Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
Member of |
Entry ID | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|
26791 | Chemical Shifts: 1 set Coupling Constants: 2 sets Heteronuclear NOE Values: 4 sets T1 Relaxation Values: 4 sets T2 Relaxation Values: 4 sets |
Backbone 1H, 13C, and 15 N Chemical Shift Assignment for human Langerin CRD | An intra-domain allosteric network modulates the Ca2+ affinity in C-type lectin receptor Langerin | Bettina G Keller, Christoph Rademacher, Elena Shanina, Jonas Hanske, Marcel Jurk, Martin Ballaschk, Monika Beerbaum, Peter Schmieder, Stevan Aleksic |
25714 | Chemical Shifts: 2 sets |
Chemical shifts of the HLA-B2705 heavy chain in complex with the peptide pVIPR | Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Martin Ballaschk, Peter Schmieder |
25715 | Chemical Shifts: 2 sets |
Chemical shifts of the HLA-B2709 heavy chain in complex with the peptide TIS | Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Martin Ballaschk, Peter Schmieder |
25711 | Chemical Shifts: 2 sets |
Chemical shifts of the HLA-B2705 heavy chain in complex with the peptide TIS | Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Martin Ballaschk, Peter Schmieder |
25713 | Chemical Shifts: 2 sets |
Chemical shifts of the HLA-B2709 heavy chain in complex with the peptide pVIPR | Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Huan Lan, Jana Sticht, Martin Ballaschk, Peter Schmieder |
19120 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2705 complexed with the nonamer peptide pVIPR (RRKWRRWHL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19121 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2705 complexed with the nonamer peptide TIS (RRLPIFSRL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19123 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2705 complexed with the nonamer peptide pGR (RRRWHRWRL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19122 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2705 complexed with the nonamer peptide pLMP2 (RRRWRRLTV) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19113 | Chemical Shifts: 2 sets |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2709 complexed with the nonamer peptide pVIPR (RRKWRRWHL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19116 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2709 complexed with the nonamer peptide TIS (RRLPIFSRL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19118 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2709 complexed with the nonamer peptide pLMP2 (RRRWRRLTV) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19119 | Chemical Shifts: 1 set |
Chemical shifts of human beta-2 microglobulin bound to HLA-B2709 complexed with the nonamer peptide pGR (RRRWHRWRL) | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |
19099 | Chemical Shifts: 1 set |
1H, 13C and 15N chemical shifts of human beta-2-microglobulin in solution | NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules. | Andreas Ziegler, Anne Diehl, Barbara Uchanska-Ziegler, Christina Schnick, Martin Ballaschk, Monika Beerbaum, Natalja Erdmann, Peter Schmieder |