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Yorodumi- PDB-1jcu: Solution Structure of MTH1692 Protein from Methanobacterium therm... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jcu | ||||||
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Title | Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum | ||||||
Components | conserved protein MTH1692 | ||||||
Keywords | STRUCTURAL GENOMICS / mixed alpha-beta structure | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Methanothermobacter thermautotrophicus (archaea) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Kozlov, G. / Ekiel, I. / Gehring, K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2002 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jcu.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1jcu.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 1jcu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jcu_validation.pdf.gz | 342.6 KB | Display | wwPDB validaton report |
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Full document | 1jcu_full_validation.pdf.gz | 552.1 KB | Display | |
Data in XML | 1jcu_validation.xml.gz | 86.5 KB | Display | |
Data in CIF | 1jcu_validation.cif.gz | 112.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jc/1jcu ftp://data.pdbj.org/pub/pdb/validation_reports/jc/1jcu | HTTPS FTP |
-Related structure data
Related structure data | 1jdqC 1je3C 1jrmC 1jw2C 1jw3C 1ryjC 1rykC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 22642.176 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea) Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Gold Magic / References: UniProt: O27727 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using standard triple-resonance NMR techniques. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0.3M / pH: 6.0 / Pressure: ambient / Temperature: 320 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: simulated annealing / Software ordinal: 1 Details: The structures are based on 1467 non-redundant NOE-derived distance constraints, 197 dihedral angle restraints, and 86 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 |