+Open data
-Basic information
Entry | Database: PDB / ID: 1hxv | ||||||
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Title | PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR | ||||||
Components | TRIGGER FACTOR | ||||||
Keywords | CHAPERONE / FKBP fold / PPIase | ||||||
Function / homology | Function and homology information 'de novo' cotranslational protein folding / protein unfolding / chaperone-mediated protein folding / protein folding chaperone / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / ribosome binding / protein transport / cell cycle / cell division / cytoplasm Similarity search - Function | ||||||
Biological species | Mycoplasma genitalium (bacteria) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Vogtherr, M. / Parac, T.N. / Maurer, M. / Pahl, A. / Fiebig, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein. Authors: Vogtherr, M. / Jacobs, D.M. / Parac, T.N. / Maurer, M. / Pahl, A. / Saxena, K. / Ruterjans, H. / Griesinger, C. / Fiebig, K.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hxv.cif.gz | 337.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hxv.ent.gz | 283 KB | Display | PDB format |
PDBx/mmJSON format | 1hxv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/1hxv ftp://data.pdbj.org/pub/pdb/validation_reports/hx/1hxv | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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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: 12456.365 Da / Num. of mol.: 1 / Fragment: PPIASE DOMAIN (RESIDUES 150-250) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycoplasma genitalium (bacteria) / Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / References: UniProt: P47480 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: partially aligned samples: 4 % C12E5/n-hexanol, ratio=0.96 (Rueckert and Otting, JACS 122, 7793-7797 (2000)) |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50 mM sodium phosphate / pH: 6.5 / Pressure: atmospheric atm / Temperature: 298 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-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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NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 160 / Conformers submitted total number: 12 |