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Yorodumi- PDB-1win: Solution Structure of the Band 7 Domain of the mouse Flotillin 2 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1win | ||||||
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Title | Solution Structure of the Band 7 Domain of the mouse Flotillin 2 Protein | ||||||
Components | Flotillin 2 | ||||||
Keywords | CELL ADHESION / Band 7 Domain / Flotillin 2 / structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information : / protein localization to plasma membrane raft / anterograde dendritic transport / RIPK1-mediated regulated necrosis / regulation of myoblast differentiation / Synaptic adhesion-like molecules / membrane raft assembly / Regulation of necroptotic cell death / acrosomal membrane / uropod ...: / protein localization to plasma membrane raft / anterograde dendritic transport / RIPK1-mediated regulated necrosis / regulation of myoblast differentiation / Synaptic adhesion-like molecules / membrane raft assembly / Regulation of necroptotic cell death / acrosomal membrane / uropod / negative regulation of amyloid precursor protein catabolic process / flotillin complex / cell-cell contact zone / regulation of postsynaptic membrane neurotransmitter receptor levels / endocytic vesicle / positive regulation of establishment of T cell polarity / dendrite cytoplasm / caveola / protein localization to plasma membrane / adherens junction / ionotropic glutamate receptor binding / lamellipodium / positive regulation of NF-kappaB transcription factor activity / cytoplasmic vesicle / basolateral plasma membrane / protease binding / vesicle / protein stabilization / cell adhesion / endosome / membrane raft / negative regulation of gene expression / intracellular membrane-bounded organelle / glutamatergic synapse / synapse / perinuclear region of cytoplasm / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Miyamoto, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of the Band 7 Domain of the mouse Flotillin 2 Protein Authors: Miyamoto, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1win.cif.gz | 847.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1win.ent.gz | 713.2 KB | Display | PDB format |
PDBx/mmJSON format | 1win.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1win_validation.pdf.gz | 342 KB | Display | wwPDB validaton report |
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Full document | 1win_full_validation.pdf.gz | 500 KB | Display | |
Data in XML | 1win_validation.xml.gz | 63.6 KB | Display | |
Data in CIF | 1win_validation.cif.gz | 78.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wi/1win ftp://data.pdbj.org/pub/pdb/validation_reports/wi/1win | HTTPS FTP |
-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: 15475.596 Da / Num. of mol.: 1 / Fragment: Band 7 Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 1200003P16 / Plasmid: P030818-03 / References: UniProt: Q60634 |
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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: 1.02mM Band 7 Domain U-13C,15N; 20mM PiNa(pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / 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, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |