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 P07237


[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 PDIA1_HUMAN
Primary accession number P07237
Secondary accession numbers P30037 P32079 Q15205 Q6LDE5
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on November 1, 1997 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 129)
Name and origin of the protein
Protein name Protein disulfide-isomerase [Precursor]
Synonyms PDI
EC 5.3.4.1
Prolyl 4-hydroxylase subunit beta
Cellular thyroid hormone-binding protein
p55
Gene name
Name: P4HB
Synonyms: ERBA2L, PDI, PDIA1, PO4DB
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].
PubMed=3034602 [NCBI, ExPASy, EBI, Israel, Japan]
Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L., Koivu J., Kivirikko K.I.;
"Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.";
EMBO J. 6:643-649(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3611107 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E., Merlino G.T., Pastan I.;
"The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum.";
J. Biol. Chem. 262:11221-11227(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=2846539 [NCBI, ExPASy, EBI, Israel, Japan]
Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T.;
"Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase.";
J. Biol. Chem. 263:16218-16224(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Lung, and Skin;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=1597478 [NCBI, ExPASy, EBI, Israel, Japan]
Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T.;
"Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements.";
J. Biol. Chem. 267:11513-11519(1992).
[6]
PROTEIN SEQUENCE OF 18-41.
TISSUE=Colon carcinoma;
DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[7]
PROTEIN SEQUENCE OF 18-30.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 18-29.
TISSUE=Liver;
Frutiger S., Hughes G.J.;
Submitted (FEB-1996) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 18-26.
PubMed=2079031 [NCBI, ExPASy, EBI, Israel, Japan]
Ward L.D., Hong J., Whitehead R.H., Simpson R.J.;
"Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis.";
Electrophoresis 11:883-891(1990).
[10]
PRELIMINARY PROTEIN SEQUENCE OF 19-28.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[11]
PROTEIN SEQUENCE OF 19-28.
PubMed=9399589 [NCBI, ExPASy, EBI, Israel, Japan]
Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease.";
J. Biochem. 122:834-842(1997).
[12]
PROTEIN SEQUENCE OF 286-300, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
DOI=10.1016/0167-4781(88)90080-2; PubMed=3342239 [NCBI, ExPASy, EBI, Israel, Japan]
Morris J.I., Varandani P.T.;
"Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase).";
Biochim. Biophys. Acta 949:169-180(1988).
[14]
PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
PubMed=1699755 [NCBI, ExPASy, EBI, Israel, Japan]
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes.";
Electrophoresis 11:528-536(1990).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.275.3.1920; PubMed=10636893 [NCBI, ExPASy, EBI, Israel, Japan]
Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P., Miquelis R.;
"Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes.";
J. Biol. Chem. 275:1920-1929(2000).
[16]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
DOI=10.1086/318823; PubMed=11181151 [NCBI, ExPASy, EBI, Israel, Japan]
Fenouillet E., Barbouche R., Courageot J., Miquelis R.;
"The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding.";
J. Infect. Dis. 183:744-752(2001).
[17]
FUNCTION.
DOI=10.1093/emboj/cdf685; PubMed=12485997 [NCBI, ExPASy, EBI, Israel, Japan]
Lumb R.A., Bulleid N.J.;
"Is protein disulfide isomerase a redox-dependent molecular chaperone?";
EMBO J. 21:6763-6770(2002).
[18]
INTERACTION WITH UBQLN1.
DOI=10.1074/jbc.M203412200; PubMed=12095988 [NCBI, ExPASy, EBI, Israel, Japan]
Ko H.S., Uehara T., Nomura Y.;
"Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death.";
J. Biol. Chem. 277:35386-35392(2002).
[19]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
DOI=10.1074/jbc.M204547200; PubMed=12218051 [NCBI, ExPASy, EBI, Israel, Japan]
Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J.;
"Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry.";
J. Biol. Chem. 277:50579-50588(2002).
[20]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
DOI=10.1074/jbc.M205467200; PubMed=12218052 [NCBI, ExPASy, EBI, Israel, Japan]
Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
"Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion.";
J. Biol. Chem. 278:3131-3136(2003).
[21]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr025562r; PubMed=12643545 [NCBI, ExPASy, EBI, Israel, Japan]
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[22]
REVIEW.
DOI=10.1016/j.bbapap.2004.02.017; PubMed=15158710 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson B., Gilbert H.F.;
"Protein disulfide isomerase.";
Biochim. Biophys. Acta 1699:35-44(2004).
[23]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
DOI=10.1182/blood-2003-05-1390; PubMed=14592831 [NCBI, ExPASy, EBI, Israel, Japan]
Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M., Weiss C.D., Broder C.C., Strebel K., Clouse K.A.;
"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry.";
Blood 103:1586-1594(2004).
[24]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
DOI=10.1124/mol.104.008276; PubMed=15644496 [NCBI, ExPASy, EBI, Israel, Japan]
Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.;
"Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env.";
Mol. Pharmacol. 67:1111-1118(2005).
[25]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[26]
STRUCTURE BY NMR OF 18-137.
PubMed=8580850 [NCBI, ExPASy, EBI, Israel, Japan]
Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E.;
"Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.";
Protein Sci. 4:2587-2593(1995).
[27]
STRUCTURE BY NMR OF 18-137, AND DISULFIDE BOND.
DOI=10.1021/bi960335m; PubMed=8672469 [NCBI, ExPASy, EBI, Israel, Japan]
Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E.;
"Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.";
Biochemistry 35:7684-7691(1996).
[28]
STRUCTURE BY NMR OF 136-245.
DOI=10.1023/A:1008341820489; PubMed=10383197 [NCBI, ExPASy, EBI, Israel, Japan]
Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M., Darby N.J.;
"The structure in solution of the B domain of protein disulfide isomerase.";
J. Biomol. NMR 13:357-368(1999).
[29]
STRUCTURE BY NMR OF 368-477.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase.";
Submitted (NOV-2005) to the PDB data bank.
Comments
  • FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.
  • CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in proteins.
  • SUBUNIT: Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity (By similarity). Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex.
  • INTERACTION:
    O95400:CD2BP2; NbExp=1; IntAct=EBI-395883, EBI-768015;
    Q13617:CUL2; NbExp=1; IntAct=EBI-395883, EBI-456179;
    P78545:ELF3; NbExp=1; IntAct=EBI-395883, EBI-1057285;
    Q9UHX1:PUF60; NbExp=1; IntAct=EBI-395883, EBI-1053259;
    Q03518:TAP1; NbExp=3; IntAct=EBI-395883, EBI-780739;
    Q15654:TRIP6; NbExp=1; IntAct=EBI-395883, EBI-742327;
  • SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein (Potential). Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
  • MISCELLANEOUS: Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.
  • SIMILARITY: Belongs to the protein disulfide isomerase family.
  • SIMILARITY: Contains 2 thioredoxin domains.
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
X05130; CAA28775.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02783; AAA61169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22806; AAC13652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22803; AAC13652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22804; AAC13652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22805; AAC13652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010859; AAH10859.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029617; AAH29617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071892; AAH71892.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S37207; AAB22262.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07077; CAA30112.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31913; ISHUSS.
RefSeq NP_000909.2; -.
UniGene Hs.464336
3D structure databases
PDB
1BJX; NMR; -; A=136-245.[ExPASy / RCSB / EBI]
1MEK; NMR; -; A=18-137.[ExPASy / RCSB / EBI]
1X5C; NMR; -; A=368-477.[ExPASy / RCSB / EBI]
2BJX; NMR; -; A=136-245.[ExPASy / RCSB / EBI]
2K18; NMR; -; A=135-357.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BJX; -.
1MEK; -.
1X5C; -.
2BJX; -.
2K18; -.
ModBase P07237.
Protein-protein interaction databases
IntAct P07237; 20.
PTM databases
PhosphoSite P07237; -.
Enzyme and pathway databases
Reactome REACT_602; Lipid and lipoprotein metabolism.
2D gel databases
SWISS-2DPAGE P07237; -.
Aarhus/Ghent-2DPAGE 8412; IEF.
Cornea-2DPAGE P07237; -.
DOSAC-COBS-2DPAGE P07237; -.
OGP P07237; -.
REPRODUCTION-2DPAGE IPI00010796; -.
P07237; -.
Siena-2DPAGE P07237; -.
Organism-specific databases
GeneCards GC17M077394; -.
H-InvDB HIX0014256; -.
HIX0048655; -.
HGNC HGNC:8548; P4HB.
GenAtlas P4HB.
HPA CAB012463; -.
MIM 176790; gene. [NCBI / EBI]
PharmGKB PA32876; -.
GeneCards P07237.
Gene expression databases
ArrayExpress P07237; -.
CleanEx HS_P4HB; -.
GermOnline ENSG00000185624; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005783; Cellular component: endoplasmic reticulum (traceable author statement from ProtInc).
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005793; Cellular component: ER-Golgi intermediate compartment (inferred from direct assay from UniProtKB).
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004656; Molecular function: procollagen-proline 4-dioxygenase activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003756; Molecular function: protein disulfide isomerase activity (traceable author statement from ProtInc).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0018401; Biological process: peptidyl-proline hydroxylation to 4-hydroxy-L-proline (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR005788; Disulph_isom.
IPR005792; Disulphide_isom.
IPR000886; ER_targeting_sequence.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 2.
Pfam PF00085; Thioredoxin; 2.
Pfam graphical view of domain structure.
PRINTS PR00421; THIOREDOXIN.
TIGRFAMs TIGR01130; ER_PDI_fam; 1.
TIGR01126; pdi_dom; 2.
PROSITE PS00014; ER_TARGET; 1.
PS00194; THIOREDOXIN_1; 2.
PS51352; THIOREDOXIN_2; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P07237; -.
Proteomics databases
PRIDE P07237; -.
Genome annotation databases
Ensembl ENSG00000185624; Homo sapiens. [Contig view]
GeneID 5034; -.
KEGG hsa:5034; -.
NMPDR fig|9606.3.peg.14582; -.
Phylogenomic databases
HOGENOM P07237; -.
HOVERGEN P07237; -.
Other
LinkHub P07237; -.
NextBio 19398; -.
SOURCE P4HB; Homo sapiens.
ProtoNet P07237.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Chaperone; Direct protein sequencing; Endoplasmic reticulum; Isomerase; Membrane; Redox-active center; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17      
CHAIN   18   508  491     Protein disulfide-isomerase. PRO_0000034195
DOMAIN   18   134  117     Thioredoxin 1. 
DOMAIN   349   475  127     Thioredoxin 2. 
MOTIF   505   508  4     Prevents secretion from ER. 
ACT_SITE   53    53        Nucleophile. 
ACT_SITE   56    56        Nucleophile. 
ACT_SITE   397   397        Nucleophile (By similarity). 
ACT_SITE   400   400        Nucleophile (By similarity). 
SITE   54    54  1     Contributes to redox potential value. 
SITE   55    55  1     Contributes to redox potential value. 
SITE   120   120  1     Lowers pKa of C-terminal Cys of first active site. 
SITE   398   398  1     Contributes to redox potential value (By similarity). 
SITE   399   399  1     Contributes to redox potential value (By similarity). 
SITE   461   461  1     Lowers pKa of C-terminal Cys of second active site (By similarity). 
DISULFID   53    56        Redox-active. 
DISULFID   397   400        Redox-active (By similarity). 
CONFLICT   10    11        AV -> PW (in Ref. 1; CAA28775). 
CONFLICT   21    21        E -> D (in Ref. 11; AA sequence). 
CONFLICT   24    24        D -> V (in Ref. 11; AA sequence). 
CONFLICT   44    45        LL -> PP (in Ref. 1; CAA28775). 
CONFLICT   49    49        Y -> H (in Ref. 1; CAA28775). 
CONFLICT   141   141        P -> R (in Ref. 2; AAA61169). 
CONFLICT   360   362        LPE -> RAG (in Ref. 2; AAA61169). 
CONFLICT   372   372        L -> P (in Ref. 2; AAA61169). 
CONFLICT   439   439        S -> G (in Ref. 1; CAA28775). 
CONFLICT   444   444        K -> G (in Ref. 1; CAA28775). 
CONFLICT   460   460        E -> Q (in Ref. 13; CAA30112). 
CONFLICT   481   481        D -> V (in Ref. 1; CAA28775). 
STRAND   26    28  3      
TURN   31    33  3      
HELIX   34    40  7      
STRAND   42    49  8      
HELIX   60    68  9      
TURN   69    73  5      
STRAND   80    83  4      
TURN   84    86  3      
HELIX   91    94  4      
STRAND   98   108  11      
STRAND   110   112  3      
HELIX   122   130  9      
STRAND   137   139  3      
HELIX   143   152  10      
STRAND   153   160  8      
TURN   162   165  4      
HELIX   167   178  12      
STRAND   180   182  3      
STRAND   184   187  4     <