISSUE=Colon;
PubMed=1977364 [NCBI, ExPASy, EBI, Israel, Japan]
Darmoul D., Lacasa M., Chantret I., Swallow D., Trugnan G.;
"Isolation of a cDNA probe for the human intestinal dipeptidylpeptidase IV and assignment of the gene locus DPP4 to chromosome 2.";
Ann. Hum. Genet. 54:191-197(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
PubMed=7487939 [NCBI, ExPASy, EBI, Israel, Japan]
Boehm S.K., Gum J.R. Jr., Erickson R.H., Hicks J.W., Kim Y.S.;
"Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter.";
Biochem. J. 311:835-843(1995).
[9]
PROTEIN SEQUENCE OF 1-22, AND TISSUE SPECIFICITY.
PubMed=1677636 [NCBI, ExPASy, EBI, Israel, Japan]
Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.;
"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon.";
Gastroenterology 101:618-625(1991).
[10]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Kidney;
DOI=10.1084/jem.177.4.1135; PubMed=8096237 [NCBI, ExPASy, EBI, Israel, Japan]
Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P., Houghton A.N.;
"A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase.";
J. Exp. Med. 177:1135-1143(1993).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH INHIBITOR, AND HOMODIMERIZATION.
DOI=10.1107/S0907444903010059; PubMed=12832764 [NCBI, ExPASy, EBI, Israel, Japan]
Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R., Dale G.E.;
"High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine.";
Acta Crystallogr. D 59:1206-1212(2003).
[13]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, AND DISULFIDE BONDS.
DOI=10.1016/S0006-291X(03)00258-4; PubMed=12646248 [NCBI, ExPASy, EBI, Israel, Japan]
Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H., Sugiyama S., Inaka K., Yamamoto A., Shimizu R.;
"The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold.";
Biochem. Biophys. Res. Commun. 302:849-854(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND ASN-520, AND DISULFIDE BONDS.
DOI=10.1038/nsb882; PubMed=12483204 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.;
"Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.";
Nat. Struct. Biol. 10:19-25(2003).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, AND DISULFIDE BONDS.
DOI=10.1016/S0969-2126(03)00160-6; PubMed=12906826 [NCBI, ExPASy, EBI, Israel, Japan]
Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.;
"Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV.";
Structure 11:947-959(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U13735; AAB60646.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13710; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13711; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13712; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13713; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13714; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13715; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13716; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13717; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13718; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13719; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13720; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13721; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13722; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13723; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13724; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13725; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13726; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13727; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13728; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13729; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13730; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13731; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13732; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13733; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13734; AAB60646.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M74777; AAA51943.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013329; AAH13329.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065265; AAH65265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M80536; AAA52308.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60708; CAA43118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79876; AAB35614.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S24313; CDHU26.
