BMRB

Biological Magnetic Resonance Data Bank


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

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Entry ID Data summary Entry Title Citation Title Authors
51506 Chemical Shifts: 1 set
Solid-state NMR 1H-13C-15N assignment of African cichlid nackednavirus capsid protein Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style Download bibtex for citation iamge Alexander A Malar, Anja Bockmann, Beat H Meier, Daniel Boehringer, Julius Rabl, Lauriane Lecoq, Michael Nassal, Ralf Bartenschlager, Sara Pfister, Simone Mattei, Stefan Seitz, Thomas Wiegand
50380 Chemical Shifts: 1 set
Hepatits C virus NS5A protein AHD1 domain Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly Sensitive 1 H-Detected Solid-State NMR Download bibtex for citation iamge Alexander A Malar, Alons Lends, Anja Bockmann, Beat H Meier, Marco E Weber, Marie-Laure Fogeron, Nils-Alexander Lakomek, Ralf Bartenschlager, Susanne Smith-Penzel, Vlastimil Jirasko
30037 Chemical Shifts: 1 set
NMR Structure of NS5A-D2 (JFH1) peptide (304-323) Cyclophilin A allows the allosteric regulation of a structural motif in the disordered domain 2 of NS5A and thereby fine-tunes HCV RNA replication Download bibtex for citation iamge Francois-Xavier Cantrelle, Guy Lippens, Helene Launay, Isabelle Huvent, Marie Dujardin, Neha S Gandhi, Ralf Bartenschlager, Vanesa Madan, Xavier Hanoulle
26702 Chemical Shifts: 4 sets
Partial assignments of full-length (deltaAH)-NS5A protein from Hepatitis C Virus (Con1) produced in wheat germ cell-free system Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A Download bibtex for citation iamge Anja Bockmann, Aurelie Badillo, Francois Penin, Francois-Xavier X Cantrelle, Frederic Delolme, Guy Lippens, Jennifer Molle, Marie-Laure L Fogeron, Ralf Bartenschlager, Roland Montserret, Stephane Sarrazin, Sylvie Ricard-Blum, Veronique Receveur-Brechot, Volker Lohmann, Xavier Hanoulle
17043 Chemical Shifts: 1 set
TMS2 domain of Dengue virus NS4A protein TMS2 domain of Dengue virus NS4A protein Download bibtex for citation iamge Francois Penin, Ralf Bartenschlager, Roland Montserret
16892 Chemical Shifts: 1 set
NS2 [60-99] Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. Download bibtex for citation iamge Darius Moradpour, Francois Penin, Jerome Gouttenoire, Ji Young Lee, Ralf Bartenschlager, Roland Montserret, Vlastimil Jirasko
16886 Chemical Shifts: 1 set
NS2 [27-59] Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. Download bibtex for citation iamge Darius Moradpour, Francois Penin, Jerome Gouttenoire, Ji Young Lee, Ralf Bartenschlager, Roland Montserret, Vlastimil Jirasko
16798 Chemical Shifts: 1 set
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (JFH-1) Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A. Download bibtex for citation iamge Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle
16799 Chemical Shifts: 1 set
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (JFH-1) in presence of 50%TFE Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A. Download bibtex for citation iamge Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle
16800 Chemical Shifts: 1 set
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) in presence of 50%TFE Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A. Download bibtex for citation iamge Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle
16165 Chemical Shifts: 1 set
1H, 15N and 13C backbone resonance assignments of domain 2 (D2) of the non-structural 5A protein (NS5A) from the JFH1 Hepatitis C virus (HCV) strain. Hepatitis C Virus NS5A protein is a substrate for the Peptidyl-Prolyl cis/trans Isomerase activity of Cyclophilins A and B. Download bibtex for citation iamge Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle
15579 Chemical Shifts: 1 set
NS2(1-27) Structural and functional characterization of non-structural protein 2 for its role in hepatitis C virus assembly Download bibtex for citation iamge Anne Janvier, Christiane Brohm, Eike Steinmann, Francois Penin, Leah Eustachi, Nicole Appel, Ralf Bartenschlager, Roland Montserret, Thomas Pietschmann, Vlastimil Jirasko
5978 Chemical Shifts: 3 sets
Structure and function of the membrane domain of hepatitis C virus nonstructural protein 5A Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A Download bibtex for citation iamge Damien Ficheux, Darius Moradpour, Francois Penin, Hubert E Blum, Nicole Appel, Ralf Bartenschlager, Roland Montserret, Stephanie Ramboarina, Volker Brass