+Open data
-Basic information
Entry | Database: PDB / ID: 1wfo | ||||||
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Title | The eighth FN3 domain of human sidekick-2 | ||||||
Components | sidekick 2 | ||||||
Keywords | CELL ADHESION / sidekick-2 / fn3 / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information SDK interactions / camera-type eye photoreceptor cell differentiation / retina layer formation / homophilic cell adhesion via plasma membrane adhesion molecules / synapse assembly / synapse / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Nagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: TO BE PUBLISHED Title: The eighth FN3 domain of human sidekick-2 Authors: Nagashima, T. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wfo.cif.gz | 748.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wfo.ent.gz | 647.9 KB | Display | PDB format |
PDBx/mmJSON format | 1wfo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/1wfo ftp://data.pdbj.org/pub/pdb/validation_reports/wf/1wfo | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13736.438 Da / Num. of mol.: 1 / Fragment: FN3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: Kazusa cDNA fh00815 / Plasmid: P040223-52 / References: UniProt: Q58EX2 |
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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: 1.00mM 13C/15N-labeled protein; 20mM d-TRIS, 200mM NaCl, 1mM d-DTT, 0.02% NaN3 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 220mM / pH: 7.0 / 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: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |