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Yorodumi- PDB-2jta: NMR structure of immunosuppressory ubiquitin fragment is similar ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jta | ||||||
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Title | NMR structure of immunosuppressory ubiquitin fragment is similar to related ubiquitin region. | ||||||
Components | 10-mer ubiquitin peptide | ||||||
Keywords | SIGNALING PROTEIN / alpha helix / immunosuppression / ubiquitin | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Jaremko, M. / Jaremko, L. / Zhukov, I. / Cebrat, M. | ||||||
Citation | Journal: Biopolymers / Year: 2009 Title: The immunosuppressive activity and solution structures of ubiquitin fragments. Authors: Jaremko, L. / Jaremko, M. / Pasikowski, P. / Cebrat, M. / Stefanowicz, P. / Lisowski, M. / Artym, J. / Zimecki, M. / Zhukov, I. / Szewczuk, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jta.cif.gz | 55.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jta.ent.gz | 37.5 KB | Display | PDB format |
PDBx/mmJSON format | 2jta.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jta_validation.pdf.gz | 334.4 KB | Display | wwPDB validaton report |
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Full document | 2jta_full_validation.pdf.gz | 423.9 KB | Display | |
Data in XML | 2jta_validation.xml.gz | 7.1 KB | Display | |
Data in CIF | 2jta_validation.cif.gz | 10.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/2jta ftp://data.pdbj.org/pub/pdb/validation_reports/jt/2jta | 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/peptide | Mass: 1169.221 Da / Num. of mol.: 1 / Fragment: 10-residue fragment of ubiquitin / Source method: obtained synthetically / Details: Solid-phase peptide synthesis, FMOC strategy |
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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: 3.0 mM peptide, methanol / Solvent system: methanol |
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Sample | Conc.: 3.0 mM / Component: peptide |
Sample conditions | Ionic strength: 0.15 / pH: 5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian UnityPlus / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
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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: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |