##gff-version 3 P09619 UniProtKB Signal peptide 1 32 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15340161;Dbxref=PMID:15340161 P09619 UniProtKB Chain 33 1106 . . . ID=PRO_0000016757;Note=Platelet-derived growth factor receptor beta P09619 UniProtKB Topological domain 33 532 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Transmembrane 533 553 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Topological domain 554 1106 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Domain 33 120 . . . Note=Ig-like C2-type 1 P09619 UniProtKB Domain 129 210 . . . Note=Ig-like C2-type 2 P09619 UniProtKB Domain 214 309 . . . Note=Ig-like C2-type 3 P09619 UniProtKB Domain 331 403 . . . Note=Ig-like C2-type 4 P09619 UniProtKB Domain 416 524 . . . Note=Ig-like C2-type 5 P09619 UniProtKB Domain 600 962 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P09619 UniProtKB Region 1019 1106 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09619 UniProtKB Compositional bias 1041 1063 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09619 UniProtKB Compositional bias 1066 1080 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09619 UniProtKB Active site 826 826 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 P09619 UniProtKB Binding site 606 614 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P09619 UniProtKB Binding site 634 634 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P09619 UniProtKB Site 527 528 . . . Note=Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein P09619 UniProtKB Site 527 528 . . . Note=Breakpoint for translocation to form TRIP11-PDGFRB P09619 UniProtKB Site 558 559 . . . Note=Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein P09619 UniProtKB Modified residue 562 562 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821867;Dbxref=PMID:10821867 P09619 UniProtKB Modified residue 579 579 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14966296,ECO:0000269|PubMed:15902258,ECO:0000269|PubMed:7685273;Dbxref=PMID:14966296,PMID:15902258,PMID:7685273 P09619 UniProtKB Modified residue 581 581 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15902258,ECO:0000269|PubMed:7685273;Dbxref=PMID:15902258,PMID:7685273 P09619 UniProtKB Modified residue 686 686 . . . Note=Phosphotyrosine%3B by ABL1 and ABL2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05622 P09619 UniProtKB Modified residue 716 716 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15902258;Dbxref=PMID:15902258 P09619 UniProtKB Modified residue 740 740 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:15902258;Dbxref=PMID:1314164,PMID:15902258 P09619 UniProtKB Modified residue 751 751 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821867,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:14966296,ECO:0000269|PubMed:1709159,ECO:0000269|PubMed:2550144;Dbxref=PMID:10821867,PMID:1314164,PMID:14966296,PMID:1709159,PMID:2550144 P09619 UniProtKB Modified residue 763 763 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821867;Dbxref=PMID:10821867 P09619 UniProtKB Modified residue 771 771 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821867,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:14966296,ECO:0000269|PubMed:15902258;Dbxref=PMID:10821867,PMID:1314164,PMID:14966296,PMID:15902258 P09619 UniProtKB Modified residue 775 775 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821867;Dbxref=PMID:10821867 P09619 UniProtKB Modified residue 778 778 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821867;Dbxref=PMID:10821867 P09619 UniProtKB Modified residue 857 857 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821867,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:15902258,ECO:0000269|PubMed:1709159,ECO:0000269|PubMed:2550144;Dbxref=PMID:10821867,PMID:1314164,PMID:15902258,PMID:1709159,PMID:2550144 P09619 UniProtKB Modified residue 934 934 . . . Note=Phosphotyrosine%3B by ABL1 and ABL2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05622 P09619 UniProtKB Modified residue 970 970 . . . Note=Phosphotyrosine%3B by ABL1 and ABL2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05622 P09619 UniProtKB Modified residue 1009 1009 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821867,ECO:0000269|PubMed:1396585,ECO:0000269|PubMed:15902258;Dbxref=PMID:10821867,PMID:1396585,PMID:15902258 P09619 UniProtKB Modified residue 1021 1021 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821867,ECO:0000269|PubMed:1396585,ECO:0000269|PubMed:14966296,ECO:0000269|PubMed:15902258;Dbxref=PMID:10821867,PMID:1396585,PMID:14966296,PMID:15902258 P09619 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 230 230 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 292 292 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 307 307 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Glycosylation 354 354 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Glycosylation 479 479 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09619 UniProtKB Disulfide bond 54 100 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Disulfide bond 149 190 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Disulfide bond 235 291 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20534510;Dbxref=PMID:20534510 P09619 UniProtKB Disulfide bond 436 508 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P09619 UniProtKB Alternative sequence 311 336 . . . ID=VSP_056008;Note=In isoform 2. VESGYVRLLGEVGTLQFAELHRSRTL->RAATCGSWERWAHYNLLSCIGAGHCR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:18593464;Dbxref=PMID:18593464 P09619 UniProtKB Alternative sequence 337 1106 . . . ID=VSP_056009;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:18593464;Dbxref=PMID:18593464 P09619 UniProtKB Natural variant 29 29 . . . ID=VAR_034377;Note=I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs17110944,PMID:17344846 P09619 UniProtKB Natural variant 180 180 . . . ID=VAR_035125;Note=S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17853027,PMID:15489334 P09619 UniProtKB Natural variant 282 282 . . . ID=VAR_042027;Note=E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34586048,PMID:17344846 P09619 UniProtKB Natural variant 345 345 . . . ID=VAR_049717;Note=P->S;Dbxref=dbSNP:rs2229558 P09619 UniProtKB Natural variant 485 485 . . . ID=VAR_042028;Note=E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs41287110,PMID:17344846 P09619 UniProtKB Natural variant 561 561 . . . ID=VAR_069925;Note=In IMF1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23731537;Dbxref=dbSNP:rs367543286,PMID:23731537 P09619 UniProtKB Natural variant 584 584 . . . ID=VAR_075865;Note=In KOGS. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25454926;Dbxref=dbSNP:rs863224946,PMID:25454926 P09619 UniProtKB Natural variant 589 589 . . . ID=VAR_042029;Note=In a gastric adenocarcinoma sample%3B somatic mutation. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P09619 UniProtKB Natural variant 658 658 . . . ID=VAR_069320;Note=In IBGC4%3B no effect on protein abundance%3B loss of PDGF beta receptor activity. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23255827,ECO:0000269|PubMed:24065723,ECO:0000269|PubMed:26599395;Dbxref=dbSNP:rs397509381,PMID:23255827,PMID:24065723,PMID:26599395 P09619 UniProtKB Natural variant 660 660 . . . ID=VAR_069926;Note=In IMF1. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23731542;Dbxref=dbSNP:rs144050370,PMID:23731542 P09619 UniProtKB Natural variant 665 665 . . . ID=VAR_075866;Note=In PENTT%3B gain of function in protein tyrosine kinase activity%3B shows ligand-independent constitutive signaling. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26279204;Dbxref=dbSNP:rs1554108211,PMID:26279204 P09619 UniProtKB Natural variant 718 718 . . . ID=VAR_042030;Note=N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35322465,PMID:17344846 P09619 UniProtKB Natural variant 882 882 . . . ID=VAR_042031;Note=In a breast infiltrating ductal carcinoma sample%3B somatic mutation. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P09619 UniProtKB Natural variant 987 987 . . . ID=VAR_069321;Note=In IBGC4%3B decreased protein abundance%3B no effect on receptor activity%3B decreased PDGF signaling pathway. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23255827,ECO:0000269|PubMed:24065723,ECO:0000269|PubMed:26599395;Dbxref=dbSNP:rs397509382,PMID:23255827,PMID:24065723,PMID:26599395 P09619 UniProtKB Natural variant 1071 1071 . . . ID=VAR_075395;Note=In IBGC4%3B no effect on protein abundance%3B no effect on receptor activity%3B decreased PDGF signaling pathway. E->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24065723,ECO:0000269|PubMed:26599395;Dbxref=PMID:24065723,PMID:26599395 P09619 UniProtKB Mutagenesis 579 579 . . . Note=Loss of kinase activity%3B when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:7685273;Dbxref=PMID:10454568,PMID:7685273 P09619 UniProtKB Mutagenesis 581 581 . . . Note=Loss of kinase activity%3B when associated with F-579. No effect on interaction with GRB10. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:7685273;Dbxref=PMID:10454568,PMID:7685273 P09619 UniProtKB Mutagenesis 634 634 . . . Note=Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:1846866,ECO:0000269|PubMed:20494825;Dbxref=PMID:1314164,PMID:1846866,PMID:20494825 P09619 UniProtKB Mutagenesis 716 716 . . . Note=No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1314164;Dbxref=PMID:10454568,PMID:1314164 P09619 UniProtKB Mutagenesis 740 740 . . . Note=Strongly reduces up-regulation of cell proliferation%3B when associated with F-751. Strongly decreases phosphatidylinositol 3-kinase activity. No effect on interaction with GRB10 and RASA1. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:1375321,ECO:0000269|PubMed:21679854;Dbxref=PMID:10454568,PMID:1314164,PMID:1375321,PMID:21679854 P09619 UniProtKB Mutagenesis 751 751 . . . Note=Strongly reduces up-regulation of cell proliferation%3B when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction with NCK1%2C and slightly reduces interaction with RASA1. No effect on interaction with GRB10. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:1375321,ECO:0000269|PubMed:1653029,ECO:0000269|PubMed:21679854,ECO:0000269|PubMed:7692233;Dbxref=PMID:10454568,PMID:1314164,PMID:1375321,PMID:1653029,PMID:21679854,PMID:7692233 P09619 UniProtKB Mutagenesis 763 763 . . . Note=No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1314164;Dbxref=PMID:1314164 P09619 UniProtKB Mutagenesis 771 771 . . . Note=Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:1375321;Dbxref=PMID:10454568,PMID:1314164,PMID:1375321 P09619 UniProtKB Mutagenesis 775 775 . . . Note=No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1314164;Dbxref=PMID:1314164 P09619 UniProtKB Mutagenesis 778 778 . . . Note=Strongly reduces expression levels. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1314164;Dbxref=PMID:1314164 P09619 UniProtKB Mutagenesis 857 857 . . . Note=Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1314164,ECO:0000269|PubMed:1653029,ECO:0000269|PubMed:20494825;Dbxref=PMID:10454568,PMID:1314164,PMID:1653029,PMID:20494825 P09619 UniProtKB Mutagenesis 1009 1009 . . . Note=No effect on interaction with GRB10. Abolishes interaction with PLCG1%3B when associated with F-1021. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1396585,ECO:0000269|PubMed:7691811;Dbxref=PMID:10454568,PMID:1396585,PMID:7691811 P09619 UniProtKB Mutagenesis 1021 1021 . . . Note=Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1%3B when associated with F-1009. No effect on interaction with GRB10. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10454568,ECO:0000269|PubMed:1396585,ECO:0000269|PubMed:17620338,ECO:0000269|PubMed:21679854;Dbxref=PMID:10454568,PMID:1396585,PMID:17620338,PMID:21679854 P09619 UniProtKB Sequence conflict 241 241 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09619 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 50 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 70 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 81 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 96 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 114 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Helix 132 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 158 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 178 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 185 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 204 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 217 221 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 231 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 241 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 252 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 261 265 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Turn 267 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 271 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 287 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Turn 296 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Beta strand 300 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MJG P09619 UniProtKB Helix 530 556 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L6W