| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 51540 |
2022-08-04 |
: sets
|
Proteolytic processing induces a conformational switch required for antibacterial toxin delivery |
Proteolytic processing induces a conformational switch required for antibacterial toxin delivery
|
Andrzej Joachimiak, Bonnie J Cuthbert, Celia W Goulding, Christopher S Hayes, David A Low, Dihn Q Nahn, Elizabeth C Seacord, Frederick W Dahlquist, Hongjun Zhou, Isaac Poonen-Honig, Jesse S Basra, Karolina Michalska, Kiho Song, Lucy M Stols, Nicholas G Wilson, Nicholas L Bartelli, Ricardo Cortes, Victor J Passanisi, William H Eschenfeldt, Youssef Gabraiel, Zainab Noorsher |
| 27754 |
2019-01-18 |
Chemical Shifts: 1 set
|
The cytoplasm-entry domain of antibacterial CdiA is a dynamic alpha-helical bundle with disulfide-dependent structural features |
The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features
|
Christopher S Hayes, Frederick W Dahlquist, Grant C Gucinski, Hongjun Zhou, Kiho Song, Nicholas L Bartelli, Sheng Sun |
| 27755 |
2019-01-18 |
Chemical Shifts: 1 set
|
The cytoplasm-entry domain of antibacterial CdiA is a dynamic alpha-helical bundle with disulfide-dependent structural features |
The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features
|
Christopher S Hayes, Frederick W Dahlquist, Grant C Gucinski, Hongjun Zhou, Kiho Song, Nicholas L Bartelli, Sheng Sun |
| 27753 |
2019-01-18 |
Chemical Shifts: 1 set
|
The cytoplasm-entry domain of antibacterial CdiA is a dynamic alpha-helical bundle with disulfide-dependent structural features |
The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features
|
Christopher S Hayes, Frederick W Dahlquist, Grant C Gucinski, Hongjun Zhou, Kiho Song, Nicholas L Bartelli, Sheng Sun |
| 26908 |
2017-02-15 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C, 15N chemical shift assignments of portions of Thermotoga maritima flagellar motor proteins FliG (N-terminal domain; FliGN) and FliF (C-terminal domain; FliFC) in complex |
Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor
|
Brian R Crane, David F Blair, Eun A Kim, Frederick W Dahlquist, Michael J Lynch, Ria J Sircar, Robert W Levenson |
| 25247 |
2019-07-11 |
Chemical Shifts: 1 set
|
Chemical Shift 1H, 13C, 15N Assignments of FliG bound to unlabeled FliF C-terminal peptide |
Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor
|
Brian R Crane, David F Blair, Eun A Kim, Frederick W Dahlquist, Michael J Lynch, Ria Sircar, Robert Levenson |
| 18310 |
2012-06-13 |
Chemical Shifts: 1 set
|
Chemical Shift 1H, 13C, 15N Assignments of N-terminal domain of Thermotoga Maritima flagellar motor protein FliG bound to unlabeled FliF C-terminal peptide |
Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG.
|
Frederick W Dahlquist, Hongjun Zhou, Robert Levenson |
| 18309 |
2012-06-13 |
Chemical Shifts: 1 set
|
Chemical Shift 1H, 13C, 15N Assignments of N-terminal domain of Thermotoga Maritima flagellar motor protein FliG |
Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG.
|
Frederick W Dahlquist, Hongjun Zhou, Robert Levenson |
| 17651 |
2011-10-12 |
Chemical Shifts: 1 set
|
Solution Structure of Histidine Phosphotransfer Domain of CheA |
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima.
|
Anh Vu, Damon J Hamel, Frederick W Dahlquist, Hongjun Zhou |
| 17604 |
2011-06-01 |
Chemical Shifts: 1 set
|
Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant |
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.
|
Alaji Bah, Bruno E Correia, David Baker, D Flemming Hansen, Frederick W Dahlquist, Guillaume Bouvignies, Lewis E Kay, Oliver Lange, Pramodh Vallurupalli, Robert M Vernon |
| 17603 |
2011-06-01 |
Chemical Shifts: 1 set
|
Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant |
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.
|
Alaji Bah, Bruno E Correia, David Baker, D Flemming Hansen, Frederick W Dahlquist, Guillaume Bouvignies, Lewis E Kay, Oliver Lange, Pramodh Vallurupalli, Robert M Vernon |
| 17234 |
2011-02-24 |
Chemical Shifts: 1 set
|
NMR structure of the DNA-binding domain of E.coli Lrp |
The Design Involved in PapI and Lrp Regulation of the pap Operon.
