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Open data
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Basic information
| Entry | Database: PDB / ID: 1id6 | ||||||
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| Title | SOLUTION STRUCTURES OF SYR6 | ||||||
Components | SYR6 | ||||||
Keywords | ANTIVIRAL PROTEIN / SYR6 | ||||||
| Function / homology | : Function and homology information | ||||||
| Method | SOLUTION NMR / 4D simulated annealing | ||||||
Authors | Sato, A. / Kawaguchi, K. / Kimura, K. / Tanimura, R. / Sone, S. | ||||||
Citation | Journal: To be PublishedTitle: A peptide mimetic of IFN, the first proof of a small peptidic agonist for heterodimeric cytokine receptor Authors: Sato, A. / Kawaguchi, K. / Kimura, K. / Tanimura, R. / Sone, S. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1id6.cif.gz | 54.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1id6.ent.gz | 37.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1id6.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/id/1id6 ftp://data.pdbj.org/pub/pdb/validation_reports/id/1id6 | HTTPS FTP |
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-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 1784.942 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: chemically synthesized / References: GenBank: 15076606 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||
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| NMR experiment |
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| NMR details | Text: These structures were determined using standard 2D homonuclear techniques. |
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Sample preparation
| Details | Contents: 2.0mM SYR6; deuterated dimethyl sulfoxide 100% / Solvent system: deuterated dimethyl sulfoxide 100% |
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| Sample conditions | Pressure: ambient / Temperature: 293 K |
-NMR measurement
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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| Radiation wavelength | Relative weight: 1 |
| NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
| NMR software |
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| Refinement | Method: 4D simulated annealing / Software ordinal: 1 Details: The structures are based on 66 NOE-derived distance constraints. | ||||||||||||
| NMR representative | Selection criteria: fewest violations | ||||||||||||
| NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 750 / Conformers submitted total number: 11 |
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