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 |
---|---|---|---|---|
52155 | Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T1rho Relaxation Values: 1 set Order Parameters: 1 set T2 Relaxation Values: 1 set |
Endo-b-1,4-xylanase (Xylanase A) D11F/R122D double mutant from Bacillus subtilis Lipari-Szabo order parameters and relaxation data | Effects of Xylanase A double mutation on substrate specificity and structural dynamics | Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells |
52154 | Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T1rho Relaxation Values: 1 set Order Parameters: 1 set T2 Relaxation Values: 1 set |
Endo-b-1,4-xylanase (Xylanase A) WT from Bacillus subtilis Lipari-Szabo order parameters and relaxation data | Effects of Xylanase A double mutation on substrate specificity and structural dynamics | Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells |
52153 | Chemical Shifts: 1 set |
Endo-b-1,4-xylanase (Xylanase A) D11F/R122D mutant from Bacillus subtilis | Effects of Xylanase A double mutation on substrate specificity and structural dynamics | Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells |
52152 | Chemical Shifts: 1 set |
Endo-b-1,4-xylanase (Xylanase A) WT peak assignments from Bacillus subtilis | Effects of Xylanase A double mutation on substrate specificity and structural dynamics | Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells |
30995 | Chemical Shifts: 1 set |
Solution NMR structure of Vibrio cholerae ferrous iron transport protein C (FeoC) | The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain | A T Smith, J B Brown, M A Lee |
30944 | Chemical Shifts: 1 set Spectral_peak_list: 3 sets |
The solution structure of remipede double-ICK toxin phi-Xibalbin3-Xt3a | Characterization of remipede double-ICK toxin and its effects on ryanodine receptor subtypes one and two | A Dulhunty, B Launikonis, C Thekkedam, E AB Undheim, J Smith, M Maxwell, M Mobli, X Jia, Y K Chin |
30693 | Chemical Shifts: 1 set |
EROS3 RDC and NOE Derived Ubiquitin Ensemble | Enhancing NMR derived ensembles with kinetics on multiple timescales. | A K Rout, A Mazur, B L de Groot, C A Smith, C Griesinger, D Lee, S Becker |
27845 | Chemical Shifts: 1 set |
Solid-state NMR backbone assignment of HBV core protein at 100 kHz | 100 kHz MAS Proton-Detected NMR Spectroscopy of Hepatitis B Virus Capsids | Alexander Malar, Anja Bockmann, Beat Meier, Lauriane Lecoq, Maarten Schledorn, Michael Nassal, Morgane Callon, Shishan Wang, Susanne Smith-Penzel |
30314 | Chemical Shifts: 1 set |
Solution Structure and Dynamics of an Ultra-Stable Single-Chain Insulin Analog STUDIES OF AN ENGINEERED MONOMER AND IMPLICATIONS FOR RECEPTOR BINDING | Solution structure of an ultra-stable single-chain insulin analog connects protein dynamics to a novel mechanism of receptor binding | Brian J Smith, Faramarz Ismail-Beigi, Kelley Carr, Michael A Weiss, Michael C Lawrence, Michael D Glidden, Nalinda P Wickramasinghe, Nelson B Phillips, Nicholas A Smith, Yanwu Yang |
34153 | Chemical Shifts: 1 set |
M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1 | Structure of a Wbl protein and implications for NO sensing by M. tuberculosis | A M Hounslow, B K Kudhair, D M Hunt, J C Crack, J Green, L J Smith, M D Rolfe, M P Williamson, N E Le Brun, R S Buxton |
26787 | Chemical Shifts: 1 set |
Backbone 1H, 13C, and 15N Chemical Shift Assignments for human RIT1 | Biochemical Classification of Disease-associated Mutants of RAS-like Protein Expressed in Many Tissues (RIT1) | Benjamin G Neel, Christopher B Marshall, Genevieve MC Gasmi-Seabrook, Jiani C Yin, Matthew J Smith, Mitsuhiko Ikura, Mohammad T Mazhab-Jafari, Yang Xu, Zhenhao Fang |
25389 | Chemical Shifts: 1 set Coupling Constants: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Backbone 1HN,15N assignments, 15N relaxation data and 3JHNHA coupling constants for wild-type Hydrogenobacter thermophilus cytochrome c552 | Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant | Christina Redfield, Kaeko Tozawa, Lorna Smith, Stuart Ferguson |
25390 | Chemical Shifts: 1 set Coupling Constants: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Backbone 1HN,15N assignments, 15N relaxation data and 3JHNHA coupling constants for the C10A/C13A variant of Hydrogenobacter thermophilus cytochrome c552 | Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant | Christina Redfield, Kaeko Tozawa, Lorna Smith, Stuart Ferguson |
25114 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site | Benjamin G Neel, Christopher B Marshall, Fuyuhiko Inagaki, Genevieve M C Gasmi-Seabrook, Lewis E Kay, Matthew J Smith, Mitsuhiko Ikura, Mohammad T Mazhab-Jafari, Peter B Stathopoulos |
25116 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site | Benjamin G Neel, Christopher B Marshall, Fuyuhiko Inagaki, Genevieve M C Gasmi-Seabrook, Lewis E Kay, Matthew J Smith, Mitsuhiko Ikura, Mohammad T Mazhab-Jafari, Peter B Stathopoulos |
25115 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site | Benjamin G Neel, Christopher B Marshall, Fuyuhiko Inagaki, Genevieve M C Gasmi-Seabrook, Lewis E Kay, Matthew J Smith, Mitsuhiko Ikura, Mohammad T Mazhab-Jafari, Peter B Stathopoulos |
19979 | Chemical Shifts: 1 set |
Solution structure of B24G insulin | Protective hinge in insulin opens to enable its receptor engagement | Brian J Smith, Charles T Roberts, Colin W Ward, Donald F Steiner, Faramarz Ismail-Beigi, John G Menting, Jonathan Whittaker, Julie M Carroll, Linda J Whittaker, Michael A Weiss, Michael C Lawrence, Nalinda P Wickramasinghe, Natalie Strokes, Nelson B Phillips, Satya P Yadav, Shu Jin Chan, Vijay Pandyarajan, Virander S Chauhan, Wieslawa Milewski, Yanwu Yang, Zhu-li Wan |
19822 | Chemical Shifts: 1 set |
NMR structure of B25-(alpha, beta)-dehydro-phenylalanine insulin | Protective hinge in insulin opens to enable its receptor engagement | Brian J Smith, Charles T Roberts, Colin W Ward, Donald F Steiner, Faramarz Ismail-Beigi, John G Menting, Jonathan Whittaker, Julie M Carroll, Linda J Whittaker, Michael A Weiss, Michael C Lawrence, Nalinda P Wickramasinghe, Natalie Strokes, Nelson B Phillips, Satya P Yadav, ShuJin Chan, Vijay Pandyarajan, Virander S Chauhan, Wieslawa Milewski, Yanwu Yang, Zhu-li Wan |
18484 | Chemical Shifts: 1 set |
Conformational analysis of StrH, the surface-attached exo- -D-N-acetylglucosaminidase from Streptococcus pneumoniae. | Conformational Analysis of StrH, the Surface-Attached exo--d-N-Acetylglucosaminidase from Streptococcus pneumoniae. | Alisdair B Boraston, Benjamin Pluvinage, D Wade Abbott, Elizabeth Ficko-Blean, Holly L Spencer, Jobby Maroor Kunjachen, Julie Grondin, Seth Chitayat, Steven P Smith |
18443 | Chemical Shifts: 1 set |
Solution structure of a thioredoxin from Thermus thermophilus | Solution structure of a thioredoxin from Thermus thermophilus | A Celikgil, A D Bandaranayake, A Gizzi, A Kar, B Evans, B Hillerich, B Matikainen, B Smith, D A Calarese, H Patel, J B Bonanno, J Lafleur, J Love, M E Girvin, M K Chan, M Stead, R Banu, R Chaparro, R D Seidel, R Harris, S C Almo, S Chamala, S Garforth, S Lim |
18415 | Chemical Shifts: 1 set |
Solution structure of human C-type lectin domain family 4 member D | Solution structure of human C-type lectin domain family 4 member D | A Celikgil, A D Bandaranayake, A Gizzi, A Kar, B Evans, B Hillerich, B Matikainen, B Smith, D A Calarese, H Patel, J B Bonanno, J Gaudette, J Lafleur, J Love, M E Girvin, M K Chan, M Stead, R Banu, R Chaparro, R D Seidel, R Harris, S C Almo, S Chamala, S Garforth, S Lim |
18411 | Chemical Shifts: 1 set |
Solution structure of a putative protein disulfide isomerase from Bacteroides thetaiotaomicron | Solution structure of a putative protein disulfide isomerase from Bacteroides thetaiotaomicron | A Celikgil, A D Bandaranayake, A Gizzi, A Kar, B Evans, B Hillerich, B Matikainen, B Smith, D A Calarese, H Patel, J B Bonanno, J Lafleur, J Love, M E Girvin, M K Chan, M Stead, R Banu, R Chaparro, R D Seidel, R Harris, S C Almo, S Chamala, S Garforth, S Lim |
18394 | Chemical Shifts: 1 set |
Solution structure of the uncharacterized thioredoxin-like protein BVU_1432 from Bacteroides vulgatus | Solution structure of the uncharacterized thioredoxin-like protein BVU_1432 from Bacteroides vulgatus | A Celikgil, A D Bandaranayake, A Gizzi, A Kar, B Evans, B Hillerich, B Matikainen, B Smith, D A Calarese, H Patel, J B Bonanno, J Lafleur, J Love, M E Girvin, M K Chan, M Stead, R Banu, R Chaparro, R D Seidel, R Harris, S C Almo, S Chamala, S Garforth, S Lim |
18387 | Chemical Shifts: 1 set |
Solution structure of a thiol:disulfide interchange protein from Bacteroides sp. | Solution structure of a thiol:disulfide interchange protein from Bacteroides sp. | A Celikgil, A D Bandaranayake, A Gizzi, A Kar, B Evans, B Hillerich, B Matikainen, B Smith, D A Calarese, H Patel, J B Bonanno, J Lafleur, J Love, M E Girvin, M K Chan, M Stead, R Banu, R Chaparro, R D Seidel, R Harris, S C Almo, S Chamala, S Garforth, S Lim |