RefSeq NP_001926.2; -.
UniGene Hs.368912
3D structure databases
PDB
1J2E; X-ray; 2.60 A; A/B=33-766.[ExPASy / RCSB / EBI]
1N1M; X-ray; 2.50 A; A/B=39-766.[ExPASy / RCSB / EBI]
1NU6; X-ray; 2.10 A; A/B=39-766.[ExPASy / RCSB / EBI]
1NU8; X-ray; 2.50 A; A/B=39-766.[ExPASy / RCSB / EBI]
1PFQ; X-ray; 1.90 A; A/B=36-766.[ExPASy / RCSB / EBI]
1R9M; X-ray; 2.10 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
1R9N; X-ray; 2.30 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
1RWQ; X-ray; 2.20 A; A/B=39-766.[ExPASy / RCSB / EBI]
1TK3; X-ray; 2.00 A; A/B=39-766.[ExPASy / RCSB / EBI]
1TKR; X-ray; 2.70 A; A/B=39-766.[ExPASy / RCSB / EBI]
1U8E; X-ray; 2.20 A; A/B=39-766.[ExPASy / RCSB / EBI]
1W1I; X-ray; 3.03 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
1WCY; X-ray; 2.20 A; A/B=33-766.[ExPASy / RCSB / EBI]
1X70; X-ray; 2.10 A; A/B=40-766.[ExPASy / RCSB / EBI]
2AJL; X-ray; 2.50 A; I/J=39-766.[ExPASy / RCSB / EBI]
2BGN; X-ray; 3.15 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2BGR; X-ray; 2.00 A; A/B=29-766.[ExPASy / RCSB / EBI]
2BUB; X-ray; 2.66 A; A/B=39-766.[ExPASy / RCSB / EBI]
2FJP; X-ray; 2.40 A; A/B=39-766.[ExPASy / RCSB / EBI]
2G5P; X-ray; 2.40 A; A/B=39-764.[ExPASy / RCSB / EBI]
2G5T; X-ray; 2.30 A; A/B=39-764.[ExPASy / RCSB / EBI]
2G63; X-ray; 2.00 A; A/B/C/D=39-764.[ExPASy / RCSB / EBI]
2HHA; X-ray; 2.35 A; A/B=39-766.[ExPASy / RCSB / EBI]
2I03; X-ray; 2.40 A; A/B/C/D=39-764.[ExPASy / RCSB / EBI]
2I78; X-ray; 2.50 A; A/B/C/D=39-764.[ExPASy / RCSB / EBI]
2IIT; X-ray; 2.35 A; A/B=39-766.[ExPASy / RCSB / EBI]
2IIV; X-ray; 2.15 A; A/B=39-766.[ExPASy / RCSB / EBI]
2JID; X-ray; 2.80 A; A/B=31-766.[ExPASy / RCSB / EBI]
2OAG; X-ray; 2.30 A; A/B/C/D=39-764.[ExPASy / RCSB / EBI]
2OGZ; X-ray; 2.10 A; A/B=39-766.[ExPASy / RCSB / EBI]
2OLE; X-ray; 2.40 A; A/B=39-766.[ExPASy / RCSB / EBI]
2ONC; X-ray; 2.55 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2OPH; X-ray; 2.40 A; A/B=39-766.[ExPASy / RCSB / EBI]
2OQI; X-ray; 2.80 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2OQV; X-ray; 2.80 A; A/B=39-764.[ExPASy / RCSB / EBI]
2P8S; X-ray; 2.20 A; A/B=39-766.[ExPASy / RCSB / EBI]
2QKY; X-ray; 3.10 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2QOE; X-ray; 2.30 A; A/B=39-766.[ExPASy / RCSB / EBI]
2QT9; X-ray; 2.10 A; A/B=1-766.[ExPASy / RCSB / EBI]
2QTB; X-ray; 2.25 A; A/B=1-766.[ExPASy / RCSB / EBI]
2RGU; X-ray; 2.60 A; A/B=39-766.[ExPASy / RCSB / EBI]
2RIP; X-ray; 2.90 A; A=38-766.[ExPASy / RCSB / EBI]
3BJM; X-ray; 2.35 A; A/B=39-766.[ExPASy / RCSB / EBI]
3C43; X-ray; 2.30 A; A/B=39-766.[ExPASy / RCSB / EBI]
3C45; X-ray; 2.05 A; A/B=39-766.[ExPASy / RCSB / EBI]
3D4L; X-ray; 2.00 A; A/B=39-766.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1J2E; -.
1N1M; -.
1NU6; -.
1NU8; -.
1PFQ; -.
1R9M; -.
1R9N; -.
1RWQ; -.
1TK3; -.
1TKR; -.
1U8E; -.
1W1I; -.
1WCY; -.
1X70; -.
2AJL; -.
2BGN; -.
2BGR; -.
2BUB; -.
2FJP; -.
2G5P; -.
2G5T; -.
2G63; -.
2HHA; -.
2I03; -.
2I78; -.
2IIT; -.
2IIV; -.
2JID; -.
2OAG; -.
2OGZ; -.
2OLE; -.
2ONC; -.
2OPH; -.
2OQI; -.
2OQV; -.
2P8S; -.
2QKY; -.
2QOE; -.
2QT9; -.
2QTB; -.
2RGU; -.
2RIP; -.
3BJM; -.
3C43; -.
3C45; -.
3D4L; -.
ModBase P27487.
Protein-protein interaction databases
DIP DIP:351N; -.
Protein family/group databases
MEROPS S09.003; -.
PTM databases
PhosphoSite P27487; -.
Organism-specific databases
H-InvDB HIX0002546; -.
HGNC HGNC:3009; DPP4.
GenAtlas DPP4.
MIM 102720; gene. [NCBI / EBI]
PharmGKB PA27467; -.
GeneCards P27487.
Gene expression databases
ArrayExpress P27487; -.
CleanEx HS_DPP4; -.
GermOnline ENSG00000197635; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004177; Molecular function: aminopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008239; Molecular function: dipeptidyl-peptidase activity (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0033632; Biological process: regulation of cell-cell adhesion mediated by integrin (inferred from direct assay from UniProtKB).
GO:0001666; Biological process: response to hypoxia (inferred from direct assay from UniProtKB).
GO:0042110; Biological process: T cell activation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002469; Peptidase_S9B.
Graphical view of domain structure.
Pfam PF00930; DPPIV_N; 1.
PF00326; Peptidase_S9; 1.
Pfam graphical view of domain structure.
PROSITE PS00708; PRO_ENDOPEP_SER; 1.
BLOCKS P27487.
ProtoNet P27487.
Proteomic databases
PeptideAtlas P27487; -.
Genome annotation databases
Ensembl ENSG00000197635; Homo sapiens. [Contig view]
GeneID 1803; -.
KEGG hsa:1803; -.
Phylogenomic databases
HOGENOM P27487; -.
HOVERGEN P27487; -.
Other
DrugBank DB01261; Sitagliptin.
LinkHub P27487; -.
NextBio 7345; -.
SOURCE DPP4; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminopeptidase; Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Protease; Secreted; Serine protease; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   766  766     Dipeptidyl peptidase 4 membrane form. PRO_0000027213
CHAIN   39   766  728     Dipeptidyl peptidase 4 soluble form. PRO_0000027214
TOPO_DOM   1     6  6     Cytoplasmic (Potential). 
TRANSMEM   7    28  22     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   29   766  738     Extracellular (Potential). 
ACT_SITE   630   630        Charge relay system (By similarity). 
ACT_SITE   708   708        Charge relay system (By similarity). 
ACT_SITE   740   740        Charge relay system (By similarity). 
CARBOHYD   85    85        N-linked (GlcNAc...). 
CARBOHYD   92    92        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   150   150        N-linked (GlcNAc...). 
CARBOHYD   219   219        N-linked (GlcNAc...). 
CARBOHYD   229   229        N-linked (GlcNAc...). 
CARBOHYD   281   281        N-linked (GlcNAc...). 
CARBOHYD   321   321        N-linked (GlcNAc...). 
CARBOHYD   520   520        N-linked (GlcNAc...). 
CARBOHYD   685   685        N-linked (GlcNAc...). 
DISULFID   328   339         
DISULFID   385   394         
DISULFID   444   447         
DISULFID   454   472         
DISULFID   649   762         
CONFLICT   6     6        K -> R (in Ref. 6; AAA52308). 
CONFLICT   7     7        V -> I (in Ref. 1; CAA43118). 
CONFLICT   437   437        S -> I (in Ref. 1; CAA43118). 
CONFLICT   557   557        T -> I (in Ref. 7; AAA52308). 
CONFLICT   663   663        D -> E (in Ref. 7; AAA52308). 
HELIX   45    50  6      
STRAND   64    72  9      
STRAND   75    80  6      
TURN   81    83  3      
STRAND   86    90  5      
TURN   92    95  4      
HELIX   96    98  3      
STRAND   102   107  6      
STRAND   111   122  12      
STRAND   124   126  3      
STRAND   128   136  9      
TURN   137   140  4      
STRAND   154   157  4      
STRAND   159   162  4      
STRAND   164   168  5      
STRAND   171   177  7      
TURN   191   193  3      
STRAND   194   198  5      
HELIX   201   205  5      
STRAND   208   212  5      
STRAND   214   216  3      
STRAND   220   229  10      
STRAND   235   240  6      
STRAND   250   255  6      
STRAND   265   272  8      
STRAND   278   280  3      
STRAND   284   287  4      
HELIX   291   294  4      
STRAND   298   307  10      
STRAND   310   319  10      
STRAND   322   330  9      
TURN   332   334  3      
STRAND   337   339  3