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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 | Authors |
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51795 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of Annexin A11-PRD(residues 2-52) |
ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution
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Aman Shihora, Lalit Deshmukh, R Hammond, Rodolfo Ghirlando, Ruben Elias |
51796 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments of human S100A6 |
ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution
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Aman Shihora, Lalit Deshmukh, R Hammond, Rodolfo Ghirlando, Ruben Elias |
51514 | Chemical Shifts: 1 set Coupling Constants: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments, experimental 3JHN-HA scalar couplings, and 15N-relaxation rates of the C-terminal portion of human CHMP4C (residues 121-233) |
Reversible phase separation of ESCRT protein ALIX through tyrosine phosphorylation
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Jin Zhang, Lalit Deshmukh, Qi Su, Rodolfo Ghirlando, Ruben D Elias, Yingqi Zu |
51513 | Chemical Shifts: 1 set Coupling Constants: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments, experimental 3JHN-HA scalar couplings, and 15N-relaxation rates of the C-terminal portion of human CHMP4B (residues 121-224) |
Reversible phase separation of ESCRT protein ALIX through tyrosine phosphorylation
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Jin Zhang, Lalit Deshmukh, Qi Su, Rodolfo Ghirlando, Ruben D Elias, Yingqi Zu |
51048 | Chemical Shifts: 1 set |
Backbone chemical shift assignments for the post-fusion six-helix bundle (6HB) state of SARS-CoV-2 S2 protein |
Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion
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Ad Bax, John M Louis, Rodolfo Ghirlando, Sai Chaitanya C Chiliveri |
30931 | Chemical Shifts: 1 set |
Membrane bound structure of HR1 domain of SARS-CoV-2 spike protein |
Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion
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Ad Bax, John M Louis, Rodolfo Ghirlando, Sai Chaitanya C Chiliveri |
50916 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments of HIV-1 p6. |
Quantitative NMR Study of Insulin-Degrading Enzyme Using Amyloid-beta and HIV-1 p6 Elucidates Its Chaperone Activity
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Bhargavi Ramaraju, Lalit Deshmukh, Rodolfo Ghirlando, Spencer L Nelson, Wenwei Zheng |
50694 | Chemical Shifts: 1 set |
1H, 15N, 13C backbone resonance assignment of the monomer C-terminal domain of Enzyme I from Thermoanaerobacter tengcongensis |
Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity
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Julien Roche, Rodolfo Ghirlando, Trang T Nguyen, Vincenzo Venditti |
50695 | Chemical Shifts: 1 set |
1H, 15N, 13C backbone resonance assignment of the monomer C-terminal domain of Enzyme I from Thermoanaerobacter tengcongensis |
Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity
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Julien Roche, Rodolfo Ghirlando, Trang T Nguyen, Vincenzo Venditti |
28111 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of ALIX-PRD |
Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids
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Charles D Schwieters, Lalit Deshmukh, Rodolfo Ghirlando, Ruben D Elias, Vijay Reddy, Wen Ma |
28079 | Chemical Shifts: 1 set |
teEIC backbone and I/L/V methyl resonance assignment |
Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I
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Charles E Stewart, Davit A Potoyan, Rochelle R Dotas, Rodolfo Ghirlando, Trang T Nguyen, Vincenzo Venditti |
28080 | Chemical Shifts: 1 set |
etEIC backbone and I/L/V methyl resonance assignment |
Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I
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Charles E Stewart, Davit A Potoyan, Rochelle R Dotas, Rodolfo Ghirlando, Trang T Nguyen, Vincenzo Venditti |
50122 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N Chemical Shift Assignments for Full length Exon-1 Huntington protein |
Abrogation of pre-nucleation, transient oligomerization of the Huntingtin exon-1 protein by human profilin-I
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Alberto Ceccon, G Marius Clore, Rodolfo Ghirlando, Vitali Tugarinov |
50008 | Chemical Shifts: 1 set |
ngMinE/I24N |
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
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G Marius M Clore, Kiyoshi Mizuuchi, Mengli Cai, Michiyo Mizuuchi, Min Li, Rodolfo Ghirlando, Yang Shen, Ying Huang |
30663 | Chemical Shifts: 1 set |
Solution NMR Structure Of The delta30-ngMinE Protein From Neisseria gonorrheae |
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
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G Marius M Clore, Kiyoshi Mizuuchi, Mengli Cai, Michiyo Mizuuchi, Min Li, Rodolfo Ghirlando, Yang Shen, Ying Huang |
30661 | Chemical Shifts: 1 set |
Solution NMR Structure Of The Full Length Latent Form MinE Protein From Neisseria gonorrheae |
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
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G Marius M Clore, Kiyoshi Mizuuchi, Mengli Cai, Michiyo Mizuuchi, Min Li, Rodolfo Ghirlando, Yang Shen, Ying Huang |
30662 | Chemical Shifts: 1 set |
Solution NMR Structure Of The Partially Activated MTS Deleted Form MinE Protein (delta10-ngMinE) From Neisseria gonorrheae |
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
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G Marius M Clore, Kiyoshi Mizuuchi, Mengli Cai, Michiyo Mizuuchi, Min Li, Rodolfo Ghirlando, Yang Shen, Ying Huang |
30664 | Chemical Shifts: 1 set |
Solution NMR Structure Of The I24N-delta10-ngMinE Protein From Neisseria gonorrheae |
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy
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G Marius M Clore, Kiyoshi Mizuuchi, Mengli Cai, Michiyo Mizuuchi, Min Li, Rodolfo Ghirlando, Yang Shen, Ying Huang |
26955 | Chemical Shifts: 1 set Residual Dipolar Couplings: 1 set |
Fyn SH3 WT delta57 |
Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR
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David S Libich, G Marius Clore, Rodolfo Ghirlando, Vitali Tugarinov |
26954 | Chemical Shifts: 1 set Residual Dipolar Couplings: 1 set |
Fyn SH3 V39V/N53P/V55L delta56 |
Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR
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David S Libich, G Marius Clore, Rodolfo Ghirlando, Vitali Tugarinov |
25532 | Chemical Shifts: 1 set |
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. |
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
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Lalit Deshmukh, Marius Clore, Rodolfo Ghirlando |
19264 | Chemical Shifts: 1 set |
The structure of the W184AM185A mutant of the HIV-1 capsid protein |
Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution.
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Alexander Grishaev, Charles D Schwieters, G Marius Clore, James L Baber, Lalit Deshmukh, Rodolfo Ghirlando |
19261 | Chemical Shifts: 1 set |
HIV capsid dimer structure |
Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution.
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Alexander Grishaev, Charles D Schwieters, G Marius Clore, James L Baber, Lalit Deshmukh, Rodolfo Ghirlando |
18713 | Chemical Shifts: 1 set |
The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant |
The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the
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Hanqiao Feng, Jingjun Hong, Rodolfo Ghirlando, Yawen Bai, Zheng Zhou |
17625 | Chemical Shifts: 1 set |
Microvirin:mannobiose complex |
Solution Structure of the Monovalent Lectin Microvirin in Complex with Man{alpha}(1-2)Man Provides a Basis for Anti-HIV Activity with Low Toxicity.
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Carole A Bewley, Elena Gustchina, G Marius Clore, Rodolfo Ghirlando, Syed Shahzad-Ul-Hussan |