17694 | Chemical Shifts: 1 set |
1H, 15N and 13C backbone and side-chain assignments of a family 32 carbohydrate-binding module (CBM32) from the Clostridium perfringens NagH | 1H, 15N and 13C backbone and side-chain resonance assignments of a family 32 carbohydrate-binding module from the Clostridium perfringens NagH. | Alisdair B Boraston, Elizabeth Ficko-Blean, Julie M Grondin, Seth Chitayat, Steven P Smith |
15983 | Chemical Shifts: 1 set |
NMR SOLUTION STRUCTURE FOR ShK-192: A POTENT KV1.3-SPECIFIC IMMUNOSUPPRESSIVE POLYPEPTIDE | Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes | A Garcia, A Giuffrida, A Orzel, B J Smith, C A Galea, C Beeton, C Dixon, D Nugent, D Plank, G Crossley, I Khaytin, I Peshenko, K G Chandy, K P Monaghan, M W Pennington, R S Norton, R V Moore, S Chauhan, S Rangaraju, T Inoue, V Chi, X Hu, Y LeFievre |
7270 | Chemical Shifts: 1 set |
1H, 13C, 15N sequence-specific backbone and sidechain resonance assignments for a putative protein-protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens | NMR assignment of backbone and side chain resonances for a putative protein-protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens | Alisdair B Boraston, Elizabeth Ficko-Blean, Jarrett J Adams, Katie Gregg, Seth Chitayat, Steven P Smith |
6166 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Solution structure of the second complement control protein (CCP) module of the GABA(B)R1a receptor, Pro-119 cis conformer | Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded. | B O Smith, D C Soares, D Uhrin, J H White, P N Barlow, RA J McIlhinney, R Ginham, S C Blein, S Veltel |
6171 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Solution structure of the second complement control protein (CCP) module of the GABA(B)R1a receptor, Pro-119 trans conformer | Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded | B O Smith, D C Soares, D Uhrin, J H White, P N Barlow, R Ginham, R J McIlhinney, S C Blein, S Veltel |
6078 | Chemical Shifts: 1 set |
IA3, an Aspartic Proteinase Inhibitor for Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution | IA3, an Aspartic Proteinase Inhibitor from Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution. | Arthur S Edison, Ben M Dunn, Kyle Perry, Leif Smith, Lowri H Phylip, Omjoy Ganesh, Stephen J Hagen, Terry B Green, Timothy M Logan |
6033 | Chemical Shifts: 1 set |
NMR characterisation shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native fold | NMR analysis shows that a b-type variant of hydrogenobacter thermophilus cytochrome c552 retains its native structure | Christina Redfield, Lorna J Smith, Rachel Wain |
5077 | Chemical Shifts: 1 set |
1H, 15N, 13C NMR Assignments of M156R Protein from myxoma virus, NESG target OP2 | Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2a | Adelinda A Yee, Aled M Edwards, Cheryl H Arrowsmith, John R Cort, L Furong, M B Goshe, Michael A Kennedy, R D Smith, T E Dever, Theresa A Ramelot |
1461 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1459 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1457 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1455 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1033 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1032 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1031 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1030 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1029 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1028 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1471 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1027 | Chemical Shifts: 1 set |
1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | 1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin | Gerd N La Mar, Irene N Rezzano, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey |
1469 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1467 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1465 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |
1463 | Chemical Shifts: 1 set |
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers | Daniel W Parish, Gerd N La Mar, Jai P Singh, Jon B Hauksson, Kevin M Smith, Ravindra K Pandey, Usha Pande |