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Yorodumi- PDB-2gi4: Solution Structure of the Low Molecular Weight Protein Tyrosine P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2gi4 | ||||||
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Title | Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni. | ||||||
Components | possible phosphotyrosine protein phosphatase | ||||||
Keywords | HYDROLASE / low molecular weight / protein tyrosine phosphatase / bacterial phosphatase / prokaryotic phosphatase / phosphatase | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Campylobacter jejuni (Campylobacter) | ||||||
Method | SOLUTION NMR / Simulated annealing using torsion angle, Cartesian dynamics | ||||||
Authors | Tolkatchev, D. / Shaykhutdinov, R. / Xu, P. / Ni, F. | ||||||
Citation | Journal: Protein Sci. / Year: 2006 Title: Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni. Authors: Tolkatchev, D. / Shaykhutdinov, R. / Xu, P. / Plamondon, J. / Watson, D.C. / Young, N.M. / Ni, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2gi4.cif.gz | 489.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2gi4.ent.gz | 422.6 KB | Display | PDB format |
PDBx/mmJSON format | 2gi4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gi/2gi4 ftp://data.pdbj.org/pub/pdb/validation_reports/gi/2gi4 | HTTPS FTP |
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-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: 18003.680 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Campylobacter jejuni (Campylobacter) / Strain: 11168 / Gene: CJ1258 / Plasmid: pCWori+ / Production host: Escherichia coli (E. coli) / Strain (production host): AD202, BL21(DE3) References: GenBank: 6968691, UniProt: Q0P8Z8*PLUS, protein-tyrosine-phosphatase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 20 mM sodium phosphate / pH: 5.8 / 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 | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: Simulated annealing using torsion angle, Cartesian dynamics Software ordinal: 1 Details: the structures are based on a total of 1464 restraints, 1152 are NOE-derived distance constraints, 64 dihedral angle restraints, 198 chemical shift-based dihedral angle restraints predicted ...Details: the structures are based on a total of 1464 restraints, 1152 are NOE-derived distance constraints, 64 dihedral angle restraints, 198 chemical shift-based dihedral angle restraints predicted by TALOS,50 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |