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Yorodumi- PDB-2nxu: Atomic structure of translation initiation factor aIF2 beta-subun... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2nxu | ||||||
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Title | Atomic structure of translation initiation factor aIF2 beta-subunit from Archaebacteria sulfolobus solfataricus: high resolution NMR in solution | ||||||
Components | Translation initiation factor 2 beta subunit | ||||||
Keywords | TRANSLATION / translation initiation factor / archaea / AIF2beta | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Sulfolobus solfataricus (archaea) | ||||||
Method | SOLUTION NMR / the structures were obtained by torsion angle dynamic calculation, energy minimization. | ||||||
Authors | Vasile, F. / Pechkova, E. / Stolboushkina, E. / Garber, M. / Nicolini, C. | ||||||
Citation | Journal: Proteins / Year: 2007 Title: Solution structure of the beta-subunit of the translation initiation factor aIF2 from archaebacteria Sulfolobus solfataricus. Authors: Vasile, F. / Pechkova, E. / Nicolini, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nxu.cif.gz | 439 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nxu.ent.gz | 360.1 KB | Display | PDB format |
PDBx/mmJSON format | 2nxu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2nxu_validation.pdf.gz | 364.4 KB | Display | wwPDB validaton report |
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Full document | 2nxu_full_validation.pdf.gz | 446 KB | Display | |
Data in XML | 2nxu_validation.xml.gz | 24 KB | Display | |
Data in CIF | 2nxu_validation.cif.gz | 39.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nx/2nxu ftp://data.pdbj.org/pub/pdb/validation_reports/nx/2nxu | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16828.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Strain: P2 / Gene: eif2b / Plasmid: pET-28b(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q97W59 |
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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 TOCSY spectra were performed with a mixing time of 80 ms. NOESY spectra were acquired with mixing time of 200 and 300 ms. For all spectra watergate was used as scheme for solvent ...Text: The TOCSY spectra were performed with a mixing time of 80 ms. NOESY spectra were acquired with mixing time of 200 and 300 ms. For all spectra watergate was used as scheme for solvent suppression. For the first six residues no signals were observed. |
-Sample preparation
Details | Contents: concentration 10 mg/ml, 20 mM NaCl, 10% D2O in H2O Solvent system: 10% D2O in H2O |
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Sample conditions | Ionic strength: 0.2 M / pH: 8 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: the structures were obtained by torsion angle dynamic calculation, energy minimization. Software ordinal: 1 Details: The structure were obtained using 635 non redundant NOE-derived distance restraints and were minimised with 1000 steps of conjugated gradient and 1000 of steepest discent. For the first six ...Details: The structure were obtained using 635 non redundant NOE-derived distance restraints and were minimised with 1000 steps of conjugated gradient and 1000 of steepest discent. For the first six residues no signals were observed. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 10 |