+Open data
-Basic information
Entry | Database: PDB / ID: 1vd8 | ||||||
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Title | Solution structure of FMBP-1 tandem repeat 2 | ||||||
Components | fibroin-modulator-binding-protein-1 | ||||||
Keywords | TRANSCRIPTION / TANDEM REPEAT / N-CAP / DNA BINDING | ||||||
Function / homology | : / STPRs (score and three amino acid peptide repeats) / Fibroin-modulator-binding protein-1 Function and homology information | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Authors | Yamaki, T. / Kawaguchi, K. / Aizawa, T. / Takiya, S. / Demura, M. / Nitta, K. | ||||||
Citation | Journal: To be Published Title: Solution structure of FMBP-1 tandem repeat 2 Authors: Yamaki, T. / Kawaguchi, K. / Aizawa, T. / Takiya, S. / Demura, M. / Nitta, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vd8.cif.gz | 115.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vd8.ent.gz | 74.8 KB | Display | PDB format |
PDBx/mmJSON format | 1vd8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1vd8_validation.pdf.gz | 335.8 KB | Display | wwPDB validaton report |
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Full document | 1vd8_full_validation.pdf.gz | 405.7 KB | Display | |
Data in XML | 1vd8_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | 1vd8_validation.cif.gz | 9.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vd/1vd8 ftp://data.pdbj.org/pub/pdb/validation_reports/vd/1vd8 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar 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: 2701.069 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic construct / References: UniProt: Q5FBS0*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 1.5mM peptide; pH 4 (10mM sodium phosphate buffer, 60mM NaCl); 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 60mM / pH: 4 / 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 |
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-Processing
NMR software | Name: CNS / Version: 1.1 / Classification: refinement |
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 138 restraints, 136 are NOE-derived distance constraints and 2 are dihedral angle restraints. |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 15 |