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- PDB-1jw3: Solution Structure of Methanobacterium Thermoautotrophicum Protei... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jw3 | ||||||
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Title | Solution Structure of Methanobacterium Thermoautotrophicum Protein 1598. Ontario Centre for Structural Proteomics target MTH1598_1_140; Northeast Structural Genomics Target TT6 | ||||||
![]() | Conserved Hypothetical Protein MTH1598 | ||||||
![]() | Structural Genomics / Unknown Function / MTH1598 / hypothetical protein / Protein Structure Initiative / OCSP / NESG / beta-alpha-beta sandwich fold / PSI / Northeast Structural Genomics Consortium | ||||||
Function / homology | ![]() tRNA splicing, via endonucleolytic cleavage and ligation / calcium ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
![]() | Chang, X. / Connelly, G. / Yee, A. / 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 | ![]() | 439.5 KB | Display | ![]() |
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PDB format | ![]() | 363.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 340.8 KB | Display | ![]() |
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Full document | ![]() | 475.8 KB | Display | |
Data in XML | ![]() | 41.8 KB | Display | |
Data in CIF | ![]() | 55.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jcuC ![]() 1jdqC ![]() 1je3C ![]() 1jrmC ![]() 1jw2C ![]() 1ryjC ![]() 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: 16202.257 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Plasmid: PET15B / References: UniProt: O27635 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 2mM MTH1598 U-15N,13C Solvent system: 300 mM NaCl,10 mM Phosphate, 10% D2O, pH 6.5 |
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Sample conditions | Ionic strength: 300 mM NaCl / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-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: distance geometry simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1347 restraints, 1157 are NOE-derived distance constraints, 190 dihedral angle restraints. | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |