Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title(s) | Authors |
---|---|---|---|---|
51616 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 pH 2.8 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51609 | Chemical Shifts: 1 set |
Single alpha helix peptide u(P3-7)3 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51608 | Chemical Shifts: 1 set |
Single alpha helix peptide u(P3-7)2 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51595 | Chemical Shifts: 1 set |
Synthetic peptide P5-9 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51594 | Chemical Shifts: 1 set |
Synthetic peptide P3-7 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51593 | Chemical Shifts: 1 set |
Synthetic peptide P2-6 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51591 | Chemical Shifts: 2 sets Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets Residual Dipolar Couplings: 3 sets Spectral Density Values: 1 set |
Single alpha helix peptide (P3-7)2 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51592 | Chemical Shifts: 1 set |
Synthetic peptide P1-5 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51597 | Chemical Shifts: 2 sets |
Single alpha helix peptide (P3-7)3 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51596 | Chemical Shifts: 3 sets |
Switchable single alpha helix peptide E(P3-7)3 | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51577 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3V | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51567 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3A | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51568 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3E | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51569 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3F | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51570 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3H | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51571 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3I | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51572 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3K | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51573 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3M | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51574 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3R | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51575 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3S | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51576 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3T | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51578 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3W | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51579 | Chemical Shifts: 1 set |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant L3Y | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51580 | Chemical Shifts: 2 sets |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant Q1E | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51581 | Chemical Shifts: 2 sets |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant Q4E | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51582 | Chemical Shifts: 2 sets |
Androgen receptor (AR) polyQ derived peptide L4Q16 variant Q5E | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
51583 | Chemical Shifts: 2 sets |
TATA-box binding protein (TBP) derived polyQ peptide (16-mer pQ) | A glutamine-based single alpha-helix scaffold to target globular proteins | Albert Escobedo, Birthe B Kragelund, Borja Mateos, Busra Topal, Carla Garcia-Cabau, Jesus Garcia, Jonathan G Piccirillo, Juan Aranda, Lasse Staby, Macarena Sanchez-Navarro, Mateusz Biesaga, Modesto Orozco, Murray Coles, Oscar Millet, Ramon Crehuet, Tammo Diercks, Xavier Salvatella |
34613 | Chemical Shifts: 1 set |
Solution structure of Boskar4; a de novo designed G-CSF agonist | A topological refactoring design strategy yields highly stable granulopoietic proteins | Andrei N Lupas, Ann-Christin Krahl, Baubak Bajoghli, Birte H Alvarez, Jeremy Haaf, Julia Skokowa, Karl Welte, Kateryna Maksymenko, Katherine W Rogers, Malte Ritter, Masoud Nasri, Mohammad ElGamacy, Murray Coles, Narges Aghaallaei, Patrick Muller, Perihan Mir, Yun Xu |
34489 | Chemical Shifts: 1 set |
Designing a Granulopoietic Protein by Topological Rescaffolding 1: Sohair | Design of novel granulopoietic proteins by topological rescaffolding | Andrei N Lupas, Birte H Alvarez, Julia Skokowa, Karl Welte, Kateryna Maksymenko, Katherine W Rogers, Laura Weidmann, Masoud Nasri, Mohammad ElGamacy, Murray Coles, Patrick Muller, Perihan Mir |
34488 | Chemical Shifts: 1 set |
Designing a Granulopoietic Protein by Topological Rescaffolding 2: Moevan | Design of novel granulopoietic proteins by topological rescaffolding | Andrei N Lupas, Birte H Alvarez, Julia Skokowa, Karl Welte, Kateryna Maksymenko, Katherine W Rogers, Laura Weidmann, Masoud Nasri, Mohammad ElGamacy, Murray Coles, Patrick Muller, Perihan Mir |
26713 | Heteronuclear NOE Values: 6 sets Order Parameters: 3 sets |
Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:09 in complex with the peptide TIS | Flexibility of the DsbA Oxidoreductase from Vibrio cholerae - a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbA | Edward J d'Auvergne, James H Horne, Martin Scanlon J, Murray H Coles, Paul R Gooley, Richard H Prankerd, Tony H Velkov, William N Charman, Yanni H Chen |
26711 | Heteronuclear NOE Values: 6 sets Order Parameters: 3 sets |
Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide TIS |
1: Flexibility of the DsbA Oxidoreductase from Vibrio cholerae - a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbA 2: Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. |
Edward J d'Auvergne, James H Horne, Martin Scanlon J, Murray H Coles, Paul R Gooley, Richard H Prankerd, Tony H Velkov, William N Charman, Yanni H Chen |
26712 | Heteronuclear NOE Values: 6 sets Order Parameters: 3 sets |
Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:09 in complex with the peptide pVIPR | Flexibility of the DsbA Oxidoreductase from Vibrio cholerae - a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbA | Edward J d'Auvergne, James H Horne, Martin Scanlon J, Murray H Coles, Paul R Gooley, Richard H Prankerd, Tony H Velkov, William N Charman, Yanni H Chen |
26710 | Heteronuclear NOE Values: 6 sets Order Parameters: 3 sets |
Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR | Probing the Flexibility of the DsbA Oxidoreductase from Vibrio cholerae - a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbA | Edward J d'Auvergne, James H Horne, Martin Scanlon J, Murray H Coles, Paul R Gooley, Richard H Prankerd, Tony H Velkov, William N Charman, Yanni H Chen |
25277 | Chemical Shifts: 1 set |
Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024 | Distinct mechanisms contribute to immunity in the lantibiotic NAI-107 producer strain Microbispora ATCC PTA-5024 | Andreas Kulik, Dirk Linke, Evi Stegmann, Mulugeta Nega, Murray Coles, Paul Schwartz, Roberta Pozzi, Wolfgang Wohlleben |
25241 | Chemical Shifts: 1 set |
The N-domain of the AAA metalloproteinase Yme1 from Saccharomyces cerevisiae | Structure and Evolution of N-domains in AAA Metalloproteases | Andrei N Lupas, Franka Scharfenberg, Joerg Martin, Justyna Serek-Heuberger, Marcus D Hartmann, Michael Habeck, Murray Coles, Vikram Alva |
25235 | Chemical Shifts: 1 set |
The solution structure of the FtsH periplasmic N-domain | Structure and Evolution of N-domains in AAA Metalloproteases | Andrei N Lupas, Franka Scharfenberg, Joerg Martin, Justyna Serek-Heuberger, Marcus D Hartmann, Michael Habeck, Murray Coles, Vikram Alva |
25002 | Chemical Shifts: 1 set |
Solution structure of the LysM region of the E. coli Intimin periplasmic domain | The intimin periplasmic domain mediates dimerisation and binding to peptidoglycan | Daniel Kuehner, Dirk Linke, Friedrich Goetz, Ingo B Autenrieth, Jack C Leo, Manish Chaubey, Monika Schuetz, Murray Coles, Philipp Oberhettinger |
18978 | Chemical Shifts: 1 set |
Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller | Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric -propeller. | Astrid Ursinus, Horst Kessler, Ilka Varnay, Murray Coles, Sergej Djuranovic, Vincent Truffault |
18720 | Chemical Shifts: 1 set |
The solution structure of the Dm DCP1 EVH1 domain in complex with the XRN1 DBM peptide | A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation. | Andreas Boland, Chung-Te Chang, Elisa Izaurralde, Eric Huntzinger, Gabrielle Haas, Joerg E Braun, Murray Coles, Oliver Weichenrieder, Vincent Truffault |
18044 | Chemical Shifts: 1 set |
Computational design of an eight-stranded (beta/alpha)-barrel from fragments of different folds | Potential of fragment recombination for rational design of proteins | Birte Hocker, Jens Meiler, Murray Coles, Simone Eisenbeis, Sooruban Shanmugarantam, Vincent Truffault, William Proffitt |
17776 | Chemical Shifts: 1 set |
Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant | Mechanism of regulation of receptor histidine kinases. | Andrei N Lupas, Hedda U Ferris, Joachim E Schultz, Jorg Martin, Kornelius Zeth, Michael Hulko, Murray Coles, Nora Hornig, Stanislaw Dunin-Horkawicz |
17775 | Chemical Shifts: 1 set |
Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer | Mechanism of regulation of receptor histidine kinases. | Andrei N Lupas, Hedda U Ferris, Joachim E Schultz, Jorg Martin, Kornelius Zeth, Michael Hulko, Murray Coles, Nora Hornig, Stanislaw Dunin-Horkawicz |
17686 | Chemical Shifts: 1 set |
Solution structure of the RMM-CTD domains of human LINE-1 ORF1p | Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition. | Elena Khazina, Murray Coles, Oliver Weichenrieder, Regina Buttner, Steffen Schmidt, Vincent Truffault |
16249 | Chemical Shifts: 1 set |
The carboxy-terminal non-repetitive domain of a spider dragline silk protein regulates nucleation of silk assembly | A conserved spider silk domain acts as a molecular switch that controls fibre assembly. | Charlotte Vendrely, Franz Hagn, Horst Kessler, John G Hardy, Lukas Eisoldt, Murray Coles, Thomas Scheibel |
15956 | Chemical Shifts: 1 set |
NMR structure analysis of a BMP receptor | The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding | Alexander Kotzsch, Horst Kessler, Joachim Nickel, Jochen Klages, Murray Coles, Thomas Mueller |
6478 | Chemical Shifts: 1 set |
The N-domain of the transcription factor AbrB | AbrB-like Transcription Factors Assume a Swapped Hairpin Fold that Is Evolutionarily Related to Double-Psi beta Barrels | Andrei N Lupas, Joerg Martin, Johannes Soding, Kristin Koretke, Murray Coles, Sergej Djuranovic, Tancred Frickey, Vincent Truffault |
6030 | Chemical Shifts: 1 set |
1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli | Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli | Horst Kessler, Karlheinz Altendorf, Marc Bramkamp, Melina Haupt, Murray Coles, Vincent Truffault |
6029 | Chemical Shifts: 1 set |
1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli | Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli | Horst Kessler, Karlheinz Altendorf, Marc Bramkamp, Melina Haupt, Murray Coles, Vincent Truffault |
5936 | Chemical Shifts: 1 set |
Backbone 1H, 15N, 13C Resonance Assignment of b-ADT | Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT | Gundula Bosch, Horst Kessler, Markus Heller, Michael John, Murray Coles, Wolfgang Baumeister |
5930 | Chemical Shifts: 1 set |
Backbone 1H, 15N, 13C Resonance Assignment of a-ADT | Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT | Gundula Bosch, Horst Kessler, Markus Heller, Michael John, Murray Coles, Wolfgang Baumeister |
4954 | Chemical Shifts: 1 set |
1H, 13C and 15N chemical shifts assignments for the N-terminal domain of riboflavin synthase of E. Coli with riboflavin as a bound ligand | The Solution Strucutre of the N-terminal Domain of Riboflavin Synthase | Adelbert Bacher, Holger Luettgen, Horst Kessler, Kerstin Abelmann, Murray Coles, Sabine Eberhardt, Tammo Diercks, Vincent Truffault |
4376 | Chemical Shifts: 1 set Coupling Constants: 1 set Heteronuclear NOE Values: 1 set |
Chemical shift assignments, 3JHNHA coupling constants, secondary structure and 15N{1H} Heteronuclear NOE values of the N-domain of VAT (VCP like ATPase of Thermoplasma). A group II AAA ATPase. | The Solution Strucutre of VAT-N Reveals a Missing Link in the Evolution of Complex Enzymes from a Simple bbab Element. | Adriane Groeger, Andrei Lupas, Beate Rockel, Horst Kessler, Jens Liermann, Juergen Peters, Kirstin K Koretke, Murray Coles, Tammo Diercks, Wolfgang Baumeister |
4267 | Chemical Shifts: 1 set Coupling Constants: 1 set Heteronuclear NOE Values: 9 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets Order Parameters: 1 set |
Chemical shift assignments, 3JHNHA coupling constants and secondary structure of HNGAL (Human Neutrophil Gelatinase-Associated Lipocalin) in its apo form. | The Solution Strucuture and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin. | Bernd Muehlenweg, Harald Tschesche, Horst Kessler, Murray Coles, Stefan Bartsch, Tammo Diercks, Volker Zoelzer |
4136 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Chemical Shift Assignments, 3JHNHA Coupling Constants and Secondary Structure of E.coli Multidrug Resistance Protein (EmrE) | NMR-Investigations of the Multidrug Transporter EmrE, an Integral Membrane Protein | Adriane Groeger, Christian Schwarz, Hagit Yerushalmi, Horst Kessler, Manfred Schwaiger, Mario Lebendiker, Murray Coles, Shimon Schuldiner |