+Open data
-Basic information
Entry | Database: PDB / ID: 2l0o | ||||||
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Title | DsbB3 peptide structure in 100% TFE | ||||||
Components | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I | ||||||
Keywords | MEMBRANE PROTEIN / DsbB / organic solvent / folding | ||||||
Function / homology | : Function and homology information | ||||||
Biological species | Escherichia coli BW2952 (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Hwang, S. / Hilty, C. | ||||||
Citation | Journal: Proteins / Year: 2011 Title: Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy. Authors: Hwang, S. / Hilty, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l0o.cif.gz | 242.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l0o.ent.gz | 206.4 KB | Display | PDB format |
PDBx/mmJSON format | 2l0o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l0o_validation.pdf.gz | 342.7 KB | Display | wwPDB validaton report |
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Full document | 2l0o_full_validation.pdf.gz | 435.9 KB | Display | |
Data in XML | 2l0o_validation.xml.gz | 9.3 KB | Display | |
Data in CIF | 2l0o_validation.cif.gz | 14.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/2l0o ftp://data.pdbj.org/pub/pdb/validation_reports/l0/2l0o | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3696.453 Da / Num. of mol.: 1 / Fragment: UNP Residues 70-95 / Source method: obtained synthetically / Details: Synthetic peptide / Source: (synth.) Escherichia coli BW2952 (bacteria) / References: UniProt: C4ZTM6 |
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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: 1 mM [U-100% 2H] TFE, 1mM DsbB protein fragment, trifluoroethanol/water Solvent system: trifluoroethanol/water | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |