BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

Instant search results.

These results are sorted by relevance. You can sort the results by clicking on the table headers.

Entry ID Data summary Entry Title Citation Title Authors
34850 Chemical Shifts: 1 set
Spectral_peak_list: 1 set
Conformations of macrocyclic peptides sampled by exact NOEs: models for cell-permeability. NMR structure of Omphalotin A in methanol / water indoleOut conformation. Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability. Download bibtex for citation iamge A D Gossert, E Matabaro, L Sonderegger, M Kunzler, P Guntert, S H Rudisser
34849 Chemical Shifts: 1 set
Spectral_peak_list: 1 set
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Omphalotin A in methanol / water Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability Download bibtex for citation iamge A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser
34848 Chemical Shifts: 1 set
Spectral_peak_list: 1 set
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Omphalotin A in apolar solvents Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability Download bibtex for citation iamge A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser
34846 Chemical Shifts: 1 set
Spectral_peak_list: 1 set
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Cyclosporin A in apolar solvents Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability Download bibtex for citation iamge A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser
34704 Chemical Shifts: 1 set
Solution structure of the DNA-binding minor pilin FimT from Legionella pneumophila The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation Download bibtex for citation iamge Alvar D Gossert, Francesca L Short, Manuela K Hospenthal, Matthew Stedman, Sebastian Braus, Stefanie Holz
30403 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang
30401 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state) Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang
30400 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang
15032 Chemical Shifts: 1 set
Chemical shift assignments of the type 1 pilus subunit FimF NMR assignment of the E. coli type 1 pilus protein FimF. Download bibtex for citation iamge Alvar D Gossert, Francesco Fiorito, Kurt Wuthrich, Sebastian Hiller
6383 Chemical Shifts: 1 set
NMR solution structure of the recombinant elk and mouse/elk variant prion proteins Prion protein NMR structures of the elk and of mouse/elk hybrids Download bibtex for citation iamge Alvar D Gossert, Dominikus A Lysek, Francesco Fiorito, Kurt Wuthrich, Sophie Bonjour