|
Armand S Vartanian, Frederick W Dahlquist, Hongjun Zhou, Tetsuya Kawamura |
| 16395 |
2009-09-04 |
Chemical Shifts: 1 set
|
Assignments of M.HhaI bound with hemimethylated DNA |
The recognition Pathway for the DNA Cytosine Methyltransferase M.HhaI
|
Frederick W Dahlquist, Hongjun Zhou, Matthew M Murdy, Norbert O Reich |
| 7132 |
2006-10-30 |
Chemical Shifts: 1 set
|
1H, 13C and 15N Chemical Shift Assignments for the CheA P1 domain from Thermotoga maritima |
Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima.
|
Andrew R Byrd, Damon J Hamel, Frederick W Dahlquist, Hongjun Zhou, Mary R Starich |
| 7133 |
2006-10-30 |
Chemical Shifts: 1 set
|
Backbone 1H and 15N Chemical Shift Assignments for the CheA P4 domain from Thermotoga maritima, in the context of a P3P4 construct |
Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima
|
Andrew R Byrd, Damon J Hamel, Frederick W Dahlquist, Hongjun Zhou, Mary R Starich |
| 6566 |
2005-06-03 |
Chemical Shifts: 1 set
|
Measles virus N protein (amino acids 477-505) |
Structural basis for the attachment of a paramyxoviral polymerase to its template
|
Brian W Matthews, Damon J Hamel, Frederick W Dahlquist, Leslie S Gay, Richard L Kingston |
| 6567 |
2005-06-03 |
Chemical Shifts: 1 set
|
Measles virus N protein (amino acids 477-505) bound to the Measles virus P protein (amino acids 457-507). |
Structural basis for the attachment of a paramyxoviral polymerase to its template
|
Brian W Matthews, Damon J Hamel, Frederick W Dahlquist, Leslie S Gay, Richard L Kingston |
| 6568 |
2005-06-03 |
Chemical Shifts: 1 set
|
Measles virus P protein (amino acids 457-407) |
Structural basis for the attachment of a paramyxoviral polymerase to its template
|
Brian W Matthews, Damon J Hamel, Frederick W Dahlquist, Leslie S Gay, Richard L Kingston |
| 6569 |
2005-06-03 |
Chemical Shifts: 1 set
|
Measles virus P protein (amino acids 457-507) bound to the Measles virus N protein (amino acids 477-505) |
Structural basis for the attachment of a paramyxoviral polymerase to its template
|
Brian W Matthews, Damon J Hamel, Frederick W Dahlquist, Leslie S Gay, Richard L Kingston |
| 4984 |
2002-04-04 |
Chemical Shifts: 1 set
|
The Solution Structure and Interactions of CheW from Thermotoga maritima |
The Solution Structure and Interactions of CheW from Thermotoga maritima
|
Frederick W Dahlquist, Hongjun Zhou, Ian J Griswold, Lawrence P McIntosh, Melvin I Simon, Mikenzie Matison, Ronald V Swanson |
| 4083 |
2001-02-17 |
Chemical Shifts: 1 set
|
Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy |
Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy
|
David F Lowry, Frankln L Moy, Frederick W Dahlquist, James E Krywko, Peter J Domaille, Philip Matsumura |
| 915 |
1995-07-31 |
Chemical Shifts: 1 set
|
Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme |
Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme
|
A Joshua Wand, Alfred G Redfield, David F Lowry, Frederick W Dahlquist, Lawrence P McIntosh |
| 371 |
1995-07-31 |
Chemical Shifts: 1 set
|
Secondary Structure of a Leucine Zipper Determined by Nuclear Magnetic Resonance Spectroscopy |
Secondary Structure of a Leucine Zipper Determined by Nuclear Magnetic Resonance Spectroscopy
|
Erin O'Shea, Frederick W Dahlquist, Lawrence P McIntosh, Peter S Kim, Terrence G Oas |
| 887 |
1999-06-14 |
Chemical Shifts: 1 set
|
pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme |
pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme
|
D Eric Anderson, Frederick W Dahlquist, Wayne J Becktel |
| 888 |
1995-07-31 |
Chemical Shifts: 1 set
|
pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme |
pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme
|
D Eric Anderson, Frederick W Dahlquist, Wayne J Becktel |
