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- PDB-1ryj: Solution NMR Structure of Protein Mth1743 from Methanobacterium t... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ryj | |||||||||
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Title | Solution NMR Structure of Protein Mth1743 from Methanobacterium thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH1743_1_70; Northeast Structural Genomics Consortium Target TT526. | |||||||||
![]() | unknown | |||||||||
![]() | structural genomics / unknown function / beta/alpha protein / Protein Structure Initiative / OCSP / NESG / PSI / Northeast Structural Genomics Consortium | |||||||||
Function / homology | Sulfur carrier ThiS/MoaD-like / ThiS family / Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp / Beta-grasp domain / Beta-grasp domain superfamily / Ubiquitin-like (UB roll) / Roll / Alpha Beta / Uncharacterized protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / torsion angle dyanmics simulated annealing restrained molecular dynamic simulations | |||||||||
![]() | Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. ...Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / Liao, J. / Finak, G. / Chen, L. / Wishart, D. / Lee, W. / McIntosh, L.P. / Gehring, K. / Kennedy, M.A. / Edwards, A.M. / Arrowsmith, C.H. / Northeast Structural Genomics Consortium (NESG) | |||||||||
![]() | ![]() Title: AN NMR APPROACH TO STRUCTURAL PROTEOMICS Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / ...Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / Liao, J. / Finak, G. / Chen, L. / Wishart, D. / Lee, W. / McIntosh, L.P. / Gehring, K. / Kennedy, M.A. / Edwards, A.M. / Arrowsmith, C.H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 431.7 KB | Display | ![]() |
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PDB format | ![]() | 362.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 338.1 KB | Display | ![]() |
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Full document | ![]() | 461.4 KB | Display | |
Data in XML | ![]() | 21.8 KB | Display | |
Data in CIF | ![]() | 36.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jcuC ![]() 1jdqC ![]() 1je3C ![]() 1jrmC ![]() 1jw2C ![]() 1jw3C ![]() 1rykC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7765.070 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: archaea / Plasmid: PET15B / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 3D 13C,15N-simultaneous NOESY |
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Sample preparation
Details | Contents: 1mM mth1743, 450 mM NaCl, 25 mM Na2PO4, 1mM Benzamidine, 1xinhibitor cooktail, 0.01% NaN3, pH 6.5 Solvent system: 95% H2O/5% D2O |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: torsion angle dyanmics simulated annealing restrained molecular dynamic simulations Software ordinal: 1 Details: 1496 NOE-derived distance constraints, 103 dihedral angle constraints, 34 hydrogen bonds | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |