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Yorodumi- PDB-1r8t: Solution structures of high affinity miniprotein ligands to Strep... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1r8t | ||||||
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| Title | Solution structures of high affinity miniprotein ligands to Streptavidin | ||||||
Components | MP1 | ||||||
Keywords | UNKNOWN FUNCTION / miniprotein / streptavidin / high-affinity | ||||||
| Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Luo, J. / Mukherjee, M. / Fan, X. / Yang, H. / Liu, D. / Khan, R. / White, M. / Fox, R.O. | ||||||
Citation | Journal: To be PublishedTitle: Structure-based design of high affinity miniprotein ligands Authors: Luo, J. / Mukherjee, M. / Fan, X. / Yang, H. / Liu, D. / Khan, R. / White, M. / Fox, R.O. | ||||||
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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 | 1r8t.cif.gz | 113.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1r8t.ent.gz | 81.6 KB | Display | PDB format |
| PDBx/mmJSON format | 1r8t.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1r8t_validation.pdf.gz | 331.4 KB | Display | wwPDB validaton report |
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| Full document | 1r8t_full_validation.pdf.gz | 495.8 KB | Display | |
| Data in XML | 1r8t_validation.xml.gz | 7.8 KB | Display | |
| Data in CIF | 1r8t_validation.cif.gz | 12.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r8/1r8t ftp://data.pdbj.org/pub/pdb/validation_reports/r8/1r8t | HTTPS FTP |
-Related structure data
| Related structure data | |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 1687.003 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This sequence was identified to be a high affinity streptavidin binding ligand by phage display |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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| NMR details | Text: This structure was determined using standard 2D homonuclear experiments. |
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Sample preparation
| Details | Contents: 1.3 mM MP1, 20mM sodium acetate(d3), pH 5.3, 90% H2O and 10% D2O Solvent system: 90% H2O and 10% D2O |
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| Sample conditions | pH: 5.3 / Pressure: ambient / Temperature: 283 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 UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 750 MHz |
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Processing
| NMR software |
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| Refinement | Method: distance geometry, 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: 30 |
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